data_9GP0
# 
_entry.id   9GP0 
# 
_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   9GP0         pdb_00009gp0 10.2210/pdb9gp0/pdb 
WWPDB D_1292141576 ?            ?                   
# 
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                        9GP0 
_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 
'Mattevi, A.'  1 0000-0002-9523-7128 
'Alvigini, L.' 2 ?                   
# 
_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 'FLAVIN-ADENINE DINUCLEOTIDE'                         785.550   2   ? ? ? ? 
3 non-polymer syn 4-hydroxy-3-methoxybenzaldehyde                       152.147   2   ? ? ? ? 
4 water       nat water                                                 18.015    558 ? ? ? ? 
# 
_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 'FLAVIN-ADENINE DINUCLEOTIDE'   FAD 
3 4-hydroxy-3-methoxybenzaldehyde V55 
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 
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 
V55 non-polymer         . 4-hydroxy-3-methoxybenzaldehyde p-vanillin 'C8 H8 O3'          152.147 
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 ASP 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   3   ARG ARG 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 ASP 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        V55 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   V55 
_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 FAD 1   601  601  FAD FAD A . 
D 3 V55 1   602  602  V55 V55 A . 
E 2 FAD 1   601  601  FAD FAD B . 
F 3 V55 1   602  602  V55 V55 B . 
G 4 HOH 1   701  703  HOH HOH A . 
G 4 HOH 2   702  704  HOH HOH A . 
G 4 HOH 3   703  705  HOH HOH A . 
G 4 HOH 4   704  706  HOH HOH A . 
G 4 HOH 5   705  707  HOH HOH A . 
G 4 HOH 6   706  708  HOH HOH A . 
G 4 HOH 7   707  709  HOH HOH A . 
G 4 HOH 8   708  710  HOH HOH A . 
G 4 HOH 9   709  711  HOH HOH A . 
G 4 HOH 10  710  712  HOH HOH A . 
G 4 HOH 11  711  713  HOH HOH A . 
G 4 HOH 12  712  714  HOH HOH A . 
G 4 HOH 13  713  716  HOH HOH A . 
G 4 HOH 14  714  715  HOH HOH A . 
G 4 HOH 15  715  717  HOH HOH A . 
G 4 HOH 16  716  718  HOH HOH A . 
G 4 HOH 17  717  719  HOH HOH A . 
G 4 HOH 18  718  720  HOH HOH A . 
G 4 HOH 19  719  721  HOH HOH A . 
G 4 HOH 20  720  722  HOH HOH A . 
G 4 HOH 21  721  723  HOH HOH A . 
G 4 HOH 22  722  724  HOH HOH A . 
G 4 HOH 23  723  725  HOH HOH A . 
G 4 HOH 24  724  727  HOH HOH A . 
G 4 HOH 25  725  728  HOH HOH A . 
G 4 HOH 26  726  729  HOH HOH A . 
G 4 HOH 27  727  730  HOH HOH A . 
G 4 HOH 28  728  731  HOH HOH A . 
G 4 HOH 29  729  732  HOH HOH A . 
G 4 HOH 30  730  733  HOH HOH A . 
G 4 HOH 31  731  702  HOH HOH A . 
G 4 HOH 32  732  734  HOH HOH A . 
G 4 HOH 33  733  735  HOH HOH A . 
G 4 HOH 34  734  736  HOH HOH A . 
G 4 HOH 35  735  737  HOH HOH A . 
G 4 HOH 36  736  738  HOH HOH A . 
G 4 HOH 37  737  739  HOH HOH A . 
G 4 HOH 38  738  740  HOH HOH A . 
G 4 HOH 39  739  741  HOH HOH A . 
G 4 HOH 40  740  742  HOH HOH A . 
G 4 HOH 41  741  743  HOH HOH A . 
G 4 HOH 42  742  744  HOH HOH A . 
G 4 HOH 43  743  745  HOH HOH A . 
G 4 HOH 44  744  746  HOH HOH A . 
G 4 HOH 45  745  747  HOH HOH A . 
G 4 HOH 46  746  751  HOH HOH A . 
G 4 HOH 47  747  748  HOH HOH A . 
G 4 HOH 48  748  749  HOH HOH A . 
G 4 HOH 49  749  750  HOH HOH A . 
G 4 HOH 50  750  752  HOH HOH A . 
G 4 HOH 51  751  753  HOH HOH A . 
G 4 HOH 52  752  754  HOH HOH A . 
G 4 HOH 53  753  755  HOH HOH A . 
G 4 HOH 54  754  756  HOH HOH A . 
G 4 HOH 55  755  757  HOH HOH A . 
G 4 HOH 56  756  758  HOH HOH A . 
G 4 HOH 57  757  759  HOH HOH A . 
G 4 HOH 58  758  760  HOH HOH A . 
G 4 HOH 59  759  761  HOH HOH A . 
G 4 HOH 60  760  762  HOH HOH A . 
G 4 HOH 61  761  763  HOH HOH A . 
G 4 HOH 62  762  764  HOH HOH A . 
G 4 HOH 63  763  765  HOH HOH A . 
G 4 HOH 64  764  766  HOH HOH A . 
G 4 HOH 65  765  767  HOH HOH A . 
G 4 HOH 66  766  768  HOH HOH A . 
G 4 HOH 67  767  769  HOH HOH A . 
G 4 HOH 68  768  770  HOH HOH A . 
G 4 HOH 69  769  771  HOH HOH A . 
G 4 HOH 70  770  772  HOH HOH A . 
G 4 HOH 71  771  773  HOH HOH A . 
G 4 HOH 72  772  774  HOH HOH A . 
G 4 HOH 73  773  775  HOH HOH A . 
G 4 HOH 74  774  776  HOH HOH A . 
G 4 HOH 75  775  777  HOH HOH A . 
G 4 HOH 76  776  778  HOH HOH A . 
G 4 HOH 77  777  779  HOH HOH A . 
G 4 HOH 78  778  780  HOH HOH A . 
G 4 HOH 79  779  781  HOH HOH A . 
G 4 HOH 80  780  782  HOH HOH A . 
G 4 HOH 81  781  783  HOH HOH A . 
G 4 HOH 82  782  784  HOH HOH A . 
G 4 HOH 83  783  785  HOH HOH A . 
G 4 HOH 84  784  786  HOH HOH A . 
G 4 HOH 85  785  787  HOH HOH A . 
G 4 HOH 86  786  788  HOH HOH A . 
G 4 HOH 87  787  789  HOH HOH A . 
G 4 HOH 88  788  790  HOH HOH A . 
G 4 HOH 89  789  791  HOH HOH A . 
G 4 HOH 90  790  792  HOH HOH A . 
G 4 HOH 91  791  793  HOH HOH A . 
G 4 HOH 92  792  794  HOH HOH A . 
G 4 HOH 93  793  795  HOH HOH A . 
G 4 HOH 94  794  796  HOH HOH A . 
G 4 HOH 95  795  797  HOH HOH A . 
G 4 HOH 96  796  798  HOH HOH A . 
G 4 HOH 97  797  799  HOH HOH A . 
G 4 HOH 98  798  800  HOH HOH A . 
G 4 HOH 99  799  801  HOH HOH A . 
G 4 HOH 100 800  802  HOH HOH A . 
G 4 HOH 101 801  803  HOH HOH A . 
G 4 HOH 102 802  804  HOH HOH A . 
G 4 HOH 103 803  805  HOH HOH A . 
G 4 HOH 104 804  806  HOH HOH A . 
G 4 HOH 105 805  807  HOH HOH A . 
G 4 HOH 106 806  808  HOH HOH A . 
G 4 HOH 107 807  809  HOH HOH A . 
G 4 HOH 108 808  810  HOH HOH A . 
G 4 HOH 109 809  811  HOH HOH A . 
G 4 HOH 110 810  813  HOH HOH A . 
G 4 HOH 111 811  814  HOH HOH A . 
G 4 HOH 112 812  815  HOH HOH A . 
G 4 HOH 113 813  816  HOH HOH A . 
G 4 HOH 114 814  817  HOH HOH A . 
G 4 HOH 115 815  818  HOH HOH A . 
G 4 HOH 116 816  819  HOH HOH A . 
G 4 HOH 117 817  820  HOH HOH A . 
G 4 HOH 118 818  821  HOH HOH A . 
G 4 HOH 119 819  822  HOH HOH A . 
G 4 HOH 120 820  823  HOH HOH A . 
G 4 HOH 121 821  824  HOH HOH A . 
G 4 HOH 122 822  825  HOH HOH A . 
G 4 HOH 123 823  826  HOH HOH A . 
G 4 HOH 124 824  827  HOH HOH A . 
G 4 HOH 125 825  828  HOH HOH A . 
G 4 HOH 126 826  812  HOH HOH A . 
G 4 HOH 127 827  829  HOH HOH A . 
G 4 HOH 128 828  830  HOH HOH A . 
G 4 HOH 129 829  831  HOH HOH A . 
G 4 HOH 130 830  832  HOH HOH A . 
G 4 HOH 131 831  833  HOH HOH A . 
G 4 HOH 132 832  834  HOH HOH A . 
G 4 HOH 133 833  835  HOH HOH A . 
G 4 HOH 134 834  836  HOH HOH A . 
G 4 HOH 135 835  837  HOH HOH A . 
G 4 HOH 136 836  838  HOH HOH A . 
G 4 HOH 137 837  839  HOH HOH A . 
G 4 HOH 138 838  840  HOH HOH A . 
G 4 HOH 139 839  841  HOH HOH A . 
G 4 HOH 140 840  842  HOH HOH A . 
G 4 HOH 141 841  843  HOH HOH A . 
G 4 HOH 142 842  844  HOH HOH A . 
G 4 HOH 143 843  845  HOH HOH A . 
G 4 HOH 144 844  846  HOH HOH A . 
G 4 HOH 145 845  726  HOH HOH A . 
G 4 HOH 146 846  847  HOH HOH A . 
G 4 HOH 147 847  848  HOH HOH A . 
G 4 HOH 148 848  849  HOH HOH A . 
G 4 HOH 149 849  850  HOH HOH A . 
G 4 HOH 150 850  851  HOH HOH A . 
G 4 HOH 151 851  852  HOH HOH A . 
G 4 HOH 152 852  853  HOH HOH A . 
G 4 HOH 153 853  854  HOH HOH A . 
G 4 HOH 154 854  855  HOH HOH A . 
G 4 HOH 155 855  856  HOH HOH A . 
G 4 HOH 156 856  857  HOH HOH A . 
G 4 HOH 157 857  858  HOH HOH A . 
G 4 HOH 158 858  859  HOH HOH A . 
G 4 HOH 159 859  860  HOH HOH A . 
G 4 HOH 160 860  861  HOH HOH A . 
G 4 HOH 161 861  862  HOH HOH A . 
G 4 HOH 162 862  863  HOH HOH A . 
G 4 HOH 163 863  864  HOH HOH A . 
G 4 HOH 164 864  865  HOH HOH A . 
G 4 HOH 165 865  866  HOH HOH A . 
G 4 HOH 166 866  867  HOH HOH A . 
G 4 HOH 167 867  868  HOH HOH A . 
G 4 HOH 168 868  869  HOH HOH A . 
G 4 HOH 169 869  870  HOH HOH A . 
G 4 HOH 170 870  871  HOH HOH A . 
G 4 HOH 171 871  872  HOH HOH A . 
G 4 HOH 172 872  873  HOH HOH A . 
G 4 HOH 173 873  874  HOH HOH A . 
G 4 HOH 174 874  875  HOH HOH A . 
G 4 HOH 175 875  876  HOH HOH A . 
G 4 HOH 176 876  877  HOH HOH A . 
G 4 HOH 177 877  878  HOH HOH A . 
G 4 HOH 178 878  879  HOH HOH A . 
G 4 HOH 179 879  880  HOH HOH A . 
G 4 HOH 180 880  881  HOH HOH A . 
G 4 HOH 181 881  882  HOH HOH A . 
G 4 HOH 182 882  883  HOH HOH A . 
G 4 HOH 183 883  884  HOH HOH A . 
G 4 HOH 184 884  885  HOH HOH A . 
G 4 HOH 185 885  886  HOH HOH A . 
G 4 HOH 186 886  887  HOH HOH A . 
G 4 HOH 187 887  888  HOH HOH A . 
G 4 HOH 188 888  889  HOH HOH A . 
G 4 HOH 189 889  890  HOH HOH A . 
G 4 HOH 190 890  891  HOH HOH A . 
G 4 HOH 191 891  892  HOH HOH A . 
G 4 HOH 192 892  893  HOH HOH A . 
G 4 HOH 193 893  894  HOH HOH A . 
G 4 HOH 194 894  895  HOH HOH A . 
G 4 HOH 195 895  896  HOH HOH A . 
G 4 HOH 196 896  897  HOH HOH A . 
G 4 HOH 197 897  898  HOH HOH A . 
G 4 HOH 198 898  899  HOH HOH A . 
G 4 HOH 199 899  900  HOH HOH A . 
G 4 HOH 200 900  901  HOH HOH A . 
G 4 HOH 201 901  902  HOH HOH A . 
G 4 HOH 202 902  903  HOH HOH A . 
G 4 HOH 203 903  904  HOH HOH A . 
G 4 HOH 204 904  905  HOH HOH A . 
G 4 HOH 205 905  906  HOH HOH A . 
G 4 HOH 206 906  907  HOH HOH A . 
G 4 HOH 207 907  908  HOH HOH A . 
G 4 HOH 208 908  909  HOH HOH A . 
G 4 HOH 209 909  910  HOH HOH A . 
G 4 HOH 210 910  911  HOH HOH A . 
G 4 HOH 211 911  912  HOH HOH A . 
G 4 HOH 212 912  913  HOH HOH A . 
G 4 HOH 213 913  914  HOH HOH A . 
G 4 HOH 214 914  915  HOH HOH A . 
G 4 HOH 215 915  916  HOH HOH A . 
G 4 HOH 216 916  917  HOH HOH A . 
G 4 HOH 217 917  918  HOH HOH A . 
G 4 HOH 218 918  919  HOH HOH A . 
G 4 HOH 219 919  920  HOH HOH A . 
G 4 HOH 220 920  921  HOH HOH A . 
G 4 HOH 221 921  922  HOH HOH A . 
G 4 HOH 222 922  923  HOH HOH A . 
G 4 HOH 223 923  924  HOH HOH A . 
G 4 HOH 224 924  925  HOH HOH A . 
G 4 HOH 225 925  926  HOH HOH A . 
G 4 HOH 226 926  927  HOH HOH A . 
G 4 HOH 227 927  928  HOH HOH A . 
G 4 HOH 228 928  929  HOH HOH A . 
G 4 HOH 229 929  930  HOH HOH A . 
G 4 HOH 230 930  931  HOH HOH A . 
G 4 HOH 231 931  932  HOH HOH A . 
G 4 HOH 232 932  933  HOH HOH A . 
G 4 HOH 233 933  934  HOH HOH A . 
G 4 HOH 234 934  935  HOH HOH A . 
G 4 HOH 235 935  936  HOH HOH A . 
G 4 HOH 236 936  937  HOH HOH A . 
G 4 HOH 237 937  938  HOH HOH A . 
G 4 HOH 238 938  939  HOH HOH A . 
G 4 HOH 239 939  940  HOH HOH A . 
G 4 HOH 240 940  941  HOH HOH A . 
G 4 HOH 241 941  942  HOH HOH A . 
G 4 HOH 242 942  943  HOH HOH A . 
G 4 HOH 243 943  944  HOH HOH A . 
G 4 HOH 244 944  945  HOH HOH A . 
G 4 HOH 245 945  946  HOH HOH A . 
G 4 HOH 246 946  947  HOH HOH A . 
G 4 HOH 247 947  948  HOH HOH A . 
G 4 HOH 248 948  949  HOH HOH A . 
G 4 HOH 249 949  950  HOH HOH A . 
G 4 HOH 250 950  951  HOH HOH A . 
G 4 HOH 251 951  952  HOH HOH A . 
G 4 HOH 252 952  953  HOH HOH A . 
G 4 HOH 253 953  954  HOH HOH A . 
G 4 HOH 254 954  955  HOH HOH A . 
G 4 HOH 255 955  956  HOH HOH A . 
G 4 HOH 256 956  957  HOH HOH A . 
G 4 HOH 257 957  958  HOH HOH A . 
G 4 HOH 258 958  959  HOH HOH A . 
G 4 HOH 259 959  960  HOH HOH A . 
G 4 HOH 260 960  961  HOH HOH A . 
G 4 HOH 261 961  962  HOH HOH A . 
G 4 HOH 262 962  963  HOH HOH A . 
G 4 HOH 263 963  964  HOH HOH A . 
G 4 HOH 264 964  965  HOH HOH A . 
G 4 HOH 265 965  966  HOH HOH A . 
G 4 HOH 266 966  967  HOH HOH A . 
G 4 HOH 267 967  968  HOH HOH A . 
G 4 HOH 268 968  969  HOH HOH A . 
G 4 HOH 269 969  970  HOH HOH A . 
G 4 HOH 270 970  971  HOH HOH A . 
G 4 HOH 271 971  972  HOH HOH A . 
G 4 HOH 272 972  973  HOH HOH A . 
G 4 HOH 273 973  974  HOH HOH A . 
G 4 HOH 274 974  975  HOH HOH A . 
G 4 HOH 275 975  976  HOH HOH A . 
G 4 HOH 276 976  977  HOH HOH A . 
G 4 HOH 277 977  978  HOH HOH A . 
G 4 HOH 278 978  979  HOH HOH A . 
G 4 HOH 279 979  980  HOH HOH A . 
G 4 HOH 280 980  981  HOH HOH A . 
G 4 HOH 281 981  982  HOH HOH A . 
G 4 HOH 282 982  983  HOH HOH A . 
G 4 HOH 283 983  984  HOH HOH A . 
G 4 HOH 284 984  985  HOH HOH A . 
G 4 HOH 285 985  986  HOH HOH A . 
G 4 HOH 286 986  987  HOH HOH A . 
G 4 HOH 287 987  988  HOH HOH A . 
G 4 HOH 288 988  989  HOH HOH A . 
G 4 HOH 289 989  990  HOH HOH A . 
G 4 HOH 290 990  991  HOH HOH A . 
G 4 HOH 291 991  992  HOH HOH A . 
G 4 HOH 292 992  993  HOH HOH A . 
G 4 HOH 293 993  994  HOH HOH A . 
G 4 HOH 294 994  995  HOH HOH A . 
G 4 HOH 295 995  996  HOH HOH A . 
G 4 HOH 296 996  997  HOH HOH A . 
G 4 HOH 297 997  998  HOH HOH A . 
G 4 HOH 298 998  999  HOH HOH A . 
G 4 HOH 299 999  1000 HOH HOH A . 
G 4 HOH 300 1000 1001 HOH HOH A . 
G 4 HOH 301 1001 1002 HOH HOH A . 
G 4 HOH 302 1002 1003 HOH HOH A . 
G 4 HOH 303 1003 1004 HOH HOH A . 
G 4 HOH 304 1004 1005 HOH HOH A . 
G 4 HOH 305 1005 1006 HOH HOH A . 
G 4 HOH 306 1006 1007 HOH HOH A . 
G 4 HOH 307 1007 1008 HOH HOH A . 
G 4 HOH 308 1008 1010 HOH HOH A . 
G 4 HOH 309 1009 1011 HOH HOH A . 
G 4 HOH 310 1010 1009 HOH HOH A . 
G 4 HOH 311 1011 1012 HOH HOH A . 
G 4 HOH 312 1012 1013 HOH HOH A . 
G 4 HOH 313 1013 1014 HOH HOH A . 
G 4 HOH 314 1014 1015 HOH HOH A . 
G 4 HOH 315 1015 1016 HOH HOH A . 
G 4 HOH 316 1016 1017 HOH HOH A . 
G 4 HOH 317 1017 1018 HOH HOH A . 
G 4 HOH 318 1018 1019 HOH HOH A . 
H 4 HOH 1   701  702  HOH HOH B . 
H 4 HOH 2   702  703  HOH HOH B . 
H 4 HOH 3   703  704  HOH HOH B . 
H 4 HOH 4   704  705  HOH HOH B . 
H 4 HOH 5   705  706  HOH HOH B . 
H 4 HOH 6   706  708  HOH HOH B . 
H 4 HOH 7   707  709  HOH HOH B . 
H 4 HOH 8   708  710  HOH HOH B . 
H 4 HOH 9   709  711  HOH HOH B . 
H 4 HOH 10  710  712  HOH HOH B . 
H 4 HOH 11  711  713  HOH HOH B . 
H 4 HOH 12  712  714  HOH HOH B . 
H 4 HOH 13  713  715  HOH HOH B . 
H 4 HOH 14  714  716  HOH HOH B . 
H 4 HOH 15  715  717  HOH HOH B . 
H 4 HOH 16  716  718  HOH HOH B . 
H 4 HOH 17  717  719  HOH HOH B . 
H 4 HOH 18  718  720  HOH HOH B . 
H 4 HOH 19  719  721  HOH HOH B . 
H 4 HOH 20  720  723  HOH HOH B . 
H 4 HOH 21  721  724  HOH HOH B . 
H 4 HOH 22  722  725  HOH HOH B . 
H 4 HOH 23  723  727  HOH HOH B . 
H 4 HOH 24  724  729  HOH HOH B . 
H 4 HOH 25  725  730  HOH HOH B . 
H 4 HOH 26  726  731  HOH HOH B . 
H 4 HOH 27  727  732  HOH HOH B . 
H 4 HOH 28  728  733  HOH HOH B . 
H 4 HOH 29  729  707  HOH HOH B . 
H 4 HOH 30  730  734  HOH HOH B . 
H 4 HOH 31  731  735  HOH HOH B . 
H 4 HOH 32  732  736  HOH HOH B . 
H 4 HOH 33  733  737  HOH HOH B . 
H 4 HOH 34  734  739  HOH HOH B . 
H 4 HOH 35  735  740  HOH HOH B . 
H 4 HOH 36  736  741  HOH HOH B . 
H 4 HOH 37  737  742  HOH HOH B . 
H 4 HOH 38  738  743  HOH HOH B . 
H 4 HOH 39  739  745  HOH HOH B . 
H 4 HOH 40  740  746  HOH HOH B . 
H 4 HOH 41  741  748  HOH HOH B . 
H 4 HOH 42  742  747  HOH HOH B . 
H 4 HOH 43  743  749  HOH HOH B . 
H 4 HOH 44  744  750  HOH HOH B . 
H 4 HOH 45  745  751  HOH HOH B . 
H 4 HOH 46  746  752  HOH HOH B . 
H 4 HOH 47  747  753  HOH HOH B . 
H 4 HOH 48  748  754  HOH HOH B . 
H 4 HOH 49  749  755  HOH HOH B . 
H 4 HOH 50  750  756  HOH HOH B . 
H 4 HOH 51  751  757  HOH HOH B . 
H 4 HOH 52  752  758  HOH HOH B . 
H 4 HOH 53  753  760  HOH HOH B . 
H 4 HOH 54  754  761  HOH HOH B . 
H 4 HOH 55  755  762  HOH HOH B . 
H 4 HOH 56  756  763  HOH HOH B . 
H 4 HOH 57  757  764  HOH HOH B . 
H 4 HOH 58  758  765  HOH HOH B . 
H 4 HOH 59  759  766  HOH HOH B . 
H 4 HOH 60  760  767  HOH HOH B . 
H 4 HOH 61  761  722  HOH HOH B . 
H 4 HOH 62  762  768  HOH HOH B . 
H 4 HOH 63  763  769  HOH HOH B . 
H 4 HOH 64  764  771  HOH HOH B . 
H 4 HOH 65  765  772  HOH HOH B . 
H 4 HOH 66  766  773  HOH HOH B . 
H 4 HOH 67  767  774  HOH HOH B . 
H 4 HOH 68  768  775  HOH HOH B . 
H 4 HOH 69  769  776  HOH HOH B . 
H 4 HOH 70  770  738  HOH HOH B . 
H 4 HOH 71  771  777  HOH HOH B . 
H 4 HOH 72  772  778  HOH HOH B . 
H 4 HOH 73  773  779  HOH HOH B . 
H 4 HOH 74  774  780  HOH HOH B . 
H 4 HOH 75  775  781  HOH HOH B . 
H 4 HOH 76  776  782  HOH HOH B . 
H 4 HOH 77  777  783  HOH HOH B . 
H 4 HOH 78  778  785  HOH HOH B . 
H 4 HOH 79  779  786  HOH HOH B . 
H 4 HOH 80  780  770  HOH HOH B . 
H 4 HOH 81  781  787  HOH HOH B . 
H 4 HOH 82  782  788  HOH HOH B . 
H 4 HOH 83  783  789  HOH HOH B . 
H 4 HOH 84  784  790  HOH HOH B . 
H 4 HOH 85  785  791  HOH HOH B . 
H 4 HOH 86  786  792  HOH HOH B . 
H 4 HOH 87  787  793  HOH HOH B . 
H 4 HOH 88  788  794  HOH HOH B . 
H 4 HOH 89  789  795  HOH HOH B . 
H 4 HOH 90  790  796  HOH HOH B . 
H 4 HOH 91  791  797  HOH HOH B . 
H 4 HOH 92  792  726  HOH HOH B . 
H 4 HOH 93  793  798  HOH HOH B . 
H 4 HOH 94  794  728  HOH HOH B . 
H 4 HOH 95  795  799  HOH HOH B . 
H 4 HOH 96  796  800  HOH HOH B . 
H 4 HOH 97  797  801  HOH HOH B . 
H 4 HOH 98  798  802  HOH HOH B . 
H 4 HOH 99  799  803  HOH HOH B . 
H 4 HOH 100 800  759  HOH HOH B . 
H 4 HOH 101 801  744  HOH HOH B . 
H 4 HOH 102 802  804  HOH HOH B . 
H 4 HOH 103 803  805  HOH HOH B . 
H 4 HOH 104 804  806  HOH HOH B . 
H 4 HOH 105 805  807  HOH HOH B . 
H 4 HOH 106 806  808  HOH HOH B . 
H 4 HOH 107 807  809  HOH HOH B . 
H 4 HOH 108 808  810  HOH HOH B . 
H 4 HOH 109 809  811  HOH HOH B . 
H 4 HOH 110 810  812  HOH HOH B . 
H 4 HOH 111 811  813  HOH HOH B . 
H 4 HOH 112 812  814  HOH HOH B . 
H 4 HOH 113 813  815  HOH HOH B . 
H 4 HOH 114 814  816  HOH HOH B . 
H 4 HOH 115 815  824  HOH HOH B . 
H 4 HOH 116 816  817  HOH HOH B . 
H 4 HOH 117 817  818  HOH HOH B . 
H 4 HOH 118 818  819  HOH HOH B . 
H 4 HOH 119 819  820  HOH HOH B . 
H 4 HOH 120 820  821  HOH HOH B . 
H 4 HOH 121 821  822  HOH HOH B . 
H 4 HOH 122 822  784  HOH HOH B . 
H 4 HOH 123 823  823  HOH HOH B . 
H 4 HOH 124 824  825  HOH HOH B . 
H 4 HOH 125 825  826  HOH HOH B . 
H 4 HOH 126 826  827  HOH HOH B . 
H 4 HOH 127 827  828  HOH HOH B . 
H 4 HOH 128 828  829  HOH HOH B . 
H 4 HOH 129 829  830  HOH HOH B . 
H 4 HOH 130 830  831  HOH HOH B . 
H 4 HOH 131 831  832  HOH HOH B . 
H 4 HOH 132 832  833  HOH HOH B . 
H 4 HOH 133 833  834  HOH HOH B . 
H 4 HOH 134 834  835  HOH HOH B . 
H 4 HOH 135 835  836  HOH HOH B . 
H 4 HOH 136 836  837  HOH HOH B . 
H 4 HOH 137 837  838  HOH HOH B . 
H 4 HOH 138 838  839  HOH HOH B . 
H 4 HOH 139 839  840  HOH HOH B . 
H 4 HOH 140 840  841  HOH HOH B . 
H 4 HOH 141 841  842  HOH HOH B . 
H 4 HOH 142 842  843  HOH HOH B . 
H 4 HOH 143 843  844  HOH HOH B . 
H 4 HOH 144 844  845  HOH HOH B . 
H 4 HOH 145 845  846  HOH HOH B . 
H 4 HOH 146 846  847  HOH HOH B . 
H 4 HOH 147 847  848  HOH HOH B . 
H 4 HOH 148 848  849  HOH HOH B . 
H 4 HOH 149 849  850  HOH HOH B . 
H 4 HOH 150 850  852  HOH HOH B . 
H 4 HOH 151 851  853  HOH HOH B . 
H 4 HOH 152 852  854  HOH HOH B . 
H 4 HOH 153 853  855  HOH HOH B . 
H 4 HOH 154 854  856  HOH HOH B . 
H 4 HOH 155 855  857  HOH HOH B . 
H 4 HOH 156 856  859  HOH HOH B . 
H 4 HOH 157 857  860  HOH HOH B . 
H 4 HOH 158 858  861  HOH HOH B . 
H 4 HOH 159 859  862  HOH HOH B . 
H 4 HOH 160 860  863  HOH HOH B . 
H 4 HOH 161 861  864  HOH HOH B . 
H 4 HOH 162 862  865  HOH HOH B . 
H 4 HOH 163 863  866  HOH HOH B . 
H 4 HOH 164 864  851  HOH HOH B . 
H 4 HOH 165 865  867  HOH HOH B . 
H 4 HOH 166 866  868  HOH HOH B . 
H 4 HOH 167 867  869  HOH HOH B . 
H 4 HOH 168 868  870  HOH HOH B . 
H 4 HOH 169 869  871  HOH HOH B . 
H 4 HOH 170 870  872  HOH HOH B . 
H 4 HOH 171 871  858  HOH HOH B . 
H 4 HOH 172 872  873  HOH HOH B . 
H 4 HOH 173 873  874  HOH HOH B . 
H 4 HOH 174 874  875  HOH HOH B . 
H 4 HOH 175 875  876  HOH HOH B . 
H 4 HOH 176 876  877  HOH HOH B . 
H 4 HOH 177 877  878  HOH HOH B . 
H 4 HOH 178 878  879  HOH HOH B . 
H 4 HOH 179 879  880  HOH HOH B . 
H 4 HOH 180 880  881  HOH HOH B . 
H 4 HOH 181 881  882  HOH HOH B . 
H 4 HOH 182 882  883  HOH HOH B . 
H 4 HOH 183 883  884  HOH HOH B . 
H 4 HOH 184 884  885  HOH HOH B . 
H 4 HOH 185 885  886  HOH HOH B . 
H 4 HOH 186 886  887  HOH HOH B . 
H 4 HOH 187 887  888  HOH HOH B . 
H 4 HOH 188 888  889  HOH HOH B . 
H 4 HOH 189 889  890  HOH HOH B . 
H 4 HOH 190 890  891  HOH HOH B . 
H 4 HOH 191 891  892  HOH HOH B . 
H 4 HOH 192 892  893  HOH HOH B . 
H 4 HOH 193 893  894  HOH HOH B . 
H 4 HOH 194 894  895  HOH HOH B . 
H 4 HOH 195 895  896  HOH HOH B . 
H 4 HOH 196 896  897  HOH HOH B . 
H 4 HOH 197 897  898  HOH HOH B . 
H 4 HOH 198 898  899  HOH HOH B . 
H 4 HOH 199 899  900  HOH HOH B . 
H 4 HOH 200 900  901  HOH HOH B . 
H 4 HOH 201 901  902  HOH HOH B . 
H 4 HOH 202 902  903  HOH HOH B . 
H 4 HOH 203 903  904  HOH HOH B . 
H 4 HOH 204 904  905  HOH HOH B . 
H 4 HOH 205 905  907  HOH HOH B . 
H 4 HOH 206 906  908  HOH HOH B . 
H 4 HOH 207 907  909  HOH HOH B . 
H 4 HOH 208 908  910  HOH HOH B . 
H 4 HOH 209 909  911  HOH HOH B . 
H 4 HOH 210 910  912  HOH HOH B . 
H 4 HOH 211 911  914  HOH HOH B . 
H 4 HOH 212 912  915  HOH HOH B . 
H 4 HOH 213 913  913  HOH HOH B . 
H 4 HOH 214 914  916  HOH HOH B . 
H 4 HOH 215 915  917  HOH HOH B . 
H 4 HOH 216 916  918  HOH HOH B . 
H 4 HOH 217 917  906  HOH HOH B . 
H 4 HOH 218 918  919  HOH HOH B . 
H 4 HOH 219 919  920  HOH HOH B . 
H 4 HOH 220 920  921  HOH HOH B . 
H 4 HOH 221 921  922  HOH HOH B . 
H 4 HOH 222 922  923  HOH HOH B . 
H 4 HOH 223 923  924  HOH HOH B . 
H 4 HOH 224 924  925  HOH HOH B . 
H 4 HOH 225 925  926  HOH HOH B . 
H 4 HOH 226 926  927  HOH HOH B . 
H 4 HOH 227 927  928  HOH HOH B . 
H 4 HOH 228 928  929  HOH HOH B . 
H 4 HOH 229 929  930  HOH HOH B . 
H 4 HOH 230 930  931  HOH HOH B . 
H 4 HOH 231 931  932  HOH HOH B . 
H 4 HOH 232 932  933  HOH HOH B . 
H 4 HOH 233 933  934  HOH HOH B . 
H 4 HOH 234 934  935  HOH HOH B . 
H 4 HOH 235 935  936  HOH HOH B . 
H 4 HOH 236 936  937  HOH HOH B . 
H 4 HOH 237 937  938  HOH HOH B . 
H 4 HOH 238 938  939  HOH HOH B . 
H 4 HOH 239 939  940  HOH HOH B . 
H 4 HOH 240 940  941  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                     9GP0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     83.419 
_cell.length_a_esd                 ? 
_cell.length_b                     83.419 
_cell.length_b_esd                 ? 
_cell.length_c                     298.892 
_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                         9GP0 
_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                   9GP0 
_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             2.46 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.02 
_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              ? 
_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 MgCl2  6 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 EIGER R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-01-13 
_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   0.965460 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.965460 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-3 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GP0 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.75 
_reflns.d_resolution_low                               74.72 
_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                                     116790 
_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                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.08 
_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                                0.118 
_reflns.pdbx_Rpim_I_all                                0.048 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       630911 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.107 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.75 
_reflns_shell.d_res_low                                     1.78 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           27255 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5798 
_reflns_shell.percent_possible_obs                          98.9 
_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                               4.7 
_reflns_shell.pdbx_chi_squared                              0.84 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.9 
_reflns_shell.pdbx_Rrim_I_all                               1.524 
_reflns_shell.pdbx_Rpim_I_all                               0.636 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.307 
_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                                  1.371 
_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]                            0.37000 
_refine.aniso_B[1][2]                            0.18000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            0.37000 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -1.20000 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.61 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_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                                 9GP0 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.75 
_refine.ls_d_res_low                             72.24 
_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                     110831 
_refine.ls_number_reflns_R_free                  5790 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.0 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.196 
_refine.ls_R_factor_R_free                       0.227 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.194 
_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                       0.119 
_refine.pdbx_overall_ESU_R_Free                  0.115 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             3.544 
_refine.overall_SU_ML                            0.105 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.75 
_refine_hist.d_res_low                        72.24 
_refine_hist.number_atoms_solvent             558 
_refine_hist.number_atoms_total               8824 
_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        8138 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         128 
_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  8475  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  7684  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.577  1.649  11529 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.389  1.577  17798 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.218  5.000  1039  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 34.554 21.850 454   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.686 15.000 1320  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.719 15.000 62    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.085  0.200  1066  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  9579  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1793  ? 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' ? 2.369  2.967  4183  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.365  2.967  4182  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.187  4.442  5213  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.188  4.443  5214  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.374  3.305  4292  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.374  3.305  4293  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.065  4.828  6317  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.014  57.592 37878 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.002  57.554 37515 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.75 
_refine_ls_shell.d_res_low                        1.80 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             387 
_refine_ls_shell.number_reflns_R_work             8228 
_refine_ls_shell.percent_reflns_obs               98.81 
_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                  0.3500 
_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                  0.3770 
# 
_struct.entry_id                     9GP0 
_struct.title                        '4-allyl syringol oxidase from Streptomyces cavernae: complex with Vanillyl alcohol' 
_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        9GP0 
_struct_keywords.text            'FAD, flavi, biocatalysis, 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 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9GP0 
_struct_ref.pdbx_db_accession          9GP0 
_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 9GP0 A 1 ? 554 ? 9GP0 1 ? 554 ? 1 554 
2 1 9GP0 B 1 ? 554 ? 9GP0 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)' 9660  ? 
1 MORE         -75   ? 
1 'SSA (A^2)'  32700 ? 
# 
_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  ? ALA A 38  ? ASP A 33  ALA A 38  1 ? 6  
HELX_P HELX_P3  AA3 ARG A 39  ? HIS A 41  ? ARG A 39  HIS A 41  5 ? 3  
HELX_P HELX_P4  AA4 ASP A 62  ? GLY A 77  ? ASP A 62  GLY A 77  1 ? 16 
HELX_P HELX_P5  AA5 THR A 130 ? ALA A 142 ? THR A 130 ALA A 142 1 ? 13 
HELX_P HELX_P6  AA6 SER A 156 ? ASP A 163 ? SER A 156 ASP A 163 1 ? 8  
HELX_P HELX_P7  AA7 ASP A 173 ? TRP A 177 ? ASP A 173 TRP A 177 1 ? 5  
HELX_P HELX_P8  AA8 GLY A 194 ? LEU A 198 ? GLY A 194 LEU A 198 5 ? 5  
HELX_P HELX_P9  AA9 PRO A 215 ? THR A 220 ? PRO A 215 THR A 220 5 ? 6  
HELX_P HELX_P10 AB1 ASN A 250 ? SER A 252 ? ASN A 250 SER A 252 5 ? 3  
HELX_P HELX_P11 AB2 ASP A 253 ? ILE A 266 ? ASP A 253 ILE A 266 1 ? 14 
HELX_P HELX_P12 AB3 ILE A 280 ? SER A 288 ? ILE A 280 SER A 288 1 ? 9  
HELX_P HELX_P13 AB4 GLN A 289 ? TRP A 293 ? GLN A 289 TRP A 293 5 ? 5  
HELX_P HELX_P14 AB5 PRO A 301 ? GLY A 313 ? PRO A 301 GLY A 313 1 ? 13 
HELX_P HELX_P15 AB6 PRO A 326 ? GLY A 342 ? PRO A 326 GLY A 342 1 ? 17 
HELX_P HELX_P16 AB7 ASP A 357 ? GLY A 359 ? ASP A 357 GLY A 359 5 ? 3  
HELX_P HELX_P17 AB8 ALA A 360 ? ASN A 370 ? ALA A 360 ASN A 370 1 ? 11 
HELX_P HELX_P18 AB9 LEU A 376 ? TRP A 384 ? LEU A 376 TRP A 384 5 ? 9  
HELX_P HELX_P19 AC1 VAL A 400 ? TYR A 418 ? VAL A 400 TYR A 418 1 ? 19 
HELX_P HELX_P20 AC2 ASP A 445 ? GLU A 466 ? ASP A 445 GLU A 466 1 ? 22 
HELX_P HELX_P21 AC3 HIS A 474 ? ALA A 476 ? HIS A 474 ALA A 476 5 ? 3  
HELX_P HELX_P22 AC4 LEU A 477 ? TYR A 485 ? LEU A 477 TYR A 485 1 ? 9  
HELX_P HELX_P23 AC5 ASN A 486 ? ASP A 504 ? ASN A 486 ASP A 504 1 ? 19 
HELX_P HELX_P24 AC6 GLY A 512 ? VAL A 516 ? GLY A 512 VAL A 516 5 ? 5  
HELX_P HELX_P25 AC7 PRO A 518 ? ARG A 522 ? PRO A 518 ARG A 522 5 ? 5  
HELX_P HELX_P26 AC8 SER B 10  ? GLY B 26  ? SER B 10  GLY B 26  1 ? 17 
HELX_P HELX_P27 AC9 ASP B 33  ? ALA B 38  ? ASP B 33  ALA B 38  1 ? 6  
HELX_P HELX_P28 AD1 ARG B 39  ? HIS B 41  ? ARG B 39  HIS B 41  5 ? 3  
HELX_P HELX_P29 AD2 ASP B 62  ? GLY B 77  ? ASP B 62  GLY B 77  1 ? 16 
HELX_P HELX_P30 AD3 THR B 130 ? ALA B 142 ? THR B 130 ALA B 142 1 ? 13 
HELX_P HELX_P31 AD4 SER B 156 ? ASP B 163 ? SER B 156 ASP B 163 1 ? 8  
HELX_P HELX_P32 AD5 ASP B 173 ? TRP B 177 ? ASP B 173 TRP B 177 1 ? 5  
HELX_P HELX_P33 AD6 GLY B 194 ? LEU B 198 ? GLY B 194 LEU B 198 5 ? 5  
HELX_P HELX_P34 AD7 PRO B 215 ? THR B 220 ? PRO B 215 THR B 220 5 ? 6  
HELX_P HELX_P35 AD8 ASN B 250 ? SER B 252 ? ASN B 250 SER B 252 5 ? 3  
HELX_P HELX_P36 AD9 ASP B 253 ? ILE B 266 ? ASP B 253 ILE B 266 1 ? 14 
HELX_P HELX_P37 AE1 ILE B 280 ? ALA B 285 ? ILE B 280 ALA B 285 1 ? 6  
HELX_P HELX_P38 AE2 GLN B 289 ? TRP B 293 ? GLN B 289 TRP B 293 5 ? 5  
HELX_P HELX_P39 AE3 PRO B 301 ? GLY B 313 ? PRO B 301 GLY B 313 1 ? 13 
HELX_P HELX_P40 AE4 PRO B 326 ? GLY B 342 ? PRO B 326 GLY B 342 1 ? 17 
HELX_P HELX_P41 AE5 ASP B 357 ? GLY B 359 ? ASP B 357 GLY B 359 5 ? 3  
HELX_P HELX_P42 AE6 ALA B 360 ? ASN B 370 ? ALA B 360 ASN B 370 1 ? 11 
HELX_P HELX_P43 AE7 LEU B 376 ? TRP B 384 ? LEU B 376 TRP B 384 5 ? 9  
HELX_P HELX_P44 AE8 VAL B 400 ? TYR B 418 ? VAL B 400 TYR B 418 1 ? 19 
HELX_P HELX_P45 AE9 ASP B 445 ? GLU B 466 ? ASP B 445 GLU B 466 1 ? 22 
HELX_P HELX_P46 AF1 HIS B 474 ? ALA B 476 ? HIS B 474 ALA B 476 5 ? 3  
HELX_P HELX_P47 AF2 LEU B 477 ? TYR B 485 ? LEU B 477 TYR B 485 1 ? 9  
HELX_P HELX_P48 AF3 ASN B 486 ? ASP B 504 ? ASN B 486 ASP B 504 1 ? 19 
HELX_P HELX_P49 AF4 GLY B 512 ? VAL B 516 ? GLY B 512 VAL B 516 5 ? 5  
HELX_P HELX_P50 AF5 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 -1.53 
2 ALA 269 B . ? ALA 269 B PRO 270 B ? PRO 270 B 1 -0.86 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 8 ? 
AA6 ? 4 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
AA9 ? 7 ? 
AB1 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? 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 
AA5 7 8 ? 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 
# 
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 54  ? ILE A 58  ? ALA A 54  ILE A 58  
AA1 3 ALA A 101 ? ASN A 105 ? ALA A 101 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 423 ? VAL A 428 ? ALA A 423 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 423 ? VAL A 428 ? ALA A 423 VAL A 428 
AA5 6 MET A 433 ? ASP A 442 ? MET A 433 ASP A 442 
AA5 7 PRO A 395 ? SER A 397 ? PRO A 395 SER A 397 
AA5 8 GLY A 469 ? GLU A 470 ? GLY A 469 GLU A 470 
AA6 1 VAL B 30  ? ARG B 31  ? VAL B 30  ARG B 31  
AA6 2 ALA B 54  ? ILE B 58  ? ALA B 54  ILE B 58  
AA6 3 ALA B 101 ? ASN B 105 ? ALA B 101 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 424 ? VAL B 428 ? ALA B 424 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 424 ? VAL B 428 ? ALA B 424 VAL B 428 
AB1 6 MET B 433 ? ASP B 442 ? MET B 433 ASP B 442 
AB1 7 ILE B 396 ? SER B 397 ? ILE B 396 SER B 397 
# 
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 ASN A 105 ? O ASN A 105 
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 ASN A 279 ? N ASN A 279 O ALA A 424 ? O ALA A 424 
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 ASN A 279 ? N ASN A 279 O ALA A 424 ? O ALA A 424 
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 
AA5 7 8 N ILE A 396 ? N ILE A 396 O GLY A 469 ? O GLY A 469 
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 LEU B 277 ? N LEU B 277 O PHE B 426 ? O PHE B 426 
AA9 5 6 N VAL B 427 ? N VAL B 427 O HIS B 434 ? O HIS B 434 
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 LEU B 277 ? N LEU B 277 O PHE B 426 ? O PHE B 426 
AB1 5 6 N VAL B 427 ? N VAL B 427 O HIS B 434 ? O HIS B 434 
AB1 6 7 O MET B 433 ? O MET B 433 N SER B 397 ? N SER B 397 
# 
_pdbx_entry_details.entry_id                   9GP0 
_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 O   A HOH 718 ? ? O   A HOH 977 ? ? 1.08 
2  1 O   B HOH 762 ? ? O   B HOH 873 ? ? 1.20 
3  1 NE2 A HIS 390 ? ? C8M A FAD 601 ? ? 1.70 
4  1 O   B HOH 789 ? ? O   B HOH 911 ? ? 1.79 
5  1 O   B HOH 904 ? ? O   B HOH 925 ? ? 1.93 
6  1 O   A HOH 927 ? ? O   A HOH 943 ? ? 1.95 
7  1 O   A HOH 926 ? ? O   A HOH 987 ? ? 2.01 
8  1 O   B HOH 748 ? ? O   B HOH 918 ? ? 2.01 
9  1 O   A HOH 705 ? ? O   A HOH 710 ? ? 2.02 
10 1 O   A HOH 718 ? ? O   A HOH 887 ? ? 2.15 
11 1 CB  A LEU 206 ? ? O   A HOH 986 ? ? 2.16 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              181 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              181 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              181 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                89.46 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            -10.74 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 84  ? ? -91.71  -78.94  
2  1 PRO A 150 ? ? -69.42  -173.29 
3  1 TYR A 171 ? ? -96.64  32.34   
4  1 TYR A 294 ? ? -173.65 132.38  
5  1 HIS A 356 ? ? -141.92 20.26   
6  1 SER A 394 ? ? -154.10 61.71   
7  1 LEU A 430 ? ? -146.50 -64.67  
8  1 TYR A 485 ? ? -90.66  51.59   
9  1 ALA A 510 ? ? 24.92   62.29   
10 1 HIS B 52  ? ? 61.91   63.72   
11 1 SER B 84  ? ? -93.89  -79.67  
12 1 TYR B 171 ? ? -95.91  32.41   
13 1 TYR B 294 ? ? -172.37 133.12  
14 1 HIS B 356 ? ? -145.69 23.45   
15 1 SER B 394 ? ? -147.70 58.66   
16 1 LEU B 430 ? ? -148.46 -62.30  
17 1 TYR B 485 ? ? -91.15  53.22   
18 1 ALA B 510 ? ? 23.84   62.63   
# 
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 ALA 527 ? B ALA 527 
34 1 Y 1 B ALA 528 ? B ALA 528 
35 1 Y 1 B ALA 529 ? B ALA 529 
36 1 Y 1 B LEU 530 ? B LEU 530 
37 1 Y 1 B LYS 531 ? B LYS 531 
38 1 Y 1 B LEU 532 ? B LEU 532 
39 1 Y 1 B ARG 533 ? B ARG 533 
40 1 Y 1 B VAL 534 ? B VAL 534 
41 1 Y 1 B ASP 535 ? B ASP 535 
42 1 Y 1 B PRO 536 ? B PRO 536 
43 1 Y 1 B ALA 537 ? B ALA 537 
44 1 Y 1 B ALA 538 ? B ALA 538 
45 1 Y 1 B ASN 539 ? B ASN 539 
46 1 Y 1 B LYS 540 ? B LYS 540 
47 1 Y 1 B ALA 541 ? B ALA 541 
48 1 Y 1 B ARG 542 ? B ARG 542 
49 1 Y 1 B LYS 543 ? B LYS 543 
50 1 Y 1 B GLU 544 ? B GLU 544 
51 1 Y 1 B ALA 545 ? B ALA 545 
52 1 Y 1 B GLU 546 ? B GLU 546 
53 1 Y 1 B LEU 547 ? B LEU 547 
54 1 Y 1 B ALA 548 ? B ALA 548 
55 1 Y 1 B ALA 549 ? B ALA 549 
56 1 Y 1 B ALA 550 ? B ALA 550 
57 1 Y 1 B THR 551 ? B THR 551 
58 1 Y 1 B ALA 552 ? B ALA 552 
59 1 Y 1 B GLU 553 ? B GLU 553 
60 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 
SER N      N N N 376 
SER CA     C N S 377 
SER C      C N N 378 
SER O      O N N 379 
SER CB     C N N 380 
SER OG     O N N 381 
SER OXT    O N N 382 
SER H      H N N 383 
SER H2     H N N 384 
SER HA     H N N 385 
SER HB2    H N N 386 
SER HB3    H N N 387 
SER HG     H N N 388 
SER HXT    H N N 389 
THR N      N N N 390 
THR CA     C N S 391 
THR C      C N N 392 
THR O      O N N 393 
THR CB     C N R 394 
THR OG1    O N N 395 
THR CG2    C N N 396 
THR OXT    O N N 397 
THR H      H N N 398 
THR H2     H N N 399 
THR HA     H N N 400 
THR HB     H N N 401 
THR HG1    H N N 402 
THR HG21   H N N 403 
THR HG22   H N N 404 
THR HG23   H N N 405 
THR HXT    H N N 406 
TRP N      N N N 407 
TRP CA     C N S 408 
TRP C      C N N 409 
TRP O      O N N 410 
TRP CB     C N N 411 
TRP CG     C Y N 412 
TRP CD1    C Y N 413 
TRP CD2    C Y N 414 
TRP NE1    N Y N 415 
TRP CE2    C Y N 416 
TRP CE3    C Y N 417 
TRP CZ2    C Y N 418 
TRP CZ3    C Y N 419 
TRP CH2    C Y N 420 
TRP OXT    O N N 421 
TRP H      H N N 422 
TRP H2     H N N 423 
TRP HA     H N N 424 
TRP HB2    H N N 425 
TRP HB3    H N N 426 
TRP HD1    H N N 427 
TRP HE1    H N N 428 
TRP HE3    H N N 429 
TRP HZ2    H N N 430 
TRP HZ3    H N N 431 
TRP HH2    H N N 432 
TRP HXT    H N N 433 
TYR N      N N N 434 
TYR CA     C N S 435 
TYR C      C N N 436 
TYR O      O N N 437 
TYR CB     C N N 438 
TYR CG     C Y N 439 
TYR CD1    C Y N 440 
TYR CD2    C Y N 441 
TYR CE1    C Y N 442 
TYR CE2    C Y N 443 
TYR CZ     C Y N 444 
TYR OH     O N N 445 
TYR OXT    O N N 446 
TYR H      H N N 447 
TYR H2     H N N 448 
TYR HA     H N N 449 
TYR HB2    H N N 450 
TYR HB3    H N N 451 
TYR HD1    H N N 452 
TYR HD2    H N N 453 
TYR HE1    H N N 454 
TYR HE2    H N N 455 
TYR HH     H N N 456 
TYR HXT    H N N 457 
V55 CAI    C Y N 458 
V55 CAG    C Y N 459 
V55 CAK    C Y N 460 
V55 CAJ    C Y N 461 
V55 CAF    C Y N 462 
V55 OAB    O N N 463 
V55 CAE    C Y N 464 
V55 CAD    C N N 465 
V55 CAA    C N N 466 
V55 OAH    O N N 467 
V55 OAC    O N N 468 
V55 HAG    H N N 469 
V55 HAD    H N N 470 
V55 HAE    H N N 471 
V55 HAF    H N N 472 
V55 HAC    H N N 473 
V55 HAA1   H N N 474 
V55 HAA2   H N N 475 
V55 HAA3   H N N 476 
VAL N      N N N 477 
VAL CA     C N S 478 
VAL C      C N N 479 
VAL O      O N N 480 
VAL CB     C N N 481 
VAL CG1    C N N 482 
VAL CG2    C N N 483 
VAL OXT    O N N 484 
VAL H      H N N 485 
VAL H2     H N N 486 
VAL HA     H N N 487 
VAL HB     H N N 488 
VAL HG11   H N N 489 
VAL HG12   H N N 490 
VAL HG13   H N N 491 
VAL HG21   H N N 492 
VAL HG22   H N N 493 
VAL HG23   H N N 494 
VAL HXT    H N N 495 
# 
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 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TYR N     CA     sing N N 425 
TYR N     H      sing N N 426 
TYR N     H2     sing N N 427 
TYR CA    C      sing N N 428 
TYR CA    CB     sing N N 429 
TYR CA    HA     sing N N 430 
TYR C     O      doub N N 431 
TYR C     OXT    sing N N 432 
TYR CB    CG     sing N N 433 
TYR CB    HB2    sing N N 434 
TYR CB    HB3    sing N N 435 
TYR CG    CD1    doub Y N 436 
TYR CG    CD2    sing Y N 437 
TYR CD1   CE1    sing Y N 438 
TYR CD1   HD1    sing N N 439 
TYR CD2   CE2    doub Y N 440 
TYR CD2   HD2    sing N N 441 
TYR CE1   CZ     doub Y N 442 
TYR CE1   HE1    sing N N 443 
TYR CE2   CZ     sing Y N 444 
TYR CE2   HE2    sing N N 445 
TYR CZ    OH     sing N N 446 
TYR OH    HH     sing N N 447 
TYR OXT   HXT    sing N N 448 
V55 CAK   CAG    doub Y N 449 
V55 CAK   CAJ    sing Y N 450 
V55 CAK   OAH    sing N N 451 
V55 CAG   CAI    sing Y N 452 
V55 CAI   CAD    sing N N 453 
V55 CAI   CAE    doub Y N 454 
V55 CAD   OAB    doub N N 455 
V55 CAF   CAJ    doub Y N 456 
V55 CAF   CAE    sing Y N 457 
V55 CAJ   OAC    sing N N 458 
V55 CAA   OAH    sing N N 459 
V55 CAG   HAG    sing N N 460 
V55 CAD   HAD    sing N N 461 
V55 CAE   HAE    sing N N 462 
V55 CAF   HAF    sing N N 463 
V55 OAC   HAC    sing N N 464 
V55 CAA   HAA1   sing N N 465 
V55 CAA   HAA2   sing N N 466 
V55 CAA   HAA3   sing N N 467 
VAL N     CA     sing N N 468 
VAL N     H      sing N N 469 
VAL N     H2     sing N N 470 
VAL CA    C      sing N N 471 
VAL CA    CB     sing N N 472 
VAL CA    HA     sing N N 473 
VAL C     O      doub N N 474 
VAL C     OXT    sing N N 475 
VAL CB    CG1    sing N N 476 
VAL CB    CG2    sing N N 477 
VAL CB    HB     sing N N 478 
VAL CG1   HG11   sing N N 479 
VAL CG1   HG12   sing N N 480 
VAL CG1   HG13   sing N N 481 
VAL CG2   HG21   sing N N 482 
VAL CG2   HG22   sing N N 483 
VAL CG2   HG23   sing N N 484 
VAL OXT   HXT    sing N N 485 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9GOV 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GP0 
_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]   0.011988 
_atom_sites.fract_transf_matrix[1][2]   0.006921 
_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]   0.013842 
_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]   0.003346 
_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   ? 6.245   6.638   33.334  1.00 48.02 ? 3    ARG A N     1 
ATOM   2    C CA    . ARG A 1 3   ? 5.475   5.355   33.539  1.00 47.61 ? 3    ARG A CA    1 
ATOM   3    C C     . ARG A 1 3   ? 4.920   4.848   32.196  1.00 40.01 ? 3    ARG A C     1 
ATOM   4    O O     . ARG A 1 3   ? 4.117   5.558   31.576  1.00 35.77 ? 3    ARG A O     1 
ATOM   5    C CB    . ARG A 1 3   ? 4.308   5.604   34.488  1.00 51.62 ? 3    ARG A CB    1 
ATOM   6    C CG    . ARG A 1 3   ? 3.412   4.391   34.681  1.00 47.66 ? 3    ARG A CG    1 
ATOM   7    C CD    . ARG A 1 3   ? 1.939   4.750   34.714  1.00 45.99 ? 3    ARG A CD    1 
ATOM   8    N NE    . ARG A 1 3   ? 1.242   3.825   35.577  1.00 43.19 ? 3    ARG A NE    1 
ATOM   9    C CZ    . ARG A 1 3   ? -0.066  3.791   35.808  1.00 42.95 ? 3    ARG A CZ    1 
ATOM   10   N NH1   . ARG A 1 3   ? -0.895  4.631   35.222  1.00 47.66 ? 3    ARG A NH1   1 
ATOM   11   N NH2   . ARG A 1 3   ? -0.531  2.885   36.637  1.00 41.85 ? 3    ARG A NH2   1 
ATOM   12   N N     . THR A 1 4   ? 5.322   3.660   31.754  1.00 40.67 ? 4    THR A N     1 
ATOM   13   C CA    . THR A 1 4   ? 4.936   3.109   30.422  1.00 38.65 ? 4    THR A CA    1 
ATOM   14   C C     . THR A 1 4   ? 3.411   2.883   30.380  1.00 36.66 ? 4    THR A C     1 
ATOM   15   O O     . THR A 1 4   ? 2.908   2.182   31.265  1.00 32.45 ? 4    THR A O     1 
ATOM   16   C CB    . THR A 1 4   ? 5.729   1.828   30.141  1.00 38.83 ? 4    THR A CB    1 
ATOM   17   O OG1   . THR A 1 4   ? 7.127   2.099   30.286  1.00 37.33 ? 4    THR A OG1   1 
ATOM   18   C CG2   . THR A 1 4   ? 5.440   1.272   28.768  1.00 40.31 ? 4    THR A CG2   1 
ATOM   19   N N     . LEU A 1 5   ? 2.698   3.523   29.442  1.00 35.01 ? 5    LEU A N     1 
ATOM   20   C CA    . LEU A 1 5   ? 1.244   3.310   29.208  1.00 34.67 ? 5    LEU A CA    1 
ATOM   21   C C     . LEU A 1 5   ? 1.101   2.566   27.897  1.00 35.43 ? 5    LEU A C     1 
ATOM   22   O O     . LEU A 1 5   ? 1.880   2.813   26.973  1.00 31.14 ? 5    LEU A O     1 
ATOM   23   C CB    . LEU A 1 5   ? 0.464   4.627   29.148  1.00 38.40 ? 5    LEU A CB    1 
ATOM   24   C CG    . LEU A 1 5   ? 0.394   5.417   30.456  1.00 41.74 ? 5    LEU A CG    1 
ATOM   25   C CD1   . LEU A 1 5   ? -0.436  6.677   30.299  1.00 43.25 ? 5    LEU A CD1   1 
ATOM   26   C CD2   . LEU A 1 5   ? -0.173  4.544   31.561  1.00 46.25 ? 5    LEU A CD2   1 
ATOM   27   N N     . PRO A 1 6   ? 0.136   1.628   27.787  1.00 36.05 ? 6    PRO A N     1 
ATOM   28   C CA    . PRO A 1 6   ? -0.165  1.018   26.497  1.00 32.34 ? 6    PRO A CA    1 
ATOM   29   C C     . PRO A 1 6   ? -0.601  2.097   25.511  1.00 34.71 ? 6    PRO A C     1 
ATOM   30   O O     . PRO A 1 6   ? -1.287  3.053   25.882  1.00 27.34 ? 6    PRO A O     1 
ATOM   31   C CB    . PRO A 1 6   ? -1.299  0.027   26.783  1.00 32.66 ? 6    PRO A CB    1 
ATOM   32   C CG    . PRO A 1 6   ? -1.191  -0.249  28.274  1.00 34.15 ? 6    PRO A CG    1 
ATOM   33   C CD    . PRO A 1 6   ? -0.635  1.026   28.885  1.00 34.89 ? 6    PRO A CD    1 
ATOM   34   N N     . PRO A 1 7   ? -0.234  1.965   24.218  1.00 33.65 ? 7    PRO A N     1 
ATOM   35   C CA    . PRO A 1 7   ? -0.762  2.855   23.190  1.00 34.63 ? 7    PRO A CA    1 
ATOM   36   C C     . PRO A 1 7   ? -2.296  2.801   23.109  1.00 34.60 ? 7    PRO A C     1 
ATOM   37   O O     . PRO A 1 7   ? -2.858  1.714   23.105  1.00 33.28 ? 7    PRO A O     1 
ATOM   38   C CB    . PRO A 1 7   ? -0.153  2.295   21.891  1.00 36.99 ? 7    PRO A CB    1 
ATOM   39   C CG    . PRO A 1 7   ? 1.054   1.523   22.341  1.00 38.29 ? 7    PRO A CG    1 
ATOM   40   C CD    . PRO A 1 7   ? 0.703   0.959   23.697  1.00 35.01 ? 7    PRO A CD    1 
ATOM   41   N N     . GLY A 1 8   ? -2.933  3.966   23.066  1.00 38.53 ? 8    GLY A N     1 
ATOM   42   C CA    . GLY A 1 8   ? -4.393  4.111   22.933  1.00 41.30 ? 8    GLY A CA    1 
ATOM   43   C C     . GLY A 1 8   ? -5.124  3.881   24.253  1.00 42.96 ? 8    GLY A C     1 
ATOM   44   O O     . GLY A 1 8   ? -6.361  3.718   24.208  1.00 41.82 ? 8    GLY A O     1 
ATOM   45   N N     . VAL A 1 9   ? -4.419  3.816   25.390  1.00 36.83 ? 9    VAL A N     1 
ATOM   46   C CA    . VAL A 1 9   ? -5.100  3.650   26.710  1.00 34.60 ? 9    VAL A CA    1 
ATOM   47   C C     . VAL A 1 9   ? -4.691  4.817   27.615  1.00 31.29 ? 9    VAL A C     1 
ATOM   48   O O     . VAL A 1 9   ? -3.479  5.060   27.774  1.00 30.34 ? 9    VAL A O     1 
ATOM   49   C CB    . VAL A 1 9   ? -4.872  2.264   27.355  1.00 34.64 ? 9    VAL A CB    1 
ATOM   50   C CG1   . VAL A 1 9   ? -4.847  1.133   26.324  1.00 32.10 ? 9    VAL A CG1   1 
ATOM   51   C CG2   . VAL A 1 9   ? -3.649  2.215   28.214  1.00 40.85 ? 9    VAL A CG2   1 
ATOM   52   N N     . SER A 1 10  ? -5.691  5.521   28.153  1.00 33.61 ? 10   SER A N     1 
ATOM   53   C CA    . SER A 1 10  ? -5.529  6.639   29.121  1.00 31.20 ? 10   SER A CA    1 
ATOM   54   C C     . SER A 1 10  ? -4.903  6.120   30.414  1.00 31.68 ? 10   SER A C     1 
ATOM   55   O O     . SER A 1 10  ? -5.084  4.925   30.725  1.00 32.43 ? 10   SER A O     1 
ATOM   56   C CB    . SER A 1 10  ? -6.854  7.306   29.408  1.00 29.87 ? 10   SER A CB    1 
ATOM   57   O OG    . SER A 1 10  ? -7.752  6.404   30.020  1.00 29.39 ? 10   SER A OG    1 
ATOM   58   N N     . ASP A 1 11  ? -4.198  6.982   31.143  1.00 30.83 ? 11   ASP A N     1 
ATOM   59   C CA    . ASP A 1 11  ? -3.670  6.679   32.497  1.00 35.60 ? 11   ASP A CA    1 
ATOM   60   C C     . ASP A 1 11  ? -4.795  6.082   33.367  1.00 34.73 ? 11   ASP A C     1 
ATOM   61   O O     . ASP A 1 11  ? -4.522  5.125   34.112  1.00 32.68 ? 11   ASP A O     1 
ATOM   62   C CB    . ASP A 1 11  ? -3.074  7.938   33.128  1.00 38.81 ? 11   ASP A CB    1 
ATOM   63   C CG    . ASP A 1 11  ? -2.519  7.684   34.513  1.00 42.40 ? 11   ASP A CG    1 
ATOM   64   O OD1   . ASP A 1 11  ? -1.411  7.143   34.604  1.00 41.75 ? 11   ASP A OD1   1 
ATOM   65   O OD2   . ASP A 1 11  ? -3.228  8.005   35.479  1.00 46.41 ? 11   ASP A OD2   1 
ATOM   66   N N     . GLU A 1 12  ? -6.004  6.633   33.267  1.00 37.69 ? 12   GLU A N     1 
ATOM   67   C CA    . GLU A 1 12  ? -7.187  6.263   34.108  1.00 43.12 ? 12   GLU A CA    1 
ATOM   68   C C     . GLU A 1 12  ? -7.640  4.837   33.756  1.00 37.83 ? 12   GLU A C     1 
ATOM   69   O O     . GLU A 1 12  ? -7.888  4.037   34.667  1.00 33.77 ? 12   GLU A O     1 
ATOM   70   C CB    . GLU A 1 12  ? -8.306  7.293   33.893  1.00 49.60 ? 12   GLU A CB    1 
ATOM   71   C CG    . GLU A 1 12  ? -9.431  7.228   34.910  1.00 61.79 ? 12   GLU A CG    1 
ATOM   72   C CD    . GLU A 1 12  ? -10.584 6.281   34.593  1.00 72.73 ? 12   GLU A CD    1 
ATOM   73   O OE1   . GLU A 1 12  ? -10.326 5.099   34.219  1.00 81.01 ? 12   GLU A OE1   1 
ATOM   74   O OE2   . GLU A 1 12  ? -11.756 6.740   34.707  1.00 74.36 ? 12   GLU A OE2   1 
ATOM   75   N N     . ASP A 1 13  ? -7.789  4.543   32.461  1.00 33.89 ? 13   ASP A N     1 
ATOM   76   C CA    . ASP A 1 13  ? -8.190  3.201   31.985  1.00 32.73 ? 13   ASP A CA    1 
ATOM   77   C C     . ASP A 1 13  ? -7.107  2.173   32.351  1.00 30.18 ? 13   ASP A C     1 
ATOM   78   O O     . ASP A 1 13  ? -7.478  1.033   32.682  1.00 27.18 ? 13   ASP A O     1 
ATOM   79   C CB    . ASP A 1 13  ? -8.553  3.231   30.503  1.00 36.33 ? 13   ASP A CB    1 
ATOM   80   C CG    . ASP A 1 13  ? -9.933  3.822   30.260  1.00 35.43 ? 13   ASP A CG    1 
ATOM   81   O OD1   . ASP A 1 13  ? -10.713 3.871   31.212  1.00 37.42 ? 13   ASP A OD1   1 
ATOM   82   O OD2   . ASP A 1 13  ? -10.212 4.232   29.135  1.00 34.77 ? 13   ASP A OD2   1 
ATOM   83   N N     . PHE A 1 14  ? -5.830  2.543   32.323  1.00 27.79 ? 14   PHE A N     1 
ATOM   84   C CA    . PHE A 1 14  ? -4.736  1.620   32.693  1.00 28.33 ? 14   PHE A CA    1 
ATOM   85   C C     . PHE A 1 14  ? -4.799  1.335   34.195  1.00 31.54 ? 14   PHE A C     1 
ATOM   86   O O     . PHE A 1 14  ? -4.559  0.183   34.604  1.00 26.62 ? 14   PHE A O     1 
ATOM   87   C CB    . PHE A 1 14  ? -3.378  2.179   32.304  1.00 26.48 ? 14   PHE A CB    1 
ATOM   88   C CG    . PHE A 1 14  ? -2.250  1.189   32.422  1.00 26.73 ? 14   PHE A CG    1 
ATOM   89   C CD1   . PHE A 1 14  ? -2.323  -0.059  31.815  1.00 28.89 ? 14   PHE A CD1   1 
ATOM   90   C CD2   . PHE A 1 14  ? -1.088  1.521   33.090  1.00 30.60 ? 14   PHE A CD2   1 
ATOM   91   C CE1   . PHE A 1 14  ? -1.264  -0.941  31.890  1.00 24.93 ? 14   PHE A CE1   1 
ATOM   92   C CE2   . PHE A 1 14  ? -0.025  0.631   33.173  1.00 28.79 ? 14   PHE A CE2   1 
ATOM   93   C CZ    . PHE A 1 14  ? -0.139  -0.610  32.594  1.00 28.26 ? 14   PHE A CZ    1 
ATOM   94   N N     . THR A 1 15  ? -5.094  2.352   35.005  1.00 30.67 ? 15   THR A N     1 
ATOM   95   C CA    . THR A 1 15  ? -5.213  2.203   36.479  1.00 27.48 ? 15   THR A CA    1 
ATOM   96   C C     . THR A 1 15  ? -6.345  1.225   36.773  1.00 25.86 ? 15   THR A C     1 
ATOM   97   O O     . THR A 1 15  ? -6.140  0.315   37.602  1.00 26.63 ? 15   THR A O     1 
ATOM   98   C CB    . THR A 1 15  ? -5.404  3.561   37.170  1.00 31.41 ? 15   THR A CB    1 
ATOM   99   O OG1   . THR A 1 15  ? -4.209  4.308   36.933  1.00 31.63 ? 15   THR A OG1   1 
ATOM   100  C CG2   . THR A 1 15  ? -5.646  3.448   38.663  1.00 29.09 ? 15   THR A CG2   1 
ATOM   101  N N     . SER A 1 16  ? -7.484  1.411   36.122  1.00 24.95 ? 16   SER A N     1 
ATOM   102  C CA    . SER A 1 16  ? -8.710  0.596   36.286  1.00 24.10 ? 16   SER A CA    1 
ATOM   103  C C     . SER A 1 16  ? -8.405  -0.857  35.890  1.00 25.89 ? 16   SER A C     1 
ATOM   104  O O     . SER A 1 16  ? -8.774  -1.780  36.620  1.00 23.32 ? 16   SER A O     1 
ATOM   105  C CB    . SER A 1 16  ? -9.859  1.179   35.513  1.00 27.15 ? 16   SER A CB    1 
ATOM   106  O OG    . SER A 1 16  ? -10.200 2.470   36.009  1.00 28.99 ? 16   SER A OG    1 
ATOM   107  N N     . ALA A 1 17  ? -7.728  -1.054  34.759  1.00 23.29 ? 17   ALA A N     1 
ATOM   108  C CA    . ALA A 1 17  ? -7.396  -2.386  34.225  1.00 23.30 ? 17   ALA A CA    1 
ATOM   109  C C     . ALA A 1 17  ? -6.466  -3.110  35.184  1.00 21.69 ? 17   ALA A C     1 
ATOM   110  O O     . ALA A 1 17  ? -6.735  -4.266  35.457  1.00 20.86 ? 17   ALA A O     1 
ATOM   111  C CB    . ALA A 1 17  ? -6.774  -2.264  32.854  1.00 24.42 ? 17   ALA A CB    1 
ATOM   112  N N     . LEU A 1 18  ? -5.429  -2.438  35.703  1.00 23.88 ? 18   LEU A N     1 
ATOM   113  C CA    . LEU A 1 18  ? -4.470  -3.083  36.620  1.00 23.63 ? 18   LEU A CA    1 
ATOM   114  C C     . LEU A 1 18  ? -5.229  -3.551  37.861  1.00 22.95 ? 18   LEU A C     1 
ATOM   115  O O     . LEU A 1 18  ? -4.928  -4.661  38.339  1.00 23.30 ? 18   LEU A O     1 
ATOM   116  C CB    . LEU A 1 18  ? -3.349  -2.120  36.979  1.00 26.18 ? 18   LEU A CB    1 
ATOM   117  C CG    . LEU A 1 18  ? -2.386  -1.778  35.838  1.00 26.77 ? 18   LEU A CG    1 
ATOM   118  C CD1   . LEU A 1 18  ? -1.450  -0.659  36.261  1.00 26.80 ? 18   LEU A CD1   1 
ATOM   119  C CD2   . LEU A 1 18  ? -1.616  -3.011  35.391  1.00 26.18 ? 18   LEU A CD2   1 
ATOM   120  N N     . THR A 1 19  ? -6.162  -2.738  38.352  1.00 25.35 ? 19   THR A N     1 
ATOM   121  C CA    . THR A 1 19  ? -6.974  -3.098  39.540  1.00 22.83 ? 19   THR A CA    1 
ATOM   122  C C     . THR A 1 19  ? -7.769  -4.363  39.198  1.00 21.98 ? 19   THR A C     1 
ATOM   123  O O     . THR A 1 19  ? -7.738  -5.326  39.994  1.00 22.52 ? 19   THR A O     1 
ATOM   124  C CB    . THR A 1 19  ? -7.843  -1.933  40.023  1.00 25.76 ? 19   THR A CB    1 
ATOM   125  O OG1   . THR A 1 19  ? -6.921  -0.942  40.475  1.00 23.18 ? 19   THR A OG1   1 
ATOM   126  C CG2   . THR A 1 19  ? -8.788  -2.371  41.130  1.00 26.60 ? 19   THR A CG2   1 
ATOM   127  N N     . ALA A 1 20  ? -8.462  -4.377  38.050  1.00 21.54 ? 20   ALA A N     1 
ATOM   128  C CA    . ALA A 1 20  ? -9.288  -5.516  37.615  1.00 24.00 ? 20   ALA A CA    1 
ATOM   129  C C     . ALA A 1 20  ? -8.408  -6.758  37.466  1.00 20.56 ? 20   ALA A C     1 
ATOM   130  O O     . ALA A 1 20  ? -8.861  -7.852  37.837  1.00 21.18 ? 20   ALA A O     1 
ATOM   131  C CB    . ALA A 1 20  ? -10.019 -5.200  36.346  1.00 25.21 ? 20   ALA A CB    1 
ATOM   132  N N     . PHE A 1 21  ? -7.197  -6.615  36.916  1.00 24.08 ? 21   PHE A N     1 
ATOM   133  C CA    . PHE A 1 21  ? -6.251  -7.753  36.741  1.00 22.37 ? 21   PHE A CA    1 
ATOM   134  C C     . PHE A 1 21  ? -5.869  -8.293  38.127  1.00 21.69 ? 21   PHE A C     1 
ATOM   135  O O     . PHE A 1 21  ? -5.893  -9.515  38.338  1.00 20.33 ? 21   PHE A O     1 
ATOM   136  C CB    . PHE A 1 21  ? -5.007  -7.340  35.958  1.00 20.73 ? 21   PHE A CB    1 
ATOM   137  C CG    . PHE A 1 21  ? -5.194  -6.988  34.496  1.00 20.89 ? 21   PHE A CG    1 
ATOM   138  C CD1   . PHE A 1 21  ? -6.051  -7.713  33.678  1.00 21.52 ? 21   PHE A CD1   1 
ATOM   139  C CD2   . PHE A 1 21  ? -4.401  -6.012  33.912  1.00 21.30 ? 21   PHE A CD2   1 
ATOM   140  C CE1   . PHE A 1 21  ? -6.176  -7.419  32.329  1.00 20.83 ? 21   PHE A CE1   1 
ATOM   141  C CE2   . PHE A 1 21  ? -4.509  -5.718  32.561  1.00 20.76 ? 21   PHE A CE2   1 
ATOM   142  C CZ    . PHE A 1 21  ? -5.406  -6.416  31.777  1.00 22.15 ? 21   PHE A CZ    1 
ATOM   143  N N     . ARG A 1 22  ? -5.499  -7.401  39.051  1.00 21.56 ? 22   ARG A N     1 
ATOM   144  C CA    . ARG A 1 22  ? -5.164  -7.813  40.445  1.00 21.75 ? 22   ARG A CA    1 
ATOM   145  C C     . ARG A 1 22  ? -6.359  -8.525  41.081  1.00 21.26 ? 22   ARG A C     1 
ATOM   146  O O     . ARG A 1 22  ? -6.132  -9.504  41.784  1.00 21.02 ? 22   ARG A O     1 
ATOM   147  C CB    . ARG A 1 22  ? -4.791  -6.632  41.338  1.00 20.93 ? 22   ARG A CB    1 
ATOM   148  C CG    . ARG A 1 22  ? -3.482  -5.957  40.988  1.00 23.98 ? 22   ARG A CG    1 
ATOM   149  C CD    . ARG A 1 22  ? -3.086  -4.849  41.969  1.00 25.15 ? 22   ARG A CD    1 
ATOM   150  N NE    . ARG A 1 22  ? -2.026  -4.085  41.341  1.00 26.36 ? 22   ARG A NE    1 
ATOM   151  C CZ    . ARG A 1 22  ? -2.177  -2.925  40.732  1.00 25.42 ? 22   ARG A CZ    1 
ATOM   152  N NH1   . ARG A 1 22  ? -3.335  -2.287  40.739  1.00 26.54 ? 22   ARG A NH1   1 
ATOM   153  N NH2   . ARG A 1 22  ? -1.138  -2.395  40.136  1.00 29.04 ? 22   ARG A NH2   1 
ATOM   154  N N     . ASP A 1 23  ? -7.571  -8.059  40.821  1.00 22.78 ? 23   ASP A N     1 
ATOM   155  C CA    . ASP A 1 23  ? -8.820  -8.619  41.393  1.00 21.73 ? 23   ASP A CA    1 
ATOM   156  C C     . ASP A 1 23  ? -8.986  -10.071 40.944  1.00 23.55 ? 23   ASP A C     1 
ATOM   157  O O     . ASP A 1 23  ? -9.702  -10.796 41.607  1.00 23.08 ? 23   ASP A O     1 
ATOM   158  C CB    . ASP A 1 23  ? -10.034 -7.796  40.973  1.00 22.71 ? 23   ASP A CB    1 
ATOM   159  C CG    . ASP A 1 23  ? -10.112 -6.435  41.639  1.00 23.37 ? 23   ASP A CG    1 
ATOM   160  O OD1   . ASP A 1 23  ? -9.301  -6.172  42.579  1.00 26.21 ? 23   ASP A OD1   1 
ATOM   161  O OD2   . ASP A 1 23  ? -10.955 -5.643  41.183  1.00 24.06 ? 23   ASP A OD2   1 
ATOM   162  N N     . VAL A 1 24  ? -8.414  -10.450 39.799  1.00 22.46 ? 24   VAL A N     1 
ATOM   163  C CA    . VAL A 1 24  ? -8.502  -11.833 39.262  1.00 22.63 ? 24   VAL A CA    1 
ATOM   164  C C     . VAL A 1 24  ? -7.287  -12.641 39.732  1.00 24.41 ? 24   VAL A C     1 
ATOM   165  O O     . VAL A 1 24  ? -7.524  -13.710 40.309  1.00 24.69 ? 24   VAL A O     1 
ATOM   166  C CB    . VAL A 1 24  ? -8.635  -11.846 37.726  1.00 25.36 ? 24   VAL A CB    1 
ATOM   167  C CG1   . VAL A 1 24  ? -8.471  -13.249 37.167  1.00 26.36 ? 24   VAL A CG1   1 
ATOM   168  C CG2   . VAL A 1 24  ? -9.968  -11.267 37.282  1.00 27.38 ? 24   VAL A CG2   1 
ATOM   169  N N     . VAL A 1 25  ? -6.044  -12.211 39.435  1.00 21.63 ? 25   VAL A N     1 
ATOM   170  C CA    . VAL A 1 25  ? -4.840  -13.084 39.540  1.00 21.27 ? 25   VAL A CA    1 
ATOM   171  C C     . VAL A 1 25  ? -4.161  -12.926 40.904  1.00 20.41 ? 25   VAL A C     1 
ATOM   172  O O     . VAL A 1 25  ? -3.377  -13.787 41.266  1.00 21.74 ? 25   VAL A O     1 
ATOM   173  C CB    . VAL A 1 25  ? -3.846  -12.834 38.392  1.00 21.44 ? 25   VAL A CB    1 
ATOM   174  C CG1   . VAL A 1 25  ? -4.544  -13.029 37.055  1.00 20.49 ? 25   VAL A CG1   1 
ATOM   175  C CG2   . VAL A 1 25  ? -3.164  -11.498 38.457  1.00 21.32 ? 25   VAL A CG2   1 
ATOM   176  N N     . GLY A 1 26  ? -4.427  -11.834 41.614  1.00 21.90 ? 26   GLY A N     1 
ATOM   177  C CA    . GLY A 1 26  ? -3.707  -11.548 42.861  1.00 23.66 ? 26   GLY A CA    1 
ATOM   178  C C     . GLY A 1 26  ? -2.667  -10.470 42.651  1.00 26.70 ? 26   GLY A C     1 
ATOM   179  O O     . GLY A 1 26  ? -1.993  -10.439 41.590  1.00 25.68 ? 26   GLY A O     1 
ATOM   180  N N     . ASP A 1 27  ? -2.524  -9.600  43.650  1.00 24.55 ? 27   ASP A N     1 
ATOM   181  C CA    . ASP A 1 27  ? -1.542  -8.497  43.665  1.00 28.11 ? 27   ASP A CA    1 
ATOM   182  C C     . ASP A 1 27  ? -0.140  -8.997  43.245  1.00 24.48 ? 27   ASP A C     1 
ATOM   183  O O     . ASP A 1 27  ? 0.541   -8.331  42.442  1.00 27.48 ? 27   ASP A O     1 
ATOM   184  C CB    . ASP A 1 27  ? -1.594  -7.886  45.069  1.00 32.97 ? 27   ASP A CB    1 
ATOM   185  C CG    . ASP A 1 27  ? -0.549  -6.826  45.262  1.00 45.73 ? 27   ASP A CG    1 
ATOM   186  O OD1   . ASP A 1 27  ? -0.771  -5.701  44.751  1.00 53.77 ? 27   ASP A OD1   1 
ATOM   187  O OD2   . ASP A 1 27  ? 0.483   -7.149  45.890  1.00 51.17 ? 27   ASP A OD2   1 
ATOM   188  N N     . GLU A 1 28  ? 0.280   -10.146 43.749  1.00 23.92 ? 28   GLU A N     1 
ATOM   189  C CA    . GLU A 1 28  ? 1.623   -10.721 43.536  1.00 25.02 ? 28   GLU A CA    1 
ATOM   190  C C     . GLU A 1 28  ? 1.886   -10.945 42.032  1.00 24.14 ? 28   GLU A C     1 
ATOM   191  O O     . GLU A 1 28  ? 3.064   -10.879 41.599  1.00 27.47 ? 28   GLU A O     1 
ATOM   192  C CB    . GLU A 1 28  ? 1.686   -12.035 44.283  1.00 28.61 ? 28   GLU A CB    1 
ATOM   193  C CG    . GLU A 1 28  ? 2.818   -12.910 43.834  1.00 31.03 ? 28   GLU A CG    1 
ATOM   194  C CD    . GLU A 1 28  ? 3.032   -14.156 44.675  1.00 34.34 ? 28   GLU A CD    1 
ATOM   195  O OE1   . GLU A 1 28  ? 2.080   -14.634 45.351  1.00 31.35 ? 28   GLU A OE1   1 
ATOM   196  O OE2   . GLU A 1 28  ? 4.157   -14.642 44.630  1.00 39.09 ? 28   GLU A OE2   1 
ATOM   197  N N     . PHE A 1 29  ? 0.827   -11.163 41.263  1.00 21.18 ? 29   PHE A N     1 
ATOM   198  C CA    . PHE A 1 29  ? 0.905   -11.652 39.854  1.00 23.11 ? 29   PHE A CA    1 
ATOM   199  C C     . PHE A 1 29  ? 0.538   -10.532 38.881  1.00 26.10 ? 29   PHE A C     1 
ATOM   200  O O     . PHE A 1 29  ? 0.283   -10.801 37.669  1.00 24.63 ? 29   PHE A O     1 
ATOM   201  C CB    . PHE A 1 29  ? 0.043   -12.908 39.734  1.00 22.97 ? 29   PHE A CB    1 
ATOM   202  C CG    . PHE A 1 29  ? 0.602   -14.060 40.518  1.00 24.56 ? 29   PHE A CG    1 
ATOM   203  C CD1   . PHE A 1 29  ? 1.865   -14.562 40.241  1.00 24.13 ? 29   PHE A CD1   1 
ATOM   204  C CD2   . PHE A 1 29  ? -0.122  -14.625 41.544  1.00 25.04 ? 29   PHE A CD2   1 
ATOM   205  C CE1   . PHE A 1 29  ? 2.392   -15.611 40.972  1.00 26.83 ? 29   PHE A CE1   1 
ATOM   206  C CE2   . PHE A 1 29  ? 0.402   -15.676 42.279  1.00 27.20 ? 29   PHE A CE2   1 
ATOM   207  C CZ    . PHE A 1 29  ? 1.656   -16.176 41.987  1.00 28.11 ? 29   PHE A CZ    1 
ATOM   208  N N     . VAL A 1 30  ? 0.544   -9.286  39.367  1.00 23.78 ? 30   VAL A N     1 
ATOM   209  C CA    . VAL A 1 30  ? 0.499   -8.088  38.494  1.00 24.99 ? 30   VAL A CA    1 
ATOM   210  C C     . VAL A 1 30  ? 1.750   -7.263  38.806  1.00 26.39 ? 30   VAL A C     1 
ATOM   211  O O     . VAL A 1 30  ? 1.861   -6.701  39.907  1.00 24.57 ? 30   VAL A O     1 
ATOM   212  C CB    . VAL A 1 30  ? -0.817  -7.306  38.662  1.00 25.48 ? 30   VAL A CB    1 
ATOM   213  C CG1   . VAL A 1 30  ? -0.833  -6.051  37.805  1.00 25.49 ? 30   VAL A CG1   1 
ATOM   214  C CG2   . VAL A 1 30  ? -2.026  -8.185  38.332  1.00 25.21 ? 30   VAL A CG2   1 
ATOM   215  N N     . ARG A 1 31  ? 2.693   -7.286  37.875  1.00 26.18 ? 31   ARG A N     1 
ATOM   216  C CA    . ARG A 1 31  ? 3.967   -6.645  38.094  1.00 28.83 ? 31   ARG A CA    1 
ATOM   217  C C     . ARG A 1 31  ? 4.139   -5.406  37.261  1.00 28.87 ? 31   ARG A C     1 
ATOM   218  O O     . ARG A 1 31  ? 3.957   -5.440  36.065  1.00 23.89 ? 31   ARG A O     1 
ATOM   219  C CB    . ARG A 1 31  ? 5.113   -7.636  37.917  1.00 32.89 ? 31   ARG A CB    1 
ATOM   220  C CG    . ARG A 1 31  ? 5.042   -8.780  38.910  1.00 39.69 ? 31   ARG A CG    1 
ATOM   221  C CD    . ARG A 1 31  ? 6.107   -9.814  38.646  1.00 42.76 ? 31   ARG A CD    1 
ATOM   222  N NE    . ARG A 1 31  ? 6.247   -10.760 39.744  1.00 44.44 ? 31   ARG A NE    1 
ATOM   223  C CZ    . ARG A 1 31  ? 5.735   -11.981 39.730  1.00 47.09 ? 31   ARG A CZ    1 
ATOM   224  N NH1   . ARG A 1 31  ? 5.041   -12.385 38.687  1.00 45.50 ? 31   ARG A NH1   1 
ATOM   225  N NH2   . ARG A 1 31  ? 5.910   -12.794 40.756  1.00 46.72 ? 31   ARG A NH2   1 
ATOM   226  N N     . THR A 1 32  ? 4.483   -4.319  37.929  1.00 28.18 ? 32   THR A N     1 
ATOM   227  C CA    . THR A 1 32  ? 4.608   -3.033  37.272  1.00 30.24 ? 32   THR A CA    1 
ATOM   228  C C     . THR A 1 32  ? 5.864   -2.267  37.641  1.00 30.73 ? 32   THR A C     1 
ATOM   229  O O     . THR A 1 32  ? 6.104   -1.212  37.114  1.00 33.90 ? 32   THR A O     1 
ATOM   230  C CB    . THR A 1 32  ? 3.440   -2.116  37.658  1.00 33.45 ? 32   THR A CB    1 
ATOM   231  O OG1   . THR A 1 32  ? 3.340   -2.039  39.078  1.00 31.19 ? 32   THR A OG1   1 
ATOM   232  C CG2   . THR A 1 32  ? 2.127   -2.592  37.044  1.00 33.51 ? 32   THR A CG2   1 
ATOM   233  N N     . ASP A 1 33  ? 6.649   -2.806  38.549  1.00 29.98 ? 33   ASP A N     1 
ATOM   234  C CA    . ASP A 1 33  ? 7.870   -2.149  38.949  1.00 36.77 ? 33   ASP A CA    1 
ATOM   235  C C     . ASP A 1 33  ? 8.906   -2.172  37.844  1.00 36.65 ? 33   ASP A C     1 
ATOM   236  O O     . ASP A 1 33  ? 9.051   -3.144  37.152  1.00 30.52 ? 33   ASP A O     1 
ATOM   237  C CB    . ASP A 1 33  ? 8.451   -2.780  40.200  1.00 42.76 ? 33   ASP A CB    1 
ATOM   238  C CG    . ASP A 1 33  ? 7.636   -2.487  41.430  1.00 57.77 ? 33   ASP A CG    1 
ATOM   239  O OD1   . ASP A 1 33  ? 6.863   -1.510  41.412  1.00 64.79 ? 33   ASP A OD1   1 
ATOM   240  O OD2   . ASP A 1 33  ? 7.770   -3.233  42.419  1.00 64.32 ? 33   ASP A OD2   1 
ATOM   241  N N     . GLU A 1 34  ? 9.645   -1.098  37.721  1.00 40.22 ? 34   GLU A N     1 
ATOM   242  C CA    . GLU A 1 34  ? 10.614  -0.996  36.644  1.00 46.69 ? 34   GLU A CA    1 
ATOM   243  C C     . GLU A 1 34  ? 11.595  -2.127  36.708  1.00 39.10 ? 34   GLU A C     1 
ATOM   244  O O     . GLU A 1 34  ? 11.944  -2.688  35.707  1.00 38.31 ? 34   GLU A O     1 
ATOM   245  C CB    . GLU A 1 34  ? 11.300  0.384   36.629  1.00 54.75 ? 34   GLU A CB    1 
ATOM   246  C CG    . GLU A 1 34  ? 12.041  0.775   37.894  1.00 64.93 ? 34   GLU A CG    1 
ATOM   247  C CD    . GLU A 1 34  ? 13.021  1.906   37.663  1.00 71.53 ? 34   GLU A CD    1 
ATOM   248  O OE1   . GLU A 1 34  ? 14.016  1.695   36.936  1.00 67.95 ? 34   GLU A OE1   1 
ATOM   249  O OE2   . GLU A 1 34  ? 12.788  3.007   38.204  1.00 68.94 ? 34   GLU A OE2   1 
ATOM   250  N N     . ALA A 1 35  ? 11.973  -2.505  37.900  1.00 36.41 ? 35   ALA A N     1 
ATOM   251  C CA    . ALA A 1 35  ? 12.919  -3.629  38.113  1.00 37.56 ? 35   ALA A CA    1 
ATOM   252  C C     . ALA A 1 35  ? 12.331  -4.965  37.635  1.00 38.14 ? 35   ALA A C     1 
ATOM   253  O O     . ALA A 1 35  ? 13.098  -5.791  37.082  1.00 35.20 ? 35   ALA A O     1 
ATOM   254  C CB    . ALA A 1 35  ? 13.324  -3.697  39.564  1.00 41.18 ? 35   ALA A CB    1 
ATOM   255  N N     . GLU A 1 36  ? 11.029  -5.196  37.823  1.00 35.98 ? 36   GLU A N     1 
ATOM   256  C CA    . GLU A 1 36  ? 10.379  -6.457  37.372  1.00 37.55 ? 36   GLU A CA    1 
ATOM   257  C C     . GLU A 1 36  ? 10.166  -6.388  35.851  1.00 33.61 ? 36   GLU A C     1 
ATOM   258  O O     . GLU A 1 36  ? 10.373  -7.418  35.167  1.00 35.57 ? 36   GLU A O     1 
ATOM   259  C CB    . GLU A 1 36  ? 9.128   -6.741  38.202  1.00 41.74 ? 36   GLU A CB    1 
ATOM   260  C CG    . GLU A 1 36  ? 9.475   -7.276  39.592  1.00 50.85 ? 36   GLU A CG    1 
ATOM   261  C CD    . GLU A 1 36  ? 8.308   -7.511  40.552  1.00 58.36 ? 36   GLU A CD    1 
ATOM   262  O OE1   . GLU A 1 36  ? 8.291   -8.563  41.239  1.00 60.51 ? 36   GLU A OE1   1 
ATOM   263  O OE2   . GLU A 1 36  ? 7.423   -6.628  40.629  1.00 57.49 ? 36   GLU A OE2   1 
ATOM   264  N N     . LEU A 1 37  ? 9.814   -5.220  35.319  1.00 31.07 ? 37   LEU A N     1 
ATOM   265  C CA    . LEU A 1 37  ? 9.578   -5.031  33.854  1.00 31.08 ? 37   LEU A CA    1 
ATOM   266  C C     . LEU A 1 37  ? 10.900  -5.217  33.087  1.00 33.49 ? 37   LEU A C     1 
ATOM   267  O O     . LEU A 1 37  ? 10.859  -5.833  32.002  1.00 34.41 ? 37   LEU A O     1 
ATOM   268  C CB    . LEU A 1 37  ? 8.965   -3.654  33.599  1.00 31.44 ? 37   LEU A CB    1 
ATOM   269  C CG    . LEU A 1 37  ? 7.574   -3.415  34.187  1.00 32.63 ? 37   LEU A CG    1 
ATOM   270  C CD1   . LEU A 1 37  ? 7.078   -2.010  33.847  1.00 37.37 ? 37   LEU A CD1   1 
ATOM   271  C CD2   . LEU A 1 37  ? 6.598   -4.472  33.713  1.00 32.08 ? 37   LEU A CD2   1 
ATOM   272  N N     . ALA A 1 38  ? 12.032  -4.760  33.645  1.00 31.54 ? 38   ALA A N     1 
ATOM   273  C CA    . ALA A 1 38  ? 13.387  -4.863  33.047  1.00 35.71 ? 38   ALA A CA    1 
ATOM   274  C C     . ALA A 1 38  ? 13.717  -6.329  32.768  1.00 34.08 ? 38   ALA A C     1 
ATOM   275  O O     . ALA A 1 38  ? 14.463  -6.618  31.822  1.00 31.73 ? 38   ALA A O     1 
ATOM   276  C CB    . ALA A 1 38  ? 14.437  -4.238  33.941  1.00 37.78 ? 38   ALA A CB    1 
ATOM   277  N N     . ARG A 1 39  ? 13.122  -7.235  33.531  1.00 34.65 ? 39   ARG A N     1 
ATOM   278  C CA    . ARG A 1 39  ? 13.372  -8.684  33.404  1.00 36.34 ? 39   ARG A CA    1 
ATOM   279  C C     . ARG A 1 39  ? 12.774  -9.203  32.085  1.00 34.21 ? 39   ARG A C     1 
ATOM   280  O O     . ARG A 1 39  ? 13.192  -10.280 31.668  1.00 34.13 ? 39   ARG A O     1 
ATOM   281  C CB    . ARG A 1 39  ? 12.823  -9.393  34.643  1.00 45.93 ? 39   ARG A CB    1 
ATOM   282  C CG    . ARG A 1 39  ? 13.754  -10.440 35.236  1.00 55.11 ? 39   ARG A CG    1 
ATOM   283  C CD    . ARG A 1 39  ? 13.576  -10.608 36.741  1.00 60.57 ? 39   ARG A CD    1 
ATOM   284  N NE    . ARG A 1 39  ? 12.197  -10.933 37.088  1.00 71.94 ? 39   ARG A NE    1 
ATOM   285  C CZ    . ARG A 1 39  ? 11.617  -12.124 36.918  1.00 80.26 ? 39   ARG A CZ    1 
ATOM   286  N NH1   . ARG A 1 39  ? 12.292  -13.137 36.396  1.00 83.11 ? 39   ARG A NH1   1 
ATOM   287  N NH2   . ARG A 1 39  ? 10.350  -12.292 37.258  1.00 84.91 ? 39   ARG A NH2   1 
ATOM   288  N N     . PHE A 1 40  ? 11.850  -8.467  31.457  1.00 32.50 ? 40   PHE A N     1 
ATOM   289  C CA    . PHE A 1 40  ? 11.105  -8.892  30.230  1.00 31.68 ? 40   PHE A CA    1 
ATOM   290  C C     . PHE A 1 40  ? 11.622  -8.122  29.021  1.00 28.78 ? 40   PHE A C     1 
ATOM   291  O O     . PHE A 1 40  ? 11.019  -8.205  27.949  1.00 28.65 ? 40   PHE A O     1 
ATOM   292  C CB    . PHE A 1 40  ? 9.603   -8.710  30.438  1.00 33.88 ? 40   PHE A CB    1 
ATOM   293  C CG    . PHE A 1 40  ? 9.065   -9.715  31.424  1.00 34.32 ? 40   PHE A CG    1 
ATOM   294  C CD1   . PHE A 1 40  ? 9.239   -9.526  32.786  1.00 37.91 ? 40   PHE A CD1   1 
ATOM   295  C CD2   . PHE A 1 40  ? 8.470   -10.893 30.995  1.00 35.98 ? 40   PHE A CD2   1 
ATOM   296  C CE1   . PHE A 1 40  ? 8.780   -10.463 33.697  1.00 36.37 ? 40   PHE A CE1   1 
ATOM   297  C CE2   . PHE A 1 40  ? 8.012   -11.826 31.906  1.00 32.34 ? 40   PHE A CE2   1 
ATOM   298  C CZ    . PHE A 1 40  ? 8.169   -11.613 33.256  1.00 36.77 ? 40   PHE A CZ    1 
ATOM   299  N N     . HIS A 1 41  ? 12.695  -7.349  29.231  1.00 28.19 ? 41   HIS A N     1 
ATOM   300  C CA    . HIS A 1 41  ? 13.428  -6.639  28.159  1.00 27.07 ? 41   HIS A CA    1 
ATOM   301  C C     . HIS A 1 41  ? 13.968  -7.695  27.208  1.00 24.32 ? 41   HIS A C     1 
ATOM   302  O O     . HIS A 1 41  ? 14.457  -8.737  27.672  1.00 25.57 ? 41   HIS A O     1 
ATOM   303  C CB    . HIS A 1 41  ? 14.581  -5.788  28.715  1.00 31.96 ? 41   HIS A CB    1 
ATOM   304  C CG    . HIS A 1 41  ? 14.157  -4.486  29.298  1.00 34.24 ? 41   HIS A CG    1 
ATOM   305  N ND1   . HIS A 1 41  ? 15.044  -3.664  29.971  1.00 37.15 ? 41   HIS A ND1   1 
ATOM   306  C CD2   . HIS A 1 41  ? 12.964  -3.862  29.312  1.00 36.99 ? 41   HIS A CD2   1 
ATOM   307  C CE1   . HIS A 1 41  ? 14.414  -2.586  30.365  1.00 37.11 ? 41   HIS A CE1   1 
ATOM   308  N NE2   . HIS A 1 41  ? 13.139  -2.678  29.969  1.00 41.04 ? 41   HIS A NE2   1 
ATOM   309  N N     . ASP A 1 42  ? 13.926  -7.415  25.916  1.00 23.99 ? 42   ASP A N     1 
ATOM   310  C CA    . ASP A 1 42  ? 14.673  -8.227  24.930  1.00 23.39 ? 42   ASP A CA    1 
ATOM   311  C C     . ASP A 1 42  ? 16.136  -8.194  25.351  1.00 24.39 ? 42   ASP A C     1 
ATOM   312  O O     . ASP A 1 42  ? 16.722  -7.128  25.459  1.00 22.41 ? 42   ASP A O     1 
ATOM   313  C CB    . ASP A 1 42  ? 14.427  -7.656  23.541  1.00 21.09 ? 42   ASP A CB    1 
ATOM   314  C CG    . ASP A 1 42  ? 15.120  -8.388  22.424  1.00 22.92 ? 42   ASP A CG    1 
ATOM   315  O OD1   . ASP A 1 42  ? 15.834  -9.361  22.719  1.00 25.05 ? 42   ASP A OD1   1 
ATOM   316  O OD2   . ASP A 1 42  ? 14.932  -7.935  21.290  1.00 26.23 ? 42   ASP A OD2   1 
ATOM   317  N N     . PRO A 1 43  ? 16.798  -9.339  25.602  1.00 25.88 ? 43   PRO A N     1 
ATOM   318  C CA    . PRO A 1 43  ? 18.216  -9.326  25.936  1.00 26.32 ? 43   PRO A CA    1 
ATOM   319  C C     . PRO A 1 43  ? 19.107  -8.947  24.739  1.00 27.26 ? 43   PRO A C     1 
ATOM   320  O O     . PRO A 1 43  ? 20.237  -8.544  24.949  1.00 27.04 ? 43   PRO A O     1 
ATOM   321  C CB    . PRO A 1 43  ? 18.518  -10.767 26.333  1.00 26.65 ? 43   PRO A CB    1 
ATOM   322  C CG    . PRO A 1 43  ? 17.479  -11.568 25.566  1.00 28.52 ? 43   PRO A CG    1 
ATOM   323  C CD    . PRO A 1 43  ? 16.243  -10.699 25.529  1.00 25.81 ? 43   PRO A CD    1 
ATOM   324  N N     . TYR A 1 44  ? 18.589  -9.094  23.513  1.00 26.14 ? 44   TYR A N     1 
ATOM   325  C CA    . TYR A 1 44  ? 19.380  -8.911  22.269  1.00 25.55 ? 44   TYR A CA    1 
ATOM   326  C C     . TYR A 1 44  ? 18.657  -7.897  21.391  1.00 25.07 ? 44   TYR A C     1 
ATOM   327  O O     . TYR A 1 44  ? 18.297  -8.206  20.250  1.00 23.94 ? 44   TYR A O     1 
ATOM   328  C CB    . TYR A 1 44  ? 19.589  -10.252 21.558  1.00 25.59 ? 44   TYR A CB    1 
ATOM   329  C CG    . TYR A 1 44  ? 20.154  -11.396 22.365  1.00 25.53 ? 44   TYR A CG    1 
ATOM   330  C CD1   . TYR A 1 44  ? 21.020  -11.198 23.430  1.00 25.80 ? 44   TYR A CD1   1 
ATOM   331  C CD2   . TYR A 1 44  ? 19.854  -12.712 22.029  1.00 25.30 ? 44   TYR A CD2   1 
ATOM   332  C CE1   . TYR A 1 44  ? 21.555  -12.269 24.132  1.00 25.02 ? 44   TYR A CE1   1 
ATOM   333  C CE2   . TYR A 1 44  ? 20.399  -13.788 22.703  1.00 23.92 ? 44   TYR A CE2   1 
ATOM   334  C CZ    . TYR A 1 44  ? 21.239  -13.564 23.776  1.00 25.38 ? 44   TYR A CZ    1 
ATOM   335  O OH    . TYR A 1 44  ? 21.776  -14.627 24.444  1.00 26.10 ? 44   TYR A OH    1 
ATOM   336  N N     . PRO A 1 45  ? 18.433  -6.658  21.890  1.00 24.34 ? 45   PRO A N     1 
ATOM   337  C CA    . PRO A 1 45  ? 17.708  -5.638  21.141  1.00 25.06 ? 45   PRO A CA    1 
ATOM   338  C C     . PRO A 1 45  ? 18.483  -5.234  19.881  1.00 27.96 ? 45   PRO A C     1 
ATOM   339  O O     . PRO A 1 45  ? 19.704  -5.206  19.907  1.00 26.24 ? 45   PRO A O     1 
ATOM   340  C CB    . PRO A 1 45  ? 17.642  -4.431  22.087  1.00 26.77 ? 45   PRO A CB    1 
ATOM   341  C CG    . PRO A 1 45  ? 18.807  -4.625  22.980  1.00 25.94 ? 45   PRO A CG    1 
ATOM   342  C CD    . PRO A 1 45  ? 18.917  -6.126  23.175  1.00 25.17 ? 45   PRO A CD    1 
ATOM   343  N N     . VAL A 1 46  ? 17.759  -4.950  18.810  1.00 33.22 ? 46   VAL A N     1 
ATOM   344  C CA    . VAL A 1 46  ? 18.378  -4.752  17.474  1.00 41.00 ? 46   VAL A CA    1 
ATOM   345  C C     . VAL A 1 46  ? 18.306  -3.282  17.055  1.00 48.56 ? 46   VAL A C     1 
ATOM   346  O O     . VAL A 1 46  ? 19.294  -2.813  16.497  1.00 60.31 ? 46   VAL A O     1 
ATOM   347  C CB    . VAL A 1 46  ? 17.753  -5.749  16.499  1.00 42.38 ? 46   VAL A CB    1 
ATOM   348  C CG1   . VAL A 1 46  ? 17.191  -5.116  15.250  1.00 47.38 ? 46   VAL A CG1   1 
ATOM   349  C CG2   . VAL A 1 46  ? 18.740  -6.881  16.226  1.00 43.75 ? 46   VAL A CG2   1 
ATOM   350  N N     . GLY A 1 47  ? 17.216  -2.573  17.315  1.00 55.48 ? 47   GLY A N     1 
ATOM   351  C CA    . GLY A 1 47  ? 17.177  -1.131  17.015  1.00 59.30 ? 47   GLY A CA    1 
ATOM   352  C C     . GLY A 1 47  ? 17.542  -0.342  18.258  1.00 54.44 ? 47   GLY A C     1 
ATOM   353  O O     . GLY A 1 47  ? 18.531  -0.696  18.924  1.00 53.00 ? 47   GLY A O     1 
ATOM   354  N N     . ASP A 1 48  ? 16.714  0.639   18.621  1.00 56.40 ? 48   ASP A N     1 
ATOM   355  C CA    . ASP A 1 48  ? 16.698  1.227   19.984  1.00 54.82 ? 48   ASP A CA    1 
ATOM   356  C C     . ASP A 1 48  ? 16.487  0.074   20.976  1.00 61.38 ? 48   ASP A C     1 
ATOM   357  O O     . ASP A 1 48  ? 15.588  -0.769  20.740  1.00 61.36 ? 48   ASP A O     1 
ATOM   358  C CB    . ASP A 1 48  ? 15.596  2.285   20.092  1.00 53.62 ? 48   ASP A CB    1 
ATOM   359  N N     . ALA A 1 49  ? 17.271  0.010   22.051  1.00 63.78 ? 49   ALA A N     1 
ATOM   360  C CA    . ALA A 1 49  ? 17.044  -0.962  23.147  1.00 63.08 ? 49   ALA A CA    1 
ATOM   361  C C     . ALA A 1 49  ? 15.694  -0.662  23.826  1.00 62.46 ? 49   ALA A C     1 
ATOM   362  O O     . ALA A 1 49  ? 15.093  -1.611  24.323  1.00 62.69 ? 49   ALA A O     1 
ATOM   363  C CB    . ALA A 1 49  ? 18.204  -0.944  24.110  1.00 61.08 ? 49   ALA A CB    1 
ATOM   364  N N     . ASP A 1 50  ? 15.227  0.596   23.788  1.00 61.57 ? 50   ASP A N     1 
ATOM   365  C CA    . ASP A 1 50  ? 13.981  1.124   24.423  1.00 56.25 ? 50   ASP A CA    1 
ATOM   366  C C     . ASP A 1 50  ? 12.717  0.818   23.584  1.00 49.96 ? 50   ASP A C     1 
ATOM   367  O O     . ASP A 1 50  ? 11.618  1.220   23.989  1.00 48.21 ? 50   ASP A O     1 
ATOM   368  C CB    . ASP A 1 50  ? 14.159  2.626   24.696  1.00 59.72 ? 50   ASP A CB    1 
ATOM   369  C CG    . ASP A 1 50  ? 13.094  3.571   24.153  1.00 70.66 ? 50   ASP A CG    1 
ATOM   370  O OD1   . ASP A 1 50  ? 13.049  3.769   22.919  1.00 76.41 ? 50   ASP A OD1   1 
ATOM   371  O OD2   . ASP A 1 50  ? 12.335  4.142   24.975  1.00 76.38 ? 50   ASP A OD2   1 
ATOM   372  N N     . ALA A 1 51  ? 12.824  0.211   22.412  1.00 43.62 ? 51   ALA A N     1 
ATOM   373  C CA    . ALA A 1 51  ? 11.646  -0.291  21.671  1.00 46.42 ? 51   ALA A CA    1 
ATOM   374  C C     . ALA A 1 51  ? 11.198  -1.566  22.401  1.00 42.87 ? 51   ALA A C     1 
ATOM   375  O O     . ALA A 1 51  ? 12.006  -2.167  23.116  1.00 57.43 ? 51   ALA A O     1 
ATOM   376  C CB    . ALA A 1 51  ? 11.983  -0.535  20.222  1.00 44.62 ? 51   ALA A CB    1 
ATOM   377  N N     . HIS A 1 52  ? 9.955   -1.964  22.241  1.00 40.77 ? 52   HIS A N     1 
ATOM   378  C CA    . HIS A 1 52  ? 9.417   -3.240  22.785  1.00 31.87 ? 52   HIS A CA    1 
ATOM   379  C C     . HIS A 1 52  ? 9.505   -3.271  24.321  1.00 30.97 ? 52   HIS A C     1 
ATOM   380  O O     . HIS A 1 52  ? 10.138  -4.202  24.862  1.00 28.20 ? 52   HIS A O     1 
ATOM   381  C CB    . HIS A 1 52  ? 10.136  -4.399  22.085  1.00 27.69 ? 52   HIS A CB    1 
ATOM   382  C CG    . HIS A 1 52  ? 10.075  -4.184  20.616  1.00 29.10 ? 52   HIS A CG    1 
ATOM   383  N ND1   . HIS A 1 52  ? 11.206  -3.906  19.859  1.00 31.34 ? 52   HIS A ND1   1 
ATOM   384  C CD2   . HIS A 1 52  ? 9.016   -4.056  19.795  1.00 26.25 ? 52   HIS A CD2   1 
ATOM   385  C CE1   . HIS A 1 52  ? 10.832  -3.666  18.601  1.00 27.11 ? 52   HIS A CE1   1 
ATOM   386  N NE2   . HIS A 1 52  ? 9.494   -3.739  18.541  1.00 29.66 ? 52   HIS A NE2   1 
ATOM   387  N N     . LEU A 1 53  ? 8.864   -2.309  24.993  1.00 27.96 ? 53   LEU A N     1 
ATOM   388  C CA    . LEU A 1 53  ? 8.761   -2.278  26.478  1.00 27.88 ? 53   LEU A CA    1 
ATOM   389  C C     . LEU A 1 53  ? 7.411   -2.881  26.872  1.00 26.40 ? 53   LEU A C     1 
ATOM   390  O O     . LEU A 1 53  ? 6.457   -2.758  26.110  1.00 26.86 ? 53   LEU A O     1 
ATOM   391  C CB    . LEU A 1 53  ? 8.851   -0.834  26.968  1.00 29.87 ? 53   LEU A CB    1 
ATOM   392  C CG    . LEU A 1 53  ? 10.182  -0.127  26.704  1.00 32.26 ? 53   LEU A CG    1 
ATOM   393  C CD1   . LEU A 1 53  ? 10.103  1.328   27.162  1.00 33.64 ? 53   LEU A CD1   1 
ATOM   394  C CD2   . LEU A 1 53  ? 11.348  -0.855  27.359  1.00 31.53 ? 53   LEU A CD2   1 
ATOM   395  N N     . ALA A 1 54  ? 7.355   -3.467  28.052  1.00 27.23 ? 54   ALA A N     1 
ATOM   396  C CA    . ALA A 1 54  ? 6.116   -3.957  28.678  1.00 28.27 ? 54   ALA A CA    1 
ATOM   397  C C     . ALA A 1 54  ? 5.637   -2.884  29.655  1.00 27.08 ? 54   ALA A C     1 
ATOM   398  O O     . ALA A 1 54  ? 6.502   -2.293  30.319  1.00 28.97 ? 54   ALA A O     1 
ATOM   399  C CB    . ALA A 1 54  ? 6.386   -5.262  29.371  1.00 26.22 ? 54   ALA A CB    1 
ATOM   400  N N     . SER A 1 55  ? 4.332   -2.629  29.692  1.00 28.43 ? 55   SER A N     1 
ATOM   401  C CA    . SER A 1 55  ? 3.697   -1.705  30.678  1.00 29.36 ? 55   SER A CA    1 
ATOM   402  C C     . SER A 1 55  ? 3.391   -2.485  31.964  1.00 28.61 ? 55   SER A C     1 
ATOM   403  O O     . SER A 1 55  ? 3.306   -1.870  33.049  1.00 26.04 ? 55   SER A O     1 
ATOM   404  C CB    . SER A 1 55  ? 2.488   -1.045  30.104  1.00 29.92 ? 55   SER A CB    1 
ATOM   405  O OG    . SER A 1 55  ? 1.494   -1.995  29.743  1.00 31.66 ? 55   SER A OG    1 
ATOM   406  N N     . ALA A 1 56  ? 3.237   -3.800  31.867  1.00 24.96 ? 56   ALA A N     1 
ATOM   407  C CA    . ALA A 1 56  ? 2.943   -4.658  33.030  1.00 24.07 ? 56   ALA A CA    1 
ATOM   408  C C     . ALA A 1 56  ? 3.105   -6.112  32.618  1.00 26.44 ? 56   ALA A C     1 
ATOM   409  O O     . ALA A 1 56  ? 3.135   -6.374  31.415  1.00 23.97 ? 56   ALA A O     1 
ATOM   410  C CB    . ALA A 1 56  ? 1.551   -4.377  33.509  1.00 25.66 ? 56   ALA A CB    1 
ATOM   411  N N     . VAL A 1 57  ? 3.226   -7.004  33.597  1.00 23.87 ? 57   VAL A N     1 
ATOM   412  C CA    . VAL A 1 57  ? 3.231   -8.479  33.374  1.00 22.71 ? 57   VAL A CA    1 
ATOM   413  C C     . VAL A 1 57  ? 2.159   -9.082  34.288  1.00 24.88 ? 57   VAL A C     1 
ATOM   414  O O     . VAL A 1 57  ? 2.167   -8.766  35.506  1.00 25.14 ? 57   VAL A O     1 
ATOM   415  C CB    . VAL A 1 57  ? 4.619   -9.097  33.603  1.00 21.36 ? 57   VAL A CB    1 
ATOM   416  C CG1   . VAL A 1 57  ? 4.607   -10.591 33.326  1.00 23.67 ? 57   VAL A CG1   1 
ATOM   417  C CG2   . VAL A 1 57  ? 5.674   -8.395  32.757  1.00 23.29 ? 57   VAL A CG2   1 
ATOM   418  N N     . ILE A 1 58  ? 1.264   -9.877  33.710  1.00 22.37 ? 58   ILE A N     1 
ATOM   419  C CA    . ILE A 1 58  ? 0.115   -10.521 34.405  1.00 25.16 ? 58   ILE A CA    1 
ATOM   420  C C     . ILE A 1 58  ? 0.335   -12.023 34.345  1.00 24.48 ? 58   ILE A C     1 
ATOM   421  O O     . ILE A 1 58  ? 0.572   -12.537 33.232  1.00 23.91 ? 58   ILE A O     1 
ATOM   422  C CB    . ILE A 1 58  ? -1.229  -10.158 33.734  1.00 28.59 ? 58   ILE A CB    1 
ATOM   423  C CG1   . ILE A 1 58  ? -1.372  -8.665  33.450  1.00 33.05 ? 58   ILE A CG1   1 
ATOM   424  C CG2   . ILE A 1 58  ? -2.400  -10.715 34.540  1.00 34.22 ? 58   ILE A CG2   1 
ATOM   425  C CD1   . ILE A 1 58  ? -1.223  -7.800  34.651  1.00 29.34 ? 58   ILE A CD1   1 
ATOM   426  N N     . SER A 1 59  ? 0.223   -12.721 35.466  1.00 20.42 ? 59   SER A N     1 
ATOM   427  C CA    . SER A 1 59  ? 0.452   -14.187 35.531  1.00 22.32 ? 59   SER A CA    1 
ATOM   428  C C     . SER A 1 59  ? -0.830  -14.882 35.966  1.00 22.73 ? 59   SER A C     1 
ATOM   429  O O     . SER A 1 59  ? -1.117  -15.014 37.165  1.00 22.82 ? 59   SER A O     1 
ATOM   430  C CB    . SER A 1 59  ? 1.594   -14.521 36.417  1.00 21.79 ? 59   SER A CB    1 
ATOM   431  O OG    . SER A 1 59  ? 2.793   -13.881 35.962  1.00 20.85 ? 59   SER A OG    1 
ATOM   432  N N     . PRO A 1 60  ? -1.677  -15.291 35.007  1.00 21.29 ? 60   PRO A N     1 
ATOM   433  C CA    . PRO A 1 60  ? -2.937  -15.956 35.324  1.00 19.77 ? 60   PRO A CA    1 
ATOM   434  C C     . PRO A 1 60  ? -2.698  -17.374 35.861  1.00 19.53 ? 60   PRO A C     1 
ATOM   435  O O     . PRO A 1 60  ? -1.696  -18.025 35.518  1.00 20.17 ? 60   PRO A O     1 
ATOM   436  C CB    . PRO A 1 60  ? -3.732  -15.882 34.010  1.00 22.03 ? 60   PRO A CB    1 
ATOM   437  C CG    . PRO A 1 60  ? -2.679  -15.766 32.949  1.00 23.67 ? 60   PRO A CG    1 
ATOM   438  C CD    . PRO A 1 60  ? -1.475  -15.095 33.565  1.00 21.63 ? 60   PRO A CD    1 
ATOM   439  N N     . ARG A 1 61  ? -3.544  -17.813 36.794  1.00 19.17 ? 61   ARG A N     1 
ATOM   440  C CA    . ARG A 1 61  ? -3.365  -19.112 37.483  1.00 20.14 ? 61   ARG A CA    1 
ATOM   441  C C     . ARG A 1 61  ? -3.708  -20.272 36.538  1.00 20.47 ? 61   ARG A C     1 
ATOM   442  O O     . ARG A 1 61  ? -3.115  -21.358 36.641  1.00 23.12 ? 61   ARG A O     1 
ATOM   443  C CB    . ARG A 1 61  ? -4.264  -19.212 38.724  1.00 18.69 ? 61   ARG A CB    1 
ATOM   444  C CG    . ARG A 1 61  ? -4.096  -20.527 39.461  1.00 18.60 ? 61   ARG A CG    1 
ATOM   445  C CD    . ARG A 1 61  ? -4.862  -20.458 40.790  1.00 20.97 ? 61   ARG A CD    1 
ATOM   446  N NE    . ARG A 1 61  ? -6.286  -20.237 40.570  1.00 20.72 ? 61   ARG A NE    1 
ATOM   447  C CZ    . ARG A 1 61  ? -7.108  -19.633 41.430  1.00 22.00 ? 61   ARG A CZ    1 
ATOM   448  N NH1   . ARG A 1 61  ? -6.616  -19.060 42.524  1.00 21.79 ? 61   ARG A NH1   1 
ATOM   449  N NH2   . ARG A 1 61  ? -8.387  -19.514 41.124  1.00 24.08 ? 61   ARG A NH2   1 
ATOM   450  N N     . ASP A 1 62  ? -4.714  -20.074 35.703  1.00 20.48 ? 62   ASP A N     1 
ATOM   451  C CA    . ASP A 1 62  ? -5.402  -21.178 34.985  1.00 22.59 ? 62   ASP A CA    1 
ATOM   452  C C     . ASP A 1 62  ? -6.221  -20.579 33.850  1.00 20.05 ? 62   ASP A C     1 
ATOM   453  O O     . ASP A 1 62  ? -6.267  -19.346 33.713  1.00 21.59 ? 62   ASP A O     1 
ATOM   454  C CB    . ASP A 1 62  ? -6.288  -21.992 35.946  1.00 21.46 ? 62   ASP A CB    1 
ATOM   455  C CG    . ASP A 1 62  ? -7.206  -21.126 36.809  1.00 23.11 ? 62   ASP A CG    1 
ATOM   456  O OD1   . ASP A 1 62  ? -7.766  -20.145 36.290  1.00 22.10 ? 62   ASP A OD1   1 
ATOM   457  O OD2   . ASP A 1 62  ? -7.332  -21.437 38.006  1.00 22.79 ? 62   ASP A OD2   1 
ATOM   458  N N     . THR A 1 63  ? -6.791  -21.438 33.017  1.00 21.07 ? 63   THR A N     1 
ATOM   459  C CA    . THR A 1 63  ? -7.632  -21.076 31.849  1.00 19.85 ? 63   THR A CA    1 
ATOM   460  C C     . THR A 1 63  ? -8.680  -20.023 32.221  1.00 22.87 ? 63   THR A C     1 
ATOM   461  O O     . THR A 1 63  ? -8.846  -19.018 31.503  1.00 20.86 ? 63   THR A O     1 
ATOM   462  C CB    . THR A 1 63  ? -8.275  -22.354 31.273  1.00 19.93 ? 63   THR A CB    1 
ATOM   463  O OG1   . THR A 1 63  ? -7.192  -23.185 30.874  1.00 20.66 ? 63   THR A OG1   1 
ATOM   464  C CG2   . THR A 1 63  ? -9.174  -22.054 30.103  1.00 20.65 ? 63   THR A CG2   1 
ATOM   465  N N     . GLU A 1 64  ? -9.381  -20.237 33.335  1.00 23.65 ? 64   GLU A N     1 
ATOM   466  C CA    . GLU A 1 64  ? -10.485 -19.353 33.763  1.00 23.17 ? 64   GLU A CA    1 
ATOM   467  C C     . GLU A 1 64  ? -9.921  -17.944 33.962  1.00 19.90 ? 64   GLU A C     1 
ATOM   468  O O     . GLU A 1 64  ? -10.560 -16.984 33.563  1.00 21.99 ? 64   GLU A O     1 
ATOM   469  C CB    . GLU A 1 64  ? -11.147 -19.943 35.024  1.00 25.17 ? 64   GLU A CB    1 
ATOM   470  C CG    . GLU A 1 64  ? -11.810 -21.284 34.798  1.00 33.83 ? 64   GLU A CG    1 
ATOM   471  C CD    . GLU A 1 64  ? -11.007 -22.593 34.673  1.00 41.13 ? 64   GLU A CD    1 
ATOM   472  O OE1   . GLU A 1 64  ? -9.731  -22.618 34.873  1.00 29.59 ? 64   GLU A OE1   1 
ATOM   473  O OE2   . GLU A 1 64  ? -11.668 -23.616 34.320  1.00 55.22 ? 64   GLU A OE2   1 
ATOM   474  N N     . GLN A 1 65  ? -8.764  -17.818 34.595  1.00 20.94 ? 65   GLN A N     1 
ATOM   475  C CA    . GLN A 1 65  ? -8.129  -16.498 34.837  1.00 20.48 ? 65   GLN A CA    1 
ATOM   476  C C     . GLN A 1 65  ? -7.673  -15.892 33.505  1.00 19.95 ? 65   GLN A C     1 
ATOM   477  O O     . GLN A 1 65  ? -7.808  -14.674 33.354  1.00 21.43 ? 65   GLN A O     1 
ATOM   478  C CB    . GLN A 1 65  ? -7.033  -16.629 35.874  1.00 21.57 ? 65   GLN A CB    1 
ATOM   479  C CG    . GLN A 1 65  ? -7.617  -16.768 37.282  1.00 21.11 ? 65   GLN A CG    1 
ATOM   480  C CD    . GLN A 1 65  ? -6.589  -16.543 38.356  1.00 22.31 ? 65   GLN A CD    1 
ATOM   481  O OE1   . GLN A 1 65  ? -5.456  -16.177 38.065  1.00 19.71 ? 65   GLN A OE1   1 
ATOM   482  N NE2   . GLN A 1 65  ? -6.978  -16.788 39.605  1.00 20.21 ? 65   GLN A NE2   1 
ATOM   483  N N     . VAL A 1 66  ? -7.234  -16.712 32.559  1.00 20.68 ? 66   VAL A N     1 
ATOM   484  C CA    . VAL A 1 66  ? -6.813  -16.190 31.223  1.00 19.95 ? 66   VAL A CA    1 
ATOM   485  C C     . VAL A 1 66  ? -8.036  -15.553 30.578  1.00 18.94 ? 66   VAL A C     1 
ATOM   486  O O     . VAL A 1 66  ? -7.927  -14.404 30.106  1.00 20.91 ? 66   VAL A O     1 
ATOM   487  C CB    . VAL A 1 66  ? -6.184  -17.270 30.321  1.00 20.45 ? 66   VAL A CB    1 
ATOM   488  C CG1   . VAL A 1 66  ? -5.911  -16.713 28.944  1.00 21.36 ? 66   VAL A CG1   1 
ATOM   489  C CG2   . VAL A 1 66  ? -4.910  -17.843 30.913  1.00 20.20 ? 66   VAL A CG2   1 
ATOM   490  N N     . GLN A 1 67  ? -9.169  -16.255 30.577  1.00 20.64 ? 67   GLN A N     1 
ATOM   491  C CA    . GLN A 1 67  ? -10.431 -15.724 30.038  1.00 19.95 ? 67   GLN A CA    1 
ATOM   492  C C     . GLN A 1 67  ? -10.770 -14.402 30.718  1.00 21.16 ? 67   GLN A C     1 
ATOM   493  O O     . GLN A 1 67  ? -11.114 -13.452 30.034  1.00 22.22 ? 67   GLN A O     1 
ATOM   494  C CB    . GLN A 1 67  ? -11.555 -16.726 30.233  1.00 22.11 ? 67   GLN A CB    1 
ATOM   495  C CG    . GLN A 1 67  ? -11.362 -18.016 29.479  1.00 20.75 ? 67   GLN A CG    1 
ATOM   496  C CD    . GLN A 1 67  ? -12.531 -18.914 29.770  1.00 21.97 ? 67   GLN A CD    1 
ATOM   497  O OE1   . GLN A 1 67  ? -12.479 -19.722 30.675  1.00 22.66 ? 67   GLN A OE1   1 
ATOM   498  N NE2   . GLN A 1 67  ? -13.602 -18.738 29.024  1.00 21.51 ? 67   GLN A NE2   1 
ATOM   499  N N     . GLU A 1 68  ? -10.667 -14.324 32.042  1.00 21.50 ? 68   GLU A N     1 
ATOM   500  C CA    . GLU A 1 68  ? -11.105 -13.095 32.756  1.00 22.96 ? 68   GLU A CA    1 
ATOM   501  C C     . GLU A 1 68  ? -10.114 -11.957 32.469  1.00 22.24 ? 68   GLU A C     1 
ATOM   502  O O     . GLU A 1 68  ? -10.596 -10.848 32.238  1.00 21.87 ? 68   GLU A O     1 
ATOM   503  C CB    . GLU A 1 68  ? -11.308 -13.375 34.250  1.00 27.24 ? 68   GLU A CB    1 
ATOM   504  C CG    . GLU A 1 68  ? -12.236 -12.378 34.912  1.00 34.84 ? 68   GLU A CG    1 
ATOM   505  C CD    . GLU A 1 68  ? -13.473 -11.916 34.142  1.00 36.99 ? 68   GLU A CD    1 
ATOM   506  O OE1   . GLU A 1 68  ? -14.225 -12.762 33.623  1.00 36.11 ? 68   GLU A OE1   1 
ATOM   507  O OE2   . GLU A 1 68  ? -13.702 -10.696 34.102  1.00 39.14 ? 68   GLU A OE2   1 
ATOM   508  N N     . VAL A 1 69  ? -8.811  -12.210 32.366  1.00 20.79 ? 69   VAL A N     1 
ATOM   509  C CA    . VAL A 1 69  ? -7.838  -11.124 32.024  1.00 23.37 ? 69   VAL A CA    1 
ATOM   510  C C     . VAL A 1 69  ? -8.129  -10.685 30.589  1.00 20.52 ? 69   VAL A C     1 
ATOM   511  O O     . VAL A 1 69  ? -8.063  -9.499  30.338  1.00 19.51 ? 69   VAL A O     1 
ATOM   512  C CB    . VAL A 1 69  ? -6.349  -11.439 32.265  1.00 28.13 ? 69   VAL A CB    1 
ATOM   513  C CG1   . VAL A 1 69  ? -6.054  -11.786 33.719  1.00 25.81 ? 69   VAL A CG1   1 
ATOM   514  C CG2   . VAL A 1 69  ? -5.780  -12.487 31.342  1.00 33.45 ? 69   VAL A CG2   1 
ATOM   515  N N     . VAL A 1 70  ? -8.487  -11.602 29.698  1.00 20.62 ? 70   VAL A N     1 
ATOM   516  C CA    . VAL A 1 70  ? -8.821  -11.220 28.296  1.00 22.16 ? 70   VAL A CA    1 
ATOM   517  C C     . VAL A 1 70  ? -10.090 -10.355 28.283  1.00 21.07 ? 70   VAL A C     1 
ATOM   518  O O     . VAL A 1 70  ? -10.111 -9.328  27.605  1.00 20.43 ? 70   VAL A O     1 
ATOM   519  C CB    . VAL A 1 70  ? -8.896  -12.443 27.366  1.00 22.10 ? 70   VAL A CB    1 
ATOM   520  C CG1   . VAL A 1 70  ? -9.442  -12.053 26.013  1.00 23.32 ? 70   VAL A CG1   1 
ATOM   521  C CG2   . VAL A 1 70  ? -7.537  -13.122 27.238  1.00 21.52 ? 70   VAL A CG2   1 
ATOM   522  N N     . ARG A 1 71  ? -11.121 -10.713 29.033  1.00 22.29 ? 71   ARG A N     1 
ATOM   523  C CA    . ARG A 1 71  ? -12.359 -9.886  29.135  1.00 23.79 ? 71   ARG A CA    1 
ATOM   524  C C     . ARG A 1 71  ? -12.031 -8.492  29.694  1.00 21.55 ? 71   ARG A C     1 
ATOM   525  O O     . ARG A 1 71  ? -12.593 -7.546  29.208  1.00 24.71 ? 71   ARG A O     1 
ATOM   526  C CB    . ARG A 1 71  ? -13.421 -10.585 29.987  1.00 23.28 ? 71   ARG A CB    1 
ATOM   527  C CG    . ARG A 1 71  ? -13.921 -11.900 29.397  1.00 24.82 ? 71   ARG A CG    1 
ATOM   528  C CD    . ARG A 1 71  ? -15.037 -12.503 30.225  1.00 27.69 ? 71   ARG A CD    1 
ATOM   529  N NE    . ARG A 1 71  ? -15.325 -13.866 29.818  1.00 26.86 ? 71   ARG A NE    1 
ATOM   530  C CZ    . ARG A 1 71  ? -15.124 -14.946 30.556  1.00 26.73 ? 71   ARG A CZ    1 
ATOM   531  N NH1   . ARG A 1 71  ? -14.591 -14.862 31.764  1.00 28.45 ? 71   ARG A NH1   1 
ATOM   532  N NH2   . ARG A 1 71  ? -15.413 -16.126 30.055  1.00 26.07 ? 71   ARG A NH2   1 
ATOM   533  N N     . ILE A 1 72  ? -11.167 -8.389  30.703  1.00 21.28 ? 72   ILE A N     1 
ATOM   534  C CA    . ILE A 1 72  ? -10.777 -7.082  31.309  1.00 22.74 ? 72   ILE A CA    1 
ATOM   535  C C     . ILE A 1 72  ? -10.058 -6.262  30.239  1.00 22.77 ? 72   ILE A C     1 
ATOM   536  O O     . ILE A 1 72  ? -10.399 -5.096  30.068  1.00 21.68 ? 72   ILE A O     1 
ATOM   537  C CB    . ILE A 1 72  ? -9.910  -7.291  32.552  1.00 24.39 ? 72   ILE A CB    1 
ATOM   538  C CG1   . ILE A 1 72  ? -10.731 -7.898  33.686  1.00 22.90 ? 72   ILE A CG1   1 
ATOM   539  C CG2   . ILE A 1 72  ? -9.209  -6.002  32.976  1.00 24.43 ? 72   ILE A CG2   1 
ATOM   540  C CD1   . ILE A 1 72  ? -9.859  -8.534  34.729  1.00 24.88 ? 72   ILE A CD1   1 
ATOM   541  N N     . ALA A 1 73  ? -9.130  -6.887  29.516  1.00 22.50 ? 73   ALA A N     1 
ATOM   542  C CA    . ALA A 1 73  ? -8.389  -6.242  28.413  1.00 20.97 ? 73   ALA A CA    1 
ATOM   543  C C     . ALA A 1 73  ? -9.380  -5.692  27.386  1.00 19.50 ? 73   ALA A C     1 
ATOM   544  O O     . ALA A 1 73  ? -9.156  -4.575  26.894  1.00 23.60 ? 73   ALA A O     1 
ATOM   545  C CB    . ALA A 1 73  ? -7.407  -7.231  27.820  1.00 19.89 ? 73   ALA A CB    1 
ATOM   546  N N     . ASN A 1 74  ? -10.432 -6.438  27.065  1.00 21.38 ? 74   ASN A N     1 
ATOM   547  C CA    . ASN A 1 74  ? -11.460 -6.005  26.086  1.00 21.81 ? 74   ASN A CA    1 
ATOM   548  C C     . ASN A 1 74  ? -12.191 -4.773  26.633  1.00 25.58 ? 74   ASN A C     1 
ATOM   549  O O     . ASN A 1 74  ? -12.455 -3.828  25.860  1.00 23.43 ? 74   ASN A O     1 
ATOM   550  C CB    . ASN A 1 74  ? -12.439 -7.122  25.732  1.00 22.71 ? 74   ASN A CB    1 
ATOM   551  C CG    . ASN A 1 74  ? -11.923 -8.035  24.638  1.00 21.28 ? 74   ASN A CG    1 
ATOM   552  O OD1   . ASN A 1 74  ? -12.236 -7.834  23.469  1.00 22.90 ? 74   ASN A OD1   1 
ATOM   553  N ND2   . ASN A 1 74  ? -11.137 -9.030  25.003  1.00 21.08 ? 74   ASN A ND2   1 
ATOM   554  N N     . ARG A 1 75  ? -12.479 -4.753  27.934  1.00 24.75 ? 75   ARG A N     1 
ATOM   555  C CA    . ARG A 1 75  ? -13.240 -3.630  28.524  1.00 26.99 ? 75   ARG A CA    1 
ATOM   556  C C     . ARG A 1 75  ? -12.415 -2.353  28.369  1.00 24.73 ? 75   ARG A C     1 
ATOM   557  O O     . ARG A 1 75  ? -13.002 -1.339  28.045  1.00 23.49 ? 75   ARG A O     1 
ATOM   558  C CB    . ARG A 1 75  ? -13.609 -3.906  29.990  1.00 27.85 ? 75   ARG A CB    1 
ATOM   559  C CG    . ARG A 1 75  ? -14.103 -2.666  30.734  1.00 30.43 ? 75   ARG A CG    1 
ATOM   560  C CD    . ARG A 1 75  ? -14.598 -3.015  32.129  1.00 31.95 ? 75   ARG A CD    1 
ATOM   561  N NE    . ARG A 1 75  ? -15.914 -3.632  32.093  1.00 33.07 ? 75   ARG A NE    1 
ATOM   562  C CZ    . ARG A 1 75  ? -17.067 -2.961  32.020  1.00 33.07 ? 75   ARG A CZ    1 
ATOM   563  N NH1   . ARG A 1 75  ? -17.078 -1.645  31.979  1.00 35.08 ? 75   ARG A NH1   1 
ATOM   564  N NH2   . ARG A 1 75  ? -18.208 -3.611  31.975  1.00 35.11 ? 75   ARG A NH2   1 
ATOM   565  N N     . TYR A 1 76  ? -11.107 -2.397  28.624  1.00 22.73 ? 76   TYR A N     1 
ATOM   566  C CA    . TYR A 1 76  ? -10.263 -1.175  28.779  1.00 23.97 ? 76   TYR A CA    1 
ATOM   567  C C     . TYR A 1 76  ? -9.358  -0.918  27.567  1.00 23.65 ? 76   TYR A C     1 
ATOM   568  O O     . TYR A 1 76  ? -8.627  0.059   27.614  1.00 28.67 ? 76   TYR A O     1 
ATOM   569  C CB    . TYR A 1 76  ? -9.461  -1.266  30.066  1.00 21.72 ? 76   TYR A CB    1 
ATOM   570  C CG    . TYR A 1 76  ? -10.355 -1.209  31.279  1.00 21.85 ? 76   TYR A CG    1 
ATOM   571  C CD1   . TYR A 1 76  ? -11.048 -0.047  31.578  1.00 28.49 ? 76   TYR A CD1   1 
ATOM   572  C CD2   . TYR A 1 76  ? -10.511 -2.304  32.112  1.00 24.55 ? 76   TYR A CD2   1 
ATOM   573  C CE1   . TYR A 1 76  ? -11.866 0.029   32.698  1.00 30.03 ? 76   TYR A CE1   1 
ATOM   574  C CE2   . TYR A 1 76  ? -11.349 -2.257  33.219  1.00 25.73 ? 76   TYR A CE2   1 
ATOM   575  C CZ    . TYR A 1 76  ? -11.981 -1.068  33.537  1.00 27.66 ? 76   TYR A CZ    1 
ATOM   576  O OH    . TYR A 1 76  ? -12.816 -1.032  34.611  1.00 28.68 ? 76   TYR A OH    1 
ATOM   577  N N     . GLY A 1 77  ? -9.482  -1.741  26.525  1.00 25.75 ? 77   GLY A N     1 
ATOM   578  C CA    . GLY A 1 77  ? -8.655  -1.685  25.306  1.00 24.44 ? 77   GLY A CA    1 
ATOM   579  C C     . GLY A 1 77  ? -7.184  -1.904  25.605  1.00 23.87 ? 77   GLY A C     1 
ATOM   580  O O     . GLY A 1 77  ? -6.327  -1.257  24.948  1.00 25.26 ? 77   GLY A O     1 
ATOM   581  N N     . ILE A 1 78  ? -6.872  -2.800  26.540  1.00 21.89 ? 78   ILE A N     1 
ATOM   582  C CA    . ILE A 1 78  ? -5.468  -3.112  26.916  1.00 22.60 ? 78   ILE A CA    1 
ATOM   583  C C     . ILE A 1 78  ? -4.916  -4.108  25.896  1.00 21.63 ? 78   ILE A C     1 
ATOM   584  O O     . ILE A 1 78  ? -5.415  -5.224  25.795  1.00 19.37 ? 78   ILE A O     1 
ATOM   585  C CB    . ILE A 1 78  ? -5.328  -3.679  28.323  1.00 21.92 ? 78   ILE A CB    1 
ATOM   586  C CG1   . ILE A 1 78  ? -6.035  -2.815  29.379  1.00 24.39 ? 78   ILE A CG1   1 
ATOM   587  C CG2   . ILE A 1 78  ? -3.858  -3.879  28.634  1.00 22.67 ? 78   ILE A CG2   1 
ATOM   588  C CD1   . ILE A 1 78  ? -5.514  -1.401  29.515  1.00 25.24 ? 78   ILE A CD1   1 
ATOM   589  N N     . PRO A 1 79  ? -3.835  -3.751  25.168  1.00 20.93 ? 79   PRO A N     1 
ATOM   590  C CA    . PRO A 1 79  ? -3.184  -4.716  24.291  1.00 22.40 ? 79   PRO A CA    1 
ATOM   591  C C     . PRO A 1 79  ? -2.422  -5.734  25.144  1.00 23.74 ? 79   PRO A C     1 
ATOM   592  O O     . PRO A 1 79  ? -1.740  -5.334  26.110  1.00 24.34 ? 79   PRO A O     1 
ATOM   593  C CB    . PRO A 1 79  ? -2.285  -3.840  23.414  1.00 23.82 ? 79   PRO A CB    1 
ATOM   594  C CG    . PRO A 1 79  ? -1.937  -2.675  24.296  1.00 23.90 ? 79   PRO A CG    1 
ATOM   595  C CD    . PRO A 1 79  ? -3.194  -2.431  25.123  1.00 22.17 ? 79   PRO A CD    1 
ATOM   596  N N     . LEU A 1 80  ? -2.568  -7.019  24.840  1.00 21.71 ? 80   LEU A N     1 
ATOM   597  C CA    . LEU A 1 80  ? -1.845  -8.038  25.619  1.00 26.40 ? 80   LEU A CA    1 
ATOM   598  C C     . LEU A 1 80  ? -1.015  -8.966  24.730  1.00 24.35 ? 80   LEU A C     1 
ATOM   599  O O     . LEU A 1 80  ? -1.520  -9.626  23.814  1.00 22.70 ? 80   LEU A O     1 
ATOM   600  C CB    . LEU A 1 80  ? -2.738  -8.738  26.636  1.00 35.01 ? 80   LEU A CB    1 
ATOM   601  C CG    . LEU A 1 80  ? -4.031  -9.354  26.182  1.00 39.56 ? 80   LEU A CG    1 
ATOM   602  C CD1   . LEU A 1 80  ? -3.746  -10.723 25.614  1.00 49.64 ? 80   LEU A CD1   1 
ATOM   603  C CD2   . LEU A 1 80  ? -5.005  -9.471  27.339  1.00 31.13 ? 80   LEU A CD2   1 
ATOM   604  N N     . SER A 1 81  ? 0.264   -8.973  25.033  1.00 21.05 ? 81   SER A N     1 
ATOM   605  C CA    . SER A 1 81  ? 1.241   -9.869  24.385  1.00 22.67 ? 81   SER A CA    1 
ATOM   606  C C     . SER A 1 81  ? 1.273   -11.150 25.212  1.00 21.98 ? 81   SER A C     1 
ATOM   607  O O     . SER A 1 81  ? 0.674   -11.175 26.306  1.00 20.85 ? 81   SER A O     1 
ATOM   608  C CB    . SER A 1 81  ? 2.554   -9.209  24.263  1.00 20.20 ? 81   SER A CB    1 
ATOM   609  O OG    . SER A 1 81  ? 3.081   -8.966  25.548  1.00 23.20 ? 81   SER A OG    1 
ATOM   610  N N     . VAL A 1 82  ? 1.938   -12.177 24.719  1.00 22.96 ? 82   VAL A N     1 
ATOM   611  C CA    . VAL A 1 82  ? 1.835   -13.532 25.323  1.00 22.15 ? 82   VAL A CA    1 
ATOM   612  C C     . VAL A 1 82  ? 3.209   -14.185 25.314  1.00 24.00 ? 82   VAL A C     1 
ATOM   613  O O     . VAL A 1 82  ? 3.927   -14.113 24.283  1.00 24.57 ? 82   VAL A O     1 
ATOM   614  C CB    . VAL A 1 82  ? 0.803   -14.383 24.562  1.00 22.15 ? 82   VAL A CB    1 
ATOM   615  C CG1   . VAL A 1 82  ? 0.411   -15.579 25.373  1.00 24.47 ? 82   VAL A CG1   1 
ATOM   616  C CG2   . VAL A 1 82  ? -0.423  -13.575 24.195  1.00 25.26 ? 82   VAL A CG2   1 
ATOM   617  N N     . ILE A 1 83  ? 3.566   -14.783 26.443  1.00 21.80 ? 83   ILE A N     1 
ATOM   618  C CA    . ILE A 1 83  ? 4.730   -15.687 26.542  1.00 21.28 ? 83   ILE A CA    1 
ATOM   619  C C     . ILE A 1 83  ? 4.255   -16.977 27.225  1.00 20.99 ? 83   ILE A C     1 
ATOM   620  O O     . ILE A 1 83  ? 3.203   -16.974 27.892  1.00 20.36 ? 83   ILE A O     1 
ATOM   621  C CB    . ILE A 1 83  ? 5.917   -15.020 27.279  1.00 20.40 ? 83   ILE A CB    1 
ATOM   622  C CG1   . ILE A 1 83  ? 5.596   -14.787 28.761  1.00 19.85 ? 83   ILE A CG1   1 
ATOM   623  C CG2   . ILE A 1 83  ? 6.335   -13.730 26.581  1.00 23.45 ? 83   ILE A CG2   1 
ATOM   624  C CD1   . ILE A 1 83  ? 6.786   -14.506 29.604  1.00 21.29 ? 83   ILE A CD1   1 
ATOM   625  N N     . SER A 1 84  ? 4.969   -18.046 26.969  1.00 21.86 ? 84   SER A N     1 
ATOM   626  C CA    . SER A 1 84  ? 5.014   -19.277 27.791  1.00 22.06 ? 84   SER A CA    1 
ATOM   627  C C     . SER A 1 84  ? 6.155   -19.124 28.782  1.00 23.30 ? 84   SER A C     1 
ATOM   628  O O     . SER A 1 84  ? 5.877   -18.670 29.919  1.00 24.17 ? 84   SER A O     1 
ATOM   629  C CB    . SER A 1 84  ? 5.143   -20.474 26.907  1.00 21.43 ? 84   SER A CB    1 
ATOM   630  O OG    . SER A 1 84  ? 3.950   -20.625 26.151  1.00 20.76 ? 84   SER A OG    1 
ATOM   631  N N     . THR A 1 85  ? 7.400   -19.337 28.351  1.00 24.40 ? 85   THR A N     1 
ATOM   632  C CA    . THR A 1 85  ? 8.617   -19.089 29.166  1.00 22.01 ? 85   THR A CA    1 
ATOM   633  C C     . THR A 1 85  ? 9.263   -17.757 28.748  1.00 24.99 ? 85   THR A C     1 
ATOM   634  O O     . THR A 1 85  ? 10.049  -17.213 29.536  1.00 23.78 ? 85   THR A O     1 
ATOM   635  C CB    . THR A 1 85  ? 9.545   -20.305 29.125  1.00 25.13 ? 85   THR A CB    1 
ATOM   636  O OG1   . THR A 1 85  ? 9.667   -20.765 27.784  1.00 25.52 ? 85   THR A OG1   1 
ATOM   637  C CG2   . THR A 1 85  ? 9.019   -21.456 29.950  1.00 23.46 ? 85   THR A CG2   1 
ATOM   638  N N     . GLY A 1 86  ? 8.949   -17.241 27.561  1.00 22.85 ? 86   GLY A N     1 
ATOM   639  C CA    . GLY A 1 86  ? 9.469   -15.950 27.084  1.00 25.42 ? 86   GLY A CA    1 
ATOM   640  C C     . GLY A 1 86  ? 10.976  -15.981 26.834  1.00 24.47 ? 86   GLY A C     1 
ATOM   641  O O     . GLY A 1 86  ? 11.644  -14.959 27.026  1.00 27.25 ? 86   GLY A O     1 
ATOM   642  N N     . ARG A 1 87  ? 11.511  -17.115 26.405  1.00 23.55 ? 87   ARG A N     1 
ATOM   643  C CA    . ARG A 1 87  ? 12.960  -17.236 26.113  1.00 25.65 ? 87   ARG A CA    1 
ATOM   644  C C     . ARG A 1 87  ? 13.164  -17.177 24.597  1.00 23.62 ? 87   ARG A C     1 
ATOM   645  O O     . ARG A 1 87  ? 14.114  -17.831 24.151  1.00 23.14 ? 87   ARG A O     1 
ATOM   646  C CB    . ARG A 1 87  ? 13.548  -18.528 26.685  1.00 27.68 ? 87   ARG A CB    1 
ATOM   647  C CG    . ARG A 1 87  ? 13.185  -18.801 28.136  1.00 32.94 ? 87   ARG A CG    1 
ATOM   648  C CD    . ARG A 1 87  ? 13.412  -17.620 29.047  1.00 36.19 ? 87   ARG A CD    1 
ATOM   649  N NE    . ARG A 1 87  ? 14.833  -17.317 29.239  1.00 39.70 ? 87   ARG A NE    1 
ATOM   650  C CZ    . ARG A 1 87  ? 15.640  -17.867 30.153  1.00 38.90 ? 87   ARG A CZ    1 
ATOM   651  N NH1   . ARG A 1 87  ? 15.210  -18.806 30.973  1.00 37.36 ? 87   ARG A NH1   1 
ATOM   652  N NH2   . ARG A 1 87  ? 16.896  -17.470 30.235  1.00 39.32 ? 87   ARG A NH2   1 
ATOM   653  N N     . ASN A 1 88  ? 12.345  -16.389 23.873  1.00 22.88 ? 88   ASN A N     1 
ATOM   654  C CA    . ASN A 1 88  ? 12.374  -16.325 22.380  1.00 21.53 ? 88   ASN A CA    1 
ATOM   655  C C     . ASN A 1 88  ? 13.543  -15.438 21.933  1.00 20.87 ? 88   ASN A C     1 
ATOM   656  O O     . ASN A 1 88  ? 13.334  -14.517 21.138  1.00 18.44 ? 88   ASN A O     1 
ATOM   657  C CB    . ASN A 1 88  ? 11.025  -15.871 21.831  1.00 20.44 ? 88   ASN A CB    1 
ATOM   658  C CG    . ASN A 1 88  ? 10.756  -16.387 20.434  1.00 19.32 ? 88   ASN A CG    1 
ATOM   659  O OD1   . ASN A 1 88  ? 11.366  -17.361 20.003  1.00 21.97 ? 88   ASN A OD1   1 
ATOM   660  N ND2   . ASN A 1 88  ? 9.850   -15.749 19.731  1.00 19.65 ? 88   ASN A ND2   1 
ATOM   661  N N     . ASN A 1 89  ? 14.725  -15.735 22.434  1.00 22.98 ? 89   ASN A N     1 
ATOM   662  C CA    . ASN A 1 89  ? 15.957  -14.941 22.232  1.00 26.36 ? 89   ASN A CA    1 
ATOM   663  C C     . ASN A 1 89  ? 16.383  -15.092 20.774  1.00 23.69 ? 89   ASN A C     1 
ATOM   664  O O     . ASN A 1 89  ? 16.359  -16.217 20.262  1.00 25.31 ? 89   ASN A O     1 
ATOM   665  C CB    . ASN A 1 89  ? 17.044  -15.387 23.199  1.00 25.53 ? 89   ASN A CB    1 
ATOM   666  C CG    . ASN A 1 89  ? 16.641  -15.114 24.630  1.00 24.11 ? 89   ASN A CG    1 
ATOM   667  O OD1   . ASN A 1 89  ? 15.730  -14.330 24.887  1.00 24.37 ? 89   ASN A OD1   1 
ATOM   668  N ND2   . ASN A 1 89  ? 17.338  -15.741 25.563  1.00 26.63 ? 89   ASN A ND2   1 
ATOM   669  N N     . GLY A 1 90  ? 16.689  -13.976 20.134  1.00 24.92 ? 90   GLY A N     1 
ATOM   670  C CA    . GLY A 1 90  ? 16.908  -13.877 18.689  1.00 25.06 ? 90   GLY A CA    1 
ATOM   671  C C     . GLY A 1 90  ? 15.688  -13.317 17.999  1.00 23.97 ? 90   GLY A C     1 
ATOM   672  O O     . GLY A 1 90  ? 15.818  -12.865 16.827  1.00 20.15 ? 90   GLY A O     1 
ATOM   673  N N     . TYR A 1 91  ? 14.522  -13.375 18.664  1.00 22.44 ? 91   TYR A N     1 
ATOM   674  C CA    . TYR A 1 91  ? 13.231  -12.924 18.095  1.00 22.64 ? 91   TYR A CA    1 
ATOM   675  C C     . TYR A 1 91  ? 12.527  -11.887 18.979  1.00 19.30 ? 91   TYR A C     1 
ATOM   676  O O     . TYR A 1 91  ? 11.404  -11.463 18.609  1.00 20.89 ? 91   TYR A O     1 
ATOM   677  C CB    . TYR A 1 91  ? 12.336  -14.134 17.825  1.00 23.43 ? 91   TYR A CB    1 
ATOM   678  C CG    . TYR A 1 91  ? 12.968  -15.113 16.874  1.00 23.22 ? 91   TYR A CG    1 
ATOM   679  C CD1   . TYR A 1 91  ? 13.326  -14.721 15.591  1.00 24.82 ? 91   TYR A CD1   1 
ATOM   680  C CD2   . TYR A 1 91  ? 13.200  -16.417 17.248  1.00 23.43 ? 91   TYR A CD2   1 
ATOM   681  C CE1   . TYR A 1 91  ? 13.900  -15.613 14.700  1.00 25.55 ? 91   TYR A CE1   1 
ATOM   682  C CE2   . TYR A 1 91  ? 13.746  -17.333 16.359  1.00 26.25 ? 91   TYR A CE2   1 
ATOM   683  C CZ    . TYR A 1 91  ? 14.131  -16.916 15.096  1.00 27.45 ? 91   TYR A CZ    1 
ATOM   684  O OH    . TYR A 1 91  ? 14.673  -17.838 14.246  1.00 29.21 ? 91   TYR A OH    1 
ATOM   685  N N     . GLY A 1 92  ? 13.135  -11.498 20.086  1.00 20.37 ? 92   GLY A N     1 
ATOM   686  C CA    . GLY A 1 92  ? 12.572  -10.484 20.952  1.00 22.03 ? 92   GLY A CA    1 
ATOM   687  C C     . GLY A 1 92  ? 12.490  -10.853 22.413  1.00 21.36 ? 92   GLY A C     1 
ATOM   688  O O     . GLY A 1 92  ? 12.104  -10.051 23.212  1.00 22.83 ? 92   GLY A O     1 
ATOM   689  N N     . GLY A 1 93  ? 12.906  -12.048 22.753  1.00 22.60 ? 93   GLY A N     1 
ATOM   690  C CA    . GLY A 1 93  ? 12.746  -12.517 24.108  1.00 24.56 ? 93   GLY A CA    1 
ATOM   691  C C     . GLY A 1 93  ? 11.293  -12.499 24.541  1.00 23.40 ? 93   GLY A C     1 
ATOM   692  O O     . GLY A 1 93  ? 10.422  -12.934 23.819  1.00 24.49 ? 93   GLY A O     1 
ATOM   693  N N     . SER A 1 94  ? 11.029  -11.975 25.727  1.00 26.31 ? 94   SER A N     1 
ATOM   694  C CA    . SER A 1 94  ? 9.673   -11.869 26.235  1.00 24.85 ? 94   SER A CA    1 
ATOM   695  C C     . SER A 1 94  ? 9.074   -10.502 25.895  1.00 24.49 ? 94   SER A C     1 
ATOM   696  O O     . SER A 1 94  ? 8.017   -10.154 26.355  1.00 21.87 ? 94   SER A O     1 
ATOM   697  C CB    . SER A 1 94  ? 9.669   -12.097 27.744  1.00 29.14 ? 94   SER A CB    1 
ATOM   698  O OG    . SER A 1 94  ? 10.848  -12.659 28.224  1.00 32.85 ? 94   SER A OG    1 
ATOM   699  N N     . ALA A 1 95  ? 9.778   -9.731  25.069  1.00 22.68 ? 95   ALA A N     1 
ATOM   700  C CA    . ALA A 1 95  ? 9.322   -8.415  24.744  1.00 22.94 ? 95   ALA A CA    1 
ATOM   701  C C     . ALA A 1 95  ? 8.109   -8.348  23.761  1.00 24.23 ? 95   ALA A C     1 
ATOM   702  O O     . ALA A 1 95  ? 8.101   -9.069  22.802  1.00 23.60 ? 95   ALA A O     1 
ATOM   703  C CB    . ALA A 1 95  ? 10.438  -7.527  24.265  1.00 24.68 ? 95   ALA A CB    1 
ATOM   704  N N     . PRO A 1 96  ? 7.109   -7.440  24.008  1.00 22.60 ? 96   PRO A N     1 
ATOM   705  C CA    . PRO A 1 96  ? 5.990   -7.382  23.075  1.00 21.50 ? 96   PRO A CA    1 
ATOM   706  C C     . PRO A 1 96  ? 6.365   -6.688  21.758  1.00 21.71 ? 96   PRO A C     1 
ATOM   707  O O     . PRO A 1 96  ? 7.125   -5.730  21.785  1.00 21.16 ? 96   PRO A O     1 
ATOM   708  C CB    . PRO A 1 96  ? 4.950   -6.568  23.855  1.00 21.59 ? 96   PRO A CB    1 
ATOM   709  C CG    . PRO A 1 96  ? 5.809   -5.626  24.666  1.00 22.72 ? 96   PRO A CG    1 
ATOM   710  C CD    . PRO A 1 96  ? 6.953   -6.498  25.125  1.00 22.45 ? 96   PRO A CD    1 
ATOM   711  N N     . ARG A 1 97  ? 5.795   -7.139  20.641  1.00 20.67 ? 97   ARG A N     1 
ATOM   712  C CA    . ARG A 1 97  ? 5.905   -6.389  19.364  1.00 21.67 ? 97   ARG A CA    1 
ATOM   713  C C     . ARG A 1 97  ? 5.390   -4.965  19.580  1.00 23.75 ? 97   ARG A C     1 
ATOM   714  O O     . ARG A 1 97  ? 6.079   -4.007  19.138  1.00 19.79 ? 97   ARG A O     1 
ATOM   715  C CB    . ARG A 1 97  ? 5.145   -7.072  18.230  1.00 21.19 ? 97   ARG A CB    1 
ATOM   716  C CG    . ARG A 1 97  ? 4.991   -6.189  16.999  1.00 20.34 ? 97   ARG A CG    1 
ATOM   717  C CD    . ARG A 1 97  ? 6.353   -5.930  16.404  1.00 24.13 ? 97   ARG A CD    1 
ATOM   718  N NE    . ARG A 1 97  ? 6.236   -5.037  15.259  1.00 23.22 ? 97   ARG A NE    1 
ATOM   719  C CZ    . ARG A 1 97  ? 6.292   -3.723  15.308  1.00 24.23 ? 97   ARG A CZ    1 
ATOM   720  N NH1   . ARG A 1 97  ? 6.405   -3.087  16.473  1.00 25.47 ? 97   ARG A NH1   1 
ATOM   721  N NH2   . ARG A 1 97  ? 6.145   -3.035  14.183  1.00 26.62 ? 97   ARG A NH2   1 
ATOM   722  N N     . LEU A 1 98  ? 4.202   -4.809  20.197  1.00 23.32 ? 98   LEU A N     1 
ATOM   723  C CA    . LEU A 1 98  ? 3.614   -3.473  20.429  1.00 22.82 ? 98   LEU A CA    1 
ATOM   724  C C     . LEU A 1 98  ? 4.181   -2.917  21.734  1.00 24.46 ? 98   LEU A C     1 
ATOM   725  O O     . LEU A 1 98  ? 3.765   -3.386  22.822  1.00 24.64 ? 98   LEU A O     1 
ATOM   726  C CB    . LEU A 1 98  ? 2.092   -3.529  20.482  1.00 24.60 ? 98   LEU A CB    1 
ATOM   727  C CG    . LEU A 1 98  ? 1.421   -2.185  20.732  1.00 25.41 ? 98   LEU A CG    1 
ATOM   728  C CD1   . LEU A 1 98  ? 1.808   -1.173  19.669  1.00 25.67 ? 98   LEU A CD1   1 
ATOM   729  C CD2   . LEU A 1 98  ? -0.080  -2.326  20.799  1.00 27.28 ? 98   LEU A CD2   1 
ATOM   730  N N     . SER A 1 99  ? 5.075   -1.947  21.639  1.00 22.96 ? 99   SER A N     1 
ATOM   731  C CA    . SER A 1 99  ? 5.726   -1.358  22.838  1.00 24.49 ? 99   SER A CA    1 
ATOM   732  C C     . SER A 1 99  ? 4.632   -0.795  23.766  1.00 23.84 ? 99   SER A C     1 
ATOM   733  O O     . SER A 1 99  ? 3.690   -0.147  23.250  1.00 23.37 ? 99   SER A O     1 
ATOM   734  C CB    . SER A 1 99  ? 6.706   -0.303  22.449  1.00 25.77 ? 99   SER A CB    1 
ATOM   735  O OG    . SER A 1 99  ? 7.446   0.031   23.601  1.00 28.41 ? 99   SER A OG    1 
ATOM   736  N N     . GLY A 1 100 ? 4.713   -1.102  25.061  1.00 26.46 ? 100  GLY A N     1 
ATOM   737  C CA    . GLY A 1 100 ? 3.687   -0.702  26.043  1.00 26.76 ? 100  GLY A CA    1 
ATOM   738  C C     . GLY A 1 100 ? 2.609   -1.757  26.252  1.00 26.49 ? 100  GLY A C     1 
ATOM   739  O O     . GLY A 1 100 ? 1.749   -1.537  27.113  1.00 26.42 ? 100  GLY A O     1 
ATOM   740  N N     . ALA A 1 101 ? 2.610   -2.867  25.510  1.00 22.62 ? 101  ALA A N     1 
ATOM   741  C CA    . ALA A 1 101 ? 1.608   -3.933  25.723  1.00 21.64 ? 101  ALA A CA    1 
ATOM   742  C C     . ALA A 1 101 ? 1.796   -4.482  27.126  1.00 20.85 ? 101  ALA A C     1 
ATOM   743  O O     . ALA A 1 101 ? 2.905   -4.338  27.707  1.00 22.56 ? 101  ALA A O     1 
ATOM   744  C CB    . ALA A 1 101 ? 1.708   -5.018  24.680  1.00 22.37 ? 101  ALA A CB    1 
ATOM   745  N N     . VAL A 1 102 ? 0.736   -5.062  27.658  1.00 21.70 ? 102  VAL A N     1 
ATOM   746  C CA    . VAL A 1 102 ? 0.786   -5.873  28.899  1.00 22.08 ? 102  VAL A CA    1 
ATOM   747  C C     . VAL A 1 102 ? 1.100   -7.318  28.514  1.00 21.22 ? 102  VAL A C     1 
ATOM   748  O O     . VAL A 1 102 ? 0.359   -7.896  27.684  1.00 26.22 ? 102  VAL A O     1 
ATOM   749  C CB    . VAL A 1 102 ? -0.544  -5.765  29.660  1.00 22.14 ? 102  VAL A CB    1 
ATOM   750  C CG1   . VAL A 1 102 ? -0.570  -6.734  30.840  1.00 24.95 ? 102  VAL A CG1   1 
ATOM   751  C CG2   . VAL A 1 102 ? -0.815  -4.334  30.094  1.00 23.50 ? 102  VAL A CG2   1 
ATOM   752  N N     . VAL A 1 103 ? 2.130   -7.887  29.130  1.00 20.71 ? 103  VAL A N     1 
ATOM   753  C CA    . VAL A 1 103 ? 2.589   -9.270  28.877  1.00 21.77 ? 103  VAL A CA    1 
ATOM   754  C C     . VAL A 1 103 ? 1.707   -10.200 29.702  1.00 23.64 ? 103  VAL A C     1 
ATOM   755  O O     . VAL A 1 103 ? 1.683   -10.059 30.948  1.00 20.81 ? 103  VAL A O     1 
ATOM   756  C CB    . VAL A 1 103 ? 4.080   -9.465  29.209  1.00 22.70 ? 103  VAL A CB    1 
ATOM   757  C CG1   . VAL A 1 103 ? 4.503   -10.911 28.965  1.00 23.94 ? 103  VAL A CG1   1 
ATOM   758  C CG2   . VAL A 1 103 ? 4.972   -8.511  28.426  1.00 24.79 ? 103  VAL A CG2   1 
ATOM   759  N N     . VAL A 1 104 ? 1.063   -11.147 29.050  1.00 20.78 ? 104  VAL A N     1 
ATOM   760  C CA    . VAL A 1 104 ? 0.424   -12.302 29.741  1.00 21.18 ? 104  VAL A CA    1 
ATOM   761  C C     . VAL A 1 104 ? 1.479   -13.401 29.858  1.00 20.84 ? 104  VAL A C     1 
ATOM   762  O O     . VAL A 1 104 ? 1.893   -14.031 28.828  1.00 21.12 ? 104  VAL A O     1 
ATOM   763  C CB    . VAL A 1 104 ? -0.857  -12.759 29.033  1.00 21.23 ? 104  VAL A CB    1 
ATOM   764  C CG1   . VAL A 1 104 ? -1.509  -13.917 29.772  1.00 22.32 ? 104  VAL A CG1   1 
ATOM   765  C CG2   . VAL A 1 104 ? -1.833  -11.620 28.854  1.00 21.45 ? 104  VAL A CG2   1 
ATOM   766  N N     . ASN A 1 105 ? 1.973   -13.600 31.075  1.00 19.66 ? 105  ASN A N     1 
ATOM   767  C CA    . ASN A 1 105 ? 2.948   -14.650 31.437  1.00 20.24 ? 105  ASN A CA    1 
ATOM   768  C C     . ASN A 1 105 ? 2.154   -15.925 31.731  1.00 21.72 ? 105  ASN A C     1 
ATOM   769  O O     . ASN A 1 105 ? 1.775   -16.145 32.894  1.00 20.02 ? 105  ASN A O     1 
ATOM   770  C CB    . ASN A 1 105 ? 3.847   -14.195 32.591  1.00 20.40 ? 105  ASN A CB    1 
ATOM   771  C CG    . ASN A 1 105 ? 4.937   -15.183 32.939  1.00 20.66 ? 105  ASN A CG    1 
ATOM   772  O OD1   . ASN A 1 105 ? 4.910   -16.339 32.528  1.00 26.21 ? 105  ASN A OD1   1 
ATOM   773  N ND2   . ASN A 1 105 ? 5.880   -14.746 33.751  1.00 24.91 ? 105  ASN A ND2   1 
ATOM   774  N N     . THR A 1 106 ? 1.914   -16.763 30.718  1.00 21.15 ? 106  THR A N     1 
ATOM   775  C CA    . THR A 1 106 ? 1.164   -18.021 30.907  1.00 21.29 ? 106  THR A CA    1 
ATOM   776  C C     . THR A 1 106 ? 2.011   -19.041 31.678  1.00 22.50 ? 106  THR A C     1 
ATOM   777  O O     . THR A 1 106 ? 1.395   -19.859 32.414  1.00 28.84 ? 106  THR A O     1 
ATOM   778  C CB    . THR A 1 106 ? 0.553   -18.543 29.605  1.00 21.72 ? 106  THR A CB    1 
ATOM   779  O OG1   . THR A 1 106 ? 1.604   -18.980 28.753  1.00 20.25 ? 106  THR A OG1   1 
ATOM   780  C CG2   . THR A 1 106 ? -0.343  -17.501 28.979  1.00 22.30 ? 106  THR A CG2   1 
ATOM   781  N N     . GLY A 1 107 ? 3.339   -18.996 31.582  1.00 21.17 ? 107  GLY A N     1 
ATOM   782  C CA    . GLY A 1 107 ? 4.194   -20.095 32.059  1.00 19.87 ? 107  GLY A CA    1 
ATOM   783  C C     . GLY A 1 107 ? 4.431   -20.069 33.559  1.00 22.48 ? 107  GLY A C     1 
ATOM   784  O O     . GLY A 1 107 ? 4.797   -21.118 34.131  1.00 22.87 ? 107  GLY A O     1 
ATOM   785  N N     . GLU A 1 108 ? 4.326   -18.901 34.182  1.00 22.03 ? 108  GLU A N     1 
ATOM   786  C CA    . GLU A 1 108 ? 4.744   -18.755 35.603  1.00 23.19 ? 108  GLU A CA    1 
ATOM   787  C C     . GLU A 1 108 ? 3.901   -19.700 36.454  1.00 21.25 ? 108  GLU A C     1 
ATOM   788  O O     . GLU A 1 108 ? 4.456   -20.398 37.313  1.00 22.24 ? 108  GLU A O     1 
ATOM   789  C CB    . GLU A 1 108 ? 4.541   -17.322 36.095  1.00 24.55 ? 108  GLU A CB    1 
ATOM   790  C CG    . GLU A 1 108 ? 4.992   -17.186 37.561  1.00 26.31 ? 108  GLU A CG    1 
ATOM   791  C CD    . GLU A 1 108 ? 5.103   -15.781 38.079  1.00 29.08 ? 108  GLU A CD    1 
ATOM   792  O OE1   . GLU A 1 108 ? 5.605   -15.621 39.212  1.00 31.92 ? 108  GLU A OE1   1 
ATOM   793  O OE2   . GLU A 1 108 ? 4.674   -14.861 37.371  1.00 31.13 ? 108  GLU A OE2   1 
ATOM   794  N N     . ARG A 1 109 ? 2.585   -19.694 36.259  1.00 20.82 ? 109  ARG A N     1 
ATOM   795  C CA    . ARG A 1 109 ? 1.677   -20.506 37.111  1.00 21.17 ? 109  ARG A CA    1 
ATOM   796  C C     . ARG A 1 109 ? 1.117   -21.704 36.362  1.00 22.75 ? 109  ARG A C     1 
ATOM   797  O O     . ARG A 1 109 ? 0.783   -22.697 37.022  1.00 21.81 ? 109  ARG A O     1 
ATOM   798  C CB    . ARG A 1 109 ? 0.562   -19.636 37.671  1.00 20.14 ? 109  ARG A CB    1 
ATOM   799  C CG    . ARG A 1 109 ? 1.098   -18.510 38.524  1.00 21.46 ? 109  ARG A CG    1 
ATOM   800  C CD    . ARG A 1 109 ? 0.072   -17.451 38.753  1.00 22.30 ? 109  ARG A CD    1 
ATOM   801  N NE    . ARG A 1 109 ? -0.814  -17.846 39.826  1.00 22.40 ? 109  ARG A NE    1 
ATOM   802  C CZ    . ARG A 1 109 ? -1.854  -17.139 40.248  1.00 24.43 ? 109  ARG A CZ    1 
ATOM   803  N NH1   . ARG A 1 109 ? -2.211  -16.016 39.631  1.00 22.61 ? 109  ARG A NH1   1 
ATOM   804  N NH2   . ARG A 1 109 ? -2.543  -17.578 41.297  1.00 22.73 ? 109  ARG A NH2   1 
ATOM   805  N N     . MET A 1 110 ? 0.933   -21.590 35.042  1.00 23.91 ? 110  MET A N     1 
ATOM   806  C CA    . MET A 1 110 ? 0.390   -22.740 34.272  1.00 24.07 ? 110  MET A CA    1 
ATOM   807  C C     . MET A 1 110 ? 1.576   -23.561 33.767  1.00 24.16 ? 110  MET A C     1 
ATOM   808  O O     . MET A 1 110 ? 1.972   -23.398 32.599  1.00 21.56 ? 110  MET A O     1 
ATOM   809  C CB    . MET A 1 110 ? -0.547  -22.259 33.159  1.00 24.89 ? 110  MET A CB    1 
ATOM   810  C CG    . MET A 1 110 ? -1.631  -21.305 33.715  1.00 27.70 ? 110  MET A CG    1 
ATOM   811  S SD    . MET A 1 110 ? -2.644  -20.565 32.392  1.00 27.82 ? 110  MET A SD    1 
ATOM   812  C CE    . MET A 1 110 ? -3.395  -22.050 31.804  1.00 24.61 ? 110  MET A CE    1 
ATOM   813  N N     . ASN A 1 111 ? 2.148   -24.390 34.637  1.00 20.64 ? 111  ASN A N     1 
ATOM   814  C CA    . ASN A 1 111 ? 3.450   -25.059 34.405  1.00 23.69 ? 111  ASN A CA    1 
ATOM   815  C C     . ASN A 1 111 ? 3.360   -26.564 34.675  1.00 23.69 ? 111  ASN A C     1 
ATOM   816  O O     . ASN A 1 111 ? 4.408   -27.185 34.882  1.00 22.95 ? 111  ASN A O     1 
ATOM   817  C CB    . ASN A 1 111 ? 4.537   -24.409 35.256  1.00 26.01 ? 111  ASN A CB    1 
ATOM   818  C CG    . ASN A 1 111 ? 4.225   -24.531 36.730  1.00 26.51 ? 111  ASN A CG    1 
ATOM   819  O OD1   . ASN A 1 111 ? 3.224   -25.121 37.099  1.00 25.53 ? 111  ASN A OD1   1 
ATOM   820  N ND2   . ASN A 1 111 ? 5.079   -23.967 37.565  1.00 32.00 ? 111  ASN A ND2   1 
ATOM   821  N N     . ARG A 1 112 ? 2.178   -27.149 34.560  1.00 23.18 ? 112  ARG A N     1 
ATOM   822  C CA    . ARG A 1 112 ? 1.947   -28.572 34.888  1.00 24.96 ? 112  ARG A CA    1 
ATOM   823  C C     . ARG A 1 112 ? 2.046   -29.414 33.613  1.00 24.92 ? 112  ARG A C     1 
ATOM   824  O O     . ARG A 1 112 ? 1.562   -28.990 32.541  1.00 23.17 ? 112  ARG A O     1 
ATOM   825  C CB    . ARG A 1 112 ? 0.625   -28.749 35.633  1.00 33.27 ? 112  ARG A CB    1 
ATOM   826  C CG    . ARG A 1 112 ? 0.574   -28.066 37.003  1.00 40.66 ? 112  ARG A CG    1 
ATOM   827  C CD    . ARG A 1 112 ? -0.829  -27.772 37.554  1.00 50.02 ? 112  ARG A CD    1 
ATOM   828  N NE    . ARG A 1 112 ? -1.577  -26.728 36.827  1.00 57.85 ? 112  ARG A NE    1 
ATOM   829  C CZ    . ARG A 1 112 ? -1.891  -25.489 37.248  1.00 61.78 ? 112  ARG A CZ    1 
ATOM   830  N NH1   . ARG A 1 112 ? -1.547  -25.053 38.449  1.00 66.89 ? 112  ARG A NH1   1 
ATOM   831  N NH2   . ARG A 1 112 ? -2.597  -24.685 36.465  1.00 69.09 ? 112  ARG A NH2   1 
ATOM   832  N N     . ILE A 1 113 ? 2.676   -30.569 33.760  1.00 22.92 ? 113  ILE A N     1 
ATOM   833  C CA    . ILE A 1 113 ? 2.539   -31.729 32.843  1.00 24.17 ? 113  ILE A CA    1 
ATOM   834  C C     . ILE A 1 113 ? 1.224   -32.400 33.225  1.00 25.15 ? 113  ILE A C     1 
ATOM   835  O O     . ILE A 1 113 ? 1.150   -32.957 34.321  1.00 22.56 ? 113  ILE A O     1 
ATOM   836  C CB    . ILE A 1 113 ? 3.758   -32.653 32.974  1.00 25.84 ? 113  ILE A CB    1 
ATOM   837  C CG1   . ILE A 1 113 ? 5.048   -31.889 32.672  1.00 24.26 ? 113  ILE A CG1   1 
ATOM   838  C CG2   . ILE A 1 113 ? 3.568   -33.884 32.104  1.00 24.95 ? 113  ILE A CG2   1 
ATOM   839  C CD1   . ILE A 1 113 ? 6.312   -32.650 32.977  1.00 25.02 ? 113  ILE A CD1   1 
ATOM   840  N N     . LEU A 1 114 ? 0.204   -32.259 32.389  1.00 23.84 ? 114  LEU A N     1 
ATOM   841  C CA    . LEU A 1 114 ? -1.181  -32.651 32.735  1.00 25.24 ? 114  LEU A CA    1 
ATOM   842  C C     . LEU A 1 114 ? -1.338  -34.156 32.529  1.00 27.75 ? 114  LEU A C     1 
ATOM   843  O O     . LEU A 1 114 ? -2.068  -34.809 33.313  1.00 25.53 ? 114  LEU A O     1 
ATOM   844  C CB    . LEU A 1 114 ? -2.159  -31.843 31.886  1.00 24.62 ? 114  LEU A CB    1 
ATOM   845  C CG    . LEU A 1 114 ? -2.181  -30.344 32.169  1.00 25.39 ? 114  LEU A CG    1 
ATOM   846  C CD1   . LEU A 1 114 ? -3.139  -29.655 31.220  1.00 24.90 ? 114  LEU A CD1   1 
ATOM   847  C CD2   . LEU A 1 114 ? -2.597  -30.070 33.611  1.00 27.63 ? 114  LEU A CD2   1 
ATOM   848  N N     . GLU A 1 115 ? -0.664  -34.716 31.534  1.00 26.96 ? 115  GLU A N     1 
ATOM   849  C CA    . GLU A 1 115 ? -0.847  -36.155 31.242  1.00 27.92 ? 115  GLU A CA    1 
ATOM   850  C C     . GLU A 1 115 ? 0.310   -36.621 30.371  1.00 27.59 ? 115  GLU A C     1 
ATOM   851  O O     . GLU A 1 115 ? 0.739   -35.855 29.481  1.00 22.18 ? 115  GLU A O     1 
ATOM   852  C CB    . GLU A 1 115 ? -2.247  -36.341 30.635  1.00 31.10 ? 115  GLU A CB    1 
ATOM   853  C CG    . GLU A 1 115 ? -2.376  -37.544 29.752  1.00 33.79 ? 115  GLU A CG    1 
ATOM   854  C CD    . GLU A 1 115 ? -3.766  -37.802 29.160  1.00 37.62 ? 115  GLU A CD    1 
ATOM   855  O OE1   . GLU A 1 115 ? -4.603  -36.883 29.085  1.00 40.45 ? 115  GLU A OE1   1 
ATOM   856  O OE2   . GLU A 1 115 ? -3.989  -38.936 28.717  1.00 43.02 ? 115  GLU A OE2   1 
ATOM   857  N N     . VAL A 1 116 ? 0.841   -37.802 30.671  1.00 28.21 ? 116  VAL A N     1 
ATOM   858  C CA    . VAL A 1 116 ? 1.802   -38.496 29.778  1.00 27.67 ? 116  VAL A CA    1 
ATOM   859  C C     . VAL A 1 116 ? 1.286   -39.917 29.608  1.00 29.81 ? 116  VAL A C     1 
ATOM   860  O O     . VAL A 1 116 ? 1.047   -40.545 30.623  1.00 26.26 ? 116  VAL A O     1 
ATOM   861  C CB    . VAL A 1 116 ? 3.228   -38.473 30.335  1.00 28.12 ? 116  VAL A CB    1 
ATOM   862  C CG1   . VAL A 1 116 ? 4.197   -39.276 29.478  1.00 27.81 ? 116  VAL A CG1   1 
ATOM   863  C CG2   . VAL A 1 116 ? 3.711   -37.045 30.503  1.00 30.44 ? 116  VAL A CG2   1 
ATOM   864  N N     . ASP A 1 117 ? 1.050   -40.326 28.365  1.00 24.77 ? 117  ASP A N     1 
ATOM   865  C CA    . ASP A 1 117 ? 0.678   -41.715 28.015  1.00 26.48 ? 117  ASP A CA    1 
ATOM   866  C C     . ASP A 1 117 ? 1.920   -42.358 27.408  1.00 26.05 ? 117  ASP A C     1 
ATOM   867  O O     . ASP A 1 117 ? 2.291   -42.014 26.278  1.00 22.91 ? 117  ASP A O     1 
ATOM   868  C CB    . ASP A 1 117 ? -0.520  -41.779 27.077  1.00 26.21 ? 117  ASP A CB    1 
ATOM   869  C CG    . ASP A 1 117 ? -1.117  -43.170 26.961  1.00 30.22 ? 117  ASP A CG    1 
ATOM   870  O OD1   . ASP A 1 117 ? -0.371  -44.118 26.630  1.00 28.10 ? 117  ASP A OD1   1 
ATOM   871  O OD2   . ASP A 1 117 ? -2.335  -43.292 27.204  1.00 35.52 ? 117  ASP A OD2   1 
ATOM   872  N N     . GLU A 1 118 ? 2.526   -43.288 28.131  1.00 26.12 ? 118  GLU A N     1 
ATOM   873  C CA    . GLU A 1 118 ? 3.775   -43.933 27.684  1.00 28.46 ? 118  GLU A CA    1 
ATOM   874  C C     . GLU A 1 118 ? 3.511   -44.816 26.469  1.00 29.71 ? 118  GLU A C     1 
ATOM   875  O O     . GLU A 1 118 ? 4.289   -44.697 25.488  1.00 29.49 ? 118  GLU A O     1 
ATOM   876  C CB    . GLU A 1 118 ? 4.412   -44.726 28.825  1.00 30.06 ? 118  GLU A CB    1 
ATOM   877  C CG    . GLU A 1 118 ? 5.827   -45.101 28.498  1.00 31.75 ? 118  GLU A CG    1 
ATOM   878  C CD    . GLU A 1 118 ? 6.662   -45.613 29.656  1.00 31.34 ? 118  GLU A CD    1 
ATOM   879  O OE1   . GLU A 1 118 ? 6.152   -45.694 30.777  1.00 32.63 ? 118  GLU A OE1   1 
ATOM   880  O OE2   . GLU A 1 118 ? 7.840   -45.882 29.422  1.00 34.41 ? 118  GLU A OE2   1 
ATOM   881  N N     . LYS A 1 119 ? 2.444   -45.625 26.485  1.00 30.73 ? 119  LYS A N     1 
ATOM   882  C CA    . LYS A 1 119 ? 2.187   -46.605 25.395  1.00 33.13 ? 119  LYS A CA    1 
ATOM   883  C C     . LYS A 1 119 ? 1.805   -45.860 24.112  1.00 27.95 ? 119  LYS A C     1 
ATOM   884  O O     . LYS A 1 119 ? 2.276   -46.267 23.062  1.00 28.18 ? 119  LYS A O     1 
ATOM   885  C CB    . LYS A 1 119 ? 1.099   -47.624 25.751  1.00 41.78 ? 119  LYS A CB    1 
ATOM   886  C CG    . LYS A 1 119 ? 1.459   -48.624 26.846  1.00 49.25 ? 119  LYS A CG    1 
ATOM   887  C CD    . LYS A 1 119 ? 1.646   -48.007 28.227  1.00 59.31 ? 119  LYS A CD    1 
ATOM   888  C CE    . LYS A 1 119 ? 0.464   -47.174 28.700  1.00 60.48 ? 119  LYS A CE    1 
ATOM   889  N NZ    . LYS A 1 119 ? 0.901   -46.009 29.502  1.00 58.59 ? 119  LYS A NZ    1 
ATOM   890  N N     . LEU A 1 120 ? 0.994   -44.805 24.179  1.00 24.64 ? 120  LEU A N     1 
ATOM   891  C CA    . LEU A 1 120 ? 0.508   -44.125 22.949  1.00 23.85 ? 120  LEU A CA    1 
ATOM   892  C C     . LEU A 1 120 ? 1.425   -42.940 22.618  1.00 25.43 ? 120  LEU A C     1 
ATOM   893  O O     . LEU A 1 120 ? 1.179   -42.268 21.600  1.00 25.17 ? 120  LEU A O     1 
ATOM   894  C CB    . LEU A 1 120 ? -0.930  -43.663 23.158  1.00 25.58 ? 120  LEU A CB    1 
ATOM   895  C CG    . LEU A 1 120 ? -1.931  -44.799 23.405  1.00 27.09 ? 120  LEU A CG    1 
ATOM   896  C CD1   . LEU A 1 120 ? -3.344  -44.272 23.511  1.00 27.87 ? 120  LEU A CD1   1 
ATOM   897  C CD2   . LEU A 1 120 ? -1.841  -45.833 22.312  1.00 30.54 ? 120  LEU A CD2   1 
ATOM   898  N N     . GLY A 1 121 ? 2.381   -42.658 23.492  1.00 25.32 ? 121  GLY A N     1 
ATOM   899  C CA    . GLY A 1 121 ? 3.500   -41.727 23.254  1.00 25.57 ? 121  GLY A CA    1 
ATOM   900  C C     . GLY A 1 121 ? 3.016   -40.312 23.057  1.00 23.83 ? 121  GLY A C     1 
ATOM   901  O O     . GLY A 1 121 ? 3.169   -39.772 21.948  1.00 23.80 ? 121  GLY A O     1 
ATOM   902  N N     . TYR A 1 122 ? 2.460   -39.688 24.095  1.00 23.29 ? 122  TYR A N     1 
ATOM   903  C CA    . TYR A 1 122 ? 2.127   -38.242 24.048  1.00 23.12 ? 122  TYR A CA    1 
ATOM   904  C C     . TYR A 1 122 ? 2.195   -37.640 25.435  1.00 23.80 ? 122  TYR A C     1 
ATOM   905  O O     . TYR A 1 122 ? 2.196   -38.405 26.415  1.00 22.09 ? 122  TYR A O     1 
ATOM   906  C CB    . TYR A 1 122 ? 0.747   -37.973 23.445  1.00 22.02 ? 122  TYR A CB    1 
ATOM   907  C CG    . TYR A 1 122 ? -0.426  -38.463 24.244  1.00 22.50 ? 122  TYR A CG    1 
ATOM   908  C CD1   . TYR A 1 122 ? -0.877  -37.768 25.361  1.00 24.46 ? 122  TYR A CD1   1 
ATOM   909  C CD2   . TYR A 1 122 ? -1.099  -39.615 23.874  1.00 24.66 ? 122  TYR A CD2   1 
ATOM   910  C CE1   . TYR A 1 122 ? -1.995  -38.188 26.060  1.00 26.67 ? 122  TYR A CE1   1 
ATOM   911  C CE2   . TYR A 1 122 ? -2.211  -40.056 24.567  1.00 24.82 ? 122  TYR A CE2   1 
ATOM   912  C CZ    . TYR A 1 122 ? -2.659  -39.337 25.657  1.00 25.91 ? 122  TYR A CZ    1 
ATOM   913  O OH    . TYR A 1 122 ? -3.751  -39.762 26.351  1.00 25.87 ? 122  TYR A OH    1 
ATOM   914  N N     . ALA A 1 123 ? 2.131   -36.305 25.446  1.00 21.50 ? 123  ALA A N     1 
ATOM   915  C CA    . ALA A 1 123 ? 2.034   -35.549 26.678  1.00 21.67 ? 123  ALA A CA    1 
ATOM   916  C C     . ALA A 1 123 ? 0.999   -34.441 26.470  1.00 21.53 ? 123  ALA A C     1 
ATOM   917  O O     . ALA A 1 123 ? 0.874   -33.955 25.373  1.00 21.38 ? 123  ALA A O     1 
ATOM   918  C CB    . ALA A 1 123 ? 3.342   -34.919 27.057  1.00 19.42 ? 123  ALA A CB    1 
ATOM   919  N N     . LEU A 1 124 ? 0.268   -34.061 27.506  1.00 18.98 ? 124  LEU A N     1 
ATOM   920  C CA    . LEU A 1 124 ? -0.646  -32.922 27.449  1.00 20.00 ? 124  LEU A CA    1 
ATOM   921  C C     . LEU A 1 124 ? 0.016   -31.945 28.385  1.00 21.99 ? 124  LEU A C     1 
ATOM   922  O O     . LEU A 1 124 ? 0.238   -32.253 29.535  1.00 20.45 ? 124  LEU A O     1 
ATOM   923  C CB    . LEU A 1 124 ? -2.073  -33.243 27.869  1.00 20.33 ? 124  LEU A CB    1 
ATOM   924  C CG    . LEU A 1 124 ? -3.085  -32.105 27.938  1.00 19.57 ? 124  LEU A CG    1 
ATOM   925  C CD1   . LEU A 1 124 ? -3.248  -31.387 26.614  1.00 19.23 ? 124  LEU A CD1   1 
ATOM   926  C CD2   . LEU A 1 124 ? -4.415  -32.636 28.435  1.00 22.95 ? 124  LEU A CD2   1 
ATOM   927  N N     . LEU A 1 125 ? 0.304   -30.777 27.873  1.00 19.42 ? 125  LEU A N     1 
ATOM   928  C CA    . LEU A 1 125 ? 1.086   -29.846 28.605  1.00 20.30 ? 125  LEU A CA    1 
ATOM   929  C C     . LEU A 1 125 ? 0.571   -28.452 28.758  1.00 19.94 ? 125  LEU A C     1 
ATOM   930  O O     . LEU A 1 125 ? -0.195  -27.971 27.968  1.00 18.87 ? 125  LEU A O     1 
ATOM   931  C CB    . LEU A 1 125 ? 2.444   -29.737 27.890  1.00 21.61 ? 125  LEU A CB    1 
ATOM   932  C CG    . LEU A 1 125 ? 3.258   -30.996 27.664  1.00 21.08 ? 125  LEU A CG    1 
ATOM   933  C CD1   . LEU A 1 125 ? 4.370   -30.702 26.698  1.00 24.60 ? 125  LEU A CD1   1 
ATOM   934  C CD2   . LEU A 1 125 ? 3.806   -31.528 28.970  1.00 24.53 ? 125  LEU A CD2   1 
ATOM   935  N N     . GLU A 1 126 ? 1.024   -27.813 29.816  1.00 40.31 ? 126  GLU A N     1 
ATOM   936  C CA    . GLU A 1 126 ? 0.725   -26.436 30.040  1.00 39.09 ? 126  GLU A CA    1 
ATOM   937  C C     . GLU A 1 126 ? 1.991   -25.590 29.567  1.00 24.26 ? 126  GLU A C     1 
ATOM   938  O O     . GLU A 1 126 ? 3.056   -26.149 29.463  1.00 22.31 ? 126  GLU A O     1 
ATOM   939  C CB    . GLU A 1 126 ? 0.351   -26.133 31.482  1.00 47.12 ? 126  GLU A CB    1 
ATOM   940  C CG    . GLU A 1 126 ? -1.051  -26.568 31.849  1.00 46.62 ? 126  GLU A CG    1 
ATOM   941  C CD    . GLU A 1 126 ? -1.462  -26.156 33.247  1.00 59.03 ? 126  GLU A CD    1 
ATOM   942  O OE1   . GLU A 1 126 ? -2.672  -26.050 33.490  1.00 77.80 ? 126  GLU A OE1   1 
ATOM   943  O OE2   . GLU A 1 126 ? -0.582  -25.945 34.098  1.00 41.89 ? 126  GLU A OE2   1 
ATOM   944  N N     . PRO A 1 127 ? 1.849   -24.269 29.270  1.00 20.11 ? 127  PRO A N     1 
ATOM   945  C CA    . PRO A 1 127 ? 2.957   -23.471 28.707  1.00 21.69 ? 127  PRO A CA    1 
ATOM   946  C C     . PRO A 1 127 ? 4.251   -23.362 29.507  1.00 20.56 ? 127  PRO A C     1 
ATOM   947  O O     . PRO A 1 127 ? 5.297   -23.254 28.947  1.00 22.18 ? 127  PRO A O     1 
ATOM   948  C CB    . PRO A 1 127 ? 2.311   -22.119 28.566  1.00 19.51 ? 127  PRO A CB    1 
ATOM   949  C CG    . PRO A 1 127 ? 0.886   -22.398 28.306  1.00 20.07 ? 127  PRO A CG    1 
ATOM   950  C CD    . PRO A 1 127 ? 0.587   -23.508 29.240  1.00 19.95 ? 127  PRO A CD    1 
ATOM   951  N N     . GLY A 1 128 ? 4.157   -23.442 30.793  1.00 20.57 ? 128  GLY A N     1 
ATOM   952  C CA    . GLY A 1 128 ? 5.294   -23.302 31.710  1.00 21.19 ? 128  GLY A CA    1 
ATOM   953  C C     . GLY A 1 128 ? 6.228   -24.510 31.742  1.00 22.45 ? 128  GLY A C     1 
ATOM   954  O O     . GLY A 1 128 ? 7.347   -24.384 32.297  1.00 19.94 ? 128  GLY A O     1 
ATOM   955  N N     . VAL A 1 129 ? 5.835   -25.651 31.171  1.00 21.19 ? 129  VAL A N     1 
ATOM   956  C CA    . VAL A 1 129 ? 6.719   -26.846 31.120  1.00 21.17 ? 129  VAL A CA    1 
ATOM   957  C C     . VAL A 1 129 ? 7.898   -26.572 30.177  1.00 21.25 ? 129  VAL A C     1 
ATOM   958  O O     . VAL A 1 129 ? 7.661   -26.419 28.973  1.00 20.20 ? 129  VAL A O     1 
ATOM   959  C CB    . VAL A 1 129 ? 5.963   -28.107 30.662  1.00 19.32 ? 129  VAL A CB    1 
ATOM   960  C CG1   . VAL A 1 129 ? 6.877   -29.301 30.696  1.00 18.97 ? 129  VAL A CG1   1 
ATOM   961  C CG2   . VAL A 1 129 ? 4.725   -28.369 31.509  1.00 21.80 ? 129  VAL A CG2   1 
ATOM   962  N N     . THR A 1 130 ? 9.119   -26.587 30.703  1.00 19.82 ? 130  THR A N     1 
ATOM   963  C CA    . THR A 1 130 ? 10.350  -26.418 29.893  1.00 22.51 ? 130  THR A CA    1 
ATOM   964  C C     . THR A 1 130 ? 10.745  -27.769 29.325  1.00 20.07 ? 130  THR A C     1 
ATOM   965  O O     . THR A 1 130 ? 10.209  -28.811 29.795  1.00 20.62 ? 130  THR A O     1 
ATOM   966  C CB    . THR A 1 130 ? 11.499  -25.812 30.708  1.00 22.21 ? 130  THR A CB    1 
ATOM   967  O OG1   . THR A 1 130 ? 11.847  -26.737 31.748  1.00 21.91 ? 130  THR A OG1   1 
ATOM   968  C CG2   . THR A 1 130 ? 11.155  -24.472 31.306  1.00 23.45 ? 130  THR A CG2   1 
ATOM   969  N N     . TYR A 1 131 ? 11.664  -27.776 28.362  1.00 18.86 ? 131  TYR A N     1 
ATOM   970  C CA    . TYR A 1 131 ? 12.230  -29.037 27.839  1.00 20.06 ? 131  TYR A CA    1 
ATOM   971  C C     . TYR A 1 131 ? 12.932  -29.778 28.969  1.00 20.30 ? 131  TYR A C     1 
ATOM   972  O O     . TYR A 1 131 ? 12.794  -31.005 29.031  1.00 20.42 ? 131  TYR A O     1 
ATOM   973  C CB    . TYR A 1 131 ? 13.170  -28.763 26.671  1.00 20.76 ? 131  TYR A CB    1 
ATOM   974  C CG    . TYR A 1 131 ? 12.437  -28.233 25.466  1.00 20.05 ? 131  TYR A CG    1 
ATOM   975  C CD1   . TYR A 1 131 ? 11.771  -29.103 24.624  1.00 21.46 ? 131  TYR A CD1   1 
ATOM   976  C CD2   . TYR A 1 131 ? 12.375  -26.880 25.179  1.00 22.04 ? 131  TYR A CD2   1 
ATOM   977  C CE1   . TYR A 1 131 ? 11.108  -28.648 23.500  1.00 21.00 ? 131  TYR A CE1   1 
ATOM   978  C CE2   . TYR A 1 131 ? 11.710  -26.403 24.066  1.00 21.96 ? 131  TYR A CE2   1 
ATOM   979  C CZ    . TYR A 1 131 ? 11.070  -27.294 23.217  1.00 20.63 ? 131  TYR A CZ    1 
ATOM   980  O OH    . TYR A 1 131 ? 10.435  -26.851 22.083  1.00 21.49 ? 131  TYR A OH    1 
ATOM   981  N N     . PHE A 1 132 ? 13.618  -29.053 29.862  1.00 22.32 ? 132  PHE A N     1 
ATOM   982  C CA    . PHE A 1 132 ? 14.248  -29.674 31.054  1.00 23.38 ? 132  PHE A CA    1 
ATOM   983  C C     . PHE A 1 132 ? 13.165  -30.373 31.885  1.00 22.36 ? 132  PHE A C     1 
ATOM   984  O O     . PHE A 1 132 ? 13.382  -31.524 32.300  1.00 22.64 ? 132  PHE A O     1 
ATOM   985  C CB    . PHE A 1 132 ? 14.994  -28.625 31.892  1.00 24.70 ? 132  PHE A CB    1 
ATOM   986  C CG    . PHE A 1 132 ? 16.314  -28.211 31.299  1.00 26.55 ? 132  PHE A CG    1 
ATOM   987  C CD1   . PHE A 1 132 ? 17.332  -29.138 31.175  1.00 28.83 ? 132  PHE A CD1   1 
ATOM   988  C CD2   . PHE A 1 132 ? 16.534  -26.920 30.862  1.00 27.34 ? 132  PHE A CD2   1 
ATOM   989  C CE1   . PHE A 1 132 ? 18.549  -28.785 30.619  1.00 31.07 ? 132  PHE A CE1   1 
ATOM   990  C CE2   . PHE A 1 132 ? 17.769  -26.559 30.335  1.00 28.61 ? 132  PHE A CE2   1 
ATOM   991  C CZ    . PHE A 1 132 ? 18.763  -27.497 30.202  1.00 28.56 ? 132  PHE A CZ    1 
ATOM   992  N N     . ASP A 1 133 ? 12.067  -29.672 32.168  1.00 24.34 ? 133  ASP A N     1 
ATOM   993  C CA    . ASP A 1 133 ? 10.941  -30.193 32.989  1.00 22.21 ? 133  ASP A CA    1 
ATOM   994  C C     . ASP A 1 133 ? 10.427  -31.500 32.375  1.00 22.03 ? 133  ASP A C     1 
ATOM   995  O O     . ASP A 1 133 ? 10.241  -32.490 33.091  1.00 22.38 ? 133  ASP A O     1 
ATOM   996  C CB    . ASP A 1 133 ? 9.790   -29.194 33.115  1.00 24.26 ? 133  ASP A CB    1 
ATOM   997  C CG    . ASP A 1 133 ? 10.109  -27.945 33.930  1.00 27.46 ? 133  ASP A CG    1 
ATOM   998  O OD1   . ASP A 1 133 ? 11.049  -28.007 34.735  1.00 25.23 ? 133  ASP A OD1   1 
ATOM   999  O OD2   . ASP A 1 133 ? 9.392   -26.929 33.745  1.00 28.54 ? 133  ASP A OD2   1 
ATOM   1000 N N     . LEU A 1 134 ? 10.120  -31.495 31.083  1.00 22.27 ? 134  LEU A N     1 
ATOM   1001 C CA    . LEU A 1 134 ? 9.520   -32.691 30.466  1.00 21.64 ? 134  LEU A CA    1 
ATOM   1002 C C     . LEU A 1 134 ? 10.531  -33.830 30.416  1.00 24.93 ? 134  LEU A C     1 
ATOM   1003 O O     . LEU A 1 134 ? 10.107  -35.000 30.633  1.00 23.26 ? 134  LEU A O     1 
ATOM   1004 C CB    . LEU A 1 134 ? 8.990   -32.353 29.083  1.00 22.32 ? 134  LEU A CB    1 
ATOM   1005 C CG    . LEU A 1 134 ? 8.215   -33.488 28.424  1.00 20.15 ? 134  LEU A CG    1 
ATOM   1006 C CD1   . LEU A 1 134 ? 7.065   -33.946 29.311  1.00 22.47 ? 134  LEU A CD1   1 
ATOM   1007 C CD2   . LEU A 1 134 ? 7.684   -33.055 27.080  1.00 21.36 ? 134  LEU A CD2   1 
ATOM   1008 N N     . HIS A 1 135 ? 11.788  -33.538 30.079  1.00 24.02 ? 135  HIS A N     1 
ATOM   1009 C CA    . HIS A 1 135 ? 12.874  -34.544 30.101  1.00 26.41 ? 135  HIS A CA    1 
ATOM   1010 C C     . HIS A 1 135 ? 12.951  -35.195 31.485  1.00 26.18 ? 135  HIS A C     1 
ATOM   1011 O O     . HIS A 1 135 ? 12.976  -36.436 31.542  1.00 25.41 ? 135  HIS A O     1 
ATOM   1012 C CB    . HIS A 1 135 ? 14.193  -33.923 29.691  1.00 26.30 ? 135  HIS A CB    1 
ATOM   1013 C CG    . HIS A 1 135 ? 15.360  -34.800 29.963  1.00 26.72 ? 135  HIS A CG    1 
ATOM   1014 N ND1   . HIS A 1 135 ? 15.669  -35.885 29.165  1.00 27.35 ? 135  HIS A ND1   1 
ATOM   1015 C CD2   . HIS A 1 135 ? 16.275  -34.773 30.946  1.00 25.55 ? 135  HIS A CD2   1 
ATOM   1016 C CE1   . HIS A 1 135 ? 16.763  -36.455 29.628  1.00 27.47 ? 135  HIS A CE1   1 
ATOM   1017 N NE2   . HIS A 1 135 ? 17.144  -35.814 30.710  1.00 27.95 ? 135  HIS A NE2   1 
ATOM   1018 N N     . GLU A 1 136 ? 12.990  -34.390 32.542  1.00 30.03 ? 136  GLU A N     1 
ATOM   1019 C CA    . GLU A 1 136 ? 13.060  -34.894 33.940  1.00 30.15 ? 136  GLU A CA    1 
ATOM   1020 C C     . GLU A 1 136 ? 11.850  -35.805 34.204  1.00 29.58 ? 136  GLU A C     1 
ATOM   1021 O O     . GLU A 1 136 ? 12.041  -36.906 34.728  1.00 28.16 ? 136  GLU A O     1 
ATOM   1022 C CB    . GLU A 1 136 ? 13.090  -33.738 34.948  1.00 37.52 ? 136  GLU A CB    1 
ATOM   1023 C CG    . GLU A 1 136 ? 14.405  -32.973 34.982  1.00 43.94 ? 136  GLU A CG    1 
ATOM   1024 C CD    . GLU A 1 136 ? 14.331  -31.628 35.715  1.00 51.94 ? 136  GLU A CD    1 
ATOM   1025 O OE1   . GLU A 1 136 ? 13.462  -31.469 36.631  1.00 49.78 ? 136  GLU A OE1   1 
ATOM   1026 O OE2   . GLU A 1 136 ? 15.134  -30.729 35.368  1.00 56.72 ? 136  GLU A OE2   1 
ATOM   1027 N N     . TYR A 1 137 ? 10.643  -35.378 33.837  1.00 25.68 ? 137  TYR A N     1 
ATOM   1028 C CA    . TYR A 1 137 ? 9.404   -36.156 34.064  1.00 25.30 ? 137  TYR A CA    1 
ATOM   1029 C C     . TYR A 1 137 ? 9.489   -37.498 33.316  1.00 26.95 ? 137  TYR A C     1 
ATOM   1030 O O     . TYR A 1 137 ? 9.172   -38.557 33.885  1.00 25.30 ? 137  TYR A O     1 
ATOM   1031 C CB    . TYR A 1 137 ? 8.175   -35.372 33.620  1.00 29.10 ? 137  TYR A CB    1 
ATOM   1032 C CG    . TYR A 1 137 ? 6.884   -36.057 33.987  1.00 30.33 ? 137  TYR A CG    1 
ATOM   1033 C CD1   . TYR A 1 137 ? 6.368   -37.050 33.175  1.00 29.97 ? 137  TYR A CD1   1 
ATOM   1034 C CD2   . TYR A 1 137 ? 6.187   -35.716 35.134  1.00 30.82 ? 137  TYR A CD2   1 
ATOM   1035 C CE1   . TYR A 1 137 ? 5.195   -37.703 33.495  1.00 31.69 ? 137  TYR A CE1   1 
ATOM   1036 C CE2   . TYR A 1 137 ? 5.007   -36.362 35.464  1.00 35.15 ? 137  TYR A CE2   1 
ATOM   1037 C CZ    . TYR A 1 137 ? 4.524   -37.372 34.651  1.00 34.29 ? 137  TYR A CZ    1 
ATOM   1038 O OH    . TYR A 1 137 ? 3.368   -38.034 34.926  1.00 40.66 ? 137  TYR A OH    1 
ATOM   1039 N N     . LEU A 1 138 ? 9.869   -37.490 32.035  1.00 26.63 ? 138  LEU A N     1 
ATOM   1040 C CA    . LEU A 1 138 ? 9.903   -38.757 31.271  1.00 26.16 ? 138  LEU A CA    1 
ATOM   1041 C C     . LEU A 1 138 ? 10.963  -39.675 31.896  1.00 28.23 ? 138  LEU A C     1 
ATOM   1042 O O     . LEU A 1 138 ? 10.706  -40.860 31.979  1.00 28.54 ? 138  LEU A O     1 
ATOM   1043 C CB    . LEU A 1 138 ? 10.253  -38.509 29.809  1.00 27.28 ? 138  LEU A CB    1 
ATOM   1044 C CG    . LEU A 1 138 ? 9.307   -37.641 29.000  1.00 27.74 ? 138  LEU A CG    1 
ATOM   1045 C CD1   . LEU A 1 138 ? 9.813   -37.587 27.556  1.00 27.83 ? 138  LEU A CD1   1 
ATOM   1046 C CD2   . LEU A 1 138 ? 7.881   -38.164 29.075  1.00 27.12 ? 138  LEU A CD2   1 
ATOM   1047 N N     . GLU A 1 139 ? 12.117  -39.154 32.288  1.00 26.29 ? 139  GLU A N     1 
ATOM   1048 C CA    . GLU A 1 139 ? 13.206  -39.990 32.850  1.00 31.10 ? 139  GLU A CA    1 
ATOM   1049 C C     . GLU A 1 139 ? 12.723  -40.665 34.146  1.00 31.11 ? 139  GLU A C     1 
ATOM   1050 O O     . GLU A 1 139 ? 13.125  -41.822 34.399  1.00 30.35 ? 139  GLU A O     1 
ATOM   1051 C CB    . GLU A 1 139 ? 14.477  -39.154 33.043  1.00 31.89 ? 139  GLU A CB    1 
ATOM   1052 C CG    . GLU A 1 139 ? 15.226  -38.874 31.752  1.00 33.75 ? 139  GLU A CG    1 
ATOM   1053 C CD    . GLU A 1 139 ? 15.589  -40.093 30.922  1.00 38.44 ? 139  GLU A CD    1 
ATOM   1054 O OE1   . GLU A 1 139 ? 15.112  -40.190 29.755  1.00 35.70 ? 139  GLU A OE1   1 
ATOM   1055 O OE2   . GLU A 1 139 ? 16.322  -40.962 31.448  1.00 40.97 ? 139  GLU A OE2   1 
ATOM   1056 N N     . ALA A 1 140 ? 11.869  -39.995 34.920  1.00 31.96 ? 140  ALA A N     1 
ATOM   1057 C CA    . ALA A 1 140 ? 11.359  -40.489 36.221  1.00 34.19 ? 140  ALA A CA    1 
ATOM   1058 C C     . ALA A 1 140 ? 10.119  -41.366 36.044  1.00 36.10 ? 140  ALA A C     1 
ATOM   1059 O O     . ALA A 1 140 ? 10.014  -42.343 36.802  1.00 33.48 ? 140  ALA A O     1 
ATOM   1060 C CB    . ALA A 1 140 ? 11.089  -39.337 37.153  1.00 35.39 ? 140  ALA A CB    1 
ATOM   1061 N N     . HIS A 1 141 ? 9.223   -41.060 35.096  1.00 32.58 ? 141  HIS A N     1 
ATOM   1062 C CA    . HIS A 1 141 ? 7.862   -41.665 35.052  1.00 36.12 ? 141  HIS A CA    1 
ATOM   1063 C C     . HIS A 1 141 ? 7.508   -42.319 33.719  1.00 35.57 ? 141  HIS A C     1 
ATOM   1064 O O     . HIS A 1 141 ? 6.494   -43.016 33.696  1.00 35.57 ? 141  HIS A O     1 
ATOM   1065 C CB    . HIS A 1 141 ? 6.806   -40.605 35.394  1.00 38.08 ? 141  HIS A CB    1 
ATOM   1066 C CG    . HIS A 1 141 ? 7.079   -39.908 36.677  1.00 39.77 ? 141  HIS A CG    1 
ATOM   1067 N ND1   . HIS A 1 141 ? 7.158   -40.589 37.888  1.00 43.15 ? 141  HIS A ND1   1 
ATOM   1068 C CD2   . HIS A 1 141 ? 7.306   -38.605 36.941  1.00 41.81 ? 141  HIS A CD2   1 
ATOM   1069 C CE1   . HIS A 1 141 ? 7.426   -39.730 38.850  1.00 44.22 ? 141  HIS A CE1   1 
ATOM   1070 N NE2   . HIS A 1 141 ? 7.518   -38.502 38.297  1.00 46.33 ? 141  HIS A NE2   1 
ATOM   1071 N N     . ALA A 1 142 ? 8.202   -42.031 32.621  1.00 36.30 ? 142  ALA A N     1 
ATOM   1072 C CA    . ALA A 1 142 ? 7.866   -42.626 31.306  1.00 34.64 ? 142  ALA A CA    1 
ATOM   1073 C C     . ALA A 1 142 ? 9.141   -42.753 30.483  1.00 34.67 ? 142  ALA A C     1 
ATOM   1074 O O     . ALA A 1 142 ? 9.261   -42.171 29.403  1.00 29.37 ? 142  ALA A O     1 
ATOM   1075 C CB    . ALA A 1 142 ? 6.797   -41.819 30.609  1.00 34.75 ? 142  ALA A CB    1 
ATOM   1076 N N     . PRO A 1 143 ? 10.113  -43.564 30.967  1.00 32.26 ? 143  PRO A N     1 
ATOM   1077 C CA    . PRO A 1 143 ? 11.474  -43.550 30.441  1.00 28.27 ? 143  PRO A CA    1 
ATOM   1078 C C     . PRO A 1 143 ? 11.644  -44.170 29.051  1.00 26.49 ? 143  PRO A C     1 
ATOM   1079 O O     . PRO A 1 143 ? 12.706  -44.044 28.524  1.00 27.64 ? 143  PRO A O     1 
ATOM   1080 C CB    . PRO A 1 143 ? 12.298  -44.319 31.498  1.00 28.72 ? 143  PRO A CB    1 
ATOM   1081 C CG    . PRO A 1 143 ? 11.311  -45.183 32.204  1.00 31.79 ? 143  PRO A CG    1 
ATOM   1082 C CD    . PRO A 1 143 ? 9.965   -44.490 32.105  1.00 33.41 ? 143  PRO A CD    1 
ATOM   1083 N N     . SER A 1 144 ? 10.606  -44.738 28.446  1.00 26.63 ? 144  SER A N     1 
ATOM   1084 C CA    . SER A 1 144 ? 10.706  -45.272 27.077  1.00 27.53 ? 144  SER A CA    1 
ATOM   1085 C C     . SER A 1 144 ? 10.554  -44.125 26.070  1.00 25.72 ? 144  SER A C     1 
ATOM   1086 O O     . SER A 1 144 ? 10.770  -44.366 24.889  1.00 26.48 ? 144  SER A O     1 
ATOM   1087 C CB    . SER A 1 144 ? 9.699   -46.346 26.825  1.00 28.40 ? 144  SER A CB    1 
ATOM   1088 O OG    . SER A 1 144 ? 8.397   -45.822 26.856  1.00 28.18 ? 144  SER A OG    1 
ATOM   1089 N N     . LEU A 1 145 ? 10.129  -42.955 26.508  1.00 24.71 ? 145  LEU A N     1 
ATOM   1090 C CA    . LEU A 1 145 ? 9.890   -41.799 25.602  1.00 24.05 ? 145  LEU A CA    1 
ATOM   1091 C C     . LEU A 1 145 ? 11.067  -40.818 25.695  1.00 23.37 ? 145  LEU A C     1 
ATOM   1092 O O     . LEU A 1 145 ? 11.771  -40.769 26.724  1.00 25.28 ? 145  LEU A O     1 
ATOM   1093 C CB    . LEU A 1 145 ? 8.579   -41.116 25.994  1.00 23.83 ? 145  LEU A CB    1 
ATOM   1094 C CG    . LEU A 1 145 ? 7.325   -41.986 25.911  1.00 24.95 ? 145  LEU A CG    1 
ATOM   1095 C CD1   . LEU A 1 145 ? 6.072   -41.186 26.295  1.00 26.26 ? 145  LEU A CD1   1 
ATOM   1096 C CD2   . LEU A 1 145 ? 7.172   -42.611 24.514  1.00 26.03 ? 145  LEU A CD2   1 
ATOM   1097 N N     . MET A 1 146 ? 11.204  -39.982 24.682  1.00 22.98 ? 146  MET A N     1 
ATOM   1098 C CA    . MET A 1 146 ? 12.154  -38.853 24.706  1.00 24.18 ? 146  MET A CA    1 
ATOM   1099 C C     . MET A 1 146 ? 11.465  -37.629 24.094  1.00 24.68 ? 146  MET A C     1 
ATOM   1100 O O     . MET A 1 146 ? 10.526  -37.787 23.239  1.00 23.32 ? 146  MET A O     1 
ATOM   1101 C CB    . MET A 1 146 ? 13.418  -39.194 23.905  1.00 23.96 ? 146  MET A CB    1 
ATOM   1102 C CG    . MET A 1 146 ? 13.101  -39.716 22.538  1.00 26.09 ? 146  MET A CG    1 
ATOM   1103 S SD    . MET A 1 146 ? 14.565  -40.208 21.642  1.00 30.76 ? 146  MET A SD    1 
ATOM   1104 C CE    . MET A 1 146 ? 15.130  -38.661 20.931  1.00 29.22 ? 146  MET A CE    1 
ATOM   1105 N N     . ILE A 1 147 ? 11.925  -36.456 24.513  1.00 23.39 ? 147  ILE A N     1 
ATOM   1106 C CA    . ILE A 1 147 ? 11.468  -35.160 23.961  1.00 23.93 ? 147  ILE A CA    1 
ATOM   1107 C C     . ILE A 1 147 ? 12.206  -34.886 22.657  1.00 23.34 ? 147  ILE A C     1 
ATOM   1108 O O     . ILE A 1 147 ? 13.175  -35.591 22.330  1.00 23.69 ? 147  ILE A O     1 
ATOM   1109 C CB    . ILE A 1 147 ? 11.684  -34.010 24.954  1.00 22.67 ? 147  ILE A CB    1 
ATOM   1110 C CG1   . ILE A 1 147 ? 13.173  -33.721 25.163  1.00 23.65 ? 147  ILE A CG1   1 
ATOM   1111 C CG2   . ILE A 1 147 ? 10.938  -34.289 26.258  1.00 22.70 ? 147  ILE A CG2   1 
ATOM   1112 C CD1   . ILE A 1 147 ? 13.429  -32.503 26.008  1.00 26.01 ? 147  ILE A CD1   1 
ATOM   1113 N N     . ASP A 1 148 ? 11.759  -33.864 21.952  1.00 22.00 ? 148  ASP A N     1 
ATOM   1114 C CA    . ASP A 1 148 ? 12.553  -33.252 20.873  1.00 21.98 ? 148  ASP A CA    1 
ATOM   1115 C C     . ASP A 1 148 ? 12.776  -31.801 21.291  1.00 22.08 ? 148  ASP A C     1 
ATOM   1116 O O     . ASP A 1 148 ? 11.751  -31.080 21.491  1.00 22.59 ? 148  ASP A O     1 
ATOM   1117 C CB    . ASP A 1 148 ? 11.854  -33.382 19.519  1.00 24.42 ? 148  ASP A CB    1 
ATOM   1118 C CG    . ASP A 1 148 ? 12.735  -32.775 18.449  1.00 25.43 ? 148  ASP A CG    1 
ATOM   1119 O OD1   . ASP A 1 148 ? 12.907  -31.564 18.492  1.00 23.82 ? 148  ASP A OD1   1 
ATOM   1120 O OD2   . ASP A 1 148 ? 13.300  -33.539 17.638  1.00 26.69 ? 148  ASP A OD2   1 
ATOM   1121 N N     . CYS A 1 149 ? 14.033  -31.419 21.524  1.00 22.33 ? 149  CYS A N     1 
ATOM   1122 C CA    . CYS A 1 149 ? 14.382  -30.080 22.065  1.00 22.31 ? 149  CYS A CA    1 
ATOM   1123 C C     . CYS A 1 149 ? 15.154  -29.270 21.039  1.00 22.82 ? 149  CYS A C     1 
ATOM   1124 O O     . CYS A 1 149 ? 15.924  -29.816 20.235  1.00 21.46 ? 149  CYS A O     1 
ATOM   1125 C CB    . CYS A 1 149 ? 15.142  -30.162 23.381  1.00 22.80 ? 149  CYS A CB    1 
ATOM   1126 S SG    . CYS A 1 149 ? 16.549  -31.276 23.318  1.00 25.08 ? 149  CYS A SG    1 
ATOM   1127 N N     . PRO A 1 150 ? 14.976  -27.927 21.088  1.00 21.42 ? 150  PRO A N     1 
ATOM   1128 C CA    . PRO A 1 150 ? 15.864  -27.009 20.389  1.00 22.96 ? 150  PRO A CA    1 
ATOM   1129 C C     . PRO A 1 150 ? 17.236  -27.034 21.086  1.00 22.16 ? 150  PRO A C     1 
ATOM   1130 O O     . PRO A 1 150 ? 17.434  -27.799 22.038  1.00 20.21 ? 150  PRO A O     1 
ATOM   1131 C CB    . PRO A 1 150 ? 15.168  -25.642 20.514  1.00 22.56 ? 150  PRO A CB    1 
ATOM   1132 C CG    . PRO A 1 150 ? 14.427  -25.747 21.838  1.00 24.28 ? 150  PRO A CG    1 
ATOM   1133 C CD    . PRO A 1 150 ? 14.054  -27.207 21.977  1.00 20.38 ? 150  PRO A CD    1 
ATOM   1134 N N     . ASP A 1 151 ? 18.138  -26.155 20.671  1.00 22.33 ? 151  ASP A N     1 
ATOM   1135 C CA    . ASP A 1 151 ? 19.476  -26.115 21.246  1.00 24.54 ? 151  ASP A CA    1 
ATOM   1136 C C     . ASP A 1 151 ? 19.488  -25.822 22.727  1.00 24.39 ? 151  ASP A C     1 
ATOM   1137 O O     . ASP A 1 151 ? 20.344  -26.294 23.428  1.00 27.74 ? 151  ASP A O     1 
ATOM   1138 C CB    . ASP A 1 151 ? 20.347  -25.087 20.565  1.00 26.18 ? 151  ASP A CB    1 
ATOM   1139 C CG    . ASP A 1 151 ? 20.659  -25.422 19.158  1.00 29.13 ? 151  ASP A CG    1 
ATOM   1140 O OD1   . ASP A 1 151 ? 20.645  -26.603 18.800  1.00 27.60 ? 151  ASP A OD1   1 
ATOM   1141 O OD2   . ASP A 1 151 ? 20.926  -24.475 18.409  1.00 34.77 ? 151  ASP A OD2   1 
ATOM   1142 N N     . LEU A 1 152 ? 18.539  -25.040 23.189  1.00 25.01 ? 152  LEU A N     1 
ATOM   1143 C CA    . LEU A 1 152 ? 18.535  -24.647 24.584  1.00 26.70 ? 152  LEU A CA    1 
ATOM   1144 C C     . LEU A 1 152 ? 17.319  -25.161 25.305  1.00 29.28 ? 152  LEU A C     1 
ATOM   1145 O O     . LEU A 1 152 ? 16.211  -24.931 24.900  1.00 37.55 ? 152  LEU A O     1 
ATOM   1146 C CB    . LEU A 1 152 ? 18.609  -23.148 24.701  1.00 27.16 ? 152  LEU A CB    1 
ATOM   1147 C CG    . LEU A 1 152 ? 19.746  -22.449 23.954  1.00 29.18 ? 152  LEU A CG    1 
ATOM   1148 C CD1   . LEU A 1 152 ? 19.574  -20.944 23.964  1.00 30.44 ? 152  LEU A CD1   1 
ATOM   1149 C CD2   . LEU A 1 152 ? 21.094  -22.852 24.519  1.00 29.46 ? 152  LEU A CD2   1 
ATOM   1150 N N     . GLY A 1 153 ? 17.529  -25.832 26.396  1.00 32.61 ? 153  GLY A N     1 
ATOM   1151 C CA    . GLY A 1 153 ? 16.392  -26.455 27.045  1.00 38.22 ? 153  GLY A CA    1 
ATOM   1152 C C     . GLY A 1 153 ? 15.496  -25.663 27.936  1.00 27.83 ? 153  GLY A C     1 
ATOM   1153 O O     . GLY A 1 153 ? 14.525  -26.172 28.423  1.00 22.94 ? 153  GLY A O     1 
ATOM   1154 N N     . TRP A 1 154 ? 15.844  -24.408 28.139  1.00 26.22 ? 154  TRP A N     1 
ATOM   1155 C CA    . TRP A 1 154 ? 15.067  -23.546 29.012  1.00 25.01 ? 154  TRP A CA    1 
ATOM   1156 C C     . TRP A 1 154 ? 13.801  -22.998 28.381  1.00 25.14 ? 154  TRP A C     1 
ATOM   1157 O O     . TRP A 1 154 ? 12.998  -22.390 29.027  1.00 24.71 ? 154  TRP A O     1 
ATOM   1158 C CB    . TRP A 1 154 ? 15.958  -22.452 29.591  1.00 26.96 ? 154  TRP A CB    1 
ATOM   1159 C CG    . TRP A 1 154 ? 16.623  -21.503 28.641  1.00 25.96 ? 154  TRP A CG    1 
ATOM   1160 C CD1   . TRP A 1 154 ? 16.289  -21.233 27.350  1.00 25.60 ? 154  TRP A CD1   1 
ATOM   1161 C CD2   . TRP A 1 154 ? 17.739  -20.668 28.942  1.00 28.13 ? 154  TRP A CD2   1 
ATOM   1162 N NE1   . TRP A 1 154 ? 17.130  -20.297 26.828  1.00 25.08 ? 154  TRP A NE1   1 
ATOM   1163 C CE2   . TRP A 1 154 ? 18.034  -19.932 27.785  1.00 26.70 ? 154  TRP A CE2   1 
ATOM   1164 C CE3   . TRP A 1 154 ? 18.525  -20.481 30.077  1.00 30.56 ? 154  TRP A CE3   1 
ATOM   1165 C CZ2   . TRP A 1 154 ? 19.073  -19.022 27.730  1.00 30.50 ? 154  TRP A CZ2   1 
ATOM   1166 C CZ3   . TRP A 1 154 ? 19.560  -19.583 30.020  1.00 34.11 ? 154  TRP A CZ3   1 
ATOM   1167 C CH2   . TRP A 1 154 ? 19.824  -18.860 28.858  1.00 33.35 ? 154  TRP A CH2   1 
ATOM   1168 N N     . GLY A 1 155 ? 13.625  -23.256 27.101  1.00 22.81 ? 155  GLY A N     1 
ATOM   1169 C CA    . GLY A 1 155 ? 12.427  -22.840 26.438  1.00 21.96 ? 155  GLY A CA    1 
ATOM   1170 C C     . GLY A 1 155 ? 11.211  -23.691 26.759  1.00 21.88 ? 155  GLY A C     1 
ATOM   1171 O O     . GLY A 1 155 ? 11.341  -24.678 27.449  1.00 23.33 ? 155  GLY A O     1 
ATOM   1172 N N     . SER A 1 156 ? 10.050  -23.314 26.244  1.00 20.58 ? 156  SER A N     1 
ATOM   1173 C CA    . SER A 1 156 ? 8.824   -24.024 26.491  1.00 20.10 ? 156  SER A CA    1 
ATOM   1174 C C     . SER A 1 156 ? 8.482   -24.997 25.393  1.00 21.56 ? 156  SER A C     1 
ATOM   1175 O O     . SER A 1 156 ? 8.569   -24.652 24.243  1.00 21.78 ? 156  SER A O     1 
ATOM   1176 C CB    . SER A 1 156 ? 7.647   -23.055 26.609  1.00 20.31 ? 156  SER A CB    1 
ATOM   1177 O OG    . SER A 1 156 ? 6.418   -23.718 26.546  1.00 20.94 ? 156  SER A OG    1 
ATOM   1178 N N     . VAL A 1 157 ? 8.082   -26.193 25.773  1.00 20.28 ? 157  VAL A N     1 
ATOM   1179 C CA    . VAL A 1 157 ? 7.629   -27.199 24.762  1.00 20.81 ? 157  VAL A CA    1 
ATOM   1180 C C     . VAL A 1 157 ? 6.487   -26.575 23.970  1.00 18.76 ? 157  VAL A C     1 
ATOM   1181 O O     . VAL A 1 157 ? 6.448   -26.724 22.746  1.00 20.13 ? 157  VAL A O     1 
ATOM   1182 C CB    . VAL A 1 157 ? 7.215   -28.534 25.419  1.00 20.88 ? 157  VAL A CB    1 
ATOM   1183 C CG1   . VAL A 1 157 ? 6.844   -29.554 24.365  1.00 20.32 ? 157  VAL A CG1   1 
ATOM   1184 C CG2   . VAL A 1 157 ? 8.297   -29.084 26.329  1.00 24.60 ? 157  VAL A CG2   1 
ATOM   1185 N N     . VAL A 1 158 ? 5.564   -25.891 24.651  1.00 18.89 ? 158  VAL A N     1 
ATOM   1186 C CA    . VAL A 1 158 ? 4.403   -25.188 24.048  1.00 20.28 ? 158  VAL A CA    1 
ATOM   1187 C C     . VAL A 1 158 ? 4.857   -23.949 23.281  1.00 18.84 ? 158  VAL A C     1 
ATOM   1188 O O     . VAL A 1 158 ? 4.569   -23.838 22.066  1.00 19.88 ? 158  VAL A O     1 
ATOM   1189 C CB    . VAL A 1 158 ? 3.372   -24.823 25.135  1.00 18.27 ? 158  VAL A CB    1 
ATOM   1190 C CG1   . VAL A 1 158 ? 2.329   -23.891 24.570  1.00 20.87 ? 158  VAL A CG1   1 
ATOM   1191 C CG2   . VAL A 1 158 ? 2.746   -26.072 25.690  1.00 17.77 ? 158  VAL A CG2   1 
ATOM   1192 N N     . GLY A 1 159 ? 5.524   -23.020 23.963  1.00 18.19 ? 159  GLY A N     1 
ATOM   1193 C CA    . GLY A 1 159 ? 5.938   -21.728 23.383  1.00 19.03 ? 159  GLY A CA    1 
ATOM   1194 C C     . GLY A 1 159 ? 6.729   -21.903 22.093  1.00 17.70 ? 159  GLY A C     1 
ATOM   1195 O O     . GLY A 1 159 ? 6.443   -21.207 21.096  1.00 19.06 ? 159  GLY A O     1 
ATOM   1196 N N     . ASN A 1 160 ? 7.668   -22.830 22.105  1.00 18.80 ? 160  ASN A N     1 
ATOM   1197 C CA    . ASN A 1 160 ? 8.557   -23.056 20.942  1.00 19.22 ? 160  ASN A CA    1 
ATOM   1198 C C     . ASN A 1 160 ? 7.683   -23.542 19.779  1.00 18.87 ? 160  ASN A C     1 
ATOM   1199 O O     . ASN A 1 160 ? 7.799   -23.006 18.641  1.00 18.77 ? 160  ASN A O     1 
ATOM   1200 C CB    . ASN A 1 160 ? 9.692   -23.990 21.319  1.00 20.17 ? 160  ASN A CB    1 
ATOM   1201 C CG    . ASN A 1 160 ? 10.559  -24.334 20.128  1.00 22.39 ? 160  ASN A CG    1 
ATOM   1202 O OD1   . ASN A 1 160 ? 10.128  -25.090 19.272  1.00 24.50 ? 160  ASN A OD1   1 
ATOM   1203 N ND2   . ASN A 1 160 ? 11.765  -23.793 20.078  1.00 24.31 ? 160  ASN A ND2   1 
ATOM   1204 N N     . ALA A 1 161 ? 6.801   -24.500 20.029  1.00 18.93 ? 161  ALA A N     1 
ATOM   1205 C CA    . ALA A 1 161 ? 5.917   -25.065 18.975  1.00 18.33 ? 161  ALA A CA    1 
ATOM   1206 C C     . ALA A 1 161 ? 4.966   -23.981 18.429  1.00 20.59 ? 161  ALA A C     1 
ATOM   1207 O O     . ALA A 1 161 ? 4.693   -23.969 17.205  1.00 20.72 ? 161  ALA A O     1 
ATOM   1208 C CB    . ALA A 1 161 ? 5.184   -26.249 19.559  1.00 17.40 ? 161  ALA A CB    1 
ATOM   1209 N N     . LEU A 1 162 ? 4.526   -23.024 19.254  1.00 18.78 ? 162  LEU A N     1 
ATOM   1210 C CA    . LEU A 1 162 ? 3.582   -21.961 18.826  1.00 20.81 ? 162  LEU A CA    1 
ATOM   1211 C C     . LEU A 1 162 ? 4.311   -20.937 17.962  1.00 20.18 ? 162  LEU A C     1 
ATOM   1212 O O     . LEU A 1 162 ? 3.607   -20.151 17.310  1.00 21.59 ? 162  LEU A O     1 
ATOM   1213 C CB    . LEU A 1 162 ? 2.937   -21.292 20.047  1.00 23.01 ? 162  LEU A CB    1 
ATOM   1214 C CG    . LEU A 1 162 ? 2.002   -22.208 20.832  1.00 22.87 ? 162  LEU A CG    1 
ATOM   1215 C CD1   . LEU A 1 162 ? 1.378   -21.467 21.992  1.00 24.34 ? 162  LEU A CD1   1 
ATOM   1216 C CD2   . LEU A 1 162 ? 0.937   -22.814 19.918  1.00 23.27 ? 162  LEU A CD2   1 
ATOM   1217 N N     . ASP A 1 163 ? 5.651   -20.933 17.951  1.00 19.17 ? 163  ASP A N     1 
ATOM   1218 C CA    . ASP A 1 163 ? 6.403   -20.052 17.023  1.00 19.80 ? 163  ASP A CA    1 
ATOM   1219 C C     . ASP A 1 163 ? 6.925   -20.911 15.867  1.00 20.51 ? 163  ASP A C     1 
ATOM   1220 O O     . ASP A 1 163 ? 7.720   -20.385 15.065  1.00 21.29 ? 163  ASP A O     1 
ATOM   1221 C CB    . ASP A 1 163 ? 7.534   -19.293 17.724  1.00 21.55 ? 163  ASP A CB    1 
ATOM   1222 C CG    . ASP A 1 163 ? 7.618   -17.822 17.316  1.00 24.06 ? 163  ASP A CG    1 
ATOM   1223 O OD1   . ASP A 1 163 ? 6.556   -17.256 16.979  1.00 20.55 ? 163  ASP A OD1   1 
ATOM   1224 O OD2   . ASP A 1 163 ? 8.756   -17.263 17.319  1.00 24.90 ? 163  ASP A OD2   1 
ATOM   1225 N N     . ARG A 1 164 ? 6.443   -22.150 15.766  1.00 20.29 ? 164  ARG A N     1 
ATOM   1226 C CA    . ARG A 1 164 ? 6.954   -23.217 14.847  1.00 22.22 ? 164  ARG A CA    1 
ATOM   1227 C C     . ARG A 1 164 ? 8.483   -23.336 14.950  1.00 23.88 ? 164  ARG A C     1 
ATOM   1228 O O     . ARG A 1 164 ? 9.208   -23.399 13.906  1.00 23.17 ? 164  ARG A O     1 
ATOM   1229 C CB    . ARG A 1 164 ? 6.424   -22.962 13.440  1.00 23.24 ? 164  ARG A CB    1 
ATOM   1230 C CG    . ARG A 1 164 ? 4.905   -22.994 13.353  1.00 25.46 ? 164  ARG A CG    1 
ATOM   1231 C CD    . ARG A 1 164 ? 4.433   -23.160 11.913  1.00 26.04 ? 164  ARG A CD    1 
ATOM   1232 N NE    . ARG A 1 164 ? 4.809   -22.020 11.097  1.00 23.57 ? 164  ARG A NE    1 
ATOM   1233 C CZ    . ARG A 1 164 ? 4.026   -20.957 10.875  1.00 23.95 ? 164  ARG A CZ    1 
ATOM   1234 N NH1   . ARG A 1 164 ? 2.830   -20.860 11.450  1.00 23.50 ? 164  ARG A NH1   1 
ATOM   1235 N NH2   . ARG A 1 164 ? 4.443   -19.975 10.079  1.00 22.27 ? 164  ARG A NH2   1 
ATOM   1236 N N     . GLY A 1 165 ? 8.988   -23.457 16.175  1.00 20.28 ? 165  GLY A N     1 
ATOM   1237 C CA    . GLY A 1 165 ? 10.383  -23.821 16.440  1.00 22.25 ? 165  GLY A CA    1 
ATOM   1238 C C     . GLY A 1 165 ? 10.642  -25.284 16.106  1.00 23.75 ? 165  GLY A C     1 
ATOM   1239 O O     . GLY A 1 165 ? 9.686   -26.018 15.690  1.00 20.06 ? 165  GLY A O     1 
ATOM   1240 N N     . ALA A 1 166 ? 11.885  -25.712 16.250  1.00 20.13 ? 166  ALA A N     1 
ATOM   1241 C CA    . ALA A 1 166 ? 12.328  -27.030 15.763  1.00 22.29 ? 166  ALA A CA    1 
ATOM   1242 C C     . ALA A 1 166 ? 13.489  -27.571 16.588  1.00 23.04 ? 166  ALA A C     1 
ATOM   1243 O O     . ALA A 1 166 ? 14.279  -26.762 17.169  1.00 23.05 ? 166  ALA A O     1 
ATOM   1244 C CB    . ALA A 1 166 ? 12.686  -26.941 14.306  1.00 25.16 ? 166  ALA A CB    1 
ATOM   1245 N N     . GLY A 1 167 ? 13.564  -28.897 16.637  1.00 22.01 ? 167  GLY A N     1 
ATOM   1246 C CA    . GLY A 1 167 ? 14.712  -29.646 17.157  1.00 22.91 ? 167  GLY A CA    1 
ATOM   1247 C C     . GLY A 1 167 ? 15.260  -30.541 16.080  1.00 21.18 ? 167  GLY A C     1 
ATOM   1248 O O     . GLY A 1 167 ? 15.102  -30.208 14.848  1.00 20.49 ? 167  GLY A O     1 
ATOM   1249 N N     . TYR A 1 168 ? 15.914  -31.616 16.493  1.00 23.27 ? 168  TYR A N     1 
ATOM   1250 C CA    . TYR A 1 168 ? 16.891  -32.318 15.625  1.00 23.72 ? 168  TYR A CA    1 
ATOM   1251 C C     . TYR A 1 168 ? 16.717  -33.832 15.653  1.00 23.26 ? 168  TYR A C     1 
ATOM   1252 O O     . TYR A 1 168 ? 17.432  -34.523 14.903  1.00 21.49 ? 168  TYR A O     1 
ATOM   1253 C CB    . TYR A 1 168 ? 18.298  -31.860 16.015  1.00 25.55 ? 168  TYR A CB    1 
ATOM   1254 C CG    . TYR A 1 168 ? 18.419  -30.368 15.945  1.00 24.44 ? 168  TYR A CG    1 
ATOM   1255 C CD1   . TYR A 1 168 ? 18.617  -29.723 14.736  1.00 24.48 ? 168  TYR A CD1   1 
ATOM   1256 C CD2   . TYR A 1 168 ? 18.192  -29.601 17.067  1.00 26.25 ? 168  TYR A CD2   1 
ATOM   1257 C CE1   . TYR A 1 168 ? 18.653  -28.339 14.662  1.00 24.72 ? 168  TYR A CE1   1 
ATOM   1258 C CE2   . TYR A 1 168 ? 18.224  -28.220 17.012  1.00 25.84 ? 168  TYR A CE2   1 
ATOM   1259 C CZ    . TYR A 1 168 ? 18.449  -27.587 15.799  1.00 24.02 ? 168  TYR A CZ    1 
ATOM   1260 O OH    . TYR A 1 168 ? 18.441  -26.228 15.735  1.00 23.69 ? 168  TYR A OH    1 
ATOM   1261 N N     . THR A 1 169 ? 15.768  -34.346 16.430  1.00 23.81 ? 169  THR A N     1 
ATOM   1262 C CA    . THR A 1 169 ? 15.374  -35.770 16.357  1.00 21.73 ? 169  THR A CA    1 
ATOM   1263 C C     . THR A 1 169 ? 14.445  -35.932 15.165  1.00 22.18 ? 169  THR A C     1 
ATOM   1264 O O     . THR A 1 169 ? 14.093  -34.949 14.501  1.00 23.44 ? 169  THR A O     1 
ATOM   1265 C CB    . THR A 1 169 ? 14.763  -36.255 17.670  1.00 21.09 ? 169  THR A CB    1 
ATOM   1266 O OG1   . THR A 1 169 ? 13.365  -35.951 17.715  1.00 23.49 ? 169  THR A OG1   1 
ATOM   1267 C CG2   . THR A 1 169 ? 15.495  -35.714 18.870  1.00 21.62 ? 169  THR A CG2   1 
ATOM   1268 N N     . PRO A 1 170 ? 14.018  -37.170 14.848  1.00 24.23 ? 170  PRO A N     1 
ATOM   1269 C CA    . PRO A 1 170 ? 12.992  -37.372 13.833  1.00 23.38 ? 170  PRO A CA    1 
ATOM   1270 C C     . PRO A 1 170 ? 11.692  -36.623 14.150  1.00 24.58 ? 170  PRO A C     1 
ATOM   1271 O O     . PRO A 1 170 ? 10.949  -36.393 13.212  1.00 25.65 ? 170  PRO A O     1 
ATOM   1272 C CB    . PRO A 1 170 ? 12.790  -38.890 13.840  1.00 26.99 ? 170  PRO A CB    1 
ATOM   1273 C CG    . PRO A 1 170 ? 14.084  -39.444 14.359  1.00 25.57 ? 170  PRO A CG    1 
ATOM   1274 C CD    . PRO A 1 170 ? 14.533  -38.441 15.388  1.00 24.22 ? 170  PRO A CD    1 
ATOM   1275 N N     . TYR A 1 171 ? 11.477  -36.213 15.404  1.00 21.16 ? 171  TYR A N     1 
ATOM   1276 C CA    . TYR A 1 171 ? 10.316  -35.388 15.826  1.00 21.48 ? 171  TYR A CA    1 
ATOM   1277 C C     . TYR A 1 171 ? 10.697  -33.900 15.877  1.00 22.63 ? 171  TYR A C     1 
ATOM   1278 O O     . TYR A 1 171 ? 10.112  -33.130 16.653  1.00 22.65 ? 171  TYR A O     1 
ATOM   1279 C CB    . TYR A 1 171 ? 9.749   -35.915 17.150  1.00 22.08 ? 171  TYR A CB    1 
ATOM   1280 C CG    . TYR A 1 171 ? 8.760   -37.063 17.052  1.00 22.51 ? 171  TYR A CG    1 
ATOM   1281 C CD1   . TYR A 1 171 ? 8.943   -38.125 16.184  1.00 21.49 ? 171  TYR A CD1   1 
ATOM   1282 C CD2   . TYR A 1 171 ? 7.620   -37.091 17.852  1.00 23.27 ? 171  TYR A CD2   1 
ATOM   1283 C CE1   . TYR A 1 171 ? 8.043   -39.177 16.100  1.00 23.68 ? 171  TYR A CE1   1 
ATOM   1284 C CE2   . TYR A 1 171 ? 6.729   -38.154 17.810  1.00 23.48 ? 171  TYR A CE2   1 
ATOM   1285 C CZ    . TYR A 1 171 ? 6.936   -39.203 16.929  1.00 23.07 ? 171  TYR A CZ    1 
ATOM   1286 O OH    . TYR A 1 171 ? 6.022   -40.217 16.866  1.00 22.43 ? 171  TYR A OH    1 
ATOM   1287 N N     . GLY A 1 172 ? 11.607  -33.453 15.003  1.00 22.59 ? 172  GLY A N     1 
ATOM   1288 C CA    . GLY A 1 172 ? 12.161  -32.092 15.028  1.00 21.73 ? 172  GLY A CA    1 
ATOM   1289 C C     . GLY A 1 172 ? 11.151  -31.021 14.665  1.00 21.59 ? 172  GLY A C     1 
ATOM   1290 O O     . GLY A 1 172 ? 11.303  -29.896 15.126  1.00 23.02 ? 172  GLY A O     1 
ATOM   1291 N N     . ASP A 1 173 ? 10.131  -31.333 13.867  1.00 23.03 ? 173  ASP A N     1 
ATOM   1292 C CA    . ASP A 1 173 ? 9.112   -30.339 13.457  1.00 22.14 ? 173  ASP A CA    1 
ATOM   1293 C C     . ASP A 1 173 ? 8.078   -30.266 14.583  1.00 22.50 ? 173  ASP A C     1 
ATOM   1294 O O     . ASP A 1 173 ? 7.194   -31.109 14.627  1.00 22.13 ? 173  ASP A O     1 
ATOM   1295 C CB    . ASP A 1 173 ? 8.481   -30.711 12.119  1.00 24.93 ? 173  ASP A CB    1 
ATOM   1296 C CG    . ASP A 1 173 ? 7.477   -29.674 11.653  1.00 28.40 ? 173  ASP A CG    1 
ATOM   1297 O OD1   . ASP A 1 173 ? 7.025   -28.861 12.498  1.00 27.68 ? 173  ASP A OD1   1 
ATOM   1298 O OD2   . ASP A 1 173 ? 7.151   -29.684 10.467  1.00 29.49 ? 173  ASP A OD2   1 
ATOM   1299 N N     . HIS A 1 174 ? 8.238   -29.321 15.505  1.00 20.72 ? 174  HIS A N     1 
ATOM   1300 C CA    . HIS A 1 174 ? 7.443   -29.300 16.766  1.00 23.39 ? 174  HIS A CA    1 
ATOM   1301 C C     . HIS A 1 174 ? 5.956   -29.115 16.457  1.00 24.81 ? 174  HIS A C     1 
ATOM   1302 O O     . HIS A 1 174 ? 5.113   -29.818 17.058  1.00 24.75 ? 174  HIS A O     1 
ATOM   1303 C CB    . HIS A 1 174 ? 8.015   -28.227 17.679  1.00 22.28 ? 174  HIS A CB    1 
ATOM   1304 C CG    . HIS A 1 174 ? 9.360   -28.598 18.183  1.00 22.41 ? 174  HIS A CG    1 
ATOM   1305 N ND1   . HIS A 1 174 ? 10.165  -27.708 18.857  1.00 23.03 ? 174  HIS A ND1   1 
ATOM   1306 C CD2   . HIS A 1 174 ? 10.032  -29.763 18.138  1.00 24.17 ? 174  HIS A CD2   1 
ATOM   1307 C CE1   . HIS A 1 174 ? 11.276  -28.322 19.203  1.00 27.44 ? 174  HIS A CE1   1 
ATOM   1308 N NE2   . HIS A 1 174 ? 11.217  -29.581 18.784  1.00 24.39 ? 174  HIS A NE2   1 
ATOM   1309 N N     . PHE A 1 175 ? 5.626   -28.246 15.506  1.00 24.14 ? 175  PHE A N     1 
ATOM   1310 C CA    . PHE A 1 175 ? 4.211   -27.973 15.178  1.00 26.62 ? 175  PHE A CA    1 
ATOM   1311 C C     . PHE A 1 175 ? 3.601   -29.246 14.595  1.00 25.18 ? 175  PHE A C     1 
ATOM   1312 O O     . PHE A 1 175 ? 2.464   -29.533 14.935  1.00 25.70 ? 175  PHE A O     1 
ATOM   1313 C CB    . PHE A 1 175 ? 4.019   -26.787 14.235  1.00 28.23 ? 175  PHE A CB    1 
ATOM   1314 C CG    . PHE A 1 175 ? 2.594   -26.739 13.749  1.00 30.13 ? 175  PHE A CG    1 
ATOM   1315 C CD1   . PHE A 1 175 ? 1.568   -26.412 14.626  1.00 32.54 ? 175  PHE A CD1   1 
ATOM   1316 C CD2   . PHE A 1 175 ? 2.251   -27.212 12.496  1.00 32.22 ? 175  PHE A CD2   1 
ATOM   1317 C CE1   . PHE A 1 175 ? 0.249   -26.443 14.215  1.00 29.49 ? 175  PHE A CE1   1 
ATOM   1318 C CE2   . PHE A 1 175 ? 0.922   -27.283 12.098  1.00 31.61 ? 175  PHE A CE2   1 
ATOM   1319 C CZ    . PHE A 1 175 ? -0.078  -26.875 12.954  1.00 28.89 ? 175  PHE A CZ    1 
ATOM   1320 N N     . MET A 1 176 ? 4.340   -29.989 13.756  1.00 22.67 ? 176  MET A N     1 
ATOM   1321 C CA    . MET A 1 176 ? 3.854   -31.257 13.154  1.00 23.94 ? 176  MET A CA    1 
ATOM   1322 C C     . MET A 1 176 ? 3.366   -32.173 14.270  1.00 23.33 ? 176  MET A C     1 
ATOM   1323 O O     . MET A 1 176 ? 2.301   -32.744 14.114  1.00 23.44 ? 176  MET A O     1 
ATOM   1324 C CB    . MET A 1 176 ? 4.937   -31.962 12.331  1.00 27.31 ? 176  MET A CB    1 
ATOM   1325 C CG    . MET A 1 176 ? 4.630   -33.446 11.976  1.00 33.82 ? 176  MET A CG    1 
ATOM   1326 S SD    . MET A 1 176 ? 5.948   -34.152 10.902  1.00 38.29 ? 176  MET A SD    1 
ATOM   1327 C CE    . MET A 1 176 ? 5.692   -33.164 9.424   1.00 42.45 ? 176  MET A CE    1 
ATOM   1328 N N     . TRP A 1 177 ? 4.100   -32.270 15.383  1.00 21.25 ? 177  TRP A N     1 
ATOM   1329 C CA    . TRP A 1 177 ? 3.794   -33.274 16.432  1.00 19.38 ? 177  TRP A CA    1 
ATOM   1330 C C     . TRP A 1 177 ? 2.842   -32.680 17.469  1.00 19.47 ? 177  TRP A C     1 
ATOM   1331 O O     . TRP A 1 177 ? 2.323   -33.438 18.279  1.00 19.25 ? 177  TRP A O     1 
ATOM   1332 C CB    . TRP A 1 177 ? 5.098   -33.834 17.016  1.00 20.05 ? 177  TRP A CB    1 
ATOM   1333 C CG    . TRP A 1 177 ? 5.847   -34.582 15.959  1.00 20.32 ? 177  TRP A CG    1 
ATOM   1334 C CD1   . TRP A 1 177 ? 6.966   -34.172 15.311  1.00 21.78 ? 177  TRP A CD1   1 
ATOM   1335 C CD2   . TRP A 1 177 ? 5.399   -35.765 15.279  1.00 22.88 ? 177  TRP A CD2   1 
ATOM   1336 N NE1   . TRP A 1 177 ? 7.272   -35.043 14.305  1.00 23.41 ? 177  TRP A NE1   1 
ATOM   1337 C CE2   . TRP A 1 177 ? 6.345   -36.049 14.283  1.00 22.91 ? 177  TRP A CE2   1 
ATOM   1338 C CE3   . TRP A 1 177 ? 4.328   -36.652 15.457  1.00 23.90 ? 177  TRP A CE3   1 
ATOM   1339 C CZ2   . TRP A 1 177 ? 6.233   -37.169 13.452  1.00 26.56 ? 177  TRP A CZ2   1 
ATOM   1340 C CZ3   . TRP A 1 177 ? 4.222   -37.760 14.645  1.00 26.17 ? 177  TRP A CZ3   1 
ATOM   1341 C CH2   . TRP A 1 177 ? 5.172   -38.024 13.663  1.00 27.32 ? 177  TRP A CH2   1 
ATOM   1342 N N     . GLN A 1 178 ? 2.620   -31.362 17.442  1.00 21.02 ? 178  GLN A N     1 
ATOM   1343 C CA    . GLN A 1 178 ? 1.556   -30.731 18.270  1.00 22.08 ? 178  GLN A CA    1 
ATOM   1344 C C     . GLN A 1 178 ? 0.223   -31.408 17.911  1.00 21.27 ? 178  GLN A C     1 
ATOM   1345 O O     . GLN A 1 178 ? -0.087  -31.544 16.738  1.00 19.79 ? 178  GLN A O     1 
ATOM   1346 C CB    . GLN A 1 178 ? 1.496   -29.218 18.073  1.00 22.69 ? 178  GLN A CB    1 
ATOM   1347 C CG    . GLN A 1 178 ? 0.326   -28.585 18.823  1.00 22.96 ? 178  GLN A CG    1 
ATOM   1348 C CD    . GLN A 1 178 ? -0.934  -28.431 18.012  1.00 26.78 ? 178  GLN A CD    1 
ATOM   1349 O OE1   . GLN A 1 178 ? -0.873  -28.155 16.817  1.00 27.15 ? 178  GLN A OE1   1 
ATOM   1350 N NE2   . GLN A 1 178 ? -2.089  -28.523 18.675  1.00 25.15 ? 178  GLN A NE2   1 
ATOM   1351 N N     . THR A 1 179 ? -0.508  -31.876 18.916  1.00 20.90 ? 179  THR A N     1 
ATOM   1352 C CA    . THR A 1 179 ? -1.767  -32.624 18.713  1.00 20.60 ? 179  THR A CA    1 
ATOM   1353 C C     . THR A 1 179 ? -2.773  -32.164 19.760  1.00 18.70 ? 179  THR A C     1 
ATOM   1354 O O     . THR A 1 179 ? -2.615  -32.564 20.918  1.00 19.82 ? 179  THR A O     1 
ATOM   1355 C CB    . THR A 1 179 ? -1.509  -34.139 18.761  1.00 20.71 ? 179  THR A CB    1 
ATOM   1356 O OG1   . THR A 1 179 ? -0.371  -34.468 17.956  1.00 21.38 ? 179  THR A OG1   1 
ATOM   1357 C CG2   . THR A 1 179 ? -2.717  -34.911 18.275  1.00 21.05 ? 179  THR A CG2   1 
ATOM   1358 N N     . GLY A 1 180 ? -3.741  -31.353 19.364  1.00 20.48 ? 180  GLY A N     1 
ATOM   1359 C CA    . GLY A 1 180 ? -4.725  -30.787 20.300  1.00 19.55 ? 180  GLY A CA    1 
ATOM   1360 C C     . GLY A 1 180 ? -4.197  -29.541 21.016  1.00 18.80 ? 180  GLY A C     1 
ATOM   1361 O O     . GLY A 1 180 ? -2.999  -29.504 21.421  1.00 19.08 ? 180  GLY A O     1 
ATOM   1362 N N     . MET A 1 181 ? -5.100  -28.580 21.183  1.00 19.54 ? 181  MET A N     1 
ATOM   1363 C CA    . MET A 1 181 ? -4.915  -27.315 21.914  1.00 20.90 ? 181  MET A CA    1 
ATOM   1364 C C     . MET A 1 181 ? -6.176  -26.975 22.683  1.00 19.84 ? 181  MET A C     1 
ATOM   1365 O O     . MET A 1 181 ? -7.282  -27.128 22.094  1.00 20.64 ? 181  MET A O     1 
ATOM   1366 C CB    . MET A 1 181 ? -4.851  -26.199 20.881  1.00 26.96 ? 181  MET A CB    1 
ATOM   1367 C CG    . MET A 1 181 ? -3.611  -25.650 20.709  1.00 32.40 ? 181  MET A CG    1 
ATOM   1368 S SD    . MET A 1 181 ? -3.931  -24.320 19.502  1.00 26.56 ? 181  MET A SD    1 
ATOM   1369 C CE    . MET A 1 181 ? -2.322  -24.613 18.778  1.00 26.93 ? 181  MET A CE    1 
ATOM   1370 N N     . GLU A 1 182 ? -5.982  -26.277 23.793  1.00 19.95 ? 182  GLU A N     1 
ATOM   1371 C CA    . GLU A 1 182 ? -7.028  -25.442 24.434  1.00 19.08 ? 182  GLU A CA    1 
ATOM   1372 C C     . GLU A 1 182 ? -6.571  -24.003 24.281  1.00 18.37 ? 182  GLU A C     1 
ATOM   1373 O O     . GLU A 1 182 ? -5.392  -23.696 24.560  1.00 18.92 ? 182  GLU A O     1 
ATOM   1374 C CB    . GLU A 1 182 ? -7.219  -25.789 25.906  1.00 19.85 ? 182  GLU A CB    1 
ATOM   1375 C CG    . GLU A 1 182 ? -8.393  -25.068 26.550  1.00 19.39 ? 182  GLU A CG    1 
ATOM   1376 C CD    . GLU A 1 182 ? -8.516  -25.500 27.999  1.00 23.87 ? 182  GLU A CD    1 
ATOM   1377 O OE1   . GLU A 1 182 ? -7.727  -25.015 28.800  1.00 23.93 ? 182  GLU A OE1   1 
ATOM   1378 O OE2   . GLU A 1 182 ? -9.289  -26.443 28.265  1.00 23.23 ? 182  GLU A OE2   1 
ATOM   1379 N N     . VAL A 1 183 ? -7.450  -23.164 23.764  1.00 20.00 ? 183  VAL A N     1 
ATOM   1380 C CA    . VAL A 1 183 ? -7.077  -21.778 23.427  1.00 20.31 ? 183  VAL A CA    1 
ATOM   1381 C C     . VAL A 1 183 ? -8.181  -20.823 23.853  1.00 19.12 ? 183  VAL A C     1 
ATOM   1382 O O     . VAL A 1 183 ? -9.375  -21.119 23.637  1.00 19.86 ? 183  VAL A O     1 
ATOM   1383 C CB    . VAL A 1 183 ? -6.731  -21.686 21.925  1.00 20.42 ? 183  VAL A CB    1 
ATOM   1384 C CG1   . VAL A 1 183 ? -7.896  -22.106 21.051  1.00 23.34 ? 183  VAL A CG1   1 
ATOM   1385 C CG2   . VAL A 1 183 ? -6.269  -20.281 21.599  1.00 21.66 ? 183  VAL A CG2   1 
ATOM   1386 N N     . VAL A 1 184 ? -7.768  -19.700 24.453  1.00 17.83 ? 184  VAL A N     1 
ATOM   1387 C CA    . VAL A 1 184 ? -8.697  -18.613 24.827  1.00 19.40 ? 184  VAL A CA    1 
ATOM   1388 C C     . VAL A 1 184 ? -8.665  -17.627 23.659  1.00 19.78 ? 184  VAL A C     1 
ATOM   1389 O O     . VAL A 1 184 ? -7.588  -17.099 23.331  1.00 19.23 ? 184  VAL A O     1 
ATOM   1390 C CB    . VAL A 1 184 ? -8.333  -17.966 26.170  1.00 19.37 ? 184  VAL A CB    1 
ATOM   1391 C CG1   . VAL A 1 184 ? -9.200  -16.750 26.417  1.00 19.79 ? 184  VAL A CG1   1 
ATOM   1392 C CG2   . VAL A 1 184 ? -8.430  -18.982 27.294  1.00 19.15 ? 184  VAL A CG2   1 
ATOM   1393 N N     . LEU A 1 185 ? -9.813  -17.418 23.056  1.00 19.84 ? 185  LEU A N     1 
ATOM   1394 C CA    . LEU A 1 185 ? -9.983  -16.549 21.878  1.00 21.43 ? 185  LEU A CA    1 
ATOM   1395 C C     . LEU A 1 185 ? -10.019 -15.091 22.331  1.00 22.40 ? 185  LEU A C     1 
ATOM   1396 O O     . LEU A 1 185 ? -10.096 -14.801 23.524  1.00 19.92 ? 185  LEU A O     1 
ATOM   1397 C CB    . LEU A 1 185 ? -11.238 -16.989 21.140  1.00 21.26 ? 185  LEU A CB    1 
ATOM   1398 C CG    . LEU A 1 185 ? -11.149 -18.381 20.536  1.00 23.23 ? 185  LEU A CG    1 
ATOM   1399 C CD1   . LEU A 1 185 ? -12.494 -18.752 19.953  1.00 23.61 ? 185  LEU A CD1   1 
ATOM   1400 C CD2   . LEU A 1 185 ? -10.045 -18.442 19.464  1.00 22.53 ? 185  LEU A CD2   1 
ATOM   1401 N N     . PRO A 1 186 ? -9.809  -14.129 21.415  1.00 19.94 ? 186  PRO A N     1 
ATOM   1402 C CA    . PRO A 1 186 ? -9.491  -12.759 21.824  1.00 20.41 ? 186  PRO A CA    1 
ATOM   1403 C C     . PRO A 1 186 ? -10.570 -11.983 22.608  1.00 21.27 ? 186  PRO A C     1 
ATOM   1404 O O     . PRO A 1 186 ? -10.228 -10.961 23.146  1.00 23.28 ? 186  PRO A O     1 
ATOM   1405 C CB    . PRO A 1 186 ? -9.190  -12.060 20.483  1.00 21.02 ? 186  PRO A CB    1 
ATOM   1406 C CG    . PRO A 1 186 ? -8.711  -13.211 19.603  1.00 20.15 ? 186  PRO A CG    1 
ATOM   1407 C CD    . PRO A 1 186 ? -9.652  -14.340 19.968  1.00 22.07 ? 186  PRO A CD    1 
ATOM   1408 N N     . GLN A 1 187 ? -11.805 -12.469 22.654  1.00 22.09 ? 187  GLN A N     1 
ATOM   1409 C CA    . GLN A 1 187 ? -12.869 -11.872 23.516  1.00 22.64 ? 187  GLN A CA    1 
ATOM   1410 C C     . GLN A 1 187 ? -13.083 -12.714 24.780  1.00 22.53 ? 187  GLN A C     1 
ATOM   1411 O O     . GLN A 1 187 ? -13.954 -12.333 25.568  1.00 21.96 ? 187  GLN A O     1 
ATOM   1412 C CB    . GLN A 1 187 ? -14.165 -11.700 22.725  1.00 22.91 ? 187  GLN A CB    1 
ATOM   1413 C CG    . GLN A 1 187 ? -13.993 -10.638 21.649  1.00 22.69 ? 187  GLN A CG    1 
ATOM   1414 C CD    . GLN A 1 187 ? -15.282 -10.394 20.917  1.00 24.82 ? 187  GLN A CD    1 
ATOM   1415 O OE1   . GLN A 1 187 ? -15.587 -11.071 19.944  1.00 30.10 ? 187  GLN A OE1   1 
ATOM   1416 N NE2   . GLN A 1 187 ? -16.032 -9.421  21.395  1.00 26.26 ? 187  GLN A NE2   1 
ATOM   1417 N N     . GLY A 1 188 ? -12.296 -13.772 24.986  1.00 23.02 ? 188  GLY A N     1 
ATOM   1418 C CA    . GLY A 1 188 ? -12.312 -14.558 26.237  1.00 22.86 ? 188  GLY A CA    1 
ATOM   1419 C C     . GLY A 1 188 ? -13.064 -15.890 26.178  1.00 22.10 ? 188  GLY A C     1 
ATOM   1420 O O     . GLY A 1 188 ? -13.067 -16.571 27.196  1.00 21.44 ? 188  GLY A O     1 
ATOM   1421 N N     . ASP A 1 189 ? -13.611 -16.305 25.037  1.00 22.85 ? 189  ASP A N     1 
ATOM   1422 C CA    . ASP A 1 189 ? -14.221 -17.652 24.845  1.00 24.16 ? 189  ASP A CA    1 
ATOM   1423 C C     . ASP A 1 189 ? -13.097 -18.689 24.844  1.00 26.39 ? 189  ASP A C     1 
ATOM   1424 O O     . ASP A 1 189 ? -11.983 -18.342 24.408  1.00 30.08 ? 189  ASP A O     1 
ATOM   1425 C CB    . ASP A 1 189 ? -15.059 -17.690 23.573  1.00 25.77 ? 189  ASP A CB    1 
ATOM   1426 C CG    . ASP A 1 189 ? -16.174 -16.656 23.652  1.00 34.07 ? 189  ASP A CG    1 
ATOM   1427 O OD1   . ASP A 1 189 ? -17.036 -16.848 24.542  1.00 36.95 ? 189  ASP A OD1   1 
ATOM   1428 O OD2   . ASP A 1 189 ? -16.072 -15.581 22.959  1.00 32.68 ? 189  ASP A OD2   1 
ATOM   1429 N N     . VAL A 1 190 ? -13.339 -19.878 25.377  1.00 24.36 ? 190  VAL A N     1 
ATOM   1430 C CA    . VAL A 1 190 ? -12.323 -20.968 25.352  1.00 24.90 ? 190  VAL A CA    1 
ATOM   1431 C C     . VAL A 1 190 ? -12.843 -22.063 24.440  1.00 22.51 ? 190  VAL A C     1 
ATOM   1432 O O     . VAL A 1 190 ? -14.074 -22.395 24.460  1.00 21.60 ? 190  VAL A O     1 
ATOM   1433 C CB    . VAL A 1 190 ? -11.983 -21.601 26.715  1.00 27.97 ? 190  VAL A CB    1 
ATOM   1434 C CG1   . VAL A 1 190 ? -11.067 -20.739 27.531  1.00 39.34 ? 190  VAL A CG1   1 
ATOM   1435 C CG2   . VAL A 1 190 ? -13.227 -21.987 27.504  1.00 26.76 ? 190  VAL A CG2   1 
ATOM   1436 N N     . MET A 1 191 ? -11.928 -22.627 23.683  1.00 22.34 ? 191  MET A N     1 
ATOM   1437 C CA    . MET A 1 191 ? -12.244 -23.714 22.738  1.00 22.43 ? 191  MET A CA    1 
ATOM   1438 C C     . MET A 1 191 ? -11.140 -24.769 22.783  1.00 22.07 ? 191  MET A C     1 
ATOM   1439 O O     . MET A 1 191 ? -9.984  -24.406 23.064  1.00 23.01 ? 191  MET A O     1 
ATOM   1440 C CB    . MET A 1 191 ? -12.366 -23.071 21.362  1.00 25.00 ? 191  MET A CB    1 
ATOM   1441 C CG    . MET A 1 191 ? -11.656 -23.719 20.262  1.00 28.95 ? 191  MET A CG    1 
ATOM   1442 S SD    . MET A 1 191 ? -12.111 -22.821 18.762  1.00 27.18 ? 191  MET A SD    1 
ATOM   1443 C CE    . MET A 1 191 ? -10.483 -22.524 18.080  1.00 31.16 ? 191  MET A CE    1 
ATOM   1444 N N     . ARG A 1 192 ? -11.503 -26.033 22.549  1.00 20.88 ? 192  ARG A N     1 
ATOM   1445 C CA    . ARG A 1 192 ? -10.539 -27.120 22.341  1.00 20.75 ? 192  ARG A CA    1 
ATOM   1446 C C     . ARG A 1 192 ? -10.584 -27.532 20.880  1.00 23.57 ? 192  ARG A C     1 
ATOM   1447 O O     . ARG A 1 192 ? -11.702 -27.654 20.298  1.00 23.76 ? 192  ARG A O     1 
ATOM   1448 C CB    . ARG A 1 192 ? -10.854 -28.305 23.238  1.00 20.79 ? 192  ARG A CB    1 
ATOM   1449 C CG    . ARG A 1 192 ? -10.532 -27.965 24.680  1.00 19.97 ? 192  ARG A CG    1 
ATOM   1450 C CD    . ARG A 1 192 ? -10.752 -29.108 25.620  1.00 22.52 ? 192  ARG A CD    1 
ATOM   1451 N NE    . ARG A 1 192 ? -10.242 -28.784 26.947  1.00 20.81 ? 192  ARG A NE    1 
ATOM   1452 C CZ    . ARG A 1 192 ? -10.070 -29.672 27.915  1.00 23.97 ? 192  ARG A CZ    1 
ATOM   1453 N NH1   . ARG A 1 192 ? -10.464 -30.916 27.748  1.00 23.68 ? 192  ARG A NH1   1 
ATOM   1454 N NH2   . ARG A 1 192 ? -9.588  -29.290 29.086  1.00 24.86 ? 192  ARG A NH2   1 
ATOM   1455 N N     . THR A 1 193 ? -9.413  -27.748 20.314  1.00 22.63 ? 193  THR A N     1 
ATOM   1456 C CA    . THR A 1 193 ? -9.303  -28.133 18.886  1.00 22.31 ? 193  THR A CA    1 
ATOM   1457 C C     . THR A 1 193 ? -9.391  -29.648 18.772  1.00 20.85 ? 193  THR A C     1 
ATOM   1458 O O     . THR A 1 193 ? -9.128  -30.376 19.755  1.00 20.49 ? 193  THR A O     1 
ATOM   1459 C CB    . THR A 1 193 ? -8.019  -27.589 18.239  1.00 21.51 ? 193  THR A CB    1 
ATOM   1460 O OG1   . THR A 1 193 ? -6.877  -28.190 18.842  1.00 21.41 ? 193  THR A OG1   1 
ATOM   1461 C CG2   . THR A 1 193 ? -7.911  -26.088 18.339  1.00 22.07 ? 193  THR A CG2   1 
ATOM   1462 N N     . GLY A 1 194 ? -9.596  -30.111 17.548  1.00 20.20 ? 194  GLY A N     1 
ATOM   1463 C CA    . GLY A 1 194 ? -9.457  -31.532 17.216  1.00 21.74 ? 194  GLY A CA    1 
ATOM   1464 C C     . GLY A 1 194 ? -10.450 -32.379 17.995  1.00 21.13 ? 194  GLY A C     1 
ATOM   1465 O O     . GLY A 1 194 ? -11.628 -31.948 18.194  1.00 20.28 ? 194  GLY A O     1 
ATOM   1466 N N     . MET A 1 195 ? -10.000 -33.557 18.403  1.00 23.88 ? 195  MET A N     1 
ATOM   1467 C CA    . MET A 1 195 ? -10.873 -34.549 19.067  1.00 25.60 ? 195  MET A CA    1 
ATOM   1468 C C     . MET A 1 195 ? -11.186 -34.070 20.492  1.00 26.35 ? 195  MET A C     1 
ATOM   1469 O O     . MET A 1 195 ? -12.123 -34.619 21.104  1.00 23.68 ? 195  MET A O     1 
ATOM   1470 C CB    . MET A 1 195 ? -10.227 -35.927 19.089  1.00 26.30 ? 195  MET A CB    1 
ATOM   1471 C CG    . MET A 1 195 ? -9.896  -36.459 17.702  1.00 27.10 ? 195  MET A CG    1 
ATOM   1472 S SD    . MET A 1 195 ? -11.357 -36.406 16.670  1.00 33.22 ? 195  MET A SD    1 
ATOM   1473 C CE    . MET A 1 195 ? -12.350 -37.689 17.413  1.00 33.53 ? 195  MET A CE    1 
ATOM   1474 N N     . GLY A 1 196 ? -10.481 -33.041 20.983  1.00 25.22 ? 196  GLY A N     1 
ATOM   1475 C CA    . GLY A 1 196 ? -10.764 -32.390 22.279  1.00 24.36 ? 196  GLY A CA    1 
ATOM   1476 C C     . GLY A 1 196 ? -12.106 -31.670 22.300  1.00 23.68 ? 196  GLY A C     1 
ATOM   1477 O O     . GLY A 1 196 ? -12.631 -31.483 23.390  1.00 23.17 ? 196  GLY A O     1 
ATOM   1478 N N     . ALA A 1 197 ? -12.665 -31.294 21.145  1.00 22.05 ? 197  ALA A N     1 
ATOM   1479 C CA    . ALA A 1 197 ? -13.991 -30.642 21.036  1.00 22.24 ? 197  ALA A CA    1 
ATOM   1480 C C     . ALA A 1 197 ? -15.104 -31.649 21.361  1.00 23.25 ? 197  ALA A C     1 
ATOM   1481 O O     . ALA A 1 197 ? -16.235 -31.210 21.558  1.00 23.77 ? 197  ALA A O     1 
ATOM   1482 C CB    . ALA A 1 197 ? -14.195 -30.048 19.676  1.00 21.95 ? 197  ALA A CB    1 
ATOM   1483 N N     . LEU A 1 198 ? -14.802 -32.937 21.358  1.00 25.79 ? 198  LEU A N     1 
ATOM   1484 C CA    . LEU A 1 198 ? -15.774 -34.004 21.698  1.00 25.79 ? 198  LEU A CA    1 
ATOM   1485 C C     . LEU A 1 198 ? -15.685 -34.289 23.187  1.00 25.47 ? 198  LEU A C     1 
ATOM   1486 O O     . LEU A 1 198 ? -14.718 -34.879 23.624  1.00 24.86 ? 198  LEU A O     1 
ATOM   1487 C CB    . LEU A 1 198 ? -15.474 -35.277 20.905  1.00 27.88 ? 198  LEU A CB    1 
ATOM   1488 C CG    . LEU A 1 198 ? -16.566 -36.335 21.010  1.00 28.80 ? 198  LEU A CG    1 
ATOM   1489 C CD1   . LEU A 1 198 ? -17.303 -36.435 19.679  1.00 32.64 ? 198  LEU A CD1   1 
ATOM   1490 C CD2   . LEU A 1 198 ? -15.996 -37.676 21.407  1.00 32.69 ? 198  LEU A CD2   1 
ATOM   1491 N N     . PRO A 1 199 ? -16.684 -33.892 24.014  1.00 27.34 ? 199  PRO A N     1 
ATOM   1492 C CA    . PRO A 1 199 ? -16.601 -34.114 25.457  1.00 27.74 ? 199  PRO A CA    1 
ATOM   1493 C C     . PRO A 1 199 ? -16.343 -35.590 25.747  1.00 23.46 ? 199  PRO A C     1 
ATOM   1494 O O     . PRO A 1 199 ? -16.988 -36.405 25.135  1.00 25.24 ? 199  PRO A O     1 
ATOM   1495 C CB    . PRO A 1 199 ? -17.986 -33.671 25.948  1.00 27.45 ? 199  PRO A CB    1 
ATOM   1496 C CG    . PRO A 1 199 ? -18.364 -32.610 24.961  1.00 29.87 ? 199  PRO A CG    1 
ATOM   1497 C CD    . PRO A 1 199 ? -17.909 -33.184 23.633  1.00 26.20 ? 199  PRO A CD    1 
ATOM   1498 N N     . GLY A 1 200 ? -15.392 -35.874 26.627  1.00 23.39 ? 200  GLY A N     1 
ATOM   1499 C CA    . GLY A 1 200 ? -15.016 -37.234 27.044  1.00 25.67 ? 200  GLY A CA    1 
ATOM   1500 C C     . GLY A 1 200 ? -14.141 -37.967 26.035  1.00 27.52 ? 200  GLY A C     1 
ATOM   1501 O O     . GLY A 1 200 ? -13.890 -39.145 26.241  1.00 29.03 ? 200  GLY A O     1 
ATOM   1502 N N     . SER A 1 201 ? -13.690 -37.333 24.953  1.00 30.29 ? 201  SER A N     1 
ATOM   1503 C CA    . SER A 1 201 ? -12.832 -38.045 23.967  1.00 29.14 ? 201  SER A CA    1 
ATOM   1504 C C     . SER A 1 201 ? -11.564 -38.542 24.657  1.00 29.22 ? 201  SER A C     1 
ATOM   1505 O O     . SER A 1 201 ? -11.080 -37.917 25.582  1.00 25.20 ? 201  SER A O     1 
ATOM   1506 C CB    . SER A 1 201 ? -12.481 -37.222 22.793  1.00 29.40 ? 201  SER A CB    1 
ATOM   1507 O OG    . SER A 1 201 ? -11.721 -36.124 23.197  1.00 37.51 ? 201  SER A OG    1 
ATOM   1508 N N     . THR A 1 202 ? -11.047 -39.646 24.155  1.00 27.58 ? 202  THR A N     1 
ATOM   1509 C CA    . THR A 1 202 ? -9.827  -40.342 24.607  1.00 30.08 ? 202  THR A CA    1 
ATOM   1510 C C     . THR A 1 202 ? -8.738  -40.158 23.545  1.00 27.19 ? 202  THR A C     1 
ATOM   1511 O O     . THR A 1 202 ? -7.683  -40.766 23.661  1.00 32.76 ? 202  THR A O     1 
ATOM   1512 C CB    . THR A 1 202 ? -10.268 -41.781 24.868  1.00 33.06 ? 202  THR A CB    1 
ATOM   1513 O OG1   . THR A 1 202 ? -11.015 -42.225 23.720  1.00 37.49 ? 202  THR A OG1   1 
ATOM   1514 C CG2   . THR A 1 202 ? -11.222 -41.843 26.040  1.00 37.95 ? 202  THR A CG2   1 
ATOM   1515 N N     . THR A 1 203 ? -8.983  -39.309 22.552  1.00 25.56 ? 203  THR A N     1 
ATOM   1516 C CA    . THR A 1 203 ? -8.179  -39.251 21.322  1.00 22.73 ? 203  THR A CA    1 
ATOM   1517 C C     . THR A 1 203 ? -7.610  -37.845 21.082  1.00 22.92 ? 203  THR A C     1 
ATOM   1518 O O     . THR A 1 203 ? -7.048  -37.630 20.006  1.00 21.65 ? 203  THR A O     1 
ATOM   1519 C CB    . THR A 1 203 ? -9.039  -39.689 20.131  1.00 23.40 ? 203  THR A CB    1 
ATOM   1520 O OG1   . THR A 1 203 ? -10.158 -38.811 20.024  1.00 23.92 ? 203  THR A OG1   1 
ATOM   1521 C CG2   . THR A 1 203 ? -9.458  -41.130 20.240  1.00 24.52 ? 203  THR A CG2   1 
ATOM   1522 N N     . TRP A 1 204 ? -7.710  -36.923 22.036  1.00 21.02 ? 204  TRP A N     1 
ATOM   1523 C CA    . TRP A 1 204 ? -7.276  -35.525 21.816  1.00 20.47 ? 204  TRP A CA    1 
ATOM   1524 C C     . TRP A 1 204 ? -5.833  -35.477 21.280  1.00 19.60 ? 204  TRP A C     1 
ATOM   1525 O O     . TRP A 1 204 ? -5.563  -34.651 20.421  1.00 21.86 ? 204  TRP A O     1 
ATOM   1526 C CB    . TRP A 1 204 ? -7.405  -34.722 23.103  1.00 20.45 ? 204  TRP A CB    1 
ATOM   1527 C CG    . TRP A 1 204 ? -7.402  -33.246 22.920  1.00 19.76 ? 204  TRP A CG    1 
ATOM   1528 C CD1   . TRP A 1 204 ? -7.497  -32.529 21.758  1.00 18.17 ? 204  TRP A CD1   1 
ATOM   1529 C CD2   . TRP A 1 204 ? -7.382  -32.288 23.985  1.00 18.09 ? 204  TRP A CD2   1 
ATOM   1530 N NE1   . TRP A 1 204 ? -7.512  -31.193 22.031  1.00 19.00 ? 204  TRP A NE1   1 
ATOM   1531 C CE2   . TRP A 1 204 ? -7.446  -31.017 23.393  1.00 18.29 ? 204  TRP A CE2   1 
ATOM   1532 C CE3   . TRP A 1 204 ? -7.249  -32.395 25.372  1.00 20.25 ? 204  TRP A CE3   1 
ATOM   1533 C CZ2   . TRP A 1 204 ? -7.467  -29.848 24.155  1.00 19.37 ? 204  TRP A CZ2   1 
ATOM   1534 C CZ3   . TRP A 1 204 ? -7.292  -31.237 26.127  1.00 19.46 ? 204  TRP A CZ3   1 
ATOM   1535 C CH2   . TRP A 1 204 ? -7.375  -29.987 25.520  1.00 20.22 ? 204  TRP A CH2   1 
ATOM   1536 N N     . GLN A 1 205 ? -4.937  -36.253 21.855  1.00 20.95 ? 205  GLN A N     1 
ATOM   1537 C CA    . GLN A 1 205 ? -3.486  -36.251 21.547  1.00 22.48 ? 205  GLN A CA    1 
ATOM   1538 C C     . GLN A 1 205 ? -3.129  -37.370 20.554  1.00 21.72 ? 205  GLN A C     1 
ATOM   1539 O O     . GLN A 1 205 ? -1.931  -37.568 20.336  1.00 21.64 ? 205  GLN A O     1 
ATOM   1540 C CB    . GLN A 1 205 ? -2.647  -36.358 22.825  1.00 20.97 ? 205  GLN A CB    1 
ATOM   1541 C CG    . GLN A 1 205 ? -2.394  -35.000 23.488  1.00 20.01 ? 205  GLN A CG    1 
ATOM   1542 C CD    . GLN A 1 205 ? -3.651  -34.345 24.027  1.00 20.33 ? 205  GLN A CD    1 
ATOM   1543 O OE1   . GLN A 1 205 ? -4.247  -34.831 24.990  1.00 20.64 ? 205  GLN A OE1   1 
ATOM   1544 N NE2   . GLN A 1 205 ? -4.121  -33.305 23.340  1.00 17.59 ? 205  GLN A NE2   1 
ATOM   1545 N N     . LEU A 1 206 ? -4.071  -38.031 19.888  1.00 23.77 ? 206  LEU A N     1 
ATOM   1546 C CA    . LEU A 1 206 ? -3.565  -39.084 18.961  1.00 26.88 ? 206  LEU A CA    1 
ATOM   1547 C C     . LEU A 1 206 ? -3.877  -38.835 17.493  1.00 24.34 ? 206  LEU A C     1 
ATOM   1548 O O     . LEU A 1 206 ? -3.333  -39.600 16.685  1.00 26.16 ? 206  LEU A O     1 
ATOM   1549 C CB    . LEU A 1 206 ? -3.953  -40.486 19.410  1.00 31.57 ? 206  LEU A CB    1 
ATOM   1550 C CG    . LEU A 1 206 ? -5.331  -40.664 19.981  1.00 37.92 ? 206  LEU A CG    1 
ATOM   1551 C CD1   . LEU A 1 206 ? -6.276  -40.749 18.805  1.00 48.00 ? 206  LEU A CD1   1 
ATOM   1552 C CD2   . LEU A 1 206 ? -5.428  -41.906 20.860  1.00 35.82 ? 206  LEU A CD2   1 
ATOM   1553 N N     . ILE A 1 207 ? -4.663  -37.823 17.160  1.00 23.20 ? 207  ILE A N     1 
ATOM   1554 C CA    . ILE A 1 207 ? -4.850  -37.361 15.760  1.00 24.12 ? 207  ILE A CA    1 
ATOM   1555 C C     . ILE A 1 207 ? -5.005  -35.851 15.803  1.00 25.27 ? 207  ILE A C     1 
ATOM   1556 O O     . ILE A 1 207 ? -5.668  -35.331 16.688  1.00 23.52 ? 207  ILE A O     1 
ATOM   1557 C CB    . ILE A 1 207 ? -6.039  -38.083 15.096  1.00 27.96 ? 207  ILE A CB    1 
ATOM   1558 C CG1   . ILE A 1 207 ? -6.081  -37.830 13.590  1.00 31.15 ? 207  ILE A CG1   1 
ATOM   1559 C CG2   . ILE A 1 207 ? -7.365  -37.722 15.757  1.00 26.89 ? 207  ILE A CG2   1 
ATOM   1560 C CD1   . ILE A 1 207 ? -4.924  -38.462 12.838  1.00 35.79 ? 207  ILE A CD1   1 
ATOM   1561 N N     . PRO A 1 208 ? -4.305  -35.078 14.950  1.00 25.80 ? 208  PRO A N     1 
ATOM   1562 C CA    . PRO A 1 208 ? -4.385  -33.613 15.057  1.00 26.51 ? 208  PRO A CA    1 
ATOM   1563 C C     . PRO A 1 208 ? -5.717  -32.965 14.655  1.00 27.79 ? 208  PRO A C     1 
ATOM   1564 O O     . PRO A 1 208 ? -5.986  -31.902 15.157  1.00 33.19 ? 208  PRO A O     1 
ATOM   1565 C CB    . PRO A 1 208 ? -3.262  -33.086 14.140  1.00 27.99 ? 208  PRO A CB    1 
ATOM   1566 C CG    . PRO A 1 208 ? -2.849  -34.273 13.276  1.00 26.49 ? 208  PRO A CG    1 
ATOM   1567 C CD    . PRO A 1 208 ? -3.279  -35.529 14.007  1.00 27.57 ? 208  PRO A CD    1 
ATOM   1568 N N     . TYR A 1 209 ? -6.522  -33.576 13.777  1.00 28.52 ? 209  TYR A N     1 
ATOM   1569 C CA    . TYR A 1 209 ? -7.521  -32.861 12.926  1.00 31.97 ? 209  TYR A CA    1 
ATOM   1570 C C     . TYR A 1 209 ? -8.890  -32.585 13.580  1.00 35.33 ? 209  TYR A C     1 
ATOM   1571 O O     . TYR A 1 209 ? -9.359  -31.379 13.571  1.00 51.62 ? 209  TYR A O     1 
ATOM   1572 C CB    . TYR A 1 209 ? -7.709  -33.638 11.631  1.00 33.66 ? 209  TYR A CB    1 
ATOM   1573 C CG    . TYR A 1 209 ? -6.417  -33.866 10.907  1.00 32.08 ? 209  TYR A CG    1 
ATOM   1574 C CD1   . TYR A 1 209 ? -5.543  -32.812 10.668  1.00 31.16 ? 209  TYR A CD1   1 
ATOM   1575 C CD2   . TYR A 1 209 ? -6.046  -35.134 10.499  1.00 36.06 ? 209  TYR A CD2   1 
ATOM   1576 C CE1   . TYR A 1 209 ? -4.344  -33.015 10.018  1.00 34.20 ? 209  TYR A CE1   1 
ATOM   1577 C CE2   . TYR A 1 209 ? -4.854  -35.348 9.826   1.00 38.80 ? 209  TYR A CE2   1 
ATOM   1578 C CZ    . TYR A 1 209 ? -4.003  -34.285 9.581   1.00 39.07 ? 209  TYR A CZ    1 
ATOM   1579 O OH    . TYR A 1 209 ? -2.801  -34.489 8.969   1.00 37.83 ? 209  TYR A OH    1 
ATOM   1580 N N     . GLY A 1 210 ? -9.590  -33.618 14.007  1.00 31.18 ? 210  GLY A N     1 
ATOM   1581 C CA    . GLY A 1 210 ? -11.019 -33.489 14.356  1.00 32.50 ? 210  GLY A CA    1 
ATOM   1582 C C     . GLY A 1 210 ? -11.904 -33.408 13.116  1.00 35.08 ? 210  GLY A C     1 
ATOM   1583 O O     . GLY A 1 210 ? -11.476 -33.821 12.011  1.00 39.00 ? 210  GLY A O     1 
ATOM   1584 N N     . PHE A 1 211 ? -13.106 -32.857 13.275  1.00 31.40 ? 211  PHE A N     1 
ATOM   1585 C CA    . PHE A 1 211 ? -14.138 -32.776 12.212  1.00 27.71 ? 211  PHE A CA    1 
ATOM   1586 C C     . PHE A 1 211 ? -14.240 -31.331 11.761  1.00 23.59 ? 211  PHE A C     1 
ATOM   1587 O O     . PHE A 1 211 ? -14.257 -30.457 12.631  1.00 26.35 ? 211  PHE A O     1 
ATOM   1588 C CB    . PHE A 1 211 ? -15.494 -33.269 12.727  1.00 25.51 ? 211  PHE A CB    1 
ATOM   1589 C CG    . PHE A 1 211 ? -16.600 -33.195 11.712  1.00 23.89 ? 211  PHE A CG    1 
ATOM   1590 C CD1   . PHE A 1 211 ? -16.623 -34.077 10.652  1.00 25.33 ? 211  PHE A CD1   1 
ATOM   1591 C CD2   . PHE A 1 211 ? -17.596 -32.232 11.801  1.00 23.03 ? 211  PHE A CD2   1 
ATOM   1592 C CE1   . PHE A 1 211 ? -17.616 -33.997 9.684   1.00 24.60 ? 211  PHE A CE1   1 
ATOM   1593 C CE2   . PHE A 1 211 ? -18.602 -32.167 10.852  1.00 24.96 ? 211  PHE A CE2   1 
ATOM   1594 C CZ    . PHE A 1 211 ? -18.615 -33.059 9.802   1.00 25.27 ? 211  PHE A CZ    1 
ATOM   1595 N N     . GLY A 1 212 ? -14.348 -31.093 10.456  1.00 21.27 ? 212  GLY A N     1 
ATOM   1596 C CA    . GLY A 1 212 ? -14.443 -29.732 9.903   1.00 22.55 ? 212  GLY A CA    1 
ATOM   1597 C C     . GLY A 1 212 ? -13.073 -29.047 9.761   1.00 20.82 ? 212  GLY A C     1 
ATOM   1598 O O     . GLY A 1 212 ? -12.045 -29.702 9.826   1.00 21.82 ? 212  GLY A O     1 
ATOM   1599 N N     . PRO A 1 213 ? -13.098 -27.691 9.521   1.00 23.38 ? 213  PRO A N     1 
ATOM   1600 C CA    . PRO A 1 213 ? -11.801 -27.044 9.286   1.00 25.10 ? 213  PRO A CA    1 
ATOM   1601 C C     . PRO A 1 213 ? -10.780 -27.239 10.387  1.00 24.98 ? 213  PRO A C     1 
ATOM   1602 O O     . PRO A 1 213 ? -11.139 -27.195 11.533  1.00 24.10 ? 213  PRO A O     1 
ATOM   1603 C CB    . PRO A 1 213 ? -12.159 -25.579 9.141   1.00 26.97 ? 213  PRO A CB    1 
ATOM   1604 C CG    . PRO A 1 213 ? -13.545 -25.570 8.650   1.00 27.31 ? 213  PRO A CG    1 
ATOM   1605 C CD    . PRO A 1 213 ? -14.176 -26.666 9.428   1.00 24.74 ? 213  PRO A CD    1 
ATOM   1606 N N     . TYR A 1 214 ? -9.534  -27.458 10.010  1.00 26.79 ? 214  TYR A N     1 
ATOM   1607 C CA    . TYR A 1 214 ? -8.468  -27.733 10.960  1.00 24.51 ? 214  TYR A CA    1 
ATOM   1608 C C     . TYR A 1 214 ? -7.831  -26.408 11.342  1.00 24.92 ? 214  TYR A C     1 
ATOM   1609 O O     . TYR A 1 214 ? -7.211  -25.754 10.533  1.00 23.19 ? 214  TYR A O     1 
ATOM   1610 C CB    . TYR A 1 214 ? -7.522  -28.779 10.338  1.00 24.52 ? 214  TYR A CB    1 
ATOM   1611 C CG    . TYR A 1 214 ? -6.172  -28.962 10.964  1.00 22.56 ? 214  TYR A CG    1 
ATOM   1612 C CD1   . TYR A 1 214 ? -6.021  -29.194 12.320  1.00 22.24 ? 214  TYR A CD1   1 
ATOM   1613 C CD2   . TYR A 1 214 ? -5.044  -28.954 10.175  1.00 23.45 ? 214  TYR A CD2   1 
ATOM   1614 C CE1   . TYR A 1 214 ? -4.772  -29.372 12.870  1.00 23.78 ? 214  TYR A CE1   1 
ATOM   1615 C CE2   . TYR A 1 214 ? -3.798  -29.133 10.710  1.00 24.38 ? 214  TYR A CE2   1 
ATOM   1616 C CZ    . TYR A 1 214 ? -3.665  -29.341 12.054  1.00 25.17 ? 214  TYR A CZ    1 
ATOM   1617 O OH    . TYR A 1 214 ? -2.410  -29.518 12.543  1.00 25.92 ? 214  TYR A OH    1 
ATOM   1618 N N     . PRO A 1 215 ? -7.974  -26.020 12.607  1.00 22.89 ? 215  PRO A N     1 
ATOM   1619 C CA    . PRO A 1 215 ? -7.544  -24.677 12.990  1.00 22.86 ? 215  PRO A CA    1 
ATOM   1620 C C     . PRO A 1 215 ? -6.227  -24.386 13.699  1.00 20.36 ? 215  PRO A C     1 
ATOM   1621 O O     . PRO A 1 215 ? -5.869  -23.255 13.775  1.00 22.14 ? 215  PRO A O     1 
ATOM   1622 C CB    . PRO A 1 215 ? -8.652  -24.286 13.954  1.00 26.08 ? 215  PRO A CB    1 
ATOM   1623 C CG    . PRO A 1 215 ? -9.045  -25.555 14.622  1.00 22.80 ? 215  PRO A CG    1 
ATOM   1624 C CD    . PRO A 1 215 ? -8.715  -26.685 13.692  1.00 24.71 ? 215  PRO A CD    1 
ATOM   1625 N N     . ASP A 1 216 ? -5.589  -25.390 14.252  1.00 48.31 ? 216  ASP A N     1 
ATOM   1626 C CA    . ASP A 1 216 ? -4.436  -25.250 15.157  1.00 34.28 ? 216  ASP A CA    1 
ATOM   1627 C C     . ASP A 1 216 ? -3.312  -24.398 14.610  1.00 27.91 ? 216  ASP A C     1 
ATOM   1628 O O     . ASP A 1 216 ? -2.750  -23.620 15.314  1.00 23.11 ? 216  ASP A O     1 
ATOM   1629 C CB    . ASP A 1 216 ? -3.871  -26.593 15.496  1.00 42.26 ? 216  ASP A CB    1 
ATOM   1630 C CG    . ASP A 1 216 ? -4.877  -27.486 16.203  1.00 29.97 ? 216  ASP A CG    1 
ATOM   1631 O OD1   . ASP A 1 216 ? -4.583  -27.967 17.308  1.00 26.65 ? 216  ASP A OD1   1 
ATOM   1632 O OD2   . ASP A 1 216 ? -5.959  -27.716 15.650  1.00 24.16 ? 216  ASP A OD2   1 
ATOM   1633 N N     . GLY A 1 217 ? -3.015  -24.558 13.328  1.00 22.84 ? 217  GLY A N     1 
ATOM   1634 C CA    . GLY A 1 217 ? -1.995  -23.758 12.705  1.00 22.03 ? 217  GLY A CA    1 
ATOM   1635 C C     . GLY A 1 217 ? -2.234  -22.267 12.753  1.00 21.06 ? 217  GLY A C     1 
ATOM   1636 O O     . GLY A 1 217 ? -1.299  -21.506 12.735  1.00 21.67 ? 217  GLY A O     1 
ATOM   1637 N N     . MET A 1 218 ? -3.495  -21.882 12.817  1.00 23.19 ? 218  MET A N     1 
ATOM   1638 C CA    . MET A 1 218 ? -3.863  -20.447 12.876  1.00 22.44 ? 218  MET A CA    1 
ATOM   1639 C C     . MET A 1 218 ? -3.455  -19.842 14.224  1.00 20.42 ? 218  MET A C     1 
ATOM   1640 O O     . MET A 1 218 ? -3.459  -18.617 14.322  1.00 19.60 ? 218  MET A O     1 
ATOM   1641 C CB    . MET A 1 218 ? -5.341  -20.211 12.582  1.00 24.05 ? 218  MET A CB    1 
ATOM   1642 C CG    . MET A 1 218 ? -5.681  -20.455 11.091  1.00 26.50 ? 218  MET A CG    1 
ATOM   1643 S SD    . MET A 1 218 ? -4.840  -19.296 9.988   1.00 30.57 ? 218  MET A SD    1 
ATOM   1644 C CE    . MET A 1 218 ? -5.821  -17.828 10.300  1.00 33.08 ? 218  MET A CE    1 
ATOM   1645 N N     . PHE A 1 219 ? -3.071  -20.660 15.201  1.00 19.62 ? 219  PHE A N     1 
ATOM   1646 C CA    . PHE A 1 219 ? -2.609  -20.214 16.544  1.00 18.27 ? 219  PHE A CA    1 
ATOM   1647 C C     . PHE A 1 219 ? -1.085  -20.311 16.670  1.00 19.48 ? 219  PHE A C     1 
ATOM   1648 O O     . PHE A 1 219 ? -0.545  -20.158 17.795  1.00 22.21 ? 219  PHE A O     1 
ATOM   1649 C CB    . PHE A 1 219 ? -3.361  -20.983 17.637  1.00 19.35 ? 219  PHE A CB    1 
ATOM   1650 C CG    . PHE A 1 219 ? -4.852  -20.811 17.542  1.00 21.10 ? 219  PHE A CG    1 
ATOM   1651 C CD1   . PHE A 1 219 ? -5.446  -19.618 17.926  1.00 21.40 ? 219  PHE A CD1   1 
ATOM   1652 C CD2   . PHE A 1 219 ? -5.663  -21.812 17.029  1.00 23.77 ? 219  PHE A CD2   1 
ATOM   1653 C CE1   . PHE A 1 219 ? -6.809  -19.446 17.835  1.00 20.94 ? 219  PHE A CE1   1 
ATOM   1654 C CE2   . PHE A 1 219 ? -7.030  -21.617 16.894  1.00 24.03 ? 219  PHE A CE2   1 
ATOM   1655 C CZ    . PHE A 1 219 ? -7.602  -20.441 17.307  1.00 22.97 ? 219  PHE A CZ    1 
ATOM   1656 N N     . THR A 1 220 ? -0.373  -20.549 15.567  1.00 18.60 ? 220  THR A N     1 
ATOM   1657 C CA    . THR A 1 220 ? 1.120   -20.593 15.516  1.00 19.69 ? 220  THR A CA    1 
ATOM   1658 C C     . THR A 1 220 ? 1.626   -19.366 14.752  1.00 18.45 ? 220  THR A C     1 
ATOM   1659 O O     . THR A 1 220 ? 0.948   -18.906 13.805  1.00 19.07 ? 220  THR A O     1 
ATOM   1660 C CB    . THR A 1 220 ? 1.645   -21.933 14.972  1.00 18.36 ? 220  THR A CB    1 
ATOM   1661 O OG1   . THR A 1 220 ? 1.378   -22.025 13.587  1.00 20.63 ? 220  THR A OG1   1 
ATOM   1662 C CG2   . THR A 1 220 ? 1.027   -23.116 15.667  1.00 22.86 ? 220  THR A CG2   1 
ATOM   1663 N N     . GLN A 1 221 ? 2.682   -18.746 15.277  1.00 20.22 ? 221  GLN A N     1 
ATOM   1664 C CA    . GLN A 1 221 ? 3.165   -17.406 14.840  1.00 20.88 ? 221  GLN A CA    1 
ATOM   1665 C C     . GLN A 1 221 ? 1.956   -16.485 14.703  1.00 19.69 ? 221  GLN A C     1 
ATOM   1666 O O     . GLN A 1 221 ? 1.823   -15.827 13.691  1.00 19.77 ? 221  GLN A O     1 
ATOM   1667 C CB    . GLN A 1 221 ? 3.950   -17.532 13.534  1.00 20.00 ? 221  GLN A CB    1 
ATOM   1668 C CG    . GLN A 1 221 ? 5.208   -18.370 13.669  1.00 20.82 ? 221  GLN A CG    1 
ATOM   1669 C CD    . GLN A 1 221 ? 6.172   -18.091 12.541  1.00 22.86 ? 221  GLN A CD    1 
ATOM   1670 O OE1   . GLN A 1 221 ? 5.850   -17.360 11.615  1.00 23.18 ? 221  GLN A OE1   1 
ATOM   1671 N NE2   . GLN A 1 221 ? 7.348   -18.689 12.615  1.00 21.86 ? 221  GLN A NE2   1 
ATOM   1672 N N     . SER A 1 222 ? 1.132   -16.410 15.749  1.00 20.33 ? 222  SER A N     1 
ATOM   1673 C CA    . SER A 1 222 ? -0.243  -15.895 15.663  1.00 20.59 ? 222  SER A CA    1 
ATOM   1674 C C     . SER A 1 222 ? -0.610  -15.052 16.886  1.00 21.45 ? 222  SER A C     1 
ATOM   1675 O O     . SER A 1 222 ? -0.119  -15.345 18.006  1.00 20.89 ? 222  SER A O     1 
ATOM   1676 C CB    . SER A 1 222 ? -1.180  -17.040 15.494  1.00 22.12 ? 222  SER A CB    1 
ATOM   1677 O OG    . SER A 1 222 ? -2.518  -16.579 15.455  1.00 25.30 ? 222  SER A OG    1 
ATOM   1678 N N     . ASN A 1 223 ? -1.478  -14.071 16.667  1.00 20.57 ? 223  ASN A N     1 
ATOM   1679 C CA    . ASN A 1 223 ? -2.133  -13.295 17.752  1.00 20.80 ? 223  ASN A CA    1 
ATOM   1680 C C     . ASN A 1 223 ? -3.640  -13.586 17.835  1.00 21.28 ? 223  ASN A C     1 
ATOM   1681 O O     . ASN A 1 223 ? -4.358  -12.691 18.237  1.00 22.85 ? 223  ASN A O     1 
ATOM   1682 C CB    . ASN A 1 223 ? -1.829  -11.813 17.596  1.00 20.68 ? 223  ASN A CB    1 
ATOM   1683 C CG    . ASN A 1 223 ? -2.229  -11.249 16.254  1.00 20.41 ? 223  ASN A CG    1 
ATOM   1684 O OD1   . ASN A 1 223 ? -3.043  -11.840 15.561  1.00 22.83 ? 223  ASN A OD1   1 
ATOM   1685 N ND2   . ASN A 1 223 ? -1.656  -10.105 15.897  1.00 22.78 ? 223  ASN A ND2   1 
ATOM   1686 N N     . LEU A 1 224 ? -4.092  -14.779 17.436  1.00 21.58 ? 224  LEU A N     1 
ATOM   1687 C CA    . LEU A 1 224 ? -5.537  -15.124 17.427  1.00 20.89 ? 224  LEU A CA    1 
ATOM   1688 C C     . LEU A 1 224 ? -5.965  -15.776 18.732  1.00 21.03 ? 224  LEU A C     1 
ATOM   1689 O O     . LEU A 1 224 ? -7.162  -16.001 18.863  1.00 22.05 ? 224  LEU A O     1 
ATOM   1690 C CB    . LEU A 1 224 ? -5.889  -16.035 16.254  1.00 20.88 ? 224  LEU A CB    1 
ATOM   1691 C CG    . LEU A 1 224 ? -5.589  -15.450 14.883  1.00 21.38 ? 224  LEU A CG    1 
ATOM   1692 C CD1   . LEU A 1 224 ? -6.067  -16.393 13.792  1.00 23.92 ? 224  LEU A CD1   1 
ATOM   1693 C CD2   . LEU A 1 224 ? -6.211  -14.066 14.734  1.00 21.81 ? 224  LEU A CD2   1 
ATOM   1694 N N     . GLY A 1 225 ? -5.053  -16.081 19.637  1.00 20.37 ? 225  GLY A N     1 
ATOM   1695 C CA    . GLY A 1 225 ? -5.475  -16.796 20.851  1.00 21.13 ? 225  GLY A CA    1 
ATOM   1696 C C     . GLY A 1 225 ? -4.390  -16.912 21.863  1.00 21.28 ? 225  GLY A C     1 
ATOM   1697 O O     . GLY A 1 225 ? -3.184  -16.831 21.504  1.00 22.49 ? 225  GLY A O     1 
ATOM   1698 N N     . ILE A 1 226 ? -4.778  -17.129 23.119  1.00 21.44 ? 226  ILE A N     1 
ATOM   1699 C CA    . ILE A 1 226 ? -3.807  -17.504 24.180  1.00 20.36 ? 226  ILE A CA    1 
ATOM   1700 C C     . ILE A 1 226 ? -3.988  -18.984 24.443  1.00 20.25 ? 226  ILE A C     1 
ATOM   1701 O O     . ILE A 1 226 ? -5.053  -19.375 24.930  1.00 18.53 ? 226  ILE A O     1 
ATOM   1702 C CB    . ILE A 1 226 ? -4.010  -16.645 25.450  1.00 20.55 ? 226  ILE A CB    1 
ATOM   1703 C CG1   . ILE A 1 226 ? -3.830  -15.154 25.155  1.00 20.86 ? 226  ILE A CG1   1 
ATOM   1704 C CG2   . ILE A 1 226 ? -3.089  -17.133 26.557  1.00 20.49 ? 226  ILE A CG2   1 
ATOM   1705 C CD1   . ILE A 1 226 ? -4.055  -14.238 26.337  1.00 20.97 ? 226  ILE A CD1   1 
ATOM   1706 N N     . VAL A 1 227 ? -2.967  -19.782 24.138  1.00 19.30 ? 227  VAL A N     1 
ATOM   1707 C CA    . VAL A 1 227 ? -2.980  -21.247 24.347  1.00 18.97 ? 227  VAL A CA    1 
ATOM   1708 C C     . VAL A 1 227 ? -2.761  -21.544 25.830  1.00 19.22 ? 227  VAL A C     1 
ATOM   1709 O O     . VAL A 1 227 ? -1.836  -21.002 26.404  1.00 19.85 ? 227  VAL A O     1 
ATOM   1710 C CB    . VAL A 1 227 ? -1.947  -21.919 23.435  1.00 18.57 ? 227  VAL A CB    1 
ATOM   1711 C CG1   . VAL A 1 227 ? -1.844  -23.394 23.716  1.00 20.39 ? 227  VAL A CG1   1 
ATOM   1712 C CG2   . VAL A 1 227 ? -2.301  -21.682 21.993  1.00 19.03 ? 227  VAL A CG2   1 
ATOM   1713 N N     . THR A 1 228 ? -3.616  -22.403 26.397  1.00 20.90 ? 228  THR A N     1 
ATOM   1714 C CA    . THR A 1 228 ? -3.610  -22.784 27.825  1.00 20.81 ? 228  THR A CA    1 
ATOM   1715 C C     . THR A 1 228 ? -3.238  -24.242 28.011  1.00 20.33 ? 228  THR A C     1 
ATOM   1716 O O     . THR A 1 228 ? -2.811  -24.628 29.109  1.00 19.21 ? 228  THR A O     1 
ATOM   1717 C CB    . THR A 1 228 ? -4.976  -22.454 28.441  1.00 21.19 ? 228  THR A CB    1 
ATOM   1718 O OG1   . THR A 1 228 ? -6.045  -23.053 27.700  1.00 20.86 ? 228  THR A OG1   1 
ATOM   1719 C CG2   . THR A 1 228 ? -5.199  -20.964 28.461  1.00 22.20 ? 228  THR A CG2   1 
ATOM   1720 N N     . LYS A 1 229 ? -3.435  -25.058 26.985  1.00 19.31 ? 229  LYS A N     1 
ATOM   1721 C CA    . LYS A 1 229 ? -3.048  -26.476 27.005  1.00 20.22 ? 229  LYS A CA    1 
ATOM   1722 C C     . LYS A 1 229 ? -2.663  -26.865 25.580  1.00 19.40 ? 229  LYS A C     1 
ATOM   1723 O O     . LYS A 1 229 ? -3.282  -26.355 24.635  1.00 20.32 ? 229  LYS A O     1 
ATOM   1724 C CB    . LYS A 1 229 ? -4.170  -27.401 27.479  1.00 21.70 ? 229  LYS A CB    1 
ATOM   1725 C CG    . LYS A 1 229 ? -4.744  -27.119 28.863  1.00 22.19 ? 229  LYS A CG    1 
ATOM   1726 C CD    . LYS A 1 229 ? -5.893  -28.070 29.195  1.00 20.98 ? 229  LYS A CD    1 
ATOM   1727 C CE    . LYS A 1 229 ? -6.360  -27.944 30.631  1.00 22.94 ? 229  LYS A CE    1 
ATOM   1728 N NZ    . LYS A 1 229 ? -6.822  -26.566 30.893  1.00 24.75 ? 229  LYS A NZ    1 
ATOM   1729 N N     . MET A 1 230 ? -1.668  -27.733 25.464  1.00 20.21 ? 230  MET A N     1 
ATOM   1730 C CA    . MET A 1 230 ? -1.213  -28.231 24.139  1.00 21.60 ? 230  MET A CA    1 
ATOM   1731 C C     . MET A 1 230 ? -0.705  -29.659 24.296  1.00 21.16 ? 230  MET A C     1 
ATOM   1732 O O     . MET A 1 230 ? 0.041   -29.947 25.223  1.00 21.68 ? 230  MET A O     1 
ATOM   1733 C CB    . MET A 1 230 ? -0.104  -27.340 23.580  1.00 20.15 ? 230  MET A CB    1 
ATOM   1734 C CG    . MET A 1 230 ? 0.197   -27.615 22.121  1.00 20.24 ? 230  MET A CG    1 
ATOM   1735 S SD    . MET A 1 230 ? 1.784   -26.920 21.621  1.00 21.88 ? 230  MET A SD    1 
ATOM   1736 C CE    . MET A 1 230 ? 2.905   -28.204 22.163  1.00 23.68 ? 230  MET A CE    1 
ATOM   1737 N N     . GLY A 1 231 ? -1.172  -30.543 23.429  1.00 21.19 ? 231  GLY A N     1 
ATOM   1738 C CA    . GLY A 1 231 ? -0.689  -31.921 23.363  1.00 20.18 ? 231  GLY A CA    1 
ATOM   1739 C C     . GLY A 1 231 ? 0.480   -31.992 22.404  1.00 22.40 ? 231  GLY A C     1 
ATOM   1740 O O     . GLY A 1 231 ? 0.567   -31.167 21.450  1.00 21.70 ? 231  GLY A O     1 
ATOM   1741 N N     . ILE A 1 232 ? 1.376   -32.918 22.646  1.00 20.81 ? 232  ILE A N     1 
ATOM   1742 C CA    . ILE A 1 232 ? 2.489   -33.174 21.704  1.00 22.47 ? 232  ILE A CA    1 
ATOM   1743 C C     . ILE A 1 232 ? 2.753   -34.673 21.714  1.00 21.04 ? 232  ILE A C     1 
ATOM   1744 O O     . ILE A 1 232 ? 2.788   -35.295 22.802  1.00 21.38 ? 232  ILE A O     1 
ATOM   1745 C CB    . ILE A 1 232 ? 3.722   -32.311 22.052  1.00 23.25 ? 232  ILE A CB    1 
ATOM   1746 C CG1   . ILE A 1 232 ? 4.682   -32.248 20.856  1.00 25.68 ? 232  ILE A CG1   1 
ATOM   1747 C CG2   . ILE A 1 232 ? 4.400   -32.800 23.314  1.00 23.94 ? 232  ILE A CG2   1 
ATOM   1748 C CD1   . ILE A 1 232 ? 5.744   -31.157 20.958  1.00 24.89 ? 232  ILE A CD1   1 
ATOM   1749 N N     . ALA A 1 233 ? 2.919   -35.254 20.541  1.00 19.52 ? 233  ALA A N     1 
ATOM   1750 C CA    . ALA A 1 233 ? 3.406   -36.640 20.403  1.00 20.51 ? 233  ALA A CA    1 
ATOM   1751 C C     . ALA A 1 233 ? 4.879   -36.694 20.855  1.00 21.99 ? 233  ALA A C     1 
ATOM   1752 O O     . ALA A 1 233 ? 5.619   -35.748 20.616  1.00 23.40 ? 233  ALA A O     1 
ATOM   1753 C CB    . ALA A 1 233 ? 3.218   -37.107 18.980  1.00 17.75 ? 233  ALA A CB    1 
ATOM   1754 N N     . LEU A 1 234 ? 5.256   -37.789 21.504  1.00 19.83 ? 234  LEU A N     1 
ATOM   1755 C CA    . LEU A 1 234 ? 6.600   -38.096 22.011  1.00 21.34 ? 234  LEU A CA    1 
ATOM   1756 C C     . LEU A 1 234 ? 7.119   -39.377 21.365  1.00 23.30 ? 234  LEU A C     1 
ATOM   1757 O O     . LEU A 1 234 ? 6.434   -40.406 21.448  1.00 20.32 ? 234  LEU A O     1 
ATOM   1758 C CB    . LEU A 1 234 ? 6.507   -38.235 23.531  1.00 21.69 ? 234  LEU A CB    1 
ATOM   1759 C CG    . LEU A 1 234 ? 6.175   -36.934 24.267  1.00 24.50 ? 234  LEU A CG    1 
ATOM   1760 C CD1   . LEU A 1 234 ? 5.973   -37.182 25.753  1.00 24.71 ? 234  LEU A CD1   1 
ATOM   1761 C CD2   . LEU A 1 234 ? 7.232   -35.867 24.015  1.00 25.32 ? 234  LEU A CD2   1 
ATOM   1762 N N     . MET A 1 235 ? 8.328   -39.321 20.778  1.00 21.96 ? 235  MET A N     1 
ATOM   1763 C CA    . MET A 1 235 ? 8.962   -40.500 20.149  1.00 24.61 ? 235  MET A CA    1 
ATOM   1764 C C     . MET A 1 235 ? 9.439   -41.495 21.215  1.00 23.52 ? 235  MET A C     1 
ATOM   1765 O O     . MET A 1 235 ? 9.960   -41.075 22.270  1.00 23.70 ? 235  MET A O     1 
ATOM   1766 C CB    . MET A 1 235 ? 10.170  -40.072 19.323  1.00 28.34 ? 235  MET A CB    1 
ATOM   1767 C CG    . MET A 1 235 ? 10.542  -41.047 18.247  1.00 30.84 ? 235  MET A CG    1 
ATOM   1768 S SD    . MET A 1 235 ? 11.913  -40.320 17.317  1.00 34.54 ? 235  MET A SD    1 
ATOM   1769 C CE    . MET A 1 235 ? 13.287  -41.009 18.245  1.00 38.84 ? 235  MET A CE    1 
ATOM   1770 N N     . GLN A 1 236 ? 9.324   -42.777 20.907  1.00 26.19 ? 236  GLN A N     1 
ATOM   1771 C CA    . GLN A 1 236 ? 10.006  -43.859 21.660  1.00 25.73 ? 236  GLN A CA    1 
ATOM   1772 C C     . GLN A 1 236 ? 11.522  -43.758 21.462  1.00 26.76 ? 236  GLN A C     1 
ATOM   1773 O O     . GLN A 1 236 ? 11.990  -43.617 20.329  1.00 26.53 ? 236  GLN A O     1 
ATOM   1774 C CB    . GLN A 1 236 ? 9.518   -45.223 21.197  1.00 28.46 ? 236  GLN A CB    1 
ATOM   1775 C CG    . GLN A 1 236 ? 8.250   -45.657 21.895  1.00 29.79 ? 236  GLN A CG    1 
ATOM   1776 C CD    . GLN A 1 236 ? 7.798   -46.975 21.328  1.00 30.97 ? 236  GLN A CD    1 
ATOM   1777 O OE1   . GLN A 1 236 ? 8.615   -47.754 20.851  1.00 33.01 ? 236  GLN A OE1   1 
ATOM   1778 N NE2   . GLN A 1 236 ? 6.499   -47.220 21.402  1.00 31.16 ? 236  GLN A NE2   1 
ATOM   1779 N N     . LYS A 1 237 ? 12.262  -43.846 22.556  1.00 28.37 ? 237  LYS A N     1 
ATOM   1780 C CA    . LYS A 1 237 ? 13.731  -44.029 22.514  1.00 30.22 ? 237  LYS A CA    1 
ATOM   1781 C C     . LYS A 1 237 ? 14.024  -45.269 21.695  1.00 27.68 ? 237  LYS A C     1 
ATOM   1782 O O     . LYS A 1 237 ? 13.437  -46.312 21.928  1.00 25.46 ? 237  LYS A O     1 
ATOM   1783 C CB    . LYS A 1 237 ? 14.321  -44.214 23.910  1.00 32.74 ? 237  LYS A CB    1 
ATOM   1784 C CG    . LYS A 1 237 ? 14.285  -42.967 24.779  1.00 34.38 ? 237  LYS A CG    1 
ATOM   1785 C CD    . LYS A 1 237 ? 14.989  -43.202 26.085  1.00 37.03 ? 237  LYS A CD    1 
ATOM   1786 C CE    . LYS A 1 237 ? 14.798  -42.077 27.075  1.00 39.45 ? 237  LYS A CE    1 
ATOM   1787 N NZ    . LYS A 1 237 ? 15.252  -42.496 28.417  1.00 43.15 ? 237  LYS A NZ    1 
ATOM   1788 N N     . PRO A 1 238 ? 14.904  -45.166 20.689  1.00 30.96 ? 238  PRO A N     1 
ATOM   1789 C CA    . PRO A 1 238 ? 15.394  -46.350 20.005  1.00 31.79 ? 238  PRO A CA    1 
ATOM   1790 C C     . PRO A 1 238 ? 16.316  -47.123 20.942  1.00 29.50 ? 238  PRO A C     1 
ATOM   1791 O O     . PRO A 1 238 ? 16.707  -46.619 21.996  1.00 27.52 ? 238  PRO A O     1 
ATOM   1792 C CB    . PRO A 1 238 ? 16.125  -45.812 18.774  1.00 33.70 ? 238  PRO A CB    1 
ATOM   1793 C CG    . PRO A 1 238 ? 16.452  -44.377 19.110  1.00 37.19 ? 238  PRO A CG    1 
ATOM   1794 C CD    . PRO A 1 238 ? 15.468  -43.913 20.164  1.00 33.70 ? 238  PRO A CD    1 
ATOM   1795 N N     . PRO A 1 239 ? 16.641  -48.387 20.589  1.00 34.58 ? 239  PRO A N     1 
ATOM   1796 C CA    . PRO A 1 239 ? 17.469  -49.242 21.440  1.00 33.39 ? 239  PRO A CA    1 
ATOM   1797 C C     . PRO A 1 239 ? 18.914  -48.748 21.585  1.00 31.82 ? 239  PRO A C     1 
ATOM   1798 O O     . PRO A 1 239 ? 19.533  -49.012 22.594  1.00 32.71 ? 239  PRO A O     1 
ATOM   1799 C CB    . PRO A 1 239 ? 17.445  -50.621 20.756  1.00 36.10 ? 239  PRO A CB    1 
ATOM   1800 C CG    . PRO A 1 239 ? 16.964  -50.354 19.326  1.00 37.28 ? 239  PRO A CG    1 
ATOM   1801 C CD    . PRO A 1 239 ? 16.150  -49.075 19.383  1.00 35.53 ? 239  PRO A CD    1 
ATOM   1802 N N     . ALA A 1 240 ? 19.412  -48.015 20.596  1.00 30.04 ? 240  ALA A N     1 
ATOM   1803 C CA    . ALA A 1 240 ? 20.760  -47.414 20.610  1.00 30.82 ? 240  ALA A CA    1 
ATOM   1804 C C     . ALA A 1 240 ? 20.795  -46.227 19.658  1.00 29.32 ? 240  ALA A C     1 
ATOM   1805 O O     . ALA A 1 240 ? 19.898  -46.102 18.815  1.00 32.27 ? 240  ALA A O     1 
ATOM   1806 C CB    . ALA A 1 240 ? 21.777  -48.455 20.193  1.00 30.53 ? 240  ALA A CB    1 
ATOM   1807 N N     . SER A 1 241 ? 21.826  -45.404 19.787  1.00 29.61 ? 241  SER A N     1 
ATOM   1808 C CA    . SER A 1 241 ? 22.061  -44.240 18.902  1.00 29.09 ? 241  SER A CA    1 
ATOM   1809 C C     . SER A 1 241 ? 23.564  -43.987 18.800  1.00 28.80 ? 241  SER A C     1 
ATOM   1810 O O     . SER A 1 241 ? 24.337  -44.362 19.720  1.00 31.45 ? 241  SER A O     1 
ATOM   1811 C CB    . SER A 1 241 ? 21.277  -43.013 19.359  1.00 28.63 ? 241  SER A CB    1 
ATOM   1812 O OG    . SER A 1 241 ? 21.880  -42.356 20.455  1.00 31.52 ? 241  SER A OG    1 
ATOM   1813 N N     . MET A 1 242 ? 23.970  -43.380 17.705  1.00 28.28 ? 242  MET A N     1 
ATOM   1814 C CA    . MET A 1 242 ? 25.355  -42.907 17.531  1.00 28.16 ? 242  MET A CA    1 
ATOM   1815 C C     . MET A 1 242 ? 25.286  -41.591 16.772  1.00 26.37 ? 242  MET A C     1 
ATOM   1816 O O     . MET A 1 242 ? 24.460  -41.488 15.814  1.00 26.90 ? 242  MET A O     1 
ATOM   1817 C CB    . MET A 1 242 ? 26.171  -43.945 16.754  1.00 31.85 ? 242  MET A CB    1 
ATOM   1818 C CG    . MET A 1 242 ? 27.634  -43.553 16.570  1.00 35.71 ? 242  MET A CG    1 
ATOM   1819 S SD    . MET A 1 242 ? 27.849  -42.492 15.117  1.00 36.97 ? 242  MET A SD    1 
ATOM   1820 C CE    . MET A 1 242 ? 27.684  -43.722 13.826  1.00 39.82 ? 242  MET A CE    1 
ATOM   1821 N N     . THR A 1 243 ? 26.086  -40.619 17.220  1.00 27.58 ? 243  THR A N     1 
ATOM   1822 C CA    . THR A 1 243 ? 26.233  -39.286 16.599  1.00 29.76 ? 243  THR A CA    1 
ATOM   1823 C C     . THR A 1 243 ? 27.622  -39.200 15.973  1.00 30.52 ? 243  THR A C     1 
ATOM   1824 O O     . THR A 1 243 ? 28.606  -39.627 16.611  1.00 28.24 ? 243  THR A O     1 
ATOM   1825 C CB    . THR A 1 243 ? 25.938  -38.173 17.604  1.00 29.91 ? 243  THR A CB    1 
ATOM   1826 O OG1   . THR A 1 243 ? 24.633  -38.450 18.095  1.00 28.08 ? 243  THR A OG1   1 
ATOM   1827 C CG2   . THR A 1 243 ? 25.987  -36.792 16.990  1.00 31.34 ? 243  THR A CG2   1 
ATOM   1828 N N     . TYR A 1 244 ? 27.692  -38.671 14.759  1.00 28.74 ? 244  TYR A N     1 
ATOM   1829 C CA    . TYR A 1 244 ? 28.970  -38.532 14.028  1.00 27.85 ? 244  TYR A CA    1 
ATOM   1830 C C     . TYR A 1 244 ? 29.131  -37.085 13.565  1.00 30.54 ? 244  TYR A C     1 
ATOM   1831 O O     . TYR A 1 244 ? 28.130  -36.362 13.337  1.00 29.56 ? 244  TYR A O     1 
ATOM   1832 C CB    . TYR A 1 244 ? 29.012  -39.520 12.863  1.00 27.12 ? 244  TYR A CB    1 
ATOM   1833 C CG    . TYR A 1 244 ? 27.860  -39.340 11.922  1.00 26.83 ? 244  TYR A CG    1 
ATOM   1834 C CD1   . TYR A 1 244 ? 26.623  -39.913 12.179  1.00 26.07 ? 244  TYR A CD1   1 
ATOM   1835 C CD2   . TYR A 1 244 ? 27.989  -38.532 10.809  1.00 29.53 ? 244  TYR A CD2   1 
ATOM   1836 C CE1   . TYR A 1 244 ? 25.546  -39.704 11.334  1.00 27.25 ? 244  TYR A CE1   1 
ATOM   1837 C CE2   . TYR A 1 244 ? 26.917  -38.312 9.962   1.00 27.13 ? 244  TYR A CE2   1 
ATOM   1838 C CZ    . TYR A 1 244 ? 25.694  -38.901 10.226  1.00 26.79 ? 244  TYR A CZ    1 
ATOM   1839 O OH    . TYR A 1 244 ? 24.647  -38.667 9.390   1.00 26.32 ? 244  TYR A OH    1 
ATOM   1840 N N     . GLN A 1 245 ? 30.398  -36.709 13.397  1.00 30.25 ? 245  GLN A N     1 
ATOM   1841 C CA    . GLN A 1 245 ? 30.867  -35.425 12.831  1.00 28.73 ? 245  GLN A CA    1 
ATOM   1842 C C     . GLN A 1 245 ? 31.596  -35.725 11.518  1.00 31.20 ? 245  GLN A C     1 
ATOM   1843 O O     . GLN A 1 245 ? 32.466  -36.594 11.508  1.00 30.79 ? 245  GLN A O     1 
ATOM   1844 C CB    . GLN A 1 245 ? 31.813  -34.764 13.826  1.00 28.90 ? 245  GLN A CB    1 
ATOM   1845 C CG    . GLN A 1 245 ? 32.548  -33.544 13.297  1.00 30.14 ? 245  GLN A CG    1 
ATOM   1846 C CD    . GLN A 1 245 ? 33.679  -33.178 14.225  1.00 29.25 ? 245  GLN A CD    1 
ATOM   1847 O OE1   . GLN A 1 245 ? 34.634  -33.939 14.387  1.00 31.16 ? 245  GLN A OE1   1 
ATOM   1848 N NE2   . GLN A 1 245 ? 33.569  -32.017 14.852  1.00 30.14 ? 245  GLN A NE2   1 
ATOM   1849 N N     . ILE A 1 246 ? 31.219  -35.044 10.441  1.00 29.98 ? 246  ILE A N     1 
ATOM   1850 C CA    . ILE A 1 246 ? 32.051  -35.006 9.211   1.00 28.53 ? 246  ILE A CA    1 
ATOM   1851 C C     . ILE A 1 246 ? 32.602  -33.591 9.054   1.00 29.05 ? 246  ILE A C     1 
ATOM   1852 O O     . ILE A 1 246 ? 31.792  -32.637 8.972   1.00 29.75 ? 246  ILE A O     1 
ATOM   1853 C CB    . ILE A 1 246 ? 31.270  -35.424 7.964   1.00 28.00 ? 246  ILE A CB    1 
ATOM   1854 C CG1   . ILE A 1 246 ? 30.207  -36.492 8.241   1.00 28.13 ? 246  ILE A CG1   1 
ATOM   1855 C CG2   . ILE A 1 246 ? 32.264  -35.847 6.891   1.00 28.71 ? 246  ILE A CG2   1 
ATOM   1856 C CD1   . ILE A 1 246 ? 29.356  -36.778 7.037   1.00 28.00 ? 246  ILE A CD1   1 
ATOM   1857 N N     . THR A 1 247 ? 33.931  -33.454 9.068   1.00 30.76 ? 247  THR A N     1 
ATOM   1858 C CA    . THR A 1 247 ? 34.643  -32.180 8.782   1.00 29.79 ? 247  THR A CA    1 
ATOM   1859 C C     . THR A 1 247 ? 34.925  -32.153 7.284   1.00 32.61 ? 247  THR A C     1 
ATOM   1860 O O     . THR A 1 247 ? 35.305  -33.196 6.726   1.00 30.70 ? 247  THR A O     1 
ATOM   1861 C CB    . THR A 1 247 ? 35.921  -32.023 9.613   1.00 33.10 ? 247  THR A CB    1 
ATOM   1862 O OG1   . THR A 1 247 ? 36.821  -33.096 9.303   1.00 31.28 ? 247  THR A OG1   1 
ATOM   1863 C CG2   . THR A 1 247 ? 35.631  -32.022 11.099  1.00 32.86 ? 247  THR A CG2   1 
ATOM   1864 N N     . PHE A 1 248 ? 34.674  -31.006 6.666   1.00 30.84 ? 248  PHE A N     1 
ATOM   1865 C CA    . PHE A 1 248 ? 34.987  -30.723 5.253   1.00 31.74 ? 248  PHE A CA    1 
ATOM   1866 C C     . PHE A 1 248 ? 35.919  -29.513 5.220   1.00 34.99 ? 248  PHE A C     1 
ATOM   1867 O O     . PHE A 1 248 ? 35.611  -28.477 5.858   1.00 35.25 ? 248  PHE A O     1 
ATOM   1868 C CB    . PHE A 1 248 ? 33.690  -30.475 4.484   1.00 31.25 ? 248  PHE A CB    1 
ATOM   1869 C CG    . PHE A 1 248 ? 32.745  -31.645 4.465   1.00 30.85 ? 248  PHE A CG    1 
ATOM   1870 C CD1   . PHE A 1 248 ? 32.902  -32.667 3.544   1.00 28.89 ? 248  PHE A CD1   1 
ATOM   1871 C CD2   . PHE A 1 248 ? 31.682  -31.713 5.352   1.00 27.50 ? 248  PHE A CD2   1 
ATOM   1872 C CE1   . PHE A 1 248 ? 32.020  -33.740 3.523   1.00 30.35 ? 248  PHE A CE1   1 
ATOM   1873 C CE2   . PHE A 1 248 ? 30.803  -32.786 5.322   1.00 28.22 ? 248  PHE A CE2   1 
ATOM   1874 C CZ    . PHE A 1 248 ? 30.964  -33.790 4.393   1.00 29.74 ? 248  PHE A CZ    1 
ATOM   1875 N N     . GLU A 1 249 ? 37.035  -29.637 4.502   1.00 36.80 ? 249  GLU A N     1 
ATOM   1876 C CA    . GLU A 1 249 ? 38.160  -28.668 4.571   1.00 35.70 ? 249  GLU A CA    1 
ATOM   1877 C C     . GLU A 1 249 ? 37.757  -27.347 3.916   1.00 31.34 ? 249  GLU A C     1 
ATOM   1878 O O     . GLU A 1 249 ? 38.091  -26.323 4.484   1.00 34.07 ? 249  GLU A O     1 
ATOM   1879 C CB    . GLU A 1 249 ? 39.407  -29.243 3.896   1.00 41.17 ? 249  GLU A CB    1 
ATOM   1880 C CG    . GLU A 1 249 ? 39.999  -30.415 4.655   1.00 48.16 ? 249  GLU A CG    1 
ATOM   1881 C CD    . GLU A 1 249 ? 41.377  -30.889 4.215   1.00 59.78 ? 249  GLU A CD    1 
ATOM   1882 O OE1   . GLU A 1 249 ? 41.804  -30.589 3.072   1.00 66.81 ? 249  GLU A OE1   1 
ATOM   1883 O OE2   . GLU A 1 249 ? 42.016  -31.592 5.016   1.00 67.52 ? 249  GLU A OE2   1 
ATOM   1884 N N     . ASN A 1 250 ? 37.068  -27.374 2.779   1.00 30.71 ? 250  ASN A N     1 
ATOM   1885 C CA    . ASN A 1 250 ? 36.951  -26.217 1.863   1.00 32.57 ? 250  ASN A CA    1 
ATOM   1886 C C     . ASN A 1 250 ? 35.575  -25.566 1.983   1.00 34.15 ? 250  ASN A C     1 
ATOM   1887 O O     . ASN A 1 250 ? 34.569  -26.290 1.956   1.00 32.62 ? 250  ASN A O     1 
ATOM   1888 C CB    . ASN A 1 250 ? 37.203  -26.654 0.424   1.00 32.61 ? 250  ASN A CB    1 
ATOM   1889 C CG    . ASN A 1 250 ? 38.491  -27.440 0.334   1.00 35.89 ? 250  ASN A CG    1 
ATOM   1890 O OD1   . ASN A 1 250 ? 39.541  -26.959 0.757   1.00 36.02 ? 250  ASN A OD1   1 
ATOM   1891 N ND2   . ASN A 1 250 ? 38.400  -28.668 -0.141  1.00 36.77 ? 250  ASN A ND2   1 
ATOM   1892 N N     . GLU A 1 251 ? 35.535  -24.242 2.038   1.00 32.16 ? 251  GLU A N     1 
ATOM   1893 C CA    . GLU A 1 251 ? 34.246  -23.514 2.031   1.00 36.47 ? 251  GLU A CA    1 
ATOM   1894 C C     . GLU A 1 251 ? 33.471  -23.917 0.772   1.00 35.68 ? 251  GLU A C     1 
ATOM   1895 O O     . GLU A 1 251 ? 32.236  -24.056 0.867   1.00 33.83 ? 251  GLU A O     1 
ATOM   1896 C CB    . GLU A 1 251 ? 34.480  -22.024 2.254   1.00 41.67 ? 251  GLU A CB    1 
ATOM   1897 C CG    . GLU A 1 251 ? 35.215  -21.305 1.168   1.00 43.72 ? 251  GLU A CG    1 
ATOM   1898 C CD    . GLU A 1 251 ? 35.382  -19.831 1.509   1.00 42.57 ? 251  GLU A CD    1 
ATOM   1899 O OE1   . GLU A 1 251 ? 35.853  -19.512 2.634   1.00 40.24 ? 251  GLU A OE1   1 
ATOM   1900 O OE2   . GLU A 1 251 ? 35.023  -19.017 0.660   1.00 44.12 ? 251  GLU A OE2   1 
ATOM   1901 N N     . SER A 1 252 ? 34.154  -24.204 -0.343  1.00 31.97 ? 252  SER A N     1 
ATOM   1902 C CA    . SER A 1 252 ? 33.481  -24.570 -1.619  1.00 28.92 ? 252  SER A CA    1 
ATOM   1903 C C     . SER A 1 252 ? 32.920  -26.008 -1.576  1.00 25.97 ? 252  SER A C     1 
ATOM   1904 O O     . SER A 1 252 ? 32.183  -26.362 -2.500  1.00 28.92 ? 252  SER A O     1 
ATOM   1905 C CB    . SER A 1 252 ? 34.413  -24.400 -2.778  1.00 34.30 ? 252  SER A CB    1 
ATOM   1906 O OG    . SER A 1 252 ? 35.481  -25.337 -2.664  1.00 37.38 ? 252  SER A OG    1 
ATOM   1907 N N     . ASP A 1 253 ? 33.207  -26.811 -0.546  1.00 27.59 ? 253  ASP A N     1 
ATOM   1908 C CA    . ASP A 1 253 ? 32.612  -28.173 -0.397  1.00 30.34 ? 253  ASP A CA    1 
ATOM   1909 C C     . ASP A 1 253 ? 31.081  -28.098 -0.181  1.00 29.62 ? 253  ASP A C     1 
ATOM   1910 O O     . ASP A 1 253 ? 30.377  -29.107 -0.447  1.00 30.72 ? 253  ASP A O     1 
ATOM   1911 C CB    . ASP A 1 253 ? 33.267  -28.948 0.744   1.00 31.99 ? 253  ASP A CB    1 
ATOM   1912 C CG    . ASP A 1 253 ? 34.707  -29.366 0.493   1.00 30.34 ? 253  ASP A CG    1 
ATOM   1913 O OD1   . ASP A 1 253 ? 35.083  -29.526 -0.683  1.00 30.86 ? 253  ASP A OD1   1 
ATOM   1914 O OD2   . ASP A 1 253 ? 35.424  -29.537 1.474   1.00 32.23 ? 253  ASP A OD2   1 
ATOM   1915 N N     . LEU A 1 254 ? 30.559  -26.953 0.251   1.00 30.71 ? 254  LEU A N     1 
ATOM   1916 C CA    . LEU A 1 254 ? 29.109  -26.783 0.586   1.00 27.82 ? 254  LEU A CA    1 
ATOM   1917 C C     . LEU A 1 254 ? 28.214  -27.311 -0.547  1.00 26.70 ? 254  LEU A C     1 
ATOM   1918 O O     . LEU A 1 254 ? 27.264  -28.040 -0.260  1.00 26.08 ? 254  LEU A O     1 
ATOM   1919 C CB    . LEU A 1 254 ? 28.841  -25.301 0.839   1.00 25.65 ? 254  LEU A CB    1 
ATOM   1920 C CG    . LEU A 1 254 ? 27.384  -24.928 1.069   1.00 26.86 ? 254  LEU A CG    1 
ATOM   1921 C CD1   . LEU A 1 254 ? 26.861  -25.602 2.341   1.00 25.21 ? 254  LEU A CD1   1 
ATOM   1922 C CD2   . LEU A 1 254 ? 27.239  -23.411 1.126   1.00 26.71 ? 254  LEU A CD2   1 
ATOM   1923 N N     . GLU A 1 255 ? 28.500  -26.939 -1.789  1.00 26.80 ? 255  GLU A N     1 
ATOM   1924 C CA    . GLU A 1 255 ? 27.697  -27.331 -2.964  1.00 29.96 ? 255  GLU A CA    1 
ATOM   1925 C C     . GLU A 1 255 ? 27.551  -28.863 -2.995  1.00 30.82 ? 255  GLU A C     1 
ATOM   1926 O O     . GLU A 1 255 ? 26.404  -29.348 -3.112  1.00 29.18 ? 255  GLU A O     1 
ATOM   1927 C CB    . GLU A 1 255 ? 28.318  -26.835 -4.267  1.00 33.24 ? 255  GLU A CB    1 
ATOM   1928 C CG    . GLU A 1 255 ? 27.449  -27.166 -5.449  1.00 34.30 ? 255  GLU A CG    1 
ATOM   1929 C CD    . GLU A 1 255 ? 27.876  -26.539 -6.755  1.00 41.72 ? 255  GLU A CD    1 
ATOM   1930 O OE1   . GLU A 1 255 ? 28.936  -25.858 -6.775  1.00 48.22 ? 255  GLU A OE1   1 
ATOM   1931 O OE2   . GLU A 1 255 ? 27.116  -26.709 -7.727  1.00 44.75 ? 255  GLU A OE2   1 
ATOM   1932 N N     . GLN A 1 256 ? 28.660  -29.599 -2.893  1.00 28.96 ? 256  GLN A N     1 
ATOM   1933 C CA    . GLN A 1 256 ? 28.619  -31.073 -3.036  1.00 31.15 ? 256  GLN A CA    1 
ATOM   1934 C C     . GLN A 1 256 ? 27.986  -31.700 -1.789  1.00 27.85 ? 256  GLN A C     1 
ATOM   1935 O O     . GLN A 1 256 ? 27.326  -32.749 -1.920  1.00 28.02 ? 256  GLN A O     1 
ATOM   1936 C CB    . GLN A 1 256 ? 30.019  -31.628 -3.306  1.00 34.24 ? 256  GLN A CB    1 
ATOM   1937 C CG    . GLN A 1 256 ? 29.980  -33.106 -3.664  1.00 41.30 ? 256  GLN A CG    1 
ATOM   1938 C CD    . GLN A 1 256 ? 31.213  -33.583 -4.389  1.00 47.33 ? 256  GLN A CD    1 
ATOM   1939 O OE1   . GLN A 1 256 ? 32.197  -32.857 -4.503  1.00 49.70 ? 256  GLN A OE1   1 
ATOM   1940 N NE2   . GLN A 1 256 ? 31.169  -34.826 -4.852  1.00 43.56 ? 256  GLN A NE2   1 
ATOM   1941 N N     . ILE A 1 257 ? 28.214  -31.106 -0.620  1.00 26.60 ? 257  ILE A N     1 
ATOM   1942 C CA    . ILE A 1 257 ? 27.683  -31.623 0.668   1.00 26.71 ? 257  ILE A CA    1 
ATOM   1943 C C     . ILE A 1 257 ? 26.160  -31.597 0.576   1.00 24.79 ? 257  ILE A C     1 
ATOM   1944 O O     . ILE A 1 257 ? 25.550  -32.601 0.883   1.00 24.63 ? 257  ILE A O     1 
ATOM   1945 C CB    . ILE A 1 257 ? 28.168  -30.819 1.881   1.00 25.15 ? 257  ILE A CB    1 
ATOM   1946 C CG1   . ILE A 1 257 ? 29.680  -30.929 2.083   1.00 25.84 ? 257  ILE A CG1   1 
ATOM   1947 C CG2   . ILE A 1 257 ? 27.421  -31.246 3.131   1.00 24.78 ? 257  ILE A CG2   1 
ATOM   1948 C CD1   . ILE A 1 257 ? 30.256  -29.763 2.874   1.00 26.52 ? 257  ILE A CD1   1 
ATOM   1949 N N     . VAL A 1 258 ? 25.595  -30.501 0.100   1.00 23.30 ? 258  VAL A N     1 
ATOM   1950 C CA    . VAL A 1 258 ? 24.120  -30.337 0.062   1.00 26.40 ? 258  VAL A CA    1 
ATOM   1951 C C     . VAL A 1 258 ? 23.568  -31.322 -0.972  1.00 27.91 ? 258  VAL A C     1 
ATOM   1952 O O     . VAL A 1 258 ? 22.551  -31.970 -0.689  1.00 23.64 ? 258  VAL A O     1 
ATOM   1953 C CB    . VAL A 1 258 ? 23.719  -28.880 -0.204  1.00 25.89 ? 258  VAL A CB    1 
ATOM   1954 C CG1   . VAL A 1 258 ? 22.230  -28.757 -0.504  1.00 25.09 ? 258  VAL A CG1   1 
ATOM   1955 C CG2   . VAL A 1 258 ? 24.119  -27.992 0.971   1.00 26.59 ? 258  VAL A CG2   1 
ATOM   1956 N N     . ASP A 1 259 ? 24.257  -31.500 -2.100  1.00 26.06 ? 259  ASP A N     1 
ATOM   1957 C CA    . ASP A 1 259 ? 23.721  -32.376 -3.174  1.00 28.06 ? 259  ASP A CA    1 
ATOM   1958 C C     . ASP A 1 259 ? 23.808  -33.851 -2.768  1.00 25.35 ? 259  ASP A C     1 
ATOM   1959 O O     . ASP A 1 259 ? 23.028  -34.646 -3.299  1.00 29.13 ? 259  ASP A O     1 
ATOM   1960 C CB    . ASP A 1 259 ? 24.398  -32.087 -4.510  1.00 28.48 ? 259  ASP A CB    1 
ATOM   1961 C CG    . ASP A 1 259 ? 23.928  -30.757 -5.056  1.00 32.49 ? 259  ASP A CG    1 
ATOM   1962 O OD1   . ASP A 1 259 ? 22.779  -30.330 -4.683  1.00 31.23 ? 259  ASP A OD1   1 
ATOM   1963 O OD2   . ASP A 1 259 ? 24.714  -30.139 -5.810  1.00 30.67 ? 259  ASP A OD2   1 
ATOM   1964 N N     . ILE A 1 260 ? 24.738  -34.224 -1.899  1.00 27.70 ? 260  ILE A N     1 
ATOM   1965 C CA    . ILE A 1 260 ? 24.836  -35.608 -1.366  1.00 30.47 ? 260  ILE A CA    1 
ATOM   1966 C C     . ILE A 1 260 ? 23.807  -35.760 -0.231  1.00 32.27 ? 260  ILE A C     1 
ATOM   1967 O O     . ILE A 1 260 ? 23.186  -36.838 -0.137  1.00 36.40 ? 260  ILE A O     1 
ATOM   1968 C CB    . ILE A 1 260 ? 26.273  -35.928 -0.927  1.00 31.18 ? 260  ILE A CB    1 
ATOM   1969 C CG1   . ILE A 1 260 ? 27.224  -35.991 -2.125  1.00 33.83 ? 260  ILE A CG1   1 
ATOM   1970 C CG2   . ILE A 1 260 ? 26.315  -37.210 -0.106  1.00 33.78 ? 260  ILE A CG2   1 
ATOM   1971 C CD1   . ILE A 1 260 ? 28.688  -35.953 -1.756  1.00 33.51 ? 260  ILE A CD1   1 
ATOM   1972 N N     . MET A 1 261 ? 23.618  -34.714 0.573   1.00 30.31 ? 261  MET A N     1 
ATOM   1973 C CA    . MET A 1 261 ? 22.732  -34.729 1.760   1.00 31.40 ? 261  MET A CA    1 
ATOM   1974 C C     . MET A 1 261 ? 21.289  -35.016 1.334   1.00 31.99 ? 261  MET A C     1 
ATOM   1975 O O     . MET A 1 261 ? 20.655  -35.892 1.961   1.00 30.27 ? 261  MET A O     1 
ATOM   1976 C CB    . MET A 1 261 ? 22.753  -33.382 2.482   1.00 34.69 ? 261  MET A CB    1 
ATOM   1977 C CG    . MET A 1 261 ? 22.280  -33.483 3.910   1.00 35.17 ? 261  MET A CG    1 
ATOM   1978 S SD    . MET A 1 261 ? 22.205  -31.869 4.721   1.00 42.07 ? 261  MET A SD    1 
ATOM   1979 C CE    . MET A 1 261 ? 23.635  -31.056 4.006   1.00 33.18 ? 261  MET A CE    1 
ATOM   1980 N N     . LEU A 1 262 ? 20.784  -34.307 0.320   1.00 28.00 ? 262  LEU A N     1 
ATOM   1981 C CA    . LEU A 1 262 ? 19.336  -34.332 0.010   1.00 30.57 ? 262  LEU A CA    1 
ATOM   1982 C C     . LEU A 1 262 ? 18.855  -35.761 -0.241  1.00 29.54 ? 262  LEU A C     1 
ATOM   1983 O O     . LEU A 1 262 ? 17.902  -36.180 0.404   1.00 26.80 ? 262  LEU A O     1 
ATOM   1984 C CB    . LEU A 1 262 ? 18.961  -33.436 -1.171  1.00 30.82 ? 262  LEU A CB    1 
ATOM   1985 C CG    . LEU A 1 262 ? 17.517  -33.694 -1.621  1.00 31.94 ? 262  LEU A CG    1 
ATOM   1986 C CD1   . LEU A 1 262 ? 16.556  -33.110 -0.579  1.00 32.20 ? 262  LEU A CD1   1 
ATOM   1987 C CD2   . LEU A 1 262 ? 17.239  -33.206 -3.026  1.00 35.76 ? 262  LEU A CD2   1 
ATOM   1988 N N     . PRO A 1 263 ? 19.449  -36.530 -1.194  1.00 32.76 ? 263  PRO A N     1 
ATOM   1989 C CA    . PRO A 1 263 ? 18.972  -37.884 -1.507  1.00 31.93 ? 263  PRO A CA    1 
ATOM   1990 C C     . PRO A 1 263 ? 19.035  -38.809 -0.287  1.00 27.92 ? 263  PRO A C     1 
ATOM   1991 O O     . PRO A 1 263 ? 18.295  -39.765 -0.222  1.00 29.14 ? 263  PRO A O     1 
ATOM   1992 C CB    . PRO A 1 263 ? 19.926  -38.451 -2.585  1.00 33.00 ? 263  PRO A CB    1 
ATOM   1993 C CG    . PRO A 1 263 ? 20.764  -37.273 -3.051  1.00 34.49 ? 263  PRO A CG    1 
ATOM   1994 C CD    . PRO A 1 263 ? 20.593  -36.148 -2.042  1.00 32.35 ? 263  PRO A CD    1 
ATOM   1995 N N     . LEU A 1 264 ? 19.925  -38.503 0.655   1.00 27.63 ? 264  LEU A N     1 
ATOM   1996 C CA    . LEU A 1 264 ? 20.136  -39.340 1.855   1.00 25.47 ? 264  LEU A CA    1 
ATOM   1997 C C     . LEU A 1 264 ? 19.157  -38.948 2.961   1.00 24.15 ? 264  LEU A C     1 
ATOM   1998 O O     . LEU A 1 264 ? 19.064  -39.724 3.898   1.00 28.21 ? 264  LEU A O     1 
ATOM   1999 C CB    . LEU A 1 264 ? 21.582  -39.209 2.337   1.00 26.12 ? 264  LEU A CB    1 
ATOM   2000 C CG    . LEU A 1 264 ? 22.661  -39.749 1.390   1.00 28.58 ? 264  LEU A CG    1 
ATOM   2001 C CD1   . LEU A 1 264 ? 24.023  -39.741 2.072   1.00 27.90 ? 264  LEU A CD1   1 
ATOM   2002 C CD2   . LEU A 1 264 ? 22.321  -41.141 0.889   1.00 32.28 ? 264  LEU A CD2   1 
ATOM   2003 N N     . ARG A 1 265 ? 18.501  -37.796 2.870   1.00 24.52 ? 265  ARG A N     1 
ATOM   2004 C CA    . ARG A 1 265 ? 17.578  -37.297 3.938   1.00 24.96 ? 265  ARG A CA    1 
ATOM   2005 C C     . ARG A 1 265 ? 16.110  -37.434 3.497   1.00 23.80 ? 265  ARG A C     1 
ATOM   2006 O O     . ARG A 1 265 ? 15.243  -37.579 4.353   1.00 22.91 ? 265  ARG A O     1 
ATOM   2007 C CB    . ARG A 1 265 ? 17.894  -35.834 4.259   1.00 26.51 ? 265  ARG A CB    1 
ATOM   2008 C CG    . ARG A 1 265 ? 16.946  -35.177 5.250   1.00 25.85 ? 265  ARG A CG    1 
ATOM   2009 C CD    . ARG A 1 265 ? 16.860  -35.970 6.545   1.00 27.03 ? 265  ARG A CD    1 
ATOM   2010 N NE    . ARG A 1 265 ? 15.879  -35.374 7.458   1.00 26.80 ? 265  ARG A NE    1 
ATOM   2011 C CZ    . ARG A 1 265 ? 15.236  -36.016 8.424   1.00 27.16 ? 265  ARG A CZ    1 
ATOM   2012 N NH1   . ARG A 1 265 ? 15.447  -37.298 8.652   1.00 27.19 ? 265  ARG A NH1   1 
ATOM   2013 N NH2   . ARG A 1 265 ? 14.350  -35.359 9.154   1.00 28.72 ? 265  ARG A NH2   1 
ATOM   2014 N N     . ILE A 1 266 ? 15.822  -37.295 2.214   1.00 25.48 ? 266  ILE A N     1 
ATOM   2015 C CA    . ILE A 1 266 ? 14.432  -37.076 1.717   1.00 26.01 ? 266  ILE A CA    1 
ATOM   2016 C C     . ILE A 1 266 ? 13.544  -38.284 2.083   1.00 28.80 ? 266  ILE A C     1 
ATOM   2017 O O     . ILE A 1 266 ? 12.341  -38.077 2.246   1.00 26.79 ? 266  ILE A O     1 
ATOM   2018 C CB    . ILE A 1 266 ? 14.431  -36.772 0.210   1.00 26.07 ? 266  ILE A CB    1 
ATOM   2019 C CG1   . ILE A 1 266 ? 13.054  -36.288 -0.258  1.00 31.59 ? 266  ILE A CG1   1 
ATOM   2020 C CG2   . ILE A 1 266 ? 14.933  -37.968 -0.586  1.00 28.67 ? 266  ILE A CG2   1 
ATOM   2021 C CD1   . ILE A 1 266 ? 13.046  -35.647 -1.627  1.00 30.89 ? 266  ILE A CD1   1 
ATOM   2022 N N     . ASN A 1 267 ? 14.117  -39.483 2.234   1.00 28.62 ? 267  ASN A N     1 
ATOM   2023 C CA    . ASN A 1 267 ? 13.385  -40.715 2.625   1.00 29.35 ? 267  ASN A CA    1 
ATOM   2024 C C     . ASN A 1 267 ? 13.516  -40.917 4.137   1.00 29.60 ? 267  ASN A C     1 
ATOM   2025 O O     . ASN A 1 267 ? 13.129  -41.978 4.587   1.00 28.54 ? 267  ASN A O     1 
ATOM   2026 C CB    . ASN A 1 267 ? 13.885  -41.956 1.870   1.00 28.95 ? 267  ASN A CB    1 
ATOM   2027 C CG    . ASN A 1 267 ? 13.782  -41.797 0.369   1.00 29.36 ? 267  ASN A CG    1 
ATOM   2028 O OD1   . ASN A 1 267 ? 12.715  -41.527 -0.154  1.00 34.98 ? 267  ASN A OD1   1 
ATOM   2029 N ND2   . ASN A 1 267 ? 14.887  -41.957 -0.320  1.00 30.54 ? 267  ASN A ND2   1 
ATOM   2030 N N     . MET A 1 268 ? 14.079  -39.951 4.870   1.00 31.07 ? 268  MET A N     1 
ATOM   2031 C CA    . MET A 1 268 ? 14.352  -40.020 6.339   1.00 33.72 ? 268  MET A CA    1 
ATOM   2032 C C     . MET A 1 268 ? 15.331  -41.152 6.706   1.00 31.71 ? 268  MET A C     1 
ATOM   2033 O O     . MET A 1 268 ? 15.392  -41.548 7.892   1.00 30.40 ? 268  MET A O     1 
ATOM   2034 C CB    . MET A 1 268 ? 13.053  -40.180 7.128   1.00 38.44 ? 268  MET A CB    1 
ATOM   2035 C CG    . MET A 1 268 ? 11.999  -39.158 6.720   1.00 45.66 ? 268  MET A CG    1 
ATOM   2036 S SD    . MET A 1 268 ? 10.414  -39.368 7.565   1.00 52.82 ? 268  MET A SD    1 
ATOM   2037 C CE    . MET A 1 268 ? 10.876  -38.937 9.243   1.00 53.56 ? 268  MET A CE    1 
ATOM   2038 N N     . ALA A 1 269 ? 16.143  -41.598 5.761   1.00 30.22 ? 269  ALA A N     1 
ATOM   2039 C CA    . ALA A 1 269 ? 17.181  -42.622 5.983   1.00 27.28 ? 269  ALA A CA    1 
ATOM   2040 C C     . ALA A 1 269 ? 18.040  -42.652 4.735   1.00 29.42 ? 269  ALA A C     1 
ATOM   2041 O O     . ALA A 1 269 ? 17.521  -42.401 3.650   1.00 28.61 ? 269  ALA A O     1 
ATOM   2042 C CB    . ALA A 1 269 ? 16.547  -43.967 6.249   1.00 29.72 ? 269  ALA A CB    1 
ATOM   2043 N N     . PRO A 1 270 ? 19.364  -42.896 4.849   1.00 29.32 ? 270  PRO A N     1 
ATOM   2044 C CA    . PRO A 1 270 ? 20.033  -43.105 6.133   1.00 27.67 ? 270  PRO A CA    1 
ATOM   2045 C C     . PRO A 1 270 ? 20.207  -41.891 7.064   1.00 27.90 ? 270  PRO A C     1 
ATOM   2046 O O     . PRO A 1 270 ? 20.542  -42.088 8.217   1.00 29.43 ? 270  PRO A O     1 
ATOM   2047 C CB    . PRO A 1 270 ? 21.431  -43.589 5.709   1.00 30.66 ? 270  PRO A CB    1 
ATOM   2048 C CG    . PRO A 1 270 ? 21.632  -42.944 4.362   1.00 29.25 ? 270  PRO A CG    1 
ATOM   2049 C CD    . PRO A 1 270 ? 20.273  -43.048 3.705   1.00 30.58 ? 270  PRO A CD    1 
ATOM   2050 N N     . LEU A 1 271 ? 19.993  -40.664 6.583   1.00 25.34 ? 271  LEU A N     1 
ATOM   2051 C CA    . LEU A 1 271 ? 20.031  -39.466 7.474   1.00 26.70 ? 271  LEU A CA    1 
ATOM   2052 C C     . LEU A 1 271 ? 18.720  -39.404 8.273   1.00 23.63 ? 271  LEU A C     1 
ATOM   2053 O O     . LEU A 1 271 ? 17.769  -38.754 7.805   1.00 25.59 ? 271  LEU A O     1 
ATOM   2054 C CB    . LEU A 1 271 ? 20.253  -38.212 6.625   1.00 25.94 ? 271  LEU A CB    1 
ATOM   2055 C CG    . LEU A 1 271 ? 21.625  -38.125 5.952   1.00 26.50 ? 271  LEU A CG    1 
ATOM   2056 C CD1   . LEU A 1 271 ? 21.778  -36.811 5.247   1.00 26.90 ? 271  LEU A CD1   1 
ATOM   2057 C CD2   . LEU A 1 271 ? 22.766  -38.345 6.942   1.00 31.66 ? 271  LEU A CD2   1 
ATOM   2058 N N     . GLN A 1 272 ? 18.705  -40.050 9.432   1.00 26.41 ? 272  GLN A N     1 
ATOM   2059 C CA    . GLN A 1 272 ? 17.485  -40.381 10.214  1.00 27.22 ? 272  GLN A CA    1 
ATOM   2060 C C     . GLN A 1 272 ? 17.054  -39.197 11.076  1.00 26.22 ? 272  GLN A C     1 
ATOM   2061 O O     . GLN A 1 272 ? 15.854  -38.990 11.245  1.00 28.31 ? 272  GLN A O     1 
ATOM   2062 C CB    . GLN A 1 272 ? 17.728  -41.606 11.094  1.00 27.01 ? 272  GLN A CB    1 
ATOM   2063 C CG    . GLN A 1 272 ? 17.898  -42.905 10.323  1.00 29.90 ? 272  GLN A CG    1 
ATOM   2064 C CD    . GLN A 1 272 ? 18.324  -43.999 11.275  1.00 28.76 ? 272  GLN A CD    1 
ATOM   2065 O OE1   . GLN A 1 272 ? 19.336  -43.880 11.950  1.00 33.50 ? 272  GLN A OE1   1 
ATOM   2066 N NE2   . GLN A 1 272 ? 17.528  -45.049 11.390  1.00 29.53 ? 272  GLN A NE2   1 
ATOM   2067 N N     . ASN A 1 273 ? 17.988  -38.405 11.562  1.00 25.61 ? 273  ASN A N     1 
ATOM   2068 C CA    . ASN A 1 273 ? 17.648  -37.194 12.345  1.00 25.02 ? 273  ASN A CA    1 
ATOM   2069 C C     . ASN A 1 273 ? 17.713  -35.992 11.399  1.00 24.65 ? 273  ASN A C     1 
ATOM   2070 O O     . ASN A 1 273 ? 17.895  -36.170 10.163  1.00 24.59 ? 273  ASN A O     1 
ATOM   2071 C CB    . ASN A 1 273 ? 18.526  -37.078 13.595  1.00 27.57 ? 273  ASN A CB    1 
ATOM   2072 C CG    . ASN A 1 273 ? 19.799  -36.303 13.338  1.00 28.94 ? 273  ASN A CG    1 
ATOM   2073 O OD1   . ASN A 1 273 ? 20.541  -36.642 12.421  1.00 26.14 ? 273  ASN A OD1   1 
ATOM   2074 N ND2   . ASN A 1 273 ? 20.038  -35.255 14.118  1.00 26.47 ? 273  ASN A ND2   1 
ATOM   2075 N N     . VAL A 1 274 ? 17.564  -34.794 11.944  1.00 24.93 ? 274  VAL A N     1 
ATOM   2076 C CA    . VAL A 1 274 ? 17.689  -33.545 11.144  1.00 23.73 ? 274  VAL A CA    1 
ATOM   2077 C C     . VAL A 1 274 ? 19.183  -33.278 10.983  1.00 22.97 ? 274  VAL A C     1 
ATOM   2078 O O     . VAL A 1 274 ? 19.851  -33.002 11.974  1.00 21.62 ? 274  VAL A O     1 
ATOM   2079 C CB    . VAL A 1 274 ? 16.993  -32.358 11.824  1.00 24.58 ? 274  VAL A CB    1 
ATOM   2080 C CG1   . VAL A 1 274 ? 17.218  -31.105 11.001  1.00 26.44 ? 274  VAL A CG1   1 
ATOM   2081 C CG2   . VAL A 1 274 ? 15.506  -32.598 12.072  1.00 26.37 ? 274  VAL A CG2   1 
ATOM   2082 N N     . PRO A 1 275 ? 19.754  -33.321 9.765   1.00 21.73 ? 275  PRO A N     1 
ATOM   2083 C CA    . PRO A 1 275 ? 21.179  -33.056 9.591   1.00 26.10 ? 275  PRO A CA    1 
ATOM   2084 C C     . PRO A 1 275 ? 21.473  -31.551 9.661   1.00 24.97 ? 275  PRO A C     1 
ATOM   2085 O O     . PRO A 1 275 ? 20.701  -30.729 9.148   1.00 24.60 ? 275  PRO A O     1 
ATOM   2086 C CB    . PRO A 1 275 ? 21.486  -33.624 8.204   1.00 24.65 ? 275  PRO A CB    1 
ATOM   2087 C CG    . PRO A 1 275 ? 20.176  -33.467 7.464   1.00 25.72 ? 275  PRO A CG    1 
ATOM   2088 C CD    . PRO A 1 275 ? 19.086  -33.598 8.495   1.00 23.50 ? 275  PRO A CD    1 
ATOM   2089 N N     . VAL A 1 276 ? 22.565  -31.211 10.332  1.00 24.79 ? 276  VAL A N     1 
ATOM   2090 C CA    . VAL A 1 276 ? 23.033  -29.801 10.451  1.00 26.96 ? 276  VAL A CA    1 
ATOM   2091 C C     . VAL A 1 276 ? 24.461  -29.699 9.905   1.00 27.43 ? 276  VAL A C     1 
ATOM   2092 O O     . VAL A 1 276 ? 25.286  -30.616 10.131  1.00 27.19 ? 276  VAL A O     1 
ATOM   2093 C CB    . VAL A 1 276 ? 22.934  -29.266 11.885  1.00 25.32 ? 276  VAL A CB    1 
ATOM   2094 C CG1   . VAL A 1 276 ? 21.514  -29.398 12.401  1.00 25.27 ? 276  VAL A CG1   1 
ATOM   2095 C CG2   . VAL A 1 276 ? 23.941  -29.915 12.811  1.00 26.86 ? 276  VAL A CG2   1 
ATOM   2096 N N     . LEU A 1 277 ? 24.703  -28.632 9.164   1.00 26.58 ? 277  LEU A N     1 
ATOM   2097 C CA    . LEU A 1 277 ? 26.033  -28.349 8.588   1.00 25.97 ? 277  LEU A CA    1 
ATOM   2098 C C     . LEU A 1 277 ? 26.455  -26.975 9.090   1.00 26.37 ? 277  LEU A C     1 
ATOM   2099 O O     . LEU A 1 277 ? 25.888  -25.975 8.592   1.00 24.87 ? 277  LEU A O     1 
ATOM   2100 C CB    . LEU A 1 277 ? 25.951  -28.370 7.068   1.00 25.64 ? 277  LEU A CB    1 
ATOM   2101 C CG    . LEU A 1 277 ? 27.305  -28.230 6.378   1.00 25.93 ? 277  LEU A CG    1 
ATOM   2102 C CD1   . LEU A 1 277 ? 28.127  -29.509 6.542   1.00 26.77 ? 277  LEU A CD1   1 
ATOM   2103 C CD2   . LEU A 1 277 ? 27.129  -27.885 4.926   1.00 27.06 ? 277  LEU A CD2   1 
ATOM   2104 N N     . ARG A 1 278 ? 27.357  -26.968 10.074  1.00 24.18 ? 278  ARG A N     1 
ATOM   2105 C CA    . ARG A 1 278 ? 27.761  -25.764 10.811  1.00 24.47 ? 278  ARG A CA    1 
ATOM   2106 C C     . ARG A 1 278 ? 29.113  -25.283 10.289  1.00 25.92 ? 278  ARG A C     1 
ATOM   2107 O O     . ARG A 1 278 ? 30.002  -26.125 10.104  1.00 26.19 ? 278  ARG A O     1 
ATOM   2108 C CB    . ARG A 1 278 ? 27.838  -26.100 12.301  1.00 26.50 ? 278  ARG A CB    1 
ATOM   2109 C CG    . ARG A 1 278 ? 26.495  -26.500 12.894  1.00 27.07 ? 278  ARG A CG    1 
ATOM   2110 C CD    . ARG A 1 278 ? 26.716  -27.161 14.238  1.00 27.49 ? 278  ARG A CD    1 
ATOM   2111 N NE    . ARG A 1 278 ? 27.300  -26.265 15.216  1.00 26.19 ? 278  ARG A NE    1 
ATOM   2112 C CZ    . ARG A 1 278 ? 26.661  -25.668 16.224  1.00 30.74 ? 278  ARG A CZ    1 
ATOM   2113 N NH1   . ARG A 1 278 ? 25.362  -25.851 16.413  1.00 28.23 ? 278  ARG A NH1   1 
ATOM   2114 N NH2   . ARG A 1 278 ? 27.341  -24.884 17.052  1.00 30.72 ? 278  ARG A NH2   1 
ATOM   2115 N N     . ASN A 1 279 ? 29.246  -23.981 10.044  1.00 26.23 ? 279  ASN A N     1 
ATOM   2116 C CA    . ASN A 1 279 ? 30.530  -23.422 9.547   1.00 25.26 ? 279  ASN A CA    1 
ATOM   2117 C C     . ASN A 1 279 ? 31.505  -23.360 10.727  1.00 25.89 ? 279  ASN A C     1 
ATOM   2118 O O     . ASN A 1 279 ? 31.080  -23.507 11.900  1.00 25.25 ? 279  ASN A O     1 
ATOM   2119 C CB    . ASN A 1 279 ? 30.302  -22.116 8.788   1.00 25.51 ? 279  ASN A CB    1 
ATOM   2120 C CG    . ASN A 1 279 ? 30.423  -20.873 9.644   1.00 26.04 ? 279  ASN A CG    1 
ATOM   2121 O OD1   . ASN A 1 279 ? 29.814  -20.804 10.704  1.00 35.83 ? 279  ASN A OD1   1 
ATOM   2122 N ND2   . ASN A 1 279 ? 31.164  -19.882 9.222   1.00 22.92 ? 279  ASN A ND2   1 
ATOM   2123 N N     . ILE A 1 280 ? 32.794  -23.181 10.429  1.00 28.91 ? 280  ILE A N     1 
ATOM   2124 C CA    . ILE A 1 280 ? 33.896  -23.147 11.438  1.00 27.75 ? 280  ILE A CA    1 
ATOM   2125 C C     . ILE A 1 280 ? 33.534  -22.164 12.549  1.00 27.31 ? 280  ILE A C     1 
ATOM   2126 O O     . ILE A 1 280 ? 33.770  -22.486 13.734  1.00 26.95 ? 280  ILE A O     1 
ATOM   2127 C CB    . ILE A 1 280 ? 35.255  -22.800 10.785  1.00 29.52 ? 280  ILE A CB    1 
ATOM   2128 C CG1   . ILE A 1 280 ? 36.395  -22.725 11.817  1.00 31.70 ? 280  ILE A CG1   1 
ATOM   2129 C CG2   . ILE A 1 280 ? 35.139  -21.503 9.993   1.00 27.14 ? 280  ILE A CG2   1 
ATOM   2130 C CD1   . ILE A 1 280 ? 37.101  -24.036 12.150  1.00 37.67 ? 280  ILE A CD1   1 
ATOM   2131 N N     . ILE A 1 281 ? 32.968  -21.010 12.206  1.00 28.24 ? 281  ILE A N     1 
ATOM   2132 C CA    . ILE A 1 281 ? 32.762  -19.949 13.236  1.00 30.99 ? 281  ILE A CA    1 
ATOM   2133 C C     . ILE A 1 281 ? 31.678  -20.374 14.250  1.00 31.50 ? 281  ILE A C     1 
ATOM   2134 O O     . ILE A 1 281 ? 31.911  -20.240 15.476  1.00 27.31 ? 281  ILE A O     1 
ATOM   2135 C CB    . ILE A 1 281 ? 32.596  -18.589 12.538  1.00 37.15 ? 281  ILE A CB    1 
ATOM   2136 C CG1   . ILE A 1 281 ? 33.992  -17.975 12.344  1.00 42.32 ? 281  ILE A CG1   1 
ATOM   2137 C CG2   . ILE A 1 281 ? 31.671  -17.672 13.314  1.00 39.81 ? 281  ILE A CG2   1 
ATOM   2138 C CD1   . ILE A 1 281 ? 34.143  -17.180 11.096  1.00 50.69 ? 281  ILE A CD1   1 
ATOM   2139 N N     . LEU A 1 282 ? 30.560  -20.970 13.844  1.00 32.34 ? 282  LEU A N     1 
ATOM   2140 C CA    . LEU A 1 282 ? 29.579  -21.312 14.913  1.00 35.65 ? 282  LEU A CA    1 
ATOM   2141 C C     . LEU A 1 282 ? 30.016  -22.591 15.646  1.00 33.10 ? 282  LEU A C     1 
ATOM   2142 O O     . LEU A 1 282 ? 29.644  -22.713 16.828  1.00 34.68 ? 282  LEU A O     1 
ATOM   2143 C CB    . LEU A 1 282 ? 28.132  -21.283 14.408  1.00 45.01 ? 282  LEU A CB    1 
ATOM   2144 C CG    . LEU A 1 282 ? 27.558  -22.573 13.881  1.00 42.90 ? 282  LEU A CG    1 
ATOM   2145 C CD1   . LEU A 1 282 ? 26.057  -22.485 13.698  1.00 43.71 ? 282  LEU A CD1   1 
ATOM   2146 C CD2   . LEU A 1 282 ? 28.223  -22.888 12.567  1.00 55.61 ? 282  LEU A CD2   1 
ATOM   2147 N N     . ASP A 1 283 ? 30.903  -23.421 15.081  1.00 29.06 ? 283  ASP A N     1 
ATOM   2148 C CA    . ASP A 1 283 ? 31.571  -24.488 15.880  1.00 29.41 ? 283  ASP A CA    1 
ATOM   2149 C C     . ASP A 1 283 ? 32.655  -23.902 16.802  1.00 30.52 ? 283  ASP A C     1 
ATOM   2150 O O     . ASP A 1 283 ? 32.702  -24.301 17.986  1.00 35.35 ? 283  ASP A O     1 
ATOM   2151 C CB    . ASP A 1 283 ? 32.175  -25.577 14.997  1.00 33.66 ? 283  ASP A CB    1 
ATOM   2152 C CG    . ASP A 1 283 ? 31.260  -26.777 14.809  1.00 32.46 ? 283  ASP A CG    1 
ATOM   2153 O OD1   . ASP A 1 283 ? 30.037  -26.639 15.051  1.00 32.37 ? 283  ASP A OD1   1 
ATOM   2154 O OD2   . ASP A 1 283 ? 31.776  -27.829 14.434  1.00 39.60 ? 283  ASP A OD2   1 
ATOM   2155 N N     . ALA A 1 284 ? 33.501  -22.982 16.323  1.00 27.20 ? 284  ALA A N     1 
ATOM   2156 C CA    . ALA A 1 284 ? 34.647  -22.465 17.118  1.00 28.19 ? 284  ALA A CA    1 
ATOM   2157 C C     . ALA A 1 284 ? 34.148  -21.606 18.293  1.00 28.48 ? 284  ALA A C     1 
ATOM   2158 O O     . ALA A 1 284 ? 34.757  -21.669 19.385  1.00 32.08 ? 284  ALA A O     1 
ATOM   2159 C CB    . ALA A 1 284 ? 35.580  -21.681 16.234  1.00 31.78 ? 284  ALA A CB    1 
ATOM   2160 N N     . ALA A 1 285 ? 33.035  -20.890 18.097  1.00 29.63 ? 285  ALA A N     1 
ATOM   2161 C CA    . ALA A 1 285 ? 32.467  -19.904 19.031  1.00 30.34 ? 285  ALA A CA    1 
ATOM   2162 C C     . ALA A 1 285 ? 31.883  -20.575 20.274  1.00 31.66 ? 285  ALA A C     1 
ATOM   2163 O O     . ALA A 1 285 ? 31.724  -19.891 21.304  1.00 34.70 ? 285  ALA A O     1 
ATOM   2164 C CB    . ALA A 1 285 ? 31.439  -19.062 18.310  1.00 31.76 ? 285  ALA A CB    1 
ATOM   2165 N N     . VAL A 1 286 ? 31.594  -21.871 20.214  1.00 36.37 ? 286  VAL A N     1 
ATOM   2166 C CA    . VAL A 1 286 ? 31.123  -22.649 21.404  1.00 34.35 ? 286  VAL A CA    1 
ATOM   2167 C C     . VAL A 1 286 ? 32.291  -22.886 22.367  1.00 35.80 ? 286  VAL A C     1 
ATOM   2168 O O     . VAL A 1 286 ? 32.028  -22.935 23.577  1.00 40.83 ? 286  VAL A O     1 
ATOM   2169 C CB    . VAL A 1 286 ? 30.450  -23.962 20.979  1.00 34.61 ? 286  VAL A CB    1 
ATOM   2170 C CG1   . VAL A 1 286 ? 30.076  -24.828 22.173  1.00 37.16 ? 286  VAL A CG1   1 
ATOM   2171 C CG2   . VAL A 1 286 ? 29.219  -23.670 20.121  1.00 36.95 ? 286  VAL A CG2   1 
ATOM   2172 N N     . VAL A 1 287 ? 33.533  -22.977 21.878  1.00 36.83 ? 287  VAL A N     1 
ATOM   2173 C CA    . VAL A 1 287 ? 34.690  -23.461 22.687  1.00 32.94 ? 287  VAL A CA    1 
ATOM   2174 C C     . VAL A 1 287 ? 35.804  -22.412 22.753  1.00 38.02 ? 287  VAL A C     1 
ATOM   2175 O O     . VAL A 1 287 ? 36.869  -22.737 23.295  1.00 35.19 ? 287  VAL A O     1 
ATOM   2176 C CB    . VAL A 1 287 ? 35.233  -24.781 22.124  1.00 35.34 ? 287  VAL A CB    1 
ATOM   2177 C CG1   . VAL A 1 287 ? 34.213  -25.895 22.236  1.00 39.28 ? 287  VAL A CG1   1 
ATOM   2178 C CG2   . VAL A 1 287 ? 35.740  -24.642 20.702  1.00 34.71 ? 287  VAL A CG2   1 
ATOM   2179 N N     . SER A 1 288 ? 35.598  -21.227 22.193  1.00 36.80 ? 288  SER A N     1 
ATOM   2180 C CA    . SER A 1 288 ? 36.643  -20.184 22.100  1.00 36.05 ? 288  SER A CA    1 
ATOM   2181 C C     . SER A 1 288 ? 35.977  -18.814 21.945  1.00 37.66 ? 288  SER A C     1 
ATOM   2182 O O     . SER A 1 288 ? 34.742  -18.759 21.731  1.00 33.35 ? 288  SER A O     1 
ATOM   2183 C CB    . SER A 1 288 ? 37.603  -20.488 20.970  1.00 33.31 ? 288  SER A CB    1 
ATOM   2184 O OG    . SER A 1 288 ? 37.015  -20.284 19.688  1.00 29.08 ? 288  SER A OG    1 
ATOM   2185 N N     . GLN A 1 289 ? 36.781  -17.756 22.068  1.00 34.73 ? 289  GLN A N     1 
ATOM   2186 C CA    . GLN A 1 289 ? 36.375  -16.346 21.891  1.00 36.20 ? 289  GLN A CA    1 
ATOM   2187 C C     . GLN A 1 289 ? 37.064  -15.779 20.647  1.00 33.85 ? 289  GLN A C     1 
ATOM   2188 O O     . GLN A 1 289 ? 38.096  -16.312 20.235  1.00 33.25 ? 289  GLN A O     1 
ATOM   2189 C CB    . GLN A 1 289 ? 36.682  -15.603 23.190  1.00 42.79 ? 289  GLN A CB    1 
ATOM   2190 C CG    . GLN A 1 289 ? 36.230  -16.395 24.415  1.00 47.93 ? 289  GLN A CG    1 
ATOM   2191 C CD    . GLN A 1 289 ? 36.249  -15.572 25.673  1.00 56.26 ? 289  GLN A CD    1 
ATOM   2192 O OE1   . GLN A 1 289 ? 36.024  -16.084 26.763  1.00 66.90 ? 289  GLN A OE1   1 
ATOM   2193 N NE2   . GLN A 1 289 ? 36.523  -14.285 25.530  1.00 57.13 ? 289  GLN A NE2   1 
ATOM   2194 N N     . ARG A 1 290 ? 36.457  -14.767 20.031  1.00 34.23 ? 290  ARG A N     1 
ATOM   2195 C CA    . ARG A 1 290 ? 36.949  -14.178 18.758  1.00 33.90 ? 290  ARG A CA    1 
ATOM   2196 C C     . ARG A 1 290 ? 38.396  -13.677 18.964  1.00 35.88 ? 290  ARG A C     1 
ATOM   2197 O O     . ARG A 1 290 ? 39.249  -13.929 18.099  1.00 33.36 ? 290  ARG A O     1 
ATOM   2198 C CB    . ARG A 1 290 ? 36.008  -13.054 18.329  1.00 32.42 ? 290  ARG A CB    1 
ATOM   2199 C CG    . ARG A 1 290 ? 36.168  -12.645 16.880  1.00 29.63 ? 290  ARG A CG    1 
ATOM   2200 C CD    . ARG A 1 290 ? 35.378  -11.405 16.605  1.00 29.09 ? 290  ARG A CD    1 
ATOM   2201 N NE    . ARG A 1 290 ? 35.303  -11.007 15.215  1.00 31.01 ? 290  ARG A NE    1 
ATOM   2202 C CZ    . ARG A 1 290 ? 36.108  -10.140 14.611  1.00 32.81 ? 290  ARG A CZ    1 
ATOM   2203 N NH1   . ARG A 1 290 ? 37.122  -9.589  15.261  1.00 32.95 ? 290  ARG A NH1   1 
ATOM   2204 N NH2   . ARG A 1 290 ? 35.906  -9.844  13.346  1.00 34.56 ? 290  ARG A NH2   1 
ATOM   2205 N N     . ALA A 1 291 ? 38.648  -13.041 20.112  1.00 36.42 ? 291  ALA A N     1 
ATOM   2206 C CA    . ALA A 1 291 ? 39.943  -12.467 20.538  1.00 37.78 ? 291  ALA A CA    1 
ATOM   2207 C C     . ALA A 1 291 ? 41.040  -13.538 20.538  1.00 37.79 ? 291  ALA A C     1 
ATOM   2208 O O     . ALA A 1 291 ? 42.196  -13.167 20.331  1.00 42.68 ? 291  ALA A O     1 
ATOM   2209 C CB    . ALA A 1 291 ? 39.787  -11.808 21.883  1.00 34.17 ? 291  ALA A CB    1 
ATOM   2210 N N     . ASP A 1 292 ? 40.699  -14.823 20.697  1.00 38.84 ? 292  ASP A N     1 
ATOM   2211 C CA    . ASP A 1 292 ? 41.673  -15.947 20.708  1.00 39.22 ? 292  ASP A CA    1 
ATOM   2212 C C     . ASP A 1 292 ? 42.310  -16.126 19.325  1.00 40.54 ? 292  ASP A C     1 
ATOM   2213 O O     . ASP A 1 292 ? 43.382  -16.724 19.262  1.00 43.95 ? 292  ASP A O     1 
ATOM   2214 C CB    . ASP A 1 292 ? 41.030  -17.272 21.107  1.00 38.72 ? 292  ASP A CB    1 
ATOM   2215 C CG    . ASP A 1 292 ? 40.416  -17.245 22.489  1.00 42.46 ? 292  ASP A CG    1 
ATOM   2216 O OD1   . ASP A 1 292 ? 40.743  -16.317 23.244  1.00 42.17 ? 292  ASP A OD1   1 
ATOM   2217 O OD2   . ASP A 1 292 ? 39.590  -18.128 22.784  1.00 37.43 ? 292  ASP A OD2   1 
ATOM   2218 N N     . TRP A 1 293 ? 41.658  -15.674 18.258  1.00 37.50 ? 293  TRP A N     1 
ATOM   2219 C CA    . TRP A 1 293 ? 42.068  -15.978 16.863  1.00 37.88 ? 293  TRP A CA    1 
ATOM   2220 C C     . TRP A 1 293 ? 42.534  -14.727 16.132  1.00 37.67 ? 293  TRP A C     1 
ATOM   2221 O O     . TRP A 1 293 ? 43.163  -14.881 15.083  1.00 42.82 ? 293  TRP A O     1 
ATOM   2222 C CB    . TRP A 1 293 ? 40.896  -16.626 16.112  1.00 38.24 ? 293  TRP A CB    1 
ATOM   2223 C CG    . TRP A 1 293 ? 40.325  -17.775 16.868  1.00 35.07 ? 293  TRP A CG    1 
ATOM   2224 C CD1   . TRP A 1 293 ? 39.147  -17.791 17.550  1.00 35.56 ? 293  TRP A CD1   1 
ATOM   2225 C CD2   . TRP A 1 293 ? 40.951  -19.046 17.105  1.00 34.81 ? 293  TRP A CD2   1 
ATOM   2226 N NE1   . TRP A 1 293 ? 38.978  -18.998 18.161  1.00 32.36 ? 293  TRP A NE1   1 
ATOM   2227 C CE2   . TRP A 1 293 ? 40.069  -19.785 17.923  1.00 34.01 ? 293  TRP A CE2   1 
ATOM   2228 C CE3   . TRP A 1 293 ? 42.167  -19.627 16.718  1.00 35.37 ? 293  TRP A CE3   1 
ATOM   2229 C CZ2   . TRP A 1 293 ? 40.347  -21.087 18.331  1.00 35.88 ? 293  TRP A CZ2   1 
ATOM   2230 C CZ3   . TRP A 1 293 ? 42.443  -20.915 17.120  1.00 36.56 ? 293  TRP A CZ3   1 
ATOM   2231 C CH2   . TRP A 1 293 ? 41.551  -21.630 17.923  1.00 36.30 ? 293  TRP A CH2   1 
ATOM   2232 N N     . TYR A 1 294 ? 42.143  -13.556 16.615  1.00 38.82 ? 294  TYR A N     1 
ATOM   2233 C CA    . TYR A 1 294 ? 42.229  -12.269 15.882  1.00 43.75 ? 294  TYR A CA    1 
ATOM   2234 C C     . TYR A 1 294 ? 41.828  -11.145 16.839  1.00 48.49 ? 294  TYR A C     1 
ATOM   2235 O O     . TYR A 1 294 ? 40.828  -11.264 17.576  1.00 53.58 ? 294  TYR A O     1 
ATOM   2236 C CB    . TYR A 1 294 ? 41.344  -12.279 14.633  1.00 41.58 ? 294  TYR A CB    1 
ATOM   2237 C CG    . TYR A 1 294 ? 41.548  -11.114 13.701  1.00 41.46 ? 294  TYR A CG    1 
ATOM   2238 C CD1   . TYR A 1 294 ? 42.746  -10.960 13.021  1.00 46.64 ? 294  TYR A CD1   1 
ATOM   2239 C CD2   . TYR A 1 294 ? 40.555  -10.171 13.489  1.00 41.79 ? 294  TYR A CD2   1 
ATOM   2240 C CE1   . TYR A 1 294 ? 42.953  -9.898  12.158  1.00 47.23 ? 294  TYR A CE1   1 
ATOM   2241 C CE2   . TYR A 1 294 ? 40.741  -9.111  12.617  1.00 44.26 ? 294  TYR A CE2   1 
ATOM   2242 C CZ    . TYR A 1 294 ? 41.948  -8.970  11.950  1.00 47.03 ? 294  TYR A CZ    1 
ATOM   2243 O OH    . TYR A 1 294 ? 42.141  -7.942  11.072  1.00 48.16 ? 294  TYR A OH    1 
ATOM   2244 N N     . ASP A 1 295 ? 42.649  -10.099 16.854  1.00 57.07 ? 295  ASP A N     1 
ATOM   2245 C CA    . ASP A 1 295 ? 42.516  -8.928  17.754  1.00 61.23 ? 295  ASP A CA    1 
ATOM   2246 C C     . ASP A 1 295 ? 42.638  -7.645  16.925  1.00 58.56 ? 295  ASP A C     1 
ATOM   2247 O O     . ASP A 1 295 ? 42.646  -6.580  17.540  1.00 58.57 ? 295  ASP A O     1 
ATOM   2248 C CB    . ASP A 1 295 ? 43.557  -9.012  18.876  1.00 68.49 ? 295  ASP A CB    1 
ATOM   2249 C CG    . ASP A 1 295 ? 44.969  -9.282  18.366  1.00 74.92 ? 295  ASP A CG    1 
ATOM   2250 O OD1   . ASP A 1 295 ? 45.326  -8.721  17.312  1.00 76.43 ? 295  ASP A OD1   1 
ATOM   2251 O OD2   . ASP A 1 295 ? 45.688  -10.088 18.999  1.00 82.95 ? 295  ASP A OD2   1 
ATOM   2252 N N     . GLY A 1 296 ? 42.753  -7.757  15.593  1.00 58.67 ? 296  GLY A N     1 
ATOM   2253 C CA    . GLY A 1 296 ? 42.723  -6.630  14.637  1.00 59.40 ? 296  GLY A CA    1 
ATOM   2254 C C     . GLY A 1 296 ? 41.296  -6.189  14.381  1.00 56.87 ? 296  GLY A C     1 
ATOM   2255 O O     . GLY A 1 296 ? 40.392  -6.847  14.895  1.00 60.58 ? 296  GLY A O     1 
ATOM   2256 N N     . ASP A 1 297 ? 41.084  -5.118  13.618  1.00 59.12 ? 297  ASP A N     1 
ATOM   2257 C CA    . ASP A 1 297 ? 39.715  -4.644  13.265  1.00 65.75 ? 297  ASP A CA    1 
ATOM   2258 C C     . ASP A 1 297 ? 39.353  -5.221  11.890  1.00 55.46 ? 297  ASP A C     1 
ATOM   2259 O O     . ASP A 1 297 ? 40.227  -5.862  11.268  1.00 55.96 ? 297  ASP A O     1 
ATOM   2260 C CB    . ASP A 1 297 ? 39.597  -3.118  13.360  1.00 70.89 ? 297  ASP A CB    1 
ATOM   2261 C CG    . ASP A 1 297 ? 40.875  -2.386  13.005  1.00 70.58 ? 297  ASP A CG    1 
ATOM   2262 O OD1   . ASP A 1 297 ? 41.668  -2.958  12.244  1.00 78.03 ? 297  ASP A OD1   1 
ATOM   2263 O OD2   . ASP A 1 297 ? 41.074  -1.263  13.509  1.00 74.48 ? 297  ASP A OD2   1 
ATOM   2264 N N     . GLY A 1 298 ? 38.101  -5.052  11.464  1.00 53.62 ? 298  GLY A N     1 
ATOM   2265 C CA    . GLY A 1 298 ? 37.558  -5.617  10.211  1.00 48.86 ? 298  GLY A CA    1 
ATOM   2266 C C     . GLY A 1 298 ? 37.177  -7.086  10.371  1.00 44.47 ? 298  GLY A C     1 
ATOM   2267 O O     . GLY A 1 298 ? 37.357  -7.666  11.430  1.00 43.95 ? 298  GLY A O     1 
ATOM   2268 N N     . PRO A 1 299 ? 36.663  -7.744  9.310   1.00 43.81 ? 299  PRO A N     1 
ATOM   2269 C CA    . PRO A 1 299 ? 36.328  -9.164  9.360   1.00 41.06 ? 299  PRO A CA    1 
ATOM   2270 C C     . PRO A 1 299 ? 37.517  -10.050 9.732   1.00 38.56 ? 299  PRO A C     1 
ATOM   2271 O O     . PRO A 1 299 ? 38.645  -9.637  9.557   1.00 36.15 ? 299  PRO A O     1 
ATOM   2272 C CB    . PRO A 1 299 ? 35.889  -9.513  7.929   1.00 40.44 ? 299  PRO A CB    1 
ATOM   2273 C CG    . PRO A 1 299 ? 35.467  -8.187  7.330   1.00 43.76 ? 299  PRO A CG    1 
ATOM   2274 C CD    . PRO A 1 299 ? 36.330  -7.141  8.011   1.00 44.31 ? 299  PRO A CD    1 
ATOM   2275 N N     . LEU A 1 300 ? 37.234  -11.259 10.207  1.00 36.77 ? 300  LEU A N     1 
ATOM   2276 C CA    . LEU A 1 300 ? 38.267  -12.292 10.444  1.00 36.51 ? 300  LEU A CA    1 
ATOM   2277 C C     . LEU A 1 300 ? 38.933  -12.576 9.102   1.00 41.03 ? 300  LEU A C     1 
ATOM   2278 O O     . LEU A 1 300 ? 38.250  -12.874 8.117   1.00 39.31 ? 300  LEU A O     1 
ATOM   2279 C CB    . LEU A 1 300 ? 37.646  -13.561 11.026  1.00 35.46 ? 300  LEU A CB    1 
ATOM   2280 C CG    . LEU A 1 300 ? 36.963  -13.401 12.382  1.00 35.39 ? 300  LEU A CG    1 
ATOM   2281 C CD1   . LEU A 1 300 ? 35.947  -14.528 12.597  1.00 34.06 ? 300  LEU A CD1   1 
ATOM   2282 C CD2   . LEU A 1 300 ? 37.996  -13.376 13.498  1.00 34.05 ? 300  LEU A CD2   1 
ATOM   2283 N N     . PRO A 1 301 ? 40.278  -12.471 9.025   1.00 42.90 ? 301  PRO A N     1 
ATOM   2284 C CA    . PRO A 1 301 ? 40.996  -12.792 7.798   1.00 39.88 ? 301  PRO A CA    1 
ATOM   2285 C C     . PRO A 1 301 ? 41.021  -14.302 7.599   1.00 39.41 ? 301  PRO A C     1 
ATOM   2286 O O     . PRO A 1 301 ? 40.913  -15.060 8.567   1.00 36.80 ? 301  PRO A O     1 
ATOM   2287 C CB    . PRO A 1 301 ? 42.398  -12.219 8.036   1.00 41.32 ? 301  PRO A CB    1 
ATOM   2288 C CG    . PRO A 1 301 ? 42.573  -12.258 9.535   1.00 44.59 ? 301  PRO A CG    1 
ATOM   2289 C CD    . PRO A 1 301 ? 41.181  -12.048 10.109  1.00 44.49 ? 301  PRO A CD    1 
ATOM   2290 N N     . PRO A 1 302 ? 41.215  -14.779 6.351   1.00 39.45 ? 302  PRO A N     1 
ATOM   2291 C CA    . PRO A 1 302 ? 41.345  -16.210 6.081   1.00 38.26 ? 302  PRO A CA    1 
ATOM   2292 C C     . PRO A 1 302 ? 42.312  -16.956 7.002   1.00 37.21 ? 302  PRO A C     1 
ATOM   2293 O O     . PRO A 1 302 ? 42.041  -18.087 7.315   1.00 39.71 ? 302  PRO A O     1 
ATOM   2294 C CB    . PRO A 1 302 ? 41.849  -16.238 4.636   1.00 39.44 ? 302  PRO A CB    1 
ATOM   2295 C CG    . PRO A 1 302 ? 41.220  -15.013 4.024   1.00 41.26 ? 302  PRO A CG    1 
ATOM   2296 C CD    . PRO A 1 302 ? 41.289  -13.971 5.123   1.00 41.80 ? 302  PRO A CD    1 
ATOM   2297 N N     . GLU A 1 303 ? 43.416  -16.330 7.413   1.00 39.00 ? 303  GLU A N     1 
ATOM   2298 C CA    . GLU A 1 303 ? 44.464  -17.036 8.211   1.00 39.95 ? 303  GLU A CA    1 
ATOM   2299 C C     . GLU A 1 303 ? 43.945  -17.266 9.640   1.00 35.14 ? 303  GLU A C     1 
ATOM   2300 O O     . GLU A 1 303 ? 44.320  -18.290 10.228  1.00 33.98 ? 303  GLU A O     1 
ATOM   2301 C CB    . GLU A 1 303 ? 45.831  -16.331 8.184   1.00 43.18 ? 303  GLU A CB    1 
ATOM   2302 C CG    . GLU A 1 303 ? 45.798  -14.854 8.514   1.00 49.72 ? 303  GLU A CG    1 
ATOM   2303 C CD    . GLU A 1 303 ? 45.732  -13.947 7.285   1.00 57.13 ? 303  GLU A CD    1 
ATOM   2304 O OE1   . GLU A 1 303 ? 46.402  -12.890 7.294   1.00 71.45 ? 303  GLU A OE1   1 
ATOM   2305 O OE2   . GLU A 1 303 ? 44.981  -14.272 6.327   1.00 47.04 ? 303  GLU A OE2   1 
ATOM   2306 N N     . ALA A 1 304 ? 43.094  -16.375 10.159  1.00 35.53 ? 304  ALA A N     1 
ATOM   2307 C CA    . ALA A 1 304 ? 42.356  -16.588 11.432  1.00 38.00 ? 304  ALA A CA    1 
ATOM   2308 C C     . ALA A 1 304 ? 41.438  -17.816 11.313  1.00 34.03 ? 304  ALA A C     1 
ATOM   2309 O O     . ALA A 1 304 ? 41.472  -18.671 12.211  1.00 34.44 ? 304  ALA A O     1 
ATOM   2310 C CB    . ALA A 1 304 ? 41.578  -15.359 11.806  1.00 38.78 ? 304  ALA A CB    1 
ATOM   2311 N N     . ILE A 1 305 ? 40.683  -17.925 10.222  1.00 35.05 ? 305  ILE A N     1 
ATOM   2312 C CA    . ILE A 1 305 ? 39.809  -19.115 9.947   1.00 35.39 ? 305  ILE A CA    1 
ATOM   2313 C C     . ILE A 1 305 ? 40.684  -20.373 9.907   1.00 35.66 ? 305  ILE A C     1 
ATOM   2314 O O     . ILE A 1 305 ? 40.304  -21.413 10.496  1.00 34.65 ? 305  ILE A O     1 
ATOM   2315 C CB    . ILE A 1 305 ? 39.019  -18.942 8.631   1.00 37.99 ? 305  ILE A CB    1 
ATOM   2316 C CG1   . ILE A 1 305 ? 38.092  -17.716 8.623   1.00 43.01 ? 305  ILE A CG1   1 
ATOM   2317 C CG2   . ILE A 1 305 ? 38.274  -20.225 8.270   1.00 35.69 ? 305  ILE A CG2   1 
ATOM   2318 C CD1   . ILE A 1 305 ? 37.350  -17.428 9.880   1.00 42.74 ? 305  ILE A CD1   1 
ATOM   2319 N N     . GLU A 1 306 ? 41.821  -20.302 9.209   1.00 35.93 ? 306  GLU A N     1 
ATOM   2320 C CA    . GLU A 1 306 ? 42.713  -21.476 9.033   1.00 35.63 ? 306  GLU A CA    1 
ATOM   2321 C C     . GLU A 1 306 ? 43.251  -21.878 10.401  1.00 31.86 ? 306  GLU A C     1 
ATOM   2322 O O     . GLU A 1 306 ? 43.363  -23.083 10.662  1.00 32.65 ? 306  GLU A O     1 
ATOM   2323 C CB    . GLU A 1 306 ? 43.817  -21.219 7.996   1.00 35.26 ? 306  GLU A CB    1 
ATOM   2324 C CG    . GLU A 1 306 ? 43.337  -21.309 6.554   1.00 38.59 ? 306  GLU A CG    1 
ATOM   2325 C CD    . GLU A 1 306 ? 42.453  -22.506 6.202   1.00 37.46 ? 306  GLU A CD    1 
ATOM   2326 O OE1   . GLU A 1 306 ? 42.732  -23.580 6.699   1.00 45.46 ? 306  GLU A OE1   1 
ATOM   2327 O OE2   . GLU A 1 306 ? 41.503  -22.345 5.437   1.00 43.78 ? 306  GLU A OE2   1 
ATOM   2328 N N     . ARG A 1 307 ? 43.566  -20.905 11.251  1.00 34.79 ? 307  ARG A N     1 
ATOM   2329 C CA    . ARG A 1 307 ? 44.072  -21.191 12.626  1.00 37.18 ? 307  ARG A CA    1 
ATOM   2330 C C     . ARG A 1 307 ? 42.997  -21.928 13.440  1.00 33.72 ? 307  ARG A C     1 
ATOM   2331 O O     . ARG A 1 307 ? 43.358  -22.828 14.201  1.00 33.94 ? 307  ARG A O     1 
ATOM   2332 C CB    . ARG A 1 307 ? 44.520  -19.905 13.330  1.00 38.88 ? 307  ARG A CB    1 
ATOM   2333 C CG    . ARG A 1 307 ? 46.020  -19.651 13.239  1.00 45.83 ? 307  ARG A CG    1 
ATOM   2334 C CD    . ARG A 1 307 ? 46.504  -18.608 14.241  1.00 49.78 ? 307  ARG A CD    1 
ATOM   2335 N NE    . ARG A 1 307 ? 45.811  -17.328 14.145  1.00 49.56 ? 307  ARG A NE    1 
ATOM   2336 C CZ    . ARG A 1 307 ? 45.946  -16.456 13.149  1.00 52.24 ? 307  ARG A CZ    1 
ATOM   2337 N NH1   . ARG A 1 307 ? 46.732  -16.707 12.115  1.00 58.51 ? 307  ARG A NH1   1 
ATOM   2338 N NH2   . ARG A 1 307 ? 45.270  -15.322 13.169  1.00 55.72 ? 307  ARG A NH2   1 
ATOM   2339 N N     . MET A 1 308 ? 41.725  -21.526 13.318  1.00 36.63 ? 308  MET A N     1 
ATOM   2340 C CA    . MET A 1 308 ? 40.594  -22.216 14.007  1.00 32.44 ? 308  MET A CA    1 
ATOM   2341 C C     . MET A 1 308 ? 40.503  -23.662 13.505  1.00 28.71 ? 308  MET A C     1 
ATOM   2342 O O     . MET A 1 308 ? 40.443  -24.572 14.339  1.00 32.20 ? 308  MET A O     1 
ATOM   2343 C CB    . MET A 1 308 ? 39.262  -21.524 13.726  1.00 32.43 ? 308  MET A CB    1 
ATOM   2344 C CG    . MET A 1 308 ? 39.165  -20.161 14.337  1.00 30.98 ? 308  MET A CG    1 
ATOM   2345 S SD    . MET A 1 308 ? 37.699  -19.320 13.745  1.00 34.65 ? 308  MET A SD    1 
ATOM   2346 C CE    . MET A 1 308 ? 38.115  -17.606 14.051  1.00 37.23 ? 308  MET A CE    1 
ATOM   2347 N N     . LYS A 1 309 ? 40.466  -23.869 12.195  1.00 29.37 ? 309  LYS A N     1 
ATOM   2348 C CA    . LYS A 1 309 ? 40.373  -25.234 11.608  1.00 33.48 ? 309  LYS A CA    1 
ATOM   2349 C C     . LYS A 1 309 ? 41.479  -26.137 12.171  1.00 34.11 ? 309  LYS A C     1 
ATOM   2350 O O     . LYS A 1 309 ? 41.179  -27.258 12.663  1.00 35.74 ? 309  LYS A O     1 
ATOM   2351 C CB    . LYS A 1 309 ? 40.545  -25.185 10.095  1.00 33.19 ? 309  LYS A CB    1 
ATOM   2352 C CG    . LYS A 1 309 ? 39.382  -24.614 9.297   1.00 37.29 ? 309  LYS A CG    1 
ATOM   2353 C CD    . LYS A 1 309 ? 39.750  -24.702 7.840   1.00 42.10 ? 309  LYS A CD    1 
ATOM   2354 C CE    . LYS A 1 309 ? 38.795  -24.051 6.882   1.00 48.86 ? 309  LYS A CE    1 
ATOM   2355 N NZ    . LYS A 1 309 ? 39.356  -24.110 5.510   1.00 49.14 ? 309  LYS A NZ    1 
ATOM   2356 N N     . LYS A 1 310 ? 42.722  -25.649 12.098  1.00 38.67 ? 310  LYS A N     1 
ATOM   2357 C CA    . LYS A 1 310 ? 43.935  -26.437 12.450  1.00 40.05 ? 310  LYS A CA    1 
ATOM   2358 C C     . LYS A 1 310 ? 43.942  -26.712 13.957  1.00 38.78 ? 310  LYS A C     1 
ATOM   2359 O O     . LYS A 1 310 ? 44.014  -27.886 14.348  1.00 42.63 ? 310  LYS A O     1 
ATOM   2360 C CB    . LYS A 1 310 ? 45.200  -25.683 12.006  1.00 44.69 ? 310  LYS A CB    1 
ATOM   2361 C CG    . LYS A 1 310 ? 46.480  -26.508 11.918  1.00 48.22 ? 310  LYS A CG    1 
ATOM   2362 C CD    . LYS A 1 310 ? 46.431  -27.519 10.774  1.00 58.09 ? 310  LYS A CD    1 
ATOM   2363 C CE    . LYS A 1 310 ? 47.741  -28.242 10.527  1.00 60.43 ? 310  LYS A CE    1 
ATOM   2364 N NZ    . LYS A 1 310 ? 48.034  -29.285 11.535  1.00 61.13 ? 310  LYS A NZ    1 
ATOM   2365 N N     . GLU A 1 311 ? 43.846  -25.664 14.774  1.00 37.13 ? 311  GLU A N     1 
ATOM   2366 C CA    . GLU A 1 311 ? 43.947  -25.773 16.253  1.00 39.09 ? 311  GLU A CA    1 
ATOM   2367 C C     . GLU A 1 311 ? 42.830  -26.691 16.778  1.00 40.32 ? 311  GLU A C     1 
ATOM   2368 O O     . GLU A 1 311 ? 43.097  -27.473 17.698  1.00 40.25 ? 311  GLU A O     1 
ATOM   2369 C CB    . GLU A 1 311 ? 43.914  -24.374 16.864  1.00 43.54 ? 311  GLU A CB    1 
ATOM   2370 C CG    . GLU A 1 311 ? 43.863  -24.351 18.392  1.00 55.03 ? 311  GLU A CG    1 
ATOM   2371 C CD    . GLU A 1 311 ? 45.116  -24.781 19.135  1.00 62.70 ? 311  GLU A CD    1 
ATOM   2372 O OE1   . GLU A 1 311 ? 45.828  -25.685 18.643  1.00 59.75 ? 311  GLU A OE1   1 
ATOM   2373 O OE2   . GLU A 1 311 ? 45.384  -24.186 20.213  1.00 67.04 ? 311  GLU A OE2   1 
ATOM   2374 N N     . LEU A 1 312 ? 41.634  -26.597 16.222  1.00 41.40 ? 312  LEU A N     1 
ATOM   2375 C CA    . LEU A 1 312 ? 40.511  -27.330 16.764  1.00 37.16 ? 312  LEU A CA    1 
ATOM   2376 C C     . LEU A 1 312 ? 40.158  -28.613 16.065  1.00 35.03 ? 312  LEU A C     1 
ATOM   2377 O O     . LEU A 1 312 ? 39.293  -29.311 16.511  1.00 40.90 ? 312  LEU A O     1 
ATOM   2378 C CB    . LEU A 1 312 ? 39.310  -26.413 16.804  1.00 35.75 ? 312  LEU A CB    1 
ATOM   2379 C CG    . LEU A 1 312 ? 39.402  -25.130 17.609  1.00 37.80 ? 312  LEU A CG    1 
ATOM   2380 C CD1   . LEU A 1 312 ? 38.281  -24.203 17.195  1.00 38.16 ? 312  LEU A CD1   1 
ATOM   2381 C CD2   . LEU A 1 312 ? 39.315  -25.447 19.085  1.00 38.50 ? 312  LEU A CD2   1 
ATOM   2382 N N     . GLY A 1 313 ? 40.820  -28.913 14.964  1.00 37.89 ? 313  GLY A N     1 
ATOM   2383 C CA    . GLY A 1 313 ? 40.534  -30.124 14.211  1.00 37.51 ? 313  GLY A CA    1 
ATOM   2384 C C     . GLY A 1 313 ? 39.190  -30.093 13.513  1.00 38.29 ? 313  GLY A C     1 
ATOM   2385 O O     . GLY A 1 313 ? 38.492  -31.077 13.487  1.00 41.18 ? 313  GLY A O     1 
ATOM   2386 N N     . LEU A 1 314 ? 38.844  -28.967 12.920  1.00 36.63 ? 314  LEU A N     1 
ATOM   2387 C CA    . LEU A 1 314 ? 37.553  -28.819 12.306  1.00 35.91 ? 314  LEU A CA    1 
ATOM   2388 C C     . LEU A 1 314 ? 37.698  -28.405 10.876  1.00 34.11 ? 314  LEU A C     1 
ATOM   2389 O O     . LEU A 1 314 ? 38.759  -28.029 10.457  1.00 34.50 ? 314  LEU A O     1 
ATOM   2390 C CB    . LEU A 1 314 ? 36.750  -27.759 13.052  1.00 37.10 ? 314  LEU A CB    1 
ATOM   2391 C CG    . LEU A 1 314 ? 36.404  -27.956 14.519  1.00 41.78 ? 314  LEU A CG    1 
ATOM   2392 C CD1   . LEU A 1 314 ? 35.774  -26.696 15.079  1.00 41.29 ? 314  LEU A CD1   1 
ATOM   2393 C CD2   . LEU A 1 314 ? 35.477  -29.143 14.676  1.00 36.59 ? 314  LEU A CD2   1 
ATOM   2394 N N     . GLY A 1 315 ? 36.626  -28.478 10.124  1.00 29.28 ? 315  GLY A N     1 
ATOM   2395 C CA    . GLY A 1 315 ? 36.648  -28.018 8.769   1.00 28.25 ? 315  GLY A CA    1 
ATOM   2396 C C     . GLY A 1 315 ? 35.948  -26.689 8.653   1.00 26.51 ? 315  GLY A C     1 
ATOM   2397 O O     . GLY A 1 315 ? 35.552  -26.142 9.650   1.00 28.25 ? 315  GLY A O     1 
ATOM   2398 N N     . TYR A 1 316 ? 35.848  -26.144 7.453   1.00 27.12 ? 316  TYR A N     1 
ATOM   2399 C CA    . TYR A 1 316 ? 35.082  -24.920 7.290   1.00 27.51 ? 316  TYR A CA    1 
ATOM   2400 C C     . TYR A 1 316 ? 33.628  -25.310 7.528   1.00 27.65 ? 316  TYR A C     1 
ATOM   2401 O O     . TYR A 1 316 ? 32.934  -24.583 8.136   1.00 25.14 ? 316  TYR A O     1 
ATOM   2402 C CB    . TYR A 1 316 ? 35.238  -24.257 5.933   1.00 27.44 ? 316  TYR A CB    1 
ATOM   2403 C CG    . TYR A 1 316 ? 34.539  -22.931 5.929   1.00 28.82 ? 316  TYR A CG    1 
ATOM   2404 C CD1   . TYR A 1 316 ? 35.187  -21.793 6.351   1.00 29.11 ? 316  TYR A CD1   1 
ATOM   2405 C CD2   . TYR A 1 316 ? 33.208  -22.826 5.564   1.00 27.05 ? 316  TYR A CD2   1 
ATOM   2406 C CE1   . TYR A 1 316 ? 34.534  -20.584 6.390   1.00 29.28 ? 316  TYR A CE1   1 
ATOM   2407 C CE2   . TYR A 1 316 ? 32.551  -21.633 5.610   1.00 28.25 ? 316  TYR A CE2   1 
ATOM   2408 C CZ    . TYR A 1 316 ? 33.217  -20.515 6.018   1.00 30.01 ? 316  TYR A CZ    1 
ATOM   2409 O OH    . TYR A 1 316 ? 32.543  -19.336 6.051   1.00 26.76 ? 316  TYR A OH    1 
ATOM   2410 N N     . TRP A 1 317 ? 33.201  -26.436 6.997   1.00 28.58 ? 317  TRP A N     1 
ATOM   2411 C CA    . TRP A 1 317 ? 31.847  -27.010 7.198   1.00 26.09 ? 317  TRP A CA    1 
ATOM   2412 C C     . TRP A 1 317 ? 31.981  -28.269 8.039   1.00 26.12 ? 317  TRP A C     1 
ATOM   2413 O O     . TRP A 1 317 ? 32.841  -29.131 7.740   1.00 25.87 ? 317  TRP A O     1 
ATOM   2414 C CB    . TRP A 1 317 ? 31.140  -27.289 5.866   1.00 25.01 ? 317  TRP A CB    1 
ATOM   2415 C CG    . TRP A 1 317 ? 30.917  -26.060 5.052   1.00 24.10 ? 317  TRP A CG    1 
ATOM   2416 C CD1   . TRP A 1 317 ? 31.537  -25.744 3.880   1.00 25.86 ? 317  TRP A CD1   1 
ATOM   2417 C CD2   . TRP A 1 317 ? 30.011  -24.979 5.336   1.00 26.74 ? 317  TRP A CD2   1 
ATOM   2418 N NE1   . TRP A 1 317 ? 31.085  -24.543 3.419   1.00 28.29 ? 317  TRP A NE1   1 
ATOM   2419 C CE2   . TRP A 1 317 ? 30.140  -24.053 4.281   1.00 25.77 ? 317  TRP A CE2   1 
ATOM   2420 C CE3   . TRP A 1 317 ? 29.097  -24.702 6.365   1.00 23.66 ? 317  TRP A CE3   1 
ATOM   2421 C CZ2   . TRP A 1 317 ? 29.421  -22.858 4.231   1.00 28.05 ? 317  TRP A CZ2   1 
ATOM   2422 C CZ3   . TRP A 1 317 ? 28.371  -23.533 6.299   1.00 25.05 ? 317  TRP A CZ3   1 
ATOM   2423 C CH2   . TRP A 1 317 ? 28.524  -22.623 5.246   1.00 25.45 ? 317  TRP A CH2   1 
ATOM   2424 N N     . ASN A 1 318 ? 31.145  -28.355 9.068   1.00 24.71 ? 318  ASN A N     1 
ATOM   2425 C CA    . ASN A 1 318 ? 31.109  -29.452 10.043  1.00 23.42 ? 318  ASN A CA    1 
ATOM   2426 C C     . ASN A 1 318 ? 29.688  -30.023 10.102  1.00 23.58 ? 318  ASN A C     1 
ATOM   2427 O O     . ASN A 1 318 ? 28.778  -29.324 10.580  1.00 26.01 ? 318  ASN A O     1 
ATOM   2428 C CB    . ASN A 1 318 ? 31.657  -28.951 11.360  1.00 21.99 ? 318  ASN A CB    1 
ATOM   2429 C CG    . ASN A 1 318 ? 33.005  -28.301 11.129  1.00 28.03 ? 318  ASN A CG    1 
ATOM   2430 O OD1   . ASN A 1 318 ? 34.004  -29.006 11.031  1.00 26.58 ? 318  ASN A OD1   1 
ATOM   2431 N ND2   . ASN A 1 318 ? 33.036  -26.976 11.013  1.00 24.34 ? 318  ASN A ND2   1 
ATOM   2432 N N     . PHE A 1 319 ? 29.538  -31.250 9.623   1.00 25.20 ? 319  PHE A N     1 
ATOM   2433 C CA    . PHE A 1 319 ? 28.258  -31.990 9.508   1.00 26.87 ? 319  PHE A CA    1 
ATOM   2434 C C     . PHE A 1 319 ? 28.063  -32.808 10.773  1.00 27.36 ? 319  PHE A C     1 
ATOM   2435 O O     . PHE A 1 319 ? 29.010  -33.470 11.178  1.00 30.21 ? 319  PHE A O     1 
ATOM   2436 C CB    . PHE A 1 319 ? 28.287  -32.925 8.302   1.00 29.29 ? 319  PHE A CB    1 
ATOM   2437 C CG    . PHE A 1 319 ? 26.987  -33.636 8.019   1.00 27.65 ? 319  PHE A CG    1 
ATOM   2438 C CD1   . PHE A 1 319 ? 26.641  -34.787 8.706   1.00 27.13 ? 319  PHE A CD1   1 
ATOM   2439 C CD2   . PHE A 1 319 ? 26.135  -33.168 7.037   1.00 29.39 ? 319  PHE A CD2   1 
ATOM   2440 C CE1   . PHE A 1 319 ? 25.448  -35.434 8.444   1.00 28.00 ? 319  PHE A CE1   1 
ATOM   2441 C CE2   . PHE A 1 319 ? 24.959  -33.838 6.741   1.00 30.22 ? 319  PHE A CE2   1 
ATOM   2442 C CZ    . PHE A 1 319 ? 24.615  -34.965 7.452   1.00 31.06 ? 319  PHE A CZ    1 
ATOM   2443 N N     . TYR A 1 320 ? 26.876  -32.741 11.376  1.00 26.18 ? 320  TYR A N     1 
ATOM   2444 C CA    . TYR A 1 320 ? 26.500  -33.545 12.563  1.00 24.90 ? 320  TYR A CA    1 
ATOM   2445 C C     . TYR A 1 320 ? 25.183  -34.243 12.281  1.00 24.79 ? 320  TYR A C     1 
ATOM   2446 O O     . TYR A 1 320 ? 24.261  -33.566 11.783  1.00 23.04 ? 320  TYR A O     1 
ATOM   2447 C CB    . TYR A 1 320 ? 26.380  -32.696 13.832  1.00 24.64 ? 320  TYR A CB    1 
ATOM   2448 C CG    . TYR A 1 320 ? 27.661  -31.982 14.158  1.00 25.84 ? 320  TYR A CG    1 
ATOM   2449 C CD1   . TYR A 1 320 ? 28.614  -32.587 14.967  1.00 26.87 ? 320  TYR A CD1   1 
ATOM   2450 C CD2   . TYR A 1 320 ? 27.958  -30.759 13.595  1.00 25.31 ? 320  TYR A CD2   1 
ATOM   2451 C CE1   . TYR A 1 320 ? 29.819  -31.960 15.255  1.00 26.38 ? 320  TYR A CE1   1 
ATOM   2452 C CE2   . TYR A 1 320 ? 29.165  -30.126 13.861  1.00 24.63 ? 320  TYR A CE2   1 
ATOM   2453 C CZ    . TYR A 1 320 ? 30.108  -30.747 14.665  1.00 27.92 ? 320  TYR A CZ    1 
ATOM   2454 O OH    . TYR A 1 320 ? 31.286  -30.124 14.947  1.00 28.25 ? 320  TYR A OH    1 
ATOM   2455 N N     . GLY A 1 321 ? 25.163  -35.553 12.502  1.00 24.30 ? 321  GLY A N     1 
ATOM   2456 C CA    . GLY A 1 321 ? 23.994  -36.419 12.304  1.00 25.15 ? 321  GLY A CA    1 
ATOM   2457 C C     . GLY A 1 321 ? 23.976  -37.490 13.350  1.00 28.04 ? 321  GLY A C     1 
ATOM   2458 O O     . GLY A 1 321 ? 25.036  -37.764 13.961  1.00 27.27 ? 321  GLY A O     1 
ATOM   2459 N N     . THR A 1 322 ? 22.806  -38.082 13.553  1.00 28.70 ? 322  THR A N     1 
ATOM   2460 C CA    . THR A 1 322 ? 22.609  -39.154 14.541  1.00 27.25 ? 322  THR A CA    1 
ATOM   2461 C C     . THR A 1 322 ? 21.913  -40.293 13.811  1.00 28.86 ? 322  THR A C     1 
ATOM   2462 O O     . THR A 1 322 ? 21.090  -40.037 12.894  1.00 25.42 ? 322  THR A O     1 
ATOM   2463 C CB    . THR A 1 322 ? 21.899  -38.645 15.802  1.00 29.50 ? 322  THR A CB    1 
ATOM   2464 O OG1   . THR A 1 322 ? 22.798  -37.730 16.442  1.00 26.67 ? 322  THR A OG1   1 
ATOM   2465 C CG2   . THR A 1 322 ? 21.523  -39.754 16.761  1.00 25.68 ? 322  THR A CG2   1 
ATOM   2466 N N     . LEU A 1 323 ? 22.317  -41.497 14.180  1.00 27.60 ? 323  LEU A N     1 
ATOM   2467 C CA    . LEU A 1 323 ? 21.717  -42.747 13.691  1.00 30.88 ? 323  LEU A CA    1 
ATOM   2468 C C     . LEU A 1 323 ? 21.068  -43.440 14.878  1.00 27.59 ? 323  LEU A C     1 
ATOM   2469 O O     . LEU A 1 323 ? 21.606  -43.350 15.985  1.00 27.26 ? 323  LEU A O     1 
ATOM   2470 C CB    . LEU A 1 323 ? 22.811  -43.596 13.046  1.00 31.63 ? 323  LEU A CB    1 
ATOM   2471 C CG    . LEU A 1 323 ? 23.474  -42.957 11.830  1.00 30.10 ? 323  LEU A CG    1 
ATOM   2472 C CD1   . LEU A 1 323 ? 24.657  -43.788 11.351  1.00 32.09 ? 323  LEU A CD1   1 
ATOM   2473 C CD2   . LEU A 1 323 ? 22.466  -42.776 10.718  1.00 28.60 ? 323  LEU A CD2   1 
ATOM   2474 N N     . TYR A 1 324 ? 19.958  -44.108 14.613  1.00 28.10 ? 324  TYR A N     1 
ATOM   2475 C CA    . TYR A 1 324 ? 19.144  -44.814 15.633  1.00 29.82 ? 324  TYR A CA    1 
ATOM   2476 C C     . TYR A 1 324 ? 18.901  -46.261 15.184  1.00 29.80 ? 324  TYR A C     1 
ATOM   2477 O O     . TYR A 1 324 ? 18.757  -46.513 13.971  1.00 32.15 ? 324  TYR A O     1 
ATOM   2478 C CB    . TYR A 1 324 ? 17.796  -44.106 15.808  1.00 29.90 ? 324  TYR A CB    1 
ATOM   2479 C CG    . TYR A 1 324 ? 17.846  -42.615 16.017  1.00 28.52 ? 324  TYR A CG    1 
ATOM   2480 C CD1   . TYR A 1 324 ? 18.207  -42.061 17.233  1.00 28.72 ? 324  TYR A CD1   1 
ATOM   2481 C CD2   . TYR A 1 324 ? 17.517  -41.742 14.984  1.00 29.07 ? 324  TYR A CD2   1 
ATOM   2482 C CE1   . TYR A 1 324 ? 18.261  -40.684 17.418  1.00 28.89 ? 324  TYR A CE1   1 
ATOM   2483 C CE2   . TYR A 1 324 ? 17.579  -40.363 15.150  1.00 28.28 ? 324  TYR A CE2   1 
ATOM   2484 C CZ    . TYR A 1 324 ? 17.932  -39.826 16.380  1.00 27.63 ? 324  TYR A CZ    1 
ATOM   2485 O OH    . TYR A 1 324 ? 17.969  -38.468 16.573  1.00 26.36 ? 324  TYR A OH    1 
ATOM   2486 N N     . GLY A 1 325 ? 18.784  -47.164 16.155  1.00 30.40 ? 325  GLY A N     1 
ATOM   2487 C CA    . GLY A 1 325 ? 18.326  -48.543 15.942  1.00 35.07 ? 325  GLY A CA    1 
ATOM   2488 C C     . GLY A 1 325 ? 19.281  -49.541 16.585  1.00 33.34 ? 325  GLY A C     1 
ATOM   2489 O O     . GLY A 1 325 ? 20.182  -49.161 17.333  1.00 34.36 ? 325  GLY A O     1 
ATOM   2490 N N     . PRO A 1 326 ? 19.148  -50.844 16.260  1.00 36.42 ? 326  PRO A N     1 
ATOM   2491 C CA    . PRO A 1 326 ? 20.106  -51.835 16.731  1.00 38.70 ? 326  PRO A CA    1 
ATOM   2492 C C     . PRO A 1 326 ? 21.474  -51.532 16.115  1.00 38.73 ? 326  PRO A C     1 
ATOM   2493 O O     . PRO A 1 326 ? 21.560  -50.974 15.013  1.00 38.61 ? 326  PRO A O     1 
ATOM   2494 C CB    . PRO A 1 326 ? 19.539  -53.207 16.317  1.00 37.06 ? 326  PRO A CB    1 
ATOM   2495 C CG    . PRO A 1 326 ? 18.376  -52.910 15.387  1.00 41.96 ? 326  PRO A CG    1 
ATOM   2496 C CD    . PRO A 1 326 ? 18.091  -51.418 15.414  1.00 39.32 ? 326  PRO A CD    1 
ATOM   2497 N N     . PRO A 1 327 ? 22.582  -51.867 16.816  1.00 40.12 ? 327  PRO A N     1 
ATOM   2498 C CA    . PRO A 1 327 ? 23.930  -51.594 16.310  1.00 42.93 ? 327  PRO A CA    1 
ATOM   2499 C C     . PRO A 1 327 ? 24.190  -52.010 14.855  1.00 41.41 ? 327  PRO A C     1 
ATOM   2500 O O     . PRO A 1 327 ? 25.003  -51.369 14.222  1.00 47.00 ? 327  PRO A O     1 
ATOM   2501 C CB    . PRO A 1 327 ? 24.824  -52.385 17.281  1.00 45.62 ? 327  PRO A CB    1 
ATOM   2502 C CG    . PRO A 1 327 ? 24.055  -52.337 18.588  1.00 46.96 ? 327  PRO A CG    1 
ATOM   2503 C CD    . PRO A 1 327 ? 22.602  -52.451 18.171  1.00 42.65 ? 327  PRO A CD    1 
ATOM   2504 N N     . GLN A 1 328 ? 23.530  -53.053 14.356  1.00 41.21 ? 328  GLN A N     1 
ATOM   2505 C CA    . GLN A 1 328 ? 23.706  -53.562 12.967  1.00 46.85 ? 328  GLN A CA    1 
ATOM   2506 C C     . GLN A 1 328 ? 23.146  -52.547 11.962  1.00 43.26 ? 328  GLN A C     1 
ATOM   2507 O O     . GLN A 1 328 ? 23.750  -52.366 10.887  1.00 33.59 ? 328  GLN A O     1 
ATOM   2508 C CB    . GLN A 1 328 ? 22.982  -54.892 12.759  1.00 53.96 ? 328  GLN A CB    1 
ATOM   2509 C CG    . GLN A 1 328 ? 23.388  -55.989 13.739  1.00 67.44 ? 328  GLN A CG    1 
ATOM   2510 C CD    . GLN A 1 328 ? 22.195  -56.658 14.384  1.00 71.74 ? 328  GLN A CD    1 
ATOM   2511 O OE1   . GLN A 1 328 ? 21.259  -57.106 13.717  1.00 77.49 ? 328  GLN A OE1   1 
ATOM   2512 N NE2   . GLN A 1 328 ? 22.213  -56.701 15.705  1.00 72.59 ? 328  GLN A NE2   1 
ATOM   2513 N N     . LEU A 1 329 ? 21.990  -51.954 12.263  1.00 39.19 ? 329  LEU A N     1 
ATOM   2514 C CA    . LEU A 1 329 ? 21.393  -50.906 11.398  1.00 35.49 ? 329  LEU A CA    1 
ATOM   2515 C C     . LEU A 1 329 ? 22.308  -49.670 11.420  1.00 32.64 ? 329  LEU A C     1 
ATOM   2516 O O     . LEU A 1 329 ? 22.602  -49.134 10.335  1.00 33.23 ? 329  LEU A O     1 
ATOM   2517 C CB    . LEU A 1 329 ? 19.976  -50.598 11.896  1.00 36.28 ? 329  LEU A CB    1 
ATOM   2518 C CG    . LEU A 1 329 ? 19.177  -49.595 11.061  1.00 35.73 ? 329  LEU A CG    1 
ATOM   2519 C CD1   . LEU A 1 329 ? 18.979  -50.099 9.635   1.00 34.99 ? 329  LEU A CD1   1 
ATOM   2520 C CD2   . LEU A 1 329 ? 17.829  -49.316 11.716  1.00 36.53 ? 329  LEU A CD2   1 
ATOM   2521 N N     . ILE A 1 330 ? 22.774  -49.245 12.598  1.00 33.95 ? 330  ILE A N     1 
ATOM   2522 C CA    . ILE A 1 330 ? 23.641  -48.039 12.752  1.00 35.44 ? 330  ILE A CA    1 
ATOM   2523 C C     . ILE A 1 330 ? 24.891  -48.243 11.880  1.00 39.08 ? 330  ILE A C     1 
ATOM   2524 O O     . ILE A 1 330 ? 25.151  -47.378 11.018  1.00 35.87 ? 330  ILE A O     1 
ATOM   2525 C CB    . ILE A 1 330 ? 23.963  -47.761 14.234  1.00 34.27 ? 330  ILE A CB    1 
ATOM   2526 C CG1   . ILE A 1 330 ? 22.718  -47.279 14.990  1.00 32.31 ? 330  ILE A CG1   1 
ATOM   2527 C CG2   . ILE A 1 330 ? 25.133  -46.783 14.357  1.00 33.94 ? 330  ILE A CG2   1 
ATOM   2528 C CD1   . ILE A 1 330 ? 22.881  -47.166 16.495  1.00 31.06 ? 330  ILE A CD1   1 
ATOM   2529 N N     . GLU A 1 331 ? 25.601  -49.368 12.050  1.00 39.66 ? 331  GLU A N     1 
ATOM   2530 C CA    . GLU A 1 331 ? 26.833  -49.687 11.275  1.00 44.97 ? 331  GLU A CA    1 
ATOM   2531 C C     . GLU A 1 331 ? 26.530  -49.578 9.779   1.00 39.18 ? 331  GLU A C     1 
ATOM   2532 O O     . GLU A 1 331 ? 27.356  -49.008 9.036   1.00 33.50 ? 331  GLU A O     1 
ATOM   2533 C CB    . GLU A 1 331 ? 27.330  -51.111 11.536  1.00 52.93 ? 331  GLU A CB    1 
ATOM   2534 C CG    . GLU A 1 331 ? 27.859  -51.354 12.938  1.00 65.57 ? 331  GLU A CG    1 
ATOM   2535 C CD    . GLU A 1 331 ? 27.902  -52.831 13.334  1.00 76.97 ? 331  GLU A CD    1 
ATOM   2536 O OE1   . GLU A 1 331 ? 28.088  -53.689 12.429  1.00 75.17 ? 331  GLU A OE1   1 
ATOM   2537 O OE2   . GLU A 1 331 ? 27.775  -53.133 14.548  1.00 81.86 ? 331  GLU A OE2   1 
ATOM   2538 N N     . MET A 1 332 ? 25.395  -50.139 9.357   1.00 38.40 ? 332  MET A N     1 
ATOM   2539 C CA    . MET A 1 332 ? 25.030  -50.250 7.925   1.00 39.02 ? 332  MET A CA    1 
ATOM   2540 C C     . MET A 1 332 ? 24.782  -48.837 7.401   1.00 36.65 ? 332  MET A C     1 
ATOM   2541 O O     . MET A 1 332 ? 25.412  -48.464 6.418   1.00 37.79 ? 332  MET A O     1 
ATOM   2542 C CB    . MET A 1 332 ? 23.781  -51.114 7.754   1.00 47.09 ? 332  MET A CB    1 
ATOM   2543 C CG    . MET A 1 332 ? 23.417  -51.416 6.326   1.00 52.38 ? 332  MET A CG    1 
ATOM   2544 S SD    . MET A 1 332 ? 21.952  -52.528 6.229   1.00 66.65 ? 332  MET A SD    1 
ATOM   2545 C CE    . MET A 1 332 ? 22.440  -53.882 7.303   1.00 60.97 ? 332  MET A CE    1 
ATOM   2546 N N     . ASN A 1 333 ? 23.950  -48.057 8.090   1.00 33.41 ? 333  ASN A N     1 
ATOM   2547 C CA    . ASN A 1 333 ? 23.619  -46.671 7.662   1.00 33.11 ? 333  ASN A CA    1 
ATOM   2548 C C     . ASN A 1 333 ? 24.881  -45.801 7.676   1.00 29.26 ? 333  ASN A C     1 
ATOM   2549 O O     . ASN A 1 333 ? 25.069  -45.037 6.705   1.00 29.62 ? 333  ASN A O     1 
ATOM   2550 C CB    . ASN A 1 333 ? 22.496  -46.084 8.520   1.00 29.78 ? 333  ASN A CB    1 
ATOM   2551 C CG    . ASN A 1 333 ? 21.147  -46.590 8.064   1.00 29.99 ? 333  ASN A CG    1 
ATOM   2552 O OD1   . ASN A 1 333 ? 20.974  -46.873 6.874   1.00 31.09 ? 333  ASN A OD1   1 
ATOM   2553 N ND2   . ASN A 1 333 ? 20.200  -46.669 8.988   1.00 29.44 ? 333  ASN A ND2   1 
ATOM   2554 N N     . TYR A 1 334 ? 25.710  -45.910 8.717   1.00 29.10 ? 334  TYR A N     1 
ATOM   2555 C CA    . TYR A 1 334 ? 26.964  -45.125 8.834   1.00 32.24 ? 334  TYR A CA    1 
ATOM   2556 C C     . TYR A 1 334 ? 27.878  -45.466 7.649   1.00 34.97 ? 334  TYR A C     1 
ATOM   2557 O O     . TYR A 1 334 ? 28.515  -44.552 7.086   1.00 33.20 ? 334  TYR A O     1 
ATOM   2558 C CB    . TYR A 1 334 ? 27.662  -45.404 10.164  1.00 34.26 ? 334  TYR A CB    1 
ATOM   2559 C CG    . TYR A 1 334 ? 28.790  -44.459 10.488  1.00 37.93 ? 334  TYR A CG    1 
ATOM   2560 C CD1   . TYR A 1 334 ? 28.639  -43.088 10.329  1.00 36.35 ? 334  TYR A CD1   1 
ATOM   2561 C CD2   . TYR A 1 334 ? 30.003  -44.925 10.978  1.00 38.49 ? 334  TYR A CD2   1 
ATOM   2562 C CE1   . TYR A 1 334 ? 29.666  -42.212 10.634  1.00 39.90 ? 334  TYR A CE1   1 
ATOM   2563 C CE2   . TYR A 1 334 ? 31.039  -44.059 11.295  1.00 38.03 ? 334  TYR A CE2   1 
ATOM   2564 C CZ    . TYR A 1 334 ? 30.869  -42.693 11.126  1.00 40.91 ? 334  TYR A CZ    1 
ATOM   2565 O OH    . TYR A 1 334 ? 31.850  -41.788 11.417  1.00 39.06 ? 334  TYR A OH    1 
ATOM   2566 N N     . GLY A 1 335 ? 27.935  -46.752 7.284   1.00 34.37 ? 335  GLY A N     1 
ATOM   2567 C CA    . GLY A 1 335 ? 28.639  -47.230 6.079   1.00 36.29 ? 335  GLY A CA    1 
ATOM   2568 C C     . GLY A 1 335 ? 28.192  -46.488 4.834   1.00 35.12 ? 335  GLY A C     1 
ATOM   2569 O O     . GLY A 1 335 ? 29.060  -46.022 4.070   1.00 32.91 ? 335  GLY A O     1 
ATOM   2570 N N     . ILE A 1 336 ? 26.881  -46.366 4.619   1.00 31.60 ? 336  ILE A N     1 
ATOM   2571 C CA    . ILE A 1 336 ? 26.316  -45.671 3.430   1.00 32.52 ? 336  ILE A CA    1 
ATOM   2572 C C     . ILE A 1 336 ? 26.720  -44.186 3.499   1.00 31.34 ? 336  ILE A C     1 
ATOM   2573 O O     . ILE A 1 336 ? 27.101  -43.624 2.459   1.00 29.65 ? 336  ILE A O     1 
ATOM   2574 C CB    . ILE A 1 336 ? 24.789  -45.872 3.336   1.00 33.20 ? 336  ILE A CB    1 
ATOM   2575 C CG1   . ILE A 1 336 ? 24.389  -47.339 3.161   1.00 34.71 ? 336  ILE A CG1   1 
ATOM   2576 C CG2   . ILE A 1 336 ? 24.209  -45.008 2.228   1.00 34.19 ? 336  ILE A CG2   1 
ATOM   2577 C CD1   . ILE A 1 336 ? 22.898  -47.630 3.456   1.00 36.18 ? 336  ILE A CD1   1 
ATOM   2578 N N     . ILE A 1 337 ? 26.587  -43.560 4.670   1.00 32.43 ? 337  ILE A N     1 
ATOM   2579 C CA    . ILE A 1 337 ? 26.931  -42.125 4.893   1.00 34.40 ? 337  ILE A CA    1 
ATOM   2580 C C     . ILE A 1 337 ? 28.416  -41.908 4.566   1.00 32.41 ? 337  ILE A C     1 
ATOM   2581 O O     . ILE A 1 337 ? 28.711  -40.966 3.830   1.00 31.66 ? 337  ILE A O     1 
ATOM   2582 C CB    . ILE A 1 337 ? 26.606  -41.686 6.340   1.00 33.82 ? 337  ILE A CB    1 
ATOM   2583 C CG1   . ILE A 1 337 ? 25.126  -41.855 6.692   1.00 37.18 ? 337  ILE A CG1   1 
ATOM   2584 C CG2   . ILE A 1 337 ? 27.069  -40.264 6.594   1.00 32.26 ? 337  ILE A CG2   1 
ATOM   2585 C CD1   . ILE A 1 337 ? 24.213  -41.411 5.620   1.00 40.90 ? 337  ILE A CD1   1 
ATOM   2586 N N     . LYS A 1 338 ? 29.313  -42.707 5.152   1.00 33.09 ? 338  LYS A N     1 
ATOM   2587 C CA    . LYS A 1 338 ? 30.782  -42.573 4.956   1.00 35.14 ? 338  LYS A CA    1 
ATOM   2588 C C     . LYS A 1 338 ? 31.103  -42.724 3.471   1.00 34.78 ? 338  LYS A C     1 
ATOM   2589 O O     . LYS A 1 338 ? 31.839  -41.873 2.936   1.00 39.95 ? 338  LYS A O     1 
ATOM   2590 C CB    . LYS A 1 338 ? 31.554  -43.601 5.783   1.00 38.02 ? 338  LYS A CB    1 
ATOM   2591 C CG    . LYS A 1 338 ? 31.717  -43.254 7.251   1.00 40.28 ? 338  LYS A CG    1 
ATOM   2592 C CD    . LYS A 1 338 ? 32.576  -44.245 7.996   1.00 42.45 ? 338  LYS A CD    1 
ATOM   2593 C CE    . LYS A 1 338 ? 32.060  -45.668 7.878   1.00 48.47 ? 338  LYS A CE    1 
ATOM   2594 N NZ    . LYS A 1 338 ? 32.718  -46.603 8.819   1.00 51.46 ? 338  LYS A NZ    1 
ATOM   2595 N N     . ASP A 1 339 ? 30.516  -43.723 2.813   1.00 34.55 ? 339  ASP A N     1 
ATOM   2596 C CA    . ASP A 1 339 ? 30.722  -43.951 1.363   1.00 38.88 ? 339  ASP A CA    1 
ATOM   2597 C C     . ASP A 1 339 ? 30.293  -42.713 0.562   1.00 39.76 ? 339  ASP A C     1 
ATOM   2598 O O     . ASP A 1 339 ? 31.054  -42.299 -0.348  1.00 38.63 ? 339  ASP A O     1 
ATOM   2599 C CB    . ASP A 1 339 ? 29.991  -45.195 0.886   1.00 42.78 ? 339  ASP A CB    1 
ATOM   2600 C CG    . ASP A 1 339 ? 30.055  -45.364 -0.620  1.00 58.23 ? 339  ASP A CG    1 
ATOM   2601 O OD1   . ASP A 1 339 ? 31.137  -45.777 -1.118  1.00 69.39 ? 339  ASP A OD1   1 
ATOM   2602 O OD2   . ASP A 1 339 ? 29.035  -45.047 -1.294  1.00 63.47 ? 339  ASP A OD2   1 
ATOM   2603 N N     . ALA A 1 340 ? 29.116  -42.143 0.853   1.00 35.18 ? 340  ALA A N     1 
ATOM   2604 C CA    . ALA A 1 340 ? 28.528  -41.026 0.081   1.00 33.38 ? 340  ALA A CA    1 
ATOM   2605 C C     . ALA A 1 340 ? 29.363  -39.756 0.301   1.00 30.37 ? 340  ALA A C     1 
ATOM   2606 O O     . ALA A 1 340 ? 29.856  -39.190 -0.682  1.00 33.90 ? 340  ALA A O     1 
ATOM   2607 C CB    . ALA A 1 340 ? 27.074  -40.834 0.450   1.00 35.35 ? 340  ALA A CB    1 
ATOM   2608 N N     . PHE A 1 341 ? 29.548  -39.313 1.540   1.00 31.44 ? 341  PHE A N     1 
ATOM   2609 C CA    . PHE A 1 341 ? 30.261  -38.035 1.824   1.00 30.27 ? 341  PHE A CA    1 
ATOM   2610 C C     . PHE A 1 341 ? 31.781  -38.163 1.641   1.00 32.01 ? 341  PHE A C     1 
ATOM   2611 O O     . PHE A 1 341 ? 32.413  -37.118 1.382   1.00 32.05 ? 341  PHE A O     1 
ATOM   2612 C CB    . PHE A 1 341 ? 29.911  -37.529 3.216   1.00 29.93 ? 341  PHE A CB    1 
ATOM   2613 C CG    . PHE A 1 341 ? 28.516  -36.969 3.312   1.00 30.85 ? 341  PHE A CG    1 
ATOM   2614 C CD1   . PHE A 1 341 ? 28.200  -35.737 2.756   1.00 31.35 ? 341  PHE A CD1   1 
ATOM   2615 C CD2   . PHE A 1 341 ? 27.518  -37.678 3.957   1.00 31.02 ? 341  PHE A CD2   1 
ATOM   2616 C CE1   . PHE A 1 341 ? 26.919  -35.221 2.865   1.00 30.25 ? 341  PHE A CE1   1 
ATOM   2617 C CE2   . PHE A 1 341 ? 26.242  -37.153 4.070   1.00 31.37 ? 341  PHE A CE2   1 
ATOM   2618 C CZ    . PHE A 1 341 ? 25.947  -35.923 3.532   1.00 30.76 ? 341  PHE A CZ    1 
ATOM   2619 N N     . GLY A 1 342 ? 32.331  -39.378 1.767   1.00 36.08 ? 342  GLY A N     1 
ATOM   2620 C CA    . GLY A 1 342 ? 33.742  -39.716 1.497   1.00 39.64 ? 342  GLY A CA    1 
ATOM   2621 C C     . GLY A 1 342 ? 34.162  -39.429 0.062   1.00 38.04 ? 342  GLY A C     1 
ATOM   2622 O O     . GLY A 1 342 ? 35.374  -39.341 -0.166  1.00 38.51 ? 342  GLY A O     1 
ATOM   2623 N N     . GLN A 1 343 ? 33.208  -39.265 -0.856  1.00 35.98 ? 343  GLN A N     1 
ATOM   2624 C CA    . GLN A 1 343 ? 33.459  -38.849 -2.262  1.00 41.49 ? 343  GLN A CA    1 
ATOM   2625 C C     . GLN A 1 343 ? 34.057  -37.432 -2.278  1.00 42.29 ? 343  GLN A C     1 
ATOM   2626 O O     . GLN A 1 343 ? 34.607  -37.036 -3.326  1.00 39.01 ? 343  GLN A O     1 
ATOM   2627 C CB    . GLN A 1 343 ? 32.176  -38.854 -3.096  1.00 45.17 ? 343  GLN A CB    1 
ATOM   2628 C CG    . GLN A 1 343 ? 31.483  -40.209 -3.181  1.00 50.75 ? 343  GLN A CG    1 
ATOM   2629 C CD    . GLN A 1 343 ? 30.067  -40.114 -3.712  1.00 60.76 ? 343  GLN A CD    1 
ATOM   2630 O OE1   . GLN A 1 343 ? 29.169  -39.466 -3.140  1.00 49.74 ? 343  GLN A OE1   1 
ATOM   2631 N NE2   . GLN A 1 343 ? 29.851  -40.798 -4.825  1.00 68.76 ? 343  GLN A NE2   1 
ATOM   2632 N N     . ILE A 1 344 ? 33.880  -36.665 -1.196  1.00 35.82 ? 344  ILE A N     1 
ATOM   2633 C CA    . ILE A 1 344 ? 34.418  -35.281 -1.088  1.00 35.69 ? 344  ILE A CA    1 
ATOM   2634 C C     . ILE A 1 344 ? 35.832  -35.383 -0.525  1.00 33.26 ? 344  ILE A C     1 
ATOM   2635 O O     . ILE A 1 344 ? 36.020  -35.748 0.634   1.00 32.77 ? 344  ILE A O     1 
ATOM   2636 C CB    . ILE A 1 344 ? 33.510  -34.362 -0.237  1.00 33.40 ? 344  ILE A CB    1 
ATOM   2637 C CG1   . ILE A 1 344 ? 32.084  -34.316 -0.793  1.00 32.74 ? 344  ILE A CG1   1 
ATOM   2638 C CG2   . ILE A 1 344 ? 34.125  -32.971 -0.147  1.00 33.79 ? 344  ILE A CG2   1 
ATOM   2639 C CD1   . ILE A 1 344 ? 31.123  -33.419 -0.018  1.00 33.07 ? 344  ILE A CD1   1 
ATOM   2640 N N     . PRO A 1 345 ? 36.873  -35.035 -1.322  1.00 36.21 ? 345  PRO A N     1 
ATOM   2641 C CA    . PRO A 1 345 ? 38.252  -35.030 -0.829  1.00 35.10 ? 345  PRO A CA    1 
ATOM   2642 C C     . PRO A 1 345 ? 38.386  -34.170 0.433   1.00 34.80 ? 345  PRO A C     1 
ATOM   2643 O O     . PRO A 1 345 ? 37.842  -33.090 0.462   1.00 36.33 ? 345  PRO A O     1 
ATOM   2644 C CB    . PRO A 1 345 ? 39.052  -34.413 -1.982  1.00 35.56 ? 345  PRO A CB    1 
ATOM   2645 C CG    . PRO A 1 345 ? 38.220  -34.720 -3.197  1.00 37.67 ? 345  PRO A CG    1 
ATOM   2646 C CD    . PRO A 1 345 ? 36.782  -34.618 -2.725  1.00 35.61 ? 345  PRO A CD    1 
ATOM   2647 N N     . GLY A 1 346 ? 39.084  -34.686 1.435   1.00 34.42 ? 346  GLY A N     1 
ATOM   2648 C CA    . GLY A 1 346 ? 39.403  -33.954 2.669   1.00 38.17 ? 346  GLY A CA    1 
ATOM   2649 C C     . GLY A 1 346 ? 38.382  -34.231 3.757   1.00 36.72 ? 346  GLY A C     1 
ATOM   2650 O O     . GLY A 1 346 ? 38.624  -33.802 4.889   1.00 39.32 ? 346  GLY A O     1 
ATOM   2651 N N     . SER A 1 347 ? 37.291  -34.935 3.439   1.00 39.17 ? 347  SER A N     1 
ATOM   2652 C CA    . SER A 1 347 ? 36.240  -35.290 4.428   1.00 35.05 ? 347  SER A CA    1 
ATOM   2653 C C     . SER A 1 347 ? 36.822  -36.245 5.462   1.00 35.58 ? 347  SER A C     1 
ATOM   2654 O O     . SER A 1 347 ? 37.521  -37.161 5.053   1.00 34.97 ? 347  SER A O     1 
ATOM   2655 C CB    . SER A 1 347 ? 34.995  -35.854 3.782   1.00 35.54 ? 347  SER A CB    1 
ATOM   2656 O OG    . SER A 1 347 ? 35.261  -36.940 2.928   1.00 35.24 ? 347  SER A OG    1 
ATOM   2657 N N     . ARG A 1 348 ? 36.541  -36.009 6.750   1.00 34.32 ? 348  ARG A N     1 
ATOM   2658 C CA    . ARG A 1 348 ? 36.984  -36.856 7.881   1.00 33.85 ? 348  ARG A CA    1 
ATOM   2659 C C     . ARG A 1 348 ? 35.789  -37.116 8.809   1.00 34.14 ? 348  ARG A C     1 
ATOM   2660 O O     . ARG A 1 348 ? 35.054  -36.167 9.125   1.00 31.05 ? 348  ARG A O     1 
ATOM   2661 C CB    . ARG A 1 348 ? 38.164  -36.241 8.642   1.00 36.51 ? 348  ARG A CB    1 
ATOM   2662 C CG    . ARG A 1 348 ? 39.370  -35.951 7.753   1.00 45.80 ? 348  ARG A CG    1 
ATOM   2663 C CD    . ARG A 1 348 ? 40.677  -35.598 8.455   1.00 53.65 ? 348  ARG A CD    1 
ATOM   2664 N NE    . ARG A 1 348 ? 40.514  -34.571 9.478   1.00 62.20 ? 348  ARG A NE    1 
ATOM   2665 C CZ    . ARG A 1 348 ? 41.478  -33.804 9.975   1.00 67.47 ? 348  ARG A CZ    1 
ATOM   2666 N NH1   . ARG A 1 348 ? 42.721  -33.920 9.536   1.00 69.86 ? 348  ARG A NH1   1 
ATOM   2667 N NH2   . ARG A 1 348 ? 41.181  -32.908 10.904  1.00 63.79 ? 348  ARG A NH2   1 
ATOM   2668 N N     . PHE A 1 349 ? 35.680  -38.362 9.273   1.00 35.30 ? 349  PHE A N     1 
ATOM   2669 C CA    . PHE A 1 349 ? 34.531  -38.933 10.011  1.00 33.81 ? 349  PHE A CA    1 
ATOM   2670 C C     . PHE A 1 349 ? 34.971  -39.276 11.422  1.00 36.26 ? 349  PHE A C     1 
ATOM   2671 O O     . PHE A 1 349 ? 35.993  -39.970 11.567  1.00 32.99 ? 349  PHE A O     1 
ATOM   2672 C CB    . PHE A 1 349 ? 34.028  -40.175 9.285   1.00 35.61 ? 349  PHE A CB    1 
ATOM   2673 C CG    . PHE A 1 349 ? 33.527  -39.863 7.907   1.00 37.56 ? 349  PHE A CG    1 
ATOM   2674 C CD1   . PHE A 1 349 ? 34.410  -39.703 6.854   1.00 40.07 ? 349  PHE A CD1   1 
ATOM   2675 C CD2   . PHE A 1 349 ? 32.181  -39.664 7.681   1.00 37.80 ? 349  PHE A CD2   1 
ATOM   2676 C CE1   . PHE A 1 349 ? 33.950  -39.381 5.590   1.00 40.91 ? 349  PHE A CE1   1 
ATOM   2677 C CE2   . PHE A 1 349 ? 31.716  -39.365 6.412   1.00 37.12 ? 349  PHE A CE2   1 
ATOM   2678 C CZ    . PHE A 1 349 ? 32.600  -39.214 5.373   1.00 40.32 ? 349  PHE A CZ    1 
ATOM   2679 N N     . GLN A 1 350 ? 34.238  -38.785 12.423  1.00 33.83 ? 350  GLN A N     1 
ATOM   2680 C CA    . GLN A 1 350 ? 34.478  -39.132 13.839  1.00 34.78 ? 350  GLN A CA    1 
ATOM   2681 C C     . GLN A 1 350 ? 33.111  -39.357 14.508  1.00 34.51 ? 350  GLN A C     1 
ATOM   2682 O O     . GLN A 1 350 ? 32.168  -38.563 14.282  1.00 28.61 ? 350  GLN A O     1 
ATOM   2683 C CB    . GLN A 1 350 ? 35.334  -38.066 14.531  1.00 38.60 ? 350  GLN A CB    1 
ATOM   2684 C CG    . GLN A 1 350 ? 36.601  -37.660 13.765  1.00 42.03 ? 350  GLN A CG    1 
ATOM   2685 C CD    . GLN A 1 350 ? 36.473  -36.447 12.847  1.00 54.34 ? 350  GLN A CD    1 
ATOM   2686 O OE1   . GLN A 1 350 ? 35.372  -35.955 12.503  1.00 38.32 ? 350  GLN A OE1   1 
ATOM   2687 N NE2   . GLN A 1 350 ? 37.634  -35.949 12.410  1.00 47.79 ? 350  GLN A NE2   1 
ATOM   2688 N N     . THR A 1 351 ? 33.048  -40.397 15.322  1.00 30.85 ? 351  THR A N     1 
ATOM   2689 C CA    . THR A 1 351 ? 31.885  -40.855 16.121  1.00 33.79 ? 351  THR A CA    1 
ATOM   2690 C C     . THR A 1 351 ? 31.958  -40.164 17.489  1.00 33.14 ? 351  THR A C     1 
ATOM   2691 O O     . THR A 1 351 ? 33.057  -39.778 17.880  1.00 31.92 ? 351  THR A O     1 
ATOM   2692 C CB    . THR A 1 351 ? 31.988  -42.387 16.130  1.00 36.86 ? 351  THR A CB    1 
ATOM   2693 O OG1   . THR A 1 351 ? 31.309  -42.873 14.967  1.00 38.56 ? 351  THR A OG1   1 
ATOM   2694 C CG2   . THR A 1 351 ? 31.513  -43.044 17.392  1.00 38.64 ? 351  THR A CG2   1 
ATOM   2695 N N     . HIS A 1 352 ? 30.840  -40.045 18.206  1.00 30.13 ? 352  HIS A N     1 
ATOM   2696 C CA    . HIS A 1 352 ? 30.764  -39.501 19.584  1.00 33.33 ? 352  HIS A CA    1 
ATOM   2697 C C     . HIS A 1 352 ? 31.587  -40.344 20.572  1.00 34.01 ? 352  HIS A C     1 
ATOM   2698 O O     . HIS A 1 352 ? 31.912  -39.815 21.656  1.00 32.09 ? 352  HIS A O     1 
ATOM   2699 C CB    . HIS A 1 352 ? 29.296  -39.381 20.055  1.00 34.54 ? 352  HIS A CB    1 
ATOM   2700 C CG    . HIS A 1 352 ? 28.723  -40.676 20.516  1.00 33.29 ? 352  HIS A CG    1 
ATOM   2701 N ND1   . HIS A 1 352 ? 28.132  -41.568 19.645  1.00 32.30 ? 352  HIS A ND1   1 
ATOM   2702 C CD2   . HIS A 1 352 ? 28.667  -41.242 21.745  1.00 32.24 ? 352  HIS A CD2   1 
ATOM   2703 C CE1   . HIS A 1 352 ? 27.726  -42.634 20.331  1.00 32.94 ? 352  HIS A CE1   1 
ATOM   2704 N NE2   . HIS A 1 352 ? 28.045  -42.454 21.614  1.00 34.35 ? 352  HIS A NE2   1 
ATOM   2705 N N     . GLU A 1 353 ? 31.897  -41.605 20.262  1.00 39.55 ? 353  GLU A N     1 
ATOM   2706 C CA    . GLU A 1 353 ? 32.778  -42.425 21.153  1.00 44.28 ? 353  GLU A CA    1 
ATOM   2707 C C     . GLU A 1 353 ? 34.247  -42.339 20.709  1.00 40.12 ? 353  GLU A C     1 
ATOM   2708 O O     . GLU A 1 353 ? 35.079  -42.827 21.452  1.00 40.00 ? 353  GLU A O     1 
ATOM   2709 C CB    . GLU A 1 353 ? 32.336  -43.883 21.300  1.00 49.96 ? 353  GLU A CB    1 
ATOM   2710 C CG    . GLU A 1 353 ? 31.412  -44.413 20.232  1.00 52.24 ? 353  GLU A CG    1 
ATOM   2711 C CD    . GLU A 1 353 ? 30.602  -45.611 20.684  1.00 59.49 ? 353  GLU A CD    1 
ATOM   2712 O OE1   . GLU A 1 353 ? 30.425  -45.772 21.906  1.00 63.34 ? 353  GLU A OE1   1 
ATOM   2713 O OE2   . GLU A 1 353 ? 30.189  -46.407 19.814  1.00 59.72 ? 353  GLU A OE2   1 
ATOM   2714 N N     . GLU A 1 354 ? 34.556  -41.708 19.580  1.00 38.29 ? 354  GLU A N     1 
ATOM   2715 C CA    . GLU A 1 354 ? 35.942  -41.615 19.048  1.00 43.18 ? 354  GLU A CA    1 
ATOM   2716 C C     . GLU A 1 354 ? 36.588  -40.282 19.425  1.00 43.31 ? 354  GLU A C     1 
ATOM   2717 O O     . GLU A 1 354 ? 37.810  -40.269 19.650  1.00 40.19 ? 354  GLU A O     1 
ATOM   2718 C CB    . GLU A 1 354 ? 35.944  -41.777 17.531  1.00 44.77 ? 354  GLU A CB    1 
ATOM   2719 C CG    . GLU A 1 354 ? 35.511  -43.154 17.093  1.00 43.10 ? 354  GLU A CG    1 
ATOM   2720 C CD    . GLU A 1 354 ? 35.498  -43.303 15.593  1.00 43.32 ? 354  GLU A CD    1 
ATOM   2721 O OE1   . GLU A 1 354 ? 35.034  -42.359 14.912  1.00 38.50 ? 354  GLU A OE1   1 
ATOM   2722 O OE2   . GLU A 1 354 ? 36.009  -44.327 15.112  1.00 47.87 ? 354  GLU A OE2   1 
ATOM   2723 N N     . ARG A 1 355 ? 35.812  -39.197 19.518  1.00 40.84 ? 355  ARG A N     1 
ATOM   2724 C CA    . ARG A 1 355 ? 36.370  -37.818 19.619  1.00 37.82 ? 355  ARG A CA    1 
ATOM   2725 C C     . ARG A 1 355 ? 35.896  -37.149 20.913  1.00 39.78 ? 355  ARG A C     1 
ATOM   2726 O O     . ARG A 1 355 ? 34.671  -37.090 21.147  1.00 39.79 ? 355  ARG A O     1 
ATOM   2727 C CB    . ARG A 1 355 ? 36.004  -37.019 18.369  1.00 39.77 ? 355  ARG A CB    1 
ATOM   2728 C CG    . ARG A 1 355 ? 37.023  -35.942 18.047  1.00 41.08 ? 355  ARG A CG    1 
ATOM   2729 C CD    . ARG A 1 355 ? 36.534  -34.883 17.096  1.00 37.41 ? 355  ARG A CD    1 
ATOM   2730 N NE    . ARG A 1 355 ? 37.421  -33.734 17.153  1.00 39.40 ? 355  ARG A NE    1 
ATOM   2731 C CZ    . ARG A 1 355 ? 37.594  -32.839 16.186  1.00 40.42 ? 355  ARG A CZ    1 
ATOM   2732 N NH1   . ARG A 1 355 ? 36.923  -32.934 15.047  1.00 41.52 ? 355  ARG A NH1   1 
ATOM   2733 N NH2   . ARG A 1 355 ? 38.450  -31.844 16.367  1.00 45.40 ? 355  ARG A NH2   1 
ATOM   2734 N N     . HIS A 1 356 ? 36.838  -36.657 21.719  1.00 35.75 ? 356  HIS A N     1 
ATOM   2735 C CA    . HIS A 1 356 ? 36.585  -36.187 23.103  1.00 40.29 ? 356  HIS A CA    1 
ATOM   2736 C C     . HIS A 1 356 ? 37.403  -34.945 23.449  1.00 41.41 ? 356  HIS A C     1 
ATOM   2737 O O     . HIS A 1 356 ? 37.523  -34.670 24.654  1.00 53.26 ? 356  HIS A O     1 
ATOM   2738 C CB    . HIS A 1 356 ? 36.837  -37.352 24.062  1.00 41.32 ? 356  HIS A CB    1 
ATOM   2739 C CG    . HIS A 1 356 ? 35.711  -38.325 24.052  1.00 43.33 ? 356  HIS A CG    1 
ATOM   2740 N ND1   . HIS A 1 356 ? 35.818  -39.561 23.451  1.00 44.86 ? 356  HIS A ND1   1 
ATOM   2741 C CD2   . HIS A 1 356 ? 34.439  -38.221 24.504  1.00 44.74 ? 356  HIS A CD2   1 
ATOM   2742 C CE1   . HIS A 1 356 ? 34.662  -40.195 23.564  1.00 44.41 ? 356  HIS A CE1   1 
ATOM   2743 N NE2   . HIS A 1 356 ? 33.798  -39.391 24.202  1.00 48.83 ? 356  HIS A NE2   1 
ATOM   2744 N N     . ASP A 1 357 ? 37.878  -34.214 22.438  1.00 41.36 ? 357  ASP A N     1 
ATOM   2745 C CA    . ASP A 1 357 ? 38.790  -33.054 22.580  1.00 44.26 ? 357  ASP A CA    1 
ATOM   2746 C C     . ASP A 1 357 ? 37.979  -31.754 22.475  1.00 46.71 ? 357  ASP A C     1 
ATOM   2747 O O     . ASP A 1 357 ? 36.731  -31.820 22.275  1.00 51.65 ? 357  ASP A O     1 
ATOM   2748 C CB    . ASP A 1 357 ? 39.919  -33.159 21.551  1.00 43.99 ? 357  ASP A CB    1 
ATOM   2749 C CG    . ASP A 1 357 ? 39.466  -33.072 20.103  1.00 45.90 ? 357  ASP A CG    1 
ATOM   2750 O OD1   . ASP A 1 357 ? 38.259  -33.261 19.858  1.00 43.46 ? 357  ASP A OD1   1 
ATOM   2751 O OD2   . ASP A 1 357 ? 40.307  -32.766 19.246  1.00 46.29 ? 357  ASP A OD2   1 
ATOM   2752 N N     . ARG A 1 358 ? 38.652  -30.614 22.629  1.00 46.13 ? 358  ARG A N     1 
ATOM   2753 C CA    . ARG A 1 358 ? 38.019  -29.276 22.556  1.00 43.56 ? 358  ARG A CA    1 
ATOM   2754 C C     . ARG A 1 358 ? 37.105  -29.218 21.321  1.00 43.86 ? 358  ARG A C     1 
ATOM   2755 O O     . ARG A 1 358 ? 35.937  -28.796 21.460  1.00 43.29 ? 358  ARG A O     1 
ATOM   2756 C CB    . ARG A 1 358 ? 39.107  -28.207 22.560  1.00 47.36 ? 358  ARG A CB    1 
ATOM   2757 C CG    . ARG A 1 358 ? 38.561  -26.792 22.644  1.00 50.40 ? 358  ARG A CG    1 
ATOM   2758 C CD    . ARG A 1 358 ? 39.449  -25.882 23.454  1.00 52.50 ? 358  ARG A CD    1 
ATOM   2759 N NE    . ARG A 1 358 ? 40.508  -25.317 22.643  1.00 57.24 ? 358  ARG A NE    1 
ATOM   2760 C CZ    . ARG A 1 358 ? 40.693  -24.022 22.415  1.00 56.17 ? 358  ARG A CZ    1 
ATOM   2761 N NH1   . ARG A 1 358 ? 39.871  -23.122 22.927  1.00 54.55 ? 358  ARG A NH1   1 
ATOM   2762 N NH2   . ARG A 1 358 ? 41.710  -23.630 21.669  1.00 58.93 ? 358  ARG A NH2   1 
ATOM   2763 N N     . GLY A 1 359 ? 37.594  -29.709 20.183  1.00 40.50 ? 359  GLY A N     1 
ATOM   2764 C CA    . GLY A 1 359 ? 36.911  -29.698 18.879  1.00 38.02 ? 359  GLY A CA    1 
ATOM   2765 C C     . GLY A 1 359 ? 35.698  -30.612 18.839  1.00 40.28 ? 359  GLY A C     1 
ATOM   2766 O O     . GLY A 1 359 ? 34.934  -30.472 17.888  1.00 41.15 ? 359  GLY A O     1 
ATOM   2767 N N     . ALA A 1 360 ? 35.539  -31.534 19.798  1.00 35.99 ? 360  ALA A N     1 
ATOM   2768 C CA    . ALA A 1 360 ? 34.409  -32.492 19.861  1.00 37.11 ? 360  ALA A CA    1 
ATOM   2769 C C     . ALA A 1 360 ? 33.282  -31.974 20.777  1.00 37.64 ? 360  ALA A C     1 
ATOM   2770 O O     . ALA A 1 360 ? 32.299  -32.738 21.005  1.00 34.63 ? 360  ALA A O     1 
ATOM   2771 C CB    . ALA A 1 360 ? 34.911  -33.843 20.315  1.00 38.67 ? 360  ALA A CB    1 
ATOM   2772 N N     . HIS A 1 361 ? 33.395  -30.752 21.302  1.00 32.39 ? 361  HIS A N     1 
ATOM   2773 C CA    . HIS A 1 361 ? 32.384  -30.199 22.245  1.00 37.32 ? 361  HIS A CA    1 
ATOM   2774 C C     . HIS A 1 361 ? 31.007  -30.143 21.555  1.00 33.62 ? 361  HIS A C     1 
ATOM   2775 O O     . HIS A 1 361 ? 30.014  -30.575 22.164  1.00 33.37 ? 361  HIS A O     1 
ATOM   2776 C CB    . HIS A 1 361 ? 32.811  -28.842 22.789  1.00 38.01 ? 361  HIS A CB    1 
ATOM   2777 C CG    . HIS A 1 361 ? 31.959  -28.423 23.936  1.00 45.93 ? 361  HIS A CG    1 
ATOM   2778 N ND1   . HIS A 1 361 ? 32.191  -28.884 25.216  1.00 45.94 ? 361  HIS A ND1   1 
ATOM   2779 C CD2   . HIS A 1 361 ? 30.853  -27.638 24.007  1.00 48.80 ? 361  HIS A CD2   1 
ATOM   2780 C CE1   . HIS A 1 361 ? 31.275  -28.379 26.037  1.00 51.90 ? 361  HIS A CE1   1 
ATOM   2781 N NE2   . HIS A 1 361 ? 30.442  -27.606 25.321  1.00 47.46 ? 361  HIS A NE2   1 
ATOM   2782 N N     . VAL A 1 362 ? 30.946  -29.612 20.336  1.00 30.42 ? 362  VAL A N     1 
ATOM   2783 C CA    . VAL A 1 362 ? 29.664  -29.519 19.576  1.00 30.68 ? 362  VAL A CA    1 
ATOM   2784 C C     . VAL A 1 362 ? 29.155  -30.939 19.284  1.00 30.67 ? 362  VAL A C     1 
ATOM   2785 O O     . VAL A 1 362 ? 27.955  -31.189 19.505  1.00 33.99 ? 362  VAL A O     1 
ATOM   2786 C CB    . VAL A 1 362 ? 29.799  -28.643 18.318  1.00 30.19 ? 362  VAL A CB    1 
ATOM   2787 C CG1   . VAL A 1 362 ? 28.633  -28.840 17.372  1.00 32.24 ? 362  VAL A CG1   1 
ATOM   2788 C CG2   . VAL A 1 362 ? 29.921  -27.184 18.703  1.00 31.70 ? 362  VAL A CG2   1 
ATOM   2789 N N     . LEU A 1 363 ? 30.025  -31.853 18.863  1.00 30.77 ? 363  LEU A N     1 
ATOM   2790 C CA    . LEU A 1 363 ? 29.666  -33.275 18.611  1.00 28.57 ? 363  LEU A CA    1 
ATOM   2791 C C     . LEU A 1 363 ? 28.984  -33.865 19.844  1.00 28.36 ? 363  LEU A C     1 
ATOM   2792 O O     . LEU A 1 363 ? 27.941  -34.497 19.686  1.00 26.95 ? 363  LEU A O     1 
ATOM   2793 C CB    . LEU A 1 363 ? 30.922  -34.078 18.250  1.00 30.23 ? 363  LEU A CB    1 
ATOM   2794 C CG    . LEU A 1 363 ? 30.741  -35.592 18.155  1.00 31.03 ? 363  LEU A CG    1 
ATOM   2795 C CD1   . LEU A 1 363 ? 29.681  -35.957 17.131  1.00 32.36 ? 363  LEU A CD1   1 
ATOM   2796 C CD2   . LEU A 1 363 ? 32.064  -36.279 17.806  1.00 31.14 ? 363  LEU A CD2   1 
ATOM   2797 N N     . GLN A 1 364 ? 29.567  -33.697 21.029  1.00 28.89 ? 364  GLN A N     1 
ATOM   2798 C CA    . GLN A 1 364 ? 29.013  -34.296 22.264  1.00 29.92 ? 364  GLN A CA    1 
ATOM   2799 C C     . GLN A 1 364 ? 27.689  -33.613 22.601  1.00 27.91 ? 364  GLN A C     1 
ATOM   2800 O O     . GLN A 1 364 ? 26.794  -34.305 23.100  1.00 27.81 ? 364  GLN A O     1 
ATOM   2801 C CB    . GLN A 1 364 ? 30.001  -34.231 23.428  1.00 32.23 ? 364  GLN A CB    1 
ATOM   2802 C CG    . GLN A 1 364 ? 31.292  -34.999 23.178  1.00 35.43 ? 364  GLN A CG    1 
ATOM   2803 C CD    . GLN A 1 364 ? 31.068  -36.464 22.912  1.00 34.75 ? 364  GLN A CD    1 
ATOM   2804 O OE1   . GLN A 1 364 ? 30.063  -37.035 23.334  1.00 32.80 ? 364  GLN A OE1   1 
ATOM   2805 N NE2   . GLN A 1 364 ? 32.017  -37.080 22.218  1.00 35.89 ? 364  GLN A NE2   1 
ATOM   2806 N N     . ASP A 1 365 ? 27.573  -32.312 22.355  1.00 29.24 ? 365  ASP A N     1 
ATOM   2807 C CA    . ASP A 1 365 ? 26.314  -31.581 22.618  1.00 28.04 ? 365  ASP A CA    1 
ATOM   2808 C C     . ASP A 1 365 ? 25.232  -32.058 21.641  1.00 27.94 ? 365  ASP A C     1 
ATOM   2809 O O     . ASP A 1 365 ? 24.099  -32.278 22.092  1.00 27.65 ? 365  ASP A O     1 
ATOM   2810 C CB    . ASP A 1 365 ? 26.506  -30.070 22.540  1.00 31.98 ? 365  ASP A CB    1 
ATOM   2811 C CG    . ASP A 1 365 ? 25.395  -29.316 23.257  1.00 32.97 ? 365  ASP A CG    1 
ATOM   2812 O OD1   . ASP A 1 365 ? 25.043  -29.726 24.405  1.00 32.49 ? 365  ASP A OD1   1 
ATOM   2813 O OD2   . ASP A 1 365 ? 24.918  -28.316 22.683  1.00 32.68 ? 365  ASP A OD2   1 
ATOM   2814 N N     . ARG A 1 366 ? 25.552  -32.185 20.352  1.00 27.50 ? 366  ARG A N     1 
ATOM   2815 C CA    . ARG A 1 366 ? 24.572  -32.682 19.346  1.00 28.03 ? 366  ARG A CA    1 
ATOM   2816 C C     . ARG A 1 366 ? 24.105  -34.083 19.760  1.00 29.20 ? 366  ARG A C     1 
ATOM   2817 O O     . ARG A 1 366 ? 22.913  -34.379 19.597  1.00 25.79 ? 366  ARG A O     1 
ATOM   2818 C CB    . ARG A 1 366 ? 25.134  -32.688 17.920  1.00 29.97 ? 366  ARG A CB    1 
ATOM   2819 C CG    . ARG A 1 366 ? 25.673  -31.343 17.426  1.00 29.61 ? 366  ARG A CG    1 
ATOM   2820 C CD    . ARG A 1 366 ? 24.936  -30.109 17.921  1.00 30.17 ? 366  ARG A CD    1 
ATOM   2821 N NE    . ARG A 1 366 ? 23.608  -30.015 17.330  1.00 27.62 ? 366  ARG A NE    1 
ATOM   2822 C CZ    . ARG A 1 366 ? 22.779  -28.988 17.500  1.00 29.55 ? 366  ARG A CZ    1 
ATOM   2823 N NH1   . ARG A 1 366 ? 23.118  -27.968 18.271  1.00 27.46 ? 366  ARG A NH1   1 
ATOM   2824 N NH2   . ARG A 1 366 ? 21.607  -28.976 16.887  1.00 29.31 ? 366  ARG A NH2   1 
ATOM   2825 N N     . HIS A 1 367 ? 24.992  -34.908 20.308  1.00 27.68 ? 367  HIS A N     1 
ATOM   2826 C CA    . HIS A 1 367 ? 24.645  -36.284 20.751  1.00 29.80 ? 367  HIS A CA    1 
ATOM   2827 C C     . HIS A 1 367 ? 23.575  -36.248 21.863  1.00 30.53 ? 367  HIS A C     1 
ATOM   2828 O O     . HIS A 1 367 ? 22.733  -37.163 21.906  1.00 29.40 ? 367  HIS A O     1 
ATOM   2829 C CB    . HIS A 1 367 ? 25.901  -37.040 21.184  1.00 30.42 ? 367  HIS A CB    1 
ATOM   2830 C CG    . HIS A 1 367 ? 25.624  -38.473 21.498  1.00 30.60 ? 367  HIS A CG    1 
ATOM   2831 N ND1   . HIS A 1 367 ? 25.043  -39.311 20.580  1.00 30.31 ? 367  HIS A ND1   1 
ATOM   2832 C CD2   . HIS A 1 367 ? 25.827  -39.196 22.622  1.00 31.84 ? 367  HIS A CD2   1 
ATOM   2833 C CE1   . HIS A 1 367 ? 24.926  -40.511 21.114  1.00 34.12 ? 367  HIS A CE1   1 
ATOM   2834 N NE2   . HIS A 1 367 ? 25.388  -40.461 22.365  1.00 32.59 ? 367  HIS A NE2   1 
ATOM   2835 N N     . LYS A 1 368 ? 23.620  -35.257 22.750  1.00 27.36 ? 368  LYS A N     1 
ATOM   2836 C CA    . LYS A 1 368 ? 22.556  -35.034 23.772  1.00 28.15 ? 368  LYS A CA    1 
ATOM   2837 C C     . LYS A 1 368 ? 21.274  -34.582 23.059  1.00 25.69 ? 368  LYS A C     1 
ATOM   2838 O O     . LYS A 1 368 ? 20.285  -35.280 23.105  1.00 25.79 ? 368  LYS A O     1 
ATOM   2839 C CB    . LYS A 1 368 ? 23.042  -34.011 24.808  1.00 31.11 ? 368  LYS A CB    1 
ATOM   2840 C CG    . LYS A 1 368 ? 24.162  -34.525 25.709  1.00 39.08 ? 368  LYS A CG    1 
ATOM   2841 C CD    . LYS A 1 368 ? 24.933  -33.446 26.454  1.00 42.63 ? 368  LYS A CD    1 
ATOM   2842 C CE    . LYS A 1 368 ? 24.233  -32.977 27.711  1.00 53.31 ? 368  LYS A CE    1 
ATOM   2843 N NZ    . LYS A 1 368 ? 24.643  -31.598 28.095  1.00 62.16 ? 368  LYS A NZ    1 
ATOM   2844 N N     . ILE A 1 369 ? 21.355  -33.462 22.352  1.00 24.52 ? 369  ILE A N     1 
ATOM   2845 C CA    . ILE A 1 369 ? 20.204  -32.803 21.684  1.00 24.69 ? 369  ILE A CA    1 
ATOM   2846 C C     . ILE A 1 369 ? 19.500  -33.825 20.774  1.00 25.82 ? 369  ILE A C     1 
ATOM   2847 O O     . ILE A 1 369 ? 18.255  -33.951 20.862  1.00 26.17 ? 369  ILE A O     1 
ATOM   2848 C CB    . ILE A 1 369 ? 20.691  -31.544 20.934  1.00 25.29 ? 369  ILE A CB    1 
ATOM   2849 C CG1   . ILE A 1 369 ? 21.071  -30.438 21.921  1.00 24.54 ? 369  ILE A CG1   1 
ATOM   2850 C CG2   . ILE A 1 369 ? 19.652  -31.078 19.941  1.00 26.18 ? 369  ILE A CG2   1 
ATOM   2851 C CD1   . ILE A 1 369 ? 21.983  -29.398 21.355  1.00 27.00 ? 369  ILE A CD1   1 
ATOM   2852 N N     . ASN A 1 370 ? 20.269  -34.555 19.958  1.00 24.73 ? 370  ASN A N     1 
ATOM   2853 C CA    . ASN A 1 370 ? 19.733  -35.510 18.952  1.00 25.82 ? 370  ASN A CA    1 
ATOM   2854 C C     . ASN A 1 370 ? 19.117  -36.747 19.634  1.00 24.62 ? 370  ASN A C     1 
ATOM   2855 O O     . ASN A 1 370 ? 18.422  -37.511 18.938  1.00 27.57 ? 370  ASN A O     1 
ATOM   2856 C CB    . ASN A 1 370 ? 20.819  -35.870 17.939  1.00 25.99 ? 370  ASN A CB    1 
ATOM   2857 C CG    . ASN A 1 370 ? 21.215  -34.695 17.070  1.00 26.24 ? 370  ASN A CG    1 
ATOM   2858 O OD1   . ASN A 1 370 ? 20.642  -33.617 17.216  1.00 25.14 ? 370  ASN A OD1   1 
ATOM   2859 N ND2   . ASN A 1 370 ? 22.172  -34.891 16.160  1.00 22.00 ? 370  ASN A ND2   1 
ATOM   2860 N N     . ASN A 1 371 ? 19.301  -36.902 20.955  1.00 25.40 ? 371  ASN A N     1 
ATOM   2861 C CA    . ASN A 1 371 ? 18.712  -37.996 21.762  1.00 26.11 ? 371  ASN A CA    1 
ATOM   2862 C C     . ASN A 1 371 ? 17.706  -37.425 22.771  1.00 26.58 ? 371  ASN A C     1 
ATOM   2863 O O     . ASN A 1 371 ? 17.351  -38.144 23.715  1.00 25.91 ? 371  ASN A O     1 
ATOM   2864 C CB    . ASN A 1 371 ? 19.822  -38.831 22.404  1.00 27.51 ? 371  ASN A CB    1 
ATOM   2865 C CG    . ASN A 1 371 ? 20.416  -39.787 21.390  1.00 31.26 ? 371  ASN A CG    1 
ATOM   2866 O OD1   . ASN A 1 371 ? 19.752  -40.754 21.008  1.00 32.66 ? 371  ASN A OD1   1 
ATOM   2867 N ND2   . ASN A 1 371 ? 21.632  -39.511 20.924  1.00 29.53 ? 371  ASN A ND2   1 
ATOM   2868 N N     . GLY A 1 372 ? 17.252  -36.186 22.569  1.00 26.52 ? 372  GLY A N     1 
ATOM   2869 C CA    . GLY A 1 372 ? 16.239  -35.550 23.425  1.00 25.52 ? 372  GLY A CA    1 
ATOM   2870 C C     . GLY A 1 372 ? 16.754  -35.350 24.830  1.00 26.18 ? 372  GLY A C     1 
ATOM   2871 O O     . GLY A 1 372 ? 15.942  -35.398 25.792  1.00 28.02 ? 372  GLY A O     1 
ATOM   2872 N N     . ILE A 1 373 ? 18.049  -35.102 24.971  1.00 26.18 ? 373  ILE A N     1 
ATOM   2873 C CA    . ILE A 1 373 ? 18.642  -34.710 26.283  1.00 26.87 ? 373  ILE A CA    1 
ATOM   2874 C C     . ILE A 1 373 ? 18.947  -33.230 26.196  1.00 28.02 ? 373  ILE A C     1 
ATOM   2875 O O     . ILE A 1 373 ? 19.824  -32.816 25.439  1.00 29.02 ? 373  ILE A O     1 
ATOM   2876 C CB    . ILE A 1 373 ? 19.863  -35.568 26.635  1.00 29.94 ? 373  ILE A CB    1 
ATOM   2877 C CG1   . ILE A 1 373 ? 19.427  -37.025 26.844  1.00 32.39 ? 373  ILE A CG1   1 
ATOM   2878 C CG2   . ILE A 1 373 ? 20.575  -34.998 27.856  1.00 30.12 ? 373  ILE A CG2   1 
ATOM   2879 C CD1   . ILE A 1 373 ? 20.194  -38.026 26.044  1.00 36.26 ? 373  ILE A CD1   1 
ATOM   2880 N N     . PRO A 1 374 ? 18.158  -32.386 26.888  1.00 25.47 ? 374  PRO A N     1 
ATOM   2881 C CA    . PRO A 1 374 ? 18.289  -30.939 26.761  1.00 26.90 ? 374  PRO A CA    1 
ATOM   2882 C C     . PRO A 1 374 ? 19.585  -30.422 27.395  1.00 26.78 ? 374  PRO A C     1 
ATOM   2883 O O     . PRO A 1 374 ? 20.116  -31.067 28.298  1.00 26.24 ? 374  PRO A O     1 
ATOM   2884 C CB    . PRO A 1 374 ? 17.016  -30.414 27.434  1.00 28.15 ? 374  PRO A CB    1 
ATOM   2885 C CG    . PRO A 1 374 ? 16.715  -31.469 28.485  1.00 28.29 ? 374  PRO A CG    1 
ATOM   2886 C CD    . PRO A 1 374 ? 17.086  -32.774 27.808  1.00 28.50 ? 374  PRO A CD    1 
ATOM   2887 N N     . SER A 1 375 ? 20.089  -29.311 26.867  1.00 26.49 ? 375  SER A N     1 
ATOM   2888 C CA    . SER A 1 375 ? 21.431  -28.750 27.161  1.00 26.52 ? 375  SER A CA    1 
ATOM   2889 C C     . SER A 1 375 ? 21.364  -27.222 27.150  1.00 26.20 ? 375  SER A C     1 
ATOM   2890 O O     . SER A 1 375 ? 20.468  -26.668 26.474  1.00 26.02 ? 375  SER A O     1 
ATOM   2891 C CB    . SER A 1 375 ? 22.415  -29.238 26.125  1.00 26.00 ? 375  SER A CB    1 
ATOM   2892 O OG    . SER A 1 375 ? 23.677  -28.645 26.316  1.00 26.10 ? 375  SER A OG    1 
ATOM   2893 N N     . LEU A 1 376 ? 22.305  -26.558 27.832  1.00 26.91 ? 376  LEU A N     1 
ATOM   2894 C CA    . LEU A 1 376 ? 22.525  -25.109 27.680  1.00 28.52 ? 376  LEU A CA    1 
ATOM   2895 C C     . LEU A 1 376 ? 23.950  -24.832 27.172  1.00 28.73 ? 376  LEU A C     1 
ATOM   2896 O O     . LEU A 1 376 ? 24.341  -23.662 27.209  1.00 26.85 ? 376  LEU A O     1 
ATOM   2897 C CB    . LEU A 1 376 ? 22.233  -24.415 29.016  1.00 32.34 ? 376  LEU A CB    1 
ATOM   2898 C CG    . LEU A 1 376 ? 20.760  -24.381 29.436  1.00 30.85 ? 376  LEU A CG    1 
ATOM   2899 C CD1   . LEU A 1 376 ? 20.609  -23.787 30.827  1.00 31.35 ? 376  LEU A CD1   1 
ATOM   2900 C CD2   . LEU A 1 376 ? 19.899  -23.607 28.452  1.00 32.59 ? 376  LEU A CD2   1 
ATOM   2901 N N     . SER A 1 377 ? 24.648  -25.825 26.616  1.00 29.84 ? 377  SER A N     1 
ATOM   2902 C CA    . SER A 1 377 ? 26.046  -25.688 26.121  1.00 32.43 ? 377  SER A CA    1 
ATOM   2903 C C     . SER A 1 377 ? 26.127  -24.605 25.047  1.00 29.85 ? 377  SER A C     1 
ATOM   2904 O O     . SER A 1 377 ? 27.108  -23.871 25.065  1.00 31.60 ? 377  SER A O     1 
ATOM   2905 C CB    . SER A 1 377 ? 26.629  -26.985 25.612  1.00 34.42 ? 377  SER A CB    1 
ATOM   2906 O OG    . SER A 1 377 ? 26.867  -27.888 26.689  1.00 40.08 ? 377  SER A OG    1 
ATOM   2907 N N     . GLU A 1 378 ? 25.146  -24.500 24.164  1.00 33.29 ? 378  GLU A N     1 
ATOM   2908 C CA    . GLU A 1 378 ? 25.176  -23.541 23.066  1.00 33.50 ? 378  GLU A CA    1 
ATOM   2909 C C     . GLU A 1 378 ? 25.152  -22.087 23.503  1.00 31.66 ? 378  GLU A C     1 
ATOM   2910 O O     . GLU A 1 378 ? 25.425  -21.222 22.722  1.00 32.70 ? 378  GLU A O     1 
ATOM   2911 C CB    . GLU A 1 378 ? 24.063  -23.808 22.042  1.00 39.00 ? 378  GLU A CB    1 
ATOM   2912 C CG    . GLU A 1 378 ? 24.268  -25.024 21.162  1.00 47.49 ? 378  GLU A CG    1 
ATOM   2913 C CD    . GLU A 1 378 ? 25.260  -24.798 20.041  1.00 56.09 ? 378  GLU A CD    1 
ATOM   2914 O OE1   . GLU A 1 378 ? 24.937  -24.089 19.078  1.00 40.33 ? 378  GLU A OE1   1 
ATOM   2915 O OE2   . GLU A 1 378 ? 26.359  -25.361 20.117  1.00 63.44 ? 378  GLU A OE2   1 
ATOM   2916 N N     . MET A 1 379 ? 24.799  -21.823 24.748  1.00 30.31 ? 379  MET A N     1 
ATOM   2917 C CA    . MET A 1 379 ? 24.853  -20.463 25.256  1.00 30.68 ? 379  MET A CA    1 
ATOM   2918 C C     . MET A 1 379 ? 26.283  -19.924 25.291  1.00 28.35 ? 379  MET A C     1 
ATOM   2919 O O     . MET A 1 379 ? 26.481  -18.740 25.295  1.00 28.63 ? 379  MET A O     1 
ATOM   2920 C CB    . MET A 1 379 ? 24.205  -20.346 26.621  1.00 29.83 ? 379  MET A CB    1 
ATOM   2921 C CG    . MET A 1 379 ? 22.711  -20.140 26.571  1.00 30.49 ? 379  MET A CG    1 
ATOM   2922 S SD    . MET A 1 379 ? 22.259  -18.673 25.644  1.00 35.87 ? 379  MET A SD    1 
ATOM   2923 C CE    . MET A 1 379 ? 22.904  -17.392 26.712  1.00 35.61 ? 379  MET A CE    1 
ATOM   2924 N N     . LYS A 1 380 ? 27.271  -20.801 25.262  1.00 30.54 ? 380  LYS A N     1 
ATOM   2925 C CA    . LYS A 1 380 ? 28.658  -20.363 25.200  1.00 32.77 ? 380  LYS A CA    1 
ATOM   2926 C C     . LYS A 1 380 ? 28.968  -19.618 23.918  1.00 32.58 ? 380  LYS A C     1 
ATOM   2927 O O     . LYS A 1 380 ? 29.926  -18.885 23.867  1.00 31.38 ? 380  LYS A O     1 
ATOM   2928 C CB    . LYS A 1 380 ? 29.596  -21.526 25.427  1.00 36.40 ? 380  LYS A CB    1 
ATOM   2929 C CG    . LYS A 1 380 ? 29.655  -21.962 26.874  1.00 37.17 ? 380  LYS A CG    1 
ATOM   2930 C CD    . LYS A 1 380 ? 30.832  -22.880 27.108  1.00 46.38 ? 380  LYS A CD    1 
ATOM   2931 C CE    . LYS A 1 380 ? 30.659  -24.183 26.357  1.00 49.49 ? 380  LYS A CE    1 
ATOM   2932 N NZ    . LYS A 1 380 ? 29.453  -24.910 26.812  1.00 52.31 ? 380  LYS A NZ    1 
ATOM   2933 N N     . LEU A 1 381 ? 28.144  -19.771 22.891  1.00 32.42 ? 381  LEU A N     1 
ATOM   2934 C CA    . LEU A 1 381 ? 28.305  -18.995 21.679  1.00 33.69 ? 381  LEU A CA    1 
ATOM   2935 C C     . LEU A 1 381 ? 28.233  -17.520 22.019  1.00 32.09 ? 381  LEU A C     1 
ATOM   2936 O O     . LEU A 1 381 ? 28.879  -16.717 21.392  1.00 31.00 ? 381  LEU A O     1 
ATOM   2937 C CB    . LEU A 1 381 ? 27.179  -19.300 20.695  1.00 42.56 ? 381  LEU A CB    1 
ATOM   2938 C CG    . LEU A 1 381 ? 27.336  -20.324 19.588  1.00 54.88 ? 381  LEU A CG    1 
ATOM   2939 C CD1   . LEU A 1 381 ? 25.978  -20.928 19.298  1.00 61.90 ? 381  LEU A CD1   1 
ATOM   2940 C CD2   . LEU A 1 381 ? 27.850  -19.627 18.348  1.00 65.68 ? 381  LEU A CD2   1 
ATOM   2941 N N     . MET A 1 382 ? 27.433  -17.176 23.015  1.00 28.35 ? 382  MET A N     1 
ATOM   2942 C CA    . MET A 1 382 ? 27.255  -15.787 23.415  1.00 30.89 ? 382  MET A CA    1 
ATOM   2943 C C     . MET A 1 382 ? 28.440  -15.162 24.174  1.00 30.70 ? 382  MET A C     1 
ATOM   2944 O O     . MET A 1 382 ? 28.346  -14.043 24.629  1.00 30.03 ? 382  MET A O     1 
ATOM   2945 C CB    . MET A 1 382 ? 25.911  -15.634 24.140  1.00 32.09 ? 382  MET A CB    1 
ATOM   2946 C CG    . MET A 1 382 ? 24.751  -16.342 23.460  1.00 32.80 ? 382  MET A CG    1 
ATOM   2947 S SD    . MET A 1 382 ? 24.653  -16.083 21.686  1.00 33.49 ? 382  MET A SD    1 
ATOM   2948 C CE    . MET A 1 382 ? 24.307  -14.351 21.641  1.00 32.63 ? 382  MET A CE    1 
ATOM   2949 N N     . ASP A 1 383 ? 29.529  -15.903 24.317  1.00 31.91 ? 383  ASP A N     1 
ATOM   2950 C CA    . ASP A 1 383 ? 30.744  -15.381 24.915  1.00 30.23 ? 383  ASP A CA    1 
ATOM   2951 C C     . ASP A 1 383 ? 31.792  -15.102 23.822  1.00 30.80 ? 383  ASP A C     1 
ATOM   2952 O O     . ASP A 1 383 ? 32.932  -14.872 24.132  1.00 30.63 ? 383  ASP A O     1 
ATOM   2953 C CB    . ASP A 1 383 ? 31.341  -16.391 25.891  1.00 32.00 ? 383  ASP A CB    1 
ATOM   2954 C CG    . ASP A 1 383 ? 30.437  -16.703 27.058  1.00 38.07 ? 383  ASP A CG    1 
ATOM   2955 O OD1   . ASP A 1 383 ? 29.626  -15.846 27.446  1.00 37.82 ? 383  ASP A OD1   1 
ATOM   2956 O OD2   . ASP A 1 383 ? 30.563  -17.817 27.598  1.00 39.27 ? 383  ASP A OD2   1 
ATOM   2957 N N     . TRP A 1 384 ? 31.412  -15.189 22.558  1.00 27.72 ? 384  TRP A N     1 
ATOM   2958 C CA    . TRP A 1 384 ? 32.347  -14.965 21.446  1.00 28.17 ? 384  TRP A CA    1 
ATOM   2959 C C     . TRP A 1 384 ? 32.936  -13.584 21.528  1.00 30.61 ? 384  TRP A C     1 
ATOM   2960 O O     . TRP A 1 384 ? 34.118  -13.439 21.327  1.00 33.80 ? 384  TRP A O     1 
ATOM   2961 C CB    . TRP A 1 384 ? 31.598  -15.108 20.131  1.00 29.16 ? 384  TRP A CB    1 
ATOM   2962 C CG    . TRP A 1 384 ? 32.343  -15.015 18.829  1.00 27.23 ? 384  TRP A CG    1 
ATOM   2963 C CD1   . TRP A 1 384 ? 32.079  -14.152 17.816  1.00 25.84 ? 384  TRP A CD1   1 
ATOM   2964 C CD2   . TRP A 1 384 ? 33.396  -15.867 18.358  1.00 26.21 ? 384  TRP A CD2   1 
ATOM   2965 N NE1   . TRP A 1 384 ? 32.905  -14.390 16.759  1.00 26.46 ? 384  TRP A NE1   1 
ATOM   2966 C CE2   . TRP A 1 384 ? 33.725  -15.440 17.063  1.00 26.07 ? 384  TRP A CE2   1 
ATOM   2967 C CE3   . TRP A 1 384 ? 34.108  -16.929 18.910  1.00 30.46 ? 384  TRP A CE3   1 
ATOM   2968 C CZ2   . TRP A 1 384 ? 34.732  -16.039 16.316  1.00 25.54 ? 384  TRP A CZ2   1 
ATOM   2969 C CZ3   . TRP A 1 384 ? 35.097  -17.530 18.159  1.00 28.84 ? 384  TRP A CZ3   1 
ATOM   2970 C CH2   . TRP A 1 384 ? 35.402  -17.080 16.883  1.00 27.03 ? 384  TRP A CH2   1 
ATOM   2971 N N     . ILE A 1 385 ? 32.080  -12.597 21.784  1.00 31.37 ? 385  ILE A N     1 
ATOM   2972 C CA    . ILE A 1 385 ? 32.485  -11.216 21.886  1.00 31.61 ? 385  ILE A CA    1 
ATOM   2973 C C     . ILE A 1 385 ? 31.755  -10.660 23.095  1.00 34.01 ? 385  ILE A C     1 
ATOM   2974 O O     . ILE A 1 385 ? 30.764  -11.206 23.533  1.00 32.53 ? 385  ILE A O     1 
ATOM   2975 C CB    . ILE A 1 385 ? 32.106  -10.393 20.637  1.00 32.68 ? 385  ILE A CB    1 
ATOM   2976 C CG1   . ILE A 1 385 ? 30.627  -10.529 20.296  1.00 34.05 ? 385  ILE A CG1   1 
ATOM   2977 C CG2   . ILE A 1 385 ? 32.973  -10.745 19.441  1.00 30.27 ? 385  ILE A CG2   1 
ATOM   2978 C CD1   . ILE A 1 385 ? 30.128  -9.445  19.374  1.00 35.58 ? 385  ILE A CD1   1 
ATOM   2979 N N     . PRO A 1 386 ? 32.306  -9.597  23.681  1.00 39.59 ? 386  PRO A N     1 
ATOM   2980 C CA    . PRO A 1 386 ? 31.614  -8.994  24.822  1.00 35.93 ? 386  PRO A CA    1 
ATOM   2981 C C     . PRO A 1 386 ? 30.271  -8.391  24.444  1.00 31.80 ? 386  PRO A C     1 
ATOM   2982 O O     . PRO A 1 386 ? 30.096  -7.765  23.433  1.00 30.35 ? 386  PRO A O     1 
ATOM   2983 C CB    . PRO A 1 386 ? 32.601  -7.940  25.314  1.00 38.26 ? 386  PRO A CB    1 
ATOM   2984 C CG    . PRO A 1 386 ? 33.928  -8.426  24.859  1.00 40.35 ? 386  PRO A CG    1 
ATOM   2985 C CD    . PRO A 1 386 ? 33.671  -9.064  23.531  1.00 38.67 ? 386  PRO A CD    1 
ATOM   2986 N N     . GLY A 1 387 ? 29.309  -8.638  25.316  1.00 50.19 ? 387  GLY A N     1 
ATOM   2987 C CA    . GLY A 1 387 ? 27.930  -8.243  25.144  1.00 36.68 ? 387  GLY A CA    1 
ATOM   2988 C C     . GLY A 1 387 ? 27.225  -8.860  23.970  1.00 30.61 ? 387  GLY A C     1 
ATOM   2989 O O     . GLY A 1 387 ? 26.323  -8.278  23.435  1.00 33.03 ? 387  GLY A O     1 
ATOM   2990 N N     . ALA A 1 388 ? 27.616  -10.056 23.596  1.00 28.50 ? 388  ALA A N     1 
ATOM   2991 C CA    . ALA A 1 388 ? 27.034  -10.699 22.431  1.00 28.66 ? 388  ALA A CA    1 
ATOM   2992 C C     . ALA A 1 388 ? 25.557  -10.927 22.444  1.00 29.23 ? 388  ALA A C     1 
ATOM   2993 O O     . ALA A 1 388 ? 25.000  -11.308 23.436  1.00 29.14 ? 388  ALA A O     1 
ATOM   2994 C CB    . ALA A 1 388 ? 27.733  -11.998 22.111  1.00 27.90 ? 388  ALA A CB    1 
ATOM   2995 N N     . GLY A 1 389 ? 24.936  -10.657 21.329  1.00 29.87 ? 389  GLY A N     1 
ATOM   2996 C CA    . GLY A 1 389 ? 23.541  -10.942 21.174  1.00 31.15 ? 389  GLY A CA    1 
ATOM   2997 C C     . GLY A 1 389 ? 23.382  -11.478 19.770  1.00 31.07 ? 389  GLY A C     1 
ATOM   2998 O O     . GLY A 1 389 ? 24.262  -11.280 18.959  1.00 28.49 ? 389  GLY A O     1 
ATOM   2999 N N     . HIS A 1 390 ? 22.293  -12.174 19.487  1.00 27.86 ? 390  HIS A N     1 
ATOM   3000 C CA    . HIS A 1 390 ? 22.062  -12.587 18.096  1.00 26.56 ? 390  HIS A CA    1 
ATOM   3001 C C     . HIS A 1 390 ? 20.658  -12.194 17.702  1.00 26.66 ? 390  HIS A C     1 
ATOM   3002 O O     . HIS A 1 390 ? 19.744  -12.079 18.589  1.00 25.50 ? 390  HIS A O     1 
ATOM   3003 C CB    . HIS A 1 390 ? 22.405  -14.074 17.929  1.00 29.44 ? 390  HIS A CB    1 
ATOM   3004 C CG    . HIS A 1 390 ? 21.375  -14.980 18.500  1.00 29.29 ? 390  HIS A CG    1 
ATOM   3005 N ND1   . HIS A 1 390 ? 20.206  -15.274 17.830  1.00 28.27 ? 390  HIS A ND1   1 
ATOM   3006 C CD2   . HIS A 1 390 ? 21.325  -15.635 19.671  1.00 27.04 ? 390  HIS A CD2   1 
ATOM   3007 C CE1   . HIS A 1 390 ? 19.488  -16.096 18.560  1.00 29.78 ? 390  HIS A CE1   1 
ATOM   3008 N NE2   . HIS A 1 390 ? 20.148  -16.332 19.677  1.00 29.23 ? 390  HIS A NE2   1 
ATOM   3009 N N     . VAL A 1 391 ? 20.486  -11.989 16.410  1.00 25.97 ? 391  VAL A N     1 
ATOM   3010 C CA    . VAL A 1 391 ? 19.150  -11.916 15.781  1.00 26.28 ? 391  VAL A CA    1 
ATOM   3011 C C     . VAL A 1 391 ? 19.115  -13.035 14.745  1.00 28.45 ? 391  VAL A C     1 
ATOM   3012 O O     . VAL A 1 391 ? 20.191  -13.335 14.137  1.00 31.04 ? 391  VAL A O     1 
ATOM   3013 C CB    . VAL A 1 391 ? 18.863  -10.523 15.204  1.00 27.73 ? 391  VAL A CB    1 
ATOM   3014 C CG1   . VAL A 1 391 ? 19.858  -10.142 14.130  1.00 29.67 ? 391  VAL A CG1   1 
ATOM   3015 C CG2   . VAL A 1 391 ? 17.451  -10.422 14.676  1.00 30.65 ? 391  VAL A CG2   1 
ATOM   3016 N N     . GLY A 1 392 ? 17.955  -13.701 14.692  1.00 27.20 ? 392  GLY A N     1 
ATOM   3017 C CA    . GLY A 1 392 ? 17.698  -14.857 13.829  1.00 27.78 ? 392  GLY A CA    1 
ATOM   3018 C C     . GLY A 1 392 ? 17.451  -14.413 12.405  1.00 25.39 ? 392  GLY A C     1 
ATOM   3019 O O     . GLY A 1 392 ? 16.711  -13.433 12.175  1.00 23.79 ? 392  GLY A O     1 
ATOM   3020 N N     . PHE A 1 393 ? 18.158  -15.049 11.492  1.00 26.21 ? 393  PHE A N     1 
ATOM   3021 C CA    . PHE A 1 393 ? 17.934  -14.938 10.035  1.00 25.15 ? 393  PHE A CA    1 
ATOM   3022 C C     . PHE A 1 393 ? 17.965  -16.384 9.538   1.00 23.67 ? 393  PHE A C     1 
ATOM   3023 O O     . PHE A 1 393 ? 18.967  -17.049 9.783   1.00 22.50 ? 393  PHE A O     1 
ATOM   3024 C CB    . PHE A 1 393 ? 19.018  -14.057 9.397   1.00 25.56 ? 393  PHE A CB    1 
ATOM   3025 C CG    . PHE A 1 393 ? 18.880  -13.957 7.897   1.00 23.63 ? 393  PHE A CG    1 
ATOM   3026 C CD1   . PHE A 1 393 ? 17.811  -13.289 7.328   1.00 24.99 ? 393  PHE A CD1   1 
ATOM   3027 C CD2   . PHE A 1 393 ? 19.765  -14.611 7.053   1.00 25.96 ? 393  PHE A CD2   1 
ATOM   3028 C CE1   . PHE A 1 393 ? 17.651  -13.242 5.955   1.00 24.22 ? 393  PHE A CE1   1 
ATOM   3029 C CE2   . PHE A 1 393 ? 19.624  -14.526 5.681   1.00 22.01 ? 393  PHE A CE2   1 
ATOM   3030 C CZ    . PHE A 1 393 ? 18.564  -13.860 5.141   1.00 22.82 ? 393  PHE A CZ    1 
ATOM   3031 N N     . SER A 1 394 ? 16.888  -16.874 8.931   1.00 22.83 ? 394  SER A N     1 
ATOM   3032 C CA    . SER A 1 394 ? 16.742  -18.323 8.627   1.00 23.82 ? 394  SER A CA    1 
ATOM   3033 C C     . SER A 1 394 ? 15.818  -18.540 7.442   1.00 23.22 ? 394  SER A C     1 
ATOM   3034 O O     . SER A 1 394 ? 14.775  -19.192 7.541   1.00 25.09 ? 394  SER A O     1 
ATOM   3035 C CB    . SER A 1 394 ? 16.231  -19.045 9.822   1.00 24.55 ? 394  SER A CB    1 
ATOM   3036 O OG    . SER A 1 394 ? 15.026  -18.439 10.264  1.00 25.28 ? 394  SER A OG    1 
ATOM   3037 N N     . PRO A 1 395 ? 16.176  -18.024 6.260   1.00 20.49 ? 395  PRO A N     1 
ATOM   3038 C CA    . PRO A 1 395 ? 15.315  -18.197 5.104   1.00 21.97 ? 395  PRO A CA    1 
ATOM   3039 C C     . PRO A 1 395 ? 15.329  -19.639 4.614   1.00 19.63 ? 395  PRO A C     1 
ATOM   3040 O O     . PRO A 1 395 ? 16.253  -20.400 4.906   1.00 21.36 ? 395  PRO A O     1 
ATOM   3041 C CB    . PRO A 1 395 ? 15.920  -17.274 4.050   1.00 23.00 ? 395  PRO A CB    1 
ATOM   3042 C CG    . PRO A 1 395 ? 17.370  -17.207 4.452   1.00 22.09 ? 395  PRO A CG    1 
ATOM   3043 C CD    . PRO A 1 395 ? 17.351  -17.175 5.976   1.00 23.19 ? 395  PRO A CD    1 
ATOM   3044 N N     . ILE A 1 396 ? 14.280  -19.959 3.862   1.00 20.09 ? 396  ILE A N     1 
ATOM   3045 C CA    . ILE A 1 396 ? 14.019  -21.316 3.339   1.00 21.41 ? 396  ILE A CA    1 
ATOM   3046 C C     . ILE A 1 396 ? 14.382  -21.303 1.853   1.00 21.92 ? 396  ILE A C     1 
ATOM   3047 O O     . ILE A 1 396 ? 13.966  -20.359 1.135   1.00 22.76 ? 396  ILE A O     1 
ATOM   3048 C CB    . ILE A 1 396 ? 12.573  -21.774 3.541   1.00 21.85 ? 396  ILE A CB    1 
ATOM   3049 C CG1   . ILE A 1 396 ? 12.074  -21.599 4.979   1.00 24.19 ? 396  ILE A CG1   1 
ATOM   3050 C CG2   . ILE A 1 396 ? 12.420  -23.193 3.070   1.00 22.56 ? 396  ILE A CG2   1 
ATOM   3051 C CD1   . ILE A 1 396 ? 12.898  -22.295 6.000   1.00 24.46 ? 396  ILE A CD1   1 
ATOM   3052 N N     . SER A 1 397 ? 15.082  -22.344 1.438   1.00 22.11 ? 397  SER A N     1 
ATOM   3053 C CA    . SER A 1 397 ? 15.588  -22.492 0.046   1.00 22.57 ? 397  SER A CA    1 
ATOM   3054 C C     . SER A 1 397 ? 15.440  -23.944 -0.365  1.00 20.73 ? 397  SER A C     1 
ATOM   3055 O O     . SER A 1 397 ? 15.240  -24.820 0.481   1.00 22.23 ? 397  SER A O     1 
ATOM   3056 C CB    . SER A 1 397 ? 17.033  -22.020 -0.056  1.00 21.86 ? 397  SER A CB    1 
ATOM   3057 O OG    . SER A 1 397 ? 17.900  -22.856 0.667   1.00 24.91 ? 397  SER A OG    1 
ATOM   3058 N N     . PRO A 1 398 ? 15.515  -24.250 -1.680  1.00 21.55 ? 398  PRO A N     1 
ATOM   3059 C CA    . PRO A 1 398 ? 15.620  -25.633 -2.116  1.00 20.62 ? 398  PRO A CA    1 
ATOM   3060 C C     . PRO A 1 398 ? 16.917  -26.215 -1.590  1.00 22.79 ? 398  PRO A C     1 
ATOM   3061 O O     . PRO A 1 398 ? 17.927  -25.509 -1.560  1.00 23.77 ? 398  PRO A O     1 
ATOM   3062 C CB    . PRO A 1 398 ? 15.606  -25.525 -3.645  1.00 23.17 ? 398  PRO A CB    1 
ATOM   3063 C CG    . PRO A 1 398 ? 14.954  -24.192 -3.934  1.00 21.28 ? 398  PRO A CG    1 
ATOM   3064 C CD    . PRO A 1 398 ? 15.405  -23.299 -2.793  1.00 21.44 ? 398  PRO A CD    1 
ATOM   3065 N N     . PRO A 1 399 ? 16.917  -27.515 -1.205  1.00 23.16 ? 399  PRO A N     1 
ATOM   3066 C CA    . PRO A 1 399 ? 18.102  -28.219 -0.714  1.00 24.13 ? 399  PRO A CA    1 
ATOM   3067 C C     . PRO A 1 399 ? 19.020  -28.670 -1.857  1.00 23.92 ? 399  PRO A C     1 
ATOM   3068 O O     . PRO A 1 399 ? 19.131  -29.861 -2.170  1.00 24.25 ? 399  PRO A O     1 
ATOM   3069 C CB    . PRO A 1 399 ? 17.504  -29.400 0.043   1.00 23.78 ? 399  PRO A CB    1 
ATOM   3070 C CG    . PRO A 1 399 ? 16.215  -29.704 -0.700  1.00 23.91 ? 399  PRO A CG    1 
ATOM   3071 C CD    . PRO A 1 399 ? 15.705  -28.357 -1.155  1.00 23.99 ? 399  PRO A CD    1 
ATOM   3072 N N     . VAL A 1 400 ? 19.583  -27.678 -2.514  1.00 24.36 ? 400  VAL A N     1 
ATOM   3073 C CA    . VAL A 1 400 ? 20.336  -27.799 -3.789  1.00 25.48 ? 400  VAL A CA    1 
ATOM   3074 C C     . VAL A 1 400 ? 21.639  -27.015 -3.584  1.00 25.47 ? 400  VAL A C     1 
ATOM   3075 O O     . VAL A 1 400 ? 21.581  -25.877 -3.063  1.00 21.84 ? 400  VAL A O     1 
ATOM   3076 C CB    . VAL A 1 400 ? 19.489  -27.265 -4.950  1.00 25.60 ? 400  VAL A CB    1 
ATOM   3077 C CG1   . VAL A 1 400 ? 20.279  -27.245 -6.257  1.00 28.46 ? 400  VAL A CG1   1 
ATOM   3078 C CG2   . VAL A 1 400 ? 18.183  -28.034 -5.110  1.00 27.51 ? 400  VAL A CG2   1 
ATOM   3079 N N     . GLY A 1 401 ? 22.775  -27.646 -3.873  1.00 25.30 ? 401  GLY A N     1 
ATOM   3080 C CA    . GLY A 1 401 ? 24.112  -27.085 -3.622  1.00 27.10 ? 401  GLY A CA    1 
ATOM   3081 C C     . GLY A 1 401 ? 24.259  -25.699 -4.214  1.00 27.36 ? 401  GLY A C     1 
ATOM   3082 O O     . GLY A 1 401 ? 24.824  -24.828 -3.544  1.00 24.73 ? 401  GLY A O     1 
ATOM   3083 N N     . ARG A 1 402 ? 23.738  -25.481 -5.406  1.00 28.74 ? 402  ARG A N     1 
ATOM   3084 C CA    . ARG A 1 402 ? 23.833  -24.176 -6.090  1.00 31.15 ? 402  ARG A CA    1 
ATOM   3085 C C     . ARG A 1 402 ? 23.114  -23.119 -5.244  1.00 28.21 ? 402  ARG A C     1 
ATOM   3086 O O     . ARG A 1 402 ? 23.649  -22.018 -5.121  1.00 25.05 ? 402  ARG A O     1 
ATOM   3087 C CB    . ARG A 1 402 ? 23.257  -24.309 -7.498  1.00 38.00 ? 402  ARG A CB    1 
ATOM   3088 C CG    . ARG A 1 402 ? 23.505  -23.113 -8.399  1.00 51.31 ? 402  ARG A CG    1 
ATOM   3089 C CD    . ARG A 1 402 ? 22.225  -22.351 -8.650  1.00 64.43 ? 402  ARG A CD    1 
ATOM   3090 N NE    . ARG A 1 402 ? 21.162  -23.243 -9.110  1.00 70.55 ? 402  ARG A NE    1 
ATOM   3091 C CZ    . ARG A 1 402 ? 19.856  -23.034 -8.943  1.00 79.19 ? 402  ARG A CZ    1 
ATOM   3092 N NH1   . ARG A 1 402 ? 19.408  -21.946 -8.332  1.00 77.79 ? 402  ARG A NH1   1 
ATOM   3093 N NH2   . ARG A 1 402 ? 18.998  -23.929 -9.395  1.00 85.55 ? 402  ARG A NH2   1 
ATOM   3094 N N     . ASP A 1 403 ? 21.948  -23.442 -4.675  1.00 27.19 ? 403  ASP A N     1 
ATOM   3095 C CA    . ASP A 1 403 ? 21.212  -22.506 -3.779  1.00 25.84 ? 403  ASP A CA    1 
ATOM   3096 C C     . ASP A 1 403 ? 22.026  -22.257 -2.511  1.00 26.81 ? 403  ASP A C     1 
ATOM   3097 O O     . ASP A 1 403 ? 22.038  -21.094 -2.027  1.00 26.74 ? 403  ASP A O     1 
ATOM   3098 C CB    . ASP A 1 403 ? 19.808  -23.013 -3.445  1.00 27.38 ? 403  ASP A CB    1 
ATOM   3099 C CG    . ASP A 1 403 ? 18.897  -22.982 -4.666  1.00 28.41 ? 403  ASP A CG    1 
ATOM   3100 O OD1   . ASP A 1 403 ? 18.357  -21.917 -4.994  1.00 24.36 ? 403  ASP A OD1   1 
ATOM   3101 O OD2   . ASP A 1 403 ? 18.798  -24.015 -5.308  1.00 29.74 ? 403  ASP A OD2   1 
ATOM   3102 N N     . ALA A 1 404 ? 22.635  -23.302 -1.945  1.00 26.13 ? 404  ALA A N     1 
ATOM   3103 C CA    . ALA A 1 404 ? 23.478  -23.172 -0.741  1.00 25.59 ? 404  ALA A CA    1 
ATOM   3104 C C     . ALA A 1 404 ? 24.625  -22.204 -1.038  1.00 26.41 ? 404  ALA A C     1 
ATOM   3105 O O     . ALA A 1 404 ? 24.850  -21.308 -0.245  1.00 25.20 ? 404  ALA A O     1 
ATOM   3106 C CB    . ALA A 1 404 ? 23.977  -24.508 -0.308  1.00 25.22 ? 404  ALA A CB    1 
ATOM   3107 N N     . MET A 1 405 ? 25.339  -22.385 -2.157  1.00 24.46 ? 405  MET A N     1 
ATOM   3108 C CA    . MET A 1 405 ? 26.533  -21.561 -2.463  1.00 26.02 ? 405  MET A CA    1 
ATOM   3109 C C     . MET A 1 405 ? 26.102  -20.100 -2.633  1.00 23.57 ? 405  MET A C     1 
ATOM   3110 O O     . MET A 1 405 ? 26.792  -19.221 -2.093  1.00 24.13 ? 405  MET A O     1 
ATOM   3111 C CB    . MET A 1 405 ? 27.218  -22.055 -3.746  1.00 27.23 ? 405  MET A CB    1 
ATOM   3112 C CG    . MET A 1 405 ? 27.912  -23.372 -3.572  1.00 30.69 ? 405  MET A CG    1 
ATOM   3113 S SD    . MET A 1 405 ? 29.237  -23.386 -2.346  1.00 36.10 ? 405  MET A SD    1 
ATOM   3114 C CE    . MET A 1 405 ? 30.213  -21.970 -2.862  1.00 39.22 ? 405  MET A CE    1 
ATOM   3115 N N     . LYS A 1 406 ? 25.014  -19.860 -3.370  1.00 25.51 ? 406  LYS A N     1 
ATOM   3116 C CA    . LYS A 1 406 ? 24.486  -18.498 -3.623  1.00 28.81 ? 406  LYS A CA    1 
ATOM   3117 C C     . LYS A 1 406 ? 24.210  -17.834 -2.265  1.00 28.73 ? 406  LYS A C     1 
ATOM   3118 O O     . LYS A 1 406 ? 24.667  -16.698 -2.048  1.00 23.16 ? 406  LYS A O     1 
ATOM   3119 C CB    . LYS A 1 406 ? 23.245  -18.545 -4.508  1.00 31.50 ? 406  LYS A CB    1 
ATOM   3120 C CG    . LYS A 1 406 ? 22.738  -17.173 -4.912  1.00 35.42 ? 406  LYS A CG    1 
ATOM   3121 C CD    . LYS A 1 406 ? 21.693  -17.232 -6.009  1.00 40.65 ? 406  LYS A CD    1 
ATOM   3122 C CE    . LYS A 1 406 ? 20.431  -17.929 -5.581  1.00 38.58 ? 406  LYS A CE    1 
ATOM   3123 N NZ    . LYS A 1 406 ? 19.382  -17.842 -6.611  1.00 33.30 ? 406  LYS A NZ    1 
ATOM   3124 N N     . GLN A 1 407 ? 23.572  -18.554 -1.343  1.00 25.70 ? 407  GLN A N     1 
ATOM   3125 C CA    . GLN A 1 407 ? 23.185  -17.936 -0.052  1.00 25.96 ? 407  GLN A CA    1 
ATOM   3126 C C     . GLN A 1 407 ? 24.420  -17.706 0.829   1.00 23.77 ? 407  GLN A C     1 
ATOM   3127 O O     . GLN A 1 407 ? 24.518  -16.652 1.467   1.00 24.22 ? 407  GLN A O     1 
ATOM   3128 C CB    . GLN A 1 407 ? 22.176  -18.825 0.656   1.00 25.97 ? 407  GLN A CB    1 
ATOM   3129 C CG    . GLN A 1 407 ? 20.793  -18.700 0.035   1.00 26.39 ? 407  GLN A CG    1 
ATOM   3130 C CD    . GLN A 1 407 ? 19.936  -19.793 0.606   1.00 26.28 ? 407  GLN A CD    1 
ATOM   3131 O OE1   . GLN A 1 407 ? 19.948  -20.935 0.134   1.00 29.57 ? 407  GLN A OE1   1 
ATOM   3132 N NE2   . GLN A 1 407 ? 19.211  -19.435 1.638   1.00 25.12 ? 407  GLN A NE2   1 
ATOM   3133 N N     . PHE A 1 408 ? 25.278  -18.701 0.931   1.00 24.34 ? 408  PHE A N     1 
ATOM   3134 C CA    . PHE A 1 408 ? 26.576  -18.603 1.642   1.00 26.64 ? 408  PHE A CA    1 
ATOM   3135 C C     . PHE A 1 408 ? 27.280  -17.305 1.211   1.00 28.28 ? 408  PHE A C     1 
ATOM   3136 O O     . PHE A 1 408 ? 27.614  -16.475 2.086   1.00 27.46 ? 408  PHE A O     1 
ATOM   3137 C CB    . PHE A 1 408 ? 27.387  -19.870 1.384   1.00 27.28 ? 408  PHE A CB    1 
ATOM   3138 C CG    . PHE A 1 408 ? 28.836  -19.802 1.782   1.00 29.07 ? 408  PHE A CG    1 
ATOM   3139 C CD1   . PHE A 1 408 ? 29.200  -19.282 3.007   1.00 31.77 ? 408  PHE A CD1   1 
ATOM   3140 C CD2   . PHE A 1 408 ? 29.836  -20.283 0.945   1.00 33.10 ? 408  PHE A CD2   1 
ATOM   3141 C CE1   . PHE A 1 408 ? 30.528  -19.248 3.397   1.00 35.21 ? 408  PHE A CE1   1 
ATOM   3142 C CE2   . PHE A 1 408 ? 31.167  -20.247 1.338   1.00 34.62 ? 408  PHE A CE2   1 
ATOM   3143 C CZ    . PHE A 1 408 ? 31.507  -19.729 2.561   1.00 32.84 ? 408  PHE A CZ    1 
ATOM   3144 N N     . ARG A 1 409 ? 27.452  -17.096 -0.096  1.00 28.72 ? 409  ARG A N     1 
ATOM   3145 C CA    . ARG A 1 409 ? 28.194  -15.925 -0.643  1.00 29.39 ? 409  ARG A CA    1 
ATOM   3146 C C     . ARG A 1 409 ? 27.440  -14.620 -0.380  1.00 29.95 ? 409  ARG A C     1 
ATOM   3147 O O     . ARG A 1 409 ? 28.090  -13.669 0.094   1.00 29.96 ? 409  ARG A O     1 
ATOM   3148 C CB    . ARG A 1 409 ? 28.531  -16.113 -2.129  1.00 35.33 ? 409  ARG A CB    1 
ATOM   3149 C CG    . ARG A 1 409 ? 29.300  -17.401 -2.404  1.00 41.25 ? 409  ARG A CG    1 
ATOM   3150 C CD    . ARG A 1 409 ? 30.425  -17.329 -3.423  1.00 50.81 ? 409  ARG A CD    1 
ATOM   3151 N NE    . ARG A 1 409 ? 31.214  -18.564 -3.449  1.00 57.54 ? 409  ARG A NE    1 
ATOM   3152 C CZ    . ARG A 1 409 ? 32.290  -18.831 -2.688  1.00 64.33 ? 409  ARG A CZ    1 
ATOM   3153 N NH1   . ARG A 1 409 ? 32.755  -17.944 -1.821  1.00 67.60 ? 409  ARG A NH1   1 
ATOM   3154 N NH2   . ARG A 1 409 ? 32.911  -19.996 -2.803  1.00 66.65 ? 409  ARG A NH2   1 
ATOM   3155 N N     . MET A 1 410 ? 26.144  -14.557 -0.688  1.00 30.45 ? 410  MET A N     1 
ATOM   3156 C CA    . MET A 1 410 ? 25.250  -13.381 -0.466  1.00 30.61 ? 410  MET A CA    1 
ATOM   3157 C C     . MET A 1 410 ? 25.332  -12.912 0.996   1.00 26.41 ? 410  MET A C     1 
ATOM   3158 O O     . MET A 1 410 ? 25.458  -11.718 1.264   1.00 29.29 ? 410  MET A O     1 
ATOM   3159 C CB    . MET A 1 410 ? 23.781  -13.772 -0.644  1.00 33.77 ? 410  MET A CB    1 
ATOM   3160 C CG    . MET A 1 410 ? 23.359  -13.974 -2.035  1.00 39.20 ? 410  MET A CG    1 
ATOM   3161 S SD    . MET A 1 410 ? 21.700  -14.582 -1.950  1.00 30.50 ? 410  MET A SD    1 
ATOM   3162 C CE    . MET A 1 410 ? 20.808  -13.026 -1.829  1.00 29.89 ? 410  MET A CE    1 
ATOM   3163 N N     . VAL A 1 411 ? 25.128  -13.831 1.918   1.00 25.88 ? 411  VAL A N     1 
ATOM   3164 C CA    . VAL A 1 411 ? 24.993  -13.468 3.356   1.00 24.28 ? 411  VAL A CA    1 
ATOM   3165 C C     . VAL A 1 411 ? 26.384  -13.105 3.908   1.00 25.54 ? 411  VAL A C     1 
ATOM   3166 O O     . VAL A 1 411 ? 26.492  -12.076 4.605   1.00 24.38 ? 411  VAL A O     1 
ATOM   3167 C CB    . VAL A 1 411 ? 24.322  -14.594 4.143   1.00 24.86 ? 411  VAL A CB    1 
ATOM   3168 C CG1   . VAL A 1 411 ? 24.368  -14.324 5.654   1.00 23.95 ? 411  VAL A CG1   1 
ATOM   3169 C CG2   . VAL A 1 411 ? 22.893  -14.814 3.646   1.00 24.94 ? 411  VAL A CG2   1 
ATOM   3170 N N     . ARG A 1 412 ? 27.407  -13.919 3.634   1.00 24.64 ? 412  ARG A N     1 
ATOM   3171 C CA    . ARG A 1 412 ? 28.767  -13.630 4.152   1.00 27.65 ? 412  ARG A CA    1 
ATOM   3172 C C     . ARG A 1 412 ? 29.249  -12.275 3.624   1.00 28.31 ? 412  ARG A C     1 
ATOM   3173 O O     . ARG A 1 412 ? 29.817  -11.535 4.434   1.00 29.08 ? 412  ARG A O     1 
ATOM   3174 C CB    . ARG A 1 412 ? 29.803  -14.704 3.819   1.00 31.32 ? 412  ARG A CB    1 
ATOM   3175 C CG    . ARG A 1 412 ? 31.172  -14.373 4.403   1.00 29.49 ? 412  ARG A CG    1 
ATOM   3176 C CD    . ARG A 1 412 ? 32.175  -15.480 4.292   1.00 29.88 ? 412  ARG A CD    1 
ATOM   3177 N NE    . ARG A 1 412 ? 32.520  -15.747 2.908   1.00 30.74 ? 412  ARG A NE    1 
ATOM   3178 C CZ    . ARG A 1 412 ? 33.418  -16.630 2.518   1.00 29.56 ? 412  ARG A CZ    1 
ATOM   3179 N NH1   . ARG A 1 412 ? 34.076  -17.341 3.415   1.00 28.35 ? 412  ARG A NH1   1 
ATOM   3180 N NH2   . ARG A 1 412 ? 33.645  -16.810 1.222   1.00 32.83 ? 412  ARG A NH2   1 
ATOM   3181 N N     . SER A 1 413 ? 29.044  -11.961 2.344   1.00 26.61 ? 413  SER A N     1 
ATOM   3182 C CA    . SER A 1 413 ? 29.557  -10.691 1.761   1.00 33.22 ? 413  SER A CA    1 
ATOM   3183 C C     . SER A 1 413 ? 28.863  -9.512  2.454   1.00 29.83 ? 413  SER A C     1 
ATOM   3184 O O     . SER A 1 413 ? 29.546  -8.548  2.811   1.00 26.63 ? 413  SER A O     1 
ATOM   3185 C CB    . SER A 1 413 ? 29.440  -10.627 0.261   1.00 33.78 ? 413  SER A CB    1 
ATOM   3186 O OG    . SER A 1 413 ? 28.093  -10.716 -0.133  1.00 41.23 ? 413  SER A OG    1 
ATOM   3187 N N     . ARG A 1 414 ? 27.560  -9.619  2.717   1.00 27.00 ? 414  ARG A N     1 
ATOM   3188 C CA    . ARG A 1 414 ? 26.821  -8.551  3.432   1.00 27.87 ? 414  ARG A CA    1 
ATOM   3189 C C     . ARG A 1 414 ? 27.297  -8.511  4.892   1.00 26.76 ? 414  ARG A C     1 
ATOM   3190 O O     . ARG A 1 414 ? 27.500  -7.411  5.404   1.00 27.22 ? 414  ARG A O     1 
ATOM   3191 C CB    . ARG A 1 414 ? 25.305  -8.749  3.289   1.00 30.17 ? 414  ARG A CB    1 
ATOM   3192 C CG    . ARG A 1 414 ? 24.757  -8.472  1.900   1.00 28.94 ? 414  ARG A CG    1 
ATOM   3193 C CD    . ARG A 1 414 ? 25.345  -7.271  1.213   1.00 29.55 ? 414  ARG A CD    1 
ATOM   3194 N NE    . ARG A 1 414 ? 24.638  -6.971  -0.014  1.00 29.59 ? 414  ARG A NE    1 
ATOM   3195 C CZ    . ARG A 1 414 ? 24.854  -5.895  -0.782  1.00 33.24 ? 414  ARG A CZ    1 
ATOM   3196 N NH1   . ARG A 1 414 ? 25.769  -4.995  -0.457  1.00 32.83 ? 414  ARG A NH1   1 
ATOM   3197 N NH2   . ARG A 1 414 ? 24.143  -5.710  -1.879  1.00 33.89 ? 414  ARG A NH2   1 
ATOM   3198 N N     . ALA A 1 415 ? 27.442  -9.647  5.558   1.00 26.93 ? 415  ALA A N     1 
ATOM   3199 C CA    . ALA A 1 415 ? 27.914  -9.679  6.962   1.00 25.59 ? 415  ALA A CA    1 
ATOM   3200 C C     . ALA A 1 415 ? 29.274  -8.954  7.030   1.00 29.57 ? 415  ALA A C     1 
ATOM   3201 O O     . ALA A 1 415 ? 29.469  -8.089  7.902   1.00 27.55 ? 415  ALA A O     1 
ATOM   3202 C CB    . ALA A 1 415 ? 27.985  -11.103 7.459   1.00 28.93 ? 415  ALA A CB    1 
ATOM   3203 N N     . ASP A 1 416 ? 30.182  -9.258  6.099   1.00 30.98 ? 416  ASP A N     1 
ATOM   3204 C CA    . ASP A 1 416 ? 31.540  -8.641  6.042   1.00 30.53 ? 416  ASP A CA    1 
ATOM   3205 C C     . ASP A 1 416 ? 31.384  -7.123  5.950   1.00 28.99 ? 416  ASP A C     1 
ATOM   3206 O O     . ASP A 1 416 ? 31.987  -6.420  6.772   1.00 30.24 ? 416  ASP A O     1 
ATOM   3207 C CB    . ASP A 1 416 ? 32.347  -9.194  4.865   1.00 30.48 ? 416  ASP A CB    1 
ATOM   3208 C CG    . ASP A 1 416 ? 32.905  -10.594 5.071   1.00 32.11 ? 416  ASP A CG    1 
ATOM   3209 O OD1   . ASP A 1 416 ? 32.964  -11.049 6.234   1.00 29.05 ? 416  ASP A OD1   1 
ATOM   3210 O OD2   . ASP A 1 416 ? 33.305  -11.220 4.057   1.00 33.62 ? 416  ASP A OD2   1 
ATOM   3211 N N     . GLU A 1 417 ? 30.550  -6.662  5.018   1.00 27.25 ? 417  GLU A N     1 
ATOM   3212 C CA    . GLU A 1 417 ? 30.254  -5.235  4.763   1.00 31.02 ? 417  GLU A CA    1 
ATOM   3213 C C     . GLU A 1 417 ? 29.764  -4.586  6.063   1.00 30.91 ? 417  GLU A C     1 
ATOM   3214 O O     . GLU A 1 417 ? 30.248  -3.484  6.352   1.00 26.96 ? 417  GLU A O     1 
ATOM   3215 C CB    . GLU A 1 417 ? 29.239  -5.158  3.629   1.00 33.21 ? 417  GLU A CB    1 
ATOM   3216 C CG    . GLU A 1 417 ? 28.829  -3.761  3.196   1.00 34.25 ? 417  GLU A CG    1 
ATOM   3217 C CD    . GLU A 1 417 ? 27.863  -3.819  2.020   1.00 36.63 ? 417  GLU A CD    1 
ATOM   3218 O OE1   . GLU A 1 417 ? 27.331  -2.736  1.598   1.00 39.27 ? 417  GLU A OE1   1 
ATOM   3219 O OE2   . GLU A 1 417 ? 27.652  -4.952  1.508   1.00 33.66 ? 417  GLU A OE2   1 
ATOM   3220 N N     . TYR A 1 418 ? 28.913  -5.271  6.845   1.00 26.32 ? 418  TYR A N     1 
ATOM   3221 C CA    . TYR A 1 418 ? 28.233  -4.702  8.045   1.00 28.21 ? 418  TYR A CA    1 
ATOM   3222 C C     . TYR A 1 418 ? 28.950  -5.087  9.335   1.00 28.52 ? 418  TYR A C     1 
ATOM   3223 O O     . TYR A 1 418 ? 28.371  -4.828  10.433  1.00 26.01 ? 418  TYR A O     1 
ATOM   3224 C CB    . TYR A 1 418 ? 26.749  -5.100  8.057   1.00 28.12 ? 418  TYR A CB    1 
ATOM   3225 C CG    . TYR A 1 418 ? 25.927  -4.244  7.134   1.00 25.92 ? 418  TYR A CG    1 
ATOM   3226 C CD1   . TYR A 1 418 ? 25.937  -4.467  5.774   1.00 25.34 ? 418  TYR A CD1   1 
ATOM   3227 C CD2   . TYR A 1 418 ? 25.132  -3.216  7.600   1.00 24.75 ? 418  TYR A CD2   1 
ATOM   3228 C CE1   . TYR A 1 418 ? 25.218  -3.666  4.906   1.00 25.47 ? 418  TYR A CE1   1 
ATOM   3229 C CE2   . TYR A 1 418 ? 24.400  -2.417  6.747   1.00 24.37 ? 418  TYR A CE2   1 
ATOM   3230 C CZ    . TYR A 1 418 ? 24.437  -2.641  5.389   1.00 25.06 ? 418  TYR A CZ    1 
ATOM   3231 O OH    . TYR A 1 418 ? 23.724  -1.868  4.523   1.00 29.40 ? 418  TYR A OH    1 
ATOM   3232 N N     . ALA A 1 419 ? 30.170  -5.580  9.215   1.00 28.99 ? 419  ALA A N     1 
ATOM   3233 C CA    . ALA A 1 419 ? 31.009  -5.872  10.364  1.00 31.51 ? 419  ALA A CA    1 
ATOM   3234 C C     . ALA A 1 419 ? 30.537  -6.953  11.307  1.00 30.34 ? 419  ALA A C     1 
ATOM   3235 O O     . ALA A 1 419 ? 30.776  -6.882  12.493  1.00 29.86 ? 419  ALA A O     1 
ATOM   3236 C CB    . ALA A 1 419 ? 31.358  -4.578  11.094  1.00 34.17 ? 419  ALA A CB    1 
ATOM   3237 N N     . LYS A 1 420 ? 29.877  -7.954  10.760  1.00 29.08 ? 420  LYS A N     1 
ATOM   3238 C CA    . LYS A 1 420 ? 29.392  -9.045  11.563  1.00 29.44 ? 420  LYS A CA    1 
ATOM   3239 C C     . LYS A 1 420 ? 30.007  -10.327 11.043  1.00 28.88 ? 420  LYS A C     1 
ATOM   3240 O O     . LYS A 1 420 ? 30.140  -10.524 9.868   1.00 28.60 ? 420  LYS A O     1 
ATOM   3241 C CB    . LYS A 1 420 ? 27.862  -9.125  11.534  1.00 29.31 ? 420  LYS A CB    1 
ATOM   3242 C CG    . LYS A 1 420 ? 27.133  -7.833  11.862  1.00 28.78 ? 420  LYS A CG    1 
ATOM   3243 C CD    . LYS A 1 420 ? 27.319  -7.438  13.311  1.00 28.95 ? 420  LYS A CD    1 
ATOM   3244 C CE    . LYS A 1 420 ? 27.091  -5.954  13.510  1.00 30.81 ? 420  LYS A CE    1 
ATOM   3245 N NZ    . LYS A 1 420 ? 28.330  -5.171  13.338  1.00 33.43 ? 420  LYS A NZ    1 
ATOM   3246 N N     . ASP A 1 421 ? 30.412  -11.171 11.964  1.00 47.02 ? 421  ASP A N     1 
ATOM   3247 C CA    . ASP A 1 421 ? 31.016  -12.427 11.616  1.00 41.41 ? 421  ASP A CA    1 
ATOM   3248 C C     . ASP A 1 421 ? 30.026  -13.374 10.966  1.00 34.46 ? 421  ASP A C     1 
ATOM   3249 O O     . ASP A 1 421 ? 28.877  -13.424 11.326  1.00 30.95 ? 421  ASP A O     1 
ATOM   3250 C CB    . ASP A 1 421 ? 31.596  -13.133 12.821  1.00 43.10 ? 421  ASP A CB    1 
ATOM   3251 C CG    . ASP A 1 421 ? 32.809  -12.449 13.377  1.00 34.97 ? 421  ASP A CG    1 
ATOM   3252 O OD1   . ASP A 1 421 ? 33.479  -11.689 12.662  1.00 39.60 ? 421  ASP A OD1   1 
ATOM   3253 O OD2   . ASP A 1 421 ? 33.095  -12.700 14.546  1.00 34.84 ? 421  ASP A OD2   1 
ATOM   3254 N N     . TYR A 1 422 ? 30.513  -14.118 9.995   1.00 33.13 ? 422  TYR A N     1 
ATOM   3255 C CA    . TYR A 1 422 ? 29.678  -15.107 9.361   1.00 29.49 ? 422  TYR A CA    1 
ATOM   3256 C C     . TYR A 1 422 ? 29.719  -16.440 10.082  1.00 26.34 ? 422  TYR A C     1 
ATOM   3257 O O     . TYR A 1 422 ? 30.649  -17.188 9.921   1.00 26.46 ? 422  TYR A O     1 
ATOM   3258 C CB    . TYR A 1 422 ? 29.919  -15.224 7.869   1.00 29.92 ? 422  TYR A CB    1 
ATOM   3259 C CG    . TYR A 1 422 ? 29.076  -16.287 7.211   1.00 27.68 ? 422  TYR A CG    1 
ATOM   3260 C CD1   . TYR A 1 422 ? 27.755  -16.050 6.886   1.00 26.41 ? 422  TYR A CD1   1 
ATOM   3261 C CD2   . TYR A 1 422 ? 29.607  -17.531 6.918   1.00 27.66 ? 422  TYR A CD2   1 
ATOM   3262 C CE1   . TYR A 1 422 ? 26.989  -17.022 6.286   1.00 27.29 ? 422  TYR A CE1   1 
ATOM   3263 C CE2   . TYR A 1 422 ? 28.845  -18.510 6.345   1.00 28.31 ? 422  TYR A CE2   1 
ATOM   3264 C CZ    . TYR A 1 422 ? 27.544  -18.248 6.011   1.00 26.19 ? 422  TYR A CZ    1 
ATOM   3265 O OH    . TYR A 1 422 ? 26.810  -19.239 5.425   1.00 25.39 ? 422  TYR A OH    1 
ATOM   3266 N N     . ALA A 1 423 ? 28.772  -16.653 10.944  1.00 25.89 ? 423  ALA A N     1 
ATOM   3267 C CA    . ALA A 1 423 ? 28.505  -17.886 11.690  1.00 29.06 ? 423  ALA A CA    1 
ATOM   3268 C C     . ALA A 1 423 ? 27.145  -18.379 11.201  1.00 29.53 ? 423  ALA A C     1 
ATOM   3269 O O     . ALA A 1 423 ? 26.137  -17.648 11.355  1.00 29.21 ? 423  ALA A O     1 
ATOM   3270 C CB    . ALA A 1 423 ? 28.472  -17.580 13.161  1.00 27.86 ? 423  ALA A CB    1 
ATOM   3271 N N     . ALA A 1 424 ? 27.101  -19.550 10.589  1.00 30.27 ? 424  ALA A N     1 
ATOM   3272 C CA    . ALA A 1 424 ? 25.853  -20.026 9.984   1.00 29.08 ? 424  ALA A CA    1 
ATOM   3273 C C     . ALA A 1 424 ? 25.895  -21.538 9.848   1.00 28.13 ? 424  ALA A C     1 
ATOM   3274 O O     . ALA A 1 424 ? 26.999  -22.124 9.820   1.00 25.03 ? 424  ALA A O     1 
ATOM   3275 C CB    . ALA A 1 424 ? 25.640  -19.366 8.651   1.00 28.84 ? 424  ALA A CB    1 
ATOM   3276 N N     . GLN A 1 425 ? 24.706  -22.120 9.719   1.00 25.22 ? 425  GLN A N     1 
ATOM   3277 C CA    . GLN A 1 425 ? 24.559  -23.539 9.353   1.00 24.52 ? 425  GLN A CA    1 
ATOM   3278 C C     . GLN A 1 425 ? 23.495  -23.669 8.270   1.00 25.06 ? 425  GLN A C     1 
ATOM   3279 O O     . GLN A 1 425 ? 22.656  -22.780 8.135   1.00 23.98 ? 425  GLN A O     1 
ATOM   3280 C CB    . GLN A 1 425 ? 24.221  -24.348 10.595  1.00 25.43 ? 425  GLN A CB    1 
ATOM   3281 C CG    . GLN A 1 425 ? 22.918  -23.942 11.243  1.00 25.90 ? 425  GLN A CG    1 
ATOM   3282 C CD    . GLN A 1 425 ? 22.679  -24.764 12.470  1.00 25.00 ? 425  GLN A CD    1 
ATOM   3283 O OE1   . GLN A 1 425 ? 22.884  -25.982 12.486  1.00 28.17 ? 425  GLN A OE1   1 
ATOM   3284 N NE2   . GLN A 1 425 ? 22.279  -24.073 13.525  1.00 26.74 ? 425  GLN A NE2   1 
ATOM   3285 N N     . PHE A 1 426 ? 23.608  -24.724 7.479   1.00 23.50 ? 426  PHE A N     1 
ATOM   3286 C CA    . PHE A 1 426 ? 22.540  -25.201 6.580   1.00 24.34 ? 426  PHE A CA    1 
ATOM   3287 C C     . PHE A 1 426 ? 21.920  -26.438 7.223   1.00 25.12 ? 426  PHE A C     1 
ATOM   3288 O O     . PHE A 1 426 ? 22.651  -27.340 7.681   1.00 26.70 ? 426  PHE A O     1 
ATOM   3289 C CB    . PHE A 1 426 ? 23.125  -25.462 5.199   1.00 24.00 ? 426  PHE A CB    1 
ATOM   3290 C CG    . PHE A 1 426 ? 23.486  -24.214 4.464   1.00 24.72 ? 426  PHE A CG    1 
ATOM   3291 C CD1   . PHE A 1 426 ? 24.734  -23.631 4.629   1.00 23.98 ? 426  PHE A CD1   1 
ATOM   3292 C CD2   . PHE A 1 426 ? 22.541  -23.576 3.673   1.00 25.31 ? 426  PHE A CD2   1 
ATOM   3293 C CE1   . PHE A 1 426 ? 25.058  -22.471 3.948   1.00 26.75 ? 426  PHE A CE1   1 
ATOM   3294 C CE2   . PHE A 1 426 ? 22.867  -22.413 3.003   1.00 25.65 ? 426  PHE A CE2   1 
ATOM   3295 C CZ    . PHE A 1 426 ? 24.121  -21.851 3.159   1.00 26.79 ? 426  PHE A CZ    1 
ATOM   3296 N N     . VAL A 1 427 ? 20.591  -26.471 7.250   1.00 26.04 ? 427  VAL A N     1 
ATOM   3297 C CA    . VAL A 1 427 ? 19.794  -27.555 7.891   1.00 26.70 ? 427  VAL A CA    1 
ATOM   3298 C C     . VAL A 1 427 ? 18.769  -28.012 6.861   1.00 29.29 ? 427  VAL A C     1 
ATOM   3299 O O     . VAL A 1 427 ? 18.125  -27.136 6.258   1.00 24.91 ? 427  VAL A O     1 
ATOM   3300 C CB    . VAL A 1 427 ? 19.095  -27.038 9.158   1.00 28.73 ? 427  VAL A CB    1 
ATOM   3301 C CG1   . VAL A 1 427 ? 18.240  -28.113 9.814   1.00 26.92 ? 427  VAL A CG1   1 
ATOM   3302 C CG2   . VAL A 1 427 ? 20.099  -26.448 10.132  1.00 29.69 ? 427  VAL A CG2   1 
ATOM   3303 N N     . VAL A 1 428 ? 18.668  -29.311 6.596   1.00 30.80 ? 428  VAL A N     1 
ATOM   3304 C CA    . VAL A 1 428 ? 17.581  -29.801 5.699   1.00 32.36 ? 428  VAL A CA    1 
ATOM   3305 C C     . VAL A 1 428 ? 16.568  -30.553 6.574   1.00 32.02 ? 428  VAL A C     1 
ATOM   3306 O O     . VAL A 1 428 ? 16.924  -31.525 7.242   1.00 30.73 ? 428  VAL A O     1 
ATOM   3307 C CB    . VAL A 1 428 ? 18.102  -30.615 4.500   1.00 37.35 ? 428  VAL A CB    1 
ATOM   3308 C CG1   . VAL A 1 428 ? 19.120  -29.819 3.698   1.00 36.29 ? 428  VAL A CG1   1 
ATOM   3309 C CG2   . VAL A 1 428 ? 18.663  -31.946 4.926   1.00 44.65 ? 428  VAL A CG2   1 
ATOM   3310 N N     . GLY A 1 429 ? 15.339  -30.074 6.581   1.00 29.41 ? 429  GLY A N     1 
ATOM   3311 C CA    . GLY A 1 429 ? 14.244  -30.733 7.307   1.00 30.83 ? 429  GLY A CA    1 
ATOM   3312 C C     . GLY A 1 429 ? 13.919  -32.051 6.640   1.00 27.57 ? 429  GLY A C     1 
ATOM   3313 O O     . GLY A 1 429 ? 14.148  -33.078 7.257   1.00 30.84 ? 429  GLY A O     1 
ATOM   3314 N N     . LEU A 1 430 ? 13.405  -31.987 5.421   1.00 26.88 ? 430  LEU A N     1 
ATOM   3315 C CA    . LEU A 1 430 ? 13.069  -33.162 4.588   1.00 26.60 ? 430  LEU A CA    1 
ATOM   3316 C C     . LEU A 1 430 ? 13.314  -32.808 3.128   1.00 26.84 ? 430  LEU A C     1 
ATOM   3317 O O     . LEU A 1 430 ? 14.219  -33.421 2.516   1.00 28.05 ? 430  LEU A O     1 
ATOM   3318 C CB    . LEU A 1 430 ? 11.616  -33.560 4.844   1.00 28.54 ? 430  LEU A CB    1 
ATOM   3319 C CG    . LEU A 1 430 ? 11.220  -34.926 4.305   1.00 29.10 ? 430  LEU A CG    1 
ATOM   3320 C CD1   . LEU A 1 430 ? 12.060  -36.021 4.930   1.00 28.08 ? 430  LEU A CD1   1 
ATOM   3321 C CD2   . LEU A 1 430 ? 9.729   -35.179 4.553   1.00 32.12 ? 430  LEU A CD2   1 
ATOM   3322 N N     . ARG A 1 431 ? 12.546  -31.854 2.613   1.00 23.49 ? 431  ARG A N     1 
ATOM   3323 C CA    . ARG A 1 431 ? 12.657  -31.348 1.221   1.00 25.44 ? 431  ARG A CA    1 
ATOM   3324 C C     . ARG A 1 431 ? 13.043  -29.874 1.193   1.00 22.97 ? 431  ARG A C     1 
ATOM   3325 O O     . ARG A 1 431 ? 13.055  -29.292 0.105   1.00 24.27 ? 431  ARG A O     1 
ATOM   3326 C CB    . ARG A 1 431 ? 11.303  -31.425 0.527   1.00 25.31 ? 431  ARG A CB    1 
ATOM   3327 C CG    . ARG A 1 431 ? 10.868  -32.823 0.169   1.00 28.35 ? 431  ARG A CG    1 
ATOM   3328 C CD    . ARG A 1 431 ? 9.524   -32.732 -0.527  1.00 25.87 ? 431  ARG A CD    1 
ATOM   3329 N NE    . ARG A 1 431 ? 9.260   -34.056 -1.001  1.00 25.78 ? 431  ARG A NE    1 
ATOM   3330 C CZ    . ARG A 1 431 ? 8.900   -35.072 -0.232  1.00 27.14 ? 431  ARG A CZ    1 
ATOM   3331 N NH1   . ARG A 1 431 ? 8.641   -34.884 1.049   1.00 26.82 ? 431  ARG A NH1   1 
ATOM   3332 N NH2   . ARG A 1 431 ? 8.720   -36.268 -0.767  1.00 29.75 ? 431  ARG A NH2   1 
ATOM   3333 N N     . GLU A 1 432 ? 13.258  -29.269 2.355   1.00 23.60 ? 432  GLU A N     1 
ATOM   3334 C CA    . GLU A 1 432 ? 13.479  -27.811 2.455   1.00 23.96 ? 432  GLU A CA    1 
ATOM   3335 C C     . GLU A 1 432 ? 14.799  -27.573 3.181   1.00 23.12 ? 432  GLU A C     1 
ATOM   3336 O O     . GLU A 1 432 ? 15.138  -28.367 4.075   1.00 23.22 ? 432  GLU A O     1 
ATOM   3337 C CB    . GLU A 1 432 ? 12.287  -27.117 3.113   1.00 23.49 ? 432  GLU A CB    1 
ATOM   3338 C CG    . GLU A 1 432 ? 12.360  -26.974 4.616   1.00 25.31 ? 432  GLU A CG    1 
ATOM   3339 C CD    . GLU A 1 432 ? 12.370  -28.224 5.462   1.00 25.95 ? 432  GLU A CD    1 
ATOM   3340 O OE1   . GLU A 1 432 ? 12.609  -28.082 6.684   1.00 25.15 ? 432  GLU A OE1   1 
ATOM   3341 O OE2   . GLU A 1 432 ? 12.170  -29.327 4.921   1.00 26.50 ? 432  GLU A OE2   1 
ATOM   3342 N N     . MET A 1 433 ? 15.495  -26.500 2.803   1.00 24.36 ? 433  MET A N     1 
ATOM   3343 C CA    . MET A 1 433 ? 16.783  -26.108 3.414   1.00 23.01 ? 433  MET A CA    1 
ATOM   3344 C C     . MET A 1 433 ? 16.598  -24.790 4.181   1.00 23.19 ? 433  MET A C     1 
ATOM   3345 O O     . MET A 1 433 ? 15.848  -23.923 3.717   1.00 21.96 ? 433  MET A O     1 
ATOM   3346 C CB    . MET A 1 433 ? 17.860  -25.950 2.338   1.00 23.66 ? 433  MET A CB    1 
ATOM   3347 C CG    . MET A 1 433 ? 19.233  -25.754 2.933   1.00 24.65 ? 433  MET A CG    1 
ATOM   3348 S SD    . MET A 1 433 ? 20.568  -26.208 1.746   1.00 26.32 ? 433  MET A SD    1 
ATOM   3349 C CE    . MET A 1 433 ? 20.349  -24.869 0.576   1.00 29.28 ? 433  MET A CE    1 
ATOM   3350 N N     . HIS A 1 434 ? 17.215  -24.696 5.351   1.00 23.07 ? 434  HIS A N     1 
ATOM   3351 C CA    . HIS A 1 434 ? 17.273  -23.468 6.165   1.00 24.71 ? 434  HIS A CA    1 
ATOM   3352 C C     . HIS A 1 434 ? 18.729  -23.006 6.199   1.00 24.24 ? 434  HIS A C     1 
ATOM   3353 O O     . HIS A 1 434 ? 19.627  -23.860 6.424   1.00 23.01 ? 434  HIS A O     1 
ATOM   3354 C CB    . HIS A 1 434 ? 16.781  -23.737 7.591   1.00 24.23 ? 434  HIS A CB    1 
ATOM   3355 C CG    . HIS A 1 434 ? 15.486  -24.464 7.681   1.00 26.10 ? 434  HIS A CG    1 
ATOM   3356 N ND1   . HIS A 1 434 ? 14.416  -23.962 8.380   1.00 29.85 ? 434  HIS A ND1   1 
ATOM   3357 C CD2   . HIS A 1 434 ? 15.099  -25.684 7.243   1.00 28.75 ? 434  HIS A CD2   1 
ATOM   3358 C CE1   . HIS A 1 434 ? 13.418  -24.835 8.353   1.00 30.03 ? 434  HIS A CE1   1 
ATOM   3359 N NE2   . HIS A 1 434 ? 13.795  -25.877 7.643   1.00 28.92 ? 434  HIS A NE2   1 
ATOM   3360 N N     . HIS A 1 435 ? 18.932  -21.715 5.973   1.00 22.48 ? 435  HIS A N     1 
ATOM   3361 C CA    . HIS A 1 435 ? 20.240  -21.046 6.143   1.00 23.25 ? 435  HIS A CA    1 
ATOM   3362 C C     . HIS A 1 435 ? 20.125  -20.210 7.409   1.00 22.31 ? 435  HIS A C     1 
ATOM   3363 O O     . HIS A 1 435 ? 19.508  -19.163 7.315   1.00 24.52 ? 435  HIS A O     1 
ATOM   3364 C CB    . HIS A 1 435 ? 20.585  -20.230 4.900   1.00 22.30 ? 435  HIS A CB    1 
ATOM   3365 C CG    . HIS A 1 435 ? 21.956  -19.649 4.971   1.00 22.61 ? 435  HIS A CG    1 
ATOM   3366 N ND1   . HIS A 1 435 ? 22.311  -18.554 4.243   1.00 21.61 ? 435  HIS A ND1   1 
ATOM   3367 C CD2   . HIS A 1 435 ? 23.031  -19.965 5.713   1.00 24.40 ? 435  HIS A CD2   1 
ATOM   3368 C CE1   . HIS A 1 435 ? 23.577  -18.253 4.490   1.00 22.05 ? 435  HIS A CE1   1 
ATOM   3369 N NE2   . HIS A 1 435 ? 24.035  -19.084 5.400   1.00 23.51 ? 435  HIS A NE2   1 
ATOM   3370 N N     . ILE A 1 436 ? 20.547  -20.771 8.543   1.00 23.95 ? 436  ILE A N     1 
ATOM   3371 C CA    . ILE A 1 436 ? 20.373  -20.181 9.896   1.00 22.45 ? 436  ILE A CA    1 
ATOM   3372 C C     . ILE A 1 436 ? 21.673  -19.457 10.242  1.00 22.61 ? 436  ILE A C     1 
ATOM   3373 O O     . ILE A 1 436 ? 22.668  -20.124 10.528  1.00 24.07 ? 436  ILE A O     1 
ATOM   3374 C CB    . ILE A 1 436 ? 20.011  -21.249 10.933  1.00 23.97 ? 436  ILE A CB    1 
ATOM   3375 C CG1   . ILE A 1 436 ? 18.859  -22.120 10.417  1.00 25.87 ? 436  ILE A CG1   1 
ATOM   3376 C CG2   . ILE A 1 436 ? 19.696  -20.578 12.261  1.00 25.82 ? 436  ILE A CG2   1 
ATOM   3377 C CD1   . ILE A 1 436 ? 18.420  -23.233 11.343  1.00 25.50 ? 436  ILE A CD1   1 
ATOM   3378 N N     . ALA A 1 437 ? 21.652  -18.139 10.162  1.00 23.77 ? 437  ALA A N     1 
ATOM   3379 C CA    . ALA A 1 437 ? 22.842  -17.282 10.346  1.00 26.15 ? 437  ALA A CA    1 
ATOM   3380 C C     . ALA A 1 437 ? 22.711  -16.664 11.726  1.00 29.68 ? 437  ALA A C     1 
ATOM   3381 O O     . ALA A 1 437 ? 21.645  -16.076 11.999  1.00 32.17 ? 437  ALA A O     1 
ATOM   3382 C CB    . ALA A 1 437 ? 22.928  -16.229 9.286   1.00 27.85 ? 437  ALA A CB    1 
ATOM   3383 N N     . LEU A 1 438 ? 23.709  -16.904 12.569  1.00 32.19 ? 438  LEU A N     1 
ATOM   3384 C CA    . LEU A 1 438 ? 23.789  -16.259 13.895  1.00 35.90 ? 438  LEU A CA    1 
ATOM   3385 C C     . LEU A 1 438 ? 24.614  -14.998 13.688  1.00 34.23 ? 438  LEU A C     1 
ATOM   3386 O O     . LEU A 1 438 ? 25.843  -15.103 13.526  1.00 33.03 ? 438  LEU A O     1 
ATOM   3387 C CB    . LEU A 1 438 ? 24.347  -17.225 14.941  1.00 42.41 ? 438  LEU A CB    1 
ATOM   3388 C CG    . LEU A 1 438 ? 23.481  -17.343 16.206  1.00 52.73 ? 438  LEU A CG    1 
ATOM   3389 C CD1   . LEU A 1 438 ? 21.986  -17.416 15.876  1.00 60.74 ? 438  LEU A CD1   1 
ATOM   3390 C CD2   . LEU A 1 438 ? 23.881  -18.563 17.018  1.00 58.11 ? 438  LEU A CD2   1 
ATOM   3391 N N     . LEU A 1 439 ? 23.888  -13.885 13.590  1.00 38.74 ? 439  LEU A N     1 
ATOM   3392 C CA    . LEU A 1 439 ? 24.428  -12.517 13.422  1.00 44.05 ? 439  LEU A CA    1 
ATOM   3393 C C     . LEU A 1 439 ? 24.765  -11.987 14.817  1.00 37.32 ? 439  LEU A C     1 
ATOM   3394 O O     . LEU A 1 439 ? 23.798  -11.578 15.550  1.00 41.92 ? 439  LEU A O     1 
ATOM   3395 C CB    . LEU A 1 439 ? 23.349  -11.683 12.728  1.00 47.77 ? 439  LEU A CB    1 
ATOM   3396 C CG    . LEU A 1 439 ? 22.925  -12.206 11.355  1.00 50.34 ? 439  LEU A CG    1 
ATOM   3397 C CD1   . LEU A 1 439 ? 21.944  -11.230 10.713  1.00 51.91 ? 439  LEU A CD1   1 
ATOM   3398 C CD2   . LEU A 1 439 ? 24.146  -12.459 10.456  1.00 46.11 ? 439  LEU A CD2   1 
ATOM   3399 N N     . LEU A 1 440 ? 26.030  -12.148 15.227  1.00 31.65 ? 440  LEU A N     1 
ATOM   3400 C CA    . LEU A 1 440 ? 26.465  -11.805 16.610  1.00 30.79 ? 440  LEU A CA    1 
ATOM   3401 C C     . LEU A 1 440 ? 26.829  -10.325 16.632  1.00 28.39 ? 440  LEU A C     1 
ATOM   3402 O O     . LEU A 1 440 ? 27.546  -9.859  15.696  1.00 27.88 ? 440  LEU A O     1 
ATOM   3403 C CB    . LEU A 1 440 ? 27.646  -12.674 17.046  1.00 33.87 ? 440  LEU A CB    1 
ATOM   3404 C CG    . LEU A 1 440 ? 27.296  -14.022 17.669  1.00 39.60 ? 440  LEU A CG    1 
ATOM   3405 C CD1   . LEU A 1 440 ? 26.144  -14.698 16.949  1.00 47.18 ? 440  LEU A CD1   1 
ATOM   3406 C CD2   . LEU A 1 440 ? 28.521  -14.916 17.660  1.00 41.48 ? 440  LEU A CD2   1 
ATOM   3407 N N     . PHE A 1 441 ? 26.379  -9.608  17.654  1.00 26.14 ? 441  PHE A N     1 
ATOM   3408 C CA    . PHE A 1 441 ? 26.639  -8.162  17.759  1.00 26.06 ? 441  PHE A CA    1 
ATOM   3409 C C     . PHE A 1 441 ? 26.782  -7.800  19.224  1.00 28.23 ? 441  PHE A C     1 
ATOM   3410 O O     . PHE A 1 441 ? 26.313  -8.569  20.105  1.00 29.04 ? 441  PHE A O     1 
ATOM   3411 C CB    . PHE A 1 441 ? 25.537  -7.374  17.062  1.00 27.28 ? 441  PHE A CB    1 
ATOM   3412 C CG    . PHE A 1 441 ? 24.173  -7.489  17.689  1.00 27.52 ? 441  PHE A CG    1 
ATOM   3413 C CD1   . PHE A 1 441 ? 23.371  -8.581  17.408  1.00 25.98 ? 441  PHE A CD1   1 
ATOM   3414 C CD2   . PHE A 1 441 ? 23.689  -6.498  18.534  1.00 27.49 ? 441  PHE A CD2   1 
ATOM   3415 C CE1   . PHE A 1 441 ? 22.107  -8.687  17.966  1.00 28.20 ? 441  PHE A CE1   1 
ATOM   3416 C CE2   . PHE A 1 441 ? 22.418  -6.606  19.075  1.00 27.89 ? 441  PHE A CE2   1 
ATOM   3417 C CZ    . PHE A 1 441 ? 21.633  -7.698  18.790  1.00 27.25 ? 441  PHE A CZ    1 
ATOM   3418 N N     . ASP A 1 442 ? 27.406  -6.655  19.453  1.00 27.68 ? 442  ASP A N     1 
ATOM   3419 C CA    . ASP A 1 442 ? 27.528  -6.051  20.803  1.00 28.19 ? 442  ASP A CA    1 
ATOM   3420 C C     . ASP A 1 442 ? 26.206  -5.351  21.129  1.00 25.46 ? 442  ASP A C     1 
ATOM   3421 O O     . ASP A 1 442 ? 25.939  -4.272  20.553  1.00 27.59 ? 442  ASP A O     1 
ATOM   3422 C CB    . ASP A 1 442 ? 28.704  -5.077  20.868  1.00 30.32 ? 442  ASP A CB    1 
ATOM   3423 C CG    . ASP A 1 442 ? 28.943  -4.515  22.251  1.00 31.70 ? 442  ASP A CG    1 
ATOM   3424 O OD1   . ASP A 1 442 ? 28.162  -4.851  23.169  1.00 30.60 ? 442  ASP A OD1   1 
ATOM   3425 O OD2   . ASP A 1 442 ? 29.934  -3.768  22.402  1.00 40.32 ? 442  ASP A OD2   1 
ATOM   3426 N N     . THR A 1 443 ? 25.417  -5.929  22.041  1.00 27.15 ? 443  THR A N     1 
ATOM   3427 C CA    . THR A 1 443 ? 24.073  -5.412  22.407  1.00 28.70 ? 443  THR A CA    1 
ATOM   3428 C C     . THR A 1 443 ? 24.233  -4.060  23.106  1.00 28.25 ? 443  THR A C     1 
ATOM   3429 O O     . THR A 1 443 ? 23.263  -3.327  23.106  1.00 27.72 ? 443  THR A O     1 
ATOM   3430 C CB    . THR A 1 443 ? 23.306  -6.390  23.313  1.00 28.35 ? 443  THR A CB    1 
ATOM   3431 O OG1   . THR A 1 443 ? 24.111  -6.590  24.470  1.00 29.43 ? 443  THR A OG1   1 
ATOM   3432 C CG2   . THR A 1 443 ? 23.013  -7.715  22.645  1.00 30.24 ? 443  THR A CG2   1 
ATOM   3433 N N     . GLN A 1 444 ? 25.408  -3.794  23.693  1.00 29.32 ? 444  GLN A N     1 
ATOM   3434 C CA    . GLN A 1 444 ? 25.707  -2.571  24.497  1.00 35.00 ? 444  GLN A CA    1 
ATOM   3435 C C     . GLN A 1 444 ? 26.116  -1.396  23.608  1.00 35.86 ? 444  GLN A C     1 
ATOM   3436 O O     . GLN A 1 444 ? 26.318  -0.313  24.151  1.00 34.06 ? 444  GLN A O     1 
ATOM   3437 C CB    . GLN A 1 444 ? 26.808  -2.870  25.522  1.00 35.31 ? 444  GLN A CB    1 
ATOM   3438 C CG    . GLN A 1 444 ? 26.468  -4.040  26.444  1.00 39.64 ? 444  GLN A CG    1 
ATOM   3439 C CD    . GLN A 1 444 ? 25.109  -3.866  27.089  1.00 44.18 ? 444  GLN A CD    1 
ATOM   3440 O OE1   . GLN A 1 444 ? 24.882  -2.909  27.834  1.00 50.97 ? 444  GLN A OE1   1 
ATOM   3441 N NE2   . GLN A 1 444 ? 24.185  -4.775  26.801  1.00 38.75 ? 444  GLN A NE2   1 
ATOM   3442 N N     . ASP A 1 445 ? 26.188  -1.587  22.289  1.00 34.47 ? 445  ASP A N     1 
ATOM   3443 C CA    . ASP A 1 445 ? 26.769  -0.624  21.324  1.00 32.07 ? 445  ASP A CA    1 
ATOM   3444 C C     . ASP A 1 445 ? 25.675  -0.190  20.360  1.00 30.55 ? 445  ASP A C     1 
ATOM   3445 O O     . ASP A 1 445 ? 25.284  -1.024  19.533  1.00 30.94 ? 445  ASP A O     1 
ATOM   3446 C CB    . ASP A 1 445 ? 27.940  -1.308  20.618  1.00 33.85 ? 445  ASP A CB    1 
ATOM   3447 C CG    . ASP A 1 445 ? 28.718  -0.465  19.631  1.00 36.62 ? 445  ASP A CG    1 
ATOM   3448 O OD1   . ASP A 1 445 ? 28.131  0.384   18.945  1.00 37.52 ? 445  ASP A OD1   1 
ATOM   3449 O OD2   . ASP A 1 445 ? 29.919  -0.754  19.492  1.00 49.31 ? 445  ASP A OD2   1 
ATOM   3450 N N     . ALA A 1 446 ? 25.206  1.056   20.458  1.00 26.57 ? 446  ALA A N     1 
ATOM   3451 C CA    . ALA A 1 446 ? 24.082  1.588   19.658  1.00 29.35 ? 446  ALA A CA    1 
ATOM   3452 C C     . ALA A 1 446 ? 24.390  1.406   18.159  1.00 30.95 ? 446  ALA A C     1 
ATOM   3453 O O     . ALA A 1 446 ? 23.461  1.020   17.403  1.00 29.36 ? 446  ALA A O     1 
ATOM   3454 C CB    . ALA A 1 446 ? 23.808  3.027   20.000  1.00 28.89 ? 446  ALA A CB    1 
ATOM   3455 N N     . THR A 1 447 ? 25.633  1.665   17.746  1.00 29.50 ? 447  THR A N     1 
ATOM   3456 C CA    . THR A 1 447 ? 26.063  1.550   16.323  1.00 30.54 ? 447  THR A CA    1 
ATOM   3457 C C     . THR A 1 447 ? 25.971  0.077   15.886  1.00 26.54 ? 447  THR A C     1 
ATOM   3458 O O     . THR A 1 447 ? 25.445  -0.165  14.790  1.00 27.50 ? 447  THR A O     1 
ATOM   3459 C CB    . THR A 1 447 ? 27.472  2.105   16.075  1.00 29.64 ? 447  THR A CB    1 
ATOM   3460 O OG1   . THR A 1 447 ? 27.385  3.507   16.343  1.00 31.24 ? 447  THR A OG1   1 
ATOM   3461 C CG2   . THR A 1 447 ? 27.937  1.876   14.656  1.00 33.35 ? 447  THR A CG2   1 
ATOM   3462 N N     . ALA A 1 448 ? 26.456  -0.856  16.695  1.00 26.42 ? 448  ALA A N     1 
ATOM   3463 C CA    . ALA A 1 448 ? 26.404  -2.308  16.384  1.00 27.67 ? 448  ALA A CA    1 
ATOM   3464 C C     . ALA A 1 448 ? 24.934  -2.772  16.281  1.00 27.16 ? 448  ALA A C     1 
ATOM   3465 O O     . ALA A 1 448 ? 24.609  -3.486  15.321  1.00 26.16 ? 448  ALA A O     1 
ATOM   3466 C CB    . ALA A 1 448 ? 27.186  -3.105  17.385  1.00 27.61 ? 448  ALA A CB    1 
ATOM   3467 N N     . ARG A 1 449 ? 24.052  -2.339  17.190  1.00 26.66 ? 449  ARG A N     1 
ATOM   3468 C CA    . ARG A 1 449 ? 22.599  -2.665  17.093  1.00 28.13 ? 449  ARG A CA    1 
ATOM   3469 C C     . ARG A 1 449 ? 22.028  -2.121  15.774  1.00 27.56 ? 449  ARG A C     1 
ATOM   3470 O O     . ARG A 1 449 ? 21.300  -2.891  15.080  1.00 27.60 ? 449  ARG A O     1 
ATOM   3471 C CB    . ARG A 1 449 ? 21.819  -2.118  18.295  1.00 29.21 ? 449  ARG A CB    1 
ATOM   3472 C CG    . ARG A 1 449 ? 22.243  -2.726  19.622  1.00 27.76 ? 449  ARG A CG    1 
ATOM   3473 C CD    . ARG A 1 449 ? 21.239  -2.366  20.709  1.00 30.59 ? 449  ARG A CD    1 
ATOM   3474 N NE    . ARG A 1 449 ? 21.072  -0.923  20.882  1.00 32.98 ? 449  ARG A NE    1 
ATOM   3475 C CZ    . ARG A 1 449 ? 21.726  -0.177  21.769  1.00 32.71 ? 449  ARG A CZ    1 
ATOM   3476 N NH1   . ARG A 1 449 ? 22.615  -0.720  22.581  1.00 33.22 ? 449  ARG A NH1   1 
ATOM   3477 N NH2   . ARG A 1 449 ? 21.488  1.124   21.830  1.00 34.40 ? 449  ARG A NH2   1 
ATOM   3478 N N     . ASN A 1 450 ? 22.341  -0.869  15.410  1.00 26.53 ? 450  ASN A N     1 
ATOM   3479 C CA    . ASN A 1 450 ? 21.852  -0.222  14.162  1.00 26.99 ? 450  ASN A CA    1 
ATOM   3480 C C     . ASN A 1 450 ? 22.381  -0.992  12.941  1.00 26.18 ? 450  ASN A C     1 
ATOM   3481 O O     . ASN A 1 450 ? 21.625  -1.191  11.991  1.00 24.14 ? 450  ASN A O     1 
ATOM   3482 C CB    . ASN A 1 450 ? 22.258  1.255   14.075  1.00 28.42 ? 450  ASN A CB    1 
ATOM   3483 C CG    . ASN A 1 450 ? 21.545  2.112   15.102  1.00 34.15 ? 450  ASN A CG    1 
ATOM   3484 O OD1   . ASN A 1 450 ? 20.570  1.682   15.717  1.00 32.34 ? 450  ASN A OD1   1 
ATOM   3485 N ND2   . ASN A 1 450 ? 22.033  3.326   15.299  1.00 34.79 ? 450  ASN A ND2   1 
ATOM   3486 N N     . GLU A 1 451 ? 23.661  -1.356  12.955  1.00 25.07 ? 451  GLU A N     1 
ATOM   3487 C CA    . GLU A 1 451 ? 24.306  -2.125  11.859  1.00 25.50 ? 451  GLU A CA    1 
ATOM   3488 C C     . GLU A 1 451 ? 23.618  -3.485  11.703  1.00 26.47 ? 451  GLU A C     1 
ATOM   3489 O O     . GLU A 1 451 ? 23.496  -3.938  10.589  1.00 25.29 ? 451  GLU A O     1 
ATOM   3490 C CB    . GLU A 1 451 ? 25.775  -2.370  12.147  1.00 27.58 ? 451  GLU A CB    1 
ATOM   3491 C CG    . GLU A 1 451 ? 26.668  -1.189  11.893  1.00 29.54 ? 451  GLU A CG    1 
ATOM   3492 C CD    . GLU A 1 451 ? 28.070  -1.464  12.420  1.00 32.25 ? 451  GLU A CD    1 
ATOM   3493 O OE1   . GLU A 1 451 ? 28.217  -2.280  13.381  1.00 32.63 ? 451  GLU A OE1   1 
ATOM   3494 O OE2   . GLU A 1 451 ? 29.009  -0.973  11.807  1.00 35.12 ? 451  GLU A OE2   1 
ATOM   3495 N N     . THR A 1 452 ? 23.268  -4.149  12.806  1.00 25.46 ? 452  THR A N     1 
ATOM   3496 C CA    . THR A 1 452 ? 22.637  -5.488  12.785  1.00 23.72 ? 452  THR A CA    1 
ATOM   3497 C C     . THR A 1 452 ? 21.228  -5.351  12.203  1.00 23.52 ? 452  THR A C     1 
ATOM   3498 O O     . THR A 1 452 ? 20.876  -6.160  11.330  1.00 25.71 ? 452  THR A O     1 
ATOM   3499 C CB    . THR A 1 452 ? 22.683  -6.129  14.172  1.00 25.18 ? 452  THR A CB    1 
ATOM   3500 O OG1   . THR A 1 452 ? 24.050  -6.294  14.535  1.00 25.75 ? 452  THR A OG1   1 
ATOM   3501 C CG2   . THR A 1 452 ? 22.009  -7.478  14.193  1.00 25.75 ? 452  THR A CG2   1 
ATOM   3502 N N     . LEU A 1 453 ? 20.463  -4.332  12.598  1.00 22.01 ? 453  LEU A N     1 
ATOM   3503 C CA    . LEU A 1 453 ? 19.102  -4.119  12.050  1.00 23.75 ? 453  LEU A CA    1 
ATOM   3504 C C     . LEU A 1 453 ? 19.206  -3.840  10.545  1.00 26.26 ? 453  LEU A C     1 
ATOM   3505 O O     . LEU A 1 453 ? 18.440  -4.482  9.777   1.00 23.62 ? 453  LEU A O     1 
ATOM   3506 C CB    . LEU A 1 453 ? 18.387  -2.966  12.757  1.00 23.90 ? 453  LEU A CB    1 
ATOM   3507 C CG    . LEU A 1 453 ? 16.989  -2.621  12.260  1.00 23.38 ? 453  LEU A CG    1 
ATOM   3508 C CD1   . LEU A 1 453 ? 16.077  -3.851  12.265  1.00 24.54 ? 453  LEU A CD1   1 
ATOM   3509 C CD2   . LEU A 1 453 ? 16.377  -1.497  13.115  1.00 25.77 ? 453  LEU A CD2   1 
ATOM   3510 N N     . ALA A 1 454 ? 20.113  -2.944  10.140  1.00 26.71 ? 454  ALA A N     1 
ATOM   3511 C CA    . ALA A 1 454 ? 20.316  -2.576  8.717   1.00 25.58 ? 454  ALA A CA    1 
ATOM   3512 C C     . ALA A 1 454 ? 20.716  -3.825  7.936   1.00 22.76 ? 454  ALA A C     1 
ATOM   3513 O O     . ALA A 1 454 ? 20.112  -4.059  6.858   1.00 21.85 ? 454  ALA A O     1 
ATOM   3514 C CB    . ALA A 1 454 ? 21.353  -1.494  8.602   1.00 28.99 ? 454  ALA A CB    1 
ATOM   3515 N N     . LEU A 1 455 ? 21.649  -4.617  8.473   1.00 21.29 ? 455  LEU A N     1 
ATOM   3516 C CA    . LEU A 1 455 ? 22.134  -5.850  7.813   1.00 23.63 ? 455  LEU A CA    1 
ATOM   3517 C C     . LEU A 1 455 ? 20.953  -6.797  7.610   1.00 22.14 ? 455  LEU A C     1 
ATOM   3518 O O     . LEU A 1 455 ? 20.794  -7.343  6.496   1.00 21.18 ? 455  LEU A O     1 
ATOM   3519 C CB    . LEU A 1 455 ? 23.218  -6.528  8.640   1.00 23.49 ? 455  LEU A CB    1 
ATOM   3520 C CG    . LEU A 1 455 ? 23.638  -7.911  8.160   1.00 24.30 ? 455  LEU A CG    1 
ATOM   3521 C CD1   . LEU A 1 455 ? 24.175  -7.886  6.718   1.00 24.95 ? 455  LEU A CD1   1 
ATOM   3522 C CD2   . LEU A 1 455 ? 24.653  -8.524  9.103   1.00 26.56 ? 455  LEU A CD2   1 
ATOM   3523 N N     . THR A 1 456 ? 20.150  -7.011  8.652   1.00 20.84 ? 456  THR A N     1 
ATOM   3524 C CA    . THR A 1 456 ? 19.114  -8.061  8.609   1.00 20.03 ? 456  THR A CA    1 
ATOM   3525 C C     . THR A 1 456 ? 18.046  -7.649  7.605   1.00 19.51 ? 456  THR A C     1 
ATOM   3526 O O     . THR A 1 456 ? 17.603  -8.514  6.814   1.00 20.73 ? 456  THR A O     1 
ATOM   3527 C CB    . THR A 1 456 ? 18.609  -8.417  10.019  1.00 21.27 ? 456  THR A CB    1 
ATOM   3528 O OG1   . THR A 1 456 ? 19.732  -8.708  10.853  1.00 23.49 ? 456  THR A OG1   1 
ATOM   3529 C CG2   . THR A 1 456 ? 17.704  -9.623  9.990   1.00 23.12 ? 456  THR A CG2   1 
ATOM   3530 N N     . ARG A 1 457 ? 17.654  -6.380  7.571   1.00 20.89 ? 457  ARG A N     1 
ATOM   3531 C CA    . ARG A 1 457 ? 16.632  -5.881  6.622   1.00 20.88 ? 457  ARG A CA    1 
ATOM   3532 C C     . ARG A 1 457 ? 17.137  -6.117  5.194   1.00 22.02 ? 457  ARG A C     1 
ATOM   3533 O O     . ARG A 1 457 ? 16.355  -6.556  4.344   1.00 19.69 ? 457  ARG A O     1 
ATOM   3534 C CB    . ARG A 1 457 ? 16.368  -4.390  6.812   1.00 22.66 ? 457  ARG A CB    1 
ATOM   3535 C CG    . ARG A 1 457 ? 15.643  -4.041  8.110   1.00 21.58 ? 457  ARG A CG    1 
ATOM   3536 C CD    . ARG A 1 457 ? 14.723  -2.857  7.878   1.00 24.31 ? 457  ARG A CD    1 
ATOM   3537 N NE    . ARG A 1 457 ? 14.132  -2.427  9.135   1.00 26.48 ? 457  ARG A NE    1 
ATOM   3538 C CZ    . ARG A 1 457 ? 13.105  -3.038  9.723   1.00 26.42 ? 457  ARG A CZ    1 
ATOM   3539 N NH1   . ARG A 1 457 ? 12.543  -4.075  9.139   1.00 25.56 ? 457  ARG A NH1   1 
ATOM   3540 N NH2   . ARG A 1 457 ? 12.605  -2.572  10.862  1.00 26.04 ? 457  ARG A NH2   1 
ATOM   3541 N N     . LEU A 1 458 ? 18.423  -5.867  4.979   1.00 22.48 ? 458  LEU A N     1 
ATOM   3542 C CA    . LEU A 1 458 ? 19.043  -6.051  3.638   1.00 23.54 ? 458  LEU A CA    1 
ATOM   3543 C C     . LEU A 1 458 ? 19.090  -7.546  3.280   1.00 23.15 ? 458  LEU A C     1 
ATOM   3544 O O     . LEU A 1 458 ? 18.698  -7.906  2.162   1.00 22.57 ? 458  LEU A O     1 
ATOM   3545 C CB    . LEU A 1 458 ? 20.437  -5.422  3.649   1.00 22.53 ? 458  LEU A CB    1 
ATOM   3546 C CG    . LEU A 1 458 ? 21.199  -5.578  2.329   1.00 25.89 ? 458  LEU A CG    1 
ATOM   3547 C CD1   . LEU A 1 458 ? 20.403  -4.994  1.181   1.00 27.08 ? 458  LEU A CD1   1 
ATOM   3548 C CD2   . LEU A 1 458 ? 22.562  -4.940  2.432   1.00 25.84 ? 458  LEU A CD2   1 
ATOM   3549 N N     . LEU A 1 459 ? 19.485  -8.401  4.219   1.00 22.21 ? 459  LEU A N     1 
ATOM   3550 C CA    . LEU A 1 459 ? 19.523  -9.877  4.012   1.00 19.46 ? 459  LEU A CA    1 
ATOM   3551 C C     . LEU A 1 459 ? 18.136  -10.394 3.642   1.00 22.68 ? 459  LEU A C     1 
ATOM   3552 O O     . LEU A 1 459 ? 18.043  -11.266 2.755   1.00 21.52 ? 459  LEU A O     1 
ATOM   3553 C CB    . LEU A 1 459 ? 20.045  -10.561 5.274   1.00 20.55 ? 459  LEU A CB    1 
ATOM   3554 C CG    . LEU A 1 459 ? 21.530  -10.353 5.557   1.00 20.41 ? 459  LEU A CG    1 
ATOM   3555 C CD1   . LEU A 1 459 ? 21.901  -11.053 6.845   1.00 22.05 ? 459  LEU A CD1   1 
ATOM   3556 C CD2   . LEU A 1 459 ? 22.420  -10.829 4.397   1.00 21.79 ? 459  LEU A CD2   1 
ATOM   3557 N N     . ILE A 1 460 ? 17.090  -9.952  4.351   1.00 20.71 ? 460  ILE A N     1 
ATOM   3558 C CA    . ILE A 1 460 ? 15.692  -10.401 4.093   1.00 20.91 ? 460  ILE A CA    1 
ATOM   3559 C C     . ILE A 1 460 ? 15.277  -9.980  2.681   1.00 21.26 ? 460  ILE A C     1 
ATOM   3560 O O     . ILE A 1 460 ? 14.713  -10.804 1.960   1.00 21.32 ? 460  ILE A O     1 
ATOM   3561 C CB    . ILE A 1 460 ? 14.719  -9.836  5.152   1.00 21.53 ? 460  ILE A CB    1 
ATOM   3562 C CG1   . ILE A 1 460 ? 14.949  -10.475 6.521   1.00 21.94 ? 460  ILE A CG1   1 
ATOM   3563 C CG2   . ILE A 1 460 ? 13.292  -9.995  4.676   1.00 20.41 ? 460  ILE A CG2   1 
ATOM   3564 C CD1   . ILE A 1 460 ? 14.428  -9.665  7.677   1.00 22.73 ? 460  ILE A CD1   1 
ATOM   3565 N N     . ASP A 1 461 ? 15.555  -8.734  2.298   1.00 20.72 ? 461  ASP A N     1 
ATOM   3566 C CA    . ASP A 1 461 ? 15.133  -8.220  0.970   1.00 21.69 ? 461  ASP A CA    1 
ATOM   3567 C C     . ASP A 1 461 ? 15.894  -8.983  -0.120  1.00 20.29 ? 461  ASP A C     1 
ATOM   3568 O O     . ASP A 1 461 ? 15.249  -9.383  -1.114  1.00 22.19 ? 461  ASP A O     1 
ATOM   3569 C CB    . ASP A 1 461 ? 15.290  -6.705  0.869   1.00 21.43 ? 461  ASP A CB    1 
ATOM   3570 C CG    . ASP A 1 461 ? 14.158  -5.920  1.524   1.00 27.12 ? 461  ASP A CG    1 
ATOM   3571 O OD1   . ASP A 1 461 ? 13.127  -6.534  1.893   1.00 23.87 ? 461  ASP A OD1   1 
ATOM   3572 O OD2   . ASP A 1 461 ? 14.321  -4.725  1.679   1.00 27.72 ? 461  ASP A OD2   1 
ATOM   3573 N N     . GLU A 1 462 ? 17.196  -9.183  0.038   1.00 20.44 ? 462  GLU A N     1 
ATOM   3574 C CA    . GLU A 1 462 ? 17.999  -9.844  -1.032  1.00 23.82 ? 462  GLU A CA    1 
ATOM   3575 C C     . GLU A 1 462 ? 17.619  -11.327 -1.133  1.00 22.96 ? 462  GLU A C     1 
ATOM   3576 O O     . GLU A 1 462 ? 17.523  -11.821 -2.246  1.00 23.53 ? 462  GLU A O     1 
ATOM   3577 C CB    . GLU A 1 462 ? 19.500  -9.671  -0.801  1.00 26.52 ? 462  GLU A CB    1 
ATOM   3578 C CG    . GLU A 1 462 ? 19.876  -8.213  -0.889  1.00 29.45 ? 462  GLU A CG    1 
ATOM   3579 C CD    . GLU A 1 462 ? 21.340  -7.937  -1.136  1.00 28.55 ? 462  GLU A CD    1 
ATOM   3580 O OE1   . GLU A 1 462 ? 22.197  -8.593  -0.502  1.00 26.07 ? 462  GLU A OE1   1 
ATOM   3581 O OE2   . GLU A 1 462 ? 21.595  -7.013  -1.919  1.00 28.89 ? 462  GLU A OE2   1 
ATOM   3582 N N     . ALA A 1 463 ? 17.391  -11.991 -0.004  1.00 20.52 ? 463  ALA A N     1 
ATOM   3583 C CA    . ALA A 1 463 ? 16.895  -13.384 0.040   1.00 22.28 ? 463  ALA A CA    1 
ATOM   3584 C C     . ALA A 1 463 ? 15.545  -13.485 -0.666  1.00 19.34 ? 463  ALA A C     1 
ATOM   3585 O O     . ALA A 1 463 ? 15.396  -14.362 -1.519  1.00 22.41 ? 463  ALA A O     1 
ATOM   3586 C CB    . ALA A 1 463 ? 16.820  -13.849 1.475   1.00 23.45 ? 463  ALA A CB    1 
ATOM   3587 N N     . ALA A 1 464 ? 14.629  -12.555 -0.405  1.00 19.51 ? 464  ALA A N     1 
ATOM   3588 C CA    . ALA A 1 464 ? 13.249  -12.593 -0.951  1.00 20.78 ? 464  ALA A CA    1 
ATOM   3589 C C     . ALA A 1 464 ? 13.317  -12.406 -2.474  1.00 20.18 ? 464  ALA A C     1 
ATOM   3590 O O     . ALA A 1 464 ? 12.642  -13.175 -3.209  1.00 20.31 ? 464  ALA A O     1 
ATOM   3591 C CB    . ALA A 1 464 ? 12.375  -11.561 -0.308  1.00 22.74 ? 464  ALA A CB    1 
ATOM   3592 N N     . ALA A 1 465 ? 14.176  -11.509 -2.939  1.00 21.65 ? 465  ALA A N     1 
ATOM   3593 C CA    . ALA A 1 465 ? 14.367  -11.286 -4.400  1.00 21.15 ? 465  ALA A CA    1 
ATOM   3594 C C     . ALA A 1 465 ? 14.834  -12.580 -5.072  1.00 20.61 ? 465  ALA A C     1 
ATOM   3595 O O     . ALA A 1 465 ? 14.433  -12.810 -6.258  1.00 21.10 ? 465  ALA A O     1 
ATOM   3596 C CB    . ALA A 1 465 ? 15.340  -10.146 -4.638  1.00 22.05 ? 465  ALA A CB    1 
ATOM   3597 N N     . GLU A 1 466 ? 15.588  -13.446 -4.379  1.00 21.39 ? 466  GLU A N     1 
ATOM   3598 C CA    . GLU A 1 466 ? 16.071  -14.755 -4.926  1.00 23.31 ? 466  GLU A CA    1 
ATOM   3599 C C     . GLU A 1 466 ? 15.039  -15.870 -4.732  1.00 24.14 ? 466  GLU A C     1 
ATOM   3600 O O     . GLU A 1 466 ? 15.270  -17.014 -5.215  1.00 24.43 ? 466  GLU A O     1 
ATOM   3601 C CB    . GLU A 1 466 ? 17.376  -15.206 -4.275  1.00 23.74 ? 466  GLU A CB    1 
ATOM   3602 C CG    . GLU A 1 466 ? 18.555  -14.342 -4.612  1.00 26.89 ? 466  GLU A CG    1 
ATOM   3603 C CD    . GLU A 1 466 ? 18.846  -14.221 -6.103  1.00 31.30 ? 466  GLU A CD    1 
ATOM   3604 O OE1   . GLU A 1 466 ? 18.660  -15.225 -6.864  1.00 27.05 ? 466  GLU A OE1   1 
ATOM   3605 O OE2   . GLU A 1 466 ? 19.271  -13.141 -6.495  1.00 35.43 ? 466  GLU A OE2   1 
ATOM   3606 N N     . GLY A 1 467 ? 13.898  -15.570 -4.109  1.00 24.22 ? 467  GLY A N     1 
ATOM   3607 C CA    . GLY A 1 467 ? 12.842  -16.568 -3.924  1.00 22.35 ? 467  GLY A CA    1 
ATOM   3608 C C     . GLY A 1 467 ? 12.983  -17.310 -2.606  1.00 20.71 ? 467  GLY A C     1 
ATOM   3609 O O     . GLY A 1 467 ? 12.352  -18.339 -2.468  1.00 20.15 ? 467  GLY A O     1 
ATOM   3610 N N     . TYR A 1 468 ? 13.685  -16.732 -1.635  1.00 19.94 ? 468  TYR A N     1 
ATOM   3611 C CA    . TYR A 1 468 ? 13.956  -17.377 -0.316  1.00 20.43 ? 468  TYR A CA    1 
ATOM   3612 C C     . TYR A 1 468 ? 13.254  -16.561 0.770   1.00 21.77 ? 468  TYR A C     1 
ATOM   3613 O O     . TYR A 1 468 ? 13.700  -15.427 1.065   1.00 25.21 ? 468  TYR A O     1 
ATOM   3614 C CB    . TYR A 1 468 ? 15.454  -17.426 -0.018  1.00 21.79 ? 468  TYR A CB    1 
ATOM   3615 C CG    . TYR A 1 468 ? 16.334  -18.008 -1.097  1.00 21.14 ? 468  TYR A CG    1 
ATOM   3616 C CD1   . TYR A 1 468 ? 15.934  -19.107 -1.852  1.00 21.61 ? 468  TYR A CD1   1 
ATOM   3617 C CD2   . TYR A 1 468 ? 17.594  -17.484 -1.334  1.00 24.33 ? 468  TYR A CD2   1 
ATOM   3618 C CE1   . TYR A 1 468 ? 16.769  -19.647 -2.821  1.00 24.56 ? 468  TYR A CE1   1 
ATOM   3619 C CE2   . TYR A 1 468 ? 18.428  -18.008 -2.310  1.00 22.36 ? 468  TYR A CE2   1 
ATOM   3620 C CZ    . TYR A 1 468 ? 18.022  -19.115 -3.035  1.00 24.25 ? 468  TYR A CZ    1 
ATOM   3621 O OH    . TYR A 1 468 ? 18.861  -19.664 -3.971  1.00 23.71 ? 468  TYR A OH    1 
ATOM   3622 N N     . GLY A 1 469 ? 12.155  -17.082 1.305   1.00 20.27 ? 469  GLY A N     1 
ATOM   3623 C CA    . GLY A 1 469 ? 11.386  -16.366 2.329   1.00 19.70 ? 469  GLY A CA    1 
ATOM   3624 C C     . GLY A 1 469 ? 11.869  -16.726 3.722   1.00 20.53 ? 469  GLY A C     1 
ATOM   3625 O O     . GLY A 1 469 ? 12.279  -17.879 3.964   1.00 19.75 ? 469  GLY A O     1 
ATOM   3626 N N     . GLU A 1 470 ? 11.782  -15.756 4.622   1.00 22.34 ? 470  GLU A N     1 
ATOM   3627 C CA    . GLU A 1 470 ? 12.098  -15.956 6.043   1.00 21.57 ? 470  GLU A CA    1 
ATOM   3628 C C     . GLU A 1 470 ? 10.946  -16.736 6.698   1.00 21.51 ? 470  GLU A C     1 
ATOM   3629 O O     . GLU A 1 470 ? 9.770   -16.477 6.389   1.00 20.82 ? 470  GLU A O     1 
ATOM   3630 C CB    . GLU A 1 470 ? 12.324  -14.596 6.691   1.00 22.17 ? 470  GLU A CB    1 
ATOM   3631 C CG    . GLU A 1 470 ? 12.552  -14.691 8.171   1.00 26.64 ? 470  GLU A CG    1 
ATOM   3632 C CD    . GLU A 1 470 ? 13.733  -15.569 8.566   1.00 28.17 ? 470  GLU A CD    1 
ATOM   3633 O OE1   . GLU A 1 470 ? 14.834  -15.002 8.776   1.00 30.68 ? 470  GLU A OE1   1 
ATOM   3634 O OE2   . GLU A 1 470 ? 13.548  -16.809 8.693   1.00 27.49 ? 470  GLU A OE2   1 
ATOM   3635 N N     . TYR A 1 471 ? 11.294  -17.629 7.612   1.00 21.43 ? 471  TYR A N     1 
ATOM   3636 C CA    . TYR A 1 471 ? 10.392  -18.610 8.257   1.00 25.68 ? 471  TYR A CA    1 
ATOM   3637 C C     . TYR A 1 471 ? 9.936   -18.077 9.620   1.00 22.19 ? 471  TYR A C     1 
ATOM   3638 O O     . TYR A 1 471 ? 8.846   -18.429 10.122  1.00 21.53 ? 471  TYR A O     1 
ATOM   3639 C CB    . TYR A 1 471 ? 11.155  -19.918 8.437   1.00 32.05 ? 471  TYR A CB    1 
ATOM   3640 C CG    . TYR A 1 471 ? 10.300  -21.013 8.993   1.00 43.51 ? 471  TYR A CG    1 
ATOM   3641 C CD1   . TYR A 1 471 ? 9.221   -21.488 8.267   1.00 57.57 ? 471  TYR A CD1   1 
ATOM   3642 C CD2   . TYR A 1 471 ? 10.504  -21.500 10.276  1.00 50.79 ? 471  TYR A CD2   1 
ATOM   3643 C CE1   . TYR A 1 471 ? 8.383   -22.466 8.782   1.00 66.35 ? 471  TYR A CE1   1 
ATOM   3644 C CE2   . TYR A 1 471 ? 9.681   -22.481 10.801  1.00 64.86 ? 471  TYR A CE2   1 
ATOM   3645 C CZ    . TYR A 1 471 ? 8.614   -22.966 10.055  1.00 73.35 ? 471  TYR A CZ    1 
ATOM   3646 O OH    . TYR A 1 471 ? 7.781   -23.917 10.579  1.00 76.74 ? 471  TYR A OH    1 
ATOM   3647 N N     . ARG A 1 472 ? 10.796  -17.288 10.239  1.00 20.23 ? 472  ARG A N     1 
ATOM   3648 C CA    . ARG A 1 472 ? 10.581  -16.806 11.624  1.00 21.22 ? 472  ARG A CA    1 
ATOM   3649 C C     . ARG A 1 472 ? 11.406  -15.547 11.811  1.00 21.46 ? 472  ARG A C     1 
ATOM   3650 O O     . ARG A 1 472 ? 12.506  -15.488 11.244  1.00 21.68 ? 472  ARG A O     1 
ATOM   3651 C CB    . ARG A 1 472 ? 11.002  -17.933 12.561  1.00 20.90 ? 472  ARG A CB    1 
ATOM   3652 C CG    . ARG A 1 472 ? 10.647  -17.726 14.025  1.00 19.79 ? 472  ARG A CG    1 
ATOM   3653 C CD    . ARG A 1 472 ? 11.006  -19.048 14.714  1.00 19.18 ? 472  ARG A CD    1 
ATOM   3654 N NE    . ARG A 1 472 ? 10.839  -18.931 16.159  1.00 19.52 ? 472  ARG A NE    1 
ATOM   3655 C CZ    . ARG A 1 472 ? 11.356  -19.814 17.002  1.00 20.64 ? 472  ARG A CZ    1 
ATOM   3656 N NH1   . ARG A 1 472 ? 12.045  -20.837 16.535  1.00 21.62 ? 472  ARG A NH1   1 
ATOM   3657 N NH2   . ARG A 1 472 ? 11.209  -19.658 18.303  1.00 22.50 ? 472  ARG A NH2   1 
ATOM   3658 N N     . THR A 1 473 ? 10.897  -14.541 12.503  1.00 18.74 ? 473  THR A N     1 
ATOM   3659 C CA    . THR A 1 473 ? 11.696  -13.303 12.635  1.00 20.15 ? 473  THR A CA    1 
ATOM   3660 C C     . THR A 1 473 ? 11.455  -12.598 13.967  1.00 21.39 ? 473  THR A C     1 
ATOM   3661 O O     . THR A 1 473 ? 10.550  -12.979 14.722  1.00 21.20 ? 473  THR A O     1 
ATOM   3662 C CB    . THR A 1 473 ? 11.481  -12.376 11.434  1.00 20.42 ? 473  THR A CB    1 
ATOM   3663 O OG1   . THR A 1 473 ? 12.671  -11.581 11.391  1.00 21.08 ? 473  THR A OG1   1 
ATOM   3664 C CG2   . THR A 1 473 ? 10.197  -11.576 11.503  1.00 20.71 ? 473  THR A CG2   1 
ATOM   3665 N N     . HIS A 1 474 ? 12.299  -11.611 14.212  1.00 21.34 ? 474  HIS A N     1 
ATOM   3666 C CA    . HIS A 1 474 ? 12.255  -10.704 15.384  1.00 21.97 ? 474  HIS A CA    1 
ATOM   3667 C C     . HIS A 1 474 ? 11.092  -9.710  15.251  1.00 20.92 ? 474  HIS A C     1 
ATOM   3668 O O     . HIS A 1 474 ? 10.733  -9.301  14.130  1.00 20.95 ? 474  HIS A O     1 
ATOM   3669 C CB    . HIS A 1 474 ? 13.620  -10.045 15.489  1.00 21.36 ? 474  HIS A CB    1 
ATOM   3670 C CG    . HIS A 1 474 ? 13.883  -9.315  16.756  1.00 20.79 ? 474  HIS A CG    1 
ATOM   3671 N ND1   . HIS A 1 474 ? 13.357  -8.073  16.988  1.00 23.20 ? 474  HIS A ND1   1 
ATOM   3672 C CD2   . HIS A 1 474 ? 14.713  -9.615  17.783  1.00 21.59 ? 474  HIS A CD2   1 
ATOM   3673 C CE1   . HIS A 1 474 ? 13.787  -7.646  18.171  1.00 24.27 ? 474  HIS A CE1   1 
ATOM   3674 N NE2   . HIS A 1 474 ? 14.644  -8.568  18.680  1.00 21.75 ? 474  HIS A NE2   1 
ATOM   3675 N N     . ASN A 1 475 ? 10.532  -9.303  16.394  1.00 20.93 ? 475  ASN A N     1 
ATOM   3676 C CA    . ASN A 1 475 ? 9.588   -8.167  16.510  1.00 19.27 ? 475  ASN A CA    1 
ATOM   3677 C C     . ASN A 1 475 ? 9.919   -7.049  15.485  1.00 20.54 ? 475  ASN A C     1 
ATOM   3678 O O     . ASN A 1 475 ? 8.998   -6.556  14.809  1.00 21.21 ? 475  ASN A O     1 
ATOM   3679 C CB    . ASN A 1 475 ? 9.657   -7.549  17.916  1.00 19.36 ? 475  ASN A CB    1 
ATOM   3680 C CG    . ASN A 1 475 ? 8.920   -8.388  18.949  1.00 19.13 ? 475  ASN A CG    1 
ATOM   3681 O OD1   . ASN A 1 475 ? 8.002   -9.079  18.592  1.00 20.32 ? 475  ASN A OD1   1 
ATOM   3682 N ND2   . ASN A 1 475 ? 9.283   -8.294  20.225  1.00 20.80 ? 475  ASN A ND2   1 
ATOM   3683 N N     . ALA A 1 476 ? 11.188  -6.622  15.421  1.00 21.18 ? 476  ALA A N     1 
ATOM   3684 C CA    . ALA A 1 476 ? 11.611  -5.403  14.688  1.00 20.82 ? 476  ALA A CA    1 
ATOM   3685 C C     . ALA A 1 476 ? 11.465  -5.636  13.179  1.00 22.55 ? 476  ALA A C     1 
ATOM   3686 O O     . ALA A 1 476 ? 11.350  -4.647  12.455  1.00 25.47 ? 476  ALA A O     1 
ATOM   3687 C CB    . ALA A 1 476 ? 13.032  -5.046  15.068  1.00 20.81 ? 476  ALA A CB    1 
ATOM   3688 N N     . LEU A 1 477 ? 11.374  -6.905  12.759  1.00 21.77 ? 477  LEU A N     1 
ATOM   3689 C CA    . LEU A 1 477 ? 11.407  -7.301  11.322  1.00 21.87 ? 477  LEU A CA    1 
ATOM   3690 C C     . LEU A 1 477 ? 10.066  -7.877  10.861  1.00 21.99 ? 477  LEU A C     1 
ATOM   3691 O O     . LEU A 1 477 ? 9.932   -8.187  9.656   1.00 20.40 ? 477  LEU A O     1 
ATOM   3692 C CB    . LEU A 1 477 ? 12.519  -8.331  11.181  1.00 21.67 ? 477  LEU A CB    1 
ATOM   3693 C CG    . LEU A 1 477 ? 13.908  -7.818  11.563  1.00 24.53 ? 477  LEU A CG    1 
ATOM   3694 C CD1   . LEU A 1 477 ? 14.876  -8.961  11.740  1.00 25.12 ? 477  LEU A CD1   1 
ATOM   3695 C CD2   . LEU A 1 477 ? 14.425  -6.841  10.515  1.00 24.34 ? 477  LEU A CD2   1 
ATOM   3696 N N     . MET A 1 478 ? 9.075   -7.994  11.746  1.00 20.37 ? 478  MET A N     1 
ATOM   3697 C CA    . MET A 1 478 ? 7.820   -8.711  11.436  1.00 20.16 ? 478  MET A CA    1 
ATOM   3698 C C     . MET A 1 478 ? 7.060   -8.018  10.319  1.00 20.12 ? 478  MET A C     1 
ATOM   3699 O O     . MET A 1 478 ? 6.571   -8.746  9.392   1.00 17.97 ? 478  MET A O     1 
ATOM   3700 C CB    . MET A 1 478 ? 6.941   -8.871  12.683  1.00 19.12 ? 478  MET A CB    1 
ATOM   3701 C CG    . MET A 1 478 ? 7.510   -9.869  13.617  1.00 19.65 ? 478  MET A CG    1 
ATOM   3702 S SD    . MET A 1 478 ? 6.533   -9.967  15.119  1.00 20.71 ? 478  MET A SD    1 
ATOM   3703 C CE    . MET A 1 478 ? 7.451   -11.236 15.991  1.00 21.59 ? 478  MET A CE    1 
ATOM   3704 N N     . ASP A 1 479 ? 7.008   -6.683  10.327  1.00 18.88 ? 479  ASP A N     1 
ATOM   3705 C CA    . ASP A 1 479 ? 6.262   -5.934  9.290   1.00 19.17 ? 479  ASP A CA    1 
ATOM   3706 C C     . ASP A 1 479 ? 6.968   -6.171  7.961   1.00 18.76 ? 479  ASP A C     1 
ATOM   3707 O O     . ASP A 1 479 ? 6.277   -6.434  6.982   1.00 17.75 ? 479  ASP A O     1 
ATOM   3708 C CB    . ASP A 1 479 ? 6.150   -4.447  9.583   1.00 20.47 ? 479  ASP A CB    1 
ATOM   3709 C CG    . ASP A 1 479 ? 5.181   -4.157  10.718  1.00 22.50 ? 479  ASP A CG    1 
ATOM   3710 O OD1   . ASP A 1 479 ? 4.163   -4.905  10.819  1.00 23.97 ? 479  ASP A OD1   1 
ATOM   3711 O OD2   . ASP A 1 479 ? 5.468   -3.242  11.460  1.00 25.15 ? 479  ASP A OD2   1 
ATOM   3712 N N     . GLN A 1 480 ? 8.282   -6.072  7.964   1.00 21.03 ? 480  GLN A N     1 
ATOM   3713 C CA    . GLN A 1 480 ? 9.056   -6.251  6.700   1.00 22.47 ? 480  GLN A CA    1 
ATOM   3714 C C     . GLN A 1 480 ? 8.832   -7.674  6.175   1.00 23.69 ? 480  GLN A C     1 
ATOM   3715 O O     . GLN A 1 480 ? 8.542   -7.815  4.980   1.00 22.29 ? 480  GLN A O     1 
ATOM   3716 C CB    . GLN A 1 480 ? 10.542  -6.035  6.905   1.00 21.48 ? 480  GLN A CB    1 
ATOM   3717 C CG    . GLN A 1 480 ? 11.320  -6.161  5.599   1.00 21.84 ? 480  GLN A CG    1 
ATOM   3718 C CD    . GLN A 1 480 ? 12.807  -6.034  5.751   1.00 22.96 ? 480  GLN A CD    1 
ATOM   3719 O OE1   . GLN A 1 480 ? 13.308  -5.654  6.808   1.00 24.38 ? 480  GLN A OE1   1 
ATOM   3720 N NE2   . GLN A 1 480 ? 13.527  -6.329  4.669   1.00 20.01 ? 480  GLN A NE2   1 
ATOM   3721 N N     . VAL A 1 481 ? 8.998   -8.696  7.025   1.00 21.19 ? 481  VAL A N     1 
ATOM   3722 C CA    . VAL A 1 481 ? 8.911   -10.110 6.563   1.00 20.03 ? 481  VAL A CA    1 
ATOM   3723 C C     . VAL A 1 481 ? 7.502   -10.383 6.038   1.00 20.68 ? 481  VAL A C     1 
ATOM   3724 O O     . VAL A 1 481 ? 7.394   -10.945 4.907   1.00 20.48 ? 481  VAL A O     1 
ATOM   3725 C CB    . VAL A 1 481 ? 9.360   -11.106 7.644   1.00 19.19 ? 481  VAL A CB    1 
ATOM   3726 C CG1   . VAL A 1 481 ? 9.050   -12.533 7.231   1.00 17.78 ? 481  VAL A CG1   1 
ATOM   3727 C CG2   . VAL A 1 481 ? 10.840  -10.965 7.937   1.00 18.88 ? 481  VAL A CG2   1 
ATOM   3728 N N     . MET A 1 482 ? 6.440   -9.982  6.757   1.00 19.57 ? 482  MET A N     1 
ATOM   3729 C CA    . MET A 1 482 ? 5.079   -10.213 6.227   1.00 19.77 ? 482  MET A CA    1 
ATOM   3730 C C     . MET A 1 482 ? 4.933   -9.470  4.893   1.00 18.85 ? 482  MET A C     1 
ATOM   3731 O O     . MET A 1 482 ? 4.270   -10.008 4.002   1.00 21.77 ? 482  MET A O     1 
ATOM   3732 C CB    . MET A 1 482 ? 3.984   -9.759  7.189   1.00 21.49 ? 482  MET A CB    1 
ATOM   3733 C CG    . MET A 1 482 ? 2.587   -10.049 6.682   1.00 23.94 ? 482  MET A CG    1 
ATOM   3734 S SD    . MET A 1 482 ? 2.302   -11.774 6.139   1.00 24.59 ? 482  MET A SD    1 
ATOM   3735 C CE    . MET A 1 482 ? 1.784   -12.521 7.695   1.00 26.94 ? 482  MET A CE    1 
ATOM   3736 N N     . GLY A 1 483 ? 5.575   -8.309  4.774   1.00 18.87 ? 483  GLY A N     1 
ATOM   3737 C CA    . GLY A 1 483 ? 5.546   -7.469  3.558   1.00 19.64 ? 483  GLY A CA    1 
ATOM   3738 C C     . GLY A 1 483 ? 6.165   -8.175  2.371   1.00 20.73 ? 483  GLY A C     1 
ATOM   3739 O O     . GLY A 1 483 ? 5.824   -7.785  1.235   1.00 22.07 ? 483  GLY A O     1 
ATOM   3740 N N     . THR A 1 484 ? 7.050   -9.155  2.587   1.00 18.65 ? 484  THR A N     1 
ATOM   3741 C CA    . THR A 1 484 ? 7.668   -9.914  1.452   1.00 19.61 ? 484  THR A CA    1 
ATOM   3742 C C     . THR A 1 484 ? 6.677   -10.935 0.911   1.00 21.52 ? 484  THR A C     1 
ATOM   3743 O O     . THR A 1 484 ? 6.847   -11.318 -0.246  1.00 21.77 ? 484  THR A O     1 
ATOM   3744 C CB    . THR A 1 484 ? 8.993   -10.590 1.798   1.00 19.11 ? 484  THR A CB    1 
ATOM   3745 O OG1   . THR A 1 484 ? 8.764   -11.646 2.736   1.00 19.97 ? 484  THR A OG1   1 
ATOM   3746 C CG2   . THR A 1 484 ? 10.028  -9.604  2.284   1.00 19.26 ? 484  THR A CG2   1 
ATOM   3747 N N     . TYR A 1 485 ? 5.705   -11.393 1.719   1.00 19.80 ? 485  TYR A N     1 
ATOM   3748 C CA    . TYR A 1 485 ? 4.704   -12.415 1.326   1.00 18.50 ? 485  TYR A CA    1 
ATOM   3749 C C     . TYR A 1 485 ? 3.463   -11.733 0.734   1.00 21.12 ? 485  TYR A C     1 
ATOM   3750 O O     . TYR A 1 485 ? 2.309   -12.032 1.151   1.00 18.01 ? 485  TYR A O     1 
ATOM   3751 C CB    . TYR A 1 485 ? 4.403   -13.322 2.531   1.00 18.79 ? 485  TYR A CB    1 
ATOM   3752 C CG    . TYR A 1 485 ? 5.538   -14.223 2.947   1.00 18.19 ? 485  TYR A CG    1 
ATOM   3753 C CD1   . TYR A 1 485 ? 5.732   -15.459 2.344   1.00 20.40 ? 485  TYR A CD1   1 
ATOM   3754 C CD2   . TYR A 1 485 ? 6.415   -13.865 3.951   1.00 20.21 ? 485  TYR A CD2   1 
ATOM   3755 C CE1   . TYR A 1 485 ? 6.775   -16.299 2.708   1.00 21.24 ? 485  TYR A CE1   1 
ATOM   3756 C CE2   . TYR A 1 485 ? 7.448   -14.697 4.351   1.00 19.81 ? 485  TYR A CE2   1 
ATOM   3757 C CZ    . TYR A 1 485 ? 7.653   -15.902 3.707   1.00 18.99 ? 485  TYR A CZ    1 
ATOM   3758 O OH    . TYR A 1 485 ? 8.645   -16.745 4.079   1.00 18.52 ? 485  TYR A OH    1 
ATOM   3759 N N     . ASN A 1 486 ? 3.665   -10.847 -0.246  1.00 18.53 ? 486  ASN A N     1 
ATOM   3760 C CA    . ASN A 1 486 ? 2.605   -9.946  -0.746  1.00 21.26 ? 486  ASN A CA    1 
ATOM   3761 C C     . ASN A 1 486 ? 2.090   -10.348 -2.120  1.00 20.24 ? 486  ASN A C     1 
ATOM   3762 O O     . ASN A 1 486 ? 1.552   -9.449  -2.801  1.00 20.62 ? 486  ASN A O     1 
ATOM   3763 C CB    . ASN A 1 486 ? 3.067   -8.489  -0.731  1.00 22.77 ? 486  ASN A CB    1 
ATOM   3764 C CG    . ASN A 1 486 ? 4.245   -8.201  -1.639  1.00 25.66 ? 486  ASN A CG    1 
ATOM   3765 O OD1   . ASN A 1 486 ? 4.892   -9.100  -2.136  1.00 26.35 ? 486  ASN A OD1   1 
ATOM   3766 N ND2   . ASN A 1 486 ? 4.570   -6.927  -1.812  1.00 27.79 ? 486  ASN A ND2   1 
ATOM   3767 N N     . TRP A 1 487 ? 2.139   -11.620 -2.495  1.00 21.41 ? 487  TRP A N     1 
ATOM   3768 C CA    . TRP A 1 487 ? 1.428   -12.125 -3.702  1.00 22.76 ? 487  TRP A CA    1 
ATOM   3769 C C     . TRP A 1 487 ? -0.034  -11.646 -3.670  1.00 24.08 ? 487  TRP A C     1 
ATOM   3770 O O     . TRP A 1 487 ? -0.653  -11.586 -2.589  1.00 19.73 ? 487  TRP A O     1 
ATOM   3771 C CB    . TRP A 1 487 ? 1.533   -13.653 -3.762  1.00 22.85 ? 487  TRP A CB    1 
ATOM   3772 C CG    . TRP A 1 487 ? 1.070   -14.293 -5.034  1.00 20.59 ? 487  TRP A CG    1 
ATOM   3773 C CD1   . TRP A 1 487 ? 1.870   -14.697 -6.072  1.00 21.86 ? 487  TRP A CD1   1 
ATOM   3774 C CD2   . TRP A 1 487 ? -0.273  -14.666 -5.394  1.00 22.93 ? 487  TRP A CD2   1 
ATOM   3775 N NE1   . TRP A 1 487 ? 1.111   -15.302 -7.040  1.00 20.88 ? 487  TRP A NE1   1 
ATOM   3776 C CE2   . TRP A 1 487 ? -0.204  -15.274 -6.666  1.00 21.26 ? 487  TRP A CE2   1 
ATOM   3777 C CE3   . TRP A 1 487 ? -1.522  -14.554 -4.772  1.00 23.25 ? 487  TRP A CE3   1 
ATOM   3778 C CZ2   . TRP A 1 487 ? -1.340  -15.747 -7.327  1.00 22.56 ? 487  TRP A CZ2   1 
ATOM   3779 C CZ3   . TRP A 1 487 ? -2.645  -15.024 -5.421  1.00 23.17 ? 487  TRP A CZ3   1 
ATOM   3780 C CH2   . TRP A 1 487 ? -2.549  -15.619 -6.685  1.00 24.10 ? 487  TRP A CH2   1 
ATOM   3781 N N     . GLY A 1 488 ? -0.622  -11.364 -4.827  1.00 21.83 ? 488  GLY A N     1 
ATOM   3782 C CA    . GLY A 1 488 ? -2.023  -10.936 -4.948  1.00 23.93 ? 488  GLY A CA    1 
ATOM   3783 C C     . GLY A 1 488 ? -2.261  -9.619  -4.233  1.00 22.76 ? 488  GLY A C     1 
ATOM   3784 O O     . GLY A 1 488 ? -3.303  -9.472  -3.576  1.00 27.67 ? 488  GLY A O     1 
ATOM   3785 N N     . ASP A 1 489 ? -1.332  -8.689  -4.344  1.00 22.61 ? 489  ASP A N     1 
ATOM   3786 C CA    . ASP A 1 489 ? -1.436  -7.318  -3.796  1.00 25.72 ? 489  ASP A CA    1 
ATOM   3787 C C     . ASP A 1 489 ? -1.688  -7.442  -2.280  1.00 24.67 ? 489  ASP A C     1 
ATOM   3788 O O     . ASP A 1 489 ? -2.626  -6.800  -1.763  1.00 26.29 ? 489  ASP A O     1 
ATOM   3789 C CB    . ASP A 1 489 ? -2.486  -6.531  -4.592  1.00 30.65 ? 489  ASP A CB    1 
ATOM   3790 C CG    . ASP A 1 489 ? -2.183  -6.302  -6.094  1.00 44.80 ? 489  ASP A CG    1 
ATOM   3791 O OD1   . ASP A 1 489 ? -0.981  -6.049  -6.529  1.00 41.22 ? 489  ASP A OD1   1 
ATOM   3792 O OD2   . ASP A 1 489 ? -3.161  -6.389  -6.869  1.00 55.73 ? 489  ASP A OD2   1 
ATOM   3793 N N     . GLY A 1 490 ? -0.882  -8.252  -1.594  1.00 23.21 ? 490  GLY A N     1 
ATOM   3794 C CA    . GLY A 1 490 ? -0.939  -8.455  -0.126  1.00 21.97 ? 490  GLY A CA    1 
ATOM   3795 C C     . GLY A 1 490 ? -2.131  -9.304  0.311   1.00 23.12 ? 490  GLY A C     1 
ATOM   3796 O O     . GLY A 1 490 ? -2.690  -9.031  1.355   1.00 22.12 ? 490  GLY A O     1 
ATOM   3797 N N     . ALA A 1 491 ? -2.537  -10.301 -0.475  1.00 21.79 ? 491  ALA A N     1 
ATOM   3798 C CA    . ALA A 1 491 ? -3.728  -11.128 -0.227  1.00 22.96 ? 491  ALA A CA    1 
ATOM   3799 C C     . ALA A 1 491 ? -3.573  -11.881 1.092   1.00 23.22 ? 491  ALA A C     1 
ATOM   3800 O O     . ALA A 1 491 ? -4.587  -11.992 1.815   1.00 23.12 ? 491  ALA A O     1 
ATOM   3801 C CB    . ALA A 1 491 ? -3.964  -12.123 -1.332  1.00 24.96 ? 491  ALA A CB    1 
ATOM   3802 N N     . LEU A 1 492 ? -2.384  -12.377 1.412   1.00 20.24 ? 492  LEU A N     1 
ATOM   3803 C CA    . LEU A 1 492 ? -2.197  -13.208 2.629   1.00 22.55 ? 492  LEU A CA    1 
ATOM   3804 C C     . LEU A 1 492 ? -2.461  -12.317 3.855   1.00 22.11 ? 492  LEU A C     1 
ATOM   3805 O O     . LEU A 1 492 ? -3.237  -12.728 4.732   1.00 21.52 ? 492  LEU A O     1 
ATOM   3806 C CB    . LEU A 1 492 ? -0.794  -13.800 2.696   1.00 22.96 ? 492  LEU A CB    1 
ATOM   3807 C CG    . LEU A 1 492 ? -0.558  -14.716 3.899   1.00 23.21 ? 492  LEU A CG    1 
ATOM   3808 C CD1   . LEU A 1 492 ? -1.410  -15.980 3.822   1.00 25.23 ? 492  LEU A CD1   1 
ATOM   3809 C CD2   . LEU A 1 492 ? 0.900   -15.060 4.059   1.00 25.39 ? 492  LEU A CD2   1 
ATOM   3810 N N     . LEU A 1 493 ? -1.880  -11.132 3.886   1.00 22.39 ? 493  LEU A N     1 
ATOM   3811 C CA    . LEU A 1 493 ? -2.048  -10.229 5.057   1.00 21.96 ? 493  LEU A CA    1 
ATOM   3812 C C     . LEU A 1 493 ? -3.507  -9.740  5.138   1.00 24.76 ? 493  LEU A C     1 
ATOM   3813 O O     . LEU A 1 493 ? -4.034  -9.638  6.261   1.00 23.33 ? 493  LEU A O     1 
ATOM   3814 C CB    . LEU A 1 493 ? -1.040  -9.087  4.975   1.00 21.64 ? 493  LEU A CB    1 
ATOM   3815 C CG    . LEU A 1 493 ? -1.155  -8.091  6.124   1.00 20.81 ? 493  LEU A CG    1 
ATOM   3816 C CD1   . LEU A 1 493 ? -1.054  -8.836  7.448   1.00 21.03 ? 493  LEU A CD1   1 
ATOM   3817 C CD2   . LEU A 1 493 ? -0.094  -7.032  6.021   1.00 21.26 ? 493  LEU A CD2   1 
ATOM   3818 N N     . LYS A 1 494 ? -4.178  -9.467  4.011   1.00 24.21 ? 494  LYS A N     1 
ATOM   3819 C CA    . LYS A 1 494 ? -5.594  -9.026  4.038   1.00 27.78 ? 494  LYS A CA    1 
ATOM   3820 C C     . LYS A 1 494 ? -6.468  -10.131 4.643   1.00 26.68 ? 494  LYS A C     1 
ATOM   3821 O O     . LYS A 1 494 ? -7.426  -9.801  5.376   1.00 29.15 ? 494  LYS A O     1 
ATOM   3822 C CB    . LYS A 1 494 ? -6.094  -8.630  2.645   1.00 28.75 ? 494  LYS A CB    1 
ATOM   3823 C CG    . LYS A 1 494 ? -5.528  -7.298  2.173   1.00 33.25 ? 494  LYS A CG    1 
ATOM   3824 C CD    . LYS A 1 494 ? -5.898  -6.911  0.752   1.00 35.71 ? 494  LYS A CD    1 
ATOM   3825 C CE    . LYS A 1 494 ? -5.074  -5.735  0.263   1.00 34.64 ? 494  LYS A CE    1 
ATOM   3826 N NZ    . LYS A 1 494 ? -5.109  -5.651  -1.216  1.00 34.85 ? 494  LYS A NZ    1 
ATOM   3827 N N     . PHE A 1 495 ? -6.206  -11.387 4.299   1.00 23.46 ? 495  PHE A N     1 
ATOM   3828 C CA    . PHE A 1 495 ? -6.906  -12.566 4.878   1.00 23.05 ? 495  PHE A CA    1 
ATOM   3829 C C     . PHE A 1 495 ? -6.670  -12.581 6.392   1.00 22.67 ? 495  PHE A C     1 
ATOM   3830 O O     . PHE A 1 495 ? -7.672  -12.724 7.148   1.00 21.08 ? 495  PHE A O     1 
ATOM   3831 C CB    . PHE A 1 495 ? -6.416  -13.834 4.175   1.00 22.03 ? 495  PHE A CB    1 
ATOM   3832 C CG    . PHE A 1 495 ? -6.744  -15.136 4.846   1.00 22.13 ? 495  PHE A CG    1 
ATOM   3833 C CD1   . PHE A 1 495 ? -7.954  -15.763 4.605   1.00 21.21 ? 495  PHE A CD1   1 
ATOM   3834 C CD2   . PHE A 1 495 ? -5.797  -15.777 5.642   1.00 21.93 ? 495  PHE A CD2   1 
ATOM   3835 C CE1   . PHE A 1 495 ? -8.223  -16.998 5.162   1.00 23.33 ? 495  PHE A CE1   1 
ATOM   3836 C CE2   . PHE A 1 495 ? -6.088  -16.996 6.232   1.00 21.54 ? 495  PHE A CE2   1 
ATOM   3837 C CZ    . PHE A 1 495 ? -7.279  -17.627 5.959   1.00 22.86 ? 495  PHE A CZ    1 
ATOM   3838 N N     . HIS A 1 496 ? -5.406  -12.477 6.822   1.00 23.18 ? 496  HIS A N     1 
ATOM   3839 C CA    . HIS A 1 496 ? -5.042  -12.496 8.263   1.00 22.80 ? 496  HIS A CA    1 
ATOM   3840 C C     . HIS A 1 496 ? -5.769  -11.355 8.966   1.00 22.76 ? 496  HIS A C     1 
ATOM   3841 O O     . HIS A 1 496 ? -6.273  -11.578 10.087  1.00 20.49 ? 496  HIS A O     1 
ATOM   3842 C CB    . HIS A 1 496 ? -3.532  -12.458 8.487   1.00 21.68 ? 496  HIS A CB    1 
ATOM   3843 C CG    . HIS A 1 496 ? -2.863  -13.744 8.179   1.00 23.25 ? 496  HIS A CG    1 
ATOM   3844 N ND1   . HIS A 1 496 ? -3.387  -14.964 8.563   1.00 25.22 ? 496  HIS A ND1   1 
ATOM   3845 C CD2   . HIS A 1 496 ? -1.746  -14.017 7.467   1.00 24.13 ? 496  HIS A CD2   1 
ATOM   3846 C CE1   . HIS A 1 496 ? -2.592  -15.927 8.130   1.00 27.85 ? 496  HIS A CE1   1 
ATOM   3847 N NE2   . HIS A 1 496 ? -1.578  -15.380 7.461   1.00 23.36 ? 496  HIS A NE2   1 
ATOM   3848 N N     . GLU A 1 497 ? -5.827  -10.175 8.351   1.00 22.07 ? 497  GLU A N     1 
ATOM   3849 C CA    . GLU A 1 497 ? -6.485  -8.994  8.958   1.00 23.77 ? 497  GLU A CA    1 
ATOM   3850 C C     . GLU A 1 497 ? -7.986  -9.253  9.075   1.00 22.06 ? 497  GLU A C     1 
ATOM   3851 O O     . GLU A 1 497 ? -8.552  -8.911  10.128  1.00 23.83 ? 497  GLU A O     1 
ATOM   3852 C CB    . GLU A 1 497 ? -6.217  -7.730  8.141   1.00 22.90 ? 497  GLU A CB    1 
ATOM   3853 C CG    . GLU A 1 497 ? -4.788  -7.226  8.277   1.00 22.90 ? 497  GLU A CG    1 
ATOM   3854 C CD    . GLU A 1 497 ? -4.419  -6.175  7.240   1.00 24.48 ? 497  GLU A CD    1 
ATOM   3855 O OE1   . GLU A 1 497 ? -5.255  -5.918  6.345   1.00 29.42 ? 497  GLU A OE1   1 
ATOM   3856 O OE2   . GLU A 1 497 ? -3.324  -5.628  7.333   1.00 29.23 ? 497  GLU A OE2   1 
ATOM   3857 N N     . ALA A 1 498 ? -8.626  -9.797  8.056   1.00 20.94 ? 498  ALA A N     1 
ATOM   3858 C CA    . ALA A 1 498 ? -10.074 -10.108 8.077   1.00 23.38 ? 498  ALA A CA    1 
ATOM   3859 C C     . ALA A 1 498 ? -10.347 -11.049 9.265   1.00 24.35 ? 498  ALA A C     1 
ATOM   3860 O O     . ALA A 1 498 ? -11.286 -10.801 10.047  1.00 25.31 ? 498  ALA A O     1 
ATOM   3861 C CB    . ALA A 1 498 ? -10.517 -10.715 6.766   1.00 25.02 ? 498  ALA A CB    1 
ATOM   3862 N N     . ILE A 1 499 ? -9.541  -12.083 9.428   1.00 22.40 ? 499  ILE A N     1 
ATOM   3863 C CA    . ILE A 1 499 ? -9.741  -13.043 10.550  1.00 22.34 ? 499  ILE A CA    1 
ATOM   3864 C C     . ILE A 1 499 ? -9.435  -12.354 11.894  1.00 22.12 ? 499  ILE A C     1 
ATOM   3865 O O     . ILE A 1 499 ? -10.279 -12.475 12.826  1.00 21.86 ? 499  ILE A O     1 
ATOM   3866 C CB    . ILE A 1 499 ? -8.975  -14.350 10.326  1.00 23.75 ? 499  ILE A CB    1 
ATOM   3867 C CG1   . ILE A 1 499 ? -9.591  -15.147 9.176   1.00 25.21 ? 499  ILE A CG1   1 
ATOM   3868 C CG2   . ILE A 1 499 ? -8.963  -15.179 11.601  1.00 23.13 ? 499  ILE A CG2   1 
ATOM   3869 C CD1   . ILE A 1 499 ? -8.732  -16.287 8.706   1.00 25.12 ? 499  ILE A CD1   1 
ATOM   3870 N N     . LYS A 1 500 ? -8.320  -11.641 12.007  1.00 21.89 ? 500  LYS A N     1 
ATOM   3871 C CA    . LYS A 1 500 ? -7.947  -10.911 13.253  1.00 21.46 ? 500  LYS A CA    1 
ATOM   3872 C C     . LYS A 1 500 ? -9.092  -9.981  13.686  1.00 23.87 ? 500  LYS A C     1 
ATOM   3873 O O     . LYS A 1 500 ? -9.448  -9.982  14.896  1.00 23.24 ? 500  LYS A O     1 
ATOM   3874 C CB    . LYS A 1 500 ? -6.657  -10.138 13.017  1.00 20.81 ? 500  LYS A CB    1 
ATOM   3875 C CG    . LYS A 1 500 ? -6.212  -9.290  14.185  1.00 20.53 ? 500  LYS A CG    1 
ATOM   3876 C CD    . LYS A 1 500 ? -5.970  -10.101 15.394  1.00 22.63 ? 500  LYS A CD    1 
ATOM   3877 C CE    . LYS A 1 500 ? -5.166  -9.324  16.402  1.00 23.65 ? 500  LYS A CE    1 
ATOM   3878 N NZ    . LYS A 1 500 ? -5.095  -10.048 17.693  1.00 23.83 ? 500  LYS A NZ    1 
ATOM   3879 N N     . ASP A 1 501 ? -9.624  -9.179  12.767  1.00 24.71 ? 501  ASP A N     1 
ATOM   3880 C CA    . ASP A 1 501 ? -10.667 -8.159  13.080  1.00 26.11 ? 501  ASP A CA    1 
ATOM   3881 C C     . ASP A 1 501 ? -11.971 -8.861  13.474  1.00 26.80 ? 501  ASP A C     1 
ATOM   3882 O O     . ASP A 1 501 ? -12.634 -8.334  14.377  1.00 28.95 ? 501  ASP A O     1 
ATOM   3883 C CB    . ASP A 1 501 ? -10.796 -7.121  11.962  1.00 26.26 ? 501  ASP A CB    1 
ATOM   3884 C CG    . ASP A 1 501 ? -9.633  -6.134  11.895  1.00 28.63 ? 501  ASP A CG    1 
ATOM   3885 O OD1   . ASP A 1 501 ? -8.980  -5.856  12.963  1.00 24.41 ? 501  ASP A OD1   1 
ATOM   3886 O OD2   . ASP A 1 501 ? -9.332  -5.668  10.775  1.00 27.36 ? 501  ASP A OD2   1 
ATOM   3887 N N     . ALA A 1 502 ? -12.299 -10.027 12.903  1.00 26.08 ? 502  ALA A N     1 
ATOM   3888 C CA    . ALA A 1 502 ? -13.543 -10.759 13.239  1.00 27.82 ? 502  ALA A CA    1 
ATOM   3889 C C     . ALA A 1 502 ? -13.425 -11.357 14.649  1.00 29.17 ? 502  ALA A C     1 
ATOM   3890 O O     . ALA A 1 502 ? -14.379 -11.163 15.468  1.00 29.24 ? 502  ALA A O     1 
ATOM   3891 C CB    . ALA A 1 502 ? -13.838 -11.831 12.244  1.00 27.20 ? 502  ALA A CB    1 
ATOM   3892 N N     . LEU A 1 503 ? -12.309 -12.029 14.931  1.00 24.60 ? 503  LEU A N     1 
ATOM   3893 C CA    . LEU A 1 503 ? -12.070 -12.707 16.235  1.00 26.09 ? 503  LEU A CA    1 
ATOM   3894 C C     . LEU A 1 503 ? -11.734 -11.693 17.318  1.00 24.93 ? 503  LEU A C     1 
ATOM   3895 O O     . LEU A 1 503 ? -12.003 -12.006 18.507  1.00 24.20 ? 503  LEU A O     1 
ATOM   3896 C CB    . LEU A 1 503 ? -10.932 -13.734 16.112  1.00 24.65 ? 503  LEU A CB    1 
ATOM   3897 C CG    . LEU A 1 503 ? -11.222 -14.979 15.275  1.00 24.02 ? 503  LEU A CG    1 
ATOM   3898 C CD1   . LEU A 1 503 ? -10.031 -15.917 15.263  1.00 26.68 ? 503  LEU A CD1   1 
ATOM   3899 C CD2   . LEU A 1 503 ? -12.463 -15.693 15.736  1.00 27.89 ? 503  LEU A CD2   1 
ATOM   3900 N N     . ASP A 1 504 ? -11.112 -10.576 16.946  1.00 22.39 ? 504  ASP A N     1 
ATOM   3901 C CA    . ASP A 1 504 ? -10.524 -9.621  17.911  1.00 23.34 ? 504  ASP A CA    1 
ATOM   3902 C C     . ASP A 1 504 ? -11.002 -8.217  17.556  1.00 24.16 ? 504  ASP A C     1 
ATOM   3903 O O     . ASP A 1 504 ? -10.196 -7.360  17.192  1.00 22.01 ? 504  ASP A O     1 
ATOM   3904 C CB    . ASP A 1 504 ? -9.006  -9.770  17.904  1.00 24.40 ? 504  ASP A CB    1 
ATOM   3905 C CG    . ASP A 1 504 ? -8.319  -9.168  19.112  1.00 24.49 ? 504  ASP A CG    1 
ATOM   3906 O OD1   . ASP A 1 504 ? -8.999  -8.476  19.904  1.00 26.87 ? 504  ASP A OD1   1 
ATOM   3907 O OD2   . ASP A 1 504 ? -7.105  -9.409  19.254  1.00 25.61 ? 504  ASP A OD2   1 
ATOM   3908 N N     . PRO A 1 505 ? -12.324 -7.930  17.644  1.00 24.44 ? 505  PRO A N     1 
ATOM   3909 C CA    . PRO A 1 505 ? -12.846 -6.617  17.244  1.00 28.02 ? 505  PRO A CA    1 
ATOM   3910 C C     . PRO A 1 505 ? -12.312 -5.431  18.065  1.00 25.58 ? 505  PRO A C     1 
ATOM   3911 O O     . PRO A 1 505 ? -12.331 -4.340  17.557  1.00 27.40 ? 505  PRO A O     1 
ATOM   3912 C CB    . PRO A 1 505 ? -14.364 -6.800  17.404  1.00 29.26 ? 505  PRO A CB    1 
ATOM   3913 C CG    . PRO A 1 505 ? -14.483 -7.837  18.491  1.00 28.22 ? 505  PRO A CG    1 
ATOM   3914 C CD    . PRO A 1 505 ? -13.373 -8.814  18.167  1.00 27.90 ? 505  PRO A CD    1 
ATOM   3915 N N     . ASN A 1 506 ? -11.861 -5.651  19.310  1.00 24.49 ? 506  ASN A N     1 
ATOM   3916 C CA    . ASN A 1 506 ? -11.287 -4.592  20.175  1.00 23.78 ? 506  ASN A CA    1 
ATOM   3917 C C     . ASN A 1 506 ? -9.754  -4.560  20.049  1.00 22.14 ? 506  ASN A C     1 
ATOM   3918 O O     . ASN A 1 506 ? -9.119  -3.752  20.736  1.00 23.55 ? 506  ASN A O     1 
ATOM   3919 C CB    . ASN A 1 506 ? -11.742 -4.770  21.629  1.00 23.97 ? 506  ASN A CB    1 
ATOM   3920 C CG    . ASN A 1 506 ? -13.246 -4.715  21.772  1.00 26.62 ? 506  ASN A CG    1 
ATOM   3921 O OD1   . ASN A 1 506 ? -13.886 -3.845  21.192  1.00 26.31 ? 506  ASN A OD1   1 
ATOM   3922 N ND2   . ASN A 1 506 ? -13.828 -5.693  22.451  1.00 25.81 ? 506  ASN A ND2   1 
ATOM   3923 N N     . GLY A 1 507 ? -9.159  -5.406  19.220  1.00 24.34 ? 507  GLY A N     1 
ATOM   3924 C CA    . GLY A 1 507 ? -7.720  -5.351  18.908  1.00 22.86 ? 507  GLY A CA    1 
ATOM   3925 C C     . GLY A 1 507 ? -6.842  -5.544  20.116  1.00 21.69 ? 507  GLY A C     1 
ATOM   3926 O O     . GLY A 1 507 ? -5.969  -4.698  20.377  1.00 23.12 ? 507  GLY A O     1 
ATOM   3927 N N     . ILE A 1 508 ? -7.039  -6.647  20.815  1.00 23.55 ? 508  ILE A N     1 
ATOM   3928 C CA    . ILE A 1 508 ? -6.423  -6.921  22.150  1.00 23.26 ? 508  ILE A CA    1 
ATOM   3929 C C     . ILE A 1 508 ? -5.159  -7.773  22.025  1.00 19.31 ? 508  ILE A C     1 
ATOM   3930 O O     . ILE A 1 508 ? -4.160  -7.378  22.620  1.00 21.64 ? 508  ILE A O     1 
ATOM   3931 C CB    . ILE A 1 508 ? -7.479  -7.576  23.052  1.00 22.82 ? 508  ILE A CB    1 
ATOM   3932 C CG1   . ILE A 1 508 ? -8.672  -6.639  23.255  1.00 24.51 ? 508  ILE A CG1   1 
ATOM   3933 C CG2   . ILE A 1 508 ? -6.866  -8.013  24.369  1.00 23.03 ? 508  ILE A CG2   1 
ATOM   3934 C CD1   . ILE A 1 508 ? -8.306  -5.253  23.753  1.00 24.11 ? 508  ILE A CD1   1 
ATOM   3935 N N     . ILE A 1 509 ? -5.197  -8.926  21.346  1.00 21.80 ? 509  ILE A N     1 
ATOM   3936 C CA    . ILE A 1 509 ? -4.113  -9.948  21.488  1.00 22.78 ? 509  ILE A CA    1 
ATOM   3937 C C     . ILE A 1 509 ? -2.920  -9.582  20.595  1.00 24.48 ? 509  ILE A C     1 
ATOM   3938 O O     . ILE A 1 509 ? -3.139  -9.395  19.362  1.00 25.07 ? 509  ILE A O     1 
ATOM   3939 C CB    . ILE A 1 509 ? -4.601  -11.373 21.177  1.00 23.30 ? 509  ILE A CB    1 
ATOM   3940 C CG1   . ILE A 1 509 ? -5.831  -11.753 22.008  1.00 25.36 ? 509  ILE A CG1   1 
ATOM   3941 C CG2   . ILE A 1 509 ? -3.472  -12.383 21.363  1.00 24.15 ? 509  ILE A CG2   1 
ATOM   3942 C CD1   . ILE A 1 509 ? -5.572  -11.758 23.483  1.00 26.23 ? 509  ILE A CD1   1 
ATOM   3943 N N     . ALA A 1 510 ? -1.725  -9.547  21.200  1.00 23.16 ? 510  ALA A N     1 
ATOM   3944 C CA    . ALA A 1 510 ? -0.363  -9.366  20.604  1.00 21.35 ? 510  ALA A CA    1 
ATOM   3945 C C     . ALA A 1 510 ? -0.418  -8.621  19.270  1.00 22.17 ? 510  ALA A C     1 
ATOM   3946 O O     . ALA A 1 510 ? -0.048  -9.186  18.225  1.00 21.83 ? 510  ALA A O     1 
ATOM   3947 C CB    . ALA A 1 510 ? 0.325   -10.714 20.463  1.00 21.75 ? 510  ALA A CB    1 
ATOM   3948 N N     . PRO A 1 511 ? -0.890  -7.354  19.254  1.00 22.59 ? 511  PRO A N     1 
ATOM   3949 C CA    . PRO A 1 511 ? -1.006  -6.589  18.013  1.00 22.08 ? 511  PRO A CA    1 
ATOM   3950 C C     . PRO A 1 511 ? 0.347   -6.529  17.290  1.00 21.72 ? 511  PRO A C     1 
ATOM   3951 O O     . PRO A 1 511 ? 1.386   -6.336  17.938  1.00 21.25 ? 511  PRO A O     1 
ATOM   3952 C CB    . PRO A 1 511 ? -1.478  -5.202  18.474  1.00 23.52 ? 511  PRO A CB    1 
ATOM   3953 C CG    . PRO A 1 511 ? -2.185  -5.500  19.756  1.00 25.06 ? 511  PRO A CG    1 
ATOM   3954 C CD    . PRO A 1 511 ? -1.323  -6.552  20.419  1.00 23.78 ? 511  PRO A CD    1 
ATOM   3955 N N     . GLY A 1 512 ? 0.316   -6.743  15.976  1.00 22.86 ? 512  GLY A N     1 
ATOM   3956 C CA    . GLY A 1 512 ? 1.512   -6.683  15.112  1.00 21.78 ? 512  GLY A CA    1 
ATOM   3957 C C     . GLY A 1 512 ? 2.306   -7.979  15.062  1.00 22.62 ? 512  GLY A C     1 
ATOM   3958 O O     . GLY A 1 512 ? 3.289   -8.028  14.327  1.00 22.20 ? 512  GLY A O     1 
ATOM   3959 N N     . LYS A 1 513 ? 1.941   -9.012  15.822  1.00 21.87 ? 513  LYS A N     1 
ATOM   3960 C CA    . LYS A 1 513 ? 2.610   -10.334 15.718  1.00 21.13 ? 513  LYS A CA    1 
ATOM   3961 C C     . LYS A 1 513 ? 2.538   -10.774 14.255  1.00 19.00 ? 513  LYS A C     1 
ATOM   3962 O O     . LYS A 1 513 ? 1.431   -10.727 13.702  1.00 17.28 ? 513  LYS A O     1 
ATOM   3963 C CB    . LYS A 1 513 ? 1.914   -11.393 16.573  1.00 21.23 ? 513  LYS A CB    1 
ATOM   3964 C CG    . LYS A 1 513 ? 2.469   -12.810 16.443  1.00 23.02 ? 513  LYS A CG    1 
ATOM   3965 C CD    . LYS A 1 513 ? 3.961   -12.942 16.749  1.00 25.17 ? 513  LYS A CD    1 
ATOM   3966 C CE    . LYS A 1 513 ? 4.506   -14.333 16.495  1.00 24.82 ? 513  LYS A CE    1 
ATOM   3967 N NZ    . LYS A 1 513 ? 5.958   -14.472 16.769  1.00 23.67 ? 513  LYS A NZ    1 
ATOM   3968 N N     . SER A 1 514 ? 3.667   -11.153 13.653  1.00 18.85 ? 514  SER A N     1 
ATOM   3969 C CA    . SER A 1 514 ? 3.732   -11.614 12.236  1.00 19.60 ? 514  SER A CA    1 
ATOM   3970 C C     . SER A 1 514 ? 3.232   -10.524 11.275  1.00 21.81 ? 514  SER A C     1 
ATOM   3971 O O     . SER A 1 514 ? 2.752   -10.888 10.145  1.00 20.46 ? 514  SER A O     1 
ATOM   3972 C CB    . SER A 1 514 ? 2.955   -12.891 12.055  1.00 17.99 ? 514  SER A CB    1 
ATOM   3973 O OG    . SER A 1 514 ? 3.486   -13.903 12.868  1.00 19.23 ? 514  SER A OG    1 
ATOM   3974 N N     . GLY A 1 515 ? 3.317   -9.257  11.686  1.00 21.50 ? 515  GLY A N     1 
ATOM   3975 C CA    . GLY A 1 515 ? 2.850   -8.115  10.871  1.00 23.24 ? 515  GLY A CA    1 
ATOM   3976 C C     . GLY A 1 515 ? 1.330   -8.009  10.784  1.00 23.30 ? 515  GLY A C     1 
ATOM   3977 O O     . GLY A 1 515 ? 0.842   -7.215  9.954   1.00 20.95 ? 515  GLY A O     1 
ATOM   3978 N N     . VAL A 1 516 ? 0.576   -8.721  11.652  1.00 20.69 ? 516  VAL A N     1 
ATOM   3979 C CA    . VAL A 1 516 ? -0.912  -8.699  11.588  1.00 20.03 ? 516  VAL A CA    1 
ATOM   3980 C C     . VAL A 1 516 ? -1.408  -7.747  12.664  1.00 21.25 ? 516  VAL A C     1 
ATOM   3981 O O     . VAL A 1 516 ? -1.309  -8.090  13.854  1.00 21.12 ? 516  VAL A O     1 
ATOM   3982 C CB    . VAL A 1 516 ? -1.498  -10.117 11.720  1.00 20.85 ? 516  VAL A CB    1 
ATOM   3983 C CG1   . VAL A 1 516 ? -3.015  -10.138 11.564  1.00 20.78 ? 516  VAL A CG1   1 
ATOM   3984 C CG2   . VAL A 1 516 ? -0.815  -11.071 10.742  1.00 20.66 ? 516  VAL A CG2   1 
ATOM   3985 N N     . TRP A 1 517 ? -1.883  -6.580  12.229  1.00 21.19 ? 517  TRP A N     1 
ATOM   3986 C CA    . TRP A 1 517 ? -2.352  -5.515  13.134  1.00 23.13 ? 517  TRP A CA    1 
ATOM   3987 C C     . TRP A 1 517 ? -3.864  -5.551  13.112  1.00 23.61 ? 517  TRP A C     1 
ATOM   3988 O O     . TRP A 1 517 ? -4.484  -5.589  12.045  1.00 22.48 ? 517  TRP A O     1 
ATOM   3989 C CB    . TRP A 1 517 ? -1.807  -4.148  12.686  1.00 24.44 ? 517  TRP A CB    1 
ATOM   3990 C CG    . TRP A 1 517 ? -0.329  -4.037  12.863  1.00 23.17 ? 517  TRP A CG    1 
ATOM   3991 C CD1   . TRP A 1 517 ? 0.636   -4.284  11.921  1.00 22.51 ? 517  TRP A CD1   1 
ATOM   3992 C CD2   . TRP A 1 517 ? 0.367   -3.664  14.055  1.00 21.99 ? 517  TRP A CD2   1 
ATOM   3993 N NE1   . TRP A 1 517 ? 1.879   -4.068  12.440  1.00 21.84 ? 517  TRP A NE1   1 
ATOM   3994 C CE2   . TRP A 1 517 ? 1.743   -3.687  13.752  1.00 24.56 ? 517  TRP A CE2   1 
ATOM   3995 C CE3   . TRP A 1 517 ? -0.036  -3.303  15.341  1.00 21.82 ? 517  TRP A CE3   1 
ATOM   3996 C CZ2   . TRP A 1 517 ? 2.726   -3.374  14.688  1.00 22.81 ? 517  TRP A CZ2   1 
ATOM   3997 C CZ3   . TRP A 1 517 ? 0.932   -2.984  16.265  1.00 22.30 ? 517  TRP A CZ3   1 
ATOM   3998 C CH2   . TRP A 1 517 ? 2.294   -3.031  15.949  1.00 23.62 ? 517  TRP A CH2   1 
ATOM   3999 N N     . PRO A 1 518 ? -4.515  -5.474  14.291  1.00 24.44 ? 518  PRO A N     1 
ATOM   4000 C CA    . PRO A 1 518 ? -5.941  -5.206  14.305  1.00 26.19 ? 518  PRO A CA    1 
ATOM   4001 C C     . PRO A 1 518 ? -6.148  -3.752  13.838  1.00 23.99 ? 518  PRO A C     1 
ATOM   4002 O O     . PRO A 1 518 ? -5.227  -2.946  13.970  1.00 21.02 ? 518  PRO A O     1 
ATOM   4003 C CB    . PRO A 1 518 ? -6.310  -5.428  15.783  1.00 25.24 ? 518  PRO A CB    1 
ATOM   4004 C CG    . PRO A 1 518 ? -5.052  -5.028  16.519  1.00 24.29 ? 518  PRO A CG    1 
ATOM   4005 C CD    . PRO A 1 518 ? -3.903  -5.458  15.626  1.00 23.97 ? 518  PRO A CD    1 
ATOM   4006 N N     . ALA A 1 519 ? -7.364  -3.475  13.376  1.00 24.29 ? 519  ALA A N     1 
ATOM   4007 C CA    . ALA A 1 519 ? -7.818  -2.200  12.776  1.00 27.55 ? 519  ALA A CA    1 
ATOM   4008 C C     . ALA A 1 519 ? -7.339  -1.009  13.600  1.00 28.12 ? 519  ALA A C     1 
ATOM   4009 O O     . ALA A 1 519 ? -6.789  -0.095  13.023  1.00 27.87 ? 519  ALA A O     1 
ATOM   4010 C CB    . ALA A 1 519 ? -9.311  -2.222  12.642  1.00 29.69 ? 519  ALA A CB    1 
ATOM   4011 N N     . ARG A 1 520 ? -7.491  -1.017  14.923  1.00 25.67 ? 520  ARG A N     1 
ATOM   4012 C CA    . ARG A 1 520 ? -7.262  0.217   15.711  1.00 26.47 ? 520  ARG A CA    1 
ATOM   4013 C C     . ARG A 1 520 ? -5.774  0.589   15.747  1.00 25.45 ? 520  ARG A C     1 
ATOM   4014 O O     . ARG A 1 520 ? -5.483  1.757   16.106  1.00 28.15 ? 520  ARG A O     1 
ATOM   4015 C CB    . ARG A 1 520 ? -7.847  0.073   17.117  1.00 27.57 ? 520  ARG A CB    1 
ATOM   4016 C CG    . ARG A 1 520 ? -7.090  -0.874  18.020  1.00 29.79 ? 520  ARG A CG    1 
ATOM   4017 C CD    . ARG A 1 520 ? -7.621  -0.657  19.414  1.00 30.31 ? 520  ARG A CD    1 
ATOM   4018 N NE    . ARG A 1 520 ? -7.028  -1.622  20.296  1.00 33.43 ? 520  ARG A NE    1 
ATOM   4019 C CZ    . ARG A 1 520 ? -6.685  -1.406  21.557  1.00 29.65 ? 520  ARG A CZ    1 
ATOM   4020 N NH1   . ARG A 1 520 ? -6.817  -0.212  22.109  1.00 31.97 ? 520  ARG A NH1   1 
ATOM   4021 N NH2   . ARG A 1 520 ? -6.184  -2.407  22.250  1.00 30.50 ? 520  ARG A NH2   1 
ATOM   4022 N N     . TYR A 1 521 ? -4.851  -0.323  15.409  1.00 25.26 ? 521  TYR A N     1 
ATOM   4023 C CA    . TYR A 1 521 ? -3.389  -0.090  15.503  1.00 24.70 ? 521  TYR A CA    1 
ATOM   4024 C C     . TYR A 1 521 ? -2.721  -0.131  14.124  1.00 26.25 ? 521  TYR A C     1 
ATOM   4025 O O     . TYR A 1 521 ? -1.541  0.153   14.042  1.00 27.66 ? 521  TYR A O     1 
ATOM   4026 C CB    . TYR A 1 521 ? -2.693  -1.123  16.386  1.00 27.33 ? 521  TYR A CB    1 
ATOM   4027 C CG    . TYR A 1 521 ? -2.964  -0.955  17.855  1.00 26.20 ? 521  TYR A CG    1 
ATOM   4028 C CD1   . TYR A 1 521 ? -2.682  0.240   18.504  1.00 28.07 ? 521  TYR A CD1   1 
ATOM   4029 C CD2   . TYR A 1 521 ? -3.420  -2.027  18.603  1.00 27.34 ? 521  TYR A CD2   1 
ATOM   4030 C CE1   . TYR A 1 521 ? -2.922  0.386   19.863  1.00 28.44 ? 521  TYR A CE1   1 
ATOM   4031 C CE2   . TYR A 1 521 ? -3.639  -1.901  19.960  1.00 26.19 ? 521  TYR A CE2   1 
ATOM   4032 C CZ    . TYR A 1 521 ? -3.371  -0.702  20.589  1.00 28.02 ? 521  TYR A CZ    1 
ATOM   4033 O OH    . TYR A 1 521 ? -3.594  -0.596  21.934  1.00 27.68 ? 521  TYR A OH    1 
ATOM   4034 N N     . ARG A 1 522 ? -3.462  -0.465  13.088  1.00 29.41 ? 522  ARG A N     1 
ATOM   4035 C CA    . ARG A 1 522 ? -2.879  -0.741  11.754  1.00 30.66 ? 522  ARG A CA    1 
ATOM   4036 C C     . ARG A 1 522 ? -2.605  0.611   11.081  1.00 32.73 ? 522  ARG A C     1 
ATOM   4037 O O     . ARG A 1 522 ? -3.426  1.503   11.225  1.00 31.92 ? 522  ARG A O     1 
ATOM   4038 C CB    . ARG A 1 522 ? -3.841  -1.633  10.975  1.00 30.04 ? 522  ARG A CB    1 
ATOM   4039 C CG    . ARG A 1 522 ? -3.409  -1.905  9.548   1.00 32.04 ? 522  ARG A CG    1 
ATOM   4040 C CD    . ARG A 1 522 ? -4.471  -2.672  8.762   1.00 31.81 ? 522  ARG A CD    1 
ATOM   4041 N NE    . ARG A 1 522 ? -5.050  -3.686  9.603   1.00 32.69 ? 522  ARG A NE    1 
ATOM   4042 C CZ    . ARG A 1 522 ? -6.341  -4.005  9.664   1.00 31.14 ? 522  ARG A CZ    1 
ATOM   4043 N NH1   . ARG A 1 522 ? -7.230  -3.405  8.896   1.00 34.01 ? 522  ARG A NH1   1 
ATOM   4044 N NH2   . ARG A 1 522 ? -6.737  -4.954  10.489  1.00 27.56 ? 522  ARG A NH2   1 
ATOM   4045 N N     . GLY A 1 523 ? -1.475  0.739   10.388  1.00 35.38 ? 523  GLY A N     1 
ATOM   4046 C CA    . GLY A 1 523 ? -1.066  1.970   9.685   1.00 36.14 ? 523  GLY A CA    1 
ATOM   4047 C C     . GLY A 1 523 ? -0.789  3.141   10.606  1.00 38.48 ? 523  GLY A C     1 
ATOM   4048 O O     . GLY A 1 523 ? -0.840  4.277   10.112  1.00 36.47 ? 523  GLY A O     1 
ATOM   4049 N N     . LYS A 1 524 ? -0.438  2.899   11.877  1.00 39.31 ? 524  LYS A N     1 
ATOM   4050 C CA    . LYS A 1 524 ? -0.175  3.971   12.880  1.00 40.16 ? 524  LYS A CA    1 
ATOM   4051 C C     . LYS A 1 524 ? 1.334   4.079   13.148  1.00 36.26 ? 524  LYS A C     1 
ATOM   4052 O O     . LYS A 1 524 ? 1.715   4.764   14.090  1.00 36.58 ? 524  LYS A O     1 
ATOM   4053 C CB    . LYS A 1 524 ? -0.941  3.705   14.179  1.00 43.72 ? 524  LYS A CB    1 
ATOM   4054 C CG    . LYS A 1 524 ? -2.447  3.513   14.040  1.00 49.13 ? 524  LYS A CG    1 
ATOM   4055 C CD    . LYS A 1 524 ? -3.249  4.767   13.775  1.00 54.24 ? 524  LYS A CD    1 
ATOM   4056 C CE    . LYS A 1 524 ? -4.739  4.499   13.700  1.00 55.88 ? 524  LYS A CE    1 
ATOM   4057 N NZ    . LYS A 1 524 ? -5.381  4.671   15.022  1.00 59.46 ? 524  LYS A NZ    1 
ATOM   4058 N N     . GLY A 1 525 ? 2.156   3.389   12.361  1.00 35.60 ? 525  GLY A N     1 
ATOM   4059 C CA    . GLY A 1 525 ? 3.615   3.283   12.539  1.00 35.47 ? 525  GLY A CA    1 
ATOM   4060 C C     . GLY A 1 525 ? 3.986   2.754   13.903  1.00 37.42 ? 525  GLY A C     1 
ATOM   4061 O O     . GLY A 1 525 ? 5.096   3.100   14.343  1.00 31.60 ? 525  GLY A O     1 
ATOM   4062 N N     . LEU A 1 526 ? 3.090   1.939   14.498  1.00 37.65 ? 526  LEU A N     1 
ATOM   4063 C CA    . LEU A 1 526 ? 3.099   1.390   15.891  1.00 41.85 ? 526  LEU A CA    1 
ATOM   4064 C C     . LEU A 1 526 ? 2.212   2.217   16.839  1.00 43.33 ? 526  LEU A C     1 
ATOM   4065 O O     . LEU A 1 526 ? 1.124   1.828   17.233  1.00 50.80 ? 526  LEU A O     1 
ATOM   4066 C CB    . LEU A 1 526 ? 4.546   1.383   16.368  1.00 41.61 ? 526  LEU A CB    1 
ATOM   4067 C CG    . LEU A 1 526 ? 5.319   0.135   15.968  1.00 29.70 ? 526  LEU A CG    1 
ATOM   4068 C CD1   . LEU A 1 526 ? 4.988   -0.907  16.953  1.00 33.38 ? 526  LEU A CD1   1 
ATOM   4069 C CD2   . LEU A 1 526 ? 5.011   -0.285  14.524  1.00 26.57 ? 526  LEU A CD2   1 
ATOM   4070 N N     . ARG B 1 3   ? -38.696 -26.045 -11.718 1.00 60.06 ? 3    ARG B N     1 
ATOM   4071 C CA    . ARG B 1 3   ? -37.276 -25.602 -11.975 1.00 61.61 ? 3    ARG B CA    1 
ATOM   4072 C C     . ARG B 1 3   ? -36.567 -25.320 -10.643 1.00 59.73 ? 3    ARG B C     1 
ATOM   4073 O O     . ARG B 1 3   ? -37.007 -24.388 -9.941  1.00 62.43 ? 3    ARG B O     1 
ATOM   4074 C CB    . ARG B 1 3   ? -37.270 -24.332 -12.824 1.00 61.95 ? 3    ARG B CB    1 
ATOM   4075 C CG    . ARG B 1 3   ? -35.882 -23.775 -13.097 1.00 59.84 ? 3    ARG B CG    1 
ATOM   4076 C CD    . ARG B 1 3   ? -35.855 -22.258 -13.031 1.00 59.02 ? 3    ARG B CD    1 
ATOM   4077 N NE    . ARG B 1 3   ? -34.867 -21.710 -13.953 1.00 56.89 ? 3    ARG B NE    1 
ATOM   4078 C CZ    . ARG B 1 3   ? -34.521 -20.428 -14.059 1.00 53.85 ? 3    ARG B CZ    1 
ATOM   4079 N NH1   . ARG B 1 3   ? -35.042 -19.504 -13.269 1.00 52.76 ? 3    ARG B NH1   1 
ATOM   4080 N NH2   . ARG B 1 3   ? -33.595 -20.081 -14.931 1.00 57.06 ? 3    ARG B NH2   1 
ATOM   4081 N N     . THR B 1 4   ? -35.509 -26.071 -10.307 1.00 58.78 ? 4    THR B N     1 
ATOM   4082 C CA    . THR B 1 4   ? -34.784 -25.946 -9.010  1.00 55.22 ? 4    THR B CA    1 
ATOM   4083 C C     . THR B 1 4   ? -34.172 -24.542 -8.907  1.00 50.22 ? 4    THR B C     1 
ATOM   4084 O O     . THR B 1 4   ? -33.406 -24.173 -9.820  1.00 52.20 ? 4    THR B O     1 
ATOM   4085 C CB    . THR B 1 4   ? -33.736 -27.052 -8.839  1.00 53.23 ? 4    THR B CB    1 
ATOM   4086 O OG1   . THR B 1 4   ? -34.423 -28.298 -8.918  1.00 53.26 ? 4    THR B OG1   1 
ATOM   4087 C CG2   . THR B 1 4   ? -33.001 -26.984 -7.519  1.00 54.01 ? 4    THR B CG2   1 
ATOM   4088 N N     . LEU B 1 5   ? -34.554 -23.782 -7.875  1.00 47.66 ? 5    LEU B N     1 
ATOM   4089 C CA    . LEU B 1 5   ? -33.974 -22.455 -7.545  1.00 49.94 ? 5    LEU B CA    1 
ATOM   4090 C C     . LEU B 1 5   ? -33.126 -22.624 -6.295  1.00 46.93 ? 5    LEU B C     1 
ATOM   4091 O O     . LEU B 1 5   ? -33.456 -23.423 -5.426  1.00 46.85 ? 5    LEU B O     1 
ATOM   4092 C CB    . LEU B 1 5   ? -35.077 -21.421 -7.288  1.00 53.34 ? 5    LEU B CB    1 
ATOM   4093 C CG    . LEU B 1 5   ? -35.882 -20.945 -8.498  1.00 58.77 ? 5    LEU B CG    1 
ATOM   4094 C CD1   . LEU B 1 5   ? -36.724 -19.732 -8.119  1.00 60.22 ? 5    LEU B CD1   1 
ATOM   4095 C CD2   . LEU B 1 5   ? -34.994 -20.589 -9.685  1.00 60.16 ? 5    LEU B CD2   1 
ATOM   4096 N N     . PRO B 1 6   ? -32.001 -21.894 -6.178  1.00 44.55 ? 6    PRO B N     1 
ATOM   4097 C CA    . PRO B 1 6   ? -31.287 -21.836 -4.910  1.00 44.67 ? 6    PRO B CA    1 
ATOM   4098 C C     . PRO B 1 6   ? -32.172 -21.242 -3.820  1.00 43.07 ? 6    PRO B C     1 
ATOM   4099 O O     . PRO B 1 6   ? -32.942 -20.324 -4.077  1.00 44.89 ? 6    PRO B O     1 
ATOM   4100 C CB    . PRO B 1 6   ? -30.086 -20.927 -5.202  1.00 43.62 ? 6    PRO B CB    1 
ATOM   4101 C CG    . PRO B 1 6   ? -29.916 -20.981 -6.709  1.00 46.92 ? 6    PRO B CG    1 
ATOM   4102 C CD    . PRO B 1 6   ? -31.314 -21.175 -7.261  1.00 42.99 ? 6    PRO B CD    1 
ATOM   4103 N N     . PRO B 1 7   ? -32.069 -21.731 -2.567  1.00 42.16 ? 7    PRO B N     1 
ATOM   4104 C CA    . PRO B 1 7   ? -32.729 -21.097 -1.433  1.00 42.23 ? 7    PRO B CA    1 
ATOM   4105 C C     . PRO B 1 7   ? -32.349 -19.622 -1.273  1.00 44.37 ? 7    PRO B C     1 
ATOM   4106 O O     . PRO B 1 7   ? -31.164 -19.319 -1.304  1.00 47.24 ? 7    PRO B O     1 
ATOM   4107 C CB    . PRO B 1 7   ? -32.228 -21.895 -0.229  1.00 43.16 ? 7    PRO B CB    1 
ATOM   4108 C CG    . PRO B 1 7   ? -31.884 -23.240 -0.803  1.00 45.90 ? 7    PRO B CG    1 
ATOM   4109 C CD    . PRO B 1 7   ? -31.328 -22.933 -2.175  1.00 44.99 ? 7    PRO B CD    1 
ATOM   4110 N N     . GLY B 1 8   ? -33.359 -18.753 -1.152  1.00 47.97 ? 8    GLY B N     1 
ATOM   4111 C CA    . GLY B 1 8   ? -33.193 -17.313 -0.886  1.00 46.67 ? 8    GLY B CA    1 
ATOM   4112 C C     . GLY B 1 8   ? -32.796 -16.534 -2.130  1.00 50.96 ? 8    GLY B C     1 
ATOM   4113 O O     . GLY B 1 8   ? -32.290 -15.405 -1.968  1.00 55.25 ? 8    GLY B O     1 
ATOM   4114 N N     . VAL B 1 9   ? -32.979 -17.093 -3.332  1.00 44.48 ? 9    VAL B N     1 
ATOM   4115 C CA    . VAL B 1 9   ? -32.700 -16.338 -4.591  1.00 49.19 ? 9    VAL B CA    1 
ATOM   4116 C C     . VAL B 1 9   ? -33.977 -16.317 -5.442  1.00 46.99 ? 9    VAL B C     1 
ATOM   4117 O O     . VAL B 1 9   ? -34.571 -17.380 -5.642  1.00 41.22 ? 9    VAL B O     1 
ATOM   4118 C CB    . VAL B 1 9   ? -31.478 -16.880 -5.365  1.00 50.90 ? 9    VAL B CB    1 
ATOM   4119 C CG1   . VAL B 1 9   ? -30.340 -17.265 -4.432  1.00 49.01 ? 9    VAL B CG1   1 
ATOM   4120 C CG2   . VAL B 1 9   ? -31.811 -18.038 -6.291  1.00 55.92 ? 9    VAL B CG2   1 
ATOM   4121 N N     . SER B 1 10  ? -34.389 -15.133 -5.895  1.00 48.41 ? 10   SER B N     1 
ATOM   4122 C CA    . SER B 1 10  ? -35.557 -14.939 -6.801  1.00 51.61 ? 10   SER B CA    1 
ATOM   4123 C C     . SER B 1 10  ? -35.261 -15.575 -8.166  1.00 52.00 ? 10   SER B C     1 
ATOM   4124 O O     . SER B 1 10  ? -34.080 -15.679 -8.543  1.00 53.84 ? 10   SER B O     1 
ATOM   4125 C CB    . SER B 1 10  ? -35.891 -13.479 -6.946  1.00 52.21 ? 10   SER B CB    1 
ATOM   4126 O OG    . SER B 1 10  ? -34.809 -12.787 -7.551  1.00 53.22 ? 10   SER B OG    1 
ATOM   4127 N N     . ASP B 1 11  ? -36.297 -15.989 -8.888  1.00 52.09 ? 11   ASP B N     1 
ATOM   4128 C CA    . ASP B 1 11  ? -36.182 -16.497 -10.281 1.00 51.78 ? 11   ASP B CA    1 
ATOM   4129 C C     . ASP B 1 11  ? -35.403 -15.478 -11.130 1.00 49.35 ? 11   ASP B C     1 
ATOM   4130 O O     . ASP B 1 11  ? -34.582 -15.895 -11.967 1.00 47.93 ? 11   ASP B O     1 
ATOM   4131 C CB    . ASP B 1 11  ? -37.574 -16.764 -10.846 1.00 58.37 ? 11   ASP B CB    1 
ATOM   4132 C CG    . ASP B 1 11  ? -37.537 -17.257 -12.270 1.00 64.51 ? 11   ASP B CG    1 
ATOM   4133 O OD1   . ASP B 1 11  ? -37.313 -18.458 -12.448 1.00 73.90 ? 11   ASP B OD1   1 
ATOM   4134 O OD2   . ASP B 1 11  ? -37.719 -16.430 -13.179 1.00 74.54 ? 11   ASP B OD2   1 
ATOM   4135 N N     . GLU B 1 12  ? -35.647 -14.182 -10.915 1.00 55.25 ? 12   GLU B N     1 
ATOM   4136 C CA    . GLU B 1 12  ? -35.049 -13.052 -11.683 1.00 58.04 ? 12   GLU B CA    1 
ATOM   4137 C C     . GLU B 1 12  ? -33.535 -13.000 -11.421 1.00 52.71 ? 12   GLU B C     1 
ATOM   4138 O O     . GLU B 1 12  ? -32.742 -12.896 -12.389 1.00 45.73 ? 12   GLU B O     1 
ATOM   4139 C CB    . GLU B 1 12  ? -35.733 -11.735 -11.291 1.00 64.63 ? 12   GLU B CB    1 
ATOM   4140 C CG    . GLU B 1 12  ? -35.489 -10.594 -12.263 1.00 72.05 ? 12   GLU B CG    1 
ATOM   4141 C CD    . GLU B 1 12  ? -34.250 -9.745  -12.016 1.00 89.11 ? 12   GLU B CD    1 
ATOM   4142 O OE1   . GLU B 1 12  ? -33.160 -10.308 -11.695 1.00 99.78 ? 12   GLU B OE1   1 
ATOM   4143 O OE2   . GLU B 1 12  ? -34.373 -8.506  -12.152 1.00 92.83 ? 12   GLU B OE2   1 
ATOM   4144 N N     . ASP B 1 13  ? -33.140 -13.020 -10.151 1.00 52.64 ? 13   ASP B N     1 
ATOM   4145 C CA    . ASP B 1 13  ? -31.713 -12.988 -9.743  1.00 52.66 ? 13   ASP B CA    1 
ATOM   4146 C C     . ASP B 1 13  ? -31.009 -14.253 -10.256 1.00 47.91 ? 13   ASP B C     1 
ATOM   4147 O O     . ASP B 1 13  ? -29.847 -14.140 -10.672 1.00 51.84 ? 13   ASP B O     1 
ATOM   4148 C CB    . ASP B 1 13  ? -31.589 -12.757 -8.236  1.00 49.87 ? 13   ASP B CB    1 
ATOM   4149 C CG    . ASP B 1 13  ? -31.835 -11.314 -7.839  1.00 54.25 ? 13   ASP B CG    1 
ATOM   4150 O OD1   . ASP B 1 13  ? -31.781 -10.441 -8.739  1.00 57.59 ? 13   ASP B OD1   1 
ATOM   4151 O OD2   . ASP B 1 13  ? -32.062 -11.066 -6.641  1.00 48.58 ? 13   ASP B OD2   1 
ATOM   4152 N N     . PHE B 1 14  ? -31.677 -15.409 -10.263 1.00 44.98 ? 14   PHE B N     1 
ATOM   4153 C CA    . PHE B 1 14  ? -31.091 -16.675 -10.757 1.00 45.19 ? 14   PHE B CA    1 
ATOM   4154 C C     . PHE B 1 14  ? -30.860 -16.567 -12.269 1.00 46.16 ? 14   PHE B C     1 
ATOM   4155 O O     . PHE B 1 14  ? -29.819 -17.035 -12.762 1.00 47.04 ? 14   PHE B O     1 
ATOM   4156 C CB    . PHE B 1 14  ? -31.969 -17.872 -10.396 1.00 41.56 ? 14   PHE B CB    1 
ATOM   4157 C CG    . PHE B 1 14  ? -31.326 -19.210 -10.662 1.00 43.47 ? 14   PHE B CG    1 
ATOM   4158 C CD1   . PHE B 1 14  ? -30.077 -19.520 -10.144 1.00 44.60 ? 14   PHE B CD1   1 
ATOM   4159 C CD2   . PHE B 1 14  ? -31.973 -20.182 -11.404 1.00 41.82 ? 14   PHE B CD2   1 
ATOM   4160 C CE1   . PHE B 1 14  ? -29.499 -20.764 -10.368 1.00 43.25 ? 14   PHE B CE1   1 
ATOM   4161 C CE2   . PHE B 1 14  ? -31.395 -21.427 -11.625 1.00 47.43 ? 14   PHE B CE2   1 
ATOM   4162 C CZ    . PHE B 1 14  ? -30.146 -21.714 -11.124 1.00 45.26 ? 14   PHE B CZ    1 
ATOM   4163 N N     . THR B 1 15  ? -31.813 -15.979 -12.997 1.00 45.73 ? 15   THR B N     1 
ATOM   4164 C CA    . THR B 1 15  ? -31.705 -15.784 -14.472 1.00 42.91 ? 15   THR B CA    1 
ATOM   4165 C C     . THR B 1 15  ? -30.502 -14.888 -14.756 1.00 39.61 ? 15   THR B C     1 
ATOM   4166 O O     . THR B 1 15  ? -29.714 -15.227 -15.650 1.00 43.32 ? 15   THR B O     1 
ATOM   4167 C CB    . THR B 1 15  ? -33.002 -15.220 -15.079 1.00 41.53 ? 15   THR B CB    1 
ATOM   4168 O OG1   . THR B 1 15  ? -34.005 -16.204 -14.844 1.00 41.08 ? 15   THR B OG1   1 
ATOM   4169 C CG2   . THR B 1 15  ? -32.891 -14.924 -16.560 1.00 38.34 ? 15   THR B CG2   1 
ATOM   4170 N N     . SER B 1 16  ? -30.382 -13.784 -14.028 1.00 42.76 ? 16   SER B N     1 
ATOM   4171 C CA    . SER B 1 16  ? -29.306 -12.771 -14.196 1.00 46.04 ? 16   SER B CA    1 
ATOM   4172 C C     . SER B 1 16  ? -27.947 -13.436 -13.953 1.00 45.47 ? 16   SER B C     1 
ATOM   4173 O O     . SER B 1 16  ? -27.019 -13.237 -14.773 1.00 44.14 ? 16   SER B O     1 
ATOM   4174 C CB    . SER B 1 16  ? -29.520 -11.589 -13.282 1.00 48.56 ? 16   SER B CB    1 
ATOM   4175 O OG    . SER B 1 16  ? -30.717 -10.905 -13.612 1.00 51.01 ? 16   SER B OG    1 
ATOM   4176 N N     . ALA B 1 17  ? -27.860 -14.238 -12.889 1.00 46.17 ? 17   ALA B N     1 
ATOM   4177 C CA    . ALA B 1 17  ? -26.616 -14.912 -12.465 1.00 42.56 ? 17   ALA B CA    1 
ATOM   4178 C C     . ALA B 1 17  ? -26.207 -15.904 -13.552 1.00 41.17 ? 17   ALA B C     1 
ATOM   4179 O O     . ALA B 1 17  ? -25.034 -15.875 -13.939 1.00 44.38 ? 17   ALA B O     1 
ATOM   4180 C CB    . ALA B 1 17  ? -26.803 -15.567 -11.114 1.00 43.81 ? 17   ALA B CB    1 
ATOM   4181 N N     . LEU B 1 18  ? -27.126 -16.743 -14.037 1.00 40.93 ? 18   LEU B N     1 
ATOM   4182 C CA    . LEU B 1 18  ? -26.802 -17.759 -15.073 1.00 37.69 ? 18   LEU B CA    1 
ATOM   4183 C C     . LEU B 1 18  ? -26.269 -17.048 -16.323 1.00 39.43 ? 18   LEU B C     1 
ATOM   4184 O O     . LEU B 1 18  ? -25.327 -17.563 -16.925 1.00 40.54 ? 18   LEU B O     1 
ATOM   4185 C CB    . LEU B 1 18  ? -28.034 -18.599 -15.401 1.00 40.34 ? 18   LEU B CB    1 
ATOM   4186 C CG    . LEU B 1 18  ? -28.530 -19.530 -14.294 1.00 43.39 ? 18   LEU B CG    1 
ATOM   4187 C CD1   . LEU B 1 18  ? -29.873 -20.145 -14.680 1.00 44.75 ? 18   LEU B CD1   1 
ATOM   4188 C CD2   . LEU B 1 18  ? -27.509 -20.618 -13.976 1.00 43.25 ? 18   LEU B CD2   1 
ATOM   4189 N N     . THR B 1 19  ? -26.844 -15.900 -16.695 1.00 42.81 ? 19   THR B N     1 
ATOM   4190 C CA    . THR B 1 19  ? -26.401 -15.136 -17.891 1.00 44.01 ? 19   THR B CA    1 
ATOM   4191 C C     . THR B 1 19  ? -24.964 -14.669 -17.659 1.00 41.69 ? 19   THR B C     1 
ATOM   4192 O O     . THR B 1 19  ? -24.108 -14.887 -18.541 1.00 40.68 ? 19   THR B O     1 
ATOM   4193 C CB    . THR B 1 19  ? -27.360 -13.984 -18.226 1.00 44.33 ? 19   THR B CB    1 
ATOM   4194 O OG1   . THR B 1 19  ? -28.574 -14.608 -18.644 1.00 45.83 ? 19   THR B OG1   1 
ATOM   4195 C CG2   . THR B 1 19  ? -26.823 -13.077 -19.312 1.00 44.19 ? 19   THR B CG2   1 
ATOM   4196 N N     . ALA B 1 20  ? -24.705 -14.081 -16.488 1.00 43.72 ? 20   ALA B N     1 
ATOM   4197 C CA    . ALA B 1 20  ? -23.365 -13.565 -16.124 1.00 41.72 ? 20   ALA B CA    1 
ATOM   4198 C C     . ALA B 1 20  ? -22.382 -14.739 -16.101 1.00 40.08 ? 20   ALA B C     1 
ATOM   4199 O O     . ALA B 1 20  ? -21.267 -14.545 -16.576 1.00 38.91 ? 20   ALA B O     1 
ATOM   4200 C CB    . ALA B 1 20  ? -23.421 -12.841 -14.808 1.00 44.13 ? 20   ALA B CB    1 
ATOM   4201 N N     . PHE B 1 21  ? -22.782 -15.903 -15.559 1.00 38.90 ? 21   PHE B N     1 
ATOM   4202 C CA    . PHE B 1 21  ? -21.936 -17.122 -15.522 1.00 38.17 ? 21   PHE B CA    1 
ATOM   4203 C C     . PHE B 1 21  ? -21.619 -17.554 -16.958 1.00 38.96 ? 21   PHE B C     1 
ATOM   4204 O O     . PHE B 1 21  ? -20.453 -17.842 -17.240 1.00 36.03 ? 21   PHE B O     1 
ATOM   4205 C CB    . PHE B 1 21  ? -22.586 -18.294 -14.780 1.00 40.61 ? 21   PHE B CB    1 
ATOM   4206 C CG    . PHE B 1 21  ? -22.796 -18.156 -13.291 1.00 38.73 ? 21   PHE B CG    1 
ATOM   4207 C CD1   . PHE B 1 21  ? -21.911 -17.464 -12.469 1.00 40.21 ? 21   PHE B CD1   1 
ATOM   4208 C CD2   . PHE B 1 21  ? -23.889 -18.771 -12.701 1.00 37.52 ? 21   PHE B CD2   1 
ATOM   4209 C CE1   . PHE B 1 21  ? -22.133 -17.369 -11.105 1.00 36.61 ? 21   PHE B CE1   1 
ATOM   4210 C CE2   . PHE B 1 21  ? -24.102 -18.688 -11.334 1.00 36.69 ? 21   PHE B CE2   1 
ATOM   4211 C CZ    . PHE B 1 21  ? -23.227 -17.977 -10.540 1.00 39.38 ? 21   PHE B CZ    1 
ATOM   4212 N N     . ARG B 1 22  ? -22.621 -17.632 -17.844 1.00 37.28 ? 22   ARG B N     1 
ATOM   4213 C CA    . ARG B 1 22  ? -22.389 -17.976 -19.277 1.00 39.02 ? 22   ARG B CA    1 
ATOM   4214 C C     . ARG B 1 22  ? -21.400 -16.990 -19.900 1.00 36.04 ? 22   ARG B C     1 
ATOM   4215 O O     . ARG B 1 22  ? -20.512 -17.439 -20.635 1.00 37.43 ? 22   ARG B O     1 
ATOM   4216 C CB    . ARG B 1 22  ? -23.695 -17.975 -20.077 1.00 37.71 ? 22   ARG B CB    1 
ATOM   4217 C CG    . ARG B 1 22  ? -24.587 -19.167 -19.784 1.00 39.28 ? 22   ARG B CG    1 
ATOM   4218 C CD    . ARG B 1 22  ? -25.847 -19.225 -20.633 1.00 40.56 ? 22   ARG B CD    1 
ATOM   4219 N NE    . ARG B 1 22  ? -26.805 -20.097 -19.972 1.00 41.05 ? 22   ARG B NE    1 
ATOM   4220 C CZ    . ARG B 1 22  ? -27.847 -19.691 -19.252 1.00 42.27 ? 22   ARG B CZ    1 
ATOM   4221 N NH1   . ARG B 1 22  ? -28.158 -18.405 -19.141 1.00 45.12 ? 22   ARG B NH1   1 
ATOM   4222 N NH2   . ARG B 1 22  ? -28.604 -20.600 -18.663 1.00 45.19 ? 22   ARG B NH2   1 
ATOM   4223 N N     . ASP B 1 23  ? -21.544 -15.700 -19.603 1.00 38.12 ? 23   ASP B N     1 
ATOM   4224 C CA    . ASP B 1 23  ? -20.669 -14.618 -20.131 1.00 39.21 ? 23   ASP B CA    1 
ATOM   4225 C C     . ASP B 1 23  ? -19.208 -14.867 -19.719 1.00 39.88 ? 23   ASP B C     1 
ATOM   4226 O O     . ASP B 1 23  ? -18.300 -14.380 -20.404 1.00 35.83 ? 23   ASP B O     1 
ATOM   4227 C CB    . ASP B 1 23  ? -21.142 -13.250 -19.645 1.00 45.03 ? 23   ASP B CB    1 
ATOM   4228 C CG    . ASP B 1 23  ? -22.494 -12.816 -20.213 1.00 54.34 ? 23   ASP B CG    1 
ATOM   4229 O OD1   . ASP B 1 23  ? -22.983 -13.466 -21.165 1.00 56.46 ? 23   ASP B OD1   1 
ATOM   4230 O OD2   . ASP B 1 23  ? -23.065 -11.835 -19.689 1.00 64.25 ? 23   ASP B OD2   1 
ATOM   4231 N N     . VAL B 1 24  ? -18.976 -15.580 -18.614 1.00 40.08 ? 24   VAL B N     1 
ATOM   4232 C CA    . VAL B 1 24  ? -17.610 -15.849 -18.085 1.00 36.22 ? 24   VAL B CA    1 
ATOM   4233 C C     . VAL B 1 24  ? -17.107 -17.186 -18.628 1.00 35.30 ? 24   VAL B C     1 
ATOM   4234 O O     . VAL B 1 24  ? -16.023 -17.181 -19.202 1.00 35.09 ? 24   VAL B O     1 
ATOM   4235 C CB    . VAL B 1 24  ? -17.575 -15.816 -16.544 1.00 39.15 ? 24   VAL B CB    1 
ATOM   4236 C CG1   . VAL B 1 24  ? -16.277 -16.408 -16.005 1.00 37.58 ? 24   VAL B CG1   1 
ATOM   4237 C CG2   . VAL B 1 24  ? -17.780 -14.406 -16.011 1.00 37.94 ? 24   VAL B CG2   1 
ATOM   4238 N N     . VAL B 1 25  ? -17.820 -18.296 -18.391 1.00 32.78 ? 25   VAL B N     1 
ATOM   4239 C CA    . VAL B 1 25  ? -17.264 -19.662 -18.618 1.00 33.05 ? 25   VAL B CA    1 
ATOM   4240 C C     . VAL B 1 25  ? -17.605 -20.174 -20.018 1.00 34.62 ? 25   VAL B C     1 
ATOM   4241 O O     . VAL B 1 25  ? -16.948 -21.139 -20.460 1.00 33.46 ? 25   VAL B O     1 
ATOM   4242 C CB    . VAL B 1 25  ? -17.708 -20.660 -17.536 1.00 33.13 ? 25   VAL B CB    1 
ATOM   4243 C CG1   . VAL B 1 25  ? -17.312 -20.144 -16.166 1.00 32.23 ? 25   VAL B CG1   1 
ATOM   4244 C CG2   . VAL B 1 25  ? -19.190 -20.972 -17.579 1.00 32.62 ? 25   VAL B CG2   1 
ATOM   4245 N N     . GLY B 1 26  ? -18.594 -19.593 -20.688 1.00 38.86 ? 26   GLY B N     1 
ATOM   4246 C CA    . GLY B 1 26  ? -19.081 -20.158 -21.958 1.00 40.49 ? 26   GLY B CA    1 
ATOM   4247 C C     . GLY B 1 26  ? -20.378 -20.921 -21.775 1.00 40.40 ? 26   GLY B C     1 
ATOM   4248 O O     . GLY B 1 26  ? -20.577 -21.587 -20.730 1.00 40.11 ? 26   GLY B O     1 
ATOM   4249 N N     . ASP B 1 27  ? -21.251 -20.823 -22.772 1.00 43.54 ? 27   ASP B N     1 
ATOM   4250 C CA    . ASP B 1 27  ? -22.604 -21.436 -22.787 1.00 44.96 ? 27   ASP B CA    1 
ATOM   4251 C C     . ASP B 1 27  ? -22.522 -22.922 -22.406 1.00 36.56 ? 27   ASP B C     1 
ATOM   4252 O O     . ASP B 1 27  ? -23.312 -23.397 -21.553 1.00 41.67 ? 27   ASP B O     1 
ATOM   4253 C CB    . ASP B 1 27  ? -23.238 -21.221 -24.165 1.00 50.52 ? 27   ASP B CB    1 
ATOM   4254 C CG    . ASP B 1 27  ? -24.606 -21.858 -24.261 1.00 66.94 ? 27   ASP B CG    1 
ATOM   4255 O OD1   . ASP B 1 27  ? -25.554 -21.302 -23.663 1.00 83.87 ? 27   ASP B OD1   1 
ATOM   4256 O OD2   . ASP B 1 27  ? -24.701 -22.938 -24.886 1.00 80.19 ? 27   ASP B OD2   1 
ATOM   4257 N N     . GLU B 1 28  ? -21.584 -23.636 -23.009 1.00 35.61 ? 28   GLU B N     1 
ATOM   4258 C CA    . GLU B 1 28  ? -21.431 -25.099 -22.863 1.00 40.33 ? 28   GLU B CA    1 
ATOM   4259 C C     . GLU B 1 28  ? -21.164 -25.454 -21.395 1.00 35.82 ? 28   GLU B C     1 
ATOM   4260 O O     . GLU B 1 28  ? -21.490 -26.591 -20.999 1.00 41.06 ? 28   GLU B O     1 
ATOM   4261 C CB    . GLU B 1 28  ? -20.291 -25.558 -23.763 1.00 45.74 ? 28   GLU B CB    1 
ATOM   4262 C CG    . GLU B 1 28  ? -19.645 -26.855 -23.339 1.00 54.47 ? 28   GLU B CG    1 
ATOM   4263 C CD    . GLU B 1 28  ? -18.541 -27.333 -24.272 1.00 62.12 ? 28   GLU B CD    1 
ATOM   4264 O OE1   . GLU B 1 28  ? -17.912 -26.477 -24.947 1.00 61.94 ? 28   GLU B OE1   1 
ATOM   4265 O OE2   . GLU B 1 28  ? -18.305 -28.567 -24.317 1.00 63.94 ? 28   GLU B OE2   1 
ATOM   4266 N N     . PHE B 1 29  ? -20.588 -24.528 -20.627 1.00 36.46 ? 29   PHE B N     1 
ATOM   4267 C CA    . PHE B 1 29  ? -20.057 -24.816 -19.263 1.00 34.52 ? 29   PHE B CA    1 
ATOM   4268 C C     . PHE B 1 29  ? -20.982 -24.264 -18.178 1.00 36.03 ? 29   PHE B C     1 
ATOM   4269 O O     . PHE B 1 29  ? -20.588 -24.217 -16.973 1.00 37.34 ? 29   PHE B O     1 
ATOM   4270 C CB    . PHE B 1 29  ? -18.616 -24.323 -19.189 1.00 34.08 ? 29   PHE B CB    1 
ATOM   4271 C CG    . PHE B 1 29  ? -17.706 -25.110 -20.084 1.00 32.59 ? 29   PHE B CG    1 
ATOM   4272 C CD1   . PHE B 1 29  ? -17.534 -26.477 -19.887 1.00 34.52 ? 29   PHE B CD1   1 
ATOM   4273 C CD2   . PHE B 1 29  ? -17.052 -24.495 -21.136 1.00 35.40 ? 29   PHE B CD2   1 
ATOM   4274 C CE1   . PHE B 1 29  ? -16.695 -27.207 -20.711 1.00 36.57 ? 29   PHE B CE1   1 
ATOM   4275 C CE2   . PHE B 1 29  ? -16.216 -25.229 -21.962 1.00 37.24 ? 29   PHE B CE2   1 
ATOM   4276 C CZ    . PHE B 1 29  ? -16.036 -26.579 -21.746 1.00 37.86 ? 29   PHE B CZ    1 
ATOM   4277 N N     . VAL B 1 30  ? -22.202 -23.889 -18.567 1.00 37.32 ? 30   VAL B N     1 
ATOM   4278 C CA    . VAL B 1 30  ? -23.310 -23.651 -17.606 1.00 38.37 ? 30   VAL B CA    1 
ATOM   4279 C C     . VAL B 1 30  ? -24.410 -24.666 -17.932 1.00 46.13 ? 30   VAL B C     1 
ATOM   4280 O O     . VAL B 1 30  ? -25.043 -24.558 -19.001 1.00 46.90 ? 30   VAL B O     1 
ATOM   4281 C CB    . VAL B 1 30  ? -23.778 -22.188 -17.632 1.00 37.70 ? 30   VAL B CB    1 
ATOM   4282 C CG1   . VAL B 1 30  ? -24.950 -21.948 -16.702 1.00 38.71 ? 30   VAL B CG1   1 
ATOM   4283 C CG2   . VAL B 1 30  ? -22.645 -21.234 -17.313 1.00 38.74 ? 30   VAL B CG2   1 
ATOM   4284 N N     . ARG B 1 31  ? -24.540 -25.665 -17.068 1.00 46.99 ? 31   ARG B N     1 
ATOM   4285 C CA    . ARG B 1 31  ? -25.496 -26.725 -17.280 1.00 46.69 ? 31   ARG B CA    1 
ATOM   4286 C C     . ARG B 1 31  ? -26.670 -26.645 -16.356 1.00 48.82 ? 31   ARG B C     1 
ATOM   4287 O O     . ARG B 1 31  ? -26.492 -26.511 -15.163 1.00 40.06 ? 31   ARG B O     1 
ATOM   4288 C CB    . ARG B 1 31  ? -24.802 -28.064 -17.178 1.00 50.67 ? 31   ARG B CB    1 
ATOM   4289 C CG    . ARG B 1 31  ? -23.739 -28.250 -18.242 1.00 54.33 ? 31   ARG B CG    1 
ATOM   4290 C CD    . ARG B 1 31  ? -22.913 -29.494 -18.005 1.00 59.86 ? 31   ARG B CD    1 
ATOM   4291 N NE    . ARG B 1 31  ? -22.116 -29.843 -19.176 1.00 63.15 ? 31   ARG B NE    1 
ATOM   4292 C CZ    . ARG B 1 31  ? -20.827 -29.557 -19.313 1.00 62.69 ? 31   ARG B CZ    1 
ATOM   4293 N NH1   . ARG B 1 31  ? -20.187 -28.912 -18.356 1.00 60.48 ? 31   ARG B NH1   1 
ATOM   4294 N NH2   . ARG B 1 31  ? -20.177 -29.914 -20.410 1.00 65.48 ? 31   ARG B NH2   1 
ATOM   4295 N N     . THR B 1 32  ? -27.877 -26.714 -16.916 1.00 45.20 ? 32   THR B N     1 
ATOM   4296 C CA    . THR B 1 32  ? -29.097 -26.605 -16.143 1.00 44.61 ? 32   THR B CA    1 
ATOM   4297 C C     . THR B 1 32  ? -30.138 -27.631 -16.598 1.00 45.18 ? 32   THR B C     1 
ATOM   4298 O O     . THR B 1 32  ? -31.222 -27.683 -16.056 1.00 45.28 ? 32   THR B O     1 
ATOM   4299 C CB    . THR B 1 32  ? -29.715 -25.224 -16.340 1.00 49.20 ? 32   THR B CB    1 
ATOM   4300 O OG1   . THR B 1 32  ? -29.809 -24.949 -17.740 1.00 51.60 ? 32   THR B OG1   1 
ATOM   4301 C CG2   . THR B 1 32  ? -28.916 -24.130 -15.659 1.00 52.59 ? 32   THR B CG2   1 
ATOM   4302 N N     . ASP B 1 33  ? -29.810 -28.440 -17.591 1.00 48.89 ? 33   ASP B N     1 
ATOM   4303 C CA    . ASP B 1 33  ? -30.711 -29.475 -18.078 1.00 50.22 ? 33   ASP B CA    1 
ATOM   4304 C C     . ASP B 1 33  ? -30.885 -30.538 -17.042 1.00 55.68 ? 33   ASP B C     1 
ATOM   4305 O O     . ASP B 1 33  ? -29.929 -30.961 -16.438 1.00 53.15 ? 33   ASP B O     1 
ATOM   4306 C CB    . ASP B 1 33  ? -30.093 -30.125 -19.300 1.00 57.96 ? 33   ASP B CB    1 
ATOM   4307 C CG    . ASP B 1 33  ? -31.088 -30.414 -20.386 1.00 70.41 ? 33   ASP B CG    1 
ATOM   4308 O OD1   . ASP B 1 33  ? -32.293 -30.565 -20.091 1.00 76.74 ? 33   ASP B OD1   1 
ATOM   4309 O OD2   . ASP B 1 33  ? -30.651 -30.497 -21.552 1.00 76.81 ? 33   ASP B OD2   1 
ATOM   4310 N N     . GLU B 1 34  ? -32.111 -30.992 -16.845 1.00 59.76 ? 34   GLU B N     1 
ATOM   4311 C CA    . GLU B 1 34  ? -32.403 -32.016 -15.851 1.00 59.02 ? 34   GLU B CA    1 
ATOM   4312 C C     . GLU B 1 34  ? -31.556 -33.244 -16.031 1.00 52.18 ? 34   GLU B C     1 
ATOM   4313 O O     . GLU B 1 34  ? -31.124 -33.834 -15.062 1.00 50.10 ? 34   GLU B O     1 
ATOM   4314 C CB    . GLU B 1 34  ? -33.888 -32.391 -15.895 1.00 64.82 ? 34   GLU B CB    1 
ATOM   4315 C CG    . GLU B 1 34  ? -34.494 -32.546 -17.277 1.00 70.39 ? 34   GLU B CG    1 
ATOM   4316 C CD    . GLU B 1 34  ? -35.706 -33.458 -17.267 1.00 73.94 ? 34   GLU B CD    1 
ATOM   4317 O OE1   . GLU B 1 34  ? -35.545 -34.666 -16.999 1.00 70.57 ? 34   GLU B OE1   1 
ATOM   4318 O OE2   . GLU B 1 34  ? -36.823 -32.964 -17.519 1.00 75.45 ? 34   GLU B OE2   1 
ATOM   4319 N N     . ALA B 1 35  ? -31.324 -33.623 -17.260 1.00 48.52 ? 35   ALA B N     1 
ATOM   4320 C CA    . ALA B 1 35  ? -30.482 -34.797 -17.601 1.00 49.30 ? 35   ALA B CA    1 
ATOM   4321 C C     . ALA B 1 35  ? -29.022 -34.566 -17.174 1.00 52.63 ? 35   ALA B C     1 
ATOM   4322 O O     . ALA B 1 35  ? -28.377 -35.544 -16.730 1.00 56.30 ? 35   ALA B O     1 
ATOM   4323 C CB    . ALA B 1 35  ? -30.582 -35.109 -19.076 1.00 48.39 ? 35   ALA B CB    1 
ATOM   4324 N N     . GLU B 1 36  ? -28.502 -33.340 -17.291 1.00 51.05 ? 36   GLU B N     1 
ATOM   4325 C CA    . GLU B 1 36  ? -27.100 -33.041 -16.891 1.00 50.86 ? 36   GLU B CA    1 
ATOM   4326 C C     . GLU B 1 36  ? -27.039 -32.925 -15.360 1.00 47.26 ? 36   GLU B C     1 
ATOM   4327 O O     . GLU B 1 36  ? -26.063 -33.427 -14.776 1.00 52.34 ? 36   GLU B O     1 
ATOM   4328 C CB    . GLU B 1 36  ? -26.568 -31.827 -17.657 1.00 58.90 ? 36   GLU B CB    1 
ATOM   4329 C CG    . GLU B 1 36  ? -26.210 -32.177 -19.098 1.00 64.56 ? 36   GLU B CG    1 
ATOM   4330 C CD    . GLU B 1 36  ? -25.752 -31.029 -19.986 1.00 69.50 ? 36   GLU B CD    1 
ATOM   4331 O OE1   . GLU B 1 36  ? -24.745 -31.207 -20.722 1.00 68.52 ? 36   GLU B OE1   1 
ATOM   4332 O OE2   . GLU B 1 36  ? -26.413 -29.964 -19.956 1.00 64.11 ? 36   GLU B OE2   1 
ATOM   4333 N N     . LEU B 1 37  ? -28.058 -32.342 -14.728 1.00 42.28 ? 37   LEU B N     1 
ATOM   4334 C CA    . LEU B 1 37  ? -28.141 -32.184 -13.252 1.00 43.26 ? 37   LEU B CA    1 
ATOM   4335 C C     . LEU B 1 37  ? -28.213 -33.567 -12.582 1.00 46.94 ? 37   LEU B C     1 
ATOM   4336 O O     . LEU B 1 37  ? -27.556 -33.742 -11.528 1.00 48.05 ? 37   LEU B O     1 
ATOM   4337 C CB    . LEU B 1 37  ? -29.346 -31.305 -12.890 1.00 39.44 ? 37   LEU B CB    1 
ATOM   4338 C CG    . LEU B 1 37  ? -29.260 -29.844 -13.342 1.00 42.32 ? 37   LEU B CG    1 
ATOM   4339 C CD1   . LEU B 1 37  ? -30.463 -29.046 -12.857 1.00 43.51 ? 37   LEU B CD1   1 
ATOM   4340 C CD2   . LEU B 1 37  ? -27.961 -29.177 -12.874 1.00 41.51 ? 37   LEU B CD2   1 
ATOM   4341 N N     . ALA B 1 38  ? -28.951 -34.519 -13.170 1.00 48.72 ? 38   ALA B N     1 
ATOM   4342 C CA    . ALA B 1 38  ? -29.144 -35.896 -12.641 1.00 51.81 ? 38   ALA B CA    1 
ATOM   4343 C C     . ALA B 1 38  ? -27.783 -36.572 -12.490 1.00 48.76 ? 38   ALA B C     1 
ATOM   4344 O O     . ALA B 1 38  ? -27.626 -37.430 -11.608 1.00 48.05 ? 38   ALA B O     1 
ATOM   4345 C CB    . ALA B 1 38  ? -30.045 -36.706 -13.545 1.00 52.23 ? 38   ALA B CB    1 
ATOM   4346 N N     . ARG B 1 39  ? -26.813 -36.160 -13.297 1.00 47.41 ? 39   ARG B N     1 
ATOM   4347 C CA    . ARG B 1 39  ? -25.456 -36.745 -13.286 1.00 49.18 ? 39   ARG B CA    1 
ATOM   4348 C C     . ARG B 1 39  ? -24.730 -36.366 -11.979 1.00 44.21 ? 39   ARG B C     1 
ATOM   4349 O O     . ARG B 1 39  ? -23.769 -37.056 -11.653 1.00 38.49 ? 39   ARG B O     1 
ATOM   4350 C CB    . ARG B 1 39  ? -24.697 -36.281 -14.530 1.00 58.88 ? 39   ARG B CB    1 
ATOM   4351 C CG    . ARG B 1 39  ? -23.953 -37.396 -15.242 1.00 68.34 ? 39   ARG B CG    1 
ATOM   4352 C CD    . ARG B 1 39  ? -23.535 -36.950 -16.629 1.00 73.99 ? 39   ARG B CD    1 
ATOM   4353 N NE    . ARG B 1 39  ? -22.588 -35.841 -16.571 1.00 81.37 ? 39   ARG B NE    1 
ATOM   4354 C CZ    . ARG B 1 39  ? -21.298 -35.945 -16.240 1.00 84.26 ? 39   ARG B CZ    1 
ATOM   4355 N NH1   . ARG B 1 39  ? -20.770 -37.117 -15.924 1.00 84.33 ? 39   ARG B NH1   1 
ATOM   4356 N NH2   . ARG B 1 39  ? -20.531 -34.868 -16.231 1.00 81.23 ? 39   ARG B NH2   1 
ATOM   4357 N N     . PHE B 1 40  ? -25.185 -35.336 -11.251 1.00 42.27 ? 40   PHE B N     1 
ATOM   4358 C CA    . PHE B 1 40  ? -24.532 -34.814 -10.019 1.00 42.56 ? 40   PHE B CA    1 
ATOM   4359 C C     . PHE B 1 40  ? -25.340 -35.220 -8.782  1.00 43.30 ? 40   PHE B C     1 
ATOM   4360 O O     . PHE B 1 40  ? -25.043 -34.733 -7.654  1.00 42.00 ? 40   PHE B O     1 
ATOM   4361 C CB    . PHE B 1 40  ? -24.360 -33.302 -10.134 1.00 41.85 ? 40   PHE B CB    1 
ATOM   4362 C CG    . PHE B 1 40  ? -23.317 -32.937 -11.153 1.00 45.24 ? 40   PHE B CG    1 
ATOM   4363 C CD1   . PHE B 1 40  ? -23.629 -32.939 -12.502 1.00 46.13 ? 40   PHE B CD1   1 
ATOM   4364 C CD2   . PHE B 1 40  ? -22.014 -32.654 -10.776 1.00 47.45 ? 40   PHE B CD2   1 
ATOM   4365 C CE1   . PHE B 1 40  ? -22.670 -32.630 -13.457 1.00 46.22 ? 40   PHE B CE1   1 
ATOM   4366 C CE2   . PHE B 1 40  ? -21.052 -32.364 -11.734 1.00 45.90 ? 40   PHE B CE2   1 
ATOM   4367 C CZ    . PHE B 1 40  ? -21.382 -32.344 -13.069 1.00 46.86 ? 40   PHE B CZ    1 
ATOM   4368 N N     . HIS B 1 41  ? -26.353 -36.061 -8.996  1.00 41.93 ? 41   HIS B N     1 
ATOM   4369 C CA    . HIS B 1 41  ? -27.133 -36.727 -7.924  1.00 42.15 ? 41   HIS B CA    1 
ATOM   4370 C C     . HIS B 1 41  ? -26.179 -37.560 -7.084  1.00 34.76 ? 41   HIS B C     1 
ATOM   4371 O O     . HIS B 1 41  ? -25.299 -38.232 -7.659  1.00 32.85 ? 41   HIS B O     1 
ATOM   4372 C CB    . HIS B 1 41  ? -28.248 -37.629 -8.481  1.00 47.43 ? 41   HIS B CB    1 
ATOM   4373 C CG    . HIS B 1 41  ? -29.468 -36.899 -8.931  1.00 55.29 ? 41   HIS B CG    1 
ATOM   4374 N ND1   . HIS B 1 41  ? -30.495 -37.532 -9.606  1.00 57.80 ? 41   HIS B ND1   1 
ATOM   4375 C CD2   . HIS B 1 41  ? -29.830 -35.603 -8.817  1.00 61.83 ? 41   HIS B CD2   1 
ATOM   4376 C CE1   . HIS B 1 41  ? -31.442 -36.660 -9.874  1.00 58.35 ? 41   HIS B CE1   1 
ATOM   4377 N NE2   . HIS B 1 41  ? -31.060 -35.471 -9.403  1.00 61.42 ? 41   HIS B NE2   1 
ATOM   4378 N N     . ASP B 1 42  ? -26.353 -37.529 -5.766  1.00 35.51 ? 42   ASP B N     1 
ATOM   4379 C CA    . ASP B 1 42  ? -25.699 -38.510 -4.867  1.00 34.19 ? 42   ASP B CA    1 
ATOM   4380 C C     . ASP B 1 42  ? -26.075 -39.902 -5.364  1.00 35.82 ? 42   ASP B C     1 
ATOM   4381 O O     . ASP B 1 42  ? -27.247 -40.230 -5.453  1.00 34.58 ? 42   ASP B O     1 
ATOM   4382 C CB    . ASP B 1 42  ? -26.130 -38.255 -3.428  1.00 33.63 ? 42   ASP B CB    1 
ATOM   4383 C CG    . ASP B 1 42  ? -25.507 -39.197 -2.404  1.00 32.09 ? 42   ASP B CG    1 
ATOM   4384 O OD1   . ASP B 1 42  ? -24.735 -40.081 -2.791  1.00 33.02 ? 42   ASP B OD1   1 
ATOM   4385 O OD2   . ASP B 1 42  ? -25.822 -39.029 -1.218  1.00 33.06 ? 42   ASP B OD2   1 
ATOM   4386 N N     . PRO B 1 43  ? -25.119 -40.776 -5.730  1.00 39.53 ? 43   PRO B N     1 
ATOM   4387 C CA    . PRO B 1 43  ? -25.479 -42.129 -6.160  1.00 39.51 ? 43   PRO B CA    1 
ATOM   4388 C C     . PRO B 1 43  ? -25.963 -43.010 -4.999  1.00 40.67 ? 43   PRO B C     1 
ATOM   4389 O O     . PRO B 1 43  ? -26.616 -43.995 -5.243  1.00 39.04 ? 43   PRO B O     1 
ATOM   4390 C CB    . PRO B 1 43  ? -24.162 -42.684 -6.709  1.00 39.29 ? 43   PRO B CB    1 
ATOM   4391 C CG    . PRO B 1 43  ? -23.103 -41.928 -5.914  1.00 39.58 ? 43   PRO B CG    1 
ATOM   4392 C CD    . PRO B 1 43  ? -23.672 -40.534 -5.733  1.00 37.25 ? 43   PRO B CD    1 
ATOM   4393 N N     . TYR B 1 44  ? -25.599 -42.663 -3.760  1.00 38.40 ? 44   TYR B N     1 
ATOM   4394 C CA    . TYR B 1 44  ? -25.883 -43.489 -2.561  1.00 36.81 ? 44   TYR B CA    1 
ATOM   4395 C C     . TYR B 1 44  ? -26.658 -42.639 -1.562  1.00 38.61 ? 44   TYR B C     1 
ATOM   4396 O O     . TYR B 1 44  ? -26.204 -42.452 -0.433  1.00 37.30 ? 44   TYR B O     1 
ATOM   4397 C CB    . TYR B 1 44  ? -24.584 -44.037 -1.960  1.00 35.34 ? 44   TYR B CB    1 
ATOM   4398 C CG    . TYR B 1 44  ? -23.658 -44.779 -2.895  1.00 35.55 ? 44   TYR B CG    1 
ATOM   4399 C CD1   . TYR B 1 44  ? -24.126 -45.495 -3.996  1.00 34.12 ? 44   TYR B CD1   1 
ATOM   4400 C CD2   . TYR B 1 44  ? -22.299 -44.830 -2.627  1.00 32.64 ? 44   TYR B CD2   1 
ATOM   4401 C CE1   . TYR B 1 44  ? -23.254 -46.172 -4.838  1.00 32.18 ? 44   TYR B CE1   1 
ATOM   4402 C CE2   . TYR B 1 44  ? -21.419 -45.527 -3.435  1.00 32.73 ? 44   TYR B CE2   1 
ATOM   4403 C CZ    . TYR B 1 44  ? -21.897 -46.193 -4.550  1.00 34.90 ? 44   TYR B CZ    1 
ATOM   4404 O OH    . TYR B 1 44  ? -21.024 -46.868 -5.348  1.00 34.77 ? 44   TYR B OH    1 
ATOM   4405 N N     . PRO B 1 45  ? -27.844 -42.101 -1.949  1.00 38.07 ? 45   PRO B N     1 
ATOM   4406 C CA    . PRO B 1 45  ? -28.625 -41.237 -1.066  1.00 37.85 ? 45   PRO B CA    1 
ATOM   4407 C C     . PRO B 1 45  ? -29.101 -41.983 0.187   1.00 39.12 ? 45   PRO B C     1 
ATOM   4408 O O     . PRO B 1 45  ? -29.426 -43.130 0.103   1.00 36.47 ? 45   PRO B O     1 
ATOM   4409 C CB    . PRO B 1 45  ? -29.822 -40.814 -1.931  1.00 36.63 ? 45   PRO B CB    1 
ATOM   4410 C CG    . PRO B 1 45  ? -29.980 -41.957 -2.902  1.00 36.08 ? 45   PRO B CG    1 
ATOM   4411 C CD    . PRO B 1 45  ? -28.557 -42.376 -3.214  1.00 36.89 ? 45   PRO B CD    1 
ATOM   4412 N N     . VAL B 1 46  ? -29.057 -41.313 1.331   1.00 43.60 ? 46   VAL B N     1 
ATOM   4413 C CA    . VAL B 1 46  ? -29.530 -41.866 2.630   1.00 44.31 ? 46   VAL B CA    1 
ATOM   4414 C C     . VAL B 1 46  ? -30.755 -41.047 3.017   1.00 45.06 ? 46   VAL B C     1 
ATOM   4415 O O     . VAL B 1 46  ? -30.763 -39.840 2.734   1.00 44.94 ? 46   VAL B O     1 
ATOM   4416 C CB    . VAL B 1 46  ? -28.456 -41.834 3.729   1.00 44.83 ? 46   VAL B CB    1 
ATOM   4417 C CG1   . VAL B 1 46  ? -27.399 -42.906 3.511   1.00 45.35 ? 46   VAL B CG1   1 
ATOM   4418 C CG2   . VAL B 1 46  ? -27.819 -40.462 3.874   1.00 46.30 ? 46   VAL B CG2   1 
ATOM   4419 N N     . GLY B 1 47  ? -31.776 -41.673 3.597   1.00 48.13 ? 47   GLY B N     1 
ATOM   4420 C CA    . GLY B 1 47  ? -33.088 -41.015 3.748   1.00 53.28 ? 47   GLY B CA    1 
ATOM   4421 C C     . GLY B 1 47  ? -33.622 -40.608 2.381   1.00 53.99 ? 47   GLY B C     1 
ATOM   4422 O O     . GLY B 1 47  ? -33.541 -41.439 1.479   1.00 48.26 ? 47   GLY B O     1 
ATOM   4423 N N     . ASP B 1 48  ? -34.056 -39.357 2.210   1.00 50.97 ? 48   ASP B N     1 
ATOM   4424 C CA    . ASP B 1 48  ? -34.752 -38.906 0.972   1.00 54.24 ? 48   ASP B CA    1 
ATOM   4425 C C     . ASP B 1 48  ? -33.739 -38.806 -0.177  1.00 55.97 ? 48   ASP B C     1 
ATOM   4426 O O     . ASP B 1 48  ? -32.743 -38.084 -0.023  1.00 57.19 ? 48   ASP B O     1 
ATOM   4427 C CB    . ASP B 1 48  ? -35.479 -37.579 1.208   1.00 54.44 ? 48   ASP B CB    1 
ATOM   4428 N N     . ALA B 1 49  ? -33.987 -39.495 -1.293  1.00 51.21 ? 49   ALA B N     1 
ATOM   4429 C CA    . ALA B 1 49  ? -33.123 -39.446 -2.497  1.00 55.17 ? 49   ALA B CA    1 
ATOM   4430 C C     . ALA B 1 49  ? -33.095 -38.022 -3.078  1.00 59.00 ? 49   ALA B C     1 
ATOM   4431 O O     . ALA B 1 49  ? -32.030 -37.636 -3.588  1.00 56.24 ? 49   ALA B O     1 
ATOM   4432 C CB    . ALA B 1 49  ? -33.563 -40.458 -3.525  1.00 50.31 ? 49   ALA B CB    1 
ATOM   4433 N N     . ASP B 1 50  ? -34.201 -37.271 -2.961  1.00 63.85 ? 50   ASP B N     1 
ATOM   4434 C CA    . ASP B 1 50  ? -34.414 -35.932 -3.589  1.00 63.22 ? 50   ASP B CA    1 
ATOM   4435 C C     . ASP B 1 50  ? -33.771 -34.803 -2.755  1.00 61.21 ? 50   ASP B C     1 
ATOM   4436 O O     . ASP B 1 50  ? -33.794 -33.634 -3.212  1.00 59.47 ? 50   ASP B O     1 
ATOM   4437 C CB    . ASP B 1 50  ? -35.905 -35.617 -3.732  1.00 67.42 ? 50   ASP B CB    1 
ATOM   4438 C CG    . ASP B 1 50  ? -36.362 -34.601 -2.693  1.00 78.93 ? 50   ASP B CG    1 
ATOM   4439 O OD1   . ASP B 1 50  ? -36.125 -34.852 -1.483  1.00 83.68 ? 50   ASP B OD1   1 
ATOM   4440 O OD2   . ASP B 1 50  ? -36.890 -33.539 -3.099  1.00 83.10 ? 50   ASP B OD2   1 
ATOM   4441 N N     . ALA B 1 51  ? -33.275 -35.081 -1.540  1.00 53.31 ? 51   ALA B N     1 
ATOM   4442 C CA    . ALA B 1 51  ? -32.476 -34.093 -0.773  1.00 51.24 ? 51   ALA B CA    1 
ATOM   4443 C C     . ALA B 1 51  ? -31.177 -33.858 -1.556  1.00 50.01 ? 51   ALA B C     1 
ATOM   4444 O O     . ALA B 1 51  ? -30.792 -34.757 -2.347  1.00 64.76 ? 51   ALA B O     1 
ATOM   4445 C CB    . ALA B 1 51  ? -32.208 -34.584 0.626   1.00 46.05 ? 51   ALA B CB    1 
ATOM   4446 N N     . HIS B 1 52  ? -30.545 -32.705 -1.395  1.00 52.07 ? 52   HIS B N     1 
ATOM   4447 C CA    . HIS B 1 52  ? -29.226 -32.398 -2.022  1.00 44.93 ? 52   HIS B CA    1 
ATOM   4448 C C     . HIS B 1 52  ? -29.300 -32.425 -3.562  1.00 44.25 ? 52   HIS B C     1 
ATOM   4449 O O     . HIS B 1 52  ? -28.598 -33.251 -4.187  1.00 43.87 ? 52   HIS B O     1 
ATOM   4450 C CB    . HIS B 1 52  ? -28.186 -33.355 -1.437  1.00 42.04 ? 52   HIS B CB    1 
ATOM   4451 C CG    . HIS B 1 52  ? -28.297 -33.371 0.041   1.00 36.57 ? 52   HIS B CG    1 
ATOM   4452 N ND1   . HIS B 1 52  ? -28.723 -34.480 0.742   1.00 42.11 ? 52   HIS B ND1   1 
ATOM   4453 C CD2   . HIS B 1 52  ? -28.159 -32.385 0.938   1.00 36.04 ? 52   HIS B CD2   1 
ATOM   4454 C CE1   . HIS B 1 52  ? -28.783 -34.189 2.024   1.00 39.22 ? 52   HIS B CE1   1 
ATOM   4455 N NE2   . HIS B 1 52  ? -28.428 -32.915 2.175   1.00 37.68 ? 52   HIS B NE2   1 
ATOM   4456 N N     . LEU B 1 53  ? -30.086 -31.518 -4.150  1.00 40.74 ? 53   LEU B N     1 
ATOM   4457 C CA    . LEU B 1 53  ? -30.149 -31.296 -5.620  1.00 39.99 ? 53   LEU B CA    1 
ATOM   4458 C C     . LEU B 1 53  ? -29.303 -30.077 -5.967  1.00 37.09 ? 53   LEU B C     1 
ATOM   4459 O O     . LEU B 1 53  ? -29.182 -29.182 -5.132  1.00 38.20 ? 53   LEU B O     1 
ATOM   4460 C CB    . LEU B 1 53  ? -31.598 -31.043 -6.054  1.00 44.49 ? 53   LEU B CB    1 
ATOM   4461 C CG    . LEU B 1 53  ? -32.589 -32.173 -5.800  1.00 47.89 ? 53   LEU B CG    1 
ATOM   4462 C CD1   . LEU B 1 53  ? -34.009 -31.706 -6.117  1.00 49.57 ? 53   LEU B CD1   1 
ATOM   4463 C CD2   . LEU B 1 53  ? -32.215 -33.396 -6.623  1.00 46.73 ? 53   LEU B CD2   1 
ATOM   4464 N N     . ALA B 1 54  ? -28.784 -30.033 -7.185  1.00 38.20 ? 54   ALA B N     1 
ATOM   4465 C CA    . ALA B 1 54  ? -28.064 -28.875 -7.743  1.00 38.09 ? 54   ALA B CA    1 
ATOM   4466 C C     . ALA B 1 54  ? -29.047 -28.109 -8.630  1.00 39.38 ? 54   ALA B C     1 
ATOM   4467 O O     . ALA B 1 54  ? -29.852 -28.794 -9.303  1.00 37.48 ? 54   ALA B O     1 
ATOM   4468 C CB    . ALA B 1 54  ? -26.868 -29.365 -8.518  1.00 39.75 ? 54   ALA B CB    1 
ATOM   4469 N N     . SER B 1 55  ? -28.984 -26.777 -8.625  1.00 36.91 ? 55   SER B N     1 
ATOM   4470 C CA    . SER B 1 55  ? -29.791 -25.888 -9.503  1.00 38.60 ? 55   SER B CA    1 
ATOM   4471 C C     . SER B 1 55  ? -29.057 -25.678 -10.832 1.00 39.66 ? 55   SER B C     1 
ATOM   4472 O O     . SER B 1 55  ? -29.701 -25.365 -11.843 1.00 38.20 ? 55   SER B O     1 
ATOM   4473 C CB    . SER B 1 55  ? -30.115 -24.579 -8.824  1.00 39.67 ? 55   SER B CB    1 
ATOM   4474 O OG    . SER B 1 55  ? -28.936 -23.853 -8.504  1.00 46.63 ? 55   SER B OG    1 
ATOM   4475 N N     . ALA B 1 56  ? -27.744 -25.864 -10.845 1.00 36.37 ? 56   ALA B N     1 
ATOM   4476 C CA    . ALA B 1 56  ? -26.898 -25.665 -12.038 1.00 33.00 ? 56   ALA B CA    1 
ATOM   4477 C C     . ALA B 1 56  ? -25.499 -26.187 -11.730 1.00 34.89 ? 56   ALA B C     1 
ATOM   4478 O O     . ALA B 1 56  ? -25.175 -26.358 -10.539 1.00 33.10 ? 56   ALA B O     1 
ATOM   4479 C CB    . ALA B 1 56  ? -26.866 -24.199 -12.412 1.00 34.76 ? 56   ALA B CB    1 
ATOM   4480 N N     . VAL B 1 57  ? -24.713 -26.418 -12.775 1.00 33.94 ? 57   VAL B N     1 
ATOM   4481 C CA    . VAL B 1 57  ? -23.281 -26.792 -12.670 1.00 34.51 ? 57   VAL B CA    1 
ATOM   4482 C C     . VAL B 1 57  ? -22.501 -25.833 -13.572 1.00 36.91 ? 57   VAL B C     1 
ATOM   4483 O O     . VAL B 1 57  ? -22.858 -25.697 -14.753 1.00 36.34 ? 57   VAL B O     1 
ATOM   4484 C CB    . VAL B 1 57  ? -23.031 -28.272 -13.012 1.00 36.68 ? 57   VAL B CB    1 
ATOM   4485 C CG1   . VAL B 1 57  ? -21.565 -28.639 -12.826 1.00 38.38 ? 57   VAL B CG1   1 
ATOM   4486 C CG2   . VAL B 1 57  ? -23.912 -29.208 -12.196 1.00 36.42 ? 57   VAL B CG2   1 
ATOM   4487 N N     . ILE B 1 58  ? -21.510 -25.162 -12.994 1.00 31.73 ? 58   ILE B N     1 
ATOM   4488 C CA    . ILE B 1 58  ? -20.646 -24.155 -13.662 1.00 36.33 ? 58   ILE B CA    1 
ATOM   4489 C C     . ILE B 1 58  ? -19.242 -24.741 -13.716 1.00 35.56 ? 58   ILE B C     1 
ATOM   4490 O O     . ILE B 1 58  ? -18.727 -25.159 -12.640 1.00 30.64 ? 58   ILE B O     1 
ATOM   4491 C CB    . ILE B 1 58  ? -20.647 -22.818 -12.887 1.00 40.43 ? 58   ILE B CB    1 
ATOM   4492 C CG1   . ILE B 1 58  ? -22.050 -22.353 -12.503 1.00 42.98 ? 58   ILE B CG1   1 
ATOM   4493 C CG2   . ILE B 1 58  ? -19.900 -21.763 -13.675 1.00 42.57 ? 58   ILE B CG2   1 
ATOM   4494 C CD1   . ILE B 1 58  ? -23.000 -22.217 -13.661 1.00 45.40 ? 58   ILE B CD1   1 
ATOM   4495 N N     . SER B 1 59  ? -18.612 -24.733 -14.888 1.00 35.34 ? 59   SER B N     1 
ATOM   4496 C CA    . SER B 1 59  ? -17.245 -25.294 -15.067 1.00 33.50 ? 59   SER B CA    1 
ATOM   4497 C C     . SER B 1 59  ? -16.306 -24.179 -15.482 1.00 33.80 ? 59   SER B C     1 
ATOM   4498 O O     . SER B 1 59  ? -16.163 -23.891 -16.671 1.00 31.53 ? 59   SER B O     1 
ATOM   4499 C CB    . SER B 1 59  ? -17.220 -26.436 -16.037 1.00 31.89 ? 59   SER B CB    1 
ATOM   4500 O OG    . SER B 1 59  ? -18.048 -27.474 -15.584 1.00 28.36 ? 59   SER B OG    1 
ATOM   4501 N N     . PRO B 1 60  ? -15.645 -23.519 -14.506 1.00 32.61 ? 60   PRO B N     1 
ATOM   4502 C CA    . PRO B 1 60  ? -14.696 -22.445 -14.820 1.00 30.24 ? 60   PRO B CA    1 
ATOM   4503 C C     . PRO B 1 60  ? -13.430 -23.009 -15.476 1.00 29.98 ? 60   PRO B C     1 
ATOM   4504 O O     . PRO B 1 60  ? -13.038 -24.148 -15.237 1.00 30.91 ? 60   PRO B O     1 
ATOM   4505 C CB    . PRO B 1 60  ? -14.480 -21.727 -13.481 1.00 32.31 ? 60   PRO B CB    1 
ATOM   4506 C CG    . PRO B 1 60  ? -14.832 -22.760 -12.438 1.00 35.79 ? 60   PRO B CG    1 
ATOM   4507 C CD    . PRO B 1 60  ? -15.828 -23.713 -13.063 1.00 33.32 ? 60   PRO B CD    1 
ATOM   4508 N N     . ARG B 1 61  ? -12.874 -22.248 -16.415 1.00 31.30 ? 61   ARG B N     1 
ATOM   4509 C CA    . ARG B 1 61  ? -11.677 -22.668 -17.182 1.00 32.70 ? 61   ARG B CA    1 
ATOM   4510 C C     . ARG B 1 61  ? -10.420 -22.570 -16.311 1.00 31.15 ? 61   ARG B C     1 
ATOM   4511 O O     . ARG B 1 61  ? -9.506  -23.407 -16.515 1.00 31.84 ? 61   ARG B O     1 
ATOM   4512 C CB    . ARG B 1 61  ? -11.458 -21.743 -18.378 1.00 32.71 ? 61   ARG B CB    1 
ATOM   4513 C CG    . ARG B 1 61  ? -10.309 -22.169 -19.271 1.00 35.33 ? 61   ARG B CG    1 
ATOM   4514 C CD    . ARG B 1 61  ? -10.284 -21.209 -20.441 1.00 37.40 ? 61   ARG B CD    1 
ATOM   4515 N NE    . ARG B 1 61  ? -9.913  -19.873 -19.993 1.00 38.30 ? 61   ARG B NE    1 
ATOM   4516 C CZ    . ARG B 1 61  ? -10.154 -18.746 -20.653 1.00 41.96 ? 61   ARG B CZ    1 
ATOM   4517 N NH1   . ARG B 1 61  ? -10.761 -18.772 -21.825 1.00 43.87 ? 61   ARG B NH1   1 
ATOM   4518 N NH2   . ARG B 1 61  ? -9.750  -17.594 -20.156 1.00 42.61 ? 61   ARG B NH2   1 
ATOM   4519 N N     . ASP B 1 62  ? -10.361 -21.590 -15.407 1.00 31.89 ? 62   ASP B N     1 
ATOM   4520 C CA    . ASP B 1 62  ? -9.107  -21.240 -14.679 1.00 30.62 ? 62   ASP B CA    1 
ATOM   4521 C C     . ASP B 1 62  ? -9.427  -20.395 -13.442 1.00 29.99 ? 62   ASP B C     1 
ATOM   4522 O O     . ASP B 1 62  ? -10.614 -20.035 -13.250 1.00 26.35 ? 62   ASP B O     1 
ATOM   4523 C CB    . ASP B 1 62  ? -8.142  -20.490 -15.601 1.00 27.41 ? 62   ASP B CB    1 
ATOM   4524 C CG    . ASP B 1 62  ? -8.785  -19.340 -16.366 1.00 31.22 ? 62   ASP B CG    1 
ATOM   4525 O OD1   . ASP B 1 62  ? -9.623  -18.598 -15.781 1.00 29.46 ? 62   ASP B OD1   1 
ATOM   4526 O OD2   . ASP B 1 62  ? -8.432  -19.176 -17.558 1.00 32.94 ? 62   ASP B OD2   1 
ATOM   4527 N N     . THR B 1 63  ? -8.393  -20.082 -12.644 1.00 28.53 ? 63   THR B N     1 
ATOM   4528 C CA    . THR B 1 63  ? -8.505  -19.275 -11.405 1.00 27.25 ? 63   THR B CA    1 
ATOM   4529 C C     . THR B 1 63  ? -9.296  -17.979 -11.674 1.00 30.92 ? 63   THR B C     1 
ATOM   4530 O O     . THR B 1 63  ? -10.205 -17.633 -10.870 1.00 26.38 ? 63   THR B O     1 
ATOM   4531 C CB    . THR B 1 63  ? -7.112  -18.982 -10.841 1.00 28.14 ? 63   THR B CB    1 
ATOM   4532 O OG1   . THR B 1 63  ? -6.495  -20.250 -10.596 1.00 29.33 ? 63   THR B OG1   1 
ATOM   4533 C CG2   . THR B 1 63  ? -7.165  -18.137 -9.580  1.00 27.88 ? 63   THR B CG2   1 
ATOM   4534 N N     . GLU B 1 64  ? -8.968  -17.260 -12.761 1.00 26.25 ? 64   GLU B N     1 
ATOM   4535 C CA    . GLU B 1 64  ? -9.590  -15.953 -13.055 1.00 29.54 ? 64   GLU B CA    1 
ATOM   4536 C C     . GLU B 1 64  ? -11.108 -16.149 -13.196 1.00 26.75 ? 64   GLU B C     1 
ATOM   4537 O O     . GLU B 1 64  ? -11.851 -15.315 -12.685 1.00 26.11 ? 64   GLU B O     1 
ATOM   4538 C CB    . GLU B 1 64  ? -8.930  -15.338 -14.292 1.00 30.99 ? 64   GLU B CB    1 
ATOM   4539 C CG    . GLU B 1 64  ? -7.456  -14.990 -14.077 1.00 32.98 ? 64   GLU B CG    1 
ATOM   4540 C CD    . GLU B 1 64  ? -6.385  -16.078 -14.234 1.00 31.95 ? 64   GLU B CD    1 
ATOM   4541 O OE1   . GLU B 1 64  ? -6.712  -17.302 -14.405 1.00 28.70 ? 64   GLU B OE1   1 
ATOM   4542 O OE2   . GLU B 1 64  ? -5.178  -15.698 -14.160 1.00 36.74 ? 64   GLU B OE2   1 
ATOM   4543 N N     . GLN B 1 65  ? -11.543 -17.204 -13.883 1.00 29.15 ? 65   GLN B N     1 
ATOM   4544 C CA    . GLN B 1 65  ? -12.990 -17.494 -14.076 1.00 28.34 ? 65   GLN B CA    1 
ATOM   4545 C C     . GLN B 1 65  ? -13.618 -17.884 -12.738 1.00 27.89 ? 65   GLN B C     1 
ATOM   4546 O O     . GLN B 1 65  ? -14.752 -17.442 -12.476 1.00 27.65 ? 65   GLN B O     1 
ATOM   4547 C CB    . GLN B 1 65  ? -13.218 -18.540 -15.167 1.00 25.39 ? 65   GLN B CB    1 
ATOM   4548 C CG    . GLN B 1 65  ? -13.014 -17.937 -16.549 1.00 29.13 ? 65   GLN B CG    1 
ATOM   4549 C CD    . GLN B 1 65  ? -13.435 -18.857 -17.662 1.00 29.63 ? 65   GLN B CD    1 
ATOM   4550 O OE1   . GLN B 1 65  ? -14.066 -19.884 -17.415 1.00 29.80 ? 65   GLN B OE1   1 
ATOM   4551 N NE2   . GLN B 1 65  ? -13.082 -18.497 -18.902 1.00 29.24 ? 65   GLN B NE2   1 
ATOM   4552 N N     . VAL B 1 66  ? -12.899 -18.613 -11.889 1.00 30.10 ? 66   VAL B N     1 
ATOM   4553 C CA    . VAL B 1 66  ? -13.426 -18.965 -10.532 1.00 25.94 ? 66   VAL B CA    1 
ATOM   4554 C C     . VAL B 1 66  ? -13.702 -17.658 -9.785  1.00 27.41 ? 66   VAL B C     1 
ATOM   4555 O O     . VAL B 1 66  ? -14.792 -17.510 -9.209  1.00 28.56 ? 66   VAL B O     1 
ATOM   4556 C CB    . VAL B 1 66  ? -12.472 -19.881 -9.747  1.00 26.74 ? 66   VAL B CB    1 
ATOM   4557 C CG1   . VAL B 1 66  ? -12.978 -20.117 -8.321  1.00 27.66 ? 66   VAL B CG1   1 
ATOM   4558 C CG2   . VAL B 1 66  ? -12.226 -21.216 -10.436 1.00 28.16 ? 66   VAL B CG2   1 
ATOM   4559 N N     . GLN B 1 67  ? -12.755 -16.724 -9.794  1.00 28.28 ? 67   GLN B N     1 
ATOM   4560 C CA    . GLN B 1 67  ? -12.932 -15.423 -9.104  1.00 29.75 ? 67   GLN B CA    1 
ATOM   4561 C C     . GLN B 1 67  ? -14.170 -14.714 -9.660  1.00 31.02 ? 67   GLN B C     1 
ATOM   4562 O O     . GLN B 1 67  ? -14.973 -14.222 -8.868  1.00 27.76 ? 67   GLN B O     1 
ATOM   4563 C CB    . GLN B 1 67  ? -11.712 -14.546 -9.283  1.00 29.08 ? 67   GLN B CB    1 
ATOM   4564 C CG    . GLN B 1 67  ? -10.481 -15.116 -8.607  1.00 27.72 ? 67   GLN B CG    1 
ATOM   4565 C CD    . GLN B 1 67  ? -9.341  -14.176 -8.862  1.00 25.37 ? 67   GLN B CD    1 
ATOM   4566 O OE1   . GLN B 1 67  ? -8.608  -14.359 -9.829  1.00 29.57 ? 67   GLN B OE1   1 
ATOM   4567 N NE2   . GLN B 1 67  ? -9.243  -13.135 -8.032  1.00 24.42 ? 67   GLN B NE2   1 
ATOM   4568 N N     . GLU B 1 68  ? -14.347 -14.698 -10.973 1.00 33.76 ? 68   GLU B N     1 
ATOM   4569 C CA    . GLU B 1 68  ? -15.484 -13.944 -11.565 1.00 35.54 ? 68   GLU B CA    1 
ATOM   4570 C C     . GLU B 1 68  ? -16.797 -14.670 -11.252 1.00 32.30 ? 68   GLU B C     1 
ATOM   4571 O O     . GLU B 1 68  ? -17.753 -13.975 -10.899 1.00 34.32 ? 68   GLU B O     1 
ATOM   4572 C CB    . GLU B 1 68  ? -15.267 -13.685 -13.053 1.00 41.78 ? 68   GLU B CB    1 
ATOM   4573 C CG    . GLU B 1 68  ? -16.094 -12.507 -13.574 1.00 49.62 ? 68   GLU B CG    1 
ATOM   4574 C CD    . GLU B 1 68  ? -16.204 -11.265 -12.684 1.00 54.71 ? 68   GLU B CD    1 
ATOM   4575 O OE1   . GLU B 1 68  ? -15.180 -10.796 -12.141 1.00 58.02 ? 68   GLU B OE1   1 
ATOM   4576 O OE2   . GLU B 1 68  ? -17.329 -10.751 -12.539 1.00 55.65 ? 68   GLU B OE2   1 
ATOM   4577 N N     . VAL B 1 69  ? -16.845 -16.003 -11.269 1.00 32.90 ? 69   VAL B N     1 
ATOM   4578 C CA    . VAL B 1 69  ? -18.114 -16.713 -10.912 1.00 32.86 ? 69   VAL B CA    1 
ATOM   4579 C C     . VAL B 1 69  ? -18.400 -16.464 -9.433  1.00 32.49 ? 69   VAL B C     1 
ATOM   4580 O O     . VAL B 1 69  ? -19.582 -16.282 -9.102  1.00 31.18 ? 69   VAL B O     1 
ATOM   4581 C CB    . VAL B 1 69  ? -18.175 -18.211 -11.272 1.00 35.80 ? 69   VAL B CB    1 
ATOM   4582 C CG1   . VAL B 1 69  ? -17.994 -18.455 -12.758 1.00 34.35 ? 69   VAL B CG1   1 
ATOM   4583 C CG2   . VAL B 1 69  ? -17.227 -19.069 -10.473 1.00 43.41 ? 69   VAL B CG2   1 
ATOM   4584 N N     . VAL B 1 70  ? -17.372 -16.385 -8.586  1.00 29.74 ? 70   VAL B N     1 
ATOM   4585 C CA    . VAL B 1 70  ? -17.588 -16.106 -7.136  1.00 28.95 ? 70   VAL B CA    1 
ATOM   4586 C C     . VAL B 1 70  ? -18.120 -14.678 -6.975  1.00 28.01 ? 70   VAL B C     1 
ATOM   4587 O O     . VAL B 1 70  ? -19.074 -14.492 -6.212  1.00 28.39 ? 70   VAL B O     1 
ATOM   4588 C CB    . VAL B 1 70  ? -16.328 -16.388 -6.295  1.00 25.36 ? 70   VAL B CB    1 
ATOM   4589 C CG1   . VAL B 1 70  ? -16.475 -15.871 -4.868  1.00 26.49 ? 70   VAL B CG1   1 
ATOM   4590 C CG2   . VAL B 1 70  ? -16.003 -17.868 -6.292  1.00 25.26 ? 70   VAL B CG2   1 
ATOM   4591 N N     . ARG B 1 71  ? -17.562 -13.692 -7.676  1.00 29.23 ? 71   ARG B N     1 
ATOM   4592 C CA    . ARG B 1 71  ? -18.071 -12.298 -7.611  1.00 31.35 ? 71   ARG B CA    1 
ATOM   4593 C C     . ARG B 1 71  ? -19.524 -12.246 -8.088  1.00 32.25 ? 71   ARG B C     1 
ATOM   4594 O O     . ARG B 1 71  ? -20.282 -11.496 -7.470  1.00 30.87 ? 71   ARG B O     1 
ATOM   4595 C CB    . ARG B 1 71  ? -17.222 -11.336 -8.436  1.00 32.63 ? 71   ARG B CB    1 
ATOM   4596 C CG    . ARG B 1 71  ? -15.829 -11.150 -7.858  1.00 34.99 ? 71   ARG B CG    1 
ATOM   4597 C CD    . ARG B 1 71  ? -15.013 -10.179 -8.654  1.00 37.15 ? 71   ARG B CD    1 
ATOM   4598 N NE    . ARG B 1 71  ? -13.605 -10.314 -8.337  1.00 37.99 ? 71   ARG B NE    1 
ATOM   4599 C CZ    . ARG B 1 71  ? -12.666 -10.690 -9.192  1.00 38.67 ? 71   ARG B CZ    1 
ATOM   4600 N NH1   . ARG B 1 71  ? -12.972 -11.019 -10.435 1.00 37.99 ? 71   ARG B NH1   1 
ATOM   4601 N NH2   . ARG B 1 71  ? -11.409 -10.735 -8.799  1.00 40.97 ? 71   ARG B NH2   1 
ATOM   4602 N N     . ILE B 1 72  ? -19.891 -12.996 -9.125  1.00 32.22 ? 72   ILE B N     1 
ATOM   4603 C CA    . ILE B 1 72  ? -21.282 -12.985 -9.658  1.00 34.26 ? 72   ILE B CA    1 
ATOM   4604 C C     . ILE B 1 72  ? -22.188 -13.582 -8.579  1.00 36.92 ? 72   ILE B C     1 
ATOM   4605 O O     . ILE B 1 72  ? -23.224 -12.984 -8.280  1.00 32.48 ? 72   ILE B O     1 
ATOM   4606 C CB    . ILE B 1 72  ? -21.370 -13.746 -10.996 1.00 38.00 ? 72   ILE B CB    1 
ATOM   4607 C CG1   . ILE B 1 72  ? -20.684 -12.957 -12.114 1.00 34.46 ? 72   ILE B CG1   1 
ATOM   4608 C CG2   . ILE B 1 72  ? -22.811 -14.086 -11.360 1.00 39.42 ? 72   ILE B CG2   1 
ATOM   4609 C CD1   . ILE B 1 72  ? -20.296 -13.807 -13.299 1.00 33.90 ? 72   ILE B CD1   1 
ATOM   4610 N N     . ALA B 1 73  ? -21.783 -14.709 -7.994  1.00 32.89 ? 73   ALA B N     1 
ATOM   4611 C CA    . ALA B 1 73  ? -22.510 -15.364 -6.889  1.00 32.94 ? 73   ALA B CA    1 
ATOM   4612 C C     . ALA B 1 73  ? -22.743 -14.363 -5.755  1.00 31.18 ? 73   ALA B C     1 
ATOM   4613 O O     . ALA B 1 73  ? -23.848 -14.361 -5.186  1.00 31.82 ? 73   ALA B O     1 
ATOM   4614 C CB    . ALA B 1 73  ? -21.744 -16.591 -6.429  1.00 34.41 ? 73   ALA B CB    1 
ATOM   4615 N N     . ASN B 1 74  ? -21.745 -13.549 -5.418  1.00 31.48 ? 74   ASN B N     1 
ATOM   4616 C CA    . ASN B 1 74  ? -21.849 -12.562 -4.310  1.00 31.93 ? 74   ASN B CA    1 
ATOM   4617 C C     . ASN B 1 74  ? -22.879 -11.499 -4.702  1.00 36.14 ? 74   ASN B C     1 
ATOM   4618 O O     . ASN B 1 74  ? -23.646 -11.071 -3.846  1.00 32.78 ? 74   ASN B O     1 
ATOM   4619 C CB    . ASN B 1 74  ? -20.499 -11.911 -3.982  1.00 31.44 ? 74   ASN B CB    1 
ATOM   4620 C CG    . ASN B 1 74  ? -19.683 -12.721 -2.996  1.00 31.37 ? 74   ASN B CG    1 
ATOM   4621 O OD1   . ASN B 1 74  ? -19.727 -12.461 -1.785  1.00 31.33 ? 74   ASN B OD1   1 
ATOM   4622 N ND2   . ASN B 1 74  ? -18.993 -13.737 -3.503  1.00 29.29 ? 74   ASN B ND2   1 
ATOM   4623 N N     . ARG B 1 75  ? -22.885 -11.080 -5.965  1.00 38.78 ? 75   ARG B N     1 
ATOM   4624 C CA    . ARG B 1 75  ? -23.805 -10.008 -6.419  1.00 42.68 ? 75   ARG B CA    1 
ATOM   4625 C C     . ARG B 1 75  ? -25.243 -10.510 -6.253  1.00 39.56 ? 75   ARG B C     1 
ATOM   4626 O O     . ARG B 1 75  ? -26.046 -9.730  -5.802  1.00 36.31 ? 75   ARG B O     1 
ATOM   4627 C CB    . ARG B 1 75  ? -23.493 -9.589  -7.856  1.00 46.28 ? 75   ARG B CB    1 
ATOM   4628 C CG    . ARG B 1 75  ? -24.584 -8.755  -8.510  1.00 55.55 ? 75   ARG B CG    1 
ATOM   4629 C CD    . ARG B 1 75  ? -24.164 -8.308  -9.898  1.00 66.45 ? 75   ARG B CD    1 
ATOM   4630 N NE    . ARG B 1 75  ? -23.215 -7.212  -9.897  1.00 78.15 ? 75   ARG B NE    1 
ATOM   4631 C CZ    . ARG B 1 75  ? -23.536 -5.931  -9.759  1.00 83.57 ? 75   ARG B CZ    1 
ATOM   4632 N NH1   . ARG B 1 75  ? -24.799 -5.562  -9.600  1.00 82.58 ? 75   ARG B NH1   1 
ATOM   4633 N NH2   . ARG B 1 75  ? -22.580 -5.017  -9.779  1.00 86.01 ? 75   ARG B NH2   1 
ATOM   4634 N N     . TYR B 1 76  ? -25.545 -11.768 -6.581  1.00 37.23 ? 76   TYR B N     1 
ATOM   4635 C CA    . TYR B 1 76  ? -26.943 -12.269 -6.711  1.00 38.52 ? 76   TYR B CA    1 
ATOM   4636 C C     . TYR B 1 76  ? -27.340 -13.206 -5.568  1.00 39.77 ? 76   TYR B C     1 
ATOM   4637 O O     . TYR B 1 76  ? -28.467 -13.727 -5.614  1.00 39.22 ? 76   TYR B O     1 
ATOM   4638 C CB    . TYR B 1 76  ? -27.113 -12.932 -8.076  1.00 41.27 ? 76   TYR B CB    1 
ATOM   4639 C CG    . TYR B 1 76  ? -27.022 -11.932 -9.201  1.00 41.93 ? 76   TYR B CG    1 
ATOM   4640 C CD1   . TYR B 1 76  ? -27.964 -10.920 -9.336  1.00 47.64 ? 76   TYR B CD1   1 
ATOM   4641 C CD2   . TYR B 1 76  ? -25.991 -11.980 -10.119 1.00 43.16 ? 76   TYR B CD2   1 
ATOM   4642 C CE1   . TYR B 1 76  ? -27.897 -9.991  -10.366 1.00 47.91 ? 76   TYR B CE1   1 
ATOM   4643 C CE2   . TYR B 1 76  ? -25.911 -11.064 -11.156 1.00 43.65 ? 76   TYR B CE2   1 
ATOM   4644 C CZ    . TYR B 1 76  ? -26.863 -10.066 -11.281 1.00 44.94 ? 76   TYR B CZ    1 
ATOM   4645 O OH    . TYR B 1 76  ? -26.754 -9.158  -12.292 1.00 44.75 ? 76   TYR B OH    1 
ATOM   4646 N N     . GLY B 1 77  ? -26.472 -13.369 -4.563  1.00 39.01 ? 77   GLY B N     1 
ATOM   4647 C CA    . GLY B 1 77  ? -26.704 -14.255 -3.408  1.00 34.49 ? 77   GLY B CA    1 
ATOM   4648 C C     . GLY B 1 77  ? -26.844 -15.718 -3.809  1.00 33.98 ? 77   GLY B C     1 
ATOM   4649 O O     . GLY B 1 77  ? -27.615 -16.441 -3.147  1.00 33.34 ? 77   GLY B O     1 
ATOM   4650 N N     . ILE B 1 78  ? -26.116 -16.164 -4.837  1.00 33.29 ? 78   ILE B N     1 
ATOM   4651 C CA    . ILE B 1 78  ? -26.190 -17.570 -5.321  1.00 33.29 ? 78   ILE B CA    1 
ATOM   4652 C C     . ILE B 1 78  ? -25.271 -18.410 -4.440  1.00 32.95 ? 78   ILE B C     1 
ATOM   4653 O O     . ILE B 1 78  ? -24.057 -18.204 -4.446  1.00 30.59 ? 78   ILE B O     1 
ATOM   4654 C CB    . ILE B 1 78  ? -25.756 -17.718 -6.789  1.00 32.24 ? 78   ILE B CB    1 
ATOM   4655 C CG1   . ILE B 1 78  ? -26.477 -16.747 -7.728  1.00 35.02 ? 78   ILE B CG1   1 
ATOM   4656 C CG2   . ILE B 1 78  ? -25.900 -19.165 -7.222  1.00 32.90 ? 78   ILE B CG2   1 
ATOM   4657 C CD1   . ILE B 1 78  ? -27.980 -16.911 -7.774  1.00 34.17 ? 78   ILE B CD1   1 
ATOM   4658 N N     . PRO B 1 79  ? -25.801 -19.412 -3.720  1.00 32.62 ? 79   PRO B N     1 
ATOM   4659 C CA    . PRO B 1 79  ? -24.958 -20.320 -2.942  1.00 33.25 ? 79   PRO B CA    1 
ATOM   4660 C C     . PRO B 1 79  ? -24.201 -21.241 -3.907  1.00 33.98 ? 79   PRO B C     1 
ATOM   4661 O O     . PRO B 1 79  ? -24.805 -21.751 -4.865  1.00 34.02 ? 79   PRO B O     1 
ATOM   4662 C CB    . PRO B 1 79  ? -25.969 -21.074 -2.063  1.00 34.06 ? 79   PRO B CB    1 
ATOM   4663 C CG    . PRO B 1 79  ? -27.237 -21.089 -2.907  1.00 32.21 ? 79   PRO B CG    1 
ATOM   4664 C CD    . PRO B 1 79  ? -27.229 -19.755 -3.618  1.00 33.25 ? 79   PRO B CD    1 
ATOM   4665 N N     . LEU B 1 80  ? -22.900 -21.417 -3.702  1.00 29.63 ? 80   LEU B N     1 
ATOM   4666 C CA    . LEU B 1 80  ? -22.144 -22.334 -4.587  1.00 34.11 ? 80   LEU B CA    1 
ATOM   4667 C C     . LEU B 1 80  ? -21.375 -23.397 -3.800  1.00 32.04 ? 80   LEU B C     1 
ATOM   4668 O O     . LEU B 1 80  ? -20.625 -23.107 -2.862  1.00 35.50 ? 80   LEU B O     1 
ATOM   4669 C CB    . LEU B 1 80  ? -21.307 -21.575 -5.621  1.00 44.09 ? 80   LEU B CB    1 
ATOM   4670 C CG    . LEU B 1 80  ? -20.376 -20.480 -5.138  1.00 47.74 ? 80   LEU B CG    1 
ATOM   4671 C CD1   . LEU B 1 80  ? -19.070 -21.089 -4.653  1.00 57.64 ? 80   LEU B CD1   1 
ATOM   4672 C CD2   . LEU B 1 80  ? -20.095 -19.494 -6.256  1.00 39.20 ? 80   LEU B CD2   1 
ATOM   4673 N N     . SER B 1 81  ? -21.642 -24.629 -4.157  1.00 29.00 ? 81   SER B N     1 
ATOM   4674 C CA    . SER B 1 81  ? -20.943 -25.818 -3.628  1.00 28.95 ? 81   SER B CA    1 
ATOM   4675 C C     . SER B 1 81  ? -19.756 -26.084 -4.536  1.00 28.80 ? 81   SER B C     1 
ATOM   4676 O O     . SER B 1 81  ? -19.646 -25.400 -5.608  1.00 29.04 ? 81   SER B O     1 
ATOM   4677 C CB    . SER B 1 81  ? -21.878 -26.971 -3.554  1.00 28.69 ? 81   SER B CB    1 
ATOM   4678 O OG    . SER B 1 81  ? -22.293 -27.329 -4.855  1.00 27.17 ? 81   SER B OG    1 
ATOM   4679 N N     . VAL B 1 82  ? -18.910 -27.043 -4.169  1.00 28.00 ? 82   VAL B N     1 
ATOM   4680 C CA    . VAL B 1 82  ? -17.613 -27.223 -4.860  1.00 29.18 ? 82   VAL B CA    1 
ATOM   4681 C C     . VAL B 1 82  ? -17.321 -28.706 -5.034  1.00 27.41 ? 82   VAL B C     1 
ATOM   4682 O O     . VAL B 1 82  ? -17.428 -29.471 -4.065  1.00 28.43 ? 82   VAL B O     1 
ATOM   4683 C CB    . VAL B 1 82  ? -16.484 -26.503 -4.102  1.00 30.37 ? 82   VAL B CB    1 
ATOM   4684 C CG1   . VAL B 1 82  ? -15.301 -26.312 -5.008  1.00 31.06 ? 82   VAL B CG1   1 
ATOM   4685 C CG2   . VAL B 1 82  ? -16.943 -25.162 -3.535  1.00 34.26 ? 82   VAL B CG2   1 
ATOM   4686 N N     . ILE B 1 83  ? -16.900 -29.092 -6.229  1.00 25.79 ? 83   ILE B N     1 
ATOM   4687 C CA    . ILE B 1 83  ? -16.270 -30.420 -6.462  1.00 26.66 ? 83   ILE B CA    1 
ATOM   4688 C C     . ILE B 1 83  ? -14.947 -30.223 -7.201  1.00 26.31 ? 83   ILE B C     1 
ATOM   4689 O O     . ILE B 1 83  ? -14.747 -29.164 -7.821  1.00 27.30 ? 83   ILE B O     1 
ATOM   4690 C CB    . ILE B 1 83  ? -17.215 -31.377 -7.211  1.00 28.57 ? 83   ILE B CB    1 
ATOM   4691 C CG1   . ILE B 1 83  ? -17.519 -30.879 -8.627  1.00 29.31 ? 83   ILE B CG1   1 
ATOM   4692 C CG2   . ILE B 1 83  ? -18.478 -31.608 -6.383  1.00 28.29 ? 83   ILE B CG2   1 
ATOM   4693 C CD1   . ILE B 1 83  ? -18.061 -31.952 -9.529  1.00 31.36 ? 83   ILE B CD1   1 
ATOM   4694 N N     . SER B 1 84  ? -14.079 -31.202 -7.075  1.00 27.29 ? 84   SER B N     1 
ATOM   4695 C CA    . SER B 1 84  ? -12.925 -31.433 -7.975  1.00 29.07 ? 84   SER B CA    1 
ATOM   4696 C C     . SER B 1 84  ? -13.395 -32.433 -9.041  1.00 31.80 ? 84   SER B C     1 
ATOM   4697 O O     . SER B 1 84  ? -13.864 -31.987 -10.093 1.00 33.25 ? 84   SER B O     1 
ATOM   4698 C CB    . SER B 1 84  ? -11.725 -31.872 -7.171  1.00 26.72 ? 84   SER B CB    1 
ATOM   4699 O OG    . SER B 1 84  ? -11.302 -30.796 -6.332  1.00 26.67 ? 84   SER B OG    1 
ATOM   4700 N N     . THR B 1 85  ? -13.428 -33.720 -8.710  1.00 31.49 ? 85   THR B N     1 
ATOM   4701 C CA    . THR B 1 85  ? -13.975 -34.807 -9.562  1.00 31.05 ? 85   THR B CA    1 
ATOM   4702 C C     . THR B 1 85  ? -15.382 -35.185 -9.064  1.00 33.25 ? 85   THR B C     1 
ATOM   4703 O O     . THR B 1 85  ? -16.127 -35.801 -9.829  1.00 30.34 ? 85   THR B O     1 
ATOM   4704 C CB    . THR B 1 85  ? -12.963 -35.957 -9.608  1.00 34.38 ? 85   THR B CB    1 
ATOM   4705 O OG1   . THR B 1 85  ? -12.495 -36.246 -8.282  1.00 34.30 ? 85   THR B OG1   1 
ATOM   4706 C CG2   . THR B 1 85  ? -11.766 -35.636 -10.479 1.00 32.69 ? 85   THR B CG2   1 
ATOM   4707 N N     . GLY B 1 86  ? -15.758 -34.820 -7.835  1.00 30.25 ? 86   GLY B N     1 
ATOM   4708 C CA    . GLY B 1 86  ? -17.120 -35.052 -7.314  1.00 30.28 ? 86   GLY B CA    1 
ATOM   4709 C C     . GLY B 1 86  ? -17.411 -36.521 -7.096  1.00 31.31 ? 86   GLY B C     1 
ATOM   4710 O O     . GLY B 1 86  ? -18.587 -36.916 -7.221  1.00 30.91 ? 86   GLY B O     1 
ATOM   4711 N N     . ARG B 1 87  ? -16.398 -37.327 -6.781  1.00 32.12 ? 87   ARG B N     1 
ATOM   4712 C CA    . ARG B 1 87  ? -16.572 -38.778 -6.536  1.00 33.24 ? 87   ARG B CA    1 
ATOM   4713 C C     . ARG B 1 87  ? -16.601 -39.047 -5.031  1.00 29.93 ? 87   ARG B C     1 
ATOM   4714 O O     . ARG B 1 87  ? -16.164 -40.148 -4.646  1.00 33.55 ? 87   ARG B O     1 
ATOM   4715 C CB    . ARG B 1 87  ? -15.454 -39.589 -7.188  1.00 34.59 ? 87   ARG B CB    1 
ATOM   4716 C CG    . ARG B 1 87  ? -15.170 -39.229 -8.636  1.00 42.50 ? 87   ARG B CG    1 
ATOM   4717 C CD    . ARG B 1 87  ? -16.404 -39.082 -9.491  1.00 46.36 ? 87   ARG B CD    1 
ATOM   4718 N NE    . ARG B 1 87  ? -17.035 -40.353 -9.777  1.00 52.78 ? 87   ARG B NE    1 
ATOM   4719 C CZ    . ARG B 1 87  ? -16.743 -41.143 -10.808 1.00 54.95 ? 87   ARG B CZ    1 
ATOM   4720 N NH1   . ARG B 1 87  ? -15.778 -40.827 -11.654 1.00 53.18 ? 87   ARG B NH1   1 
ATOM   4721 N NH2   . ARG B 1 87  ? -17.411 -42.274 -10.971 1.00 54.04 ? 87   ARG B NH2   1 
ATOM   4722 N N     . ASN B 1 88  ? -17.151 -38.125 -4.228  1.00 27.85 ? 88   ASN B N     1 
ATOM   4723 C CA    . ASN B 1 88  ? -17.158 -38.244 -2.742  1.00 27.66 ? 88   ASN B CA    1 
ATOM   4724 C C     . ASN B 1 88  ? -18.262 -39.235 -2.317  1.00 27.79 ? 88   ASN B C     1 
ATOM   4725 O O     . ASN B 1 88  ? -19.063 -38.909 -1.439  1.00 29.09 ? 88   ASN B O     1 
ATOM   4726 C CB    . ASN B 1 88  ? -17.310 -36.883 -2.074  1.00 27.45 ? 88   ASN B CB    1 
ATOM   4727 C CG    . ASN B 1 88  ? -16.651 -36.814 -0.713  1.00 25.00 ? 88   ASN B CG    1 
ATOM   4728 O OD1   . ASN B 1 88  ? -15.814 -37.648 -0.393  1.00 28.25 ? 88   ASN B OD1   1 
ATOM   4729 N ND2   . ASN B 1 88  ? -17.018 -35.827 0.085   1.00 26.91 ? 88   ASN B ND2   1 
ATOM   4730 N N     . ASN B 1 89  ? -18.272 -40.417 -2.924  1.00 25.82 ? 89   ASN B N     1 
ATOM   4731 C CA    . ASN B 1 89  ? -19.307 -41.457 -2.745  1.00 27.76 ? 89   ASN B CA    1 
ATOM   4732 C C     . ASN B 1 89  ? -19.178 -42.015 -1.338  1.00 29.06 ? 89   ASN B C     1 
ATOM   4733 O O     . ASN B 1 89  ? -18.011 -42.304 -0.904  1.00 30.69 ? 89   ASN B O     1 
ATOM   4734 C CB    . ASN B 1 89  ? -19.164 -42.537 -3.801  1.00 29.41 ? 89   ASN B CB    1 
ATOM   4735 C CG    . ASN B 1 89  ? -19.419 -41.976 -5.181  1.00 32.28 ? 89   ASN B CG    1 
ATOM   4736 O OD1   . ASN B 1 89  ? -19.989 -40.886 -5.321  1.00 31.99 ? 89   ASN B OD1   1 
ATOM   4737 N ND2   . ASN B 1 89  ? -19.041 -42.735 -6.196  1.00 32.74 ? 89   ASN B ND2   1 
ATOM   4738 N N     . GLY B 1 90  ? -20.309 -42.120 -0.648  1.00 27.85 ? 90   GLY B N     1 
ATOM   4739 C CA    . GLY B 1 90  ? -20.369 -42.438 0.786   1.00 28.16 ? 90   GLY B CA    1 
ATOM   4740 C C     . GLY B 1 90  ? -20.567 -41.184 1.613   1.00 28.41 ? 90   GLY B C     1 
ATOM   4741 O O     . GLY B 1 90  ? -20.969 -41.315 2.794   1.00 32.89 ? 90   GLY B O     1 
ATOM   4742 N N     . TYR B 1 91  ? -20.310 -40.012 1.029   1.00 27.00 ? 91   TYR B N     1 
ATOM   4743 C CA    . TYR B 1 91  ? -20.404 -38.696 1.710   1.00 27.79 ? 91   TYR B CA    1 
ATOM   4744 C C     . TYR B 1 91  ? -21.286 -37.710 0.937   1.00 29.03 ? 91   TYR B C     1 
ATOM   4745 O O     . TYR B 1 91  ? -21.428 -36.544 1.394   1.00 30.46 ? 91   TYR B O     1 
ATOM   4746 C CB    . TYR B 1 91  ? -19.006 -38.130 1.952   1.00 27.71 ? 91   TYR B CB    1 
ATOM   4747 C CG    . TYR B 1 91  ? -18.151 -39.033 2.792   1.00 28.92 ? 91   TYR B CG    1 
ATOM   4748 C CD1   . TYR B 1 91  ? -18.544 -39.412 4.067   1.00 29.67 ? 91   TYR B CD1   1 
ATOM   4749 C CD2   . TYR B 1 91  ? -16.946 -39.501 2.315   1.00 31.35 ? 91   TYR B CD2   1 
ATOM   4750 C CE1   . TYR B 1 91  ? -17.749 -40.235 4.845   1.00 31.96 ? 91   TYR B CE1   1 
ATOM   4751 C CE2   . TYR B 1 91  ? -16.132 -40.303 3.086   1.00 32.12 ? 91   TYR B CE2   1 
ATOM   4752 C CZ    . TYR B 1 91  ? -16.531 -40.673 4.359   1.00 33.24 ? 91   TYR B CZ    1 
ATOM   4753 O OH    . TYR B 1 91  ? -15.709 -41.465 5.103   1.00 31.11 ? 91   TYR B OH    1 
ATOM   4754 N N     . GLY B 1 92  ? -21.903 -38.147 -0.173  1.00 29.19 ? 92   GLY B N     1 
ATOM   4755 C CA    . GLY B 1 92  ? -22.858 -37.324 -0.940  1.00 27.37 ? 92   GLY B CA    1 
ATOM   4756 C C     . GLY B 1 92  ? -22.542 -37.220 -2.421  1.00 28.79 ? 92   GLY B C     1 
ATOM   4757 O O     . GLY B 1 92  ? -23.299 -36.541 -3.115  1.00 30.60 ? 92   GLY B O     1 
ATOM   4758 N N     . GLY B 1 93  ? -21.422 -37.748 -2.858  1.00 26.66 ? 93   GLY B N     1 
ATOM   4759 C CA    . GLY B 1 93  ? -20.999 -37.600 -4.227  1.00 30.15 ? 93   GLY B CA    1 
ATOM   4760 C C     . GLY B 1 93  ? -20.710 -36.165 -4.556  1.00 30.95 ? 93   GLY B C     1 
ATOM   4761 O O     . GLY B 1 93  ? -20.045 -35.492 -3.799  1.00 31.25 ? 93   GLY B O     1 
ATOM   4762 N N     . SER B 1 94  ? -21.225 -35.694 -5.676  1.00 26.77 ? 94   SER B N     1 
ATOM   4763 C CA    . SER B 1 94  ? -21.053 -34.321 -6.084  1.00 28.85 ? 94   SER B CA    1 
ATOM   4764 C C     . SER B 1 94  ? -22.240 -33.493 -5.644  1.00 28.35 ? 94   SER B C     1 
ATOM   4765 O O     . SER B 1 94  ? -22.424 -32.384 -6.088  1.00 30.64 ? 94   SER B O     1 
ATOM   4766 C CB    . SER B 1 94  ? -20.885 -34.227 -7.601  1.00 33.50 ? 94   SER B CB    1 
ATOM   4767 O OG    . SER B 1 94  ? -20.739 -35.466 -8.236  1.00 41.32 ? 94   SER B OG    1 
ATOM   4768 N N     . ALA B 1 95  ? -23.035 -34.040 -4.750  1.00 29.30 ? 95   ALA B N     1 
ATOM   4769 C CA    . ALA B 1 95  ? -24.195 -33.349 -4.295  1.00 30.08 ? 95   ALA B CA    1 
ATOM   4770 C C     . ALA B 1 95  ? -23.977 -32.217 -3.240  1.00 29.39 ? 95   ALA B C     1 
ATOM   4771 O O     . ALA B 1 95  ? -23.283 -32.442 -2.289  1.00 28.42 ? 95   ALA B O     1 
ATOM   4772 C CB    . ALA B 1 95  ? -25.276 -34.300 -3.836  1.00 31.34 ? 95   ALA B CB    1 
ATOM   4773 N N     . PRO B 1 96  ? -24.627 -31.021 -3.419  1.00 28.92 ? 96   PRO B N     1 
ATOM   4774 C CA    . PRO B 1 96  ? -24.393 -29.967 -2.438  1.00 29.82 ? 96   PRO B CA    1 
ATOM   4775 C C     . PRO B 1 96  ? -25.101 -30.235 -1.107  1.00 31.50 ? 96   PRO B C     1 
ATOM   4776 O O     . PRO B 1 96  ? -26.209 -30.767 -1.100  1.00 31.41 ? 96   PRO B O     1 
ATOM   4777 C CB    . PRO B 1 96  ? -24.984 -28.724 -3.100  1.00 30.30 ? 96   PRO B CB    1 
ATOM   4778 C CG    . PRO B 1 96  ? -26.128 -29.297 -3.916  1.00 29.87 ? 96   PRO B CG    1 
ATOM   4779 C CD    . PRO B 1 96  ? -25.574 -30.595 -4.468  1.00 30.25 ? 96   PRO B CD    1 
ATOM   4780 N N     . ARG B 1 97  ? -24.448 -29.868 0.004   1.00 30.82 ? 97   ARG B N     1 
ATOM   4781 C CA    . ARG B 1 97  ? -25.100 -29.938 1.325   1.00 28.71 ? 97   ARG B CA    1 
ATOM   4782 C C     . ARG B 1 97  ? -26.380 -29.092 1.271   1.00 27.80 ? 97   ARG B C     1 
ATOM   4783 O O     . ARG B 1 97  ? -27.418 -29.577 1.749   1.00 27.58 ? 97   ARG B O     1 
ATOM   4784 C CB    . ARG B 1 97  ? -24.156 -29.493 2.441   1.00 26.13 ? 97   ARG B CB    1 
ATOM   4785 C CG    . ARG B 1 97  ? -24.895 -29.262 3.750   1.00 25.67 ? 97   ARG B CG    1 
ATOM   4786 C CD    . ARG B 1 97  ? -25.485 -30.552 4.247   1.00 25.81 ? 97   ARG B CD    1 
ATOM   4787 N NE    . ARG B 1 97  ? -26.240 -30.309 5.461   1.00 26.87 ? 97   ARG B NE    1 
ATOM   4788 C CZ    . ARG B 1 97  ? -27.534 -30.090 5.524   1.00 29.15 ? 97   ARG B CZ    1 
ATOM   4789 N NH1   . ARG B 1 97  ? -28.257 -30.072 4.415   1.00 27.99 ? 97   ARG B NH1   1 
ATOM   4790 N NH2   . ARG B 1 97  ? -28.098 -29.881 6.706   1.00 29.57 ? 97   ARG B NH2   1 
ATOM   4791 N N     . LEU B 1 98  ? -26.306 -27.875 0.722   1.00 29.25 ? 98   LEU B N     1 
ATOM   4792 C CA    . LEU B 1 98  ? -27.479 -26.977 0.599   1.00 28.93 ? 98   LEU B CA    1 
ATOM   4793 C C     . LEU B 1 98  ? -28.228 -27.322 -0.689  1.00 33.02 ? 98   LEU B C     1 
ATOM   4794 O O     . LEU B 1 98  ? -27.743 -26.940 -1.774  1.00 32.09 ? 98   LEU B O     1 
ATOM   4795 C CB    . LEU B 1 98  ? -27.067 -25.508 0.563   1.00 28.37 ? 98   LEU B CB    1 
ATOM   4796 C CG    . LEU B 1 98  ? -28.246 -24.537 0.477   1.00 30.37 ? 98   LEU B CG    1 
ATOM   4797 C CD1   . LEU B 1 98  ? -29.249 -24.776 1.610   1.00 30.18 ? 98   LEU B CD1   1 
ATOM   4798 C CD2   . LEU B 1 98  ? -27.752 -23.102 0.485   1.00 31.52 ? 98   LEU B CD2   1 
ATOM   4799 N N     . SER B 1 99  ? -29.374 -27.997 -0.571  1.00 34.37 ? 99   SER B N     1 
ATOM   4800 C CA    . SER B 1 99  ? -30.194 -28.374 -1.749  1.00 34.70 ? 99   SER B CA    1 
ATOM   4801 C C     . SER B 1 99  ? -30.525 -27.120 -2.565  1.00 29.43 ? 99   SER B C     1 
ATOM   4802 O O     . SER B 1 99  ? -30.931 -26.142 -1.974  1.00 31.22 ? 99   SER B O     1 
ATOM   4803 C CB    . SER B 1 99  ? -31.436 -29.124 -1.356  1.00 38.43 ? 99   SER B CB    1 
ATOM   4804 O OG    . SER B 1 99  ? -31.986 -29.699 -2.522  1.00 36.48 ? 99   SER B OG    1 
ATOM   4805 N N     . GLY B 1 100 ? -30.306 -27.165 -3.884  1.00 35.10 ? 100  GLY B N     1 
ATOM   4806 C CA    . GLY B 1 100 ? -30.506 -26.037 -4.806  1.00 31.58 ? 100  GLY B CA    1 
ATOM   4807 C C     . GLY B 1 100 ? -29.252 -25.207 -5.034  1.00 35.11 ? 100  GLY B C     1 
ATOM   4808 O O     . GLY B 1 100 ? -29.315 -24.246 -5.823  1.00 35.44 ? 100  GLY B O     1 
ATOM   4809 N N     . ALA B 1 101 ? -28.136 -25.495 -4.351  1.00 37.35 ? 101  ALA B N     1 
ATOM   4810 C CA    . ALA B 1 101 ? -26.884 -24.738 -4.581  1.00 33.26 ? 101  ALA B CA    1 
ATOM   4811 C C     . ALA B 1 101 ? -26.487 -24.887 -6.052  1.00 34.39 ? 101  ALA B C     1 
ATOM   4812 O O     . ALA B 1 101 ? -26.884 -25.885 -6.690  1.00 33.33 ? 101  ALA B O     1 
ATOM   4813 C CB    . ALA B 1 101 ? -25.770 -25.207 -3.680  1.00 33.54 ? 101  ALA B CB    1 
ATOM   4814 N N     . VAL B 1 102 ? -25.707 -23.934 -6.557  1.00 31.15 ? 102  VAL B N     1 
ATOM   4815 C CA    . VAL B 1 102 ? -24.983 -24.098 -7.846  1.00 34.04 ? 102  VAL B CA    1 
ATOM   4816 C C     . VAL B 1 102 ? -23.644 -24.791 -7.581  1.00 33.01 ? 102  VAL B C     1 
ATOM   4817 O O     . VAL B 1 102 ? -22.886 -24.288 -6.747  1.00 32.00 ? 102  VAL B O     1 
ATOM   4818 C CB    . VAL B 1 102 ? -24.801 -22.742 -8.543  1.00 34.52 ? 102  VAL B CB    1 
ATOM   4819 C CG1   . VAL B 1 102 ? -23.923 -22.864 -9.781  1.00 37.10 ? 102  VAL B CG1   1 
ATOM   4820 C CG2   . VAL B 1 102 ? -26.156 -22.141 -8.905  1.00 38.25 ? 102  VAL B CG2   1 
ATOM   4821 N N     . VAL B 1 103 ? -23.374 -25.888 -8.282  1.00 32.03 ? 103  VAL B N     1 
ATOM   4822 C CA    . VAL B 1 103 ? -22.102 -26.659 -8.170  1.00 31.48 ? 103  VAL B CA    1 
ATOM   4823 C C     . VAL B 1 103 ? -21.041 -25.944 -9.004  1.00 32.83 ? 103  VAL B C     1 
ATOM   4824 O O     . VAL B 1 103 ? -21.243 -25.773 -10.232 1.00 32.50 ? 103  VAL B O     1 
ATOM   4825 C CB    . VAL B 1 103 ? -22.278 -28.119 -8.608  1.00 32.93 ? 103  VAL B CB    1 
ATOM   4826 C CG1   . VAL B 1 103 ? -20.971 -28.908 -8.573  1.00 33.33 ? 103  VAL B CG1   1 
ATOM   4827 C CG2   . VAL B 1 103 ? -23.328 -28.833 -7.773  1.00 32.15 ? 103  VAL B CG2   1 
ATOM   4828 N N     . VAL B 1 104 ? -19.936 -25.565 -8.370  1.00 29.26 ? 104  VAL B N     1 
ATOM   4829 C CA    . VAL B 1 104 ? -18.692 -25.201 -9.104  1.00 28.18 ? 104  VAL B CA    1 
ATOM   4830 C C     . VAL B 1 104 ? -17.906 -26.491 -9.375  1.00 29.10 ? 104  VAL B C     1 
ATOM   4831 O O     . VAL B 1 104 ? -17.354 -27.111 -8.429  1.00 27.47 ? 104  VAL B O     1 
ATOM   4832 C CB    . VAL B 1 104 ? -17.883 -24.117 -8.367  1.00 28.94 ? 104  VAL B CB    1 
ATOM   4833 C CG1   . VAL B 1 104 ? -16.647 -23.711 -9.146  1.00 28.79 ? 104  VAL B CG1   1 
ATOM   4834 C CG2   . VAL B 1 104 ? -18.747 -22.900 -8.068  1.00 31.73 ? 104  VAL B CG2   1 
ATOM   4835 N N     . ASN B 1 105 ? -17.892 -26.912 -10.641 1.00 27.36 ? 105  ASN B N     1 
ATOM   4836 C CA    . ASN B 1 105 ? -17.127 -28.068 -11.141 1.00 28.93 ? 105  ASN B CA    1 
ATOM   4837 C C     . ASN B 1 105 ? -15.724 -27.576 -11.485 1.00 29.68 ? 105  ASN B C     1 
ATOM   4838 O O     . ASN B 1 105 ? -15.489 -27.163 -12.642 1.00 27.25 ? 105  ASN B O     1 
ATOM   4839 C CB    . ASN B 1 105 ? -17.842 -28.753 -12.309 1.00 30.28 ? 105  ASN B CB    1 
ATOM   4840 C CG    . ASN B 1 105 ? -17.170 -30.031 -12.776 1.00 29.75 ? 105  ASN B CG    1 
ATOM   4841 O OD1   . ASN B 1 105 ? -16.019 -30.321 -12.450 1.00 29.48 ? 105  ASN B OD1   1 
ATOM   4842 N ND2   . ASN B 1 105 ? -17.877 -30.801 -13.585 1.00 31.59 ? 105  ASN B ND2   1 
ATOM   4843 N N     . THR B 1 106 ? -14.789 -27.646 -10.531 1.00 27.66 ? 106  THR B N     1 
ATOM   4844 C CA    . THR B 1 106 ? -13.405 -27.171 -10.770 1.00 27.54 ? 106  THR B CA    1 
ATOM   4845 C C     . THR B 1 106 ? -12.661 -28.169 -11.664 1.00 27.82 ? 106  THR B C     1 
ATOM   4846 O O     . THR B 1 106 ? -11.785 -27.717 -12.430 1.00 32.73 ? 106  THR B O     1 
ATOM   4847 C CB    . THR B 1 106 ? -12.692 -26.811 -9.455  1.00 24.92 ? 106  THR B CB    1 
ATOM   4848 O OG1   . THR B 1 106 ? -12.501 -28.026 -8.727  1.00 28.88 ? 106  THR B OG1   1 
ATOM   4849 C CG2   . THR B 1 106 ? -13.486 -25.818 -8.644  1.00 25.60 ? 106  THR B CG2   1 
ATOM   4850 N N     . GLY B 1 107 ? -13.008 -29.460 -11.627 1.00 26.77 ? 107  GLY B N     1 
ATOM   4851 C CA    . GLY B 1 107 ? -12.164 -30.522 -12.195 1.00 26.17 ? 107  GLY B CA    1 
ATOM   4852 C C     . GLY B 1 107 ? -12.336 -30.676 -13.698 1.00 27.44 ? 107  GLY B C     1 
ATOM   4853 O O     . GLY B 1 107 ? -11.403 -31.186 -14.337 1.00 31.05 ? 107  GLY B O     1 
ATOM   4854 N N     . GLU B 1 108 ? -13.471 -30.269 -14.239 1.00 30.12 ? 108  GLU B N     1 
ATOM   4855 C CA    . GLU B 1 108 ? -13.788 -30.561 -15.657 1.00 31.92 ? 108  GLU B CA    1 
ATOM   4856 C C     . GLU B 1 108 ? -12.703 -29.926 -16.529 1.00 31.25 ? 108  GLU B C     1 
ATOM   4857 O O     . GLU B 1 108 ? -12.192 -30.604 -17.400 1.00 30.09 ? 108  GLU B O     1 
ATOM   4858 C CB    . GLU B 1 108 ? -15.171 -30.035 -16.047 1.00 36.41 ? 108  GLU B CB    1 
ATOM   4859 C CG    . GLU B 1 108 ? -15.503 -30.367 -17.488 1.00 37.81 ? 108  GLU B CG    1 
ATOM   4860 C CD    . GLU B 1 108 ? -16.921 -30.079 -17.925 1.00 45.19 ? 108  GLU B CD    1 
ATOM   4861 O OE1   . GLU B 1 108 ? -17.265 -30.461 -19.069 1.00 51.05 ? 108  GLU B OE1   1 
ATOM   4862 O OE2   . GLU B 1 108 ? -17.675 -29.482 -17.136 1.00 46.73 ? 108  GLU B OE2   1 
ATOM   4863 N N     . ARG B 1 109 ? -12.385 -28.652 -16.305 1.00 29.35 ? 109  ARG B N     1 
ATOM   4864 C CA    . ARG B 1 109 ? -11.452 -27.903 -17.181 1.00 30.35 ? 109  ARG B CA    1 
ATOM   4865 C C     . ARG B 1 109 ? -10.141 -27.582 -16.458 1.00 32.40 ? 109  ARG B C     1 
ATOM   4866 O O     . ARG B 1 109 ? -9.122  -27.425 -17.154 1.00 29.56 ? 109  ARG B O     1 
ATOM   4867 C CB    . ARG B 1 109 ? -12.119 -26.608 -17.635 1.00 30.52 ? 109  ARG B CB    1 
ATOM   4868 C CG    . ARG B 1 109 ? -13.430 -26.851 -18.373 1.00 32.60 ? 109  ARG B CG    1 
ATOM   4869 C CD    . ARG B 1 109 ? -14.210 -25.563 -18.514 1.00 34.28 ? 109  ARG B CD    1 
ATOM   4870 N NE    . ARG B 1 109 ? -13.681 -24.745 -19.585 1.00 33.60 ? 109  ARG B NE    1 
ATOM   4871 C CZ    . ARG B 1 109 ? -14.115 -23.539 -19.893 1.00 34.75 ? 109  ARG B CZ    1 
ATOM   4872 N NH1   . ARG B 1 109 ? -15.045 -22.945 -19.156 1.00 30.17 ? 109  ARG B NH1   1 
ATOM   4873 N NH2   . ARG B 1 109 ? -13.581 -22.915 -20.937 1.00 35.58 ? 109  ARG B NH2   1 
ATOM   4874 N N     . MET B 1 110 ? -10.142 -27.441 -15.132 1.00 31.36 ? 110  MET B N     1 
ATOM   4875 C CA    . MET B 1 110 ? -8.870  -27.208 -14.402 1.00 30.26 ? 110  MET B CA    1 
ATOM   4876 C C     . MET B 1 110 ? -8.304  -28.573 -13.998 1.00 28.61 ? 110  MET B C     1 
ATOM   4877 O O     . MET B 1 110 ? -8.447  -28.984 -12.829 1.00 28.38 ? 110  MET B O     1 
ATOM   4878 C CB    . MET B 1 110 ? -9.086  -26.270 -13.209 1.00 29.53 ? 110  MET B CB    1 
ATOM   4879 C CG    . MET B 1 110 ? -9.750  -24.988 -13.618 1.00 31.90 ? 110  MET B CG    1 
ATOM   4880 S SD    . MET B 1 110 ? -10.226 -23.950 -12.213 1.00 35.17 ? 110  MET B SD    1 
ATOM   4881 C CE    . MET B 1 110 ? -8.581  -23.579 -11.628 1.00 31.03 ? 110  MET B CE    1 
ATOM   4882 N N     . ASN B 1 111 ? -7.639  -29.247 -14.938 1.00 25.54 ? 111  ASN B N     1 
ATOM   4883 C CA    . ASN B 1 111 ? -7.280  -30.682 -14.815 1.00 27.62 ? 111  ASN B CA    1 
ATOM   4884 C C     . ASN B 1 111 ? -5.830  -30.911 -15.203 1.00 27.70 ? 111  ASN B C     1 
ATOM   4885 O O     . ASN B 1 111 ? -5.482  -32.061 -15.484 1.00 30.33 ? 111  ASN B O     1 
ATOM   4886 C CB    . ASN B 1 111 ? -8.210  -31.553 -15.660 1.00 28.63 ? 111  ASN B CB    1 
ATOM   4887 C CG    . ASN B 1 111 ? -8.109  -31.178 -17.120 1.00 31.95 ? 111  ASN B CG    1 
ATOM   4888 O OD1   . ASN B 1 111 ? -7.350  -30.264 -17.485 1.00 26.08 ? 111  ASN B OD1   1 
ATOM   4889 N ND2   . ASN B 1 111 ? -8.875  -31.874 -17.943 1.00 36.21 ? 111  ASN B ND2   1 
ATOM   4890 N N     . ARG B 1 112 ? -4.985  -29.884 -15.095 1.00 31.12 ? 112  ARG B N     1 
ATOM   4891 C CA    . ARG B 1 112 ? -3.579  -29.955 -15.534 1.00 34.66 ? 112  ARG B CA    1 
ATOM   4892 C C     . ARG B 1 112 ? -2.712  -30.319 -14.329 1.00 32.16 ? 112  ARG B C     1 
ATOM   4893 O O     . ARG B 1 112 ? -2.966  -29.792 -13.208 1.00 27.90 ? 112  ARG B O     1 
ATOM   4894 C CB    . ARG B 1 112 ? -3.172  -28.639 -16.206 1.00 41.16 ? 112  ARG B CB    1 
ATOM   4895 C CG    . ARG B 1 112 ? -3.869  -28.390 -17.539 1.00 52.44 ? 112  ARG B CG    1 
ATOM   4896 C CD    . ARG B 1 112 ? -3.871  -26.934 -18.029 1.00 60.48 ? 112  ARG B CD    1 
ATOM   4897 N NE    . ARG B 1 112 ? -4.661  -26.023 -17.184 1.00 75.57 ? 112  ARG B NE    1 
ATOM   4898 C CZ    . ARG B 1 112 ? -5.826  -25.417 -17.486 1.00 81.64 ? 112  ARG B CZ    1 
ATOM   4899 N NH1   . ARG B 1 112 ? -6.410  -25.569 -18.665 1.00 83.69 ? 112  ARG B NH1   1 
ATOM   4900 N NH2   . ARG B 1 112 ? -6.401  -24.629 -16.588 1.00 84.03 ? 112  ARG B NH2   1 
ATOM   4901 N N     . ILE B 1 113 ? -1.749  -31.187 -14.581 1.00 27.05 ? 113  ILE B N     1 
ATOM   4902 C CA    . ILE B 1 113 ? -0.535  -31.392 -13.750 1.00 30.46 ? 113  ILE B CA    1 
ATOM   4903 C C     . ILE B 1 113 ? 0.390   -30.239 -14.107 1.00 30.83 ? 113  ILE B C     1 
ATOM   4904 O O     . ILE B 1 113 ? 0.876   -30.195 -15.267 1.00 29.05 ? 113  ILE B O     1 
ATOM   4905 C CB    . ILE B 1 113 ? 0.083   -32.773 -14.017 1.00 28.88 ? 113  ILE B CB    1 
ATOM   4906 C CG1   . ILE B 1 113 ? -0.921  -33.887 -13.700 1.00 29.95 ? 113  ILE B CG1   1 
ATOM   4907 C CG2   . ILE B 1 113 ? 1.392   -32.932 -13.269 1.00 27.66 ? 113  ILE B CG2   1 
ATOM   4908 C CD1   . ILE B 1 113 ? -0.467  -35.269 -14.100 1.00 29.50 ? 113  ILE B CD1   1 
ATOM   4909 N N     . LEU B 1 114 ? 0.539   -29.286 -13.203 1.00 27.55 ? 114  LEU B N     1 
ATOM   4910 C CA    . LEU B 1 114 ? 1.219   -28.002 -13.519 1.00 30.53 ? 114  LEU B CA    1 
ATOM   4911 C C     . LEU B 1 114 ? 2.730   -28.193 -13.453 1.00 30.79 ? 114  LEU B C     1 
ATOM   4912 O O     . LEU B 1 114 ? 3.444   -27.534 -14.203 1.00 31.06 ? 114  LEU B O     1 
ATOM   4913 C CB    . LEU B 1 114 ? 0.734   -26.916 -12.556 1.00 28.75 ? 114  LEU B CB    1 
ATOM   4914 C CG    . LEU B 1 114 ? -0.727  -26.528 -12.731 1.00 28.89 ? 114  LEU B CG    1 
ATOM   4915 C CD1   . LEU B 1 114 ? -1.132  -25.526 -11.659 1.00 28.41 ? 114  LEU B CD1   1 
ATOM   4916 C CD2   . LEU B 1 114 ? -0.980  -25.949 -14.117 1.00 31.65 ? 114  LEU B CD2   1 
ATOM   4917 N N     . GLU B 1 115 ? 3.210   -29.056 -12.568 1.00 31.46 ? 115  GLU B N     1 
ATOM   4918 C CA    . GLU B 1 115 ? 4.658   -29.232 -12.359 1.00 31.61 ? 115  GLU B CA    1 
ATOM   4919 C C     . GLU B 1 115 ? 4.859   -30.520 -11.577 1.00 30.85 ? 115  GLU B C     1 
ATOM   4920 O O     . GLU B 1 115 ? 4.025   -30.811 -10.691 1.00 29.92 ? 115  GLU B O     1 
ATOM   4921 C CB    . GLU B 1 115 ? 5.191   -27.969 -11.676 1.00 36.68 ? 115  GLU B CB    1 
ATOM   4922 C CG    . GLU B 1 115 ? 6.414   -28.198 -10.819 1.00 42.33 ? 115  GLU B CG    1 
ATOM   4923 C CD    . GLU B 1 115 ? 7.023   -26.946 -10.204 1.00 41.93 ? 115  GLU B CD    1 
ATOM   4924 O OE1   . GLU B 1 115 ? 6.301   -25.953 -10.006 1.00 47.52 ? 115  GLU B OE1   1 
ATOM   4925 O OE2   . GLU B 1 115 ? 8.224   -27.002 -9.877  1.00 48.33 ? 115  GLU B OE2   1 
ATOM   4926 N N     . VAL B 1 116 ? 5.868   -31.290 -11.949 1.00 26.70 ? 116  VAL B N     1 
ATOM   4927 C CA    . VAL B 1 116 ? 6.388   -32.416 -11.133 1.00 28.94 ? 116  VAL B CA    1 
ATOM   4928 C C     . VAL B 1 116 ? 7.896   -32.228 -11.054 1.00 30.35 ? 116  VAL B C     1 
ATOM   4929 O O     . VAL B 1 116 ? 8.496   -32.110 -12.132 1.00 27.75 ? 116  VAL B O     1 
ATOM   4930 C CB    . VAL B 1 116 ? 6.021   -33.776 -11.738 1.00 27.07 ? 116  VAL B CB    1 
ATOM   4931 C CG1   . VAL B 1 116 ? 6.680   -34.929 -10.970 1.00 26.17 ? 116  VAL B CG1   1 
ATOM   4932 C CG2   . VAL B 1 116 ? 4.514   -33.939 -11.817 1.00 27.75 ? 116  VAL B CG2   1 
ATOM   4933 N N     . ASP B 1 117 ? 8.453   -32.128 -9.845  1.00 29.76 ? 117  ASP B N     1 
ATOM   4934 C CA    . ASP B 1 117 ? 9.912   -32.145 -9.594  1.00 26.19 ? 117  ASP B CA    1 
ATOM   4935 C C     . ASP B 1 117 ? 10.302  -33.530 -9.090  1.00 27.67 ? 117  ASP B C     1 
ATOM   4936 O O     . ASP B 1 117 ? 9.987   -33.888 -7.940  1.00 23.79 ? 117  ASP B O     1 
ATOM   4937 C CB    . ASP B 1 117 ? 10.335  -31.059 -8.603  1.00 30.24 ? 117  ASP B CB    1 
ATOM   4938 C CG    . ASP B 1 117 ? 11.842  -30.814 -8.583  1.00 29.56 ? 117  ASP B CG    1 
ATOM   4939 O OD1   . ASP B 1 117 ? 12.601  -31.760 -8.304  1.00 30.47 ? 117  ASP B OD1   1 
ATOM   4940 O OD2   . ASP B 1 117 ? 12.242  -29.689 -8.916  1.00 36.80 ? 117  ASP B OD2   1 
ATOM   4941 N N     . GLU B 1 118 ? 11.013  -34.284 -9.919  1.00 28.13 ? 118  GLU B N     1 
ATOM   4942 C CA    . GLU B 1 118 ? 11.402  -35.662 -9.577  1.00 28.01 ? 118  GLU B CA    1 
ATOM   4943 C C     . GLU B 1 118 ? 12.398  -35.688 -8.419  1.00 29.34 ? 118  GLU B C     1 
ATOM   4944 O O     . GLU B 1 118 ? 12.185  -36.500 -7.497  1.00 32.26 ? 118  GLU B O     1 
ATOM   4945 C CB    . GLU B 1 118 ? 11.943  -36.377 -10.817 1.00 30.91 ? 118  GLU B CB    1 
ATOM   4946 C CG    . GLU B 1 118 ? 11.991  -37.864 -10.602 1.00 29.03 ? 118  GLU B CG    1 
ATOM   4947 C CD    . GLU B 1 118 ? 12.232  -38.685 -11.856 1.00 30.47 ? 118  GLU B CD    1 
ATOM   4948 O OE1   . GLU B 1 118 ? 12.366  -38.088 -12.949 1.00 30.40 ? 118  GLU B OE1   1 
ATOM   4949 O OE2   . GLU B 1 118 ? 12.272  -39.914 -11.723 1.00 31.43 ? 118  GLU B OE2   1 
ATOM   4950 N N     . LYS B 1 119 ? 13.441  -34.848 -8.433  1.00 28.40 ? 119  LYS B N     1 
ATOM   4951 C CA    . LYS B 1 119 ? 14.517  -34.910 -7.411  1.00 27.75 ? 119  LYS B CA    1 
ATOM   4952 C C     . LYS B 1 119 ? 13.963  -34.461 -6.052  1.00 24.69 ? 119  LYS B C     1 
ATOM   4953 O O     . LYS B 1 119 ? 14.313  -35.073 -5.071  1.00 27.08 ? 119  LYS B O     1 
ATOM   4954 C CB    . LYS B 1 119 ? 15.741  -34.060 -7.758  1.00 32.50 ? 119  LYS B CB    1 
ATOM   4955 C CG    . LYS B 1 119 ? 16.564  -34.572 -8.942  1.00 41.10 ? 119  LYS B CG    1 
ATOM   4956 C CD    . LYS B 1 119 ? 15.856  -34.484 -10.285 1.00 48.96 ? 119  LYS B CD    1 
ATOM   4957 C CE    . LYS B 1 119 ? 15.280  -33.113 -10.628 1.00 49.94 ? 119  LYS B CE    1 
ATOM   4958 N NZ    . LYS B 1 119 ? 13.994  -33.221 -11.356 1.00 46.32 ? 119  LYS B NZ    1 
ATOM   4959 N N     . LEU B 1 120 ? 13.121  -33.434 -6.010  1.00 26.45 ? 120  LEU B N     1 
ATOM   4960 C CA    . LEU B 1 120 ? 12.634  -32.885 -4.715  1.00 26.64 ? 120  LEU B CA    1 
ATOM   4961 C C     . LEU B 1 120 ? 11.305  -33.547 -4.344  1.00 25.54 ? 120  LEU B C     1 
ATOM   4962 O O     . LEU B 1 120 ? 10.791  -33.262 -3.273  1.00 26.47 ? 120  LEU B O     1 
ATOM   4963 C CB    . LEU B 1 120 ? 12.488  -31.372 -4.844  1.00 26.80 ? 120  LEU B CB    1 
ATOM   4964 C CG    . LEU B 1 120 ? 13.784  -30.598 -5.073  1.00 29.59 ? 120  LEU B CG    1 
ATOM   4965 C CD1   . LEU B 1 120 ? 13.526  -29.122 -4.967  1.00 29.49 ? 120  LEU B CD1   1 
ATOM   4966 C CD2   . LEU B 1 120 ? 14.887  -31.013 -4.111  1.00 32.34 ? 120  LEU B CD2   1 
ATOM   4967 N N     . GLY B 1 121 ? 10.761  -34.365 -5.237  1.00 23.54 ? 121  GLY B N     1 
ATOM   4968 C CA    . GLY B 1 121 ? 9.581   -35.208 -5.012  1.00 24.94 ? 121  GLY B CA    1 
ATOM   4969 C C     . GLY B 1 121 ? 8.340   -34.414 -4.673  1.00 24.66 ? 121  GLY B C     1 
ATOM   4970 O O     . GLY B 1 121 ? 7.869   -34.537 -3.535  1.00 25.69 ? 121  GLY B O     1 
ATOM   4971 N N     . TYR B 1 122 ? 7.782   -33.672 -5.622  1.00 21.86 ? 122  TYR B N     1 
ATOM   4972 C CA    . TYR B 1 122 ? 6.464   -33.009 -5.447  1.00 22.11 ? 122  TYR B CA    1 
ATOM   4973 C C     . TYR B 1 122 ? 5.794   -32.804 -6.789  1.00 25.54 ? 122  TYR B C     1 
ATOM   4974 O O     . TYR B 1 122 ? 6.472   -32.907 -7.834  1.00 25.89 ? 122  TYR B O     1 
ATOM   4975 C CB    . TYR B 1 122 ? 6.576   -31.649 -4.750  1.00 22.99 ? 122  TYR B CB    1 
ATOM   4976 C CG    . TYR B 1 122 ? 7.299   -30.573 -5.523  1.00 22.40 ? 122  TYR B CG    1 
ATOM   4977 C CD1   . TYR B 1 122 ? 6.657   -29.882 -6.537  1.00 25.50 ? 122  TYR B CD1   1 
ATOM   4978 C CD2   . TYR B 1 122 ? 8.597   -30.205 -5.205  1.00 24.76 ? 122  TYR B CD2   1 
ATOM   4979 C CE1   . TYR B 1 122 ? 7.280   -28.853 -7.207  1.00 26.90 ? 122  TYR B CE1   1 
ATOM   4980 C CE2   . TYR B 1 122 ? 9.244   -29.180 -5.870  1.00 25.77 ? 122  TYR B CE2   1 
ATOM   4981 C CZ    . TYR B 1 122 ? 8.576   -28.507 -6.881  1.00 30.38 ? 122  TYR B CZ    1 
ATOM   4982 O OH    . TYR B 1 122 ? 9.158   -27.503 -7.592  1.00 32.60 ? 122  TYR B OH    1 
ATOM   4983 N N     . ALA B 1 123 ? 4.494   -32.544 -6.741  1.00 25.10 ? 123  ALA B N     1 
ATOM   4984 C CA    . ALA B 1 123 ? 3.671   -32.105 -7.887  1.00 24.89 ? 123  ALA B CA    1 
ATOM   4985 C C     . ALA B 1 123 ? 2.915   -30.844 -7.476  1.00 26.54 ? 123  ALA B C     1 
ATOM   4986 O O     . ALA B 1 123 ? 2.547   -30.720 -6.282  1.00 26.27 ? 123  ALA B O     1 
ATOM   4987 C CB    . ALA B 1 123 ? 2.689   -33.189 -8.282  1.00 26.42 ? 123  ALA B CB    1 
ATOM   4988 N N     . LEU B 1 124 ? 2.589   -30.017 -8.458  1.00 21.57 ? 124  LEU B N     1 
ATOM   4989 C CA    . LEU B 1 124 ? 1.711   -28.886 -8.258  1.00 25.79 ? 124  LEU B CA    1 
ATOM   4990 C C     . LEU B 1 124 ? 0.545   -29.288 -9.158  1.00 26.80 ? 124  LEU B C     1 
ATOM   4991 O O     . LEU B 1 124 ? 0.746   -29.576 -10.327 1.00 24.78 ? 124  LEU B O     1 
ATOM   4992 C CB    . LEU B 1 124 ? 2.304   -27.577 -8.719  1.00 24.43 ? 124  LEU B CB    1 
ATOM   4993 C CG    . LEU B 1 124 ? 1.389   -26.356 -8.608  1.00 26.97 ? 124  LEU B CG    1 
ATOM   4994 C CD1   . LEU B 1 124 ? 0.870   -26.135 -7.196  1.00 28.16 ? 124  LEU B CD1   1 
ATOM   4995 C CD2   . LEU B 1 124 ? 2.108   -25.123 -9.120  1.00 26.94 ? 124  LEU B CD2   1 
ATOM   4996 N N     . LEU B 1 125 ? -0.664  -29.296 -8.630  1.00 25.39 ? 125  LEU B N     1 
ATOM   4997 C CA    . LEU B 1 125 ? -1.803  -29.814 -9.359  1.00 26.24 ? 125  LEU B CA    1 
ATOM   4998 C C     . LEU B 1 125 ? -3.021  -28.941 -9.341  1.00 28.63 ? 125  LEU B C     1 
ATOM   4999 O O     . LEU B 1 125 ? -3.242  -28.145 -8.463  1.00 25.80 ? 125  LEU B O     1 
ATOM   5000 C CB    . LEU B 1 125 ? -2.210  -31.162 -8.767  1.00 25.94 ? 125  LEU B CB    1 
ATOM   5001 C CG    . LEU B 1 125 ? -1.148  -32.230 -8.592  1.00 26.50 ? 125  LEU B CG    1 
ATOM   5002 C CD1   . LEU B 1 125 ? -1.617  -33.287 -7.630  1.00 28.55 ? 125  LEU B CD1   1 
ATOM   5003 C CD2   . LEU B 1 125 ? -0.774  -32.836 -9.927  1.00 27.24 ? 125  LEU B CD2   1 
ATOM   5004 N N     . GLU B 1 126 ? -3.817  -29.164 -10.361 1.00 48.90 ? 126  GLU B N     1 
ATOM   5005 C CA    . GLU B 1 126 ? -5.153  -28.680 -10.434 1.00 44.43 ? 126  GLU B CA    1 
ATOM   5006 C C     . GLU B 1 126 ? -6.170  -29.707 -9.978  1.00 29.37 ? 126  GLU B C     1 
ATOM   5007 O O     . GLU B 1 126 ? -5.875  -30.870 -9.928  1.00 28.03 ? 126  GLU B O     1 
ATOM   5008 C CB    . GLU B 1 126 ? -5.411  -28.137 -11.834 1.00 51.55 ? 126  GLU B CB    1 
ATOM   5009 C CG    . GLU B 1 126 ? -4.617  -26.882 -12.125 1.00 50.20 ? 126  GLU B CG    1 
ATOM   5010 C CD    . GLU B 1 126 ? -5.004  -26.225 -13.426 1.00 61.34 ? 126  GLU B CD    1 
ATOM   5011 O OE1   . GLU B 1 126 ? -4.865  -24.997 -13.526 1.00 77.71 ? 126  GLU B OE1   1 
ATOM   5012 O OE2   . GLU B 1 126 ? -5.442  -26.939 -14.340 1.00 39.87 ? 126  GLU B OE2   1 
ATOM   5013 N N     . PRO B 1 127 ? -7.363  -29.244 -9.612  1.00 24.24 ? 127  PRO B N     1 
ATOM   5014 C CA    . PRO B 1 127 ? -8.350  -30.159 -9.043  1.00 26.26 ? 127  PRO B CA    1 
ATOM   5015 C C     . PRO B 1 127 ? -8.801  -31.370 -9.858  1.00 24.70 ? 127  PRO B C     1 
ATOM   5016 O O     . PRO B 1 127 ? -9.129  -32.381 -9.304  1.00 23.71 ? 127  PRO B O     1 
ATOM   5017 C CB    . PRO B 1 127 ? -9.512  -29.238 -8.739  1.00 24.86 ? 127  PRO B CB    1 
ATOM   5018 C CG    . PRO B 1 127 ? -8.889  -27.933 -8.457  1.00 26.88 ? 127  PRO B CG    1 
ATOM   5019 C CD    . PRO B 1 127 ? -7.792  -27.842 -9.457  1.00 25.90 ? 127  PRO B CD    1 
ATOM   5020 N N     . GLY B 1 128 ? -8.801  -31.255 -11.165 1.00 25.42 ? 128  GLY B N     1 
ATOM   5021 C CA    . GLY B 1 128 ? -9.198  -32.359 -12.007 1.00 27.05 ? 128  GLY B CA    1 
ATOM   5022 C C     . GLY B 1 128 ? -8.234  -33.502 -12.223 1.00 27.17 ? 128  GLY B C     1 
ATOM   5023 O O     . GLY B 1 128 ? -8.562  -34.474 -12.857 1.00 27.95 ? 128  GLY B O     1 
ATOM   5024 N N     . VAL B 1 129 ? -7.032  -33.381 -11.702 1.00 25.84 ? 129  VAL B N     1 
ATOM   5025 C CA    . VAL B 1 129 ? -6.078  -34.457 -11.820 1.00 25.50 ? 129  VAL B CA    1 
ATOM   5026 C C     . VAL B 1 129 ? -6.520  -35.623 -10.944 1.00 29.42 ? 129  VAL B C     1 
ATOM   5027 O O     . VAL B 1 129 ? -6.598  -35.484 -9.741  1.00 25.18 ? 129  VAL B O     1 
ATOM   5028 C CB    . VAL B 1 129 ? -4.654  -34.032 -11.457 1.00 25.85 ? 129  VAL B CB    1 
ATOM   5029 C CG1   . VAL B 1 129 ? -3.683  -35.185 -11.588 1.00 25.47 ? 129  VAL B CG1   1 
ATOM   5030 C CG2   . VAL B 1 129 ? -4.231  -32.840 -12.279 1.00 27.43 ? 129  VAL B CG2   1 
ATOM   5031 N N     . THR B 1 130 ? -6.824  -36.750 -11.574 1.00 24.89 ? 130  THR B N     1 
ATOM   5032 C CA    . THR B 1 130 ? -7.230  -37.962 -10.838 1.00 25.92 ? 130  THR B CA    1 
ATOM   5033 C C     . THR B 1 130 ? -5.969  -38.697 -10.409 1.00 24.25 ? 130  THR B C     1 
ATOM   5034 O O     . THR B 1 130 ? -4.877  -38.385 -10.904 1.00 24.32 ? 130  THR B O     1 
ATOM   5035 C CB    . THR B 1 130 ? -8.120  -38.886 -11.685 1.00 25.96 ? 130  THR B CB    1 
ATOM   5036 O OG1   . THR B 1 130 ? -7.380  -39.302 -12.827 1.00 26.54 ? 130  THR B OG1   1 
ATOM   5037 C CG2   . THR B 1 130 ? -9.367  -38.230 -12.194 1.00 27.21 ? 130  THR B CG2   1 
ATOM   5038 N N     . TYR B 1 131 ? -6.109  -39.666 -9.518  1.00 23.97 ? 131  TYR B N     1 
ATOM   5039 C CA    . TYR B 1 131 ? -4.991  -40.538 -9.114  1.00 25.13 ? 131  TYR B CA    1 
ATOM   5040 C C     . TYR B 1 131 ? -4.505  -41.299 -10.345 1.00 25.99 ? 131  TYR B C     1 
ATOM   5041 O O     . TYR B 1 131 ? -3.277  -41.449 -10.483 1.00 27.81 ? 131  TYR B O     1 
ATOM   5042 C CB    . TYR B 1 131 ? -5.421  -41.469 -7.996  1.00 25.78 ? 131  TYR B CB    1 
ATOM   5043 C CG    . TYR B 1 131 ? -5.689  -40.736 -6.714  1.00 25.35 ? 131  TYR B CG    1 
ATOM   5044 C CD1   . TYR B 1 131 ? -4.643  -40.337 -5.909  1.00 26.94 ? 131  TYR B CD1   1 
ATOM   5045 C CD2   . TYR B 1 131 ? -6.977  -40.399 -6.324  1.00 27.44 ? 131  TYR B CD2   1 
ATOM   5046 C CE1   . TYR B 1 131 ? -4.874  -39.658 -4.718  1.00 28.66 ? 131  TYR B CE1   1 
ATOM   5047 C CE2   . TYR B 1 131 ? -7.222  -39.728 -5.135  1.00 28.20 ? 131  TYR B CE2   1 
ATOM   5048 C CZ    . TYR B 1 131 ? -6.162  -39.348 -4.333  1.00 24.94 ? 131  TYR B CZ    1 
ATOM   5049 O OH    . TYR B 1 131 ? -6.373  -38.716 -3.139  1.00 26.19 ? 131  TYR B OH    1 
ATOM   5050 N N     . PHE B 1 132 ? -5.419  -41.720 -11.224 1.00 28.13 ? 132  PHE B N     1 
ATOM   5051 C CA    . PHE B 1 132 ? -5.039  -42.369 -12.511 1.00 26.62 ? 132  PHE B CA    1 
ATOM   5052 C C     . PHE B 1 132 ? -4.161  -41.419 -13.325 1.00 24.87 ? 132  PHE B C     1 
ATOM   5053 O O     . PHE B 1 132 ? -3.076  -41.857 -13.779 1.00 28.08 ? 132  PHE B O     1 
ATOM   5054 C CB    . PHE B 1 132 ? -6.270  -42.813 -13.304 1.00 28.59 ? 132  PHE B CB    1 
ATOM   5055 C CG    . PHE B 1 132 ? -6.896  -44.083 -12.787 1.00 29.36 ? 132  PHE B CG    1 
ATOM   5056 C CD1   . PHE B 1 132 ? -6.205  -45.290 -12.817 1.00 29.07 ? 132  PHE B CD1   1 
ATOM   5057 C CD2   . PHE B 1 132 ? -8.169  -44.065 -12.234 1.00 31.21 ? 132  PHE B CD2   1 
ATOM   5058 C CE1   . PHE B 1 132 ? -6.774  -46.453 -12.318 1.00 32.57 ? 132  PHE B CE1   1 
ATOM   5059 C CE2   . PHE B 1 132 ? -8.751  -45.238 -11.778 1.00 31.78 ? 132  PHE B CE2   1 
ATOM   5060 C CZ    . PHE B 1 132 ? -8.050  -46.424 -11.797 1.00 30.96 ? 132  PHE B CZ    1 
ATOM   5061 N N     . ASP B 1 133 ? -4.608  -40.177 -13.496 1.00 29.02 ? 133  ASP B N     1 
ATOM   5062 C CA    . ASP B 1 133 ? -3.884  -39.120 -14.255 1.00 27.68 ? 133  ASP B CA    1 
ATOM   5063 C C     . ASP B 1 133 ? -2.459  -38.975 -13.705 1.00 30.02 ? 133  ASP B C     1 
ATOM   5064 O O     . ASP B 1 133 ? -1.490  -39.032 -14.494 1.00 27.40 ? 133  ASP B O     1 
ATOM   5065 C CB    . ASP B 1 133 ? -4.611  -37.783 -14.195 1.00 27.13 ? 133  ASP B CB    1 
ATOM   5066 C CG    . ASP B 1 133 ? -5.924  -37.712 -14.963 1.00 30.09 ? 133  ASP B CG    1 
ATOM   5067 O OD1   . ASP B 1 133 ? -6.146  -38.570 -15.857 1.00 31.09 ? 133  ASP B OD1   1 
ATOM   5068 O OD2   . ASP B 1 133 ? -6.734  -36.784 -14.664 1.00 29.90 ? 133  ASP B OD2   1 
ATOM   5069 N N     . LEU B 1 134 ? -2.317  -38.811 -12.386 1.00 27.22 ? 134  LEU B N     1 
ATOM   5070 C CA    . LEU B 1 134 ? -0.995  -38.547 -11.802 1.00 26.64 ? 134  LEU B CA    1 
ATOM   5071 C C     . LEU B 1 134 ? -0.102  -39.779 -11.914 1.00 28.99 ? 134  LEU B C     1 
ATOM   5072 O O     . LEU B 1 134 ? 1.102   -39.609 -12.201 1.00 30.24 ? 134  LEU B O     1 
ATOM   5073 C CB    . LEU B 1 134 ? -1.136  -38.093 -10.352 1.00 26.25 ? 134  LEU B CB    1 
ATOM   5074 C CG    . LEU B 1 134 ? 0.169   -37.588 -9.746  1.00 26.54 ? 134  LEU B CG    1 
ATOM   5075 C CD1   . LEU B 1 134 ? 0.799   -36.512 -10.609 1.00 28.86 ? 134  LEU B CD1   1 
ATOM   5076 C CD2   . LEU B 1 134 ? -0.052  -37.061 -8.331  1.00 27.09 ? 134  LEU B CD2   1 
ATOM   5077 N N     . HIS B 1 135 ? -0.642  -40.967 -11.640 1.00 29.21 ? 135  HIS B N     1 
ATOM   5078 C CA    . HIS B 1 135 ? 0.095   -42.244 -11.761 1.00 28.47 ? 135  HIS B CA    1 
ATOM   5079 C C     . HIS B 1 135 ? 0.619   -42.375 -13.197 1.00 29.66 ? 135  HIS B C     1 
ATOM   5080 O O     . HIS B 1 135 ? 1.808   -42.701 -13.356 1.00 28.75 ? 135  HIS B O     1 
ATOM   5081 C CB    . HIS B 1 135 ? -0.801  -43.432 -11.388 1.00 32.47 ? 135  HIS B CB    1 
ATOM   5082 C CG    . HIS B 1 135 ? -0.222  -44.741 -11.787 1.00 31.84 ? 135  HIS B CG    1 
ATOM   5083 N ND1   . HIS B 1 135 ? 0.840   -45.330 -11.107 1.00 34.81 ? 135  HIS B ND1   1 
ATOM   5084 C CD2   . HIS B 1 135 ? -0.505  -45.557 -12.823 1.00 31.42 ? 135  HIS B CD2   1 
ATOM   5085 C CE1   . HIS B 1 135 ? 1.142   -46.473 -11.686 1.00 32.08 ? 135  HIS B CE1   1 
ATOM   5086 N NE2   . HIS B 1 135 ? 0.345   -46.622 -12.740 1.00 32.10 ? 135  HIS B NE2   1 
ATOM   5087 N N     . GLU B 1 136 ? -0.243  -42.154 -14.186 1.00 30.77 ? 136  GLU B N     1 
ATOM   5088 C CA    . GLU B 1 136 ? 0.142   -42.251 -15.623 1.00 33.24 ? 136  GLU B CA    1 
ATOM   5089 C C     . GLU B 1 136 ? 1.289   -41.272 -15.903 1.00 34.21 ? 136  GLU B C     1 
ATOM   5090 O O     . GLU B 1 136 ? 2.296   -41.704 -16.506 1.00 30.11 ? 136  GLU B O     1 
ATOM   5091 C CB    . GLU B 1 136 ? -1.046  -41.974 -16.537 1.00 39.65 ? 136  GLU B CB    1 
ATOM   5092 C CG    . GLU B 1 136 ? -2.085  -43.085 -16.549 1.00 49.66 ? 136  GLU B CG    1 
ATOM   5093 C CD    . GLU B 1 136 ? -3.400  -42.729 -17.236 1.00 55.69 ? 136  GLU B CD    1 
ATOM   5094 O OE1   . GLU B 1 136 ? -3.425  -41.735 -18.006 1.00 62.47 ? 136  GLU B OE1   1 
ATOM   5095 O OE2   . GLU B 1 136 ? -4.396  -43.445 -17.002 1.00 59.72 ? 136  GLU B OE2   1 
ATOM   5096 N N     . TYR B 1 137 ? 1.164   -40.015 -15.464 1.00 28.44 ? 137  TYR B N     1 
ATOM   5097 C CA    . TYR B 1 137 ? 2.207   -38.977 -15.654 1.00 31.05 ? 137  TYR B CA    1 
ATOM   5098 C C     . TYR B 1 137 ? 3.532   -39.408 -15.015 1.00 31.60 ? 137  TYR B C     1 
ATOM   5099 O O     . TYR B 1 137 ? 4.607   -39.297 -15.657 1.00 29.40 ? 137  TYR B O     1 
ATOM   5100 C CB    . TYR B 1 137 ? 1.753   -37.635 -15.088 1.00 31.94 ? 137  TYR B CB    1 
ATOM   5101 C CG    . TYR B 1 137 ? 2.686   -36.509 -15.434 1.00 33.25 ? 137  TYR B CG    1 
ATOM   5102 C CD1   . TYR B 1 137 ? 3.831   -36.277 -14.695 1.00 34.62 ? 137  TYR B CD1   1 
ATOM   5103 C CD2   . TYR B 1 137 ? 2.430   -35.689 -16.518 1.00 39.54 ? 137  TYR B CD2   1 
ATOM   5104 C CE1   . TYR B 1 137 ? 4.691   -35.238 -15.012 1.00 40.24 ? 137  TYR B CE1   1 
ATOM   5105 C CE2   . TYR B 1 137 ? 3.282   -34.650 -16.853 1.00 40.28 ? 137  TYR B CE2   1 
ATOM   5106 C CZ    . TYR B 1 137 ? 4.419   -34.436 -16.104 1.00 39.48 ? 137  TYR B CZ    1 
ATOM   5107 O OH    . TYR B 1 137 ? 5.248   -33.408 -16.424 1.00 49.50 ? 137  TYR B OH    1 
ATOM   5108 N N     . LEU B 1 138 ? 3.506   -39.872 -13.767 1.00 29.27 ? 138  LEU B N     1 
ATOM   5109 C CA    . LEU B 1 138 ? 4.763   -40.262 -13.090 1.00 29.46 ? 138  LEU B CA    1 
ATOM   5110 C C     . LEU B 1 138 ? 5.390   -41.432 -13.854 1.00 31.48 ? 138  LEU B C     1 
ATOM   5111 O O     . LEU B 1 138 ? 6.594   -41.432 -14.010 1.00 28.24 ? 138  LEU B O     1 
ATOM   5112 C CB    . LEU B 1 138 ? 4.515   -40.658 -11.633 1.00 30.04 ? 138  LEU B CB    1 
ATOM   5113 C CG    . LEU B 1 138 ? 3.959   -39.560 -10.733 1.00 29.19 ? 138  LEU B CG    1 
ATOM   5114 C CD1   . LEU B 1 138 ? 3.891   -40.067 -9.298  1.00 29.00 ? 138  LEU B CD1   1 
ATOM   5115 C CD2   . LEU B 1 138 ? 4.797   -38.290 -10.809 1.00 29.66 ? 138  LEU B CD2   1 
ATOM   5116 N N     . GLU B 1 139 ? 4.601   -42.412 -14.281 1.00 30.51 ? 139  GLU B N     1 
ATOM   5117 C CA    . GLU B 1 139 ? 5.150   -43.614 -14.960 1.00 33.13 ? 139  GLU B CA    1 
ATOM   5118 C C     . GLU B 1 139 ? 5.840   -43.193 -16.271 1.00 36.31 ? 139  GLU B C     1 
ATOM   5119 O O     . GLU B 1 139 ? 6.854   -43.815 -16.625 1.00 36.79 ? 139  GLU B O     1 
ATOM   5120 C CB    . GLU B 1 139 ? 4.036   -44.644 -15.150 1.00 34.61 ? 139  GLU B CB    1 
ATOM   5121 C CG    . GLU B 1 139 ? 3.708   -45.403 -13.871 1.00 33.98 ? 139  GLU B CG    1 
ATOM   5122 C CD    . GLU B 1 139 ? 4.894   -46.081 -13.201 1.00 38.91 ? 139  GLU B CD    1 
ATOM   5123 O OE1   . GLU B 1 139 ? 5.228   -45.721 -12.034 1.00 36.71 ? 139  GLU B OE1   1 
ATOM   5124 O OE2   . GLU B 1 139 ? 5.490   -46.977 -13.839 1.00 43.11 ? 139  GLU B OE2   1 
ATOM   5125 N N     . ALA B 1 140 ? 5.344   -42.149 -16.936 1.00 36.61 ? 140  ALA B N     1 
ATOM   5126 C CA    . ALA B 1 140 ? 5.856   -41.666 -18.242 1.00 36.16 ? 140  ALA B CA    1 
ATOM   5127 C C     . ALA B 1 140 ? 7.001   -40.656 -18.054 1.00 40.44 ? 140  ALA B C     1 
ATOM   5128 O O     . ALA B 1 140 ? 7.933   -40.705 -18.863 1.00 38.29 ? 140  ALA B O     1 
ATOM   5129 C CB    . ALA B 1 140 ? 4.736   -41.076 -19.050 1.00 36.10 ? 140  ALA B CB    1 
ATOM   5130 N N     . HIS B 1 141 ? 6.956   -39.777 -17.041 1.00 37.03 ? 141  HIS B N     1 
ATOM   5131 C CA    . HIS B 1 141 ? 7.841   -38.579 -16.959 1.00 36.07 ? 141  HIS B CA    1 
ATOM   5132 C C     . HIS B 1 141 ? 8.610   -38.471 -15.646 1.00 35.53 ? 141  HIS B C     1 
ATOM   5133 O O     . HIS B 1 141 ? 9.582   -37.688 -15.620 1.00 33.70 ? 141  HIS B O     1 
ATOM   5134 C CB    . HIS B 1 141 ? 7.031   -37.303 -17.166 1.00 36.58 ? 141  HIS B CB    1 
ATOM   5135 C CG    . HIS B 1 141 ? 6.207   -37.332 -18.404 1.00 37.69 ? 141  HIS B CG    1 
ATOM   5136 N ND1   . HIS B 1 141 ? 6.769   -37.467 -19.662 1.00 40.74 ? 141  HIS B ND1   1 
ATOM   5137 C CD2   . HIS B 1 141 ? 4.875   -37.259 -18.591 1.00 40.01 ? 141  HIS B CD2   1 
ATOM   5138 C CE1   . HIS B 1 141 ? 5.813   -37.480 -20.569 1.00 39.30 ? 141  HIS B CE1   1 
ATOM   5139 N NE2   . HIS B 1 141 ? 4.642   -37.332 -19.939 1.00 42.33 ? 141  HIS B NE2   1 
ATOM   5140 N N     . ALA B 1 142 ? 8.205   -39.154 -14.573 1.00 31.38 ? 142  ALA B N     1 
ATOM   5141 C CA    . ALA B 1 142 ? 8.959   -39.097 -13.301 1.00 31.94 ? 142  ALA B CA    1 
ATOM   5142 C C     . ALA B 1 142 ? 8.866   -40.424 -12.573 1.00 34.58 ? 142  ALA B C     1 
ATOM   5143 O O     . ALA B 1 142 ? 8.348   -40.491 -11.453 1.00 27.36 ? 142  ALA B O     1 
ATOM   5144 C CB    . ALA B 1 142 ? 8.465   -37.927 -12.472 1.00 33.45 ? 142  ALA B CB    1 
ATOM   5145 N N     . PRO B 1 143 ? 9.398   -41.508 -13.188 1.00 35.41 ? 143  PRO B N     1 
ATOM   5146 C CA    . PRO B 1 143 ? 9.140   -42.865 -12.706 1.00 34.34 ? 143  PRO B CA    1 
ATOM   5147 C C     . PRO B 1 143 ? 9.800   -43.264 -11.381 1.00 32.41 ? 143  PRO B C     1 
ATOM   5148 O O     . PRO B 1 143 ? 9.474   -44.325 -10.868 1.00 30.36 ? 143  PRO B O     1 
ATOM   5149 C CB    . PRO B 1 143 ? 9.648   -43.790 -13.844 1.00 36.43 ? 143  PRO B CB    1 
ATOM   5150 C CG    . PRO B 1 143 ? 10.577  -42.925 -14.663 1.00 35.05 ? 143  PRO B CG    1 
ATOM   5151 C CD    . PRO B 1 143 ? 10.146  -41.489 -14.459 1.00 33.44 ? 143  PRO B CD    1 
ATOM   5152 N N     . SER B 1 144 ? 10.662  -42.431 -10.799 1.00 27.71 ? 144  SER B N     1 
ATOM   5153 C CA    . SER B 1 144 ? 11.228  -42.738 -9.465  1.00 27.82 ? 144  SER B CA    1 
ATOM   5154 C C     . SER B 1 144 ? 10.211  -42.387 -8.368  1.00 25.01 ? 144  SER B C     1 
ATOM   5155 O O     . SER B 1 144 ? 10.470  -42.731 -7.212  1.00 29.90 ? 144  SER B O     1 
ATOM   5156 C CB    . SER B 1 144 ? 12.532  -42.065 -9.222  1.00 27.86 ? 144  SER B CB    1 
ATOM   5157 O OG    . SER B 1 144 ? 12.363  -40.664 -9.213  1.00 29.46 ? 144  SER B OG    1 
ATOM   5158 N N     . LEU B 1 145 ? 9.125   -41.722 -8.698  1.00 26.81 ? 145  LEU B N     1 
ATOM   5159 C CA    . LEU B 1 145 ? 8.107   -41.288 -7.691  1.00 28.67 ? 145  LEU B CA    1 
ATOM   5160 C C     . LEU B 1 145 ? 6.868   -42.184 -7.774  1.00 27.44 ? 145  LEU B C     1 
ATOM   5161 O O     . LEU B 1 145 ? 6.619   -42.779 -8.819  1.00 27.08 ? 145  LEU B O     1 
ATOM   5162 C CB    . LEU B 1 145 ? 7.733   -39.825 -7.939  1.00 27.09 ? 145  LEU B CB    1 
ATOM   5163 C CG    . LEU B 1 145 ? 8.874   -38.819 -7.848  1.00 27.15 ? 145  LEU B CG    1 
ATOM   5164 C CD1   . LEU B 1 145 ? 8.358   -37.400 -8.092  1.00 27.89 ? 145  LEU B CD1   1 
ATOM   5165 C CD2   . LEU B 1 145 ? 9.601   -38.927 -6.518  1.00 29.03 ? 145  LEU B CD2   1 
ATOM   5166 N N     . MET B 1 146 ? 6.052   -42.180 -6.719  1.00 26.71 ? 146  MET B N     1 
ATOM   5167 C CA    . MET B 1 146 ? 4.744   -42.848 -6.700  1.00 24.54 ? 146  MET B CA    1 
ATOM   5168 C C     . MET B 1 146 ? 3.760   -41.945 -5.953  1.00 28.32 ? 146  MET B C     1 
ATOM   5169 O O     . MET B 1 146 ? 4.194   -41.129 -5.070  1.00 24.43 ? 146  MET B O     1 
ATOM   5170 C CB    . MET B 1 146 ? 4.836   -44.199 -5.996  1.00 28.64 ? 146  MET B CB    1 
ATOM   5171 C CG    . MET B 1 146 ? 5.471   -44.129 -4.624  1.00 29.37 ? 146  MET B CG    1 
ATOM   5172 S SD    . MET B 1 146 ? 5.652   -45.783 -3.876  1.00 34.17 ? 146  MET B SD    1 
ATOM   5173 C CE    . MET B 1 146 ? 4.046   -45.989 -3.125  1.00 37.30 ? 146  MET B CE    1 
ATOM   5174 N N     . ILE B 1 147 ? 2.488   -42.082 -6.297  1.00 23.53 ? 147  ILE B N     1 
ATOM   5175 C CA    . ILE B 1 147 ? 1.369   -41.403 -5.601  1.00 24.92 ? 147  ILE B CA    1 
ATOM   5176 C C     . ILE B 1 147 ? 1.016   -42.176 -4.329  1.00 25.98 ? 147  ILE B C     1 
ATOM   5177 O O     . ILE B 1 147 ? 1.456   -43.295 -4.155  1.00 24.33 ? 147  ILE B O     1 
ATOM   5178 C CB    . ILE B 1 147 ? 0.152   -41.286 -6.524  1.00 26.71 ? 147  ILE B CB    1 
ATOM   5179 C CG1   . ILE B 1 147 ? -0.495  -42.661 -6.793  1.00 26.13 ? 147  ILE B CG1   1 
ATOM   5180 C CG2   . ILE B 1 147 ? 0.524   -40.558 -7.811  1.00 26.84 ? 147  ILE B CG2   1 
ATOM   5181 C CD1   . ILE B 1 147 ? -1.766  -42.569 -7.600  1.00 23.44 ? 147  ILE B CD1   1 
ATOM   5182 N N     . ASP B 1 148 ? 0.167   -41.558 -3.513  1.00 24.59 ? 148  ASP B N     1 
ATOM   5183 C CA    . ASP B 1 148 ? -0.583  -42.272 -2.474  1.00 25.08 ? 148  ASP B CA    1 
ATOM   5184 C C     . ASP B 1 148 ? -2.066  -42.131 -2.825  1.00 23.39 ? 148  ASP B C     1 
ATOM   5185 O O     . ASP B 1 148 ? -2.554  -40.994 -2.916  1.00 26.87 ? 148  ASP B O     1 
ATOM   5186 C CB    . ASP B 1 148 ? -0.215  -41.729 -1.102  1.00 25.72 ? 148  ASP B CB    1 
ATOM   5187 C CG    . ASP B 1 148 ? -0.954  -42.518 -0.039  1.00 25.91 ? 148  ASP B CG    1 
ATOM   5188 O OD1   . ASP B 1 148 ? -2.182  -42.387 -0.002  1.00 27.40 ? 148  ASP B OD1   1 
ATOM   5189 O OD2   . ASP B 1 148 ? -0.292  -43.308 0.669   1.00 27.32 ? 148  ASP B OD2   1 
ATOM   5190 N N     . CYS B 1 149 ? -2.730  -43.244 -3.116  1.00 24.81 ? 149  CYS B N     1 
ATOM   5191 C CA    . CYS B 1 149 ? -4.137  -43.262 -3.573  1.00 24.21 ? 149  CYS B CA    1 
ATOM   5192 C C     . CYS B 1 149 ? -5.037  -43.926 -2.537  1.00 26.34 ? 149  CYS B C     1 
ATOM   5193 O O     . CYS B 1 149 ? -4.644  -44.853 -1.799  1.00 25.41 ? 149  CYS B O     1 
ATOM   5194 C CB    . CYS B 1 149 ? -4.285  -43.955 -4.928  1.00 27.75 ? 149  CYS B CB    1 
ATOM   5195 S SG    . CYS B 1 149 ? -3.530  -45.598 -4.989  1.00 28.96 ? 149  CYS B SG    1 
ATOM   5196 N N     . PRO B 1 150 ? -6.302  -43.474 -2.499  1.00 26.22 ? 150  PRO B N     1 
ATOM   5197 C CA    . PRO B 1 150 ? -7.337  -44.190 -1.772  1.00 27.73 ? 150  PRO B CA    1 
ATOM   5198 C C     . PRO B 1 150 ? -7.685  -45.468 -2.566  1.00 30.17 ? 150  PRO B C     1 
ATOM   5199 O O     . PRO B 1 150 ? -7.037  -45.775 -3.555  1.00 29.87 ? 150  PRO B O     1 
ATOM   5200 C CB    . PRO B 1 150 ? -8.476  -43.175 -1.738  1.00 25.64 ? 150  PRO B CB    1 
ATOM   5201 C CG    . PRO B 1 150 ? -8.341  -42.433 -3.050  1.00 27.55 ? 150  PRO B CG    1 
ATOM   5202 C CD    . PRO B 1 150 ? -6.847  -42.359 -3.280  1.00 26.93 ? 150  PRO B CD    1 
ATOM   5203 N N     . ASP B 1 151 ? -8.696  -46.188 -2.123  1.00 32.09 ? 151  ASP B N     1 
ATOM   5204 C CA    . ASP B 1 151 ? -9.106  -47.426 -2.789  1.00 31.86 ? 151  ASP B CA    1 
ATOM   5205 C C     . ASP B 1 151 ? -9.463  -47.275 -4.246  1.00 30.97 ? 151  ASP B C     1 
ATOM   5206 O O     . ASP B 1 151 ? -9.230  -48.171 -5.022  1.00 30.16 ? 151  ASP B O     1 
ATOM   5207 C CB    . ASP B 1 151 ? -10.302 -48.032 -2.066  1.00 31.55 ? 151  ASP B CB    1 
ATOM   5208 C CG    . ASP B 1 151 ? -9.955  -48.578 -0.715  1.00 34.10 ? 151  ASP B CG    1 
ATOM   5209 O OD1   . ASP B 1 151 ? -8.772  -48.861 -0.466  1.00 37.85 ? 151  ASP B OD1   1 
ATOM   5210 O OD2   . ASP B 1 151 ? -10.878 -48.728 0.096   1.00 36.67 ? 151  ASP B OD2   1 
ATOM   5211 N N     . LEU B 1 152 ? -10.038 -46.148 -4.605  1.00 31.61 ? 152  LEU B N     1 
ATOM   5212 C CA    . LEU B 1 152 ? -10.479 -45.946 -5.962  1.00 35.62 ? 152  LEU B CA    1 
ATOM   5213 C C     . LEU B 1 152 ? -9.753  -44.797 -6.612  1.00 41.64 ? 152  LEU B C     1 
ATOM   5214 O O     . LEU B 1 152 ? -9.758  -43.690 -6.108  1.00 54.94 ? 152  LEU B O     1 
ATOM   5215 C CB    . LEU B 1 152 ? -11.982 -45.715 -6.013  1.00 32.75 ? 152  LEU B CB    1 
ATOM   5216 C CG    . LEU B 1 152 ? -12.865 -46.680 -5.225  1.00 35.72 ? 152  LEU B CG    1 
ATOM   5217 C CD1   . LEU B 1 152 ? -14.271 -46.132 -5.105  1.00 36.57 ? 152  LEU B CD1   1 
ATOM   5218 C CD2   . LEU B 1 152 ? -12.860 -48.063 -5.847  1.00 35.21 ? 152  LEU B CD2   1 
ATOM   5219 N N     . GLY B 1 153 ? -9.165  -45.045 -7.755  1.00 46.79 ? 153  GLY B N     1 
ATOM   5220 C CA    . GLY B 1 153 ? -8.370  -44.026 -8.395  1.00 48.51 ? 153  GLY B CA    1 
ATOM   5221 C C     . GLY B 1 153 ? -9.029  -42.919 -9.186  1.00 37.03 ? 153  GLY B C     1 
ATOM   5222 O O     . GLY B 1 153 ? -8.347  -42.052 -9.688  1.00 32.98 ? 153  GLY B O     1 
ATOM   5223 N N     . TRP B 1 154 ? -10.339 -42.948 -9.299  1.00 29.76 ? 154  TRP B N     1 
ATOM   5224 C CA    . TRP B 1 154 ? -11.027 -41.940 -10.068 1.00 30.81 ? 154  TRP B CA    1 
ATOM   5225 C C     . TRP B 1 154 ? -11.239 -40.658 -9.291  1.00 28.38 ? 154  TRP B C     1 
ATOM   5226 O O     . TRP B 1 154 ? -11.752 -39.696 -9.819  1.00 31.36 ? 154  TRP B O     1 
ATOM   5227 C CB    . TRP B 1 154 ? -12.348 -42.460 -10.623 1.00 35.57 ? 154  TRP B CB    1 
ATOM   5228 C CG    . TRP B 1 154 ? -13.350 -42.992 -9.644  1.00 36.51 ? 154  TRP B CG    1 
ATOM   5229 C CD1   . TRP B 1 154 ? -13.455 -42.720 -8.312  1.00 35.59 ? 154  TRP B CD1   1 
ATOM   5230 C CD2   . TRP B 1 154 ? -14.413 -43.885 -9.951  1.00 38.75 ? 154  TRP B CD2   1 
ATOM   5231 N NE1   . TRP B 1 154 ? -14.512 -43.391 -7.774  1.00 38.34 ? 154  TRP B NE1   1 
ATOM   5232 C CE2   . TRP B 1 154 ? -15.118 -44.120 -8.760  1.00 41.60 ? 154  TRP B CE2   1 
ATOM   5233 C CE3   . TRP B 1 154 ? -14.835 -44.518 -11.122 1.00 40.12 ? 154  TRP B CE3   1 
ATOM   5234 C CZ2   . TRP B 1 154 ? -16.222 -44.954 -8.705  1.00 41.06 ? 154  TRP B CZ2   1 
ATOM   5235 C CZ3   . TRP B 1 154 ? -15.926 -45.348 -11.064 1.00 45.37 ? 154  TRP B CZ3   1 
ATOM   5236 C CH2   . TRP B 1 154 ? -16.612 -45.557 -9.867  1.00 42.83 ? 154  TRP B CH2   1 
ATOM   5237 N N     . GLY B 1 155 ? -10.874 -40.677 -8.023  1.00 30.39 ? 155  GLY B N     1 
ATOM   5238 C CA    . GLY B 1 155 ? -10.953 -39.475 -7.181  1.00 26.98 ? 155  GLY B CA    1 
ATOM   5239 C C     . GLY B 1 155 ? -9.877  -38.476 -7.565  1.00 27.77 ? 155  GLY B C     1 
ATOM   5240 O O     . GLY B 1 155 ? -9.009  -38.802 -8.446  1.00 28.74 ? 155  GLY B O     1 
ATOM   5241 N N     . SER B 1 156 ? -9.936  -37.304 -6.932  1.00 27.38 ? 156  SER B N     1 
ATOM   5242 C CA    . SER B 1 156 ? -9.075  -36.134 -7.194  1.00 24.86 ? 156  SER B CA    1 
ATOM   5243 C C     . SER B 1 156 ? -7.955  -36.155 -6.159  1.00 27.95 ? 156  SER B C     1 
ATOM   5244 O O     . SER B 1 156 ? -8.281  -36.270 -4.939  1.00 24.80 ? 156  SER B O     1 
ATOM   5245 C CB    . SER B 1 156 ? -9.847  -34.862 -7.132  1.00 25.40 ? 156  SER B CB    1 
ATOM   5246 O OG    . SER B 1 156 ? -8.970  -33.735 -7.100  1.00 24.73 ? 156  SER B OG    1 
ATOM   5247 N N     . VAL B 1 157 ? -6.709  -36.014 -6.598  1.00 25.37 ? 157  VAL B N     1 
ATOM   5248 C CA    . VAL B 1 157 ? -5.571  -35.858 -5.649  1.00 24.76 ? 157  VAL B CA    1 
ATOM   5249 C C     . VAL B 1 157 ? -5.874  -34.655 -4.746  1.00 25.27 ? 157  VAL B C     1 
ATOM   5250 O O     . VAL B 1 157 ? -5.646  -34.739 -3.524  1.00 22.83 ? 157  VAL B O     1 
ATOM   5251 C CB    . VAL B 1 157 ? -4.217  -35.703 -6.350  1.00 26.79 ? 157  VAL B CB    1 
ATOM   5252 C CG1   . VAL B 1 157 ? -3.085  -35.695 -5.328  1.00 27.09 ? 157  VAL B CG1   1 
ATOM   5253 C CG2   . VAL B 1 157 ? -3.976  -36.811 -7.367  1.00 25.47 ? 157  VAL B CG2   1 
ATOM   5254 N N     . VAL B 1 158 ? -6.378  -33.571 -5.319  1.00 22.69 ? 158  VAL B N     1 
ATOM   5255 C CA    . VAL B 1 158 ? -6.768  -32.337 -4.596  1.00 25.35 ? 158  VAL B CA    1 
ATOM   5256 C C     . VAL B 1 158 ? -8.038  -32.567 -3.776  1.00 28.48 ? 158  VAL B C     1 
ATOM   5257 O O     . VAL B 1 158 ? -8.007  -32.316 -2.540  1.00 25.03 ? 158  VAL B O     1 
ATOM   5258 C CB    . VAL B 1 158 ? -6.960  -31.178 -5.586  1.00 26.04 ? 158  VAL B CB    1 
ATOM   5259 C CG1   . VAL B 1 158 ? -7.692  -30.003 -4.953  1.00 26.20 ? 158  VAL B CG1   1 
ATOM   5260 C CG2   . VAL B 1 158 ? -5.631  -30.776 -6.179  1.00 25.44 ? 158  VAL B CG2   1 
ATOM   5261 N N     . GLY B 1 159 ? -9.137  -32.948 -4.426  1.00 25.49 ? 159  GLY B N     1 
ATOM   5262 C CA    . GLY B 1 159 ? -10.435 -33.086 -3.755  1.00 25.11 ? 159  GLY B CA    1 
ATOM   5263 C C     . GLY B 1 159 ? -10.371 -34.019 -2.555  1.00 27.01 ? 159  GLY B C     1 
ATOM   5264 O O     . GLY B 1 159 ? -10.939 -33.670 -1.495  1.00 25.43 ? 159  GLY B O     1 
ATOM   5265 N N     . ASN B 1 160 ? -9.711  -35.150 -2.701  1.00 24.49 ? 160  ASN B N     1 
ATOM   5266 C CA    . ASN B 1 160 ? -9.589  -36.153 -1.614  1.00 25.95 ? 160  ASN B CA    1 
ATOM   5267 C C     . ASN B 1 160 ? -8.852  -35.502 -0.442  1.00 25.66 ? 160  ASN B C     1 
ATOM   5268 O O     . ASN B 1 160 ? -9.378  -35.573 0.710   1.00 24.84 ? 160  ASN B O     1 
ATOM   5269 C CB    . ASN B 1 160 ? -8.959  -37.439 -2.118  1.00 24.38 ? 160  ASN B CB    1 
ATOM   5270 C CG    . ASN B 1 160 ? -8.746  -38.449 -1.017  1.00 27.38 ? 160  ASN B CG    1 
ATOM   5271 O OD1   . ASN B 1 160 ? -7.878  -38.249 -0.174  1.00 30.09 ? 160  ASN B OD1   1 
ATOM   5272 N ND2   . ASN B 1 160 ? -9.533  -39.515 -0.994  1.00 26.13 ? 160  ASN B ND2   1 
ATOM   5273 N N     . ALA B 1 161 ? -7.717  -34.835 -0.720  1.00 22.32 ? 161  ALA B N     1 
ATOM   5274 C CA    . ALA B 1 161 ? -6.934  -34.139 0.334   1.00 24.01 ? 161  ALA B CA    1 
ATOM   5275 C C     . ALA B 1 161 ? -7.788  -33.069 1.037   1.00 25.60 ? 161  ALA B C     1 
ATOM   5276 O O     . ALA B 1 161 ? -7.659  -32.937 2.269   1.00 26.63 ? 161  ALA B O     1 
ATOM   5277 C CB    . ALA B 1 161 ? -5.668  -33.586 -0.252  1.00 23.36 ? 161  ALA B CB    1 
ATOM   5278 N N     . LEU B 1 162 ? -8.655  -32.352 0.303   1.00 25.28 ? 162  LEU B N     1 
ATOM   5279 C CA    . LEU B 1 162 ? -9.481  -31.250 0.868   1.00 24.34 ? 162  LEU B CA    1 
ATOM   5280 C C     . LEU B 1 162 ? -10.586 -31.805 1.776   1.00 26.81 ? 162  LEU B C     1 
ATOM   5281 O O     . LEU B 1 162 ? -11.142 -31.001 2.543   1.00 27.19 ? 162  LEU B O     1 
ATOM   5282 C CB    . LEU B 1 162 ? -10.057 -30.401 -0.264  1.00 25.50 ? 162  LEU B CB    1 
ATOM   5283 C CG    . LEU B 1 162 ? -9.000  -29.615 -1.042  1.00 24.67 ? 162  LEU B CG    1 
ATOM   5284 C CD1   . LEU B 1 162 ? -9.629  -28.756 -2.120  1.00 25.53 ? 162  LEU B CD1   1 
ATOM   5285 C CD2   . LEU B 1 162 ? -8.153  -28.775 -0.102  1.00 26.35 ? 162  LEU B CD2   1 
ATOM   5286 N N     . ASP B 1 163 ? -10.873 -33.110 1.722   1.00 24.39 ? 163  ASP B N     1 
ATOM   5287 C CA    . ASP B 1 163 ? -11.847 -33.728 2.670   1.00 26.53 ? 163  ASP B CA    1 
ATOM   5288 C C     . ASP B 1 163 ? -11.069 -34.489 3.738   1.00 24.87 ? 163  ASP B C     1 
ATOM   5289 O O     . ASP B 1 163 ? -11.725 -35.203 4.523   1.00 30.31 ? 163  ASP B O     1 
ATOM   5290 C CB    . ASP B 1 163 ? -12.891 -34.597 1.956   1.00 26.16 ? 163  ASP B CB    1 
ATOM   5291 C CG    . ASP B 1 163 ? -14.315 -34.384 2.479   1.00 29.17 ? 163  ASP B CG    1 
ATOM   5292 O OD1   . ASP B 1 163 ? -14.606 -33.259 2.933   1.00 28.28 ? 163  ASP B OD1   1 
ATOM   5293 O OD2   . ASP B 1 163 ? -15.119 -35.351 2.475   1.00 29.84 ? 163  ASP B OD2   1 
ATOM   5294 N N     . ARG B 1 164 ? -9.749  -34.286 3.777   1.00 24.40 ? 164  ARG B N     1 
ATOM   5295 C CA    . ARG B 1 164 ? -8.755  -35.079 4.567   1.00 24.84 ? 164  ARG B CA    1 
ATOM   5296 C C     . ARG B 1 164 ? -9.000  -36.581 4.389   1.00 25.06 ? 164  ARG B C     1 
ATOM   5297 O O     . ARG B 1 164 ? -8.971  -37.307 5.365   1.00 25.21 ? 164  ARG B O     1 
ATOM   5298 C CB    . ARG B 1 164 ? -8.775  -34.624 6.027   1.00 25.92 ? 164  ARG B CB    1 
ATOM   5299 C CG    . ARG B 1 164 ? -8.347  -33.175 6.195   1.00 26.83 ? 164  ARG B CG    1 
ATOM   5300 C CD    . ARG B 1 164 ? -7.986  -32.798 7.618   1.00 26.76 ? 164  ARG B CD    1 
ATOM   5301 N NE    . ARG B 1 164 ? -9.132  -33.005 8.486   1.00 25.67 ? 164  ARG B NE    1 
ATOM   5302 C CZ    . ARG B 1 164 ? -10.025 -32.083 8.831   1.00 26.43 ? 164  ARG B CZ    1 
ATOM   5303 N NH1   . ARG B 1 164 ? -9.942  -30.855 8.354   1.00 23.89 ? 164  ARG B NH1   1 
ATOM   5304 N NH2   . ARG B 1 164 ? -11.020 -32.410 9.656   1.00 26.90 ? 164  ARG B NH2   1 
ATOM   5305 N N     . GLY B 1 165 ? -9.120  -37.031 3.138   1.00 25.27 ? 165  GLY B N     1 
ATOM   5306 C CA    . GLY B 1 165 ? -9.076  -38.443 2.752   1.00 24.85 ? 165  GLY B CA    1 
ATOM   5307 C C     . GLY B 1 165 ? -7.674  -39.005 2.935   1.00 26.36 ? 165  GLY B C     1 
ATOM   5308 O O     . GLY B 1 165 ? -6.741  -38.245 3.314   1.00 25.26 ? 165  GLY B O     1 
ATOM   5309 N N     . ALA B 1 166 ? -7.527  -40.302 2.692   1.00 24.13 ? 166  ALA B N     1 
ATOM   5310 C CA    . ALA B 1 166 ? -6.312  -41.042 3.049   1.00 25.46 ? 166  ALA B CA    1 
ATOM   5311 C C     . ALA B 1 166 ? -6.094  -42.232 2.126   1.00 25.53 ? 166  ALA B C     1 
ATOM   5312 O O     . ALA B 1 166 ? -7.074  -42.801 1.603   1.00 25.38 ? 166  ALA B O     1 
ATOM   5313 C CB    . ALA B 1 166 ? -6.389  -41.470 4.492   1.00 26.53 ? 166  ALA B CB    1 
ATOM   5314 N N     . GLY B 1 167 ? -4.823  -42.587 1.977   1.00 24.44 ? 167  GLY B N     1 
ATOM   5315 C CA    . GLY B 1 167 ? -4.372  -43.837 1.348   1.00 26.96 ? 167  GLY B CA    1 
ATOM   5316 C C     . GLY B 1 167 ? -3.546  -44.632 2.322   1.00 25.45 ? 167  GLY B C     1 
ATOM   5317 O O     . GLY B 1 167 ? -3.756  -44.457 3.523   1.00 24.21 ? 167  GLY B O     1 
ATOM   5318 N N     . TYR B 1 168 ? -2.661  -45.491 1.814   1.00 22.93 ? 168  TYR B N     1 
ATOM   5319 C CA    . TYR B 1 168 ? -2.147  -46.659 2.570   1.00 24.74 ? 168  TYR B CA    1 
ATOM   5320 C C     . TYR B 1 168 ? -0.639  -46.828 2.417   1.00 28.21 ? 168  TYR B C     1 
ATOM   5321 O O     . TYR B 1 168 ? -0.086  -47.738 3.063   1.00 26.68 ? 168  TYR B O     1 
ATOM   5322 C CB    . TYR B 1 168 ? -2.949  -47.903 2.164   1.00 25.71 ? 168  TYR B CB    1 
ATOM   5323 C CG    . TYR B 1 168 ? -4.427  -47.674 2.303   1.00 25.08 ? 168  TYR B CG    1 
ATOM   5324 C CD1   . TYR B 1 168 ? -5.050  -47.777 3.537   1.00 27.47 ? 168  TYR B CD1   1 
ATOM   5325 C CD2   . TYR B 1 168 ? -5.175  -47.206 1.242   1.00 26.61 ? 168  TYR B CD2   1 
ATOM   5326 C CE1   . TYR B 1 168 ? -6.406  -47.536 3.681   1.00 27.57 ? 168  TYR B CE1   1 
ATOM   5327 C CE2   . TYR B 1 168 ? -6.526  -46.944 1.367   1.00 26.82 ? 168  TYR B CE2   1 
ATOM   5328 C CZ    . TYR B 1 168 ? -7.145  -47.102 2.594   1.00 26.47 ? 168  TYR B CZ    1 
ATOM   5329 O OH    . TYR B 1 168 ? -8.467  -46.802 2.710   1.00 27.14 ? 168  TYR B OH    1 
ATOM   5330 N N     . THR B 1 169 ? 0.033   -45.966 1.653   1.00 25.24 ? 169  THR B N     1 
ATOM   5331 C CA    . THR B 1 169 ? 1.512   -45.907 1.650   1.00 26.24 ? 169  THR B CA    1 
ATOM   5332 C C     . THR B 1 169 ? 1.957   -45.111 2.872   1.00 25.23 ? 169  THR B C     1 
ATOM   5333 O O     . THR B 1 169 ? 1.131   -44.619 3.637   1.00 28.16 ? 169  THR B O     1 
ATOM   5334 C CB    . THR B 1 169 ? 2.043   -45.323 0.335   1.00 27.86 ? 169  THR B CB    1 
ATOM   5335 O OG1   . THR B 1 169 ? 2.032   -43.895 0.410   1.00 26.32 ? 169  THR B OG1   1 
ATOM   5336 C CG2   . THR B 1 169 ? 1.260   -45.813 -0.862  1.00 25.17 ? 169  THR B CG2   1 
ATOM   5337 N N     . PRO B 1 170 ? 3.280   -44.981 3.118   1.00 25.98 ? 170  PRO B N     1 
ATOM   5338 C CA    . PRO B 1 170 ? 3.768   -44.111 4.180   1.00 26.15 ? 170  PRO B CA    1 
ATOM   5339 C C     . PRO B 1 170 ? 3.285   -42.670 4.012   1.00 23.73 ? 170  PRO B C     1 
ATOM   5340 O O     . PRO B 1 170 ? 3.233   -41.977 5.018   1.00 22.28 ? 170  PRO B O     1 
ATOM   5341 C CB    . PRO B 1 170 ? 5.288   -44.266 4.117   1.00 25.22 ? 170  PRO B CB    1 
ATOM   5342 C CG    . PRO B 1 170 ? 5.488   -45.615 3.479   1.00 25.99 ? 170  PRO B CG    1 
ATOM   5343 C CD    . PRO B 1 170 ? 4.358   -45.757 2.493   1.00 27.82 ? 170  PRO B CD    1 
ATOM   5344 N N     . TYR B 1 171 ? 2.876   -42.278 2.795   1.00 22.27 ? 171  TYR B N     1 
ATOM   5345 C CA    . TYR B 1 171 ? 2.309   -40.937 2.502   1.00 22.30 ? 171  TYR B CA    1 
ATOM   5346 C C     . TYR B 1 171 ? 0.765   -40.978 2.535   1.00 23.55 ? 171  TYR B C     1 
ATOM   5347 O O     . TYR B 1 171 ? 0.111   -40.173 1.827   1.00 24.67 ? 171  TYR B O     1 
ATOM   5348 C CB    . TYR B 1 171 ? 2.902   -40.409 1.190   1.00 21.15 ? 171  TYR B CB    1 
ATOM   5349 C CG    . TYR B 1 171 ? 4.242   -39.715 1.285   1.00 22.34 ? 171  TYR B CG    1 
ATOM   5350 C CD1   . TYR B 1 171 ? 5.291   -40.222 2.028   1.00 23.21 ? 171  TYR B CD1   1 
ATOM   5351 C CD2   . TYR B 1 171 ? 4.493   -38.580 0.536   1.00 21.60 ? 171  TYR B CD2   1 
ATOM   5352 C CE1   . TYR B 1 171 ? 6.532   -39.598 2.080   1.00 25.15 ? 171  TYR B CE1   1 
ATOM   5353 C CE2   . TYR B 1 171 ? 5.729   -37.966 0.540   1.00 22.82 ? 171  TYR B CE2   1 
ATOM   5354 C CZ    . TYR B 1 171 ? 6.753   -38.459 1.336   1.00 24.86 ? 171  TYR B CZ    1 
ATOM   5355 O OH    . TYR B 1 171 ? 7.943   -37.786 1.380   1.00 24.89 ? 171  TYR B OH    1 
ATOM   5356 N N     . GLY B 1 172 ? 0.183   -41.830 3.386   1.00 22.79 ? 172  GLY B N     1 
ATOM   5357 C CA    . GLY B 1 172 ? -1.280  -42.054 3.451   1.00 24.11 ? 172  GLY B CA    1 
ATOM   5358 C C     . GLY B 1 172 ? -2.057  -40.848 3.936   1.00 23.36 ? 172  GLY B C     1 
ATOM   5359 O O     . GLY B 1 172 ? -3.208  -40.718 3.548   1.00 24.71 ? 172  GLY B O     1 
ATOM   5360 N N     . ASP B 1 173 ? -1.477  -39.995 4.786   1.00 22.00 ? 173  ASP B N     1 
ATOM   5361 C CA    . ASP B 1 173 ? -2.192  -38.795 5.294   1.00 24.07 ? 173  ASP B CA    1 
ATOM   5362 C C     . ASP B 1 173 ? -2.099  -37.693 4.235   1.00 23.99 ? 173  ASP B C     1 
ATOM   5363 O O     . ASP B 1 173 ? -1.092  -37.005 4.191   1.00 25.97 ? 173  ASP B O     1 
ATOM   5364 C CB    . ASP B 1 173 ? -1.628  -38.340 6.635   1.00 28.19 ? 173  ASP B CB    1 
ATOM   5365 C CG    . ASP B 1 173 ? -2.377  -37.165 7.233   1.00 28.21 ? 173  ASP B CG    1 
ATOM   5366 O OD1   . ASP B 1 173 ? -3.110  -36.490 6.493   1.00 29.37 ? 173  ASP B OD1   1 
ATOM   5367 O OD2   . ASP B 1 173 ? -2.173  -36.918 8.425   1.00 28.36 ? 173  ASP B OD2   1 
ATOM   5368 N N     . HIS B 1 174 ? -3.089  -37.582 3.361   1.00 25.53 ? 174  HIS B N     1 
ATOM   5369 C CA    . HIS B 1 174 ? -3.025  -36.714 2.152   1.00 23.07 ? 174  HIS B CA    1 
ATOM   5370 C C     . HIS B 1 174 ? -2.832  -35.259 2.553   1.00 24.34 ? 174  HIS B C     1 
ATOM   5371 O O     . HIS B 1 174 ? -2.012  -34.568 1.945   1.00 25.44 ? 174  HIS B O     1 
ATOM   5372 C CB    . HIS B 1 174 ? -4.265  -36.952 1.291   1.00 24.55 ? 174  HIS B CB    1 
ATOM   5373 C CG    . HIS B 1 174 ? -4.239  -38.319 0.701   1.00 27.34 ? 174  HIS B CG    1 
ATOM   5374 N ND1   . HIS B 1 174 ? -5.328  -38.873 0.053   1.00 26.34 ? 174  HIS B ND1   1 
ATOM   5375 C CD2   . HIS B 1 174 ? -3.242  -39.231 0.634   1.00 25.46 ? 174  HIS B CD2   1 
ATOM   5376 C CE1   . HIS B 1 174 ? -4.999  -40.072 -0.380  1.00 26.53 ? 174  HIS B CE1   1 
ATOM   5377 N NE2   . HIS B 1 174 ? -3.729  -40.318 -0.042  1.00 25.73 ? 174  HIS B NE2   1 
ATOM   5378 N N     . PHE B 1 175 ? -3.577  -34.795 3.548   1.00 25.94 ? 175  PHE B N     1 
ATOM   5379 C CA    . PHE B 1 175 ? -3.480  -33.401 4.014   1.00 29.18 ? 175  PHE B CA    1 
ATOM   5380 C C     . PHE B 1 175 ? -2.051  -33.122 4.509   1.00 27.57 ? 175  PHE B C     1 
ATOM   5381 O O     . PHE B 1 175 ? -1.552  -32.049 4.227   1.00 28.84 ? 175  PHE B O     1 
ATOM   5382 C CB    . PHE B 1 175 ? -4.518  -33.076 5.087   1.00 29.61 ? 175  PHE B CB    1 
ATOM   5383 C CG    . PHE B 1 175 ? -4.235  -31.704 5.648   1.00 33.09 ? 175  PHE B CG    1 
ATOM   5384 C CD1   . PHE B 1 175 ? -4.411  -30.574 4.863   1.00 34.55 ? 175  PHE B CD1   1 
ATOM   5385 C CD2   . PHE B 1 175 ? -3.600  -31.563 6.867   1.00 36.29 ? 175  PHE B CD2   1 
ATOM   5386 C CE1   . PHE B 1 175 ? -4.067  -29.316 5.337   1.00 33.56 ? 175  PHE B CE1   1 
ATOM   5387 C CE2   . PHE B 1 175 ? -3.237  -30.307 7.334   1.00 34.23 ? 175  PHE B CE2   1 
ATOM   5388 C CZ    . PHE B 1 175 ? -3.498  -29.189 6.579   1.00 33.80 ? 175  PHE B CZ    1 
ATOM   5389 N N     . MET B 1 176 ? -1.436  -34.055 5.233   1.00 26.52 ? 176  MET B N     1 
ATOM   5390 C CA    . MET B 1 176 ? -0.075  -33.894 5.802   1.00 26.33 ? 176  MET B CA    1 
ATOM   5391 C C     . MET B 1 176 ? 0.867   -33.567 4.644   1.00 23.95 ? 176  MET B C     1 
ATOM   5392 O O     . MET B 1 176 ? 1.676   -32.697 4.804   1.00 22.88 ? 176  MET B O     1 
ATOM   5393 C CB    . MET B 1 176 ? 0.396   -35.167 6.524   1.00 30.17 ? 176  MET B CB    1 
ATOM   5394 C CG    . MET B 1 176 ? 1.906   -35.248 6.821   1.00 38.24 ? 176  MET B CG    1 
ATOM   5395 S SD    . MET B 1 176 ? 2.348   -36.794 7.739   1.00 44.09 ? 176  MET B SD    1 
ATOM   5396 C CE    . MET B 1 176 ? 1.523   -36.509 9.305   1.00 51.44 ? 176  MET B CE    1 
ATOM   5397 N N     . TRP B 1 177 ? 0.730   -34.234 3.504   1.00 22.35 ? 177  TRP B N     1 
ATOM   5398 C CA    . TRP B 1 177 ? 1.692   -34.117 2.382   1.00 22.03 ? 177  TRP B CA    1 
ATOM   5399 C C     . TRP B 1 177 ? 1.273   -33.003 1.419   1.00 22.41 ? 177  TRP B C     1 
ATOM   5400 O O     . TRP B 1 177 ? 2.108   -32.594 0.603   1.00 22.74 ? 177  TRP B O     1 
ATOM   5401 C CB    . TRP B 1 177 ? 1.893   -35.484 1.718   1.00 23.37 ? 177  TRP B CB    1 
ATOM   5402 C CG    . TRP B 1 177 ? 2.518   -36.427 2.691   1.00 22.70 ? 177  TRP B CG    1 
ATOM   5403 C CD1   . TRP B 1 177 ? 1.896   -37.465 3.316   1.00 25.93 ? 177  TRP B CD1   1 
ATOM   5404 C CD2   . TRP B 1 177 ? 3.816   -36.321 3.285   1.00 23.88 ? 177  TRP B CD2   1 
ATOM   5405 N NE1   . TRP B 1 177 ? 2.731   -38.039 4.232   1.00 26.14 ? 177  TRP B NE1   1 
ATOM   5406 C CE2   . TRP B 1 177 ? 3.930   -37.372 4.218   1.00 26.28 ? 177  TRP B CE2   1 
ATOM   5407 C CE3   . TRP B 1 177 ? 4.917   -35.475 3.090   1.00 25.51 ? 177  TRP B CE3   1 
ATOM   5408 C CZ2   . TRP B 1 177 ? 5.091   -37.582 4.961   1.00 28.24 ? 177  TRP B CZ2   1 
ATOM   5409 C CZ3   . TRP B 1 177 ? 6.063   -35.682 3.829   1.00 26.21 ? 177  TRP B CZ3   1 
ATOM   5410 C CH2   . TRP B 1 177 ? 6.152   -36.723 4.749   1.00 26.07 ? 177  TRP B CH2   1 
ATOM   5411 N N     . GLN B 1 178 ? 0.055   -32.492 1.533   1.00 22.25 ? 178  GLN B N     1 
ATOM   5412 C CA    . GLN B 1 178 ? -0.353  -31.238 0.852   1.00 22.97 ? 178  GLN B CA    1 
ATOM   5413 C C     . GLN B 1 178 ? 0.640   -30.130 1.243   1.00 23.04 ? 178  GLN B C     1 
ATOM   5414 O O     . GLN B 1 178 ? 0.937   -29.962 2.423   1.00 21.81 ? 178  GLN B O     1 
ATOM   5415 C CB    . GLN B 1 178 ? -1.802  -30.889 1.156   1.00 23.04 ? 178  GLN B CB    1 
ATOM   5416 C CG    . GLN B 1 178 ? -2.225  -29.552 0.563   1.00 26.06 ? 178  GLN B CG    1 
ATOM   5417 C CD    . GLN B 1 178 ? -2.040  -28.376 1.485   1.00 25.64 ? 178  GLN B CD    1 
ATOM   5418 O OE1   . GLN B 1 178 ? -2.254  -28.505 2.689   1.00 27.90 ? 178  GLN B OE1   1 
ATOM   5419 N NE2   . GLN B 1 178 ? -1.701  -27.215 0.923   1.00 24.72 ? 178  GLN B NE2   1 
ATOM   5420 N N     . THR B 1 179 ? 1.182   -29.424 0.262   1.00 20.42 ? 179  THR B N     1 
ATOM   5421 C CA    . THR B 1 179 ? 2.220   -28.390 0.471   1.00 20.19 ? 179  THR B CA    1 
ATOM   5422 C C     . THR B 1 179 ? 1.934   -27.195 -0.444  1.00 21.23 ? 179  THR B C     1 
ATOM   5423 O O     . THR B 1 179 ? 2.217   -27.295 -1.635  1.00 24.17 ? 179  THR B O     1 
ATOM   5424 C CB    . THR B 1 179 ? 3.626   -28.975 0.272   1.00 22.15 ? 179  THR B CB    1 
ATOM   5425 O OG1   . THR B 1 179 ? 3.713   -30.236 0.946   1.00 22.75 ? 179  THR B OG1   1 
ATOM   5426 C CG2   . THR B 1 179 ? 4.684   -28.015 0.773   1.00 24.71 ? 179  THR B CG2   1 
ATOM   5427 N N     . GLY B 1 180 ? 1.358   -26.125 0.099   1.00 19.25 ? 180  GLY B N     1 
ATOM   5428 C CA    . GLY B 1 180 ? 0.952   -24.972 -0.726  1.00 20.49 ? 180  GLY B CA    1 
ATOM   5429 C C     . GLY B 1 180 ? -0.388  -25.181 -1.409  1.00 20.24 ? 180  GLY B C     1 
ATOM   5430 O O     . GLY B 1 180 ? -0.717  -26.328 -1.834  1.00 22.33 ? 180  GLY B O     1 
ATOM   5431 N N     . MET B 1 181 ? -1.148  -24.091 -1.453  1.00 22.00 ? 181  MET B N     1 
ATOM   5432 C CA    . MET B 1 181 ? -2.480  -23.969 -2.075  1.00 25.72 ? 181  MET B CA    1 
ATOM   5433 C C     . MET B 1 181 ? -2.585  -22.611 -2.728  1.00 23.96 ? 181  MET B C     1 
ATOM   5434 O O     . MET B 1 181 ? -2.154  -21.597 -2.083  1.00 23.09 ? 181  MET B O     1 
ATOM   5435 C CB    . MET B 1 181 ? -3.539  -23.859 -0.987  1.00 29.76 ? 181  MET B CB    1 
ATOM   5436 C CG    . MET B 1 181 ? -4.278  -25.016 -0.782  1.00 38.49 ? 181  MET B CG    1 
ATOM   5437 S SD    . MET B 1 181 ? -5.467  -24.555 0.491   1.00 32.47 ? 181  MET B SD    1 
ATOM   5438 C CE    . MET B 1 181 ? -5.474  -26.211 1.147   1.00 35.40 ? 181  MET B CE    1 
ATOM   5439 N N     . GLU B 1 182 ? -3.340  -22.563 -3.821  1.00 22.23 ? 182  GLU B N     1 
ATOM   5440 C CA    . GLU B 1 182 ? -3.988  -21.326 -4.303  1.00 23.40 ? 182  GLU B CA    1 
ATOM   5441 C C     . GLU B 1 182 ? -5.484  -21.469 -4.037  1.00 22.50 ? 182  GLU B C     1 
ATOM   5442 O O     . GLU B 1 182 ? -6.056  -22.509 -4.389  1.00 22.34 ? 182  GLU B O     1 
ATOM   5443 C CB    . GLU B 1 182 ? -3.676  -21.116 -5.789  1.00 23.91 ? 182  GLU B CB    1 
ATOM   5444 C CG    . GLU B 1 182 ? -4.138  -19.785 -6.323  1.00 24.97 ? 182  GLU B CG    1 
ATOM   5445 C CD    . GLU B 1 182 ? -3.773  -19.667 -7.792  1.00 26.54 ? 182  GLU B CD    1 
ATOM   5446 O OE1   . GLU B 1 182 ? -4.472  -20.279 -8.585  1.00 24.01 ? 182  GLU B OE1   1 
ATOM   5447 O OE2   . GLU B 1 182 ? -2.702  -19.066 -8.106  1.00 25.69 ? 182  GLU B OE2   1 
ATOM   5448 N N     . VAL B 1 183 ? -6.095  -20.441 -3.451  1.00 23.79 ? 183  VAL B N     1 
ATOM   5449 C CA    . VAL B 1 183 ? -7.514  -20.526 -3.038  1.00 23.16 ? 183  VAL B CA    1 
ATOM   5450 C C     . VAL B 1 183 ? -8.206  -19.221 -3.386  1.00 25.74 ? 183  VAL B C     1 
ATOM   5451 O O     . VAL B 1 183 ? -7.635  -18.127 -3.134  1.00 24.75 ? 183  VAL B O     1 
ATOM   5452 C CB    . VAL B 1 183 ? -7.630  -20.894 -1.549  1.00 23.29 ? 183  VAL B CB    1 
ATOM   5453 C CG1   . VAL B 1 183 ? -6.967  -19.879 -0.651  1.00 24.55 ? 183  VAL B CG1   1 
ATOM   5454 C CG2   . VAL B 1 183 ? -9.082  -21.110 -1.164  1.00 23.63 ? 183  VAL B CG2   1 
ATOM   5455 N N     . VAL B 1 184 ? -9.400  -19.330 -3.955  1.00 25.11 ? 184  VAL B N     1 
ATOM   5456 C CA    . VAL B 1 184 ? -10.282 -18.159 -4.170  1.00 24.12 ? 184  VAL B CA    1 
ATOM   5457 C C     . VAL B 1 184 ? -11.160 -18.035 -2.928  1.00 23.93 ? 184  VAL B C     1 
ATOM   5458 O O     . VAL B 1 184 ? -11.914 -18.993 -2.604  1.00 22.12 ? 184  VAL B O     1 
ATOM   5459 C CB    . VAL B 1 184 ? -11.096 -18.268 -5.469  1.00 24.31 ? 184  VAL B CB    1 
ATOM   5460 C CG1   . VAL B 1 184 ? -12.060 -17.105 -5.559  1.00 27.81 ? 184  VAL B CG1   1 
ATOM   5461 C CG2   . VAL B 1 184 ? -10.182 -18.333 -6.684  1.00 27.76 ? 184  VAL B CG2   1 
ATOM   5462 N N     . LEU B 1 185 ? -11.032 -16.903 -2.250  1.00 24.62 ? 185  LEU B N     1 
ATOM   5463 C CA    . LEU B 1 185 ? -11.756 -16.640 -0.985  1.00 24.53 ? 185  LEU B CA    1 
ATOM   5464 C C     . LEU B 1 185 ? -13.196 -16.247 -1.312  1.00 25.96 ? 185  LEU B C     1 
ATOM   5465 O O     . LEU B 1 185 ? -13.548 -16.021 -2.472  1.00 24.01 ? 185  LEU B O     1 
ATOM   5466 C CB    . LEU B 1 185 ? -10.973 -15.593 -0.198  1.00 24.24 ? 185  LEU B CB    1 
ATOM   5467 C CG    . LEU B 1 185 ? -9.604  -16.096 0.275   1.00 24.61 ? 185  LEU B CG    1 
ATOM   5468 C CD1   . LEU B 1 185 ? -8.769  -14.976 0.868   1.00 26.40 ? 185  LEU B CD1   1 
ATOM   5469 C CD2   . LEU B 1 185 ? -9.771  -17.209 1.293   1.00 23.42 ? 185  LEU B CD2   1 
ATOM   5470 N N     . PRO B 1 186 ? -14.117 -16.314 -0.333  1.00 23.83 ? 186  PRO B N     1 
ATOM   5471 C CA    . PRO B 1 186 ? -15.541 -16.309 -0.654  1.00 26.87 ? 186  PRO B CA    1 
ATOM   5472 C C     . PRO B 1 186 ? -16.105 -15.065 -1.354  1.00 25.25 ? 186  PRO B C     1 
ATOM   5473 O O     . PRO B 1 186 ? -17.186 -15.186 -1.862  1.00 27.97 ? 186  PRO B O     1 
ATOM   5474 C CB    . PRO B 1 186 ? -16.209 -16.553 0.711   1.00 26.52 ? 186  PRO B CB    1 
ATOM   5475 C CG    . PRO B 1 186 ? -15.144 -17.288 1.481   1.00 25.73 ? 186  PRO B CG    1 
ATOM   5476 C CD    . PRO B 1 186 ? -13.854 -16.616 1.074   1.00 24.05 ? 186  PRO B CD    1 
ATOM   5477 N N     . GLN B 1 187 ? -15.372 -13.945 -1.367  1.00 27.15 ? 187  GLN B N     1 
ATOM   5478 C CA    . GLN B 1 187 ? -15.770 -12.715 -2.095  1.00 28.83 ? 187  GLN B CA    1 
ATOM   5479 C C     . GLN B 1 187 ? -15.006 -12.588 -3.414  1.00 29.49 ? 187  GLN B C     1 
ATOM   5480 O O     . GLN B 1 187 ? -15.230 -11.581 -4.111  1.00 30.63 ? 187  GLN B O     1 
ATOM   5481 C CB    . GLN B 1 187 ? -15.598 -11.488 -1.207  1.00 32.27 ? 187  GLN B CB    1 
ATOM   5482 C CG    . GLN B 1 187 ? -16.512 -11.516 0.001   1.00 32.21 ? 187  GLN B CG    1 
ATOM   5483 C CD    . GLN B 1 187 ? -16.339 -10.280 0.845   1.00 35.86 ? 187  GLN B CD    1 
ATOM   5484 O OE1   . GLN B 1 187 ? -15.540 -10.263 1.774   1.00 37.17 ? 187  GLN B OE1   1 
ATOM   5485 N NE2   . GLN B 1 187 ? -17.104 -9.243  0.549   1.00 35.71 ? 187  GLN B NE2   1 
ATOM   5486 N N     . GLY B 1 188 ? -14.137 -13.543 -3.745  1.00 25.58 ? 188  GLY B N     1 
ATOM   5487 C CA    . GLY B 1 188 ? -13.486 -13.592 -5.072  1.00 27.25 ? 188  GLY B CA    1 
ATOM   5488 C C     . GLY B 1 188 ? -12.020 -13.197 -5.074  1.00 27.86 ? 188  GLY B C     1 
ATOM   5489 O O     . GLY B 1 188 ? -11.424 -13.272 -6.141  1.00 32.07 ? 188  GLY B O     1 
ATOM   5490 N N     . ASP B 1 189 ? -11.434 -12.849 -3.934  1.00 32.25 ? 189  ASP B N     1 
ATOM   5491 C CA    . ASP B 1 189 ? -9.976  -12.558 -3.797  1.00 32.24 ? 189  ASP B CA    1 
ATOM   5492 C C     . ASP B 1 189 ? -9.223  -13.878 -3.943  1.00 30.43 ? 189  ASP B C     1 
ATOM   5493 O O     . ASP B 1 189 ? -9.759  -14.908 -3.517  1.00 35.09 ? 189  ASP B O     1 
ATOM   5494 C CB    . ASP B 1 189 ? -9.684  -11.855 -2.472  1.00 33.19 ? 189  ASP B CB    1 
ATOM   5495 C CG    . ASP B 1 189 ? -10.504 -10.582 -2.320  1.00 38.41 ? 189  ASP B CG    1 
ATOM   5496 O OD1   . ASP B 1 189 ? -10.251 -9.667  -3.084  1.00 39.46 ? 189  ASP B OD1   1 
ATOM   5497 O OD2   . ASP B 1 189 ? -11.459 -10.575 -1.517  1.00 38.17 ? 189  ASP B OD2   1 
ATOM   5498 N N     . VAL B 1 190 ? -8.048  -13.878 -4.559  1.00 26.63 ? 190  VAL B N     1 
ATOM   5499 C CA    . VAL B 1 190 ? -7.220  -15.111 -4.642  1.00 26.16 ? 190  VAL B CA    1 
ATOM   5500 C C     . VAL B 1 190 ? -6.019  -14.913 -3.739  1.00 24.65 ? 190  VAL B C     1 
ATOM   5501 O O     . VAL B 1 190 ? -5.501  -13.793 -3.641  1.00 22.80 ? 190  VAL B O     1 
ATOM   5502 C CB    . VAL B 1 190 ? -6.712  -15.489 -6.045  1.00 28.63 ? 190  VAL B CB    1 
ATOM   5503 C CG1   . VAL B 1 190 ? -7.788  -16.161 -6.844  1.00 36.85 ? 190  VAL B CG1   1 
ATOM   5504 C CG2   . VAL B 1 190 ? -6.095  -14.306 -6.774  1.00 27.93 ? 190  VAL B CG2   1 
ATOM   5505 N N     . MET B 1 191 ? -5.601  -16.003 -3.126  1.00 22.60 ? 191  MET B N     1 
ATOM   5506 C CA    . MET B 1 191 ? -4.482  -15.990 -2.188  1.00 23.58 ? 191  MET B CA    1 
ATOM   5507 C C     . MET B 1 191 ? -3.680  -17.276 -2.367  1.00 22.70 ? 191  MET B C     1 
ATOM   5508 O O     . MET B 1 191 ? -4.297  -18.338 -2.635  1.00 23.23 ? 191  MET B O     1 
ATOM   5509 C CB    . MET B 1 191 ? -5.064  -15.837 -0.786  1.00 26.53 ? 191  MET B CB    1 
ATOM   5510 C CG    . MET B 1 191 ? -4.272  -16.462 0.256   1.00 28.62 ? 191  MET B CG    1 
ATOM   5511 S SD    . MET B 1 191 ? -4.993  -16.105 1.900   1.00 26.29 ? 191  MET B SD    1 
ATOM   5512 C CE    . MET B 1 191 ? -5.646  -17.735 2.255   1.00 25.87 ? 191  MET B CE    1 
ATOM   5513 N N     . ARG B 1 192 ? -2.356  -17.195 -2.236  1.00 20.83 ? 192  ARG B N     1 
ATOM   5514 C CA    . ARG B 1 192 ? -1.502  -18.390 -2.132  1.00 19.93 ? 192  ARG B CA    1 
ATOM   5515 C C     . ARG B 1 192 ? -1.014  -18.572 -0.701  1.00 20.03 ? 192  ARG B C     1 
ATOM   5516 O O     . ARG B 1 192 ? -0.639  -17.576 -0.038  1.00 19.55 ? 192  ARG B O     1 
ATOM   5517 C CB    . ARG B 1 192 ? -0.330  -18.311 -3.101  1.00 21.64 ? 192  ARG B CB    1 
ATOM   5518 C CG    . ARG B 1 192 ? -0.810  -18.356 -4.538  1.00 21.46 ? 192  ARG B CG    1 
ATOM   5519 C CD    . ARG B 1 192 ? 0.330   -18.429 -5.530  1.00 22.67 ? 192  ARG B CD    1 
ATOM   5520 N NE    . ARG B 1 192 ? -0.151  -18.756 -6.854  1.00 22.86 ? 192  ARG B NE    1 
ATOM   5521 C CZ    . ARG B 1 192 ? 0.642   -19.024 -7.888  1.00 24.16 ? 192  ARG B CZ    1 
ATOM   5522 N NH1   . ARG B 1 192 ? 1.957   -18.945 -7.763  1.00 22.94 ? 192  ARG B NH1   1 
ATOM   5523 N NH2   . ARG B 1 192 ? 0.104   -19.356 -9.050  1.00 25.56 ? 192  ARG B NH2   1 
ATOM   5524 N N     . THR B 1 193 ? -0.981  -19.823 -0.254  1.00 21.02 ? 193  THR B N     1 
ATOM   5525 C CA    . THR B 1 193 ? -0.542  -20.129 1.133   1.00 21.90 ? 193  THR B CA    1 
ATOM   5526 C C     . THR B 1 193 ? 0.952   -20.414 1.151   1.00 22.41 ? 193  THR B C     1 
ATOM   5527 O O     . THR B 1 193 ? 1.542   -20.686 0.108   1.00 22.39 ? 193  THR B O     1 
ATOM   5528 C CB    . THR B 1 193 ? -1.343  -21.281 1.741   1.00 23.42 ? 193  THR B CB    1 
ATOM   5529 O OG1   . THR B 1 193 ? -1.023  -22.503 1.069   1.00 26.35 ? 193  THR B OG1   1 
ATOM   5530 C CG2   . THR B 1 193 ? -2.831  -21.013 1.742   1.00 25.72 ? 193  THR B CG2   1 
ATOM   5531 N N     . GLY B 1 194 ? 1.531   -20.423 2.342   1.00 20.94 ? 194  GLY B N     1 
ATOM   5532 C CA    . GLY B 1 194 ? 2.897   -20.878 2.567   1.00 21.32 ? 194  GLY B CA    1 
ATOM   5533 C C     . GLY B 1 194 ? 3.884   -20.011 1.805   1.00 21.70 ? 194  GLY B C     1 
ATOM   5534 O O     . GLY B 1 194 ? 3.701   -18.764 1.715   1.00 19.85 ? 194  GLY B O     1 
ATOM   5535 N N     . MET B 1 195 ? 4.921   -20.652 1.299   1.00 22.05 ? 195  MET B N     1 
ATOM   5536 C CA    . MET B 1 195 ? 6.045   -19.951 0.636   1.00 25.67 ? 195  MET B CA    1 
ATOM   5537 C C     . MET B 1 195 ? 5.585   -19.420 -0.729  1.00 25.33 ? 195  MET B C     1 
ATOM   5538 O O     . MET B 1 195 ? 6.327   -18.579 -1.294  1.00 23.09 ? 195  MET B O     1 
ATOM   5539 C CB    . MET B 1 195 ? 7.256   -20.876 0.471   1.00 26.77 ? 195  MET B CB    1 
ATOM   5540 C CG    . MET B 1 195 ? 7.785   -21.415 1.782   1.00 30.60 ? 195  MET B CG    1 
ATOM   5541 S SD    . MET B 1 195 ? 8.130   -20.067 2.925   1.00 32.50 ? 195  MET B SD    1 
ATOM   5542 C CE    . MET B 1 195 ? 9.530   -19.294 2.156   1.00 32.29 ? 195  MET B CE    1 
ATOM   5543 N N     . GLY B 1 196 ? 4.403   -19.847 -1.204  1.00 23.69 ? 196  GLY B N     1 
ATOM   5544 C CA    . GLY B 1 196 ? 3.786   -19.331 -2.445  1.00 22.70 ? 196  GLY B CA    1 
ATOM   5545 C C     . GLY B 1 196 ? 3.333   -17.892 -2.324  1.00 23.06 ? 196  GLY B C     1 
ATOM   5546 O O     . GLY B 1 196 ? 3.136   -17.265 -3.370  1.00 21.33 ? 196  GLY B O     1 
ATOM   5547 N N     . ALA B 1 197 ? 3.142   -17.360 -1.101  1.00 20.60 ? 197  ALA B N     1 
ATOM   5548 C CA    . ALA B 1 197 ? 2.731   -15.957 -0.862  1.00 20.64 ? 197  ALA B CA    1 
ATOM   5549 C C     . ALA B 1 197 ? 3.866   -14.999 -1.210  1.00 18.33 ? 197  ALA B C     1 
ATOM   5550 O O     . ALA B 1 197 ? 3.611   -13.761 -1.317  1.00 20.59 ? 197  ALA B O     1 
ATOM   5551 C CB    . ALA B 1 197 ? 2.274   -15.741 0.576   1.00 18.37 ? 197  ALA B CB    1 
ATOM   5552 N N     . LEU B 1 198 ? 5.089   -15.507 -1.310  1.00 21.18 ? 198  LEU B N     1 
ATOM   5553 C CA    . LEU B 1 198 ? 6.275   -14.712 -1.693  1.00 21.77 ? 198  LEU B CA    1 
ATOM   5554 C C     . LEU B 1 198 ? 6.400   -14.769 -3.216  1.00 20.34 ? 198  LEU B C     1 
ATOM   5555 O O     . LEU B 1 198 ? 6.723   -15.816 -3.759  1.00 20.42 ? 198  LEU B O     1 
ATOM   5556 C CB    . LEU B 1 198 ? 7.514   -15.316 -1.042  1.00 26.42 ? 198  LEU B CB    1 
ATOM   5557 C CG    . LEU B 1 198 ? 8.807   -14.511 -1.220  1.00 31.00 ? 198  LEU B CG    1 
ATOM   5558 C CD1   . LEU B 1 198 ? 9.253   -13.958 0.126   1.00 36.62 ? 198  LEU B CD1   1 
ATOM   5559 C CD2   . LEU B 1 198 ? 9.916   -15.375 -1.765  1.00 31.89 ? 198  LEU B CD2   1 
ATOM   5560 N N     . PRO B 1 199 ? 6.172   -13.665 -3.943  1.00 22.93 ? 199  PRO B N     1 
ATOM   5561 C CA    . PRO B 1 199 ? 6.314   -13.674 -5.399  1.00 20.13 ? 199  PRO B CA    1 
ATOM   5562 C C     . PRO B 1 199 ? 7.719   -14.129 -5.793  1.00 19.65 ? 199  PRO B C     1 
ATOM   5563 O O     . PRO B 1 199 ? 8.643   -13.683 -5.217  1.00 18.60 ? 199  PRO B O     1 
ATOM   5564 C CB    . PRO B 1 199 ? 6.058   -12.228 -5.803  1.00 21.52 ? 199  PRO B CB    1 
ATOM   5565 C CG    . PRO B 1 199 ? 5.222   -11.669 -4.674  1.00 23.36 ? 199  PRO B CG    1 
ATOM   5566 C CD    . PRO B 1 199 ? 5.744   -12.358 -3.430  1.00 21.54 ? 199  PRO B CD    1 
ATOM   5567 N N     . GLY B 1 200 ? 7.795   -15.054 -6.738  1.00 21.39 ? 200  GLY B N     1 
ATOM   5568 C CA    . GLY B 1 200 ? 9.048   -15.649 -7.237  1.00 22.64 ? 200  GLY B CA    1 
ATOM   5569 C C     . GLY B 1 200 ? 9.671   -16.668 -6.296  1.00 20.42 ? 200  GLY B C     1 
ATOM   5570 O O     . GLY B 1 200 ? 10.807  -17.113 -6.567  1.00 22.41 ? 200  GLY B O     1 
ATOM   5571 N N     . SER B 1 201 ? 9.005   -17.081 -5.209  1.00 21.12 ? 201  SER B N     1 
ATOM   5572 C CA    . SER B 1 201 ? 9.572   -18.120 -4.322  1.00 24.51 ? 201  SER B CA    1 
ATOM   5573 C C     . SER B 1 201 ? 9.855   -19.388 -5.126  1.00 20.11 ? 201  SER B C     1 
ATOM   5574 O O     . SER B 1 201 ? 9.112   -19.685 -6.053  1.00 22.57 ? 201  SER B O     1 
ATOM   5575 C CB    . SER B 1 201 ? 8.709   -18.486 -3.147  1.00 26.64 ? 201  SER B CB    1 
ATOM   5576 O OG    . SER B 1 201 ? 7.477   -18.966 -3.608  1.00 33.15 ? 201  SER B OG    1 
ATOM   5577 N N     . THR B 1 202 ? 10.830  -20.146 -4.672  1.00 22.37 ? 202  THR B N     1 
ATOM   5578 C CA    . THR B 1 202 ? 11.258  -21.421 -5.290  1.00 23.87 ? 202  THR B CA    1 
ATOM   5579 C C     . THR B 1 202 ? 10.913  -22.585 -4.364  1.00 22.41 ? 202  THR B C     1 
ATOM   5580 O O     . THR B 1 202 ? 11.379  -23.694 -4.615  1.00 23.99 ? 202  THR B O     1 
ATOM   5581 C CB    . THR B 1 202 ? 12.733  -21.259 -5.642  1.00 25.62 ? 202  THR B CB    1 
ATOM   5582 O OG1   . THR B 1 202 ? 13.473  -20.860 -4.485  1.00 27.22 ? 202  THR B OG1   1 
ATOM   5583 C CG2   . THR B 1 202 ? 12.884  -20.238 -6.745  1.00 27.71 ? 202  THR B CG2   1 
ATOM   5584 N N     . THR B 1 203 ? 10.153  -22.325 -3.311  1.00 23.39 ? 203  THR B N     1 
ATOM   5585 C CA    . THR B 1 203 ? 9.976   -23.275 -2.186  1.00 21.77 ? 203  THR B CA    1 
ATOM   5586 C C     . THR B 1 203 ? 8.500   -23.587 -1.901  1.00 21.91 ? 203  THR B C     1 
ATOM   5587 O O     . THR B 1 203 ? 8.239   -24.239 -0.873  1.00 21.04 ? 203  THR B O     1 
ATOM   5588 C CB    . THR B 1 203 ? 10.632  -22.679 -0.930  1.00 23.14 ? 203  THR B CB    1 
ATOM   5589 O OG1   . THR B 1 203 ? 10.002  -21.440 -0.660  1.00 23.35 ? 203  THR B OG1   1 
ATOM   5590 C CG2   . THR B 1 203 ? 12.128  -22.502 -1.063  1.00 23.50 ? 203  THR B CG2   1 
ATOM   5591 N N     . TRP B 1 204 ? 7.553   -23.192 -2.757  1.00 22.99 ? 204  TRP B N     1 
ATOM   5592 C CA    . TRP B 1 204 ? 6.102   -23.392 -2.484  1.00 22.72 ? 204  TRP B CA    1 
ATOM   5593 C C     . TRP B 1 204 ? 5.786   -24.831 -2.061  1.00 21.18 ? 204  TRP B C     1 
ATOM   5594 O O     . TRP B 1 204 ? 4.964   -24.987 -1.153  1.00 20.64 ? 204  TRP B O     1 
ATOM   5595 C CB    . TRP B 1 204 ? 5.249   -23.022 -3.696  1.00 22.84 ? 204  TRP B CB    1 
ATOM   5596 C CG    . TRP B 1 204 ? 3.814   -22.745 -3.382  1.00 20.21 ? 204  TRP B CG    1 
ATOM   5597 C CD1   . TRP B 1 204 ? 3.208   -22.583 -2.160  1.00 19.96 ? 204  TRP B CD1   1 
ATOM   5598 C CD2   . TRP B 1 204 ? 2.813   -22.474 -4.358  1.00 20.18 ? 204  TRP B CD2   1 
ATOM   5599 N NE1   . TRP B 1 204 ? 1.892   -22.265 -2.323  1.00 19.71 ? 204  TRP B NE1   1 
ATOM   5600 C CE2   . TRP B 1 204 ? 1.617   -22.188 -3.667  1.00 21.34 ? 204  TRP B CE2   1 
ATOM   5601 C CE3   . TRP B 1 204 ? 2.802   -22.489 -5.759  1.00 21.62 ? 204  TRP B CE3   1 
ATOM   5602 C CZ2   . TRP B 1 204 ? 0.422   -21.900 -4.330  1.00 20.84 ? 204  TRP B CZ2   1 
ATOM   5603 C CZ3   . TRP B 1 204 ? 1.618   -22.222 -6.406  1.00 20.21 ? 204  TRP B CZ3   1 
ATOM   5604 C CH2   . TRP B 1 204 ? 0.451   -21.910 -5.705  1.00 20.42 ? 204  TRP B CH2   1 
ATOM   5605 N N     . GLN B 1 205 ? 6.342   -25.831 -2.753  1.00 21.41 ? 205  GLN B N     1 
ATOM   5606 C CA    . GLN B 1 205 ? 6.034   -27.259 -2.516  1.00 23.51 ? 205  GLN B CA    1 
ATOM   5607 C C     . GLN B 1 205 ? 7.060   -27.940 -1.614  1.00 21.45 ? 205  GLN B C     1 
ATOM   5608 O O     . GLN B 1 205 ? 7.000   -29.186 -1.475  1.00 19.85 ? 205  GLN B O     1 
ATOM   5609 C CB    . GLN B 1 205 ? 5.861   -28.020 -3.845  1.00 24.12 ? 205  GLN B CB    1 
ATOM   5610 C CG    . GLN B 1 205 ? 4.439   -27.917 -4.382  1.00 23.27 ? 205  GLN B CG    1 
ATOM   5611 C CD    . GLN B 1 205 ? 4.036   -26.518 -4.798  1.00 25.29 ? 205  GLN B CD    1 
ATOM   5612 O OE1   . GLN B 1 205 ? 4.558   -25.972 -5.791  1.00 21.59 ? 205  GLN B OE1   1 
ATOM   5613 N NE2   . GLN B 1 205 ? 3.141   -25.905 -4.026  1.00 21.19 ? 205  GLN B NE2   1 
ATOM   5614 N N     . LEU B 1 206 ? 7.955   -27.226 -0.944  1.00 22.76 ? 206  LEU B N     1 
ATOM   5615 C CA    . LEU B 1 206 ? 8.917   -28.010 -0.133  1.00 26.24 ? 206  LEU B CA    1 
ATOM   5616 C C     . LEU B 1 206 ? 8.807   -27.764 1.376   1.00 24.96 ? 206  LEU B C     1 
ATOM   5617 O O     . LEU B 1 206 ? 9.465   -28.528 2.071   1.00 23.66 ? 206  LEU B O     1 
ATOM   5618 C CB    . LEU B 1 206 ? 10.336  -27.876 -0.666  1.00 36.48 ? 206  LEU B CB    1 
ATOM   5619 C CG    . LEU B 1 206 ? 10.774  -26.514 -1.125  1.00 36.50 ? 206  LEU B CG    1 
ATOM   5620 C CD1   . LEU B 1 206 ? 11.127  -25.710 0.107   1.00 46.77 ? 206  LEU B CD1   1 
ATOM   5621 C CD2   . LEU B 1 206 ? 11.963  -26.606 -2.088  1.00 36.82 ? 206  LEU B CD2   1 
ATOM   5622 N N     . ILE B 1 207 ? 7.984   -26.819 1.831   1.00 23.05 ? 207  ILE B N     1 
ATOM   5623 C CA    . ILE B 1 207 ? 7.623   -26.695 3.272   1.00 23.70 ? 207  ILE B CA    1 
ATOM   5624 C C     . ILE B 1 207 ? 6.178   -26.226 3.344   1.00 25.17 ? 207  ILE B C     1 
ATOM   5625 O O     . ILE B 1 207 ? 5.770   -25.359 2.574   1.00 22.89 ? 207  ILE B O     1 
ATOM   5626 C CB    . ILE B 1 207 ? 8.615   -25.769 4.002   1.00 26.37 ? 207  ILE B CB    1 
ATOM   5627 C CG1   . ILE B 1 207 ? 8.435   -25.830 5.521   1.00 28.16 ? 207  ILE B CG1   1 
ATOM   5628 C CG2   . ILE B 1 207 ? 8.536   -24.339 3.471   1.00 25.84 ? 207  ILE B CG2   1 
ATOM   5629 C CD1   . ILE B 1 207 ? 8.815   -27.157 6.140   1.00 37.03 ? 207  ILE B CD1   1 
ATOM   5630 N N     . PRO B 1 208 ? 5.318   -26.833 4.197   1.00 27.11 ? 208  PRO B N     1 
ATOM   5631 C CA    . PRO B 1 208 ? 3.904   -26.450 4.217   1.00 26.11 ? 208  PRO B CA    1 
ATOM   5632 C C     . PRO B 1 208 ? 3.579   -25.064 4.792   1.00 28.03 ? 208  PRO B C     1 
ATOM   5633 O O     . PRO B 1 208 ? 2.561   -24.533 4.401   1.00 31.92 ? 208  PRO B O     1 
ATOM   5634 C CB    . PRO B 1 208 ? 3.203   -27.550 5.036   1.00 28.38 ? 208  PRO B CB    1 
ATOM   5635 C CG    . PRO B 1 208 ? 4.301   -28.266 5.790   1.00 27.71 ? 208  PRO B CG    1 
ATOM   5636 C CD    . PRO B 1 208 ? 5.594   -28.024 5.020   1.00 26.62 ? 208  PRO B CD    1 
ATOM   5637 N N     . TYR B 1 209 ? 4.409   -24.484 5.664   1.00 26.04 ? 209  TYR B N     1 
ATOM   5638 C CA    . TYR B 1 209 ? 3.963   -23.417 6.626   1.00 30.74 ? 209  TYR B CA    1 
ATOM   5639 C C     . TYR B 1 209 ? 3.959   -21.967 6.110   1.00 37.18 ? 209  TYR B C     1 
ATOM   5640 O O     . TYR B 1 209 ? 2.887   -21.250 6.253   1.00 50.45 ? 209  TYR B O     1 
ATOM   5641 C CB    . TYR B 1 209 ? 4.776   -23.486 7.920   1.00 33.00 ? 209  TYR B CB    1 
ATOM   5642 C CG    . TYR B 1 209 ? 4.767   -24.864 8.513   1.00 30.26 ? 209  TYR B CG    1 
ATOM   5643 C CD1   . TYR B 1 209 ? 3.573   -25.519 8.736   1.00 31.70 ? 209  TYR B CD1   1 
ATOM   5644 C CD2   . TYR B 1 209 ? 5.946   -25.535 8.795   1.00 32.91 ? 209  TYR B CD2   1 
ATOM   5645 C CE1   . TYR B 1 209 ? 3.543   -26.803 9.247   1.00 33.35 ? 209  TYR B CE1   1 
ATOM   5646 C CE2   . TYR B 1 209 ? 5.937   -26.816 9.307   1.00 31.59 ? 209  TYR B CE2   1 
ATOM   5647 C CZ    . TYR B 1 209 ? 4.734   -27.458 9.534   1.00 35.08 ? 209  TYR B CZ    1 
ATOM   5648 O OH    . TYR B 1 209 ? 4.731   -28.727 10.045  1.00 34.77 ? 209  TYR B OH    1 
ATOM   5649 N N     . GLY B 1 210 ? 5.090   -21.479 5.656   1.00 31.46 ? 210  GLY B N     1 
ATOM   5650 C CA    . GLY B 1 210 ? 5.265   -20.044 5.377   1.00 29.44 ? 210  GLY B CA    1 
ATOM   5651 C C     . GLY B 1 210 ? 5.501   -19.237 6.643   1.00 30.96 ? 210  GLY B C     1 
ATOM   5652 O O     . GLY B 1 210 ? 6.011   -19.811 7.647   1.00 34.21 ? 210  GLY B O     1 
ATOM   5653 N N     . PHE B 1 211 ? 5.136   -17.963 6.610   1.00 26.39 ? 211  PHE B N     1 
ATOM   5654 C CA    . PHE B 1 211 ? 5.387   -17.002 7.716   1.00 25.24 ? 211  PHE B CA    1 
ATOM   5655 C C     . PHE B 1 211 ? 4.035   -16.602 8.288   1.00 21.68 ? 211  PHE B C     1 
ATOM   5656 O O     . PHE B 1 211 ? 3.122   -16.334 7.554   1.00 24.16 ? 211  PHE B O     1 
ATOM   5657 C CB    . PHE B 1 211 ? 6.148   -15.764 7.232   1.00 23.41 ? 211  PHE B CB    1 
ATOM   5658 C CG    . PHE B 1 211 ? 6.362   -14.720 8.293   1.00 21.18 ? 211  PHE B CG    1 
ATOM   5659 C CD1   . PHE B 1 211 ? 7.286   -14.942 9.296   1.00 22.63 ? 211  PHE B CD1   1 
ATOM   5660 C CD2   . PHE B 1 211 ? 5.641   -13.533 8.283   1.00 23.09 ? 211  PHE B CD2   1 
ATOM   5661 C CE1   . PHE B 1 211 ? 7.502   -13.987 10.272  1.00 23.69 ? 211  PHE B CE1   1 
ATOM   5662 C CE2   . PHE B 1 211 ? 5.850   -12.576 9.265   1.00 21.38 ? 211  PHE B CE2   1 
ATOM   5663 C CZ    . PHE B 1 211 ? 6.777   -12.808 10.254  1.00 24.38 ? 211  PHE B CZ    1 
ATOM   5664 N N     . GLY B 1 212 ? 3.924   -16.522 9.603   1.00 20.41 ? 212  GLY B N     1 
ATOM   5665 C CA    . GLY B 1 212 ? 2.660   -16.093 10.211  1.00 19.48 ? 212  GLY B CA    1 
ATOM   5666 C C     . GLY B 1 212 ? 1.694   -17.250 10.371  1.00 20.38 ? 212  GLY B C     1 
ATOM   5667 O O     . GLY B 1 212 ? 2.103   -18.405 10.297  1.00 20.67 ? 212  GLY B O     1 
ATOM   5668 N N     . PRO B 1 213 ? 0.423   -16.973 10.738  1.00 20.67 ? 213  PRO B N     1 
ATOM   5669 C CA    . PRO B 1 213 ? -0.527  -18.046 11.059  1.00 21.86 ? 213  PRO B CA    1 
ATOM   5670 C C     . PRO B 1 213 ? -0.663  -18.989 9.851   1.00 23.30 ? 213  PRO B C     1 
ATOM   5671 O O     . PRO B 1 213 ? -0.666  -18.509 8.722   1.00 22.99 ? 213  PRO B O     1 
ATOM   5672 C CB    . PRO B 1 213 ? -1.798  -17.282 11.399  1.00 22.62 ? 213  PRO B CB    1 
ATOM   5673 C CG    . PRO B 1 213 ? -1.304  -15.926 11.854  1.00 22.39 ? 213  PRO B CG    1 
ATOM   5674 C CD    . PRO B 1 213 ? -0.139  -15.638 10.941  1.00 23.16 ? 213  PRO B CD    1 
ATOM   5675 N N     . TYR B 1 214 ? -0.640  -20.290 10.101  1.00 22.44 ? 214  TYR B N     1 
ATOM   5676 C CA    . TYR B 1 214 ? -0.609  -21.348 9.063   1.00 21.75 ? 214  TYR B CA    1 
ATOM   5677 C C     . TYR B 1 214 ? -2.056  -21.690 8.723   1.00 22.11 ? 214  TYR B C     1 
ATOM   5678 O O     . TYR B 1 214 ? -2.805  -22.165 9.569   1.00 22.25 ? 214  TYR B O     1 
ATOM   5679 C CB    . TYR B 1 214 ? 0.231   -22.535 9.562   1.00 22.25 ? 214  TYR B CB    1 
ATOM   5680 C CG    . TYR B 1 214 ? 0.046   -23.842 8.832   1.00 21.04 ? 214  TYR B CG    1 
ATOM   5681 C CD1   . TYR B 1 214 ? 0.087   -23.909 7.444   1.00 22.54 ? 214  TYR B CD1   1 
ATOM   5682 C CD2   . TYR B 1 214 ? -0.120  -25.030 9.525   1.00 22.74 ? 214  TYR B CD2   1 
ATOM   5683 C CE1   . TYR B 1 214 ? -0.074  -25.112 6.777   1.00 22.48 ? 214  TYR B CE1   1 
ATOM   5684 C CE2   . TYR B 1 214 ? -0.301  -26.241 8.870   1.00 26.20 ? 214  TYR B CE2   1 
ATOM   5685 C CZ    . TYR B 1 214 ? -0.308  -26.276 7.485   1.00 25.69 ? 214  TYR B CZ    1 
ATOM   5686 O OH    . TYR B 1 214 ? -0.445  -27.485 6.873   1.00 26.08 ? 214  TYR B OH    1 
ATOM   5687 N N     . PRO B 1 215 ? -2.549  -21.351 7.516   1.00 21.42 ? 215  PRO B N     1 
ATOM   5688 C CA    . PRO B 1 215 ? -3.980  -21.457 7.260   1.00 22.64 ? 215  PRO B CA    1 
ATOM   5689 C C     . PRO B 1 215 ? -4.516  -22.632 6.438   1.00 23.25 ? 215  PRO B C     1 
ATOM   5690 O O     . PRO B 1 215 ? -5.692  -22.704 6.374   1.00 23.42 ? 215  PRO B O     1 
ATOM   5691 C CB    . PRO B 1 215 ? -4.191  -20.214 6.395   1.00 22.28 ? 215  PRO B CB    1 
ATOM   5692 C CG    . PRO B 1 215 ? -2.948  -20.193 5.528   1.00 21.73 ? 215  PRO B CG    1 
ATOM   5693 C CD    . PRO B 1 215 ? -1.829  -20.640 6.439   1.00 21.72 ? 215  PRO B CD    1 
ATOM   5694 N N     . ASP B 1 216 ? -3.674  -23.448 5.808   1.00 22.15 ? 216  ASP B N     1 
ATOM   5695 C CA    . ASP B 1 216 ? -4.108  -24.454 4.799   1.00 22.52 ? 216  ASP B CA    1 
ATOM   5696 C C     . ASP B 1 216 ? -5.127  -25.416 5.403   1.00 23.14 ? 216  ASP B C     1 
ATOM   5697 O O     . ASP B 1 216 ? -6.081  -25.710 4.720   1.00 23.11 ? 216  ASP B O     1 
ATOM   5698 C CB    . ASP B 1 216 ? -2.912  -25.240 4.273   1.00 22.97 ? 216  ASP B CB    1 
ATOM   5699 C CG    . ASP B 1 216 ? -1.942  -24.324 3.550   1.00 22.73 ? 216  ASP B CG    1 
ATOM   5700 O OD1   . ASP B 1 216 ? -1.460  -23.358 4.167   1.00 21.04 ? 216  ASP B OD1   1 
ATOM   5701 O OD2   . ASP B 1 216 ? -1.657  -24.646 2.399   1.00 22.17 ? 216  ASP B OD2   1 
ATOM   5702 N N     . GLY B 1 217 ? -5.002  -25.784 6.685   1.00 20.77 ? 217  GLY B N     1 
ATOM   5703 C CA    . GLY B 1 217 ? -5.962  -26.701 7.319   1.00 21.54 ? 217  GLY B CA    1 
ATOM   5704 C C     . GLY B 1 217 ? -7.384  -26.144 7.349   1.00 21.23 ? 217  GLY B C     1 
ATOM   5705 O O     . GLY B 1 217 ? -8.357  -26.954 7.332   1.00 23.00 ? 217  GLY B O     1 
ATOM   5706 N N     . MET B 1 218 ? -7.531  -24.822 7.337   1.00 22.37 ? 218  MET B N     1 
ATOM   5707 C CA    . MET B 1 218 ? -8.852  -24.153 7.422   1.00 24.68 ? 218  MET B CA    1 
ATOM   5708 C C     . MET B 1 218 ? -9.615  -24.333 6.097   1.00 21.99 ? 218  MET B C     1 
ATOM   5709 O O     . MET B 1 218 ? -10.815 -24.027 6.079   1.00 23.90 ? 218  MET B O     1 
ATOM   5710 C CB    . MET B 1 218 ? -8.729  -22.659 7.754   1.00 27.26 ? 218  MET B CB    1 
ATOM   5711 C CG    . MET B 1 218 ? -8.242  -22.349 9.168   1.00 32.09 ? 218  MET B CG    1 
ATOM   5712 S SD    . MET B 1 218 ? -9.377  -22.934 10.420  1.00 36.39 ? 218  MET B SD    1 
ATOM   5713 C CE    . MET B 1 218 ? -10.717 -21.750 10.241  1.00 43.14 ? 218  MET B CE    1 
ATOM   5714 N N     . PHE B 1 219 ? -8.961  -24.784 5.028   1.00 23.85 ? 219  PHE B N     1 
ATOM   5715 C CA    . PHE B 1 219 ? -9.590  -25.022 3.701   1.00 23.79 ? 219  PHE B CA    1 
ATOM   5716 C C     . PHE B 1 219 ? -9.869  -26.521 3.481   1.00 24.24 ? 219  PHE B C     1 
ATOM   5717 O O     . PHE B 1 219 ? -10.209 -26.896 2.337   1.00 24.43 ? 219  PHE B O     1 
ATOM   5718 C CB    . PHE B 1 219 ? -8.710  -24.427 2.588   1.00 22.83 ? 219  PHE B CB    1 
ATOM   5719 C CG    . PHE B 1 219 ? -8.543  -22.944 2.745   1.00 23.41 ? 219  PHE B CG    1 
ATOM   5720 C CD1   . PHE B 1 219 ? -9.596  -22.070 2.489   1.00 21.54 ? 219  PHE B CD1   1 
ATOM   5721 C CD2   . PHE B 1 219 ? -7.339  -22.416 3.177   1.00 23.69 ? 219  PHE B CD2   1 
ATOM   5722 C CE1   . PHE B 1 219 ? -9.457  -20.718 2.711   1.00 22.61 ? 219  PHE B CE1   1 
ATOM   5723 C CE2   . PHE B 1 219 ? -7.195  -21.049 3.367   1.00 24.42 ? 219  PHE B CE2   1 
ATOM   5724 C CZ    . PHE B 1 219 ? -8.256  -20.202 3.146   1.00 25.76 ? 219  PHE B CZ    1 
ATOM   5725 N N     . THR B 1 220 ? -9.715  -27.359 4.513   1.00 21.82 ? 220  THR B N     1 
ATOM   5726 C CA    . THR B 1 220 ? -10.014 -28.805 4.467   1.00 24.29 ? 220  THR B CA    1 
ATOM   5727 C C     . THR B 1 220 ? -11.281 -29.093 5.301   1.00 22.59 ? 220  THR B C     1 
ATOM   5728 O O     . THR B 1 220 ? -11.534 -28.388 6.322   1.00 22.37 ? 220  THR B O     1 
ATOM   5729 C CB    . THR B 1 220 ? -8.807  -29.658 4.886   1.00 25.64 ? 220  THR B CB    1 
ATOM   5730 O OG1   . THR B 1 220 ? -8.545  -29.473 6.274   1.00 28.09 ? 220  THR B OG1   1 
ATOM   5731 C CG2   . THR B 1 220 ? -7.554  -29.314 4.117   1.00 28.26 ? 220  THR B CG2   1 
ATOM   5732 N N     . GLN B 1 221 ? -12.125 -29.980 4.789   1.00 22.15 ? 221  GLN B N     1 
ATOM   5733 C CA    . GLN B 1 221 ? -13.530 -30.162 5.248   1.00 25.03 ? 221  GLN B CA    1 
ATOM   5734 C C     . GLN B 1 221 ? -14.171 -28.798 5.517   1.00 22.34 ? 221  GLN B C     1 
ATOM   5735 O O     . GLN B 1 221 ? -14.718 -28.582 6.603   1.00 21.80 ? 221  GLN B O     1 
ATOM   5736 C CB    . GLN B 1 221 ? -13.531 -31.046 6.493   1.00 23.88 ? 221  GLN B CB    1 
ATOM   5737 C CG    . GLN B 1 221 ? -13.061 -32.460 6.215   1.00 25.22 ? 221  GLN B CG    1 
ATOM   5738 C CD    . GLN B 1 221 ? -13.441 -33.402 7.322   1.00 25.97 ? 221  GLN B CD    1 
ATOM   5739 O OE1   . GLN B 1 221 ? -14.000 -32.975 8.339   1.00 26.57 ? 221  GLN B OE1   1 
ATOM   5740 N NE2   . GLN B 1 221 ? -13.112 -34.673 7.145   1.00 27.41 ? 221  GLN B NE2   1 
ATOM   5741 N N     . SER B 1 222 ? -14.121 -27.907 4.537   1.00 22.84 ? 222  SER B N     1 
ATOM   5742 C CA    . SER B 1 222 ? -14.294 -26.463 4.738   1.00 23.90 ? 222  SER B CA    1 
ATOM   5743 C C     . SER B 1 222 ? -15.095 -25.838 3.599   1.00 25.06 ? 222  SER B C     1 
ATOM   5744 O O     . SER B 1 222 ? -15.032 -26.309 2.464   1.00 25.84 ? 222  SER B O     1 
ATOM   5745 C CB    . SER B 1 222 ? -12.944 -25.814 4.877   1.00 25.66 ? 222  SER B CB    1 
ATOM   5746 O OG    . SER B 1 222 ? -13.051 -24.418 4.952   1.00 27.20 ? 222  SER B OG    1 
ATOM   5747 N N     . ASN B 1 223 ? -15.757 -24.736 3.901   1.00 25.41 ? 223  ASN B N     1 
ATOM   5748 C CA    . ASN B 1 223 ? -16.452 -23.895 2.901   1.00 26.79 ? 223  ASN B CA    1 
ATOM   5749 C C     . ASN B 1 223 ? -15.842 -22.487 2.912   1.00 27.24 ? 223  ASN B C     1 
ATOM   5750 O O     . ASN B 1 223 ? -16.586 -21.535 2.624   1.00 31.83 ? 223  ASN B O     1 
ATOM   5751 C CB    . ASN B 1 223 ? -17.954 -23.895 3.153   1.00 26.02 ? 223  ASN B CB    1 
ATOM   5752 C CG    . ASN B 1 223 ? -18.338 -23.476 4.550   1.00 26.91 ? 223  ASN B CG    1 
ATOM   5753 O OD1   . ASN B 1 223 ? -17.541 -22.846 5.241   1.00 29.50 ? 223  ASN B OD1   1 
ATOM   5754 N ND2   . ASN B 1 223 ? -19.561 -23.802 4.953   1.00 29.19 ? 223  ASN B ND2   1 
ATOM   5755 N N     . LEU B 1 224 ? -14.559 -22.330 3.245   1.00 24.57 ? 224  LEU B N     1 
ATOM   5756 C CA    . LEU B 1 224 ? -13.906 -20.995 3.310   1.00 24.94 ? 224  LEU B CA    1 
ATOM   5757 C C     . LEU B 1 224 ? -13.245 -20.625 1.974   1.00 22.88 ? 224  LEU B C     1 
ATOM   5758 O O     . LEU B 1 224 ? -12.688 -19.521 1.876   1.00 22.02 ? 224  LEU B O     1 
ATOM   5759 C CB    . LEU B 1 224 ? -12.872 -20.971 4.440   1.00 26.31 ? 224  LEU B CB    1 
ATOM   5760 C CG    . LEU B 1 224 ? -13.457 -21.218 5.828   1.00 27.65 ? 224  LEU B CG    1 
ATOM   5761 C CD1   . LEU B 1 224 ? -12.392 -21.094 6.904   1.00 25.55 ? 224  LEU B CD1   1 
ATOM   5762 C CD2   . LEU B 1 224 ? -14.628 -20.283 6.111   1.00 27.95 ? 224  LEU B CD2   1 
ATOM   5763 N N     . GLY B 1 225 ? -13.293 -21.485 0.968   1.00 24.92 ? 225  GLY B N     1 
ATOM   5764 C CA    . GLY B 1 225 ? -12.760 -21.067 -0.333  1.00 24.71 ? 225  GLY B CA    1 
ATOM   5765 C C     . GLY B 1 225 ? -12.747 -22.160 -1.360  1.00 23.49 ? 225  GLY B C     1 
ATOM   5766 O O     . GLY B 1 225 ? -12.920 -23.319 -1.008  1.00 27.15 ? 225  GLY B O     1 
ATOM   5767 N N     . ILE B 1 226 ? -12.505 -21.771 -2.602  1.00 21.80 ? 226  ILE B N     1 
ATOM   5768 C CA    . ILE B 1 226 ? -12.403 -22.725 -3.739  1.00 23.52 ? 226  ILE B CA    1 
ATOM   5769 C C     . ILE B 1 226 ? -10.926 -22.828 -4.110  1.00 22.01 ? 226  ILE B C     1 
ATOM   5770 O O     . ILE B 1 226 ? -10.377 -21.844 -4.592  1.00 25.88 ? 226  ILE B O     1 
ATOM   5771 C CB    . ILE B 1 226 ? -13.285 -22.292 -4.927  1.00 24.88 ? 226  ILE B CB    1 
ATOM   5772 C CG1   . ILE B 1 226 ? -14.759 -22.192 -4.542  1.00 26.08 ? 226  ILE B CG1   1 
ATOM   5773 C CG2   . ILE B 1 226 ? -13.068 -23.205 -6.117  1.00 27.78 ? 226  ILE B CG2   1 
ATOM   5774 C CD1   . ILE B 1 226 ? -15.630 -21.568 -5.614  1.00 25.29 ? 226  ILE B CD1   1 
ATOM   5775 N N     . VAL B 1 227 ? -10.349 -24.001 -3.910  1.00 24.25 ? 227  VAL B N     1 
ATOM   5776 C CA    . VAL B 1 227 ? -8.933  -24.318 -4.181  1.00 24.22 ? 227  VAL B CA    1 
ATOM   5777 C C     . VAL B 1 227 ? -8.772  -24.521 -5.691  1.00 26.55 ? 227  VAL B C     1 
ATOM   5778 O O     . VAL B 1 227 ? -9.563  -25.274 -6.286  1.00 26.16 ? 227  VAL B O     1 
ATOM   5779 C CB    . VAL B 1 227 ? -8.491  -25.540 -3.376  1.00 24.02 ? 227  VAL B CB    1 
ATOM   5780 C CG1   . VAL B 1 227 ? -7.099  -26.003 -3.761  1.00 24.16 ? 227  VAL B CG1   1 
ATOM   5781 C CG2   . VAL B 1 227 ? -8.574  -25.234 -1.893  1.00 27.01 ? 227  VAL B CG2   1 
ATOM   5782 N N     . THR B 1 228 ? -7.795  -23.832 -6.261  1.00 24.23 ? 228  THR B N     1 
ATOM   5783 C CA    . THR B 1 228 ? -7.525  -23.817 -7.725  1.00 25.18 ? 228  THR B CA    1 
ATOM   5784 C C     . THR B 1 228 ? -6.186  -24.470 -8.036  1.00 25.13 ? 228  THR B C     1 
ATOM   5785 O O     . THR B 1 228 ? -5.992  -24.882 -9.194  1.00 23.28 ? 228  THR B O     1 
ATOM   5786 C CB    . THR B 1 228 ? -7.580  -22.375 -8.226  1.00 25.12 ? 228  THR B CB    1 
ATOM   5787 O OG1   . THR B 1 228 ? -6.689  -21.571 -7.448  1.00 25.99 ? 228  THR B OG1   1 
ATOM   5788 C CG2   . THR B 1 228 ? -8.989  -21.846 -8.134  1.00 24.08 ? 228  THR B CG2   1 
ATOM   5789 N N     . LYS B 1 229 ? -5.274  -24.506 -7.068  1.00 23.54 ? 229  LYS B N     1 
ATOM   5790 C CA    . LYS B 1 229 ? -3.993  -25.221 -7.204  1.00 23.09 ? 229  LYS B CA    1 
ATOM   5791 C C     . LYS B 1 229 ? -3.645  -25.796 -5.829  1.00 23.69 ? 229  LYS B C     1 
ATOM   5792 O O     . LYS B 1 229 ? -3.957  -25.166 -4.799  1.00 21.99 ? 229  LYS B O     1 
ATOM   5793 C CB    . LYS B 1 229 ? -2.858  -24.304 -7.677  1.00 23.82 ? 229  LYS B CB    1 
ATOM   5794 C CG    . LYS B 1 229 ? -3.068  -23.605 -9.013  1.00 26.05 ? 229  LYS B CG    1 
ATOM   5795 C CD    . LYS B 1 229 ? -1.900  -22.680 -9.355  1.00 25.48 ? 229  LYS B CD    1 
ATOM   5796 C CE    . LYS B 1 229 ? -2.031  -22.088 -10.754 1.00 26.21 ? 229  LYS B CE    1 
ATOM   5797 N NZ    . LYS B 1 229 ? -3.296  -21.331 -10.907 1.00 25.70 ? 229  LYS B NZ    1 
ATOM   5798 N N     . MET B 1 230 ? -2.978  -26.927 -5.844  1.00 22.77 ? 230  MET B N     1 
ATOM   5799 C CA    . MET B 1 230 ? -2.512  -27.583 -4.601  1.00 24.77 ? 230  MET B CA    1 
ATOM   5800 C C     . MET B 1 230 ? -1.236  -28.360 -4.911  1.00 24.10 ? 230  MET B C     1 
ATOM   5801 O O     . MET B 1 230 ? -1.201  -29.117 -5.900  1.00 23.55 ? 230  MET B O     1 
ATOM   5802 C CB    . MET B 1 230 ? -3.575  -28.540 -4.074  1.00 25.82 ? 230  MET B CB    1 
ATOM   5803 C CG    . MET B 1 230 ? -3.303  -28.992 -2.661  1.00 27.22 ? 230  MET B CG    1 
ATOM   5804 S SD    . MET B 1 230 ? -4.316  -30.395 -2.198  1.00 26.39 ? 230  MET B SD    1 
ATOM   5805 C CE    . MET B 1 230 ? -3.349  -31.734 -2.887  1.00 27.82 ? 230  MET B CE    1 
ATOM   5806 N N     . GLY B 1 231 ? -0.218  -28.152 -4.073  1.00 22.27 ? 231  GLY B N     1 
ATOM   5807 C CA    . GLY B 1 231 ? 1.007   -28.939 -4.103  1.00 19.92 ? 231  GLY B CA    1 
ATOM   5808 C C     . GLY B 1 231 ? 0.860   -30.176 -3.266  1.00 22.72 ? 231  GLY B C     1 
ATOM   5809 O O     . GLY B 1 231 ? 0.120   -30.148 -2.266  1.00 22.61 ? 231  GLY B O     1 
ATOM   5810 N N     . ILE B 1 232 ? 1.563   -31.230 -3.638  1.00 22.50 ? 232  ILE B N     1 
ATOM   5811 C CA    . ILE B 1 232 ? 1.617   -32.448 -2.793  1.00 22.55 ? 232  ILE B CA    1 
ATOM   5812 C C     . ILE B 1 232 ? 2.998   -33.077 -2.940  1.00 22.99 ? 232  ILE B C     1 
ATOM   5813 O O     . ILE B 1 232 ? 3.519   -33.141 -4.055  1.00 23.81 ? 232  ILE B O     1 
ATOM   5814 C CB    . ILE B 1 232 ? 0.468   -33.421 -3.121  1.00 22.93 ? 232  ILE B CB    1 
ATOM   5815 C CG1   . ILE B 1 232 ? 0.310   -34.463 -2.012  1.00 23.43 ? 232  ILE B CG1   1 
ATOM   5816 C CG2   . ILE B 1 232 ? 0.661   -34.065 -4.484  1.00 22.64 ? 232  ILE B CG2   1 
ATOM   5817 C CD1   . ILE B 1 232 ? -1.023  -35.189 -2.030  1.00 26.70 ? 232  ILE B CD1   1 
ATOM   5818 N N     . ALA B 1 233 ? 3.612   -33.429 -1.822  1.00 20.89 ? 233  ALA B N     1 
ATOM   5819 C CA    . ALA B 1 233 ? 4.866   -34.197 -1.769  1.00 22.65 ? 233  ALA B CA    1 
ATOM   5820 C C     . ALA B 1 233 ? 4.589   -35.609 -2.276  1.00 23.47 ? 233  ALA B C     1 
ATOM   5821 O O     . ALA B 1 233 ? 3.526   -36.175 -1.995  1.00 23.36 ? 233  ALA B O     1 
ATOM   5822 C CB    . ALA B 1 233 ? 5.420   -34.229 -0.374  1.00 23.48 ? 233  ALA B CB    1 
ATOM   5823 N N     . LEU B 1 234 ? 5.545   -36.144 -3.015  1.00 22.92 ? 234  LEU B N     1 
ATOM   5824 C CA    . LEU B 1 234 ? 5.481   -37.477 -3.635  1.00 23.21 ? 234  LEU B CA    1 
ATOM   5825 C C     . LEU B 1 234 ? 6.652   -38.311 -3.134  1.00 23.75 ? 234  LEU B C     1 
ATOM   5826 O O     . LEU B 1 234 ? 7.804   -37.893 -3.294  1.00 25.93 ? 234  LEU B O     1 
ATOM   5827 C CB    . LEU B 1 234 ? 5.527   -37.294 -5.155  1.00 24.52 ? 234  LEU B CB    1 
ATOM   5828 C CG    . LEU B 1 234 ? 4.312   -36.615 -5.765  1.00 22.05 ? 234  LEU B CG    1 
ATOM   5829 C CD1   . LEU B 1 234 ? 4.526   -36.358 -7.256  1.00 24.09 ? 234  LEU B CD1   1 
ATOM   5830 C CD2   . LEU B 1 234 ? 3.063   -37.436 -5.508  1.00 23.84 ? 234  LEU B CD2   1 
ATOM   5831 N N     . MET B 1 235 ? 6.358   -39.491 -2.612  1.00 24.87 ? 235  MET B N     1 
ATOM   5832 C CA    . MET B 1 235 ? 7.360   -40.447 -2.102  1.00 27.03 ? 235  MET B CA    1 
ATOM   5833 C C     . MET B 1 235 ? 8.146   -41.065 -3.266  1.00 25.92 ? 235  MET B C     1 
ATOM   5834 O O     . MET B 1 235 ? 7.545   -41.377 -4.316  1.00 26.30 ? 235  MET B O     1 
ATOM   5835 C CB    . MET B 1 235 ? 6.682   -41.581 -1.343  1.00 30.24 ? 235  MET B CB    1 
ATOM   5836 C CG    . MET B 1 235 ? 7.599   -42.287 -0.370  1.00 31.99 ? 235  MET B CG    1 
ATOM   5837 S SD    . MET B 1 235 ? 6.620   -43.547 0.503   1.00 35.93 ? 235  MET B SD    1 
ATOM   5838 C CE    . MET B 1 235 ? 6.902   -44.940 -0.579  1.00 43.44 ? 235  MET B CE    1 
ATOM   5839 N N     . GLN B 1 236 ? 9.430   -41.292 -3.029  1.00 28.10 ? 236  GLN B N     1 
ATOM   5840 C CA    . GLN B 1 236 ? 10.295  -42.099 -3.922  1.00 29.93 ? 236  GLN B CA    1 
ATOM   5841 C C     . GLN B 1 236 ? 9.878   -43.560 -3.818  1.00 28.81 ? 236  GLN B C     1 
ATOM   5842 O O     . GLN B 1 236 ? 9.697   -44.061 -2.693  1.00 25.48 ? 236  GLN B O     1 
ATOM   5843 C CB    . GLN B 1 236 ? 11.771  -41.976 -3.543  1.00 31.81 ? 236  GLN B CB    1 
ATOM   5844 C CG    . GLN B 1 236 ? 12.431  -40.715 -4.052  1.00 36.75 ? 236  GLN B CG    1 
ATOM   5845 C CD    . GLN B 1 236 ? 13.890  -40.702 -3.667  1.00 35.45 ? 236  GLN B CD    1 
ATOM   5846 O OE1   . GLN B 1 236 ? 14.440  -41.686 -3.188  1.00 35.30 ? 236  GLN B OE1   1 
ATOM   5847 N NE2   . GLN B 1 236 ? 14.528  -39.575 -3.896  1.00 41.04 ? 236  GLN B NE2   1 
ATOM   5848 N N     . LYS B 1 237 ? 9.711   -44.224 -4.962  1.00 30.95 ? 237  LYS B N     1 
ATOM   5849 C CA    . LYS B 1 237 ? 9.522   -45.695 -4.993  1.00 31.72 ? 237  LYS B CA    1 
ATOM   5850 C C     . LYS B 1 237 ? 10.705  -46.333 -4.286  1.00 31.72 ? 237  LYS B C     1 
ATOM   5851 O O     . LYS B 1 237 ? 11.855  -46.002 -4.558  1.00 32.39 ? 237  LYS B O     1 
ATOM   5852 C CB    . LYS B 1 237 ? 9.493   -46.237 -6.419  1.00 35.06 ? 237  LYS B CB    1 
ATOM   5853 C CG    . LYS B 1 237 ? 8.288   -45.857 -7.246  1.00 36.66 ? 237  LYS B CG    1 
ATOM   5854 C CD    . LYS B 1 237 ? 8.307   -46.588 -8.560  1.00 36.02 ? 237  LYS B CD    1 
ATOM   5855 C CE    . LYS B 1 237 ? 7.233   -46.138 -9.502  1.00 34.26 ? 237  LYS B CE    1 
ATOM   5856 N NZ    . LYS B 1 237 ? 7.520   -46.634 -10.870 1.00 36.92 ? 237  LYS B NZ    1 
ATOM   5857 N N     . PRO B 1 238 ? 10.462  -47.229 -3.323  1.00 30.98 ? 238  PRO B N     1 
ATOM   5858 C CA    . PRO B 1 238 ? 11.533  -48.006 -2.731  1.00 33.86 ? 238  PRO B CA    1 
ATOM   5859 C C     . PRO B 1 238 ? 12.062  -48.997 -3.758  1.00 29.86 ? 238  PRO B C     1 
ATOM   5860 O O     . PRO B 1 238 ? 11.471  -49.160 -4.816  1.00 29.09 ? 238  PRO B O     1 
ATOM   5861 C CB    . PRO B 1 238 ? 10.914  -48.704 -1.521  1.00 35.81 ? 238  PRO B CB    1 
ATOM   5862 C CG    . PRO B 1 238 ? 9.431   -48.655 -1.776  1.00 39.38 ? 238  PRO B CG    1 
ATOM   5863 C CD    . PRO B 1 238 ? 9.153   -47.527 -2.748  1.00 34.44 ? 238  PRO B CD    1 
ATOM   5864 N N     . PRO B 1 239 ? 13.243  -49.594 -3.495  1.00 31.75 ? 239  PRO B N     1 
ATOM   5865 C CA    . PRO B 1 239 ? 13.864  -50.528 -4.439  1.00 33.54 ? 239  PRO B CA    1 
ATOM   5866 C C     . PRO B 1 239 ? 13.042  -51.810 -4.641  1.00 33.19 ? 239  PRO B C     1 
ATOM   5867 O O     . PRO B 1 239 ? 13.118  -52.399 -5.679  1.00 32.17 ? 239  PRO B O     1 
ATOM   5868 C CB    . PRO B 1 239 ? 15.223  -50.853 -3.817  1.00 33.23 ? 239  PRO B CB    1 
ATOM   5869 C CG    . PRO B 1 239 ? 15.146  -50.393 -2.373  1.00 35.45 ? 239  PRO B CG    1 
ATOM   5870 C CD    . PRO B 1 239 ? 14.072  -49.330 -2.309  1.00 33.43 ? 239  PRO B CD    1 
ATOM   5871 N N     . ALA B 1 240 ? 12.248  -52.200 -3.647  1.00 32.80 ? 240  ALA B N     1 
ATOM   5872 C CA    . ALA B 1 240 ? 11.375  -53.392 -3.715  1.00 31.92 ? 240  ALA B CA    1 
ATOM   5873 C C     . ALA B 1 240 ? 10.260  -53.237 -2.682  1.00 33.35 ? 240  ALA B C     1 
ATOM   5874 O O     . ALA B 1 240 ? 10.386  -52.392 -1.764  1.00 28.26 ? 240  ALA B O     1 
ATOM   5875 C CB    . ALA B 1 240 ? 12.171  -54.646 -3.465  1.00 33.04 ? 240  ALA B CB    1 
ATOM   5876 N N     . SER B 1 241 ? 9.208   -54.024 -2.842  1.00 30.67 ? 241  SER B N     1 
ATOM   5877 C CA    . SER B 1 241 ? 8.065   -54.050 -1.897  1.00 31.91 ? 241  SER B CA    1 
ATOM   5878 C C     . SER B 1 241 ? 7.502   -55.472 -1.855  1.00 34.17 ? 241  SER B C     1 
ATOM   5879 O O     . SER B 1 241 ? 7.655   -56.240 -2.818  1.00 32.25 ? 241  SER B O     1 
ATOM   5880 C CB    . SER B 1 241 ? 7.033   -52.996 -2.240  1.00 33.77 ? 241  SER B CB    1 
ATOM   5881 O OG    . SER B 1 241 ? 6.153   -53.391 -3.286  1.00 33.14 ? 241  SER B OG    1 
ATOM   5882 N N     . MET B 1 242 ? 6.914   -55.831 -0.732  1.00 30.90 ? 242  MET B N     1 
ATOM   5883 C CA    . MET B 1 242 ? 6.124   -57.075 -0.628  1.00 30.36 ? 242  MET B CA    1 
ATOM   5884 C C     . MET B 1 242 ? 4.887   -56.750 0.214   1.00 30.03 ? 242  MET B C     1 
ATOM   5885 O O     . MET B 1 242 ? 5.048   -56.016 1.247   1.00 29.63 ? 242  MET B O     1 
ATOM   5886 C CB    . MET B 1 242 ? 6.970   -58.162 0.031   1.00 30.95 ? 242  MET B CB    1 
ATOM   5887 C CG    . MET B 1 242 ? 6.274   -59.495 0.152   1.00 33.07 ? 242  MET B CG    1 
ATOM   5888 S SD    . MET B 1 242 ? 5.285   -59.533 1.667   1.00 36.24 ? 242  MET B SD    1 
ATOM   5889 C CE    . MET B 1 242 ? 6.595   -59.854 2.846   1.00 36.35 ? 242  MET B CE    1 
ATOM   5890 N N     . THR B 1 243 ? 3.725   -57.257 -0.214  1.00 29.62 ? 243  THR B N     1 
ATOM   5891 C CA    . THR B 1 243 ? 2.436   -57.146 0.509   1.00 28.25 ? 243  THR B CA    1 
ATOM   5892 C C     . THR B 1 243 ? 2.063   -58.528 1.042   1.00 29.33 ? 243  THR B C     1 
ATOM   5893 O O     . THR B 1 243 ? 2.252   -59.519 0.332   1.00 29.72 ? 243  THR B O     1 
ATOM   5894 C CB    . THR B 1 243 ? 1.360   -56.536 -0.385  1.00 28.54 ? 243  THR B CB    1 
ATOM   5895 O OG1   . THR B 1 243 ? 1.896   -55.285 -0.828  1.00 28.43 ? 243  THR B OG1   1 
ATOM   5896 C CG2   . THR B 1 243 ? 0.022   -56.356 0.308   1.00 27.45 ? 243  THR B CG2   1 
ATOM   5897 N N     . TYR B 1 244 ? 1.583   -58.579 2.276   1.00 28.60 ? 244  TYR B N     1 
ATOM   5898 C CA    . TYR B 1 244 ? 1.237   -59.841 2.954   1.00 27.20 ? 244  TYR B CA    1 
ATOM   5899 C C     . TYR B 1 244 ? -0.171  -59.726 3.539   1.00 29.32 ? 244  TYR B C     1 
ATOM   5900 O O     . TYR B 1 244 ? -0.650  -58.594 3.845   1.00 26.08 ? 244  TYR B O     1 
ATOM   5901 C CB    . TYR B 1 244 ? 2.275   -60.159 4.023   1.00 27.29 ? 244  TYR B CB    1 
ATOM   5902 C CG    . TYR B 1 244 ? 2.389   -59.075 5.062   1.00 31.27 ? 244  TYR B CG    1 
ATOM   5903 C CD1   . TYR B 1 244 ? 3.213   -57.984 4.843   1.00 28.64 ? 244  TYR B CD1   1 
ATOM   5904 C CD2   . TYR B 1 244 ? 1.627   -59.108 6.224   1.00 28.26 ? 244  TYR B CD2   1 
ATOM   5905 C CE1   . TYR B 1 244 ? 3.319   -56.971 5.781   1.00 29.16 ? 244  TYR B CE1   1 
ATOM   5906 C CE2   . TYR B 1 244 ? 1.715   -58.095 7.164   1.00 28.54 ? 244  TYR B CE2   1 
ATOM   5907 C CZ    . TYR B 1 244 ? 2.575   -57.030 6.947   1.00 28.91 ? 244  TYR B CZ    1 
ATOM   5908 O OH    . TYR B 1 244 ? 2.652   -55.994 7.841   1.00 28.06 ? 244  TYR B OH    1 
ATOM   5909 N N     . GLN B 1 245 ? -0.797  -60.889 3.691   1.00 28.15 ? 245  GLN B N     1 
ATOM   5910 C CA    . GLN B 1 245 ? -2.132  -61.088 4.296   1.00 29.91 ? 245  GLN B CA    1 
ATOM   5911 C C     . GLN B 1 245 ? -1.937  -61.934 5.543   1.00 28.18 ? 245  GLN B C     1 
ATOM   5912 O O     . GLN B 1 245 ? -1.286  -62.974 5.460   1.00 28.03 ? 245  GLN B O     1 
ATOM   5913 C CB    . GLN B 1 245 ? -3.064  -61.762 3.287   1.00 30.36 ? 245  GLN B CB    1 
ATOM   5914 C CG    . GLN B 1 245 ? -4.409  -62.210 3.846   1.00 29.17 ? 245  GLN B CG    1 
ATOM   5915 C CD    . GLN B 1 245 ? -5.099  -63.155 2.886   1.00 30.64 ? 245  GLN B CD    1 
ATOM   5916 O OE1   . GLN B 1 245 ? -4.644  -64.279 2.665   1.00 35.20 ? 245  GLN B OE1   1 
ATOM   5917 N NE2   . GLN B 1 245 ? -6.201  -62.725 2.299   1.00 28.57 ? 245  GLN B NE2   1 
ATOM   5918 N N     . ILE B 1 246 ? -2.471  -61.499 6.672   1.00 29.08 ? 246  ILE B N     1 
ATOM   5919 C CA    . ILE B 1 246 ? -2.608  -62.382 7.856   1.00 29.42 ? 246  ILE B CA    1 
ATOM   5920 C C     . ILE B 1 246 ? -4.104  -62.618 8.076   1.00 32.42 ? 246  ILE B C     1 
ATOM   5921 O O     . ILE B 1 246 ? -4.830  -61.625 8.273   1.00 31.91 ? 246  ILE B O     1 
ATOM   5922 C CB    . ILE B 1 246 ? -1.956  -61.817 9.124   1.00 30.55 ? 246  ILE B CB    1 
ATOM   5923 C CG1   . ILE B 1 246 ? -0.696  -60.999 8.833   1.00 33.69 ? 246  ILE B CG1   1 
ATOM   5924 C CG2   . ILE B 1 246 ? -1.714  -62.957 10.099  1.00 29.66 ? 246  ILE B CG2   1 
ATOM   5925 C CD1   . ILE B 1 246 ? -0.170  -60.315 10.071  1.00 33.27 ? 246  ILE B CD1   1 
ATOM   5926 N N     . THR B 1 247 ? -4.537  -63.884 8.018   1.00 29.34 ? 247  THR B N     1 
ATOM   5927 C CA    . THR B 1 247 ? -5.916  -64.301 8.345   1.00 30.99 ? 247  THR B CA    1 
ATOM   5928 C C     . THR B 1 247 ? -5.916  -64.678 9.823   1.00 28.91 ? 247  THR B C     1 
ATOM   5929 O O     . THR B 1 247 ? -4.975  -65.333 10.275  1.00 28.43 ? 247  THR B O     1 
ATOM   5930 C CB    . THR B 1 247 ? -6.406  -65.451 7.448   1.00 31.84 ? 247  THR B CB    1 
ATOM   5931 O OG1   . THR B 1 247 ? -5.577  -66.593 7.651   1.00 29.94 ? 247  THR B OG1   1 
ATOM   5932 C CG2   . THR B 1 247 ? -6.422  -65.069 5.991   1.00 31.87 ? 247  THR B CG2   1 
ATOM   5933 N N     . PHE B 1 248 ? -6.946  -64.236 10.529  1.00 30.70 ? 248  PHE B N     1 
ATOM   5934 C CA    . PHE B 1 248 ? -7.210  -64.575 11.938  1.00 28.38 ? 248  PHE B CA    1 
ATOM   5935 C C     . PHE B 1 248 ? -8.596  -65.209 12.014  1.00 28.50 ? 248  PHE B C     1 
ATOM   5936 O O     . PHE B 1 248 ? -9.577  -64.631 11.477  1.00 29.17 ? 248  PHE B O     1 
ATOM   5937 C CB    . PHE B 1 248 ? -7.110  -63.312 12.799  1.00 28.91 ? 248  PHE B CB    1 
ATOM   5938 C CG    . PHE B 1 248 ? -5.759  -62.651 12.774  1.00 28.70 ? 248  PHE B CG    1 
ATOM   5939 C CD1   . PHE B 1 248 ? -4.739  -63.103 13.599  1.00 29.28 ? 248  PHE B CD1   1 
ATOM   5940 C CD2   . PHE B 1 248 ? -5.527  -61.554 11.954  1.00 27.61 ? 248  PHE B CD2   1 
ATOM   5941 C CE1   . PHE B 1 248 ? -3.505  -62.473 13.607  1.00 29.12 ? 248  PHE B CE1   1 
ATOM   5942 C CE2   . PHE B 1 248 ? -4.288  -60.924 11.963  1.00 27.42 ? 248  PHE B CE2   1 
ATOM   5943 C CZ    . PHE B 1 248 ? -3.284  -61.383 12.792  1.00 27.21 ? 248  PHE B CZ    1 
ATOM   5944 N N     . GLU B 1 249 ? -8.685  -66.325 12.731  1.00 31.41 ? 249  GLU B N     1 
ATOM   5945 C CA    . GLU B 1 249 ? -9.869  -67.214 12.672  1.00 34.36 ? 249  GLU B CA    1 
ATOM   5946 C C     . GLU B 1 249 ? -11.049 -66.598 13.405  1.00 36.41 ? 249  GLU B C     1 
ATOM   5947 O O     . GLU B 1 249 ? -12.145 -66.690 12.888  1.00 29.83 ? 249  GLU B O     1 
ATOM   5948 C CB    . GLU B 1 249 ? -9.521  -68.604 13.215  1.00 37.77 ? 249  GLU B CB    1 
ATOM   5949 C CG    . GLU B 1 249 ? -8.626  -69.390 12.254  1.00 43.13 ? 249  GLU B CG    1 
ATOM   5950 C CD    . GLU B 1 249 ? -9.340  -70.073 11.076  1.00 54.22 ? 249  GLU B CD    1 
ATOM   5951 O OE1   . GLU B 1 249 ? -10.324 -70.812 11.315  1.00 69.48 ? 249  GLU B OE1   1 
ATOM   5952 O OE2   . GLU B 1 249 ? -8.914  -69.861 9.911   1.00 57.89 ? 249  GLU B OE2   1 
ATOM   5953 N N     . ASN B 1 250 ? -10.811 -66.009 14.574  1.00 35.37 ? 250  ASN B N     1 
ATOM   5954 C CA    . ASN B 1 250 ? -11.874 -65.716 15.564  1.00 33.35 ? 250  ASN B CA    1 
ATOM   5955 C C     . ASN B 1 250 ? -12.212 -64.237 15.534  1.00 32.11 ? 250  ASN B C     1 
ATOM   5956 O O     . ASN B 1 250 ? -11.287 -63.425 15.550  1.00 34.86 ? 250  ASN B O     1 
ATOM   5957 C CB    . ASN B 1 250 ? -11.418 -66.150 16.947  1.00 37.01 ? 250  ASN B CB    1 
ATOM   5958 C CG    . ASN B 1 250 ? -10.946 -67.585 16.937  1.00 36.10 ? 250  ASN B CG    1 
ATOM   5959 O OD1   . ASN B 1 250 ? -11.683 -68.478 16.520  1.00 34.81 ? 250  ASN B OD1   1 
ATOM   5960 N ND2   . ASN B 1 250 ? -9.709  -67.802 17.322  1.00 32.83 ? 250  ASN B ND2   1 
ATOM   5961 N N     . GLU B 1 251 ? -13.493 -63.905 15.566  1.00 30.52 ? 251  GLU B N     1 
ATOM   5962 C CA    . GLU B 1 251 ? -13.927 -62.504 15.687  1.00 33.45 ? 251  GLU B CA    1 
ATOM   5963 C C     . GLU B 1 251 ? -13.299 -61.920 16.966  1.00 32.43 ? 251  GLU B C     1 
ATOM   5964 O O     . GLU B 1 251 ? -12.901 -60.744 16.935  1.00 28.45 ? 251  GLU B O     1 
ATOM   5965 C CB    . GLU B 1 251 ? -15.444 -62.409 15.568  1.00 36.95 ? 251  GLU B CB    1 
ATOM   5966 C CG    . GLU B 1 251 ? -16.219 -63.030 16.699  1.00 38.30 ? 251  GLU B CG    1 
ATOM   5967 C CD    . GLU B 1 251 ? -17.713 -62.879 16.471  1.00 39.28 ? 251  GLU B CD    1 
ATOM   5968 O OE1   . GLU B 1 251 ? -18.181 -63.195 15.359  1.00 39.17 ? 251  GLU B OE1   1 
ATOM   5969 O OE2   . GLU B 1 251 ? -18.385 -62.394 17.381  1.00 45.10 ? 251  GLU B OE2   1 
ATOM   5970 N N     . SER B 1 252 ? -13.104 -62.730 18.014  1.00 30.75 ? 252  SER B N     1 
ATOM   5971 C CA    . SER B 1 252 ? -12.539 -62.267 19.303  1.00 32.98 ? 252  SER B CA    1 
ATOM   5972 C C     . SER B 1 252 ? -11.022 -62.030 19.200  1.00 30.63 ? 252  SER B C     1 
ATOM   5973 O O     . SER B 1 252 ? -10.447 -61.491 20.164  1.00 30.81 ? 252  SER B O     1 
ATOM   5974 C CB    . SER B 1 252 ? -12.874 -63.241 20.404  1.00 34.11 ? 252  SER B CB    1 
ATOM   5975 O OG    . SER B 1 252 ? -12.177 -64.454 20.195  1.00 34.97 ? 252  SER B OG    1 
ATOM   5976 N N     . ASP B 1 253 ? -10.369 -62.385 18.087  1.00 29.11 ? 253  ASP B N     1 
ATOM   5977 C CA    . ASP B 1 253 ? -8.915  -62.129 17.890  1.00 29.97 ? 253  ASP B CA    1 
ATOM   5978 C C     . ASP B 1 253 ? -8.641  -60.625 17.782  1.00 29.07 ? 253  ASP B C     1 
ATOM   5979 O O     . ASP B 1 253 ? -7.486  -60.224 18.005  1.00 29.93 ? 253  ASP B O     1 
ATOM   5980 C CB    . ASP B 1 253 ? -8.372  -62.841 16.654  1.00 31.48 ? 253  ASP B CB    1 
ATOM   5981 C CG    . ASP B 1 253 ? -8.225  -64.341 16.826  1.00 32.26 ? 253  ASP B CG    1 
ATOM   5982 O OD1   . ASP B 1 253 ? -8.068  -64.785 17.980  1.00 31.58 ? 253  ASP B OD1   1 
ATOM   5983 O OD2   . ASP B 1 253 ? -8.260  -65.029 15.802  1.00 31.78 ? 253  ASP B OD2   1 
ATOM   5984 N N     . LEU B 1 254 ? -9.655  -59.832 17.430  1.00 29.35 ? 254  LEU B N     1 
ATOM   5985 C CA    . LEU B 1 254 ? -9.521  -58.374 17.183  1.00 29.26 ? 254  LEU B CA    1 
ATOM   5986 C C     . LEU B 1 254 ? -8.747  -57.720 18.330  1.00 30.85 ? 254  LEU B C     1 
ATOM   5987 O O     . LEU B 1 254 ? -7.846  -56.913 18.041  1.00 28.27 ? 254  LEU B O     1 
ATOM   5988 C CB    . LEU B 1 254 ? -10.915 -57.766 17.041  1.00 31.50 ? 254  LEU B CB    1 
ATOM   5989 C CG    . LEU B 1 254 ? -10.957 -56.247 16.917  1.00 32.24 ? 254  LEU B CG    1 
ATOM   5990 C CD1   . LEU B 1 254 ? -10.261 -55.800 15.635  1.00 29.80 ? 254  LEU B CD1   1 
ATOM   5991 C CD2   . LEU B 1 254 ? -12.399 -55.765 16.951  1.00 33.61 ? 254  LEU B CD2   1 
ATOM   5992 N N     . GLU B 1 255 ? -9.078  -58.053 19.578  1.00 30.95 ? 255  GLU B N     1 
ATOM   5993 C CA    . GLU B 1 255 ? -8.455  -57.393 20.758  1.00 33.94 ? 255  GLU B CA    1 
ATOM   5994 C C     . GLU B 1 255 ? -6.937  -57.567 20.690  1.00 31.42 ? 255  GLU B C     1 
ATOM   5995 O O     . GLU B 1 255 ? -6.212  -56.570 20.849  1.00 30.22 ? 255  GLU B O     1 
ATOM   5996 C CB    . GLU B 1 255 ? -9.015  -57.939 22.072  1.00 36.70 ? 255  GLU B CB    1 
ATOM   5997 C CG    . GLU B 1 255 ? -8.377  -57.302 23.293  1.00 38.08 ? 255  GLU B CG    1 
ATOM   5998 C CD    . GLU B 1 255 ? -9.137  -57.538 24.595  1.00 46.34 ? 255  GLU B CD    1 
ATOM   5999 O OE1   . GLU B 1 255 ? -10.279 -58.036 24.551  1.00 46.87 ? 255  GLU B OE1   1 
ATOM   6000 O OE2   . GLU B 1 255 ? -8.599  -57.188 25.645  1.00 53.85 ? 255  GLU B OE2   1 
ATOM   6001 N N     . GLN B 1 256 ? -6.460  -58.787 20.483  1.00 30.85 ? 256  GLN B N     1 
ATOM   6002 C CA    . GLN B 1 256 ? -5.017  -59.093 20.532  1.00 32.90 ? 256  GLN B CA    1 
ATOM   6003 C C     . GLN B 1 256 ? -4.342  -58.551 19.267  1.00 30.87 ? 256  GLN B C     1 
ATOM   6004 O O     . GLN B 1 256 ? -3.156  -58.153 19.338  1.00 30.77 ? 256  GLN B O     1 
ATOM   6005 C CB    . GLN B 1 256 ? -4.804  -60.590 20.686  1.00 38.41 ? 256  GLN B CB    1 
ATOM   6006 C CG    . GLN B 1 256 ? -3.359  -60.948 20.984  1.00 46.74 ? 256  GLN B CG    1 
ATOM   6007 C CD    . GLN B 1 256 ? -3.235  -62.326 21.595  1.00 48.76 ? 256  GLN B CD    1 
ATOM   6008 O OE1   . GLN B 1 256 ? -4.203  -63.083 21.672  1.00 52.50 ? 256  GLN B OE1   1 
ATOM   6009 N NE2   . GLN B 1 256 ? -2.019  -62.683 21.988  1.00 51.99 ? 256  GLN B NE2   1 
ATOM   6010 N N     . ILE B 1 257 ? -5.046  -58.555 18.142  1.00 27.70 ? 257  ILE B N     1 
ATOM   6011 C CA    . ILE B 1 257 ? -4.487  -58.055 16.857  1.00 26.26 ? 257  ILE B CA    1 
ATOM   6012 C C     . ILE B 1 257 ? -4.171  -56.571 17.024  1.00 26.84 ? 257  ILE B C     1 
ATOM   6013 O O     . ILE B 1 257 ? -3.077  -56.157 16.652  1.00 26.33 ? 257  ILE B O     1 
ATOM   6014 C CB    . ILE B 1 257 ? -5.437  -58.260 15.674  1.00 27.10 ? 257  ILE B CB    1 
ATOM   6015 C CG1   . ILE B 1 257 ? -5.695  -59.742 15.400  1.00 25.18 ? 257  ILE B CG1   1 
ATOM   6016 C CG2   . ILE B 1 257 ? -4.879  -57.562 14.433  1.00 24.82 ? 257  ILE B CG2   1 
ATOM   6017 C CD1   . ILE B 1 257 ? -6.978  -59.976 14.688  1.00 24.36 ? 257  ILE B CD1   1 
ATOM   6018 N N     . VAL B 1 258 ? -5.083  -55.818 17.609  1.00 25.74 ? 258  VAL B N     1 
ATOM   6019 C CA    . VAL B 1 258 ? -4.918  -54.351 17.742  1.00 28.75 ? 258  VAL B CA    1 
ATOM   6020 C C     . VAL B 1 258 ? -3.770  -54.112 18.727  1.00 28.95 ? 258  VAL B C     1 
ATOM   6021 O O     . VAL B 1 258 ? -2.915  -53.260 18.438  1.00 30.09 ? 258  VAL B O     1 
ATOM   6022 C CB    . VAL B 1 258 ? -6.237  -53.663 18.122  1.00 27.25 ? 258  VAL B CB    1 
ATOM   6023 C CG1   . VAL B 1 258 ? -6.046  -52.204 18.507  1.00 25.18 ? 258  VAL B CG1   1 
ATOM   6024 C CG2   . VAL B 1 258 ? -7.244  -53.780 16.985  1.00 27.21 ? 258  VAL B CG2   1 
ATOM   6025 N N     . ASP B 1 259 ? -3.687  -54.894 19.796  1.00 28.07 ? 259  ASP B N     1 
ATOM   6026 C CA    . ASP B 1 259 ? -2.648  -54.666 20.838  1.00 31.67 ? 259  ASP B CA    1 
ATOM   6027 C C     . ASP B 1 259 ? -1.256  -55.046 20.336  1.00 32.09 ? 259  ASP B C     1 
ATOM   6028 O O     . ASP B 1 259 ? -0.282  -54.465 20.833  1.00 30.11 ? 259  ASP B O     1 
ATOM   6029 C CB    . ASP B 1 259 ? -3.006  -55.364 22.146  1.00 30.96 ? 259  ASP B CB    1 
ATOM   6030 C CG    . ASP B 1 259 ? -4.153  -54.647 22.825  1.00 31.02 ? 259  ASP B CG    1 
ATOM   6031 O OD1   . ASP B 1 259 ? -4.350  -53.427 22.536  1.00 29.54 ? 259  ASP B OD1   1 
ATOM   6032 O OD2   . ASP B 1 259 ? -4.845  -55.287 23.616  1.00 31.66 ? 259  ASP B OD2   1 
ATOM   6033 N N     . ILE B 1 260 ? -1.155  -55.954 19.375  1.00 34.00 ? 260  ILE B N     1 
ATOM   6034 C CA    . ILE B 1 260 ? 0.143   -56.298 18.735  1.00 34.89 ? 260  ILE B CA    1 
ATOM   6035 C C     . ILE B 1 260 ? 0.449   -55.254 17.654  1.00 33.71 ? 260  ILE B C     1 
ATOM   6036 O O     . ILE B 1 260 ? 1.627   -54.894 17.511  1.00 34.72 ? 260  ILE B O     1 
ATOM   6037 C CB    . ILE B 1 260 ? 0.118   -57.746 18.203  1.00 35.30 ? 260  ILE B CB    1 
ATOM   6038 C CG1   . ILE B 1 260 ? 0.048   -58.746 19.362  1.00 35.69 ? 260  ILE B CG1   1 
ATOM   6039 C CG2   . ILE B 1 260 ? 1.312   -58.023 17.294  1.00 37.32 ? 260  ILE B CG2   1 
ATOM   6040 C CD1   . ILE B 1 260 ? -0.332  -60.145 18.941  1.00 34.83 ? 260  ILE B CD1   1 
ATOM   6041 N N     . MET B 1 261 ? -0.565  -54.789 16.927  1.00 31.34 ? 261  MET B N     1 
ATOM   6042 C CA    . MET B 1 261 ? -0.422  -53.836 15.793  1.00 33.22 ? 261  MET B CA    1 
ATOM   6043 C C     . MET B 1 261 ? 0.209   -52.528 16.283  1.00 35.95 ? 261  MET B C     1 
ATOM   6044 O O     . MET B 1 261 ? 1.182   -52.065 15.649  1.00 36.30 ? 261  MET B O     1 
ATOM   6045 C CB    . MET B 1 261 ? -1.777  -53.516 15.172  1.00 33.83 ? 261  MET B CB    1 
ATOM   6046 C CG    . MET B 1 261 ? -1.686  -52.915 13.808  1.00 38.18 ? 261  MET B CG    1 
ATOM   6047 S SD    . MET B 1 261 ? -3.320  -52.459 13.148  1.00 45.98 ? 261  MET B SD    1 
ATOM   6048 C CE    . MET B 1 261 ? -4.324  -53.810 13.757  1.00 30.76 ? 261  MET B CE    1 
ATOM   6049 N N     . LEU B 1 262 ? -0.301  -51.965 17.381  1.00 31.12 ? 262  LEU B N     1 
ATOM   6050 C CA    . LEU B 1 262 ? 0.065   -50.587 17.769  1.00 30.91 ? 262  LEU B CA    1 
ATOM   6051 C C     . LEU B 1 262 ? 1.581   -50.467 17.955  1.00 29.07 ? 262  LEU B C     1 
ATOM   6052 O O     . LEU B 1 262 ? 2.195   -49.604 17.328  1.00 29.80 ? 262  LEU B O     1 
ATOM   6053 C CB    . LEU B 1 262 ? -0.693  -50.114 19.007  1.00 30.41 ? 262  LEU B CB    1 
ATOM   6054 C CG    . LEU B 1 262 ? -0.094  -48.826 19.573  1.00 35.20 ? 262  LEU B CG    1 
ATOM   6055 C CD1   . LEU B 1 262 ? -0.435  -47.660 18.660  1.00 37.79 ? 262  LEU B CD1   1 
ATOM   6056 C CD2   . LEU B 1 262 ? -0.544  -48.596 21.009  1.00 39.91 ? 262  LEU B CD2   1 
ATOM   6057 N N     . PRO B 1 263 ? 2.240   -51.284 18.802  1.00 28.17 ? 263  PRO B N     1 
ATOM   6058 C CA    . PRO B 1 263 ? 3.680   -51.155 19.041  1.00 28.96 ? 263  PRO B CA    1 
ATOM   6059 C C     . PRO B 1 263 ? 4.524   -51.372 17.785  1.00 26.90 ? 263  PRO B C     1 
ATOM   6060 O O     . PRO B 1 263 ? 5.620   -50.840 17.694  1.00 27.77 ? 263  PRO B O     1 
ATOM   6061 C CB    . PRO B 1 263 ? 4.052   -52.235 20.066  1.00 29.42 ? 263  PRO B CB    1 
ATOM   6062 C CG    . PRO B 1 263 ? 2.747   -52.815 20.552  1.00 28.86 ? 263  PRO B CG    1 
ATOM   6063 C CD    . PRO B 1 263 ? 1.645   -52.349 19.622  1.00 30.98 ? 263  PRO B CD    1 
ATOM   6064 N N     . LEU B 1 264 ? 3.979   -52.095 16.819  1.00 29.31 ? 264  LEU B N     1 
ATOM   6065 C CA    . LEU B 1 264 ? 4.693   -52.383 15.544  1.00 28.59 ? 264  LEU B CA    1 
ATOM   6066 C C     . LEU B 1 264 ? 4.477   -51.259 14.534  1.00 26.03 ? 264  LEU B C     1 
ATOM   6067 O O     . LEU B 1 264 ? 5.222   -51.253 13.534  1.00 24.59 ? 264  LEU B O     1 
ATOM   6068 C CB    . LEU B 1 264 ? 4.193   -53.716 14.972  1.00 30.25 ? 264  LEU B CB    1 
ATOM   6069 C CG    . LEU B 1 264 ? 4.513   -54.957 15.810  1.00 34.57 ? 264  LEU B CG    1 
ATOM   6070 C CD1   . LEU B 1 264 ? 4.152   -56.207 15.047  1.00 36.09 ? 264  LEU B CD1   1 
ATOM   6071 C CD2   . LEU B 1 264 ? 5.972   -55.006 16.218  1.00 38.95 ? 264  LEU B CD2   1 
ATOM   6072 N N     . ARG B 1 265 ? 3.498   -50.370 14.750  1.00 26.63 ? 265  ARG B N     1 
ATOM   6073 C CA    . ARG B 1 265 ? 3.178   -49.285 13.780  1.00 26.59 ? 265  ARG B CA    1 
ATOM   6074 C C     . ARG B 1 265 ? 3.667   -47.924 14.303  1.00 25.64 ? 265  ARG B C     1 
ATOM   6075 O O     . ARG B 1 265 ? 3.965   -47.047 13.484  1.00 27.54 ? 265  ARG B O     1 
ATOM   6076 C CB    . ARG B 1 265 ? 1.668   -49.237 13.518  1.00 27.06 ? 265  ARG B CB    1 
ATOM   6077 C CG    . ARG B 1 265 ? 1.213   -48.083 12.634  1.00 25.88 ? 265  ARG B CG    1 
ATOM   6078 C CD    . ARG B 1 265 ? 1.918   -48.070 11.290  1.00 28.56 ? 265  ARG B CD    1 
ATOM   6079 N NE    . ARG B 1 265 ? 1.499   -46.910 10.494  1.00 27.26 ? 265  ARG B NE    1 
ATOM   6080 C CZ    . ARG B 1 265 ? 2.213   -46.340 9.524   1.00 28.59 ? 265  ARG B CZ    1 
ATOM   6081 N NH1   . ARG B 1 265 ? 3.413   -46.787 9.195   1.00 27.38 ? 265  ARG B NH1   1 
ATOM   6082 N NH2   . ARG B 1 265 ? 1.707   -45.300 8.888   1.00 34.30 ? 265  ARG B NH2   1 
ATOM   6083 N N     . ILE B 1 266 ? 3.675   -47.720 15.610  1.00 25.36 ? 266  ILE B N     1 
ATOM   6084 C CA    . ILE B 1 266 ? 3.779   -46.350 16.200  1.00 25.86 ? 266  ILE B CA    1 
ATOM   6085 C C     . ILE B 1 266 ? 5.131   -45.724 15.812  1.00 25.86 ? 266  ILE B C     1 
ATOM   6086 O O     . ILE B 1 266 ? 5.199   -44.487 15.739  1.00 25.21 ? 266  ILE B O     1 
ATOM   6087 C CB    . ILE B 1 266 ? 3.527   -46.388 17.713  1.00 26.45 ? 266  ILE B CB    1 
ATOM   6088 C CG1   . ILE B 1 266 ? 3.358   -44.981 18.293  1.00 27.83 ? 266  ILE B CG1   1 
ATOM   6089 C CG2   . ILE B 1 266 ? 4.608   -47.189 18.416  1.00 27.74 ? 266  ILE B CG2   1 
ATOM   6090 C CD1   . ILE B 1 266 ? 2.853   -44.978 19.725  1.00 26.15 ? 266  ILE B CD1   1 
ATOM   6091 N N     . ASN B 1 267 ? 6.155   -46.548 15.554  1.00 25.07 ? 267  ASN B N     1 
ATOM   6092 C CA    . ASN B 1 267 ? 7.511   -46.106 15.143  1.00 25.86 ? 267  ASN B CA    1 
ATOM   6093 C C     . ASN B 1 267 ? 7.622   -46.197 13.621  1.00 28.06 ? 267  ASN B C     1 
ATOM   6094 O O     . ASN B 1 267 ? 8.739   -46.047 13.142  1.00 33.72 ? 267  ASN B O     1 
ATOM   6095 C CB    . ASN B 1 267 ? 8.626   -46.910 15.826  1.00 26.68 ? 267  ASN B CB    1 
ATOM   6096 C CG    . ASN B 1 267 ? 8.556   -46.819 17.335  1.00 29.05 ? 267  ASN B CG    1 
ATOM   6097 O OD1   . ASN B 1 267 ? 8.558   -45.719 17.891  1.00 35.16 ? 267  ASN B OD1   1 
ATOM   6098 N ND2   . ASN B 1 267 ? 8.479   -47.954 18.011  1.00 27.56 ? 267  ASN B ND2   1 
ATOM   6099 N N     . MET B 1 268 ? 6.515   -46.422 12.896  1.00 28.55 ? 268  MET B N     1 
ATOM   6100 C CA    . MET B 1 268 ? 6.442   -46.580 11.411  1.00 32.35 ? 268  MET B CA    1 
ATOM   6101 C C     . MET B 1 268 ? 7.323   -47.736 10.890  1.00 33.20 ? 268  MET B C     1 
ATOM   6102 O O     . MET B 1 268 ? 7.643   -47.771 9.685   1.00 28.52 ? 268  MET B O     1 
ATOM   6103 C CB    . MET B 1 268 ? 6.839   -45.278 10.721  1.00 40.02 ? 268  MET B CB    1 
ATOM   6104 C CG    . MET B 1 268 ? 6.177   -44.048 11.350  1.00 44.33 ? 268  MET B CG    1 
ATOM   6105 S SD    . MET B 1 268 ? 6.424   -42.593 10.346  1.00 53.52 ? 268  MET B SD    1 
ATOM   6106 C CE    . MET B 1 268 ? 5.119   -42.878 9.149   1.00 51.39 ? 268  MET B CE    1 
ATOM   6107 N N     . ALA B 1 269 ? 7.621   -48.710 11.742  1.00 31.07 ? 269  ALA B N     1 
ATOM   6108 C CA    . ALA B 1 269 ? 8.376   -49.925 11.393  1.00 30.39 ? 269  ALA B CA    1 
ATOM   6109 C C     . ALA B 1 269 ? 8.233   -50.858 12.578  1.00 31.45 ? 269  ALA B C     1 
ATOM   6110 O O     . ALA B 1 269 ? 8.203   -50.381 13.720  1.00 30.19 ? 269  ALA B O     1 
ATOM   6111 C CB    . ALA B 1 269 ? 9.828   -49.592 11.119  1.00 32.06 ? 269  ALA B CB    1 
ATOM   6112 N N     . PRO B 1 270 ? 8.146   -52.189 12.360  1.00 30.53 ? 270  PRO B N     1 
ATOM   6113 C CA    . PRO B 1 270 ? 8.165   -52.787 11.010  1.00 29.91 ? 270  PRO B CA    1 
ATOM   6114 C C     . PRO B 1 270 ? 6.900   -52.602 10.150  1.00 29.63 ? 270  PRO B C     1 
ATOM   6115 O O     . PRO B 1 270 ? 6.958   -52.846 8.958   1.00 26.86 ? 270  PRO B O     1 
ATOM   6116 C CB    . PRO B 1 270 ? 8.336   -54.277 11.310  1.00 32.81 ? 270  PRO B CB    1 
ATOM   6117 C CG    . PRO B 1 270 ? 7.725   -54.434 12.693  1.00 31.94 ? 270  PRO B CG    1 
ATOM   6118 C CD    . PRO B 1 270 ? 8.139   -53.189 13.439  1.00 30.81 ? 270  PRO B CD    1 
ATOM   6119 N N     . LEU B 1 271 ? 5.775   -52.166 10.728  1.00 26.46 ? 271  LEU B N     1 
ATOM   6120 C CA    . LEU B 1 271 ? 4.552   -51.849 9.938   1.00 27.55 ? 271  LEU B CA    1 
ATOM   6121 C C     . LEU B 1 271 ? 4.754   -50.494 9.254   1.00 28.34 ? 271  LEU B C     1 
ATOM   6122 O O     . LEU B 1 271 ? 4.336   -49.465 9.807   1.00 26.52 ? 271  LEU B O     1 
ATOM   6123 C CB    . LEU B 1 271 ? 3.321   -51.859 10.844  1.00 27.13 ? 271  LEU B CB    1 
ATOM   6124 C CG    . LEU B 1 271 ? 2.976   -53.215 11.451  1.00 27.61 ? 271  LEU B CG    1 
ATOM   6125 C CD1   . LEU B 1 271 ? 1.700   -53.129 12.279  1.00 28.21 ? 271  LEU B CD1   1 
ATOM   6126 C CD2   . LEU B 1 271 ? 2.842   -54.271 10.365  1.00 27.79 ? 271  LEU B CD2   1 
ATOM   6127 N N     . GLN B 1 272 ? 5.332   -50.536 8.055   1.00 30.82 ? 272  GLN B N     1 
ATOM   6128 C CA    . GLN B 1 272 ? 5.879   -49.365 7.324   1.00 29.47 ? 272  GLN B CA    1 
ATOM   6129 C C     . GLN B 1 272 ? 4.754   -48.634 6.590   1.00 29.72 ? 272  GLN B C     1 
ATOM   6130 O O     . GLN B 1 272 ? 4.814   -47.411 6.502   1.00 32.63 ? 272  GLN B O     1 
ATOM   6131 C CB    . GLN B 1 272 ? 6.961   -49.837 6.351   1.00 30.33 ? 272  GLN B CB    1 
ATOM   6132 C CG    . GLN B 1 272 ? 8.247   -50.295 7.024   1.00 29.72 ? 272  GLN B CG    1 
ATOM   6133 C CD    . GLN B 1 272 ? 9.137   -50.929 5.980   1.00 34.61 ? 272  GLN B CD    1 
ATOM   6134 O OE1   . GLN B 1 272 ? 8.732   -51.851 5.266   1.00 31.86 ? 272  GLN B OE1   1 
ATOM   6135 N NE2   . GLN B 1 272 ? 10.341  -50.396 5.831   1.00 32.94 ? 272  GLN B NE2   1 
ATOM   6136 N N     . ASN B 1 273 ? 3.749   -49.342 6.104   1.00 26.25 ? 273  ASN B N     1 
ATOM   6137 C CA    . ASN B 1 273 ? 2.594   -48.707 5.429   1.00 26.36 ? 273  ASN B CA    1 
ATOM   6138 C C     . ASN B 1 273 ? 1.452   -48.581 6.446   1.00 24.33 ? 273  ASN B C     1 
ATOM   6139 O O     . ASN B 1 273 ? 1.672   -48.840 7.641   1.00 22.71 ? 273  ASN B O     1 
ATOM   6140 C CB    . ASN B 1 273 ? 2.213   -49.453 4.144   1.00 27.91 ? 273  ASN B CB    1 
ATOM   6141 C CG    . ASN B 1 273 ? 1.180   -50.540 4.375   1.00 26.17 ? 273  ASN B CG    1 
ATOM   6142 O OD1   . ASN B 1 273 ? 1.377   -51.396 5.235   1.00 25.20 ? 273  ASN B OD1   1 
ATOM   6143 N ND2   . ASN B 1 273 ? 0.082   -50.486 3.641   1.00 24.05 ? 273  ASN B ND2   1 
ATOM   6144 N N     . VAL B 1 274 ? 0.276   -48.147 5.987   1.00 23.05 ? 274  VAL B N     1 
ATOM   6145 C CA    . VAL B 1 274 ? -0.920  -48.036 6.857   1.00 23.99 ? 274  VAL B CA    1 
ATOM   6146 C C     . VAL B 1 274 ? -1.497  -49.447 6.963   1.00 24.74 ? 274  VAL B C     1 
ATOM   6147 O O     . VAL B 1 274 ? -1.970  -49.973 5.967   1.00 24.59 ? 274  VAL B O     1 
ATOM   6148 C CB    . VAL B 1 274 ? -1.961  -47.049 6.301   1.00 24.79 ? 274  VAL B CB    1 
ATOM   6149 C CG1   . VAL B 1 274 ? -3.214  -47.050 7.166   1.00 23.60 ? 274  VAL B CG1   1 
ATOM   6150 C CG2   . VAL B 1 274 ? -1.385  -45.640 6.109   1.00 23.12 ? 274  VAL B CG2   1 
ATOM   6151 N N     . PRO B 1 275 ? -1.499  -50.086 8.146   1.00 25.58 ? 275  PRO B N     1 
ATOM   6152 C CA    . PRO B 1 275 ? -2.089  -51.411 8.301   1.00 28.81 ? 275  PRO B CA    1 
ATOM   6153 C C     . PRO B 1 275 ? -3.618  -51.342 8.308   1.00 29.98 ? 275  PRO B C     1 
ATOM   6154 O O     . PRO B 1 275 ? -4.205  -50.426 8.890   1.00 29.93 ? 275  PRO B O     1 
ATOM   6155 C CB    . PRO B 1 275 ? -1.575  -51.903 9.646   1.00 26.65 ? 275  PRO B CB    1 
ATOM   6156 C CG    . PRO B 1 275 ? -1.350  -50.636 10.436  1.00 30.36 ? 275  PRO B CG    1 
ATOM   6157 C CD    . PRO B 1 275 ? -1.007  -49.563 9.422   1.00 28.30 ? 275  PRO B CD    1 
ATOM   6158 N N     . VAL B 1 276 ? -4.234  -52.290 7.616   1.00 29.04 ? 276  VAL B N     1 
ATOM   6159 C CA    . VAL B 1 276 ? -5.715  -52.403 7.550   1.00 27.44 ? 276  VAL B CA    1 
ATOM   6160 C C     . VAL B 1 276 ? -6.092  -53.812 8.000   1.00 26.79 ? 276  VAL B C     1 
ATOM   6161 O O     . VAL B 1 276 ? -5.394  -54.778 7.663   1.00 26.16 ? 276  VAL B O     1 
ATOM   6162 C CB    . VAL B 1 276 ? -6.286  -52.091 6.160   1.00 27.80 ? 276  VAL B CB    1 
ATOM   6163 C CG1   . VAL B 1 276 ? -5.864  -50.717 5.685   1.00 30.70 ? 276  VAL B CG1   1 
ATOM   6164 C CG2   . VAL B 1 276 ? -5.920  -53.143 5.125   1.00 28.55 ? 276  VAL B CG2   1 
ATOM   6165 N N     . LEU B 1 277 ? -7.158  -53.893 8.776   1.00 25.99 ? 277  LEU B N     1 
ATOM   6166 C CA    . LEU B 1 277 ? -7.700  -55.160 9.301   1.00 28.11 ? 277  LEU B CA    1 
ATOM   6167 C C     . LEU B 1 277 ? -9.160  -55.225 8.862   1.00 28.50 ? 277  LEU B C     1 
ATOM   6168 O O     . LEU B 1 277 ? -9.980  -54.494 9.450   1.00 28.58 ? 277  LEU B O     1 
ATOM   6169 C CB    . LEU B 1 277 ? -7.584  -55.195 10.818  1.00 27.03 ? 277  LEU B CB    1 
ATOM   6170 C CG    . LEU B 1 277 ? -7.994  -56.546 11.413  1.00 27.63 ? 277  LEU B CG    1 
ATOM   6171 C CD1   . LEU B 1 277 ? -6.949  -57.607 11.116  1.00 30.15 ? 277  LEU B CD1   1 
ATOM   6172 C CD2   . LEU B 1 277 ? -8.207  -56.440 12.911  1.00 29.55 ? 277  LEU B CD2   1 
ATOM   6173 N N     . ARG B 1 278 ? -9.422  -55.990 7.810   1.00 24.92 ? 278  ARG B N     1 
ATOM   6174 C CA    . ARG B 1 278 ? -10.737 -56.070 7.134   1.00 27.70 ? 278  ARG B CA    1 
ATOM   6175 C C     . ARG B 1 278 ? -11.478 -57.322 7.609   1.00 26.19 ? 278  ARG B C     1 
ATOM   6176 O O     . ARG B 1 278 ? -10.847 -58.379 7.676   1.00 28.51 ? 278  ARG B O     1 
ATOM   6177 C CB    . ARG B 1 278 ? -10.500 -56.108 5.625   1.00 31.19 ? 278  ARG B CB    1 
ATOM   6178 C CG    . ARG B 1 278 ? -9.857  -54.844 5.079   1.00 32.03 ? 278  ARG B CG    1 
ATOM   6179 C CD    . ARG B 1 278 ? -9.337  -55.082 3.677   1.00 31.90 ? 278  ARG B CD    1 
ATOM   6180 N NE    . ARG B 1 278 ? -10.372 -55.406 2.707   1.00 29.37 ? 278  ARG B NE    1 
ATOM   6181 C CZ    . ARG B 1 278 ? -10.908 -54.591 1.806   1.00 31.57 ? 278  ARG B CZ    1 
ATOM   6182 N NH1   . ARG B 1 278 ? -10.566 -53.319 1.712   1.00 32.26 ? 278  ARG B NH1   1 
ATOM   6183 N NH2   . ARG B 1 278 ? -11.810 -55.062 0.967   1.00 32.92 ? 278  ARG B NH2   1 
ATOM   6184 N N     . ASN B 1 279 ? -12.760 -57.192 7.933   1.00 25.43 ? 279  ASN B N     1 
ATOM   6185 C CA    . ASN B 1 279 ? -13.584 -58.336 8.384   1.00 25.79 ? 279  ASN B CA    1 
ATOM   6186 C C     . ASN B 1 279 ? -13.946 -59.186 7.168   1.00 27.08 ? 279  ASN B C     1 
ATOM   6187 O O     . ASN B 1 279 ? -13.753 -58.713 5.983   1.00 24.21 ? 279  ASN B O     1 
ATOM   6188 C CB    . ASN B 1 279 ? -14.771 -57.870 9.223   1.00 23.44 ? 279  ASN B CB    1 
ATOM   6189 C CG    . ASN B 1 279 ? -16.054 -57.683 8.450   1.00 26.95 ? 279  ASN B CG    1 
ATOM   6190 O OD1   . ASN B 1 279 ? -16.042 -57.041 7.402   1.00 33.49 ? 279  ASN B OD1   1 
ATOM   6191 N ND2   . ASN B 1 279 ? -17.138 -58.267 8.896   1.00 21.81 ? 279  ASN B ND2   1 
ATOM   6192 N N     . ILE B 1 280 ? -14.408 -60.412 7.419   1.00 25.44 ? 280  ILE B N     1 
ATOM   6193 C CA    . ILE B 1 280 ? -14.742 -61.388 6.340   1.00 26.24 ? 280  ILE B CA    1 
ATOM   6194 C C     . ILE B 1 280 ? -15.656 -60.731 5.300   1.00 28.00 ? 280  ILE B C     1 
ATOM   6195 O O     . ILE B 1 280 ? -15.463 -60.940 4.088   1.00 30.70 ? 280  ILE B O     1 
ATOM   6196 C CB    . ILE B 1 280 ? -15.364 -62.670 6.930   1.00 28.17 ? 280  ILE B CB    1 
ATOM   6197 C CG1   . ILE B 1 280 ? -15.743 -63.693 5.850   1.00 29.80 ? 280  ILE B CG1   1 
ATOM   6198 C CG2   . ILE B 1 280 ? -16.539 -62.324 7.828   1.00 29.19 ? 280  ILE B CG2   1 
ATOM   6199 C CD1   . ILE B 1 280 ? -14.600 -64.609 5.352   1.00 33.13 ? 280  ILE B CD1   1 
ATOM   6200 N N     . ILE B 1 281 ? -16.635 -59.956 5.734   1.00 28.71 ? 281  ILE B N     1 
ATOM   6201 C CA    . ILE B 1 281 ? -17.683 -59.451 4.816   1.00 31.62 ? 281  ILE B CA    1 
ATOM   6202 C C     . ILE B 1 281 ? -17.091 -58.405 3.853   1.00 34.21 ? 281  ILE B C     1 
ATOM   6203 O O     . ILE B 1 281 ? -17.356 -58.512 2.638   1.00 34.28 ? 281  ILE B O     1 
ATOM   6204 C CB    . ILE B 1 281 ? -18.931 -59.054 5.636   1.00 35.35 ? 281  ILE B CB    1 
ATOM   6205 C CG1   . ILE B 1 281 ? -19.813 -60.299 5.813   1.00 40.59 ? 281  ILE B CG1   1 
ATOM   6206 C CG2   . ILE B 1 281 ? -19.690 -57.914 5.003   1.00 38.72 ? 281  ILE B CG2   1 
ATOM   6207 C CD1   . ILE B 1 281 ? -20.524 -60.383 7.118   1.00 47.75 ? 281  ILE B CD1   1 
ATOM   6208 N N     . LEU B 1 282 ? -16.229 -57.485 4.267   1.00 32.89 ? 282  LEU B N     1 
ATOM   6209 C CA    . LEU B 1 282 ? -15.739 -56.516 3.241   1.00 36.42 ? 282  LEU B CA    1 
ATOM   6210 C C     . LEU B 1 282 ? -14.644 -57.177 2.385   1.00 32.04 ? 282  LEU B C     1 
ATOM   6211 O O     . LEU B 1 282 ? -14.477 -56.754 1.241   1.00 35.60 ? 282  LEU B O     1 
ATOM   6212 C CB    . LEU B 1 282 ? -15.385 -55.142 3.835   1.00 43.11 ? 282  LEU B CB    1 
ATOM   6213 C CG    . LEU B 1 282 ? -13.967 -54.930 4.311   1.00 45.15 ? 282  LEU B CG    1 
ATOM   6214 C CD1   . LEU B 1 282 ? -13.687 -53.460 4.602   1.00 43.84 ? 282  LEU B CD1   1 
ATOM   6215 C CD2   . LEU B 1 282 ? -13.742 -55.756 5.557   1.00 53.30 ? 282  LEU B CD2   1 
ATOM   6216 N N     . ASP B 1 283 ? -14.009 -58.265 2.832   1.00 30.61 ? 283  ASP B N     1 
ATOM   6217 C CA    . ASP B 1 283 ? -13.160 -59.096 1.934   1.00 29.38 ? 283  ASP B CA    1 
ATOM   6218 C C     . ASP B 1 283 ? -14.033 -59.934 0.992   1.00 31.69 ? 283  ASP B C     1 
ATOM   6219 O O     . ASP B 1 283 ? -13.703 -60.007 -0.217  1.00 32.71 ? 283  ASP B O     1 
ATOM   6220 C CB    . ASP B 1 283 ? -12.176 -59.974 2.704   1.00 31.26 ? 283  ASP B CB    1 
ATOM   6221 C CG    . ASP B 1 283 ? -10.802 -59.344 2.880   1.00 33.89 ? 283  ASP B CG    1 
ATOM   6222 O OD1   . ASP B 1 283 ? -10.702 -58.118 2.699   1.00 32.23 ? 283  ASP B OD1   1 
ATOM   6223 O OD2   . ASP B 1 283 ? -9.837  -60.082 3.160   1.00 35.21 ? 283  ASP B OD2   1 
ATOM   6224 N N     . ALA B 1 284 ? -15.084 -60.578 1.485   1.00 31.15 ? 284  ALA B N     1 
ATOM   6225 C CA    . ALA B 1 284 ? -15.909 -61.509 0.660   1.00 31.81 ? 284  ALA B CA    1 
ATOM   6226 C C     . ALA B 1 284 ? -16.712 -60.739 -0.392  1.00 32.78 ? 284  ALA B C     1 
ATOM   6227 O O     . ALA B 1 284 ? -16.870 -61.250 -1.520  1.00 33.31 ? 284  ALA B O     1 
ATOM   6228 C CB    . ALA B 1 284 ? -16.821 -62.329 1.543   1.00 31.95 ? 284  ALA B CB    1 
ATOM   6229 N N     . ALA B 1 285 ? -17.155 -59.523 -0.053  1.00 32.67 ? 285  ALA B N     1 
ATOM   6230 C CA    . ALA B 1 285 ? -18.051 -58.675 -0.867  1.00 33.51 ? 285  ALA B CA    1 
ATOM   6231 C C     . ALA B 1 285 ? -17.333 -58.168 -2.123  1.00 34.21 ? 285  ALA B C     1 
ATOM   6232 O O     . ALA B 1 285 ? -18.053 -57.829 -3.090  1.00 34.28 ? 285  ALA B O     1 
ATOM   6233 C CB    . ALA B 1 285 ? -18.604 -57.540 -0.044  1.00 34.28 ? 285  ALA B CB    1 
ATOM   6234 N N     . VAL B 1 286 ? -15.996 -58.169 -2.136  1.00 33.18 ? 286  VAL B N     1 
ATOM   6235 C CA    . VAL B 1 286 ? -15.201 -57.810 -3.349  1.00 35.12 ? 286  VAL B CA    1 
ATOM   6236 C C     . VAL B 1 286 ? -15.306 -58.929 -4.399  1.00 34.10 ? 286  VAL B C     1 
ATOM   6237 O O     . VAL B 1 286 ? -15.248 -58.604 -5.582  1.00 35.59 ? 286  VAL B O     1 
ATOM   6238 C CB    . VAL B 1 286 ? -13.730 -57.498 -3.007  1.00 35.74 ? 286  VAL B CB    1 
ATOM   6239 C CG1   . VAL B 1 286 ? -12.903 -57.202 -4.252  1.00 38.21 ? 286  VAL B CG1   1 
ATOM   6240 C CG2   . VAL B 1 286 ? -13.639 -56.328 -2.048  1.00 39.31 ? 286  VAL B CG2   1 
ATOM   6241 N N     . VAL B 1 287 ? -15.469 -60.188 -4.000  1.00 34.07 ? 287  VAL B N     1 
ATOM   6242 C CA    . VAL B 1 287 ? -15.313 -61.362 -4.914  1.00 37.84 ? 287  VAL B CA    1 
ATOM   6243 C C     . VAL B 1 287 ? -16.585 -62.208 -4.963  1.00 38.68 ? 287  VAL B C     1 
ATOM   6244 O O     . VAL B 1 287 ? -16.552 -63.270 -5.571  1.00 43.52 ? 287  VAL B O     1 
ATOM   6245 C CB    . VAL B 1 287 ? -14.119 -62.239 -4.503  1.00 38.92 ? 287  VAL B CB    1 
ATOM   6246 C CG1   . VAL B 1 287 ? -12.799 -61.485 -4.636  1.00 39.67 ? 287  VAL B CG1   1 
ATOM   6247 C CG2   . VAL B 1 287 ? -14.277 -62.827 -3.109  1.00 38.25 ? 287  VAL B CG2   1 
ATOM   6248 N N     . SER B 1 288 ? -17.664 -61.779 -4.330  1.00 38.68 ? 288  SER B N     1 
ATOM   6249 C CA    . SER B 1 288 ? -18.898 -62.597 -4.211  1.00 37.68 ? 288  SER B CA    1 
ATOM   6250 C C     . SER B 1 288 ? -20.080 -61.689 -3.892  1.00 38.06 ? 288  SER B C     1 
ATOM   6251 O O     . SER B 1 288 ? -19.854 -60.474 -3.609  1.00 35.68 ? 288  SER B O     1 
ATOM   6252 C CB    . SER B 1 288 ? -18.728 -63.676 -3.178  1.00 35.35 ? 288  SER B CB    1 
ATOM   6253 O OG    . SER B 1 288 ? -18.693 -63.139 -1.865  1.00 32.20 ? 288  SER B OG    1 
ATOM   6254 N N     . GLN B 1 289 ? -21.281 -62.270 -3.937  1.00 36.95 ? 289  GLN B N     1 
ATOM   6255 C CA    . GLN B 1 289 ? -22.560 -61.585 -3.648  1.00 41.61 ? 289  GLN B CA    1 
ATOM   6256 C C     . GLN B 1 289 ? -23.172 -62.219 -2.396  1.00 38.20 ? 289  GLN B C     1 
ATOM   6257 O O     . GLN B 1 289 ? -22.840 -63.372 -2.097  1.00 39.65 ? 289  GLN B O     1 
ATOM   6258 C CB    . GLN B 1 289 ? -23.440 -61.663 -4.894  1.00 47.66 ? 289  GLN B CB    1 
ATOM   6259 C CG    . GLN B 1 289 ? -22.653 -61.340 -6.161  1.00 56.65 ? 289  GLN B CG    1 
ATOM   6260 C CD    . GLN B 1 289 ? -23.533 -61.080 -7.353  1.00 66.62 ? 289  GLN B CD    1 
ATOM   6261 O OE1   . GLN B 1 289 ? -23.052 -60.899 -8.464  1.00 74.01 ? 289  GLN B OE1   1 
ATOM   6262 N NE2   . GLN B 1 289 ? -24.834 -61.049 -7.125  1.00 75.86 ? 289  GLN B NE2   1 
ATOM   6263 N N     . ARG B 1 290 ? -23.984 -61.459 -1.660  1.00 35.97 ? 290  ARG B N     1 
ATOM   6264 C CA    . ARG B 1 290 ? -24.573 -61.912 -0.369  1.00 37.03 ? 290  ARG B CA    1 
ATOM   6265 C C     . ARG B 1 290 ? -25.383 -63.199 -0.625  1.00 38.78 ? 290  ARG B C     1 
ATOM   6266 O O     . ARG B 1 290 ? -25.264 -64.156 0.154   1.00 33.18 ? 290  ARG B O     1 
ATOM   6267 C CB    . ARG B 1 290 ? -25.446 -60.809 0.233   1.00 37.73 ? 290  ARG B CB    1 
ATOM   6268 C CG    . ARG B 1 290 ? -25.767 -61.031 1.707   1.00 37.20 ? 290  ARG B CG    1 
ATOM   6269 C CD    . ARG B 1 290 ? -26.759 -60.001 2.171   1.00 37.97 ? 290  ARG B CD    1 
ATOM   6270 N NE    . ARG B 1 290 ? -26.978 -60.010 3.605   1.00 34.86 ? 290  ARG B NE    1 
ATOM   6271 C CZ    . ARG B 1 290 ? -27.989 -60.617 4.238   1.00 37.57 ? 290  ARG B CZ    1 
ATOM   6272 N NH1   . ARG B 1 290 ? -28.871 -61.345 3.574   1.00 35.78 ? 290  ARG B NH1   1 
ATOM   6273 N NH2   . ARG B 1 290 ? -28.099 -60.503 5.550   1.00 35.65 ? 290  ARG B NH2   1 
ATOM   6274 N N     . ALA B 1 291 ? -26.145 -63.214 -1.724  1.00 45.61 ? 291  ALA B N     1 
ATOM   6275 C CA    . ALA B 1 291 ? -27.029 -64.321 -2.154  1.00 43.48 ? 291  ALA B CA    1 
ATOM   6276 C C     . ALA B 1 291 ? -26.221 -65.619 -2.326  1.00 46.00 ? 291  ALA B C     1 
ATOM   6277 O O     . ALA B 1 291 ? -26.820 -66.693 -2.126  1.00 40.37 ? 291  ALA B O     1 
ATOM   6278 C CB    . ALA B 1 291 ? -27.753 -63.921 -3.414  1.00 45.73 ? 291  ALA B CB    1 
ATOM   6279 N N     . ASP B 1 292 ? -24.910 -65.540 -2.617  1.00 43.53 ? 292  ASP B N     1 
ATOM   6280 C CA    . ASP B 1 292 ? -24.026 -66.730 -2.766  1.00 42.47 ? 292  ASP B CA    1 
ATOM   6281 C C     . ASP B 1 292 ? -23.889 -67.496 -1.451  1.00 41.04 ? 292  ASP B C     1 
ATOM   6282 O O     . ASP B 1 292 ? -23.547 -68.675 -1.516  1.00 43.59 ? 292  ASP B O     1 
ATOM   6283 C CB    . ASP B 1 292 ? -22.615 -66.368 -3.224  1.00 45.75 ? 292  ASP B CB    1 
ATOM   6284 C CG    . ASP B 1 292 ? -22.585 -65.669 -4.562  1.00 50.03 ? 292  ASP B CG    1 
ATOM   6285 O OD1   . ASP B 1 292 ? -23.613 -65.729 -5.263  1.00 53.37 ? 292  ASP B OD1   1 
ATOM   6286 O OD2   . ASP B 1 292 ? -21.547 -65.052 -4.871  1.00 51.73 ? 292  ASP B OD2   1 
ATOM   6287 N N     . TRP B 1 293 ? -24.102 -66.852 -0.304  1.00 39.81 ? 293  TRP B N     1 
ATOM   6288 C CA    . TRP B 1 293 ? -23.800 -67.441 1.027   1.00 38.40 ? 293  TRP B CA    1 
ATOM   6289 C C     . TRP B 1 293 ? -25.078 -67.685 1.841   1.00 37.21 ? 293  TRP B C     1 
ATOM   6290 O O     . TRP B 1 293 ? -25.014 -68.469 2.799   1.00 38.11 ? 293  TRP B O     1 
ATOM   6291 C CB    . TRP B 1 293 ? -22.839 -66.512 1.775   1.00 36.68 ? 293  TRP B CB    1 
ATOM   6292 C CG    . TRP B 1 293 ? -21.670 -66.110 0.933   1.00 35.52 ? 293  TRP B CG    1 
ATOM   6293 C CD1   . TRP B 1 293 ? -21.446 -64.889 0.363   1.00 34.38 ? 293  TRP B CD1   1 
ATOM   6294 C CD2   . TRP B 1 293 ? -20.577 -66.949 0.530   1.00 33.61 ? 293  TRP B CD2   1 
ATOM   6295 N NE1   . TRP B 1 293 ? -20.268 -64.902 -0.335  1.00 33.38 ? 293  TRP B NE1   1 
ATOM   6296 C CE2   . TRP B 1 293 ? -19.714 -66.152 -0.259  1.00 33.37 ? 293  TRP B CE2   1 
ATOM   6297 C CE3   . TRP B 1 293 ? -20.237 -68.284 0.755   1.00 34.65 ? 293  TRP B CE3   1 
ATOM   6298 C CZ2   . TRP B 1 293 ? -18.535 -66.651 -0.810  1.00 35.98 ? 293  TRP B CZ2   1 
ATOM   6299 C CZ3   . TRP B 1 293 ? -19.074 -68.782 0.202   1.00 39.10 ? 293  TRP B CZ3   1 
ATOM   6300 C CH2   . TRP B 1 293 ? -18.232 -67.970 -0.569  1.00 36.78 ? 293  TRP B CH2   1 
ATOM   6301 N N     . TYR B 1 294 ? -26.159 -66.984 1.510   1.00 40.83 ? 294  TYR B N     1 
ATOM   6302 C CA    . TYR B 1 294 ? -27.394 -66.874 2.329   1.00 44.08 ? 294  TYR B CA    1 
ATOM   6303 C C     . TYR B 1 294 ? -28.463 -66.140 1.515   1.00 49.94 ? 294  TYR B C     1 
ATOM   6304 O O     . TYR B 1 294 ? -28.155 -65.111 0.861   1.00 46.31 ? 294  TYR B O     1 
ATOM   6305 C CB    . TYR B 1 294 ? -27.108 -66.149 3.645   1.00 46.06 ? 294  TYR B CB    1 
ATOM   6306 C CG    . TYR B 1 294 ? -28.236 -66.177 4.646   1.00 48.81 ? 294  TYR B CG    1 
ATOM   6307 C CD1   . TYR B 1 294 ? -28.631 -67.371 5.237   1.00 49.30 ? 294  TYR B CD1   1 
ATOM   6308 C CD2   . TYR B 1 294 ? -28.895 -65.013 5.025   1.00 46.65 ? 294  TYR B CD2   1 
ATOM   6309 C CE1   . TYR B 1 294 ? -29.647 -67.410 6.175   1.00 48.27 ? 294  TYR B CE1   1 
ATOM   6310 C CE2   . TYR B 1 294 ? -29.915 -65.036 5.969   1.00 47.08 ? 294  TYR B CE2   1 
ATOM   6311 C CZ    . TYR B 1 294 ? -30.291 -66.240 6.542   1.00 52.23 ? 294  TYR B CZ    1 
ATOM   6312 O OH    . TYR B 1 294 ? -31.299 -66.281 7.461   1.00 55.25 ? 294  TYR B OH    1 
ATOM   6313 N N     . ASP B 1 295 ? -29.680 -66.692 1.507   1.00 59.89 ? 295  ASP B N     1 
ATOM   6314 C CA    . ASP B 1 295 ? -30.825 -66.139 0.736   1.00 65.56 ? 295  ASP B CA    1 
ATOM   6315 C C     . ASP B 1 295 ? -32.055 -66.046 1.645   1.00 67.36 ? 295  ASP B C     1 
ATOM   6316 O O     . ASP B 1 295 ? -33.120 -65.691 1.114   1.00 63.03 ? 295  ASP B O     1 
ATOM   6317 C CB    . ASP B 1 295 ? -31.094 -66.974 -0.520  1.00 71.76 ? 295  ASP B CB    1 
ATOM   6318 C CG    . ASP B 1 295 ? -31.193 -68.463 -0.242  1.00 72.77 ? 295  ASP B CG    1 
ATOM   6319 O OD1   . ASP B 1 295 ? -31.724 -68.832 0.822   1.00 73.25 ? 295  ASP B OD1   1 
ATOM   6320 O OD2   . ASP B 1 295 ? -30.738 -69.241 -1.094  1.00 78.63 ? 295  ASP B OD2   1 
ATOM   6321 N N     . GLY B 1 296 ? -31.903 -66.356 2.944   1.00 69.37 ? 296  GLY B N     1 
ATOM   6322 C CA    . GLY B 1 296 ? -32.921 -66.137 3.991   1.00 65.65 ? 296  GLY B CA    1 
ATOM   6323 C C     . GLY B 1 296 ? -32.974 -64.672 4.391   1.00 63.72 ? 296  GLY B C     1 
ATOM   6324 O O     . GLY B 1 296 ? -32.130 -63.909 3.920   1.00 70.46 ? 296  GLY B O     1 
ATOM   6325 N N     . ASP B 1 297 ? -33.935 -64.274 5.221   1.00 66.87 ? 297  ASP B N     1 
ATOM   6326 C CA    . ASP B 1 297 ? -34.017 -62.884 5.747   1.00 66.05 ? 297  ASP B CA    1 
ATOM   6327 C C     . ASP B 1 297 ? -33.318 -62.864 7.115   1.00 56.46 ? 297  ASP B C     1 
ATOM   6328 O O     . ASP B 1 297 ? -32.898 -63.929 7.589   1.00 50.97 ? 297  ASP B O     1 
ATOM   6329 C CB    . ASP B 1 297 ? -35.459 -62.363 5.755   1.00 74.08 ? 297  ASP B CB    1 
ATOM   6330 C CG    . ASP B 1 297 ? -36.496 -63.430 6.054   1.00 77.22 ? 297  ASP B CG    1 
ATOM   6331 O OD1   . ASP B 1 297 ? -36.128 -64.442 6.679   1.00 81.55 ? 297  ASP B OD1   1 
ATOM   6332 O OD2   . ASP B 1 297 ? -37.655 -63.242 5.660   1.00 82.71 ? 297  ASP B OD2   1 
ATOM   6333 N N     . GLY B 1 298 ? -33.157 -61.677 7.697   1.00 49.65 ? 298  GLY B N     1 
ATOM   6334 C CA    . GLY B 1 298 ? -32.410 -61.462 8.943   1.00 44.54 ? 298  GLY B CA    1 
ATOM   6335 C C     . GLY B 1 298 ? -30.908 -61.401 8.680   1.00 42.45 ? 298  GLY B C     1 
ATOM   6336 O O     . GLY B 1 298 ? -30.449 -61.550 7.551   1.00 44.23 ? 298  GLY B O     1 
ATOM   6337 N N     . PRO B 1 299 ? -30.097 -61.207 9.735   1.00 41.71 ? 299  PRO B N     1 
ATOM   6338 C CA    . PRO B 1 299 ? -28.650 -61.095 9.573   1.00 37.66 ? 299  PRO B CA    1 
ATOM   6339 C C     . PRO B 1 299 ? -28.028 -62.375 8.993   1.00 41.64 ? 299  PRO B C     1 
ATOM   6340 O O     . PRO B 1 299 ? -28.644 -63.422 9.065   1.00 37.62 ? 299  PRO B O     1 
ATOM   6341 C CB    . PRO B 1 299 ? -28.138 -60.899 11.004  1.00 42.52 ? 299  PRO B CB    1 
ATOM   6342 C CG    . PRO B 1 299 ? -29.347 -60.410 11.797  1.00 42.37 ? 299  PRO B CG    1 
ATOM   6343 C CD    . PRO B 1 299 ? -30.541 -61.052 11.129  1.00 43.22 ? 299  PRO B CD    1 
ATOM   6344 N N     . LEU B 1 300 ? -26.821 -62.274 8.450   1.00 35.20 ? 300  LEU B N     1 
ATOM   6345 C CA    . LEU B 1 300 ? -26.030 -63.464 8.048   1.00 36.91 ? 300  LEU B CA    1 
ATOM   6346 C C     . LEU B 1 300 ? -25.828 -64.335 9.277   1.00 38.84 ? 300  LEU B C     1 
ATOM   6347 O O     . LEU B 1 300 ? -25.334 -63.862 10.311  1.00 37.86 ? 300  LEU B O     1 
ATOM   6348 C CB    . LEU B 1 300 ? -24.694 -63.034 7.434   1.00 35.85 ? 300  LEU B CB    1 
ATOM   6349 C CG    . LEU B 1 300 ? -24.829 -62.306 6.098   1.00 39.17 ? 300  LEU B CG    1 
ATOM   6350 C CD1   . LEU B 1 300 ? -23.587 -61.471 5.781   1.00 39.71 ? 300  LEU B CD1   1 
ATOM   6351 C CD2   . LEU B 1 300 ? -25.144 -63.294 4.966   1.00 36.99 ? 300  LEU B CD2   1 
ATOM   6352 N N     . PRO B 1 301 ? -26.214 -65.629 9.210   1.00 38.57 ? 301  PRO B N     1 
ATOM   6353 C CA    . PRO B 1 301 ? -25.969 -66.541 10.321  1.00 40.33 ? 301  PRO B CA    1 
ATOM   6354 C C     . PRO B 1 301 ? -24.485 -66.886 10.390  1.00 35.29 ? 301  PRO B C     1 
ATOM   6355 O O     . PRO B 1 301 ? -23.783 -66.827 9.388   1.00 35.94 ? 301  PRO B O     1 
ATOM   6356 C CB    . PRO B 1 301 ? -26.830 -67.770 9.996   1.00 40.63 ? 301  PRO B CB    1 
ATOM   6357 C CG    . PRO B 1 301 ? -26.962 -67.752 8.487   1.00 41.76 ? 301  PRO B CG    1 
ATOM   6358 C CD    . PRO B 1 301 ? -26.883 -66.289 8.072   1.00 40.78 ? 301  PRO B CD    1 
ATOM   6359 N N     . PRO B 1 302 ? -23.976 -67.271 11.575  1.00 35.97 ? 302  PRO B N     1 
ATOM   6360 C CA    . PRO B 1 302 ? -22.577 -67.656 11.727  1.00 38.05 ? 302  PRO B CA    1 
ATOM   6361 C C     . PRO B 1 302 ? -22.077 -68.681 10.703  1.00 43.78 ? 302  PRO B C     1 
ATOM   6362 O O     . PRO B 1 302 ? -20.915 -68.602 10.317  1.00 44.17 ? 302  PRO B O     1 
ATOM   6363 C CB    . PRO B 1 302 ? -22.563 -68.243 13.142  1.00 39.29 ? 302  PRO B CB    1 
ATOM   6364 C CG    . PRO B 1 302 ? -23.597 -67.415 13.874  1.00 39.21 ? 302  PRO B CG    1 
ATOM   6365 C CD    . PRO B 1 302 ? -24.709 -67.290 12.857  1.00 37.87 ? 302  PRO B CD    1 
ATOM   6366 N N     . GLU B 1 303 ? -22.933 -69.608 10.265  1.00 44.15 ? 303  GLU B N     1 
ATOM   6367 C CA    . GLU B 1 303 ? -22.489 -70.697 9.350   1.00 41.70 ? 303  GLU B CA    1 
ATOM   6368 C C     . GLU B 1 303 ? -22.291 -70.116 7.944   1.00 40.53 ? 303  GLU B C     1 
ATOM   6369 O O     . GLU B 1 303 ? -21.432 -70.640 7.231   1.00 37.63 ? 303  GLU B O     1 
ATOM   6370 C CB    . GLU B 1 303 ? -23.429 -71.914 9.380   1.00 43.48 ? 303  GLU B CB    1 
ATOM   6371 C CG    . GLU B 1 303 ? -24.880 -71.621 9.091   1.00 45.51 ? 303  GLU B CG    1 
ATOM   6372 C CD    . GLU B 1 303 ? -25.745 -71.466 10.323  1.00 46.26 ? 303  GLU B CD    1 
ATOM   6373 O OE1   . GLU B 1 303 ? -26.885 -72.030 10.310  1.00 39.85 ? 303  GLU B OE1   1 
ATOM   6374 O OE2   . GLU B 1 303 ? -25.274 -70.798 11.288  1.00 45.92 ? 303  GLU B OE2   1 
ATOM   6375 N N     . ALA B 1 304 ? -23.032 -69.070 7.559   1.00 34.16 ? 304  ALA B N     1 
ATOM   6376 C CA    . ALA B 1 304 ? -22.789 -68.307 6.312   1.00 35.46 ? 304  ALA B CA    1 
ATOM   6377 C C     . ALA B 1 304 ? -21.394 -67.661 6.385   1.00 36.48 ? 304  ALA B C     1 
ATOM   6378 O O     . ALA B 1 304 ? -20.668 -67.763 5.404   1.00 37.88 ? 304  ALA B O     1 
ATOM   6379 C CB    . ALA B 1 304 ? -23.848 -67.275 6.075   1.00 36.81 ? 304  ALA B CB    1 
ATOM   6380 N N     . ILE B 1 305 ? -21.031 -67.035 7.509   1.00 35.41 ? 305  ILE B N     1 
ATOM   6381 C CA    . ILE B 1 305 ? -19.679 -66.432 7.712   1.00 33.52 ? 305  ILE B CA    1 
ATOM   6382 C C     . ILE B 1 305 ? -18.629 -67.534 7.571   1.00 34.71 ? 305  ILE B C     1 
ATOM   6383 O O     . ILE B 1 305 ? -17.586 -67.297 6.908   1.00 28.88 ? 305  ILE B O     1 
ATOM   6384 C CB    . ILE B 1 305 ? -19.587 -65.739 9.092   1.00 37.25 ? 305  ILE B CB    1 
ATOM   6385 C CG1   . ILE B 1 305 ? -20.561 -64.564 9.236   1.00 38.87 ? 305  ILE B CG1   1 
ATOM   6386 C CG2   . ILE B 1 305 ? -18.148 -65.374 9.439   1.00 38.28 ? 305  ILE B CG2   1 
ATOM   6387 C CD1   . ILE B 1 305 ? -20.751 -63.698 8.036   1.00 38.04 ? 305  ILE B CD1   1 
ATOM   6388 N N     . GLU B 1 306 ? -18.856 -68.681 8.222   1.00 31.02 ? 306  GLU B N     1 
ATOM   6389 C CA    . GLU B 1 306 ? -17.892 -69.798 8.193   1.00 30.56 ? 306  GLU B CA    1 
ATOM   6390 C C     . GLU B 1 306 ? -17.763 -70.293 6.752   1.00 29.47 ? 306  GLU B C     1 
ATOM   6391 O O     . GLU B 1 306 ? -16.644 -70.636 6.355   1.00 29.01 ? 306  GLU B O     1 
ATOM   6392 C CB    . GLU B 1 306 ? -18.277 -70.895 9.185   1.00 31.16 ? 306  GLU B CB    1 
ATOM   6393 C CG    . GLU B 1 306 ? -17.871 -70.570 10.609  1.00 32.29 ? 306  GLU B CG    1 
ATOM   6394 C CD    . GLU B 1 306 ? -16.409 -70.211 10.816  1.00 32.76 ? 306  GLU B CD    1 
ATOM   6395 O OE1   . GLU B 1 306 ? -15.557 -70.624 10.032  1.00 33.74 ? 306  GLU B OE1   1 
ATOM   6396 O OE2   . GLU B 1 306 ? -16.110 -69.520 11.805  1.00 32.72 ? 306  GLU B OE2   1 
ATOM   6397 N N     . ARG B 1 307 ? -18.844 -70.316 5.985   1.00 33.14 ? 307  ARG B N     1 
ATOM   6398 C CA    . ARG B 1 307 ? -18.799 -70.757 4.568   1.00 37.84 ? 307  ARG B CA    1 
ATOM   6399 C C     . ARG B 1 307 ? -17.920 -69.786 3.768   1.00 35.65 ? 307  ARG B C     1 
ATOM   6400 O O     . ARG B 1 307 ? -17.172 -70.257 2.897   1.00 32.79 ? 307  ARG B O     1 
ATOM   6401 C CB    . ARG B 1 307 ? -20.205 -70.882 3.962   1.00 45.20 ? 307  ARG B CB    1 
ATOM   6402 C CG    . ARG B 1 307 ? -20.727 -72.313 3.903   1.00 57.73 ? 307  ARG B CG    1 
ATOM   6403 C CD    . ARG B 1 307 ? -21.948 -72.524 3.015   1.00 59.79 ? 307  ARG B CD    1 
ATOM   6404 N NE    . ARG B 1 307 ? -23.062 -71.616 3.317   1.00 67.17 ? 307  ARG B NE    1 
ATOM   6405 C CZ    . ARG B 1 307 ? -23.828 -71.649 4.420   1.00 64.12 ? 307  ARG B CZ    1 
ATOM   6406 N NH1   . ARG B 1 307 ? -23.619 -72.545 5.375   1.00 65.00 ? 307  ARG B NH1   1 
ATOM   6407 N NH2   . ARG B 1 307 ? -24.807 -70.771 4.560   1.00 64.20 ? 307  ARG B NH2   1 
ATOM   6408 N N     . MET B 1 308 ? -18.051 -68.476 4.001   1.00 32.45 ? 308  MET B N     1 
ATOM   6409 C CA    . MET B 1 308 ? -17.194 -67.454 3.330   1.00 35.63 ? 308  MET B CA    1 
ATOM   6410 C C     . MET B 1 308 ? -15.724 -67.695 3.681   1.00 30.93 ? 308  MET B C     1 
ATOM   6411 O O     . MET B 1 308 ? -14.896 -67.716 2.769   1.00 32.75 ? 308  MET B O     1 
ATOM   6412 C CB    . MET B 1 308 ? -17.571 -66.042 3.771   1.00 35.42 ? 308  MET B CB    1 
ATOM   6413 C CG    . MET B 1 308 ? -18.926 -65.642 3.329   1.00 36.60 ? 308  MET B CG    1 
ATOM   6414 S SD    . MET B 1 308 ? -19.371 -64.084 4.104   1.00 36.36 ? 308  MET B SD    1 
ATOM   6415 C CE    . MET B 1 308 ? -21.154 -64.122 3.914   1.00 36.01 ? 308  MET B CE    1 
ATOM   6416 N N     . LYS B 1 309 ? -15.415 -67.868 4.942   1.00 31.84 ? 309  LYS B N     1 
ATOM   6417 C CA    . LYS B 1 309 ? -14.066 -68.111 5.362   1.00 32.16 ? 309  LYS B CA    1 
ATOM   6418 C C     . LYS B 1 309 ? -13.451 -69.294 4.675   1.00 34.34 ? 309  LYS B C     1 
ATOM   6419 O O     . LYS B 1 309 ? -12.380 -69.208 4.147   1.00 30.93 ? 309  LYS B O     1 
ATOM   6420 C CB    . LYS B 1 309 ? -14.067 -68.406 6.844   1.00 34.53 ? 309  LYS B CB    1 
ATOM   6421 C CG    . LYS B 1 309 ? -14.258 -67.231 7.763   1.00 38.41 ? 309  LYS B CG    1 
ATOM   6422 C CD    . LYS B 1 309 ? -13.392 -67.451 8.972   1.00 44.09 ? 309  LYS B CD    1 
ATOM   6423 C CE    . LYS B 1 309 ? -14.189 -67.397 10.239  1.00 57.41 ? 309  LYS B CE    1 
ATOM   6424 N NZ    . LYS B 1 309 ? -13.575 -68.349 11.197  1.00 61.87 ? 309  LYS B NZ    1 
ATOM   6425 N N     . LYS B 1 310 ? -14.141 -70.405 4.696   1.00 30.94 ? 310  LYS B N     1 
ATOM   6426 C CA    . LYS B 1 310 ? -13.568 -71.621 4.161   1.00 32.25 ? 310  LYS B CA    1 
ATOM   6427 C C     . LYS B 1 310 ? -13.468 -71.645 2.644   1.00 31.56 ? 310  LYS B C     1 
ATOM   6428 O O     . LYS B 1 310 ? -12.445 -71.985 2.107   1.00 31.59 ? 310  LYS B O     1 
ATOM   6429 C CB    . LYS B 1 310 ? -14.319 -72.821 4.728   1.00 34.82 ? 310  LYS B CB    1 
ATOM   6430 C CG    . LYS B 1 310 ? -13.664 -73.451 5.940   1.00 38.64 ? 310  LYS B CG    1 
ATOM   6431 C CD    . LYS B 1 310 ? -14.007 -72.701 7.211   1.00 43.91 ? 310  LYS B CD    1 
ATOM   6432 C CE    . LYS B 1 310 ? -13.108 -73.111 8.355   1.00 57.23 ? 310  LYS B CE    1 
ATOM   6433 N NZ    . LYS B 1 310 ? -13.124 -72.100 9.441   1.00 72.16 ? 310  LYS B NZ    1 
ATOM   6434 N N     . GLU B 1 311 ? -14.528 -71.268 1.971   1.00 30.58 ? 311  GLU B N     1 
ATOM   6435 C CA    . GLU B 1 311 ? -14.504 -71.230 0.532   1.00 34.72 ? 311  GLU B CA    1 
ATOM   6436 C C     . GLU B 1 311 ? -13.460 -70.271 -0.011  1.00 35.91 ? 311  GLU B C     1 
ATOM   6437 O O     . GLU B 1 311 ? -12.806 -70.572 -0.988  1.00 35.77 ? 311  GLU B O     1 
ATOM   6438 C CB    . GLU B 1 311 ? -15.880 -70.832 0.012   1.00 37.00 ? 311  GLU B CB    1 
ATOM   6439 C CG    . GLU B 1 311 ? -16.024 -70.731 -1.497  1.00 44.76 ? 311  GLU B CG    1 
ATOM   6440 C CD    . GLU B 1 311 ? -15.791 -72.040 -2.220  1.00 49.80 ? 311  GLU B CD    1 
ATOM   6441 O OE1   . GLU B 1 311 ? -16.092 -73.113 -1.662  1.00 56.00 ? 311  GLU B OE1   1 
ATOM   6442 O OE2   . GLU B 1 311 ? -15.310 -71.992 -3.366  1.00 60.13 ? 311  GLU B OE2   1 
ATOM   6443 N N     . LEU B 1 312 ? -13.280 -69.143 0.650   1.00 33.02 ? 312  LEU B N     1 
ATOM   6444 C CA    . LEU B 1 312 ? -12.375 -68.084 0.119   1.00 32.01 ? 312  LEU B CA    1 
ATOM   6445 C C     . LEU B 1 312 ? -11.014 -68.142 0.808   1.00 33.93 ? 312  LEU B C     1 
ATOM   6446 O O     . LEU B 1 312 ? -10.129 -67.421 0.339   1.00 31.03 ? 312  LEU B O     1 
ATOM   6447 C CB    . LEU B 1 312 ? -13.022 -66.713 0.320   1.00 32.87 ? 312  LEU B CB    1 
ATOM   6448 C CG    . LEU B 1 312 ? -14.349 -66.494 -0.384  1.00 31.61 ? 312  LEU B CG    1 
ATOM   6449 C CD1   . LEU B 1 312 ? -14.957 -65.173 0.009   1.00 33.27 ? 312  LEU B CD1   1 
ATOM   6450 C CD2   . LEU B 1 312 ? -14.199 -66.572 -1.897  1.00 34.18 ? 312  LEU B CD2   1 
ATOM   6451 N N     . GLY B 1 313 ? -10.836 -68.992 1.830   1.00 30.00 ? 313  GLY B N     1 
ATOM   6452 C CA    . GLY B 1 313 ? -9.566  -69.152 2.572   1.00 29.21 ? 313  GLY B CA    1 
ATOM   6453 C C     . GLY B 1 313 ? -9.209  -67.871 3.330   1.00 35.13 ? 313  GLY B C     1 
ATOM   6454 O O     . GLY B 1 313 ? -8.045  -67.414 3.278   1.00 33.49 ? 313  GLY B O     1 
ATOM   6455 N N     . LEU B 1 314 ? -10.191 -67.297 4.013   1.00 33.37 ? 314  LEU B N     1 
ATOM   6456 C CA    . LEU B 1 314 ? -10.106 -65.994 4.700   1.00 32.08 ? 314  LEU B CA    1 
ATOM   6457 C C     . LEU B 1 314 ? -10.375 -66.226 6.182   1.00 34.51 ? 314  LEU B C     1 
ATOM   6458 O O     . LEU B 1 314 ? -10.942 -67.298 6.534   1.00 29.61 ? 314  LEU B O     1 
ATOM   6459 C CB    . LEU B 1 314 ? -11.155 -65.074 4.086   1.00 33.12 ? 314  LEU B CB    1 
ATOM   6460 C CG    . LEU B 1 314 ? -10.671 -63.933 3.186   1.00 40.60 ? 314  LEU B CG    1 
ATOM   6461 C CD1   . LEU B 1 314 ? -9.307  -64.169 2.556   1.00 38.90 ? 314  LEU B CD1   1 
ATOM   6462 C CD2   . LEU B 1 314 ? -11.713 -63.619 2.122   1.00 36.48 ? 314  LEU B CD2   1 
ATOM   6463 N N     . GLY B 1 315 ? -9.933  -65.290 7.023   1.00 29.86 ? 315  GLY B N     1 
ATOM   6464 C CA    . GLY B 1 315 ? -10.213 -65.291 8.472   1.00 29.42 ? 315  GLY B CA    1 
ATOM   6465 C C     . GLY B 1 315 ? -11.447 -64.459 8.733   1.00 27.28 ? 315  GLY B C     1 
ATOM   6466 O O     . GLY B 1 315 ? -12.022 -63.905 7.754   1.00 27.67 ? 315  GLY B O     1 
ATOM   6467 N N     . TYR B 1 316 ? -11.888 -64.355 9.989   1.00 26.19 ? 316  TYR B N     1 
ATOM   6468 C CA    . TYR B 1 316 ? -12.944 -63.372 10.331  1.00 28.02 ? 316  TYR B CA    1 
ATOM   6469 C C     . TYR B 1 316 ? -12.329 -61.973 10.137  1.00 26.28 ? 316  TYR B C     1 
ATOM   6470 O O     . TYR B 1 316 ? -13.006 -61.062 9.635   1.00 27.01 ? 316  TYR B O     1 
ATOM   6471 C CB    . TYR B 1 316 ? -13.511 -63.535 11.748  1.00 28.14 ? 316  TYR B CB    1 
ATOM   6472 C CG    . TYR B 1 316 ? -14.655 -62.573 11.893  1.00 30.01 ? 316  TYR B CG    1 
ATOM   6473 C CD1   . TYR B 1 316 ? -14.423 -61.241 12.211  1.00 29.04 ? 316  TYR B CD1   1 
ATOM   6474 C CD2   . TYR B 1 316 ? -15.952 -62.951 11.573  1.00 27.78 ? 316  TYR B CD2   1 
ATOM   6475 C CE1   . TYR B 1 316 ? -15.448 -60.315 12.247  1.00 30.50 ? 316  TYR B CE1   1 
ATOM   6476 C CE2   . TYR B 1 316 ? -16.990 -62.039 11.607  1.00 30.59 ? 316  TYR B CE2   1 
ATOM   6477 C CZ    . TYR B 1 316 ? -16.731 -60.708 11.916  1.00 31.46 ? 316  TYR B CZ    1 
ATOM   6478 O OH    . TYR B 1 316 ? -17.713 -59.770 11.954  1.00 30.62 ? 316  TYR B OH    1 
ATOM   6479 N N     . TRP B 1 317 ? -11.075 -61.835 10.578  1.00 25.91 ? 317  TRP B N     1 
ATOM   6480 C CA    . TRP B 1 317 ? -10.232 -60.622 10.418  1.00 27.50 ? 317  TRP B CA    1 
ATOM   6481 C C     . TRP B 1 317 ? -9.076  -60.932 9.465   1.00 25.54 ? 317  TRP B C     1 
ATOM   6482 O O     . TRP B 1 317 ? -8.415  -61.951 9.643   1.00 28.14 ? 317  TRP B O     1 
ATOM   6483 C CB    . TRP B 1 317 ? -9.729  -60.132 11.784  1.00 26.15 ? 317  TRP B CB    1 
ATOM   6484 C CG    . TRP B 1 317 ? -10.823 -59.668 12.682  1.00 24.00 ? 317  TRP B CG    1 
ATOM   6485 C CD1   . TRP B 1 317 ? -11.212 -60.283 13.831  1.00 25.08 ? 317  TRP B CD1   1 
ATOM   6486 C CD2   . TRP B 1 317 ? -11.688 -58.529 12.526  1.00 25.31 ? 317  TRP B CD2   1 
ATOM   6487 N NE1   . TRP B 1 317 ? -12.250 -59.606 14.402  1.00 24.85 ? 317  TRP B NE1   1 
ATOM   6488 C CE2   . TRP B 1 317 ? -12.572 -58.529 13.632  1.00 26.28 ? 317  TRP B CE2   1 
ATOM   6489 C CE3   . TRP B 1 317 ? -11.836 -57.514 11.566  1.00 23.89 ? 317  TRP B CE3   1 
ATOM   6490 C CZ2   . TRP B 1 317 ? -13.578 -57.577 13.804  1.00 25.37 ? 317  TRP B CZ2   1 
ATOM   6491 C CZ3   . TRP B 1 317 ? -12.807 -56.563 11.750  1.00 24.65 ? 317  TRP B CZ3   1 
ATOM   6492 C CH2   . TRP B 1 317 ? -13.663 -56.581 12.856  1.00 25.43 ? 317  TRP B CH2   1 
ATOM   6493 N N     . ASN B 1 318 ? -8.878  -60.049 8.490   1.00 26.91 ? 318  ASN B N     1 
ATOM   6494 C CA    . ASN B 1 318 ? -7.844  -60.173 7.439   1.00 25.37 ? 318  ASN B CA    1 
ATOM   6495 C C     . ASN B 1 318 ? -6.961  -58.916 7.445   1.00 25.28 ? 318  ASN B C     1 
ATOM   6496 O O     . ASN B 1 318 ? -7.453  -57.838 7.092   1.00 24.71 ? 318  ASN B O     1 
ATOM   6497 C CB    . ASN B 1 318 ? -8.554  -60.465 6.133   1.00 29.03 ? 318  ASN B CB    1 
ATOM   6498 C CG    . ASN B 1 318 ? -9.462  -61.670 6.298   1.00 28.37 ? 318  ASN B CG    1 
ATOM   6499 O OD1   . ASN B 1 318 ? -8.972  -62.799 6.295   1.00 29.93 ? 318  ASN B OD1   1 
ATOM   6500 N ND2   . ASN B 1 318 ? -10.742 -61.415 6.526   1.00 30.03 ? 318  ASN B ND2   1 
ATOM   6501 N N     . PHE B 1 319 ? -5.710  -59.092 7.857   1.00 28.86 ? 319  PHE B N     1 
ATOM   6502 C CA    . PHE B 1 319 ? -4.701  -58.020 8.026   1.00 26.26 ? 319  PHE B CA    1 
ATOM   6503 C C     . PHE B 1 319 ? -3.928  -57.899 6.720   1.00 26.69 ? 319  PHE B C     1 
ATOM   6504 O O     . PHE B 1 319 ? -3.497  -58.939 6.214   1.00 28.09 ? 319  PHE B O     1 
ATOM   6505 C CB    . PHE B 1 319 ? -3.745  -58.346 9.165   1.00 24.34 ? 319  PHE B CB    1 
ATOM   6506 C CG    . PHE B 1 319 ? -2.745  -57.265 9.474   1.00 27.36 ? 319  PHE B CG    1 
ATOM   6507 C CD1   . PHE B 1 319 ? -1.584  -57.126 8.726   1.00 28.71 ? 319  PHE B CD1   1 
ATOM   6508 C CD2   . PHE B 1 319 ? -2.948  -56.401 10.531  1.00 31.00 ? 319  PHE B CD2   1 
ATOM   6509 C CE1   . PHE B 1 319 ? -0.658  -56.132 9.019   1.00 29.54 ? 319  PHE B CE1   1 
ATOM   6510 C CE2   . PHE B 1 319 ? -2.021  -55.415 10.832  1.00 30.37 ? 319  PHE B CE2   1 
ATOM   6511 C CZ    . PHE B 1 319 ? -0.893  -55.264 10.053  1.00 29.04 ? 319  PHE B CZ    1 
ATOM   6512 N N     . TYR B 1 320 ? -3.798  -56.687 6.178   1.00 26.24 ? 320  TYR B N     1 
ATOM   6513 C CA    . TYR B 1 320 ? -2.972  -56.428 4.972   1.00 26.30 ? 320  TYR B CA    1 
ATOM   6514 C C     . TYR B 1 320 ? -1.961  -55.353 5.313   1.00 28.72 ? 320  TYR B C     1 
ATOM   6515 O O     . TYR B 1 320 ? -2.355  -54.321 5.852   1.00 28.45 ? 320  TYR B O     1 
ATOM   6516 C CB    . TYR B 1 320 ? -3.822  -56.028 3.770   1.00 27.73 ? 320  TYR B CB    1 
ATOM   6517 C CG    . TYR B 1 320 ? -4.825  -57.093 3.412   1.00 27.74 ? 320  TYR B CG    1 
ATOM   6518 C CD1   . TYR B 1 320 ? -6.068  -57.138 4.029   1.00 29.13 ? 320  TYR B CD1   1 
ATOM   6519 C CD2   . TYR B 1 320 ? -4.515  -58.078 2.494   1.00 29.54 ? 320  TYR B CD2   1 
ATOM   6520 C CE1   . TYR B 1 320 ? -6.994  -58.122 3.721   1.00 28.88 ? 320  TYR B CE1   1 
ATOM   6521 C CE2   . TYR B 1 320 ? -5.430  -59.066 2.172   1.00 28.85 ? 320  TYR B CE2   1 
ATOM   6522 C CZ    . TYR B 1 320 ? -6.659  -59.103 2.802   1.00 30.76 ? 320  TYR B CZ    1 
ATOM   6523 O OH    . TYR B 1 320 ? -7.554  -60.088 2.512   1.00 28.32 ? 320  TYR B OH    1 
ATOM   6524 N N     . GLY B 1 321 ? -0.703  -55.633 4.999   1.00 31.10 ? 321  GLY B N     1 
ATOM   6525 C CA    . GLY B 1 321 ? 0.419   -54.699 5.182   1.00 30.40 ? 321  GLY B CA    1 
ATOM   6526 C C     . GLY B 1 321 ? 1.369   -54.836 4.028   1.00 32.56 ? 321  GLY B C     1 
ATOM   6527 O O     . GLY B 1 321 ? 1.319   -55.877 3.311   1.00 27.87 ? 321  GLY B O     1 
ATOM   6528 N N     . THR B 1 322 ? 2.206   -53.824 3.851   1.00 32.18 ? 322  THR B N     1 
ATOM   6529 C CA    . THR B 1 322 ? 3.257   -53.814 2.826   1.00 28.14 ? 322  THR B CA    1 
ATOM   6530 C C     . THR B 1 322 ? 4.557   -53.455 3.517   1.00 30.66 ? 322  THR B C     1 
ATOM   6531 O O     . THR B 1 322 ? 4.541   -52.651 4.506   1.00 28.58 ? 322  THR B O     1 
ATOM   6532 C CB    . THR B 1 322 ? 2.852   -52.910 1.659   1.00 29.99 ? 322  THR B CB    1 
ATOM   6533 O OG1   . THR B 1 322 ? 1.710   -53.491 1.040   1.00 28.17 ? 322  THR B OG1   1 
ATOM   6534 C CG2   . THR B 1 322 ? 3.963   -52.741 0.641   1.00 31.21 ? 322  THR B CG2   1 
ATOM   6535 N N     . LEU B 1 323 ? 5.633   -54.059 3.023   1.00 30.99 ? 323  LEU B N     1 
ATOM   6536 C CA    . LEU B 1 323 ? 7.008   -53.797 3.463   1.00 30.62 ? 323  LEU B CA    1 
ATOM   6537 C C     . LEU B 1 323 ? 7.771   -53.241 2.269   1.00 32.13 ? 323  LEU B C     1 
ATOM   6538 O O     . LEU B 1 323 ? 7.495   -53.663 1.135   1.00 32.86 ? 323  LEU B O     1 
ATOM   6539 C CB    . LEU B 1 323 ? 7.628   -55.096 3.964   1.00 31.65 ? 323  LEU B CB    1 
ATOM   6540 C CG    . LEU B 1 323 ? 6.943   -55.696 5.184   1.00 32.32 ? 323  LEU B CG    1 
ATOM   6541 C CD1   . LEU B 1 323 ? 7.528   -57.070 5.514   1.00 32.66 ? 323  LEU B CD1   1 
ATOM   6542 C CD2   . LEU B 1 323 ? 7.047   -54.759 6.372   1.00 30.82 ? 323  LEU B CD2   1 
ATOM   6543 N N     . TYR B 1 324 ? 8.693   -52.331 2.553   1.00 30.42 ? 324  TYR B N     1 
ATOM   6544 C CA    . TYR B 1 324 ? 9.507   -51.613 1.547   1.00 31.84 ? 324  TYR B CA    1 
ATOM   6545 C C     . TYR B 1 324 ? 10.985  -51.729 1.923   1.00 31.39 ? 324  TYR B C     1 
ATOM   6546 O O     . TYR B 1 324 ? 11.334  -51.686 3.125   1.00 32.53 ? 324  TYR B O     1 
ATOM   6547 C CB    . TYR B 1 324 ? 9.092   -50.143 1.489   1.00 31.87 ? 324  TYR B CB    1 
ATOM   6548 C CG    . TYR B 1 324 ? 7.613   -49.868 1.374   1.00 29.03 ? 324  TYR B CG    1 
ATOM   6549 C CD1   . TYR B 1 324 ? 6.931   -50.006 0.175   1.00 27.32 ? 324  TYR B CD1   1 
ATOM   6550 C CD2   . TYR B 1 324 ? 6.886   -49.439 2.471   1.00 28.38 ? 324  TYR B CD2   1 
ATOM   6551 C CE1   . TYR B 1 324 ? 5.575   -49.731 0.064   1.00 26.91 ? 324  TYR B CE1   1 
ATOM   6552 C CE2   . TYR B 1 324 ? 5.522   -49.187 2.387   1.00 27.94 ? 324  TYR B CE2   1 
ATOM   6553 C CZ    . TYR B 1 324 ? 4.865   -49.302 1.180   1.00 25.38 ? 324  TYR B CZ    1 
ATOM   6554 O OH    . TYR B 1 324 ? 3.527   -49.025 1.097   1.00 30.01 ? 324  TYR B OH    1 
ATOM   6555 N N     . GLY B 1 325 ? 11.840  -51.762 0.906   1.00 33.18 ? 325  GLY B N     1 
ATOM   6556 C CA    . GLY B 1 325 ? 13.296  -51.631 1.058   1.00 33.61 ? 325  GLY B CA    1 
ATOM   6557 C C     . GLY B 1 325 ? 13.997  -52.712 0.253   1.00 37.33 ? 325  GLY B C     1 
ATOM   6558 O O     . GLY B 1 325 ? 13.358  -53.407 -0.529  1.00 36.44 ? 325  GLY B O     1 
ATOM   6559 N N     . PRO B 1 326 ? 15.311  -52.928 0.453   1.00 40.69 ? 326  PRO B N     1 
ATOM   6560 C CA    . PRO B 1 326 ? 15.981  -54.066 -0.176  1.00 43.09 ? 326  PRO B CA    1 
ATOM   6561 C C     . PRO B 1 326 ? 15.400  -55.361 0.389   1.00 39.77 ? 326  PRO B C     1 
ATOM   6562 O O     . PRO B 1 326 ? 14.943  -55.405 1.524   1.00 34.03 ? 326  PRO B O     1 
ATOM   6563 C CB    . PRO B 1 326 ? 17.481  -53.874 0.110   1.00 42.30 ? 326  PRO B CB    1 
ATOM   6564 C CG    . PRO B 1 326 ? 17.563  -52.793 1.191   1.00 44.33 ? 326  PRO B CG    1 
ATOM   6565 C CD    . PRO B 1 326 ? 16.207  -52.113 1.287   1.00 42.39 ? 326  PRO B CD    1 
ATOM   6566 N N     . PRO B 1 327 ? 15.371  -56.456 -0.400  1.00 42.18 ? 327  PRO B N     1 
ATOM   6567 C CA    . PRO B 1 327 ? 14.829  -57.733 0.069   1.00 39.96 ? 327  PRO B CA    1 
ATOM   6568 C C     . PRO B 1 327 ? 15.314  -58.221 1.441   1.00 40.86 ? 327  PRO B C     1 
ATOM   6569 O O     . PRO B 1 327 ? 14.575  -58.935 2.070   1.00 42.65 ? 327  PRO B O     1 
ATOM   6570 C CB    . PRO B 1 327 ? 15.271  -58.699 -1.043  1.00 41.95 ? 327  PRO B CB    1 
ATOM   6571 C CG    . PRO B 1 327 ? 15.202  -57.838 -2.284  1.00 39.61 ? 327  PRO B CG    1 
ATOM   6572 C CD    . PRO B 1 327 ? 15.774  -56.513 -1.819  1.00 41.09 ? 327  PRO B CD    1 
ATOM   6573 N N     . GLN B 1 328 ? 16.504  -57.836 1.899   1.00 41.46 ? 328  GLN B N     1 
ATOM   6574 C CA    . GLN B 1 328 ? 17.042  -58.263 3.225   1.00 40.99 ? 328  GLN B CA    1 
ATOM   6575 C C     . GLN B 1 328 ? 16.270  -57.552 4.337   1.00 38.08 ? 328  GLN B C     1 
ATOM   6576 O O     . GLN B 1 328 ? 16.028  -58.166 5.390   1.00 35.62 ? 328  GLN B O     1 
ATOM   6577 C CB    . GLN B 1 328 ? 18.526  -57.928 3.369   1.00 49.06 ? 328  GLN B CB    1 
ATOM   6578 C CG    . GLN B 1 328 ? 19.397  -58.605 2.316   1.00 61.12 ? 328  GLN B CG    1 
ATOM   6579 C CD    . GLN B 1 328 ? 20.381  -57.648 1.682   1.00 68.33 ? 328  GLN B CD    1 
ATOM   6580 O OE1   . GLN B 1 328 ? 21.187  -57.016 2.363   1.00 77.69 ? 328  GLN B OE1   1 
ATOM   6581 N NE2   . GLN B 1 328 ? 20.314  -57.528 0.364   1.00 72.98 ? 328  GLN B NE2   1 
ATOM   6582 N N     . LEU B 1 329 ? 15.964  -56.268 4.149   1.00 36.05 ? 329  LEU B N     1 
ATOM   6583 C CA    . LEU B 1 329 ? 15.145  -55.501 5.118   1.00 36.07 ? 329  LEU B CA    1 
ATOM   6584 C C     . LEU B 1 329 ? 13.723  -56.098 5.137   1.00 30.14 ? 329  LEU B C     1 
ATOM   6585 O O     . LEU B 1 329 ? 13.203  -56.338 6.246   1.00 32.58 ? 329  LEU B O     1 
ATOM   6586 C CB    . LEU B 1 329 ? 15.169  -54.011 4.748   1.00 33.68 ? 329  LEU B CB    1 
ATOM   6587 C CG    . LEU B 1 329 ? 14.453  -53.093 5.743   1.00 35.48 ? 329  LEU B CG    1 
ATOM   6588 C CD1   . LEU B 1 329 ? 15.107  -53.160 7.119   1.00 35.28 ? 329  LEU B CD1   1 
ATOM   6589 C CD2   . LEU B 1 329 ? 14.400  -51.651 5.262   1.00 35.09 ? 329  LEU B CD2   1 
ATOM   6590 N N     . ILE B 1 330 ? 13.139  -56.364 3.972   1.00 30.78 ? 330  ILE B N     1 
ATOM   6591 C CA    . ILE B 1 330 ? 11.764  -56.936 3.853   1.00 34.95 ? 330  ILE B CA    1 
ATOM   6592 C C     . ILE B 1 330 ? 11.723  -58.257 4.644   1.00 34.63 ? 330  ILE B C     1 
ATOM   6593 O O     . ILE B 1 330 ? 10.877  -58.380 5.543   1.00 34.51 ? 330  ILE B O     1 
ATOM   6594 C CB    . ILE B 1 330 ? 11.330  -57.080 2.381   1.00 34.12 ? 330  ILE B CB    1 
ATOM   6595 C CG1   . ILE B 1 330 ? 11.087  -55.706 1.740   1.00 35.41 ? 330  ILE B CG1   1 
ATOM   6596 C CG2   . ILE B 1 330 ? 10.109  -57.991 2.270   1.00 33.62 ? 330  ILE B CG2   1 
ATOM   6597 C CD1   . ILE B 1 330 ? 10.909  -55.716 0.236   1.00 35.96 ? 330  ILE B CD1   1 
ATOM   6598 N N     . GLU B 1 331 ? 12.630  -59.192 4.361   1.00 39.70 ? 331  GLU B N     1 
ATOM   6599 C CA    . GLU B 1 331 ? 12.712  -60.513 5.051   1.00 42.58 ? 331  GLU B CA    1 
ATOM   6600 C C     . GLU B 1 331 ? 12.778  -60.292 6.561   1.00 41.29 ? 331  GLU B C     1 
ATOM   6601 O O     . GLU B 1 331 ? 12.100  -61.027 7.307   1.00 38.16 ? 331  GLU B O     1 
ATOM   6602 C CB    . GLU B 1 331 ? 13.949  -61.311 4.628   1.00 49.45 ? 331  GLU B CB    1 
ATOM   6603 C CG    . GLU B 1 331 ? 13.900  -61.794 3.185   1.00 62.32 ? 331  GLU B CG    1 
ATOM   6604 C CD    . GLU B 1 331 ? 15.255  -62.180 2.598   1.00 76.44 ? 331  GLU B CD    1 
ATOM   6605 O OE1   . GLU B 1 331 ? 16.124  -62.660 3.375   1.00 81.05 ? 331  GLU B OE1   1 
ATOM   6606 O OE2   . GLU B 1 331 ? 15.440  -62.026 1.364   1.00 81.48 ? 331  GLU B OE2   1 
ATOM   6607 N N     . MET B 1 332 ? 13.592  -59.333 6.996   1.00 37.51 ? 332  MET B N     1 
ATOM   6608 C CA    . MET B 1 332 ? 13.868  -59.103 8.432   1.00 39.00 ? 332  MET B CA    1 
ATOM   6609 C C     . MET B 1 332 ? 12.575  -58.586 9.068   1.00 37.04 ? 332  MET B C     1 
ATOM   6610 O O     . MET B 1 332 ? 12.127  -59.174 10.039  1.00 34.00 ? 332  MET B O     1 
ATOM   6611 C CB    . MET B 1 332 ? 15.010  -58.105 8.635   1.00 45.35 ? 332  MET B CB    1 
ATOM   6612 C CG    . MET B 1 332 ? 15.428  -57.970 10.095  1.00 52.54 ? 332  MET B CG    1 
ATOM   6613 S SD    . MET B 1 332 ? 16.600  -56.617 10.412  1.00 64.46 ? 332  MET B SD    1 
ATOM   6614 C CE    . MET B 1 332 ? 17.866  -56.950 9.186   1.00 62.70 ? 332  MET B CE    1 
ATOM   6615 N N     . ASN B 1 333 ? 11.978  -57.553 8.489   1.00 33.06 ? 333  ASN B N     1 
ATOM   6616 C CA    . ASN B 1 333 ? 10.724  -56.952 9.013   1.00 34.97 ? 333  ASN B CA    1 
ATOM   6617 C C     . ASN B 1 333 ? 9.592   -57.985 8.991   1.00 31.26 ? 333  ASN B C     1 
ATOM   6618 O O     . ASN B 1 333 ? 8.856   -58.057 9.991   1.00 31.41 ? 333  ASN B O     1 
ATOM   6619 C CB    . ASN B 1 333 ? 10.380  -55.664 8.265   1.00 32.70 ? 333  ASN B CB    1 
ATOM   6620 C CG    . ASN B 1 333 ? 11.215  -54.503 8.774   1.00 34.77 ? 333  ASN B CG    1 
ATOM   6621 O OD1   . ASN B 1 333 ? 11.596  -54.476 9.940   1.00 32.62 ? 333  ASN B OD1   1 
ATOM   6622 N ND2   . ASN B 1 333 ? 11.491  -53.545 7.914   1.00 32.47 ? 333  ASN B ND2   1 
ATOM   6623 N N     . TYR B 1 334 ? 9.454   -58.751 7.901   1.00 34.19 ? 334  TYR B N     1 
ATOM   6624 C CA    . TYR B 1 334 ? 8.416   -59.815 7.768   1.00 34.15 ? 334  TYR B CA    1 
ATOM   6625 C C     . TYR B 1 334 ? 8.611   -60.848 8.877   1.00 34.47 ? 334  TYR B C     1 
ATOM   6626 O O     . TYR B 1 334 ? 7.612   -61.300 9.473   1.00 30.73 ? 334  TYR B O     1 
ATOM   6627 C CB    . TYR B 1 334 ? 8.456   -60.494 6.396   1.00 35.11 ? 334  TYR B CB    1 
ATOM   6628 C CG    . TYR B 1 334 ? 7.229   -61.319 6.072   1.00 34.88 ? 334  TYR B CG    1 
ATOM   6629 C CD1   . TYR B 1 334 ? 5.941   -60.857 6.354   1.00 34.76 ? 334  TYR B CD1   1 
ATOM   6630 C CD2   . TYR B 1 334 ? 7.341   -62.562 5.468   1.00 36.91 ? 334  TYR B CD2   1 
ATOM   6631 C CE1   . TYR B 1 334 ? 4.810   -61.603 6.050   1.00 33.31 ? 334  TYR B CE1   1 
ATOM   6632 C CE2   . TYR B 1 334 ? 6.215   -63.322 5.157   1.00 36.51 ? 334  TYR B CE2   1 
ATOM   6633 C CZ    . TYR B 1 334 ? 4.947   -62.842 5.447   1.00 35.64 ? 334  TYR B CZ    1 
ATOM   6634 O OH    . TYR B 1 334 ? 3.828   -63.570 5.145   1.00 33.56 ? 334  TYR B OH    1 
ATOM   6635 N N     . GLY B 1 335 ? 9.870   -61.203 9.150   1.00 34.57 ? 335  GLY B N     1 
ATOM   6636 C CA    . GLY B 1 335 ? 10.240  -62.082 10.277  1.00 36.32 ? 335  GLY B CA    1 
ATOM   6637 C C     . GLY B 1 335 ? 9.682   -61.576 11.600  1.00 37.81 ? 335  GLY B C     1 
ATOM   6638 O O     . GLY B 1 335 ? 9.075   -62.380 12.359  1.00 35.83 ? 335  GLY B O     1 
ATOM   6639 N N     . ILE B 1 336 ? 9.871   -60.285 11.899  1.00 36.46 ? 336  ILE B N     1 
ATOM   6640 C CA    . ILE B 1 336 ? 9.378   -59.670 13.163  1.00 32.40 ? 336  ILE B CA    1 
ATOM   6641 C C     . ILE B 1 336 ? 7.841   -59.738 13.167  1.00 30.65 ? 336  ILE B C     1 
ATOM   6642 O O     . ILE B 1 336 ? 7.266   -60.049 14.228  1.00 29.12 ? 336  ILE B O     1 
ATOM   6643 C CB    . ILE B 1 336 ? 9.902   -58.229 13.329  1.00 36.07 ? 336  ILE B CB    1 
ATOM   6644 C CG1   . ILE B 1 336 ? 11.432  -58.173 13.436  1.00 37.90 ? 336  ILE B CG1   1 
ATOM   6645 C CG2   . ILE B 1 336 ? 9.235   -57.556 14.513  1.00 34.67 ? 336  ILE B CG2   1 
ATOM   6646 C CD1   . ILE B 1 336 ? 12.012  -56.785 13.177  1.00 37.50 ? 336  ILE B CD1   1 
ATOM   6647 N N     . ILE B 1 337 ? 7.195   -59.392 12.049  1.00 31.33 ? 337  ILE B N     1 
ATOM   6648 C CA    . ILE B 1 337 ? 5.710   -59.364 11.924  1.00 32.63 ? 337  ILE B CA    1 
ATOM   6649 C C     . ILE B 1 337 ? 5.170   -60.777 12.180  1.00 31.88 ? 337  ILE B C     1 
ATOM   6650 O O     . ILE B 1 337 ? 4.230   -60.907 12.952  1.00 30.64 ? 337  ILE B O     1 
ATOM   6651 C CB    . ILE B 1 337 ? 5.283   -58.847 10.530  1.00 33.76 ? 337  ILE B CB    1 
ATOM   6652 C CG1   . ILE B 1 337 ? 5.761   -57.421 10.255  1.00 37.64 ? 337  ILE B CG1   1 
ATOM   6653 C CG2   . ILE B 1 337 ? 3.784   -58.955 10.349  1.00 33.54 ? 337  ILE B CG2   1 
ATOM   6654 C CD1   . ILE B 1 337 ? 5.593   -56.519 11.404  1.00 41.28 ? 337  ILE B CD1   1 
ATOM   6655 N N     . LYS B 1 338 ? 5.715   -61.785 11.497  1.00 33.02 ? 338  LYS B N     1 
ATOM   6656 C CA    . LYS B 1 338 ? 5.271   -63.202 11.631  1.00 35.94 ? 338  LYS B CA    1 
ATOM   6657 C C     . LYS B 1 338 ? 5.436   -63.649 13.082  1.00 35.34 ? 338  LYS B C     1 
ATOM   6658 O O     . LYS B 1 338 ? 4.494   -64.239 13.632  1.00 30.92 ? 338  LYS B O     1 
ATOM   6659 C CB    . LYS B 1 338 ? 6.042   -64.105 10.669  1.00 35.93 ? 338  LYS B CB    1 
ATOM   6660 C CG    . LYS B 1 338 ? 5.571   -64.030 9.227   1.00 38.15 ? 338  LYS B CG    1 
ATOM   6661 C CD    . LYS B 1 338 ? 6.198   -65.085 8.357   1.00 41.29 ? 338  LYS B CD    1 
ATOM   6662 C CE    . LYS B 1 338 ? 7.709   -65.023 8.340   1.00 45.89 ? 338  LYS B CE    1 
ATOM   6663 N NZ    . LYS B 1 338 ? 8.255   -65.876 7.260   1.00 51.35 ? 338  LYS B NZ    1 
ATOM   6664 N N     . ASP B 1 339 ? 6.570   -63.336 13.705  1.00 36.73 ? 339  ASP B N     1 
ATOM   6665 C CA    . ASP B 1 339 ? 6.841   -63.720 15.113  1.00 36.85 ? 339  ASP B CA    1 
ATOM   6666 C C     . ASP B 1 339 ? 5.780   -63.091 16.032  1.00 38.83 ? 339  ASP B C     1 
ATOM   6667 O O     . ASP B 1 339 ? 5.266   -63.807 16.906  1.00 33.58 ? 339  ASP B O     1 
ATOM   6668 C CB    . ASP B 1 339 ? 8.248   -63.303 15.544  1.00 45.68 ? 339  ASP B CB    1 
ATOM   6669 C CG    . ASP B 1 339 ? 8.497   -63.509 17.024  1.00 54.94 ? 339  ASP B CG    1 
ATOM   6670 O OD1   . ASP B 1 339 ? 8.707   -64.674 17.425  1.00 66.20 ? 339  ASP B OD1   1 
ATOM   6671 O OD2   . ASP B 1 339 ? 8.450   -62.506 17.769  1.00 60.14 ? 339  ASP B OD2   1 
ATOM   6672 N N     . ALA B 1 340 ? 5.479   -61.795 15.852  1.00 32.58 ? 340  ALA B N     1 
ATOM   6673 C CA    . ALA B 1 340 ? 4.549   -61.024 16.708  1.00 31.69 ? 340  ALA B CA    1 
ATOM   6674 C C     . ALA B 1 340 ? 3.122   -61.562 16.520  1.00 28.15 ? 340  ALA B C     1 
ATOM   6675 O O     . ALA B 1 340 ? 2.517   -61.970 17.508  1.00 31.84 ? 340  ALA B O     1 
ATOM   6676 C CB    . ALA B 1 340 ? 4.652   -59.539 16.401  1.00 29.93 ? 340  ALA B CB    1 
ATOM   6677 N N     . PHE B 1 341 ? 2.579   -61.550 15.304  1.00 31.01 ? 341  PHE B N     1 
ATOM   6678 C CA    . PHE B 1 341 ? 1.155   -61.924 15.072  1.00 33.10 ? 341  PHE B CA    1 
ATOM   6679 C C     . PHE B 1 341 ? 0.957   -63.452 15.144  1.00 33.36 ? 341  PHE B C     1 
ATOM   6680 O O     . PHE B 1 341 ? -0.179  -63.863 15.427  1.00 33.57 ? 341  PHE B O     1 
ATOM   6681 C CB    . PHE B 1 341 ? 0.641   -61.372 13.748  1.00 31.12 ? 341  PHE B CB    1 
ATOM   6682 C CG    . PHE B 1 341 ? 0.417   -59.885 13.761  1.00 33.27 ? 341  PHE B CG    1 
ATOM   6683 C CD1   . PHE B 1 341 ? -0.675  -59.341 14.421  1.00 31.79 ? 341  PHE B CD1   1 
ATOM   6684 C CD2   . PHE B 1 341 ? 1.302   -59.028 13.129  1.00 32.42 ? 341  PHE B CD2   1 
ATOM   6685 C CE1   . PHE B 1 341 ? -0.901  -57.975 14.425  1.00 31.07 ? 341  PHE B CE1   1 
ATOM   6686 C CE2   . PHE B 1 341 ? 1.084   -57.663 13.145  1.00 32.80 ? 341  PHE B CE2   1 
ATOM   6687 C CZ    . PHE B 1 341 ? -0.021  -57.141 13.784  1.00 34.22 ? 341  PHE B CZ    1 
ATOM   6688 N N     . GLY B 1 342 ? 2.012   -64.242 14.915  1.00 38.88 ? 342  GLY B N     1 
ATOM   6689 C CA    . GLY B 1 342 ? 2.041   -65.715 15.079  1.00 34.84 ? 342  GLY B CA    1 
ATOM   6690 C C     . GLY B 1 342 ? 1.754   -66.142 16.511  1.00 39.17 ? 342  GLY B C     1 
ATOM   6691 O O     . GLY B 1 342 ? 1.399   -67.317 16.700  1.00 36.63 ? 342  GLY B O     1 
ATOM   6692 N N     . GLN B 1 343 ? 1.869   -65.238 17.490  1.00 35.90 ? 343  GLN B N     1 
ATOM   6693 C CA    . GLN B 1 343 ? 1.484   -65.490 18.906  1.00 38.76 ? 343  GLN B CA    1 
ATOM   6694 C C     . GLN B 1 343 ? -0.034  -65.703 18.993  1.00 37.99 ? 343  GLN B C     1 
ATOM   6695 O O     . GLN B 1 343 ? -0.507  -66.183 20.031  1.00 34.81 ? 343  GLN B O     1 
ATOM   6696 C CB    . GLN B 1 343 ? 1.852   -64.326 19.828  1.00 40.24 ? 343  GLN B CB    1 
ATOM   6697 C CG    . GLN B 1 343 ? 3.320   -63.923 19.842  1.00 46.15 ? 343  GLN B CG    1 
ATOM   6698 C CD    . GLN B 1 343 ? 3.521   -62.558 20.476  1.00 58.27 ? 343  GLN B CD    1 
ATOM   6699 O OE1   . GLN B 1 343 ? 3.044   -61.510 19.992  1.00 50.28 ? 343  GLN B OE1   1 
ATOM   6700 N NE2   . GLN B 1 343 ? 4.229   -62.561 21.600  1.00 62.56 ? 343  GLN B NE2   1 
ATOM   6701 N N     . ILE B 1 344 ? -0.796  -65.301 17.969  1.00 35.81 ? 344  ILE B N     1 
ATOM   6702 C CA    . ILE B 1 344 ? -2.264  -65.532 17.928  1.00 35.55 ? 344  ILE B CA    1 
ATOM   6703 C C     . ILE B 1 344 ? -2.501  -66.904 17.292  1.00 34.52 ? 344  ILE B C     1 
ATOM   6704 O O     . ILE B 1 344 ? -2.222  -67.110 16.115  1.00 33.64 ? 344  ILE B O     1 
ATOM   6705 C CB    . ILE B 1 344 ? -3.011  -64.381 17.224  1.00 32.85 ? 344  ILE B CB    1 
ATOM   6706 C CG1   . ILE B 1 344 ? -2.741  -63.036 17.907  1.00 35.19 ? 344  ILE B CG1   1 
ATOM   6707 C CG2   . ILE B 1 344 ? -4.503  -64.678 17.154  1.00 32.93 ? 344  ILE B CG2   1 
ATOM   6708 C CD1   . ILE B 1 344 ? -3.409  -61.843 17.238  1.00 35.60 ? 344  ILE B CD1   1 
ATOM   6709 N N     . PRO B 1 345 ? -3.030  -67.880 18.059  1.00 35.38 ? 345  PRO B N     1 
ATOM   6710 C CA    . PRO B 1 345 ? -3.384  -69.189 17.503  1.00 35.59 ? 345  PRO B CA    1 
ATOM   6711 C C     . PRO B 1 345 ? -4.317  -69.046 16.294  1.00 32.95 ? 345  PRO B C     1 
ATOM   6712 O O     . PRO B 1 345 ? -5.243  -68.260 16.356  1.00 31.21 ? 345  PRO B O     1 
ATOM   6713 C CB    . PRO B 1 345 ? -4.118  -69.906 18.652  1.00 33.54 ? 345  PRO B CB    1 
ATOM   6714 C CG    . PRO B 1 345 ? -3.648  -69.203 19.918  1.00 34.20 ? 345  PRO B CG    1 
ATOM   6715 C CD    . PRO B 1 345 ? -3.351  -67.776 19.497  1.00 35.87 ? 345  PRO B CD    1 
ATOM   6716 N N     . GLY B 1 346 ? -4.038  -69.784 15.227  1.00 31.47 ? 346  GLY B N     1 
ATOM   6717 C CA    . GLY B 1 346 ? -4.880  -69.839 14.022  1.00 34.89 ? 346  GLY B CA    1 
ATOM   6718 C C     . GLY B 1 346 ? -4.452  -68.805 13.002  1.00 35.09 ? 346  GLY B C     1 
ATOM   6719 O O     . GLY B 1 346 ? -5.044  -68.780 11.933  1.00 36.18 ? 346  GLY B O     1 
ATOM   6720 N N     . SER B 1 347 ? -3.461  -67.960 13.316  1.00 34.56 ? 347  SER B N     1 
ATOM   6721 C CA    . SER B 1 347 ? -2.982  -66.922 12.363  1.00 31.29 ? 347  SER B CA    1 
ATOM   6722 C C     . SER B 1 347 ? -2.283  -67.623 11.205  1.00 31.33 ? 347  SER B C     1 
ATOM   6723 O O     . SER B 1 347 ? -1.515  -68.549 11.489  1.00 28.31 ? 347  SER B O     1 
ATOM   6724 C CB    . SER B 1 347 ? -2.083  -65.883 13.001  1.00 29.93 ? 347  SER B CB    1 
ATOM   6725 O OG    . SER B 1 347 ? -1.024  -66.472 13.719  1.00 30.73 ? 347  SER B OG    1 
ATOM   6726 N N     . ARG B 1 348 ? -2.553  -67.195 9.963   1.00 33.12 ? 348  ARG B N     1 
ATOM   6727 C CA    . ARG B 1 348 ? -1.892  -67.728 8.745   1.00 37.02 ? 348  ARG B CA    1 
ATOM   6728 C C     . ARG B 1 348 ? -1.410  -66.555 7.881   1.00 35.78 ? 348  ARG B C     1 
ATOM   6729 O O     . ARG B 1 348 ? -2.173  -65.576 7.703   1.00 35.70 ? 348  ARG B O     1 
ATOM   6730 C CB    . ARG B 1 348 ? -2.841  -68.680 7.999   1.00 39.60 ? 348  ARG B CB    1 
ATOM   6731 C CG    . ARG B 1 348 ? -3.305  -69.851 8.860   1.00 45.55 ? 348  ARG B CG    1 
ATOM   6732 C CD    . ARG B 1 348 ? -3.938  -71.029 8.145   1.00 55.63 ? 348  ARG B CD    1 
ATOM   6733 N NE    . ARG B 1 348 ? -5.130  -70.627 7.405   1.00 68.03 ? 348  ARG B NE    1 
ATOM   6734 C CZ    . ARG B 1 348 ? -6.013  -71.470 6.850   1.00 69.00 ? 348  ARG B CZ    1 
ATOM   6735 N NH1   . ARG B 1 348 ? -5.860  -72.783 6.966   1.00 66.63 ? 348  ARG B NH1   1 
ATOM   6736 N NH2   . ARG B 1 348 ? -7.054  -70.988 6.187   1.00 64.75 ? 348  ARG B NH2   1 
ATOM   6737 N N     . PHE B 1 349 ? -0.216  -66.702 7.307   1.00 36.52 ? 349  PHE B N     1 
ATOM   6738 C CA    . PHE B 1 349 ? 0.535   -65.647 6.588   1.00 35.07 ? 349  PHE B CA    1 
ATOM   6739 C C     . PHE B 1 349 ? 0.673   -66.042 5.125   1.00 35.96 ? 349  PHE B C     1 
ATOM   6740 O O     . PHE B 1 349 ? 1.108   -67.162 4.838   1.00 33.10 ? 349  PHE B O     1 
ATOM   6741 C CB    . PHE B 1 349 ? 1.902   -65.464 7.224   1.00 34.17 ? 349  PHE B CB    1 
ATOM   6742 C CG    . PHE B 1 349 ? 1.823   -65.020 8.654   1.00 35.58 ? 349  PHE B CG    1 
ATOM   6743 C CD1   . PHE B 1 349 ? 1.580   -65.933 9.663   1.00 37.40 ? 349  PHE B CD1   1 
ATOM   6744 C CD2   . PHE B 1 349 ? 1.943   -63.685 8.984   1.00 36.47 ? 349  PHE B CD2   1 
ATOM   6745 C CE1   . PHE B 1 349 ? 1.480   -65.519 10.981  1.00 39.37 ? 349  PHE B CE1   1 
ATOM   6746 C CE2   . PHE B 1 349 ? 1.845   -63.271 10.304  1.00 34.33 ? 349  PHE B CE2   1 
ATOM   6747 C CZ    . PHE B 1 349 ? 1.606   -64.187 11.298  1.00 36.94 ? 349  PHE B CZ    1 
ATOM   6748 N N     . GLN B 1 350 ? 0.285   -65.144 4.225   1.00 37.41 ? 350  GLN B N     1 
ATOM   6749 C CA    . GLN B 1 350 ? 0.458   -65.338 2.764   1.00 39.88 ? 350  GLN B CA    1 
ATOM   6750 C C     . GLN B 1 350 ? 0.981   -64.021 2.171   1.00 37.53 ? 350  GLN B C     1 
ATOM   6751 O O     . GLN B 1 350 ? 0.505   -62.961 2.541   1.00 33.80 ? 350  GLN B O     1 
ATOM   6752 C CB    . GLN B 1 350 ? -0.842  -65.840 2.122   1.00 43.17 ? 350  GLN B CB    1 
ATOM   6753 C CG    . GLN B 1 350 ? -1.476  -67.040 2.829   1.00 49.62 ? 350  GLN B CG    1 
ATOM   6754 C CD    . GLN B 1 350 ? -2.530  -66.723 3.885   1.00 62.30 ? 350  GLN B CD    1 
ATOM   6755 O OE1   . GLN B 1 350 ? -2.701  -65.575 4.344   1.00 44.58 ? 350  GLN B OE1   1 
ATOM   6756 N NE2   . GLN B 1 350 ? -3.267  -67.762 4.298   1.00 55.01 ? 350  GLN B NE2   1 
ATOM   6757 N N     . THR B 1 351 ? 1.974   -64.139 1.307   1.00 34.39 ? 351  THR B N     1 
ATOM   6758 C CA    . THR B 1 351 ? 2.662   -63.068 0.565   1.00 35.46 ? 351  THR B CA    1 
ATOM   6759 C C     . THR B 1 351 ? 1.919   -62.871 -0.756  1.00 35.89 ? 351  THR B C     1 
ATOM   6760 O O     . THR B 1 351 ? 1.251   -63.816 -1.198  1.00 36.61 ? 351  THR B O     1 
ATOM   6761 C CB    . THR B 1 351 ? 4.123   -63.521 0.467   1.00 40.19 ? 351  THR B CB    1 
ATOM   6762 O OG1   . THR B 1 351 ? 4.790   -62.982 1.601   1.00 41.23 ? 351  THR B OG1   1 
ATOM   6763 C CG2   . THR B 1 351 ? 4.827   -63.147 -0.803  1.00 41.97 ? 351  THR B CG2   1 
ATOM   6764 N N     . HIS B 1 352 ? 2.058   -61.707 -1.397  1.00 34.32 ? 352  HIS B N     1 
ATOM   6765 C CA    . HIS B 1 352 ? 1.472   -61.430 -2.736  1.00 32.36 ? 352  HIS B CA    1 
ATOM   6766 C C     . HIS B 1 352 ? 2.062   -62.367 -3.817  1.00 33.76 ? 352  HIS B C     1 
ATOM   6767 O O     . HIS B 1 352 ? 1.442   -62.488 -4.888  1.00 34.84 ? 352  HIS B O     1 
ATOM   6768 C CB    . HIS B 1 352 ? 1.690   -59.964 -3.114  1.00 31.99 ? 352  HIS B CB    1 
ATOM   6769 C CG    . HIS B 1 352 ? 3.061   -59.667 -3.622  1.00 29.76 ? 352  HIS B CG    1 
ATOM   6770 N ND1   . HIS B 1 352 ? 4.111   -59.359 -2.783  1.00 31.14 ? 352  HIS B ND1   1 
ATOM   6771 C CD2   . HIS B 1 352 ? 3.559   -59.643 -4.879  1.00 29.30 ? 352  HIS B CD2   1 
ATOM   6772 C CE1   . HIS B 1 352 ? 5.193   -59.127 -3.517  1.00 30.78 ? 352  HIS B CE1   1 
ATOM   6773 N NE2   . HIS B 1 352 ? 4.879   -59.267 -4.791  1.00 28.53 ? 352  HIS B NE2   1 
ATOM   6774 N N     . GLU B 1 353 ? 3.222   -62.981 -3.595  1.00 37.33 ? 353  GLU B N     1 
ATOM   6775 C CA    . GLU B 1 353 ? 3.760   -63.985 -4.560  1.00 46.29 ? 353  GLU B CA    1 
ATOM   6776 C C     . GLU B 1 353 ? 3.351   -65.415 -4.178  1.00 49.42 ? 353  GLU B C     1 
ATOM   6777 O O     . GLU B 1 353 ? 3.569   -66.310 -5.007  1.00 52.24 ? 353  GLU B O     1 
ATOM   6778 C CB    . GLU B 1 353 ? 5.276   -63.926 -4.758  1.00 50.22 ? 353  GLU B CB    1 
ATOM   6779 C CG    . GLU B 1 353 ? 6.067   -63.105 -3.768  1.00 51.05 ? 353  GLU B CG    1 
ATOM   6780 C CD    . GLU B 1 353 ? 7.343   -62.530 -4.363  1.00 52.89 ? 353  GLU B CD    1 
ATOM   6781 O OE1   . GLU B 1 353 ? 7.419   -62.405 -5.598  1.00 60.44 ? 353  GLU B OE1   1 
ATOM   6782 O OE2   . GLU B 1 353 ? 8.247   -62.180 -3.596  1.00 58.54 ? 353  GLU B OE2   1 
ATOM   6783 N N     . GLU B 1 354 ? 2.701   -65.629 -3.032  1.00 47.18 ? 354  GLU B N     1 
ATOM   6784 C CA    . GLU B 1 354 ? 2.327   -66.982 -2.553  1.00 44.63 ? 354  GLU B CA    1 
ATOM   6785 C C     . GLU B 1 354 ? 0.859   -67.302 -2.848  1.00 46.95 ? 354  GLU B C     1 
ATOM   6786 O O     . GLU B 1 354 ? 0.535   -68.498 -2.808  1.00 41.68 ? 354  GLU B O     1 
ATOM   6787 C CB    . GLU B 1 354 ? 2.547   -67.094 -1.050  1.00 47.09 ? 354  GLU B CB    1 
ATOM   6788 C CG    . GLU B 1 354 ? 4.007   -67.075 -0.659  1.00 48.18 ? 354  GLU B CG    1 
ATOM   6789 C CD    . GLU B 1 354 ? 4.204   -67.229 0.834   1.00 50.75 ? 354  GLU B CD    1 
ATOM   6790 O OE1   . GLU B 1 354 ? 3.498   -66.538 1.590   1.00 43.81 ? 354  GLU B OE1   1 
ATOM   6791 O OE2   . GLU B 1 354 ? 5.044   -68.060 1.236   1.00 55.23 ? 354  GLU B OE2   1 
ATOM   6792 N N     . ARG B 1 355 ? -0.003  -66.297 -3.041  1.00 44.53 ? 355  ARG B N     1 
ATOM   6793 C CA    . ARG B 1 355 ? -1.472  -66.497 -3.091  1.00 42.74 ? 355  ARG B CA    1 
ATOM   6794 C C     . ARG B 1 355 ? -2.087  -65.759 -4.284  1.00 43.87 ? 355  ARG B C     1 
ATOM   6795 O O     . ARG B 1 355 ? -1.887  -64.547 -4.409  1.00 43.74 ? 355  ARG B O     1 
ATOM   6796 C CB    . ARG B 1 355 ? -2.086  -66.043 -1.761  1.00 42.77 ? 355  ARG B CB    1 
ATOM   6797 C CG    . ARG B 1 355 ? -3.355  -66.793 -1.415  1.00 40.50 ? 355  ARG B CG    1 
ATOM   6798 C CD    . ARG B 1 355 ? -4.169  -66.076 -0.369  1.00 37.98 ? 355  ARG B CD    1 
ATOM   6799 N NE    . ARG B 1 355 ? -5.496  -66.653 -0.408  1.00 43.62 ? 355  ARG B NE    1 
ATOM   6800 C CZ    . ARG B 1 355 ? -6.348  -66.676 0.594   1.00 44.22 ? 355  ARG B CZ    1 
ATOM   6801 N NH1   . ARG B 1 355 ? -6.034  -66.132 1.754   1.00 43.66 ? 355  ARG B NH1   1 
ATOM   6802 N NH2   . ARG B 1 355 ? -7.513  -67.269 0.428   1.00 49.81 ? 355  ARG B NH2   1 
ATOM   6803 N N     . HIS B 1 356 ? -2.841  -66.473 -5.124  1.00 44.82 ? 356  HIS B N     1 
ATOM   6804 C CA    . HIS B 1 356 ? -3.320  -65.998 -6.452  1.00 44.04 ? 356  HIS B CA    1 
ATOM   6805 C C     . HIS B 1 356 ? -4.709  -66.558 -6.769  1.00 43.93 ? 356  HIS B C     1 
ATOM   6806 O O     . HIS B 1 356 ? -5.053  -66.577 -7.956  1.00 50.14 ? 356  HIS B O     1 
ATOM   6807 C CB    . HIS B 1 356 ? -2.293  -66.390 -7.525  1.00 44.09 ? 356  HIS B CB    1 
ATOM   6808 C CG    . HIS B 1 356 ? -1.051  -65.571 -7.456  1.00 41.09 ? 356  HIS B CG    1 
ATOM   6809 N ND1   . HIS B 1 356 ? 0.136   -66.061 -6.940  1.00 44.09 ? 356  HIS B ND1   1 
ATOM   6810 C CD2   . HIS B 1 356 ? -0.821  -64.287 -7.803  1.00 39.73 ? 356  HIS B CD2   1 
ATOM   6811 C CE1   . HIS B 1 356 ? 1.049   -65.107 -6.974  1.00 41.81 ? 356  HIS B CE1   1 
ATOM   6812 N NE2   . HIS B 1 356 ? 0.487   -64.016 -7.507  1.00 43.43 ? 356  HIS B NE2   1 
ATOM   6813 N N     . ASP B 1 357 ? -5.482  -66.937 -5.745  1.00 44.84 ? 357  ASP B N     1 
ATOM   6814 C CA    . ASP B 1 357 ? -6.846  -67.525 -5.855  1.00 43.48 ? 357  ASP B CA    1 
ATOM   6815 C C     . ASP B 1 357 ? -7.908  -66.434 -5.633  1.00 45.90 ? 357  ASP B C     1 
ATOM   6816 O O     . ASP B 1 357 ? -7.540  -65.254 -5.364  1.00 42.56 ? 357  ASP B O     1 
ATOM   6817 C CB    . ASP B 1 357 ? -7.017  -68.685 -4.868  1.00 47.92 ? 357  ASP B CB    1 
ATOM   6818 C CG    . ASP B 1 357 ? -6.764  -68.333 -3.408  1.00 49.64 ? 357  ASP B CG    1 
ATOM   6819 O OD1   . ASP B 1 357 ? -6.322  -67.223 -3.129  1.00 49.98 ? 357  ASP B OD1   1 
ATOM   6820 O OD2   . ASP B 1 357 ? -6.986  -69.190 -2.559  1.00 59.08 ? 357  ASP B OD2   1 
ATOM   6821 N N     . ARG B 1 358 ? -9.180  -66.802 -5.753  1.00 41.95 ? 358  ARG B N     1 
ATOM   6822 C CA    . ARG B 1 358 ? -10.333 -65.885 -5.589  1.00 47.62 ? 358  ARG B CA    1 
ATOM   6823 C C     . ARG B 1 358 ? -10.134 -65.105 -4.277  1.00 44.88 ? 358  ARG B C     1 
ATOM   6824 O O     . ARG B 1 358 ? -10.306 -63.876 -4.282  1.00 40.02 ? 358  ARG B O     1 
ATOM   6825 C CB    . ARG B 1 358 ? -11.635 -66.698 -5.647  1.00 50.88 ? 358  ARG B CB    1 
ATOM   6826 C CG    . ARG B 1 358 ? -12.903 -65.867 -5.491  1.00 57.27 ? 358  ARG B CG    1 
ATOM   6827 C CD    . ARG B 1 358 ? -14.066 -66.419 -6.279  1.00 60.37 ? 358  ARG B CD    1 
ATOM   6828 N NE    . ARG B 1 358 ? -14.810 -67.433 -5.550  1.00 62.48 ? 358  ARG B NE    1 
ATOM   6829 C CZ    . ARG B 1 358 ? -16.097 -67.354 -5.212  1.00 61.07 ? 358  ARG B CZ    1 
ATOM   6830 N NH1   . ARG B 1 358 ? -16.815 -66.286 -5.519  1.00 56.07 ? 358  ARG B NH1   1 
ATOM   6831 N NH2   . ARG B 1 358 ? -16.664 -68.353 -4.555  1.00 59.61 ? 358  ARG B NH2   1 
ATOM   6832 N N     . GLY B 1 359 ? -9.710  -65.792 -3.216  1.00 41.01 ? 359  GLY B N     1 
ATOM   6833 C CA    . GLY B 1 359 ? -9.517  -65.214 -1.873  1.00 44.76 ? 359  GLY B CA    1 
ATOM   6834 C C     . GLY B 1 359 ? -8.340  -64.248 -1.785  1.00 47.79 ? 359  GLY B C     1 
ATOM   6835 O O     . GLY B 1 359 ? -8.260  -63.526 -0.760  1.00 41.92 ? 359  GLY B O     1 
ATOM   6836 N N     . ALA B 1 360 ? -7.437  -64.245 -2.776  1.00 42.90 ? 360  ALA B N     1 
ATOM   6837 C CA    . ALA B 1 360 ? -6.235  -63.374 -2.812  1.00 41.79 ? 360  ALA B CA    1 
ATOM   6838 C C     . ALA B 1 360 ? -6.520  -62.086 -3.601  1.00 40.03 ? 360  ALA B C     1 
ATOM   6839 O O     . ALA B 1 360 ? -5.570  -61.297 -3.798  1.00 41.07 ? 360  ALA B O     1 
ATOM   6840 C CB    . ALA B 1 360 ? -5.064  -64.117 -3.402  1.00 41.44 ? 360  ALA B CB    1 
ATOM   6841 N N     . HIS B 1 361 ? -7.757  -61.888 -4.056  1.00 34.86 ? 361  HIS B N     1 
ATOM   6842 C CA    . HIS B 1 361 ? -8.142  -60.709 -4.852  1.00 36.23 ? 361  HIS B CA    1 
ATOM   6843 C C     . HIS B 1 361 ? -7.809  -59.435 -4.059  1.00 33.49 ? 361  HIS B C     1 
ATOM   6844 O O     . HIS B 1 361 ? -7.201  -58.497 -4.646  1.00 33.19 ? 361  HIS B O     1 
ATOM   6845 C CB    . HIS B 1 361 ? -9.616  -60.745 -5.263  1.00 38.87 ? 361  HIS B CB    1 
ATOM   6846 C CG    . HIS B 1 361 ? -9.887  -59.731 -6.322  1.00 47.47 ? 361  HIS B CG    1 
ATOM   6847 N ND1   . HIS B 1 361 ? -9.553  -59.965 -7.652  1.00 48.97 ? 361  HIS B ND1   1 
ATOM   6848 C CD2   . HIS B 1 361 ? -10.359 -58.462 -6.254  1.00 48.28 ? 361  HIS B CD2   1 
ATOM   6849 C CE1   . HIS B 1 361 ? -9.821  -58.888 -8.362  1.00 56.09 ? 361  HIS B CE1   1 
ATOM   6850 N NE2   . HIS B 1 361 ? -10.333 -57.951 -7.526  1.00 52.61 ? 361  HIS B NE2   1 
ATOM   6851 N N     . VAL B 1 362 ? -8.221  -59.369 -2.796  1.00 32.70 ? 362  VAL B N     1 
ATOM   6852 C CA    . VAL B 1 362 ? -8.007  -58.150 -1.975  1.00 30.75 ? 362  VAL B CA    1 
ATOM   6853 C C     . VAL B 1 362 ? -6.499  -57.999 -1.734  1.00 29.48 ? 362  VAL B C     1 
ATOM   6854 O O     . VAL B 1 362 ? -5.995  -56.872 -1.909  1.00 32.10 ? 362  VAL B O     1 
ATOM   6855 C CB    . VAL B 1 362 ? -8.846  -58.168 -0.686  1.00 30.66 ? 362  VAL B CB    1 
ATOM   6856 C CG1   . VAL B 1 362 ? -8.338  -57.135 0.312   1.00 32.32 ? 362  VAL B CG1   1 
ATOM   6857 C CG2   . VAL B 1 362 ? -10.305 -57.939 -1.021  1.00 29.96 ? 362  VAL B CG2   1 
ATOM   6858 N N     . LEU B 1 363 ? -5.791  -59.086 -1.426  1.00 29.96 ? 363  LEU B N     1 
ATOM   6859 C CA    . LEU B 1 363 ? -4.318  -59.072 -1.257  1.00 29.35 ? 363  LEU B CA    1 
ATOM   6860 C C     . LEU B 1 363 ? -3.652  -58.440 -2.492  1.00 31.39 ? 363  LEU B C     1 
ATOM   6861 O O     . LEU B 1 363 ? -2.795  -57.592 -2.321  1.00 28.58 ? 363  LEU B O     1 
ATOM   6862 C CB    . LEU B 1 363 ? -3.804  -60.486 -1.011  1.00 29.68 ? 363  LEU B CB    1 
ATOM   6863 C CG    . LEU B 1 363 ? -2.284  -60.657 -1.057  1.00 31.27 ? 363  LEU B CG    1 
ATOM   6864 C CD1   . LEU B 1 363 ? -1.577  -59.817 0.006   1.00 33.18 ? 363  LEU B CD1   1 
ATOM   6865 C CD2   . LEU B 1 363 ? -1.906  -62.104 -0.897  1.00 29.05 ? 363  LEU B CD2   1 
ATOM   6866 N N     . GLN B 1 364 ? -4.013  -58.858 -3.698  1.00 30.66 ? 364  GLN B N     1 
ATOM   6867 C CA    . GLN B 1 364 ? -3.367  -58.358 -4.934  1.00 31.27 ? 364  GLN B CA    1 
ATOM   6868 C C     . GLN B 1 364 ? -3.773  -56.906 -5.158  1.00 30.14 ? 364  GLN B C     1 
ATOM   6869 O O     . GLN B 1 364 ? -2.928  -56.152 -5.627  1.00 30.95 ? 364  GLN B O     1 
ATOM   6870 C CB    . GLN B 1 364 ? -3.703  -59.250 -6.132  1.00 32.38 ? 364  GLN B CB    1 
ATOM   6871 C CG    . GLN B 1 364 ? -3.186  -60.677 -5.967  1.00 34.74 ? 364  GLN B CG    1 
ATOM   6872 C CD    . GLN B 1 364 ? -1.690  -60.770 -5.821  1.00 34.59 ? 364  GLN B CD    1 
ATOM   6873 O OE1   . GLN B 1 364 ? -0.949  -59.863 -6.194  1.00 36.29 ? 364  GLN B OE1   1 
ATOM   6874 N NE2   . GLN B 1 364 ? -1.228  -61.887 -5.285  1.00 35.53 ? 364  GLN B NE2   1 
ATOM   6875 N N     . ASP B 1 365 ? -4.997  -56.517 -4.800  1.00 30.21 ? 365  ASP B N     1 
ATOM   6876 C CA    . ASP B 1 365 ? -5.440  -55.106 -4.924  1.00 31.42 ? 365  ASP B CA    1 
ATOM   6877 C C     . ASP B 1 365 ? -4.665  -54.243 -3.926  1.00 30.75 ? 365  ASP B C     1 
ATOM   6878 O O     . ASP B 1 365 ? -4.235  -53.149 -4.310  1.00 29.49 ? 365  ASP B O     1 
ATOM   6879 C CB    . ASP B 1 365 ? -6.940  -54.945 -4.737  1.00 30.13 ? 365  ASP B CB    1 
ATOM   6880 C CG    . ASP B 1 365 ? -7.478  -53.660 -5.340  1.00 29.85 ? 365  ASP B CG    1 
ATOM   6881 O OD1   . ASP B 1 365 ? -7.092  -53.330 -6.490  1.00 29.82 ? 365  ASP B OD1   1 
ATOM   6882 O OD2   . ASP B 1 365 ? -8.304  -53.008 -4.684  1.00 29.39 ? 365  ASP B OD2   1 
ATOM   6883 N N     . ARG B 1 366 ? -4.487  -54.713 -2.695  1.00 29.62 ? 366  ARG B N     1 
ATOM   6884 C CA    . ARG B 1 366 ? -3.750  -53.943 -1.657  1.00 30.03 ? 366  ARG B CA    1 
ATOM   6885 C C     . ARG B 1 366 ? -2.309  -53.768 -2.125  1.00 30.55 ? 366  ARG B C     1 
ATOM   6886 O O     . ARG B 1 366 ? -1.738  -52.671 -1.903  1.00 32.45 ? 366  ARG B O     1 
ATOM   6887 C CB    . ARG B 1 366 ? -3.801  -54.621 -0.287  1.00 28.50 ? 366  ARG B CB    1 
ATOM   6888 C CG    . ARG B 1 366 ? -5.204  -54.855 0.260   1.00 28.04 ? 366  ARG B CG    1 
ATOM   6889 C CD    . ARG B 1 366 ? -6.251  -53.842 -0.089  1.00 28.40 ? 366  ARG B CD    1 
ATOM   6890 N NE    . ARG B 1 366 ? -6.027  -52.573 0.614   1.00 29.41 ? 366  ARG B NE    1 
ATOM   6891 C CZ    . ARG B 1 366 ? -6.853  -51.533 0.568   1.00 28.73 ? 366  ARG B CZ    1 
ATOM   6892 N NH1   . ARG B 1 366 ? -7.959  -51.608 -0.154  1.00 27.38 ? 366  ARG B NH1   1 
ATOM   6893 N NH2   . ARG B 1 366 ? -6.570  -50.423 1.243   1.00 29.82 ? 366  ARG B NH2   1 
ATOM   6894 N N     . HIS B 1 367 ? -1.749  -54.775 -2.793  1.00 31.18 ? 367  HIS B N     1 
ATOM   6895 C CA    . HIS B 1 367 ? -0.360  -54.729 -3.318  1.00 30.08 ? 367  HIS B CA    1 
ATOM   6896 C C     . HIS B 1 367 ? -0.219  -53.590 -4.336  1.00 30.15 ? 367  HIS B C     1 
ATOM   6897 O O     . HIS B 1 367 ? 0.860   -52.972 -4.381  1.00 33.64 ? 367  HIS B O     1 
ATOM   6898 C CB    . HIS B 1 367 ? 0.049   -56.093 -3.871  1.00 32.01 ? 367  HIS B CB    1 
ATOM   6899 C CG    . HIS B 1 367 ? 1.476   -56.134 -4.291  1.00 31.59 ? 367  HIS B CG    1 
ATOM   6900 N ND1   . HIS B 1 367 ? 2.489   -55.814 -3.421  1.00 32.22 ? 367  HIS B ND1   1 
ATOM   6901 C CD2   . HIS B 1 367 ? 2.056   -56.415 -5.478  1.00 33.92 ? 367  HIS B CD2   1 
ATOM   6902 C CE1   . HIS B 1 367 ? 3.642   -55.893 -4.047  1.00 33.79 ? 367  HIS B CE1   1 
ATOM   6903 N NE2   . HIS B 1 367 ? 3.404   -56.271 -5.310  1.00 31.24 ? 367  HIS B NE2   1 
ATOM   6904 N N     . LYS B 1 368 ? -1.246  -53.337 -5.142  1.00 30.66 ? 368  LYS B N     1 
ATOM   6905 C CA    . LYS B 1 368 ? -1.281  -52.198 -6.080  1.00 32.17 ? 368  LYS B CA    1 
ATOM   6906 C C     . LYS B 1 368 ? -1.379  -50.904 -5.264  1.00 33.06 ? 368  LYS B C     1 
ATOM   6907 O O     . LYS B 1 368 ? -0.454  -50.092 -5.314  1.00 30.34 ? 368  LYS B O     1 
ATOM   6908 C CB    . LYS B 1 368 ? -2.448  -52.364 -7.056  1.00 36.70 ? 368  LYS B CB    1 
ATOM   6909 C CG    . LYS B 1 368 ? -2.276  -53.512 -8.052  1.00 39.72 ? 368  LYS B CG    1 
ATOM   6910 C CD    . LYS B 1 368 ? -3.572  -53.939 -8.723  1.00 48.04 ? 368  LYS B CD    1 
ATOM   6911 C CE    . LYS B 1 368 ? -3.987  -53.045 -9.869  1.00 56.69 ? 368  LYS B CE    1 
ATOM   6912 N NZ    . LYS B 1 368 ? -5.403  -53.277 -10.255 1.00 62.84 ? 368  LYS B NZ    1 
ATOM   6913 N N     . ILE B 1 369 ? -2.441  -50.767 -4.487  1.00 29.29 ? 369  ILE B N     1 
ATOM   6914 C CA    . ILE B 1 369 ? -2.760  -49.535 -3.719  1.00 27.07 ? 369  ILE B CA    1 
ATOM   6915 C C     . ILE B 1 369 ? -1.559  -49.156 -2.842  1.00 26.34 ? 369  ILE B C     1 
ATOM   6916 O O     . ILE B 1 369 ? -1.175  -47.968 -2.846  1.00 25.43 ? 369  ILE B O     1 
ATOM   6917 C CB    . ILE B 1 369 ? -4.054  -49.762 -2.908  1.00 28.95 ? 369  ILE B CB    1 
ATOM   6918 C CG1   . ILE B 1 369 ? -5.283  -49.813 -3.816  1.00 28.32 ? 369  ILE B CG1   1 
ATOM   6919 C CG2   . ILE B 1 369 ? -4.206  -48.696 -1.835  1.00 28.18 ? 369  ILE B CG2   1 
ATOM   6920 C CD1   . ILE B 1 369 ? -6.443  -50.555 -3.212  1.00 31.54 ? 369  ILE B CD1   1 
ATOM   6921 N N     . ASN B 1 370 ? -0.984  -50.115 -2.120  1.00 24.94 ? 370  ASN B N     1 
ATOM   6922 C CA    . ASN B 1 370 ? 0.120   -49.890 -1.160  1.00 27.57 ? 370  ASN B CA    1 
ATOM   6923 C C     . ASN B 1 370 ? 1.423   -49.530 -1.905  1.00 28.95 ? 370  ASN B C     1 
ATOM   6924 O O     . ASN B 1 370 ? 2.355   -49.088 -1.237  1.00 27.71 ? 370  ASN B O     1 
ATOM   6925 C CB    . ASN B 1 370 ? 0.272   -51.081 -0.226  1.00 27.46 ? 370  ASN B CB    1 
ATOM   6926 C CG    . ASN B 1 370 ? -0.933  -51.291 0.671   1.00 25.08 ? 370  ASN B CG    1 
ATOM   6927 O OD1   . ASN B 1 370 ? -1.868  -50.489 0.644   1.00 26.70 ? 370  ASN B OD1   1 
ATOM   6928 N ND2   . ASN B 1 370 ? -0.893  -52.343 1.467   1.00 25.30 ? 370  ASN B ND2   1 
ATOM   6929 N N     . ASN B 1 371 ? 1.446   -49.647 -3.240  1.00 32.85 ? 371  ASN B N     1 
ATOM   6930 C CA    . ASN B 1 371 ? 2.581   -49.248 -4.113  1.00 32.61 ? 371  ASN B CA    1 
ATOM   6931 C C     . ASN B 1 371 ? 2.178   -48.083 -5.027  1.00 31.21 ? 371  ASN B C     1 
ATOM   6932 O O     . ASN B 1 371 ? 2.889   -47.832 -6.013  1.00 31.23 ? 371  ASN B O     1 
ATOM   6933 C CB    . ASN B 1 371 ? 3.109   -50.456 -4.896  1.00 31.95 ? 371  ASN B CB    1 
ATOM   6934 C CG    . ASN B 1 371 ? 3.962   -51.333 -4.016  1.00 30.88 ? 371  ASN B CG    1 
ATOM   6935 O OD1   . ASN B 1 371 ? 5.061   -50.921 -3.649  1.00 36.17 ? 371  ASN B OD1   1 
ATOM   6936 N ND2   . ASN B 1 371 ? 3.450   -52.497 -3.629  1.00 31.34 ? 371  ASN B ND2   1 
ATOM   6937 N N     . GLY B 1 372 ? 1.105   -47.365 -4.686  1.00 27.67 ? 372  GLY B N     1 
ATOM   6938 C CA    . GLY B 1 372 ? 0.634   -46.191 -5.429  1.00 27.89 ? 372  GLY B CA    1 
ATOM   6939 C C     . GLY B 1 372 ? 0.238   -46.553 -6.849  1.00 30.57 ? 372  GLY B C     1 
ATOM   6940 O O     . GLY B 1 372 ? 0.404   -45.712 -7.749  1.00 30.12 ? 372  GLY B O     1 
ATOM   6941 N N     . ILE B 1 373 ? -0.288  -47.761 -7.046  1.00 29.49 ? 373  ILE B N     1 
ATOM   6942 C CA    . ILE B 1 373 ? -0.891  -48.154 -8.342  1.00 30.80 ? 373  ILE B CA    1 
ATOM   6943 C C     . ILE B 1 373 ? -2.392  -48.120 -8.146  1.00 29.37 ? 373  ILE B C     1 
ATOM   6944 O O     . ILE B 1 373 ? -2.942  -48.955 -7.428  1.00 31.48 ? 373  ILE B O     1 
ATOM   6945 C CB    . ILE B 1 373 ? -0.357  -49.508 -8.833  1.00 34.29 ? 373  ILE B CB    1 
ATOM   6946 C CG1   . ILE B 1 373 ? 1.141   -49.421 -9.133  1.00 37.35 ? 373  ILE B CG1   1 
ATOM   6947 C CG2   . ILE B 1 373 ? -1.146  -49.977 -10.059 1.00 32.72 ? 373  ILE B CG2   1 
ATOM   6948 C CD1   . ILE B 1 373 ? 1.964   -50.477 -8.468  1.00 38.28 ? 373  ILE B CD1   1 
ATOM   6949 N N     . PRO B 1 374 ? -3.079  -47.126 -8.748  1.00 28.49 ? 374  PRO B N     1 
ATOM   6950 C CA    . PRO B 1 374 ? -4.499  -46.927 -8.506  1.00 28.67 ? 374  PRO B CA    1 
ATOM   6951 C C     . PRO B 1 374 ? -5.317  -48.047 -9.161  1.00 31.99 ? 374  PRO B C     1 
ATOM   6952 O O     . PRO B 1 374 ? -4.861  -48.657 -10.136 1.00 34.25 ? 374  PRO B O     1 
ATOM   6953 C CB    . PRO B 1 374 ? -4.770  -45.535 -9.091  1.00 30.38 ? 374  PRO B CB    1 
ATOM   6954 C CG    . PRO B 1 374 ? -3.725  -45.386 -10.181 1.00 28.65 ? 374  PRO B CG    1 
ATOM   6955 C CD    . PRO B 1 374 ? -2.518  -46.130 -9.665  1.00 28.46 ? 374  PRO B CD    1 
ATOM   6956 N N     . SER B 1 375 ? -6.494  -48.306 -8.599  1.00 32.79 ? 375  SER B N     1 
ATOM   6957 C CA    . SER B 1 375 ? -7.367  -49.454 -8.953  1.00 32.68 ? 375  SER B CA    1 
ATOM   6958 C C     . SER B 1 375 ? -8.835  -49.046 -8.840  1.00 33.91 ? 375  SER B C     1 
ATOM   6959 O O     . SER B 1 375 ? -9.121  -48.093 -8.104  1.00 30.20 ? 375  SER B O     1 
ATOM   6960 C CB    . SER B 1 375 ? -7.054  -50.612 -8.063  1.00 36.54 ? 375  SER B CB    1 
ATOM   6961 O OG    . SER B 1 375 ? -7.920  -51.701 -8.323  1.00 37.97 ? 375  SER B OG    1 
ATOM   6962 N N     . LEU B 1 376 ? -9.735  -49.727 -9.552  1.00 31.49 ? 376  LEU B N     1 
ATOM   6963 C CA    . LEU B 1 376 ? -11.195 -49.637 -9.297  1.00 32.02 ? 376  LEU B CA    1 
ATOM   6964 C C     . LEU B 1 376 ? -11.749 -51.005 -8.870  1.00 32.08 ? 376  LEU B C     1 
ATOM   6965 O O     . LEU B 1 376 ? -12.962 -51.121 -8.848  1.00 31.70 ? 376  LEU B O     1 
ATOM   6966 C CB    . LEU B 1 376 ? -11.909 -49.098 -10.544 1.00 34.92 ? 376  LEU B CB    1 
ATOM   6967 C CG    . LEU B 1 376 ? -11.562 -47.661 -10.926 1.00 36.15 ? 376  LEU B CG    1 
ATOM   6968 C CD1   . LEU B 1 376 ? -12.139 -47.291 -12.284 1.00 36.68 ? 376  LEU B CD1   1 
ATOM   6969 C CD2   . LEU B 1 376 ? -12.048 -46.693 -9.857  1.00 31.17 ? 376  LEU B CD2   1 
ATOM   6970 N N     . SER B 1 377 ? -10.905 -51.953 -8.461  1.00 32.86 ? 377  SER B N     1 
ATOM   6971 C CA    . SER B 1 377 ? -11.313 -53.313 -8.020  1.00 38.19 ? 377  SER B CA    1 
ATOM   6972 C C     . SER B 1 377 ? -12.318 -53.231 -6.871  1.00 38.13 ? 377  SER B C     1 
ATOM   6973 O O     . SER B 1 377 ? -13.272 -54.011 -6.903  1.00 33.10 ? 377  SER B O     1 
ATOM   6974 C CB    . SER B 1 377 ? -10.145 -54.174 -7.626  1.00 41.50 ? 377  SER B CB    1 
ATOM   6975 O OG    . SER B 1 377 ? -9.377  -54.517 -8.771  1.00 46.80 ? 377  SER B OG    1 
ATOM   6976 N N     . GLU B 1 378 ? -12.155 -52.301 -5.922  1.00 36.63 ? 378  GLU B N     1 
ATOM   6977 C CA    . GLU B 1 378 ? -13.028 -52.263 -4.717  1.00 36.94 ? 378  GLU B CA    1 
ATOM   6978 C C     . GLU B 1 378 ? -14.459 -51.875 -5.086  1.00 34.17 ? 378  GLU B C     1 
ATOM   6979 O O     . GLU B 1 378 ? -15.325 -52.053 -4.226  1.00 33.87 ? 378  GLU B O     1 
ATOM   6980 C CB    . GLU B 1 378 ? -12.506 -51.304 -3.642  1.00 42.70 ? 378  GLU B CB    1 
ATOM   6981 C CG    . GLU B 1 378 ? -11.147 -51.698 -3.113  1.00 49.75 ? 378  GLU B CG    1 
ATOM   6982 C CD    . GLU B 1 378 ? -11.106 -52.816 -2.087  1.00 54.93 ? 378  GLU B CD    1 
ATOM   6983 O OE1   . GLU B 1 378 ? -12.050 -52.874 -1.255  1.00 46.59 ? 378  GLU B OE1   1 
ATOM   6984 O OE2   . GLU B 1 378 ? -10.072 -53.579 -2.086  1.00 63.16 ? 378  GLU B OE2   1 
ATOM   6985 N N     . MET B 1 379 ? -14.713 -51.349 -6.295  1.00 34.86 ? 379  MET B N     1 
ATOM   6986 C CA    . MET B 1 379 ? -16.100 -51.048 -6.744  1.00 37.11 ? 379  MET B CA    1 
ATOM   6987 C C     . MET B 1 379 ? -16.940 -52.332 -6.846  1.00 33.30 ? 379  MET B C     1 
ATOM   6988 O O     . MET B 1 379 ? -18.171 -52.216 -6.797  1.00 32.59 ? 379  MET B O     1 
ATOM   6989 C CB    . MET B 1 379 ? -16.124 -50.297 -8.077  1.00 38.81 ? 379  MET B CB    1 
ATOM   6990 C CG    . MET B 1 379 ? -15.928 -48.809 -7.882  1.00 39.88 ? 379  MET B CG    1 
ATOM   6991 S SD    . MET B 1 379 ? -17.190 -48.061 -6.802  1.00 43.56 ? 379  MET B SD    1 
ATOM   6992 C CE    . MET B 1 379 ? -18.639 -48.288 -7.836  1.00 42.23 ? 379  MET B CE    1 
ATOM   6993 N N     . LYS B 1 380 ? -16.308 -53.503 -6.889  1.00 32.92 ? 380  LYS B N     1 
ATOM   6994 C CA    . LYS B 1 380 ? -17.016 -54.815 -6.953  1.00 34.95 ? 380  LYS B CA    1 
ATOM   6995 C C     . LYS B 1 380 ? -17.778 -55.020 -5.642  1.00 38.95 ? 380  LYS B C     1 
ATOM   6996 O O     . LYS B 1 380 ? -18.780 -55.745 -5.604  1.00 34.18 ? 380  LYS B O     1 
ATOM   6997 C CB    . LYS B 1 380 ? -16.013 -55.923 -7.269  1.00 37.11 ? 380  LYS B CB    1 
ATOM   6998 C CG    . LYS B 1 380 ? -15.636 -56.007 -8.741  1.00 39.22 ? 380  LYS B CG    1 
ATOM   6999 C CD    . LYS B 1 380 ? -14.909 -57.286 -9.134  1.00 42.35 ? 380  LYS B CD    1 
ATOM   7000 C CE    . LYS B 1 380 ? -13.662 -57.569 -8.316  1.00 45.97 ? 380  LYS B CE    1 
ATOM   7001 N NZ    . LYS B 1 380 ? -12.732 -56.408 -8.295  1.00 50.00 ? 380  LYS B NZ    1 
ATOM   7002 N N     . LEU B 1 381 ? -17.349 -54.317 -4.601  1.00 36.40 ? 381  LEU B N     1 
ATOM   7003 C CA    . LEU B 1 381 ? -18.014 -54.326 -3.296  1.00 38.29 ? 381  LEU B CA    1 
ATOM   7004 C C     . LEU B 1 381 ? -19.485 -53.947 -3.495  1.00 38.08 ? 381  LEU B C     1 
ATOM   7005 O O     . LEU B 1 381 ? -20.354 -54.546 -2.806  1.00 34.39 ? 381  LEU B O     1 
ATOM   7006 C CB    . LEU B 1 381 ? -17.245 -53.349 -2.411  1.00 44.20 ? 381  LEU B CB    1 
ATOM   7007 C CG    . LEU B 1 381 ? -17.354 -53.618 -0.928  1.00 53.46 ? 381  LEU B CG    1 
ATOM   7008 C CD1   . LEU B 1 381 ? -15.975 -53.612 -0.291  1.00 56.07 ? 381  LEU B CD1   1 
ATOM   7009 C CD2   . LEU B 1 381 ? -18.275 -52.580 -0.318  1.00 58.75 ? 381  LEU B CD2   1 
ATOM   7010 N N     . MET B 1 382 ? -19.769 -53.045 -4.444  1.00 36.00 ? 382  MET B N     1 
ATOM   7011 C CA    . MET B 1 382 ? -21.126 -52.478 -4.649  1.00 37.09 ? 382  MET B CA    1 
ATOM   7012 C C     . MET B 1 382 ? -22.020 -53.445 -5.445  1.00 34.12 ? 382  MET B C     1 
ATOM   7013 O O     . MET B 1 382 ? -23.147 -53.042 -5.763  1.00 35.56 ? 382  MET B O     1 
ATOM   7014 C CB    . MET B 1 382 ? -21.035 -51.124 -5.362  1.00 36.74 ? 382  MET B CB    1 
ATOM   7015 C CG    . MET B 1 382 ? -20.119 -50.116 -4.665  1.00 40.63 ? 382  MET B CG    1 
ATOM   7016 S SD    . MET B 1 382 ? -20.223 -50.153 -2.866  1.00 38.27 ? 382  MET B SD    1 
ATOM   7017 C CE    . MET B 1 382 ? -21.821 -49.406 -2.623  1.00 37.61 ? 382  MET B CE    1 
ATOM   7018 N N     . ASP B 1 383 ? -21.555 -54.667 -5.728  1.00 35.28 ? 383  ASP B N     1 
ATOM   7019 C CA    . ASP B 1 383 ? -22.369 -55.767 -6.325  1.00 37.37 ? 383  ASP B CA    1 
ATOM   7020 C C     . ASP B 1 383 ? -22.794 -56.758 -5.234  1.00 37.69 ? 383  ASP B C     1 
ATOM   7021 O O     . ASP B 1 383 ? -23.256 -57.871 -5.585  1.00 40.64 ? 383  ASP B O     1 
ATOM   7022 C CB    . ASP B 1 383 ? -21.605 -56.535 -7.408  1.00 38.66 ? 383  ASP B CB    1 
ATOM   7023 C CG    . ASP B 1 383 ? -21.194 -55.673 -8.589  1.00 40.95 ? 383  ASP B CG    1 
ATOM   7024 O OD1   . ASP B 1 383 ? -21.891 -54.679 -8.853  1.00 41.07 ? 383  ASP B OD1   1 
ATOM   7025 O OD2   . ASP B 1 383 ? -20.170 -55.994 -9.220  1.00 45.82 ? 383  ASP B OD2   1 
ATOM   7026 N N     . TRP B 1 384 ? -22.611 -56.405 -3.959  1.00 34.82 ? 384  TRP B N     1 
ATOM   7027 C CA    . TRP B 1 384 ? -22.909 -57.315 -2.827  1.00 33.10 ? 384  TRP B CA    1 
ATOM   7028 C C     . TRP B 1 384 ? -24.387 -57.694 -2.848  1.00 33.66 ? 384  TRP B C     1 
ATOM   7029 O O     . TRP B 1 384 ? -24.694 -58.867 -2.601  1.00 32.20 ? 384  TRP B O     1 
ATOM   7030 C CB    . TRP B 1 384 ? -22.555 -56.640 -1.506  1.00 31.66 ? 384  TRP B CB    1 
ATOM   7031 C CG    . TRP B 1 384 ? -22.781 -57.461 -0.280  1.00 30.19 ? 384  TRP B CG    1 
ATOM   7032 C CD1   . TRP B 1 384 ? -23.555 -57.120 0.794   1.00 29.47 ? 384  TRP B CD1   1 
ATOM   7033 C CD2   . TRP B 1 384 ? -22.155 -58.711 0.052   1.00 29.18 ? 384  TRP B CD2   1 
ATOM   7034 N NE1   . TRP B 1 384 ? -23.448 -58.075 1.762   1.00 29.94 ? 384  TRP B NE1   1 
ATOM   7035 C CE2   . TRP B 1 384 ? -22.617 -59.071 1.331   1.00 28.82 ? 384  TRP B CE2   1 
ATOM   7036 C CE3   . TRP B 1 384 ? -21.283 -59.571 -0.623  1.00 30.83 ? 384  TRP B CE3   1 
ATOM   7037 C CZ2   . TRP B 1 384 ? -22.216 -60.244 1.961   1.00 29.23 ? 384  TRP B CZ2   1 
ATOM   7038 C CZ3   . TRP B 1 384 ? -20.872 -60.723 0.002   1.00 30.68 ? 384  TRP B CZ3   1 
ATOM   7039 C CH2   . TRP B 1 384 ? -21.345 -61.060 1.274   1.00 30.75 ? 384  TRP B CH2   1 
ATOM   7040 N N     . ILE B 1 385 ? -25.235 -56.690 -3.033  1.00 36.06 ? 385  ILE B N     1 
ATOM   7041 C CA    . ILE B 1 385 ? -26.672 -56.883 -3.051  1.00 41.13 ? 385  ILE B CA    1 
ATOM   7042 C C     . ILE B 1 385 ? -27.120 -55.976 -4.158  1.00 46.65 ? 385  ILE B C     1 
ATOM   7043 O O     . ILE B 1 385 ? -26.436 -55.038 -4.493  1.00 53.08 ? 385  ILE B O     1 
ATOM   7044 C CB    . ILE B 1 385 ? -27.335 -56.424 -1.731  1.00 41.82 ? 385  ILE B CB    1 
ATOM   7045 C CG1   . ILE B 1 385 ? -26.761 -55.092 -1.237  1.00 44.66 ? 385  ILE B CG1   1 
ATOM   7046 C CG2   . ILE B 1 385 ? -27.201 -57.471 -0.649  1.00 41.32 ? 385  ILE B CG2   1 
ATOM   7047 C CD1   . ILE B 1 385 ? -27.722 -54.274 -0.416  1.00 44.91 ? 385  ILE B CD1   1 
ATOM   7048 N N     . PRO B 1 386 ? -28.269 -56.261 -4.759  1.00 50.73 ? 386  PRO B N     1 
ATOM   7049 C CA    . PRO B 1 386 ? -28.780 -55.347 -5.779  1.00 46.54 ? 386  PRO B CA    1 
ATOM   7050 C C     . PRO B 1 386 ? -29.039 -53.932 -5.285  1.00 40.13 ? 386  PRO B C     1 
ATOM   7051 O O     . PRO B 1 386 ? -29.570 -53.702 -4.225  1.00 39.81 ? 386  PRO B O     1 
ATOM   7052 C CB    . PRO B 1 386 ? -30.074 -56.014 -6.252  1.00 46.95 ? 386  PRO B CB    1 
ATOM   7053 C CG    . PRO B 1 386 ? -30.298 -57.193 -5.374  1.00 49.56 ? 386  PRO B CG    1 
ATOM   7054 C CD    . PRO B 1 386 ? -28.997 -57.540 -4.748  1.00 51.52 ? 386  PRO B CD    1 
ATOM   7055 N N     . GLY B 1 387 ? -28.622 -52.992 -6.115  1.00 53.52 ? 387  GLY B N     1 
ATOM   7056 C CA    . GLY B 1 387 ? -28.742 -51.573 -5.879  1.00 44.38 ? 387  GLY B CA    1 
ATOM   7057 C C     . GLY B 1 387 ? -27.865 -51.046 -4.760  1.00 36.67 ? 387  GLY B C     1 
ATOM   7058 O O     . GLY B 1 387 ? -28.125 -50.002 -4.203  1.00 37.02 ? 387  GLY B O     1 
ATOM   7059 N N     . ALA B 1 388 ? -26.821 -51.763 -4.443  1.00 35.35 ? 388  ALA B N     1 
ATOM   7060 C CA    . ALA B 1 388 ? -25.965 -51.381 -3.333  1.00 35.69 ? 388  ALA B CA    1 
ATOM   7061 C C     . ALA B 1 388 ? -25.341 -50.005 -3.336  1.00 38.54 ? 388  ALA B C     1 
ATOM   7062 O O     . ALA B 1 388 ? -24.857 -49.521 -4.334  1.00 33.98 ? 388  ALA B O     1 
ATOM   7063 C CB    . ALA B 1 388 ? -24.924 -52.434 -3.061  1.00 34.80 ? 388  ALA B CB    1 
ATOM   7064 N N     . GLY B 1 389 ? -25.389 -49.382 -2.183  1.00 41.07 ? 389  GLY B N     1 
ATOM   7065 C CA    . GLY B 1 389 ? -24.783 -48.101 -2.004  1.00 39.40 ? 389  GLY B CA    1 
ATOM   7066 C C     . GLY B 1 389 ? -24.240 -48.159 -0.611  1.00 40.34 ? 389  GLY B C     1 
ATOM   7067 O O     . GLY B 1 389 ? -24.601 -49.027 0.152   1.00 34.49 ? 389  GLY B O     1 
ATOM   7068 N N     . HIS B 1 390 ? -23.376 -47.230 -0.283  1.00 36.65 ? 390  HIS B N     1 
ATOM   7069 C CA    . HIS B 1 390 ? -22.892 -47.191 1.053   1.00 34.40 ? 390  HIS B CA    1 
ATOM   7070 C C     . HIS B 1 390 ? -22.799 -45.796 1.650   1.00 33.76 ? 390  HIS B C     1 
ATOM   7071 O O     . HIS B 1 390 ? -22.765 -44.812 0.935   1.00 29.27 ? 390  HIS B O     1 
ATOM   7072 C CB    . HIS B 1 390 ? -21.572 -47.889 1.128   1.00 34.98 ? 390  HIS B CB    1 
ATOM   7073 C CG    . HIS B 1 390 ? -20.463 -46.951 1.102   1.00 34.22 ? 390  HIS B CG    1 
ATOM   7074 N ND1   . HIS B 1 390 ? -19.869 -46.521 2.254   1.00 33.48 ? 390  HIS B ND1   1 
ATOM   7075 C CD2   . HIS B 1 390 ? -19.934 -46.234 0.095   1.00 35.38 ? 390  HIS B CD2   1 
ATOM   7076 C CE1   . HIS B 1 390 ? -19.001 -45.596 1.955   1.00 34.78 ? 390  HIS B CE1   1 
ATOM   7077 N NE2   . HIS B 1 390 ? -18.994 -45.414 0.653   1.00 34.48 ? 390  HIS B NE2   1 
ATOM   7078 N N     . VAL B 1 391 ? -22.823 -45.727 2.974   1.00 34.12 ? 391  VAL B N     1 
ATOM   7079 C CA    . VAL B 1 391 ? -22.638 -44.483 3.674   1.00 34.15 ? 391  VAL B CA    1 
ATOM   7080 C C     . VAL B 1 391 ? -21.441 -44.726 4.581   1.00 36.06 ? 391  VAL B C     1 
ATOM   7081 O O     . VAL B 1 391 ? -21.246 -45.818 5.087   1.00 35.05 ? 391  VAL B O     1 
ATOM   7082 C CB    . VAL B 1 391 ? -23.880 -44.034 4.469   1.00 36.74 ? 391  VAL B CB    1 
ATOM   7083 C CG1   . VAL B 1 391 ? -24.208 -44.967 5.612   1.00 35.40 ? 391  VAL B CG1   1 
ATOM   7084 C CG2   . VAL B 1 391 ? -23.744 -42.601 4.949   1.00 36.33 ? 391  VAL B CG2   1 
ATOM   7085 N N     . GLY B 1 392 ? -20.595 -43.722 4.708   1.00 35.96 ? 392  GLY B N     1 
ATOM   7086 C CA    . GLY B 1 392 ? -19.434 -43.849 5.557   1.00 35.66 ? 392  GLY B CA    1 
ATOM   7087 C C     . GLY B 1 392 ? -19.630 -43.592 7.026   1.00 30.83 ? 392  GLY B C     1 
ATOM   7088 O O     . GLY B 1 392 ? -20.262 -42.623 7.387   1.00 32.53 ? 392  GLY B O     1 
ATOM   7089 N N     . PHE B 1 393 ? -19.116 -44.476 7.851   1.00 29.42 ? 393  PHE B N     1 
ATOM   7090 C CA    . PHE B 1 393 ? -19.152 -44.302 9.276   1.00 29.31 ? 393  PHE B CA    1 
ATOM   7091 C C     . PHE B 1 393 ? -17.723 -44.645 9.642   1.00 28.66 ? 393  PHE B C     1 
ATOM   7092 O O     . PHE B 1 393 ? -17.279 -45.732 9.372   1.00 27.49 ? 393  PHE B O     1 
ATOM   7093 C CB    . PHE B 1 393 ? -20.147 -45.233 9.934   1.00 30.19 ? 393  PHE B CB    1 
ATOM   7094 C CG    . PHE B 1 393 ? -20.120 -45.176 11.434  1.00 28.11 ? 393  PHE B CG    1 
ATOM   7095 C CD1   . PHE B 1 393 ? -20.471 -44.022 12.096  1.00 27.37 ? 393  PHE B CD1   1 
ATOM   7096 C CD2   . PHE B 1 393 ? -19.730 -46.274 12.178  1.00 29.39 ? 393  PHE B CD2   1 
ATOM   7097 C CE1   . PHE B 1 393 ? -20.435 -43.960 13.471  1.00 25.52 ? 393  PHE B CE1   1 
ATOM   7098 C CE2   . PHE B 1 393 ? -19.702 -46.219 13.553  1.00 28.30 ? 393  PHE B CE2   1 
ATOM   7099 C CZ    . PHE B 1 393 ? -20.052 -45.059 14.199  1.00 26.87 ? 393  PHE B CZ    1 
ATOM   7100 N N     . SER B 1 394 ? -17.004 -43.711 10.246  1.00 27.86 ? 394  SER B N     1 
ATOM   7101 C CA    . SER B 1 394 ? -15.585 -43.905 10.492  1.00 28.12 ? 394  SER B CA    1 
ATOM   7102 C C     . SER B 1 394 ? -15.021 -43.248 11.762  1.00 26.94 ? 394  SER B C     1 
ATOM   7103 O O     . SER B 1 394 ? -14.115 -42.456 11.700  1.00 28.36 ? 394  SER B O     1 
ATOM   7104 C CB    . SER B 1 394 ? -14.827 -43.379 9.263   1.00 27.93 ? 394  SER B CB    1 
ATOM   7105 O OG    . SER B 1 394 ? -15.191 -42.083 8.886   1.00 27.32 ? 394  SER B OG    1 
ATOM   7106 N N     . PRO B 1 395 ? -15.559 -43.604 12.913  1.00 28.06 ? 395  PRO B N     1 
ATOM   7107 C CA    . PRO B 1 395 ? -15.068 -42.905 14.086  1.00 28.44 ? 395  PRO B CA    1 
ATOM   7108 C C     . PRO B 1 395 ? -13.627 -43.184 14.507  1.00 25.03 ? 395  PRO B C     1 
ATOM   7109 O O     . PRO B 1 395 ? -13.074 -44.212 14.174  1.00 24.65 ? 395  PRO B O     1 
ATOM   7110 C CB    . PRO B 1 395 ? -16.054 -43.353 15.163  1.00 31.10 ? 395  PRO B CB    1 
ATOM   7111 C CG    . PRO B 1 395 ? -16.408 -44.717 14.764  1.00 32.67 ? 395  PRO B CG    1 
ATOM   7112 C CD    . PRO B 1 395 ? -16.496 -44.672 13.276  1.00 30.17 ? 395  PRO B CD    1 
ATOM   7113 N N     . ILE B 1 396 ? -13.053 -42.262 15.266  1.00 24.35 ? 396  ILE B N     1 
ATOM   7114 C CA    . ILE B 1 396 ? -11.688 -42.402 15.740  1.00 24.42 ? 396  ILE B CA    1 
ATOM   7115 C C     . ILE B 1 396 ? -11.641 -42.870 17.188  1.00 25.75 ? 396  ILE B C     1 
ATOM   7116 O O     . ILE B 1 396 ? -12.407 -42.403 18.000  1.00 24.79 ? 396  ILE B O     1 
ATOM   7117 C CB    . ILE B 1 396 ? -10.876 -41.086 15.613  1.00 27.11 ? 396  ILE B CB    1 
ATOM   7118 C CG1   . ILE B 1 396 ? -11.087 -40.449 14.252  1.00 28.34 ? 396  ILE B CG1   1 
ATOM   7119 C CG2   . ILE B 1 396 ? -9.395  -41.303 15.851  1.00 28.26 ? 396  ILE B CG2   1 
ATOM   7120 C CD1   . ILE B 1 396 ? -10.352 -41.167 13.165  1.00 31.20 ? 396  ILE B CD1   1 
ATOM   7121 N N     . SER B 1 397 ? -10.709 -43.755 17.489  1.00 24.38 ? 397  SER B N     1 
ATOM   7122 C CA    . SER B 1 397 ? -10.589 -44.307 18.808  1.00 25.80 ? 397  SER B CA    1 
ATOM   7123 C C     . SER B 1 397 ? -9.139  -44.571 19.160  1.00 28.39 ? 397  SER B C     1 
ATOM   7124 O O     . SER B 1 397 ? -8.275  -44.521 18.306  1.00 26.36 ? 397  SER B O     1 
ATOM   7125 C CB    . SER B 1 397 ? -11.314 -45.656 18.820  1.00 24.82 ? 397  SER B CB    1 
ATOM   7126 O OG    . SER B 1 397 ? -10.787 -46.544 17.876  1.00 25.73 ? 397  SER B OG    1 
ATOM   7127 N N     . PRO B 1 398 ? -8.880  -44.864 20.439  1.00 26.94 ? 398  PRO B N     1 
ATOM   7128 C CA    . PRO B 1 398 ? -7.523  -45.277 20.760  1.00 29.20 ? 398  PRO B CA    1 
ATOM   7129 C C     . PRO B 1 398 ? -7.236  -46.626 20.112  1.00 28.26 ? 398  PRO B C     1 
ATOM   7130 O O     . PRO B 1 398 ? -8.124  -47.428 20.048  1.00 25.57 ? 398  PRO B O     1 
ATOM   7131 C CB    . PRO B 1 398 ? -7.550  -45.408 22.278  1.00 27.69 ? 398  PRO B CB    1 
ATOM   7132 C CG    . PRO B 1 398 ? -8.618  -44.497 22.717  1.00 28.45 ? 398  PRO B CG    1 
ATOM   7133 C CD    . PRO B 1 398 ? -9.662  -44.585 21.654  1.00 29.65 ? 398  PRO B CD    1 
ATOM   7134 N N     . PRO B 1 399 ? -6.005  -46.849 19.642  1.00 25.85 ? 399  PRO B N     1 
ATOM   7135 C CA    . PRO B 1 399 ? -5.599  -48.123 19.032  1.00 25.96 ? 399  PRO B CA    1 
ATOM   7136 C C     . PRO B 1 399 ? -5.350  -49.141 20.114  1.00 26.41 ? 399  PRO B C     1 
ATOM   7137 O O     . PRO B 1 399 ? -4.237  -49.576 20.299  1.00 25.73 ? 399  PRO B O     1 
ATOM   7138 C CB    . PRO B 1 399 ? -4.342  -47.763 18.259  1.00 26.79 ? 399  PRO B CB    1 
ATOM   7139 C CG    . PRO B 1 399 ? -3.807  -46.558 18.944  1.00 28.28 ? 399  PRO B CG    1 
ATOM   7140 C CD    . PRO B 1 399 ? -4.896  -45.894 19.725  1.00 26.96 ? 399  PRO B CD    1 
ATOM   7141 N N     . VAL B 1 400 ? -6.409  -49.515 20.809  1.00 28.30 ? 400  VAL B N     1 
ATOM   7142 C CA    . VAL B 1 400 ? -6.320  -50.419 21.927  1.00 29.58 ? 400  VAL B CA    1 
ATOM   7143 C C     . VAL B 1 400 ? -7.380  -51.488 21.701  1.00 28.71 ? 400  VAL B C     1 
ATOM   7144 O O     . VAL B 1 400 ? -8.488  -51.175 21.331  1.00 29.38 ? 400  VAL B O     1 
ATOM   7145 C CB    . VAL B 1 400 ? -6.579  -49.648 23.253  1.00 31.21 ? 400  VAL B CB    1 
ATOM   7146 C CG1   . VAL B 1 400 ? -6.614  -50.576 24.450  1.00 30.58 ? 400  VAL B CG1   1 
ATOM   7147 C CG2   . VAL B 1 400 ? -5.544  -48.554 23.474  1.00 30.60 ? 400  VAL B CG2   1 
ATOM   7148 N N     . GLY B 1 401 ? -7.021  -52.741 21.909  1.00 32.22 ? 401  GLY B N     1 
ATOM   7149 C CA    . GLY B 1 401 ? -7.929  -53.838 21.666  1.00 33.13 ? 401  GLY B CA    1 
ATOM   7150 C C     . GLY B 1 401 ? -9.285  -53.776 22.315  1.00 32.59 ? 401  GLY B C     1 
ATOM   7151 O O     . GLY B 1 401 ? -10.266 -54.101 21.702  1.00 27.28 ? 401  GLY B O     1 
ATOM   7152 N N     . ARG B 1 402 ? -9.319  -53.365 23.571  1.00 33.47 ? 402  ARG B N     1 
ATOM   7153 C CA    . ARG B 1 402 ? -10.589 -53.241 24.269  1.00 37.29 ? 402  ARG B CA    1 
ATOM   7154 C C     . ARG B 1 402 ? -11.530 -52.281 23.565  1.00 29.36 ? 402  ARG B C     1 
ATOM   7155 O O     . ARG B 1 402 ? -12.695 -52.555 23.434  1.00 29.00 ? 402  ARG B O     1 
ATOM   7156 C CB    . ARG B 1 402 ? -10.376 -52.832 25.720  1.00 42.54 ? 402  ARG B CB    1 
ATOM   7157 C CG    . ARG B 1 402 ? -11.601 -53.002 26.595  1.00 53.78 ? 402  ARG B CG    1 
ATOM   7158 C CD    . ARG B 1 402 ? -12.152 -51.664 27.051  1.00 64.85 ? 402  ARG B CD    1 
ATOM   7159 N NE    . ARG B 1 402 ? -11.085 -50.755 27.450  1.00 75.69 ? 402  ARG B NE    1 
ATOM   7160 C CZ    . ARG B 1 402 ? -11.111 -49.440 27.263  1.00 79.24 ? 402  ARG B CZ    1 
ATOM   7161 N NH1   . ARG B 1 402 ? -12.156 -48.866 26.683  1.00 70.95 ? 402  ARG B NH1   1 
ATOM   7162 N NH2   . ARG B 1 402 ? -10.088 -48.701 27.664  1.00 82.98 ? 402  ARG B NH2   1 
ATOM   7163 N N     . ASP B 1 403 ? -10.999 -51.174 23.089  1.00 27.45 ? 403  ASP B N     1 
ATOM   7164 C CA    . ASP B 1 403 ? -11.803 -50.194 22.382  1.00 26.63 ? 403  ASP B CA    1 
ATOM   7165 C C     . ASP B 1 403 ? -12.297 -50.735 21.055  1.00 24.47 ? 403  ASP B C     1 
ATOM   7166 O O     . ASP B 1 403 ? -13.414 -50.514 20.678  1.00 24.35 ? 403  ASP B O     1 
ATOM   7167 C CB    . ASP B 1 403 ? -10.980 -48.950 22.145  1.00 28.00 ? 403  ASP B CB    1 
ATOM   7168 C CG    . ASP B 1 403 ? -10.644 -48.213 23.422  1.00 29.07 ? 403  ASP B CG    1 
ATOM   7169 O OD1   . ASP B 1 403 ? -11.284 -47.199 23.712  1.00 28.87 ? 403  ASP B OD1   1 
ATOM   7170 O OD2   . ASP B 1 403 ? -9.731  -48.642 24.131  1.00 33.89 ? 403  ASP B OD2   1 
ATOM   7171 N N     . ALA B 1 404 ? -11.439 -51.452 20.358  1.00 28.01 ? 404  ALA B N     1 
ATOM   7172 C CA    . ALA B 1 404 ? -11.835 -52.081 19.097  1.00 27.92 ? 404  ALA B CA    1 
ATOM   7173 C C     . ALA B 1 404 ? -12.975 -53.049 19.304  1.00 26.85 ? 404  ALA B C     1 
ATOM   7174 O O     . ALA B 1 404 ? -13.911 -53.039 18.567  1.00 24.99 ? 404  ALA B O     1 
ATOM   7175 C CB    . ALA B 1 404 ? -10.673 -52.811 18.496  1.00 28.09 ? 404  ALA B CB    1 
ATOM   7176 N N     . MET B 1 405 ? -12.862 -53.884 20.321  1.00 27.25 ? 405  MET B N     1 
ATOM   7177 C CA    . MET B 1 405 ? -13.877 -54.880 20.598  1.00 29.67 ? 405  MET B CA    1 
ATOM   7178 C C     . MET B 1 405 ? -15.191 -54.234 20.965  1.00 28.68 ? 405  MET B C     1 
ATOM   7179 O O     . MET B 1 405 ? -16.218 -54.634 20.486  1.00 27.97 ? 405  MET B O     1 
ATOM   7180 C CB    . MET B 1 405 ? -13.411 -55.821 21.701  1.00 30.93 ? 405  MET B CB    1 
ATOM   7181 C CG    . MET B 1 405 ? -12.317 -56.772 21.292  1.00 33.29 ? 405  MET B CG    1 
ATOM   7182 S SD    . MET B 1 405 ? -12.850 -58.103 20.213  1.00 39.24 ? 405  MET B SD    1 
ATOM   7183 C CE    . MET B 1 405 ? -14.305 -58.669 21.069  1.00 41.32 ? 405  MET B CE    1 
ATOM   7184 N N     . LYS B 1 406 ? -15.139 -53.210 21.799  1.00 29.92 ? 406  LYS B N     1 
ATOM   7185 C CA    . LYS B 1 406 ? -16.341 -52.469 22.138  1.00 28.67 ? 406  LYS B CA    1 
ATOM   7186 C C     . LYS B 1 406 ? -17.015 -51.958 20.884  1.00 26.64 ? 406  LYS B C     1 
ATOM   7187 O O     . LYS B 1 406 ? -18.185 -52.146 20.697  1.00 26.75 ? 406  LYS B O     1 
ATOM   7188 C CB    . LYS B 1 406 ? -16.015 -51.300 23.073  1.00 31.20 ? 406  LYS B CB    1 
ATOM   7189 C CG    . LYS B 1 406 ? -17.225 -50.564 23.599  1.00 34.15 ? 406  LYS B CG    1 
ATOM   7190 C CD    . LYS B 1 406 ? -16.904 -49.848 24.890  1.00 40.44 ? 406  LYS B CD    1 
ATOM   7191 C CE    . LYS B 1 406 ? -16.082 -48.627 24.576  1.00 42.24 ? 406  LYS B CE    1 
ATOM   7192 N NZ    . LYS B 1 406 ? -15.597 -47.831 25.730  1.00 40.40 ? 406  LYS B NZ    1 
ATOM   7193 N N     . GLN B 1 407 ? -16.241 -51.351 20.005  1.00 27.75 ? 407  GLN B N     1 
ATOM   7194 C CA    . GLN B 1 407 ? -16.797 -50.796 18.798  1.00 28.34 ? 407  GLN B CA    1 
ATOM   7195 C C     . GLN B 1 407 ? -17.354 -51.850 17.862  1.00 25.81 ? 407  GLN B C     1 
ATOM   7196 O O     . GLN B 1 407 ? -18.415 -51.681 17.347  1.00 28.53 ? 407  GLN B O     1 
ATOM   7197 C CB    . GLN B 1 407 ? -15.742 -49.973 18.095  1.00 27.51 ? 407  GLN B CB    1 
ATOM   7198 C CG    . GLN B 1 407 ? -15.431 -48.665 18.777  1.00 26.44 ? 407  GLN B CG    1 
ATOM   7199 C CD    . GLN B 1 407 ? -14.192 -48.015 18.220  1.00 26.13 ? 407  GLN B CD    1 
ATOM   7200 O OE1   . GLN B 1 407 ? -13.090 -48.308 18.649  1.00 30.15 ? 407  GLN B OE1   1 
ATOM   7201 N NE2   . GLN B 1 407 ? -14.371 -47.140 17.251  1.00 23.06 ? 407  GLN B NE2   1 
ATOM   7202 N N     . PHE B 1 408 ? -16.614 -52.916 17.648  1.00 27.19 ? 408  PHE B N     1 
ATOM   7203 C CA    . PHE B 1 408 ? -17.059 -54.027 16.814  1.00 29.38 ? 408  PHE B CA    1 
ATOM   7204 C C     . PHE B 1 408 ? -18.434 -54.489 17.249  1.00 28.29 ? 408  PHE B C     1 
ATOM   7205 O O     . PHE B 1 408 ? -19.351 -54.545 16.468  1.00 28.40 ? 408  PHE B O     1 
ATOM   7206 C CB    . PHE B 1 408 ? -16.006 -55.124 16.954  1.00 28.68 ? 408  PHE B CB    1 
ATOM   7207 C CG    . PHE B 1 408 ? -16.423 -56.496 16.506  1.00 29.01 ? 408  PHE B CG    1 
ATOM   7208 C CD1   . PHE B 1 408 ? -17.007 -56.714 15.283  1.00 31.46 ? 408  PHE B CD1   1 
ATOM   7209 C CD2   . PHE B 1 408 ? -16.144 -57.587 17.301  1.00 33.84 ? 408  PHE B CD2   1 
ATOM   7210 C CE1   . PHE B 1 408 ? -17.357 -57.979 14.881  1.00 31.14 ? 408  PHE B CE1   1 
ATOM   7211 C CE2   . PHE B 1 408 ? -16.489 -58.856 16.905  1.00 33.42 ? 408  PHE B CE2   1 
ATOM   7212 C CZ    . PHE B 1 408 ? -17.093 -59.050 15.691  1.00 32.52 ? 408  PHE B CZ    1 
ATOM   7213 N N     . ARG B 1 409 ? -18.566 -54.754 18.525  1.00 30.35 ? 409  ARG B N     1 
ATOM   7214 C CA    . ARG B 1 409 ? -19.834 -55.228 19.047  1.00 33.78 ? 409  ARG B CA    1 
ATOM   7215 C C     . ARG B 1 409 ? -20.967 -54.218 18.985  1.00 32.75 ? 409  ARG B C     1 
ATOM   7216 O O     . ARG B 1 409 ? -22.034 -54.549 18.541  1.00 31.60 ? 409  ARG B O     1 
ATOM   7217 C CB    . ARG B 1 409 ? -19.623 -55.753 20.449  1.00 37.59 ? 409  ARG B CB    1 
ATOM   7218 C CG    . ARG B 1 409 ? -18.572 -56.841 20.502  1.00 44.89 ? 409  ARG B CG    1 
ATOM   7219 C CD    . ARG B 1 409 ? -18.785 -57.823 21.637  1.00 48.98 ? 409  ARG B CD    1 
ATOM   7220 N NE    . ARG B 1 409 ? -17.818 -58.910 21.558  1.00 53.78 ? 409  ARG B NE    1 
ATOM   7221 C CZ    . ARG B 1 409 ? -17.996 -60.030 20.863  1.00 59.09 ? 409  ARG B CZ    1 
ATOM   7222 N NH1   . ARG B 1 409 ? -19.122 -60.230 20.199  1.00 58.62 ? 409  ARG B NH1   1 
ATOM   7223 N NH2   . ARG B 1 409 ? -17.049 -60.957 20.842  1.00 56.65 ? 409  ARG B NH2   1 
ATOM   7224 N N     . MET B 1 410 ? -20.715 -52.982 19.397  1.00 31.18 ? 410  MET B N     1 
ATOM   7225 C CA    . MET B 1 410 ? -21.720 -51.928 19.354  1.00 32.61 ? 410  MET B CA    1 
ATOM   7226 C C     . MET B 1 410 ? -22.266 -51.729 17.960  1.00 29.53 ? 410  MET B C     1 
ATOM   7227 O O     . MET B 1 410 ? -23.450 -51.643 17.765  1.00 30.13 ? 410  MET B O     1 
ATOM   7228 C CB    . MET B 1 410 ? -21.070 -50.601 19.724  1.00 36.88 ? 410  MET B CB    1 
ATOM   7229 C CG    . MET B 1 410 ? -20.763 -50.312 21.164  1.00 43.08 ? 410  MET B CG    1 
ATOM   7230 S SD    . MET B 1 410 ? -19.661 -48.890 21.114  1.00 38.62 ? 410  MET B SD    1 
ATOM   7231 C CE    . MET B 1 410 ? -20.867 -47.587 21.016  1.00 36.12 ? 410  MET B CE    1 
ATOM   7232 N N     . VAL B 1 411 ? -21.366 -51.616 16.993  1.00 28.85 ? 411  VAL B N     1 
ATOM   7233 C CA    . VAL B 1 411 ? -21.762 -51.365 15.626  1.00 28.02 ? 411  VAL B CA    1 
ATOM   7234 C C     . VAL B 1 411 ? -22.495 -52.565 15.001  1.00 30.07 ? 411  VAL B C     1 
ATOM   7235 O O     . VAL B 1 411 ? -23.538 -52.401 14.411  1.00 30.17 ? 411  VAL B O     1 
ATOM   7236 C CB    . VAL B 1 411 ? -20.548 -50.896 14.778  1.00 28.62 ? 411  VAL B CB    1 
ATOM   7237 C CG1   . VAL B 1 411 ? -20.915 -50.713 13.318  1.00 31.88 ? 411  VAL B CG1   1 
ATOM   7238 C CG2   . VAL B 1 411 ? -19.996 -49.595 15.332  1.00 31.03 ? 411  VAL B CG2   1 
ATOM   7239 N N     . ARG B 1 412 ? -21.948 -53.757 15.166  1.00 30.05 ? 412  ARG B N     1 
ATOM   7240 C CA    . ARG B 1 412 ? -22.582 -54.944 14.606  1.00 33.88 ? 412  ARG B CA    1 
ATOM   7241 C C     . ARG B 1 412 ? -23.964 -55.169 15.195  1.00 32.90 ? 412  ARG B C     1 
ATOM   7242 O O     . ARG B 1 412 ? -24.876 -55.498 14.484  1.00 31.98 ? 412  ARG B O     1 
ATOM   7243 C CB    . ARG B 1 412 ? -21.730 -56.196 14.798  1.00 32.18 ? 412  ARG B CB    1 
ATOM   7244 C CG    . ARG B 1 412 ? -22.247 -57.384 14.012  1.00 34.41 ? 412  ARG B CG    1 
ATOM   7245 C CD    . ARG B 1 412 ? -21.304 -58.558 14.070  1.00 33.52 ? 412  ARG B CD    1 
ATOM   7246 N NE    . ARG B 1 412 ? -21.079 -58.993 15.436  1.00 33.01 ? 412  ARG B NE    1 
ATOM   7247 C CZ    . ARG B 1 412 ? -20.501 -60.138 15.761  1.00 32.02 ? 412  ARG B CZ    1 
ATOM   7248 N NH1   . ARG B 1 412 ? -20.092 -60.965 14.816  1.00 34.38 ? 412  ARG B NH1   1 
ATOM   7249 N NH2   . ARG B 1 412 ? -20.328 -60.448 17.031  1.00 33.08 ? 412  ARG B NH2   1 
ATOM   7250 N N     . SER B 1 413 ? -24.095 -54.956 16.496  1.00 34.28 ? 413  SER B N     1 
ATOM   7251 C CA    . SER B 1 413 ? -25.367 -55.169 17.149  1.00 38.20 ? 413  SER B CA    1 
ATOM   7252 C C     . SER B 1 413 ? -26.437 -54.266 16.571  1.00 37.51 ? 413  SER B C     1 
ATOM   7253 O O     . SER B 1 413 ? -27.519 -54.721 16.250  1.00 30.04 ? 413  SER B O     1 
ATOM   7254 C CB    . SER B 1 413 ? -25.269 -55.038 18.668  1.00 38.68 ? 413  SER B CB    1 
ATOM   7255 O OG    . SER B 1 413 ? -24.925 -53.736 19.058  1.00 48.13 ? 413  SER B OG    1 
ATOM   7256 N N     . ARG B 1 414 ? -26.093 -52.995 16.375  1.00 32.76 ? 414  ARG B N     1 
ATOM   7257 C CA    . ARG B 1 414 ? -27.036 -52.073 15.817  1.00 29.90 ? 414  ARG B CA    1 
ATOM   7258 C C     . ARG B 1 414 ? -27.280 -52.336 14.346  1.00 30.94 ? 414  ARG B C     1 
ATOM   7259 O O     . ARG B 1 414 ? -28.369 -52.205 13.877  1.00 29.95 ? 414  ARG B O     1 
ATOM   7260 C CB    . ARG B 1 414 ? -26.595 -50.640 16.056  1.00 33.61 ? 414  ARG B CB    1 
ATOM   7261 C CG    . ARG B 1 414 ? -26.518 -50.229 17.513  1.00 32.82 ? 414  ARG B CG    1 
ATOM   7262 C CD    . ARG B 1 414 ? -27.768 -50.598 18.287  1.00 32.67 ? 414  ARG B CD    1 
ATOM   7263 N NE    . ARG B 1 414 ? -27.774 -49.996 19.612  1.00 34.70 ? 414  ARG B NE    1 
ATOM   7264 C CZ    . ARG B 1 414 ? -28.866 -49.813 20.345  1.00 41.87 ? 414  ARG B CZ    1 
ATOM   7265 N NH1   . ARG B 1 414 ? -30.046 -50.182 19.882  1.00 39.55 ? 414  ARG B NH1   1 
ATOM   7266 N NH2   . ARG B 1 414 ? -28.783 -49.261 21.545  1.00 38.42 ? 414  ARG B NH2   1 
ATOM   7267 N N     . ALA B 1 415 ? -26.242 -52.688 13.617  1.00 31.07 ? 415  ALA B N     1 
ATOM   7268 C CA    . ALA B 1 415 ? -26.415 -53.022 12.219  1.00 30.27 ? 415  ALA B CA    1 
ATOM   7269 C C     . ALA B 1 415 ? -27.424 -54.160 12.089  1.00 30.72 ? 415  ALA B C     1 
ATOM   7270 O O     . ALA B 1 415 ? -28.316 -54.077 11.284  1.00 34.10 ? 415  ALA B O     1 
ATOM   7271 C CB    . ALA B 1 415 ? -25.091 -53.385 11.586  1.00 30.38 ? 415  ALA B CB    1 
ATOM   7272 N N     . ASP B 1 416 ? -27.276 -55.204 12.886  1.00 32.40 ? 416  ASP B N     1 
ATOM   7273 C CA    . ASP B 1 416 ? -28.227 -56.319 12.887  1.00 36.52 ? 416  ASP B CA    1 
ATOM   7274 C C     . ASP B 1 416 ? -29.653 -55.838 13.139  1.00 38.01 ? 416  ASP B C     1 
ATOM   7275 O O     . ASP B 1 416 ? -30.563 -56.202 12.433  1.00 34.90 ? 416  ASP B O     1 
ATOM   7276 C CB    . ASP B 1 416 ? -27.850 -57.307 13.975  1.00 35.94 ? 416  ASP B CB    1 
ATOM   7277 C CG    . ASP B 1 416 ? -26.624 -58.129 13.638  1.00 37.62 ? 416  ASP B CG    1 
ATOM   7278 O OD1   . ASP B 1 416 ? -26.204 -58.149 12.472  1.00 38.02 ? 416  ASP B OD1   1 
ATOM   7279 O OD2   . ASP B 1 416 ? -26.075 -58.762 14.558  1.00 38.36 ? 416  ASP B OD2   1 
ATOM   7280 N N     . GLU B 1 417 ? -29.822 -55.009 14.149  1.00 36.95 ? 417  GLU B N     1 
ATOM   7281 C CA    . GLU B 1 417 ? -31.122 -54.453 14.476  1.00 37.89 ? 417  GLU B CA    1 
ATOM   7282 C C     . GLU B 1 417 ? -31.714 -53.666 13.335  1.00 39.48 ? 417  GLU B C     1 
ATOM   7283 O O     . GLU B 1 417 ? -32.905 -53.722 13.103  1.00 38.50 ? 417  GLU B O     1 
ATOM   7284 C CB    . GLU B 1 417 ? -30.946 -53.592 15.722  1.00 41.21 ? 417  GLU B CB    1 
ATOM   7285 C CG    . GLU B 1 417 ? -32.143 -52.844 16.260  1.00 42.38 ? 417  GLU B CG    1 
ATOM   7286 C CD    . GLU B 1 417 ? -31.798 -52.126 17.549  1.00 45.18 ? 417  GLU B CD    1 
ATOM   7287 O OE1   . GLU B 1 417 ? -32.615 -51.325 18.037  1.00 46.30 ? 417  GLU B OE1   1 
ATOM   7288 O OE2   . GLU B 1 417 ? -30.702 -52.378 18.079  1.00 44.20 ? 417  GLU B OE2   1 
ATOM   7289 N N     . TYR B 1 418 ? -30.877 -52.968 12.588  1.00 34.65 ? 418  TYR B N     1 
ATOM   7290 C CA    . TYR B 1 418 ? -31.337 -52.142 11.493  1.00 33.94 ? 418  TYR B CA    1 
ATOM   7291 C C     . TYR B 1 418 ? -31.211 -52.832 10.142  1.00 31.84 ? 418  TYR B C     1 
ATOM   7292 O O     . TYR B 1 418 ? -31.319 -52.179 9.125   1.00 32.69 ? 418  TYR B O     1 
ATOM   7293 C CB    . TYR B 1 418 ? -30.656 -50.771 11.534  1.00 33.86 ? 418  TYR B CB    1 
ATOM   7294 C CG    . TYR B 1 418 ? -31.191 -49.865 12.610  1.00 32.46 ? 418  TYR B CG    1 
ATOM   7295 C CD1   . TYR B 1 418 ? -30.842 -50.051 13.934  1.00 33.18 ? 418  TYR B CD1   1 
ATOM   7296 C CD2   . TYR B 1 418 ? -32.049 -48.832 12.305  1.00 34.02 ? 418  TYR B CD2   1 
ATOM   7297 C CE1   . TYR B 1 418 ? -31.336 -49.242 14.924  1.00 33.66 ? 418  TYR B CE1   1 
ATOM   7298 C CE2   . TYR B 1 418 ? -32.544 -48.010 13.291  1.00 37.67 ? 418  TYR B CE2   1 
ATOM   7299 C CZ    . TYR B 1 418 ? -32.181 -48.221 14.599  1.00 34.61 ? 418  TYR B CZ    1 
ATOM   7300 O OH    . TYR B 1 418 ? -32.669 -47.406 15.585  1.00 44.02 ? 418  TYR B OH    1 
ATOM   7301 N N     . ALA B 1 419 ? -31.008 -54.140 10.157  1.00 32.18 ? 419  ALA B N     1 
ATOM   7302 C CA    . ALA B 1 419 ? -30.947 -54.942 8.937   1.00 35.37 ? 419  ALA B CA    1 
ATOM   7303 C C     . ALA B 1 419 ? -29.859 -54.623 7.936   1.00 34.65 ? 419  ALA B C     1 
ATOM   7304 O O     . ALA B 1 419 ? -30.074 -54.709 6.747   1.00 35.12 ? 419  ALA B O     1 
ATOM   7305 C CB    . ALA B 1 419 ? -32.315 -55.018 8.275   1.00 37.05 ? 419  ALA B CB    1 
ATOM   7306 N N     . LYS B 1 420 ? -28.689 -54.261 8.428   1.00 35.14 ? 420  LYS B N     1 
ATOM   7307 C CA    . LYS B 1 420 ? -27.561 -53.985 7.558   1.00 34.16 ? 420  LYS B CA    1 
ATOM   7308 C C     . LYS B 1 420 ? -26.401 -54.892 7.939   1.00 32.45 ? 420  LYS B C     1 
ATOM   7309 O O     . LYS B 1 420 ? -26.181 -55.165 9.092   1.00 32.30 ? 420  LYS B O     1 
ATOM   7310 C CB    . LYS B 1 420 ? -27.164 -52.531 7.643   1.00 33.96 ? 420  LYS B CB    1 
ATOM   7311 C CG    . LYS B 1 420 ? -28.288 -51.535 7.404   1.00 32.34 ? 420  LYS B CG    1 
ATOM   7312 C CD    . LYS B 1 420 ? -28.759 -51.553 5.965   1.00 35.66 ? 420  LYS B CD    1 
ATOM   7313 C CE    . LYS B 1 420 ? -30.165 -50.995 5.822   1.00 36.13 ? 420  LYS B CE    1 
ATOM   7314 N NZ    . LYS B 1 420 ? -31.225 -51.927 6.269   1.00 37.85 ? 420  LYS B NZ    1 
ATOM   7315 N N     . ASP B 1 421 ? -25.684 -55.392 6.949   1.00 51.03 ? 421  ASP B N     1 
ATOM   7316 C CA    . ASP B 1 421 ? -24.539 -56.234 7.228   1.00 43.21 ? 421  ASP B CA    1 
ATOM   7317 C C     . ASP B 1 421 ? -23.382 -55.461 7.845   1.00 38.27 ? 421  ASP B C     1 
ATOM   7318 O O     . ASP B 1 421 ? -23.187 -54.303 7.558   1.00 35.19 ? 421  ASP B O     1 
ATOM   7319 C CB    . ASP B 1 421 ? -24.033 -56.952 6.004   1.00 46.73 ? 421  ASP B CB    1 
ATOM   7320 C CG    . ASP B 1 421 ? -25.049 -57.854 5.390   1.00 37.51 ? 421  ASP B CG    1 
ATOM   7321 O OD1   . ASP B 1 421 ? -25.814 -58.502 6.118   1.00 45.34 ? 421  ASP B OD1   1 
ATOM   7322 O OD2   . ASP B 1 421 ? -25.060 -57.922 4.160   1.00 36.31 ? 421  ASP B OD2   1 
ATOM   7323 N N     . TYR B 1 422 ? -22.634 -56.127 8.701   1.00 33.55 ? 422  TYR B N     1 
ATOM   7324 C CA    . TYR B 1 422 ? -21.454 -55.504 9.272   1.00 32.17 ? 422  TYR B CA    1 
ATOM   7325 C C     . TYR B 1 422 ? -20.280 -55.799 8.400   1.00 27.29 ? 422  TYR B C     1 
ATOM   7326 O O     . TYR B 1 422 ? -19.801 -56.912 8.376   1.00 29.44 ? 422  TYR B O     1 
ATOM   7327 C CB    . TYR B 1 422 ? -21.210 -55.977 10.693  1.00 30.76 ? 422  TYR B CB    1 
ATOM   7328 C CG    . TYR B 1 422 ? -19.959 -55.472 11.335  1.00 29.50 ? 422  TYR B CG    1 
ATOM   7329 C CD1   . TYR B 1 422 ? -19.879 -54.183 11.818  1.00 27.98 ? 422  TYR B CD1   1 
ATOM   7330 C CD2   . TYR B 1 422 ? -18.863 -56.295 11.479  1.00 29.45 ? 422  TYR B CD2   1 
ATOM   7331 C CE1   . TYR B 1 422 ? -18.729 -53.724 12.415  1.00 27.79 ? 422  TYR B CE1   1 
ATOM   7332 C CE2   . TYR B 1 422 ? -17.710 -55.841 12.054  1.00 30.86 ? 422  TYR B CE2   1 
ATOM   7333 C CZ    . TYR B 1 422 ? -17.651 -54.559 12.532  1.00 28.55 ? 422  TYR B CZ    1 
ATOM   7334 O OH    . TYR B 1 422 ? -16.496 -54.125 13.113  1.00 30.99 ? 422  TYR B OH    1 
ATOM   7335 N N     . ALA B 1 423 ? -19.862 -54.803 7.664   1.00 27.73 ? 423  ALA B N     1 
ATOM   7336 C CA    . ALA B 1 423 ? -18.701 -54.919 6.840   1.00 31.00 ? 423  ALA B CA    1 
ATOM   7337 C C     . ALA B 1 423 ? -17.851 -53.787 7.340   1.00 30.41 ? 423  ALA B C     1 
ATOM   7338 O O     . ALA B 1 423 ? -18.239 -52.648 7.232   1.00 30.86 ? 423  ALA B O     1 
ATOM   7339 C CB    . ALA B 1 423 ? -19.042 -54.678 5.402   1.00 29.32 ? 423  ALA B CB    1 
ATOM   7340 N N     . ALA B 1 424 ? -16.692 -54.118 7.857   1.00 29.27 ? 424  ALA B N     1 
ATOM   7341 C CA    . ALA B 1 424 ? -15.864 -53.098 8.428   1.00 29.53 ? 424  ALA B CA    1 
ATOM   7342 C C     . ALA B 1 424 ? -14.418 -53.421 8.569   1.00 28.88 ? 424  ALA B C     1 
ATOM   7343 O O     . ALA B 1 424 ? -14.029 -54.564 8.550   1.00 29.06 ? 424  ALA B O     1 
ATOM   7344 C CB    . ALA B 1 424 ? -16.398 -52.707 9.777   1.00 27.50 ? 424  ALA B CB    1 
ATOM   7345 N N     . GLN B 1 425 ? -13.635 -52.384 8.759   1.00 28.89 ? 425  GLN B N     1 
ATOM   7346 C CA    . GLN B 1 425 ? -12.237 -52.553 8.971   1.00 29.28 ? 425  GLN B CA    1 
ATOM   7347 C C     . GLN B 1 425 ? -11.690 -51.667 10.065  1.00 29.57 ? 425  GLN B C     1 
ATOM   7348 O O     . GLN B 1 425 ? -12.258 -50.648 10.378  1.00 30.01 ? 425  GLN B O     1 
ATOM   7349 C CB    . GLN B 1 425 ? -11.442 -52.269 7.704   1.00 30.33 ? 425  GLN B CB    1 
ATOM   7350 C CG    . GLN B 1 425 ? -11.573 -50.878 7.147   1.00 29.65 ? 425  GLN B CG    1 
ATOM   7351 C CD    . GLN B 1 425 ? -10.738 -50.701 5.908   1.00 29.09 ? 425  GLN B CD    1 
ATOM   7352 O OE1   . GLN B 1 425 ? -9.600  -51.132 5.853   1.00 32.11 ? 425  GLN B OE1   1 
ATOM   7353 N NE2   . GLN B 1 425 ? -11.308 -50.074 4.907   1.00 34.89 ? 425  GLN B NE2   1 
ATOM   7354 N N     . PHE B 1 426 ? -10.602 -52.100 10.667  1.00 28.45 ? 426  PHE B N     1 
ATOM   7355 C CA    . PHE B 1 426 ? -9.931  -51.269 11.643  1.00 28.67 ? 426  PHE B CA    1 
ATOM   7356 C C     . PHE B 1 426 ? -8.607  -50.844 11.026  1.00 29.65 ? 426  PHE B C     1 
ATOM   7357 O O     . PHE B 1 426 ? -7.889  -51.660 10.487  1.00 29.12 ? 426  PHE B O     1 
ATOM   7358 C CB    . PHE B 1 426 ? -9.754  -51.977 12.961  1.00 28.21 ? 426  PHE B CB    1 
ATOM   7359 C CG    . PHE B 1 426 ? -11.002 -52.043 13.785  1.00 31.44 ? 426  PHE B CG    1 
ATOM   7360 C CD1   . PHE B 1 426 ? -11.876 -53.104 13.653  1.00 31.25 ? 426  PHE B CD1   1 
ATOM   7361 C CD2   . PHE B 1 426 ? -11.297 -51.050 14.693  1.00 29.28 ? 426  PHE B CD2   1 
ATOM   7362 C CE1   . PHE B 1 426 ? -13.022 -53.168 14.409  1.00 31.82 ? 426  PHE B CE1   1 
ATOM   7363 C CE2   . PHE B 1 426 ? -12.438 -51.109 15.454  1.00 31.44 ? 426  PHE B CE2   1 
ATOM   7364 C CZ    . PHE B 1 426 ? -13.301 -52.172 15.314  1.00 32.20 ? 426  PHE B CZ    1 
ATOM   7365 N N     . VAL B 1 427 ? -8.313  -49.558 11.079  1.00 29.43 ? 427  VAL B N     1 
ATOM   7366 C CA    . VAL B 1 427 ? -7.106  -49.011 10.470  1.00 30.00 ? 427  VAL B CA    1 
ATOM   7367 C C     . VAL B 1 427 ? -6.318  -48.179 11.463  1.00 29.70 ? 427  VAL B C     1 
ATOM   7368 O O     . VAL B 1 427 ? -6.885  -47.371 12.146  1.00 29.24 ? 427  VAL B O     1 
ATOM   7369 C CB    . VAL B 1 427 ? -7.491  -48.122 9.283   1.00 32.48 ? 427  VAL B CB    1 
ATOM   7370 C CG1   . VAL B 1 427 ? -6.316  -47.360 8.723   1.00 33.87 ? 427  VAL B CG1   1 
ATOM   7371 C CG2   . VAL B 1 427 ? -8.162  -48.936 8.196   1.00 35.18 ? 427  VAL B CG2   1 
ATOM   7372 N N     . VAL B 1 428 ? -5.021  -48.430 11.579  1.00 32.70 ? 428  VAL B N     1 
ATOM   7373 C CA    . VAL B 1 428 ? -4.199  -47.593 12.431  1.00 34.75 ? 428  VAL B CA    1 
ATOM   7374 C C     . VAL B 1 428 ? -3.264  -46.675 11.627  1.00 31.63 ? 428  VAL B C     1 
ATOM   7375 O O     . VAL B 1 428 ? -2.436  -47.115 10.868  1.00 26.95 ? 428  VAL B O     1 
ATOM   7376 C CB    . VAL B 1 428 ? -3.594  -48.288 13.689  1.00 41.00 ? 428  VAL B CB    1 
ATOM   7377 C CG1   . VAL B 1 428 ? -4.605  -49.154 14.410  1.00 38.80 ? 428  VAL B CG1   1 
ATOM   7378 C CG2   . VAL B 1 428 ? -2.303  -49.013 13.435  1.00 50.77 ? 428  VAL B CG2   1 
ATOM   7379 N N     . GLY B 1 429 ? -3.479  -45.381 11.773  1.00 29.46 ? 429  GLY B N     1 
ATOM   7380 C CA    . GLY B 1 429 ? -2.649  -44.438 11.065  1.00 31.10 ? 429  GLY B CA    1 
ATOM   7381 C C     . GLY B 1 429 ? -1.280  -44.431 11.672  1.00 30.59 ? 429  GLY B C     1 
ATOM   7382 O O     . GLY B 1 429 ? -0.344  -44.809 11.016  1.00 32.07 ? 429  GLY B O     1 
ATOM   7383 N N     . LEU B 1 430 ? -1.173  -44.019 12.922  1.00 29.98 ? 430  LEU B N     1 
ATOM   7384 C CA    . LEU B 1 430 ? 0.077   -44.036 13.636  1.00 27.88 ? 430  LEU B CA    1 
ATOM   7385 C C     . LEU B 1 430 ? -0.232  -44.277 15.102  1.00 27.96 ? 430  LEU B C     1 
ATOM   7386 O O     . LEU B 1 430 ? 0.184   -45.262 15.661  1.00 33.45 ? 430  LEU B O     1 
ATOM   7387 C CB    . LEU B 1 430 ? 0.779   -42.692 13.487  1.00 30.27 ? 430  LEU B CB    1 
ATOM   7388 C CG    . LEU B 1 430 ? 2.227   -42.642 13.952  1.00 29.64 ? 430  LEU B CG    1 
ATOM   7389 C CD1   . LEU B 1 430 ? 3.032   -43.612 13.117  1.00 29.00 ? 430  LEU B CD1   1 
ATOM   7390 C CD2   . LEU B 1 430 ? 2.775   -41.234 13.827  1.00 30.95 ? 430  LEU B CD2   1 
ATOM   7391 N N     . ARG B 1 431 ? -0.963  -43.361 15.714  1.00 28.37 ? 431  ARG B N     1 
ATOM   7392 C CA    . ARG B 1 431 ? -1.342  -43.470 17.121  1.00 24.82 ? 431  ARG B CA    1 
ATOM   7393 C C     . ARG B 1 431 ? -2.850  -43.462 17.277  1.00 24.37 ? 431  ARG B C     1 
ATOM   7394 O O     . ARG B 1 431 ? -3.331  -43.419 18.368  1.00 23.11 ? 431  ARG B O     1 
ATOM   7395 C CB    . ARG B 1 431 ? -0.852  -42.240 17.870  1.00 28.11 ? 431  ARG B CB    1 
ATOM   7396 C CG    . ARG B 1 431 ? 0.612   -42.140 18.092  1.00 27.49 ? 431  ARG B CG    1 
ATOM   7397 C CD    . ARG B 1 431 ? 0.911   -40.843 18.801  1.00 22.98 ? 431  ARG B CD    1 
ATOM   7398 N NE    . ARG B 1 431 ? 2.238   -40.928 19.352  1.00 24.08 ? 431  ARG B NE    1 
ATOM   7399 C CZ    . ARG B 1 431 ? 3.329   -40.670 18.658  1.00 24.73 ? 431  ARG B CZ    1 
ATOM   7400 N NH1   . ARG B 1 431 ? 3.228   -40.268 17.403  1.00 22.79 ? 431  ARG B NH1   1 
ATOM   7401 N NH2   . ARG B 1 431 ? 4.509   -40.783 19.230  1.00 27.23 ? 431  ARG B NH2   1 
ATOM   7402 N N     . GLU B 1 432 ? -3.566  -43.439 16.170  1.00 26.36 ? 432  GLU B N     1 
ATOM   7403 C CA    . GLU B 1 432 ? -5.009  -43.412 16.181  1.00 26.44 ? 432  GLU B CA    1 
ATOM   7404 C C     . GLU B 1 432 ? -5.622  -44.551 15.396  1.00 28.33 ? 432  GLU B C     1 
ATOM   7405 O O     . GLU B 1 432 ? -5.024  -45.050 14.468  1.00 26.08 ? 432  GLU B O     1 
ATOM   7406 C CB    . GLU B 1 432 ? -5.511  -42.089 15.603  1.00 27.38 ? 432  GLU B CB    1 
ATOM   7407 C CG    . GLU B 1 432 ? -5.812  -42.025 14.114  1.00 27.96 ? 432  GLU B CG    1 
ATOM   7408 C CD    . GLU B 1 432 ? -4.588  -42.093 13.206  1.00 28.08 ? 432  GLU B CD    1 
ATOM   7409 O OE1   . GLU B 1 432 ? -4.785  -42.067 11.989  1.00 28.93 ? 432  GLU B OE1   1 
ATOM   7410 O OE2   . GLU B 1 432 ? -3.442  -42.175 13.674  1.00 26.83 ? 432  GLU B OE2   1 
ATOM   7411 N N     . MET B 1 433 ? -6.824  -44.946 15.790  1.00 28.92 ? 433  MET B N     1 
ATOM   7412 C CA    . MET B 1 433 ? -7.539  -46.007 15.109  1.00 30.98 ? 433  MET B CA    1 
ATOM   7413 C C     . MET B 1 433 ? -8.820  -45.559 14.460  1.00 28.07 ? 433  MET B C     1 
ATOM   7414 O O     . MET B 1 433 ? -9.527  -44.774 15.014  1.00 28.24 ? 433  MET B O     1 
ATOM   7415 C CB    . MET B 1 433 ? -7.889  -47.132 16.083  1.00 30.92 ? 433  MET B CB    1 
ATOM   7416 C CG    . MET B 1 433 ? -8.326  -48.423 15.426  1.00 32.98 ? 433  MET B CG    1 
ATOM   7417 S SD    . MET B 1 433 ? -8.163  -49.840 16.505  1.00 30.24 ? 433  MET B SD    1 
ATOM   7418 C CE    . MET B 1 433 ? -9.330  -49.450 17.790  1.00 30.80 ? 433  MET B CE    1 
ATOM   7419 N N     . HIS B 1 434 ? -9.101  -46.092 13.289  1.00 25.12 ? 434  HIS B N     1 
ATOM   7420 C CA    . HIS B 1 434 ? -10.314 -45.796 12.595  1.00 27.88 ? 434  HIS B CA    1 
ATOM   7421 C C     . HIS B 1 434 ? -11.156 -47.069 12.460  1.00 28.49 ? 434  HIS B C     1 
ATOM   7422 O O     . HIS B 1 434 ? -10.630 -48.104 12.135  1.00 28.45 ? 434  HIS B O     1 
ATOM   7423 C CB    . HIS B 1 434 ? -10.033 -45.285 11.177  1.00 28.79 ? 434  HIS B CB    1 
ATOM   7424 C CG    . HIS B 1 434 ? -9.004  -44.200 11.088  1.00 30.03 ? 434  HIS B CG    1 
ATOM   7425 N ND1   . HIS B 1 434 ? -9.267  -42.984 10.500  1.00 36.65 ? 434  HIS B ND1   1 
ATOM   7426 C CD2   . HIS B 1 434 ? -7.699  -44.161 11.444  1.00 31.77 ? 434  HIS B CD2   1 
ATOM   7427 C CE1   . HIS B 1 434 ? -8.187  -42.232 10.534  1.00 34.09 ? 434  HIS B CE1   1 
ATOM   7428 N NE2   . HIS B 1 434 ? -7.223  -42.922 11.104  1.00 33.17 ? 434  HIS B NE2   1 
ATOM   7429 N N     . HIS B 1 435 ? -12.446 -46.972 12.714  1.00 26.58 ? 435  HIS B N     1 
ATOM   7430 C CA    . HIS B 1 435 ? -13.351 -48.093 12.527  1.00 28.29 ? 435  HIS B CA    1 
ATOM   7431 C C     . HIS B 1 435 ? -14.171 -47.677 11.337  1.00 28.67 ? 435  HIS B C     1 
ATOM   7432 O O     . HIS B 1 435 ? -15.114 -46.957 11.481  1.00 24.70 ? 435  HIS B O     1 
ATOM   7433 C CB    . HIS B 1 435 ? -14.231 -48.318 13.748  1.00 29.93 ? 435  HIS B CB    1 
ATOM   7434 C CG    . HIS B 1 435 ? -15.114 -49.518 13.658  1.00 29.59 ? 435  HIS B CG    1 
ATOM   7435 N ND1   . HIS B 1 435 ? -16.153 -49.735 14.533  1.00 27.44 ? 435  HIS B ND1   1 
ATOM   7436 C CD2   . HIS B 1 435 ? -15.111 -50.570 12.809  1.00 28.54 ? 435  HIS B CD2   1 
ATOM   7437 C CE1   . HIS B 1 435 ? -16.752 -50.866 14.227  1.00 27.49 ? 435  HIS B CE1   1 
ATOM   7438 N NE2   . HIS B 1 435 ? -16.142 -51.391 13.185  1.00 30.17 ? 435  HIS B NE2   1 
ATOM   7439 N N     . ILE B 1 436 ? -13.786 -48.153 10.166  1.00 25.46 ? 436  ILE B N     1 
ATOM   7440 C CA    . ILE B 1 436 ? -14.462 -47.777 8.958   1.00 28.31 ? 436  ILE B CA    1 
ATOM   7441 C C     . ILE B 1 436 ? -15.495 -48.809 8.561   1.00 27.73 ? 436  ILE B C     1 
ATOM   7442 O O     . ILE B 1 436 ? -15.162 -49.850 8.051   1.00 26.86 ? 436  ILE B O     1 
ATOM   7443 C CB    . ILE B 1 436 ? -13.482 -47.509 7.799   1.00 27.49 ? 436  ILE B CB    1 
ATOM   7444 C CG1   . ILE B 1 436 ? -12.300 -46.684 8.293   1.00 29.76 ? 436  ILE B CG1   1 
ATOM   7445 C CG2   . ILE B 1 436 ? -14.202 -46.837 6.646   1.00 27.39 ? 436  ILE B CG2   1 
ATOM   7446 C CD1   . ILE B 1 436 ? -11.130 -46.671 7.348   1.00 30.73 ? 436  ILE B CD1   1 
ATOM   7447 N N     . ALA B 1 437 ? -16.746 -48.493 8.822   1.00 28.51 ? 437  ALA B N     1 
ATOM   7448 C CA    . ALA B 1 437 ? -17.825 -49.383 8.493   1.00 34.70 ? 437  ALA B CA    1 
ATOM   7449 C C     . ALA B 1 437 ? -18.497 -49.044 7.193   1.00 33.11 ? 437  ALA B C     1 
ATOM   7450 O O     . ALA B 1 437 ? -18.939 -47.942 6.987   1.00 36.98 ? 437  ALA B O     1 
ATOM   7451 C CB    . ALA B 1 437 ? -18.853 -49.386 9.600   1.00 36.53 ? 437  ALA B CB    1 
ATOM   7452 N N     . LEU B 1 438 ? -18.565 -50.012 6.321   1.00 36.80 ? 438  LEU B N     1 
ATOM   7453 C CA    . LEU B 1 438 ? -19.263 -49.805 5.082   1.00 41.77 ? 438  LEU B CA    1 
ATOM   7454 C C     . LEU B 1 438 ? -20.659 -50.337 5.275   1.00 40.28 ? 438  LEU B C     1 
ATOM   7455 O O     . LEU B 1 438 ? -20.855 -51.534 5.325   1.00 35.45 ? 438  LEU B O     1 
ATOM   7456 C CB    . LEU B 1 438 ? -18.576 -50.510 3.941   1.00 47.43 ? 438  LEU B CB    1 
ATOM   7457 C CG    . LEU B 1 438 ? -17.803 -49.587 2.987   1.00 63.86 ? 438  LEU B CG    1 
ATOM   7458 C CD1   . LEU B 1 438 ? -17.166 -48.388 3.675   1.00 64.14 ? 438  LEU B CD1   1 
ATOM   7459 C CD2   . LEU B 1 438 ? -16.750 -50.353 2.217   1.00 64.53 ? 438  LEU B CD2   1 
ATOM   7460 N N     . LEU B 1 439 ? -21.608 -49.431 5.435   1.00 40.28 ? 439  LEU B N     1 
ATOM   7461 C CA    . LEU B 1 439 ? -22.982 -49.827 5.655   1.00 41.66 ? 439  LEU B CA    1 
ATOM   7462 C C     . LEU B 1 439 ? -23.664 -49.907 4.308   1.00 40.66 ? 439  LEU B C     1 
ATOM   7463 O O     . LEU B 1 439 ? -24.051 -48.900 3.750   1.00 41.39 ? 439  LEU B O     1 
ATOM   7464 C CB    . LEU B 1 439 ? -23.660 -48.868 6.598   1.00 44.70 ? 439  LEU B CB    1 
ATOM   7465 C CG    . LEU B 1 439 ? -22.920 -48.644 7.914   1.00 48.46 ? 439  LEU B CG    1 
ATOM   7466 C CD1   . LEU B 1 439 ? -23.447 -47.410 8.618   1.00 53.07 ? 439  LEU B CD1   1 
ATOM   7467 C CD2   . LEU B 1 439 ? -23.012 -49.863 8.815   1.00 43.25 ? 439  LEU B CD2   1 
ATOM   7468 N N     . LEU B 1 440 ? -23.784 -51.113 3.787   1.00 36.16 ? 440  LEU B N     1 
ATOM   7469 C CA    . LEU B 1 440 ? -24.357 -51.313 2.478   1.00 38.40 ? 440  LEU B CA    1 
ATOM   7470 C C     . LEU B 1 440 ? -25.882 -51.358 2.488   1.00 37.92 ? 440  LEU B C     1 
ATOM   7471 O O     . LEU B 1 440 ? -26.477 -51.938 3.368   1.00 37.03 ? 440  LEU B O     1 
ATOM   7472 C CB    . LEU B 1 440 ? -23.801 -52.596 1.875   1.00 41.97 ? 440  LEU B CB    1 
ATOM   7473 C CG    . LEU B 1 440 ? -22.561 -52.612 0.985   1.00 52.16 ? 440  LEU B CG    1 
ATOM   7474 C CD1   . LEU B 1 440 ? -21.703 -51.389 1.199   1.00 60.83 ? 440  LEU B CD1   1 
ATOM   7475 C CD2   . LEU B 1 440 ? -21.742 -53.858 1.269   1.00 55.22 ? 440  LEU B CD2   1 
ATOM   7476 N N     . PHE B 1 441 ? -26.498 -50.751 1.494   1.00 37.70 ? 441  PHE B N     1 
ATOM   7477 C CA    . PHE B 1 441 ? -27.940 -50.693 1.439   1.00 38.98 ? 441  PHE B CA    1 
ATOM   7478 C C     . PHE B 1 441 ? -28.492 -50.631 0.026   1.00 39.52 ? 441  PHE B C     1 
ATOM   7479 O O     . PHE B 1 441 ? -27.779 -50.271 -0.881  1.00 39.34 ? 441  PHE B O     1 
ATOM   7480 C CB    . PHE B 1 441 ? -28.472 -49.505 2.240   1.00 39.88 ? 441  PHE B CB    1 
ATOM   7481 C CG    . PHE B 1 441 ? -28.087 -48.155 1.707   1.00 39.62 ? 441  PHE B CG    1 
ATOM   7482 C CD1   . PHE B 1 441 ? -26.861 -47.597 2.007   1.00 39.15 ? 441  PHE B CD1   1 
ATOM   7483 C CD2   . PHE B 1 441 ? -28.979 -47.414 0.968   1.00 39.75 ? 441  PHE B CD2   1 
ATOM   7484 C CE1   . PHE B 1 441 ? -26.516 -46.353 1.540   1.00 40.58 ? 441  PHE B CE1   1 
ATOM   7485 C CE2   . PHE B 1 441 ? -28.638 -46.173 0.496   1.00 39.27 ? 441  PHE B CE2   1 
ATOM   7486 C CZ    . PHE B 1 441 ? -27.405 -45.641 0.780   1.00 39.04 ? 441  PHE B CZ    1 
ATOM   7487 N N     . ASP B 1 442 ? -29.751 -51.000 -0.151  1.00 39.44 ? 442  ASP B N     1 
ATOM   7488 C CA    . ASP B 1 442 ? -30.423 -50.891 -1.469  1.00 37.73 ? 442  ASP B CA    1 
ATOM   7489 C C     . ASP B 1 442 ? -30.825 -49.432 -1.665  1.00 36.68 ? 442  ASP B C     1 
ATOM   7490 O O     . ASP B 1 442 ? -31.768 -48.982 -0.992  1.00 39.75 ? 442  ASP B O     1 
ATOM   7491 C CB    . ASP B 1 442 ? -31.625 -51.832 -1.548  1.00 41.31 ? 442  ASP B CB    1 
ATOM   7492 C CG    . ASP B 1 442 ? -32.289 -51.844 -2.913  1.00 44.22 ? 442  ASP B CG    1 
ATOM   7493 O OD1   . ASP B 1 442 ? -31.837 -51.078 -3.788  1.00 42.47 ? 442  ASP B OD1   1 
ATOM   7494 O OD2   . ASP B 1 442 ? -33.240 -52.636 -3.099  1.00 45.17 ? 442  ASP B OD2   1 
ATOM   7495 N N     . THR B 1 443 ? -30.142 -48.719 -2.553  1.00 36.56 ? 443  THR B N     1 
ATOM   7496 C CA    . THR B 1 443 ? -30.373 -47.274 -2.804  1.00 37.89 ? 443  THR B CA    1 
ATOM   7497 C C     . THR B 1 443 ? -31.748 -47.083 -3.443  1.00 39.24 ? 443  THR B C     1 
ATOM   7498 O O     . THR B 1 443 ? -32.274 -45.987 -3.322  1.00 38.51 ? 443  THR B O     1 
ATOM   7499 C CB    . THR B 1 443 ? -29.288 -46.663 -3.698  1.00 37.49 ? 443  THR B CB    1 
ATOM   7500 O OG1   . THR B 1 443 ? -29.319 -47.394 -4.919  1.00 36.75 ? 443  THR B OG1   1 
ATOM   7501 C CG2   . THR B 1 443 ? -27.896 -46.727 -3.107  1.00 34.63 ? 443  THR B CG2   1 
ATOM   7502 N N     . GLN B 1 444 ? -32.293 -48.121 -4.086  1.00 43.61 ? 444  GLN B N     1 
ATOM   7503 C CA    . GLN B 1 444 ? -33.590 -48.081 -4.827  1.00 48.43 ? 444  GLN B CA    1 
ATOM   7504 C C     . GLN B 1 444 ? -34.776 -48.324 -3.875  1.00 46.16 ? 444  GLN B C     1 
ATOM   7505 O O     . GLN B 1 444 ? -35.919 -48.290 -4.342  1.00 47.01 ? 444  GLN B O     1 
ATOM   7506 C CB    . GLN B 1 444 ? -33.598 -49.123 -5.950  1.00 45.69 ? 444  GLN B CB    1 
ATOM   7507 C CG    . GLN B 1 444 ? -32.403 -49.021 -6.892  1.00 48.62 ? 444  GLN B CG    1 
ATOM   7508 C CD    . GLN B 1 444 ? -32.246 -47.633 -7.457  1.00 52.98 ? 444  GLN B CD    1 
ATOM   7509 O OE1   . GLN B 1 444 ? -33.136 -47.095 -8.109  1.00 53.82 ? 444  GLN B OE1   1 
ATOM   7510 N NE2   . GLN B 1 444 ? -31.107 -47.020 -7.184  1.00 60.20 ? 444  GLN B NE2   1 
ATOM   7511 N N     . ASP B 1 445 ? -34.521 -48.531 -2.582  1.00 47.74 ? 445  ASP B N     1 
ATOM   7512 C CA    . ASP B 1 445 ? -35.527 -48.962 -1.579  1.00 45.89 ? 445  ASP B CA    1 
ATOM   7513 C C     . ASP B 1 445 ? -35.652 -47.877 -0.511  1.00 46.89 ? 445  ASP B C     1 
ATOM   7514 O O     . ASP B 1 445 ? -34.717 -47.755 0.300   1.00 45.98 ? 445  ASP B O     1 
ATOM   7515 C CB    . ASP B 1 445 ? -35.085 -50.304 -1.005  1.00 51.17 ? 445  ASP B CB    1 
ATOM   7516 C CG    . ASP B 1 445 ? -36.048 -50.962 -0.044  1.00 54.90 ? 445  ASP B CG    1 
ATOM   7517 O OD1   . ASP B 1 445 ? -36.677 -50.246 0.748   1.00 51.51 ? 445  ASP B OD1   1 
ATOM   7518 O OD2   . ASP B 1 445 ? -36.129 -52.211 -0.089  1.00 67.61 ? 445  ASP B OD2   1 
ATOM   7519 N N     . ALA B 1 446 ? -36.766 -47.142 -0.497  1.00 42.56 ? 446  ALA B N     1 
ATOM   7520 C CA    . ALA B 1 446 ? -37.016 -46.010 0.431   1.00 44.98 ? 446  ALA B CA    1 
ATOM   7521 C C     . ALA B 1 446 ? -36.838 -46.470 1.880   1.00 45.82 ? 446  ALA B C     1 
ATOM   7522 O O     . ALA B 1 446 ? -36.235 -45.712 2.661   1.00 47.23 ? 446  ALA B O     1 
ATOM   7523 C CB    . ALA B 1 446 ? -38.391 -45.435 0.208   1.00 43.33 ? 446  ALA B CB    1 
ATOM   7524 N N     . THR B 1 447 ? -37.321 -47.669 2.218   1.00 43.82 ? 447  THR B N     1 
ATOM   7525 C CA    . THR B 1 447 ? -37.250 -48.242 3.590   1.00 44.16 ? 447  THR B CA    1 
ATOM   7526 C C     . THR B 1 447 ? -35.781 -48.453 3.965   1.00 42.71 ? 447  THR B C     1 
ATOM   7527 O O     . THR B 1 447 ? -35.403 -48.034 5.068   1.00 42.47 ? 447  THR B O     1 
ATOM   7528 C CB    . THR B 1 447 ? -38.043 -49.550 3.717   1.00 45.62 ? 447  THR B CB    1 
ATOM   7529 O OG1   . THR B 1 447 ? -39.426 -49.249 3.537   1.00 53.24 ? 447  THR B OG1   1 
ATOM   7530 C CG2   . THR B 1 447 ? -37.873 -50.230 5.053   1.00 45.64 ? 447  THR B CG2   1 
ATOM   7531 N N     . ALA B 1 448 ? -34.999 -49.065 3.076   1.00 41.05 ? 448  ALA B N     1 
ATOM   7532 C CA    . ALA B 1 448 ? -33.564 -49.352 3.295   1.00 40.00 ? 448  ALA B CA    1 
ATOM   7533 C C     . ALA B 1 448 ? -32.794 -48.031 3.457   1.00 38.82 ? 448  ALA B C     1 
ATOM   7534 O O     . ALA B 1 448 ? -32.004 -47.941 4.422   1.00 35.74 ? 448  ALA B O     1 
ATOM   7535 C CB    . ALA B 1 448 ? -33.024 -50.211 2.177   1.00 39.80 ? 448  ALA B CB    1 
ATOM   7536 N N     . ARG B 1 449 ? -33.055 -47.014 2.626   1.00 39.88 ? 449  ARG B N     1 
ATOM   7537 C CA    . ARG B 1 449 ? -32.421 -45.670 2.763   1.00 37.85 ? 449  ARG B CA    1 
ATOM   7538 C C     . ARG B 1 449 ? -32.741 -45.086 4.148   1.00 37.70 ? 449  ARG B C     1 
ATOM   7539 O O     . ARG B 1 449 ? -31.797 -44.602 4.831   1.00 40.93 ? 449  ARG B O     1 
ATOM   7540 C CB    . ARG B 1 449 ? -32.872 -44.710 1.657   1.00 39.40 ? 449  ARG B CB    1 
ATOM   7541 C CG    . ARG B 1 449 ? -32.424 -45.130 0.265   1.00 42.16 ? 449  ARG B CG    1 
ATOM   7542 C CD    . ARG B 1 449 ? -32.598 -44.011 -0.738  1.00 44.74 ? 449  ARG B CD    1 
ATOM   7543 N NE    . ARG B 1 449 ? -33.975 -43.521 -0.782  1.00 49.62 ? 449  ARG B NE    1 
ATOM   7544 C CZ    . ARG B 1 449 ? -34.913 -43.930 -1.642  1.00 49.46 ? 449  ARG B CZ    1 
ATOM   7545 N NH1   . ARG B 1 449 ? -34.641 -44.855 -2.550  1.00 43.27 ? 449  ARG B NH1   1 
ATOM   7546 N NH2   . ARG B 1 449 ? -36.126 -43.408 -1.578  1.00 50.71 ? 449  ARG B NH2   1 
ATOM   7547 N N     . ASN B 1 450 ? -34.007 -45.142 4.569   1.00 37.72 ? 450  ASN B N     1 
ATOM   7548 C CA    . ASN B 1 450 ? -34.474 -44.575 5.862   1.00 35.70 ? 450  ASN B CA    1 
ATOM   7549 C C     . ASN B 1 450 ? -33.810 -45.314 7.020   1.00 34.87 ? 450  ASN B C     1 
ATOM   7550 O O     . ASN B 1 450 ? -33.385 -44.640 7.983   1.00 33.96 ? 450  ASN B O     1 
ATOM   7551 C CB    . ASN B 1 450 ? -35.997 -44.601 5.999   1.00 43.47 ? 450  ASN B CB    1 
ATOM   7552 C CG    . ASN B 1 450 ? -36.668 -43.647 5.036   1.00 45.51 ? 450  ASN B CG    1 
ATOM   7553 O OD1   . ASN B 1 450 ? -36.014 -42.796 4.432   1.00 45.18 ? 450  ASN B OD1   1 
ATOM   7554 N ND2   . ASN B 1 450 ? -37.968 -43.798 4.866   1.00 51.33 ? 450  ASN B ND2   1 
ATOM   7555 N N     . GLU B 1 451 ? -33.751 -46.643 6.938   1.00 33.68 ? 451  GLU B N     1 
ATOM   7556 C CA    . GLU B 1 451 ? -33.133 -47.500 7.972   1.00 35.31 ? 451  GLU B CA    1 
ATOM   7557 C C     . GLU B 1 451 ? -31.632 -47.187 8.075   1.00 35.64 ? 451  GLU B C     1 
ATOM   7558 O O     . GLU B 1 451 ? -31.106 -47.247 9.186   1.00 31.44 ? 451  GLU B O     1 
ATOM   7559 C CB    . GLU B 1 451 ? -33.272 -48.982 7.638   1.00 38.61 ? 451  GLU B CB    1 
ATOM   7560 C CG    . GLU B 1 451 ? -34.656 -49.558 7.890   1.00 41.30 ? 451  GLU B CG    1 
ATOM   7561 C CD    . GLU B 1 451 ? -34.759 -50.973 7.329   1.00 44.65 ? 451  GLU B CD    1 
ATOM   7562 O OE1   . GLU B 1 451 ? -34.042 -51.292 6.318   1.00 44.76 ? 451  GLU B OE1   1 
ATOM   7563 O OE2   . GLU B 1 451 ? -35.540 -51.751 7.882   1.00 45.78 ? 451  GLU B OE2   1 
ATOM   7564 N N     . THR B 1 452 ? -30.960 -46.949 6.947   1.00 35.85 ? 452  THR B N     1 
ATOM   7565 C CA    . THR B 1 452 ? -29.504 -46.678 6.921   1.00 33.40 ? 452  THR B CA    1 
ATOM   7566 C C     . THR B 1 452 ? -29.261 -45.324 7.600   1.00 32.09 ? 452  THR B C     1 
ATOM   7567 O O     . THR B 1 452 ? -28.349 -45.260 8.459   1.00 31.16 ? 452  THR B O     1 
ATOM   7568 C CB    . THR B 1 452 ? -28.946 -46.763 5.495   1.00 35.61 ? 452  THR B CB    1 
ATOM   7569 O OG1   . THR B 1 452 ? -29.142 -48.090 5.014   1.00 31.65 ? 452  THR B OG1   1 
ATOM   7570 C CG2   . THR B 1 452 ? -27.468 -46.427 5.433   1.00 35.69 ? 452  THR B CG2   1 
ATOM   7571 N N     . LEU B 1 453 ? -30.060 -44.301 7.277   1.00 29.87 ? 453  LEU B N     1 
ATOM   7572 C CA    . LEU B 1 453 ? -29.908 -42.966 7.903   1.00 30.88 ? 453  LEU B CA    1 
ATOM   7573 C C     . LEU B 1 453 ? -30.152 -43.086 9.407   1.00 34.37 ? 453  LEU B C     1 
ATOM   7574 O O     . LEU B 1 453 ? -29.316 -42.542 10.171  1.00 32.33 ? 453  LEU B O     1 
ATOM   7575 C CB    . LEU B 1 453 ? -30.842 -41.939 7.269   1.00 31.93 ? 453  LEU B CB    1 
ATOM   7576 C CG    . LEU B 1 453 ? -30.779 -40.531 7.869   1.00 31.04 ? 453  LEU B CG    1 
ATOM   7577 C CD1   . LEU B 1 453 ? -29.385 -39.952 7.761   1.00 29.03 ? 453  LEU B CD1   1 
ATOM   7578 C CD2   . LEU B 1 453 ? -31.796 -39.605 7.227   1.00 35.04 ? 453  LEU B CD2   1 
ATOM   7579 N N     . ALA B 1 454 ? -31.233 -43.768 9.821   1.00 33.62 ? 454  ALA B N     1 
ATOM   7580 C CA    . ALA B 1 454 ? -31.579 -43.989 11.249  1.00 33.10 ? 454  ALA B CA    1 
ATOM   7581 C C     . ALA B 1 454 ? -30.417 -44.690 11.956  1.00 31.19 ? 454  ALA B C     1 
ATOM   7582 O O     . ALA B 1 454 ? -30.021 -44.224 13.045  1.00 33.87 ? 454  ALA B O     1 
ATOM   7583 C CB    . ALA B 1 454 ? -32.866 -44.775 11.391  1.00 34.55 ? 454  ALA B CB    1 
ATOM   7584 N N     . LEU B 1 455 ? -29.885 -45.757 11.345  1.00 32.20 ? 455  LEU B N     1 
ATOM   7585 C CA    . LEU B 1 455 ? -28.767 -46.548 11.916  1.00 29.78 ? 455  LEU B CA    1 
ATOM   7586 C C     . LEU B 1 455 ? -27.561 -45.620 12.104  1.00 28.75 ? 455  LEU B C     1 
ATOM   7587 O O     . LEU B 1 455 ? -26.940 -45.656 13.177  1.00 27.61 ? 455  LEU B O     1 
ATOM   7588 C CB    . LEU B 1 455 ? -28.419 -47.723 10.996  1.00 30.80 ? 455  LEU B CB    1 
ATOM   7589 C CG    . LEU B 1 455 ? -27.118 -48.455 11.332  1.00 30.41 ? 455  LEU B CG    1 
ATOM   7590 C CD1   . LEU B 1 455 ? -27.181 -49.072 12.729  1.00 33.60 ? 455  LEU B CD1   1 
ATOM   7591 C CD2   . LEU B 1 455 ? -26.796 -49.517 10.281  1.00 28.78 ? 455  LEU B CD2   1 
ATOM   7592 N N     . THR B 1 456 ? -27.217 -44.828 11.085  1.00 28.32 ? 456  THR B N     1 
ATOM   7593 C CA    . THR B 1 456 ? -25.947 -44.058 11.119  1.00 29.98 ? 456  THR B CA    1 
ATOM   7594 C C     . THR B 1 456 ? -26.056 -42.977 12.205  1.00 28.46 ? 456  THR B C     1 
ATOM   7595 O O     . THR B 1 456 ? -25.085 -42.799 12.961  1.00 31.63 ? 456  THR B O     1 
ATOM   7596 C CB    . THR B 1 456 ? -25.564 -43.545 9.724   1.00 31.76 ? 456  THR B CB    1 
ATOM   7597 O OG1   . THR B 1 456 ? -25.610 -44.646 8.825   1.00 31.43 ? 456  THR B OG1   1 
ATOM   7598 C CG2   . THR B 1 456 ? -24.181 -42.927 9.705   1.00 32.86 ? 456  THR B CG2   1 
ATOM   7599 N N     . ARG B 1 457 ? -27.206 -42.321 12.332  1.00 28.62 ? 457  ARG B N     1 
ATOM   7600 C CA    . ARG B 1 457 ? -27.434 -41.301 13.393  1.00 29.03 ? 457  ARG B CA    1 
ATOM   7601 C C     . ARG B 1 457 ? -27.254 -41.932 14.767  1.00 31.10 ? 457  ARG B C     1 
ATOM   7602 O O     . ARG B 1 457 ? -26.622 -41.306 15.656  1.00 28.64 ? 457  ARG B O     1 
ATOM   7603 C CB    . ARG B 1 457 ? -28.831 -40.700 13.291  1.00 29.43 ? 457  ARG B CB    1 
ATOM   7604 C CG    . ARG B 1 457 ? -29.029 -39.853 12.047  1.00 29.28 ? 457  ARG B CG    1 
ATOM   7605 C CD    . ARG B 1 457 ? -30.037 -38.776 12.301  1.00 30.25 ? 457  ARG B CD    1 
ATOM   7606 N NE    . ARG B 1 457 ? -30.319 -38.019 11.110  1.00 29.89 ? 457  ARG B NE    1 
ATOM   7607 C CZ    . ARG B 1 457 ? -29.532 -37.067 10.620  1.00 33.26 ? 457  ARG B CZ    1 
ATOM   7608 N NH1   . ARG B 1 457 ? -28.391 -36.744 11.227  1.00 28.66 ? 457  ARG B NH1   1 
ATOM   7609 N NH2   . ARG B 1 457 ? -29.899 -36.429 9.522   1.00 30.97 ? 457  ARG B NH2   1 
ATOM   7610 N N     . LEU B 1 458 ? -27.756 -43.147 14.929  1.00 32.60 ? 458  LEU B N     1 
ATOM   7611 C CA    . LEU B 1 458 ? -27.652 -43.879 16.214  1.00 32.77 ? 458  LEU B CA    1 
ATOM   7612 C C     . LEU B 1 458 ? -26.180 -44.258 16.462  1.00 29.93 ? 458  LEU B C     1 
ATOM   7613 O O     . LEU B 1 458 ? -25.689 -44.072 17.593  1.00 28.79 ? 458  LEU B O     1 
ATOM   7614 C CB    . LEU B 1 458 ? -28.570 -45.101 16.172  1.00 32.48 ? 458  LEU B CB    1 
ATOM   7615 C CG    . LEU B 1 458 ? -28.420 -46.034 17.367  1.00 33.15 ? 458  LEU B CG    1 
ATOM   7616 C CD1   . LEU B 1 458 ? -28.820 -45.313 18.649  1.00 36.13 ? 458  LEU B CD1   1 
ATOM   7617 C CD2   . LEU B 1 458 ? -29.224 -47.315 17.186  1.00 36.88 ? 458  LEU B CD2   1 
ATOM   7618 N N     . LEU B 1 459 ? -25.486 -44.753 15.437  1.00 26.70 ? 459  LEU B N     1 
ATOM   7619 C CA    . LEU B 1 459 ? -24.058 -45.155 15.554  1.00 26.91 ? 459  LEU B CA    1 
ATOM   7620 C C     . LEU B 1 459 ? -23.218 -43.945 15.978  1.00 23.29 ? 459  LEU B C     1 
ATOM   7621 O O     . LEU B 1 459 ? -22.305 -44.110 16.797  1.00 27.63 ? 459  LEU B O     1 
ATOM   7622 C CB    . LEU B 1 459 ? -23.592 -45.717 14.208  1.00 25.28 ? 459  LEU B CB    1 
ATOM   7623 C CG    . LEU B 1 459 ? -24.122 -47.105 13.852  1.00 27.71 ? 459  LEU B CG    1 
ATOM   7624 C CD1   . LEU B 1 459 ? -23.608 -47.532 12.491  1.00 28.11 ? 459  LEU B CD1   1 
ATOM   7625 C CD2   . LEU B 1 459 ? -23.739 -48.147 14.887  1.00 27.11 ? 459  LEU B CD2   1 
ATOM   7626 N N     . ILE B 1 460 ? -23.475 -42.779 15.391  1.00 27.92 ? 460  ILE B N     1 
ATOM   7627 C CA    . ILE B 1 460 ? -22.717 -41.529 15.684  1.00 28.50 ? 460  ILE B CA    1 
ATOM   7628 C C     . ILE B 1 460 ? -22.945 -41.153 17.156  1.00 29.43 ? 460  ILE B C     1 
ATOM   7629 O O     . ILE B 1 460 ? -21.953 -40.867 17.855  1.00 26.90 ? 460  ILE B O     1 
ATOM   7630 C CB    . ILE B 1 460 ? -23.118 -40.394 14.724  1.00 29.36 ? 460  ILE B CB    1 
ATOM   7631 C CG1   . ILE B 1 460 ? -22.600 -40.679 13.305  1.00 28.85 ? 460  ILE B CG1   1 
ATOM   7632 C CG2   . ILE B 1 460 ? -22.621 -39.062 15.271  1.00 29.29 ? 460  ILE B CG2   1 
ATOM   7633 C CD1   . ILE B 1 460 ? -23.301 -39.909 12.222  1.00 28.75 ? 460  ILE B CD1   1 
ATOM   7634 N N     . ASP B 1 461 ? -24.191 -41.173 17.613  1.00 27.73 ? 461  ASP B N     1 
ATOM   7635 C CA    . ASP B 1 461 ? -24.531 -40.778 19.006  1.00 29.99 ? 461  ASP B CA    1 
ATOM   7636 C C     . ASP B 1 461 ? -23.889 -41.775 19.984  1.00 28.24 ? 461  ASP B C     1 
ATOM   7637 O O     . ASP B 1 461 ? -23.305 -41.325 20.976  1.00 26.10 ? 461  ASP B O     1 
ATOM   7638 C CB    . ASP B 1 461 ? -26.039 -40.624 19.194  1.00 31.54 ? 461  ASP B CB    1 
ATOM   7639 C CG    . ASP B 1 461 ? -26.600 -39.309 18.659  1.00 35.45 ? 461  ASP B CG    1 
ATOM   7640 O OD1   . ASP B 1 461 ? -25.813 -38.391 18.307  1.00 35.48 ? 461  ASP B OD1   1 
ATOM   7641 O OD2   . ASP B 1 461 ? -27.816 -39.221 18.573  1.00 36.95 ? 461  ASP B OD2   1 
ATOM   7642 N N     . GLU B 1 462 ? -23.958 -43.079 19.713  1.00 28.13 ? 462  GLU B N     1 
ATOM   7643 C CA    . GLU B 1 462 ? -23.427 -44.093 20.662  1.00 28.53 ? 462  GLU B CA    1 
ATOM   7644 C C     . GLU B 1 462 ? -21.897 -44.036 20.678  1.00 27.13 ? 462  GLU B C     1 
ATOM   7645 O O     . GLU B 1 462 ? -21.332 -44.178 21.750  1.00 27.08 ? 462  GLU B O     1 
ATOM   7646 C CB    . GLU B 1 462 ? -23.943 -45.492 20.344  1.00 29.59 ? 462  GLU B CB    1 
ATOM   7647 C CG    . GLU B 1 462 ? -25.442 -45.574 20.495  1.00 32.38 ? 462  GLU B CG    1 
ATOM   7648 C CD    . GLU B 1 462 ? -26.017 -46.962 20.676  1.00 36.16 ? 462  GLU B CD    1 
ATOM   7649 O OE1   . GLU B 1 462 ? -25.631 -47.887 19.925  1.00 30.53 ? 462  GLU B OE1   1 
ATOM   7650 O OE2   . GLU B 1 462 ? -26.899 -47.088 21.545  1.00 39.35 ? 462  GLU B OE2   1 
ATOM   7651 N N     . ALA B 1 463 ? -21.261 -43.865 19.519  1.00 27.39 ? 463  ALA B N     1 
ATOM   7652 C CA    . ALA B 1 463 ? -19.803 -43.688 19.398  1.00 24.27 ? 463  ALA B CA    1 
ATOM   7653 C C     . ALA B 1 463 ? -19.383 -42.468 20.231  1.00 24.25 ? 463  ALA B C     1 
ATOM   7654 O O     . ALA B 1 463 ? -18.430 -42.582 21.031  1.00 24.32 ? 463  ALA B O     1 
ATOM   7655 C CB    . ALA B 1 463 ? -19.425 -43.542 17.950  1.00 23.64 ? 463  ALA B CB    1 
ATOM   7656 N N     . ALA B 1 464 ? -20.108 -41.360 20.094  1.00 25.23 ? 464  ALA B N     1 
ATOM   7657 C CA    . ALA B 1 464 ? -19.760 -40.064 20.728  1.00 28.01 ? 464  ALA B CA    1 
ATOM   7658 C C     . ALA B 1 464 ? -19.876 -40.210 22.253  1.00 28.37 ? 464  ALA B C     1 
ATOM   7659 O O     . ALA B 1 464 ? -18.969 -39.769 22.972  1.00 28.67 ? 464  ALA B O     1 
ATOM   7660 C CB    . ALA B 1 464 ? -20.652 -38.977 20.197  1.00 27.65 ? 464  ALA B CB    1 
ATOM   7661 N N     . ALA B 1 465 ? -20.912 -40.894 22.729  1.00 31.36 ? 465  ALA B N     1 
ATOM   7662 C CA    . ALA B 1 465 ? -21.105 -41.183 24.172  1.00 29.98 ? 465  ALA B CA    1 
ATOM   7663 C C     . ALA B 1 465 ? -19.908 -41.969 24.723  1.00 31.10 ? 465  ALA B C     1 
ATOM   7664 O O     . ALA B 1 465 ? -19.640 -41.847 25.922  1.00 30.13 ? 465  ALA B O     1 
ATOM   7665 C CB    . ALA B 1 465 ? -22.407 -41.911 24.393  1.00 30.26 ? 465  ALA B CB    1 
ATOM   7666 N N     . GLU B 1 466 ? -19.197 -42.748 23.906  1.00 27.57 ? 466  GLU B N     1 
ATOM   7667 C CA    . GLU B 1 466 ? -18.002 -43.539 24.336  1.00 30.89 ? 466  GLU B CA    1 
ATOM   7668 C C     . GLU B 1 466 ? -16.709 -42.742 24.113  1.00 31.82 ? 466  GLU B C     1 
ATOM   7669 O O     . GLU B 1 466 ? -15.623 -43.264 24.440  1.00 33.86 ? 466  GLU B O     1 
ATOM   7670 C CB    . GLU B 1 466 ? -17.892 -44.863 23.570  1.00 34.89 ? 466  GLU B CB    1 
ATOM   7671 C CG    . GLU B 1 466 ? -19.010 -45.845 23.844  1.00 35.43 ? 466  GLU B CG    1 
ATOM   7672 C CD    . GLU B 1 466 ? -19.195 -46.191 25.314  1.00 39.64 ? 466  GLU B CD    1 
ATOM   7673 O OE1   . GLU B 1 466 ? -18.174 -46.372 26.030  1.00 40.60 ? 466  GLU B OE1   1 
ATOM   7674 O OE2   . GLU B 1 466 ? -20.361 -46.244 25.737  1.00 40.35 ? 466  GLU B OE2   1 
ATOM   7675 N N     . GLY B 1 467 ? -16.803 -41.510 23.600  1.00 31.03 ? 467  GLY B N     1 
ATOM   7676 C CA    . GLY B 1 467 ? -15.637 -40.626 23.375  1.00 30.45 ? 467  GLY B CA    1 
ATOM   7677 C C     . GLY B 1 467 ? -14.998 -40.875 22.018  1.00 30.47 ? 467  GLY B C     1 
ATOM   7678 O O     . GLY B 1 467 ? -13.814 -40.535 21.852  1.00 36.07 ? 467  GLY B O     1 
ATOM   7679 N N     . TYR B 1 468 ? -15.761 -41.407 21.059  1.00 27.32 ? 468  TYR B N     1 
ATOM   7680 C CA    . TYR B 1 468 ? -15.268 -41.739 19.695  1.00 27.44 ? 468  TYR B CA    1 
ATOM   7681 C C     . TYR B 1 468 ? -15.959 -40.832 18.686  1.00 27.40 ? 468  TYR B C     1 
ATOM   7682 O O     . TYR B 1 468 ? -17.150 -41.001 18.440  1.00 27.07 ? 468  TYR B O     1 
ATOM   7683 C CB    . TYR B 1 468 ? -15.547 -43.197 19.329  1.00 26.04 ? 468  TYR B CB    1 
ATOM   7684 C CG    . TYR B 1 468 ? -15.092 -44.239 20.314  1.00 28.38 ? 468  TYR B CG    1 
ATOM   7685 C CD1   . TYR B 1 468 ? -13.875 -44.153 20.971  1.00 27.71 ? 468  TYR B CD1   1 
ATOM   7686 C CD2   . TYR B 1 468 ? -15.874 -45.368 20.545  1.00 28.68 ? 468  TYR B CD2   1 
ATOM   7687 C CE1   . TYR B 1 468 ? -13.462 -45.145 21.850  1.00 29.99 ? 468  TYR B CE1   1 
ATOM   7688 C CE2   . TYR B 1 468 ? -15.474 -46.372 21.416  1.00 27.64 ? 468  TYR B CE2   1 
ATOM   7689 C CZ    . TYR B 1 468 ? -14.265 -46.263 22.074  1.00 29.38 ? 468  TYR B CZ    1 
ATOM   7690 O OH    . TYR B 1 468 ? -13.884 -47.246 22.948  1.00 28.11 ? 468  TYR B OH    1 
ATOM   7691 N N     . GLY B 1 469 ? -15.251 -39.834 18.177  1.00 26.37 ? 469  GLY B N     1 
ATOM   7692 C CA    . GLY B 1 469 ? -15.837 -38.848 17.262  1.00 25.02 ? 469  GLY B CA    1 
ATOM   7693 C C     . GLY B 1 469 ? -15.680 -39.279 15.811  1.00 25.24 ? 469  GLY B C     1 
ATOM   7694 O O     . GLY B 1 469 ? -14.655 -39.916 15.471  1.00 25.89 ? 469  GLY B O     1 
ATOM   7695 N N     . GLU B 1 470 ? -16.630 -38.881 14.980  1.00 24.35 ? 470  GLU B N     1 
ATOM   7696 C CA    . GLU B 1 470 ? -16.579 -39.138 13.529  1.00 25.54 ? 470  GLU B CA    1 
ATOM   7697 C C     . GLU B 1 470 ? -15.562 -38.183 12.893  1.00 26.38 ? 470  GLU B C     1 
ATOM   7698 O O     . GLU B 1 470 ? -15.536 -36.983 13.274  1.00 23.94 ? 470  GLU B O     1 
ATOM   7699 C CB    . GLU B 1 470 ? -17.984 -39.012 12.956  1.00 28.68 ? 470  GLU B CB    1 
ATOM   7700 C CG    . GLU B 1 470 ? -18.008 -39.105 11.456  1.00 30.97 ? 470  GLU B CG    1 
ATOM   7701 C CD    . GLU B 1 470 ? -17.470 -40.429 10.935  1.00 34.68 ? 470  GLU B CD    1 
ATOM   7702 O OE1   . GLU B 1 470 ? -18.305 -41.364 10.736  1.00 37.45 ? 470  GLU B OE1   1 
ATOM   7703 O OE2   . GLU B 1 470 ? -16.226 -40.537 10.738  1.00 30.22 ? 470  GLU B OE2   1 
ATOM   7704 N N     . TYR B 1 471 ? -14.812 -38.696 11.920  1.00 27.41 ? 471  TYR B N     1 
ATOM   7705 C CA    . TYR B 1 471 ? -13.691 -37.998 11.243  1.00 31.02 ? 471  TYR B CA    1 
ATOM   7706 C C     . TYR B 1 471 ? -14.175 -37.286 9.973   1.00 28.06 ? 471  TYR B C     1 
ATOM   7707 O O     . TYR B 1 471 ? -13.610 -36.266 9.554   1.00 27.81 ? 471  TYR B O     1 
ATOM   7708 C CB    . TYR B 1 471 ? -12.602 -39.018 10.890  1.00 38.19 ? 471  TYR B CB    1 
ATOM   7709 C CG    . TYR B 1 471 ? -11.380 -38.369 10.314  1.00 48.06 ? 471  TYR B CG    1 
ATOM   7710 C CD1   . TYR B 1 471 ? -10.627 -37.501 11.090  1.00 64.29 ? 471  TYR B CD1   1 
ATOM   7711 C CD2   . TYR B 1 471 ? -11.024 -38.537 8.983   1.00 55.68 ? 471  TYR B CD2   1 
ATOM   7712 C CE1   . TYR B 1 471 ? -9.526  -36.835 10.573  1.00 71.89 ? 471  TYR B CE1   1 
ATOM   7713 C CE2   . TYR B 1 471 ? -9.920  -37.886 8.454   1.00 65.87 ? 471  TYR B CE2   1 
ATOM   7714 C CZ    . TYR B 1 471 ? -9.171  -37.026 9.248   1.00 73.90 ? 471  TYR B CZ    1 
ATOM   7715 O OH    . TYR B 1 471 ? -8.086  -36.369 8.737   1.00 84.55 ? 471  TYR B OH    1 
ATOM   7716 N N     . ARG B 1 472 ? -15.192 -37.848 9.343   1.00 25.50 ? 472  ARG B N     1 
ATOM   7717 C CA    . ARG B 1 472 ? -15.633 -37.445 7.985   1.00 27.71 ? 472  ARG B CA    1 
ATOM   7718 C C     . ARG B 1 472 ? -17.047 -37.978 7.807   1.00 24.77 ? 472  ARG B C     1 
ATOM   7719 O O     . ARG B 1 472 ? -17.323 -39.083 8.288   1.00 26.52 ? 472  ARG B O     1 
ATOM   7720 C CB    . ARG B 1 472 ? -14.654 -38.054 6.980   1.00 27.90 ? 472  ARG B CB    1 
ATOM   7721 C CG    . ARG B 1 472 ? -14.824 -37.577 5.549   1.00 27.77 ? 472  ARG B CG    1 
ATOM   7722 C CD    . ARG B 1 472 ? -13.716 -38.162 4.711   1.00 28.15 ? 472  ARG B CD    1 
ATOM   7723 N NE    . ARG B 1 472 ? -13.877 -37.866 3.295   1.00 26.45 ? 472  ARG B NE    1 
ATOM   7724 C CZ    . ARG B 1 472 ? -13.219 -38.490 2.334   1.00 25.50 ? 472  ARG B CZ    1 
ATOM   7725 N NH1   . ARG B 1 472 ? -12.360 -39.449 2.633   1.00 26.27 ? 472  ARG B NH1   1 
ATOM   7726 N NH2   . ARG B 1 472 ? -13.430 -38.163 1.069   1.00 24.53 ? 472  ARG B NH2   1 
ATOM   7727 N N     . THR B 1 473 ? -17.959 -37.200 7.241   1.00 26.95 ? 473  THR B N     1 
ATOM   7728 C CA    . THR B 1 473 ? -19.356 -37.695 7.178   1.00 27.28 ? 473  THR B CA    1 
ATOM   7729 C C     . THR B 1 473 ? -20.060 -37.190 5.937   1.00 26.21 ? 473  THR B C     1 
ATOM   7730 O O     . THR B 1 473 ? -19.514 -36.312 5.220   1.00 26.68 ? 473  THR B O     1 
ATOM   7731 C CB    . THR B 1 473 ? -20.139 -37.377 8.463   1.00 26.96 ? 473  THR B CB    1 
ATOM   7732 O OG1   . THR B 1 473 ? -21.187 -38.343 8.527   1.00 30.58 ? 473  THR B OG1   1 
ATOM   7733 C CG2   . THR B 1 473 ? -20.682 -35.974 8.541   1.00 28.70 ? 473  THR B CG2   1 
ATOM   7734 N N     . HIS B 1 474 ? -21.231 -37.775 5.721   1.00 26.12 ? 474  HIS B N     1 
ATOM   7735 C CA    . HIS B 1 474 ? -22.158 -37.443 4.614   1.00 26.85 ? 474  HIS B CA    1 
ATOM   7736 C C     . HIS B 1 474 ? -22.839 -36.099 4.872   1.00 25.74 ? 474  HIS B C     1 
ATOM   7737 O O     . HIS B 1 474 ? -23.091 -35.747 6.051   1.00 27.61 ? 474  HIS B O     1 
ATOM   7738 C CB    . HIS B 1 474 ? -23.128 -38.624 4.488   1.00 26.74 ? 474  HIS B CB    1 
ATOM   7739 C CG    . HIS B 1 474 ? -23.963 -38.634 3.259   1.00 28.14 ? 474  HIS B CG    1 
ATOM   7740 N ND1   . HIS B 1 474 ? -25.027 -37.785 3.099   1.00 28.32 ? 474  HIS B ND1   1 
ATOM   7741 C CD2   . HIS B 1 474 ? -23.923 -39.420 2.167   1.00 26.49 ? 474  HIS B CD2   1 
ATOM   7742 C CE1   . HIS B 1 474 ? -25.607 -38.036 1.943   1.00 29.46 ? 474  HIS B CE1   1 
ATOM   7743 N NE2   . HIS B 1 474 ? -24.952 -39.036 1.353   1.00 29.16 ? 474  HIS B NE2   1 
ATOM   7744 N N     . ASN B 1 475 ? -23.174 -35.382 3.799   1.00 27.99 ? 475  ASN B N     1 
ATOM   7745 C CA    . ASN B 1 475 ? -24.073 -34.200 3.819   1.00 26.38 ? 475  ASN B CA    1 
ATOM   7746 C C     . ASN B 1 475 ? -25.168 -34.356 4.882   1.00 26.03 ? 475  ASN B C     1 
ATOM   7747 O O     . ASN B 1 475 ? -25.393 -33.382 5.646   1.00 26.90 ? 475  ASN B O     1 
ATOM   7748 C CB    . ASN B 1 475 ? -24.747 -34.003 2.459   1.00 30.02 ? 475  ASN B CB    1 
ATOM   7749 C CG    . ASN B 1 475 ? -23.838 -33.357 1.439   1.00 26.34 ? 475  ASN B CG    1 
ATOM   7750 O OD1   . ASN B 1 475 ? -22.923 -32.633 1.805   1.00 26.85 ? 475  ASN B OD1   1 
ATOM   7751 N ND2   . ASN B 1 475 ? -24.099 -33.600 0.162   1.00 28.47 ? 475  ASN B ND2   1 
ATOM   7752 N N     . ALA B 1 476 ? -25.855 -35.502 4.901   1.00 25.47 ? 476  ALA B N     1 
ATOM   7753 C CA    . ALA B 1 476 ? -27.097 -35.703 5.694   1.00 29.39 ? 476  ALA B CA    1 
ATOM   7754 C C     . ALA B 1 476 ? -26.771 -35.688 7.189   1.00 27.65 ? 476  ALA B C     1 
ATOM   7755 O O     . ALA B 1 476 ? -27.681 -35.407 7.989   1.00 27.94 ? 476  ALA B O     1 
ATOM   7756 C CB    . ALA B 1 476 ? -27.765 -37.007 5.305   1.00 32.23 ? 476  ALA B CB    1 
ATOM   7757 N N     . LEU B 1 477 ? -25.513 -35.936 7.540   1.00 26.90 ? 477  LEU B N     1 
ATOM   7758 C CA    . LEU B 1 477 ? -25.064 -36.165 8.931   1.00 26.59 ? 477  LEU B CA    1 
ATOM   7759 C C     . LEU B 1 477 ? -24.195 -35.014 9.450   1.00 28.22 ? 477  LEU B C     1 
ATOM   7760 O O     . LEU B 1 477 ? -23.849 -35.054 10.651  1.00 26.63 ? 477  LEU B O     1 
ATOM   7761 C CB    . LEU B 1 477 ? -24.315 -37.490 8.946   1.00 28.83 ? 477  LEU B CB    1 
ATOM   7762 C CG    . LEU B 1 477 ? -25.135 -38.702 8.502   1.00 29.79 ? 477  LEU B CG    1 
ATOM   7763 C CD1   . LEU B 1 477 ? -24.234 -39.885 8.199   1.00 30.83 ? 477  LEU B CD1   1 
ATOM   7764 C CD2   . LEU B 1 477 ? -26.148 -39.063 9.574   1.00 32.68 ? 477  LEU B CD2   1 
ATOM   7765 N N     . MET B 1 478 ? -23.879 -34.013 8.622   1.00 27.33 ? 478  MET B N     1 
ATOM   7766 C CA    . MET B 1 478 ? -22.849 -33.002 8.980   1.00 28.07 ? 478  MET B CA    1 
ATOM   7767 C C     . MET B 1 478 ? -23.288 -32.189 10.210  1.00 27.70 ? 478  MET B C     1 
ATOM   7768 O O     . MET B 1 478 ? -22.448 -31.984 11.104  1.00 24.70 ? 478  MET B O     1 
ATOM   7769 C CB    . MET B 1 478 ? -22.540 -32.082 7.798   1.00 26.52 ? 478  MET B CB    1 
ATOM   7770 C CG    . MET B 1 478 ? -21.801 -32.797 6.719   1.00 26.60 ? 478  MET B CG    1 
ATOM   7771 S SD    . MET B 1 478 ? -21.514 -31.726 5.304   1.00 26.53 ? 478  MET B SD    1 
ATOM   7772 C CE    . MET B 1 478 ? -20.570 -32.868 4.301   1.00 27.51 ? 478  MET B CE    1 
ATOM   7773 N N     . ASP B 1 479 ? -24.567 -31.814 10.292  1.00 28.09 ? 479  ASP B N     1 
ATOM   7774 C CA    . ASP B 1 479 ? -25.107 -31.037 11.433  1.00 27.50 ? 479  ASP B CA    1 
ATOM   7775 C C     . ASP B 1 479 ? -24.957 -31.866 12.701  1.00 25.93 ? 479  ASP B C     1 
ATOM   7776 O O     . ASP B 1 479 ? -24.500 -31.321 13.727  1.00 26.79 ? 479  ASP B O     1 
ATOM   7777 C CB    . ASP B 1 479 ? -26.554 -30.596 11.178  1.00 29.80 ? 479  ASP B CB    1 
ATOM   7778 C CG    . ASP B 1 479 ? -26.635 -29.475 10.144  1.00 28.92 ? 479  ASP B CG    1 
ATOM   7779 O OD1   . ASP B 1 479 ? -25.690 -28.637 10.076  1.00 32.28 ? 479  ASP B OD1   1 
ATOM   7780 O OD2   . ASP B 1 479 ? -27.644 -29.411 9.447   1.00 33.30 ? 479  ASP B OD2   1 
ATOM   7781 N N     . GLN B 1 480 ? -25.354 -33.123 12.647  1.00 27.01 ? 480  GLN B N     1 
ATOM   7782 C CA    . GLN B 1 480 ? -25.290 -34.023 13.826  1.00 24.71 ? 480  GLN B CA    1 
ATOM   7783 C C     . GLN B 1 480 ? -23.830 -34.176 14.257  1.00 26.39 ? 480  GLN B C     1 
ATOM   7784 O O     . GLN B 1 480 ? -23.543 -34.049 15.460  1.00 22.13 ? 480  GLN B O     1 
ATOM   7785 C CB    . GLN B 1 480 ? -25.903 -35.390 13.523  1.00 24.87 ? 480  GLN B CB    1 
ATOM   7786 C CG    . GLN B 1 480 ? -25.903 -36.285 14.748  1.00 25.61 ? 480  GLN B CG    1 
ATOM   7787 C CD    . GLN B 1 480 ? -26.408 -37.680 14.506  1.00 25.95 ? 480  GLN B CD    1 
ATOM   7788 O OE1   . GLN B 1 480 ? -26.949 -37.996 13.441  1.00 27.78 ? 480  GLN B OE1   1 
ATOM   7789 N NE2   . GLN B 1 480 ? -26.235 -38.507 15.521  1.00 26.19 ? 480  GLN B NE2   1 
ATOM   7790 N N     . VAL B 1 481 ? -22.927 -34.484 13.318  1.00 26.28 ? 481  VAL B N     1 
ATOM   7791 C CA    . VAL B 1 481 ? -21.501 -34.749 13.670  1.00 26.10 ? 481  VAL B CA    1 
ATOM   7792 C C     . VAL B 1 481 ? -20.877 -33.487 14.283  1.00 25.14 ? 481  VAL B C     1 
ATOM   7793 O O     . VAL B 1 481 ? -20.224 -33.588 15.363  1.00 24.27 ? 481  VAL B O     1 
ATOM   7794 C CB    . VAL B 1 481 ? -20.714 -35.299 12.467  1.00 26.14 ? 481  VAL B CB    1 
ATOM   7795 C CG1   . VAL B 1 481 ? -19.219 -35.324 12.770  1.00 26.23 ? 481  VAL B CG1   1 
ATOM   7796 C CG2   . VAL B 1 481 ? -21.209 -36.696 12.120  1.00 26.93 ? 481  VAL B CG2   1 
ATOM   7797 N N     . MET B 1 482 ? -21.090 -32.322 13.691  1.00 26.22 ? 482  MET B N     1 
ATOM   7798 C CA    . MET B 1 482 ? -20.517 -31.084 14.273  1.00 25.11 ? 482  MET B CA    1 
ATOM   7799 C C     . MET B 1 482 ? -21.112 -30.890 15.668  1.00 26.56 ? 482  MET B C     1 
ATOM   7800 O O     . MET B 1 482 ? -20.369 -30.407 16.568  1.00 25.00 ? 482  MET B O     1 
ATOM   7801 C CB    . MET B 1 482 ? -20.791 -29.851 13.416  1.00 26.01 ? 482  MET B CB    1 
ATOM   7802 C CG    . MET B 1 482 ? -20.172 -28.587 13.965  1.00 24.49 ? 482  MET B CG    1 
ATOM   7803 S SD    . MET B 1 482 ? -18.386 -28.747 14.371  1.00 27.81 ? 482  MET B SD    1 
ATOM   7804 C CE    . MET B 1 482 ? -17.659 -28.396 12.767  1.00 28.11 ? 482  MET B CE    1 
ATOM   7805 N N     . GLY B 1 483 ? -22.386 -31.271 15.841  1.00 25.47 ? 483  GLY B N     1 
ATOM   7806 C CA    . GLY B 1 483 ? -23.130 -31.132 17.103  1.00 23.39 ? 483  GLY B CA    1 
ATOM   7807 C C     . GLY B 1 483 ? -22.493 -31.964 18.209  1.00 24.96 ? 483  GLY B C     1 
ATOM   7808 O O     . GLY B 1 483 ? -22.671 -31.597 19.399  1.00 24.66 ? 483  GLY B O     1 
ATOM   7809 N N     . THR B 1 484 ? -21.785 -33.048 17.867  1.00 23.20 ? 484  THR B N     1 
ATOM   7810 C CA    . THR B 1 484 ? -21.098 -33.908 18.870  1.00 23.59 ? 484  THR B CA    1 
ATOM   7811 C C     . THR B 1 484 ? -19.806 -33.249 19.360  1.00 22.86 ? 484  THR B C     1 
ATOM   7812 O O     . THR B 1 484 ? -19.324 -33.661 20.402  1.00 22.44 ? 484  THR B O     1 
ATOM   7813 C CB    . THR B 1 484 ? -20.807 -35.331 18.383  1.00 26.33 ? 484  THR B CB    1 
ATOM   7814 O OG1   . THR B 1 484 ? -19.796 -35.303 17.376  1.00 27.59 ? 484  THR B OG1   1 
ATOM   7815 C CG2   . THR B 1 484 ? -22.060 -36.045 17.915  1.00 29.93 ? 484  THR B CG2   1 
ATOM   7816 N N     . TYR B 1 485 ? -19.223 -32.318 18.603  1.00 25.50 ? 485  TYR B N     1 
ATOM   7817 C CA    . TYR B 1 485 ? -17.947 -31.629 18.954  1.00 24.79 ? 485  TYR B CA    1 
ATOM   7818 C C     . TYR B 1 485 ? -18.268 -30.349 19.741  1.00 24.50 ? 485  TYR B C     1 
ATOM   7819 O O     . TYR B 1 485 ? -17.778 -29.260 19.392  1.00 23.49 ? 485  TYR B O     1 
ATOM   7820 C CB    . TYR B 1 485 ? -17.118 -31.413 17.682  1.00 24.19 ? 485  TYR B CB    1 
ATOM   7821 C CG    . TYR B 1 485 ? -16.485 -32.675 17.144  1.00 24.37 ? 485  TYR B CG    1 
ATOM   7822 C CD1   . TYR B 1 485 ? -15.223 -33.078 17.538  1.00 23.07 ? 485  TYR B CD1   1 
ATOM   7823 C CD2   . TYR B 1 485 ? -17.134 -33.457 16.201  1.00 25.90 ? 485  TYR B CD2   1 
ATOM   7824 C CE1   . TYR B 1 485 ? -14.634 -34.235 17.043  1.00 24.84 ? 485  TYR B CE1   1 
ATOM   7825 C CE2   . TYR B 1 485 ? -16.558 -34.609 15.687  1.00 24.53 ? 485  TYR B CE2   1 
ATOM   7826 C CZ    . TYR B 1 485 ? -15.305 -35.012 16.113  1.00 24.63 ? 485  TYR B CZ    1 
ATOM   7827 O OH    . TYR B 1 485 ? -14.740 -36.145 15.604  1.00 24.50 ? 485  TYR B OH    1 
ATOM   7828 N N     . ASN B 1 486 ? -19.053 -30.491 20.817  1.00 22.44 ? 486  ASN B N     1 
ATOM   7829 C CA    . ASN B 1 486 ? -19.704 -29.327 21.448  1.00 23.81 ? 486  ASN B CA    1 
ATOM   7830 C C     . ASN B 1 486 ? -19.101 -29.057 22.816  1.00 23.38 ? 486  ASN B C     1 
ATOM   7831 O O     . ASN B 1 486 ? -19.798 -28.368 23.596  1.00 22.43 ? 486  ASN B O     1 
ATOM   7832 C CB    . ASN B 1 486 ? -21.227 -29.459 21.512  1.00 27.02 ? 486  ASN B CB    1 
ATOM   7833 C CG    . ASN B 1 486 ? -21.691 -30.575 22.413  1.00 27.51 ? 486  ASN B CG    1 
ATOM   7834 O OD1   . ASN B 1 486 ? -20.938 -31.502 22.697  1.00 29.02 ? 486  ASN B OD1   1 
ATOM   7835 N ND2   . ASN B 1 486 ? -22.927 -30.461 22.887  1.00 30.56 ? 486  ASN B ND2   1 
ATOM   7836 N N     . TRP B 1 487 ? -17.833 -29.415 23.048  1.00 22.78 ? 487  TRP B N     1 
ATOM   7837 C CA    . TRP B 1 487 ? -17.094 -28.970 24.260  1.00 23.07 ? 487  TRP B CA    1 
ATOM   7838 C C     . TRP B 1 487 ? -17.311 -27.459 24.448  1.00 23.15 ? 487  TRP B C     1 
ATOM   7839 O O     . TRP B 1 487 ? -17.292 -26.699 23.440  1.00 24.68 ? 487  TRP B O     1 
ATOM   7840 C CB    . TRP B 1 487 ? -15.604 -29.351 24.194  1.00 23.06 ? 487  TRP B CB    1 
ATOM   7841 C CG    . TRP B 1 487 ? -14.847 -29.122 25.474  1.00 20.62 ? 487  TRP B CG    1 
ATOM   7842 C CD1   . TRP B 1 487 ? -14.617 -30.011 26.487  1.00 24.51 ? 487  TRP B CD1   1 
ATOM   7843 C CD2   . TRP B 1 487 ? -14.241 -27.891 25.888  1.00 21.41 ? 487  TRP B CD2   1 
ATOM   7844 N NE1   . TRP B 1 487 ? -13.857 -29.429 27.471  1.00 24.41 ? 487  TRP B NE1   1 
ATOM   7845 C CE2   . TRP B 1 487 ? -13.643 -28.119 27.141  1.00 22.38 ? 487  TRP B CE2   1 
ATOM   7846 C CE3   . TRP B 1 487 ? -14.107 -26.629 25.297  1.00 21.14 ? 487  TRP B CE3   1 
ATOM   7847 C CZ2   . TRP B 1 487 ? -12.931 -27.122 27.809  1.00 22.50 ? 487  TRP B CZ2   1 
ATOM   7848 C CZ3   . TRP B 1 487 ? -13.423 -25.644 25.963  1.00 23.65 ? 487  TRP B CZ3   1 
ATOM   7849 C CH2   . TRP B 1 487 ? -12.854 -25.891 27.212  1.00 23.55 ? 487  TRP B CH2   1 
ATOM   7850 N N     . GLY B 1 488 ? -17.483 -27.014 25.694  1.00 25.42 ? 488  GLY B N     1 
ATOM   7851 C CA    . GLY B 1 488 ? -17.553 -25.579 26.018  1.00 25.76 ? 488  GLY B CA    1 
ATOM   7852 C C     . GLY B 1 488 ? -18.750 -24.922 25.377  1.00 23.90 ? 488  GLY B C     1 
ATOM   7853 O O     . GLY B 1 488 ? -18.602 -23.819 24.831  1.00 25.25 ? 488  GLY B O     1 
ATOM   7854 N N     . ASP B 1 489 ? -19.912 -25.581 25.475  1.00 26.51 ? 489  ASP B N     1 
ATOM   7855 C CA    . ASP B 1 489 ? -21.191 -25.048 24.954  1.00 30.14 ? 489  ASP B CA    1 
ATOM   7856 C C     . ASP B 1 489 ? -21.011 -24.709 23.466  1.00 27.67 ? 489  ASP B C     1 
ATOM   7857 O O     . ASP B 1 489 ? -21.437 -23.623 23.074  1.00 28.23 ? 489  ASP B O     1 
ATOM   7858 C CB    . ASP B 1 489 ? -21.646 -23.841 25.799  1.00 35.27 ? 489  ASP B CB    1 
ATOM   7859 C CG    . ASP B 1 489 ? -22.041 -24.157 27.239  1.00 50.21 ? 489  ASP B CG    1 
ATOM   7860 O OD1   . ASP B 1 489 ? -22.840 -25.104 27.429  1.00 65.69 ? 489  ASP B OD1   1 
ATOM   7861 O OD2   . ASP B 1 489 ? -21.582 -23.436 28.174  1.00 57.55 ? 489  ASP B OD2   1 
ATOM   7862 N N     . GLY B 1 490 ? -20.465 -25.632 22.673  1.00 26.77 ? 490  GLY B N     1 
ATOM   7863 C CA    . GLY B 1 490 ? -20.350 -25.530 21.196  1.00 25.87 ? 490  GLY B CA    1 
ATOM   7864 C C     . GLY B 1 490 ? -19.303 -24.506 20.770  1.00 23.31 ? 490  GLY B C     1 
ATOM   7865 O O     . GLY B 1 490 ? -19.525 -23.795 19.736  1.00 23.36 ? 490  GLY B O     1 
ATOM   7866 N N     . ALA B 1 491 ? -18.189 -24.397 21.499  1.00 22.41 ? 491  ALA B N     1 
ATOM   7867 C CA    . ALA B 1 491 ? -17.207 -23.315 21.250  1.00 21.50 ? 491  ALA B CA    1 
ATOM   7868 C C     . ALA B 1 491 ? -16.600 -23.492 19.845  1.00 21.74 ? 491  ALA B C     1 
ATOM   7869 O O     . ALA B 1 491 ? -16.364 -22.486 19.186  1.00 24.81 ? 491  ALA B O     1 
ATOM   7870 C CB    . ALA B 1 491 ? -16.140 -23.315 22.320  1.00 24.89 ? 491  ALA B CB    1 
ATOM   7871 N N     . LEU B 1 492 ? -16.375 -24.737 19.414  1.00 21.68 ? 492  LEU B N     1 
ATOM   7872 C CA    . LEU B 1 492 ? -15.695 -25.014 18.120  1.00 22.96 ? 492  LEU B CA    1 
ATOM   7873 C C     . LEU B 1 492 ? -16.549 -24.474 16.981  1.00 25.83 ? 492  LEU B C     1 
ATOM   7874 O O     . LEU B 1 492 ? -15.997 -23.734 16.114  1.00 22.34 ? 492  LEU B O     1 
ATOM   7875 C CB    . LEU B 1 492 ? -15.422 -26.501 17.948  1.00 23.38 ? 492  LEU B CB    1 
ATOM   7876 C CG    . LEU B 1 492 ? -14.634 -26.854 16.676  1.00 25.01 ? 492  LEU B CG    1 
ATOM   7877 C CD1   . LEU B 1 492 ? -13.240 -26.253 16.689  1.00 25.50 ? 492  LEU B CD1   1 
ATOM   7878 C CD2   . LEU B 1 492 ? -14.519 -28.345 16.506  1.00 27.56 ? 492  LEU B CD2   1 
ATOM   7879 N N     . LEU B 1 493 ? -17.846 -24.788 16.978  1.00 23.95 ? 493  LEU B N     1 
ATOM   7880 C CA    . LEU B 1 493 ? -18.726 -24.329 15.868  1.00 23.93 ? 493  LEU B CA    1 
ATOM   7881 C C     . LEU B 1 493 ? -18.883 -22.804 15.906  1.00 22.44 ? 493  LEU B C     1 
ATOM   7882 O O     . LEU B 1 493 ? -18.911 -22.201 14.828  1.00 24.08 ? 493  LEU B O     1 
ATOM   7883 C CB    . LEU B 1 493 ? -20.069 -25.044 15.938  1.00 23.60 ? 493  LEU B CB    1 
ATOM   7884 C CG    . LEU B 1 493 ? -21.043 -24.632 14.847  1.00 23.78 ? 493  LEU B CG    1 
ATOM   7885 C CD1   . LEU B 1 493 ? -20.393 -24.767 13.473  1.00 24.54 ? 493  LEU B CD1   1 
ATOM   7886 C CD2   . LEU B 1 493 ? -22.353 -25.424 14.966  1.00 25.15 ? 493  LEU B CD2   1 
ATOM   7887 N N     . LYS B 1 494 ? -18.950 -22.184 17.091  1.00 24.84 ? 494  LYS B N     1 
ATOM   7888 C CA    . LYS B 1 494 ? -19.072 -20.709 17.195  1.00 23.16 ? 494  LYS B CA    1 
ATOM   7889 C C     . LYS B 1 494 ? -17.835 -20.058 16.556  1.00 23.53 ? 494  LYS B C     1 
ATOM   7890 O O     . LYS B 1 494 ? -17.996 -19.019 15.880  1.00 24.34 ? 494  LYS B O     1 
ATOM   7891 C CB    . LYS B 1 494 ? -19.299 -20.248 18.631  1.00 24.68 ? 494  LYS B CB    1 
ATOM   7892 C CG    . LYS B 1 494 ? -20.665 -20.644 19.193  1.00 28.20 ? 494  LYS B CG    1 
ATOM   7893 C CD    . LYS B 1 494 ? -20.888 -20.240 20.641  1.00 27.72 ? 494  LYS B CD    1 
ATOM   7894 C CE    . LYS B 1 494 ? -22.111 -20.883 21.258  1.00 29.47 ? 494  LYS B CE    1 
ATOM   7895 N NZ    . LYS B 1 494 ? -21.994 -20.897 22.733  1.00 30.03 ? 494  LYS B NZ    1 
ATOM   7896 N N     . PHE B 1 495 ? -16.647 -20.616 16.802  1.00 23.31 ? 495  PHE B N     1 
ATOM   7897 C CA    . PHE B 1 495 ? -15.387 -20.144 16.171  1.00 25.17 ? 495  PHE B CA    1 
ATOM   7898 C C     . PHE B 1 495 ? -15.514 -20.250 14.646  1.00 21.88 ? 495  PHE B C     1 
ATOM   7899 O O     . PHE B 1 495 ? -15.238 -19.232 13.949  1.00 23.44 ? 495  PHE B O     1 
ATOM   7900 C CB    . PHE B 1 495 ? -14.202 -20.938 16.724  1.00 25.17 ? 495  PHE B CB    1 
ATOM   7901 C CG    . PHE B 1 495 ? -12.903 -20.817 15.959  1.00 25.25 ? 495  PHE B CG    1 
ATOM   7902 C CD1   . PHE B 1 495 ? -12.041 -19.747 16.181  1.00 23.47 ? 495  PHE B CD1   1 
ATOM   7903 C CD2   . PHE B 1 495 ? -12.524 -21.816 15.067  1.00 24.31 ? 495  PHE B CD2   1 
ATOM   7904 C CE1   . PHE B 1 495 ? -10.840 -19.661 15.483  1.00 23.62 ? 495  PHE B CE1   1 
ATOM   7905 C CE2   . PHE B 1 495 ? -11.323 -21.731 14.373  1.00 23.70 ? 495  PHE B CE2   1 
ATOM   7906 C CZ    . PHE B 1 495 ? -10.481 -20.653 14.580  1.00 22.68 ? 495  PHE B CZ    1 
ATOM   7907 N N     . HIS B 1 496 ? -15.866 -21.434 14.146  1.00 23.90 ? 496  HIS B N     1 
ATOM   7908 C CA    . HIS B 1 496 ? -16.002 -21.678 12.680  1.00 24.94 ? 496  HIS B CA    1 
ATOM   7909 C C     . HIS B 1 496 ? -17.026 -20.696 12.092  1.00 24.84 ? 496  HIS B C     1 
ATOM   7910 O O     . HIS B 1 496 ? -16.779 -20.142 11.004  1.00 24.66 ? 496  HIS B O     1 
ATOM   7911 C CB    . HIS B 1 496 ? -16.384 -23.119 12.359  1.00 23.65 ? 496  HIS B CB    1 
ATOM   7912 C CG    . HIS B 1 496 ? -15.307 -24.106 12.612  1.00 27.72 ? 496  HIS B CG    1 
ATOM   7913 N ND1   . HIS B 1 496 ? -14.022 -23.903 12.184  1.00 27.68 ? 496  HIS B ND1   1 
ATOM   7914 C CD2   . HIS B 1 496 ? -15.331 -25.312 13.210  1.00 27.71 ? 496  HIS B CD2   1 
ATOM   7915 C CE1   . HIS B 1 496 ? -13.286 -24.926 12.541  1.00 29.90 ? 496  HIS B CE1   1 
ATOM   7916 N NE2   . HIS B 1 496 ? -14.075 -25.818 13.139  1.00 27.46 ? 496  HIS B NE2   1 
ATOM   7917 N N     . GLU B 1 497 ? -18.127 -20.440 12.792  1.00 28.20 ? 497  GLU B N     1 
ATOM   7918 C CA    . GLU B 1 497 ? -19.171 -19.491 12.307  1.00 26.16 ? 497  GLU B CA    1 
ATOM   7919 C C     . GLU B 1 497 ? -18.613 -18.065 12.249  1.00 26.48 ? 497  GLU B C     1 
ATOM   7920 O O     . GLU B 1 497 ? -18.882 -17.355 11.274  1.00 26.46 ? 497  GLU B O     1 
ATOM   7921 C CB    . GLU B 1 497 ? -20.418 -19.557 13.191  1.00 27.31 ? 497  GLU B CB    1 
ATOM   7922 C CG    . GLU B 1 497 ? -21.232 -20.823 12.979  1.00 28.23 ? 497  GLU B CG    1 
ATOM   7923 C CD    . GLU B 1 497 ? -22.285 -21.068 14.055  1.00 31.79 ? 497  GLU B CD    1 
ATOM   7924 O OE1   . GLU B 1 497 ? -22.302 -20.318 15.048  1.00 35.22 ? 497  GLU B OE1   1 
ATOM   7925 O OE2   . GLU B 1 497 ? -23.082 -22.002 13.901  1.00 29.54 ? 497  GLU B OE2   1 
ATOM   7926 N N     . ALA B 1 498 ? -17.886 -17.623 13.276  1.00 26.26 ? 498  ALA B N     1 
ATOM   7927 C CA    . ALA B 1 498 ? -17.263 -16.279 13.302  1.00 26.71 ? 498  ALA B CA    1 
ATOM   7928 C C     . ALA B 1 498 ? -16.353 -16.123 12.067  1.00 28.31 ? 498  ALA B C     1 
ATOM   7929 O O     . ALA B 1 498 ? -16.413 -15.101 11.363  1.00 27.36 ? 498  ALA B O     1 
ATOM   7930 C CB    . ALA B 1 498 ? -16.503 -16.082 14.597  1.00 26.90 ? 498  ALA B CB    1 
ATOM   7931 N N     . ILE B 1 499 ? -15.551 -17.126 11.773  1.00 26.40 ? 499  ILE B N     1 
ATOM   7932 C CA    . ILE B 1 499 ? -14.609 -17.051 10.622  1.00 25.68 ? 499  ILE B CA    1 
ATOM   7933 C C     . ILE B 1 499 ? -15.406 -17.094 9.307   1.00 26.31 ? 499  ILE B C     1 
ATOM   7934 O O     . ILE B 1 499 ? -15.103 -16.259 8.420   1.00 25.07 ? 499  ILE B O     1 
ATOM   7935 C CB    . ILE B 1 499 ? -13.514 -18.122 10.726  1.00 26.36 ? 499  ILE B CB    1 
ATOM   7936 C CG1   . ILE B 1 499 ? -12.568 -17.764 11.875  1.00 26.62 ? 499  ILE B CG1   1 
ATOM   7937 C CG2   . ILE B 1 499 ? -12.758 -18.254 9.409   1.00 25.62 ? 499  ILE B CG2   1 
ATOM   7938 C CD1   . ILE B 1 499 ? -11.601 -18.813 12.200  1.00 31.49 ? 499  ILE B CD1   1 
ATOM   7939 N N     . LYS B 1 500 ? -16.359 -18.013 9.174   1.00 24.78 ? 500  LYS B N     1 
ATOM   7940 C CA    . LYS B 1 500 ? -17.239 -18.094 7.977   1.00 25.94 ? 500  LYS B CA    1 
ATOM   7941 C C     . LYS B 1 500 ? -17.884 -16.733 7.681   1.00 26.70 ? 500  LYS B C     1 
ATOM   7942 O O     . LYS B 1 500 ? -17.859 -16.281 6.501   1.00 26.67 ? 500  LYS B O     1 
ATOM   7943 C CB    . LYS B 1 500 ? -18.298 -19.169 8.187   1.00 25.70 ? 500  LYS B CB    1 
ATOM   7944 C CG    . LYS B 1 500 ? -19.256 -19.325 7.022   1.00 24.05 ? 500  LYS B CG    1 
ATOM   7945 C CD    . LYS B 1 500 ? -18.558 -19.657 5.755   1.00 23.69 ? 500  LYS B CD    1 
ATOM   7946 C CE    . LYS B 1 500 ? -19.533 -20.181 4.722   1.00 24.18 ? 500  LYS B CE    1 
ATOM   7947 N NZ    . LYS B 1 500 ? -18.903 -20.303 3.391   1.00 24.96 ? 500  LYS B NZ    1 
ATOM   7948 N N     . ASP B 1 501 ? -18.466 -16.090 8.688   1.00 27.01 ? 501  ASP B N     1 
ATOM   7949 C CA    . ASP B 1 501 ? -19.212 -14.818 8.501   1.00 29.11 ? 501  ASP B CA    1 
ATOM   7950 C C     . ASP B 1 501 ? -18.233 -13.694 8.132   1.00 28.06 ? 501  ASP B C     1 
ATOM   7951 O O     . ASP B 1 501 ? -18.624 -12.857 7.306   1.00 29.96 ? 501  ASP B O     1 
ATOM   7952 C CB    . ASP B 1 501 ? -20.148 -14.522 9.684   1.00 29.84 ? 501  ASP B CB    1 
ATOM   7953 C CG    . ASP B 1 501 ? -21.348 -15.461 9.754   1.00 31.54 ? 501  ASP B CG    1 
ATOM   7954 O OD1   . ASP B 1 501 ? -21.829 -15.891 8.670   1.00 31.06 ? 501  ASP B OD1   1 
ATOM   7955 O OD2   . ASP B 1 501 ? -21.805 -15.767 10.886  1.00 32.41 ? 501  ASP B OD2   1 
ATOM   7956 N N     . ALA B 1 502 ? -16.999 -13.708 8.641   1.00 29.15 ? 502  ALA B N     1 
ATOM   7957 C CA    . ALA B 1 502 ? -15.978 -12.678 8.328   1.00 28.77 ? 502  ALA B CA    1 
ATOM   7958 C C     . ALA B 1 502 ? -15.522 -12.813 6.865   1.00 26.82 ? 502  ALA B C     1 
ATOM   7959 O O     . ALA B 1 502 ? -15.509 -11.801 6.154   1.00 30.55 ? 502  ALA B O     1 
ATOM   7960 C CB    . ALA B 1 502 ? -14.802 -12.781 9.264   1.00 30.46 ? 502  ALA B CB    1 
ATOM   7961 N N     . LEU B 1 503 ? -15.160 -14.021 6.452   1.00 26.70 ? 503  LEU B N     1 
ATOM   7962 C CA    . LEU B 1 503 ? -14.614 -14.316 5.101   1.00 26.73 ? 503  LEU B CA    1 
ATOM   7963 C C     . LEU B 1 503 ? -15.752 -14.317 4.071   1.00 28.12 ? 503  LEU B C     1 
ATOM   7964 O O     . LEU B 1 503 ? -15.463 -14.041 2.890   1.00 26.65 ? 503  LEU B O     1 
ATOM   7965 C CB    . LEU B 1 503 ? -13.902 -15.665 5.118   1.00 26.63 ? 503  LEU B CB    1 
ATOM   7966 C CG    . LEU B 1 503 ? -12.578 -15.707 5.888   1.00 27.95 ? 503  LEU B CG    1 
ATOM   7967 C CD1   . LEU B 1 503 ? -11.962 -17.092 5.804   1.00 28.06 ? 503  LEU B CD1   1 
ATOM   7968 C CD2   . LEU B 1 503 ? -11.597 -14.653 5.378   1.00 28.67 ? 503  LEU B CD2   1 
ATOM   7969 N N     . ASP B 1 504 ? -16.973 -14.651 4.494   1.00 26.12 ? 504  ASP B N     1 
ATOM   7970 C CA    . ASP B 1 504 ? -18.085 -14.943 3.566   1.00 29.29 ? 504  ASP B CA    1 
ATOM   7971 C C     . ASP B 1 504 ? -19.317 -14.181 4.030   1.00 27.26 ? 504  ASP B C     1 
ATOM   7972 O O     . ASP B 1 504 ? -20.302 -14.797 4.396   1.00 26.71 ? 504  ASP B O     1 
ATOM   7973 C CB    . ASP B 1 504 ? -18.316 -16.451 3.461   1.00 27.18 ? 504  ASP B CB    1 
ATOM   7974 C CG    . ASP B 1 504 ? -19.131 -16.848 2.239   1.00 28.86 ? 504  ASP B CG    1 
ATOM   7975 O OD1   . ASP B 1 504 ? -19.666 -15.932 1.522   1.00 29.28 ? 504  ASP B OD1   1 
ATOM   7976 O OD2   . ASP B 1 504 ? -19.239 -18.051 2.008   1.00 29.97 ? 504  ASP B OD2   1 
ATOM   7977 N N     . PRO B 1 505 ? -19.285 -12.833 4.060   1.00 29.29 ? 505  PRO B N     1 
ATOM   7978 C CA    . PRO B 1 505 ? -20.404 -12.058 4.599   1.00 31.93 ? 505  PRO B CA    1 
ATOM   7979 C C     . PRO B 1 505 ? -21.724 -12.218 3.823   1.00 30.99 ? 505  PRO B C     1 
ATOM   7980 O O     . PRO B 1 505 ? -22.757 -12.018 4.424   1.00 31.24 ? 505  PRO B O     1 
ATOM   7981 C CB    . PRO B 1 505 ? -19.893 -10.615 4.534   1.00 29.82 ? 505  PRO B CB    1 
ATOM   7982 C CG    . PRO B 1 505 ? -18.896 -10.641 3.406   1.00 32.00 ? 505  PRO B CG    1 
ATOM   7983 C CD    . PRO B 1 505 ? -18.202 -11.979 3.550   1.00 29.51 ? 505  PRO B CD    1 
ATOM   7984 N N     . ASN B 1 506 ? -21.671 -12.587 2.535   1.00 31.94 ? 506  ASN B N     1 
ATOM   7985 C CA    . ASN B 1 506 ? -22.871 -12.818 1.690   1.00 32.01 ? 506  ASN B CA    1 
ATOM   7986 C C     . ASN B 1 506 ? -23.279 -14.300 1.730   1.00 31.63 ? 506  ASN B C     1 
ATOM   7987 O O     . ASN B 1 506 ? -24.268 -14.654 1.083   1.00 29.51 ? 506  ASN B O     1 
ATOM   7988 C CB    . ASN B 1 506 ? -22.659 -12.293 0.269   1.00 33.54 ? 506  ASN B CB    1 
ATOM   7989 C CG    . ASN B 1 506 ? -22.360 -10.807 0.251   1.00 36.25 ? 506  ASN B CG    1 
ATOM   7990 O OD1   . ASN B 1 506 ? -22.971 -10.026 0.973   1.00 38.36 ? 506  ASN B OD1   1 
ATOM   7991 N ND2   . ASN B 1 506 ? -21.377 -10.408 -0.530  1.00 34.03 ? 506  ASN B ND2   1 
ATOM   7992 N N     . GLY B 1 507 ? -22.548 -15.149 2.465   1.00 30.78 ? 507  GLY B N     1 
ATOM   7993 C CA    . GLY B 1 507 ? -22.935 -16.556 2.715   1.00 30.36 ? 507  GLY B CA    1 
ATOM   7994 C C     . GLY B 1 507 ? -23.048 -17.358 1.428   1.00 30.92 ? 507  GLY B C     1 
ATOM   7995 O O     . GLY B 1 507 ? -24.096 -17.995 1.188   1.00 28.44 ? 507  GLY B O     1 
ATOM   7996 N N     . ILE B 1 508 ? -21.980 -17.365 0.636   1.00 30.32 ? 508  ILE B N     1 
ATOM   7997 C CA    . ILE B 1 508 ? -21.958 -17.941 -0.738  1.00 29.75 ? 508  ILE B CA    1 
ATOM   7998 C C     . ILE B 1 508 ? -21.403 -19.374 -0.751  1.00 30.90 ? 508  ILE B C     1 
ATOM   7999 O O     . ILE B 1 508 ? -22.070 -20.231 -1.351  1.00 31.66 ? 508  ILE B O     1 
ATOM   8000 C CB    . ILE B 1 508 ? -21.153 -17.008 -1.657  1.00 30.55 ? 508  ILE B CB    1 
ATOM   8001 C CG1   . ILE B 1 508 ? -21.778 -15.612 -1.688  1.00 31.92 ? 508  ILE B CG1   1 
ATOM   8002 C CG2   . ILE B 1 508 ? -20.971 -17.621 -3.037  1.00 32.26 ? 508  ILE B CG2   1 
ATOM   8003 C CD1   . ILE B 1 508 ? -23.242 -15.582 -2.079  1.00 31.78 ? 508  ILE B CD1   1 
ATOM   8004 N N     . ILE B 1 509 ? -20.228 -19.643 -0.166  1.00 27.45 ? 509  ILE B N     1 
ATOM   8005 C CA    . ILE B 1 509 ? -19.490 -20.923 -0.425  1.00 29.11 ? 509  ILE B CA    1 
ATOM   8006 C C     . ILE B 1 509 ? -20.070 -22.056 0.423   1.00 25.21 ? 509  ILE B C     1 
ATOM   8007 O O     . ILE B 1 509 ? -20.130 -21.898 1.661   1.00 28.00 ? 509  ILE B O     1 
ATOM   8008 C CB    . ILE B 1 509 ? -17.972 -20.792 -0.187  1.00 30.16 ? 509  ILE B CB    1 
ATOM   8009 C CG1   . ILE B 1 509 ? -17.368 -19.614 -0.951  1.00 30.91 ? 509  ILE B CG1   1 
ATOM   8010 C CG2   . ILE B 1 509 ? -17.274 -22.096 -0.518  1.00 31.63 ? 509  ILE B CG2   1 
ATOM   8011 C CD1   . ILE B 1 509 ? -17.477 -19.749 -2.444  1.00 32.15 ? 509  ILE B CD1   1 
ATOM   8012 N N     . ALA B 1 510 ? -20.402 -23.170 -0.248  1.00 25.45 ? 510  ALA B N     1 
ATOM   8013 C CA    . ALA B 1 510 ? -20.857 -24.491 0.276   1.00 24.54 ? 510  ALA B CA    1 
ATOM   8014 C C     . ALA B 1 510 ? -21.486 -24.376 1.664   1.00 26.74 ? 510  ALA B C     1 
ATOM   8015 O O     . ALA B 1 510 ? -20.978 -24.963 2.621   1.00 26.06 ? 510  ALA B O     1 
ATOM   8016 C CB    . ALA B 1 510 ? -19.700 -25.459 0.280   1.00 26.10 ? 510  ALA B CB    1 
ATOM   8017 N N     . PRO B 1 511 ? -22.611 -23.638 1.810   1.00 29.66 ? 511  PRO B N     1 
ATOM   8018 C CA    . PRO B 1 511 ? -23.252 -23.450 3.104   1.00 29.12 ? 511  PRO B CA    1 
ATOM   8019 C C     . PRO B 1 511 ? -23.590 -24.803 3.736   1.00 27.60 ? 511  PRO B C     1 
ATOM   8020 O O     . PRO B 1 511 ? -24.055 -25.711 3.047   1.00 29.30 ? 511  PRO B O     1 
ATOM   8021 C CB    . PRO B 1 511 ? -24.502 -22.615 2.779   1.00 30.23 ? 511  PRO B CB    1 
ATOM   8022 C CG    . PRO B 1 511 ? -24.147 -21.922 1.512   1.00 30.09 ? 511  PRO B CG    1 
ATOM   8023 C CD    . PRO B 1 511 ? -23.369 -22.963 0.728   1.00 30.66 ? 511  PRO B CD    1 
ATOM   8024 N N     . GLY B 1 512 ? -23.303 -24.919 5.034   1.00 25.10 ? 512  GLY B N     1 
ATOM   8025 C CA    . GLY B 1 512 ? -23.595 -26.119 5.830   1.00 27.40 ? 512  GLY B CA    1 
ATOM   8026 C C     . GLY B 1 512 ? -22.516 -27.186 5.760   1.00 27.24 ? 512  GLY B C     1 
ATOM   8027 O O     . GLY B 1 512 ? -22.679 -28.209 6.449   1.00 22.86 ? 512  GLY B O     1 
ATOM   8028 N N     . LYS B 1 513 ? -21.452 -26.989 4.970   1.00 27.84 ? 513  LYS B N     1 
ATOM   8029 C CA    . LYS B 1 513 ? -20.341 -27.964 4.937   1.00 26.98 ? 513  LYS B CA    1 
ATOM   8030 C C     . LYS B 1 513 ? -19.829 -28.123 6.371   1.00 25.04 ? 513  LYS B C     1 
ATOM   8031 O O     . LYS B 1 513 ? -19.583 -27.101 6.977   1.00 25.81 ? 513  LYS B O     1 
ATOM   8032 C CB    . LYS B 1 513 ? -19.208 -27.490 4.025   1.00 26.12 ? 513  LYS B CB    1 
ATOM   8033 C CG    . LYS B 1 513 ? -17.962 -28.371 4.036   1.00 27.39 ? 513  LYS B CG    1 
ATOM   8034 C CD    . LYS B 1 513 ? -18.205 -29.828 3.657   1.00 26.50 ? 513  LYS B CD    1 
ATOM   8035 C CE    . LYS B 1 513 ? -16.929 -30.644 3.716   1.00 26.99 ? 513  LYS B CE    1 
ATOM   8036 N NZ    . LYS B 1 513 ? -17.147 -32.072 3.379   1.00 26.43 ? 513  LYS B NZ    1 
ATOM   8037 N N     . SER B 1 514 ? -19.695 -29.359 6.863   1.00 24.89 ? 514  SER B N     1 
ATOM   8038 C CA    . SER B 1 514 ? -19.203 -29.669 8.232   1.00 25.55 ? 514  SER B CA    1 
ATOM   8039 C C     . SER B 1 514 ? -20.092 -29.008 9.299   1.00 26.22 ? 514  SER B C     1 
ATOM   8040 O O     . SER B 1 514 ? -19.611 -28.813 10.423  1.00 22.80 ? 514  SER B O     1 
ATOM   8041 C CB    . SER B 1 514 ? -17.768 -29.221 8.398   1.00 24.52 ? 514  SER B CB    1 
ATOM   8042 O OG    . SER B 1 514 ? -16.912 -29.858 7.461   1.00 24.59 ? 514  SER B OG    1 
ATOM   8043 N N     . GLY B 1 515 ? -21.352 -28.707 8.981   1.00 27.03 ? 515  GLY B N     1 
ATOM   8044 C CA    . GLY B 1 515 ? -22.285 -28.052 9.915   1.00 26.40 ? 515  GLY B CA    1 
ATOM   8045 C C     . GLY B 1 515 ? -22.012 -26.567 10.077  1.00 26.34 ? 515  GLY B C     1 
ATOM   8046 O O     . GLY B 1 515 ? -22.584 -25.992 11.020  1.00 26.09 ? 515  GLY B O     1 
ATOM   8047 N N     . VAL B 1 516 ? -21.198 -25.945 9.210   1.00 23.70 ? 516  VAL B N     1 
ATOM   8048 C CA    . VAL B 1 516 ? -20.879 -24.500 9.315   1.00 25.87 ? 516  VAL B CA    1 
ATOM   8049 C C     . VAL B 1 516 ? -21.766 -23.726 8.340   1.00 27.80 ? 516  VAL B C     1 
ATOM   8050 O O     . VAL B 1 516 ? -21.519 -23.779 7.100   1.00 27.03 ? 516  VAL B O     1 
ATOM   8051 C CB    . VAL B 1 516 ? -19.390 -24.186 9.096   1.00 23.23 ? 516  VAL B CB    1 
ATOM   8052 C CG1   . VAL B 1 516 ? -19.108 -22.723 9.368   1.00 23.93 ? 516  VAL B CG1   1 
ATOM   8053 C CG2   . VAL B 1 516 ? -18.513 -25.072 9.965   1.00 24.49 ? 516  VAL B CG2   1 
ATOM   8054 N N     . TRP B 1 517 ? -22.739 -23.011 8.893   1.00 27.11 ? 517  TRP B N     1 
ATOM   8055 C CA    . TRP B 1 517 ? -23.734 -22.253 8.103   1.00 30.22 ? 517  TRP B CA    1 
ATOM   8056 C C     . TRP B 1 517 ? -23.373 -20.795 8.215   1.00 29.23 ? 517  TRP B C     1 
ATOM   8057 O O     . TRP B 1 517 ? -23.166 -20.309 9.325   1.00 32.28 ? 517  TRP B O     1 
ATOM   8058 C CB    . TRP B 1 517 ? -25.157 -22.511 8.610   1.00 31.21 ? 517  TRP B CB    1 
ATOM   8059 C CG    . TRP B 1 517 ? -25.619 -23.908 8.368   1.00 29.29 ? 517  TRP B CG    1 
ATOM   8060 C CD1   . TRP B 1 517 ? -25.540 -24.967 9.225   1.00 29.17 ? 517  TRP B CD1   1 
ATOM   8061 C CD2   . TRP B 1 517 ? -26.218 -24.404 7.163   1.00 27.77 ? 517  TRP B CD2   1 
ATOM   8062 N NE1   . TRP B 1 517 ? -26.077 -26.079 8.649   1.00 28.54 ? 517  TRP B NE1   1 
ATOM   8063 C CE2   . TRP B 1 517 ? -26.492 -25.769 7.381   1.00 29.97 ? 517  TRP B CE2   1 
ATOM   8064 C CE3   . TRP B 1 517 ? -26.502 -23.846 5.921   1.00 29.02 ? 517  TRP B CE3   1 
ATOM   8065 C CZ2   . TRP B 1 517 ? -27.051 -26.579 6.400   1.00 27.68 ? 517  TRP B CZ2   1 
ATOM   8066 C CZ3   . TRP B 1 517 ? -27.096 -24.637 4.960   1.00 29.47 ? 517  TRP B CZ3   1 
ATOM   8067 C CH2   . TRP B 1 517 ? -27.348 -25.983 5.193   1.00 29.58 ? 517  TRP B CH2   1 
ATOM   8068 N N     . PRO B 1 518 ? -23.358 -20.043 7.102   1.00 30.06 ? 518  PRO B N     1 
ATOM   8069 C CA    . PRO B 1 518 ? -23.283 -18.594 7.189   1.00 29.56 ? 518  PRO B CA    1 
ATOM   8070 C C     . PRO B 1 518 ? -24.600 -18.084 7.777   1.00 31.19 ? 518  PRO B C     1 
ATOM   8071 O O     . PRO B 1 518 ? -25.601 -18.778 7.643   1.00 32.08 ? 518  PRO B O     1 
ATOM   8072 C CB    . PRO B 1 518 ? -23.117 -18.151 5.733   1.00 31.82 ? 518  PRO B CB    1 
ATOM   8073 C CG    . PRO B 1 518 ? -23.804 -19.246 4.942   1.00 30.84 ? 518  PRO B CG    1 
ATOM   8074 C CD    . PRO B 1 518 ? -23.554 -20.516 5.727   1.00 29.82 ? 518  PRO B CD    1 
ATOM   8075 N N     . ALA B 1 519 ? -24.556 -16.893 8.366   1.00 29.77 ? 519  ALA B N     1 
ATOM   8076 C CA    . ALA B 1 519 ? -25.658 -16.211 9.075   1.00 34.55 ? 519  ALA B CA    1 
ATOM   8077 C C     . ALA B 1 519 ? -26.981 -16.341 8.294   1.00 33.44 ? 519  ALA B C     1 
ATOM   8078 O O     . ALA B 1 519 ? -27.973 -16.721 8.890   1.00 33.79 ? 519  ALA B O     1 
ATOM   8079 C CB    . ALA B 1 519 ? -25.273 -14.768 9.278   1.00 30.71 ? 519  ALA B CB    1 
ATOM   8080 N N     . ARG B 1 520 ? -27.006 -16.074 6.991   1.00 36.33 ? 520  ARG B N     1 
ATOM   8081 C CA    . ARG B 1 520 ? -28.303 -15.958 6.266   1.00 39.29 ? 520  ARG B CA    1 
ATOM   8082 C C     . ARG B 1 520 ? -29.006 -17.328 6.160   1.00 39.64 ? 520  ARG B C     1 
ATOM   8083 O O     . ARG B 1 520 ? -30.218 -17.334 5.856   1.00 35.93 ? 520  ARG B O     1 
ATOM   8084 C CB    . ARG B 1 520 ? -28.088 -15.303 4.898   1.00 37.73 ? 520  ARG B CB    1 
ATOM   8085 C CG    . ARG B 1 520 ? -27.389 -16.178 3.876   1.00 37.70 ? 520  ARG B CG    1 
ATOM   8086 C CD    . ARG B 1 520 ? -27.528 -15.501 2.527   1.00 39.86 ? 520  ARG B CD    1 
ATOM   8087 N NE    . ARG B 1 520 ? -26.794 -16.218 1.513   1.00 35.44 ? 520  ARG B NE    1 
ATOM   8088 C CZ    . ARG B 1 520 ? -27.170 -16.409 0.257   1.00 34.67 ? 520  ARG B CZ    1 
ATOM   8089 N NH1   . ARG B 1 520 ? -28.329 -15.955 -0.194  1.00 37.30 ? 520  ARG B NH1   1 
ATOM   8090 N NH2   . ARG B 1 520 ? -26.372 -17.076 -0.555  1.00 38.02 ? 520  ARG B NH2   1 
ATOM   8091 N N     . TYR B 1 521 ? -28.305 -18.451 6.372   1.00 37.27 ? 521  TYR B N     1 
ATOM   8092 C CA    . TYR B 1 521 ? -28.857 -19.821 6.198   1.00 36.07 ? 521  TYR B CA    1 
ATOM   8093 C C     . TYR B 1 521 ? -28.882 -20.589 7.517   1.00 36.29 ? 521  TYR B C     1 
ATOM   8094 O O     . TYR B 1 521 ? -29.401 -21.715 7.535   1.00 47.38 ? 521  TYR B O     1 
ATOM   8095 C CB    . TYR B 1 521 ? -28.046 -20.633 5.190   1.00 35.95 ? 521  TYR B CB    1 
ATOM   8096 C CG    . TYR B 1 521 ? -28.237 -20.217 3.758   1.00 35.47 ? 521  TYR B CG    1 
ATOM   8097 C CD1   . TYR B 1 521 ? -29.501 -20.166 3.177   1.00 35.51 ? 521  TYR B CD1   1 
ATOM   8098 C CD2   . TYR B 1 521 ? -27.146 -19.949 2.956   1.00 33.67 ? 521  TYR B CD2   1 
ATOM   8099 C CE1   . TYR B 1 521 ? -29.669 -19.813 1.846   1.00 35.24 ? 521  TYR B CE1   1 
ATOM   8100 C CE2   . TYR B 1 521 ? -27.295 -19.597 1.626   1.00 33.76 ? 521  TYR B CE2   1 
ATOM   8101 C CZ    . TYR B 1 521 ? -28.559 -19.539 1.067   1.00 35.22 ? 521  TYR B CZ    1 
ATOM   8102 O OH    . TYR B 1 521 ? -28.693 -19.197 -0.237  1.00 34.61 ? 521  TYR B OH    1 
ATOM   8103 N N     . ARG B 1 522 ? -28.354 -20.010 8.591   1.00 35.07 ? 522  ARG B N     1 
ATOM   8104 C CA    . ARG B 1 522 ? -28.120 -20.753 9.853   1.00 34.99 ? 522  ARG B CA    1 
ATOM   8105 C C     . ARG B 1 522 ? -29.436 -20.831 10.614  1.00 33.95 ? 522  ARG B C     1 
ATOM   8106 O O     . ARG B 1 522 ? -30.165 -19.839 10.593  1.00 37.00 ? 522  ARG B O     1 
ATOM   8107 C CB    . ARG B 1 522 ? -27.012 -20.069 10.659  1.00 37.28 ? 522  ARG B CB    1 
ATOM   8108 C CG    . ARG B 1 522 ? -26.756 -20.706 12.019  1.00 37.25 ? 522  ARG B CG    1 
ATOM   8109 C CD    . ARG B 1 522 ? -25.697 -19.978 12.835  1.00 35.57 ? 522  ARG B CD    1 
ATOM   8110 N NE    . ARG B 1 522 ? -24.639 -19.554 11.940  1.00 36.43 ? 522  ARG B NE    1 
ATOM   8111 C CZ    . ARG B 1 522 ? -24.034 -18.371 11.947  1.00 36.18 ? 522  ARG B CZ    1 
ATOM   8112 N NH1   . ARG B 1 522 ? -24.350 -17.444 12.831  1.00 35.82 ? 522  ARG B NH1   1 
ATOM   8113 N NH2   . ARG B 1 522 ? -23.109 -18.113 11.047  1.00 31.41 ? 522  ARG B NH2   1 
ATOM   8114 N N     . GLY B 1 523 ? -29.713 -21.974 11.238  1.00 37.85 ? 523  GLY B N     1 
ATOM   8115 C CA    . GLY B 1 523 ? -30.904 -22.199 12.083  1.00 40.21 ? 523  GLY B CA    1 
ATOM   8116 C C     . GLY B 1 523 ? -32.206 -22.180 11.288  1.00 41.10 ? 523  GLY B C     1 
ATOM   8117 O O     . GLY B 1 523 ? -33.245 -21.926 11.906  1.00 52.29 ? 523  GLY B O     1 
ATOM   8118 N N     . LYS B 1 524 ? -32.176 -22.469 9.986   1.00 43.62 ? 524  LYS B N     1 
ATOM   8119 C CA    . LYS B 1 524 ? -33.372 -22.468 9.097   1.00 42.79 ? 524  LYS B CA    1 
ATOM   8120 C C     . LYS B 1 524 ? -33.795 -23.916 8.797   1.00 43.58 ? 524  LYS B C     1 
ATOM   8121 O O     . LYS B 1 524 ? -34.688 -24.105 7.969   1.00 41.86 ? 524  LYS B O     1 
ATOM   8122 C CB    . LYS B 1 524 ? -33.068 -21.734 7.788   1.00 44.59 ? 524  LYS B CB    1 
ATOM   8123 C CG    . LYS B 1 524 ? -32.539 -20.311 7.924   1.00 49.51 ? 524  LYS B CG    1 
ATOM   8124 C CD    . LYS B 1 524 ? -33.604 -19.286 8.282   1.00 54.79 ? 524  LYS B CD    1 
ATOM   8125 C CE    . LYS B 1 524 ? -33.266 -17.865 7.861   1.00 56.22 ? 524  LYS B CE    1 
ATOM   8126 N NZ    . LYS B 1 524 ? -33.262 -17.721 6.386   1.00 60.19 ? 524  LYS B NZ    1 
ATOM   8127 N N     . GLY B 1 525 ? -33.151 -24.905 9.425   1.00 44.91 ? 525  GLY B N     1 
ATOM   8128 C CA    . GLY B 1 525 ? -33.372 -26.337 9.155   1.00 42.52 ? 525  GLY B CA    1 
ATOM   8129 C C     . GLY B 1 525 ? -33.136 -26.686 7.696   1.00 47.83 ? 525  GLY B C     1 
ATOM   8130 O O     . GLY B 1 525 ? -33.719 -27.702 7.262   1.00 43.57 ? 525  GLY B O     1 
ATOM   8131 N N     . LEU B 1 526 ? -32.297 -25.888 7.003   1.00 47.29 ? 526  LEU B N     1 
ATOM   8132 C CA    . LEU B 1 526 ? -31.989 -25.896 5.542   1.00 48.21 ? 526  LEU B CA    1 
ATOM   8133 C C     . LEU B 1 526 ? -32.818 -24.842 4.792   1.00 54.61 ? 526  LEU B C     1 
ATOM   8134 O O     . LEU B 1 526 ? -32.262 -23.860 4.324   1.00 60.91 ? 526  LEU B O     1 
ATOM   8135 C CB    . LEU B 1 526 ? -32.256 -27.291 4.988   1.00 53.05 ? 526  LEU B CB    1 
ATOM   8136 C CG    . LEU B 1 526 ? -31.107 -28.269 5.189   1.00 44.80 ? 526  LEU B CG    1 
ATOM   8137 C CD1   . LEU B 1 526 ? -30.056 -28.000 4.152   1.00 46.97 ? 526  LEU B CD1   1 
ATOM   8138 C CD2   . LEU B 1 526 ? -30.536 -28.173 6.593   1.00 39.49 ? 526  LEU B CD2   1 
HETATM 8139 P PA    . FAD C 2 .   ? 8.152   -18.234 24.223  1.00 22.23 ? 601  FAD A PA    1 
HETATM 8140 O O1A   . FAD C 2 .   ? 9.062   -17.047 24.153  1.00 20.67 ? 601  FAD A O1A   1 
HETATM 8141 O O2A   . FAD C 2 .   ? 7.422   -18.493 25.510  1.00 19.62 ? 601  FAD A O2A   1 
HETATM 8142 O O5B   . FAD C 2 .   ? 7.053   -18.132 23.065  1.00 19.82 ? 601  FAD A O5B   1 
HETATM 8143 C C5B   . FAD C 2 .   ? 7.406   -17.917 21.683  1.00 21.41 ? 601  FAD A C5B   1 
HETATM 8144 C C4B   . FAD C 2 .   ? 6.277   -17.154 21.034  1.00 20.14 ? 601  FAD A C4B   1 
HETATM 8145 O O4B   . FAD C 2 .   ? 5.084   -17.982 20.984  1.00 20.04 ? 601  FAD A O4B   1 
HETATM 8146 C C3B   . FAD C 2 .   ? 5.830   -15.879 21.759  1.00 20.47 ? 601  FAD A C3B   1 
HETATM 8147 O O3B   . FAD C 2 .   ? 6.712   -14.792 21.475  1.00 20.75 ? 601  FAD A O3B   1 
HETATM 8148 C C2B   . FAD C 2 .   ? 4.395   -15.733 21.236  1.00 20.89 ? 601  FAD A C2B   1 
HETATM 8149 O O2B   . FAD C 2 .   ? 4.337   -15.237 19.910  1.00 20.69 ? 601  FAD A O2B   1 
HETATM 8150 C C1B   . FAD C 2 .   ? 3.931   -17.189 21.238  1.00 20.89 ? 601  FAD A C1B   1 
HETATM 8151 N N9A   . FAD C 2 .   ? 3.309   -17.700 22.467  1.00 20.40 ? 601  FAD A N9A   1 
HETATM 8152 C C8A   . FAD C 2 .   ? 3.963   -18.268 23.526  1.00 21.00 ? 601  FAD A C8A   1 
HETATM 8153 N N7A   . FAD C 2 .   ? 3.142   -18.718 24.451  1.00 19.10 ? 601  FAD A N7A   1 
HETATM 8154 C C5A   . FAD C 2 .   ? 1.875   -18.547 23.905  1.00 18.57 ? 601  FAD A C5A   1 
HETATM 8155 C C6A   . FAD C 2 .   ? 0.586   -18.845 24.395  1.00 18.60 ? 601  FAD A C6A   1 
HETATM 8156 N N6A   . FAD C 2 .   ? 0.385   -19.488 25.549  1.00 17.41 ? 601  FAD A N6A   1 
HETATM 8157 N N1A   . FAD C 2 .   ? -0.478  -18.571 23.591  1.00 16.95 ? 601  FAD A N1A   1 
HETATM 8158 C C2A   . FAD C 2 .   ? -0.240  -17.954 22.418  1.00 19.47 ? 601  FAD A C2A   1 
HETATM 8159 N N3A   . FAD C 2 .   ? 0.932   -17.594 21.879  1.00 20.48 ? 601  FAD A N3A   1 
HETATM 8160 C C4A   . FAD C 2 .   ? 1.966   -17.930 22.675  1.00 19.62 ? 601  FAD A C4A   1 
HETATM 8161 N N1    . FAD C 2 .   ? 14.849  -22.071 18.332  1.00 21.51 ? 601  FAD A N1    1 
HETATM 8162 C C2    . FAD C 2 .   ? 14.560  -23.253 17.833  1.00 22.76 ? 601  FAD A C2    1 
HETATM 8163 O O2    . FAD C 2 .   ? 13.411  -23.524 17.479  1.00 22.03 ? 601  FAD A O2    1 
HETATM 8164 N N3    . FAD C 2 .   ? 15.505  -24.195 17.654  1.00 22.16 ? 601  FAD A N3    1 
HETATM 8165 C C4    . FAD C 2 .   ? 16.813  -24.024 18.032  1.00 23.50 ? 601  FAD A C4    1 
HETATM 8166 O O4    . FAD C 2 .   ? 17.599  -24.971 17.941  1.00 22.41 ? 601  FAD A O4    1 
HETATM 8167 C C4X   . FAD C 2 .   ? 17.170  -22.772 18.533  1.00 23.21 ? 601  FAD A C4X   1 
HETATM 8168 N N5    . FAD C 2 .   ? 18.417  -22.561 18.889  1.00 24.32 ? 601  FAD A N5    1 
HETATM 8169 C C5X   . FAD C 2 .   ? 18.730  -21.308 19.352  1.00 24.70 ? 601  FAD A C5X   1 
HETATM 8170 C C6    . FAD C 2 .   ? 20.080  -21.034 19.655  1.00 26.90 ? 601  FAD A C6    1 
HETATM 8171 C C7    . FAD C 2 .   ? 20.477  -19.800 20.132  1.00 27.20 ? 601  FAD A C7    1 
HETATM 8172 C C7M   . FAD C 2 .   ? 21.936  -19.542 20.404  1.00 27.80 ? 601  FAD A C7M   1 
HETATM 8173 C C8    . FAD C 2 .   ? 19.492  -18.792 20.340  1.00 25.91 ? 601  FAD A C8    1 
HETATM 8174 C C8M   . FAD C 2 .   ? 19.855  -17.455 20.920  1.00 29.25 ? 601  FAD A C8M   1 
HETATM 8175 C C9    . FAD C 2 .   ? 18.165  -19.057 20.069  1.00 24.00 ? 601  FAD A C9    1 
HETATM 8176 C C9A   . FAD C 2 .   ? 17.752  -20.306 19.573  1.00 25.55 ? 601  FAD A C9A   1 
HETATM 8177 N N10   . FAD C 2 .   ? 16.416  -20.582 19.236  1.00 22.68 ? 601  FAD A N10   1 
HETATM 8178 C C10   . FAD C 2 .   ? 16.092  -21.824 18.680  1.00 22.65 ? 601  FAD A C10   1 
HETATM 8179 C "C1'" . FAD C 2 .   ? 15.374  -19.537 19.365  1.00 23.87 ? 601  FAD A "C1'" 1 
HETATM 8180 C "C2'" . FAD C 2 .   ? 14.694  -19.535 20.721  1.00 24.43 ? 601  FAD A "C2'" 1 
HETATM 8181 O "O2'" . FAD C 2 .   ? 15.704  -19.438 21.695  1.00 32.59 ? 601  FAD A "O2'" 1 
HETATM 8182 C "C3'" . FAD C 2 .   ? 13.878  -20.804 21.007  1.00 22.29 ? 601  FAD A "C3'" 1 
HETATM 8183 O "O3'" . FAD C 2 .   ? 13.010  -21.121 19.886  1.00 22.75 ? 601  FAD A "O3'" 1 
HETATM 8184 C "C4'" . FAD C 2 .   ? 13.037  -20.740 22.294  1.00 21.91 ? 601  FAD A "C4'" 1 
HETATM 8185 O "O4'" . FAD C 2 .   ? 12.670  -22.055 22.716  1.00 22.44 ? 601  FAD A "O4'" 1 
HETATM 8186 C "C5'" . FAD C 2 .   ? 11.761  -19.957 22.112  1.00 20.34 ? 601  FAD A "C5'" 1 
HETATM 8187 O "O5'" . FAD C 2 .   ? 11.360  -19.349 23.355  1.00 20.89 ? 601  FAD A "O5'" 1 
HETATM 8188 P P     . FAD C 2 .   ? 10.336  -20.131 24.310  1.00 21.85 ? 601  FAD A P     1 
HETATM 8189 O O1P   . FAD C 2 .   ? 10.576  -19.621 25.709  1.00 22.09 ? 601  FAD A O1P   1 
HETATM 8190 O O2P   . FAD C 2 .   ? 10.414  -21.604 24.059  1.00 22.22 ? 601  FAD A O2P   1 
HETATM 8191 O O3P   . FAD C 2 .   ? 8.949   -19.555 23.825  1.00 20.76 ? 601  FAD A O3P   1 
HETATM 8192 C CAI   . V55 D 3 .   ? 19.404  -21.651 16.003  1.00 44.13 ? 602  V55 A CAI   1 
HETATM 8193 C CAG   . V55 D 3 .   ? 18.906  -20.355 16.123  1.00 43.28 ? 602  V55 A CAG   1 
HETATM 8194 C CAK   . V55 D 3 .   ? 17.637  -20.122 15.679  1.00 41.91 ? 602  V55 A CAK   1 
HETATM 8195 C CAJ   . V55 D 3 .   ? 16.871  -21.158 15.138  1.00 45.03 ? 602  V55 A CAJ   1 
HETATM 8196 C CAF   . V55 D 3 .   ? 17.349  -22.446 15.032  1.00 34.71 ? 602  V55 A CAF   1 
HETATM 8197 O OAB   . V55 D 3 .   ? 21.546  -20.797 16.266  1.00 50.94 ? 602  V55 A OAB   1 
HETATM 8198 C CAE   . V55 D 3 .   ? 18.632  -22.683 15.487  1.00 38.59 ? 602  V55 A CAE   1 
HETATM 8199 C CAD   . V55 D 3 .   ? 20.678  -21.929 16.444  1.00 43.75 ? 602  V55 A CAD   1 
HETATM 8200 C CAA   . V55 D 3 .   ? 17.529  -17.936 16.640  1.00 42.69 ? 602  V55 A CAA   1 
HETATM 8201 O OAH   . V55 D 3 .   ? 17.045  -18.891 15.712  1.00 49.15 ? 602  V55 A OAH   1 
HETATM 8202 O OAC   . V55 D 3 .   ? 15.609  -20.814 14.732  1.00 52.80 ? 602  V55 A OAC   1 
HETATM 8203 P PA    . FAD E 2 .   ? -14.367 -34.426 -4.497  1.00 27.37 ? 601  FAD B PA    1 
HETATM 8204 O O1A   . FAD E 2 .   ? -15.698 -35.106 -4.327  1.00 28.05 ? 601  FAD B O1A   1 
HETATM 8205 O O2A   . FAD E 2 .   ? -14.108 -33.656 -5.756  1.00 26.84 ? 601  FAD B O2A   1 
HETATM 8206 O O5B   . FAD E 2 .   ? -14.052 -33.419 -3.266  1.00 26.64 ? 601  FAD B O5B   1 
HETATM 8207 C C5B   . FAD E 2 .   ? -14.367 -33.829 -1.891  1.00 27.42 ? 601  FAD B C5B   1 
HETATM 8208 C C4B   . FAD E 2 .   ? -14.832 -32.612 -1.122  1.00 26.54 ? 601  FAD B C4B   1 
HETATM 8209 O O4B   . FAD E 2 .   ? -13.772 -31.621 -1.054  1.00 25.32 ? 601  FAD B O4B   1 
HETATM 8210 C C3B   . FAD E 2 .   ? -16.019 -31.844 -1.713  1.00 29.37 ? 601  FAD B C3B   1 
HETATM 8211 O O3B   . FAD E 2 .   ? -17.274 -32.431 -1.369  1.00 27.93 ? 601  FAD B O3B   1 
HETATM 8212 C C2B   . FAD E 2 .   ? -15.818 -30.445 -1.116  1.00 28.46 ? 601  FAD B C2B   1 
HETATM 8213 O O2B   . FAD E 2 .   ? -16.292 -30.342 0.212   1.00 26.40 ? 601  FAD B O2B   1 
HETATM 8214 C C1B   . FAD E 2 .   ? -14.294 -30.315 -1.161  1.00 26.43 ? 601  FAD B C1B   1 
HETATM 8215 N N9A   . FAD E 2 .   ? -13.717 -29.739 -2.389  1.00 25.49 ? 601  FAD B N9A   1 
HETATM 8216 C C8A   . FAD E 2 .   ? -13.491 -30.404 -3.573  1.00 28.11 ? 601  FAD B C8A   1 
HETATM 8217 N N7A   . FAD E 2 .   ? -12.880 -29.657 -4.463  1.00 27.51 ? 601  FAD B N7A   1 
HETATM 8218 C C5A   . FAD E 2 .   ? -12.693 -28.442 -3.824  1.00 24.88 ? 601  FAD B C5A   1 
HETATM 8219 C C6A   . FAD E 2 .   ? -12.090 -27.247 -4.240  1.00 26.76 ? 601  FAD B C6A   1 
HETATM 8220 N N6A   . FAD E 2 .   ? -11.517 -27.094 -5.436  1.00 25.36 ? 601  FAD B N6A   1 
HETATM 8221 N N1A   . FAD E 2 .   ? -12.055 -26.222 -3.352  1.00 26.87 ? 601  FAD B N1A   1 
HETATM 8222 C C2A   . FAD E 2 .   ? -12.642 -26.391 -2.162  1.00 29.20 ? 601  FAD B C2A   1 
HETATM 8223 N N3A   . FAD E 2 .   ? -13.216 -27.478 -1.654  1.00 26.55 ? 601  FAD B N3A   1 
HETATM 8224 C C4A   . FAD E 2 .   ? -13.215 -28.480 -2.551  1.00 26.15 ? 601  FAD B C4A   1 
HETATM 8225 N N1    . FAD E 2 .   ? -11.909 -42.173 0.731   1.00 29.15 ? 601  FAD B N1    1 
HETATM 8226 C C2    . FAD E 2 .   ? -10.649 -42.175 1.217   1.00 28.27 ? 601  FAD B C2    1 
HETATM 8227 O O2    . FAD E 2 .   ? -10.152 -41.130 1.648   1.00 25.58 ? 601  FAD B O2    1 
HETATM 8228 N N3    . FAD E 2 .   ? -9.892  -43.307 1.265   1.00 27.24 ? 601  FAD B N3    1 
HETATM 8229 C C4    . FAD E 2 .   ? -10.366 -44.519 0.787   1.00 29.85 ? 601  FAD B C4    1 
HETATM 8230 O O4    . FAD E 2 .   ? -9.641  -45.513 0.783   1.00 28.66 ? 601  FAD B O4    1 
HETATM 8231 C C4X   . FAD E 2 .   ? -11.712 -44.564 0.330   1.00 30.30 ? 601  FAD B C4X   1 
HETATM 8232 N N5    . FAD E 2 .   ? -12.210 -45.716 -0.062  1.00 32.05 ? 601  FAD B N5    1 
HETATM 8233 C C5X   . FAD E 2 .   ? -13.513 -45.728 -0.478  1.00 31.43 ? 601  FAD B C5X   1 
HETATM 8234 C C6    . FAD E 2 .   ? -14.082 -46.966 -0.855  1.00 35.56 ? 601  FAD B C6    1 
HETATM 8235 C C7    . FAD E 2 .   ? -15.390 -47.065 -1.291  1.00 34.70 ? 601  FAD B C7    1 
HETATM 8236 C C7M   . FAD E 2 .   ? -15.980 -48.398 -1.690  1.00 35.55 ? 601  FAD B C7M   1 
HETATM 8237 C C8    . FAD E 2 .   ? -16.164 -45.905 -1.374  1.00 32.93 ? 601  FAD B C8    1 
HETATM 8238 C C8M   . FAD E 2 .   ? -17.560 -45.969 -1.932  1.00 34.64 ? 601  FAD B C8M   1 
HETATM 8239 C C9    . FAD E 2 .   ? -15.621 -44.673 -1.006  1.00 33.13 ? 601  FAD B C9    1 
HETATM 8240 C C9A   . FAD E 2 .   ? -14.298 -44.558 -0.536  1.00 32.39 ? 601  FAD B C9A   1 
HETATM 8241 N N10   . FAD E 2 .   ? -13.723 -43.342 -0.136  1.00 31.59 ? 601  FAD B N10   1 
HETATM 8242 C C10   . FAD E 2 .   ? -12.424 -43.313 0.323   1.00 32.18 ? 601  FAD B C10   1 
HETATM 8243 C "C1'" . FAD E 2 .   ? -14.501 -42.085 -0.154  1.00 31.03 ? 601  FAD B "C1'" 1 
HETATM 8244 C "C2'" . FAD E 2 .   ? -14.419 -41.361 -1.478  1.00 31.57 ? 601  FAD B "C2'" 1 
HETATM 8245 O "O2'" . FAD E 2 .   ? -14.784 -42.271 -2.475  1.00 40.44 ? 601  FAD B "O2'" 1 
HETATM 8246 C "C3'" . FAD E 2 .   ? -13.011 -40.835 -1.801  1.00 27.54 ? 601  FAD B "C3'" 1 
HETATM 8247 O "O3'" . FAD E 2 .   ? -12.523 -40.060 -0.704  1.00 26.63 ? 601  FAD B "O3'" 1 
HETATM 8248 C "C4'" . FAD E 2 .   ? -12.936 -39.934 -3.039  1.00 25.89 ? 601  FAD B "C4'" 1 
HETATM 8249 O "O4'" . FAD E 2 .   ? -11.562 -39.859 -3.434  1.00 27.71 ? 601  FAD B "O4'" 1 
HETATM 8250 C "C5'" . FAD E 2 .   ? -13.462 -38.543 -2.745  1.00 27.87 ? 601  FAD B "C5'" 1 
HETATM 8251 O "O5'" . FAD E 2 .   ? -14.030 -37.866 -3.920  1.00 27.28 ? 601  FAD B "O5'" 1 
HETATM 8252 P P     . FAD E 2 .   ? -13.063 -36.992 -4.848  1.00 27.26 ? 601  FAD B P     1 
HETATM 8253 O O1P   . FAD E 2 .   ? -13.706 -36.945 -6.215  1.00 27.66 ? 601  FAD B O1P   1 
HETATM 8254 O O2P   . FAD E 2 .   ? -11.660 -37.446 -4.696  1.00 28.93 ? 601  FAD B O2P   1 
HETATM 8255 O O3P   . FAD E 2 .   ? -13.235 -35.531 -4.279  1.00 26.49 ? 601  FAD B O3P   1 
HETATM 8256 C CAI   . V55 F 3 .   ? -12.793 -46.473 3.119   1.00 50.64 ? 602  V55 B CAI   1 
HETATM 8257 C CAG   . V55 F 3 .   ? -13.986 -45.811 2.899   1.00 51.45 ? 602  V55 B CAG   1 
HETATM 8258 C CAK   . V55 F 3 .   ? -14.100 -44.495 3.372   1.00 51.75 ? 602  V55 B CAK   1 
HETATM 8259 C CAJ   . V55 F 3 .   ? -13.041 -43.869 4.034   1.00 53.01 ? 602  V55 B CAJ   1 
HETATM 8260 C CAF   . V55 F 3 .   ? -11.856 -44.537 4.243   1.00 50.08 ? 602  V55 B CAF   1 
HETATM 8261 O OAB   . V55 F 3 .   ? -13.791 -48.475 2.511   1.00 53.60 ? 602  V55 B OAB   1 
HETATM 8262 C CAE   . V55 F 3 .   ? -11.753 -45.831 3.779   1.00 48.79 ? 602  V55 B CAE   1 
HETATM 8263 C CAD   . V55 F 3 .   ? -12.583 -47.766 2.687   1.00 49.86 ? 602  V55 B CAD   1 
HETATM 8264 C CAA   . V55 F 3 .   ? -16.368 -44.509 2.811   1.00 61.77 ? 602  V55 B CAA   1 
HETATM 8265 O OAH   . V55 F 3 .   ? -15.218 -43.736 3.216   1.00 58.43 ? 602  V55 B OAH   1 
HETATM 8266 O OAC   . V55 F 3 .   ? -13.213 -42.590 4.464   1.00 55.63 ? 602  V55 B OAC   1 
HETATM 8267 O O     . HOH G 4 .   ? 8.389   -30.948 8.808   1.00 34.95 ? 701  HOH A O     1 
HETATM 8268 O O     . HOH G 4 .   ? 7.011   -46.274 24.901  1.00 34.38 ? 702  HOH A O     1 
HETATM 8269 O O     . HOH G 4 .   ? 35.447  -27.785 -2.711  1.00 45.24 ? 703  HOH A O     1 
HETATM 8270 O O     . HOH G 4 .   ? -5.573  -36.210 26.524  1.00 32.54 ? 704  HOH A O     1 
HETATM 8271 O O     . HOH G 4 .   ? 0.177   -30.836 14.376  1.00 26.01 ? 705  HOH A O     1 
HETATM 8272 O O     . HOH G 4 .   ? -9.919  -6.512  8.511   1.00 32.33 ? 706  HOH A O     1 
HETATM 8273 O O     . HOH G 4 .   ? 30.035  -2.039  24.191  1.00 44.66 ? 707  HOH A O     1 
HETATM 8274 O O     . HOH G 4 .   ? -3.220  -41.174 29.510  1.00 49.65 ? 708  HOH A O     1 
HETATM 8275 O O     . HOH G 4 .   ? -12.511 -5.809  39.232  1.00 28.47 ? 709  HOH A O     1 
HETATM 8276 O O     . HOH G 4 .   ? 0.246   -32.131 12.821  1.00 34.22 ? 710  HOH A O     1 
HETATM 8277 O O     . HOH G 4 .   ? -8.469  1.959   25.955  1.00 33.11 ? 711  HOH A O     1 
HETATM 8278 O O     . HOH G 4 .   ? 13.343  -25.799 33.571  1.00 33.88 ? 712  HOH A O     1 
HETATM 8279 O O     . HOH G 4 .   ? 21.017  -33.975 -4.701  1.00 33.32 ? 713  HOH A O     1 
HETATM 8280 O O     . HOH G 4 .   ? -2.066  -29.631 15.125  1.00 28.75 ? 714  HOH A O     1 
HETATM 8281 O O     . HOH G 4 .   ? 8.085   -14.651 23.613  1.00 20.86 ? 715  HOH A O     1 
HETATM 8282 O O     . HOH G 4 .   ? -13.156 -9.141  9.526   1.00 31.35 ? 716  HOH A O     1 
HETATM 8283 O O     . HOH G 4 .   ? 38.489  -33.141 11.241  1.00 42.30 ? 717  HOH A O     1 
HETATM 8284 O O     . HOH G 4 .   ? 8.661   -15.101 13.616  1.00 36.28 ? 718  HOH A O     1 
HETATM 8285 O O     . HOH G 4 .   ? -8.272  1.222   40.705  1.00 36.60 ? 719  HOH A O     1 
HETATM 8286 O O     . HOH G 4 .   ? -13.810 -26.907 21.547  1.00 21.46 ? 720  HOH A O     1 
HETATM 8287 O O     . HOH G 4 .   ? 6.871   -27.877 34.746  1.00 35.90 ? 721  HOH A O     1 
HETATM 8288 O O     . HOH G 4 .   ? 7.109   -1.377  10.831  1.00 37.22 ? 722  HOH A O     1 
HETATM 8289 O O     . HOH G 4 .   ? 29.919  -39.356 24.411  1.00 39.91 ? 723  HOH A O     1 
HETATM 8290 O O     . HOH G 4 .   ? 26.832  -17.355 27.429  1.00 42.50 ? 724  HOH A O     1 
HETATM 8291 O O     . HOH G 4 .   ? 11.906  -46.800 23.932  1.00 29.49 ? 725  HOH A O     1 
HETATM 8292 O O     . HOH G 4 .   ? 14.096  -21.475 8.939   1.00 33.88 ? 726  HOH A O     1 
HETATM 8293 O O     . HOH G 4 .   ? 1.091   -34.281 12.447  1.00 44.99 ? 727  HOH A O     1 
HETATM 8294 O O     . HOH G 4 .   ? 8.632   -6.089  3.072   1.00 24.35 ? 728  HOH A O     1 
HETATM 8295 O O     . HOH G 4 .   ? 14.280  -40.937 10.637  1.00 39.90 ? 729  HOH A O     1 
HETATM 8296 O O     . HOH G 4 .   ? 6.861   -46.662 33.059  1.00 40.26 ? 730  HOH A O     1 
HETATM 8297 O O     . HOH G 4 .   ? 25.888  -12.122 25.720  1.00 37.20 ? 731  HOH A O     1 
HETATM 8298 O O     . HOH G 4 .   ? 12.015  -1.245  33.566  1.00 33.50 ? 732  HOH A O     1 
HETATM 8299 O O     . HOH G 4 .   ? 16.061  -21.339 -6.028  1.00 26.59 ? 733  HOH A O     1 
HETATM 8300 O O     . HOH G 4 .   ? 11.711  -44.726 18.008  1.00 44.87 ? 734  HOH A O     1 
HETATM 8301 O O     . HOH G 4 .   ? -15.041 -7.605  28.367  1.00 44.13 ? 735  HOH A O     1 
HETATM 8302 O O     . HOH G 4 .   ? -8.799  -7.619  5.070   1.00 32.78 ? 736  HOH A O     1 
HETATM 8303 O O     . HOH G 4 .   ? 34.045  -17.261 6.475   1.00 32.93 ? 737  HOH A O     1 
HETATM 8304 O O     . HOH G 4 .   ? 8.277   -28.044 21.266  1.00 21.35 ? 738  HOH A O     1 
HETATM 8305 O O     . HOH G 4 .   ? 9.753   -36.874 20.931  1.00 20.15 ? 739  HOH A O     1 
HETATM 8306 O O     . HOH G 4 .   ? 8.747   -10.376 -1.750  1.00 32.14 ? 740  HOH A O     1 
HETATM 8307 O O     . HOH G 4 .   ? -0.038  -4.024  -5.197  1.00 39.13 ? 741  HOH A O     1 
HETATM 8308 O O     . HOH G 4 .   ? 12.994  -20.825 31.106  1.00 29.85 ? 742  HOH A O     1 
HETATM 8309 O O     . HOH G 4 .   ? 4.189   -17.298 18.060  1.00 24.54 ? 743  HOH A O     1 
HETATM 8310 O O     . HOH G 4 .   ? 36.592  -31.670 2.405   1.00 35.77 ? 744  HOH A O     1 
HETATM 8311 O O     . HOH G 4 .   ? 13.594  -39.009 27.999  1.00 35.45 ? 745  HOH A O     1 
HETATM 8312 O O     . HOH G 4 .   ? 31.843  -6.735  21.799  1.00 40.11 ? 746  HOH A O     1 
HETATM 8313 O O     . HOH G 4 .   ? 4.951   -9.786  43.023  1.00 39.64 ? 747  HOH A O     1 
HETATM 8314 O O     . HOH G 4 .   ? 24.818  -2.091  2.169   1.00 39.71 ? 748  HOH A O     1 
HETATM 8315 O O     . HOH G 4 .   ? 37.079  -31.357 -1.328  1.00 33.18 ? 749  HOH A O     1 
HETATM 8316 O O     . HOH G 4 .   ? 6.652   -13.306 19.002  1.00 21.60 ? 750  HOH A O     1 
HETATM 8317 O O     . HOH G 4 .   ? 23.294  -27.018 14.851  1.00 32.61 ? 751  HOH A O     1 
HETATM 8318 O O     . HOH G 4 .   ? 21.144  -25.474 16.002  1.00 28.29 ? 752  HOH A O     1 
HETATM 8319 O O     . HOH G 4 .   ? -12.017 -2.008  24.032  1.00 32.86 ? 753  HOH A O     1 
HETATM 8320 O O     . HOH G 4 .   ? -12.500 -39.815 19.414  1.00 31.95 ? 754  HOH A O     1 
HETATM 8321 O O     . HOH G 4 .   ? 2.317   -5.411  8.756   1.00 20.35 ? 755  HOH A O     1 
HETATM 8322 O O     . HOH G 4 .   ? 0.967   -23.065 39.610  1.00 38.75 ? 756  HOH A O     1 
HETATM 8323 O O     . HOH G 4 .   ? -1.472  -40.296 14.976  1.00 29.58 ? 757  HOH A O     1 
HETATM 8324 O O     . HOH G 4 .   ? -10.068 -1.688  22.043  1.00 29.99 ? 758  HOH A O     1 
HETATM 8325 O O     . HOH G 4 .   ? 9.517   -32.287 35.603  1.00 33.56 ? 759  HOH A O     1 
HETATM 8326 O O     . HOH G 4 .   ? 17.903  -21.381 3.117   1.00 24.73 ? 760  HOH A O     1 
HETATM 8327 O O     . HOH G 4 .   ? 23.930  -27.948 -7.028  1.00 25.77 ? 761  HOH A O     1 
HETATM 8328 O O     . HOH G 4 .   ? -10.912 -1.575  38.141  1.00 37.19 ? 762  HOH A O     1 
HETATM 8329 O O     . HOH G 4 .   ? -13.192 -16.927 33.649  1.00 30.31 ? 763  HOH A O     1 
HETATM 8330 O O     . HOH G 4 .   ? 3.716   3.074   25.099  1.00 42.08 ? 764  HOH A O     1 
HETATM 8331 O O     . HOH G 4 .   ? 16.592  -18.630 -6.827  1.00 30.52 ? 765  HOH A O     1 
HETATM 8332 O O     . HOH G 4 .   ? 0.204   -1.247  9.946   1.00 33.68 ? 766  HOH A O     1 
HETATM 8333 O O     . HOH G 4 .   ? 16.243  -32.313 19.440  1.00 21.36 ? 767  HOH A O     1 
HETATM 8334 O O     . HOH G 4 .   ? 1.577   -3.550  40.336  1.00 33.75 ? 768  HOH A O     1 
HETATM 8335 O O     . HOH G 4 .   ? 29.891  -10.555 14.700  1.00 33.65 ? 769  HOH A O     1 
HETATM 8336 O O     . HOH G 4 .   ? 7.077   -17.832 32.118  1.00 30.55 ? 770  HOH A O     1 
HETATM 8337 O O     . HOH G 4 .   ? 26.706  -50.040 4.738   1.00 40.53 ? 771  HOH A O     1 
HETATM 8338 O O     . HOH G 4 .   ? 0.255   -14.860 20.579  1.00 24.89 ? 772  HOH A O     1 
HETATM 8339 O O     . HOH G 4 .   ? -7.148  -4.881  43.412  1.00 26.72 ? 773  HOH A O     1 
HETATM 8340 O O     . HOH G 4 .   ? 34.196  -42.770 12.436  1.00 35.17 ? 774  HOH A O     1 
HETATM 8341 O O     . HOH G 4 .   ? 27.106  -31.094 -6.417  1.00 41.94 ? 775  HOH A O     1 
HETATM 8342 O O     . HOH G 4 .   ? -13.102 -22.168 31.474  1.00 45.03 ? 776  HOH A O     1 
HETATM 8343 O O     . HOH G 4 .   ? -12.853 -28.336 13.372  1.00 26.12 ? 777  HOH A O     1 
HETATM 8344 O O     . HOH G 4 .   ? 17.689  -41.826 22.280  1.00 50.51 ? 778  HOH A O     1 
HETATM 8345 O O     . HOH G 4 .   ? 20.242  -31.197 -4.174  1.00 30.88 ? 779  HOH A O     1 
HETATM 8346 O O     . HOH G 4 .   ? 18.578  0.054   15.061  1.00 42.76 ? 780  HOH A O     1 
HETATM 8347 O O     . HOH G 4 .   ? 8.368   -22.343 33.655  1.00 33.51 ? 781  HOH A O     1 
HETATM 8348 O O     . HOH G 4 .   ? 4.047   0.655   33.407  1.00 32.39 ? 782  HOH A O     1 
HETATM 8349 O O     . HOH G 4 .   ? 32.579  -18.301 23.252  1.00 32.27 ? 783  HOH A O     1 
HETATM 8350 O O     . HOH G 4 .   ? -16.299 -22.278 25.907  1.00 28.74 ? 784  HOH A O     1 
HETATM 8351 O O     . HOH G 4 .   ? 26.946  -30.577 26.055  1.00 32.45 ? 785  HOH A O     1 
HETATM 8352 O O     . HOH G 4 .   ? 32.541  -10.281 8.750   1.00 36.41 ? 786  HOH A O     1 
HETATM 8353 O O     . HOH G 4 .   ? 4.867   -6.238  13.152  1.00 22.73 ? 787  HOH A O     1 
HETATM 8354 O O     . HOH G 4 .   ? 38.253  -32.428 7.161   1.00 33.91 ? 788  HOH A O     1 
HETATM 8355 O O     . HOH G 4 .   ? 17.190  -24.779 -7.289  1.00 28.03 ? 789  HOH A O     1 
HETATM 8356 O O     . HOH G 4 .   ? 16.263  -19.517 24.302  1.00 39.15 ? 790  HOH A O     1 
HETATM 8357 O O     . HOH G 4 .   ? 14.802  -12.637 10.182  1.00 26.85 ? 791  HOH A O     1 
HETATM 8358 O O     . HOH G 4 .   ? 14.091  -37.302 36.389  1.00 30.36 ? 792  HOH A O     1 
HETATM 8359 O O     . HOH G 4 .   ? 3.666   -6.180  6.484   1.00 27.01 ? 793  HOH A O     1 
HETATM 8360 O O     . HOH G 4 .   ? 26.731  -44.639 0.015   1.00 35.09 ? 794  HOH A O     1 
HETATM 8361 O O     . HOH G 4 .   ? 1.205   0.348   13.468  1.00 31.41 ? 795  HOH A O     1 
HETATM 8362 O O     . HOH G 4 .   ? 2.746   -6.574  44.587  1.00 42.36 ? 796  HOH A O     1 
HETATM 8363 O O     . HOH G 4 .   ? 9.190   -47.945 30.461  1.00 43.03 ? 797  HOH A O     1 
HETATM 8364 O O     . HOH G 4 .   ? 38.410  -10.144 17.821  1.00 44.24 ? 798  HOH A O     1 
HETATM 8365 O O     . HOH G 4 .   ? 15.174  -28.483 12.802  1.00 31.80 ? 799  HOH A O     1 
HETATM 8366 O O     . HOH G 4 .   ? -8.178  4.518   27.416  1.00 31.13 ? 800  HOH A O     1 
HETATM 8367 O O     . HOH G 4 .   ? 18.879  -10.783 -4.311  1.00 32.23 ? 801  HOH A O     1 
HETATM 8368 O O     . HOH G 4 .   ? -8.716  -26.549 32.793  1.00 33.71 ? 802  HOH A O     1 
HETATM 8369 O O     . HOH G 4 .   ? 0.036   -5.651  42.051  1.00 35.04 ? 803  HOH A O     1 
HETATM 8370 O O     . HOH G 4 .   ? 8.034   8.556   33.910  1.00 49.28 ? 804  HOH A O     1 
HETATM 8371 O O     . HOH G 4 .   ? 8.261   -5.076  12.693  1.00 18.55 ? 805  HOH A O     1 
HETATM 8372 O O     . HOH G 4 .   ? 13.748  -36.671 26.681  1.00 29.99 ? 806  HOH A O     1 
HETATM 8373 O O     . HOH G 4 .   ? 16.607  -39.065 26.129  1.00 39.54 ? 807  HOH A O     1 
HETATM 8374 O O     . HOH G 4 .   ? -15.795 -20.164 29.651  1.00 36.73 ? 808  HOH A O     1 
HETATM 8375 O O     . HOH G 4 .   ? 15.038  -22.627 24.135  1.00 28.68 ? 809  HOH A O     1 
HETATM 8376 O O     . HOH G 4 .   ? -7.146  -33.811 18.401  1.00 22.84 ? 810  HOH A O     1 
HETATM 8377 O O     . HOH G 4 .   ? -10.487 -25.962 30.637  1.00 30.44 ? 811  HOH A O     1 
HETATM 8378 O O     . HOH G 4 .   ? 1.009   -17.736 34.939  1.00 23.25 ? 812  HOH A O     1 
HETATM 8379 O O     . HOH G 4 .   ? 29.931  -48.460 9.647   1.00 43.55 ? 813  HOH A O     1 
HETATM 8380 O O     . HOH G 4 .   ? -11.699 -32.501 25.718  1.00 25.17 ? 814  HOH A O     1 
HETATM 8381 O O     . HOH G 4 .   ? -3.135  -13.117 13.176  1.00 27.42 ? 815  HOH A O     1 
HETATM 8382 O O     . HOH G 4 .   ? 16.679  -40.570 1.796   1.00 26.91 ? 816  HOH A O     1 
HETATM 8383 O O     . HOH G 4 .   ? 12.846  -8.317  -1.771  1.00 31.74 ? 817  HOH A O     1 
HETATM 8384 O O     . HOH G 4 .   ? 13.906  -5.444  20.986  1.00 31.88 ? 818  HOH A O     1 
HETATM 8385 O O     . HOH G 4 .   ? -13.446 -14.015 19.617  1.00 38.85 ? 819  HOH A O     1 
HETATM 8386 O O     . HOH G 4 .   ? -8.131  -24.798 34.660  1.00 51.19 ? 820  HOH A O     1 
HETATM 8387 O O     . HOH G 4 .   ? 18.965  -46.106 5.220   1.00 42.74 ? 821  HOH A O     1 
HETATM 8388 O O     . HOH G 4 .   ? 25.336  -20.887 -6.921  1.00 31.69 ? 822  HOH A O     1 
HETATM 8389 O O     . HOH G 4 .   ? 5.483   -10.186 25.212  1.00 20.61 ? 823  HOH A O     1 
HETATM 8390 O O     . HOH G 4 .   ? -13.503 -9.361  36.459  1.00 39.47 ? 824  HOH A O     1 
HETATM 8391 O O     . HOH G 4 .   ? -4.180  0.273   39.482  1.00 25.85 ? 825  HOH A O     1 
HETATM 8392 O O     . HOH G 4 .   ? -4.171  -30.625 16.724  1.00 26.58 ? 826  HOH A O     1 
HETATM 8393 O O     . HOH G 4 .   ? 12.176  -36.981 19.930  1.00 22.28 ? 827  HOH A O     1 
HETATM 8394 O O     . HOH G 4 .   ? 8.317   -11.728 22.285  1.00 22.02 ? 828  HOH A O     1 
HETATM 8395 O O     . HOH G 4 .   ? -11.544 -12.739 42.085  1.00 25.38 ? 829  HOH A O     1 
HETATM 8396 O O     . HOH G 4 .   ? 32.217  -30.763 17.422  1.00 32.20 ? 830  HOH A O     1 
HETATM 8397 O O     . HOH G 4 .   ? 17.072  -40.622 -2.496  1.00 29.58 ? 831  HOH A O     1 
HETATM 8398 O O     . HOH G 4 .   ? 36.676  -11.835 24.356  1.00 40.69 ? 832  HOH A O     1 
HETATM 8399 O O     . HOH G 4 .   ? -15.902 -13.781 26.799  1.00 36.58 ? 833  HOH A O     1 
HETATM 8400 O O     . HOH G 4 .   ? 1.188   -18.115 18.277  1.00 22.98 ? 834  HOH A O     1 
HETATM 8401 O O     . HOH G 4 .   ? 3.398   -11.308 36.616  1.00 30.41 ? 835  HOH A O     1 
HETATM 8402 O O     . HOH G 4 .   ? -11.597 -8.155  20.840  1.00 23.95 ? 836  HOH A O     1 
HETATM 8403 O O     . HOH G 4 .   ? -13.593 -14.875 22.076  1.00 23.14 ? 837  HOH A O     1 
HETATM 8404 O O     . HOH G 4 .   ? 8.481   -32.537 18.757  1.00 20.84 ? 838  HOH A O     1 
HETATM 8405 O O     . HOH G 4 .   ? 28.194  -13.720 13.952  1.00 40.84 ? 839  HOH A O     1 
HETATM 8406 O O     . HOH G 4 .   ? -14.611 -9.711  25.957  1.00 27.07 ? 840  HOH A O     1 
HETATM 8407 O O     . HOH G 4 .   ? -3.271  -5.364  4.549   1.00 41.94 ? 841  HOH A O     1 
HETATM 8408 O O     . HOH G 4 .   ? 4.081   -21.149 39.914  1.00 40.12 ? 842  HOH A O     1 
HETATM 8409 O O     . HOH G 4 .   ? 7.478   -26.351 14.110  1.00 23.89 ? 843  HOH A O     1 
HETATM 8410 O O     . HOH G 4 .   ? -1.755  -5.551  9.574   1.00 25.61 ? 844  HOH A O     1 
HETATM 8411 O O     . HOH G 4 .   ? -7.720  -29.775 15.259  1.00 25.61 ? 845  HOH A O     1 
HETATM 8412 O O     . HOH G 4 .   ? 3.172   -48.767 22.398  1.00 31.08 ? 846  HOH A O     1 
HETATM 8413 O O     . HOH G 4 .   ? 29.765  -30.754 24.886  1.00 43.77 ? 847  HOH A O     1 
HETATM 8414 O O     . HOH G 4 .   ? 5.315   -26.313 27.561  1.00 19.98 ? 848  HOH A O     1 
HETATM 8415 O O     . HOH G 4 .   ? 27.548  -36.544 24.491  1.00 31.05 ? 849  HOH A O     1 
HETATM 8416 O O     . HOH G 4 .   ? 13.067  -11.082 27.362  1.00 28.93 ? 850  HOH A O     1 
HETATM 8417 O O     . HOH G 4 .   ? 23.548  -27.689 30.002  1.00 45.90 ? 851  HOH A O     1 
HETATM 8418 O O     . HOH G 4 .   ? 11.395  -13.836 -5.563  1.00 22.07 ? 852  HOH A O     1 
HETATM 8419 O O     . HOH G 4 .   ? -1.972  -6.617  2.449   1.00 33.55 ? 853  HOH A O     1 
HETATM 8420 O O     . HOH G 4 .   ? -0.068  -6.688  48.543  1.00 44.28 ? 854  HOH A O     1 
HETATM 8421 O O     . HOH G 4 .   ? 0.204   -34.508 15.264  1.00 30.05 ? 855  HOH A O     1 
HETATM 8422 O O     . HOH G 4 .   ? 20.687  -46.278 11.855  1.00 30.40 ? 856  HOH A O     1 
HETATM 8423 O O     . HOH G 4 .   ? -2.174  1.887   38.611  1.00 31.88 ? 857  HOH A O     1 
HETATM 8424 O O     . HOH G 4 .   ? -19.276 -37.105 23.766  1.00 35.54 ? 858  HOH A O     1 
HETATM 8425 O O     . HOH G 4 .   ? -1.481  6.007   26.126  1.00 39.60 ? 859  HOH A O     1 
HETATM 8426 O O     . HOH G 4 .   ? 20.286  -17.192 2.831   1.00 25.43 ? 860  HOH A O     1 
HETATM 8427 O O     . HOH G 4 .   ? 8.104   -34.545 20.621  1.00 19.90 ? 861  HOH A O     1 
HETATM 8428 O O     . HOH G 4 .   ? -16.629 -16.161 27.576  1.00 39.97 ? 862  HOH A O     1 
HETATM 8429 O O     . HOH G 4 .   ? 8.422   -0.372  30.821  1.00 33.36 ? 863  HOH A O     1 
HETATM 8430 O O     . HOH G 4 .   ? 2.294   -6.980  20.471  1.00 17.73 ? 864  HOH A O     1 
HETATM 8431 O O     . HOH G 4 .   ? 36.480  -12.049 21.713  1.00 31.98 ? 865  HOH A O     1 
HETATM 8432 O O     . HOH G 4 .   ? -0.176  -37.241 18.221  1.00 24.18 ? 866  HOH A O     1 
HETATM 8433 O O     . HOH G 4 .   ? 7.072   -8.727  -3.802  1.00 23.68 ? 867  HOH A O     1 
HETATM 8434 O O     . HOH G 4 .   ? 14.698  -14.329 27.458  1.00 32.53 ? 868  HOH A O     1 
HETATM 8435 O O     . HOH G 4 .   ? 19.397  -32.606 30.488  1.00 40.12 ? 869  HOH A O     1 
HETATM 8436 O O     . HOH G 4 .   ? -5.442  -8.180  -2.376  1.00 34.20 ? 870  HOH A O     1 
HETATM 8437 O O     . HOH G 4 .   ? 20.304  -12.555 1.797   1.00 23.50 ? 871  HOH A O     1 
HETATM 8438 O O     . HOH G 4 .   ? 7.524   -6.462  -0.512  1.00 48.32 ? 872  HOH A O     1 
HETATM 8439 O O     . HOH G 4 .   ? 31.306  -28.644 -3.814  1.00 32.85 ? 873  HOH A O     1 
HETATM 8440 O O     . HOH G 4 .   ? -8.696  4.663   37.251  1.00 39.17 ? 874  HOH A O     1 
HETATM 8441 O O     . HOH G 4 .   ? 13.436  -13.266 2.795   1.00 20.16 ? 875  HOH A O     1 
HETATM 8442 O O     . HOH G 4 .   ? 2.217   -8.627  2.732   1.00 26.51 ? 876  HOH A O     1 
HETATM 8443 O O     . HOH G 4 .   ? 18.862  -15.610 -9.612  1.00 32.78 ? 877  HOH A O     1 
HETATM 8444 O O     . HOH G 4 .   ? -8.029  -5.704  6.262   1.00 34.43 ? 878  HOH A O     1 
HETATM 8445 O O     . HOH G 4 .   ? -11.139 -1.836  17.811  1.00 29.22 ? 879  HOH A O     1 
HETATM 8446 O O     . HOH G 4 .   ? 5.752   -12.277 23.249  1.00 21.48 ? 880  HOH A O     1 
HETATM 8447 O O     . HOH G 4 .   ? 22.407  -11.020 0.864   1.00 23.87 ? 881  HOH A O     1 
HETATM 8448 O O     . HOH G 4 .   ? 10.896  -13.241 3.791   1.00 21.82 ? 882  HOH A O     1 
HETATM 8449 O O     . HOH G 4 .   ? 3.912   1.451   20.970  1.00 36.20 ? 883  HOH A O     1 
HETATM 8450 O O     . HOH G 4 .   ? -6.990  -1.879  6.568   1.00 44.03 ? 884  HOH A O     1 
HETATM 8451 O O     . HOH G 4 .   ? 38.074  -23.079 2.126   1.00 39.00 ? 885  HOH A O     1 
HETATM 8452 O O     . HOH G 4 .   ? 10.616  -39.772 -0.722  1.00 24.39 ? 886  HOH A O     1 
HETATM 8453 O O     . HOH G 4 .   ? 8.658   -14.943 15.763  1.00 24.31 ? 887  HOH A O     1 
HETATM 8454 O O     . HOH G 4 .   ? 23.102  -26.548 23.863  1.00 25.54 ? 888  HOH A O     1 
HETATM 8455 O O     . HOH G 4 .   ? -6.311  -23.798 39.103  1.00 36.43 ? 889  HOH A O     1 
HETATM 8456 O O     . HOH G 4 .   ? 9.529   -34.058 12.617  1.00 24.73 ? 890  HOH A O     1 
HETATM 8457 O O     . HOH G 4 .   ? 18.678  -28.340 24.487  1.00 27.29 ? 891  HOH A O     1 
HETATM 8458 O O     . HOH G 4 .   ? 32.029  -8.082  1.593   1.00 39.32 ? 892  HOH A O     1 
HETATM 8459 O O     . HOH G 4 .   ? 2.234   -17.273 46.303  1.00 45.48 ? 893  HOH A O     1 
HETATM 8460 O O     . HOH G 4 .   ? -9.679  -19.688 38.303  1.00 27.39 ? 894  HOH A O     1 
HETATM 8461 O O     . HOH G 4 .   ? -11.655 -8.191  37.918  1.00 29.02 ? 895  HOH A O     1 
HETATM 8462 O O     . HOH G 4 .   ? 22.005  -9.077  27.075  1.00 37.10 ? 896  HOH A O     1 
HETATM 8463 O O     . HOH G 4 .   ? 9.148   -33.100 22.684  1.00 21.15 ? 897  HOH A O     1 
HETATM 8464 O O     . HOH G 4 .   ? 18.508  -44.461 22.222  1.00 46.27 ? 898  HOH A O     1 
HETATM 8465 O O     . HOH G 4 .   ? -0.557  -19.804 41.840  1.00 24.65 ? 899  HOH A O     1 
HETATM 8466 O O     . HOH G 4 .   ? -15.604 -8.350  23.970  1.00 33.92 ? 900  HOH A O     1 
HETATM 8467 O O     . HOH G 4 .   ? -13.206 -31.500 15.894  1.00 40.57 ? 901  HOH A O     1 
HETATM 8468 O O     . HOH G 4 .   ? 13.042  -4.791  25.352  1.00 29.57 ? 902  HOH A O     1 
HETATM 8469 O O     . HOH G 4 .   ? 33.076  -16.654 8.564   1.00 40.62 ? 903  HOH A O     1 
HETATM 8470 O O     . HOH G 4 .   ? 29.510  -19.343 -5.578  1.00 53.34 ? 904  HOH A O     1 
HETATM 8471 O O     . HOH G 4 .   ? 41.434  -30.928 23.084  1.00 48.11 ? 905  HOH A O     1 
HETATM 8472 O O     . HOH G 4 .   ? 2.065   -13.315 47.866  1.00 48.90 ? 906  HOH A O     1 
HETATM 8473 O O     . HOH G 4 .   ? 21.646  5.574   16.991  1.00 42.67 ? 907  HOH A O     1 
HETATM 8474 O O     . HOH G 4 .   ? 3.370   -6.771  42.313  1.00 41.10 ? 908  HOH A O     1 
HETATM 8475 O O     . HOH G 4 .   ? 8.958   -30.830 21.022  1.00 23.21 ? 909  HOH A O     1 
HETATM 8476 O O     . HOH G 4 .   ? 46.676  -19.674 9.423   1.00 39.08 ? 910  HOH A O     1 
HETATM 8477 O O     . HOH G 4 .   ? 17.077  -23.090 21.696  1.00 23.08 ? 911  HOH A O     1 
HETATM 8478 O O     . HOH G 4 .   ? 5.661   -10.660 19.049  1.00 22.47 ? 912  HOH A O     1 
HETATM 8479 O O     . HOH G 4 .   ? 5.800   -43.129 20.837  1.00 25.98 ? 913  HOH A O     1 
HETATM 8480 O O     . HOH G 4 .   ? 17.520  -46.958 8.026   1.00 35.90 ? 914  HOH A O     1 
HETATM 8481 O O     . HOH G 4 .   ? 23.830  -36.562 -5.270  1.00 45.21 ? 915  HOH A O     1 
HETATM 8482 O O     . HOH G 4 .   ? 9.903   -5.635  27.332  1.00 32.88 ? 916  HOH A O     1 
HETATM 8483 O O     . HOH G 4 .   ? 13.317  -44.804 4.131   1.00 44.30 ? 917  HOH A O     1 
HETATM 8484 O O     . HOH G 4 .   ? 37.925  -40.081 8.771   1.00 45.48 ? 918  HOH A O     1 
HETATM 8485 O O     . HOH G 4 .   ? 13.845  -43.751 8.896   1.00 45.80 ? 919  HOH A O     1 
HETATM 8486 O O     . HOH G 4 .   ? -5.076  -13.931 11.221  1.00 27.34 ? 920  HOH A O     1 
HETATM 8487 O O     . HOH G 4 .   ? 2.698   -7.827  -4.878  1.00 29.04 ? 921  HOH A O     1 
HETATM 8488 O O     . HOH G 4 .   ? 1.826   -15.967 -9.743  1.00 28.55 ? 922  HOH A O     1 
HETATM 8489 O O     . HOH G 4 .   ? -7.139  -11.671 0.523   1.00 23.82 ? 923  HOH A O     1 
HETATM 8490 O O     . HOH G 4 .   ? 6.106   -13.386 13.943  1.00 23.71 ? 924  HOH A O     1 
HETATM 8491 O O     . HOH G 4 .   ? 33.271  -14.119 9.167   1.00 36.26 ? 925  HOH A O     1 
HETATM 8492 O O     . HOH G 4 .   ? 45.272  -17.383 16.985  1.00 42.70 ? 926  HOH A O     1 
HETATM 8493 O O     . HOH G 4 .   ? -2.010  -4.532  -3.453  1.00 39.52 ? 927  HOH A O     1 
HETATM 8494 O O     . HOH G 4 .   ? 33.660  -12.129 24.708  1.00 39.16 ? 928  HOH A O     1 
HETATM 8495 O O     . HOH G 4 .   ? -5.057  -16.247 41.840  1.00 25.85 ? 929  HOH A O     1 
HETATM 8496 O O     . HOH G 4 .   ? 12.366  -44.170 35.917  1.00 46.76 ? 930  HOH A O     1 
HETATM 8497 O O     . HOH G 4 .   ? 9.798   -4.572  9.979   1.00 19.13 ? 931  HOH A O     1 
HETATM 8498 O O     . HOH G 4 .   ? 6.864   -21.819 36.061  1.00 30.09 ? 932  HOH A O     1 
HETATM 8499 O O     . HOH G 4 .   ? -5.776  -24.127 33.509  1.00 21.97 ? 933  HOH A O     1 
HETATM 8500 O O     . HOH G 4 .   ? -3.187  9.341   29.758  1.00 41.96 ? 934  HOH A O     1 
HETATM 8501 O O     . HOH G 4 .   ? -2.206  -17.827 18.942  1.00 30.33 ? 935  HOH A O     1 
HETATM 8502 O O     . HOH G 4 .   ? -5.555  -38.453 23.674  1.00 24.06 ? 936  HOH A O     1 
HETATM 8503 O O     . HOH G 4 .   ? 10.774  -2.012  13.582  1.00 43.07 ? 937  HOH A O     1 
HETATM 8504 O O     . HOH G 4 .   ? 12.503  -21.877 13.834  1.00 34.09 ? 938  HOH A O     1 
HETATM 8505 O O     . HOH G 4 .   ? -8.144  -37.307 24.909  1.00 28.89 ? 939  HOH A O     1 
HETATM 8506 O O     . HOH G 4 .   ? 33.231  -28.039 19.389  1.00 43.74 ? 940  HOH A O     1 
HETATM 8507 O O     . HOH G 4 .   ? 17.466  -15.089 28.421  1.00 41.70 ? 941  HOH A O     1 
HETATM 8508 O O     . HOH G 4 .   ? 37.008  -23.334 -1.142  1.00 30.73 ? 942  HOH A O     1 
HETATM 8509 O O     . HOH G 4 .   ? -3.915  -4.789  -3.766  1.00 41.41 ? 943  HOH A O     1 
HETATM 8510 O O     . HOH G 4 .   ? 5.971   -12.460 35.894  1.00 35.39 ? 944  HOH A O     1 
HETATM 8511 O O     . HOH G 4 .   ? 9.141   -12.753 19.992  1.00 25.93 ? 945  HOH A O     1 
HETATM 8512 O O     . HOH G 4 .   ? 17.033  -9.010  29.082  1.00 43.49 ? 946  HOH A O     1 
HETATM 8513 O O     . HOH G 4 .   ? -16.467 -9.080  15.350  1.00 37.31 ? 947  HOH A O     1 
HETATM 8514 O O     . HOH G 4 .   ? -9.030  -3.051  16.409  1.00 22.43 ? 948  HOH A O     1 
HETATM 8515 O O     . HOH G 4 .   ? 5.085   -44.935 22.634  1.00 27.04 ? 949  HOH A O     1 
HETATM 8516 O O     . HOH G 4 .   ? 3.859   -9.375  20.565  1.00 17.96 ? 950  HOH A O     1 
HETATM 8517 O O     . HOH G 4 .   ? 3.208   -11.762 22.079  1.00 21.74 ? 951  HOH A O     1 
HETATM 8518 O O     . HOH G 4 .   ? -1.185  -11.879 45.663  1.00 31.05 ? 952  HOH A O     1 
HETATM 8519 O O     . HOH G 4 .   ? 7.888   -35.682 39.151  1.00 41.01 ? 953  HOH A O     1 
HETATM 8520 O O     . HOH G 4 .   ? -16.093 -19.761 26.489  1.00 35.04 ? 954  HOH A O     1 
HETATM 8521 O O     . HOH G 4 .   ? -3.408  -4.496  45.455  1.00 38.67 ? 955  HOH A O     1 
HETATM 8522 O O     . HOH G 4 .   ? 19.677  -17.090 24.281  1.00 38.60 ? 956  HOH A O     1 
HETATM 8523 O O     . HOH G 4 .   ? -0.385  -13.105 13.851  1.00 24.33 ? 957  HOH A O     1 
HETATM 8524 O O     . HOH G 4 .   ? 3.904   -31.114 36.440  1.00 30.62 ? 958  HOH A O     1 
HETATM 8525 O O     . HOH G 4 .   ? 7.789   -32.379 2.467   1.00 23.71 ? 959  HOH A O     1 
HETATM 8526 O O     . HOH G 4 .   ? 12.828  -0.177  12.660  1.00 42.78 ? 960  HOH A O     1 
HETATM 8527 O O     . HOH G 4 .   ? -3.001  -14.903 44.032  1.00 24.48 ? 961  HOH A O     1 
HETATM 8528 O O     . HOH G 4 .   ? 1.896   1.453   37.697  1.00 37.95 ? 962  HOH A O     1 
HETATM 8529 O O     . HOH G 4 .   ? 14.983  -3.900  19.372  1.00 38.58 ? 963  HOH A O     1 
HETATM 8530 O O     . HOH G 4 .   ? 27.172  -46.471 19.639  1.00 50.43 ? 964  HOH A O     1 
HETATM 8531 O O     . HOH G 4 .   ? 6.409   -43.480 38.368  1.00 51.29 ? 965  HOH A O     1 
HETATM 8532 O O     . HOH G 4 .   ? -10.211 -34.729 25.421  1.00 31.03 ? 966  HOH A O     1 
HETATM 8533 O O     . HOH G 4 .   ? -6.694  9.402   32.234  1.00 38.56 ? 967  HOH A O     1 
HETATM 8534 O O     . HOH G 4 .   ? 31.070  -14.122 0.556   1.00 29.52 ? 968  HOH A O     1 
HETATM 8535 O O     . HOH G 4 .   ? 4.524   -4.874  40.930  1.00 32.52 ? 969  HOH A O     1 
HETATM 8536 O O     . HOH G 4 .   ? 5.650   -0.125  19.225  1.00 28.50 ? 970  HOH A O     1 
HETATM 8537 O O     . HOH G 4 .   ? 9.099   1.221   39.677  1.00 43.25 ? 971  HOH A O     1 
HETATM 8538 O O     . HOH G 4 .   ? 20.652  -49.881 6.241   1.00 47.20 ? 972  HOH A O     1 
HETATM 8539 O O     . HOH G 4 .   ? 11.866  -48.356 20.173  1.00 53.20 ? 973  HOH A O     1 
HETATM 8540 O O     . HOH G 4 .   ? 23.269  -45.847 22.520  1.00 38.24 ? 974  HOH A O     1 
HETATM 8541 O O     . HOH G 4 .   ? 6.454   -24.396 40.337  1.00 49.51 ? 975  HOH A O     1 
HETATM 8542 O O     . HOH G 4 .   ? -13.675 -33.427 27.542  1.00 30.89 ? 976  HOH A O     1 
HETATM 8543 O O     . HOH G 4 .   ? 7.750   -15.359 13.103  1.00 29.46 ? 977  HOH A O     1 
HETATM 8544 O O     . HOH G 4 .   ? 16.391  -25.822 13.378  1.00 50.29 ? 978  HOH A O     1 
HETATM 8545 O O     . HOH G 4 .   ? -8.824  -33.070 29.441  1.00 35.25 ? 979  HOH A O     1 
HETATM 8546 O O     . HOH G 4 .   ? 9.049   -2.424  12.225  1.00 39.71 ? 980  HOH A O     1 
HETATM 8547 O O     . HOH G 4 .   ? -12.299 -3.904  14.307  1.00 30.55 ? 981  HOH A O     1 
HETATM 8548 O O     . HOH G 4 .   ? 46.550  -21.969 10.276  1.00 40.91 ? 982  HOH A O     1 
HETATM 8549 O O     . HOH G 4 .   ? -10.316 -17.259 39.619  1.00 28.36 ? 983  HOH A O     1 
HETATM 8550 O O     . HOH G 4 .   ? 31.137  -8.332  15.501  1.00 49.71 ? 984  HOH A O     1 
HETATM 8551 O O     . HOH G 4 .   ? 39.791  -38.077 1.240   1.00 46.80 ? 985  HOH A O     1 
HETATM 8552 O O     . HOH G 4 .   ? -3.273  -41.155 21.343  1.00 33.55 ? 986  HOH A O     1 
HETATM 8553 O O     . HOH G 4 .   ? 45.918  -19.280 17.161  1.00 44.20 ? 987  HOH A O     1 
HETATM 8554 O O     . HOH G 4 .   ? -10.529 0.854   14.486  1.00 40.53 ? 988  HOH A O     1 
HETATM 8555 O O     . HOH G 4 .   ? 14.850  -39.961 36.969  1.00 44.10 ? 989  HOH A O     1 
HETATM 8556 O O     . HOH G 4 .   ? 15.674  -45.283 2.496   1.00 51.15 ? 990  HOH A O     1 
HETATM 8557 O O     . HOH G 4 .   ? -2.367  4.460   40.129  1.00 48.93 ? 991  HOH A O     1 
HETATM 8558 O O     . HOH G 4 .   ? 36.946  -17.514 5.744   1.00 36.81 ? 992  HOH A O     1 
HETATM 8559 O O     . HOH G 4 .   ? -12.649 -3.700  38.426  1.00 37.32 ? 993  HOH A O     1 
HETATM 8560 O O     . HOH G 4 .   ? 30.873  -3.780  17.326  1.00 39.18 ? 994  HOH A O     1 
HETATM 8561 O O     . HOH G 4 .   ? -6.904  6.872   38.004  1.00 45.41 ? 995  HOH A O     1 
HETATM 8562 O O     . HOH G 4 .   ? 21.678  -40.937 24.525  1.00 47.24 ? 996  HOH A O     1 
HETATM 8563 O O     . HOH G 4 .   ? 0.488   6.115   38.621  1.00 52.28 ? 997  HOH A O     1 
HETATM 8564 O O     . HOH G 4 .   ? 36.810  -9.595  20.127  1.00 40.56 ? 998  HOH A O     1 
HETATM 8565 O O     . HOH G 4 .   ? 9.056   -2.290  8.897   1.00 37.93 ? 999  HOH A O     1 
HETATM 8566 O O     . HOH G 4 .   ? 12.502  -46.964 18.019  1.00 51.84 ? 1000 HOH A O     1 
HETATM 8567 O O     . HOH G 4 .   ? -3.602  0.721   6.968   1.00 54.23 ? 1001 HOH A O     1 
HETATM 8568 O O     . HOH G 4 .   ? -15.944 -2.401  24.439  1.00 46.70 ? 1002 HOH A O     1 
HETATM 8569 O O     . HOH G 4 .   ? 16.427  -3.442  37.600  1.00 45.19 ? 1003 HOH A O     1 
HETATM 8570 O O     . HOH G 4 .   ? 2.689   -5.272  4.232   1.00 29.08 ? 1004 HOH A O     1 
HETATM 8571 O O     . HOH G 4 .   ? 8.310   0.294   19.020  1.00 38.70 ? 1005 HOH A O     1 
HETATM 8572 O O     . HOH G 4 .   ? 15.166  -23.026 -7.845  1.00 38.93 ? 1006 HOH A O     1 
HETATM 8573 O O     . HOH G 4 .   ? -8.340  -35.313 27.583  1.00 43.09 ? 1007 HOH A O     1 
HETATM 8574 O O     . HOH G 4 .   ? 20.213  -15.203 0.839   1.00 25.43 ? 1008 HOH A O     1 
HETATM 8575 O O     . HOH G 4 .   ? 12.452  -40.703 40.044  1.00 51.27 ? 1009 HOH A O     1 
HETATM 8576 O O     . HOH G 4 .   ? 32.961  -11.749 27.547  1.00 42.99 ? 1010 HOH A O     1 
HETATM 8577 O O     . HOH G 4 .   ? 3.949   3.995   21.223  1.00 44.94 ? 1011 HOH A O     1 
HETATM 8578 O O     . HOH G 4 .   ? 1.516   -19.559 43.531  1.00 48.84 ? 1012 HOH A O     1 
HETATM 8579 O O     . HOH G 4 .   ? 9.202   -44.649 4.580   1.00 49.81 ? 1013 HOH A O     1 
HETATM 8580 O O     . HOH G 4 .   ? 8.584   -18.089 36.187  1.00 42.68 ? 1014 HOH A O     1 
HETATM 8581 O O     . HOH G 4 .   ? 25.620  5.332   22.675  1.00 45.19 ? 1015 HOH A O     1 
HETATM 8582 O O     . HOH G 4 .   ? 33.030  -2.862  13.975  1.00 46.43 ? 1016 HOH A O     1 
HETATM 8583 O O     . HOH G 4 .   ? 18.240  -50.865 6.536   1.00 40.22 ? 1017 HOH A O     1 
HETATM 8584 O O     . HOH G 4 .   ? 16.066  -49.586 7.493   1.00 38.01 ? 1018 HOH A O     1 
HETATM 8585 O O     . HOH H 4 .   ? -21.795 -47.818 -7.368  1.00 48.34 ? 701  HOH B O     1 
HETATM 8586 O O     . HOH H 4 .   ? -26.971 -70.415 12.963  1.00 42.21 ? 702  HOH B O     1 
HETATM 8587 O O     . HOH H 4 .   ? -31.632 -43.355 14.651  1.00 38.04 ? 703  HOH B O     1 
HETATM 8588 O O     . HOH H 4 .   ? -3.908  -13.569 -14.286 1.00 32.44 ? 704  HOH B O     1 
HETATM 8589 O O     . HOH H 4 .   ? -4.734  -37.066 -2.256  1.00 24.23 ? 705  HOH B O     1 
HETATM 8590 O O     . HOH H 4 .   ? 0.231   -30.182 4.807   1.00 26.76 ? 706  HOH B O     1 
HETATM 8591 O O     . HOH H 4 .   ? -2.348  -45.736 -1.375  1.00 28.41 ? 707  HOH B O     1 
HETATM 8592 O O     . HOH H 4 .   ? -7.009  -55.186 -8.348  1.00 39.95 ? 708  HOH B O     1 
HETATM 8593 O O     . HOH H 4 .   ? 13.756  -41.528 -12.921 1.00 38.53 ? 709  HOH B O     1 
HETATM 8594 O O     . HOH H 4 .   ? -1.194  -57.136 -7.138  1.00 33.17 ? 710  HOH B O     1 
HETATM 8595 O O     . HOH H 4 .   ? 11.522  -19.588 0.087   1.00 31.94 ? 711  HOH B O     1 
HETATM 8596 O O     . HOH H 4 .   ? 11.775  -33.422 -12.537 1.00 34.07 ? 712  HOH B O     1 
HETATM 8597 O O     . HOH H 4 .   ? -8.551  -40.455 -14.742 1.00 41.23 ? 713  HOH B O     1 
HETATM 8598 O O     . HOH H 4 .   ? -23.545 -23.114 11.681  1.00 26.05 ? 714  HOH B O     1 
HETATM 8599 O O     . HOH H 4 .   ? -17.831 -33.626 -3.526  1.00 24.38 ? 715  HOH B O     1 
HETATM 8600 O O     . HOH H 4 .   ? 13.227  -60.830 11.604  1.00 41.10 ? 716  HOH B O     1 
HETATM 8601 O O     . HOH H 4 .   ? 1.616   -51.825 7.721   1.00 25.38 ? 717  HOH B O     1 
HETATM 8602 O O     . HOH H 4 .   ? -14.338 -45.175 25.505  1.00 37.31 ? 718  HOH B O     1 
HETATM 8603 O O     . HOH H 4 .   ? 4.610   -23.625 1.117   1.00 21.78 ? 719  HOH B O     1 
HETATM 8604 O O     . HOH H 4 .   ? 7.553   -43.525 18.703  1.00 25.11 ? 720  HOH B O     1 
HETATM 8605 O O     . HOH H 4 .   ? -15.145 -32.706 -12.273 1.00 37.99 ? 721  HOH B O     1 
HETATM 8606 O O     . HOH H 4 .   ? -27.942 -16.463 -20.783 1.00 43.86 ? 722  HOH B O     1 
HETATM 8607 O O     . HOH H 4 .   ? -22.129 -14.700 6.419   1.00 32.33 ? 723  HOH B O     1 
HETATM 8608 O O     . HOH H 4 .   ? -7.144  -61.272 -0.205  1.00 31.13 ? 724  HOH B O     1 
HETATM 8609 O O     . HOH H 4 .   ? -19.780 -10.747 8.246   1.00 43.17 ? 725  HOH B O     1 
HETATM 8610 O O     . HOH H 4 .   ? -17.691 -10.800 -4.203  1.00 38.93 ? 726  HOH B O     1 
HETATM 8611 O O     . HOH H 4 .   ? 1.050   -22.441 4.529   1.00 28.32 ? 727  HOH B O     1 
HETATM 8612 O O     . HOH H 4 .   ? -20.620 -40.742 9.318   1.00 34.24 ? 728  HOH B O     1 
HETATM 8613 O O     . HOH H 4 .   ? -10.734 -34.820 -14.223 1.00 30.97 ? 729  HOH B O     1 
HETATM 8614 O O     . HOH H 4 .   ? -20.068 -60.835 11.765  1.00 35.15 ? 730  HOH B O     1 
HETATM 8615 O O     . HOH H 4 .   ? -5.990  -11.299 -4.167  1.00 30.41 ? 731  HOH B O     1 
HETATM 8616 O O     . HOH H 4 .   ? -29.836 -30.631 10.115  1.00 35.65 ? 732  HOH B O     1 
HETATM 8617 O O     . HOH H 4 .   ? 2.112   -43.901 -8.524  1.00 30.41 ? 733  HOH B O     1 
HETATM 8618 O O     . HOH H 4 .   ? -19.705 -52.563 -8.879  1.00 44.79 ? 734  HOH B O     1 
HETATM 8619 O O     . HOH H 4 .   ? 6.141   -24.575 -7.326  1.00 40.19 ? 735  HOH B O     1 
HETATM 8620 O O     . HOH H 4 .   ? -16.582 -27.222 20.976  1.00 24.59 ? 736  HOH B O     1 
HETATM 8621 O O     . HOH H 4 .   ? 6.932   -42.536 15.944  1.00 28.25 ? 737  HOH B O     1 
HETATM 8622 O O     . HOH H 4 .   ? -6.434  -67.935 9.729   1.00 34.14 ? 738  HOH B O     1 
HETATM 8623 O O     . HOH H 4 .   ? -17.786 -28.198 0.384   1.00 29.87 ? 739  HOH B O     1 
HETATM 8624 O O     . HOH H 4 .   ? -19.718 -17.167 16.572  1.00 35.31 ? 740  HOH B O     1 
HETATM 8625 O O     . HOH H 4 .   ? 3.494   -40.287 -2.680  1.00 24.82 ? 741  HOH B O     1 
HETATM 8626 O O     . HOH H 4 .   ? -22.968 -53.219 5.173   1.00 43.89 ? 742  HOH B O     1 
HETATM 8627 O O     . HOH H 4 .   ? -6.773  -54.063 24.921  1.00 35.28 ? 743  HOH B O     1 
HETATM 8628 O O     . HOH H 4 .   ? -28.594 -35.813 -4.784  1.00 36.23 ? 744  HOH B O     1 
HETATM 8629 O O     . HOH H 4 .   ? 3.161   -42.810 -1.704  1.00 27.40 ? 745  HOH B O     1 
HETATM 8630 O O     . HOH H 4 .   ? -19.798 -58.190 -5.029  1.00 35.32 ? 746  HOH B O     1 
HETATM 8631 O O     . HOH H 4 .   ? 3.696   -53.733 6.981   1.00 26.78 ? 747  HOH B O     1 
HETATM 8632 O O     . HOH H 4 .   ? -7.977  -61.269 21.057  1.00 33.98 ? 748  HOH B O     1 
HETATM 8633 O O     . HOH H 4 .   ? -15.509 -26.298 -0.130  1.00 32.70 ? 749  HOH B O     1 
HETATM 8634 O O     . HOH H 4 .   ? -17.508 -12.849 12.193  1.00 28.74 ? 750  HOH B O     1 
HETATM 8635 O O     . HOH H 4 .   ? -28.230 -24.157 11.261  1.00 41.45 ? 751  HOH B O     1 
HETATM 8636 O O     . HOH H 4 .   ? -2.975  -19.598 -12.873 1.00 39.11 ? 752  HOH B O     1 
HETATM 8637 O O     . HOH H 4 .   ? -19.831 -39.624 -7.637  1.00 35.38 ? 753  HOH B O     1 
HETATM 8638 O O     . HOH H 4 .   ? 6.663   -49.476 15.685  1.00 24.81 ? 754  HOH B O     1 
HETATM 8639 O O     . HOH H 4 .   ? 0.574   -17.033 6.912   1.00 22.82 ? 755  HOH B O     1 
HETATM 8640 O O     . HOH H 4 .   ? 3.776   -18.018 -5.824  1.00 25.80 ? 756  HOH B O     1 
HETATM 8641 O O     . HOH H 4 .   ? 9.642   -19.522 -8.640  1.00 34.13 ? 757  HOH B O     1 
HETATM 8642 O O     . HOH H 4 .   ? -20.731 -15.590 13.303  1.00 47.58 ? 758  HOH B O     1 
HETATM 8643 O O     . HOH H 4 .   ? 4.282   -65.988 4.064   1.00 36.59 ? 759  HOH B O     1 
HETATM 8644 O O     . HOH H 4 .   ? 10.920  -43.731 -0.359  1.00 33.20 ? 760  HOH B O     1 
HETATM 8645 O O     . HOH H 4 .   ? -11.816 -42.356 10.097  1.00 36.98 ? 761  HOH B O     1 
HETATM 8646 O O     . HOH H 4 .   ? -1.590  -38.784 -1.799  1.00 46.04 ? 762  HOH B O     1 
HETATM 8647 O O     . HOH H 4 .   ? -4.890  -19.235 -14.551 1.00 39.77 ? 763  HOH B O     1 
HETATM 8648 O O     . HOH H 4 .   ? -32.296 -24.869 -12.232 1.00 41.20 ? 764  HOH B O     1 
HETATM 8649 O O     . HOH H 4 .   ? -12.675 -12.794 -0.656  1.00 26.99 ? 765  HOH B O     1 
HETATM 8650 O O     . HOH H 4 .   ? 9.772   -30.715 3.580   1.00 25.91 ? 766  HOH B O     1 
HETATM 8651 O O     . HOH H 4 .   ? -20.731 -33.259 -2.209  1.00 28.40 ? 767  HOH B O     1 
HETATM 8652 O O     . HOH H 4 .   ? 8.302   -60.042 16.701  1.00 34.55 ? 768  HOH B O     1 
HETATM 8653 O O     . HOH H 4 .   ? -21.074 -30.751 1.294   1.00 29.62 ? 769  HOH B O     1 
HETATM 8654 O O     . HOH H 4 .   ? -24.373 -50.332 -6.851  1.00 43.77 ? 770  HOH B O     1 
HETATM 8655 O O     . HOH H 4 .   ? -26.500 -10.939 -16.071 1.00 39.36 ? 771  HOH B O     1 
HETATM 8656 O O     . HOH H 4 .   ? 4.429   -44.153 -9.998  1.00 33.48 ? 772  HOH B O     1 
HETATM 8657 O O     . HOH H 4 .   ? -22.808 -45.344 23.683  1.00 37.21 ? 773  HOH B O     1 
HETATM 8658 O O     . HOH H 4 .   ? -6.771  -67.118 18.372  1.00 30.64 ? 774  HOH B O     1 
HETATM 8659 O O     . HOH H 4 .   ? -19.350 -13.306 0.750   1.00 27.15 ? 775  HOH B O     1 
HETATM 8660 O O     . HOH H 4 .   ? -24.724 -29.517 7.631   1.00 25.86 ? 776  HOH B O     1 
HETATM 8661 O O     . HOH H 4 .   ? 2.226   -43.776 -18.237 1.00 31.10 ? 777  HOH B O     1 
HETATM 8662 O O     . HOH H 4 .   ? 0.959   -26.053 2.835   1.00 25.17 ? 778  HOH B O     1 
HETATM 8663 O O     . HOH H 4 .   ? -0.308  -52.379 22.560  1.00 33.61 ? 779  HOH B O     1 
HETATM 8664 O O     . HOH H 4 .   ? -2.922  -51.160 22.059  1.00 30.44 ? 780  HOH B O     1 
HETATM 8665 O O     . HOH H 4 .   ? -13.288 -9.874  -4.919  1.00 42.19 ? 781  HOH B O     1 
HETATM 8666 O O     . HOH H 4 .   ? -18.308 -8.893  -1.854  1.00 40.02 ? 782  HOH B O     1 
HETATM 8667 O O     . HOH H 4 .   ? -5.720  -36.293 4.894   1.00 28.92 ? 783  HOH B O     1 
HETATM 8668 O O     . HOH H 4 .   ? -6.398  -66.444 14.429  1.00 32.36 ? 784  HOH B O     1 
HETATM 8669 O O     . HOH H 4 .   ? 1.780   -38.252 -2.008  1.00 23.65 ? 785  HOH B O     1 
HETATM 8670 O O     . HOH H 4 .   ? 12.061  -49.341 -7.460  1.00 46.08 ? 786  HOH B O     1 
HETATM 8671 O O     . HOH H 4 .   ? -1.678  -37.924 -16.966 1.00 32.65 ? 787  HOH B O     1 
HETATM 8672 O O     . HOH H 4 .   ? -23.994 -39.079 22.339  1.00 32.94 ? 788  HOH B O     1 
HETATM 8673 O O     . HOH H 4 .   ? -21.317 -28.484 25.847  1.00 43.28 ? 789  HOH B O     1 
HETATM 8674 O O     . HOH H 4 .   ? -19.566 -21.479 23.816  1.00 36.85 ? 790  HOH B O     1 
HETATM 8675 O O     . HOH H 4 .   ? 13.249  -39.092 -7.174  1.00 33.18 ? 791  HOH B O     1 
HETATM 8676 O O     . HOH H 4 .   ? -25.385 -54.226 -6.873  1.00 46.75 ? 792  HOH B O     1 
HETATM 8677 O O     . HOH H 4 .   ? -27.746 -23.811 -19.111 1.00 44.61 ? 793  HOH B O     1 
HETATM 8678 O O     . HOH H 4 .   ? -8.267  -47.041 25.782  1.00 33.06 ? 794  HOH B O     1 
HETATM 8679 O O     . HOH H 4 .   ? -17.301 -34.884 4.042   1.00 28.48 ? 795  HOH B O     1 
HETATM 8680 O O     . HOH H 4 .   ? -30.729 -52.621 1.813   1.00 40.56 ? 796  HOH B O     1 
HETATM 8681 O O     . HOH H 4 .   ? -20.629 -35.497 21.955  1.00 26.05 ? 797  HOH B O     1 
HETATM 8682 O O     . HOH H 4 .   ? -25.890 -22.564 -21.161 1.00 36.21 ? 798  HOH B O     1 
HETATM 8683 O O     . HOH H 4 .   ? -5.368  -44.503 5.736   1.00 35.44 ? 799  HOH B O     1 
HETATM 8684 O O     . HOH H 4 .   ? -26.442 -54.470 4.484   1.00 36.38 ? 800  HOH B O     1 
HETATM 8685 O O     . HOH H 4 .   ? -8.729  -51.814 3.347   1.00 32.14 ? 801  HOH B O     1 
HETATM 8686 O O     . HOH H 4 .   ? -22.682 -37.296 -7.355  1.00 33.39 ? 802  HOH B O     1 
HETATM 8687 O O     . HOH H 4 .   ? -26.485 -32.411 7.968   1.00 25.62 ? 803  HOH B O     1 
HETATM 8688 O O     . HOH H 4 .   ? -4.668  -34.680 -15.609 1.00 47.09 ? 804  HOH B O     1 
HETATM 8689 O O     . HOH H 4 .   ? -18.579 -32.163 1.038   1.00 26.63 ? 805  HOH B O     1 
HETATM 8690 O O     . HOH H 4 .   ? -9.782  -50.754 -5.775  1.00 32.10 ? 806  HOH B O     1 
HETATM 8691 O O     . HOH H 4 .   ? -9.839  -49.347 2.562   1.00 37.59 ? 807  HOH B O     1 
HETATM 8692 O O     . HOH H 4 .   ? -13.967 -26.760 -14.893 1.00 33.30 ? 808  HOH B O     1 
HETATM 8693 O O     . HOH H 4 .   ? -24.152 -28.659 14.321  1.00 33.66 ? 809  HOH B O     1 
HETATM 8694 O O     . HOH H 4 .   ? -21.454 -29.946 -4.678  1.00 27.17 ? 810  HOH B O     1 
HETATM 8695 O O     . HOH H 4 .   ? -3.387  -48.377 -12.452 1.00 35.79 ? 811  HOH B O     1 
HETATM 8696 O O     . HOH H 4 .   ? -23.758 -26.422 0.394   1.00 25.77 ? 812  HOH B O     1 
HETATM 8697 O O     . HOH H 4 .   ? -6.281  -68.298 5.592   1.00 36.87 ? 813  HOH B O     1 
HETATM 8698 O O     . HOH H 4 .   ? -2.366  -70.310 4.883   1.00 41.19 ? 814  HOH B O     1 
HETATM 8699 O O     . HOH H 4 .   ? -27.166 -57.633 9.927   1.00 36.18 ? 815  HOH B O     1 
HETATM 8700 O O     . HOH H 4 .   ? -26.860 -60.516 -3.109  1.00 30.57 ? 816  HOH B O     1 
HETATM 8701 O O     . HOH H 4 .   ? -18.850 -37.508 15.992  1.00 26.04 ? 817  HOH B O     1 
HETATM 8702 O O     . HOH H 4 .   ? -6.806  -58.073 -7.355  1.00 39.70 ? 818  HOH B O     1 
HETATM 8703 O O     . HOH H 4 .   ? -18.951 -26.758 18.584  1.00 26.35 ? 819  HOH B O     1 
HETATM 8704 O O     . HOH H 4 .   ? 5.819   -19.702 -5.704  1.00 34.42 ? 820  HOH B O     1 
HETATM 8705 O O     . HOH H 4 .   ? -24.714 -27.247 12.277  1.00 27.24 ? 821  HOH B O     1 
HETATM 8706 O O     . HOH H 4 .   ? -6.178  -33.139 -8.306  1.00 25.61 ? 822  HOH B O     1 
HETATM 8707 O O     . HOH H 4 .   ? 9.309   -11.124 -4.348  1.00 23.71 ? 823  HOH B O     1 
HETATM 8708 O O     . HOH H 4 .   ? -9.195  -51.551 -11.585 1.00 42.86 ? 824  HOH B O     1 
HETATM 8709 O O     . HOH H 4 .   ? 1.717   -56.007 22.011  1.00 41.05 ? 825  HOH B O     1 
HETATM 8710 O O     . HOH H 4 .   ? 3.724   -31.217 3.622   1.00 31.80 ? 826  HOH B O     1 
HETATM 8711 O O     . HOH H 4 .   ? -2.806  -69.215 -5.637  1.00 38.01 ? 827  HOH B O     1 
HETATM 8712 O O     . HOH H 4 .   ? 3.490   -56.100 19.208  1.00 43.72 ? 828  HOH B O     1 
HETATM 8713 O O     . HOH H 4 .   ? -15.911 -20.094 20.557  1.00 26.37 ? 829  HOH B O     1 
HETATM 8714 O O     . HOH H 4 .   ? 6.340   -31.073 0.483   1.00 27.26 ? 830  HOH B O     1 
HETATM 8715 O O     . HOH H 4 .   ? -21.123 -28.208 18.127  1.00 35.30 ? 831  HOH B O     1 
HETATM 8716 O O     . HOH H 4 .   ? -19.409 -40.184 16.903  1.00 24.89 ? 832  HOH B O     1 
HETATM 8717 O O     . HOH H 4 .   ? 10.574  -37.866 -2.875  1.00 26.21 ? 833  HOH B O     1 
HETATM 8718 O O     . HOH H 4 .   ? -11.077 -12.618 -12.679 1.00 38.57 ? 834  HOH B O     1 
HETATM 8719 O O     . HOH H 4 .   ? -23.356 -48.341 18.344  1.00 35.24 ? 835  HOH B O     1 
HETATM 8720 O O     . HOH H 4 .   ? -22.187 -23.970 18.861  1.00 35.81 ? 836  HOH B O     1 
HETATM 8721 O O     . HOH H 4 .   ? -13.190 -12.907 1.694   1.00 41.43 ? 837  HOH B O     1 
HETATM 8722 O O     . HOH H 4 .   ? -6.693  -20.738 -19.127 1.00 34.71 ? 838  HOH B O     1 
HETATM 8723 O O     . HOH H 4 .   ? -30.134 -24.338 8.253   1.00 41.70 ? 839  HOH B O     1 
HETATM 8724 O O     . HOH H 4 .   ? -19.858 -34.499 0.254   1.00 31.91 ? 840  HOH B O     1 
HETATM 8725 O O     . HOH H 4 .   ? 6.897   -50.139 20.108  1.00 31.53 ? 841  HOH B O     1 
HETATM 8726 O O     . HOH H 4 .   ? 1.318   -40.074 5.848   1.00 25.21 ? 842  HOH B O     1 
HETATM 8727 O O     . HOH H 4 .   ? -20.853 -27.488 -15.920 1.00 41.71 ? 843  HOH B O     1 
HETATM 8728 O O     . HOH H 4 .   ? -16.066 -23.362 7.595   1.00 24.59 ? 844  HOH B O     1 
HETATM 8729 O O     . HOH H 4 .   ? -25.338 -23.415 14.856  1.00 39.89 ? 845  HOH B O     1 
HETATM 8730 O O     . HOH H 4 .   ? -10.077 -9.997  -6.415  1.00 49.59 ? 846  HOH B O     1 
HETATM 8731 O O     . HOH H 4 .   ? -25.840 -35.631 -0.759  1.00 40.92 ? 847  HOH B O     1 
HETATM 8732 O O     . HOH H 4 .   ? -24.059 -18.911 -23.373 1.00 44.99 ? 848  HOH B O     1 
HETATM 8733 O O     . HOH H 4 .   ? -9.949  -16.406 -17.549 1.00 31.47 ? 849  HOH B O     1 
HETATM 8734 O O     . HOH H 4 .   ? -7.571  -10.904 -8.568  1.00 36.58 ? 850  HOH B O     1 
HETATM 8735 O O     . HOH H 4 .   ? -1.550  -32.530 -17.075 1.00 38.79 ? 851  HOH B O     1 
HETATM 8736 O O     . HOH H 4 .   ? -0.117  -38.187 -0.195  1.00 22.41 ? 852  HOH B O     1 
HETATM 8737 O O     . HOH H 4 .   ? -3.276  -17.517 -10.435 1.00 42.18 ? 853  HOH B O     1 
HETATM 8738 O O     . HOH H 4 .   ? -7.019  -46.791 -6.225  1.00 29.46 ? 854  HOH B O     1 
HETATM 8739 O O     . HOH H 4 .   ? -29.358 -27.175 8.953   1.00 39.29 ? 855  HOH B O     1 
HETATM 8740 O O     . HOH H 4 .   ? -30.482 -17.266 -17.520 1.00 41.40 ? 856  HOH B O     1 
HETATM 8741 O O     . HOH H 4 .   ? -11.827 -26.069 -21.337 1.00 46.21 ? 857  HOH B O     1 
HETATM 8742 O O     . HOH H 4 .   ? -25.570 -12.609 4.362   1.00 36.52 ? 858  HOH B O     1 
HETATM 8743 O O     . HOH H 4 .   ? -19.699 -30.804 -2.907  1.00 28.24 ? 859  HOH B O     1 
HETATM 8744 O O     . HOH H 4 .   ? -14.418 -19.976 -21.185 1.00 39.72 ? 860  HOH B O     1 
HETATM 8745 O O     . HOH H 4 .   ? -6.071  -21.570 -13.468 1.00 27.94 ? 861  HOH B O     1 
HETATM 8746 O O     . HOH H 4 .   ? -24.933 -30.020 20.225  1.00 41.46 ? 862  HOH B O     1 
HETATM 8747 O O     . HOH H 4 .   ? -13.184 -30.211 30.170  1.00 35.89 ? 863  HOH B O     1 
HETATM 8748 O O     . HOH H 4 .   ? -19.569 -52.948 23.104  1.00 43.01 ? 864  HOH B O     1 
HETATM 8749 O O     . HOH H 4 .   ? -28.563 -32.531 -9.093  1.00 51.22 ? 865  HOH B O     1 
HETATM 8750 O O     . HOH H 4 .   ? 1.122   -69.161 8.065   1.00 38.95 ? 866  HOH B O     1 
HETATM 8751 O O     . HOH H 4 .   ? -29.410 -38.186 0.772   1.00 50.43 ? 867  HOH B O     1 
HETATM 8752 O O     . HOH H 4 .   ? -27.159 -34.192 10.601  1.00 30.36 ? 868  HOH B O     1 
HETATM 8753 O O     . HOH H 4 .   ? -39.583 -50.185 0.581   1.00 49.87 ? 869  HOH B O     1 
HETATM 8754 O O     . HOH H 4 .   ? 3.468   -17.166 4.146   1.00 26.98 ? 870  HOH B O     1 
HETATM 8755 O O     . HOH H 4 .   ? -17.120 -47.524 16.180  1.00 28.42 ? 871  HOH B O     1 
HETATM 8756 O O     . HOH H 4 .   ? -0.204  -38.719 -4.096  1.00 23.66 ? 872  HOH B O     1 
HETATM 8757 O O     . HOH H 4 .   ? -2.347  -38.109 -2.435  1.00 30.59 ? 873  HOH B O     1 
HETATM 8758 O O     . HOH H 4 .   ? -23.192 -64.013 12.315  1.00 42.31 ? 874  HOH B O     1 
HETATM 8759 O O     . HOH H 4 .   ? 14.461  -54.820 10.566  1.00 36.16 ? 875  HOH B O     1 
HETATM 8760 O O     . HOH H 4 .   ? -23.449 -21.844 17.301  1.00 42.76 ? 876  HOH B O     1 
HETATM 8761 O O     . HOH H 4 .   ? -27.963 -36.894 -0.781  1.00 43.63 ? 877  HOH B O     1 
HETATM 8762 O O     . HOH H 4 .   ? -17.413 -28.613 28.177  1.00 34.07 ? 878  HOH B O     1 
HETATM 8763 O O     . HOH H 4 .   ? -14.880 -21.780 9.434   1.00 28.04 ? 879  HOH B O     1 
HETATM 8764 O O     . HOH H 4 .   ? -21.386 -46.839 17.483  1.00 25.96 ? 880  HOH B O     1 
HETATM 8765 O O     . HOH H 4 .   ? -35.919 -52.613 -4.359  1.00 55.17 ? 881  HOH B O     1 
HETATM 8766 O O     . HOH H 4 .   ? 12.455  -37.460 -4.703  1.00 26.38 ? 882  HOH B O     1 
HETATM 8767 O O     . HOH H 4 .   ? -12.179 -24.568 1.584   1.00 37.57 ? 883  HOH B O     1 
HETATM 8768 O O     . HOH H 4 .   ? -16.908 -25.812 6.849   1.00 26.35 ? 884  HOH B O     1 
HETATM 8769 O O     . HOH H 4 .   ? -19.500 -28.390 -1.586  1.00 26.23 ? 885  HOH B O     1 
HETATM 8770 O O     . HOH H 4 .   ? -33.199 -38.475 10.504  1.00 38.00 ? 886  HOH B O     1 
HETATM 8771 O O     . HOH H 4 .   ? -27.621 -26.743 -19.889 1.00 42.44 ? 887  HOH B O     1 
HETATM 8772 O O     . HOH H 4 .   ? 7.108   -30.364 -14.506 1.00 36.93 ? 888  HOH B O     1 
HETATM 8773 O O     . HOH H 4 .   ? -5.798  -14.555 -10.835 1.00 40.82 ? 889  HOH B O     1 
HETATM 8774 O O     . HOH H 4 .   ? -32.651 -36.014 8.413   1.00 47.72 ? 890  HOH B O     1 
HETATM 8775 O O     . HOH H 4 .   ? -20.563 -18.758 -24.833 1.00 50.99 ? 891  HOH B O     1 
HETATM 8776 O O     . HOH H 4 .   ? 7.740   -22.324 -5.679  1.00 27.13 ? 892  HOH B O     1 
HETATM 8777 O O     . HOH H 4 .   ? -11.554 -44.298 -2.797  1.00 32.82 ? 893  HOH B O     1 
HETATM 8778 O O     . HOH H 4 .   ? 8.516   -25.464 -4.788  1.00 25.01 ? 894  HOH B O     1 
HETATM 8779 O O     . HOH H 4 .   ? 12.305  -50.783 8.764   1.00 30.78 ? 895  HOH B O     1 
HETATM 8780 O O     . HOH H 4 .   ? -26.084 -58.333 -6.504  1.00 51.92 ? 896  HOH B O     1 
HETATM 8781 O O     . HOH H 4 .   ? -9.468  -10.879 -11.095 1.00 39.89 ? 897  HOH B O     1 
HETATM 8782 O O     . HOH H 4 .   ? 1.172   -18.757 4.839   1.00 26.75 ? 898  HOH B O     1 
HETATM 8783 O O     . HOH H 4 .   ? -11.374 -40.399 5.450   1.00 38.58 ? 899  HOH B O     1 
HETATM 8784 O O     . HOH H 4 .   ? -14.654 -65.325 18.684  1.00 33.15 ? 900  HOH B O     1 
HETATM 8785 O O     . HOH H 4 .   ? -23.445 -58.953 9.443   1.00 35.87 ? 901  HOH B O     1 
HETATM 8786 O O     . HOH H 4 .   ? -21.757 -28.456 -0.075  1.00 27.19 ? 902  HOH B O     1 
HETATM 8787 O O     . HOH H 4 .   ? -8.431  -44.765 4.973   1.00 37.84 ? 903  HOH B O     1 
HETATM 8788 O O     . HOH H 4 .   ? -19.251 -23.047 -24.879 1.00 52.25 ? 904  HOH B O     1 
HETATM 8789 O O     . HOH H 4 .   ? -30.978 -28.356 2.016   1.00 32.46 ? 905  HOH B O     1 
HETATM 8790 O O     . HOH H 4 .   ? -24.629 -15.023 5.363   1.00 28.97 ? 906  HOH B O     1 
HETATM 8791 O O     . HOH H 4 .   ? -10.992 -33.450 -16.372 1.00 34.98 ? 907  HOH B O     1 
HETATM 8792 O O     . HOH H 4 .   ? 11.694  -35.533 -14.538 1.00 42.45 ? 908  HOH B O     1 
HETATM 8793 O O     . HOH H 4 .   ? -29.223 -32.768 8.401   1.00 40.28 ? 909  HOH B O     1 
HETATM 8794 O O     . HOH H 4 .   ? -34.223 -25.709 -3.500  1.00 48.40 ? 910  HOH B O     1 
HETATM 8795 O O     . HOH H 4 .   ? -20.209 -28.129 27.211  1.00 44.17 ? 911  HOH B O     1 
HETATM 8796 O O     . HOH H 4 .   ? -20.872 -59.571 9.565   1.00 33.48 ? 912  HOH B O     1 
HETATM 8797 O O     . HOH H 4 .   ? -22.181 -57.645 18.016  1.00 33.61 ? 913  HOH B O     1 
HETATM 8798 O O     . HOH H 4 .   ? -12.978 -56.682 25.494  1.00 49.92 ? 914  HOH B O     1 
HETATM 8799 O O     . HOH H 4 .   ? 9.091   -65.257 14.006  1.00 50.76 ? 915  HOH B O     1 
HETATM 8800 O O     . HOH H 4 .   ? -30.476 -34.591 3.989   1.00 41.08 ? 916  HOH B O     1 
HETATM 8801 O O     . HOH H 4 .   ? 0.720   -38.716 16.083  1.00 26.05 ? 917  HOH B O     1 
HETATM 8802 O O     . HOH H 4 .   ? -7.124  -60.899 22.844  1.00 51.88 ? 918  HOH B O     1 
HETATM 8803 O O     . HOH H 4 .   ? -16.648 -41.241 27.031  1.00 48.57 ? 919  HOH B O     1 
HETATM 8804 O O     . HOH H 4 .   ? -32.879 -41.029 10.517  1.00 35.92 ? 920  HOH B O     1 
HETATM 8805 O O     . HOH H 4 .   ? -17.272 -9.072  6.719   1.00 43.32 ? 921  HOH B O     1 
HETATM 8806 O O     . HOH H 4 .   ? -20.305 -63.411 12.248  1.00 36.71 ? 922  HOH B O     1 
HETATM 8807 O O     . HOH H 4 .   ? 7.694   -65.898 2.719   1.00 54.55 ? 923  HOH B O     1 
HETATM 8808 O O     . HOH H 4 .   ? -1.906  -14.323 -15.308 1.00 37.34 ? 924  HOH B O     1 
HETATM 8809 O O     . HOH H 4 .   ? -18.622 -21.306 -25.433 1.00 54.71 ? 925  HOH B O     1 
HETATM 8810 O O     . HOH H 4 .   ? -15.789 -32.411 28.749  1.00 42.94 ? 926  HOH B O     1 
HETATM 8811 O O     . HOH H 4 .   ? 4.904   -53.002 -7.164  1.00 38.17 ? 927  HOH B O     1 
HETATM 8812 O O     . HOH H 4 .   ? -9.837  -10.905 1.996   1.00 46.31 ? 928  HOH B O     1 
HETATM 8813 O O     . HOH H 4 .   ? -18.976 -61.536 -8.230  1.00 51.80 ? 929  HOH B O     1 
HETATM 8814 O O     . HOH H 4 .   ? -26.026 -24.961 12.811  1.00 40.82 ? 930  HOH B O     1 
HETATM 8815 O O     . HOH H 4 .   ? -32.184 -30.941 1.825   1.00 41.17 ? 931  HOH B O     1 
HETATM 8816 O O     . HOH H 4 .   ? -24.516 -27.831 16.778  1.00 33.80 ? 932  HOH B O     1 
HETATM 8817 O O     . HOH H 4 .   ? -22.840 -49.223 24.221  1.00 55.74 ? 933  HOH B O     1 
HETATM 8818 O O     . HOH H 4 .   ? -18.921 -47.106 18.028  1.00 32.94 ? 934  HOH B O     1 
HETATM 8819 O O     . HOH H 4 .   ? 5.888   -31.940 4.514   1.00 35.76 ? 935  HOH B O     1 
HETATM 8820 O O     . HOH H 4 .   ? 0.811   -55.761 -8.721  1.00 46.80 ? 936  HOH B O     1 
HETATM 8821 O O     . HOH H 4 .   ? -25.066 -44.434 24.439  1.00 48.60 ? 937  HOH B O     1 
HETATM 8822 O O     . HOH H 4 .   ? -16.509 -23.347 28.599  1.00 39.49 ? 938  HOH B O     1 
HETATM 8823 O O     . HOH H 4 .   ? 1.891   -50.871 23.359  1.00 40.51 ? 939  HOH B O     1 
HETATM 8824 O O     . HOH H 4 .   ? -8.611  -45.181 -16.097 1.00 52.73 ? 940  HOH B O     1 
# 
