data_9GOV
# 
_entry.id   9GOV 
# 
_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   9GOV         pdb_00009gov 10.2210/pdb9gov/pdb 
WWPDB D_1292141567 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-02-05 
2 'Structure model' 1 1 2025-02-12 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GOV 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              andrea.mattevi@unipv.it 
_pdbx_contact_author.name_first         Andrea 
_pdbx_contact_author.name_last          Mattevi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9523-7128 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Alvigini, L.' 1 ?                   
'Mattevi, A.'  2 0000-0002-9523-7128 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Arch.Biochem.Biophys. 
_citation.journal_id_ASTM           ABBIA4 
_citation.journal_id_CSD            0158 
_citation.journal_id_ISSN           1096-0384 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            765 
_citation.language                  ? 
_citation.page_first                110320 
_citation.page_last                 110320 
_citation.title                     
'Kinetic and structural investigation of the 4-allyl syringol oxidase from Streptomyces cavernae.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.abb.2025.110320 
_citation.pdbx_database_id_PubMed   39870290 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Eggerichs, D.'   1 ? 
primary 'Weddeling, H.G.' 2 ? 
primary 'Alvigini, L.'    3 ? 
primary 'Rapsch, T.'      4 ? 
primary 'Weindorf, N.'    5 ? 
primary 'Mattevi, A.'     6 ? 
primary 'Tischler, D.'    7 ? 
# 
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 '4-Allyl syringol oxidase from Streptomyces cavernae' 60996.961 2   ? ? ? ? 
2 non-polymer syn '2,6-dimethoxy-4-(3-oxidanylpropyl)phenol'            212.242   2   ? ? ? ? 
3 non-polymer nat 'FLAVIN-ADENINE DINUCLEOTIDE'                         785.550   2   ? ? ? ? 
4 water       nat water                                                 18.015    576 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MTRTLPPGVSDEDFTSALTAFRDVVGDEFVRTDEAELARFHDPYPVGDADAHLASAVISPRDTEQVQEVVRIANRYGIPL
SVISTGRNNGYGGSAPRLSGAVVVNTGERMNRILEVDEKLGYALLEPGVTYFDLHEYLEAHAPSLMIDCPDLGWGSVVGN
ALDRGAGYTPYGDHFMWQTGMEVVLPQGDVMRTGMGALPGSTTWQLIPYGFGPYPDGMFTQSNLGIVTKMGIALMQKPPA
SMTYQITFENESDLEQIVDIMLPLRINMAPLQNVPVLRNIILDAAVVSQRADWYDGDGPLPPEAIERMKKELGLGYWNFY
GTLYGPPQLIEMNYGIIKDAFGQIPGSRFQTHEERHDRGAHVLQDRHKINNGIPSLSEMKLMDWIPGAGHVGFSPISPPV
GRDAMKQFRMVRSRADEYAKDYAAQFVVGLREMHHIALLLFDTQDATARNETLALTRLLIDEAAAEGYGEYRTHNALMDQ
VMGTYNWGDGALLKFHEAIKDALDPNGIIAPGKSGVWPARYRGKGLAAALKLRVDPAANKARKEAELAAATAEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTRTLPPGVSDEDFTSALTAFRDVVGDEFVRTDEAELARFHDPYPVGDADAHLASAVISPRDTEQVQEVVRIANRYGIPL
SVISTGRNNGYGGSAPRLSGAVVVNTGERMNRILEVDEKLGYALLEPGVTYFDLHEYLEAHAPSLMIDCPDLGWGSVVGN
ALDRGAGYTPYGDHFMWQTGMEVVLPQGDVMRTGMGALPGSTTWQLIPYGFGPYPDGMFTQSNLGIVTKMGIALMQKPPA
SMTYQITFENESDLEQIVDIMLPLRINMAPLQNVPVLRNIILDAAVVSQRADWYDGDGPLPPEAIERMKKELGLGYWNFY
GTLYGPPQLIEMNYGIIKDAFGQIPGSRFQTHEERHDRGAHVLQDRHKINNGIPSLSEMKLMDWIPGAGHVGFSPISPPV
GRDAMKQFRMVRSRADEYAKDYAAQFVVGLREMHHIALLLFDTQDATARNETLALTRLLIDEAAAEGYGEYRTHNALMDQ
VMGTYNWGDGALLKFHEAIKDALDPNGIIAPGKSGVWPARYRGKGLAAALKLRVDPAANKARKEAELAAATAEQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2,6-dimethoxy-4-(3-oxidanylpropyl)phenol' QBF 
3 'FLAVIN-ADENINE DINUCLEOTIDE'              FAD 
4 water                                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   ARG n 
1 4   THR n 
1 5   LEU n 
1 6   PRO n 
1 7   PRO n 
1 8   GLY n 
1 9   VAL n 
1 10  SER n 
1 11  ASP n 
1 12  GLU n 
1 13  ASP n 
1 14  PHE n 
1 15  THR n 
1 16  SER n 
1 17  ALA n 
1 18  LEU n 
1 19  THR n 
1 20  ALA n 
1 21  PHE n 
1 22  ARG n 
1 23  ASP n 
1 24  VAL n 
1 25  VAL n 
1 26  GLY n 
1 27  ASP n 
1 28  GLU n 
1 29  PHE n 
1 30  VAL n 
1 31  ARG n 
1 32  THR n 
1 33  ASP n 
1 34  GLU n 
1 35  ALA n 
1 36  GLU n 
1 37  LEU n 
1 38  ALA n 
1 39  ARG n 
1 40  PHE n 
1 41  HIS n 
1 42  ASP n 
1 43  PRO n 
1 44  TYR n 
1 45  PRO n 
1 46  VAL n 
1 47  GLY n 
1 48  ASP n 
1 49  ALA n 
1 50  ASP n 
1 51  ALA n 
1 52  HIS n 
1 53  LEU n 
1 54  ALA n 
1 55  SER n 
1 56  ALA n 
1 57  VAL n 
1 58  ILE n 
1 59  SER n 
1 60  PRO n 
1 61  ARG n 
1 62  ASP n 
1 63  THR n 
1 64  GLU n 
1 65  GLN n 
1 66  VAL n 
1 67  GLN n 
1 68  GLU n 
1 69  VAL n 
1 70  VAL n 
1 71  ARG n 
1 72  ILE n 
1 73  ALA n 
1 74  ASN n 
1 75  ARG n 
1 76  TYR n 
1 77  GLY n 
1 78  ILE n 
1 79  PRO n 
1 80  LEU n 
1 81  SER n 
1 82  VAL n 
1 83  ILE n 
1 84  SER n 
1 85  THR n 
1 86  GLY n 
1 87  ARG n 
1 88  ASN n 
1 89  ASN n 
1 90  GLY n 
1 91  TYR n 
1 92  GLY n 
1 93  GLY n 
1 94  SER n 
1 95  ALA n 
1 96  PRO n 
1 97  ARG n 
1 98  LEU n 
1 99  SER n 
1 100 GLY n 
1 101 ALA n 
1 102 VAL n 
1 103 VAL n 
1 104 VAL n 
1 105 ASN n 
1 106 THR n 
1 107 GLY n 
1 108 GLU n 
1 109 ARG n 
1 110 MET n 
1 111 ASN n 
1 112 ARG n 
1 113 ILE n 
1 114 LEU n 
1 115 GLU n 
1 116 VAL n 
1 117 ASP n 
1 118 GLU n 
1 119 LYS n 
1 120 LEU n 
1 121 GLY n 
1 122 TYR n 
1 123 ALA n 
1 124 LEU n 
1 125 LEU n 
1 126 GLU n 
1 127 PRO n 
1 128 GLY n 
1 129 VAL n 
1 130 THR n 
1 131 TYR n 
1 132 PHE n 
1 133 ASP n 
1 134 LEU n 
1 135 HIS n 
1 136 GLU n 
1 137 TYR n 
1 138 LEU n 
1 139 GLU n 
1 140 ALA n 
1 141 HIS n 
1 142 ALA n 
1 143 PRO n 
1 144 SER n 
1 145 LEU n 
1 146 MET n 
1 147 ILE n 
1 148 ASP n 
1 149 CYS n 
1 150 PRO n 
1 151 ASP n 
1 152 LEU n 
1 153 GLY n 
1 154 TRP n 
1 155 GLY n 
1 156 SER n 
1 157 VAL n 
1 158 VAL n 
1 159 GLY n 
1 160 ASN n 
1 161 ALA n 
1 162 LEU n 
1 163 ASP n 
1 164 ARG n 
1 165 GLY n 
1 166 ALA n 
1 167 GLY n 
1 168 TYR n 
1 169 THR n 
1 170 PRO n 
1 171 TYR n 
1 172 GLY n 
1 173 ASP n 
1 174 HIS n 
1 175 PHE n 
1 176 MET n 
1 177 TRP n 
1 178 GLN n 
1 179 THR n 
1 180 GLY n 
1 181 MET n 
1 182 GLU n 
1 183 VAL n 
1 184 VAL n 
1 185 LEU n 
1 186 PRO n 
1 187 GLN n 
1 188 GLY n 
1 189 ASP n 
1 190 VAL n 
1 191 MET n 
1 192 ARG n 
1 193 THR n 
1 194 GLY n 
1 195 MET n 
1 196 GLY n 
1 197 ALA n 
1 198 LEU n 
1 199 PRO n 
1 200 GLY n 
1 201 SER n 
1 202 THR n 
1 203 THR n 
1 204 TRP n 
1 205 GLN n 
1 206 LEU n 
1 207 ILE n 
1 208 PRO n 
1 209 TYR n 
1 210 GLY n 
1 211 PHE n 
1 212 GLY n 
1 213 PRO n 
1 214 TYR n 
1 215 PRO n 
1 216 ASP n 
1 217 GLY n 
1 218 MET n 
1 219 PHE n 
1 220 THR n 
1 221 GLN n 
1 222 SER n 
1 223 ASN n 
1 224 LEU n 
1 225 GLY n 
1 226 ILE n 
1 227 VAL n 
1 228 THR n 
1 229 LYS n 
1 230 MET n 
1 231 GLY n 
1 232 ILE n 
1 233 ALA n 
1 234 LEU n 
1 235 MET n 
1 236 GLN n 
1 237 LYS n 
1 238 PRO n 
1 239 PRO n 
1 240 ALA n 
1 241 SER n 
1 242 MET n 
1 243 THR n 
1 244 TYR n 
1 245 GLN n 
1 246 ILE n 
1 247 THR n 
1 248 PHE n 
1 249 GLU n 
1 250 ASN n 
1 251 GLU n 
1 252 SER n 
1 253 ASP n 
1 254 LEU n 
1 255 GLU n 
1 256 GLN n 
1 257 ILE n 
1 258 VAL n 
1 259 ASP n 
1 260 ILE n 
1 261 MET n 
1 262 LEU n 
1 263 PRO n 
1 264 LEU n 
1 265 ARG n 
1 266 ILE n 
1 267 ASN n 
1 268 MET n 
1 269 ALA n 
1 270 PRO n 
1 271 LEU n 
1 272 GLN n 
1 273 ASN n 
1 274 VAL n 
1 275 PRO n 
1 276 VAL n 
1 277 LEU n 
1 278 ARG n 
1 279 ASN n 
1 280 ILE n 
1 281 ILE n 
1 282 LEU n 
1 283 ASP n 
1 284 ALA n 
1 285 ALA n 
1 286 VAL n 
1 287 VAL n 
1 288 SER n 
1 289 GLN n 
1 290 ARG n 
1 291 ALA n 
1 292 ASP n 
1 293 TRP n 
1 294 TYR n 
1 295 ASP n 
1 296 GLY n 
1 297 ASP n 
1 298 GLY n 
1 299 PRO n 
1 300 LEU n 
1 301 PRO n 
1 302 PRO n 
1 303 GLU n 
1 304 ALA n 
1 305 ILE n 
1 306 GLU n 
1 307 ARG n 
1 308 MET n 
1 309 LYS n 
1 310 LYS n 
1 311 GLU n 
1 312 LEU n 
1 313 GLY n 
1 314 LEU n 
1 315 GLY n 
1 316 TYR n 
1 317 TRP n 
1 318 ASN n 
1 319 PHE n 
1 320 TYR n 
1 321 GLY n 
1 322 THR n 
1 323 LEU n 
1 324 TYR n 
1 325 GLY n 
1 326 PRO n 
1 327 PRO n 
1 328 GLN n 
1 329 LEU n 
1 330 ILE n 
1 331 GLU n 
1 332 MET n 
1 333 ASN n 
1 334 TYR n 
1 335 GLY n 
1 336 ILE n 
1 337 ILE n 
1 338 LYS n 
1 339 ASP n 
1 340 ALA n 
1 341 PHE n 
1 342 GLY n 
1 343 GLN n 
1 344 ILE n 
1 345 PRO n 
1 346 GLY n 
1 347 SER n 
1 348 ARG n 
1 349 PHE n 
1 350 GLN n 
1 351 THR n 
1 352 HIS n 
1 353 GLU n 
1 354 GLU n 
1 355 ARG n 
1 356 HIS n 
1 357 ASP n 
1 358 ARG n 
1 359 GLY n 
1 360 ALA n 
1 361 HIS n 
1 362 VAL n 
1 363 LEU n 
1 364 GLN n 
1 365 ASP n 
1 366 ARG n 
1 367 HIS n 
1 368 LYS n 
1 369 ILE n 
1 370 ASN n 
1 371 ASN n 
1 372 GLY n 
1 373 ILE n 
1 374 PRO n 
1 375 SER n 
1 376 LEU n 
1 377 SER n 
1 378 GLU n 
1 379 MET n 
1 380 LYS n 
1 381 LEU n 
1 382 MET n 
1 383 ASP n 
1 384 TRP n 
1 385 ILE n 
1 386 PRO n 
1 387 GLY n 
1 388 ALA n 
1 389 GLY n 
1 390 HIS n 
1 391 VAL n 
1 392 GLY n 
1 393 PHE n 
1 394 SER n 
1 395 PRO n 
1 396 ILE n 
1 397 SER n 
1 398 PRO n 
1 399 PRO n 
1 400 VAL n 
1 401 GLY n 
1 402 ARG n 
1 403 ASP n 
1 404 ALA n 
1 405 MET n 
1 406 LYS n 
1 407 GLN n 
1 408 PHE n 
1 409 ARG n 
1 410 MET n 
1 411 VAL n 
1 412 ARG n 
1 413 SER n 
1 414 ARG n 
1 415 ALA n 
1 416 ASP n 
1 417 GLU n 
1 418 TYR n 
1 419 ALA n 
1 420 LYS n 
1 421 ASP n 
1 422 TYR n 
1 423 ALA n 
1 424 ALA n 
1 425 GLN n 
1 426 PHE n 
1 427 VAL n 
1 428 VAL n 
1 429 GLY n 
1 430 LEU n 
1 431 ARG n 
1 432 GLU n 
1 433 MET n 
1 434 HIS n 
1 435 HIS n 
1 436 ILE n 
1 437 ALA n 
1 438 LEU n 
1 439 LEU n 
1 440 LEU n 
1 441 PHE n 
1 442 ASP n 
1 443 THR n 
1 444 GLN n 
1 445 ASP n 
1 446 ALA n 
1 447 THR n 
1 448 ALA n 
1 449 ARG n 
1 450 ASN n 
1 451 GLU n 
1 452 THR n 
1 453 LEU n 
1 454 ALA n 
1 455 LEU n 
1 456 THR n 
1 457 ARG n 
1 458 LEU n 
1 459 LEU n 
1 460 ILE n 
1 461 ASP n 
1 462 GLU n 
1 463 ALA n 
1 464 ALA n 
1 465 ALA n 
1 466 GLU n 
1 467 GLY n 
1 468 TYR n 
1 469 GLY n 
1 470 GLU n 
1 471 TYR n 
1 472 ARG n 
1 473 THR n 
1 474 HIS n 
1 475 ASN n 
1 476 ALA n 
1 477 LEU n 
1 478 MET n 
1 479 ASP n 
1 480 GLN n 
1 481 VAL n 
1 482 MET n 
1 483 GLY n 
1 484 THR n 
1 485 TYR n 
1 486 ASN n 
1 487 TRP n 
1 488 GLY n 
1 489 ASP n 
1 490 GLY n 
1 491 ALA n 
1 492 LEU n 
1 493 LEU n 
1 494 LYS n 
1 495 PHE n 
1 496 HIS n 
1 497 GLU n 
1 498 ALA n 
1 499 ILE n 
1 500 LYS n 
1 501 ASP n 
1 502 ALA n 
1 503 LEU n 
1 504 ASP n 
1 505 PRO n 
1 506 ASN n 
1 507 GLY n 
1 508 ILE n 
1 509 ILE n 
1 510 ALA n 
1 511 PRO n 
1 512 GLY n 
1 513 LYS n 
1 514 SER n 
1 515 GLY n 
1 516 VAL n 
1 517 TRP n 
1 518 PRO n 
1 519 ALA n 
1 520 ARG n 
1 521 TYR n 
1 522 ARG n 
1 523 GLY n 
1 524 LYS n 
1 525 GLY n 
1 526 LEU n 
1 527 ALA n 
1 528 ALA n 
1 529 ALA n 
1 530 LEU n 
1 531 LYS n 
1 532 LEU n 
1 533 ARG n 
1 534 VAL n 
1 535 ASP n 
1 536 PRO n 
1 537 ALA n 
1 538 ALA n 
1 539 ASN n 
1 540 LYS n 
1 541 ALA n 
1 542 ARG n 
1 543 LYS n 
1 544 GLU n 
1 545 ALA n 
1 546 GLU n 
1 547 LEU n 
1 548 ALA n 
1 549 ALA n 
1 550 ALA n 
1 551 THR n 
1 552 ALA n 
1 553 GLU n 
1 554 GLN 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                   554 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Streptomyces cavernae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2259034 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                    ?                   'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                   ?                   'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                 ?                   'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                            ?                   'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                   ?                   'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE'              ?                   'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                                  ?                   'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                            ?                   'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                    ?                   'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                  ?                   'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                      ?                   'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                 ?                   'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                    ?                   'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                     ?                   'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                 ?                   'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE                              ?                   'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                    ?                   'C5 H9 N O2'        115.130 
QBF non-polymer         . '2,6-dimethoxy-4-(3-oxidanylpropyl)phenol' 'propanol syringol' 'C11 H16 O4'        212.242 
SER 'L-peptide linking' y SERINE                                     ?                   'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                                  ?                   'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                 ?                   'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                   ?                   'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                     ?                   'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   ARG 3   3   3   ARG ARG A . n 
A 1 4   THR 4   4   4   THR THR A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   PRO 7   7   7   PRO PRO A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  PHE 14  14  14  PHE PHE A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  PHE 29  29  29  PHE PHE A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  ASP 48  48  48  ASP GLU A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  HIS 52  52  52  HIS HIS A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  SER 55  55  55  SER SER A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  VAL 66  66  66  VAL VAL A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  GLU 68  68  68  GLU GLU A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  ARG 75  75  75  ARG ARG A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 ALA 101 101 101 ALA ALA A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 MET 110 110 110 MET MET A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 ASP 117 117 117 ASP ASP A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 TYR 122 122 122 TYR TYR A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 TYR 131 131 131 TYR TYR A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 HIS 135 135 135 HIS HIS A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 HIS 141 141 141 HIS HIS A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 MET 146 146 146 MET MET A . n 
A 1 147 ILE 147 147 147 ILE ILE A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 CYS 149 149 149 CYS CYS A . n 
A 1 150 PRO 150 150 150 PRO PRO A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 ASN 160 160 160 ASN ASN A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 TYR 168 168 168 TYR TYR A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 TYR 171 171 171 TYR TYR A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 HIS 174 174 174 HIS HIS A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 MET 176 176 176 MET MET A . n 
A 1 177 TRP 177 177 177 TRP TRP A . n 
A 1 178 GLN 178 178 178 GLN GLN A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 MET 181 181 181 MET MET A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 MET 191 191 191 MET MET A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 MET 195 195 195 MET MET A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 GLY 200 200 200 GLY GLY A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 TRP 204 204 204 TRP TRP A . n 
A 1 205 GLN 205 205 205 GLN GLN A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 PRO 208 208 208 PRO PRO A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 PRO 213 213 213 PRO PRO A . n 
A 1 214 TYR 214 214 214 TYR TYR A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 MET 218 218 218 MET MET A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 THR 220 220 220 THR THR A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 ASN 223 223 223 ASN ASN A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 VAL 227 227 227 VAL VAL A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 LYS 229 229 229 LYS LYS A . n 
A 1 230 MET 230 230 230 MET MET A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 GLN 236 236 236 GLN GLN A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 TYR 244 244 244 TYR TYR A . n 
A 1 245 GLN 245 245 245 GLN GLN A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 THR 247 247 247 THR THR A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 GLU 249 249 249 GLU GLU A . n 
A 1 250 ASN 250 250 250 ASN ASN A . n 
A 1 251 GLU 251 251 251 GLU GLU A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 GLU 255 255 255 GLU GLU A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 ILE 257 257 257 ILE ILE A . n 
A 1 258 VAL 258 258 258 VAL VAL A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 ILE 260 260 260 ILE ILE A . n 
A 1 261 MET 261 261 261 MET MET A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 PRO 263 263 263 PRO PRO A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 ILE 266 266 266 ILE ILE A . n 
A 1 267 ASN 267 267 267 ASN ASN A . n 
A 1 268 MET 268 268 268 MET MET A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 PRO 270 270 270 PRO PRO A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 GLN 272 272 272 GLN GLN A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 VAL 274 274 274 VAL VAL A . n 
A 1 275 PRO 275 275 275 PRO PRO A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 ARG 278 278 278 ARG ARG A . n 
A 1 279 ASN 279 279 279 ASN ASN A . n 
A 1 280 ILE 280 280 280 ILE ILE A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 ASP 283 283 283 ASP ASP A . n 
A 1 284 ALA 284 284 284 ALA ALA A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 SER 288 288 288 SER SER A . n 
A 1 289 GLN 289 289 289 GLN GLN A . n 
A 1 290 ARG 290 290 290 ARG ARG A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 TRP 293 293 293 TRP TRP A . n 
A 1 294 TYR 294 294 294 TYR TYR A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 GLY 298 298 298 GLY GLY A . n 
A 1 299 PRO 299 299 299 PRO PRO A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 PRO 302 302 302 PRO PRO A . n 
A 1 303 GLU 303 303 303 GLU GLU A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 ILE 305 305 305 ILE ILE A . n 
A 1 306 GLU 306 306 306 GLU GLU A . n 
A 1 307 ARG 307 307 307 ARG ARG A . n 
A 1 308 MET 308 308 308 MET MET A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 GLU 311 311 311 GLU GLU A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 LEU 314 314 314 LEU LEU A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 TYR 316 316 316 TYR TYR A . n 
A 1 317 TRP 317 317 317 TRP TRP A . n 
A 1 318 ASN 318 318 318 ASN ASN A . n 
A 1 319 PHE 319 319 319 PHE PHE A . n 
A 1 320 TYR 320 320 320 TYR TYR A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 THR 322 322 322 THR THR A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 TYR 324 324 324 TYR TYR A . n 
A 1 325 GLY 325 325 325 GLY GLY A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 PRO 327 327 327 PRO PRO A . n 
A 1 328 GLN 328 328 328 GLN GLN A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 ILE 330 330 330 ILE ILE A . n 
A 1 331 GLU 331 331 331 GLU GLU A . n 
A 1 332 MET 332 332 332 MET MET A . n 
A 1 333 ASN 333 333 333 ASN ASN A . n 
A 1 334 TYR 334 334 334 TYR TYR A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 ILE 336 336 336 ILE ILE A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 LYS 338 338 338 LYS LYS A . n 
A 1 339 ASP 339 339 339 ASP ASP A . n 
A 1 340 ALA 340 340 340 ALA ALA A . n 
A 1 341 PHE 341 341 341 PHE PHE A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 GLN 343 343 343 GLN GLN A . n 
A 1 344 ILE 344 344 344 ILE ILE A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 GLY 346 346 346 GLY GLY A . n 
A 1 347 SER 347 347 347 SER SER A . n 
A 1 348 ARG 348 348 348 ARG ARG A . n 
A 1 349 PHE 349 349 349 PHE PHE A . n 
A 1 350 GLN 350 350 350 GLN GLN A . n 
A 1 351 THR 351 351 351 THR THR A . n 
A 1 352 HIS 352 352 352 HIS HIS A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 GLU 354 354 354 GLU GLU A . n 
A 1 355 ARG 355 355 355 ARG ARG A . n 
A 1 356 HIS 356 356 356 HIS HIS A . n 
A 1 357 ASP 357 357 357 ASP ASP A . n 
A 1 358 ARG 358 358 358 ARG ARG A . n 
A 1 359 GLY 359 359 359 GLY GLY A . n 
A 1 360 ALA 360 360 360 ALA ALA A . n 
A 1 361 HIS 361 361 361 HIS HIS A . n 
A 1 362 VAL 362 362 362 VAL VAL A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 GLN 364 364 364 GLN GLN A . n 
A 1 365 ASP 365 365 365 ASP ASP A . n 
A 1 366 ARG 366 366 366 ARG ARG A . n 
A 1 367 HIS 367 367 367 HIS HIS A . n 
A 1 368 LYS 368 368 368 LYS LYS A . n 
A 1 369 ILE 369 369 369 ILE ILE A . n 
A 1 370 ASN 370 370 370 ASN ASN A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 GLY 372 372 372 GLY GLY A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 PRO 374 374 374 PRO PRO A . n 
A 1 375 SER 375 375 375 SER SER A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 SER 377 377 377 SER SER A . n 
A 1 378 GLU 378 378 378 GLU GLU A . n 
A 1 379 MET 379 379 379 MET MET A . n 
A 1 380 LYS 380 380 380 LYS LYS A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 MET 382 382 382 MET MET A . n 
A 1 383 ASP 383 383 383 ASP ASP A . n 
A 1 384 TRP 384 384 384 TRP TRP A . n 
A 1 385 ILE 385 385 385 ILE ILE A . n 
A 1 386 PRO 386 386 386 PRO PRO A . n 
A 1 387 GLY 387 387 387 GLY GLY A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 HIS 390 390 390 HIS HIS A . n 
A 1 391 VAL 391 391 391 VAL VAL A . n 
A 1 392 GLY 392 392 392 GLY GLY A . n 
A 1 393 PHE 393 393 393 PHE PHE A . n 
A 1 394 SER 394 394 394 SER SER A . n 
A 1 395 PRO 395 395 395 PRO PRO A . n 
A 1 396 ILE 396 396 396 ILE ILE A . n 
A 1 397 SER 397 397 397 SER SER A . n 
A 1 398 PRO 398 398 398 PRO PRO A . n 
A 1 399 PRO 399 399 399 PRO PRO A . n 
A 1 400 VAL 400 400 400 VAL VAL A . n 
A 1 401 GLY 401 401 401 GLY GLY A . n 
A 1 402 ARG 402 402 402 ARG ARG A . n 
A 1 403 ASP 403 403 403 ASP ASP A . n 
A 1 404 ALA 404 404 404 ALA ALA A . n 
A 1 405 MET 405 405 405 MET MET A . n 
A 1 406 LYS 406 406 406 LYS LYS A . n 
A 1 407 GLN 407 407 407 GLN GLN A . n 
A 1 408 PHE 408 408 408 PHE PHE A . n 
A 1 409 ARG 409 409 409 ARG ARG A . n 
A 1 410 MET 410 410 410 MET MET A . n 
A 1 411 VAL 411 411 411 VAL VAL A . n 
A 1 412 ARG 412 412 412 ARG ARG A . n 
A 1 413 SER 413 413 413 SER SER A . n 
A 1 414 ARG 414 414 414 ARG ARG A . n 
A 1 415 ALA 415 415 415 ALA ALA A . n 
A 1 416 ASP 416 416 416 ASP ASP A . n 
A 1 417 GLU 417 417 417 GLU GLU A . n 
A 1 418 TYR 418 418 418 TYR TYR A . n 
A 1 419 ALA 419 419 419 ALA ALA A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 ASP 421 421 421 ASP ASP A . n 
A 1 422 TYR 422 422 422 TYR TYR A . n 
A 1 423 ALA 423 423 423 ALA ALA A . n 
A 1 424 ALA 424 424 424 ALA ALA A . n 
A 1 425 GLN 425 425 425 GLN GLN A . n 
A 1 426 PHE 426 426 426 PHE PHE A . n 
A 1 427 VAL 427 427 427 VAL VAL A . n 
A 1 428 VAL 428 428 428 VAL VAL A . n 
A 1 429 GLY 429 429 429 GLY GLY A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 ARG 431 431 431 ARG ARG A . n 
A 1 432 GLU 432 432 432 GLU GLU A . n 
A 1 433 MET 433 433 433 MET MET A . n 
A 1 434 HIS 434 434 434 HIS HIS A . n 
A 1 435 HIS 435 435 435 HIS HIS A . n 
A 1 436 ILE 436 436 436 ILE ILE A . n 
A 1 437 ALA 437 437 437 ALA ALA A . n 
A 1 438 LEU 438 438 438 LEU LEU A . n 
A 1 439 LEU 439 439 439 LEU LEU A . n 
A 1 440 LEU 440 440 440 LEU LEU A . n 
A 1 441 PHE 441 441 441 PHE PHE A . n 
A 1 442 ASP 442 442 442 ASP ASP A . n 
A 1 443 THR 443 443 443 THR THR A . n 
A 1 444 GLN 444 444 444 GLN GLN A . n 
A 1 445 ASP 445 445 445 ASP ASP A . n 
A 1 446 ALA 446 446 446 ALA ALA A . n 
A 1 447 THR 447 447 447 THR THR A . n 
A 1 448 ALA 448 448 448 ALA ALA A . n 
A 1 449 ARG 449 449 449 ARG ARG A . n 
A 1 450 ASN 450 450 450 ASN ASN A . n 
A 1 451 GLU 451 451 451 GLU GLU A . n 
A 1 452 THR 452 452 452 THR THR A . n 
A 1 453 LEU 453 453 453 LEU LEU A . n 
A 1 454 ALA 454 454 454 ALA ALA A . n 
A 1 455 LEU 455 455 455 LEU LEU A . n 
A 1 456 THR 456 456 456 THR THR A . n 
A 1 457 ARG 457 457 457 ARG ARG A . n 
A 1 458 LEU 458 458 458 LEU LEU A . n 
A 1 459 LEU 459 459 459 LEU LEU A . n 
A 1 460 ILE 460 460 460 ILE ILE A . n 
A 1 461 ASP 461 461 461 ASP ASP A . n 
A 1 462 GLU 462 462 462 GLU GLU A . n 
A 1 463 ALA 463 463 463 ALA ALA A . n 
A 1 464 ALA 464 464 464 ALA ALA A . n 
A 1 465 ALA 465 465 465 ALA ALA A . n 
A 1 466 GLU 466 466 466 GLU GLU A . n 
A 1 467 GLY 467 467 467 GLY GLY A . n 
A 1 468 TYR 468 468 468 TYR TYR A . n 
A 1 469 GLY 469 469 469 GLY GLY A . n 
A 1 470 GLU 470 470 470 GLU GLU A . n 
A 1 471 TYR 471 471 471 TYR TYR A . n 
A 1 472 ARG 472 472 472 ARG ARG A . n 
A 1 473 THR 473 473 473 THR THR A . n 
A 1 474 HIS 474 474 474 HIS HIS A . n 
A 1 475 ASN 475 475 475 ASN ASN A . n 
A 1 476 ALA 476 476 476 ALA ALA A . n 
A 1 477 LEU 477 477 477 LEU LEU A . n 
A 1 478 MET 478 478 478 MET MET A . n 
A 1 479 ASP 479 479 479 ASP ASP A . n 
A 1 480 GLN 480 480 480 GLN GLN A . n 
A 1 481 VAL 481 481 481 VAL VAL A . n 
A 1 482 MET 482 482 482 MET MET A . n 
A 1 483 GLY 483 483 483 GLY GLY A . n 
A 1 484 THR 484 484 484 THR THR A . n 
A 1 485 TYR 485 485 485 TYR TYR A . n 
A 1 486 ASN 486 486 486 ASN ASN A . n 
A 1 487 TRP 487 487 487 TRP TRP A . n 
A 1 488 GLY 488 488 488 GLY GLY A . n 
A 1 489 ASP 489 489 489 ASP ASP A . n 
A 1 490 GLY 490 490 490 GLY GLY A . n 
A 1 491 ALA 491 491 491 ALA ALA A . n 
A 1 492 LEU 492 492 492 LEU LEU A . n 
A 1 493 LEU 493 493 493 LEU LEU A . n 
A 1 494 LYS 494 494 494 LYS LYS A . n 
A 1 495 PHE 495 495 495 PHE PHE A . n 
A 1 496 HIS 496 496 496 HIS HIS A . n 
A 1 497 GLU 497 497 497 GLU GLU A . n 
A 1 498 ALA 498 498 498 ALA ALA A . n 
A 1 499 ILE 499 499 499 ILE ILE A . n 
A 1 500 LYS 500 500 500 LYS LYS A . n 
A 1 501 ASP 501 501 501 ASP ASP A . n 
A 1 502 ALA 502 502 502 ALA ALA A . n 
A 1 503 LEU 503 503 503 LEU LEU A . n 
A 1 504 ASP 504 504 504 ASP ASP A . n 
A 1 505 PRO 505 505 505 PRO PRO A . n 
A 1 506 ASN 506 506 506 ASN ASN A . n 
A 1 507 GLY 507 507 507 GLY GLY A . n 
A 1 508 ILE 508 508 508 ILE ILE A . n 
A 1 509 ILE 509 509 509 ILE ILE A . n 
A 1 510 ALA 510 510 510 ALA ALA A . n 
A 1 511 PRO 511 511 511 PRO PRO A . n 
A 1 512 GLY 512 512 512 GLY GLY A . n 
A 1 513 LYS 513 513 513 LYS LYS A . n 
A 1 514 SER 514 514 514 SER SER A . n 
A 1 515 GLY 515 515 515 GLY GLY A . n 
A 1 516 VAL 516 516 516 VAL VAL A . n 
A 1 517 TRP 517 517 517 TRP TRP A . n 
A 1 518 PRO 518 518 518 PRO PRO A . n 
A 1 519 ALA 519 519 519 ALA ALA A . n 
A 1 520 ARG 520 520 520 ARG ARG A . n 
A 1 521 TYR 521 521 521 TYR TYR A . n 
A 1 522 ARG 522 522 522 ARG ARG A . n 
A 1 523 GLY 523 523 523 GLY GLY A . n 
A 1 524 LYS 524 524 524 LYS LYS A . n 
A 1 525 GLY 525 525 525 GLY GLY A . n 
A 1 526 LEU 526 526 526 LEU LEU A . n 
A 1 527 ALA 527 527 ?   ?   ?   A . n 
A 1 528 ALA 528 528 ?   ?   ?   A . n 
A 1 529 ALA 529 529 ?   ?   ?   A . n 
A 1 530 LEU 530 530 ?   ?   ?   A . n 
A 1 531 LYS 531 531 ?   ?   ?   A . n 
A 1 532 LEU 532 532 ?   ?   ?   A . n 
A 1 533 ARG 533 533 ?   ?   ?   A . n 
A 1 534 VAL 534 534 ?   ?   ?   A . n 
A 1 535 ASP 535 535 ?   ?   ?   A . n 
A 1 536 PRO 536 536 ?   ?   ?   A . n 
A 1 537 ALA 537 537 ?   ?   ?   A . n 
A 1 538 ALA 538 538 ?   ?   ?   A . n 
A 1 539 ASN 539 539 ?   ?   ?   A . n 
A 1 540 LYS 540 540 ?   ?   ?   A . n 
A 1 541 ALA 541 541 ?   ?   ?   A . n 
A 1 542 ARG 542 542 ?   ?   ?   A . n 
A 1 543 LYS 543 543 ?   ?   ?   A . n 
A 1 544 GLU 544 544 ?   ?   ?   A . n 
A 1 545 ALA 545 545 ?   ?   ?   A . n 
A 1 546 GLU 546 546 ?   ?   ?   A . n 
A 1 547 LEU 547 547 ?   ?   ?   A . n 
A 1 548 ALA 548 548 ?   ?   ?   A . n 
A 1 549 ALA 549 549 ?   ?   ?   A . n 
A 1 550 ALA 550 550 ?   ?   ?   A . n 
A 1 551 THR 551 551 ?   ?   ?   A . n 
A 1 552 ALA 552 552 ?   ?   ?   A . n 
A 1 553 GLU 553 553 ?   ?   ?   A . n 
A 1 554 GLN 554 554 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   ?   ?   ?   B . n 
B 1 3   ARG 3   3   ?   ?   ?   B . n 
B 1 4   THR 4   4   4   THR THR B . n 
B 1 5   LEU 5   5   5   LEU LEU B . n 
B 1 6   PRO 6   6   6   PRO PRO B . n 
B 1 7   PRO 7   7   7   PRO PRO B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ASP 13  13  13  ASP ASP B . n 
B 1 14  PHE 14  14  14  PHE PHE B . n 
B 1 15  THR 15  15  15  THR THR B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  ASP 23  23  23  ASP ASP B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  VAL 25  25  25  VAL VAL B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  GLU 28  28  28  GLU GLU B . n 
B 1 29  PHE 29  29  29  PHE PHE B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  ARG 31  31  31  ARG ARG B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  GLU 34  34  34  GLU GLU B . n 
B 1 35  ALA 35  35  35  ALA ALA B . n 
B 1 36  GLU 36  36  36  GLU GLU B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ARG 39  39  39  ARG ARG B . n 
B 1 40  PHE 40  40  40  PHE PHE B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  ASP 42  42  42  ASP ASP B . n 
B 1 43  PRO 43  43  43  PRO PRO B . n 
B 1 44  TYR 44  44  44  TYR TYR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  ASP 48  48  48  ASP GLU B . n 
B 1 49  ALA 49  49  49  ALA ALA B . n 
B 1 50  ASP 50  50  50  ASP ASP B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  HIS 52  52  52  HIS HIS B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  SER 55  55  55  SER SER B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  ILE 58  58  58  ILE ILE B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  ARG 61  61  61  ARG ARG B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  GLN 65  65  65  GLN GLN B . n 
B 1 66  VAL 66  66  66  VAL VAL B . n 
B 1 67  GLN 67  67  67  GLN GLN B . n 
B 1 68  GLU 68  68  68  GLU GLU B . n 
B 1 69  VAL 69  69  69  VAL VAL B . n 
B 1 70  VAL 70  70  70  VAL VAL B . n 
B 1 71  ARG 71  71  71  ARG ARG B . n 
B 1 72  ILE 72  72  72  ILE ILE B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  ARG 75  75  75  ARG ARG B . n 
B 1 76  TYR 76  76  76  TYR TYR B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  PRO 79  79  79  PRO PRO B . n 
B 1 80  LEU 80  80  80  LEU LEU B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  ILE 83  83  83  ILE ILE B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  THR 85  85  85  THR THR B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  ARG 87  87  87  ARG ARG B . n 
B 1 88  ASN 88  88  88  ASN ASN B . n 
B 1 89  ASN 89  89  89  ASN ASN B . n 
B 1 90  GLY 90  90  90  GLY GLY B . n 
B 1 91  TYR 91  91  91  TYR TYR B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  SER 94  94  94  SER SER B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  ARG 97  97  97  ARG ARG B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 ALA 101 101 101 ALA ALA B . n 
B 1 102 VAL 102 102 102 VAL VAL B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ASN 105 105 105 ASN ASN B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 GLY 107 107 107 GLY GLY B . n 
B 1 108 GLU 108 108 108 GLU GLU B . n 
B 1 109 ARG 109 109 109 ARG ARG B . n 
B 1 110 MET 110 110 110 MET MET B . n 
B 1 111 ASN 111 111 111 ASN ASN B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 LEU 114 114 114 LEU LEU B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 VAL 116 116 116 VAL VAL B . n 
B 1 117 ASP 117 117 117 ASP ASP B . n 
B 1 118 GLU 118 118 118 GLU GLU B . n 
B 1 119 LYS 119 119 119 LYS LYS B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 GLY 121 121 121 GLY GLY B . n 
B 1 122 TYR 122 122 122 TYR TYR B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 LEU 124 124 124 LEU LEU B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 GLY 128 128 128 GLY GLY B . n 
B 1 129 VAL 129 129 129 VAL VAL B . n 
B 1 130 THR 130 130 130 THR THR B . n 
B 1 131 TYR 131 131 131 TYR TYR B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 LEU 134 134 134 LEU LEU B . n 
B 1 135 HIS 135 135 135 HIS HIS B . n 
B 1 136 GLU 136 136 136 GLU GLU B . n 
B 1 137 TYR 137 137 137 TYR TYR B . n 
B 1 138 LEU 138 138 138 LEU LEU B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 HIS 141 141 141 HIS HIS B . n 
B 1 142 ALA 142 142 142 ALA ALA B . n 
B 1 143 PRO 143 143 143 PRO PRO B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 MET 146 146 146 MET MET B . n 
B 1 147 ILE 147 147 147 ILE ILE B . n 
B 1 148 ASP 148 148 148 ASP ASP B . n 
B 1 149 CYS 149 149 149 CYS CYS B . n 
B 1 150 PRO 150 150 150 PRO PRO B . n 
B 1 151 ASP 151 151 151 ASP ASP B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 GLY 153 153 153 GLY GLY B . n 
B 1 154 TRP 154 154 154 TRP TRP B . n 
B 1 155 GLY 155 155 155 GLY GLY B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 VAL 158 158 158 VAL VAL B . n 
B 1 159 GLY 159 159 159 GLY GLY B . n 
B 1 160 ASN 160 160 160 ASN ASN B . n 
B 1 161 ALA 161 161 161 ALA ALA B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 ASP 163 163 163 ASP ASP B . n 
B 1 164 ARG 164 164 164 ARG ARG B . n 
B 1 165 GLY 165 165 165 GLY GLY B . n 
B 1 166 ALA 166 166 166 ALA ALA B . n 
B 1 167 GLY 167 167 167 GLY GLY B . n 
B 1 168 TYR 168 168 168 TYR TYR B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 TYR 171 171 171 TYR TYR B . n 
B 1 172 GLY 172 172 172 GLY GLY B . n 
B 1 173 ASP 173 173 173 ASP ASP B . n 
B 1 174 HIS 174 174 174 HIS HIS B . n 
B 1 175 PHE 175 175 175 PHE PHE B . n 
B 1 176 MET 176 176 176 MET MET B . n 
B 1 177 TRP 177 177 177 TRP TRP B . n 
B 1 178 GLN 178 178 178 GLN GLN B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 GLY 180 180 180 GLY GLY B . n 
B 1 181 MET 181 181 181 MET MET B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 VAL 183 183 183 VAL VAL B . n 
B 1 184 VAL 184 184 184 VAL VAL B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 PRO 186 186 186 PRO PRO B . n 
B 1 187 GLN 187 187 187 GLN GLN B . n 
B 1 188 GLY 188 188 188 GLY GLY B . n 
B 1 189 ASP 189 189 189 ASP ASP B . n 
B 1 190 VAL 190 190 190 VAL VAL B . n 
B 1 191 MET 191 191 191 MET MET B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 GLY 194 194 194 GLY GLY B . n 
B 1 195 MET 195 195 195 MET MET B . n 
B 1 196 GLY 196 196 196 GLY GLY B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 LEU 198 198 198 LEU LEU B . n 
B 1 199 PRO 199 199 199 PRO PRO B . n 
B 1 200 GLY 200 200 200 GLY GLY B . n 
B 1 201 SER 201 201 201 SER SER B . n 
B 1 202 THR 202 202 202 THR THR B . n 
B 1 203 THR 203 203 203 THR THR B . n 
B 1 204 TRP 204 204 204 TRP TRP B . n 
B 1 205 GLN 205 205 205 GLN GLN B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 ILE 207 207 207 ILE ILE B . n 
B 1 208 PRO 208 208 208 PRO PRO B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 GLY 210 210 210 GLY GLY B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 GLY 212 212 212 GLY GLY B . n 
B 1 213 PRO 213 213 213 PRO PRO B . n 
B 1 214 TYR 214 214 214 TYR TYR B . n 
B 1 215 PRO 215 215 215 PRO PRO B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 GLY 217 217 217 GLY GLY B . n 
B 1 218 MET 218 218 218 MET MET B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 THR 220 220 220 THR THR B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 ASN 223 223 223 ASN ASN B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 GLY 225 225 225 GLY GLY B . n 
B 1 226 ILE 226 226 226 ILE ILE B . n 
B 1 227 VAL 227 227 227 VAL VAL B . n 
B 1 228 THR 228 228 228 THR THR B . n 
B 1 229 LYS 229 229 229 LYS LYS B . n 
B 1 230 MET 230 230 230 MET MET B . n 
B 1 231 GLY 231 231 231 GLY GLY B . n 
B 1 232 ILE 232 232 232 ILE ILE B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 LEU 234 234 234 LEU LEU B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 GLN 236 236 236 GLN GLN B . n 
B 1 237 LYS 237 237 237 LYS LYS B . n 
B 1 238 PRO 238 238 238 PRO PRO B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 ALA 240 240 240 ALA ALA B . n 
B 1 241 SER 241 241 241 SER SER B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 TYR 244 244 244 TYR TYR B . n 
B 1 245 GLN 245 245 245 GLN GLN B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 THR 247 247 247 THR THR B . n 
B 1 248 PHE 248 248 248 PHE PHE B . n 
B 1 249 GLU 249 249 249 GLU GLU B . n 
B 1 250 ASN 250 250 250 ASN ASN B . n 
B 1 251 GLU 251 251 251 GLU GLU B . n 
B 1 252 SER 252 252 252 SER SER B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 LEU 254 254 254 LEU LEU B . n 
B 1 255 GLU 255 255 255 GLU GLU B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 ILE 257 257 257 ILE ILE B . n 
B 1 258 VAL 258 258 258 VAL VAL B . n 
B 1 259 ASP 259 259 259 ASP ASP B . n 
B 1 260 ILE 260 260 260 ILE ILE B . n 
B 1 261 MET 261 261 261 MET MET B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 PRO 263 263 263 PRO PRO B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 ARG 265 265 265 ARG ARG B . n 
B 1 266 ILE 266 266 266 ILE ILE B . n 
B 1 267 ASN 267 267 267 ASN ASN B . n 
B 1 268 MET 268 268 268 MET MET B . n 
B 1 269 ALA 269 269 269 ALA ALA B . n 
B 1 270 PRO 270 270 270 PRO PRO B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 GLN 272 272 272 GLN GLN B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 VAL 274 274 274 VAL VAL B . n 
B 1 275 PRO 275 275 275 PRO PRO B . n 
B 1 276 VAL 276 276 276 VAL VAL B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 ARG 278 278 278 ARG ARG B . n 
B 1 279 ASN 279 279 279 ASN ASN B . n 
B 1 280 ILE 280 280 280 ILE ILE B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 ASP 283 283 283 ASP ASP B . n 
B 1 284 ALA 284 284 284 ALA ALA B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 VAL 287 287 287 VAL VAL B . n 
B 1 288 SER 288 288 288 SER SER B . n 
B 1 289 GLN 289 289 289 GLN GLN B . n 
B 1 290 ARG 290 290 290 ARG ARG B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 ASP 292 292 292 ASP ASP B . n 
B 1 293 TRP 293 293 293 TRP TRP B . n 
B 1 294 TYR 294 294 294 TYR TYR B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 ASP 297 297 297 ASP ASP B . n 
B 1 298 GLY 298 298 298 GLY GLY B . n 
B 1 299 PRO 299 299 299 PRO PRO B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 PRO 301 301 301 PRO PRO B . n 
B 1 302 PRO 302 302 302 PRO PRO B . n 
B 1 303 GLU 303 303 303 GLU GLU B . n 
B 1 304 ALA 304 304 304 ALA ALA B . n 
B 1 305 ILE 305 305 305 ILE ILE B . n 
B 1 306 GLU 306 306 306 GLU GLU B . n 
B 1 307 ARG 307 307 307 ARG ARG B . n 
B 1 308 MET 308 308 308 MET MET B . n 
B 1 309 LYS 309 309 309 LYS LYS B . n 
B 1 310 LYS 310 310 310 LYS LYS B . n 
B 1 311 GLU 311 311 311 GLU GLU B . n 
B 1 312 LEU 312 312 312 LEU LEU B . n 
B 1 313 GLY 313 313 313 GLY GLY B . n 
B 1 314 LEU 314 314 314 LEU LEU B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 TYR 316 316 316 TYR TYR B . n 
B 1 317 TRP 317 317 317 TRP TRP B . n 
B 1 318 ASN 318 318 318 ASN ASN B . n 
B 1 319 PHE 319 319 319 PHE PHE B . n 
B 1 320 TYR 320 320 320 TYR TYR B . n 
B 1 321 GLY 321 321 321 GLY GLY B . n 
B 1 322 THR 322 322 322 THR THR B . n 
B 1 323 LEU 323 323 323 LEU LEU B . n 
B 1 324 TYR 324 324 324 TYR TYR B . n 
B 1 325 GLY 325 325 325 GLY GLY B . n 
B 1 326 PRO 326 326 326 PRO PRO B . n 
B 1 327 PRO 327 327 327 PRO PRO B . n 
B 1 328 GLN 328 328 328 GLN GLN B . n 
B 1 329 LEU 329 329 329 LEU LEU B . n 
B 1 330 ILE 330 330 330 ILE ILE B . n 
B 1 331 GLU 331 331 331 GLU GLU B . n 
B 1 332 MET 332 332 332 MET MET B . n 
B 1 333 ASN 333 333 333 ASN ASN B . n 
B 1 334 TYR 334 334 334 TYR TYR B . n 
B 1 335 GLY 335 335 335 GLY GLY B . n 
B 1 336 ILE 336 336 336 ILE ILE B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 LYS 338 338 338 LYS LYS B . n 
B 1 339 ASP 339 339 339 ASP ASP B . n 
B 1 340 ALA 340 340 340 ALA ALA B . n 
B 1 341 PHE 341 341 341 PHE PHE B . n 
B 1 342 GLY 342 342 342 GLY GLY B . n 
B 1 343 GLN 343 343 343 GLN GLN B . n 
B 1 344 ILE 344 344 344 ILE ILE B . n 
B 1 345 PRO 345 345 345 PRO PRO B . n 
B 1 346 GLY 346 346 346 GLY GLY B . n 
B 1 347 SER 347 347 347 SER SER B . n 
B 1 348 ARG 348 348 348 ARG ARG B . n 
B 1 349 PHE 349 349 349 PHE PHE B . n 
B 1 350 GLN 350 350 350 GLN GLN B . n 
B 1 351 THR 351 351 351 THR THR B . n 
B 1 352 HIS 352 352 352 HIS HIS B . n 
B 1 353 GLU 353 353 353 GLU GLU B . n 
B 1 354 GLU 354 354 354 GLU GLU B . n 
B 1 355 ARG 355 355 355 ARG ARG B . n 
B 1 356 HIS 356 356 356 HIS HIS B . n 
B 1 357 ASP 357 357 357 ASP ASP B . n 
B 1 358 ARG 358 358 358 ARG ARG B . n 
B 1 359 GLY 359 359 359 GLY GLY B . n 
B 1 360 ALA 360 360 360 ALA ALA B . n 
B 1 361 HIS 361 361 361 HIS HIS B . n 
B 1 362 VAL 362 362 362 VAL VAL B . n 
B 1 363 LEU 363 363 363 LEU LEU B . n 
B 1 364 GLN 364 364 364 GLN GLN B . n 
B 1 365 ASP 365 365 365 ASP ASP B . n 
B 1 366 ARG 366 366 366 ARG ARG B . n 
B 1 367 HIS 367 367 367 HIS HIS B . n 
B 1 368 LYS 368 368 368 LYS LYS B . n 
B 1 369 ILE 369 369 369 ILE ILE B . n 
B 1 370 ASN 370 370 370 ASN ASN B . n 
B 1 371 ASN 371 371 371 ASN ASN B . n 
B 1 372 GLY 372 372 372 GLY GLY B . n 
B 1 373 ILE 373 373 373 ILE ILE B . n 
B 1 374 PRO 374 374 374 PRO PRO B . n 
B 1 375 SER 375 375 375 SER SER B . n 
B 1 376 LEU 376 376 376 LEU LEU B . n 
B 1 377 SER 377 377 377 SER SER B . n 
B 1 378 GLU 378 378 378 GLU GLU B . n 
B 1 379 MET 379 379 379 MET MET B . n 
B 1 380 LYS 380 380 380 LYS LYS B . n 
B 1 381 LEU 381 381 381 LEU LEU B . n 
B 1 382 MET 382 382 382 MET MET B . n 
B 1 383 ASP 383 383 383 ASP ASP B . n 
B 1 384 TRP 384 384 384 TRP TRP B . n 
B 1 385 ILE 385 385 385 ILE ILE B . n 
B 1 386 PRO 386 386 386 PRO PRO B . n 
B 1 387 GLY 387 387 387 GLY GLY B . n 
B 1 388 ALA 388 388 388 ALA ALA B . n 
B 1 389 GLY 389 389 389 GLY GLY B . n 
B 1 390 HIS 390 390 390 HIS HIS B . n 
B 1 391 VAL 391 391 391 VAL VAL B . n 
B 1 392 GLY 392 392 392 GLY GLY B . n 
B 1 393 PHE 393 393 393 PHE PHE B . n 
B 1 394 SER 394 394 394 SER SER B . n 
B 1 395 PRO 395 395 395 PRO PRO B . n 
B 1 396 ILE 396 396 396 ILE ILE B . n 
B 1 397 SER 397 397 397 SER SER B . n 
B 1 398 PRO 398 398 398 PRO PRO B . n 
B 1 399 PRO 399 399 399 PRO PRO B . n 
B 1 400 VAL 400 400 400 VAL VAL B . n 
B 1 401 GLY 401 401 401 GLY GLY B . n 
B 1 402 ARG 402 402 402 ARG ARG B . n 
B 1 403 ASP 403 403 403 ASP ASP B . n 
B 1 404 ALA 404 404 404 ALA ALA B . n 
B 1 405 MET 405 405 405 MET MET B . n 
B 1 406 LYS 406 406 406 LYS LYS B . n 
B 1 407 GLN 407 407 407 GLN GLN B . n 
B 1 408 PHE 408 408 408 PHE PHE B . n 
B 1 409 ARG 409 409 409 ARG ARG B . n 
B 1 410 MET 410 410 410 MET MET B . n 
B 1 411 VAL 411 411 411 VAL VAL B . n 
B 1 412 ARG 412 412 412 ARG ARG B . n 
B 1 413 SER 413 413 413 SER SER B . n 
B 1 414 ARG 414 414 414 ARG ARG B . n 
B 1 415 ALA 415 415 415 ALA ALA B . n 
B 1 416 ASP 416 416 416 ASP ASP B . n 
B 1 417 GLU 417 417 417 GLU GLU B . n 
B 1 418 TYR 418 418 418 TYR TYR B . n 
B 1 419 ALA 419 419 419 ALA ALA B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 ASP 421 421 421 ASP ASP B . n 
B 1 422 TYR 422 422 422 TYR TYR B . n 
B 1 423 ALA 423 423 423 ALA ALA B . n 
B 1 424 ALA 424 424 424 ALA ALA B . n 
B 1 425 GLN 425 425 425 GLN GLN B . n 
B 1 426 PHE 426 426 426 PHE PHE B . n 
B 1 427 VAL 427 427 427 VAL VAL B . n 
B 1 428 VAL 428 428 428 VAL VAL B . n 
B 1 429 GLY 429 429 429 GLY GLY B . n 
B 1 430 LEU 430 430 430 LEU LEU B . n 
B 1 431 ARG 431 431 431 ARG ARG B . n 
B 1 432 GLU 432 432 432 GLU GLU B . n 
B 1 433 MET 433 433 433 MET MET B . n 
B 1 434 HIS 434 434 434 HIS HIS B . n 
B 1 435 HIS 435 435 435 HIS HIS B . n 
B 1 436 ILE 436 436 436 ILE ILE B . n 
B 1 437 ALA 437 437 437 ALA ALA B . n 
B 1 438 LEU 438 438 438 LEU LEU B . n 
B 1 439 LEU 439 439 439 LEU LEU B . n 
B 1 440 LEU 440 440 440 LEU LEU B . n 
B 1 441 PHE 441 441 441 PHE PHE B . n 
B 1 442 ASP 442 442 442 ASP ASP B . n 
B 1 443 THR 443 443 443 THR THR B . n 
B 1 444 GLN 444 444 444 GLN GLN B . n 
B 1 445 ASP 445 445 445 ASP ASP B . n 
B 1 446 ALA 446 446 446 ALA ALA B . n 
B 1 447 THR 447 447 447 THR THR B . n 
B 1 448 ALA 448 448 448 ALA ALA B . n 
B 1 449 ARG 449 449 449 ARG ARG B . n 
B 1 450 ASN 450 450 450 ASN ASN B . n 
B 1 451 GLU 451 451 451 GLU GLU B . n 
B 1 452 THR 452 452 452 THR THR B . n 
B 1 453 LEU 453 453 453 LEU LEU B . n 
B 1 454 ALA 454 454 454 ALA ALA B . n 
B 1 455 LEU 455 455 455 LEU LEU B . n 
B 1 456 THR 456 456 456 THR THR B . n 
B 1 457 ARG 457 457 457 ARG ARG B . n 
B 1 458 LEU 458 458 458 LEU LEU B . n 
B 1 459 LEU 459 459 459 LEU LEU B . n 
B 1 460 ILE 460 460 460 ILE ILE B . n 
B 1 461 ASP 461 461 461 ASP ASP B . n 
B 1 462 GLU 462 462 462 GLU GLU B . n 
B 1 463 ALA 463 463 463 ALA ALA B . n 
B 1 464 ALA 464 464 464 ALA ALA B . n 
B 1 465 ALA 465 465 465 ALA ALA B . n 
B 1 466 GLU 466 466 466 GLU GLU B . n 
B 1 467 GLY 467 467 467 GLY GLY B . n 
B 1 468 TYR 468 468 468 TYR TYR B . n 
B 1 469 GLY 469 469 469 GLY GLY B . n 
B 1 470 GLU 470 470 470 GLU GLU B . n 
B 1 471 TYR 471 471 471 TYR TYR B . n 
B 1 472 ARG 472 472 472 ARG ARG B . n 
B 1 473 THR 473 473 473 THR THR B . n 
B 1 474 HIS 474 474 474 HIS HIS B . n 
B 1 475 ASN 475 475 475 ASN ASN B . n 
B 1 476 ALA 476 476 476 ALA ALA B . n 
B 1 477 LEU 477 477 477 LEU LEU B . n 
B 1 478 MET 478 478 478 MET MET B . n 
B 1 479 ASP 479 479 479 ASP ASP B . n 
B 1 480 GLN 480 480 480 GLN GLN B . n 
B 1 481 VAL 481 481 481 VAL VAL B . n 
B 1 482 MET 482 482 482 MET MET B . n 
B 1 483 GLY 483 483 483 GLY GLY B . n 
B 1 484 THR 484 484 484 THR THR B . n 
B 1 485 TYR 485 485 485 TYR TYR B . n 
B 1 486 ASN 486 486 486 ASN ASN B . n 
B 1 487 TRP 487 487 487 TRP TRP B . n 
B 1 488 GLY 488 488 488 GLY GLY B . n 
B 1 489 ASP 489 489 489 ASP ASP B . n 
B 1 490 GLY 490 490 490 GLY GLY B . n 
B 1 491 ALA 491 491 491 ALA ALA B . n 
B 1 492 LEU 492 492 492 LEU LEU B . n 
B 1 493 LEU 493 493 493 LEU LEU B . n 
B 1 494 LYS 494 494 494 LYS LYS B . n 
B 1 495 PHE 495 495 495 PHE PHE B . n 
B 1 496 HIS 496 496 496 HIS HIS B . n 
B 1 497 GLU 497 497 497 GLU GLU B . n 
B 1 498 ALA 498 498 498 ALA ALA B . n 
B 1 499 ILE 499 499 499 ILE ILE B . n 
B 1 500 LYS 500 500 500 LYS LYS B . n 
B 1 501 ASP 501 501 501 ASP ASP B . n 
B 1 502 ALA 502 502 502 ALA ALA B . n 
B 1 503 LEU 503 503 503 LEU LEU B . n 
B 1 504 ASP 504 504 504 ASP ASP B . n 
B 1 505 PRO 505 505 505 PRO PRO B . n 
B 1 506 ASN 506 506 506 ASN ASN B . n 
B 1 507 GLY 507 507 507 GLY GLY B . n 
B 1 508 ILE 508 508 508 ILE ILE B . n 
B 1 509 ILE 509 509 509 ILE ILE B . n 
B 1 510 ALA 510 510 510 ALA ALA B . n 
B 1 511 PRO 511 511 511 PRO PRO B . n 
B 1 512 GLY 512 512 512 GLY GLY B . n 
B 1 513 LYS 513 513 513 LYS LYS B . n 
B 1 514 SER 514 514 514 SER SER B . n 
B 1 515 GLY 515 515 515 GLY GLY B . n 
B 1 516 VAL 516 516 516 VAL VAL B . n 
B 1 517 TRP 517 517 517 TRP TRP B . n 
B 1 518 PRO 518 518 518 PRO PRO B . n 
B 1 519 ALA 519 519 519 ALA ALA B . n 
B 1 520 ARG 520 520 520 ARG ARG B . n 
B 1 521 TYR 521 521 521 TYR TYR B . n 
B 1 522 ARG 522 522 522 ARG ARG B . n 
B 1 523 GLY 523 523 523 GLY GLY B . n 
B 1 524 LYS 524 524 524 LYS LYS B . n 
B 1 525 GLY 525 525 525 GLY GLY B . n 
B 1 526 LEU 526 526 526 LEU LEU B . n 
B 1 527 ALA 527 527 ?   ?   ?   B . n 
B 1 528 ALA 528 528 ?   ?   ?   B . n 
B 1 529 ALA 529 529 ?   ?   ?   B . n 
B 1 530 LEU 530 530 ?   ?   ?   B . n 
B 1 531 LYS 531 531 ?   ?   ?   B . n 
B 1 532 LEU 532 532 ?   ?   ?   B . n 
B 1 533 ARG 533 533 ?   ?   ?   B . n 
B 1 534 VAL 534 534 ?   ?   ?   B . n 
B 1 535 ASP 535 535 ?   ?   ?   B . n 
B 1 536 PRO 536 536 ?   ?   ?   B . n 
B 1 537 ALA 537 537 ?   ?   ?   B . n 
B 1 538 ALA 538 538 ?   ?   ?   B . n 
B 1 539 ASN 539 539 ?   ?   ?   B . n 
B 1 540 LYS 540 540 ?   ?   ?   B . n 
B 1 541 ALA 541 541 ?   ?   ?   B . n 
B 1 542 ARG 542 542 ?   ?   ?   B . n 
B 1 543 LYS 543 543 ?   ?   ?   B . n 
B 1 544 GLU 544 544 ?   ?   ?   B . n 
B 1 545 ALA 545 545 ?   ?   ?   B . n 
B 1 546 GLU 546 546 ?   ?   ?   B . n 
B 1 547 LEU 547 547 ?   ?   ?   B . n 
B 1 548 ALA 548 548 ?   ?   ?   B . n 
B 1 549 ALA 549 549 ?   ?   ?   B . n 
B 1 550 ALA 550 550 ?   ?   ?   B . n 
B 1 551 THR 551 551 ?   ?   ?   B . n 
B 1 552 ALA 552 552 ?   ?   ?   B . n 
B 1 553 GLU 553 553 ?   ?   ?   B . n 
B 1 554 GLN 554 554 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        QBF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   QBF 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 QBF 1   701  701 QBF DRG A . 
D 3 FAD 1   702  600 FAD FAD A . 
E 3 FAD 1   601  600 FAD FAD B . 
F 2 QBF 1   602  701 QBF DRG B . 
G 4 HOH 1   801  109 HOH HOH A . 
G 4 HOH 2   802  316 HOH HOH A . 
G 4 HOH 3   803  371 HOH HOH A . 
G 4 HOH 4   804  489 HOH HOH A . 
G 4 HOH 5   805  564 HOH HOH A . 
G 4 HOH 6   806  418 HOH HOH A . 
G 4 HOH 7   807  4   HOH HOH A . 
G 4 HOH 8   808  366 HOH HOH A . 
G 4 HOH 9   809  457 HOH HOH A . 
G 4 HOH 10  810  217 HOH HOH A . 
G 4 HOH 11  811  503 HOH HOH A . 
G 4 HOH 12  812  495 HOH HOH A . 
G 4 HOH 13  813  65  HOH HOH A . 
G 4 HOH 14  814  560 HOH HOH A . 
G 4 HOH 15  815  398 HOH HOH A . 
G 4 HOH 16  816  160 HOH HOH A . 
G 4 HOH 17  817  192 HOH HOH A . 
G 4 HOH 18  818  204 HOH HOH A . 
G 4 HOH 19  819  483 HOH HOH A . 
G 4 HOH 20  820  293 HOH HOH A . 
G 4 HOH 21  821  230 HOH HOH A . 
G 4 HOH 22  822  77  HOH HOH A . 
G 4 HOH 23  823  187 HOH HOH A . 
G 4 HOH 24  824  359 HOH HOH A . 
G 4 HOH 25  825  207 HOH HOH A . 
G 4 HOH 26  826  523 HOH HOH A . 
G 4 HOH 27  827  477 HOH HOH A . 
G 4 HOH 28  828  11  HOH HOH A . 
G 4 HOH 29  829  250 HOH HOH A . 
G 4 HOH 30  830  79  HOH HOH A . 
G 4 HOH 31  831  143 HOH HOH A . 
G 4 HOH 32  832  152 HOH HOH A . 
G 4 HOH 33  833  189 HOH HOH A . 
G 4 HOH 34  834  356 HOH HOH A . 
G 4 HOH 35  835  3   HOH HOH A . 
G 4 HOH 36  836  488 HOH HOH A . 
G 4 HOH 37  837  214 HOH HOH A . 
G 4 HOH 38  838  114 HOH HOH A . 
G 4 HOH 39  839  343 HOH HOH A . 
G 4 HOH 40  840  102 HOH HOH A . 
G 4 HOH 41  841  122 HOH HOH A . 
G 4 HOH 42  842  148 HOH HOH A . 
G 4 HOH 43  843  226 HOH HOH A . 
G 4 HOH 44  844  128 HOH HOH A . 
G 4 HOH 45  845  241 HOH HOH A . 
G 4 HOH 46  846  48  HOH HOH A . 
G 4 HOH 47  847  267 HOH HOH A . 
G 4 HOH 48  848  412 HOH HOH A . 
G 4 HOH 49  849  30  HOH HOH A . 
G 4 HOH 50  850  234 HOH HOH A . 
G 4 HOH 51  851  97  HOH HOH A . 
G 4 HOH 52  852  389 HOH HOH A . 
G 4 HOH 53  853  53  HOH HOH A . 
G 4 HOH 54  854  120 HOH HOH A . 
G 4 HOH 55  855  289 HOH HOH A . 
G 4 HOH 56  856  156 HOH HOH A . 
G 4 HOH 57  857  271 HOH HOH A . 
G 4 HOH 58  858  338 HOH HOH A . 
G 4 HOH 59  859  140 HOH HOH A . 
G 4 HOH 60  860  93  HOH HOH A . 
G 4 HOH 61  861  15  HOH HOH A . 
G 4 HOH 62  862  56  HOH HOH A . 
G 4 HOH 63  863  104 HOH HOH A . 
G 4 HOH 64  864  40  HOH HOH A . 
G 4 HOH 65  865  496 HOH HOH A . 
G 4 HOH 66  866  515 HOH HOH A . 
G 4 HOH 67  867  396 HOH HOH A . 
G 4 HOH 68  868  262 HOH HOH A . 
G 4 HOH 69  869  545 HOH HOH A . 
G 4 HOH 70  870  183 HOH HOH A . 
G 4 HOH 71  871  73  HOH HOH A . 
G 4 HOH 72  872  327 HOH HOH A . 
G 4 HOH 73  873  261 HOH HOH A . 
G 4 HOH 74  874  222 HOH HOH A . 
G 4 HOH 75  875  25  HOH HOH A . 
G 4 HOH 76  876  23  HOH HOH A . 
G 4 HOH 77  877  178 HOH HOH A . 
G 4 HOH 78  878  320 HOH HOH A . 
G 4 HOH 79  879  60  HOH HOH A . 
G 4 HOH 80  880  57  HOH HOH A . 
G 4 HOH 81  881  280 HOH HOH A . 
G 4 HOH 82  882  566 HOH HOH A . 
G 4 HOH 83  883  49  HOH HOH A . 
G 4 HOH 84  884  144 HOH HOH A . 
G 4 HOH 85  885  506 HOH HOH A . 
G 4 HOH 86  886  35  HOH HOH A . 
G 4 HOH 87  887  126 HOH HOH A . 
G 4 HOH 88  888  557 HOH HOH A . 
G 4 HOH 89  889  185 HOH HOH A . 
G 4 HOH 90  890  202 HOH HOH A . 
G 4 HOH 91  891  36  HOH HOH A . 
G 4 HOH 92  892  237 HOH HOH A . 
G 4 HOH 93  893  484 HOH HOH A . 
G 4 HOH 94  894  265 HOH HOH A . 
G 4 HOH 95  895  469 HOH HOH A . 
G 4 HOH 96  896  213 HOH HOH A . 
G 4 HOH 97  897  121 HOH HOH A . 
G 4 HOH 98  898  22  HOH HOH A . 
G 4 HOH 99  899  123 HOH HOH A . 
G 4 HOH 100 900  43  HOH HOH A . 
G 4 HOH 101 901  63  HOH HOH A . 
G 4 HOH 102 902  350 HOH HOH A . 
G 4 HOH 103 903  196 HOH HOH A . 
G 4 HOH 104 904  508 HOH HOH A . 
G 4 HOH 105 905  283 HOH HOH A . 
G 4 HOH 106 906  555 HOH HOH A . 
G 4 HOH 107 907  83  HOH HOH A . 
G 4 HOH 108 908  75  HOH HOH A . 
G 4 HOH 109 909  105 HOH HOH A . 
G 4 HOH 110 910  87  HOH HOH A . 
G 4 HOH 111 911  368 HOH HOH A . 
G 4 HOH 112 912  37  HOH HOH A . 
G 4 HOH 113 913  149 HOH HOH A . 
G 4 HOH 114 914  78  HOH HOH A . 
G 4 HOH 115 915  9   HOH HOH A . 
G 4 HOH 116 916  494 HOH HOH A . 
G 4 HOH 117 917  450 HOH HOH A . 
G 4 HOH 118 918  17  HOH HOH A . 
G 4 HOH 119 919  263 HOH HOH A . 
G 4 HOH 120 920  251 HOH HOH A . 
G 4 HOH 121 921  70  HOH HOH A . 
G 4 HOH 122 922  20  HOH HOH A . 
G 4 HOH 123 923  145 HOH HOH A . 
G 4 HOH 124 924  24  HOH HOH A . 
G 4 HOH 125 925  16  HOH HOH A . 
G 4 HOH 126 926  141 HOH HOH A . 
G 4 HOH 127 927  425 HOH HOH A . 
G 4 HOH 128 928  291 HOH HOH A . 
G 4 HOH 129 929  103 HOH HOH A . 
G 4 HOH 130 930  157 HOH HOH A . 
G 4 HOH 131 931  68  HOH HOH A . 
G 4 HOH 132 932  479 HOH HOH A . 
G 4 HOH 133 933  404 HOH HOH A . 
G 4 HOH 134 934  274 HOH HOH A . 
G 4 HOH 135 935  299 HOH HOH A . 
G 4 HOH 136 936  150 HOH HOH A . 
G 4 HOH 137 937  7   HOH HOH A . 
G 4 HOH 138 938  42  HOH HOH A . 
G 4 HOH 139 939  296 HOH HOH A . 
G 4 HOH 140 940  80  HOH HOH A . 
G 4 HOH 141 941  562 HOH HOH A . 
G 4 HOH 142 942  2   HOH HOH A . 
G 4 HOH 143 943  429 HOH HOH A . 
G 4 HOH 144 944  1   HOH HOH A . 
G 4 HOH 145 945  84  HOH HOH A . 
G 4 HOH 146 946  307 HOH HOH A . 
G 4 HOH 147 947  446 HOH HOH A . 
G 4 HOH 148 948  266 HOH HOH A . 
G 4 HOH 149 949  393 HOH HOH A . 
G 4 HOH 150 950  365 HOH HOH A . 
G 4 HOH 151 951  129 HOH HOH A . 
G 4 HOH 152 952  520 HOH HOH A . 
G 4 HOH 153 953  52  HOH HOH A . 
G 4 HOH 154 954  354 HOH HOH A . 
G 4 HOH 155 955  117 HOH HOH A . 
G 4 HOH 156 956  499 HOH HOH A . 
G 4 HOH 157 957  195 HOH HOH A . 
G 4 HOH 158 958  90  HOH HOH A . 
G 4 HOH 159 959  308 HOH HOH A . 
G 4 HOH 160 960  27  HOH HOH A . 
G 4 HOH 161 961  521 HOH HOH A . 
G 4 HOH 162 962  357 HOH HOH A . 
G 4 HOH 163 963  235 HOH HOH A . 
G 4 HOH 164 964  44  HOH HOH A . 
G 4 HOH 165 965  45  HOH HOH A . 
G 4 HOH 166 966  208 HOH HOH A . 
G 4 HOH 167 967  62  HOH HOH A . 
G 4 HOH 168 968  210 HOH HOH A . 
G 4 HOH 169 969  576 HOH HOH A . 
G 4 HOH 170 970  177 HOH HOH A . 
G 4 HOH 171 971  125 HOH HOH A . 
G 4 HOH 172 972  29  HOH HOH A . 
G 4 HOH 173 973  312 HOH HOH A . 
G 4 HOH 174 974  6   HOH HOH A . 
G 4 HOH 175 975  474 HOH HOH A . 
G 4 HOH 176 976  391 HOH HOH A . 
G 4 HOH 177 977  248 HOH HOH A . 
G 4 HOH 178 978  28  HOH HOH A . 
G 4 HOH 179 979  12  HOH HOH A . 
G 4 HOH 180 980  54  HOH HOH A . 
G 4 HOH 181 981  448 HOH HOH A . 
G 4 HOH 182 982  194 HOH HOH A . 
G 4 HOH 183 983  249 HOH HOH A . 
G 4 HOH 184 984  563 HOH HOH A . 
G 4 HOH 185 985  171 HOH HOH A . 
G 4 HOH 186 986  336 HOH HOH A . 
G 4 HOH 187 987  511 HOH HOH A . 
G 4 HOH 188 988  182 HOH HOH A . 
G 4 HOH 189 989  170 HOH HOH A . 
G 4 HOH 190 990  58  HOH HOH A . 
G 4 HOH 191 991  133 HOH HOH A . 
G 4 HOH 192 992  142 HOH HOH A . 
G 4 HOH 193 993  546 HOH HOH A . 
G 4 HOH 194 994  554 HOH HOH A . 
G 4 HOH 195 995  531 HOH HOH A . 
G 4 HOH 196 996  384 HOH HOH A . 
G 4 HOH 197 997  571 HOH HOH A . 
G 4 HOH 198 998  197 HOH HOH A . 
G 4 HOH 199 999  572 HOH HOH A . 
G 4 HOH 200 1000 88  HOH HOH A . 
G 4 HOH 201 1001 467 HOH HOH A . 
G 4 HOH 202 1002 34  HOH HOH A . 
G 4 HOH 203 1003 421 HOH HOH A . 
G 4 HOH 204 1004 442 HOH HOH A . 
G 4 HOH 205 1005 272 HOH HOH A . 
G 4 HOH 206 1006 548 HOH HOH A . 
G 4 HOH 207 1007 46  HOH HOH A . 
G 4 HOH 208 1008 50  HOH HOH A . 
G 4 HOH 209 1009 167 HOH HOH A . 
G 4 HOH 210 1010 330 HOH HOH A . 
G 4 HOH 211 1011 408 HOH HOH A . 
G 4 HOH 212 1012 518 HOH HOH A . 
G 4 HOH 213 1013 529 HOH HOH A . 
G 4 HOH 214 1014 561 HOH HOH A . 
G 4 HOH 215 1015 85  HOH HOH A . 
G 4 HOH 216 1016 574 HOH HOH A . 
G 4 HOH 217 1017 487 HOH HOH A . 
G 4 HOH 218 1018 246 HOH HOH A . 
G 4 HOH 219 1019 577 HOH HOH A . 
G 4 HOH 220 1020 14  HOH HOH A . 
G 4 HOH 221 1021 329 HOH HOH A . 
G 4 HOH 222 1022 118 HOH HOH A . 
G 4 HOH 223 1023 47  HOH HOH A . 
G 4 HOH 224 1024 232 HOH HOH A . 
G 4 HOH 225 1025 288 HOH HOH A . 
G 4 HOH 226 1026 394 HOH HOH A . 
G 4 HOH 227 1027 203 HOH HOH A . 
G 4 HOH 228 1028 21  HOH HOH A . 
G 4 HOH 229 1029 98  HOH HOH A . 
G 4 HOH 230 1030 136 HOH HOH A . 
G 4 HOH 231 1031 228 HOH HOH A . 
G 4 HOH 232 1032 328 HOH HOH A . 
G 4 HOH 233 1033 191 HOH HOH A . 
G 4 HOH 234 1034 206 HOH HOH A . 
G 4 HOH 235 1035 346 HOH HOH A . 
G 4 HOH 236 1036 397 HOH HOH A . 
G 4 HOH 237 1037 537 HOH HOH A . 
G 4 HOH 238 1038 362 HOH HOH A . 
G 4 HOH 239 1039 146 HOH HOH A . 
G 4 HOH 240 1040 353 HOH HOH A . 
G 4 HOH 241 1041 351 HOH HOH A . 
G 4 HOH 242 1042 8   HOH HOH A . 
G 4 HOH 243 1043 544 HOH HOH A . 
G 4 HOH 244 1044 486 HOH HOH A . 
G 4 HOH 245 1045 242 HOH HOH A . 
G 4 HOH 246 1046 127 HOH HOH A . 
G 4 HOH 247 1047 413 HOH HOH A . 
G 4 HOH 248 1048 480 HOH HOH A . 
G 4 HOH 249 1049 556 HOH HOH A . 
G 4 HOH 250 1050 352 HOH HOH A . 
G 4 HOH 251 1051 387 HOH HOH A . 
G 4 HOH 252 1052 174 HOH HOH A . 
G 4 HOH 253 1053 535 HOH HOH A . 
G 4 HOH 254 1054 244 HOH HOH A . 
G 4 HOH 255 1055 416 HOH HOH A . 
G 4 HOH 256 1056 349 HOH HOH A . 
G 4 HOH 257 1057 158 HOH HOH A . 
G 4 HOH 258 1058 106 HOH HOH A . 
G 4 HOH 259 1059 172 HOH HOH A . 
G 4 HOH 260 1060 505 HOH HOH A . 
G 4 HOH 261 1061 163 HOH HOH A . 
G 4 HOH 262 1062 409 HOH HOH A . 
G 4 HOH 263 1063 240 HOH HOH A . 
G 4 HOH 264 1064 369 HOH HOH A . 
G 4 HOH 265 1065 400 HOH HOH A . 
G 4 HOH 266 1066 459 HOH HOH A . 
G 4 HOH 267 1067 318 HOH HOH A . 
G 4 HOH 268 1068 399 HOH HOH A . 
G 4 HOH 269 1069 107 HOH HOH A . 
G 4 HOH 270 1070 229 HOH HOH A . 
G 4 HOH 271 1071 435 HOH HOH A . 
G 4 HOH 272 1072 297 HOH HOH A . 
G 4 HOH 273 1073 502 HOH HOH A . 
G 4 HOH 274 1074 558 HOH HOH A . 
G 4 HOH 275 1075 225 HOH HOH A . 
G 4 HOH 276 1076 383 HOH HOH A . 
G 4 HOH 277 1077 395 HOH HOH A . 
G 4 HOH 278 1078 500 HOH HOH A . 
G 4 HOH 279 1079 319 HOH HOH A . 
G 4 HOH 280 1080 538 HOH HOH A . 
G 4 HOH 281 1081 573 HOH HOH A . 
G 4 HOH 282 1082 405 HOH HOH A . 
G 4 HOH 283 1083 552 HOH HOH A . 
G 4 HOH 284 1084 444 HOH HOH A . 
G 4 HOH 285 1085 470 HOH HOH A . 
G 4 HOH 286 1086 277 HOH HOH A . 
G 4 HOH 287 1087 360 HOH HOH A . 
G 4 HOH 288 1088 464 HOH HOH A . 
G 4 HOH 289 1089 290 HOH HOH A . 
G 4 HOH 290 1090 430 HOH HOH A . 
G 4 HOH 291 1091 517 HOH HOH A . 
G 4 HOH 292 1092 462 HOH HOH A . 
G 4 HOH 293 1093 218 HOH HOH A . 
G 4 HOH 294 1094 335 HOH HOH A . 
G 4 HOH 295 1095 485 HOH HOH A . 
G 4 HOH 296 1096 427 HOH HOH A . 
G 4 HOH 297 1097 428 HOH HOH A . 
G 4 HOH 298 1098 184 HOH HOH A . 
G 4 HOH 299 1099 238 HOH HOH A . 
G 4 HOH 300 1100 514 HOH HOH A . 
G 4 HOH 301 1101 333 HOH HOH A . 
G 4 HOH 302 1102 282 HOH HOH A . 
G 4 HOH 303 1103 33  HOH HOH A . 
G 4 HOH 304 1104 392 HOH HOH A . 
G 4 HOH 305 1105 575 HOH HOH A . 
G 4 HOH 306 1106 382 HOH HOH A . 
G 4 HOH 307 1107 516 HOH HOH A . 
G 4 HOH 308 1108 549 HOH HOH A . 
G 4 HOH 309 1109 476 HOH HOH A . 
G 4 HOH 310 1110 124 HOH HOH A . 
G 4 HOH 311 1111 256 HOH HOH A . 
G 4 HOH 312 1112 337 HOH HOH A . 
G 4 HOH 313 1113 411 HOH HOH A . 
G 4 HOH 314 1114 456 HOH HOH A . 
G 4 HOH 315 1115 539 HOH HOH A . 
G 4 HOH 316 1116 370 HOH HOH A . 
G 4 HOH 317 1117 134 HOH HOH A . 
G 4 HOH 318 1118 410 HOH HOH A . 
H 4 HOH 1   701  377 HOH HOH B . 
H 4 HOH 2   702  284 HOH HOH B . 
H 4 HOH 3   703  245 HOH HOH B . 
H 4 HOH 4   704  414 HOH HOH B . 
H 4 HOH 5   705  434 HOH HOH B . 
H 4 HOH 6   706  294 HOH HOH B . 
H 4 HOH 7   707  100 HOH HOH B . 
H 4 HOH 8   708  92  HOH HOH B . 
H 4 HOH 9   709  5   HOH HOH B . 
H 4 HOH 10  710  367 HOH HOH B . 
H 4 HOH 11  711  305 HOH HOH B . 
H 4 HOH 12  712  423 HOH HOH B . 
H 4 HOH 13  713  200 HOH HOH B . 
H 4 HOH 14  714  567 HOH HOH B . 
H 4 HOH 15  715  173 HOH HOH B . 
H 4 HOH 16  716  199 HOH HOH B . 
H 4 HOH 17  717  69  HOH HOH B . 
H 4 HOH 18  718  159 HOH HOH B . 
H 4 HOH 19  719  542 HOH HOH B . 
H 4 HOH 20  720  269 HOH HOH B . 
H 4 HOH 21  721  420 HOH HOH B . 
H 4 HOH 22  722  455 HOH HOH B . 
H 4 HOH 23  723  303 HOH HOH B . 
H 4 HOH 24  724  355 HOH HOH B . 
H 4 HOH 25  725  135 HOH HOH B . 
H 4 HOH 26  726  536 HOH HOH B . 
H 4 HOH 27  727  243 HOH HOH B . 
H 4 HOH 28  728  431 HOH HOH B . 
H 4 HOH 29  729  478 HOH HOH B . 
H 4 HOH 30  730  55  HOH HOH B . 
H 4 HOH 31  731  51  HOH HOH B . 
H 4 HOH 32  732  345 HOH HOH B . 
H 4 HOH 33  733  273 HOH HOH B . 
H 4 HOH 34  734  322 HOH HOH B . 
H 4 HOH 35  735  543 HOH HOH B . 
H 4 HOH 36  736  304 HOH HOH B . 
H 4 HOH 37  737  66  HOH HOH B . 
H 4 HOH 38  738  139 HOH HOH B . 
H 4 HOH 39  739  239 HOH HOH B . 
H 4 HOH 40  740  221 HOH HOH B . 
H 4 HOH 41  741  38  HOH HOH B . 
H 4 HOH 42  742  276 HOH HOH B . 
H 4 HOH 43  743  376 HOH HOH B . 
H 4 HOH 44  744  339 HOH HOH B . 
H 4 HOH 45  745  72  HOH HOH B . 
H 4 HOH 46  746  176 HOH HOH B . 
H 4 HOH 47  747  331 HOH HOH B . 
H 4 HOH 48  748  211 HOH HOH B . 
H 4 HOH 49  749  181 HOH HOH B . 
H 4 HOH 50  750  379 HOH HOH B . 
H 4 HOH 51  751  94  HOH HOH B . 
H 4 HOH 52  752  285 HOH HOH B . 
H 4 HOH 53  753  358 HOH HOH B . 
H 4 HOH 54  754  447 HOH HOH B . 
H 4 HOH 55  755  155 HOH HOH B . 
H 4 HOH 56  756  168 HOH HOH B . 
H 4 HOH 57  757  375 HOH HOH B . 
H 4 HOH 58  758  510 HOH HOH B . 
H 4 HOH 59  759  119 HOH HOH B . 
H 4 HOH 60  760  275 HOH HOH B . 
H 4 HOH 61  761  18  HOH HOH B . 
H 4 HOH 62  762  95  HOH HOH B . 
H 4 HOH 63  763  161 HOH HOH B . 
H 4 HOH 64  764  198 HOH HOH B . 
H 4 HOH 65  765  317 HOH HOH B . 
H 4 HOH 66  766  162 HOH HOH B . 
H 4 HOH 67  767  364 HOH HOH B . 
H 4 HOH 68  768  390 HOH HOH B . 
H 4 HOH 69  769  112 HOH HOH B . 
H 4 HOH 70  770  223 HOH HOH B . 
H 4 HOH 71  771  138 HOH HOH B . 
H 4 HOH 72  772  131 HOH HOH B . 
H 4 HOH 73  773  31  HOH HOH B . 
H 4 HOH 74  774  96  HOH HOH B . 
H 4 HOH 75  775  533 HOH HOH B . 
H 4 HOH 76  776  19  HOH HOH B . 
H 4 HOH 77  777  74  HOH HOH B . 
H 4 HOH 78  778  151 HOH HOH B . 
H 4 HOH 79  779  216 HOH HOH B . 
H 4 HOH 80  780  259 HOH HOH B . 
H 4 HOH 81  781  264 HOH HOH B . 
H 4 HOH 82  782  551 HOH HOH B . 
H 4 HOH 83  783  115 HOH HOH B . 
H 4 HOH 84  784  378 HOH HOH B . 
H 4 HOH 85  785  110 HOH HOH B . 
H 4 HOH 86  786  344 HOH HOH B . 
H 4 HOH 87  787  463 HOH HOH B . 
H 4 HOH 88  788  347 HOH HOH B . 
H 4 HOH 89  789  32  HOH HOH B . 
H 4 HOH 90  790  279 HOH HOH B . 
H 4 HOH 91  791  59  HOH HOH B . 
H 4 HOH 92  792  445 HOH HOH B . 
H 4 HOH 93  793  432 HOH HOH B . 
H 4 HOH 94  794  224 HOH HOH B . 
H 4 HOH 95  795  449 HOH HOH B . 
H 4 HOH 96  796  438 HOH HOH B . 
H 4 HOH 97  797  417 HOH HOH B . 
H 4 HOH 98  798  132 HOH HOH B . 
H 4 HOH 99  799  361 HOH HOH B . 
H 4 HOH 100 800  82  HOH HOH B . 
H 4 HOH 101 801  193 HOH HOH B . 
H 4 HOH 102 802  212 HOH HOH B . 
H 4 HOH 103 803  270 HOH HOH B . 
H 4 HOH 104 804  278 HOH HOH B . 
H 4 HOH 105 805  454 HOH HOH B . 
H 4 HOH 106 806  559 HOH HOH B . 
H 4 HOH 107 807  306 HOH HOH B . 
H 4 HOH 108 808  111 HOH HOH B . 
H 4 HOH 109 809  255 HOH HOH B . 
H 4 HOH 110 810  541 HOH HOH B . 
H 4 HOH 111 811  180 HOH HOH B . 
H 4 HOH 112 812  419 HOH HOH B . 
H 4 HOH 113 813  169 HOH HOH B . 
H 4 HOH 114 814  524 HOH HOH B . 
H 4 HOH 115 815  153 HOH HOH B . 
H 4 HOH 116 816  91  HOH HOH B . 
H 4 HOH 117 817  233 HOH HOH B . 
H 4 HOH 118 818  236 HOH HOH B . 
H 4 HOH 119 819  175 HOH HOH B . 
H 4 HOH 120 820  522 HOH HOH B . 
H 4 HOH 121 821  471 HOH HOH B . 
H 4 HOH 122 822  147 HOH HOH B . 
H 4 HOH 123 823  219 HOH HOH B . 
H 4 HOH 124 824  321 HOH HOH B . 
H 4 HOH 125 825  525 HOH HOH B . 
H 4 HOH 126 826  260 HOH HOH B . 
H 4 HOH 127 827  71  HOH HOH B . 
H 4 HOH 128 828  424 HOH HOH B . 
H 4 HOH 129 829  164 HOH HOH B . 
H 4 HOH 130 830  137 HOH HOH B . 
H 4 HOH 131 831  569 HOH HOH B . 
H 4 HOH 132 832  309 HOH HOH B . 
H 4 HOH 133 833  67  HOH HOH B . 
H 4 HOH 134 834  301 HOH HOH B . 
H 4 HOH 135 835  257 HOH HOH B . 
H 4 HOH 136 836  116 HOH HOH B . 
H 4 HOH 137 837  295 HOH HOH B . 
H 4 HOH 138 838  300 HOH HOH B . 
H 4 HOH 139 839  415 HOH HOH B . 
H 4 HOH 140 840  86  HOH HOH B . 
H 4 HOH 141 841  165 HOH HOH B . 
H 4 HOH 142 842  13  HOH HOH B . 
H 4 HOH 143 843  340 HOH HOH B . 
H 4 HOH 144 844  130 HOH HOH B . 
H 4 HOH 145 845  443 HOH HOH B . 
H 4 HOH 146 846  64  HOH HOH B . 
H 4 HOH 147 847  512 HOH HOH B . 
H 4 HOH 148 848  186 HOH HOH B . 
H 4 HOH 149 849  380 HOH HOH B . 
H 4 HOH 150 850  81  HOH HOH B . 
H 4 HOH 151 851  89  HOH HOH B . 
H 4 HOH 152 852  433 HOH HOH B . 
H 4 HOH 153 853  342 HOH HOH B . 
H 4 HOH 154 854  473 HOH HOH B . 
H 4 HOH 155 855  254 HOH HOH B . 
H 4 HOH 156 856  227 HOH HOH B . 
H 4 HOH 157 857  528 HOH HOH B . 
H 4 HOH 158 858  258 HOH HOH B . 
H 4 HOH 159 859  76  HOH HOH B . 
H 4 HOH 160 860  268 HOH HOH B . 
H 4 HOH 161 861  113 HOH HOH B . 
H 4 HOH 162 862  326 HOH HOH B . 
H 4 HOH 163 863  315 HOH HOH B . 
H 4 HOH 164 864  108 HOH HOH B . 
H 4 HOH 165 865  310 HOH HOH B . 
H 4 HOH 166 866  39  HOH HOH B . 
H 4 HOH 167 867  61  HOH HOH B . 
H 4 HOH 168 868  302 HOH HOH B . 
H 4 HOH 169 869  482 HOH HOH B . 
H 4 HOH 170 870  332 HOH HOH B . 
H 4 HOH 171 871  99  HOH HOH B . 
H 4 HOH 172 872  388 HOH HOH B . 
H 4 HOH 173 873  41  HOH HOH B . 
H 4 HOH 174 874  422 HOH HOH B . 
H 4 HOH 175 875  381 HOH HOH B . 
H 4 HOH 176 876  101 HOH HOH B . 
H 4 HOH 177 877  493 HOH HOH B . 
H 4 HOH 178 878  205 HOH HOH B . 
H 4 HOH 179 879  386 HOH HOH B . 
H 4 HOH 180 880  314 HOH HOH B . 
H 4 HOH 181 881  461 HOH HOH B . 
H 4 HOH 182 882  281 HOH HOH B . 
H 4 HOH 183 883  323 HOH HOH B . 
H 4 HOH 184 884  452 HOH HOH B . 
H 4 HOH 185 885  201 HOH HOH B . 
H 4 HOH 186 886  298 HOH HOH B . 
H 4 HOH 187 887  166 HOH HOH B . 
H 4 HOH 188 888  465 HOH HOH B . 
H 4 HOH 189 889  334 HOH HOH B . 
H 4 HOH 190 890  292 HOH HOH B . 
H 4 HOH 191 891  527 HOH HOH B . 
H 4 HOH 192 892  519 HOH HOH B . 
H 4 HOH 193 893  209 HOH HOH B . 
H 4 HOH 194 894  385 HOH HOH B . 
H 4 HOH 195 895  26  HOH HOH B . 
H 4 HOH 196 896  247 HOH HOH B . 
H 4 HOH 197 897  540 HOH HOH B . 
H 4 HOH 198 898  286 HOH HOH B . 
H 4 HOH 199 899  436 HOH HOH B . 
H 4 HOH 200 900  490 HOH HOH B . 
H 4 HOH 201 901  426 HOH HOH B . 
H 4 HOH 202 902  472 HOH HOH B . 
H 4 HOH 203 903  372 HOH HOH B . 
H 4 HOH 204 904  491 HOH HOH B . 
H 4 HOH 205 905  188 HOH HOH B . 
H 4 HOH 206 906  439 HOH HOH B . 
H 4 HOH 207 907  513 HOH HOH B . 
H 4 HOH 208 908  453 HOH HOH B . 
H 4 HOH 209 909  10  HOH HOH B . 
H 4 HOH 210 910  313 HOH HOH B . 
H 4 HOH 211 911  403 HOH HOH B . 
H 4 HOH 212 912  341 HOH HOH B . 
H 4 HOH 213 913  407 HOH HOH B . 
H 4 HOH 214 914  220 HOH HOH B . 
H 4 HOH 215 915  568 HOH HOH B . 
H 4 HOH 216 916  374 HOH HOH B . 
H 4 HOH 217 917  475 HOH HOH B . 
H 4 HOH 218 918  190 HOH HOH B . 
H 4 HOH 219 919  547 HOH HOH B . 
H 4 HOH 220 920  373 HOH HOH B . 
H 4 HOH 221 921  311 HOH HOH B . 
H 4 HOH 222 922  550 HOH HOH B . 
H 4 HOH 223 923  501 HOH HOH B . 
H 4 HOH 224 924  437 HOH HOH B . 
H 4 HOH 225 925  253 HOH HOH B . 
H 4 HOH 226 926  287 HOH HOH B . 
H 4 HOH 227 927  532 HOH HOH B . 
H 4 HOH 228 928  401 HOH HOH B . 
H 4 HOH 229 929  324 HOH HOH B . 
H 4 HOH 230 930  497 HOH HOH B . 
H 4 HOH 231 931  402 HOH HOH B . 
H 4 HOH 232 932  526 HOH HOH B . 
H 4 HOH 233 933  468 HOH HOH B . 
H 4 HOH 234 934  466 HOH HOH B . 
H 4 HOH 235 935  553 HOH HOH B . 
H 4 HOH 236 936  570 HOH HOH B . 
H 4 HOH 237 937  458 HOH HOH B . 
H 4 HOH 238 938  406 HOH HOH B . 
H 4 HOH 239 939  231 HOH HOH B . 
H 4 HOH 240 940  441 HOH HOH B . 
H 4 HOH 241 941  481 HOH HOH B . 
H 4 HOH 242 942  504 HOH HOH B . 
H 4 HOH 243 943  325 HOH HOH B . 
H 4 HOH 244 944  498 HOH HOH B . 
H 4 HOH 245 945  252 HOH HOH B . 
H 4 HOH 246 946  507 HOH HOH B . 
H 4 HOH 247 947  492 HOH HOH B . 
H 4 HOH 248 948  179 HOH HOH B . 
H 4 HOH 249 949  534 HOH HOH B . 
H 4 HOH 250 950  509 HOH HOH B . 
H 4 HOH 251 951  530 HOH HOH B . 
H 4 HOH 252 952  154 HOH HOH B . 
H 4 HOH 253 953  215 HOH HOH B . 
H 4 HOH 254 954  440 HOH HOH B . 
H 4 HOH 255 955  565 HOH HOH B . 
H 4 HOH 256 956  451 HOH HOH B . 
H 4 HOH 257 957  460 HOH HOH B . 
H 4 HOH 258 958  363 HOH HOH B . 
# 
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 ASP 48 ? CG  ? A ASP 48 CG  
2 1 Y 1 A ASP 48 ? OD1 ? A ASP 48 OD1 
3 1 Y 1 A ASP 48 ? OD2 ? A ASP 48 OD2 
4 1 Y 1 B ASP 48 ? CG  ? B ASP 48 CG  
5 1 Y 1 B ASP 48 ? OD1 ? B ASP 48 OD1 
6 1 Y 1 B ASP 48 ? OD2 ? B ASP 48 OD2 
# 
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  ? ? ? 5.8.0258 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GOV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     82.993 
_cell.length_a_esd                 ? 
_cell.length_b                     82.993 
_cell.length_b_esd                 ? 
_cell.length_c                     297.577 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9GOV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                170 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 65' 
_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                   9GOV 
_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             2.43 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.28 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.06 M of MgCl26 H2O, CaCl2 2 H2O, 0.1 M Tris, bicine, 20% glycerol, 10% PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-15 
_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   0.965459 
_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                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.965459 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GOV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               45.88 
_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                                     77465 
_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                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.05 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.107 
_reflns.pdbx_Rpim_I_all                                0.053 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.092 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.00 
_reflns_shell.d_res_low                                     2.04 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           18567 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4585 
_reflns_shell.percent_possible_obs                          100.0 
_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                               4.0 
_reflns_shell.pdbx_chi_squared                              1.01 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               0.933 
_reflns_shell.pdbx_Rpim_I_all                               0.459 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.524 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.810 
_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]                            -0.23 
_refine.aniso_B[1][2]                            -0.12 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.23 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.75 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               35.887 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.936 
_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                                 9GOV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.00 
_refine.ls_d_res_low                             45.84 
_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                     73450 
_refine.ls_number_reflns_R_free                  3915 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.40 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18589 
_refine.ls_R_factor_R_free                       0.22921 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18362 
_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                       0.179 
_refine.pdbx_overall_ESU_R_Free                  0.162 
_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                             4.924 
_refine.overall_SU_ML                            0.132 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        45.84 
_refine_hist.number_atoms_solvent             576 
_refine_hist.number_atoms_total               8839 
_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        8127 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         136 
_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' ? 0.009  0.013  8408  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  7643  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.636  1.650  11428 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.314  1.580  17700 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.656  5.000  1026  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 34.757 21.871 449   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.390 15.000 1310  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.954 15.000 61    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.079  0.200  1057  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  9467  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  1771  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.981  3.653  4143  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.980  3.653  4142  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.078  5.464  5156  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.078  5.464  5157  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.458  3.982  4265  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.458  3.983  4266  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.118  5.846  6273  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.117  70.327 37473 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.108  70.312 37057 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.000 
_refine_ls_shell.d_res_low                        2.052 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             296 
_refine_ls_shell.number_reflns_R_work             5445 
_refine_ls_shell.percent_reflns_obs               99.97 
_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                  0.284 
_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                  0.345 
# 
_struct.entry_id                     9GOV 
_struct.title                        '4-Allyl syringol oxidase from Streptomyces cavernae: complex with Propanol syringol' 
_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        9GOV 
_struct_keywords.text            'flavin, oxidase, biocatalysis, FAD, 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 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 2 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9GOV 
_struct_ref.pdbx_db_accession          9GOV 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
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 9GOV A 1 ? 554 ? 9GOV 1 ? 554 ? 1 554 
2 1 9GOV B 1 ? 554 ? 9GOV 1 ? 554 ? 1 554 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 9700  ? 
1 MORE         -78   ? 
1 'SSA (A^2)'  32910 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? GLY A 26  ? SER A 10  GLY A 26  1 ? 17 
HELX_P HELX_P2  AA2 ASP A 33  ? ARG A 39  ? ASP A 33  ARG A 39  1 ? 7  
HELX_P HELX_P3  AA3 ASP A 62  ? GLY A 77  ? ASP A 62  GLY A 77  1 ? 16 
HELX_P HELX_P4  AA4 THR A 130 ? ALA A 142 ? THR A 130 ALA A 142 1 ? 13 
HELX_P HELX_P5  AA5 SER A 156 ? ASP A 163 ? SER A 156 ASP A 163 1 ? 8  
HELX_P HELX_P6  AA6 ASP A 173 ? TRP A 177 ? ASP A 173 TRP A 177 1 ? 5  
HELX_P HELX_P7  AA7 GLY A 194 ? LEU A 198 ? GLY A 194 LEU A 198 5 ? 5  
HELX_P HELX_P8  AA8 PRO A 215 ? THR A 220 ? PRO A 215 THR A 220 5 ? 6  
HELX_P HELX_P9  AA9 ASN A 250 ? SER A 252 ? ASN A 250 SER A 252 5 ? 3  
HELX_P HELX_P10 AB1 ASP A 253 ? ILE A 266 ? ASP A 253 ILE A 266 1 ? 14 
HELX_P HELX_P11 AB2 ILE A 280 ? SER A 288 ? ILE A 280 SER A 288 1 ? 9  
HELX_P HELX_P12 AB3 GLN A 289 ? TRP A 293 ? GLN A 289 TRP A 293 5 ? 5  
HELX_P HELX_P13 AB4 PRO A 301 ? GLY A 313 ? PRO A 301 GLY A 313 1 ? 13 
HELX_P HELX_P14 AB5 PRO A 326 ? GLY A 342 ? PRO A 326 GLY A 342 1 ? 17 
HELX_P HELX_P15 AB6 ASP A 357 ? GLY A 359 ? ASP A 357 GLY A 359 5 ? 3  
HELX_P HELX_P16 AB7 ALA A 360 ? ASN A 370 ? ALA A 360 ASN A 370 1 ? 11 
HELX_P HELX_P17 AB8 LEU A 376 ? TRP A 384 ? LEU A 376 TRP A 384 5 ? 9  
HELX_P HELX_P18 AB9 VAL A 400 ? TYR A 418 ? VAL A 400 TYR A 418 1 ? 19 
HELX_P HELX_P19 AC1 ASP A 445 ? GLU A 466 ? ASP A 445 GLU A 466 1 ? 22 
HELX_P HELX_P20 AC2 HIS A 474 ? ALA A 476 ? HIS A 474 ALA A 476 5 ? 3  
HELX_P HELX_P21 AC3 LEU A 477 ? TYR A 485 ? LEU A 477 TYR A 485 1 ? 9  
HELX_P HELX_P22 AC4 ASN A 486 ? ASP A 504 ? ASN A 486 ASP A 504 1 ? 19 
HELX_P HELX_P23 AC5 GLY A 512 ? VAL A 516 ? GLY A 512 VAL A 516 5 ? 5  
HELX_P HELX_P24 AC6 PRO A 518 ? ARG A 522 ? PRO A 518 ARG A 522 5 ? 5  
HELX_P HELX_P25 AC7 SER B 10  ? GLY B 26  ? SER B 10  GLY B 26  1 ? 17 
HELX_P HELX_P26 AC8 ASP B 33  ? ARG B 39  ? ASP B 33  ARG B 39  1 ? 7  
HELX_P HELX_P27 AC9 ASP B 62  ? GLY B 77  ? ASP B 62  GLY B 77  1 ? 16 
HELX_P HELX_P28 AD1 THR B 130 ? ALA B 142 ? THR B 130 ALA B 142 1 ? 13 
HELX_P HELX_P29 AD2 SER B 156 ? ASP B 163 ? SER B 156 ASP B 163 1 ? 8  
HELX_P HELX_P30 AD3 ASP B 173 ? TRP B 177 ? ASP B 173 TRP B 177 1 ? 5  
HELX_P HELX_P31 AD4 GLY B 194 ? LEU B 198 ? GLY B 194 LEU B 198 5 ? 5  
HELX_P HELX_P32 AD5 PRO B 215 ? THR B 220 ? PRO B 215 THR B 220 5 ? 6  
HELX_P HELX_P33 AD6 ASN B 250 ? SER B 252 ? ASN B 250 SER B 252 5 ? 3  
HELX_P HELX_P34 AD7 ASP B 253 ? ILE B 266 ? ASP B 253 ILE B 266 1 ? 14 
HELX_P HELX_P35 AD8 ILE B 280 ? ALA B 285 ? ILE B 280 ALA B 285 1 ? 6  
HELX_P HELX_P36 AD9 GLN B 289 ? TRP B 293 ? GLN B 289 TRP B 293 5 ? 5  
HELX_P HELX_P37 AE1 PRO B 301 ? GLY B 313 ? PRO B 301 GLY B 313 1 ? 13 
HELX_P HELX_P38 AE2 PRO B 326 ? GLY B 342 ? PRO B 326 GLY B 342 1 ? 17 
HELX_P HELX_P39 AE3 ASP B 357 ? GLY B 359 ? ASP B 357 GLY B 359 5 ? 3  
HELX_P HELX_P40 AE4 ALA B 360 ? ASN B 370 ? ALA B 360 ASN B 370 1 ? 11 
HELX_P HELX_P41 AE5 LEU B 376 ? TRP B 384 ? LEU B 376 TRP B 384 5 ? 9  
HELX_P HELX_P42 AE6 VAL B 400 ? TYR B 418 ? VAL B 400 TYR B 418 1 ? 19 
HELX_P HELX_P43 AE7 ASP B 445 ? GLU B 466 ? ASP B 445 GLU B 466 1 ? 22 
HELX_P HELX_P44 AE8 HIS B 474 ? ALA B 476 ? HIS B 474 ALA B 476 5 ? 3  
HELX_P HELX_P45 AE9 LEU B 477 ? TYR B 485 ? LEU B 477 TYR B 485 1 ? 9  
HELX_P HELX_P46 AF1 ASN B 486 ? ASP B 504 ? ASN B 486 ASP B 504 1 ? 19 
HELX_P HELX_P47 AF2 GLY B 512 ? VAL B 516 ? GLY B 512 VAL B 516 5 ? 5  
HELX_P HELX_P48 AF3 PRO B 518 ? ARG B 522 ? PRO B 518 ARG B 522 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
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 ALA 269 A . ? ALA 269 A PRO 270 A ? PRO 270 A 1 -1.49 
2 ALA 269 B . ? ALA 269 B PRO 270 B ? PRO 270 B 1 3.72  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 7 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 7 ? 
AB1 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AA9 6 7 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB1 5 6 ? anti-parallel 
AB1 6 7 ? anti-parallel 
AB1 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 30  ? ARG A 31  ? VAL A 30  ARG A 31  
AA1 2 ALA A 56  ? ILE A 58  ? ALA A 56  ILE A 58  
AA1 3 VAL A 102 ? ASN A 105 ? VAL A 102 ASN A 105 
AA1 4 LEU A 80  ? ILE A 83  ? LEU A 80  ILE A 83  
AA2 1 ILE A 113 ? ASP A 117 ? ILE A 113 ASP A 117 
AA2 2 TYR A 122 ? LEU A 125 ? TYR A 122 LEU A 125 
AA2 3 ILE A 226 ? ALA A 233 ? ILE A 226 ALA A 233 
AA2 4 GLN A 178 ? VAL A 184 ? GLN A 178 VAL A 184 
AA2 5 VAL A 190 ? ARG A 192 ? VAL A 190 ARG A 192 
AA3 1 LEU A 145 ? MET A 146 ? LEU A 145 MET A 146 
AA3 2 MET A 235 ? GLN A 236 ? MET A 235 GLN A 236 
AA4 1 ARG A 348 ? THR A 351 ? ARG A 348 THR A 351 
AA4 2 SER A 241 ? PHE A 248 ? SER A 241 PHE A 248 
AA4 3 TRP A 317 ? TYR A 324 ? TRP A 317 TYR A 324 
AA4 4 VAL A 276 ? ASN A 279 ? VAL A 276 ASN A 279 
AA4 5 ALA A 424 ? VAL A 428 ? ALA A 424 VAL A 428 
AA4 6 MET A 433 ? ASP A 442 ? MET A 433 ASP A 442 
AA4 7 ALA A 388 ? PHE A 393 ? ALA A 388 PHE A 393 
AA5 1 ARG A 348 ? THR A 351 ? ARG A 348 THR A 351 
AA5 2 SER A 241 ? PHE A 248 ? SER A 241 PHE A 248 
AA5 3 TRP A 317 ? TYR A 324 ? TRP A 317 TYR A 324 
AA5 4 VAL A 276 ? ASN A 279 ? VAL A 276 ASN A 279 
AA5 5 ALA A 424 ? VAL A 428 ? ALA A 424 VAL A 428 
AA5 6 MET A 433 ? ASP A 442 ? MET A 433 ASP A 442 
AA5 7 ILE A 396 ? SER A 397 ? ILE A 396 SER A 397 
AA6 1 VAL B 30  ? ARG B 31  ? VAL B 30  ARG B 31  
AA6 2 ALA B 56  ? ILE B 58  ? ALA B 56  ILE B 58  
AA6 3 VAL B 102 ? ASN B 105 ? VAL B 102 ASN B 105 
AA6 4 LEU B 80  ? ILE B 83  ? LEU B 80  ILE B 83  
AA7 1 ILE B 113 ? ASP B 117 ? ILE B 113 ASP B 117 
AA7 2 TYR B 122 ? LEU B 125 ? TYR B 122 LEU B 125 
AA7 3 ILE B 226 ? ALA B 233 ? ILE B 226 ALA B 233 
AA7 4 GLN B 178 ? VAL B 184 ? GLN B 178 VAL B 184 
AA7 5 VAL B 190 ? ARG B 192 ? VAL B 190 ARG B 192 
AA8 1 LEU B 145 ? MET B 146 ? LEU B 145 MET B 146 
AA8 2 MET B 235 ? GLN B 236 ? MET B 235 GLN B 236 
AA9 1 ARG B 348 ? THR B 351 ? ARG B 348 THR B 351 
AA9 2 SER B 241 ? PHE B 248 ? SER B 241 PHE B 248 
AA9 3 TRP B 317 ? TYR B 324 ? TRP B 317 TYR B 324 
AA9 4 VAL B 276 ? ASN B 279 ? VAL B 276 ASN B 279 
AA9 5 ALA B 423 ? VAL B 428 ? ALA B 423 VAL B 428 
AA9 6 MET B 433 ? ASP B 442 ? MET B 433 ASP B 442 
AA9 7 ALA B 388 ? PHE B 393 ? ALA B 388 PHE B 393 
AB1 1 ARG B 348 ? THR B 351 ? ARG B 348 THR B 351 
AB1 2 SER B 241 ? PHE B 248 ? SER B 241 PHE B 248 
AB1 3 TRP B 317 ? TYR B 324 ? TRP B 317 TYR B 324 
AB1 4 VAL B 276 ? ASN B 279 ? VAL B 276 ASN B 279 
AB1 5 ALA B 423 ? VAL B 428 ? ALA B 423 VAL B 428 
AB1 6 MET B 433 ? ASP B 442 ? MET B 433 ASP B 442 
AB1 7 PRO B 395 ? SER B 397 ? PRO B 395 SER B 397 
AB1 8 GLY B 469 ? GLU B 470 ? GLY B 469 GLU B 470 
# 
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 ARG A 31  ? N ARG A 31  O VAL A 57  ? O VAL A 57  
AA1 2 3 N ILE A 58  ? N ILE A 58  O VAL A 103 ? O VAL A 103 
AA1 3 4 O VAL A 104 ? O VAL A 104 N SER A 81  ? N SER A 81  
AA2 1 2 N GLU A 115 ? N GLU A 115 O LEU A 124 ? O LEU A 124 
AA2 2 3 N LEU A 125 ? N LEU A 125 O MET A 230 ? O MET A 230 
AA2 3 4 O ILE A 226 ? O ILE A 226 N VAL A 184 ? N VAL A 184 
AA2 4 5 N VAL A 183 ? N VAL A 183 O MET A 191 ? O MET A 191 
AA3 1 2 N MET A 146 ? N MET A 146 O MET A 235 ? O MET A 235 
AA4 1 2 O GLN A 350 ? O GLN A 350 N GLN A 245 ? N GLN A 245 
AA4 2 3 N ILE A 246 ? N ILE A 246 O PHE A 319 ? O PHE A 319 
AA4 3 4 O ASN A 318 ? O ASN A 318 N ARG A 278 ? N ARG A 278 
AA4 4 5 N LEU A 277 ? N LEU A 277 O PHE A 426 ? O PHE A 426 
AA4 5 6 N VAL A 427 ? N VAL A 427 O HIS A 434 ? O HIS A 434 
AA4 6 7 O ALA A 437 ? O ALA A 437 N PHE A 393 ? N PHE A 393 
AA5 1 2 O GLN A 350 ? O GLN A 350 N GLN A 245 ? N GLN A 245 
AA5 2 3 N ILE A 246 ? N ILE A 246 O PHE A 319 ? O PHE A 319 
AA5 3 4 O ASN A 318 ? O ASN A 318 N ARG A 278 ? N ARG A 278 
AA5 4 5 N LEU A 277 ? N LEU A 277 O PHE A 426 ? O PHE A 426 
AA5 5 6 N VAL A 427 ? N VAL A 427 O HIS A 434 ? O HIS A 434 
AA5 6 7 O MET A 433 ? O MET A 433 N SER A 397 ? N SER A 397 
AA6 1 2 N ARG B 31  ? N ARG B 31  O VAL B 57  ? O VAL B 57  
AA6 2 3 N ILE B 58  ? N ILE B 58  O ASN B 105 ? O ASN B 105 
AA6 3 4 O VAL B 104 ? O VAL B 104 N SER B 81  ? N SER B 81  
AA7 1 2 N GLU B 115 ? N GLU B 115 O LEU B 124 ? O LEU B 124 
AA7 2 3 N LEU B 125 ? N LEU B 125 O MET B 230 ? O MET B 230 
AA7 3 4 O ILE B 226 ? O ILE B 226 N VAL B 184 ? N VAL B 184 
AA7 4 5 N VAL B 183 ? N VAL B 183 O MET B 191 ? O MET B 191 
AA8 1 2 N MET B 146 ? N MET B 146 O MET B 235 ? O MET B 235 
AA9 1 2 O GLN B 350 ? O GLN B 350 N GLN B 245 ? N GLN B 245 
AA9 2 3 N ILE B 246 ? N ILE B 246 O PHE B 319 ? O PHE B 319 
AA9 3 4 O ASN B 318 ? O ASN B 318 N ARG B 278 ? N ARG B 278 
AA9 4 5 N ASN B 279 ? N ASN B 279 O ALA B 424 ? O ALA B 424 
AA9 5 6 N ALA B 423 ? N ALA B 423 O LEU B 438 ? O LEU B 438 
AA9 6 7 O ALA B 437 ? O ALA B 437 N PHE B 393 ? N PHE B 393 
AB1 1 2 O GLN B 350 ? O GLN B 350 N GLN B 245 ? N GLN B 245 
AB1 2 3 N ILE B 246 ? N ILE B 246 O PHE B 319 ? O PHE B 319 
AB1 3 4 O ASN B 318 ? O ASN B 318 N ARG B 278 ? N ARG B 278 
AB1 4 5 N ASN B 279 ? N ASN B 279 O ALA B 424 ? O ALA B 424 
AB1 5 6 N ALA B 423 ? N ALA B 423 O LEU B 438 ? O LEU B 438 
AB1 6 7 O MET B 433 ? O MET B 433 N SER B 397 ? N SER B 397 
AB1 7 8 N ILE B 396 ? N ILE B 396 O GLY B 469 ? O GLY B 469 
# 
_pdbx_entry_details.entry_id                   9GOV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OG  A SER 99   ? ? O   A HOH 801  ? ? 1.27 
2  1 OE1 A GLN 221  ? ? O   B PHE 211  ? ? 1.83 
3  1 NE2 B HIS 390  ? ? C8M B FAD 601  ? ? 1.95 
4  1 OH  B TYR 471  ? ? O   B HOH 701  ? ? 1.95 
5  1 O   B HOH 918  ? ? O   B HOH 921  ? ? 2.00 
6  1 CB  A SER 99   ? ? O   A HOH 801  ? ? 2.04 
7  1 O   A HOH 1117 ? ? O   A HOH 1118 ? ? 2.06 
8  1 O   B HOH 723  ? ? O   B HOH 917  ? ? 2.08 
9  1 O   B HOH 753  ? ? O   B HOH 940  ? ? 2.08 
10 1 O   B HOH 947  ? ? O   B HOH 949  ? ? 2.10 
11 1 O   A HOH 1075 ? ? O   A HOH 1113 ? ? 2.10 
12 1 OD2 A ASP 23   ? ? O   A HOH 802  ? ? 2.10 
13 1 O   A HOH 807  ? ? O   A HOH 977  ? ? 2.13 
14 1 O   B HOH 709  ? ? O   B HOH 901  ? ? 2.14 
15 1 NZ  B LYS 368  ? ? O   B HOH 702  ? ? 2.17 
16 1 O   A HOH 1067 ? ? O   A HOH 1115 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     880 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     906 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_545 
_pdbx_validate_symm_contact.dist              2.07 
# 
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 ASP A 48  ? ? -84.43  -110.20 
2  1 ALA A 49  ? ? -174.23 -24.11  
3  1 SER A 84  ? ? -94.42  -76.05  
4  1 TYR A 171 ? ? -96.65  31.12   
5  1 TYR A 294 ? ? -174.89 132.87  
6  1 HIS A 356 ? ? -152.17 61.18   
7  1 SER A 394 ? ? -147.04 58.91   
8  1 LEU A 430 ? ? -140.91 -63.71  
9  1 TYR A 485 ? ? -90.61  50.08   
10 1 ALA A 510 ? ? 25.15   64.31   
11 1 TYR B 44  ? ? -118.48 58.64   
12 1 SER B 84  ? ? -94.68  -74.03  
13 1 PRO B 150 ? ? -79.61  -167.78 
14 1 TYR B 171 ? ? -92.58  30.78   
15 1 VAL B 287 ? ? 85.34   0.99    
16 1 PRO B 327 ? ? -35.78  -39.67  
17 1 ARG B 355 ? ? -121.98 -86.49  
18 1 SER B 394 ? ? -153.15 57.96   
19 1 LEU B 430 ? ? -139.59 -60.07  
20 1 ALA B 510 ? ? 26.01   64.77   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A ALA 527 ? A ALA 527 
4  1 Y 1 A ALA 528 ? A ALA 528 
5  1 Y 1 A ALA 529 ? A ALA 529 
6  1 Y 1 A LEU 530 ? A LEU 530 
7  1 Y 1 A LYS 531 ? A LYS 531 
8  1 Y 1 A LEU 532 ? A LEU 532 
9  1 Y 1 A ARG 533 ? A ARG 533 
10 1 Y 1 A VAL 534 ? A VAL 534 
11 1 Y 1 A ASP 535 ? A ASP 535 
12 1 Y 1 A PRO 536 ? A PRO 536 
13 1 Y 1 A ALA 537 ? A ALA 537 
14 1 Y 1 A ALA 538 ? A ALA 538 
15 1 Y 1 A ASN 539 ? A ASN 539 
16 1 Y 1 A LYS 540 ? A LYS 540 
17 1 Y 1 A ALA 541 ? A ALA 541 
18 1 Y 1 A ARG 542 ? A ARG 542 
19 1 Y 1 A LYS 543 ? A LYS 543 
20 1 Y 1 A GLU 544 ? A GLU 544 
21 1 Y 1 A ALA 545 ? A ALA 545 
22 1 Y 1 A GLU 546 ? A GLU 546 
23 1 Y 1 A LEU 547 ? A LEU 547 
24 1 Y 1 A ALA 548 ? A ALA 548 
25 1 Y 1 A ALA 549 ? A ALA 549 
26 1 Y 1 A ALA 550 ? A ALA 550 
27 1 Y 1 A THR 551 ? A THR 551 
28 1 Y 1 A ALA 552 ? A ALA 552 
29 1 Y 1 A GLU 553 ? A GLU 553 
30 1 Y 1 A GLN 554 ? A GLN 554 
31 1 Y 1 B MET 1   ? B MET 1   
32 1 Y 1 B THR 2   ? B THR 2   
33 1 Y 1 B ARG 3   ? B ARG 3   
34 1 Y 1 B ALA 527 ? B ALA 527 
35 1 Y 1 B ALA 528 ? B ALA 528 
36 1 Y 1 B ALA 529 ? B ALA 529 
37 1 Y 1 B LEU 530 ? B LEU 530 
38 1 Y 1 B LYS 531 ? B LYS 531 
39 1 Y 1 B LEU 532 ? B LEU 532 
40 1 Y 1 B ARG 533 ? B ARG 533 
41 1 Y 1 B VAL 534 ? B VAL 534 
42 1 Y 1 B ASP 535 ? B ASP 535 
43 1 Y 1 B PRO 536 ? B PRO 536 
44 1 Y 1 B ALA 537 ? B ALA 537 
45 1 Y 1 B ALA 538 ? B ALA 538 
46 1 Y 1 B ASN 539 ? B ASN 539 
47 1 Y 1 B LYS 540 ? B LYS 540 
48 1 Y 1 B ALA 541 ? B ALA 541 
49 1 Y 1 B ARG 542 ? B ARG 542 
50 1 Y 1 B LYS 543 ? B LYS 543 
51 1 Y 1 B GLU 544 ? B GLU 544 
52 1 Y 1 B ALA 545 ? B ALA 545 
53 1 Y 1 B GLU 546 ? B GLU 546 
54 1 Y 1 B LEU 547 ? B LEU 547 
55 1 Y 1 B ALA 548 ? B ALA 548 
56 1 Y 1 B ALA 549 ? B ALA 549 
57 1 Y 1 B ALA 550 ? B ALA 550 
58 1 Y 1 B THR 551 ? B THR 551 
59 1 Y 1 B ALA 552 ? B ALA 552 
60 1 Y 1 B GLU 553 ? B GLU 553 
61 1 Y 1 B GLN 554 ? B GLN 554 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
GLN N      N N N 174 
GLN CA     C N S 175 
GLN C      C N N 176 
GLN O      O N N 177 
GLN CB     C N N 178 
GLN CG     C N N 179 
GLN CD     C N N 180 
GLN OE1    O N N 181 
GLN NE2    N N N 182 
GLN OXT    O N N 183 
GLN H      H N N 184 
GLN H2     H N N 185 
GLN HA     H N N 186 
GLN HB2    H N N 187 
GLN HB3    H N N 188 
GLN HG2    H N N 189 
GLN HG3    H N N 190 
GLN HE21   H N N 191 
GLN HE22   H N N 192 
GLN HXT    H N N 193 
GLU N      N N N 194 
GLU CA     C N S 195 
GLU C      C N N 196 
GLU O      O N N 197 
GLU CB     C N N 198 
GLU CG     C N N 199 
GLU CD     C N N 200 
GLU OE1    O N N 201 
GLU OE2    O N N 202 
GLU OXT    O N N 203 
GLU H      H N N 204 
GLU H2     H N N 205 
GLU HA     H N N 206 
GLU HB2    H N N 207 
GLU HB3    H N N 208 
GLU HG2    H N N 209 
GLU HG3    H N N 210 
GLU HE2    H N N 211 
GLU HXT    H N N 212 
GLY N      N N N 213 
GLY CA     C N N 214 
GLY C      C N N 215 
GLY O      O N N 216 
GLY OXT    O N N 217 
GLY H      H N N 218 
GLY H2     H N N 219 
GLY HA2    H N N 220 
GLY HA3    H N N 221 
GLY HXT    H N N 222 
HIS N      N N N 223 
HIS CA     C N S 224 
HIS C      C N N 225 
HIS O      O N N 226 
HIS CB     C N N 227 
HIS CG     C Y N 228 
HIS ND1    N Y N 229 
HIS CD2    C Y N 230 
HIS CE1    C Y N 231 
HIS NE2    N Y N 232 
HIS OXT    O N N 233 
HIS H      H N N 234 
HIS H2     H N N 235 
HIS HA     H N N 236 
HIS HB2    H N N 237 
HIS HB3    H N N 238 
HIS HD1    H N N 239 
HIS HD2    H N N 240 
HIS HE1    H N N 241 
HIS HE2    H N N 242 
HIS HXT    H N N 243 
HOH O      O N N 244 
HOH H1     H N N 245 
HOH H2     H N N 246 
ILE N      N N N 247 
ILE CA     C N S 248 
ILE C      C N N 249 
ILE O      O N N 250 
ILE CB     C N S 251 
ILE CG1    C N N 252 
ILE CG2    C N N 253 
ILE CD1    C N N 254 
ILE OXT    O N N 255 
ILE H      H N N 256 
ILE H2     H N N 257 
ILE HA     H N N 258 
ILE HB     H N N 259 
ILE HG12   H N N 260 
ILE HG13   H N N 261 
ILE HG21   H N N 262 
ILE HG22   H N N 263 
ILE HG23   H N N 264 
ILE HD11   H N N 265 
ILE HD12   H N N 266 
ILE HD13   H N N 267 
ILE HXT    H N N 268 
LEU N      N N N 269 
LEU CA     C N S 270 
LEU C      C N N 271 
LEU O      O N N 272 
LEU CB     C N N 273 
LEU CG     C N N 274 
LEU CD1    C N N 275 
LEU CD2    C N N 276 
LEU OXT    O N N 277 
LEU H      H N N 278 
LEU H2     H N N 279 
LEU HA     H N N 280 
LEU HB2    H N N 281 
LEU HB3    H N N 282 
LEU HG     H N N 283 
LEU HD11   H N N 284 
LEU HD12   H N N 285 
LEU HD13   H N N 286 
LEU HD21   H N N 287 
LEU HD22   H N N 288 
LEU HD23   H N N 289 
LEU HXT    H N N 290 
LYS N      N N N 291 
LYS CA     C N S 292 
LYS C      C N N 293 
LYS O      O N N 294 
LYS CB     C N N 295 
LYS CG     C N N 296 
LYS CD     C N N 297 
LYS CE     C N N 298 
LYS NZ     N N N 299 
LYS OXT    O N N 300 
LYS H      H N N 301 
LYS H2     H N N 302 
LYS HA     H N N 303 
LYS HB2    H N N 304 
LYS HB3    H N N 305 
LYS HG2    H N N 306 
LYS HG3    H N N 307 
LYS HD2    H N N 308 
LYS HD3    H N N 309 
LYS HE2    H N N 310 
LYS HE3    H N N 311 
LYS HZ1    H N N 312 
LYS HZ2    H N N 313 
LYS HZ3    H N N 314 
LYS HXT    H N N 315 
MET N      N N N 316 
MET CA     C N S 317 
MET C      C N N 318 
MET O      O N N 319 
MET CB     C N N 320 
MET CG     C N N 321 
MET SD     S N N 322 
MET CE     C N N 323 
MET OXT    O N N 324 
MET H      H N N 325 
MET H2     H N N 326 
MET HA     H N N 327 
MET HB2    H N N 328 
MET HB3    H N N 329 
MET HG2    H N N 330 
MET HG3    H N N 331 
MET HE1    H N N 332 
MET HE2    H N N 333 
MET HE3    H N N 334 
MET HXT    H N N 335 
PHE N      N N N 336 
PHE CA     C N S 337 
PHE C      C N N 338 
PHE O      O N N 339 
PHE CB     C N N 340 
PHE CG     C Y N 341 
PHE CD1    C Y N 342 
PHE CD2    C Y N 343 
PHE CE1    C Y N 344 
PHE CE2    C Y N 345 
PHE CZ     C Y N 346 
PHE OXT    O N N 347 
PHE H      H N N 348 
PHE H2     H N N 349 
PHE HA     H N N 350 
PHE HB2    H N N 351 
PHE HB3    H N N 352 
PHE HD1    H N N 353 
PHE HD2    H N N 354 
PHE HE1    H N N 355 
PHE HE2    H N N 356 
PHE HZ     H N N 357 
PHE HXT    H N N 358 
PRO N      N N N 359 
PRO CA     C N S 360 
PRO C      C N N 361 
PRO O      O N N 362 
PRO CB     C N N 363 
PRO CG     C N N 364 
PRO CD     C N N 365 
PRO OXT    O N N 366 
PRO H      H N N 367 
PRO HA     H N N 368 
PRO HB2    H N N 369 
PRO HB3    H N N 370 
PRO HG2    H N N 371 
PRO HG3    H N N 372 
PRO HD2    H N N 373 
PRO HD3    H N N 374 
PRO HXT    H N N 375 
QBF CAA    C N N 376 
QBF CAC    C Y N 377 
QBF CAD    C Y N 378 
QBF CAE    C Y N 379 
QBF CAF    C Y N 380 
QBF CAG    C Y N 381 
QBF CAH    C Y N 382 
QBF CAK    C N N 383 
QBF CAL    C N N 384 
QBF CAM    C N N 385 
QBF CAN    C N N 386 
QBF OAB    O N N 387 
QBF OAI    O N N 388 
QBF OAJ    O N N 389 
QBF OAO    O N N 390 
QBF H1     H N N 391 
QBF H2     H N N 392 
QBF H3     H N N 393 
QBF H4     H N N 394 
QBF H5     H N N 395 
QBF H6     H N N 396 
QBF H7     H N N 397 
QBF H8     H N N 398 
QBF H9     H N N 399 
QBF H10    H N N 400 
QBF H11    H N N 401 
QBF H12    H N N 402 
QBF H13    H N N 403 
QBF H14    H N N 404 
QBF H15    H N N 405 
QBF H16    H N N 406 
SER N      N N N 407 
SER CA     C N S 408 
SER C      C N N 409 
SER O      O N N 410 
SER CB     C N N 411 
SER OG     O N N 412 
SER OXT    O N N 413 
SER H      H N N 414 
SER H2     H N N 415 
SER HA     H N N 416 
SER HB2    H N N 417 
SER HB3    H N N 418 
SER HG     H N N 419 
SER HXT    H N N 420 
THR N      N N N 421 
THR CA     C N S 422 
THR C      C N N 423 
THR O      O N N 424 
THR CB     C N R 425 
THR OG1    O N N 426 
THR CG2    C N N 427 
THR OXT    O N N 428 
THR H      H N N 429 
THR H2     H N N 430 
THR HA     H N N 431 
THR HB     H N N 432 
THR HG1    H N N 433 
THR HG21   H N N 434 
THR HG22   H N N 435 
THR HG23   H N N 436 
THR HXT    H N N 437 
TRP N      N N N 438 
TRP CA     C N S 439 
TRP C      C N N 440 
TRP O      O N N 441 
TRP CB     C N N 442 
TRP CG     C Y N 443 
TRP CD1    C Y N 444 
TRP CD2    C Y N 445 
TRP NE1    N Y N 446 
TRP CE2    C Y N 447 
TRP CE3    C Y N 448 
TRP CZ2    C Y N 449 
TRP CZ3    C Y N 450 
TRP CH2    C Y N 451 
TRP OXT    O N N 452 
TRP H      H N N 453 
TRP H2     H N N 454 
TRP HA     H N N 455 
TRP HB2    H N N 456 
TRP HB3    H N N 457 
TRP HD1    H N N 458 
TRP HE1    H N N 459 
TRP HE3    H N N 460 
TRP HZ2    H N N 461 
TRP HZ3    H N N 462 
TRP HH2    H N N 463 
TRP HXT    H N N 464 
TYR N      N N N 465 
TYR CA     C N S 466 
TYR C      C N N 467 
TYR O      O N N 468 
TYR CB     C N N 469 
TYR CG     C Y N 470 
TYR CD1    C Y N 471 
TYR CD2    C Y N 472 
TYR CE1    C Y N 473 
TYR CE2    C Y N 474 
TYR CZ     C Y N 475 
TYR OH     O N N 476 
TYR OXT    O N N 477 
TYR H      H N N 478 
TYR H2     H N N 479 
TYR HA     H N N 480 
TYR HB2    H N N 481 
TYR HB3    H N N 482 
TYR HD1    H N N 483 
TYR HD2    H N N 484 
TYR HE1    H N N 485 
TYR HE2    H N N 486 
TYR HH     H N N 487 
TYR HXT    H N N 488 
VAL N      N N N 489 
VAL CA     C N S 490 
VAL C      C N N 491 
VAL O      O N N 492 
VAL CB     C N N 493 
VAL CG1    C N N 494 
VAL CG2    C N N 495 
VAL OXT    O N N 496 
VAL H      H N N 497 
VAL H2     H N N 498 
VAL HA     H N N 499 
VAL HB     H N N 500 
VAL HG11   H N N 501 
VAL HG12   H N N 502 
VAL HG13   H N N 503 
VAL HG21   H N N 504 
VAL HG22   H N N 505 
VAL HG23   H N N 506 
VAL HXT    H N N 507 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
HIS N     CA     sing N N 220 
HIS N     H      sing N N 221 
HIS N     H2     sing N N 222 
HIS CA    C      sing N N 223 
HIS CA    CB     sing N N 224 
HIS CA    HA     sing N N 225 
HIS C     O      doub N N 226 
HIS C     OXT    sing N N 227 
HIS CB    CG     sing N N 228 
HIS CB    HB2    sing N N 229 
HIS CB    HB3    sing N N 230 
HIS CG    ND1    sing Y N 231 
HIS CG    CD2    doub Y N 232 
HIS ND1   CE1    doub Y N 233 
HIS ND1   HD1    sing N N 234 
HIS CD2   NE2    sing Y N 235 
HIS CD2   HD2    sing N N 236 
HIS CE1   NE2    sing Y N 237 
HIS CE1   HE1    sing N N 238 
HIS NE2   HE2    sing N N 239 
HIS OXT   HXT    sing N N 240 
HOH O     H1     sing N N 241 
HOH O     H2     sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
QBF OAI   CAH    sing N N 368 
QBF OAJ   CAK    sing N N 369 
QBF OAJ   CAG    sing N N 370 
QBF CAH   CAG    doub Y N 371 
QBF CAH   CAC    sing Y N 372 
QBF CAG   CAF    sing Y N 373 
QBF OAB   CAC    sing N N 374 
QBF OAB   CAA    sing N N 375 
QBF CAC   CAD    doub Y N 376 
QBF CAF   CAE    doub Y N 377 
QBF CAD   CAE    sing Y N 378 
QBF CAE   CAL    sing N N 379 
QBF CAL   CAM    sing N N 380 
QBF CAM   CAN    sing N N 381 
QBF CAN   OAO    sing N N 382 
QBF CAA   H1     sing N N 383 
QBF CAA   H2     sing N N 384 
QBF CAA   H3     sing N N 385 
QBF CAD   H4     sing N N 386 
QBF CAF   H5     sing N N 387 
QBF CAK   H6     sing N N 388 
QBF CAK   H7     sing N N 389 
QBF CAK   H8     sing N N 390 
QBF CAL   H9     sing N N 391 
QBF CAL   H10    sing N N 392 
QBF CAM   H11    sing N N 393 
QBF CAM   H12    sing N N 394 
QBF CAN   H13    sing N N 395 
QBF CAN   H14    sing N N 396 
QBF OAI   H15    sing N N 397 
QBF OAO   H16    sing N N 398 
SER N     CA     sing N N 399 
SER N     H      sing N N 400 
SER N     H2     sing N N 401 
SER CA    C      sing N N 402 
SER CA    CB     sing N N 403 
SER CA    HA     sing N N 404 
SER C     O      doub N N 405 
SER C     OXT    sing N N 406 
SER CB    OG     sing N N 407 
SER CB    HB2    sing N N 408 
SER CB    HB3    sing N N 409 
SER OG    HG     sing N N 410 
SER OXT   HXT    sing N N 411 
THR N     CA     sing N N 412 
THR N     H      sing N N 413 
THR N     H2     sing N N 414 
THR CA    C      sing N N 415 
THR CA    CB     sing N N 416 
THR CA    HA     sing N N 417 
THR C     O      doub N N 418 
THR C     OXT    sing N N 419 
THR CB    OG1    sing N N 420 
THR CB    CG2    sing N N 421 
THR CB    HB     sing N N 422 
THR OG1   HG1    sing N N 423 
THR CG2   HG21   sing N N 424 
THR CG2   HG22   sing N N 425 
THR CG2   HG23   sing N N 426 
THR OXT   HXT    sing N N 427 
TRP N     CA     sing N N 428 
TRP N     H      sing N N 429 
TRP N     H2     sing N N 430 
TRP CA    C      sing N N 431 
TRP CA    CB     sing N N 432 
TRP CA    HA     sing N N 433 
TRP C     O      doub N N 434 
TRP C     OXT    sing N N 435 
TRP CB    CG     sing N N 436 
TRP CB    HB2    sing N N 437 
TRP CB    HB3    sing N N 438 
TRP CG    CD1    doub Y N 439 
TRP CG    CD2    sing Y N 440 
TRP CD1   NE1    sing Y N 441 
TRP CD1   HD1    sing N N 442 
TRP CD2   CE2    doub Y N 443 
TRP CD2   CE3    sing Y N 444 
TRP NE1   CE2    sing Y N 445 
TRP NE1   HE1    sing N N 446 
TRP CE2   CZ2    sing Y N 447 
TRP CE3   CZ3    doub Y N 448 
TRP CE3   HE3    sing N N 449 
TRP CZ2   CH2    doub Y N 450 
TRP CZ2   HZ2    sing N N 451 
TRP CZ3   CH2    sing Y N 452 
TRP CZ3   HZ3    sing N N 453 
TRP CH2   HH2    sing N N 454 
TRP OXT   HXT    sing N N 455 
TYR N     CA     sing N N 456 
TYR N     H      sing N N 457 
TYR N     H2     sing N N 458 
TYR CA    C      sing N N 459 
TYR CA    CB     sing N N 460 
TYR CA    HA     sing N N 461 
TYR C     O      doub N N 462 
TYR C     OXT    sing N N 463 
TYR CB    CG     sing N N 464 
TYR CB    HB2    sing N N 465 
TYR CB    HB3    sing N N 466 
TYR CG    CD1    doub Y N 467 
TYR CG    CD2    sing Y N 468 
TYR CD1   CE1    sing Y N 469 
TYR CD1   HD1    sing N N 470 
TYR CD2   CE2    doub Y N 471 
TYR CD2   HD2    sing N N 472 
TYR CE1   CZ     doub Y N 473 
TYR CE1   HE1    sing N N 474 
TYR CE2   CZ     sing Y N 475 
TYR CE2   HE2    sing N N 476 
TYR CZ    OH     sing N N 477 
TYR OH    HH     sing N N 478 
TYR OXT   HXT    sing N N 479 
VAL N     CA     sing N N 480 
VAL N     H      sing N N 481 
VAL N     H2     sing N N 482 
VAL CA    C      sing N N 483 
VAL CA    CB     sing N N 484 
VAL CA    HA     sing N N 485 
VAL C     O      doub N N 486 
VAL C     OXT    sing N N 487 
VAL CB    CG1    sing N N 488 
VAL CB    CG2    sing N N 489 
VAL CB    HB     sing N N 490 
VAL CG1   HG11   sing N N 491 
VAL CG1   HG12   sing N N 492 
VAL CG1   HG13   sing N N 493 
VAL CG2   HG21   sing N N 494 
VAL CG2   HG22   sing N N 495 
VAL CG2   HG23   sing N N 496 
VAL OXT   HXT    sing N N 497 
# 
_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             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GOV 
_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]   0.012049 
_atom_sites.fract_transf_matrix[1][2]   0.006957 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013913 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.003360 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . ARG A 1 3   ? 5.794   -6.529  -32.904 1.00 52.97  ? 3    ARG A N     1 
ATOM   2    C CA    . ARG A 1 3   ? 5.089   -5.233  -33.135 1.00 50.49  ? 3    ARG A CA    1 
ATOM   3    C C     . ARG A 1 3   ? 4.544   -4.687  -31.810 1.00 42.78  ? 3    ARG A C     1 
ATOM   4    O O     . ARG A 1 3   ? 3.769   -5.392  -31.148 1.00 38.03  ? 3    ARG A O     1 
ATOM   5    C CB    . ARG A 1 3   ? 3.942   -5.437  -34.115 1.00 53.91  ? 3    ARG A CB    1 
ATOM   6    C CG    . ARG A 1 3   ? 3.236   -4.145  -34.491 1.00 56.36  ? 3    ARG A CG    1 
ATOM   7    C CD    . ARG A 1 3   ? 1.738   -4.318  -34.361 1.00 58.38  ? 3    ARG A CD    1 
ATOM   8    N NE    . ARG A 1 3   ? 0.969   -3.437  -35.228 1.00 54.91  ? 3    ARG A NE    1 
ATOM   9    C CZ    . ARG A 1 3   ? -0.354  -3.500  -35.400 1.00 56.40  ? 3    ARG A CZ    1 
ATOM   10   N NH1   . ARG A 1 3   ? -1.070  -4.408  -34.761 1.00 53.63  ? 3    ARG A NH1   1 
ATOM   11   N NH2   . ARG A 1 3   ? -0.961  -2.643  -36.206 1.00 51.87  ? 3    ARG A NH2   1 
ATOM   12   N N     . THR A 1 4   ? 4.954   -3.476  -31.425 1.00 45.27  ? 4    THR A N     1 
ATOM   13   C CA    . THR A 1 4   ? 4.585   -2.856  -30.126 1.00 41.36  ? 4    THR A CA    1 
ATOM   14   C C     . THR A 1 4   ? 3.066   -2.655  -30.105 1.00 40.98  ? 4    THR A C     1 
ATOM   15   O O     . THR A 1 4   ? 2.535   -2.000  -31.020 1.00 48.55  ? 4    THR A O     1 
ATOM   16   C CB    . THR A 1 4   ? 5.399   -1.581  -29.881 1.00 41.89  ? 4    THR A CB    1 
ATOM   17   O OG1   . THR A 1 4   ? 6.762   -1.941  -30.082 1.00 39.37  ? 4    THR A OG1   1 
ATOM   18   C CG2   . THR A 1 4   ? 5.210   -0.999  -28.498 1.00 37.55  ? 4    THR A CG2   1 
ATOM   19   N N     . LEU A 1 5   ? 2.389   -3.283  -29.148 1.00 39.88  ? 5    LEU A N     1 
ATOM   20   C CA    . LEU A 1 5   ? 0.959   -3.052  -28.844 1.00 40.27  ? 5    LEU A CA    1 
ATOM   21   C C     . LEU A 1 5   ? 0.879   -2.289  -27.533 1.00 39.00  ? 5    LEU A C     1 
ATOM   22   O O     . LEU A 1 5   ? 1.632   -2.563  -26.614 1.00 37.68  ? 5    LEU A O     1 
ATOM   23   C CB    . LEU A 1 5   ? 0.216   -4.386  -28.694 1.00 38.85  ? 5    LEU A CB    1 
ATOM   24   C CG    . LEU A 1 5   ? 0.042   -5.219  -29.953 1.00 42.13  ? 5    LEU A CG    1 
ATOM   25   C CD1   . LEU A 1 5   ? -0.915  -6.372  -29.670 1.00 47.40  ? 5    LEU A CD1   1 
ATOM   26   C CD2   . LEU A 1 5   ? -0.462  -4.380  -31.111 1.00 42.78  ? 5    LEU A CD2   1 
ATOM   27   N N     . PRO A 1 6   ? -0.052  -1.330  -27.392 1.00 39.24  ? 6    PRO A N     1 
ATOM   28   C CA    . PRO A 1 6   ? -0.338  -0.758  -26.082 1.00 37.23  ? 6    PRO A CA    1 
ATOM   29   C C     . PRO A 1 6   ? -0.753  -1.838  -25.091 1.00 39.41  ? 6    PRO A C     1 
ATOM   30   O O     . PRO A 1 6   ? -1.412  -2.803  -25.471 1.00 36.29  ? 6    PRO A O     1 
ATOM   31   C CB    . PRO A 1 6   ? -1.523  0.171   -26.357 1.00 39.60  ? 6    PRO A CB    1 
ATOM   32   C CG    . PRO A 1 6   ? -1.396  0.522   -27.825 1.00 39.66  ? 6    PRO A CG    1 
ATOM   33   C CD    . PRO A 1 6   ? -0.817  -0.715  -28.482 1.00 39.61  ? 6    PRO A CD    1 
ATOM   34   N N     . PRO A 1 7   ? -0.419  -1.710  -23.791 1.00 41.17  ? 7    PRO A N     1 
ATOM   35   C CA    . PRO A 1 7   ? -0.911  -2.654  -22.789 1.00 41.87  ? 7    PRO A CA    1 
ATOM   36   C C     . PRO A 1 7   ? -2.441  -2.573  -22.672 1.00 43.24  ? 7    PRO A C     1 
ATOM   37   O O     . PRO A 1 7   ? -2.977  -1.471  -22.669 1.00 42.71  ? 7    PRO A O     1 
ATOM   38   C CB    . PRO A 1 7   ? -0.228  -2.206  -21.485 1.00 44.02  ? 7    PRO A CB    1 
ATOM   39   C CG    . PRO A 1 7   ? 0.935   -1.365  -21.942 1.00 43.51  ? 7    PRO A CG    1 
ATOM   40   C CD    . PRO A 1 7   ? 0.474   -0.698  -23.219 1.00 42.60  ? 7    PRO A CD    1 
ATOM   41   N N     . GLY A 1 8   ? -3.101  -3.731  -22.630 1.00 40.79  ? 8    GLY A N     1 
ATOM   42   C CA    . GLY A 1 8   ? -4.561  -3.831  -22.471 1.00 44.47  ? 8    GLY A CA    1 
ATOM   43   C C     . GLY A 1 8   ? -5.333  -3.702  -23.784 1.00 46.58  ? 8    GLY A C     1 
ATOM   44   O O     . GLY A 1 8   ? -6.579  -3.701  -23.714 1.00 52.75  ? 8    GLY A O     1 
ATOM   45   N N     . VAL A 1 9   ? -4.662  -3.598  -24.939 1.00 42.15  ? 9    VAL A N     1 
ATOM   46   C CA    . VAL A 1 9   ? -5.362  -3.440  -26.251 1.00 38.81  ? 9    VAL A CA    1 
ATOM   47   C C     . VAL A 1 9   ? -5.033  -4.643  -27.148 1.00 35.29  ? 9    VAL A C     1 
ATOM   48   O O     . VAL A 1 9   ? -3.855  -4.929  -27.350 1.00 31.90  ? 9    VAL A O     1 
ATOM   49   C CB    . VAL A 1 9   ? -5.066  -2.077  -26.922 1.00 39.60  ? 9    VAL A CB    1 
ATOM   50   C CG1   . VAL A 1 9   ? -5.046  -0.935  -25.912 1.00 38.21  ? 9    VAL A CG1   1 
ATOM   51   C CG2   . VAL A 1 9   ? -3.787  -2.073  -27.735 1.00 45.30  ? 9    VAL A CG2   1 
ATOM   52   N N     . SER A 1 10  ? -6.054  -5.303  -27.696 1.00 36.23  ? 10   SER A N     1 
ATOM   53   C CA    . SER A 1 10  ? -5.896  -6.414  -28.670 1.00 41.26  ? 10   SER A CA    1 
ATOM   54   C C     . SER A 1 10  ? -5.225  -5.891  -29.939 1.00 39.79  ? 10   SER A C     1 
ATOM   55   O O     . SER A 1 10  ? -5.381  -4.716  -30.236 1.00 34.91  ? 10   SER A O     1 
ATOM   56   C CB    . SER A 1 10  ? -7.214  -7.045  -29.004 1.00 41.53  ? 10   SER A CB    1 
ATOM   57   O OG    . SER A 1 10  ? -8.137  -6.064  -29.447 1.00 41.76  ? 10   SER A OG    1 
ATOM   58   N N     . ASP A 1 11  ? -4.551  -6.760  -30.689 1.00 40.94  ? 11   ASP A N     1 
ATOM   59   C CA    . ASP A 1 11  ? -4.025  -6.426  -32.035 1.00 45.21  ? 11   ASP A CA    1 
ATOM   60   C C     . ASP A 1 11  ? -5.168  -5.874  -32.919 1.00 41.46  ? 11   ASP A C     1 
ATOM   61   O O     . ASP A 1 11  ? -4.922  -4.910  -33.663 1.00 34.77  ? 11   ASP A O     1 
ATOM   62   C CB    . ASP A 1 11  ? -3.331  -7.647  -32.636 1.00 48.33  ? 11   ASP A CB    1 
ATOM   63   C CG    . ASP A 1 11  ? -2.859  -7.422  -34.053 1.00 51.99  ? 11   ASP A CG    1 
ATOM   64   O OD1   . ASP A 1 11  ? -1.718  -6.947  -34.204 1.00 57.51  ? 11   ASP A OD1   1 
ATOM   65   O OD2   . ASP A 1 11  ? -3.652  -7.701  -34.991 1.00 53.52  ? 11   ASP A OD2   1 
ATOM   66   N N     . GLU A 1 12  ? -6.366  -6.462  -32.848 1.00 41.04  ? 12   GLU A N     1 
ATOM   67   C CA    . GLU A 1 12  ? -7.540  -6.081  -33.686 1.00 45.66  ? 12   GLU A CA    1 
ATOM   68   C C     . GLU A 1 12  ? -7.936  -4.642  -33.341 1.00 42.75  ? 12   GLU A C     1 
ATOM   69   O O     . GLU A 1 12  ? -8.100  -3.826  -34.276 1.00 38.36  ? 12   GLU A O     1 
ATOM   70   C CB    . GLU A 1 12  ? -8.720  -7.038  -33.471 1.00 50.21  ? 12   GLU A CB    1 
ATOM   71   C CG    . GLU A 1 12  ? -8.480  -8.458  -33.968 1.00 63.55  ? 12   GLU A CG    1 
ATOM   72   C CD    . GLU A 1 12  ? -9.562  -9.516  -33.744 1.00 78.35  ? 12   GLU A CD    1 
ATOM   73   O OE1   . GLU A 1 12  ? -10.550 -9.265  -32.993 1.00 77.44  ? 12   GLU A OE1   1 
ATOM   74   O OE2   . GLU A 1 12  ? -9.419  -10.612 -34.339 1.00 86.96  ? 12   GLU A OE2   1 
ATOM   75   N N     . ASP A 1 13  ? -8.099  -4.348  -32.046 1.00 39.16  ? 13   ASP A N     1 
ATOM   76   C CA    . ASP A 1 13  ? -8.519  -3.003  -31.570 1.00 37.57  ? 13   ASP A CA    1 
ATOM   77   C C     . ASP A 1 13  ? -7.444  -1.979  -31.915 1.00 34.31  ? 13   ASP A C     1 
ATOM   78   O O     . ASP A 1 13  ? -7.815  -0.865  -32.281 1.00 34.02  ? 13   ASP A O     1 
ATOM   79   C CB    . ASP A 1 13  ? -8.882  -2.996  -30.093 1.00 39.12  ? 13   ASP A CB    1 
ATOM   80   C CG    . ASP A 1 13  ? -10.256 -3.580  -29.844 1.00 41.14  ? 13   ASP A CG    1 
ATOM   81   O OD1   . ASP A 1 13  ? -11.001 -3.777  -30.830 1.00 40.58  ? 13   ASP A OD1   1 
ATOM   82   O OD2   . ASP A 1 13  ? -10.575 -3.830  -28.676 1.00 42.23  ? 13   ASP A OD2   1 
ATOM   83   N N     . PHE A 1 14  ? -6.168  -2.351  -31.849 1.00 34.39  ? 14   PHE A N     1 
ATOM   84   C CA    . PHE A 1 14  ? -5.060  -1.445  -32.233 1.00 32.17  ? 14   PHE A CA    1 
ATOM   85   C C     . PHE A 1 14  ? -5.159  -1.143  -33.743 1.00 34.42  ? 14   PHE A C     1 
ATOM   86   O O     . PHE A 1 14  ? -4.966  0.010   -34.138 1.00 28.89  ? 14   PHE A O     1 
ATOM   87   C CB    . PHE A 1 14  ? -3.694  -1.996  -31.819 1.00 30.17  ? 14   PHE A CB    1 
ATOM   88   C CG    . PHE A 1 14  ? -2.604  -0.968  -31.968 1.00 32.53  ? 14   PHE A CG    1 
ATOM   89   C CD1   . PHE A 1 14  ? -2.699  0.253   -31.323 1.00 34.48  ? 14   PHE A CD1   1 
ATOM   90   C CD2   . PHE A 1 14  ? -1.530  -1.182  -32.802 1.00 35.67  ? 14   PHE A CD2   1 
ATOM   91   C CE1   . PHE A 1 14  ? -1.709  1.204   -31.464 1.00 35.92  ? 14   PHE A CE1   1 
ATOM   92   C CE2   . PHE A 1 14  ? -0.548  -0.221  -32.952 1.00 39.82  ? 14   PHE A CE2   1 
ATOM   93   C CZ    . PHE A 1 14  ? -0.640  0.974   -32.288 1.00 34.45  ? 14   PHE A CZ    1 
ATOM   94   N N     . THR A 1 15  ? -5.440  -2.158  -34.563 1.00 35.97  ? 15   THR A N     1 
ATOM   95   C CA    . THR A 1 15  ? -5.562  -2.025  -36.036 1.00 33.33  ? 15   THR A CA    1 
ATOM   96   C C     . THR A 1 15  ? -6.695  -1.046  -36.360 1.00 33.83  ? 15   THR A C     1 
ATOM   97   O O     . THR A 1 15  ? -6.483  -0.148  -37.234 1.00 30.34  ? 15   THR A O     1 
ATOM   98   C CB    . THR A 1 15  ? -5.748  -3.397  -36.706 1.00 36.69  ? 15   THR A CB    1 
ATOM   99   O OG1   . THR A 1 15  ? -4.503  -4.090  -36.573 1.00 33.33  ? 15   THR A OG1   1 
ATOM   100  C CG2   . THR A 1 15  ? -6.122  -3.305  -38.177 1.00 35.49  ? 15   THR A CG2   1 
ATOM   101  N N     . SER A 1 16  ? -7.829  -1.200  -35.668 1.00 32.53  ? 16   SER A N     1 
ATOM   102  C CA    . SER A 1 16  ? -9.054  -0.380  -35.840 1.00 32.69  ? 16   SER A CA    1 
ATOM   103  C C     . SER A 1 16  ? -8.763  1.069   -35.458 1.00 31.34  ? 16   SER A C     1 
ATOM   104  O O     . SER A 1 16  ? -9.144  1.950   -36.220 1.00 29.59  ? 16   SER A O     1 
ATOM   105  C CB    . SER A 1 16  ? -10.208 -0.951  -35.043 1.00 32.62  ? 16   SER A CB    1 
ATOM   106  O OG    . SER A 1 16  ? -10.580 -2.204  -35.574 1.00 31.28  ? 16   SER A OG    1 
ATOM   107  N N     . ALA A 1 17  ? -8.072  1.283   -34.337 1.00 30.00  ? 17   ALA A N     1 
ATOM   108  C CA    . ALA A 1 17  ? -7.699  2.613   -33.810 1.00 28.39  ? 17   ALA A CA    1 
ATOM   109  C C     . ALA A 1 17  ? -6.796  3.346   -34.804 1.00 28.26  ? 17   ALA A C     1 
ATOM   110  O O     . ALA A 1 17  ? -7.054  4.540   -35.081 1.00 28.32  ? 17   ALA A O     1 
ATOM   111  C CB    . ALA A 1 17  ? -7.035  2.438   -32.459 1.00 31.39  ? 17   ALA A CB    1 
ATOM   112  N N     . LEU A 1 18  ? -5.760  2.670   -35.307 1.00 27.70  ? 18   LEU A N     1 
ATOM   113  C CA    . LEU A 1 18  ? -4.811  3.252   -36.285 1.00 28.77  ? 18   LEU A CA    1 
ATOM   114  C C     . LEU A 1 18  ? -5.578  3.718   -37.530 1.00 29.66  ? 18   LEU A C     1 
ATOM   115  O O     . LEU A 1 18  ? -5.282  4.819   -38.002 1.00 28.87  ? 18   LEU A O     1 
ATOM   116  C CB    . LEU A 1 18  ? -3.722  2.237   -36.656 1.00 31.10  ? 18   LEU A CB    1 
ATOM   117  C CG    . LEU A 1 18  ? -2.704  1.882   -35.567 1.00 34.53  ? 18   LEU A CG    1 
ATOM   118  C CD1   . LEU A 1 18  ? -1.714  0.838   -36.077 1.00 36.36  ? 18   LEU A CD1   1 
ATOM   119  C CD2   . LEU A 1 18  ? -1.950  3.097   -35.036 1.00 34.50  ? 18   LEU A CD2   1 
ATOM   120  N N     . THR A 1 19  ? -6.485  2.896   -38.077 1.00 28.35  ? 19   THR A N     1 
ATOM   121  C CA    . THR A 1 19  ? -7.355  3.266   -39.232 1.00 29.79  ? 19   THR A CA    1 
ATOM   122  C C     . THR A 1 19  ? -8.155  4.524   -38.869 1.00 29.01  ? 19   THR A C     1 
ATOM   123  O O     . THR A 1 19  ? -8.171  5.470   -39.653 1.00 29.13  ? 19   THR A O     1 
ATOM   124  C CB    . THR A 1 19  ? -8.264  2.081   -39.610 1.00 28.81  ? 19   THR A CB    1 
ATOM   125  O OG1   . THR A 1 19  ? -7.400  1.026   -40.057 1.00 26.69  ? 19   THR A OG1   1 
ATOM   126  C CG2   . THR A 1 19  ? -9.304  2.401   -40.665 1.00 28.61  ? 19   THR A CG2   1 
ATOM   127  N N     . ALA A 1 20  ? -8.837  4.507   -37.729 1.00 27.85  ? 20   ALA A N     1 
ATOM   128  C CA    . ALA A 1 20  ? -9.632  5.646   -37.224 1.00 30.33  ? 20   ALA A CA    1 
ATOM   129  C C     . ALA A 1 20  ? -8.726  6.877   -37.048 1.00 27.78  ? 20   ALA A C     1 
ATOM   130  O O     . ALA A 1 20  ? -9.183  7.974   -37.403 1.00 29.32  ? 20   ALA A O     1 
ATOM   131  C CB    . ALA A 1 20  ? -10.340 5.253   -35.946 1.00 26.91  ? 20   ALA A CB    1 
ATOM   132  N N     . PHE A 1 21  ? -7.490  6.725   -36.540 1.00 28.09  ? 21   PHE A N     1 
ATOM   133  C CA    . PHE A 1 21  ? -6.572  7.888   -36.360 1.00 26.65  ? 21   PHE A CA    1 
ATOM   134  C C     . PHE A 1 21  ? -6.184  8.404   -37.739 1.00 26.03  ? 21   PHE A C     1 
ATOM   135  O O     . PHE A 1 21  ? -6.207  9.583   -37.911 1.00 23.53  ? 21   PHE A O     1 
ATOM   136  C CB    . PHE A 1 21  ? -5.306  7.573   -35.561 1.00 25.60  ? 21   PHE A CB    1 
ATOM   137  C CG    . PHE A 1 21  ? -5.486  7.222   -34.105 1.00 24.18  ? 21   PHE A CG    1 
ATOM   138  C CD1   . PHE A 1 21  ? -6.357  7.926   -33.301 1.00 23.31  ? 21   PHE A CD1   1 
ATOM   139  C CD2   . PHE A 1 21  ? -4.698  6.241   -33.522 1.00 25.36  ? 21   PHE A CD2   1 
ATOM   140  C CE1   . PHE A 1 21  ? -6.469  7.640   -31.949 1.00 24.37  ? 21   PHE A CE1   1 
ATOM   141  C CE2   . PHE A 1 21  ? -4.816  5.948   -32.168 1.00 26.03  ? 21   PHE A CE2   1 
ATOM   142  C CZ    . PHE A 1 21  ? -5.708  6.644   -31.387 1.00 26.01  ? 21   PHE A CZ    1 
ATOM   143  N N     . ARG A 1 22  ? -5.867  7.526   -38.691 1.00 27.59  ? 22   ARG A N     1 
ATOM   144  C CA    . ARG A 1 22  ? -5.562  7.963   -40.081 1.00 30.05  ? 22   ARG A CA    1 
ATOM   145  C C     . ARG A 1 22  ? -6.760  8.726   -40.635 1.00 26.87  ? 22   ARG A C     1 
ATOM   146  O O     . ARG A 1 22  ? -6.541  9.698   -41.347 1.00 28.22  ? 22   ARG A O     1 
ATOM   147  C CB    . ARG A 1 22  ? -5.263  6.801   -41.030 1.00 30.18  ? 22   ARG A CB    1 
ATOM   148  C CG    . ARG A 1 22  ? -3.953  6.096   -40.732 1.00 32.56  ? 22   ARG A CG    1 
ATOM   149  C CD    . ARG A 1 22  ? -3.681  4.925   -41.670 1.00 34.42  ? 22   ARG A CD    1 
ATOM   150  N NE    . ARG A 1 22  ? -2.630  4.155   -41.036 1.00 34.94  ? 22   ARG A NE    1 
ATOM   151  C CZ    . ARG A 1 22  ? -2.790  2.973   -40.451 1.00 34.35  ? 22   ARG A CZ    1 
ATOM   152  N NH1   . ARG A 1 22  ? -3.957  2.350   -40.483 1.00 33.23  ? 22   ARG A NH1   1 
ATOM   153  N NH2   . ARG A 1 22  ? -1.755  2.407   -39.852 1.00 33.77  ? 22   ARG A NH2   1 
ATOM   154  N N     . ASP A 1 23  ? -7.964  8.261   -40.329 1.00 26.07  ? 23   ASP A N     1 
ATOM   155  C CA    . ASP A 1 23  ? -9.233  8.827   -40.857 1.00 27.59  ? 23   ASP A CA    1 
ATOM   156  C C     . ASP A 1 23  ? -9.334  10.297  -40.461 1.00 26.92  ? 23   ASP A C     1 
ATOM   157  O O     . ASP A 1 23  ? -9.883  11.075  -41.220 1.00 26.75  ? 23   ASP A O     1 
ATOM   158  C CB    . ASP A 1 23  ? -10.418 7.985   -40.364 1.00 27.43  ? 23   ASP A CB    1 
ATOM   159  C CG    . ASP A 1 23  ? -10.546 6.670   -41.109 1.00 28.48  ? 23   ASP A CG    1 
ATOM   160  O OD1   . ASP A 1 23  ? -9.742  6.464   -42.085 1.00 26.64  ? 23   ASP A OD1   1 
ATOM   161  O OD2   . ASP A 1 23  ? -11.403 5.839   -40.679 1.00 26.94  ? 23   ASP A OD2   1 
ATOM   162  N N     . VAL A 1 24  ? -8.778  10.656  -39.312 1.00 27.28  ? 24   VAL A N     1 
ATOM   163  C CA    . VAL A 1 24  ? -8.801  12.034  -38.770 1.00 30.84  ? 24   VAL A CA    1 
ATOM   164  C C     . VAL A 1 24  ? -7.619  12.878  -39.262 1.00 32.29  ? 24   VAL A C     1 
ATOM   165  O O     . VAL A 1 24  ? -7.910  13.991  -39.748 1.00 34.85  ? 24   VAL A O     1 
ATOM   166  C CB    . VAL A 1 24  ? -8.864  12.008  -37.233 1.00 31.29  ? 24   VAL A CB    1 
ATOM   167  C CG1   . VAL A 1 24  ? -8.670  13.408  -36.674 1.00 30.92  ? 24   VAL A CG1   1 
ATOM   168  C CG2   . VAL A 1 24  ? -10.181 11.422  -36.803 1.00 29.60  ? 24   VAL A CG2   1 
ATOM   169  N N     . VAL A 1 25  ? -6.361  12.425  -39.101 1.00 30.06  ? 25   VAL A N     1 
ATOM   170  C CA    . VAL A 1 25  ? -5.150  13.306  -39.206 1.00 28.92  ? 25   VAL A CA    1 
ATOM   171  C C     . VAL A 1 25  ? -4.505  13.157  -40.581 1.00 29.08  ? 25   VAL A C     1 
ATOM   172  O O     . VAL A 1 25  ? -3.782  14.055  -40.993 1.00 27.47  ? 25   VAL A O     1 
ATOM   173  C CB    . VAL A 1 25  ? -4.114  13.040  -38.089 1.00 28.71  ? 25   VAL A CB    1 
ATOM   174  C CG1   . VAL A 1 25  ? -4.719  13.282  -36.720 1.00 29.82  ? 25   VAL A CG1   1 
ATOM   175  C CG2   . VAL A 1 25  ? -3.493  11.657  -38.161 1.00 30.77  ? 25   VAL A CG2   1 
ATOM   176  N N     . GLY A 1 26  ? -4.759  12.050  -41.261 1.00 29.55  ? 26   GLY A N     1 
ATOM   177  C CA    . GLY A 1 26  ? -4.048  11.714  -42.499 1.00 31.65  ? 26   GLY A CA    1 
ATOM   178  C C     . GLY A 1 26  ? -3.003  10.652  -42.266 1.00 36.05  ? 26   GLY A C     1 
ATOM   179  O O     . GLY A 1 26  ? -2.277  10.706  -41.230 1.00 34.28  ? 26   GLY A O     1 
ATOM   180  N N     . ASP A 1 27  ? -2.921  9.716   -43.210 1.00 31.61  ? 27   ASP A N     1 
ATOM   181  C CA    . ASP A 1 27  ? -2.003  8.561   -43.185 1.00 33.85  ? 27   ASP A CA    1 
ATOM   182  C C     . ASP A 1 27  ? -0.577  9.046   -42.841 1.00 30.96  ? 27   ASP A C     1 
ATOM   183  O O     . ASP A 1 27  ? 0.110   8.385   -42.030 1.00 37.82  ? 27   ASP A O     1 
ATOM   184  C CB    . ASP A 1 27  ? -2.136  7.849   -44.537 1.00 42.97  ? 27   ASP A CB    1 
ATOM   185  C CG    . ASP A 1 27  ? -1.031  6.868   -44.831 1.00 51.75  ? 27   ASP A CG    1 
ATOM   186  O OD1   . ASP A 1 27  ? -1.106  5.721   -44.312 1.00 62.26  ? 27   ASP A OD1   1 
ATOM   187  O OD2   . ASP A 1 27  ? -0.093  7.270   -45.553 1.00 59.43  ? 27   ASP A OD2   1 
ATOM   188  N N     . GLU A 1 28  ? -0.149  10.165  -43.411 1.00 29.76  ? 28   GLU A N     1 
ATOM   189  C CA    . GLU A 1 28  ? 1.205   10.761  -43.233 1.00 31.11  ? 28   GLU A CA    1 
ATOM   190  C C     . GLU A 1 28  ? 1.486   11.045  -41.743 1.00 30.16  ? 28   GLU A C     1 
ATOM   191  O O     . GLU A 1 28  ? 2.644   10.929  -41.332 1.00 28.05  ? 28   GLU A O     1 
ATOM   192  C CB    . GLU A 1 28  ? 1.269   12.032  -44.062 1.00 33.78  ? 28   GLU A CB    1 
ATOM   193  C CG    . GLU A 1 28  ? 2.362   12.986  -43.660 1.00 40.73  ? 28   GLU A CG    1 
ATOM   194  C CD    . GLU A 1 28  ? 2.492   14.202  -44.565 1.00 42.18  ? 28   GLU A CD    1 
ATOM   195  O OE1   . GLU A 1 28  ? 1.472   14.667  -45.130 1.00 41.45  ? 28   GLU A OE1   1 
ATOM   196  O OE2   . GLU A 1 28  ? 3.618   14.705  -44.670 1.00 53.58  ? 28   GLU A OE2   1 
ATOM   197  N N     . PHE A 1 29  ? 0.448   11.338  -40.969 1.00 29.13  ? 29   PHE A N     1 
ATOM   198  C CA    . PHE A 1 29  ? 0.527   11.827  -39.571 1.00 29.91  ? 29   PHE A CA    1 
ATOM   199  C C     . PHE A 1 29  ? 0.123   10.732  -38.568 1.00 32.59  ? 29   PHE A C     1 
ATOM   200  O O     . PHE A 1 29  ? -0.133  11.045  -37.344 1.00 28.14  ? 29   PHE A O     1 
ATOM   201  C CB    . PHE A 1 29  ? -0.324  13.087  -39.477 1.00 30.42  ? 29   PHE A CB    1 
ATOM   202  C CG    . PHE A 1 29  ? 0.214   14.222  -40.290 1.00 29.04  ? 29   PHE A CG    1 
ATOM   203  C CD1   . PHE A 1 29  ? 1.465   14.735  -40.012 1.00 31.45  ? 29   PHE A CD1   1 
ATOM   204  C CD2   . PHE A 1 29  ? -0.509  14.748  -41.346 1.00 30.33  ? 29   PHE A CD2   1 
ATOM   205  C CE1   . PHE A 1 29  ? 1.971   15.781  -40.757 1.00 33.86  ? 29   PHE A CE1   1 
ATOM   206  C CE2   . PHE A 1 29  ? -0.008  15.805  -42.083 1.00 32.42  ? 29   PHE A CE2   1 
ATOM   207  C CZ    . PHE A 1 29  ? 1.226   16.326  -41.781 1.00 33.89  ? 29   PHE A CZ    1 
ATOM   208  N N     . VAL A 1 30  ? 0.115   9.476   -39.037 1.00 31.17  ? 30   VAL A N     1 
ATOM   209  C CA    . VAL A 1 30  ? 0.114   8.271   -38.165 1.00 31.15  ? 30   VAL A CA    1 
ATOM   210  C C     . VAL A 1 30  ? 1.351   7.417   -38.503 1.00 33.88  ? 30   VAL A C     1 
ATOM   211  O O     . VAL A 1 30  ? 1.425   6.841   -39.603 1.00 30.90  ? 30   VAL A O     1 
ATOM   212  C CB    . VAL A 1 30  ? -1.192  7.483   -38.257 1.00 29.89  ? 30   VAL A CB    1 
ATOM   213  C CG1   . VAL A 1 30  ? -1.163  6.311   -37.289 1.00 31.80  ? 30   VAL A CG1   1 
ATOM   214  C CG2   . VAL A 1 30  ? -2.406  8.355   -38.016 1.00 29.41  ? 30   VAL A CG2   1 
ATOM   215  N N     . ARG A 1 31  ? 2.310   7.414   -37.583 1.00 31.62  ? 31   ARG A N     1 
ATOM   216  C CA    . ARG A 1 31  ? 3.586   6.765   -37.800 1.00 34.27  ? 31   ARG A CA    1 
ATOM   217  C C     . ARG A 1 31  ? 3.758   5.521   -36.972 1.00 32.85  ? 31   ARG A C     1 
ATOM   218  O O     . ARG A 1 31  ? 3.649   5.573   -35.770 1.00 32.32  ? 31   ARG A O     1 
ATOM   219  C CB    . ARG A 1 31  ? 4.661   7.773   -37.457 1.00 35.06  ? 31   ARG A CB    1 
ATOM   220  C CG    . ARG A 1 31  ? 5.141   8.570   -38.635 1.00 44.01  ? 31   ARG A CG    1 
ATOM   221  C CD    . ARG A 1 31  ? 4.476   9.905   -38.780 1.00 49.72  ? 31   ARG A CD    1 
ATOM   222  N NE    . ARG A 1 31  ? 5.217   10.778  -39.680 1.00 51.04  ? 31   ARG A NE    1 
ATOM   223  C CZ    . ARG A 1 31  ? 5.326   12.084  -39.499 1.00 51.37  ? 31   ARG A CZ    1 
ATOM   224  N NH1   . ARG A 1 31  ? 4.748   12.640  -38.458 1.00 47.48  ? 31   ARG A NH1   1 
ATOM   225  N NH2   . ARG A 1 31  ? 6.006   12.831  -40.351 1.00 54.24  ? 31   ARG A NH2   1 
ATOM   226  N N     . THR A 1 32  ? 4.040   4.413   -37.619 1.00 29.55  ? 32   THR A N     1 
ATOM   227  C CA    . THR A 1 32  ? 4.148   3.144   -36.943 1.00 32.12  ? 32   THR A CA    1 
ATOM   228  C C     . THR A 1 32  ? 5.425   2.423   -37.320 1.00 35.00  ? 32   THR A C     1 
ATOM   229  O O     . THR A 1 32  ? 5.737   1.391   -36.766 1.00 34.12  ? 32   THR A O     1 
ATOM   230  C CB    . THR A 1 32  ? 3.007   2.232   -37.387 1.00 36.71  ? 32   THR A CB    1 
ATOM   231  O OG1   . THR A 1 32  ? 2.888   2.272   -38.810 1.00 33.16  ? 32   THR A OG1   1 
ATOM   232  C CG2   . THR A 1 32  ? 1.697   2.642   -36.740 1.00 37.69  ? 32   THR A CG2   1 
ATOM   233  N N     . ASP A 1 33  ? 6.153   2.968   -38.277 1.00 37.52  ? 33   ASP A N     1 
ATOM   234  C CA    . ASP A 1 33  ? 7.369   2.342   -38.734 1.00 41.76  ? 33   ASP A CA    1 
ATOM   235  C C     . ASP A 1 33  ? 8.464   2.420   -37.701 1.00 43.38  ? 33   ASP A C     1 
ATOM   236  O O     . ASP A 1 33  ? 8.624   3.434   -37.066 1.00 41.36  ? 33   ASP A O     1 
ATOM   237  C CB    . ASP A 1 33  ? 7.823   2.953   -40.034 1.00 42.76  ? 33   ASP A CB    1 
ATOM   238  C CG    . ASP A 1 33  ? 6.868   2.693   -41.167 1.00 58.91  ? 33   ASP A CG    1 
ATOM   239  O OD1   . ASP A 1 33  ? 6.290   1.589   -41.229 1.00 54.03  ? 33   ASP A OD1   1 
ATOM   240  O OD2   . ASP A 1 33  ? 6.695   3.598   -42.007 1.00 72.71  ? 33   ASP A OD2   1 
ATOM   241  N N     . GLU A 1 34  ? 9.222   1.344   -37.546 1.00 48.14  ? 34   GLU A N     1 
ATOM   242  C CA    . GLU A 1 34  ? 10.284  1.279   -36.548 1.00 49.31  ? 34   GLU A CA    1 
ATOM   243  C C     . GLU A 1 34  ? 11.260  2.414   -36.613 1.00 48.50  ? 34   GLU A C     1 
ATOM   244  O O     . GLU A 1 34  ? 11.715  2.887   -35.598 1.00 46.16  ? 34   GLU A O     1 
ATOM   245  C CB    . GLU A 1 34  ? 11.034  -0.039  -36.655 1.00 55.07  ? 34   GLU A CB    1 
ATOM   246  C CG    . GLU A 1 34  ? 11.332  -0.511  -38.073 1.00 63.50  ? 34   GLU A CG    1 
ATOM   247  C CD    . GLU A 1 34  ? 12.620  -1.314  -38.163 1.00 70.53  ? 34   GLU A CD    1 
ATOM   248  O OE1   . GLU A 1 34  ? 13.224  -1.584  -37.105 1.00 74.15  ? 34   GLU A OE1   1 
ATOM   249  O OE2   . GLU A 1 34  ? 13.030  -1.678  -39.286 1.00 66.06  ? 34   GLU A OE2   1 
ATOM   250  N N     . ALA A 1 35  ? 11.572  2.853   -37.809 1.00 44.36  ? 35   ALA A N     1 
ATOM   251  C CA    . ALA A 1 35  ? 12.481  3.940   -37.966 1.00 49.21  ? 35   ALA A CA    1 
ATOM   252  C C     . ALA A 1 35  ? 11.932  5.229   -37.433 1.00 48.50  ? 35   ALA A C     1 
ATOM   253  O O     . ALA A 1 35  ? 12.670  6.037   -36.894 1.00 47.45  ? 35   ALA A O     1 
ATOM   254  C CB    . ALA A 1 35  ? 12.795  4.100   -39.414 1.00 55.56  ? 35   ALA A CB    1 
ATOM   255  N N     . GLU A 1 36  ? 10.637  5.438   -37.606 1.00 50.61  ? 36   GLU A N     1 
ATOM   256  C CA    . GLU A 1 36  ? 10.029  6.727   -37.167 1.00 48.20  ? 36   GLU A CA    1 
ATOM   257  C C     . GLU A 1 36  ? 9.873   6.673   -35.638 1.00 42.89  ? 36   GLU A C     1 
ATOM   258  O O     . GLU A 1 36  ? 10.083  7.703   -34.988 1.00 44.68  ? 36   GLU A O     1 
ATOM   259  C CB    . GLU A 1 36  ? 8.757   7.025   -37.983 1.00 54.12  ? 36   GLU A CB    1 
ATOM   260  C CG    . GLU A 1 36  ? 9.077   7.533   -39.398 1.00 60.59  ? 36   GLU A CG    1 
ATOM   261  C CD    . GLU A 1 36  ? 7.952   7.839   -40.394 1.00 68.73  ? 36   GLU A CD    1 
ATOM   262  O OE1   . GLU A 1 36  ? 8.026   8.915   -41.049 1.00 67.08  ? 36   GLU A OE1   1 
ATOM   263  O OE2   . GLU A 1 36  ? 7.020   7.006   -40.557 1.00 61.40  ? 36   GLU A OE2   1 
ATOM   264  N N     . LEU A 1 37  ? 9.564   5.503   -35.080 1.00 39.62  ? 37   LEU A N     1 
ATOM   265  C CA    . LEU A 1 37  ? 9.391   5.292   -33.615 1.00 41.36  ? 37   LEU A CA    1 
ATOM   266  C C     . LEU A 1 37  ? 10.723  5.466   -32.858 1.00 45.61  ? 37   LEU A C     1 
ATOM   267  O O     . LEU A 1 37  ? 10.712  6.022   -31.732 1.00 43.48  ? 37   LEU A O     1 
ATOM   268  C CB    . LEU A 1 37  ? 8.818   3.888   -33.392 1.00 39.71  ? 37   LEU A CB    1 
ATOM   269  C CG    . LEU A 1 37  ? 7.408   3.655   -33.933 1.00 39.42  ? 37   LEU A CG    1 
ATOM   270  C CD1   . LEU A 1 37  ? 6.903   2.271   -33.553 1.00 40.81  ? 37   LEU A CD1   1 
ATOM   271  C CD2   . LEU A 1 37  ? 6.456   4.736   -33.461 1.00 40.01  ? 37   LEU A CD2   1 
ATOM   272  N N     . ALA A 1 38  ? 11.834  4.993   -33.431 1.00 49.15  ? 38   ALA A N     1 
ATOM   273  C CA    . ALA A 1 38  ? 13.183  5.024   -32.811 1.00 49.08  ? 38   ALA A CA    1 
ATOM   274  C C     . ALA A 1 38  ? 13.524  6.482   -32.511 1.00 45.78  ? 38   ALA A C     1 
ATOM   275  O O     . ALA A 1 38  ? 14.229  6.749   -31.546 1.00 41.19  ? 38   ALA A O     1 
ATOM   276  C CB    . ALA A 1 38  ? 14.211  4.407   -33.734 1.00 48.85  ? 38   ALA A CB    1 
ATOM   277  N N     . ARG A 1 39  ? 12.964  7.391   -33.302 1.00 44.00  ? 39   ARG A N     1 
ATOM   278  C CA    . ARG A 1 39  ? 13.214  8.849   -33.201 1.00 45.79  ? 39   ARG A CA    1 
ATOM   279  C C     . ARG A 1 39  ? 12.541  9.426   -31.937 1.00 41.51  ? 39   ARG A C     1 
ATOM   280  O O     . ARG A 1 39  ? 12.853  10.581  -31.628 1.00 38.14  ? 39   ARG A O     1 
ATOM   281  C CB    . ARG A 1 39  ? 12.725  9.510   -34.491 1.00 50.49  ? 39   ARG A CB    1 
ATOM   282  C CG    . ARG A 1 39  ? 13.500  10.760  -34.874 1.00 59.10  ? 39   ARG A CG    1 
ATOM   283  C CD    . ARG A 1 39  ? 13.253  11.211  -36.315 1.00 62.98  ? 39   ARG A CD    1 
ATOM   284  N NE    . ARG A 1 39  ? 11.900  11.698  -36.574 1.00 64.54  ? 39   ARG A NE    1 
ATOM   285  C CZ    . ARG A 1 39  ? 11.351  12.807  -36.061 1.00 60.25  ? 39   ARG A CZ    1 
ATOM   286  N NH1   . ARG A 1 39  ? 12.014  13.582  -35.218 1.00 61.88  ? 39   ARG A NH1   1 
ATOM   287  N NH2   . ARG A 1 39  ? 10.116  13.136  -36.390 1.00 59.52  ? 39   ARG A NH2   1 
ATOM   288  N N     . PHE A 1 40  ? 11.664  8.655   -31.264 1.00 40.69  ? 40   PHE A N     1 
ATOM   289  C CA    . PHE A 1 40  ? 10.904  9.017   -30.027 1.00 37.85  ? 40   PHE A CA    1 
ATOM   290  C C     . PHE A 1 40  ? 11.390  8.170   -28.853 1.00 38.37  ? 40   PHE A C     1 
ATOM   291  O O     . PHE A 1 40  ? 10.753  8.198   -27.778 1.00 36.84  ? 40   PHE A O     1 
ATOM   292  C CB    . PHE A 1 40  ? 9.393   8.841   -30.213 1.00 34.09  ? 40   PHE A CB    1 
ATOM   293  C CG    . PHE A 1 40  ? 8.813   9.838   -31.185 1.00 33.88  ? 40   PHE A CG    1 
ATOM   294  C CD1   . PHE A 1 40  ? 9.010   9.698   -32.547 1.00 33.44  ? 40   PHE A CD1   1 
ATOM   295  C CD2   . PHE A 1 40  ? 8.153   10.970  -30.734 1.00 37.36  ? 40   PHE A CD2   1 
ATOM   296  C CE1   . PHE A 1 40  ? 8.498   10.618  -33.451 1.00 36.86  ? 40   PHE A CE1   1 
ATOM   297  C CE2   . PHE A 1 40  ? 7.669   11.902  -31.639 1.00 38.49  ? 40   PHE A CE2   1 
ATOM   298  C CZ    . PHE A 1 40  ? 7.845   11.731  -32.990 1.00 36.25  ? 40   PHE A CZ    1 
ATOM   299  N N     . HIS A 1 41  ? 12.503  7.458   -29.043 1.00 38.13  ? 41   HIS A N     1 
ATOM   300  C CA    . HIS A 1 41  ? 13.260  6.828   -27.937 1.00 39.81  ? 41   HIS A CA    1 
ATOM   301  C C     . HIS A 1 41  ? 13.762  7.930   -27.002 1.00 34.64  ? 41   HIS A C     1 
ATOM   302  O O     . HIS A 1 41  ? 14.220  8.975   -27.452 1.00 34.22  ? 41   HIS A O     1 
ATOM   303  C CB    . HIS A 1 41  ? 14.415  5.956   -28.451 1.00 43.78  ? 41   HIS A CB    1 
ATOM   304  C CG    . HIS A 1 41  ? 13.978  4.654   -29.033 1.00 52.55  ? 41   HIS A CG    1 
ATOM   305  N ND1   . HIS A 1 41  ? 14.823  3.867   -29.794 1.00 58.16  ? 41   HIS A ND1   1 
ATOM   306  C CD2   . HIS A 1 41  ? 12.787  4.017   -29.000 1.00 58.30  ? 41   HIS A CD2   1 
ATOM   307  C CE1   . HIS A 1 41  ? 14.180  2.785   -30.181 1.00 63.60  ? 41   HIS A CE1   1 
ATOM   308  N NE2   . HIS A 1 41  ? 12.925  2.851   -29.704 1.00 63.27  ? 41   HIS A NE2   1 
ATOM   309  N N     . ASP A 1 42  ? 13.672  7.701   -25.709 1.00 35.44  ? 42   ASP A N     1 
ATOM   310  C CA    . ASP A 1 42  ? 14.433  8.512   -24.744 1.00 33.06  ? 42   ASP A CA    1 
ATOM   311  C C     . ASP A 1 42  ? 15.897  8.444   -25.185 1.00 32.88  ? 42   ASP A C     1 
ATOM   312  O O     . ASP A 1 42  ? 16.434  7.354   -25.290 1.00 33.28  ? 42   ASP A O     1 
ATOM   313  C CB    . ASP A 1 42  ? 14.208  7.947   -23.349 1.00 32.03  ? 42   ASP A CB    1 
ATOM   314  C CG    . ASP A 1 42  ? 14.970  8.666   -22.261 1.00 27.47  ? 42   ASP A CG    1 
ATOM   315  O OD1   . ASP A 1 42  ? 15.716  9.620   -22.578 1.00 31.04  ? 42   ASP A OD1   1 
ATOM   316  O OD2   . ASP A 1 42  ? 14.784  8.267   -21.109 1.00 30.18  ? 42   ASP A OD2   1 
ATOM   317  N N     . PRO A 1 43  ? 16.584  9.574   -25.461 1.00 29.90  ? 43   PRO A N     1 
ATOM   318  C CA    . PRO A 1 43  ? 17.991  9.530   -25.846 1.00 31.42  ? 43   PRO A CA    1 
ATOM   319  C C     . PRO A 1 43  ? 18.870  9.177   -24.639 1.00 33.15  ? 43   PRO A C     1 
ATOM   320  O O     . PRO A 1 43  ? 19.980  8.773   -24.844 1.00 28.29  ? 43   PRO A O     1 
ATOM   321  C CB    . PRO A 1 43  ? 18.325  10.969  -26.258 1.00 33.54  ? 43   PRO A CB    1 
ATOM   322  C CG    . PRO A 1 43  ? 17.306  11.826  -25.486 1.00 31.00  ? 43   PRO A CG    1 
ATOM   323  C CD    . PRO A 1 43  ? 16.084  10.953  -25.313 1.00 31.19  ? 43   PRO A CD    1 
ATOM   324  N N     . TYR A 1 44  ? 18.373  9.400   -23.438 1.00 27.87  ? 44   TYR A N     1 
ATOM   325  C CA    . TYR A 1 44  ? 19.166  9.176   -22.252 1.00 32.30  ? 44   TYR A CA    1 
ATOM   326  C C     . TYR A 1 44  ? 18.518  8.152   -21.349 1.00 31.29  ? 44   TYR A C     1 
ATOM   327  O O     . TYR A 1 44  ? 18.154  8.459   -20.240 1.00 33.08  ? 44   TYR A O     1 
ATOM   328  C CB    . TYR A 1 44  ? 19.366  10.492  -21.490 1.00 31.46  ? 44   TYR A CB    1 
ATOM   329  C CG    . TYR A 1 44  ? 19.918  11.678  -22.257 1.00 31.02  ? 44   TYR A CG    1 
ATOM   330  C CD1   . TYR A 1 44  ? 20.767  11.522  -23.340 1.00 31.48  ? 44   TYR A CD1   1 
ATOM   331  C CD2   . TYR A 1 44  ? 19.612  12.960  -21.866 1.00 32.25  ? 44   TYR A CD2   1 
ATOM   332  C CE1   . TYR A 1 44  ? 21.278  12.604  -24.013 1.00 31.89  ? 44   TYR A CE1   1 
ATOM   333  C CE2   . TYR A 1 44  ? 20.119  14.045  -22.531 1.00 32.80  ? 44   TYR A CE2   1 
ATOM   334  C CZ    . TYR A 1 44  ? 20.950  13.862  -23.602 1.00 36.05  ? 44   TYR A CZ    1 
ATOM   335  O OH    . TYR A 1 44  ? 21.445  14.952  -24.259 1.00 35.59  ? 44   TYR A OH    1 
ATOM   336  N N     . PRO A 1 45  ? 18.373  6.882   -21.844 1.00 35.03  ? 45   PRO A N     1 
ATOM   337  C CA    . PRO A 1 45  ? 17.667  5.978   -20.941 1.00 34.91  ? 45   PRO A CA    1 
ATOM   338  C C     . PRO A 1 45  ? 18.433  5.613   -19.694 1.00 37.48  ? 45   PRO A C     1 
ATOM   339  O O     . PRO A 1 45  ? 19.624  5.492   -19.714 1.00 36.37  ? 45   PRO A O     1 
ATOM   340  C CB    . PRO A 1 45  ? 17.455  4.769   -21.795 1.00 34.94  ? 45   PRO A CB    1 
ATOM   341  C CG    . PRO A 1 45  ? 18.625  4.707   -22.677 1.00 32.96  ? 45   PRO A CG    1 
ATOM   342  C CD    . PRO A 1 45  ? 18.835  6.122   -23.044 1.00 35.21  ? 45   PRO A CD    1 
ATOM   343  N N     . VAL A 1 46  ? 17.722  5.435   -18.605 1.00 44.53  ? 46   VAL A N     1 
ATOM   344  C CA    . VAL A 1 46  ? 18.357  5.110   -17.340 1.00 50.34  ? 46   VAL A CA    1 
ATOM   345  C C     . VAL A 1 46  ? 18.141  3.668   -16.889 1.00 54.68  ? 46   VAL A C     1 
ATOM   346  O O     . VAL A 1 46  ? 18.757  3.195   -15.976 1.00 55.68  ? 46   VAL A O     1 
ATOM   347  C CB    . VAL A 1 46  ? 17.965  6.080   -16.220 1.00 48.18  ? 46   VAL A CB    1 
ATOM   348  C CG1   . VAL A 1 46  ? 18.618  7.423   -16.426 1.00 52.89  ? 46   VAL A CG1   1 
ATOM   349  C CG2   . VAL A 1 46  ? 16.464  6.200   -16.114 1.00 46.96  ? 46   VAL A CG2   1 
ATOM   350  N N     . GLY A 1 47  ? 17.256  2.952   -17.514 1.00 69.32  ? 47   GLY A N     1 
ATOM   351  C CA    . GLY A 1 47  ? 17.129  1.569   -17.134 1.00 75.45  ? 47   GLY A CA    1 
ATOM   352  C C     . GLY A 1 47  ? 17.665  0.853   -18.307 1.00 73.52  ? 47   GLY A C     1 
ATOM   353  O O     . GLY A 1 47  ? 18.846  0.863   -18.563 1.00 80.13  ? 47   GLY A O     1 
ATOM   354  N N     . ASP A 1 48  ? 16.792  0.216   -19.048 1.00 67.45  ? 48   ASP A N     1 
ATOM   355  C CA    . ASP A 1 48  ? 17.237  -0.401  -20.252 1.00 74.20  ? 48   ASP A CA    1 
ATOM   356  C C     . ASP A 1 48  ? 17.214  0.676   -21.253 1.00 71.44  ? 48   ASP A C     1 
ATOM   357  O O     . ASP A 1 48  ? 17.984  1.606   -21.185 1.00 73.79  ? 48   ASP A O     1 
ATOM   358  C CB    . ASP A 1 48  ? 16.295  -1.514  -20.701 1.00 83.66  ? 48   ASP A CB    1 
ATOM   359  N N     . ALA A 1 49  ? 16.295  0.576   -22.177 1.00 66.12  ? 49   ALA A N     1 
ATOM   360  C CA    . ALA A 1 49  ? 16.263  1.511   -23.244 1.00 65.85  ? 49   ALA A CA    1 
ATOM   361  C C     . ALA A 1 49  ? 15.001  1.044   -23.873 1.00 64.82  ? 49   ALA A C     1 
ATOM   362  O O     . ALA A 1 49  ? 14.316  1.804   -24.550 1.00 66.87  ? 49   ALA A O     1 
ATOM   363  C CB    . ALA A 1 49  ? 17.464  1.272   -24.147 1.00 57.11  ? 49   ALA A CB    1 
ATOM   364  N N     . ASP A 1 50  ? 14.670  -0.213  -23.630 1.00 67.11  ? 50   ASP A N     1 
ATOM   365  C CA    . ASP A 1 50  ? 13.440  -0.788  -24.135 1.00 62.62  ? 50   ASP A CA    1 
ATOM   366  C C     . ASP A 1 50  ? 12.313  -0.502  -23.156 1.00 52.35  ? 50   ASP A C     1 
ATOM   367  O O     . ASP A 1 50  ? 11.192  -0.918  -23.370 1.00 46.72  ? 50   ASP A O     1 
ATOM   368  C CB    . ASP A 1 50  ? 13.655  -2.304  -24.211 1.00 66.77  ? 50   ASP A CB    1 
ATOM   369  C CG    . ASP A 1 50  ? 12.662  -3.009  -25.111 1.00 71.13  ? 50   ASP A CG    1 
ATOM   370  O OD1   . ASP A 1 50  ? 12.671  -2.760  -26.333 1.00 66.23  ? 50   ASP A OD1   1 
ATOM   371  O OD2   . ASP A 1 50  ? 11.879  -3.830  -24.592 1.00 76.86  ? 50   ASP A OD2   1 
ATOM   372  N N     . ALA A 1 51  ? 12.608  0.193   -22.062 1.00 47.37  ? 51   ALA A N     1 
ATOM   373  C CA    . ALA A 1 51  ? 11.572  0.392   -21.068 1.00 51.82  ? 51   ALA A CA    1 
ATOM   374  C C     . ALA A 1 51  ? 10.392  1.293   -21.420 1.00 51.46  ? 51   ALA A C     1 
ATOM   375  O O     . ALA A 1 51  ? 9.325   1.111   -20.881 1.00 71.64  ? 51   ALA A O     1 
ATOM   376  C CB    . ALA A 1 51  ? 12.205  0.856   -19.781 1.00 50.13  ? 51   ALA A CB    1 
ATOM   377  N N     . HIS A 1 52  ? 10.580  2.262   -22.286 1.00 44.40  ? 52   HIS A N     1 
ATOM   378  C CA    . HIS A 1 52  ? 9.519   3.217   -22.595 1.00 40.68  ? 52   HIS A CA    1 
ATOM   379  C C     . HIS A 1 52  ? 9.393   3.408   -24.104 1.00 36.61  ? 52   HIS A C     1 
ATOM   380  O O     . HIS A 1 52  ? 10.059  4.232   -24.687 1.00 38.46  ? 52   HIS A O     1 
ATOM   381  C CB    . HIS A 1 52  ? 9.757   4.523   -21.836 1.00 36.09  ? 52   HIS A CB    1 
ATOM   382  C CG    . HIS A 1 52  ? 9.848   4.352   -20.354 1.00 34.51  ? 52   HIS A CG    1 
ATOM   383  N ND1   . HIS A 1 52  ? 11.047  4.320   -19.681 1.00 35.16  ? 52   HIS A ND1   1 
ATOM   384  C CD2   . HIS A 1 52  ? 8.890   4.167   -19.421 1.00 32.48  ? 52   HIS A CD2   1 
ATOM   385  C CE1   . HIS A 1 52  ? 10.823  4.138   -18.394 1.00 34.62  ? 52   HIS A CE1   1 
ATOM   386  N NE2   . HIS A 1 52  ? 9.521   4.038   -18.210 1.00 35.39  ? 52   HIS A NE2   1 
ATOM   387  N N     . LEU A 1 53  ? 8.538   2.627   -24.730 1.00 32.50  ? 53   LEU A N     1 
ATOM   388  C CA    . LEU A 1 53  ? 8.380   2.690   -26.164 1.00 36.32  ? 53   LEU A CA    1 
ATOM   389  C C     . LEU A 1 53  ? 7.038   3.158   -26.654 1.00 31.84  ? 53   LEU A C     1 
ATOM   390  O O     . LEU A 1 53  ? 6.059   3.005   -25.978 1.00 30.81  ? 53   LEU A O     1 
ATOM   391  C CB    . LEU A 1 53  ? 8.685   1.356   -26.813 1.00 40.96  ? 53   LEU A CB    1 
ATOM   392  C CG    . LEU A 1 53  ? 9.814   0.492   -26.276 1.00 46.71  ? 53   LEU A CG    1 
ATOM   393  C CD1   . LEU A 1 53  ? 9.518   -0.959  -26.600 1.00 48.06  ? 53   LEU A CD1   1 
ATOM   394  C CD2   . LEU A 1 53  ? 11.145  0.932   -26.857 1.00 46.81  ? 53   LEU A CD2   1 
ATOM   395  N N     . ALA A 1 54  ? 7.018   3.708   -27.839 1.00 30.82  ? 54   ALA A N     1 
ATOM   396  C CA    . ALA A 1 54  ? 5.810   4.198   -28.511 1.00 31.67  ? 54   ALA A CA    1 
ATOM   397  C C     . ALA A 1 54  ? 5.318   3.101   -29.457 1.00 31.97  ? 54   ALA A C     1 
ATOM   398  O O     . ALA A 1 54  ? 6.149   2.486   -30.147 1.00 34.34  ? 54   ALA A O     1 
ATOM   399  C CB    . ALA A 1 54  ? 6.170   5.481   -29.207 1.00 35.70  ? 54   ALA A CB    1 
ATOM   400  N N     . SER A 1 55  ? 4.035   2.779   -29.412 1.00 31.81  ? 55   SER A N     1 
ATOM   401  C CA    . SER A 1 55  ? 3.400   1.847   -30.385 1.00 33.68  ? 55   SER A CA    1 
ATOM   402  C C     . SER A 1 55  ? 3.082   2.620   -31.674 1.00 32.88  ? 55   SER A C     1 
ATOM   403  O O     . SER A 1 55  ? 3.039   2.002   -32.730 1.00 30.87  ? 55   SER A O     1 
ATOM   404  C CB    . SER A 1 55  ? 2.184   1.200   -29.799 1.00 32.39  ? 55   SER A CB    1 
ATOM   405  O OG    . SER A 1 55  ? 1.249   2.205   -29.419 1.00 32.04  ? 55   SER A OG    1 
ATOM   406  N N     . ALA A 1 56  ? 2.914   3.947   -31.584 1.00 34.51  ? 56   ALA A N     1 
ATOM   407  C CA    . ALA A 1 56  ? 2.685   4.842   -32.738 1.00 31.78  ? 56   ALA A CA    1 
ATOM   408  C C     . ALA A 1 56  ? 2.812   6.295   -32.308 1.00 30.60  ? 56   ALA A C     1 
ATOM   409  O O     . ALA A 1 56  ? 2.773   6.584   -31.087 1.00 28.91  ? 56   ALA A O     1 
ATOM   410  C CB    . ALA A 1 56  ? 1.307   4.589   -33.297 1.00 33.21  ? 56   ALA A CB    1 
ATOM   411  N N     . VAL A 1 57  ? 2.897   7.174   -33.297 1.00 29.11  ? 57   VAL A N     1 
ATOM   412  C CA    . VAL A 1 57  ? 2.922   8.645   -33.104 1.00 29.70  ? 57   VAL A CA    1 
ATOM   413  C C     . VAL A 1 57  ? 1.854   9.252   -34.018 1.00 32.35  ? 57   VAL A C     1 
ATOM   414  O O     . VAL A 1 57  ? 1.854   8.961   -35.251 1.00 30.19  ? 57   VAL A O     1 
ATOM   415  C CB    . VAL A 1 57  ? 4.321   9.216   -33.363 1.00 28.78  ? 57   VAL A CB    1 
ATOM   416  C CG1   . VAL A 1 57  ? 4.353   10.719  -33.172 1.00 32.58  ? 57   VAL A CG1   1 
ATOM   417  C CG2   . VAL A 1 57  ? 5.357   8.540   -32.485 1.00 28.83  ? 57   VAL A CG2   1 
ATOM   418  N N     . ILE A 1 58  ? 0.970   10.042  -33.412 1.00 31.58  ? 58   ILE A N     1 
ATOM   419  C CA    . ILE A 1 58  ? -0.175  10.720  -34.077 1.00 32.02  ? 58   ILE A CA    1 
ATOM   420  C C     . ILE A 1 58  ? 0.063   12.219  -34.032 1.00 30.89  ? 58   ILE A C     1 
ATOM   421  O O     . ILE A 1 58  ? 0.205   12.774  -32.911 1.00 28.27  ? 58   ILE A O     1 
ATOM   422  C CB    . ILE A 1 58  ? -1.498  10.413  -33.373 1.00 35.66  ? 58   ILE A CB    1 
ATOM   423  C CG1   . ILE A 1 58  ? -1.678  8.923   -33.108 1.00 40.75  ? 58   ILE A CG1   1 
ATOM   424  C CG2   . ILE A 1 58  ? -2.638  11.004  -34.191 1.00 40.43  ? 58   ILE A CG2   1 
ATOM   425  C CD1   . ILE A 1 58  ? -1.449  8.075   -34.319 1.00 39.77  ? 58   ILE A CD1   1 
ATOM   426  N N     . SER A 1 59  ? 0.005   12.871  -35.179 1.00 25.69  ? 59   SER A N     1 
ATOM   427  C CA    . SER A 1 59  ? 0.207   14.334  -35.279 1.00 24.98  ? 59   SER A CA    1 
ATOM   428  C C     . SER A 1 59  ? -1.085  15.017  -35.727 1.00 27.45  ? 59   SER A C     1 
ATOM   429  O O     . SER A 1 59  ? -1.331  15.160  -36.932 1.00 29.86  ? 59   SER A O     1 
ATOM   430  C CB    . SER A 1 59  ? 1.373   14.630  -36.166 1.00 25.13  ? 59   SER A CB    1 
ATOM   431  O OG    . SER A 1 59  ? 2.570   13.966  -35.702 1.00 23.89  ? 59   SER A OG    1 
ATOM   432  N N     . PRO A 1 60  ? -1.941  15.471  -34.785 1.00 27.61  ? 60   PRO A N     1 
ATOM   433  C CA    . PRO A 1 60  ? -3.199  16.136  -35.125 1.00 28.28  ? 60   PRO A CA    1 
ATOM   434  C C     . PRO A 1 60  ? -2.960  17.566  -35.620 1.00 28.31  ? 60   PRO A C     1 
ATOM   435  O O     . PRO A 1 60  ? -1.998  18.223  -35.215 1.00 27.85  ? 60   PRO A O     1 
ATOM   436  C CB    . PRO A 1 60  ? -3.990  16.105  -33.805 1.00 30.57  ? 60   PRO A CB    1 
ATOM   437  C CG    . PRO A 1 60  ? -2.900  16.170  -32.758 1.00 31.95  ? 60   PRO A CG    1 
ATOM   438  C CD    . PRO A 1 60  ? -1.789  15.321  -33.328 1.00 29.68  ? 60   PRO A CD    1 
ATOM   439  N N     . ARG A 1 61  ? -3.807  18.009  -36.545 1.00 25.65  ? 61   ARG A N     1 
ATOM   440  C CA    . ARG A 1 61  ? -3.654  19.324  -37.199 1.00 26.43  ? 61   ARG A CA    1 
ATOM   441  C C     . ARG A 1 61  ? -4.034  20.446  -36.229 1.00 25.04  ? 61   ARG A C     1 
ATOM   442  O O     . ARG A 1 61  ? -3.442  21.499  -36.311 1.00 23.02  ? 61   ARG A O     1 
ATOM   443  C CB    . ARG A 1 61  ? -4.564  19.423  -38.430 1.00 26.73  ? 61   ARG A CB    1 
ATOM   444  C CG    . ARG A 1 61  ? -4.440  20.747  -39.160 1.00 27.94  ? 61   ARG A CG    1 
ATOM   445  C CD    . ARG A 1 61  ? -5.187  20.680  -40.493 1.00 29.76  ? 61   ARG A CD    1 
ATOM   446  N NE    . ARG A 1 61  ? -6.625  20.543  -40.275 1.00 26.77  ? 61   ARG A NE    1 
ATOM   447  C CZ    . ARG A 1 61  ? -7.452  19.839  -41.040 1.00 31.26  ? 61   ARG A CZ    1 
ATOM   448  N NH1   . ARG A 1 61  ? -6.999  19.198  -42.109 1.00 30.53  ? 61   ARG A NH1   1 
ATOM   449  N NH2   . ARG A 1 61  ? -8.748  19.787  -40.741 1.00 28.11  ? 61   ARG A NH2   1 
ATOM   450  N N     . ASP A 1 62  ? -5.039  20.241  -35.385 1.00 27.67  ? 62   ASP A N     1 
ATOM   451  C CA    . ASP A 1 62  ? -5.730  21.366  -34.706 1.00 27.25  ? 62   ASP A CA    1 
ATOM   452  C C     . ASP A 1 62  ? -6.510  20.797  -33.523 1.00 26.06  ? 62   ASP A C     1 
ATOM   453  O O     . ASP A 1 62  ? -6.545  19.555  -33.347 1.00 26.09  ? 62   ASP A O     1 
ATOM   454  C CB    . ASP A 1 62  ? -6.577  22.186  -35.693 1.00 26.05  ? 62   ASP A CB    1 
ATOM   455  C CG    . ASP A 1 62  ? -7.547  21.348  -36.518 1.00 29.28  ? 62   ASP A CG    1 
ATOM   456  O OD1   . ASP A 1 62  ? -8.068  20.348  -35.987 1.00 29.81  ? 62   ASP A OD1   1 
ATOM   457  O OD2   . ASP A 1 62  ? -7.776  21.699  -37.680 1.00 29.87  ? 62   ASP A OD2   1 
ATOM   458  N N     . THR A 1 63  ? -7.115  21.669  -32.728 1.00 25.43  ? 63   THR A N     1 
ATOM   459  C CA    . THR A 1 63  ? -7.855  21.248  -31.513 1.00 24.40  ? 63   THR A CA    1 
ATOM   460  C C     . THR A 1 63  ? -8.918  20.216  -31.866 1.00 27.90  ? 63   THR A C     1 
ATOM   461  O O     . THR A 1 63  ? -9.003  19.187  -31.190 1.00 26.36  ? 63   THR A O     1 
ATOM   462  C CB    . THR A 1 63  ? -8.511  22.459  -30.867 1.00 24.36  ? 63   THR A CB    1 
ATOM   463  O OG1   . THR A 1 63  ? -7.484  23.421  -30.657 1.00 22.84  ? 63   THR A OG1   1 
ATOM   464  C CG2   . THR A 1 63  ? -9.244  22.093  -29.605 1.00 25.15  ? 63   THR A CG2   1 
ATOM   465  N N     . GLU A 1 64  ? -9.677  20.475  -32.934 1.00 28.85  ? 64   GLU A N     1 
ATOM   466  C CA    . GLU A 1 64  ? -10.768 19.582  -33.391 1.00 31.14  ? 64   GLU A CA    1 
ATOM   467  C C     . GLU A 1 64  ? -10.213 18.165  -33.605 1.00 24.67  ? 64   GLU A C     1 
ATOM   468  O O     . GLU A 1 64  ? -10.874 17.204  -33.145 1.00 24.78  ? 64   GLU A O     1 
ATOM   469  C CB    . GLU A 1 64  ? -11.430 20.160  -34.656 1.00 35.15  ? 64   GLU A CB    1 
ATOM   470  C CG    . GLU A 1 64  ? -12.112 21.500  -34.420 1.00 41.39  ? 64   GLU A CG    1 
ATOM   471  C CD    . GLU A 1 64  ? -11.321 22.792  -34.671 1.00 50.34  ? 64   GLU A CD    1 
ATOM   472  O OE1   . GLU A 1 64  ? -10.044 22.822  -34.539 1.00 41.10  ? 64   GLU A OE1   1 
ATOM   473  O OE2   . GLU A 1 64  ? -11.995 23.812  -34.975 1.00 62.90  ? 64   GLU A OE2   1 
ATOM   474  N N     . GLN A 1 65  ? -9.078  18.019  -34.293 1.00 22.49  ? 65   GLN A N     1 
ATOM   475  C CA    . GLN A 1 65  ? -8.445  16.685  -34.482 1.00 24.13  ? 65   GLN A CA    1 
ATOM   476  C C     . GLN A 1 65  ? -7.977  16.116  -33.133 1.00 24.21  ? 65   GLN A C     1 
ATOM   477  O O     . GLN A 1 65  ? -8.136  14.886  -32.936 1.00 27.01  ? 65   GLN A O     1 
ATOM   478  C CB    . GLN A 1 65  ? -7.313  16.757  -35.505 1.00 24.60  ? 65   GLN A CB    1 
ATOM   479  C CG    . GLN A 1 65  ? -7.849  17.074  -36.909 1.00 23.53  ? 65   GLN A CG    1 
ATOM   480  C CD    . GLN A 1 65  ? -6.859  16.816  -38.010 1.00 26.78  ? 65   GLN A CD    1 
ATOM   481  O OE1   . GLN A 1 65  ? -5.722  16.422  -37.753 1.00 26.29  ? 65   GLN A OE1   1 
ATOM   482  N NE2   . GLN A 1 65  ? -7.271  17.067  -39.256 1.00 24.79  ? 65   GLN A NE2   1 
ATOM   483  N N     . VAL A 1 66  ? -7.454  16.951  -32.222 1.00 22.88  ? 66   VAL A N     1 
ATOM   484  C CA    . VAL A 1 66  ? -7.045  16.456  -30.876 1.00 24.26  ? 66   VAL A CA    1 
ATOM   485  C C     . VAL A 1 66  ? -8.270  15.812  -30.224 1.00 23.55  ? 66   VAL A C     1 
ATOM   486  O O     . VAL A 1 66  ? -8.153  14.695  -29.700 1.00 25.94  ? 66   VAL A O     1 
ATOM   487  C CB    . VAL A 1 66  ? -6.415  17.551  -29.991 1.00 24.16  ? 66   VAL A CB    1 
ATOM   488  C CG1   . VAL A 1 66  ? -6.166  17.045  -28.571 1.00 24.00  ? 66   VAL A CG1   1 
ATOM   489  C CG2   . VAL A 1 66  ? -5.112  18.044  -30.590 1.00 24.29  ? 66   VAL A CG2   1 
ATOM   490  N N     . GLN A 1 67  ? -9.417  16.494  -30.270 1.00 24.82  ? 67   GLN A N     1 
ATOM   491  C CA    . GLN A 1 67  ? -10.695 16.005  -29.708 1.00 25.74  ? 67   GLN A CA    1 
ATOM   492  C C     . GLN A 1 67  ? -11.085 14.661  -30.333 1.00 25.77  ? 67   GLN A C     1 
ATOM   493  O O     . GLN A 1 67  ? -11.419 13.757  -29.621 1.00 23.34  ? 67   GLN A O     1 
ATOM   494  C CB    . GLN A 1 67  ? -11.776 17.051  -29.960 1.00 29.46  ? 67   GLN A CB    1 
ATOM   495  C CG    . GLN A 1 67  ? -11.646 18.270  -29.067 1.00 27.60  ? 67   GLN A CG    1 
ATOM   496  C CD    . GLN A 1 67  ? -12.744 19.227  -29.408 1.00 28.09  ? 67   GLN A CD    1 
ATOM   497  O OE1   . GLN A 1 67  ? -12.620 20.027  -30.336 1.00 27.96  ? 67   GLN A OE1   1 
ATOM   498  N NE2   . GLN A 1 67  ? -13.832 19.113  -28.673 1.00 27.76  ? 67   GLN A NE2   1 
ATOM   499  N N     . GLU A 1 68  ? -11.015 14.544  -31.649 1.00 27.29  ? 68   GLU A N     1 
ATOM   500  C CA    . GLU A 1 68  ? -11.447 13.319  -32.338 1.00 30.56  ? 68   GLU A CA    1 
ATOM   501  C C     . GLU A 1 68  ? -10.463 12.185  -32.033 1.00 27.78  ? 68   GLU A C     1 
ATOM   502  O O     . GLU A 1 68  ? -10.949 11.064  -31.796 1.00 25.03  ? 68   GLU A O     1 
ATOM   503  C CB    . GLU A 1 68  ? -11.630 13.573  -33.837 1.00 34.53  ? 68   GLU A CB    1 
ATOM   504  C CG    . GLU A 1 68  ? -12.451 12.471  -34.494 1.00 41.19  ? 68   GLU A CG    1 
ATOM   505  C CD    . GLU A 1 68  ? -13.741 12.115  -33.764 1.00 45.00  ? 68   GLU A CD    1 
ATOM   506  O OE1   . GLU A 1 68  ? -14.402 13.043  -33.259 1.00 45.92  ? 68   GLU A OE1   1 
ATOM   507  O OE2   . GLU A 1 68  ? -14.071 10.913  -33.679 1.00 55.45  ? 68   GLU A OE2   1 
ATOM   508  N N     . VAL A 1 69  ? -9.143  12.418  -32.049 1.00 27.65  ? 69   VAL A N     1 
ATOM   509  C CA    . VAL A 1 69  ? -8.197  11.317  -31.696 1.00 28.67  ? 69   VAL A CA    1 
ATOM   510  C C     . VAL A 1 69  ? -8.452  10.899  -30.246 1.00 26.77  ? 69   VAL A C     1 
ATOM   511  O O     . VAL A 1 69  ? -8.385  9.728   -29.982 1.00 26.65  ? 69   VAL A O     1 
ATOM   512  C CB    . VAL A 1 69  ? -6.713  11.610  -31.981 1.00 30.36  ? 69   VAL A CB    1 
ATOM   513  C CG1   . VAL A 1 69  ? -6.502  12.005  -33.429 1.00 29.65  ? 69   VAL A CG1   1 
ATOM   514  C CG2   . VAL A 1 69  ? -6.094  12.613  -31.045 1.00 35.40  ? 69   VAL A CG2   1 
ATOM   515  N N     . VAL A 1 70  ? -8.805  11.814  -29.349 1.00 27.37  ? 70   VAL A N     1 
ATOM   516  C CA    . VAL A 1 70  ? -9.059  11.439  -27.924 1.00 26.09  ? 70   VAL A CA    1 
ATOM   517  C C     . VAL A 1 70  ? -10.308 10.555  -27.887 1.00 26.86  ? 70   VAL A C     1 
ATOM   518  O O     . VAL A 1 70  ? -10.244 9.491   -27.215 1.00 25.91  ? 70   VAL A O     1 
ATOM   519  C CB    . VAL A 1 70  ? -9.115  12.667  -26.985 1.00 22.74  ? 70   VAL A CB    1 
ATOM   520  C CG1   . VAL A 1 70  ? -9.667  12.351  -25.615 1.00 23.76  ? 70   VAL A CG1   1 
ATOM   521  C CG2   . VAL A 1 70  ? -7.738  13.297  -26.834 1.00 23.02  ? 70   VAL A CG2   1 
ATOM   522  N N     . ARG A 1 71  ? -11.374 10.911  -28.617 1.00 29.48  ? 71   ARG A N     1 
ATOM   523  C CA    . ARG A 1 71  ? -12.636 10.094  -28.664 1.00 28.48  ? 71   ARG A CA    1 
ATOM   524  C C     . ARG A 1 71  ? -12.340 8.699   -29.242 1.00 26.48  ? 71   ARG A C     1 
ATOM   525  O O     . ARG A 1 71  ? -12.959 7.735   -28.778 1.00 28.07  ? 71   ARG A O     1 
ATOM   526  C CB    . ARG A 1 71  ? -13.735 10.793  -29.479 1.00 27.93  ? 71   ARG A CB    1 
ATOM   527  C CG    . ARG A 1 71  ? -14.264 12.080  -28.855 1.00 29.58  ? 71   ARG A CG    1 
ATOM   528  C CD    . ARG A 1 71  ? -15.328 12.688  -29.754 1.00 33.12  ? 71   ARG A CD    1 
ATOM   529  N NE    . ARG A 1 71  ? -15.606 14.062  -29.380 1.00 35.70  ? 71   ARG A NE    1 
ATOM   530  C CZ    . ARG A 1 71  ? -15.415 15.120  -30.146 1.00 32.90  ? 71   ARG A CZ    1 
ATOM   531  N NH1   . ARG A 1 71  ? -14.893 14.987  -31.353 1.00 35.34  ? 71   ARG A NH1   1 
ATOM   532  N NH2   . ARG A 1 71  ? -15.686 16.324  -29.677 1.00 32.26  ? 71   ARG A NH2   1 
ATOM   533  N N     . ILE A 1 72  ? -11.461 8.607   -30.245 1.00 25.46  ? 72   ILE A N     1 
ATOM   534  C CA    . ILE A 1 72  ? -11.062 7.323   -30.874 1.00 28.44  ? 72   ILE A CA    1 
ATOM   535  C C     . ILE A 1 72  ? -10.334 6.486   -29.822 1.00 30.57  ? 72   ILE A C     1 
ATOM   536  O O     . ILE A 1 72  ? -10.693 5.306   -29.663 1.00 28.52  ? 72   ILE A O     1 
ATOM   537  C CB    . ILE A 1 72  ? -10.219 7.537   -32.138 1.00 29.35  ? 72   ILE A CB    1 
ATOM   538  C CG1   . ILE A 1 72  ? -11.089 8.024   -33.303 1.00 29.04  ? 72   ILE A CG1   1 
ATOM   539  C CG2   . ILE A 1 72  ? -9.475  6.266   -32.511 1.00 28.23  ? 72   ILE A CG2   1 
ATOM   540  C CD1   . ILE A 1 72  ? -10.280 8.530   -34.445 1.00 30.13  ? 72   ILE A CD1   1 
ATOM   541  N N     . ALA A 1 73  ? -9.364  7.098   -29.129 1.00 32.26  ? 73   ALA A N     1 
ATOM   542  C CA    . ALA A 1 73  ? -8.602  6.469   -28.020 1.00 30.54  ? 73   ALA A CA    1 
ATOM   543  C C     . ALA A 1 73  ? -9.583  5.917   -26.975 1.00 27.13  ? 73   ALA A C     1 
ATOM   544  O O     . ALA A 1 73  ? -9.367  4.793   -26.535 1.00 25.04  ? 73   ALA A O     1 
ATOM   545  C CB    . ALA A 1 73  ? -7.609  7.456   -27.440 1.00 27.37  ? 73   ALA A CB    1 
ATOM   546  N N     . ASN A 1 74  ? -10.649 6.650   -26.636 1.00 27.72  ? 74   ASN A N     1 
ATOM   547  C CA    . ASN A 1 74  ? -11.660 6.223   -25.624 1.00 28.84  ? 74   ASN A CA    1 
ATOM   548  C C     . ASN A 1 74  ? -12.402 4.986   -26.156 1.00 30.38  ? 74   ASN A C     1 
ATOM   549  O O     . ASN A 1 74  ? -12.543 4.003   -25.417 1.00 27.80  ? 74   ASN A O     1 
ATOM   550  C CB    . ASN A 1 74  ? -12.657 7.323   -25.251 1.00 28.06  ? 74   ASN A CB    1 
ATOM   551  C CG    . ASN A 1 74  ? -12.157 8.276   -24.178 1.00 30.02  ? 74   ASN A CG    1 
ATOM   552  O OD1   . ASN A 1 74  ? -12.483 8.116   -23.001 1.00 31.14  ? 74   ASN A OD1   1 
ATOM   553  N ND2   . ASN A 1 74  ? -11.369 9.271   -24.568 1.00 25.92  ? 74   ASN A ND2   1 
ATOM   554  N N     . ARG A 1 75  ? -12.802 5.004   -27.430 1.00 30.05  ? 75   ARG A N     1 
ATOM   555  C CA    . ARG A 1 75  ? -13.594 3.900   -28.027 1.00 29.78  ? 75   ARG A CA    1 
ATOM   556  C C     . ARG A 1 75  ? -12.784 2.614   -27.887 1.00 27.95  ? 75   ARG A C     1 
ATOM   557  O O     . ARG A 1 75  ? -13.357 1.578   -27.498 1.00 29.93  ? 75   ARG A O     1 
ATOM   558  C CB    . ARG A 1 75  ? -13.951 4.209   -29.489 1.00 32.67  ? 75   ARG A CB    1 
ATOM   559  C CG    . ARG A 1 75  ? -14.304 2.979   -30.313 1.00 37.45  ? 75   ARG A CG    1 
ATOM   560  C CD    . ARG A 1 75  ? -14.887 3.346   -31.673 1.00 42.05  ? 75   ARG A CD    1 
ATOM   561  N NE    . ARG A 1 75  ? -16.176 4.014   -31.530 1.00 44.00  ? 75   ARG A NE    1 
ATOM   562  C CZ    . ARG A 1 75  ? -17.365 3.415   -31.593 1.00 41.65  ? 75   ARG A CZ    1 
ATOM   563  N NH1   . ARG A 1 75  ? -17.470 2.111   -31.789 1.00 42.26  ? 75   ARG A NH1   1 
ATOM   564  N NH2   . ARG A 1 75  ? -18.452 4.134   -31.428 1.00 41.79  ? 75   ARG A NH2   1 
ATOM   565  N N     . TYR A 1 76  ? -11.483 2.664   -28.162 1.00 27.77  ? 76   TYR A N     1 
ATOM   566  C CA    . TYR A 1 76  ? -10.648 1.445   -28.317 1.00 29.33  ? 76   TYR A CA    1 
ATOM   567  C C     . TYR A 1 76  ? -9.726  1.199   -27.116 1.00 27.96  ? 76   TYR A C     1 
ATOM   568  O O     . TYR A 1 76  ? -9.018  0.224   -27.205 1.00 29.31  ? 76   TYR A O     1 
ATOM   569  C CB    . TYR A 1 76  ? -9.830  1.514   -29.609 1.00 29.14  ? 76   TYR A CB    1 
ATOM   570  C CG    . TYR A 1 76  ? -10.703 1.377   -30.832 1.00 31.31  ? 76   TYR A CG    1 
ATOM   571  C CD1   . TYR A 1 76  ? -11.421 0.205   -31.084 1.00 34.61  ? 76   TYR A CD1   1 
ATOM   572  C CD2   . TYR A 1 76  ? -10.868 2.442   -31.702 1.00 32.51  ? 76   TYR A CD2   1 
ATOM   573  C CE1   . TYR A 1 76  ? -12.242 0.086   -32.201 1.00 36.93  ? 76   TYR A CE1   1 
ATOM   574  C CE2   . TYR A 1 76  ? -11.682 2.338   -32.820 1.00 32.79  ? 76   TYR A CE2   1 
ATOM   575  C CZ    . TYR A 1 76  ? -12.372 1.165   -33.068 1.00 34.09  ? 76   TYR A CZ    1 
ATOM   576  O OH    . TYR A 1 76  ? -13.172 1.121   -34.170 1.00 34.82  ? 76   TYR A OH    1 
ATOM   577  N N     . GLY A 1 77  ? -9.740  2.029   -26.077 1.00 28.01  ? 77   GLY A N     1 
ATOM   578  C CA    . GLY A 1 77  ? -8.889  1.868   -24.878 1.00 26.88  ? 77   GLY A CA    1 
ATOM   579  C C     . GLY A 1 77  ? -7.434  2.149   -25.167 1.00 25.67  ? 77   GLY A C     1 
ATOM   580  O O     . GLY A 1 77  ? -6.605  1.587   -24.501 1.00 26.55  ? 77   GLY A O     1 
ATOM   581  N N     . ILE A 1 78  ? -7.125  3.013   -26.131 1.00 27.25  ? 78   ILE A N     1 
ATOM   582  C CA    . ILE A 1 78  ? -5.721  3.318   -26.510 1.00 27.29  ? 78   ILE A CA    1 
ATOM   583  C C     . ILE A 1 78  ? -5.123  4.326   -25.530 1.00 26.85  ? 78   ILE A C     1 
ATOM   584  O O     . ILE A 1 78  ? -5.588  5.469   -25.446 1.00 26.95  ? 78   ILE A O     1 
ATOM   585  C CB    . ILE A 1 78  ? -5.624  3.874   -27.926 1.00 28.26  ? 78   ILE A CB    1 
ATOM   586  C CG1   . ILE A 1 78  ? -6.408  3.030   -28.946 1.00 30.48  ? 78   ILE A CG1   1 
ATOM   587  C CG2   . ILE A 1 78  ? -4.148  4.018   -28.255 1.00 27.87  ? 78   ILE A CG2   1 
ATOM   588  C CD1   . ILE A 1 78  ? -5.827  1.658   -29.198 1.00 31.94  ? 78   ILE A CD1   1 
ATOM   589  N N     . PRO A 1 79  ? -4.035  3.979   -24.816 1.00 27.96  ? 79   PRO A N     1 
ATOM   590  C CA    . PRO A 1 79  ? -3.359  4.949   -23.953 1.00 30.42  ? 79   PRO A CA    1 
ATOM   591  C C     . PRO A 1 79  ? -2.633  5.955   -24.850 1.00 26.20  ? 79   PRO A C     1 
ATOM   592  O O     . PRO A 1 79  ? -1.966  5.560   -25.815 1.00 26.88  ? 79   PRO A O     1 
ATOM   593  C CB    . PRO A 1 79  ? -2.397  4.121   -23.083 1.00 29.50  ? 79   PRO A CB    1 
ATOM   594  C CG    . PRO A 1 79  ? -2.170  2.858   -23.881 1.00 31.75  ? 79   PRO A CG    1 
ATOM   595  C CD    . PRO A 1 79  ? -3.401  2.658   -24.759 1.00 32.82  ? 79   PRO A CD    1 
ATOM   596  N N     . LEU A 1 80  ? -2.790  7.231   -24.560 1.00 26.93  ? 80   LEU A N     1 
ATOM   597  C CA    . LEU A 1 80  ? -2.026  8.240   -25.324 1.00 32.95  ? 80   LEU A CA    1 
ATOM   598  C C     . LEU A 1 80  ? -1.185  9.148   -24.413 1.00 30.03  ? 80   LEU A C     1 
ATOM   599  O O     . LEU A 1 80  ? -1.662  9.716   -23.424 1.00 29.43  ? 80   LEU A O     1 
ATOM   600  C CB    . LEU A 1 80  ? -2.936  8.958   -26.324 1.00 41.71  ? 80   LEU A CB    1 
ATOM   601  C CG    . LEU A 1 80  ? -4.122  9.742   -25.805 1.00 50.79  ? 80   LEU A CG    1 
ATOM   602  C CD1   . LEU A 1 80  ? -3.657  11.114  -25.323 1.00 62.24  ? 80   LEU A CD1   1 
ATOM   603  C CD2   . LEU A 1 80  ? -5.184  9.888   -26.906 1.00 41.92  ? 80   LEU A CD2   1 
ATOM   604  N N     . SER A 1 81  ? 0.086   9.220   -24.744 1.00 25.44  ? 81   SER A N     1 
ATOM   605  C CA    . SER A 1 81  ? 1.070   10.126  -24.108 1.00 27.79  ? 81   SER A CA    1 
ATOM   606  C C     . SER A 1 81  ? 1.109   11.407  -24.935 1.00 27.10  ? 81   SER A C     1 
ATOM   607  O O     . SER A 1 81  ? 0.547   11.411  -26.028 1.00 25.18  ? 81   SER A O     1 
ATOM   608  C CB    . SER A 1 81  ? 2.406   9.455   -23.994 1.00 28.24  ? 81   SER A CB    1 
ATOM   609  O OG    . SER A 1 81  ? 2.948   9.132   -25.273 1.00 27.87  ? 81   SER A OG    1 
ATOM   610  N N     . VAL A 1 82  ? 1.732   12.463  -24.435 1.00 25.68  ? 82   VAL A N     1 
ATOM   611  C CA    . VAL A 1 82  ? 1.615   13.811  -25.059 1.00 26.05  ? 82   VAL A CA    1 
ATOM   612  C C     . VAL A 1 82  ? 2.993   14.453  -25.103 1.00 26.95  ? 82   VAL A C     1 
ATOM   613  O O     . VAL A 1 82  ? 3.694   14.467  -24.066 1.00 25.88  ? 82   VAL A O     1 
ATOM   614  C CB    . VAL A 1 82  ? 0.630   14.721  -24.302 1.00 27.00  ? 82   VAL A CB    1 
ATOM   615  C CG1   . VAL A 1 82  ? 0.195   15.881  -25.180 1.00 30.02  ? 82   VAL A CG1   1 
ATOM   616  C CG2   . VAL A 1 82  ? -0.585  13.956  -23.791 1.00 30.97  ? 82   VAL A CG2   1 
ATOM   617  N N     . ILE A 1 83  ? 3.379   14.953  -26.267 1.00 23.53  ? 83   ILE A N     1 
ATOM   618  C CA    . ILE A 1 83  ? 4.567   15.829  -26.360 1.00 26.40  ? 83   ILE A CA    1 
ATOM   619  C C     . ILE A 1 83  ? 4.114   17.150  -26.972 1.00 29.30  ? 83   ILE A C     1 
ATOM   620  O O     . ILE A 1 83  ? 3.024   17.175  -27.639 1.00 25.68  ? 83   ILE A O     1 
ATOM   621  C CB    . ILE A 1 83  ? 5.710   15.168  -27.145 1.00 24.81  ? 83   ILE A CB    1 
ATOM   622  C CG1   . ILE A 1 83  ? 5.362   14.961  -28.616 1.00 26.24  ? 83   ILE A CG1   1 
ATOM   623  C CG2   . ILE A 1 83  ? 6.139   13.884  -26.460 1.00 24.19  ? 83   ILE A CG2   1 
ATOM   624  C CD1   . ILE A 1 83  ? 6.519   14.506  -29.449 1.00 28.65  ? 83   ILE A CD1   1 
ATOM   625  N N     . SER A 1 84  ? 4.900   18.200  -26.720 1.00 28.38  ? 84   SER A N     1 
ATOM   626  C CA    . SER A 1 84  ? 4.854   19.451  -27.491 1.00 25.19  ? 84   SER A CA    1 
ATOM   627  C C     . SER A 1 84  ? 5.921   19.312  -28.555 1.00 26.46  ? 84   SER A C     1 
ATOM   628  O O     . SER A 1 84  ? 5.581   18.946  -29.673 1.00 27.97  ? 84   SER A O     1 
ATOM   629  C CB    . SER A 1 84  ? 4.972   20.673  -26.621 1.00 26.05  ? 84   SER A CB    1 
ATOM   630  O OG    . SER A 1 84  ? 3.773   20.878  -25.896 1.00 24.94  ? 84   SER A OG    1 
ATOM   631  N N     . THR A 1 85  ? 7.183   19.463  -28.175 1.00 31.31  ? 85   THR A N     1 
ATOM   632  C CA    . THR A 1 85  ? 8.368   19.218  -29.039 1.00 31.56  ? 85   THR A CA    1 
ATOM   633  C C     . THR A 1 85  ? 9.089   17.932  -28.599 1.00 30.51  ? 85   THR A C     1 
ATOM   634  O O     . THR A 1 85  ? 9.917   17.452  -29.365 1.00 28.92  ? 85   THR A O     1 
ATOM   635  C CB    . THR A 1 85  ? 9.269   20.458  -29.023 1.00 31.36  ? 85   THR A CB    1 
ATOM   636  O OG1   . THR A 1 85  ? 9.362   20.932  -27.678 1.00 32.40  ? 85   THR A OG1   1 
ATOM   637  C CG2   . THR A 1 85  ? 8.722   21.541  -29.918 1.00 30.38  ? 85   THR A CG2   1 
ATOM   638  N N     . GLY A 1 86  ? 8.782   17.405  -27.406 1.00 28.19  ? 86   GLY A N     1 
ATOM   639  C CA    . GLY A 1 86  ? 9.332   16.134  -26.904 1.00 30.76  ? 86   GLY A CA    1 
ATOM   640  C C     . GLY A 1 86  ? 10.833  16.196  -26.618 1.00 29.71  ? 86   GLY A C     1 
ATOM   641  O O     . GLY A 1 86  ? 11.489  15.197  -26.829 1.00 27.60  ? 86   GLY A O     1 
ATOM   642  N N     . ARG A 1 87  ? 11.368  17.334  -26.179 1.00 30.69  ? 87   ARG A N     1 
ATOM   643  C CA    . ARG A 1 87  ? 12.814  17.479  -25.879 1.00 32.67  ? 87   ARG A CA    1 
ATOM   644  C C     . ARG A 1 87  ? 13.021  17.412  -24.366 1.00 28.14  ? 87   ARG A C     1 
ATOM   645  O O     . ARG A 1 87  ? 13.908  18.113  -23.864 1.00 29.14  ? 87   ARG A O     1 
ATOM   646  C CB    . ARG A 1 87  ? 13.362  18.794  -26.442 1.00 39.00  ? 87   ARG A CB    1 
ATOM   647  C CG    . ARG A 1 87  ? 12.943  19.107  -27.873 1.00 45.38  ? 87   ARG A CG    1 
ATOM   648  C CD    . ARG A 1 87  ? 13.137  17.956  -28.841 1.00 51.05  ? 87   ARG A CD    1 
ATOM   649  N NE    . ARG A 1 87  ? 14.525  17.569  -29.062 1.00 53.37  ? 87   ARG A NE    1 
ATOM   650  C CZ    . ARG A 1 87  ? 15.332  18.057  -30.014 1.00 51.10  ? 87   ARG A CZ    1 
ATOM   651  N NH1   . ARG A 1 87  ? 14.914  19.003  -30.836 1.00 48.48  ? 87   ARG A NH1   1 
ATOM   652  N NH2   . ARG A 1 87  ? 16.570  17.594  -30.133 1.00 45.58  ? 87   ARG A NH2   1 
ATOM   653  N N     . ASN A 1 88  ? 12.229  16.607  -23.677 1.00 27.84  ? 88   ASN A N     1 
ATOM   654  C CA    . ASN A 1 88  ? 12.235  16.535  -22.200 1.00 26.34  ? 88   ASN A CA    1 
ATOM   655  C C     . ASN A 1 88  ? 13.429  15.679  -21.769 1.00 26.24  ? 88   ASN A C     1 
ATOM   656  O O     . ASN A 1 88  ? 13.243  14.768  -20.993 1.00 25.71  ? 88   ASN A O     1 
ATOM   657  C CB    . ASN A 1 88  ? 10.921  15.997  -21.656 1.00 24.93  ? 88   ASN A CB    1 
ATOM   658  C CG    . ASN A 1 88  ? 10.619  16.580  -20.287 1.00 26.21  ? 88   ASN A CG    1 
ATOM   659  O OD1   . ASN A 1 88  ? 11.150  17.634  -19.952 1.00 27.19  ? 88   ASN A OD1   1 
ATOM   660  N ND2   . ASN A 1 88  ? 9.724   15.961  -19.528 1.00 23.60  ? 88   ASN A ND2   1 
ATOM   661  N N     . ASN A 1 89  ? 14.615  16.030  -22.235 1.00 27.64  ? 89   ASN A N     1 
ATOM   662  C CA    . ASN A 1 89  ? 15.851  15.235  -22.034 1.00 31.43  ? 89   ASN A CA    1 
ATOM   663  C C     . ASN A 1 89  ? 16.282  15.398  -20.569 1.00 31.16  ? 89   ASN A C     1 
ATOM   664  O O     . ASN A 1 89  ? 16.181  16.522  -20.050 1.00 31.72  ? 89   ASN A O     1 
ATOM   665  C CB    . ASN A 1 89  ? 16.888  15.631  -23.068 1.00 31.22  ? 89   ASN A CB    1 
ATOM   666  C CG    . ASN A 1 89  ? 16.433  15.317  -24.477 1.00 32.50  ? 89   ASN A CG    1 
ATOM   667  O OD1   . ASN A 1 89  ? 15.509  14.530  -24.695 1.00 32.89  ? 89   ASN A OD1   1 
ATOM   668  N ND2   . ASN A 1 89  ? 17.110  15.906  -25.443 1.00 33.56  ? 89   ASN A ND2   1 
ATOM   669  N N     . GLY A 1 90  ? 16.623  14.291  -19.915 1.00 29.20  ? 90   GLY A N     1 
ATOM   670  C CA    . GLY A 1 90  ? 16.791  14.221  -18.453 1.00 27.59  ? 90   GLY A CA    1 
ATOM   671  C C     . GLY A 1 90  ? 15.579  13.614  -17.787 1.00 27.98  ? 90   GLY A C     1 
ATOM   672  O O     . GLY A 1 90  ? 15.689  13.231  -16.604 1.00 27.82  ? 90   GLY A O     1 
ATOM   673  N N     . TYR A 1 91  ? 14.454  13.535  -18.512 1.00 25.76  ? 91   TYR A N     1 
ATOM   674  C CA    . TYR A 1 91  ? 13.124  13.220  -17.938 1.00 29.05  ? 91   TYR A CA    1 
ATOM   675  C C     . TYR A 1 91  ? 12.388  12.138  -18.759 1.00 28.15  ? 91   TYR A C     1 
ATOM   676  O O     . TYR A 1 91  ? 11.291  11.713  -18.353 1.00 27.71  ? 91   TYR A O     1 
ATOM   677  C CB    . TYR A 1 91  ? 12.358  14.537  -17.791 1.00 27.66  ? 91   TYR A CB    1 
ATOM   678  C CG    . TYR A 1 91  ? 12.971  15.528  -16.829 1.00 26.53  ? 91   TYR A CG    1 
ATOM   679  C CD1   . TYR A 1 91  ? 13.271  15.174  -15.517 1.00 25.77  ? 91   TYR A CD1   1 
ATOM   680  C CD2   . TYR A 1 91  ? 13.235  16.824  -17.216 1.00 27.38  ? 91   TYR A CD2   1 
ATOM   681  C CE1   . TYR A 1 91  ? 13.823  16.085  -14.628 1.00 27.08  ? 91   TYR A CE1   1 
ATOM   682  C CE2   . TYR A 1 91  ? 13.774  17.752  -16.337 1.00 28.48  ? 91   TYR A CE2   1 
ATOM   683  C CZ    . TYR A 1 91  ? 14.037  17.394  -15.031 1.00 29.23  ? 91   TYR A CZ    1 
ATOM   684  O OH    . TYR A 1 91  ? 14.582  18.322  -14.200 1.00 32.65  ? 91   TYR A OH    1 
ATOM   685  N N     . GLY A 1 92  ? 12.973  11.682  -19.872 1.00 28.87  ? 92   GLY A N     1 
ATOM   686  C CA    . GLY A 1 92  ? 12.387  10.649  -20.740 1.00 28.41  ? 92   GLY A CA    1 
ATOM   687  C C     . GLY A 1 92  ? 12.336  11.048  -22.204 1.00 27.62  ? 92   GLY A C     1 
ATOM   688  O O     . GLY A 1 92  ? 11.986  10.200  -23.022 1.00 26.47  ? 92   GLY A O     1 
ATOM   689  N N     . GLY A 1 93  ? 12.698  12.282  -22.553 1.00 31.22  ? 93   GLY A N     1 
ATOM   690  C CA    . GLY A 1 93  ? 12.580  12.763  -23.937 1.00 32.41  ? 93   GLY A CA    1 
ATOM   691  C C     . GLY A 1 93  ? 11.131  12.716  -24.371 1.00 32.65  ? 93   GLY A C     1 
ATOM   692  O O     . GLY A 1 93  ? 10.246  13.199  -23.610 1.00 33.91  ? 93   GLY A O     1 
ATOM   693  N N     . SER A 1 94  ? 10.836  12.088  -25.512 1.00 34.72  ? 94   SER A N     1 
ATOM   694  C CA    . SER A 1 94  ? 9.431   11.991  -25.984 1.00 32.65  ? 94   SER A CA    1 
ATOM   695  C C     . SER A 1 94  ? 8.821   10.631  -25.629 1.00 31.94  ? 94   SER A C     1 
ATOM   696  O O     . SER A 1 94  ? 7.697   10.385  -26.045 1.00 29.75  ? 94   SER A O     1 
ATOM   697  C CB    . SER A 1 94  ? 9.293   12.360  -27.431 1.00 36.07  ? 94   SER A CB    1 
ATOM   698  O OG    . SER A 1 94  ? 10.442  12.057  -28.156 1.00 40.74  ? 94   SER A OG    1 
ATOM   699  N N     . ALA A 1 95  ? 9.494   9.807   -24.820 1.00 27.78  ? 95   ALA A N     1 
ATOM   700  C CA    . ALA A 1 95  ? 9.062   8.428   -24.558 1.00 29.52  ? 95   ALA A CA    1 
ATOM   701  C C     . ALA A 1 95  ? 7.925   8.480   -23.542 1.00 30.41  ? 95   ALA A C     1 
ATOM   702  O O     . ALA A 1 95  ? 7.924   9.273   -22.611 1.00 29.85  ? 95   ALA A O     1 
ATOM   703  C CB    . ALA A 1 95  ? 10.218  7.553   -24.123 1.00 30.71  ? 95   ALA A CB    1 
ATOM   704  N N     . PRO A 1 96  ? 6.906   7.629   -23.719 1.00 27.78  ? 96   PRO A N     1 
ATOM   705  C CA    . PRO A 1 96  ? 5.780   7.581   -22.795 1.00 30.18  ? 96   PRO A CA    1 
ATOM   706  C C     . PRO A 1 96  ? 6.147   6.911   -21.473 1.00 29.69  ? 96   PRO A C     1 
ATOM   707  O O     . PRO A 1 96  ? 6.909   5.962   -21.478 1.00 30.74  ? 96   PRO A O     1 
ATOM   708  C CB    . PRO A 1 96  ? 4.756   6.738   -23.550 1.00 28.46  ? 96   PRO A CB    1 
ATOM   709  C CG    . PRO A 1 96  ? 5.619   5.826   -24.379 1.00 27.15  ? 96   PRO A CG    1 
ATOM   710  C CD    . PRO A 1 96  ? 6.769   6.689   -24.836 1.00 28.38  ? 96   PRO A CD    1 
ATOM   711  N N     . ARG A 1 97  ? 5.588   7.406   -20.378 1.00 25.34  ? 97   ARG A N     1 
ATOM   712  C CA    . ARG A 1 97  ? 5.694   6.686   -19.092 1.00 26.77  ? 97   ARG A CA    1 
ATOM   713  C C     . ARG A 1 97  ? 5.192   5.249   -19.298 1.00 26.62  ? 97   ARG A C     1 
ATOM   714  O O     . ARG A 1 97  ? 5.909   4.299   -18.933 1.00 28.80  ? 97   ARG A O     1 
ATOM   715  C CB    . ARG A 1 97  ? 4.912   7.384   -17.980 1.00 24.27  ? 97   ARG A CB    1 
ATOM   716  C CG    . ARG A 1 97  ? 4.821   6.530   -16.733 1.00 26.46  ? 97   ARG A CG    1 
ATOM   717  C CD    . ARG A 1 97  ? 6.209   6.240   -16.187 1.00 27.19  ? 97   ARG A CD    1 
ATOM   718  N NE    . ARG A 1 97  ? 6.064   5.422   -14.994 1.00 28.75  ? 97   ARG A NE    1 
ATOM   719  C CZ    . ARG A 1 97  ? 6.107   4.093   -14.986 1.00 30.95  ? 97   ARG A CZ    1 
ATOM   720  N NH1   . ARG A 1 97  ? 6.287   3.421   -16.114 1.00 29.69  ? 97   ARG A NH1   1 
ATOM   721  N NH2   . ARG A 1 97  ? 5.948   3.437   -13.851 1.00 33.80  ? 97   ARG A NH2   1 
ATOM   722  N N     . LEU A 1 98  ? 4.008   5.091   -19.887 1.00 26.67  ? 98   LEU A N     1 
ATOM   723  C CA    . LEU A 1 98  ? 3.427   3.749   -20.110 1.00 27.20  ? 98   LEU A CA    1 
ATOM   724  C C     . LEU A 1 98  ? 3.957   3.213   -21.426 1.00 30.21  ? 98   LEU A C     1 
ATOM   725  O O     . LEU A 1 98  ? 3.512   3.706   -22.502 1.00 30.65  ? 98   LEU A O     1 
ATOM   726  C CB    . LEU A 1 98  ? 1.912   3.788   -20.156 1.00 27.71  ? 98   LEU A CB    1 
ATOM   727  C CG    . LEU A 1 98  ? 1.282   2.441   -20.487 1.00 27.58  ? 98   LEU A CG    1 
ATOM   728  C CD1   . LEU A 1 98  ? 1.644   1.405   -19.421 1.00 29.12  ? 98   LEU A CD1   1 
ATOM   729  C CD2   . LEU A 1 98  ? -0.219  2.585   -20.599 1.00 30.40  ? 98   LEU A CD2   1 
ATOM   730  N N     . SER A 1 99  ? 4.832   2.223   -21.322 1.00 27.83  ? 99   SER A N     1 
ATOM   731  C CA    . SER A 1 99  ? 5.465   1.538   -22.469 1.00 34.43  ? 99   SER A CA    1 
ATOM   732  C C     . SER A 1 99  ? 4.378   1.009   -23.417 1.00 31.69  ? 99   SER A C     1 
ATOM   733  O O     . SER A 1 99  ? 3.483   0.310   -22.949 1.00 33.36  ? 99   SER A O     1 
ATOM   734  C CB    . SER A 1 99  ? 6.328   0.427   -21.952 1.00 38.17  ? 99   SER A CB    1 
ATOM   735  O OG    . SER A 1 99  ? 6.906   -0.269  -23.031 1.00 48.82  ? 99   SER A OG    1 
ATOM   736  N N     . GLY A 1 100 ? 4.444   1.348   -24.702 1.00 33.51  ? 100  GLY A N     1 
ATOM   737  C CA    . GLY A 1 100 ? 3.410   0.959   -25.677 1.00 34.23  ? 100  GLY A CA    1 
ATOM   738  C C     . GLY A 1 100 ? 2.392   2.060   -25.910 1.00 35.10  ? 100  GLY A C     1 
ATOM   739  O O     . GLY A 1 100 ? 1.578   1.897   -26.826 1.00 36.19  ? 100  GLY A O     1 
ATOM   740  N N     . ALA A 1 101 ? 2.425   3.162   -25.154 1.00 28.50  ? 101  ALA A N     1 
ATOM   741  C CA    . ALA A 1 101 ? 1.432   4.239   -25.365 1.00 29.47  ? 101  ALA A CA    1 
ATOM   742  C C     . ALA A 1 101 ? 1.589   4.742   -26.798 1.00 28.21  ? 101  ALA A C     1 
ATOM   743  O O     . ALA A 1 101 ? 2.678   4.585   -27.415 1.00 29.09  ? 101  ALA A O     1 
ATOM   744  C CB    . ALA A 1 101 ? 1.542   5.365   -24.375 1.00 26.59  ? 101  ALA A CB    1 
ATOM   745  N N     . VAL A 1 102 ? 0.517   5.299   -27.315 1.00 24.67  ? 102  VAL A N     1 
ATOM   746  C CA    . VAL A 1 102 ? 0.580   6.109   -28.552 1.00 26.01  ? 102  VAL A CA    1 
ATOM   747  C C     . VAL A 1 102 ? 0.881   7.562   -28.201 1.00 25.50  ? 102  VAL A C     1 
ATOM   748  O O     . VAL A 1 102 ? 0.146   8.153   -27.394 1.00 30.97  ? 102  VAL A O     1 
ATOM   749  C CB    . VAL A 1 102 ? -0.726  5.932   -29.336 1.00 25.01  ? 102  VAL A CB    1 
ATOM   750  C CG1   . VAL A 1 102 ? -0.837  6.945   -30.450 1.00 25.89  ? 102  VAL A CG1   1 
ATOM   751  C CG2   . VAL A 1 102 ? -0.767  4.523   -29.879 1.00 24.23  ? 102  VAL A CG2   1 
ATOM   752  N N     . VAL A 1 103 ? 1.913   8.121   -28.817 1.00 25.16  ? 103  VAL A N     1 
ATOM   753  C CA    . VAL A 1 103 ? 2.348   9.518   -28.571 1.00 26.10  ? 103  VAL A CA    1 
ATOM   754  C C     . VAL A 1 103 ? 1.481   10.451  -29.416 1.00 27.33  ? 103  VAL A C     1 
ATOM   755  O O     . VAL A 1 103 ? 1.444   10.300  -30.663 1.00 24.77  ? 103  VAL A O     1 
ATOM   756  C CB    . VAL A 1 103 ? 3.842   9.699   -28.869 1.00 25.54  ? 103  VAL A CB    1 
ATOM   757  C CG1   . VAL A 1 103 ? 4.305   11.131  -28.646 1.00 24.86  ? 103  VAL A CG1   1 
ATOM   758  C CG2   . VAL A 1 103 ? 4.706   8.722   -28.081 1.00 27.59  ? 103  VAL A CG2   1 
ATOM   759  N N     . VAL A 1 104 ? 0.840   11.416  -28.766 1.00 25.72  ? 104  VAL A N     1 
ATOM   760  C CA    . VAL A 1 104 ? 0.184   12.554  -29.479 1.00 25.07  ? 104  VAL A CA    1 
ATOM   761  C C     . VAL A 1 104 ? 1.213   13.665  -29.602 1.00 25.47  ? 104  VAL A C     1 
ATOM   762  O O     . VAL A 1 104 ? 1.605   14.271  -28.578 1.00 24.55  ? 104  VAL A O     1 
ATOM   763  C CB    . VAL A 1 104 ? -1.097  13.018  -28.785 1.00 23.30  ? 104  VAL A CB    1 
ATOM   764  C CG1   . VAL A 1 104 ? -1.780  14.145  -29.538 1.00 25.48  ? 104  VAL A CG1   1 
ATOM   765  C CG2   . VAL A 1 104 ? -2.031  11.859  -28.591 1.00 23.32  ? 104  VAL A CG2   1 
ATOM   766  N N     . ASN A 1 105 ? 1.687   13.880  -30.822 1.00 26.28  ? 105  ASN A N     1 
ATOM   767  C CA    . ASN A 1 105 ? 2.673   14.924  -31.166 1.00 27.70  ? 105  ASN A CA    1 
ATOM   768  C C     . ASN A 1 105 ? 1.896   16.194  -31.514 1.00 25.52  ? 105  ASN A C     1 
ATOM   769  O O     . ASN A 1 105 ? 1.514   16.378  -32.690 1.00 25.29  ? 105  ASN A O     1 
ATOM   770  C CB    . ASN A 1 105 ? 3.606   14.416  -32.272 1.00 29.21  ? 105  ASN A CB    1 
ATOM   771  C CG    . ASN A 1 105 ? 4.689   15.406  -32.629 1.00 28.93  ? 105  ASN A CG    1 
ATOM   772  O OD1   . ASN A 1 105 ? 4.626   16.562  -32.245 1.00 31.89  ? 105  ASN A OD1   1 
ATOM   773  N ND2   . ASN A 1 105 ? 5.685   14.965  -33.377 1.00 29.18  ? 105  ASN A ND2   1 
ATOM   774  N N     . THR A 1 106 ? 1.695   17.053  -30.530 1.00 23.41  ? 106  THR A N     1 
ATOM   775  C CA    . THR A 1 106 ? 0.886   18.283  -30.667 1.00 26.89  ? 106  THR A CA    1 
ATOM   776  C C     . THR A 1 106 ? 1.686   19.328  -31.454 1.00 26.76  ? 106  THR A C     1 
ATOM   777  O O     . THR A 1 106 ? 1.041   20.129  -32.134 1.00 31.85  ? 106  THR A O     1 
ATOM   778  C CB    . THR A 1 106 ? 0.382   18.770  -29.300 1.00 25.03  ? 106  THR A CB    1 
ATOM   779  O OG1   . THR A 1 106 ? 1.500   19.186  -28.526 1.00 28.41  ? 106  THR A OG1   1 
ATOM   780  C CG2   . THR A 1 106 ? -0.417  17.719  -28.578 1.00 27.96  ? 106  THR A CG2   1 
ATOM   781  N N     . GLY A 1 107 ? 3.026   19.310  -31.367 1.00 25.46  ? 107  GLY A N     1 
ATOM   782  C CA    . GLY A 1 107 ? 3.906   20.363  -31.887 1.00 25.45  ? 107  GLY A CA    1 
ATOM   783  C C     . GLY A 1 107 ? 4.107   20.256  -33.385 1.00 25.15  ? 107  GLY A C     1 
ATOM   784  O O     . GLY A 1 107 ? 4.462   21.257  -33.983 1.00 22.59  ? 107  GLY A O     1 
ATOM   785  N N     . GLU A 1 108 ? 3.978   19.071  -33.979 1.00 26.40  ? 108  GLU A N     1 
ATOM   786  C CA    . GLU A 1 108 ? 4.397   18.921  -35.397 1.00 29.12  ? 108  GLU A CA    1 
ATOM   787  C C     . GLU A 1 108 ? 3.569   19.867  -36.289 1.00 26.42  ? 108  GLU A C     1 
ATOM   788  O O     . GLU A 1 108 ? 4.141   20.565  -37.123 1.00 27.51  ? 108  GLU A O     1 
ATOM   789  C CB    . GLU A 1 108 ? 4.254   17.489  -35.884 1.00 31.57  ? 108  GLU A CB    1 
ATOM   790  C CG    . GLU A 1 108 ? 4.776   17.367  -37.312 1.00 32.74  ? 108  GLU A CG    1 
ATOM   791  C CD    . GLU A 1 108 ? 4.835   15.967  -37.861 1.00 34.59  ? 108  GLU A CD    1 
ATOM   792  O OE1   . GLU A 1 108 ? 5.250   15.826  -39.030 1.00 43.91  ? 108  GLU A OE1   1 
ATOM   793  O OE2   . GLU A 1 108 ? 4.488   15.026  -37.117 1.00 36.48  ? 108  GLU A OE2   1 
ATOM   794  N N     . ARG A 1 109 ? 2.255   19.879  -36.131 1.00 27.23  ? 109  ARG A N     1 
ATOM   795  C CA    . ARG A 1 109 ? 1.343   20.699  -36.965 1.00 28.18  ? 109  ARG A CA    1 
ATOM   796  C C     . ARG A 1 109 ? 0.781   21.871  -36.154 1.00 28.56  ? 109  ARG A C     1 
ATOM   797  O O     . ARG A 1 109 ? 0.484   22.906  -36.759 1.00 25.60  ? 109  ARG A O     1 
ATOM   798  C CB    . ARG A 1 109 ? 0.213   19.820  -37.495 1.00 28.00  ? 109  ARG A CB    1 
ATOM   799  C CG    . ARG A 1 109 ? 0.717   18.634  -38.298 1.00 31.19  ? 109  ARG A CG    1 
ATOM   800  C CD    . ARG A 1 109 ? -0.370  17.620  -38.548 1.00 30.75  ? 109  ARG A CD    1 
ATOM   801  N NE    . ARG A 1 109 ? -1.235  18.004  -39.633 1.00 30.40  ? 109  ARG A NE    1 
ATOM   802  C CZ    . ARG A 1 109 ? -2.316  17.332  -40.025 1.00 29.05  ? 109  ARG A CZ    1 
ATOM   803  N NH1   . ARG A 1 109 ? -2.701  16.246  -39.387 1.00 27.04  ? 109  ARG A NH1   1 
ATOM   804  N NH2   . ARG A 1 109 ? -2.999  17.748  -41.077 1.00 32.24  ? 109  ARG A NH2   1 
ATOM   805  N N     . MET A 1 110 ? 0.631   21.758  -34.836 1.00 28.31  ? 110  MET A N     1 
ATOM   806  C CA    . MET A 1 110 ? 0.141   22.928  -34.057 1.00 29.94  ? 110  MET A CA    1 
ATOM   807  C C     . MET A 1 110 ? 1.352   23.712  -33.528 1.00 29.33  ? 110  MET A C     1 
ATOM   808  O O     . MET A 1 110 ? 1.734   23.559  -32.330 1.00 26.01  ? 110  MET A O     1 
ATOM   809  C CB    . MET A 1 110 ? -0.828  22.515  -32.948 1.00 31.13  ? 110  MET A CB    1 
ATOM   810  C CG    . MET A 1 110 ? -1.994  21.676  -33.448 1.00 37.08  ? 110  MET A CG    1 
ATOM   811  S SD    . MET A 1 110 ? -2.923  20.892  -32.083 1.00 37.55  ? 110  MET A SD    1 
ATOM   812  C CE    . MET A 1 110 ? -3.585  22.400  -31.422 1.00 37.38  ? 110  MET A CE    1 
ATOM   813  N N     . ASN A 1 111 ? 1.900   24.568  -34.390 1.00 27.85  ? 111  ASN A N     1 
ATOM   814  C CA    . ASN A 1 111 ? 3.237   25.201  -34.219 1.00 28.32  ? 111  ASN A CA    1 
ATOM   815  C C     . ASN A 1 111 ? 3.156   26.701  -34.471 1.00 25.83  ? 111  ASN A C     1 
ATOM   816  O O     . ASN A 1 111 ? 4.211   27.297  -34.688 1.00 28.71  ? 111  ASN A O     1 
ATOM   817  C CB    . ASN A 1 111 ? 4.304   24.593  -35.132 1.00 30.67  ? 111  ASN A CB    1 
ATOM   818  C CG    . ASN A 1 111 ? 3.995   24.813  -36.593 1.00 31.01  ? 111  ASN A CG    1 
ATOM   819  O OD1   . ASN A 1 111 ? 2.960   25.368  -36.927 1.00 31.84  ? 111  ASN A OD1   1 
ATOM   820  N ND2   . ASN A 1 111 ? 4.869   24.354  -37.464 1.00 35.73  ? 111  ASN A ND2   1 
ATOM   821  N N     . ARG A 1 112 ? 1.968   27.295  -34.365 1.00 25.99  ? 112  ARG A N     1 
ATOM   822  C CA    . ARG A 1 112 ? 1.739   28.702  -34.741 1.00 31.54  ? 112  ARG A CA    1 
ATOM   823  C C     . ARG A 1 112 ? 1.826   29.580  -33.480 1.00 31.80  ? 112  ARG A C     1 
ATOM   824  O O     . ARG A 1 112 ? 1.330   29.174  -32.407 1.00 28.71  ? 112  ARG A O     1 
ATOM   825  C CB    . ARG A 1 112 ? 0.420   28.797  -35.519 1.00 36.43  ? 112  ARG A CB    1 
ATOM   826  C CG    . ARG A 1 112 ? 0.440   28.020  -36.836 1.00 41.76  ? 112  ARG A CG    1 
ATOM   827  C CD    . ARG A 1 112 ? -0.899  27.472  -37.361 1.00 51.57  ? 112  ARG A CD    1 
ATOM   828  N NE    . ARG A 1 112 ? -1.742  26.653  -36.462 1.00 48.52  ? 112  ARG A NE    1 
ATOM   829  C CZ    . ARG A 1 112 ? -2.307  25.469  -36.746 1.00 51.14  ? 112  ARG A CZ    1 
ATOM   830  N NH1   . ARG A 1 112 ? -2.127  24.878  -37.919 1.00 57.81  ? 112  ARG A NH1   1 
ATOM   831  N NH2   . ARG A 1 112 ? -3.085  24.874  -35.851 1.00 47.79  ? 112  ARG A NH2   1 
ATOM   832  N N     . ILE A 1 113 ? 2.453   30.739  -33.633 1.00 31.68  ? 113  ILE A N     1 
ATOM   833  C CA    . ILE A 1 113 ? 2.308   31.912  -32.731 1.00 33.24  ? 113  ILE A CA    1 
ATOM   834  C C     . ILE A 1 113 ? 0.989   32.568  -33.127 1.00 34.98  ? 113  ILE A C     1 
ATOM   835  O O     . ILE A 1 113 ? 0.907   33.122  -34.256 1.00 30.95  ? 113  ILE A O     1 
ATOM   836  C CB    . ILE A 1 113 ? 3.540   32.833  -32.834 1.00 34.12  ? 113  ILE A CB    1 
ATOM   837  C CG1   . ILE A 1 113 ? 4.820   32.080  -32.437 1.00 32.63  ? 113  ILE A CG1   1 
ATOM   838  C CG2   . ILE A 1 113 ? 3.325   34.084  -31.993 1.00 37.50  ? 113  ILE A CG2   1 
ATOM   839  C CD1   . ILE A 1 113 ? 6.114   32.734  -32.849 1.00 33.06  ? 113  ILE A CD1   1 
ATOM   840  N N     . LEU A 1 114 ? -0.031  32.446  -32.273 1.00 32.97  ? 114  LEU A N     1 
ATOM   841  C CA    . LEU A 1 114 ? -1.417  32.852  -32.619 1.00 31.99  ? 114  LEU A CA    1 
ATOM   842  C C     . LEU A 1 114 ? -1.568  34.350  -32.390 1.00 33.42  ? 114  LEU A C     1 
ATOM   843  O O     . LEU A 1 114 ? -2.332  34.992  -33.112 1.00 28.09  ? 114  LEU A O     1 
ATOM   844  C CB    . LEU A 1 114 ? -2.417  32.070  -31.773 1.00 32.84  ? 114  LEU A CB    1 
ATOM   845  C CG    . LEU A 1 114 ? -2.536  30.591  -32.111 1.00 36.02  ? 114  LEU A CG    1 
ATOM   846  C CD1   . LEU A 1 114 ? -3.467  29.910  -31.126 1.00 35.63  ? 114  LEU A CD1   1 
ATOM   847  C CD2   . LEU A 1 114 ? -3.013  30.382  -33.553 1.00 36.32  ? 114  LEU A CD2   1 
ATOM   848  N N     . GLU A 1 115 ? -0.900  34.900  -31.388 1.00 32.62  ? 115  GLU A N     1 
ATOM   849  C CA    . GLU A 1 115 ? -0.972  36.368  -31.197 1.00 33.67  ? 115  GLU A CA    1 
ATOM   850  C C     . GLU A 1 115 ? 0.165   36.832  -30.291 1.00 33.18  ? 115  GLU A C     1 
ATOM   851  O O     . GLU A 1 115 ? 0.573   36.081  -29.350 1.00 30.96  ? 115  GLU A O     1 
ATOM   852  C CB    . GLU A 1 115 ? -2.387  36.732  -30.740 1.00 38.12  ? 115  GLU A CB    1 
ATOM   853  C CG    . GLU A 1 115 ? -2.550  37.077  -29.293 1.00 45.91  ? 115  GLU A CG    1 
ATOM   854  C CD    . GLU A 1 115 ? -3.955  37.585  -29.006 1.00 50.79  ? 115  GLU A CD    1 
ATOM   855  O OE1   . GLU A 1 115 ? -4.902  36.775  -29.086 1.00 63.59  ? 115  GLU A OE1   1 
ATOM   856  O OE2   . GLU A 1 115 ? -4.103  38.800  -28.752 1.00 54.56  ? 115  GLU A OE2   1 
ATOM   857  N N     . VAL A 1 116 ? 0.664   38.027  -30.573 1.00 31.74  ? 116  VAL A N     1 
ATOM   858  C CA    . VAL A 1 116 ? 1.640   38.727  -29.700 1.00 33.52  ? 116  VAL A CA    1 
ATOM   859  C C     . VAL A 1 116 ? 1.153   40.159  -29.500 1.00 33.18  ? 116  VAL A C     1 
ATOM   860  O O     . VAL A 1 116 ? 0.950   40.838  -30.501 1.00 30.41  ? 116  VAL A O     1 
ATOM   861  C CB    . VAL A 1 116 ? 3.058   38.682  -30.279 1.00 31.73  ? 116  VAL A CB    1 
ATOM   862  C CG1   . VAL A 1 116 ? 4.015   39.561  -29.488 1.00 30.95  ? 116  VAL A CG1   1 
ATOM   863  C CG2   . VAL A 1 116 ? 3.562   37.256  -30.334 1.00 33.42  ? 116  VAL A CG2   1 
ATOM   864  N N     . ASP A 1 117 ? 0.932   40.557  -28.251 1.00 30.35  ? 117  ASP A N     1 
ATOM   865  C CA    . ASP A 1 117 ? 0.569   41.955  -27.918 1.00 31.15  ? 117  ASP A CA    1 
ATOM   866  C C     . ASP A 1 117 ? 1.815   42.608  -27.337 1.00 30.75  ? 117  ASP A C     1 
ATOM   867  O O     . ASP A 1 117 ? 2.197   42.258  -26.197 1.00 34.15  ? 117  ASP A O     1 
ATOM   868  C CB    . ASP A 1 117 ? -0.627  42.018  -26.979 1.00 32.58  ? 117  ASP A CB    1 
ATOM   869  C CG    . ASP A 1 117 ? -1.226  43.416  -26.855 1.00 35.80  ? 117  ASP A CG    1 
ATOM   870  O OD1   . ASP A 1 117 ? -0.471  44.338  -26.595 1.00 35.30  ? 117  ASP A OD1   1 
ATOM   871  O OD2   . ASP A 1 117 ? -2.461  43.564  -27.036 1.00 41.79  ? 117  ASP A OD2   1 
ATOM   872  N N     . GLU A 1 118 ? 2.411   43.523  -28.087 1.00 31.23  ? 118  GLU A N     1 
ATOM   873  C CA    . GLU A 1 118 ? 3.659   44.230  -27.699 1.00 33.43  ? 118  GLU A CA    1 
ATOM   874  C C     . GLU A 1 118 ? 3.417   45.082  -26.459 1.00 34.56  ? 118  GLU A C     1 
ATOM   875  O O     . GLU A 1 118 ? 4.245   45.013  -25.538 1.00 42.82  ? 118  GLU A O     1 
ATOM   876  C CB    . GLU A 1 118 ? 4.212   45.066  -28.852 1.00 35.72  ? 118  GLU A CB    1 
ATOM   877  C CG    . GLU A 1 118 ? 5.592   45.597  -28.546 1.00 35.82  ? 118  GLU A CG    1 
ATOM   878  C CD    . GLU A 1 118 ? 6.471   45.986  -29.727 1.00 36.58  ? 118  GLU A CD    1 
ATOM   879  O OE1   . GLU A 1 118 ? 5.949   46.173  -30.841 1.00 36.28  ? 118  GLU A OE1   1 
ATOM   880  O OE2   . GLU A 1 118 ? 7.690   46.165  -29.500 1.00 40.24  ? 118  GLU A OE2   1 
ATOM   881  N N     . LYS A 1 119 ? 2.301   45.802  -26.389 1.00 37.98  ? 119  LYS A N     1 
ATOM   882  C CA    . LYS A 1 119 ? 2.093   46.835  -25.338 1.00 37.27  ? 119  LYS A CA    1 
ATOM   883  C C     . LYS A 1 119 ? 1.744   46.144  -24.016 1.00 33.39  ? 119  LYS A C     1 
ATOM   884  O O     . LYS A 1 119 ? 2.257   46.580  -22.974 1.00 31.98  ? 119  LYS A O     1 
ATOM   885  C CB    . LYS A 1 119 ? 0.996   47.826  -25.737 1.00 40.02  ? 119  LYS A CB    1 
ATOM   886  C CG    . LYS A 1 119 ? 1.326   48.697  -26.945 1.00 48.33  ? 119  LYS A CG    1 
ATOM   887  C CD    . LYS A 1 119 ? 1.499   47.932  -28.263 1.00 57.79  ? 119  LYS A CD    1 
ATOM   888  C CE    . LYS A 1 119 ? 0.288   47.118  -28.698 1.00 58.58  ? 119  LYS A CE    1 
ATOM   889  N NZ    . LYS A 1 119 ? 0.673   45.953  -29.533 1.00 54.79  ? 119  LYS A NZ    1 
ATOM   890  N N     . LEU A 1 120 ? 0.907   45.107  -24.051 1.00 28.78  ? 120  LEU A N     1 
ATOM   891  C CA    . LEU A 1 120 ? 0.450   44.403  -22.816 1.00 30.55  ? 120  LEU A CA    1 
ATOM   892  C C     . LEU A 1 120 ? 1.365   43.202  -22.538 1.00 27.80  ? 120  LEU A C     1 
ATOM   893  O O     . LEU A 1 120 ? 1.236   42.616  -21.495 1.00 32.20  ? 120  LEU A O     1 
ATOM   894  C CB    . LEU A 1 120 ? -1.011  43.966  -22.958 1.00 31.89  ? 120  LEU A CB    1 
ATOM   895  C CG    . LEU A 1 120 ? -2.010  45.055  -23.319 1.00 33.29  ? 120  LEU A CG    1 
ATOM   896  C CD1   . LEU A 1 120 ? -3.433  44.492  -23.427 1.00 34.54  ? 120  LEU A CD1   1 
ATOM   897  C CD2   . LEU A 1 120 ? -1.960  46.192  -22.314 1.00 35.63  ? 120  LEU A CD2   1 
ATOM   898  N N     . GLY A 1 121 ? 2.281   42.879  -23.448 1.00 29.81  ? 121  GLY A N     1 
ATOM   899  C CA    . GLY A 1 121 ? 3.432   41.989  -23.215 1.00 27.79  ? 121  GLY A CA    1 
ATOM   900  C C     . GLY A 1 121 ? 2.988   40.557  -22.993 1.00 29.57  ? 121  GLY A C     1 
ATOM   901  O O     . GLY A 1 121 ? 3.043   40.090  -21.827 1.00 28.96  ? 121  GLY A O     1 
ATOM   902  N N     . TYR A 1 122 ? 2.449   39.920  -24.034 1.00 25.81  ? 122  TYR A N     1 
ATOM   903  C CA    . TYR A 1 122 ? 2.039   38.496  -23.984 1.00 26.68  ? 122  TYR A CA    1 
ATOM   904  C C     . TYR A 1 122 ? 2.067   37.892  -25.379 1.00 26.01  ? 122  TYR A C     1 
ATOM   905  O O     . TYR A 1 122 ? 2.109   38.618  -26.369 1.00 25.66  ? 122  TYR A O     1 
ATOM   906  C CB    . TYR A 1 122 ? 0.671   38.328  -23.344 1.00 26.88  ? 122  TYR A CB    1 
ATOM   907  C CG    . TYR A 1 122 ? -0.517  38.774  -24.168 1.00 31.47  ? 122  TYR A CG    1 
ATOM   908  C CD1   . TYR A 1 122 ? -0.992  38.005  -25.226 1.00 33.43  ? 122  TYR A CD1   1 
ATOM   909  C CD2   . TYR A 1 122 ? -1.194  39.939  -23.858 1.00 32.94  ? 122  TYR A CD2   1 
ATOM   910  C CE1   . TYR A 1 122 ? -2.110  38.383  -25.951 1.00 33.73  ? 122  TYR A CE1   1 
ATOM   911  C CE2   . TYR A 1 122 ? -2.330  40.323  -24.554 1.00 35.65  ? 122  TYR A CE2   1 
ATOM   912  C CZ    . TYR A 1 122 ? -2.784  39.543  -25.604 1.00 36.54  ? 122  TYR A CZ    1 
ATOM   913  O OH    . TYR A 1 122 ? -3.869  39.949  -26.312 1.00 33.82  ? 122  TYR A OH    1 
ATOM   914  N N     . ALA A 1 123 ? 2.082   36.567  -25.408 1.00 26.97  ? 123  ALA A N     1 
ATOM   915  C CA    . ALA A 1 123 ? 1.942   35.745  -26.623 1.00 27.40  ? 123  ALA A CA    1 
ATOM   916  C C     . ALA A 1 123 ? 0.845   34.729  -26.349 1.00 29.10  ? 123  ALA A C     1 
ATOM   917  O O     . ALA A 1 123 ? 0.726   34.282  -25.167 1.00 27.75  ? 123  ALA A O     1 
ATOM   918  C CB    . ALA A 1 123 ? 3.239   35.060  -26.932 1.00 27.59  ? 123  ALA A CB    1 
ATOM   919  N N     . LEU A 1 124 ? 0.128   34.314  -27.396 1.00 27.06  ? 124  LEU A N     1 
ATOM   920  C CA    . LEU A 1 124 ? -0.827  33.209  -27.329 1.00 27.32  ? 124  LEU A CA    1 
ATOM   921  C C     . LEU A 1 124 ? -0.161  32.205  -28.241 1.00 27.80  ? 124  LEU A C     1 
ATOM   922  O O     . LEU A 1 124 ? 0.064   32.494  -29.402 1.00 25.04  ? 124  LEU A O     1 
ATOM   923  C CB    . LEU A 1 124 ? -2.209  33.541  -27.828 1.00 28.18  ? 124  LEU A CB    1 
ATOM   924  C CG    . LEU A 1 124 ? -3.201  32.379  -27.857 1.00 27.81  ? 124  LEU A CG    1 
ATOM   925  C CD1   . LEU A 1 124 ? -3.395  31.770  -26.480 1.00 30.24  ? 124  LEU A CD1   1 
ATOM   926  C CD2   . LEU A 1 124 ? -4.523  32.835  -28.439 1.00 29.49  ? 124  LEU A CD2   1 
ATOM   927  N N     . LEU A 1 125 ? 0.172   31.045  -27.712 1.00 27.00  ? 125  LEU A N     1 
ATOM   928  C CA    . LEU A 1 125 ? 0.946   30.069  -28.451 1.00 32.42  ? 125  LEU A CA    1 
ATOM   929  C C     . LEU A 1 125 ? 0.362   28.685  -28.601 1.00 30.61  ? 125  LEU A C     1 
ATOM   930  O O     . LEU A 1 125 ? -0.298  28.183  -27.730 1.00 44.20  ? 125  LEU A O     1 
ATOM   931  C CB    . LEU A 1 125 ? 2.274   29.902  -27.733 1.00 30.38  ? 125  LEU A CB    1 
ATOM   932  C CG    . LEU A 1 125 ? 3.104   31.155  -27.528 1.00 30.11  ? 125  LEU A CG    1 
ATOM   933  C CD1   . LEU A 1 125 ? 4.269   30.812  -26.646 1.00 29.60  ? 125  LEU A CD1   1 
ATOM   934  C CD2   . LEU A 1 125 ? 3.593   31.693  -28.854 1.00 30.95  ? 125  LEU A CD2   1 
ATOM   935  N N     . GLU A 1 126 ? 0.695   28.066  -29.717 1.00 43.90  ? 126  GLU A N     1 
ATOM   936  C CA    . GLU A 1 126 ? 0.600   26.637  -29.912 1.00 42.94  ? 126  GLU A CA    1 
ATOM   937  C C     . GLU A 1 126 ? 1.796   25.811  -29.429 1.00 29.86  ? 126  GLU A C     1 
ATOM   938  O O     . GLU A 1 126 ? 2.868   26.338  -29.257 1.00 24.09  ? 126  GLU A O     1 
ATOM   939  C CB    . GLU A 1 126 ? 0.208   26.347  -31.336 1.00 51.63  ? 126  GLU A CB    1 
ATOM   940  C CG    . GLU A 1 126 ? -1.210  26.800  -31.611 1.00 58.31  ? 126  GLU A CG    1 
ATOM   941  C CD    . GLU A 1 126 ? -1.657  26.464  -33.007 1.00 73.31  ? 126  GLU A CD    1 
ATOM   942  O OE1   . GLU A 1 126 ? -2.867  26.488  -33.275 1.00 87.17  ? 126  GLU A OE1   1 
ATOM   943  O OE2   . GLU A 1 126 ? -0.789  26.171  -33.835 1.00 85.25  ? 126  GLU A OE2   1 
ATOM   944  N N     . PRO A 1 127 ? 1.571   24.505  -29.179 1.00 26.55  ? 127  PRO A N     1 
ATOM   945  C CA    . PRO A 1 127 ? 2.670   23.727  -28.589 1.00 27.66  ? 127  PRO A CA    1 
ATOM   946  C C     . PRO A 1 127 ? 3.989   23.560  -29.373 1.00 25.75  ? 127  PRO A C     1 
ATOM   947  O O     . PRO A 1 127 ? 4.997   23.359  -28.767 1.00 26.80  ? 127  PRO A O     1 
ATOM   948  C CB    . PRO A 1 127 ? 2.004   22.392  -28.271 1.00 26.16  ? 127  PRO A CB    1 
ATOM   949  C CG    . PRO A 1 127 ? 0.567   22.699  -28.128 1.00 25.27  ? 127  PRO A CG    1 
ATOM   950  C CD    . PRO A 1 127 ? 0.317   23.733  -29.169 1.00 24.70  ? 127  PRO A CD    1 
ATOM   951  N N     . GLY A 1 128 ? 3.978   23.663  -30.681 1.00 25.57  ? 128  GLY A N     1 
ATOM   952  C CA    . GLY A 1 128 ? 5.179   23.524  -31.461 1.00 24.37  ? 128  GLY A CA    1 
ATOM   953  C C     . GLY A 1 128 ? 6.065   24.731  -31.549 1.00 25.79  ? 128  GLY A C     1 
ATOM   954  O O     . GLY A 1 128 ? 7.098   24.672  -32.177 1.00 28.33  ? 128  GLY A O     1 
ATOM   955  N N     . VAL A 1 129 ? 5.647   25.826  -30.942 1.00 24.93  ? 129  VAL A N     1 
ATOM   956  C CA    . VAL A 1 129 ? 6.505   27.047  -30.903 1.00 24.99  ? 129  VAL A CA    1 
ATOM   957  C C     . VAL A 1 129 ? 7.698   26.774  -29.985 1.00 25.89  ? 129  VAL A C     1 
ATOM   958  O O     . VAL A 1 129 ? 7.500   26.565  -28.780 1.00 23.29  ? 129  VAL A O     1 
ATOM   959  C CB    . VAL A 1 129 ? 5.744   28.318  -30.461 1.00 26.51  ? 129  VAL A CB    1 
ATOM   960  C CG1   . VAL A 1 129 ? 6.648   29.524  -30.470 1.00 25.92  ? 129  VAL A CG1   1 
ATOM   961  C CG2   . VAL A 1 129 ? 4.527   28.598  -31.329 1.00 28.56  ? 129  VAL A CG2   1 
ATOM   962  N N     . THR A 1 130 ? 8.905   26.810  -30.537 1.00 26.49  ? 130  THR A N     1 
ATOM   963  C CA    . THR A 1 130 ? 10.148  26.650  -29.759 1.00 27.30  ? 130  THR A CA    1 
ATOM   964  C C     . THR A 1 130 ? 10.544  28.021  -29.221 1.00 25.64  ? 130  THR A C     1 
ATOM   965  O O     . THR A 1 130 ? 10.082  29.080  -29.747 1.00 27.93  ? 130  THR A O     1 
ATOM   966  C CB    . THR A 1 130 ? 11.293  26.010  -30.575 1.00 26.89  ? 130  THR A CB    1 
ATOM   967  O OG1   . THR A 1 130 ? 11.697  26.881  -31.636 1.00 21.43  ? 130  THR A OG1   1 
ATOM   968  C CG2   . THR A 1 130 ? 10.917  24.668  -31.162 1.00 25.15  ? 130  THR A CG2   1 
ATOM   969  N N     . TYR A 1 131 ? 11.436  28.013  -28.241 1.00 26.10  ? 131  TYR A N     1 
ATOM   970  C CA    . TYR A 1 131 ? 12.075  29.247  -27.743 1.00 24.52  ? 131  TYR A CA    1 
ATOM   971  C C     . TYR A 1 131 ? 12.752  29.991  -28.897 1.00 26.31  ? 131  TYR A C     1 
ATOM   972  O O     . TYR A 1 131 ? 12.639  31.233  -28.943 1.00 27.25  ? 131  TYR A O     1 
ATOM   973  C CB    . TYR A 1 131 ? 13.023  28.911  -26.611 1.00 25.07  ? 131  TYR A CB    1 
ATOM   974  C CG    . TYR A 1 131 ? 12.297  28.447  -25.379 1.00 25.67  ? 131  TYR A CG    1 
ATOM   975  C CD1   . TYR A 1 131 ? 11.653  29.349  -24.556 1.00 25.10  ? 131  TYR A CD1   1 
ATOM   976  C CD2   . TYR A 1 131 ? 12.208  27.093  -25.071 1.00 27.87  ? 131  TYR A CD2   1 
ATOM   977  C CE1   . TYR A 1 131 ? 10.953  28.920  -23.436 1.00 26.48  ? 131  TYR A CE1   1 
ATOM   978  C CE2   . TYR A 1 131 ? 11.533  26.653  -23.945 1.00 27.11  ? 131  TYR A CE2   1 
ATOM   979  C CZ    . TYR A 1 131 ? 10.897  27.570  -23.129 1.00 25.30  ? 131  TYR A CZ    1 
ATOM   980  O OH    . TYR A 1 131 ? 10.272  27.114  -22.002 1.00 30.30  ? 131  TYR A OH    1 
ATOM   981  N N     . PHE A 1 132 ? 13.435  29.270  -29.785 1.00 27.65  ? 132  PHE A N     1 
ATOM   982  C CA    . PHE A 1 132 ? 14.032  29.827  -31.022 1.00 28.42  ? 132  PHE A CA    1 
ATOM   983  C C     . PHE A 1 132 ? 12.940  30.499  -31.864 1.00 27.52  ? 132  PHE A C     1 
ATOM   984  O O     . PHE A 1 132 ? 13.181  31.615  -32.329 1.00 27.82  ? 132  PHE A O     1 
ATOM   985  C CB    . PHE A 1 132 ? 14.780  28.761  -31.834 1.00 30.45  ? 132  PHE A CB    1 
ATOM   986  C CG    . PHE A 1 132 ? 16.119  28.376  -31.252 1.00 31.14  ? 132  PHE A CG    1 
ATOM   987  C CD1   . PHE A 1 132 ? 17.119  29.322  -31.088 1.00 35.30  ? 132  PHE A CD1   1 
ATOM   988  C CD2   . PHE A 1 132 ? 16.374  27.074  -30.839 1.00 33.39  ? 132  PHE A CD2   1 
ATOM   989  C CE1   . PHE A 1 132 ? 18.352  28.972  -30.541 1.00 33.54  ? 132  PHE A CE1   1 
ATOM   990  C CE2   . PHE A 1 132 ? 17.600  26.728  -30.278 1.00 33.35  ? 132  PHE A CE2   1 
ATOM   991  C CZ    . PHE A 1 132 ? 18.589  27.672  -30.148 1.00 34.90  ? 132  PHE A CZ    1 
ATOM   992  N N     . ASP A 1 133 ? 11.837  29.805  -32.140 1.00 28.54  ? 133  ASP A N     1 
ATOM   993  C CA    . ASP A 1 133 ? 10.718  30.366  -32.941 1.00 30.66  ? 133  ASP A CA    1 
ATOM   994  C C     . ASP A 1 133 ? 10.271  31.693  -32.318 1.00 30.23  ? 133  ASP A C     1 
ATOM   995  O O     . ASP A 1 133 ? 10.221  32.684  -33.042 1.00 26.96  ? 133  ASP A O     1 
ATOM   996  C CB    . ASP A 1 133 ? 9.545   29.400  -33.049 1.00 28.86  ? 133  ASP A CB    1 
ATOM   997  C CG    . ASP A 1 133 ? 9.857   28.155  -33.851 1.00 32.95  ? 133  ASP A CG    1 
ATOM   998  O OD1   . ASP A 1 133 ? 10.830  28.184  -34.629 1.00 33.80  ? 133  ASP A OD1   1 
ATOM   999  O OD2   . ASP A 1 133 ? 9.154   27.149  -33.646 1.00 37.07  ? 133  ASP A OD2   1 
ATOM   1000 N N     . LEU A 1 134 ? 10.005  31.712  -31.014 1.00 27.04  ? 134  LEU A N     1 
ATOM   1001 C CA    . LEU A 1 134 ? 9.329   32.872  -30.393 1.00 28.50  ? 134  LEU A CA    1 
ATOM   1002 C C     . LEU A 1 134 ? 10.299  34.036  -30.418 1.00 29.92  ? 134  LEU A C     1 
ATOM   1003 O O     . LEU A 1 134 ? 9.856   35.146  -30.745 1.00 31.67  ? 134  LEU A O     1 
ATOM   1004 C CB    . LEU A 1 134 ? 8.870   32.582  -28.961 1.00 27.35  ? 134  LEU A CB    1 
ATOM   1005 C CG    . LEU A 1 134 ? 8.193   33.759  -28.251 1.00 26.39  ? 134  LEU A CG    1 
ATOM   1006 C CD1   . LEU A 1 134 ? 7.061   34.314  -29.080 1.00 27.34  ? 134  LEU A CD1   1 
ATOM   1007 C CD2   . LEU A 1 134 ? 7.681   33.322  -26.877 1.00 27.67  ? 134  LEU A CD2   1 
ATOM   1008 N N     . HIS A 1 135 ? 11.538  33.766  -30.025 1.00 30.72  ? 135  HIS A N     1 
ATOM   1009 C CA    . HIS A 1 135 ? 12.684  34.693  -30.132 1.00 32.98  ? 135  HIS A CA    1 
ATOM   1010 C C     . HIS A 1 135 ? 12.697  35.321  -31.529 1.00 32.79  ? 135  HIS A C     1 
ATOM   1011 O O     . HIS A 1 135 ? 12.781  36.553  -31.595 1.00 30.09  ? 135  HIS A O     1 
ATOM   1012 C CB    . HIS A 1 135 ? 14.007  33.984  -29.837 1.00 31.45  ? 135  HIS A CB    1 
ATOM   1013 C CG    . HIS A 1 135 ? 15.175  34.899  -30.017 1.00 32.22  ? 135  HIS A CG    1 
ATOM   1014 N ND1   . HIS A 1 135 ? 15.499  35.891  -29.092 1.00 31.73  ? 135  HIS A ND1   1 
ATOM   1015 C CD2   . HIS A 1 135 ? 16.051  35.020  -31.028 1.00 28.83  ? 135  HIS A CD2   1 
ATOM   1016 C CE1   . HIS A 1 135 ? 16.549  36.550  -29.529 1.00 31.08  ? 135  HIS A CE1   1 
ATOM   1017 N NE2   . HIS A 1 135 ? 16.890  36.053  -30.712 1.00 33.59  ? 135  HIS A NE2   1 
ATOM   1018 N N     . GLU A 1 136 ? 12.687  34.497  -32.579 1.00 33.04  ? 136  GLU A N     1 
ATOM   1019 C CA    . GLU A 1 136 ? 12.803  34.978  -33.985 1.00 38.55  ? 136  GLU A CA    1 
ATOM   1020 C C     . GLU A 1 136 ? 11.641  35.933  -34.232 1.00 37.01  ? 136  GLU A C     1 
ATOM   1021 O O     . GLU A 1 136 ? 11.889  37.065  -34.715 1.00 36.93  ? 136  GLU A O     1 
ATOM   1022 C CB    . GLU A 1 136 ? 12.737  33.837  -35.000 1.00 45.11  ? 136  GLU A CB    1 
ATOM   1023 C CG    . GLU A 1 136 ? 14.030  33.062  -35.163 1.00 52.48  ? 136  GLU A CG    1 
ATOM   1024 C CD    . GLU A 1 136 ? 14.084  32.238  -36.445 1.00 63.46  ? 136  GLU A CD    1 
ATOM   1025 O OE1   . GLU A 1 136 ? 13.038  32.116  -37.125 1.00 60.44  ? 136  GLU A OE1   1 
ATOM   1026 O OE2   . GLU A 1 136 ? 15.180  31.727  -36.772 1.00 74.55  ? 136  GLU A OE2   1 
ATOM   1027 N N     . TYR A 1 137 ? 10.436  35.513  -33.841 1.00 34.98  ? 137  TYR A N     1 
ATOM   1028 C CA    . TYR A 1 137 ? 9.194   36.294  -34.059 1.00 37.11  ? 137  TYR A CA    1 
ATOM   1029 C C     . TYR A 1 137 ? 9.291   37.641  -33.341 1.00 34.39  ? 137  TYR A C     1 
ATOM   1030 O O     . TYR A 1 137 ? 9.003   38.662  -33.985 1.00 29.98  ? 137  TYR A O     1 
ATOM   1031 C CB    . TYR A 1 137 ? 7.956   35.534  -33.600 1.00 37.74  ? 137  TYR A CB    1 
ATOM   1032 C CG    . TYR A 1 137 ? 6.667   36.207  -33.985 1.00 39.12  ? 137  TYR A CG    1 
ATOM   1033 C CD1   . TYR A 1 137 ? 6.059   35.933  -35.197 1.00 40.77  ? 137  TYR A CD1   1 
ATOM   1034 C CD2   . TYR A 1 137 ? 6.076   37.138  -33.154 1.00 37.61  ? 137  TYR A CD2   1 
ATOM   1035 C CE1   . TYR A 1 137 ? 4.874   36.550  -35.557 1.00 45.66  ? 137  TYR A CE1   1 
ATOM   1036 C CE2   . TYR A 1 137 ? 4.886   37.754  -33.492 1.00 43.46  ? 137  TYR A CE2   1 
ATOM   1037 C CZ    . TYR A 1 137 ? 4.282   37.458  -34.699 1.00 45.52  ? 137  TYR A CZ    1 
ATOM   1038 O OH    . TYR A 1 137 ? 3.129   38.087  -35.045 1.00 49.99  ? 137  TYR A OH    1 
ATOM   1039 N N     . LEU A 1 138 ? 9.626   37.636  -32.049 1.00 33.02  ? 138  LEU A N     1 
ATOM   1040 C CA    . LEU A 1 138 ? 9.729   38.879  -31.259 1.00 34.96  ? 138  LEU A CA    1 
ATOM   1041 C C     . LEU A 1 138 ? 10.780  39.755  -31.926 1.00 40.85  ? 138  LEU A C     1 
ATOM   1042 O O     . LEU A 1 138 ? 10.503  40.977  -31.962 1.00 43.56  ? 138  LEU A O     1 
ATOM   1043 C CB    . LEU A 1 138 ? 10.143  38.646  -29.812 1.00 31.61  ? 138  LEU A CB    1 
ATOM   1044 C CG    . LEU A 1 138 ? 9.190   37.823  -28.956 1.00 33.36  ? 138  LEU A CG    1 
ATOM   1045 C CD1   . LEU A 1 138 ? 9.693   37.815  -27.507 1.00 34.81  ? 138  LEU A CD1   1 
ATOM   1046 C CD2   . LEU A 1 138 ? 7.767   38.347  -29.049 1.00 32.98  ? 138  LEU A CD2   1 
ATOM   1047 N N     . GLU A 1 139 ? 11.967  39.231  -32.310 1.00 37.90  ? 139  GLU A N     1 
ATOM   1048 C CA    . GLU A 1 139 ? 13.049  40.067  -32.931 1.00 42.10  ? 139  GLU A CA    1 
ATOM   1049 C C     . GLU A 1 139 ? 12.512  40.772  -34.191 1.00 39.15  ? 139  GLU A C     1 
ATOM   1050 O O     . GLU A 1 139 ? 12.843  41.943  -34.370 1.00 39.73  ? 139  GLU A O     1 
ATOM   1051 C CB    . GLU A 1 139 ? 14.325  39.273  -33.171 1.00 43.19  ? 139  GLU A CB    1 
ATOM   1052 C CG    . GLU A 1 139 ? 15.190  39.212  -31.919 1.00 49.16  ? 139  GLU A CG    1 
ATOM   1053 C CD    . GLU A 1 139 ? 15.600  40.560  -31.332 1.00 51.67  ? 139  GLU A CD    1 
ATOM   1054 O OE1   . GLU A 1 139 ? 15.238  40.831  -30.153 1.00 47.28  ? 139  GLU A OE1   1 
ATOM   1055 O OE2   . GLU A 1 139 ? 16.286  41.335  -32.048 1.00 51.56  ? 139  GLU A OE2   1 
ATOM   1056 N N     . ALA A 1 140 ? 11.609  40.131  -34.931 1.00 37.92  ? 140  ALA A N     1 
ATOM   1057 C CA    . ALA A 1 140 ? 11.115  40.597  -36.248 1.00 41.87  ? 140  ALA A CA    1 
ATOM   1058 C C     . ALA A 1 140 ? 9.892   41.504  -36.068 1.00 43.84  ? 140  ALA A C     1 
ATOM   1059 O O     . ALA A 1 140 ? 9.836   42.510  -36.749 1.00 38.31  ? 140  ALA A O     1 
ATOM   1060 C CB    . ALA A 1 140 ? 10.806  39.412  -37.127 1.00 42.31  ? 140  ALA A CB    1 
ATOM   1061 N N     . HIS A 1 141 ? 9.006   41.169  -35.126 1.00 42.37  ? 141  HIS A N     1 
ATOM   1062 C CA    . HIS A 1 141 ? 7.736   41.863  -34.959 1.00 43.67  ? 141  HIS A CA    1 
ATOM   1063 C C     . HIS A 1 141 ? 7.389   42.575  -33.642 1.00 47.08  ? 141  HIS A C     1 
ATOM   1064 O O     . HIS A 1 141 ? 6.544   43.454  -33.652 1.00 44.80  ? 141  HIS A O     1 
ATOM   1065 C CB    . HIS A 1 141 ? 6.627   40.842  -35.224 1.00 44.67  ? 141  HIS A CB    1 
ATOM   1066 C CG    . HIS A 1 141 ? 6.735   40.139  -36.537 1.00 48.77  ? 141  HIS A CG    1 
ATOM   1067 N ND1   . HIS A 1 141 ? 6.403   40.737  -37.731 1.00 51.92  ? 141  HIS A ND1   1 
ATOM   1068 C CD2   . HIS A 1 141 ? 7.126   38.882  -36.844 1.00 49.94  ? 141  HIS A CD2   1 
ATOM   1069 C CE1   . HIS A 1 141 ? 6.591   39.880  -38.717 1.00 53.19  ? 141  HIS A CE1   1 
ATOM   1070 N NE2   . HIS A 1 141 ? 7.027   38.745  -38.205 1.00 47.10  ? 141  HIS A NE2   1 
ATOM   1071 N N     . ALA A 1 142 ? 7.974   42.171  -32.518 1.00 49.51  ? 142  ALA A N     1 
ATOM   1072 C CA    . ALA A 1 142 ? 7.740   42.845  -31.223 1.00 47.93  ? 142  ALA A CA    1 
ATOM   1073 C C     . ALA A 1 142 ? 9.012   42.969  -30.433 1.00 53.17  ? 142  ALA A C     1 
ATOM   1074 O O     . ALA A 1 142 ? 9.109   42.443  -29.344 1.00 48.15  ? 142  ALA A O     1 
ATOM   1075 C CB    . ALA A 1 142 ? 6.709   42.113  -30.437 1.00 46.53  ? 142  ALA A CB    1 
ATOM   1076 N N     . PRO A 1 143 ? 9.983   43.723  -30.949 1.00 70.26  ? 143  PRO A N     1 
ATOM   1077 C CA    . PRO A 1 143 ? 11.310  43.776  -30.337 1.00 68.37  ? 143  PRO A CA    1 
ATOM   1078 C C     . PRO A 1 143 ? 11.507  44.406  -28.979 1.00 56.58  ? 143  PRO A C     1 
ATOM   1079 O O     . PRO A 1 143 ? 12.614  44.412  -28.518 1.00 67.78  ? 143  PRO A O     1 
ATOM   1080 C CB    . PRO A 1 143 ? 12.097  44.551  -31.381 1.00 77.82  ? 143  PRO A CB    1 
ATOM   1081 C CG    . PRO A 1 143 ? 11.116  45.505  -31.942 1.00 76.71  ? 143  PRO A CG    1 
ATOM   1082 C CD    . PRO A 1 143 ? 9.827   44.751  -31.995 1.00 75.66  ? 143  PRO A CD    1 
ATOM   1083 N N     . SER A 1 144 ? 10.485  44.948  -28.370 1.00 40.65  ? 144  SER A N     1 
ATOM   1084 C CA    . SER A 1 144 ? 10.585  45.509  -27.069 1.00 34.36  ? 144  SER A CA    1 
ATOM   1085 C C     . SER A 1 144 ? 10.441  44.401  -26.069 1.00 31.73  ? 144  SER A C     1 
ATOM   1086 O O     . SER A 1 144 ? 10.706  44.600  -24.926 1.00 30.42  ? 144  SER A O     1 
ATOM   1087 C CB    . SER A 1 144 ? 9.442   46.460  -26.879 1.00 41.97  ? 144  SER A CB    1 
ATOM   1088 O OG    . SER A 1 144 ? 8.261   45.736  -26.863 1.00 33.00  ? 144  SER A OG    1 
ATOM   1089 N N     . LEU A 1 145 ? 9.998   43.242  -26.518 1.00 31.04  ? 145  LEU A N     1 
ATOM   1090 C CA    . LEU A 1 145 ? 9.793   42.113  -25.641 1.00 29.54  ? 145  LEU A CA    1 
ATOM   1091 C C     . LEU A 1 145 ? 10.899  41.061  -25.693 1.00 32.25  ? 145  LEU A C     1 
ATOM   1092 O O     . LEU A 1 145 ? 11.628  40.984  -26.667 1.00 35.12  ? 145  LEU A O     1 
ATOM   1093 C CB    . LEU A 1 145 ? 8.455   41.465  -25.955 1.00 28.29  ? 145  LEU A CB    1 
ATOM   1094 C CG    . LEU A 1 145 ? 7.188   42.308  -25.851 1.00 27.46  ? 145  LEU A CG    1 
ATOM   1095 C CD1   . LEU A 1 145 ? 6.000   41.532  -26.380 1.00 27.80  ? 145  LEU A CD1   1 
ATOM   1096 C CD2   . LEU A 1 145 ? 6.954   42.735  -24.418 1.00 28.07  ? 145  LEU A CD2   1 
ATOM   1097 N N     . MET A 1 146 ? 11.007  40.255  -24.644 1.00 31.37  ? 146  MET A N     1 
ATOM   1098 C CA    . MET A 1 146 ? 12.000  39.165  -24.648 1.00 31.54  ? 146  MET A CA    1 
ATOM   1099 C C     . MET A 1 146 ? 11.349  37.908  -24.060 1.00 32.82  ? 146  MET A C     1 
ATOM   1100 O O     . MET A 1 146 ? 10.417  38.040  -23.246 1.00 28.93  ? 146  MET A O     1 
ATOM   1101 C CB    . MET A 1 146 ? 13.227  39.588  -23.849 1.00 33.03  ? 146  MET A CB    1 
ATOM   1102 C CG    . MET A 1 146 ? 12.899  39.980  -22.428 1.00 35.88  ? 146  MET A CG    1 
ATOM   1103 S SD    . MET A 1 146 ? 14.347  40.625  -21.557 1.00 39.76  ? 146  MET A SD    1 
ATOM   1104 C CE    . MET A 1 146 ? 15.126  39.092  -21.063 1.00 40.55  ? 146  MET A CE    1 
ATOM   1105 N N     . ILE A 1 147 ? 11.840  36.729  -24.447 1.00 30.24  ? 147  ILE A N     1 
ATOM   1106 C CA    . ILE A 1 147 ? 11.359  35.429  -23.895 1.00 29.54  ? 147  ILE A CA    1 
ATOM   1107 C C     . ILE A 1 147 ? 12.093  35.163  -22.580 1.00 30.03  ? 147  ILE A C     1 
ATOM   1108 O O     . ILE A 1 147 ? 13.012  35.914  -22.220 1.00 31.64  ? 147  ILE A O     1 
ATOM   1109 C CB    . ILE A 1 147 ? 11.553  34.273  -24.890 1.00 29.73  ? 147  ILE A CB    1 
ATOM   1110 C CG1   . ILE A 1 147 ? 13.028  33.910  -25.076 1.00 28.92  ? 147  ILE A CG1   1 
ATOM   1111 C CG2   . ILE A 1 147 ? 10.907  34.603  -26.235 1.00 31.56  ? 147  ILE A CG2   1 
ATOM   1112 C CD1   . ILE A 1 147 ? 13.224  32.666  -25.935 1.00 28.27  ? 147  ILE A CD1   1 
ATOM   1113 N N     . ASP A 1 148 ? 11.658  34.141  -21.873 1.00 26.69  ? 148  ASP A N     1 
ATOM   1114 C CA    . ASP A 1 148 ? 12.470  33.514  -20.811 1.00 27.44  ? 148  ASP A CA    1 
ATOM   1115 C C     . ASP A 1 148 ? 12.718  32.073  -21.245 1.00 27.00  ? 148  ASP A C     1 
ATOM   1116 O O     . ASP A 1 148 ? 11.732  31.306  -21.360 1.00 29.63  ? 148  ASP A O     1 
ATOM   1117 C CB    . ASP A 1 148 ? 11.790  33.636  -19.459 1.00 26.04  ? 148  ASP A CB    1 
ATOM   1118 C CG    . ASP A 1 148 ? 12.676  33.051  -18.387 1.00 28.12  ? 148  ASP A CG    1 
ATOM   1119 O OD1   . ASP A 1 148 ? 12.780  31.805  -18.365 1.00 25.92  ? 148  ASP A OD1   1 
ATOM   1120 O OD2   . ASP A 1 148 ? 13.253  33.849  -17.615 1.00 26.65  ? 148  ASP A OD2   1 
ATOM   1121 N N     . CYS A 1 149 ? 13.978  31.728  -21.498 1.00 28.24  ? 149  CYS A N     1 
ATOM   1122 C CA    . CYS A 1 149 ? 14.346  30.392  -22.035 1.00 27.20  ? 149  CYS A CA    1 
ATOM   1123 C C     . CYS A 1 149 ? 15.093  29.605  -20.964 1.00 28.14  ? 149  CYS A C     1 
ATOM   1124 O O     . CYS A 1 149 ? 15.808  30.162  -20.130 1.00 26.97  ? 149  CYS A O     1 
ATOM   1125 C CB    . CYS A 1 149 ? 15.148  30.495  -23.331 1.00 27.46  ? 149  CYS A CB    1 
ATOM   1126 S SG    . CYS A 1 149 ? 16.576  31.604  -23.206 1.00 33.65  ? 149  CYS A SG    1 
ATOM   1127 N N     . PRO A 1 150 ? 14.959  28.263  -21.005 1.00 29.24  ? 150  PRO A N     1 
ATOM   1128 C CA    . PRO A 1 150 ? 15.800  27.378  -20.216 1.00 32.60  ? 150  PRO A CA    1 
ATOM   1129 C C     . PRO A 1 150 ? 17.138  27.305  -20.966 1.00 32.60  ? 150  PRO A C     1 
ATOM   1130 O O     . PRO A 1 150 ? 17.308  28.009  -21.962 1.00 35.11  ? 150  PRO A O     1 
ATOM   1131 C CB    . PRO A 1 150 ? 14.998  26.062  -20.207 1.00 33.57  ? 150  PRO A CB    1 
ATOM   1132 C CG    . PRO A 1 150 ? 14.334  26.053  -21.584 1.00 32.37  ? 150  PRO A CG    1 
ATOM   1133 C CD    . PRO A 1 150 ? 14.052  27.519  -21.890 1.00 31.41  ? 150  PRO A CD    1 
ATOM   1134 N N     . ASP A 1 151 ? 18.061  26.486  -20.480 1.00 32.87  ? 151  ASP A N     1 
ATOM   1135 C CA    . ASP A 1 151 ? 19.444  26.409  -21.025 1.00 36.48  ? 151  ASP A CA    1 
ATOM   1136 C C     . ASP A 1 151 ? 19.422  26.188  -22.545 1.00 34.43  ? 151  ASP A C     1 
ATOM   1137 O O     . ASP A 1 151 ? 20.275  26.778  -23.207 1.00 33.80  ? 151  ASP A O     1 
ATOM   1138 C CB    . ASP A 1 151 ? 20.257  25.316  -20.339 1.00 35.21  ? 151  ASP A CB    1 
ATOM   1139 C CG    . ASP A 1 151 ? 20.563  25.608  -18.876 1.00 41.86  ? 151  ASP A CG    1 
ATOM   1140 O OD1   . ASP A 1 151 ? 20.565  26.799  -18.483 1.00 37.07  ? 151  ASP A OD1   1 
ATOM   1141 O OD2   . ASP A 1 151 ? 20.803  24.637  -18.140 1.00 52.12  ? 151  ASP A OD2   1 
ATOM   1142 N N     . LEU A 1 152 ? 18.477  25.418  -23.093 1.00 36.91  ? 152  LEU A N     1 
ATOM   1143 C CA    . LEU A 1 152 ? 18.612  24.893  -24.486 1.00 39.94  ? 152  LEU A CA    1 
ATOM   1144 C C     . LEU A 1 152 ? 17.730  25.605  -25.523 1.00 44.32  ? 152  LEU A C     1 
ATOM   1145 O O     . LEU A 1 152 ? 18.263  25.953  -26.590 1.00 55.74  ? 152  LEU A O     1 
ATOM   1146 C CB    . LEU A 1 152 ? 18.388  23.383  -24.469 1.00 38.26  ? 152  LEU A CB    1 
ATOM   1147 C CG    . LEU A 1 152 ? 19.497  22.638  -23.725 1.00 40.69  ? 152  LEU A CG    1 
ATOM   1148 C CD1   . LEU A 1 152 ? 19.264  21.139  -23.755 1.00 41.27  ? 152  LEU A CD1   1 
ATOM   1149 C CD2   . LEU A 1 152 ? 20.873  22.991  -24.294 1.00 40.58  ? 152  LEU A CD2   1 
ATOM   1150 N N     . GLY A 1 153 ? 16.438  25.783  -25.332 1.00 44.29  ? 153  GLY A N     1 
ATOM   1151 C CA    . GLY A 1 153 ? 15.740  26.648  -26.319 1.00 46.43  ? 153  GLY A CA    1 
ATOM   1152 C C     . GLY A 1 153 ? 15.306  25.963  -27.618 1.00 36.62  ? 153  GLY A C     1 
ATOM   1153 O O     . GLY A 1 153 ? 14.516  26.589  -28.351 1.00 34.12  ? 153  GLY A O     1 
ATOM   1154 N N     . TRP A 1 154 ? 15.701  24.710  -27.894 1.00 32.31  ? 154  TRP A N     1 
ATOM   1155 C CA    . TRP A 1 154 ? 15.001  23.879  -28.918 1.00 31.77  ? 154  TRP A CA    1 
ATOM   1156 C C     . TRP A 1 154 ? 13.707  23.307  -28.338 1.00 28.16  ? 154  TRP A C     1 
ATOM   1157 O O     . TRP A 1 154 ? 12.996  22.660  -29.080 1.00 26.67  ? 154  TRP A O     1 
ATOM   1158 C CB    . TRP A 1 154 ? 15.869  22.759  -29.535 1.00 35.12  ? 154  TRP A CB    1 
ATOM   1159 C CG    . TRP A 1 154 ? 16.469  21.773  -28.579 1.00 35.54  ? 154  TRP A CG    1 
ATOM   1160 C CD1   . TRP A 1 154 ? 16.105  21.524  -27.286 1.00 36.50  ? 154  TRP A CD1   1 
ATOM   1161 C CD2   . TRP A 1 154 ? 17.533  20.850  -28.879 1.00 36.69  ? 154  TRP A CD2   1 
ATOM   1162 N NE1   . TRP A 1 154 ? 16.914  20.563  -26.736 1.00 35.15  ? 154  TRP A NE1   1 
ATOM   1163 C CE2   . TRP A 1 154 ? 17.791  20.119  -27.696 1.00 39.53  ? 154  TRP A CE2   1 
ATOM   1164 C CE3   . TRP A 1 154 ? 18.325  20.612  -30.009 1.00 37.65  ? 154  TRP A CE3   1 
ATOM   1165 C CZ2   . TRP A 1 154 ? 18.781  19.133  -27.632 1.00 39.05  ? 154  TRP A CZ2   1 
ATOM   1166 C CZ3   . TRP A 1 154 ? 19.314  19.650  -29.938 1.00 40.39  ? 154  TRP A CZ3   1 
ATOM   1167 C CH2   . TRP A 1 154 ? 19.541  18.930  -28.765 1.00 39.31  ? 154  TRP A CH2   1 
ATOM   1168 N N     . GLY A 1 155 ? 13.414  23.526  -27.054 1.00 24.75  ? 155  GLY A N     1 
ATOM   1169 C CA    . GLY A 1 155 ? 12.169  23.025  -26.458 1.00 28.27  ? 155  GLY A CA    1 
ATOM   1170 C C     . GLY A 1 155 ? 10.973  23.921  -26.749 1.00 25.97  ? 155  GLY A C     1 
ATOM   1171 O O     . GLY A 1 155 ? 11.114  24.919  -27.480 1.00 28.86  ? 155  GLY A O     1 
ATOM   1172 N N     . SER A 1 156 ? 9.820   23.570  -26.195 1.00 25.34  ? 156  SER A N     1 
ATOM   1173 C CA    . SER A 1 156 ? 8.517   24.246  -26.452 1.00 25.12  ? 156  SER A CA    1 
ATOM   1174 C C     . SER A 1 156 ? 8.235   25.211  -25.301 1.00 25.01  ? 156  SER A C     1 
ATOM   1175 O O     . SER A 1 156 ? 8.278   24.798  -24.139 1.00 25.69  ? 156  SER A O     1 
ATOM   1176 C CB    . SER A 1 156 ? 7.395   23.246  -26.647 1.00 25.35  ? 156  SER A CB    1 
ATOM   1177 O OG    . SER A 1 156 ? 6.096   23.834  -26.482 1.00 26.83  ? 156  SER A OG    1 
ATOM   1178 N N     . VAL A 1 157 ? 7.881   26.442  -25.637 1.00 25.97  ? 157  VAL A N     1 
ATOM   1179 C CA    . VAL A 1 157 ? 7.430   27.447  -24.636 1.00 27.54  ? 157  VAL A CA    1 
ATOM   1180 C C     . VAL A 1 157 ? 6.259   26.867  -23.846 1.00 27.10  ? 157  VAL A C     1 
ATOM   1181 O O     . VAL A 1 157 ? 6.206   27.089  -22.616 1.00 26.10  ? 157  VAL A O     1 
ATOM   1182 C CB    . VAL A 1 157 ? 7.046   28.781  -25.281 1.00 25.66  ? 157  VAL A CB    1 
ATOM   1183 C CG1   . VAL A 1 157 ? 6.679   29.799  -24.221 1.00 25.20  ? 157  VAL A CG1   1 
ATOM   1184 C CG2   . VAL A 1 157 ? 8.135   29.292  -26.201 1.00 27.61  ? 157  VAL A CG2   1 
ATOM   1185 N N     . VAL A 1 158 ? 5.360   26.159  -24.532 1.00 25.73  ? 158  VAL A N     1 
ATOM   1186 C CA    . VAL A 1 158 ? 4.200   25.463  -23.917 1.00 24.39  ? 158  VAL A CA    1 
ATOM   1187 C C     . VAL A 1 158 ? 4.684   24.232  -23.155 1.00 23.49  ? 158  VAL A C     1 
ATOM   1188 O O     . VAL A 1 158 ? 4.461   24.184  -21.942 1.00 25.33  ? 158  VAL A O     1 
ATOM   1189 C CB    . VAL A 1 158 ? 3.166   25.059  -24.971 1.00 26.41  ? 158  VAL A CB    1 
ATOM   1190 C CG1   . VAL A 1 158 ? 2.099   24.157  -24.370 1.00 25.36  ? 158  VAL A CG1   1 
ATOM   1191 C CG2   . VAL A 1 158 ? 2.568   26.288  -25.643 1.00 30.98  ? 158  VAL A CG2   1 
ATOM   1192 N N     . GLY A 1 159 ? 5.324   23.292  -23.843 1.00 23.30  ? 159  GLY A N     1 
ATOM   1193 C CA    . GLY A 1 159 ? 5.783   22.007  -23.258 1.00 23.47  ? 159  GLY A CA    1 
ATOM   1194 C C     . GLY A 1 159 ? 6.572   22.218  -21.973 1.00 22.75  ? 159  GLY A C     1 
ATOM   1195 O O     . GLY A 1 159 ? 6.271   21.542  -20.965 1.00 21.64  ? 159  GLY A O     1 
ATOM   1196 N N     . ASN A 1 160 ? 7.547   23.139  -21.991 1.00 24.59  ? 160  ASN A N     1 
ATOM   1197 C CA    . ASN A 1 160 ? 8.383   23.423  -20.802 1.00 27.52  ? 160  ASN A CA    1 
ATOM   1198 C C     . ASN A 1 160 ? 7.491   23.908  -19.656 1.00 28.30  ? 160  ASN A C     1 
ATOM   1199 O O     . ASN A 1 160 ? 7.659   23.352  -18.523 1.00 28.05  ? 160  ASN A O     1 
ATOM   1200 C CB    . ASN A 1 160 ? 9.556   24.375  -21.090 1.00 28.39  ? 160  ASN A CB    1 
ATOM   1201 C CG    . ASN A 1 160 ? 10.417  24.609  -19.869 1.00 29.14  ? 160  ASN A CG    1 
ATOM   1202 O OD1   . ASN A 1 160 ? 10.022  25.304  -18.918 1.00 32.42  ? 160  ASN A OD1   1 
ATOM   1203 N ND2   . ASN A 1 160 ? 11.588  24.016  -19.877 1.00 27.18  ? 160  ASN A ND2   1 
ATOM   1204 N N     . ALA A 1 161 ? 6.582   24.864  -19.909 1.00 27.93  ? 161  ALA A N     1 
ATOM   1205 C CA    . ALA A 1 161 ? 5.685   25.445  -18.878 1.00 24.92  ? 161  ALA A CA    1 
ATOM   1206 C C     . ALA A 1 161 ? 4.796   24.361  -18.273 1.00 27.93  ? 161  ALA A C     1 
ATOM   1207 O O     . ALA A 1 161 ? 4.515   24.410  -17.038 1.00 27.44  ? 161  ALA A O     1 
ATOM   1208 C CB    . ALA A 1 161 ? 4.854   26.568  -19.435 1.00 27.53  ? 161  ALA A CB    1 
ATOM   1209 N N     . LEU A 1 162 ? 4.352   23.418  -19.098 1.00 25.68  ? 162  LEU A N     1 
ATOM   1210 C CA    . LEU A 1 162 ? 3.488   22.305  -18.653 1.00 26.38  ? 162  LEU A CA    1 
ATOM   1211 C C     . LEU A 1 162 ? 4.274   21.286  -17.818 1.00 26.59  ? 162  LEU A C     1 
ATOM   1212 O O     . LEU A 1 162 ? 3.619   20.566  -17.067 1.00 31.51  ? 162  LEU A O     1 
ATOM   1213 C CB    . LEU A 1 162 ? 2.838   21.644  -19.873 1.00 27.23  ? 162  LEU A CB    1 
ATOM   1214 C CG    . LEU A 1 162 ? 1.867   22.525  -20.667 1.00 27.61  ? 162  LEU A CG    1 
ATOM   1215 C CD1   . LEU A 1 162 ? 1.255   21.747  -21.816 1.00 26.22  ? 162  LEU A CD1   1 
ATOM   1216 C CD2   . LEU A 1 162 ? 0.778   23.105  -19.767 1.00 25.32  ? 162  LEU A CD2   1 
ATOM   1217 N N     . ASP A 1 163 ? 5.608   21.212  -17.896 1.00 27.40  ? 163  ASP A N     1 
ATOM   1218 C CA    . ASP A 1 163 ? 6.365   20.379  -16.924 1.00 26.03  ? 163  ASP A CA    1 
ATOM   1219 C C     . ASP A 1 163 ? 6.861   21.271  -15.784 1.00 27.60  ? 163  ASP A C     1 
ATOM   1220 O O     . ASP A 1 163 ? 7.643   20.790  -14.963 1.00 29.33  ? 163  ASP A O     1 
ATOM   1221 C CB    . ASP A 1 163 ? 7.456   19.546  -17.599 1.00 29.16  ? 163  ASP A CB    1 
ATOM   1222 C CG    . ASP A 1 163 ? 7.527   18.104  -17.091 1.00 28.68  ? 163  ASP A CG    1 
ATOM   1223 O OD1   . ASP A 1 163 ? 6.450   17.551  -16.722 1.00 24.73  ? 163  ASP A OD1   1 
ATOM   1224 O OD2   . ASP A 1 163 ? 8.676   17.544  -17.017 1.00 30.73  ? 163  ASP A OD2   1 
ATOM   1225 N N     . ARG A 1 164 ? 6.390   22.518  -15.729 1.00 26.09  ? 164  ARG A N     1 
ATOM   1226 C CA    . ARG A 1 164 ? 6.801   23.557  -14.757 1.00 26.65  ? 164  ARG A CA    1 
ATOM   1227 C C     . ARG A 1 164 ? 8.320   23.729  -14.791 1.00 25.85  ? 164  ARG A C     1 
ATOM   1228 O O     . ARG A 1 164 ? 8.934   23.840  -13.721 1.00 26.43  ? 164  ARG A O     1 
ATOM   1229 C CB    . ARG A 1 164 ? 6.250   23.226  -13.366 1.00 27.96  ? 164  ARG A CB    1 
ATOM   1230 C CG    . ARG A 1 164 ? 4.752   23.471  -13.240 1.00 29.42  ? 164  ARG A CG    1 
ATOM   1231 C CD    . ARG A 1 164 ? 4.317   23.717  -11.793 1.00 31.26  ? 164  ARG A CD    1 
ATOM   1232 N NE    . ARG A 1 164 ? 4.603   22.579  -10.911 1.00 30.77  ? 164  ARG A NE    1 
ATOM   1233 C CZ    . ARG A 1 164 ? 3.871   21.470  -10.798 1.00 29.46  ? 164  ARG A CZ    1 
ATOM   1234 N NH1   . ARG A 1 164 ? 2.750   21.308  -11.479 1.00 30.66  ? 164  ARG A NH1   1 
ATOM   1235 N NH2   . ARG A 1 164 ? 4.253   20.508  -9.976  1.00 32.13  ? 164  ARG A NH2   1 
ATOM   1236 N N     . GLY A 1 165 ? 8.889   23.832  -15.989 1.00 23.79  ? 165  GLY A N     1 
ATOM   1237 C CA    . GLY A 1 165 ? 10.296  24.200  -16.220 1.00 26.62  ? 165  GLY A CA    1 
ATOM   1238 C C     . GLY A 1 165 ? 10.578  25.639  -15.825 1.00 27.40  ? 165  GLY A C     1 
ATOM   1239 O O     . GLY A 1 165 ? 9.659   26.335  -15.373 1.00 25.79  ? 165  GLY A O     1 
ATOM   1240 N N     . ALA A 1 166 ? 11.822  26.077  -15.984 1.00 28.89  ? 166  ALA A N     1 
ATOM   1241 C CA    . ALA A 1 166 ? 12.252  27.429  -15.569 1.00 30.84  ? 166  ALA A CA    1 
ATOM   1242 C C     . ALA A 1 166 ? 13.394  27.919  -16.452 1.00 28.39  ? 166  ALA A C     1 
ATOM   1243 O O     . ALA A 1 166 ? 14.100  27.088  -17.079 1.00 27.81  ? 166  ALA A O     1 
ATOM   1244 C CB    . ALA A 1 166 ? 12.659  27.428  -14.103 1.00 32.38  ? 166  ALA A CB    1 
ATOM   1245 N N     . GLY A 1 167 ? 13.510  29.241  -16.525 1.00 27.51  ? 167  GLY A N     1 
ATOM   1246 C CA    . GLY A 1 167 ? 14.672  29.968  -17.076 1.00 29.87  ? 167  GLY A CA    1 
ATOM   1247 C C     . GLY A 1 167 ? 15.200  30.935  -16.040 1.00 26.23  ? 167  GLY A C     1 
ATOM   1248 O O     . GLY A 1 167 ? 14.945  30.703  -14.847 1.00 25.12  ? 167  GLY A O     1 
ATOM   1249 N N     . TYR A 1 168 ? 15.946  31.954  -16.453 1.00 29.55  ? 168  TYR A N     1 
ATOM   1250 C CA    . TYR A 1 168 ? 16.885  32.655  -15.537 1.00 29.32  ? 168  TYR A CA    1 
ATOM   1251 C C     . TYR A 1 168 ? 16.681  34.175  -15.561 1.00 29.73  ? 168  TYR A C     1 
ATOM   1252 O O     . TYR A 1 168 ? 17.284  34.834  -14.720 1.00 34.98  ? 168  TYR A O     1 
ATOM   1253 C CB    . TYR A 1 168 ? 18.292  32.143  -15.846 1.00 30.36  ? 168  TYR A CB    1 
ATOM   1254 C CG    . TYR A 1 168 ? 18.390  30.643  -15.700 1.00 29.29  ? 168  TYR A CG    1 
ATOM   1255 C CD1   . TYR A 1 168 ? 18.674  30.030  -14.488 1.00 31.34  ? 168  TYR A CD1   1 
ATOM   1256 C CD2   . TYR A 1 168 ? 18.179  29.835  -16.796 1.00 30.74  ? 168  TYR A CD2   1 
ATOM   1257 C CE1   . TYR A 1 168 ? 18.741  28.645  -14.378 1.00 32.07  ? 168  TYR A CE1   1 
ATOM   1258 C CE2   . TYR A 1 168 ? 18.237  28.461  -16.703 1.00 31.69  ? 168  TYR A CE2   1 
ATOM   1259 C CZ    . TYR A 1 168 ? 18.504  27.860  -15.494 1.00 32.67  ? 168  TYR A CZ    1 
ATOM   1260 O OH    . TYR A 1 168 ? 18.493  26.491  -15.474 1.00 36.89  ? 168  TYR A OH    1 
ATOM   1261 N N     . THR A 1 169 ? 15.812  34.707  -16.422 1.00 29.50  ? 169  THR A N     1 
ATOM   1262 C CA    . THR A 1 169 ? 15.388  36.130  -16.378 1.00 30.23  ? 169  THR A CA    1 
ATOM   1263 C C     . THR A 1 169 ? 14.441  36.308  -15.192 1.00 30.71  ? 169  THR A C     1 
ATOM   1264 O O     . THR A 1 169 ? 14.083  35.343  -14.511 1.00 30.36  ? 169  THR A O     1 
ATOM   1265 C CB    . THR A 1 169 ? 14.711  36.598  -17.671 1.00 29.34  ? 169  THR A CB    1 
ATOM   1266 O OG1   . THR A 1 169 ? 13.315  36.300  -17.577 1.00 28.11  ? 169  THR A OG1   1 
ATOM   1267 C CG2   . THR A 1 169 ? 15.308  35.990  -18.919 1.00 30.85  ? 169  THR A CG2   1 
ATOM   1268 N N     . PRO A 1 170 ? 14.013  37.554  -14.897 1.00 32.11  ? 170  PRO A N     1 
ATOM   1269 C CA    . PRO A 1 170 ? 12.968  37.771  -13.903 1.00 31.70  ? 170  PRO A CA    1 
ATOM   1270 C C     . PRO A 1 170 ? 11.670  36.986  -14.188 1.00 27.53  ? 170  PRO A C     1 
ATOM   1271 O O     . PRO A 1 170 ? 10.952  36.749  -13.278 1.00 30.25  ? 170  PRO A O     1 
ATOM   1272 C CB    . PRO A 1 170 ? 12.793  39.289  -13.990 1.00 31.85  ? 170  PRO A CB    1 
ATOM   1273 C CG    . PRO A 1 170 ? 14.161  39.763  -14.332 1.00 33.03  ? 170  PRO A CG    1 
ATOM   1274 C CD    . PRO A 1 170 ? 14.553  38.816  -15.442 1.00 32.76  ? 170  PRO A CD    1 
ATOM   1275 N N     . TYR A 1 171 ? 11.427  36.547  -15.423 1.00 26.84  ? 171  TYR A N     1 
ATOM   1276 C CA    . TYR A 1 171 ? 10.241  35.718  -15.776 1.00 28.73  ? 171  TYR A CA    1 
ATOM   1277 C C     . TYR A 1 171 ? 10.602  34.222  -15.790 1.00 28.55  ? 171  TYR A C     1 
ATOM   1278 O O     . TYR A 1 171 ? 9.929   33.449  -16.490 1.00 26.79  ? 171  TYR A O     1 
ATOM   1279 C CB    . TYR A 1 171 ? 9.639   36.194  -17.104 1.00 30.37  ? 171  TYR A CB    1 
ATOM   1280 C CG    . TYR A 1 171 ? 8.674   37.349  -16.991 1.00 28.35  ? 171  TYR A CG    1 
ATOM   1281 C CD1   . TYR A 1 171 ? 8.872   38.389  -16.094 1.00 30.82  ? 171  TYR A CD1   1 
ATOM   1282 C CD2   . TYR A 1 171 ? 7.550   37.410  -17.804 1.00 29.04  ? 171  TYR A CD2   1 
ATOM   1283 C CE1   . TYR A 1 171 ? 7.982   39.448  -15.999 1.00 30.41  ? 171  TYR A CE1   1 
ATOM   1284 C CE2   . TYR A 1 171 ? 6.670   38.482  -17.752 1.00 29.55  ? 171  TYR A CE2   1 
ATOM   1285 C CZ    . TYR A 1 171 ? 6.866   39.488  -16.828 1.00 29.66  ? 171  TYR A CZ    1 
ATOM   1286 O OH    . TYR A 1 171 ? 5.982   40.537  -16.763 1.00 32.59  ? 171  TYR A OH    1 
ATOM   1287 N N     . GLY A 1 172 ? 11.554  33.802  -14.951 1.00 28.14  ? 172  GLY A N     1 
ATOM   1288 C CA    . GLY A 1 172 ? 12.125  32.435  -14.935 1.00 27.73  ? 172  GLY A CA    1 
ATOM   1289 C C     . GLY A 1 172 ? 11.124  31.338  -14.623 1.00 25.75  ? 172  GLY A C     1 
ATOM   1290 O O     . GLY A 1 172 ? 11.269  30.259  -15.183 1.00 29.36  ? 172  GLY A O     1 
ATOM   1291 N N     . ASP A 1 173 ? 10.145  31.592  -13.755 1.00 26.35  ? 173  ASP A N     1 
ATOM   1292 C CA    . ASP A 1 173 ? 9.101   30.618  -13.354 1.00 26.70  ? 173  ASP A CA    1 
ATOM   1293 C C     . ASP A 1 173 ? 8.082   30.577  -14.495 1.00 24.98  ? 173  ASP A C     1 
ATOM   1294 O O     . ASP A 1 173 ? 7.214   31.440  -14.525 1.00 27.53  ? 173  ASP A O     1 
ATOM   1295 C CB    . ASP A 1 173 ? 8.459   31.005  -12.021 1.00 26.64  ? 173  ASP A CB    1 
ATOM   1296 C CG    . ASP A 1 173 ? 7.421   30.004  -11.525 1.00 30.87  ? 173  ASP A CG    1 
ATOM   1297 O OD1   . ASP A 1 173 ? 7.039   29.104  -12.310 1.00 29.55  ? 173  ASP A OD1   1 
ATOM   1298 O OD2   . ASP A 1 173 ? 7.016   30.110  -10.355 1.00 28.40  ? 173  ASP A OD2   1 
ATOM   1299 N N     . HIS A 1 174 ? 8.211   29.631  -15.417 1.00 23.33  ? 174  HIS A N     1 
ATOM   1300 C CA    . HIS A 1 174 ? 7.383   29.570  -16.654 1.00 26.44  ? 174  HIS A CA    1 
ATOM   1301 C C     . HIS A 1 174 ? 5.899   29.379  -16.312 1.00 25.43  ? 174  HIS A C     1 
ATOM   1302 O O     . HIS A 1 174 ? 5.040   30.074  -16.903 1.00 24.37  ? 174  HIS A O     1 
ATOM   1303 C CB    . HIS A 1 174 ? 7.912   28.482  -17.598 1.00 25.34  ? 174  HIS A CB    1 
ATOM   1304 C CG    . HIS A 1 174 ? 9.259   28.837  -18.095 1.00 26.16  ? 174  HIS A CG    1 
ATOM   1305 N ND1   . HIS A 1 174 ? 10.081  27.937  -18.749 1.00 26.93  ? 174  HIS A ND1   1 
ATOM   1306 C CD2   . HIS A 1 174 ? 9.930   30.010  -18.032 1.00 27.74  ? 174  HIS A CD2   1 
ATOM   1307 C CE1   . HIS A 1 174 ? 11.199  28.565  -19.095 1.00 26.14  ? 174  HIS A CE1   1 
ATOM   1308 N NE2   . HIS A 1 174 ? 11.132  29.825  -18.657 1.00 27.95  ? 174  HIS A NE2   1 
ATOM   1309 N N     . PHE A 1 175 ? 5.571   28.506  -15.367 1.00 25.53  ? 175  PHE A N     1 
ATOM   1310 C CA    . PHE A 1 175 ? 4.147   28.293  -15.016 1.00 25.94  ? 175  PHE A CA    1 
ATOM   1311 C C     . PHE A 1 175 ? 3.510   29.582  -14.477 1.00 26.71  ? 175  PHE A C     1 
ATOM   1312 O O     . PHE A 1 175 ? 2.359   29.893  -14.881 1.00 25.02  ? 175  PHE A O     1 
ATOM   1313 C CB    . PHE A 1 175 ? 3.969   27.163  -14.013 1.00 28.36  ? 175  PHE A CB    1 
ATOM   1314 C CG    . PHE A 1 175 ? 2.550   27.088  -13.536 1.00 30.34  ? 175  PHE A CG    1 
ATOM   1315 C CD1   . PHE A 1 175 ? 1.554   26.668  -14.392 1.00 30.63  ? 175  PHE A CD1   1 
ATOM   1316 C CD2   . PHE A 1 175 ? 2.190   27.555  -12.282 1.00 31.54  ? 175  PHE A CD2   1 
ATOM   1317 C CE1   . PHE A 1 175 ? 0.232   26.622  -13.966 1.00 31.84  ? 175  PHE A CE1   1 
ATOM   1318 C CE2   . PHE A 1 175 ? 0.869   27.516  -11.869 1.00 32.64  ? 175  PHE A CE2   1 
ATOM   1319 C CZ    . PHE A 1 175 ? -0.106  27.046  -12.707 1.00 29.12  ? 175  PHE A CZ    1 
ATOM   1320 N N     . MET A 1 176 ? 4.216   30.307  -13.605 1.00 26.97  ? 176  MET A N     1 
ATOM   1321 C CA    . MET A 1 176 ? 3.758   31.611  -13.047 1.00 30.75  ? 176  MET A CA    1 
ATOM   1322 C C     . MET A 1 176 ? 3.261   32.511  -14.191 1.00 26.28  ? 176  MET A C     1 
ATOM   1323 O O     . MET A 1 176 ? 2.166   33.013  -14.087 1.00 31.15  ? 176  MET A O     1 
ATOM   1324 C CB    . MET A 1 176 ? 4.895   32.321  -12.317 1.00 31.72  ? 176  MET A CB    1 
ATOM   1325 C CG    . MET A 1 176 ? 4.563   33.749  -11.890 1.00 36.77  ? 176  MET A CG    1 
ATOM   1326 S SD    . MET A 1 176 ? 5.874   34.446  -10.846 1.00 43.57  ? 176  MET A SD    1 
ATOM   1327 C CE    . MET A 1 176 ? 5.638   33.449  -9.372  1.00 41.82  ? 176  MET A CE    1 
ATOM   1328 N N     . TRP A 1 177 ? 4.052   32.674  -15.251 1.00 24.90  ? 177  TRP A N     1 
ATOM   1329 C CA    . TRP A 1 177 ? 3.766   33.630  -16.353 1.00 26.59  ? 177  TRP A CA    1 
ATOM   1330 C C     . TRP A 1 177 ? 2.826   32.995  -17.391 1.00 26.56  ? 177  TRP A C     1 
ATOM   1331 O O     . TRP A 1 177 ? 2.279   33.720  -18.219 1.00 26.22  ? 177  TRP A O     1 
ATOM   1332 C CB    . TRP A 1 177 ? 5.080   34.209  -16.900 1.00 27.83  ? 177  TRP A CB    1 
ATOM   1333 C CG    . TRP A 1 177 ? 5.828   34.901  -15.800 1.00 30.00  ? 177  TRP A CG    1 
ATOM   1334 C CD1   . TRP A 1 177 ? 6.945   34.442  -15.151 1.00 30.39  ? 177  TRP A CD1   1 
ATOM   1335 C CD2   . TRP A 1 177 ? 5.433   36.103  -15.114 1.00 29.71  ? 177  TRP A CD2   1 
ATOM   1336 N NE1   . TRP A 1 177 ? 7.294   35.289  -14.137 1.00 31.03  ? 177  TRP A NE1   1 
ATOM   1337 C CE2   . TRP A 1 177 ? 6.371   36.307  -14.071 1.00 33.18  ? 177  TRP A CE2   1 
ATOM   1338 C CE3   . TRP A 1 177 ? 4.380   37.010  -15.245 1.00 28.55  ? 177  TRP A CE3   1 
ATOM   1339 C CZ2   . TRP A 1 177 ? 6.287   37.398  -13.201 1.00 30.82  ? 177  TRP A CZ2   1 
ATOM   1340 C CZ3   . TRP A 1 177 ? 4.314   38.095  -14.399 1.00 28.59  ? 177  TRP A CZ3   1 
ATOM   1341 C CH2   . TRP A 1 177 ? 5.269   38.301  -13.411 1.00 31.03  ? 177  TRP A CH2   1 
ATOM   1342 N N     . GLN A 1 178 ? 2.572   31.699  -17.299 1.00 27.31  ? 178  GLN A N     1 
ATOM   1343 C CA    . GLN A 1 178 ? 1.516   31.078  -18.118 1.00 28.59  ? 178  GLN A CA    1 
ATOM   1344 C C     . GLN A 1 178 ? 0.202   31.777  -17.746 1.00 25.01  ? 178  GLN A C     1 
ATOM   1345 O O     . GLN A 1 178 ? -0.089  31.930  -16.548 1.00 21.98  ? 178  GLN A O     1 
ATOM   1346 C CB    . GLN A 1 178 ? 1.477   29.565  -17.922 1.00 28.03  ? 178  GLN A CB    1 
ATOM   1347 C CG    . GLN A 1 178 ? 0.345   28.893  -18.687 1.00 30.16  ? 178  GLN A CG    1 
ATOM   1348 C CD    . GLN A 1 178 ? -0.903  28.722  -17.867 1.00 28.15  ? 178  GLN A CD    1 
ATOM   1349 O OE1   . GLN A 1 178 ? -0.814  28.504  -16.664 1.00 25.97  ? 178  GLN A OE1   1 
ATOM   1350 N NE2   . GLN A 1 178 ? -2.060  28.766  -18.530 1.00 26.06  ? 178  GLN A NE2   1 
ATOM   1351 N N     . THR A 1 179 ? -0.535  32.221  -18.753 1.00 23.29  ? 179  THR A N     1 
ATOM   1352 C CA    . THR A 1 179 ? -1.796  32.967  -18.588 1.00 23.78  ? 179  THR A CA    1 
ATOM   1353 C C     . THR A 1 179 ? -2.781  32.453  -19.633 1.00 24.72  ? 179  THR A C     1 
ATOM   1354 O O     . THR A 1 179 ? -2.620  32.812  -20.806 1.00 23.30  ? 179  THR A O     1 
ATOM   1355 C CB    . THR A 1 179 ? -1.559  34.483  -18.630 1.00 25.25  ? 179  THR A CB    1 
ATOM   1356 O OG1   . THR A 1 179 ? -0.353  34.798  -17.914 1.00 27.52  ? 179  THR A OG1   1 
ATOM   1357 C CG2   . THR A 1 179 ? -2.710  35.236  -18.015 1.00 25.37  ? 179  THR A CG2   1 
ATOM   1358 N N     . GLY A 1 180 ? -3.737  31.646  -19.176 1.00 25.22  ? 180  GLY A N     1 
ATOM   1359 C CA    . GLY A 1 180 ? -4.807  31.034  -19.982 1.00 26.22  ? 180  GLY A CA    1 
ATOM   1360 C C     . GLY A 1 180 ? -4.342  29.806  -20.737 1.00 24.83  ? 180  GLY A C     1 
ATOM   1361 O O     . GLY A 1 180 ? -3.151  29.751  -21.196 1.00 24.36  ? 180  GLY A O     1 
ATOM   1362 N N     . MET A 1 181 ? -5.260  28.853  -20.855 1.00 25.05  ? 181  MET A N     1 
ATOM   1363 C CA    . MET A 1 181 ? -5.098  27.608  -21.650 1.00 29.50  ? 181  MET A CA    1 
ATOM   1364 C C     . MET A 1 181 ? -6.371  27.270  -22.388 1.00 23.80  ? 181  MET A C     1 
ATOM   1365 O O     . MET A 1 181 ? -7.442  27.415  -21.770 1.00 26.91  ? 181  MET A O     1 
ATOM   1366 C CB    . MET A 1 181 ? -5.035  26.393  -20.737 1.00 32.60  ? 181  MET A CB    1 
ATOM   1367 C CG    . MET A 1 181 ? -3.775  26.033  -20.321 1.00 36.29  ? 181  MET A CG    1 
ATOM   1368 S SD    . MET A 1 181 ? -4.065  24.633  -19.232 1.00 33.29  ? 181  MET A SD    1 
ATOM   1369 C CE    . MET A 1 181 ? -2.446  24.806  -18.495 1.00 31.78  ? 181  MET A CE    1 
ATOM   1370 N N     . GLU A 1 182 ? -6.189  26.615  -23.523 1.00 24.98  ? 182  GLU A N     1 
ATOM   1371 C CA    . GLU A 1 182 ? -7.175  25.731  -24.182 1.00 22.70  ? 182  GLU A CA    1 
ATOM   1372 C C     . GLU A 1 182 ? -6.698  24.290  -24.016 1.00 22.59  ? 182  GLU A C     1 
ATOM   1373 O O     . GLU A 1 182 ? -5.520  23.984  -24.346 1.00 27.17  ? 182  GLU A O     1 
ATOM   1374 C CB    . GLU A 1 182 ? -7.325  26.084  -25.661 1.00 22.71  ? 182  GLU A CB    1 
ATOM   1375 C CG    . GLU A 1 182 ? -8.477  25.347  -26.305 1.00 23.99  ? 182  GLU A CG    1 
ATOM   1376 C CD    . GLU A 1 182 ? -8.590  25.725  -27.762 1.00 27.10  ? 182  GLU A CD    1 
ATOM   1377 O OE1   . GLU A 1 182 ? -7.851  25.130  -28.592 1.00 25.60  ? 182  GLU A OE1   1 
ATOM   1378 O OE2   . GLU A 1 182 ? -9.333  26.680  -28.039 1.00 29.71  ? 182  GLU A OE2   1 
ATOM   1379 N N     . VAL A 1 183 ? -7.554  23.444  -23.464 1.00 22.48  ? 183  VAL A N     1 
ATOM   1380 C CA    . VAL A 1 183 ? -7.182  22.049  -23.141 1.00 24.87  ? 183  VAL A CA    1 
ATOM   1381 C C     . VAL A 1 183 ? -8.311  21.105  -23.554 1.00 23.19  ? 183  VAL A C     1 
ATOM   1382 O O     . VAL A 1 183 ? -9.488  21.406  -23.319 1.00 25.52  ? 183  VAL A O     1 
ATOM   1383 C CB    . VAL A 1 183 ? -6.812  21.919  -21.649 1.00 27.13  ? 183  VAL A CB    1 
ATOM   1384 C CG1   . VAL A 1 183 ? -7.949  22.361  -20.749 1.00 25.93  ? 183  VAL A CG1   1 
ATOM   1385 C CG2   . VAL A 1 183 ? -6.348  20.495  -21.333 1.00 27.74  ? 183  VAL A CG2   1 
ATOM   1386 N N     . VAL A 1 184 ? -7.935  20.016  -24.207 1.00 23.27  ? 184  VAL A N     1 
ATOM   1387 C CA    . VAL A 1 184 ? -8.853  18.900  -24.529 1.00 24.29  ? 184  VAL A CA    1 
ATOM   1388 C C     . VAL A 1 184 ? -8.825  17.929  -23.360 1.00 25.80  ? 184  VAL A C     1 
ATOM   1389 O O     . VAL A 1 184 ? -7.755  17.359  -23.083 1.00 23.86  ? 184  VAL A O     1 
ATOM   1390 C CB    . VAL A 1 184 ? -8.463  18.222  -25.847 1.00 24.34  ? 184  VAL A CB    1 
ATOM   1391 C CG1   . VAL A 1 184 ? -9.300  16.985  -26.101 1.00 24.66  ? 184  VAL A CG1   1 
ATOM   1392 C CG2   . VAL A 1 184 ? -8.545  19.209  -26.994 1.00 22.40  ? 184  VAL A CG2   1 
ATOM   1393 N N     . LEU A 1 185 ? -9.978  17.759  -22.717 1.00 27.67  ? 185  LEU A N     1 
ATOM   1394 C CA    . LEU A 1 185 ? -10.152 16.854  -21.550 1.00 27.50  ? 185  LEU A CA    1 
ATOM   1395 C C     . LEU A 1 185 ? -10.150 15.403  -22.021 1.00 27.33  ? 185  LEU A C     1 
ATOM   1396 O O     . LEU A 1 185 ? -10.269 15.105  -23.207 1.00 25.57  ? 185  LEU A O     1 
ATOM   1397 C CB    . LEU A 1 185 ? -11.443 17.248  -20.824 1.00 27.47  ? 185  LEU A CB    1 
ATOM   1398 C CG    . LEU A 1 185 ? -11.381 18.638  -20.201 1.00 28.40  ? 185  LEU A CG    1 
ATOM   1399 C CD1   . LEU A 1 185 ? -12.682 18.961  -19.503 1.00 28.19  ? 185  LEU A CD1   1 
ATOM   1400 C CD2   . LEU A 1 185 ? -10.201 18.763  -19.228 1.00 31.70  ? 185  LEU A CD2   1 
ATOM   1401 N N     . PRO A 1 186 ? -9.901  14.452  -21.103 1.00 25.70  ? 186  PRO A N     1 
ATOM   1402 C CA    . PRO A 1 186 ? -9.678  13.063  -21.492 1.00 25.19  ? 186  PRO A CA    1 
ATOM   1403 C C     . PRO A 1 186 ? -10.784 12.307  -22.245 1.00 25.52  ? 186  PRO A C     1 
ATOM   1404 O O     . PRO A 1 186 ? -10.468 11.304  -22.793 1.00 25.48  ? 186  PRO A O     1 
ATOM   1405 C CB    . PRO A 1 186 ? -9.424  12.379  -20.145 1.00 25.13  ? 186  PRO A CB    1 
ATOM   1406 C CG    . PRO A 1 186 ? -8.865  13.472  -19.288 1.00 25.32  ? 186  PRO A CG    1 
ATOM   1407 C CD    . PRO A 1 186 ? -9.685  14.689  -19.667 1.00 24.89  ? 186  PRO A CD    1 
ATOM   1408 N N     . GLN A 1 187 ? -12.024 12.796  -22.278 1.00 30.60  ? 187  GLN A N     1 
ATOM   1409 C CA    . GLN A 1 187 ? -13.101 12.179  -23.109 1.00 29.62  ? 187  GLN A CA    1 
ATOM   1410 C C     . GLN A 1 187 ? -13.337 12.980  -24.388 1.00 28.57  ? 187  GLN A C     1 
ATOM   1411 O O     . GLN A 1 187 ? -14.164 12.545  -25.184 1.00 31.75  ? 187  GLN A O     1 
ATOM   1412 C CB    . GLN A 1 187 ? -14.365 12.043  -22.274 1.00 31.68  ? 187  GLN A CB    1 
ATOM   1413 C CG    . GLN A 1 187 ? -14.140 11.083  -21.118 1.00 30.65  ? 187  GLN A CG    1 
ATOM   1414 C CD    . GLN A 1 187 ? -15.436 10.692  -20.469 1.00 31.30  ? 187  GLN A CD    1 
ATOM   1415 O OE1   . GLN A 1 187 ? -15.811 11.287  -19.479 1.00 33.56  ? 187  GLN A OE1   1 
ATOM   1416 N NE2   . GLN A 1 187 ? -16.122 9.713   -21.044 1.00 33.83  ? 187  GLN A NE2   1 
ATOM   1417 N N     . GLY A 1 188 ? -12.635 14.095  -24.575 1.00 27.39  ? 188  GLY A N     1 
ATOM   1418 C CA    . GLY A 1 188 ? -12.584 14.803  -25.866 1.00 29.83  ? 188  GLY A CA    1 
ATOM   1419 C C     . GLY A 1 188 ? -13.329 16.111  -25.854 1.00 28.44  ? 188  GLY A C     1 
ATOM   1420 O O     . GLY A 1 188 ? -13.441 16.729  -26.926 1.00 31.70  ? 188  GLY A O     1 
ATOM   1421 N N     . ASP A 1 189 ? -13.779 16.565  -24.688 1.00 27.41  ? 189  ASP A N     1 
ATOM   1422 C CA    . ASP A 1 189 ? -14.328 17.933  -24.521 1.00 28.96  ? 189  ASP A CA    1 
ATOM   1423 C C     . ASP A 1 189 ? -13.168 18.934  -24.518 1.00 29.07  ? 189  ASP A C     1 
ATOM   1424 O O     . ASP A 1 189 ? -12.017 18.550  -24.193 1.00 30.77  ? 189  ASP A O     1 
ATOM   1425 C CB    . ASP A 1 189 ? -15.230 18.026  -23.294 1.00 31.69  ? 189  ASP A CB    1 
ATOM   1426 C CG    . ASP A 1 189 ? -16.442 17.120  -23.457 1.00 38.99  ? 189  ASP A CG    1 
ATOM   1427 O OD1   . ASP A 1 189 ? -16.906 16.965  -24.610 1.00 39.69  ? 189  ASP A OD1   1 
ATOM   1428 O OD2   . ASP A 1 189 ? -16.861 16.529  -22.465 1.00 45.85  ? 189  ASP A OD2   1 
ATOM   1429 N N     . VAL A 1 190 ? -13.445 20.151  -24.966 1.00 26.99  ? 190  VAL A N     1 
ATOM   1430 C CA    . VAL A 1 190 ? -12.450 21.260  -25.000 1.00 31.71  ? 190  VAL A CA    1 
ATOM   1431 C C     . VAL A 1 190 ? -12.962 22.333  -24.073 1.00 27.21  ? 190  VAL A C     1 
ATOM   1432 O O     . VAL A 1 190 ? -14.172 22.558  -24.043 1.00 31.28  ? 190  VAL A O     1 
ATOM   1433 C CB    . VAL A 1 190 ? -12.179 21.898  -26.374 1.00 32.66  ? 190  VAL A CB    1 
ATOM   1434 C CG1   . VAL A 1 190 ? -11.213 21.063  -27.169 1.00 45.16  ? 190  VAL A CG1   1 
ATOM   1435 C CG2   . VAL A 1 190 ? -13.458 22.177  -27.145 1.00 32.41  ? 190  VAL A CG2   1 
ATOM   1436 N N     . MET A 1 191 ? -12.041 22.988  -23.393 1.00 27.40  ? 191  MET A N     1 
ATOM   1437 C CA    . MET A 1 191 ? -12.389 24.095  -22.487 1.00 26.39  ? 191  MET A CA    1 
ATOM   1438 C C     . MET A 1 191 ? -11.245 25.085  -22.519 1.00 23.38  ? 191  MET A C     1 
ATOM   1439 O O     . MET A 1 191 ? -10.104 24.690  -22.828 1.00 23.86  ? 191  MET A O     1 
ATOM   1440 C CB    . MET A 1 191 ? -12.666 23.576  -21.076 1.00 29.55  ? 191  MET A CB    1 
ATOM   1441 C CG    . MET A 1 191 ? -11.533 23.652  -20.106 1.00 31.98  ? 191  MET A CG    1 
ATOM   1442 S SD    . MET A 1 191 ? -12.106 22.994  -18.485 1.00 35.95  ? 191  MET A SD    1 
ATOM   1443 C CE    . MET A 1 191 ? -10.514 22.720  -17.710 1.00 34.16  ? 191  MET A CE    1 
ATOM   1444 N N     . ARG A 1 192 ? -11.575 26.339  -22.292 1.00 23.20  ? 192  ARG A N     1 
ATOM   1445 C CA    . ARG A 1 192 ? -10.628 27.447  -22.130 1.00 21.97  ? 192  ARG A CA    1 
ATOM   1446 C C     . ARG A 1 192 ? -10.643 27.859  -20.672 1.00 24.89  ? 192  ARG A C     1 
ATOM   1447 O O     . ARG A 1 192 ? -11.739 28.006  -20.137 1.00 24.98  ? 192  ARG A O     1 
ATOM   1448 C CB    . ARG A 1 192 ? -10.986 28.597  -23.046 1.00 21.97  ? 192  ARG A CB    1 
ATOM   1449 C CG    . ARG A 1 192 ? -10.720 28.235  -24.491 1.00 23.14  ? 192  ARG A CG    1 
ATOM   1450 C CD    . ARG A 1 192 ? -10.761 29.456  -25.364 1.00 24.46  ? 192  ARG A CD    1 
ATOM   1451 N NE    . ARG A 1 192 ? -10.252 29.122  -26.681 1.00 26.95  ? 192  ARG A NE    1 
ATOM   1452 C CZ    . ARG A 1 192 ? -10.163 29.959  -27.711 1.00 30.11  ? 192  ARG A CZ    1 
ATOM   1453 N NH1   . ARG A 1 192 ? -10.550 31.219  -27.590 1.00 30.85  ? 192  ARG A NH1   1 
ATOM   1454 N NH2   . ARG A 1 192 ? -9.675  29.520  -28.869 1.00 31.08  ? 192  ARG A NH2   1 
ATOM   1455 N N     . THR A 1 193 ? -9.452  28.059  -20.081 1.00 24.57  ? 193  THR A N     1 
ATOM   1456 C CA    . THR A 1 193 ? -9.324  28.448  -18.660 1.00 23.31  ? 193  THR A CA    1 
ATOM   1457 C C     . THR A 1 193 ? -9.354  29.963  -18.549 1.00 27.00  ? 193  THR A C     1 
ATOM   1458 O O     . THR A 1 193 ? -9.072  30.625  -19.550 1.00 25.68  ? 193  THR A O     1 
ATOM   1459 C CB    . THR A 1 193 ? -8.074  27.828  -18.033 1.00 24.38  ? 193  THR A CB    1 
ATOM   1460 O OG1   . THR A 1 193 ? -6.893  28.378  -18.622 1.00 26.15  ? 193  THR A OG1   1 
ATOM   1461 C CG2   . THR A 1 193 ? -8.058  26.322  -18.182 1.00 25.00  ? 193  THR A CG2   1 
ATOM   1462 N N     . GLY A 1 194 ? -9.582  30.440  -17.322 1.00 25.94  ? 194  GLY A N     1 
ATOM   1463 C CA    . GLY A 1 194 ? -9.558  31.845  -16.927 1.00 27.40  ? 194  GLY A CA    1 
ATOM   1464 C C     . GLY A 1 194 ? -10.540 32.656  -17.751 1.00 27.64  ? 194  GLY A C     1 
ATOM   1465 O O     . GLY A 1 194 ? -11.692 32.201  -18.011 1.00 28.93  ? 194  GLY A O     1 
ATOM   1466 N N     . MET A 1 195 ? -10.084 33.815  -18.186 1.00 29.80  ? 195  MET A N     1 
ATOM   1467 C CA    . MET A 1 195 ? -10.919 34.833  -18.868 1.00 30.55  ? 195  MET A CA    1 
ATOM   1468 C C     . MET A 1 195 ? -11.204 34.354  -20.294 1.00 29.92  ? 195  MET A C     1 
ATOM   1469 O O     . MET A 1 195 ? -12.057 34.944  -20.957 1.00 30.60  ? 195  MET A O     1 
ATOM   1470 C CB    . MET A 1 195 ? -10.207 36.187  -18.874 1.00 31.03  ? 195  MET A CB    1 
ATOM   1471 C CG    . MET A 1 195 ? -9.883  36.710  -17.471 1.00 34.25  ? 195  MET A CG    1 
ATOM   1472 S SD    . MET A 1 195 ? -11.315 36.779  -16.357 1.00 35.37  ? 195  MET A SD    1 
ATOM   1473 C CE    . MET A 1 195 ? -12.316 37.949  -17.261 1.00 40.19  ? 195  MET A CE    1 
ATOM   1474 N N     . GLY A 1 196 ? -10.537 33.288  -20.743 1.00 29.19  ? 196  GLY A N     1 
ATOM   1475 C CA    . GLY A 1 196 ? -10.816 32.674  -22.050 1.00 28.18  ? 196  GLY A CA    1 
ATOM   1476 C C     . GLY A 1 196 ? -12.178 31.998  -22.061 1.00 25.29  ? 196  GLY A C     1 
ATOM   1477 O O     . GLY A 1 196 ? -12.689 31.769  -23.135 1.00 24.38  ? 196  GLY A O     1 
ATOM   1478 N N     . ALA A 1 197 ? -12.731 31.624  -20.906 1.00 24.76  ? 197  ALA A N     1 
ATOM   1479 C CA    . ALA A 1 197 ? -14.025 30.904  -20.836 1.00 26.44  ? 197  ALA A CA    1 
ATOM   1480 C C     . ALA A 1 197 ? -15.163 31.894  -21.114 1.00 27.34  ? 197  ALA A C     1 
ATOM   1481 O O     . ALA A 1 197 ? -16.255 31.401  -21.345 1.00 28.31  ? 197  ALA A O     1 
ATOM   1482 C CB    . ALA A 1 197 ? -14.236 30.235  -19.504 1.00 26.49  ? 197  ALA A CB    1 
ATOM   1483 N N     . LEU A 1 198 ? -14.915 33.201  -21.008 1.00 26.35  ? 198  LEU A N     1 
ATOM   1484 C CA    . LEU A 1 198 ? -15.863 34.276  -21.414 1.00 32.32  ? 198  LEU A CA    1 
ATOM   1485 C C     . LEU A 1 198 ? -15.776 34.541  -22.918 1.00 30.51  ? 198  LEU A C     1 
ATOM   1486 O O     . LEU A 1 198 ? -14.791 35.091  -23.391 1.00 29.88  ? 198  LEU A O     1 
ATOM   1487 C CB    . LEU A 1 198 ? -15.585 35.572  -20.653 1.00 32.64  ? 198  LEU A CB    1 
ATOM   1488 C CG    . LEU A 1 198 ? -16.705 36.614  -20.799 1.00 36.25  ? 198  LEU A CG    1 
ATOM   1489 C CD1   . LEU A 1 198 ? -17.506 36.758  -19.514 1.00 37.92  ? 198  LEU A CD1   1 
ATOM   1490 C CD2   . LEU A 1 198 ? -16.156 37.951  -21.220 1.00 36.56  ? 198  LEU A CD2   1 
ATOM   1491 N N     . PRO A 1 199 ? -16.804 34.209  -23.731 1.00 33.53  ? 199  PRO A N     1 
ATOM   1492 C CA    . PRO A 1 199 ? -16.726 34.453  -25.184 1.00 32.39  ? 199  PRO A CA    1 
ATOM   1493 C C     . PRO A 1 199 ? -16.403 35.911  -25.528 1.00 30.93  ? 199  PRO A C     1 
ATOM   1494 O O     . PRO A 1 199 ? -16.996 36.782  -24.947 1.00 31.85  ? 199  PRO A O     1 
ATOM   1495 C CB    . PRO A 1 199 ? -18.112 34.088  -25.707 1.00 30.92  ? 199  PRO A CB    1 
ATOM   1496 C CG    . PRO A 1 199 ? -18.648 33.138  -24.660 1.00 35.78  ? 199  PRO A CG    1 
ATOM   1497 C CD    . PRO A 1 199 ? -18.071 33.584  -23.330 1.00 30.90  ? 199  PRO A CD    1 
ATOM   1498 N N     . GLY A 1 200 ? -15.419 36.134  -26.404 1.00 32.71  ? 200  GLY A N     1 
ATOM   1499 C CA    . GLY A 1 200 ? -15.044 37.471  -26.890 1.00 31.43  ? 200  GLY A CA    1 
ATOM   1500 C C     . GLY A 1 200 ? -14.211 38.251  -25.889 1.00 33.46  ? 200  GLY A C     1 
ATOM   1501 O O     . GLY A 1 200 ? -13.975 39.455  -26.133 1.00 35.07  ? 200  GLY A O     1 
ATOM   1502 N N     . SER A 1 201 ? -13.737 37.611  -24.817 1.00 33.25  ? 201  SER A N     1 
ATOM   1503 C CA    . SER A 1 201 ? -12.905 38.297  -23.798 1.00 35.11  ? 201  SER A CA    1 
ATOM   1504 C C     . SER A 1 201 ? -11.594 38.706  -24.474 1.00 32.37  ? 201  SER A C     1 
ATOM   1505 O O     . SER A 1 201 ? -11.167 37.999  -25.389 1.00 31.74  ? 201  SER A O     1 
ATOM   1506 C CB    . SER A 1 201 ? -12.663 37.429  -22.607 1.00 38.04  ? 201  SER A CB    1 
ATOM   1507 O OG    . SER A 1 201 ? -11.836 36.337  -22.951 1.00 36.30  ? 201  SER A OG    1 
ATOM   1508 N N     . THR A 1 202 ? -11.024 39.817  -24.036 1.00 30.60  ? 202  THR A N     1 
ATOM   1509 C CA    . THR A 1 202 ? -9.782  40.451  -24.532 1.00 34.75  ? 202  THR A CA    1 
ATOM   1510 C C     . THR A 1 202 ? -8.703  40.308  -23.450 1.00 32.58  ? 202  THR A C     1 
ATOM   1511 O O     . THR A 1 202 ? -7.643  40.880  -23.608 1.00 35.70  ? 202  THR A O     1 
ATOM   1512 C CB    . THR A 1 202 ? -10.138 41.903  -24.886 1.00 38.12  ? 202  THR A CB    1 
ATOM   1513 O OG1   . THR A 1 202 ? -10.861 42.412  -23.753 1.00 40.80  ? 202  THR A OG1   1 
ATOM   1514 C CG2   . THR A 1 202 ? -11.011 41.991  -26.124 1.00 37.87  ? 202  THR A CG2   1 
ATOM   1515 N N     . THR A 1 203 ? -8.964  39.523  -22.406 1.00 30.97  ? 203  THR A N     1 
ATOM   1516 C CA    . THR A 1 203 ? -8.166  39.503  -21.151 1.00 30.04  ? 203  THR A CA    1 
ATOM   1517 C C     . THR A 1 203 ? -7.580  38.101  -20.868 1.00 28.94  ? 203  THR A C     1 
ATOM   1518 O O     . THR A 1 203 ? -7.054  37.901  -19.756 1.00 28.37  ? 203  THR A O     1 
ATOM   1519 C CB    . THR A 1 203 ? -9.038  40.000  -19.989 1.00 29.97  ? 203  THR A CB    1 
ATOM   1520 O OG1   . THR A 1 203 ? -10.181 39.151  -19.953 1.00 30.91  ? 203  THR A OG1   1 
ATOM   1521 C CG2   . THR A 1 203 ? -9.463  41.452  -20.113 1.00 30.25  ? 203  THR A CG2   1 
ATOM   1522 N N     . TRP A 1 204 ? -7.687  37.152  -21.803 1.00 25.87  ? 204  TRP A N     1 
ATOM   1523 C CA    . TRP A 1 204 ? -7.276  35.733  -21.618 1.00 27.19  ? 204  TRP A CA    1 
ATOM   1524 C C     . TRP A 1 204 ? -5.829  35.667  -21.123 1.00 25.94  ? 204  TRP A C     1 
ATOM   1525 O O     . TRP A 1 204 ? -5.527  34.879  -20.208 1.00 28.64  ? 204  TRP A O     1 
ATOM   1526 C CB    . TRP A 1 204 ? -7.440  34.952  -22.925 1.00 26.08  ? 204  TRP A CB    1 
ATOM   1527 C CG    . TRP A 1 204 ? -7.447  33.466  -22.756 1.00 24.51  ? 204  TRP A CG    1 
ATOM   1528 C CD1   . TRP A 1 204 ? -7.549  32.752  -21.597 1.00 24.84  ? 204  TRP A CD1   1 
ATOM   1529 C CD2   . TRP A 1 204 ? -7.431  32.504  -23.825 1.00 23.96  ? 204  TRP A CD2   1 
ATOM   1530 N NE1   . TRP A 1 204 ? -7.551  31.408  -21.873 1.00 24.21  ? 204  TRP A NE1   1 
ATOM   1531 C CE2   . TRP A 1 204 ? -7.478  31.230  -23.234 1.00 24.56  ? 204  TRP A CE2   1 
ATOM   1532 C CE3   . TRP A 1 204 ? -7.362  32.609  -25.220 1.00 25.84  ? 204  TRP A CE3   1 
ATOM   1533 C CZ2   . TRP A 1 204 ? -7.462  30.057  -23.992 1.00 24.42  ? 204  TRP A CZ2   1 
ATOM   1534 C CZ3   . TRP A 1 204 ? -7.334  31.458  -25.966 1.00 24.06  ? 204  TRP A CZ3   1 
ATOM   1535 C CH2   . TRP A 1 204 ? -7.394  30.199  -25.360 1.00 26.00  ? 204  TRP A CH2   1 
ATOM   1536 N N     . GLN A 1 205 ? -4.978  36.501  -21.702 1.00 25.57  ? 205  GLN A N     1 
ATOM   1537 C CA    . GLN A 1 205 ? -3.527  36.485  -21.430 1.00 27.47  ? 205  GLN A CA    1 
ATOM   1538 C C     . GLN A 1 205 ? -3.108  37.575  -20.436 1.00 30.13  ? 205  GLN A C     1 
ATOM   1539 O O     . GLN A 1 205 ? -1.912  37.815  -20.325 1.00 31.58  ? 205  GLN A O     1 
ATOM   1540 C CB    . GLN A 1 205 ? -2.783  36.609  -22.751 1.00 26.35  ? 205  GLN A CB    1 
ATOM   1541 C CG    . GLN A 1 205 ? -2.561  35.257  -23.425 1.00 25.87  ? 205  GLN A CG    1 
ATOM   1542 C CD    . GLN A 1 205 ? -3.841  34.626  -23.917 1.00 27.99  ? 205  GLN A CD    1 
ATOM   1543 O OE1   . GLN A 1 205 ? -4.399  35.070  -24.924 1.00 28.49  ? 205  GLN A OE1   1 
ATOM   1544 N NE2   . GLN A 1 205 ? -4.290  33.559  -23.233 1.00 24.02  ? 205  GLN A NE2   1 
ATOM   1545 N N     . LEU A 1 206 ? -3.995  38.219  -19.674 1.00 31.95  ? 206  LEU A N     1 
ATOM   1546 C CA    . LEU A 1 206 ? -3.437  39.290  -18.810 1.00 32.87  ? 206  LEU A CA    1 
ATOM   1547 C C     . LEU A 1 206 ? -3.777  39.107  -17.337 1.00 32.78  ? 206  LEU A C     1 
ATOM   1548 O O     . LEU A 1 206 ? -3.203  39.845  -16.534 1.00 29.85  ? 206  LEU A O     1 
ATOM   1549 C CB    . LEU A 1 206 ? -3.805  40.660  -19.360 1.00 40.53  ? 206  LEU A CB    1 
ATOM   1550 C CG    . LEU A 1 206 ? -5.196  40.818  -19.914 1.00 42.57  ? 206  LEU A CG    1 
ATOM   1551 C CD1   . LEU A 1 206 ? -6.125  41.123  -18.760 1.00 49.86  ? 206  LEU A CD1   1 
ATOM   1552 C CD2   . LEU A 1 206 ? -5.218  41.917  -20.958 1.00 37.29  ? 206  LEU A CD2   1 
ATOM   1553 N N     . ILE A 1 207 ? -4.578  38.106  -16.991 1.00 30.70  ? 207  ILE A N     1 
ATOM   1554 C CA    . ILE A 1 207 ? -4.757  37.671  -15.579 1.00 33.22  ? 207  ILE A CA    1 
ATOM   1555 C C     . ILE A 1 207 ? -4.937  36.165  -15.651 1.00 30.71  ? 207  ILE A C     1 
ATOM   1556 O O     . ILE A 1 207 ? -5.658  35.688  -16.517 1.00 31.62  ? 207  ILE A O     1 
ATOM   1557 C CB    . ILE A 1 207 ? -5.935  38.391  -14.885 1.00 33.35  ? 207  ILE A CB    1 
ATOM   1558 C CG1   . ILE A 1 207 ? -6.073  37.984  -13.416 1.00 38.17  ? 207  ILE A CG1   1 
ATOM   1559 C CG2   . ILE A 1 207 ? -7.246  38.152  -15.610 1.00 31.80  ? 207  ILE A CG2   1 
ATOM   1560 C CD1   . ILE A 1 207 ? -5.080  38.649  -12.514 1.00 45.44  ? 207  ILE A CD1   1 
ATOM   1561 N N     . PRO A 1 208 ? -4.211  35.382  -14.834 1.00 31.60  ? 208  PRO A N     1 
ATOM   1562 C CA    . PRO A 1 208 ? -4.259  33.922  -14.950 1.00 35.34  ? 208  PRO A CA    1 
ATOM   1563 C C     . PRO A 1 208 ? -5.535  33.207  -14.441 1.00 34.72  ? 208  PRO A C     1 
ATOM   1564 O O     . PRO A 1 208 ? -5.738  32.102  -14.876 1.00 35.79  ? 208  PRO A O     1 
ATOM   1565 C CB    . PRO A 1 208 ? -2.989  33.496  -14.176 1.00 35.55  ? 208  PRO A CB    1 
ATOM   1566 C CG    . PRO A 1 208 ? -2.774  34.596  -13.144 1.00 36.02  ? 208  PRO A CG    1 
ATOM   1567 C CD    . PRO A 1 208 ? -3.225  35.864  -13.848 1.00 32.83  ? 208  PRO A CD    1 
ATOM   1568 N N     . TYR A 1 209 ? -6.407  33.846  -13.642 1.00 35.21  ? 209  TYR A N     1 
ATOM   1569 C CA    . TYR A 1 209 ? -7.401  33.166  -12.763 1.00 39.27  ? 209  TYR A CA    1 
ATOM   1570 C C     . TYR A 1 209 ? -8.818  32.990  -13.346 1.00 41.64  ? 209  TYR A C     1 
ATOM   1571 O O     . TYR A 1 209 ? -9.361  31.836  -13.239 1.00 52.44  ? 209  TYR A O     1 
ATOM   1572 C CB    . TYR A 1 209 ? -7.551  33.911  -11.437 1.00 40.50  ? 209  TYR A CB    1 
ATOM   1573 C CG    . TYR A 1 209 ? -6.251  34.123  -10.713 1.00 36.57  ? 209  TYR A CG    1 
ATOM   1574 C CD1   . TYR A 1 209 ? -5.428  33.051  -10.407 1.00 33.81  ? 209  TYR A CD1   1 
ATOM   1575 C CD2   . TYR A 1 209 ? -5.825  35.392  -10.373 1.00 34.85  ? 209  TYR A CD2   1 
ATOM   1576 C CE1   . TYR A 1 209 ? -4.217  33.237  -9.766  1.00 34.17  ? 209  TYR A CE1   1 
ATOM   1577 C CE2   . TYR A 1 209 ? -4.627  35.596  -9.722  1.00 34.92  ? 209  TYR A CE2   1 
ATOM   1578 C CZ    . TYR A 1 209 ? -3.825  34.510  -9.408  1.00 36.32  ? 209  TYR A CZ    1 
ATOM   1579 O OH    . TYR A 1 209 ? -2.642  34.695  -8.779  1.00 33.38  ? 209  TYR A OH    1 
ATOM   1580 N N     . GLY A 1 210 ? -9.465  34.067  -13.776 1.00 38.32  ? 210  GLY A N     1 
ATOM   1581 C CA    . GLY A 1 210 ? -10.921 34.066  -14.064 1.00 40.66  ? 210  GLY A CA    1 
ATOM   1582 C C     . GLY A 1 210 ? -11.830 33.859  -12.844 1.00 39.45  ? 210  GLY A C     1 
ATOM   1583 O O     . GLY A 1 210 ? -11.394 34.048  -11.702 1.00 39.29  ? 210  GLY A O     1 
ATOM   1584 N N     . PHE A 1 211 ? -13.086 33.449  -13.068 1.00 39.22  ? 211  PHE A N     1 
ATOM   1585 C CA    . PHE A 1 211 ? -14.122 33.275  -12.009 1.00 34.03  ? 211  PHE A CA    1 
ATOM   1586 C C     . PHE A 1 211 ? -14.209 31.809  -11.591 1.00 30.35  ? 211  PHE A C     1 
ATOM   1587 O O     . PHE A 1 211 ? -14.215 30.920  -12.449 1.00 27.95  ? 211  PHE A O     1 
ATOM   1588 C CB    . PHE A 1 211 ? -15.483 33.796  -12.494 1.00 36.17  ? 211  PHE A CB    1 
ATOM   1589 C CG    . PHE A 1 211 ? -16.580 33.665  -11.480 1.00 30.65  ? 211  PHE A CG    1 
ATOM   1590 C CD1   . PHE A 1 211 ? -16.692 34.575  -10.448 1.00 30.46  ? 211  PHE A CD1   1 
ATOM   1591 C CD2   . PHE A 1 211 ? -17.461 32.597  -11.528 1.00 30.33  ? 211  PHE A CD2   1 
ATOM   1592 C CE1   . PHE A 1 211 ? -17.680 34.428  -9.482  1.00 33.00  ? 211  PHE A CE1   1 
ATOM   1593 C CE2   . PHE A 1 211 ? -18.471 32.474  -10.586 1.00 29.97  ? 211  PHE A CE2   1 
ATOM   1594 C CZ    . PHE A 1 211 ? -18.572 33.378  -9.556  1.00 29.45  ? 211  PHE A CZ    1 
ATOM   1595 N N     . GLY A 1 212 ? -14.331 31.569  -10.288 1.00 27.12  ? 212  GLY A N     1 
ATOM   1596 C CA    . GLY A 1 212 ? -14.488 30.219  -9.731  1.00 30.84  ? 212  GLY A CA    1 
ATOM   1597 C C     . GLY A 1 212 ? -13.130 29.539  -9.594  1.00 31.17  ? 212  GLY A C     1 
ATOM   1598 O O     . GLY A 1 212 ? -12.105 30.214  -9.640  1.00 31.46  ? 212  GLY A O     1 
ATOM   1599 N N     . PRO A 1 213 ? -13.108 28.212  -9.372  1.00 30.10  ? 213  PRO A N     1 
ATOM   1600 C CA    . PRO A 1 213 ? -11.872 27.482  -9.102  1.00 34.24  ? 213  PRO A CA    1 
ATOM   1601 C C     . PRO A 1 213 ? -10.845 27.666  -10.227 1.00 32.37  ? 213  PRO A C     1 
ATOM   1602 O O     . PRO A 1 213 ? -11.226 27.699  -11.374 1.00 32.15  ? 213  PRO A O     1 
ATOM   1603 C CB    . PRO A 1 213 ? -12.325 26.020  -8.970  1.00 33.56  ? 213  PRO A CB    1 
ATOM   1604 C CG    . PRO A 1 213 ? -13.786 26.107  -8.593  1.00 33.59  ? 213  PRO A CG    1 
ATOM   1605 C CD    . PRO A 1 213 ? -14.293 27.347  -9.301  1.00 34.07  ? 213  PRO A CD    1 
ATOM   1606 N N     . TYR A 1 214 ? -9.584  27.865  -9.855  1.00 30.35  ? 214  TYR A N     1 
ATOM   1607 C CA    . TYR A 1 214 ? -8.505  28.127  -10.813 1.00 28.86  ? 214  TYR A CA    1 
ATOM   1608 C C     . TYR A 1 214 ? -7.881  26.808  -11.169 1.00 30.32  ? 214  TYR A C     1 
ATOM   1609 O O     . TYR A 1 214 ? -7.276  26.182  -10.329 1.00 29.41  ? 214  TYR A O     1 
ATOM   1610 C CB    . TYR A 1 214 ? -7.528  29.138  -10.205 1.00 28.30  ? 214  TYR A CB    1 
ATOM   1611 C CG    . TYR A 1 214 ? -6.161  29.268  -10.806 1.00 28.98  ? 214  TYR A CG    1 
ATOM   1612 C CD1   . TYR A 1 214 ? -5.977  29.496  -12.157 1.00 27.62  ? 214  TYR A CD1   1 
ATOM   1613 C CD2   . TYR A 1 214 ? -5.049  29.216  -9.997  1.00 31.47  ? 214  TYR A CD2   1 
ATOM   1614 C CE1   . TYR A 1 214 ? -4.713  29.633  -12.685 1.00 29.32  ? 214  TYR A CE1   1 
ATOM   1615 C CE2   . TYR A 1 214 ? -3.786  29.350  -10.513 1.00 35.67  ? 214  TYR A CE2   1 
ATOM   1616 C CZ    . TYR A 1 214 ? -3.625  29.560  -11.854 1.00 32.07  ? 214  TYR A CZ    1 
ATOM   1617 O OH    . TYR A 1 214 ? -2.358  29.690  -12.328 1.00 29.18  ? 214  TYR A OH    1 
ATOM   1618 N N     . PRO A 1 215 ? -8.035  26.374  -12.422 1.00 29.99  ? 215  PRO A N     1 
ATOM   1619 C CA    . PRO A 1 215 ? -7.607  25.027  -12.804 1.00 28.79  ? 215  PRO A CA    1 
ATOM   1620 C C     . PRO A 1 215 ? -6.256  24.741  -13.482 1.00 28.02  ? 215  PRO A C     1 
ATOM   1621 O O     . PRO A 1 215 ? -5.881  23.596  -13.539 1.00 25.64  ? 215  PRO A O     1 
ATOM   1622 C CB    . PRO A 1 215 ? -8.719  24.628  -13.758 1.00 32.03  ? 215  PRO A CB    1 
ATOM   1623 C CG    . PRO A 1 215 ? -9.159  25.900  -14.400 1.00 31.64  ? 215  PRO A CG    1 
ATOM   1624 C CD    . PRO A 1 215 ? -8.766  27.039  -13.509 1.00 29.22  ? 215  PRO A CD    1 
ATOM   1625 N N     . ASP A 1 216 ? -5.569  25.753  -13.992 1.00 53.04  ? 216  ASP A N     1 
ATOM   1626 C CA    . ASP A 1 216 ? -4.426  25.567  -14.899 1.00 40.61  ? 216  ASP A CA    1 
ATOM   1627 C C     . ASP A 1 216 ? -3.327  24.702  -14.314 1.00 33.10  ? 216  ASP A C     1 
ATOM   1628 O O     . ASP A 1 216 ? -2.771  23.895  -15.006 1.00 26.21  ? 216  ASP A O     1 
ATOM   1629 C CB    . ASP A 1 216 ? -3.854  26.888  -15.341 1.00 42.64  ? 216  ASP A CB    1 
ATOM   1630 C CG    . ASP A 1 216 ? -4.871  27.762  -16.045 1.00 30.09  ? 216  ASP A CG    1 
ATOM   1631 O OD1   . ASP A 1 216 ? -5.949  28.016  -15.491 1.00 24.85  ? 216  ASP A OD1   1 
ATOM   1632 O OD2   . ASP A 1 216 ? -4.573  28.221  -17.154 1.00 27.41  ? 216  ASP A OD2   1 
ATOM   1633 N N     . GLY A 1 217 ? -3.042  24.875  -13.037 1.00 27.74  ? 217  GLY A N     1 
ATOM   1634 C CA    . GLY A 1 217 ? -2.054  24.053  -12.374 1.00 26.96  ? 217  GLY A CA    1 
ATOM   1635 C C     . GLY A 1 217 ? -2.289  22.571  -12.477 1.00 27.09  ? 217  GLY A C     1 
ATOM   1636 O O     . GLY A 1 217 ? -1.358  21.799  -12.523 1.00 27.23  ? 217  GLY A O     1 
ATOM   1637 N N     . MET A 1 218 ? -3.545  22.170  -12.517 1.00 25.75  ? 218  MET A N     1 
ATOM   1638 C CA    . MET A 1 218 ? -3.889  20.773  -12.619 1.00 25.78  ? 218  MET A CA    1 
ATOM   1639 C C     . MET A 1 218 ? -3.566  20.187  -13.983 1.00 26.06  ? 218  MET A C     1 
ATOM   1640 O O     . MET A 1 218 ? -3.725  19.019  -14.167 1.00 26.23  ? 218  MET A O     1 
ATOM   1641 C CB    . MET A 1 218 ? -5.354  20.563  -12.299 1.00 29.98  ? 218  MET A CB    1 
ATOM   1642 C CG    . MET A 1 218 ? -5.748  20.799  -10.856 1.00 32.80  ? 218  MET A CG    1 
ATOM   1643 S SD    . MET A 1 218 ? -4.942  19.703  -9.688  1.00 37.22  ? 218  MET A SD    1 
ATOM   1644 C CE    . MET A 1 218 ? -5.568  18.100  -10.132 1.00 39.29  ? 218  MET A CE    1 
ATOM   1645 N N     . PHE A 1 219 ? -3.193  21.016  -14.935 1.00 25.42  ? 219  PHE A N     1 
ATOM   1646 C CA    . PHE A 1 219 ? -2.779  20.551  -16.252 1.00 24.14  ? 219  PHE A CA    1 
ATOM   1647 C C     . PHE A 1 219 ? -1.250  20.667  -16.409 1.00 21.59  ? 219  PHE A C     1 
ATOM   1648 O O     . PHE A 1 219 ? -0.744  20.559  -17.501 1.00 23.17  ? 219  PHE A O     1 
ATOM   1649 C CB    . PHE A 1 219 ? -3.553  21.290  -17.326 1.00 27.15  ? 219  PHE A CB    1 
ATOM   1650 C CG    . PHE A 1 219 ? -5.017  21.127  -17.198 1.00 26.27  ? 219  PHE A CG    1 
ATOM   1651 C CD1   . PHE A 1 219 ? -5.611  19.945  -17.567 1.00 26.25  ? 219  PHE A CD1   1 
ATOM   1652 C CD2   . PHE A 1 219 ? -5.792  22.132  -16.665 1.00 28.29  ? 219  PHE A CD2   1 
ATOM   1653 C CE1   . PHE A 1 219 ? -6.963  19.771  -17.431 1.00 27.23  ? 219  PHE A CE1   1 
ATOM   1654 C CE2   . PHE A 1 219 ? -7.144  21.962  -16.520 1.00 28.61  ? 219  PHE A CE2   1 
ATOM   1655 C CZ    . PHE A 1 219 ? -7.728  20.779  -16.904 1.00 24.94  ? 219  PHE A CZ    1 
ATOM   1656 N N     . THR A 1 220 ? -0.544  20.913  -15.317 1.00 20.98  ? 220  THR A N     1 
ATOM   1657 C CA    . THR A 1 220 ? 0.954   20.941  -15.320 1.00 23.65  ? 220  THR A CA    1 
ATOM   1658 C C     . THR A 1 220 ? 1.458   19.735  -14.519 1.00 24.06  ? 220  THR A C     1 
ATOM   1659 O O     . THR A 1 220 ? 0.778   19.368  -13.508 1.00 21.47  ? 220  THR A O     1 
ATOM   1660 C CB    . THR A 1 220 ? 1.500   22.275  -14.787 1.00 24.09  ? 220  THR A CB    1 
ATOM   1661 O OG1   . THR A 1 220 ? 1.179   22.404  -13.406 1.00 26.80  ? 220  THR A OG1   1 
ATOM   1662 C CG2   . THR A 1 220 ? 0.912   23.464  -15.508 1.00 26.45  ? 220  THR A CG2   1 
ATOM   1663 N N     . GLN A 1 221 ? 2.536   19.114  -15.024 1.00 23.40  ? 221  GLN A N     1 
ATOM   1664 C CA    . GLN A 1 221 ? 3.065   17.791  -14.601 1.00 25.46  ? 221  GLN A CA    1 
ATOM   1665 C C     . GLN A 1 221 ? 1.887   16.817  -14.480 1.00 26.29  ? 221  GLN A C     1 
ATOM   1666 O O     . GLN A 1 221 ? 1.788   16.121  -13.451 1.00 25.53  ? 221  GLN A O     1 
ATOM   1667 C CB    . GLN A 1 221 ? 3.852   17.948  -13.293 1.00 25.17  ? 221  GLN A CB    1 
ATOM   1668 C CG    . GLN A 1 221 ? 5.041   18.876  -13.434 1.00 24.21  ? 221  GLN A CG    1 
ATOM   1669 C CD    . GLN A 1 221 ? 6.105   18.679  -12.376 1.00 28.26  ? 221  GLN A CD    1 
ATOM   1670 O OE1   . GLN A 1 221 ? 5.942   17.896  -11.458 1.00 28.69  ? 221  GLN A OE1   1 
ATOM   1671 N NE2   . GLN A 1 221 ? 7.210   19.392  -12.490 1.00 25.54  ? 221  GLN A NE2   1 
ATOM   1672 N N     . SER A 1 222 ? 1.024   16.774  -15.495 1.00 24.19  ? 222  SER A N     1 
ATOM   1673 C CA    . SER A 1 222 ? -0.343  16.220  -15.410 1.00 24.33  ? 222  SER A CA    1 
ATOM   1674 C C     . SER A 1 222 ? -0.692  15.391  -16.647 1.00 26.41  ? 222  SER A C     1 
ATOM   1675 O O     . SER A 1 222 ? -0.171  15.698  -17.772 1.00 24.80  ? 222  SER A O     1 
ATOM   1676 C CB    . SER A 1 222 ? -1.330  17.346  -15.237 1.00 28.35  ? 222  SER A CB    1 
ATOM   1677 O OG    . SER A 1 222 ? -2.669  16.873  -15.253 1.00 31.15  ? 222  SER A OG    1 
ATOM   1678 N N     . ASN A 1 223 ? -1.629  14.460  -16.447 1.00 22.96  ? 223  ASN A N     1 
ATOM   1679 C CA    . ASN A 1 223 ? -2.266  13.639  -17.515 1.00 24.47  ? 223  ASN A CA    1 
ATOM   1680 C C     . ASN A 1 223 ? -3.781  13.911  -17.548 1.00 24.08  ? 223  ASN A C     1 
ATOM   1681 O O     . ASN A 1 223 ? -4.516  13.027  -18.000 1.00 29.73  ? 223  ASN A O     1 
ATOM   1682 C CB    . ASN A 1 223 ? -1.943  12.163  -17.332 1.00 25.74  ? 223  ASN A CB    1 
ATOM   1683 C CG    . ASN A 1 223 ? -2.376  11.621  -15.986 1.00 25.52  ? 223  ASN A CG    1 
ATOM   1684 O OD1   . ASN A 1 223 ? -3.177  12.238  -15.274 1.00 26.02  ? 223  ASN A OD1   1 
ATOM   1685 N ND2   . ASN A 1 223 ? -1.811  10.486  -15.620 1.00 26.51  ? 223  ASN A ND2   1 
ATOM   1686 N N     . LEU A 1 224 ? -4.233  15.080  -17.097 1.00 23.34  ? 224  LEU A N     1 
ATOM   1687 C CA    . LEU A 1 224 ? -5.673  15.451  -17.074 1.00 25.20  ? 224  LEU A CA    1 
ATOM   1688 C C     . LEU A 1 224 ? -6.096  16.080  -18.399 1.00 24.01  ? 224  LEU A C     1 
ATOM   1689 O O     . LEU A 1 224 ? -7.256  16.282  -18.572 1.00 27.48  ? 224  LEU A O     1 
ATOM   1690 C CB    . LEU A 1 224 ? -5.971  16.388  -15.909 1.00 24.60  ? 224  LEU A CB    1 
ATOM   1691 C CG    . LEU A 1 224 ? -5.781  15.748  -14.544 1.00 26.95  ? 224  LEU A CG    1 
ATOM   1692 C CD1   . LEU A 1 224 ? -6.210  16.718  -13.458 1.00 29.00  ? 224  LEU A CD1   1 
ATOM   1693 C CD2   . LEU A 1 224 ? -6.541  14.421  -14.421 1.00 26.52  ? 224  LEU A CD2   1 
ATOM   1694 N N     . GLY A 1 225 ? -5.195  16.343  -19.322 1.00 24.93  ? 225  GLY A N     1 
ATOM   1695 C CA    . GLY A 1 225 ? -5.613  16.983  -20.583 1.00 25.69  ? 225  GLY A CA    1 
ATOM   1696 C C     . GLY A 1 225 ? -4.478  17.159  -21.561 1.00 23.44  ? 225  GLY A C     1 
ATOM   1697 O O     . GLY A 1 225 ? -3.317  17.160  -21.159 1.00 26.94  ? 225  GLY A O     1 
ATOM   1698 N N     . ILE A 1 226 ? -4.838  17.369  -22.815 1.00 24.07  ? 226  ILE A N     1 
ATOM   1699 C CA    . ILE A 1 226 ? -3.924  17.783  -23.911 1.00 24.68  ? 226  ILE A CA    1 
ATOM   1700 C C     . ILE A 1 226 ? -4.151  19.266  -24.191 1.00 25.86  ? 226  ILE A C     1 
ATOM   1701 O O     . ILE A 1 226 ? -5.242  19.636  -24.680 1.00 24.59  ? 226  ILE A O     1 
ATOM   1702 C CB    . ILE A 1 226 ? -4.185  16.923  -25.150 1.00 24.70  ? 226  ILE A CB    1 
ATOM   1703 C CG1   . ILE A 1 226 ? -4.029  15.437  -24.827 1.00 24.57  ? 226  ILE A CG1   1 
ATOM   1704 C CG2   . ILE A 1 226 ? -3.312  17.360  -26.306 1.00 23.34  ? 226  ILE A CG2   1 
ATOM   1705 C CD1   . ILE A 1 226 ? -4.180  14.544  -26.030 1.00 24.53  ? 226  ILE A CD1   1 
ATOM   1706 N N     . VAL A 1 227 ? -3.122  20.073  -23.921 1.00 25.57  ? 227  VAL A N     1 
ATOM   1707 C CA    . VAL A 1 227 ? -3.132  21.540  -24.111 1.00 25.87  ? 227  VAL A CA    1 
ATOM   1708 C C     . VAL A 1 227 ? -2.902  21.829  -25.588 1.00 26.34  ? 227  VAL A C     1 
ATOM   1709 O O     . VAL A 1 227 ? -2.026  21.209  -26.162 1.00 25.22  ? 227  VAL A O     1 
ATOM   1710 C CB    . VAL A 1 227 ? -2.091  22.205  -23.203 1.00 25.98  ? 227  VAL A CB    1 
ATOM   1711 C CG1   . VAL A 1 227 ? -1.978  23.692  -23.468 1.00 27.74  ? 227  VAL A CG1   1 
ATOM   1712 C CG2   . VAL A 1 227 ? -2.465  21.942  -21.751 1.00 25.71  ? 227  VAL A CG2   1 
ATOM   1713 N N     . THR A 1 228 ? -3.730  22.701  -26.166 1.00 23.04  ? 228  THR A N     1 
ATOM   1714 C CA    . THR A 1 228 ? -3.728  23.013  -27.608 1.00 26.68  ? 228  THR A CA    1 
ATOM   1715 C C     . THR A 1 228 ? -3.342  24.472  -27.815 1.00 29.97  ? 228  THR A C     1 
ATOM   1716 O O     . THR A 1 228 ? -2.917  24.788  -28.937 1.00 25.71  ? 228  THR A O     1 
ATOM   1717 C CB    . THR A 1 228 ? -5.076  22.682  -28.250 1.00 27.02  ? 228  THR A CB    1 
ATOM   1718 O OG1   . THR A 1 228 ? -6.096  23.392  -27.557 1.00 24.85  ? 228  THR A OG1   1 
ATOM   1719 C CG2   . THR A 1 228 ? -5.380  21.195  -28.268 1.00 26.96  ? 228  THR A CG2   1 
ATOM   1720 N N     . LYS A 1 229 ? -3.541  25.317  -26.789 1.00 28.51  ? 229  LYS A N     1 
ATOM   1721 C CA    . LYS A 1 229 ? -3.165  26.747  -26.806 1.00 25.84  ? 229  LYS A CA    1 
ATOM   1722 C C     . LYS A 1 229 ? -2.836  27.164  -25.379 1.00 23.45  ? 229  LYS A C     1 
ATOM   1723 O O     . LYS A 1 229 ? -3.442  26.628  -24.446 1.00 22.38  ? 229  LYS A O     1 
ATOM   1724 C CB    . LYS A 1 229 ? -4.259  27.668  -27.330 1.00 27.87  ? 229  LYS A CB    1 
ATOM   1725 C CG    . LYS A 1 229 ? -4.904  27.328  -28.671 1.00 28.43  ? 229  LYS A CG    1 
ATOM   1726 C CD    . LYS A 1 229 ? -6.054  28.321  -28.950 1.00 29.55  ? 229  LYS A CD    1 
ATOM   1727 C CE    . LYS A 1 229 ? -6.667  28.180  -30.326 1.00 28.77  ? 229  LYS A CE    1 
ATOM   1728 N NZ    . LYS A 1 229 ? -6.885  26.749  -30.635 1.00 29.72  ? 229  LYS A NZ    1 
ATOM   1729 N N     . MET A 1 230 ? -1.848  28.032  -25.243 1.00 24.88  ? 230  MET A N     1 
ATOM   1730 C CA    . MET A 1 230 ? -1.367  28.525  -23.934 1.00 26.16  ? 230  MET A CA    1 
ATOM   1731 C C     . MET A 1 230 ? -0.823  29.928  -24.127 1.00 25.06  ? 230  MET A C     1 
ATOM   1732 O O     . MET A 1 230 ? -0.030  30.161  -25.079 1.00 27.44  ? 230  MET A O     1 
ATOM   1733 C CB    . MET A 1 230 ? -0.271  27.628  -23.359 1.00 27.10  ? 230  MET A CB    1 
ATOM   1734 C CG    . MET A 1 230 ? 0.059   27.927  -21.906 1.00 28.16  ? 230  MET A CG    1 
ATOM   1735 S SD    . MET A 1 230 ? 1.687   27.201  -21.482 1.00 27.96  ? 230  MET A SD    1 
ATOM   1736 C CE    . MET A 1 230 ? 2.799   28.496  -22.018 1.00 27.85  ? 230  MET A CE    1 
ATOM   1737 N N     . GLY A 1 231 ? -1.303  30.834  -23.281 1.00 24.49  ? 231  GLY A N     1 
ATOM   1738 C CA    . GLY A 1 231 ? -0.781  32.191  -23.179 1.00 26.12  ? 231  GLY A CA    1 
ATOM   1739 C C     . GLY A 1 231 ? 0.436   32.224  -22.297 1.00 24.11  ? 231  GLY A C     1 
ATOM   1740 O O     . GLY A 1 231 ? 0.495   31.447  -21.343 1.00 24.16  ? 231  GLY A O     1 
ATOM   1741 N N     . ILE A 1 232 ? 1.343   33.146  -22.572 1.00 26.02  ? 232  ILE A N     1 
ATOM   1742 C CA    . ILE A 1 232 ? 2.467   33.442  -21.647 1.00 26.69  ? 232  ILE A CA    1 
ATOM   1743 C C     . ILE A 1 232 ? 2.747   34.948  -21.677 1.00 25.74  ? 232  ILE A C     1 
ATOM   1744 O O     . ILE A 1 232 ? 2.774   35.572  -22.755 1.00 25.51  ? 232  ILE A O     1 
ATOM   1745 C CB    . ILE A 1 232 ? 3.695   32.583  -21.987 1.00 30.26  ? 232  ILE A CB    1 
ATOM   1746 C CG1   . ILE A 1 232 ? 4.724   32.616  -20.841 1.00 31.42  ? 232  ILE A CG1   1 
ATOM   1747 C CG2   . ILE A 1 232 ? 4.275   33.008  -23.317 1.00 29.45  ? 232  ILE A CG2   1 
ATOM   1748 C CD1   . ILE A 1 232 ? 5.653   31.437  -20.797 1.00 28.75  ? 232  ILE A CD1   1 
ATOM   1749 N N     . ALA A 1 233 ? 2.909   35.537  -20.509 1.00 22.82  ? 233  ALA A N     1 
ATOM   1750 C CA    . ALA A 1 233 ? 3.326   36.940  -20.366 1.00 23.20  ? 233  ALA A CA    1 
ATOM   1751 C C     . ALA A 1 233 ? 4.787   37.045  -20.819 1.00 26.92  ? 233  ALA A C     1 
ATOM   1752 O O     . ALA A 1 233 ? 5.566   36.077  -20.593 1.00 25.54  ? 233  ALA A O     1 
ATOM   1753 C CB    . ALA A 1 233 ? 3.157   37.337  -18.933 1.00 25.69  ? 233  ALA A CB    1 
ATOM   1754 N N     . LEU A 1 234 ? 5.143   38.160  -21.449 1.00 26.81  ? 234  LEU A N     1 
ATOM   1755 C CA    . LEU A 1 234 ? 6.498   38.452  -21.981 1.00 27.28  ? 234  LEU A CA    1 
ATOM   1756 C C     . LEU A 1 234 ? 7.023   39.748  -21.367 1.00 30.54  ? 234  LEU A C     1 
ATOM   1757 O O     . LEU A 1 234 ? 6.363   40.790  -21.494 1.00 30.53  ? 234  LEU A O     1 
ATOM   1758 C CB    . LEU A 1 234 ? 6.422   38.581  -23.499 1.00 26.08  ? 234  LEU A CB    1 
ATOM   1759 C CG    . LEU A 1 234 ? 6.025   37.309  -24.236 1.00 27.25  ? 234  LEU A CG    1 
ATOM   1760 C CD1   . LEU A 1 234 ? 5.822   37.603  -25.719 1.00 25.08  ? 234  LEU A CD1   1 
ATOM   1761 C CD2   . LEU A 1 234 ? 7.065   36.215  -24.050 1.00 26.32  ? 234  LEU A CD2   1 
ATOM   1762 N N     . MET A 1 235 ? 8.197   39.668  -20.741 1.00 31.05  ? 235  MET A N     1 
ATOM   1763 C CA    . MET A 1 235 ? 8.903   40.816  -20.144 1.00 31.39  ? 235  MET A CA    1 
ATOM   1764 C C     . MET A 1 235 ? 9.347   41.779  -21.259 1.00 30.42  ? 235  MET A C     1 
ATOM   1765 O O     . MET A 1 235 ? 9.753   41.323  -22.355 1.00 29.88  ? 235  MET A O     1 
ATOM   1766 C CB    . MET A 1 235 ? 10.125  40.325  -19.359 1.00 34.12  ? 235  MET A CB    1 
ATOM   1767 C CG    . MET A 1 235 ? 10.478  41.208  -18.183 1.00 38.76  ? 235  MET A CG    1 
ATOM   1768 S SD    . MET A 1 235 ? 11.969  40.597  -17.347 1.00 37.74  ? 235  MET A SD    1 
ATOM   1769 C CE    . MET A 1 235 ? 13.206  41.341  -18.398 1.00 43.58  ? 235  MET A CE    1 
ATOM   1770 N N     . GLN A 1 236 ? 9.246   43.073  -20.973 1.00 31.42  ? 236  GLN A N     1 
ATOM   1771 C CA    . GLN A 1 236 ? 9.907   44.169  -21.726 1.00 35.88  ? 236  GLN A CA    1 
ATOM   1772 C C     . GLN A 1 236 ? 11.434  44.038  -21.573 1.00 34.51  ? 236  GLN A C     1 
ATOM   1773 O O     . GLN A 1 236 ? 11.903  43.785  -20.463 1.00 33.48  ? 236  GLN A O     1 
ATOM   1774 C CB    . GLN A 1 236 ? 9.425   45.516  -21.193 1.00 36.71  ? 236  GLN A CB    1 
ATOM   1775 C CG    . GLN A 1 236 ? 8.362   46.172  -22.041 1.00 39.65  ? 236  GLN A CG    1 
ATOM   1776 C CD    . GLN A 1 236 ? 7.750   47.351  -21.327 1.00 44.86  ? 236  GLN A CD    1 
ATOM   1777 O OE1   . GLN A 1 236 ? 8.428   48.133  -20.651 1.00 39.38  ? 236  GLN A OE1   1 
ATOM   1778 N NE2   . GLN A 1 236 ? 6.434   47.428  -21.417 1.00 43.14  ? 236  GLN A NE2   1 
ATOM   1779 N N     . LYS A 1 237 ? 12.186  44.186  -22.655 1.00 32.33  ? 237  LYS A N     1 
ATOM   1780 C CA    . LYS A 1 237 ? 13.658  44.339  -22.568 1.00 36.08  ? 237  LYS A CA    1 
ATOM   1781 C C     . LYS A 1 237 ? 13.925  45.587  -21.736 1.00 37.74  ? 237  LYS A C     1 
ATOM   1782 O O     . LYS A 1 237 ? 13.243  46.588  -21.909 1.00 35.40  ? 237  LYS A O     1 
ATOM   1783 C CB    . LYS A 1 237 ? 14.309  44.470  -23.945 1.00 37.39  ? 237  LYS A CB    1 
ATOM   1784 C CG    . LYS A 1 237 ? 14.054  43.321  -24.907 1.00 37.66  ? 237  LYS A CG    1 
ATOM   1785 C CD    . LYS A 1 237 ? 14.908  43.439  -26.147 1.00 38.62  ? 237  LYS A CD    1 
ATOM   1786 C CE    . LYS A 1 237 ? 14.703  42.297  -27.112 1.00 40.47  ? 237  LYS A CE    1 
ATOM   1787 N NZ    . LYS A 1 237 ? 15.058  42.699  -28.494 1.00 41.84  ? 237  LYS A NZ    1 
ATOM   1788 N N     . PRO A 1 238 ? 14.864  45.539  -20.766 1.00 39.12  ? 238  PRO A N     1 
ATOM   1789 C CA    . PRO A 1 238 ? 15.305  46.739  -20.049 1.00 39.96  ? 238  PRO A CA    1 
ATOM   1790 C C     . PRO A 1 238 ? 16.239  47.553  -20.933 1.00 38.84  ? 238  PRO A C     1 
ATOM   1791 O O     . PRO A 1 238 ? 16.678  47.064  -21.966 1.00 33.28  ? 238  PRO A O     1 
ATOM   1792 C CB    . PRO A 1 238 ? 16.018  46.201  -18.804 1.00 41.96  ? 238  PRO A CB    1 
ATOM   1793 C CG    . PRO A 1 238 ? 16.472  44.813  -19.214 1.00 44.92  ? 238  PRO A CG    1 
ATOM   1794 C CD    . PRO A 1 238 ? 15.491  44.316  -20.261 1.00 39.32  ? 238  PRO A CD    1 
ATOM   1795 N N     . PRO A 1 239 ? 16.521  48.852  -20.539 1.00 44.28  ? 239  PRO A N     1 
ATOM   1796 C CA    . PRO A 1 239 ? 17.383  49.595  -21.467 1.00 44.25  ? 239  PRO A CA    1 
ATOM   1797 C C     . PRO A 1 239 ? 18.789  49.046  -21.585 1.00 41.33  ? 239  PRO A C     1 
ATOM   1798 O O     . PRO A 1 239 ? 19.420  49.237  -22.614 1.00 39.21  ? 239  PRO A O     1 
ATOM   1799 C CB    . PRO A 1 239 ? 17.406  51.002  -20.867 1.00 41.42  ? 239  PRO A CB    1 
ATOM   1800 C CG    . PRO A 1 239 ? 17.071  50.836  -19.445 1.00 44.24  ? 239  PRO A CG    1 
ATOM   1801 C CD    . PRO A 1 239 ? 16.038  49.774  -19.471 1.00 42.38  ? 239  PRO A CD    1 
ATOM   1802 N N     . ALA A 1 240 ? 19.262  48.389  -20.544 1.00 37.47  ? 240  ALA A N     1 
ATOM   1803 C CA    . ALA A 1 240 ? 20.572  47.805  -20.567 1.00 38.88  ? 240  ALA A CA    1 
ATOM   1804 C C     . ALA A 1 240 ? 20.681  46.621  -19.642 1.00 35.92  ? 240  ALA A C     1 
ATOM   1805 O O     . ALA A 1 240 ? 19.851  46.436  -18.779 1.00 36.07  ? 240  ALA A O     1 
ATOM   1806 C CB    . ALA A 1 240 ? 21.620  48.839  -20.206 1.00 40.29  ? 240  ALA A CB    1 
ATOM   1807 N N     . SER A 1 241 ? 21.728  45.841  -19.824 1.00 36.40  ? 241  SER A N     1 
ATOM   1808 C CA    . SER A 1 241 ? 21.957  44.680  -18.993 1.00 38.46  ? 241  SER A CA    1 
ATOM   1809 C C     . SER A 1 241 ? 23.424  44.365  -18.828 1.00 38.06  ? 241  SER A C     1 
ATOM   1810 O O     . SER A 1 241 ? 24.224  44.665  -19.695 1.00 34.96  ? 241  SER A O     1 
ATOM   1811 C CB    . SER A 1 241 ? 21.255  43.455  -19.583 1.00 37.38  ? 241  SER A CB    1 
ATOM   1812 O OG    . SER A 1 241 ? 22.113  42.691  -20.391 1.00 37.05  ? 241  SER A OG    1 
ATOM   1813 N N     . MET A 1 242 ? 23.764  43.738  -17.725 1.00 35.97  ? 242  MET A N     1 
ATOM   1814 C CA    . MET A 1 242 ? 25.116  43.317  -17.512 1.00 37.39  ? 242  MET A CA    1 
ATOM   1815 C C     . MET A 1 242 ? 25.122  41.991  -16.776 1.00 36.10  ? 242  MET A C     1 
ATOM   1816 O O     . MET A 1 242 ? 24.431  41.860  -15.800 1.00 34.94  ? 242  MET A O     1 
ATOM   1817 C CB    . MET A 1 242 ? 25.914  44.358  -16.734 1.00 40.96  ? 242  MET A CB    1 
ATOM   1818 C CG    . MET A 1 242 ? 27.398  44.047  -16.619 1.00 42.43  ? 242  MET A CG    1 
ATOM   1819 S SD    . MET A 1 242 ? 27.816  43.084  -15.156 1.00 50.68  ? 242  MET A SD    1 
ATOM   1820 C CE    . MET A 1 242 ? 27.478  44.284  -13.890 1.00 47.88  ? 242  MET A CE    1 
ATOM   1821 N N     . THR A 1 243 ? 25.919  41.039  -17.222 1.00 33.18  ? 243  THR A N     1 
ATOM   1822 C CA    . THR A 1 243 ? 26.063  39.711  -16.584 1.00 34.58  ? 243  THR A CA    1 
ATOM   1823 C C     . THR A 1 243 ? 27.451  39.594  -15.953 1.00 34.37  ? 243  THR A C     1 
ATOM   1824 O O     . THR A 1 243 ? 28.419  39.923  -16.631 1.00 37.91  ? 243  THR A O     1 
ATOM   1825 C CB    . THR A 1 243 ? 25.834  38.599  -17.615 1.00 38.28  ? 243  THR A CB    1 
ATOM   1826 O OG1   . THR A 1 243 ? 24.495  38.769  -18.086 1.00 37.09  ? 243  THR A OG1   1 
ATOM   1827 C CG2   . THR A 1 243 ? 26.070  37.219  -17.034 1.00 38.42  ? 243  THR A CG2   1 
ATOM   1828 N N     . TYR A 1 244 ? 27.550  39.040  -14.746 1.00 35.06  ? 244  TYR A N     1 
ATOM   1829 C CA    . TYR A 1 244 ? 28.839  38.906  -14.025 1.00 38.52  ? 244  TYR A CA    1 
ATOM   1830 C C     . TYR A 1 244 ? 29.062  37.448  -13.594 1.00 43.81  ? 244  TYR A C     1 
ATOM   1831 O O     . TYR A 1 244 ? 28.098  36.657  -13.400 1.00 36.25  ? 244  TYR A O     1 
ATOM   1832 C CB    . TYR A 1 244 ? 28.867  39.887  -12.849 1.00 36.49  ? 244  TYR A CB    1 
ATOM   1833 C CG    . TYR A 1 244 ? 27.693  39.748  -11.918 1.00 40.37  ? 244  TYR A CG    1 
ATOM   1834 C CD1   . TYR A 1 244 ? 26.463  40.342  -12.181 1.00 39.60  ? 244  TYR A CD1   1 
ATOM   1835 C CD2   . TYR A 1 244 ? 27.796  38.953  -10.792 1.00 42.57  ? 244  TYR A CD2   1 
ATOM   1836 C CE1   . TYR A 1 244 ? 25.381  40.182  -11.325 1.00 37.28  ? 244  TYR A CE1   1 
ATOM   1837 C CE2   . TYR A 1 244 ? 26.731  38.795  -9.917  1.00 39.88  ? 244  TYR A CE2   1 
ATOM   1838 C CZ    . TYR A 1 244 ? 25.522  39.401  -10.187 1.00 38.70  ? 244  TYR A CZ    1 
ATOM   1839 O OH    . TYR A 1 244 ? 24.512  39.187  -9.302  1.00 39.26  ? 244  TYR A OH    1 
ATOM   1840 N N     . GLN A 1 245 ? 30.339  37.106  -13.421 1.00 39.87  ? 245  GLN A N     1 
ATOM   1841 C CA    . GLN A 1 245 ? 30.805  35.830  -12.835 1.00 38.30  ? 245  GLN A CA    1 
ATOM   1842 C C     . GLN A 1 245 ? 31.535  36.138  -11.521 1.00 39.52  ? 245  GLN A C     1 
ATOM   1843 O O     . GLN A 1 245 ? 32.397  37.039  -11.511 1.00 38.52  ? 245  GLN A O     1 
ATOM   1844 C CB    . GLN A 1 245 ? 31.686  35.118  -13.850 1.00 35.27  ? 245  GLN A CB    1 
ATOM   1845 C CG    . GLN A 1 245 ? 32.377  33.886  -13.301 1.00 39.22  ? 245  GLN A CG    1 
ATOM   1846 C CD    . GLN A 1 245 ? 33.539  33.486  -14.174 1.00 39.89  ? 245  GLN A CD    1 
ATOM   1847 O OE1   . GLN A 1 245 ? 34.430  34.286  -14.446 1.00 46.07  ? 245  GLN A OE1   1 
ATOM   1848 N NE2   . GLN A 1 245 ? 33.507  32.257  -14.658 1.00 44.45  ? 245  GLN A NE2   1 
ATOM   1849 N N     . ILE A 1 246 ? 31.177  35.431  -10.450 1.00 37.29  ? 246  ILE A N     1 
ATOM   1850 C CA    . ILE A 1 246 ? 31.977  35.369  -9.199  1.00 38.21  ? 246  ILE A CA    1 
ATOM   1851 C C     . ILE A 1 246 ? 32.507  33.945  -9.030  1.00 37.71  ? 246  ILE A C     1 
ATOM   1852 O O     . ILE A 1 246 ? 31.685  33.021  -8.842  1.00 38.68  ? 246  ILE A O     1 
ATOM   1853 C CB    . ILE A 1 246 ? 31.179  35.814  -7.959  1.00 39.54  ? 246  ILE A CB    1 
ATOM   1854 C CG1   . ILE A 1 246 ? 30.183  36.934  -8.257  1.00 37.65  ? 246  ILE A CG1   1 
ATOM   1855 C CG2   . ILE A 1 246 ? 32.144  36.197  -6.841  1.00 40.80  ? 246  ILE A CG2   1 
ATOM   1856 C CD1   . ILE A 1 246 ? 29.171  37.128  -7.141  1.00 34.85  ? 246  ILE A CD1   1 
ATOM   1857 N N     . THR A 1 247 ? 33.832  33.788  -9.125  1.00 38.44  ? 247  THR A N     1 
ATOM   1858 C CA    . THR A 1 247 ? 34.575  32.541  -8.815  1.00 35.79  ? 247  THR A CA    1 
ATOM   1859 C C     . THR A 1 247 ? 34.823  32.529  -7.300  1.00 33.89  ? 247  THR A C     1 
ATOM   1860 O O     . THR A 1 247 ? 35.016  33.612  -6.725  1.00 36.51  ? 247  THR A O     1 
ATOM   1861 C CB    . THR A 1 247 ? 35.844  32.453  -9.669  1.00 38.42  ? 247  THR A CB    1 
ATOM   1862 O OG1   . THR A 1 247 ? 36.653  33.584  -9.356  1.00 41.96  ? 247  THR A OG1   1 
ATOM   1863 C CG2   . THR A 1 247 ? 35.556  32.448  -11.154 1.00 40.74  ? 247  THR A CG2   1 
ATOM   1864 N N     . PHE A 1 248 ? 34.701  31.363  -6.682  1.00 34.46  ? 248  PHE A N     1 
ATOM   1865 C CA    . PHE A 1 248 ? 35.003  31.085  -5.259  1.00 37.64  ? 248  PHE A CA    1 
ATOM   1866 C C     . PHE A 1 248 ? 35.900  29.841  -5.197  1.00 43.61  ? 248  PHE A C     1 
ATOM   1867 O O     . PHE A 1 248 ? 35.559  28.791  -5.819  1.00 41.20  ? 248  PHE A O     1 
ATOM   1868 C CB    . PHE A 1 248 ? 33.722  30.843  -4.463  1.00 38.29  ? 248  PHE A CB    1 
ATOM   1869 C CG    . PHE A 1 248 ? 32.769  32.003  -4.405  1.00 35.96  ? 248  PHE A CG    1 
ATOM   1870 C CD1   . PHE A 1 248 ? 32.961  33.027  -3.495  1.00 34.07  ? 248  PHE A CD1   1 
ATOM   1871 C CD2   . PHE A 1 248 ? 31.668  32.054  -5.240  1.00 36.52  ? 248  PHE A CD2   1 
ATOM   1872 C CE1   . PHE A 1 248 ? 32.080  34.093  -3.439  1.00 35.39  ? 248  PHE A CE1   1 
ATOM   1873 C CE2   . PHE A 1 248 ? 30.783  33.116  -5.174  1.00 35.42  ? 248  PHE A CE2   1 
ATOM   1874 C CZ    . PHE A 1 248 ? 30.973  34.117  -4.254  1.00 36.87  ? 248  PHE A CZ    1 
ATOM   1875 N N     . GLU A 1 249 ? 37.020  29.955  -4.474  1.00 41.46  ? 249  GLU A N     1 
ATOM   1876 C CA    . GLU A 1 249 ? 38.135  28.979  -4.533  1.00 42.57  ? 249  GLU A CA    1 
ATOM   1877 C C     . GLU A 1 249 ? 37.693  27.687  -3.865  1.00 39.00  ? 249  GLU A C     1 
ATOM   1878 O O     . GLU A 1 249 ? 38.000  26.630  -4.400  1.00 41.34  ? 249  GLU A O     1 
ATOM   1879 C CB    . GLU A 1 249 ? 39.375  29.513  -3.800  1.00 53.52  ? 249  GLU A CB    1 
ATOM   1880 C CG    . GLU A 1 249 ? 39.889  30.819  -4.370  1.00 58.54  ? 249  GLU A CG    1 
ATOM   1881 C CD    . GLU A 1 249 ? 41.363  31.143  -4.164  1.00 72.81  ? 249  GLU A CD    1 
ATOM   1882 O OE1   . GLU A 1 249 ? 41.916  30.808  -3.089  1.00 83.62  ? 249  GLU A OE1   1 
ATOM   1883 O OE2   . GLU A 1 249 ? 41.956  31.748  -5.082  1.00 80.50  ? 249  GLU A OE2   1 
ATOM   1884 N N     . ASN A 1 250 ? 36.976  27.781  -2.748  1.00 34.58  ? 250  ASN A N     1 
ATOM   1885 C CA    . ASN A 1 250 ? 36.838  26.646  -1.807  1.00 40.40  ? 250  ASN A CA    1 
ATOM   1886 C C     . ASN A 1 250 ? 35.453  26.025  -1.917  1.00 42.37  ? 250  ASN A C     1 
ATOM   1887 O O     . ASN A 1 250 ? 34.447  26.748  -1.923  1.00 36.49  ? 250  ASN A O     1 
ATOM   1888 C CB    . ASN A 1 250 ? 37.162  27.082  -0.380  1.00 42.32  ? 250  ASN A CB    1 
ATOM   1889 C CG    . ASN A 1 250 ? 38.476  27.819  -0.376  1.00 41.94  ? 250  ASN A CG    1 
ATOM   1890 O OD1   . ASN A 1 250 ? 39.443  27.330  -0.950  1.00 43.18  ? 250  ASN A OD1   1 
ATOM   1891 N ND2   . ASN A 1 250 ? 38.482  29.025  0.158   1.00 42.34  ? 250  ASN A ND2   1 
ATOM   1892 N N     . GLU A 1 251 ? 35.418  24.700  -1.910  1.00 42.59  ? 251  GLU A N     1 
ATOM   1893 C CA    . GLU A 1 251 ? 34.142  23.965  -1.931  1.00 42.04  ? 251  GLU A CA    1 
ATOM   1894 C C     . GLU A 1 251 ? 33.377  24.332  -0.649  1.00 42.71  ? 251  GLU A C     1 
ATOM   1895 O O     . GLU A 1 251 ? 32.133  24.402  -0.699  1.00 39.74  ? 251  GLU A O     1 
ATOM   1896 C CB    . GLU A 1 251 ? 34.439  22.494  -2.214  1.00 43.32  ? 251  GLU A CB    1 
ATOM   1897 C CG    . GLU A 1 251 ? 35.097  21.755  -1.082  1.00 45.29  ? 251  GLU A CG    1 
ATOM   1898 C CD    . GLU A 1 251 ? 35.281  20.286  -1.423  1.00 43.08  ? 251  GLU A CD    1 
ATOM   1899 O OE1   . GLU A 1 251 ? 35.764  20.000  -2.538  1.00 39.33  ? 251  GLU A OE1   1 
ATOM   1900 O OE2   . GLU A 1 251 ? 34.886  19.443  -0.588  1.00 44.35  ? 251  GLU A OE2   1 
ATOM   1901 N N     . SER A 1 252 ? 34.083  24.630  0.448   1.00 37.10  ? 252  SER A N     1 
ATOM   1902 C CA    . SER A 1 252 ? 33.469  25.013  1.745   1.00 39.88  ? 252  SER A CA    1 
ATOM   1903 C C     . SER A 1 252 ? 32.911  26.444  1.680   1.00 34.28  ? 252  SER A C     1 
ATOM   1904 O O     . SER A 1 252 ? 32.173  26.803  2.611   1.00 33.71  ? 252  SER A O     1 
ATOM   1905 C CB    . SER A 1 252 ? 34.455  24.853  2.886   1.00 44.42  ? 252  SER A CB    1 
ATOM   1906 O OG    . SER A 1 252 ? 35.471  25.830  2.765   1.00 48.39  ? 252  SER A OG    1 
ATOM   1907 N N     . ASP A 1 253 ? 33.204  27.230  0.627   1.00 32.92  ? 253  ASP A N     1 
ATOM   1908 C CA    . ASP A 1 253 ? 32.620  28.595  0.476   1.00 35.78  ? 253  ASP A CA    1 
ATOM   1909 C C     . ASP A 1 253 ? 31.087  28.526  0.320   1.00 38.51  ? 253  ASP A C     1 
ATOM   1910 O O     . ASP A 1 253 ? 30.424  29.503  0.711   1.00 38.80  ? 253  ASP A O     1 
ATOM   1911 C CB    . ASP A 1 253 ? 33.222  29.369  -0.703  1.00 37.37  ? 253  ASP A CB    1 
ATOM   1912 C CG    . ASP A 1 253 ? 34.640  29.842  -0.442  1.00 37.30  ? 253  ASP A CG    1 
ATOM   1913 O OD1   . ASP A 1 253 ? 34.947  30.027  0.726   1.00 36.53  ? 253  ASP A OD1   1 
ATOM   1914 O OD2   . ASP A 1 253 ? 35.427  29.977  -1.409  1.00 37.37  ? 253  ASP A OD2   1 
ATOM   1915 N N     . LEU A 1 254 ? 30.531  27.419  -0.196  1.00 37.35  ? 254  LEU A N     1 
ATOM   1916 C CA    . LEU A 1 254 ? 29.075  27.277  -0.498  1.00 32.51  ? 254  LEU A CA    1 
ATOM   1917 C C     . LEU A 1 254 ? 28.232  27.791  0.671   1.00 30.89  ? 254  LEU A C     1 
ATOM   1918 O O     . LEU A 1 254 ? 27.199  28.390  0.427   1.00 27.72  ? 254  LEU A O     1 
ATOM   1919 C CB    . LEU A 1 254 ? 28.766  25.801  -0.771  1.00 33.28  ? 254  LEU A CB    1 
ATOM   1920 C CG    . LEU A 1 254 ? 27.298  25.425  -0.965  1.00 30.62  ? 254  LEU A CG    1 
ATOM   1921 C CD1   . LEU A 1 254 ? 26.758  26.043  -2.237  1.00 29.53  ? 254  LEU A CD1   1 
ATOM   1922 C CD2   . LEU A 1 254 ? 27.126  23.899  -0.975  1.00 32.47  ? 254  LEU A CD2   1 
ATOM   1923 N N     . GLU A 1 255 ? 28.625  27.518  1.915   1.00 30.58  ? 255  GLU A N     1 
ATOM   1924 C CA    . GLU A 1 255 ? 27.758  27.839  3.063   1.00 32.39  ? 255  GLU A CA    1 
ATOM   1925 C C     . GLU A 1 255 ? 27.552  29.348  3.126   1.00 34.86  ? 255  GLU A C     1 
ATOM   1926 O O     . GLU A 1 255 ? 26.392  29.778  3.257   1.00 35.04  ? 255  GLU A O     1 
ATOM   1927 C CB    . GLU A 1 255 ? 28.325  27.355  4.386   1.00 37.10  ? 255  GLU A CB    1 
ATOM   1928 C CG    . GLU A 1 255 ? 27.396  27.684  5.537   1.00 38.48  ? 255  GLU A CG    1 
ATOM   1929 C CD    . GLU A 1 255 ? 27.856  27.077  6.843   1.00 44.56  ? 255  GLU A CD    1 
ATOM   1930 O OE1   . GLU A 1 255 ? 28.996  26.585  6.874   1.00 50.34  ? 255  GLU A OE1   1 
ATOM   1931 O OE2   . GLU A 1 255 ? 27.066  27.076  7.795   1.00 47.06  ? 255  GLU A OE2   1 
ATOM   1932 N N     . GLN A 1 256 ? 28.644  30.102  3.041   1.00 36.99  ? 256  GLN A N     1 
ATOM   1933 C CA    . GLN A 1 256 ? 28.625  31.580  3.113   1.00 38.03  ? 256  GLN A CA    1 
ATOM   1934 C C     . GLN A 1 256 ? 28.003  32.129  1.823   1.00 35.61  ? 256  GLN A C     1 
ATOM   1935 O O     . GLN A 1 256 ? 27.234  33.085  1.907   1.00 32.42  ? 256  GLN A O     1 
ATOM   1936 C CB    . GLN A 1 256 ? 30.034  32.121  3.345   1.00 43.68  ? 256  GLN A CB    1 
ATOM   1937 C CG    . GLN A 1 256 ? 30.057  33.639  3.452   1.00 50.50  ? 256  GLN A CG    1 
ATOM   1938 C CD    . GLN A 1 256 ? 30.958  34.131  4.555   1.00 54.24  ? 256  GLN A CD    1 
ATOM   1939 O OE1   . GLN A 1 256 ? 32.075  33.647  4.722   1.00 57.41  ? 256  GLN A OE1   1 
ATOM   1940 N NE2   . GLN A 1 256 ? 30.468  35.101  5.314   1.00 49.67  ? 256  GLN A NE2   1 
ATOM   1941 N N     . ILE A 1 257 ? 28.336  31.572  0.661   1.00 32.72  ? 257  ILE A N     1 
ATOM   1942 C CA    . ILE A 1 257 ? 27.760  32.074  -0.625  1.00 32.56  ? 257  ILE A CA    1 
ATOM   1943 C C     . ILE A 1 257 ? 26.215  32.054  -0.542  1.00 31.66  ? 257  ILE A C     1 
ATOM   1944 O O     . ILE A 1 257 ? 25.586  33.053  -0.897  1.00 33.37  ? 257  ILE A O     1 
ATOM   1945 C CB    . ILE A 1 257 ? 28.252  31.266  -1.833  1.00 29.21  ? 257  ILE A CB    1 
ATOM   1946 C CG1   . ILE A 1 257 ? 29.778  31.166  -1.899  1.00 29.56  ? 257  ILE A CG1   1 
ATOM   1947 C CG2   . ILE A 1 257 ? 27.673  31.853  -3.124  1.00 28.08  ? 257  ILE A CG2   1 
ATOM   1948 C CD1   . ILE A 1 257 ? 30.255  30.028  -2.766  1.00 27.14  ? 257  ILE A CD1   1 
ATOM   1949 N N     . VAL A 1 258 ? 25.615  30.962  -0.074  1.00 30.90  ? 258  VAL A N     1 
ATOM   1950 C CA    . VAL A 1 258 ? 24.128  30.827  -0.031  1.00 32.15  ? 258  VAL A CA    1 
ATOM   1951 C C     . VAL A 1 258 ? 23.531  31.799  1.007   1.00 37.20  ? 258  VAL A C     1 
ATOM   1952 O O     . VAL A 1 258 ? 22.473  32.407  0.709   1.00 30.76  ? 258  VAL A O     1 
ATOM   1953 C CB    . VAL A 1 258 ? 23.709  29.367  0.214   1.00 31.50  ? 258  VAL A CB    1 
ATOM   1954 C CG1   . VAL A 1 258 ? 22.242  29.255  0.577   1.00 32.72  ? 258  VAL A CG1   1 
ATOM   1955 C CG2   . VAL A 1 258 ? 24.037  28.496  -0.994  1.00 30.94  ? 258  VAL A CG2   1 
ATOM   1956 N N     . ASP A 1 259 ? 24.179  31.968  2.166   1.00 30.94  ? 259  ASP A N     1 
ATOM   1957 C CA    . ASP A 1 259 ? 23.690  32.863  3.248   1.00 32.43  ? 259  ASP A CA    1 
ATOM   1958 C C     . ASP A 1 259 ? 23.780  34.335  2.833   1.00 31.17  ? 259  ASP A C     1 
ATOM   1959 O O     . ASP A 1 259 ? 23.017  35.126  3.392   1.00 34.13  ? 259  ASP A O     1 
ATOM   1960 C CB    . ASP A 1 259 ? 24.424  32.583  4.563   1.00 34.44  ? 259  ASP A CB    1 
ATOM   1961 C CG    . ASP A 1 259 ? 23.993  31.272  5.187   1.00 35.67  ? 259  ASP A CG    1 
ATOM   1962 O OD1   . ASP A 1 259 ? 22.819  30.873  4.951   1.00 35.29  ? 259  ASP A OD1   1 
ATOM   1963 O OD2   . ASP A 1 259 ? 24.828  30.645  5.890   1.00 39.25  ? 259  ASP A OD2   1 
ATOM   1964 N N     . ILE A 1 260 ? 24.671  34.700  1.908   1.00 34.69  ? 260  ILE A N     1 
ATOM   1965 C CA    . ILE A 1 260 ? 24.761  36.076  1.349   1.00 36.95  ? 260  ILE A CA    1 
ATOM   1966 C C     . ILE A 1 260 ? 23.730  36.191  0.220   1.00 41.90  ? 260  ILE A C     1 
ATOM   1967 O O     . ILE A 1 260 ? 23.053  37.235  0.112   1.00 34.60  ? 260  ILE A O     1 
ATOM   1968 C CB    . ILE A 1 260 ? 26.204  36.376  0.889   1.00 42.38  ? 260  ILE A CB    1 
ATOM   1969 C CG1   . ILE A 1 260 ? 27.158  36.441  2.084   1.00 42.20  ? 260  ILE A CG1   1 
ATOM   1970 C CG2   . ILE A 1 260 ? 26.269  37.654  0.058   1.00 44.63  ? 260  ILE A CG2   1 
ATOM   1971 C CD1   . ILE A 1 260 ? 28.620  36.384  1.710   1.00 42.36  ? 260  ILE A CD1   1 
ATOM   1972 N N     . MET A 1 261 ? 23.607  35.141  -0.596  1.00 41.78  ? 261  MET A N     1 
ATOM   1973 C CA    . MET A 1 261 ? 22.695  35.134  -1.763  1.00 42.48  ? 261  MET A CA    1 
ATOM   1974 C C     . MET A 1 261 ? 21.249  35.392  -1.299  1.00 41.22  ? 261  MET A C     1 
ATOM   1975 O O     . MET A 1 261 ? 20.618  36.285  -1.872  1.00 37.98  ? 261  MET A O     1 
ATOM   1976 C CB    . MET A 1 261 ? 22.780  33.802  -2.505  1.00 45.61  ? 261  MET A CB    1 
ATOM   1977 C CG    . MET A 1 261 ? 22.246  33.874  -3.909  1.00 51.16  ? 261  MET A CG    1 
ATOM   1978 S SD    . MET A 1 261 ? 22.050  32.225  -4.614  1.00 52.74  ? 261  MET A SD    1 
ATOM   1979 C CE    . MET A 1 261 ? 23.623  31.485  -4.157  1.00 42.33  ? 261  MET A CE    1 
ATOM   1980 N N     . LEU A 1 262 ? 20.735  34.690  -0.283  1.00 38.55  ? 262  LEU A N     1 
ATOM   1981 C CA    . LEU A 1 262 ? 19.284  34.762  0.024   1.00 36.46  ? 262  LEU A CA    1 
ATOM   1982 C C     . LEU A 1 262 ? 18.842  36.207  0.262   1.00 37.02  ? 262  LEU A C     1 
ATOM   1983 O O     . LEU A 1 262 ? 17.866  36.666  -0.360  1.00 31.78  ? 262  LEU A O     1 
ATOM   1984 C CB    . LEU A 1 262 ? 18.891  33.899  1.222   1.00 37.98  ? 262  LEU A CB    1 
ATOM   1985 C CG    . LEU A 1 262 ? 17.440  34.131  1.647   1.00 41.45  ? 262  LEU A CG    1 
ATOM   1986 C CD1   . LEU A 1 262 ? 16.481  33.559  0.603   1.00 39.40  ? 262  LEU A CD1   1 
ATOM   1987 C CD2   . LEU A 1 262 ? 17.156  33.575  3.021   1.00 43.28  ? 262  LEU A CD2   1 
ATOM   1988 N N     . PRO A 1 263 ? 19.462  36.937  1.224   1.00 38.05  ? 263  PRO A N     1 
ATOM   1989 C CA    . PRO A 1 263 ? 19.015  38.283  1.563   1.00 37.67  ? 263  PRO A CA    1 
ATOM   1990 C C     . PRO A 1 263 ? 19.081  39.228  0.368   1.00 34.41  ? 263  PRO A C     1 
ATOM   1991 O O     . PRO A 1 263 ? 18.342  40.182  0.393   1.00 39.37  ? 263  PRO A O     1 
ATOM   1992 C CB    . PRO A 1 263 ? 20.006  38.760  2.640   1.00 39.18  ? 263  PRO A CB    1 
ATOM   1993 C CG    . PRO A 1 263 ? 20.551  37.495  3.229   1.00 39.76  ? 263  PRO A CG    1 
ATOM   1994 C CD    . PRO A 1 263 ? 20.581  36.513  2.082   1.00 37.38  ? 263  PRO A CD    1 
ATOM   1995 N N     . LEU A 1 264 ? 19.983  38.954  -0.586  1.00 31.80  ? 264  LEU A N     1 
ATOM   1996 C CA    . LEU A 1 264 ? 20.206  39.755  -1.814  1.00 31.95  ? 264  LEU A CA    1 
ATOM   1997 C C     . LEU A 1 264 ? 19.194  39.378  -2.912  1.00 32.34  ? 264  LEU A C     1 
ATOM   1998 O O     . LEU A 1 264 ? 19.092  40.129  -3.902  1.00 34.11  ? 264  LEU A O     1 
ATOM   1999 C CB    . LEU A 1 264 ? 21.640  39.530  -2.303  1.00 34.85  ? 264  LEU A CB    1 
ATOM   2000 C CG    . LEU A 1 264 ? 22.764  40.116  -1.436  1.00 37.48  ? 264  LEU A CG    1 
ATOM   2001 C CD1   . LEU A 1 264 ? 24.050  40.154  -2.234  1.00 39.23  ? 264  LEU A CD1   1 
ATOM   2002 C CD2   . LEU A 1 264 ? 22.428  41.517  -0.931  1.00 39.00  ? 264  LEU A CD2   1 
ATOM   2003 N N     . ARG A 1 265 ? 18.490  38.259  -2.783  1.00 32.77  ? 265  ARG A N     1 
ATOM   2004 C CA    . ARG A 1 265 ? 17.572  37.750  -3.839  1.00 32.25  ? 265  ARG A CA    1 
ATOM   2005 C C     . ARG A 1 265 ? 16.104  37.836  -3.405  1.00 29.89  ? 265  ARG A C     1 
ATOM   2006 O O     . ARG A 1 265 ? 15.242  37.934  -4.291  1.00 33.14  ? 265  ARG A O     1 
ATOM   2007 C CB    . ARG A 1 265 ? 17.897  36.297  -4.186  1.00 34.06  ? 265  ARG A CB    1 
ATOM   2008 C CG    . ARG A 1 265 ? 16.970  35.684  -5.228  1.00 33.60  ? 265  ARG A CG    1 
ATOM   2009 C CD    . ARG A 1 265 ? 16.911  36.494  -6.506  1.00 33.26  ? 265  ARG A CD    1 
ATOM   2010 N NE    . ARG A 1 265 ? 15.862  35.940  -7.323  1.00 34.47  ? 265  ARG A NE    1 
ATOM   2011 C CZ    . ARG A 1 265 ? 15.216  36.565  -8.305  1.00 35.16  ? 265  ARG A CZ    1 
ATOM   2012 N NH1   . ARG A 1 265 ? 15.540  37.794  -8.667  1.00 34.74  ? 265  ARG A NH1   1 
ATOM   2013 N NH2   . ARG A 1 265 ? 14.243  35.942  -8.943  1.00 36.81  ? 265  ARG A NH2   1 
ATOM   2014 N N     . ILE A 1 266 ? 15.804  37.730  -2.116  1.00 29.25  ? 266  ILE A N     1 
ATOM   2015 C CA    . ILE A 1 266 ? 14.410  37.555  -1.621  1.00 31.84  ? 266  ILE A CA    1 
ATOM   2016 C C     . ILE A 1 266 ? 13.543  38.783  -1.970  1.00 33.33  ? 266  ILE A C     1 
ATOM   2017 O O     . ILE A 1 266 ? 12.339  38.616  -2.078  1.00 30.63  ? 266  ILE A O     1 
ATOM   2018 C CB    . ILE A 1 266 ? 14.405  37.271  -0.111  1.00 34.38  ? 266  ILE A CB    1 
ATOM   2019 C CG1   . ILE A 1 266 ? 13.028  36.778  0.353   1.00 36.74  ? 266  ILE A CG1   1 
ATOM   2020 C CG2   . ILE A 1 266 ? 14.877  38.494  0.666   1.00 33.52  ? 266  ILE A CG2   1 
ATOM   2021 C CD1   . ILE A 1 266 ? 13.048  36.051  1.678   1.00 35.49  ? 266  ILE A CD1   1 
ATOM   2022 N N     . ASN A 1 267 ? 14.134  39.972  -2.127  1.00 35.20  ? 267  ASN A N     1 
ATOM   2023 C CA    . ASN A 1 267 ? 13.440  41.211  -2.582  1.00 33.49  ? 267  ASN A CA    1 
ATOM   2024 C C     . ASN A 1 267 ? 13.639  41.403  -4.090  1.00 34.53  ? 267  ASN A C     1 
ATOM   2025 O O     . ASN A 1 267 ? 13.268  42.479  -4.589  1.00 33.06  ? 267  ASN A O     1 
ATOM   2026 C CB    . ASN A 1 267 ? 13.945  42.441  -1.826  1.00 31.40  ? 267  ASN A CB    1 
ATOM   2027 C CG    . ASN A 1 267 ? 13.707  42.299  -0.341  1.00 36.22  ? 267  ASN A CG    1 
ATOM   2028 O OD1   . ASN A 1 267 ? 12.590  41.989  0.088   1.00 39.28  ? 267  ASN A OD1   1 
ATOM   2029 N ND2   . ASN A 1 267 ? 14.763  42.459  0.441   1.00 36.08  ? 267  ASN A ND2   1 
ATOM   2030 N N     . MET A 1 268 ? 14.259  40.434  -4.775  1.00 35.03  ? 268  MET A N     1 
ATOM   2031 C CA    . MET A 1 268 ? 14.435  40.428  -6.253  1.00 39.02  ? 268  MET A CA    1 
ATOM   2032 C C     . MET A 1 268 ? 15.355  41.574  -6.665  1.00 37.62  ? 268  MET A C     1 
ATOM   2033 O O     . MET A 1 268 ? 15.382  41.908  -7.850  1.00 34.15  ? 268  MET A O     1 
ATOM   2034 C CB    . MET A 1 268 ? 13.102  40.566  -7.001  1.00 40.21  ? 268  MET A CB    1 
ATOM   2035 C CG    . MET A 1 268 ? 12.007  39.649  -6.481  1.00 43.97  ? 268  MET A CG    1 
ATOM   2036 S SD    . MET A 1 268 ? 10.403  39.926  -7.292  1.00 56.82  ? 268  MET A SD    1 
ATOM   2037 C CE    . MET A 1 268 ? 10.899  39.750  -9.007  1.00 54.22  ? 268  MET A CE    1 
ATOM   2038 N N     . ALA A 1 269 ? 16.113  42.112  -5.708  1.00 39.57  ? 269  ALA A N     1 
ATOM   2039 C CA    . ALA A 1 269 ? 17.193  43.095  -5.912  1.00 36.35  ? 269  ALA A CA    1 
ATOM   2040 C C     . ALA A 1 269 ? 18.058  43.087  -4.659  1.00 35.26  ? 269  ALA A C     1 
ATOM   2041 O O     . ALA A 1 269 ? 17.553  42.865  -3.565  1.00 37.88  ? 269  ALA A O     1 
ATOM   2042 C CB    . ALA A 1 269 ? 16.630  44.467  -6.207  1.00 37.71  ? 269  ALA A CB    1 
ATOM   2043 N N     . PRO A 1 270 ? 19.380  43.315  -4.784  1.00 31.68  ? 270  PRO A N     1 
ATOM   2044 C CA    . PRO A 1 270 ? 19.998  43.535  -6.086  1.00 31.96  ? 270  PRO A CA    1 
ATOM   2045 C C     . PRO A 1 270 ? 20.122  42.325  -7.032  1.00 32.97  ? 270  PRO A C     1 
ATOM   2046 O O     . PRO A 1 270 ? 20.473  42.540  -8.182  1.00 35.02  ? 270  PRO A O     1 
ATOM   2047 C CB    . PRO A 1 270 ? 21.405  44.000  -5.702  1.00 33.19  ? 270  PRO A CB    1 
ATOM   2048 C CG    . PRO A 1 270 ? 21.656  43.319  -4.380  1.00 32.24  ? 270  PRO A CG    1 
ATOM   2049 C CD    . PRO A 1 270 ? 20.329  43.462  -3.674  1.00 33.61  ? 270  PRO A CD    1 
ATOM   2050 N N     . LEU A 1 271 ? 19.916  41.095  -6.554  1.00 32.20  ? 271  LEU A N     1 
ATOM   2051 C CA    . LEU A 1 271 ? 20.016  39.894  -7.439  1.00 32.13  ? 271  LEU A CA    1 
ATOM   2052 C C     . LEU A 1 271 ? 18.737  39.833  -8.286  1.00 32.13  ? 271  LEU A C     1 
ATOM   2053 O O     . LEU A 1 271 ? 17.743  39.224  -7.839  1.00 29.56  ? 271  LEU A O     1 
ATOM   2054 C CB    . LEU A 1 271 ? 20.216  38.635  -6.595  1.00 32.08  ? 271  LEU A CB    1 
ATOM   2055 C CG    . LEU A 1 271 ? 21.559  38.529  -5.874  1.00 31.15  ? 271  LEU A CG    1 
ATOM   2056 C CD1   . LEU A 1 271 ? 21.697  37.170  -5.226  1.00 31.40  ? 271  LEU A CD1   1 
ATOM   2057 C CD2   . LEU A 1 271 ? 22.713  38.762  -6.849  1.00 33.96  ? 271  LEU A CD2   1 
ATOM   2058 N N     . GLN A 1 272 ? 18.747  40.535  -9.416  1.00 31.67  ? 272  GLN A N     1 
ATOM   2059 C CA    . GLN A 1 272 ? 17.520  40.850  -10.191 1.00 35.20  ? 272  GLN A CA    1 
ATOM   2060 C C     . GLN A 1 272 ? 17.081  39.608  -10.969 1.00 33.81  ? 272  GLN A C     1 
ATOM   2061 O O     . GLN A 1 272 ? 15.879  39.399  -11.126 1.00 29.71  ? 272  GLN A O     1 
ATOM   2062 C CB    . GLN A 1 272 ? 17.784  42.037  -11.112 1.00 32.76  ? 272  GLN A CB    1 
ATOM   2063 C CG    . GLN A 1 272 ? 17.845  43.353  -10.357 1.00 34.94  ? 272  GLN A CG    1 
ATOM   2064 C CD    . GLN A 1 272 ? 18.300  44.448  -11.281 1.00 32.54  ? 272  GLN A CD    1 
ATOM   2065 O OE1   . GLN A 1 272 ? 19.362  44.360  -11.871 1.00 38.21  ? 272  GLN A OE1   1 
ATOM   2066 N NE2   . GLN A 1 272 ? 17.473  45.458  -11.464 1.00 39.20  ? 272  GLN A NE2   1 
ATOM   2067 N N     . ASN A 1 273 ? 18.004  38.795  -11.467 1.00 35.14  ? 273  ASN A N     1 
ATOM   2068 C CA    . ASN A 1 273 ? 17.558  37.580  -12.195 1.00 33.83  ? 273  ASN A CA    1 
ATOM   2069 C C     . ASN A 1 273 ? 17.703  36.397  -11.239 1.00 35.01  ? 273  ASN A C     1 
ATOM   2070 O O     . ASN A 1 273 ? 17.980  36.610  -10.023 1.00 32.80  ? 273  ASN A O     1 
ATOM   2071 C CB    . ASN A 1 273 ? 18.287  37.425  -13.516 1.00 37.51  ? 273  ASN A CB    1 
ATOM   2072 C CG    . ASN A 1 273 ? 19.627  36.750  -13.347 1.00 38.66  ? 273  ASN A CG    1 
ATOM   2073 O OD1   . ASN A 1 273 ? 20.405  37.119  -12.463 1.00 34.85  ? 273  ASN A OD1   1 
ATOM   2074 N ND2   . ASN A 1 273 ? 19.877  35.752  -14.174 1.00 33.35  ? 273  ASN A ND2   1 
ATOM   2075 N N     . VAL A 1 274 ? 17.474  35.204  -11.768 1.00 30.58  ? 274  VAL A N     1 
ATOM   2076 C CA    . VAL A 1 274 ? 17.634  33.927  -11.037 1.00 28.17  ? 274  VAL A CA    1 
ATOM   2077 C C     . VAL A 1 274 ? 19.132  33.673  -10.916 1.00 26.69  ? 274  VAL A C     1 
ATOM   2078 O O     . VAL A 1 274 ? 19.831  33.438  -11.902 1.00 27.64  ? 274  VAL A O     1 
ATOM   2079 C CB    . VAL A 1 274 ? 16.915  32.765  -11.749 1.00 25.67  ? 274  VAL A CB    1 
ATOM   2080 C CG1   . VAL A 1 274 ? 17.132  31.465  -11.005 1.00 24.79  ? 274  VAL A CG1   1 
ATOM   2081 C CG2   . VAL A 1 274 ? 15.419  33.030  -11.953 1.00 26.81  ? 274  VAL A CG2   1 
ATOM   2082 N N     . PRO A 1 275 ? 19.677  33.726  -9.696  1.00 26.81  ? 275  PRO A N     1 
ATOM   2083 C CA    . PRO A 1 275 ? 21.105  33.525  -9.519  1.00 28.87  ? 275  PRO A CA    1 
ATOM   2084 C C     . PRO A 1 275 ? 21.390  32.019  -9.536  1.00 28.75  ? 275  PRO A C     1 
ATOM   2085 O O     . PRO A 1 275 ? 20.624  31.261  -8.954  1.00 29.19  ? 275  PRO A O     1 
ATOM   2086 C CB    . PRO A 1 275 ? 21.381  34.219  -8.179  1.00 29.45  ? 275  PRO A CB    1 
ATOM   2087 C CG    . PRO A 1 275 ? 20.064  34.137  -7.418  1.00 31.78  ? 275  PRO A CG    1 
ATOM   2088 C CD    . PRO A 1 275 ? 18.963  33.938  -8.433  1.00 29.19  ? 275  PRO A CD    1 
ATOM   2089 N N     . VAL A 1 276 ? 22.471  31.627  -10.207 1.00 27.74  ? 276  VAL A N     1 
ATOM   2090 C CA    . VAL A 1 276 ? 22.970  30.227  -10.248 1.00 31.24  ? 276  VAL A CA    1 
ATOM   2091 C C     . VAL A 1 276 ? 24.405  30.191  -9.720  1.00 32.20  ? 276  VAL A C     1 
ATOM   2092 O O     . VAL A 1 276 ? 25.228  31.086  -10.099 1.00 34.14  ? 276  VAL A O     1 
ATOM   2093 C CB    . VAL A 1 276 ? 22.884  29.640  -11.668 1.00 31.51  ? 276  VAL A CB    1 
ATOM   2094 C CG1   . VAL A 1 276 ? 21.462  29.754  -12.203 1.00 34.42  ? 276  VAL A CG1   1 
ATOM   2095 C CG2   . VAL A 1 276 ? 23.880  30.282  -12.616 1.00 32.24  ? 276  VAL A CG2   1 
ATOM   2096 N N     . LEU A 1 277 ? 24.675  29.187  -8.893  1.00 31.70  ? 277  LEU A N     1 
ATOM   2097 C CA    . LEU A 1 277 ? 26.023  28.815  -8.399  1.00 30.59  ? 277  LEU A CA    1 
ATOM   2098 C C     . LEU A 1 277 ? 26.385  27.434  -8.949  1.00 28.61  ? 277  LEU A C     1 
ATOM   2099 O O     . LEU A 1 277 ? 25.855  26.462  -8.430  1.00 30.74  ? 277  LEU A O     1 
ATOM   2100 C CB    . LEU A 1 277 ? 25.990  28.802  -6.877  1.00 29.85  ? 277  LEU A CB    1 
ATOM   2101 C CG    . LEU A 1 277 ? 27.357  28.671  -6.212  1.00 28.05  ? 277  LEU A CG    1 
ATOM   2102 C CD1   . LEU A 1 277 ? 28.142  29.942  -6.428  1.00 29.42  ? 277  LEU A CD1   1 
ATOM   2103 C CD2   . LEU A 1 277 ? 27.204  28.378  -4.736  1.00 30.54  ? 277  LEU A CD2   1 
ATOM   2104 N N     . ARG A 1 278 ? 27.208  27.389  -9.990  1.00 28.51  ? 278  ARG A N     1 
ATOM   2105 C CA    . ARG A 1 278 ? 27.648  26.160  -10.686 1.00 32.81  ? 278  ARG A CA    1 
ATOM   2106 C C     . ARG A 1 278 ? 29.015  25.694  -10.145 1.00 33.88  ? 278  ARG A C     1 
ATOM   2107 O O     . ARG A 1 278 ? 29.908  26.546  -9.917  1.00 33.35  ? 278  ARG A O     1 
ATOM   2108 C CB    . ARG A 1 278 ? 27.693  26.459  -12.186 1.00 30.87  ? 278  ARG A CB    1 
ATOM   2109 C CG    . ARG A 1 278 ? 26.324  26.776  -12.779 1.00 33.40  ? 278  ARG A CG    1 
ATOM   2110 C CD    . ARG A 1 278 ? 26.428  27.504  -14.105 1.00 35.05  ? 278  ARG A CD    1 
ATOM   2111 N NE    . ARG A 1 278 ? 27.069  26.717  -15.143 1.00 35.69  ? 278  ARG A NE    1 
ATOM   2112 C CZ    . ARG A 1 278 ? 26.459  26.068  -16.140 1.00 39.75  ? 278  ARG A CZ    1 
ATOM   2113 N NH1   . ARG A 1 278 ? 25.141  26.053  -16.263 1.00 38.47  ? 278  ARG A NH1   1 
ATOM   2114 N NH2   . ARG A 1 278 ? 27.196  25.432  -17.030 1.00 40.53  ? 278  ARG A NH2   1 
ATOM   2115 N N     . ASN A 1 279 ? 29.168  24.388  -9.934  1.00 36.08  ? 279  ASN A N     1 
ATOM   2116 C CA    . ASN A 1 279 ? 30.444  23.768  -9.494  1.00 35.97  ? 279  ASN A CA    1 
ATOM   2117 C C     . ASN A 1 279 ? 31.398  23.757  -10.702 1.00 36.96  ? 279  ASN A C     1 
ATOM   2118 O O     . ASN A 1 279 ? 30.950  23.937  -11.868 1.00 31.23  ? 279  ASN A O     1 
ATOM   2119 C CB    . ASN A 1 279 ? 30.209  22.406  -8.837  1.00 40.17  ? 279  ASN A CB    1 
ATOM   2120 C CG    . ASN A 1 279 ? 30.252  21.256  -9.824  1.00 44.44  ? 279  ASN A CG    1 
ATOM   2121 O OD1   . ASN A 1 279 ? 31.156  20.434  -9.782  1.00 58.16  ? 279  ASN A OD1   1 
ATOM   2122 N ND2   . ASN A 1 279 ? 29.321  21.211  -10.745 1.00 40.61  ? 279  ASN A ND2   1 
ATOM   2123 N N     . ILE A 1 280 ? 32.674  23.547  -10.444 1.00 36.02  ? 280  ILE A N     1 
ATOM   2124 C CA    . ILE A 1 280 ? 33.693  23.545  -11.479 1.00 37.96  ? 280  ILE A CA    1 
ATOM   2125 C C     . ILE A 1 280 ? 33.416  22.573  -12.608 1.00 37.81  ? 280  ILE A C     1 
ATOM   2126 O O     . ILE A 1 280 ? 33.671  22.883  -13.728 1.00 36.88  ? 280  ILE A O     1 
ATOM   2127 C CB    . ILE A 1 280 ? 35.072  23.284  -10.818 1.00 44.25  ? 280  ILE A CB    1 
ATOM   2128 C CG1   . ILE A 1 280 ? 36.186  23.148  -11.838 1.00 48.78  ? 280  ILE A CG1   1 
ATOM   2129 C CG2   . ILE A 1 280 ? 35.030  22.057  -9.932  1.00 44.51  ? 280  ILE A CG2   1 
ATOM   2130 C CD1   . ILE A 1 280 ? 36.590  24.455  -12.449 1.00 54.65  ? 280  ILE A CD1   1 
ATOM   2131 N N     . ILE A 1 281 ? 32.848  21.422  -12.305 1.00 41.05  ? 281  ILE A N     1 
ATOM   2132 C CA    . ILE A 1 281 ? 32.575  20.409  -13.316 1.00 42.98  ? 281  ILE A CA    1 
ATOM   2133 C C     . ILE A 1 281 ? 31.536  20.830  -14.333 1.00 41.88  ? 281  ILE A C     1 
ATOM   2134 O O     . ILE A 1 281 ? 31.755  20.680  -15.499 1.00 35.51  ? 281  ILE A O     1 
ATOM   2135 C CB    . ILE A 1 281 ? 32.167  19.078  -12.692 1.00 50.93  ? 281  ILE A CB    1 
ATOM   2136 C CG1   . ILE A 1 281 ? 33.186  18.662  -11.652 1.00 53.01  ? 281  ILE A CG1   1 
ATOM   2137 C CG2   . ILE A 1 281 ? 32.076  17.986  -13.743 1.00 56.92  ? 281  ILE A CG2   1 
ATOM   2138 C CD1   . ILE A 1 281 ? 34.504  18.300  -12.261 1.00 61.23  ? 281  ILE A CD1   1 
ATOM   2139 N N     . LEU A 1 282 ? 30.426  21.369  -13.878 1.00 37.68  ? 282  LEU A N     1 
ATOM   2140 C CA    . LEU A 1 282 ? 29.375  21.788  -14.775 1.00 46.25  ? 282  LEU A CA    1 
ATOM   2141 C C     . LEU A 1 282 ? 29.945  22.868  -15.645 1.00 42.00  ? 282  LEU A C     1 
ATOM   2142 O O     . LEU A 1 282 ? 29.596  23.004  -16.803 1.00 42.81  ? 282  LEU A O     1 
ATOM   2143 C CB    . LEU A 1 282 ? 28.201  22.319  -13.959 1.00 50.96  ? 282  LEU A CB    1 
ATOM   2144 C CG    . LEU A 1 282 ? 26.807  22.355  -14.547 1.00 55.56  ? 282  LEU A CG    1 
ATOM   2145 C CD1   . LEU A 1 282 ? 26.337  20.942  -14.817 1.00 54.32  ? 282  LEU A CD1   1 
ATOM   2146 C CD2   . LEU A 1 282 ? 25.885  23.035  -13.561 1.00 69.54  ? 282  LEU A CD2   1 
ATOM   2147 N N     . ASP A 1 283 ? 30.860  23.606  -15.093 1.00 39.48  ? 283  ASP A N     1 
ATOM   2148 C CA    . ASP A 1 283 ? 31.503  24.752  -15.796 1.00 36.93  ? 283  ASP A CA    1 
ATOM   2149 C C     . ASP A 1 283 ? 32.591  24.224  -16.748 1.00 37.11  ? 283  ASP A C     1 
ATOM   2150 O O     . ASP A 1 283 ? 32.620  24.617  -17.934 1.00 40.76  ? 283  ASP A O     1 
ATOM   2151 C CB    . ASP A 1 283 ? 32.005  25.778  -14.779 1.00 39.67  ? 283  ASP A CB    1 
ATOM   2152 C CG    . ASP A 1 283 ? 31.180  27.048  -14.721 1.00 44.23  ? 283  ASP A CG    1 
ATOM   2153 O OD1   . ASP A 1 283 ? 29.934  26.978  -14.862 1.00 42.52  ? 283  ASP A OD1   1 
ATOM   2154 O OD2   . ASP A 1 283 ? 31.790  28.105  -14.582 1.00 49.69  ? 283  ASP A OD2   1 
ATOM   2155 N N     . ALA A 1 284 ? 33.463  23.336  -16.284 1.00 36.18  ? 284  ALA A N     1 
ATOM   2156 C CA    . ALA A 1 284 ? 34.572  22.780  -17.096 1.00 37.83  ? 284  ALA A CA    1 
ATOM   2157 C C     . ALA A 1 284 ? 34.025  21.947  -18.269 1.00 36.59  ? 284  ALA A C     1 
ATOM   2158 O O     . ALA A 1 284 ? 34.600  21.992  -19.356 1.00 34.94  ? 284  ALA A O     1 
ATOM   2159 C CB    . ALA A 1 284 ? 35.476  21.969  -16.206 1.00 40.88  ? 284  ALA A CB    1 
ATOM   2160 N N     . ALA A 1 285 ? 32.925  21.235  -18.054 1.00 36.94  ? 285  ALA A N     1 
ATOM   2161 C CA    . ALA A 1 285 ? 32.332  20.264  -19.004 1.00 39.21  ? 285  ALA A CA    1 
ATOM   2162 C C     . ALA A 1 285 ? 31.728  20.944  -20.241 1.00 39.41  ? 285  ALA A C     1 
ATOM   2163 O O     . ALA A 1 285 ? 31.518  20.229  -21.231 1.00 41.18  ? 285  ALA A O     1 
ATOM   2164 C CB    . ALA A 1 285 ? 31.316  19.408  -18.295 1.00 39.28  ? 285  ALA A CB    1 
ATOM   2165 N N     . VAL A 1 286 ? 31.478  22.252  -20.221 1.00 37.95  ? 286  VAL A N     1 
ATOM   2166 C CA    . VAL A 1 286 ? 30.988  22.982  -21.429 1.00 39.71  ? 286  VAL A CA    1 
ATOM   2167 C C     . VAL A 1 286 ? 32.166  23.243  -22.363 1.00 41.94  ? 286  VAL A C     1 
ATOM   2168 O O     . VAL A 1 286 ? 31.904  23.360  -23.566 1.00 39.38  ? 286  VAL A O     1 
ATOM   2169 C CB    . VAL A 1 286 ? 30.249  24.296  -21.098 1.00 42.53  ? 286  VAL A CB    1 
ATOM   2170 C CG1   . VAL A 1 286 ? 29.806  25.014  -22.363 1.00 46.55  ? 286  VAL A CG1   1 
ATOM   2171 C CG2   . VAL A 1 286 ? 29.040  24.074  -20.194 1.00 43.97  ? 286  VAL A CG2   1 
ATOM   2172 N N     . VAL A 1 287 ? 33.394  23.348  -21.831 1.00 41.70  ? 287  VAL A N     1 
ATOM   2173 C CA    . VAL A 1 287 ? 34.580  23.851  -22.581 1.00 41.30  ? 287  VAL A CA    1 
ATOM   2174 C C     . VAL A 1 287 ? 35.654  22.766  -22.685 1.00 43.80  ? 287  VAL A C     1 
ATOM   2175 O O     . VAL A 1 287 ? 36.699  23.036  -23.331 1.00 42.88  ? 287  VAL A O     1 
ATOM   2176 C CB    . VAL A 1 287 ? 35.149  25.131  -21.942 1.00 42.05  ? 287  VAL A CB    1 
ATOM   2177 C CG1   . VAL A 1 287 ? 34.108  26.220  -21.932 1.00 43.74  ? 287  VAL A CG1   1 
ATOM   2178 C CG2   . VAL A 1 287 ? 35.711  24.911  -20.544 1.00 41.00  ? 287  VAL A CG2   1 
ATOM   2179 N N     . SER A 1 288 ? 35.419  21.586  -22.109 1.00 40.29  ? 288  SER A N     1 
ATOM   2180 C CA    . SER A 1 288 ? 36.440  20.518  -22.023 1.00 37.23  ? 288  SER A CA    1 
ATOM   2181 C C     . SER A 1 288 ? 35.790  19.146  -21.842 1.00 40.15  ? 288  SER A C     1 
ATOM   2182 O O     . SER A 1 288 ? 34.567  19.068  -21.546 1.00 41.52  ? 288  SER A O     1 
ATOM   2183 C CB    . SER A 1 288 ? 37.396  20.841  -20.909 1.00 38.32  ? 288  SER A CB    1 
ATOM   2184 O OG    . SER A 1 288 ? 36.817  20.576  -19.638 1.00 36.86  ? 288  SER A OG    1 
ATOM   2185 N N     . GLN A 1 289 ? 36.589  18.090  -22.013 1.00 38.24  ? 289  GLN A N     1 
ATOM   2186 C CA    . GLN A 1 289 ? 36.153  16.681  -21.865 1.00 38.64  ? 289  GLN A CA    1 
ATOM   2187 C C     . GLN A 1 289 ? 36.813  16.072  -20.618 1.00 36.82  ? 289  GLN A C     1 
ATOM   2188 O O     . GLN A 1 289 ? 37.863  16.558  -20.181 1.00 41.36  ? 289  GLN A O     1 
ATOM   2189 C CB    . GLN A 1 289 ? 36.439  15.941  -23.171 1.00 44.18  ? 289  GLN A CB    1 
ATOM   2190 C CG    . GLN A 1 289 ? 36.008  16.730  -24.404 1.00 48.12  ? 289  GLN A CG    1 
ATOM   2191 C CD    . GLN A 1 289 ? 35.943  15.863  -25.634 1.00 53.91  ? 289  GLN A CD    1 
ATOM   2192 O OE1   . GLN A 1 289 ? 35.671  16.336  -26.729 1.00 65.91  ? 289  GLN A OE1   1 
ATOM   2193 N NE2   . GLN A 1 289 ? 36.175  14.573  -25.465 1.00 55.98  ? 289  GLN A NE2   1 
ATOM   2194 N N     . ARG A 1 290 ? 36.190  15.055  -20.040 1.00 35.88  ? 290  ARG A N     1 
ATOM   2195 C CA    . ARG A 1 290 ? 36.664  14.414  -18.795 1.00 35.44  ? 290  ARG A CA    1 
ATOM   2196 C C     . ARG A 1 290 ? 38.105  13.890  -18.995 1.00 40.43  ? 290  ARG A C     1 
ATOM   2197 O O     . ARG A 1 290 ? 38.919  14.081  -18.078 1.00 35.10  ? 290  ARG A O     1 
ATOM   2198 C CB    . ARG A 1 290 ? 35.718  13.288  -18.394 1.00 34.55  ? 290  ARG A CB    1 
ATOM   2199 C CG    . ARG A 1 290 ? 35.837  12.869  -16.943 1.00 31.76  ? 290  ARG A CG    1 
ATOM   2200 C CD    . ARG A 1 290 ? 35.055  11.622  -16.654 1.00 32.45  ? 290  ARG A CD    1 
ATOM   2201 N NE    . ARG A 1 290 ? 34.929  11.323  -15.229 1.00 33.22  ? 290  ARG A NE    1 
ATOM   2202 C CZ    . ARG A 1 290 ? 35.649  10.422  -14.567 1.00 33.83  ? 290  ARG A CZ    1 
ATOM   2203 N NH1   . ARG A 1 290 ? 36.616  9.761   -15.174 1.00 37.05  ? 290  ARG A NH1   1 
ATOM   2204 N NH2   . ARG A 1 290 ? 35.420  10.199  -13.292 1.00 32.80  ? 290  ARG A NH2   1 
ATOM   2205 N N     . ALA A 1 291 ? 38.392  13.282  -20.155 1.00 45.12  ? 291  ALA A N     1 
ATOM   2206 C CA    . ALA A 1 291 ? 39.684  12.651  -20.530 1.00 47.15  ? 291  ALA A CA    1 
ATOM   2207 C C     . ALA A 1 291 ? 40.818  13.691  -20.528 1.00 51.38  ? 291  ALA A C     1 
ATOM   2208 O O     . ALA A 1 291 ? 41.961  13.299  -20.280 1.00 53.18  ? 291  ALA A O     1 
ATOM   2209 C CB    . ALA A 1 291 ? 39.543  11.979  -21.869 1.00 46.78  ? 291  ALA A CB    1 
ATOM   2210 N N     . ASP A 1 292 ? 40.505  14.970  -20.757 1.00 51.28  ? 292  ASP A N     1 
ATOM   2211 C CA    . ASP A 1 292 ? 41.472  16.099  -20.715 1.00 51.29  ? 292  ASP A CA    1 
ATOM   2212 C C     . ASP A 1 292 ? 42.080  16.279  -19.311 1.00 56.65  ? 292  ASP A C     1 
ATOM   2213 O O     . ASP A 1 292 ? 43.165  16.873  -19.243 1.00 58.76  ? 292  ASP A O     1 
ATOM   2214 C CB    . ASP A 1 292 ? 40.822  17.413  -21.155 1.00 50.43  ? 292  ASP A CB    1 
ATOM   2215 C CG    . ASP A 1 292 ? 40.162  17.346  -22.523 1.00 54.17  ? 292  ASP A CG    1 
ATOM   2216 O OD1   . ASP A 1 292 ? 40.365  16.343  -23.230 1.00 58.29  ? 292  ASP A OD1   1 
ATOM   2217 O OD2   . ASP A 1 292 ? 39.424  18.287  -22.860 1.00 53.03  ? 292  ASP A OD2   1 
ATOM   2218 N N     . TRP A 1 293 ? 41.411  15.831  -18.240 1.00 48.15  ? 293  TRP A N     1 
ATOM   2219 C CA    . TRP A 1 293 ? 41.772  16.147  -16.829 1.00 47.88  ? 293  TRP A CA    1 
ATOM   2220 C C     . TRP A 1 293 ? 42.192  14.880  -16.098 1.00 48.79  ? 293  TRP A C     1 
ATOM   2221 O O     . TRP A 1 293 ? 42.861  14.988  -15.063 1.00 47.18  ? 293  TRP A O     1 
ATOM   2222 C CB    . TRP A 1 293 ? 40.594  16.811  -16.113 1.00 43.51  ? 293  TRP A CB    1 
ATOM   2223 C CG    . TRP A 1 293 ? 40.068  17.968  -16.892 1.00 44.96  ? 293  TRP A CG    1 
ATOM   2224 C CD1   . TRP A 1 293 ? 38.934  18.000  -17.644 1.00 43.33  ? 293  TRP A CD1   1 
ATOM   2225 C CD2   . TRP A 1 293 ? 40.725  19.232  -17.091 1.00 48.20  ? 293  TRP A CD2   1 
ATOM   2226 N NE1   . TRP A 1 293 ? 38.821  19.208  -18.269 1.00 45.92  ? 293  TRP A NE1   1 
ATOM   2227 C CE2   . TRP A 1 293 ? 39.900  19.986  -17.950 1.00 45.49  ? 293  TRP A CE2   1 
ATOM   2228 C CE3   . TRP A 1 293 ? 41.917  19.801  -16.620 1.00 48.02  ? 293  TRP A CE3   1 
ATOM   2229 C CZ2   . TRP A 1 293 ? 40.229  21.279  -18.346 1.00 48.34  ? 293  TRP A CZ2   1 
ATOM   2230 C CZ3   . TRP A 1 293 ? 42.244  21.078  -17.016 1.00 47.51  ? 293  TRP A CZ3   1 
ATOM   2231 C CH2   . TRP A 1 293 ? 41.411  21.803  -17.870 1.00 50.06  ? 293  TRP A CH2   1 
ATOM   2232 N N     . TYR A 1 294 ? 41.790  13.736  -16.631 1.00 47.94  ? 294  TYR A N     1 
ATOM   2233 C CA    . TYR A 1 294 ? 41.833  12.439  -15.932 1.00 52.79  ? 294  TYR A CA    1 
ATOM   2234 C C     . TYR A 1 294 ? 41.411  11.335  -16.900 1.00 63.09  ? 294  TYR A C     1 
ATOM   2235 O O     . TYR A 1 294 ? 40.403  11.506  -17.608 1.00 67.33  ? 294  TYR A O     1 
ATOM   2236 C CB    . TYR A 1 294 ? 40.909  12.487  -14.722 1.00 51.74  ? 294  TYR A CB    1 
ATOM   2237 C CG    . TYR A 1 294 ? 41.133  11.341  -13.785 1.00 49.05  ? 294  TYR A CG    1 
ATOM   2238 C CD1   . TYR A 1 294 ? 42.377  11.151  -13.208 1.00 50.69  ? 294  TYR A CD1   1 
ATOM   2239 C CD2   . TYR A 1 294 ? 40.129  10.439  -13.498 1.00 46.80  ? 294  TYR A CD2   1 
ATOM   2240 C CE1   . TYR A 1 294 ? 42.615  10.096  -12.348 1.00 50.96  ? 294  TYR A CE1   1 
ATOM   2241 C CE2   . TYR A 1 294 ? 40.349  9.378   -12.635 1.00 53.71  ? 294  TYR A CE2   1 
ATOM   2242 C CZ    . TYR A 1 294 ? 41.599  9.207   -12.066 1.00 51.65  ? 294  TYR A CZ    1 
ATOM   2243 O OH    . TYR A 1 294 ? 41.829  8.170   -11.217 1.00 65.81  ? 294  TYR A OH    1 
ATOM   2244 N N     . ASP A 1 295 ? 42.168  10.245  -16.949 1.00 66.17  ? 295  ASP A N     1 
ATOM   2245 C CA    . ASP A 1 295 ? 41.843  9.104   -17.843 1.00 76.03  ? 295  ASP A CA    1 
ATOM   2246 C C     . ASP A 1 295 ? 41.852  7.800   -17.037 1.00 78.63  ? 295  ASP A C     1 
ATOM   2247 O O     . ASP A 1 295 ? 41.701  6.729   -17.663 1.00 80.42  ? 295  ASP A O     1 
ATOM   2248 C CB    . ASP A 1 295 ? 42.788  9.079   -19.047 1.00 79.89  ? 295  ASP A CB    1 
ATOM   2249 C CG    . ASP A 1 295 ? 44.248  8.903   -18.667 1.00 82.35  ? 295  ASP A CG    1 
ATOM   2250 O OD1   . ASP A 1 295 ? 44.523  8.157   -17.702 1.00 80.28  ? 295  ASP A OD1   1 
ATOM   2251 O OD2   . ASP A 1 295 ? 45.097  9.514   -19.336 1.00 88.40  ? 295  ASP A OD2   1 
ATOM   2252 N N     . GLY A 1 296 ? 42.005  7.890   -15.710 1.00 74.46  ? 296  GLY A N     1 
ATOM   2253 C CA    . GLY A 1 296 ? 41.961  6.742   -14.783 1.00 70.49  ? 296  GLY A CA    1 
ATOM   2254 C C     . GLY A 1 296 ? 40.535  6.358   -14.429 1.00 71.07  ? 296  GLY A C     1 
ATOM   2255 O O     . GLY A 1 296 ? 39.599  7.071   -14.829 1.00 72.95  ? 296  GLY A O     1 
ATOM   2256 N N     . ASP A 1 297 ? 40.373  5.265   -13.686 1.00 72.87  ? 297  ASP A N     1 
ATOM   2257 C CA    . ASP A 1 297 ? 39.050  4.782   -13.206 1.00 73.70  ? 297  ASP A CA    1 
ATOM   2258 C C     . ASP A 1 297 ? 38.747  5.491   -11.882 1.00 64.82  ? 297  ASP A C     1 
ATOM   2259 O O     . ASP A 1 297 ? 39.632  6.207   -11.376 1.00 62.73  ? 297  ASP A O     1 
ATOM   2260 C CB    . ASP A 1 297 ? 39.018  3.254   -13.113 1.00 80.42  ? 297  ASP A CB    1 
ATOM   2261 C CG    . ASP A 1 297 ? 40.350  2.655   -12.699 1.00 84.70  ? 297  ASP A CG    1 
ATOM   2262 O OD1   . ASP A 1 297 ? 41.133  3.385   -12.057 1.00 86.53  ? 297  ASP A OD1   1 
ATOM   2263 O OD2   . ASP A 1 297 ? 40.603  1.478   -13.041 1.00 86.55  ? 297  ASP A OD2   1 
ATOM   2264 N N     . GLY A 1 298 ? 37.533  5.326   -11.364 1.00 59.14  ? 298  GLY A N     1 
ATOM   2265 C CA    . GLY A 1 298 ? 37.078  5.967   -10.116 1.00 51.64  ? 298  GLY A CA    1 
ATOM   2266 C C     . GLY A 1 298 ? 36.728  7.437   -10.322 1.00 49.00  ? 298  GLY A C     1 
ATOM   2267 O O     . GLY A 1 298 ? 36.892  7.984   -11.415 1.00 45.46  ? 298  GLY A O     1 
ATOM   2268 N N     . PRO A 1 299 ? 36.207  8.113   -9.272  1.00 47.53  ? 299  PRO A N     1 
ATOM   2269 C CA    . PRO A 1 299 ? 35.922  9.542   -9.339  1.00 43.36  ? 299  PRO A CA    1 
ATOM   2270 C C     . PRO A 1 299 ? 37.157  10.368  -9.715  1.00 43.23  ? 299  PRO A C     1 
ATOM   2271 O O     . PRO A 1 299 ? 38.256  9.887   -9.582  1.00 45.61  ? 299  PRO A O     1 
ATOM   2272 C CB    . PRO A 1 299 ? 35.427  9.949   -7.937  1.00 43.75  ? 299  PRO A CB    1 
ATOM   2273 C CG    . PRO A 1 299 ? 35.381  8.677   -7.112  1.00 49.69  ? 299  PRO A CG    1 
ATOM   2274 C CD    . PRO A 1 299 ? 35.793  7.515   -7.998  1.00 48.03  ? 299  PRO A CD    1 
ATOM   2275 N N     . LEU A 1 300 ? 36.926  11.588  -10.197 1.00 43.08  ? 300  LEU A N     1 
ATOM   2276 C CA    . LEU A 1 300 ? 37.979  12.583  -10.490 1.00 40.40  ? 300  LEU A CA    1 
ATOM   2277 C C     . LEU A 1 300 ? 38.698  12.889  -9.183  1.00 46.59  ? 300  LEU A C     1 
ATOM   2278 O O     . LEU A 1 300 ? 38.054  13.208  -8.189  1.00 42.50  ? 300  LEU A O     1 
ATOM   2279 C CB    . LEU A 1 300 ? 37.349  13.852  -11.043 1.00 40.35  ? 300  LEU A CB    1 
ATOM   2280 C CG    . LEU A 1 300 ? 36.729  13.737  -12.429 1.00 40.19  ? 300  LEU A CG    1 
ATOM   2281 C CD1   . LEU A 1 300 ? 35.775  14.911  -12.661 1.00 39.45  ? 300  LEU A CD1   1 
ATOM   2282 C CD2   . LEU A 1 300 ? 37.820  13.676  -13.503 1.00 39.70  ? 300  LEU A CD2   1 
ATOM   2283 N N     . PRO A 1 301 ? 40.043  12.776  -9.132  1.00 46.11  ? 301  PRO A N     1 
ATOM   2284 C CA    . PRO A 1 301 ? 40.781  13.096  -7.910  1.00 46.27  ? 301  PRO A CA    1 
ATOM   2285 C C     . PRO A 1 301 ? 40.858  14.609  -7.691  1.00 44.01  ? 301  PRO A C     1 
ATOM   2286 O O     . PRO A 1 301 ? 40.704  15.378  -8.640  1.00 44.51  ? 301  PRO A O     1 
ATOM   2287 C CB    . PRO A 1 301 ? 42.146  12.431  -8.161  1.00 42.81  ? 301  PRO A CB    1 
ATOM   2288 C CG    . PRO A 1 301 ? 42.310  12.464  -9.665  1.00 44.26  ? 301  PRO A CG    1 
ATOM   2289 C CD    . PRO A 1 301 ? 40.909  12.299  -10.224 1.00 45.75  ? 301  PRO A CD    1 
ATOM   2290 N N     . PRO A 1 302 ? 41.057  15.076  -6.431  1.00 43.76  ? 302  PRO A N     1 
ATOM   2291 C CA    . PRO A 1 302 ? 41.177  16.500  -6.125  1.00 41.68  ? 302  PRO A CA    1 
ATOM   2292 C C     . PRO A 1 302 ? 42.111  17.306  -7.025  1.00 38.82  ? 302  PRO A C     1 
ATOM   2293 O O     . PRO A 1 302 ? 41.799  18.426  -7.286  1.00 40.26  ? 302  PRO A O     1 
ATOM   2294 C CB    . PRO A 1 302 ? 41.737  16.481  -4.699  1.00 44.15  ? 302  PRO A CB    1 
ATOM   2295 C CG    . PRO A 1 302 ? 41.056  15.283  -4.092  1.00 44.91  ? 302  PRO A CG    1 
ATOM   2296 C CD    . PRO A 1 302 ? 41.094  14.260  -5.208  1.00 43.02  ? 302  PRO A CD    1 
ATOM   2297 N N     . GLU A 1 303 ? 43.233  16.730  -7.440  1.00 42.00  ? 303  GLU A N     1 
ATOM   2298 C CA    . GLU A 1 303 ? 44.267  17.449  -8.235  1.00 44.83  ? 303  GLU A CA    1 
ATOM   2299 C C     . GLU A 1 303 ? 43.732  17.661  -9.655  1.00 42.11  ? 303  GLU A C     1 
ATOM   2300 O O     . GLU A 1 303 ? 44.094  18.679  -10.261 1.00 39.74  ? 303  GLU A O     1 
ATOM   2301 C CB    . GLU A 1 303 ? 45.616  16.714  -8.233  1.00 52.11  ? 303  GLU A CB    1 
ATOM   2302 C CG    . GLU A 1 303 ? 45.538  15.215  -8.462  1.00 57.99  ? 303  GLU A CG    1 
ATOM   2303 C CD    . GLU A 1 303 ? 45.350  14.361  -7.213  1.00 67.49  ? 303  GLU A CD    1 
ATOM   2304 O OE1   . GLU A 1 303 ? 45.682  13.162  -7.280  1.00 77.97  ? 303  GLU A OE1   1 
ATOM   2305 O OE2   . GLU A 1 303 ? 44.836  14.877  -6.189  1.00 70.01  ? 303  GLU A OE2   1 
ATOM   2306 N N     . ALA A 1 304 ? 42.877  16.755  -10.150 1.00 41.78  ? 304  ALA A N     1 
ATOM   2307 C CA    . ALA A 1 304 ? 42.151  16.918  -11.435 1.00 45.15  ? 304  ALA A CA    1 
ATOM   2308 C C     . ALA A 1 304 ? 41.245  18.150  -11.324 1.00 41.16  ? 304  ALA A C     1 
ATOM   2309 O O     . ALA A 1 304 ? 41.321  19.040  -12.193 1.00 43.34  ? 304  ALA A O     1 
ATOM   2310 C CB    . ALA A 1 304 ? 41.373  15.664  -11.766 1.00 46.44  ? 304  ALA A CB    1 
ATOM   2311 N N     . ILE A 1 305 ? 40.481  18.231  -10.233 1.00 44.78  ? 305  ILE A N     1 
ATOM   2312 C CA    . ILE A 1 305 ? 39.623  19.407  -9.900  1.00 44.37  ? 305  ILE A CA    1 
ATOM   2313 C C     . ILE A 1 305 ? 40.517  20.641  -9.853  1.00 43.55  ? 305  ILE A C     1 
ATOM   2314 O O     . ILE A 1 305 ? 40.189  21.646  -10.516 1.00 41.77  ? 305  ILE A O     1 
ATOM   2315 C CB    . ILE A 1 305 ? 38.881  19.227  -8.561  1.00 44.75  ? 305  ILE A CB    1 
ATOM   2316 C CG1   . ILE A 1 305 ? 37.951  18.009  -8.550  1.00 50.38  ? 305  ILE A CG1   1 
ATOM   2317 C CG2   . ILE A 1 305 ? 38.159  20.514  -8.188  1.00 46.96  ? 305  ILE A CG2   1 
ATOM   2318 C CD1   . ILE A 1 305 ? 37.308  17.672  -9.862  1.00 47.01  ? 305  ILE A CD1   1 
ATOM   2319 N N     . GLU A 1 306 ? 41.612  20.568  -9.098  1.00 41.05  ? 306  GLU A N     1 
ATOM   2320 C CA    . GLU A 1 306 ? 42.505  21.736  -8.890  1.00 41.46  ? 306  GLU A CA    1 
ATOM   2321 C C     . GLU A 1 306 ? 43.023  22.224  -10.245 1.00 36.85  ? 306  GLU A C     1 
ATOM   2322 O O     . GLU A 1 306 ? 43.005  23.418  -10.459 1.00 39.04  ? 306  GLU A O     1 
ATOM   2323 C CB    . GLU A 1 306 ? 43.605  21.386  -7.884  1.00 44.02  ? 306  GLU A CB    1 
ATOM   2324 C CG    . GLU A 1 306 ? 43.108  21.365  -6.453  1.00 47.24  ? 306  GLU A CG    1 
ATOM   2325 C CD    . GLU A 1 306 ? 42.299  22.584  -6.044  1.00 50.07  ? 306  GLU A CD    1 
ATOM   2326 O OE1   . GLU A 1 306 ? 42.657  23.692  -6.461  1.00 56.44  ? 306  GLU A OE1   1 
ATOM   2327 O OE2   . GLU A 1 306 ? 41.297  22.418  -5.322  1.00 56.03  ? 306  GLU A OE2   1 
ATOM   2328 N N     . ARG A 1 307 ? 43.433  21.319  -11.125 1.00 43.27  ? 307  ARG A N     1 
ATOM   2329 C CA    . ARG A 1 307 ? 43.916  21.612  -12.511 1.00 47.00  ? 307  ARG A CA    1 
ATOM   2330 C C     . ARG A 1 307 ? 42.828  22.275  -13.371 1.00 46.76  ? 307  ARG A C     1 
ATOM   2331 O O     . ARG A 1 307 ? 43.205  23.059  -14.255 1.00 44.02  ? 307  ARG A O     1 
ATOM   2332 C CB    . ARG A 1 307 ? 44.352  20.330  -13.229 1.00 47.79  ? 307  ARG A CB    1 
ATOM   2333 C CG    . ARG A 1 307 ? 45.855  20.101  -13.252 1.00 53.65  ? 307  ARG A CG    1 
ATOM   2334 C CD    . ARG A 1 307 ? 46.267  19.061  -14.278 1.00 57.64  ? 307  ARG A CD    1 
ATOM   2335 N NE    . ARG A 1 307 ? 45.525  17.804  -14.197 1.00 55.27  ? 307  ARG A NE    1 
ATOM   2336 C CZ    . ARG A 1 307 ? 45.652  16.920  -13.210 1.00 58.53  ? 307  ARG A CZ    1 
ATOM   2337 N NH1   . ARG A 1 307 ? 46.471  17.156  -12.196 1.00 62.64  ? 307  ARG A NH1   1 
ATOM   2338 N NH2   . ARG A 1 307 ? 44.949  15.804  -13.222 1.00 53.76  ? 307  ARG A NH2   1 
ATOM   2339 N N     . MET A 1 308 ? 41.550  21.914  -13.194 1.00 44.53  ? 308  MET A N     1 
ATOM   2340 C CA    . MET A 1 308 ? 40.404  22.585  -13.878 1.00 42.11  ? 308  MET A CA    1 
ATOM   2341 C C     . MET A 1 308 ? 40.308  24.039  -13.387 1.00 41.38  ? 308  MET A C     1 
ATOM   2342 O O     . MET A 1 308 ? 40.261  24.946  -14.226 1.00 40.47  ? 308  MET A O     1 
ATOM   2343 C CB    . MET A 1 308 ? 39.079  21.869  -13.597 1.00 40.98  ? 308  MET A CB    1 
ATOM   2344 C CG    . MET A 1 308 ? 38.928  20.549  -14.308 1.00 42.14  ? 308  MET A CG    1 
ATOM   2345 S SD    . MET A 1 308 ? 37.553  19.603  -13.597 1.00 43.55  ? 308  MET A SD    1 
ATOM   2346 C CE    . MET A 1 308 ? 37.855  17.976  -14.285 1.00 51.90  ? 308  MET A CE    1 
ATOM   2347 N N     . LYS A 1 309 ? 40.313  24.250  -12.066 1.00 38.41  ? 309  LYS A N     1 
ATOM   2348 C CA    . LYS A 1 309 ? 40.246  25.597  -11.453 1.00 40.64  ? 309  LYS A CA    1 
ATOM   2349 C C     . LYS A 1 309 ? 41.328  26.484  -12.070 1.00 42.58  ? 309  LYS A C     1 
ATOM   2350 O O     . LYS A 1 309 ? 40.970  27.567  -12.608 1.00 40.49  ? 309  LYS A O     1 
ATOM   2351 C CB    . LYS A 1 309 ? 40.451  25.539  -9.939  1.00 42.19  ? 309  LYS A CB    1 
ATOM   2352 C CG    . LYS A 1 309 ? 39.382  24.815  -9.138  1.00 46.75  ? 309  LYS A CG    1 
ATOM   2353 C CD    . LYS A 1 309 ? 39.761  24.823  -7.679  1.00 50.29  ? 309  LYS A CD    1 
ATOM   2354 C CE    . LYS A 1 309 ? 38.671  24.340  -6.758  1.00 57.77  ? 309  LYS A CE    1 
ATOM   2355 N NZ    . LYS A 1 309 ? 39.182  24.066  -5.390  1.00 60.58  ? 309  LYS A NZ    1 
ATOM   2356 N N     . LYS A 1 310 ? 42.597  26.057  -11.967 1.00 43.45  ? 310  LYS A N     1 
ATOM   2357 C CA    . LYS A 1 310 ? 43.787  26.820  -12.443 1.00 46.71  ? 310  LYS A CA    1 
ATOM   2358 C C     . LYS A 1 310 ? 43.734  27.018  -13.961 1.00 43.61  ? 310  LYS A C     1 
ATOM   2359 O O     . LYS A 1 310 ? 43.787  28.183  -14.420 1.00 52.08  ? 310  LYS A O     1 
ATOM   2360 C CB    . LYS A 1 310 ? 45.096  26.105  -12.087 1.00 51.76  ? 310  LYS A CB    1 
ATOM   2361 C CG    . LYS A 1 310 ? 46.346  26.987  -12.123 1.00 59.68  ? 310  LYS A CG    1 
ATOM   2362 C CD    . LYS A 1 310 ? 46.420  27.988  -10.970 1.00 64.31  ? 310  LYS A CD    1 
ATOM   2363 C CE    . LYS A 1 310 ? 47.832  28.392  -10.606 1.00 63.87  ? 310  LYS A CE    1 
ATOM   2364 N NZ    . LYS A 1 310 ? 48.331  29.507  -11.438 1.00 68.99  ? 310  LYS A NZ    1 
ATOM   2365 N N     . GLU A 1 311 ? 43.690  25.927  -14.720 1.00 45.39  ? 311  GLU A N     1 
ATOM   2366 C CA    . GLU A 1 311 ? 43.794  25.959  -16.204 1.00 43.87  ? 311  GLU A CA    1 
ATOM   2367 C C     . GLU A 1 311 ? 42.677  26.840  -16.795 1.00 44.89  ? 311  GLU A C     1 
ATOM   2368 O O     . GLU A 1 311 ? 42.980  27.555  -17.745 1.00 40.08  ? 311  GLU A O     1 
ATOM   2369 C CB    . GLU A 1 311 ? 43.809  24.531  -16.741 1.00 51.86  ? 311  GLU A CB    1 
ATOM   2370 C CG    . GLU A 1 311 ? 43.848  24.422  -18.256 1.00 63.53  ? 311  GLU A CG    1 
ATOM   2371 C CD    . GLU A 1 311 ? 45.172  24.741  -18.922 1.00 72.51  ? 311  GLU A CD    1 
ATOM   2372 O OE1   . GLU A 1 311 ? 45.844  25.695  -18.484 1.00 79.74  ? 311  GLU A OE1   1 
ATOM   2373 O OE2   . GLU A 1 311 ? 45.521  24.031  -19.888 1.00 81.10  ? 311  GLU A OE2   1 
ATOM   2374 N N     . LEU A 1 312 ? 41.443  26.800  -16.260 1.00 47.00  ? 312  LEU A N     1 
ATOM   2375 C CA    . LEU A 1 312 ? 40.256  27.530  -16.818 1.00 49.05  ? 312  LEU A CA    1 
ATOM   2376 C C     . LEU A 1 312 ? 39.985  28.845  -16.068 1.00 43.91  ? 312  LEU A C     1 
ATOM   2377 O O     . LEU A 1 312 ? 39.052  29.569  -16.463 1.00 49.35  ? 312  LEU A O     1 
ATOM   2378 C CB    . LEU A 1 312 ? 39.027  26.614  -16.765 1.00 47.23  ? 312  LEU A CB    1 
ATOM   2379 C CG    . LEU A 1 312 ? 39.182  25.293  -17.507 1.00 47.71  ? 312  LEU A CG    1 
ATOM   2380 C CD1   . LEU A 1 312 ? 38.143  24.282  -17.052 1.00 49.84  ? 312  LEU A CD1   1 
ATOM   2381 C CD2   . LEU A 1 312 ? 39.126  25.503  -19.018 1.00 49.10  ? 312  LEU A CD2   1 
ATOM   2382 N N     . GLY A 1 313 ? 40.727  29.144  -15.026 1.00 44.43  ? 313  GLY A N     1 
ATOM   2383 C CA    . GLY A 1 313 ? 40.507  30.352  -14.268 1.00 42.74  ? 313  GLY A CA    1 
ATOM   2384 C C     . GLY A 1 313 ? 39.183  30.356  -13.563 1.00 44.53  ? 313  GLY A C     1 
ATOM   2385 O O     . GLY A 1 313 ? 38.487  31.349  -13.571 1.00 45.45  ? 313  GLY A O     1 
ATOM   2386 N N     . LEU A 1 314 ? 38.832  29.250  -12.935 1.00 46.86  ? 314  LEU A N     1 
ATOM   2387 C CA    . LEU A 1 314 ? 37.541  29.132  -12.302 1.00 45.34  ? 314  LEU A CA    1 
ATOM   2388 C C     . LEU A 1 314 ? 37.629  28.745  -10.859 1.00 45.05  ? 314  LEU A C     1 
ATOM   2389 O O     . LEU A 1 314 ? 38.662  28.341  -10.388 1.00 43.87  ? 314  LEU A O     1 
ATOM   2390 C CB    . LEU A 1 314 ? 36.718  28.079  -13.036 1.00 44.49  ? 314  LEU A CB    1 
ATOM   2391 C CG    . LEU A 1 314 ? 36.232  28.348  -14.452 1.00 48.52  ? 314  LEU A CG    1 
ATOM   2392 C CD1   . LEU A 1 314 ? 35.557  27.128  -15.040 1.00 53.80  ? 314  LEU A CD1   1 
ATOM   2393 C CD2   . LEU A 1 314 ? 35.284  29.518  -14.450 1.00 47.22  ? 314  LEU A CD2   1 
ATOM   2394 N N     . GLY A 1 315 ? 36.536  28.864  -10.144 1.00 36.77  ? 315  GLY A N     1 
ATOM   2395 C CA    . GLY A 1 315 ? 36.513  28.414  -8.787  1.00 36.58  ? 315  GLY A CA    1 
ATOM   2396 C C     . GLY A 1 315 ? 35.807  27.096  -8.690  1.00 33.79  ? 315  GLY A C     1 
ATOM   2397 O O     . GLY A 1 315 ? 35.376  26.592  -9.696  1.00 34.87  ? 315  GLY A O     1 
ATOM   2398 N N     . TYR A 1 316 ? 35.732  26.515  -7.499  1.00 35.51  ? 316  TYR A N     1 
ATOM   2399 C CA    . TYR A 1 316 ? 34.966  25.299  -7.328  1.00 35.15  ? 316  TYR A CA    1 
ATOM   2400 C C     . TYR A 1 316 ? 33.532  25.710  -7.523  1.00 34.83  ? 316  TYR A C     1 
ATOM   2401 O O     . TYR A 1 316 ? 32.796  25.007  -8.114  1.00 36.28  ? 316  TYR A O     1 
ATOM   2402 C CB    . TYR A 1 316 ? 35.135  24.619  -5.973  1.00 35.06  ? 316  TYR A CB    1 
ATOM   2403 C CG    . TYR A 1 316 ? 34.445  23.279  -5.943  1.00 36.59  ? 316  TYR A CG    1 
ATOM   2404 C CD1   . TYR A 1 316 ? 35.094  22.135  -6.354  1.00 34.21  ? 316  TYR A CD1   1 
ATOM   2405 C CD2   . TYR A 1 316 ? 33.123  23.168  -5.555  1.00 37.17  ? 316  TYR A CD2   1 
ATOM   2406 C CE1   . TYR A 1 316 ? 34.450  20.919  -6.362  1.00 33.54  ? 316  TYR A CE1   1 
ATOM   2407 C CE2   . TYR A 1 316 ? 32.474  21.967  -5.569  1.00 36.56  ? 316  TYR A CE2   1 
ATOM   2408 C CZ    . TYR A 1 316 ? 33.140  20.844  -5.968  1.00 36.25  ? 316  TYR A CZ    1 
ATOM   2409 O OH    . TYR A 1 316 ? 32.475  19.654  -5.964  1.00 34.91  ? 316  TYR A OH    1 
ATOM   2410 N N     . TRP A 1 317 ? 33.162  26.840  -6.997  1.00 31.42  ? 317  TRP A N     1 
ATOM   2411 C CA    . TRP A 1 317 ? 31.800  27.417  -7.169  1.00 34.45  ? 317  TRP A CA    1 
ATOM   2412 C C     . TRP A 1 317 ? 31.892  28.709  -7.993  1.00 33.53  ? 317  TRP A C     1 
ATOM   2413 O O     . TRP A 1 317 ? 32.744  29.588  -7.680  1.00 33.32  ? 317  TRP A O     1 
ATOM   2414 C CB    . TRP A 1 317 ? 31.158  27.686  -5.809  1.00 32.69  ? 317  TRP A CB    1 
ATOM   2415 C CG    . TRP A 1 317 ? 30.928  26.466  -4.976  1.00 33.59  ? 317  TRP A CG    1 
ATOM   2416 C CD1   . TRP A 1 317 ? 31.560  26.131  -3.813  1.00 31.73  ? 317  TRP A CD1   1 
ATOM   2417 C CD2   . TRP A 1 317 ? 29.998  25.405  -5.244  1.00 32.08  ? 317  TRP A CD2   1 
ATOM   2418 N NE1   . TRP A 1 317 ? 31.087  24.942  -3.343  1.00 31.63  ? 317  TRP A NE1   1 
ATOM   2419 C CE2   . TRP A 1 317 ? 30.116  24.478  -4.187  1.00 30.83  ? 317  TRP A CE2   1 
ATOM   2420 C CE3   . TRP A 1 317 ? 29.100  25.138  -6.281  1.00 32.13  ? 317  TRP A CE3   1 
ATOM   2421 C CZ2   . TRP A 1 317 ? 29.349  23.318  -4.123  1.00 31.77  ? 317  TRP A CZ2   1 
ATOM   2422 C CZ3   . TRP A 1 317 ? 28.346  23.992  -6.223  1.00 29.53  ? 317  TRP A CZ3   1 
ATOM   2423 C CH2   . TRP A 1 317 ? 28.465  23.096  -5.157  1.00 32.67  ? 317  TRP A CH2   1 
ATOM   2424 N N     . ASN A 1 318 ? 31.063  28.800  -9.029  1.00 31.67  ? 318  ASN A N     1 
ATOM   2425 C CA    . ASN A 1 318 ? 31.029  29.910  -10.005 1.00 33.40  ? 318  ASN A CA    1 
ATOM   2426 C C     . ASN A 1 318 ? 29.605  30.475  -10.063 1.00 35.25  ? 318  ASN A C     1 
ATOM   2427 O O     . ASN A 1 318 ? 28.678  29.779  -10.550 1.00 34.55  ? 318  ASN A O     1 
ATOM   2428 C CB    . ASN A 1 318 ? 31.585  29.424  -11.335 1.00 35.07  ? 318  ASN A CB    1 
ATOM   2429 C CG    . ASN A 1 318 ? 32.943  28.796  -11.110 1.00 39.27  ? 318  ASN A CG    1 
ATOM   2430 O OD1   . ASN A 1 318 ? 33.915  29.523  -10.958 1.00 34.86  ? 318  ASN A OD1   1 
ATOM   2431 N ND2   . ASN A 1 318 ? 33.001  27.471  -11.019 1.00 38.50  ? 318  ASN A ND2   1 
ATOM   2432 N N     . PHE A 1 319 ? 29.446  31.672  -9.510  1.00 36.02  ? 319  PHE A N     1 
ATOM   2433 C CA    . PHE A 1 319 ? 28.180  32.431  -9.442  1.00 37.24  ? 319  PHE A CA    1 
ATOM   2434 C C     . PHE A 1 319 ? 28.013  33.258  -10.717 1.00 37.66  ? 319  PHE A C     1 
ATOM   2435 O O     . PHE A 1 319 ? 28.997  33.904  -11.151 1.00 39.19  ? 319  PHE A O     1 
ATOM   2436 C CB    . PHE A 1 319 ? 28.193  33.321  -8.209  1.00 37.22  ? 319  PHE A CB    1 
ATOM   2437 C CG    . PHE A 1 319 ? 26.902  34.043  -7.953  1.00 34.58  ? 319  PHE A CG    1 
ATOM   2438 C CD1   . PHE A 1 319 ? 26.561  35.174  -8.678  1.00 36.83  ? 319  PHE A CD1   1 
ATOM   2439 C CD2   . PHE A 1 319 ? 26.052  33.619  -6.944  1.00 35.33  ? 319  PHE A CD2   1 
ATOM   2440 C CE1   . PHE A 1 319 ? 25.369  35.843  -8.426  1.00 35.01  ? 319  PHE A CE1   1 
ATOM   2441 C CE2   . PHE A 1 319 ? 24.856  34.281  -6.702  1.00 37.05  ? 319  PHE A CE2   1 
ATOM   2442 C CZ    . PHE A 1 319 ? 24.514  35.390  -7.446  1.00 33.91  ? 319  PHE A CZ    1 
ATOM   2443 N N     . TYR A 1 320 ? 26.794  33.258  -11.268 1.00 33.74  ? 320  TYR A N     1 
ATOM   2444 C CA    . TYR A 1 320 ? 26.400  33.993  -12.494 1.00 33.29  ? 320  TYR A CA    1 
ATOM   2445 C C     . TYR A 1 320 ? 25.066  34.684  -12.225 1.00 31.43  ? 320  TYR A C     1 
ATOM   2446 O O     . TYR A 1 320 ? 24.092  34.036  -11.789 1.00 27.96  ? 320  TYR A O     1 
ATOM   2447 C CB    . TYR A 1 320 ? 26.263  33.076  -13.711 1.00 35.35  ? 320  TYR A CB    1 
ATOM   2448 C CG    . TYR A 1 320 ? 27.539  32.392  -14.108 1.00 35.62  ? 320  TYR A CG    1 
ATOM   2449 C CD1   . TYR A 1 320 ? 28.451  33.026  -14.939 1.00 35.14  ? 320  TYR A CD1   1 
ATOM   2450 C CD2   . TYR A 1 320 ? 27.864  31.148  -13.591 1.00 36.32  ? 320  TYR A CD2   1 
ATOM   2451 C CE1   . TYR A 1 320 ? 29.647  32.423  -15.272 1.00 37.44  ? 320  TYR A CE1   1 
ATOM   2452 C CE2   . TYR A 1 320 ? 29.044  30.517  -13.935 1.00 37.05  ? 320  TYR A CE2   1 
ATOM   2453 C CZ    . TYR A 1 320 ? 29.943  31.172  -14.759 1.00 40.50  ? 320  TYR A CZ    1 
ATOM   2454 O OH    . TYR A 1 320 ? 31.111  30.588  -15.106 1.00 40.48  ? 320  TYR A OH    1 
ATOM   2455 N N     . GLY A 1 321 ? 25.058  35.991  -12.443 1.00 32.85  ? 321  GLY A N     1 
ATOM   2456 C CA    . GLY A 1 321 ? 23.898  36.873  -12.238 1.00 33.60  ? 321  GLY A CA    1 
ATOM   2457 C C     . GLY A 1 321 ? 23.903  37.920  -13.320 1.00 33.91  ? 321  GLY A C     1 
ATOM   2458 O O     . GLY A 1 321 ? 24.962  38.141  -13.906 1.00 36.22  ? 321  GLY A O     1 
ATOM   2459 N N     . THR A 1 322 ? 22.739  38.483  -13.623 1.00 32.22  ? 322  THR A N     1 
ATOM   2460 C CA    . THR A 1 322 ? 22.575  39.602  -14.563 1.00 30.87  ? 322  THR A CA    1 
ATOM   2461 C C     . THR A 1 322 ? 21.885  40.708  -13.781 1.00 31.21  ? 322  THR A C     1 
ATOM   2462 O O     . THR A 1 322 ? 21.116  40.401  -12.837 1.00 31.83  ? 322  THR A O     1 
ATOM   2463 C CB    . THR A 1 322 ? 21.859  39.121  -15.829 1.00 31.53  ? 322  THR A CB    1 
ATOM   2464 O OG1   . THR A 1 322 ? 22.709  38.110  -16.379 1.00 28.31  ? 322  THR A OG1   1 
ATOM   2465 C CG2   . THR A 1 322 ? 21.551  40.219  -16.821 1.00 32.26  ? 322  THR A CG2   1 
ATOM   2466 N N     . LEU A 1 323 ? 22.242  41.934  -14.130 1.00 32.16  ? 323  LEU A N     1 
ATOM   2467 C CA    . LEU A 1 323 ? 21.637  43.192  -13.659 1.00 33.47  ? 323  LEU A CA    1 
ATOM   2468 C C     . LEU A 1 323 ? 20.998  43.846  -14.877 1.00 32.38  ? 323  LEU A C     1 
ATOM   2469 O O     . LEU A 1 323 ? 21.478  43.598  -15.986 1.00 31.74  ? 323  LEU A O     1 
ATOM   2470 C CB    . LEU A 1 323 ? 22.731  44.068  -13.044 1.00 35.06  ? 323  LEU A CB    1 
ATOM   2471 C CG    . LEU A 1 323 ? 23.446  43.436  -11.853 1.00 35.77  ? 323  LEU A CG    1 
ATOM   2472 C CD1   . LEU A 1 323 ? 24.610  44.314  -11.404 1.00 37.70  ? 323  LEU A CD1   1 
ATOM   2473 C CD2   . LEU A 1 323 ? 22.469  43.186  -10.721 1.00 37.59  ? 323  LEU A CD2   1 
ATOM   2474 N N     . TYR A 1 324 ? 19.905  44.557  -14.649 1.00 32.97  ? 324  TYR A N     1 
ATOM   2475 C CA    . TYR A 1 324 ? 19.054  45.184  -15.682 1.00 37.31  ? 324  TYR A CA    1 
ATOM   2476 C C     . TYR A 1 324 ? 18.770  46.634  -15.279 1.00 39.69  ? 324  TYR A C     1 
ATOM   2477 O O     . TYR A 1 324 ? 18.583  46.930  -14.057 1.00 39.43  ? 324  TYR A O     1 
ATOM   2478 C CB    . TYR A 1 324 ? 17.711  44.455  -15.801 1.00 35.35  ? 324  TYR A CB    1 
ATOM   2479 C CG    . TYR A 1 324 ? 17.776  42.965  -15.992 1.00 30.36  ? 324  TYR A CG    1 
ATOM   2480 C CD1   . TYR A 1 324 ? 18.064  42.426  -17.225 1.00 31.37  ? 324  TYR A CD1   1 
ATOM   2481 C CD2   . TYR A 1 324 ? 17.538  42.092  -14.941 1.00 31.53  ? 324  TYR A CD2   1 
ATOM   2482 C CE1   . TYR A 1 324 ? 18.125  41.057  -17.432 1.00 32.19  ? 324  TYR A CE1   1 
ATOM   2483 C CE2   . TYR A 1 324 ? 17.605  40.719  -15.116 1.00 31.25  ? 324  TYR A CE2   1 
ATOM   2484 C CZ    . TYR A 1 324 ? 17.878  40.198  -16.375 1.00 31.65  ? 324  TYR A CZ    1 
ATOM   2485 O OH    . TYR A 1 324 ? 17.924  38.857  -16.593 1.00 28.79  ? 324  TYR A OH    1 
ATOM   2486 N N     . GLY A 1 325 ? 18.629  47.480  -16.294 1.00 40.11  ? 325  GLY A N     1 
ATOM   2487 C CA    . GLY A 1 325 ? 18.124  48.851  -16.152 1.00 42.55  ? 325  GLY A CA    1 
ATOM   2488 C C     . GLY A 1 325 ? 19.158  49.864  -16.617 1.00 43.75  ? 325  GLY A C     1 
ATOM   2489 O O     . GLY A 1 325 ? 20.111  49.501  -17.308 1.00 43.22  ? 325  GLY A O     1 
ATOM   2490 N N     . PRO A 1 326 ? 18.997  51.153  -16.239 1.00 48.50  ? 326  PRO A N     1 
ATOM   2491 C CA    . PRO A 1 326 ? 19.913  52.195  -16.686 1.00 46.74  ? 326  PRO A CA    1 
ATOM   2492 C C     . PRO A 1 326 ? 21.281  51.925  -16.071 1.00 45.49  ? 326  PRO A C     1 
ATOM   2493 O O     . PRO A 1 326 ? 21.368  51.491  -14.926 1.00 46.09  ? 326  PRO A O     1 
ATOM   2494 C CB    . PRO A 1 326 ? 19.292  53.512  -16.200 1.00 50.55  ? 326  PRO A CB    1 
ATOM   2495 C CG    . PRO A 1 326 ? 18.265  53.127  -15.139 1.00 52.81  ? 326  PRO A CG    1 
ATOM   2496 C CD    . PRO A 1 326 ? 17.970  51.649  -15.309 1.00 52.08  ? 326  PRO A CD    1 
ATOM   2497 N N     . PRO A 1 327 ? 22.385  52.143  -16.823 1.00 47.23  ? 327  PRO A N     1 
ATOM   2498 C CA    . PRO A 1 327 ? 23.734  51.863  -16.323 1.00 48.46  ? 327  PRO A CA    1 
ATOM   2499 C C     . PRO A 1 327 ? 24.072  52.396  -14.919 1.00 48.57  ? 327  PRO A C     1 
ATOM   2500 O O     . PRO A 1 327 ? 24.970  51.878  -14.338 1.00 49.14  ? 327  PRO A O     1 
ATOM   2501 C CB    . PRO A 1 327 ? 24.631  52.547  -17.363 1.00 46.57  ? 327  PRO A CB    1 
ATOM   2502 C CG    . PRO A 1 327 ? 23.836  52.450  -18.643 1.00 48.55  ? 327  PRO A CG    1 
ATOM   2503 C CD    . PRO A 1 327 ? 22.392  52.624  -18.214 1.00 43.42  ? 327  PRO A CD    1 
ATOM   2504 N N     . GLN A 1 328 ? 23.360  53.399  -14.410 1.00 48.23  ? 328  GLN A N     1 
ATOM   2505 C CA    . GLN A 1 328 ? 23.605  53.996  -13.067 1.00 50.98  ? 328  GLN A CA    1 
ATOM   2506 C C     . GLN A 1 328 ? 23.118  53.016  -11.993 1.00 53.04  ? 328  GLN A C     1 
ATOM   2507 O O     . GLN A 1 328 ? 23.786  52.890  -10.935 1.00 49.79  ? 328  GLN A O     1 
ATOM   2508 C CB    . GLN A 1 328 ? 22.836  55.309  -12.891 1.00 55.22  ? 328  GLN A CB    1 
ATOM   2509 C CG    . GLN A 1 328 ? 22.940  56.270  -14.070 1.00 61.16  ? 328  GLN A CG    1 
ATOM   2510 C CD    . GLN A 1 328 ? 21.676  57.071  -14.279 1.00 65.40  ? 328  GLN A CD    1 
ATOM   2511 O OE1   . GLN A 1 328 ? 20.916  57.346  -13.349 1.00 72.89  ? 328  GLN A OE1   1 
ATOM   2512 N NE2   . GLN A 1 328 ? 21.444  57.456  -15.521 1.00 67.24  ? 328  GLN A NE2   1 
ATOM   2513 N N     . LEU A 1 329 ? 21.963  52.388  -12.252 1.00 45.43  ? 329  LEU A N     1 
ATOM   2514 C CA    . LEU A 1 329 ? 21.347  51.367  -11.372 1.00 45.25  ? 329  LEU A CA    1 
ATOM   2515 C C     . LEU A 1 329 ? 22.226  50.106  -11.398 1.00 39.44  ? 329  LEU A C     1 
ATOM   2516 O O     . LEU A 1 329 ? 22.588  49.640  -10.325 1.00 38.78  ? 329  LEU A O     1 
ATOM   2517 C CB    . LEU A 1 329 ? 19.914  51.109  -11.858 1.00 48.02  ? 329  LEU A CB    1 
ATOM   2518 C CG    . LEU A 1 329 ? 19.101  50.087  -11.058 1.00 49.32  ? 329  LEU A CG    1 
ATOM   2519 C CD1   . LEU A 1 329 ? 18.724  50.629  -9.690  1.00 50.96  ? 329  LEU A CD1   1 
ATOM   2520 C CD2   . LEU A 1 329 ? 17.863  49.645  -11.829 1.00 46.14  ? 329  LEU A CD2   1 
ATOM   2521 N N     . ILE A 1 330 ? 22.604  49.619  -12.582 1.00 37.56  ? 330  ILE A N     1 
ATOM   2522 C CA    . ILE A 1 330 ? 23.508  48.437  -12.778 1.00 42.84  ? 330  ILE A CA    1 
ATOM   2523 C C     . ILE A 1 330 ? 24.788  48.612  -11.939 1.00 44.21  ? 330  ILE A C     1 
ATOM   2524 O O     . ILE A 1 330 ? 25.025  47.767  -11.069 1.00 46.90  ? 330  ILE A O     1 
ATOM   2525 C CB    . ILE A 1 330 ? 23.807  48.204  -14.277 1.00 42.70  ? 330  ILE A CB    1 
ATOM   2526 C CG1   . ILE A 1 330 ? 22.576  47.659  -15.023 1.00 39.73  ? 330  ILE A CG1   1 
ATOM   2527 C CG2   . ILE A 1 330 ? 25.041  47.316  -14.454 1.00 40.46  ? 330  ILE A CG2   1 
ATOM   2528 C CD1   . ILE A 1 330 ? 22.762  47.500  -16.519 1.00 36.33  ? 330  ILE A CD1   1 
ATOM   2529 N N     . GLU A 1 331 ? 25.546  49.693  -12.150 1.00 45.21  ? 331  GLU A N     1 
ATOM   2530 C CA    . GLU A 1 331 ? 26.798  50.009  -11.402 1.00 51.44  ? 331  GLU A CA    1 
ATOM   2531 C C     . GLU A 1 331 ? 26.534  49.931  -9.896  1.00 46.27  ? 331  GLU A C     1 
ATOM   2532 O O     . GLU A 1 331 ? 27.363  49.352  -9.197  1.00 48.52  ? 331  GLU A O     1 
ATOM   2533 C CB    . GLU A 1 331 ? 27.316  51.416  -11.729 1.00 56.97  ? 331  GLU A CB    1 
ATOM   2534 C CG    . GLU A 1 331 ? 27.846  51.585  -13.150 1.00 62.15  ? 331  GLU A CG    1 
ATOM   2535 C CD    . GLU A 1 331 ? 27.926  53.028  -13.643 1.00 66.27  ? 331  GLU A CD    1 
ATOM   2536 O OE1   . GLU A 1 331 ? 28.048  53.945  -12.792 1.00 66.46  ? 331  GLU A OE1   1 
ATOM   2537 O OE2   . GLU A 1 331 ? 27.865  53.240  -14.878 1.00 68.19  ? 331  GLU A OE2   1 
ATOM   2538 N N     . MET A 1 332 ? 25.423  50.515  -9.433  1.00 44.95  ? 332  MET A N     1 
ATOM   2539 C CA    . MET A 1 332 ? 25.079  50.631  -7.994  1.00 46.34  ? 332  MET A CA    1 
ATOM   2540 C C     . MET A 1 332 ? 24.781  49.235  -7.445  1.00 43.81  ? 332  MET A C     1 
ATOM   2541 O O     . MET A 1 332 ? 25.422  48.822  -6.457  1.00 40.26  ? 332  MET A O     1 
ATOM   2542 C CB    . MET A 1 332 ? 23.864  51.536  -7.783  1.00 49.62  ? 332  MET A CB    1 
ATOM   2543 C CG    . MET A 1 332 ? 23.427  51.636  -6.331  1.00 53.09  ? 332  MET A CG    1 
ATOM   2544 S SD    . MET A 1 332 ? 21.793  52.415  -6.179  1.00 68.31  ? 332  MET A SD    1 
ATOM   2545 C CE    . MET A 1 332 ? 22.036  53.926  -7.119  1.00 67.24  ? 332  MET A CE    1 
ATOM   2546 N N     . ASN A 1 333 ? 23.872  48.514  -8.100  1.00 41.24  ? 333  ASN A N     1 
ATOM   2547 C CA    . ASN A 1 333 ? 23.518  47.134  -7.698  1.00 41.07  ? 333  ASN A CA    1 
ATOM   2548 C C     . ASN A 1 333 ? 24.772  46.263  -7.709  1.00 37.53  ? 333  ASN A C     1 
ATOM   2549 O O     . ASN A 1 333 ? 24.981  45.554  -6.717  1.00 39.18  ? 333  ASN A O     1 
ATOM   2550 C CB    . ASN A 1 333 ? 22.398  46.567  -8.560  1.00 41.43  ? 333  ASN A CB    1 
ATOM   2551 C CG    . ASN A 1 333 ? 21.045  46.999  -8.047  1.00 43.58  ? 333  ASN A CG    1 
ATOM   2552 O OD1   . ASN A 1 333 ? 20.875  47.173  -6.842  1.00 45.14  ? 333  ASN A OD1   1 
ATOM   2553 N ND2   . ASN A 1 333 ? 20.090  47.161  -8.948  1.00 42.77  ? 333  ASN A ND2   1 
ATOM   2554 N N     . TYR A 1 334 ? 25.566  46.324  -8.772  1.00 37.55  ? 334  TYR A N     1 
ATOM   2555 C CA    . TYR A 1 334 ? 26.835  45.559  -8.896  1.00 43.05  ? 334  TYR A CA    1 
ATOM   2556 C C     . TYR A 1 334 ? 27.772  45.931  -7.736  1.00 47.03  ? 334  TYR A C     1 
ATOM   2557 O O     . TYR A 1 334 ? 28.527  45.043  -7.244  1.00 43.99  ? 334  TYR A O     1 
ATOM   2558 C CB    . TYR A 1 334 ? 27.505  45.806  -10.248 1.00 39.78  ? 334  TYR A CB    1 
ATOM   2559 C CG    . TYR A 1 334 ? 28.649  44.872  -10.534 1.00 45.59  ? 334  TYR A CG    1 
ATOM   2560 C CD1   . TYR A 1 334 ? 28.525  43.506  -10.338 1.00 45.16  ? 334  TYR A CD1   1 
ATOM   2561 C CD2   . TYR A 1 334 ? 29.875  45.351  -10.978 1.00 47.73  ? 334  TYR A CD2   1 
ATOM   2562 C CE1   . TYR A 1 334 ? 29.578  42.638  -10.590 1.00 45.86  ? 334  TYR A CE1   1 
ATOM   2563 C CE2   . TYR A 1 334 ? 30.938  44.496  -11.236 1.00 45.98  ? 334  TYR A CE2   1 
ATOM   2564 C CZ    . TYR A 1 334 ? 30.792  43.132  -11.036 1.00 47.75  ? 334  TYR A CZ    1 
ATOM   2565 O OH    . TYR A 1 334 ? 31.829  42.273  -11.290 1.00 47.52  ? 334  TYR A OH    1 
ATOM   2566 N N     . GLY A 1 335 ? 27.719  47.195  -7.290  1.00 42.99  ? 335  GLY A N     1 
ATOM   2567 C CA    . GLY A 1 335 ? 28.485  47.658  -6.116  1.00 44.39  ? 335  GLY A CA    1 
ATOM   2568 C C     . GLY A 1 335 ? 28.065  46.928  -4.849  1.00 42.00  ? 335  GLY A C     1 
ATOM   2569 O O     . GLY A 1 335 ? 28.966  46.451  -4.122  1.00 38.40  ? 335  GLY A O     1 
ATOM   2570 N N     . ILE A 1 336 ? 26.752  46.840  -4.591  1.00 41.49  ? 336  ILE A N     1 
ATOM   2571 C CA    . ILE A 1 336 ? 26.189  46.064  -3.442  1.00 43.28  ? 336  ILE A CA    1 
ATOM   2572 C C     . ILE A 1 336 ? 26.625  44.597  -3.567  1.00 44.26  ? 336  ILE A C     1 
ATOM   2573 O O     . ILE A 1 336 ? 26.997  43.999  -2.547  1.00 42.74  ? 336  ILE A O     1 
ATOM   2574 C CB    . ILE A 1 336 ? 24.660  46.186  -3.344  1.00 45.36  ? 336  ILE A CB    1 
ATOM   2575 C CG1   . ILE A 1 336 ? 24.204  47.629  -3.108  1.00 44.76  ? 336  ILE A CG1   1 
ATOM   2576 C CG2   . ILE A 1 336 ? 24.131  45.254  -2.262  1.00 48.05  ? 336  ILE A CG2   1 
ATOM   2577 C CD1   . ILE A 1 336 ? 22.773  47.883  -3.532  1.00 41.28  ? 336  ILE A CD1   1 
ATOM   2578 N N     . ILE A 1 337 ? 26.612  44.040  -4.776  1.00 41.55  ? 337  ILE A N     1 
ATOM   2579 C CA    . ILE A 1 337 ? 26.920  42.595  -5.001  1.00 43.06  ? 337  ILE A CA    1 
ATOM   2580 C C     . ILE A 1 337 ? 28.386  42.339  -4.630  1.00 39.95  ? 337  ILE A C     1 
ATOM   2581 O O     . ILE A 1 337 ? 28.646  41.382  -3.885  1.00 38.19  ? 337  ILE A O     1 
ATOM   2582 C CB    . ILE A 1 337 ? 26.637  42.168  -6.457  1.00 40.52  ? 337  ILE A CB    1 
ATOM   2583 C CG1   . ILE A 1 337 ? 25.193  42.454  -6.892  1.00 43.95  ? 337  ILE A CG1   1 
ATOM   2584 C CG2   . ILE A 1 337 ? 26.993  40.701  -6.652  1.00 39.03  ? 337  ILE A CG2   1 
ATOM   2585 C CD1   . ILE A 1 337 ? 24.177  41.829  -6.006  1.00 47.88  ? 337  ILE A CD1   1 
ATOM   2586 N N     . LYS A 1 338 ? 29.287  43.150  -5.195  1.00 42.88  ? 338  LYS A N     1 
ATOM   2587 C CA    . LYS A 1 338 ? 30.760  43.097  -4.999  1.00 44.47  ? 338  LYS A CA    1 
ATOM   2588 C C     . LYS A 1 338 ? 31.099  43.262  -3.512  1.00 41.58  ? 338  LYS A C     1 
ATOM   2589 O O     . LYS A 1 338 ? 31.876  42.462  -2.994  1.00 43.80  ? 338  LYS A O     1 
ATOM   2590 C CB    . LYS A 1 338 ? 31.423  44.184  -5.840  1.00 46.13  ? 338  LYS A CB    1 
ATOM   2591 C CG    . LYS A 1 338 ? 31.671  43.803  -7.287  1.00 50.69  ? 338  LYS A CG    1 
ATOM   2592 C CD    . LYS A 1 338 ? 32.588  44.775  -8.002  1.00 54.89  ? 338  LYS A CD    1 
ATOM   2593 C CE    . LYS A 1 338 ? 31.994  46.168  -8.133  1.00 57.75  ? 338  LYS A CE    1 
ATOM   2594 N NZ    . LYS A 1 338 ? 32.758  47.000  -9.096  1.00 57.75  ? 338  LYS A NZ    1 
ATOM   2595 N N     . ASP A 1 339 ? 30.487  44.219  -2.832  1.00 42.40  ? 339  ASP A N     1 
ATOM   2596 C CA    . ASP A 1 339 ? 30.731  44.442  -1.387  1.00 46.38  ? 339  ASP A CA    1 
ATOM   2597 C C     . ASP A 1 339 ? 30.291  43.204  -0.581  1.00 51.32  ? 339  ASP A C     1 
ATOM   2598 O O     . ASP A 1 339 ? 31.006  42.834  0.379   1.00 58.33  ? 339  ASP A O     1 
ATOM   2599 C CB    . ASP A 1 339 ? 30.064  45.730  -0.912  1.00 50.87  ? 339  ASP A CB    1 
ATOM   2600 C CG    . ASP A 1 339 ? 30.238  45.930  0.580   1.00 63.66  ? 339  ASP A CG    1 
ATOM   2601 O OD1   . ASP A 1 339 ? 31.358  46.323  0.994   1.00 69.81  ? 339  ASP A OD1   1 
ATOM   2602 O OD2   . ASP A 1 339 ? 29.271  45.639  1.323   1.00 71.35  ? 339  ASP A OD2   1 
ATOM   2603 N N     . ALA A 1 340 ? 29.167  42.575  -0.932  1.00 47.10  ? 340  ALA A N     1 
ATOM   2604 C CA    . ALA A 1 340 ? 28.560  41.479  -0.139  1.00 46.09  ? 340  ALA A CA    1 
ATOM   2605 C C     . ALA A 1 340 ? 29.376  40.194  -0.317  1.00 42.00  ? 340  ALA A C     1 
ATOM   2606 O O     . ALA A 1 340 ? 29.806  39.625  0.685   1.00 35.36  ? 340  ALA A O     1 
ATOM   2607 C CB    . ALA A 1 340 ? 27.110  41.270  -0.519  1.00 46.85  ? 340  ALA A CB    1 
ATOM   2608 N N     . PHE A 1 341 ? 29.559  39.741  -1.553  1.00 41.34  ? 341  PHE A N     1 
ATOM   2609 C CA    . PHE A 1 341 ? 30.244  38.457  -1.857  1.00 40.50  ? 341  PHE A CA    1 
ATOM   2610 C C     . PHE A 1 341 ? 31.757  38.603  -1.667  1.00 42.40  ? 341  PHE A C     1 
ATOM   2611 O O     . PHE A 1 341 ? 32.375  37.564  -1.360  1.00 41.05  ? 341  PHE A O     1 
ATOM   2612 C CB    . PHE A 1 341 ? 29.888  37.974  -3.262  1.00 40.02  ? 341  PHE A CB    1 
ATOM   2613 C CG    . PHE A 1 341 ? 28.478  37.452  -3.385  1.00 39.41  ? 341  PHE A CG    1 
ATOM   2614 C CD1   . PHE A 1 341 ? 28.115  36.238  -2.815  1.00 37.14  ? 341  PHE A CD1   1 
ATOM   2615 C CD2   . PHE A 1 341 ? 27.515  38.178  -4.074  1.00 39.70  ? 341  PHE A CD2   1 
ATOM   2616 C CE1   . PHE A 1 341 ? 26.819  35.758  -2.941  1.00 39.68  ? 341  PHE A CE1   1 
ATOM   2617 C CE2   . PHE A 1 341 ? 26.220  37.700  -4.195  1.00 38.56  ? 341  PHE A CE2   1 
ATOM   2618 C CZ    . PHE A 1 341 ? 25.878  36.487  -3.635  1.00 38.50  ? 341  PHE A CZ    1 
ATOM   2619 N N     . GLY A 1 342 ? 32.301  39.830  -1.784  1.00 45.92  ? 342  GLY A N     1 
ATOM   2620 C CA    . GLY A 1 342 ? 33.707  40.204  -1.477  1.00 43.12  ? 342  GLY A CA    1 
ATOM   2621 C C     . GLY A 1 342 ? 34.100  39.919  -0.034  1.00 41.27  ? 342  GLY A C     1 
ATOM   2622 O O     . GLY A 1 342 ? 35.287  39.735  0.220   1.00 46.59  ? 342  GLY A O     1 
ATOM   2623 N N     . GLN A 1 343 ? 33.143  39.820  0.883   1.00 43.76  ? 343  GLN A N     1 
ATOM   2624 C CA    . GLN A 1 343 ? 33.381  39.365  2.282   1.00 48.61  ? 343  GLN A CA    1 
ATOM   2625 C C     . GLN A 1 343 ? 34.033  37.969  2.293   1.00 47.28  ? 343  GLN A C     1 
ATOM   2626 O O     . GLN A 1 343 ? 34.588  37.582  3.344   1.00 43.33  ? 343  GLN A O     1 
ATOM   2627 C CB    . GLN A 1 343 ? 32.066  39.289  3.065   1.00 50.59  ? 343  GLN A CB    1 
ATOM   2628 C CG    . GLN A 1 343 ? 31.368  40.632  3.230   1.00 55.71  ? 343  GLN A CG    1 
ATOM   2629 C CD    . GLN A 1 343 ? 29.922  40.461  3.632   1.00 62.36  ? 343  GLN A CD    1 
ATOM   2630 O OE1   . GLN A 1 343 ? 29.186  39.620  3.100   1.00 55.75  ? 343  GLN A OE1   1 
ATOM   2631 N NE2   . GLN A 1 343 ? 29.498  41.280  4.580   1.00 69.45  ? 343  GLN A NE2   1 
ATOM   2632 N N     . ILE A 1 344 ? 33.921  37.213  1.200   1.00 44.00  ? 344  ILE A N     1 
ATOM   2633 C CA    . ILE A 1 344 ? 34.404  35.803  1.116   1.00 46.35  ? 344  ILE A CA    1 
ATOM   2634 C C     . ILE A 1 344 ? 35.815  35.830  0.558   1.00 43.79  ? 344  ILE A C     1 
ATOM   2635 O O     . ILE A 1 344 ? 36.000  36.188  -0.606  1.00 45.18  ? 344  ILE A O     1 
ATOM   2636 C CB    . ILE A 1 344 ? 33.473  34.918  0.256   1.00 49.96  ? 344  ILE A CB    1 
ATOM   2637 C CG1   . ILE A 1 344 ? 32.062  34.865  0.849   1.00 49.57  ? 344  ILE A CG1   1 
ATOM   2638 C CG2   . ILE A 1 344 ? 34.070  33.524  0.074   1.00 48.61  ? 344  ILE A CG2   1 
ATOM   2639 C CD1   . ILE A 1 344 ? 31.089  34.023  0.054   1.00 50.05  ? 344  ILE A CD1   1 
ATOM   2640 N N     . PRO A 1 345 ? 36.838  35.478  1.376   1.00 45.96  ? 345  PRO A N     1 
ATOM   2641 C CA    . PRO A 1 345 ? 38.220  35.406  0.898   1.00 45.77  ? 345  PRO A CA    1 
ATOM   2642 C C     . PRO A 1 345 ? 38.335  34.522  -0.345  1.00 44.45  ? 345  PRO A C     1 
ATOM   2643 O O     . PRO A 1 345 ? 37.797  33.420  -0.333  1.00 43.12  ? 345  PRO A O     1 
ATOM   2644 C CB    . PRO A 1 345 ? 38.997  34.763  2.058   1.00 40.52  ? 345  PRO A CB    1 
ATOM   2645 C CG    . PRO A 1 345 ? 38.189  35.123  3.278   1.00 43.78  ? 345  PRO A CG    1 
ATOM   2646 C CD    . PRO A 1 345 ? 36.743  35.185  2.815   1.00 46.60  ? 345  PRO A CD    1 
ATOM   2647 N N     . GLY A 1 346 ? 39.029  35.026  -1.361  1.00 43.04  ? 346  GLY A N     1 
ATOM   2648 C CA    . GLY A 1 346 ? 39.325  34.297  -2.601  1.00 43.60  ? 346  GLY A CA    1 
ATOM   2649 C C     . GLY A 1 346 ? 38.326  34.613  -3.698  1.00 43.78  ? 346  GLY A C     1 
ATOM   2650 O O     . GLY A 1 346 ? 38.578  34.189  -4.839  1.00 41.26  ? 346  GLY A O     1 
ATOM   2651 N N     . SER A 1 347 ? 37.236  35.327  -3.386  1.00 45.33  ? 347  SER A N     1 
ATOM   2652 C CA    . SER A 1 347 ? 36.195  35.721  -4.377  1.00 43.88  ? 347  SER A CA    1 
ATOM   2653 C C     . SER A 1 347 ? 36.809  36.637  -5.439  1.00 41.07  ? 347  SER A C     1 
ATOM   2654 O O     . SER A 1 347 ? 37.515  37.568  -5.034  1.00 41.96  ? 347  SER A O     1 
ATOM   2655 C CB    . SER A 1 347 ? 35.023  36.385  -3.705  1.00 43.47  ? 347  SER A CB    1 
ATOM   2656 O OG    . SER A 1 347 ? 35.452  37.481  -2.921  1.00 44.16  ? 347  SER A OG    1 
ATOM   2657 N N     . ARG A 1 348 ? 36.541  36.376  -6.727  1.00 44.48  ? 348  ARG A N     1 
ATOM   2658 C CA    . ARG A 1 348 ? 36.974  37.205  -7.893  1.00 44.63  ? 348  ARG A CA    1 
ATOM   2659 C C     . ARG A 1 348 ? 35.761  37.528  -8.795  1.00 45.84  ? 348  ARG A C     1 
ATOM   2660 O O     . ARG A 1 348 ? 34.947  36.622  -9.061  1.00 37.23  ? 348  ARG A O     1 
ATOM   2661 C CB    . ARG A 1 348 ? 38.091  36.519  -8.685  1.00 50.08  ? 348  ARG A CB    1 
ATOM   2662 C CG    . ARG A 1 348 ? 39.314  36.154  -7.850  1.00 56.38  ? 348  ARG A CG    1 
ATOM   2663 C CD    . ARG A 1 348 ? 40.571  35.854  -8.652  1.00 64.01  ? 348  ARG A CD    1 
ATOM   2664 N NE    . ARG A 1 348 ? 40.418  34.812  -9.672  1.00 66.05  ? 348  ARG A NE    1 
ATOM   2665 C CZ    . ARG A 1 348 ? 41.321  33.865  -9.957  1.00 71.93  ? 348  ARG A CZ    1 
ATOM   2666 N NH1   . ARG A 1 348 ? 42.462  33.795  -9.286  1.00 67.85  ? 348  ARG A NH1   1 
ATOM   2667 N NH2   . ARG A 1 348 ? 41.066  32.973  -10.904 1.00 70.25  ? 348  ARG A NH2   1 
ATOM   2668 N N     . PHE A 1 349 ? 35.641  38.792  -9.223  1.00 41.57  ? 349  PHE A N     1 
ATOM   2669 C CA    . PHE A 1 349 ? 34.505  39.341  -9.996  1.00 42.99  ? 349  PHE A CA    1 
ATOM   2670 C C     . PHE A 1 349 ? 34.968  39.646  -11.411 1.00 44.21  ? 349  PHE A C     1 
ATOM   2671 O O     . PHE A 1 349 ? 36.039  40.213  -11.554 1.00 40.45  ? 349  PHE A O     1 
ATOM   2672 C CB    . PHE A 1 349 ? 33.959  40.582  -9.304  1.00 43.12  ? 349  PHE A CB    1 
ATOM   2673 C CG    . PHE A 1 349 ? 33.424  40.259  -7.943  1.00 41.41  ? 349  PHE A CG    1 
ATOM   2674 C CD1   . PHE A 1 349 ? 34.291  40.018  -6.886  1.00 44.83  ? 349  PHE A CD1   1 
ATOM   2675 C CD2   . PHE A 1 349 ? 32.062  40.125  -7.735  1.00 45.17  ? 349  PHE A CD2   1 
ATOM   2676 C CE1   . PHE A 1 349 ? 33.802  39.678  -5.638  1.00 45.56  ? 349  PHE A CE1   1 
ATOM   2677 C CE2   . PHE A 1 349 ? 31.576  39.783  -6.484  1.00 44.44  ? 349  PHE A CE2   1 
ATOM   2678 C CZ    . PHE A 1 349 ? 32.445  39.552  -5.443  1.00 44.64  ? 349  PHE A CZ    1 
ATOM   2679 N N     . GLN A 1 350 ? 34.175  39.231  -12.398 1.00 45.70  ? 350  GLN A N     1 
ATOM   2680 C CA    . GLN A 1 350 ? 34.401  39.486  -13.836 1.00 48.03  ? 350  GLN A CA    1 
ATOM   2681 C C     . GLN A 1 350 ? 33.034  39.742  -14.480 1.00 48.94  ? 350  GLN A C     1 
ATOM   2682 O O     . GLN A 1 350 ? 32.090  38.973  -14.237 1.00 41.55  ? 350  GLN A O     1 
ATOM   2683 C CB    . GLN A 1 350 ? 35.134  38.317  -14.504 1.00 52.70  ? 350  GLN A CB    1 
ATOM   2684 C CG    . GLN A 1 350 ? 36.432  37.897  -13.813 1.00 59.80  ? 350  GLN A CG    1 
ATOM   2685 C CD    . GLN A 1 350 ? 36.292  36.736  -12.846 1.00 71.33  ? 350  GLN A CD    1 
ATOM   2686 O OE1   . GLN A 1 350 ? 35.191  36.334  -12.454 1.00 63.81  ? 350  GLN A OE1   1 
ATOM   2687 N NE2   . GLN A 1 350 ? 37.425  36.171  -12.443 1.00 66.68  ? 350  GLN A NE2   1 
ATOM   2688 N N     . THR A 1 351 ? 32.974  40.795  -15.281 1.00 44.91  ? 351  THR A N     1 
ATOM   2689 C CA    . THR A 1 351 ? 31.815  41.253  -16.084 1.00 47.19  ? 351  THR A CA    1 
ATOM   2690 C C     . THR A 1 351 ? 31.861  40.528  -17.428 1.00 42.19  ? 351  THR A C     1 
ATOM   2691 O O     . THR A 1 351 ? 32.941  40.085  -17.776 1.00 36.86  ? 351  THR A O     1 
ATOM   2692 C CB    . THR A 1 351 ? 31.919  42.777  -16.159 1.00 46.01  ? 351  THR A CB    1 
ATOM   2693 O OG1   . THR A 1 351 ? 31.346  43.222  -14.927 1.00 47.69  ? 351  THR A OG1   1 
ATOM   2694 C CG2   . THR A 1 351 ? 31.279  43.405  -17.366 1.00 46.69  ? 351  THR A CG2   1 
ATOM   2695 N N     . HIS A 1 352 ? 30.737  40.436  -18.144 1.00 43.87  ? 352  HIS A N     1 
ATOM   2696 C CA    . HIS A 1 352 ? 30.648  39.862  -19.516 1.00 43.24  ? 352  HIS A CA    1 
ATOM   2697 C C     . HIS A 1 352 ? 31.543  40.625  -20.509 1.00 44.56  ? 352  HIS A C     1 
ATOM   2698 O O     . HIS A 1 352 ? 31.893  40.034  -21.555 1.00 44.39  ? 352  HIS A O     1 
ATOM   2699 C CB    . HIS A 1 352 ? 29.190  39.803  -19.998 1.00 38.15  ? 352  HIS A CB    1 
ATOM   2700 C CG    . HIS A 1 352 ? 28.642  41.084  -20.537 1.00 39.62  ? 352  HIS A CG    1 
ATOM   2701 N ND1   . HIS A 1 352 ? 27.961  41.999  -19.737 1.00 37.69  ? 352  HIS A ND1   1 
ATOM   2702 C CD2   . HIS A 1 352 ? 28.600  41.574  -21.796 1.00 33.37  ? 352  HIS A CD2   1 
ATOM   2703 C CE1   . HIS A 1 352 ? 27.548  43.000  -20.481 1.00 33.99  ? 352  HIS A CE1   1 
ATOM   2704 N NE2   . HIS A 1 352 ? 27.912  42.757  -21.744 1.00 35.63  ? 352  HIS A NE2   1 
ATOM   2705 N N     . GLU A 1 353 ? 31.893  41.883  -20.231 1.00 48.77  ? 353  GLU A N     1 
ATOM   2706 C CA    . GLU A 1 353 ? 32.765  42.676  -21.142 1.00 51.37  ? 353  GLU A CA    1 
ATOM   2707 C C     . GLU A 1 353 ? 34.219  42.652  -20.652 1.00 50.10  ? 353  GLU A C     1 
ATOM   2708 O O     . GLU A 1 353 ? 35.068  43.171  -21.380 1.00 58.42  ? 353  GLU A O     1 
ATOM   2709 C CB    . GLU A 1 353 ? 32.242  44.094  -21.367 1.00 57.21  ? 353  GLU A CB    1 
ATOM   2710 C CG    . GLU A 1 353 ? 31.333  44.628  -20.281 1.00 58.10  ? 353  GLU A CG    1 
ATOM   2711 C CD    . GLU A 1 353 ? 30.409  45.735  -20.747 1.00 61.04  ? 353  GLU A CD    1 
ATOM   2712 O OE1   . GLU A 1 353 ? 30.423  46.046  -21.954 1.00 67.57  ? 353  GLU A OE1   1 
ATOM   2713 O OE2   . GLU A 1 353 ? 29.668  46.273  -19.907 1.00 61.14  ? 353  GLU A OE2   1 
ATOM   2714 N N     . GLU A 1 354 ? 34.504  42.024  -19.510 1.00 46.48  ? 354  GLU A N     1 
ATOM   2715 C CA    . GLU A 1 354 ? 35.876  41.919  -18.938 1.00 51.06  ? 354  GLU A CA    1 
ATOM   2716 C C     . GLU A 1 354 ? 36.496  40.535  -19.184 1.00 53.62  ? 354  GLU A C     1 
ATOM   2717 O O     . GLU A 1 354 ? 37.722  40.432  -19.013 1.00 59.34  ? 354  GLU A O     1 
ATOM   2718 C CB    . GLU A 1 354 ? 35.849  42.158  -17.434 1.00 47.22  ? 354  GLU A CB    1 
ATOM   2719 C CG    . GLU A 1 354 ? 35.470  43.566  -17.051 1.00 48.78  ? 354  GLU A CG    1 
ATOM   2720 C CD    . GLU A 1 354 ? 35.318  43.680  -15.551 1.00 52.92  ? 354  GLU A CD    1 
ATOM   2721 O OE1   . GLU A 1 354 ? 35.067  42.628  -14.899 1.00 46.97  ? 354  GLU A OE1   1 
ATOM   2722 O OE2   . GLU A 1 354 ? 35.456  44.803  -15.038 1.00 60.59  ? 354  GLU A OE2   1 
ATOM   2723 N N     . ARG A 1 355 ? 35.713  39.498  -19.511 1.00 51.68  ? 355  ARG A N     1 
ATOM   2724 C CA    . ARG A 1 355 ? 36.243  38.106  -19.613 1.00 52.78  ? 355  ARG A CA    1 
ATOM   2725 C C     . ARG A 1 355 ? 35.798  37.483  -20.941 1.00 55.28  ? 355  ARG A C     1 
ATOM   2726 O O     . ARG A 1 355 ? 34.572  37.451  -21.204 1.00 60.80  ? 355  ARG A O     1 
ATOM   2727 C CB    . ARG A 1 355 ? 35.842  37.278  -18.383 1.00 51.30  ? 355  ARG A CB    1 
ATOM   2728 C CG    . ARG A 1 355 ? 36.804  36.140  -18.092 1.00 51.24  ? 355  ARG A CG    1 
ATOM   2729 C CD    . ARG A 1 355 ? 36.317  35.086  -17.116 1.00 50.51  ? 355  ARG A CD    1 
ATOM   2730 N NE    . ARG A 1 355 ? 37.230  33.940  -17.149 1.00 50.29  ? 355  ARG A NE    1 
ATOM   2731 C CZ    . ARG A 1 355 ? 37.454  33.101  -16.146 1.00 50.60  ? 355  ARG A CZ    1 
ATOM   2732 N NH1   . ARG A 1 355 ? 36.818  33.242  -14.995 1.00 50.87  ? 355  ARG A NH1   1 
ATOM   2733 N NH2   . ARG A 1 355 ? 38.318  32.111  -16.301 1.00 56.51  ? 355  ARG A NH2   1 
ATOM   2734 N N     . HIS A 1 356 ? 36.774  36.991  -21.722 1.00 52.08  ? 356  HIS A N     1 
ATOM   2735 C CA    . HIS A 1 356 ? 36.636  36.463  -23.108 1.00 55.54  ? 356  HIS A CA    1 
ATOM   2736 C C     . HIS A 1 356 ? 37.731  35.424  -23.356 1.00 61.68  ? 356  HIS A C     1 
ATOM   2737 O O     . HIS A 1 356 ? 38.587  35.655  -24.224 1.00 80.47  ? 356  HIS A O     1 
ATOM   2738 C CB    . HIS A 1 356 ? 36.743  37.588  -24.143 1.00 55.30  ? 356  HIS A CB    1 
ATOM   2739 C CG    . HIS A 1 356 ? 35.610  38.553  -24.115 1.00 63.37  ? 356  HIS A CG    1 
ATOM   2740 N ND1   . HIS A 1 356 ? 35.762  39.844  -23.648 1.00 68.86  ? 356  HIS A ND1   1 
ATOM   2741 C CD2   . HIS A 1 356 ? 34.318  38.427  -24.493 1.00 62.47  ? 356  HIS A CD2   1 
ATOM   2742 C CE1   . HIS A 1 356 ? 34.608  40.476  -23.741 1.00 66.81  ? 356  HIS A CE1   1 
ATOM   2743 N NE2   . HIS A 1 356 ? 33.703  39.626  -24.250 1.00 65.42  ? 356  HIS A NE2   1 
ATOM   2744 N N     . ASP A 1 357 ? 37.728  34.351  -22.578 1.00 57.98  ? 357  ASP A N     1 
ATOM   2745 C CA    . ASP A 1 357 ? 38.703  33.245  -22.667 1.00 56.46  ? 357  ASP A CA    1 
ATOM   2746 C C     . ASP A 1 357 ? 37.913  31.948  -22.492 1.00 56.91  ? 357  ASP A C     1 
ATOM   2747 O O     . ASP A 1 357 ? 36.694  32.044  -22.236 1.00 59.22  ? 357  ASP A O     1 
ATOM   2748 C CB    . ASP A 1 357 ? 39.800  33.455  -21.626 1.00 58.89  ? 357  ASP A CB    1 
ATOM   2749 C CG    . ASP A 1 357 ? 39.289  33.594  -20.199 1.00 63.44  ? 357  ASP A CG    1 
ATOM   2750 O OD1   . ASP A 1 357 ? 38.062  33.620  -19.998 1.00 71.23  ? 357  ASP A OD1   1 
ATOM   2751 O OD2   . ASP A 1 357 ? 40.124  33.674  -19.294 1.00 70.77  ? 357  ASP A OD2   1 
ATOM   2752 N N     . ARG A 1 358 ? 38.566  30.795  -22.627 1.00 53.90  ? 358  ARG A N     1 
ATOM   2753 C CA    . ARG A 1 358 ? 37.925  29.462  -22.445 1.00 53.02  ? 358  ARG A CA    1 
ATOM   2754 C C     . ARG A 1 358 ? 36.991  29.516  -21.223 1.00 52.25  ? 358  ARG A C     1 
ATOM   2755 O O     . ARG A 1 358 ? 35.799  29.142  -21.356 1.00 51.19  ? 358  ARG A O     1 
ATOM   2756 C CB    . ARG A 1 358 ? 39.009  28.387  -22.327 1.00 54.81  ? 358  ARG A CB    1 
ATOM   2757 C CG    . ARG A 1 358 ? 38.518  26.964  -22.548 1.00 61.02  ? 358  ARG A CG    1 
ATOM   2758 C CD    . ARG A 1 358 ? 39.493  26.146  -23.376 1.00 64.85  ? 358  ARG A CD    1 
ATOM   2759 N NE    . ARG A 1 358 ? 40.571  25.544  -22.602 1.00 71.07  ? 358  ARG A NE    1 
ATOM   2760 C CZ    . ARG A 1 358 ? 40.780  24.231  -22.444 1.00 69.92  ? 358  ARG A CZ    1 
ATOM   2761 N NH1   . ARG A 1 358 ? 39.976  23.340  -23.001 1.00 65.04  ? 358  ARG A NH1   1 
ATOM   2762 N NH2   . ARG A 1 358 ? 41.806  23.812  -21.719 1.00 70.44  ? 358  ARG A NH2   1 
ATOM   2763 N N     . GLY A 1 359 ? 37.503  30.016  -20.094 1.00 45.23  ? 359  GLY A N     1 
ATOM   2764 C CA    . GLY A 1 359 ? 36.833  30.032  -18.785 1.00 49.53  ? 359  GLY A CA    1 
ATOM   2765 C C     . GLY A 1 359 ? 35.562  30.872  -18.783 1.00 52.14  ? 359  GLY A C     1 
ATOM   2766 O O     . GLY A 1 359 ? 34.759  30.667  -17.860 1.00 52.05  ? 359  GLY A O     1 
ATOM   2767 N N     . ALA A 1 360 ? 35.400  31.786  -19.753 1.00 45.67  ? 360  ALA A N     1 
ATOM   2768 C CA    . ALA A 1 360 ? 34.276  32.749  -19.855 1.00 46.26  ? 360  ALA A CA    1 
ATOM   2769 C C     . ALA A 1 360 ? 33.186  32.253  -20.808 1.00 46.38  ? 360  ALA A C     1 
ATOM   2770 O O     . ALA A 1 360 ? 32.200  33.005  -20.990 1.00 46.66  ? 360  ALA A O     1 
ATOM   2771 C CB    . ALA A 1 360 ? 34.777  34.094  -20.318 1.00 50.22  ? 360  ALA A CB    1 
ATOM   2772 N N     . HIS A 1 361 ? 33.321  31.055  -21.392 1.00 46.52  ? 361  HIS A N     1 
ATOM   2773 C CA    . HIS A 1 361 ? 32.293  30.487  -22.306 1.00 47.39  ? 361  HIS A CA    1 
ATOM   2774 C C     . HIS A 1 361 ? 30.928  30.477  -21.596 1.00 43.19  ? 361  HIS A C     1 
ATOM   2775 O O     . HIS A 1 361 ? 29.960  30.948  -22.198 1.00 40.22  ? 361  HIS A O     1 
ATOM   2776 C CB    . HIS A 1 361 ? 32.685  29.097  -22.826 1.00 48.16  ? 361  HIS A CB    1 
ATOM   2777 C CG    . HIS A 1 361 ? 31.872  28.665  -23.999 1.00 57.12  ? 361  HIS A CG    1 
ATOM   2778 N ND1   . HIS A 1 361 ? 32.114  29.125  -25.284 1.00 61.55  ? 361  HIS A ND1   1 
ATOM   2779 C CD2   . HIS A 1 361 ? 30.806  27.836  -24.090 1.00 61.07  ? 361  HIS A CD2   1 
ATOM   2780 C CE1   . HIS A 1 361 ? 31.235  28.589  -26.112 1.00 64.41  ? 361  HIS A CE1   1 
ATOM   2781 N NE2   . HIS A 1 361 ? 30.429  27.785  -25.407 1.00 61.14  ? 361  HIS A NE2   1 
ATOM   2782 N N     . VAL A 1 362 ? 30.854  29.954  -20.370 1.00 40.15  ? 362  VAL A N     1 
ATOM   2783 C CA    . VAL A 1 362 ? 29.582  29.852  -19.596 1.00 39.39  ? 362  VAL A CA    1 
ATOM   2784 C C     . VAL A 1 362 ? 29.083  31.270  -19.291 1.00 39.56  ? 362  VAL A C     1 
ATOM   2785 O O     . VAL A 1 362 ? 27.861  31.488  -19.451 1.00 39.99  ? 362  VAL A O     1 
ATOM   2786 C CB    . VAL A 1 362 ? 29.732  29.008  -18.312 1.00 38.29  ? 362  VAL A CB    1 
ATOM   2787 C CG1   . VAL A 1 362 ? 28.568  29.232  -17.368 1.00 39.66  ? 362  VAL A CG1   1 
ATOM   2788 C CG2   . VAL A 1 362 ? 29.895  27.525  -18.617 1.00 37.03  ? 362  VAL A CG2   1 
ATOM   2789 N N     . LEU A 1 363 ? 29.970  32.183  -18.851 1.00 36.02  ? 363  LEU A N     1 
ATOM   2790 C CA    . LEU A 1 363 ? 29.625  33.598  -18.547 1.00 36.39  ? 363  LEU A CA    1 
ATOM   2791 C C     . LEU A 1 363 ? 28.923  34.222  -19.766 1.00 39.58  ? 363  LEU A C     1 
ATOM   2792 O O     . LEU A 1 363 ? 27.861  34.849  -19.578 1.00 36.74  ? 363  LEU A O     1 
ATOM   2793 C CB    . LEU A 1 363 ? 30.884  34.392  -18.175 1.00 39.31  ? 363  LEU A CB    1 
ATOM   2794 C CG    . LEU A 1 363 ? 30.725  35.916  -18.124 1.00 37.72  ? 363  LEU A CG    1 
ATOM   2795 C CD1   . LEU A 1 363 ? 29.687  36.316  -17.102 1.00 37.22  ? 363  LEU A CD1   1 
ATOM   2796 C CD2   . LEU A 1 363 ? 32.051  36.576  -17.793 1.00 39.06  ? 363  LEU A CD2   1 
ATOM   2797 N N     . GLN A 1 364 ? 29.487  34.041  -20.964 1.00 36.20  ? 364  GLN A N     1 
ATOM   2798 C CA    . GLN A 1 364 ? 28.962  34.610  -22.225 1.00 35.89  ? 364  GLN A CA    1 
ATOM   2799 C C     . GLN A 1 364 ? 27.640  33.906  -22.570 1.00 37.50  ? 364  GLN A C     1 
ATOM   2800 O O     . GLN A 1 364 ? 26.740  34.581  -23.098 1.00 36.03  ? 364  GLN A O     1 
ATOM   2801 C CB    . GLN A 1 364 ? 30.001  34.500  -23.346 1.00 35.35  ? 364  GLN A CB    1 
ATOM   2802 C CG    . GLN A 1 364 ? 31.285  35.290  -23.086 1.00 38.98  ? 364  GLN A CG    1 
ATOM   2803 C CD    . GLN A 1 364 ? 31.061  36.768  -22.873 1.00 37.18  ? 364  GLN A CD    1 
ATOM   2804 O OE1   . GLN A 1 364 ? 30.069  37.331  -23.317 1.00 43.26  ? 364  GLN A OE1   1 
ATOM   2805 N NE2   . GLN A 1 364 ? 31.973  37.415  -22.167 1.00 39.16  ? 364  GLN A NE2   1 
ATOM   2806 N N     . ASP A 1 365 ? 27.532  32.601  -22.314 1.00 33.41  ? 365  ASP A N     1 
ATOM   2807 C CA    . ASP A 1 365 ? 26.291  31.829  -22.598 1.00 36.16  ? 365  ASP A CA    1 
ATOM   2808 C C     . ASP A 1 365 ? 25.205  32.263  -21.613 1.00 32.41  ? 365  ASP A C     1 
ATOM   2809 O O     . ASP A 1 365 ? 24.075  32.420  -22.061 1.00 31.62  ? 365  ASP A O     1 
ATOM   2810 C CB    . ASP A 1 365 ? 26.459  30.306  -22.530 1.00 35.50  ? 365  ASP A CB    1 
ATOM   2811 C CG    . ASP A 1 365 ? 25.303  29.580  -23.203 1.00 37.97  ? 365  ASP A CG    1 
ATOM   2812 O OD1   . ASP A 1 365 ? 24.914  30.011  -24.291 1.00 42.02  ? 365  ASP A OD1   1 
ATOM   2813 O OD2   . ASP A 1 365 ? 24.789  28.603  -22.630 1.00 39.31  ? 365  ASP A OD2   1 
ATOM   2814 N N     . ARG A 1 366 ? 25.555  32.441  -20.336 1.00 32.07  ? 366  ARG A N     1 
ATOM   2815 C CA    . ARG A 1 366 ? 24.628  32.934  -19.292 1.00 33.33  ? 366  ARG A CA    1 
ATOM   2816 C C     . ARG A 1 366 ? 24.127  34.321  -19.696 1.00 34.57  ? 366  ARG A C     1 
ATOM   2817 O O     . ARG A 1 366 ? 22.953  34.623  -19.454 1.00 33.98  ? 366  ARG A O     1 
ATOM   2818 C CB    . ARG A 1 366 ? 25.283  33.011  -17.908 1.00 33.41  ? 366  ARG A CB    1 
ATOM   2819 C CG    . ARG A 1 366 ? 25.713  31.681  -17.307 1.00 33.49  ? 366  ARG A CG    1 
ATOM   2820 C CD    . ARG A 1 366 ? 24.945  30.458  -17.762 1.00 37.45  ? 366  ARG A CD    1 
ATOM   2821 N NE    . ARG A 1 366 ? 23.611  30.383  -17.190 1.00 36.79  ? 366  ARG A NE    1 
ATOM   2822 C CZ    . ARG A 1 366 ? 22.763  29.366  -17.358 1.00 36.04  ? 366  ARG A CZ    1 
ATOM   2823 N NH1   . ARG A 1 366 ? 23.082  28.319  -18.107 1.00 33.69  ? 366  ARG A NH1   1 
ATOM   2824 N NH2   . ARG A 1 366 ? 21.577  29.416  -16.773 1.00 34.60  ? 366  ARG A NH2   1 
ATOM   2825 N N     . HIS A 1 367 ? 24.991  35.138  -20.284 1.00 31.57  ? 367  HIS A N     1 
ATOM   2826 C CA    . HIS A 1 367 ? 24.636  36.513  -20.703 1.00 36.16  ? 367  HIS A CA    1 
ATOM   2827 C C     . HIS A 1 367 ? 23.524  36.451  -21.754 1.00 35.43  ? 367  HIS A C     1 
ATOM   2828 O O     . HIS A 1 367 ? 22.646  37.302  -21.713 1.00 31.09  ? 367  HIS A O     1 
ATOM   2829 C CB    . HIS A 1 367 ? 25.858  37.276  -21.213 1.00 37.21  ? 367  HIS A CB    1 
ATOM   2830 C CG    . HIS A 1 367 ? 25.542  38.693  -21.523 1.00 34.18  ? 367  HIS A CG    1 
ATOM   2831 N ND1   . HIS A 1 367 ? 24.959  39.531  -20.590 1.00 31.89  ? 367  HIS A ND1   1 
ATOM   2832 C CD2   . HIS A 1 367 ? 25.739  39.415  -22.651 1.00 35.81  ? 367  HIS A CD2   1 
ATOM   2833 C CE1   . HIS A 1 367 ? 24.796  40.721  -21.129 1.00 37.07  ? 367  HIS A CE1   1 
ATOM   2834 N NE2   . HIS A 1 367 ? 25.265  40.673  -22.413 1.00 34.69  ? 367  HIS A NE2   1 
ATOM   2835 N N     . LYS A 1 368 ? 23.588  35.489  -22.669 1.00 34.93  ? 368  LYS A N     1 
ATOM   2836 C CA    . LYS A 1 368 ? 22.516  35.290  -23.686 1.00 40.62  ? 368  LYS A CA    1 
ATOM   2837 C C     . LYS A 1 368 ? 21.240  34.853  -22.966 1.00 37.24  ? 368  LYS A C     1 
ATOM   2838 O O     . LYS A 1 368 ? 20.244  35.586  -23.055 1.00 34.74  ? 368  LYS A O     1 
ATOM   2839 C CB    . LYS A 1 368 ? 22.946  34.317  -24.784 1.00 37.85  ? 368  LYS A CB    1 
ATOM   2840 C CG    . LYS A 1 368 ? 23.930  34.932  -25.771 1.00 43.86  ? 368  LYS A CG    1 
ATOM   2841 C CD    . LYS A 1 368 ? 24.728  33.908  -26.550 1.00 47.39  ? 368  LYS A CD    1 
ATOM   2842 C CE    . LYS A 1 368 ? 23.941  33.324  -27.700 1.00 52.34  ? 368  LYS A CE    1 
ATOM   2843 N NZ    . LYS A 1 368 ? 24.311  31.913  -27.952 1.00 58.84  ? 368  LYS A NZ    1 
ATOM   2844 N N     . ILE A 1 369 ? 21.318  33.770  -22.187 1.00 36.17  ? 369  ILE A N     1 
ATOM   2845 C CA    . ILE A 1 369 ? 20.133  33.109  -21.576 1.00 31.23  ? 369  ILE A CA    1 
ATOM   2846 C C     . ILE A 1 369 ? 19.399  34.090  -20.660 1.00 31.57  ? 369  ILE A C     1 
ATOM   2847 O O     . ILE A 1 369 ? 18.143  34.079  -20.656 1.00 32.19  ? 369  ILE A O     1 
ATOM   2848 C CB    . ILE A 1 369 ? 20.576  31.850  -20.831 1.00 33.08  ? 369  ILE A CB    1 
ATOM   2849 C CG1   . ILE A 1 369 ? 20.949  30.746  -21.826 1.00 33.39  ? 369  ILE A CG1   1 
ATOM   2850 C CG2   . ILE A 1 369 ? 19.507  31.411  -19.844 1.00 35.59  ? 369  ILE A CG2   1 
ATOM   2851 C CD1   . ILE A 1 369 ? 21.967  29.760  -21.285 1.00 35.64  ? 369  ILE A CD1   1 
ATOM   2852 N N     . ASN A 1 370 ? 20.151  34.866  -19.881 1.00 27.49  ? 370  ASN A N     1 
ATOM   2853 C CA    . ASN A 1 370 ? 19.640  35.806  -18.855 1.00 29.34  ? 370  ASN A CA    1 
ATOM   2854 C C     . ASN A 1 370 ? 19.012  37.033  -19.540 1.00 27.61  ? 370  ASN A C     1 
ATOM   2855 O O     . ASN A 1 370 ? 18.370  37.829  -18.857 1.00 23.83  ? 370  ASN A O     1 
ATOM   2856 C CB    . ASN A 1 370 ? 20.762  36.167  -17.879 1.00 31.52  ? 370  ASN A CB    1 
ATOM   2857 C CG    . ASN A 1 370 ? 21.182  35.005  -16.996 1.00 31.76  ? 370  ASN A CG    1 
ATOM   2858 O OD1   . ASN A 1 370 ? 20.618  33.908  -17.059 1.00 33.37  ? 370  ASN A OD1   1 
ATOM   2859 N ND2   . ASN A 1 370 ? 22.186  35.232  -16.166 1.00 30.94  ? 370  ASN A ND2   1 
ATOM   2860 N N     . ASN A 1 371 ? 19.198  37.169  -20.851 1.00 29.51  ? 371  ASN A N     1 
ATOM   2861 C CA    . ASN A 1 371 ? 18.647  38.282  -21.657 1.00 33.37  ? 371  ASN A CA    1 
ATOM   2862 C C     . ASN A 1 371 ? 17.721  37.676  -22.701 1.00 34.32  ? 371  ASN A C     1 
ATOM   2863 O O     . ASN A 1 371 ? 17.426  38.381  -23.645 1.00 35.55  ? 371  ASN A O     1 
ATOM   2864 C CB    . ASN A 1 371 ? 19.747  39.124  -22.310 1.00 36.10  ? 371  ASN A CB    1 
ATOM   2865 C CG    . ASN A 1 371 ? 20.427  40.042  -21.318 1.00 36.03  ? 371  ASN A CG    1 
ATOM   2866 O OD1   . ASN A 1 371 ? 19.807  40.941  -20.775 1.00 34.55  ? 371  ASN A OD1   1 
ATOM   2867 N ND2   . ASN A 1 371 ? 21.709  39.834  -21.086 1.00 37.47  ? 371  ASN A ND2   1 
ATOM   2868 N N     . GLY A 1 372 ? 17.261  36.435  -22.474 1.00 33.70  ? 372  GLY A N     1 
ATOM   2869 C CA    . GLY A 1 372 ? 16.191  35.789  -23.255 1.00 33.76  ? 372  GLY A CA    1 
ATOM   2870 C C     . GLY A 1 372 ? 16.625  35.531  -24.681 1.00 33.22  ? 372  GLY A C     1 
ATOM   2871 O O     . GLY A 1 372 ? 15.769  35.541  -25.571 1.00 31.92  ? 372  GLY A O     1 
ATOM   2872 N N     . ILE A 1 373 ? 17.922  35.308  -24.892 1.00 34.37  ? 373  ILE A N     1 
ATOM   2873 C CA    . ILE A 1 373 ? 18.482  34.904  -26.201 1.00 33.57  ? 373  ILE A CA    1 
ATOM   2874 C C     . ILE A 1 373 ? 18.785  33.423  -26.070 1.00 34.75  ? 373  ILE A C     1 
ATOM   2875 O O     . ILE A 1 373 ? 19.635  33.024  -25.276 1.00 33.36  ? 373  ILE A O     1 
ATOM   2876 C CB    . ILE A 1 373 ? 19.704  35.742  -26.604 1.00 38.83  ? 373  ILE A CB    1 
ATOM   2877 C CG1   . ILE A 1 373 ? 19.309  37.206  -26.841 1.00 39.01  ? 373  ILE A CG1   1 
ATOM   2878 C CG2   . ILE A 1 373 ? 20.372  35.132  -27.831 1.00 35.60  ? 373  ILE A CG2   1 
ATOM   2879 C CD1   . ILE A 1 373 ? 19.937  38.189  -25.893 1.00 42.48  ? 373  ILE A CD1   1 
ATOM   2880 N N     . PRO A 1 374 ? 18.002  32.581  -26.784 1.00 32.63  ? 374  PRO A N     1 
ATOM   2881 C CA    . PRO A 1 374 ? 18.117  31.130  -26.685 1.00 32.97  ? 374  PRO A CA    1 
ATOM   2882 C C     . PRO A 1 374 ? 19.435  30.635  -27.306 1.00 32.44  ? 374  PRO A C     1 
ATOM   2883 O O     . PRO A 1 374 ? 19.958  31.272  -28.229 1.00 31.77  ? 374  PRO A O     1 
ATOM   2884 C CB    . PRO A 1 374 ? 16.876  30.649  -27.453 1.00 32.79  ? 374  PRO A CB    1 
ATOM   2885 C CG    . PRO A 1 374 ? 16.629  31.722  -28.469 1.00 32.25  ? 374  PRO A CG    1 
ATOM   2886 C CD    . PRO A 1 374 ? 16.979  33.005  -27.749 1.00 31.66  ? 374  PRO A CD    1 
ATOM   2887 N N     . SER A 1 375 ? 19.949  29.538  -26.774 1.00 29.95  ? 375  SER A N     1 
ATOM   2888 C CA    . SER A 1 375 ? 21.320  29.008  -27.009 1.00 36.69  ? 375  SER A CA    1 
ATOM   2889 C C     . SER A 1 375 ? 21.265  27.492  -26.981 1.00 36.34  ? 375  SER A C     1 
ATOM   2890 O O     . SER A 1 375 ? 20.387  26.969  -26.260 1.00 36.67  ? 375  SER A O     1 
ATOM   2891 C CB    . SER A 1 375 ? 22.278  29.487  -25.959 1.00 37.63  ? 375  SER A CB    1 
ATOM   2892 O OG    . SER A 1 375 ? 23.582  28.975  -26.195 1.00 37.99  ? 375  SER A OG    1 
ATOM   2893 N N     . LEU A 1 376 ? 22.152  26.828  -27.725 1.00 33.84  ? 376  LEU A N     1 
ATOM   2894 C CA    . LEU A 1 376 ? 22.371  25.360  -27.598 1.00 33.84  ? 376  LEU A CA    1 
ATOM   2895 C C     . LEU A 1 376 ? 23.780  25.080  -27.045 1.00 35.90  ? 376  LEU A C     1 
ATOM   2896 O O     . LEU A 1 376 ? 24.208  23.922  -27.080 1.00 40.81  ? 376  LEU A O     1 
ATOM   2897 C CB    . LEU A 1 376 ? 22.138  24.695  -28.957 1.00 33.09  ? 376  LEU A CB    1 
ATOM   2898 C CG    . LEU A 1 376 ? 20.679  24.574  -29.404 1.00 35.15  ? 376  LEU A CG    1 
ATOM   2899 C CD1   . LEU A 1 376 ? 20.544  23.870  -30.754 1.00 37.42  ? 376  LEU A CD1   1 
ATOM   2900 C CD2   . LEU A 1 376 ? 19.882  23.817  -28.363 1.00 39.11  ? 376  LEU A CD2   1 
ATOM   2901 N N     . SER A 1 377 ? 24.471  26.093  -26.523 1.00 39.79  ? 377  SER A N     1 
ATOM   2902 C CA    . SER A 1 377 ? 25.878  25.974  -26.062 1.00 40.71  ? 377  SER A CA    1 
ATOM   2903 C C     . SER A 1 377 ? 25.983  24.899  -24.972 1.00 36.19  ? 377  SER A C     1 
ATOM   2904 O O     . SER A 1 377 ? 26.942  24.124  -25.021 1.00 36.25  ? 377  SER A O     1 
ATOM   2905 C CB    . SER A 1 377 ? 26.429  27.306  -25.598 1.00 43.00  ? 377  SER A CB    1 
ATOM   2906 O OG    . SER A 1 377 ? 26.641  28.172  -26.707 1.00 44.63  ? 377  SER A OG    1 
ATOM   2907 N N     . GLU A 1 378 ? 25.022  24.807  -24.055 1.00 34.71  ? 378  GLU A N     1 
ATOM   2908 C CA    . GLU A 1 378 ? 25.134  23.892  -22.890 1.00 37.66  ? 378  GLU A CA    1 
ATOM   2909 C C     . GLU A 1 378 ? 25.131  22.424  -23.357 1.00 36.28  ? 378  GLU A C     1 
ATOM   2910 O O     . GLU A 1 378 ? 25.494  21.565  -22.538 1.00 34.38  ? 378  GLU A O     1 
ATOM   2911 C CB    . GLU A 1 378 ? 24.021  24.113  -21.860 1.00 43.82  ? 378  GLU A CB    1 
ATOM   2912 C CG    . GLU A 1 378 ? 23.977  25.522  -21.290 1.00 53.73  ? 378  GLU A CG    1 
ATOM   2913 C CD    . GLU A 1 378 ? 24.963  25.846  -20.186 1.00 62.43  ? 378  GLU A CD    1 
ATOM   2914 O OE1   . GLU A 1 378 ? 25.250  24.926  -19.374 1.00 60.37  ? 378  GLU A OE1   1 
ATOM   2915 O OE2   . GLU A 1 378 ? 25.410  27.042  -20.128 1.00 67.53  ? 378  GLU A OE2   1 
ATOM   2916 N N     . MET A 1 379 ? 24.712  22.128  -24.593 1.00 35.21  ? 379  MET A N     1 
ATOM   2917 C CA    . MET A 1 379 ? 24.711  20.744  -25.148 1.00 39.77  ? 379  MET A CA    1 
ATOM   2918 C C     . MET A 1 379 ? 26.148  20.231  -25.315 1.00 36.35  ? 379  MET A C     1 
ATOM   2919 O O     . MET A 1 379 ? 26.293  19.016  -25.376 1.00 36.83  ? 379  MET A O     1 
ATOM   2920 C CB    . MET A 1 379 ? 23.987  20.647  -26.495 1.00 39.62  ? 379  MET A CB    1 
ATOM   2921 C CG    . MET A 1 379 ? 22.485  20.479  -26.351 1.00 40.04  ? 379  MET A CG    1 
ATOM   2922 S SD    . MET A 1 379 ? 22.023  19.098  -25.280 1.00 42.97  ? 379  MET A SD    1 
ATOM   2923 C CE    . MET A 1 379 ? 22.367  17.730  -26.386 1.00 44.89  ? 379  MET A CE    1 
ATOM   2924 N N     . LYS A 1 380 ? 27.150  21.113  -25.321 1.00 34.56  ? 380  LYS A N     1 
ATOM   2925 C CA    . LYS A 1 380 ? 28.589  20.730  -25.357 1.00 40.93  ? 380  LYS A CA    1 
ATOM   2926 C C     . LYS A 1 380 ? 28.954  19.985  -24.065 1.00 40.20  ? 380  LYS A C     1 
ATOM   2927 O O     . LYS A 1 380 ? 29.916  19.191  -24.063 1.00 37.45  ? 380  LYS A O     1 
ATOM   2928 C CB    . LYS A 1 380 ? 29.447  21.975  -25.602 1.00 42.52  ? 380  LYS A CB    1 
ATOM   2929 C CG    . LYS A 1 380 ? 29.374  22.485  -27.035 1.00 47.51  ? 380  LYS A CG    1 
ATOM   2930 C CD    . LYS A 1 380 ? 30.404  23.555  -27.362 1.00 55.93  ? 380  LYS A CD    1 
ATOM   2931 C CE    . LYS A 1 380 ? 30.459  24.672  -26.338 1.00 57.55  ? 380  LYS A CE    1 
ATOM   2932 N NZ    . LYS A 1 380 ? 29.134  25.303  -26.157 1.00 56.67  ? 380  LYS A NZ    1 
ATOM   2933 N N     . LEU A 1 381 ? 28.174  20.205  -23.014 1.00 36.24  ? 381  LEU A N     1 
ATOM   2934 C CA    . LEU A 1 381 ? 28.253  19.455  -21.741 1.00 40.46  ? 381  LEU A CA    1 
ATOM   2935 C C     . LEU A 1 381 ? 28.121  17.942  -22.024 1.00 37.08  ? 381  LEU A C     1 
ATOM   2936 O O     . LEU A 1 381 ? 28.733  17.142  -21.326 1.00 34.86  ? 381  LEU A O     1 
ATOM   2937 C CB    . LEU A 1 381 ? 27.122  20.042  -20.897 1.00 46.06  ? 381  LEU A CB    1 
ATOM   2938 C CG    . LEU A 1 381 ? 27.092  19.715  -19.418 1.00 55.46  ? 381  LEU A CG    1 
ATOM   2939 C CD1   . LEU A 1 381 ? 26.893  20.981  -18.595 1.00 54.70  ? 381  LEU A CD1   1 
ATOM   2940 C CD2   . LEU A 1 381 ? 25.979  18.722  -19.164 1.00 60.34  ? 381  LEU A CD2   1 
ATOM   2941 N N     . MET A 1 382 ? 27.383  17.549  -23.056 1.00 38.13  ? 382  MET A N     1 
ATOM   2942 C CA    . MET A 1 382 ? 27.136  16.123  -23.409 1.00 39.83  ? 382  MET A CA    1 
ATOM   2943 C C     . MET A 1 382 ? 28.275  15.560  -24.282 1.00 43.00  ? 382  MET A C     1 
ATOM   2944 O O     . MET A 1 382 ? 28.199  14.360  -24.645 1.00 43.39  ? 382  MET A O     1 
ATOM   2945 C CB    . MET A 1 382 ? 25.783  15.980  -24.109 1.00 38.28  ? 382  MET A CB    1 
ATOM   2946 C CG    . MET A 1 382 ? 24.658  16.667  -23.339 1.00 38.31  ? 382  MET A CG    1 
ATOM   2947 S SD    . MET A 1 382 ? 24.600  16.205  -21.573 1.00 37.72  ? 382  MET A SD    1 
ATOM   2948 C CE    . MET A 1 382 ? 24.209  14.466  -21.660 1.00 33.84  ? 382  MET A CE    1 
ATOM   2949 N N     . ASP A 1 383 ? 29.345  16.339  -24.498 1.00 41.68  ? 383  ASP A N     1 
ATOM   2950 C CA    . ASP A 1 383 ? 30.645  15.838  -25.015 1.00 41.48  ? 383  ASP A CA    1 
ATOM   2951 C C     . ASP A 1 383 ? 31.618  15.486  -23.875 1.00 44.02  ? 383  ASP A C     1 
ATOM   2952 O O     . ASP A 1 383 ? 32.754  15.117  -24.191 1.00 46.47  ? 383  ASP A O     1 
ATOM   2953 C CB    . ASP A 1 383 ? 31.266  16.860  -25.957 1.00 42.54  ? 383  ASP A CB    1 
ATOM   2954 C CG    . ASP A 1 383 ? 30.461  17.027  -27.223 1.00 41.98  ? 383  ASP A CG    1 
ATOM   2955 O OD1   . ASP A 1 383 ? 29.914  16.019  -27.694 1.00 45.21  ? 383  ASP A OD1   1 
ATOM   2956 O OD2   . ASP A 1 383 ? 30.388  18.169  -27.713 1.00 45.71  ? 383  ASP A OD2   1 
ATOM   2957 N N     . TRP A 1 384 ? 31.201  15.572  -22.608 1.00 39.65  ? 384  TRP A N     1 
ATOM   2958 C CA    . TRP A 1 384 ? 32.046  15.270  -21.422 1.00 39.37  ? 384  TRP A CA    1 
ATOM   2959 C C     . TRP A 1 384 ? 32.650  13.864  -21.509 1.00 39.74  ? 384  TRP A C     1 
ATOM   2960 O O     . TRP A 1 384 ? 33.827  13.716  -21.271 1.00 39.20  ? 384  TRP A O     1 
ATOM   2961 C CB    . TRP A 1 384 ? 31.196  15.384  -20.160 1.00 38.75  ? 384  TRP A CB    1 
ATOM   2962 C CG    . TRP A 1 384 ? 31.947  15.268  -18.875 1.00 36.57  ? 384  TRP A CG    1 
ATOM   2963 C CD1   . TRP A 1 384 ? 31.733  14.368  -17.875 1.00 34.71  ? 384  TRP A CD1   1 
ATOM   2964 C CD2   . TRP A 1 384 ? 33.035  16.091  -18.453 1.00 32.20  ? 384  TRP A CD2   1 
ATOM   2965 N NE1   . TRP A 1 384 ? 32.564  14.623  -16.823 1.00 35.53  ? 384  TRP A NE1   1 
ATOM   2966 C CE2   . TRP A 1 384 ? 33.376  15.676  -17.146 1.00 35.45  ? 384  TRP A CE2   1 
ATOM   2967 C CE3   . TRP A 1 384 ? 33.724  17.162  -19.023 1.00 32.90  ? 384  TRP A CE3   1 
ATOM   2968 C CZ2   . TRP A 1 384 ? 34.408  16.268  -16.423 1.00 31.61  ? 384  TRP A CZ2   1 
ATOM   2969 C CZ3   . TRP A 1 384 ? 34.725  17.768  -18.294 1.00 34.71  ? 384  TRP A CZ3   1 
ATOM   2970 C CH2   . TRP A 1 384 ? 35.064  17.320  -17.016 1.00 32.28  ? 384  TRP A CH2   1 
ATOM   2971 N N     . ILE A 1 385 ? 31.805  12.897  -21.812 1.00 42.09  ? 385  ILE A N     1 
ATOM   2972 C CA    . ILE A 1 385 ? 32.229  11.539  -21.934 1.00 40.50  ? 385  ILE A CA    1 
ATOM   2973 C C     . ILE A 1 385 ? 31.557  11.018  -23.178 1.00 39.49  ? 385  ILE A C     1 
ATOM   2974 O O     . ILE A 1 385 ? 30.594  11.581  -23.634 1.00 34.09  ? 385  ILE A O     1 
ATOM   2975 C CB    . ILE A 1 385 ? 31.827  10.712  -20.697 1.00 40.56  ? 385  ILE A CB    1 
ATOM   2976 C CG1   . ILE A 1 385 ? 30.434  11.061  -20.198 1.00 41.03  ? 385  ILE A CG1   1 
ATOM   2977 C CG2   . ILE A 1 385 ? 32.820  10.892  -19.569 1.00 37.37  ? 385  ILE A CG2   1 
ATOM   2978 C CD1   . ILE A 1 385 ? 29.755  9.890   -19.540 1.00 41.28  ? 385  ILE A CD1   1 
ATOM   2979 N N     . PRO A 1 386 ? 32.115  9.969   -23.770 1.00 48.04  ? 386  PRO A N     1 
ATOM   2980 C CA    . PRO A 1 386 ? 31.451  9.358   -24.918 1.00 47.34  ? 386  PRO A CA    1 
ATOM   2981 C C     . PRO A 1 386 ? 30.103  8.733   -24.575 1.00 48.20  ? 386  PRO A C     1 
ATOM   2982 O O     . PRO A 1 386 ? 29.961  8.076   -23.555 1.00 48.42  ? 386  PRO A O     1 
ATOM   2983 C CB    . PRO A 1 386 ? 32.430  8.270   -25.352 1.00 49.44  ? 386  PRO A CB    1 
ATOM   2984 C CG    . PRO A 1 386 ? 33.483  8.195   -24.300 1.00 53.61  ? 386  PRO A CG    1 
ATOM   2985 C CD    . PRO A 1 386 ? 33.516  9.543   -23.669 1.00 52.37  ? 386  PRO A CD    1 
ATOM   2986 N N     . GLY A 1 387 ? 29.120  8.962   -25.451 1.00 60.41  ? 387  GLY A N     1 
ATOM   2987 C CA    . GLY A 1 387 ? 27.769  8.457   -25.326 1.00 45.45  ? 387  GLY A CA    1 
ATOM   2988 C C     . GLY A 1 387 ? 27.064  9.030   -24.136 1.00 38.67  ? 387  GLY A C     1 
ATOM   2989 O O     . GLY A 1 387 ? 26.224  8.397   -23.556 1.00 38.44  ? 387  GLY A O     1 
ATOM   2990 N N     . ALA A 1 388 ? 27.409  10.244  -23.784 1.00 33.60  ? 388  ALA A N     1 
ATOM   2991 C CA    . ALA A 1 388 ? 26.860  10.829  -22.599 1.00 35.96  ? 388  ALA A CA    1 
ATOM   2992 C C     . ALA A 1 388 ? 25.388  11.079  -22.593 1.00 36.92  ? 388  ALA A C     1 
ATOM   2993 O O     . ALA A 1 388 ? 24.812  11.526  -23.564 1.00 31.93  ? 388  ALA A O     1 
ATOM   2994 C CB    . ALA A 1 388 ? 27.605  12.083  -22.209 1.00 35.21  ? 388  ALA A CB    1 
ATOM   2995 N N     . GLY A 1 389 ? 24.798  10.787  -21.464 1.00 36.47  ? 389  GLY A N     1 
ATOM   2996 C CA    . GLY A 1 389 ? 23.416  11.052  -21.299 1.00 38.31  ? 389  GLY A CA    1 
ATOM   2997 C C     . GLY A 1 389 ? 23.283  11.614  -19.921 1.00 38.08  ? 389  GLY A C     1 
ATOM   2998 O O     . GLY A 1 389 ? 24.178  11.485  -19.122 1.00 36.64  ? 389  GLY A O     1 
ATOM   2999 N N     . HIS A 1 390 ? 22.164  12.251  -19.654 1.00 34.65  ? 390  HIS A N     1 
ATOM   3000 C CA    . HIS A 1 390 ? 21.941  12.753  -18.346 1.00 30.23  ? 390  HIS A CA    1 
ATOM   3001 C C     . HIS A 1 390 ? 20.576  12.490  -17.772 1.00 30.29  ? 390  HIS A C     1 
ATOM   3002 O O     . HIS A 1 390 ? 19.624  12.341  -18.513 1.00 28.94  ? 390  HIS A O     1 
ATOM   3003 C CB    . HIS A 1 390 ? 22.280  14.230  -18.322 1.00 31.78  ? 390  HIS A CB    1 
ATOM   3004 C CG    . HIS A 1 390 ? 21.165  15.110  -17.890 1.00 34.18  ? 390  HIS A CG    1 
ATOM   3005 N ND1   . HIS A 1 390 ? 21.106  15.658  -16.630 1.00 31.45  ? 390  HIS A ND1   1 
ATOM   3006 C CD2   . HIS A 1 390 ? 20.062  15.524  -18.538 1.00 32.93  ? 390  HIS A CD2   1 
ATOM   3007 C CE1   . HIS A 1 390 ? 20.007  16.383  -16.528 1.00 32.97  ? 390  HIS A CE1   1 
ATOM   3008 N NE2   . HIS A 1 390 ? 19.355  16.314  -17.671 1.00 35.37  ? 390  HIS A NE2   1 
ATOM   3009 N N     . VAL A 1 391 ? 20.500  12.405  -16.457 1.00 30.98  ? 391  VAL A N     1 
ATOM   3010 C CA    . VAL A 1 391 ? 19.229  12.325  -15.780 1.00 33.79  ? 391  VAL A CA    1 
ATOM   3011 C C     . VAL A 1 391 ? 19.219  13.480  -14.769 1.00 33.42  ? 391  VAL A C     1 
ATOM   3012 O O     . VAL A 1 391 ? 20.248  13.854  -14.225 1.00 35.24  ? 391  VAL A O     1 
ATOM   3013 C CB    . VAL A 1 391 ? 18.946  10.964  -15.125 1.00 35.82  ? 391  VAL A CB    1 
ATOM   3014 C CG1   . VAL A 1 391 ? 19.758  10.741  -13.876 1.00 38.04  ? 391  VAL A CG1   1 
ATOM   3015 C CG2   . VAL A 1 391 ? 17.470  10.814  -14.805 1.00 36.70  ? 391  VAL A CG2   1 
ATOM   3016 N N     . GLY A 1 392 ? 18.068  14.088  -14.576 1.00 32.10  ? 392  GLY A N     1 
ATOM   3017 C CA    . GLY A 1 392 ? 17.955  15.180  -13.653 1.00 29.67  ? 392  GLY A CA    1 
ATOM   3018 C C     . GLY A 1 392 ? 17.628  14.850  -12.225 1.00 29.44  ? 392  GLY A C     1 
ATOM   3019 O O     . GLY A 1 392 ? 16.818  13.989  -11.975 1.00 31.29  ? 392  GLY A O     1 
ATOM   3020 N N     . PHE A 1 393 ? 18.288  15.514  -11.301 1.00 28.55  ? 393  PHE A N     1 
ATOM   3021 C CA    . PHE A 1 393 ? 18.006  15.377  -9.885  1.00 29.58  ? 393  PHE A CA    1 
ATOM   3022 C C     . PHE A 1 393 ? 17.970  16.821  -9.412  1.00 26.47  ? 393  PHE A C     1 
ATOM   3023 O O     . PHE A 1 393 ? 18.942  17.516  -9.537  1.00 24.73  ? 393  PHE A O     1 
ATOM   3024 C CB    . PHE A 1 393 ? 19.065  14.564  -9.161  1.00 32.44  ? 393  PHE A CB    1 
ATOM   3025 C CG    . PHE A 1 393 ? 18.869  14.493  -7.682  1.00 31.69  ? 393  PHE A CG    1 
ATOM   3026 C CD1   . PHE A 1 393 ? 17.755  13.878  -7.146  1.00 30.26  ? 393  PHE A CD1   1 
ATOM   3027 C CD2   . PHE A 1 393 ? 19.805  15.036  -6.827  1.00 30.62  ? 393  PHE A CD2   1 
ATOM   3028 C CE1   . PHE A 1 393 ? 17.575  13.814  -5.784  1.00 32.83  ? 393  PHE A CE1   1 
ATOM   3029 C CE2   . PHE A 1 393 ? 19.633  14.966  -5.466  1.00 29.80  ? 393  PHE A CE2   1 
ATOM   3030 C CZ    . PHE A 1 393 ? 18.518  14.357  -4.943  1.00 28.83  ? 393  PHE A CZ    1 
ATOM   3031 N N     . SER A 1 394 ? 16.847  17.264  -8.878  1.00 27.24  ? 394  SER A N     1 
ATOM   3032 C CA    . SER A 1 394 ? 16.664  18.659  -8.527  1.00 28.85  ? 394  SER A CA    1 
ATOM   3033 C C     . SER A 1 394 ? 15.779  18.927  -7.297  1.00 29.14  ? 394  SER A C     1 
ATOM   3034 O O     . SER A 1 394 ? 14.781  19.626  -7.396  1.00 30.56  ? 394  SER A O     1 
ATOM   3035 C CB    . SER A 1 394 ? 16.059  19.376  -9.733  1.00 29.75  ? 394  SER A CB    1 
ATOM   3036 O OG    . SER A 1 394 ? 14.844  18.802  -10.122 1.00 31.81  ? 394  SER A OG    1 
ATOM   3037 N N     . PRO A 1 395 ? 16.154  18.394  -6.140  1.00 25.54  ? 395  PRO A N     1 
ATOM   3038 C CA    . PRO A 1 395 ? 15.276  18.629  -5.016  1.00 24.35  ? 395  PRO A CA    1 
ATOM   3039 C C     . PRO A 1 395 ? 15.203  20.055  -4.491  1.00 22.70  ? 395  PRO A C     1 
ATOM   3040 O O     . PRO A 1 395 ? 16.063  20.858  -4.774  1.00 21.80  ? 395  PRO A O     1 
ATOM   3041 C CB    . PRO A 1 395 ? 15.846  17.710  -3.952  1.00 27.68  ? 395  PRO A CB    1 
ATOM   3042 C CG    . PRO A 1 395 ? 17.289  17.709  -4.224  1.00 26.66  ? 395  PRO A CG    1 
ATOM   3043 C CD    . PRO A 1 395 ? 17.396  17.733  -5.717  1.00 28.26  ? 395  PRO A CD    1 
ATOM   3044 N N     . ILE A 1 396 ? 14.160  20.343  -3.739  1.00 24.48  ? 396  ILE A N     1 
ATOM   3045 C CA    . ILE A 1 396 ? 13.957  21.664  -3.163  1.00 26.64  ? 396  ILE A CA    1 
ATOM   3046 C C     . ILE A 1 396 ? 14.378  21.761  -1.709  1.00 25.95  ? 396  ILE A C     1 
ATOM   3047 O O     . ILE A 1 396 ? 14.043  20.912  -0.919  1.00 27.42  ? 396  ILE A O     1 
ATOM   3048 C CB    . ILE A 1 396 ? 12.479  22.123  -3.253  1.00 26.03  ? 396  ILE A CB    1 
ATOM   3049 C CG1   . ILE A 1 396 ? 11.858  21.717  -4.574  1.00 30.82  ? 396  ILE A CG1   1 
ATOM   3050 C CG2   . ILE A 1 396 ? 12.343  23.618  -3.041  1.00 28.00  ? 396  ILE A CG2   1 
ATOM   3051 C CD1   . ILE A 1 396 ? 12.194  22.678  -5.668  1.00 32.45  ? 396  ILE A CD1   1 
ATOM   3052 N N     . SER A 1 397 ? 15.051  22.833  -1.361  1.00 26.11  ? 397  SER A N     1 
ATOM   3053 C CA    . SER A 1 397 ? 15.544  23.027  -0.025  1.00 31.19  ? 397  SER A CA    1 
ATOM   3054 C C     . SER A 1 397 ? 15.360  24.450  0.453   1.00 27.29  ? 397  SER A C     1 
ATOM   3055 O O     . SER A 1 397 ? 15.109  25.341  -0.324  1.00 26.09  ? 397  SER A O     1 
ATOM   3056 C CB    . SER A 1 397 ? 17.056  22.743  -0.020  1.00 30.16  ? 397  SER A CB    1 
ATOM   3057 O OG    . SER A 1 397 ? 17.694  23.249  -1.159  1.00 36.41  ? 397  SER A OG    1 
ATOM   3058 N N     . PRO A 1 398 ? 15.513  24.664  1.757   1.00 27.71  ? 398  PRO A N     1 
ATOM   3059 C CA    . PRO A 1 398 ? 15.512  26.044  2.198   1.00 27.45  ? 398  PRO A CA    1 
ATOM   3060 C C     . PRO A 1 398 ? 16.824  26.669  1.749   1.00 29.49  ? 398  PRO A C     1 
ATOM   3061 O O     . PRO A 1 398 ? 17.823  25.978  1.764   1.00 30.13  ? 398  PRO A O     1 
ATOM   3062 C CB    . PRO A 1 398 ? 15.473  25.919  3.706   1.00 30.15  ? 398  PRO A CB    1 
ATOM   3063 C CG    . PRO A 1 398 ? 14.889  24.592  3.985   1.00 27.45  ? 398  PRO A CG    1 
ATOM   3064 C CD    . PRO A 1 398 ? 15.410  23.731  2.891   1.00 28.92  ? 398  PRO A CD    1 
ATOM   3065 N N     . PRO A 1 399 ? 16.822  27.945  1.359   1.00 27.70  ? 399  PRO A N     1 
ATOM   3066 C CA    . PRO A 1 399 ? 18.033  28.673  0.934   1.00 27.25  ? 399  PRO A CA    1 
ATOM   3067 C C     . PRO A 1 399 ? 18.941  29.059  2.098   1.00 28.64  ? 399  PRO A C     1 
ATOM   3068 O O     . PRO A 1 399 ? 19.103  30.225  2.350   1.00 28.58  ? 399  PRO A O     1 
ATOM   3069 C CB    . PRO A 1 399 ? 17.468  29.888  0.233   1.00 28.03  ? 399  PRO A CB    1 
ATOM   3070 C CG    . PRO A 1 399 ? 16.127  30.081  0.823   1.00 29.19  ? 399  PRO A CG    1 
ATOM   3071 C CD    . PRO A 1 399 ? 15.632  28.791  1.365   1.00 27.51  ? 399  PRO A CD    1 
ATOM   3072 N N     . VAL A 1 400 ? 19.529  28.076  2.756   1.00 29.22  ? 400  VAL A N     1 
ATOM   3073 C CA    . VAL A 1 400 ? 20.365  28.278  3.909   1.00 31.44  ? 400  VAL A CA    1 
ATOM   3074 C C     . VAL A 1 400 ? 21.656  27.482  3.698   1.00 33.01  ? 400  VAL A C     1 
ATOM   3075 O O     . VAL A 1 400 ? 21.610  26.355  3.260   1.00 29.07  ? 400  VAL A O     1 
ATOM   3076 C CB    . VAL A 1 400 ? 19.608  27.792  5.161   1.00 35.10  ? 400  VAL A CB    1 
ATOM   3077 C CG1   . VAL A 1 400 ? 20.497  27.745  6.387   1.00 38.14  ? 400  VAL A CG1   1 
ATOM   3078 C CG2   . VAL A 1 400 ? 18.364  28.619  5.436   1.00 32.52  ? 400  VAL A CG2   1 
ATOM   3079 N N     . GLY A 1 401 ? 22.803  28.079  3.984   1.00 32.71  ? 401  GLY A N     1 
ATOM   3080 C CA    . GLY A 1 401 ? 24.079  27.424  3.795   1.00 33.36  ? 401  GLY A CA    1 
ATOM   3081 C C     . GLY A 1 401 ? 24.267  26.051  4.375   1.00 31.97  ? 401  GLY A C     1 
ATOM   3082 O O     . GLY A 1 401 ? 24.819  25.211  3.734   1.00 30.14  ? 401  GLY A O     1 
ATOM   3083 N N     . ARG A 1 402 ? 23.812  25.848  5.591   1.00 33.49  ? 402  ARG A N     1 
ATOM   3084 C CA    . ARG A 1 402 ? 23.878  24.556  6.224   1.00 37.25  ? 402  ARG A CA    1 
ATOM   3085 C C     . ARG A 1 402 ? 23.148  23.517  5.379   1.00 36.75  ? 402  ARG A C     1 
ATOM   3086 O O     . ARG A 1 402 ? 23.643  22.432  5.174   1.00 34.51  ? 402  ARG A O     1 
ATOM   3087 C CB    . ARG A 1 402 ? 23.230  24.689  7.589   1.00 43.45  ? 402  ARG A CB    1 
ATOM   3088 C CG    . ARG A 1 402 ? 23.479  23.600  8.600   1.00 53.50  ? 402  ARG A CG    1 
ATOM   3089 C CD    . ARG A 1 402 ? 22.233  22.759  8.790   1.00 63.88  ? 402  ARG A CD    1 
ATOM   3090 N NE    . ARG A 1 402 ? 21.139  23.513  9.383   1.00 73.04  ? 402  ARG A NE    1 
ATOM   3091 C CZ    . ARG A 1 402 ? 19.860  23.310  9.096   1.00 75.53  ? 402  ARG A CZ    1 
ATOM   3092 N NH1   . ARG A 1 402 ? 19.521  22.380  8.218   1.00 72.90  ? 402  ARG A NH1   1 
ATOM   3093 N NH2   . ARG A 1 402 ? 18.926  24.037  9.686   1.00 77.83  ? 402  ARG A NH2   1 
ATOM   3094 N N     . ASP A 1 403 ? 21.971  23.860  4.877   1.00 35.32  ? 403  ASP A N     1 
ATOM   3095 C CA    . ASP A 1 403 ? 21.228  22.951  4.004   1.00 32.80  ? 403  ASP A CA    1 
ATOM   3096 C C     . ASP A 1 403 ? 21.983  22.679  2.726   1.00 30.86  ? 403  ASP A C     1 
ATOM   3097 O O     . ASP A 1 403 ? 22.030  21.561  2.264   1.00 32.15  ? 403  ASP A O     1 
ATOM   3098 C CB    . ASP A 1 403 ? 19.843  23.496  3.685   1.00 33.98  ? 403  ASP A CB    1 
ATOM   3099 C CG    . ASP A 1 403 ? 18.957  23.546  4.881   1.00 32.08  ? 403  ASP A CG    1 
ATOM   3100 O OD1   . ASP A 1 403 ? 18.408  22.510  5.237   1.00 30.35  ? 403  ASP A OD1   1 
ATOM   3101 O OD2   . ASP A 1 403 ? 18.809  24.614  5.471   1.00 34.66  ? 403  ASP A OD2   1 
ATOM   3102 N N     . ALA A 1 404 ? 22.584  23.708  2.168   1.00 31.18  ? 404  ALA A N     1 
ATOM   3103 C CA    . ALA A 1 404 ? 23.371  23.547  0.970   1.00 30.99  ? 404  ALA A CA    1 
ATOM   3104 C C     . ALA A 1 404 ? 24.531  22.616  1.193   1.00 32.04  ? 404  ALA A C     1 
ATOM   3105 O O     . ALA A 1 404 ? 24.750  21.719  0.428   1.00 31.96  ? 404  ALA A O     1 
ATOM   3106 C CB    . ALA A 1 404 ? 23.860  24.883  0.508   1.00 27.73  ? 404  ALA A CB    1 
ATOM   3107 N N     . MET A 1 405 ? 25.259  22.838  2.265   1.00 32.61  ? 405  MET A N     1 
ATOM   3108 C CA    . MET A 1 405 ? 26.410  22.022  2.564   1.00 32.78  ? 405  MET A CA    1 
ATOM   3109 C C     . MET A 1 405 ? 26.007  20.583  2.754   1.00 28.82  ? 405  MET A C     1 
ATOM   3110 O O     . MET A 1 405 ? 26.633  19.715  2.204   1.00 27.42  ? 405  MET A O     1 
ATOM   3111 C CB    . MET A 1 405 ? 27.160  22.568  3.767   1.00 34.54  ? 405  MET A CB    1 
ATOM   3112 C CG    . MET A 1 405 ? 27.919  23.848  3.500   1.00 35.32  ? 405  MET A CG    1 
ATOM   3113 S SD    . MET A 1 405 ? 29.309  23.692  2.372   1.00 46.48  ? 405  MET A SD    1 
ATOM   3114 C CE    . MET A 1 405 ? 30.249  22.400  3.163   1.00 43.02  ? 405  MET A CE    1 
ATOM   3115 N N     . LYS A 1 406 ? 24.930  20.351  3.483   1.00 28.52  ? 406  LYS A N     1 
ATOM   3116 C CA    . LYS A 1 406 ? 24.432  19.011  3.679   1.00 30.48  ? 406  LYS A CA    1 
ATOM   3117 C C     . LYS A 1 406 ? 24.180  18.313  2.353   1.00 32.23  ? 406  LYS A C     1 
ATOM   3118 O O     . LYS A 1 406 ? 24.709  17.257  2.121   1.00 24.50  ? 406  LYS A O     1 
ATOM   3119 C CB    . LYS A 1 406 ? 23.180  19.014  4.517   1.00 33.51  ? 406  LYS A CB    1 
ATOM   3120 C CG    . LYS A 1 406 ? 22.817  17.637  5.025   1.00 37.37  ? 406  LYS A CG    1 
ATOM   3121 C CD    . LYS A 1 406 ? 21.869  17.728  6.192   1.00 42.88  ? 406  LYS A CD    1 
ATOM   3122 C CE    . LYS A 1 406 ? 20.465  17.926  5.682   1.00 49.11  ? 406  LYS A CE    1 
ATOM   3123 N NZ    . LYS A 1 406 ? 19.556  18.548  6.675   1.00 49.71  ? 406  LYS A NZ    1 
ATOM   3124 N N     . GLN A 1 407 ? 23.411  18.945  1.485   1.00 30.49  ? 407  GLN A N     1 
ATOM   3125 C CA    . GLN A 1 407 ? 23.119  18.377  0.177   1.00 31.65  ? 407  GLN A CA    1 
ATOM   3126 C C     . GLN A 1 407 ? 24.351  18.147  -0.682  1.00 32.39  ? 407  GLN A C     1 
ATOM   3127 O O     . GLN A 1 407 ? 24.497  17.086  -1.237  1.00 31.21  ? 407  GLN A O     1 
ATOM   3128 C CB    . GLN A 1 407 ? 22.151  19.270  -0.551  1.00 30.32  ? 407  GLN A CB    1 
ATOM   3129 C CG    . GLN A 1 407 ? 20.815  19.405  0.124   1.00 30.57  ? 407  GLN A CG    1 
ATOM   3130 C CD    . GLN A 1 407 ? 19.964  20.466  -0.517  1.00 31.56  ? 407  GLN A CD    1 
ATOM   3131 O OE1   . GLN A 1 407 ? 20.090  21.637  -0.203  1.00 33.50  ? 407  GLN A OE1   1 
ATOM   3132 N NE2   . GLN A 1 407 ? 19.102  20.063  -1.428  1.00 30.19  ? 407  GLN A NE2   1 
ATOM   3133 N N     . PHE A 1 408 ? 25.212  19.145  -0.804  1.00 34.50  ? 408  PHE A N     1 
ATOM   3134 C CA    . PHE A 1 408 ? 26.462  19.027  -1.538  1.00 32.30  ? 408  PHE A CA    1 
ATOM   3135 C C     . PHE A 1 408 ? 27.193  17.772  -1.116  1.00 29.82  ? 408  PHE A C     1 
ATOM   3136 O O     . PHE A 1 408 ? 27.501  16.932  -1.929  1.00 26.98  ? 408  PHE A O     1 
ATOM   3137 C CB    . PHE A 1 408 ? 27.259  20.271  -1.204  1.00 35.96  ? 408  PHE A CB    1 
ATOM   3138 C CG    . PHE A 1 408 ? 28.702  20.252  -1.627  1.00 37.24  ? 408  PHE A CG    1 
ATOM   3139 C CD1   . PHE A 1 408 ? 29.087  19.822  -2.875  1.00 35.50  ? 408  PHE A CD1   1 
ATOM   3140 C CD2   . PHE A 1 408 ? 29.672  20.734  -0.770  1.00 37.54  ? 408  PHE A CD2   1 
ATOM   3141 C CE1   . PHE A 1 408 ? 30.410  19.831  -3.246  1.00 38.88  ? 408  PHE A CE1   1 
ATOM   3142 C CE2   . PHE A 1 408 ? 30.996  20.752  -1.137  1.00 39.44  ? 408  PHE A CE2   1 
ATOM   3143 C CZ    . PHE A 1 408 ? 31.366  20.299  -2.379  1.00 38.33  ? 408  PHE A CZ    1 
ATOM   3144 N N     . ARG A 1 409 ? 27.403  17.633  0.173   1.00 31.11  ? 409  ARG A N     1 
ATOM   3145 C CA    . ARG A 1 409 ? 28.076  16.471  0.698   1.00 35.00  ? 409  ARG A CA    1 
ATOM   3146 C C     . ARG A 1 409 ? 27.355  15.143  0.465   1.00 31.67  ? 409  ARG A C     1 
ATOM   3147 O O     . ARG A 1 409 ? 27.961  14.215  0.001   1.00 35.06  ? 409  ARG A O     1 
ATOM   3148 C CB    . ARG A 1 409 ? 28.389  16.695  2.170   1.00 38.95  ? 409  ARG A CB    1 
ATOM   3149 C CG    . ARG A 1 409 ? 29.226  17.940  2.403   1.00 50.86  ? 409  ARG A CG    1 
ATOM   3150 C CD    . ARG A 1 409 ? 30.407  17.727  3.328   1.00 61.39  ? 409  ARG A CD    1 
ATOM   3151 N NE    . ARG A 1 409 ? 31.280  18.902  3.363   1.00 67.72  ? 409  ARG A NE    1 
ATOM   3152 C CZ    . ARG A 1 409 ? 32.279  19.124  2.514   1.00 65.49  ? 409  ARG A CZ    1 
ATOM   3153 N NH1   . ARG A 1 409 ? 32.548  18.249  1.559   1.00 65.22  ? 409  ARG A NH1   1 
ATOM   3154 N NH2   . ARG A 1 409 ? 33.017  20.219  2.624   1.00 65.22  ? 409  ARG A NH2   1 
ATOM   3155 N N     . MET A 1 410 ? 26.072  15.069  0.748   1.00 31.91  ? 410  MET A N     1 
ATOM   3156 C CA    . MET A 1 410 ? 25.297  13.855  0.542   1.00 33.84  ? 410  MET A CA    1 
ATOM   3157 C C     . MET A 1 410 ? 25.318  13.393  -0.900  1.00 31.87  ? 410  MET A C     1 
ATOM   3158 O O     . MET A 1 410 ? 25.539  12.236  -1.172  1.00 32.19  ? 410  MET A O     1 
ATOM   3159 C CB    . MET A 1 410 ? 23.833  14.085  0.874   1.00 39.46  ? 410  MET A CB    1 
ATOM   3160 C CG    . MET A 1 410 ? 23.419  14.267  2.306   1.00 42.67  ? 410  MET A CG    1 
ATOM   3161 S SD    . MET A 1 410 ? 21.786  15.012  2.215   1.00 35.36  ? 410  MET A SD    1 
ATOM   3162 C CE    . MET A 1 410 ? 20.807  13.549  1.986   1.00 35.40  ? 410  MET A CE    1 
ATOM   3163 N N     . VAL A 1 411 ? 25.075  14.302  -1.815  1.00 30.13  ? 411  VAL A N     1 
ATOM   3164 C CA    . VAL A 1 411 ? 24.998  13.923  -3.205  1.00 28.09  ? 411  VAL A CA    1 
ATOM   3165 C C     . VAL A 1 411 ? 26.364  13.538  -3.784  1.00 31.17  ? 411  VAL A C     1 
ATOM   3166 O O     . VAL A 1 411 ? 26.484  12.512  -4.404  1.00 30.40  ? 411  VAL A O     1 
ATOM   3167 C CB    . VAL A 1 411 ? 24.254  14.989  -4.021  1.00 27.59  ? 411  VAL A CB    1 
ATOM   3168 C CG1   . VAL A 1 411 ? 24.242  14.668  -5.506  1.00 24.25  ? 411  VAL A CG1   1 
ATOM   3169 C CG2   . VAL A 1 411 ? 22.847  15.167  -3.486  1.00 28.04  ? 411  VAL A CG2   1 
ATOM   3170 N N     . ARG A 1 412 ? 27.381  14.350  -3.539  1.00 31.35  ? 412  ARG A N     1 
ATOM   3171 C CA    . ARG A 1 412 ? 28.715  14.039  -4.039  1.00 33.94  ? 412  ARG A CA    1 
ATOM   3172 C C     . ARG A 1 412 ? 29.230  12.710  -3.527  1.00 31.28  ? 412  ARG A C     1 
ATOM   3173 O O     . ARG A 1 412 ? 29.747  11.925  -4.278  1.00 31.48  ? 412  ARG A O     1 
ATOM   3174 C CB    . ARG A 1 412 ? 29.723  15.138  -3.762  1.00 32.85  ? 412  ARG A CB    1 
ATOM   3175 C CG    . ARG A 1 412 ? 31.049  14.905  -4.452  1.00 35.46  ? 412  ARG A CG    1 
ATOM   3176 C CD    . ARG A 1 412 ? 31.955  16.097  -4.299  1.00 38.66  ? 412  ARG A CD    1 
ATOM   3177 N NE    . ARG A 1 412 ? 32.375  16.249  -2.921  1.00 35.79  ? 412  ARG A NE    1 
ATOM   3178 C CZ    . ARG A 1 412 ? 33.307  17.094  -2.523  1.00 38.43  ? 412  ARG A CZ    1 
ATOM   3179 N NH1   . ARG A 1 412 ? 33.921  17.869  -3.400  1.00 41.58  ? 412  ARG A NH1   1 
ATOM   3180 N NH2   . ARG A 1 412 ? 33.622  17.156  -1.247  1.00 39.28  ? 412  ARG A NH2   1 
ATOM   3181 N N     . SER A 1 413 ? 29.060  12.475  -2.245  1.00 33.40  ? 413  SER A N     1 
ATOM   3182 C CA    . SER A 1 413 ? 29.491  11.231  -1.671  1.00 37.02  ? 413  SER A CA    1 
ATOM   3183 C C     . SER A 1 413 ? 28.836  10.051  -2.366  1.00 36.29  ? 413  SER A C     1 
ATOM   3184 O O     . SER A 1 413 ? 29.512  9.109   -2.743  1.00 34.31  ? 413  SER A O     1 
ATOM   3185 C CB    . SER A 1 413 ? 29.255  11.210  -0.165  1.00 38.08  ? 413  SER A CB    1 
ATOM   3186 O OG    . SER A 1 413 ? 27.894  11.034  0.153   1.00 50.33  ? 413  SER A OG    1 
ATOM   3187 N N     . ARG A 1 414 ? 27.534  10.121  -2.576  1.00 31.23  ? 414  ARG A N     1 
ATOM   3188 C CA    . ARG A 1 414 ? 26.850  9.058   -3.264  1.00 33.12  ? 414  ARG A CA    1 
ATOM   3189 C C     . ARG A 1 414 ? 27.270  8.947   -4.723  1.00 29.38  ? 414  ARG A C     1 
ATOM   3190 O O     . ARG A 1 414 ? 27.473  7.872   -5.215  1.00 32.71  ? 414  ARG A O     1 
ATOM   3191 C CB    . ARG A 1 414 ? 25.351  9.189   -3.102  1.00 33.43  ? 414  ARG A CB    1 
ATOM   3192 C CG    . ARG A 1 414 ? 24.841  8.976   -1.693  1.00 35.70  ? 414  ARG A CG    1 
ATOM   3193 C CD    . ARG A 1 414 ? 25.379  7.704   -1.073  1.00 34.64  ? 414  ARG A CD    1 
ATOM   3194 N NE    . ARG A 1 414 ? 24.625  7.338   0.115   1.00 31.85  ? 414  ARG A NE    1 
ATOM   3195 C CZ    . ARG A 1 414 ? 24.977  6.381   0.961   1.00 36.80  ? 414  ARG A CZ    1 
ATOM   3196 N NH1   . ARG A 1 414 ? 26.074  5.682   0.753   1.00 37.77  ? 414  ARG A NH1   1 
ATOM   3197 N NH2   . ARG A 1 414 ? 24.229  6.120   2.017   1.00 36.30  ? 414  ARG A NH2   1 
ATOM   3198 N N     . ALA A 1 415 ? 27.416  10.053  -5.396  1.00 27.68  ? 415  ALA A N     1 
ATOM   3199 C CA    . ALA A 1 415 ? 27.863  10.032  -6.759  1.00 29.33  ? 415  ALA A CA    1 
ATOM   3200 C C     . ALA A 1 415 ? 29.243  9.394   -6.902  1.00 30.77  ? 415  ALA A C     1 
ATOM   3201 O O     . ALA A 1 415 ? 29.452  8.612   -7.798  1.00 28.68  ? 415  ALA A O     1 
ATOM   3202 C CB    . ALA A 1 415 ? 27.832  11.429  -7.312  1.00 29.15  ? 415  ALA A CB    1 
ATOM   3203 N N     . ASP A 1 416 ? 30.154  9.695   -5.994  1.00 31.91  ? 416  ASP A N     1 
ATOM   3204 C CA    . ASP A 1 416 ? 31.484  9.103   -6.002  1.00 35.10  ? 416  ASP A CA    1 
ATOM   3205 C C     . ASP A 1 416 ? 31.372  7.608   -5.871  1.00 33.86  ? 416  ASP A C     1 
ATOM   3206 O O     . ASP A 1 416 ? 31.993  6.879   -6.608  1.00 34.05  ? 416  ASP A O     1 
ATOM   3207 C CB    . ASP A 1 416 ? 32.296  9.672   -4.846  1.00 34.40  ? 416  ASP A CB    1 
ATOM   3208 C CG    . ASP A 1 416 ? 32.814  11.064  -5.116  1.00 37.09  ? 416  ASP A CG    1 
ATOM   3209 O OD1   . ASP A 1 416 ? 32.688  11.555  -6.246  1.00 36.09  ? 416  ASP A OD1   1 
ATOM   3210 O OD2   . ASP A 1 416 ? 33.350  11.680  -4.183  1.00 38.15  ? 416  ASP A OD2   1 
ATOM   3211 N N     . GLU A 1 417 ? 30.555  7.157   -4.945  1.00 33.76  ? 417  GLU A N     1 
ATOM   3212 C CA    . GLU A 1 417 ? 30.299  5.736   -4.767  1.00 37.13  ? 417  GLU A CA    1 
ATOM   3213 C C     . GLU A 1 417 ? 29.747  5.060   -6.030  1.00 40.30  ? 417  GLU A C     1 
ATOM   3214 O O     . GLU A 1 417 ? 30.072  3.925   -6.311  1.00 38.34  ? 417  GLU A O     1 
ATOM   3215 C CB    . GLU A 1 417 ? 29.326  5.585   -3.605  1.00 37.69  ? 417  GLU A CB    1 
ATOM   3216 C CG    . GLU A 1 417 ? 28.811  4.204   -3.280  1.00 42.62  ? 417  GLU A CG    1 
ATOM   3217 C CD    . GLU A 1 417 ? 27.851  4.250   -2.114  1.00 50.86  ? 417  GLU A CD    1 
ATOM   3218 O OE1   . GLU A 1 417 ? 27.149  3.250   -1.860  1.00 53.02  ? 417  GLU A OE1   1 
ATOM   3219 O OE2   . GLU A 1 417 ? 27.805  5.300   -1.449  1.00 40.68  ? 417  GLU A OE2   1 
ATOM   3220 N N     . TYR A 1 418 ? 28.943  5.769   -6.804  1.00 36.18  ? 418  TYR A N     1 
ATOM   3221 C CA    . TYR A 1 418 ? 28.322  5.199   -7.988  1.00 34.54  ? 418  TYR A CA    1 
ATOM   3222 C C     . TYR A 1 418 ? 29.034  5.594   -9.241  1.00 34.35  ? 418  TYR A C     1 
ATOM   3223 O O     . TYR A 1 418 ? 28.464  5.480   -10.304 1.00 39.54  ? 418  TYR A O     1 
ATOM   3224 C CB    . TYR A 1 418 ? 26.847  5.557   -8.039  1.00 33.91  ? 418  TYR A CB    1 
ATOM   3225 C CG    . TYR A 1 418 ? 25.993  4.765   -7.079  1.00 31.39  ? 418  TYR A CG    1 
ATOM   3226 C CD1   . TYR A 1 418 ? 25.930  5.095   -5.740  1.00 30.58  ? 418  TYR A CD1   1 
ATOM   3227 C CD2   . TYR A 1 418 ? 25.251  3.687   -7.515  1.00 31.86  ? 418  TYR A CD2   1 
ATOM   3228 C CE1   . TYR A 1 418 ? 25.164  4.374   -4.861  1.00 34.01  ? 418  TYR A CE1   1 
ATOM   3229 C CE2   . TYR A 1 418 ? 24.478  2.959   -6.641  1.00 31.36  ? 418  TYR A CE2   1 
ATOM   3230 C CZ    . TYR A 1 418 ? 24.439  3.310   -5.316  1.00 34.16  ? 418  TYR A CZ    1 
ATOM   3231 O OH    . TYR A 1 418 ? 23.672  2.589   -4.440  1.00 36.09  ? 418  TYR A OH    1 
ATOM   3232 N N     . ALA A 1 419 ? 30.283  6.015   -9.112  1.00 34.00  ? 419  ALA A N     1 
ATOM   3233 C CA    . ALA A 1 419 ? 31.104  6.442   -10.226 1.00 34.83  ? 419  ALA A CA    1 
ATOM   3234 C C     . ALA A 1 419 ? 30.494  7.461   -11.153 1.00 37.85  ? 419  ALA A C     1 
ATOM   3235 O O     . ALA A 1 419 ? 30.631  7.348   -12.355 1.00 35.32  ? 419  ALA A O     1 
ATOM   3236 C CB    . ALA A 1 419 ? 31.630  5.249   -10.997 1.00 34.92  ? 419  ALA A CB    1 
ATOM   3237 N N     . LYS A 1 420 ? 29.821  8.450   -10.590 1.00 34.78  ? 420  LYS A N     1 
ATOM   3238 C CA    . LYS A 1 420 ? 29.229  9.491   -11.383 1.00 35.64  ? 420  LYS A CA    1 
ATOM   3239 C C     . LYS A 1 420 ? 29.774  10.810  -10.909 1.00 32.46  ? 420  LYS A C     1 
ATOM   3240 O O     . LYS A 1 420 ? 29.891  11.040  -9.742  1.00 39.63  ? 420  LYS A O     1 
ATOM   3241 C CB    . LYS A 1 420 ? 27.708  9.470   -11.304 1.00 34.48  ? 420  LYS A CB    1 
ATOM   3242 C CG    . LYS A 1 420 ? 27.027  8.172   -11.698 1.00 36.47  ? 420  LYS A CG    1 
ATOM   3243 C CD    . LYS A 1 420 ? 27.143  7.891   -13.182 1.00 35.84  ? 420  LYS A CD    1 
ATOM   3244 C CE    . LYS A 1 420 ? 26.984  6.415   -13.477 1.00 38.60  ? 420  LYS A CE    1 
ATOM   3245 N NZ    . LYS A 1 420 ? 28.215  5.648   -13.184 1.00 42.34  ? 420  LYS A NZ    1 
ATOM   3246 N N     . ASP A 1 421 ? 30.139  11.665  -11.834 1.00 40.67  ? 421  ASP A N     1 
ATOM   3247 C CA    . ASP A 1 421 ? 30.666  12.960  -11.489 1.00 40.99  ? 421  ASP A CA    1 
ATOM   3248 C C     . ASP A 1 421 ? 29.665  13.864  -10.833 1.00 36.06  ? 421  ASP A C     1 
ATOM   3249 O O     . ASP A 1 421 ? 28.499  13.836  -11.145 1.00 29.68  ? 421  ASP A O     1 
ATOM   3250 C CB    . ASP A 1 421 ? 31.255  13.660  -12.702 1.00 47.14  ? 421  ASP A CB    1 
ATOM   3251 C CG    . ASP A 1 421 ? 32.396  12.874  -13.327 1.00 43.74  ? 421  ASP A CG    1 
ATOM   3252 O OD1   . ASP A 1 421 ? 32.966  11.998  -12.657 1.00 47.32  ? 421  ASP A OD1   1 
ATOM   3253 O OD2   . ASP A 1 421 ? 32.726  13.130  -14.490 1.00 41.08  ? 421  ASP A OD2   1 
ATOM   3254 N N     . TYR A 1 422 ? 30.141  14.638  -9.876  1.00 34.40  ? 422  TYR A N     1 
ATOM   3255 C CA    . TYR A 1 422 ? 29.289  15.608  -9.246  1.00 33.04  ? 422  TYR A CA    1 
ATOM   3256 C C     . TYR A 1 422 ? 29.341  16.861  -10.068 1.00 31.98  ? 422  TYR A C     1 
ATOM   3257 O O     . TYR A 1 422 ? 30.304  17.588  -10.010 1.00 30.08  ? 422  TYR A O     1 
ATOM   3258 C CB    . TYR A 1 422 ? 29.674  15.867  -7.803  1.00 35.26  ? 422  TYR A CB    1 
ATOM   3259 C CG    . TYR A 1 422 ? 28.862  16.938  -7.124  1.00 32.23  ? 422  TYR A CG    1 
ATOM   3260 C CD1   . TYR A 1 422 ? 27.560  16.703  -6.723  1.00 34.26  ? 422  TYR A CD1   1 
ATOM   3261 C CD2   . TYR A 1 422 ? 29.404  18.180  -6.877  1.00 32.67  ? 422  TYR A CD2   1 
ATOM   3262 C CE1   . TYR A 1 422 ? 26.822  17.681  -6.098  1.00 31.12  ? 422  TYR A CE1   1 
ATOM   3263 C CE2   . TYR A 1 422 ? 28.672  19.165  -6.270  1.00 34.38  ? 422  TYR A CE2   1 
ATOM   3264 C CZ    . TYR A 1 422 ? 27.387  18.911  -5.875  1.00 29.91  ? 422  TYR A CZ    1 
ATOM   3265 O OH    . TYR A 1 422 ? 26.680  19.907  -5.265  1.00 29.29  ? 422  TYR A OH    1 
ATOM   3266 N N     . ALA A 1 423 ? 28.313  17.071  -10.871 1.00 31.60  ? 423  ALA A N     1 
ATOM   3267 C CA    . ALA A 1 423 ? 28.195  18.259  -11.664 1.00 30.45  ? 423  ALA A CA    1 
ATOM   3268 C C     . ALA A 1 423 ? 26.868  18.818  -11.234 1.00 33.51  ? 423  ALA A C     1 
ATOM   3269 O O     . ALA A 1 423 ? 25.841  18.262  -11.557 1.00 33.02  ? 423  ALA A O     1 
ATOM   3270 C CB    . ALA A 1 423 ? 28.199  17.937  -13.127 1.00 30.64  ? 423  ALA A CB    1 
ATOM   3271 N N     . ALA A 1 424 ? 26.892  19.910  -10.503 1.00 31.30  ? 424  ALA A N     1 
ATOM   3272 C CA    . ALA A 1 424 ? 25.705  20.465  -9.956  1.00 30.82  ? 424  ALA A CA    1 
ATOM   3273 C C     . ALA A 1 424 ? 25.679  21.949  -9.834  1.00 31.67  ? 424  ALA A C     1 
ATOM   3274 O O     . ALA A 1 424 ? 26.698  22.604  -9.969  1.00 30.38  ? 424  ALA A O     1 
ATOM   3275 C CB    . ALA A 1 424 ? 25.484  19.889  -8.584  1.00 29.80  ? 424  ALA A CB    1 
ATOM   3276 N N     . GLN A 1 425 ? 24.497  22.464  -9.549  1.00 31.20  ? 425  GLN A N     1 
ATOM   3277 C CA    . GLN A 1 425 ? 24.329  23.859  -9.324  1.00 31.02  ? 425  GLN A CA    1 
ATOM   3278 C C     . GLN A 1 425 ? 23.286  24.120  -8.264  1.00 31.80  ? 425  GLN A C     1 
ATOM   3279 O O     . GLN A 1 425 ? 22.360  23.367  -8.104  1.00 31.98  ? 425  GLN A O     1 
ATOM   3280 C CB    . GLN A 1 425 ? 23.947  24.578  -10.597 1.00 35.40  ? 425  GLN A CB    1 
ATOM   3281 C CG    . GLN A 1 425 ? 22.672  24.152  -11.270 1.00 35.20  ? 425  GLN A CG    1 
ATOM   3282 C CD    . GLN A 1 425 ? 22.308  25.117  -12.359 1.00 36.87  ? 425  GLN A CD    1 
ATOM   3283 O OE1   . GLN A 1 425 ? 22.587  26.295  -12.247 1.00 45.46  ? 425  GLN A OE1   1 
ATOM   3284 N NE2   . GLN A 1 425 ? 21.700  24.627  -13.421 1.00 41.29  ? 425  GLN A NE2   1 
ATOM   3285 N N     . PHE A 1 426 ? 23.460  25.192  -7.522  1.00 32.27  ? 426  PHE A N     1 
ATOM   3286 C CA    . PHE A 1 426 ? 22.477  25.590  -6.548  1.00 28.40  ? 426  PHE A CA    1 
ATOM   3287 C C     . PHE A 1 426 ? 21.865  26.848  -7.107  1.00 29.46  ? 426  PHE A C     1 
ATOM   3288 O O     . PHE A 1 426 ? 22.559  27.764  -7.502  1.00 30.53  ? 426  PHE A O     1 
ATOM   3289 C CB    . PHE A 1 426 ? 23.061  25.823  -5.164  1.00 28.72  ? 426  PHE A CB    1 
ATOM   3290 C CG    . PHE A 1 426 ? 23.402  24.577  -4.413  1.00 28.41  ? 426  PHE A CG    1 
ATOM   3291 C CD1   . PHE A 1 426 ? 24.644  23.989  -4.544  1.00 30.18  ? 426  PHE A CD1   1 
ATOM   3292 C CD2   . PHE A 1 426 ? 22.492  24.014  -3.546  1.00 29.09  ? 426  PHE A CD2   1 
ATOM   3293 C CE1   . PHE A 1 426 ? 24.961  22.853  -3.838  1.00 27.85  ? 426  PHE A CE1   1 
ATOM   3294 C CE2   . PHE A 1 426 ? 22.803  22.877  -2.835  1.00 32.00  ? 426  PHE A CE2   1 
ATOM   3295 C CZ    . PHE A 1 426 ? 24.041  22.298  -2.979  1.00 28.44  ? 426  PHE A CZ    1 
ATOM   3296 N N     . VAL A 1 427 ? 20.557  26.876  -7.159  1.00 29.39  ? 427  VAL A N     1 
ATOM   3297 C CA    . VAL A 1 427 ? 19.851  27.999  -7.717  1.00 32.90  ? 427  VAL A CA    1 
ATOM   3298 C C     . VAL A 1 427 ? 18.877  28.488  -6.671  1.00 32.11  ? 427  VAL A C     1 
ATOM   3299 O O     . VAL A 1 427 ? 18.157  27.716  -6.096  1.00 34.02  ? 427  VAL A O     1 
ATOM   3300 C CB    . VAL A 1 427 ? 19.071  27.539  -8.965  1.00 31.05  ? 427  VAL A CB    1 
ATOM   3301 C CG1   . VAL A 1 427 ? 18.138  28.597  -9.465  1.00 34.65  ? 427  VAL A CG1   1 
ATOM   3302 C CG2   . VAL A 1 427 ? 19.986  27.037  -10.058 1.00 33.10  ? 427  VAL A CG2   1 
ATOM   3303 N N     . VAL A 1 428 ? 18.792  29.786  -6.416  1.00 38.79  ? 428  VAL A N     1 
ATOM   3304 C CA    . VAL A 1 428 ? 17.721  30.299  -5.534  1.00 39.46  ? 428  VAL A CA    1 
ATOM   3305 C C     . VAL A 1 428 ? 16.627  31.070  -6.311  1.00 43.37  ? 428  VAL A C     1 
ATOM   3306 O O     . VAL A 1 428 ? 16.904  32.009  -7.031  1.00 37.08  ? 428  VAL A O     1 
ATOM   3307 C CB    . VAL A 1 428 ? 18.187  31.012  -4.227  1.00 39.63  ? 428  VAL A CB    1 
ATOM   3308 C CG1   . VAL A 1 428 ? 19.253  30.232  -3.485  1.00 40.75  ? 428  VAL A CG1   1 
ATOM   3309 C CG2   . VAL A 1 428 ? 18.539  32.466  -4.411  1.00 45.49  ? 428  VAL A CG2   1 
ATOM   3310 N N     . GLY A 1 429 ? 15.380  30.629  -6.193  1.00 47.20  ? 429  GLY A N     1 
ATOM   3311 C CA    . GLY A 1 429 ? 14.283  31.299  -6.866  1.00 52.38  ? 429  GLY A CA    1 
ATOM   3312 C C     . GLY A 1 429 ? 13.927  32.593  -6.192  1.00 66.95  ? 429  GLY A C     1 
ATOM   3313 O O     . GLY A 1 429 ? 14.198  33.641  -6.739  1.00 84.55  ? 429  GLY A O     1 
ATOM   3314 N N     . LEU A 1 430 ? 13.318  32.523  -5.023  1.00 48.19  ? 430  LEU A N     1 
ATOM   3315 C CA    . LEU A 1 430 ? 13.041  33.708  -4.234  1.00 46.00  ? 430  LEU A CA    1 
ATOM   3316 C C     . LEU A 1 430 ? 13.294  33.320  -2.790  1.00 39.31  ? 430  LEU A C     1 
ATOM   3317 O O     . LEU A 1 430 ? 14.185  33.863  -2.169  1.00 36.70  ? 430  LEU A O     1 
ATOM   3318 C CB    . LEU A 1 430 ? 11.623  34.176  -4.426  1.00 53.80  ? 430  LEU A CB    1 
ATOM   3319 C CG    . LEU A 1 430 ? 11.286  35.581  -3.980  1.00 50.63  ? 430  LEU A CG    1 
ATOM   3320 C CD1   . LEU A 1 430 ? 12.130  36.488  -4.840  1.00 60.79  ? 430  LEU A CD1   1 
ATOM   3321 C CD2   . LEU A 1 430 ? 9.811   35.824  -4.241  1.00 40.38  ? 430  LEU A CD2   1 
ATOM   3322 N N     . ARG A 1 431 ? 12.516  32.380  -2.261  1.00 33.59  ? 431  ARG A N     1 
ATOM   3323 C CA    . ARG A 1 431 ? 12.727  31.877  -0.904  1.00 34.67  ? 431  ARG A CA    1 
ATOM   3324 C C     . ARG A 1 431 ? 12.983  30.376  -0.877  1.00 30.17  ? 431  ARG A C     1 
ATOM   3325 O O     . ARG A 1 431 ? 12.865  29.772  0.158   1.00 32.03  ? 431  ARG A O     1 
ATOM   3326 C CB    . ARG A 1 431 ? 11.549  32.154  0.001   1.00 35.77  ? 431  ARG A CB    1 
ATOM   3327 C CG    . ARG A 1 431 ? 10.570  33.169  -0.475  1.00 40.70  ? 431  ARG A CG    1 
ATOM   3328 C CD    . ARG A 1 431 ? 9.432   33.254  0.518   1.00 34.90  ? 431  ARG A CD    1 
ATOM   3329 N NE    . ARG A 1 431 ? 9.326   34.575  1.107   1.00 35.78  ? 431  ARG A NE    1 
ATOM   3330 C CZ    . ARG A 1 431 ? 8.889   35.645  0.463   1.00 34.48  ? 431  ARG A CZ    1 
ATOM   3331 N NH1   . ARG A 1 431 ? 8.502   35.559  -0.798  1.00 31.28  ? 431  ARG A NH1   1 
ATOM   3332 N NH2   . ARG A 1 431 ? 8.829   36.801  1.091   1.00 35.66  ? 431  ARG A NH2   1 
ATOM   3333 N N     . GLU A 1 432 ? 13.305  29.792  -2.009  1.00 29.88  ? 432  GLU A N     1 
ATOM   3334 C CA    . GLU A 1 432 ? 13.524  28.362  -2.111  1.00 30.11  ? 432  GLU A CA    1 
ATOM   3335 C C     . GLU A 1 432 ? 14.788  28.072  -2.866  1.00 29.94  ? 432  GLU A C     1 
ATOM   3336 O O     . GLU A 1 432 ? 15.208  28.875  -3.684  1.00 29.33  ? 432  GLU A O     1 
ATOM   3337 C CB    . GLU A 1 432 ? 12.321  27.682  -2.776  1.00 31.26  ? 432  GLU A CB    1 
ATOM   3338 C CG    . GLU A 1 432 ? 12.407  27.424  -4.274  1.00 30.31  ? 432  GLU A CG    1 
ATOM   3339 C CD    . GLU A 1 432 ? 12.231  28.668  -5.131  1.00 32.66  ? 432  GLU A CD    1 
ATOM   3340 O OE1   . GLU A 1 432 ? 12.288  28.540  -6.360  1.00 33.99  ? 432  GLU A OE1   1 
ATOM   3341 O OE2   . GLU A 1 432 ? 12.047  29.772  -4.601  1.00 29.49  ? 432  GLU A OE2   1 
ATOM   3342 N N     . MET A 1 433 ? 15.397  26.935  -2.581  1.00 28.50  ? 433  MET A N     1 
ATOM   3343 C CA    . MET A 1 433 ? 16.601  26.562  -3.230  1.00 28.30  ? 433  MET A CA    1 
ATOM   3344 C C     . MET A 1 433 ? 16.461  25.266  -3.991  1.00 27.88  ? 433  MET A C     1 
ATOM   3345 O O     . MET A 1 433 ? 15.804  24.365  -3.555  1.00 24.35  ? 433  MET A O     1 
ATOM   3346 C CB    . MET A 1 433 ? 17.733  26.465  -2.221  1.00 28.89  ? 433  MET A CB    1 
ATOM   3347 C CG    . MET A 1 433 ? 19.131  26.311  -2.799  1.00 31.81  ? 433  MET A CG    1 
ATOM   3348 S SD    . MET A 1 433 ? 20.466  26.719  -1.659  1.00 30.22  ? 433  MET A SD    1 
ATOM   3349 C CE    . MET A 1 433 ? 20.281  25.425  -0.451  1.00 33.27  ? 433  MET A CE    1 
ATOM   3350 N N     . HIS A 1 434 ? 17.102  25.203  -5.133  1.00 25.98  ? 434  HIS A N     1 
ATOM   3351 C CA    . HIS A 1 434 ? 17.101  24.007  -5.919  1.00 26.71  ? 434  HIS A CA    1 
ATOM   3352 C C     . HIS A 1 434 ? 18.522  23.471  -6.012  1.00 26.19  ? 434  HIS A C     1 
ATOM   3353 O O     . HIS A 1 434 ? 19.441  24.223  -6.270  1.00 31.25  ? 434  HIS A O     1 
ATOM   3354 C CB    . HIS A 1 434 ? 16.610  24.314  -7.337  1.00 27.25  ? 434  HIS A CB    1 
ATOM   3355 C CG    . HIS A 1 434 ? 15.291  25.008  -7.409  1.00 28.72  ? 434  HIS A CG    1 
ATOM   3356 N ND1   . HIS A 1 434 ? 14.145  24.370  -7.825  1.00 27.88  ? 434  HIS A ND1   1 
ATOM   3357 C CD2   . HIS A 1 434 ? 14.938  26.291  -7.170  1.00 32.43  ? 434  HIS A CD2   1 
ATOM   3358 C CE1   . HIS A 1 434 ? 13.139  25.221  -7.810  1.00 28.84  ? 434  HIS A CE1   1 
ATOM   3359 N NE2   . HIS A 1 434 ? 13.594  26.393  -7.417  1.00 30.29  ? 434  HIS A NE2   1 
ATOM   3360 N N     . HIS A 1 435 ? 18.718  22.188  -5.793  1.00 24.93  ? 435  HIS A N     1 
ATOM   3361 C CA    . HIS A 1 435 ? 20.020  21.596  -6.003  1.00 24.29  ? 435  HIS A CA    1 
ATOM   3362 C C     . HIS A 1 435 ? 19.917  20.782  -7.266  1.00 25.87  ? 435  HIS A C     1 
ATOM   3363 O O     . HIS A 1 435 ? 19.460  19.674  -7.232  1.00 29.56  ? 435  HIS A O     1 
ATOM   3364 C CB    . HIS A 1 435 ? 20.425  20.711  -4.843  1.00 25.21  ? 435  HIS A CB    1 
ATOM   3365 C CG    . HIS A 1 435 ? 21.808  20.139  -4.948  1.00 22.97  ? 435  HIS A CG    1 
ATOM   3366 N ND1   . HIS A 1 435 ? 22.239  19.110  -4.157  1.00 24.18  ? 435  HIS A ND1   1 
ATOM   3367 C CD2   . HIS A 1 435 ? 22.848  20.468  -5.751  1.00 26.26  ? 435  HIS A CD2   1 
ATOM   3368 C CE1   . HIS A 1 435 ? 23.494  18.814  -4.464  1.00 25.51  ? 435  HIS A CE1   1 
ATOM   3369 N NE2   . HIS A 1 435 ? 23.879  19.621  -5.427  1.00 26.60  ? 435  HIS A NE2   1 
ATOM   3370 N N     . ILE A 1 436 ? 20.355  21.333  -8.377  1.00 26.95  ? 436  ILE A N     1 
ATOM   3371 C CA    . ILE A 1 436 ? 20.255  20.656  -9.658  1.00 28.91  ? 436  ILE A CA    1 
ATOM   3372 C C     . ILE A 1 436 ? 21.523  19.933  -10.082 1.00 28.16  ? 436  ILE A C     1 
ATOM   3373 O O     . ILE A 1 436 ? 22.472  20.549  -10.508 1.00 30.07  ? 436  ILE A O     1 
ATOM   3374 C CB    . ILE A 1 436 ? 19.762  21.591  -10.794 1.00 28.43  ? 436  ILE A CB    1 
ATOM   3375 C CG1   . ILE A 1 436 ? 18.558  22.403  -10.320 1.00 34.92  ? 436  ILE A CG1   1 
ATOM   3376 C CG2   . ILE A 1 436 ? 19.423  20.801  -12.043 1.00 27.12  ? 436  ILE A CG2   1 
ATOM   3377 C CD1   . ILE A 1 436 ? 18.253  23.607  -11.170 1.00 33.61  ? 436  ILE A CD1   1 
ATOM   3378 N N     . ALA A 1 437 ? 21.507  18.628  -9.975  1.00 28.31  ? 437  ALA A N     1 
ATOM   3379 C CA    . ALA A 1 437 ? 22.631  17.831  -10.380 1.00 28.90  ? 437  ALA A CA    1 
ATOM   3380 C C     . ALA A 1 437 ? 22.392  17.146  -11.688 1.00 32.32  ? 437  ALA A C     1 
ATOM   3381 O O     . ALA A 1 437 ? 21.353  16.550  -11.898 1.00 36.13  ? 437  ALA A O     1 
ATOM   3382 C CB    . ALA A 1 437 ? 22.962  16.810  -9.330  1.00 30.34  ? 437  ALA A CB    1 
ATOM   3383 N N     . LEU A 1 438 ? 23.359  17.240  -12.570 1.00 33.06  ? 438  LEU A N     1 
ATOM   3384 C CA    . LEU A 1 438 ? 23.271  16.592  -13.852 1.00 36.28  ? 438  LEU A CA    1 
ATOM   3385 C C     . LEU A 1 438 ? 24.073  15.336  -13.724 1.00 35.27  ? 438  LEU A C     1 
ATOM   3386 O O     . LEU A 1 438 ? 25.282  15.382  -13.624 1.00 29.30  ? 438  LEU A O     1 
ATOM   3387 C CB    . LEU A 1 438 ? 23.812  17.471  -14.950 1.00 39.73  ? 438  LEU A CB    1 
ATOM   3388 C CG    . LEU A 1 438 ? 22.815  18.373  -15.663 1.00 51.74  ? 438  LEU A CG    1 
ATOM   3389 C CD1   . LEU A 1 438 ? 21.947  19.177  -14.715 1.00 53.32  ? 438  LEU A CD1   1 
ATOM   3390 C CD2   . LEU A 1 438 ? 23.474  19.278  -16.674 1.00 53.18  ? 438  LEU A CD2   1 
ATOM   3391 N N     . LEU A 1 439 ? 23.380  14.213  -13.686 1.00 36.06  ? 439  LEU A N     1 
ATOM   3392 C CA    . LEU A 1 439 ? 24.034  12.936  -13.524 1.00 37.50  ? 439  LEU A CA    1 
ATOM   3393 C C     . LEU A 1 439 ? 24.406  12.371  -14.875 1.00 41.10  ? 439  LEU A C     1 
ATOM   3394 O O     . LEU A 1 439 ? 23.552  11.883  -15.591 1.00 35.62  ? 439  LEU A O     1 
ATOM   3395 C CB    . LEU A 1 439 ? 23.134  12.010  -12.732 1.00 39.99  ? 439  LEU A CB    1 
ATOM   3396 C CG    . LEU A 1 439 ? 22.689  12.638  -11.413 1.00 40.58  ? 439  LEU A CG    1 
ATOM   3397 C CD1   . LEU A 1 439 ? 21.514  11.911  -10.808 1.00 45.38  ? 439  LEU A CD1   1 
ATOM   3398 C CD2   . LEU A 1 439 ? 23.833  12.691  -10.422 1.00 43.97  ? 439  LEU A CD2   1 
ATOM   3399 N N     . LEU A 1 440 ? 25.679  12.437  -15.221 1.00 35.95  ? 440  LEU A N     1 
ATOM   3400 C CA    . LEU A 1 440 ? 26.131  12.033  -16.541 1.00 38.05  ? 440  LEU A CA    1 
ATOM   3401 C C     . LEU A 1 440 ? 26.573  10.589  -16.636 1.00 36.52  ? 440  LEU A C     1 
ATOM   3402 O O     . LEU A 1 440 ? 27.222  10.085  -15.745 1.00 37.55  ? 440  LEU A O     1 
ATOM   3403 C CB    . LEU A 1 440 ? 27.229  12.985  -17.025 1.00 39.35  ? 440  LEU A CB    1 
ATOM   3404 C CG    . LEU A 1 440 ? 26.955  14.260  -17.829 1.00 47.70  ? 440  LEU A CG    1 
ATOM   3405 C CD1   . LEU A 1 440 ? 25.680  14.966  -17.433 1.00 51.21  ? 440  LEU A CD1   1 
ATOM   3406 C CD2   . LEU A 1 440 ? 28.114  15.229  -17.692 1.00 48.01  ? 440  LEU A CD2   1 
ATOM   3407 N N     . PHE A 1 441 ? 26.254  9.943   -17.740 1.00 33.93  ? 441  PHE A N     1 
ATOM   3408 C CA    . PHE A 1 441 ? 26.550  8.536   -17.891 1.00 31.58  ? 441  PHE A CA    1 
ATOM   3409 C C     . PHE A 1 441 ? 26.621  8.055   -19.321 1.00 35.94  ? 441  PHE A C     1 
ATOM   3410 O O     . PHE A 1 441 ? 26.041  8.651   -20.196 1.00 39.42  ? 441  PHE A O     1 
ATOM   3411 C CB    . PHE A 1 441 ? 25.514  7.687   -17.152 1.00 33.84  ? 441  PHE A CB    1 
ATOM   3412 C CG    . PHE A 1 441 ? 24.117  7.793   -17.698 1.00 32.73  ? 441  PHE A CG    1 
ATOM   3413 C CD1   . PHE A 1 441 ? 23.301  8.859   -17.368 1.00 32.37  ? 441  PHE A CD1   1 
ATOM   3414 C CD2   . PHE A 1 441 ? 23.608  6.807   -18.515 1.00 36.69  ? 441  PHE A CD2   1 
ATOM   3415 C CE1   . PHE A 1 441 ? 22.023  8.956   -17.864 1.00 30.11  ? 441  PHE A CE1   1 
ATOM   3416 C CE2   . PHE A 1 441 ? 22.334  6.902   -19.016 1.00 33.85  ? 441  PHE A CE2   1 
ATOM   3417 C CZ    . PHE A 1 441 ? 21.541  7.977   -18.693 1.00 31.28  ? 441  PHE A CZ    1 
ATOM   3418 N N     . ASP A 1 442 ? 27.325  6.968   -19.549 1.00 36.43  ? 442  ASP A N     1 
ATOM   3419 C CA    . ASP A 1 442 ? 27.426  6.339   -20.886 1.00 34.86  ? 442  ASP A CA    1 
ATOM   3420 C C     . ASP A 1 442 ? 26.091  5.637   -21.183 1.00 34.69  ? 442  ASP A C     1 
ATOM   3421 O O     . ASP A 1 442 ? 25.835  4.567   -20.586 1.00 35.13  ? 442  ASP A O     1 
ATOM   3422 C CB    . ASP A 1 442 ? 28.619  5.383   -20.907 1.00 35.11  ? 442  ASP A CB    1 
ATOM   3423 C CG    . ASP A 1 442 ? 28.893  4.839   -22.290 1.00 37.97  ? 442  ASP A CG    1 
ATOM   3424 O OD1   . ASP A 1 442 ? 28.109  5.147   -23.217 1.00 38.97  ? 442  ASP A OD1   1 
ATOM   3425 O OD2   . ASP A 1 442 ? 29.875  4.128   -22.420 1.00 43.11  ? 442  ASP A OD2   1 
ATOM   3426 N N     . THR A 1 443 ? 25.265  6.201   -22.068 1.00 34.61  ? 443  THR A N     1 
ATOM   3427 C CA    . THR A 1 443 ? 23.907  5.671   -22.373 1.00 38.40  ? 443  THR A CA    1 
ATOM   3428 C C     . THR A 1 443 ? 24.024  4.293   -23.026 1.00 36.91  ? 443  THR A C     1 
ATOM   3429 O O     . THR A 1 443 ? 23.043  3.546   -22.984 1.00 36.63  ? 443  THR A O     1 
ATOM   3430 C CB    . THR A 1 443 ? 23.136  6.597   -23.317 1.00 42.42  ? 443  THR A CB    1 
ATOM   3431 O OG1   . THR A 1 443 ? 23.977  6.857   -24.447 1.00 40.12  ? 443  THR A OG1   1 
ATOM   3432 C CG2   . THR A 1 443 ? 22.723  7.892   -22.654 1.00 44.41  ? 443  THR A CG2   1 
ATOM   3433 N N     . GLN A 1 444 ? 25.185  4.022   -23.639 1.00 40.62  ? 444  GLN A N     1 
ATOM   3434 C CA    . GLN A 1 444 ? 25.483  2.808   -24.436 1.00 40.14  ? 444  GLN A CA    1 
ATOM   3435 C C     . GLN A 1 444 ? 26.037  1.702   -23.531 1.00 40.70  ? 444  GLN A C     1 
ATOM   3436 O O     . GLN A 1 444 ? 26.360  0.641   -24.058 1.00 40.60  ? 444  GLN A O     1 
ATOM   3437 C CB    . GLN A 1 444 ? 26.477  3.159   -25.550 1.00 43.03  ? 444  GLN A CB    1 
ATOM   3438 C CG    . GLN A 1 444 ? 26.001  4.258   -26.502 1.00 43.59  ? 444  GLN A CG    1 
ATOM   3439 C CD    . GLN A 1 444 ? 24.571  4.071   -26.944 1.00 48.83  ? 444  GLN A CD    1 
ATOM   3440 O OE1   . GLN A 1 444 ? 24.182  3.015   -27.445 1.00 52.48  ? 444  GLN A OE1   1 
ATOM   3441 N NE2   . GLN A 1 444 ? 23.757  5.093   -26.737 1.00 51.17  ? 444  GLN A NE2   1 
ATOM   3442 N N     . ASP A 1 445 ? 26.139  1.936   -22.222 1.00 38.14  ? 445  ASP A N     1 
ATOM   3443 C CA    . ASP A 1 445 ? 26.724  0.977   -21.257 1.00 37.61  ? 445  ASP A CA    1 
ATOM   3444 C C     . ASP A 1 445 ? 25.643  0.621   -20.242 1.00 38.15  ? 445  ASP A C     1 
ATOM   3445 O O     . ASP A 1 445 ? 25.332  1.486   -19.399 1.00 36.16  ? 445  ASP A O     1 
ATOM   3446 C CB    . ASP A 1 445 ? 27.949  1.593   -20.588 1.00 39.32  ? 445  ASP A CB    1 
ATOM   3447 C CG    . ASP A 1 445 ? 28.619  0.693   -19.577 1.00 40.55  ? 445  ASP A CG    1 
ATOM   3448 O OD1   . ASP A 1 445 ? 27.923  0.169   -18.703 1.00 42.40  ? 445  ASP A OD1   1 
ATOM   3449 O OD2   . ASP A 1 445 ? 29.826  0.525   -19.679 1.00 48.62  ? 445  ASP A OD2   1 
ATOM   3450 N N     . ALA A 1 446 ? 25.075  -0.584  -20.355 1.00 32.62  ? 446  ALA A N     1 
ATOM   3451 C CA    . ALA A 1 446 ? 23.972  -1.093  -19.524 1.00 34.89  ? 446  ALA A CA    1 
ATOM   3452 C C     . ALA A 1 446 ? 24.306  -0.907  -18.040 1.00 34.95  ? 446  ALA A C     1 
ATOM   3453 O O     . ALA A 1 446 ? 23.384  -0.596  -17.255 1.00 35.02  ? 446  ALA A O     1 
ATOM   3454 C CB    . ALA A 1 446 ? 23.695  -2.544  -19.856 1.00 35.32  ? 446  ALA A CB    1 
ATOM   3455 N N     . THR A 1 447 ? 25.550  -1.165  -17.640 1.00 34.65  ? 447  THR A N     1 
ATOM   3456 C CA    . THR A 1 447 ? 25.971  -1.074  -16.214 1.00 37.53  ? 447  THR A CA    1 
ATOM   3457 C C     . THR A 1 447 ? 25.852  0.380   -15.738 1.00 37.10  ? 447  THR A C     1 
ATOM   3458 O O     . THR A 1 447 ? 25.336  0.569   -14.629 1.00 37.96  ? 447  THR A O     1 
ATOM   3459 C CB    . THR A 1 447 ? 27.372  -1.645  -15.962 1.00 35.71  ? 447  THR A CB    1 
ATOM   3460 O OG1   . THR A 1 447 ? 27.263  -3.065  -16.023 1.00 38.23  ? 447  THR A OG1   1 
ATOM   3461 C CG2   . THR A 1 447 ? 27.943  -1.258  -14.619 1.00 36.91  ? 447  THR A CG2   1 
ATOM   3462 N N     . ALA A 1 448 ? 26.339  1.333   -16.535 1.00 34.38  ? 448  ALA A N     1 
ATOM   3463 C CA    . ALA A 1 448 ? 26.302  2.788   -16.257 1.00 36.07  ? 448  ALA A CA    1 
ATOM   3464 C C     . ALA A 1 448 ? 24.839  3.245   -16.131 1.00 35.48  ? 448  ALA A C     1 
ATOM   3465 O O     . ALA A 1 448 ? 24.535  3.958   -15.173 1.00 33.40  ? 448  ALA A O     1 
ATOM   3466 C CB    . ALA A 1 448 ? 27.050  3.537   -17.327 1.00 36.65  ? 448  ALA A CB    1 
ATOM   3467 N N     . ARG A 1 449 ? 23.959  2.775   -17.018 1.00 32.45  ? 449  ARG A N     1 
ATOM   3468 C CA    . ARG A 1 449 ? 22.509  3.080   -16.985 1.00 34.17  ? 449  ARG A CA    1 
ATOM   3469 C C     . ARG A 1 449 ? 21.963  2.635   -15.630 1.00 35.14  ? 449  ARG A C     1 
ATOM   3470 O O     . ARG A 1 449 ? 21.286  3.443   -14.962 1.00 35.18  ? 449  ARG A O     1 
ATOM   3471 C CB    . ARG A 1 449 ? 21.766  2.401   -18.148 1.00 32.92  ? 449  ARG A CB    1 
ATOM   3472 C CG    . ARG A 1 449 ? 22.099  2.978   -19.511 1.00 32.76  ? 449  ARG A CG    1 
ATOM   3473 C CD    . ARG A 1 449 ? 21.052  2.607   -20.546 1.00 35.50  ? 449  ARG A CD    1 
ATOM   3474 N NE    . ARG A 1 449 ? 20.938  1.170   -20.776 1.00 38.94  ? 449  ARG A NE    1 
ATOM   3475 C CZ    . ARG A 1 449 ? 21.658  0.476   -21.644 1.00 38.57  ? 449  ARG A CZ    1 
ATOM   3476 N NH1   . ARG A 1 449 ? 22.596  1.056   -22.375 1.00 40.29  ? 449  ARG A NH1   1 
ATOM   3477 N NH2   . ARG A 1 449 ? 21.458  -0.819  -21.743 1.00 45.45  ? 449  ARG A NH2   1 
ATOM   3478 N N     . ASN A 1 450 ? 22.311  1.417   -15.213 1.00 36.15  ? 450  ASN A N     1 
ATOM   3479 C CA    . ASN A 1 450 ? 21.783  0.772   -13.986 1.00 33.29  ? 450  ASN A CA    1 
ATOM   3480 C C     . ASN A 1 450 ? 22.272  1.513   -12.732 1.00 30.45  ? 450  ASN A C     1 
ATOM   3481 O O     . ASN A 1 450 ? 21.458  1.662   -11.772 1.00 31.52  ? 450  ASN A O     1 
ATOM   3482 C CB    . ASN A 1 450 ? 22.180  -0.700  -13.925 1.00 35.66  ? 450  ASN A CB    1 
ATOM   3483 C CG    . ASN A 1 450 ? 21.533  -1.554  -14.993 1.00 40.36  ? 450  ASN A CG    1 
ATOM   3484 O OD1   . ASN A 1 450 ? 20.663  -1.083  -15.729 1.00 38.92  ? 450  ASN A OD1   1 
ATOM   3485 N ND2   . ASN A 1 450 ? 21.983  -2.806  -15.091 1.00 35.55  ? 450  ASN A ND2   1 
ATOM   3486 N N     . GLU A 1 451 ? 23.547  1.895   -12.717 1.00 31.14  ? 451  GLU A N     1 
ATOM   3487 C CA    . GLU A 1 451 ? 24.195  2.687   -11.640 1.00 31.41  ? 451  GLU A CA    1 
ATOM   3488 C C     . GLU A 1 451 ? 23.478  4.032   -11.516 1.00 30.18  ? 451  GLU A C     1 
ATOM   3489 O O     . GLU A 1 451 ? 23.255  4.486   -10.382 1.00 27.85  ? 451  GLU A O     1 
ATOM   3490 C CB    . GLU A 1 451 ? 25.652  2.984   -11.989 1.00 35.46  ? 451  GLU A CB    1 
ATOM   3491 C CG    . GLU A 1 451 ? 26.580  1.803   -11.822 1.00 39.27  ? 451  GLU A CG    1 
ATOM   3492 C CD    . GLU A 1 451 ? 27.997  2.043   -12.307 1.00 38.71  ? 451  GLU A CD    1 
ATOM   3493 O OE1   . GLU A 1 451 ? 28.172  2.775   -13.305 1.00 40.44  ? 451  GLU A OE1   1 
ATOM   3494 O OE2   . GLU A 1 451 ? 28.933  1.522   -11.647 1.00 46.05  ? 451  GLU A OE2   1 
ATOM   3495 N N     . THR A 1 452 ? 23.180  4.677   -12.649 1.00 28.48  ? 452  THR A N     1 
ATOM   3496 C CA    . THR A 1 452 ? 22.562  6.033   -12.670 1.00 27.54  ? 452  THR A CA    1 
ATOM   3497 C C     . THR A 1 452 ? 21.178  5.906   -12.047 1.00 28.16  ? 452  THR A C     1 
ATOM   3498 O O     . THR A 1 452 ? 20.819  6.731   -11.177 1.00 34.02  ? 452  THR A O     1 
ATOM   3499 C CB    . THR A 1 452 ? 22.534  6.625   -14.082 1.00 29.02  ? 452  THR A CB    1 
ATOM   3500 O OG1   . THR A 1 452 ? 23.880  6.657   -14.538 1.00 27.98  ? 452  THR A OG1   1 
ATOM   3501 C CG2   . THR A 1 452 ? 21.970  8.030   -14.131 1.00 30.65  ? 452  THR A CG2   1 
ATOM   3502 N N     . LEU A 1 453 ? 20.451  4.859   -12.407 1.00 27.53  ? 453  LEU A N     1 
ATOM   3503 C CA    . LEU A 1 453 ? 19.089  4.651   -11.869 1.00 29.43  ? 453  LEU A CA    1 
ATOM   3504 C C     . LEU A 1 453 ? 19.190  4.369   -10.367 1.00 30.88  ? 453  LEU A C     1 
ATOM   3505 O O     . LEU A 1 453 ? 18.358  4.919   -9.614  1.00 26.71  ? 453  LEU A O     1 
ATOM   3506 C CB    . LEU A 1 453 ? 18.411  3.495   -12.596 1.00 29.11  ? 453  LEU A CB    1 
ATOM   3507 C CG    . LEU A 1 453 ? 16.995  3.178   -12.128 1.00 32.89  ? 453  LEU A CG    1 
ATOM   3508 C CD1   . LEU A 1 453 ? 16.129  4.424   -12.106 1.00 35.61  ? 453  LEU A CD1   1 
ATOM   3509 C CD2   . LEU A 1 453 ? 16.370  2.115   -13.006 1.00 34.39  ? 453  LEU A CD2   1 
ATOM   3510 N N     . ALA A 1 454 ? 20.132  3.501   -9.973  1.00 27.61  ? 454  ALA A N     1 
ATOM   3511 C CA    . ALA A 1 454 ? 20.341  3.105   -8.567  1.00 31.67  ? 454  ALA A CA    1 
ATOM   3512 C C     . ALA A 1 454 ? 20.703  4.370   -7.799  1.00 27.55  ? 454  ALA A C     1 
ATOM   3513 O O     . ALA A 1 454 ? 20.074  4.623   -6.789  1.00 28.98  ? 454  ALA A O     1 
ATOM   3514 C CB    . ALA A 1 454 ? 21.403  2.032   -8.456  1.00 30.64  ? 454  ALA A CB    1 
ATOM   3515 N N     . LEU A 1 455 ? 21.680  5.133   -8.292  1.00 29.86  ? 455  LEU A N     1 
ATOM   3516 C CA    . LEU A 1 455 ? 22.131  6.378   -7.646  1.00 28.98  ? 455  LEU A CA    1 
ATOM   3517 C C     . LEU A 1 455 ? 20.932  7.335   -7.464  1.00 29.83  ? 455  LEU A C     1 
ATOM   3518 O O     . LEU A 1 455 ? 20.779  7.926   -6.357  1.00 26.61  ? 455  LEU A O     1 
ATOM   3519 C CB    . LEU A 1 455 ? 23.219  7.054   -8.479  1.00 29.20  ? 455  LEU A CB    1 
ATOM   3520 C CG    . LEU A 1 455 ? 23.588  8.451   -7.968  1.00 27.18  ? 455  LEU A CG    1 
ATOM   3521 C CD1   . LEU A 1 455 ? 24.125  8.364   -6.540  1.00 26.89  ? 455  LEU A CD1   1 
ATOM   3522 C CD2   . LEU A 1 455 ? 24.565  9.140   -8.900  1.00 28.59  ? 455  LEU A CD2   1 
ATOM   3523 N N     . THR A 1 456 ? 20.143  7.553   -8.515  1.00 28.36  ? 456  THR A N     1 
ATOM   3524 C CA    . THR A 1 456 ? 19.059  8.559   -8.487  1.00 29.71  ? 456  THR A CA    1 
ATOM   3525 C C     . THR A 1 456 ? 18.025  8.137   -7.449  1.00 28.24  ? 456  THR A C     1 
ATOM   3526 O O     . THR A 1 456 ? 17.596  8.999   -6.698  1.00 27.97  ? 456  THR A O     1 
ATOM   3527 C CB    . THR A 1 456 ? 18.492  8.871   -9.875  1.00 29.60  ? 456  THR A CB    1 
ATOM   3528 O OG1   . THR A 1 456 ? 19.594  9.210   -10.715 1.00 30.53  ? 456  THR A OG1   1 
ATOM   3529 C CG2   . THR A 1 456 ? 17.572  10.066  -9.833  1.00 33.41  ? 456  THR A CG2   1 
ATOM   3530 N N     . ARG A 1 457 ? 17.662  6.865   -7.400  1.00 27.17  ? 457  ARG A N     1 
ATOM   3531 C CA    . ARG A 1 457 ? 16.663  6.348   -6.435  1.00 29.10  ? 457  ARG A CA    1 
ATOM   3532 C C     . ARG A 1 457 ? 17.166  6.596   -5.014  1.00 29.19  ? 457  ARG A C     1 
ATOM   3533 O O     . ARG A 1 457 ? 16.336  6.892   -4.141  1.00 24.10  ? 457  ARG A O     1 
ATOM   3534 C CB    . ARG A 1 457 ? 16.395  4.847   -6.616  1.00 28.41  ? 457  ARG A CB    1 
ATOM   3535 C CG    . ARG A 1 457 ? 15.602  4.509   -7.871  1.00 29.71  ? 457  ARG A CG    1 
ATOM   3536 C CD    . ARG A 1 457 ? 14.710  3.309   -7.610  1.00 31.17  ? 457  ARG A CD    1 
ATOM   3537 N NE    . ARG A 1 457 ? 14.139  2.833   -8.849  1.00 30.28  ? 457  ARG A NE    1 
ATOM   3538 C CZ    . ARG A 1 457 ? 13.128  3.406   -9.486  1.00 29.88  ? 457  ARG A CZ    1 
ATOM   3539 N NH1   . ARG A 1 457 ? 12.561  4.486   -8.985  1.00 29.87  ? 457  ARG A NH1   1 
ATOM   3540 N NH2   . ARG A 1 457 ? 12.686  2.900   -10.626 1.00 31.33  ? 457  ARG A NH2   1 
ATOM   3541 N N     . LEU A 1 458 ? 18.475  6.416   -4.801  1.00 30.30  ? 458  LEU A N     1 
ATOM   3542 C CA    . LEU A 1 458 ? 19.093  6.594   -3.460  1.00 29.79  ? 458  LEU A CA    1 
ATOM   3543 C C     . LEU A 1 458 ? 19.067  8.095   -3.122  1.00 26.06  ? 458  LEU A C     1 
ATOM   3544 O O     . LEU A 1 458 ? 18.660  8.437   -2.009  1.00 26.57  ? 458  LEU A O     1 
ATOM   3545 C CB    . LEU A 1 458 ? 20.511  6.014   -3.468  1.00 29.58  ? 458  LEU A CB    1 
ATOM   3546 C CG    . LEU A 1 458 ? 21.271  6.114   -2.139  1.00 29.76  ? 458  LEU A CG    1 
ATOM   3547 C CD1   . LEU A 1 458 ? 20.480  5.522   -0.987  1.00 30.48  ? 458  LEU A CD1   1 
ATOM   3548 C CD2   . LEU A 1 458 ? 22.610  5.420   -2.265  1.00 33.96  ? 458  LEU A CD2   1 
ATOM   3549 N N     . LEU A 1 459 ? 19.448  8.943   -4.076  1.00 26.63  ? 459  LEU A N     1 
ATOM   3550 C CA    . LEU A 1 459 ? 19.523  10.424  -3.916  1.00 27.72  ? 459  LEU A CA    1 
ATOM   3551 C C     . LEU A 1 459 ? 18.156  10.963  -3.525  1.00 26.00  ? 459  LEU A C     1 
ATOM   3552 O O     . LEU A 1 459 ? 18.115  11.833  -2.663  1.00 28.14  ? 459  LEU A O     1 
ATOM   3553 C CB    . LEU A 1 459 ? 20.001  11.081  -5.212  1.00 28.97  ? 459  LEU A CB    1 
ATOM   3554 C CG    . LEU A 1 459 ? 21.473  10.892  -5.544  1.00 28.30  ? 459  LEU A CG    1 
ATOM   3555 C CD1   . LEU A 1 459 ? 21.801  11.661  -6.803  1.00 29.38  ? 459  LEU A CD1   1 
ATOM   3556 C CD2   . LEU A 1 459 ? 22.381  11.331  -4.384  1.00 25.83  ? 459  LEU A CD2   1 
ATOM   3557 N N     . ILE A 1 460 ? 17.100  10.436  -4.145  1.00 25.41  ? 460  ILE A N     1 
ATOM   3558 C CA    . ILE A 1 460 ? 15.685  10.827  -3.888  1.00 26.22  ? 460  ILE A CA    1 
ATOM   3559 C C     . ILE A 1 460 ? 15.256  10.370  -2.489  1.00 26.34  ? 460  ILE A C     1 
ATOM   3560 O O     . ILE A 1 460 ? 14.637  11.151  -1.787  1.00 26.28  ? 460  ILE A O     1 
ATOM   3561 C CB    . ILE A 1 460 ? 14.762  10.255  -4.973  1.00 26.71  ? 460  ILE A CB    1 
ATOM   3562 C CG1   . ILE A 1 460 ? 14.956  11.008  -6.291  1.00 27.91  ? 460  ILE A CG1   1 
ATOM   3563 C CG2   . ILE A 1 460 ? 13.316  10.262  -4.491  1.00 26.95  ? 460  ILE A CG2   1 
ATOM   3564 C CD1   . ILE A 1 460 ? 14.310  10.318  -7.493  1.00 30.95  ? 460  ILE A CD1   1 
ATOM   3565 N N     . ASP A 1 461 ? 15.502  9.128   -2.111  1.00 26.81  ? 461  ASP A N     1 
ATOM   3566 C CA    . ASP A 1 461 ? 15.112  8.648   -0.756  1.00 28.04  ? 461  ASP A CA    1 
ATOM   3567 C C     . ASP A 1 461 ? 15.828  9.452   0.331   1.00 25.59  ? 461  ASP A C     1 
ATOM   3568 O O     . ASP A 1 461 ? 15.153  9.852   1.288   1.00 29.77  ? 461  ASP A O     1 
ATOM   3569 C CB    . ASP A 1 461 ? 15.332  7.143   -0.595  1.00 30.75  ? 461  ASP A CB    1 
ATOM   3570 C CG    . ASP A 1 461 ? 14.257  6.329   -1.306  1.00 33.48  ? 461  ASP A CG    1 
ATOM   3571 O OD1   . ASP A 1 461 ? 13.197  6.910   -1.623  1.00 33.59  ? 461  ASP A OD1   1 
ATOM   3572 O OD2   . ASP A 1 461 ? 14.501  5.126   -1.554  1.00 35.11  ? 461  ASP A OD2   1 
ATOM   3573 N N     . GLU A 1 462 ? 17.129  9.672   0.193   1.00 27.61  ? 462  GLU A N     1 
ATOM   3574 C CA    . GLU A 1 462 ? 17.979  10.328  1.233   1.00 31.31  ? 462  GLU A CA    1 
ATOM   3575 C C     . GLU A 1 462 ? 17.630  11.817  1.313   1.00 29.18  ? 462  GLU A C     1 
ATOM   3576 O O     . GLU A 1 462 ? 17.447  12.320  2.423   1.00 26.68  ? 462  GLU A O     1 
ATOM   3577 C CB    . GLU A 1 462 ? 19.470  10.103  0.946   1.00 29.86  ? 462  GLU A CB    1 
ATOM   3578 C CG    . GLU A 1 462 ? 19.852  8.660   1.154   1.00 30.20  ? 462  GLU A CG    1 
ATOM   3579 C CD    . GLU A 1 462 ? 21.335  8.352   1.285   1.00 35.21  ? 462  GLU A CD    1 
ATOM   3580 O OE1   . GLU A 1 462 ? 22.183  9.038   0.648   1.00 29.89  ? 462  GLU A OE1   1 
ATOM   3581 O OE2   . GLU A 1 462 ? 21.630  7.394   2.027   1.00 39.01  ? 462  GLU A OE2   1 
ATOM   3582 N N     . ALA A 1 463 ? 17.497  12.487  0.173   1.00 26.84  ? 463  ALA A N     1 
ATOM   3583 C CA    . ALA A 1 463 ? 16.998  13.881  0.106   1.00 25.80  ? 463  ALA A CA    1 
ATOM   3584 C C     . ALA A 1 463 ? 15.646  13.958  0.821   1.00 24.10  ? 463  ALA A C     1 
ATOM   3585 O O     . ALA A 1 463 ? 15.438  14.853  1.692   1.00 28.21  ? 463  ALA A O     1 
ATOM   3586 C CB    . ALA A 1 463 ? 16.911  14.321  -1.338  1.00 25.63  ? 463  ALA A CB    1 
ATOM   3587 N N     . ALA A 1 464 ? 14.747  13.042  0.522   1.00 23.07  ? 464  ALA A N     1 
ATOM   3588 C CA    . ALA A 1 464 ? 13.376  13.049  1.074   1.00 23.88  ? 464  ALA A CA    1 
ATOM   3589 C C     . ALA A 1 464 ? 13.422  12.828  2.588   1.00 25.21  ? 464  ALA A C     1 
ATOM   3590 O O     . ALA A 1 464 ? 12.681  13.548  3.300   1.00 23.19  ? 464  ALA A O     1 
ATOM   3591 C CB    . ALA A 1 464 ? 12.509  12.003  0.411   1.00 23.40  ? 464  ALA A CB    1 
ATOM   3592 N N     . ALA A 1 465 ? 14.246  11.885  3.075   1.00 25.85  ? 465  ALA A N     1 
ATOM   3593 C CA    . ALA A 1 465 ? 14.413  11.657  4.529   1.00 24.82  ? 465  ALA A CA    1 
ATOM   3594 C C     . ALA A 1 465 ? 14.876  12.970  5.194   1.00 24.60  ? 465  ALA A C     1 
ATOM   3595 O O     . ALA A 1 465 ? 14.449  13.245  6.314   1.00 25.49  ? 465  ALA A O     1 
ATOM   3596 C CB    . ALA A 1 465 ? 15.327  10.465  4.774   1.00 25.28  ? 465  ALA A CB    1 
ATOM   3597 N N     . GLU A 1 466 ? 15.603  13.837  4.488   1.00 24.51  ? 466  GLU A N     1 
ATOM   3598 C CA    . GLU A 1 466 ? 16.089  15.124  5.052   1.00 26.09  ? 466  GLU A CA    1 
ATOM   3599 C C     . GLU A 1 466 ? 15.050  16.248  4.905   1.00 27.45  ? 466  GLU A C     1 
ATOM   3600 O O     . GLU A 1 466 ? 15.295  17.314  5.453   1.00 28.75  ? 466  GLU A O     1 
ATOM   3601 C CB    . GLU A 1 466 ? 17.402  15.543  4.413   1.00 25.66  ? 466  GLU A CB    1 
ATOM   3602 C CG    . GLU A 1 466 ? 18.549  14.659  4.821   1.00 29.13  ? 466  GLU A CG    1 
ATOM   3603 C CD    . GLU A 1 466 ? 18.789  14.633  6.328   1.00 30.58  ? 466  GLU A CD    1 
ATOM   3604 O OE1   . GLU A 1 466 ? 18.454  15.620  7.000   1.00 28.55  ? 466  GLU A OE1   1 
ATOM   3605 O OE2   . GLU A 1 466 ? 19.276  13.619  6.820   1.00 34.80  ? 466  GLU A OE2   1 
ATOM   3606 N N     . GLY A 1 467 ? 13.903  16.000  4.277   1.00 25.63  ? 467  GLY A N     1 
ATOM   3607 C CA    . GLY A 1 467 ? 12.864  17.026  4.074   1.00 27.76  ? 467  GLY A CA    1 
ATOM   3608 C C     . GLY A 1 467 ? 12.996  17.749  2.742   1.00 27.26  ? 467  GLY A C     1 
ATOM   3609 O O     . GLY A 1 467 ? 12.403  18.836  2.608   1.00 28.75  ? 467  GLY A O     1 
ATOM   3610 N N     . TYR A 1 468 ? 13.731  17.184  1.782   1.00 24.13  ? 468  TYR A N     1 
ATOM   3611 C CA    . TYR A 1 468 ? 13.997  17.825  0.472   1.00 25.10  ? 468  TYR A CA    1 
ATOM   3612 C C     . TYR A 1 468 ? 13.304  17.016  -0.618  1.00 24.73  ? 468  TYR A C     1 
ATOM   3613 O O     . TYR A 1 468 ? 13.803  15.932  -0.941  1.00 24.81  ? 468  TYR A O     1 
ATOM   3614 C CB    . TYR A 1 468 ? 15.493  17.890  0.156   1.00 25.91  ? 468  TYR A CB    1 
ATOM   3615 C CG    . TYR A 1 468 ? 16.354  18.515  1.223   1.00 29.16  ? 468  TYR A CG    1 
ATOM   3616 C CD1   . TYR A 1 468 ? 15.938  19.620  1.962   1.00 28.61  ? 468  TYR A CD1   1 
ATOM   3617 C CD2   . TYR A 1 468 ? 17.606  17.995  1.484   1.00 30.97  ? 468  TYR A CD2   1 
ATOM   3618 C CE1   . TYR A 1 468 ? 16.744  20.178  2.940   1.00 30.07  ? 468  TYR A CE1   1 
ATOM   3619 C CE2   . TYR A 1 468 ? 18.426  18.548  2.448   1.00 35.12  ? 468  TYR A CE2   1 
ATOM   3620 C CZ    . TYR A 1 468 ? 17.999  19.651  3.173   1.00 35.03  ? 468  TYR A CZ    1 
ATOM   3621 O OH    . TYR A 1 468 ? 18.856  20.197  4.083   1.00 32.36  ? 468  TYR A OH    1 
ATOM   3622 N N     . GLY A 1 469 ? 12.195  17.533  -1.151  1.00 23.97  ? 469  GLY A N     1 
ATOM   3623 C CA    . GLY A 1 469 ? 11.324  16.844  -2.121  1.00 24.49  ? 469  GLY A CA    1 
ATOM   3624 C C     . GLY A 1 469 ? 11.754  17.083  -3.552  1.00 23.47  ? 469  GLY A C     1 
ATOM   3625 O O     . GLY A 1 469 ? 12.213  18.180  -3.847  1.00 25.77  ? 469  GLY A O     1 
ATOM   3626 N N     . GLU A 1 470 ? 11.671  16.063  -4.402  1.00 24.20  ? 470  GLU A N     1 
ATOM   3627 C CA    . GLU A 1 470 ? 12.009  16.234  -5.841  1.00 26.27  ? 470  GLU A CA    1 
ATOM   3628 C C     . GLU A 1 470 ? 10.867  17.018  -6.525  1.00 27.33  ? 470  GLU A C     1 
ATOM   3629 O O     . GLU A 1 470 ? 9.654   16.847  -6.151  1.00 23.98  ? 470  GLU A O     1 
ATOM   3630 C CB    . GLU A 1 470 ? 12.305  14.894  -6.515  1.00 27.29  ? 470  GLU A CB    1 
ATOM   3631 C CG    . GLU A 1 470 ? 12.543  15.032  -8.013  1.00 27.99  ? 470  GLU A CG    1 
ATOM   3632 C CD    . GLU A 1 470 ? 13.724  15.908  -8.394  1.00 30.16  ? 470  GLU A CD    1 
ATOM   3633 O OE1   . GLU A 1 470 ? 14.833  15.341  -8.569  1.00 28.65  ? 470  GLU A OE1   1 
ATOM   3634 O OE2   . GLU A 1 470 ? 13.552  17.166  -8.493  1.00 31.56  ? 470  GLU A OE2   1 
ATOM   3635 N N     . TYR A 1 471 ? 11.258  17.912  -7.429  1.00 25.36  ? 471  TYR A N     1 
ATOM   3636 C CA    . TYR A 1 471 ? 10.385  18.897  -8.096  1.00 29.87  ? 471  TYR A CA    1 
ATOM   3637 C C     . TYR A 1 471 ? 9.937   18.380  -9.467  1.00 29.86  ? 471  TYR A C     1 
ATOM   3638 O O     . TYR A 1 471 ? 8.807   18.692  -9.936  1.00 28.49  ? 471  TYR A O     1 
ATOM   3639 C CB    . TYR A 1 471 ? 11.109  20.233  -8.226  1.00 33.38  ? 471  TYR A CB    1 
ATOM   3640 C CG    . TYR A 1 471 ? 10.170  21.276  -8.762  1.00 36.79  ? 471  TYR A CG    1 
ATOM   3641 C CD1   . TYR A 1 471 ? 9.052   21.639  -8.035  1.00 42.35  ? 471  TYR A CD1   1 
ATOM   3642 C CD2   . TYR A 1 471 ? 10.328  21.802  -10.035 1.00 38.89  ? 471  TYR A CD2   1 
ATOM   3643 C CE1   . TYR A 1 471 ? 8.128   22.539  -8.548  1.00 50.60  ? 471  TYR A CE1   1 
ATOM   3644 C CE2   . TYR A 1 471 ? 9.428   22.717  -10.559 1.00 43.76  ? 471  TYR A CE2   1 
ATOM   3645 C CZ    . TYR A 1 471 ? 8.316   23.072  -9.815  1.00 50.95  ? 471  TYR A CZ    1 
ATOM   3646 O OH    . TYR A 1 471 ? 7.415   23.953  -10.323 1.00 54.03  ? 471  TYR A OH    1 
ATOM   3647 N N     . ARG A 1 472 ? 10.805  17.634  -10.134 1.00 29.74  ? 472  ARG A N     1 
ATOM   3648 C CA    . ARG A 1 472 ? 10.540  17.163  -11.517 1.00 31.13  ? 472  ARG A CA    1 
ATOM   3649 C C     . ARG A 1 472 ? 11.420  15.937  -11.733 1.00 31.15  ? 472  ARG A C     1 
ATOM   3650 O O     . ARG A 1 472 ? 12.579  15.978  -11.252 1.00 26.80  ? 472  ARG A O     1 
ATOM   3651 C CB    . ARG A 1 472 ? 10.847  18.340  -12.450 1.00 31.87  ? 472  ARG A CB    1 
ATOM   3652 C CG    . ARG A 1 472 ? 10.441  18.184  -13.905 1.00 33.96  ? 472  ARG A CG    1 
ATOM   3653 C CD    . ARG A 1 472 ? 10.910  19.399  -14.685 1.00 30.85  ? 472  ARG A CD    1 
ATOM   3654 N NE    . ARG A 1 472 ? 10.701  19.255  -16.115 1.00 30.92  ? 472  ARG A NE    1 
ATOM   3655 C CZ    . ARG A 1 472 ? 11.206  20.094  -17.009 1.00 28.95  ? 472  ARG A CZ    1 
ATOM   3656 N NH1   . ARG A 1 472 ? 11.976  21.081  -16.599 1.00 28.21  ? 472  ARG A NH1   1 
ATOM   3657 N NH2   . ARG A 1 472 ? 10.993  19.928  -18.303 1.00 30.17  ? 472  ARG A NH2   1 
ATOM   3658 N N     . THR A 1 473 ? 10.919  14.896  -12.406 1.00 26.16  ? 473  THR A N     1 
ATOM   3659 C CA    . THR A 1 473 ? 11.713  13.656  -12.550 1.00 27.85  ? 473  THR A CA    1 
ATOM   3660 C C     . THR A 1 473 ? 11.413  12.890  -13.839 1.00 30.33  ? 473  THR A C     1 
ATOM   3661 O O     . THR A 1 473 ? 10.428  13.194  -14.548 1.00 27.91  ? 473  THR A O     1 
ATOM   3662 C CB    . THR A 1 473 ? 11.527  12.764  -11.319 1.00 27.97  ? 473  THR A CB    1 
ATOM   3663 O OG1   . THR A 1 473 ? 12.701  11.950  -11.239 1.00 27.84  ? 473  THR A OG1   1 
ATOM   3664 C CG2   . THR A 1 473 ? 10.263  11.933  -11.374 1.00 28.39  ? 473  THR A CG2   1 
ATOM   3665 N N     . HIS A 1 474 ? 12.280  11.911  -14.098 1.00 27.56  ? 474  HIS A N     1 
ATOM   3666 C CA    . HIS A 1 474 ? 12.214  10.965  -15.231 1.00 27.19  ? 474  HIS A CA    1 
ATOM   3667 C C     . HIS A 1 474 ? 11.023  9.993   -15.056 1.00 28.29  ? 474  HIS A C     1 
ATOM   3668 O O     . HIS A 1 474 ? 10.619  9.608   -13.873 1.00 23.76  ? 474  HIS A O     1 
ATOM   3669 C CB    . HIS A 1 474 ? 13.606  10.321  -15.329 1.00 27.47  ? 474  HIS A CB    1 
ATOM   3670 C CG    . HIS A 1 474 ? 13.864  9.558   -16.576 1.00 26.84  ? 474  HIS A CG    1 
ATOM   3671 N ND1   . HIS A 1 474 ? 13.343  8.316   -16.781 1.00 29.56  ? 474  HIS A ND1   1 
ATOM   3672 C CD2   . HIS A 1 474 ? 14.633  9.829   -17.649 1.00 26.62  ? 474  HIS A CD2   1 
ATOM   3673 C CE1   . HIS A 1 474 ? 13.742  7.864   -17.956 1.00 28.83  ? 474  HIS A CE1   1 
ATOM   3674 N NE2   . HIS A 1 474 ? 14.528  8.778   -18.512 1.00 23.52  ? 474  HIS A NE2   1 
ATOM   3675 N N     . ASN A 1 475 ? 10.437  9.590   -16.186 1.00 26.63  ? 475  ASN A N     1 
ATOM   3676 C CA    . ASN A 1 475 ? 9.495   8.440   -16.280 1.00 25.23  ? 475  ASN A CA    1 
ATOM   3677 C C     . ASN A 1 475 ? 9.860   7.360   -15.245 1.00 25.09  ? 475  ASN A C     1 
ATOM   3678 O O     . ASN A 1 475 ? 8.989   6.942   -14.476 1.00 25.68  ? 475  ASN A O     1 
ATOM   3679 C CB    . ASN A 1 475 ? 9.525   7.849   -17.686 1.00 26.40  ? 475  ASN A CB    1 
ATOM   3680 C CG    . ASN A 1 475 ? 8.709   8.684   -18.657 1.00 29.50  ? 475  ASN A CG    1 
ATOM   3681 O OD1   . ASN A 1 475 ? 7.726   9.319   -18.263 1.00 26.06  ? 475  ASN A OD1   1 
ATOM   3682 N ND2   . ASN A 1 475 ? 9.143   8.725   -19.907 1.00 30.46  ? 475  ASN A ND2   1 
ATOM   3683 N N     . ALA A 1 476 ? 11.117  6.917   -15.239 1.00 26.03  ? 476  ALA A N     1 
ATOM   3684 C CA    . ALA A 1 476 ? 11.571  5.740   -14.475 1.00 28.21  ? 476  ALA A CA    1 
ATOM   3685 C C     . ALA A 1 476 ? 11.416  6.020   -12.980 1.00 27.20  ? 476  ALA A C     1 
ATOM   3686 O O     . ALA A 1 476 ? 11.303  5.068   -12.223 1.00 29.88  ? 476  ALA A O     1 
ATOM   3687 C CB    . ALA A 1 476 ? 12.984  5.409   -14.861 1.00 30.80  ? 476  ALA A CB    1 
ATOM   3688 N N     . LEU A 1 477 ? 11.296  7.283   -12.595 1.00 28.21  ? 477  LEU A N     1 
ATOM   3689 C CA    . LEU A 1 477 ? 11.377  7.701   -11.167 1.00 29.05  ? 477  LEU A CA    1 
ATOM   3690 C C     . LEU A 1 477 ? 10.067  8.285   -10.660 1.00 27.93  ? 477  LEU A C     1 
ATOM   3691 O O     . LEU A 1 477 ? 10.000  8.604   -9.467  1.00 25.00  ? 477  LEU A O     1 
ATOM   3692 C CB    . LEU A 1 477 ? 12.470  8.752   -11.055 1.00 29.10  ? 477  LEU A CB    1 
ATOM   3693 C CG    . LEU A 1 477 ? 13.872  8.257   -11.375 1.00 33.11  ? 477  LEU A CG    1 
ATOM   3694 C CD1   . LEU A 1 477 ? 14.814  9.447   -11.488 1.00 37.51  ? 477  LEU A CD1   1 
ATOM   3695 C CD2   . LEU A 1 477 ? 14.349  7.288   -10.313 1.00 31.74  ? 477  LEU A CD2   1 
ATOM   3696 N N     . MET A 1 478 ? 9.060   8.434   -11.521 1.00 29.43  ? 478  MET A N     1 
ATOM   3697 C CA    . MET A 1 478 ? 7.808   9.160   -11.168 1.00 25.58  ? 478  MET A CA    1 
ATOM   3698 C C     . MET A 1 478 ? 7.054   8.479   -10.024 1.00 26.55  ? 478  MET A C     1 
ATOM   3699 O O     . MET A 1 478 ? 6.604   9.207   -9.112  1.00 24.84  ? 478  MET A O     1 
ATOM   3700 C CB    . MET A 1 478 ? 6.912   9.298   -12.388 1.00 24.50  ? 478  MET A CB    1 
ATOM   3701 C CG    . MET A 1 478 ? 7.497   10.251  -13.378 1.00 25.15  ? 478  MET A CG    1 
ATOM   3702 S SD    . MET A 1 478 ? 6.487   10.302  -14.855 1.00 26.44  ? 478  MET A SD    1 
ATOM   3703 C CE    . MET A 1 478 ? 7.390   11.525  -15.799 1.00 25.98  ? 478  MET A CE    1 
ATOM   3704 N N     . ASP A 1 479 ? 6.913   7.147   -10.044 1.00 26.84  ? 479  ASP A N     1 
ATOM   3705 C CA    . ASP A 1 479 ? 6.175   6.413   -8.982  1.00 27.25  ? 479  ASP A CA    1 
ATOM   3706 C C     . ASP A 1 479 ? 6.863   6.631   -7.637  1.00 23.54  ? 479  ASP A C     1 
ATOM   3707 O O     . ASP A 1 479 ? 6.146   6.837   -6.647  1.00 29.23  ? 479  ASP A O     1 
ATOM   3708 C CB    . ASP A 1 479 ? 6.046   4.917   -9.281  1.00 27.65  ? 479  ASP A CB    1 
ATOM   3709 C CG    . ASP A 1 479 ? 5.091   4.656   -10.431 1.00 30.61  ? 479  ASP A CG    1 
ATOM   3710 O OD1   . ASP A 1 479 ? 4.059   5.381   -10.491 1.00 28.69  ? 479  ASP A OD1   1 
ATOM   3711 O OD2   . ASP A 1 479 ? 5.388   3.747   -11.249 1.00 31.82  ? 479  ASP A OD2   1 
ATOM   3712 N N     . GLN A 1 480 ? 8.184   6.558   -7.619  1.00 26.04  ? 480  GLN A N     1 
ATOM   3713 C CA    . GLN A 1 480 ? 8.994   6.708   -6.382  1.00 26.84  ? 480  GLN A CA    1 
ATOM   3714 C C     . GLN A 1 480 ? 8.857   8.145   -5.869  1.00 27.73  ? 480  GLN A C     1 
ATOM   3715 O O     . GLN A 1 480 ? 8.598   8.308   -4.651  1.00 27.26  ? 480  GLN A O     1 
ATOM   3716 C CB    . GLN A 1 480 ? 10.458  6.347   -6.616  1.00 26.41  ? 480  GLN A CB    1 
ATOM   3717 C CG    . GLN A 1 480 ? 11.309  6.605   -5.377  1.00 25.55  ? 480  GLN A CG    1 
ATOM   3718 C CD    . GLN A 1 480 ? 12.797  6.471   -5.567  1.00 28.98  ? 480  GLN A CD    1 
ATOM   3719 O OE1   . GLN A 1 480 ? 13.299  6.188   -6.659  1.00 28.25  ? 480  GLN A OE1   1 
ATOM   3720 N NE2   . GLN A 1 480 ? 13.517  6.646   -4.463  1.00 27.96  ? 480  GLN A NE2   1 
ATOM   3721 N N     . VAL A 1 481 ? 8.998   9.154   -6.739  1.00 26.30  ? 481  VAL A N     1 
ATOM   3722 C CA    . VAL A 1 481 ? 8.876   10.584  -6.310  1.00 28.54  ? 481  VAL A CA    1 
ATOM   3723 C C     . VAL A 1 481 ? 7.465   10.826  -5.778  1.00 25.88  ? 481  VAL A C     1 
ATOM   3724 O O     . VAL A 1 481 ? 7.361   11.331  -4.665  1.00 22.57  ? 481  VAL A O     1 
ATOM   3725 C CB    . VAL A 1 481 ? 9.290   11.590  -7.394  1.00 26.66  ? 481  VAL A CB    1 
ATOM   3726 C CG1   . VAL A 1 481 ? 9.008   13.035  -6.972  1.00 25.19  ? 481  VAL A CG1   1 
ATOM   3727 C CG2   . VAL A 1 481 ? 10.754  11.417  -7.745  1.00 27.48  ? 481  VAL A CG2   1 
ATOM   3728 N N     . MET A 1 482 ? 6.414   10.419  -6.495  1.00 24.94  ? 482  MET A N     1 
ATOM   3729 C CA    . MET A 1 482 ? 5.043   10.618  -5.977  1.00 25.19  ? 482  MET A CA    1 
ATOM   3730 C C     . MET A 1 482 ? 4.878   9.862   -4.649  1.00 26.60  ? 482  MET A C     1 
ATOM   3731 O O     . MET A 1 482 ? 4.146   10.384  -3.777  1.00 24.61  ? 482  MET A O     1 
ATOM   3732 C CB    . MET A 1 482 ? 3.960   10.180  -6.953  1.00 25.91  ? 482  MET A CB    1 
ATOM   3733 C CG    . MET A 1 482 ? 2.564   10.457  -6.440  1.00 27.94  ? 482  MET A CG    1 
ATOM   3734 S SD    . MET A 1 482 ? 2.270   12.160  -5.839  1.00 28.95  ? 482  MET A SD    1 
ATOM   3735 C CE    . MET A 1 482 ? 2.017   13.014  -7.396  1.00 30.92  ? 482  MET A CE    1 
ATOM   3736 N N     . GLY A 1 483 ? 5.499   8.677   -4.550  1.00 25.00  ? 483  GLY A N     1 
ATOM   3737 C CA    . GLY A 1 483 ? 5.603   7.834   -3.354  1.00 26.50  ? 483  GLY A CA    1 
ATOM   3738 C C     . GLY A 1 483 ? 6.177   8.575   -2.153  1.00 26.45  ? 483  GLY A C     1 
ATOM   3739 O O     . GLY A 1 483 ? 5.766   8.246   -1.056  1.00 30.59  ? 483  GLY A O     1 
ATOM   3740 N N     . THR A 1 484 ? 7.084   9.541   -2.340  1.00 28.86  ? 484  THR A N     1 
ATOM   3741 C CA    . THR A 1 484 ? 7.668   10.345  -1.234  1.00 28.58  ? 484  THR A CA    1 
ATOM   3742 C C     . THR A 1 484 ? 6.638   11.362  -0.714  1.00 28.86  ? 484  THR A C     1 
ATOM   3743 O O     . THR A 1 484 ? 6.723   11.717  0.476   1.00 25.77  ? 484  THR A O     1 
ATOM   3744 C CB    . THR A 1 484 ? 8.992   11.005  -1.638  1.00 29.92  ? 484  THR A CB    1 
ATOM   3745 O OG1   . THR A 1 484 ? 8.780   12.054  -2.592  1.00 28.23  ? 484  THR A OG1   1 
ATOM   3746 C CG2   . THR A 1 484 ? 9.987   9.996   -2.162  1.00 25.76  ? 484  THR A CG2   1 
ATOM   3747 N N     . TYR A 1 485 ? 5.680   11.790  -1.541  1.00 26.65  ? 485  TYR A N     1 
ATOM   3748 C CA    . TYR A 1 485 ? 4.683   12.838  -1.183  1.00 25.83  ? 485  TYR A CA    1 
ATOM   3749 C C     . TYR A 1 485 ? 3.455   12.152  -0.573  1.00 27.86  ? 485  TYR A C     1 
ATOM   3750 O O     . TYR A 1 485 ? 2.311   12.464  -0.957  1.00 27.90  ? 485  TYR A O     1 
ATOM   3751 C CB    . TYR A 1 485 ? 4.380   13.725  -2.394  1.00 25.89  ? 485  TYR A CB    1 
ATOM   3752 C CG    . TYR A 1 485 ? 5.507   14.651  -2.793  1.00 25.54  ? 485  TYR A CG    1 
ATOM   3753 C CD1   . TYR A 1 485 ? 5.677   15.883  -2.188  1.00 24.88  ? 485  TYR A CD1   1 
ATOM   3754 C CD2   . TYR A 1 485 ? 6.397   14.310  -3.786  1.00 24.40  ? 485  TYR A CD2   1 
ATOM   3755 C CE1   . TYR A 1 485 ? 6.688   16.752  -2.558  1.00 26.21  ? 485  TYR A CE1   1 
ATOM   3756 C CE2   . TYR A 1 485 ? 7.428   15.148  -4.154  1.00 25.27  ? 485  TYR A CE2   1 
ATOM   3757 C CZ    . TYR A 1 485 ? 7.592   16.372  -3.534  1.00 24.87  ? 485  TYR A CZ    1 
ATOM   3758 O OH    . TYR A 1 485 ? 8.591   17.199  -3.938  1.00 26.52  ? 485  TYR A OH    1 
ATOM   3759 N N     . ASN A 1 486 ? 3.685   11.268  0.411   1.00 27.98  ? 486  ASN A N     1 
ATOM   3760 C CA    . ASN A 1 486 ? 2.650   10.354  0.950   1.00 27.72  ? 486  ASN A CA    1 
ATOM   3761 C C     . ASN A 1 486 ? 2.179   10.795  2.349   1.00 28.58  ? 486  ASN A C     1 
ATOM   3762 O O     . ASN A 1 486 ? 1.694   9.926   3.086   1.00 28.15  ? 486  ASN A O     1 
ATOM   3763 C CB    . ASN A 1 486 ? 3.127   8.907   0.916   1.00 29.94  ? 486  ASN A CB    1 
ATOM   3764 C CG    . ASN A 1 486 ? 4.279   8.627   1.861   1.00 28.93  ? 486  ASN A CG    1 
ATOM   3765 O OD1   . ASN A 1 486 ? 4.937   9.549   2.350   1.00 29.05  ? 486  ASN A OD1   1 
ATOM   3766 N ND2   . ASN A 1 486 ? 4.555   7.349   2.055   1.00 26.69  ? 486  ASN A ND2   1 
ATOM   3767 N N     . TRP A 1 487 ? 2.160   12.099  2.656   1.00 26.71  ? 487  TRP A N     1 
ATOM   3768 C CA    . TRP A 1 487 ? 1.448   12.616  3.859   1.00 26.60  ? 487  TRP A CA    1 
ATOM   3769 C C     . TRP A 1 487 ? -0.011  12.099  3.844   1.00 30.31  ? 487  TRP A C     1 
ATOM   3770 O O     . TRP A 1 487 ? -0.593  11.938  2.748   1.00 25.59  ? 487  TRP A O     1 
ATOM   3771 C CB    . TRP A 1 487 ? 1.524   14.151  3.874   1.00 29.59  ? 487  TRP A CB    1 
ATOM   3772 C CG    . TRP A 1 487 ? 1.135   14.796  5.163   1.00 26.34  ? 487  TRP A CG    1 
ATOM   3773 C CD1   . TRP A 1 487 ? 1.970   15.134  6.196   1.00 27.06  ? 487  TRP A CD1   1 
ATOM   3774 C CD2   . TRP A 1 487 ? -0.191  15.133  5.592   1.00 26.80  ? 487  TRP A CD2   1 
ATOM   3775 N NE1   . TRP A 1 487 ? 1.254   15.688  7.219   1.00 23.45  ? 487  TRP A NE1   1 
ATOM   3776 C CE2   . TRP A 1 487 ? -0.073  15.684  6.888   1.00 25.94  ? 487  TRP A CE2   1 
ATOM   3777 C CE3   . TRP A 1 487 ? -1.458  15.075  4.994   1.00 26.50  ? 487  TRP A CE3   1 
ATOM   3778 C CZ2   . TRP A 1 487 ? -1.179  16.154  7.587   1.00 28.06  ? 487  TRP A CZ2   1 
ATOM   3779 C CZ3   . TRP A 1 487 ? -2.545  15.550  5.683   1.00 27.93  ? 487  TRP A CZ3   1 
ATOM   3780 C CH2   . TRP A 1 487 ? -2.407  16.083  6.965   1.00 28.36  ? 487  TRP A CH2   1 
ATOM   3781 N N     . GLY A 1 488 ? -0.621  11.852  5.007   1.00 26.68  ? 488  GLY A N     1 
ATOM   3782 C CA    . GLY A 1 488 ? -2.026  11.406  5.087   1.00 28.06  ? 488  GLY A CA    1 
ATOM   3783 C C     . GLY A 1 488 ? -2.246  10.048  4.444   1.00 29.06  ? 488  GLY A C     1 
ATOM   3784 O O     . GLY A 1 488 ? -3.333  9.825   3.823   1.00 29.05  ? 488  GLY A O     1 
ATOM   3785 N N     . ASP A 1 489 ? -1.297  9.137   4.638   1.00 30.71  ? 489  ASP A N     1 
ATOM   3786 C CA    . ASP A 1 489 ? -1.325  7.768   4.067   1.00 33.26  ? 489  ASP A CA    1 
ATOM   3787 C C     . ASP A 1 489 ? -1.617  7.884   2.552   1.00 31.98  ? 489  ASP A C     1 
ATOM   3788 O O     . ASP A 1 489 ? -2.566  7.258   2.068   1.00 32.79  ? 489  ASP A O     1 
ATOM   3789 C CB    . ASP A 1 489 ? -2.298  6.875   4.850   1.00 36.67  ? 489  ASP A CB    1 
ATOM   3790 C CG    . ASP A 1 489 ? -1.922  6.627   6.322   1.00 43.77  ? 489  ASP A CG    1 
ATOM   3791 O OD1   . ASP A 1 489 ? -0.702  6.618   6.684   1.00 41.77  ? 489  ASP A OD1   1 
ATOM   3792 O OD2   . ASP A 1 489 ? -2.848  6.429   7.113   1.00 44.91  ? 489  ASP A OD2   1 
ATOM   3793 N N     . GLY A 1 490 ? -0.817  8.677   1.842   1.00 31.24  ? 490  GLY A N     1 
ATOM   3794 C CA    . GLY A 1 490 ? -0.875  8.854   0.376   1.00 29.43  ? 490  GLY A CA    1 
ATOM   3795 C C     . GLY A 1 490 ? -2.064  9.701   -0.051  1.00 29.87  ? 490  GLY A C     1 
ATOM   3796 O O     . GLY A 1 490 ? -2.607  9.433   -1.136  1.00 29.72  ? 490  GLY A O     1 
ATOM   3797 N N     . ALA A 1 491 ? -2.461  10.685  0.761   1.00 26.68  ? 491  ALA A N     1 
ATOM   3798 C CA    . ALA A 1 491 ? -3.631  11.558  0.523   1.00 28.99  ? 491  ALA A CA    1 
ATOM   3799 C C     . ALA A 1 491 ? -3.519  12.299  -0.823  1.00 28.00  ? 491  ALA A C     1 
ATOM   3800 O O     . ALA A 1 491 ? -4.514  12.311  -1.513  1.00 25.78  ? 491  ALA A O     1 
ATOM   3801 C CB    . ALA A 1 491 ? -3.821  12.524  1.651   1.00 32.04  ? 491  ALA A CB    1 
ATOM   3802 N N     . LEU A 1 492 ? -2.374  12.903  -1.158  1.00 27.44  ? 492  LEU A N     1 
ATOM   3803 C CA    . LEU A 1 492 ? -2.201  13.675  -2.410  1.00 26.43  ? 492  LEU A CA    1 
ATOM   3804 C C     . LEU A 1 492 ? -2.502  12.769  -3.612  1.00 26.76  ? 492  LEU A C     1 
ATOM   3805 O O     . LEU A 1 492 ? -3.211  13.226  -4.530  1.00 27.03  ? 492  LEU A O     1 
ATOM   3806 C CB    . LEU A 1 492 ? -0.781  14.228  -2.495  1.00 26.06  ? 492  LEU A CB    1 
ATOM   3807 C CG    . LEU A 1 492 ? -0.484  15.137  -3.699  1.00 26.91  ? 492  LEU A CG    1 
ATOM   3808 C CD1   . LEU A 1 492 ? -1.306  16.401  -3.672  1.00 26.88  ? 492  LEU A CD1   1 
ATOM   3809 C CD2   . LEU A 1 492 ? 0.965   15.545  -3.704  1.00 27.90  ? 492  LEU A CD2   1 
ATOM   3810 N N     . LEU A 1 493 ? -1.906  11.573  -3.663  1.00 27.08  ? 493  LEU A N     1 
ATOM   3811 C CA    . LEU A 1 493 ? -2.072  10.651  -4.812  1.00 27.78  ? 493  LEU A CA    1 
ATOM   3812 C C     . LEU A 1 493 ? -3.537  10.193  -4.877  1.00 28.66  ? 493  LEU A C     1 
ATOM   3813 O O     . LEU A 1 493 ? -4.046  10.015  -5.995  1.00 26.50  ? 493  LEU A O     1 
ATOM   3814 C CB    . LEU A 1 493 ? -1.058  9.500   -4.734  1.00 27.78  ? 493  LEU A CB    1 
ATOM   3815 C CG    . LEU A 1 493 ? -1.115  8.488   -5.886  1.00 29.95  ? 493  LEU A CG    1 
ATOM   3816 C CD1   . LEU A 1 493 ? -0.760  9.125   -7.206  1.00 31.73  ? 493  LEU A CD1   1 
ATOM   3817 C CD2   . LEU A 1 493 ? -0.190  7.307   -5.653  1.00 32.21  ? 493  LEU A CD2   1 
ATOM   3818 N N     . LYS A 1 494 ? -4.220  10.025  -3.739  1.00 30.43  ? 494  LYS A N     1 
ATOM   3819 C CA    . LYS A 1 494 ? -5.623  9.542   -3.722  1.00 32.63  ? 494  LYS A CA    1 
ATOM   3820 C C     . LYS A 1 494 ? -6.512  10.649  -4.304  1.00 32.73  ? 494  LYS A C     1 
ATOM   3821 O O     . LYS A 1 494 ? -7.400  10.320  -5.095  1.00 33.64  ? 494  LYS A O     1 
ATOM   3822 C CB    . LYS A 1 494 ? -6.066  9.067   -2.337  1.00 33.66  ? 494  LYS A CB    1 
ATOM   3823 C CG    . LYS A 1 494 ? -5.631  7.633   -2.024  1.00 39.76  ? 494  LYS A CG    1 
ATOM   3824 C CD    . LYS A 1 494 ? -5.880  7.199   -0.586  1.00 41.09  ? 494  LYS A CD    1 
ATOM   3825 C CE    . LYS A 1 494 ? -5.129  5.944   -0.189  1.00 43.43  ? 494  LYS A CE    1 
ATOM   3826 N NZ    . LYS A 1 494 ? -4.704  6.044   1.226   1.00 44.00  ? 494  LYS A NZ    1 
ATOM   3827 N N     . PHE A 1 495 ? -6.242  11.903  -3.959  1.00 30.84  ? 495  PHE A N     1 
ATOM   3828 C CA    . PHE A 1 495 ? -6.888  13.101  -4.547  1.00 29.06  ? 495  PHE A CA    1 
ATOM   3829 C C     . PHE A 1 495 ? -6.689  13.071  -6.071  1.00 28.80  ? 495  PHE A C     1 
ATOM   3830 O O     . PHE A 1 495 ? -7.674  13.183  -6.825  1.00 30.26  ? 495  PHE A O     1 
ATOM   3831 C CB    . PHE A 1 495 ? -6.297  14.347  -3.890  1.00 30.34  ? 495  PHE A CB    1 
ATOM   3832 C CG    . PHE A 1 495 ? -6.695  15.650  -4.540  1.00 30.07  ? 495  PHE A CG    1 
ATOM   3833 C CD1   . PHE A 1 495 ? -7.915  16.241  -4.260  1.00 30.85  ? 495  PHE A CD1   1 
ATOM   3834 C CD2   . PHE A 1 495 ? -5.831  16.294  -5.412  1.00 29.62  ? 495  PHE A CD2   1 
ATOM   3835 C CE1   . PHE A 1 495 ? -8.277  17.438  -4.853  1.00 33.57  ? 495  PHE A CE1   1 
ATOM   3836 C CE2   . PHE A 1 495 ? -6.193  17.489  -6.011  1.00 30.81  ? 495  PHE A CE2   1 
ATOM   3837 C CZ    . PHE A 1 495 ? -7.410  18.064  -5.730  1.00 31.63  ? 495  PHE A CZ    1 
ATOM   3838 N N     . HIS A 1 496 ? -5.457  12.869  -6.524  1.00 26.98  ? 496  HIS A N     1 
ATOM   3839 C CA    . HIS A 1 496 ? -5.115  12.900  -7.974  1.00 30.01  ? 496  HIS A CA    1 
ATOM   3840 C C     . HIS A 1 496 ? -5.837  11.769  -8.686  1.00 27.73  ? 496  HIS A C     1 
ATOM   3841 O O     . HIS A 1 496 ? -6.326  12.020  -9.809  1.00 26.05  ? 496  HIS A O     1 
ATOM   3842 C CB    . HIS A 1 496 ? -3.603  12.822  -8.214  1.00 29.93  ? 496  HIS A CB    1 
ATOM   3843 C CG    . HIS A 1 496 ? -2.898  14.093  -7.899  1.00 28.20  ? 496  HIS A CG    1 
ATOM   3844 N ND1   . HIS A 1 496 ? -3.408  15.319  -8.273  1.00 30.91  ? 496  HIS A ND1   1 
ATOM   3845 C CD2   . HIS A 1 496 ? -1.734  14.329  -7.256  1.00 26.88  ? 496  HIS A CD2   1 
ATOM   3846 C CE1   . HIS A 1 496 ? -2.566  16.270  -7.885  1.00 32.13  ? 496  HIS A CE1   1 
ATOM   3847 N NE2   . HIS A 1 496 ? -1.537  15.680  -7.234  1.00 29.45  ? 496  HIS A NE2   1 
ATOM   3848 N N     . GLU A 1 497 ? -5.877  10.576  -8.079  1.00 27.72  ? 497  GLU A N     1 
ATOM   3849 C CA    . GLU A 1 497 ? -6.521  9.374   -8.662  1.00 28.05  ? 497  GLU A CA    1 
ATOM   3850 C C     . GLU A 1 497 ? -8.029  9.607   -8.764  1.00 29.17  ? 497  GLU A C     1 
ATOM   3851 O O     . GLU A 1 497 ? -8.638  9.252   -9.810  1.00 28.79  ? 497  GLU A O     1 
ATOM   3852 C CB    . GLU A 1 497 ? -6.223  8.124   -7.838  1.00 30.59  ? 497  GLU A CB    1 
ATOM   3853 C CG    . GLU A 1 497 ? -4.822  7.584   -8.022  1.00 32.01  ? 497  GLU A CG    1 
ATOM   3854 C CD    . GLU A 1 497 ? -4.451  6.542   -6.976  1.00 30.77  ? 497  GLU A CD    1 
ATOM   3855 O OE1   . GLU A 1 497 ? -5.242  6.335   -6.054  1.00 35.52  ? 497  GLU A OE1   1 
ATOM   3856 O OE2   . GLU A 1 497 ? -3.388  5.931   -7.106  1.00 33.48  ? 497  GLU A OE2   1 
ATOM   3857 N N     . ALA A 1 498 ? -8.623  10.207  -7.741  1.00 30.25  ? 498  ALA A N     1 
ATOM   3858 C CA    . ALA A 1 498 ? -10.081 10.445  -7.712  1.00 31.43  ? 498  ALA A CA    1 
ATOM   3859 C C     . ALA A 1 498 ? -10.424 11.347  -8.900  1.00 32.91  ? 498  ALA A C     1 
ATOM   3860 O O     . ALA A 1 498 ? -11.347 11.002  -9.674  1.00 34.05  ? 498  ALA A O     1 
ATOM   3861 C CB    . ALA A 1 498 ? -10.509 11.059  -6.406  1.00 30.62  ? 498  ALA A CB    1 
ATOM   3862 N N     . ILE A 1 499 ? -9.679  12.433  -9.066  1.00 27.07  ? 499  ILE A N     1 
ATOM   3863 C CA    . ILE A 1 499 ? -9.869  13.375  -10.205 1.00 28.64  ? 499  ILE A CA    1 
ATOM   3864 C C     . ILE A 1 499 ? -9.582  12.653  -11.527 1.00 29.87  ? 499  ILE A C     1 
ATOM   3865 O O     . ILE A 1 499 ? -10.405 12.768  -12.463 1.00 33.27  ? 499  ILE A O     1 
ATOM   3866 C CB    . ILE A 1 499 ? -8.996  14.624  -10.030 1.00 30.32  ? 499  ILE A CB    1 
ATOM   3867 C CG1   . ILE A 1 499 ? -9.498  15.435  -8.832  1.00 30.46  ? 499  ILE A CG1   1 
ATOM   3868 C CG2   . ILE A 1 499 ? -8.952  15.448  -11.319 1.00 29.45  ? 499  ILE A CG2   1 
ATOM   3869 C CD1   . ILE A 1 499 ? -8.720  16.684  -8.584  1.00 31.89  ? 499  ILE A CD1   1 
ATOM   3870 N N     . LYS A 1 500 ? -8.479  11.922  -11.621 1.00 27.96  ? 500  LYS A N     1 
ATOM   3871 C CA    . LYS A 1 500 ? -8.099  11.233  -12.890 1.00 29.93  ? 500  LYS A CA    1 
ATOM   3872 C C     . LYS A 1 500 ? -9.230  10.295  -13.356 1.00 30.52  ? 500  LYS A C     1 
ATOM   3873 O O     . LYS A 1 500 ? -9.551  10.244  -14.582 1.00 26.36  ? 500  LYS A O     1 
ATOM   3874 C CB    . LYS A 1 500 ? -6.833  10.418  -12.671 1.00 27.08  ? 500  LYS A CB    1 
ATOM   3875 C CG    . LYS A 1 500 ? -6.325  9.700   -13.895 1.00 29.38  ? 500  LYS A CG    1 
ATOM   3876 C CD    . LYS A 1 500 ? -6.105  10.608  -15.073 1.00 27.15  ? 500  LYS A CD    1 
ATOM   3877 C CE    . LYS A 1 500 ? -5.352  9.856   -16.139 1.00 29.57  ? 500  LYS A CE    1 
ATOM   3878 N NZ    . LYS A 1 500 ? -5.307  10.618  -17.403 1.00 28.08  ? 500  LYS A NZ    1 
ATOM   3879 N N     . ASP A 1 501 ? -9.759  9.516   -12.425 1.00 29.26  ? 501  ASP A N     1 
ATOM   3880 C CA    . ASP A 1 501 ? -10.755 8.458   -12.726 1.00 32.06  ? 501  ASP A CA    1 
ATOM   3881 C C     . ASP A 1 501 ? -12.086 9.127   -13.123 1.00 34.03  ? 501  ASP A C     1 
ATOM   3882 O O     . ASP A 1 501 ? -12.794 8.563   -13.977 1.00 34.63  ? 501  ASP A O     1 
ATOM   3883 C CB    . ASP A 1 501 ? -10.844 7.458   -11.568 1.00 30.65  ? 501  ASP A CB    1 
ATOM   3884 C CG    . ASP A 1 501 ? -9.670  6.489   -11.500 1.00 30.99  ? 501  ASP A CG    1 
ATOM   3885 O OD1   . ASP A 1 501 ? -9.043  6.231   -12.551 1.00 33.73  ? 501  ASP A OD1   1 
ATOM   3886 O OD2   . ASP A 1 501 ? -9.357  6.000   -10.378 1.00 31.01  ? 501  ASP A OD2   1 
ATOM   3887 N N     . ALA A 1 502 ? -12.410 10.291  -12.554 1.00 32.44  ? 502  ALA A N     1 
ATOM   3888 C CA    . ALA A 1 502 ? -13.630 11.059  -12.887 1.00 33.54  ? 502  ALA A CA    1 
ATOM   3889 C C     . ALA A 1 502 ? -13.495 11.658  -14.296 1.00 34.55  ? 502  ALA A C     1 
ATOM   3890 O O     . ALA A 1 502 ? -14.457 11.467  -15.080 1.00 31.56  ? 502  ALA A O     1 
ATOM   3891 C CB    . ALA A 1 502 ? -13.892 12.128  -11.873 1.00 33.01  ? 502  ALA A CB    1 
ATOM   3892 N N     . LEU A 1 503 ? -12.393 12.363  -14.601 1.00 27.39  ? 503  LEU A N     1 
ATOM   3893 C CA    . LEU A 1 503 ? -12.225 13.063  -15.905 1.00 31.99  ? 503  LEU A CA    1 
ATOM   3894 C C     . LEU A 1 503 ? -11.890 12.022  -16.972 1.00 30.35  ? 503  LEU A C     1 
ATOM   3895 O O     . LEU A 1 503 ? -12.182 12.273  -18.163 1.00 31.87  ? 503  LEU A O     1 
ATOM   3896 C CB    . LEU A 1 503 ? -11.129 14.146  -15.840 1.00 32.95  ? 503  LEU A CB    1 
ATOM   3897 C CG    . LEU A 1 503 ? -11.399 15.360  -14.945 1.00 34.70  ? 503  LEU A CG    1 
ATOM   3898 C CD1   . LEU A 1 503 ? -10.259 16.361  -15.014 1.00 35.61  ? 503  LEU A CD1   1 
ATOM   3899 C CD2   . LEU A 1 503 ? -12.704 16.038  -15.296 1.00 36.60  ? 503  LEU A CD2   1 
ATOM   3900 N N     . ASP A 1 504 ? -11.244 10.923  -16.570 1.00 28.46  ? 504  ASP A N     1 
ATOM   3901 C CA    . ASP A 1 504 ? -10.689 9.914   -17.504 1.00 29.21  ? 504  ASP A CA    1 
ATOM   3902 C C     . ASP A 1 504 ? -11.167 8.513   -17.139 1.00 28.68  ? 504  ASP A C     1 
ATOM   3903 O O     . ASP A 1 504 ? -10.343 7.664   -16.778 1.00 28.50  ? 504  ASP A O     1 
ATOM   3904 C CB    . ASP A 1 504 ? -9.169  10.000  -17.511 1.00 29.61  ? 504  ASP A CB    1 
ATOM   3905 C CG    . ASP A 1 504 ? -8.499  9.408   -18.731 1.00 31.75  ? 504  ASP A CG    1 
ATOM   3906 O OD1   . ASP A 1 504 ? -9.207  8.721   -19.534 1.00 32.63  ? 504  ASP A OD1   1 
ATOM   3907 O OD2   . ASP A 1 504 ? -7.268  9.672   -18.890 1.00 29.40  ? 504  ASP A OD2   1 
ATOM   3908 N N     . PRO A 1 505 ? -12.479 8.198   -17.276 1.00 31.37  ? 505  PRO A N     1 
ATOM   3909 C CA    . PRO A 1 505 ? -13.004 6.886   -16.868 1.00 29.65  ? 505  PRO A CA    1 
ATOM   3910 C C     . PRO A 1 505 ? -12.452 5.700   -17.684 1.00 28.53  ? 505  PRO A C     1 
ATOM   3911 O O     . PRO A 1 505 ? -12.415 4.614   -17.167 1.00 29.21  ? 505  PRO A O     1 
ATOM   3912 C CB    . PRO A 1 505 ? -14.527 7.051   -17.029 1.00 32.88  ? 505  PRO A CB    1 
ATOM   3913 C CG    . PRO A 1 505 ? -14.687 8.128   -18.097 1.00 31.17  ? 505  PRO A CG    1 
ATOM   3914 C CD    . PRO A 1 505 ? -13.517 9.064   -17.859 1.00 32.75  ? 505  PRO A CD    1 
ATOM   3915 N N     . ASN A 1 506 ? -11.969 5.917   -18.911 1.00 30.58  ? 506  ASN A N     1 
ATOM   3916 C CA    . ASN A 1 506 ? -11.384 4.849   -19.770 1.00 29.76  ? 506  ASN A CA    1 
ATOM   3917 C C     . ASN A 1 506 ? -9.849  4.799   -19.648 1.00 27.69  ? 506  ASN A C     1 
ATOM   3918 O O     . ASN A 1 506 ? -9.236  3.999   -20.337 1.00 29.49  ? 506  ASN A O     1 
ATOM   3919 C CB    . ASN A 1 506 ? -11.878 4.989   -21.212 1.00 31.97  ? 506  ASN A CB    1 
ATOM   3920 C CG    . ASN A 1 506 ? -13.394 5.025   -21.314 1.00 30.45  ? 506  ASN A CG    1 
ATOM   3921 O OD1   . ASN A 1 506 ? -14.061 4.140   -20.825 1.00 29.11  ? 506  ASN A OD1   1 
ATOM   3922 N ND2   . ASN A 1 506 ? -13.951 6.048   -21.945 1.00 29.92  ? 506  ASN A ND2   1 
ATOM   3923 N N     . GLY A 1 507 ? -9.232  5.584   -18.769 1.00 29.78  ? 507  GLY A N     1 
ATOM   3924 C CA    . GLY A 1 507 ? -7.782  5.526   -18.501 1.00 28.78  ? 507  GLY A CA    1 
ATOM   3925 C C     . GLY A 1 507 ? -6.928  5.791   -19.731 1.00 25.60  ? 507  GLY A C     1 
ATOM   3926 O O     . GLY A 1 507 ? -6.050  4.986   -20.010 1.00 30.12  ? 507  GLY A O     1 
ATOM   3927 N N     . ILE A 1 508 ? -7.138  6.904   -20.438 1.00 28.88  ? 508  ILE A N     1 
ATOM   3928 C CA    . ILE A 1 508 ? -6.506  7.163   -21.767 1.00 27.15  ? 508  ILE A CA    1 
ATOM   3929 C C     . ILE A 1 508 ? -5.251  8.041   -21.645 1.00 26.32  ? 508  ILE A C     1 
ATOM   3930 O O     . ILE A 1 508 ? -4.220  7.695   -22.294 1.00 27.10  ? 508  ILE A O     1 
ATOM   3931 C CB    . ILE A 1 508 ? -7.562  7.776   -22.731 1.00 29.67  ? 508  ILE A CB    1 
ATOM   3932 C CG1   . ILE A 1 508 ? -8.789  6.869   -22.880 1.00 28.33  ? 508  ILE A CG1   1 
ATOM   3933 C CG2   . ILE A 1 508 ? -6.963  8.117   -24.081 1.00 29.63  ? 508  ILE A CG2   1 
ATOM   3934 C CD1   . ILE A 1 508 ? -8.495  5.468   -23.410 1.00 28.79  ? 508  ILE A CD1   1 
ATOM   3935 N N     . ILE A 1 509 ? -5.327  9.196   -20.984 1.00 25.62  ? 509  ILE A N     1 
ATOM   3936 C CA    . ILE A 1 509 ? -4.262  10.235  -21.132 1.00 28.08  ? 509  ILE A CA    1 
ATOM   3937 C C     . ILE A 1 509 ? -3.064  9.904   -20.228 1.00 25.28  ? 509  ILE A C     1 
ATOM   3938 O O     . ILE A 1 509 ? -3.259  9.796   -18.974 1.00 25.95  ? 509  ILE A O     1 
ATOM   3939 C CB    . ILE A 1 509 ? -4.765  11.668  -20.845 1.00 29.11  ? 509  ILE A CB    1 
ATOM   3940 C CG1   . ILE A 1 509 ? -6.001  12.052  -21.658 1.00 29.63  ? 509  ILE A CG1   1 
ATOM   3941 C CG2   . ILE A 1 509 ? -3.618  12.655  -21.055 1.00 29.72  ? 509  ILE A CG2   1 
ATOM   3942 C CD1   . ILE A 1 509 ? -5.796  12.008  -23.150 1.00 30.13  ? 509  ILE A CD1   1 
ATOM   3943 N N     . ALA A 1 510 ? -1.885  9.812   -20.856 1.00 28.90  ? 510  ALA A N     1 
ATOM   3944 C CA    . ALA A 1 510 ? -0.523  9.622   -20.276 1.00 27.03  ? 510  ALA A CA    1 
ATOM   3945 C C     . ALA A 1 510 ? -0.572  8.932   -18.911 1.00 26.53  ? 510  ALA A C     1 
ATOM   3946 O O     . ALA A 1 510 ? -0.104  9.469   -17.907 1.00 28.68  ? 510  ALA A O     1 
ATOM   3947 C CB    . ALA A 1 510 ? 0.155   10.948  -20.184 1.00 24.86  ? 510  ALA A CB    1 
ATOM   3948 N N     . PRO A 1 511 ? -1.036  7.670   -18.868 1.00 24.89  ? 511  PRO A N     1 
ATOM   3949 C CA    . PRO A 1 511 ? -1.086  6.884   -17.639 1.00 26.17  ? 511  PRO A CA    1 
ATOM   3950 C C     . PRO A 1 511 ? 0.296   6.804   -16.971 1.00 24.35  ? 511  PRO A C     1 
ATOM   3951 O O     . PRO A 1 511 ? 1.312   6.677   -17.673 1.00 25.18  ? 511  PRO A O     1 
ATOM   3952 C CB    . PRO A 1 511 ? -1.531  5.485   -18.109 1.00 25.73  ? 511  PRO A CB    1 
ATOM   3953 C CG    . PRO A 1 511 ? -2.188  5.739   -19.412 1.00 25.10  ? 511  PRO A CG    1 
ATOM   3954 C CD    . PRO A 1 511 ? -1.374  6.845   -20.041 1.00 25.53  ? 511  PRO A CD    1 
ATOM   3955 N N     . GLY A 1 512 ? 0.314   6.991   -15.653 1.00 24.92  ? 512  GLY A N     1 
ATOM   3956 C CA    . GLY A 1 512 ? 1.551   6.989   -14.856 1.00 25.67  ? 512  GLY A CA    1 
ATOM   3957 C C     . GLY A 1 512 ? 2.255   8.325   -14.787 1.00 27.21  ? 512  GLY A C     1 
ATOM   3958 O O     . GLY A 1 512 ? 3.221   8.409   -14.008 1.00 26.35  ? 512  GLY A O     1 
ATOM   3959 N N     . LYS A 1 513 ? 1.872   9.341   -15.568 1.00 27.38  ? 513  LYS A N     1 
ATOM   3960 C CA    . LYS A 1 513 ? 2.516   10.682  -15.440 1.00 25.83  ? 513  LYS A CA    1 
ATOM   3961 C C     . LYS A 1 513 ? 2.449   11.116  -13.972 1.00 23.95  ? 513  LYS A C     1 
ATOM   3962 O O     . LYS A 1 513 ? 1.365   11.106  -13.403 1.00 23.34  ? 513  LYS A O     1 
ATOM   3963 C CB    . LYS A 1 513 ? 1.831   11.750  -16.290 1.00 26.45  ? 513  LYS A CB    1 
ATOM   3964 C CG    . LYS A 1 513 ? 2.430   13.147  -16.182 1.00 28.28  ? 513  LYS A CG    1 
ATOM   3965 C CD    . LYS A 1 513 ? 3.853   13.296  -16.671 1.00 31.39  ? 513  LYS A CD    1 
ATOM   3966 C CE    . LYS A 1 513 ? 4.311   14.737  -16.605 1.00 34.73  ? 513  LYS A CE    1 
ATOM   3967 N NZ    . LYS A 1 513 ? 5.784   14.898  -16.515 1.00 33.36  ? 513  LYS A NZ    1 
ATOM   3968 N N     . SER A 1 514 ? 3.555   11.561  -13.393 1.00 25.47  ? 514  SER A N     1 
ATOM   3969 C CA    . SER A 1 514 ? 3.611   12.039  -11.985 1.00 23.04  ? 514  SER A CA    1 
ATOM   3970 C C     . SER A 1 514 ? 3.171   10.945  -11.017 1.00 26.87  ? 514  SER A C     1 
ATOM   3971 O O     . SER A 1 514 ? 2.720   11.291  -9.919  1.00 27.20  ? 514  SER A O     1 
ATOM   3972 C CB    . SER A 1 514 ? 2.779   13.276  -11.838 1.00 25.24  ? 514  SER A CB    1 
ATOM   3973 O OG    . SER A 1 514 ? 3.405   14.339  -12.522 1.00 25.54  ? 514  SER A OG    1 
ATOM   3974 N N     . GLY A 1 515 ? 3.234   9.677   -11.450 1.00 26.54  ? 515  GLY A N     1 
ATOM   3975 C CA    . GLY A 1 515 ? 2.802   8.513   -10.666 1.00 28.19  ? 515  GLY A CA    1 
ATOM   3976 C C     . GLY A 1 515 ? 1.305   8.422   -10.542 1.00 27.05  ? 515  GLY A C     1 
ATOM   3977 O O     . GLY A 1 515 ? 0.860   7.683   -9.687  1.00 26.58  ? 515  GLY A O     1 
ATOM   3978 N N     . VAL A 1 516 ? 0.551   9.117   -11.399 1.00 24.61  ? 516  VAL A N     1 
ATOM   3979 C CA    . VAL A 1 516 ? -0.932  9.087   -11.327 1.00 26.75  ? 516  VAL A CA    1 
ATOM   3980 C C     . VAL A 1 516 ? -1.436  8.107   -12.386 1.00 28.50  ? 516  VAL A C     1 
ATOM   3981 O O     . VAL A 1 516 ? -1.349  8.412   -13.601 1.00 28.64  ? 516  VAL A O     1 
ATOM   3982 C CB    . VAL A 1 516 ? -1.565  10.483  -11.470 1.00 25.76  ? 516  VAL A CB    1 
ATOM   3983 C CG1   . VAL A 1 516 ? -3.080  10.398  -11.289 1.00 25.28  ? 516  VAL A CG1   1 
ATOM   3984 C CG2   . VAL A 1 516 ? -0.950  11.445  -10.462 1.00 25.21  ? 516  VAL A CG2   1 
ATOM   3985 N N     . TRP A 1 517 ? -1.922  6.963   -11.928 1.00 27.06  ? 517  TRP A N     1 
ATOM   3986 C CA    . TRP A 1 517 ? -2.387  5.885   -12.822 1.00 27.04  ? 517  TRP A CA    1 
ATOM   3987 C C     . TRP A 1 517 ? -3.889  5.857   -12.754 1.00 27.92  ? 517  TRP A C     1 
ATOM   3988 O O     . TRP A 1 517 ? -4.422  5.916   -11.656 1.00 25.61  ? 517  TRP A O     1 
ATOM   3989 C CB    . TRP A 1 517 ? -1.821  4.537   -12.393 1.00 29.16  ? 517  TRP A CB    1 
ATOM   3990 C CG    . TRP A 1 517 ? -0.353  4.411   -12.603 1.00 27.40  ? 517  TRP A CG    1 
ATOM   3991 C CD1   . TRP A 1 517 ? 0.637   4.671   -11.697 1.00 27.81  ? 517  TRP A CD1   1 
ATOM   3992 C CD2   . TRP A 1 517 ? 0.292   3.988   -13.807 1.00 27.30  ? 517  TRP A CD2   1 
ATOM   3993 N NE1   . TRP A 1 517 ? 1.861   4.438   -12.268 1.00 28.00  ? 517  TRP A NE1   1 
ATOM   3994 C CE2   . TRP A 1 517 ? 1.681   3.999   -13.553 1.00 28.40  ? 517  TRP A CE2   1 
ATOM   3995 C CE3   . TRP A 1 517 ? -0.162  3.606   -15.072 1.00 27.44  ? 517  TRP A CE3   1 
ATOM   3996 C CZ2   . TRP A 1 517 ? 2.613   3.624   -14.517 1.00 30.44  ? 517  TRP A CZ2   1 
ATOM   3997 C CZ3   . TRP A 1 517 ? 0.761   3.244   -16.026 1.00 27.56  ? 517  TRP A CZ3   1 
ATOM   3998 C CH2   . TRP A 1 517 ? 2.133   3.256   -15.752 1.00 29.25  ? 517  TRP A CH2   1 
ATOM   3999 N N     . PRO A 1 518 ? -4.580  5.695   -13.904 1.00 27.29  ? 518  PRO A N     1 
ATOM   4000 C CA    . PRO A 1 518 ? -6.012  5.438   -13.902 1.00 28.03  ? 518  PRO A CA    1 
ATOM   4001 C C     . PRO A 1 518 ? -6.249  3.979   -13.466 1.00 28.41  ? 518  PRO A C     1 
ATOM   4002 O O     . PRO A 1 518 ? -5.332  3.170   -13.570 1.00 27.55  ? 518  PRO A O     1 
ATOM   4003 C CB    . PRO A 1 518 ? -6.398  5.708   -15.358 1.00 26.42  ? 518  PRO A CB    1 
ATOM   4004 C CG    . PRO A 1 518 ? -5.179  5.238   -16.124 1.00 27.85  ? 518  PRO A CG    1 
ATOM   4005 C CD    . PRO A 1 518 ? -4.011  5.659   -15.258 1.00 29.61  ? 518  PRO A CD    1 
ATOM   4006 N N     . ALA A 1 519 ? -7.462  3.695   -12.998 1.00 30.37  ? 519  ALA A N     1 
ATOM   4007 C CA    . ALA A 1 519 ? -7.861  2.438   -12.313 1.00 31.59  ? 519  ALA A CA    1 
ATOM   4008 C C     . ALA A 1 519 ? -7.397  1.227   -13.117 1.00 32.14  ? 519  ALA A C     1 
ATOM   4009 O O     . ALA A 1 519 ? -6.779  0.369   -12.537 1.00 31.79  ? 519  ALA A O     1 
ATOM   4010 C CB    . ALA A 1 519 ? -9.339  2.435   -12.098 1.00 30.54  ? 519  ALA A CB    1 
ATOM   4011 N N     . ARG A 1 520 ? -7.572  1.223   -14.437 1.00 36.36  ? 520  ARG A N     1 
ATOM   4012 C CA    . ARG A 1 520 ? -7.334  0.018   -15.266 1.00 33.13  ? 520  ARG A CA    1 
ATOM   4013 C C     . ARG A 1 520 ? -5.843  -0.308  -15.333 1.00 30.73  ? 520  ARG A C     1 
ATOM   4014 O O     . ARG A 1 520 ? -5.528  -1.442  -15.714 1.00 32.81  ? 520  ARG A O     1 
ATOM   4015 C CB    . ARG A 1 520 ? -7.931  0.190   -16.668 1.00 34.63  ? 520  ARG A CB    1 
ATOM   4016 C CG    . ARG A 1 520 ? -7.129  1.069   -17.617 1.00 36.31  ? 520  ARG A CG    1 
ATOM   4017 C CD    . ARG A 1 520 ? -7.571  0.806   -19.051 1.00 38.05  ? 520  ARG A CD    1 
ATOM   4018 N NE    . ARG A 1 520 ? -7.120  1.842   -19.953 1.00 39.73  ? 520  ARG A NE    1 
ATOM   4019 C CZ    . ARG A 1 520 ? -6.771  1.668   -21.225 1.00 37.75  ? 520  ARG A CZ    1 
ATOM   4020 N NH1   . ARG A 1 520 ? -6.790  0.467   -21.786 1.00 36.63  ? 520  ARG A NH1   1 
ATOM   4021 N NH2   . ARG A 1 520 ? -6.399  2.728   -21.930 1.00 36.73  ? 520  ARG A NH2   1 
ATOM   4022 N N     . TYR A 1 521 ? -4.945  0.629   -15.005 1.00 33.00  ? 521  TYR A N     1 
ATOM   4023 C CA    . TYR A 1 521 ? -3.486  0.390   -15.102 1.00 31.99  ? 521  TYR A CA    1 
ATOM   4024 C C     . TYR A 1 521 ? -2.815  0.391   -13.710 1.00 35.35  ? 521  TYR A C     1 
ATOM   4025 O O     . TYR A 1 521 ? -1.607  0.101   -13.626 1.00 35.47  ? 521  TYR A O     1 
ATOM   4026 C CB    . TYR A 1 521 ? -2.821  1.424   -16.006 1.00 31.65  ? 521  TYR A CB    1 
ATOM   4027 C CG    . TYR A 1 521 ? -3.096  1.298   -17.483 1.00 32.26  ? 521  TYR A CG    1 
ATOM   4028 C CD1   . TYR A 1 521 ? -2.910  0.101   -18.144 1.00 30.18  ? 521  TYR A CD1   1 
ATOM   4029 C CD2   . TYR A 1 521 ? -3.493  2.403   -18.233 1.00 31.39  ? 521  TYR A CD2   1 
ATOM   4030 C CE1   . TYR A 1 521 ? -3.122  -0.009  -19.511 1.00 34.41  ? 521  TYR A CE1   1 
ATOM   4031 C CE2   . TYR A 1 521 ? -3.738  2.301   -19.595 1.00 29.85  ? 521  TYR A CE2   1 
ATOM   4032 C CZ    . TYR A 1 521 ? -3.554  1.090   -20.237 1.00 31.61  ? 521  TYR A CZ    1 
ATOM   4033 O OH    . TYR A 1 521 ? -3.719  0.968   -21.586 1.00 35.69  ? 521  TYR A OH    1 
ATOM   4034 N N     . ARG A 1 522 ? -3.500  0.787   -12.645 1.00 37.75  ? 522  ARG A N     1 
ATOM   4035 C CA    . ARG A 1 522 ? -2.790  0.991   -11.357 1.00 40.93  ? 522  ARG A CA    1 
ATOM   4036 C C     . ARG A 1 522 ? -2.659  -0.366  -10.653 1.00 40.95  ? 522  ARG A C     1 
ATOM   4037 O O     . ARG A 1 522 ? -3.558  -1.192  -10.783 1.00 38.21  ? 522  ARG A O     1 
ATOM   4038 C CB    . ARG A 1 522 ? -3.460  2.111   -10.562 1.00 41.95  ? 522  ARG A CB    1 
ATOM   4039 C CG    . ARG A 1 522 ? -4.027  1.718   -9.213  1.00 47.24  ? 522  ARG A CG    1 
ATOM   4040 C CD    . ARG A 1 522 ? -4.720  2.871   -8.511  1.00 44.85  ? 522  ARG A CD    1 
ATOM   4041 N NE    . ARG A 1 522 ? -5.330  3.847   -9.409  1.00 49.29  ? 522  ARG A NE    1 
ATOM   4042 C CZ    . ARG A 1 522 ? -6.517  4.416   -9.251  1.00 43.70  ? 522  ARG A CZ    1 
ATOM   4043 N NH1   . ARG A 1 522 ? -7.282  4.094   -8.223  1.00 48.38  ? 522  ARG A NH1   1 
ATOM   4044 N NH2   . ARG A 1 522 ? -6.929  5.324   -10.117 1.00 39.20  ? 522  ARG A NH2   1 
ATOM   4045 N N     . GLY A 1 523 ? -1.542  -0.581  -9.957  1.00 42.34  ? 523  GLY A N     1 
ATOM   4046 C CA    . GLY A 1 523 ? -1.265  -1.827  -9.225  1.00 43.17  ? 523  GLY A CA    1 
ATOM   4047 C C     . GLY A 1 523 ? -1.088  -3.010  -10.160 1.00 43.88  ? 523  GLY A C     1 
ATOM   4048 O O     . GLY A 1 523 ? -1.308  -4.134  -9.701  1.00 41.24  ? 523  GLY A O     1 
ATOM   4049 N N     . LYS A 1 524 ? -0.715  -2.762  -11.421 1.00 45.08  ? 524  LYS A N     1 
ATOM   4050 C CA    . LYS A 1 524 ? -0.396  -3.800  -12.441 1.00 46.55  ? 524  LYS A CA    1 
ATOM   4051 C C     . LYS A 1 524 ? 1.121   -3.801  -12.714 1.00 45.13  ? 524  LYS A C     1 
ATOM   4052 O O     . LYS A 1 524 ? 1.540   -4.527  -13.627 1.00 49.22  ? 524  LYS A O     1 
ATOM   4053 C CB    . LYS A 1 524 ? -1.183  -3.578  -13.741 1.00 45.26  ? 524  LYS A CB    1 
ATOM   4054 C CG    . LYS A 1 524 ? -2.668  -3.277  -13.601 1.00 51.10  ? 524  LYS A CG    1 
ATOM   4055 C CD    . LYS A 1 524 ? -3.560  -4.478  -13.379 1.00 58.97  ? 524  LYS A CD    1 
ATOM   4056 C CE    . LYS A 1 524 ? -4.898  -4.325  -14.059 1.00 65.34  ? 524  LYS A CE    1 
ATOM   4057 N NZ    . LYS A 1 524 ? -4.749  -4.585  -15.511 1.00 79.04  ? 524  LYS A NZ    1 
ATOM   4058 N N     . GLY A 1 525 ? 1.917   -3.031  -11.957 1.00 42.23  ? 525  GLY A N     1 
ATOM   4059 C CA    . GLY A 1 525 ? 3.377   -2.881  -12.152 1.00 43.61  ? 525  GLY A CA    1 
ATOM   4060 C C     . GLY A 1 525 ? 3.745   -2.447  -13.565 1.00 45.33  ? 525  GLY A C     1 
ATOM   4061 O O     . GLY A 1 525 ? 4.878   -2.801  -13.999 1.00 39.63  ? 525  GLY A O     1 
ATOM   4062 N N     . LEU A 1 526 ? 2.853   -1.669  -14.208 1.00 47.51  ? 526  LEU A N     1 
ATOM   4063 C CA    . LEU A 1 526 ? 2.876   -1.176  -15.627 1.00 49.83  ? 526  LEU A CA    1 
ATOM   4064 C C     . LEU A 1 526 ? 1.969   -2.039  -16.525 1.00 51.05  ? 526  LEU A C     1 
ATOM   4065 O O     . LEU A 1 526 ? 0.858   -1.668  -16.920 1.00 54.61  ? 526  LEU A O     1 
ATOM   4066 C CB    . LEU A 1 526 ? 4.316   -1.173  -16.138 1.00 51.08  ? 526  LEU A CB    1 
ATOM   4067 C CG    . LEU A 1 526 ? 5.118   0.084   -15.809 1.00 45.40  ? 526  LEU A CG    1 
ATOM   4068 C CD1   . LEU A 1 526 ? 4.944   1.091   -16.923 1.00 45.93  ? 526  LEU A CD1   1 
ATOM   4069 C CD2   . LEU A 1 526 ? 4.715   0.651   -14.451 1.00 42.46  ? 526  LEU A CD2   1 
ATOM   4070 N N     . THR B 1 4   ? -35.587 26.813  10.140  1.00 45.27  ? 4    THR B N     1 
ATOM   4071 C CA    . THR B 1 4   ? -34.691 26.622  9.004   1.00 41.36  ? 4    THR B CA    1 
ATOM   4072 C C     . THR B 1 4   ? -34.093 25.235  8.964   1.00 40.98  ? 4    THR B C     1 
ATOM   4073 O O     . THR B 1 4   ? -33.455 24.806  9.913   1.00 48.55  ? 4    THR B O     1 
ATOM   4074 C CB    . THR B 1 4   ? -33.597 27.693  8.945   1.00 41.89  ? 4    THR B CB    1 
ATOM   4075 O OG1   . THR B 1 4   ? -34.161 28.964  9.287   1.00 39.37  ? 4    THR B OG1   1 
ATOM   4076 C CG2   . THR B 1 4   ? -33.003 27.775  7.549   1.00 37.55  ? 4    THR B CG2   1 
ATOM   4077 N N     . LEU B 1 5   ? -34.342 24.519  7.883   1.00 39.88  ? 5    LEU B N     1 
ATOM   4078 C CA    . LEU B 1 5   ? -33.806 23.190  7.721   1.00 40.27  ? 5    LEU B CA    1 
ATOM   4079 C C     . LEU B 1 5   ? -33.001 23.228  6.470   1.00 39.00  ? 5    LEU B C     1 
ATOM   4080 O O     . LEU B 1 5   ? -33.287 23.993  5.571   1.00 37.68  ? 5    LEU B O     1 
ATOM   4081 C CB    . LEU B 1 5   ? -34.928 22.190  7.528   1.00 38.85  ? 5    LEU B CB    1 
ATOM   4082 C CG    . LEU B 1 5   ? -35.334 21.312  8.704   1.00 42.13  ? 5    LEU B CG    1 
ATOM   4083 C CD1   . LEU B 1 5   ? -36.806 20.960  8.600   1.00 47.40  ? 5    LEU B CD1   1 
ATOM   4084 C CD2   . LEU B 1 5   ? -34.501 20.053  8.689   1.00 42.78  ? 5    LEU B CD2   1 
ATOM   4085 N N     . PRO B 1 6   ? -31.979 22.404  6.407   1.00 39.24  ? 6    PRO B N     1 
ATOM   4086 C CA    . PRO B 1 6   ? -31.237 22.326  5.162   1.00 37.23  ? 6    PRO B CA    1 
ATOM   4087 C C     . PRO B 1 6   ? -32.033 21.629  4.077   1.00 39.41  ? 6    PRO B C     1 
ATOM   4088 O O     . PRO B 1 6   ? -32.669 20.617  4.329   1.00 36.29  ? 6    PRO B O     1 
ATOM   4089 C CB    . PRO B 1 6   ? -30.013 21.508  5.542   1.00 39.60  ? 6    PRO B CB    1 
ATOM   4090 C CG    . PRO B 1 6   ? -29.882 21.606  7.008   1.00 39.66  ? 6    PRO B CG    1 
ATOM   4091 C CD    . PRO B 1 6   ? -31.272 21.766  7.526   1.00 39.61  ? 6    PRO B CD    1 
ATOM   4092 N N     . PRO B 1 7   ? -32.004 22.172  2.874   1.00 41.17  ? 7    PRO B N     1 
ATOM   4093 C CA    . PRO B 1 7   ? -32.695 21.548  1.762   1.00 41.87  ? 7    PRO B CA    1 
ATOM   4094 C C     . PRO B 1 7   ? -32.252 20.140  1.544   1.00 43.24  ? 7    PRO B C     1 
ATOM   4095 O O     . PRO B 1 7   ? -31.080 19.832  1.558   1.00 42.71  ? 7    PRO B O     1 
ATOM   4096 C CB    . PRO B 1 7   ? -32.263 22.390  0.591   1.00 44.02  ? 7    PRO B CB    1 
ATOM   4097 C CG    . PRO B 1 7   ? -31.962 23.711  1.169   1.00 43.51  ? 7    PRO B CG    1 
ATOM   4098 C CD    . PRO B 1 7   ? -31.297 23.386  2.464   1.00 42.60  ? 7    PRO B CD    1 
ATOM   4099 N N     . GLY B 1 8   ? -33.212 19.260  1.350   1.00 40.79  ? 8    GLY B N     1 
ATOM   4100 C CA    . GLY B 1 8   ? -32.904 17.867  1.166   1.00 44.47  ? 8    GLY B CA    1 
ATOM   4101 C C     . GLY B 1 8   ? -33.047 17.110  2.457   1.00 46.58  ? 8    GLY B C     1 
ATOM   4102 O O     . GLY B 1 8   ? -33.458 15.960  2.452   1.00 52.75  ? 8    GLY B O     1 
ATOM   4103 N N     . VAL B 1 9   ? -32.747 17.748  3.575   1.00 42.15  ? 9    VAL B N     1 
ATOM   4104 C CA    . VAL B 1 9   ? -32.755 17.014  4.825   1.00 38.81  ? 9    VAL B CA    1 
ATOM   4105 C C     . VAL B 1 9   ? -34.056 16.994  5.625   1.00 35.29  ? 9    VAL B C     1 
ATOM   4106 O O     . VAL B 1 9   ? -34.757 17.991  5.729   1.00 31.90  ? 9    VAL B O     1 
ATOM   4107 C CB    . VAL B 1 9   ? -31.485 17.277  5.691   1.00 39.60  ? 9    VAL B CB    1 
ATOM   4108 C CG1   . VAL B 1 9   ? -30.374 17.864  4.847   1.00 38.21  ? 9    VAL B CG1   1 
ATOM   4109 C CG2   . VAL B 1 9   ? -31.757 18.146  6.894   1.00 45.30  ? 9    VAL B CG2   1 
ATOM   4110 N N     . SER B 1 10  ? -34.379 15.826  6.156   1.00 36.23  ? 10   SER B N     1 
ATOM   4111 C CA    . SER B 1 10  ? -35.548 15.689  7.012   1.00 41.26  ? 10   SER B CA    1 
ATOM   4112 C C     . SER B 1 10  ? -35.189 16.266  8.373   1.00 39.79  ? 10   SER B C     1 
ATOM   4113 O O     . SER B 1 10  ? -34.014 16.398  8.699   1.00 34.91  ? 10   SER B O     1 
ATOM   4114 C CB    . SER B 1 10  ? -35.858 14.201  7.167   1.00 41.53  ? 10   SER B CB    1 
ATOM   4115 O OG    . SER B 1 10  ? -34.806 13.521  7.822   1.00 41.76  ? 10   SER B OG    1 
ATOM   4116 N N     . ASP B 1 11  ? -36.172 16.573  9.203   1.00 40.94  ? 11   ASP B N     1 
ATOM   4117 C CA    . ASP B 1 11  ? -35.828 17.057  10.536  1.00 45.21  ? 11   ASP B CA    1 
ATOM   4118 C C     . ASP B 1 11  ? -35.163 15.981  11.370  1.00 41.46  ? 11   ASP B C     1 
ATOM   4119 O O     . ASP B 1 11  ? -34.302 16.266  12.193  1.00 34.77  ? 11   ASP B O     1 
ATOM   4120 C CB    . ASP B 1 11  ? -37.028 17.668  11.267  1.00 48.33  ? 11   ASP B CB    1 
ATOM   4121 C CG    . ASP B 1 11  ? -36.613 18.429  12.516  1.00 51.99  ? 11   ASP B CG    1 
ATOM   4122 O OD1   . ASP B 1 11  ? -35.912 19.452  12.387  1.00 57.51  ? 11   ASP B OD1   1 
ATOM   4123 O OD2   . ASP B 1 11  ? -36.965 17.992  13.629  1.00 53.52  ? 11   ASP B OD2   1 
ATOM   4124 N N     . GLU B 1 12  ? -35.552 14.744  11.142  1.00 41.04  ? 12   GLU B N     1 
ATOM   4125 C CA    . GLU B 1 12  ? -34.937 13.657  11.853  1.00 45.66  ? 12   GLU B CA    1 
ATOM   4126 C C     . GLU B 1 12  ? -33.460 13.681  11.614  1.00 42.75  ? 12   GLU B C     1 
ATOM   4127 O O     . GLU B 1 12  ? -32.675 13.691  12.550  1.00 38.36  ? 12   GLU B O     1 
ATOM   4128 C CB    . GLU B 1 12  ? -35.489 12.334  11.346  1.00 50.21  ? 12   GLU B CB    1 
ATOM   4129 C CG    . GLU B 1 12  ? -35.044 11.120  12.142  1.00 63.55  ? 12   GLU B CG    1 
ATOM   4130 C CD    . GLU B 1 12  ? -35.991 9.951   11.979  1.00 78.35  ? 12   GLU B CD    1 
ATOM   4131 O OE1   . GLU B 1 12  ? -37.168 10.185  11.635  1.00 77.44  ? 12   GLU B OE1   1 
ATOM   4132 O OE2   . GLU B 1 12  ? -35.563 8.800   12.189  1.00 86.96  ? 12   GLU B OE2   1 
ATOM   4133 N N     . ASP B 1 13  ? -33.074 13.698  10.349  1.00 39.16  ? 13   ASP B N     1 
ATOM   4134 C CA    . ASP B 1 13  ? -31.671 13.636  10.036  1.00 37.57  ? 13   ASP B CA    1 
ATOM   4135 C C     . ASP B 1 13  ? -30.929 14.851  10.528  1.00 34.31  ? 13   ASP B C     1 
ATOM   4136 O O     . ASP B 1 13  ? -29.816 14.738  10.986  1.00 34.02  ? 13   ASP B O     1 
ATOM   4137 C CB    . ASP B 1 13  ? -31.486 13.373  8.551   1.00 39.12  ? 13   ASP B CB    1 
ATOM   4138 C CG    . ASP B 1 13  ? -31.604 11.911  8.220   1.00 41.14  ? 13   ASP B CG    1 
ATOM   4139 O OD1   . ASP B 1 13  ? -31.703 11.110  9.168   1.00 40.58  ? 13   ASP B OD1   1 
ATOM   4140 O OD2   . ASP B 1 13  ? -31.599 11.557  7.028   1.00 42.23  ? 13   ASP B OD2   1 
ATOM   4141 N N     . PHE B 1 14  ? -31.558 16.000  10.481  1.00 34.39  ? 14   PHE B N     1 
ATOM   4142 C CA    . PHE B 1 14  ? -30.934 17.198  10.968  1.00 32.17  ? 14   PHE B CA    1 
ATOM   4143 C C     . PHE B 1 14  ? -30.624 17.071  12.446  1.00 34.42  ? 14   PHE B C     1 
ATOM   4144 O O     . PHE B 1 14  ? -29.529 17.361  12.851  1.00 28.89  ? 14   PHE B O     1 
ATOM   4145 C CB    . PHE B 1 14  ? -31.839 18.389  10.700  1.00 30.17  ? 14   PHE B CB    1 
ATOM   4146 C CG    . PHE B 1 14  ? -31.196 19.724  10.904  1.00 32.53  ? 14   PHE B CG    1 
ATOM   4147 C CD1   . PHE B 1 14  ? -29.876 19.941  10.572  1.00 34.48  ? 14   PHE B CD1   1 
ATOM   4148 C CD2   . PHE B 1 14  ? -31.935 20.778  11.404  1.00 35.67  ? 14   PHE B CD2   1 
ATOM   4149 C CE1   . PHE B 1 14  ? -29.297 21.179  10.754  1.00 35.92  ? 14   PHE B CE1   1 
ATOM   4150 C CE2   . PHE B 1 14  ? -31.364 22.019  11.586  1.00 39.82  ? 14   PHE B CE2   1 
ATOM   4151 C CZ    . PHE B 1 14  ? -30.041 22.217  11.268  1.00 34.45  ? 14   PHE B CZ    1 
ATOM   4152 N N     . THR B 1 15  ? -31.557 16.594  13.252  1.00 35.97  ? 15   THR B N     1 
ATOM   4153 C CA    . THR B 1 15  ? -31.319 16.550  14.685  1.00 33.33  ? 15   THR B CA    1 
ATOM   4154 C C     . THR B 1 15  ? -30.323 15.479  15.038  1.00 33.83  ? 15   THR B C     1 
ATOM   4155 O O     . THR B 1 15  ? -29.550 15.639  15.962  1.00 30.34  ? 15   THR B O     1 
ATOM   4156 C CB    . THR B 1 15  ? -32.633 16.359  15.461  1.00 36.69  ? 15   THR B CB    1 
ATOM   4157 O OG1   . THR B 1 15  ? -33.466 15.430  14.764  1.00 33.33  ? 15   THR B OG1   1 
ATOM   4158 C CG2   . THR B 1 15  ? -33.366 17.680  15.592  1.00 35.49  ? 15   THR B CG2   1 
ATOM   4159 N N     . SER B 1 16  ? -30.317 14.402  14.280  1.00 32.53  ? 16   SER B N     1 
ATOM   4160 C CA    . SER B 1 16  ? -29.345 13.365  14.506  1.00 32.69  ? 16   SER B CA    1 
ATOM   4161 C C     . SER B 1 16  ? -27.953 13.864  14.206  1.00 31.34  ? 16   SER B C     1 
ATOM   4162 O O     . SER B 1 16  ? -27.003 13.484  14.863  1.00 29.59  ? 16   SER B O     1 
ATOM   4163 C CB    . SER B 1 16  ? -29.668 12.119  13.673  1.00 32.62  ? 16   SER B CB    1 
ATOM   4164 O OG    . SER B 1 16  ? -31.004 11.704  13.835  1.00 31.28  ? 16   SER B OG    1 
ATOM   4165 N N     . ALA B 1 17  ? -27.831 14.727  13.216  1.00 58.09  ? 17   ALA B N     1 
ATOM   4166 C CA    . ALA B 1 17  ? -26.546 15.288  12.880  1.00 56.10  ? 17   ALA B CA    1 
ATOM   4167 C C     . ALA B 1 17  ? -26.156 16.327  13.885  1.00 52.52  ? 17   ALA B C     1 
ATOM   4168 O O     . ALA B 1 17  ? -25.041 16.330  14.316  1.00 57.34  ? 17   ALA B O     1 
ATOM   4169 C CB    . ALA B 1 17  ? -26.588 15.893  11.506  1.00 58.84  ? 17   ALA B CB    1 
ATOM   4170 N N     . LEU B 1 18  ? -27.077 17.189  14.272  1.00 52.62  ? 18   LEU B N     1 
ATOM   4171 C CA    . LEU B 1 18  ? -26.822 18.257  15.280  1.00 50.63  ? 18   LEU B CA    1 
ATOM   4172 C C     . LEU B 1 18  ? -26.290 17.614  16.559  1.00 50.76  ? 18   LEU B C     1 
ATOM   4173 O O     . LEU B 1 18  ? -25.340 18.160  17.147  1.00 48.67  ? 18   LEU B O     1 
ATOM   4174 C CB    . LEU B 1 18  ? -28.115 19.027  15.562  1.00 53.08  ? 18   LEU B CB    1 
ATOM   4175 C CG    . LEU B 1 18  ? -28.659 19.876  14.412  1.00 56.89  ? 18   LEU B CG    1 
ATOM   4176 C CD1   . LEU B 1 18  ? -30.013 20.475  14.761  1.00 55.77  ? 18   LEU B CD1   1 
ATOM   4177 C CD2   . LEU B 1 18  ? -27.679 20.979  14.044  1.00 57.91  ? 18   LEU B CD2   1 
ATOM   4178 N N     . THR B 1 19  ? -26.875 16.479  16.946  1.00 52.72  ? 19   THR B N     1 
ATOM   4179 C CA    . THR B 1 19  ? -26.453 15.683  18.127  1.00 55.93  ? 19   THR B CA    1 
ATOM   4180 C C     . THR B 1 19  ? -25.015 15.239  17.885  1.00 48.01  ? 19   THR B C     1 
ATOM   4181 O O     . THR B 1 19  ? -24.164 15.573  18.730  1.00 54.41  ? 19   THR B O     1 
ATOM   4182 C CB    . THR B 1 19  ? -27.391 14.499  18.413  1.00 53.84  ? 19   THR B CB    1 
ATOM   4183 O OG1   . THR B 1 19  ? -28.670 15.030  18.761  1.00 56.56  ? 19   THR B OG1   1 
ATOM   4184 C CG2   . THR B 1 19  ? -26.887 13.607  19.529  1.00 55.08  ? 19   THR B CG2   1 
ATOM   4185 N N     . ALA B 1 20  ? -24.766 14.549  16.767  1.00 48.42  ? 20   ALA B N     1 
ATOM   4186 C CA    . ALA B 1 20  ? -23.434 14.000  16.411  1.00 48.63  ? 20   ALA B CA    1 
ATOM   4187 C C     . ALA B 1 20  ? -22.424 15.151  16.308  1.00 47.05  ? 20   ALA B C     1 
ATOM   4188 O O     . ALA B 1 20  ? -21.288 14.959  16.790  1.00 48.12  ? 20   ALA B O     1 
ATOM   4189 C CB    . ALA B 1 20  ? -23.496 13.167  15.156  1.00 51.04  ? 20   ALA B CB    1 
ATOM   4190 N N     . PHE B 1 21  ? -22.822 16.308  15.751  1.00 44.68  ? 21   PHE B N     1 
ATOM   4191 C CA    . PHE B 1 21  ? -22.011 17.557  15.764  1.00 45.78  ? 21   PHE B CA    1 
ATOM   4192 C C     . PHE B 1 21  ? -21.677 17.915  17.212  1.00 44.10  ? 21   PHE B C     1 
ATOM   4193 O O     . PHE B 1 21  ? -20.507 18.207  17.497  1.00 49.65  ? 21   PHE B O     1 
ATOM   4194 C CB    . PHE B 1 21  ? -22.708 18.737  15.069  1.00 43.86  ? 21   PHE B CB    1 
ATOM   4195 C CG    . PHE B 1 21  ? -22.879 18.607  13.575  1.00 43.67  ? 21   PHE B CG    1 
ATOM   4196 C CD1   . PHE B 1 21  ? -21.927 17.964  12.790  1.00 46.17  ? 21   PHE B CD1   1 
ATOM   4197 C CD2   . PHE B 1 21  ? -23.993 19.140  12.947  1.00 40.34  ? 21   PHE B CD2   1 
ATOM   4198 C CE1   . PHE B 1 21  ? -22.097 17.840  11.417  1.00 45.07  ? 21   PHE B CE1   1 
ATOM   4199 C CE2   . PHE B 1 21  ? -24.144 19.052  11.574  1.00 39.76  ? 21   PHE B CE2   1 
ATOM   4200 C CZ    . PHE B 1 21  ? -23.210 18.382  10.814  1.00 42.48  ? 21   PHE B CZ    1 
ATOM   4201 N N     . ARG B 1 22  ? -22.670 17.891  18.103  1.00 47.76  ? 22   ARG B N     1 
ATOM   4202 C CA    . ARG B 1 22  ? -22.474 18.259  19.536  1.00 50.10  ? 22   ARG B CA    1 
ATOM   4203 C C     . ARG B 1 22  ? -21.410 17.343  20.153  1.00 43.72  ? 22   ARG B C     1 
ATOM   4204 O O     . ARG B 1 22  ? -20.500 17.880  20.804  1.00 46.73  ? 22   ARG B O     1 
ATOM   4205 C CB    . ARG B 1 22  ? -23.802 18.272  20.301  1.00 46.98  ? 22   ARG B CB    1 
ATOM   4206 C CG    . ARG B 1 22  ? -24.697 19.434  19.892  1.00 53.07  ? 22   ARG B CG    1 
ATOM   4207 C CD    . ARG B 1 22  ? -25.745 19.845  20.906  1.00 54.07  ? 22   ARG B CD    1 
ATOM   4208 N NE    . ARG B 1 22  ? -26.837 20.522  20.226  1.00 54.13  ? 22   ARG B NE    1 
ATOM   4209 C CZ    . ARG B 1 22  ? -27.779 19.903  19.528  1.00 53.75  ? 22   ARG B CZ    1 
ATOM   4210 N NH1   . ARG B 1 22  ? -27.772 18.585  19.414  1.00 60.40  ? 22   ARG B NH1   1 
ATOM   4211 N NH2   . ARG B 1 22  ? -28.724 20.603  18.932  1.00 58.70  ? 22   ARG B NH2   1 
ATOM   4212 N N     . ASP B 1 23  ? -21.477 16.034  19.904  1.00 47.87  ? 23   ASP B N     1 
ATOM   4213 C CA    . ASP B 1 23  ? -20.512 15.054  20.467  1.00 49.16  ? 23   ASP B CA    1 
ATOM   4214 C C     . ASP B 1 23  ? -19.095 15.408  20.018  1.00 50.97  ? 23   ASP B C     1 
ATOM   4215 O O     . ASP B 1 23  ? -18.165 15.206  20.818  1.00 48.89  ? 23   ASP B O     1 
ATOM   4216 C CB    . ASP B 1 23  ? -20.853 13.610  20.091  1.00 51.98  ? 23   ASP B CB    1 
ATOM   4217 C CG    . ASP B 1 23  ? -22.036 13.059  20.873  1.00 57.76  ? 23   ASP B CG    1 
ATOM   4218 O OD1   . ASP B 1 23  ? -22.436 13.713  21.872  1.00 55.33  ? 23   ASP B OD1   1 
ATOM   4219 O OD2   . ASP B 1 23  ? -22.573 12.006  20.459  1.00 59.67  ? 23   ASP B OD2   1 
ATOM   4220 N N     . VAL B 1 24  ? -18.933 15.914  18.791  1.00 47.88  ? 24   VAL B N     1 
ATOM   4221 C CA    . VAL B 1 24  ? -17.591 16.201  18.212  1.00 43.46  ? 24   VAL B CA    1 
ATOM   4222 C C     . VAL B 1 24  ? -17.087 17.534  18.764  1.00 40.42  ? 24   VAL B C     1 
ATOM   4223 O O     . VAL B 1 24  ? -16.047 17.534  19.391  1.00 38.07  ? 24   VAL B O     1 
ATOM   4224 C CB    . VAL B 1 24  ? -17.632 16.180  16.671  1.00 44.05  ? 24   VAL B CB    1 
ATOM   4225 C CG1   . VAL B 1 24  ? -16.343 16.698  16.075  1.00 41.30  ? 24   VAL B CG1   1 
ATOM   4226 C CG2   . VAL B 1 24  ? -17.942 14.790  16.139  1.00 42.09  ? 24   VAL B CG2   1 
ATOM   4227 N N     . VAL B 1 25  ? -17.815 18.629  18.553  1.00 42.17  ? 25   VAL B N     1 
ATOM   4228 C CA    . VAL B 1 25  ? -17.305 20.006  18.827  1.00 45.00  ? 25   VAL B CA    1 
ATOM   4229 C C     . VAL B 1 25  ? -17.711 20.481  20.230  1.00 43.81  ? 25   VAL B C     1 
ATOM   4230 O O     . VAL B 1 25  ? -17.103 21.455  20.685  1.00 41.75  ? 25   VAL B O     1 
ATOM   4231 C CB    . VAL B 1 25  ? -17.758 21.014  17.748  1.00 42.92  ? 25   VAL B CB    1 
ATOM   4232 C CG1   . VAL B 1 25  ? -17.342 20.560  16.362  1.00 43.36  ? 25   VAL B CG1   1 
ATOM   4233 C CG2   . VAL B 1 25  ? -19.254 21.279  17.788  1.00 47.09  ? 25   VAL B CG2   1 
ATOM   4234 N N     . GLY B 1 26  ? -18.709 19.849  20.860  1.00 48.80  ? 26   GLY B N     1 
ATOM   4235 C CA    . GLY B 1 26  ? -19.267 20.295  22.153  1.00 55.04  ? 26   GLY B CA    1 
ATOM   4236 C C     . GLY B 1 26  ? -20.476 21.208  21.985  1.00 56.41  ? 26   GLY B C     1 
ATOM   4237 O O     . GLY B 1 26  ? -20.566 21.902  20.947  1.00 51.05  ? 26   GLY B O     1 
ATOM   4238 N N     . ASP B 1 27  ? -21.340 21.247  23.007  1.00 55.48  ? 27   ASP B N     1 
ATOM   4239 C CA    . ASP B 1 27  ? -22.691 21.871  22.989  1.00 53.54  ? 27   ASP B CA    1 
ATOM   4240 C C     . ASP B 1 27  ? -22.572 23.358  22.675  1.00 48.33  ? 27   ASP B C     1 
ATOM   4241 O O     . ASP B 1 27  ? -23.415 23.854  21.914  1.00 56.51  ? 27   ASP B O     1 
ATOM   4242 C CB    . ASP B 1 27  ? -23.428 21.697  24.321  1.00 56.12  ? 27   ASP B CB    1 
ATOM   4243 C CG    . ASP B 1 27  ? -23.594 20.251  24.761  1.00 60.99  ? 27   ASP B CG    1 
ATOM   4244 O OD1   . ASP B 1 27  ? -23.613 19.362  23.886  1.00 61.23  ? 27   ASP B OD1   1 
ATOM   4245 O OD2   . ASP B 1 27  ? -23.708 20.025  25.984  1.00 70.31  ? 27   ASP B OD2   1 
ATOM   4246 N N     . GLU B 1 28  ? -21.564 24.032  23.222  1.00 45.55  ? 28   GLU B N     1 
ATOM   4247 C CA    . GLU B 1 28  ? -21.398 25.502  23.072  1.00 48.91  ? 28   GLU B CA    1 
ATOM   4248 C C     . GLU B 1 28  ? -21.075 25.878  21.618  1.00 47.04  ? 28   GLU B C     1 
ATOM   4249 O O     . GLU B 1 28  ? -21.267 27.040  21.261  1.00 45.03  ? 28   GLU B O     1 
ATOM   4250 C CB    . GLU B 1 28  ? -20.284 26.028  23.976  1.00 54.23  ? 28   GLU B CB    1 
ATOM   4251 C CG    . GLU B 1 28  ? -20.356 27.530  24.173  1.00 61.11  ? 28   GLU B CG    1 
ATOM   4252 C CD    . GLU B 1 28  ? -19.031 28.222  24.445  1.00 69.94  ? 28   GLU B CD    1 
ATOM   4253 O OE1   . GLU B 1 28  ? -18.926 29.423  24.107  1.00 75.36  ? 28   GLU B OE1   1 
ATOM   4254 O OE2   . GLU B 1 28  ? -18.108 27.563  24.986  1.00 72.96  ? 28   GLU B OE2   1 
ATOM   4255 N N     . PHE B 1 29  ? -20.526 24.966  20.819  1.00 52.47  ? 29   PHE B N     1 
ATOM   4256 C CA    . PHE B 1 29  ? -19.981 25.300  19.476  1.00 52.12  ? 29   PHE B CA    1 
ATOM   4257 C C     . PHE B 1 29  ? -20.883 24.711  18.385  1.00 53.41  ? 29   PHE B C     1 
ATOM   4258 O O     . PHE B 1 29  ? -20.429 24.605  17.232  1.00 48.62  ? 29   PHE B O     1 
ATOM   4259 C CB    . PHE B 1 29  ? -18.514 24.871  19.399  1.00 51.40  ? 29   PHE B CB    1 
ATOM   4260 C CG    . PHE B 1 29  ? -17.618 25.586  20.379  1.00 48.37  ? 29   PHE B CG    1 
ATOM   4261 C CD1   . PHE B 1 29  ? -17.423 26.959  20.293  1.00 47.44  ? 29   PHE B CD1   1 
ATOM   4262 C CD2   . PHE B 1 29  ? -16.983 24.887  21.397  1.00 44.07  ? 29   PHE B CD2   1 
ATOM   4263 C CE1   . PHE B 1 29  ? -16.606 27.615  21.201  1.00 47.46  ? 29   PHE B CE1   1 
ATOM   4264 C CE2   . PHE B 1 29  ? -16.159 25.545  22.298  1.00 47.50  ? 29   PHE B CE2   1 
ATOM   4265 C CZ    . PHE B 1 29  ? -15.972 26.905  22.200  1.00 48.02  ? 29   PHE B CZ    1 
ATOM   4266 N N     . VAL B 1 30  ? -22.126 24.365  18.746  1.00 51.12  ? 30   VAL B N     1 
ATOM   4267 C CA    . VAL B 1 30  ? -23.257 24.094  17.814  1.00 47.17  ? 30   VAL B CA    1 
ATOM   4268 C C     . VAL B 1 30  ? -24.376 25.080  18.157  1.00 55.39  ? 30   VAL B C     1 
ATOM   4269 O O     . VAL B 1 30  ? -25.019 24.903  19.209  1.00 57.92  ? 30   VAL B O     1 
ATOM   4270 C CB    . VAL B 1 30  ? -23.730 22.634  17.918  1.00 47.14  ? 30   VAL B CB    1 
ATOM   4271 C CG1   . VAL B 1 30  ? -24.853 22.324  16.942  1.00 47.69  ? 30   VAL B CG1   1 
ATOM   4272 C CG2   . VAL B 1 30  ? -22.574 21.664  17.738  1.00 49.29  ? 30   VAL B CG2   1 
ATOM   4273 N N     . ARG B 1 31  ? -24.575 26.098  17.318  1.00 55.58  ? 31   ARG B N     1 
ATOM   4274 C CA    . ARG B 1 31  ? -25.509 27.225  17.575  1.00 58.88  ? 31   ARG B CA    1 
ATOM   4275 C C     . ARG B 1 31  ? -26.695 27.103  16.609  1.00 60.90  ? 31   ARG B C     1 
ATOM   4276 O O     . ARG B 1 31  ? -26.468 27.043  15.367  1.00 50.29  ? 31   ARG B O     1 
ATOM   4277 C CB    . ARG B 1 31  ? -24.741 28.548  17.502  1.00 60.92  ? 31   ARG B CB    1 
ATOM   4278 C CG    . ARG B 1 31  ? -23.549 28.581  18.450  1.00 66.87  ? 31   ARG B CG    1 
ATOM   4279 C CD    . ARG B 1 31  ? -23.226 29.948  19.008  1.00 76.30  ? 31   ARG B CD    1 
ATOM   4280 N NE    . ARG B 1 31  ? -22.453 30.775  18.094  1.00 85.93  ? 31   ARG B NE    1 
ATOM   4281 C CZ    . ARG B 1 31  ? -21.125 30.862  18.079  1.00 91.60  ? 31   ARG B CZ    1 
ATOM   4282 N NH1   . ARG B 1 31  ? -20.389 30.163  18.932  1.00 85.84  ? 31   ARG B NH1   1 
ATOM   4283 N NH2   . ARG B 1 31  ? -20.538 31.657  17.200  1.00 96.57  ? 31   ARG B NH2   1 
ATOM   4284 N N     . THR B 1 32  ? -27.901 26.974  17.179  1.00 57.49  ? 32   THR B N     1 
ATOM   4285 C CA    . THR B 1 32  ? -29.192 26.830  16.458  1.00 58.58  ? 32   THR B CA    1 
ATOM   4286 C C     . THR B 1 32  ? -30.187 27.915  16.903  1.00 53.87  ? 32   THR B C     1 
ATOM   4287 O O     . THR B 1 32  ? -31.279 27.944  16.337  1.00 56.57  ? 32   THR B O     1 
ATOM   4288 C CB    . THR B 1 32  ? -29.768 25.424  16.665  1.00 60.86  ? 32   THR B CB    1 
ATOM   4289 O OG1   . THR B 1 32  ? -29.842 25.184  18.072  1.00 61.81  ? 32   THR B OG1   1 
ATOM   4290 C CG2   . THR B 1 32  ? -28.942 24.343  16.001  1.00 59.40  ? 32   THR B CG2   1 
ATOM   4291 N N     . ASP B 1 33  ? -29.847 28.769  17.872  1.00 53.74  ? 33   ASP B N     1 
ATOM   4292 C CA    . ASP B 1 33  ? -30.745 29.872  18.313  1.00 59.70  ? 33   ASP B CA    1 
ATOM   4293 C C     . ASP B 1 33  ? -30.810 30.944  17.225  1.00 64.86  ? 33   ASP B C     1 
ATOM   4294 O O     . ASP B 1 33  ? -29.740 31.343  16.718  1.00 57.29  ? 33   ASP B O     1 
ATOM   4295 C CB    . ASP B 1 33  ? -30.300 30.526  19.621  1.00 63.65  ? 33   ASP B CB    1 
ATOM   4296 C CG    . ASP B 1 33  ? -30.559 29.659  20.842  1.00 76.94  ? 33   ASP B CG    1 
ATOM   4297 O OD1   . ASP B 1 33  ? -31.418 28.744  20.752  1.00 79.68  ? 33   ASP B OD1   1 
ATOM   4298 O OD2   . ASP B 1 33  ? -29.894 29.895  21.874  1.00 87.06  ? 33   ASP B OD2   1 
ATOM   4299 N N     . GLU B 1 34  ? -32.023 31.411  16.920  1.00 68.63  ? 34   GLU B N     1 
ATOM   4300 C CA    . GLU B 1 34  ? -32.296 32.463  15.906  1.00 74.69  ? 34   GLU B CA    1 
ATOM   4301 C C     . GLU B 1 34  ? -31.603 33.770  16.322  1.00 72.93  ? 34   GLU B C     1 
ATOM   4302 O O     . GLU B 1 34  ? -31.390 34.608  15.444  1.00 85.32  ? 34   GLU B O     1 
ATOM   4303 C CB    . GLU B 1 34  ? -33.806 32.594  15.657  1.00 81.14  ? 34   GLU B CB    1 
ATOM   4304 C CG    . GLU B 1 34  ? -34.465 31.392  14.989  1.00 87.28  ? 34   GLU B CG    1 
ATOM   4305 C CD    . GLU B 1 34  ? -35.974 31.493  14.808  1.00 92.96  ? 34   GLU B CD    1 
ATOM   4306 O OE1   . GLU B 1 34  ? -36.577 32.431  15.372  1.00 94.84  ? 34   GLU B OE1   1 
ATOM   4307 O OE2   . GLU B 1 34  ? -36.546 30.635  14.095  1.00 91.84  ? 34   GLU B OE2   1 
ATOM   4308 N N     . ALA B 1 35  ? -31.220 33.936  17.590  1.00 69.80  ? 35   ALA B N     1 
ATOM   4309 C CA    . ALA B 1 35  ? -30.403 35.087  18.046  1.00 68.59  ? 35   ALA B CA    1 
ATOM   4310 C C     . ALA B 1 35  ? -28.961 34.911  17.558  1.00 69.02  ? 35   ALA B C     1 
ATOM   4311 O O     . ALA B 1 35  ? -28.389 35.871  17.001  1.00 64.65  ? 35   ALA B O     1 
ATOM   4312 C CB    . ALA B 1 35  ? -30.461 35.209  19.547  1.00 70.68  ? 35   ALA B CB    1 
ATOM   4313 N N     . GLU B 1 36  ? -28.398 33.716  17.760  1.00 64.41  ? 36   GLU B N     1 
ATOM   4314 C CA    . GLU B 1 36  ? -26.993 33.385  17.402  1.00 61.38  ? 36   GLU B CA    1 
ATOM   4315 C C     . GLU B 1 36  ? -26.879 33.334  15.871  1.00 61.96  ? 36   GLU B C     1 
ATOM   4316 O O     . GLU B 1 36  ? -25.840 33.755  15.331  1.00 63.34  ? 36   GLU B O     1 
ATOM   4317 C CB    . GLU B 1 36  ? -26.572 32.072  18.069  1.00 65.06  ? 36   GLU B CB    1 
ATOM   4318 C CG    . GLU B 1 36  ? -26.737 32.070  19.588  1.00 66.30  ? 36   GLU B CG    1 
ATOM   4319 C CD    . GLU B 1 36  ? -26.630 30.708  20.269  1.00 72.09  ? 36   GLU B CD    1 
ATOM   4320 O OE1   . GLU B 1 36  ? -27.071 29.688  19.674  1.00 60.74  ? 36   GLU B OE1   1 
ATOM   4321 O OE2   . GLU B 1 36  ? -26.087 30.658  21.396  1.00 72.73  ? 36   GLU B OE2   1 
ATOM   4322 N N     . LEU B 1 37  ? -27.918 32.844  15.193  1.00 58.18  ? 37   LEU B N     1 
ATOM   4323 C CA    . LEU B 1 37  ? -27.957 32.713  13.713  1.00 59.61  ? 37   LEU B CA    1 
ATOM   4324 C C     . LEU B 1 37  ? -28.002 34.110  13.081  1.00 63.11  ? 37   LEU B C     1 
ATOM   4325 O O     . LEU B 1 37  ? -27.414 34.287  11.983  1.00 60.65  ? 37   LEU B O     1 
ATOM   4326 C CB    . LEU B 1 37  ? -29.169 31.877  13.293  1.00 55.09  ? 37   LEU B CB    1 
ATOM   4327 C CG    . LEU B 1 37  ? -29.145 30.397  13.676  1.00 55.01  ? 37   LEU B CG    1 
ATOM   4328 C CD1   . LEU B 1 37  ? -30.389 29.700  13.152  1.00 56.68  ? 37   LEU B CD1   1 
ATOM   4329 C CD2   . LEU B 1 37  ? -27.894 29.685  13.169  1.00 54.43  ? 37   LEU B CD2   1 
ATOM   4330 N N     . ALA B 1 38  ? -28.638 35.071  13.758  1.00 58.79  ? 38   ALA B N     1 
ATOM   4331 C CA    . ALA B 1 38  ? -28.875 36.441  13.247  1.00 62.31  ? 38   ALA B CA    1 
ATOM   4332 C C     . ALA B 1 38  ? -27.537 37.118  12.917  1.00 59.64  ? 38   ALA B C     1 
ATOM   4333 O O     . ALA B 1 38  ? -27.500 37.876  11.943  1.00 49.70  ? 38   ALA B O     1 
ATOM   4334 C CB    . ALA B 1 38  ? -29.677 37.250  14.245  1.00 63.42  ? 38   ALA B CB    1 
ATOM   4335 N N     . ARG B 1 39  ? -26.480 36.840  13.691  1.00 61.13  ? 39   ARG B N     1 
ATOM   4336 C CA    . ARG B 1 39  ? -25.121 37.432  13.509  1.00 63.01  ? 39   ARG B CA    1 
ATOM   4337 C C     . ARG B 1 39  ? -24.435 36.887  12.241  1.00 55.45  ? 39   ARG B C     1 
ATOM   4338 O O     . ARG B 1 39  ? -23.400 37.461  11.872  1.00 51.72  ? 39   ARG B O     1 
ATOM   4339 C CB    . ARG B 1 39  ? -24.238 37.160  14.736  1.00 71.22  ? 39   ARG B CB    1 
ATOM   4340 C CG    . ARG B 1 39  ? -24.750 37.780  16.031  1.00 81.01  ? 39   ARG B CG    1 
ATOM   4341 C CD    . ARG B 1 39  ? -23.774 37.628  17.188  1.00 88.97  ? 39   ARG B CD    1 
ATOM   4342 N NE    . ARG B 1 39  ? -23.761 36.278  17.751  1.00 94.96  ? 39   ARG B NE    1 
ATOM   4343 C CZ    . ARG B 1 39  ? -22.874 35.314  17.472  1.00 105.83 ? 39   ARG B CZ    1 
ATOM   4344 N NH1   . ARG B 1 39  ? -22.992 34.130  18.052  1.00 105.08 ? 39   ARG B NH1   1 
ATOM   4345 N NH2   . ARG B 1 39  ? -21.878 35.514  16.620  1.00 107.86 ? 39   ARG B NH2   1 
ATOM   4346 N N     . PHE B 1 40  ? -24.965 35.833  11.603  1.00 54.84  ? 40   PHE B N     1 
ATOM   4347 C CA    . PHE B 1 40  ? -24.406 35.220  10.361  1.00 54.53  ? 40   PHE B CA    1 
ATOM   4348 C C     . PHE B 1 40  ? -25.238 35.612  9.132   1.00 53.50  ? 40   PHE B C     1 
ATOM   4349 O O     . PHE B 1 40  ? -24.953 35.083  8.026   1.00 53.09  ? 40   PHE B O     1 
ATOM   4350 C CB    . PHE B 1 40  ? -24.293 33.699  10.517  1.00 53.53  ? 40   PHE B CB    1 
ATOM   4351 C CG    . PHE B 1 40  ? -23.263 33.290  11.532  1.00 54.26  ? 40   PHE B CG    1 
ATOM   4352 C CD1   . PHE B 1 40  ? -23.582 33.266  12.882  1.00 54.01  ? 40   PHE B CD1   1 
ATOM   4353 C CD2   . PHE B 1 40  ? -21.963 32.998  11.151  1.00 50.22  ? 40   PHE B CD2   1 
ATOM   4354 C CE1   . PHE B 1 40  ? -22.630 32.925  13.829  1.00 55.27  ? 40   PHE B CE1   1 
ATOM   4355 C CE2   . PHE B 1 40  ? -21.015 32.647  12.098  1.00 51.76  ? 40   PHE B CE2   1 
ATOM   4356 C CZ    . PHE B 1 40  ? -21.343 32.625  13.436  1.00 55.33  ? 40   PHE B CZ    1 
ATOM   4357 N N     . HIS B 1 41  ? -26.228 36.495  9.321   1.00 56.99  ? 41   HIS B N     1 
ATOM   4358 C CA    . HIS B 1 41  ? -26.998 37.170  8.239   1.00 56.47  ? 41   HIS B CA    1 
ATOM   4359 C C     . HIS B 1 41  ? -26.027 37.925  7.332   1.00 51.15  ? 41   HIS B C     1 
ATOM   4360 O O     . HIS B 1 41  ? -25.072 38.506  7.848   1.00 52.40  ? 41   HIS B O     1 
ATOM   4361 C CB    . HIS B 1 41  ? -28.046 38.154  8.796   1.00 62.54  ? 41   HIS B CB    1 
ATOM   4362 C CG    . HIS B 1 41  ? -29.342 37.516  9.170   1.00 71.70  ? 41   HIS B CG    1 
ATOM   4363 N ND1   . HIS B 1 41  ? -29.806 37.493  10.473  1.00 79.11  ? 41   HIS B ND1   1 
ATOM   4364 C CD2   . HIS B 1 41  ? -30.271 36.874  8.426   1.00 78.84  ? 41   HIS B CD2   1 
ATOM   4365 C CE1   . HIS B 1 41  ? -30.963 36.861  10.518  1.00 79.93  ? 41   HIS B CE1   1 
ATOM   4366 N NE2   . HIS B 1 41  ? -31.272 36.469  9.273   1.00 78.26  ? 41   HIS B NE2   1 
ATOM   4367 N N     . ASP B 1 42  ? -26.278 37.921  6.025   1.00 48.59  ? 42   ASP B N     1 
ATOM   4368 C CA    . ASP B 1 42  ? -25.652 38.882  5.088   1.00 44.49  ? 42   ASP B CA    1 
ATOM   4369 C C     . ASP B 1 42  ? -26.077 40.266  5.568   1.00 44.20  ? 42   ASP B C     1 
ATOM   4370 O O     . ASP B 1 42  ? -27.275 40.547  5.630   1.00 48.93  ? 42   ASP B O     1 
ATOM   4371 C CB    . ASP B 1 42  ? -26.072 38.574  3.645   1.00 45.46  ? 42   ASP B CB    1 
ATOM   4372 C CG    . ASP B 1 42  ? -25.564 39.577  2.626   1.00 40.67  ? 42   ASP B CG    1 
ATOM   4373 O OD1   . ASP B 1 42  ? -24.794 40.454  3.034   1.00 47.04  ? 42   ASP B OD1   1 
ATOM   4374 O OD2   . ASP B 1 42  ? -25.966 39.477  1.425   1.00 39.68  ? 42   ASP B OD2   1 
ATOM   4375 N N     . PRO B 1 43  ? -25.141 41.145  5.987   1.00 42.70  ? 43   PRO B N     1 
ATOM   4376 C CA    . PRO B 1 43  ? -25.507 42.493  6.422   1.00 42.81  ? 43   PRO B CA    1 
ATOM   4377 C C     . PRO B 1 43  ? -25.911 43.415  5.262   1.00 42.51  ? 43   PRO B C     1 
ATOM   4378 O O     . PRO B 1 43  ? -26.566 44.395  5.520   1.00 40.54  ? 43   PRO B O     1 
ATOM   4379 C CB    . PRO B 1 43  ? -24.226 43.009  7.093   1.00 43.08  ? 43   PRO B CB    1 
ATOM   4380 C CG    . PRO B 1 43  ? -23.126 42.301  6.325   1.00 44.51  ? 43   PRO B CG    1 
ATOM   4381 C CD    . PRO B 1 43  ? -23.691 40.915  6.059   1.00 42.50  ? 43   PRO B CD    1 
ATOM   4382 N N     . TYR B 1 44  ? -25.479 43.113  4.030   1.00 42.38  ? 44   TYR B N     1 
ATOM   4383 C CA    . TYR B 1 44  ? -25.772 43.928  2.824   1.00 40.24  ? 44   TYR B CA    1 
ATOM   4384 C C     . TYR B 1 44  ? -26.562 43.079  1.835   1.00 45.32  ? 44   TYR B C     1 
ATOM   4385 O O     . TYR B 1 44  ? -26.116 42.867  0.711   1.00 46.67  ? 44   TYR B O     1 
ATOM   4386 C CB    . TYR B 1 44  ? -24.483 44.473  2.202   1.00 42.85  ? 44   TYR B CB    1 
ATOM   4387 C CG    . TYR B 1 44  ? -23.561 45.221  3.138   1.00 41.71  ? 44   TYR B CG    1 
ATOM   4388 C CD1   . TYR B 1 44  ? -24.017 45.797  4.317   1.00 41.14  ? 44   TYR B CD1   1 
ATOM   4389 C CD2   . TYR B 1 44  ? -22.222 45.395  2.817   1.00 40.62  ? 44   TYR B CD2   1 
ATOM   4390 C CE1   . TYR B 1 44  ? -23.164 46.488  5.171   1.00 39.02  ? 44   TYR B CE1   1 
ATOM   4391 C CE2   . TYR B 1 44  ? -21.352 46.078  3.660   1.00 42.88  ? 44   TYR B CE2   1 
ATOM   4392 C CZ    . TYR B 1 44  ? -21.825 46.627  4.844   1.00 41.56  ? 44   TYR B CZ    1 
ATOM   4393 O OH    . TYR B 1 44  ? -20.971 47.301  5.674   1.00 40.60  ? 44   TYR B OH    1 
ATOM   4394 N N     . PRO B 1 45  ? -27.751 42.547  2.217   1.00 45.47  ? 45   PRO B N     1 
ATOM   4395 C CA    . PRO B 1 45  ? -28.481 41.630  1.350   1.00 44.92  ? 45   PRO B CA    1 
ATOM   4396 C C     . PRO B 1 45  ? -28.926 42.359  0.080   1.00 47.84  ? 45   PRO B C     1 
ATOM   4397 O O     . PRO B 1 45  ? -29.139 43.551  0.121   1.00 48.12  ? 45   PRO B O     1 
ATOM   4398 C CB    . PRO B 1 45  ? -29.699 41.189  2.172   1.00 42.16  ? 45   PRO B CB    1 
ATOM   4399 C CG    . PRO B 1 45  ? -29.886 42.305  3.172   1.00 41.96  ? 45   PRO B CG    1 
ATOM   4400 C CD    . PRO B 1 45  ? -28.487 42.825  3.462   1.00 45.00  ? 45   PRO B CD    1 
ATOM   4401 N N     . VAL B 1 46  ? -29.013 41.629  -1.004  1.00 49.58  ? 46   VAL B N     1 
ATOM   4402 C CA    . VAL B 1 46  ? -29.337 42.223  -2.268  1.00 52.90  ? 46   VAL B CA    1 
ATOM   4403 C C     . VAL B 1 46  ? -30.552 41.460  -2.719  1.00 54.78  ? 46   VAL B C     1 
ATOM   4404 O O     . VAL B 1 46  ? -30.567 40.239  -2.685  1.00 55.45  ? 46   VAL B O     1 
ATOM   4405 C CB    . VAL B 1 46  ? -28.091 42.162  -3.164  1.00 54.18  ? 46   VAL B CB    1 
ATOM   4406 C CG1   . VAL B 1 46  ? -28.415 41.937  -4.589  1.00 60.52  ? 46   VAL B CG1   1 
ATOM   4407 C CG2   . VAL B 1 46  ? -27.285 43.435  -3.037  1.00 53.07  ? 46   VAL B CG2   1 
ATOM   4408 N N     . GLY B 1 47  ? -31.601 42.172  -3.086  1.00 56.82  ? 47   GLY B N     1 
ATOM   4409 C CA    . GLY B 1 47  ? -32.843 41.516  -3.409  1.00 61.49  ? 47   GLY B CA    1 
ATOM   4410 C C     . GLY B 1 47  ? -33.482 41.223  -2.074  1.00 65.10  ? 47   GLY B C     1 
ATOM   4411 O O     . GLY B 1 47  ? -33.698 42.117  -1.291  1.00 77.35  ? 47   GLY B O     1 
ATOM   4412 N N     . ASP B 1 48  ? -33.789 39.964  -1.834  1.00 59.98  ? 48   ASP B N     1 
ATOM   4413 C CA    . ASP B 1 48  ? -34.391 39.564  -0.578  1.00 64.20  ? 48   ASP B CA    1 
ATOM   4414 C C     . ASP B 1 48  ? -33.395 39.425  0.549   1.00 65.82  ? 48   ASP B C     1 
ATOM   4415 O O     . ASP B 1 48  ? -32.353 38.815  0.394   1.00 60.09  ? 48   ASP B O     1 
ATOM   4416 C CB    . ASP B 1 48  ? -35.143 38.263  -0.766  1.00 62.84  ? 48   ASP B CB    1 
ATOM   4417 N N     . ALA B 1 49  ? -33.735 39.984  1.699   1.00 62.55  ? 49   ALA B N     1 
ATOM   4418 C CA    . ALA B 1 49  ? -32.854 39.931  2.839   1.00 58.69  ? 49   ALA B CA    1 
ATOM   4419 C C     . ALA B 1 49  ? -32.923 38.624  3.577   1.00 61.35  ? 49   ALA B C     1 
ATOM   4420 O O     . ALA B 1 49  ? -32.144 38.380  4.480   1.00 66.34  ? 49   ALA B O     1 
ATOM   4421 C CB    . ALA B 1 49  ? -33.179 41.061  3.759   1.00 58.32  ? 49   ALA B CB    1 
ATOM   4422 N N     . ASP B 1 50  ? -33.847 37.769  3.186   1.00 72.22  ? 50   ASP B N     1 
ATOM   4423 C CA    . ASP B 1 50  ? -34.007 36.469  3.814   1.00 71.41  ? 50   ASP B CA    1 
ATOM   4424 C C     . ASP B 1 50  ? -33.567 35.375  2.858   1.00 70.95  ? 50   ASP B C     1 
ATOM   4425 O O     . ASP B 1 50  ? -33.790 34.199  3.120   1.00 70.17  ? 50   ASP B O     1 
ATOM   4426 C CB    . ASP B 1 50  ? -35.476 36.277  4.190   1.00 70.25  ? 50   ASP B CB    1 
ATOM   4427 C CG    . ASP B 1 50  ? -36.374 36.135  2.987   1.00 75.22  ? 50   ASP B CG    1 
ATOM   4428 O OD1   . ASP B 1 50  ? -36.572 37.134  2.270   1.00 77.74  ? 50   ASP B OD1   1 
ATOM   4429 O OD2   . ASP B 1 50  ? -36.890 35.021  2.762   1.00 81.96  ? 50   ASP B OD2   1 
ATOM   4430 N N     . ALA B 1 51  ? -32.930 35.751  1.754   1.00 65.02  ? 51   ALA B N     1 
ATOM   4431 C CA    . ALA B 1 51  ? -32.528 34.781  0.747   1.00 61.13  ? 51   ALA B CA    1 
ATOM   4432 C C     . ALA B 1 51  ? -31.455 33.788  1.154   1.00 66.04  ? 51   ALA B C     1 
ATOM   4433 O O     . ALA B 1 51  ? -31.431 32.691  0.622   1.00 68.25  ? 51   ALA B O     1 
ATOM   4434 C CB    . ALA B 1 51  ? -32.112 35.484  -0.518  1.00 55.89  ? 51   ALA B CB    1 
ATOM   4435 N N     . HIS B 1 52  ? -30.564 34.158  2.070   1.00 61.31  ? 52   HIS B N     1 
ATOM   4436 C CA    . HIS B 1 52  ? -29.451 33.276  2.435   1.00 54.50  ? 52   HIS B CA    1 
ATOM   4437 C C     . HIS B 1 52  ? -29.331 33.077  3.927   1.00 51.49  ? 52   HIS B C     1 
ATOM   4438 O O     . HIS B 1 52  ? -28.683 33.835  4.599   1.00 54.36  ? 52   HIS B O     1 
ATOM   4439 C CB    . HIS B 1 52  ? -28.166 33.812  1.825   1.00 48.91  ? 52   HIS B CB    1 
ATOM   4440 C CG    . HIS B 1 52  ? -28.206 33.915  0.335   1.00 43.93  ? 52   HIS B CG    1 
ATOM   4441 N ND1   . HIS B 1 52  ? -28.208 32.811  -0.485  1.00 41.05  ? 52   HIS B ND1   1 
ATOM   4442 C CD2   . HIS B 1 52  ? -28.273 34.990  -0.481  1.00 46.18  ? 52   HIS B CD2   1 
ATOM   4443 C CE1   . HIS B 1 52  ? -28.263 33.202  -1.744  1.00 40.49  ? 52   HIS B CE1   1 
ATOM   4444 N NE2   . HIS B 1 52  ? -28.302 34.520  -1.768  1.00 42.42  ? 52   HIS B NE2   1 
ATOM   4445 N N     . LEU B 1 53  ? -29.942 32.028  4.438   1.00 56.22  ? 53   LEU B N     1 
ATOM   4446 C CA    . LEU B 1 53  ? -29.963 31.789  5.869   1.00 54.14  ? 53   LEU B CA    1 
ATOM   4447 C C     . LEU B 1 53  ? -29.258 30.517  6.302   1.00 49.56  ? 53   LEU B C     1 
ATOM   4448 O O     . LEU B 1 53  ? -29.229 29.570  5.569   1.00 44.85  ? 53   LEU B O     1 
ATOM   4449 C CB    . LEU B 1 53  ? -31.417 31.718  6.338   1.00 54.40  ? 53   LEU B CB    1 
ATOM   4450 C CG    . LEU B 1 53  ? -32.351 32.863  5.944   1.00 56.90  ? 53   LEU B CG    1 
ATOM   4451 C CD1   . LEU B 1 53  ? -33.785 32.548  6.328   1.00 56.39  ? 53   LEU B CD1   1 
ATOM   4452 C CD2   . LEU B 1 53  ? -31.909 34.179  6.556   1.00 53.50  ? 53   LEU B CD2   1 
ATOM   4453 N N     . ALA B 1 54  ? -28.700 30.515  7.502   1.00 50.28  ? 54   ALA B N     1 
ATOM   4454 C CA    . ALA B 1 54  ? -28.018 29.334  8.062   1.00 50.00  ? 54   ALA B CA    1 
ATOM   4455 C C     . ALA B 1 54  ? -29.008 28.599  8.974   1.00 51.92  ? 54   ALA B C     1 
ATOM   4456 O O     . ALA B 1 54  ? -29.772 29.295  9.685   1.00 52.96  ? 54   ALA B O     1 
ATOM   4457 C CB    . ALA B 1 54  ? -26.778 29.787  8.795   1.00 53.17  ? 54   ALA B CB    1 
ATOM   4458 N N     . SER B 1 55  ? -29.010 27.262  8.929   1.00 46.52  ? 55   SER B N     1 
ATOM   4459 C CA    . SER B 1 55  ? -29.792 26.378  9.835   1.00 47.81  ? 55   SER B CA    1 
ATOM   4460 C C     . SER B 1 55  ? -29.043 26.174  11.157  1.00 47.59  ? 55   SER B C     1 
ATOM   4461 O O     . SER B 1 55  ? -29.693 25.839  12.159  1.00 48.46  ? 55   SER B O     1 
ATOM   4462 C CB    . SER B 1 55  ? -30.113 25.067  9.177   1.00 46.68  ? 55   SER B CB    1 
ATOM   4463 O OG    . SER B 1 55  ? -28.929 24.339  8.884   1.00 47.06  ? 55   SER B OG    1 
ATOM   4464 N N     . ALA B 1 56  ? -27.732 26.413  11.166  1.00 47.05  ? 56   ALA B N     1 
ATOM   4465 C CA    . ALA B 1 56  ? -26.847 26.234  12.335  1.00 44.57  ? 56   ALA B CA    1 
ATOM   4466 C C     . ALA B 1 56  ? -25.448 26.763  12.016  1.00 47.52  ? 56   ALA B C     1 
ATOM   4467 O O     . ALA B 1 56  ? -25.127 26.944  10.829  1.00 51.27  ? 56   ALA B O     1 
ATOM   4468 C CB    . ALA B 1 56  ? -26.798 24.774  12.715  1.00 48.56  ? 56   ALA B CB    1 
ATOM   4469 N N     . VAL B 1 57  ? -24.639 26.957  13.055  1.00 47.01  ? 57   VAL B N     1 
ATOM   4470 C CA    . VAL B 1 57  ? -23.207 27.355  12.959  1.00 47.71  ? 57   VAL B CA    1 
ATOM   4471 C C     . VAL B 1 57  ? -22.388 26.414  13.851  1.00 52.66  ? 57   VAL B C     1 
ATOM   4472 O O     . VAL B 1 57  ? -22.688 26.306  15.063  1.00 47.24  ? 57   VAL B O     1 
ATOM   4473 C CB    . VAL B 1 57  ? -23.013 28.831  13.344  1.00 49.11  ? 57   VAL B CB    1 
ATOM   4474 C CG1   . VAL B 1 57  ? -21.553 29.259  13.251  1.00 47.95  ? 57   VAL B CG1   1 
ATOM   4475 C CG2   . VAL B 1 57  ? -23.901 29.737  12.511  1.00 48.16  ? 57   VAL B CG2   1 
ATOM   4476 N N     . ILE B 1 58  ? -21.392 25.755  13.267  1.00 46.64  ? 58   ILE B N     1 
ATOM   4477 C CA    . ILE B 1 58  ? -20.538 24.766  13.972  1.00 46.37  ? 58   ILE B CA    1 
ATOM   4478 C C     . ILE B 1 58  ? -19.101 25.263  13.907  1.00 48.16  ? 58   ILE B C     1 
ATOM   4479 O O     . ILE B 1 58  ? -18.651 25.678  12.815  1.00 49.86  ? 58   ILE B O     1 
ATOM   4480 C CB    . ILE B 1 58  ? -20.742 23.375  13.372  1.00 50.15  ? 58   ILE B CB    1 
ATOM   4481 C CG1   . ILE B 1 58  ? -22.189 22.940  13.593  1.00 49.48  ? 58   ILE B CG1   1 
ATOM   4482 C CG2   . ILE B 1 58  ? -19.749 22.376  13.953  1.00 57.59  ? 58   ILE B CG2   1 
ATOM   4483 C CD1   . ILE B 1 58  ? -22.556 21.717  12.847  1.00 55.23  ? 58   ILE B CD1   1 
ATOM   4484 N N     . SER B 1 59  ? -18.457 25.298  15.069  1.00 41.74  ? 59   SER B N     1 
ATOM   4485 C CA    . SER B 1 59  ? -17.094 25.827  15.276  1.00 42.74  ? 59   SER B CA    1 
ATOM   4486 C C     . SER B 1 59  ? -16.207 24.675  15.722  1.00 45.68  ? 59   SER B C     1 
ATOM   4487 O O     . SER B 1 59  ? -16.105 24.418  16.917  1.00 43.16  ? 59   SER B O     1 
ATOM   4488 C CB    . SER B 1 59  ? -17.133 26.954  16.248  1.00 41.55  ? 59   SER B CB    1 
ATOM   4489 O OG    . SER B 1 59  ? -18.057 27.929  15.802  1.00 39.67  ? 59   SER B OG    1 
ATOM   4490 N N     . PRO B 1 60  ? -15.601 23.921  14.766  1.00 48.41  ? 60   PRO B N     1 
ATOM   4491 C CA    . PRO B 1 60  ? -14.687 22.829  15.104  1.00 42.92  ? 60   PRO B CA    1 
ATOM   4492 C C     . PRO B 1 60  ? -13.418 23.368  15.771  1.00 38.87  ? 60   PRO B C     1 
ATOM   4493 O O     . PRO B 1 60  ? -12.974 24.440  15.457  1.00 35.29  ? 60   PRO B O     1 
ATOM   4494 C CB    . PRO B 1 60  ? -14.385 22.141  13.762  1.00 46.56  ? 60   PRO B CB    1 
ATOM   4495 C CG    . PRO B 1 60  ? -14.697 23.189  12.713  1.00 51.36  ? 60   PRO B CG    1 
ATOM   4496 C CD    . PRO B 1 60  ? -15.765 24.083  13.310  1.00 48.32  ? 60   PRO B CD    1 
ATOM   4497 N N     . ARG B 1 61  ? -12.854 22.600  16.703  1.00 39.04  ? 61   ARG B N     1 
ATOM   4498 C CA    . ARG B 1 61  ? -11.640 22.992  17.456  1.00 37.03  ? 61   ARG B CA    1 
ATOM   4499 C C     . ARG B 1 61  ? -10.415 22.909  16.549  1.00 35.05  ? 61   ARG B C     1 
ATOM   4500 O O     . ARG B 1 61  ? -9.505  23.720  16.744  1.00 32.81  ? 61   ARG B O     1 
ATOM   4501 C CB    . ARG B 1 61  ? -11.456 22.066  18.661  1.00 40.79  ? 61   ARG B CB    1 
ATOM   4502 C CG    . ARG B 1 61  ? -10.407 22.535  19.658  1.00 43.42  ? 61   ARG B CG    1 
ATOM   4503 C CD    . ARG B 1 61  ? -10.283 21.534  20.803  1.00 46.12  ? 61   ARG B CD    1 
ATOM   4504 N NE    . ARG B 1 61  ? -10.002 20.179  20.319  1.00 49.36  ? 61   ARG B NE    1 
ATOM   4505 C CZ    . ARG B 1 61  ? -10.067 19.060  21.046  1.00 51.76  ? 61   ARG B CZ    1 
ATOM   4506 N NH1   . ARG B 1 61  ? -10.392 19.102  22.330  1.00 48.70  ? 61   ARG B NH1   1 
ATOM   4507 N NH2   . ARG B 1 61  ? -9.791  17.896  20.476  1.00 51.09  ? 61   ARG B NH2   1 
ATOM   4508 N N     . ASP B 1 62  ? -10.365 21.934  15.637  1.00 34.58  ? 62   ASP B N     1 
ATOM   4509 C CA    . ASP B 1 62  ? -9.105  21.522  14.963  1.00 35.08  ? 62   ASP B CA    1 
ATOM   4510 C C     . ASP B 1 62  ? -9.411  20.698  13.706  1.00 32.93  ? 62   ASP B C     1 
ATOM   4511 O O     . ASP B 1 62  ? -10.600 20.425  13.439  1.00 30.51  ? 62   ASP B O     1 
ATOM   4512 C CB    . ASP B 1 62  ? -8.192  20.788  15.944  1.00 37.85  ? 62   ASP B CB    1 
ATOM   4513 C CG    . ASP B 1 62  ? -8.847  19.639  16.684  1.00 41.49  ? 62   ASP B CG    1 
ATOM   4514 O OD1   . ASP B 1 62  ? -9.743  18.969  16.102  1.00 42.29  ? 62   ASP B OD1   1 
ATOM   4515 O OD2   . ASP B 1 62  ? -8.466  19.426  17.844  1.00 50.77  ? 62   ASP B OD2   1 
ATOM   4516 N N     . THR B 1 63  ? -8.373  20.348  12.945  1.00 34.05  ? 63   THR B N     1 
ATOM   4517 C CA    . THR B 1 63  ? -8.495  19.569  11.677  1.00 33.92  ? 63   THR B CA    1 
ATOM   4518 C C     . THR B 1 63  ? -9.289  18.274  11.923  1.00 39.91  ? 63   THR B C     1 
ATOM   4519 O O     . THR B 1 63  ? -10.219 17.960  11.116  1.00 36.32  ? 63   THR B O     1 
ATOM   4520 C CB    . THR B 1 63  ? -7.112  19.279  11.090  1.00 34.18  ? 63   THR B CB    1 
ATOM   4521 O OG1   . THR B 1 63  ? -6.521  20.554  10.869  1.00 37.24  ? 63   THR B OG1   1 
ATOM   4522 C CG2   . THR B 1 63  ? -7.160  18.460  9.820   1.00 36.14  ? 63   THR B CG2   1 
ATOM   4523 N N     . GLU B 1 64  ? -8.939  17.541  12.990  1.00 34.53  ? 64   GLU B N     1 
ATOM   4524 C CA    . GLU B 1 64  ? -9.567  16.242  13.338  1.00 35.27  ? 64   GLU B CA    1 
ATOM   4525 C C     . GLU B 1 64  ? -11.077 16.464  13.515  1.00 32.22  ? 64   GLU B C     1 
ATOM   4526 O O     . GLU B 1 64  ? -11.872 15.682  12.969  1.00 34.53  ? 64   GLU B O     1 
ATOM   4527 C CB    . GLU B 1 64  ? -8.868  15.666  14.577  1.00 37.06  ? 64   GLU B CB    1 
ATOM   4528 C CG    . GLU B 1 64  ? -7.392  15.344  14.392  1.00 39.30  ? 64   GLU B CG    1 
ATOM   4529 C CD    . GLU B 1 64  ? -6.347  16.458  14.514  1.00 43.55  ? 64   GLU B CD    1 
ATOM   4530 O OE1   . GLU B 1 64  ? -6.713  17.644  14.666  1.00 42.19  ? 64   GLU B OE1   1 
ATOM   4531 O OE2   . GLU B 1 64  ? -5.134  16.130  14.432  1.00 45.90  ? 64   GLU B OE2   1 
ATOM   4532 N N     . GLN B 1 65  ? -11.480 17.535  14.200  1.00 36.66  ? 65   GLN B N     1 
ATOM   4533 C CA    . GLN B 1 65  ? -12.920 17.873  14.392  1.00 34.98  ? 65   GLN B CA    1 
ATOM   4534 C C     . GLN B 1 65  ? -13.546 18.287  13.045  1.00 36.02  ? 65   GLN B C     1 
ATOM   4535 O O     . GLN B 1 65  ? -14.665 17.824  12.744  1.00 35.56  ? 65   GLN B O     1 
ATOM   4536 C CB    . GLN B 1 65  ? -13.070 18.916  15.494  1.00 37.44  ? 65   GLN B CB    1 
ATOM   4537 C CG    . GLN B 1 65  ? -12.925 18.320  16.896  1.00 39.01  ? 65   GLN B CG    1 
ATOM   4538 C CD    . GLN B 1 65  ? -13.436 19.219  17.996  1.00 41.37  ? 65   GLN B CD    1 
ATOM   4539 O OE1   . GLN B 1 65  ? -14.109 20.220  17.755  1.00 41.73  ? 65   GLN B OE1   1 
ATOM   4540 N NE2   . GLN B 1 65  ? -13.100 18.874  19.232  1.00 42.23  ? 65   GLN B NE2   1 
ATOM   4541 N N     . VAL B 1 66  ? -12.869 19.088  12.219  1.00 36.94  ? 66   VAL B N     1 
ATOM   4542 C CA    . VAL B 1 66  ? -13.425 19.439  10.873  1.00 37.78  ? 66   VAL B CA    1 
ATOM   4543 C C     . VAL B 1 66  ? -13.726 18.141  10.125  1.00 36.34  ? 66   VAL B C     1 
ATOM   4544 O O     . VAL B 1 66  ? -14.845 18.028  9.575   1.00 39.23  ? 66   VAL B O     1 
ATOM   4545 C CB    . VAL B 1 66  ? -12.516 20.345  10.028  1.00 37.05  ? 66   VAL B CB    1 
ATOM   4546 C CG1   . VAL B 1 66  ? -13.140 20.605  8.662   1.00 36.32  ? 66   VAL B CG1   1 
ATOM   4547 C CG2   . VAL B 1 66  ? -12.219 21.645  10.742  1.00 36.87  ? 66   VAL B CG2   1 
ATOM   4548 N N     . GLN B 1 67  ? -12.768 17.207  10.103  1.00 38.01  ? 67   GLN B N     1 
ATOM   4549 C CA    . GLN B 1 67  ? -12.913 15.902  9.405   1.00 38.27  ? 67   GLN B CA    1 
ATOM   4550 C C     . GLN B 1 67  ? -14.148 15.176  9.925   1.00 37.72  ? 67   GLN B C     1 
ATOM   4551 O O     . GLN B 1 67  ? -14.940 14.675  9.104   1.00 36.76  ? 67   GLN B O     1 
ATOM   4552 C CB    . GLN B 1 67  ? -11.704 14.999  9.626   1.00 36.25  ? 67   GLN B CB    1 
ATOM   4553 C CG    . GLN B 1 67  ? -10.478 15.417  8.846   1.00 35.78  ? 67   GLN B CG    1 
ATOM   4554 C CD    . GLN B 1 67  ? -9.383  14.398  8.982   1.00 33.54  ? 67   GLN B CD    1 
ATOM   4555 O OE1   . GLN B 1 67  ? -9.292  13.448  8.198   1.00 33.85  ? 67   GLN B OE1   1 
ATOM   4556 N NE2   . GLN B 1 67  ? -8.522  14.626  9.965   1.00 34.60  ? 67   GLN B NE2   1 
ATOM   4557 N N     . GLU B 1 68  ? -14.276 15.052  11.247  1.00 42.81  ? 68   GLU B N     1 
ATOM   4558 C CA    . GLU B 1 68  ? -15.397 14.277  11.836  1.00 46.11  ? 68   GLU B CA    1 
ATOM   4559 C C     . GLU B 1 68  ? -16.716 14.985  11.488  1.00 41.47  ? 68   GLU B C     1 
ATOM   4560 O O     . GLU B 1 68  ? -17.662 14.277  11.128  1.00 40.54  ? 68   GLU B O     1 
ATOM   4561 C CB    . GLU B 1 68  ? -15.181 14.029  13.336  1.00 53.85  ? 68   GLU B CB    1 
ATOM   4562 C CG    . GLU B 1 68  ? -16.114 12.974  13.925  1.00 58.81  ? 68   GLU B CG    1 
ATOM   4563 C CD    . GLU B 1 68  ? -16.316 11.702  13.105  1.00 62.12  ? 68   GLU B CD    1 
ATOM   4564 O OE1   . GLU B 1 68  ? -15.304 11.085  12.687  1.00 62.49  ? 68   GLU B OE1   1 
ATOM   4565 O OE2   . GLU B 1 68  ? -17.496 11.326  12.883  1.00 61.64  ? 68   GLU B OE2   1 
ATOM   4566 N N     . VAL B 1 69  ? -16.785 16.322  11.532  1.00 41.44  ? 69   VAL B N     1 
ATOM   4567 C CA    . VAL B 1 69  ? -18.062 17.039  11.223  1.00 40.05  ? 69   VAL B CA    1 
ATOM   4568 C C     . VAL B 1 69  ? -18.349 16.859  9.734   1.00 38.83  ? 69   VAL B C     1 
ATOM   4569 O O     . VAL B 1 69  ? -19.527 16.684  9.371   1.00 39.34  ? 69   VAL B O     1 
ATOM   4570 C CB    . VAL B 1 69  ? -18.100 18.516  11.661  1.00 46.09  ? 69   VAL B CB    1 
ATOM   4571 C CG1   . VAL B 1 69  ? -17.949 18.652  13.165  1.00 46.03  ? 69   VAL B CG1   1 
ATOM   4572 C CG2   . VAL B 1 69  ? -17.101 19.405  10.945  1.00 48.72  ? 69   VAL B CG2   1 
ATOM   4573 N N     . VAL B 1 70  ? -17.311 16.784  8.902   1.00 36.56  ? 70   VAL B N     1 
ATOM   4574 C CA    . VAL B 1 70  ? -17.545 16.519  7.458   1.00 34.98  ? 70   VAL B CA    1 
ATOM   4575 C C     . VAL B 1 70  ? -18.084 15.092  7.283   1.00 35.29  ? 70   VAL B C     1 
ATOM   4576 O O     . VAL B 1 70  ? -19.014 14.939  6.485   1.00 35.03  ? 70   VAL B O     1 
ATOM   4577 C CB    . VAL B 1 70  ? -16.303 16.837  6.612   1.00 30.62  ? 70   VAL B CB    1 
ATOM   4578 C CG1   . VAL B 1 70  ? -16.426 16.317  5.191   1.00 30.27  ? 70   VAL B CG1   1 
ATOM   4579 C CG2   . VAL B 1 70  ? -16.065 18.336  6.600   1.00 30.34  ? 70   VAL B CG2   1 
ATOM   4580 N N     . ARG B 1 71  ? -17.550 14.089  7.988   1.00 35.41  ? 71   ARG B N     1 
ATOM   4581 C CA    . ARG B 1 71  ? -18.045 12.677  7.910   1.00 37.69  ? 71   ARG B CA    1 
ATOM   4582 C C     . ARG B 1 71  ? -19.506 12.581  8.366   1.00 37.01  ? 71   ARG B C     1 
ATOM   4583 O O     . ARG B 1 71  ? -20.272 11.813  7.733   1.00 40.43  ? 71   ARG B O     1 
ATOM   4584 C CB    . ARG B 1 71  ? -17.196 11.730  8.761   1.00 40.01  ? 71   ARG B CB    1 
ATOM   4585 C CG    . ARG B 1 71  ? -15.814 11.466  8.187   1.00 44.63  ? 71   ARG B CG    1 
ATOM   4586 C CD    . ARG B 1 71  ? -15.047 10.395  8.939   1.00 46.43  ? 71   ARG B CD    1 
ATOM   4587 N NE    . ARG B 1 71  ? -13.614 10.487  8.696   1.00 47.00  ? 71   ARG B NE    1 
ATOM   4588 C CZ    . ARG B 1 71  ? -12.728 11.096  9.491   1.00 46.58  ? 71   ARG B CZ    1 
ATOM   4589 N NH1   . ARG B 1 71  ? -13.100 11.714  10.600  1.00 49.44  ? 71   ARG B NH1   1 
ATOM   4590 N NH2   . ARG B 1 71  ? -11.453 11.105  9.161   1.00 48.74  ? 71   ARG B NH2   1 
ATOM   4591 N N     . ILE B 1 72  ? -19.882 13.313  9.417   1.00 37.03  ? 72   ILE B N     1 
ATOM   4592 C CA    . ILE B 1 72  ? -21.284 13.358  9.938   1.00 41.22  ? 72   ILE B CA    1 
ATOM   4593 C C     . ILE B 1 72  ? -22.171 13.976  8.856   1.00 38.88  ? 72   ILE B C     1 
ATOM   4594 O O     . ILE B 1 72  ? -23.261 13.444  8.592   1.00 41.95  ? 72   ILE B O     1 
ATOM   4595 C CB    . ILE B 1 72  ? -21.393 14.132  11.274  1.00 40.84  ? 72   ILE B CB    1 
ATOM   4596 C CG1   . ILE B 1 72  ? -20.672 13.416  12.415  1.00 38.55  ? 72   ILE B CG1   1 
ATOM   4597 C CG2   . ILE B 1 72  ? -22.840 14.411  11.636  1.00 44.22  ? 72   ILE B CG2   1 
ATOM   4598 C CD1   . ILE B 1 72  ? -20.316 14.337  13.547  1.00 39.98  ? 72   ILE B CD1   1 
ATOM   4599 N N     . ALA B 1 73  ? -21.724 15.076  8.261   1.00 39.62  ? 73   ALA B N     1 
ATOM   4600 C CA    . ALA B 1 73  ? -22.453 15.754  7.168   1.00 42.00  ? 73   ALA B CA    1 
ATOM   4601 C C     . ALA B 1 73  ? -22.762 14.759  6.043   1.00 42.82  ? 73   ALA B C     1 
ATOM   4602 O O     . ALA B 1 73  ? -23.924 14.752  5.565   1.00 42.66  ? 73   ALA B O     1 
ATOM   4603 C CB    . ALA B 1 73  ? -21.638 16.904  6.671   1.00 43.35  ? 73   ALA B CB    1 
ATOM   4604 N N     . ASN B 1 74  ? -21.767 13.944  5.667   1.00 39.25  ? 74   ASN B N     1 
ATOM   4605 C CA    . ASN B 1 74  ? -21.849 12.947  4.566   1.00 39.88  ? 74   ASN B CA    1 
ATOM   4606 C C     . ASN B 1 74  ? -22.854 11.827  4.894   1.00 42.08  ? 74   ASN B C     1 
ATOM   4607 O O     . ASN B 1 74  ? -23.512 11.330  3.943   1.00 35.72  ? 74   ASN B O     1 
ATOM   4608 C CB    . ASN B 1 74  ? -20.472 12.354  4.261   1.00 40.14  ? 74   ASN B CB    1 
ATOM   4609 C CG    . ASN B 1 74  ? -19.740 13.135  3.184   1.00 38.86  ? 74   ASN B CG    1 
ATOM   4610 O OD1   . ASN B 1 74  ? -19.853 12.809  1.998   1.00 40.49  ? 74   ASN B OD1   1 
ATOM   4611 N ND2   . ASN B 1 74  ? -19.043 14.187  3.581   1.00 34.00  ? 74   ASN B ND2   1 
ATOM   4612 N N     . ARG B 1 75  ? -22.903 11.421  6.172   1.00 48.10  ? 75   ARG B N     1 
ATOM   4613 C CA    . ARG B 1 75  ? -23.805 10.374  6.727   1.00 49.99  ? 75   ARG B CA    1 
ATOM   4614 C C     . ARG B 1 75  ? -25.260 10.819  6.548   1.00 46.33  ? 75   ARG B C     1 
ATOM   4615 O O     . ARG B 1 75  ? -26.039 10.008  6.028   1.00 48.73  ? 75   ARG B O     1 
ATOM   4616 C CB    . ARG B 1 75  ? -23.505 10.096  8.203   1.00 58.67  ? 75   ARG B CB    1 
ATOM   4617 C CG    . ARG B 1 75  ? -23.869 8.680   8.648   1.00 68.73  ? 75   ARG B CG    1 
ATOM   4618 C CD    . ARG B 1 75  ? -23.904 8.478   10.154  1.00 75.02  ? 75   ARG B CD    1 
ATOM   4619 N NE    . ARG B 1 75  ? -22.576 8.527   10.766  1.00 84.13  ? 75   ARG B NE    1 
ATOM   4620 C CZ    . ARG B 1 75  ? -21.829 7.473   11.095  1.00 86.02  ? 75   ARG B CZ    1 
ATOM   4621 N NH1   . ARG B 1 75  ? -22.264 6.241   10.882  1.00 88.16  ? 75   ARG B NH1   1 
ATOM   4622 N NH2   . ARG B 1 75  ? -20.641 7.662   11.647  1.00 83.00  ? 75   ARG B NH2   1 
ATOM   4623 N N     . TYR B 1 76  ? -25.582 12.075  6.895   1.00 45.34  ? 76   TYR B N     1 
ATOM   4624 C CA    . TYR B 1 76  ? -26.968 12.606  7.006   1.00 46.64  ? 76   TYR B CA    1 
ATOM   4625 C C     . TYR B 1 76  ? -27.312 13.569  5.857   1.00 45.89  ? 76   TYR B C     1 
ATOM   4626 O O     . TYR B 1 76  ? -28.415 14.103  5.874   1.00 49.65  ? 76   TYR B O     1 
ATOM   4627 C CB    . TYR B 1 76  ? -27.146 13.268  8.377   1.00 47.36  ? 76   TYR B CB    1 
ATOM   4628 C CG    . TYR B 1 76  ? -27.083 12.280  9.512   1.00 52.39  ? 76   TYR B CG    1 
ATOM   4629 C CD1   . TYR B 1 76  ? -28.112 11.367  9.715   1.00 59.82  ? 76   TYR B CD1   1 
ATOM   4630 C CD2   . TYR B 1 76  ? -25.974 12.199  10.338  1.00 52.51  ? 76   TYR B CD2   1 
ATOM   4631 C CE1   . TYR B 1 76  ? -28.060 10.431  10.739  1.00 61.06  ? 76   TYR B CE1   1 
ATOM   4632 C CE2   . TYR B 1 76  ? -25.906 11.270  11.366  1.00 54.02  ? 76   TYR B CE2   1 
ATOM   4633 C CZ    . TYR B 1 76  ? -26.954 10.389  11.571  1.00 59.20  ? 76   TYR B CZ    1 
ATOM   4634 O OH    . TYR B 1 76  ? -26.890 9.469   12.573  1.00 64.16  ? 76   TYR B OH    1 
ATOM   4635 N N     . GLY B 1 77  ? -26.411 13.779  4.897   1.00 44.32  ? 77   GLY B N     1 
ATOM   4636 C CA    . GLY B 1 77  ? -26.653 14.605  3.703   1.00 41.72  ? 77   GLY B CA    1 
ATOM   4637 C C     . GLY B 1 77  ? -26.817 16.068  4.058   1.00 40.34  ? 77   GLY B C     1 
ATOM   4638 O O     . GLY B 1 77  ? -27.610 16.746  3.413   1.00 41.64  ? 77   GLY B O     1 
ATOM   4639 N N     . ILE B 1 78  ? -26.070 16.561  5.034   1.00 39.95  ? 78   ILE B N     1 
ATOM   4640 C CA    . ILE B 1 78  ? -26.185 17.965  5.510   1.00 38.62  ? 78   ILE B CA    1 
ATOM   4641 C C     . ILE B 1 78  ? -25.229 18.844  4.706   1.00 42.60  ? 78   ILE B C     1 
ATOM   4642 O O     . ILE B 1 78  ? -24.016 18.623  4.750   1.00 40.65  ? 78   ILE B O     1 
ATOM   4643 C CB    . ILE B 1 78  ? -25.867 17.993  7.015   1.00 39.91  ? 78   ILE B CB    1 
ATOM   4644 C CG1   . ILE B 1 78  ? -26.818 17.076  7.799   1.00 40.32  ? 78   ILE B CG1   1 
ATOM   4645 C CG2   . ILE B 1 78  ? -25.823 19.427  7.521   1.00 39.77  ? 78   ILE B CG2   1 
ATOM   4646 C CD1   . ILE B 1 78  ? -27.839 17.766  8.642   1.00 44.21  ? 78   ILE B CD1   1 
ATOM   4647 N N     . PRO B 1 79  ? -25.801 19.862  3.975   1.00 40.50  ? 79   PRO B N     1 
ATOM   4648 C CA    . PRO B 1 79  ? -24.869 20.758  3.306   1.00 39.62  ? 79   PRO B CA    1 
ATOM   4649 C C     . PRO B 1 79  ? -24.123 21.628  4.276   1.00 39.06  ? 79   PRO B C     1 
ATOM   4650 O O     . PRO B 1 79  ? -24.688 22.130  5.234   1.00 39.36  ? 79   PRO B O     1 
ATOM   4651 C CB    . PRO B 1 79  ? -25.776 21.620  2.437   1.00 41.22  ? 79   PRO B CB    1 
ATOM   4652 C CG    . PRO B 1 79  ? -27.090 21.601  3.097   1.00 40.77  ? 79   PRO B CG    1 
ATOM   4653 C CD    . PRO B 1 79  ? -27.186 20.188  3.528   1.00 40.28  ? 79   PRO B CD    1 
ATOM   4654 N N     . LEU B 1 80  ? -22.846 21.790  4.032   1.00 35.45  ? 80   LEU B N     1 
ATOM   4655 C CA    . LEU B 1 80  ? -22.042 22.609  4.881   1.00 38.32  ? 80   LEU B CA    1 
ATOM   4656 C C     . LEU B 1 80  ? -21.397 23.738  4.141   1.00 38.74  ? 80   LEU B C     1 
ATOM   4657 O O     . LEU B 1 80  ? -20.637 23.507  3.236   1.00 41.24  ? 80   LEU B O     1 
ATOM   4658 C CB    . LEU B 1 80  ? -20.931 21.795  5.511   1.00 44.31  ? 80   LEU B CB    1 
ATOM   4659 C CG    . LEU B 1 80  ? -21.144 20.571  6.373   1.00 45.78  ? 80   LEU B CG    1 
ATOM   4660 C CD1   . LEU B 1 80  ? -19.766 20.034  6.707   1.00 45.46  ? 80   LEU B CD1   1 
ATOM   4661 C CD2   . LEU B 1 80  ? -21.890 20.956  7.635   1.00 53.03  ? 80   LEU B CD2   1 
ATOM   4662 N N     . SER B 1 81  ? -21.685 24.957  4.528   1.00 35.91  ? 81   SER B N     1 
ATOM   4663 C CA    . SER B 1 81  ? -21.011 26.090  3.968   1.00 37.72  ? 81   SER B CA    1 
ATOM   4664 C C     . SER B 1 81  ? -19.829 26.405  4.869   1.00 36.09  ? 81   SER B C     1 
ATOM   4665 O O     . SER B 1 81  ? -19.711 25.840  5.928   1.00 35.78  ? 81   SER B O     1 
ATOM   4666 C CB    . SER B 1 81  ? -21.945 27.266  3.882   1.00 38.10  ? 81   SER B CB    1 
ATOM   4667 O OG    . SER B 1 81  ? -22.401 27.632  5.154   1.00 42.16  ? 81   SER B OG    1 
ATOM   4668 N N     . VAL B 1 82  ? -18.953 27.300  4.444   1.00 37.34  ? 82   VAL B N     1 
ATOM   4669 C CA    . VAL B 1 82  ? -17.730 27.580  5.185   1.00 36.85  ? 82   VAL B CA    1 
ATOM   4670 C C     . VAL B 1 82  ? -17.263 29.021  5.317   1.00 35.66  ? 82   VAL B C     1 
ATOM   4671 O O     . VAL B 1 82  ? -17.257 29.744  4.342   1.00 32.38  ? 82   VAL B O     1 
ATOM   4672 C CB    . VAL B 1 82  ? -16.491 26.848  4.567   1.00 37.62  ? 82   VAL B CB    1 
ATOM   4673 C CG1   . VAL B 1 82  ? -15.445 26.554  5.619   1.00 38.03  ? 82   VAL B CG1   1 
ATOM   4674 C CG2   . VAL B 1 82  ? -16.843 25.597  3.780   1.00 39.23  ? 82   VAL B CG2   1 
ATOM   4675 N N     . ILE B 1 83  ? -16.908 29.445  6.523   1.00 33.45  ? 83   ILE B N     1 
ATOM   4676 C CA    . ILE B 1 83  ? -16.251 30.762  6.731   1.00 36.78  ? 83   ILE B CA    1 
ATOM   4677 C C     . ILE B 1 83  ? -14.920 30.530  7.444   1.00 36.64  ? 83   ILE B C     1 
ATOM   4678 O O     . ILE B 1 83  ? -14.733 29.451  8.051   1.00 33.97  ? 83   ILE B O     1 
ATOM   4679 C CB    . ILE B 1 83  ? -17.186 31.709  7.505   1.00 38.99  ? 83   ILE B CB    1 
ATOM   4680 C CG1   . ILE B 1 83  ? -17.399 31.245  8.949   1.00 40.02  ? 83   ILE B CG1   1 
ATOM   4681 C CG2   . ILE B 1 83  ? -18.497 31.843  6.746   1.00 36.99  ? 83   ILE B CG2   1 
ATOM   4682 C CD1   . ILE B 1 83  ? -17.838 32.350  9.892   1.00 44.32  ? 83   ILE B CD1   1 
ATOM   4683 N N     . SER B 1 84  ? -14.041 31.512  7.329   1.00 35.28  ? 84   SER B N     1 
ATOM   4684 C CA    . SER B 1 84  ? -12.919 31.794  8.251   1.00 36.13  ? 84   SER B CA    1 
ATOM   4685 C C     . SER B 1 84  ? -13.353 32.846  9.290   1.00 32.77  ? 84   SER B C     1 
ATOM   4686 O O     . SER B 1 84  ? -13.628 32.486  10.427  1.00 37.33  ? 84   SER B O     1 
ATOM   4687 C CB    . SER B 1 84  ? -11.739 32.198  7.444   1.00 35.08  ? 84   SER B CB    1 
ATOM   4688 O OG    . SER B 1 84  ? -11.283 31.080  6.682   1.00 33.56  ? 84   SER B OG    1 
ATOM   4689 N N     . THR B 1 85  ? -13.470 34.105  8.911   1.00 35.54  ? 85   THR B N     1 
ATOM   4690 C CA    . THR B 1 85  ? -13.990 35.162  9.813   1.00 39.44  ? 85   THR B CA    1 
ATOM   4691 C C     . THR B 1 85  ? -15.351 35.667  9.304   1.00 41.44  ? 85   THR B C     1 
ATOM   4692 O O     . THR B 1 85  ? -15.970 36.432  10.035  1.00 44.46  ? 85   THR B O     1 
ATOM   4693 C CB    . THR B 1 85  ? -12.917 36.235  10.013  1.00 38.49  ? 85   THR B CB    1 
ATOM   4694 O OG1   . THR B 1 85  ? -12.428 36.628  8.724   1.00 40.44  ? 85   THR B OG1   1 
ATOM   4695 C CG2   . THR B 1 85  ? -11.790 35.732  10.894  1.00 37.31  ? 85   THR B CG2   1 
ATOM   4696 N N     . GLY B 1 86  ? -15.782 35.259  8.097   1.00 42.89  ? 86   GLY B N     1 
ATOM   4697 C CA    . GLY B 1 86  ? -17.094 35.598  7.500   1.00 42.31  ? 86   GLY B CA    1 
ATOM   4698 C C     . GLY B 1 86  ? -17.340 37.098  7.362   1.00 41.30  ? 86   GLY B C     1 
ATOM   4699 O O     . GLY B 1 86  ? -18.454 37.539  7.640   1.00 43.77  ? 86   GLY B O     1 
ATOM   4700 N N     . ARG B 1 87  ? -16.345 37.867  6.933   1.00 42.30  ? 87   ARG B N     1 
ATOM   4701 C CA    . ARG B 1 87  ? -16.475 39.329  6.706   1.00 42.25  ? 87   ARG B CA    1 
ATOM   4702 C C     . ARG B 1 87  ? -16.531 39.585  5.203   1.00 38.93  ? 87   ARG B C     1 
ATOM   4703 O O     . ARG B 1 87  ? -15.960 40.615  4.754   1.00 39.44  ? 87   ARG B O     1 
ATOM   4704 C CB    . ARG B 1 87  ? -15.280 40.032  7.341   1.00 45.80  ? 87   ARG B CB    1 
ATOM   4705 C CG    . ARG B 1 87  ? -15.152 39.778  8.831   1.00 47.51  ? 87   ARG B CG    1 
ATOM   4706 C CD    . ARG B 1 87  ? -16.004 40.781  9.561   1.00 50.42  ? 87   ARG B CD    1 
ATOM   4707 N NE    . ARG B 1 87  ? -15.703 40.800  10.976  1.00 51.73  ? 87   ARG B NE    1 
ATOM   4708 C CZ    . ARG B 1 87  ? -16.371 41.523  11.858  1.00 54.48  ? 87   ARG B CZ    1 
ATOM   4709 N NH1   . ARG B 1 87  ? -17.381 42.291  11.470  1.00 51.94  ? 87   ARG B NH1   1 
ATOM   4710 N NH2   . ARG B 1 87  ? -16.023 41.467  13.129  1.00 62.07  ? 87   ARG B NH2   1 
ATOM   4711 N N     . ASN B 1 88  ? -17.127 38.648  4.460   1.00 35.60  ? 88   ASN B N     1 
ATOM   4712 C CA    . ASN B 1 88  ? -17.179 38.679  2.975   1.00 37.12  ? 88   ASN B CA    1 
ATOM   4713 C C     . ASN B 1 88  ? -18.270 39.678  2.561   1.00 35.78  ? 88   ASN B C     1 
ATOM   4714 O O     . ASN B 1 88  ? -19.171 39.335  1.765   1.00 38.73  ? 88   ASN B O     1 
ATOM   4715 C CB    . ASN B 1 88  ? -17.320 37.269  2.386   1.00 35.27  ? 88   ASN B CB    1 
ATOM   4716 C CG    . ASN B 1 88  ? -16.599 37.134  1.060   1.00 34.54  ? 88   ASN B CG    1 
ATOM   4717 O OD1   . ASN B 1 88  ? -15.806 38.002  0.696   1.00 32.66  ? 88   ASN B OD1   1 
ATOM   4718 N ND2   . ASN B 1 88  ? -16.877 36.077  0.319   1.00 32.48  ? 88   ASN B ND2   1 
ATOM   4719 N N     . ASN B 1 89  ? -18.142 40.903  3.056   1.00 37.95  ? 89   ASN B N     1 
ATOM   4720 C CA    . ASN B 1 89  ? -19.136 41.995  2.927   1.00 38.64  ? 89   ASN B CA    1 
ATOM   4721 C C     . ASN B 1 89  ? -19.046 42.577  1.514   1.00 36.74  ? 89   ASN B C     1 
ATOM   4722 O O     . ASN B 1 89  ? -17.930 42.899  1.052   1.00 34.54  ? 89   ASN B O     1 
ATOM   4723 C CB    . ASN B 1 89  ? -18.944 43.027  4.033   1.00 40.40  ? 89   ASN B CB    1 
ATOM   4724 C CG    . ASN B 1 89  ? -19.173 42.441  5.409   1.00 41.35  ? 89   ASN B CG    1 
ATOM   4725 O OD1   . ASN B 1 89  ? -19.754 41.366  5.538   1.00 43.23  ? 89   ASN B OD1   1 
ATOM   4726 N ND2   . ASN B 1 89  ? -18.713 43.137  6.435   1.00 44.95  ? 89   ASN B ND2   1 
ATOM   4727 N N     . GLY B 1 90  ? -20.192 42.630  0.844   1.00 36.89  ? 90   GLY B N     1 
ATOM   4728 C CA    . GLY B 1 90  ? -20.322 42.886  -0.598  1.00 37.74  ? 90   GLY B CA    1 
ATOM   4729 C C     . GLY B 1 90  ? -20.552 41.601  -1.365  1.00 37.78  ? 90   GLY B C     1 
ATOM   4730 O O     . GLY B 1 90  ? -20.868 41.700  -2.572  1.00 35.60  ? 90   GLY B O     1 
ATOM   4731 N N     . TYR B 1 91  ? -20.345 40.441  -0.724  1.00 35.11  ? 91   TYR B N     1 
ATOM   4732 C CA    . TYR B 1 91  ? -20.360 39.120  -1.405  1.00 34.90  ? 91   TYR B CA    1 
ATOM   4733 C C     . TYR B 1 91  ? -21.279 38.125  -0.692  1.00 37.56  ? 91   TYR B C     1 
ATOM   4734 O O     . TYR B 1 91  ? -21.445 37.017  -1.224  1.00 35.41  ? 91   TYR B O     1 
ATOM   4735 C CB    . TYR B 1 91  ? -18.943 38.567  -1.553  1.00 36.10  ? 91   TYR B CB    1 
ATOM   4736 C CG    . TYR B 1 91  ? -18.023 39.429  -2.372  1.00 33.60  ? 91   TYR B CG    1 
ATOM   4737 C CD1   . TYR B 1 91  ? -18.281 39.682  -3.706  1.00 39.63  ? 91   TYR B CD1   1 
ATOM   4738 C CD2   . TYR B 1 91  ? -16.894 39.993  -1.816  1.00 36.75  ? 91   TYR B CD2   1 
ATOM   4739 C CE1   . TYR B 1 91  ? -17.444 40.481  -4.468  1.00 37.07  ? 91   TYR B CE1   1 
ATOM   4740 C CE2   . TYR B 1 91  ? -16.042 40.793  -2.558  1.00 36.60  ? 91   TYR B CE2   1 
ATOM   4741 C CZ    . TYR B 1 91  ? -16.312 41.030  -3.895  1.00 39.01  ? 91   TYR B CZ    1 
ATOM   4742 O OH    . TYR B 1 91  ? -15.475 41.813  -4.644  1.00 38.43  ? 91   TYR B OH    1 
ATOM   4743 N N     . GLY B 1 92  ? -21.920 38.536  0.409   1.00 40.27  ? 92   GLY B N     1 
ATOM   4744 C CA    . GLY B 1 92  ? -22.900 37.701  1.133   1.00 40.95  ? 92   GLY B CA    1 
ATOM   4745 C C     . GLY B 1 92  ? -22.553 37.551  2.601   1.00 38.77  ? 92   GLY B C     1 
ATOM   4746 O O     . GLY B 1 92  ? -23.326 36.893  3.303   1.00 37.48  ? 92   GLY B O     1 
ATOM   4747 N N     . GLY B 1 93  ? -21.432 38.128  3.045   1.00 41.26  ? 93   GLY B N     1 
ATOM   4748 C CA    . GLY B 1 93  ? -20.955 38.034  4.437   1.00 42.00  ? 93   GLY B CA    1 
ATOM   4749 C C     . GLY B 1 93  ? -20.722 36.580  4.780   1.00 42.32  ? 93   GLY B C     1 
ATOM   4750 O O     . GLY B 1 93  ? -20.107 35.890  3.938   1.00 47.24  ? 93   GLY B O     1 
ATOM   4751 N N     . SER B 1 94  ? -21.251 36.093  5.904   1.00 38.92  ? 94   SER B N     1 
ATOM   4752 C CA    . SER B 1 94  ? -21.042 34.686  6.336   1.00 41.26  ? 94   SER B CA    1 
ATOM   4753 C C     . SER B 1 94  ? -22.256 33.856  5.938   1.00 38.85  ? 94   SER B C     1 
ATOM   4754 O O     . SER B 1 94  ? -22.403 32.715  6.435   1.00 39.64  ? 94   SER B O     1 
ATOM   4755 C CB    . SER B 1 94  ? -20.694 34.585  7.815   1.00 42.31  ? 94   SER B CB    1 
ATOM   4756 O OG    . SER B 1 94  ? -21.656 35.238  8.606   1.00 52.38  ? 94   SER B OG    1 
ATOM   4757 N N     . ALA B 1 95  ? -23.083 34.388  5.034   1.00 38.07  ? 95   ALA B N     1 
ATOM   4758 C CA    . ALA B 1 95  ? -24.338 33.735  4.599   1.00 38.80  ? 95   ALA B CA    1 
ATOM   4759 C C     . ALA B 1 95  ? -24.035 32.672  3.546   1.00 39.33  ? 95   ALA B C     1 
ATOM   4760 O O     . ALA B 1 95  ? -23.275 32.911  2.614   1.00 40.16  ? 95   ALA B O     1 
ATOM   4761 C CB    . ALA B 1 95  ? -25.308 34.766  4.063   1.00 40.27  ? 95   ALA B CB    1 
ATOM   4762 N N     . PRO B 1 96  ? -24.667 31.485  3.633   1.00 38.01  ? 96   PRO B N     1 
ATOM   4763 C CA    . PRO B 1 96  ? -24.418 30.419  2.677   1.00 38.47  ? 96   PRO B CA    1 
ATOM   4764 C C     . PRO B 1 96  ? -25.117 30.698  1.345   1.00 39.97  ? 96   PRO B C     1 
ATOM   4765 O O     . PRO B 1 96  ? -26.189 31.273  1.357   1.00 39.55  ? 96   PRO B O     1 
ATOM   4766 C CB    . PRO B 1 96  ? -25.020 29.179  3.352   1.00 38.55  ? 96   PRO B CB    1 
ATOM   4767 C CG    . PRO B 1 96  ? -26.135 29.735  4.207   1.00 35.76  ? 96   PRO B CG    1 
ATOM   4768 C CD    . PRO B 1 96  ? -25.669 31.109  4.645   1.00 37.03  ? 96   PRO B CD    1 
ATOM   4769 N N     . ARG B 1 97  ? -24.505 30.260  0.248   1.00 34.77  ? 97   ARG B N     1 
ATOM   4770 C CA    . ARG B 1 97  ? -25.109 30.330  -1.096  1.00 35.16  ? 97   ARG B CA    1 
ATOM   4771 C C     . ARG B 1 97  ? -26.392 29.496  -1.048  1.00 38.39  ? 97   ARG B C     1 
ATOM   4772 O O     . ARG B 1 97  ? -27.459 30.050  -1.398  1.00 39.17  ? 97   ARG B O     1 
ATOM   4773 C CB    . ARG B 1 97  ? -24.133 29.829  -2.160  1.00 33.24  ? 97   ARG B CB    1 
ATOM   4774 C CG    . ARG B 1 97  ? -24.765 29.678  -3.533  1.00 32.84  ? 97   ARG B CG    1 
ATOM   4775 C CD    . ARG B 1 97  ? -25.428 30.954  -4.019  1.00 34.50  ? 97   ARG B CD    1 
ATOM   4776 N NE    . ARG B 1 97  ? -26.246 30.668  -5.191  1.00 35.98  ? 97   ARG B NE    1 
ATOM   4777 C CZ    . ARG B 1 97  ? -27.563 30.459  -5.194  1.00 36.49  ? 97   ARG B CZ    1 
ATOM   4778 N NH1   . ARG B 1 97  ? -28.258 30.530  -4.076  1.00 38.80  ? 97   ARG B NH1   1 
ATOM   4779 N NH2   . ARG B 1 97  ? -28.192 30.195  -6.331  1.00 34.57  ? 97   ARG B NH2   1 
ATOM   4780 N N     . LEU B 1 98  ? -26.286 28.238  -0.595  1.00 39.58  ? 98   LEU B N     1 
ATOM   4781 C CA    . LEU B 1 98  ? -27.450 27.327  -0.392  1.00 40.28  ? 98   LEU B CA    1 
ATOM   4782 C C     . LEU B 1 98  ? -28.163 27.712  0.908   1.00 40.24  ? 98   LEU B C     1 
ATOM   4783 O O     . LEU B 1 98  ? -27.622 27.436  2.007   1.00 40.79  ? 98   LEU B O     1 
ATOM   4784 C CB    . LEU B 1 98  ? -27.004 25.864  -0.345  1.00 39.48  ? 98   LEU B CB    1 
ATOM   4785 C CG    . LEU B 1 98  ? -28.141 24.849  -0.237  1.00 41.41  ? 98   LEU B CG    1 
ATOM   4786 C CD1   . LEU B 1 98  ? -29.092 24.970  -1.413  1.00 45.04  ? 98   LEU B CD1   1 
ATOM   4787 C CD2   . LEU B 1 98  ? -27.599 23.436  -0.133  1.00 43.79  ? 98   LEU B CD2   1 
ATOM   4788 N N     . SER B 1 99  ? -29.322 28.350  0.787   1.00 37.75  ? 99   SER B N     1 
ATOM   4789 C CA    . SER B 1 99  ? -30.122 28.786  1.955   1.00 40.94  ? 99   SER B CA    1 
ATOM   4790 C C     . SER B 1 99  ? -30.444 27.535  2.783   1.00 41.79  ? 99   SER B C     1 
ATOM   4791 O O     . SER B 1 99  ? -30.743 26.472  2.173   1.00 43.38  ? 99   SER B O     1 
ATOM   4792 C CB    . SER B 1 99  ? -31.347 29.539  1.547   1.00 41.12  ? 99   SER B CB    1 
ATOM   4793 O OG    . SER B 1 99  ? -31.793 30.334  2.637   1.00 44.42  ? 99   SER B OG    1 
ATOM   4794 N N     . GLY B 1 100 ? -30.250 27.582  4.086   1.00 39.84  ? 100  GLY B N     1 
ATOM   4795 C CA    . GLY B 1 100 ? -30.472 26.428  4.920   1.00 39.94  ? 100  GLY B CA    1 
ATOM   4796 C C     . GLY B 1 100 ? -29.245 25.662  5.322   1.00 44.02  ? 100  GLY B C     1 
ATOM   4797 O O     . GLY B 1 100 ? -29.321 24.761  6.119   1.00 44.65  ? 100  GLY B O     1 
ATOM   4798 N N     . ALA B 1 101 ? -28.107 25.985  4.742   1.00 44.29  ? 101  ALA B N     1 
ATOM   4799 C CA    . ALA B 1 101 ? -26.893 25.235  5.043   1.00 40.84  ? 101  ALA B CA    1 
ATOM   4800 C C     . ALA B 1 101 ? -26.357 25.433  6.427   1.00 38.69  ? 101  ALA B C     1 
ATOM   4801 O O     . ALA B 1 101 ? -26.619 26.427  7.069   1.00 37.17  ? 101  ALA B O     1 
ATOM   4802 C CB    . ALA B 1 101 ? -25.796 25.539  4.051   1.00 39.73  ? 101  ALA B CB    1 
ATOM   4803 N N     . VAL B 1 102 ? -25.590 24.467  6.874   1.00 39.02  ? 102  VAL B N     1 
ATOM   4804 C CA    . VAL B 1 102 ? -24.950 24.602  8.148   1.00 38.76  ? 102  VAL B CA    1 
ATOM   4805 C C     . VAL B 1 102 ? -23.588 25.256  7.921   1.00 41.39  ? 102  VAL B C     1 
ATOM   4806 O O     . VAL B 1 102 ? -22.779 24.763  7.177   1.00 37.90  ? 102  VAL B O     1 
ATOM   4807 C CB    . VAL B 1 102 ? -24.800 23.253  8.854   1.00 34.02  ? 102  VAL B CB    1 
ATOM   4808 C CG1   . VAL B 1 102 ? -23.970 23.406  10.103  1.00 35.25  ? 102  VAL B CG1   1 
ATOM   4809 C CG2   . VAL B 1 102 ? -26.150 22.677  9.200   1.00 37.69  ? 102  VAL B CG2   1 
ATOM   4810 N N     . VAL B 1 103 ? -23.346 26.373  8.569   1.00 40.70  ? 103  VAL B N     1 
ATOM   4811 C CA    . VAL B 1 103 ? -22.083 27.045  8.424   1.00 40.99  ? 103  VAL B CA    1 
ATOM   4812 C C     . VAL B 1 103 ? -20.978 26.433  9.258   1.00 46.12  ? 103  VAL B C     1 
ATOM   4813 O O     . VAL B 1 103 ? -21.148 26.243  10.446  1.00 42.47  ? 103  VAL B O     1 
ATOM   4814 C CB    . VAL B 1 103 ? -22.198 28.530  8.791   1.00 40.48  ? 103  VAL B CB    1 
ATOM   4815 C CG1   . VAL B 1 103 ? -20.878 29.262  8.636   1.00 42.08  ? 103  VAL B CG1   1 
ATOM   4816 C CG2   . VAL B 1 103 ? -23.284 29.208  7.986   1.00 38.54  ? 103  VAL B CG2   1 
ATOM   4817 N N     . VAL B 1 104 ? -19.869 26.066  8.633   1.00 41.26  ? 104  VAL B N     1 
ATOM   4818 C CA    . VAL B 1 104 ? -18.681 25.623  9.406   1.00 35.78  ? 104  VAL B CA    1 
ATOM   4819 C C     . VAL B 1 104 ? -17.837 26.866  9.653   1.00 38.01  ? 104  VAL B C     1 
ATOM   4820 O O     . VAL B 1 104 ? -17.369 27.507  8.690   1.00 33.32  ? 104  VAL B O     1 
ATOM   4821 C CB    . VAL B 1 104 ? -17.910 24.491  8.713   1.00 34.29  ? 104  VAL B CB    1 
ATOM   4822 C CG1   . VAL B 1 104 ? -16.730 24.047  9.549   1.00 32.84  ? 104  VAL B CG1   1 
ATOM   4823 C CG2   . VAL B 1 104 ? -18.831 23.327  8.399   1.00 33.61  ? 104  VAL B CG2   1 
ATOM   4824 N N     . ASN B 1 105 ? -17.715 27.228  10.923  1.00 35.97  ? 105  ASN B N     1 
ATOM   4825 C CA    . ASN B 1 105 ? -16.994 28.432  11.364  1.00 35.99  ? 105  ASN B CA    1 
ATOM   4826 C C     . ASN B 1 105 ? -15.596 27.981  11.791  1.00 39.79  ? 105  ASN B C     1 
ATOM   4827 O O     . ASN B 1 105 ? -15.423 27.623  12.980  1.00 35.85  ? 105  ASN B O     1 
ATOM   4828 C CB    . ASN B 1 105 ? -17.781 29.125  12.473  1.00 41.18  ? 105  ASN B CB    1 
ATOM   4829 C CG    . ASN B 1 105 ? -17.079 30.354  12.990  1.00 39.37  ? 105  ASN B CG    1 
ATOM   4830 O OD1   . ASN B 1 105 ? -15.913 30.596  12.688  1.00 44.03  ? 105  ASN B OD1   1 
ATOM   4831 N ND2   . ASN B 1 105 ? -17.797 31.133  13.762  1.00 40.00  ? 105  ASN B ND2   1 
ATOM   4832 N N     . THR B 1 106 ? -14.631 28.026  10.866  1.00 35.91  ? 106  THR B N     1 
ATOM   4833 C CA    . THR B 1 106 ? -13.257 27.507  11.056  1.00 35.40  ? 106  THR B CA    1 
ATOM   4834 C C     . THR B 1 106 ? -12.469 28.488  11.939  1.00 36.31  ? 106  THR B C     1 
ATOM   4835 O O     . THR B 1 106 ? -11.623 28.007  12.736  1.00 41.85  ? 106  THR B O     1 
ATOM   4836 C CB    . THR B 1 106 ? -12.609 27.222  9.689   1.00 35.12  ? 106  THR B CB    1 
ATOM   4837 O OG1   . THR B 1 106 ? -12.547 28.444  8.961   1.00 32.55  ? 106  THR B OG1   1 
ATOM   4838 C CG2   . THR B 1 106 ? -13.351 26.184  8.876   1.00 35.85  ? 106  THR B CG2   1 
ATOM   4839 N N     . GLY B 1 107 ? -12.784 29.785  11.851  1.00 33.60  ? 107  GLY B N     1 
ATOM   4840 C CA    . GLY B 1 107 ? -12.030 30.901  12.462  1.00 37.13  ? 107  GLY B CA    1 
ATOM   4841 C C     . GLY B 1 107 ? -12.263 31.053  13.967  1.00 37.20  ? 107  GLY B C     1 
ATOM   4842 O O     . GLY B 1 107 ? -11.375 31.604  14.640  1.00 41.77  ? 107  GLY B O     1 
ATOM   4843 N N     . GLU B 1 108 ? -13.394 30.606  14.507  1.00 36.81  ? 108  GLU B N     1 
ATOM   4844 C CA    . GLU B 1 108 ? -13.701 30.871  15.936  1.00 40.70  ? 108  GLU B CA    1 
ATOM   4845 C C     . GLU B 1 108 ? -12.591 30.269  16.814  1.00 37.85  ? 108  GLU B C     1 
ATOM   4846 O O     . GLU B 1 108 ? -11.994 31.026  17.571  1.00 36.60  ? 108  GLU B O     1 
ATOM   4847 C CB    . GLU B 1 108 ? -15.075 30.361  16.357  1.00 44.97  ? 108  GLU B CB    1 
ATOM   4848 C CG    . GLU B 1 108 ? -15.377 30.705  17.813  1.00 46.95  ? 108  GLU B CG    1 
ATOM   4849 C CD    . GLU B 1 108 ? -16.761 30.315  18.301  1.00 52.86  ? 108  GLU B CD    1 
ATOM   4850 O OE1   . GLU B 1 108 ? -17.517 29.697  17.522  1.00 46.15  ? 108  GLU B OE1   1 
ATOM   4851 O OE2   . GLU B 1 108 ? -17.086 30.646  19.465  1.00 58.93  ? 108  GLU B OE2   1 
ATOM   4852 N N     . ARG B 1 109 ? -12.298 28.979  16.660  1.00 40.48  ? 109  ARG B N     1 
ATOM   4853 C CA    . ARG B 1 109 ? -11.323 28.219  17.497  1.00 38.85  ? 109  ARG B CA    1 
ATOM   4854 C C     . ARG B 1 109 ? -10.003 27.975  16.745  1.00 39.13  ? 109  ARG B C     1 
ATOM   4855 O O     . ARG B 1 109 ? -8.939  27.909  17.410  1.00 34.47  ? 109  ARG B O     1 
ATOM   4856 C CB    . ARG B 1 109 ? -11.983 26.914  17.936  1.00 36.19  ? 109  ARG B CB    1 
ATOM   4857 C CG    . ARG B 1 109 ? -13.208 27.135  18.810  1.00 38.74  ? 109  ARG B CG    1 
ATOM   4858 C CD    . ARG B 1 109 ? -14.055 25.891  18.948  1.00 38.39  ? 109  ARG B CD    1 
ATOM   4859 N NE    . ARG B 1 109 ? -13.614 24.990  19.995  1.00 43.94  ? 109  ARG B NE    1 
ATOM   4860 C CZ    . ARG B 1 109 ? -14.075 23.748  20.168  1.00 44.28  ? 109  ARG B CZ    1 
ATOM   4861 N NH1   . ARG B 1 109 ? -14.997 23.257  19.360  1.00 44.52  ? 109  ARG B NH1   1 
ATOM   4862 N NH2   . ARG B 1 109 ? -13.612 22.994  21.149  1.00 45.32  ? 109  ARG B NH2   1 
ATOM   4863 N N     . MET B 1 110 ? -10.015 27.886  15.411  1.00 37.34  ? 110  MET B N     1 
ATOM   4864 C CA    . MET B 1 110 ? -8.755  27.671  14.649  1.00 35.65  ? 110  MET B CA    1 
ATOM   4865 C C     . MET B 1 110 ? -8.214  29.029  14.211  1.00 38.33  ? 110  MET B C     1 
ATOM   4866 O O     . MET B 1 110 ? -8.387  29.423  13.023  1.00 35.24  ? 110  MET B O     1 
ATOM   4867 C CB    . MET B 1 110 ? -8.962  26.710  13.471  1.00 36.94  ? 110  MET B CB    1 
ATOM   4868 C CG    . MET B 1 110 ? -9.582  25.404  13.899  1.00 35.64  ? 110  MET B CG    1 
ATOM   4869 S SD    . MET B 1 110 ? -10.075 24.310  12.538  1.00 40.27  ? 110  MET B SD    1 
ATOM   4870 C CE    . MET B 1 110 ? -8.471  23.894  11.867  1.00 36.12  ? 110  MET B CE    1 
ATOM   4871 N N     . ASN B 1 111 ? -7.532  29.704  15.145  1.00 35.19  ? 111  ASN B N     1 
ATOM   4872 C CA    . ASN B 1 111 ? -7.206  31.141  15.046  1.00 34.18  ? 111  ASN B CA    1 
ATOM   4873 C C     . ASN B 1 111 ? -5.750  31.386  15.428  1.00 34.89  ? 111  ASN B C     1 
ATOM   4874 O O     . ASN B 1 111 ? -5.417  32.543  15.728  1.00 39.52  ? 111  ASN B O     1 
ATOM   4875 C CB    . ASN B 1 111 ? -8.160  31.954  15.918  1.00 37.55  ? 111  ASN B CB    1 
ATOM   4876 C CG    . ASN B 1 111 ? -8.059  31.610  17.390  1.00 40.25  ? 111  ASN B CG    1 
ATOM   4877 O OD1   . ASN B 1 111 ? -7.361  30.676  17.783  1.00 36.66  ? 111  ASN B OD1   1 
ATOM   4878 N ND2   . ASN B 1 111 ? -8.759  32.365  18.215  1.00 43.84  ? 111  ASN B ND2   1 
ATOM   4879 N N     . ARG B 1 112 ? -4.893  30.368  15.369  1.00 36.47  ? 112  ARG B N     1 
ATOM   4880 C CA    . ARG B 1 112 ? -3.492  30.500  15.835  1.00 39.21  ? 112  ARG B CA    1 
ATOM   4881 C C     . ARG B 1 112 ? -2.580  30.800  14.655  1.00 35.91  ? 112  ARG B C     1 
ATOM   4882 O O     . ARG B 1 112 ? -2.746  30.200  13.568  1.00 33.98  ? 112  ARG B O     1 
ATOM   4883 C CB    . ARG B 1 112 ? -3.048  29.244  16.584  1.00 45.22  ? 112  ARG B CB    1 
ATOM   4884 C CG    . ARG B 1 112 ? -4.165  28.628  17.410  1.00 53.61  ? 112  ARG B CG    1 
ATOM   4885 C CD    . ARG B 1 112 ? -3.681  27.572  18.379  1.00 63.81  ? 112  ARG B CD    1 
ATOM   4886 N NE    . ARG B 1 112 ? -4.539  26.396  18.279  1.00 72.59  ? 112  ARG B NE    1 
ATOM   4887 C CZ    . ARG B 1 112 ? -4.149  25.186  17.897  1.00 77.22  ? 112  ARG B CZ    1 
ATOM   4888 N NH1   . ARG B 1 112 ? -2.884  24.943  17.589  1.00 81.21  ? 112  ARG B NH1   1 
ATOM   4889 N NH2   . ARG B 1 112 ? -5.035  24.208  17.849  1.00 81.09  ? 112  ARG B NH2   1 
ATOM   4890 N N     . ILE B 1 113 ? -1.630  31.694  14.877  1.00 33.11  ? 113  ILE B N     1 
ATOM   4891 C CA    . ILE B 1 113 ? -0.416  31.798  14.024  1.00 35.49  ? 113  ILE B CA    1 
ATOM   4892 C C     . ILE B 1 113 ? 0.475   30.598  14.364  1.00 34.55  ? 113  ILE B C     1 
ATOM   4893 O O     . ILE B 1 113 ? 0.904   30.491  15.521  1.00 31.46  ? 113  ILE B O     1 
ATOM   4894 C CB    . ILE B 1 113 ? 0.238   33.176  14.229  1.00 35.98  ? 113  ILE B CB    1 
ATOM   4895 C CG1   . ILE B 1 113 ? -0.784  34.275  13.929  1.00 38.33  ? 113  ILE B CG1   1 
ATOM   4896 C CG2   . ILE B 1 113 ? 1.485   33.311  13.372  1.00 36.30  ? 113  ILE B CG2   1 
ATOM   4897 C CD1   . ILE B 1 113 ? -0.302  35.672  14.225  1.00 40.23  ? 113  ILE B CD1   1 
ATOM   4898 N N     . LEU B 1 114 ? 0.659   29.657  13.435  1.00 33.94  ? 114  LEU B N     1 
ATOM   4899 C CA    . LEU B 1 114 ? 1.295   28.360  13.757  1.00 35.01  ? 114  LEU B CA    1 
ATOM   4900 C C     . LEU B 1 114 ? 2.808   28.534  13.676  1.00 34.35  ? 114  LEU B C     1 
ATOM   4901 O O     . LEU B 1 114 ? 3.509   27.832  14.392  1.00 31.34  ? 114  LEU B O     1 
ATOM   4902 C CB    . LEU B 1 114 ? 0.813   27.271  12.797  1.00 38.70  ? 114  LEU B CB    1 
ATOM   4903 C CG    . LEU B 1 114 ? -0.648  26.856  12.948  1.00 38.22  ? 114  LEU B CG    1 
ATOM   4904 C CD1   . LEU B 1 114 ? -0.999  25.800  11.925  1.00 37.34  ? 114  LEU B CD1   1 
ATOM   4905 C CD2   . LEU B 1 114 ? -0.948  26.338  14.348  1.00 39.94  ? 114  LEU B CD2   1 
ATOM   4906 N N     . GLU B 1 115 ? 3.284   29.437  12.827  1.00 35.46  ? 115  GLU B N     1 
ATOM   4907 C CA    . GLU B 1 115 ? 4.732   29.601  12.555  1.00 36.08  ? 115  GLU B CA    1 
ATOM   4908 C C     . GLU B 1 115 ? 4.921   30.897  11.788  1.00 36.01  ? 115  GLU B C     1 
ATOM   4909 O O     . GLU B 1 115 ? 4.114   31.169  10.874  1.00 31.44  ? 115  GLU B O     1 
ATOM   4910 C CB    . GLU B 1 115 ? 5.264   28.425  11.742  1.00 44.75  ? 115  GLU B CB    1 
ATOM   4911 C CG    . GLU B 1 115 ? 6.774   28.379  11.613  1.00 48.95  ? 115  GLU B CG    1 
ATOM   4912 C CD    . GLU B 1 115 ? 7.260   27.384  10.569  1.00 55.56  ? 115  GLU B CD    1 
ATOM   4913 O OE1   . GLU B 1 115 ? 6.451   26.521  10.144  1.00 58.37  ? 115  GLU B OE1   1 
ATOM   4914 O OE2   . GLU B 1 115 ? 8.451   27.470  10.177  1.00 56.80  ? 115  GLU B OE2   1 
ATOM   4915 N N     . VAL B 1 116 ? 5.912   31.677  12.200  1.00 30.91  ? 116  VAL B N     1 
ATOM   4916 C CA    . VAL B 1 116 ? 6.492   32.766  11.380  1.00 33.88  ? 116  VAL B CA    1 
ATOM   4917 C C     . VAL B 1 116 ? 7.984   32.527  11.304  1.00 34.76  ? 116  VAL B C     1 
ATOM   4918 O O     . VAL B 1 116 ? 8.570   32.358  12.367  1.00 36.42  ? 116  VAL B O     1 
ATOM   4919 C CB    . VAL B 1 116 ? 6.213   34.152  11.959  1.00 33.38  ? 116  VAL B CB    1 
ATOM   4920 C CG1   . VAL B 1 116 ? 7.014   35.194  11.200  1.00 34.74  ? 116  VAL B CG1   1 
ATOM   4921 C CG2   . VAL B 1 116 ? 4.733   34.454  11.931  1.00 32.47  ? 116  VAL B CG2   1 
ATOM   4922 N N     . ASP B 1 117 ? 8.532   32.523  10.089  1.00 32.74  ? 117  ASP B N     1 
ATOM   4923 C CA    . ASP B 1 117 ? 9.984   32.509  9.838   1.00 32.68  ? 117  ASP B CA    1 
ATOM   4924 C C     . ASP B 1 117 ? 10.359  33.894  9.314   1.00 35.56  ? 117  ASP B C     1 
ATOM   4925 O O     . ASP B 1 117 ? 9.982   34.228  8.161   1.00 36.03  ? 117  ASP B O     1 
ATOM   4926 C CB    . ASP B 1 117 ? 10.353  31.347  8.911   1.00 33.44  ? 117  ASP B CB    1 
ATOM   4927 C CG    . ASP B 1 117 ? 11.849  31.116  8.735   1.00 35.16  ? 117  ASP B CG    1 
ATOM   4928 O OD1   . ASP B 1 117 ? 12.593  32.082  8.497   1.00 33.40  ? 117  ASP B OD1   1 
ATOM   4929 O OD2   . ASP B 1 117 ? 12.250  29.967  8.786   1.00 40.33  ? 117  ASP B OD2   1 
ATOM   4930 N N     . GLU B 1 118 ? 11.104  34.667  10.111  1.00 33.49  ? 118  GLU B N     1 
ATOM   4931 C CA    . GLU B 1 118 ? 11.464  36.070  9.773   1.00 34.27  ? 118  GLU B CA    1 
ATOM   4932 C C     . GLU B 1 118 ? 12.439  36.096  8.595   1.00 34.30  ? 118  GLU B C     1 
ATOM   4933 O O     . GLU B 1 118 ? 12.218  36.872  7.637   1.00 38.25  ? 118  GLU B O     1 
ATOM   4934 C CB    . GLU B 1 118 ? 12.046  36.756  11.008  1.00 36.73  ? 118  GLU B CB    1 
ATOM   4935 C CG    . GLU B 1 118 ? 12.311  38.236  10.816  1.00 35.70  ? 118  GLU B CG    1 
ATOM   4936 C CD    . GLU B 1 118 ? 12.408  39.049  12.105  1.00 38.77  ? 118  GLU B CD    1 
ATOM   4937 O OE1   . GLU B 1 118 ? 12.479  38.427  13.201  1.00 36.17  ? 118  GLU B OE1   1 
ATOM   4938 O OE2   . GLU B 1 118 ? 12.347  40.318  12.017  1.00 43.19  ? 118  GLU B OE2   1 
ATOM   4939 N N     . LYS B 1 119 ? 13.510  35.317  8.678   1.00 32.77  ? 119  LYS B N     1 
ATOM   4940 C CA    . LYS B 1 119 ? 14.585  35.266  7.652   1.00 39.09  ? 119  LYS B CA    1 
ATOM   4941 C C     . LYS B 1 119 ? 14.038  34.836  6.273   1.00 32.09  ? 119  LYS B C     1 
ATOM   4942 O O     . LYS B 1 119 ? 14.491  35.395  5.274   1.00 31.83  ? 119  LYS B O     1 
ATOM   4943 C CB    . LYS B 1 119 ? 15.732  34.343  8.088   1.00 45.40  ? 119  LYS B CB    1 
ATOM   4944 C CG    . LYS B 1 119 ? 16.562  34.792  9.288   1.00 62.39  ? 119  LYS B CG    1 
ATOM   4945 C CD    . LYS B 1 119 ? 17.667  33.806  9.671   1.00 72.17  ? 119  LYS B CD    1 
ATOM   4946 C CE    . LYS B 1 119 ? 18.511  34.262  10.851  1.00 74.47  ? 119  LYS B CE    1 
ATOM   4947 N NZ    . LYS B 1 119 ? 19.550  33.264  11.198  1.00 74.54  ? 119  LYS B NZ    1 
ATOM   4948 N N     . LEU B 1 120 ? 13.139  33.855  6.211   1.00 31.39  ? 120  LEU B N     1 
ATOM   4949 C CA    . LEU B 1 120 ? 12.653  33.274  4.922   1.00 32.96  ? 120  LEU B CA    1 
ATOM   4950 C C     . LEU B 1 120 ? 11.310  33.898  4.542   1.00 31.48  ? 120  LEU B C     1 
ATOM   4951 O O     . LEU B 1 120 ? 10.874  33.652  3.398   1.00 33.21  ? 120  LEU B O     1 
ATOM   4952 C CB    . LEU B 1 120 ? 12.587  31.744  5.020   1.00 28.71  ? 120  LEU B CB    1 
ATOM   4953 C CG    . LEU B 1 120 ? 13.951  31.071  5.157   1.00 31.09  ? 120  LEU B CG    1 
ATOM   4954 C CD1   . LEU B 1 120 ? 13.846  29.554  5.115   1.00 30.67  ? 120  LEU B CD1   1 
ATOM   4955 C CD2   . LEU B 1 120 ? 14.883  31.549  4.067   1.00 33.03  ? 120  LEU B CD2   1 
ATOM   4956 N N     . GLY B 1 121 ? 10.709  34.677  5.455   1.00 31.63  ? 121  GLY B N     1 
ATOM   4957 C CA    . GLY B 1 121 ? 9.572   35.579  5.187   1.00 29.65  ? 121  GLY B CA    1 
ATOM   4958 C C     . GLY B 1 121 ? 8.281   34.823  4.886   1.00 29.12  ? 121  GLY B C     1 
ATOM   4959 O O     . GLY B 1 121 ? 7.816   34.870  3.739   1.00 28.76  ? 121  GLY B O     1 
ATOM   4960 N N     . TYR B 1 122 ? 7.744   34.086  5.849   1.00 26.63  ? 122  TYR B N     1 
ATOM   4961 C CA    . TYR B 1 122 ? 6.446   33.398  5.696   1.00 30.09  ? 122  TYR B CA    1 
ATOM   4962 C C     . TYR B 1 122 ? 5.812   33.206  7.054   1.00 31.80  ? 122  TYR B C     1 
ATOM   4963 O O     . TYR B 1 122 ? 6.527   33.300  8.073   1.00 33.84  ? 122  TYR B O     1 
ATOM   4964 C CB    . TYR B 1 122 ? 6.576   32.042  4.993   1.00 31.17  ? 122  TYR B CB    1 
ATOM   4965 C CG    . TYR B 1 122 ? 7.264   30.938  5.756   1.00 31.75  ? 122  TYR B CG    1 
ATOM   4966 C CD1   . TYR B 1 122 ? 6.576   30.176  6.685   1.00 34.72  ? 122  TYR B CD1   1 
ATOM   4967 C CD2   . TYR B 1 122 ? 8.578   30.590  5.474   1.00 31.72  ? 122  TYR B CD2   1 
ATOM   4968 C CE1   . TYR B 1 122 ? 7.192   29.130  7.352   1.00 36.89  ? 122  TYR B CE1   1 
ATOM   4969 C CE2   . TYR B 1 122 ? 9.206   29.544  6.122   1.00 32.46  ? 122  TYR B CE2   1 
ATOM   4970 C CZ    . TYR B 1 122 ? 8.511   28.819  7.073   1.00 36.00  ? 122  TYR B CZ    1 
ATOM   4971 O OH    . TYR B 1 122 ? 9.122   27.783  7.717   1.00 37.47  ? 122  TYR B OH    1 
ATOM   4972 N N     . ALA B 1 123 ? 4.510   32.915  7.015   1.00 31.30  ? 123  ALA B N     1 
ATOM   4973 C CA    . ALA B 1 123 ? 3.692   32.462  8.151   1.00 28.89  ? 123  ALA B CA    1 
ATOM   4974 C C     . ALA B 1 123 ? 2.894   31.237  7.706   1.00 30.04  ? 123  ALA B C     1 
ATOM   4975 O O     . ALA B 1 123 ? 2.592   31.067  6.485   1.00 28.66  ? 123  ALA B O     1 
ATOM   4976 C CB    . ALA B 1 123 ? 2.821   33.580  8.658   1.00 31.05  ? 123  ALA B CB    1 
ATOM   4977 N N     . LEU B 1 124 ? 2.680   30.341  8.649   1.00 26.12  ? 124  LEU B N     1 
ATOM   4978 C CA    . LEU B 1 124 ? 1.694   29.251  8.549   1.00 28.79  ? 124  LEU B CA    1 
ATOM   4979 C C     . LEU B 1 124 ? 0.567   29.627  9.487   1.00 31.10  ? 124  LEU B C     1 
ATOM   4980 O O     . LEU B 1 124 ? 0.853   29.840  10.723  1.00 30.12  ? 124  LEU B O     1 
ATOM   4981 C CB    . LEU B 1 124 ? 2.316   27.908  8.937   1.00 30.99  ? 124  LEU B CB    1 
ATOM   4982 C CG    . LEU B 1 124 ? 1.357   26.719  8.857   1.00 30.32  ? 124  LEU B CG    1 
ATOM   4983 C CD1   . LEU B 1 124 ? 0.812   26.582  7.438   1.00 32.64  ? 124  LEU B CD1   1 
ATOM   4984 C CD2   . LEU B 1 124 ? 2.044   25.442  9.308   1.00 31.05  ? 124  LEU B CD2   1 
ATOM   4985 N N     . LEU B 1 125 ? -0.630  29.734  8.917   1.00 31.21  ? 125  LEU B N     1 
ATOM   4986 C CA    . LEU B 1 125 ? -1.806  30.384  9.542   1.00 30.85  ? 125  LEU B CA    1 
ATOM   4987 C C     . LEU B 1 125 ? -2.976  29.414  9.579   1.00 33.82  ? 125  LEU B C     1 
ATOM   4988 O O     . LEU B 1 125 ? -3.117  28.575  8.668   1.00 34.39  ? 125  LEU B O     1 
ATOM   4989 C CB    . LEU B 1 125 ? -2.172  31.619  8.715   1.00 32.71  ? 125  LEU B CB    1 
ATOM   4990 C CG    . LEU B 1 125 ? -1.121  32.715  8.708   1.00 29.61  ? 125  LEU B CG    1 
ATOM   4991 C CD1   . LEU B 1 125 ? -1.589  33.909  7.878   1.00 33.52  ? 125  LEU B CD1   1 
ATOM   4992 C CD2   . LEU B 1 125 ? -0.798  33.132  10.130  1.00 30.76  ? 125  LEU B CD2   1 
ATOM   4993 N N     . GLU B 1 126 ? -3.781  29.536  10.622  1.00 30.40  ? 126  GLU B N     1 
ATOM   4994 C CA    . GLU B 1 126 ? -5.111  28.914  10.680  1.00 30.21  ? 126  GLU B CA    1 
ATOM   4995 C C     . GLU B 1 126 ? -6.109  29.982  10.259  1.00 27.69  ? 126  GLU B C     1 
ATOM   4996 O O     . GLU B 1 126 ? -5.752  31.159  10.188  1.00 30.33  ? 126  GLU B O     1 
ATOM   4997 C CB    . GLU B 1 126 ? -5.351  28.382  12.091  1.00 32.52  ? 126  GLU B CB    1 
ATOM   4998 C CG    . GLU B 1 126 ? -4.463  27.216  12.473  1.00 33.67  ? 126  GLU B CG    1 
ATOM   4999 C CD    . GLU B 1 126 ? -4.892  26.602  13.803  1.00 36.69  ? 126  GLU B CD    1 
ATOM   5000 O OE1   . GLU B 1 126 ? -5.338  27.372  14.658  1.00 34.95  ? 126  GLU B OE1   1 
ATOM   5001 O OE2   . GLU B 1 126 ? -4.877  25.362  13.935  1.00 31.55  ? 126  GLU B OE2   1 
ATOM   5002 N N     . PRO B 1 127 ? -7.365  29.600  9.950   1.00 28.91  ? 127  PRO B N     1 
ATOM   5003 C CA    . PRO B 1 127 ? -8.334  30.523  9.346   1.00 31.81  ? 127  PRO B CA    1 
ATOM   5004 C C     . PRO B 1 127 ? -8.735  31.768  10.159  1.00 34.37  ? 127  PRO B C     1 
ATOM   5005 O O     . PRO B 1 127 ? -9.014  32.762  9.553   1.00 28.84  ? 127  PRO B O     1 
ATOM   5006 C CB    . PRO B 1 127 ? -9.539  29.607  9.091   1.00 30.69  ? 127  PRO B CB    1 
ATOM   5007 C CG    . PRO B 1 127 ? -8.912  28.254  8.866   1.00 31.24  ? 127  PRO B CG    1 
ATOM   5008 C CD    . PRO B 1 127 ? -7.846  28.208  9.941   1.00 30.30  ? 127  PRO B CD    1 
ATOM   5009 N N     . GLY B 1 128 ? -8.726  31.695  11.495  1.00 31.77  ? 128  GLY B N     1 
ATOM   5010 C CA    . GLY B 1 128 ? -9.221  32.770  12.374  1.00 32.89  ? 128  GLY B CA    1 
ATOM   5011 C C     . GLY B 1 128 ? -8.188  33.858  12.577  1.00 36.47  ? 128  GLY B C     1 
ATOM   5012 O O     . GLY B 1 128 ? -8.496  34.832  13.267  1.00 38.76  ? 128  GLY B O     1 
ATOM   5013 N N     . VAL B 1 129 ? -7.001  33.741  11.983  1.00 31.86  ? 129  VAL B N     1 
ATOM   5014 C CA    . VAL B 1 129 ? -6.013  34.851  12.068  1.00 34.15  ? 129  VAL B CA    1 
ATOM   5015 C C     . VAL B 1 129 ? -6.473  35.994  11.159  1.00 35.01  ? 129  VAL B C     1 
ATOM   5016 O O     . VAL B 1 129 ? -6.604  35.754  9.911   1.00 31.39  ? 129  VAL B O     1 
ATOM   5017 C CB    . VAL B 1 129 ? -4.589  34.399  11.728  1.00 29.69  ? 129  VAL B CB    1 
ATOM   5018 C CG1   . VAL B 1 129 ? -3.620  35.545  11.872  1.00 29.71  ? 129  VAL B CG1   1 
ATOM   5019 C CG2   . VAL B 1 129 ? -4.185  33.208  12.580  1.00 32.45  ? 129  VAL B CG2   1 
ATOM   5020 N N     . THR B 1 130 ? -6.690  37.175  11.750  1.00 31.36  ? 130  THR B N     1 
ATOM   5021 C CA    . THR B 1 130 ? -7.148  38.399  11.033  1.00 33.75  ? 130  THR B CA    1 
ATOM   5022 C C     . THR B 1 130 ? -5.911  39.169  10.598  1.00 32.20  ? 130  THR B C     1 
ATOM   5023 O O     . THR B 1 130 ? -4.810  38.872  11.098  1.00 35.79  ? 130  THR B O     1 
ATOM   5024 C CB    . THR B 1 130 ? -8.098  39.255  11.887  1.00 32.82  ? 130  THR B CB    1 
ATOM   5025 O OG1   . THR B 1 130 ? -7.383  39.703  13.040  1.00 34.41  ? 130  THR B OG1   1 
ATOM   5026 C CG2   . THR B 1 130 ? -9.318  38.511  12.356  1.00 30.28  ? 130  THR B CG2   1 
ATOM   5027 N N     . TYR B 1 131 ? -6.063  40.160  9.735   1.00 33.94  ? 131  TYR B N     1 
ATOM   5028 C CA    . TYR B 1 131 ? -4.907  40.977  9.296   1.00 31.70  ? 131  TYR B CA    1 
ATOM   5029 C C     . TYR B 1 131 ? -4.305  41.672  10.524  1.00 33.72  ? 131  TYR B C     1 
ATOM   5030 O O     . TYR B 1 131 ? -3.070  41.721  10.649  1.00 35.65  ? 131  TYR B O     1 
ATOM   5031 C CB    . TYR B 1 131 ? -5.352  41.891  8.155   1.00 35.17  ? 131  TYR B CB    1 
ATOM   5032 C CG    . TYR B 1 131 ? -5.643  41.134  6.884   1.00 34.00  ? 131  TYR B CG    1 
ATOM   5033 C CD1   . TYR B 1 131 ? -4.615  40.633  6.100   1.00 34.34  ? 131  TYR B CD1   1 
ATOM   5034 C CD2   . TYR B 1 131 ? -6.941  40.850  6.504   1.00 35.61  ? 131  TYR B CD2   1 
ATOM   5035 C CE1   . TYR B 1 131 ? -4.870  39.898  4.950   1.00 36.86  ? 131  TYR B CE1   1 
ATOM   5036 C CE2   . TYR B 1 131 ? -7.215  40.124  5.355   1.00 37.66  ? 131  TYR B CE2   1 
ATOM   5037 C CZ    . TYR B 1 131 ? -6.179  39.651  4.571   1.00 36.99  ? 131  TYR B CZ    1 
ATOM   5038 O OH    . TYR B 1 131 ? -6.442  38.952  3.428   1.00 39.25  ? 131  TYR B OH    1 
ATOM   5039 N N     . PHE B 1 132 ? -5.164  42.194  11.406  1.00 35.51  ? 132  PHE B N     1 
ATOM   5040 C CA    . PHE B 1 132 ? -4.796  42.857  12.688  1.00 36.38  ? 132  PHE B CA    1 
ATOM   5041 C C     . PHE B 1 132 ? -3.921  41.906  13.524  1.00 32.81  ? 132  PHE B C     1 
ATOM   5042 O O     . PHE B 1 132 ? -2.841  42.306  13.957  1.00 34.66  ? 132  PHE B O     1 
ATOM   5043 C CB    . PHE B 1 132 ? -6.058  43.301  13.449  1.00 33.39  ? 132  PHE B CB    1 
ATOM   5044 C CG    . PHE B 1 132 ? -6.688  44.582  12.942  1.00 36.97  ? 132  PHE B CG    1 
ATOM   5045 C CD1   . PHE B 1 132 ? -5.958  45.761  12.876  1.00 40.64  ? 132  PHE B CD1   1 
ATOM   5046 C CD2   . PHE B 1 132 ? -8.009  44.618  12.512  1.00 39.17  ? 132  PHE B CD2   1 
ATOM   5047 C CE1   . PHE B 1 132 ? -6.525  46.939  12.399  1.00 40.66  ? 132  PHE B CE1   1 
ATOM   5048 C CE2   . PHE B 1 132 ? -8.575  45.789  12.025  1.00 36.00  ? 132  PHE B CE2   1 
ATOM   5049 C CZ    . PHE B 1 132 ? -7.832  46.951  11.965  1.00 40.67  ? 132  PHE B CZ    1 
ATOM   5050 N N     . ASP B 1 133 ? -4.416  40.702  13.765  1.00 34.37  ? 133  ASP B N     1 
ATOM   5051 C CA    . ASP B 1 133 ? -3.715  39.641  14.532  1.00 38.26  ? 133  ASP B CA    1 
ATOM   5052 C C     . ASP B 1 133 ? -2.306  39.498  13.974  1.00 37.80  ? 133  ASP B C     1 
ATOM   5053 O O     . ASP B 1 133 ? -1.332  39.546  14.753  1.00 35.71  ? 133  ASP B O     1 
ATOM   5054 C CB    . ASP B 1 133 ? -4.413  38.285  14.432  1.00 37.25  ? 133  ASP B CB    1 
ATOM   5055 C CG    . ASP B 1 133 ? -5.730  38.173  15.177  1.00 42.86  ? 133  ASP B CG    1 
ATOM   5056 O OD1   . ASP B 1 133 ? -5.997  39.048  16.047  1.00 40.96  ? 133  ASP B OD1   1 
ATOM   5057 O OD2   . ASP B 1 133 ? -6.499  37.221  14.856  1.00 38.91  ? 133  ASP B OD2   1 
ATOM   5058 N N     . LEU B 1 134 ? -2.197  39.335  12.655  1.00 35.56  ? 134  LEU B N     1 
ATOM   5059 C CA    . LEU B 1 134 ? -0.897  38.978  12.055  1.00 32.81  ? 134  LEU B CA    1 
ATOM   5060 C C     . LEU B 1 134 ? 0.027   40.185  12.162  1.00 34.07  ? 134  LEU B C     1 
ATOM   5061 O O     . LEU B 1 134 ? 1.157   39.970  12.563  1.00 35.59  ? 134  LEU B O     1 
ATOM   5062 C CB    . LEU B 1 134 ? -1.073  38.490  10.619  1.00 31.99  ? 134  LEU B CB    1 
ATOM   5063 C CG    . LEU B 1 134 ? 0.205   37.978  9.964   1.00 34.68  ? 134  LEU B CG    1 
ATOM   5064 C CD1   . LEU B 1 134 ? 0.941   36.984  10.870  1.00 32.14  ? 134  LEU B CD1   1 
ATOM   5065 C CD2   . LEU B 1 134 ? -0.129  37.333  8.625   1.00 34.96  ? 134  LEU B CD2   1 
ATOM   5066 N N     . HIS B 1 135 ? -0.465  41.398  11.861  1.00 38.34  ? 135  HIS B N     1 
ATOM   5067 C CA    . HIS B 1 135 ? 0.267   42.686  12.036  1.00 38.32  ? 135  HIS B CA    1 
ATOM   5068 C C     . HIS B 1 135 ? 0.812   42.814  13.461  1.00 38.25  ? 135  HIS B C     1 
ATOM   5069 O O     . HIS B 1 135 ? 1.972   43.225  13.618  1.00 33.20  ? 135  HIS B O     1 
ATOM   5070 C CB    . HIS B 1 135 ? -0.641  43.895  11.783  1.00 39.31  ? 135  HIS B CB    1 
ATOM   5071 C CG    . HIS B 1 135 ? -0.021  45.201  12.146  1.00 38.87  ? 135  HIS B CG    1 
ATOM   5072 N ND1   . HIS B 1 135 ? 1.013   45.763  11.422  1.00 38.94  ? 135  HIS B ND1   1 
ATOM   5073 C CD2   . HIS B 1 135 ? -0.328  46.085  13.115  1.00 39.57  ? 135  HIS B CD2   1 
ATOM   5074 C CE1   . HIS B 1 135 ? 1.338   46.922  11.956  1.00 42.31  ? 135  HIS B CE1   1 
ATOM   5075 N NE2   . HIS B 1 135 ? 0.535   47.136  13.000  1.00 43.47  ? 135  HIS B NE2   1 
ATOM   5076 N N     . GLU B 1 136 ? -0.059  42.580  14.438  1.00 39.91  ? 136  GLU B N     1 
ATOM   5077 C CA    . GLU B 1 136 ? 0.240   42.710  15.889  1.00 44.21  ? 136  GLU B CA    1 
ATOM   5078 C C     . GLU B 1 136 ? 1.340   41.701  16.252  1.00 41.61  ? 136  GLU B C     1 
ATOM   5079 O O     . GLU B 1 136 ? 2.295   42.091  16.924  1.00 39.20  ? 136  GLU B O     1 
ATOM   5080 C CB    . GLU B 1 136 ? -1.049  42.482  16.671  1.00 47.02  ? 136  GLU B CB    1 
ATOM   5081 C CG    . GLU B 1 136 ? -1.080  43.168  18.010  1.00 57.59  ? 136  GLU B CG    1 
ATOM   5082 C CD    . GLU B 1 136 ? -2.432  43.021  18.688  1.00 62.79  ? 136  GLU B CD    1 
ATOM   5083 O OE1   . GLU B 1 136 ? -3.463  43.024  17.957  1.00 62.93  ? 136  GLU B OE1   1 
ATOM   5084 O OE2   . GLU B 1 136 ? -2.448  42.878  19.932  1.00 62.25  ? 136  GLU B OE2   1 
ATOM   5085 N N     . TYR B 1 137 ? 1.221   40.460  15.775  1.00 38.93  ? 137  TYR B N     1 
ATOM   5086 C CA    . TYR B 1 137 ? 2.248   39.405  15.927  1.00 40.17  ? 137  TYR B CA    1 
ATOM   5087 C C     . TYR B 1 137 ? 3.586   39.867  15.335  1.00 41.33  ? 137  TYR B C     1 
ATOM   5088 O O     . TYR B 1 137 ? 4.633   39.701  15.989  1.00 33.78  ? 137  TYR B O     1 
ATOM   5089 C CB    . TYR B 1 137 ? 1.759   38.098  15.298  1.00 41.46  ? 137  TYR B CB    1 
ATOM   5090 C CG    . TYR B 1 137 ? 2.647   36.925  15.613  1.00 41.41  ? 137  TYR B CG    1 
ATOM   5091 C CD1   . TYR B 1 137 ? 3.815   36.692  14.901  1.00 42.93  ? 137  TYR B CD1   1 
ATOM   5092 C CD2   . TYR B 1 137 ? 2.342   36.072  16.660  1.00 42.70  ? 137  TYR B CD2   1 
ATOM   5093 C CE1   . TYR B 1 137 ? 4.657   35.633  15.221  1.00 47.57  ? 137  TYR B CE1   1 
ATOM   5094 C CE2   . TYR B 1 137 ? 3.170   35.007  16.988  1.00 46.80  ? 137  TYR B CE2   1 
ATOM   5095 C CZ    . TYR B 1 137 ? 4.332   34.791  16.272  1.00 44.86  ? 137  TYR B CZ    1 
ATOM   5096 O OH    . TYR B 1 137 ? 5.119   33.731  16.601  1.00 50.79  ? 137  TYR B OH    1 
ATOM   5097 N N     . LEU B 1 138 ? 3.588   40.360  14.120  1.00 38.09  ? 138  LEU B N     1 
ATOM   5098 C CA    . LEU B 1 138 ? 4.829   40.694  13.471  1.00 39.98  ? 138  LEU B CA    1 
ATOM   5099 C C     . LEU B 1 138 ? 5.559   41.818  14.165  1.00 43.31  ? 138  LEU B C     1 
ATOM   5100 O O     . LEU B 1 138 ? 6.721   41.747  14.380  1.00 39.54  ? 138  LEU B O     1 
ATOM   5101 C CB    . LEU B 1 138 ? 4.587   41.019  12.009  1.00 38.34  ? 138  LEU B CB    1 
ATOM   5102 C CG    . LEU B 1 138 ? 4.087   39.918  11.073  1.00 40.26  ? 138  LEU B CG    1 
ATOM   5103 C CD1   . LEU B 1 138 ? 4.046   40.395  9.635   1.00 40.44  ? 138  LEU B CD1   1 
ATOM   5104 C CD2   . LEU B 1 138 ? 4.888   38.639  11.190  1.00 35.36  ? 138  LEU B CD2   1 
ATOM   5105 N N     . GLU B 1 139 ? 4.852   42.853  14.536  1.00 45.65  ? 139  GLU B N     1 
ATOM   5106 C CA    . GLU B 1 139 ? 5.473   43.979  15.183  1.00 49.36  ? 139  GLU B CA    1 
ATOM   5107 C C     . GLU B 1 139 ? 6.177   43.550  16.445  1.00 48.07  ? 139  GLU B C     1 
ATOM   5108 O O     . GLU B 1 139 ? 7.230   44.060  16.765  1.00 50.43  ? 139  GLU B O     1 
ATOM   5109 C CB    . GLU B 1 139 ? 4.406   45.001  15.496  1.00 55.91  ? 139  GLU B CB    1 
ATOM   5110 C CG    . GLU B 1 139 ? 4.012   45.879  14.328  1.00 59.05  ? 139  GLU B CG    1 
ATOM   5111 C CD    . GLU B 1 139 ? 5.204   46.472  13.615  1.00 58.74  ? 139  GLU B CD    1 
ATOM   5112 O OE1   . GLU B 1 139 ? 5.892   47.331  14.204  1.00 53.92  ? 139  GLU B OE1   1 
ATOM   5113 O OE2   . GLU B 1 139 ? 5.444   46.079  12.460  1.00 52.31  ? 139  GLU B OE2   1 
ATOM   5114 N N     . ALA B 1 140 ? 5.612   42.589  17.141  1.00 47.33  ? 140  ALA B N     1 
ATOM   5115 C CA    . ALA B 1 140 ? 6.211   42.079  18.350  1.00 52.54  ? 140  ALA B CA    1 
ATOM   5116 C C     . ALA B 1 140 ? 7.333   41.053  18.206  1.00 53.12  ? 140  ALA B C     1 
ATOM   5117 O O     . ALA B 1 140 ? 8.218   41.025  19.043  1.00 58.53  ? 140  ALA B O     1 
ATOM   5118 C CB    . ALA B 1 140 ? 5.128   41.516  19.220  1.00 51.09  ? 140  ALA B CB    1 
ATOM   5119 N N     . HIS B 1 141 ? 7.278   40.179  17.186  1.00 68.23  ? 141  HIS B N     1 
ATOM   5120 C CA    . HIS B 1 141 ? 8.224   39.041  17.010  1.00 55.35  ? 141  HIS B CA    1 
ATOM   5121 C C     . HIS B 1 141 ? 8.940   38.907  15.680  1.00 49.76  ? 141  HIS B C     1 
ATOM   5122 O O     . HIS B 1 141 ? 10.004  38.313  15.628  1.00 51.88  ? 141  HIS B O     1 
ATOM   5123 C CB    . HIS B 1 141 ? 7.534   37.743  17.219  1.00 56.97  ? 141  HIS B CB    1 
ATOM   5124 C CG    . HIS B 1 141 ? 6.489   37.785  18.262  1.00 61.76  ? 141  HIS B CG    1 
ATOM   5125 N ND1   . HIS B 1 141 ? 5.158   37.868  17.949  1.00 68.08  ? 141  HIS B ND1   1 
ATOM   5126 C CD2   . HIS B 1 141 ? 6.567   37.763  19.610  1.00 63.83  ? 141  HIS B CD2   1 
ATOM   5127 C CE1   . HIS B 1 141 ? 4.455   37.906  19.057  1.00 62.50  ? 141  HIS B CE1   1 
ATOM   5128 N NE2   . HIS B 1 141 ? 5.286   37.836  20.081  1.00 60.91  ? 141  HIS B NE2   1 
ATOM   5129 N N     . ALA B 1 142 ? 8.353   39.397  14.600  1.00 46.23  ? 142  ALA B N     1 
ATOM   5130 C CA    . ALA B 1 142 ? 9.039   39.409  13.308  1.00 41.90  ? 142  ALA B CA    1 
ATOM   5131 C C     . ALA B 1 142 ? 8.978   40.848  12.659  1.00 40.71  ? 142  ALA B C     1 
ATOM   5132 O O     . ALA B 1 142 ? 8.494   40.962  11.555  1.00 35.27  ? 142  ALA B O     1 
ATOM   5133 C CB    . ALA B 1 142 ? 8.521   38.343  12.398  1.00 43.00  ? 142  ALA B CB    1 
ATOM   5134 N N     . PRO B 1 143 ? 9.447   41.943  13.363  1.00 42.29  ? 143  PRO B N     1 
ATOM   5135 C CA    . PRO B 1 143 ? 9.378   43.305  12.823  1.00 41.43  ? 143  PRO B CA    1 
ATOM   5136 C C     . PRO B 1 143 ? 10.011  43.700  11.478  1.00 38.46  ? 143  PRO B C     1 
ATOM   5137 O O     . PRO B 1 143 ? 9.693   44.786  11.012  1.00 35.27  ? 143  PRO B O     1 
ATOM   5138 C CB    . PRO B 1 143 ? 10.215  44.133  13.823  1.00 40.24  ? 143  PRO B CB    1 
ATOM   5139 C CG    . PRO B 1 143 ? 10.150  43.378  15.107  1.00 41.81  ? 143  PRO B CG    1 
ATOM   5140 C CD    . PRO B 1 143 ? 10.065  41.923  14.702  1.00 41.78  ? 143  PRO B CD    1 
ATOM   5141 N N     . SER B 1 144 ? 10.913  42.893  10.917  1.00 34.61  ? 144  SER B N     1 
ATOM   5142 C CA    . SER B 1 144 ? 11.491  43.116  9.561   1.00 37.08  ? 144  SER B CA    1 
ATOM   5143 C C     . SER B 1 144 ? 10.439  42.845  8.463   1.00 33.71  ? 144  SER B C     1 
ATOM   5144 O O     . SER B 1 144 ? 10.714  43.180  7.294   1.00 37.00  ? 144  SER B O     1 
ATOM   5145 C CB    . SER B 1 144 ? 12.689  42.233  9.349   1.00 37.73  ? 144  SER B CB    1 
ATOM   5146 O OG    . SER B 1 144 ? 12.282  40.864  9.362   1.00 39.26  ? 144  SER B OG    1 
ATOM   5147 N N     . LEU B 1 145 ? 9.323   42.215  8.822   1.00 30.92  ? 145  LEU B N     1 
ATOM   5148 C CA    . LEU B 1 145 ? 8.265   41.734  7.896   1.00 34.62  ? 145  LEU B CA    1 
ATOM   5149 C C     . LEU B 1 145 ? 7.039   42.632  7.996   1.00 37.40  ? 145  LEU B C     1 
ATOM   5150 O O     . LEU B 1 145 ? 6.836   43.218  9.089   1.00 34.32  ? 145  LEU B O     1 
ATOM   5151 C CB    . LEU B 1 145 ? 7.844   40.304  8.262   1.00 33.67  ? 145  LEU B CB    1 
ATOM   5152 C CG    . LEU B 1 145 ? 8.917   39.238  8.101   1.00 32.53  ? 145  LEU B CG    1 
ATOM   5153 C CD1   . LEU B 1 145 ? 8.320   37.861  8.361   1.00 36.19  ? 145  LEU B CD1   1 
ATOM   5154 C CD2   . LEU B 1 145 ? 9.549   39.324  6.717   1.00 32.50  ? 145  LEU B CD2   1 
ATOM   5155 N N     . MET B 1 146 ? 6.217   42.613  6.934   1.00 34.55  ? 146  MET B N     1 
ATOM   5156 C CA    . MET B 1 146 ? 4.906   43.315  6.858   1.00 34.17  ? 146  MET B CA    1 
ATOM   5157 C C     . MET B 1 146 ? 3.873   42.427  6.154   1.00 34.31  ? 146  MET B C     1 
ATOM   5158 O O     . MET B 1 146 ? 4.251   41.585  5.285   1.00 33.97  ? 146  MET B O     1 
ATOM   5159 C CB    . MET B 1 146 ? 5.056   44.645  6.119   1.00 38.11  ? 146  MET B CB    1 
ATOM   5160 C CG    . MET B 1 146 ? 5.809   44.536  4.818   1.00 36.53  ? 146  MET B CG    1 
ATOM   5161 S SD    . MET B 1 146 ? 5.973   46.137  4.035   1.00 40.31  ? 146  MET B SD    1 
ATOM   5162 C CE    . MET B 1 146 ? 4.288   46.352  3.466   1.00 41.22  ? 146  MET B CE    1 
ATOM   5163 N N     . ILE B 1 147 ? 2.624   42.544  6.586   1.00 32.67  ? 147  ILE B N     1 
ATOM   5164 C CA    . ILE B 1 147 ? 1.454   41.870  5.959   1.00 32.33  ? 147  ILE B CA    1 
ATOM   5165 C C     . ILE B 1 147 ? 1.137   42.602  4.656   1.00 31.25  ? 147  ILE B C     1 
ATOM   5166 O O     . ILE B 1 147 ? 1.718   43.683  4.403   1.00 32.03  ? 147  ILE B O     1 
ATOM   5167 C CB    . ILE B 1 147 ? 0.240   41.815  6.903   1.00 34.94  ? 147  ILE B CB    1 
ATOM   5168 C CG1   . ILE B 1 147 ? -0.371  43.196  7.170   1.00 36.63  ? 147  ILE B CG1   1 
ATOM   5169 C CG2   . ILE B 1 147 ? 0.587   41.098  8.202   1.00 38.55  ? 147  ILE B CG2   1 
ATOM   5170 C CD1   . ILE B 1 147 ? -1.737  43.114  7.838   1.00 38.68  ? 147  ILE B CD1   1 
ATOM   5171 N N     . ASP B 1 148 ? 0.345   41.965  3.801   1.00 30.33  ? 148  ASP B N     1 
ATOM   5172 C CA    . ASP B 1 148 ? -0.406  42.661  2.737   1.00 31.37  ? 148  ASP B CA    1 
ATOM   5173 C C     . ASP B 1 148 ? -1.871  42.501  3.127   1.00 31.97  ? 148  ASP B C     1 
ATOM   5174 O O     . ASP B 1 148 ? -2.337  41.352  3.252   1.00 30.63  ? 148  ASP B O     1 
ATOM   5175 C CB    . ASP B 1 148 ? -0.078  42.131  1.347   1.00 32.20  ? 148  ASP B CB    1 
ATOM   5176 C CG    . ASP B 1 148 ? -0.825  42.898  0.264   1.00 32.28  ? 148  ASP B CG    1 
ATOM   5177 O OD1   . ASP B 1 148 ? -2.072  42.795  0.237   1.00 31.41  ? 148  ASP B OD1   1 
ATOM   5178 O OD2   . ASP B 1 148 ? -0.160  43.610  -0.511  1.00 31.29  ? 148  ASP B OD2   1 
ATOM   5179 N N     . CYS B 1 149 ? -2.548  43.618  3.323   1.00 32.46  ? 149  CYS B N     1 
ATOM   5180 C CA    . CYS B 1 149 ? -3.926  43.611  3.758   1.00 33.15  ? 149  CYS B CA    1 
ATOM   5181 C C     . CYS B 1 149 ? -4.850  44.283  2.787   1.00 30.69  ? 149  CYS B C     1 
ATOM   5182 O O     . CYS B 1 149 ? -4.453  45.127  2.035   1.00 32.86  ? 149  CYS B O     1 
ATOM   5183 C CB    . CYS B 1 149 ? -4.029  44.367  5.094   1.00 32.68  ? 149  CYS B CB    1 
ATOM   5184 S SG    . CYS B 1 149 ? -3.406  46.055  5.098   1.00 36.96  ? 149  CYS B SG    1 
ATOM   5185 N N     . PRO B 1 150 ? -6.114  43.912  2.815   1.00 33.09  ? 150  PRO B N     1 
ATOM   5186 C CA    . PRO B 1 150 ? -7.066  44.644  2.005   1.00 35.02  ? 150  PRO B CA    1 
ATOM   5187 C C     . PRO B 1 150 ? -7.442  45.946  2.725   1.00 35.92  ? 150  PRO B C     1 
ATOM   5188 O O     . PRO B 1 150 ? -6.829  46.339  3.698   1.00 35.13  ? 150  PRO B O     1 
ATOM   5189 C CB    . PRO B 1 150 ? -8.247  43.692  1.955   1.00 31.72  ? 150  PRO B CB    1 
ATOM   5190 C CG    . PRO B 1 150 ? -8.152  42.897  3.179   1.00 34.54  ? 150  PRO B CG    1 
ATOM   5191 C CD    . PRO B 1 150 ? -6.689  42.668  3.304   1.00 32.09  ? 150  PRO B CD    1 
ATOM   5192 N N     . ASP B 1 151 ? -8.485  46.600  2.235   1.00 66.03  ? 151  ASP B N     1 
ATOM   5193 C CA    . ASP B 1 151 ? -8.955  47.864  2.796   1.00 56.10  ? 151  ASP B CA    1 
ATOM   5194 C C     . ASP B 1 151 ? -9.353  47.723  4.252   1.00 49.11  ? 151  ASP B C     1 
ATOM   5195 O O     . ASP B 1 151 ? -9.128  48.632  5.022   1.00 41.07  ? 151  ASP B O     1 
ATOM   5196 C CB    . ASP B 1 151 ? -10.126 48.389  1.990   1.00 58.12  ? 151  ASP B CB    1 
ATOM   5197 C CG    . ASP B 1 151 ? -9.713  48.997  0.683   1.00 51.81  ? 151  ASP B CG    1 
ATOM   5198 O OD1   . ASP B 1 151 ? -8.524  49.298  0.516   1.00 56.68  ? 151  ASP B OD1   1 
ATOM   5199 O OD2   . ASP B 1 151 ? -10.585 49.173  -0.181  1.00 54.66  ? 151  ASP B OD2   1 
ATOM   5200 N N     . LEU B 1 152 ? -9.950  46.592  4.610   1.00 41.26  ? 152  LEU B N     1 
ATOM   5201 C CA    . LEU B 1 152 ? -10.356 46.338  5.984   1.00 46.92  ? 152  LEU B CA    1 
ATOM   5202 C C     . LEU B 1 152 ? -9.498  45.279  6.668   1.00 47.77  ? 152  LEU B C     1 
ATOM   5203 O O     . LEU B 1 152 ? -9.188  44.286  6.066   1.00 58.79  ? 152  LEU B O     1 
ATOM   5204 C CB    . LEU B 1 152 ? -11.833 46.001  6.050   1.00 45.07  ? 152  LEU B CB    1 
ATOM   5205 C CG    . LEU B 1 152 ? -12.740 46.975  5.304   1.00 45.63  ? 152  LEU B CG    1 
ATOM   5206 C CD1   . LEU B 1 152 ? -14.158 46.463  5.279   1.00 45.63  ? 152  LEU B CD1   1 
ATOM   5207 C CD2   . LEU B 1 152 ? -12.684 48.370  5.894   1.00 46.51  ? 152  LEU B CD2   1 
ATOM   5208 N N     . GLY B 1 153 ? -9.105  45.493  7.905   1.00 43.87  ? 153  GLY B N     1 
ATOM   5209 C CA    . GLY B 1 153 ? -8.188  44.610  8.636   1.00 45.06  ? 153  GLY B CA    1 
ATOM   5210 C C     . GLY B 1 153 ? -8.908  43.492  9.352   1.00 44.21  ? 153  GLY B C     1 
ATOM   5211 O O     . GLY B 1 153 ? -8.225  42.597  9.853   1.00 49.21  ? 153  GLY B O     1 
ATOM   5212 N N     . TRP B 1 154 ? -10.239 43.507  9.430   1.00 41.82  ? 154  TRP B N     1 
ATOM   5213 C CA    . TRP B 1 154 ? -10.932 42.570  10.351  1.00 37.94  ? 154  TRP B CA    1 
ATOM   5214 C C     . TRP B 1 154 ? -11.122 41.224  9.661   1.00 34.80  ? 154  TRP B C     1 
ATOM   5215 O O     . TRP B 1 154 ? -11.596 40.305  10.326  1.00 42.04  ? 154  TRP B O     1 
ATOM   5216 C CB    . TRP B 1 154 ? -12.231 43.170  10.914  1.00 40.65  ? 154  TRP B CB    1 
ATOM   5217 C CG    . TRP B 1 154 ? -13.242 43.616  9.901   1.00 44.94  ? 154  TRP B CG    1 
ATOM   5218 C CD1   . TRP B 1 154 ? -13.236 43.419  8.547   1.00 45.18  ? 154  TRP B CD1   1 
ATOM   5219 C CD2   . TRP B 1 154 ? -14.469 44.307  10.197  1.00 47.76  ? 154  TRP B CD2   1 
ATOM   5220 N NE1   . TRP B 1 154 ? -14.362 43.963  7.984   1.00 46.72  ? 154  TRP B NE1   1 
ATOM   5221 C CE2   . TRP B 1 154 ? -15.133 44.516  8.972   1.00 49.11  ? 154  TRP B CE2   1 
ATOM   5222 C CE3   . TRP B 1 154 ? -15.049 44.791  11.378  1.00 51.45  ? 154  TRP B CE3   1 
ATOM   5223 C CZ2   . TRP B 1 154 ? -16.355 45.180  8.903   1.00 48.70  ? 154  TRP B CZ2   1 
ATOM   5224 C CZ3   . TRP B 1 154 ? -16.257 45.450  11.307  1.00 52.08  ? 154  TRP B CZ3   1 
ATOM   5225 C CH2   . TRP B 1 154 ? -16.892 45.646  10.082  1.00 52.87  ? 154  TRP B CH2   1 
ATOM   5226 N N     . GLY B 1 155 ? -10.739 41.111  8.381   1.00 32.72  ? 155  GLY B N     1 
ATOM   5227 C CA    . GLY B 1 155 ? -10.891 39.886  7.582   1.00 31.59  ? 155  GLY B CA    1 
ATOM   5228 C C     . GLY B 1 155 ? -9.808  38.852  7.869   1.00 34.35  ? 155  GLY B C     1 
ATOM   5229 O O     . GLY B 1 155 ? -8.860  39.162  8.605   1.00 34.14  ? 155  GLY B O     1 
ATOM   5230 N N     . SER B 1 156 ? -9.954  37.664  7.276   1.00 34.14  ? 156  SER B N     1 
ATOM   5231 C CA    . SER B 1 156 ? -9.075  36.475  7.439   1.00 30.38  ? 156  SER B CA    1 
ATOM   5232 C C     . SER B 1 156 ? -7.948  36.498  6.395   1.00 30.13  ? 156  SER B C     1 
ATOM   5233 O O     . SER B 1 156 ? -8.206  36.649  5.192   1.00 30.17  ? 156  SER B O     1 
ATOM   5234 C CB    . SER B 1 156 ? -9.907  35.201  7.376   1.00 30.77  ? 156  SER B CB    1 
ATOM   5235 O OG    . SER B 1 156 ? -9.106  34.025  7.339   1.00 30.89  ? 156  SER B OG    1 
ATOM   5236 N N     . VAL B 1 157 ? -6.706  36.342  6.835   1.00 33.10  ? 157  VAL B N     1 
ATOM   5237 C CA    . VAL B 1 157 ? -5.555  36.262  5.889   1.00 32.89  ? 157  VAL B CA    1 
ATOM   5238 C C     . VAL B 1 157 ? -5.824  35.074  4.954   1.00 31.42  ? 157  VAL B C     1 
ATOM   5239 O O     . VAL B 1 157 ? -5.621  35.239  3.728   1.00 31.46  ? 157  VAL B O     1 
ATOM   5240 C CB    . VAL B 1 157 ? -4.209  36.155  6.617   1.00 33.26  ? 157  VAL B CB    1 
ATOM   5241 C CG1   . VAL B 1 157 ? -3.033  36.128  5.631   1.00 34.05  ? 157  VAL B CG1   1 
ATOM   5242 C CG2   . VAL B 1 157 ? -4.046  37.284  7.620   1.00 32.88  ? 157  VAL B CG2   1 
ATOM   5243 N N     . VAL B 1 158 ? -6.339  33.982  5.529   1.00 27.70  ? 158  VAL B N     1 
ATOM   5244 C CA    . VAL B 1 158 ? -6.718  32.710  4.861   1.00 30.59  ? 158  VAL B CA    1 
ATOM   5245 C C     . VAL B 1 158 ? -7.965  32.931  3.990   1.00 33.10  ? 158  VAL B C     1 
ATOM   5246 O O     . VAL B 1 158 ? -7.885  32.688  2.763   1.00 30.65  ? 158  VAL B O     1 
ATOM   5247 C CB    . VAL B 1 158 ? -6.946  31.589  5.886   1.00 35.04  ? 158  VAL B CB    1 
ATOM   5248 C CG1   . VAL B 1 158 ? -7.551  30.345  5.255   1.00 38.22  ? 158  VAL B CG1   1 
ATOM   5249 C CG2   . VAL B 1 158 ? -5.658  31.228  6.609   1.00 39.11  ? 158  VAL B CG2   1 
ATOM   5250 N N     . GLY B 1 159 ? -9.078  33.336  4.600   1.00 30.06  ? 159  GLY B N     1 
ATOM   5251 C CA    . GLY B 1 159 ? -10.393 33.431  3.932   1.00 31.93  ? 159  GLY B CA    1 
ATOM   5252 C C     . GLY B 1 159 ? -10.338 34.404  2.766   1.00 30.02  ? 159  GLY B C     1 
ATOM   5253 O O     . GLY B 1 159 ? -10.823 34.083  1.680   1.00 28.22  ? 159  GLY B O     1 
ATOM   5254 N N     . ASN B 1 160 ? -9.688  35.537  2.963   1.00 30.96  ? 160  ASN B N     1 
ATOM   5255 C CA    . ASN B 1 160 ? -9.521  36.518  1.873   1.00 32.21  ? 160  ASN B CA    1 
ATOM   5256 C C     . ASN B 1 160 ? -8.716  35.847  0.752   1.00 35.46  ? 160  ASN B C     1 
ATOM   5257 O O     . ASN B 1 160 ? -9.163  35.953  -0.402  1.00 33.01  ? 160  ASN B O     1 
ATOM   5258 C CB    . ASN B 1 160 ? -8.950  37.841  2.372   1.00 32.11  ? 160  ASN B CB    1 
ATOM   5259 C CG    . ASN B 1 160 ? -8.674  38.787  1.235   1.00 33.06  ? 160  ASN B CG    1 
ATOM   5260 O OD1   . ASN B 1 160 ? -7.779  38.534  0.436   1.00 41.46  ? 160  ASN B OD1   1 
ATOM   5261 N ND2   . ASN B 1 160 ? -9.469  39.833  1.116   1.00 34.97  ? 160  ASN B ND2   1 
ATOM   5262 N N     . ALA B 1 161 ? -7.645  35.096  1.064   1.00 33.28  ? 161  ALA B N     1 
ATOM   5263 C CA    . ALA B 1 161 ? -6.843  34.408  0.025   1.00 34.75  ? 161  ALA B CA    1 
ATOM   5264 C C     . ALA B 1 161 ? -7.715  33.405  -0.743  1.00 33.30  ? 161  ALA B C     1 
ATOM   5265 O O     . ALA B 1 161 ? -7.544  33.300  -1.982  1.00 32.10  ? 161  ALA B O     1 
ATOM   5266 C CB    . ALA B 1 161 ? -5.607  33.747  0.612   1.00 35.40  ? 161  ALA B CB    1 
ATOM   5267 N N     . LEU B 1 162 ? -8.590  32.676  -0.052  1.00 31.12  ? 162  LEU B N     1 
ATOM   5268 C CA    . LEU B 1 162 ? -9.411  31.587  -0.657  1.00 33.95  ? 162  LEU B CA    1 
ATOM   5269 C C     . LEU B 1 162 ? -10.558 32.121  -1.547  1.00 33.77  ? 162  LEU B C     1 
ATOM   5270 O O     . LEU B 1 162 ? -11.207 31.279  -2.234  1.00 32.57  ? 162  LEU B O     1 
ATOM   5271 C CB    . LEU B 1 162 ? -9.964  30.713  0.468   1.00 35.08  ? 162  LEU B CB    1 
ATOM   5272 C CG    . LEU B 1 162 ? -8.933  29.947  1.302   1.00 35.21  ? 162  LEU B CG    1 
ATOM   5273 C CD1   . LEU B 1 162 ? -9.622  29.220  2.448   1.00 35.82  ? 162  LEU B CD1   1 
ATOM   5274 C CD2   . LEU B 1 162 ? -8.169  28.959  0.442   1.00 34.50  ? 162  LEU B CD2   1 
ATOM   5275 N N     . ASP B 1 163 ? -10.853 33.423  -1.514  1.00 30.08  ? 163  ASP B N     1 
ATOM   5276 C CA    . ASP B 1 163 ? -11.793 34.083  -2.468  1.00 33.66  ? 163  ASP B CA    1 
ATOM   5277 C C     . ASP B 1 163 ? -10.968 34.899  -3.487  1.00 30.76  ? 163  ASP B C     1 
ATOM   5278 O O     . ASP B 1 163 ? -11.578 35.639  -4.274  1.00 35.15  ? 163  ASP B O     1 
ATOM   5279 C CB    . ASP B 1 163 ? -12.847 34.920  -1.718  1.00 31.05  ? 163  ASP B CB    1 
ATOM   5280 C CG    . ASP B 1 163 ? -14.271 34.815  -2.256  1.00 35.99  ? 163  ASP B CG    1 
ATOM   5281 O OD1   . ASP B 1 163 ? -14.663 33.708  -2.667  1.00 39.13  ? 163  ASP B OD1   1 
ATOM   5282 O OD2   . ASP B 1 163 ? -15.000 35.843  -2.252  1.00 40.50  ? 163  ASP B OD2   1 
ATOM   5283 N N     . ARG B 1 164 ? -9.635  34.778  -3.454  1.00 33.06  ? 164  ARG B N     1 
ATOM   5284 C CA    . ARG B 1 164 ? -8.630  35.485  -4.304  1.00 31.87  ? 164  ARG B CA    1 
ATOM   5285 C C     . ARG B 1 164 ? -8.808  36.997  -4.161  1.00 33.64  ? 164  ARG B C     1 
ATOM   5286 O O     . ARG B 1 164 ? -8.738  37.727  -5.187  1.00 33.27  ? 164  ARG B O     1 
ATOM   5287 C CB    . ARG B 1 164 ? -8.652  34.990  -5.758  1.00 31.54  ? 164  ARG B CB    1 
ATOM   5288 C CG    . ARG B 1 164 ? -8.313  33.508  -5.897  1.00 29.89  ? 164  ARG B CG    1 
ATOM   5289 C CD    . ARG B 1 164 ? -7.870  33.103  -7.289  1.00 27.46  ? 164  ARG B CD    1 
ATOM   5290 N NE    . ARG B 1 164 ? -8.955  33.317  -8.234  1.00 28.31  ? 164  ARG B NE    1 
ATOM   5291 C CZ    . ARG B 1 164 ? -9.921  32.445  -8.514  1.00 28.58  ? 164  ARG B CZ    1 
ATOM   5292 N NH1   . ARG B 1 164 ? -9.956  31.233  -7.976  1.00 29.75  ? 164  ARG B NH1   1 
ATOM   5293 N NH2   . ARG B 1 164 ? -10.857 32.794  -9.362  1.00 33.72  ? 164  ARG B NH2   1 
ATOM   5294 N N     . GLY B 1 165 ? -8.948  37.447  -2.908  1.00 33.28  ? 165  GLY B N     1 
ATOM   5295 C CA    . GLY B 1 165 ? -9.002  38.871  -2.545  1.00 31.34  ? 165  GLY B CA    1 
ATOM   5296 C C     . GLY B 1 165 ? -7.642  39.500  -2.751  1.00 30.15  ? 165  GLY B C     1 
ATOM   5297 O O     . GLY B 1 165 ? -6.696  38.784  -3.152  1.00 30.47  ? 165  GLY B O     1 
ATOM   5298 N N     . ALA B 1 166 ? -7.518  40.801  -2.538  1.00 29.53  ? 166  ALA B N     1 
ATOM   5299 C CA    . ALA B 1 166 ? -6.267  41.519  -2.855  1.00 30.99  ? 166  ALA B CA    1 
ATOM   5300 C C     . ALA B 1 166 ? -6.026  42.663  -1.877  1.00 30.72  ? 166  ALA B C     1 
ATOM   5301 O O     . ALA B 1 166 ? -6.979  43.190  -1.298  1.00 34.03  ? 166  ALA B O     1 
ATOM   5302 C CB    . ALA B 1 166 ? -6.280  42.003  -4.287  1.00 31.33  ? 166  ALA B CB    1 
ATOM   5303 N N     . GLY B 1 167 ? -4.755  42.990  -1.689  1.00 32.15  ? 167  GLY B N     1 
ATOM   5304 C CA    . GLY B 1 167 ? -4.297  44.256  -1.114  1.00 30.17  ? 167  GLY B CA    1 
ATOM   5305 C C     . GLY B 1 167 ? -3.450  44.994  -2.111  1.00 30.09  ? 167  GLY B C     1 
ATOM   5306 O O     . GLY B 1 167 ? -3.536  44.668  -3.312  1.00 29.05  ? 167  GLY B O     1 
ATOM   5307 N N     . TYR B 1 168 ? -2.647  45.947  -1.635  1.00 32.71  ? 168  TYR B N     1 
ATOM   5308 C CA    . TYR B 1 168 ? -2.088  47.038  -2.470  1.00 32.14  ? 168  TYR B CA    1 
ATOM   5309 C C     . TYR B 1 168 ? -0.578  47.190  -2.263  1.00 34.16  ? 168  TYR B C     1 
ATOM   5310 O O     . TYR B 1 168 ? -0.004  48.144  -2.866  1.00 33.86  ? 168  TYR B O     1 
ATOM   5311 C CB    . TYR B 1 168 ? -2.885  48.317  -2.204  1.00 32.62  ? 168  TYR B CB    1 
ATOM   5312 C CG    . TYR B 1 168 ? -4.369  48.092  -2.310  1.00 33.00  ? 168  TYR B CG    1 
ATOM   5313 C CD1   . TYR B 1 168 ? -5.039  48.218  -3.522  1.00 31.69  ? 168  TYR B CD1   1 
ATOM   5314 C CD2   . TYR B 1 168 ? -5.079  47.632  -1.215  1.00 33.91  ? 168  TYR B CD2   1 
ATOM   5315 C CE1   . TYR B 1 168 ? -6.392  47.945  -3.624  1.00 32.75  ? 168  TYR B CE1   1 
ATOM   5316 C CE2   . TYR B 1 168 ? -6.421  47.318  -1.313  1.00 36.84  ? 168  TYR B CE2   1 
ATOM   5317 C CZ    . TYR B 1 168 ? -7.093  47.513  -2.508  1.00 36.78  ? 168  TYR B CZ    1 
ATOM   5318 O OH    . TYR B 1 168 ? -8.430  47.205  -2.551  1.00 39.03  ? 168  TYR B OH    1 
ATOM   5319 N N     . THR B 1 169 ? 0.067   46.289  -1.506  1.00 32.10  ? 169  THR B N     1 
ATOM   5320 C CA    . THR B 1 169 ? 1.551   46.235  -1.428  1.00 30.96  ? 169  THR B CA    1 
ATOM   5321 C C     . THR B 1 169 ? 2.022   45.442  -2.645  1.00 33.18  ? 169  THR B C     1 
ATOM   5322 O O     . THR B 1 169 ? 1.204   44.964  -3.439  1.00 34.36  ? 169  THR B O     1 
ATOM   5323 C CB    . THR B 1 169 ? 2.063   45.642  -0.103  1.00 32.37  ? 169  THR B CB    1 
ATOM   5324 O OG1   . THR B 1 169 ? 2.031   44.221  -0.237  1.00 33.45  ? 169  THR B OG1   1 
ATOM   5325 C CG2   . THR B 1 169 ? 1.281   46.054  1.122   1.00 29.61  ? 169  THR B CG2   1 
ATOM   5326 N N     . PRO B 1 170 ? 3.347   45.304  -2.891  1.00 30.71  ? 170  PRO B N     1 
ATOM   5327 C CA    . PRO B 1 170 ? 3.797   44.447  -3.980  1.00 29.54  ? 170  PRO B CA    1 
ATOM   5328 C C     . PRO B 1 170 ? 3.303   43.004  -3.790  1.00 31.77  ? 170  PRO B C     1 
ATOM   5329 O O     . PRO B 1 170 ? 3.254   42.276  -4.781  1.00 34.48  ? 170  PRO B O     1 
ATOM   5330 C CB    . PRO B 1 170 ? 5.330   44.622  -3.970  1.00 29.68  ? 170  PRO B CB    1 
ATOM   5331 C CG    . PRO B 1 170 ? 5.553   45.972  -3.277  1.00 29.25  ? 170  PRO B CG    1 
ATOM   5332 C CD    . PRO B 1 170 ? 4.455   46.031  -2.236  1.00 29.24  ? 170  PRO B CD    1 
ATOM   5333 N N     . TYR B 1 171 ? 2.927   42.619  -2.563  1.00 30.07  ? 171  TYR B N     1 
ATOM   5334 C CA    . TYR B 1 171 ? 2.345   41.284  -2.251  1.00 30.93  ? 171  TYR B CA    1 
ATOM   5335 C C     . TYR B 1 171 ? 0.807   41.339  -2.318  1.00 30.85  ? 171  TYR B C     1 
ATOM   5336 O O     . TYR B 1 171 ? 0.133   40.561  -1.594  1.00 30.51  ? 171  TYR B O     1 
ATOM   5337 C CB    . TYR B 1 171 ? 2.869   40.766  -0.906  1.00 32.07  ? 171  TYR B CB    1 
ATOM   5338 C CG    . TYR B 1 171 ? 4.215   40.098  -1.009  1.00 33.23  ? 171  TYR B CG    1 
ATOM   5339 C CD1   . TYR B 1 171 ? 5.222   40.627  -1.801  1.00 34.52  ? 171  TYR B CD1   1 
ATOM   5340 C CD2   . TYR B 1 171 ? 4.495   38.950  -0.296  1.00 33.86  ? 171  TYR B CD2   1 
ATOM   5341 C CE1   . TYR B 1 171 ? 6.459   40.023  -1.907  1.00 33.36  ? 171  TYR B CE1   1 
ATOM   5342 C CE2   . TYR B 1 171 ? 5.734   38.342  -0.374  1.00 34.97  ? 171  TYR B CE2   1 
ATOM   5343 C CZ    . TYR B 1 171 ? 6.724   38.877  -1.179  1.00 36.60  ? 171  TYR B CZ    1 
ATOM   5344 O OH    . TYR B 1 171 ? 7.947   38.262  -1.268  1.00 32.62  ? 171  TYR B OH    1 
ATOM   5345 N N     . GLY B 1 172 ? 0.261   42.204  -3.179  1.00 28.88  ? 172  GLY B N     1 
ATOM   5346 C CA    . GLY B 1 172 ? -1.189  42.487  -3.288  1.00 30.77  ? 172  GLY B CA    1 
ATOM   5347 C C     . GLY B 1 172 ? -2.013  41.278  -3.723  1.00 27.82  ? 172  GLY B C     1 
ATOM   5348 O O     . GLY B 1 172 ? -3.117  41.163  -3.244  1.00 28.41  ? 172  GLY B O     1 
ATOM   5349 N N     . ASP B 1 173 ? -1.473  40.377  -4.548  1.00 28.02  ? 173  ASP B N     1 
ATOM   5350 C CA    . ASP B 1 173 ? -2.190  39.163  -5.021  1.00 30.29  ? 173  ASP B CA    1 
ATOM   5351 C C     . ASP B 1 173 ? -2.095  38.068  -3.957  1.00 30.91  ? 173  ASP B C     1 
ATOM   5352 O O     . ASP B 1 173 ? -1.120  37.293  -3.982  1.00 29.60  ? 173  ASP B O     1 
ATOM   5353 C CB    . ASP B 1 173 ? -1.653  38.678  -6.365  1.00 27.51  ? 173  ASP B CB    1 
ATOM   5354 C CG    . ASP B 1 173 ? -2.412  37.495  -6.933  1.00 27.64  ? 173  ASP B CG    1 
ATOM   5355 O OD1   . ASP B 1 173 ? -3.148  36.851  -6.166  1.00 28.49  ? 173  ASP B OD1   1 
ATOM   5356 O OD2   . ASP B 1 173 ? -2.262  37.230  -8.161  1.00 28.55  ? 173  ASP B OD2   1 
ATOM   5357 N N     . HIS B 1 174 ? -3.095  37.983  -3.081  1.00 30.75  ? 174  HIS B N     1 
ATOM   5358 C CA    . HIS B 1 174 ? -3.030  37.144  -1.855  1.00 33.12  ? 174  HIS B CA    1 
ATOM   5359 C C     . HIS B 1 174 ? -2.889  35.673  -2.249  1.00 34.67  ? 174  HIS B C     1 
ATOM   5360 O O     . HIS B 1 174 ? -2.045  34.996  -1.650  1.00 39.26  ? 174  HIS B O     1 
ATOM   5361 C CB    . HIS B 1 174 ? -4.210  37.427  -0.934  1.00 33.23  ? 174  HIS B CB    1 
ATOM   5362 C CG    . HIS B 1 174 ? -4.191  38.818  -0.411  1.00 33.65  ? 174  HIS B CG    1 
ATOM   5363 N ND1   . HIS B 1 174 ? -5.308  39.408  0.151   1.00 32.81  ? 174  HIS B ND1   1 
ATOM   5364 C CD2   . HIS B 1 174 ? -3.211  39.747  -0.403  1.00 31.84  ? 174  HIS B CD2   1 
ATOM   5365 C CE1   . HIS B 1 174 ? -4.992  40.632  0.526   1.00 33.95  ? 174  HIS B CE1   1 
ATOM   5366 N NE2   . HIS B 1 174 ? -3.705  40.858  0.206   1.00 33.68  ? 174  HIS B NE2   1 
ATOM   5367 N N     . PHE B 1 175 ? -3.591  35.216  -3.288  1.00 36.29  ? 175  PHE B N     1 
ATOM   5368 C CA    . PHE B 1 175 ? -3.485  33.811  -3.756  1.00 32.76  ? 175  PHE B CA    1 
ATOM   5369 C C     . PHE B 1 175 ? -2.058  33.536  -4.264  1.00 28.86  ? 175  PHE B C     1 
ATOM   5370 O O     . PHE B 1 175 ? -1.509  32.451  -3.967  1.00 27.82  ? 175  PHE B O     1 
ATOM   5371 C CB    . PHE B 1 175 ? -4.531  33.429  -4.812  1.00 32.88  ? 175  PHE B CB    1 
ATOM   5372 C CG    . PHE B 1 175 ? -4.204  32.074  -5.383  1.00 29.99  ? 175  PHE B CG    1 
ATOM   5373 C CD1   . PHE B 1 175 ? -4.361  30.938  -4.611  1.00 30.74  ? 175  PHE B CD1   1 
ATOM   5374 C CD2   . PHE B 1 175 ? -3.553  31.957  -6.596  1.00 31.17  ? 175  PHE B CD2   1 
ATOM   5375 C CE1   . PHE B 1 175 ? -3.991  29.692  -5.090  1.00 27.05  ? 175  PHE B CE1   1 
ATOM   5376 C CE2   . PHE B 1 175 ? -3.200  30.711  -7.085  1.00 30.31  ? 175  PHE B CE2   1 
ATOM   5377 C CZ    . PHE B 1 175 ? -3.396  29.585  -6.319  1.00 28.08  ? 175  PHE B CZ    1 
ATOM   5378 N N     . MET B 1 176 ? -1.492  34.446  -5.059  1.00 29.89  ? 176  MET B N     1 
ATOM   5379 C CA    . MET B 1 176 ? -0.101  34.326  -5.554  1.00 30.59  ? 176  MET B CA    1 
ATOM   5380 C C     . MET B 1 176 ? 0.814   33.980  -4.362  1.00 30.14  ? 176  MET B C     1 
ATOM   5381 O O     . MET B 1 176 ? 1.588   33.022  -4.479  1.00 31.27  ? 176  MET B O     1 
ATOM   5382 C CB    . MET B 1 176 ? 0.394   35.614  -6.218  1.00 35.67  ? 176  MET B CB    1 
ATOM   5383 C CG    . MET B 1 176 ? 1.684   35.431  -6.994  1.00 41.96  ? 176  MET B CG    1 
ATOM   5384 S SD    . MET B 1 176 ? 2.431   36.995  -7.554  1.00 47.69  ? 176  MET B SD    1 
ATOM   5385 C CE    . MET B 1 176 ? 3.056   36.472  -9.153  1.00 55.35  ? 176  MET B CE    1 
ATOM   5386 N N     . TRP B 1 177 ? 0.731   34.719  -3.252  1.00 29.00  ? 177  TRP B N     1 
ATOM   5387 C CA    . TRP B 1 177 ? 1.693   34.588  -2.133  1.00 28.84  ? 177  TRP B CA    1 
ATOM   5388 C C     . TRP B 1 177 ? 1.291   33.439  -1.210  1.00 28.92  ? 177  TRP B C     1 
ATOM   5389 O O     . TRP B 1 177 ? 2.173   32.991  -0.437  1.00 30.07  ? 177  TRP B O     1 
ATOM   5390 C CB    . TRP B 1 177 ? 1.899   35.943  -1.452  1.00 29.25  ? 177  TRP B CB    1 
ATOM   5391 C CG    . TRP B 1 177 ? 2.525   36.876  -2.449  1.00 30.93  ? 177  TRP B CG    1 
ATOM   5392 C CD1   . TRP B 1 177 ? 1.939   37.943  -3.051  1.00 30.33  ? 177  TRP B CD1   1 
ATOM   5393 C CD2   . TRP B 1 177 ? 3.813   36.720  -3.081  1.00 31.06  ? 177  TRP B CD2   1 
ATOM   5394 N NE1   . TRP B 1 177 ? 2.778   38.487  -3.976  1.00 31.26  ? 177  TRP B NE1   1 
ATOM   5395 C CE2   . TRP B 1 177 ? 3.930   37.753  -4.029  1.00 33.67  ? 177  TRP B CE2   1 
ATOM   5396 C CE3   . TRP B 1 177 ? 4.877   35.817  -2.927  1.00 32.13  ? 177  TRP B CE3   1 
ATOM   5397 C CZ2   . TRP B 1 177 ? 5.074   37.927  -4.810  1.00 35.79  ? 177  TRP B CZ2   1 
ATOM   5398 C CZ3   . TRP B 1 177 ? 6.003   35.977  -3.707  1.00 30.82  ? 177  TRP B CZ3   1 
ATOM   5399 C CH2   . TRP B 1 177 ? 6.099   37.021  -4.630  1.00 35.35  ? 177  TRP B CH2   1 
ATOM   5400 N N     . GLN B 1 178 ? 0.050   32.958  -1.302  1.00 30.13  ? 178  GLN B N     1 
ATOM   5401 C CA    . GLN B 1 178 ? -0.416  31.726  -0.594  1.00 29.97  ? 178  GLN B CA    1 
ATOM   5402 C C     . GLN B 1 178 ? 0.540   30.591  -0.966  1.00 31.92  ? 178  GLN B C     1 
ATOM   5403 O O     . GLN B 1 178 ? 0.808   30.381  -2.161  1.00 28.19  ? 178  GLN B O     1 
ATOM   5404 C CB    . GLN B 1 178 ? -1.871  31.366  -0.906  1.00 29.08  ? 178  GLN B CB    1 
ATOM   5405 C CG    . GLN B 1 178 ? -2.325  30.026  -0.314  1.00 26.66  ? 178  GLN B CG    1 
ATOM   5406 C CD    . GLN B 1 178 ? -2.107  28.849  -1.237  1.00 31.38  ? 178  GLN B CD    1 
ATOM   5407 O OE1   . GLN B 1 178 ? -2.246  28.995  -2.448  1.00 33.39  ? 178  GLN B OE1   1 
ATOM   5408 N NE2   . GLN B 1 178 ? -1.770  27.670  -0.689  1.00 26.67  ? 178  GLN B NE2   1 
ATOM   5409 N N     . THR B 1 179 ? 1.100   29.923  0.030   1.00 31.43  ? 179  THR B N     1 
ATOM   5410 C CA    . THR B 1 179 ? 2.150   28.918  -0.208  1.00 27.95  ? 179  THR B CA    1 
ATOM   5411 C C     . THR B 1 179 ? 1.857   27.734  0.697   1.00 29.72  ? 179  THR B C     1 
ATOM   5412 O O     . THR B 1 179 ? 2.169   27.829  1.908   1.00 27.44  ? 179  THR B O     1 
ATOM   5413 C CB    . THR B 1 179 ? 3.563   29.493  -0.057  1.00 27.94  ? 179  THR B CB    1 
ATOM   5414 O OG1   . THR B 1 179 ? 3.683   30.742  -0.744  1.00 28.89  ? 179  THR B OG1   1 
ATOM   5415 C CG2   . THR B 1 179 ? 4.597   28.535  -0.613  1.00 26.12  ? 179  THR B CG2   1 
ATOM   5416 N N     . GLY B 1 180 ? 1.234   26.706  0.120   1.00 25.50  ? 180  GLY B N     1 
ATOM   5417 C CA    . GLY B 1 180 ? 0.875   25.471  0.808   1.00 27.44  ? 180  GLY B CA    1 
ATOM   5418 C C     . GLY B 1 180 ? -0.398  25.617  1.603   1.00 28.61  ? 180  GLY B C     1 
ATOM   5419 O O     . GLY B 1 180 ? -0.751  26.750  2.034   1.00 28.91  ? 180  GLY B O     1 
ATOM   5420 N N     . MET B 1 181 ? -1.139  24.528  1.723   1.00 28.14  ? 181  MET B N     1 
ATOM   5421 C CA    . MET B 1 181 ? -2.401  24.554  2.497   1.00 30.57  ? 181  MET B CA    1 
ATOM   5422 C C     . MET B 1 181 ? -2.711  23.126  2.903   1.00 29.04  ? 181  MET B C     1 
ATOM   5423 O O     . MET B 1 181 ? -2.216  22.200  2.244   1.00 32.21  ? 181  MET B O     1 
ATOM   5424 C CB    . MET B 1 181 ? -3.565  25.183  1.700   1.00 31.06  ? 181  MET B CB    1 
ATOM   5425 C CG    . MET B 1 181 ? -3.971  24.396  0.471   1.00 31.03  ? 181  MET B CG    1 
ATOM   5426 S SD    . MET B 1 181 ? -5.481  24.993  -0.347  1.00 33.89  ? 181  MET B SD    1 
ATOM   5427 C CE    . MET B 1 181 ? -5.043  26.677  -0.771  1.00 32.71  ? 181  MET B CE    1 
ATOM   5428 N N     . GLU B 1 182 ? -3.432  22.983  4.008   1.00 27.72  ? 182  GLU B N     1 
ATOM   5429 C CA    . GLU B 1 182 ? -3.966  21.692  4.476   1.00 27.89  ? 182  GLU B CA    1 
ATOM   5430 C C     . GLU B 1 182 ? -5.477  21.759  4.286   1.00 30.02  ? 182  GLU B C     1 
ATOM   5431 O O     . GLU B 1 182 ? -6.096  22.763  4.705   1.00 30.38  ? 182  GLU B O     1 
ATOM   5432 C CB    . GLU B 1 182 ? -3.549  21.467  5.931   1.00 28.40  ? 182  GLU B CB    1 
ATOM   5433 C CG    . GLU B 1 182 ? -4.083  20.178  6.526   1.00 27.29  ? 182  GLU B CG    1 
ATOM   5434 C CD    . GLU B 1 182 ? -3.818  20.075  8.024   1.00 29.05  ? 182  GLU B CD    1 
ATOM   5435 O OE1   . GLU B 1 182 ? -4.595  20.650  8.821   1.00 27.91  ? 182  GLU B OE1   1 
ATOM   5436 O OE2   . GLU B 1 182 ? -2.808  19.498  8.371   1.00 28.97  ? 182  GLU B OE2   1 
ATOM   5437 N N     . VAL B 1 183 ? -6.064  20.754  3.641   1.00 31.59  ? 183  VAL B N     1 
ATOM   5438 C CA    . VAL B 1 183 ? -7.499  20.855  3.275   1.00 29.65  ? 183  VAL B CA    1 
ATOM   5439 C C     . VAL B 1 183 ? -8.182  19.570  3.683   1.00 31.87  ? 183  VAL B C     1 
ATOM   5440 O O     . VAL B 1 183 ? -7.558  18.465  3.541   1.00 28.76  ? 183  VAL B O     1 
ATOM   5441 C CB    . VAL B 1 183 ? -7.705  21.192  1.787   1.00 30.87  ? 183  VAL B CB    1 
ATOM   5442 C CG1   . VAL B 1 183 ? -7.194  20.104  0.866   1.00 29.66  ? 183  VAL B CG1   1 
ATOM   5443 C CG2   . VAL B 1 183 ? -9.173  21.491  1.513   1.00 31.95  ? 183  VAL B CG2   1 
ATOM   5444 N N     . VAL B 1 184 ? -9.389  19.726  4.230   1.00 28.30  ? 184  VAL B N     1 
ATOM   5445 C CA    . VAL B 1 184 ? -10.300 18.573  4.411   1.00 27.40  ? 184  VAL B CA    1 
ATOM   5446 C C     . VAL B 1 184 ? -11.187 18.450  3.178   1.00 27.12  ? 184  VAL B C     1 
ATOM   5447 O O     . VAL B 1 184 ? -12.001 19.313  2.952   1.00 28.67  ? 184  VAL B O     1 
ATOM   5448 C CB    . VAL B 1 184 ? -11.129 18.676  5.689   1.00 27.59  ? 184  VAL B CB    1 
ATOM   5449 C CG1   . VAL B 1 184 ? -12.087 17.510  5.767   1.00 29.27  ? 184  VAL B CG1   1 
ATOM   5450 C CG2   . VAL B 1 184 ? -10.223 18.736  6.917   1.00 28.07  ? 184  VAL B CG2   1 
ATOM   5451 N N     . LEU B 1 185 ? -11.040 17.358  2.445   1.00 30.16  ? 185  LEU B N     1 
ATOM   5452 C CA    . LEU B 1 185 ? -11.824 17.093  1.220   1.00 31.60  ? 185  LEU B CA    1 
ATOM   5453 C C     . LEU B 1 185 ? -13.264 16.758  1.614   1.00 35.82  ? 185  LEU B C     1 
ATOM   5454 O O     . LEU B 1 185 ? -13.557 16.441  2.773   1.00 32.12  ? 185  LEU B O     1 
ATOM   5455 C CB    . LEU B 1 185 ? -11.122 15.978  0.441   1.00 30.96  ? 185  LEU B CB    1 
ATOM   5456 C CG    . LEU B 1 185 ? -9.718  16.333  -0.064  1.00 29.80  ? 185  LEU B CG    1 
ATOM   5457 C CD1   . LEU B 1 185 ? -9.020  15.100  -0.607  1.00 29.66  ? 185  LEU B CD1   1 
ATOM   5458 C CD2   . LEU B 1 185 ? -9.753  17.434  -1.123  1.00 27.83  ? 185  LEU B CD2   1 
ATOM   5459 N N     . PRO B 1 186 ? -14.193 16.835  0.637   1.00 35.21  ? 186  PRO B N     1 
ATOM   5460 C CA    . PRO B 1 186 ? -15.627 16.765  0.907   1.00 38.15  ? 186  PRO B CA    1 
ATOM   5461 C C     . PRO B 1 186 ? -16.140 15.522  1.653   1.00 34.51  ? 186  PRO B C     1 
ATOM   5462 O O     . PRO B 1 186 ? -17.169 15.656  2.217   1.00 36.88  ? 186  PRO B O     1 
ATOM   5463 C CB    . PRO B 1 186 ? -16.230 16.768  -0.504  1.00 33.68  ? 186  PRO B CB    1 
ATOM   5464 C CG    . PRO B 1 186 ? -15.217 17.505  -1.332  1.00 34.14  ? 186  PRO B CG    1 
ATOM   5465 C CD    . PRO B 1 186 ? -13.899 17.013  -0.796  1.00 33.22  ? 186  PRO B CD    1 
ATOM   5466 N N     . GLN B 1 187 ? -15.438 14.396  1.609   1.00 36.94  ? 187  GLN B N     1 
ATOM   5467 C CA    . GLN B 1 187 ? -15.813 13.180  2.340   1.00 37.63  ? 187  GLN B CA    1 
ATOM   5468 C C     . GLN B 1 187 ? -15.019 12.980  3.637   1.00 37.91  ? 187  GLN B C     1 
ATOM   5469 O O     . GLN B 1 187 ? -15.138 11.955  4.271   1.00 39.43  ? 187  GLN B O     1 
ATOM   5470 C CB    . GLN B 1 187 ? -15.683 11.933  1.475   1.00 35.75  ? 187  GLN B CB    1 
ATOM   5471 C CG    . GLN B 1 187 ? -16.216 12.003  0.075   1.00 35.73  ? 187  GLN B CG    1 
ATOM   5472 C CD    . GLN B 1 187 ? -16.146 10.649  -0.588  1.00 36.82  ? 187  GLN B CD    1 
ATOM   5473 O OE1   . GLN B 1 187 ? -15.401 10.448  -1.539  1.00 43.04  ? 187  GLN B OE1   1 
ATOM   5474 N NE2   . GLN B 1 187 ? -16.921 9.709   -0.083  1.00 36.93  ? 187  GLN B NE2   1 
ATOM   5475 N N     . GLY B 1 188 ? -14.183 13.933  4.010   1.00 37.00  ? 188  GLY B N     1 
ATOM   5476 C CA    . GLY B 1 188 ? -13.499 13.855  5.285   1.00 36.74  ? 188  GLY B CA    1 
ATOM   5477 C C     . GLY B 1 188 ? -12.042 13.541  5.331   1.00 37.93  ? 188  GLY B C     1 
ATOM   5478 O O     . GLY B 1 188 ? -11.466 13.550  6.381   1.00 42.41  ? 188  GLY B O     1 
ATOM   5479 N N     . ASP B 1 189 ? -11.453 13.236  4.202   1.00 37.10  ? 189  ASP B N     1 
ATOM   5480 C CA    . ASP B 1 189 ? -10.033 13.009  4.142   1.00 38.63  ? 189  ASP B CA    1 
ATOM   5481 C C     . ASP B 1 189 ? -9.290  14.325  4.183   1.00 35.00  ? 189  ASP B C     1 
ATOM   5482 O O     . ASP B 1 189 ? -9.784  15.313  3.720   1.00 35.42  ? 189  ASP B O     1 
ATOM   5483 C CB    . ASP B 1 189 ? -9.695  12.238  2.882   1.00 44.53  ? 189  ASP B CB    1 
ATOM   5484 C CG    . ASP B 1 189 ? -10.555 11.007  2.709   1.00 51.93  ? 189  ASP B CG    1 
ATOM   5485 O OD1   . ASP B 1 189 ? -10.537 10.138  3.602   1.00 75.80  ? 189  ASP B OD1   1 
ATOM   5486 O OD2   . ASP B 1 189 ? -11.253 10.905  1.689   1.00 45.92  ? 189  ASP B OD2   1 
ATOM   5487 N N     . VAL B 1 190 ? -8.105  14.328  4.742   1.00 30.60  ? 190  VAL B N     1 
ATOM   5488 C CA    . VAL B 1 190 ? -7.313  15.532  4.847   1.00 29.72  ? 190  VAL B CA    1 
ATOM   5489 C C     . VAL B 1 190 ? -6.069  15.390  3.959   1.00 30.29  ? 190  VAL B C     1 
ATOM   5490 O O     . VAL B 1 190 ? -5.530  14.322  3.822   1.00 29.87  ? 190  VAL B O     1 
ATOM   5491 C CB    . VAL B 1 190 ? -6.934  15.851  6.316   1.00 27.73  ? 190  VAL B CB    1 
ATOM   5492 C CG1   . VAL B 1 190 ? -6.080  14.770  6.950   1.00 28.13  ? 190  VAL B CG1   1 
ATOM   5493 C CG2   . VAL B 1 190 ? -6.320  17.222  6.471   1.00 27.64  ? 190  VAL B CG2   1 
ATOM   5494 N N     . MET B 1 191 ? -5.615  16.484  3.377   1.00 31.48  ? 191  MET B N     1 
ATOM   5495 C CA    . MET B 1 191 ? -4.418  16.399  2.532   1.00 29.42  ? 191  MET B CA    1 
ATOM   5496 C C     . MET B 1 191 ? -3.705  17.738  2.615   1.00 27.50  ? 191  MET B C     1 
ATOM   5497 O O     . MET B 1 191 ? -4.372  18.772  2.909   1.00 26.71  ? 191  MET B O     1 
ATOM   5498 C CB    . MET B 1 191 ? -4.824  16.007  1.107   1.00 31.56  ? 191  MET B CB    1 
ATOM   5499 C CG    . MET B 1 191 ? -4.598  17.031  0.092   1.00 33.74  ? 191  MET B CG    1 
ATOM   5500 S SD    . MET B 1 191 ? -4.956  16.454  -1.590  1.00 32.56  ? 191  MET B SD    1 
ATOM   5501 C CE    . MET B 1 191 ? -5.619  18.000  -2.189  1.00 33.80  ? 191  MET B CE    1 
ATOM   5502 N N     . ARG B 1 192 ? -2.387  17.684  2.439   1.00 25.48  ? 192  ARG B N     1 
ATOM   5503 C CA    . ARG B 1 192 ? -1.524  18.869  2.327   1.00 24.39  ? 192  ARG B CA    1 
ATOM   5504 C C     . ARG B 1 192 ? -1.077  18.982  0.889   1.00 23.82  ? 192  ARG B C     1 
ATOM   5505 O O     . ARG B 1 192 ? -0.831  17.941  0.286   1.00 28.39  ? 192  ARG B O     1 
ATOM   5506 C CB    . ARG B 1 192 ? -0.343  18.773  3.277   1.00 23.53  ? 192  ARG B CB    1 
ATOM   5507 C CG    . ARG B 1 192 ? -0.771  18.897  4.725   1.00 25.25  ? 192  ARG B CG    1 
ATOM   5508 C CD    . ARG B 1 192 ? 0.437   18.936  5.658   1.00 26.17  ? 192  ARG B CD    1 
ATOM   5509 N NE    . ARG B 1 192 ? -0.062  19.246  6.979   1.00 25.09  ? 192  ARG B NE    1 
ATOM   5510 C CZ    . ARG B 1 192 ? 0.691   19.474  8.038   1.00 26.40  ? 192  ARG B CZ    1 
ATOM   5511 N NH1   . ARG B 1 192 ? 2.005   19.438  7.959   1.00 28.35  ? 192  ARG B NH1   1 
ATOM   5512 N NH2   . ARG B 1 192 ? 0.117   19.770  9.180   1.00 27.10  ? 192  ARG B NH2   1 
ATOM   5513 N N     . THR B 1 193 ? -0.993  20.212  0.400   1.00 26.17  ? 193  THR B N     1 
ATOM   5514 C CA    . THR B 1 193 ? -0.624  20.548  -0.998  1.00 26.99  ? 193  THR B CA    1 
ATOM   5515 C C     . THR B 1 193 ? 0.857   20.833  -1.040  1.00 26.47  ? 193  THR B C     1 
ATOM   5516 O O     . THR B 1 193 ? 1.423   21.070  0.032   1.00 25.49  ? 193  THR B O     1 
ATOM   5517 C CB    . THR B 1 193 ? -1.412  21.750  -1.517  1.00 27.97  ? 193  THR B CB    1 
ATOM   5518 O OG1   . THR B 1 193 ? -1.029  22.945  -0.820  1.00 29.40  ? 193  THR B OG1   1 
ATOM   5519 C CG2   . THR B 1 193 ? -2.897  21.523  -1.387  1.00 27.00  ? 193  THR B CG2   1 
ATOM   5520 N N     . GLY B 1 194 ? 1.444   20.771  -2.233  1.00 22.56  ? 194  GLY B N     1 
ATOM   5521 C CA    . GLY B 1 194 ? 2.828   21.175  -2.494  1.00 26.26  ? 194  GLY B CA    1 
ATOM   5522 C C     . GLY B 1 194 ? 3.825   20.381  -1.675  1.00 26.27  ? 194  GLY B C     1 
ATOM   5523 O O     . GLY B 1 194 ? 3.678   19.145  -1.499  1.00 24.84  ? 194  GLY B O     1 
ATOM   5524 N N     . MET B 1 195 ? 4.829   21.070  -1.154  1.00 27.74  ? 195  MET B N     1 
ATOM   5525 C CA    . MET B 1 195 ? 5.949   20.410  -0.435  1.00 28.34  ? 195  MET B CA    1 
ATOM   5526 C C     . MET B 1 195 ? 5.483   19.810  0.907   1.00 27.75  ? 195  MET B C     1 
ATOM   5527 O O     . MET B 1 195 ? 6.182   18.911  1.444   1.00 29.31  ? 195  MET B O     1 
ATOM   5528 C CB    . MET B 1 195 ? 7.075   21.424  -0.236  1.00 28.55  ? 195  MET B CB    1 
ATOM   5529 C CG    . MET B 1 195 ? 7.615   21.960  -1.545  1.00 31.63  ? 195  MET B CG    1 
ATOM   5530 S SD    . MET B 1 195 ? 7.964   20.685  -2.801  1.00 36.10  ? 195  MET B SD    1 
ATOM   5531 C CE    . MET B 1 195 ? 9.355   19.827  -2.074  1.00 36.48  ? 195  MET B CE    1 
ATOM   5532 N N     . GLY B 1 196 ? 4.330   20.232  1.421   1.00 28.04  ? 196  GLY B N     1 
ATOM   5533 C CA    . GLY B 1 196 ? 3.792   19.736  2.697   1.00 25.75  ? 196  GLY B CA    1 
ATOM   5534 C C     . GLY B 1 196 ? 3.301   18.312  2.553   1.00 28.55  ? 196  GLY B C     1 
ATOM   5535 O O     . GLY B 1 196 ? 3.088   17.694  3.587   1.00 26.16  ? 196  GLY B O     1 
ATOM   5536 N N     . ALA B 1 197 ? 3.072   17.818  1.320   1.00 28.18  ? 197  ALA B N     1 
ATOM   5537 C CA    . ALA B 1 197 ? 2.703   16.405  1.051   1.00 26.97  ? 197  ALA B CA    1 
ATOM   5538 C C     . ALA B 1 197 ? 3.857   15.455  1.358   1.00 25.72  ? 197  ALA B C     1 
ATOM   5539 O O     . ALA B 1 197 ? 3.581   14.252  1.427   1.00 23.68  ? 197  ALA B O     1 
ATOM   5540 C CB    . ALA B 1 197 ? 2.275   16.190  -0.374  1.00 28.93  ? 197  ALA B CB    1 
ATOM   5541 N N     . LEU B 1 198 ? 5.094   15.958  1.478   1.00 24.40  ? 198  LEU B N     1 
ATOM   5542 C CA    . LEU B 1 198 ? 6.270   15.150  1.875   1.00 25.04  ? 198  LEU B CA    1 
ATOM   5543 C C     . LEU B 1 198 ? 6.412   15.178  3.396   1.00 21.69  ? 198  LEU B C     1 
ATOM   5544 O O     . LEU B 1 198 ? 6.674   16.218  3.963   1.00 23.75  ? 198  LEU B O     1 
ATOM   5545 C CB    . LEU B 1 198 ? 7.513   15.719  1.202   1.00 26.24  ? 198  LEU B CB    1 
ATOM   5546 C CG    . LEU B 1 198 ? 8.774   14.863  1.319   1.00 29.97  ? 198  LEU B CG    1 
ATOM   5547 C CD1   . LEU B 1 198 ? 9.296   14.506  -0.084  1.00 31.12  ? 198  LEU B CD1   1 
ATOM   5548 C CD2   . LEU B 1 198 ? 9.837   15.617  2.080   1.00 32.65  ? 198  LEU B CD2   1 
ATOM   5549 N N     . PRO B 1 199 ? 6.182   14.073  4.126   1.00 25.21  ? 199  PRO B N     1 
ATOM   5550 C CA    . PRO B 1 199 ? 6.350   14.094  5.593   1.00 25.06  ? 199  PRO B CA    1 
ATOM   5551 C C     . PRO B 1 199 ? 7.764   14.529  5.997   1.00 23.71  ? 199  PRO B C     1 
ATOM   5552 O O     . PRO B 1 199 ? 8.714   14.061  5.414   1.00 23.77  ? 199  PRO B O     1 
ATOM   5553 C CB    . PRO B 1 199 ? 6.066   12.644  5.974   1.00 26.48  ? 199  PRO B CB    1 
ATOM   5554 C CG    . PRO B 1 199 ? 5.105   12.167  4.885   1.00 26.20  ? 199  PRO B CG    1 
ATOM   5555 C CD    . PRO B 1 199 ? 5.657   12.794  3.625   1.00 25.51  ? 199  PRO B CD    1 
ATOM   5556 N N     . GLY B 1 200 ? 7.873   15.470  6.928   1.00 28.59  ? 200  GLY B N     1 
ATOM   5557 C CA    . GLY B 1 200 ? 9.158   15.988  7.438   1.00 25.78  ? 200  GLY B CA    1 
ATOM   5558 C C     . GLY B 1 200 ? 9.720   17.047  6.514   1.00 26.28  ? 200  GLY B C     1 
ATOM   5559 O O     . GLY B 1 200 ? 10.919  17.443  6.654   1.00 26.66  ? 200  GLY B O     1 
ATOM   5560 N N     . SER B 1 201 ? 8.916   17.512  5.571   1.00 27.11  ? 201  SER B N     1 
ATOM   5561 C CA    . SER B 1 201 ? 9.344   18.594  4.675   1.00 27.30  ? 201  SER B CA    1 
ATOM   5562 C C     . SER B 1 201 ? 9.730   19.859  5.368   1.00 25.08  ? 201  SER B C     1 
ATOM   5563 O O     . SER B 1 201 ? 9.057   20.272  6.266   1.00 26.70  ? 201  SER B O     1 
ATOM   5564 C CB    . SER B 1 201 ? 8.248   19.002  3.712   1.00 27.28  ? 201  SER B CB    1 
ATOM   5565 O OG    . SER B 1 201 ? 8.745   19.850  2.706   1.00 31.69  ? 201  SER B OG    1 
ATOM   5566 N N     . THR B 1 202 ? 10.766  20.505  4.881   1.00 25.58  ? 202  THR B N     1 
ATOM   5567 C CA    . THR B 1 202 ? 11.225  21.755  5.437   1.00 32.04  ? 202  THR B CA    1 
ATOM   5568 C C     . THR B 1 202 ? 10.895  22.924  4.515   1.00 30.19  ? 202  THR B C     1 
ATOM   5569 O O     . THR B 1 202 ? 11.275  24.041  4.783   1.00 28.47  ? 202  THR B O     1 
ATOM   5570 C CB    . THR B 1 202 ? 12.749  21.664  5.633   1.00 33.50  ? 202  THR B CB    1 
ATOM   5571 O OG1   . THR B 1 202 ? 13.380  21.337  4.396   1.00 35.05  ? 202  THR B OG1   1 
ATOM   5572 C CG2   . THR B 1 202 ? 13.061  20.590  6.654   1.00 34.20  ? 202  THR B CG2   1 
ATOM   5573 N N     . THR B 1 203 ? 10.147  22.667  3.462   1.00 32.13  ? 203  THR B N     1 
ATOM   5574 C CA    . THR B 1 203 ? 9.892   23.683  2.449   1.00 29.26  ? 203  THR B CA    1 
ATOM   5575 C C     . THR B 1 203 ? 8.432   23.993  2.088   1.00 28.54  ? 203  THR B C     1 
ATOM   5576 O O     . THR B 1 203 ? 8.187   24.582  1.058   1.00 26.91  ? 203  THR B O     1 
ATOM   5577 C CB    . THR B 1 203 ? 10.529  23.211  1.148   1.00 29.25  ? 203  THR B CB    1 
ATOM   5578 O OG1   . THR B 1 203 ? 9.975   21.958  0.807   1.00 27.24  ? 203  THR B OG1   1 
ATOM   5579 C CG2   . THR B 1 203 ? 12.019  23.075  1.285   1.00 27.37  ? 203  THR B CG2   1 
ATOM   5580 N N     . TRP B 1 204 ? 7.481   23.608  2.921   1.00 30.10  ? 204  TRP B N     1 
ATOM   5581 C CA    . TRP B 1 204 ? 6.072   23.893  2.671   1.00 29.28  ? 204  TRP B CA    1 
ATOM   5582 C C     . TRP B 1 204 ? 5.743   25.316  2.274   1.00 28.14  ? 204  TRP B C     1 
ATOM   5583 O O     . TRP B 1 204 ? 4.993   25.524  1.349   1.00 28.23  ? 204  TRP B O     1 
ATOM   5584 C CB    . TRP B 1 204 ? 5.225   23.468  3.859   1.00 37.76  ? 204  TRP B CB    1 
ATOM   5585 C CG    . TRP B 1 204 ? 3.788   23.193  3.575   1.00 41.38  ? 204  TRP B CG    1 
ATOM   5586 C CD1   . TRP B 1 204 ? 3.184   23.089  2.359   1.00 45.87  ? 204  TRP B CD1   1 
ATOM   5587 C CD2   . TRP B 1 204 ? 2.767   22.985  4.543   1.00 38.77  ? 204  TRP B CD2   1 
ATOM   5588 N NE1   . TRP B 1 204 ? 1.857   22.817  2.512   1.00 40.11  ? 204  TRP B NE1   1 
ATOM   5589 C CE2   . TRP B 1 204 ? 1.572   22.759  3.848   1.00 41.23  ? 204  TRP B CE2   1 
ATOM   5590 C CE3   . TRP B 1 204 ? 2.748   22.971  5.936   1.00 36.42  ? 204  TRP B CE3   1 
ATOM   5591 C CZ2   . TRP B 1 204 ? 0.376   22.527  4.494   1.00 41.56  ? 204  TRP B CZ2   1 
ATOM   5592 C CZ3   . TRP B 1 204 ? 1.564   22.739  6.572   1.00 40.25  ? 204  TRP B CZ3   1 
ATOM   5593 C CH2   . TRP B 1 204 ? 0.390   22.528  5.856   1.00 45.06  ? 204  TRP B CH2   1 
ATOM   5594 N N     . GLN B 1 205 ? 6.331   26.289  2.942   1.00 26.24  ? 205  GLN B N     1 
ATOM   5595 C CA    . GLN B 1 205 ? 6.010   27.673  2.678   1.00 27.69  ? 205  GLN B CA    1 
ATOM   5596 C C     . GLN B 1 205 ? 7.017   28.417  1.830   1.00 27.24  ? 205  GLN B C     1 
ATOM   5597 O O     . GLN B 1 205 ? 6.990   29.624  1.763   1.00 28.01  ? 205  GLN B O     1 
ATOM   5598 C CB    . GLN B 1 205 ? 5.784   28.364  3.996   1.00 28.70  ? 205  GLN B CB    1 
ATOM   5599 C CG    . GLN B 1 205 ? 4.362   28.339  4.505   1.00 27.27  ? 205  GLN B CG    1 
ATOM   5600 C CD    . GLN B 1 205 ? 3.923   26.979  4.996   1.00 30.78  ? 205  GLN B CD    1 
ATOM   5601 O OE1   . GLN B 1 205 ? 4.400   26.489  6.012   1.00 30.51  ? 205  GLN B OE1   1 
ATOM   5602 N NE2   . GLN B 1 205 ? 3.005   26.367  4.274   1.00 26.28  ? 205  GLN B NE2   1 
ATOM   5603 N N     . LEU B 1 206 ? 7.868   27.690  1.147   1.00 27.73  ? 206  LEU B N     1 
ATOM   5604 C CA    . LEU B 1 206 ? 8.935   28.296  0.375   1.00 28.80  ? 206  LEU B CA    1 
ATOM   5605 C C     . LEU B 1 206 ? 8.700   28.228  -1.125  1.00 27.65  ? 206  LEU B C     1 
ATOM   5606 O O     . LEU B 1 206 ? 9.257   29.014  -1.845  1.00 24.86  ? 206  LEU B O     1 
ATOM   5607 C CB    . LEU B 1 206 ? 10.249  27.614  0.736   1.00 28.30  ? 206  LEU B CB    1 
ATOM   5608 C CG    . LEU B 1 206 ? 10.642  27.683  2.203   1.00 28.49  ? 206  LEU B CG    1 
ATOM   5609 C CD1   . LEU B 1 206 ? 11.982  27.018  2.394   1.00 32.78  ? 206  LEU B CD1   1 
ATOM   5610 C CD2   . LEU B 1 206 ? 10.696  29.122  2.669   1.00 28.86  ? 206  LEU B CD2   1 
ATOM   5611 N N     . ILE B 1 207 ? 7.900   27.268  -1.576  1.00 27.21  ? 207  ILE B N     1 
ATOM   5612 C CA    . ILE B 1 207 ? 7.567   27.115  -2.993  1.00 30.22  ? 207  ILE B CA    1 
ATOM   5613 C C     . ILE B 1 207 ? 6.065   26.730  -3.117  1.00 28.17  ? 207  ILE B C     1 
ATOM   5614 O O     . ILE B 1 207 ? 5.618   25.871  -2.381  1.00 27.24  ? 207  ILE B O     1 
ATOM   5615 C CB    . ILE B 1 207 ? 8.536   26.186  -3.773  1.00 31.46  ? 207  ILE B CB    1 
ATOM   5616 C CG1   . ILE B 1 207 ? 8.135   26.008  -5.234  1.00 37.32  ? 207  ILE B CG1   1 
ATOM   5617 C CG2   . ILE B 1 207 ? 8.660   24.839  -3.115  1.00 32.22  ? 207  ILE B CG2   1 
ATOM   5618 C CD1   . ILE B 1 207 ? 8.880   26.913  -6.178  1.00 42.05  ? 207  ILE B CD1   1 
ATOM   5619 N N     . PRO B 1 208 ? 5.270   27.379  -4.037  1.00 27.49  ? 208  PRO B N     1 
ATOM   5620 C CA    . PRO B 1 208 ? 3.838   27.066  -4.015  1.00 28.37  ? 208  PRO B CA    1 
ATOM   5621 C C     . PRO B 1 208 ? 3.486   25.678  -4.577  1.00 29.79  ? 208  PRO B C     1 
ATOM   5622 O O     . PRO B 1 208 ? 2.474   25.100  -4.167  1.00 32.71  ? 208  PRO B O     1 
ATOM   5623 C CB    . PRO B 1 208 ? 3.179   28.209  -4.811  1.00 27.41  ? 208  PRO B CB    1 
ATOM   5624 C CG    . PRO B 1 208 ? 4.291   28.806  -5.655  1.00 29.32  ? 208  PRO B CG    1 
ATOM   5625 C CD    . PRO B 1 208 ? 5.598   28.479  -4.948  1.00 26.98  ? 208  PRO B CD    1 
ATOM   5626 N N     . TYR B 1 209 ? 4.325   25.158  -5.471  1.00 27.14  ? 209  TYR B N     1 
ATOM   5627 C CA    . TYR B 1 209 ? 4.082   23.917  -6.237  1.00 30.37  ? 209  TYR B CA    1 
ATOM   5628 C C     . TYR B 1 209 ? 4.918   22.798  -5.639  1.00 33.93  ? 209  TYR B C     1 
ATOM   5629 O O     . TYR B 1 209 ? 6.058   23.072  -5.246  1.00 49.54  ? 209  TYR B O     1 
ATOM   5630 C CB    . TYR B 1 209 ? 4.494   24.040  -7.709  1.00 31.30  ? 209  TYR B CB    1 
ATOM   5631 C CG    . TYR B 1 209 ? 4.536   25.427  -8.285  1.00 32.89  ? 209  TYR B CG    1 
ATOM   5632 C CD1   . TYR B 1 209 ? 3.384   26.172  -8.447  1.00 35.37  ? 209  TYR B CD1   1 
ATOM   5633 C CD2   . TYR B 1 209 ? 5.736   26.000  -8.674  1.00 36.18  ? 209  TYR B CD2   1 
ATOM   5634 C CE1   . TYR B 1 209 ? 3.422   27.454  -8.982  1.00 35.57  ? 209  TYR B CE1   1 
ATOM   5635 C CE2   . TYR B 1 209 ? 5.789   27.272  -9.222  1.00 35.90  ? 209  TYR B CE2   1 
ATOM   5636 C CZ    . TYR B 1 209 ? 4.623   27.997  -9.390  1.00 34.05  ? 209  TYR B CZ    1 
ATOM   5637 O OH    . TYR B 1 209 ? 4.658   29.253  -9.921  1.00 40.01  ? 209  TYR B OH    1 
ATOM   5638 N N     . GLY B 1 210 ? 4.337   21.607  -5.565  1.00 32.94  ? 210  GLY B N     1 
ATOM   5639 C CA    . GLY B 1 210 ? 5.033   20.359  -5.232  1.00 35.08  ? 210  GLY B CA    1 
ATOM   5640 C C     . GLY B 1 210 ? 5.374   19.619  -6.504  1.00 36.16  ? 210  GLY B C     1 
ATOM   5641 O O     . GLY B 1 210 ? 5.743   20.268  -7.507  1.00 36.51  ? 210  GLY B O     1 
ATOM   5642 N N     . PHE B 1 211 ? 5.229   18.300  -6.487  1.00 36.06  ? 211  PHE B N     1 
ATOM   5643 C CA    . PHE B 1 211 ? 5.760   17.450  -7.561  1.00 35.52  ? 211  PHE B CA    1 
ATOM   5644 C C     . PHE B 1 211 ? 4.751   17.293  -8.700  1.00 40.95  ? 211  PHE B C     1 
ATOM   5645 O O     . PHE B 1 211 ? 5.136   17.611  -9.838  1.00 64.44  ? 211  PHE B O     1 
ATOM   5646 C CB    . PHE B 1 211 ? 6.228   16.114  -7.027  1.00 32.39  ? 211  PHE B CB    1 
ATOM   5647 C CG    . PHE B 1 211 ? 6.362   15.080  -8.108  1.00 28.80  ? 211  PHE B CG    1 
ATOM   5648 C CD1   . PHE B 1 211 ? 7.273   15.255  -9.136  1.00 32.37  ? 211  PHE B CD1   1 
ATOM   5649 C CD2   . PHE B 1 211 ? 5.596   13.930  -8.083  1.00 28.54  ? 211  PHE B CD2   1 
ATOM   5650 C CE1   . PHE B 1 211 ? 7.446   14.282  -10.106 1.00 30.71  ? 211  PHE B CE1   1 
ATOM   5651 C CE2   . PHE B 1 211 ? 5.775   12.952  -9.049  1.00 29.31  ? 211  PHE B CE2   1 
ATOM   5652 C CZ    . PHE B 1 211 ? 6.704   13.126  -10.047 1.00 29.03  ? 211  PHE B CZ    1 
ATOM   5653 N N     . GLY B 1 212 ? 3.546   16.796  -8.489  1.00 37.18  ? 212  GLY B N     1 
ATOM   5654 C CA    . GLY B 1 212 ? 2.723   16.485  -9.691  1.00 31.22  ? 212  GLY B CA    1 
ATOM   5655 C C     . GLY B 1 212 ? 1.801   17.632  -10.094 1.00 28.08  ? 212  GLY B C     1 
ATOM   5656 O O     . GLY B 1 212 ? 2.211   18.786  -10.093 1.00 28.34  ? 212  GLY B O     1 
ATOM   5657 N N     . PRO B 1 213 ? 0.525   17.378  -10.461 1.00 29.93  ? 213  PRO B N     1 
ATOM   5658 C CA    . PRO B 1 213 ? -0.412  18.460  -10.785 1.00 29.23  ? 213  PRO B CA    1 
ATOM   5659 C C     . PRO B 1 213 ? -0.602  19.398  -9.586  1.00 28.01  ? 213  PRO B C     1 
ATOM   5660 O O     . PRO B 1 213 ? -0.694  18.919  -8.484  1.00 28.61  ? 213  PRO B O     1 
ATOM   5661 C CB    . PRO B 1 213 ? -1.735  17.761  -11.089 1.00 27.29  ? 213  PRO B CB    1 
ATOM   5662 C CG    . PRO B 1 213 ? -1.330  16.342  -11.421 1.00 28.59  ? 213  PRO B CG    1 
ATOM   5663 C CD    . PRO B 1 213 ? -0.110  16.063  -10.574 1.00 27.98  ? 213  PRO B CD    1 
ATOM   5664 N N     . TYR B 1 214 ? -0.615  20.703  -9.845  1.00 28.80  ? 214  TYR B N     1 
ATOM   5665 C CA    . TYR B 1 214 ? -0.628  21.783  -8.829  1.00 28.69  ? 214  TYR B CA    1 
ATOM   5666 C C     . TYR B 1 214 ? -2.080  22.110  -8.495  1.00 28.35  ? 214  TYR B C     1 
ATOM   5667 O O     . TYR B 1 214 ? -2.786  22.677  -9.314  1.00 30.11  ? 214  TYR B O     1 
ATOM   5668 C CB    . TYR B 1 214 ? 0.171   22.981  -9.351  1.00 31.91  ? 214  TYR B CB    1 
ATOM   5669 C CG    . TYR B 1 214 ? 0.002   24.261  -8.575  1.00 26.74  ? 214  TYR B CG    1 
ATOM   5670 C CD1   . TYR B 1 214 ? 0.004   24.296  -7.186  1.00 27.19  ? 214  TYR B CD1   1 
ATOM   5671 C CD2   . TYR B 1 214 ? -0.173  25.451  -9.250  1.00 29.33  ? 214  TYR B CD2   1 
ATOM   5672 C CE1   . TYR B 1 214 ? -0.201  25.482  -6.499  1.00 28.32  ? 214  TYR B CE1   1 
ATOM   5673 C CE2   . TYR B 1 214 ? -0.350  26.647  -8.586  1.00 28.45  ? 214  TYR B CE2   1 
ATOM   5674 C CZ    . TYR B 1 214 ? -0.372  26.665  -7.205  1.00 29.76  ? 214  TYR B CZ    1 
ATOM   5675 O OH    . TYR B 1 214 ? -0.535  27.878  -6.613  1.00 31.23  ? 214  TYR B OH    1 
ATOM   5676 N N     . PRO B 1 215 ? -2.557  21.769  -7.282  1.00 25.87  ? 215  PRO B N     1 
ATOM   5677 C CA    . PRO B 1 215 ? -3.980  21.817  -6.970  1.00 28.51  ? 215  PRO B CA    1 
ATOM   5678 C C     . PRO B 1 215 ? -4.532  23.031  -6.207  1.00 28.02  ? 215  PRO B C     1 
ATOM   5679 O O     . PRO B 1 215 ? -5.750  23.157  -6.178  1.00 28.69  ? 215  PRO B O     1 
ATOM   5680 C CB    . PRO B 1 215 ? -4.137  20.594  -6.046  1.00 27.82  ? 215  PRO B CB    1 
ATOM   5681 C CG    . PRO B 1 215 ? -2.797  20.521  -5.298  1.00 29.12  ? 215  PRO B CG    1 
ATOM   5682 C CD    . PRO B 1 215 ? -1.762  21.160  -6.198  1.00 26.32  ? 215  PRO B CD    1 
ATOM   5683 N N     . ASP B 1 216 ? -3.686  23.840  -5.575  1.00 27.71  ? 216  ASP B N     1 
ATOM   5684 C CA    . ASP B 1 216 ? -4.129  24.863  -4.578  1.00 27.00  ? 216  ASP B CA    1 
ATOM   5685 C C     . ASP B 1 216 ? -5.207  25.768  -5.170  1.00 25.88  ? 216  ASP B C     1 
ATOM   5686 O O     . ASP B 1 216 ? -6.135  26.104  -4.432  1.00 26.78  ? 216  ASP B O     1 
ATOM   5687 C CB    . ASP B 1 216 ? -2.971  25.711  -4.061  1.00 28.11  ? 216  ASP B CB    1 
ATOM   5688 C CG    . ASP B 1 216 ? -1.982  24.848  -3.292  1.00 29.59  ? 216  ASP B CG    1 
ATOM   5689 O OD1   . ASP B 1 216 ? -1.548  23.812  -3.851  1.00 31.30  ? 216  ASP B OD1   1 
ATOM   5690 O OD2   . ASP B 1 216 ? -1.716  25.173  -2.151  1.00 27.27  ? 216  ASP B OD2   1 
ATOM   5691 N N     . GLY B 1 217 ? -5.041  26.172  -6.430  1.00 26.21  ? 217  GLY B N     1 
ATOM   5692 C CA    . GLY B 1 217 ? -5.970  27.044  -7.175  1.00 27.94  ? 217  GLY B CA    1 
ATOM   5693 C C     . GLY B 1 217 ? -7.404  26.551  -7.097  1.00 28.48  ? 217  GLY B C     1 
ATOM   5694 O O     . GLY B 1 217 ? -8.320  27.378  -7.011  1.00 28.72  ? 217  GLY B O     1 
ATOM   5695 N N     . MET B 1 218 ? -7.586  25.238  -7.120  1.00 27.79  ? 218  MET B N     1 
ATOM   5696 C CA    . MET B 1 218 ? -8.897  24.556  -7.195  1.00 27.38  ? 218  MET B CA    1 
ATOM   5697 C C     . MET B 1 218 ? -9.626  24.680  -5.859  1.00 27.23  ? 218  MET B C     1 
ATOM   5698 O O     . MET B 1 218 ? -10.839 24.330  -5.826  1.00 23.80  ? 218  MET B O     1 
ATOM   5699 C CB    . MET B 1 218 ? -8.704  23.079  -7.529  1.00 27.14  ? 218  MET B CB    1 
ATOM   5700 C CG    . MET B 1 218 ? -8.155  22.855  -8.919  1.00 31.46  ? 218  MET B CG    1 
ATOM   5701 S SD    . MET B 1 218 ? -9.393  23.255  -10.138 1.00 41.31  ? 218  MET B SD    1 
ATOM   5702 C CE    . MET B 1 218 ? -10.510 21.877  -9.896  1.00 43.23  ? 218  MET B CE    1 
ATOM   5703 N N     . PHE B 1 219 ? -8.938  25.160  -4.827  1.00 26.86  ? 219  PHE B N     1 
ATOM   5704 C CA    . PHE B 1 219 ? -9.513  25.381  -3.477  1.00 28.02  ? 219  PHE B CA    1 
ATOM   5705 C C     . PHE B 1 219 ? -9.830  26.852  -3.285  1.00 30.19  ? 219  PHE B C     1 
ATOM   5706 O O     . PHE B 1 219 ? -10.227 27.218  -2.177  1.00 30.20  ? 219  PHE B O     1 
ATOM   5707 C CB    . PHE B 1 219 ? -8.583  24.844  -2.398  1.00 28.62  ? 219  PHE B CB    1 
ATOM   5708 C CG    . PHE B 1 219 ? -8.477  23.354  -2.513  1.00 26.78  ? 219  PHE B CG    1 
ATOM   5709 C CD1   . PHE B 1 219 ? -9.579  22.559  -2.269  1.00 26.91  ? 219  PHE B CD1   1 
ATOM   5710 C CD2   . PHE B 1 219 ? -7.333  22.766  -3.017  1.00 30.64  ? 219  PHE B CD2   1 
ATOM   5711 C CE1   . PHE B 1 219 ? -9.509  21.185  -2.424  1.00 26.19  ? 219  PHE B CE1   1 
ATOM   5712 C CE2   . PHE B 1 219 ? -7.271  21.394  -3.179  1.00 29.05  ? 219  PHE B CE2   1 
ATOM   5713 C CZ    . PHE B 1 219 ? -8.360  20.615  -2.895  1.00 29.16  ? 219  PHE B CZ    1 
ATOM   5714 N N     . THR B 1 220 ? -9.717  27.650  -4.343  1.00 27.54  ? 220  THR B N     1 
ATOM   5715 C CA    . THR B 1 220 ? -10.045 29.096  -4.269  1.00 30.77  ? 220  THR B CA    1 
ATOM   5716 C C     . THR B 1 220 ? -11.319 29.337  -5.102  1.00 30.21  ? 220  THR B C     1 
ATOM   5717 O O     . THR B 1 220 ? -11.491 28.626  -6.121  1.00 30.11  ? 220  THR B O     1 
ATOM   5718 C CB    . THR B 1 220 ? -8.841  29.951  -4.673  1.00 33.46  ? 220  THR B CB    1 
ATOM   5719 O OG1   . THR B 1 220 ? -8.657  29.681  -6.061  1.00 32.79  ? 220  THR B OG1   1 
ATOM   5720 C CG2   . THR B 1 220 ? -7.589  29.658  -3.859  1.00 33.35  ? 220  THR B CG2   1 
ATOM   5721 N N     . GLN B 1 221 ? -12.161 30.266  -4.644  1.00 28.78  ? 221  GLN B N     1 
ATOM   5722 C CA    . GLN B 1 221 ? -13.554 30.532  -5.107  1.00 29.34  ? 221  GLN B CA    1 
ATOM   5723 C C     . GLN B 1 221 ? -14.256 29.186  -5.336  1.00 29.52  ? 221  GLN B C     1 
ATOM   5724 O O     . GLN B 1 221 ? -14.802 28.949  -6.426  1.00 28.88  ? 221  GLN B O     1 
ATOM   5725 C CB    . GLN B 1 221 ? -13.512 31.443  -6.333  1.00 29.73  ? 221  GLN B CB    1 
ATOM   5726 C CG    . GLN B 1 221 ? -13.172 32.883  -5.975  1.00 28.82  ? 221  GLN B CG    1 
ATOM   5727 C CD    . GLN B 1 221 ? -13.326 33.821  -7.142  1.00 29.46  ? 221  GLN B CD    1 
ATOM   5728 O OE1   . GLN B 1 221 ? -13.923 33.475  -8.150  1.00 32.98  ? 221  GLN B OE1   1 
ATOM   5729 N NE2   . GLN B 1 221 ? -12.759 35.010  -7.023  1.00 31.46  ? 221  GLN B NE2   1 
ATOM   5730 N N     . SER B 1 222 ? -14.166 28.293  -4.352  1.00 26.91  ? 222  SER B N     1 
ATOM   5731 C CA    . SER B 1 222 ? -14.355 26.843  -4.577  1.00 29.09  ? 222  SER B CA    1 
ATOM   5732 C C     . SER B 1 222 ? -15.062 26.251  -3.375  1.00 29.64  ? 222  SER B C     1 
ATOM   5733 O O     . SER B 1 222 ? -14.962 26.821  -2.262  1.00 34.68  ? 222  SER B O     1 
ATOM   5734 C CB    . SER B 1 222 ? -13.016 26.195  -4.873  1.00 31.58  ? 222  SER B CB    1 
ATOM   5735 O OG    . SER B 1 222 ? -12.950 24.831  -4.511  1.00 31.61  ? 222  SER B OG    1 
ATOM   5736 N N     . ASN B 1 223 ? -15.767 25.163  -3.638  1.00 33.47  ? 223  ASN B N     1 
ATOM   5737 C CA    . ASN B 1 223 ? -16.483 24.347  -2.634  1.00 32.20  ? 223  ASN B CA    1 
ATOM   5738 C C     . ASN B 1 223 ? -15.892 22.938  -2.637  1.00 34.06  ? 223  ASN B C     1 
ATOM   5739 O O     . ASN B 1 223 ? -16.664 22.006  -2.308  1.00 35.85  ? 223  ASN B O     1 
ATOM   5740 C CB    . ASN B 1 223 ? -17.979 24.380  -2.922  1.00 31.40  ? 223  ASN B CB    1 
ATOM   5741 C CG    . ASN B 1 223 ? -18.336 23.891  -4.306  1.00 33.14  ? 223  ASN B CG    1 
ATOM   5742 O OD1   . ASN B 1 223 ? -17.494 23.330  -4.994  1.00 34.44  ? 223  ASN B OD1   1 
ATOM   5743 N ND2   . ASN B 1 223 ? -19.597 24.044  -4.697  1.00 36.49  ? 223  ASN B ND2   1 
ATOM   5744 N N     . LEU B 1 224 ? -14.606 22.773  -3.010  1.00 28.50  ? 224  LEU B N     1 
ATOM   5745 C CA    . LEU B 1 224 ? -13.946 21.430  -3.034  1.00 29.69  ? 224  LEU B CA    1 
ATOM   5746 C C     . LEU B 1 224 ? -13.286 21.094  -1.691  1.00 29.84  ? 224  LEU B C     1 
ATOM   5747 O O     . LEU B 1 224 ? -12.739 19.986  -1.581  1.00 25.93  ? 224  LEU B O     1 
ATOM   5748 C CB    . LEU B 1 224 ? -12.911 21.376  -4.159  1.00 30.74  ? 224  LEU B CB    1 
ATOM   5749 C CG    . LEU B 1 224 ? -13.487 21.627  -5.545  1.00 29.45  ? 224  LEU B CG    1 
ATOM   5750 C CD1   . LEU B 1 224 ? -12.444 21.367  -6.618  1.00 32.79  ? 224  LEU B CD1   1 
ATOM   5751 C CD2   . LEU B 1 224 ? -14.720 20.783  -5.767  1.00 29.12  ? 224  LEU B CD2   1 
ATOM   5752 N N     . GLY B 1 225 ? -13.341 21.963  -0.684  1.00 29.82  ? 225  GLY B N     1 
ATOM   5753 C CA    . GLY B 1 225 ? -12.833 21.520  0.627   1.00 31.40  ? 225  GLY B CA    1 
ATOM   5754 C C     . GLY B 1 225 ? -12.768 22.611  1.654   1.00 30.42  ? 225  GLY B C     1 
ATOM   5755 O O     . GLY B 1 225 ? -12.977 23.763  1.278   1.00 33.62  ? 225  GLY B O     1 
ATOM   5756 N N     . ILE B 1 226 ? -12.489 22.235  2.902   1.00 30.20  ? 226  ILE B N     1 
ATOM   5757 C CA    . ILE B 1 226 ? -12.325 23.183  4.042   1.00 31.46  ? 226  ILE B CA    1 
ATOM   5758 C C     . ILE B 1 226 ? -10.836 23.262  4.395   1.00 33.31  ? 226  ILE B C     1 
ATOM   5759 O O     . ILE B 1 226 ? -10.293 22.265  4.868   1.00 34.21  ? 226  ILE B O     1 
ATOM   5760 C CB    . ILE B 1 226 ? -13.206 22.777  5.238   1.00 32.59  ? 226  ILE B CB    1 
ATOM   5761 C CG1   . ILE B 1 226 ? -14.663 22.597  4.795   1.00 34.15  ? 226  ILE B CG1   1 
ATOM   5762 C CG2   . ILE B 1 226 ? -13.084 23.773  6.378   1.00 30.35  ? 226  ILE B CG2   1 
ATOM   5763 C CD1   . ILE B 1 226 ? -15.574 21.996  5.843   1.00 36.29  ? 226  ILE B CD1   1 
ATOM   5764 N N     . VAL B 1 227 ? -10.230 24.429  4.150   1.00 30.74  ? 227  VAL B N     1 
ATOM   5765 C CA    . VAL B 1 227 ? -8.819  24.754  4.442   1.00 30.76  ? 227  VAL B CA    1 
ATOM   5766 C C     . VAL B 1 227 ? -8.679  24.918  5.963   1.00 31.38  ? 227  VAL B C     1 
ATOM   5767 O O     . VAL B 1 227 ? -9.470  25.671  6.561   1.00 31.43  ? 227  VAL B O     1 
ATOM   5768 C CB    . VAL B 1 227 ? -8.378  26.004  3.669   1.00 27.90  ? 227  VAL B CB    1 
ATOM   5769 C CG1   . VAL B 1 227 ? -6.968  26.380  4.008   1.00 27.68  ? 227  VAL B CG1   1 
ATOM   5770 C CG2   . VAL B 1 227 ? -8.534  25.803  2.167   1.00 31.72  ? 227  VAL B CG2   1 
ATOM   5771 N N     . THR B 1 228 ? -7.702  24.242  6.552   1.00 27.29  ? 228  THR B N     1 
ATOM   5772 C CA    . THR B 1 228 ? -7.475  24.208  8.026   1.00 28.16  ? 228  THR B CA    1 
ATOM   5773 C C     . THR B 1 228 ? -6.157  24.902  8.351   1.00 27.97  ? 228  THR B C     1 
ATOM   5774 O O     . THR B 1 228 ? -6.004  25.349  9.482   1.00 25.11  ? 228  THR B O     1 
ATOM   5775 C CB    . THR B 1 228 ? -7.536  22.767  8.541   1.00 29.44  ? 228  THR B CB    1 
ATOM   5776 O OG1   . THR B 1 228 ? -6.613  21.974  7.803   1.00 32.39  ? 228  THR B OG1   1 
ATOM   5777 C CG2   . THR B 1 228 ? -8.912  22.160  8.404   1.00 28.67  ? 228  THR B CG2   1 
ATOM   5778 N N     . LYS B 1 229 ? -5.248  24.976  7.375   1.00 26.28  ? 229  LYS B N     1 
ATOM   5779 C CA    . LYS B 1 229 ? -3.942  25.657  7.495   1.00 27.38  ? 229  LYS B CA    1 
ATOM   5780 C C     . LYS B 1 229 ? -3.600  26.211  6.128   1.00 25.85  ? 229  LYS B C     1 
ATOM   5781 O O     . LYS B 1 229 ? -3.933  25.560  5.131   1.00 25.55  ? 229  LYS B O     1 
ATOM   5782 C CB    . LYS B 1 229 ? -2.804  24.721  7.927   1.00 28.41  ? 229  LYS B CB    1 
ATOM   5783 C CG    . LYS B 1 229 ? -3.055  23.824  9.127   1.00 28.78  ? 229  LYS B CG    1 
ATOM   5784 C CD    . LYS B 1 229 ? -1.805  23.071  9.556   1.00 30.03  ? 229  LYS B CD    1 
ATOM   5785 C CE    . LYS B 1 229 ? -1.888  22.499  10.960  1.00 31.06  ? 229  LYS B CE    1 
ATOM   5786 N NZ    . LYS B 1 229 ? -3.177  21.813  11.205  1.00 34.39  ? 229  LYS B NZ    1 
ATOM   5787 N N     . MET B 1 230 ? -3.009  27.394  6.123   1.00 28.31  ? 230  MET B N     1 
ATOM   5788 C CA    . MET B 1 230 ? -2.538  28.068  4.895   1.00 30.09  ? 230  MET B CA    1 
ATOM   5789 C C     . MET B 1 230 ? -1.241  28.804  5.199   1.00 28.37  ? 230  MET B C     1 
ATOM   5790 O O     . MET B 1 230 ? -1.175  29.498  6.237   1.00 27.69  ? 230  MET B O     1 
ATOM   5791 C CB    . MET B 1 230 ? -3.555  29.082  4.398   1.00 32.85  ? 230  MET B CB    1 
ATOM   5792 C CG    . MET B 1 230 ? -3.323  29.465  2.956   1.00 32.39  ? 230  MET B CG    1 
ATOM   5793 S SD    . MET B 1 230 ? -4.435  30.776  2.519   1.00 32.70  ? 230  MET B SD    1 
ATOM   5794 C CE    . MET B 1 230 ? -3.434  32.153  3.068   1.00 35.42  ? 230  MET B CE    1 
ATOM   5795 N N     . GLY B 1 231 ? -0.251  28.615  4.328   1.00 25.57  ? 231  GLY B N     1 
ATOM   5796 C CA    . GLY B 1 231 ? 0.994   29.384  4.324   1.00 24.34  ? 231  GLY B CA    1 
ATOM   5797 C C     . GLY B 1 231 ? 0.840   30.646  3.509   1.00 28.11  ? 231  GLY B C     1 
ATOM   5798 O O     . GLY B 1 231 ? 0.054   30.648  2.506   1.00 27.55  ? 231  GLY B O     1 
ATOM   5799 N N     . ILE B 1 232 ? 1.586   31.679  3.877   1.00 27.55  ? 232  ILE B N     1 
ATOM   5800 C CA    . ILE B 1 232 ? 1.653   32.912  3.057   1.00 29.89  ? 232  ILE B CA    1 
ATOM   5801 C C     . ILE B 1 232 ? 3.063   33.466  3.176   1.00 29.57  ? 232  ILE B C     1 
ATOM   5802 O O     . ILE B 1 232 ? 3.610   33.476  4.292   1.00 29.75  ? 232  ILE B O     1 
ATOM   5803 C CB    . ILE B 1 232 ? 0.547   33.925  3.445   1.00 34.55  ? 232  ILE B CB    1 
ATOM   5804 C CG1   . ILE B 1 232 ? 0.405   35.039  2.403   1.00 37.79  ? 232  ILE B CG1   1 
ATOM   5805 C CG2   . ILE B 1 232 ? 0.737   34.505  4.844   1.00 32.35  ? 232  ILE B CG2   1 
ATOM   5806 C CD1   . ILE B 1 232 ? -0.683  34.788  1.410   1.00 47.18  ? 232  ILE B CD1   1 
ATOM   5807 N N     . ALA B 1 233 ? 3.631   33.850  2.038   1.00 25.53  ? 233  ALA B N     1 
ATOM   5808 C CA    . ALA B 1 233 ? 4.869   34.631  1.945   1.00 27.63  ? 233  ALA B CA    1 
ATOM   5809 C C     . ALA B 1 233 ? 4.589   36.017  2.537   1.00 31.85  ? 233  ALA B C     1 
ATOM   5810 O O     . ALA B 1 233 ? 3.466   36.541  2.370   1.00 30.75  ? 233  ALA B O     1 
ATOM   5811 C CB    . ALA B 1 233 ? 5.330   34.701  0.521   1.00 26.77  ? 233  ALA B CB    1 
ATOM   5812 N N     . LEU B 1 234 ? 5.594   36.584  3.202   1.00 31.75  ? 234  LEU B N     1 
ATOM   5813 C CA    . LEU B 1 234 ? 5.521   37.908  3.865   1.00 32.82  ? 234  LEU B CA    1 
ATOM   5814 C C     . LEU B 1 234 ? 6.691   38.737  3.384   1.00 31.85  ? 234  LEU B C     1 
ATOM   5815 O O     . LEU B 1 234 ? 7.870   38.265  3.414   1.00 33.89  ? 234  LEU B O     1 
ATOM   5816 C CB    . LEU B 1 234 ? 5.548   37.740  5.383   1.00 36.30  ? 234  LEU B CB    1 
ATOM   5817 C CG    . LEU B 1 234 ? 4.345   37.026  5.975   1.00 34.45  ? 234  LEU B CG    1 
ATOM   5818 C CD1   . LEU B 1 234 ? 4.539   36.821  7.474   1.00 37.35  ? 234  LEU B CD1   1 
ATOM   5819 C CD2   . LEU B 1 234 ? 3.067   37.807  5.698   1.00 35.41  ? 234  LEU B CD2   1 
ATOM   5820 N N     . MET B 1 235 ? 6.356   39.914  2.903   1.00 31.08  ? 235  MET B N     1 
ATOM   5821 C CA    . MET B 1 235 ? 7.330   40.833  2.306   1.00 32.64  ? 235  MET B CA    1 
ATOM   5822 C C     . MET B 1 235 ? 8.161   41.460  3.440   1.00 37.07  ? 235  MET B C     1 
ATOM   5823 O O     . MET B 1 235 ? 7.647   41.670  4.560   1.00 29.79  ? 235  MET B O     1 
ATOM   5824 C CB    . MET B 1 235 ? 6.643   41.926  1.491   1.00 34.99  ? 235  MET B CB    1 
ATOM   5825 C CG    . MET B 1 235 ? 7.633   42.685  0.645   1.00 37.59  ? 235  MET B CG    1 
ATOM   5826 S SD    . MET B 1 235 ? 6.843   43.874  -0.425  1.00 44.10  ? 235  MET B SD    1 
ATOM   5827 C CE    . MET B 1 235 ? 6.795   45.303  0.652   1.00 43.12  ? 235  MET B CE    1 
ATOM   5828 N N     . GLN B 1 236 ? 9.419   41.701  3.125   1.00 36.95  ? 236  GLN B N     1 
ATOM   5829 C CA    . GLN B 1 236 ? 10.386  42.461  3.938   1.00 41.52  ? 236  GLN B CA    1 
ATOM   5830 C C     . GLN B 1 236 ? 10.015  43.943  3.878   1.00 38.26  ? 236  GLN B C     1 
ATOM   5831 O O     . GLN B 1 236 ? 9.816   44.465  2.774   1.00 34.11  ? 236  GLN B O     1 
ATOM   5832 C CB    . GLN B 1 236 ? 11.772  42.230  3.351   1.00 44.30  ? 236  GLN B CB    1 
ATOM   5833 C CG    . GLN B 1 236 ? 12.898  42.218  4.357   1.00 50.67  ? 236  GLN B CG    1 
ATOM   5834 C CD    . GLN B 1 236 ? 14.068  41.496  3.739   1.00 47.51  ? 236  GLN B CD    1 
ATOM   5835 O OE1   . GLN B 1 236 ? 14.160  40.279  3.819   1.00 49.08  ? 236  GLN B OE1   1 
ATOM   5836 N NE2   . GLN B 1 236 ? 14.937  42.248  3.084   1.00 52.66  ? 236  GLN B NE2   1 
ATOM   5837 N N     . LYS B 1 237 ? 9.891   44.572  5.039   1.00 38.08  ? 237  LYS B N     1 
ATOM   5838 C CA    . LYS B 1 237 ? 9.770   46.047  5.184   1.00 40.99  ? 237  LYS B CA    1 
ATOM   5839 C C     . LYS B 1 237 ? 10.945  46.702  4.468   1.00 41.10  ? 237  LYS B C     1 
ATOM   5840 O O     . LYS B 1 237 ? 12.086  46.378  4.780   1.00 40.78  ? 237  LYS B O     1 
ATOM   5841 C CB    . LYS B 1 237 ? 9.781   46.397  6.673   1.00 40.24  ? 237  LYS B CB    1 
ATOM   5842 C CG    . LYS B 1 237 ? 8.537   47.068  7.200   1.00 42.27  ? 237  LYS B CG    1 
ATOM   5843 C CD    . LYS B 1 237 ? 8.595   47.243  8.693   1.00 39.74  ? 237  LYS B CD    1 
ATOM   5844 C CE    . LYS B 1 237 ? 7.516   46.469  9.407   1.00 39.21  ? 237  LYS B CE    1 
ATOM   5845 N NZ    . LYS B 1 237 ? 7.578   46.726  10.862  1.00 44.40  ? 237  LYS B NZ    1 
ATOM   5846 N N     . PRO B 1 238 ? 10.716  47.613  3.490   1.00 43.48  ? 238  PRO B N     1 
ATOM   5847 C CA    . PRO B 1 238 ? 11.799  48.349  2.843   1.00 43.53  ? 238  PRO B CA    1 
ATOM   5848 C C     . PRO B 1 238 ? 12.314  49.369  3.845   1.00 41.02  ? 238  PRO B C     1 
ATOM   5849 O O     . PRO B 1 238 ? 11.672  49.575  4.869   1.00 38.98  ? 238  PRO B O     1 
ATOM   5850 C CB    . PRO B 1 238 ? 11.116  49.021  1.645   1.00 47.33  ? 238  PRO B CB    1 
ATOM   5851 C CG    . PRO B 1 238 ? 9.728   49.268  2.163   1.00 50.01  ? 238  PRO B CG    1 
ATOM   5852 C CD    . PRO B 1 238 ? 9.402   48.036  2.988   1.00 49.39  ? 238  PRO B CD    1 
ATOM   5853 N N     . PRO B 1 239 ? 13.492  49.989  3.614   1.00 42.35  ? 239  PRO B N     1 
ATOM   5854 C CA    . PRO B 1 239 ? 14.081  50.889  4.604   1.00 43.84  ? 239  PRO B CA    1 
ATOM   5855 C C     . PRO B 1 239 ? 13.188  52.122  4.806   1.00 46.50  ? 239  PRO B C     1 
ATOM   5856 O O     . PRO B 1 239 ? 13.135  52.619  5.904   1.00 43.83  ? 239  PRO B O     1 
ATOM   5857 C CB    . PRO B 1 239 ? 15.465  51.245  4.052   1.00 42.73  ? 239  PRO B CB    1 
ATOM   5858 C CG    . PRO B 1 239 ? 15.430  50.856  2.591   1.00 46.11  ? 239  PRO B CG    1 
ATOM   5859 C CD    . PRO B 1 239 ? 14.349  49.800  2.435   1.00 44.24  ? 239  PRO B CD    1 
ATOM   5860 N N     . ALA B 1 240 ? 12.487  52.550  3.752   1.00 45.54  ? 240  ALA B N     1 
ATOM   5861 C CA    . ALA B 1 240 ? 11.624  53.750  3.757   1.00 42.82  ? 240  ALA B CA    1 
ATOM   5862 C C     . ALA B 1 240 ? 10.556  53.613  2.674   1.00 47.14  ? 240  ALA B C     1 
ATOM   5863 O O     . ALA B 1 240 ? 10.727  52.833  1.677   1.00 41.70  ? 240  ALA B O     1 
ATOM   5864 C CB    . ALA B 1 240 ? 12.445  54.997  3.534   1.00 45.43  ? 240  ALA B CB    1 
ATOM   5865 N N     . SER B 1 241 ? 9.516   54.407  2.866   1.00 47.97  ? 241  SER B N     1 
ATOM   5866 C CA    . SER B 1 241 ? 8.241   54.386  2.120   1.00 50.06  ? 241  SER B CA    1 
ATOM   5867 C C     . SER B 1 241 ? 7.742   55.822  1.999   1.00 49.67  ? 241  SER B C     1 
ATOM   5868 O O     . SER B 1 241 ? 8.058   56.633  2.900   1.00 46.26  ? 241  SER B O     1 
ATOM   5869 C CB    . SER B 1 241 ? 7.246   53.541  2.842   1.00 49.74  ? 241  SER B CB    1 
ATOM   5870 O OG    . SER B 1 241 ? 6.109   53.339  2.036   1.00 66.87  ? 241  SER B OG    1 
ATOM   5871 N N     . MET B 1 242 ? 6.994   56.120  0.941   1.00 44.77  ? 242  MET B N     1 
ATOM   5872 C CA    . MET B 1 242 ? 6.139   57.329  0.908   1.00 47.04  ? 242  MET B CA    1 
ATOM   5873 C C     . MET B 1 242 ? 4.979   57.120  -0.073  1.00 44.71  ? 242  MET B C     1 
ATOM   5874 O O     . MET B 1 242 ? 5.188   56.567  -1.201  1.00 37.31  ? 242  MET B O     1 
ATOM   5875 C CB    . MET B 1 242 ? 6.945   58.583  0.558   1.00 50.87  ? 242  MET B CB    1 
ATOM   5876 C CG    . MET B 1 242 ? 7.075   58.835  -0.900  1.00 59.98  ? 242  MET B CG    1 
ATOM   5877 S SD    . MET B 1 242 ? 7.212   60.590  -1.240  1.00 75.34  ? 242  MET B SD    1 
ATOM   5878 C CE    . MET B 1 242 ? 6.934   60.562  -3.010  1.00 58.64  ? 242  MET B CE    1 
ATOM   5879 N N     . THR B 1 243 ? 3.787   57.502  0.380   1.00 42.01  ? 243  THR B N     1 
ATOM   5880 C CA    . THR B 1 243 ? 2.524   57.411  -0.382  1.00 41.78  ? 243  THR B CA    1 
ATOM   5881 C C     . THR B 1 243 ? 2.194   58.796  -0.944  1.00 40.00  ? 243  THR B C     1 
ATOM   5882 O O     . THR B 1 243 ? 2.441   59.799  -0.256  1.00 42.47  ? 243  THR B O     1 
ATOM   5883 C CB    . THR B 1 243 ? 1.447   56.801  0.504   1.00 39.89  ? 243  THR B CB    1 
ATOM   5884 O OG1   . THR B 1 243 ? 2.045   55.571  0.925   1.00 41.25  ? 243  THR B OG1   1 
ATOM   5885 C CG2   . THR B 1 243 ? 0.129   56.597  -0.212  1.00 39.83  ? 243  THR B CG2   1 
ATOM   5886 N N     . TYR B 1 244 ? 1.706   58.841  -2.177  1.00 37.31  ? 244  TYR B N     1 
ATOM   5887 C CA    . TYR B 1 244 ? 1.366   60.105  -2.862  1.00 36.51  ? 244  TYR B CA    1 
ATOM   5888 C C     . TYR B 1 244 ? -0.044  59.989  -3.448  1.00 39.99  ? 244  TYR B C     1 
ATOM   5889 O O     . TYR B 1 244 ? -0.630  58.870  -3.549  1.00 36.61  ? 244  TYR B O     1 
ATOM   5890 C CB    . TYR B 1 244 ? 2.432   60.446  -3.897  1.00 35.57  ? 244  TYR B CB    1 
ATOM   5891 C CG    . TYR B 1 244 ? 2.544   59.394  -4.959  1.00 34.60  ? 244  TYR B CG    1 
ATOM   5892 C CD1   . TYR B 1 244 ? 3.288   58.255  -4.730  1.00 37.20  ? 244  TYR B CD1   1 
ATOM   5893 C CD2   . TYR B 1 244 ? 1.834   59.490  -6.140  1.00 34.95  ? 244  TYR B CD2   1 
ATOM   5894 C CE1   . TYR B 1 244 ? 3.348   57.234  -5.662  1.00 35.99  ? 244  TYR B CE1   1 
ATOM   5895 C CE2   . TYR B 1 244 ? 1.916   58.502  -7.105  1.00 37.31  ? 244  TYR B CE2   1 
ATOM   5896 C CZ    . TYR B 1 244 ? 2.664   57.364  -6.851  1.00 34.15  ? 244  TYR B CZ    1 
ATOM   5897 O OH    . TYR B 1 244 ? 2.770   56.383  -7.765  1.00 33.78  ? 244  TYR B OH    1 
ATOM   5898 N N     . GLN B 1 245 ? -0.585  61.162  -3.763  1.00 42.54  ? 245  GLN B N     1 
ATOM   5899 C CA    . GLN B 1 245 ? -1.943  61.390  -4.316  1.00 40.63  ? 245  GLN B CA    1 
ATOM   5900 C C     . GLN B 1 245 ? -1.778  62.311  -5.515  1.00 37.94  ? 245  GLN B C     1 
ATOM   5901 O O     . GLN B 1 245 ? -1.049  63.315  -5.389  1.00 36.74  ? 245  GLN B O     1 
ATOM   5902 C CB    . GLN B 1 245 ? -2.829  62.006  -3.240  1.00 39.41  ? 245  GLN B CB    1 
ATOM   5903 C CG    . GLN B 1 245 ? -4.236  62.349  -3.704  1.00 41.46  ? 245  GLN B CG    1 
ATOM   5904 C CD    . GLN B 1 245 ? -4.788  63.489  -2.882  1.00 39.44  ? 245  GLN B CD    1 
ATOM   5905 O OE1   . GLN B 1 245 ? -4.188  64.569  -2.816  1.00 38.16  ? 245  GLN B OE1   1 
ATOM   5906 N NE2   . GLN B 1 245 ? -5.919  63.248  -2.239  1.00 39.24  ? 245  GLN B NE2   1 
ATOM   5907 N N     . ILE B 1 246 ? -2.307  61.905  -6.663  1.00 35.19  ? 246  ILE B N     1 
ATOM   5908 C CA    . ILE B 1 246 ? -2.435  62.769  -7.866  1.00 37.24  ? 246  ILE B CA    1 
ATOM   5909 C C     . ILE B 1 246 ? -3.938  63.012  -8.044  1.00 38.72  ? 246  ILE B C     1 
ATOM   5910 O O     . ILE B 1 246 ? -4.693  62.019  -8.122  1.00 34.75  ? 246  ILE B O     1 
ATOM   5911 C CB    . ILE B 1 246 ? -1.834  62.145  -9.137  1.00 36.33  ? 246  ILE B CB    1 
ATOM   5912 C CG1   . ILE B 1 246 ? -0.524  61.384  -8.897  1.00 37.91  ? 246  ILE B CG1   1 
ATOM   5913 C CG2   . ILE B 1 246 ? -1.689  63.198  -10.213 1.00 34.69  ? 246  ILE B CG2   1 
ATOM   5914 C CD1   . ILE B 1 246 ? -0.111  60.549  -10.095 1.00 39.40  ? 246  ILE B CD1   1 
ATOM   5915 N N     . THR B 1 247 ? -4.352  64.277  -8.068  1.00 36.05  ? 247  THR B N     1 
ATOM   5916 C CA    . THR B 1 247 ? -5.760  64.685  -8.300  1.00 38.06  ? 247  THR B CA    1 
ATOM   5917 C C     . THR B 1 247 ? -5.870  65.074  -9.774  1.00 35.40  ? 247  THR B C     1 
ATOM   5918 O O     . THR B 1 247 ? -4.952  65.728  -10.274 1.00 38.47  ? 247  THR B O     1 
ATOM   5919 C CB    . THR B 1 247 ? -6.216  65.759  -7.301  1.00 35.93  ? 247  THR B CB    1 
ATOM   5920 O OG1   . THR B 1 247 ? -5.479  66.971  -7.479  1.00 39.37  ? 247  THR B OG1   1 
ATOM   5921 C CG2   . THR B 1 247 ? -6.086  65.279  -5.878  1.00 35.75  ? 247  THR B CG2   1 
ATOM   5922 N N     . PHE B 1 248 ? -6.903  64.578  -10.447 1.00 34.30  ? 248  PHE B N     1 
ATOM   5923 C CA    . PHE B 1 248 ? -7.176  64.855  -11.870 1.00 36.19  ? 248  PHE B CA    1 
ATOM   5924 C C     . PHE B 1 248 ? -8.559  65.491  -11.958 1.00 35.99  ? 248  PHE B C     1 
ATOM   5925 O O     . PHE B 1 248 ? -9.515  64.925  -11.418 1.00 37.52  ? 248  PHE B O     1 
ATOM   5926 C CB    . PHE B 1 248 ? -7.075  63.575  -12.696 1.00 37.39  ? 248  PHE B CB    1 
ATOM   5927 C CG    . PHE B 1 248 ? -5.701  62.966  -12.726 1.00 36.29  ? 248  PHE B CG    1 
ATOM   5928 C CD1   . PHE B 1 248 ? -4.741  63.438  -13.603 1.00 37.83  ? 248  PHE B CD1   1 
ATOM   5929 C CD2   . PHE B 1 248 ? -5.367  61.928  -11.864 1.00 37.13  ? 248  PHE B CD2   1 
ATOM   5930 C CE1   . PHE B 1 248 ? -3.481  62.854  -13.654 1.00 40.36  ? 248  PHE B CE1   1 
ATOM   5931 C CE2   . PHE B 1 248 ? -4.108  61.351  -11.912 1.00 37.52  ? 248  PHE B CE2   1 
ATOM   5932 C CZ    . PHE B 1 248 ? -3.169  61.811  -12.805 1.00 40.02  ? 248  PHE B CZ    1 
ATOM   5933 N N     . GLU B 1 249 ? -8.633  66.649  -12.607 1.00 41.46  ? 249  GLU B N     1 
ATOM   5934 C CA    . GLU B 1 249 ? -9.810  67.553  -12.581 1.00 39.78  ? 249  GLU B CA    1 
ATOM   5935 C C     . GLU B 1 249 ? -10.973 66.921  -13.357 1.00 39.14  ? 249  GLU B C     1 
ATOM   5936 O O     . GLU B 1 249 ? -12.102 67.061  -12.922 1.00 38.81  ? 249  GLU B O     1 
ATOM   5937 C CB    . GLU B 1 249 ? -9.418  68.929  -13.141 1.00 41.92  ? 249  GLU B CB    1 
ATOM   5938 C CG    . GLU B 1 249 ? -8.621  69.782  -12.173 1.00 39.72  ? 249  GLU B CG    1 
ATOM   5939 C CD    . GLU B 1 249 ? -9.333  70.005  -10.848 1.00 46.44  ? 249  GLU B CD    1 
ATOM   5940 O OE1   . GLU B 1 249 ? -10.535 70.368  -10.873 1.00 50.78  ? 249  GLU B OE1   1 
ATOM   5941 O OE2   . GLU B 1 249 ? -8.718  69.754  -9.803  1.00 46.95  ? 249  GLU B OE2   1 
ATOM   5942 N N     . ASN B 1 250 ? -10.707 66.257  -14.479 1.00 45.74  ? 250  ASN B N     1 
ATOM   5943 C CA    . ASN B 1 250 ? -11.758 65.919  -15.476 1.00 42.73  ? 250  ASN B CA    1 
ATOM   5944 C C     . ASN B 1 250 ? -12.093 64.439  -15.404 1.00 38.65  ? 250  ASN B C     1 
ATOM   5945 O O     . ASN B 1 250 ? -11.165 63.621  -15.375 1.00 39.84  ? 250  ASN B O     1 
ATOM   5946 C CB    . ASN B 1 250 ? -11.335 66.287  -16.895 1.00 45.42  ? 250  ASN B CB    1 
ATOM   5947 C CG    . ASN B 1 250 ? -10.848 67.712  -16.961 1.00 45.36  ? 250  ASN B CG    1 
ATOM   5948 O OD1   . ASN B 1 250 ? -11.611 68.637  -16.701 1.00 49.57  ? 250  ASN B OD1   1 
ATOM   5949 N ND2   . ASN B 1 250 ? -9.573  67.893  -17.238 1.00 45.12  ? 250  ASN B ND2   1 
ATOM   5950 N N     . GLU B 1 251 ? -13.387 64.138  -15.418 1.00 37.49  ? 251  GLU B N     1 
ATOM   5951 C CA    . GLU B 1 251 ? -13.966 62.827  -15.801 1.00 37.60  ? 251  GLU B CA    1 
ATOM   5952 C C     . GLU B 1 251 ? -13.181 62.159  -16.945 1.00 39.03  ? 251  GLU B C     1 
ATOM   5953 O O     . GLU B 1 251 ? -12.902 60.943  -16.861 1.00 34.16  ? 251  GLU B O     1 
ATOM   5954 C CB    . GLU B 1 251 ? -15.374 63.057  -16.330 1.00 42.30  ? 251  GLU B CB    1 
ATOM   5955 C CG    . GLU B 1 251 ? -16.370 63.368  -15.244 1.00 46.22  ? 251  GLU B CG    1 
ATOM   5956 C CD    . GLU B 1 251 ? -17.808 63.367  -15.718 1.00 39.36  ? 251  GLU B CD    1 
ATOM   5957 O OE1   . GLU B 1 251 ? -18.060 63.053  -16.892 1.00 44.17  ? 251  GLU B OE1   1 
ATOM   5958 O OE2   . GLU B 1 251 ? -18.667 63.651  -14.896 1.00 47.99  ? 251  GLU B OE2   1 
ATOM   5959 N N     . SER B 1 252 ? -12.956 62.907  -18.026 1.00 32.30  ? 252  SER B N     1 
ATOM   5960 C CA    . SER B 1 252 ? -12.446 62.402  -19.317 1.00 35.89  ? 252  SER B CA    1 
ATOM   5961 C C     . SER B 1 252 ? -10.929 62.171  -19.230 1.00 35.89  ? 252  SER B C     1 
ATOM   5962 O O     . SER B 1 252 ? -10.388 61.595  -20.155 1.00 37.50  ? 252  SER B O     1 
ATOM   5963 C CB    . SER B 1 252 ? -12.812 63.358  -20.422 1.00 36.83  ? 252  SER B CB    1 
ATOM   5964 O OG    . SER B 1 252 ? -12.293 64.653  -20.139 1.00 35.37  ? 252  SER B OG    1 
ATOM   5965 N N     . ASP B 1 253 ? -10.286 62.549  -18.123 1.00 36.20  ? 253  ASP B N     1 
ATOM   5966 C CA    . ASP B 1 253 ? -8.823  62.371  -17.919 1.00 38.05  ? 253  ASP B CA    1 
ATOM   5967 C C     . ASP B 1 253 ? -8.524  60.883  -17.714 1.00 36.15  ? 253  ASP B C     1 
ATOM   5968 O O     . ASP B 1 253 ? -7.366  60.484  -17.918 1.00 34.14  ? 253  ASP B O     1 
ATOM   5969 C CB    . ASP B 1 253 ? -8.286  63.135  -16.705 1.00 37.15  ? 253  ASP B CB    1 
ATOM   5970 C CG    . ASP B 1 253 ? -8.157  64.644  -16.860 1.00 40.35  ? 253  ASP B CG    1 
ATOM   5971 O OD1   . ASP B 1 253 ? -8.090  65.132  -18.014 1.00 38.50  ? 253  ASP B OD1   1 
ATOM   5972 O OD2   . ASP B 1 253 ? -8.113  65.323  -15.809 1.00 38.86  ? 253  ASP B OD2   1 
ATOM   5973 N N     . LEU B 1 254 ? -9.529  60.120  -17.286 1.00 38.39  ? 254  LEU B N     1 
ATOM   5974 C CA    . LEU B 1 254 ? -9.443  58.659  -17.046 1.00 35.68  ? 254  LEU B CA    1 
ATOM   5975 C C     . LEU B 1 254 ? -8.660  58.002  -18.185 1.00 34.27  ? 254  LEU B C     1 
ATOM   5976 O O     . LEU B 1 254 ? -7.843  57.147  -17.900 1.00 34.53  ? 254  LEU B O     1 
ATOM   5977 C CB    . LEU B 1 254 ? -10.854 58.081  -16.940 1.00 35.27  ? 254  LEU B CB    1 
ATOM   5978 C CG    . LEU B 1 254 ? -10.909 56.554  -16.859 1.00 39.23  ? 254  LEU B CG    1 
ATOM   5979 C CD1   . LEU B 1 254 ? -10.167 56.028  -15.622 1.00 35.09  ? 254  LEU B CD1   1 
ATOM   5980 C CD2   . LEU B 1 254 ? -12.345 56.057  -16.888 1.00 37.56  ? 254  LEU B CD2   1 
ATOM   5981 N N     . GLU B 1 255 ? -8.939  58.358  -19.434 1.00 35.21  ? 255  GLU B N     1 
ATOM   5982 C CA    . GLU B 1 255 ? -8.323  57.711  -20.619 1.00 37.71  ? 255  GLU B CA    1 
ATOM   5983 C C     . GLU B 1 255 ? -6.794  57.887  -20.608 1.00 39.50  ? 255  GLU B C     1 
ATOM   5984 O O     . GLU B 1 255 ? -6.092  56.855  -20.727 1.00 36.95  ? 255  GLU B O     1 
ATOM   5985 C CB    . GLU B 1 255 ? -8.952  58.234  -21.900 1.00 37.85  ? 255  GLU B CB    1 
ATOM   5986 C CG    . GLU B 1 255 ? -8.331  57.625  -23.137 1.00 40.08  ? 255  GLU B CG    1 
ATOM   5987 C CD    . GLU B 1 255 ? -9.096  57.936  -24.402 1.00 47.04  ? 255  GLU B CD    1 
ATOM   5988 O OE1   . GLU B 1 255 ? -10.094 58.692  -24.316 1.00 49.25  ? 255  GLU B OE1   1 
ATOM   5989 O OE2   . GLU B 1 255 ? -8.694  57.418  -25.453 1.00 52.02  ? 255  GLU B OE2   1 
ATOM   5990 N N     . GLN B 1 256 ? -6.290  59.123  -20.481 1.00 38.52  ? 256  GLN B N     1 
ATOM   5991 C CA    . GLN B 1 256 ? -4.836  59.422  -20.415 1.00 38.01  ? 256  GLN B CA    1 
ATOM   5992 C C     . GLN B 1 256 ? -4.202  58.799  -19.158 1.00 35.71  ? 256  GLN B C     1 
ATOM   5993 O O     . GLN B 1 256 ? -3.098  58.293  -19.260 1.00 37.46  ? 256  GLN B O     1 
ATOM   5994 C CB    . GLN B 1 256 ? -4.593  60.930  -20.408 1.00 43.92  ? 256  GLN B CB    1 
ATOM   5995 C CG    . GLN B 1 256 ? -4.439  61.533  -21.794 1.00 49.00  ? 256  GLN B CG    1 
ATOM   5996 C CD    . GLN B 1 256 ? -3.816  62.898  -21.670 1.00 57.12  ? 256  GLN B CD    1 
ATOM   5997 O OE1   . GLN B 1 256 ? -2.605  63.050  -21.824 1.00 63.67  ? 256  GLN B OE1   1 
ATOM   5998 N NE2   . GLN B 1 256 ? -4.631  63.888  -21.327 1.00 60.73  ? 256  GLN B NE2   1 
ATOM   5999 N N     . ILE B 1 257 ? -4.855  58.898  -18.005 1.00 35.42  ? 257  ILE B N     1 
ATOM   6000 C CA    . ILE B 1 257 ? -4.364  58.355  -16.706 1.00 36.31  ? 257  ILE B CA    1 
ATOM   6001 C C     . ILE B 1 257 ? -4.043  56.866  -16.889 1.00 38.61  ? 257  ILE B C     1 
ATOM   6002 O O     . ILE B 1 257 ? -2.936  56.461  -16.543 1.00 36.21  ? 257  ILE B O     1 
ATOM   6003 C CB    . ILE B 1 257 ? -5.401  58.566  -15.590 1.00 35.02  ? 257  ILE B CB    1 
ATOM   6004 C CG1   . ILE B 1 257 ? -5.612  60.054  -15.282 1.00 34.68  ? 257  ILE B CG1   1 
ATOM   6005 C CG2   . ILE B 1 257 ? -5.023  57.786  -14.338 1.00 34.03  ? 257  ILE B CG2   1 
ATOM   6006 C CD1   . ILE B 1 257 ? -6.868  60.319  -14.476 1.00 33.37  ? 257  ILE B CD1   1 
ATOM   6007 N N     . VAL B 1 258 ? -4.980  56.092  -17.432 1.00 37.08  ? 258  VAL B N     1 
ATOM   6008 C CA    . VAL B 1 258 ? -4.811  54.621  -17.602 1.00 35.22  ? 258  VAL B CA    1 
ATOM   6009 C C     . VAL B 1 258 ? -3.705  54.334  -18.632 1.00 34.64  ? 258  VAL B C     1 
ATOM   6010 O O     . VAL B 1 258 ? -2.902  53.423  -18.375 1.00 31.78  ? 258  VAL B O     1 
ATOM   6011 C CB    . VAL B 1 258 ? -6.146  53.945  -17.951 1.00 33.73  ? 258  VAL B CB    1 
ATOM   6012 C CG1   . VAL B 1 258 ? -5.976  52.470  -18.326 1.00 32.19  ? 258  VAL B CG1   1 
ATOM   6013 C CG2   . VAL B 1 258 ? -7.122  54.109  -16.804 1.00 31.92  ? 258  VAL B CG2   1 
ATOM   6014 N N     . ASP B 1 259 ? -3.614  55.111  -19.709 1.00 32.22  ? 259  ASP B N     1 
ATOM   6015 C CA    . ASP B 1 259 ? -2.604  54.903  -20.777 1.00 35.06  ? 259  ASP B CA    1 
ATOM   6016 C C     . ASP B 1 259 ? -1.201  55.302  -20.286 1.00 38.14  ? 259  ASP B C     1 
ATOM   6017 O O     . ASP B 1 259 ? -0.208  54.774  -20.842 1.00 34.81  ? 259  ASP B O     1 
ATOM   6018 C CB    . ASP B 1 259 ? -3.011  55.617  -22.075 1.00 34.07  ? 259  ASP B CB    1 
ATOM   6019 C CG    . ASP B 1 259 ? -4.118  54.925  -22.840 1.00 33.01  ? 259  ASP B CG    1 
ATOM   6020 O OD1   . ASP B 1 259 ? -4.403  53.759  -22.520 1.00 39.14  ? 259  ASP B OD1   1 
ATOM   6021 O OD2   . ASP B 1 259 ? -4.729  55.568  -23.732 1.00 34.86  ? 259  ASP B OD2   1 
ATOM   6022 N N     . ILE B 1 260 ? -1.095  56.219  -19.317 1.00 38.69  ? 260  ILE B N     1 
ATOM   6023 C CA    . ILE B 1 260 ? 0.207   56.552  -18.669 1.00 39.65  ? 260  ILE B CA    1 
ATOM   6024 C C     . ILE B 1 260 ? 0.492   55.490  -17.604 1.00 39.00  ? 260  ILE B C     1 
ATOM   6025 O O     . ILE B 1 260 ? 1.659   55.132  -17.447 1.00 42.48  ? 260  ILE B O     1 
ATOM   6026 C CB    . ILE B 1 260 ? 0.207   57.976  -18.087 1.00 41.49  ? 260  ILE B CB    1 
ATOM   6027 C CG1   . ILE B 1 260 ? 0.221   59.031  -19.193 1.00 43.24  ? 260  ILE B CG1   1 
ATOM   6028 C CG2   . ILE B 1 260 ? 1.362   58.178  -17.121 1.00 41.42  ? 260  ILE B CG2   1 
ATOM   6029 C CD1   . ILE B 1 260 ? -0.275  60.376  -18.710 1.00 45.09  ? 260  ILE B CD1   1 
ATOM   6030 N N     . MET B 1 261 ? -0.543  55.006  -16.920 1.00 38.41  ? 261  MET B N     1 
ATOM   6031 C CA    . MET B 1 261 ? -0.432  54.070  -15.774 1.00 41.72  ? 261  MET B CA    1 
ATOM   6032 C C     . MET B 1 261 ? 0.201   52.750  -16.253 1.00 42.72  ? 261  MET B C     1 
ATOM   6033 O O     . MET B 1 261 ? 1.130   52.256  -15.600 1.00 34.62  ? 261  MET B O     1 
ATOM   6034 C CB    . MET B 1 261 ? -1.809  53.801  -15.166 1.00 45.50  ? 261  MET B CB    1 
ATOM   6035 C CG    . MET B 1 261 ? -1.774  53.348  -13.730 1.00 49.38  ? 261  MET B CG    1 
ATOM   6036 S SD    . MET B 1 261 ? -3.410  52.894  -13.041 1.00 59.04  ? 261  MET B SD    1 
ATOM   6037 C CE    . MET B 1 261 ? -4.422  54.283  -13.542 1.00 45.86  ? 261  MET B CE    1 
ATOM   6038 N N     . LEU B 1 262 ? -0.272  52.192  -17.365 1.00 39.49  ? 262  LEU B N     1 
ATOM   6039 C CA    . LEU B 1 262 ? 0.108   50.821  -17.769 1.00 36.23  ? 262  LEU B CA    1 
ATOM   6040 C C     . LEU B 1 262 ? 1.621   50.712  -17.946 1.00 32.81  ? 262  LEU B C     1 
ATOM   6041 O O     . LEU B 1 262 ? 2.209   49.845  -17.307 1.00 35.92  ? 262  LEU B O     1 
ATOM   6042 C CB    . LEU B 1 262 ? -0.618  50.379  -19.039 1.00 39.52  ? 262  LEU B CB    1 
ATOM   6043 C CG    . LEU B 1 262 ? -0.063  49.082  -19.624 1.00 42.27  ? 262  LEU B CG    1 
ATOM   6044 C CD1   . LEU B 1 262 ? -0.366  47.919  -18.681 1.00 44.81  ? 262  LEU B CD1   1 
ATOM   6045 C CD2   . LEU B 1 262 ? -0.605  48.834  -21.018 1.00 46.90  ? 262  LEU B CD2   1 
ATOM   6046 N N     . PRO B 1 263 ? 2.299   51.521  -18.802 1.00 37.04  ? 263  PRO B N     1 
ATOM   6047 C CA    . PRO B 1 263 ? 3.745   51.403  -18.986 1.00 35.92  ? 263  PRO B CA    1 
ATOM   6048 C C     . PRO B 1 263 ? 4.576   51.652  -17.724 1.00 34.69  ? 263  PRO B C     1 
ATOM   6049 O O     . PRO B 1 263 ? 5.732   51.308  -17.731 1.00 34.71  ? 263  PRO B O     1 
ATOM   6050 C CB    . PRO B 1 263 ? 4.160   52.477  -20.009 1.00 37.91  ? 263  PRO B CB    1 
ATOM   6051 C CG    . PRO B 1 263 ? 2.888   53.176  -20.438 1.00 36.81  ? 263  PRO B CG    1 
ATOM   6052 C CD    . PRO B 1 263 ? 1.735   52.587  -19.651 1.00 36.44  ? 263  PRO B CD    1 
ATOM   6053 N N     . LEU B 1 264 ? 4.003   52.290  -16.701 1.00 33.53  ? 264  LEU B N     1 
ATOM   6054 C CA    . LEU B 1 264 ? 4.764   52.587  -15.466 1.00 35.85  ? 264  LEU B CA    1 
ATOM   6055 C C     . LEU B 1 264 ? 4.537   51.463  -14.453 1.00 34.45  ? 264  LEU B C     1 
ATOM   6056 O O     . LEU B 1 264 ? 5.285   51.447  -13.460 1.00 33.10  ? 264  LEU B O     1 
ATOM   6057 C CB    . LEU B 1 264 ? 4.325   53.930  -14.876 1.00 37.75  ? 264  LEU B CB    1 
ATOM   6058 C CG    . LEU B 1 264 ? 4.517   55.167  -15.751 1.00 40.72  ? 264  LEU B CG    1 
ATOM   6059 C CD1   . LEU B 1 264 ? 4.100   56.415  -14.967 1.00 41.31  ? 264  LEU B CD1   1 
ATOM   6060 C CD2   . LEU B 1 264 ? 5.951   55.309  -16.239 1.00 42.11  ? 264  LEU B CD2   1 
ATOM   6061 N N     . ARG B 1 265 ? 3.541   50.593  -14.670 1.00 27.35  ? 265  ARG B N     1 
ATOM   6062 C CA    . ARG B 1 265 ? 3.183   49.523  -13.702 1.00 30.12  ? 265  ARG B CA    1 
ATOM   6063 C C     . ARG B 1 265 ? 3.647   48.152  -14.211 1.00 33.17  ? 265  ARG B C     1 
ATOM   6064 O O     . ARG B 1 265 ? 3.981   47.293  -13.374 1.00 35.21  ? 265  ARG B O     1 
ATOM   6065 C CB    . ARG B 1 265 ? 1.671   49.437  -13.474 1.00 30.68  ? 265  ARG B CB    1 
ATOM   6066 C CG    . ARG B 1 265 ? 1.282   48.333  -12.510 1.00 28.45  ? 265  ARG B CG    1 
ATOM   6067 C CD    . ARG B 1 265 ? 2.053   48.379  -11.210 1.00 31.02  ? 265  ARG B CD    1 
ATOM   6068 N NE    . ARG B 1 265 ? 1.643   47.249  -10.395 1.00 33.11  ? 265  ARG B NE    1 
ATOM   6069 C CZ    . ARG B 1 265 ? 2.389   46.635  -9.488  1.00 34.72  ? 265  ARG B CZ    1 
ATOM   6070 N NH1   . ARG B 1 265 ? 3.608   47.060  -9.190  1.00 33.23  ? 265  ARG B NH1   1 
ATOM   6071 N NH2   . ARG B 1 265 ? 1.887   45.591  -8.861  1.00 35.63  ? 265  ARG B NH2   1 
ATOM   6072 N N     . ILE B 1 266 ? 3.656   47.939  -15.524 1.00 28.93  ? 266  ILE B N     1 
ATOM   6073 C CA    . ILE B 1 266 ? 3.848   46.582  -16.095 1.00 29.83  ? 266  ILE B CA    1 
ATOM   6074 C C     . ILE B 1 266 ? 5.241   46.047  -15.704 1.00 29.65  ? 266  ILE B C     1 
ATOM   6075 O O     . ILE B 1 266 ? 5.358   44.838  -15.545 1.00 32.87  ? 266  ILE B O     1 
ATOM   6076 C CB    . ILE B 1 266 ? 3.581   46.617  -17.602 1.00 28.83  ? 266  ILE B CB    1 
ATOM   6077 C CG1   . ILE B 1 266 ? 3.236   45.221  -18.143 1.00 29.05  ? 266  ILE B CG1   1 
ATOM   6078 C CG2   . ILE B 1 266 ? 4.727   47.284  -18.335 1.00 32.21  ? 266  ILE B CG2   1 
ATOM   6079 C CD1   . ILE B 1 266 ? 2.938   45.186  -19.608 1.00 26.25  ? 266  ILE B CD1   1 
ATOM   6080 N N     . ASN B 1 267 ? 6.241   46.904  -15.483 1.00 31.92  ? 267  ASN B N     1 
ATOM   6081 C CA    . ASN B 1 267 ? 7.602   46.465  -15.068 1.00 34.05  ? 267  ASN B CA    1 
ATOM   6082 C C     . ASN B 1 267 ? 7.726   46.496  -13.539 1.00 34.78  ? 267  ASN B C     1 
ATOM   6083 O O     . ASN B 1 267 ? 8.776   46.133  -13.070 1.00 37.52  ? 267  ASN B O     1 
ATOM   6084 C CB    . ASN B 1 267 ? 8.693   47.267  -15.780 1.00 33.25  ? 267  ASN B CB    1 
ATOM   6085 C CG    . ASN B 1 267 ? 8.584   47.111  -17.277 1.00 35.58  ? 267  ASN B CG    1 
ATOM   6086 O OD1   . ASN B 1 267 ? 8.375   46.003  -17.761 1.00 41.07  ? 267  ASN B OD1   1 
ATOM   6087 N ND2   . ASN B 1 267 ? 8.709   48.195  -18.020 1.00 33.12  ? 267  ASN B ND2   1 
ATOM   6088 N N     . MET B 1 268 ? 6.666   46.837  -12.796 1.00 36.16  ? 268  MET B N     1 
ATOM   6089 C CA    . MET B 1 268 ? 6.642   46.909  -11.305 1.00 37.77  ? 268  MET B CA    1 
ATOM   6090 C C     . MET B 1 268 ? 7.516   48.071  -10.826 1.00 38.56  ? 268  MET B C     1 
ATOM   6091 O O     . MET B 1 268 ? 7.795   48.144  -9.619  1.00 33.73  ? 268  MET B O     1 
ATOM   6092 C CB    . MET B 1 268 ? 7.117   45.614  -10.643 1.00 41.93  ? 268  MET B CB    1 
ATOM   6093 C CG    . MET B 1 268 ? 6.315   44.415  -11.106 1.00 50.54  ? 268  MET B CG    1 
ATOM   6094 S SD    . MET B 1 268 ? 6.654   42.955  -10.134 1.00 55.47  ? 268  MET B SD    1 
ATOM   6095 C CE    . MET B 1 268 ? 8.347   42.623  -10.633 1.00 60.33  ? 268  MET B CE    1 
ATOM   6096 N N     . ALA B 1 269 ? 7.852   48.994  -11.722 1.00 33.49  ? 269  ALA B N     1 
ATOM   6097 C CA    . ALA B 1 269 ? 8.516   50.267  -11.382 1.00 39.48  ? 269  ALA B CA    1 
ATOM   6098 C C     . ALA B 1 269 ? 8.332   51.190  -12.578 1.00 36.21  ? 269  ALA B C     1 
ATOM   6099 O O     . ALA B 1 269 ? 8.265   50.727  -13.713 1.00 39.19  ? 269  ALA B O     1 
ATOM   6100 C CB    . ALA B 1 269 ? 9.976   50.037  -11.018 1.00 38.85  ? 269  ALA B CB    1 
ATOM   6101 N N     . PRO B 1 270 ? 8.182   52.511  -12.370 1.00 35.02  ? 270  PRO B N     1 
ATOM   6102 C CA    . PRO B 1 270 ? 8.270   53.101  -11.031 1.00 34.47  ? 270  PRO B CA    1 
ATOM   6103 C C     . PRO B 1 270 ? 7.055   52.878  -10.120 1.00 37.15  ? 270  PRO B C     1 
ATOM   6104 O O     . PRO B 1 270 ? 7.194   53.081  -8.947  1.00 37.83  ? 270  PRO B O     1 
ATOM   6105 C CB    . PRO B 1 270 ? 8.440   54.580  -11.379 1.00 36.34  ? 270  PRO B CB    1 
ATOM   6106 C CG    . PRO B 1 270 ? 7.601   54.728  -12.636 1.00 38.36  ? 270  PRO B CG    1 
ATOM   6107 C CD    . PRO B 1 270 ? 7.948   53.492  -13.438 1.00 35.41  ? 270  PRO B CD    1 
ATOM   6108 N N     . LEU B 1 271 ? 5.896   52.500  -10.675 1.00 36.99  ? 271  LEU B N     1 
ATOM   6109 C CA    . LEU B 1 271 ? 4.680   52.176  -9.892  1.00 37.56  ? 271  LEU B CA    1 
ATOM   6110 C C     . LEU B 1 271 ? 4.892   50.838  -9.182  1.00 37.30  ? 271  LEU B C     1 
ATOM   6111 O O     . LEU B 1 271 ? 4.431   49.810  -9.690  1.00 36.98  ? 271  LEU B O     1 
ATOM   6112 C CB    . LEU B 1 271 ? 3.468   52.163  -10.828 1.00 40.32  ? 271  LEU B CB    1 
ATOM   6113 C CG    . LEU B 1 271 ? 3.091   53.531  -11.391 1.00 42.67  ? 271  LEU B CG    1 
ATOM   6114 C CD1   . LEU B 1 271 ? 1.762   53.457  -12.144 1.00 46.75  ? 271  LEU B CD1   1 
ATOM   6115 C CD2   . LEU B 1 271 ? 3.014   54.568  -10.270 1.00 40.05  ? 271  LEU B CD2   1 
ATOM   6116 N N     . GLN B 1 272 ? 5.497   50.894  -7.997  1.00 36.57  ? 272  GLN B N     1 
ATOM   6117 C CA    . GLN B 1 272 ? 6.000   49.723  -7.233  1.00 38.39  ? 272  GLN B CA    1 
ATOM   6118 C C     . GLN B 1 272 ? 4.863   48.981  -6.535  1.00 34.31  ? 272  GLN B C     1 
ATOM   6119 O O     . GLN B 1 272 ? 4.964   47.759  -6.384  1.00 33.27  ? 272  GLN B O     1 
ATOM   6120 C CB    . GLN B 1 272 ? 7.052   50.164  -6.215  1.00 39.12  ? 272  GLN B CB    1 
ATOM   6121 C CG    . GLN B 1 272 ? 8.369   50.584  -6.842  1.00 41.28  ? 272  GLN B CG    1 
ATOM   6122 C CD    . GLN B 1 272 ? 9.253   51.131  -5.751  1.00 43.31  ? 272  GLN B CD    1 
ATOM   6123 O OE1   . GLN B 1 272 ? 8.916   52.105  -5.089  1.00 43.92  ? 272  GLN B OE1   1 
ATOM   6124 N NE2   . GLN B 1 272 ? 10.370  50.471  -5.517  1.00 45.20  ? 272  GLN B NE2   1 
ATOM   6125 N N     . ASN B 1 273 ? 3.835   49.674  -6.059  1.00 33.32  ? 273  ASN B N     1 
ATOM   6126 C CA    . ASN B 1 273 ? 2.711   48.993  -5.375  1.00 29.86  ? 273  ASN B CA    1 
ATOM   6127 C C     . ASN B 1 273 ? 1.560   48.843  -6.376  1.00 30.22  ? 273  ASN B C     1 
ATOM   6128 O O     . ASN B 1 273 ? 1.765   49.151  -7.564  1.00 28.49  ? 273  ASN B O     1 
ATOM   6129 C CB    . ASN B 1 273 ? 2.378   49.717  -4.070  1.00 31.61  ? 273  ASN B CB    1 
ATOM   6130 C CG    . ASN B 1 273 ? 1.371   50.826  -4.261  1.00 27.97  ? 273  ASN B CG    1 
ATOM   6131 O OD1   . ASN B 1 273 ? 1.592   51.720  -5.080  1.00 32.51  ? 273  ASN B OD1   1 
ATOM   6132 N ND2   . ASN B 1 273 ? 0.285   50.775  -3.514  1.00 24.13  ? 273  ASN B ND2   1 
ATOM   6133 N N     . VAL B 1 274 ? 0.393   48.381  -5.923  1.00 31.77  ? 274  VAL B N     1 
ATOM   6134 C CA    . VAL B 1 274 ? -0.832  48.292  -6.775  1.00 33.99  ? 274  VAL B CA    1 
ATOM   6135 C C     . VAL B 1 274 ? -1.413  49.692  -6.917  1.00 34.94  ? 274  VAL B C     1 
ATOM   6136 O O     . VAL B 1 274 ? -1.932  50.212  -5.937  1.00 31.92  ? 274  VAL B O     1 
ATOM   6137 C CB    . VAL B 1 274 ? -1.875  47.329  -6.185  1.00 34.96  ? 274  VAL B CB    1 
ATOM   6138 C CG1   . VAL B 1 274 ? -3.139  47.279  -7.036  1.00 34.46  ? 274  VAL B CG1   1 
ATOM   6139 C CG2   . VAL B 1 274 ? -1.296  45.933  -5.993  1.00 34.98  ? 274  VAL B CG2   1 
ATOM   6140 N N     . PRO B 1 275 ? -1.353  50.337  -8.110  1.00 32.40  ? 275  PRO B N     1 
ATOM   6141 C CA    . PRO B 1 275 ? -1.868  51.694  -8.262  1.00 32.93  ? 275  PRO B CA    1 
ATOM   6142 C C     . PRO B 1 275 ? -3.401  51.660  -8.256  1.00 35.43  ? 275  PRO B C     1 
ATOM   6143 O O     . PRO B 1 275 ? -3.960  50.754  -8.858  1.00 38.26  ? 275  PRO B O     1 
ATOM   6144 C CB    . PRO B 1 275 ? -1.289  52.132  -9.616  1.00 34.53  ? 275  PRO B CB    1 
ATOM   6145 C CG    . PRO B 1 275 ? -1.179  50.845  -10.411 1.00 33.90  ? 275  PRO B CG    1 
ATOM   6146 C CD    . PRO B 1 275 ? -0.853  49.786  -9.379  1.00 35.21  ? 275  PRO B CD    1 
ATOM   6147 N N     . VAL B 1 276 ? -4.022  52.610  -7.565  1.00 36.33  ? 276  VAL B N     1 
ATOM   6148 C CA    . VAL B 1 276 ? -5.473  52.734  -7.534  1.00 34.39  ? 276  VAL B CA    1 
ATOM   6149 C C     . VAL B 1 276 ? -5.929  54.106  -8.024  1.00 36.10  ? 276  VAL B C     1 
ATOM   6150 O O     . VAL B 1 276 ? -5.238  55.086  -7.852  1.00 40.53  ? 276  VAL B O     1 
ATOM   6151 C CB    . VAL B 1 276 ? -6.063  52.455  -6.139  1.00 35.21  ? 276  VAL B CB    1 
ATOM   6152 C CG1   . VAL B 1 276 ? -5.694  51.069  -5.660  1.00 36.52  ? 276  VAL B CG1   1 
ATOM   6153 C CG2   . VAL B 1 276 ? -5.675  53.500  -5.114  1.00 32.59  ? 276  VAL B CG2   1 
ATOM   6154 N N     . LEU B 1 277 ? -7.073  54.163  -8.677  1.00 36.10  ? 277  LEU B N     1 
ATOM   6155 C CA    . LEU B 1 277 ? -7.620  55.415  -9.147  1.00 37.73  ? 277  LEU B CA    1 
ATOM   6156 C C     . LEU B 1 277 ? -9.040  55.505  -8.692  1.00 37.62  ? 277  LEU B C     1 
ATOM   6157 O O     . LEU B 1 277 ? -9.926  54.927  -9.291  1.00 32.83  ? 277  LEU B O     1 
ATOM   6158 C CB    . LEU B 1 277 ? -7.529  55.563  -10.648 1.00 39.80  ? 277  LEU B CB    1 
ATOM   6159 C CG    . LEU B 1 277 ? -7.939  56.918  -11.194 1.00 40.52  ? 277  LEU B CG    1 
ATOM   6160 C CD1   . LEU B 1 277 ? -6.828  57.925  -11.015 1.00 50.14  ? 277  LEU B CD1   1 
ATOM   6161 C CD2   . LEU B 1 277 ? -8.270  56.750  -12.656 1.00 42.02  ? 277  LEU B CD2   1 
ATOM   6162 N N     . ARG B 1 278 ? -9.243  56.246  -7.626  1.00 35.18  ? 278  ARG B N     1 
ATOM   6163 C CA    . ARG B 1 278 ? -10.548 56.391  -7.066  1.00 35.65  ? 278  ARG B CA    1 
ATOM   6164 C C     . ARG B 1 278 ? -11.296 57.637  -7.530  1.00 33.54  ? 278  ARG B C     1 
ATOM   6165 O O     . ARG B 1 278 ? -10.737 58.698  -7.606  1.00 34.41  ? 278  ARG B O     1 
ATOM   6166 C CB    . ARG B 1 278 ? -10.419 56.389  -5.543  1.00 36.96  ? 278  ARG B CB    1 
ATOM   6167 C CG    . ARG B 1 278 ? -9.654  55.205  -4.991  1.00 38.42  ? 278  ARG B CG    1 
ATOM   6168 C CD    . ARG B 1 278 ? -9.195  55.386  -3.555  1.00 36.50  ? 278  ARG B CD    1 
ATOM   6169 N NE    . ARG B 1 278 ? -10.270 55.738  -2.641  1.00 35.84  ? 278  ARG B NE    1 
ATOM   6170 C CZ    . ARG B 1 278 ? -10.792 54.919  -1.737  1.00 39.57  ? 278  ARG B CZ    1 
ATOM   6171 N NH1   . ARG B 1 278 ? -10.355 53.679  -1.625  1.00 38.22  ? 278  ARG B NH1   1 
ATOM   6172 N NH2   . ARG B 1 278 ? -11.759 55.341  -0.943  1.00 40.46  ? 278  ARG B NH2   1 
ATOM   6173 N N     . ASN B 1 279 ? -12.573 57.491  -7.815  1.00 34.93  ? 279  ASN B N     1 
ATOM   6174 C CA    . ASN B 1 279 ? -13.429 58.624  -8.233  1.00 32.48  ? 279  ASN B CA    1 
ATOM   6175 C C     . ASN B 1 279 ? -13.826 59.435  -6.992  1.00 30.99  ? 279  ASN B C     1 
ATOM   6176 O O     . ASN B 1 279 ? -13.624 58.969  -5.849  1.00 30.18  ? 279  ASN B O     1 
ATOM   6177 C CB    . ASN B 1 279 ? -14.611 58.127  -9.064  1.00 32.59  ? 279  ASN B CB    1 
ATOM   6178 C CG    . ASN B 1 279 ? -15.866 57.875  -8.265  1.00 36.30  ? 279  ASN B CG    1 
ATOM   6179 O OD1   . ASN B 1 279 ? -15.841 57.257  -7.190  1.00 33.12  ? 279  ASN B OD1   1 
ATOM   6180 N ND2   . ASN B 1 279 ? -16.969 58.361  -8.809  1.00 33.70  ? 279  ASN B ND2   1 
ATOM   6181 N N     . ILE B 1 280 ? -14.379 60.624  -7.222  1.00 33.15  ? 280  ILE B N     1 
ATOM   6182 C CA    . ILE B 1 280 ? -14.721 61.606  -6.156  1.00 32.39  ? 280  ILE B CA    1 
ATOM   6183 C C     . ILE B 1 280 ? -15.619 60.950  -5.098  1.00 32.10  ? 280  ILE B C     1 
ATOM   6184 O O     . ILE B 1 280 ? -15.380 61.152  -3.878  1.00 34.86  ? 280  ILE B O     1 
ATOM   6185 C CB    . ILE B 1 280 ? -15.348 62.867  -6.796  1.00 35.26  ? 280  ILE B CB    1 
ATOM   6186 C CG1   . ILE B 1 280 ? -15.653 63.916  -5.730  1.00 33.59  ? 280  ILE B CG1   1 
ATOM   6187 C CG2   . ILE B 1 280 ? -16.576 62.537  -7.644  1.00 34.22  ? 280  ILE B CG2   1 
ATOM   6188 C CD1   . ILE B 1 280 ? -14.451 64.276  -4.916  1.00 35.49  ? 280  ILE B CD1   1 
ATOM   6189 N N     . ILE B 1 281 ? -16.623 60.196  -5.522  1.00 35.50  ? 281  ILE B N     1 
ATOM   6190 C CA    . ILE B 1 281 ? -17.651 59.643  -4.600  1.00 38.46  ? 281  ILE B CA    1 
ATOM   6191 C C     . ILE B 1 281 ? -16.960 58.670  -3.645  1.00 48.08  ? 281  ILE B C     1 
ATOM   6192 O O     . ILE B 1 281 ? -17.237 58.729  -2.417  1.00 48.45  ? 281  ILE B O     1 
ATOM   6193 C CB    . ILE B 1 281 ? -18.817 58.999  -5.362  1.00 37.23  ? 281  ILE B CB    1 
ATOM   6194 C CG1   . ILE B 1 281 ? -19.502 60.007  -6.287  1.00 40.49  ? 281  ILE B CG1   1 
ATOM   6195 C CG2   . ILE B 1 281 ? -19.805 58.385  -4.386  1.00 36.98  ? 281  ILE B CG2   1 
ATOM   6196 C CD1   . ILE B 1 281 ? -19.783 61.347  -5.633  1.00 39.06  ? 281  ILE B CD1   1 
ATOM   6197 N N     . LEU B 1 282 ? -16.046 57.858  -4.177  1.00 44.29  ? 282  LEU B N     1 
ATOM   6198 C CA    . LEU B 1 282 ? -15.349 56.826  -3.384  1.00 41.83  ? 282  LEU B CA    1 
ATOM   6199 C C     . LEU B 1 282 ? -14.566 57.504  -2.263  1.00 41.53  ? 282  LEU B C     1 
ATOM   6200 O O     . LEU B 1 282 ? -14.590 56.955  -1.161  1.00 42.10  ? 282  LEU B O     1 
ATOM   6201 C CB    . LEU B 1 282 ? -14.433 55.989  -4.283  1.00 43.22  ? 282  LEU B CB    1 
ATOM   6202 C CG    . LEU B 1 282 ? -14.115 54.592  -3.761  1.00 44.00  ? 282  LEU B CG    1 
ATOM   6203 C CD1   . LEU B 1 282 ? -15.379 53.884  -3.296  1.00 45.35  ? 282  LEU B CD1   1 
ATOM   6204 C CD2   . LEU B 1 282 ? -13.420 53.775  -4.835  1.00 46.58  ? 282  LEU B CD2   1 
ATOM   6205 N N     . ASP B 1 283 ? -13.904 58.646  -2.476  1.00 40.03  ? 283  ASP B N     1 
ATOM   6206 C CA    . ASP B 1 283 ? -13.099 59.192  -1.344  1.00 51.14  ? 283  ASP B CA    1 
ATOM   6207 C C     . ASP B 1 283 ? -13.747 60.432  -0.705  1.00 43.89  ? 283  ASP B C     1 
ATOM   6208 O O     . ASP B 1 283 ? -13.242 60.842  0.352   1.00 48.50  ? 283  ASP B O     1 
ATOM   6209 C CB    . ASP B 1 283 ? -11.598 59.251  -1.658  1.00 59.50  ? 283  ASP B CB    1 
ATOM   6210 C CG    . ASP B 1 283 ? -11.197 59.922  -2.939  1.00 64.42  ? 283  ASP B CG    1 
ATOM   6211 O OD1   . ASP B 1 283 ? -12.050 60.657  -3.498  1.00 74.27  ? 283  ASP B OD1   1 
ATOM   6212 O OD2   . ASP B 1 283 ? -10.022 59.720  -3.336  1.00 51.42  ? 283  ASP B OD2   1 
ATOM   6213 N N     . ALA B 1 284 ? -14.867 60.934  -1.237  1.00 40.98  ? 284  ALA B N     1 
ATOM   6214 C CA    . ALA B 1 284 ? -15.803 61.827  -0.513  1.00 42.19  ? 284  ALA B CA    1 
ATOM   6215 C C     . ALA B 1 284 ? -16.572 61.005  0.524   1.00 40.28  ? 284  ALA B C     1 
ATOM   6216 O O     . ALA B 1 284 ? -16.734 61.485  1.663   1.00 41.45  ? 284  ALA B O     1 
ATOM   6217 C CB    . ALA B 1 284 ? -16.761 62.503  -1.462  1.00 41.37  ? 284  ALA B CB    1 
ATOM   6218 N N     . ALA B 1 285 ? -17.037 59.814  0.150   1.00 41.00  ? 285  ALA B N     1 
ATOM   6219 C CA    . ALA B 1 285 ? -17.938 58.973  0.980   1.00 44.26  ? 285  ALA B CA    1 
ATOM   6220 C C     . ALA B 1 285 ? -17.247 58.540  2.275   1.00 44.45  ? 285  ALA B C     1 
ATOM   6221 O O     . ALA B 1 285 ? -17.946 58.212  3.235   1.00 39.10  ? 285  ALA B O     1 
ATOM   6222 C CB    . ALA B 1 285 ? -18.426 57.779  0.205   1.00 44.54  ? 285  ALA B CB    1 
ATOM   6223 N N     . VAL B 1 286 ? -15.922 58.468  2.263   1.00 45.09  ? 286  VAL B N     1 
ATOM   6224 C CA    . VAL B 1 286 ? -15.085 58.483  3.494   1.00 53.55  ? 286  VAL B CA    1 
ATOM   6225 C C     . VAL B 1 286 ? -14.973 59.970  3.829   1.00 54.93  ? 286  VAL B C     1 
ATOM   6226 O O     . VAL B 1 286 ? -14.698 60.730  2.894   1.00 71.42  ? 286  VAL B O     1 
ATOM   6227 C CB    . VAL B 1 286 ? -13.709 57.832  3.240   1.00 55.01  ? 286  VAL B CB    1 
ATOM   6228 C CG1   . VAL B 1 286 ? -12.889 57.702  4.521   1.00 59.86  ? 286  VAL B CG1   1 
ATOM   6229 C CG2   . VAL B 1 286 ? -13.845 56.480  2.543   1.00 54.51  ? 286  VAL B CG2   1 
ATOM   6230 N N     . VAL B 1 287 ? -15.270 60.382  5.053   1.00 54.36  ? 287  VAL B N     1 
ATOM   6231 C CA    . VAL B 1 287 ? -15.165 61.807  5.513   1.00 55.49  ? 287  VAL B CA    1 
ATOM   6232 C C     . VAL B 1 287 ? -16.422 62.637  5.192   1.00 51.82  ? 287  VAL B C     1 
ATOM   6233 O O     . VAL B 1 287 ? -16.394 63.823  5.527   1.00 59.21  ? 287  VAL B O     1 
ATOM   6234 C CB    . VAL B 1 287 ? -13.903 62.527  4.989   1.00 58.21  ? 287  VAL B CB    1 
ATOM   6235 C CG1   . VAL B 1 287 ? -12.699 61.593  4.904   1.00 64.86  ? 287  VAL B CG1   1 
ATOM   6236 C CG2   . VAL B 1 287 ? -14.113 63.279  3.672   1.00 54.42  ? 287  VAL B CG2   1 
ATOM   6237 N N     . SER B 1 288 ? -17.480 62.090  4.583   1.00 50.60  ? 288  SER B N     1 
ATOM   6238 C CA    . SER B 1 288 ? -18.772 62.816  4.436   1.00 47.47  ? 288  SER B CA    1 
ATOM   6239 C C     . SER B 1 288 ? -19.947 61.885  4.110   1.00 48.93  ? 288  SER B C     1 
ATOM   6240 O O     . SER B 1 288 ? -19.760 60.657  3.844   1.00 41.08  ? 288  SER B O     1 
ATOM   6241 C CB    . SER B 1 288 ? -18.676 63.960  3.439   1.00 46.20  ? 288  SER B CB    1 
ATOM   6242 O OG    . SER B 1 288 ? -18.459 63.498  2.116   1.00 45.17  ? 288  SER B OG    1 
ATOM   6243 N N     . GLN B 1 289 ? -21.147 62.459  4.209   1.00 50.92  ? 289  GLN B N     1 
ATOM   6244 C CA    . GLN B 1 289 ? -22.440 61.797  3.909   1.00 48.60  ? 289  GLN B CA    1 
ATOM   6245 C C     . GLN B 1 289 ? -23.016 62.471  2.662   1.00 45.16  ? 289  GLN B C     1 
ATOM   6246 O O     . GLN B 1 289 ? -22.702 63.662  2.436   1.00 38.17  ? 289  GLN B O     1 
ATOM   6247 C CB    . GLN B 1 289 ? -23.382 61.908  5.107   1.00 52.62  ? 289  GLN B CB    1 
ATOM   6248 C CG    . GLN B 1 289 ? -22.908 61.160  6.347   1.00 57.11  ? 289  GLN B CG    1 
ATOM   6249 C CD    . GLN B 1 289 ? -22.566 62.052  7.517   1.00 66.12  ? 289  GLN B CD    1 
ATOM   6250 O OE1   . GLN B 1 289 ? -22.520 63.283  7.421   1.00 70.98  ? 289  GLN B OE1   1 
ATOM   6251 N NE2   . GLN B 1 289 ? -22.351 61.423  8.659   1.00 69.11  ? 289  GLN B NE2   1 
ATOM   6252 N N     . ARG B 1 290 ? -23.788 61.728  1.867   1.00 41.17  ? 290  ARG B N     1 
ATOM   6253 C CA    . ARG B 1 290 ? -24.410 62.244  0.620   1.00 42.29  ? 290  ARG B CA    1 
ATOM   6254 C C     . ARG B 1 290 ? -25.216 63.515  0.944   1.00 46.88  ? 290  ARG B C     1 
ATOM   6255 O O     . ARG B 1 290 ? -25.141 64.489  0.176   1.00 40.53  ? 290  ARG B O     1 
ATOM   6256 C CB    . ARG B 1 290 ? -25.322 61.172  0.031   1.00 41.64  ? 290  ARG B CB    1 
ATOM   6257 C CG    . ARG B 1 290 ? -25.683 61.393  -1.429  1.00 40.00  ? 290  ARG B CG    1 
ATOM   6258 C CD    . ARG B 1 290 ? -26.634 60.301  -1.826  1.00 40.23  ? 290  ARG B CD    1 
ATOM   6259 N NE    . ARG B 1 290 ? -26.867 60.268  -3.258  1.00 39.94  ? 290  ARG B NE    1 
ATOM   6260 C CZ    . ARG B 1 290 ? -27.856 60.881  -3.883  1.00 39.65  ? 290  ARG B CZ    1 
ATOM   6261 N NH1   . ARG B 1 290 ? -28.719 61.600  -3.190  1.00 38.22  ? 290  ARG B NH1   1 
ATOM   6262 N NH2   . ARG B 1 290 ? -27.989 60.753  -5.193  1.00 40.03  ? 290  ARG B NH2   1 
ATOM   6263 N N     . ALA B 1 291 ? -25.926 63.499  2.078   1.00 52.99  ? 291  ALA B N     1 
ATOM   6264 C CA    . ALA B 1 291 ? -26.733 64.622  2.621   1.00 56.48  ? 291  ALA B CA    1 
ATOM   6265 C C     . ALA B 1 291 ? -25.923 65.930  2.627   1.00 55.18  ? 291  ALA B C     1 
ATOM   6266 O O     . ALA B 1 291 ? -26.534 66.973  2.369   1.00 57.27  ? 291  ALA B O     1 
ATOM   6267 C CB    . ALA B 1 291 ? -27.207 64.277  4.011   1.00 55.36  ? 291  ALA B CB    1 
ATOM   6268 N N     . ASP B 1 292 ? -24.622 65.884  2.855   1.00 46.73  ? 292  ASP B N     1 
ATOM   6269 C CA    . ASP B 1 292 ? -23.814 67.084  2.924   1.00 46.64  ? 292  ASP B CA    1 
ATOM   6270 C C     . ASP B 1 292 ? -23.667 67.780  1.597   1.00 44.33  ? 292  ASP B C     1 
ATOM   6271 O O     . ASP B 1 292 ? -23.214 68.907  1.545   1.00 50.57  ? 292  ASP B O     1 
ATOM   6272 C CB    . ASP B 1 292 ? -22.433 66.762  3.472   1.00 48.92  ? 292  ASP B CB    1 
ATOM   6273 C CG    . ASP B 1 292 ? -22.475 66.053  4.800   1.00 55.46  ? 292  ASP B CG    1 
ATOM   6274 O OD1   . ASP B 1 292 ? -23.487 66.150  5.516   1.00 55.02  ? 292  ASP B OD1   1 
ATOM   6275 O OD2   . ASP B 1 292 ? -21.473 65.398  5.133   1.00 61.21  ? 292  ASP B OD2   1 
ATOM   6276 N N     . TRP B 1 293 ? -24.046 67.122  0.521   1.00 46.71  ? 293  TRP B N     1 
ATOM   6277 C CA    . TRP B 1 293 ? -23.844 67.692  -0.798  1.00 48.47  ? 293  TRP B CA    1 
ATOM   6278 C C     . TRP B 1 293 ? -25.092 67.810  -1.656  1.00 46.66  ? 293  TRP B C     1 
ATOM   6279 O O     . TRP B 1 293 ? -25.120 68.605  -2.576  1.00 45.81  ? 293  TRP B O     1 
ATOM   6280 C CB    . TRP B 1 293 ? -22.794 66.877  -1.559  1.00 48.14  ? 293  TRP B CB    1 
ATOM   6281 C CG    . TRP B 1 293 ? -21.658 66.391  -0.742  1.00 46.16  ? 293  TRP B CG    1 
ATOM   6282 C CD1   . TRP B 1 293 ? -21.493 65.143  -0.226  1.00 41.46  ? 293  TRP B CD1   1 
ATOM   6283 C CD2   . TRP B 1 293 ? -20.512 67.142  -0.350  1.00 42.76  ? 293  TRP B CD2   1 
ATOM   6284 N NE1   . TRP B 1 293 ? -20.320 65.073  0.467   1.00 38.89  ? 293  TRP B NE1   1 
ATOM   6285 C CE2   . TRP B 1 293 ? -19.696 66.288  0.405   1.00 40.27  ? 293  TRP B CE2   1 
ATOM   6286 C CE3   . TRP B 1 293 ? -20.094 68.455  -0.568  1.00 45.38  ? 293  TRP B CE3   1 
ATOM   6287 C CZ2   . TRP B 1 293 ? -18.492 66.705  0.945   1.00 43.31  ? 293  TRP B CZ2   1 
ATOM   6288 C CZ3   . TRP B 1 293 ? -18.904 68.862  -0.030  1.00 45.58  ? 293  TRP B CZ3   1 
ATOM   6289 C CH2   . TRP B 1 293 ? -18.115 67.993  0.717   1.00 43.88  ? 293  TRP B CH2   1 
ATOM   6290 N N     . TYR B 1 294 ? -26.115 67.030  -1.359  1.00 60.40  ? 294  TYR B N     1 
ATOM   6291 C CA    . TYR B 1 294 ? -27.327 67.015  -2.162  1.00 66.16  ? 294  TYR B CA    1 
ATOM   6292 C C     . TYR B 1 294 ? -28.404 66.391  -1.338  1.00 72.25  ? 294  TYR B C     1 
ATOM   6293 O O     . TYR B 1 294 ? -28.216 65.328  -0.774  1.00 75.23  ? 294  TYR B O     1 
ATOM   6294 C CB    . TYR B 1 294 ? -27.116 66.175  -3.422  1.00 75.68  ? 294  TYR B CB    1 
ATOM   6295 C CG    . TYR B 1 294 ? -28.194 66.277  -4.460  1.00 87.02  ? 294  TYR B CG    1 
ATOM   6296 C CD1   . TYR B 1 294 ? -28.805 65.139  -4.960  1.00 98.10  ? 294  TYR B CD1   1 
ATOM   6297 C CD2   . TYR B 1 294 ? -28.588 67.506  -4.958  1.00 101.42 ? 294  TYR B CD2   1 
ATOM   6298 C CE1   . TYR B 1 294 ? -29.788 65.222  -5.920  1.00 105.86 ? 294  TYR B CE1   1 
ATOM   6299 C CE2   . TYR B 1 294 ? -29.576 67.600  -5.914  1.00 115.39 ? 294  TYR B CE2   1 
ATOM   6300 C CZ    . TYR B 1 294 ? -30.171 66.455  -6.392  1.00 116.39 ? 294  TYR B CZ    1 
ATOM   6301 O OH    . TYR B 1 294 ? -31.150 66.548  -7.347  1.00 115.42 ? 294  TYR B OH    1 
ATOM   6302 N N     . ASP B 1 295 ? -29.551 67.044  -1.274  1.00 81.54  ? 295  ASP B N     1 
ATOM   6303 C CA    . ASP B 1 295 ? -30.675 66.495  -0.538  1.00 86.65  ? 295  ASP B CA    1 
ATOM   6304 C C     . ASP B 1 295 ? -31.768 66.216  -1.521  1.00 87.61  ? 295  ASP B C     1 
ATOM   6305 O O     . ASP B 1 295 ? -32.800 65.659  -1.168  1.00 94.67  ? 295  ASP B O     1 
ATOM   6306 C CB    . ASP B 1 295 ? -31.181 67.469  0.539   1.00 85.05  ? 295  ASP B CB    1 
ATOM   6307 C CG    . ASP B 1 295 ? -31.942 68.645  -0.037  1.00 84.17  ? 295  ASP B CG    1 
ATOM   6308 O OD1   . ASP B 1 295 ? -31.358 69.419  -0.821  1.00 80.51  ? 295  ASP B OD1   1 
ATOM   6309 O OD2   . ASP B 1 295 ? -33.130 68.798  0.307   1.00 88.56  ? 295  ASP B OD2   1 
ATOM   6310 N N     . GLY B 1 296 ? -31.538 66.590  -2.761  1.00 80.11  ? 296  GLY B N     1 
ATOM   6311 C CA    . GLY B 1 296 ? -32.544 66.421  -3.763  1.00 79.01  ? 296  GLY B CA    1 
ATOM   6312 C C     . GLY B 1 296 ? -32.838 65.046  -4.279  1.00 76.12  ? 296  GLY B C     1 
ATOM   6313 O O     . GLY B 1 296 ? -32.445 64.037  -3.710  1.00 78.81  ? 296  GLY B O     1 
ATOM   6314 N N     . ASP B 1 297 ? -33.541 65.004  -5.393  1.00 76.95  ? 297  ASP B N     1 
ATOM   6315 C CA    . ASP B 1 297 ? -33.949 63.727  -5.917  1.00 79.63  ? 297  ASP B CA    1 
ATOM   6316 C C     . ASP B 1 297 ? -33.110 63.293  -7.081  1.00 69.51  ? 297  ASP B C     1 
ATOM   6317 O O     . ASP B 1 297 ? -32.514 64.120  -7.752  1.00 68.92  ? 297  ASP B O     1 
ATOM   6318 C CB    . ASP B 1 297 ? -35.407 63.799  -6.361  1.00 84.23  ? 297  ASP B CB    1 
ATOM   6319 C CG    . ASP B 1 297 ? -36.348 64.116  -5.219  1.00 95.25  ? 297  ASP B CG    1 
ATOM   6320 O OD1   . ASP B 1 297 ? -36.025 63.768  -4.061  1.00 96.30  ? 297  ASP B OD1   1 
ATOM   6321 O OD2   . ASP B 1 297 ? -37.411 64.717  -5.478  1.00 104.54 ? 297  ASP B OD2   1 
ATOM   6322 N N     . GLY B 1 298 ? -33.068 61.989  -7.322  1.00 60.51  ? 298  GLY B N     1 
ATOM   6323 C CA    . GLY B 1 298 ? -32.348 61.470  -8.503  1.00 50.63  ? 298  GLY B CA    1 
ATOM   6324 C C     . GLY B 1 298 ? -30.831 61.461  -8.324  1.00 48.37  ? 298  GLY B C     1 
ATOM   6325 O O     . GLY B 1 298 ? -30.325 61.584  -7.213  1.00 42.36  ? 298  GLY B O     1 
ATOM   6326 N N     . PRO B 1 299 ? -30.059 61.341  -9.427  1.00 45.46  ? 299  PRO B N     1 
ATOM   6327 C CA    . PRO B 1 299 ? -28.601 61.264  -9.350  1.00 43.90  ? 299  PRO B CA    1 
ATOM   6328 C C     . PRO B 1 299 ? -27.973 62.532  -8.745  1.00 45.91  ? 299  PRO B C     1 
ATOM   6329 O O     . PRO B 1 299 ? -28.653 63.542  -8.664  1.00 45.00  ? 299  PRO B O     1 
ATOM   6330 C CB    . PRO B 1 299 ? -28.162 61.127  -10.820 1.00 44.01  ? 299  PRO B CB    1 
ATOM   6331 C CG    . PRO B 1 299 ? -29.395 60.664  -11.569 1.00 46.44  ? 299  PRO B CG    1 
ATOM   6332 C CD    . PRO B 1 299 ? -30.550 61.292  -10.815 1.00 48.10  ? 299  PRO B CD    1 
ATOM   6333 N N     . LEU B 1 300 ? -26.711 62.454  -8.320  1.00 37.90  ? 300  LEU B N     1 
ATOM   6334 C CA    . LEU B 1 300 ? -25.918 63.637  -7.903  1.00 40.49  ? 300  LEU B CA    1 
ATOM   6335 C C     . LEU B 1 300 ? -25.654 64.466  -9.159  1.00 44.62  ? 300  LEU B C     1 
ATOM   6336 O O     . LEU B 1 300 ? -24.995 63.998  -10.091 1.00 45.09  ? 300  LEU B O     1 
ATOM   6337 C CB    . LEU B 1 300 ? -24.606 63.202  -7.225  1.00 39.60  ? 300  LEU B CB    1 
ATOM   6338 C CG    . LEU B 1 300 ? -24.731 62.311  -5.984  1.00 40.44  ? 300  LEU B CG    1 
ATOM   6339 C CD1   . LEU B 1 300 ? -23.446 61.553  -5.731  1.00 40.25  ? 300  LEU B CD1   1 
ATOM   6340 C CD2   . LEU B 1 300 ? -25.104 63.115  -4.748  1.00 43.06  ? 300  LEU B CD2   1 
ATOM   6341 N N     . PRO B 1 301 ? -26.199 65.702  -9.268  1.00 51.37  ? 301  PRO B N     1 
ATOM   6342 C CA    . PRO B 1 301 ? -25.833 66.594  -10.367 1.00 46.89  ? 301  PRO B CA    1 
ATOM   6343 C C     . PRO B 1 301 ? -24.371 67.022  -10.355 1.00 44.06  ? 301  PRO B C     1 
ATOM   6344 O O     . PRO B 1 301 ? -23.699 66.952  -9.331  1.00 40.10  ? 301  PRO B O     1 
ATOM   6345 C CB    . PRO B 1 301 ? -26.700 67.845  -10.198 1.00 55.00  ? 301  PRO B CB    1 
ATOM   6346 C CG    . PRO B 1 301 ? -27.813 67.435  -9.241  1.00 60.91  ? 301  PRO B CG    1 
ATOM   6347 C CD    . PRO B 1 301 ? -27.319 66.223  -8.473  1.00 55.50  ? 301  PRO B CD    1 
ATOM   6348 N N     . PRO B 1 302 ? -23.852 67.466  -11.516 1.00 42.60  ? 302  PRO B N     1 
ATOM   6349 C CA    . PRO B 1 302 ? -22.453 67.863  -11.657 1.00 44.66  ? 302  PRO B CA    1 
ATOM   6350 C C     . PRO B 1 302 ? -21.959 68.910  -10.641 1.00 48.75  ? 302  PRO B C     1 
ATOM   6351 O O     . PRO B 1 302 ? -20.825 68.797  -10.218 1.00 46.98  ? 302  PRO B O     1 
ATOM   6352 C CB    . PRO B 1 302 ? -22.391 68.413  -13.091 1.00 45.18  ? 302  PRO B CB    1 
ATOM   6353 C CG    . PRO B 1 302 ? -23.503 67.683  -13.815 1.00 47.55  ? 302  PRO B CG    1 
ATOM   6354 C CD    . PRO B 1 302 ? -24.599 67.547  -12.786 1.00 45.40  ? 302  PRO B CD    1 
ATOM   6355 N N     . GLU B 1 303 ? -22.822 69.844  -10.225 1.00 48.28  ? 303  GLU B N     1 
ATOM   6356 C CA    . GLU B 1 303 ? -22.493 70.896  -9.228  1.00 46.42  ? 303  GLU B CA    1 
ATOM   6357 C C     . GLU B 1 303 ? -21.989 70.264  -7.934  1.00 48.10  ? 303  GLU B C     1 
ATOM   6358 O O     . GLU B 1 303 ? -20.988 70.781  -7.387  1.00 48.48  ? 303  GLU B O     1 
ATOM   6359 C CB    . GLU B 1 303 ? -23.692 71.740  -8.798  1.00 44.01  ? 303  GLU B CB    1 
ATOM   6360 C CG    . GLU B 1 303 ? -24.353 72.505  -9.903  1.00 44.52  ? 303  GLU B CG    1 
ATOM   6361 C CD    . GLU B 1 303 ? -25.595 71.789  -10.386 1.00 44.66  ? 303  GLU B CD    1 
ATOM   6362 O OE1   . GLU B 1 303 ? -25.424 70.800  -11.134 1.00 44.04  ? 303  GLU B OE1   1 
ATOM   6363 O OE2   . GLU B 1 303 ? -26.716 72.189  -9.972  1.00 40.24  ? 303  GLU B OE2   1 
ATOM   6364 N N     . ALA B 1 304 ? -22.641 69.218  -7.441  1.00 42.90  ? 304  ALA B N     1 
ATOM   6365 C CA    . ALA B 1 304 ? -22.136 68.623  -6.226  1.00 42.47  ? 304  ALA B CA    1 
ATOM   6366 C C     . ALA B 1 304 ? -20.876 67.866  -6.255  1.00 40.46  ? 304  ALA B C     1 
ATOM   6367 O O     . ALA B 1 304 ? -20.197 67.829  -5.274  1.00 44.49  ? 304  ALA B O     1 
ATOM   6368 C CB    . ALA B 1 304 ? -23.122 67.851  -5.499  1.00 41.87  ? 304  ALA B CB    1 
ATOM   6369 N N     . ILE B 1 305 ? -20.562 67.271  -7.375  1.00 38.55  ? 305  ILE B N     1 
ATOM   6370 C CA    . ILE B 1 305 ? -19.311 66.588  -7.525  1.00 40.71  ? 305  ILE B CA    1 
ATOM   6371 C C     . ILE B 1 305 ? -18.289 67.672  -7.401  1.00 36.04  ? 305  ILE B C     1 
ATOM   6372 O O     . ILE B 1 305 ? -17.304 67.521  -6.738  1.00 35.84  ? 305  ILE B O     1 
ATOM   6373 C CB    . ILE B 1 305 ? -19.239 65.956  -8.929  1.00 38.52  ? 305  ILE B CB    1 
ATOM   6374 C CG1   . ILE B 1 305 ? -20.232 64.797  -9.069  1.00 42.50  ? 305  ILE B CG1   1 
ATOM   6375 C CG2   . ILE B 1 305 ? -17.821 65.593  -9.335  1.00 37.89  ? 305  ILE B CG2   1 
ATOM   6376 C CD1   . ILE B 1 305 ? -20.601 64.076  -7.803  1.00 45.92  ? 305  ILE B CD1   1 
ATOM   6377 N N     . GLU B 1 306 ? -18.553 68.784  -8.059  1.00 36.32  ? 306  GLU B N     1 
ATOM   6378 C CA    . GLU B 1 306 ? -17.639 69.889  -7.991  1.00 41.60  ? 306  GLU B CA    1 
ATOM   6379 C C     . GLU B 1 306 ? -17.458 70.444  -6.574  1.00 40.08  ? 306  GLU B C     1 
ATOM   6380 O O     . GLU B 1 306 ? -16.364 70.741  -6.178  1.00 36.11  ? 306  GLU B O     1 
ATOM   6381 C CB    . GLU B 1 306 ? -18.018 70.964  -8.983  1.00 41.67  ? 306  GLU B CB    1 
ATOM   6382 C CG    . GLU B 1 306 ? -17.703 70.600  -10.417 1.00 44.22  ? 306  GLU B CG    1 
ATOM   6383 C CD    . GLU B 1 306 ? -16.222 70.406  -10.649 1.00 41.76  ? 306  GLU B CD    1 
ATOM   6384 O OE1   . GLU B 1 306 ? -15.419 71.041  -9.958  1.00 39.15  ? 306  GLU B OE1   1 
ATOM   6385 O OE2   . GLU B 1 306 ? -15.854 69.620  -11.528 1.00 40.03  ? 306  GLU B OE2   1 
ATOM   6386 N N     . ARG B 1 307 ? -18.540 70.584  -5.826  1.00 45.39  ? 307  ARG B N     1 
ATOM   6387 C CA    . ARG B 1 307 ? -18.406 71.168  -4.463  1.00 53.53  ? 307  ARG B CA    1 
ATOM   6388 C C     . ARG B 1 307 ? -17.668 70.156  -3.584  1.00 50.45  ? 307  ARG B C     1 
ATOM   6389 O O     . ARG B 1 307 ? -16.842 70.596  -2.761  1.00 52.14  ? 307  ARG B O     1 
ATOM   6390 C CB    . ARG B 1 307 ? -19.716 71.692  -3.860  1.00 62.45  ? 307  ARG B CB    1 
ATOM   6391 C CG    . ARG B 1 307 ? -20.936 70.816  -4.068  1.00 78.84  ? 307  ARG B CG    1 
ATOM   6392 C CD    . ARG B 1 307 ? -22.154 71.605  -4.538  1.00 93.33  ? 307  ARG B CD    1 
ATOM   6393 N NE    . ARG B 1 307 ? -23.118 71.883  -3.480  1.00 96.69  ? 307  ARG B NE    1 
ATOM   6394 C CZ    . ARG B 1 307 ? -24.428 72.059  -3.661  1.00 102.48 ? 307  ARG B CZ    1 
ATOM   6395 N NH1   . ARG B 1 307 ? -24.968 71.969  -4.868  1.00 96.68  ? 307  ARG B NH1   1 
ATOM   6396 N NH2   . ARG B 1 307 ? -25.200 72.322  -2.620  1.00 109.77 ? 307  ARG B NH2   1 
ATOM   6397 N N     . MET B 1 308 ? -17.925 68.862  -3.787  1.00 48.26  ? 308  MET B N     1 
ATOM   6398 C CA    . MET B 1 308 ? -17.110 67.760  -3.212  1.00 44.31  ? 308  MET B CA    1 
ATOM   6399 C C     . MET B 1 308 ? -15.640 68.007  -3.570  1.00 40.95  ? 308  MET B C     1 
ATOM   6400 O O     . MET B 1 308 ? -14.816 68.134  -2.641  1.00 39.46  ? 308  MET B O     1 
ATOM   6401 C CB    . MET B 1 308 ? -17.547 66.401  -3.761  1.00 42.37  ? 308  MET B CB    1 
ATOM   6402 C CG    . MET B 1 308 ? -18.826 65.891  -3.175  1.00 41.47  ? 308  MET B CG    1 
ATOM   6403 S SD    . MET B 1 308 ? -19.245 64.254  -3.836  1.00 41.57  ? 308  MET B SD    1 
ATOM   6404 C CE    . MET B 1 308 ? -21.033 64.294  -3.789  1.00 41.72  ? 308  MET B CE    1 
ATOM   6405 N N     . LYS B 1 309 ? -15.327 68.092  -4.870  1.00 32.46  ? 309  LYS B N     1 
ATOM   6406 C CA    . LYS B 1 309 ? -13.951 68.343  -5.360  1.00 33.40  ? 309  LYS B CA    1 
ATOM   6407 C C     . LYS B 1 309 ? -13.340 69.513  -4.584  1.00 37.90  ? 309  LYS B C     1 
ATOM   6408 O O     . LYS B 1 309 ? -12.278 69.315  -3.961  1.00 37.77  ? 309  LYS B O     1 
ATOM   6409 C CB    . LYS B 1 309 ? -13.932 68.559  -6.875  1.00 32.90  ? 309  LYS B CB    1 
ATOM   6410 C CG    . LYS B 1 309 ? -14.002 67.275  -7.701  1.00 36.07  ? 309  LYS B CG    1 
ATOM   6411 C CD    . LYS B 1 309 ? -14.114 67.529  -9.180  1.00 34.32  ? 309  LYS B CD    1 
ATOM   6412 C CE    . LYS B 1 309 ? -13.030 68.436  -9.703  1.00 36.84  ? 309  LYS B CE    1 
ATOM   6413 N NZ    . LYS B 1 309 ? -13.163 68.647  -11.165 1.00 40.40  ? 309  LYS B NZ    1 
ATOM   6414 N N     . LYS B 1 310 ? -13.988 70.685  -4.607  1.00 36.62  ? 310  LYS B N     1 
ATOM   6415 C CA    . LYS B 1 310 ? -13.373 71.946  -4.105  1.00 35.49  ? 310  LYS B CA    1 
ATOM   6416 C C     . LYS B 1 310 ? -13.309 71.920  -2.574  1.00 36.09  ? 310  LYS B C     1 
ATOM   6417 O O     . LYS B 1 310 ? -12.261 72.311  -2.005  1.00 36.35  ? 310  LYS B O     1 
ATOM   6418 C CB    . LYS B 1 310 ? -14.134 73.176  -4.612  1.00 35.53  ? 310  LYS B CB    1 
ATOM   6419 C CG    . LYS B 1 310 ? -14.251 73.325  -6.125  1.00 36.56  ? 310  LYS B CG    1 
ATOM   6420 C CD    . LYS B 1 310 ? -13.202 72.647  -6.947  1.00 38.04  ? 310  LYS B CD    1 
ATOM   6421 C CE    . LYS B 1 310 ? -13.130 73.157  -8.367  1.00 39.77  ? 310  LYS B CE    1 
ATOM   6422 N NZ    . LYS B 1 310 ? -12.954 72.053  -9.338  1.00 40.66  ? 310  LYS B NZ    1 
ATOM   6423 N N     . GLU B 1 311 ? -14.366 71.456  -1.912  1.00 35.95  ? 311  GLU B N     1 
ATOM   6424 C CA    . GLU B 1 311 ? -14.435 71.554  -0.440  1.00 37.70  ? 311  GLU B CA    1 
ATOM   6425 C C     . GLU B 1 311 ? -13.329 70.642  0.115   1.00 45.94  ? 311  GLU B C     1 
ATOM   6426 O O     . GLU B 1 311 ? -12.676 71.042  1.099   1.00 41.83  ? 311  GLU B O     1 
ATOM   6427 C CB    . GLU B 1 311 ? -15.854 71.266  0.041   1.00 40.57  ? 311  GLU B CB    1 
ATOM   6428 C CG    . GLU B 1 311 ? -16.019 71.315  1.551   1.00 48.45  ? 311  GLU B CG    1 
ATOM   6429 C CD    . GLU B 1 311 ? -15.654 72.625  2.248   1.00 57.52  ? 311  GLU B CD    1 
ATOM   6430 O OE1   . GLU B 1 311 ? -15.472 73.689  1.563   1.00 55.80  ? 311  GLU B OE1   1 
ATOM   6431 O OE2   . GLU B 1 311 ? -15.558 72.589  3.492   1.00 66.95  ? 311  GLU B OE2   1 
ATOM   6432 N N     . LEU B 1 312 ? -13.090 69.484  -0.527  1.00 45.43  ? 312  LEU B N     1 
ATOM   6433 C CA    . LEU B 1 312 ? -12.166 68.434  -0.019  1.00 43.58  ? 312  LEU B CA    1 
ATOM   6434 C C     . LEU B 1 312 ? -10.823 68.474  -0.761  1.00 44.70  ? 312  LEU B C     1 
ATOM   6435 O O     . LEU B 1 312 ? -9.909  67.778  -0.315  1.00 47.96  ? 312  LEU B O     1 
ATOM   6436 C CB    . LEU B 1 312 ? -12.826 67.064  -0.170  1.00 42.49  ? 312  LEU B CB    1 
ATOM   6437 C CG    . LEU B 1 312 ? -14.204 66.918  0.461   1.00 43.29  ? 312  LEU B CG    1 
ATOM   6438 C CD1   . LEU B 1 312 ? -14.808 65.575  0.093   1.00 43.82  ? 312  LEU B CD1   1 
ATOM   6439 C CD2   . LEU B 1 312 ? -14.157 67.079  1.975   1.00 41.57  ? 312  LEU B CD2   1 
ATOM   6440 N N     . GLY B 1 313 ? -10.678 69.297  -1.798  1.00 41.45  ? 313  GLY B N     1 
ATOM   6441 C CA    . GLY B 1 313 ? -9.431  69.391  -2.584  1.00 40.07  ? 313  GLY B CA    1 
ATOM   6442 C C     . GLY B 1 313 ? -9.101  68.047  -3.216  1.00 42.66  ? 313  GLY B C     1 
ATOM   6443 O O     . GLY B 1 313 ? -7.958  67.590  -3.090  1.00 40.06  ? 313  GLY B O     1 
ATOM   6444 N N     . LEU B 1 314 ? -10.096 67.409  -3.830  1.00 38.55  ? 314  LEU B N     1 
ATOM   6445 C CA    . LEU B 1 314 ? -9.947  66.144  -4.595  1.00 36.80  ? 314  LEU B CA    1 
ATOM   6446 C C     . LEU B 1 314 ? -10.234 66.410  -6.076  1.00 36.66  ? 314  LEU B C     1 
ATOM   6447 O O     . LEU B 1 314 ? -10.865 67.447  -6.405  1.00 39.57  ? 314  LEU B O     1 
ATOM   6448 C CB    . LEU B 1 314 ? -10.911 65.121  -4.003  1.00 36.36  ? 314  LEU B CB    1 
ATOM   6449 C CG    . LEU B 1 314 ? -10.594 64.699  -2.570  1.00 39.90  ? 314  LEU B CG    1 
ATOM   6450 C CD1   . LEU B 1 314 ? -11.790 64.033  -1.916  1.00 38.09  ? 314  LEU B CD1   1 
ATOM   6451 C CD2   . LEU B 1 314 ? -9.378  63.779  -2.523  1.00 40.58  ? 314  LEU B CD2   1 
ATOM   6452 N N     . GLY B 1 315 ? -9.772  65.520  -6.951  1.00 35.56  ? 315  GLY B N     1 
ATOM   6453 C CA    . GLY B 1 315 ? -10.069 65.560  -8.394  1.00 33.15  ? 315  GLY B CA    1 
ATOM   6454 C C     . GLY B 1 315 ? -11.324 64.777  -8.678  1.00 31.31  ? 315  GLY B C     1 
ATOM   6455 O O     . GLY B 1 315 ? -11.887 64.206  -7.730  1.00 32.19  ? 315  GLY B O     1 
ATOM   6456 N N     . TYR B 1 316 ? -11.773 64.710  -9.926  1.00 29.79  ? 316  TYR B N     1 
ATOM   6457 C CA    . TYR B 1 316 ? -12.790 63.691  -10.265 1.00 32.32  ? 316  TYR B CA    1 
ATOM   6458 C C     . TYR B 1 316 ? -12.145 62.313  -10.035 1.00 31.90  ? 316  TYR B C     1 
ATOM   6459 O O     . TYR B 1 316 ? -12.769 61.432  -9.428  1.00 31.24  ? 316  TYR B O     1 
ATOM   6460 C CB    . TYR B 1 316 ? -13.357 63.800  -11.682 1.00 32.70  ? 316  TYR B CB    1 
ATOM   6461 C CG    . TYR B 1 316 ? -14.490 62.819  -11.793 1.00 33.64  ? 316  TYR B CG    1 
ATOM   6462 C CD1   . TYR B 1 316 ? -15.783 63.185  -11.460 1.00 36.43  ? 316  TYR B CD1   1 
ATOM   6463 C CD2   . TYR B 1 316 ? -14.240 61.480  -12.037 1.00 32.49  ? 316  TYR B CD2   1 
ATOM   6464 C CE1   . TYR B 1 316 ? -16.818 62.268  -11.460 1.00 33.67  ? 316  TYR B CE1   1 
ATOM   6465 C CE2   . TYR B 1 316 ? -15.259 60.546  -12.037 1.00 34.20  ? 316  TYR B CE2   1 
ATOM   6466 C CZ    . TYR B 1 316 ? -16.553 60.941  -11.748 1.00 34.98  ? 316  TYR B CZ    1 
ATOM   6467 O OH    . TYR B 1 316 ? -17.559 60.018  -11.757 1.00 32.60  ? 316  TYR B OH    1 
ATOM   6468 N N     . TRP B 1 317 ? -10.909 62.144  -10.510 1.00 32.56  ? 317  TRP B N     1 
ATOM   6469 C CA    . TRP B 1 317 ? -10.134 60.887  -10.358 1.00 32.52  ? 317  TRP B CA    1 
ATOM   6470 C C     . TRP B 1 317 ? -8.923  61.123  -9.441  1.00 33.03  ? 317  TRP B C     1 
ATOM   6471 O O     . TRP B 1 317 ? -8.149  62.061  -9.692  1.00 37.01  ? 317  TRP B O     1 
ATOM   6472 C CB    . TRP B 1 317 ? -9.717  60.386  -11.738 1.00 32.76  ? 317  TRP B CB    1 
ATOM   6473 C CG    . TRP B 1 317 ? -10.847 59.919  -12.595 1.00 31.69  ? 317  TRP B CG    1 
ATOM   6474 C CD1   . TRP B 1 317 ? -11.239 60.492  -13.764 1.00 33.15  ? 317  TRP B CD1   1 
ATOM   6475 C CD2   . TRP B 1 317 ? -11.667 58.750  -12.426 1.00 34.67  ? 317  TRP B CD2   1 
ATOM   6476 N NE1   . TRP B 1 317 ? -12.271 59.794  -14.314 1.00 32.44  ? 317  TRP B NE1   1 
ATOM   6477 C CE2   . TRP B 1 317 ? -12.564 58.727  -13.514 1.00 32.25  ? 317  TRP B CE2   1 
ATOM   6478 C CE3   . TRP B 1 317 ? -11.772 57.750  -11.452 1.00 32.13  ? 317  TRP B CE3   1 
ATOM   6479 C CZ2   . TRP B 1 317 ? -13.543 57.749  -13.654 1.00 31.07  ? 317  TRP B CZ2   1 
ATOM   6480 C CZ3   . TRP B 1 317 ? -12.746 56.790  -11.585 1.00 32.66  ? 317  TRP B CZ3   1 
ATOM   6481 C CH2   . TRP B 1 317 ? -13.606 56.783  -12.681 1.00 33.23  ? 317  TRP B CH2   1 
ATOM   6482 N N     . ASN B 1 318 ? -8.770  60.273  -8.425  1.00 31.34  ? 318  ASN B N     1 
ATOM   6483 C CA    . ASN B 1 318 ? -7.744  60.405  -7.370  1.00 33.99  ? 318  ASN B CA    1 
ATOM   6484 C C     . ASN B 1 318 ? -6.816  59.184  -7.397  1.00 33.50  ? 318  ASN B C     1 
ATOM   6485 O O     . ASN B 1 318 ? -7.230  58.092  -6.953  1.00 32.21  ? 318  ASN B O     1 
ATOM   6486 C CB    . ASN B 1 318 ? -8.461  60.672  -6.056  1.00 33.33  ? 318  ASN B CB    1 
ATOM   6487 C CG    . ASN B 1 318 ? -9.299  61.925  -6.181  1.00 36.17  ? 318  ASN B CG    1 
ATOM   6488 O OD1   . ASN B 1 318 ? -8.766  63.038  -6.144  1.00 36.13  ? 318  ASN B OD1   1 
ATOM   6489 N ND2   . ASN B 1 318 ? -10.588 61.738  -6.401  1.00 33.54  ? 318  ASN B ND2   1 
ATOM   6490 N N     . PHE B 1 319 ? -5.613  59.370  -7.929  1.00 37.29  ? 319  PHE B N     1 
ATOM   6491 C CA    . PHE B 1 319 ? -4.572  58.318  -7.998  1.00 38.98  ? 319  PHE B CA    1 
ATOM   6492 C C     . PHE B 1 319 ? -3.870  58.229  -6.645  1.00 39.96  ? 319  PHE B C     1 
ATOM   6493 O O     . PHE B 1 319 ? -3.471  59.289  -6.155  1.00 36.70  ? 319  PHE B O     1 
ATOM   6494 C CB    . PHE B 1 319 ? -3.575  58.629  -9.109  1.00 39.59  ? 319  PHE B CB    1 
ATOM   6495 C CG    . PHE B 1 319 ? -2.593  57.521  -9.401  1.00 38.91  ? 319  PHE B CG    1 
ATOM   6496 C CD1   . PHE B 1 319 ? -1.475  57.335  -8.608  1.00 42.11  ? 319  PHE B CD1   1 
ATOM   6497 C CD2   . PHE B 1 319 ? -2.770  56.678  -10.486 1.00 43.09  ? 319  PHE B CD2   1 
ATOM   6498 C CE1   . PHE B 1 319 ? -0.544  56.350  -8.909  1.00 41.49  ? 319  PHE B CE1   1 
ATOM   6499 C CE2   . PHE B 1 319 ? -1.848  55.680  -10.774 1.00 40.71  ? 319  PHE B CE2   1 
ATOM   6500 C CZ    . PHE B 1 319 ? -0.740  55.514  -9.977  1.00 39.76  ? 319  PHE B CZ    1 
ATOM   6501 N N     . TYR B 1 320 ? -3.728  57.019  -6.086  1.00 37.00  ? 320  TYR B N     1 
ATOM   6502 C CA    . TYR B 1 320 ? -2.887  56.752  -4.892  1.00 37.74  ? 320  TYR B CA    1 
ATOM   6503 C C     . TYR B 1 320 ? -1.859  55.667  -5.231  1.00 39.24  ? 320  TYR B C     1 
ATOM   6504 O O     . TYR B 1 320 ? -2.262  54.598  -5.770  1.00 36.38  ? 320  TYR B O     1 
ATOM   6505 C CB    . TYR B 1 320 ? -3.747  56.382  -3.677  1.00 35.05  ? 320  TYR B CB    1 
ATOM   6506 C CG    . TYR B 1 320 ? -4.757  57.439  -3.318  1.00 35.06  ? 320  TYR B CG    1 
ATOM   6507 C CD1   . TYR B 1 320 ? -5.956  57.536  -4.008  1.00 37.10  ? 320  TYR B CD1   1 
ATOM   6508 C CD2   . TYR B 1 320 ? -4.502  58.364  -2.317  1.00 36.64  ? 320  TYR B CD2   1 
ATOM   6509 C CE1   . TYR B 1 320 ? -6.885  58.522  -3.708  1.00 37.99  ? 320  TYR B CE1   1 
ATOM   6510 C CE2   . TYR B 1 320 ? -5.416  59.363  -2.010  1.00 40.32  ? 320  TYR B CE2   1 
ATOM   6511 C CZ    . TYR B 1 320 ? -6.612  59.442  -2.707  1.00 38.19  ? 320  TYR B CZ    1 
ATOM   6512 O OH    . TYR B 1 320 ? -7.496  60.430  -2.410  1.00 38.05  ? 320  TYR B OH    1 
ATOM   6513 N N     . GLY B 1 321 ? -0.582  55.960  -4.949  1.00 35.84  ? 321  GLY B N     1 
ATOM   6514 C CA    . GLY B 1 321 ? 0.523   54.988  -5.035  1.00 36.67  ? 321  GLY B CA    1 
ATOM   6515 C C     . GLY B 1 321 ? 1.475   55.106  -3.866  1.00 36.31  ? 321  GLY B C     1 
ATOM   6516 O O     . GLY B 1 321 ? 1.450   56.138  -3.138  1.00 32.96  ? 321  GLY B O     1 
ATOM   6517 N N     . THR B 1 322 ? 2.306   54.080  -3.682  1.00 37.70  ? 322  THR B N     1 
ATOM   6518 C CA    . THR B 1 322 ? 3.391   54.079  -2.675  1.00 36.89  ? 322  THR B CA    1 
ATOM   6519 C C     . THR B 1 322 ? 4.703   53.753  -3.383  1.00 39.48  ? 322  THR B C     1 
ATOM   6520 O O     . THR B 1 322 ? 4.678   52.977  -4.362  1.00 39.88  ? 322  THR B O     1 
ATOM   6521 C CB    . THR B 1 322 ? 3.023   53.164  -1.508  1.00 39.82  ? 322  THR B CB    1 
ATOM   6522 O OG1   . THR B 1 322 ? 1.860   53.756  -0.938  1.00 37.55  ? 322  THR B OG1   1 
ATOM   6523 C CG2   . THR B 1 322 ? 4.099   53.047  -0.451  1.00 39.83  ? 322  THR B CG2   1 
ATOM   6524 N N     . LEU B 1 323 ? 5.793   54.380  -2.935  1.00 37.73  ? 323  LEU B N     1 
ATOM   6525 C CA    . LEU B 1 323 ? 7.165   54.056  -3.382  1.00 35.14  ? 323  LEU B CA    1 
ATOM   6526 C C     . LEU B 1 323 ? 7.971   53.556  -2.192  1.00 37.11  ? 323  LEU B C     1 
ATOM   6527 O O     . LEU B 1 323 ? 7.729   54.023  -1.064  1.00 35.91  ? 323  LEU B O     1 
ATOM   6528 C CB    . LEU B 1 323 ? 7.802   55.296  -3.997  1.00 36.67  ? 323  LEU B CB    1 
ATOM   6529 C CG    . LEU B 1 323 ? 7.105   55.796  -5.245  1.00 35.40  ? 323  LEU B CG    1 
ATOM   6530 C CD1   . LEU B 1 323 ? 7.642   57.159  -5.631  1.00 37.75  ? 323  LEU B CD1   1 
ATOM   6531 C CD2   . LEU B 1 323 ? 7.256   54.788  -6.373  1.00 37.01  ? 323  LEU B CD2   1 
ATOM   6532 N N     . TYR B 1 324 ? 8.878   52.615  -2.451  1.00 40.15  ? 324  TYR B N     1 
ATOM   6533 C CA    . TYR B 1 324 ? 9.632   51.881  -1.410  1.00 40.23  ? 324  TYR B CA    1 
ATOM   6534 C C     . TYR B 1 324 ? 11.122  51.957  -1.727  1.00 41.35  ? 324  TYR B C     1 
ATOM   6535 O O     . TYR B 1 324 ? 11.464  52.056  -2.905  1.00 46.98  ? 324  TYR B O     1 
ATOM   6536 C CB    . TYR B 1 324 ? 9.154   50.433  -1.339  1.00 38.57  ? 324  TYR B CB    1 
ATOM   6537 C CG    . TYR B 1 324 ? 7.668   50.208  -1.239  1.00 35.69  ? 324  TYR B CG    1 
ATOM   6538 C CD1   . TYR B 1 324 ? 7.024   50.225  -0.017  1.00 35.25  ? 324  TYR B CD1   1 
ATOM   6539 C CD2   . TYR B 1 324 ? 6.916   49.851  -2.354  1.00 38.69  ? 324  TYR B CD2   1 
ATOM   6540 C CE1   . TYR B 1 324 ? 5.673   49.944  0.099   1.00 38.69  ? 324  TYR B CE1   1 
ATOM   6541 C CE2   . TYR B 1 324 ? 5.560   49.563  -2.259  1.00 36.09  ? 324  TYR B CE2   1 
ATOM   6542 C CZ    . TYR B 1 324 ? 4.932   49.617  -1.027  1.00 38.56  ? 324  TYR B CZ    1 
ATOM   6543 O OH    . TYR B 1 324 ? 3.599   49.341  -0.883  1.00 37.40  ? 324  TYR B OH    1 
ATOM   6544 N N     . GLY B 1 325 ? 11.967  51.925  -0.695  1.00 47.32  ? 325  GLY B N     1 
ATOM   6545 C CA    . GLY B 1 325 ? 13.427  51.810  -0.853  1.00 49.70  ? 325  GLY B CA    1 
ATOM   6546 C C     . GLY B 1 325 ? 14.178  52.930  -0.139  1.00 50.90  ? 325  GLY B C     1 
ATOM   6547 O O     . GLY B 1 325 ? 13.633  53.591  0.740   1.00 48.08  ? 325  GLY B O     1 
ATOM   6548 N N     . PRO B 1 326 ? 15.478  53.130  -0.444  1.00 50.87  ? 326  PRO B N     1 
ATOM   6549 C CA    . PRO B 1 326 ? 16.212  54.267  0.103   1.00 51.96  ? 326  PRO B CA    1 
ATOM   6550 C C     . PRO B 1 326 ? 15.598  55.545  -0.464  1.00 53.31  ? 326  PRO B C     1 
ATOM   6551 O O     . PRO B 1 326 ? 15.141  55.555  -1.611  1.00 52.10  ? 326  PRO B O     1 
ATOM   6552 C CB    . PRO B 1 326 ? 17.675  54.035  -0.314  1.00 51.87  ? 326  PRO B CB    1 
ATOM   6553 C CG    . PRO B 1 326 ? 17.619  53.021  -1.439  1.00 55.07  ? 326  PRO B CG    1 
ATOM   6554 C CD    . PRO B 1 326 ? 16.318  52.255  -1.276  1.00 51.39  ? 326  PRO B CD    1 
ATOM   6555 N N     . PRO B 1 327 ? 15.490  56.619  0.353   1.00 52.69  ? 327  PRO B N     1 
ATOM   6556 C CA    . PRO B 1 327 ? 15.068  57.948  -0.113  1.00 52.73  ? 327  PRO B CA    1 
ATOM   6557 C C     . PRO B 1 327 ? 15.500  58.427  -1.512  1.00 51.80  ? 327  PRO B C     1 
ATOM   6558 O O     . PRO B 1 327 ? 14.713  59.081  -2.190  1.00 51.72  ? 327  PRO B O     1 
ATOM   6559 C CB    . PRO B 1 327 ? 15.735  58.838  0.956   1.00 53.95  ? 327  PRO B CB    1 
ATOM   6560 C CG    . PRO B 1 327 ? 15.565  58.042  2.238   1.00 51.92  ? 327  PRO B CG    1 
ATOM   6561 C CD    . PRO B 1 327 ? 15.705  56.594  1.812   1.00 50.87  ? 327  PRO B CD    1 
ATOM   6562 N N     . GLN B 1 328 ? 16.734  58.146  -1.923  1.00 46.63  ? 328  GLN B N     1 
ATOM   6563 C CA    . GLN B 1 328 ? 17.224  58.567  -3.257  1.00 49.56  ? 328  GLN B CA    1 
ATOM   6564 C C     . GLN B 1 328 ? 16.443  57.801  -4.335  1.00 47.62  ? 328  GLN B C     1 
ATOM   6565 O O     . GLN B 1 328 ? 16.149  58.392  -5.399  1.00 44.11  ? 328  GLN B O     1 
ATOM   6566 C CB    . GLN B 1 328 ? 18.738  58.371  -3.358  1.00 53.50  ? 328  GLN B CB    1 
ATOM   6567 C CG    . GLN B 1 328 ? 19.359  59.055  -4.567  1.00 57.60  ? 328  GLN B CG    1 
ATOM   6568 C CD    . GLN B 1 328 ? 20.561  59.905  -4.225  1.00 68.31  ? 328  GLN B CD    1 
ATOM   6569 O OE1   . GLN B 1 328 ? 21.088  59.874  -3.113  1.00 74.34  ? 328  GLN B OE1   1 
ATOM   6570 N NE2   . GLN B 1 328 ? 21.003  60.698  -5.190  1.00 70.39  ? 328  GLN B NE2   1 
ATOM   6571 N N     . LEU B 1 329 ? 16.105  56.534  -4.091  1.00 45.15  ? 329  LEU B N     1 
ATOM   6572 C CA    . LEU B 1 329 ? 15.333  55.732  -5.081  1.00 48.87  ? 329  LEU B CA    1 
ATOM   6573 C C     . LEU B 1 329 ? 13.884  56.243  -5.103  1.00 45.33  ? 329  LEU B C     1 
ATOM   6574 O O     . LEU B 1 329 ? 13.343  56.419  -6.214  1.00 47.41  ? 329  LEU B O     1 
ATOM   6575 C CB    . LEU B 1 329 ? 15.403  54.236  -4.750  1.00 51.15  ? 329  LEU B CB    1 
ATOM   6576 C CG    . LEU B 1 329 ? 14.702  53.328  -5.767  1.00 55.92  ? 329  LEU B CG    1 
ATOM   6577 C CD1   . LEU B 1 329 ? 15.406  53.364  -7.125  1.00 54.78  ? 329  LEU B CD1   1 
ATOM   6578 C CD2   . LEU B 1 329 ? 14.587  51.896  -5.259  1.00 53.78  ? 329  LEU B CD2   1 
ATOM   6579 N N     . ILE B 1 330 ? 13.315  56.507  -3.922  1.00 39.49  ? 330  ILE B N     1 
ATOM   6580 C CA    . ILE B 1 330 ? 11.964  57.114  -3.740  1.00 43.87  ? 330  ILE B CA    1 
ATOM   6581 C C     . ILE B 1 330 ? 11.886  58.393  -4.584  1.00 45.24  ? 330  ILE B C     1 
ATOM   6582 O O     . ILE B 1 330 ? 10.981  58.468  -5.429  1.00 43.70  ? 330  ILE B O     1 
ATOM   6583 C CB    . ILE B 1 330 ? 11.647  57.327  -2.239  1.00 42.18  ? 330  ILE B CB    1 
ATOM   6584 C CG1   . ILE B 1 330 ? 11.338  55.985  -1.569  1.00 40.35  ? 330  ILE B CG1   1 
ATOM   6585 C CG2   . ILE B 1 330 ? 10.515  58.333  -2.045  1.00 41.02  ? 330  ILE B CG2   1 
ATOM   6586 C CD1   . ILE B 1 330 ? 11.149  56.043  -0.085  1.00 41.38  ? 330  ILE B CD1   1 
ATOM   6587 N N     . GLU B 1 331 ? 12.838  59.321  -4.420  1.00 48.32  ? 331  GLU B N     1 
ATOM   6588 C CA    . GLU B 1 331 ? 12.828  60.648  -5.095  1.00 52.09  ? 331  GLU B CA    1 
ATOM   6589 C C     . GLU B 1 331 ? 12.958  60.454  -6.599  1.00 49.71  ? 331  GLU B C     1 
ATOM   6590 O O     . GLU B 1 331 ? 12.273  61.191  -7.338  1.00 47.28  ? 331  GLU B O     1 
ATOM   6591 C CB    . GLU B 1 331 ? 13.955  61.568  -4.608  1.00 59.86  ? 331  GLU B CB    1 
ATOM   6592 C CG    . GLU B 1 331 ? 13.695  62.162  -3.228  1.00 70.19  ? 331  GLU B CG    1 
ATOM   6593 C CD    . GLU B 1 331 ? 13.761  63.682  -3.132  1.00 79.27  ? 331  GLU B CD    1 
ATOM   6594 O OE1   . GLU B 1 331 ? 14.486  64.308  -3.943  1.00 86.39  ? 331  GLU B OE1   1 
ATOM   6595 O OE2   . GLU B 1 331 ? 13.081  64.242  -2.244  1.00 78.65  ? 331  GLU B OE2   1 
ATOM   6596 N N     . MET B 1 332 ? 13.819  59.534  -7.040  1.00 44.82  ? 332  MET B N     1 
ATOM   6597 C CA    . MET B 1 332 ? 14.009  59.318  -8.490  1.00 50.44  ? 332  MET B CA    1 
ATOM   6598 C C     . MET B 1 332 ? 12.684  58.810  -9.074  1.00 46.70  ? 332  MET B C     1 
ATOM   6599 O O     . MET B 1 332 ? 12.247  59.372  -10.074 1.00 42.05  ? 332  MET B O     1 
ATOM   6600 C CB    . MET B 1 332 ? 15.123  58.319  -8.811  1.00 56.53  ? 332  MET B CB    1 
ATOM   6601 C CG    . MET B 1 332 ? 15.364  58.188  -10.322 1.00 62.52  ? 332  MET B CG    1 
ATOM   6602 S SD    . MET B 1 332 ? 16.209  56.660  -10.816 1.00 77.34  ? 332  MET B SD    1 
ATOM   6603 C CE    . MET B 1 332 ? 15.068  55.398  -10.247 1.00 67.82  ? 332  MET B CE    1 
ATOM   6604 N N     . ASN B 1 333 ? 12.081  57.803  -8.439  1.00 44.88  ? 333  ASN B N     1 
ATOM   6605 C CA    . ASN B 1 333 ? 10.809  57.165  -8.866  1.00 44.48  ? 333  ASN B CA    1 
ATOM   6606 C C     . ASN B 1 333 ? 9.666   58.194  -8.870  1.00 41.87  ? 333  ASN B C     1 
ATOM   6607 O O     . ASN B 1 333 ? 8.923   58.216  -9.870  1.00 38.49  ? 333  ASN B O     1 
ATOM   6608 C CB    . ASN B 1 333 ? 10.524  55.910  -8.036  1.00 47.62  ? 333  ASN B CB    1 
ATOM   6609 C CG    . ASN B 1 333 ? 11.299  54.697  -8.524  1.00 47.01  ? 333  ASN B CG    1 
ATOM   6610 O OD1   . ASN B 1 333 ? 11.718  54.654  -9.679  1.00 43.07  ? 333  ASN B OD1   1 
ATOM   6611 N ND2   . ASN B 1 333 ? 11.507  53.722  -7.651  1.00 42.51  ? 333  ASN B ND2   1 
ATOM   6612 N N     . TYR B 1 334 ? 9.550   59.019  -7.821  1.00 42.70  ? 334  TYR B N     1 
ATOM   6613 C CA    . TYR B 1 334 ? 8.579   60.141  -7.691  1.00 45.18  ? 334  TYR B CA    1 
ATOM   6614 C C     . TYR B 1 334 ? 8.760   61.165  -8.822  1.00 41.97  ? 334  TYR B C     1 
ATOM   6615 O O     . TYR B 1 334 ? 7.747   61.626  -9.383  1.00 38.08  ? 334  TYR B O     1 
ATOM   6616 C CB    . TYR B 1 334 ? 8.681   60.828  -6.324  1.00 46.36  ? 334  TYR B CB    1 
ATOM   6617 C CG    . TYR B 1 334 ? 7.478   61.671  -5.969  1.00 45.44  ? 334  TYR B CG    1 
ATOM   6618 C CD1   . TYR B 1 334 ? 6.195   61.146  -6.051  1.00 46.63  ? 334  TYR B CD1   1 
ATOM   6619 C CD2   . TYR B 1 334 ? 7.612   62.989  -5.550  1.00 47.70  ? 334  TYR B CD2   1 
ATOM   6620 C CE1   . TYR B 1 334 ? 5.077   61.903  -5.734  1.00 48.87  ? 334  TYR B CE1   1 
ATOM   6621 C CE2   . TYR B 1 334 ? 6.504   63.764  -5.224  1.00 50.21  ? 334  TYR B CE2   1 
ATOM   6622 C CZ    . TYR B 1 334 ? 5.230   63.216  -5.317  1.00 50.55  ? 334  TYR B CZ    1 
ATOM   6623 O OH    . TYR B 1 334 ? 4.121   63.952  -5.019  1.00 48.37  ? 334  TYR B OH    1 
ATOM   6624 N N     . GLY B 1 335 ? 10.001  61.477  -9.191  1.00 40.23  ? 335  GLY B N     1 
ATOM   6625 C CA    . GLY B 1 335 ? 10.310  62.356  -10.338 1.00 38.99  ? 335  GLY B CA    1 
ATOM   6626 C C     . GLY B 1 335 ? 9.769   61.830  -11.661 1.00 40.51  ? 335  GLY B C     1 
ATOM   6627 O O     . GLY B 1 335 ? 9.329   62.651  -12.491 1.00 40.01  ? 335  GLY B O     1 
ATOM   6628 N N     . ILE B 1 336 ? 9.865   60.519  -11.902 1.00 41.34  ? 336  ILE B N     1 
ATOM   6629 C CA    . ILE B 1 336 ? 9.396   59.849  -13.155 1.00 41.99  ? 336  ILE B CA    1 
ATOM   6630 C C     . ILE B 1 336 ? 7.863   59.927  -13.218 1.00 35.23  ? 336  ILE B C     1 
ATOM   6631 O O     . ILE B 1 336 ? 7.319   60.222  -14.280 1.00 36.19  ? 336  ILE B O     1 
ATOM   6632 C CB    . ILE B 1 336 ? 9.862   58.372  -13.193 1.00 45.92  ? 336  ILE B CB    1 
ATOM   6633 C CG1   . ILE B 1 336 ? 11.385  58.234  -13.126 1.00 50.63  ? 336  ILE B CG1   1 
ATOM   6634 C CG2   . ILE B 1 336 ? 9.288   57.651  -14.400 1.00 44.91  ? 336  ILE B CG2   1 
ATOM   6635 C CD1   . ILE B 1 336 ? 12.114  58.939  -14.239 1.00 51.88  ? 336  ILE B CD1   1 
ATOM   6636 N N     . ILE B 1 337 ? 7.211   59.613  -12.107 1.00 35.45  ? 337  ILE B N     1 
ATOM   6637 C CA    . ILE B 1 337 ? 5.728   59.602  -11.946 1.00 39.13  ? 337  ILE B CA    1 
ATOM   6638 C C     . ILE B 1 337 ? 5.179   61.026  -12.132 1.00 43.42  ? 337  ILE B C     1 
ATOM   6639 O O     . ILE B 1 337 ? 4.195   61.170  -12.844 1.00 39.40  ? 337  ILE B O     1 
ATOM   6640 C CB    . ILE B 1 337 ? 5.381   59.016  -10.570 1.00 41.71  ? 337  ILE B CB    1 
ATOM   6641 C CG1   . ILE B 1 337 ? 5.738   57.529  -10.501 1.00 41.32  ? 337  ILE B CG1   1 
ATOM   6642 C CG2   . ILE B 1 337 ? 3.929   59.282  -10.201 1.00 38.64  ? 337  ILE B CG2   1 
ATOM   6643 C CD1   . ILE B 1 337 ? 5.743   56.976  -9.091  1.00 44.68  ? 337  ILE B CD1   1 
ATOM   6644 N N     . LYS B 1 338 ? 5.809   62.029  -11.510 1.00 43.11  ? 338  LYS B N     1 
ATOM   6645 C CA    . LYS B 1 338 ? 5.456   63.460  -11.684 1.00 50.27  ? 338  LYS B CA    1 
ATOM   6646 C C     . LYS B 1 338 ? 5.607   63.825  -13.164 1.00 46.90  ? 338  LYS B C     1 
ATOM   6647 O O     . LYS B 1 338 ? 4.680   64.453  -13.709 1.00 46.18  ? 338  LYS B O     1 
ATOM   6648 C CB    . LYS B 1 338 ? 6.312   64.366  -10.789 1.00 51.52  ? 338  LYS B CB    1 
ATOM   6649 C CG    . LYS B 1 338 ? 5.893   64.429  -9.326  1.00 56.19  ? 338  LYS B CG    1 
ATOM   6650 C CD    . LYS B 1 338 ? 6.903   65.116  -8.414  1.00 60.90  ? 338  LYS B CD    1 
ATOM   6651 C CE    . LYS B 1 338 ? 7.537   66.353  -9.019  1.00 69.60  ? 338  LYS B CE    1 
ATOM   6652 N NZ    . LYS B 1 338 ? 8.376   67.090  -8.042  1.00 75.81  ? 338  LYS B NZ    1 
ATOM   6653 N N     . ASP B 1 339 ? 6.734   63.478  -13.782 1.00 47.82  ? 339  ASP B N     1 
ATOM   6654 C CA    . ASP B 1 339 ? 7.037   63.882  -15.182 1.00 48.84  ? 339  ASP B CA    1 
ATOM   6655 C C     . ASP B 1 339 ? 5.976   63.298  -16.121 1.00 48.31  ? 339  ASP B C     1 
ATOM   6656 O O     . ASP B 1 339 ? 5.624   63.984  -17.096 1.00 46.77  ? 339  ASP B O     1 
ATOM   6657 C CB    . ASP B 1 339 ? 8.424   63.427  -15.638 1.00 57.96  ? 339  ASP B CB    1 
ATOM   6658 C CG    . ASP B 1 339 ? 8.719   63.748  -17.098 1.00 65.71  ? 339  ASP B CG    1 
ATOM   6659 O OD1   . ASP B 1 339 ? 8.624   64.939  -17.477 1.00 69.81  ? 339  ASP B OD1   1 
ATOM   6660 O OD2   . ASP B 1 339 ? 9.033   62.804  -17.854 1.00 79.95  ? 339  ASP B OD2   1 
ATOM   6661 N N     . ALA B 1 340 ? 5.500   62.074  -15.860 1.00 44.54  ? 340  ALA B N     1 
ATOM   6662 C CA    . ALA B 1 340 ? 4.582   61.344  -16.767 1.00 42.95  ? 340  ALA B CA    1 
ATOM   6663 C C     . ALA B 1 340 ? 3.139   61.834  -16.549 1.00 35.58  ? 340  ALA B C     1 
ATOM   6664 O O     . ALA B 1 340 ? 2.517   62.255  -17.530 1.00 38.28  ? 340  ALA B O     1 
ATOM   6665 C CB    . ALA B 1 340 ? 4.738   59.846  -16.590 1.00 39.21  ? 340  ALA B CB    1 
ATOM   6666 N N     . PHE B 1 341 ? 2.614   61.794  -15.325 1.00 40.30  ? 341  PHE B N     1 
ATOM   6667 C CA    . PHE B 1 341 ? 1.191   62.136  -15.034 1.00 39.32  ? 341  PHE B CA    1 
ATOM   6668 C C     . PHE B 1 341 ? 0.991   63.657  -15.085 1.00 38.20  ? 341  PHE B C     1 
ATOM   6669 O O     . PHE B 1 341 ? -0.145  64.081  -15.340 1.00 42.13  ? 341  PHE B O     1 
ATOM   6670 C CB    . PHE B 1 341 ? 0.728   61.573  -13.686 1.00 38.11  ? 341  PHE B CB    1 
ATOM   6671 C CG    . PHE B 1 341 ? 0.512   60.078  -13.667 1.00 41.12  ? 341  PHE B CG    1 
ATOM   6672 C CD1   . PHE B 1 341 ? -0.526  59.495  -14.379 1.00 40.39  ? 341  PHE B CD1   1 
ATOM   6673 C CD2   . PHE B 1 341 ? 1.359   59.251  -12.948 1.00 42.27  ? 341  PHE B CD2   1 
ATOM   6674 C CE1   . PHE B 1 341 ? -0.711  58.121  -14.373 1.00 38.78  ? 341  PHE B CE1   1 
ATOM   6675 C CE2   . PHE B 1 341 ? 1.168   57.879  -12.942 1.00 43.45  ? 341  PHE B CE2   1 
ATOM   6676 C CZ    . PHE B 1 341 ? 0.130   57.318  -13.658 1.00 39.68  ? 341  PHE B CZ    1 
ATOM   6677 N N     . GLY B 1 342 ? 2.058   64.425  -14.844 1.00 40.23  ? 342  GLY B N     1 
ATOM   6678 C CA    . GLY B 1 342 ? 2.143   65.890  -14.992 1.00 35.01  ? 342  GLY B CA    1 
ATOM   6679 C C     . GLY B 1 342 ? 1.879   66.333  -16.412 1.00 37.77  ? 342  GLY B C     1 
ATOM   6680 O O     . GLY B 1 342 ? 1.503   67.479  -16.589 1.00 41.67  ? 342  GLY B O     1 
ATOM   6681 N N     . GLN B 1 343 ? 1.993   65.445  -17.396 1.00 43.29  ? 343  GLN B N     1 
ATOM   6682 C CA    . GLN B 1 343 ? 1.613   65.744  -18.806 1.00 46.26  ? 343  GLN B CA    1 
ATOM   6683 C C     . GLN B 1 343 ? 0.099   65.981  -18.889 1.00 47.15  ? 343  GLN B C     1 
ATOM   6684 O O     . GLN B 1 343 ? -0.361  66.566  -19.882 1.00 47.64  ? 343  GLN B O     1 
ATOM   6685 C CB    . GLN B 1 343 ? 2.065   64.615  -19.735 1.00 50.87  ? 343  GLN B CB    1 
ATOM   6686 C CG    . GLN B 1 343 ? 3.553   64.291  -19.628 1.00 59.50  ? 343  GLN B CG    1 
ATOM   6687 C CD    . GLN B 1 343 ? 4.385   64.767  -20.791 1.00 61.85  ? 343  GLN B CD    1 
ATOM   6688 O OE1   . GLN B 1 343 ? 4.599   64.039  -21.758 1.00 66.58  ? 343  GLN B OE1   1 
ATOM   6689 N NE2   . GLN B 1 343 ? 4.898   65.982  -20.680 1.00 66.78  ? 343  GLN B NE2   1 
ATOM   6690 N N     . ILE B 1 344 ? -0.667  65.521  -17.901 1.00 46.62  ? 344  ILE B N     1 
ATOM   6691 C CA    . ILE B 1 344 ? -2.127  65.802  -17.830 1.00 44.41  ? 344  ILE B CA    1 
ATOM   6692 C C     . ILE B 1 344 ? -2.332  67.173  -17.177 1.00 44.28  ? 344  ILE B C     1 
ATOM   6693 O O     . ILE B 1 344 ? -2.035  67.375  -16.001 1.00 38.61  ? 344  ILE B O     1 
ATOM   6694 C CB    . ILE B 1 344 ? -2.867  64.658  -17.108 1.00 42.27  ? 344  ILE B CB    1 
ATOM   6695 C CG1   . ILE B 1 344 ? -2.659  63.327  -17.836 1.00 42.99  ? 344  ILE B CG1   1 
ATOM   6696 C CG2   . ILE B 1 344 ? -4.341  64.987  -16.942 1.00 42.98  ? 344  ILE B CG2   1 
ATOM   6697 C CD1   . ILE B 1 344 ? -3.424  62.156  -17.238 1.00 42.59  ? 344  ILE B CD1   1 
ATOM   6698 N N     . PRO B 1 345 ? -2.894  68.163  -17.908 1.00 44.51  ? 345  PRO B N     1 
ATOM   6699 C CA    . PRO B 1 345 ? -3.224  69.453  -17.304 1.00 42.02  ? 345  PRO B CA    1 
ATOM   6700 C C     . PRO B 1 345 ? -4.245  69.293  -16.175 1.00 41.33  ? 345  PRO B C     1 
ATOM   6701 O O     . PRO B 1 345 ? -5.160  68.491  -16.313 1.00 45.11  ? 345  PRO B O     1 
ATOM   6702 C CB    . PRO B 1 345 ? -3.839  70.299  -18.427 1.00 45.54  ? 345  PRO B CB    1 
ATOM   6703 C CG    . PRO B 1 345 ? -3.829  69.442  -19.676 1.00 45.88  ? 345  PRO B CG    1 
ATOM   6704 C CD    . PRO B 1 345 ? -3.225  68.094  -19.337 1.00 47.58  ? 345  PRO B CD    1 
ATOM   6705 N N     . GLY B 1 346 ? -4.085  70.065  -15.103 1.00 38.22  ? 346  GLY B N     1 
ATOM   6706 C CA    . GLY B 1 346 ? -4.941  69.998  -13.908 1.00 40.52  ? 346  GLY B CA    1 
ATOM   6707 C C     . GLY B 1 346 ? -4.416  68.970  -12.929 1.00 39.87  ? 346  GLY B C     1 
ATOM   6708 O O     . GLY B 1 346 ? -5.054  68.776  -11.877 1.00 46.28  ? 346  GLY B O     1 
ATOM   6709 N N     . SER B 1 347 ? -3.318  68.303  -13.284 1.00 40.89  ? 347  SER B N     1 
ATOM   6710 C CA    . SER B 1 347 ? -2.603  67.320  -12.426 1.00 44.57  ? 347  SER B CA    1 
ATOM   6711 C C     . SER B 1 347 ? -2.062  68.022  -11.195 1.00 36.71  ? 347  SER B C     1 
ATOM   6712 O O     . SER B 1 347 ? -1.351  68.984  -11.393 1.00 36.67  ? 347  SER B O     1 
ATOM   6713 C CB    . SER B 1 347 ? -1.480  66.672  -13.176 1.00 46.33  ? 347  SER B CB    1 
ATOM   6714 O OG    . SER B 1 347 ? -1.991  65.569  -13.898 1.00 56.41  ? 347  SER B OG    1 
ATOM   6715 N N     . ARG B 1 348 ? -2.358  67.536  -9.988  1.00 40.85  ? 348  ARG B N     1 
ATOM   6716 C CA    . ARG B 1 348 ? -1.724  68.067  -8.752  1.00 43.93  ? 348  ARG B CA    1 
ATOM   6717 C C     . ARG B 1 348 ? -1.222  66.896  -7.897  1.00 41.01  ? 348  ARG B C     1 
ATOM   6718 O O     . ARG B 1 348 ? -1.978  65.925  -7.694  1.00 37.56  ? 348  ARG B O     1 
ATOM   6719 C CB    . ARG B 1 348 ? -2.706  68.952  -7.974  1.00 49.43  ? 348  ARG B CB    1 
ATOM   6720 C CG    . ARG B 1 348 ? -2.960  70.330  -8.577  1.00 57.76  ? 348  ARG B CG    1 
ATOM   6721 C CD    . ARG B 1 348 ? -3.771  71.233  -7.638  1.00 65.26  ? 348  ARG B CD    1 
ATOM   6722 N NE    . ARG B 1 348 ? -4.957  70.570  -7.083  1.00 69.50  ? 348  ARG B NE    1 
ATOM   6723 C CZ    . ARG B 1 348 ? -5.028  69.900  -5.920  1.00 73.94  ? 348  ARG B CZ    1 
ATOM   6724 N NH1   . ARG B 1 348 ? -3.978  69.789  -5.115  1.00 70.14  ? 348  ARG B NH1   1 
ATOM   6725 N NH2   . ARG B 1 348 ? -6.171  69.329  -5.567  1.00 74.15  ? 348  ARG B NH2   1 
ATOM   6726 N N     . PHE B 1 349 ? 0.003   67.002  -7.384  1.00 40.54  ? 349  PHE B N     1 
ATOM   6727 C CA    . PHE B 1 349 ? 0.746   65.900  -6.713  1.00 38.11  ? 349  PHE B CA    1 
ATOM   6728 C C     . PHE B 1 349 ? 1.020   66.298  -5.279  1.00 37.88  ? 349  PHE B C     1 
ATOM   6729 O O     . PHE B 1 349 ? 1.537   67.413  -5.118  1.00 44.87  ? 349  PHE B O     1 
ATOM   6730 C CB    . PHE B 1 349 ? 2.087   65.642  -7.399  1.00 39.15  ? 349  PHE B CB    1 
ATOM   6731 C CG    . PHE B 1 349 ? 1.977   65.163  -8.817  1.00 39.89  ? 349  PHE B CG    1 
ATOM   6732 C CD1   . PHE B 1 349 ? 1.719   66.053  -9.847  1.00 40.80  ? 349  PHE B CD1   1 
ATOM   6733 C CD2   . PHE B 1 349 ? 2.102   63.818  -9.115  1.00 39.06  ? 349  PHE B CD2   1 
ATOM   6734 C CE1   . PHE B 1 349 ? 1.600   65.609  -11.156 1.00 42.15  ? 349  PHE B CE1   1 
ATOM   6735 C CE2   . PHE B 1 349 ? 1.974   63.374  -10.423 1.00 40.52  ? 349  PHE B CE2   1 
ATOM   6736 C CZ    . PHE B 1 349 ? 1.725   64.268  -11.440 1.00 42.81  ? 349  PHE B CZ    1 
ATOM   6737 N N     . GLN B 1 350 ? 0.693   65.440  -4.312  1.00 36.77  ? 350  GLN B N     1 
ATOM   6738 C CA    . GLN B 1 350 ? 0.955   65.640  -2.861  1.00 40.38  ? 350  GLN B CA    1 
ATOM   6739 C C     . GLN B 1 350 ? 1.320   64.300  -2.203  1.00 41.44  ? 350  GLN B C     1 
ATOM   6740 O O     . GLN B 1 350 ? 0.673   63.291  -2.498  1.00 41.19  ? 350  GLN B O     1 
ATOM   6741 C CB    . GLN B 1 350 ? -0.269  66.255  -2.189  1.00 43.33  ? 350  GLN B CB    1 
ATOM   6742 C CG    . GLN B 1 350 ? -0.580  67.665  -2.685  1.00 51.08  ? 350  GLN B CG    1 
ATOM   6743 C CD    . GLN B 1 350 ? -0.213  68.712  -1.666  1.00 57.25  ? 350  GLN B CD    1 
ATOM   6744 O OE1   . GLN B 1 350 ? -1.066  69.214  -0.941  1.00 60.06  ? 350  GLN B OE1   1 
ATOM   6745 N NE2   . GLN B 1 350 ? 1.074   69.008  -1.569  1.00 59.41  ? 350  GLN B NE2   1 
ATOM   6746 N N     . THR B 1 351 ? 2.316   64.307  -1.322  1.00 40.85  ? 351  THR B N     1 
ATOM   6747 C CA    . THR B 1 351 ? 2.764   63.125  -0.543  1.00 42.48  ? 351  THR B CA    1 
ATOM   6748 C C     . THR B 1 351 ? 1.998   63.071  0.781   1.00 43.98  ? 351  THR B C     1 
ATOM   6749 O O     . THR B 1 351 ? 1.354   64.096  1.150   1.00 36.40  ? 351  THR B O     1 
ATOM   6750 C CB    . THR B 1 351 ? 4.277   63.154  -0.311  1.00 41.25  ? 351  THR B CB    1 
ATOM   6751 O OG1   . THR B 1 351 ? 4.577   64.190  0.627   1.00 41.53  ? 351  THR B OG1   1 
ATOM   6752 C CG2   . THR B 1 351 ? 5.064   63.358  -1.591  1.00 40.86  ? 351  THR B CG2   1 
ATOM   6753 N N     . HIS B 1 352 ? 2.084   61.924  1.466   1.00 38.84  ? 352  HIS B N     1 
ATOM   6754 C CA    . HIS B 1 352 ? 1.518   61.684  2.820   1.00 39.03  ? 352  HIS B CA    1 
ATOM   6755 C C     . HIS B 1 352 ? 2.177   62.607  3.865   1.00 44.30  ? 352  HIS B C     1 
ATOM   6756 O O     . HIS B 1 352 ? 1.603   62.754  4.959   1.00 47.25  ? 352  HIS B O     1 
ATOM   6757 C CB    . HIS B 1 352 ? 1.682   60.207  3.199   1.00 41.62  ? 352  HIS B CB    1 
ATOM   6758 C CG    . HIS B 1 352 ? 3.079   59.875  3.616   1.00 39.91  ? 352  HIS B CG    1 
ATOM   6759 N ND1   . HIS B 1 352 ? 3.418   59.652  4.930   1.00 41.45  ? 352  HIS B ND1   1 
ATOM   6760 C CD2   . HIS B 1 352 ? 4.229   59.802  2.912   1.00 39.06  ? 352  HIS B CD2   1 
ATOM   6761 C CE1   . HIS B 1 352 ? 4.717   59.452  5.016   1.00 36.64  ? 352  HIS B CE1   1 
ATOM   6762 N NE2   . HIS B 1 352 ? 5.234   59.538  3.803   1.00 40.61  ? 352  HIS B NE2   1 
ATOM   6763 N N     . GLU B 1 353 ? 3.354   63.168  3.578   1.00 47.93  ? 353  GLU B N     1 
ATOM   6764 C CA    . GLU B 1 353 ? 4.075   64.080  4.505   1.00 57.37  ? 353  GLU B CA    1 
ATOM   6765 C C     . GLU B 1 353 ? 3.511   65.510  4.419   1.00 58.39  ? 353  GLU B C     1 
ATOM   6766 O O     . GLU B 1 353 ? 3.659   66.248  5.405   1.00 57.04  ? 353  GLU B O     1 
ATOM   6767 C CB    . GLU B 1 353 ? 5.573   64.104  4.191   1.00 58.86  ? 353  GLU B CB    1 
ATOM   6768 C CG    . GLU B 1 353 ? 6.220   62.730  4.186   1.00 60.01  ? 353  GLU B CG    1 
ATOM   6769 C CD    . GLU B 1 353 ? 7.728   62.742  4.373   1.00 63.20  ? 353  GLU B CD    1 
ATOM   6770 O OE1   . GLU B 1 353 ? 8.404   63.545  3.705   1.00 61.10  ? 353  GLU B OE1   1 
ATOM   6771 O OE2   . GLU B 1 353 ? 8.222   61.952  5.203   1.00 72.17  ? 353  GLU B OE2   1 
ATOM   6772 N N     . GLU B 1 354 ? 2.900   65.902  3.294   1.00 60.92  ? 354  GLU B N     1 
ATOM   6773 C CA    . GLU B 1 354 ? 2.643   67.338  2.985   1.00 60.94  ? 354  GLU B CA    1 
ATOM   6774 C C     . GLU B 1 354 ? 1.153   67.651  2.772   1.00 60.23  ? 354  GLU B C     1 
ATOM   6775 O O     . GLU B 1 354 ? 0.881   68.723  2.201   1.00 70.62  ? 354  GLU B O     1 
ATOM   6776 C CB    . GLU B 1 354 ? 3.487   67.776  1.786   1.00 57.28  ? 354  GLU B CB    1 
ATOM   6777 C CG    . GLU B 1 354 ? 3.093   67.138  0.480   1.00 57.77  ? 354  GLU B CG    1 
ATOM   6778 C CD    . GLU B 1 354 ? 4.046   67.432  -0.667  1.00 62.70  ? 354  GLU B CD    1 
ATOM   6779 O OE1   . GLU B 1 354 ? 3.885   66.812  -1.729  1.00 58.21  ? 354  GLU B OE1   1 
ATOM   6780 O OE2   . GLU B 1 354 ? 4.943   68.290  -0.503  1.00 63.03  ? 354  GLU B OE2   1 
ATOM   6781 N N     . ARG B 1 355 ? 0.217   66.837  3.277   1.00 59.37  ? 355  ARG B N     1 
ATOM   6782 C CA    . ARG B 1 355 ? -1.228  67.179  3.207   1.00 60.95  ? 355  ARG B CA    1 
ATOM   6783 C C     . ARG B 1 355 ? -1.862  67.230  4.609   1.00 64.78  ? 355  ARG B C     1 
ATOM   6784 O O     . ARG B 1 355 ? -1.954  68.352  5.155   1.00 76.62  ? 355  ARG B O     1 
ATOM   6785 C CB    . ARG B 1 355 ? -1.911  66.243  2.212   1.00 64.35  ? 355  ARG B CB    1 
ATOM   6786 C CG    . ARG B 1 355 ? -3.153  66.859  1.594   1.00 65.94  ? 355  ARG B CG    1 
ATOM   6787 C CD    . ARG B 1 355 ? -3.454  66.401  0.186   1.00 64.75  ? 355  ARG B CD    1 
ATOM   6788 N NE    . ARG B 1 355 ? -4.583  67.194  -0.256  1.00 70.95  ? 355  ARG B NE    1 
ATOM   6789 C CZ    . ARG B 1 355 ? -5.844  66.958  0.080   1.00 67.56  ? 355  ARG B CZ    1 
ATOM   6790 N NH1   . ARG B 1 355 ? -6.136  65.923  0.839   1.00 73.26  ? 355  ARG B NH1   1 
ATOM   6791 N NH2   . ARG B 1 355 ? -6.812  67.754  -0.337  1.00 59.35  ? 355  ARG B NH2   1 
ATOM   6792 N N     . HIS B 1 356 ? -2.332  66.101  5.154   1.00 64.75  ? 356  HIS B N     1 
ATOM   6793 C CA    . HIS B 1 356 ? -2.900  65.963  6.532   1.00 68.12  ? 356  HIS B CA    1 
ATOM   6794 C C     . HIS B 1 356 ? -4.243  66.687  6.757   1.00 60.76  ? 356  HIS B C     1 
ATOM   6795 O O     . HIS B 1 356 ? -4.649  66.749  7.922   1.00 69.20  ? 356  HIS B O     1 
ATOM   6796 C CB    . HIS B 1 356 ? -1.871  66.400  7.590   1.00 70.74  ? 356  HIS B CB    1 
ATOM   6797 C CG    . HIS B 1 356 ? -0.881  65.334  7.891   1.00 72.00  ? 356  HIS B CG    1 
ATOM   6798 N ND1   . HIS B 1 356 ? 0.323   65.255  7.230   1.00 75.13  ? 356  HIS B ND1   1 
ATOM   6799 C CD2   . HIS B 1 356 ? -0.938  64.279  8.730   1.00 73.85  ? 356  HIS B CD2   1 
ATOM   6800 C CE1   . HIS B 1 356 ? 0.988   64.206  7.671   1.00 78.28  ? 356  HIS B CE1   1 
ATOM   6801 N NE2   . HIS B 1 356 ? 0.233   63.590  8.594   1.00 78.03  ? 356  HIS B NE2   1 
ATOM   6802 N N     . ASP B 1 357 ? -4.946  67.159  5.721   1.00 61.25  ? 357  ASP B N     1 
ATOM   6803 C CA    . ASP B 1 357 ? -6.273  67.834  5.855   1.00 56.13  ? 357  ASP B CA    1 
ATOM   6804 C C     . ASP B 1 357 ? -7.410  66.809  5.715   1.00 52.41  ? 357  ASP B C     1 
ATOM   6805 O O     . ASP B 1 357 ? -7.127  65.616  5.482   1.00 47.29  ? 357  ASP B O     1 
ATOM   6806 C CB    . ASP B 1 357 ? -6.421  68.992  4.859   1.00 58.11  ? 357  ASP B CB    1 
ATOM   6807 C CG    . ASP B 1 357 ? -6.274  68.607  3.393   1.00 57.69  ? 357  ASP B CG    1 
ATOM   6808 O OD1   . ASP B 1 357 ? -6.635  67.475  3.045   1.00 56.17  ? 357  ASP B OD1   1 
ATOM   6809 O OD2   . ASP B 1 357 ? -5.785  69.449  2.616   1.00 52.08  ? 357  ASP B OD2   1 
ATOM   6810 N N     . ARG B 1 358 ? -8.655  67.268  5.834   1.00 52.00  ? 358  ARG B N     1 
ATOM   6811 C CA    . ARG B 1 358 ? -9.893  66.438  5.800   1.00 52.18  ? 358  ARG B CA    1 
ATOM   6812 C C     . ARG B 1 358 ? -9.939  65.584  4.514   1.00 54.15  ? 358  ARG B C     1 
ATOM   6813 O O     . ARG B 1 358 ? -10.366 64.386  4.590   1.00 46.12  ? 358  ARG B O     1 
ATOM   6814 C CB    . ARG B 1 358 ? -11.110 67.364  5.889   1.00 52.15  ? 358  ARG B CB    1 
ATOM   6815 C CG    . ARG B 1 358 ? -12.444 66.638  5.922   1.00 54.44  ? 358  ARG B CG    1 
ATOM   6816 C CD    . ARG B 1 358 ? -13.644 67.542  5.669   1.00 55.41  ? 358  ARG B CD    1 
ATOM   6817 N NE    . ARG B 1 358 ? -14.876 66.792  5.909   1.00 57.80  ? 358  ARG B NE    1 
ATOM   6818 C CZ    . ARG B 1 358 ? -16.093 67.142  5.505   1.00 58.77  ? 358  ARG B CZ    1 
ATOM   6819 N NH1   . ARG B 1 358 ? -16.287 68.266  4.835   1.00 59.20  ? 358  ARG B NH1   1 
ATOM   6820 N NH2   . ARG B 1 358 ? -17.118 66.358  5.789   1.00 55.51  ? 358  ARG B NH2   1 
ATOM   6821 N N     . GLY B 1 359 ? -9.542  66.178  3.381   1.00 47.62  ? 359  GLY B N     1 
ATOM   6822 C CA    . GLY B 1 359 ? -9.463  65.519  2.063   1.00 50.52  ? 359  GLY B CA    1 
ATOM   6823 C C     . GLY B 1 359 ? -8.284  64.556  1.953   1.00 52.53  ? 359  GLY B C     1 
ATOM   6824 O O     . GLY B 1 359 ? -8.202  63.848  0.920   1.00 50.22  ? 359  GLY B O     1 
ATOM   6825 N N     . ALA B 1 360 ? -7.373  64.561  2.935   1.00 45.70  ? 360  ALA B N     1 
ATOM   6826 C CA    . ALA B 1 360 ? -6.138  63.739  2.968   1.00 48.76  ? 360  ALA B CA    1 
ATOM   6827 C C     . ALA B 1 360 ? -6.400  62.427  3.707   1.00 46.39  ? 360  ALA B C     1 
ATOM   6828 O O     . ALA B 1 360 ? -5.501  61.572  3.737   1.00 47.71  ? 360  ALA B O     1 
ATOM   6829 C CB    . ALA B 1 360 ? -5.004  64.508  3.608   1.00 45.57  ? 360  ALA B CB    1 
ATOM   6830 N N     . HIS B 1 361 ? -7.593  62.270  4.271   1.00 43.53  ? 361  HIS B N     1 
ATOM   6831 C CA    . HIS B 1 361 ? -7.965  61.073  5.058   1.00 46.63  ? 361  HIS B CA    1 
ATOM   6832 C C     . HIS B 1 361 ? -7.646  59.804  4.248   1.00 42.59  ? 361  HIS B C     1 
ATOM   6833 O O     . HIS B 1 361 ? -7.063  58.878  4.817   1.00 39.09  ? 361  HIS B O     1 
ATOM   6834 C CB    . HIS B 1 361 ? -9.428  61.159  5.495   1.00 49.82  ? 361  HIS B CB    1 
ATOM   6835 C CG    . HIS B 1 361 ? -9.730  60.231  6.617   1.00 60.21  ? 361  HIS B CG    1 
ATOM   6836 N ND1   . HIS B 1 361 ? -10.222 58.953  6.400   1.00 70.33  ? 361  HIS B ND1   1 
ATOM   6837 C CD2   . HIS B 1 361 ? -9.576  60.364  7.951   1.00 63.92  ? 361  HIS B CD2   1 
ATOM   6838 C CE1   . HIS B 1 361 ? -10.374 58.345  7.559   1.00 69.52  ? 361  HIS B CE1   1 
ATOM   6839 N NE2   . HIS B 1 361 ? -9.974  59.187  8.525   1.00 69.46  ? 361  HIS B NE2   1 
ATOM   6840 N N     . VAL B 1 362 ? -8.018  59.755  2.969   1.00 44.87  ? 362  VAL B N     1 
ATOM   6841 C CA    . VAL B 1 362 ? -7.833  58.544  2.114   1.00 41.39  ? 362  VAL B CA    1 
ATOM   6842 C C     . VAL B 1 362 ? -6.339  58.360  1.817   1.00 40.87  ? 362  VAL B C     1 
ATOM   6843 O O     . VAL B 1 362 ? -5.860  57.240  2.033   1.00 39.10  ? 362  VAL B O     1 
ATOM   6844 C CB    . VAL B 1 362 ? -8.716  58.582  0.849   1.00 45.43  ? 362  VAL B CB    1 
ATOM   6845 C CG1   . VAL B 1 362 ? -8.298  57.538  -0.175  1.00 42.67  ? 362  VAL B CG1   1 
ATOM   6846 C CG2   . VAL B 1 362 ? -10.182 58.391  1.225   1.00 47.89  ? 362  VAL B CG2   1 
ATOM   6847 N N     . LEU B 1 363 ? -5.621  59.415  1.410   1.00 39.04  ? 363  LEU B N     1 
ATOM   6848 C CA    . LEU B 1 363 ? -4.144  59.395  1.216   1.00 42.55  ? 363  LEU B CA    1 
ATOM   6849 C C     . LEU B 1 363 ? -3.461  58.817  2.471   1.00 45.28  ? 363  LEU B C     1 
ATOM   6850 O O     . LEU B 1 363 ? -2.571  57.958  2.320   1.00 41.03  ? 363  LEU B O     1 
ATOM   6851 C CB    . LEU B 1 363 ? -3.663  60.810  0.866   1.00 42.15  ? 363  LEU B CB    1 
ATOM   6852 C CG    . LEU B 1 363 ? -2.197  61.144  1.139   1.00 44.39  ? 363  LEU B CG    1 
ATOM   6853 C CD1   . LEU B 1 363 ? -1.234  60.237  0.391   1.00 48.05  ? 363  LEU B CD1   1 
ATOM   6854 C CD2   . LEU B 1 363 ? -1.919  62.577  0.753   1.00 48.29  ? 363  LEU B CD2   1 
ATOM   6855 N N     . GLN B 1 364 ? -3.866  59.241  3.667   1.00 39.59  ? 364  GLN B N     1 
ATOM   6856 C CA    . GLN B 1 364 ? -3.229  58.794  4.934   1.00 39.97  ? 364  GLN B CA    1 
ATOM   6857 C C     . GLN B 1 364 ? -3.607  57.334  5.187   1.00 38.71  ? 364  GLN B C     1 
ATOM   6858 O O     . GLN B 1 364 ? -2.787  56.604  5.758   1.00 41.25  ? 364  GLN B O     1 
ATOM   6859 C CB    . GLN B 1 364 ? -3.630  59.701  6.106   1.00 39.28  ? 364  GLN B CB    1 
ATOM   6860 C CG    . GLN B 1 364 ? -3.045  61.113  6.011   1.00 38.69  ? 364  GLN B CG    1 
ATOM   6861 C CD    . GLN B 1 364 ? -1.544  61.095  5.890   1.00 40.71  ? 364  GLN B CD    1 
ATOM   6862 O OE1   . GLN B 1 364 ? -0.897  60.132  6.294   1.00 45.39  ? 364  GLN B OE1   1 
ATOM   6863 N NE2   . GLN B 1 364 ? -0.972  62.139  5.305   1.00 40.77  ? 364  GLN B NE2   1 
ATOM   6864 N N     . ASP B 1 365 ? -4.802  56.923  4.776   1.00 38.23  ? 365  ASP B N     1 
ATOM   6865 C CA    . ASP B 1 365 ? -5.288  55.536  4.965   1.00 39.79  ? 365  ASP B CA    1 
ATOM   6866 C C     . ASP B 1 365 ? -4.560  54.635  3.964   1.00 42.59  ? 365  ASP B C     1 
ATOM   6867 O O     . ASP B 1 365 ? -4.193  53.536  4.358   1.00 36.27  ? 365  ASP B O     1 
ATOM   6868 C CB    . ASP B 1 365 ? -6.797  55.411  4.798   1.00 38.55  ? 365  ASP B CB    1 
ATOM   6869 C CG    . ASP B 1 365 ? -7.362  54.145  5.417   1.00 40.85  ? 365  ASP B CG    1 
ATOM   6870 O OD1   . ASP B 1 365 ? -6.939  53.796  6.559   1.00 39.35  ? 365  ASP B OD1   1 
ATOM   6871 O OD2   . ASP B 1 365 ? -8.232  53.517  4.770   1.00 41.46  ? 365  ASP B OD2   1 
ATOM   6872 N N     . ARG B 1 366 ? -4.368  55.105  2.730   1.00 39.81  ? 366  ARG B N     1 
ATOM   6873 C CA    . ARG B 1 366 ? -3.609  54.376  1.688   1.00 40.87  ? 366  ARG B CA    1 
ATOM   6874 C C     . ARG B 1 366 ? -2.165  54.203  2.178   1.00 41.89  ? 366  ARG B C     1 
ATOM   6875 O O     . ARG B 1 366 ? -1.581  53.128  1.937   1.00 47.81  ? 366  ARG B O     1 
ATOM   6876 C CB    . ARG B 1 366 ? -3.632  55.110  0.340   1.00 38.92  ? 366  ARG B CB    1 
ATOM   6877 C CG    . ARG B 1 366 ? -5.013  55.338  -0.273  1.00 40.12  ? 366  ARG B CG    1 
ATOM   6878 C CD    . ARG B 1 366 ? -6.129  54.368  0.087   1.00 36.37  ? 366  ARG B CD    1 
ATOM   6879 N NE    . ARG B 1 366 ? -5.906  53.058  -0.520  1.00 37.48  ? 366  ARG B NE    1 
ATOM   6880 C CZ    . ARG B 1 366 ? -6.732  52.014  -0.423  1.00 34.03  ? 366  ARG B CZ    1 
ATOM   6881 N NH1   . ARG B 1 366 ? -7.845  52.103  0.279   1.00 34.18  ? 366  ARG B NH1   1 
ATOM   6882 N NH2   . ARG B 1 366 ? -6.432  50.871  -1.020  1.00 37.61  ? 366  ARG B NH2   1 
ATOM   6883 N N     . HIS B 1 367 ? -1.599  55.217  2.832   1.00 37.93  ? 367  HIS B N     1 
ATOM   6884 C CA    . HIS B 1 367 ? -0.214  55.155  3.354   1.00 40.29  ? 367  HIS B CA    1 
ATOM   6885 C C     . HIS B 1 367 ? -0.123  53.992  4.326   1.00 34.93  ? 367  HIS B C     1 
ATOM   6886 O O     . HIS B 1 367 ? 0.869   53.284  4.286   1.00 36.18  ? 367  HIS B O     1 
ATOM   6887 C CB    . HIS B 1 367 ? 0.215   56.446  4.040   1.00 42.02  ? 367  HIS B CB    1 
ATOM   6888 C CG    . HIS B 1 367 ? 1.640   56.419  4.457   1.00 40.66  ? 367  HIS B CG    1 
ATOM   6889 N ND1   . HIS B 1 367 ? 2.656   56.206  3.553   1.00 42.51  ? 367  HIS B ND1   1 
ATOM   6890 C CD2   . HIS B 1 367 ? 2.226   56.617  5.662   1.00 43.45  ? 367  HIS B CD2   1 
ATOM   6891 C CE1   . HIS B 1 367 ? 3.817   56.260  4.183   1.00 43.14  ? 367  HIS B CE1   1 
ATOM   6892 N NE2   . HIS B 1 367 ? 3.577   56.521  5.480   1.00 44.50  ? 367  HIS B NE2   1 
ATOM   6893 N N     . LYS B 1 368 ? -1.162  53.790  5.129   1.00 36.20  ? 368  LYS B N     1 
ATOM   6894 C CA    . LYS B 1 368 ? -1.212  52.669  6.088   1.00 41.34  ? 368  LYS B CA    1 
ATOM   6895 C C     . LYS B 1 368 ? -1.315  51.351  5.308   1.00 43.19  ? 368  LYS B C     1 
ATOM   6896 O O     . LYS B 1 368 ? -0.363  50.542  5.395   1.00 39.39  ? 368  LYS B O     1 
ATOM   6897 C CB    . LYS B 1 368 ? -2.352  52.915  7.074   1.00 46.45  ? 368  LYS B CB    1 
ATOM   6898 C CG    . LYS B 1 368 ? -2.092  54.074  8.021   1.00 47.46  ? 368  LYS B CG    1 
ATOM   6899 C CD    . LYS B 1 368 ? -3.320  54.578  8.731   1.00 51.59  ? 368  LYS B CD    1 
ATOM   6900 C CE    . LYS B 1 368 ? -4.014  53.523  9.557   1.00 58.02  ? 368  LYS B CE    1 
ATOM   6901 N NZ    . LYS B 1 368 ? -5.096  54.126  10.373  1.00 66.30  ? 368  LYS B NZ    1 
ATOM   6902 N N     . ILE B 1 369 ? -2.392  51.177  4.535   1.00 39.34  ? 369  ILE B N     1 
ATOM   6903 C CA    . ILE B 1 369 ? -2.731  49.912  3.816   1.00 38.66  ? 369  ILE B CA    1 
ATOM   6904 C C     . ILE B 1 369 ? -1.553  49.503  2.915   1.00 33.84  ? 369  ILE B C     1 
ATOM   6905 O O     . ILE B 1 369 ? -1.248  48.322  2.901   1.00 31.48  ? 369  ILE B O     1 
ATOM   6906 C CB    . ILE B 1 369 ? -4.038  50.075  3.018   1.00 42.62  ? 369  ILE B CB    1 
ATOM   6907 C CG1   . ILE B 1 369 ? -5.250  50.297  3.924   1.00 42.25  ? 369  ILE B CG1   1 
ATOM   6908 C CG2   . ILE B 1 369 ? -4.258  48.905  2.064   1.00 42.60  ? 369  ILE B CG2   1 
ATOM   6909 C CD1   . ILE B 1 369 ? -6.335  51.146  3.273   1.00 45.70  ? 369  ILE B CD1   1 
ATOM   6910 N N     . ASN B 1 370 ? -0.923  50.462  2.229   1.00 33.39  ? 370  ASN B N     1 
ATOM   6911 C CA    . ASN B 1 370 ? 0.200   50.261  1.283   1.00 35.79  ? 370  ASN B CA    1 
ATOM   6912 C C     . ASN B 1 370 ? 1.503   49.904  2.023   1.00 38.29  ? 370  ASN B C     1 
ATOM   6913 O O     . ASN B 1 370 ? 2.470   49.513  1.344   1.00 35.54  ? 370  ASN B O     1 
ATOM   6914 C CB    . ASN B 1 370 ? 0.425   51.497  0.409   1.00 35.34  ? 370  ASN B CB    1 
ATOM   6915 C CG    . ASN B 1 370 ? -0.711  51.772  -0.557  1.00 33.31  ? 370  ASN B CG    1 
ATOM   6916 O OD1   . ASN B 1 370 ? -1.702  51.063  -0.567  1.00 32.18  ? 370  ASN B OD1   1 
ATOM   6917 N ND2   . ASN B 1 370 ? -0.575  52.805  -1.370  1.00 33.10  ? 370  ASN B ND2   1 
ATOM   6918 N N     . ASN B 1 371 ? 1.546   50.086  3.344   1.00 37.85  ? 371  ASN B N     1 
ATOM   6919 C CA    . ASN B 1 371 ? 2.701   49.704  4.195   1.00 40.02  ? 371  ASN B CA    1 
ATOM   6920 C C     . ASN B 1 371 ? 2.298   48.544  5.117   1.00 41.20  ? 371  ASN B C     1 
ATOM   6921 O O     . ASN B 1 371 ? 3.013   48.316  6.094   1.00 38.27  ? 371  ASN B O     1 
ATOM   6922 C CB    . ASN B 1 371 ? 3.233   50.921  4.953   1.00 38.65  ? 371  ASN B CB    1 
ATOM   6923 C CG    . ASN B 1 371 ? 4.039   51.810  4.035   1.00 41.83  ? 371  ASN B CG    1 
ATOM   6924 O OD1   . ASN B 1 371 ? 5.144   51.447  3.659   1.00 43.75  ? 371  ASN B OD1   1 
ATOM   6925 N ND2   . ASN B 1 371 ? 3.485   52.940  3.627   1.00 39.34  ? 371  ASN B ND2   1 
ATOM   6926 N N     . GLY B 1 372 ? 1.217   47.825  4.791   1.00 38.75  ? 372  GLY B N     1 
ATOM   6927 C CA    . GLY B 1 372 ? 0.745   46.663  5.565   1.00 38.61  ? 372  GLY B CA    1 
ATOM   6928 C C     . GLY B 1 372 ? 0.336   47.030  6.977   1.00 38.26  ? 372  GLY B C     1 
ATOM   6929 O O     . GLY B 1 372 ? 0.379   46.139  7.867   1.00 36.44  ? 372  GLY B O     1 
ATOM   6930 N N     . ILE B 1 373 ? -0.040  48.285  7.215   1.00 39.84  ? 373  ILE B N     1 
ATOM   6931 C CA    . ILE B 1 373 ? -0.752  48.656  8.475   1.00 38.26  ? 373  ILE B CA    1 
ATOM   6932 C C     . ILE B 1 373 ? -2.237  48.507  8.189   1.00 35.56  ? 373  ILE B C     1 
ATOM   6933 O O     . ILE B 1 373 ? -2.788  49.246  7.381   1.00 39.69  ? 373  ILE B O     1 
ATOM   6934 C CB    . ILE B 1 373 ? -0.387  50.063  8.986   1.00 38.47  ? 373  ILE B CB    1 
ATOM   6935 C CG1   . ILE B 1 373 ? 1.052   50.120  9.477   1.00 40.19  ? 373  ILE B CG1   1 
ATOM   6936 C CG2   . ILE B 1 373 ? -1.356  50.517  10.073  1.00 40.51  ? 373  ILE B CG2   1 
ATOM   6937 C CD1   . ILE B 1 373 ? 2.030   50.453  8.412   1.00 43.56  ? 373  ILE B CD1   1 
ATOM   6938 N N     . PRO B 1 374 ? -2.896  47.549  8.909   1.00 38.46  ? 374  PRO B N     1 
ATOM   6939 C CA    . PRO B 1 374 ? -4.305  47.446  8.570   1.00 38.31  ? 374  PRO B CA    1 
ATOM   6940 C C     . PRO B 1 374 ? -5.216  48.494  9.191   1.00 45.03  ? 374  PRO B C     1 
ATOM   6941 O O     . PRO B 1 374 ? -4.841  49.116  10.164  1.00 38.08  ? 374  PRO B O     1 
ATOM   6942 C CB    . PRO B 1 374 ? -4.665  46.048  9.026   1.00 38.83  ? 374  PRO B CB    1 
ATOM   6943 C CG    . PRO B 1 374 ? -3.700  45.670  10.068  1.00 40.75  ? 374  PRO B CG    1 
ATOM   6944 C CD    . PRO B 1 374 ? -2.584  46.646  10.052  1.00 35.29  ? 374  PRO B CD    1 
ATOM   6945 N N     . SER B 1 375 ? -6.420  48.645  8.657   1.00 46.44  ? 375  SER B N     1 
ATOM   6946 C CA    . SER B 1 375 ? -7.315  49.709  9.082   1.00 49.08  ? 375  SER B CA    1 
ATOM   6947 C C     . SER B 1 375 ? -8.775  49.378  8.901   1.00 47.66  ? 375  SER B C     1 
ATOM   6948 O O     . SER B 1 375 ? -9.112  48.460  8.199   1.00 71.86  ? 375  SER B O     1 
ATOM   6949 C CB    . SER B 1 375 ? -6.994  50.947  8.250   1.00 46.55  ? 375  SER B CB    1 
ATOM   6950 O OG    . SER B 1 375 ? -7.862  52.010  8.523   1.00 46.56  ? 375  SER B OG    1 
ATOM   6951 N N     . LEU B 1 376 ? -9.645  50.128  9.545   1.00 70.37  ? 376  LEU B N     1 
ATOM   6952 C CA    . LEU B 1 376 ? -11.075 49.942  9.402   1.00 60.64  ? 376  LEU B CA    1 
ATOM   6953 C C     . LEU B 1 376 ? -11.648 51.295  9.023   1.00 49.76  ? 376  LEU B C     1 
ATOM   6954 O O     . LEU B 1 376 ? -12.845 51.465  8.946   1.00 44.78  ? 376  LEU B O     1 
ATOM   6955 C CB    . LEU B 1 376 ? -11.669 49.419  10.690  1.00 63.97  ? 376  LEU B CB    1 
ATOM   6956 C CG    . LEU B 1 376 ? -11.551 47.918  10.922  1.00 62.29  ? 376  LEU B CG    1 
ATOM   6957 C CD1   . LEU B 1 376 ? -12.197 47.529  12.236  1.00 59.27  ? 376  LEU B CD1   1 
ATOM   6958 C CD2   . LEU B 1 376 ? -12.170 47.153  9.773   1.00 62.47  ? 376  LEU B CD2   1 
ATOM   6959 N N     . SER B 1 377 ? -10.774 52.249  8.760   1.00 45.34  ? 377  SER B N     1 
ATOM   6960 C CA    . SER B 1 377 ? -11.196 53.584  8.354   1.00 49.26  ? 377  SER B CA    1 
ATOM   6961 C C     . SER B 1 377 ? -12.072 53.650  7.101   1.00 47.87  ? 377  SER B C     1 
ATOM   6962 O O     . SER B 1 377 ? -12.819 54.577  6.940   1.00 44.99  ? 377  SER B O     1 
ATOM   6963 C CB    . SER B 1 377 ? -9.990  54.512  8.190   1.00 50.02  ? 377  SER B CB    1 
ATOM   6964 O OG    . SER B 1 377 ? -9.241  54.598  9.384   1.00 51.37  ? 377  SER B OG    1 
ATOM   6965 N N     . GLU B 1 378 ? -11.991 52.671  6.221   1.00 43.12  ? 378  GLU B N     1 
ATOM   6966 C CA    . GLU B 1 378 ? -12.806 52.666  5.020   1.00 39.81  ? 378  GLU B CA    1 
ATOM   6967 C C     . GLU B 1 378 ? -14.255 52.304  5.318   1.00 38.31  ? 378  GLU B C     1 
ATOM   6968 O O     . GLU B 1 378 ? -15.103 52.430  4.485   1.00 37.96  ? 378  GLU B O     1 
ATOM   6969 C CB    . GLU B 1 378 ? -12.155 51.774  3.960   1.00 42.77  ? 378  GLU B CB    1 
ATOM   6970 C CG    . GLU B 1 378 ? -12.798 51.730  2.585   1.00 50.66  ? 378  GLU B CG    1 
ATOM   6971 C CD    . GLU B 1 378 ? -12.126 52.611  1.561   1.00 48.55  ? 378  GLU B CD    1 
ATOM   6972 O OE1   . GLU B 1 378 ? -12.174 52.250  0.380   1.00 54.98  ? 378  GLU B OE1   1 
ATOM   6973 O OE2   . GLU B 1 378 ? -11.571 53.663  1.918   1.00 59.00  ? 378  GLU B OE2   1 
ATOM   6974 N N     . MET B 1 379 ? -14.549 51.857  6.522   1.00 41.74  ? 379  MET B N     1 
ATOM   6975 C CA    . MET B 1 379 ? -15.936 51.612  6.894   1.00 45.72  ? 379  MET B CA    1 
ATOM   6976 C C     . MET B 1 379 ? -16.714 52.922  7.060   1.00 43.54  ? 379  MET B C     1 
ATOM   6977 O O     . MET B 1 379 ? -17.926 52.895  7.082   1.00 46.50  ? 379  MET B O     1 
ATOM   6978 C CB    . MET B 1 379 ? -16.028 50.770  8.159   1.00 49.96  ? 379  MET B CB    1 
ATOM   6979 C CG    . MET B 1 379 ? -15.731 49.297  7.959   1.00 48.36  ? 379  MET B CG    1 
ATOM   6980 S SD    . MET B 1 379 ? -16.923 48.527  6.863   1.00 53.45  ? 379  MET B SD    1 
ATOM   6981 C CE    . MET B 1 379 ? -18.372 48.554  7.905   1.00 51.20  ? 379  MET B CE    1 
ATOM   6982 N N     . LYS B 1 380 ? -16.019 54.038  7.217   1.00 41.93  ? 380  LYS B N     1 
ATOM   6983 C CA    . LYS B 1 380 ? -16.694 55.360  7.266   1.00 50.47  ? 380  LYS B CA    1 
ATOM   6984 C C     . LYS B 1 380 ? -17.622 55.432  6.060   1.00 51.15  ? 380  LYS B C     1 
ATOM   6985 O O     . LYS B 1 380 ? -18.679 56.055  6.157   1.00 52.68  ? 380  LYS B O     1 
ATOM   6986 C CB    . LYS B 1 380 ? -15.716 56.538  7.170   1.00 52.97  ? 380  LYS B CB    1 
ATOM   6987 C CG    . LYS B 1 380 ? -14.674 56.631  8.271   1.00 58.60  ? 380  LYS B CG    1 
ATOM   6988 C CD    . LYS B 1 380 ? -15.000 57.596  9.382   1.00 66.97  ? 380  LYS B CD    1 
ATOM   6989 C CE    . LYS B 1 380 ? -13.860 57.731  10.373  1.00 75.84  ? 380  LYS B CE    1 
ATOM   6990 N NZ    . LYS B 1 380 ? -13.240 56.422  10.714  1.00 76.12  ? 380  LYS B NZ    1 
ATOM   6991 N N     . LEU B 1 381 ? -17.183 54.818  4.960   1.00 52.90  ? 381  LEU B N     1 
ATOM   6992 C CA    . LEU B 1 381 ? -17.867 54.812  3.648   1.00 51.38  ? 381  LEU B CA    1 
ATOM   6993 C C     . LEU B 1 381 ? -19.332 54.413  3.824   1.00 43.88  ? 381  LEU B C     1 
ATOM   6994 O O     . LEU B 1 381 ? -20.189 54.987  3.116   1.00 44.57  ? 381  LEU B O     1 
ATOM   6995 C CB    . LEU B 1 381 ? -17.126 53.850  2.719   1.00 56.41  ? 381  LEU B CB    1 
ATOM   6996 C CG    . LEU B 1 381 ? -17.194 54.219  1.244   1.00 60.29  ? 381  LEU B CG    1 
ATOM   6997 C CD1   . LEU B 1 381 ? -16.038 53.588  0.490   1.00 64.57  ? 381  LEU B CD1   1 
ATOM   6998 C CD2   . LEU B 1 381 ? -18.535 53.814  0.652   1.00 62.96  ? 381  LEU B CD2   1 
ATOM   6999 N N     . MET B 1 382 ? -19.618 53.498  4.750   1.00 40.05  ? 382  MET B N     1 
ATOM   7000 C CA    . MET B 1 382 ? -20.965 52.903  4.911   1.00 41.96  ? 382  MET B CA    1 
ATOM   7001 C C     . MET B 1 382 ? -21.867 53.834  5.746   1.00 44.10  ? 382  MET B C     1 
ATOM   7002 O O     . MET B 1 382 ? -22.983 53.401  6.085   1.00 42.06  ? 382  MET B O     1 
ATOM   7003 C CB    . MET B 1 382 ? -20.882 51.508  5.541   1.00 44.67  ? 382  MET B CB    1 
ATOM   7004 C CG    . MET B 1 382 ? -19.850 50.599  4.854   1.00 46.56  ? 382  MET B CG    1 
ATOM   7005 S SD    . MET B 1 382 ? -20.045 50.555  3.047   1.00 50.84  ? 382  MET B SD    1 
ATOM   7006 C CE    . MET B 1 382 ? -21.651 49.765  2.917   1.00 46.55  ? 382  MET B CE    1 
ATOM   7007 N N     . ASP B 1 383 ? -21.436 55.073  6.002   1.00 42.81  ? 383  ASP B N     1 
ATOM   7008 C CA    . ASP B 1 383 ? -22.262 56.171  6.595   1.00 47.61  ? 383  ASP B CA    1 
ATOM   7009 C C     . ASP B 1 383 ? -22.720 57.157  5.512   1.00 45.85  ? 383  ASP B C     1 
ATOM   7010 O O     . ASP B 1 383 ? -23.305 58.182  5.862   1.00 46.99  ? 383  ASP B O     1 
ATOM   7011 C CB    . ASP B 1 383 ? -21.484 56.934  7.671   1.00 43.90  ? 383  ASP B CB    1 
ATOM   7012 C CG    . ASP B 1 383 ? -21.204 56.082  8.887   1.00 50.05  ? 383  ASP B CG    1 
ATOM   7013 O OD1   . ASP B 1 383 ? -22.036 55.195  9.193   1.00 51.22  ? 383  ASP B OD1   1 
ATOM   7014 O OD2   . ASP B 1 383 ? -20.156 56.303  9.511   1.00 55.77  ? 383  ASP B OD2   1 
ATOM   7015 N N     . TRP B 1 384 ? -22.441 56.862  4.246   1.00 44.27  ? 384  TRP B N     1 
ATOM   7016 C CA    . TRP B 1 384 ? -22.762 57.720  3.081   1.00 42.32  ? 384  TRP B CA    1 
ATOM   7017 C C     . TRP B 1 384 ? -24.253 58.059  3.075   1.00 39.40  ? 384  TRP B C     1 
ATOM   7018 O O     . TRP B 1 384 ? -24.563 59.192  2.779   1.00 45.16  ? 384  TRP B O     1 
ATOM   7019 C CB    . TRP B 1 384 ? -22.354 56.998  1.797   1.00 37.98  ? 384  TRP B CB    1 
ATOM   7020 C CG    . TRP B 1 384 ? -22.574 57.776  0.545   1.00 37.76  ? 384  TRP B CG    1 
ATOM   7021 C CD1   . TRP B 1 384 ? -23.369 57.409  -0.501  1.00 37.25  ? 384  TRP B CD1   1 
ATOM   7022 C CD2   . TRP B 1 384 ? -21.991 59.042  0.188   1.00 38.16  ? 384  TRP B CD2   1 
ATOM   7023 N NE1   . TRP B 1 384 ? -23.313 58.357  -1.484  1.00 39.52  ? 384  TRP B NE1   1 
ATOM   7024 C CE2   . TRP B 1 384 ? -22.482 59.368  -1.092  1.00 36.56  ? 384  TRP B CE2   1 
ATOM   7025 C CE3   . TRP B 1 384 ? -21.097 59.922  0.806   1.00 37.63  ? 384  TRP B CE3   1 
ATOM   7026 C CZ2   . TRP B 1 384 ? -22.123 60.541  -1.749  1.00 39.15  ? 384  TRP B CZ2   1 
ATOM   7027 C CZ3   . TRP B 1 384 ? -20.744 61.086  0.155   1.00 37.32  ? 384  TRP B CZ3   1 
ATOM   7028 C CH2   . TRP B 1 384 ? -21.241 61.381  -1.107  1.00 36.00  ? 384  TRP B CH2   1 
ATOM   7029 N N     . ILE B 1 385 ? -25.103 57.073  3.352   1.00 43.35  ? 385  ILE B N     1 
ATOM   7030 C CA    . ILE B 1 385 ? -26.586 57.178  3.481   1.00 46.42  ? 385  ILE B CA    1 
ATOM   7031 C C     . ILE B 1 385 ? -27.023 56.262  4.613   1.00 46.16  ? 385  ILE B C     1 
ATOM   7032 O O     . ILE B 1 385 ? -26.367 55.255  4.850   1.00 49.08  ? 385  ILE B O     1 
ATOM   7033 C CB    . ILE B 1 385 ? -27.301 56.789  2.171   1.00 43.46  ? 385  ILE B CB    1 
ATOM   7034 C CG1   . ILE B 1 385 ? -26.942 55.367  1.722   1.00 47.72  ? 385  ILE B CG1   1 
ATOM   7035 C CG2   . ILE B 1 385 ? -27.022 57.815  1.097   1.00 43.56  ? 385  ILE B CG2   1 
ATOM   7036 C CD1   . ILE B 1 385 ? -27.870 54.778  0.667   1.00 49.84  ? 385  ILE B CD1   1 
ATOM   7037 N N     . PRO B 1 386 ? -28.135 56.567  5.329   1.00 55.41  ? 386  PRO B N     1 
ATOM   7038 C CA    . PRO B 1 386 ? -28.711 55.641  6.308   1.00 51.50  ? 386  PRO B CA    1 
ATOM   7039 C C     . PRO B 1 386 ? -28.896 54.210  5.786   1.00 46.73  ? 386  PRO B C     1 
ATOM   7040 O O     . PRO B 1 386 ? -29.429 54.035  4.694   1.00 47.58  ? 386  PRO B O     1 
ATOM   7041 C CB    . PRO B 1 386 ? -30.101 56.224  6.646   1.00 50.72  ? 386  PRO B CB    1 
ATOM   7042 C CG    . PRO B 1 386 ? -30.283 57.383  5.672   1.00 56.01  ? 386  PRO B CG    1 
ATOM   7043 C CD    . PRO B 1 386 ? -28.889 57.833  5.271   1.00 51.35  ? 386  PRO B CD    1 
ATOM   7044 N N     . GLY B 1 387 ? -28.458 53.243  6.596   1.00 43.84  ? 387  GLY B N     1 
ATOM   7045 C CA    . GLY B 1 387 ? -28.598 51.792  6.381   1.00 43.66  ? 387  GLY B CA    1 
ATOM   7046 C C     . GLY B 1 387 ? -27.789 51.318  5.187   1.00 41.13  ? 387  GLY B C     1 
ATOM   7047 O O     . GLY B 1 387 ? -28.150 50.269  4.640   1.00 45.75  ? 387  GLY B O     1 
ATOM   7048 N N     . ALA B 1 388 ? -26.756 52.073  4.791   1.00 40.78  ? 388  ALA B N     1 
ATOM   7049 C CA    . ALA B 1 388 ? -25.923 51.809  3.595   1.00 42.47  ? 388  ALA B CA    1 
ATOM   7050 C C     . ALA B 1 388 ? -25.317 50.403  3.692   1.00 42.23  ? 388  ALA B C     1 
ATOM   7051 O O     . ALA B 1 388 ? -24.772 50.019  4.762   1.00 40.05  ? 388  ALA B O     1 
ATOM   7052 C CB    . ALA B 1 388 ? -24.856 52.855  3.416   1.00 42.69  ? 388  ALA B CB    1 
ATOM   7053 N N     . GLY B 1 389 ? -25.521 49.634  2.630   1.00 43.62  ? 389  GLY B N     1 
ATOM   7054 C CA    . GLY B 1 389 ? -24.778 48.406  2.317   1.00 48.11  ? 389  GLY B CA    1 
ATOM   7055 C C     . GLY B 1 389 ? -24.200 48.549  0.930   1.00 48.51  ? 389  GLY B C     1 
ATOM   7056 O O     . GLY B 1 389 ? -24.562 49.533  0.251   1.00 48.56  ? 389  GLY B O     1 
ATOM   7057 N N     . HIS B 1 390 ? -23.311 47.645  0.526   1.00 49.00  ? 390  HIS B N     1 
ATOM   7058 C CA    . HIS B 1 390 ? -22.771 47.643  -0.852  1.00 46.12  ? 390  HIS B CA    1 
ATOM   7059 C C     . HIS B 1 390 ? -22.736 46.218  -1.391  1.00 42.45  ? 390  HIS B C     1 
ATOM   7060 O O     . HIS B 1 390 ? -22.746 45.265  -0.599  1.00 39.67  ? 390  HIS B O     1 
ATOM   7061 C CB    . HIS B 1 390 ? -21.417 48.351  -0.910  1.00 50.90  ? 390  HIS B CB    1 
ATOM   7062 C CG    . HIS B 1 390 ? -20.325 47.564  -0.280  1.00 52.37  ? 390  HIS B CG    1 
ATOM   7063 N ND1   . HIS B 1 390 ? -19.830 46.415  -0.856  1.00 48.88  ? 390  HIS B ND1   1 
ATOM   7064 C CD2   . HIS B 1 390 ? -19.651 47.740  0.872   1.00 49.81  ? 390  HIS B CD2   1 
ATOM   7065 C CE1   . HIS B 1 390 ? -18.896 45.913  -0.084  1.00 48.84  ? 390  HIS B CE1   1 
ATOM   7066 N NE2   . HIS B 1 390 ? -18.762 46.711  0.970   1.00 48.66  ? 390  HIS B NE2   1 
ATOM   7067 N N     . VAL B 1 391 ? -22.767 46.116  -2.716  1.00 42.23  ? 391  VAL B N     1 
ATOM   7068 C CA    . VAL B 1 391 ? -22.506 44.870  -3.479  1.00 40.07  ? 391  VAL B CA    1 
ATOM   7069 C C     . VAL B 1 391 ? -21.312 45.158  -4.389  1.00 40.43  ? 391  VAL B C     1 
ATOM   7070 O O     . VAL B 1 391 ? -21.211 46.280  -4.924  1.00 42.04  ? 391  VAL B O     1 
ATOM   7071 C CB    . VAL B 1 391 ? -23.740 44.380  -4.256  1.00 42.72  ? 391  VAL B CB    1 
ATOM   7072 C CG1   . VAL B 1 391 ? -24.251 45.401  -5.269  1.00 42.38  ? 391  VAL B CG1   1 
ATOM   7073 C CG2   . VAL B 1 391 ? -23.458 43.052  -4.938  1.00 42.33  ? 391  VAL B CG2   1 
ATOM   7074 N N     . GLY B 1 392 ? -20.402 44.195  -4.494  1.00 43.80  ? 392  GLY B N     1 
ATOM   7075 C CA    . GLY B 1 392 ? -19.216 44.324  -5.347  1.00 42.54  ? 392  GLY B CA    1 
ATOM   7076 C C     . GLY B 1 392 ? -19.615 44.131  -6.790  1.00 38.30  ? 392  GLY B C     1 
ATOM   7077 O O     . GLY B 1 392 ? -20.355 43.178  -7.072  1.00 40.20  ? 392  GLY B O     1 
ATOM   7078 N N     . PHE B 1 393 ? -19.159 45.026  -7.651  1.00 35.45  ? 393  PHE B N     1 
ATOM   7079 C CA    . PHE B 1 393 ? -19.101 44.814  -9.114  1.00 36.14  ? 393  PHE B CA    1 
ATOM   7080 C C     . PHE B 1 393 ? -17.655 45.103  -9.524  1.00 33.95  ? 393  PHE B C     1 
ATOM   7081 O O     . PHE B 1 393 ? -17.205 46.177  -9.184  1.00 29.89  ? 393  PHE B O     1 
ATOM   7082 C CB    . PHE B 1 393 ? -20.143 45.676  -9.826  1.00 34.34  ? 393  PHE B CB    1 
ATOM   7083 C CG    . PHE B 1 393 ? -20.093 45.526  -11.322 1.00 32.27  ? 393  PHE B CG    1 
ATOM   7084 C CD1   . PHE B 1 393 ? -20.341 44.299  -11.905 1.00 34.82  ? 393  PHE B CD1   1 
ATOM   7085 C CD2   . PHE B 1 393 ? -19.720 46.573  -12.131 1.00 31.25  ? 393  PHE B CD2   1 
ATOM   7086 C CE1   . PHE B 1 393 ? -20.262 44.136  -13.278 1.00 35.86  ? 393  PHE B CE1   1 
ATOM   7087 C CE2   . PHE B 1 393 ? -19.656 46.414  -13.506 1.00 32.46  ? 393  PHE B CE2   1 
ATOM   7088 C CZ    . PHE B 1 393 ? -19.927 45.196  -14.077 1.00 33.34  ? 393  PHE B CZ    1 
ATOM   7089 N N     . SER B 1 394 ? -16.947 44.157  -10.162 1.00 32.40  ? 394  SER B N     1 
ATOM   7090 C CA    . SER B 1 394 ? -15.471 44.254  -10.340 1.00 34.03  ? 394  SER B CA    1 
ATOM   7091 C C     . SER B 1 394 ? -15.010 43.490  -11.581 1.00 35.56  ? 394  SER B C     1 
ATOM   7092 O O     . SER B 1 394 ? -14.123 42.652  -11.508 1.00 36.78  ? 394  SER B O     1 
ATOM   7093 C CB    . SER B 1 394 ? -14.736 43.787  -9.095  1.00 30.96  ? 394  SER B CB    1 
ATOM   7094 O OG    . SER B 1 394 ? -15.198 42.491  -8.720  1.00 30.36  ? 394  SER B OG    1 
ATOM   7095 N N     . PRO B 1 395 ? -15.517 43.812  -12.785 1.00 33.95  ? 395  PRO B N     1 
ATOM   7096 C CA    . PRO B 1 395 ? -15.065 43.113  -13.980 1.00 31.61  ? 395  PRO B CA    1 
ATOM   7097 C C     . PRO B 1 395 ? -13.620 43.473  -14.355 1.00 29.64  ? 395  PRO B C     1 
ATOM   7098 O O     . PRO B 1 395 ? -13.082 44.502  -13.948 1.00 26.08  ? 395  PRO B O     1 
ATOM   7099 C CB    . PRO B 1 395 ? -16.083 43.561  -15.040 1.00 33.15  ? 395  PRO B CB    1 
ATOM   7100 C CG    . PRO B 1 395 ? -16.443 44.963  -14.587 1.00 34.66  ? 395  PRO B CG    1 
ATOM   7101 C CD    . PRO B 1 395 ? -16.502 44.874  -13.075 1.00 35.14  ? 395  PRO B CD    1 
ATOM   7102 N N     . ILE B 1 396 ? -13.034 42.567  -15.125 1.00 31.12  ? 396  ILE B N     1 
ATOM   7103 C CA    . ILE B 1 396 ? -11.631 42.598  -15.606 1.00 32.28  ? 396  ILE B CA    1 
ATOM   7104 C C     . ILE B 1 396 ? -11.668 43.107  -17.053 1.00 31.03  ? 396  ILE B C     1 
ATOM   7105 O O     . ILE B 1 396 ? -12.535 42.644  -17.819 1.00 30.47  ? 396  ILE B O     1 
ATOM   7106 C CB    . ILE B 1 396 ? -11.025 41.191  -15.495 1.00 31.39  ? 396  ILE B CB    1 
ATOM   7107 C CG1   . ILE B 1 396 ? -11.035 40.658  -14.057 1.00 34.41  ? 396  ILE B CG1   1 
ATOM   7108 C CG2   . ILE B 1 396 ? -9.629  41.156  -16.086 1.00 34.88  ? 396  ILE B CG2   1 
ATOM   7109 C CD1   . ILE B 1 396 ? -10.220 41.450  -13.091 1.00 37.76  ? 396  ILE B CD1   1 
ATOM   7110 N N     . SER B 1 397 ? -10.764 44.009  -17.408 1.00 29.36  ? 397  SER B N     1 
ATOM   7111 C CA    . SER B 1 397 ? -10.676 44.627  -18.761 1.00 28.95  ? 397  SER B CA    1 
ATOM   7112 C C     . SER B 1 397 ? -9.200  44.813  -19.069 1.00 30.28  ? 397  SER B C     1 
ATOM   7113 O O     . SER B 1 397 ? -8.385  44.718  -18.143 1.00 28.25  ? 397  SER B O     1 
ATOM   7114 C CB    . SER B 1 397 ? -11.392 45.944  -18.788 1.00 26.99  ? 397  SER B CB    1 
ATOM   7115 O OG    . SER B 1 397 ? -10.882 46.793  -17.770 1.00 28.43  ? 397  SER B OG    1 
ATOM   7116 N N     . PRO B 1 398 ? -8.821  45.130  -20.328 1.00 32.53  ? 398  PRO B N     1 
ATOM   7117 C CA    . PRO B 1 398 ? -7.455  45.543  -20.636 1.00 32.39  ? 398  PRO B CA    1 
ATOM   7118 C C     . PRO B 1 398 ? -7.195  46.915  -20.022 1.00 32.02  ? 398  PRO B C     1 
ATOM   7119 O O     . PRO B 1 398 ? -8.098  47.747  -19.941 1.00 33.00  ? 398  PRO B O     1 
ATOM   7120 C CB    . PRO B 1 398 ? -7.396  45.584  -22.168 1.00 34.40  ? 398  PRO B CB    1 
ATOM   7121 C CG    . PRO B 1 398 ? -8.614  44.763  -22.592 1.00 34.16  ? 398  PRO B CG    1 
ATOM   7122 C CD    . PRO B 1 398 ? -9.657  45.082  -21.540 1.00 33.80  ? 398  PRO B CD    1 
ATOM   7123 N N     . PRO B 1 399 ? -5.967  47.170  -19.543 1.00 29.71  ? 399  PRO B N     1 
ATOM   7124 C CA    . PRO B 1 399 ? -5.636  48.446  -18.918 1.00 32.19  ? 399  PRO B CA    1 
ATOM   7125 C C     . PRO B 1 399 ? -5.330  49.455  -20.031 1.00 33.77  ? 399  PRO B C     1 
ATOM   7126 O O     . PRO B 1 399 ? -4.178  49.874  -20.205 1.00 32.43  ? 399  PRO B O     1 
ATOM   7127 C CB    . PRO B 1 399 ? -4.456  48.075  -18.000 1.00 33.77  ? 399  PRO B CB    1 
ATOM   7128 C CG    . PRO B 1 399 ? -3.794  46.872  -18.658 1.00 31.19  ? 399  PRO B CG    1 
ATOM   7129 C CD    . PRO B 1 399 ? -4.838  46.220  -19.547 1.00 31.79  ? 399  PRO B CD    1 
ATOM   7130 N N     . VAL B 1 400 ? -6.383  49.804  -20.770 1.00 30.70  ? 400  VAL B N     1 
ATOM   7131 C CA    . VAL B 1 400 ? -6.327  50.663  -21.983 1.00 31.43  ? 400  VAL B CA    1 
ATOM   7132 C C     . VAL B 1 400 ? -7.368  51.768  -21.749 1.00 30.76  ? 400  VAL B C     1 
ATOM   7133 O O     . VAL B 1 400 ? -8.443  51.445  -21.233 1.00 29.01  ? 400  VAL B O     1 
ATOM   7134 C CB    . VAL B 1 400 ? -6.579  49.824  -23.258 1.00 34.28  ? 400  VAL B CB    1 
ATOM   7135 C CG1   . VAL B 1 400 ? -6.539  50.666  -24.532 1.00 35.38  ? 400  VAL B CG1   1 
ATOM   7136 C CG2   . VAL B 1 400 ? -5.602  48.651  -23.385 1.00 33.91  ? 400  VAL B CG2   1 
ATOM   7137 N N     . GLY B 1 401 ? -6.992  53.032  -21.964 1.00 33.62  ? 401  GLY B N     1 
ATOM   7138 C CA    . GLY B 1 401 ? -7.833  54.211  -21.697 1.00 31.52  ? 401  GLY B CA    1 
ATOM   7139 C C     . GLY B 1 401 ? -9.216  54.073  -22.312 1.00 34.30  ? 401  GLY B C     1 
ATOM   7140 O O     . GLY B 1 401 ? -10.214 54.397  -21.625 1.00 36.20  ? 401  GLY B O     1 
ATOM   7141 N N     . ARG B 1 402 ? -9.269  53.665  -23.583 1.00 34.99  ? 402  ARG B N     1 
ATOM   7142 C CA    . ARG B 1 402 ? -10.513 53.398  -24.342 1.00 38.08  ? 402  ARG B CA    1 
ATOM   7143 C C     . ARG B 1 402 ? -11.425 52.463  -23.540 1.00 34.46  ? 402  ARG B C     1 
ATOM   7144 O O     . ARG B 1 402 ? -12.618 52.750  -23.435 1.00 30.24  ? 402  ARG B O     1 
ATOM   7145 C CB    . ARG B 1 402 ? -10.189 52.789  -25.709 1.00 43.61  ? 402  ARG B CB    1 
ATOM   7146 C CG    . ARG B 1 402 ? -11.375 52.761  -26.660 1.00 50.99  ? 402  ARG B CG    1 
ATOM   7147 C CD    . ARG B 1 402 ? -10.961 52.322  -28.058 1.00 56.37  ? 402  ARG B CD    1 
ATOM   7148 N NE    . ARG B 1 402 ? -10.182 53.343  -28.749 1.00 61.03  ? 402  ARG B NE    1 
ATOM   7149 C CZ    . ARG B 1 402 ? -10.671 54.468  -29.274 1.00 67.05  ? 402  ARG B CZ    1 
ATOM   7150 N NH1   . ARG B 1 402 ? -11.964 54.755  -29.198 1.00 70.42  ? 402  ARG B NH1   1 
ATOM   7151 N NH2   . ARG B 1 402 ? -9.851  55.314  -29.875 1.00 70.69  ? 402  ARG B NH2   1 
ATOM   7152 N N     . ASP B 1 403 ? -10.878 51.388  -22.982 1.00 34.52  ? 403  ASP B N     1 
ATOM   7153 C CA    . ASP B 1 403 ? -11.663 50.388  -22.210 1.00 34.10  ? 403  ASP B CA    1 
ATOM   7154 C C     . ASP B 1 403 ? -12.136 51.003  -20.886 1.00 31.82  ? 403  ASP B C     1 
ATOM   7155 O O     . ASP B 1 403 ? -13.271 50.734  -20.462 1.00 33.29  ? 403  ASP B O     1 
ATOM   7156 C CB    . ASP B 1 403 ? -10.854 49.101  -22.021 1.00 35.55  ? 403  ASP B CB    1 
ATOM   7157 C CG    . ASP B 1 403 ? -10.673 48.356  -23.334 1.00 35.02  ? 403  ASP B CG    1 
ATOM   7158 O OD1   . ASP B 1 403 ? -11.624 47.688  -23.755 1.00 35.32  ? 403  ASP B OD1   1 
ATOM   7159 O OD2   . ASP B 1 403 ? -9.618  48.519  -23.951 1.00 39.66  ? 403  ASP B OD2   1 
ATOM   7160 N N     . ALA B 1 404 ? -11.294 51.783  -20.226 1.00 29.71  ? 404  ALA B N     1 
ATOM   7161 C CA    . ALA B 1 404 ? -11.656 52.452  -18.957 1.00 31.74  ? 404  ALA B CA    1 
ATOM   7162 C C     . ALA B 1 404 ? -12.844 53.393  -19.219 1.00 31.33  ? 404  ALA B C     1 
ATOM   7163 O O     . ALA B 1 404 ? -13.817 53.306  -18.470 1.00 32.17  ? 404  ALA B O     1 
ATOM   7164 C CB    . ALA B 1 404 ? -10.455 53.163  -18.391 1.00 29.06  ? 404  ALA B CB    1 
ATOM   7165 N N     . MET B 1 405 ? -12.778 54.221  -20.272 1.00 34.46  ? 405  MET B N     1 
ATOM   7166 C CA    . MET B 1 405 ? -13.822 55.235  -20.599 1.00 34.73  ? 405  MET B CA    1 
ATOM   7167 C C     . MET B 1 405 ? -15.155 54.543  -20.915 1.00 36.55  ? 405  MET B C     1 
ATOM   7168 O O     . MET B 1 405 ? -16.193 55.021  -20.428 1.00 33.38  ? 405  MET B O     1 
ATOM   7169 C CB    . MET B 1 405 ? -13.424 56.102  -21.794 1.00 33.68  ? 405  MET B CB    1 
ATOM   7170 C CG    . MET B 1 405 ? -12.331 57.111  -21.479 1.00 38.39  ? 405  MET B CG    1 
ATOM   7171 S SD    . MET B 1 405 ? -12.719 58.322  -20.169 1.00 45.54  ? 405  MET B SD    1 
ATOM   7172 C CE    . MET B 1 405 ? -14.407 58.758  -20.591 1.00 46.09  ? 405  MET B CE    1 
ATOM   7173 N N     . LYS B 1 406 ? -15.117 53.472  -21.716 1.00 38.13  ? 406  LYS B N     1 
ATOM   7174 C CA    . LYS B 1 406 ? -16.308 52.662  -22.056 1.00 36.76  ? 406  LYS B CA    1 
ATOM   7175 C C     . LYS B 1 406 ? -16.908 52.129  -20.756 1.00 33.87  ? 406  LYS B C     1 
ATOM   7176 O O     . LYS B 1 406 ? -18.119 52.259  -20.555 1.00 30.25  ? 406  LYS B O     1 
ATOM   7177 C CB    . LYS B 1 406 ? -15.972 51.523  -23.018 1.00 38.64  ? 406  LYS B CB    1 
ATOM   7178 C CG    . LYS B 1 406 ? -17.206 50.754  -23.466 1.00 43.35  ? 406  LYS B CG    1 
ATOM   7179 C CD    . LYS B 1 406 ? -16.996 49.842  -24.634 1.00 50.60  ? 406  LYS B CD    1 
ATOM   7180 C CE    . LYS B 1 406 ? -15.895 48.836  -24.390 1.00 54.50  ? 406  LYS B CE    1 
ATOM   7181 N NZ    . LYS B 1 406 ? -15.735 47.895  -25.524 1.00 58.91  ? 406  LYS B NZ    1 
ATOM   7182 N N     . GLN B 1 407 ? -16.079 51.594  -19.868 1.00 33.41  ? 407  GLN B N     1 
ATOM   7183 C CA    . GLN B 1 407 ? -16.593 51.002  -18.613 1.00 35.37  ? 407  GLN B CA    1 
ATOM   7184 C C     . GLN B 1 407 ? -17.161 52.101  -17.707 1.00 32.14  ? 407  GLN B C     1 
ATOM   7185 O O     . GLN B 1 407 ? -18.242 51.911  -17.185 1.00 36.35  ? 407  GLN B O     1 
ATOM   7186 C CB    . GLN B 1 407 ? -15.496 50.163  -17.975 1.00 38.62  ? 407  GLN B CB    1 
ATOM   7187 C CG    . GLN B 1 407 ? -15.252 48.873  -18.736 1.00 36.10  ? 407  GLN B CG    1 
ATOM   7188 C CD    . GLN B 1 407 ? -14.115 48.115  -18.115 1.00 38.45  ? 407  GLN B CD    1 
ATOM   7189 O OE1   . GLN B 1 407 ? -14.312 47.259  -17.244 1.00 34.96  ? 407  GLN B OE1   1 
ATOM   7190 N NE2   . GLN B 1 407 ? -12.916 48.460  -18.559 1.00 36.42  ? 407  GLN B NE2   1 
ATOM   7191 N N     . PHE B 1 408 ? -16.450 53.203  -17.542 1.00 30.58  ? 408  PHE B N     1 
ATOM   7192 C CA    . PHE B 1 408 ? -16.898 54.384  -16.764 1.00 33.09  ? 408  PHE B CA    1 
ATOM   7193 C C     . PHE B 1 408 ? -18.295 54.802  -17.242 1.00 32.49  ? 408  PHE B C     1 
ATOM   7194 O O     . PHE B 1 408 ? -19.227 54.871  -16.439 1.00 34.23  ? 408  PHE B O     1 
ATOM   7195 C CB    . PHE B 1 408 ? -15.892 55.522  -16.944 1.00 31.79  ? 408  PHE B CB    1 
ATOM   7196 C CG    . PHE B 1 408 ? -16.333 56.848  -16.390 1.00 31.12  ? 408  PHE B CG    1 
ATOM   7197 C CD1   . PHE B 1 408 ? -16.831 56.945  -15.105 1.00 31.41  ? 408  PHE B CD1   1 
ATOM   7198 C CD2   . PHE B 1 408 ? -16.267 57.997  -17.162 1.00 38.63  ? 408  PHE B CD2   1 
ATOM   7199 C CE1   . PHE B 1 408 ? -17.211 58.170  -14.576 1.00 31.23  ? 408  PHE B CE1   1 
ATOM   7200 C CE2   . PHE B 1 408 ? -16.681 59.220  -16.647 1.00 37.02  ? 408  PHE B CE2   1 
ATOM   7201 C CZ    . PHE B 1 408 ? -17.159 59.296  -15.357 1.00 33.19  ? 408  PHE B CZ    1 
ATOM   7202 N N     . ARG B 1 409 ? -18.424 55.058  -18.538 1.00 35.53  ? 409  ARG B N     1 
ATOM   7203 C CA    . ARG B 1 409 ? -19.694 55.534  -19.149 1.00 40.01  ? 409  ARG B CA    1 
ATOM   7204 C C     . ARG B 1 409 ? -20.767 54.486  -18.887 1.00 37.64  ? 409  ARG B C     1 
ATOM   7205 O O     . ARG B 1 409 ? -21.779 54.836  -18.274 1.00 42.31  ? 409  ARG B O     1 
ATOM   7206 C CB    . ARG B 1 409 ? -19.557 55.782  -20.653 1.00 42.37  ? 409  ARG B CB    1 
ATOM   7207 C CG    . ARG B 1 409 ? -18.373 56.662  -21.023 1.00 52.91  ? 409  ARG B CG    1 
ATOM   7208 C CD    . ARG B 1 409 ? -18.731 57.998  -21.615 1.00 60.17  ? 409  ARG B CD    1 
ATOM   7209 N NE    . ARG B 1 409 ? -17.791 58.368  -22.668 1.00 60.89  ? 409  ARG B NE    1 
ATOM   7210 C CZ    . ARG B 1 409 ? -17.030 59.461  -22.682 1.00 61.29  ? 409  ARG B CZ    1 
ATOM   7211 N NH1   . ARG B 1 409 ? -16.232 59.682  -23.715 1.00 62.97  ? 409  ARG B NH1   1 
ATOM   7212 N NH2   . ARG B 1 409 ? -17.066 60.328  -21.682 1.00 60.15  ? 409  ARG B NH2   1 
ATOM   7213 N N     . MET B 1 410 ? -20.561 53.240  -19.316 1.00 36.69  ? 410  MET B N     1 
ATOM   7214 C CA    . MET B 1 410 ? -21.673 52.261  -19.349 1.00 37.39  ? 410  MET B CA    1 
ATOM   7215 C C     . MET B 1 410 ? -22.120 51.941  -17.912 1.00 35.34  ? 410  MET B C     1 
ATOM   7216 O O     . MET B 1 410 ? -23.319 51.736  -17.715 1.00 36.27  ? 410  MET B O     1 
ATOM   7217 C CB    . MET B 1 410 ? -21.349 51.008  -20.182 1.00 40.56  ? 410  MET B CB    1 
ATOM   7218 C CG    . MET B 1 410 ? -20.294 50.069  -19.644 1.00 38.61  ? 410  MET B CG    1 
ATOM   7219 S SD    . MET B 1 410 ? -19.646 48.940  -20.955 1.00 45.46  ? 410  MET B SD    1 
ATOM   7220 C CE    . MET B 1 410 ? -21.078 47.888  -21.154 1.00 47.00  ? 410  MET B CE    1 
ATOM   7221 N N     . VAL B 1 411 ? -21.223 51.967  -16.923 1.00 33.79  ? 411  VAL B N     1 
ATOM   7222 C CA    . VAL B 1 411 ? -21.579 51.621  -15.515 1.00 35.44  ? 411  VAL B CA    1 
ATOM   7223 C C     . VAL B 1 411 ? -22.349 52.793  -14.880 1.00 36.72  ? 411  VAL B C     1 
ATOM   7224 O O     . VAL B 1 411 ? -23.367 52.548  -14.160 1.00 35.28  ? 411  VAL B O     1 
ATOM   7225 C CB    . VAL B 1 411 ? -20.327 51.232  -14.701 1.00 35.07  ? 411  VAL B CB    1 
ATOM   7226 C CG1   . VAL B 1 411 ? -20.607 51.201  -13.217 1.00 35.50  ? 411  VAL B CG1   1 
ATOM   7227 C CG2   . VAL B 1 411 ? -19.747 49.897  -15.164 1.00 36.99  ? 411  VAL B CG2   1 
ATOM   7228 N N     . ARG B 1 412 ? -21.883 54.023  -15.089 1.00 36.25  ? 412  ARG B N     1 
ATOM   7229 C CA    . ARG B 1 412 ? -22.502 55.178  -14.400 1.00 40.57  ? 412  ARG B CA    1 
ATOM   7230 C C     . ARG B 1 412 ? -23.839 55.516  -15.085 1.00 38.96  ? 412  ARG B C     1 
ATOM   7231 O O     . ARG B 1 412 ? -24.775 55.835  -14.341 1.00 36.57  ? 412  ARG B O     1 
ATOM   7232 C CB    . ARG B 1 412 ? -21.499 56.315  -14.276 1.00 41.17  ? 412  ARG B CB    1 
ATOM   7233 C CG    . ARG B 1 412 ? -21.940 57.574  -14.981 1.00 46.57  ? 412  ARG B CG    1 
ATOM   7234 C CD    . ARG B 1 412 ? -21.340 58.840  -14.422 1.00 43.39  ? 412  ARG B CD    1 
ATOM   7235 N NE    . ARG B 1 412 ? -21.068 59.660  -15.589 1.00 39.15  ? 412  ARG B NE    1 
ATOM   7236 C CZ    . ARG B 1 412 ? -20.359 60.771  -15.585 1.00 40.54  ? 412  ARG B CZ    1 
ATOM   7237 N NH1   . ARG B 1 412 ? -20.137 61.389  -16.730 1.00 44.77  ? 412  ARG B NH1   1 
ATOM   7238 N NH2   . ARG B 1 412 ? -19.873 61.258  -14.457 1.00 38.07  ? 412  ARG B NH2   1 
ATOM   7239 N N     . SER B 1 413 ? -23.969 55.334  -16.409 1.00 38.34  ? 413  SER B N     1 
ATOM   7240 C CA    . SER B 1 413 ? -25.256 55.537  -17.134 1.00 40.82  ? 413  SER B CA    1 
ATOM   7241 C C     . SER B 1 413 ? -26.312 54.612  -16.531 1.00 41.09  ? 413  SER B C     1 
ATOM   7242 O O     . SER B 1 413 ? -27.385 55.131  -16.117 1.00 37.68  ? 413  SER B O     1 
ATOM   7243 C CB    . SER B 1 413 ? -25.149 55.391  -18.639 1.00 39.60  ? 413  SER B CB    1 
ATOM   7244 O OG    . SER B 1 413 ? -24.649 54.112  -19.011 1.00 45.64  ? 413  SER B OG    1 
ATOM   7245 N N     . ARG B 1 414 ? -26.002 53.321  -16.361 1.00 40.45  ? 414  ARG B N     1 
ATOM   7246 C CA    . ARG B 1 414 ? -26.975 52.365  -15.767 1.00 37.48  ? 414  ARG B CA    1 
ATOM   7247 C C     . ARG B 1 414 ? -27.177 52.671  -14.279 1.00 38.47  ? 414  ARG B C     1 
ATOM   7248 O O     . ARG B 1 414 ? -28.281 52.412  -13.790 1.00 36.96  ? 414  ARG B O     1 
ATOM   7249 C CB    . ARG B 1 414 ? -26.547 50.907  -15.952 1.00 38.58  ? 414  ARG B CB    1 
ATOM   7250 C CG    . ARG B 1 414 ? -26.431 50.479  -17.406 1.00 39.68  ? 414  ARG B CG    1 
ATOM   7251 C CD    . ARG B 1 414 ? -27.764 50.607  -18.128 1.00 37.69  ? 414  ARG B CD    1 
ATOM   7252 N NE    . ARG B 1 414 ? -27.717 50.000  -19.450 1.00 40.96  ? 414  ARG B NE    1 
ATOM   7253 C CZ    . ARG B 1 414 ? -28.688 50.112  -20.358 1.00 45.06  ? 414  ARG B CZ    1 
ATOM   7254 N NH1   . ARG B 1 414 ? -29.783 50.805  -20.077 1.00 45.93  ? 414  ARG B NH1   1 
ATOM   7255 N NH2   . ARG B 1 414 ? -28.569 49.545  -21.544 1.00 40.29  ? 414  ARG B NH2   1 
ATOM   7256 N N     . ALA B 1 415 ? -26.161 53.189  -13.580 1.00 41.05  ? 415  ALA B N     1 
ATOM   7257 C CA    . ALA B 1 415 ? -26.232 53.468  -12.126 1.00 40.84  ? 415  ALA B CA    1 
ATOM   7258 C C     . ALA B 1 415 ? -27.252 54.590  -11.895 1.00 40.88  ? 415  ALA B C     1 
ATOM   7259 O O     . ALA B 1 415 ? -28.136 54.443  -11.018 1.00 42.98  ? 415  ALA B O     1 
ATOM   7260 C CB    . ALA B 1 415 ? -24.873 53.841  -11.589 1.00 45.26  ? 415  ALA B CB    1 
ATOM   7261 N N     . ASP B 1 416 ? -27.116 55.661  -12.670 1.00 37.18  ? 416  ASP B N     1 
ATOM   7262 C CA    . ASP B 1 416 ? -28.084 56.790  -12.737 1.00 41.28  ? 416  ASP B CA    1 
ATOM   7263 C C     . ASP B 1 416 ? -29.506 56.235  -12.926 1.00 41.97  ? 416  ASP B C     1 
ATOM   7264 O O     . ASP B 1 416 ? -30.374 56.492  -12.037 1.00 40.73  ? 416  ASP B O     1 
ATOM   7265 C CB    . ASP B 1 416 ? -27.695 57.769  -13.846 1.00 38.47  ? 416  ASP B CB    1 
ATOM   7266 C CG    . ASP B 1 416 ? -26.449 58.562  -13.529 1.00 40.15  ? 416  ASP B CG    1 
ATOM   7267 O OD1   . ASP B 1 416 ? -26.151 58.704  -12.335 1.00 46.87  ? 416  ASP B OD1   1 
ATOM   7268 O OD2   . ASP B 1 416 ? -25.783 59.028  -14.477 1.00 43.29  ? 416  ASP B OD2   1 
ATOM   7269 N N     . GLU B 1 417 ? -29.726 55.458  -13.992 1.00 45.16  ? 417  GLU B N     1 
ATOM   7270 C CA    . GLU B 1 417 ? -31.064 54.910  -14.353 1.00 47.15  ? 417  GLU B CA    1 
ATOM   7271 C C     . GLU B 1 417 ? -31.656 54.185  -13.152 1.00 46.21  ? 417  GLU B C     1 
ATOM   7272 O O     . GLU B 1 417 ? -32.848 54.302  -12.952 1.00 51.93  ? 417  GLU B O     1 
ATOM   7273 C CB    . GLU B 1 417 ? -31.002 53.939  -15.528 1.00 49.98  ? 417  GLU B CB    1 
ATOM   7274 C CG    . GLU B 1 417 ? -30.796 54.629  -16.853 1.00 49.97  ? 417  GLU B CG    1 
ATOM   7275 C CD    . GLU B 1 417 ? -30.588 53.691  -18.026 1.00 52.04  ? 417  GLU B CD    1 
ATOM   7276 O OE1   . GLU B 1 417 ? -30.162 54.193  -19.086 1.00 50.98  ? 417  GLU B OE1   1 
ATOM   7277 O OE2   . GLU B 1 417 ? -30.855 52.469  -17.878 1.00 47.10  ? 417  GLU B OE2   1 
ATOM   7278 N N     . TYR B 1 418 ? -30.840 53.461  -12.392 1.00 45.26  ? 418  TYR B N     1 
ATOM   7279 C CA    . TYR B 1 418 ? -31.302 52.628  -11.253 1.00 43.26  ? 418  TYR B CA    1 
ATOM   7280 C C     . TYR B 1 418 ? -31.145 53.392  -9.931  1.00 39.96  ? 418  TYR B C     1 
ATOM   7281 O O     . TYR B 1 418 ? -31.267 52.755  -8.881  1.00 44.12  ? 418  TYR B O     1 
ATOM   7282 C CB    . TYR B 1 418 ? -30.582 51.278  -11.289 1.00 41.07  ? 418  TYR B CB    1 
ATOM   7283 C CG    . TYR B 1 418 ? -31.106 50.361  -12.365 1.00 41.60  ? 418  TYR B CG    1 
ATOM   7284 C CD1   . TYR B 1 418 ? -30.832 50.584  -13.703 1.00 43.20  ? 418  TYR B CD1   1 
ATOM   7285 C CD2   . TYR B 1 418 ? -31.905 49.273  -12.043 1.00 42.75  ? 418  TYR B CD2   1 
ATOM   7286 C CE1   . TYR B 1 418 ? -31.321 49.740  -14.692 1.00 44.04  ? 418  TYR B CE1   1 
ATOM   7287 C CE2   . TYR B 1 418 ? -32.417 48.435  -13.016 1.00 42.78  ? 418  TYR B CE2   1 
ATOM   7288 C CZ    . TYR B 1 418 ? -32.126 48.670  -14.345 1.00 40.75  ? 418  TYR B CZ    1 
ATOM   7289 O OH    . TYR B 1 418 ? -32.634 47.831  -15.287 1.00 44.12  ? 418  TYR B OH    1 
ATOM   7290 N N     . ALA B 1 419 ? -30.925 54.709  -9.983  1.00 40.26  ? 419  ALA B N     1 
ATOM   7291 C CA    . ALA B 1 419 ? -30.877 55.611  -8.806  1.00 43.83  ? 419  ALA B CA    1 
ATOM   7292 C C     . ALA B 1 419 ? -29.810 55.151  -7.802  1.00 47.70  ? 419  ALA B C     1 
ATOM   7293 O O     . ALA B 1 419 ? -30.106 55.148  -6.597  1.00 51.32  ? 419  ALA B O     1 
ATOM   7294 C CB    . ALA B 1 419 ? -32.240 55.653  -8.153  1.00 43.38  ? 419  ALA B CB    1 
ATOM   7295 N N     . LYS B 1 420 ? -28.608 54.792  -8.270  1.00 44.60  ? 420  LYS B N     1 
ATOM   7296 C CA    . LYS B 1 420 ? -27.472 54.373  -7.400  1.00 42.01  ? 420  LYS B CA    1 
ATOM   7297 C C     . LYS B 1 420 ? -26.266 55.241  -7.750  1.00 39.63  ? 420  LYS B C     1 
ATOM   7298 O O     . LYS B 1 420 ? -26.020 55.434  -8.965  1.00 39.92  ? 420  LYS B O     1 
ATOM   7299 C CB    . LYS B 1 420 ? -27.175 52.875  -7.580  1.00 40.16  ? 420  LYS B CB    1 
ATOM   7300 C CG    . LYS B 1 420 ? -28.353 51.944  -7.310  1.00 39.65  ? 420  LYS B CG    1 
ATOM   7301 C CD    . LYS B 1 420 ? -28.754 51.908  -5.848  1.00 39.35  ? 420  LYS B CD    1 
ATOM   7302 C CE    . LYS B 1 420 ? -30.173 51.433  -5.624  1.00 40.58  ? 420  LYS B CE    1 
ATOM   7303 N NZ    . LYS B 1 420 ? -31.144 52.461  -6.075  1.00 46.26  ? 420  LYS B NZ    1 
ATOM   7304 N N     . ASP B 1 421 ? -25.547 55.737  -6.740  1.00 39.25  ? 421  ASP B N     1 
ATOM   7305 C CA    . ASP B 1 421 ? -24.343 56.592  -6.951  1.00 40.81  ? 421  ASP B CA    1 
ATOM   7306 C C     . ASP B 1 421 ? -23.270 55.795  -7.713  1.00 39.46  ? 421  ASP B C     1 
ATOM   7307 O O     . ASP B 1 421 ? -23.245 54.544  -7.612  1.00 40.80  ? 421  ASP B O     1 
ATOM   7308 C CB    . ASP B 1 421 ? -23.847 57.179  -5.630  1.00 39.54  ? 421  ASP B CB    1 
ATOM   7309 C CG    . ASP B 1 421 ? -24.762 58.257  -5.058  1.00 40.61  ? 421  ASP B CG    1 
ATOM   7310 O OD1   . ASP B 1 421 ? -25.619 58.756  -5.800  1.00 37.16  ? 421  ASP B OD1   1 
ATOM   7311 O OD2   . ASP B 1 421 ? -24.604 58.598  -3.873  1.00 35.89  ? 421  ASP B OD2   1 
ATOM   7312 N N     . TYR B 1 422 ? -22.468 56.474  -8.527  1.00 39.41  ? 422  TYR B N     1 
ATOM   7313 C CA    . TYR B 1 422 ? -21.258 55.881  -9.151  1.00 38.39  ? 422  TYR B CA    1 
ATOM   7314 C C     . TYR B 1 422 ? -20.072 56.169  -8.237  1.00 35.17  ? 422  TYR B C     1 
ATOM   7315 O O     . TYR B 1 422 ? -19.550 57.294  -8.265  1.00 36.89  ? 422  TYR B O     1 
ATOM   7316 C CB    . TYR B 1 422 ? -21.002 56.420  -10.558 1.00 37.20  ? 422  TYR B CB    1 
ATOM   7317 C CG    . TYR B 1 422 ? -19.783 55.823  -11.206 1.00 36.44  ? 422  TYR B CG    1 
ATOM   7318 C CD1   . TYR B 1 422 ? -19.765 54.499  -11.622 1.00 37.37  ? 422  TYR B CD1   1 
ATOM   7319 C CD2   . TYR B 1 422 ? -18.639 56.579  -11.391 1.00 39.06  ? 422  TYR B CD2   1 
ATOM   7320 C CE1   . TYR B 1 422 ? -18.635 53.939  -12.201 1.00 34.02  ? 422  TYR B CE1   1 
ATOM   7321 C CE2   . TYR B 1 422 ? -17.507 56.044  -11.988 1.00 39.59  ? 422  TYR B CE2   1 
ATOM   7322 C CZ    . TYR B 1 422 ? -17.503 54.713  -12.380 1.00 36.92  ? 422  TYR B CZ    1 
ATOM   7323 O OH    . TYR B 1 422 ? -16.385 54.192  -12.949 1.00 37.34  ? 422  TYR B OH    1 
ATOM   7324 N N     . ALA B 1 423 ? -19.729 55.191  -7.407  1.00 34.17  ? 423  ALA B N     1 
ATOM   7325 C CA    . ALA B 1 423 ? -18.545 55.181  -6.515  1.00 35.79  ? 423  ALA B CA    1 
ATOM   7326 C C     . ALA B 1 423 ? -17.668 54.015  -6.979  1.00 33.87  ? 423  ALA B C     1 
ATOM   7327 O O     . ALA B 1 423 ? -18.088 52.847  -6.836  1.00 37.71  ? 423  ALA B O     1 
ATOM   7328 C CB    . ALA B 1 423 ? -18.975 55.047  -5.068  1.00 35.49  ? 423  ALA B CB    1 
ATOM   7329 N N     . ALA B 1 424 ? -16.529 54.313  -7.595  1.00 36.14  ? 424  ALA B N     1 
ATOM   7330 C CA    . ALA B 1 424 ? -15.751 53.303  -8.336  1.00 37.61  ? 424  ALA B CA    1 
ATOM   7331 C C     . ALA B 1 424 ? -14.253 53.622  -8.327  1.00 38.40  ? 424  ALA B C     1 
ATOM   7332 O O     . ALA B 1 424 ? -13.887 54.798  -8.183  1.00 40.92  ? 424  ALA B O     1 
ATOM   7333 C CB    . ALA B 1 424 ? -16.300 53.211  -9.731  1.00 39.02  ? 424  ALA B CB    1 
ATOM   7334 N N     . GLN B 1 425 ? -13.462 52.558  -8.520  1.00 37.51  ? 425  GLN B N     1 
ATOM   7335 C CA    . GLN B 1 425 ? -11.984 52.476  -8.502  1.00 41.51  ? 425  GLN B CA    1 
ATOM   7336 C C     . GLN B 1 425 ? -11.558 51.827  -9.821  1.00 37.69  ? 425  GLN B C     1 
ATOM   7337 O O     . GLN B 1 425 ? -12.147 50.809  -10.149 1.00 34.28  ? 425  GLN B O     1 
ATOM   7338 C CB    . GLN B 1 425 ? -11.584 51.556  -7.339  1.00 45.58  ? 425  GLN B CB    1 
ATOM   7339 C CG    . GLN B 1 425 ? -10.243 51.859  -6.686  1.00 51.07  ? 425  GLN B CG    1 
ATOM   7340 C CD    . GLN B 1 425 ? -10.121 51.200  -5.330  1.00 49.33  ? 425  GLN B CD    1 
ATOM   7341 O OE1   . GLN B 1 425 ? -10.474 50.038  -5.146  1.00 53.62  ? 425  GLN B OE1   1 
ATOM   7342 N NE2   . GLN B 1 425 ? -9.623  51.941  -4.351  1.00 62.46  ? 425  GLN B NE2   1 
ATOM   7343 N N     . PHE B 1 426 ? -10.567 52.354  -10.536 1.00 37.50  ? 426  PHE B N     1 
ATOM   7344 C CA    . PHE B 1 426 ? -9.795  51.541  -11.511 1.00 35.95  ? 426  PHE B CA    1 
ATOM   7345 C C     . PHE B 1 426 ? -8.453  51.191  -10.890 1.00 34.75  ? 426  PHE B C     1 
ATOM   7346 O O     . PHE B 1 426 ? -7.807  52.089  -10.349 1.00 34.79  ? 426  PHE B O     1 
ATOM   7347 C CB    . PHE B 1 426 ? -9.608  52.228  -12.855 1.00 32.87  ? 426  PHE B CB    1 
ATOM   7348 C CG    . PHE B 1 426 ? -10.878 52.295  -13.659 1.00 33.32  ? 426  PHE B CG    1 
ATOM   7349 C CD1   . PHE B 1 426 ? -11.218 51.270  -14.531 1.00 32.78  ? 426  PHE B CD1   1 
ATOM   7350 C CD2   . PHE B 1 426 ? -11.741 53.379  -13.528 1.00 32.48  ? 426  PHE B CD2   1 
ATOM   7351 C CE1   . PHE B 1 426 ? -12.380 51.346  -15.285 1.00 31.87  ? 426  PHE B CE1   1 
ATOM   7352 C CE2   . PHE B 1 426 ? -12.892 53.456  -14.286 1.00 31.30  ? 426  PHE B CE2   1 
ATOM   7353 C CZ    . PHE B 1 426 ? -13.200 52.447  -15.176 1.00 32.58  ? 426  PHE B CZ    1 
ATOM   7354 N N     . VAL B 1 427 ? -8.095  49.909  -10.969 1.00 35.60  ? 427  VAL B N     1 
ATOM   7355 C CA    . VAL B 1 427 ? -6.872  49.289  -10.381 1.00 34.12  ? 427  VAL B CA    1 
ATOM   7356 C C     . VAL B 1 427 ? -6.123  48.558  -11.493 1.00 35.67  ? 427  VAL B C     1 
ATOM   7357 O O     . VAL B 1 427 ? -6.767  47.771  -12.204 1.00 33.51  ? 427  VAL B O     1 
ATOM   7358 C CB    . VAL B 1 427 ? -7.265  48.310  -9.263  1.00 38.62  ? 427  VAL B CB    1 
ATOM   7359 C CG1   . VAL B 1 427 ? -6.063  47.535  -8.740  1.00 41.15  ? 427  VAL B CG1   1 
ATOM   7360 C CG2   . VAL B 1 427 ? -7.996  49.016  -8.121  1.00 39.84  ? 427  VAL B CG2   1 
ATOM   7361 N N     . VAL B 1 428 ? -4.814  48.774  -11.626 1.00 37.88  ? 428  VAL B N     1 
ATOM   7362 C CA    . VAL B 1 428 ? -3.973  47.942  -12.541 1.00 40.44  ? 428  VAL B CA    1 
ATOM   7363 C C     . VAL B 1 428 ? -3.130  46.987  -11.682 1.00 37.94  ? 428  VAL B C     1 
ATOM   7364 O O     . VAL B 1 428 ? -2.422  47.458  -10.784 1.00 35.87  ? 428  VAL B O     1 
ATOM   7365 C CB    . VAL B 1 428 ? -3.153  48.799  -13.520 1.00 40.65  ? 428  VAL B CB    1 
ATOM   7366 C CG1   . VAL B 1 428 ? -2.293  47.944  -14.428 1.00 44.74  ? 428  VAL B CG1   1 
ATOM   7367 C CG2   . VAL B 1 428 ? -4.073  49.676  -14.355 1.00 44.90  ? 428  VAL B CG2   1 
ATOM   7368 N N     . GLY B 1 429 ? -3.312  45.678  -11.877 1.00 36.16  ? 429  GLY B N     1 
ATOM   7369 C CA    . GLY B 1 429 ? -2.530  44.647  -11.166 1.00 36.66  ? 429  GLY B CA    1 
ATOM   7370 C C     . GLY B 1 429 ? -1.113  44.608  -11.706 1.00 37.96  ? 429  GLY B C     1 
ATOM   7371 O O     . GLY B 1 429 ? -0.191  45.102  -11.014 1.00 37.65  ? 429  GLY B O     1 
ATOM   7372 N N     . LEU B 1 430 ? -0.950  44.078  -12.919 1.00 33.33  ? 430  LEU B N     1 
ATOM   7373 C CA    . LEU B 1 430 ? 0.334   44.102  -13.659 1.00 33.49  ? 430  LEU B CA    1 
ATOM   7374 C C     . LEU B 1 430 ? 0.031   44.392  -15.129 1.00 32.91  ? 430  LEU B C     1 
ATOM   7375 O O     . LEU B 1 430 ? 0.457   45.453  -15.634 1.00 34.68  ? 430  LEU B O     1 
ATOM   7376 C CB    . LEU B 1 430 ? 1.052   42.764  -13.438 1.00 33.49  ? 430  LEU B CB    1 
ATOM   7377 C CG    . LEU B 1 430 ? 2.549   42.748  -13.751 1.00 37.37  ? 430  LEU B CG    1 
ATOM   7378 C CD1   . LEU B 1 430 ? 3.297   43.782  -12.923 1.00 37.83  ? 430  LEU B CD1   1 
ATOM   7379 C CD2   . LEU B 1 430 ? 3.150   41.359  -13.534 1.00 37.18  ? 430  LEU B CD2   1 
ATOM   7380 N N     . ARG B 1 431 ? -0.751  43.536  -15.784 1.00 35.94  ? 431  ARG B N     1 
ATOM   7381 C CA    . ARG B 1 431 ? -1.210  43.817  -17.175 1.00 33.89  ? 431  ARG B CA    1 
ATOM   7382 C C     . ARG B 1 431 ? -2.728  43.656  -17.292 1.00 33.04  ? 431  ARG B C     1 
ATOM   7383 O O     . ARG B 1 431 ? -3.193  43.591  -18.421 1.00 34.28  ? 431  ARG B O     1 
ATOM   7384 C CB    . ARG B 1 431 ? -0.451  42.956  -18.190 1.00 36.52  ? 431  ARG B CB    1 
ATOM   7385 C CG    . ARG B 1 431 ? -0.069  41.576  -17.698 1.00 37.07  ? 431  ARG B CG    1 
ATOM   7386 C CD    . ARG B 1 431 ? 0.559   40.725  -18.793 1.00 34.61  ? 431  ARG B CD    1 
ATOM   7387 N NE    . ARG B 1 431 ? 1.884   41.130  -19.200 1.00 27.51  ? 431  ARG B NE    1 
ATOM   7388 C CZ    . ARG B 1 431 ? 2.982   41.008  -18.468 1.00 28.77  ? 431  ARG B CZ    1 
ATOM   7389 N NH1   . ARG B 1 431 ? 2.929   40.565  -17.226 1.00 28.55  ? 431  ARG B NH1   1 
ATOM   7390 N NH2   . ARG B 1 431 ? 4.143   41.368  -18.966 1.00 31.27  ? 431  ARG B NH2   1 
ATOM   7391 N N     . GLU B 1 432 ? -3.473  43.645  -16.179 1.00 31.56  ? 432  GLU B N     1 
ATOM   7392 C CA    . GLU B 1 432 ? -4.964  43.609  -16.180 1.00 32.70  ? 432  GLU B CA    1 
ATOM   7393 C C     . GLU B 1 432 ? -5.498  44.832  -15.428 1.00 35.47  ? 432  GLU B C     1 
ATOM   7394 O O     . GLU B 1 432 ? -4.783  45.380  -14.561 1.00 35.51  ? 432  GLU B O     1 
ATOM   7395 C CB    . GLU B 1 432 ? -5.474  42.287  -15.594 1.00 32.14  ? 432  GLU B CB    1 
ATOM   7396 C CG    . GLU B 1 432 ? -5.728  42.274  -14.095 1.00 30.59  ? 432  GLU B CG    1 
ATOM   7397 C CD    . GLU B 1 432 ? -4.533  42.383  -13.145 1.00 31.98  ? 432  GLU B CD    1 
ATOM   7398 O OE1   . GLU B 1 432 ? -3.394  42.632  -13.605 1.00 31.74  ? 432  GLU B OE1   1 
ATOM   7399 O OE2   . GLU B 1 432 ? -4.761  42.261  -11.912 1.00 31.60  ? 432  GLU B OE2   1 
ATOM   7400 N N     . MET B 1 433 ? -6.709  45.258  -15.762 1.00 33.89  ? 433  MET B N     1 
ATOM   7401 C CA    . MET B 1 433 ? -7.394  46.366  -15.050 1.00 35.59  ? 433  MET B CA    1 
ATOM   7402 C C     . MET B 1 433 ? -8.643  45.790  -14.378 1.00 32.34  ? 433  MET B C     1 
ATOM   7403 O O     . MET B 1 433 ? -9.311  44.930  -14.978 1.00 30.76  ? 433  MET B O     1 
ATOM   7404 C CB    . MET B 1 433 ? -7.769  47.488  -16.029 1.00 33.56  ? 433  MET B CB    1 
ATOM   7405 C CG    . MET B 1 433 ? -8.369  48.708  -15.395 1.00 35.53  ? 433  MET B CG    1 
ATOM   7406 S SD    . MET B 1 433 ? -8.096  50.174  -16.414 1.00 37.50  ? 433  MET B SD    1 
ATOM   7407 C CE    . MET B 1 433 ? -9.153  49.781  -17.807 1.00 36.29  ? 433  MET B CE    1 
ATOM   7408 N N     . HIS B 1 434 ? -8.938  46.261  -13.176 1.00 30.49  ? 434  HIS B N     1 
ATOM   7409 C CA    . HIS B 1 434 ? -10.207 45.997  -12.458 1.00 31.73  ? 434  HIS B CA    1 
ATOM   7410 C C     . HIS B 1 434 ? -10.978 47.312  -12.384 1.00 36.23  ? 434  HIS B C     1 
ATOM   7411 O O     . HIS B 1 434 ? -10.359 48.349  -12.008 1.00 41.23  ? 434  HIS B O     1 
ATOM   7412 C CB    . HIS B 1 434 ? -9.945  45.433  -11.059 1.00 31.59  ? 434  HIS B CB    1 
ATOM   7413 C CG    . HIS B 1 434 ? -9.006  44.273  -11.042 1.00 32.40  ? 434  HIS B CG    1 
ATOM   7414 N ND1   . HIS B 1 434 ? -9.393  43.006  -10.659 1.00 35.33  ? 434  HIS B ND1   1 
ATOM   7415 C CD2   . HIS B 1 434 ? -7.691  44.187  -11.330 1.00 34.59  ? 434  HIS B CD2   1 
ATOM   7416 C CE1   . HIS B 1 434 ? -8.361  42.190  -10.718 1.00 33.03  ? 434  HIS B CE1   1 
ATOM   7417 N NE2   . HIS B 1 434 ? -7.308  42.888  -11.125 1.00 35.44  ? 434  HIS B NE2   1 
ATOM   7418 N N     . HIS B 1 435 ? -12.249 47.275  -12.779 1.00 33.44  ? 435  HIS B N     1 
ATOM   7419 C CA    . HIS B 1 435 ? -13.247 48.331  -12.512 1.00 30.70  ? 435  HIS B CA    1 
ATOM   7420 C C     . HIS B 1 435 ? -14.045 47.925  -11.283 1.00 30.02  ? 435  HIS B C     1 
ATOM   7421 O O     . HIS B 1 435 ? -14.972 47.106  -11.446 1.00 30.65  ? 435  HIS B O     1 
ATOM   7422 C CB    . HIS B 1 435 ? -14.116 48.562  -13.749 1.00 33.76  ? 435  HIS B CB    1 
ATOM   7423 C CG    . HIS B 1 435 ? -14.976 49.772  -13.622 1.00 32.71  ? 435  HIS B CG    1 
ATOM   7424 N ND1   . HIS B 1 435 ? -16.128 49.928  -14.348 1.00 31.04  ? 435  HIS B ND1   1 
ATOM   7425 C CD2   . HIS B 1 435 ? -14.844 50.877  -12.857 1.00 34.13  ? 435  HIS B CD2   1 
ATOM   7426 C CE1   . HIS B 1 435 ? -16.670 51.091  -14.038 1.00 35.17  ? 435  HIS B CE1   1 
ATOM   7427 N NE2   . HIS B 1 435 ? -15.899 51.699  -13.139 1.00 32.89  ? 435  HIS B NE2   1 
ATOM   7428 N N     . ILE B 1 436 ? -13.636 48.393  -10.095 1.00 27.99  ? 436  ILE B N     1 
ATOM   7429 C CA    . ILE B 1 436 ? -14.274 48.001  -8.813  1.00 31.68  ? 436  ILE B CA    1 
ATOM   7430 C C     . ILE B 1 436 ? -15.272 49.103  -8.423  1.00 32.74  ? 436  ILE B C     1 
ATOM   7431 O O     . ILE B 1 436 ? -14.847 50.153  -7.912  1.00 31.99  ? 436  ILE B O     1 
ATOM   7432 C CB    . ILE B 1 436 ? -13.230 47.707  -7.719  1.00 34.46  ? 436  ILE B CB    1 
ATOM   7433 C CG1   . ILE B 1 436 ? -12.145 46.744  -8.219  1.00 40.36  ? 436  ILE B CG1   1 
ATOM   7434 C CG2   . ILE B 1 436 ? -13.913 47.173  -6.471  1.00 35.03  ? 436  ILE B CG2   1 
ATOM   7435 C CD1   . ILE B 1 436 ? -10.966 46.583  -7.276  1.00 40.42  ? 436  ILE B CD1   1 
ATOM   7436 N N     . ALA B 1 437 ? -16.558 48.841  -8.654  1.00 31.96  ? 437  ALA B N     1 
ATOM   7437 C CA    . ALA B 1 437 ? -17.657 49.777  -8.356  1.00 36.70  ? 437  ALA B CA    1 
ATOM   7438 C C     . ALA B 1 437 ? -18.256 49.345  -7.017  1.00 40.77  ? 437  ALA B C     1 
ATOM   7439 O O     . ALA B 1 437 ? -18.453 48.134  -6.816  1.00 35.99  ? 437  ALA B O     1 
ATOM   7440 C CB    . ALA B 1 437 ? -18.678 49.780  -9.468  1.00 35.71  ? 437  ALA B CB    1 
ATOM   7441 N N     . LEU B 1 438 ? -18.493 50.302  -6.125  1.00 40.09  ? 438  LEU B N     1 
ATOM   7442 C CA    . LEU B 1 438 ? -19.270 50.053  -4.892  1.00 43.79  ? 438  LEU B CA    1 
ATOM   7443 C C     . LEU B 1 438 ? -20.675 50.623  -5.088  1.00 42.34  ? 438  LEU B C     1 
ATOM   7444 O O     . LEU B 1 438 ? -20.826 51.861  -5.192  1.00 43.25  ? 438  LEU B O     1 
ATOM   7445 C CB    . LEU B 1 438 ? -18.544 50.671  -3.705  1.00 50.74  ? 438  LEU B CB    1 
ATOM   7446 C CG    . LEU B 1 438 ? -18.560 49.789  -2.464  1.00 62.27  ? 438  LEU B CG    1 
ATOM   7447 C CD1   . LEU B 1 438 ? -17.199 49.161  -2.219  1.00 64.65  ? 438  LEU B CD1   1 
ATOM   7448 C CD2   . LEU B 1 438 ? -19.014 50.583  -1.253  1.00 61.77  ? 438  LEU B CD2   1 
ATOM   7449 N N     . LEU B 1 439 ? -21.644 49.730  -5.263  1.00 37.30  ? 439  LEU B N     1 
ATOM   7450 C CA    . LEU B 1 439 ? -23.069 50.092  -5.446  1.00 45.30  ? 439  LEU B CA    1 
ATOM   7451 C C     . LEU B 1 439 ? -23.675 50.213  -4.042  1.00 45.15  ? 439  LEU B C     1 
ATOM   7452 O O     . LEU B 1 439 ? -23.848 49.168  -3.392  1.00 44.26  ? 439  LEU B O     1 
ATOM   7453 C CB    . LEU B 1 439 ? -23.744 49.022  -6.306  1.00 40.94  ? 439  LEU B CB    1 
ATOM   7454 C CG    . LEU B 1 439 ? -23.172 48.904  -7.721  1.00 44.92  ? 439  LEU B CG    1 
ATOM   7455 C CD1   . LEU B 1 439 ? -23.866 47.809  -8.506  1.00 50.26  ? 439  LEU B CD1   1 
ATOM   7456 C CD2   . LEU B 1 439 ? -23.271 50.222  -8.464  1.00 45.29  ? 439  LEU B CD2   1 
ATOM   7457 N N     . LEU B 1 440 ? -23.846 51.448  -3.567  1.00 43.56  ? 440  LEU B N     1 
ATOM   7458 C CA    . LEU B 1 440 ? -24.345 51.764  -2.204  1.00 42.25  ? 440  LEU B CA    1 
ATOM   7459 C C     . LEU B 1 440 ? -25.867 51.861  -2.252  1.00 41.50  ? 440  LEU B C     1 
ATOM   7460 O O     . LEU B 1 440 ? -26.389 52.477  -3.206  1.00 41.89  ? 440  LEU B O     1 
ATOM   7461 C CB    . LEU B 1 440 ? -23.721 53.081  -1.746  1.00 43.40  ? 440  LEU B CB    1 
ATOM   7462 C CG    . LEU B 1 440 ? -22.233 52.994  -1.435  1.00 45.28  ? 440  LEU B CG    1 
ATOM   7463 C CD1   . LEU B 1 440 ? -21.575 54.360  -1.571  1.00 48.87  ? 440  LEU B CD1   1 
ATOM   7464 C CD2   . LEU B 1 440 ? -22.021 52.399  -0.052  1.00 46.80  ? 440  LEU B CD2   1 
ATOM   7465 N N     . PHE B 1 441 ? -26.538 51.259  -1.272  1.00 41.52  ? 441  PHE B N     1 
ATOM   7466 C CA    . PHE B 1 441 ? -28.014 51.165  -1.201  1.00 41.42  ? 441  PHE B CA    1 
ATOM   7467 C C     . PHE B 1 441 ? -28.422 51.106  0.262   1.00 45.74  ? 441  PHE B C     1 
ATOM   7468 O O     . PHE B 1 441 ? -27.585 50.767  1.124   1.00 43.90  ? 441  PHE B O     1 
ATOM   7469 C CB    . PHE B 1 441 ? -28.542 49.946  -1.957  1.00 44.56  ? 441  PHE B CB    1 
ATOM   7470 C CG    . PHE B 1 441 ? -28.079 48.601  -1.452  1.00 48.29  ? 441  PHE B CG    1 
ATOM   7471 C CD1   . PHE B 1 441 ? -26.777 48.155  -1.673  1.00 45.62  ? 441  PHE B CD1   1 
ATOM   7472 C CD2   . PHE B 1 441 ? -28.947 47.771  -0.764  1.00 45.75  ? 441  PHE B CD2   1 
ATOM   7473 C CE1   . PHE B 1 441 ? -26.364 46.909  -1.228  1.00 48.14  ? 441  PHE B CE1   1 
ATOM   7474 C CE2   . PHE B 1 441 ? -28.521 46.535  -0.299  1.00 48.90  ? 441  PHE B CE2   1 
ATOM   7475 C CZ    . PHE B 1 441 ? -27.242 46.093  -0.550  1.00 46.88  ? 441  PHE B CZ    1 
ATOM   7476 N N     . ASP B 1 442 ? -29.680 51.451  0.509   1.00 45.03  ? 442  ASP B N     1 
ATOM   7477 C CA    . ASP B 1 442 ? -30.357 51.280  1.815   1.00 44.20  ? 442  ASP B CA    1 
ATOM   7478 C C     . ASP B 1 442 ? -30.751 49.812  1.967   1.00 43.78  ? 442  ASP B C     1 
ATOM   7479 O O     . ASP B 1 442 ? -31.724 49.386  1.304   1.00 43.18  ? 442  ASP B O     1 
ATOM   7480 C CB    . ASP B 1 442 ? -31.584 52.189  1.904   1.00 48.03  ? 442  ASP B CB    1 
ATOM   7481 C CG    . ASP B 1 442 ? -32.200 52.212  3.281   1.00 47.21  ? 442  ASP B CG    1 
ATOM   7482 O OD1   . ASP B 1 442 ? -31.853 51.316  4.098   1.00 46.17  ? 442  ASP B OD1   1 
ATOM   7483 O OD2   . ASP B 1 442 ? -33.003 53.127  3.527   1.00 53.00  ? 442  ASP B OD2   1 
ATOM   7484 N N     . THR B 1 443 ? -30.036 49.089  2.830   1.00 40.87  ? 443  THR B N     1 
ATOM   7485 C CA    . THR B 1 443 ? -30.282 47.660  3.152   1.00 48.46  ? 443  THR B CA    1 
ATOM   7486 C C     . THR B 1 443 ? -31.674 47.454  3.761   1.00 51.06  ? 443  THR B C     1 
ATOM   7487 O O     . THR B 1 443 ? -32.175 46.315  3.681   1.00 49.29  ? 443  THR B O     1 
ATOM   7488 C CB    . THR B 1 443 ? -29.238 47.138  4.141   1.00 47.04  ? 443  THR B CB    1 
ATOM   7489 O OG1   . THR B 1 443 ? -29.250 48.063  5.228   1.00 45.01  ? 443  THR B OG1   1 
ATOM   7490 C CG2   . THR B 1 443 ? -27.859 47.021  3.531   1.00 43.67  ? 443  THR B CG2   1 
ATOM   7491 N N     . GLN B 1 444 ? -32.245 48.500  4.369   1.00 56.33  ? 444  GLN B N     1 
ATOM   7492 C CA    . GLN B 1 444 ? -33.551 48.462  5.085   1.00 57.55  ? 444  GLN B CA    1 
ATOM   7493 C C     . GLN B 1 444 ? -34.708 48.769  4.126   1.00 56.58  ? 444  GLN B C     1 
ATOM   7494 O O     . GLN B 1 444 ? -35.850 48.763  4.587   1.00 58.23  ? 444  GLN B O     1 
ATOM   7495 C CB    . GLN B 1 444 ? -33.540 49.463  6.239   1.00 55.29  ? 444  GLN B CB    1 
ATOM   7496 C CG    . GLN B 1 444 ? -32.367 49.279  7.188   1.00 58.75  ? 444  GLN B CG    1 
ATOM   7497 C CD    . GLN B 1 444 ? -32.337 47.900  7.804   1.00 65.62  ? 444  GLN B CD    1 
ATOM   7498 O OE1   . GLN B 1 444 ? -31.313 47.213  7.802   1.00 62.54  ? 444  GLN B OE1   1 
ATOM   7499 N NE2   . GLN B 1 444 ? -33.475 47.476  8.331   1.00 67.56  ? 444  GLN B NE2   1 
ATOM   7500 N N     . ASP B 1 445 ? -34.434 49.024  2.844   1.00 54.85  ? 445  ASP B N     1 
ATOM   7501 C CA    . ASP B 1 445 ? -35.474 49.423  1.859   1.00 55.35  ? 445  ASP B CA    1 
ATOM   7502 C C     . ASP B 1 445 ? -35.585 48.341  0.783   1.00 49.44  ? 445  ASP B C     1 
ATOM   7503 O O     . ASP B 1 445 ? -34.659 48.241  -0.046  1.00 51.86  ? 445  ASP B O     1 
ATOM   7504 C CB    . ASP B 1 445 ? -35.151 50.809  1.298   1.00 56.55  ? 445  ASP B CB    1 
ATOM   7505 C CG    . ASP B 1 445 ? -36.134 51.321  0.264   1.00 60.06  ? 445  ASP B CG    1 
ATOM   7506 O OD1   . ASP B 1 445 ? -37.071 50.579  -0.074  1.00 68.34  ? 445  ASP B OD1   1 
ATOM   7507 O OD2   . ASP B 1 445 ? -35.941 52.459  -0.201  1.00 63.71  ? 445  ASP B OD2   1 
ATOM   7508 N N     . ALA B 1 446 ? -36.675 47.568  0.778   1.00 45.92  ? 446  ALA B N     1 
ATOM   7509 C CA    . ALA B 1 446 ? -36.912 46.479  -0.208  1.00 50.32  ? 446  ALA B CA    1 
ATOM   7510 C C     . ALA B 1 446 ? -36.727 46.970  -1.656  1.00 52.61  ? 446  ALA B C     1 
ATOM   7511 O O     . ALA B 1 446 ? -36.209 46.172  -2.456  1.00 44.30  ? 446  ALA B O     1 
ATOM   7512 C CB    . ALA B 1 446 ? -38.278 45.863  -0.036  1.00 51.83  ? 446  ALA B CB    1 
ATOM   7513 N N     . THR B 1 447 ? -37.162 48.193  -2.003  1.00 50.97  ? 447  THR B N     1 
ATOM   7514 C CA    . THR B 1 447 ? -37.052 48.758  -3.384  1.00 51.73  ? 447  THR B CA    1 
ATOM   7515 C C     . THR B 1 447 ? -35.577 48.985  -3.733  1.00 49.37  ? 447  THR B C     1 
ATOM   7516 O O     . THR B 1 447 ? -35.178 48.571  -4.815  1.00 49.46  ? 447  THR B O     1 
ATOM   7517 C CB    . THR B 1 447 ? -37.801 50.089  -3.578  1.00 53.46  ? 447  THR B CB    1 
ATOM   7518 O OG1   . THR B 1 447 ? -39.168 49.951  -3.198  1.00 60.30  ? 447  THR B OG1   1 
ATOM   7519 C CG2   . THR B 1 447 ? -37.790 50.571  -5.012  1.00 53.33  ? 447  THR B CG2   1 
ATOM   7520 N N     . ALA B 1 448 ? -34.822 49.661  -2.863  1.00 47.87  ? 448  ALA B N     1 
ATOM   7521 C CA    . ALA B 1 448 ? -33.365 49.883  -2.997  1.00 46.01  ? 448  ALA B CA    1 
ATOM   7522 C C     . ALA B 1 448 ? -32.656 48.537  -3.222  1.00 43.49  ? 448  ALA B C     1 
ATOM   7523 O O     . ALA B 1 448 ? -31.892 48.442  -4.198  1.00 42.29  ? 448  ALA B O     1 
ATOM   7524 C CB    . ALA B 1 448 ? -32.838 50.614  -1.786  1.00 46.02  ? 448  ALA B CB    1 
ATOM   7525 N N     . ARG B 1 449 ? -32.955 47.523  -2.408  1.00 40.01  ? 449  ARG B N     1 
ATOM   7526 C CA    . ARG B 1 449 ? -32.348 46.162  -2.478  1.00 42.37  ? 449  ARG B CA    1 
ATOM   7527 C C     . ARG B 1 449 ? -32.662 45.501  -3.820  1.00 45.60  ? 449  ARG B C     1 
ATOM   7528 O O     . ARG B 1 449 ? -31.720 44.952  -4.442  1.00 46.56  ? 449  ARG B O     1 
ATOM   7529 C CB    . ARG B 1 449 ? -32.848 45.248  -1.358  1.00 41.48  ? 449  ARG B CB    1 
ATOM   7530 C CG    . ARG B 1 449 ? -32.341 45.636  0.022   1.00 46.79  ? 449  ARG B CG    1 
ATOM   7531 C CD    . ARG B 1 449 ? -32.399 44.469  0.980   1.00 49.04  ? 449  ARG B CD    1 
ATOM   7532 N NE    . ARG B 1 449 ? -33.726 43.876  1.042   1.00 55.21  ? 449  ARG B NE    1 
ATOM   7533 C CZ    . ARG B 1 449 ? -34.718 44.288  1.833   1.00 58.07  ? 449  ARG B CZ    1 
ATOM   7534 N NH1   . ARG B 1 449 ? -34.552 45.334  2.627   1.00 53.36  ? 449  ARG B NH1   1 
ATOM   7535 N NH2   . ARG B 1 449 ? -35.880 43.651  1.817   1.00 55.68  ? 449  ARG B NH2   1 
ATOM   7536 N N     . ASN B 1 450 ? -33.935 45.519  -4.220  1.00 45.57  ? 450  ASN B N     1 
ATOM   7537 C CA    . ASN B 1 450 ? -34.432 44.975  -5.508  1.00 43.70  ? 450  ASN B CA    1 
ATOM   7538 C C     . ASN B 1 450 ? -33.732 45.694  -6.658  1.00 40.67  ? 450  ASN B C     1 
ATOM   7539 O O     . ASN B 1 450 ? -33.264 45.010  -7.572  1.00 45.68  ? 450  ASN B O     1 
ATOM   7540 C CB    . ASN B 1 450 ? -35.950 45.118  -5.615  1.00 47.78  ? 450  ASN B CB    1 
ATOM   7541 C CG    . ASN B 1 450 ? -36.684 44.243  -4.621  1.00 52.85  ? 450  ASN B CG    1 
ATOM   7542 O OD1   . ASN B 1 450 ? -36.091 43.361  -3.999  1.00 53.56  ? 450  ASN B OD1   1 
ATOM   7543 N ND2   . ASN B 1 450 ? -37.977 44.480  -4.470  1.00 53.26  ? 450  ASN B ND2   1 
ATOM   7544 N N     . GLU B 1 451 ? -33.696 47.028  -6.628  1.00 43.53  ? 451  GLU B N     1 
ATOM   7545 C CA    . GLU B 1 451 ? -33.129 47.860  -7.723  1.00 47.71  ? 451  GLU B CA    1 
ATOM   7546 C C     . GLU B 1 451 ? -31.633 47.524  -7.841  1.00 43.23  ? 451  GLU B C     1 
ATOM   7547 O O     . GLU B 1 451 ? -31.122 47.442  -8.965  1.00 47.55  ? 451  GLU B O     1 
ATOM   7548 C CB    . GLU B 1 451 ? -33.322 49.361  -7.452  1.00 51.10  ? 451  GLU B CB    1 
ATOM   7549 C CG    . GLU B 1 451 ? -34.720 49.912  -7.715  1.00 55.08  ? 451  GLU B CG    1 
ATOM   7550 C CD    . GLU B 1 451 ? -34.811 51.429  -7.561  1.00 62.67  ? 451  GLU B CD    1 
ATOM   7551 O OE1   . GLU B 1 451 ? -35.118 52.112  -8.563  1.00 68.21  ? 451  GLU B OE1   1 
ATOM   7552 O OE2   . GLU B 1 451 ? -34.525 51.934  -6.454  1.00 58.64  ? 451  GLU B OE2   1 
ATOM   7553 N N     . THR B 1 452 ? -30.950 47.370  -6.708  1.00 41.71  ? 452  THR B N     1 
ATOM   7554 C CA    . THR B 1 452 ? -29.487 47.111  -6.669  1.00 41.55  ? 452  THR B CA    1 
ATOM   7555 C C     . THR B 1 452 ? -29.222 45.770  -7.349  1.00 39.09  ? 452  THR B C     1 
ATOM   7556 O O     . THR B 1 452 ? -28.326 45.744  -8.213  1.00 41.93  ? 452  THR B O     1 
ATOM   7557 C CB    . THR B 1 452 ? -28.912 47.209  -5.256  1.00 41.93  ? 452  THR B CB    1 
ATOM   7558 O OG1   . THR B 1 452 ? -29.148 48.542  -4.804  1.00 39.83  ? 452  THR B OG1   1 
ATOM   7559 C CG2   . THR B 1 452 ? -27.423 46.915  -5.214  1.00 42.18  ? 452  THR B CG2   1 
ATOM   7560 N N     . LEU B 1 453 ? -30.005 44.734  -7.038  1.00 37.33  ? 453  LEU B N     1 
ATOM   7561 C CA    . LEU B 1 453 ? -29.850 43.392  -7.669  1.00 40.04  ? 453  LEU B CA    1 
ATOM   7562 C C     . LEU B 1 453 ? -30.056 43.542  -9.173  1.00 44.44  ? 453  LEU B C     1 
ATOM   7563 O O     . LEU B 1 453 ? -29.202 43.044  -9.929  1.00 43.72  ? 453  LEU B O     1 
ATOM   7564 C CB    . LEU B 1 453 ? -30.856 42.380  -7.109  1.00 42.12  ? 453  LEU B CB    1 
ATOM   7565 C CG    . LEU B 1 453 ? -30.699 40.918  -7.565  1.00 41.95  ? 453  LEU B CG    1 
ATOM   7566 C CD1   . LEU B 1 453 ? -29.248 40.442  -7.494  1.00 40.19  ? 453  LEU B CD1   1 
ATOM   7567 C CD2   . LEU B 1 453 ? -31.582 39.988  -6.732  1.00 41.63  ? 453  LEU B CD2   1 
ATOM   7568 N N     . ALA B 1 454 ? -31.151 44.204  -9.578  1.00 44.52  ? 454  ALA B N     1 
ATOM   7569 C CA    . ALA B 1 454 ? -31.498 44.451  -10.998 1.00 44.27  ? 454  ALA B CA    1 
ATOM   7570 C C     . ALA B 1 454 ? -30.322 45.158  -11.666 1.00 37.99  ? 454  ALA B C     1 
ATOM   7571 O O     . ALA B 1 454 ? -29.853 44.689  -12.726 1.00 39.58  ? 454  ALA B O     1 
ATOM   7572 C CB    . ALA B 1 454 ? -32.778 45.252  -11.123 1.00 45.22  ? 454  ALA B CB    1 
ATOM   7573 N N     . LEU B 1 455 ? -29.850 46.242  -11.065 1.00 37.25  ? 455  LEU B N     1 
ATOM   7574 C CA    . LEU B 1 455 ? -28.743 47.031  -11.647 1.00 38.46  ? 455  LEU B CA    1 
ATOM   7575 C C     . LEU B 1 455 ? -27.548 46.088  -11.875 1.00 38.90  ? 455  LEU B C     1 
ATOM   7576 O O     . LEU B 1 455 ? -27.055 46.023  -13.012 1.00 39.70  ? 455  LEU B O     1 
ATOM   7577 C CB    . LEU B 1 455 ? -28.399 48.177  -10.697 1.00 38.97  ? 455  LEU B CB    1 
ATOM   7578 C CG    . LEU B 1 455 ? -27.100 48.923  -10.991 1.00 39.36  ? 455  LEU B CG    1 
ATOM   7579 C CD1   . LEU B 1 455 ? -27.102 49.533  -12.387 1.00 42.46  ? 455  LEU B CD1   1 
ATOM   7580 C CD2   . LEU B 1 455 ? -26.870 49.993  -9.943  1.00 37.65  ? 455  LEU B CD2   1 
ATOM   7581 N N     . THR B 1 456 ? -27.142 45.342  -10.849 1.00 33.99  ? 456  THR B N     1 
ATOM   7582 C CA    . THR B 1 456 ? -25.922 44.490  -10.882 1.00 36.20  ? 456  THR B CA    1 
ATOM   7583 C C     . THR B 1 456 ? -26.077 43.399  -11.949 1.00 36.33  ? 456  THR B C     1 
ATOM   7584 O O     . THR B 1 456 ? -25.113 43.169  -12.690 1.00 36.92  ? 456  THR B O     1 
ATOM   7585 C CB    . THR B 1 456 ? -25.603 43.870  -9.516  1.00 36.80  ? 456  THR B CB    1 
ATOM   7586 O OG1   . THR B 1 456 ? -25.713 44.880  -8.509  1.00 33.50  ? 456  THR B OG1   1 
ATOM   7587 C CG2   . THR B 1 456 ? -24.206 43.278  -9.495  1.00 37.04  ? 456  THR B CG2   1 
ATOM   7588 N N     . ARG B 1 457 ? -27.236 42.746  -12.036 1.00 33.48  ? 457  ARG B N     1 
ATOM   7589 C CA    . ARG B 1 457 ? -27.501 41.744  -13.102 1.00 34.85  ? 457  ARG B CA    1 
ATOM   7590 C C     . ARG B 1 457 ? -27.261 42.357  -14.478 1.00 38.34  ? 457  ARG B C     1 
ATOM   7591 O O     . ARG B 1 457 ? -26.623 41.695  -15.358 1.00 36.43  ? 457  ARG B O     1 
ATOM   7592 C CB    . ARG B 1 457 ? -28.930 41.214  -12.994 1.00 37.25  ? 457  ARG B CB    1 
ATOM   7593 C CG    . ARG B 1 457 ? -29.129 40.288  -11.806 1.00 38.61  ? 457  ARG B CG    1 
ATOM   7594 C CD    . ARG B 1 457 ? -30.071 39.135  -12.107 1.00 40.09  ? 457  ARG B CD    1 
ATOM   7595 N NE    . ARG B 1 457 ? -30.247 38.382  -10.879 1.00 38.41  ? 457  ARG B NE    1 
ATOM   7596 C CZ    . ARG B 1 457 ? -29.462 37.384  -10.477 1.00 43.55  ? 457  ARG B CZ    1 
ATOM   7597 N NH1   . ARG B 1 457 ? -28.448 36.993  -11.233 1.00 39.00  ? 457  ARG B NH1   1 
ATOM   7598 N NH2   . ARG B 1 457 ? -29.709 36.768  -9.325  1.00 40.60  ? 457  ARG B NH2   1 
ATOM   7599 N N     . LEU B 1 458 ? -27.748 43.581  -14.678 1.00 37.20  ? 458  LEU B N     1 
ATOM   7600 C CA    . LEU B 1 458 ? -27.665 44.256  -15.994 1.00 34.19  ? 458  LEU B CA    1 
ATOM   7601 C C     . LEU B 1 458 ? -26.198 44.624  -16.259 1.00 36.05  ? 458  LEU B C     1 
ATOM   7602 O O     . LEU B 1 458 ? -25.718 44.452  -17.414 1.00 40.35  ? 458  LEU B O     1 
ATOM   7603 C CB    . LEU B 1 458 ? -28.566 45.495  -15.975 1.00 33.82  ? 458  LEU B CB    1 
ATOM   7604 C CG    . LEU B 1 458 ? -28.496 46.364  -17.226 1.00 33.72  ? 458  LEU B CG    1 
ATOM   7605 C CD1   . LEU B 1 458 ? -29.051 45.609  -18.428 1.00 32.93  ? 458  LEU B CD1   1 
ATOM   7606 C CD2   . LEU B 1 458 ? -29.229 47.683  -17.016 1.00 33.77  ? 458  LEU B CD2   1 
ATOM   7607 N N     . LEU B 1 459 ? -25.501 45.130  -15.240 1.00 33.49  ? 459  LEU B N     1 
ATOM   7608 C CA    . LEU B 1 459 ? -24.074 45.531  -15.346 1.00 36.30  ? 459  LEU B CA    1 
ATOM   7609 C C     . LEU B 1 459 ? -23.214 44.339  -15.789 1.00 33.54  ? 459  LEU B C     1 
ATOM   7610 O O     . LEU B 1 459 ? -22.382 44.520  -16.695 1.00 33.45  ? 459  LEU B O     1 
ATOM   7611 C CB    . LEU B 1 459 ? -23.619 46.074  -13.991 1.00 37.68  ? 459  LEU B CB    1 
ATOM   7612 C CG    . LEU B 1 459 ? -24.099 47.487  -13.683 1.00 34.97  ? 459  LEU B CG    1 
ATOM   7613 C CD1   . LEU B 1 459 ? -23.585 47.942  -12.329 1.00 37.51  ? 459  LEU B CD1   1 
ATOM   7614 C CD2   . LEU B 1 459 ? -23.668 48.451  -14.767 1.00 34.20  ? 459  LEU B CD2   1 
ATOM   7615 N N     . ILE B 1 460 ? -23.465 43.168  -15.201 1.00 29.92  ? 460  ILE B N     1 
ATOM   7616 C CA    . ILE B 1 460 ? -22.731 41.900  -15.467 1.00 30.12  ? 460  ILE B CA    1 
ATOM   7617 C C     . ILE B 1 460 ? -22.967 41.481  -16.925 1.00 33.30  ? 460  ILE B C     1 
ATOM   7618 O O     . ILE B 1 460 ? -21.970 41.202  -17.620 1.00 32.76  ? 460  ILE B O     1 
ATOM   7619 C CB    . ILE B 1 460 ? -23.173 40.820  -14.466 1.00 30.08  ? 460  ILE B CB    1 
ATOM   7620 C CG1   . ILE B 1 460 ? -22.619 41.132  -13.076 1.00 28.36  ? 460  ILE B CG1   1 
ATOM   7621 C CG2   . ILE B 1 460 ? -22.765 39.432  -14.960 1.00 30.61  ? 460  ILE B CG2   1 
ATOM   7622 C CD1   . ILE B 1 460 ? -23.241 40.327  -11.997 1.00 29.26  ? 460  ILE B CD1   1 
ATOM   7623 N N     . ASP B 1 461 ? -24.220 41.486  -17.385 1.00 34.08  ? 461  ASP B N     1 
ATOM   7624 C CA    . ASP B 1 461 ? -24.577 41.099  -18.779 1.00 36.95  ? 461  ASP B CA    1 
ATOM   7625 C C     . ASP B 1 461 ? -23.931 42.073  -19.768 1.00 32.82  ? 461  ASP B C     1 
ATOM   7626 O O     . ASP B 1 461 ? -23.403 41.604  -20.771 1.00 37.17  ? 461  ASP B O     1 
ATOM   7627 C CB    . ASP B 1 461 ? -26.090 40.983  -18.982 1.00 39.66  ? 461  ASP B CB    1 
ATOM   7628 C CG    . ASP B 1 461 ? -26.686 39.724  -18.370 1.00 47.40  ? 461  ASP B CG    1 
ATOM   7629 O OD1   . ASP B 1 461 ? -25.946 38.697  -18.228 1.00 44.62  ? 461  ASP B OD1   1 
ATOM   7630 O OD2   . ASP B 1 461 ? -27.890 39.767  -18.030 1.00 56.63  ? 461  ASP B OD2   1 
ATOM   7631 N N     . GLU B 1 462 ? -23.972 43.380  -19.519 1.00 35.64  ? 462  GLU B N     1 
ATOM   7632 C CA    . GLU B 1 462 ? -23.470 44.381  -20.501 1.00 34.43  ? 462  GLU B CA    1 
ATOM   7633 C C     . GLU B 1 462 ? -21.940 44.320  -20.542 1.00 31.70  ? 462  GLU B C     1 
ATOM   7634 O O     . GLU B 1 462 ? -21.385 44.461  -21.640 1.00 29.88  ? 462  GLU B O     1 
ATOM   7635 C CB    . GLU B 1 462 ? -24.007 45.774  -20.194 1.00 34.30  ? 462  GLU B CB    1 
ATOM   7636 C CG    . GLU B 1 462 ? -25.503 45.856  -20.419 1.00 39.57  ? 462  GLU B CG    1 
ATOM   7637 C CD    . GLU B 1 462 ? -26.077 47.259  -20.495 1.00 40.47  ? 462  GLU B CD    1 
ATOM   7638 O OE1   . GLU B 1 462 ? -25.649 48.126  -19.697 1.00 38.60  ? 462  GLU B OE1   1 
ATOM   7639 O OE2   . GLU B 1 462 ? -26.956 47.468  -21.354 1.00 36.83  ? 462  GLU B OE2   1 
ATOM   7640 N N     . ALA B 1 463 ? -21.305 44.149  -19.380 1.00 29.88  ? 463  ALA B N     1 
ATOM   7641 C CA    . ALA B 1 463 ? -19.845 43.946  -19.206 1.00 31.70  ? 463  ALA B CA    1 
ATOM   7642 C C     . ALA B 1 463 ? -19.377 42.727  -20.016 1.00 29.75  ? 463  ALA B C     1 
ATOM   7643 O O     . ALA B 1 463 ? -18.437 42.844  -20.839 1.00 32.30  ? 463  ALA B O     1 
ATOM   7644 C CB    . ALA B 1 463 ? -19.546 43.760  -17.741 1.00 33.73  ? 463  ALA B CB    1 
ATOM   7645 N N     . ALA B 1 464 ? -20.079 41.619  -19.844 1.00 30.42  ? 464  ALA B N     1 
ATOM   7646 C CA    . ALA B 1 464 ? -19.839 40.335  -20.533 1.00 29.56  ? 464  ALA B CA    1 
ATOM   7647 C C     . ALA B 1 464 ? -19.979 40.507  -22.047 1.00 30.30  ? 464  ALA B C     1 
ATOM   7648 O O     . ALA B 1 464 ? -19.107 40.004  -22.769 1.00 30.48  ? 464  ALA B O     1 
ATOM   7649 C CB    . ALA B 1 464 ? -20.789 39.301  -19.989 1.00 31.64  ? 464  ALA B CB    1 
ATOM   7650 N N     . ALA B 1 465 ? -21.023 41.204  -22.517 1.00 32.55  ? 465  ALA B N     1 
ATOM   7651 C CA    . ALA B 1 465 ? -21.277 41.416  -23.965 1.00 34.61  ? 465  ALA B CA    1 
ATOM   7652 C C     . ALA B 1 465 ? -20.111 42.213  -24.561 1.00 37.43  ? 465  ALA B C     1 
ATOM   7653 O O     . ALA B 1 465 ? -19.830 42.060  -25.743 1.00 39.98  ? 465  ALA B O     1 
ATOM   7654 C CB    . ALA B 1 465 ? -22.608 42.103  -24.183 1.00 37.06  ? 465  ALA B CB    1 
ATOM   7655 N N     . GLU B 1 466 ? -19.402 42.968  -23.725 1.00 37.42  ? 466  GLU B N     1 
ATOM   7656 C CA    . GLU B 1 466 ? -18.265 43.819  -24.117 1.00 35.92  ? 466  GLU B CA    1 
ATOM   7657 C C     . GLU B 1 466 ? -16.944 43.047  -23.936 1.00 35.85  ? 466  GLU B C     1 
ATOM   7658 O O     . GLU B 1 466 ? -15.911 43.541  -24.352 1.00 34.51  ? 466  GLU B O     1 
ATOM   7659 C CB    . GLU B 1 466 ? -18.349 45.085  -23.263 1.00 42.84  ? 466  GLU B CB    1 
ATOM   7660 C CG    . GLU B 1 466 ? -18.183 46.357  -24.038 1.00 45.83  ? 466  GLU B CG    1 
ATOM   7661 C CD    . GLU B 1 466 ? -18.993 46.453  -25.321 1.00 44.64  ? 466  GLU B CD    1 
ATOM   7662 O OE1   . GLU B 1 466 ? -20.207 46.350  -25.261 1.00 52.82  ? 466  GLU B OE1   1 
ATOM   7663 O OE2   . GLU B 1 466 ? -18.395 46.611  -26.372 1.00 49.33  ? 466  GLU B OE2   1 
ATOM   7664 N N     . GLY B 1 467 ? -16.971 41.851  -23.360 1.00 35.11  ? 467  GLY B N     1 
ATOM   7665 C CA    . GLY B 1 467 ? -15.766 41.013  -23.203 1.00 34.59  ? 467  GLY B CA    1 
ATOM   7666 C C     . GLY B 1 467 ? -15.115 41.253  -21.854 1.00 33.18  ? 467  GLY B C     1 
ATOM   7667 O O     . GLY B 1 467 ? -13.945 40.860  -21.678 1.00 32.03  ? 467  GLY B O     1 
ATOM   7668 N N     . TYR B 1 468 ? -15.864 41.812  -20.905 1.00 32.20  ? 468  TYR B N     1 
ATOM   7669 C CA    . TYR B 1 468 ? -15.362 42.089  -19.531 1.00 32.27  ? 468  TYR B CA    1 
ATOM   7670 C C     . TYR B 1 468 ? -16.049 41.129  -18.558 1.00 32.64  ? 468  TYR B C     1 
ATOM   7671 O O     . TYR B 1 468 ? -17.275 41.203  -18.318 1.00 34.32  ? 468  TYR B O     1 
ATOM   7672 C CB    . TYR B 1 468 ? -15.561 43.553  -19.158 1.00 31.93  ? 468  TYR B CB    1 
ATOM   7673 C CG    . TYR B 1 468 ? -15.102 44.569  -20.173 1.00 32.77  ? 468  TYR B CG    1 
ATOM   7674 C CD1   . TYR B 1 468 ? -13.905 44.424  -20.855 1.00 33.35  ? 468  TYR B CD1   1 
ATOM   7675 C CD2   . TYR B 1 468 ? -15.843 45.717  -20.410 1.00 31.66  ? 468  TYR B CD2   1 
ATOM   7676 C CE1   . TYR B 1 468 ? -13.484 45.355  -21.788 1.00 31.01  ? 468  TYR B CE1   1 
ATOM   7677 C CE2   . TYR B 1 468 ? -15.417 46.681  -21.313 1.00 30.99  ? 468  TYR B CE2   1 
ATOM   7678 C CZ    . TYR B 1 468 ? -14.245 46.489  -22.020 1.00 32.02  ? 468  TYR B CZ    1 
ATOM   7679 O OH    . TYR B 1 468 ? -13.804 47.440  -22.889 1.00 32.51  ? 468  TYR B OH    1 
ATOM   7680 N N     . GLY B 1 469 ? -15.278 40.200  -18.013 1.00 29.26  ? 469  GLY B N     1 
ATOM   7681 C CA    . GLY B 1 469 ? -15.816 39.213  -17.079 1.00 29.89  ? 469  GLY B CA    1 
ATOM   7682 C C     . GLY B 1 469 ? -15.646 39.673  -15.647 1.00 28.68  ? 469  GLY B C     1 
ATOM   7683 O O     . GLY B 1 469 ? -14.637 40.312  -15.348 1.00 29.16  ? 469  GLY B O     1 
ATOM   7684 N N     . GLU B 1 470 ? -16.592 39.292  -14.797 1.00 28.27  ? 470  GLU B N     1 
ATOM   7685 C CA    . GLU B 1 470 ? -16.568 39.525  -13.339 1.00 30.63  ? 470  GLU B CA    1 
ATOM   7686 C C     . GLU B 1 470 ? -15.612 38.515  -12.669 1.00 30.26  ? 470  GLU B C     1 
ATOM   7687 O O     . GLU B 1 470 ? -15.570 37.346  -13.056 1.00 26.21  ? 470  GLU B O     1 
ATOM   7688 C CB    . GLU B 1 470 ? -18.006 39.432  -12.833 1.00 32.43  ? 470  GLU B CB    1 
ATOM   7689 C CG    . GLU B 1 470 ? -18.160 39.541  -11.329 1.00 35.65  ? 470  GLU B CG    1 
ATOM   7690 C CD    . GLU B 1 470 ? -17.574 40.813  -10.733 1.00 40.54  ? 470  GLU B CD    1 
ATOM   7691 O OE1   . GLU B 1 470 ? -18.377 41.746  -10.413 1.00 38.08  ? 470  GLU B OE1   1 
ATOM   7692 O OE2   . GLU B 1 470 ? -16.299 40.874  -10.598 1.00 37.58  ? 470  GLU B OE2   1 
ATOM   7693 N N     . TYR B 1 471 ? -14.870 38.971  -11.671 1.00 34.70  ? 471  TYR B N     1 
ATOM   7694 C CA    . TYR B 1 471 ? -13.754 38.223  -11.048 1.00 33.86  ? 471  TYR B CA    1 
ATOM   7695 C C     . TYR B 1 471 ? -14.213 37.625  -9.711  1.00 37.55  ? 471  TYR B C     1 
ATOM   7696 O O     . TYR B 1 471 ? -13.703 36.545  -9.308  1.00 32.77  ? 471  TYR B O     1 
ATOM   7697 C CB    . TYR B 1 471 ? -12.551 39.157  -10.930 1.00 39.61  ? 471  TYR B CB    1 
ATOM   7698 C CG    . TYR B 1 471 ? -11.387 38.534  -10.221 1.00 42.70  ? 471  TYR B CG    1 
ATOM   7699 C CD1   . TYR B 1 471 ? -10.490 37.714  -10.892 1.00 51.05  ? 471  TYR B CD1   1 
ATOM   7700 C CD2   . TYR B 1 471 ? -11.222 38.725  -8.858  1.00 47.81  ? 471  TYR B CD2   1 
ATOM   7701 C CE1   . TYR B 1 471 ? -9.450  37.088  -10.215 1.00 56.79  ? 471  TYR B CE1   1 
ATOM   7702 C CE2   . TYR B 1 471 ? -10.178 38.123  -8.173  1.00 53.39  ? 471  TYR B CE2   1 
ATOM   7703 C CZ    . TYR B 1 471 ? -9.293  37.302  -8.854  1.00 57.90  ? 471  TYR B CZ    1 
ATOM   7704 O OH    . TYR B 1 471 ? -8.264  36.717  -8.178  1.00 66.53  ? 471  TYR B OH    1 
ATOM   7705 N N     . ARG B 1 472 ? -15.138 38.314  -9.033  1.00 30.53  ? 472  ARG B N     1 
ATOM   7706 C CA    . ARG B 1 472 ? -15.649 37.939  -7.690  1.00 32.39  ? 472  ARG B CA    1 
ATOM   7707 C C     . ARG B 1 472 ? -17.058 38.515  -7.525  1.00 36.83  ? 472  ARG B C     1 
ATOM   7708 O O     . ARG B 1 472 ? -17.283 39.663  -7.964  1.00 36.56  ? 472  ARG B O     1 
ATOM   7709 C CB    . ARG B 1 472 ? -14.695 38.525  -6.649  1.00 31.76  ? 472  ARG B CB    1 
ATOM   7710 C CG    . ARG B 1 472 ? -14.891 38.007  -5.235  1.00 32.70  ? 472  ARG B CG    1 
ATOM   7711 C CD    . ARG B 1 472 ? -13.766 38.548  -4.386  1.00 34.22  ? 472  ARG B CD    1 
ATOM   7712 N NE    . ARG B 1 472 ? -13.891 38.250  -2.962  1.00 35.24  ? 472  ARG B NE    1 
ATOM   7713 C CZ    . ARG B 1 472 ? -13.182 38.847  -2.011  1.00 32.74  ? 472  ARG B CZ    1 
ATOM   7714 N NH1   . ARG B 1 472 ? -12.324 39.809  -2.319  1.00 33.81  ? 472  ARG B NH1   1 
ATOM   7715 N NH2   . ARG B 1 472 ? -13.331 38.481  -0.750  1.00 34.28  ? 472  ARG B NH2   1 
ATOM   7716 N N     . THR B 1 473 ? -18.004 37.789  -6.938  1.00 36.01  ? 473  THR B N     1 
ATOM   7717 C CA    . THR B 1 473 ? -19.394 38.301  -6.901  1.00 34.53  ? 473  THR B CA    1 
ATOM   7718 C C     . THR B 1 473 ? -20.166 37.730  -5.708  1.00 34.56  ? 473  THR B C     1 
ATOM   7719 O O     . THR B 1 473 ? -19.695 36.776  -5.050  1.00 34.95  ? 473  THR B O     1 
ATOM   7720 C CB    . THR B 1 473 ? -20.108 38.005  -8.228  1.00 35.17  ? 473  THR B CB    1 
ATOM   7721 O OG1   . THR B 1 473 ? -21.251 38.869  -8.347  1.00 34.29  ? 473  THR B OG1   1 
ATOM   7722 C CG2   . THR B 1 473 ? -20.483 36.546  -8.340  1.00 34.40  ? 473  THR B CG2   1 
ATOM   7723 N N     . HIS B 1 474 ? -21.340 38.299  -5.485  1.00 35.40  ? 474  HIS B N     1 
ATOM   7724 C CA    . HIS B 1 474 ? -22.255 37.959  -4.372  1.00 35.47  ? 474  HIS B CA    1 
ATOM   7725 C C     . HIS B 1 474 ? -22.897 36.598  -4.652  1.00 34.83  ? 474  HIS B C     1 
ATOM   7726 O O     . HIS B 1 474 ? -23.095 36.272  -5.850  1.00 32.23  ? 474  HIS B O     1 
ATOM   7727 C CB    . HIS B 1 474 ? -23.275 39.087  -4.246  1.00 37.31  ? 474  HIS B CB    1 
ATOM   7728 C CG    . HIS B 1 474 ? -24.155 38.974  -3.054  1.00 36.61  ? 474  HIS B CG    1 
ATOM   7729 N ND1   . HIS B 1 474 ? -25.140 38.040  -2.984  1.00 35.24  ? 474  HIS B ND1   1 
ATOM   7730 C CD2   . HIS B 1 474 ? -24.227 39.692  -1.916  1.00 37.43  ? 474  HIS B CD2   1 
ATOM   7731 C CE1   . HIS B 1 474 ? -25.787 38.163  -1.850  1.00 35.39  ? 474  HIS B CE1   1 
ATOM   7732 N NE2   . HIS B 1 474 ? -25.241 39.153  -1.170  1.00 36.61  ? 474  HIS B NE2   1 
ATOM   7733 N N     . ASN B 1 475 ? -23.223 35.858  -3.586  1.00 35.36  ? 475  ASN B N     1 
ATOM   7734 C CA    . ASN B 1 475 ? -24.102 34.653  -3.590  1.00 35.71  ? 475  ASN B CA    1 
ATOM   7735 C C     . ASN B 1 475 ? -25.222 34.743  -4.640  1.00 37.06  ? 475  ASN B C     1 
ATOM   7736 O O     . ASN B 1 475 ? -25.431 33.743  -5.369  1.00 40.09  ? 475  ASN B O     1 
ATOM   7737 C CB    . ASN B 1 475 ? -24.747 34.450  -2.215  1.00 36.44  ? 475  ASN B CB    1 
ATOM   7738 C CG    . ASN B 1 475 ? -23.766 33.895  -1.202  1.00 38.58  ? 475  ASN B CG    1 
ATOM   7739 O OD1   . ASN B 1 475 ? -22.802 33.212  -1.570  1.00 37.30  ? 475  ASN B OD1   1 
ATOM   7740 N ND2   . ASN B 1 475 ? -23.998 34.168  0.073   1.00 33.53  ? 475  ASN B ND2   1 
ATOM   7741 N N     . ALA B 1 476 ? -25.966 35.857  -4.664  1.00 35.14  ? 476  ALA B N     1 
ATOM   7742 C CA    . ALA B 1 476 ? -27.158 36.076  -5.519  1.00 36.07  ? 476  ALA B CA    1 
ATOM   7743 C C     . ALA B 1 476 ? -26.751 36.102  -6.991  1.00 34.31  ? 476  ALA B C     1 
ATOM   7744 O O     . ALA B 1 476 ? -27.623 35.892  -7.822  1.00 33.36  ? 476  ALA B O     1 
ATOM   7745 C CB    . ALA B 1 476 ? -27.865 37.362  -5.161  1.00 39.40  ? 476  ALA B CB    1 
ATOM   7746 N N     . LEU B 1 477 ? -25.480 36.358  -7.298  1.00 36.29  ? 477  LEU B N     1 
ATOM   7747 C CA    . LEU B 1 477 ? -25.029 36.601  -8.692  1.00 35.98  ? 477  LEU B CA    1 
ATOM   7748 C C     . LEU B 1 477 ? -24.159 35.454  -9.211  1.00 35.75  ? 477  LEU B C     1 
ATOM   7749 O O     . LEU B 1 477 ? -23.809 35.489  -10.421 1.00 35.40  ? 477  LEU B O     1 
ATOM   7750 C CB    . LEU B 1 477 ? -24.274 37.926  -8.721  1.00 35.68  ? 477  LEU B CB    1 
ATOM   7751 C CG    . LEU B 1 477 ? -25.094 39.159  -8.333  1.00 38.71  ? 477  LEU B CG    1 
ATOM   7752 C CD1   . LEU B 1 477 ? -24.186 40.351  -8.059  1.00 43.03  ? 477  LEU B CD1   1 
ATOM   7753 C CD2   . LEU B 1 477 ? -26.078 39.509  -9.429  1.00 36.60  ? 477  LEU B CD2   1 
ATOM   7754 N N     . MET B 1 478 ? -23.830 34.464  -8.375  1.00 34.65  ? 478  MET B N     1 
ATOM   7755 C CA    . MET B 1 478 ? -22.815 33.429  -8.739  1.00 33.42  ? 478  MET B CA    1 
ATOM   7756 C C     . MET B 1 478 ? -23.273 32.608  -9.959  1.00 34.64  ? 478  MET B C     1 
ATOM   7757 O O     . MET B 1 478 ? -22.438 32.321  -10.841 1.00 34.71  ? 478  MET B O     1 
ATOM   7758 C CB    . MET B 1 478 ? -22.527 32.495  -7.563  1.00 31.03  ? 478  MET B CB    1 
ATOM   7759 C CG    . MET B 1 478 ? -21.664 33.149  -6.527  1.00 31.30  ? 478  MET B CG    1 
ATOM   7760 S SD    . MET B 1 478 ? -21.526 32.161  -5.054  1.00 32.03  ? 478  MET B SD    1 
ATOM   7761 C CE    . MET B 1 478 ? -20.553 33.309  -4.086  1.00 33.02  ? 478  MET B CE    1 
ATOM   7762 N N     . ASP B 1 479 ? -24.535 32.198  -10.000 1.00 31.65  ? 479  ASP B N     1 
ATOM   7763 C CA    . ASP B 1 479 ? -25.071 31.412  -11.145 1.00 32.06  ? 479  ASP B CA    1 
ATOM   7764 C C     . ASP B 1 479 ? -24.938 32.246  -12.424 1.00 28.82  ? 479  ASP B C     1 
ATOM   7765 O O     . ASP B 1 479 ? -24.502 31.699  -13.469 1.00 32.86  ? 479  ASP B O     1 
ATOM   7766 C CB    . ASP B 1 479 ? -26.528 30.984  -10.924 1.00 32.94  ? 479  ASP B CB    1 
ATOM   7767 C CG    . ASP B 1 479 ? -26.722 29.866  -9.920  1.00 37.36  ? 479  ASP B CG    1 
ATOM   7768 O OD1   . ASP B 1 479 ? -25.761 29.060  -9.744  1.00 35.85  ? 479  ASP B OD1   1 
ATOM   7769 O OD2   . ASP B 1 479 ? -27.848 29.794  -9.324  1.00 36.89  ? 479  ASP B OD2   1 
ATOM   7770 N N     . GLN B 1 480 ? -25.316 33.521  -12.361 1.00 31.51  ? 480  GLN B N     1 
ATOM   7771 C CA    . GLN B 1 480 ? -25.337 34.391  -13.558 1.00 32.28  ? 480  GLN B CA    1 
ATOM   7772 C C     . GLN B 1 480 ? -23.891 34.566  -14.022 1.00 32.23  ? 480  GLN B C     1 
ATOM   7773 O O     . GLN B 1 480 ? -23.618 34.468  -15.248 1.00 28.99  ? 480  GLN B O     1 
ATOM   7774 C CB    . GLN B 1 480 ? -26.046 35.710  -13.271 1.00 29.37  ? 480  GLN B CB    1 
ATOM   7775 C CG    . GLN B 1 480 ? -26.107 36.585  -14.509 1.00 32.48  ? 480  GLN B CG    1 
ATOM   7776 C CD    . GLN B 1 480 ? -26.498 38.020  -14.254 1.00 36.34  ? 480  GLN B CD    1 
ATOM   7777 O OE1   . GLN B 1 480 ? -26.986 38.378  -13.175 1.00 35.06  ? 480  GLN B OE1   1 
ATOM   7778 N NE2   . GLN B 1 480 ? -26.276 38.850  -15.265 1.00 31.70  ? 480  GLN B NE2   1 
ATOM   7779 N N     . VAL B 1 481 ? -22.981 34.814  -13.080 1.00 33.59  ? 481  VAL B N     1 
ATOM   7780 C CA    . VAL B 1 481 ? -21.562 35.113  -13.429 1.00 31.41  ? 481  VAL B CA    1 
ATOM   7781 C C     . VAL B 1 481 ? -20.949 33.857  -14.042 1.00 31.79  ? 481  VAL B C     1 
ATOM   7782 O O     . VAL B 1 481 ? -20.384 33.971  -15.142 1.00 34.09  ? 481  VAL B O     1 
ATOM   7783 C CB    . VAL B 1 481 ? -20.780 35.680  -12.237 1.00 30.91  ? 481  VAL B CB    1 
ATOM   7784 C CG1   . VAL B 1 481 ? -19.282 35.689  -12.481 1.00 29.39  ? 481  VAL B CG1   1 
ATOM   7785 C CG2   . VAL B 1 481 ? -21.262 37.089  -11.923 1.00 31.82  ? 481  VAL B CG2   1 
ATOM   7786 N N     . MET B 1 482 ? -21.104 32.687  -13.416 1.00 33.91  ? 482  MET B N     1 
ATOM   7787 C CA    . MET B 1 482 ? -20.579 31.432  -14.020 1.00 30.00  ? 482  MET B CA    1 
ATOM   7788 C C     . MET B 1 482 ? -21.175 31.242  -15.422 1.00 32.39  ? 482  MET B C     1 
ATOM   7789 O O     . MET B 1 482 ? -20.433 30.780  -16.310 1.00 32.07  ? 482  MET B O     1 
ATOM   7790 C CB    . MET B 1 482 ? -20.872 30.209  -13.150 1.00 31.19  ? 482  MET B CB    1 
ATOM   7791 C CG    . MET B 1 482 ? -20.187 28.938  -13.627 1.00 31.51  ? 482  MET B CG    1 
ATOM   7792 S SD    . MET B 1 482 ? -18.436 29.153  -14.133 1.00 34.03  ? 482  MET B SD    1 
ATOM   7793 C CE    . MET B 1 482 ? -17.610 28.905  -12.570 1.00 29.75  ? 482  MET B CE    1 
ATOM   7794 N N     . GLY B 1 483 ? -22.457 31.596  -15.628 1.00 33.16  ? 483  GLY B N     1 
ATOM   7795 C CA    . GLY B 1 483 ? -23.162 31.472  -16.924 1.00 32.26  ? 483  GLY B CA    1 
ATOM   7796 C C     . GLY B 1 483 ? -22.546 32.332  -18.023 1.00 30.38  ? 483  GLY B C     1 
ATOM   7797 O O     . GLY B 1 483 ? -22.640 31.944  -19.220 1.00 37.08  ? 483  GLY B O     1 
ATOM   7798 N N     . THR B 1 484 ? -21.870 33.433  -17.667 1.00 30.70  ? 484  THR B N     1 
ATOM   7799 C CA    . THR B 1 484 ? -21.189 34.307  -18.669 1.00 31.43  ? 484  THR B CA    1 
ATOM   7800 C C     . THR B 1 484 ? -19.915 33.620  -19.198 1.00 32.78  ? 484  THR B C     1 
ATOM   7801 O O     . THR B 1 484 ? -19.463 33.966  -20.359 1.00 30.71  ? 484  THR B O     1 
ATOM   7802 C CB    . THR B 1 484 ? -20.884 35.707  -18.115 1.00 31.39  ? 484  THR B CB    1 
ATOM   7803 O OG1   . THR B 1 484 ? -19.917 35.600  -17.064 1.00 31.34  ? 484  THR B OG1   1 
ATOM   7804 C CG2   . THR B 1 484 ? -22.145 36.386  -17.636 1.00 32.51  ? 484  THR B CG2   1 
ATOM   7805 N N     . TYR B 1 485 ? -19.324 32.728  -18.394 1.00 31.42  ? 485  TYR B N     1 
ATOM   7806 C CA    . TYR B 1 485 ? -18.027 32.070  -18.724 1.00 32.51  ? 485  TYR B CA    1 
ATOM   7807 C C     . TYR B 1 485 ? -18.331 30.803  -19.530 1.00 32.71  ? 485  TYR B C     1 
ATOM   7808 O O     . TYR B 1 485 ? -17.854 29.760  -19.140 1.00 27.49  ? 485  TYR B O     1 
ATOM   7809 C CB    . TYR B 1 485 ? -17.209 31.800  -17.454 1.00 31.23  ? 485  TYR B CB    1 
ATOM   7810 C CG    . TYR B 1 485 ? -16.565 33.034  -16.873 1.00 30.09  ? 485  TYR B CG    1 
ATOM   7811 C CD1   . TYR B 1 485 ? -15.306 33.436  -17.282 1.00 30.97  ? 485  TYR B CD1   1 
ATOM   7812 C CD2   . TYR B 1 485 ? -17.220 33.831  -15.941 1.00 29.81  ? 485  TYR B CD2   1 
ATOM   7813 C CE1   . TYR B 1 485 ? -14.705 34.583  -16.778 1.00 33.64  ? 485  TYR B CE1   1 
ATOM   7814 C CE2   . TYR B 1 485 ? -16.635 34.986  -15.434 1.00 29.43  ? 485  TYR B CE2   1 
ATOM   7815 C CZ    . TYR B 1 485 ? -15.370 35.362  -15.852 1.00 30.36  ? 485  TYR B CZ    1 
ATOM   7816 O OH    . TYR B 1 485 ? -14.765 36.489  -15.385 1.00 29.41  ? 485  TYR B OH    1 
ATOM   7817 N N     . ASN B 1 486 ? -19.102 30.898  -20.625 1.00 32.17  ? 486  ASN B N     1 
ATOM   7818 C CA    . ASN B 1 486 ? -19.766 29.699  -21.212 1.00 32.55  ? 486  ASN B CA    1 
ATOM   7819 C C     . ASN B 1 486 ? -19.142 29.320  -22.547 1.00 30.67  ? 486  ASN B C     1 
ATOM   7820 O O     . ASN B 1 486 ? -19.819 28.622  -23.346 1.00 30.78  ? 486  ASN B O     1 
ATOM   7821 C CB    . ASN B 1 486 ? -21.271 29.855  -21.413 1.00 36.05  ? 486  ASN B CB    1 
ATOM   7822 C CG    . ASN B 1 486 ? -21.693 31.180  -22.004 1.00 36.68  ? 486  ASN B CG    1 
ATOM   7823 O OD1   . ASN B 1 486 ? -20.887 32.000  -22.427 1.00 35.67  ? 486  ASN B OD1   1 
ATOM   7824 N ND2   . ASN B 1 486 ? -22.988 31.405  -21.985 1.00 45.97  ? 486  ASN B ND2   1 
ATOM   7825 N N     . TRP B 1 487 ? -17.878 29.670  -22.754 1.00 28.21  ? 487  TRP B N     1 
ATOM   7826 C CA    . TRP B 1 487 ? -17.155 29.267  -23.978 1.00 30.06  ? 487  TRP B CA    1 
ATOM   7827 C C     . TRP B 1 487 ? -17.390 27.776  -24.207 1.00 29.28  ? 487  TRP B C     1 
ATOM   7828 O O     . TRP B 1 487 ? -17.403 27.016  -23.234 1.00 27.91  ? 487  TRP B O     1 
ATOM   7829 C CB    . TRP B 1 487 ? -15.664 29.568  -23.861 1.00 31.52  ? 487  TRP B CB    1 
ATOM   7830 C CG    . TRP B 1 487 ? -14.948 29.354  -25.157 1.00 28.55  ? 487  TRP B CG    1 
ATOM   7831 C CD1   . TRP B 1 487 ? -14.754 30.279  -26.142 1.00 29.51  ? 487  TRP B CD1   1 
ATOM   7832 C CD2   . TRP B 1 487 ? -14.309 28.141  -25.593 1.00 27.69  ? 487  TRP B CD2   1 
ATOM   7833 N NE1   . TRP B 1 487 ? -14.039 29.721  -27.169 1.00 29.24  ? 487  TRP B NE1   1 
ATOM   7834 C CE2   . TRP B 1 487 ? -13.756 28.410  -26.861 1.00 28.17  ? 487  TRP B CE2   1 
ATOM   7835 C CE3   . TRP B 1 487 ? -14.135 26.869  -25.026 1.00 28.05  ? 487  TRP B CE3   1 
ATOM   7836 C CZ2   . TRP B 1 487 ? -13.055 27.439  -27.580 1.00 30.39  ? 487  TRP B CZ2   1 
ATOM   7837 C CZ3   . TRP B 1 487 ? -13.454 25.914  -25.739 1.00 26.98  ? 487  TRP B CZ3   1 
ATOM   7838 C CH2   . TRP B 1 487 ? -12.928 26.192  -27.003 1.00 29.18  ? 487  TRP B CH2   1 
ATOM   7839 N N     . GLY B 1 488 ? -17.561 27.378  -25.455 1.00 27.05  ? 488  GLY B N     1 
ATOM   7840 C CA    . GLY B 1 488 ? -17.663 25.963  -25.831 1.00 28.75  ? 488  GLY B CA    1 
ATOM   7841 C C     . GLY B 1 488 ? -18.824 25.278  -25.151 1.00 29.43  ? 488  GLY B C     1 
ATOM   7842 O O     . GLY B 1 488 ? -18.611 24.160  -24.623 1.00 28.83  ? 488  GLY B O     1 
ATOM   7843 N N     . ASP B 1 489 ? -19.997 25.927  -25.149 1.00 34.81  ? 489  ASP B N     1 
ATOM   7844 C CA    . ASP B 1 489 ? -21.277 25.360  -24.642 1.00 36.17  ? 489  ASP B CA    1 
ATOM   7845 C C     . ASP B 1 489 ? -21.153 25.005  -23.151 1.00 34.03  ? 489  ASP B C     1 
ATOM   7846 O O     . ASP B 1 489 ? -21.550 23.880  -22.771 1.00 34.74  ? 489  ASP B O     1 
ATOM   7847 C CB    . ASP B 1 489 ? -21.655 24.144  -25.498 1.00 40.20  ? 489  ASP B CB    1 
ATOM   7848 C CG    . ASP B 1 489 ? -23.046 23.582  -25.265 1.00 45.89  ? 489  ASP B CG    1 
ATOM   7849 O OD1   . ASP B 1 489 ? -23.916 24.328  -24.767 1.00 54.46  ? 489  ASP B OD1   1 
ATOM   7850 O OD2   . ASP B 1 489 ? -23.247 22.398  -25.592 1.00 58.70  ? 489  ASP B OD2   1 
ATOM   7851 N N     . GLY B 1 490 ? -20.646 25.918  -22.322 1.00 30.76  ? 490  GLY B N     1 
ATOM   7852 C CA    . GLY B 1 490 ? -20.624 25.739  -20.853 1.00 26.13  ? 490  GLY B CA    1 
ATOM   7853 C C     . GLY B 1 490 ? -19.524 24.783  -20.404 1.00 27.03  ? 490  GLY B C     1 
ATOM   7854 O O     . GLY B 1 490 ? -19.730 24.046  -19.398 1.00 27.03  ? 490  GLY B O     1 
ATOM   7855 N N     . ALA B 1 491 ? -18.387 24.756  -21.111 1.00 25.38  ? 491  ALA B N     1 
ATOM   7856 C CA    . ALA B 1 491 ? -17.363 23.698  -20.955 1.00 26.54  ? 491  ALA B CA    1 
ATOM   7857 C C     . ALA B 1 491 ? -16.703 23.858  -19.593 1.00 26.95  ? 491  ALA B C     1 
ATOM   7858 O O     . ALA B 1 491 ? -16.413 22.839  -18.979 1.00 27.05  ? 491  ALA B O     1 
ATOM   7859 C CB    . ALA B 1 491 ? -16.332 23.759  -22.043 1.00 28.55  ? 491  ALA B CB    1 
ATOM   7860 N N     . LEU B 1 492 ? -16.440 25.102  -19.174 1.00 29.86  ? 492  LEU B N     1 
ATOM   7861 C CA    . LEU B 1 492 ? -15.718 25.354  -17.906 1.00 29.29  ? 492  LEU B CA    1 
ATOM   7862 C C     . LEU B 1 492 ? -16.597 24.886  -16.729 1.00 31.30  ? 492  LEU B C     1 
ATOM   7863 O O     . LEU B 1 492 ? -16.088 24.161  -15.820 1.00 33.00  ? 492  LEU B O     1 
ATOM   7864 C CB    . LEU B 1 492 ? -15.314 26.824  -17.806 1.00 29.70  ? 492  LEU B CB    1 
ATOM   7865 C CG    . LEU B 1 492 ? -14.653 27.202  -16.483 1.00 30.33  ? 492  LEU B CG    1 
ATOM   7866 C CD1   . LEU B 1 492 ? -13.274 26.546  -16.382 1.00 29.60  ? 492  LEU B CD1   1 
ATOM   7867 C CD2   . LEU B 1 492 ? -14.563 28.699  -16.345 1.00 30.17  ? 492  LEU B CD2   1 
ATOM   7868 N N     . LEU B 1 493 ? -17.884 25.217  -16.716 1.00 30.99  ? 493  LEU B N     1 
ATOM   7869 C CA    . LEU B 1 493 ? -18.768 24.745  -15.613 1.00 29.76  ? 493  LEU B CA    1 
ATOM   7870 C C     . LEU B 1 493 ? -18.901 23.211  -15.652 1.00 29.04  ? 493  LEU B C     1 
ATOM   7871 O O     . LEU B 1 493 ? -18.922 22.575  -14.567 1.00 28.49  ? 493  LEU B O     1 
ATOM   7872 C CB    . LEU B 1 493 ? -20.131 25.438  -15.710 1.00 31.17  ? 493  LEU B CB    1 
ATOM   7873 C CG    . LEU B 1 493 ? -21.169 25.038  -14.662 1.00 30.45  ? 493  LEU B CG    1 
ATOM   7874 C CD1   . LEU B 1 493 ? -20.633 25.308  -13.269 1.00 30.11  ? 493  LEU B CD1   1 
ATOM   7875 C CD2   . LEU B 1 493 ? -22.481 25.808  -14.898 1.00 31.00  ? 493  LEU B CD2   1 
ATOM   7876 N N     . LYS B 1 494 ? -18.996 22.600  -16.831 1.00 29.64  ? 494  LYS B N     1 
ATOM   7877 C CA    . LYS B 1 494 ? -19.141 21.119  -16.913 1.00 31.16  ? 494  LYS B CA    1 
ATOM   7878 C C     . LYS B 1 494 ? -17.918 20.429  -16.295 1.00 30.49  ? 494  LYS B C     1 
ATOM   7879 O O     . LYS B 1 494 ? -18.089 19.452  -15.570 1.00 33.33  ? 494  LYS B O     1 
ATOM   7880 C CB    . LYS B 1 494 ? -19.355 20.659  -18.353 1.00 31.86  ? 494  LYS B CB    1 
ATOM   7881 C CG    . LYS B 1 494 ? -20.729 21.004  -18.895 1.00 37.19  ? 494  LYS B CG    1 
ATOM   7882 C CD    . LYS B 1 494 ? -20.939 20.558  -20.322 1.00 40.17  ? 494  LYS B CD    1 
ATOM   7883 C CE    . LYS B 1 494 ? -22.148 21.221  -20.948 1.00 41.63  ? 494  LYS B CE    1 
ATOM   7884 N NZ    . LYS B 1 494 ? -22.116 21.094  -22.415 1.00 41.05  ? 494  LYS B NZ    1 
ATOM   7885 N N     . PHE B 1 495 ? -16.725 20.925  -16.590 1.00 29.24  ? 495  PHE B N     1 
ATOM   7886 C CA    . PHE B 1 495 ? -15.461 20.474  -15.953 1.00 28.29  ? 495  PHE B CA    1 
ATOM   7887 C C     . PHE B 1 495 ? -15.568 20.580  -14.420 1.00 27.33  ? 495  PHE B C     1 
ATOM   7888 O O     . PHE B 1 495 ? -15.336 19.577  -13.738 1.00 28.16  ? 495  PHE B O     1 
ATOM   7889 C CB    . PHE B 1 495 ? -14.318 21.302  -16.542 1.00 29.26  ? 495  PHE B CB    1 
ATOM   7890 C CG    . PHE B 1 495 ? -13.042 21.211  -15.759 1.00 30.11  ? 495  PHE B CG    1 
ATOM   7891 C CD1   . PHE B 1 495 ? -12.212 20.116  -15.908 1.00 29.48  ? 495  PHE B CD1   1 
ATOM   7892 C CD2   . PHE B 1 495 ? -12.686 22.213  -14.876 1.00 31.47  ? 495  PHE B CD2   1 
ATOM   7893 C CE1   . PHE B 1 495 ? -11.043 20.018  -15.174 1.00 30.78  ? 495  PHE B CE1   1 
ATOM   7894 C CE2   . PHE B 1 495 ? -11.520 22.103  -14.134 1.00 36.51  ? 495  PHE B CE2   1 
ATOM   7895 C CZ    . PHE B 1 495 ? -10.696 21.010  -14.294 1.00 29.30  ? 495  PHE B CZ    1 
ATOM   7896 N N     . HIS B 1 496 ? -15.937 21.751  -13.896 1.00 30.28  ? 496  HIS B N     1 
ATOM   7897 C CA    . HIS B 1 496 ? -16.035 22.017  -12.436 1.00 28.06  ? 496  HIS B CA    1 
ATOM   7898 C C     . HIS B 1 496 ? -17.046 21.055  -11.804 1.00 29.61  ? 496  HIS B C     1 
ATOM   7899 O O     . HIS B 1 496 ? -16.788 20.590  -10.699 1.00 28.97  ? 496  HIS B O     1 
ATOM   7900 C CB    . HIS B 1 496 ? -16.419 23.465  -12.169 1.00 27.28  ? 496  HIS B CB    1 
ATOM   7901 C CG    . HIS B 1 496 ? -15.335 24.442  -12.432 1.00 29.94  ? 496  HIS B CG    1 
ATOM   7902 N ND1   . HIS B 1 496 ? -14.038 24.239  -11.991 1.00 31.56  ? 496  HIS B ND1   1 
ATOM   7903 C CD2   . HIS B 1 496 ? -15.363 25.658  -13.014 1.00 28.49  ? 496  HIS B CD2   1 
ATOM   7904 C CE1   . HIS B 1 496 ? -13.305 25.255  -12.361 1.00 31.77  ? 496  HIS B CE1   1 
ATOM   7905 N NE2   . HIS B 1 496 ? -14.091 26.143  -12.984 1.00 30.18  ? 496  HIS B NE2   1 
ATOM   7906 N N     . GLU B 1 497 ? -18.127 20.730  -12.512 1.00 30.20  ? 497  GLU B N     1 
ATOM   7907 C CA    . GLU B 1 497 ? -19.210 19.855  -11.997 1.00 32.97  ? 497  GLU B CA    1 
ATOM   7908 C C     . GLU B 1 497 ? -18.690 18.430  -11.871 1.00 28.75  ? 497  GLU B C     1 
ATOM   7909 O O     . GLU B 1 497 ? -19.063 17.777  -10.893 1.00 28.75  ? 497  GLU B O     1 
ATOM   7910 C CB    . GLU B 1 497 ? -20.459 19.898  -12.886 1.00 33.51  ? 497  GLU B CB    1 
ATOM   7911 C CG    . GLU B 1 497 ? -21.280 21.157  -12.698 1.00 33.80  ? 497  GLU B CG    1 
ATOM   7912 C CD    . GLU B 1 497 ? -22.274 21.446  -13.822 1.00 38.05  ? 497  GLU B CD    1 
ATOM   7913 O OE1   . GLU B 1 497 ? -22.206 20.764  -14.853 1.00 42.82  ? 497  GLU B OE1   1 
ATOM   7914 O OE2   . GLU B 1 497 ? -23.111 22.362  -13.659 1.00 37.83  ? 497  GLU B OE2   1 
ATOM   7915 N N     . ALA B 1 498 ? -17.921 17.965  -12.857 1.00 27.90  ? 498  ALA B N     1 
ATOM   7916 C CA    . ALA B 1 498 ? -17.336 16.603  -12.909 1.00 27.81  ? 498  ALA B CA    1 
ATOM   7917 C C     . ALA B 1 498 ? -16.350 16.428  -11.737 1.00 30.68  ? 498  ALA B C     1 
ATOM   7918 O O     . ALA B 1 498 ? -16.423 15.425  -11.053 1.00 34.90  ? 498  ALA B O     1 
ATOM   7919 C CB    . ALA B 1 498 ? -16.685 16.383  -14.255 1.00 28.17  ? 498  ALA B CB    1 
ATOM   7920 N N     . ILE B 1 499 ? -15.484 17.408  -11.491 1.00 31.66  ? 499  ILE B N     1 
ATOM   7921 C CA    . ILE B 1 499 ? -14.547 17.394  -10.333 1.00 32.37  ? 499  ILE B CA    1 
ATOM   7922 C C     . ILE B 1 499 ? -15.347 17.429  -9.019  1.00 31.93  ? 499  ILE B C     1 
ATOM   7923 O O     . ILE B 1 499 ? -15.047 16.619  -8.134  1.00 33.61  ? 499  ILE B O     1 
ATOM   7924 C CB    . ILE B 1 499 ? -13.521 18.526  -10.502 1.00 32.02  ? 499  ILE B CB    1 
ATOM   7925 C CG1   . ILE B 1 499 ? -12.435 18.049  -11.477 1.00 34.32  ? 499  ILE B CG1   1 
ATOM   7926 C CG2   . ILE B 1 499 ? -12.941 18.968  -9.171  1.00 30.74  ? 499  ILE B CG2   1 
ATOM   7927 C CD1   . ILE B 1 499 ? -11.606 19.146  -12.007 1.00 39.36  ? 499  ILE B CD1   1 
ATOM   7928 N N     . LYS B 1 500 ? -16.350 18.292  -8.917  1.00 31.36  ? 500  LYS B N     1 
ATOM   7929 C CA    . LYS B 1 500 ? -17.150 18.432  -7.676  1.00 36.10  ? 500  LYS B CA    1 
ATOM   7930 C C     . LYS B 1 500 ? -17.821 17.089  -7.368  1.00 33.85  ? 500  LYS B C     1 
ATOM   7931 O O     . LYS B 1 500 ? -17.700 16.625  -6.236  1.00 32.96  ? 500  LYS B O     1 
ATOM   7932 C CB    . LYS B 1 500 ? -18.138 19.588  -7.816  1.00 33.81  ? 500  LYS B CB    1 
ATOM   7933 C CG    . LYS B 1 500 ? -19.139 19.704  -6.675  1.00 35.22  ? 500  LYS B CG    1 
ATOM   7934 C CD    . LYS B 1 500 ? -18.479 19.919  -5.364  1.00 34.16  ? 500  LYS B CD    1 
ATOM   7935 C CE    . LYS B 1 500 ? -19.420 20.497  -4.335  1.00 33.18  ? 500  LYS B CE    1 
ATOM   7936 N NZ    . LYS B 1 500 ? -18.739 20.636  -3.036  1.00 33.69  ? 500  LYS B NZ    1 
ATOM   7937 N N     . ASP B 1 501 ? -18.455 16.472  -8.360  1.00 32.72  ? 501  ASP B N     1 
ATOM   7938 C CA    . ASP B 1 501 ? -19.183 15.189  -8.209  1.00 36.18  ? 501  ASP B CA    1 
ATOM   7939 C C     . ASP B 1 501 ? -18.188 14.074  -7.834  1.00 39.28  ? 501  ASP B C     1 
ATOM   7940 O O     . ASP B 1 501 ? -18.553 13.213  -7.019  1.00 42.85  ? 501  ASP B O     1 
ATOM   7941 C CB    . ASP B 1 501 ? -20.049 14.895  -9.436  1.00 36.39  ? 501  ASP B CB    1 
ATOM   7942 C CG    . ASP B 1 501 ? -21.326 15.724  -9.476  1.00 41.57  ? 501  ASP B CG    1 
ATOM   7943 O OD1   . ASP B 1 501 ? -21.695 16.296  -8.402  1.00 37.78  ? 501  ASP B OD1   1 
ATOM   7944 O OD2   . ASP B 1 501 ? -21.935 15.827  -10.591 1.00 38.76  ? 501  ASP B OD2   1 
ATOM   7945 N N     . ALA B 1 502 ? -16.968 14.096  -8.365  1.00 36.88  ? 502  ALA B N     1 
ATOM   7946 C CA    . ALA B 1 502 ? -15.933 13.089  -8.047  1.00 35.95  ? 502  ALA B CA    1 
ATOM   7947 C C     . ALA B 1 502 ? -15.456 13.232  -6.588  1.00 32.11  ? 502  ALA B C     1 
ATOM   7948 O O     . ALA B 1 502 ? -15.378 12.231  -5.926  1.00 35.21  ? 502  ALA B O     1 
ATOM   7949 C CB    . ALA B 1 502 ? -14.784 13.222  -9.002  1.00 34.49  ? 502  ALA B CB    1 
ATOM   7950 N N     . LEU B 1 503 ? -15.156 14.443  -6.126  1.00 31.66  ? 503  LEU B N     1 
ATOM   7951 C CA    . LEU B 1 503 ? -14.571 14.707  -4.787  1.00 31.83  ? 503  LEU B CA    1 
ATOM   7952 C C     . LEU B 1 503 ? -15.686 14.727  -3.734  1.00 32.85  ? 503  LEU B C     1 
ATOM   7953 O O     . LEU B 1 503 ? -15.417 14.380  -2.578  1.00 34.89  ? 503  LEU B O     1 
ATOM   7954 C CB    . LEU B 1 503 ? -13.860 16.056  -4.843  1.00 32.12  ? 503  LEU B CB    1 
ATOM   7955 C CG    . LEU B 1 503 ? -12.592 16.115  -5.697  1.00 32.59  ? 503  LEU B CG    1 
ATOM   7956 C CD1   . LEU B 1 503 ? -11.934 17.479  -5.581  1.00 34.08  ? 503  LEU B CD1   1 
ATOM   7957 C CD2   . LEU B 1 503 ? -11.632 15.018  -5.276  1.00 34.21  ? 503  LEU B CD2   1 
ATOM   7958 N N     . ASP B 1 504 ? -16.897 15.092  -4.150  1.00 28.63  ? 504  ASP B N     1 
ATOM   7959 C CA    . ASP B 1 504 ? -18.079 15.324  -3.276  1.00 30.60  ? 504  ASP B CA    1 
ATOM   7960 C C     . ASP B 1 504 ? -19.260 14.503  -3.782  1.00 30.36  ? 504  ASP B C     1 
ATOM   7961 O O     . ASP B 1 504 ? -20.290 15.034  -4.183  1.00 29.67  ? 504  ASP B O     1 
ATOM   7962 C CB    . ASP B 1 504 ? -18.398 16.812  -3.225  1.00 30.22  ? 504  ASP B CB    1 
ATOM   7963 C CG    . ASP B 1 504 ? -19.121 17.214  -1.967  1.00 31.89  ? 504  ASP B CG    1 
ATOM   7964 O OD1   . ASP B 1 504 ? -19.619 16.301  -1.260  1.00 33.37  ? 504  ASP B OD1   1 
ATOM   7965 O OD2   . ASP B 1 504 ? -19.164 18.429  -1.699  1.00 31.52  ? 504  ASP B OD2   1 
ATOM   7966 N N     . PRO B 1 505 ? -19.172 13.161  -3.740  1.00 33.94  ? 505  PRO B N     1 
ATOM   7967 C CA    . PRO B 1 505 ? -20.248 12.319  -4.263  1.00 36.27  ? 505  PRO B CA    1 
ATOM   7968 C C     . PRO B 1 505 ? -21.601 12.522  -3.559  1.00 39.43  ? 505  PRO B C     1 
ATOM   7969 O O     . PRO B 1 505 ? -22.610 12.274  -4.189  1.00 41.89  ? 505  PRO B O     1 
ATOM   7970 C CB    . PRO B 1 505 ? -19.765 10.881  -4.044  1.00 38.19  ? 505  PRO B CB    1 
ATOM   7971 C CG    . PRO B 1 505 ? -18.621 10.988  -3.038  1.00 37.65  ? 505  PRO B CG    1 
ATOM   7972 C CD    . PRO B 1 505 ? -18.063 12.394  -3.152  1.00 33.65  ? 505  PRO B CD    1 
ATOM   7973 N N     . ASN B 1 506 ? -21.589 12.995  -2.313  1.00 35.85  ? 506  ASN B N     1 
ATOM   7974 C CA    . ASN B 1 506 ? -22.803 13.229  -1.489  1.00 38.94  ? 506  ASN B CA    1 
ATOM   7975 C C     . ASN B 1 506 ? -23.202 14.703  -1.512  1.00 39.73  ? 506  ASN B C     1 
ATOM   7976 O O     . ASN B 1 506 ? -24.203 15.030  -0.853  1.00 37.86  ? 506  ASN B O     1 
ATOM   7977 C CB    . ASN B 1 506 ? -22.587 12.802  -0.034  1.00 37.83  ? 506  ASN B CB    1 
ATOM   7978 C CG    . ASN B 1 506 ? -22.381 11.312  0.093   1.00 38.75  ? 506  ASN B CG    1 
ATOM   7979 O OD1   . ASN B 1 506 ? -23.057 10.544  -0.582  1.00 39.58  ? 506  ASN B OD1   1 
ATOM   7980 N ND2   . ASN B 1 506 ? -21.407 10.910  0.896   1.00 40.29  ? 506  ASN B ND2   1 
ATOM   7981 N N     . GLY B 1 507 ? -22.452 15.561  -2.222  1.00 39.65  ? 507  GLY B N     1 
ATOM   7982 C CA    . GLY B 1 507 ? -22.851 16.961  -2.481  1.00 36.93  ? 507  GLY B CA    1 
ATOM   7983 C C     . GLY B 1 507 ? -23.002 17.764  -1.195  1.00 37.05  ? 507  GLY B C     1 
ATOM   7984 O O     . GLY B 1 507 ? -24.079 18.374  -0.982  1.00 34.23  ? 507  GLY B O     1 
ATOM   7985 N N     . ILE B 1 508 ? -21.925 17.821  -0.404  1.00 38.67  ? 508  ILE B N     1 
ATOM   7986 C CA    . ILE B 1 508 ? -21.902 18.370  0.984   1.00 38.41  ? 508  ILE B CA    1 
ATOM   7987 C C     . ILE B 1 508 ? -21.345 19.798  0.994   1.00 35.03  ? 508  ILE B C     1 
ATOM   7988 O O     . ILE B 1 508 ? -22.035 20.659  1.521   1.00 37.04  ? 508  ILE B O     1 
ATOM   7989 C CB    . ILE B 1 508 ? -21.102 17.415  1.891   1.00 36.27  ? 508  ILE B CB    1 
ATOM   7990 C CG1   . ILE B 1 508 ? -21.641 15.981  1.805   1.00 41.09  ? 508  ILE B CG1   1 
ATOM   7991 C CG2   . ILE B 1 508 ? -21.063 17.927  3.313   1.00 36.52  ? 508  ILE B CG2   1 
ATOM   7992 C CD1   . ILE B 1 508 ? -23.107 15.811  2.199   1.00 38.96  ? 508  ILE B CD1   1 
ATOM   7993 N N     . ILE B 1 509 ? -20.142 20.050  0.456   1.00 34.53  ? 509  ILE B N     1 
ATOM   7994 C CA    . ILE B 1 509 ? -19.404 21.325  0.722   1.00 35.29  ? 509  ILE B CA    1 
ATOM   7995 C C     . ILE B 1 509 ? -19.989 22.466  -0.123  1.00 34.21  ? 509  ILE B C     1 
ATOM   7996 O O     . ILE B 1 509 ? -20.091 22.308  -1.338  1.00 38.04  ? 509  ILE B O     1 
ATOM   7997 C CB    . ILE B 1 509 ? -17.890 21.175  0.491   1.00 33.53  ? 509  ILE B CB    1 
ATOM   7998 C CG1   . ILE B 1 509 ? -17.272 20.059  1.335   1.00 36.20  ? 509  ILE B CG1   1 
ATOM   7999 C CG2   . ILE B 1 509 ? -17.194 22.495  0.739   1.00 33.00  ? 509  ILE B CG2   1 
ATOM   8000 C CD1   . ILE B 1 509 ? -17.398 20.258  2.822   1.00 34.71  ? 509  ILE B CD1   1 
ATOM   8001 N N     . ALA B 1 510 ? -20.347 23.562  0.544   1.00 36.26  ? 510  ALA B N     1 
ATOM   8002 C CA    . ALA B 1 510 ? -20.791 24.875  0.015   1.00 34.62  ? 510  ALA B CA    1 
ATOM   8003 C C     . ALA B 1 510 ? -21.424 24.764  -1.376  1.00 39.50  ? 510  ALA B C     1 
ATOM   8004 O O     . ALA B 1 510 ? -20.947 25.390  -2.324  1.00 37.57  ? 510  ALA B O     1 
ATOM   8005 C CB    . ALA B 1 510 ? -19.610 25.815  0.029   1.00 35.55  ? 510  ALA B CB    1 
ATOM   8006 N N     . PRO B 1 511 ? -22.583 24.072  -1.521  1.00 37.48  ? 511  PRO B N     1 
ATOM   8007 C CA    . PRO B 1 511 ? -23.221 23.887  -2.826  1.00 36.05  ? 511  PRO B CA    1 
ATOM   8008 C C     . PRO B 1 511 ? -23.554 25.229  -3.480  1.00 31.83  ? 511  PRO B C     1 
ATOM   8009 O O     . PRO B 1 511 ? -24.048 26.122  -2.796  1.00 30.74  ? 511  PRO B O     1 
ATOM   8010 C CB    . PRO B 1 511 ? -24.489 23.062  -2.527  1.00 35.36  ? 511  PRO B CB    1 
ATOM   8011 C CG    . PRO B 1 511 ? -24.162 22.382  -1.209  1.00 37.47  ? 511  PRO B CG    1 
ATOM   8012 C CD    . PRO B 1 511 ? -23.359 23.425  -0.446  1.00 39.28  ? 511  PRO B CD    1 
ATOM   8013 N N     . GLY B 1 512 ? -23.179 25.351  -4.758  1.00 31.19  ? 512  GLY B N     1 
ATOM   8014 C CA    . GLY B 1 512 ? -23.461 26.508  -5.613  1.00 29.14  ? 512  GLY B CA    1 
ATOM   8015 C C     . GLY B 1 512 ? -22.396 27.586  -5.523  1.00 30.86  ? 512  GLY B C     1 
ATOM   8016 O O     . GLY B 1 512 ? -22.497 28.551  -6.287  1.00 29.74  ? 512  GLY B O     1 
ATOM   8017 N N     . LYS B 1 513 ? -21.409 27.465  -4.636  1.00 31.33  ? 513  LYS B N     1 
ATOM   8018 C CA    . LYS B 1 513 ? -20.260 28.410  -4.640  1.00 31.93  ? 513  LYS B CA    1 
ATOM   8019 C C     . LYS B 1 513 ? -19.738 28.556  -6.076  1.00 28.18  ? 513  LYS B C     1 
ATOM   8020 O O     . LYS B 1 513 ? -19.550 27.535  -6.747  1.00 28.15  ? 513  LYS B O     1 
ATOM   8021 C CB    . LYS B 1 513 ? -19.188 27.922  -3.670  1.00 35.92  ? 513  LYS B CB    1 
ATOM   8022 C CG    . LYS B 1 513 ? -17.909 28.742  -3.646  1.00 36.22  ? 513  LYS B CG    1 
ATOM   8023 C CD    . LYS B 1 513 ? -18.116 30.218  -3.388  1.00 36.81  ? 513  LYS B CD    1 
ATOM   8024 C CE    . LYS B 1 513 ? -16.801 30.965  -3.411  1.00 36.23  ? 513  LYS B CE    1 
ATOM   8025 N NZ    . LYS B 1 513 ? -16.963 32.434  -3.275  1.00 36.62  ? 513  LYS B NZ    1 
ATOM   8026 N N     . SER B 1 514 ? -19.602 29.785  -6.570  1.00 28.11  ? 514  SER B N     1 
ATOM   8027 C CA    . SER B 1 514 ? -19.149 30.087  -7.955  1.00 31.26  ? 514  SER B CA    1 
ATOM   8028 C C     . SER B 1 514 ? -20.062 29.427  -9.002  1.00 30.27  ? 514  SER B C     1 
ATOM   8029 O O     . SER B 1 514 ? -19.625 29.275  -10.156 1.00 28.22  ? 514  SER B O     1 
ATOM   8030 C CB    . SER B 1 514 ? -17.712 29.654  -8.130  1.00 30.89  ? 514  SER B CB    1 
ATOM   8031 O OG    . SER B 1 514 ? -16.905 30.236  -7.122  1.00 28.26  ? 514  SER B OG    1 
ATOM   8032 N N     . GLY B 1 515 ? -21.289 29.062  -8.639  1.00 27.78  ? 515  GLY B N     1 
ATOM   8033 C CA    . GLY B 1 515 ? -22.255 28.452  -9.582  1.00 30.39  ? 515  GLY B CA    1 
ATOM   8034 C C     . GLY B 1 515 ? -22.030 26.962  -9.764  1.00 31.22  ? 515  GLY B C     1 
ATOM   8035 O O     . GLY B 1 515 ? -22.677 26.369  -10.661 1.00 35.42  ? 515  GLY B O     1 
ATOM   8036 N N     . VAL B 1 516 ? -21.135 26.367  -8.972  1.00 30.86  ? 516  VAL B N     1 
ATOM   8037 C CA    . VAL B 1 516 ? -20.824 24.907  -9.076  1.00 31.94  ? 516  VAL B CA    1 
ATOM   8038 C C     . VAL B 1 516 ? -21.698 24.152  -8.075  1.00 31.85  ? 516  VAL B C     1 
ATOM   8039 O O     . VAL B 1 516 ? -21.448 24.270  -6.834  1.00 31.38  ? 516  VAL B O     1 
ATOM   8040 C CB    . VAL B 1 516 ? -19.337 24.569  -8.879  1.00 33.13  ? 516  VAL B CB    1 
ATOM   8041 C CG1   . VAL B 1 516 ? -19.095 23.088  -9.125  1.00 33.71  ? 516  VAL B CG1   1 
ATOM   8042 C CG2   . VAL B 1 516 ? -18.425 25.396  -9.772  1.00 32.18  ? 516  VAL B CG2   1 
ATOM   8043 N N     . TRP B 1 517 ? -22.676 23.415  -8.606  1.00 29.81  ? 517  TRP B N     1 
ATOM   8044 C CA    . TRP B 1 517 ? -23.667 22.630  -7.826  1.00 29.72  ? 517  TRP B CA    1 
ATOM   8045 C C     . TRP B 1 517 ? -23.341 21.152  -7.938  1.00 28.59  ? 517  TRP B C     1 
ATOM   8046 O O     . TRP B 1 517 ? -23.185 20.621  -9.043  1.00 30.49  ? 517  TRP B O     1 
ATOM   8047 C CB    . TRP B 1 517 ? -25.095 22.874  -8.317  1.00 29.09  ? 517  TRP B CB    1 
ATOM   8048 C CG    . TRP B 1 517 ? -25.582 24.259  -8.071  1.00 30.76  ? 517  TRP B CG    1 
ATOM   8049 C CD1   . TRP B 1 517 ? -25.582 25.310  -8.941  1.00 30.40  ? 517  TRP B CD1   1 
ATOM   8050 C CD2   . TRP B 1 517 ? -26.149 24.739  -6.846  1.00 28.73  ? 517  TRP B CD2   1 
ATOM   8051 N NE1   . TRP B 1 517 ? -26.086 26.423  -8.320  1.00 31.65  ? 517  TRP B NE1   1 
ATOM   8052 C CE2   . TRP B 1 517 ? -26.454 26.097  -7.038  1.00 29.18  ? 517  TRP B CE2   1 
ATOM   8053 C CE3   . TRP B 1 517 ? -26.400 24.149  -5.605  1.00 30.74  ? 517  TRP B CE3   1 
ATOM   8054 C CZ2   . TRP B 1 517 ? -27.034 26.870  -6.037  1.00 28.56  ? 517  TRP B CZ2   1 
ATOM   8055 C CZ3   . TRP B 1 517 ? -26.962 24.911  -4.610  1.00 31.12  ? 517  TRP B CZ3   1 
ATOM   8056 C CH2   . TRP B 1 517 ? -27.273 26.256  -4.825  1.00 31.89  ? 517  TRP B CH2   1 
ATOM   8057 N N     . PRO B 1 518 ? -23.362 20.419  -6.815  1.00 28.74  ? 518  PRO B N     1 
ATOM   8058 C CA    . PRO B 1 518 ? -23.218 18.977  -6.877  1.00 32.07  ? 518  PRO B CA    1 
ATOM   8059 C C     . PRO B 1 518 ? -24.536 18.436  -7.453  1.00 35.11  ? 518  PRO B C     1 
ATOM   8060 O O     . PRO B 1 518 ? -25.536 19.173  -7.396  1.00 34.73  ? 518  PRO B O     1 
ATOM   8061 C CB    . PRO B 1 518 ? -22.922 18.629  -5.413  1.00 34.31  ? 518  PRO B CB    1 
ATOM   8062 C CG    . PRO B 1 518 ? -23.713 19.662  -4.635  1.00 35.02  ? 518  PRO B CG    1 
ATOM   8063 C CD    . PRO B 1 518 ? -23.634 20.925  -5.467  1.00 30.57  ? 518  PRO B CD    1 
ATOM   8064 N N     . ALA B 1 519 ? -24.518 17.190  -7.957  1.00 36.66  ? 519  ALA B N     1 
ATOM   8065 C CA    . ALA B 1 519 ? -25.627 16.513  -8.675  1.00 35.81  ? 519  ALA B CA    1 
ATOM   8066 C C     . ALA B 1 519 ? -26.948 16.634  -7.901  1.00 41.30  ? 519  ALA B C     1 
ATOM   8067 O O     . ALA B 1 519 ? -27.936 16.971  -8.540  1.00 44.82  ? 519  ALA B O     1 
ATOM   8068 C CB    . ALA B 1 519 ? -25.289 15.067  -8.938  1.00 35.89  ? 519  ALA B CB    1 
ATOM   8069 N N     . ARG B 1 520 ? -26.992 16.359  -6.592  1.00 41.79  ? 520  ARG B N     1 
ATOM   8070 C CA    . ARG B 1 520 ? -28.286 16.323  -5.837  1.00 40.56  ? 520  ARG B CA    1 
ATOM   8071 C C     . ARG B 1 520 ? -28.997 17.695  -5.891  1.00 43.94  ? 520  ARG B C     1 
ATOM   8072 O O     . ARG B 1 520 ? -30.238 17.730  -5.667  1.00 43.38  ? 520  ARG B O     1 
ATOM   8073 C CB    . ARG B 1 520 ? -28.073 15.868  -4.391  1.00 37.60  ? 520  ARG B CB    1 
ATOM   8074 C CG    . ARG B 1 520 ? -27.474 16.935  -3.486  1.00 38.92  ? 520  ARG B CG    1 
ATOM   8075 C CD    . ARG B 1 520 ? -26.785 16.437  -2.223  1.00 40.36  ? 520  ARG B CD    1 
ATOM   8076 N NE    . ARG B 1 520 ? -27.701 16.392  -1.104  1.00 46.08  ? 520  ARG B NE    1 
ATOM   8077 C CZ    . ARG B 1 520 ? -27.456 16.753  0.156   1.00 46.43  ? 520  ARG B CZ    1 
ATOM   8078 N NH1   . ARG B 1 520 ? -26.286 17.237  0.544   1.00 48.93  ? 520  ARG B NH1   1 
ATOM   8079 N NH2   . ARG B 1 520 ? -28.425 16.632  1.040   1.00 43.16  ? 520  ARG B NH2   1 
ATOM   8080 N N     . TYR B 1 521 ? -28.278 18.785  -6.175  1.00 40.37  ? 521  TYR B N     1 
ATOM   8081 C CA    . TYR B 1 521 ? -28.786 20.174  -6.043  1.00 42.03  ? 521  TYR B CA    1 
ATOM   8082 C C     . TYR B 1 521 ? -28.814 20.915  -7.380  1.00 42.68  ? 521  TYR B C     1 
ATOM   8083 O O     . TYR B 1 521 ? -29.306 22.039  -7.422  1.00 49.26  ? 521  TYR B O     1 
ATOM   8084 C CB    . TYR B 1 521 ? -27.913 20.975  -5.085  1.00 40.24  ? 521  TYR B CB    1 
ATOM   8085 C CG    . TYR B 1 521 ? -28.092 20.610  -3.639  1.00 42.21  ? 521  TYR B CG    1 
ATOM   8086 C CD1   . TYR B 1 521 ? -29.358 20.504  -3.090  1.00 42.95  ? 521  TYR B CD1   1 
ATOM   8087 C CD2   . TYR B 1 521 ? -26.998 20.369  -2.818  1.00 40.19  ? 521  TYR B CD2   1 
ATOM   8088 C CE1   . TYR B 1 521 ? -29.534 20.181  -1.757  1.00 43.46  ? 521  TYR B CE1   1 
ATOM   8089 C CE2   . TYR B 1 521 ? -27.155 20.033  -1.484  1.00 42.47  ? 521  TYR B CE2   1 
ATOM   8090 C CZ    . TYR B 1 521 ? -28.435 19.948  -0.953  1.00 46.55  ? 521  TYR B CZ    1 
ATOM   8091 O OH    . TYR B 1 521 ? -28.633 19.629  0.351   1.00 47.92  ? 521  TYR B OH    1 
ATOM   8092 N N     . ARG B 1 522 ? -28.279 20.329  -8.439  1.00 43.77  ? 522  ARG B N     1 
ATOM   8093 C CA    . ARG B 1 522 ? -28.046 21.069  -9.703  1.00 46.52  ? 522  ARG B CA    1 
ATOM   8094 C C     . ARG B 1 522 ? -29.393 21.266  -10.409 1.00 46.44  ? 522  ARG B C     1 
ATOM   8095 O O     . ARG B 1 522 ? -30.212 20.341  -10.340 1.00 42.86  ? 522  ARG B O     1 
ATOM   8096 C CB    . ARG B 1 522 ? -27.014 20.320  -10.550 1.00 40.28  ? 522  ARG B CB    1 
ATOM   8097 C CG    . ARG B 1 522 ? -26.468 21.135  -11.708 1.00 39.16  ? 522  ARG B CG    1 
ATOM   8098 C CD    . ARG B 1 522 ? -25.022 20.762  -11.996 1.00 41.06  ? 522  ARG B CD    1 
ATOM   8099 N NE    . ARG B 1 522 ? -24.917 19.379  -12.400 1.00 40.91  ? 522  ARG B NE    1 
ATOM   8100 C CZ    . ARG B 1 522 ? -24.162 18.442  -11.835 1.00 40.25  ? 522  ARG B CZ    1 
ATOM   8101 N NH1   . ARG B 1 522 ? -23.352 18.710  -10.825 1.00 38.36  ? 522  ARG B NH1   1 
ATOM   8102 N NH2   . ARG B 1 522 ? -24.205 17.218  -12.327 1.00 41.29  ? 522  ARG B NH2   1 
ATOM   8103 N N     . GLY B 1 523 ? -29.607 22.449  -11.005 1.00 47.89  ? 523  GLY B N     1 
ATOM   8104 C CA    . GLY B 1 523 ? -30.759 22.794  -11.865 1.00 51.71  ? 523  GLY B CA    1 
ATOM   8105 C C     . GLY B 1 523 ? -32.102 22.728  -11.140 1.00 54.32  ? 523  GLY B C     1 
ATOM   8106 O O     . GLY B 1 523 ? -33.135 22.525  -11.830 1.00 48.53  ? 523  GLY B O     1 
ATOM   8107 N N     . LYS B 1 524 ? -32.101 22.890  -9.813  1.00 49.46  ? 524  LYS B N     1 
ATOM   8108 C CA    . LYS B 1 524 ? -33.313 22.876  -8.945  1.00 52.36  ? 524  LYS B CA    1 
ATOM   8109 C C     . LYS B 1 524 ? -33.611 24.311  -8.486  1.00 53.51  ? 524  LYS B C     1 
ATOM   8110 O O     . LYS B 1 524 ? -34.383 24.477  -7.540  1.00 51.81  ? 524  LYS B O     1 
ATOM   8111 C CB    . LYS B 1 524 ? -33.104 21.949  -7.742  1.00 51.37  ? 524  LYS B CB    1 
ATOM   8112 C CG    . LYS B 1 524 ? -33.196 20.458  -8.045  1.00 55.59  ? 524  LYS B CG    1 
ATOM   8113 C CD    . LYS B 1 524 ? -33.037 19.567  -6.824  1.00 53.65  ? 524  LYS B CD    1 
ATOM   8114 C CE    . LYS B 1 524 ? -32.930 18.105  -7.192  1.00 59.86  ? 524  LYS B CE    1 
ATOM   8115 N NZ    . LYS B 1 524 ? -31.735 17.841  -8.037  1.00 67.27  ? 524  LYS B NZ    1 
ATOM   8116 N N     . GLY B 1 525 ? -32.996 25.305  -9.132  1.00 54.67  ? 525  GLY B N     1 
ATOM   8117 C CA    . GLY B 1 525 ? -33.104 26.733  -8.784  1.00 54.55  ? 525  GLY B CA    1 
ATOM   8118 C C     . GLY B 1 525 ? -32.881 27.027  -7.313  1.00 58.01  ? 525  GLY B C     1 
ATOM   8119 O O     . GLY B 1 525 ? -33.649 27.839  -6.781  1.00 59.51  ? 525  GLY B O     1 
ATOM   8120 N N     . LEU B 1 526 ? -31.851 26.438  -6.692  1.00 61.62  ? 526  LEU B N     1 
ATOM   8121 C CA    . LEU B 1 526 ? -31.413 26.704  -5.291  1.00 63.06  ? 526  LEU B CA    1 
ATOM   8122 C C     . LEU B 1 526 ? -32.294 25.884  -4.341  1.00 62.12  ? 526  LEU B C     1 
ATOM   8123 O O     . LEU B 1 526 ? -32.224 24.655  -4.353  1.00 56.06  ? 526  LEU B O     1 
ATOM   8124 C CB    . LEU B 1 526 ? -31.491 28.213  -5.006  1.00 71.95  ? 526  LEU B CB    1 
ATOM   8125 C CG    . LEU B 1 526 ? -30.906 28.712  -3.683  1.00 78.24  ? 526  LEU B CG    1 
ATOM   8126 C CD1   . LEU B 1 526 ? -31.763 28.326  -2.482  1.00 78.95  ? 526  LEU B CD1   1 
ATOM   8127 C CD2   . LEU B 1 526 ? -29.485 28.214  -3.497  1.00 84.12  ? 526  LEU B CD2   1 
HETATM 8128 C CAA   . QBF C 2 .   ? 17.807  18.129  -16.498 1.00 37.59  ? 701  QBF A CAA   1 
HETATM 8129 C CAC   . QBF C 2 .   ? 17.399  20.416  -15.737 1.00 39.10  ? 701  QBF A CAC   1 
HETATM 8130 C CAD   . QBF C 2 .   ? 18.687  20.876  -16.001 1.00 37.65  ? 701  QBF A CAD   1 
HETATM 8131 C CAE   . QBF C 2 .   ? 19.039  22.186  -15.666 1.00 39.58  ? 701  QBF A CAE   1 
HETATM 8132 C CAF   . QBF C 2 .   ? 18.096  23.050  -15.101 1.00 37.95  ? 701  QBF A CAF   1 
HETATM 8133 C CAG   . QBF C 2 .   ? 16.806  22.625  -14.856 1.00 36.75  ? 701  QBF A CAG   1 
HETATM 8134 C CAH   . QBF C 2 .   ? 16.484  21.311  -15.167 1.00 38.58  ? 701  QBF A CAH   1 
HETATM 8135 C CAK   . QBF C 2 .   ? 15.946  24.774  -14.078 1.00 42.69  ? 701  QBF A CAK   1 
HETATM 8136 C CAL   . QBF C 2 .   ? 20.345  22.681  -15.934 1.00 46.51  ? 701  QBF A CAL   1 
HETATM 8137 C CAM   . QBF C 2 .   ? 21.418  21.651  -15.518 1.00 49.24  ? 701  QBF A CAM   1 
HETATM 8138 C CAN   . QBF C 2 .   ? 22.763  22.329  -15.266 1.00 53.75  ? 701  QBF A CAN   1 
HETATM 8139 O OAB   . QBF C 2 .   ? 16.931  19.148  -15.998 1.00 41.74  ? 701  QBF A OAB   1 
HETATM 8140 O OAI   . QBF C 2 .   ? 15.210  20.906  -14.924 1.00 42.98  ? 701  QBF A OAI   1 
HETATM 8141 O OAJ   . QBF C 2 .   ? 15.786  23.378  -14.304 1.00 41.90  ? 701  QBF A OAJ   1 
HETATM 8142 O OAO   . QBF C 2 .   ? 23.078  23.165  -16.372 1.00 60.26  ? 701  QBF A OAO   1 
HETATM 8143 P PA    . FAD D 3 .   ? 7.964   18.445  -24.058 1.00 30.11  ? 702  FAD A PA    1 
HETATM 8144 O O1A   . FAD D 3 .   ? 8.842   17.238  -24.048 1.00 26.95  ? 702  FAD A O1A   1 
HETATM 8145 O O2A   . FAD D 3 .   ? 7.207   18.672  -25.327 1.00 30.73  ? 702  FAD A O2A   1 
HETATM 8146 O O5B   . FAD D 3 .   ? 6.879   18.308  -22.880 1.00 24.33  ? 702  FAD A O5B   1 
HETATM 8147 C C5B   . FAD D 3 .   ? 7.236   18.178  -21.492 1.00 27.22  ? 702  FAD A C5B   1 
HETATM 8148 C C4B   . FAD D 3 .   ? 6.123   17.408  -20.815 1.00 28.36  ? 702  FAD A C4B   1 
HETATM 8149 O O4B   . FAD D 3 .   ? 4.941   18.245  -20.757 1.00 27.57  ? 702  FAD A O4B   1 
HETATM 8150 C C3B   . FAD D 3 .   ? 5.642   16.132  -21.528 1.00 31.59  ? 702  FAD A C3B   1 
HETATM 8151 O O3B   . FAD D 3 .   ? 6.437   14.978  -21.241 1.00 30.74  ? 702  FAD A O3B   1 
HETATM 8152 C C2B   . FAD D 3 .   ? 4.211   16.026  -20.992 1.00 29.38  ? 702  FAD A C2B   1 
HETATM 8153 O O2B   . FAD D 3 .   ? 4.113   15.637  -19.636 1.00 29.98  ? 702  FAD A O2B   1 
HETATM 8154 C C1B   . FAD D 3 .   ? 3.772   17.480  -21.010 1.00 29.76  ? 702  FAD A C1B   1 
HETATM 8155 N N9A   . FAD D 3 .   ? 3.145   17.989  -22.242 1.00 29.82  ? 702  FAD A N9A   1 
HETATM 8156 C C8A   . FAD D 3 .   ? 3.793   18.487  -23.332 1.00 29.51  ? 702  FAD A C8A   1 
HETATM 8157 N N7A   . FAD D 3 .   ? 2.967   18.937  -24.252 1.00 30.66  ? 702  FAD A N7A   1 
HETATM 8158 C C5A   . FAD D 3 .   ? 1.696   18.784  -23.696 1.00 28.19  ? 702  FAD A C5A   1 
HETATM 8159 C C6A   . FAD D 3 .   ? 0.410   19.136  -24.167 1.00 28.76  ? 702  FAD A C6A   1 
HETATM 8160 N N6A   . FAD D 3 .   ? 0.194   19.738  -25.352 1.00 27.02  ? 702  FAD A N6A   1 
HETATM 8161 N N1A   . FAD D 3 .   ? -0.638  18.873  -23.343 1.00 27.99  ? 702  FAD A N1A   1 
HETATM 8162 C C2A   . FAD D 3 .   ? -0.390  18.304  -22.142 1.00 30.95  ? 702  FAD A C2A   1 
HETATM 8163 N N3A   . FAD D 3 .   ? 0.777   17.925  -21.601 1.00 28.46  ? 702  FAD A N3A   1 
HETATM 8164 C C4A   . FAD D 3 .   ? 1.797   18.215  -22.440 1.00 29.30  ? 702  FAD A C4A   1 
HETATM 8165 N N1    . FAD D 3 .   ? 14.683  22.328  -18.380 1.00 25.06  ? 702  FAD A N1    1 
HETATM 8166 C C2    . FAD D 3 .   ? 14.348  23.514  -17.817 1.00 27.88  ? 702  FAD A C2    1 
HETATM 8167 O O2    . FAD D 3 .   ? 13.177  23.776  -17.543 1.00 25.46  ? 702  FAD A O2    1 
HETATM 8168 N N3    . FAD D 3 .   ? 15.290  24.476  -17.564 1.00 29.23  ? 702  FAD A N3    1 
HETATM 8169 C C4    . FAD D 3 .   ? 16.622  24.301  -17.876 1.00 29.11  ? 702  FAD A C4    1 
HETATM 8170 O O4    . FAD D 3 .   ? 17.409  25.233  -17.698 1.00 31.35  ? 702  FAD A O4    1 
HETATM 8171 C C4X   . FAD D 3 .   ? 17.011  23.047  -18.432 1.00 29.88  ? 702  FAD A C4X   1 
HETATM 8172 N N5    . FAD D 3 .   ? 18.282  22.833  -18.727 1.00 30.89  ? 702  FAD A N5    1 
HETATM 8173 C C5X   . FAD D 3 .   ? 18.608  21.604  -19.249 1.00 32.12  ? 702  FAD A C5X   1 
HETATM 8174 C C6    . FAD D 3 .   ? 19.965  21.334  -19.516 1.00 34.48  ? 702  FAD A C6    1 
HETATM 8175 C C7    . FAD D 3 .   ? 20.382  20.122  -20.021 1.00 34.55  ? 702  FAD A C7    1 
HETATM 8176 C C7M   . FAD D 3 .   ? 21.853  19.907  -20.278 1.00 36.36  ? 702  FAD A C7M   1 
HETATM 8177 C C8    . FAD D 3 .   ? 19.412  19.106  -20.310 1.00 34.70  ? 702  FAD A C8    1 
HETATM 8178 C C8M   . FAD D 3 .   ? 19.833  17.738  -20.802 1.00 36.53  ? 702  FAD A C8M   1 
HETATM 8179 C C9    . FAD D 3 .   ? 18.070  19.369  -20.066 1.00 32.17  ? 702  FAD A C9    1 
HETATM 8180 C C9A   . FAD D 3 .   ? 17.648  20.608  -19.535 1.00 30.37  ? 702  FAD A C9A   1 
HETATM 8181 N N10   . FAD D 3 .   ? 16.314  20.882  -19.239 1.00 28.53  ? 702  FAD A N10   1 
HETATM 8182 C C10   . FAD D 3 .   ? 15.947  22.099  -18.674 1.00 27.80  ? 702  FAD A C10   1 
HETATM 8183 C "C1'" . FAD D 3 .   ? 15.274  19.880  -19.558 1.00 29.58  ? 702  FAD A "C1'" 1 
HETATM 8184 C "C2'" . FAD D 3 .   ? 14.690  20.118  -20.957 1.00 32.49  ? 702  FAD A "C2'" 1 
HETATM 8185 O "O2'" . FAD D 3 .   ? 15.763  20.425  -21.892 1.00 33.47  ? 702  FAD A "O2'" 1 
HETATM 8186 C "C3'" . FAD D 3 .   ? 13.676  21.278  -21.027 1.00 28.72  ? 702  FAD A "C3'" 1 
HETATM 8187 O "O3'" . FAD D 3 .   ? 12.808  21.301  -19.886 1.00 26.11  ? 702  FAD A "O3'" 1 
HETATM 8188 C "C4'" . FAD D 3 .   ? 12.784  21.240  -22.270 1.00 28.12  ? 702  FAD A "C4'" 1 
HETATM 8189 O "O4'" . FAD D 3 .   ? 12.320  22.565  -22.550 1.00 30.28  ? 702  FAD A "O4'" 1 
HETATM 8190 C "C5'" . FAD D 3 .   ? 11.605  20.312  -22.082 1.00 27.90  ? 702  FAD A "C5'" 1 
HETATM 8191 O "O5'" . FAD D 3 .   ? 11.221  19.667  -23.317 1.00 30.62  ? 702  FAD A "O5'" 1 
HETATM 8192 P P     . FAD D 3 .   ? 10.129  20.366  -24.254 1.00 30.39  ? 702  FAD A P     1 
HETATM 8193 O O1P   . FAD D 3 .   ? 10.225  19.814  -25.641 1.00 27.80  ? 702  FAD A O1P   1 
HETATM 8194 O O2P   . FAD D 3 .   ? 10.170  21.840  -24.006 1.00 28.04  ? 702  FAD A O2P   1 
HETATM 8195 O O3P   . FAD D 3 .   ? 8.781   19.768  -23.642 1.00 26.26  ? 702  FAD A O3P   1 
HETATM 8196 P PA    . FAD E 3 .   ? -14.396 34.785  4.744   1.00 37.53  ? 601  FAD B PA    1 
HETATM 8197 O O1A   . FAD E 3 .   ? -15.733 35.463  4.616   1.00 39.86  ? 601  FAD B O1A   1 
HETATM 8198 O O2A   . FAD E 3 .   ? -14.100 34.055  6.009   1.00 32.76  ? 601  FAD B O2A   1 
HETATM 8199 O O5B   . FAD E 3 .   ? -14.196 33.753  3.523   1.00 34.00  ? 601  FAD B O5B   1 
HETATM 8200 C C5B   . FAD E 3 .   ? -14.357 34.216  2.165   1.00 34.51  ? 601  FAD B C5B   1 
HETATM 8201 C C4B   . FAD E 3 .   ? -14.858 33.069  1.330   1.00 33.22  ? 601  FAD B C4B   1 
HETATM 8202 O O4B   . FAD E 3 .   ? -13.793 32.088  1.210   1.00 32.51  ? 601  FAD B O4B   1 
HETATM 8203 C C3B   . FAD E 3 .   ? -16.031 32.289  1.934   1.00 33.08  ? 601  FAD B C3B   1 
HETATM 8204 O O3B   . FAD E 3 .   ? -17.278 32.910  1.648   1.00 34.98  ? 601  FAD B O3B   1 
HETATM 8205 C C2B   . FAD E 3 .   ? -15.818 30.907  1.304   1.00 35.08  ? 601  FAD B C2B   1 
HETATM 8206 O O2B   . FAD E 3 .   ? -16.205 30.809  -0.056  1.00 36.15  ? 601  FAD B O2B   1 
HETATM 8207 C C1B   . FAD E 3 .   ? -14.292 30.777  1.374   1.00 33.87  ? 601  FAD B C1B   1 
HETATM 8208 N N9A   . FAD E 3 .   ? -13.687 30.205  2.606   1.00 34.26  ? 601  FAD B N9A   1 
HETATM 8209 C C8A   . FAD E 3 .   ? -13.445 30.850  3.797   1.00 33.03  ? 601  FAD B C8A   1 
HETATM 8210 N N7A   . FAD E 3 .   ? -12.840 30.089  4.673   1.00 31.20  ? 601  FAD B N7A   1 
HETATM 8211 C C5A   . FAD E 3 .   ? -12.694 28.864  4.040   1.00 32.86  ? 601  FAD B C5A   1 
HETATM 8212 C C6A   . FAD E 3 .   ? -12.120 27.648  4.460   1.00 33.69  ? 601  FAD B C6A   1 
HETATM 8213 N N6A   . FAD E 3 .   ? -11.574 27.476  5.669   1.00 34.33  ? 601  FAD B N6A   1 
HETATM 8214 N N1A   . FAD E 3 .   ? -12.121 26.618  3.570   1.00 32.65  ? 601  FAD B N1A   1 
HETATM 8215 C C2A   . FAD E 3 .   ? -12.669 26.818  2.359   1.00 33.69  ? 601  FAD B C2A   1 
HETATM 8216 N N3A   . FAD E 3 .   ? -13.230 27.921  1.860   1.00 36.54  ? 601  FAD B N3A   1 
HETATM 8217 C C4A   . FAD E 3 .   ? -13.205 28.925  2.760   1.00 35.34  ? 601  FAD B C4A   1 
HETATM 8218 N N1    . FAD E 3 .   ? -11.750 42.572  -0.365  1.00 36.38  ? 601  FAD B N1    1 
HETATM 8219 C C2    . FAD E 3 .   ? -10.506 42.562  -0.874  1.00 33.92  ? 601  FAD B C2    1 
HETATM 8220 O O2    . FAD E 3 .   ? -9.961  41.501  -1.222  1.00 30.77  ? 601  FAD B O2    1 
HETATM 8221 N N3    . FAD E 3 .   ? -9.790  43.703  -1.014  1.00 34.84  ? 601  FAD B N3    1 
HETATM 8222 C C4    . FAD E 3 .   ? -10.259 44.937  -0.621  1.00 37.89  ? 601  FAD B C4    1 
HETATM 8223 O O4    . FAD E 3 .   ? -9.536  45.933  -0.731  1.00 33.51  ? 601  FAD B O4    1 
HETATM 8224 C C4X   . FAD E 3 .   ? -11.588 44.990  -0.113  1.00 39.35  ? 601  FAD B C4X   1 
HETATM 8225 N N5    . FAD E 3 .   ? -12.099 46.152  0.241   1.00 43.88  ? 601  FAD B N5    1 
HETATM 8226 C C5X   . FAD E 3 .   ? -13.387 46.165  0.714   1.00 39.71  ? 601  FAD B C5X   1 
HETATM 8227 C C6    . FAD E 3 .   ? -13.963 47.399  1.082   1.00 39.42  ? 601  FAD B C6    1 
HETATM 8228 C C7    . FAD E 3 .   ? -15.245 47.476  1.584   1.00 39.39  ? 601  FAD B C7    1 
HETATM 8229 C C7M   . FAD E 3 .   ? -15.844 48.808  1.970   1.00 39.60  ? 601  FAD B C7M   1 
HETATM 8230 C C8    . FAD E 3 .   ? -15.994 46.293  1.718   1.00 39.05  ? 601  FAD B C8    1 
HETATM 8231 C C8M   . FAD E 3 .   ? -17.381 46.335  2.295   1.00 41.35  ? 601  FAD B C8M   1 
HETATM 8232 C C9    . FAD E 3 .   ? -15.440 45.081  1.379   1.00 35.84  ? 601  FAD B C9    1 
HETATM 8233 C C9A   . FAD E 3 .   ? -14.141 44.986  0.865   1.00 36.60  ? 601  FAD B C9A   1 
HETATM 8234 N N10   . FAD E 3 .   ? -13.561 43.772  0.485   1.00 37.71  ? 601  FAD B N10   1 
HETATM 8235 C C10   . FAD E 3 .   ? -12.275 43.730  -0.012  1.00 36.62  ? 601  FAD B C10   1 
HETATM 8236 C "C1'" . FAD E 3 .   ? -14.315 42.518  0.614   1.00 34.41  ? 601  FAD B "C1'" 1 
HETATM 8237 C "C2'" . FAD E 3 .   ? -14.141 41.900  1.998   1.00 39.59  ? 601  FAD B "C2'" 1 
HETATM 8238 O "O2'" . FAD E 3 .   ? -14.287 42.892  2.994   1.00 45.13  ? 601  FAD B "O2'" 1 
HETATM 8239 C "C3'" . FAD E 3 .   ? -12.774 41.237  2.153   1.00 35.12  ? 601  FAD B "C3'" 1 
HETATM 8240 O "O3'" . FAD E 3 .   ? -12.510 40.477  0.963   1.00 32.50  ? 601  FAD B "O3'" 1 
HETATM 8241 C "C4'" . FAD E 3 .   ? -12.664 40.311  3.370   1.00 36.75  ? 601  FAD B "C4'" 1 
HETATM 8242 O "O4'" . FAD E 3 .   ? -11.292 40.136  3.735   1.00 31.21  ? 601  FAD B "O4'" 1 
HETATM 8243 C "C5'" . FAD E 3 .   ? -13.247 38.941  3.103   1.00 36.05  ? 601  FAD B "C5'" 1 
HETATM 8244 O "O5'" . FAD E 3 .   ? -13.872 38.371  4.298   1.00 36.98  ? 601  FAD B "O5'" 1 
HETATM 8245 P P     . FAD E 3 .   ? -13.053 37.319  5.208   1.00 38.89  ? 601  FAD B P     1 
HETATM 8246 O O1P   . FAD E 3 .   ? -13.686 37.232  6.563   1.00 37.51  ? 601  FAD B O1P   1 
HETATM 8247 O O2P   . FAD E 3 .   ? -11.611 37.707  5.127   1.00 32.55  ? 601  FAD B O2P   1 
HETATM 8248 O O3P   . FAD E 3 .   ? -13.297 35.913  4.452   1.00 34.07  ? 601  FAD B O3P   1 
HETATM 8249 C CAA   . QBF F 2 .   ? -16.504 44.888  -2.528  1.00 44.68  ? 602  QBF B CAA   1 
HETATM 8250 C CAC   . QBF F 2 .   ? -14.141 44.915  -2.881  1.00 46.09  ? 602  QBF B CAC   1 
HETATM 8251 C CAD   . QBF F 2 .   ? -14.000 46.246  -2.464  1.00 45.55  ? 602  QBF B CAD   1 
HETATM 8252 C CAE   . QBF F 2 .   ? -12.800 46.924  -2.686  1.00 44.98  ? 602  QBF B CAE   1 
HETATM 8253 C CAF   . QBF F 2 .   ? -11.731 46.306  -3.328  1.00 43.23  ? 602  QBF B CAF   1 
HETATM 8254 C CAG   . QBF F 2 .   ? -11.854 44.980  -3.733  1.00 42.53  ? 602  QBF B CAG   1 
HETATM 8255 C CAH   . QBF F 2 .   ? -13.051 44.299  -3.513  1.00 46.31  ? 602  QBF B CAH   1 
HETATM 8256 C CAK   . QBF F 2 .   ? -9.586  44.791  -4.604  1.00 46.38  ? 602  QBF B CAK   1 
HETATM 8257 C CAL   . QBF F 2 .   ? -12.682 48.245  -2.261  1.00 48.78  ? 602  QBF B CAL   1 
HETATM 8258 C CAM   . QBF F 2 .   ? -13.742 49.069  -3.028  1.00 51.75  ? 602  QBF B CAM   1 
HETATM 8259 C CAN   . QBF F 2 .   ? -13.267 50.498  -3.244  1.00 54.82  ? 602  QBF B CAN   1 
HETATM 8260 O OAB   . QBF F 2 .   ? -15.275 44.161  -2.712  1.00 47.60  ? 602  QBF B OAB   1 
HETATM 8261 O OAI   . QBF F 2 .   ? -13.148 43.006  -3.946  1.00 41.82  ? 602  QBF B OAI   1 
HETATM 8262 O OAJ   . QBF F 2 .   ? -10.913 44.260  -4.368  1.00 41.93  ? 602  QBF B OAJ   1 
HETATM 8263 O OAO   . QBF F 2 .   ? -12.459 50.930  -2.117  1.00 57.54  ? 602  QBF B OAO   1 
HETATM 8264 O O     . HOH G 4 .   ? 7.672   0.650   -23.466 1.00 42.53  ? 801  HOH A O     1 
HETATM 8265 O O     . HOH G 4 .   ? -12.693 6.167   -39.051 1.00 35.64  ? 802  HOH A O     1 
HETATM 8266 O O     . HOH G 4 .   ? -13.065 9.643   -9.251  1.00 36.38  ? 803  HOH A O     1 
HETATM 8267 O O     . HOH G 4 .   ? 48.355  18.142  -11.438 1.00 52.39  ? 804  HOH A O     1 
HETATM 8268 O O     . HOH G 4 .   ? 1.331   8.981   -46.292 1.00 46.74  ? 805  HOH A O     1 
HETATM 8269 O O     . HOH G 4 .   ? 6.866   46.655  -32.947 1.00 41.68  ? 806  HOH A O     1 
HETATM 8270 O O     . HOH G 4 .   ? 0.262   31.114  -14.348 1.00 23.62  ? 807  HOH A O     1 
HETATM 8271 O O     . HOH G 4 .   ? 45.121  10.953  -7.947  1.00 51.05  ? 808  HOH A O     1 
HETATM 8272 O O     . HOH G 4 .   ? -6.848  23.585  -38.788 1.00 45.57  ? 809  HOH A O     1 
HETATM 8273 O O     . HOH G 4 .   ? -7.742  5.443   -42.900 1.00 32.11  ? 810  HOH A O     1 
HETATM 8274 O O     . HOH G 4 .   ? -4.055  -6.564  -37.057 1.00 55.93  ? 811  HOH A O     1 
HETATM 8275 O O     . HOH G 4 .   ? -6.187  42.329  -24.838 1.00 48.95  ? 812  HOH A O     1 
HETATM 8276 O O     . HOH G 4 .   ? -1.727  29.858  -14.886 1.00 31.10  ? 813  HOH A O     1 
HETATM 8277 O O     . HOH G 4 .   ? -10.064 -7.501  -29.825 1.00 48.12  ? 814  HOH A O     1 
HETATM 8278 O O     . HOH G 4 .   ? -8.744  -0.983  -39.735 1.00 52.15  ? 815  HOH A O     1 
HETATM 8279 O O     . HOH G 4 .   ? 36.945  31.293  1.336   1.00 40.13  ? 816  HOH A O     1 
HETATM 8280 O O     . HOH G 4 .   ? 16.595  18.852  6.839   1.00 36.85  ? 817  HOH A O     1 
HETATM 8281 O O     . HOH G 4 .   ? 6.830   42.647  -15.858 1.00 31.39  ? 818  HOH A O     1 
HETATM 8282 O O     . HOH G 4 .   ? 19.274  12.662  9.074   1.00 54.96  ? 819  HOH A O     1 
HETATM 8283 O O     . HOH G 4 .   ? 27.563  36.446  -24.470 1.00 48.61  ? 820  HOH A O     1 
HETATM 8284 O O     . HOH G 4 .   ? 10.187  39.800  -1.984  1.00 40.14  ? 821  HOH A O     1 
HETATM 8285 O O     . HOH G 4 .   ? 32.304  31.036  -17.216 1.00 35.36  ? 822  HOH A O     1 
HETATM 8286 O O     . HOH G 4 .   ? -15.249 7.307   -27.959 1.00 41.59  ? 823  HOH A O     1 
HETATM 8287 O O     . HOH G 4 .   ? 21.114  34.599  4.882   1.00 42.14  ? 824  HOH A O     1 
HETATM 8288 O O     . HOH G 4 .   ? 6.597   27.960  -34.692 1.00 43.84  ? 825  HOH A O     1 
HETATM 8289 O O     . HOH G 4 .   ? 26.777  30.807  -25.718 1.00 51.47  ? 826  HOH A O     1 
HETATM 8290 O O     . HOH G 4 .   ? -5.718  36.633  -26.350 1.00 45.10  ? 827  HOH A O     1 
HETATM 8291 O O     . HOH G 4 .   ? 2.409   5.761   -8.644  1.00 27.67  ? 828  HOH A O     1 
HETATM 8292 O O     . HOH G 4 .   ? 27.112  31.488  6.506   1.00 43.63  ? 829  HOH A O     1 
HETATM 8293 O O     . HOH G 4 .   ? -12.869 28.851  -12.969 1.00 29.91  ? 830  HOH A O     1 
HETATM 8294 O O     . HOH G 4 .   ? 3.244   11.607  -36.295 1.00 34.53  ? 831  HOH A O     1 
HETATM 8295 O O     . HOH G 4 .   ? 13.796  36.836  -26.492 1.00 32.64  ? 832  HOH A O     1 
HETATM 8296 O O     . HOH G 4 .   ? 5.468   10.480  -24.841 1.00 32.40  ? 833  HOH A O     1 
HETATM 8297 O O     . HOH G 4 .   ? 38.220  32.829  -6.953  1.00 39.56  ? 834  HOH A O     1 
HETATM 8298 O O     . HOH G 4 .   ? -0.054  13.024  0.516   1.00 21.98  ? 835  HOH A O     1 
HETATM 8299 O O     . HOH G 4 .   ? 6.892   46.453  -24.847 1.00 50.47  ? 836  HOH A O     1 
HETATM 8300 O O     . HOH G 4 .   ? -12.015 2.308   -23.592 1.00 38.46  ? 837  HOH A O     1 
HETATM 8301 O O     . HOH G 4 .   ? 22.074  33.694  -13.304 1.00 33.52  ? 838  HOH A O     1 
HETATM 8302 O O     . HOH G 4 .   ? 17.033  40.819  2.483   1.00 38.73  ? 839  HOH A O     1 
HETATM 8303 O O     . HOH G 4 .   ? -1.393  40.565  -14.893 1.00 31.99  ? 840  HOH A O     1 
HETATM 8304 O O     . HOH G 4 .   ? 8.861   11.021  1.684   1.00 26.60  ? 841  HOH A O     1 
HETATM 8305 O O     . HOH G 4 .   ? 12.750  21.114  -31.099 1.00 42.97  ? 842  HOH A O     1 
HETATM 8306 O O     . HOH G 4 .   ? -10.098 6.761   -8.054  1.00 40.82  ? 843  HOH A O     1 
HETATM 8307 O O     . HOH G 4 .   ? 13.821  37.771  -36.236 1.00 43.58  ? 844  HOH A O     1 
HETATM 8308 O O     . HOH G 4 .   ? 37.193  7.203   -13.968 1.00 62.15  ? 845  HOH A O     1 
HETATM 8309 O O     . HOH G 4 .   ? 2.026   7.193   -20.078 1.00 23.82  ? 846  HOH A O     1 
HETATM 8310 O O     . HOH G 4 .   ? -5.200  8.521   2.643   1.00 40.44  ? 847  HOH A O     1 
HETATM 8311 O O     . HOH G 4 .   ? -8.912  -1.795  -25.620 1.00 51.49  ? 848  HOH A O     1 
HETATM 8312 O O     . HOH G 4 .   ? -10.233 1.958   -21.544 1.00 30.94  ? 849  HOH A O     1 
HETATM 8313 O O     . HOH G 4 .   ? 14.439  14.199  -27.017 1.00 34.92  ? 850  HOH A O     1 
HETATM 8314 O O     . HOH G 4 .   ? -4.677  -0.182  -39.075 1.00 30.54  ? 851  HOH A O     1 
HETATM 8315 O O     . HOH G 4 .   ? 31.612  3.472   -20.627 1.00 46.25  ? 852  HOH A O     1 
HETATM 8316 O O     . HOH G 4 .   ? 8.693   15.317  -15.708 1.00 31.72  ? 853  HOH A O     1 
HETATM 8317 O O     . HOH G 4 .   ? 16.115  21.668  6.097   1.00 38.03  ? 854  HOH A O     1 
HETATM 8318 O O     . HOH G 4 .   ? 2.288   9.030   -2.575  1.00 39.84  ? 855  HOH A O     1 
HETATM 8319 O O     . HOH G 4 .   ? -11.629 8.435   -20.421 1.00 30.52  ? 856  HOH A O     1 
HETATM 8320 O O     . HOH G 4 .   ? 3.225   48.912  -22.369 1.00 45.69  ? 857  HOH A O     1 
HETATM 8321 O O     . HOH G 4 .   ? 25.528  12.454  -25.884 1.00 38.65  ? 858  HOH A O     1 
HETATM 8322 O O     . HOH G 4 .   ? 15.417  17.110  -12.057 1.00 44.82  ? 859  HOH A O     1 
HETATM 8323 O O     . HOH G 4 .   ? 8.645   6.391   -2.889  1.00 29.92  ? 860  HOH A O     1 
HETATM 8324 O O     . HOH G 4 .   ? 8.049   14.860  -23.332 1.00 29.00  ? 861  HOH A O     1 
HETATM 8325 O O     . HOH G 4 .   ? -14.728 10.004  -25.422 1.00 33.89  ? 862  HOH A O     1 
HETATM 8326 O O     . HOH G 4 .   ? 3.994   17.533  -17.840 1.00 28.61  ? 863  HOH A O     1 
HETATM 8327 O O     . HOH G 4 .   ? -11.793 32.671  -25.427 1.00 30.30  ? 864  HOH A O     1 
HETATM 8328 O O     . HOH G 4 .   ? 44.144  30.094  -12.662 1.00 60.73  ? 865  HOH A O     1 
HETATM 8329 O O     . HOH G 4 .   ? 32.299  10.751  -8.746  1.00 45.40  ? 866  HOH A O     1 
HETATM 8330 O O     . HOH G 4 .   ? -2.027  3.907   -6.139  1.00 43.09  ? 867  HOH A O     1 
HETATM 8331 O O     . HOH G 4 .   ? -11.728 8.530   -37.724 1.00 44.25  ? 868  HOH A O     1 
HETATM 8332 O O     . HOH G 4 .   ? -16.576 9.942   -14.809 1.00 43.47  ? 869  HOH A O     1 
HETATM 8333 O O     . HOH G 4 .   ? -12.645 3.820   -41.812 1.00 33.70  ? 870  HOH A O     1 
HETATM 8334 O O     . HOH G 4 .   ? 16.451  19.275  -24.155 1.00 34.57  ? 871  HOH A O     1 
HETATM 8335 O O     . HOH G 4 .   ? 18.675  28.485  -24.417 1.00 33.67  ? 872  HOH A O     1 
HETATM 8336 O O     . HOH G 4 .   ? -8.551  8.042   -4.439  1.00 41.67  ? 873  HOH A O     1 
HETATM 8337 O O     . HOH G 4 .   ? -6.463  -8.956  -31.980 1.00 54.69  ? 874  HOH A O     1 
HETATM 8338 O O     . HOH G 4 .   ? 16.858  41.034  -1.790  1.00 28.93  ? 875  HOH A O     1 
HETATM 8339 O O     . HOH G 4 .   ? 8.065   28.276  -21.127 1.00 23.79  ? 876  HOH A O     1 
HETATM 8340 O O     . HOH G 4 .   ? -7.562  30.199  -15.075 1.00 30.17  ? 877  HOH A O     1 
HETATM 8341 O O     . HOH G 4 .   ? 27.712  13.672  -13.670 1.00 34.45  ? 878  HOH A O     1 
HETATM 8342 O O     . HOH G 4 .   ? 12.396  37.262  -19.869 1.00 27.90  ? 879  HOH A O     1 
HETATM 8343 O O     . HOH G 4 .   ? 26.304  -5.251  -14.870 1.00 33.58  ? 880  HOH A O     1 
HETATM 8344 O O     . HOH G 4 .   ? 0.252   15.197  -20.341 1.00 31.93  ? 881  HOH A O     1 
HETATM 8345 O O     . HOH G 4 .   ? -16.801 16.673  -27.296 1.00 47.10  ? 882  HOH A O     1 
HETATM 8346 O O     . HOH G 4 .   ? -7.121  34.217  -18.192 1.00 24.93  ? 883  HOH A O     1 
HETATM 8347 O O     . HOH G 4 .   ? 20.476  46.762  -11.662 1.00 39.67  ? 884  HOH A O     1 
HETATM 8348 O O     . HOH G 4 .   ? 25.124  21.381  7.115   1.00 47.10  ? 885  HOH A O     1 
HETATM 8349 O O     . HOH G 4 .   ? 4.925   6.646   -12.926 1.00 29.53  ? 886  HOH A O     1 
HETATM 8350 O O     . HOH G 4 .   ? 0.821   17.953  -34.719 1.00 32.03  ? 887  HOH A O     1 
HETATM 8351 O O     . HOH G 4 .   ? 29.304  12.405  -26.076 1.00 47.60  ? 888  HOH A O     1 
HETATM 8352 O O     . HOH G 4 .   ? -12.605 39.994  -19.242 1.00 36.84  ? 889  HOH A O     1 
HETATM 8353 O O     . HOH G 4 .   ? 23.249  27.320  -14.616 1.00 41.50  ? 890  HOH A O     1 
HETATM 8354 O O     . HOH G 4 .   ? -4.001  30.824  -16.448 1.00 33.24  ? 891  HOH A O     1 
HETATM 8355 O O     . HOH G 4 .   ? -10.397 35.271  -24.931 1.00 33.17  ? 892  HOH A O     1 
HETATM 8356 O O     . HOH G 4 .   ? 15.274  29.671  -35.067 1.00 58.92  ? 893  HOH A O     1 
HETATM 8357 O O     . HOH G 4 .   ? 15.578  46.052  -9.668  1.00 45.41  ? 894  HOH A O     1 
HETATM 8358 O O     . HOH G 4 .   ? -13.278 14.268  -19.577 1.00 41.68  ? 895  HOH A O     1 
HETATM 8359 O O     . HOH G 4 .   ? 4.677   9.959   -42.786 1.00 41.82  ? 896  HOH A O     1 
HETATM 8360 O O     . HOH G 4 .   ? 23.055  26.961  -23.851 1.00 35.03  ? 897  HOH A O     1 
HETATM 8361 O O     . HOH G 4 .   ? 7.025   9.120   3.986   1.00 31.96  ? 898  HOH A O     1 
HETATM 8362 O O     . HOH G 4 .   ? 3.551   6.381   -6.115  1.00 33.49  ? 899  HOH A O     1 
HETATM 8363 O O     . HOH G 4 .   ? 10.908  40.095  0.992   1.00 34.32  ? 900  HOH A O     1 
HETATM 8364 O O     . HOH G 4 .   ? -4.705  25.637  -10.908 1.00 32.74  ? 901  HOH A O     1 
HETATM 8365 O O     . HOH G 4 .   ? 33.979  17.487  -6.498  1.00 45.06  ? 902  HOH A O     1 
HETATM 8366 O O     . HOH G 4 .   ? 12.918  11.573  -27.215 1.00 36.93  ? 903  HOH A O     1 
HETATM 8367 O O     . HOH G 4 .   ? 26.834  44.887  -0.010  1.00 41.00  ? 904  HOH A O     1 
HETATM 8368 O O     . HOH G 4 .   ? -13.789 22.391  -30.897 1.00 52.51  ? 905  HOH A O     1 
HETATM 8369 O O     . HOH G 4 .   ? 31.800  2.447   -4.862  1.00 43.88  ? 906  HOH A O     1 
HETATM 8370 O O     . HOH G 4 .   ? 8.249   11.885  -22.025 1.00 29.85  ? 907  HOH A O     1 
HETATM 8371 O O     . HOH G 4 .   ? -1.845  5.986   -9.318  1.00 31.97  ? 908  HOH A O     1 
HETATM 8372 O O     . HOH G 4 .   ? 14.882  13.072  -10.109 1.00 30.80  ? 909  HOH A O     1 
HETATM 8373 O O     . HOH G 4 .   ? -9.933  5.613   -15.065 1.00 30.70  ? 910  HOH A O     1 
HETATM 8374 O O     . HOH G 4 .   ? 37.667  40.445  -8.533  1.00 39.18  ? 911  HOH A O     1 
HETATM 8375 O O     . HOH G 4 .   ? 21.951  32.061  -15.601 1.00 27.38  ? 912  HOH A O     1 
HETATM 8376 O O     . HOH G 4 .   ? 17.272  25.228  7.611   1.00 45.54  ? 913  HOH A O     1 
HETATM 8377 O O     . HOH G 4 .   ? 5.179   26.570  -27.386 1.00 29.16  ? 914  HOH A O     1 
HETATM 8378 O O     . HOH G 4 .   ? 7.362   26.817  -14.022 1.00 26.52  ? 915  HOH A O     1 
HETATM 8379 O O     . HOH G 4 .   ? -1.714  -5.488  -25.656 1.00 43.65  ? 916  HOH A O     1 
HETATM 8380 O O     . HOH G 4 .   ? -2.680  17.840  -18.613 1.00 43.68  ? 917  HOH A O     1 
HETATM 8381 O O     . HOH G 4 .   ? -6.648  17.216  -43.930 1.00 27.14  ? 918  HOH A O     1 
HETATM 8382 O O     . HOH G 4 .   ? 33.178  10.687  -1.658  1.00 53.93  ? 919  HOH A O     1 
HETATM 8383 O O     . HOH G 4 .   ? 2.820   8.397   5.032   1.00 41.78  ? 920  HOH A O     1 
HETATM 8384 O O     . HOH G 4 .   ? 1.028   0.063   -12.956 1.00 36.02  ? 921  HOH A O     1 
HETATM 8385 O O     . HOH G 4 .   ? 16.107  32.762  -19.389 1.00 30.06  ? 922  HOH A O     1 
HETATM 8386 O O     . HOH G 4 .   ? 20.411  13.015  -1.808  1.00 26.50  ? 923  HOH A O     1 
HETATM 8387 O O     . HOH G 4 .   ? 15.897  11.545  -20.664 1.00 30.73  ? 924  HOH A O     1 
HETATM 8388 O O     . HOH G 4 .   ? 10.948  13.552  -3.635  1.00 26.76  ? 925  HOH A O     1 
HETATM 8389 O O     . HOH G 4 .   ? 32.482  18.599  -23.238 1.00 37.96  ? 926  HOH A O     1 
HETATM 8390 O O     . HOH G 4 .   ? 33.955  12.100  -10.118 1.00 40.38  ? 927  HOH A O     1 
HETATM 8391 O O     . HOH G 4 .   ? -5.336  16.370  -41.356 1.00 35.41  ? 928  HOH A O     1 
HETATM 8392 O O     . HOH G 4 .   ? -3.104  13.550  -12.882 1.00 28.00  ? 929  HOH A O     1 
HETATM 8393 O O     . HOH G 4 .   ? 2.368   13.538  -19.768 1.00 37.34  ? 930  HOH A O     1 
HETATM 8394 O O     . HOH G 4 .   ? -16.368 22.651  -25.669 1.00 39.35  ? 931  HOH A O     1 
HETATM 8395 O O     . HOH G 4 .   ? -1.245  14.432  -45.329 1.00 44.17  ? 932  HOH A O     1 
HETATM 8396 O O     . HOH G 4 .   ? 23.279  14.445  -26.231 1.00 43.32  ? 933  HOH A O     1 
HETATM 8397 O O     . HOH G 4 .   ? 31.319  29.104  3.830   1.00 33.69  ? 934  HOH A O     1 
HETATM 8398 O O     . HOH G 4 .   ? 10.832  44.087  0.229   1.00 45.70  ? 935  HOH A O     1 
HETATM 8399 O O     . HOH G 4 .   ? -15.705 8.668   -23.547 1.00 37.61  ? 936  HOH A O     1 
HETATM 8400 O O     . HOH G 4 .   ? 9.572   37.134  -20.796 1.00 27.43  ? 937  HOH A O     1 
HETATM 8401 O O     . HOH G 4 .   ? 9.020   31.018  -21.024 1.00 28.04  ? 938  HOH A O     1 
HETATM 8402 O O     . HOH G 4 .   ? 36.732  24.931  -25.322 1.00 61.54  ? 939  HOH A O     1 
HETATM 8403 O O     . HOH G 4 .   ? 8.022   34.844  -20.499 1.00 24.93  ? 940  HOH A O     1 
HETATM 8404 O O     . HOH G 4 .   ? 34.656  45.347  -10.204 1.00 58.71  ? 941  HOH A O     1 
HETATM 8405 O O     . HOH G 4 .   ? 8.018   5.442   -12.384 1.00 21.85  ? 942  HOH A O     1 
HETATM 8406 O O     . HOH G 4 .   ? 13.644  3.645   -22.618 1.00 42.80  ? 943  HOH A O     1 
HETATM 8407 O O     . HOH G 4 .   ? 0.311   10.799  -1.868  1.00 29.77  ? 944  HOH A O     1 
HETATM 8408 O O     . HOH G 4 .   ? -8.480  -4.207  -26.921 1.00 35.24  ? 945  HOH A O     1 
HETATM 8409 O O     . HOH G 4 .   ? 20.030  31.772  4.438   1.00 36.60  ? 946  HOH A O     1 
HETATM 8410 O O     . HOH G 4 .   ? 42.545  21.168  -21.444 1.00 59.44  ? 947  HOH A O     1 
HETATM 8411 O O     . HOH G 4 .   ? 11.593  47.294  -24.007 1.00 41.40  ? 948  HOH A O     1 
HETATM 8412 O O     . HOH G 4 .   ? 12.683  5.058   -24.967 1.00 40.24  ? 949  HOH A O     1 
HETATM 8413 O O     . HOH G 4 .   ? -0.282  5.695   -41.512 1.00 40.56  ? 950  HOH A O     1 
HETATM 8414 O O     . HOH G 4 .   ? 5.759   43.413  -20.840 1.00 29.95  ? 951  HOH A O     1 
HETATM 8415 O O     . HOH G 4 .   ? 29.875  1.876   -24.035 1.00 48.42  ? 952  HOH A O     1 
HETATM 8416 O O     . HOH G 4 .   ? 5.478   10.832  -18.845 1.00 27.29  ? 953  HOH A O     1 
HETATM 8417 O O     . HOH G 4 .   ? 12.473  37.452  -10.452 1.00 45.76  ? 954  HOH A O     1 
HETATM 8418 O O     . HOH G 4 .   ? -0.965  20.121  -41.414 1.00 32.50  ? 955  HOH A O     1 
HETATM 8419 O O     . HOH G 4 .   ? 38.462  40.054  -5.851  1.00 54.92  ? 956  HOH A O     1 
HETATM 8420 O O     . HOH G 4 .   ? 14.270  23.447  -24.329 1.00 34.89  ? 957  HOH A O     1 
HETATM 8421 O O     . HOH G 4 .   ? 17.462  10.560  -18.546 1.00 30.04  ? 958  HOH A O     1 
HETATM 8422 O O     . HOH G 4 .   ? -0.817  -0.142  -39.224 1.00 39.70  ? 959  HOH A O     1 
HETATM 8423 O O     . HOH G 4 .   ? 20.142  17.718  -2.521  1.00 28.12  ? 960  HOH A O     1 
HETATM 8424 O O     . HOH G 4 .   ? 36.350  12.025  -24.344 1.00 40.97  ? 961  HOH A O     1 
HETATM 8425 O O     . HOH G 4 .   ? 16.994  6.871   -31.191 1.00 51.54  ? 962  HOH A O     1 
HETATM 8426 O O     . HOH G 4 .   ? 21.822  39.500  -10.291 1.00 34.93  ? 963  HOH A O     1 
HETATM 8427 O O     . HOH G 4 .   ? 22.365  11.384  -0.855  1.00 27.90  ? 964  HOH A O     1 
HETATM 8428 O O     . HOH G 4 .   ? -4.424  25.326  -31.235 1.00 26.63  ? 965  HOH A O     1 
HETATM 8429 O O     . HOH G 4 .   ? -11.266 2.068   -17.365 1.00 34.33  ? 966  HOH A O     1 
HETATM 8430 O O     . HOH G 4 .   ? 6.500   13.511  -18.855 1.00 29.40  ? 967  HOH A O     1 
HETATM 8431 O O     . HOH G 4 .   ? -5.011  14.267  -10.845 1.00 31.85  ? 968  HOH A O     1 
HETATM 8432 O O     . HOH G 4 .   ? 13.313  20.810  -11.337 1.00 37.79  ? 969  HOH A O     1 
HETATM 8433 O O     . HOH G 4 .   ? 3.041   7.132   -41.874 1.00 43.03  ? 970  HOH A O     1 
HETATM 8434 O O     . HOH G 4 .   ? 9.101   33.319  -22.679 1.00 26.46  ? 971  HOH A O     1 
HETATM 8435 O O     . HOH G 4 .   ? 8.327   32.856  -18.714 1.00 27.87  ? 972  HOH A O     1 
HETATM 8436 O O     . HOH G 4 .   ? 25.974  15.141  -10.917 1.00 44.89  ? 973  HOH A O     1 
HETATM 8437 O O     . HOH G 4 .   ? -0.204  37.655  -18.103 1.00 31.41  ? 974  HOH A O     1 
HETATM 8438 O O     . HOH G 4 .   ? 19.127  11.506  4.521   1.00 44.84  ? 975  HOH A O     1 
HETATM 8439 O O     . HOH G 4 .   ? -15.899 13.543  -16.307 1.00 49.83  ? 976  HOH A O     1 
HETATM 8440 O O     . HOH G 4 .   ? -0.110  31.376  -12.264 1.00 40.27  ? 977  HOH A O     1 
HETATM 8441 O O     . HOH G 4 .   ? -7.033  12.193  -0.271  1.00 32.13  ? 978  HOH A O     1 
HETATM 8442 O O     . HOH G 4 .   ? 9.315   34.320  -12.435 1.00 24.77  ? 979  HOH A O     1 
HETATM 8443 O O     . HOH G 4 .   ? -1.876  6.946   -2.237  1.00 32.08  ? 980  HOH A O     1 
HETATM 8444 O O     . HOH G 4 .   ? -10.533 26.062  -30.513 1.00 35.60  ? 981  HOH A O     1 
HETATM 8445 O O     . HOH G 4 .   ? 20.781  37.367  -9.680  1.00 39.43  ? 982  HOH A O     1 
HETATM 8446 O O     . HOH G 4 .   ? 6.348   21.916  -35.997 1.00 37.72  ? 983  HOH A O     1 
HETATM 8447 O O     . HOH G 4 .   ? 25.544  22.709  -29.251 1.00 49.01  ? 984  HOH A O     1 
HETATM 8448 O O     . HOH G 4 .   ? 0.399   1.456   -9.713  1.00 40.63  ? 985  HOH A O     1 
HETATM 8449 O O     . HOH G 4 .   ? 46.942  9.506   -17.147 1.00 51.23  ? 986  HOH A O     1 
HETATM 8450 O O     . HOH G 4 .   ? 33.405  43.251  1.814   1.00 50.59  ? 987  HOH A O     1 
HETATM 8451 O O     . HOH G 4 .   ? 9.054   12.837  -19.666 1.00 30.72  ? 988  HOH A O     1 
HETATM 8452 O O     . HOH G 4 .   ? 0.909   3.894   -40.014 1.00 51.29  ? 989  HOH A O     1 
HETATM 8453 O O     . HOH G 4 .   ? -5.533  38.529  -23.598 1.00 30.57  ? 990  HOH A O     1 
HETATM 8454 O O     . HOH G 4 .   ? 0.183   34.804  -15.133 1.00 29.55  ? 991  HOH A O     1 
HETATM 8455 O O     . HOH G 4 .   ? -14.559 6.372   -13.651 1.00 46.64  ? 992  HOH A O     1 
HETATM 8456 O O     . HOH G 4 .   ? 19.053  17.720  -24.413 1.00 44.12  ? 993  HOH A O     1 
HETATM 8457 O O     . HOH G 4 .   ? -16.265 20.529  -29.130 1.00 49.82  ? 994  HOH A O     1 
HETATM 8458 O O     . HOH G 4 .   ? 4.043   20.578  -39.976 1.00 49.93  ? 995  HOH A O     1 
HETATM 8459 O O     . HOH G 4 .   ? 16.359  15.408  -28.292 1.00 49.57  ? 996  HOH A O     1 
HETATM 8460 O O     . HOH G 4 .   ? 37.939  23.343  -2.098  1.00 49.38  ? 997  HOH A O     1 
HETATM 8461 O O     . HOH G 4 .   ? -16.071 14.214  -26.530 1.00 42.03  ? 998  HOH A O     1 
HETATM 8462 O O     . HOH G 4 .   ? 31.854  8.865   -1.091  1.00 55.88  ? 999  HOH A O     1 
HETATM 8463 O O     . HOH G 4 .   ? -13.740 15.068  -21.864 1.00 32.11  ? 1000 HOH A O     1 
HETATM 8464 O O     . HOH G 4 .   ? 23.319  46.238  -22.189 1.00 45.69  ? 1001 HOH A O     1 
HETATM 8465 O O     . HOH G 4 .   ? 2.884   11.983  -21.841 1.00 27.29  ? 1002 HOH A O     1 
HETATM 8466 O O     . HOH G 4 .   ? 29.744  10.973  -14.675 1.00 41.43  ? 1003 HOH A O     1 
HETATM 8467 O O     . HOH G 4 .   ? 29.289  6.251   -17.568 1.00 36.49  ? 1004 HOH A O     1 
HETATM 8468 O O     . HOH G 4 .   ? 36.473  32.433  -2.695  1.00 52.32  ? 1005 HOH A O     1 
HETATM 8469 O O     . HOH G 4 .   ? -11.601 1.991   -37.726 1.00 43.10  ? 1006 HOH A O     1 
HETATM 8470 O O     . HOH G 4 .   ? 13.498  13.659  -2.691  1.00 22.20  ? 1007 HOH A O     1 
HETATM 8471 O O     . HOH G 4 .   ? 1.780   16.498  9.939   1.00 30.62  ? 1008 HOH A O     1 
HETATM 8472 O O     . HOH G 4 .   ? 13.609  5.637   -20.876 1.00 37.59  ? 1009 HOH A O     1 
HETATM 8473 O O     . HOH G 4 .   ? 26.966  50.244  -4.470  1.00 54.58  ? 1010 HOH A O     1 
HETATM 8474 O O     . HOH G 4 .   ? -10.500 15.131  -39.135 1.00 46.20  ? 1011 HOH A O     1 
HETATM 8475 O O     . HOH G 4 .   ? 33.116  21.255  -25.144 1.00 47.79  ? 1012 HOH A O     1 
HETATM 8476 O O     . HOH G 4 .   ? -15.486 18.443  -31.642 1.00 49.35  ? 1013 HOH A O     1 
HETATM 8477 O O     . HOH G 4 .   ? -0.328  39.219  -33.021 1.00 39.55  ? 1014 HOH A O     1 
HETATM 8478 O O     . HOH G 4 .   ? -10.119 19.893  -37.983 1.00 36.11  ? 1015 HOH A O     1 
HETATM 8479 O O     . HOH G 4 .   ? 33.058  28.360  -19.363 1.00 51.94  ? 1016 HOH A O     1 
HETATM 8480 O O     . HOH G 4 .   ? 12.549  8.831   2.066   1.00 45.25  ? 1017 HOH A O     1 
HETATM 8481 O O     . HOH G 4 .   ? 4.968   45.209  -22.585 1.00 32.58  ? 1018 HOH A O     1 
HETATM 8482 O O     . HOH G 4 .   ? 12.773  22.010  -13.780 1.00 40.55  ? 1019 HOH A O     1 
HETATM 8483 O O     . HOH G 4 .   ? -0.409  13.406  -13.602 1.00 26.67  ? 1020 HOH A O     1 
HETATM 8484 O O     . HOH G 4 .   ? -2.482  -1.601  -38.461 1.00 35.87  ? 1021 HOH A O     1 
HETATM 8485 O O     . HOH G 4 .   ? 23.760  28.276  7.209   1.00 30.25  ? 1022 HOH A O     1 
HETATM 8486 O O     . HOH G 4 .   ? 6.031   13.750  -13.641 1.00 26.29  ? 1023 HOH A O     1 
HETATM 8487 O O     . HOH G 4 .   ? -6.113  24.360  -33.234 1.00 27.58  ? 1024 HOH A O     1 
HETATM 8488 O O     . HOH G 4 .   ? 36.192  12.065  -21.706 1.00 44.42  ? 1025 HOH A O     1 
HETATM 8489 O O     . HOH G 4 .   ? 11.565  7.301   -20.727 1.00 41.20  ? 1026 HOH A O     1 
HETATM 8490 O O     . HOH G 4 .   ? 9.636   4.832   -9.827  1.00 24.28  ? 1027 HOH A O     1 
HETATM 8491 O O     . HOH G 4 .   ? 1.111   18.354  -18.023 1.00 26.62  ? 1028 HOH A O     1 
HETATM 8492 O O     . HOH G 4 .   ? -3.338  14.988  -43.735 1.00 23.79  ? 1029 HOH A O     1 
HETATM 8493 O O     . HOH G 4 .   ? 7.041   18.552  -32.185 1.00 45.63  ? 1030 HOH A O     1 
HETATM 8494 O O     . HOH G 4 .   ? -8.149  6.065   -5.721  1.00 42.31  ? 1031 HOH A O     1 
HETATM 8495 O O     . HOH G 4 .   ? 37.762  15.069  -5.933  1.00 52.99  ? 1032 HOH A O     1 
HETATM 8496 O O     . HOH G 4 .   ? -9.018  26.509  -32.645 1.00 37.44  ? 1033 HOH A O     1 
HETATM 8497 O O     . HOH G 4 .   ? 5.467   12.396  -22.960 1.00 32.14  ? 1034 HOH A O     1 
HETATM 8498 O O     . HOH G 4 .   ? 35.257  13.923  -4.236  1.00 47.46  ? 1035 HOH A O     1 
HETATM 8499 O O     . HOH G 4 .   ? -7.846  -2.000  -20.553 1.00 53.77  ? 1036 HOH A O     1 
HETATM 8500 O O     . HOH G 4 .   ? 25.847  15.575  4.269   1.00 49.20  ? 1037 HOH A O     1 
HETATM 8501 O O     . HOH G 4 .   ? 23.315  28.206  -30.075 1.00 49.36  ? 1038 HOH A O     1 
HETATM 8502 O O     . HOH G 4 .   ? 3.794   31.343  -36.206 1.00 38.68  ? 1039 HOH A O     1 
HETATM 8503 O O     . HOH G 4 .   ? 4.402   4.970   -40.715 1.00 38.38  ? 1040 HOH A O     1 
HETATM 8504 O O     . HOH G 4 .   ? -9.190  33.281  -29.247 1.00 40.70  ? 1041 HOH A O     1 
HETATM 8505 O O     . HOH G 4 .   ? 3.703   9.716   -20.401 1.00 26.05  ? 1042 HOH A O     1 
HETATM 8506 O O     . HOH G 4 .   ? 23.321  -2.104  -23.697 1.00 52.52  ? 1043 HOH A O     1 
HETATM 8507 O O     . HOH G 4 .   ? 21.221  26.463  9.869   1.00 48.34  ? 1044 HOH A O     1 
HETATM 8508 O O     . HOH G 4 .   ? 12.845  0.747   -12.698 1.00 44.50  ? 1045 HOH A O     1 
HETATM 8509 O O     . HOH G 4 .   ? -12.100 13.017  -41.800 1.00 30.83  ? 1046 HOH A O     1 
HETATM 8510 O O     . HOH G 4 .   ? 16.552  23.317  -21.687 1.00 22.98  ? 1047 HOH A O     1 
HETATM 8511 O O     . HOH G 4 .   ? 37.804  9.922   -17.942 1.00 40.58  ? 1048 HOH A O     1 
HETATM 8512 O O     . HOH G 4 .   ? 1.588   5.923   4.837   1.00 45.10  ? 1049 HOH A O     1 
HETATM 8513 O O     . HOH G 4 .   ? -14.025 33.548  -27.179 1.00 42.08  ? 1050 HOH A O     1 
HETATM 8514 O O     . HOH G 4 .   ? -13.513 9.807   -36.456 1.00 53.94  ? 1051 HOH A O     1 
HETATM 8515 O O     . HOH G 4 .   ? -11.065 29.161  -14.986 1.00 34.70  ? 1052 HOH A O     1 
HETATM 8516 O O     . HOH G 4 .   ? -4.774  -3.454  -9.139  1.00 53.35  ? 1053 HOH A O     1 
HETATM 8517 O O     . HOH G 4 .   ? 5.717   12.736  -35.520 1.00 39.56  ? 1054 HOH A O     1 
HETATM 8518 O O     . HOH G 4 .   ? -5.692  -2.857  -18.419 1.00 47.39  ? 1055 HOH A O     1 
HETATM 8519 O O     . HOH G 4 .   ? -16.529 9.764   -32.262 1.00 57.68  ? 1056 HOH A O     1 
HETATM 8520 O O     . HOH G 4 .   ? 8.011   15.585  -13.100 1.00 30.96  ? 1057 HOH A O     1 
HETATM 8521 O O     . HOH G 4 .   ? -8.945  3.496   -16.006 1.00 35.84  ? 1058 HOH A O     1 
HETATM 8522 O O     . HOH G 4 .   ? -10.346 17.352  -39.226 1.00 35.75  ? 1059 HOH A O     1 
HETATM 8523 O O     . HOH G 4 .   ? 11.198  44.689  -17.589 1.00 46.37  ? 1060 HOH A O     1 
HETATM 8524 O O     . HOH G 4 .   ? -16.253 20.196  -26.299 1.00 38.42  ? 1061 HOH A O     1 
HETATM 8525 O O     . HOH G 4 .   ? -2.952  5.322   -4.079  1.00 51.96  ? 1062 HOH A O     1 
HETATM 8526 O O     . HOH G 4 .   ? -1.841  11.888  -45.385 1.00 39.75  ? 1063 HOH A O     1 
HETATM 8527 O O     . HOH G 4 .   ? 31.603  27.382  8.402   1.00 62.14  ? 1064 HOH A O     1 
HETATM 8528 O O     . HOH G 4 .   ? -8.504  25.543  -34.708 1.00 49.65  ? 1065 HOH A O     1 
HETATM 8529 O O     . HOH G 4 .   ? 3.543   -3.304  -24.229 1.00 52.93  ? 1066 HOH A O     1 
HETATM 8530 O O     . HOH G 4 .   ? -8.706  31.838  -30.831 1.00 50.45  ? 1067 HOH A O     1 
HETATM 8531 O O     . HOH G 4 .   ? 4.599   25.127  -40.565 1.00 52.59  ? 1068 HOH A O     1 
HETATM 8532 O O     . HOH G 4 .   ? 45.370  19.262  -17.053 1.00 47.50  ? 1069 HOH A O     1 
HETATM 8533 O O     . HOH G 4 .   ? 7.547   32.763  -2.104  1.00 33.37  ? 1070 HOH A O     1 
HETATM 8534 O O     . HOH G 4 .   ? 33.136  30.912  3.264   1.00 47.26  ? 1071 HOH A O     1 
HETATM 8535 O O     . HOH G 4 .   ? 33.205  17.050  -8.613  1.00 39.71  ? 1072 HOH A O     1 
HETATM 8536 O O     . HOH G 4 .   ? 3.385   1.158   -11.611 1.00 54.02  ? 1073 HOH A O     1 
HETATM 8537 O O     . HOH G 4 .   ? 14.583  4.259   -19.158 1.00 45.59  ? 1074 HOH A O     1 
HETATM 8538 O O     . HOH G 4 .   ? -16.383 17.525  -19.210 1.00 45.81  ? 1075 HOH A O     1 
HETATM 8539 O O     . HOH G 4 .   ? 36.841  17.959  -5.218  1.00 62.58  ? 1076 HOH A O     1 
HETATM 8540 O O     . HOH G 4 .   ? 13.837  2.797   -17.013 1.00 54.20  ? 1077 HOH A O     1 
HETATM 8541 O O     . HOH G 4 .   ? -3.573  -3.897  -18.733 1.00 54.68  ? 1078 HOH A O     1 
HETATM 8542 O O     . HOH G 4 .   ? 13.475  26.448  -11.024 1.00 49.07  ? 1079 HOH A O     1 
HETATM 8543 O O     . HOH G 4 .   ? 30.043  11.390  -27.979 1.00 48.29  ? 1080 HOH A O     1 
HETATM 8544 O O     . HOH G 4 .   ? 0.317   10.791  -47.015 1.00 59.25  ? 1081 HOH A O     1 
HETATM 8545 O O     . HOH G 4 .   ? -15.314 7.546   -32.185 1.00 45.39  ? 1082 HOH A O     1 
HETATM 8546 O O     . HOH G 4 .   ? -13.910 5.888   -33.808 1.00 58.19  ? 1083 HOH A O     1 
HETATM 8547 O O     . HOH G 4 .   ? -13.124 3.921   -37.989 1.00 46.52  ? 1084 HOH A O     1 
HETATM 8548 O O     . HOH G 4 .   ? -12.985 2.479   -39.881 1.00 52.46  ? 1085 HOH A O     1 
HETATM 8549 O O     . HOH G 4 .   ? 9.217   2.663   -8.598  1.00 36.25  ? 1086 HOH A O     1 
HETATM 8550 O O     . HOH G 4 .   ? -10.954 0.645   -19.579 1.00 51.00  ? 1087 HOH A O     1 
HETATM 8551 O O     . HOH G 4 .   ? -9.247  -6.058  -25.177 1.00 46.28  ? 1088 HOH A O     1 
HETATM 8552 O O     . HOH G 4 .   ? 10.937  26.376  -10.232 1.00 55.29  ? 1089 HOH A O     1 
HETATM 8553 O O     . HOH G 4 .   ? -5.076  11.211  7.009   1.00 44.72  ? 1090 HOH A O     1 
HETATM 8554 O O     . HOH G 4 .   ? -9.620  11.559  -2.021  1.00 45.81  ? 1091 HOH A O     1 
HETATM 8555 O O     . HOH G 4 .   ? 12.008  32.776  -9.864  1.00 54.56  ? 1092 HOH A O     1 
HETATM 8556 O O     . HOH G 4 .   ? -7.220  44.073  -25.891 1.00 42.26  ? 1093 HOH A O     1 
HETATM 8557 O O     . HOH G 4 .   ? -11.981 1.524   -14.740 1.00 54.66  ? 1094 HOH A O     1 
HETATM 8558 O O     . HOH G 4 .   ? 38.779  25.906  -26.115 1.00 54.78  ? 1095 HOH A O     1 
HETATM 8559 O O     . HOH G 4 .   ? -6.799  10.458  1.955   1.00 37.68  ? 1096 HOH A O     1 
HETATM 8560 O O     . HOH G 4 .   ? -17.694 20.433  -22.507 1.00 35.43  ? 1097 HOH A O     1 
HETATM 8561 O O     . HOH G 4 .   ? 0.315   3.993   -8.186  1.00 45.43  ? 1098 HOH A O     1 
HETATM 8562 O O     . HOH G 4 .   ? -1.529  38.916  -12.854 1.00 46.00  ? 1099 HOH A O     1 
HETATM 8563 O O     . HOH G 4 .   ? 15.072  23.566  8.023   1.00 45.35  ? 1100 HOH A O     1 
HETATM 8564 O O     . HOH G 4 .   ? 8.304   19.671  -36.764 1.00 56.94  ? 1101 HOH A O     1 
HETATM 8565 O O     . HOH G 4 .   ? 2.414   5.742   -3.837  1.00 40.85  ? 1102 HOH A O     1 
HETATM 8566 O O     . HOH G 4 .   ? 20.209  15.741  -0.677  1.00 28.17  ? 1103 HOH A O     1 
HETATM 8567 O O     . HOH G 4 .   ? 0.418   36.975  -14.170 1.00 33.79  ? 1104 HOH A O     1 
HETATM 8568 O O     . HOH G 4 .   ? 32.776  1.672   -13.690 1.00 69.75  ? 1105 HOH A O     1 
HETATM 8569 O O     . HOH G 4 .   ? 9.357   33.875  -9.966  1.00 45.77  ? 1106 HOH A O     1 
HETATM 8570 O O     . HOH G 4 .   ? 26.420  16.851  6.228   1.00 44.73  ? 1107 HOH A O     1 
HETATM 8571 O O     . HOH G 4 .   ? 24.367  20.035  8.920   1.00 49.20  ? 1108 HOH A O     1 
HETATM 8572 O O     . HOH G 4 .   ? 15.178  27.025  -34.942 1.00 49.72  ? 1109 HOH A O     1 
HETATM 8573 O O     . HOH G 4 .   ? 10.031  8.783   1.557   1.00 33.26  ? 1110 HOH A O     1 
HETATM 8574 O O     . HOH G 4 .   ? 19.206  36.097  5.710   1.00 48.52  ? 1111 HOH A O     1 
HETATM 8575 O O     . HOH G 4 .   ? 1.108   19.965  -43.114 1.00 52.01  ? 1112 HOH A O     1 
HETATM 8576 O O     . HOH G 4 .   ? -15.417 16.132  -17.969 1.00 57.53  ? 1113 HOH A O     1 
HETATM 8577 O O     . HOH G 4 .   ? 37.441  9.905   -24.918 1.00 46.11  ? 1114 HOH A O     1 
HETATM 8578 O O     . HOH G 4 .   ? -6.715  32.438  -31.505 1.00 56.87  ? 1115 HOH A O     1 
HETATM 8579 O O     . HOH G 4 .   ? -5.700  -10.267 -27.351 1.00 49.48  ? 1116 HOH A O     1 
HETATM 8580 O O     . HOH G 4 .   ? 8.296   36.875  -9.048  1.00 49.65  ? 1117 HOH A O     1 
HETATM 8581 O O     . HOH G 4 .   ? 6.406   37.664  -9.303  1.00 43.65  ? 1118 HOH A O     1 
HETATM 8582 O O     . HOH H 4 .   ? -6.843  37.750  -7.327  1.00 46.51  ? 701  HOH B O     1 
HETATM 8583 O O     . HOH H 4 .   ? -6.744  52.798  10.869  1.00 46.23  ? 702  HOH B O     1 
HETATM 8584 O O     . HOH H 4 .   ? -29.743 30.714  -10.036 1.00 45.36  ? 703  HOH B O     1 
HETATM 8585 O O     . HOH H 4 .   ? -0.458  28.415  -4.366  1.00 29.86  ? 704  HOH B O     1 
HETATM 8586 O O     . HOH H 4 .   ? -6.489  54.419  -24.723 1.00 36.73  ? 705  HOH B O     1 
HETATM 8587 O O     . HOH H 4 .   ? 4.497   66.248  -3.957  1.00 42.80  ? 706  HOH B O     1 
HETATM 8588 O O     . HOH H 4 .   ? -19.724 58.596  5.053   1.00 41.71  ? 707  HOH B O     1 
HETATM 8589 O O     . HOH H 4 .   ? -12.168 46.486  -15.729 1.00 36.82  ? 708  HOH B O     1 
HETATM 8590 O O     . HOH H 4 .   ? 0.019   30.612  -4.490  1.00 22.46  ? 709  HOH B O     1 
HETATM 8591 O O     . HOH H 4 .   ? -26.866 70.529  -13.098 1.00 47.83  ? 710  HOH B O     1 
HETATM 8592 O O     . HOH H 4 .   ? 2.244   44.056  18.433  1.00 47.89  ? 711  HOH B O     1 
HETATM 8593 O O     . HOH H 4 .   ? -20.344 41.197  -8.998  1.00 38.77  ? 712  HOH B O     1 
HETATM 8594 O O     . HOH H 4 .   ? -27.857 37.891  1.127   1.00 44.95  ? 713  HOH B O     1 
HETATM 8595 O O     . HOH H 4 .   ? 7.429   43.929  -18.765 1.00 37.24  ? 714  HOH B O     1 
HETATM 8596 O O     . HOH H 4 .   ? -6.545  66.722  -14.465 1.00 39.22  ? 715  HOH B O     1 
HETATM 8597 O O     . HOH H 4 .   ? -16.989 42.373  -6.987  1.00 41.03  ? 716  HOH B O     1 
HETATM 8598 O O     . HOH H 4 .   ? -23.687 42.947  -0.691  1.00 36.56  ? 717  HOH B O     1 
HETATM 8599 O O     . HOH H 4 .   ? -17.825 33.968  3.857   1.00 31.54  ? 718  HOH B O     1 
HETATM 8600 O O     . HOH H 4 .   ? 6.945   63.642  1.253   1.00 50.56  ? 719  HOH B O     1 
HETATM 8601 O O     . HOH H 4 .   ? -19.769 17.669  -16.132 1.00 36.76  ? 720  HOH B O     1 
HETATM 8602 O O     . HOH H 4 .   ? -20.919 27.632  16.261  1.00 53.05  ? 721  HOH B O     1 
HETATM 8603 O O     . HOH H 4 .   ? -33.154 45.364  -15.309 1.00 45.44  ? 722  HOH B O     1 
HETATM 8604 O O     . HOH H 4 .   ? -26.695 54.851  -4.010  1.00 53.40  ? 723  HOH B O     1 
HETATM 8605 O O     . HOH H 4 .   ? -4.815  58.090  -23.866 1.00 48.44  ? 724  HOH B O     1 
HETATM 8606 O O     . HOH H 4 .   ? -8.309  47.064  -25.550 1.00 32.93  ? 725  HOH B O     1 
HETATM 8607 O O     . HOH H 4 .   ? -25.144 11.209  2.014   1.00 61.36  ? 726  HOH B O     1 
HETATM 8608 O O     . HOH H 4 .   ? -0.764  15.615  1.286   1.00 28.08  ? 727  HOH B O     1 
HETATM 8609 O O     . HOH H 4 .   ? -26.811 58.145  -9.954  1.00 45.24  ? 728  HOH B O     1 
HETATM 8610 O O     . HOH H 4 .   ? -22.486 45.831  -23.474 1.00 50.40  ? 729  HOH B O     1 
HETATM 8611 O O     . HOH H 4 .   ? 3.338   43.487  1.819   1.00 28.38  ? 730  HOH B O     1 
HETATM 8612 O O     . HOH H 4 .   ? 11.517  20.020  0.222   1.00 31.63  ? 731  HOH B O     1 
HETATM 8613 O O     . HOH H 4 .   ? -34.092 54.361  1.583   1.00 52.08  ? 732  HOH B O     1 
HETATM 8614 O O     . HOH H 4 .   ? -6.751  55.718  8.220   1.00 50.74  ? 733  HOH B O     1 
HETATM 8615 O O     . HOH H 4 .   ? -1.717  32.752  17.194  1.00 41.27  ? 734  HOH B O     1 
HETATM 8616 O O     . HOH H 4 .   ? -22.610 10.786  18.219  1.00 52.05  ? 735  HOH B O     1 
HETATM 8617 O O     . HOH H 4 .   ? -17.603 13.294  -11.816 1.00 40.79  ? 736  HOH B O     1 
HETATM 8618 O O     . HOH H 4 .   ? -23.491 23.542  -11.425 1.00 30.76  ? 737  HOH B O     1 
HETATM 8619 O O     . HOH H 4 .   ? -2.095  46.031  1.602   1.00 35.30  ? 738  HOH B O     1 
HETATM 8620 O O     . HOH H 4 .   ? -15.414 43.348  5.251   1.00 47.69  ? 739  HOH B O     1 
HETATM 8621 O O     . HOH H 4 .   ? -23.006 53.424  -4.969  1.00 46.99  ? 740  HOH B O     1 
HETATM 8622 O O     . HOH H 4 .   ? 1.884   51.962  -7.618  1.00 33.61  ? 741  HOH B O     1 
HETATM 8623 O O     . HOH H 4 .   ? -5.601  35.086  16.032  1.00 45.23  ? 742  HOH B O     1 
HETATM 8624 O O     . HOH H 4 .   ? -28.421 57.246  -17.145 1.00 49.83  ? 743  HOH B O     1 
HETATM 8625 O O     . HOH H 4 .   ? 13.281  39.392  15.445  1.00 43.22  ? 744  HOH B O     1 
HETATM 8626 O O     . HOH H 4 .   ? -20.578 35.760  -21.829 1.00 30.02  ? 745  HOH B O     1 
HETATM 8627 O O     . HOH H 4 .   ? -17.388 10.706  4.388   1.00 39.58  ? 746  HOH B O     1 
HETATM 8628 O O     . HOH H 4 .   ? 3.789   54.125  -7.049  1.00 36.86  ? 747  HOH B O     1 
HETATM 8629 O O     . HOH H 4 .   ? -6.518  67.635  -18.334 1.00 37.95  ? 748  HOH B O     1 
HETATM 8630 O O     . HOH H 4 .   ? -22.116 15.163  -6.119  1.00 36.42  ? 749  HOH B O     1 
HETATM 8631 O O     . HOH H 4 .   ? -31.615 53.680  -3.845  1.00 48.91  ? 750  HOH B O     1 
HETATM 8632 O O     . HOH H 4 .   ? -25.125 34.161  -17.331 1.00 28.82  ? 751  HOH B O     1 
HETATM 8633 O O     . HOH H 4 .   ? -23.592 48.507  -18.171 1.00 38.56  ? 752  HOH B O     1 
HETATM 8634 O O     . HOH H 4 .   ? -13.183 13.539  -1.565  1.00 50.87  ? 753  HOH B O     1 
HETATM 8635 O O     . HOH H 4 .   ? -6.438  24.046  15.538  1.00 47.56  ? 754  HOH B O     1 
HETATM 8636 O O     . HOH H 4 .   ? 2.341   44.666  8.718   1.00 40.05  ? 755  HOH B O     1 
HETATM 8637 O O     . HOH H 4 .   ? -5.945  11.811  4.349   1.00 39.92  ? 756  HOH B O     1 
HETATM 8638 O O     . HOH H 4 .   ? -1.000  57.647  7.332   1.00 38.89  ? 757  HOH B O     1 
HETATM 8639 O O     . HOH H 4 .   ? -13.459 39.493  11.950  1.00 47.87  ? 758  HOH B O     1 
HETATM 8640 O O     . HOH H 4 .   ? 2.017   21.339  -6.717  1.00 37.36  ? 759  HOH B O     1 
HETATM 8641 O O     . HOH H 4 .   ? 13.244  39.770  7.203   1.00 41.81  ? 760  HOH B O     1 
HETATM 8642 O O     . HOH H 4 .   ? 6.772   49.601  -15.526 1.00 29.63  ? 761  HOH B O     1 
HETATM 8643 O O     . HOH H 4 .   ? -3.583  51.874  -2.181  1.00 33.47  ? 762  HOH B O     1 
HETATM 8644 O O     . HOH H 4 .   ? -0.145  52.807  -22.554 1.00 33.65  ? 763  HOH B O     1 
HETATM 8645 O O     . HOH H 4 .   ? -10.864 42.308  5.774   1.00 39.99  ? 764  HOH B O     1 
HETATM 8646 O O     . HOH H 4 .   ? -17.037 68.515  -13.576 1.00 34.43  ? 765  HOH B O     1 
HETATM 8647 O O     . HOH H 4 .   ? -24.234 29.148  -13.979 1.00 34.00  ? 766  HOH B O     1 
HETATM 8648 O O     . HOH H 4 .   ? 9.526   19.802  8.796   1.00 44.08  ? 767  HOH B O     1 
HETATM 8649 O O     . HOH H 4 .   ? 0.295   49.658  13.658  1.00 51.83  ? 768  HOH B O     1 
HETATM 8650 O O     . HOH H 4 .   ? -6.132  33.561  8.560   1.00 34.81  ? 769  HOH B O     1 
HETATM 8651 O O     . HOH H 4 .   ? -20.735 33.783  2.486   1.00 36.76  ? 770  HOH B O     1 
HETATM 8652 O O     . HOH H 4 .   ? -6.409  68.104  -9.669  1.00 42.49  ? 771  HOH B O     1 
HETATM 8653 O O     . HOH H 4 .   ? -5.217  24.047  11.671  1.00 41.31  ? 772  HOH B O     1 
HETATM 8654 O O     . HOH H 4 .   ? -4.658  37.302  2.387   1.00 27.13  ? 773  HOH B O     1 
HETATM 8655 O O     . HOH H 4 .   ? 1.956   38.708  2.226   1.00 30.73  ? 774  HOH B O     1 
HETATM 8656 O O     . HOH H 4 .   ? -25.903 58.223  6.360   1.00 58.70  ? 775  HOH B O     1 
HETATM 8657 O O     . HOH H 4 .   ? -2.148  52.338  -4.376  1.00 30.88  ? 776  HOH B O     1 
HETATM 8658 O O     . HOH H 4 .   ? -25.570 59.804  -8.230  1.00 39.21  ? 777  HOH B O     1 
HETATM 8659 O O     . HOH H 4 .   ? 3.111   37.074  21.384  1.00 49.33  ? 778  HOH B O     1 
HETATM 8660 O O     . HOH H 4 .   ? -13.957 27.211  15.146  1.00 36.33  ? 779  HOH B O     1 
HETATM 8661 O O     . HOH H 4 .   ? -24.699 29.907  -7.471  1.00 34.85  ? 780  HOH B O     1 
HETATM 8662 O O     . HOH H 4 .   ? -28.370 36.436  5.360   1.00 39.43  ? 781  HOH B O     1 
HETATM 8663 O O     . HOH H 4 .   ? -11.317 61.097  -22.589 1.00 55.57  ? 782  HOH B O     1 
HETATM 8664 O O     . HOH H 4 .   ? 0.816   26.426  -2.485  1.00 34.14  ? 783  HOH B O     1 
HETATM 8665 O O     . HOH H 4 .   ? -15.439 26.817  0.348   1.00 44.21  ? 784  HOH B O     1 
HETATM 8666 O O     . HOH H 4 .   ? 3.597   40.714  2.861   1.00 34.33  ? 785  HOH B O     1 
HETATM 8667 O O     . HOH H 4 .   ? -8.793  54.046  2.226   1.00 47.38  ? 786  HOH B O     1 
HETATM 8668 O O     . HOH H 4 .   ? -27.933 27.188  19.961  1.00 53.68  ? 787  HOH B O     1 
HETATM 8669 O O     . HOH H 4 .   ? 13.071  44.757  6.645   1.00 46.96  ? 788  HOH B O     1 
HETATM 8670 O O     . HOH H 4 .   ? 4.091   18.314  5.972   1.00 30.24  ? 789  HOH B O     1 
HETATM 8671 O O     . HOH H 4 .   ? -7.084  61.575  0.088   1.00 40.22  ? 790  HOH B O     1 
HETATM 8672 O O     . HOH H 4 .   ? 9.960   31.079  -3.387  1.00 26.53  ? 791  HOH B O     1 
HETATM 8673 O O     . HOH H 4 .   ? -20.547 15.651  -12.871 1.00 49.22  ? 792  HOH B O     1 
HETATM 8674 O O     . HOH H 4 .   ? -14.560 33.403  12.762  1.00 42.43  ? 793  HOH B O     1 
HETATM 8675 O O     . HOH H 4 .   ? -2.811  51.296  -22.016 1.00 34.10  ? 794  HOH B O     1 
HETATM 8676 O O     . HOH H 4 .   ? -8.872  41.016  14.839  1.00 42.81  ? 795  HOH B O     1 
HETATM 8677 O O     . HOH H 4 .   ? -27.851 16.506  21.102  1.00 45.86  ? 796  HOH B O     1 
HETATM 8678 O O     . HOH H 4 .   ? 7.791   22.579  5.762   1.00 32.74  ? 797  HOH B O     1 
HETATM 8679 O O     . HOH H 4 .   ? -24.147 39.396  -22.096 1.00 35.18  ? 798  HOH B O     1 
HETATM 8680 O O     . HOH H 4 .   ? -5.968  14.240  10.711  1.00 37.20  ? 799  HOH B O     1 
HETATM 8681 O O     . HOH H 4 .   ? 9.219   11.610  4.407   1.00 28.71  ? 800  HOH B O     1 
HETATM 8682 O O     . HOH H 4 .   ? -3.836  13.763  14.427  1.00 35.71  ? 801  HOH B O     1 
HETATM 8683 O O     . HOH H 4 .   ? -20.786 28.059  -26.607 1.00 53.56  ? 802  HOH B O     1 
HETATM 8684 O O     . HOH H 4 .   ? -21.690 30.241  4.999   1.00 48.60  ? 803  HOH B O     1 
HETATM 8685 O O     . HOH H 4 .   ? -19.951 39.796  7.780   1.00 45.44  ? 804  HOH B O     1 
HETATM 8686 O O     . HOH H 4 .   ? -17.824 28.847  -27.723 1.00 44.43  ? 805  HOH B O     1 
HETATM 8687 O O     . HOH H 4 .   ? -13.256 10.299  6.004   1.00 49.86  ? 806  HOH B O     1 
HETATM 8688 O O     . HOH H 4 .   ? -34.788 52.999  5.581   1.00 63.82  ? 807  HOH B O     1 
HETATM 8689 O O     . HOH H 4 .   ? -31.775 43.682  -14.375 1.00 36.47  ? 808  HOH B O     1 
HETATM 8690 O O     . HOH H 4 .   ? -13.636 30.559  -29.735 1.00 40.97  ? 809  HOH B O     1 
HETATM 8691 O O     . HOH H 4 .   ? -9.951  16.909  17.881  1.00 42.75  ? 810  HOH B O     1 
HETATM 8692 O O     . HOH H 4 .   ? -19.373 40.631  -16.665 1.00 32.80  ? 811  HOH B O     1 
HETATM 8693 O O     . HOH H 4 .   ? -3.733  25.141  -8.611  1.00 38.27  ? 812  HOH B O     1 
HETATM 8694 O O     . HOH H 4 .   ? -24.685 27.679  -11.975 1.00 32.03  ? 813  HOH B O     1 
HETATM 8695 O O     . HOH H 4 .   ? -21.858 38.142  7.619   1.00 51.44  ? 814  HOH B O     1 
HETATM 8696 O O     . HOH H 4 .   ? 0.763   17.325  -6.796  1.00 30.52  ? 815  HOH B O     1 
HETATM 8697 O O     . HOH H 4 .   ? -14.034 31.175  -1.690  1.00 35.38  ? 816  HOH B O     1 
HETATM 8698 O O     . HOH H 4 .   ? -17.732 28.545  -0.315  1.00 36.49  ? 817  HOH B O     1 
HETATM 8699 O O     . HOH H 4 .   ? 3.695   31.406  -3.407  1.00 28.64  ? 818  HOH B O     1 
HETATM 8700 O O     . HOH H 4 .   ? -21.443 47.009  -17.388 1.00 34.80  ? 819  HOH B O     1 
HETATM 8701 O O     . HOH H 4 .   ? -11.450 45.126  -24.740 1.00 40.17  ? 820  HOH B O     1 
HETATM 8702 O O     . HOH H 4 .   ? -14.466 20.155  21.247  1.00 40.65  ? 821  HOH B O     1 
HETATM 8703 O O     . HOH H 4 .   ? -19.274 37.334  -23.411 1.00 36.14  ? 822  HOH B O     1 
HETATM 8704 O O     . HOH H 4 .   ? -18.845 37.828  -15.840 1.00 34.63  ? 823  HOH B O     1 
HETATM 8705 O O     . HOH H 4 .   ? 10.980  53.937  -4.903  1.00 42.34  ? 824  HOH B O     1 
HETATM 8706 O O     . HOH H 4 .   ? -29.581 38.091  -16.621 1.00 53.40  ? 825  HOH B O     1 
HETATM 8707 O O     . HOH H 4 .   ? -27.175 34.690  -10.375 1.00 33.82  ? 826  HOH B O     1 
HETATM 8708 O O     . HOH H 4 .   ? -7.033  47.142  6.411   1.00 35.96  ? 827  HOH B O     1 
HETATM 8709 O O     . HOH H 4 .   ? -12.521 28.697  -1.696  1.00 39.25  ? 828  HOH B O     1 
HETATM 8710 O O     . HOH H 4 .   ? -19.266 13.624  -0.592  1.00 38.81  ? 829  HOH B O     1 
HETATM 8711 O O     . HOH H 4 .   ? 10.624  38.233  3.036   1.00 27.45  ? 830  HOH B O     1 
HETATM 8712 O O     . HOH H 4 .   ? -25.712 26.504  21.377  1.00 51.26  ? 831  HOH B O     1 
HETATM 8713 O O     . HOH H 4 .   ? -19.467 21.689  -23.637 1.00 43.01  ? 832  HOH B O     1 
HETATM 8714 O O     . HOH H 4 .   ? 1.360   40.438  -5.702  1.00 28.26  ? 833  HOH B O     1 
HETATM 8715 O O     . HOH H 4 .   ? -11.046 35.205  14.355  1.00 45.05  ? 834  HOH B O     1 
HETATM 8716 O O     . HOH H 4 .   ? -22.725 41.136  1.279   1.00 36.51  ? 835  HOH B O     1 
HETATM 8717 O O     . HOH H 4 .   ? -18.877 27.272  -18.370 1.00 35.64  ? 836  HOH B O     1 
HETATM 8718 O O     . HOH H 4 .   ? -16.014 20.508  -20.478 1.00 33.14  ? 837  HOH B O     1 
HETATM 8719 O O     . HOH H 4 .   ? -20.978 28.591  -17.970 1.00 34.50  ? 838  HOH B O     1 
HETATM 8720 O O     . HOH H 4 .   ? -32.521 13.583  5.324   1.00 40.93  ? 839  HOH B O     1 
HETATM 8721 O O     . HOH H 4 .   ? -12.698 13.234  1.094   1.00 33.26  ? 840  HOH B O     1 
HETATM 8722 O O     . HOH H 4 .   ? -6.188  21.879  13.811  1.00 36.24  ? 841  HOH B O     1 
HETATM 8723 O O     . HOH H 4 .   ? 0.769   39.131  -16.153 1.00 28.15  ? 842  HOH B O     1 
HETATM 8724 O O     . HOH H 4 .   ? -26.710 60.914  3.337   1.00 44.75  ? 843  HOH B O     1 
HETATM 8725 O O     . HOH H 4 .   ? -0.215  38.559  0.345   1.00 29.18  ? 844  HOH B O     1 
HETATM 8726 O O     . HOH H 4 .   ? -4.617  51.477  11.671  1.00 47.80  ? 845  HOH B O     1 
HETATM 8727 O O     . HOH H 4 .   ? -16.081 23.976  -7.338  1.00 26.66  ? 846  HOH B O     1 
HETATM 8728 O O     . HOH H 4 .   ? -21.117 52.720  -7.867  1.00 43.70  ? 847  HOH B O     1 
HETATM 8729 O O     . HOH H 4 .   ? -14.585 65.575  -18.777 1.00 40.29  ? 848  HOH B O     1 
HETATM 8730 O O     . HOH H 4 .   ? 1.437   69.366  -7.949  1.00 44.45  ? 849  HOH B O     1 
HETATM 8731 O O     . HOH H 4 .   ? 6.815   50.413  -20.180 1.00 34.81  ? 850  HOH B O     1 
HETATM 8732 O O     . HOH H 4 .   ? 12.480  37.568  4.912   1.00 32.59  ? 851  HOH B O     1 
HETATM 8733 O O     . HOH H 4 .   ? -29.981 35.189  -3.939  1.00 39.32  ? 852  HOH B O     1 
HETATM 8734 O O     . HOH H 4 .   ? 9.843   25.061  9.685   1.00 52.26  ? 853  HOH B O     1 
HETATM 8735 O O     . HOH H 4 .   ? -19.921 35.133  0.229   1.00 42.37  ? 854  HOH B O     1 
HETATM 8736 O O     . HOH H 4 .   ? -23.273 59.102  -9.203  1.00 39.27  ? 855  HOH B O     1 
HETATM 8737 O O     . HOH H 4 .   ? -11.378 40.996  -4.865  1.00 40.84  ? 856  HOH B O     1 
HETATM 8738 O O     . HOH H 4 .   ? -11.286 33.652  16.594  1.00 47.94  ? 857  HOH B O     1 
HETATM 8739 O O     . HOH H 4 .   ? -7.725  61.581  -21.121 1.00 48.67  ? 858  HOH B O     1 
HETATM 8740 O O     . HOH H 4 .   ? -5.645  36.729  -4.800  1.00 29.94  ? 859  HOH B O     1 
HETATM 8741 O O     . HOH H 4 .   ? 11.167  63.775  -6.946  1.00 56.60  ? 860  HOH B O     1 
HETATM 8742 O O     . HOH H 4 .   ? -18.505 32.568  -0.895  1.00 33.15  ? 861  HOH B O     1 
HETATM 8743 O O     . HOH H 4 .   ? -27.063 33.455  7.030   1.00 45.20  ? 862  HOH B O     1 
HETATM 8744 O O     . HOH H 4 .   ? 6.857   49.499  4.843   1.00 44.30  ? 863  HOH B O     1 
HETATM 8745 O O     . HOH H 4 .   ? -23.779 26.727  -0.022  1.00 32.84  ? 864  HOH B O     1 
HETATM 8746 O O     . HOH H 4 .   ? -17.028 26.227  -6.451  1.00 35.89  ? 865  HOH B O     1 
HETATM 8747 O O     . HOH H 4 .   ? -17.022 47.826  -16.072 1.00 28.84  ? 866  HOH B O     1 
HETATM 8748 O O     . HOH H 4 .   ? 6.497   31.669  -0.190  1.00 39.49  ? 867  HOH B O     1 
HETATM 8749 O O     . HOH H 4 .   ? -17.580 45.598  5.482   1.00 52.34  ? 868  HOH B O     1 
HETATM 8750 O O     . HOH H 4 .   ? -30.907 53.174  -1.443  1.00 41.31  ? 869  HOH B O     1 
HETATM 8751 O O     . HOH H 4 .   ? 3.670   43.743  -7.556  1.00 41.29  ? 870  HOH B O     1 
HETATM 8752 O O     . HOH H 4 .   ? -20.883 31.094  -1.151  1.00 32.54  ? 871  HOH B O     1 
HETATM 8753 O O     . HOH H 4 .   ? -14.340 52.816  11.033  1.00 50.61  ? 872  HOH B O     1 
HETATM 8754 O O     . HOH H 4 .   ? -26.481 32.607  -7.826  1.00 25.75  ? 873  HOH B O     1 
HETATM 8755 O O     . HOH H 4 .   ? -22.385 58.172  -17.718 1.00 45.53  ? 874  HOH B O     1 
HETATM 8756 O O     . HOH H 4 .   ? -22.962 63.926  -12.178 1.00 57.19  ? 875  HOH B O     1 
HETATM 8757 O O     . HOH H 4 .   ? 8.393   26.039  4.997   1.00 31.34  ? 876  HOH B O     1 
HETATM 8758 O O     . HOH H 4 .   ? -3.077  19.870  13.387  1.00 45.48  ? 877  HOH B O     1 
HETATM 8759 O O     . HOH H 4 .   ? -17.994 32.767  -6.129  1.00 30.51  ? 878  HOH B O     1 
HETATM 8760 O O     . HOH H 4 .   ? -36.723 25.471  6.463   1.00 51.70  ? 879  HOH B O     1 
HETATM 8761 O O     . HOH H 4 .   ? -24.706 15.593  -4.923  1.00 38.12  ? 880  HOH B O     1 
HETATM 8762 O O     . HOH H 4 .   ? -8.765  51.880  11.731  1.00 47.49  ? 881  HOH B O     1 
HETATM 8763 O O     . HOH H 4 .   ? -14.990 22.223  -9.030  1.00 33.95  ? 882  HOH B O     1 
HETATM 8764 O O     . HOH H 4 .   ? -22.504 24.239  -18.416 1.00 40.20  ? 883  HOH B O     1 
HETATM 8765 O O     . HOH H 4 .   ? -18.369 9.549   2.489   1.00 46.48  ? 884  HOH B O     1 
HETATM 8766 O O     . HOH H 4 .   ? -33.056 38.707  -10.014 1.00 46.09  ? 885  HOH B O     1 
HETATM 8767 O O     . HOH H 4 .   ? -29.643 27.512  -8.661  1.00 42.38  ? 886  HOH B O     1 
HETATM 8768 O O     . HOH H 4 .   ? -7.605  11.776  6.401   1.00 48.25  ? 887  HOH B O     1 
HETATM 8769 O O     . HOH H 4 .   ? 6.816   31.070  14.975  1.00 46.20  ? 888  HOH B O     1 
HETATM 8770 O O     . HOH H 4 .   ? -19.607 31.133  3.120   1.00 35.35  ? 889  HOH B O     1 
HETATM 8771 O O     . HOH H 4 .   ? -22.031 17.795  -15.235 1.00 43.19  ? 890  HOH B O     1 
HETATM 8772 O O     . HOH H 4 .   ? 12.056  33.716  12.817  1.00 40.07  ? 891  HOH B O     1 
HETATM 8773 O O     . HOH H 4 .   ? -20.823 59.901  -9.119  1.00 53.94  ? 892  HOH B O     1 
HETATM 8774 O O     . HOH H 4 .   ? -19.335 28.771  1.818   1.00 36.96  ? 893  HOH B O     1 
HETATM 8775 O O     . HOH H 4 .   ? -20.352 19.302  25.121  1.00 48.82  ? 894  HOH B O     1 
HETATM 8776 O O     . HOH H 4 .   ? -11.477 44.447  3.077   1.00 31.31  ? 895  HOH B O     1 
HETATM 8777 O O     . HOH H 4 .   ? -12.435 25.054  -1.433  1.00 42.91  ? 896  HOH B O     1 
HETATM 8778 O O     . HOH H 4 .   ? -24.289 75.176  -3.289  1.00 52.13  ? 897  HOH B O     1 
HETATM 8779 O O     . HOH H 4 .   ? 12.026  35.714  14.581  1.00 48.33  ? 898  HOH B O     1 
HETATM 8780 O O     . HOH H 4 .   ? -19.405 41.842  9.142   1.00 49.56  ? 899  HOH B O     1 
HETATM 8781 O O     . HOH H 4 .   ? -10.450 61.769  1.407   1.00 55.90  ? 900  HOH B O     1 
HETATM 8782 O O     . HOH H 4 .   ? 0.796   30.676  -6.482  1.00 40.80  ? 901  HOH B O     1 
HETATM 8783 O O     . HOH H 4 .   ? 9.699   56.181  5.498   1.00 42.51  ? 902  HOH B O     1 
HETATM 8784 O O     . HOH H 4 .   ? -7.743  70.436  -17.080 1.00 49.38  ? 903  HOH B O     1 
HETATM 8785 O O     . HOH H 4 .   ? -6.080  71.546  -10.754 1.00 45.10  ? 904  HOH B O     1 
HETATM 8786 O O     . HOH H 4 .   ? -20.145 63.769  -12.096 1.00 48.55  ? 905  HOH B O     1 
HETATM 8787 O O     . HOH H 4 .   ? -15.773 66.756  -12.883 1.00 49.97  ? 906  HOH B O     1 
HETATM 8788 O O     . HOH H 4 .   ? -24.643 34.223  -20.170 1.00 50.85  ? 907  HOH B O     1 
HETATM 8789 O O     . HOH H 4 .   ? 3.051   39.760  21.280  1.00 67.97  ? 908  HOH B O     1 
HETATM 8790 O O     . HOH H 4 .   ? -21.589 28.964  0.292   1.00 28.78  ? 909  HOH B O     1 
HETATM 8791 O O     . HOH H 4 .   ? -23.931 22.606  -16.879 1.00 46.70  ? 910  HOH B O     1 
HETATM 8792 O O     . HOH H 4 .   ? -25.727 13.213  -4.115  1.00 48.29  ? 911  HOH B O     1 
HETATM 8793 O O     . HOH H 4 .   ? -29.478 37.211  2.955   1.00 55.27  ? 912  HOH B O     1 
HETATM 8794 O O     . HOH H 4 .   ? -19.904 37.824  10.641  1.00 53.01  ? 913  HOH B O     1 
HETATM 8795 O O     . HOH H 4 .   ? -16.533 34.761  -6.480  1.00 41.31  ? 914  HOH B O     1 
HETATM 8796 O O     . HOH H 4 .   ? -36.950 28.868  7.390   1.00 52.86  ? 915  HOH B O     1 
HETATM 8797 O O     . HOH H 4 .   ? -14.082 7.334   -1.769  1.00 50.80  ? 916  HOH B O     1 
HETATM 8798 O O     . HOH H 4 .   ? -28.112 56.369  -4.101  1.00 58.89  ? 917  HOH B O     1 
HETATM 8799 O O     . HOH H 4 .   ? -24.142 61.894  -13.527 1.00 46.01  ? 918  HOH B O     1 
HETATM 8800 O O     . HOH H 4 .   ? -18.702 74.395  0.597   1.00 52.49  ? 919  HOH B O     1 
HETATM 8801 O O     . HOH H 4 .   ? -28.239 32.622  -14.038 1.00 50.56  ? 920  HOH B O     1 
HETATM 8802 O O     . HOH H 4 .   ? -23.724 61.147  -11.720 1.00 46.31  ? 921  HOH B O     1 
HETATM 8803 O O     . HOH H 4 .   ? -31.885 62.022  -0.893  1.00 50.85  ? 922  HOH B O     1 
HETATM 8804 O O     . HOH H 4 .   ? -32.895 41.285  -10.487 1.00 51.28  ? 923  HOH B O     1 
HETATM 8805 O O     . HOH H 4 .   ? 5.558   20.098  5.880   1.00 47.07  ? 924  HOH B O     1 
HETATM 8806 O O     . HOH H 4 .   ? -0.037  42.660  -8.284  1.00 45.15  ? 925  HOH B O     1 
HETATM 8807 O O     . HOH H 4 .   ? -5.327  43.199  -8.060  1.00 49.19  ? 926  HOH B O     1 
HETATM 8808 O O     . HOH H 4 .   ? -24.150 24.957  -20.422 1.00 50.14  ? 927  HOH B O     1 
HETATM 8809 O O     . HOH H 4 .   ? -2.333  49.511  13.696  1.00 63.39  ? 928  HOH B O     1 
HETATM 8810 O O     . HOH H 4 .   ? -18.746 38.884  12.453  1.00 50.98  ? 929  HOH B O     1 
HETATM 8811 O O     . HOH H 4 .   ? -15.745 32.793  -28.667 1.00 48.31  ? 930  HOH B O     1 
HETATM 8812 O O     . HOH H 4 .   ? -29.196 33.236  -11.654 1.00 46.34  ? 931  HOH B O     1 
HETATM 8813 O O     . HOH H 4 .   ? -38.183 22.593  11.932  1.00 54.69  ? 932  HOH B O     1 
HETATM 8814 O O     . HOH H 4 .   ? -2.957  42.186  -7.697  1.00 52.79  ? 933  HOH B O     1 
HETATM 8815 O O     . HOH H 4 .   ? -26.070 25.577  -12.504 1.00 43.92  ? 934  HOH B O     1 
HETATM 8816 O O     . HOH H 4 .   ? -28.090 30.105  -14.191 1.00 52.71  ? 935  HOH B O     1 
HETATM 8817 O O     . HOH H 4 .   ? 21.673  33.736  7.782   1.00 56.76  ? 936  HOH B O     1 
HETATM 8818 O O     . HOH H 4 .   ? -23.463 28.148  -26.045 1.00 54.76  ? 937  HOH B O     1 
HETATM 8819 O O     . HOH H 4 .   ? -18.286 20.211  25.473  1.00 53.56  ? 938  HOH B O     1 
HETATM 8820 O O     . HOH H 4 .   ? -32.832 41.922  -13.120 1.00 44.50  ? 939  HOH B O     1 
HETATM 8821 O O     . HOH H 4 .   ? -11.858 12.261  -2.533  1.00 50.09  ? 940  HOH B O     1 
HETATM 8822 O O     . HOH H 4 .   ? -23.188 48.937  -23.811 1.00 45.45  ? 941  HOH B O     1 
HETATM 8823 O O     . HOH H 4 .   ? 14.196  25.837  7.245   1.00 54.09  ? 942  HOH B O     1 
HETATM 8824 O O     . HOH H 4 .   ? -27.437 12.421  -2.549  1.00 52.50  ? 943  HOH B O     1 
HETATM 8825 O O     . HOH H 4 .   ? -20.782 31.104  -26.652 1.00 49.23  ? 944  HOH B O     1 
HETATM 8826 O O     . HOH H 4 .   ? -24.707 28.116  -16.662 1.00 43.32  ? 945  HOH B O     1 
HETATM 8827 O O     . HOH H 4 .   ? -28.386 68.357  -13.025 1.00 50.25  ? 946  HOH B O     1 
HETATM 8828 O O     . HOH H 4 .   ? -17.132 25.478  -29.283 1.00 49.69  ? 947  HOH B O     1 
HETATM 8829 O O     . HOH H 4 .   ? -19.004 47.512  -17.919 1.00 34.63  ? 948  HOH B O     1 
HETATM 8830 O O     . HOH H 4 .   ? -15.982 24.197  -28.083 1.00 46.26  ? 949  HOH B O     1 
HETATM 8831 O O     . HOH H 4 .   ? -12.877 51.757  13.352  1.00 47.01  ? 950  HOH B O     1 
HETATM 8832 O O     . HOH H 4 .   ? 4.142   40.825  23.137  1.00 57.40  ? 951  HOH B O     1 
HETATM 8833 O O     . HOH H 4 .   ? 6.002   32.448  -4.214  1.00 31.82  ? 952  HOH B O     1 
HETATM 8834 O O     . HOH H 4 .   ? 1.354   40.387  -8.421  1.00 37.56  ? 953  HOH B O     1 
HETATM 8835 O O     . HOH H 4 .   ? 18.750  32.007  6.925   1.00 51.59  ? 954  HOH B O     1 
HETATM 8836 O O     . HOH H 4 .   ? 1.772   51.210  -23.389 1.00 48.85  ? 955  HOH B O     1 
HETATM 8837 O O     . HOH H 4 .   ? 0.360   51.996  12.943  1.00 48.79  ? 956  HOH B O     1 
HETATM 8838 O O     . HOH H 4 .   ? -27.093 33.964  -21.030 1.00 51.02  ? 957  HOH B O     1 
HETATM 8839 O O     . HOH H 4 .   ? -12.846 5.762   -3.481  1.00 61.45  ? 958  HOH B O     1 
# 
