data_4PZF
# 
_entry.id   4PZF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4PZF         
RCSB  RCSB085411   
WWPDB D_1000085411 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4PVE 'Wild-type Phl p 4.0202, a glucose dehydrogenase'                    unspecified 
PDB 4PVH 'Phl p 4 N158H variant, a glucose dehydrogenase'                     unspecified 
PDB 4PVJ 'Phl p 4 I153V variant, a glucose oxidase'                           unspecified 
PDB 4PVK 'hl p 4 I153V N158H variant, a glucose oxidase'                      unspecified 
PDB 4PWB 'Phl p 4 I153V variant, a glucose oxidase, pressurized with Xenon'   unspecified 
PDB 4PWC 'Phl p 4 I153V N158H variant, a glucose oxidase, 3.5 M NaBr soak'    unspecified 
PDB 3D2H 'Structure of berberine bridge enzyme from Eschscholzia californica' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4PZF 
_pdbx_database_status.recvd_initial_deposition_date   2014-03-30 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Zafred, D.'    1 
'Wallner, S.'   2 
'Steiner, B.'   3 
'Macheroux, P.' 4 
# 
_citation.id                        primary 
_citation.title                     'Rationally engineered flavin-dependent oxidase reveals steric control of dioxygen reduction.' 
_citation.journal_abbrev            'Febs J.' 
_citation.journal_volume            282 
_citation.page_first                3060 
_citation.page_last                 3074 
_citation.year                      2015 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25619330 
_citation.pdbx_database_id_DOI      10.1111/febs.13212 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Zafred, D.'         1 
primary 'Steiner, B.'        2 
primary 'Teufelberger, A.R.' 3 
primary 'Hromic, A.'         4 
primary 'Karplus, P.A.'      5 
primary 'Schofield, C.J.'    6 
primary 'Wallner, S.'        7 
primary 'Macheroux, P.'      8 
# 
_cell.entry_id           4PZF 
_cell.length_a           80.820 
_cell.length_b           175.440 
_cell.length_c           195.810 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4PZF 
_symmetry.space_group_name_H-M             'P 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                17 
_symmetry.space_group_name_Hall            ? 
# 
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 'Reticuline oxidase'          60061.008 4   1.21.3.3 G164A ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   4   ?        ?     ? ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE        221.208   12  ?        ?     ? ? 
4 non-polymer syn 'SULFATE ION'                 96.063    5   ?        ?     ? ? 
5 non-polymer syn 'DODECAETHYLENE GLYCOL'       546.646   2   ?        ?     ? ? 
6 water       nat water                         18.015    308 ?        ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Berberine bridge-forming enzyme, BBE, Tetrahydroprotoberberine synthase' 
# 
_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       
;MENKTPIFFSLSIFLSLLNCAEAGNDLLSCLTFNGVRNHTVFSADSDSDFNRFLHLSIQNPLFQNSLISKPSAIILPGSK
EELSNTIRCIRKGSWTIRLRSGGHSYEGLSYTSDTPFILIDLMNLNRVSIDLESETAWVESGSTLGELYYAITESSSKLG
FTAAWCPTVGTGGHISGGGFGMMSRKYGLAADNVVDAILIDANGAILDRQAMGEDVFWAIRGGGGGVWGAIYAWKIKLLP
VPEKVTVFRVTKNVAIDEATSLLHKWQFVAEELEEDFTLSVLGGADEKQVWLTMLGFHFGLKTVAKSTFDLLFPELGLVE
EDYLEMSWGESFAYLAGLETVSQLNNRFLKFDERAFKTKVDLTKEPLPSKAFYGLLERLSKEPNGFIALNGFGGQMSKIS
SDFTPFPHRSGTRLMVEYIVAWNQSEQKKKTEFLDWLEKVYEFMKPFVSKNPRLGYVNHIDLDLGGIDWGNKTVVNNAIE
ISRSWGESYFLSNYERLIRAKTLIDPNNVFNHPQSIPPMANFDYLEKTLGSDGGEVVI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MENKTPIFFSLSIFLSLLNCAEAGNDLLSCLTFNGVRNHTVFSADSDSDFNRFLHLSIQNPLFQNSLISKPSAIILPGSK
EELSNTIRCIRKGSWTIRLRSGGHSYEGLSYTSDTPFILIDLMNLNRVSIDLESETAWVESGSTLGELYYAITESSSKLG
FTAAWCPTVGTGGHISGGGFGMMSRKYGLAADNVVDAILIDANGAILDRQAMGEDVFWAIRGGGGGVWGAIYAWKIKLLP
VPEKVTVFRVTKNVAIDEATSLLHKWQFVAEELEEDFTLSVLGGADEKQVWLTMLGFHFGLKTVAKSTFDLLFPELGLVE
EDYLEMSWGESFAYLAGLETVSQLNNRFLKFDERAFKTKVDLTKEPLPSKAFYGLLERLSKEPNGFIALNGFGGQMSKIS
SDFTPFPHRSGTRLMVEYIVAWNQSEQKKKTEFLDWLEKVYEFMKPFVSKNPRLGYVNHIDLDLGGIDWGNKTVVNNAIE
ISRSWGESYFLSNYERLIRAKTLIDPNNVFNHPQSIPPMANFDYLEKTLGSDGGEVVI
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
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   GLU n 
1 3   ASN n 
1 4   LYS n 
1 5   THR n 
1 6   PRO n 
1 7   ILE n 
1 8   PHE n 
1 9   PHE n 
1 10  SER n 
1 11  LEU n 
1 12  SER n 
1 13  ILE n 
1 14  PHE n 
1 15  LEU n 
1 16  SER n 
1 17  LEU n 
1 18  LEU n 
1 19  ASN n 
1 20  CYS n 
1 21  ALA n 
1 22  GLU n 
1 23  ALA n 
1 24  GLY n 
1 25  ASN n 
1 26  ASP n 
1 27  LEU n 
1 28  LEU n 
1 29  SER n 
1 30  CYS n 
1 31  LEU n 
1 32  THR n 
1 33  PHE n 
1 34  ASN n 
1 35  GLY n 
1 36  VAL n 
1 37  ARG n 
1 38  ASN n 
1 39  HIS n 
1 40  THR n 
1 41  VAL n 
1 42  PHE n 
1 43  SER n 
1 44  ALA n 
1 45  ASP n 
1 46  SER n 
1 47  ASP n 
1 48  SER n 
1 49  ASP n 
1 50  PHE n 
1 51  ASN n 
1 52  ARG n 
1 53  PHE n 
1 54  LEU n 
1 55  HIS n 
1 56  LEU n 
1 57  SER n 
1 58  ILE n 
1 59  GLN n 
1 60  ASN n 
1 61  PRO n 
1 62  LEU n 
1 63  PHE n 
1 64  GLN n 
1 65  ASN n 
1 66  SER n 
1 67  LEU n 
1 68  ILE n 
1 69  SER n 
1 70  LYS n 
1 71  PRO n 
1 72  SER n 
1 73  ALA n 
1 74  ILE n 
1 75  ILE n 
1 76  LEU n 
1 77  PRO n 
1 78  GLY n 
1 79  SER n 
1 80  LYS n 
1 81  GLU n 
1 82  GLU n 
1 83  LEU n 
1 84  SER n 
1 85  ASN n 
1 86  THR n 
1 87  ILE n 
1 88  ARG n 
1 89  CYS n 
1 90  ILE n 
1 91  ARG n 
1 92  LYS n 
1 93  GLY n 
1 94  SER n 
1 95  TRP n 
1 96  THR n 
1 97  ILE n 
1 98  ARG n 
1 99  LEU n 
1 100 ARG n 
1 101 SER n 
1 102 GLY n 
1 103 GLY n 
1 104 HIS n 
1 105 SER n 
1 106 TYR n 
1 107 GLU n 
1 108 GLY n 
1 109 LEU n 
1 110 SER n 
1 111 TYR n 
1 112 THR n 
1 113 SER n 
1 114 ASP n 
1 115 THR n 
1 116 PRO n 
1 117 PHE n 
1 118 ILE n 
1 119 LEU n 
1 120 ILE n 
1 121 ASP n 
1 122 LEU n 
1 123 MET n 
1 124 ASN n 
1 125 LEU n 
1 126 ASN n 
1 127 ARG n 
1 128 VAL n 
1 129 SER n 
1 130 ILE n 
1 131 ASP n 
1 132 LEU n 
1 133 GLU n 
1 134 SER n 
1 135 GLU n 
1 136 THR n 
1 137 ALA n 
1 138 TRP n 
1 139 VAL n 
1 140 GLU n 
1 141 SER n 
1 142 GLY n 
1 143 SER n 
1 144 THR n 
1 145 LEU n 
1 146 GLY n 
1 147 GLU n 
1 148 LEU n 
1 149 TYR n 
1 150 TYR n 
1 151 ALA n 
1 152 ILE n 
1 153 THR n 
1 154 GLU n 
1 155 SER n 
1 156 SER n 
1 157 SER n 
1 158 LYS n 
1 159 LEU n 
1 160 GLY n 
1 161 PHE n 
1 162 THR n 
1 163 ALA n 
1 164 ALA n 
1 165 TRP n 
1 166 CYS n 
1 167 PRO n 
1 168 THR n 
1 169 VAL n 
1 170 GLY n 
1 171 THR n 
1 172 GLY n 
1 173 GLY n 
1 174 HIS n 
1 175 ILE n 
1 176 SER n 
1 177 GLY n 
1 178 GLY n 
1 179 GLY n 
1 180 PHE n 
1 181 GLY n 
1 182 MET n 
1 183 MET n 
1 184 SER n 
1 185 ARG n 
1 186 LYS n 
1 187 TYR n 
1 188 GLY n 
1 189 LEU n 
1 190 ALA n 
1 191 ALA n 
1 192 ASP n 
1 193 ASN n 
1 194 VAL n 
1 195 VAL n 
1 196 ASP n 
1 197 ALA n 
1 198 ILE n 
1 199 LEU n 
1 200 ILE n 
1 201 ASP n 
1 202 ALA n 
1 203 ASN n 
1 204 GLY n 
1 205 ALA n 
1 206 ILE n 
1 207 LEU n 
1 208 ASP n 
1 209 ARG n 
1 210 GLN n 
1 211 ALA n 
1 212 MET n 
1 213 GLY n 
1 214 GLU n 
1 215 ASP n 
1 216 VAL n 
1 217 PHE n 
1 218 TRP n 
1 219 ALA n 
1 220 ILE n 
1 221 ARG n 
1 222 GLY n 
1 223 GLY n 
1 224 GLY n 
1 225 GLY n 
1 226 GLY n 
1 227 VAL n 
1 228 TRP n 
1 229 GLY n 
1 230 ALA n 
1 231 ILE n 
1 232 TYR n 
1 233 ALA n 
1 234 TRP n 
1 235 LYS n 
1 236 ILE n 
1 237 LYS n 
1 238 LEU n 
1 239 LEU n 
1 240 PRO n 
1 241 VAL n 
1 242 PRO n 
1 243 GLU n 
1 244 LYS n 
1 245 VAL n 
1 246 THR n 
1 247 VAL n 
1 248 PHE n 
1 249 ARG n 
1 250 VAL n 
1 251 THR n 
1 252 LYS n 
1 253 ASN n 
1 254 VAL n 
1 255 ALA n 
1 256 ILE n 
1 257 ASP n 
1 258 GLU n 
1 259 ALA n 
1 260 THR n 
1 261 SER n 
1 262 LEU n 
1 263 LEU n 
1 264 HIS n 
1 265 LYS n 
1 266 TRP n 
1 267 GLN n 
1 268 PHE n 
1 269 VAL n 
1 270 ALA n 
1 271 GLU n 
1 272 GLU n 
1 273 LEU n 
1 274 GLU n 
1 275 GLU n 
1 276 ASP n 
1 277 PHE n 
1 278 THR n 
1 279 LEU n 
1 280 SER n 
1 281 VAL n 
1 282 LEU n 
1 283 GLY n 
1 284 GLY n 
1 285 ALA n 
1 286 ASP n 
1 287 GLU n 
1 288 LYS n 
1 289 GLN n 
1 290 VAL n 
1 291 TRP n 
1 292 LEU n 
1 293 THR n 
1 294 MET n 
1 295 LEU n 
1 296 GLY n 
1 297 PHE n 
1 298 HIS n 
1 299 PHE n 
1 300 GLY n 
1 301 LEU n 
1 302 LYS n 
1 303 THR n 
1 304 VAL n 
1 305 ALA n 
1 306 LYS n 
1 307 SER n 
1 308 THR n 
1 309 PHE n 
1 310 ASP n 
1 311 LEU n 
1 312 LEU n 
1 313 PHE n 
1 314 PRO n 
1 315 GLU n 
1 316 LEU n 
1 317 GLY n 
1 318 LEU n 
1 319 VAL n 
1 320 GLU n 
1 321 GLU n 
1 322 ASP n 
1 323 TYR n 
1 324 LEU n 
1 325 GLU n 
1 326 MET n 
1 327 SER n 
1 328 TRP n 
1 329 GLY n 
1 330 GLU n 
1 331 SER n 
1 332 PHE n 
1 333 ALA n 
1 334 TYR n 
1 335 LEU n 
1 336 ALA n 
1 337 GLY n 
1 338 LEU n 
1 339 GLU n 
1 340 THR n 
1 341 VAL n 
1 342 SER n 
1 343 GLN n 
1 344 LEU n 
1 345 ASN n 
1 346 ASN n 
1 347 ARG n 
1 348 PHE n 
1 349 LEU n 
1 350 LYS n 
1 351 PHE n 
1 352 ASP n 
1 353 GLU n 
1 354 ARG n 
1 355 ALA n 
1 356 PHE n 
1 357 LYS n 
1 358 THR n 
1 359 LYS n 
1 360 VAL n 
1 361 ASP n 
1 362 LEU n 
1 363 THR n 
1 364 LYS n 
1 365 GLU n 
1 366 PRO n 
1 367 LEU n 
1 368 PRO n 
1 369 SER n 
1 370 LYS n 
1 371 ALA n 
1 372 PHE n 
1 373 TYR n 
1 374 GLY n 
1 375 LEU n 
1 376 LEU n 
1 377 GLU n 
1 378 ARG n 
1 379 LEU n 
1 380 SER n 
1 381 LYS n 
1 382 GLU n 
1 383 PRO n 
1 384 ASN n 
1 385 GLY n 
1 386 PHE n 
1 387 ILE n 
1 388 ALA n 
1 389 LEU n 
1 390 ASN n 
1 391 GLY n 
1 392 PHE n 
1 393 GLY n 
1 394 GLY n 
1 395 GLN n 
1 396 MET n 
1 397 SER n 
1 398 LYS n 
1 399 ILE n 
1 400 SER n 
1 401 SER n 
1 402 ASP n 
1 403 PHE n 
1 404 THR n 
1 405 PRO n 
1 406 PHE n 
1 407 PRO n 
1 408 HIS n 
1 409 ARG n 
1 410 SER n 
1 411 GLY n 
1 412 THR n 
1 413 ARG n 
1 414 LEU n 
1 415 MET n 
1 416 VAL n 
1 417 GLU n 
1 418 TYR n 
1 419 ILE n 
1 420 VAL n 
1 421 ALA n 
1 422 TRP n 
1 423 ASN n 
1 424 GLN n 
1 425 SER n 
1 426 GLU n 
1 427 GLN n 
1 428 LYS n 
1 429 LYS n 
1 430 LYS n 
1 431 THR n 
1 432 GLU n 
1 433 PHE n 
1 434 LEU n 
1 435 ASP n 
1 436 TRP n 
1 437 LEU n 
1 438 GLU n 
1 439 LYS n 
1 440 VAL n 
1 441 TYR n 
1 442 GLU n 
1 443 PHE n 
1 444 MET n 
1 445 LYS n 
1 446 PRO n 
1 447 PHE n 
1 448 VAL n 
1 449 SER n 
1 450 LYS n 
1 451 ASN n 
1 452 PRO n 
1 453 ARG n 
1 454 LEU n 
1 455 GLY n 
1 456 TYR n 
1 457 VAL n 
1 458 ASN n 
1 459 HIS n 
1 460 ILE n 
1 461 ASP n 
1 462 LEU n 
1 463 ASP n 
1 464 LEU n 
1 465 GLY n 
1 466 GLY n 
1 467 ILE n 
1 468 ASP n 
1 469 TRP n 
1 470 GLY n 
1 471 ASN n 
1 472 LYS n 
1 473 THR n 
1 474 VAL n 
1 475 VAL n 
1 476 ASN n 
1 477 ASN n 
1 478 ALA n 
1 479 ILE n 
1 480 GLU n 
1 481 ILE n 
1 482 SER n 
1 483 ARG n 
1 484 SER n 
1 485 TRP n 
1 486 GLY n 
1 487 GLU n 
1 488 SER n 
1 489 TYR n 
1 490 PHE n 
1 491 LEU n 
1 492 SER n 
1 493 ASN n 
1 494 TYR n 
1 495 GLU n 
1 496 ARG n 
1 497 LEU n 
1 498 ILE n 
1 499 ARG n 
1 500 ALA n 
1 501 LYS n 
1 502 THR n 
1 503 LEU n 
1 504 ILE n 
1 505 ASP n 
1 506 PRO n 
1 507 ASN n 
1 508 ASN n 
1 509 VAL n 
1 510 PHE n 
1 511 ASN n 
1 512 HIS n 
1 513 PRO n 
1 514 GLN n 
1 515 SER n 
1 516 ILE n 
1 517 PRO n 
1 518 PRO n 
1 519 MET n 
1 520 ALA n 
1 521 ASN n 
1 522 PHE n 
1 523 ASP n 
1 524 TYR n 
1 525 LEU n 
1 526 GLU n 
1 527 LYS n 
1 528 THR n 
1 529 LEU n 
1 530 GLY n 
1 531 SER n 
1 532 ASP n 
1 533 GLY n 
1 534 GLY n 
1 535 GLU n 
1 536 VAL n 
1 537 VAL n 
1 538 ILE 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'California poppy' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 BBE1 
_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      'Eschscholzia californica' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3467 
_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               'Pichia pastoris' 
_entity_src_gen.pdbx_host_org_scientific_name      'Komagataella pastoris' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4922 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RETO_ESCCA 
_struct_ref.pdbx_db_accession          P30986 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MENKTPIFFSLSIFLSLLNCALGGNDLLSCLTFNGVRNHTVFSADSDSDFNRFLHLSIQNPLFQNSLISKPSAIILPGSK
EELSNTIRCIRKGSWTIRLRSGGHSYEGLSYTSDTPFILIDLMNLNRVSIDLESETAWVESGSTLGELYYAITESSSKLG
FTAGWCPTVGTGGHISGGGFGMMSRKYGLAADNVVDAILIDANGAILDRQAMGEDVFWAIRGGGGGVWGAIYAWKIKLLP
VPEKVTVFRVTKNVAIDEATSLLHKWQFVAEELEEDFTLSVLGGADEKQVWLTMLGFHFGLKTVAKSTFDLLFPELGLVE
EDYLEMSWGESFAYLAGLETVSQLNNRFLKFDERAFKTKVDLTKEPLPSKAFYGLLERLSKEPNGFIALNGFGGQMSKIS
SDFTPFPHRSGTRLMVEYIVAWNQSEQKKKTEFLDWLEKVYEFMKPFVSKNPRLGYVNHIDLDLGGIDWGNKTVVNNAIE
ISRSWGESYFLSNYERLIRAKTLIDPNNVFNHPQSIPPMANFDYLEKTLGSDGGEVVI
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
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 4PZF A 1 ? 538 ? P30986 1 ? 538 ? 1 538 
2 1 4PZF B 1 ? 538 ? P30986 1 ? 538 ? 1 538 
3 1 4PZF C 1 ? 538 ? P30986 1 ? 538 ? 1 538 
4 1 4PZF D 1 ? 538 ? P30986 1 ? 538 ? 1 538 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4PZF GLU A 22  ? UNP P30986 LEU 22  'SEE REMARK 999'      22  1  
1 4PZF ALA A 23  ? UNP P30986 GLY 23  'SEE REMARK 999'      23  2  
1 4PZF ALA A 164 ? UNP P30986 GLY 164 'ENGINEERED MUTATION' 164 3  
2 4PZF GLU B 22  ? UNP P30986 LEU 22  'SEE REMARK 999'      22  4  
2 4PZF ALA B 23  ? UNP P30986 GLY 23  'SEE REMARK 999'      23  5  
2 4PZF ALA B 164 ? UNP P30986 GLY 164 'ENGINEERED MUTATION' 164 6  
3 4PZF GLU C 22  ? UNP P30986 LEU 22  'SEE REMARK 999'      22  7  
3 4PZF ALA C 23  ? UNP P30986 GLY 23  'SEE REMARK 999'      23  8  
3 4PZF ALA C 164 ? UNP P30986 GLY 164 'ENGINEERED MUTATION' 164 9  
4 4PZF GLU D 22  ? UNP P30986 LEU 22  'SEE REMARK 999'      22  10 
4 4PZF ALA D 23  ? UNP P30986 GLY 23  'SEE REMARK 999'      23  11 
4 4PZF ALA D 164 ? UNP P30986 GLY 164 'ENGINEERED MUTATION' 164 12 
# 
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 
12P non-polymer         . 'DODECAETHYLENE GLYCOL'       'POLYETHYLENE GLYCOL PEG400' 'C24 H50 O13'       546.646 
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 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE        ?                            'C8 H15 N O6'       221.208 
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 
SO4 non-polymer         . 'SULFATE ION'                 ?                            'O4 S -2'           96.063  
THR 'L-peptide linking' y THREONINE                     ?                            'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ?                            'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ?                            'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ?                            'C5 H11 N O2'       117.146 
# 
_exptl.entry_id          4PZF 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.89 
_exptl_crystal.density_percent_sol   57.43 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    
'30mg/mL protein + 0.1 M HEPES pH 7.5, 2.0 M Ammonium sulfate, BATCH, VAPOR DIFFUSION, SITTING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 6M-F' 
_diffrn_detector.pdbx_collection_date   2014-03-10 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    
'carved single silicon (111) crystal with a channel in the middle (called channel-cut design)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97242 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.97242 
# 
_reflns.entry_id                     4PZF 
_reflns.observed_criterion_sigma_I   3 
_reflns.observed_criterion_sigma_F   3 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            2.2 
_reflns.number_obs                   140296 
_reflns.number_all                   141762 
_reflns.percent_possible_obs         99 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        11.78 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              8.2 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.2 
_reflns_shell.d_res_low              2.3 
_reflns_shell.percent_possible_all   98.4 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    1.63 
_reflns_shell.pdbx_redundancy        8.2 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      17490 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 4PZF 
_refine.ls_number_reflns_obs                     140140 
_refine.ls_number_reflns_all                     141762 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             47.378 
_refine.ls_d_res_high                            2.200 
_refine.ls_percent_reflns_obs                    98.87 
_refine.ls_R_factor_obs                          0.2209 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2198 
_refine.ls_R_factor_R_free                       0.2419 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_number_reflns_R_free                  7008 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'pdb entry 3D2H' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.27 
_refine.pdbx_overall_phase_error                 28.80 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        15713 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         455 
_refine_hist.number_atoms_solvent             308 
_refine_hist.number_atoms_total               16476 
_refine_hist.d_res_high                       2.200 
_refine_hist.d_res_low                        47.378 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
f_bond_d           0.004  ? ? 16596 ? 'X-RAY DIFFRACTION' 
f_angle_d          0.840  ? ? 22482 ? 'X-RAY DIFFRACTION' 
f_dihedral_angle_d 15.094 ? ? 5955  ? 'X-RAY DIFFRACTION' 
f_chiral_restr     0.031  ? ? 2453  ? 'X-RAY DIFFRACTION' 
f_plane_restr      0.003  ? ? 2814  ? 'X-RAY DIFFRACTION' 
# 
loop_
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
. 2.2000 2.2250  4341 0.3539 98.00  0.3716 . . 229 . . . . 'X-RAY DIFFRACTION' 
. 2.2250 2.2512  4402 0.3275 98.00  0.3955 . . 232 . . . . 'X-RAY DIFFRACTION' 
. 2.2512 2.2786  4330 0.3142 98.00  0.3242 . . 228 . . . . 'X-RAY DIFFRACTION' 
. 2.2786 2.3075  4401 0.2962 98.00  0.3378 . . 231 . . . . 'X-RAY DIFFRACTION' 
. 2.3075 2.3378  4319 0.3019 98.00  0.3115 . . 227 . . . . 'X-RAY DIFFRACTION' 
. 2.3378 2.3699  4419 0.2934 99.00  0.3195 . . 233 . . . . 'X-RAY DIFFRACTION' 
. 2.3699 2.4037  4318 0.2948 98.00  0.3375 . . 227 . . . . 'X-RAY DIFFRACTION' 
. 2.4037 2.4396  4419 0.2840 98.00  0.3124 . . 232 . . . . 'X-RAY DIFFRACTION' 
. 2.4396 2.4777  4372 0.2710 99.00  0.2930 . . 229 . . . . 'X-RAY DIFFRACTION' 
. 2.4777 2.5183  4403 0.2725 99.00  0.2940 . . 232 . . . . 'X-RAY DIFFRACTION' 
. 2.5183 2.5618  4349 0.2669 99.00  0.3199 . . 229 . . . . 'X-RAY DIFFRACTION' 
. 2.5618 2.6083  4451 0.2591 99.00  0.3039 . . 235 . . . . 'X-RAY DIFFRACTION' 
. 2.6083 2.6585  4351 0.2557 99.00  0.2715 . . 229 . . . . 'X-RAY DIFFRACTION' 
. 2.6585 2.7128  4418 0.2466 98.00  0.2808 . . 233 . . . . 'X-RAY DIFFRACTION' 
. 2.7128 2.7717  4404 0.2572 99.00  0.2831 . . 232 . . . . 'X-RAY DIFFRACTION' 
. 2.7717 2.8362  4415 0.2543 99.00  0.2726 . . 232 . . . . 'X-RAY DIFFRACTION' 
. 2.8362 2.9071  4414 0.2581 99.00  0.3224 . . 232 . . . . 'X-RAY DIFFRACTION' 
. 2.9071 2.9857  4446 0.2586 99.00  0.2824 . . 234 . . . . 'X-RAY DIFFRACTION' 
. 2.9857 3.0736  4405 0.2497 99.00  0.2663 . . 232 . . . . 'X-RAY DIFFRACTION' 
. 3.0736 3.1727  4435 0.2438 99.00  0.2631 . . 234 . . . . 'X-RAY DIFFRACTION' 
. 3.1727 3.2861  4452 0.2317 99.00  0.2409 . . 234 . . . . 'X-RAY DIFFRACTION' 
. 3.2861 3.4176  4460 0.2260 99.00  0.2447 . . 235 . . . . 'X-RAY DIFFRACTION' 
. 3.4176 3.5731  4476 0.2240 99.00  0.2385 . . 236 . . . . 'X-RAY DIFFRACTION' 
. 3.5731 3.7614  4473 0.2018 99.00  0.2315 . . 235 . . . . 'X-RAY DIFFRACTION' 
. 3.7614 3.9970  4501 0.1914 99.00  0.2264 . . 237 . . . . 'X-RAY DIFFRACTION' 
. 3.9970 4.3054  4505 0.1803 100.00 0.2077 . . 237 . . . . 'X-RAY DIFFRACTION' 
. 4.3054 4.7383  4536 0.1681 100.00 0.1825 . . 239 . . . . 'X-RAY DIFFRACTION' 
. 4.7383 5.4231  4551 0.1759 99.00  0.1981 . . 240 . . . . 'X-RAY DIFFRACTION' 
. 5.4231 6.8293  4604 0.1875 100.00 0.1960 . . 242 . . . . 'X-RAY DIFFRACTION' 
. 6.8293 47.3889 4762 0.1775 99.00  0.1814 . . 251 . . . . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4PZF 
_struct.title                     'Berberine bridge enzyme G164A variant, a reticuline dehydrogenase' 
_struct.pdbx_descriptor           'Reticuline oxidase (E.C.1.21.3.3)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4PZF 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
;FLAVOPROTEIN, BI-COVALENT FLAVINYLATION, OXIDOREDUCTASE, Reticuline oxidase, Berberine bridge-forming enzyme, Tetrahydroprotoberberine synthase
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 2 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 4 ? 
N  N N 2 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 5 ? 
S  N N 4 ? 
T  N N 4 ? 
U  N N 2 ? 
V  N N 3 ? 
W  N N 3 ? 
X  N N 3 ? 
Y  N N 5 ? 
Z  N N 4 ? 
AA N N 4 ? 
BA N N 6 ? 
CA N N 6 ? 
DA N N 6 ? 
EA N N 6 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  ASP A 26  ? ASN A 34  ? ASP A 26  ASN A 34  1 ? 9  
HELX_P HELX_P2  2  SER A 48  ? SER A 57  ? SER A 48  SER A 57  1 ? 10 
HELX_P HELX_P3  3  ASN A 60  ? GLN A 64  ? ASN A 60  GLN A 64  5 ? 5  
HELX_P HELX_P4  4  SER A 79  ? GLY A 93  ? SER A 79  GLY A 93  1 ? 15 
HELX_P HELX_P5  5  THR A 144 ? GLU A 154 ? THR A 144 GLU A 154 1 ? 11 
HELX_P HELX_P6  6  GLY A 170 ? GLY A 177 ? GLY A 170 GLY A 177 1 ? 8  
HELX_P HELX_P7  7  MET A 183 ? GLY A 188 ? MET A 183 GLY A 188 1 ? 6  
HELX_P HELX_P8  8  ALA A 190 ? ASP A 192 ? ALA A 190 ASP A 192 5 ? 3  
HELX_P HELX_P9  9  ASP A 208 ? GLY A 213 ? ASP A 208 GLY A 213 1 ? 6  
HELX_P HELX_P10 10 GLY A 213 ? ILE A 220 ? GLY A 213 ILE A 220 1 ? 8  
HELX_P HELX_P11 11 ALA A 255 ? LEU A 273 ? ALA A 255 LEU A 273 1 ? 19 
HELX_P HELX_P12 12 LEU A 301 ? PHE A 313 ? LEU A 301 PHE A 313 1 ? 13 
HELX_P HELX_P13 13 PRO A 314 ? GLY A 317 ? PRO A 314 GLY A 317 5 ? 4  
HELX_P HELX_P14 14 SER A 327 ? ALA A 336 ? SER A 327 ALA A 336 1 ? 10 
HELX_P HELX_P15 15 THR A 340 ? ASN A 346 ? THR A 340 ASN A 346 5 ? 7  
HELX_P HELX_P16 16 PRO A 368 ? LYS A 381 ? PRO A 368 LYS A 381 1 ? 14 
HELX_P HELX_P17 17 GLY A 393 ? LYS A 398 ? GLY A 393 LYS A 398 5 ? 6  
HELX_P HELX_P18 18 GLU A 426 ? LYS A 428 ? GLU A 426 LYS A 428 5 ? 3  
HELX_P HELX_P19 19 LYS A 429 ? LYS A 445 ? LYS A 429 LYS A 445 1 ? 17 
HELX_P HELX_P20 20 TYR A 456 ? ILE A 460 ? TYR A 456 ILE A 460 5 ? 5  
HELX_P HELX_P21 21 ASP A 461 ? GLY A 465 ? ASP A 461 GLY A 465 5 ? 5  
HELX_P HELX_P22 22 ASN A 471 ? ASN A 477 ? ASN A 471 ASN A 477 1 ? 7  
HELX_P HELX_P23 23 ASN A 477 ? LEU A 491 ? ASN A 477 LEU A 491 1 ? 15 
HELX_P HELX_P24 24 ASN A 493 ? ASP A 505 ? ASN A 493 ASP A 505 1 ? 13 
HELX_P HELX_P25 25 ASP B 26  ? ASN B 34  ? ASP B 26  ASN B 34  1 ? 9  
HELX_P HELX_P26 26 SER B 48  ? SER B 57  ? SER B 48  SER B 57  1 ? 10 
HELX_P HELX_P27 27 ASN B 60  ? GLN B 64  ? ASN B 60  GLN B 64  5 ? 5  
HELX_P HELX_P28 28 SER B 79  ? GLY B 93  ? SER B 79  GLY B 93  1 ? 15 
HELX_P HELX_P29 29 THR B 144 ? GLU B 154 ? THR B 144 GLU B 154 1 ? 11 
HELX_P HELX_P30 30 GLY B 170 ? GLY B 177 ? GLY B 170 GLY B 177 1 ? 8  
HELX_P HELX_P31 31 MET B 183 ? GLY B 188 ? MET B 183 GLY B 188 1 ? 6  
HELX_P HELX_P32 32 ALA B 190 ? ASP B 192 ? ALA B 190 ASP B 192 5 ? 3  
HELX_P HELX_P33 33 ASP B 208 ? ILE B 220 ? ASP B 208 ILE B 220 1 ? 13 
HELX_P HELX_P34 34 ALA B 255 ? LEU B 273 ? ALA B 255 LEU B 273 1 ? 19 
HELX_P HELX_P35 35 LEU B 301 ? PHE B 313 ? LEU B 301 PHE B 313 1 ? 13 
HELX_P HELX_P36 36 PRO B 314 ? GLY B 317 ? PRO B 314 GLY B 317 5 ? 4  
HELX_P HELX_P37 37 VAL B 319 ? TYR B 323 ? VAL B 319 TYR B 323 5 ? 5  
HELX_P HELX_P38 38 SER B 327 ? ALA B 336 ? SER B 327 ALA B 336 1 ? 10 
HELX_P HELX_P39 39 THR B 340 ? ASN B 346 ? THR B 340 ASN B 346 5 ? 7  
HELX_P HELX_P40 40 PRO B 368 ? LYS B 381 ? PRO B 368 LYS B 381 1 ? 14 
HELX_P HELX_P41 41 GLY B 394 ? ILE B 399 ? GLY B 394 ILE B 399 1 ? 6  
HELX_P HELX_P42 42 ASN B 423 ? LYS B 428 ? ASN B 423 LYS B 428 5 ? 6  
HELX_P HELX_P43 43 LYS B 429 ? LYS B 445 ? LYS B 429 LYS B 445 1 ? 17 
HELX_P HELX_P44 44 TYR B 456 ? ILE B 460 ? TYR B 456 ILE B 460 5 ? 5  
HELX_P HELX_P45 45 ASP B 461 ? GLY B 465 ? ASP B 461 GLY B 465 5 ? 5  
HELX_P HELX_P46 46 ASN B 471 ? ASN B 476 ? ASN B 471 ASN B 476 1 ? 6  
HELX_P HELX_P47 47 ASN B 477 ? LEU B 491 ? ASN B 477 LEU B 491 1 ? 15 
HELX_P HELX_P48 48 ASN B 493 ? ASP B 505 ? ASN B 493 ASP B 505 1 ? 13 
HELX_P HELX_P49 49 ASP C 26  ? ASN C 34  ? ASP C 26  ASN C 34  1 ? 9  
HELX_P HELX_P50 50 SER C 48  ? SER C 57  ? SER C 48  SER C 57  1 ? 10 
HELX_P HELX_P51 51 ASN C 60  ? GLN C 64  ? ASN C 60  GLN C 64  5 ? 5  
HELX_P HELX_P52 52 SER C 79  ? GLY C 93  ? SER C 79  GLY C 93  1 ? 15 
HELX_P HELX_P53 53 THR C 144 ? GLU C 154 ? THR C 144 GLU C 154 1 ? 11 
HELX_P HELX_P54 54 GLY C 170 ? GLY C 177 ? GLY C 170 GLY C 177 1 ? 8  
HELX_P HELX_P55 55 MET C 183 ? GLY C 188 ? MET C 183 GLY C 188 1 ? 6  
HELX_P HELX_P56 56 ALA C 190 ? ASP C 192 ? ALA C 190 ASP C 192 5 ? 3  
HELX_P HELX_P57 57 ASP C 208 ? ILE C 220 ? ASP C 208 ILE C 220 1 ? 13 
HELX_P HELX_P58 58 ALA C 255 ? GLU C 271 ? ALA C 255 GLU C 271 1 ? 17 
HELX_P HELX_P59 59 LEU C 301 ? PHE C 313 ? LEU C 301 PHE C 313 1 ? 13 
HELX_P HELX_P60 60 PRO C 314 ? GLY C 317 ? PRO C 314 GLY C 317 5 ? 4  
HELX_P HELX_P61 61 VAL C 319 ? TYR C 323 ? VAL C 319 TYR C 323 5 ? 5  
HELX_P HELX_P62 62 SER C 327 ? ALA C 336 ? SER C 327 ALA C 336 1 ? 10 
HELX_P HELX_P63 63 THR C 340 ? ASN C 346 ? THR C 340 ASN C 346 5 ? 7  
HELX_P HELX_P64 64 PRO C 368 ? LYS C 381 ? PRO C 368 LYS C 381 1 ? 14 
HELX_P HELX_P65 65 GLY C 393 ? LYS C 398 ? GLY C 393 LYS C 398 5 ? 6  
HELX_P HELX_P66 66 ASN C 423 ? LYS C 428 ? ASN C 423 LYS C 428 5 ? 6  
HELX_P HELX_P67 67 LYS C 429 ? LYS C 445 ? LYS C 429 LYS C 445 1 ? 17 
HELX_P HELX_P68 68 PRO C 446 ? VAL C 448 ? PRO C 446 VAL C 448 5 ? 3  
HELX_P HELX_P69 69 TYR C 456 ? ILE C 460 ? TYR C 456 ILE C 460 5 ? 5  
HELX_P HELX_P70 70 ASP C 461 ? GLY C 465 ? ASP C 461 GLY C 465 5 ? 5  
HELX_P HELX_P71 71 ASN C 471 ? ASN C 477 ? ASN C 471 ASN C 477 1 ? 7  
HELX_P HELX_P72 72 ASN C 477 ? SER C 482 ? ASN C 477 SER C 482 1 ? 6  
HELX_P HELX_P73 73 SER C 482 ? LEU C 491 ? SER C 482 LEU C 491 1 ? 10 
HELX_P HELX_P74 74 ASN C 493 ? ASP C 505 ? ASN C 493 ASP C 505 1 ? 13 
HELX_P HELX_P75 75 LEU D 27  ? ASN D 34  ? LEU D 27  ASN D 34  1 ? 8  
HELX_P HELX_P76 76 SER D 48  ? SER D 57  ? SER D 48  SER D 57  1 ? 10 
HELX_P HELX_P77 77 ASN D 60  ? GLN D 64  ? ASN D 60  GLN D 64  5 ? 5  
HELX_P HELX_P78 78 SER D 79  ? GLY D 93  ? SER D 79  GLY D 93  1 ? 15 
HELX_P HELX_P79 79 THR D 144 ? GLU D 154 ? THR D 144 GLU D 154 1 ? 11 
HELX_P HELX_P80 80 GLY D 170 ? GLY D 177 ? GLY D 170 GLY D 177 1 ? 8  
HELX_P HELX_P81 81 MET D 183 ? GLY D 188 ? MET D 183 GLY D 188 1 ? 6  
HELX_P HELX_P82 82 LEU D 189 ? ASP D 192 ? LEU D 189 ASP D 192 5 ? 4  
HELX_P HELX_P83 83 ASP D 208 ? GLY D 213 ? ASP D 208 GLY D 213 1 ? 6  
HELX_P HELX_P84 84 GLY D 213 ? ILE D 220 ? GLY D 213 ILE D 220 1 ? 8  
HELX_P HELX_P85 85 ALA D 255 ? LEU D 273 ? ALA D 255 LEU D 273 1 ? 19 
HELX_P HELX_P86 86 LEU D 301 ? PHE D 313 ? LEU D 301 PHE D 313 1 ? 13 
HELX_P HELX_P87 87 PRO D 314 ? GLY D 317 ? PRO D 314 GLY D 317 5 ? 4  
HELX_P HELX_P88 88 SER D 327 ? ALA D 336 ? SER D 327 ALA D 336 1 ? 10 
HELX_P HELX_P89 89 THR D 340 ? ASN D 346 ? THR D 340 ASN D 346 5 ? 7  
HELX_P HELX_P90 90 PRO D 368 ? LYS D 381 ? PRO D 368 LYS D 381 1 ? 14 
HELX_P HELX_P91 91 GLY D 394 ? ILE D 399 ? GLY D 394 ILE D 399 1 ? 6  
HELX_P HELX_P92 92 SER D 425 ? LYS D 428 ? SER D 425 LYS D 428 5 ? 4  
HELX_P HELX_P93 93 LYS D 429 ? LYS D 445 ? LYS D 429 LYS D 445 1 ? 17 
HELX_P HELX_P94 94 TYR D 456 ? ILE D 460 ? TYR D 456 ILE D 460 5 ? 5  
HELX_P HELX_P95 95 ASP D 461 ? GLY D 465 ? ASP D 461 GLY D 465 5 ? 5  
HELX_P HELX_P96 96 ASN D 471 ? ASN D 477 ? ASN D 471 ASN D 477 1 ? 7  
HELX_P HELX_P97 97 ASN D 477 ? SER D 482 ? ASN D 477 SER D 482 1 ? 6  
HELX_P HELX_P98 98 SER D 482 ? LEU D 491 ? SER D 482 LEU D 491 1 ? 10 
HELX_P HELX_P99 99 ASN D 493 ? ASP D 505 ? ASN D 493 ASP D 505 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 30  SG  ? ? ? 1_555 A CYS 89 SG  ? ? A CYS 30  A CYS 89  1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf2  disulf ? ? B CYS 30  SG  ? ? ? 1_555 B CYS 89 SG  ? ? B CYS 30  B CYS 89  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf3  disulf ? ? C CYS 30  SG  ? ? ? 1_555 C CYS 89 SG  ? ? C CYS 30  C CYS 89  1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf4  disulf ? ? D CYS 30  SG  ? ? ? 1_555 D CYS 89 SG  ? ? D CYS 30  D CYS 89  1_555 ? ? ? ? ? ? ? 2.045 ? 
covale1  covale ? ? J NAG .   O4  ? ? ? 1_555 K NAG .  C1  ? ? B NAG 602 B NAG 603 1_555 ? ? ? ? ? ? ? 1.419 ? 
covale2  covale ? ? C ASN 471 ND2 ? ? ? 1_555 Q NAG .  C1  ? ? C ASN 471 C NAG 604 1_555 ? ? ? ? ? ? ? 1.421 ? 
covale3  covale ? ? A ASN 471 ND2 ? ? ? 1_555 H NAG .  C1  ? ? A ASN 471 A NAG 604 1_555 ? ? ? ? ? ? ? 1.421 ? 
covale4  covale ? ? F NAG .   O4  ? ? ? 1_555 G NAG .  C1  ? ? A NAG 602 A NAG 603 1_555 ? ? ? ? ? ? ? 1.424 ? 
covale5  covale ? ? V NAG .   O4  ? ? ? 1_555 W NAG .  C1  ? ? D NAG 602 D NAG 603 1_555 ? ? ? ? ? ? ? 1.424 ? 
covale6  covale ? ? O NAG .   O4  ? ? ? 1_555 P NAG .  C1  ? ? C NAG 602 C NAG 603 1_555 ? ? ? ? ? ? ? 1.427 ? 
covale7  covale ? ? B ASN 38  ND2 ? ? ? 1_555 J NAG .  C1  ? ? B ASN 38  B NAG 602 1_555 ? ? ? ? ? ? ? 1.432 ? 
covale8  covale ? ? D ASN 471 ND2 ? ? ? 1_555 X NAG .  C1  ? ? D ASN 471 D NAG 604 1_555 ? ? ? ? ? ? ? 1.433 ? 
covale9  covale ? ? B ASN 471 ND2 ? ? ? 1_555 L NAG .  C1  ? ? B ASN 471 B NAG 604 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale10 covale ? ? C ASN 38  ND2 ? ? ? 1_555 O NAG .  C1  ? ? C ASN 38  C NAG 602 1_555 ? ? ? ? ? ? ? 1.437 ? 
covale11 covale ? ? A ASN 38  ND2 ? ? ? 1_555 F NAG .  C1  ? ? A ASN 38  A NAG 602 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale12 covale ? ? D ASN 38  ND2 ? ? ? 1_555 V NAG .  C1  ? ? D ASN 38  D NAG 602 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale13 covale ? ? D HIS 104 ND1 ? ? ? 1_555 U FAD .  C8M ? ? D HIS 104 D FAD 601 1_555 ? ? ? ? ? ? ? 1.534 ? 
covale14 covale ? ? C HIS 104 ND1 ? ? ? 1_555 N FAD .  C8M ? ? C HIS 104 C FAD 601 1_555 ? ? ? ? ? ? ? 1.537 ? 
covale15 covale ? ? B HIS 104 ND1 ? ? ? 1_555 I FAD .  C8M ? ? B HIS 104 B FAD 601 1_555 ? ? ? ? ? ? ? 1.537 ? 
covale16 covale ? ? A HIS 104 ND1 ? ? ? 1_555 E FAD .  C8M ? ? A HIS 104 A FAD 601 1_555 ? ? ? ? ? ? ? 1.553 ? 
covale17 covale ? ? C CYS 166 SG  ? ? ? 1_555 N FAD .  C6  ? ? C CYS 166 C FAD 601 1_555 ? ? ? ? ? ? ? 1.801 ? 
covale18 covale ? ? D CYS 166 SG  ? ? ? 1_555 U FAD .  C6  ? ? D CYS 166 D FAD 601 1_555 ? ? ? ? ? ? ? 1.802 ? 
covale19 covale ? ? B CYS 166 SG  ? ? ? 1_555 I FAD .  C6  ? ? B CYS 166 B FAD 601 1_555 ? ? ? ? ? ? ? 1.808 ? 
covale20 covale ? ? A CYS 166 SG  ? ? ? 1_555 E FAD .  C6  ? ? A CYS 166 A FAD 601 1_555 ? ? ? ? ? ? ? 1.827 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 ASN 451 A . ? ASN 451 A PRO 452 A ? PRO 452 A 1 -1.04 
2 ASN 451 B . ? ASN 451 B PRO 452 B ? PRO 452 B 1 -2.59 
3 ASN 451 C . ? ASN 451 C PRO 452 C ? PRO 452 C 1 -3.10 
4 ASN 451 D . ? ASN 451 D PRO 452 D ? PRO 452 D 1 -3.86 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 4 ? 
B ? 5 ? 
C ? 2 ? 
D ? 7 ? 
E ? 4 ? 
F ? 5 ? 
G ? 2 ? 
H ? 3 ? 
I ? 4 ? 
J ? 3 ? 
K ? 4 ? 
L ? 5 ? 
M ? 2 ? 
N ? 7 ? 
O ? 4 ? 
P ? 5 ? 
Q ? 2 ? 
R ? 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 
A 1 2 ? anti-parallel 
A 2 3 ? parallel      
A 3 4 ? parallel      
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
B 4 5 ? anti-parallel 
C 1 2 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
D 4 5 ? anti-parallel 
D 5 6 ? anti-parallel 
D 6 7 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? parallel      
E 3 4 ? parallel      
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
F 4 5 ? anti-parallel 
G 1 2 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
K 1 2 ? anti-parallel 
K 2 3 ? parallel      
K 3 4 ? parallel      
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
L 4 5 ? anti-parallel 
M 1 2 ? anti-parallel 
N 1 2 ? anti-parallel 
N 2 3 ? anti-parallel 
N 3 4 ? anti-parallel 
N 4 5 ? anti-parallel 
N 5 6 ? anti-parallel 
N 6 7 ? anti-parallel 
O 1 2 ? anti-parallel 
O 2 3 ? parallel      
O 3 4 ? parallel      
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? anti-parallel 
P 4 5 ? anti-parallel 
Q 1 2 ? anti-parallel 
R 1 2 ? anti-parallel 
R 2 3 ? anti-parallel 
R 3 4 ? anti-parallel 
R 4 5 ? anti-parallel 
R 5 6 ? anti-parallel 
R 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 
A 1 HIS A 39  ? VAL A 41  ? HIS A 39  VAL A 41  
A 2 ALA A 73  ? ILE A 75  ? ALA A 73  ILE A 75  
A 3 PHE A 117 ? ASP A 121 ? PHE A 117 ASP A 121 
A 4 THR A 96  ? ARG A 100 ? THR A 96  ARG A 100 
B 1 VAL A 128 ? ASP A 131 ? VAL A 128 ASP A 131 
B 2 THR A 136 ? GLU A 140 ? THR A 136 GLU A 140 
B 3 ALA A 230 ? LYS A 237 ? ALA A 230 LYS A 237 
B 4 VAL A 194 ? ILE A 200 ? VAL A 194 ILE A 200 
B 5 ILE A 206 ? LEU A 207 ? ILE A 206 LEU A 207 
C 1 LEU A 159 ? GLY A 160 ? LEU A 159 GLY A 160 
C 2 LEU A 239 ? PRO A 240 ? LEU A 239 PRO A 240 
D 1 LEU A 324 ? MET A 326 ? LEU A 324 MET A 326 
D 2 VAL A 245 ? VAL A 254 ? VAL A 245 VAL A 254 
D 3 VAL A 290 ? HIS A 298 ? VAL A 290 HIS A 298 
D 4 PHE A 277 ? GLY A 284 ? PHE A 277 GLY A 284 
D 5 GLY A 385 ? GLY A 391 ? GLY A 385 GLY A 391 
D 6 LEU A 414 ? TRP A 422 ? LEU A 414 TRP A 422 
D 7 ALA A 355 ? LEU A 362 ? ALA A 355 LEU A 362 
E 1 HIS B 39  ? VAL B 41  ? HIS B 39  VAL B 41  
E 2 ALA B 73  ? ILE B 75  ? ALA B 73  ILE B 75  
E 3 PHE B 117 ? ASP B 121 ? PHE B 117 ASP B 121 
E 4 THR B 96  ? ARG B 100 ? THR B 96  ARG B 100 
F 1 VAL B 128 ? ASP B 131 ? VAL B 128 ASP B 131 
F 2 THR B 136 ? GLU B 140 ? THR B 136 GLU B 140 
F 3 ALA B 230 ? LYS B 237 ? ALA B 230 LYS B 237 
F 4 VAL B 194 ? ILE B 200 ? VAL B 194 ILE B 200 
F 5 ILE B 206 ? LEU B 207 ? ILE B 206 LEU B 207 
G 1 LEU B 159 ? GLY B 160 ? LEU B 159 GLY B 160 
G 2 LEU B 239 ? PRO B 240 ? LEU B 239 PRO B 240 
H 1 PHE B 277 ? VAL B 281 ? PHE B 277 VAL B 281 
H 2 GLN B 289 ? HIS B 298 ? GLN B 289 HIS B 298 
H 3 GLY B 284 ? ASP B 286 ? GLY B 284 ASP B 286 
I 1 PHE B 277 ? VAL B 281 ? PHE B 277 VAL B 281 
I 2 GLN B 289 ? HIS B 298 ? GLN B 289 HIS B 298 
I 3 VAL B 245 ? VAL B 254 ? VAL B 245 VAL B 254 
I 4 LEU B 324 ? MET B 326 ? LEU B 324 MET B 326 
J 1 ALA B 355 ? LEU B 362 ? ALA B 355 LEU B 362 
J 2 LEU B 414 ? TRP B 422 ? LEU B 414 TRP B 422 
J 3 GLY B 385 ? GLY B 391 ? GLY B 385 GLY B 391 
K 1 HIS C 39  ? VAL C 41  ? HIS C 39  VAL C 41  
K 2 ALA C 73  ? ILE C 75  ? ALA C 73  ILE C 75  
K 3 PHE C 117 ? ASP C 121 ? PHE C 117 ASP C 121 
K 4 THR C 96  ? ARG C 100 ? THR C 96  ARG C 100 
L 1 VAL C 128 ? ASP C 131 ? VAL C 128 ASP C 131 
L 2 THR C 136 ? GLU C 140 ? THR C 136 GLU C 140 
L 3 ALA C 230 ? LYS C 237 ? ALA C 230 LYS C 237 
L 4 VAL C 194 ? ILE C 200 ? VAL C 194 ILE C 200 
L 5 ILE C 206 ? LEU C 207 ? ILE C 206 LEU C 207 
M 1 LEU C 159 ? GLY C 160 ? LEU C 159 GLY C 160 
M 2 LEU C 239 ? PRO C 240 ? LEU C 239 PRO C 240 
N 1 LEU C 324 ? MET C 326 ? LEU C 324 MET C 326 
N 2 VAL C 245 ? VAL C 254 ? VAL C 245 VAL C 254 
N 3 VAL C 290 ? HIS C 298 ? VAL C 290 HIS C 298 
N 4 PHE C 277 ? ALA C 285 ? PHE C 277 ALA C 285 
N 5 GLY C 385 ? GLY C 391 ? GLY C 385 GLY C 391 
N 6 LEU C 414 ? TRP C 422 ? LEU C 414 TRP C 422 
N 7 ALA C 355 ? LEU C 362 ? ALA C 355 LEU C 362 
O 1 HIS D 39  ? VAL D 41  ? HIS D 39  VAL D 41  
O 2 ALA D 73  ? ILE D 75  ? ALA D 73  ILE D 75  
O 3 PHE D 117 ? ASP D 121 ? PHE D 117 ASP D 121 
O 4 THR D 96  ? ARG D 100 ? THR D 96  ARG D 100 
P 1 VAL D 128 ? ASP D 131 ? VAL D 128 ASP D 131 
P 2 THR D 136 ? GLU D 140 ? THR D 136 GLU D 140 
P 3 ALA D 230 ? LYS D 237 ? ALA D 230 LYS D 237 
P 4 VAL D 194 ? ILE D 200 ? VAL D 194 ILE D 200 
P 5 ILE D 206 ? LEU D 207 ? ILE D 206 LEU D 207 
Q 1 LEU D 159 ? GLY D 160 ? LEU D 159 GLY D 160 
Q 2 LEU D 239 ? PRO D 240 ? LEU D 239 PRO D 240 
R 1 LEU D 324 ? MET D 326 ? LEU D 324 MET D 326 
R 2 VAL D 245 ? VAL D 254 ? VAL D 245 VAL D 254 
R 3 GLN D 289 ? HIS D 298 ? GLN D 289 HIS D 298 
R 4 PHE D 277 ? ASP D 286 ? PHE D 277 ASP D 286 
R 5 GLY D 385 ? GLY D 391 ? GLY D 385 GLY D 391 
R 6 LEU D 414 ? TRP D 422 ? LEU D 414 TRP D 422 
R 7 ALA D 355 ? LEU D 362 ? ALA D 355 LEU D 362 
# 
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 
A 1 2 N THR A 40  ? N THR A 40  O ILE A 74  ? O ILE A 74  
A 2 3 N ILE A 75  ? N ILE A 75  O LEU A 119 ? O LEU A 119 
A 3 4 O ILE A 120 ? O ILE A 120 N ARG A 98  ? N ARG A 98  
B 1 2 N SER A 129 ? N SER A 129 O TRP A 138 ? O TRP A 138 
B 2 3 N VAL A 139 ? N VAL A 139 O TRP A 234 ? O TRP A 234 
B 3 4 O TYR A 232 ? O TYR A 232 N ILE A 198 ? N ILE A 198 
B 4 5 N LEU A 199 ? N LEU A 199 O LEU A 207 ? O LEU A 207 
C 1 2 N GLY A 160 ? N GLY A 160 O LEU A 239 ? O LEU A 239 
D 1 2 O MET A 326 ? O MET A 326 N VAL A 245 ? N VAL A 245 
D 2 3 N LYS A 252 ? N LYS A 252 O LEU A 292 ? O LEU A 292 
D 3 4 O LEU A 295 ? O LEU A 295 N SER A 280 ? N SER A 280 
D 4 5 N GLY A 283 ? N GLY A 283 O ILE A 387 ? O ILE A 387 
D 5 6 N PHE A 386 ? N PHE A 386 O ILE A 419 ? O ILE A 419 
D 6 7 O VAL A 416 ? O VAL A 416 N ASP A 361 ? N ASP A 361 
E 1 2 N THR B 40  ? N THR B 40  O ILE B 74  ? O ILE B 74  
E 2 3 N ILE B 75  ? N ILE B 75  O LEU B 119 ? O LEU B 119 
E 3 4 O ILE B 120 ? O ILE B 120 N ARG B 98  ? N ARG B 98  
F 1 2 N SER B 129 ? N SER B 129 O TRP B 138 ? O TRP B 138 
F 2 3 N VAL B 139 ? N VAL B 139 O TRP B 234 ? O TRP B 234 
F 3 4 O TYR B 232 ? O TYR B 232 N ILE B 198 ? N ILE B 198 
F 4 5 N LEU B 199 ? N LEU B 199 O LEU B 207 ? O LEU B 207 
G 1 2 N GLY B 160 ? N GLY B 160 O LEU B 239 ? O LEU B 239 
H 1 2 N SER B 280 ? N SER B 280 O LEU B 295 ? O LEU B 295 
H 2 3 O TRP B 291 ? O TRP B 291 N GLY B 284 ? N GLY B 284 
I 1 2 N SER B 280 ? N SER B 280 O LEU B 295 ? O LEU B 295 
I 2 3 O MET B 294 ? O MET B 294 N VAL B 250 ? N VAL B 250 
I 3 4 N VAL B 245 ? N VAL B 245 O MET B 326 ? O MET B 326 
J 1 2 N ASP B 361 ? N ASP B 361 O VAL B 416 ? O VAL B 416 
J 2 3 O GLU B 417 ? O GLU B 417 N ALA B 388 ? N ALA B 388 
K 1 2 N THR C 40  ? N THR C 40  O ILE C 74  ? O ILE C 74  
K 2 3 N ILE C 75  ? N ILE C 75  O LEU C 119 ? O LEU C 119 
K 3 4 O ILE C 120 ? O ILE C 120 N ARG C 98  ? N ARG C 98  
L 1 2 N ASP C 131 ? N ASP C 131 O THR C 136 ? O THR C 136 
L 2 3 N VAL C 139 ? N VAL C 139 O TRP C 234 ? O TRP C 234 
L 3 4 O TYR C 232 ? O TYR C 232 N ILE C 198 ? N ILE C 198 
L 4 5 N LEU C 199 ? N LEU C 199 O LEU C 207 ? O LEU C 207 
M 1 2 N GLY C 160 ? N GLY C 160 O LEU C 239 ? O LEU C 239 
N 1 2 O MET C 326 ? O MET C 326 N VAL C 245 ? N VAL C 245 
N 2 3 N VAL C 254 ? N VAL C 254 O VAL C 290 ? O VAL C 290 
N 3 4 O LEU C 295 ? O LEU C 295 N SER C 280 ? N SER C 280 
N 4 5 N GLY C 283 ? N GLY C 283 O ILE C 387 ? O ILE C 387 
N 5 6 N ALA C 388 ? N ALA C 388 O GLU C 417 ? O GLU C 417 
N 6 7 O TYR C 418 ? O TYR C 418 N LYS C 359 ? N LYS C 359 
O 1 2 N THR D 40  ? N THR D 40  O ILE D 74  ? O ILE D 74  
O 2 3 N ILE D 75  ? N ILE D 75  O LEU D 119 ? O LEU D 119 
O 3 4 O ILE D 120 ? O ILE D 120 N ARG D 98  ? N ARG D 98  
P 1 2 N ASP D 131 ? N ASP D 131 O THR D 136 ? O THR D 136 
P 2 3 N VAL D 139 ? N VAL D 139 O TRP D 234 ? O TRP D 234 
P 3 4 O LYS D 235 ? O LYS D 235 N ASP D 196 ? N ASP D 196 
P 4 5 N LEU D 199 ? N LEU D 199 O LEU D 207 ? O LEU D 207 
Q 1 2 N GLY D 160 ? N GLY D 160 O LEU D 239 ? O LEU D 239 
R 1 2 O MET D 326 ? O MET D 326 N VAL D 245 ? N VAL D 245 
R 2 3 N VAL D 250 ? N VAL D 250 O MET D 294 ? O MET D 294 
R 3 4 O THR D 293 ? O THR D 293 N LEU D 282 ? N LEU D 282 
R 4 5 N GLY D 283 ? N GLY D 283 O ILE D 387 ? O ILE D 387 
R 5 6 N ALA D 388 ? N ALA D 388 O GLU D 417 ? O GLU D 417 
R 6 7 O VAL D 416 ? O VAL D 416 N ASP D 361 ? N ASP D 361 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 27 'BINDING SITE FOR RESIDUE FAD A 601'                                      
AC2 Software ? ? ? ? 30 'BINDING SITE FOR RESIDUE FAD B 601'                                      
AC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE SO4 B 605'                                      
AC4 Software ? ? ? ? 29 'BINDING SITE FOR RESIDUE FAD C 601'                                      
AC5 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE 12P C 605'                                      
AC6 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE SO4 C 606'                                      
AC7 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE SO4 C 607'                                      
AC8 Software ? ? ? ? 27 'BINDING SITE FOR RESIDUE FAD D 601'                                      
AC9 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE 12P D 605'                                      
BC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE SO4 D 606'                                      
BC2 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE SO4 D 607'                                      
BC3 Software ? ? ? ? 6  'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 38 RESIDUES 602 TO 603' 
BC4 Software ? ? ? ? 2  'BINDING SITE FOR MONO-SACCHARIDE NAG A 604 BOUND TO ASN A 471'           
BC5 Software ? ? ? ? 4  'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 38 RESIDUES 602 TO 603' 
BC6 Software ? ? ? ? 3  'BINDING SITE FOR MONO-SACCHARIDE NAG B 604 BOUND TO ASN B 471'           
BC7 Software ? ? ? ? 5  'BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C 38 RESIDUES 602 TO 603' 
BC8 Software ? ? ? ? 3  'BINDING SITE FOR MONO-SACCHARIDE NAG C 604 BOUND TO ASN C 471'           
BC9 Software ? ? ? ? 6  'BINDING SITE FOR CHAIN D OF SUGAR BOUND TO ASN D 38 RESIDUES 602 TO 603' 
CC1 Software ? ? ? ? 3  'BINDING SITE FOR MONO-SACCHARIDE NAG D 604 BOUND TO ASN D 471'           
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 27 LEU A  99  ? LEU A 99  . ? 1_555 ? 
2   AC1 27 SER A  101 ? SER A 101 . ? 1_555 ? 
3   AC1 27 GLY A  102 ? GLY A 102 . ? 1_555 ? 
4   AC1 27 GLY A  103 ? GLY A 103 . ? 1_555 ? 
5   AC1 27 HIS A  104 ? HIS A 104 . ? 1_555 ? 
6   AC1 27 SER A  105 ? SER A 105 . ? 1_555 ? 
7   AC1 27 TYR A  106 ? TYR A 106 . ? 1_555 ? 
8   AC1 27 SER A  110 ? SER A 110 . ? 1_555 ? 
9   AC1 27 LEU A  122 ? LEU A 122 . ? 1_555 ? 
10  AC1 27 SER A  141 ? SER A 141 . ? 1_555 ? 
11  AC1 27 ALA A  164 ? ALA A 164 . ? 1_555 ? 
12  AC1 27 CYS A  166 ? CYS A 166 . ? 1_555 ? 
13  AC1 27 VAL A  169 ? VAL A 169 . ? 1_555 ? 
14  AC1 27 GLY A  170 ? GLY A 170 . ? 1_555 ? 
15  AC1 27 GLY A  172 ? GLY A 172 . ? 1_555 ? 
16  AC1 27 GLY A  173 ? GLY A 173 . ? 1_555 ? 
17  AC1 27 HIS A  174 ? HIS A 174 . ? 1_555 ? 
18  AC1 27 PHE A  180 ? PHE A 180 . ? 1_555 ? 
19  AC1 27 GLY A  225 ? GLY A 225 . ? 1_555 ? 
20  AC1 27 GLY A  226 ? GLY A 226 . ? 1_555 ? 
21  AC1 27 GLY A  229 ? GLY A 229 . ? 1_555 ? 
22  AC1 27 ILE A  231 ? ILE A 231 . ? 1_555 ? 
23  AC1 27 TYR A  456 ? TYR A 456 . ? 1_555 ? 
24  AC1 27 ASN A  458 ? ASN A 458 . ? 1_555 ? 
25  AC1 27 HOH BA .   ? HOH A 725 . ? 1_555 ? 
26  AC1 27 HOH BA .   ? HOH A 729 . ? 1_555 ? 
27  AC1 27 HOH BA .   ? HOH A 791 . ? 1_555 ? 
28  AC2 30 LEU B  99  ? LEU B 99  . ? 1_555 ? 
29  AC2 30 ARG B  100 ? ARG B 100 . ? 1_555 ? 
30  AC2 30 SER B  101 ? SER B 101 . ? 1_555 ? 
31  AC2 30 GLY B  102 ? GLY B 102 . ? 1_555 ? 
32  AC2 30 GLY B  103 ? GLY B 103 . ? 1_555 ? 
33  AC2 30 HIS B  104 ? HIS B 104 . ? 1_555 ? 
34  AC2 30 SER B  105 ? SER B 105 . ? 1_555 ? 
35  AC2 30 TYR B  106 ? TYR B 106 . ? 1_555 ? 
36  AC2 30 SER B  110 ? SER B 110 . ? 1_555 ? 
37  AC2 30 LEU B  122 ? LEU B 122 . ? 1_555 ? 
38  AC2 30 SER B  141 ? SER B 141 . ? 1_555 ? 
39  AC2 30 ALA B  164 ? ALA B 164 . ? 1_555 ? 
40  AC2 30 CYS B  166 ? CYS B 166 . ? 1_555 ? 
41  AC2 30 VAL B  169 ? VAL B 169 . ? 1_555 ? 
42  AC2 30 GLY B  170 ? GLY B 170 . ? 1_555 ? 
43  AC2 30 GLY B  172 ? GLY B 172 . ? 1_555 ? 
44  AC2 30 GLY B  173 ? GLY B 173 . ? 1_555 ? 
45  AC2 30 HIS B  174 ? HIS B 174 . ? 1_555 ? 
46  AC2 30 PHE B  180 ? PHE B 180 . ? 1_555 ? 
47  AC2 30 GLY B  225 ? GLY B 225 . ? 1_555 ? 
48  AC2 30 GLY B  226 ? GLY B 226 . ? 1_555 ? 
49  AC2 30 GLY B  229 ? GLY B 229 . ? 1_555 ? 
50  AC2 30 ILE B  231 ? ILE B 231 . ? 1_555 ? 
51  AC2 30 TYR B  456 ? TYR B 456 . ? 1_555 ? 
52  AC2 30 ASN B  458 ? ASN B 458 . ? 1_555 ? 
53  AC2 30 HOH CA .   ? HOH B 717 . ? 1_555 ? 
54  AC2 30 HOH CA .   ? HOH B 728 . ? 1_555 ? 
55  AC2 30 HOH CA .   ? HOH B 748 . ? 1_555 ? 
56  AC2 30 HOH CA .   ? HOH B 756 . ? 1_555 ? 
57  AC2 30 HOH CA .   ? HOH B 763 . ? 1_555 ? 
58  AC3 4  GLY B  35  ? GLY B 35  . ? 1_555 ? 
59  AC3 4  ARG B  37  ? ARG B 37  . ? 1_555 ? 
60  AC3 4  ARG D  88  ? ARG D 88  . ? 1_555 ? 
61  AC3 4  LYS D  92  ? LYS D 92  . ? 1_555 ? 
62  AC4 29 LEU C  99  ? LEU C 99  . ? 1_555 ? 
63  AC4 29 SER C  101 ? SER C 101 . ? 1_555 ? 
64  AC4 29 GLY C  102 ? GLY C 102 . ? 1_555 ? 
65  AC4 29 GLY C  103 ? GLY C 103 . ? 1_555 ? 
66  AC4 29 HIS C  104 ? HIS C 104 . ? 1_555 ? 
67  AC4 29 SER C  105 ? SER C 105 . ? 1_555 ? 
68  AC4 29 TYR C  106 ? TYR C 106 . ? 1_555 ? 
69  AC4 29 SER C  110 ? SER C 110 . ? 1_555 ? 
70  AC4 29 LEU C  122 ? LEU C 122 . ? 1_555 ? 
71  AC4 29 SER C  141 ? SER C 141 . ? 1_555 ? 
72  AC4 29 ALA C  164 ? ALA C 164 . ? 1_555 ? 
73  AC4 29 CYS C  166 ? CYS C 166 . ? 1_555 ? 
74  AC4 29 VAL C  169 ? VAL C 169 . ? 1_555 ? 
75  AC4 29 GLY C  170 ? GLY C 170 . ? 1_555 ? 
76  AC4 29 GLY C  172 ? GLY C 172 . ? 1_555 ? 
77  AC4 29 GLY C  173 ? GLY C 173 . ? 1_555 ? 
78  AC4 29 HIS C  174 ? HIS C 174 . ? 1_555 ? 
79  AC4 29 PHE C  180 ? PHE C 180 . ? 1_555 ? 
80  AC4 29 GLY C  225 ? GLY C 225 . ? 1_555 ? 
81  AC4 29 GLY C  226 ? GLY C 226 . ? 1_555 ? 
82  AC4 29 GLY C  229 ? GLY C 229 . ? 1_555 ? 
83  AC4 29 ILE C  231 ? ILE C 231 . ? 1_555 ? 
84  AC4 29 TYR C  456 ? TYR C 456 . ? 1_555 ? 
85  AC4 29 ASN C  458 ? ASN C 458 . ? 1_555 ? 
86  AC4 29 HOH DA .   ? HOH C 712 . ? 1_555 ? 
87  AC4 29 HOH DA .   ? HOH C 715 . ? 1_555 ? 
88  AC4 29 HOH DA .   ? HOH C 716 . ? 1_555 ? 
89  AC4 29 HOH DA .   ? HOH C 757 . ? 1_555 ? 
90  AC4 29 HOH DA .   ? HOH C 765 . ? 1_555 ? 
91  AC5 13 LYS A  80  ? LYS A 80  . ? 1_555 ? 
92  AC5 13 ARG A  127 ? ARG A 127 . ? 1_555 ? 
93  AC5 13 SER A  129 ? SER A 129 . ? 1_555 ? 
94  AC5 13 TRP A  138 ? TRP A 138 . ? 1_555 ? 
95  AC5 13 GLU A  140 ? GLU A 140 . ? 1_555 ? 
96  AC5 13 ILE A  206 ? ILE A 206 . ? 1_555 ? 
97  AC5 13 ASP A  208 ? ASP A 208 . ? 1_555 ? 
98  AC5 13 LYS C  80  ? LYS C 80  . ? 1_555 ? 
99  AC5 13 SER C  129 ? SER C 129 . ? 1_555 ? 
100 AC5 13 TRP C  138 ? TRP C 138 . ? 1_555 ? 
101 AC5 13 ILE C  206 ? ILE C 206 . ? 1_555 ? 
102 AC5 13 ASP C  208 ? ASP C 208 . ? 1_555 ? 
103 AC5 13 TYR C  232 ? TYR C 232 . ? 1_555 ? 
104 AC6 4  ARG A  88  ? ARG A 88  . ? 1_555 ? 
105 AC6 4  GLY C  35  ? GLY C 35  . ? 1_555 ? 
106 AC6 4  ARG C  37  ? ARG C 37  . ? 1_555 ? 
107 AC6 4  HOH DA .   ? HOH C 766 . ? 1_555 ? 
108 AC7 3  SER C  400 ? SER C 400 . ? 1_555 ? 
109 AC7 3  SER C  401 ? SER C 401 . ? 1_555 ? 
110 AC7 3  HOH DA .   ? HOH C 742 . ? 1_555 ? 
111 AC8 27 LEU D  99  ? LEU D 99  . ? 1_555 ? 
112 AC8 27 SER D  101 ? SER D 101 . ? 1_555 ? 
113 AC8 27 GLY D  102 ? GLY D 102 . ? 1_555 ? 
114 AC8 27 GLY D  103 ? GLY D 103 . ? 1_555 ? 
115 AC8 27 HIS D  104 ? HIS D 104 . ? 1_555 ? 
116 AC8 27 SER D  105 ? SER D 105 . ? 1_555 ? 
117 AC8 27 TYR D  106 ? TYR D 106 . ? 1_555 ? 
118 AC8 27 SER D  110 ? SER D 110 . ? 1_555 ? 
119 AC8 27 LEU D  122 ? LEU D 122 . ? 1_555 ? 
120 AC8 27 SER D  141 ? SER D 141 . ? 1_555 ? 
121 AC8 27 ALA D  164 ? ALA D 164 . ? 1_555 ? 
122 AC8 27 CYS D  166 ? CYS D 166 . ? 1_555 ? 
123 AC8 27 VAL D  169 ? VAL D 169 . ? 1_555 ? 
124 AC8 27 GLY D  170 ? GLY D 170 . ? 1_555 ? 
125 AC8 27 GLY D  172 ? GLY D 172 . ? 1_555 ? 
126 AC8 27 GLY D  173 ? GLY D 173 . ? 1_555 ? 
127 AC8 27 HIS D  174 ? HIS D 174 . ? 1_555 ? 
128 AC8 27 PHE D  180 ? PHE D 180 . ? 1_555 ? 
129 AC8 27 GLY D  225 ? GLY D 225 . ? 1_555 ? 
130 AC8 27 GLY D  226 ? GLY D 226 . ? 1_555 ? 
131 AC8 27 GLY D  229 ? GLY D 229 . ? 1_555 ? 
132 AC8 27 ILE D  231 ? ILE D 231 . ? 1_555 ? 
133 AC8 27 TYR D  456 ? TYR D 456 . ? 1_555 ? 
134 AC8 27 ASN D  458 ? ASN D 458 . ? 1_555 ? 
135 AC8 27 HOH EA .   ? HOH D 712 . ? 1_555 ? 
136 AC8 27 HOH EA .   ? HOH D 713 . ? 1_555 ? 
137 AC8 27 HOH EA .   ? HOH D 739 . ? 1_555 ? 
138 AC9 7  TRP B  138 ? TRP B 138 . ? 1_555 ? 
139 AC9 7  ILE B  206 ? ILE B 206 . ? 1_555 ? 
140 AC9 7  LYS D  80  ? LYS D 80  . ? 1_555 ? 
141 AC9 7  SER D  129 ? SER D 129 . ? 1_555 ? 
142 AC9 7  TRP D  138 ? TRP D 138 . ? 1_555 ? 
143 AC9 7  ILE D  206 ? ILE D 206 . ? 1_555 ? 
144 AC9 7  ASP D  208 ? ASP D 208 . ? 1_555 ? 
145 BC1 4  TYR D  187 ? TYR D 187 . ? 1_555 ? 
146 BC1 4  ASP D  192 ? ASP D 192 . ? 1_555 ? 
147 BC1 4  ASN D  193 ? ASN D 193 . ? 1_555 ? 
148 BC1 4  GLN D  395 ? GLN D 395 . ? 1_555 ? 
149 BC2 3  ARG D  209 ? ARG D 209 . ? 1_555 ? 
150 BC2 3  ARG D  221 ? ARG D 221 . ? 1_555 ? 
151 BC2 3  PHE D  403 ? PHE D 403 . ? 1_555 ? 
152 BC3 6  ASN A  38  ? ASN A 38  . ? 1_555 ? 
153 BC3 6  ARG A  52  ? ARG A 52  . ? 1_555 ? 
154 BC3 6  LEU A  56  ? LEU A 56  . ? 1_555 ? 
155 BC3 6  LEU A  76  ? LEU A 76  . ? 1_555 ? 
156 BC3 6  ASN A  124 ? ASN A 124 . ? 1_555 ? 
157 BC3 6  HOH BA .   ? HOH A 703 . ? 1_555 ? 
158 BC4 2  ASN A  471 ? ASN A 471 . ? 1_555 ? 
159 BC4 2  VAL A  474 ? VAL A 474 . ? 1_555 ? 
160 BC5 4  ASN B  38  ? ASN B 38  . ? 1_555 ? 
161 BC5 4  ARG B  52  ? ARG B 52  . ? 1_555 ? 
162 BC5 4  LEU B  76  ? LEU B 76  . ? 1_555 ? 
163 BC5 4  ASN B  124 ? ASN B 124 . ? 1_555 ? 
164 BC6 3  ASN B  471 ? ASN B 471 . ? 1_555 ? 
165 BC6 3  VAL B  474 ? VAL B 474 . ? 1_555 ? 
166 BC6 3  LYS D  158 ? LYS D 158 . ? 3_557 ? 
167 BC7 5  ASN C  38  ? ASN C 38  . ? 1_555 ? 
168 BC7 5  ARG C  52  ? ARG C 52  . ? 1_555 ? 
169 BC7 5  LEU C  56  ? LEU C 56  . ? 1_555 ? 
170 BC7 5  LEU C  76  ? LEU C 76  . ? 1_555 ? 
171 BC7 5  ASN C  124 ? ASN C 124 . ? 1_555 ? 
172 BC8 3  ASN C  471 ? ASN C 471 . ? 1_555 ? 
173 BC8 3  THR C  473 ? THR C 473 . ? 1_555 ? 
174 BC8 3  VAL C  474 ? VAL C 474 . ? 1_555 ? 
175 BC9 6  ASN D  38  ? ASN D 38  . ? 1_555 ? 
176 BC9 6  ARG D  52  ? ARG D 52  . ? 1_555 ? 
177 BC9 6  PHE D  53  ? PHE D 53  . ? 1_555 ? 
178 BC9 6  LEU D  56  ? LEU D 56  . ? 1_555 ? 
179 BC9 6  LEU D  76  ? LEU D 76  . ? 1_555 ? 
180 BC9 6  ASN D  124 ? ASN D 124 . ? 1_555 ? 
181 CC1 3  ASN D  471 ? ASN D 471 . ? 1_555 ? 
182 CC1 3  THR D  473 ? THR D 473 . ? 1_555 ? 
183 CC1 3  VAL D  474 ? VAL D 474 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4PZF 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    4PZF 
_atom_sites.fract_transf_matrix[1][1]   0.012373 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005700 
_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]   0.005107 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
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     . ASP A  1 26  ? -10.990 28.503  177.093 1.00 53.56  ? 26  ASP A N     1 
ATOM   2     C CA    . ASP A  1 26  ? -10.424 27.786  175.954 1.00 58.04  ? 26  ASP A CA    1 
ATOM   3     C C     . ASP A  1 26  ? -9.367  28.627  175.236 1.00 48.46  ? 26  ASP A C     1 
ATOM   4     O O     . ASP A  1 26  ? -9.649  29.737  174.784 1.00 44.67  ? 26  ASP A O     1 
ATOM   5     C CB    . ASP A  1 26  ? -11.527 27.383  174.977 1.00 50.46  ? 26  ASP A CB    1 
ATOM   6     C CG    . ASP A  1 26  ? -10.991 26.638  173.775 1.00 55.86  ? 26  ASP A CG    1 
ATOM   7     O OD1   . ASP A  1 26  ? -10.244 25.656  173.969 1.00 60.31  ? 26  ASP A OD1   1 
ATOM   8     O OD2   . ASP A  1 26  ? -11.308 27.039  172.636 1.00 58.66  ? 26  ASP A OD2   1 
ATOM   9     N N     . LEU A  1 27  ? -8.155  28.088  175.135 1.00 45.46  ? 27  LEU A N     1 
ATOM   10    C CA    . LEU A  1 27  ? -7.024  28.825  174.578 1.00 47.05  ? 27  LEU A CA    1 
ATOM   11    C C     . LEU A  1 27  ? -7.231  29.189  173.109 1.00 43.88  ? 27  LEU A C     1 
ATOM   12    O O     . LEU A  1 27  ? -6.974  30.322  172.703 1.00 39.78  ? 27  LEU A O     1 
ATOM   13    C CB    . LEU A  1 27  ? -5.734  28.016  174.736 1.00 47.04  ? 27  LEU A CB    1 
ATOM   14    C CG    . LEU A  1 27  ? -4.440  28.715  174.314 1.00 37.71  ? 27  LEU A CG    1 
ATOM   15    C CD1   . LEU A  1 27  ? -4.227  29.974  175.138 1.00 38.83  ? 27  LEU A CD1   1 
ATOM   16    C CD2   . LEU A  1 27  ? -3.253  27.776  174.445 1.00 43.41  ? 27  LEU A CD2   1 
ATOM   17    N N     . LEU A  1 28  ? -7.701  28.224  172.323 1.00 46.71  ? 28  LEU A N     1 
ATOM   18    C CA    . LEU A  1 28  ? -7.908  28.429  170.892 1.00 46.03  ? 28  LEU A CA    1 
ATOM   19    C C     . LEU A  1 28  ? -8.969  29.489  170.616 1.00 46.06  ? 28  LEU A C     1 
ATOM   20    O O     . LEU A  1 28  ? -8.829  30.285  169.688 1.00 47.36  ? 28  LEU A O     1 
ATOM   21    C CB    . LEU A  1 28  ? -8.292  27.115  170.206 1.00 49.64  ? 28  LEU A CB    1 
ATOM   22    C CG    . LEU A  1 28  ? -7.173  26.078  170.067 1.00 55.38  ? 28  LEU A CG    1 
ATOM   23    C CD1   . LEU A  1 28  ? -7.509  25.041  169.001 1.00 61.72  ? 28  LEU A CD1   1 
ATOM   24    C CD2   . LEU A  1 28  ? -5.843  26.754  169.760 1.00 51.70  ? 28  LEU A CD2   1 
ATOM   25    N N     . SER A  1 29  ? -10.026 29.492  171.422 1.00 41.23  ? 29  SER A N     1 
ATOM   26    C CA    . SER A  1 29  ? -11.053 30.524  171.325 1.00 44.73  ? 29  SER A CA    1 
ATOM   27    C C     . SER A  1 29  ? -10.468 31.886  171.666 1.00 34.60  ? 29  SER A C     1 
ATOM   28    O O     . SER A  1 29  ? -10.664 32.854  170.930 1.00 36.81  ? 29  SER A O     1 
ATOM   29    C CB    . SER A  1 29  ? -12.237 30.212  172.244 1.00 46.39  ? 29  SER A CB    1 
ATOM   30    O OG    . SER A  1 29  ? -13.048 29.185  171.710 1.00 59.95  ? 29  SER A OG    1 
ATOM   31    N N     . CYS A  1 30  ? -9.752  31.954  172.784 1.00 35.23  ? 30  CYS A N     1 
ATOM   32    C CA    . CYS A  1 30  ? -9.114  33.194  173.220 1.00 42.29  ? 30  CYS A CA    1 
ATOM   33    C C     . CYS A  1 30  ? -8.160  33.744  172.162 1.00 35.86  ? 30  CYS A C     1 
ATOM   34    O O     . CYS A  1 30  ? -8.228  34.922  171.809 1.00 31.91  ? 30  CYS A O     1 
ATOM   35    C CB    . CYS A  1 30  ? -8.365  32.974  174.537 1.00 40.57  ? 30  CYS A CB    1 
ATOM   36    S SG    . CYS A  1 30  ? -7.479  34.421  175.153 1.00 49.17  ? 30  CYS A SG    1 
ATOM   37    N N     . LEU A  1 31  ? -7.283  32.880  171.655 1.00 36.59  ? 31  LEU A N     1 
ATOM   38    C CA    . LEU A  1 31  ? -6.322  33.260  170.621 1.00 38.38  ? 31  LEU A CA    1 
ATOM   39    C C     . LEU A  1 31  ? -7.017  33.744  169.352 1.00 35.30  ? 31  LEU A C     1 
ATOM   40    O O     . LEU A  1 31  ? -6.640  34.770  168.786 1.00 36.07  ? 31  LEU A O     1 
ATOM   41    C CB    . LEU A  1 31  ? -5.394  32.085  170.290 1.00 32.87  ? 31  LEU A CB    1 
ATOM   42    C CG    . LEU A  1 31  ? -4.393  31.673  171.372 1.00 37.73  ? 31  LEU A CG    1 
ATOM   43    C CD1   . LEU A  1 31  ? -3.595  30.460  170.924 1.00 39.78  ? 31  LEU A CD1   1 
ATOM   44    C CD2   . LEU A  1 31  ? -3.462  32.828  171.723 1.00 31.05  ? 31  LEU A CD2   1 
ATOM   45    N N     . THR A  1 32  ? -8.032  33.004  168.914 1.00 38.26  ? 32  THR A N     1 
ATOM   46    C CA    . THR A  1 32  ? -8.797  33.365  167.721 1.00 38.40  ? 32  THR A CA    1 
ATOM   47    C C     . THR A  1 32  ? -9.475  34.727  167.869 1.00 38.59  ? 32  THR A C     1 
ATOM   48    O O     . THR A  1 32  ? -9.414  35.561  166.963 1.00 36.84  ? 32  THR A O     1 
ATOM   49    C CB    . THR A  1 32  ? -9.867  32.303  167.396 1.00 37.94  ? 32  THR A CB    1 
ATOM   50    O OG1   . THR A  1 32  ? -9.235  31.036  167.174 1.00 41.19  ? 32  THR A OG1   1 
ATOM   51    C CG2   . THR A  1 32  ? -10.654 32.696  166.154 1.00 38.88  ? 32  THR A CG2   1 
ATOM   52    N N     . PHE A  1 33  ? -10.116 34.950  169.011 1.00 35.56  ? 33  PHE A N     1 
ATOM   53    C CA    . PHE A  1 33  ? -10.766 36.226  169.280 1.00 33.38  ? 33  PHE A CA    1 
ATOM   54    C C     . PHE A  1 33  ? -9.756  37.370  169.363 1.00 39.42  ? 33  PHE A C     1 
ATOM   55    O O     . PHE A  1 33  ? -10.055 38.502  168.980 1.00 34.78  ? 33  PHE A O     1 
ATOM   56    C CB    . PHE A  1 33  ? -11.576 36.152  170.577 1.00 37.17  ? 33  PHE A CB    1 
ATOM   57    C CG    . PHE A  1 33  ? -12.982 35.655  170.390 1.00 38.58  ? 33  PHE A CG    1 
ATOM   58    C CD1   . PHE A  1 33  ? -13.878 36.360  169.606 1.00 38.43  ? 33  PHE A CD1   1 
ATOM   59    C CD2   . PHE A  1 33  ? -13.412 34.493  171.009 1.00 41.30  ? 33  PHE A CD2   1 
ATOM   60    C CE1   . PHE A  1 33  ? -15.176 35.914  169.433 1.00 42.07  ? 33  PHE A CE1   1 
ATOM   61    C CE2   . PHE A  1 33  ? -14.710 34.039  170.843 1.00 47.70  ? 33  PHE A CE2   1 
ATOM   62    C CZ    . PHE A  1 33  ? -15.592 34.753  170.053 1.00 40.36  ? 33  PHE A CZ    1 
ATOM   63    N N     . ASN A  1 34  ? -8.560  37.069  169.863 1.00 32.69  ? 34  ASN A N     1 
ATOM   64    C CA    . ASN A  1 34  ? -7.531  38.088  170.053 1.00 37.33  ? 34  ASN A CA    1 
ATOM   65    C C     . ASN A  1 34  ? -6.686  38.328  168.806 1.00 31.67  ? 34  ASN A C     1 
ATOM   66    O O     . ASN A  1 34  ? -5.733  39.105  168.834 1.00 37.32  ? 34  ASN A O     1 
ATOM   67    C CB    . ASN A  1 34  ? -6.622  37.712  171.226 1.00 34.84  ? 34  ASN A CB    1 
ATOM   68    C CG    . ASN A  1 34  ? -7.185  38.152  172.566 1.00 36.19  ? 34  ASN A CG    1 
ATOM   69    O OD1   . ASN A  1 34  ? -6.817  39.202  173.094 1.00 37.38  ? 34  ASN A OD1   1 
ATOM   70    N ND2   . ASN A  1 34  ? -8.091  37.353  173.119 1.00 35.54  ? 34  ASN A ND2   1 
ATOM   71    N N     . GLY A  1 35  ? -7.039  37.660  167.714 1.00 33.04  ? 35  GLY A N     1 
ATOM   72    C CA    . GLY A  1 35  ? -6.363  37.871  166.446 1.00 38.77  ? 35  GLY A CA    1 
ATOM   73    C C     . GLY A  1 35  ? -4.964  37.283  166.360 1.00 34.49  ? 35  GLY A C     1 
ATOM   74    O O     . GLY A  1 35  ? -4.094  37.826  165.679 1.00 37.33  ? 35  GLY A O     1 
ATOM   75    N N     . VAL A  1 36  ? -4.743  36.173  167.055 1.00 32.45  ? 36  VAL A N     1 
ATOM   76    C CA    . VAL A  1 36  ? -3.480  35.451  166.962 1.00 39.32  ? 36  VAL A CA    1 
ATOM   77    C C     . VAL A  1 36  ? -3.704  34.150  166.197 1.00 39.34  ? 36  VAL A C     1 
ATOM   78    O O     . VAL A  1 36  ? -4.076  33.139  166.787 1.00 37.27  ? 36  VAL A O     1 
ATOM   79    C CB    . VAL A  1 36  ? -2.895  35.144  168.355 1.00 33.87  ? 36  VAL A CB    1 
ATOM   80    C CG1   . VAL A  1 36  ? -1.540  34.467  168.229 1.00 27.66  ? 36  VAL A CG1   1 
ATOM   81    C CG2   . VAL A  1 36  ? -2.788  36.423  169.183 1.00 28.51  ? 36  VAL A CG2   1 
ATOM   82    N N     . ARG A  1 37  ? -3.481  34.179  164.885 1.00 37.78  ? 37  ARG A N     1 
ATOM   83    C CA    . ARG A  1 37  ? -3.869  33.060  164.026 1.00 41.22  ? 37  ARG A CA    1 
ATOM   84    C C     . ARG A  1 37  ? -2.797  31.974  163.863 1.00 43.64  ? 37  ARG A C     1 
ATOM   85    O O     . ARG A  1 37  ? -3.134  30.813  163.626 1.00 43.81  ? 37  ARG A O     1 
ATOM   86    C CB    . ARG A  1 37  ? -4.278  33.567  162.639 1.00 43.96  ? 37  ARG A CB    1 
ATOM   87    C CG    . ARG A  1 37  ? -5.465  34.531  162.624 1.00 48.54  ? 37  ARG A CG    1 
ATOM   88    C CD    . ARG A  1 37  ? -6.570  34.121  163.599 1.00 55.24  ? 37  ARG A CD    1 
ATOM   89    N NE    . ARG A  1 37  ? -7.156  32.817  163.295 1.00 74.60  ? 37  ARG A NE    1 
ATOM   90    C CZ    . ARG A  1 37  ? -8.345  32.639  162.728 1.00 75.71  ? 37  ARG A CZ    1 
ATOM   91    N NH1   . ARG A  1 37  ? -8.795  31.412  162.501 1.00 79.31  ? 37  ARG A NH1   1 
ATOM   92    N NH2   . ARG A  1 37  ? -9.088  33.684  162.389 1.00 72.43  ? 37  ARG A NH2   1 
ATOM   93    N N     . ASN A  1 38  ? -1.518  32.330  163.973 1.00 42.20  ? 38  ASN A N     1 
ATOM   94    C CA    . ASN A  1 38  ? -0.458  31.343  163.762 1.00 47.62  ? 38  ASN A CA    1 
ATOM   95    C C     . ASN A  1 38  ? -0.161  30.546  165.031 1.00 44.03  ? 38  ASN A C     1 
ATOM   96    O O     . ASN A  1 38  ? 0.704   30.915  165.829 1.00 39.71  ? 38  ASN A O     1 
ATOM   97    C CB    . ASN A  1 38  ? 0.823   32.012  163.245 1.00 40.62  ? 38  ASN A CB    1 
ATOM   98    C CG    . ASN A  1 38  ? 1.797   31.012  162.612 1.00 45.75  ? 38  ASN A CG    1 
ATOM   99    O OD1   . ASN A  1 38  ? 1.982   29.903  163.117 1.00 48.49  ? 38  ASN A OD1   1 
ATOM   100   N ND2   . ASN A  1 38  ? 2.412   31.400  161.495 1.00 47.71  ? 38  ASN A ND2   1 
ATOM   101   N N     . HIS A  1 39  ? -0.881  29.443  165.197 1.00 38.97  ? 39  HIS A N     1 
ATOM   102   C CA    . HIS A  1 39  ? -0.705  28.559  166.341 1.00 40.19  ? 39  HIS A CA    1 
ATOM   103   C C     . HIS A  1 39  ? -0.959  27.111  165.932 1.00 45.94  ? 39  HIS A C     1 
ATOM   104   O O     . HIS A  1 39  ? -1.749  26.847  165.026 1.00 50.87  ? 39  HIS A O     1 
ATOM   105   C CB    . HIS A  1 39  ? -1.643  28.969  167.476 1.00 41.28  ? 39  HIS A CB    1 
ATOM   106   C CG    . HIS A  1 39  ? -3.072  29.105  167.051 1.00 47.67  ? 39  HIS A CG    1 
ATOM   107   N ND1   . HIS A  1 39  ? -3.959  28.052  167.072 1.00 50.93  ? 39  HIS A ND1   1 
ATOM   108   C CD2   . HIS A  1 39  ? -3.763  30.169  166.577 1.00 46.73  ? 39  HIS A CD2   1 
ATOM   109   C CE1   . HIS A  1 39  ? -5.139  28.462  166.640 1.00 54.23  ? 39  HIS A CE1   1 
ATOM   110   N NE2   . HIS A  1 39  ? -5.045  29.743  166.331 1.00 49.09  ? 39  HIS A NE2   1 
ATOM   111   N N     . THR A  1 40  ? -0.274  26.175  166.586 1.00 43.08  ? 40  THR A N     1 
ATOM   112   C CA    . THR A  1 40  ? -0.489  24.747  166.349 1.00 44.10  ? 40  THR A CA    1 
ATOM   113   C C     . THR A  1 40  ? -0.541  23.991  167.675 1.00 43.88  ? 40  THR A C     1 
ATOM   114   O O     . THR A  1 40  ? 0.291   24.215  168.553 1.00 43.52  ? 40  THR A O     1 
ATOM   115   C CB    . THR A  1 40  ? 0.624   24.121  165.474 1.00 46.09  ? 40  THR A CB    1 
ATOM   116   O OG1   . THR A  1 40  ? 1.807   23.931  166.262 1.00 55.05  ? 40  THR A OG1   1 
ATOM   117   C CG2   . THR A  1 40  ? 0.948   25.000  164.274 1.00 49.42  ? 40  THR A CG2   1 
ATOM   118   N N     . VAL A  1 41  ? -1.511  23.092  167.818 1.00 40.14  ? 41  VAL A N     1 
ATOM   119   C CA    . VAL A  1 41  ? -1.630  22.281  169.030 1.00 37.18  ? 41  VAL A CA    1 
ATOM   120   C C     . VAL A  1 41  ? -0.720  21.053  168.969 1.00 45.45  ? 41  VAL A C     1 
ATOM   121   O O     . VAL A  1 41  ? -0.218  20.700  167.900 1.00 43.63  ? 41  VAL A O     1 
ATOM   122   C CB    . VAL A  1 41  ? -3.079  21.820  169.261 1.00 44.38  ? 41  VAL A CB    1 
ATOM   123   C CG1   . VAL A  1 41  ? -4.007  23.024  169.391 1.00 42.82  ? 41  VAL A CG1   1 
ATOM   124   C CG2   . VAL A  1 41  ? -3.531  20.909  168.132 1.00 37.06  ? 41  VAL A CG2   1 
ATOM   125   N N     . PHE A  1 42  ? -0.511  20.411  170.118 1.00 43.29  ? 42  PHE A N     1 
ATOM   126   C CA    . PHE A  1 42  ? 0.345   19.227  170.197 1.00 47.49  ? 42  PHE A CA    1 
ATOM   127   C C     . PHE A  1 42  ? -0.091  18.144  169.215 1.00 50.96  ? 42  PHE A C     1 
ATOM   128   O O     . PHE A  1 42  ? -1.280  17.966  168.954 1.00 46.93  ? 42  PHE A O     1 
ATOM   129   C CB    . PHE A  1 42  ? 0.353   18.652  171.621 1.00 45.67  ? 42  PHE A CB    1 
ATOM   130   C CG    . PHE A  1 42  ? 1.177   17.394  171.764 1.00 49.59  ? 42  PHE A CG    1 
ATOM   131   C CD1   . PHE A  1 42  ? 2.504   17.460  172.156 1.00 49.48  ? 42  PHE A CD1   1 
ATOM   132   C CD2   . PHE A  1 42  ? 0.626   16.147  171.503 1.00 56.02  ? 42  PHE A CD2   1 
ATOM   133   C CE1   . PHE A  1 42  ? 3.263   16.310  172.281 1.00 58.58  ? 42  PHE A CE1   1 
ATOM   134   C CE2   . PHE A  1 42  ? 1.381   15.002  171.617 1.00 52.74  ? 42  PHE A CE2   1 
ATOM   135   C CZ    . PHE A  1 42  ? 2.699   15.080  172.014 1.00 59.42  ? 42  PHE A CZ    1 
ATOM   136   N N     . SER A  1 43  ? 0.886   17.423  168.681 1.00 45.29  ? 43  SER A N     1 
ATOM   137   C CA    . SER A  1 43  ? 0.629   16.247  167.863 1.00 46.66  ? 43  SER A CA    1 
ATOM   138   C C     . SER A  1 43  ? 1.812   15.291  167.971 1.00 52.64  ? 43  SER A C     1 
ATOM   139   O O     . SER A  1 43  ? 2.964   15.716  167.899 1.00 51.60  ? 43  SER A O     1 
ATOM   140   C CB    . SER A  1 43  ? 0.377   16.642  166.408 1.00 50.44  ? 43  SER A CB    1 
ATOM   141   O OG    . SER A  1 43  ? 0.522   15.528  165.544 1.00 56.59  ? 43  SER A OG    1 
ATOM   142   N N     . ALA A  1 44  ? 1.528   14.005  168.160 1.00 57.07  ? 44  ALA A N     1 
ATOM   143   C CA    . ALA A  1 44  ? 2.587   13.006  168.280 1.00 59.95  ? 44  ALA A CA    1 
ATOM   144   C C     . ALA A  1 44  ? 3.119   12.616  166.904 1.00 57.58  ? 44  ALA A C     1 
ATOM   145   O O     . ALA A  1 44  ? 4.136   11.929  166.790 1.00 63.32  ? 44  ALA A O     1 
ATOM   146   C CB    . ALA A  1 44  ? 2.085   11.779  169.029 1.00 56.07  ? 44  ALA A CB    1 
ATOM   147   N N     . ASP A  1 45  ? 2.418   13.060  165.865 1.00 60.87  ? 45  ASP A N     1 
ATOM   148   C CA    . ASP A  1 45  ? 2.819   12.806  164.486 1.00 58.06  ? 45  ASP A CA    1 
ATOM   149   C C     . ASP A  1 45  ? 4.114   13.548  164.155 1.00 62.09  ? 45  ASP A C     1 
ATOM   150   O O     . ASP A  1 45  ? 4.147   14.778  164.141 1.00 61.19  ? 45  ASP A O     1 
ATOM   151   C CB    . ASP A  1 45  ? 1.697   13.220  163.526 1.00 60.82  ? 45  ASP A CB    1 
ATOM   152   C CG    . ASP A  1 45  ? 1.972   12.826  162.084 1.00 63.82  ? 45  ASP A CG    1 
ATOM   153   O OD1   . ASP A  1 45  ? 3.013   12.192  161.815 1.00 69.20  ? 45  ASP A OD1   1 
ATOM   154   O OD2   . ASP A  1 45  ? 1.129   13.142  161.218 1.00 67.05  ? 45  ASP A OD2   1 
ATOM   155   N N     . SER A  1 46  ? 5.173   12.787  163.886 1.00 62.97  ? 46  SER A N     1 
ATOM   156   C CA    . SER A  1 46  ? 6.481   13.352  163.561 1.00 62.05  ? 46  SER A CA    1 
ATOM   157   C C     . SER A  1 46  ? 6.445   14.261  162.331 1.00 61.66  ? 46  SER A C     1 
ATOM   158   O O     . SER A  1 46  ? 7.324   15.103  162.150 1.00 64.03  ? 46  SER A O     1 
ATOM   159   C CB    . SER A  1 46  ? 7.503   12.233  163.336 1.00 67.54  ? 46  SER A CB    1 
ATOM   160   O OG    . SER A  1 46  ? 7.811   11.561  164.547 1.00 76.16  ? 46  SER A OG    1 
ATOM   161   N N     . ASP A  1 47  ? 5.427   14.093  161.493 1.00 62.49  ? 47  ASP A N     1 
ATOM   162   C CA    . ASP A  1 47  ? 5.326   14.856  160.252 1.00 65.96  ? 47  ASP A CA    1 
ATOM   163   C C     . ASP A  1 47  ? 4.439   16.094  160.378 1.00 65.75  ? 47  ASP A C     1 
ATOM   164   O O     . ASP A  1 47  ? 4.273   16.842  159.415 1.00 63.58  ? 47  ASP A O     1 
ATOM   165   C CB    . ASP A  1 47  ? 4.805   13.962  159.127 1.00 74.90  ? 47  ASP A CB    1 
ATOM   166   C CG    . ASP A  1 47  ? 5.712   12.780  158.861 1.00 96.63  ? 47  ASP A CG    1 
ATOM   167   O OD1   . ASP A  1 47  ? 6.891   12.836  159.267 1.00 91.57  ? 47  ASP A OD1   1 
ATOM   168   O OD2   . ASP A  1 47  ? 5.246   11.795  158.251 1.00 100.53 ? 47  ASP A OD2   1 
ATOM   169   N N     . SER A  1 48  ? 3.871   16.306  161.560 1.00 61.42  ? 48  SER A N     1 
ATOM   170   C CA    . SER A  1 48  ? 2.990   17.445  161.785 1.00 59.19  ? 48  SER A CA    1 
ATOM   171   C C     . SER A  1 48  ? 3.751   18.767  161.760 1.00 55.40  ? 48  SER A C     1 
ATOM   172   O O     . SER A  1 48  ? 4.957   18.804  162.007 1.00 54.27  ? 48  SER A O     1 
ATOM   173   C CB    . SER A  1 48  ? 2.259   17.292  163.119 1.00 58.39  ? 48  SER A CB    1 
ATOM   174   O OG    . SER A  1 48  ? 3.177   17.158  164.191 1.00 54.87  ? 48  SER A OG    1 
ATOM   175   N N     . ASP A  1 49  ? 3.037   19.847  161.449 1.00 54.77  ? 49  ASP A N     1 
ATOM   176   C CA    . ASP A  1 49  ? 3.593   21.195  161.522 1.00 51.43  ? 49  ASP A CA    1 
ATOM   177   C C     . ASP A  1 49  ? 4.077   21.488  162.937 1.00 51.93  ? 49  ASP A C     1 
ATOM   178   O O     . ASP A  1 49  ? 5.071   22.191  163.136 1.00 49.77  ? 49  ASP A O     1 
ATOM   179   C CB    . ASP A  1 49  ? 2.555   22.237  161.099 1.00 57.19  ? 49  ASP A CB    1 
ATOM   180   C CG    . ASP A  1 49  ? 2.500   22.435  159.597 1.00 64.01  ? 49  ASP A CG    1 
ATOM   181   O OD1   . ASP A  1 49  ? 3.163   21.669  158.866 1.00 65.91  ? 49  ASP A OD1   1 
ATOM   182   O OD2   . ASP A  1 49  ? 1.789   23.357  159.149 1.00 71.99  ? 49  ASP A OD2   1 
ATOM   183   N N     . PHE A  1 50  ? 3.359   20.942  163.914 1.00 47.58  ? 50  PHE A N     1 
ATOM   184   C CA    . PHE A  1 50  ? 3.715   21.103  165.317 1.00 47.79  ? 50  PHE A CA    1 
ATOM   185   C C     . PHE A  1 50  ? 5.118   20.592  165.611 1.00 49.21  ? 50  PHE A C     1 
ATOM   186   O O     . PHE A  1 50  ? 5.942   21.316  166.162 1.00 43.45  ? 50  PHE A O     1 
ATOM   187   C CB    . PHE A  1 50  ? 2.715   20.376  166.216 1.00 41.66  ? 50  PHE A CB    1 
ATOM   188   C CG    . PHE A  1 50  ? 3.123   20.334  167.665 1.00 41.18  ? 50  PHE A CG    1 
ATOM   189   C CD1   . PHE A  1 50  ? 2.870   21.409  168.499 1.00 42.43  ? 50  PHE A CD1   1 
ATOM   190   C CD2   . PHE A  1 50  ? 3.761   19.220  168.191 1.00 40.83  ? 50  PHE A CD2   1 
ATOM   191   C CE1   . PHE A  1 50  ? 3.243   21.376  169.831 1.00 40.01  ? 50  PHE A CE1   1 
ATOM   192   C CE2   . PHE A  1 50  ? 4.139   19.182  169.521 1.00 38.36  ? 50  PHE A CE2   1 
ATOM   193   C CZ    . PHE A  1 50  ? 3.878   20.260  170.342 1.00 35.52  ? 50  PHE A CZ    1 
ATOM   194   N N     . ASN A  1 51  ? 5.375   19.336  165.259 1.00 45.64  ? 51  ASN A N     1 
ATOM   195   C CA    . ASN A  1 51  ? 6.656   18.709  165.555 1.00 47.14  ? 51  ASN A CA    1 
ATOM   196   C C     . ASN A  1 51  ? 7.808   19.389  164.824 1.00 47.61  ? 51  ASN A C     1 
ATOM   197   O O     . ASN A  1 51  ? 8.921   19.469  165.343 1.00 44.58  ? 51  ASN A O     1 
ATOM   198   C CB    . ASN A  1 51  ? 6.613   17.220  165.205 1.00 50.58  ? 51  ASN A CB    1 
ATOM   199   C CG    . ASN A  1 51  ? 7.915   16.513  165.520 1.00 53.65  ? 51  ASN A CG    1 
ATOM   200   O OD1   . ASN A  1 51  ? 8.162   16.124  166.662 1.00 55.13  ? 51  ASN A OD1   1 
ATOM   201   N ND2   . ASN A  1 51  ? 8.756   16.341  164.508 1.00 50.55  ? 51  ASN A ND2   1 
ATOM   202   N N     . ARG A  1 52  ? 7.534   19.884  163.623 1.00 46.45  ? 52  ARG A N     1 
ATOM   203   C CA    . ARG A  1 52  ? 8.544   20.577  162.833 1.00 46.50  ? 52  ARG A CA    1 
ATOM   204   C C     . ARG A  1 52  ? 8.915   21.915  163.470 1.00 49.86  ? 52  ARG A C     1 
ATOM   205   O O     . ARG A  1 52  ? 10.096  22.229  163.638 1.00 45.73  ? 52  ARG A O     1 
ATOM   206   C CB    . ARG A  1 52  ? 8.047   20.790  161.401 1.00 51.88  ? 52  ARG A CB    1 
ATOM   207   C CG    . ARG A  1 52  ? 9.079   21.396  160.465 1.00 55.75  ? 52  ARG A CG    1 
ATOM   208   C CD    . ARG A  1 52  ? 8.626   21.314  159.018 1.00 61.11  ? 52  ARG A CD    1 
ATOM   209   N NE    . ARG A  1 52  ? 7.300   21.898  158.835 1.00 65.93  ? 52  ARG A NE    1 
ATOM   210   C CZ    . ARG A  1 52  ? 7.075   23.181  158.566 1.00 66.63  ? 52  ARG A CZ    1 
ATOM   211   N NH1   . ARG A  1 52  ? 8.089   24.030  158.442 1.00 61.58  ? 52  ARG A NH1   1 
ATOM   212   N NH2   . ARG A  1 52  ? 5.831   23.616  158.422 1.00 65.67  ? 52  ARG A NH2   1 
ATOM   213   N N     . PHE A  1 53  ? 7.897   22.694  163.827 1.00 43.26  ? 53  PHE A N     1 
ATOM   214   C CA    . PHE A  1 53  ? 8.099   23.976  164.495 1.00 40.80  ? 53  PHE A CA    1 
ATOM   215   C C     . PHE A  1 53  ? 8.814   23.791  165.825 1.00 42.99  ? 53  PHE A C     1 
ATOM   216   O O     . PHE A  1 53  ? 9.709   24.562  166.173 1.00 38.37  ? 53  PHE A O     1 
ATOM   217   C CB    . PHE A  1 53  ? 6.761   24.687  164.717 1.00 47.71  ? 53  PHE A CB    1 
ATOM   218   C CG    . PHE A  1 53  ? 6.190   25.305  163.476 1.00 48.78  ? 53  PHE A CG    1 
ATOM   219   C CD1   . PHE A  1 53  ? 7.024   25.815  162.494 1.00 54.32  ? 53  PHE A CD1   1 
ATOM   220   C CD2   . PHE A  1 53  ? 4.821   25.382  163.294 1.00 55.50  ? 53  PHE A CD2   1 
ATOM   221   C CE1   . PHE A  1 53  ? 6.502   26.390  161.354 1.00 56.74  ? 53  PHE A CE1   1 
ATOM   222   C CE2   . PHE A  1 53  ? 4.290   25.955  162.155 1.00 57.11  ? 53  PHE A CE2   1 
ATOM   223   C CZ    . PHE A  1 53  ? 5.133   26.458  161.183 1.00 58.56  ? 53  PHE A CZ    1 
ATOM   224   N N     . LEU A  1 54  ? 8.413   22.758  166.562 1.00 38.94  ? 54  LEU A N     1 
ATOM   225   C CA    . LEU A  1 54  ? 9.017   22.454  167.856 1.00 44.57  ? 54  LEU A CA    1 
ATOM   226   C C     . LEU A  1 54  ? 10.515  22.200  167.744 1.00 41.52  ? 54  LEU A C     1 
ATOM   227   O O     . LEU A  1 54  ? 11.288  22.667  168.576 1.00 43.32  ? 54  LEU A O     1 
ATOM   228   C CB    . LEU A  1 54  ? 8.336   21.240  168.499 1.00 39.48  ? 54  LEU A CB    1 
ATOM   229   C CG    . LEU A  1 54  ? 9.002   20.677  169.761 1.00 41.41  ? 54  LEU A CG    1 
ATOM   230   C CD1   . LEU A  1 54  ? 9.071   21.731  170.857 1.00 37.68  ? 54  LEU A CD1   1 
ATOM   231   C CD2   . LEU A  1 54  ? 8.295   19.416  170.266 1.00 41.77  ? 54  LEU A CD2   1 
ATOM   232   N N     . HIS A  1 55  ? 10.917  21.465  166.712 1.00 37.31  ? 55  HIS A N     1 
ATOM   233   C CA    . HIS A  1 55  ? 12.303  21.029  166.574 1.00 44.11  ? 55  HIS A CA    1 
ATOM   234   C C     . HIS A  1 55  ? 13.149  21.987  165.742 1.00 43.08  ? 55  HIS A C     1 
ATOM   235   O O     . HIS A  1 55  ? 14.377  21.930  165.778 1.00 40.16  ? 55  HIS A O     1 
ATOM   236   C CB    . HIS A  1 55  ? 12.356  19.632  165.955 1.00 37.95  ? 55  HIS A CB    1 
ATOM   237   C CG    . HIS A  1 55  ? 12.037  18.537  166.921 1.00 44.79  ? 55  HIS A CG    1 
ATOM   238   N ND1   . HIS A  1 55  ? 10.827  17.875  166.928 1.00 50.33  ? 55  HIS A ND1   1 
ATOM   239   C CD2   . HIS A  1 55  ? 12.764  18.000  167.928 1.00 47.89  ? 55  HIS A CD2   1 
ATOM   240   C CE1   . HIS A  1 55  ? 10.828  16.972  167.891 1.00 52.27  ? 55  HIS A CE1   1 
ATOM   241   N NE2   . HIS A  1 55  ? 11.992  17.027  168.514 1.00 52.44  ? 55  HIS A NE2   1 
ATOM   242   N N     . LEU A  1 56  ? 12.485  22.870  165.006 1.00 41.08  ? 56  LEU A N     1 
ATOM   243   C CA    . LEU A  1 56  ? 13.158  23.810  164.119 1.00 40.88  ? 56  LEU A CA    1 
ATOM   244   C C     . LEU A  1 56  ? 14.205  24.654  164.850 1.00 47.35  ? 56  LEU A C     1 
ATOM   245   O O     . LEU A  1 56  ? 15.242  25.003  164.285 1.00 46.57  ? 56  LEU A O     1 
ATOM   246   C CB    . LEU A  1 56  ? 12.123  24.715  163.457 1.00 49.53  ? 56  LEU A CB    1 
ATOM   247   C CG    . LEU A  1 56  ? 12.414  25.253  162.057 1.00 54.43  ? 56  LEU A CG    1 
ATOM   248   C CD1   . LEU A  1 56  ? 13.032  24.179  161.184 1.00 54.32  ? 56  LEU A CD1   1 
ATOM   249   C CD2   . LEU A  1 56  ? 11.121  25.746  161.452 1.00 49.96  ? 56  LEU A CD2   1 
ATOM   250   N N     . SER A  1 57  ? 13.934  24.965  166.114 1.00 43.14  ? 57  SER A N     1 
ATOM   251   C CA    . SER A  1 57  ? 14.824  25.820  166.887 1.00 43.21  ? 57  SER A CA    1 
ATOM   252   C C     . SER A  1 57  ? 15.353  25.148  168.152 1.00 44.60  ? 57  SER A C     1 
ATOM   253   O O     . SER A  1 57  ? 15.744  25.828  169.100 1.00 48.52  ? 57  SER A O     1 
ATOM   254   C CB    . SER A  1 57  ? 14.113  27.125  167.251 1.00 39.62  ? 57  SER A CB    1 
ATOM   255   O OG    . SER A  1 57  ? 13.820  27.887  166.093 1.00 44.33  ? 57  SER A OG    1 
ATOM   256   N N     . ILE A  1 58  ? 15.360  23.819  168.177 1.00 45.04  ? 58  ILE A N     1 
ATOM   257   C CA    . ILE A  1 58  ? 16.058  23.110  169.242 1.00 41.22  ? 58  ILE A CA    1 
ATOM   258   C C     . ILE A  1 58  ? 17.521  22.979  168.837 1.00 46.60  ? 58  ILE A C     1 
ATOM   259   O O     . ILE A  1 58  ? 17.850  22.267  167.888 1.00 52.90  ? 58  ILE A O     1 
ATOM   260   C CB    . ILE A  1 58  ? 15.450  21.719  169.522 1.00 41.57  ? 58  ILE A CB    1 
ATOM   261   C CG1   . ILE A  1 58  ? 13.996  21.855  169.974 1.00 41.38  ? 58  ILE A CG1   1 
ATOM   262   C CG2   . ILE A  1 58  ? 16.252  20.996  170.593 1.00 42.31  ? 58  ILE A CG2   1 
ATOM   263   C CD1   . ILE A  1 58  ? 13.346  20.545  170.364 1.00 39.65  ? 58  ILE A CD1   1 
ATOM   264   N N     . GLN A  1 59  ? 18.393  23.686  169.548 1.00 41.63  ? 59  GLN A N     1 
ATOM   265   C CA    . GLN A  1 59  ? 19.794  23.782  169.152 1.00 46.25  ? 59  GLN A CA    1 
ATOM   266   C C     . GLN A  1 59  ? 20.688  22.883  169.999 1.00 46.11  ? 59  GLN A C     1 
ATOM   267   O O     . GLN A  1 59  ? 21.893  22.785  169.762 1.00 47.63  ? 59  GLN A O     1 
ATOM   268   C CB    . GLN A  1 59  ? 20.266  25.234  169.235 1.00 40.60  ? 59  GLN A CB    1 
ATOM   269   C CG    . GLN A  1 59  ? 19.393  26.221  168.457 1.00 40.75  ? 59  GLN A CG    1 
ATOM   270   C CD    . GLN A  1 59  ? 19.511  26.073  166.947 1.00 45.82  ? 59  GLN A CD    1 
ATOM   271   O OE1   . GLN A  1 59  ? 20.238  25.215  166.444 1.00 48.38  ? 59  GLN A OE1   1 
ATOM   272   N NE2   . GLN A  1 59  ? 18.793  26.917  166.216 1.00 45.32  ? 59  GLN A NE2   1 
ATOM   273   N N     . ASN A  1 60  ? 20.090  22.235  170.992 1.00 46.47  ? 60  ASN A N     1 
ATOM   274   C CA    . ASN A  1 60  ? 20.784  21.213  171.766 1.00 49.31  ? 60  ASN A CA    1 
ATOM   275   C C     . ASN A  1 60  ? 19.974  19.922  171.771 1.00 51.32  ? 60  ASN A C     1 
ATOM   276   O O     . ASN A  1 60  ? 19.087  19.747  172.606 1.00 44.66  ? 60  ASN A O     1 
ATOM   277   C CB    . ASN A  1 60  ? 21.041  21.684  173.201 1.00 44.76  ? 60  ASN A CB    1 
ATOM   278   C CG    . ASN A  1 60  ? 21.993  20.766  173.959 1.00 46.00  ? 60  ASN A CG    1 
ATOM   279   O OD1   . ASN A  1 60  ? 22.348  19.688  173.482 1.00 48.69  ? 60  ASN A OD1   1 
ATOM   280   N ND2   . ASN A  1 60  ? 22.405  21.192  175.148 1.00 43.41  ? 60  ASN A ND2   1 
ATOM   281   N N     . PRO A  1 61  ? 20.284  19.010  170.833 1.00 53.40  ? 61  PRO A N     1 
ATOM   282   C CA    . PRO A  1 61  ? 19.635  17.702  170.678 1.00 55.56  ? 61  PRO A CA    1 
ATOM   283   C C     . PRO A  1 61  ? 19.562  16.879  171.971 1.00 56.78  ? 61  PRO A C     1 
ATOM   284   O O     . PRO A  1 61  ? 18.855  15.872  172.003 1.00 58.50  ? 61  PRO A O     1 
ATOM   285   C CB    . PRO A  1 61  ? 20.516  17.008  169.637 1.00 57.04  ? 61  PRO A CB    1 
ATOM   286   C CG    . PRO A  1 61  ? 21.014  18.132  168.793 1.00 58.77  ? 61  PRO A CG    1 
ATOM   287   C CD    . PRO A  1 61  ? 21.247  19.274  169.747 1.00 50.88  ? 61  PRO A CD    1 
ATOM   288   N N     . LEU A  1 62  ? 20.271  17.304  173.015 1.00 53.19  ? 62  LEU A N     1 
ATOM   289   C CA    . LEU A  1 62  ? 20.162  16.672  174.328 1.00 49.86  ? 62  LEU A CA    1 
ATOM   290   C C     . LEU A  1 62  ? 18.721  16.739  174.846 1.00 52.59  ? 62  LEU A C     1 
ATOM   291   O O     . LEU A  1 62  ? 18.332  15.967  175.721 1.00 57.34  ? 62  LEU A O     1 
ATOM   292   C CB    . LEU A  1 62  ? 21.120  17.333  175.332 1.00 48.09  ? 62  LEU A CB    1 
ATOM   293   C CG    . LEU A  1 62  ? 21.199  16.766  176.756 1.00 50.05  ? 62  LEU A CG    1 
ATOM   294   C CD1   . LEU A  1 62  ? 21.623  15.306  176.723 1.00 53.16  ? 62  LEU A CD1   1 
ATOM   295   C CD2   . LEU A  1 62  ? 22.138  17.574  177.643 1.00 48.22  ? 62  LEU A CD2   1 
ATOM   296   N N     . PHE A  1 63  ? 17.928  17.651  174.289 1.00 56.79  ? 63  PHE A N     1 
ATOM   297   C CA    . PHE A  1 63  ? 16.562  17.864  174.755 1.00 54.73  ? 63  PHE A CA    1 
ATOM   298   C C     . PHE A  1 63  ? 15.483  17.613  173.697 1.00 57.97  ? 63  PHE A C     1 
ATOM   299   O O     . PHE A  1 63  ? 14.364  18.101  173.833 1.00 58.31  ? 63  PHE A O     1 
ATOM   300   C CB    . PHE A  1 63  ? 16.416  19.291  175.289 1.00 49.48  ? 63  PHE A CB    1 
ATOM   301   C CG    . PHE A  1 63  ? 17.332  19.602  176.431 1.00 49.78  ? 63  PHE A CG    1 
ATOM   302   C CD1   . PHE A  1 63  ? 17.027  19.177  177.712 1.00 47.06  ? 63  PHE A CD1   1 
ATOM   303   C CD2   . PHE A  1 63  ? 18.501  20.315  176.225 1.00 45.19  ? 63  PHE A CD2   1 
ATOM   304   C CE1   . PHE A  1 63  ? 17.872  19.459  178.769 1.00 43.59  ? 63  PHE A CE1   1 
ATOM   305   C CE2   . PHE A  1 63  ? 19.348  20.602  177.276 1.00 45.99  ? 63  PHE A CE2   1 
ATOM   306   C CZ    . PHE A  1 63  ? 19.033  20.174  178.550 1.00 46.17  ? 63  PHE A CZ    1 
ATOM   307   N N     . GLN A  1 64  ? 15.803  16.843  172.662 1.00 62.41  ? 64  GLN A N     1 
ATOM   308   C CA    . GLN A  1 64  ? 14.872  16.633  171.548 1.00 70.15  ? 64  GLN A CA    1 
ATOM   309   C C     . GLN A  1 64  ? 14.032  15.358  171.687 1.00 78.86  ? 64  GLN A C     1 
ATOM   310   O O     . GLN A  1 64  ? 12.899  15.293  171.194 1.00 77.04  ? 64  GLN A O     1 
ATOM   311   C CB    . GLN A  1 64  ? 15.641  16.588  170.222 1.00 66.95  ? 64  GLN A CB    1 
ATOM   312   C CG    . GLN A  1 64  ? 16.493  15.326  170.055 1.00 75.87  ? 64  GLN A CG    1 
ATOM   313   C CD    . GLN A  1 64  ? 17.377  15.336  168.819 1.00 78.02  ? 64  GLN A CD    1 
ATOM   314   O OE1   . GLN A  1 64  ? 17.342  16.269  168.018 1.00 77.05  ? 64  GLN A OE1   1 
ATOM   315   N NE2   . GLN A  1 64  ? 18.180  14.288  168.663 1.00 78.72  ? 64  GLN A NE2   1 
ATOM   316   N N     . ASN A  1 65  ? 14.587  14.365  172.377 1.00 81.83  ? 65  ASN A N     1 
ATOM   317   C CA    . ASN A  1 65  ? 14.082  12.990  172.371 1.00 84.20  ? 65  ASN A CA    1 
ATOM   318   C C     . ASN A  1 65  ? 12.631  12.817  172.833 1.00 87.51  ? 65  ASN A C     1 
ATOM   319   O O     . ASN A  1 65  ? 12.044  13.735  173.406 1.00 85.37  ? 65  ASN A O     1 
ATOM   320   C CB    . ASN A  1 65  ? 15.006  12.130  173.234 1.00 83.31  ? 65  ASN A CB    1 
ATOM   321   C CG    . ASN A  1 65  ? 16.477  12.425  172.981 1.00 91.47  ? 65  ASN A CG    1 
ATOM   322   O OD1   . ASN A  1 65  ? 17.038  13.372  173.537 1.00 89.07  ? 65  ASN A OD1   1 
ATOM   323   N ND2   . ASN A  1 65  ? 17.107  11.618  172.135 1.00 92.23  ? 65  ASN A ND2   1 
ATOM   324   N N     . SER A  1 66  ? 12.072  11.633  172.580 1.00 95.06  ? 66  SER A N     1 
ATOM   325   C CA    . SER A  1 66  ? 10.645  11.363  172.776 1.00 98.26  ? 66  SER A CA    1 
ATOM   326   C C     . SER A  1 66  ? 10.187  11.494  174.228 1.00 96.18  ? 66  SER A C     1 
ATOM   327   O O     . SER A  1 66  ? 9.015   11.782  174.488 1.00 92.75  ? 66  SER A O     1 
ATOM   328   C CB    . SER A  1 66  ? 10.294  9.966   172.265 1.00 100.65 ? 66  SER A CB    1 
ATOM   329   O OG    . SER A  1 66  ? 10.568  8.987   173.248 1.00 99.54  ? 66  SER A OG    1 
ATOM   330   N N     . LEU A  1 67  ? 11.104  11.278  175.169 1.00 96.49  ? 67  LEU A N     1 
ATOM   331   C CA    . LEU A  1 67  ? 10.874  11.675  176.555 1.00 92.97  ? 67  LEU A CA    1 
ATOM   332   C C     . LEU A  1 67  ? 10.821  13.208  176.585 1.00 91.22  ? 67  LEU A C     1 
ATOM   333   O O     . LEU A  1 67  ? 10.434  13.825  175.592 1.00 96.83  ? 67  LEU A O     1 
ATOM   334   C CB    . LEU A  1 67  ? 11.973  11.140  177.479 1.00 97.69  ? 67  LEU A CB    1 
ATOM   335   C CG    . LEU A  1 67  ? 11.569  10.774  178.914 1.00 97.52  ? 67  LEU A CG    1 
ATOM   336   C CD1   . LEU A  1 67  ? 10.826  9.442   178.941 1.00 96.35  ? 67  LEU A CD1   1 
ATOM   337   C CD2   . LEU A  1 67  ? 12.765  10.751  179.863 1.00 96.03  ? 67  LEU A CD2   1 
ATOM   338   N N     . ILE A  1 68  ? 11.194  13.823  177.706 1.00 85.63  ? 68  ILE A N     1 
ATOM   339   C CA    . ILE A  1 68  ? 11.324  15.280  177.785 1.00 78.78  ? 68  ILE A CA    1 
ATOM   340   C C     . ILE A  1 68  ? 9.978   16.015  177.563 1.00 67.06  ? 68  ILE A C     1 
ATOM   341   O O     . ILE A  1 68  ? 9.130   15.582  176.784 1.00 71.83  ? 68  ILE A O     1 
ATOM   342   C CB    . ILE A  1 68  ? 12.407  15.786  176.773 1.00 78.14  ? 68  ILE A CB    1 
ATOM   343   C CG1   . ILE A  1 68  ? 13.756  15.147  177.098 1.00 70.62  ? 68  ILE A CG1   1 
ATOM   344   C CG2   . ILE A  1 68  ? 12.527  17.293  176.811 1.00 65.30  ? 68  ILE A CG2   1 
ATOM   345   C CD1   . ILE A  1 68  ? 14.720  15.061  175.932 1.00 73.55  ? 68  ILE A CD1   1 
ATOM   346   N N     . SER A  1 69  ? 9.768   17.113  178.278 1.00 70.66  ? 69  SER A N     1 
ATOM   347   C CA    . SER A  1 69  ? 8.504   17.835  178.185 1.00 66.61  ? 69  SER A CA    1 
ATOM   348   C C     . SER A  1 69  ? 8.238   18.404  176.792 1.00 59.56  ? 69  SER A C     1 
ATOM   349   O O     . SER A  1 69  ? 9.142   18.915  176.129 1.00 55.93  ? 69  SER A O     1 
ATOM   350   C CB    . SER A  1 69  ? 8.471   18.961  179.210 1.00 56.20  ? 69  SER A CB    1 
ATOM   351   O OG    . SER A  1 69  ? 9.648   19.745  179.144 1.00 49.76  ? 69  SER A OG    1 
ATOM   352   N N     . LYS A  1 70  ? 6.987   18.299  176.357 1.00 51.51  ? 70  LYS A N     1 
ATOM   353   C CA    . LYS A  1 70  ? 6.553   18.892  175.100 1.00 50.19  ? 70  LYS A CA    1 
ATOM   354   C C     . LYS A  1 70  ? 5.444   19.896  175.370 1.00 46.52  ? 70  LYS A C     1 
ATOM   355   O O     . LYS A  1 70  ? 4.640   19.702  176.281 1.00 45.41  ? 70  LYS A O     1 
ATOM   356   C CB    . LYS A  1 70  ? 6.074   17.816  174.126 1.00 50.31  ? 70  LYS A CB    1 
ATOM   357   C CG    . LYS A  1 70  ? 7.134   16.793  173.779 1.00 57.34  ? 70  LYS A CG    1 
ATOM   358   C CD    . LYS A  1 70  ? 7.158   16.505  172.290 1.00 59.71  ? 70  LYS A CD    1 
ATOM   359   C CE    . LYS A  1 70  ? 8.298   15.568  171.947 1.00 70.06  ? 70  LYS A CE    1 
ATOM   360   N NZ    . LYS A  1 70  ? 9.592   16.092  172.464 1.00 67.82  ? 70  LYS A NZ    1 
ATOM   361   N N     . PRO A  1 71  ? 5.398   20.983  174.586 1.00 41.75  ? 71  PRO A N     1 
ATOM   362   C CA    . PRO A  1 71  ? 4.354   21.990  174.791 1.00 39.83  ? 71  PRO A CA    1 
ATOM   363   C C     . PRO A  1 71  ? 2.991   21.505  174.305 1.00 40.30  ? 71  PRO A C     1 
ATOM   364   O O     . PRO A  1 71  ? 2.921   20.727  173.354 1.00 37.00  ? 71  PRO A O     1 
ATOM   365   C CB    . PRO A  1 71  ? 4.848   23.175  173.958 1.00 37.88  ? 71  PRO A CB    1 
ATOM   366   C CG    . PRO A  1 71  ? 5.643   22.544  172.868 1.00 36.60  ? 71  PRO A CG    1 
ATOM   367   C CD    . PRO A  1 71  ? 6.321   21.358  173.500 1.00 39.85  ? 71  PRO A CD    1 
ATOM   368   N N     . SER A  1 72  ? 1.925   21.958  174.958 1.00 36.24  ? 72  SER A N     1 
ATOM   369   C CA    . SER A  1 72  ? 0.571   21.599  174.552 1.00 40.14  ? 72  SER A CA    1 
ATOM   370   C C     . SER A  1 72  ? 0.195   22.340  173.274 1.00 39.97  ? 72  SER A C     1 
ATOM   371   O O     . SER A  1 72  ? -0.715  21.932  172.549 1.00 37.40  ? 72  SER A O     1 
ATOM   372   C CB    . SER A  1 72  ? -0.430  21.915  175.665 1.00 39.41  ? 72  SER A CB    1 
ATOM   373   O OG    . SER A  1 72  ? 0.001   21.374  176.903 1.00 43.50  ? 72  SER A OG    1 
ATOM   374   N N     . ALA A  1 73  ? 0.904   23.433  173.006 1.00 37.03  ? 73  ALA A N     1 
ATOM   375   C CA    . ALA A  1 73  ? 0.697   24.214  171.790 1.00 35.12  ? 73  ALA A CA    1 
ATOM   376   C C     . ALA A  1 73  ? 1.896   25.111  171.509 1.00 32.02  ? 73  ALA A C     1 
ATOM   377   O O     . ALA A  1 73  ? 2.628   25.486  172.423 1.00 33.81  ? 73  ALA A O     1 
ATOM   378   C CB    . ALA A  1 73  ? -0.568  25.048  171.901 1.00 36.42  ? 73  ALA A CB    1 
ATOM   379   N N     . ILE A  1 74  ? 2.089   25.454  170.240 1.00 34.02  ? 74  ILE A N     1 
ATOM   380   C CA    . ILE A  1 74  ? 3.127   26.396  169.847 1.00 36.00  ? 74  ILE A CA    1 
ATOM   381   C C     . ILE A  1 74  ? 2.497   27.598  169.155 1.00 34.91  ? 74  ILE A C     1 
ATOM   382   O O     . ILE A  1 74  ? 1.743   27.442  168.195 1.00 37.72  ? 74  ILE A O     1 
ATOM   383   C CB    . ILE A  1 74  ? 4.159   25.754  168.904 1.00 31.22  ? 74  ILE A CB    1 
ATOM   384   C CG1   . ILE A  1 74  ? 4.827   24.559  169.578 1.00 36.69  ? 74  ILE A CG1   1 
ATOM   385   C CG2   . ILE A  1 74  ? 5.206   26.781  168.489 1.00 33.42  ? 74  ILE A CG2   1 
ATOM   386   C CD1   . ILE A  1 74  ? 5.739   23.784  168.662 1.00 36.59  ? 74  ILE A CD1   1 
ATOM   387   N N     . ILE A  1 75  ? 2.800   28.795  169.643 1.00 32.88  ? 75  ILE A N     1 
ATOM   388   C CA    . ILE A  1 75  ? 2.201   30.006  169.093 1.00 35.52  ? 75  ILE A CA    1 
ATOM   389   C C     . ILE A  1 75  ? 3.268   30.910  168.490 1.00 35.45  ? 75  ILE A C     1 
ATOM   390   O O     . ILE A  1 75  ? 4.306   31.146  169.101 1.00 34.59  ? 75  ILE A O     1 
ATOM   391   C CB    . ILE A  1 75  ? 1.413   30.784  170.165 1.00 29.54  ? 75  ILE A CB    1 
ATOM   392   C CG1   . ILE A  1 75  ? 0.390   29.868  170.845 1.00 35.45  ? 75  ILE A CG1   1 
ATOM   393   C CG2   . ILE A  1 75  ? 0.725   31.995  169.553 1.00 31.34  ? 75  ILE A CG2   1 
ATOM   394   C CD1   . ILE A  1 75  ? -0.228  30.455  172.094 1.00 41.10  ? 75  ILE A CD1   1 
ATOM   395   N N     . LEU A  1 76  ? 3.008   31.401  167.282 1.00 35.24  ? 76  LEU A N     1 
ATOM   396   C CA    . LEU A  1 76  ? 3.928   32.304  166.599 1.00 35.75  ? 76  LEU A CA    1 
ATOM   397   C C     . LEU A  1 76  ? 3.307   33.681  166.385 1.00 34.49  ? 76  LEU A C     1 
ATOM   398   O O     . LEU A  1 76  ? 2.780   33.960  165.307 1.00 40.83  ? 76  LEU A O     1 
ATOM   399   C CB    . LEU A  1 76  ? 4.356   31.719  165.248 1.00 40.46  ? 76  LEU A CB    1 
ATOM   400   C CG    . LEU A  1 76  ? 5.417   30.612  165.173 1.00 38.76  ? 76  LEU A CG    1 
ATOM   401   C CD1   . LEU A  1 76  ? 4.911   29.283  165.715 1.00 36.72  ? 76  LEU A CD1   1 
ATOM   402   C CD2   . LEU A  1 76  ? 5.900   30.456  163.738 1.00 41.98  ? 76  LEU A CD2   1 
ATOM   403   N N     . PRO A  1 77  ? 3.369   34.547  167.409 1.00 35.52  ? 77  PRO A N     1 
ATOM   404   C CA    . PRO A  1 77  ? 2.838   35.908  167.266 1.00 33.68  ? 77  PRO A CA    1 
ATOM   405   C C     . PRO A  1 77  ? 3.591   36.679  166.192 1.00 34.31  ? 77  PRO A C     1 
ATOM   406   O O     . PRO A  1 77  ? 4.806   36.524  166.073 1.00 31.32  ? 77  PRO A O     1 
ATOM   407   C CB    . PRO A  1 77  ? 3.061   36.526  168.649 1.00 34.16  ? 77  PRO A CB    1 
ATOM   408   C CG    . PRO A  1 77  ? 4.160   35.715  169.258 1.00 31.59  ? 77  PRO A CG    1 
ATOM   409   C CD    . PRO A  1 77  ? 3.969   34.322  168.736 1.00 31.19  ? 77  PRO A CD    1 
ATOM   410   N N     . GLY A  1 78  ? 2.872   37.487  165.418 1.00 30.94  ? 78  GLY A N     1 
ATOM   411   C CA    . GLY A  1 78  ? 3.462   38.210  164.307 1.00 31.10  ? 78  GLY A CA    1 
ATOM   412   C C     . GLY A  1 78  ? 3.570   39.701  164.559 1.00 34.14  ? 78  GLY A C     1 
ATOM   413   O O     . GLY A  1 78  ? 3.962   40.462  163.677 1.00 32.54  ? 78  GLY A O     1 
ATOM   414   N N     . SER A  1 79  ? 3.222   40.117  165.771 1.00 29.24  ? 79  SER A N     1 
ATOM   415   C CA    . SER A  1 79  ? 3.292   41.523  166.152 1.00 33.15  ? 79  SER A CA    1 
ATOM   416   C C     . SER A  1 79  ? 3.398   41.645  167.666 1.00 28.69  ? 79  SER A C     1 
ATOM   417   O O     . SER A  1 79  ? 3.131   40.684  168.388 1.00 31.15  ? 79  SER A O     1 
ATOM   418   C CB    . SER A  1 79  ? 2.066   42.285  165.646 1.00 31.63  ? 79  SER A CB    1 
ATOM   419   O OG    . SER A  1 79  ? 0.920   41.940  166.404 1.00 27.46  ? 79  SER A OG    1 
ATOM   420   N N     . LYS A  1 80  ? 3.773   42.825  168.148 1.00 26.47  ? 80  LYS A N     1 
ATOM   421   C CA    . LYS A  1 80  ? 3.900   43.025  169.586 1.00 28.46  ? 80  LYS A CA    1 
ATOM   422   C C     . LYS A  1 80  ? 2.533   42.953  170.269 1.00 32.62  ? 80  LYS A C     1 
ATOM   423   O O     . LYS A  1 80  ? 2.427   42.499  171.408 1.00 32.40  ? 80  LYS A O     1 
ATOM   424   C CB    . LYS A  1 80  ? 4.595   44.355  169.896 1.00 25.38  ? 80  LYS A CB    1 
ATOM   425   C CG    . LYS A  1 80  ? 3.827   45.610  169.510 1.00 32.18  ? 80  LYS A CG    1 
ATOM   426   C CD    . LYS A  1 80  ? 4.660   46.853  169.810 1.00 29.67  ? 80  LYS A CD    1 
ATOM   427   C CE    . LYS A  1 80  ? 3.862   48.134  169.626 1.00 32.56  ? 80  LYS A CE    1 
ATOM   428   N NZ    . LYS A  1 80  ? 3.446   48.335  168.213 1.00 33.24  ? 80  LYS A NZ    1 
ATOM   429   N N     . GLU A  1 81  ? 1.488   43.384  169.567 1.00 31.89  ? 81  GLU A N     1 
ATOM   430   C CA    . GLU A  1 81  ? 0.132   43.295  170.100 1.00 30.59  ? 81  GLU A CA    1 
ATOM   431   C C     . GLU A  1 81  ? -0.304  41.836  170.199 1.00 29.39  ? 81  GLU A C     1 
ATOM   432   O O     . GLU A  1 81  ? -0.944  41.436  171.172 1.00 33.67  ? 81  GLU A O     1 
ATOM   433   C CB    . GLU A  1 81  ? -0.855  44.087  169.238 1.00 32.81  ? 81  GLU A CB    1 
ATOM   434   C CG    . GLU A  1 81  ? -0.637  45.595  169.271 1.00 30.02  ? 81  GLU A CG    1 
ATOM   435   C CD    . GLU A  1 81  ? 0.457   46.047  168.330 1.00 28.06  ? 81  GLU A CD    1 
ATOM   436   O OE1   . GLU A  1 81  ? 0.849   45.251  167.452 1.00 32.71  ? 81  GLU A OE1   1 
ATOM   437   O OE2   . GLU A  1 81  ? 0.926   47.197  168.466 1.00 32.02  ? 81  GLU A OE2   1 
ATOM   438   N N     . GLU A  1 82  ? 0.053   41.044  169.191 1.00 27.82  ? 82  GLU A N     1 
ATOM   439   C CA    . GLU A  1 82  ? -0.236  39.613  169.210 1.00 29.61  ? 82  GLU A CA    1 
ATOM   440   C C     . GLU A  1 82  ? 0.533   38.911  170.324 1.00 33.73  ? 82  GLU A C     1 
ATOM   441   O O     . GLU A  1 82  ? 0.029   37.971  170.939 1.00 31.21  ? 82  GLU A O     1 
ATOM   442   C CB    . GLU A  1 82  ? 0.097   38.968  167.864 1.00 30.88  ? 82  GLU A CB    1 
ATOM   443   C CG    . GLU A  1 82  ? -0.936  39.207  166.767 1.00 33.73  ? 82  GLU A CG    1 
ATOM   444   C CD    . GLU A  1 82  ? -0.688  38.349  165.540 1.00 33.03  ? 82  GLU A CD    1 
ATOM   445   O OE1   . GLU A  1 82  ? 0.115   37.399  165.630 1.00 38.78  ? 82  GLU A OE1   1 
ATOM   446   O OE2   . GLU A  1 82  ? -1.293  38.627  164.485 1.00 42.05  ? 82  GLU A OE2   1 
ATOM   447   N N     . LEU A  1 83  ? 1.755   39.373  170.574 1.00 29.47  ? 83  LEU A N     1 
ATOM   448   C CA    . LEU A  1 83  ? 2.572   38.836  171.656 1.00 31.72  ? 83  LEU A CA    1 
ATOM   449   C C     . LEU A  1 83  ? 1.927   39.158  172.998 1.00 28.42  ? 83  LEU A C     1 
ATOM   450   O O     . LEU A  1 83  ? 1.864   38.310  173.887 1.00 29.31  ? 83  LEU A O     1 
ATOM   451   C CB    . LEU A  1 83  ? 3.998   39.394  171.585 1.00 24.04  ? 83  LEU A CB    1 
ATOM   452   C CG    . LEU A  1 83  ? 4.978   39.010  172.695 1.00 30.79  ? 83  LEU A CG    1 
ATOM   453   C CD1   . LEU A  1 83  ? 5.057   37.493  172.870 1.00 28.45  ? 83  LEU A CD1   1 
ATOM   454   C CD2   . LEU A  1 83  ? 6.363   39.597  172.413 1.00 33.95  ? 83  LEU A CD2   1 
ATOM   455   N N     . SER A  1 84  ? 1.440   40.389  173.128 1.00 29.33  ? 84  SER A N     1 
ATOM   456   C CA    . SER A  1 84  ? 0.741   40.830  174.332 1.00 31.54  ? 84  SER A CA    1 
ATOM   457   C C     . SER A  1 84  ? -0.485  39.968  174.629 1.00 28.89  ? 84  SER A C     1 
ATOM   458   O O     . SER A  1 84  ? -0.659  39.480  175.746 1.00 26.68  ? 84  SER A O     1 
ATOM   459   C CB    . SER A  1 84  ? 0.327   42.298  174.197 1.00 29.85  ? 84  SER A CB    1 
ATOM   460   O OG    . SER A  1 84  ? -0.532  42.689  175.248 1.00 30.89  ? 84  SER A OG    1 
ATOM   461   N N     . ASN A  1 85  ? -1.330  39.784  173.622 1.00 27.68  ? 85  ASN A N     1 
ATOM   462   C CA    . ASN A  1 85  ? -2.559  39.012  173.783 1.00 29.86  ? 85  ASN A CA    1 
ATOM   463   C C     . ASN A  1 85  ? -2.304  37.515  173.945 1.00 35.50  ? 85  ASN A C     1 
ATOM   464   O O     . ASN A  1 85  ? -3.076  36.815  174.601 1.00 35.47  ? 85  ASN A O     1 
ATOM   465   C CB    . ASN A  1 85  ? -3.491  39.252  172.598 1.00 25.88  ? 85  ASN A CB    1 
ATOM   466   C CG    . ASN A  1 85  ? -4.073  40.655  172.590 1.00 35.43  ? 85  ASN A CG    1 
ATOM   467   O OD1   . ASN A  1 85  ? -4.241  41.279  173.638 1.00 30.72  ? 85  ASN A OD1   1 
ATOM   468   N ND2   . ASN A  1 85  ? -4.387  41.156  171.402 1.00 33.65  ? 85  ASN A ND2   1 
ATOM   469   N N     . THR A  1 86  ? -1.228  37.026  173.336 1.00 33.12  ? 86  THR A N     1 
ATOM   470   C CA    . THR A  1 86  ? -0.836  35.630  173.489 1.00 31.87  ? 86  THR A CA    1 
ATOM   471   C C     . THR A  1 86  ? -0.527  35.337  174.952 1.00 33.55  ? 86  THR A C     1 
ATOM   472   O O     . THR A  1 86  ? -0.980  34.338  175.510 1.00 34.26  ? 86  THR A O     1 
ATOM   473   C CB    . THR A  1 86  ? 0.390   35.287  172.626 1.00 32.62  ? 86  THR A CB    1 
ATOM   474   O OG1   . THR A  1 86  ? 0.035   35.356  171.239 1.00 30.79  ? 86  THR A OG1   1 
ATOM   475   C CG2   . THR A  1 86  ? 0.897   33.890  172.951 1.00 28.05  ? 86  THR A CG2   1 
ATOM   476   N N     . ILE A  1 87  ? 0.243   36.229  175.565 1.00 31.99  ? 87  ILE A N     1 
ATOM   477   C CA    . ILE A  1 87  ? 0.578   36.134  176.981 1.00 32.47  ? 87  ILE A CA    1 
ATOM   478   C C     . ILE A  1 87  ? -0.681  36.129  177.842 1.00 37.05  ? 87  ILE A C     1 
ATOM   479   O O     . ILE A  1 87  ? -0.824  35.305  178.745 1.00 36.35  ? 87  ILE A O     1 
ATOM   480   C CB    . ILE A  1 87  ? 1.494   37.297  177.413 1.00 26.90  ? 87  ILE A CB    1 
ATOM   481   C CG1   . ILE A  1 87  ? 2.894   37.130  176.813 1.00 29.04  ? 87  ILE A CG1   1 
ATOM   482   C CG2   . ILE A  1 87  ? 1.565   37.392  178.930 1.00 33.13  ? 87  ILE A CG2   1 
ATOM   483   C CD1   . ILE A  1 87  ? 3.785   38.337  177.006 1.00 26.05  ? 87  ILE A CD1   1 
ATOM   484   N N     . ARG A  1 88  ? -1.592  37.054  177.550 1.00 34.28  ? 88  ARG A N     1 
ATOM   485   C CA    . ARG A  1 88  ? -2.865  37.146  178.260 1.00 35.34  ? 88  ARG A CA    1 
ATOM   486   C C     . ARG A  1 88  ? -3.682  35.855  178.158 1.00 34.43  ? 88  ARG A C     1 
ATOM   487   O O     . ARG A  1 88  ? -4.245  35.394  179.152 1.00 33.44  ? 88  ARG A O     1 
ATOM   488   C CB    . ARG A  1 88  ? -3.692  38.317  177.724 1.00 33.58  ? 88  ARG A CB    1 
ATOM   489   C CG    . ARG A  1 88  ? -3.131  39.702  178.023 1.00 38.43  ? 88  ARG A CG    1 
ATOM   490   C CD    . ARG A  1 88  ? -4.076  40.809  177.549 1.00 38.22  ? 88  ARG A CD    1 
ATOM   491   N NE    . ARG A  1 88  ? -5.474  40.510  177.858 1.00 42.41  ? 88  ARG A NE    1 
ATOM   492   C CZ    . ARG A  1 88  ? -6.361  40.070  176.971 1.00 39.38  ? 88  ARG A CZ    1 
ATOM   493   N NH1   . ARG A  1 88  ? -6.002  39.878  175.708 1.00 34.80  ? 88  ARG A NH1   1 
ATOM   494   N NH2   . ARG A  1 88  ? -7.605  39.818  177.346 1.00 44.84  ? 88  ARG A NH2   1 
ATOM   495   N N     . CYS A  1 89  ? -3.745  35.279  176.959 1.00 35.39  ? 89  CYS A N     1 
ATOM   496   C CA    . CYS A  1 89  ? -4.570  34.094  176.711 1.00 38.83  ? 89  CYS A CA    1 
ATOM   497   C C     . CYS A  1 89  ? -4.040  32.851  177.417 1.00 39.54  ? 89  CYS A C     1 
ATOM   498   O O     . CYS A  1 89  ? -4.795  32.176  178.123 1.00 36.60  ? 89  CYS A O     1 
ATOM   499   C CB    . CYS A  1 89  ? -4.685  33.817  175.211 1.00 34.29  ? 89  CYS A CB    1 
ATOM   500   S SG    . CYS A  1 89  ? -5.707  34.983  174.298 1.00 39.62  ? 89  CYS A SG    1 
ATOM   501   N N     . ILE A  1 90  ? -2.762  32.538  177.207 1.00 41.02  ? 90  ILE A N     1 
ATOM   502   C CA    . ILE A  1 90  ? -2.106  31.412  177.867 1.00 42.26  ? 90  ILE A CA    1 
ATOM   503   C C     . ILE A  1 90  ? -2.347  31.437  179.372 1.00 42.02  ? 90  ILE A C     1 
ATOM   504   O O     . ILE A  1 90  ? -2.672  30.412  179.991 1.00 42.01  ? 90  ILE A O     1 
ATOM   505   C CB    . ILE A  1 90  ? -0.574  31.422  177.628 1.00 36.41  ? 90  ILE A CB    1 
ATOM   506   C CG1   . ILE A  1 90  ? -0.238  31.311  176.141 1.00 35.24  ? 90  ILE A CG1   1 
ATOM   507   C CG2   . ILE A  1 90  ? 0.094   30.295  178.395 1.00 41.24  ? 90  ILE A CG2   1 
ATOM   508   C CD1   . ILE A  1 90  ? 1.242   31.484  175.849 1.00 34.56  ? 90  ILE A CD1   1 
ATOM   509   N N     . ARG A  1 91  ? -2.219  32.623  179.952 1.00 43.27  ? 91  ARG A N     1 
ATOM   510   C CA    . ARG A  1 91  ? -2.335  32.792  181.384 1.00 47.64  ? 91  ARG A CA    1 
ATOM   511   C C     . ARG A  1 91  ? -3.752  32.584  181.931 1.00 48.43  ? 91  ARG A C     1 
ATOM   512   O O     . ARG A  1 91  ? -3.921  32.178  183.077 1.00 47.96  ? 91  ARG A O     1 
ATOM   513   C CB    . ARG A  1 91  ? -1.828  34.178  181.747 1.00 45.62  ? 91  ARG A CB    1 
ATOM   514   C CG    . ARG A  1 91  ? -1.986  34.527  183.190 1.00 51.97  ? 91  ARG A CG    1 
ATOM   515   C CD    . ARG A  1 91  ? -1.444  35.899  183.433 1.00 46.64  ? 91  ARG A CD    1 
ATOM   516   N NE    . ARG A  1 91  ? -1.432  36.216  184.852 1.00 48.34  ? 91  ARG A NE    1 
ATOM   517   C CZ    . ARG A  1 91  ? -1.015  37.375  185.350 1.00 45.84  ? 91  ARG A CZ    1 
ATOM   518   N NH1   . ARG A  1 91  ? -1.037  37.584  186.657 1.00 51.09  ? 91  ARG A NH1   1 
ATOM   519   N NH2   . ARG A  1 91  ? -0.575  38.329  184.541 1.00 50.76  ? 91  ARG A NH2   1 
ATOM   520   N N     . LYS A  1 92  ? -4.767  32.837  181.108 1.00 44.64  ? 92  LYS A N     1 
ATOM   521   C CA    . LYS A  1 92  ? -6.150  32.561  181.504 1.00 47.91  ? 92  LYS A CA    1 
ATOM   522   C C     . LYS A  1 92  ? -6.348  31.074  181.791 1.00 54.20  ? 92  LYS A C     1 
ATOM   523   O O     . LYS A  1 92  ? -7.252  30.686  182.534 1.00 51.97  ? 92  LYS A O     1 
ATOM   524   C CB    . LYS A  1 92  ? -7.142  33.006  180.423 1.00 49.03  ? 92  LYS A CB    1 
ATOM   525   C CG    . LYS A  1 92  ? -7.322  34.511  180.312 1.00 46.93  ? 92  LYS A CG    1 
ATOM   526   C CD    . LYS A  1 92  ? -8.437  34.842  179.326 1.00 53.17  ? 92  LYS A CD    1 
ATOM   527   C CE    . LYS A  1 92  ? -8.598  36.338  179.137 1.00 51.91  ? 92  LYS A CE    1 
ATOM   528   N NZ    . LYS A  1 92  ? -9.070  36.640  177.758 1.00 56.74  ? 92  LYS A NZ    1 
ATOM   529   N N     . GLY A  1 93  ? -5.500  30.246  181.188 1.00 50.13  ? 93  GLY A N     1 
ATOM   530   C CA    . GLY A  1 93  ? -5.470  28.827  181.472 1.00 48.23  ? 93  GLY A CA    1 
ATOM   531   C C     . GLY A  1 93  ? -4.535  28.529  182.628 1.00 53.87  ? 93  GLY A C     1 
ATOM   532   O O     . GLY A  1 93  ? -4.201  29.417  183.412 1.00 50.29  ? 93  GLY A O     1 
ATOM   533   N N     . SER A  1 94  ? -4.110  27.275  182.738 1.00 56.57  ? 94  SER A N     1 
ATOM   534   C CA    . SER A  1 94  ? -3.252  26.850  183.838 1.00 66.46  ? 94  SER A CA    1 
ATOM   535   C C     . SER A  1 94  ? -1.786  26.824  183.423 1.00 56.84  ? 94  SER A C     1 
ATOM   536   O O     . SER A  1 94  ? -0.902  26.546  184.235 1.00 63.67  ? 94  SER A O     1 
ATOM   537   C CB    . SER A  1 94  ? -3.681  25.466  184.335 1.00 63.04  ? 94  SER A CB    1 
ATOM   538   O OG    . SER A  1 94  ? -3.685  24.526  183.273 1.00 67.57  ? 94  SER A OG    1 
ATOM   539   N N     . TRP A  1 95  ? -1.537  27.140  182.157 1.00 53.06  ? 95  TRP A N     1 
ATOM   540   C CA    . TRP A  1 95  ? -0.242  26.884  181.531 1.00 48.93  ? 95  TRP A CA    1 
ATOM   541   C C     . TRP A  1 95  ? 0.911   27.773  181.981 1.00 44.19  ? 95  TRP A C     1 
ATOM   542   O O     . TRP A  1 95  ? 0.745   28.961  182.262 1.00 46.94  ? 95  TRP A O     1 
ATOM   543   C CB    . TRP A  1 95  ? -0.372  27.003  180.013 1.00 46.54  ? 95  TRP A CB    1 
ATOM   544   C CG    . TRP A  1 95  ? -1.227  25.953  179.406 1.00 49.32  ? 95  TRP A CG    1 
ATOM   545   C CD1   . TRP A  1 95  ? -0.896  24.646  179.191 1.00 47.66  ? 95  TRP A CD1   1 
ATOM   546   C CD2   . TRP A  1 95  ? -2.561  26.116  178.917 1.00 49.23  ? 95  TRP A CD2   1 
ATOM   547   N NE1   . TRP A  1 95  ? -1.946  23.983  178.603 1.00 51.14  ? 95  TRP A NE1   1 
ATOM   548   C CE2   . TRP A  1 95  ? -2.981  24.864  178.424 1.00 51.67  ? 95  TRP A CE2   1 
ATOM   549   C CE3   . TRP A  1 95  ? -3.444  27.198  178.851 1.00 41.98  ? 95  TRP A CE3   1 
ATOM   550   C CZ2   . TRP A  1 95  ? -4.245  24.666  177.871 1.00 53.37  ? 95  TRP A CZ2   1 
ATOM   551   C CZ3   . TRP A  1 95  ? -4.697  27.001  178.302 1.00 56.12  ? 95  TRP A CZ3   1 
ATOM   552   C CH2   . TRP A  1 95  ? -5.087  25.745  177.820 1.00 61.69  ? 95  TRP A CH2   1 
ATOM   553   N N     . THR A  1 96  ? 2.088   27.158  182.031 1.00 46.29  ? 96  THR A N     1 
ATOM   554   C CA    . THR A  1 96  ? 3.352   27.859  182.177 1.00 41.79  ? 96  THR A CA    1 
ATOM   555   C C     . THR A  1 96  ? 3.761   28.456  180.835 1.00 37.79  ? 96  THR A C     1 
ATOM   556   O O     . THR A  1 96  ? 3.668   27.796  179.803 1.00 37.78  ? 96  THR A O     1 
ATOM   557   C CB    . THR A  1 96  ? 4.458   26.909  182.684 1.00 38.89  ? 96  THR A CB    1 
ATOM   558   O OG1   . THR A  1 96  ? 4.099   26.400  183.976 1.00 38.79  ? 96  THR A OG1   1 
ATOM   559   C CG2   . THR A  1 96  ? 5.798   27.628  182.771 1.00 40.87  ? 96  THR A CG2   1 
ATOM   560   N N     . ILE A  1 97  ? 4.199   29.708  180.837 1.00 36.91  ? 97  ILE A N     1 
ATOM   561   C CA    . ILE A  1 97  ? 4.645   30.339  179.602 1.00 35.93  ? 97  ILE A CA    1 
ATOM   562   C C     . ILE A  1 97  ? 6.116   30.034  179.325 1.00 33.81  ? 97  ILE A C     1 
ATOM   563   O O     . ILE A  1 97  ? 6.951   30.090  180.227 1.00 33.58  ? 97  ILE A O     1 
ATOM   564   C CB    . ILE A  1 97  ? 4.431   31.862  179.651 1.00 36.67  ? 97  ILE A CB    1 
ATOM   565   C CG1   . ILE A  1 97  ? 2.938   32.182  179.634 1.00 35.44  ? 97  ILE A CG1   1 
ATOM   566   C CG2   . ILE A  1 97  ? 5.128   32.544  178.484 1.00 34.54  ? 97  ILE A CG2   1 
ATOM   567   C CD1   . ILE A  1 97  ? 2.625   33.639  179.866 1.00 38.17  ? 97  ILE A CD1   1 
ATOM   568   N N     . ARG A  1 98  ? 6.418   29.688  178.078 1.00 29.90  ? 98  ARG A N     1 
ATOM   569   C CA    . ARG A  1 98  ? 7.794   29.536  177.635 1.00 32.08  ? 98  ARG A CA    1 
ATOM   570   C C     . ARG A  1 98  ? 8.035   30.404  176.409 1.00 32.17  ? 98  ARG A C     1 
ATOM   571   O O     . ARG A  1 98  ? 7.271   30.355  175.444 1.00 36.16  ? 98  ARG A O     1 
ATOM   572   C CB    . ARG A  1 98  ? 8.115   28.071  177.330 1.00 30.31  ? 98  ARG A CB    1 
ATOM   573   C CG    . ARG A  1 98  ? 8.428   27.241  178.560 1.00 33.79  ? 98  ARG A CG    1 
ATOM   574   C CD    . ARG A  1 98  ? 9.755   27.660  179.174 1.00 31.67  ? 98  ARG A CD    1 
ATOM   575   N NE    . ARG A  1 98  ? 10.003  26.999  180.452 1.00 33.11  ? 98  ARG A NE    1 
ATOM   576   C CZ    . ARG A  1 98  ? 9.641   27.494  181.632 1.00 34.33  ? 98  ARG A CZ    1 
ATOM   577   N NH1   . ARG A  1 98  ? 9.013   28.661  181.703 1.00 30.19  ? 98  ARG A NH1   1 
ATOM   578   N NH2   . ARG A  1 98  ? 9.906   26.821  182.743 1.00 34.33  ? 98  ARG A NH2   1 
ATOM   579   N N     . LEU A  1 99  ? 9.087   31.212  176.463 1.00 30.67  ? 99  LEU A N     1 
ATOM   580   C CA    . LEU A  1 99  ? 9.461   32.057  175.337 1.00 28.94  ? 99  LEU A CA    1 
ATOM   581   C C     . LEU A  1 99  ? 10.676  31.473  174.630 1.00 32.50  ? 99  LEU A C     1 
ATOM   582   O O     . LEU A  1 99  ? 11.613  31.013  175.279 1.00 36.17  ? 99  LEU A O     1 
ATOM   583   C CB    . LEU A  1 99  ? 9.766   33.480  175.806 1.00 32.02  ? 99  LEU A CB    1 
ATOM   584   C CG    . LEU A  1 99  ? 8.670   34.246  176.548 1.00 33.26  ? 99  LEU A CG    1 
ATOM   585   C CD1   . LEU A  1 99  ? 9.272   35.445  177.256 1.00 30.74  ? 99  LEU A CD1   1 
ATOM   586   C CD2   . LEU A  1 99  ? 7.574   34.683  175.588 1.00 29.55  ? 99  LEU A CD2   1 
ATOM   587   N N     . ARG A  1 100 ? 10.665  31.481  173.302 1.00 30.37  ? 100 ARG A N     1 
ATOM   588   C CA    . ARG A  1 100 ? 11.828  31.026  172.549 1.00 33.60  ? 100 ARG A CA    1 
ATOM   589   C C     . ARG A  1 100 ? 12.157  31.961  171.397 1.00 38.54  ? 100 ARG A C     1 
ATOM   590   O O     . ARG A  1 100 ? 11.301  32.267  170.566 1.00 30.06  ? 100 ARG A O     1 
ATOM   591   C CB    . ARG A  1 100 ? 11.621  29.607  172.009 1.00 37.41  ? 100 ARG A CB    1 
ATOM   592   C CG    . ARG A  1 100 ? 12.837  29.082  171.250 1.00 34.52  ? 100 ARG A CG    1 
ATOM   593   C CD    . ARG A  1 100 ? 12.709  27.606  170.907 1.00 37.40  ? 100 ARG A CD    1 
ATOM   594   N NE    . ARG A  1 100 ? 11.729  27.360  169.853 1.00 37.45  ? 100 ARG A NE    1 
ATOM   595   C CZ    . ARG A  1 100 ? 11.387  26.150  169.420 1.00 39.62  ? 100 ARG A CZ    1 
ATOM   596   N NH1   . ARG A  1 100 ? 10.486  26.017  168.456 1.00 42.83  ? 100 ARG A NH1   1 
ATOM   597   N NH2   . ARG A  1 100 ? 11.944  25.072  169.953 1.00 39.00  ? 100 ARG A NH2   1 
ATOM   598   N N     . SER A  1 101 ? 13.409  32.404  171.357 1.00 33.44  ? 101 SER A N     1 
ATOM   599   C CA    . SER A  1 101 ? 13.898  33.244  170.273 1.00 30.21  ? 101 SER A CA    1 
ATOM   600   C C     . SER A  1 101 ? 14.737  32.416  169.310 1.00 36.38  ? 101 SER A C     1 
ATOM   601   O O     . SER A  1 101 ? 14.273  32.040  168.232 1.00 34.21  ? 101 SER A O     1 
ATOM   602   C CB    . SER A  1 101 ? 14.718  34.415  170.822 1.00 30.60  ? 101 SER A CB    1 
ATOM   603   O OG    . SER A  1 101 ? 15.213  35.227  169.773 1.00 31.53  ? 101 SER A OG    1 
ATOM   604   N N     . GLY A  1 102 ? 15.972  32.127  169.708 1.00 31.81  ? 102 GLY A N     1 
ATOM   605   C CA    . GLY A  1 102 ? 16.874  31.335  168.890 1.00 30.43  ? 102 GLY A CA    1 
ATOM   606   C C     . GLY A  1 102 ? 16.962  29.888  169.336 1.00 33.76  ? 102 GLY A C     1 
ATOM   607   O O     . GLY A  1 102 ? 17.438  29.031  168.589 1.00 33.71  ? 102 GLY A O     1 
ATOM   608   N N     . GLY A  1 103 ? 16.513  29.620  170.560 1.00 30.76  ? 103 GLY A N     1 
ATOM   609   C CA    . GLY A  1 103 ? 16.482  28.270  171.096 1.00 34.31  ? 103 GLY A CA    1 
ATOM   610   C C     . GLY A  1 103 ? 17.837  27.694  171.469 1.00 40.03  ? 103 GLY A C     1 
ATOM   611   O O     . GLY A  1 103 ? 18.006  26.472  171.519 1.00 31.74  ? 103 GLY A O     1 
ATOM   612   N N     . HIS A  1 104 ? 18.800  28.566  171.751 1.00 36.52  ? 104 HIS A N     1 
ATOM   613   C CA    . HIS A  1 104 ? 20.164  28.127  172.036 1.00 35.07  ? 104 HIS A CA    1 
ATOM   614   C C     . HIS A  1 104 ? 20.432  27.869  173.510 1.00 35.09  ? 104 HIS A C     1 
ATOM   615   O O     . HIS A  1 104 ? 21.580  27.653  173.898 1.00 35.04  ? 104 HIS A O     1 
ATOM   616   C CB    . HIS A  1 104 ? 21.174  29.155  171.519 1.00 36.54  ? 104 HIS A CB    1 
ATOM   617   C CG    . HIS A  1 104 ? 21.693  28.848  170.151 1.00 33.75  ? 104 HIS A CG    1 
ATOM   618   N ND1   . HIS A  1 104 ? 22.852  28.130  169.938 1.00 35.38  ? 104 HIS A ND1   1 
ATOM   619   C CD2   . HIS A  1 104 ? 21.199  29.142  168.927 1.00 34.10  ? 104 HIS A CD2   1 
ATOM   620   C CE1   . HIS A  1 104 ? 23.049  28.003  168.637 1.00 34.81  ? 104 HIS A CE1   1 
ATOM   621   N NE2   . HIS A  1 104 ? 22.062  28.608  168.002 1.00 35.69  ? 104 HIS A NE2   1 
ATOM   622   N N     . SER A  1 105 ? 19.378  27.894  174.321 1.00 35.23  ? 105 SER A N     1 
ATOM   623   C CA    . SER A  1 105 ? 19.504  27.623  175.749 1.00 33.72  ? 105 SER A CA    1 
ATOM   624   C C     . SER A  1 105 ? 20.297  26.347  175.998 1.00 38.23  ? 105 SER A C     1 
ATOM   625   O O     . SER A  1 105 ? 19.927  25.274  175.520 1.00 38.78  ? 105 SER A O     1 
ATOM   626   C CB    . SER A  1 105 ? 18.127  27.517  176.405 1.00 34.46  ? 105 SER A CB    1 
ATOM   627   O OG    . SER A  1 105 ? 18.241  27.088  177.750 1.00 37.21  ? 105 SER A OG    1 
ATOM   628   N N     . TYR A  1 106 ? 21.400  26.478  176.728 1.00 36.35  ? 106 TYR A N     1 
ATOM   629   C CA    . TYR A  1 106 ? 22.269  25.345  177.021 1.00 41.35  ? 106 TYR A CA    1 
ATOM   630   C C     . TYR A  1 106 ? 21.512  24.232  177.743 1.00 39.07  ? 106 TYR A C     1 
ATOM   631   O O     . TYR A  1 106 ? 21.839  23.052  177.600 1.00 39.04  ? 106 TYR A O     1 
ATOM   632   C CB    . TYR A  1 106 ? 23.464  25.800  177.858 1.00 36.99  ? 106 TYR A CB    1 
ATOM   633   C CG    . TYR A  1 106 ? 24.506  26.575  177.081 1.00 35.17  ? 106 TYR A CG    1 
ATOM   634   C CD1   . TYR A  1 106 ? 24.494  26.598  175.692 1.00 36.65  ? 106 TYR A CD1   1 
ATOM   635   C CD2   . TYR A  1 106 ? 25.510  27.272  177.739 1.00 41.57  ? 106 TYR A CD2   1 
ATOM   636   C CE1   . TYR A  1 106 ? 25.449  27.297  174.982 1.00 37.35  ? 106 TYR A CE1   1 
ATOM   637   C CE2   . TYR A  1 106 ? 26.472  27.970  177.038 1.00 42.54  ? 106 TYR A CE2   1 
ATOM   638   C CZ    . TYR A  1 106 ? 26.436  27.980  175.660 1.00 42.24  ? 106 TYR A CZ    1 
ATOM   639   O OH    . TYR A  1 106 ? 27.389  28.678  174.957 1.00 40.11  ? 106 TYR A OH    1 
ATOM   640   N N     . GLU A  1 107 ? 20.491  24.615  178.504 1.00 38.10  ? 107 GLU A N     1 
ATOM   641   C CA    . GLU A  1 107 ? 19.697  23.662  179.269 1.00 43.20  ? 107 GLU A CA    1 
ATOM   642   C C     . GLU A  1 107 ? 18.277  23.517  178.724 1.00 35.58  ? 107 GLU A C     1 
ATOM   643   O O     . GLU A  1 107 ? 17.398  22.986  179.405 1.00 40.68  ? 107 GLU A O     1 
ATOM   644   C CB    . GLU A  1 107 ? 19.647  24.082  180.740 1.00 40.81  ? 107 GLU A CB    1 
ATOM   645   C CG    . GLU A  1 107 ? 21.001  24.121  181.432 1.00 44.46  ? 107 GLU A CG    1 
ATOM   646   C CD    . GLU A  1 107 ? 21.458  22.759  181.931 1.00 47.58  ? 107 GLU A CD    1 
ATOM   647   O OE1   . GLU A  1 107 ? 21.023  21.729  181.373 1.00 47.52  ? 107 GLU A OE1   1 
ATOM   648   O OE2   . GLU A  1 107 ? 22.253  22.720  182.893 1.00 47.14  ? 107 GLU A OE2   1 
ATOM   649   N N     . GLY A  1 108 ? 18.061  23.992  177.500 1.00 39.09  ? 108 GLY A N     1 
ATOM   650   C CA    . GLY A  1 108 ? 16.775  23.863  176.836 1.00 38.36  ? 108 GLY A CA    1 
ATOM   651   C C     . GLY A  1 108 ? 15.610  24.473  177.594 1.00 37.51  ? 108 GLY A C     1 
ATOM   652   O O     . GLY A  1 108 ? 14.487  23.974  177.530 1.00 37.94  ? 108 GLY A O     1 
ATOM   653   N N     . LEU A  1 109 ? 15.880  25.563  178.305 1.00 41.02  ? 109 LEU A N     1 
ATOM   654   C CA    . LEU A  1 109 ? 14.877  26.189  179.160 1.00 39.32  ? 109 LEU A CA    1 
ATOM   655   C C     . LEU A  1 109 ? 13.832  26.982  178.382 1.00 37.29  ? 109 LEU A C     1 
ATOM   656   O O     . LEU A  1 109 ? 12.859  27.460  178.961 1.00 36.17  ? 109 LEU A O     1 
ATOM   657   C CB    . LEU A  1 109 ? 15.551  27.107  180.182 1.00 37.22  ? 109 LEU A CB    1 
ATOM   658   C CG    . LEU A  1 109 ? 16.535  26.446  181.150 1.00 32.81  ? 109 LEU A CG    1 
ATOM   659   C CD1   . LEU A  1 109 ? 17.056  27.451  182.161 1.00 33.29  ? 109 LEU A CD1   1 
ATOM   660   C CD2   . LEU A  1 109 ? 15.893  25.259  181.856 1.00 36.92  ? 109 LEU A CD2   1 
ATOM   661   N N     . SER A  1 110 ? 14.033  27.135  177.078 1.00 33.50  ? 110 SER A N     1 
ATOM   662   C CA    . SER A  1 110 ? 13.106  27.917  176.270 1.00 31.54  ? 110 SER A CA    1 
ATOM   663   C C     . SER A  1 110 ? 12.014  27.050  175.664 1.00 33.76  ? 110 SER A C     1 
ATOM   664   O O     . SER A  1 110 ? 11.039  27.571  175.130 1.00 30.58  ? 110 SER A O     1 
ATOM   665   C CB    . SER A  1 110 ? 13.844  28.660  175.157 1.00 28.64  ? 110 SER A CB    1 
ATOM   666   O OG    . SER A  1 110 ? 14.624  27.772  174.374 1.00 30.46  ? 110 SER A OG    1 
ATOM   667   N N     . TYR A  1 111 ? 12.176  25.733  175.743 1.00 31.73  ? 111 TYR A N     1 
ATOM   668   C CA    . TYR A  1 111 ? 11.200  24.822  175.155 1.00 36.31  ? 111 TYR A CA    1 
ATOM   669   C C     . TYR A  1 111 ? 10.949  23.577  176.009 1.00 36.55  ? 111 TYR A C     1 
ATOM   670   O O     . TYR A  1 111 ? 10.480  22.557  175.501 1.00 41.57  ? 111 TYR A O     1 
ATOM   671   C CB    . TYR A  1 111 ? 11.646  24.408  173.747 1.00 35.81  ? 111 TYR A CB    1 
ATOM   672   C CG    . TYR A  1 111 ? 13.086  23.945  173.660 1.00 38.12  ? 111 TYR A CG    1 
ATOM   673   C CD1   . TYR A  1 111 ? 13.422  22.615  173.877 1.00 37.69  ? 111 TYR A CD1   1 
ATOM   674   C CD2   . TYR A  1 111 ? 14.107  24.838  173.360 1.00 36.08  ? 111 TYR A CD2   1 
ATOM   675   C CE1   . TYR A  1 111 ? 14.737  22.187  173.800 1.00 41.52  ? 111 TYR A CE1   1 
ATOM   676   C CE2   . TYR A  1 111 ? 15.425  24.419  173.280 1.00 36.40  ? 111 TYR A CE2   1 
ATOM   677   C CZ    . TYR A  1 111 ? 15.734  23.094  173.501 1.00 44.51  ? 111 TYR A CZ    1 
ATOM   678   O OH    . TYR A  1 111 ? 17.041  22.673  173.424 1.00 37.71  ? 111 TYR A OH    1 
ATOM   679   N N     . THR A  1 112 ? 11.264  23.659  177.301 1.00 33.88  ? 112 THR A N     1 
ATOM   680   C CA    . THR A  1 112 ? 10.941  22.588  178.242 1.00 40.75  ? 112 THR A CA    1 
ATOM   681   C C     . THR A  1 112 ? 10.380  23.160  179.539 1.00 41.48  ? 112 THR A C     1 
ATOM   682   O O     . THR A  1 112 ? 10.646  24.311  179.887 1.00 39.55  ? 112 THR A O     1 
ATOM   683   C CB    . THR A  1 112 ? 12.172  21.708  178.582 1.00 41.04  ? 112 THR A CB    1 
ATOM   684   O OG1   . THR A  1 112 ? 13.134  22.476  179.316 1.00 37.35  ? 112 THR A OG1   1 
ATOM   685   C CG2   . THR A  1 112 ? 12.813  21.148  177.321 1.00 39.43  ? 112 THR A CG2   1 
ATOM   686   N N     . SER A  1 113 ? 9.603   22.347  180.249 1.00 38.10  ? 113 SER A N     1 
ATOM   687   C CA    . SER A  1 113 ? 9.019   22.751  181.526 1.00 39.72  ? 113 SER A CA    1 
ATOM   688   C C     . SER A  1 113 ? 8.558   21.531  182.319 1.00 48.77  ? 113 SER A C     1 
ATOM   689   O O     . SER A  1 113 ? 8.098   20.553  181.743 1.00 41.24  ? 113 SER A O     1 
ATOM   690   C CB    . SER A  1 113 ? 7.847   23.708  181.304 1.00 41.22  ? 113 SER A CB    1 
ATOM   691   O OG    . SER A  1 113 ? 7.216   24.027  182.529 1.00 42.83  ? 113 SER A OG    1 
ATOM   692   N N     . ASP A  1 114 ? 8.667   21.584  183.641 1.00 53.54  ? 114 ASP A N     1 
ATOM   693   C CA    . ASP A  1 114 ? 8.240   20.454  184.463 1.00 54.30  ? 114 ASP A CA    1 
ATOM   694   C C     . ASP A  1 114 ? 6.732   20.477  184.707 1.00 55.64  ? 114 ASP A C     1 
ATOM   695   O O     . ASP A  1 114 ? 6.189   19.605  185.383 1.00 55.56  ? 114 ASP A O     1 
ATOM   696   C CB    . ASP A  1 114 ? 8.994   20.444  185.791 1.00 66.53  ? 114 ASP A CB    1 
ATOM   697   C CG    . ASP A  1 114 ? 9.158   21.829  186.374 1.00 85.06  ? 114 ASP A CG    1 
ATOM   698   O OD1   . ASP A  1 114 ? 8.396   22.176  187.301 1.00 83.95  ? 114 ASP A OD1   1 
ATOM   699   O OD2   . ASP A  1 114 ? 10.043  22.572  185.899 1.00 85.21  ? 114 ASP A OD2   1 
ATOM   700   N N     . THR A  1 115 ? 6.067   21.482  184.149 1.00 48.18  ? 115 THR A N     1 
ATOM   701   C CA    . THR A  1 115 ? 4.616   21.601  184.216 1.00 50.75  ? 115 THR A CA    1 
ATOM   702   C C     . THR A  1 115 ? 4.090   21.846  182.803 1.00 46.48  ? 115 THR A C     1 
ATOM   703   O O     . THR A  1 115 ? 4.851   22.288  181.941 1.00 49.27  ? 115 THR A O     1 
ATOM   704   C CB    . THR A  1 115 ? 4.187   22.738  185.170 1.00 47.11  ? 115 THR A CB    1 
ATOM   705   O OG1   . THR A  1 115 ? 4.885   23.940  184.831 1.00 52.53  ? 115 THR A OG1   1 
ATOM   706   C CG2   . THR A  1 115 ? 4.505   22.370  186.613 1.00 52.61  ? 115 THR A CG2   1 
ATOM   707   N N     . PRO A  1 116 ? 2.803   21.536  182.548 1.00 49.66  ? 116 PRO A N     1 
ATOM   708   C CA    . PRO A  1 116 ? 2.230   21.783  181.218 1.00 47.14  ? 116 PRO A CA    1 
ATOM   709   C C     . PRO A  1 116 ? 2.454   23.216  180.766 1.00 42.37  ? 116 PRO A C     1 
ATOM   710   O O     . PRO A  1 116 ? 2.244   24.143  181.546 1.00 38.91  ? 116 PRO A O     1 
ATOM   711   C CB    . PRO A  1 116 ? 0.741   21.506  181.421 1.00 44.79  ? 116 PRO A CB    1 
ATOM   712   C CG    . PRO A  1 116 ? 0.700   20.521  182.520 1.00 41.67  ? 116 PRO A CG    1 
ATOM   713   C CD    . PRO A  1 116 ? 1.833   20.883  183.444 1.00 44.48  ? 116 PRO A CD    1 
ATOM   714   N N     . PHE A  1 117 ? 2.878   23.401  179.524 1.00 41.84  ? 117 PHE A N     1 
ATOM   715   C CA    . PHE A  1 117 ? 3.276   24.731  179.100 1.00 42.46  ? 117 PHE A CA    1 
ATOM   716   C C     . PHE A  1 117 ? 2.924   25.035  177.653 1.00 40.23  ? 117 PHE A C     1 
ATOM   717   O O     . PHE A  1 117 ? 2.729   24.128  176.845 1.00 40.76  ? 117 PHE A O     1 
ATOM   718   C CB    . PHE A  1 117 ? 4.781   24.918  179.319 1.00 38.65  ? 117 PHE A CB    1 
ATOM   719   C CG    . PHE A  1 117 ? 5.646   24.045  178.449 1.00 40.51  ? 117 PHE A CG    1 
ATOM   720   C CD1   . PHE A  1 117 ? 6.361   24.589  177.392 1.00 38.28  ? 117 PHE A CD1   1 
ATOM   721   C CD2   . PHE A  1 117 ? 5.760   22.685  178.696 1.00 41.57  ? 117 PHE A CD2   1 
ATOM   722   C CE1   . PHE A  1 117 ? 7.166   23.793  176.598 1.00 39.49  ? 117 PHE A CE1   1 
ATOM   723   C CE2   . PHE A  1 117 ? 6.560   21.887  177.902 1.00 37.79  ? 117 PHE A CE2   1 
ATOM   724   C CZ    . PHE A  1 117 ? 7.265   22.441  176.852 1.00 41.00  ? 117 PHE A CZ    1 
ATOM   725   N N     . ILE A  1 118 ? 2.838   26.324  177.343 1.00 38.11  ? 118 ILE A N     1 
ATOM   726   C CA    . ILE A  1 118 ? 2.625   26.775  175.977 1.00 35.19  ? 118 ILE A CA    1 
ATOM   727   C C     . ILE A  1 118 ? 3.884   27.466  175.479 1.00 35.30  ? 118 ILE A C     1 
ATOM   728   O O     . ILE A  1 118 ? 4.451   28.315  176.166 1.00 34.03  ? 118 ILE A O     1 
ATOM   729   C CB    . ILE A  1 118 ? 1.431   27.737  175.859 1.00 30.58  ? 118 ILE A CB    1 
ATOM   730   C CG1   . ILE A  1 118 ? 0.160   27.065  176.378 1.00 39.11  ? 118 ILE A CG1   1 
ATOM   731   C CG2   . ILE A  1 118 ? 1.244   28.167  174.413 1.00 26.96  ? 118 ILE A CG2   1 
ATOM   732   C CD1   . ILE A  1 118 ? -0.300  25.913  175.522 1.00 38.78  ? 118 ILE A CD1   1 
ATOM   733   N N     . LEU A  1 119 ? 4.319   27.093  174.282 1.00 36.47  ? 119 LEU A N     1 
ATOM   734   C CA    . LEU A  1 119 ? 5.546   27.628  173.710 1.00 38.53  ? 119 LEU A CA    1 
ATOM   735   C C     . LEU A  1 119 ? 5.279   28.818  172.796 1.00 31.13  ? 119 LEU A C     1 
ATOM   736   O O     . LEU A  1 119 ? 4.656   28.672  171.746 1.00 37.18  ? 119 LEU A O     1 
ATOM   737   C CB    . LEU A  1 119 ? 6.288   26.536  172.936 1.00 30.92  ? 119 LEU A CB    1 
ATOM   738   C CG    . LEU A  1 119 ? 7.589   26.937  172.241 1.00 33.98  ? 119 LEU A CG    1 
ATOM   739   C CD1   . LEU A  1 119 ? 8.530   27.606  173.222 1.00 35.70  ? 119 LEU A CD1   1 
ATOM   740   C CD2   . LEU A  1 119 ? 8.252   25.722  171.606 1.00 37.17  ? 119 LEU A CD2   1 
ATOM   741   N N     . ILE A  1 120 ? 5.751   29.993  173.202 1.00 30.54  ? 120 ILE A N     1 
ATOM   742   C CA    . ILE A  1 120 ? 5.686   31.172  172.351 1.00 30.81  ? 120 ILE A CA    1 
ATOM   743   C C     . ILE A  1 120 ? 6.964   31.272  171.536 1.00 35.27  ? 120 ILE A C     1 
ATOM   744   O O     . ILE A  1 120 ? 8.025   31.586  172.074 1.00 35.79  ? 120 ILE A O     1 
ATOM   745   C CB    . ILE A  1 120 ? 5.502   32.473  173.159 1.00 24.95  ? 120 ILE A CB    1 
ATOM   746   C CG1   . ILE A  1 120 ? 4.285   32.370  174.076 1.00 28.89  ? 120 ILE A CG1   1 
ATOM   747   C CG2   . ILE A  1 120 ? 5.347   33.663  172.224 1.00 26.20  ? 120 ILE A CG2   1 
ATOM   748   C CD1   . ILE A  1 120 ? 4.057   33.604  174.935 1.00 29.95  ? 120 ILE A CD1   1 
ATOM   749   N N     . ASP A  1 121 ? 6.869   30.988  170.242 1.00 36.62  ? 121 ASP A N     1 
ATOM   750   C CA    . ASP A  1 121 ? 8.037   31.062  169.372 1.00 37.35  ? 121 ASP A CA    1 
ATOM   751   C C     . ASP A  1 121 ? 8.044   32.384  168.612 1.00 34.42  ? 121 ASP A C     1 
ATOM   752   O O     . ASP A  1 121 ? 7.071   32.731  167.945 1.00 38.59  ? 121 ASP A O     1 
ATOM   753   C CB    . ASP A  1 121 ? 8.065   29.889  168.394 1.00 35.99  ? 121 ASP A CB    1 
ATOM   754   C CG    . ASP A  1 121 ? 9.440   29.662  167.800 1.00 40.80  ? 121 ASP A CG    1 
ATOM   755   O OD1   . ASP A  1 121 ? 10.078  28.646  168.147 1.00 48.23  ? 121 ASP A OD1   1 
ATOM   756   O OD2   . ASP A  1 121 ? 9.893   30.504  166.996 1.00 41.62  ? 121 ASP A OD2   1 
ATOM   757   N N     . LEU A  1 122 ? 9.154   33.109  168.706 1.00 31.03  ? 122 LEU A N     1 
ATOM   758   C CA    . LEU A  1 122 ? 9.224   34.487  168.231 1.00 31.27  ? 122 LEU A CA    1 
ATOM   759   C C     . LEU A  1 122 ? 9.861   34.641  166.849 1.00 35.25  ? 122 LEU A C     1 
ATOM   760   O O     . LEU A  1 122 ? 10.210  35.751  166.448 1.00 32.05  ? 122 LEU A O     1 
ATOM   761   C CB    . LEU A  1 122 ? 10.000  35.332  169.243 1.00 36.24  ? 122 LEU A CB    1 
ATOM   762   C CG    . LEU A  1 122 ? 9.439   35.280  170.667 1.00 35.29  ? 122 LEU A CG    1 
ATOM   763   C CD1   . LEU A  1 122 ? 10.439  35.822  171.677 1.00 29.38  ? 122 LEU A CD1   1 
ATOM   764   C CD2   . LEU A  1 122 ? 8.131   36.051  170.736 1.00 31.71  ? 122 LEU A CD2   1 
ATOM   765   N N     . MET A  1 123 ? 9.994   33.536  166.117 1.00 30.42  ? 123 MET A N     1 
ATOM   766   C CA    . MET A  1 123 ? 10.726  33.536  164.847 1.00 34.72  ? 123 MET A CA    1 
ATOM   767   C C     . MET A  1 123 ? 10.127  34.478  163.800 1.00 41.73  ? 123 MET A C     1 
ATOM   768   O O     . MET A  1 123 ? 10.834  34.943  162.905 1.00 43.06  ? 123 MET A O     1 
ATOM   769   C CB    . MET A  1 123 ? 10.809  32.117  164.273 1.00 39.04  ? 123 MET A CB    1 
ATOM   770   C CG    . MET A  1 123 ? 9.467   31.442  164.032 1.00 39.03  ? 123 MET A CG    1 
ATOM   771   S SD    . MET A  1 123 ? 9.623   29.938  163.049 1.00 45.99  ? 123 MET A SD    1 
ATOM   772   C CE    . MET A  1 123 ? 10.080  30.641  161.470 1.00 44.57  ? 123 MET A CE    1 
ATOM   773   N N     . ASN A  1 124 ? 8.834   34.764  163.912 1.00 35.65  ? 124 ASN A N     1 
ATOM   774   C CA    . ASN A  1 124 ? 8.189   35.681  162.978 1.00 36.20  ? 124 ASN A CA    1 
ATOM   775   C C     . ASN A  1 124 ? 8.385   37.134  163.384 1.00 35.27  ? 124 ASN A C     1 
ATOM   776   O O     . ASN A  1 124 ? 7.986   38.047  162.664 1.00 36.18  ? 124 ASN A O     1 
ATOM   777   C CB    . ASN A  1 124 ? 6.699   35.368  162.851 1.00 34.15  ? 124 ASN A CB    1 
ATOM   778   C CG    . ASN A  1 124 ? 6.444   34.130  162.020 1.00 43.93  ? 124 ASN A CG    1 
ATOM   779   O OD1   . ASN A  1 124 ? 7.343   33.635  161.342 1.00 41.04  ? 124 ASN A OD1   1 
ATOM   780   N ND2   . ASN A  1 124 ? 5.218   33.623  162.064 1.00 40.94  ? 124 ASN A ND2   1 
ATOM   781   N N     . LEU A  1 125 ? 9.004   37.341  164.540 1.00 32.49  ? 125 LEU A N     1 
ATOM   782   C CA    . LEU A  1 125 ? 9.354   38.682  164.986 1.00 32.32  ? 125 LEU A CA    1 
ATOM   783   C C     . LEU A  1 125 ? 10.841  38.917  164.768 1.00 33.61  ? 125 LEU A C     1 
ATOM   784   O O     . LEU A  1 125 ? 11.612  38.983  165.722 1.00 28.70  ? 125 LEU A O     1 
ATOM   785   C CB    . LEU A  1 125 ? 8.993   38.882  166.459 1.00 30.20  ? 125 LEU A CB    1 
ATOM   786   C CG    . LEU A  1 125 ? 7.509   38.745  166.816 1.00 36.33  ? 125 LEU A CG    1 
ATOM   787   C CD1   . LEU A  1 125 ? 7.306   38.852  168.316 1.00 32.82  ? 125 LEU A CD1   1 
ATOM   788   C CD2   . LEU A  1 125 ? 6.691   39.795  166.091 1.00 30.41  ? 125 LEU A CD2   1 
ATOM   789   N N     . ASN A  1 126 ? 11.246  39.038  163.509 1.00 35.03  ? 126 ASN A N     1 
ATOM   790   C CA    . ASN A  1 126 ? 12.664  39.164  163.187 1.00 36.58  ? 126 ASN A CA    1 
ATOM   791   C C     . ASN A  1 126 ? 12.976  40.350  162.280 1.00 35.46  ? 126 ASN A C     1 
ATOM   792   O O     . ASN A  1 126 ? 13.861  40.273  161.427 1.00 41.09  ? 126 ASN A O     1 
ATOM   793   C CB    . ASN A  1 126 ? 13.163  37.878  162.534 1.00 37.57  ? 126 ASN A CB    1 
ATOM   794   C CG    . ASN A  1 126 ? 12.440  37.566  161.242 1.00 41.82  ? 126 ASN A CG    1 
ATOM   795   O OD1   . ASN A  1 126 ? 11.393  38.141  160.946 1.00 38.89  ? 126 ASN A OD1   1 
ATOM   796   N ND2   . ASN A  1 126 ? 12.995  36.644  160.464 1.00 47.61  ? 126 ASN A ND2   1 
ATOM   797   N N     . ARG A  1 127 ? 12.247  41.444  162.463 1.00 36.52  ? 127 ARG A N     1 
ATOM   798   C CA    . ARG A  1 127 ? 12.465  42.639  161.659 1.00 39.11  ? 127 ARG A CA    1 
ATOM   799   C C     . ARG A  1 127 ? 13.519  43.534  162.288 1.00 35.95  ? 127 ARG A C     1 
ATOM   800   O O     . ARG A  1 127 ? 13.529  43.732  163.501 1.00 33.43  ? 127 ARG A O     1 
ATOM   801   C CB    . ARG A  1 127 ? 11.169  43.427  161.492 1.00 38.07  ? 127 ARG A CB    1 
ATOM   802   C CG    . ARG A  1 127 ? 10.081  42.699  160.734 1.00 46.23  ? 127 ARG A CG    1 
ATOM   803   C CD    . ARG A  1 127 ? 8.764   43.445  160.862 1.00 50.15  ? 127 ARG A CD    1 
ATOM   804   N NE    . ARG A  1 127 ? 7.632   42.646  160.403 1.00 58.08  ? 127 ARG A NE    1 
ATOM   805   C CZ    . ARG A  1 127 ? 7.119   41.621  161.077 1.00 51.39  ? 127 ARG A CZ    1 
ATOM   806   N NH1   . ARG A  1 127 ? 7.645   41.255  162.239 1.00 45.24  ? 127 ARG A NH1   1 
ATOM   807   N NH2   . ARG A  1 127 ? 6.085   40.951  160.583 1.00 50.99  ? 127 ARG A NH2   1 
ATOM   808   N N     . VAL A  1 128 ? 14.402  44.078  161.459 1.00 38.98  ? 128 VAL A N     1 
ATOM   809   C CA    . VAL A  1 128 ? 15.396  45.030  161.935 1.00 36.89  ? 128 VAL A CA    1 
ATOM   810   C C     . VAL A  1 128 ? 15.188  46.379  161.263 1.00 36.03  ? 128 VAL A C     1 
ATOM   811   O O     . VAL A  1 128 ? 15.187  46.472  160.037 1.00 40.22  ? 128 VAL A O     1 
ATOM   812   C CB    . VAL A  1 128 ? 16.829  44.541  161.668 1.00 37.57  ? 128 VAL A CB    1 
ATOM   813   C CG1   . VAL A  1 128 ? 17.839  45.589  162.124 1.00 32.16  ? 128 VAL A CG1   1 
ATOM   814   C CG2   . VAL A  1 128 ? 17.076  43.215  162.366 1.00 31.66  ? 128 VAL A CG2   1 
ATOM   815   N N     . SER A  1 129 ? 14.997  47.419  162.067 1.00 33.40  ? 129 SER A N     1 
ATOM   816   C CA    . SER A  1 129 ? 14.869  48.771  161.540 1.00 39.96  ? 129 SER A CA    1 
ATOM   817   C C     . SER A  1 129 ? 16.098  49.578  161.925 1.00 36.42  ? 129 SER A C     1 
ATOM   818   O O     . SER A  1 129 ? 16.392  49.731  163.109 1.00 38.77  ? 129 SER A O     1 
ATOM   819   C CB    . SER A  1 129 ? 13.603  49.449  162.066 1.00 34.80  ? 129 SER A CB    1 
ATOM   820   O OG    . SER A  1 129 ? 12.501  48.559  162.054 1.00 53.31  ? 129 SER A OG    1 
ATOM   821   N N     . ILE A  1 130 ? 16.817  50.090  160.932 1.00 39.34  ? 130 ILE A N     1 
ATOM   822   C CA    . ILE A  1 130 ? 18.041  50.835  161.200 1.00 35.81  ? 130 ILE A CA    1 
ATOM   823   C C     . ILE A  1 130 ? 17.859  52.320  160.910 1.00 44.62  ? 130 ILE A C     1 
ATOM   824   O O     . ILE A  1 130 ? 17.313  52.704  159.874 1.00 42.35  ? 130 ILE A O     1 
ATOM   825   C CB    . ILE A  1 130 ? 19.222  50.285  160.375 1.00 35.30  ? 130 ILE A CB    1 
ATOM   826   C CG1   . ILE A  1 130 ? 19.565  48.869  160.841 1.00 36.79  ? 130 ILE A CG1   1 
ATOM   827   C CG2   . ILE A  1 130 ? 20.442  51.183  160.509 1.00 38.73  ? 130 ILE A CG2   1 
ATOM   828   C CD1   . ILE A  1 130 ? 20.493  48.128  159.920 1.00 37.97  ? 130 ILE A CD1   1 
ATOM   829   N N     . ASP A  1 131 ? 18.302  53.149  161.850 1.00 44.03  ? 131 ASP A N     1 
ATOM   830   C CA    . ASP A  1 131 ? 18.300  54.594  161.679 1.00 42.49  ? 131 ASP A CA    1 
ATOM   831   C C     . ASP A  1 131 ? 19.745  55.084  161.611 1.00 43.79  ? 131 ASP A C     1 
ATOM   832   O O     . ASP A  1 131 ? 20.420  55.215  162.633 1.00 43.44  ? 131 ASP A O     1 
ATOM   833   C CB    . ASP A  1 131 ? 17.530  55.266  162.819 1.00 48.46  ? 131 ASP A CB    1 
ATOM   834   C CG    . ASP A  1 131 ? 17.558  56.786  162.745 1.00 53.41  ? 131 ASP A CG    1 
ATOM   835   O OD1   . ASP A  1 131 ? 17.985  57.349  161.714 1.00 57.00  ? 131 ASP A OD1   1 
ATOM   836   O OD2   . ASP A  1 131 ? 17.135  57.421  163.733 1.00 55.83  ? 131 ASP A OD2   1 
ATOM   837   N N     . LEU A  1 132 ? 20.208  55.346  160.393 1.00 43.91  ? 132 LEU A N     1 
ATOM   838   C CA    . LEU A  1 132 ? 21.594  55.722  160.145 1.00 48.90  ? 132 LEU A CA    1 
ATOM   839   C C     . LEU A  1 132 ? 21.934  57.119  160.658 1.00 49.40  ? 132 LEU A C     1 
ATOM   840   O O     . LEU A  1 132 ? 23.108  57.472  160.777 1.00 53.08  ? 132 LEU A O     1 
ATOM   841   C CB    . LEU A  1 132 ? 21.897  55.636  158.647 1.00 50.20  ? 132 LEU A CB    1 
ATOM   842   C CG    . LEU A  1 132 ? 22.040  54.227  158.064 1.00 50.75  ? 132 LEU A CG    1 
ATOM   843   C CD1   . LEU A  1 132 ? 22.301  54.284  156.569 1.00 53.94  ? 132 LEU A CD1   1 
ATOM   844   C CD2   . LEU A  1 132 ? 23.157  53.484  158.773 1.00 49.33  ? 132 LEU A CD2   1 
ATOM   845   N N     . GLU A  1 133 ? 20.907  57.909  160.960 1.00 50.67  ? 133 GLU A N     1 
ATOM   846   C CA    . GLU A  1 133 ? 21.108  59.277  161.432 1.00 57.09  ? 133 GLU A CA    1 
ATOM   847   C C     . GLU A  1 133 ? 21.470  59.316  162.914 1.00 52.97  ? 133 GLU A C     1 
ATOM   848   O O     . GLU A  1 133 ? 22.355  60.067  163.321 1.00 49.22  ? 133 GLU A O     1 
ATOM   849   C CB    . GLU A  1 133 ? 19.861  60.123  161.171 1.00 56.77  ? 133 GLU A CB    1 
ATOM   850   C CG    . GLU A  1 133 ? 19.556  60.326  159.696 1.00 66.03  ? 133 GLU A CG    1 
ATOM   851   C CD    . GLU A  1 133 ? 20.674  61.049  158.966 1.00 77.72  ? 133 GLU A CD    1 
ATOM   852   O OE1   . GLU A  1 133 ? 21.186  60.503  157.965 1.00 75.59  ? 133 GLU A OE1   1 
ATOM   853   O OE2   . GLU A  1 133 ? 21.035  62.169  159.388 1.00 81.27  ? 133 GLU A OE2   1 
ATOM   854   N N     . SER A  1 134 ? 20.784  58.512  163.720 1.00 51.48  ? 134 SER A N     1 
ATOM   855   C CA    . SER A  1 134 ? 21.093  58.428  165.143 1.00 46.98  ? 134 SER A CA    1 
ATOM   856   C C     . SER A  1 134 ? 22.040  57.265  165.412 1.00 43.64  ? 134 SER A C     1 
ATOM   857   O O     . SER A  1 134 ? 22.540  57.101  166.528 1.00 38.42  ? 134 SER A O     1 
ATOM   858   C CB    . SER A  1 134 ? 19.812  58.278  165.967 1.00 46.55  ? 134 SER A CB    1 
ATOM   859   O OG    . SER A  1 134 ? 18.976  57.261  165.443 1.00 51.50  ? 134 SER A OG    1 
ATOM   860   N N     . GLU A  1 135 ? 22.288  56.479  164.365 1.00 39.69  ? 135 GLU A N     1 
ATOM   861   C CA    . GLU A  1 135 ? 23.107  55.272  164.441 1.00 43.28  ? 135 GLU A CA    1 
ATOM   862   C C     . GLU A  1 135 ? 22.591  54.344  165.532 1.00 40.76  ? 135 GLU A C     1 
ATOM   863   O O     . GLU A  1 135 ? 23.345  53.865  166.380 1.00 38.10  ? 135 GLU A O     1 
ATOM   864   C CB    . GLU A  1 135 ? 24.577  55.626  164.662 1.00 43.12  ? 135 GLU A CB    1 
ATOM   865   C CG    . GLU A  1 135 ? 25.232  56.192  163.411 1.00 43.97  ? 135 GLU A CG    1 
ATOM   866   C CD    . GLU A  1 135 ? 26.663  56.628  163.634 1.00 51.25  ? 135 GLU A CD    1 
ATOM   867   O OE1   . GLU A  1 135 ? 27.072  56.759  164.807 1.00 53.06  ? 135 GLU A OE1   1 
ATOM   868   O OE2   . GLU A  1 135 ? 27.380  56.840  162.633 1.00 51.78  ? 135 GLU A OE2   1 
ATOM   869   N N     . THR A  1 136 ? 21.284  54.112  165.497 1.00 37.19  ? 136 THR A N     1 
ATOM   870   C CA    . THR A  1 136 ? 20.633  53.157  166.378 1.00 33.25  ? 136 THR A CA    1 
ATOM   871   C C     . THR A  1 136 ? 19.862  52.155  165.532 1.00 36.63  ? 136 THR A C     1 
ATOM   872   O O     . THR A  1 136 ? 19.772  52.303  164.315 1.00 37.27  ? 136 THR A O     1 
ATOM   873   C CB    . THR A  1 136 ? 19.669  53.840  167.361 1.00 35.55  ? 136 THR A CB    1 
ATOM   874   O OG1   . THR A  1 136 ? 18.695  54.595  166.629 1.00 37.79  ? 136 THR A OG1   1 
ATOM   875   C CG2   . THR A  1 136 ? 20.428  54.771  168.294 1.00 33.43  ? 136 THR A CG2   1 
ATOM   876   N N     . ALA A  1 137 ? 19.306  51.136  166.174 1.00 35.26  ? 137 ALA A N     1 
ATOM   877   C CA    . ALA A  1 137 ? 18.496  50.158  165.462 1.00 35.67  ? 137 ALA A CA    1 
ATOM   878   C C     . ALA A  1 137 ? 17.464  49.521  166.379 1.00 35.06  ? 137 ALA A C     1 
ATOM   879   O O     . ALA A  1 137 ? 17.751  49.214  167.535 1.00 36.92  ? 137 ALA A O     1 
ATOM   880   C CB    . ALA A  1 137 ? 19.379  49.089  164.841 1.00 35.23  ? 137 ALA A CB    1 
ATOM   881   N N     . TRP A  1 138 ? 16.257  49.331  165.860 1.00 33.77  ? 138 TRP A N     1 
ATOM   882   C CA    . TRP A  1 138 ? 15.251  48.564  166.577 1.00 30.77  ? 138 TRP A CA    1 
ATOM   883   C C     . TRP A  1 138 ? 15.300  47.122  166.098 1.00 34.59  ? 138 TRP A C     1 
ATOM   884   O O     . TRP A  1 138 ? 15.242  46.855  164.898 1.00 37.33  ? 138 TRP A O     1 
ATOM   885   C CB    . TRP A  1 138 ? 13.856  49.155  166.385 1.00 38.50  ? 138 TRP A CB    1 
ATOM   886   C CG    . TRP A  1 138 ? 13.549  50.257  167.349 1.00 33.21  ? 138 TRP A CG    1 
ATOM   887   C CD1   . TRP A  1 138 ? 13.567  51.597  167.095 1.00 36.84  ? 138 TRP A CD1   1 
ATOM   888   C CD2   . TRP A  1 138 ? 13.191  50.115  168.730 1.00 32.81  ? 138 TRP A CD2   1 
ATOM   889   N NE1   . TRP A  1 138 ? 13.239  52.298  168.230 1.00 31.89  ? 138 TRP A NE1   1 
ATOM   890   C CE2   . TRP A  1 138 ? 13.004  51.412  169.248 1.00 31.12  ? 138 TRP A CE2   1 
ATOM   891   C CE3   . TRP A  1 138 ? 13.012  49.017  169.578 1.00 33.15  ? 138 TRP A CE3   1 
ATOM   892   C CZ2   . TRP A  1 138 ? 12.643  51.641  170.575 1.00 34.06  ? 138 TRP A CZ2   1 
ATOM   893   C CZ3   . TRP A  1 138 ? 12.654  49.247  170.897 1.00 32.84  ? 138 TRP A CZ3   1 
ATOM   894   C CH2   . TRP A  1 138 ? 12.470  50.549  171.381 1.00 32.65  ? 138 TRP A CH2   1 
ATOM   895   N N     . VAL A  1 139 ? 15.423  46.198  167.043 1.00 31.06  ? 139 VAL A N     1 
ATOM   896   C CA    . VAL A  1 139 ? 15.618  44.790  166.727 1.00 29.45  ? 139 VAL A CA    1 
ATOM   897   C C     . VAL A  1 139 ? 14.565  43.923  167.404 1.00 28.83  ? 139 VAL A C     1 
ATOM   898   O O     . VAL A  1 139 ? 14.577  43.774  168.625 1.00 29.24  ? 139 VAL A O     1 
ATOM   899   C CB    . VAL A  1 139 ? 17.015  44.312  167.164 1.00 30.32  ? 139 VAL A CB    1 
ATOM   900   C CG1   . VAL A  1 139 ? 17.236  42.858  166.766 1.00 28.53  ? 139 VAL A CG1   1 
ATOM   901   C CG2   . VAL A  1 139 ? 18.088  45.203  166.570 1.00 31.24  ? 139 VAL A CG2   1 
ATOM   902   N N     . GLU A  1 140 ? 13.656  43.357  166.615 1.00 32.77  ? 140 GLU A N     1 
ATOM   903   C CA    . GLU A  1 140 ? 12.645  42.457  167.159 1.00 33.01  ? 140 GLU A CA    1 
ATOM   904   C C     . GLU A  1 140 ? 13.332  41.231  167.750 1.00 30.19  ? 140 GLU A C     1 
ATOM   905   O O     . GLU A  1 140 ? 14.327  40.750  167.212 1.00 28.82  ? 140 GLU A O     1 
ATOM   906   C CB    . GLU A  1 140 ? 11.628  42.064  166.086 1.00 33.69  ? 140 GLU A CB    1 
ATOM   907   C CG    . GLU A  1 140 ? 10.699  43.203  165.692 1.00 31.24  ? 140 GLU A CG    1 
ATOM   908   C CD    . GLU A  1 140 ? 9.607   42.784  164.722 1.00 38.71  ? 140 GLU A CD    1 
ATOM   909   O OE1   . GLU A  1 140 ? 9.784   41.764  164.025 1.00 34.23  ? 140 GLU A OE1   1 
ATOM   910   O OE2   . GLU A  1 140 ? 8.572   43.481  164.662 1.00 32.87  ? 140 GLU A OE2   1 
ATOM   911   N N     . SER A  1 141 ? 12.804  40.740  168.866 1.00 28.12  ? 141 SER A N     1 
ATOM   912   C CA    . SER A  1 141 ? 13.528  39.781  169.697 1.00 30.00  ? 141 SER A CA    1 
ATOM   913   C C     . SER A  1 141 ? 13.642  38.379  169.109 1.00 32.17  ? 141 SER A C     1 
ATOM   914   O O     . SER A  1 141 ? 14.310  37.522  169.682 1.00 35.48  ? 141 SER A O     1 
ATOM   915   C CB    . SER A  1 141 ? 12.875  39.690  171.071 1.00 31.48  ? 141 SER A CB    1 
ATOM   916   O OG    . SER A  1 141 ? 11.543  39.211  170.980 1.00 32.59  ? 141 SER A OG    1 
ATOM   917   N N     . GLY A  1 142 ? 12.987  38.141  167.978 1.00 33.86  ? 142 GLY A N     1 
ATOM   918   C CA    . GLY A  1 142 ? 13.115  36.868  167.292 1.00 35.41  ? 142 GLY A CA    1 
ATOM   919   C C     . GLY A  1 142 ? 14.291  36.878  166.335 1.00 34.21  ? 142 GLY A C     1 
ATOM   920   O O     . GLY A  1 142 ? 14.711  35.834  165.831 1.00 34.71  ? 142 GLY A O     1 
ATOM   921   N N     . SER A  1 143 ? 14.819  38.073  166.087 1.00 31.18  ? 143 SER A N     1 
ATOM   922   C CA    . SER A  1 143 ? 15.985  38.239  165.231 1.00 33.93  ? 143 SER A CA    1 
ATOM   923   C C     . SER A  1 143 ? 17.174  37.482  165.787 1.00 31.23  ? 143 SER A C     1 
ATOM   924   O O     . SER A  1 143 ? 17.441  37.526  166.988 1.00 31.84  ? 143 SER A O     1 
ATOM   925   C CB    . SER A  1 143 ? 16.352  39.715  165.083 1.00 34.04  ? 143 SER A CB    1 
ATOM   926   O OG    . SER A  1 143 ? 15.229  40.492  164.706 1.00 31.73  ? 143 SER A OG    1 
ATOM   927   N N     . THR A  1 144 ? 17.883  36.781  164.910 1.00 33.70  ? 144 THR A N     1 
ATOM   928   C CA    . THR A  1 144 ? 19.134  36.147  165.292 1.00 32.01  ? 144 THR A CA    1 
ATOM   929   C C     . THR A  1 144 ? 20.261  37.157  165.141 1.00 31.19  ? 144 THR A C     1 
ATOM   930   O O     . THR A  1 144 ? 20.088  38.195  164.497 1.00 30.77  ? 144 THR A O     1 
ATOM   931   C CB    . THR A  1 144 ? 19.438  34.901  164.436 1.00 35.97  ? 144 THR A CB    1 
ATOM   932   O OG1   . THR A  1 144 ? 19.574  35.281  163.059 1.00 35.96  ? 144 THR A OG1   1 
ATOM   933   C CG2   . THR A  1 144 ? 18.325  33.876  164.573 1.00 33.56  ? 144 THR A CG2   1 
ATOM   934   N N     . LEU A  1 145 ? 21.407  36.855  165.745 1.00 36.31  ? 145 LEU A N     1 
ATOM   935   C CA    . LEU A  1 145 ? 22.578  37.717  165.641 1.00 34.47  ? 145 LEU A CA    1 
ATOM   936   C C     . LEU A  1 145 ? 22.999  37.865  164.187 1.00 34.70  ? 145 LEU A C     1 
ATOM   937   O O     . LEU A  1 145 ? 23.374  38.951  163.748 1.00 34.92  ? 145 LEU A O     1 
ATOM   938   C CB    . LEU A  1 145 ? 23.735  37.163  166.473 1.00 34.77  ? 145 LEU A CB    1 
ATOM   939   C CG    . LEU A  1 145 ? 23.463  37.006  167.969 1.00 35.79  ? 145 LEU A CG    1 
ATOM   940   C CD1   . LEU A  1 145 ? 24.687  36.463  168.667 1.00 32.51  ? 145 LEU A CD1   1 
ATOM   941   C CD2   . LEU A  1 145 ? 23.031  38.322  168.593 1.00 32.85  ? 145 LEU A CD2   1 
ATOM   942   N N     . GLY A  1 146 ? 22.923  36.765  163.445 1.00 32.53  ? 146 GLY A N     1 
ATOM   943   C CA    . GLY A  1 146 ? 23.275  36.756  162.037 1.00 34.89  ? 146 GLY A CA    1 
ATOM   944   C C     . GLY A  1 146 ? 22.355  37.627  161.202 1.00 37.43  ? 146 GLY A C     1 
ATOM   945   O O     . GLY A  1 146 ? 22.813  38.376  160.339 1.00 36.34  ? 146 GLY A O     1 
ATOM   946   N N     . GLU A  1 147 ? 21.052  37.512  161.450 1.00 35.38  ? 147 GLU A N     1 
ATOM   947   C CA    . GLU A  1 147 ? 20.061  38.354  160.791 1.00 37.72  ? 147 GLU A CA    1 
ATOM   948   C C     . GLU A  1 147 ? 20.336  39.823  161.078 1.00 34.33  ? 147 GLU A C     1 
ATOM   949   O O     . GLU A  1 147 ? 20.184  40.671  160.202 1.00 40.36  ? 147 GLU A O     1 
ATOM   950   C CB    . GLU A  1 147 ? 18.646  37.984  161.245 1.00 36.09  ? 147 GLU A CB    1 
ATOM   951   C CG    . GLU A  1 147 ? 18.092  36.715  160.623 1.00 39.53  ? 147 GLU A CG    1 
ATOM   952   C CD    . GLU A  1 147 ? 16.740  36.334  161.196 1.00 39.88  ? 147 GLU A CD    1 
ATOM   953   O OE1   . GLU A  1 147 ? 16.391  36.844  162.281 1.00 39.28  ? 147 GLU A OE1   1 
ATOM   954   O OE2   . GLU A  1 147 ? 16.029  35.523  160.567 1.00 45.76  ? 147 GLU A OE2   1 
ATOM   955   N N     . LEU A  1 148 ? 20.744  40.111  162.311 1.00 34.93  ? 148 LEU A N     1 
ATOM   956   C CA    . LEU A  1 148 ? 21.078  41.472  162.725 1.00 38.97  ? 148 LEU A CA    1 
ATOM   957   C C     . LEU A  1 148 ? 22.335  41.986  162.031 1.00 34.10  ? 148 LEU A C     1 
ATOM   958   O O     . LEU A  1 148 ? 22.347  43.101  161.508 1.00 36.81  ? 148 LEU A O     1 
ATOM   959   C CB    . LEU A  1 148 ? 21.261  41.543  164.244 1.00 32.00  ? 148 LEU A CB    1 
ATOM   960   C CG    . LEU A  1 148 ? 21.762  42.879  164.796 1.00 34.76  ? 148 LEU A CG    1 
ATOM   961   C CD1   . LEU A  1 148 ? 20.844  44.017  164.362 1.00 30.42  ? 148 LEU A CD1   1 
ATOM   962   C CD2   . LEU A  1 148 ? 21.889  42.830  166.315 1.00 32.77  ? 148 LEU A CD2   1 
ATOM   963   N N     . TYR A  1 149 ? 23.390  41.174  162.046 1.00 35.64  ? 149 TYR A N     1 
ATOM   964   C CA    . TYR A  1 149 ? 24.653  41.529  161.402 1.00 36.56  ? 149 TYR A CA    1 
ATOM   965   C C     . TYR A  1 149 ? 24.435  41.822  159.927 1.00 36.65  ? 149 TYR A C     1 
ATOM   966   O O     . TYR A  1 149 ? 24.916  42.827  159.406 1.00 37.13  ? 149 TYR A O     1 
ATOM   967   C CB    . TYR A  1 149 ? 25.683  40.406  161.550 1.00 36.99  ? 149 TYR A CB    1 
ATOM   968   C CG    . TYR A  1 149 ? 26.062  40.084  162.974 1.00 35.86  ? 149 TYR A CG    1 
ATOM   969   C CD1   . TYR A  1 149 ? 25.969  41.042  163.974 1.00 37.02  ? 149 TYR A CD1   1 
ATOM   970   C CD2   . TYR A  1 149 ? 26.512  38.817  163.318 1.00 38.45  ? 149 TYR A CD2   1 
ATOM   971   C CE1   . TYR A  1 149 ? 26.315  40.746  165.277 1.00 34.21  ? 149 TYR A CE1   1 
ATOM   972   C CE2   . TYR A  1 149 ? 26.860  38.511  164.612 1.00 38.75  ? 149 TYR A CE2   1 
ATOM   973   C CZ    . TYR A  1 149 ? 26.761  39.476  165.587 1.00 38.16  ? 149 TYR A CZ    1 
ATOM   974   O OH    . TYR A  1 149 ? 27.109  39.161  166.877 1.00 37.05  ? 149 TYR A OH    1 
ATOM   975   N N     . TYR A  1 150 ? 23.701  40.932  159.265 1.00 42.26  ? 150 TYR A N     1 
ATOM   976   C CA    . TYR A  1 150 ? 23.400  41.074  157.847 1.00 45.23  ? 150 TYR A CA    1 
ATOM   977   C C     . TYR A  1 150 ? 22.673  42.378  157.554 1.00 41.25  ? 150 TYR A C     1 
ATOM   978   O O     . TYR A  1 150 ? 22.992  43.072  156.590 1.00 45.90  ? 150 TYR A O     1 
ATOM   979   C CB    . TYR A  1 150 ? 22.557  39.896  157.356 1.00 45.39  ? 150 TYR A CB    1 
ATOM   980   C CG    . TYR A  1 150 ? 22.092  40.047  155.927 1.00 48.94  ? 150 TYR A CG    1 
ATOM   981   C CD1   . TYR A  1 150 ? 22.943  39.762  154.869 1.00 51.68  ? 150 TYR A CD1   1 
ATOM   982   C CD2   . TYR A  1 150 ? 20.804  40.482  155.633 1.00 47.38  ? 150 TYR A CD2   1 
ATOM   983   C CE1   . TYR A  1 150 ? 22.529  39.902  153.560 1.00 53.55  ? 150 TYR A CE1   1 
ATOM   984   C CE2   . TYR A  1 150 ? 20.380  40.626  154.326 1.00 51.89  ? 150 TYR A CE2   1 
ATOM   985   C CZ    . TYR A  1 150 ? 21.247  40.334  153.294 1.00 57.72  ? 150 TYR A CZ    1 
ATOM   986   O OH    . TYR A  1 150 ? 20.832  40.473  151.989 1.00 66.76  ? 150 TYR A OH    1 
ATOM   987   N N     . ALA A  1 151 ? 21.695  42.698  158.392 1.00 38.79  ? 151 ALA A N     1 
ATOM   988   C CA    . ALA A  1 151 ? 20.888  43.894  158.206 1.00 43.38  ? 151 ALA A CA    1 
ATOM   989   C C     . ALA A  1 151 ? 21.730  45.161  158.341 1.00 44.48  ? 151 ALA A C     1 
ATOM   990   O O     . ALA A  1 151 ? 21.506  46.144  157.636 1.00 41.06  ? 151 ALA A O     1 
ATOM   991   C CB    . ALA A  1 151 ? 19.733  43.908  159.201 1.00 37.11  ? 151 ALA A CB    1 
ATOM   992   N N     . ILE A  1 152 ? 22.710  45.127  159.238 1.00 44.06  ? 152 ILE A N     1 
ATOM   993   C CA    . ILE A  1 152 ? 23.570  46.284  159.472 1.00 43.35  ? 152 ILE A CA    1 
ATOM   994   C C     . ILE A  1 152 ? 24.468  46.561  158.263 1.00 40.43  ? 152 ILE A C     1 
ATOM   995   O O     . ILE A  1 152 ? 24.598  47.706  157.830 1.00 41.04  ? 152 ILE A O     1 
ATOM   996   C CB    . ILE A  1 152 ? 24.435  46.092  160.735 1.00 45.50  ? 152 ILE A CB    1 
ATOM   997   C CG1   . ILE A  1 152 ? 23.556  46.085  161.992 1.00 38.28  ? 152 ILE A CG1   1 
ATOM   998   C CG2   . ILE A  1 152 ? 25.478  47.187  160.837 1.00 37.78  ? 152 ILE A CG2   1 
ATOM   999   C CD1   . ILE A  1 152 ? 24.274  45.605  163.242 1.00 33.07  ? 152 ILE A CD1   1 
ATOM   1000  N N     . THR A  1 153 ? 25.064  45.506  157.713 1.00 44.51  ? 153 THR A N     1 
ATOM   1001  C CA    . THR A  1 153 ? 25.937  45.622  156.543 1.00 47.43  ? 153 THR A CA    1 
ATOM   1002  C C     . THR A  1 153 ? 25.200  46.208  155.343 1.00 47.79  ? 153 THR A C     1 
ATOM   1003  O O     . THR A  1 153 ? 25.734  47.053  154.625 1.00 55.22  ? 153 THR A O     1 
ATOM   1004  C CB    . THR A  1 153 ? 26.531  44.260  156.136 1.00 45.89  ? 153 THR A CB    1 
ATOM   1005  O OG1   . THR A  1 153 ? 25.479  43.376  155.739 1.00 51.51  ? 153 THR A OG1   1 
ATOM   1006  C CG2   . THR A  1 153 ? 27.303  43.642  157.290 1.00 44.55  ? 153 THR A CG2   1 
ATOM   1007  N N     . GLU A  1 154 ? 23.966  45.754  155.139 1.00 52.49  ? 154 GLU A N     1 
ATOM   1008  C CA    . GLU A  1 154 ? 23.128  46.204  154.026 1.00 49.44  ? 154 GLU A CA    1 
ATOM   1009  C C     . GLU A  1 154 ? 22.719  47.675  154.141 1.00 53.55  ? 154 GLU A C     1 
ATOM   1010  O O     . GLU A  1 154 ? 22.080  48.222  153.241 1.00 61.59  ? 154 GLU A O     1 
ATOM   1011  C CB    . GLU A  1 154 ? 21.872  45.328  153.924 1.00 55.33  ? 154 GLU A CB    1 
ATOM   1012  C CG    . GLU A  1 154 ? 22.139  43.862  153.578 1.00 55.05  ? 154 GLU A CG    1 
ATOM   1013  C CD    . GLU A  1 154 ? 22.413  43.645  152.101 1.00 61.93  ? 154 GLU A CD    1 
ATOM   1014  O OE1   . GLU A  1 154 ? 21.660  44.193  151.266 1.00 69.74  ? 154 GLU A OE1   1 
ATOM   1015  O OE2   . GLU A  1 154 ? 23.374  42.917  151.774 1.00 66.34  ? 154 GLU A OE2   1 
ATOM   1016  N N     . SER A  1 155 ? 23.080  48.306  155.255 1.00 46.10  ? 155 SER A N     1 
ATOM   1017  C CA    . SER A  1 155 ? 22.750  49.709  155.501 1.00 54.59  ? 155 SER A CA    1 
ATOM   1018  C C     . SER A  1 155 ? 23.999  50.584  155.598 1.00 54.02  ? 155 SER A C     1 
ATOM   1019  O O     . SER A  1 155 ? 23.960  51.772  155.274 1.00 54.76  ? 155 SER A O     1 
ATOM   1020  C CB    . SER A  1 155 ? 21.928  49.851  156.788 1.00 51.33  ? 155 SER A CB    1 
ATOM   1021  O OG    . SER A  1 155 ? 20.554  50.029  156.507 1.00 67.15  ? 155 SER A OG    1 
ATOM   1022  N N     . SER A  1 156 ? 25.101  49.992  156.048 1.00 51.02  ? 156 SER A N     1 
ATOM   1023  C CA    . SER A  1 156 ? 26.338  50.734  156.257 1.00 48.49  ? 156 SER A CA    1 
ATOM   1024  C C     . SER A  1 156 ? 27.541  49.798  156.312 1.00 50.30  ? 156 SER A C     1 
ATOM   1025  O O     . SER A  1 156 ? 27.421  48.645  156.724 1.00 46.85  ? 156 SER A O     1 
ATOM   1026  C CB    . SER A  1 156 ? 26.254  51.562  157.545 1.00 49.45  ? 156 SER A CB    1 
ATOM   1027  O OG    . SER A  1 156 ? 27.533  52.045  157.929 1.00 50.40  ? 156 SER A OG    1 
ATOM   1028  N N     . SER A  1 157 ? 28.697  50.303  155.891 1.00 49.62  ? 157 SER A N     1 
ATOM   1029  C CA    . SER A  1 157 ? 29.940  49.549  155.974 1.00 52.36  ? 157 SER A CA    1 
ATOM   1030  C C     . SER A  1 157 ? 30.810  50.100  157.093 1.00 49.47  ? 157 SER A C     1 
ATOM   1031  O O     . SER A  1 157 ? 31.877  49.561  157.388 1.00 55.71  ? 157 SER A O     1 
ATOM   1032  C CB    . SER A  1 157 ? 30.700  49.595  154.648 1.00 55.34  ? 157 SER A CB    1 
ATOM   1033  O OG    . SER A  1 157 ? 30.891  50.933  154.216 1.00 59.70  ? 157 SER A OG    1 
ATOM   1034  N N     . LYS A  1 158 ? 30.351  51.187  157.704 1.00 55.45  ? 158 LYS A N     1 
ATOM   1035  C CA    . LYS A  1 158 ? 31.100  51.829  158.775 1.00 55.85  ? 158 LYS A CA    1 
ATOM   1036  C C     . LYS A  1 158 ? 30.492  51.543  160.144 1.00 55.41  ? 158 LYS A C     1 
ATOM   1037  O O     . LYS A  1 158 ? 30.928  52.105  161.147 1.00 50.39  ? 158 LYS A O     1 
ATOM   1038  C CB    . LYS A  1 158 ? 31.164  53.339  158.557 1.00 64.24  ? 158 LYS A CB    1 
ATOM   1039  C CG    . LYS A  1 158 ? 31.756  53.788  157.233 1.00 70.18  ? 158 LYS A CG    1 
ATOM   1040  C CD    . LYS A  1 158 ? 31.496  55.276  157.042 1.00 78.54  ? 158 LYS A CD    1 
ATOM   1041  C CE    . LYS A  1 158 ? 32.054  55.796  155.731 1.00 86.53  ? 158 LYS A CE    1 
ATOM   1042  N NZ    . LYS A  1 158 ? 31.636  54.964  154.571 1.00 84.88  ? 158 LYS A NZ    1 
ATOM   1043  N N     . LEU A  1 159 ? 29.486  50.676  160.186 1.00 52.26  ? 159 LEU A N     1 
ATOM   1044  C CA    . LEU A  1 159 ? 28.805  50.371  161.439 1.00 42.25  ? 159 LEU A CA    1 
ATOM   1045  C C     . LEU A  1 159 ? 28.744  48.871  161.702 1.00 39.72  ? 159 LEU A C     1 
ATOM   1046  O O     . LEU A  1 159 ? 28.684  48.069  160.773 1.00 38.76  ? 159 LEU A O     1 
ATOM   1047  C CB    . LEU A  1 159 ? 27.394  50.961  161.434 1.00 44.09  ? 159 LEU A CB    1 
ATOM   1048  C CG    . LEU A  1 159 ? 27.308  52.489  161.425 1.00 47.52  ? 159 LEU A CG    1 
ATOM   1049  C CD1   . LEU A  1 159 ? 25.870  52.938  161.204 1.00 43.62  ? 159 LEU A CD1   1 
ATOM   1050  C CD2   . LEU A  1 159 ? 27.867  53.071  162.718 1.00 39.81  ? 159 LEU A CD2   1 
ATOM   1051  N N     . GLY A  1 160 ? 28.773  48.505  162.979 1.00 41.29  ? 160 GLY A N     1 
ATOM   1052  C CA    . GLY A  1 160 ? 28.677  47.118  163.388 1.00 34.83  ? 160 GLY A CA    1 
ATOM   1053  C C     . GLY A  1 160 ? 28.045  47.016  164.761 1.00 36.76  ? 160 GLY A C     1 
ATOM   1054  O O     . GLY A  1 160 ? 27.495  47.994  165.270 1.00 36.09  ? 160 GLY A O     1 
ATOM   1055  N N     . PHE A  1 161 ? 28.116  45.836  165.365 1.00 42.07  ? 161 PHE A N     1 
ATOM   1056  C CA    . PHE A  1 161 ? 27.564  45.644  166.701 1.00 42.56  ? 161 PHE A CA    1 
ATOM   1057  C C     . PHE A  1 161 ? 28.282  44.518  167.433 1.00 39.34  ? 161 PHE A C     1 
ATOM   1058  O O     . PHE A  1 161 ? 28.727  43.553  166.812 1.00 42.49  ? 161 PHE A O     1 
ATOM   1059  C CB    . PHE A  1 161 ? 26.065  45.356  166.623 1.00 34.38  ? 161 PHE A CB    1 
ATOM   1060  C CG    . PHE A  1 161 ? 25.391  45.305  167.961 1.00 30.73  ? 161 PHE A CG    1 
ATOM   1061  C CD1   . PHE A  1 161 ? 25.175  46.465  168.686 1.00 30.97  ? 161 PHE A CD1   1 
ATOM   1062  C CD2   . PHE A  1 161 ? 24.972  44.098  168.494 1.00 32.70  ? 161 PHE A CD2   1 
ATOM   1063  C CE1   . PHE A  1 161 ? 24.555  46.423  169.921 1.00 31.97  ? 161 PHE A CE1   1 
ATOM   1064  C CE2   . PHE A  1 161 ? 24.349  44.049  169.728 1.00 30.85  ? 161 PHE A CE2   1 
ATOM   1065  C CZ    . PHE A  1 161 ? 24.138  45.215  170.442 1.00 32.90  ? 161 PHE A CZ    1 
ATOM   1066  N N     . THR A  1 162 ? 28.403  44.649  168.752 1.00 41.27  ? 162 THR A N     1 
ATOM   1067  C CA    . THR A  1 162 ? 29.142  43.668  169.536 1.00 41.41  ? 162 THR A CA    1 
ATOM   1068  C C     . THR A  1 162 ? 28.226  42.595  170.120 1.00 44.06  ? 162 THR A C     1 
ATOM   1069  O O     . THR A  1 162 ? 27.330  42.878  170.916 1.00 44.38  ? 162 THR A O     1 
ATOM   1070  C CB    . THR A  1 162 ? 29.951  44.340  170.676 1.00 41.01  ? 162 THR A CB    1 
ATOM   1071  O OG1   . THR A  1 162 ? 30.492  43.333  171.540 1.00 43.41  ? 162 THR A OG1   1 
ATOM   1072  C CG2   . THR A  1 162 ? 29.085  45.276  171.494 1.00 34.24  ? 162 THR A CG2   1 
ATOM   1073  N N     . ALA A  1 163 ? 28.459  41.358  169.691 1.00 38.23  ? 163 ALA A N     1 
ATOM   1074  C CA    . ALA A  1 163 ? 27.749  40.193  170.204 1.00 41.97  ? 163 ALA A CA    1 
ATOM   1075  C C     . ALA A  1 163 ? 28.462  38.917  169.754 1.00 42.16  ? 163 ALA A C     1 
ATOM   1076  O O     . ALA A  1 163 ? 29.493  38.977  169.082 1.00 42.70  ? 163 ALA A O     1 
ATOM   1077  C CB    . ALA A  1 163 ? 26.292  40.198  169.743 1.00 37.11  ? 163 ALA A CB    1 
ATOM   1078  N N     . ALA A  1 164 ? 27.904  37.771  170.136 1.00 45.01  ? 164 ALA A N     1 
ATOM   1079  C CA    . ALA A  1 164 ? 28.491  36.461  169.859 1.00 40.92  ? 164 ALA A CA    1 
ATOM   1080  C C     . ALA A  1 164 ? 28.804  36.220  168.385 1.00 47.43  ? 164 ALA A C     1 
ATOM   1081  O O     . ALA A  1 164 ? 28.301  36.919  167.504 1.00 52.38  ? 164 ALA A O     1 
ATOM   1082  C CB    . ALA A  1 164 ? 27.567  35.372  170.363 1.00 42.09  ? 164 ALA A CB    1 
ATOM   1083  N N     . TRP A  1 165 ? 29.632  35.212  168.130 1.00 46.29  ? 165 TRP A N     1 
ATOM   1084  C CA    . TRP A  1 165 ? 29.973  34.826  166.768 1.00 49.49  ? 165 TRP A CA    1 
ATOM   1085  C C     . TRP A  1 165 ? 28.938  33.858  166.197 1.00 52.51  ? 165 TRP A C     1 
ATOM   1086  O O     . TRP A  1 165 ? 28.769  33.770  164.983 1.00 53.36  ? 165 TRP A O     1 
ATOM   1087  C CB    . TRP A  1 165 ? 31.368  34.196  166.716 1.00 47.01  ? 165 TRP A CB    1 
ATOM   1088  C CG    . TRP A  1 165 ? 31.515  32.955  167.552 1.00 56.57  ? 165 TRP A CG    1 
ATOM   1089  C CD1   . TRP A  1 165 ? 32.016  32.876  168.820 1.00 58.47  ? 165 TRP A CD1   1 
ATOM   1090  C CD2   . TRP A  1 165 ? 31.159  31.616  167.179 1.00 65.56  ? 165 TRP A CD2   1 
ATOM   1091  N NE1   . TRP A  1 165 ? 31.994  31.575  169.260 1.00 59.96  ? 165 TRP A NE1   1 
ATOM   1092  C CE2   . TRP A  1 165 ? 31.472  30.781  168.272 1.00 68.85  ? 165 TRP A CE2   1 
ATOM   1093  C CE3   . TRP A  1 165 ? 30.606  31.042  166.028 1.00 58.03  ? 165 TRP A CE3   1 
ATOM   1094  C CZ2   . TRP A  1 165 ? 31.252  29.403  168.248 1.00 66.98  ? 165 TRP A CZ2   1 
ATOM   1095  C CZ3   . TRP A  1 165 ? 30.387  29.675  166.007 1.00 60.12  ? 165 TRP A CZ3   1 
ATOM   1096  C CH2   . TRP A  1 165 ? 30.709  28.871  167.110 1.00 62.45  ? 165 TRP A CH2   1 
ATOM   1097  N N     . CYS A  1 166 ? 28.261  33.129  167.083 1.00 49.74  ? 166 CYS A N     1 
ATOM   1098  C CA    . CYS A  1 166 ? 27.210  32.192  166.692 1.00 46.21  ? 166 CYS A CA    1 
ATOM   1099  C C     . CYS A  1 166 ? 26.039  32.935  166.052 1.00 43.11  ? 166 CYS A C     1 
ATOM   1100  O O     . CYS A  1 166 ? 25.294  33.632  166.740 1.00 43.88  ? 166 CYS A O     1 
ATOM   1101  C CB    . CYS A  1 166 ? 26.720  31.395  167.903 1.00 47.21  ? 166 CYS A CB    1 
ATOM   1102  S SG    . CYS A  1 166 ? 27.983  30.449  168.802 1.00 50.61  ? 166 CYS A SG    1 
ATOM   1103  N N     . PRO A  1 167 ? 25.864  32.782  164.729 1.00 42.78  ? 167 PRO A N     1 
ATOM   1104  C CA    . PRO A  1 167 ? 24.877  33.586  163.996 1.00 41.83  ? 167 PRO A CA    1 
ATOM   1105  C C     . PRO A  1 167 ? 23.420  33.187  164.241 1.00 40.40  ? 167 PRO A C     1 
ATOM   1106  O O     . PRO A  1 167 ? 22.529  33.995  163.983 1.00 37.81  ? 167 PRO A O     1 
ATOM   1107  C CB    . PRO A  1 167 ? 25.242  33.340  162.523 1.00 44.55  ? 167 PRO A CB    1 
ATOM   1108  C CG    . PRO A  1 167 ? 26.567  32.633  162.539 1.00 45.96  ? 167 PRO A CG    1 
ATOM   1109  C CD    . PRO A  1 167 ? 26.612  31.892  163.829 1.00 45.21  ? 167 PRO A CD    1 
ATOM   1110  N N     . THR A  1 168 ? 23.178  31.968  164.713 1.00 40.23  ? 168 THR A N     1 
ATOM   1111  C CA    . THR A  1 168 ? 21.809  31.491  164.889 1.00 42.16  ? 168 THR A CA    1 
ATOM   1112  C C     . THR A  1 168 ? 21.304  31.732  166.307 1.00 37.97  ? 168 THR A C     1 
ATOM   1113  O O     . THR A  1 168 ? 20.168  31.395  166.633 1.00 37.16  ? 168 THR A O     1 
ATOM   1114  C CB    . THR A  1 168 ? 21.679  29.994  164.555 1.00 36.26  ? 168 THR A CB    1 
ATOM   1115  O OG1   . THR A  1 168 ? 22.511  29.230  165.434 1.00 41.48  ? 168 THR A OG1   1 
ATOM   1116  C CG2   . THR A  1 168 ? 22.084  29.728  163.115 1.00 42.51  ? 168 THR A CG2   1 
ATOM   1117  N N     . VAL A  1 169 ? 22.157  32.308  167.148 1.00 32.55  ? 169 VAL A N     1 
ATOM   1118  C CA    . VAL A  1 169 ? 21.750  32.716  168.487 1.00 32.37  ? 169 VAL A CA    1 
ATOM   1119  C C     . VAL A  1 169 ? 20.755  33.870  168.395 1.00 35.64  ? 169 VAL A C     1 
ATOM   1120  O O     . VAL A  1 169 ? 20.973  34.825  167.653 1.00 31.63  ? 169 VAL A O     1 
ATOM   1121  C CB    . VAL A  1 169 ? 22.968  33.133  169.345 1.00 36.60  ? 169 VAL A CB    1 
ATOM   1122  C CG1   . VAL A  1 169 ? 22.534  33.962  170.547 1.00 33.18  ? 169 VAL A CG1   1 
ATOM   1123  C CG2   . VAL A  1 169 ? 23.748  31.906  169.783 1.00 30.67  ? 169 VAL A CG2   1 
ATOM   1124  N N     . GLY A  1 170 ? 19.653  33.771  169.133 1.00 37.64  ? 170 GLY A N     1 
ATOM   1125  C CA    . GLY A  1 170 ? 18.635  34.808  169.114 1.00 31.46  ? 170 GLY A CA    1 
ATOM   1126  C C     . GLY A  1 170 ? 18.962  35.981  170.023 1.00 30.35  ? 170 GLY A C     1 
ATOM   1127  O O     . GLY A  1 170 ? 19.503  35.800  171.111 1.00 32.19  ? 170 GLY A O     1 
ATOM   1128  N N     . THR A  1 171 ? 18.628  37.187  169.576 1.00 28.80  ? 171 THR A N     1 
ATOM   1129  C CA    . THR A  1 171 ? 18.842  38.393  170.374 1.00 28.37  ? 171 THR A CA    1 
ATOM   1130  C C     . THR A  1 171 ? 18.000  38.379  171.648 1.00 33.86  ? 171 THR A C     1 
ATOM   1131  O O     . THR A  1 171 ? 18.352  39.017  172.638 1.00 31.16  ? 171 THR A O     1 
ATOM   1132  C CB    . THR A  1 171 ? 18.507  39.665  169.579 1.00 33.20  ? 171 THR A CB    1 
ATOM   1133  O OG1   . THR A  1 171 ? 17.153  39.591  169.120 1.00 30.92  ? 171 THR A OG1   1 
ATOM   1134  C CG2   . THR A  1 171 ? 19.442  39.817  168.380 1.00 25.86  ? 171 THR A CG2   1 
ATOM   1135  N N     . GLY A  1 172 ? 16.887  37.651  171.606 1.00 33.30  ? 172 GLY A N     1 
ATOM   1136  C CA    . GLY A  1 172 ? 15.977  37.560  172.732 1.00 31.64  ? 172 GLY A CA    1 
ATOM   1137  C C     . GLY A  1 172 ? 16.646  37.059  173.996 1.00 35.19  ? 172 GLY A C     1 
ATOM   1138  O O     . GLY A  1 172 ? 16.587  37.711  175.037 1.00 35.20  ? 172 GLY A O     1 
ATOM   1139  N N     . GLY A  1 173 ? 17.287  35.899  173.907 1.00 32.10  ? 173 GLY A N     1 
ATOM   1140  C CA    . GLY A  1 173 ? 17.972  35.326  175.049 1.00 32.65  ? 173 GLY A CA    1 
ATOM   1141  C C     . GLY A  1 173 ? 19.367  35.887  175.234 1.00 30.50  ? 173 GLY A C     1 
ATOM   1142  O O     . GLY A  1 173 ? 19.806  36.109  176.361 1.00 31.27  ? 173 GLY A O     1 
ATOM   1143  N N     . HIS A  1 174 ? 20.057  36.127  174.123 1.00 27.88  ? 174 HIS A N     1 
ATOM   1144  C CA    . HIS A  1 174 ? 21.452  36.571  174.145 1.00 31.10  ? 174 HIS A CA    1 
ATOM   1145  C C     . HIS A  1 174 ? 21.638  37.898  174.872 1.00 30.89  ? 174 HIS A C     1 
ATOM   1146  O O     . HIS A  1 174 ? 22.433  38.004  175.804 1.00 27.49  ? 174 HIS A O     1 
ATOM   1147  C CB    . HIS A  1 174 ? 21.985  36.699  172.717 1.00 27.51  ? 174 HIS A CB    1 
ATOM   1148  C CG    . HIS A  1 174 ? 23.460  36.928  172.637 1.00 37.43  ? 174 HIS A CG    1 
ATOM   1149  N ND1   . HIS A  1 174 ? 24.380  36.017  173.108 1.00 36.33  ? 174 HIS A ND1   1 
ATOM   1150  C CD2   . HIS A  1 174 ? 24.177  37.966  172.142 1.00 32.27  ? 174 HIS A CD2   1 
ATOM   1151  C CE1   . HIS A  1 174 ? 25.600  36.482  172.906 1.00 31.77  ? 174 HIS A CE1   1 
ATOM   1152  N NE2   . HIS A  1 174 ? 25.504  37.662  172.319 1.00 33.23  ? 174 HIS A NE2   1 
ATOM   1153  N N     . ILE A  1 175 ? 20.901  38.910  174.431 1.00 30.74  ? 175 ILE A N     1 
ATOM   1154  C CA    . ILE A  1 175 ? 21.015  40.245  175.002 1.00 26.44  ? 175 ILE A CA    1 
ATOM   1155  C C     . ILE A  1 175 ? 20.449  40.264  176.423 1.00 30.94  ? 175 ILE A C     1 
ATOM   1156  O O     . ILE A  1 175 ? 20.970  40.954  177.301 1.00 28.57  ? 175 ILE A O     1 
ATOM   1157  C CB    . ILE A  1 175 ? 20.298  41.290  174.121 1.00 31.22  ? 175 ILE A CB    1 
ATOM   1158  C CG1   . ILE A  1 175 ? 20.924  41.331  172.722 1.00 25.85  ? 175 ILE A CG1   1 
ATOM   1159  C CG2   . ILE A  1 175 ? 20.342  42.667  174.760 1.00 27.28  ? 175 ILE A CG2   1 
ATOM   1160  C CD1   . ILE A  1 175 ? 20.403  42.462  171.853 1.00 32.67  ? 175 ILE A CD1   1 
ATOM   1161  N N     . SER A  1 176 ? 19.396  39.483  176.647 1.00 26.66  ? 176 SER A N     1 
ATOM   1162  C CA    . SER A  1 176 ? 18.786  39.369  177.970 1.00 28.67  ? 176 SER A CA    1 
ATOM   1163  C C     . SER A  1 176 ? 19.766  38.873  179.031 1.00 31.29  ? 176 SER A C     1 
ATOM   1164  O O     . SER A  1 176 ? 19.602  39.158  180.217 1.00 28.46  ? 176 SER A O     1 
ATOM   1165  C CB    . SER A  1 176 ? 17.578  38.432  177.927 1.00 27.82  ? 176 SER A CB    1 
ATOM   1166  O OG    . SER A  1 176 ? 16.489  39.020  177.241 1.00 32.11  ? 176 SER A OG    1 
ATOM   1167  N N     . GLY A  1 177 ? 20.774  38.118  178.604 1.00 27.06  ? 177 GLY A N     1 
ATOM   1168  C CA    . GLY A  1 177 ? 21.750  37.562  179.523 1.00 29.82  ? 177 GLY A CA    1 
ATOM   1169  C C     . GLY A  1 177 ? 23.121  38.211  179.462 1.00 34.56  ? 177 GLY A C     1 
ATOM   1170  O O     . GLY A  1 177 ? 24.061  37.752  180.109 1.00 30.30  ? 177 GLY A O     1 
ATOM   1171  N N     . GLY A  1 178 ? 23.243  39.277  178.680 1.00 29.40  ? 178 GLY A N     1 
ATOM   1172  C CA    . GLY A  1 178 ? 24.519  39.954  178.522 1.00 31.25  ? 178 GLY A CA    1 
ATOM   1173  C C     . GLY A  1 178 ? 24.966  40.004  177.075 1.00 32.37  ? 178 GLY A C     1 
ATOM   1174  O O     . GLY A  1 178 ? 24.683  40.967  176.363 1.00 31.91  ? 178 GLY A O     1 
ATOM   1175  N N     . GLY A  1 179 ? 25.670  38.965  176.637 1.00 27.78  ? 179 GLY A N     1 
ATOM   1176  C CA    . GLY A  1 179 ? 26.101  38.879  175.256 1.00 30.03  ? 179 GLY A CA    1 
ATOM   1177  C C     . GLY A  1 179 ? 27.557  39.242  175.052 1.00 31.49  ? 179 GLY A C     1 
ATOM   1178  O O     . GLY A  1 179 ? 27.884  40.392  174.761 1.00 32.29  ? 179 GLY A O     1 
ATOM   1179  N N     . PHE A  1 180 ? 28.431  38.251  175.193 1.00 37.24  ? 180 PHE A N     1 
ATOM   1180  C CA    . PHE A  1 180 ? 29.870  38.458  175.056 1.00 36.16  ? 180 PHE A CA    1 
ATOM   1181  C C     . PHE A  1 180 ? 30.363  38.003  173.682 1.00 38.99  ? 180 PHE A C     1 
ATOM   1182  O O     . PHE A  1 180 ? 29.923  36.971  173.169 1.00 40.44  ? 180 PHE A O     1 
ATOM   1183  C CB    . PHE A  1 180 ? 30.613  37.709  176.166 1.00 37.03  ? 180 PHE A CB    1 
ATOM   1184  C CG    . PHE A  1 180 ? 32.095  37.931  176.165 1.00 37.97  ? 180 PHE A CG    1 
ATOM   1185  C CD1   . PHE A  1 180 ? 32.645  39.021  176.821 1.00 33.01  ? 180 PHE A CD1   1 
ATOM   1186  C CD2   . PHE A  1 180 ? 32.940  37.047  175.518 1.00 38.97  ? 180 PHE A CD2   1 
ATOM   1187  C CE1   . PHE A  1 180 ? 34.011  39.229  176.826 1.00 36.79  ? 180 PHE A CE1   1 
ATOM   1188  C CE2   . PHE A  1 180 ? 34.307  37.248  175.515 1.00 38.72  ? 180 PHE A CE2   1 
ATOM   1189  C CZ    . PHE A  1 180 ? 34.844  38.342  176.172 1.00 33.01  ? 180 PHE A CZ    1 
ATOM   1190  N N     . GLY A  1 181 ? 31.268  38.780  173.087 1.00 38.61  ? 181 GLY A N     1 
ATOM   1191  C CA    . GLY A  1 181 ? 31.780  38.478  171.760 1.00 42.46  ? 181 GLY A CA    1 
ATOM   1192  C C     . GLY A  1 181 ? 33.192  38.968  171.473 1.00 35.46  ? 181 GLY A C     1 
ATOM   1193  O O     . GLY A  1 181 ? 33.883  39.468  172.363 1.00 35.44  ? 181 GLY A O     1 
ATOM   1194  N N     . MET A  1 182 ? 33.612  38.833  170.217 1.00 38.56  ? 182 MET A N     1 
ATOM   1195  C CA    . MET A  1 182 ? 34.970  39.172  169.796 1.00 43.10  ? 182 MET A CA    1 
ATOM   1196  C C     . MET A  1 182 ? 35.267  40.672  169.856 1.00 41.61  ? 182 MET A C     1 
ATOM   1197  O O     . MET A  1 182 ? 36.424  41.086  169.761 1.00 39.67  ? 182 MET A O     1 
ATOM   1198  C CB    . MET A  1 182 ? 35.217  38.656  168.375 1.00 45.27  ? 182 MET A CB    1 
ATOM   1199  C CG    . MET A  1 182 ? 35.069  37.147  168.226 1.00 46.07  ? 182 MET A CG    1 
ATOM   1200  S SD    . MET A  1 182 ? 36.482  36.223  168.858 1.00 50.80  ? 182 MET A SD    1 
ATOM   1201  C CE    . MET A  1 182 ? 37.770  36.790  167.748 1.00 49.89  ? 182 MET A CE    1 
ATOM   1202  N N     . MET A  1 183 ? 34.229  41.487  170.015 1.00 37.61  ? 183 MET A N     1 
ATOM   1203  C CA    . MET A  1 183 ? 34.413  42.935  170.073 1.00 35.70  ? 183 MET A CA    1 
ATOM   1204  C C     . MET A  1 183 ? 34.109  43.493  171.460 1.00 33.46  ? 183 MET A C     1 
ATOM   1205  O O     . MET A  1 183 ? 34.044  44.709  171.644 1.00 31.93  ? 183 MET A O     1 
ATOM   1206  C CB    . MET A  1 183 ? 33.534  43.639  169.032 1.00 48.26  ? 183 MET A CB    1 
ATOM   1207  C CG    . MET A  1 183 ? 33.767  43.186  167.595 1.00 47.50  ? 183 MET A CG    1 
ATOM   1208  S SD    . MET A  1 183 ? 33.225  44.395  166.369 1.00 58.29  ? 183 MET A SD    1 
ATOM   1209  C CE    . MET A  1 183 ? 31.666  44.920  167.072 1.00 48.79  ? 183 MET A CE    1 
ATOM   1210  N N     . SER A  1 184 ? 33.932  42.604  172.433 1.00 30.85  ? 184 SER A N     1 
ATOM   1211  C CA    . SER A  1 184 ? 33.535  43.011  173.781 1.00 35.63  ? 184 SER A CA    1 
ATOM   1212  C C     . SER A  1 184 ? 34.656  43.692  174.566 1.00 33.68  ? 184 SER A C     1 
ATOM   1213  O O     . SER A  1 184 ? 34.394  44.453  175.494 1.00 37.69  ? 184 SER A O     1 
ATOM   1214  C CB    . SER A  1 184 ? 33.021  41.807  174.573 1.00 34.70  ? 184 SER A CB    1 
ATOM   1215  O OG    . SER A  1 184 ? 31.781  41.357  174.062 1.00 36.84  ? 184 SER A OG    1 
ATOM   1216  N N     . ARG A  1 185 ? 35.902  43.409  174.205 1.00 32.02  ? 185 ARG A N     1 
ATOM   1217  C CA    . ARG A  1 185 ? 37.033  44.079  174.839 1.00 34.82  ? 185 ARG A CA    1 
ATOM   1218  C C     . ARG A  1 185 ? 37.065  45.542  174.403 1.00 34.64  ? 185 ARG A C     1 
ATOM   1219  O O     . ARG A  1 185 ? 37.652  46.395  175.067 1.00 38.87  ? 185 ARG A O     1 
ATOM   1220  C CB    . ARG A  1 185 ? 38.350  43.379  174.498 1.00 31.96  ? 185 ARG A CB    1 
ATOM   1221  C CG    . ARG A  1 185 ? 38.376  41.900  174.873 1.00 36.72  ? 185 ARG A CG    1 
ATOM   1222  C CD    . ARG A  1 185 ? 39.753  41.274  174.680 1.00 34.01  ? 185 ARG A CD    1 
ATOM   1223  N NE    . ARG A  1 185 ? 40.742  41.797  175.620 1.00 40.67  ? 185 ARG A NE    1 
ATOM   1224  C CZ    . ARG A  1 185 ? 41.655  42.716  175.319 1.00 38.07  ? 185 ARG A CZ    1 
ATOM   1225  N NH1   . ARG A  1 185 ? 41.712  43.225  174.095 1.00 36.57  ? 185 ARG A NH1   1 
ATOM   1226  N NH2   . ARG A  1 185 ? 42.510  43.129  176.243 1.00 40.37  ? 185 ARG A NH2   1 
ATOM   1227  N N     . LYS A  1 186 ? 36.414  45.820  173.280 1.00 35.13  ? 186 LYS A N     1 
ATOM   1228  C CA    . LYS A  1 186 ? 36.319  47.171  172.745 1.00 38.35  ? 186 LYS A CA    1 
ATOM   1229  C C     . LYS A  1 186 ? 35.018  47.861  173.161 1.00 32.45  ? 186 LYS A C     1 
ATOM   1230  O O     . LYS A  1 186 ? 35.024  49.028  173.552 1.00 34.42  ? 186 LYS A O     1 
ATOM   1231  C CB    . LYS A  1 186 ? 36.432  47.131  171.219 1.00 41.56  ? 186 LYS A CB    1 
ATOM   1232  C CG    . LYS A  1 186 ? 36.170  48.456  170.517 1.00 44.58  ? 186 LYS A CG    1 
ATOM   1233  C CD    . LYS A  1 186 ? 37.376  49.378  170.565 1.00 40.66  ? 186 LYS A CD    1 
ATOM   1234  C CE    . LYS A  1 186 ? 37.205  50.557  169.611 1.00 42.35  ? 186 LYS A CE    1 
ATOM   1235  N NZ    . LYS A  1 186 ? 38.307  51.555  169.725 1.00 61.03  ? 186 LYS A NZ    1 
ATOM   1236  N N     . TYR A  1 187 ? 33.905  47.138  173.081 1.00 32.26  ? 187 TYR A N     1 
ATOM   1237  C CA    . TYR A  1 187 ? 32.596  47.751  173.293 1.00 34.95  ? 187 TYR A CA    1 
ATOM   1238  C C     . TYR A  1 187 ? 31.759  47.123  174.405 1.00 35.56  ? 187 TYR A C     1 
ATOM   1239  O O     . TYR A  1 187 ? 30.610  47.510  174.608 1.00 35.25  ? 187 TYR A O     1 
ATOM   1240  C CB    . TYR A  1 187 ? 31.788  47.715  171.996 1.00 35.32  ? 187 TYR A CB    1 
ATOM   1241  C CG    . TYR A  1 187 ? 32.312  48.628  170.914 1.00 36.17  ? 187 TYR A CG    1 
ATOM   1242  C CD1   . TYR A  1 187 ? 32.373  50.000  171.109 1.00 34.25  ? 187 TYR A CD1   1 
ATOM   1243  C CD2   . TYR A  1 187 ? 32.730  48.119  169.691 1.00 36.02  ? 187 TYR A CD2   1 
ATOM   1244  C CE1   . TYR A  1 187 ? 32.848  50.843  170.121 1.00 38.54  ? 187 TYR A CE1   1 
ATOM   1245  C CE2   . TYR A  1 187 ? 33.205  48.953  168.695 1.00 40.78  ? 187 TYR A CE2   1 
ATOM   1246  C CZ    . TYR A  1 187 ? 33.262  50.314  168.917 1.00 41.50  ? 187 TYR A CZ    1 
ATOM   1247  O OH    . TYR A  1 187 ? 33.730  51.148  167.929 1.00 39.87  ? 187 TYR A OH    1 
ATOM   1248  N N     . GLY A  1 188 ? 32.319  46.156  175.120 1.00 31.79  ? 188 GLY A N     1 
ATOM   1249  C CA    . GLY A  1 188 ? 31.576  45.490  176.174 1.00 30.75  ? 188 GLY A CA    1 
ATOM   1250  C C     . GLY A  1 188 ? 30.527  44.537  175.632 1.00 32.12  ? 188 GLY A C     1 
ATOM   1251  O O     . GLY A  1 188 ? 30.583  44.121  174.474 1.00 36.16  ? 188 GLY A O     1 
ATOM   1252  N N     . LEU A  1 189 ? 29.558  44.193  176.473 1.00 26.79  ? 189 LEU A N     1 
ATOM   1253  C CA    . LEU A  1 189 ? 28.531  43.229  176.094 1.00 30.83  ? 189 LEU A CA    1 
ATOM   1254  C C     . LEU A  1 189 ? 27.469  43.831  175.178 1.00 29.95  ? 189 LEU A C     1 
ATOM   1255  O O     . LEU A  1 189 ? 27.348  45.052  175.061 1.00 29.47  ? 189 LEU A O     1 
ATOM   1256  C CB    . LEU A  1 189 ? 27.865  42.653  177.344 1.00 29.29  ? 189 LEU A CB    1 
ATOM   1257  C CG    . LEU A  1 189 ? 28.808  42.098  178.410 1.00 34.65  ? 189 LEU A CG    1 
ATOM   1258  C CD1   . LEU A  1 189 ? 28.021  41.587  179.596 1.00 29.35  ? 189 LEU A CD1   1 
ATOM   1259  C CD2   . LEU A  1 189 ? 29.684  41.004  177.827 1.00 31.77  ? 189 LEU A CD2   1 
ATOM   1260  N N     . ALA A  1 190 ? 26.704  42.961  174.527 1.00 30.34  ? 190 ALA A N     1 
ATOM   1261  C CA    . ALA A  1 190 ? 25.572  43.395  173.720 1.00 26.32  ? 190 ALA A CA    1 
ATOM   1262  C C     . ALA A  1 190 ? 24.618  44.228  174.562 1.00 26.16  ? 190 ALA A C     1 
ATOM   1263  O O     . ALA A  1 190 ? 24.166  45.290  174.138 1.00 27.62  ? 190 ALA A O     1 
ATOM   1264  C CB    . ALA A  1 190 ? 24.851  42.199  173.125 1.00 32.50  ? 190 ALA A CB    1 
ATOM   1265  N N     . ALA A  1 191 ? 24.329  43.739  175.765 1.00 27.52  ? 191 ALA A N     1 
ATOM   1266  C CA    . ALA A  1 191 ? 23.415  44.411  176.684 1.00 27.42  ? 191 ALA A CA    1 
ATOM   1267  C C     . ALA A  1 191 ? 23.944  45.759  177.162 1.00 29.61  ? 191 ALA A C     1 
ATOM   1268  O O     . ALA A  1 191 ? 23.169  46.614  177.591 1.00 28.21  ? 191 ALA A O     1 
ATOM   1269  C CB    . ALA A  1 191 ? 23.131  43.518  177.874 1.00 28.29  ? 191 ALA A CB    1 
ATOM   1270  N N     . ASP A  1 192 ? 25.261  45.942  177.105 1.00 33.39  ? 192 ASP A N     1 
ATOM   1271  C CA    . ASP A  1 192 ? 25.879  47.208  177.494 1.00 30.73  ? 192 ASP A CA    1 
ATOM   1272  C C     . ASP A  1 192 ? 25.592  48.309  176.481 1.00 27.02  ? 192 ASP A C     1 
ATOM   1273  O O     . ASP A  1 192 ? 25.808  49.487  176.757 1.00 31.35  ? 192 ASP A O     1 
ATOM   1274  C CB    . ASP A  1 192 ? 27.395  47.047  177.650 1.00 33.57  ? 192 ASP A CB    1 
ATOM   1275  C CG    . ASP A  1 192 ? 27.772  46.136  178.798 1.00 32.91  ? 192 ASP A CG    1 
ATOM   1276  O OD1   . ASP A  1 192 ? 27.005  46.057  179.777 1.00 32.89  ? 192 ASP A OD1   1 
ATOM   1277  O OD2   . ASP A  1 192 ? 28.844  45.501  178.719 1.00 39.14  ? 192 ASP A OD2   1 
ATOM   1278  N N     . ASN A  1 193 ? 25.115  47.919  175.304 1.00 29.37  ? 193 ASN A N     1 
ATOM   1279  C CA    . ASN A  1 193 ? 24.859  48.873  174.232 1.00 26.77  ? 193 ASN A CA    1 
ATOM   1280  C C     . ASN A  1 193 ? 23.377  48.961  173.865 1.00 32.57  ? 193 ASN A C     1 
ATOM   1281  O O     . ASN A  1 193 ? 23.025  49.288  172.732 1.00 31.63  ? 193 ASN A O     1 
ATOM   1282  C CB    . ASN A  1 193 ? 25.696  48.508  173.009 1.00 26.25  ? 193 ASN A CB    1 
ATOM   1283  C CG    . ASN A  1 193 ? 27.191  48.611  173.283 1.00 33.55  ? 193 ASN A CG    1 
ATOM   1284  O OD1   . ASN A  1 193 ? 27.789  49.675  173.133 1.00 34.43  ? 193 ASN A OD1   1 
ATOM   1285  N ND2   . ASN A  1 193 ? 27.794  47.506  173.703 1.00 28.74  ? 193 ASN A ND2   1 
ATOM   1286  N N     . VAL A  1 194 ? 22.516  48.673  174.836 1.00 33.68  ? 194 VAL A N     1 
ATOM   1287  C CA    . VAL A  1 194 ? 21.070  48.803  174.665 1.00 25.52  ? 194 VAL A CA    1 
ATOM   1288  C C     . VAL A  1 194 ? 20.590  50.123  175.256 1.00 29.50  ? 194 VAL A C     1 
ATOM   1289  O O     . VAL A  1 194 ? 20.867  50.416  176.416 1.00 33.44  ? 194 VAL A O     1 
ATOM   1290  C CB    . VAL A  1 194 ? 20.322  47.635  175.334 1.00 27.91  ? 194 VAL A CB    1 
ATOM   1291  C CG1   . VAL A  1 194 ? 18.816  47.910  175.378 1.00 25.70  ? 194 VAL A CG1   1 
ATOM   1292  C CG2   . VAL A  1 194 ? 20.625  46.335  174.610 1.00 29.64  ? 194 VAL A CG2   1 
ATOM   1293  N N     . VAL A  1 195 ? 19.870  50.915  174.465 1.00 28.98  ? 195 VAL A N     1 
ATOM   1294  C CA    . VAL A  1 195 ? 19.447  52.241  174.912 1.00 30.30  ? 195 VAL A CA    1 
ATOM   1295  C C     . VAL A  1 195 ? 17.945  52.336  175.185 1.00 32.81  ? 195 VAL A C     1 
ATOM   1296  O O     . VAL A  1 195 ? 17.490  53.242  175.887 1.00 34.37  ? 195 VAL A O     1 
ATOM   1297  C CB    . VAL A  1 195 ? 19.835  53.322  173.888 1.00 33.73  ? 195 VAL A CB    1 
ATOM   1298  C CG1   . VAL A  1 195 ? 21.349  53.382  173.733 1.00 30.03  ? 195 VAL A CG1   1 
ATOM   1299  C CG2   . VAL A  1 195 ? 19.172  53.051  172.546 1.00 34.99  ? 195 VAL A CG2   1 
ATOM   1300  N N     . ASP A  1 196 ? 17.180  51.407  174.622 1.00 32.89  ? 196 ASP A N     1 
ATOM   1301  C CA    . ASP A  1 196 ? 15.754  51.305  174.912 1.00 30.07  ? 196 ASP A CA    1 
ATOM   1302  C C     . ASP A  1 196 ? 15.288  49.884  174.605 1.00 35.50  ? 196 ASP A C     1 
ATOM   1303  O O     . ASP A  1 196 ? 16.026  49.098  174.009 1.00 31.58  ? 196 ASP A O     1 
ATOM   1304  C CB    . ASP A  1 196 ? 14.952  52.328  174.103 1.00 31.49  ? 196 ASP A CB    1 
ATOM   1305  C CG    . ASP A  1 196 ? 13.623  52.683  174.754 1.00 33.74  ? 196 ASP A CG    1 
ATOM   1306  O OD1   . ASP A  1 196 ? 13.007  51.804  175.394 1.00 35.98  ? 196 ASP A OD1   1 
ATOM   1307  O OD2   . ASP A  1 196 ? 13.192  53.849  174.623 1.00 37.06  ? 196 ASP A OD2   1 
ATOM   1308  N N     . ALA A  1 197 ? 14.067  49.554  175.007 1.00 27.22  ? 197 ALA A N     1 
ATOM   1309  C CA    . ALA A  1 197 ? 13.521  48.226  174.759 1.00 32.47  ? 197 ALA A CA    1 
ATOM   1310  C C     . ALA A  1 197 ? 12.015  48.229  174.920 1.00 32.31  ? 197 ALA A C     1 
ATOM   1311  O O     . ALA A  1 197 ? 11.468  49.028  175.677 1.00 30.93  ? 197 ALA A O     1 
ATOM   1312  C CB    . ALA A  1 197 ? 14.149  47.205  175.700 1.00 29.53  ? 197 ALA A CB    1 
ATOM   1313  N N     . ILE A  1 198 ? 11.345  47.336  174.202 1.00 29.60  ? 198 ILE A N     1 
ATOM   1314  C CA    . ILE A  1 198 ? 9.922   47.130  174.409 1.00 26.72  ? 198 ILE A CA    1 
ATOM   1315  C C     . ILE A  1 198 ? 9.716   45.858  175.221 1.00 32.62  ? 198 ILE A C     1 
ATOM   1316  O O     . ILE A  1 198 ? 10.034  44.758  174.769 1.00 28.67  ? 198 ILE A O     1 
ATOM   1317  C CB    . ILE A  1 198 ? 9.149   47.043  173.081 1.00 31.09  ? 198 ILE A CB    1 
ATOM   1318  C CG1   . ILE A  1 198 ? 9.353   48.323  172.272 1.00 25.38  ? 198 ILE A CG1   1 
ATOM   1319  C CG2   . ILE A  1 198 ? 7.662   46.802  173.340 1.00 31.77  ? 198 ILE A CG2   1 
ATOM   1320  C CD1   . ILE A  1 198 ? 9.022   49.585  173.041 1.00 32.83  ? 198 ILE A CD1   1 
ATOM   1321  N N     . LEU A  1 199 ? 9.205   46.022  176.435 1.00 26.50  ? 199 LEU A N     1 
ATOM   1322  C CA    . LEU A  1 199 ? 8.947   44.895  177.315 1.00 28.53  ? 199 LEU A CA    1 
ATOM   1323  C C     . LEU A  1 199 ? 7.444   44.704  177.501 1.00 32.62  ? 199 LEU A C     1 
ATOM   1324  O O     . LEU A  1 199 ? 6.709   45.659  177.765 1.00 29.13  ? 199 LEU A O     1 
ATOM   1325  C CB    . LEU A  1 199 ? 9.636   45.103  178.666 1.00 25.95  ? 199 LEU A CB    1 
ATOM   1326  C CG    . LEU A  1 199 ? 9.434   44.026  179.736 1.00 32.53  ? 199 LEU A CG    1 
ATOM   1327  C CD1   . LEU A  1 199 ? 10.089  42.709  179.340 1.00 27.69  ? 199 LEU A CD1   1 
ATOM   1328  C CD2   . LEU A  1 199 ? 9.971   44.504  181.071 1.00 36.88  ? 199 LEU A CD2   1 
ATOM   1329  N N     . ILE A  1 200 ? 6.988   43.468  177.346 1.00 26.84  ? 200 ILE A N     1 
ATOM   1330  C CA    . ILE A  1 200 ? 5.577   43.152  177.530 1.00 28.65  ? 200 ILE A CA    1 
ATOM   1331  C C     . ILE A  1 200 ? 5.420   42.350  178.814 1.00 33.23  ? 200 ILE A C     1 
ATOM   1332  O O     . ILE A  1 200 ? 5.957   41.247  178.929 1.00 31.23  ? 200 ILE A O     1 
ATOM   1333  C CB    . ILE A  1 200 ? 5.013   42.370  176.330 1.00 28.67  ? 200 ILE A CB    1 
ATOM   1334  C CG1   . ILE A  1 200 ? 5.177   43.184  175.044 1.00 31.00  ? 200 ILE A CG1   1 
ATOM   1335  C CG2   . ILE A  1 200 ? 3.547   42.025  176.551 1.00 32.50  ? 200 ILE A CG2   1 
ATOM   1336  C CD1   . ILE A  1 200 ? 4.650   42.491  173.809 1.00 31.52  ? 200 ILE A CD1   1 
ATOM   1337  N N     . ASP A  1 201 ? 4.700   42.900  179.789 1.00 32.23  ? 201 ASP A N     1 
ATOM   1338  C CA    . ASP A  1 201 ? 4.634   42.249  181.094 1.00 33.34  ? 201 ASP A CA    1 
ATOM   1339  C C     . ASP A  1 201 ? 3.542   41.190  181.163 1.00 37.14  ? 201 ASP A C     1 
ATOM   1340  O O     . ASP A  1 201 ? 2.895   40.875  180.162 1.00 30.88  ? 201 ASP A O     1 
ATOM   1341  C CB    . ASP A  1 201 ? 4.455   43.283  182.221 1.00 35.66  ? 201 ASP A CB    1 
ATOM   1342  C CG    . ASP A  1 201 ? 3.069   43.932  182.250 1.00 40.31  ? 201 ASP A CG    1 
ATOM   1343  O OD1   . ASP A  1 201 ? 2.152   43.537  181.495 1.00 42.40  ? 201 ASP A OD1   1 
ATOM   1344  O OD2   . ASP A  1 201 ? 2.898   44.857  183.071 1.00 37.28  ? 201 ASP A OD2   1 
ATOM   1345  N N     . ALA A  1 202 ? 3.343   40.655  182.361 1.00 32.93  ? 202 ALA A N     1 
ATOM   1346  C CA    . ALA A  1 202 ? 2.425   39.546  182.578 1.00 33.92  ? 202 ALA A CA    1 
ATOM   1347  C C     . ALA A  1 202 ? 0.971   39.909  182.295 1.00 36.23  ? 202 ALA A C     1 
ATOM   1348  O O     . ALA A  1 202 ? 0.140   39.027  182.086 1.00 33.69  ? 202 ALA A O     1 
ATOM   1349  C CB    . ALA A  1 202 ? 2.563   39.036  183.999 1.00 36.58  ? 202 ALA A CB    1 
ATOM   1350  N N     . ASN A  1 203 ? 0.661   41.202  182.293 1.00 39.66  ? 203 ASN A N     1 
ATOM   1351  C CA    . ASN A  1 203 ? -0.697  41.655  181.999 1.00 33.60  ? 203 ASN A CA    1 
ATOM   1352  C C     . ASN A  1 203 ? -0.858  42.064  180.540 1.00 37.75  ? 203 ASN A C     1 
ATOM   1353  O O     . ASN A  1 203 ? -1.931  42.497  180.124 1.00 30.95  ? 203 ASN A O     1 
ATOM   1354  C CB    . ASN A  1 203 ? -1.084  42.824  182.908 1.00 35.42  ? 203 ASN A CB    1 
ATOM   1355  C CG    . ASN A  1 203 ? -1.062  42.452  184.377 1.00 42.49  ? 203 ASN A CG    1 
ATOM   1356  O OD1   . ASN A  1 203 ? -1.352  41.314  184.745 1.00 42.52  ? 203 ASN A OD1   1 
ATOM   1357  N ND2   . ASN A  1 203 ? -0.708  43.411  185.226 1.00 46.94  ? 203 ASN A ND2   1 
ATOM   1358  N N     . GLY A  1 204 ? 0.214   41.927  179.767 1.00 32.22  ? 204 GLY A N     1 
ATOM   1359  C CA    . GLY A  1 204 ? 0.185   42.278  178.358 1.00 32.90  ? 204 GLY A CA    1 
ATOM   1360  C C     . GLY A  1 204 ? 0.455   43.750  178.106 1.00 31.74  ? 204 GLY A C     1 
ATOM   1361  O O     . GLY A  1 204 ? 0.399   44.213  176.965 1.00 30.19  ? 204 GLY A O     1 
ATOM   1362  N N     . ALA A  1 205 ? 0.740   44.487  179.176 1.00 30.72  ? 205 ALA A N     1 
ATOM   1363  C CA    . ALA A  1 205 ? 1.086   45.899  179.066 1.00 39.91  ? 205 ALA A CA    1 
ATOM   1364  C C     . ALA A  1 205 ? 2.344   46.057  178.228 1.00 30.91  ? 205 ALA A C     1 
ATOM   1365  O O     . ALA A  1 205 ? 3.337   45.376  178.464 1.00 29.02  ? 205 ALA A O     1 
ATOM   1366  C CB    . ALA A  1 205 ? 1.278   46.514  180.441 1.00 36.56  ? 205 ALA A CB    1 
ATOM   1367  N N     . ILE A  1 206 ? 2.293   46.949  177.245 1.00 30.33  ? 206 ILE A N     1 
ATOM   1368  C CA    . ILE A  1 206 ? 3.424   47.175  176.352 1.00 31.96  ? 206 ILE A CA    1 
ATOM   1369  C C     . ILE A  1 206 ? 4.246   48.365  176.832 1.00 38.71  ? 206 ILE A C     1 
ATOM   1370  O O     . ILE A  1 206 ? 3.780   49.503  176.801 1.00 32.25  ? 206 ILE A O     1 
ATOM   1371  C CB    . ILE A  1 206 ? 2.948   47.410  174.911 1.00 36.69  ? 206 ILE A CB    1 
ATOM   1372  C CG1   . ILE A  1 206 ? 2.142   46.198  174.436 1.00 36.07  ? 206 ILE A CG1   1 
ATOM   1373  C CG2   . ILE A  1 206 ? 4.131   47.669  173.994 1.00 33.74  ? 206 ILE A CG2   1 
ATOM   1374  C CD1   . ILE A  1 206 ? 1.522   46.356  173.068 1.00 34.75  ? 206 ILE A CD1   1 
ATOM   1375  N N     . LEU A  1 207 ? 5.473   48.096  177.270 1.00 36.30  ? 207 LEU A N     1 
ATOM   1376  C CA    . LEU A  1 207 ? 6.272   49.095  177.977 1.00 33.78  ? 207 LEU A CA    1 
ATOM   1377  C C     . LEU A  1 207 ? 7.598   49.401  177.285 1.00 31.15  ? 207 LEU A C     1 
ATOM   1378  O O     . LEU A  1 207 ? 8.298   48.489  176.846 1.00 28.48  ? 207 LEU A O     1 
ATOM   1379  C CB    . LEU A  1 207 ? 6.551   48.621  179.408 1.00 32.29  ? 207 LEU A CB    1 
ATOM   1380  C CG    . LEU A  1 207 ? 5.351   48.135  180.231 1.00 36.11  ? 207 LEU A CG    1 
ATOM   1381  C CD1   . LEU A  1 207 ? 5.808   47.279  181.400 1.00 33.49  ? 207 LEU A CD1   1 
ATOM   1382  C CD2   . LEU A  1 207 ? 4.517   49.308  180.732 1.00 30.47  ? 207 LEU A CD2   1 
ATOM   1383  N N     . ASP A  1 208 ? 7.946   50.682  177.191 1.00 33.65  ? 208 ASP A N     1 
ATOM   1384  C CA    . ASP A  1 208 ? 9.298   51.058  176.789 1.00 28.46  ? 208 ASP A CA    1 
ATOM   1385  C C     . ASP A  1 208 ? 10.111  51.409  178.030 1.00 29.92  ? 208 ASP A C     1 
ATOM   1386  O O     . ASP A  1 208 ? 9.637   51.223  179.151 1.00 30.56  ? 208 ASP A O     1 
ATOM   1387  C CB    . ASP A  1 208 ? 9.293   52.225  175.791 1.00 37.11  ? 208 ASP A CB    1 
ATOM   1388  C CG    . ASP A  1 208 ? 8.628   53.481  176.338 1.00 34.31  ? 208 ASP A CG    1 
ATOM   1389  O OD1   . ASP A  1 208 ? 8.240   53.511  177.524 1.00 32.17  ? 208 ASP A OD1   1 
ATOM   1390  O OD2   . ASP A  1 208 ? 8.504   54.450  175.562 1.00 37.06  ? 208 ASP A OD2   1 
ATOM   1391  N N     . ARG A  1 209 ? 11.326  51.913  177.823 1.00 34.47  ? 209 ARG A N     1 
ATOM   1392  C CA    . ARG A  1 209 ? 12.229  52.243  178.922 1.00 30.57  ? 209 ARG A CA    1 
ATOM   1393  C C     . ARG A  1 209 ? 11.594  53.221  179.904 1.00 31.97  ? 209 ARG A C     1 
ATOM   1394  O O     . ARG A  1 209 ? 11.654  53.024  181.116 1.00 35.21  ? 209 ARG A O     1 
ATOM   1395  C CB    . ARG A  1 209 ? 13.539  52.826  178.383 1.00 34.67  ? 209 ARG A CB    1 
ATOM   1396  C CG    . ARG A  1 209 ? 14.537  53.199  179.459 1.00 32.07  ? 209 ARG A CG    1 
ATOM   1397  C CD    . ARG A  1 209 ? 15.841  53.695  178.857 1.00 34.66  ? 209 ARG A CD    1 
ATOM   1398  N NE    . ARG A  1 209 ? 16.833  53.955  179.893 1.00 32.12  ? 209 ARG A NE    1 
ATOM   1399  C CZ    . ARG A  1 209 ? 18.094  54.302  179.657 1.00 33.00  ? 209 ARG A CZ    1 
ATOM   1400  N NH1   . ARG A  1 209 ? 18.529  54.435  178.411 1.00 30.39  ? 209 ARG A NH1   1 
ATOM   1401  N NH2   . ARG A  1 209 ? 18.923  54.509  180.670 1.00 29.67  ? 209 ARG A NH2   1 
ATOM   1402  N N     . GLN A  1 210 ? 10.982  54.269  179.363 1.00 30.25  ? 210 GLN A N     1 
ATOM   1403  C CA    . GLN A  1 210 ? 10.300  55.275  180.168 1.00 37.26  ? 210 GLN A CA    1 
ATOM   1404  C C     . GLN A  1 210 ? 9.202   54.654  181.030 1.00 35.87  ? 210 GLN A C     1 
ATOM   1405  O O     . GLN A  1 210 ? 9.079   54.959  182.218 1.00 38.59  ? 210 GLN A O     1 
ATOM   1406  C CB    . GLN A  1 210 ? 9.708   56.360  179.263 1.00 43.94  ? 210 GLN A CB    1 
ATOM   1407  C CG    . GLN A  1 210 ? 9.099   57.540  180.002 1.00 54.63  ? 210 GLN A CG    1 
ATOM   1408  C CD    . GLN A  1 210 ? 8.544   58.593  179.056 1.00 72.24  ? 210 GLN A CD    1 
ATOM   1409  O OE1   . GLN A  1 210 ? 8.013   58.272  177.992 1.00 73.97  ? 210 GLN A OE1   1 
ATOM   1410  N NE2   . GLN A  1 210 ? 8.675   59.859  179.437 1.00 70.87  ? 210 GLN A NE2   1 
ATOM   1411  N N     . ALA A  1 211 ? 8.411   53.776  180.423 1.00 32.60  ? 211 ALA A N     1 
ATOM   1412  C CA    . ALA A  1 211 ? 7.281   53.157  181.108 1.00 27.54  ? 211 ALA A CA    1 
ATOM   1413  C C     . ALA A  1 211 ? 7.693   52.099  182.130 1.00 35.55  ? 211 ALA A C     1 
ATOM   1414  O O     . ALA A  1 211 ? 7.064   51.972  183.178 1.00 35.43  ? 211 ALA A O     1 
ATOM   1415  C CB    . ALA A  1 211 ? 6.335   52.548  180.096 1.00 25.23  ? 211 ALA A CB    1 
ATOM   1416  N N     . MET A  1 212 ? 8.737   51.334  181.820 1.00 31.64  ? 212 MET A N     1 
ATOM   1417  C CA    . MET A  1 212 ? 9.149   50.233  182.687 1.00 34.44  ? 212 MET A CA    1 
ATOM   1418  C C     . MET A  1 212 ? 10.022  50.712  183.848 1.00 33.28  ? 212 MET A C     1 
ATOM   1419  O O     . MET A  1 212 ? 10.130  50.034  184.870 1.00 35.49  ? 212 MET A O     1 
ATOM   1420  C CB    . MET A  1 212 ? 9.889   49.154  181.881 1.00 32.23  ? 212 MET A CB    1 
ATOM   1421  C CG    . MET A  1 212 ? 11.304  49.526  181.450 1.00 34.72  ? 212 MET A CG    1 
ATOM   1422  S SD    . MET A  1 212 ? 12.156  48.192  180.577 1.00 38.46  ? 212 MET A SD    1 
ATOM   1423  C CE    . MET A  1 212 ? 11.430  48.341  178.946 1.00 28.95  ? 212 MET A CE    1 
ATOM   1424  N N     . GLY A  1 213 ? 10.639  51.878  183.691 1.00 34.89  ? 213 GLY A N     1 
ATOM   1425  C CA    . GLY A  1 213 ? 11.500  52.419  184.726 1.00 39.54  ? 213 GLY A CA    1 
ATOM   1426  C C     . GLY A  1 213 ? 12.933  51.940  184.591 1.00 39.56  ? 213 GLY A C     1 
ATOM   1427  O O     . GLY A  1 213 ? 13.202  50.915  183.965 1.00 33.46  ? 213 GLY A O     1 
ATOM   1428  N N     . GLU A  1 214 ? 13.853  52.681  185.200 1.00 36.52  ? 214 GLU A N     1 
ATOM   1429  C CA    . GLU A  1 214 ? 15.279  52.409  185.060 1.00 39.88  ? 214 GLU A CA    1 
ATOM   1430  C C     . GLU A  1 214 ? 15.725  51.119  185.747 1.00 36.72  ? 214 GLU A C     1 
ATOM   1431  O O     . GLU A  1 214 ? 16.703  50.504  185.331 1.00 38.75  ? 214 GLU A O     1 
ATOM   1432  C CB    . GLU A  1 214 ? 16.096  53.584  185.602 1.00 41.10  ? 214 GLU A CB    1 
ATOM   1433  C CG    . GLU A  1 214 ? 16.101  54.801  184.694 1.00 39.07  ? 214 GLU A CG    1 
ATOM   1434  C CD    . GLU A  1 214 ? 16.643  54.487  183.315 1.00 41.60  ? 214 GLU A CD    1 
ATOM   1435  O OE1   . GLU A  1 214 ? 17.845  54.165  183.205 1.00 41.16  ? 214 GLU A OE1   1 
ATOM   1436  O OE2   . GLU A  1 214 ? 15.864  54.555  182.341 1.00 41.29  ? 214 GLU A OE2   1 
ATOM   1437  N N     . ASP A  1 215 ? 15.022  50.710  186.799 1.00 32.59  ? 215 ASP A N     1 
ATOM   1438  C CA    . ASP A  1 215 ? 15.396  49.491  187.519 1.00 36.41  ? 215 ASP A CA    1 
ATOM   1439  C C     . ASP A  1 215 ? 15.088  48.231  186.708 1.00 40.41  ? 215 ASP A C     1 
ATOM   1440  O O     . ASP A  1 215 ? 15.888  47.294  186.669 1.00 37.16  ? 215 ASP A O     1 
ATOM   1441  C CB    . ASP A  1 215 ? 14.692  49.431  188.878 1.00 43.12  ? 215 ASP A CB    1 
ATOM   1442  C CG    . ASP A  1 215 ? 15.293  50.396  189.889 1.00 47.41  ? 215 ASP A CG    1 
ATOM   1443  O OD1   . ASP A  1 215 ? 16.533  50.554  189.899 1.00 46.54  ? 215 ASP A OD1   1 
ATOM   1444  O OD2   . ASP A  1 215 ? 14.525  50.992  190.673 1.00 59.22  ? 215 ASP A OD2   1 
ATOM   1445  N N     . VAL A  1 216 ? 13.922  48.209  186.071 1.00 37.12  ? 216 VAL A N     1 
ATOM   1446  C CA    . VAL A  1 216 ? 13.548  47.097  185.204 1.00 34.18  ? 216 VAL A CA    1 
ATOM   1447  C C     . VAL A  1 216 ? 14.368  47.126  183.918 1.00 33.16  ? 216 VAL A C     1 
ATOM   1448  O O     . VAL A  1 216 ? 14.812  46.083  183.437 1.00 35.60  ? 216 VAL A O     1 
ATOM   1449  C CB    . VAL A  1 216 ? 12.046  47.119  184.858 1.00 37.84  ? 216 VAL A CB    1 
ATOM   1450  C CG1   . VAL A  1 216 ? 11.707  46.001  183.883 1.00 31.73  ? 216 VAL A CG1   1 
ATOM   1451  C CG2   . VAL A  1 216 ? 11.214  47.000  186.123 1.00 40.79  ? 216 VAL A CG2   1 
ATOM   1452  N N     . PHE A  1 217 ? 14.581  48.323  183.373 1.00 30.68  ? 217 PHE A N     1 
ATOM   1453  C CA    . PHE A  1 217 ? 15.384  48.476  182.160 1.00 33.28  ? 217 PHE A CA    1 
ATOM   1454  C C     . PHE A  1 217 ? 16.821  48.022  182.389 1.00 34.21  ? 217 PHE A C     1 
ATOM   1455  O O     . PHE A  1 217 ? 17.506  47.580  181.464 1.00 30.03  ? 217 PHE A O     1 
ATOM   1456  C CB    . PHE A  1 217 ? 15.374  49.925  181.667 1.00 34.86  ? 217 PHE A CB    1 
ATOM   1457  C CG    . PHE A  1 217 ? 16.219  50.146  180.446 1.00 32.58  ? 217 PHE A CG    1 
ATOM   1458  C CD1   . PHE A  1 217 ? 15.824  49.644  179.217 1.00 30.93  ? 217 PHE A CD1   1 
ATOM   1459  C CD2   . PHE A  1 217 ? 17.415  50.840  180.529 1.00 30.34  ? 217 PHE A CD2   1 
ATOM   1460  C CE1   . PHE A  1 217 ? 16.604  49.834  178.090 1.00 29.62  ? 217 PHE A CE1   1 
ATOM   1461  C CE2   . PHE A  1 217 ? 18.199  51.033  179.405 1.00 28.67  ? 217 PHE A CE2   1 
ATOM   1462  C CZ    . PHE A  1 217 ? 17.791  50.532  178.184 1.00 26.68  ? 217 PHE A CZ    1 
ATOM   1463  N N     . TRP A  1 218 ? 17.271  48.147  183.631 1.00 34.59  ? 218 TRP A N     1 
ATOM   1464  C CA    . TRP A  1 218 ? 18.587  47.674  184.033 1.00 30.20  ? 218 TRP A CA    1 
ATOM   1465  C C     . TRP A  1 218 ? 18.596  46.148  184.050 1.00 32.26  ? 218 TRP A C     1 
ATOM   1466  O O     . TRP A  1 218 ? 19.472  45.518  183.464 1.00 32.77  ? 218 TRP A O     1 
ATOM   1467  C CB    . TRP A  1 218 ? 18.951  48.250  185.406 1.00 27.70  ? 218 TRP A CB    1 
ATOM   1468  C CG    . TRP A  1 218 ? 20.177  47.675  186.041 1.00 38.90  ? 218 TRP A CG    1 
ATOM   1469  C CD1   . TRP A  1 218 ? 21.472  48.039  185.806 1.00 33.83  ? 218 TRP A CD1   1 
ATOM   1470  C CD2   . TRP A  1 218 ? 20.223  46.653  187.043 1.00 33.74  ? 218 TRP A CD2   1 
ATOM   1471  N NE1   . TRP A  1 218 ? 22.320  47.297  186.589 1.00 36.67  ? 218 TRP A NE1   1 
ATOM   1472  C CE2   . TRP A  1 218 ? 21.579  46.439  187.359 1.00 31.79  ? 218 TRP A CE2   1 
ATOM   1473  C CE3   . TRP A  1 218 ? 19.249  45.893  187.700 1.00 32.23  ? 218 TRP A CE3   1 
ATOM   1474  C CZ2   . TRP A  1 218 ? 21.986  45.494  188.300 1.00 34.37  ? 218 TRP A CZ2   1 
ATOM   1475  C CZ3   . TRP A  1 218 ? 19.654  44.959  188.633 1.00 30.96  ? 218 TRP A CZ3   1 
ATOM   1476  C CH2   . TRP A  1 218 ? 21.010  44.767  188.926 1.00 35.71  ? 218 TRP A CH2   1 
ATOM   1477  N N     . ALA A  1 219 ? 17.590  45.566  184.695 1.00 31.00  ? 219 ALA A N     1 
ATOM   1478  C CA    . ALA A  1 219 ? 17.498  44.121  184.876 1.00 29.25  ? 219 ALA A CA    1 
ATOM   1479  C C     . ALA A  1 219 ? 17.448  43.337  183.565 1.00 31.38  ? 219 ALA A C     1 
ATOM   1480  O O     . ALA A  1 219 ? 18.065  42.282  183.453 1.00 37.66  ? 219 ALA A O     1 
ATOM   1481  C CB    . ALA A  1 219 ? 16.280  43.782  185.725 1.00 30.14  ? 219 ALA A CB    1 
ATOM   1482  N N     . ILE A  1 220 ? 16.709  43.834  182.579 1.00 32.62  ? 220 ILE A N     1 
ATOM   1483  C CA    . ILE A  1 220 ? 16.580  43.104  181.318 1.00 31.08  ? 220 ILE A CA    1 
ATOM   1484  C C     . ILE A  1 220 ? 17.879  43.104  180.512 1.00 31.04  ? 220 ILE A C     1 
ATOM   1485  O O     . ILE A  1 220 ? 18.058  42.280  179.615 1.00 27.20  ? 220 ILE A O     1 
ATOM   1486  C CB    . ILE A  1 220 ? 15.449  43.677  180.435 1.00 29.35  ? 220 ILE A CB    1 
ATOM   1487  C CG1   . ILE A  1 220 ? 15.744  45.131  180.054 1.00 29.84  ? 220 ILE A CG1   1 
ATOM   1488  C CG2   . ILE A  1 220 ? 14.105  43.556  181.140 1.00 29.68  ? 220 ILE A CG2   1 
ATOM   1489  C CD1   . ILE A  1 220 ? 14.693  45.748  179.155 1.00 30.27  ? 220 ILE A CD1   1 
ATOM   1490  N N     . ARG A  1 221 ? 18.786  44.020  180.835 1.00 29.18  ? 221 ARG A N     1 
ATOM   1491  C CA    . ARG A  1 221 ? 20.066  44.108  180.136 1.00 31.03  ? 221 ARG A CA    1 
ATOM   1492  C C     . ARG A  1 221 ? 21.135  43.216  180.761 1.00 30.56  ? 221 ARG A C     1 
ATOM   1493  O O     . ARG A  1 221 ? 22.248  43.672  181.022 1.00 29.25  ? 221 ARG A O     1 
ATOM   1494  C CB    . ARG A  1 221 ? 20.566  45.554  180.112 1.00 30.77  ? 221 ARG A CB    1 
ATOM   1495  C CG    . ARG A  1 221 ? 19.849  46.458  179.123 1.00 28.82  ? 221 ARG A CG    1 
ATOM   1496  C CD    . ARG A  1 221 ? 20.387  47.886  179.204 1.00 27.96  ? 221 ARG A CD    1 
ATOM   1497  N NE    . ARG A  1 221 ? 20.084  48.519  180.486 1.00 28.90  ? 221 ARG A NE    1 
ATOM   1498  C CZ    . ARG A  1 221 ? 20.841  49.447  181.065 1.00 33.32  ? 221 ARG A CZ    1 
ATOM   1499  N NH1   . ARG A  1 221 ? 21.963  49.853  180.484 1.00 30.46  ? 221 ARG A NH1   1 
ATOM   1500  N NH2   . ARG A  1 221 ? 20.479  49.965  182.232 1.00 34.31  ? 221 ARG A NH2   1 
ATOM   1501  N N     . GLY A  1 222 ? 20.803  41.951  181.001 1.00 29.58  ? 222 GLY A N     1 
ATOM   1502  C CA    . GLY A  1 222 ? 21.767  41.014  181.553 1.00 29.17  ? 222 GLY A CA    1 
ATOM   1503  C C     . GLY A  1 222 ? 21.227  40.128  182.662 1.00 33.80  ? 222 GLY A C     1 
ATOM   1504  O O     . GLY A  1 222 ? 21.860  39.142  183.043 1.00 32.16  ? 222 GLY A O     1 
ATOM   1505  N N     . GLY A  1 223 ? 20.048  40.466  183.174 1.00 29.81  ? 223 GLY A N     1 
ATOM   1506  C CA    . GLY A  1 223 ? 19.460  39.731  184.282 1.00 37.82  ? 223 GLY A CA    1 
ATOM   1507  C C     . GLY A  1 223 ? 18.940  38.349  183.927 1.00 38.38  ? 223 GLY A C     1 
ATOM   1508  O O     . GLY A  1 223 ? 18.488  37.612  184.803 1.00 38.79  ? 223 GLY A O     1 
ATOM   1509  N N     . GLY A  1 224 ? 19.001  37.992  182.648 1.00 33.09  ? 224 GLY A N     1 
ATOM   1510  C CA    . GLY A  1 224 ? 18.584  36.671  182.212 1.00 31.96  ? 224 GLY A CA    1 
ATOM   1511  C C     . GLY A  1 224 ? 17.211  36.654  181.566 1.00 34.34  ? 224 GLY A C     1 
ATOM   1512  O O     . GLY A  1 224 ? 16.283  37.314  182.032 1.00 34.28  ? 224 GLY A O     1 
ATOM   1513  N N     . GLY A  1 225 ? 17.082  35.884  180.490 1.00 32.23  ? 225 GLY A N     1 
ATOM   1514  C CA    . GLY A  1 225 ? 15.830  35.792  179.763 1.00 37.03  ? 225 GLY A CA    1 
ATOM   1515  C C     . GLY A  1 225 ? 14.777  34.966  180.478 1.00 32.49  ? 225 GLY A C     1 
ATOM   1516  O O     . GLY A  1 225 ? 15.096  34.127  181.320 1.00 35.82  ? 225 GLY A O     1 
ATOM   1517  N N     . GLY A  1 226 ? 13.515  35.210  180.135 1.00 34.23  ? 226 GLY A N     1 
ATOM   1518  C CA    . GLY A  1 226 ? 12.400  34.448  180.667 1.00 28.44  ? 226 GLY A CA    1 
ATOM   1519  C C     . GLY A  1 226 ? 12.086  34.736  182.123 1.00 35.09  ? 226 GLY A C     1 
ATOM   1520  O O     . GLY A  1 226 ? 11.608  33.861  182.845 1.00 35.25  ? 226 GLY A O     1 
ATOM   1521  N N     . VAL A  1 227 ? 12.339  35.968  182.556 1.00 35.45  ? 227 VAL A N     1 
ATOM   1522  C CA    . VAL A  1 227 ? 12.203  36.326  183.965 1.00 33.65  ? 227 VAL A CA    1 
ATOM   1523  C C     . VAL A  1 227 ? 11.360  37.585  184.170 1.00 33.99  ? 227 VAL A C     1 
ATOM   1524  O O     . VAL A  1 227 ? 10.623  37.699  185.150 1.00 37.33  ? 227 VAL A O     1 
ATOM   1525  C CB    . VAL A  1 227 ? 13.597  36.535  184.614 1.00 35.47  ? 227 VAL A CB    1 
ATOM   1526  C CG1   . VAL A  1 227 ? 13.477  36.984  186.069 1.00 32.16  ? 227 VAL A CG1   1 
ATOM   1527  C CG2   . VAL A  1 227 ? 14.419  35.264  184.517 1.00 32.83  ? 227 VAL A CG2   1 
ATOM   1528  N N     . TRP A  1 228 ? 11.454  38.516  183.229 1.00 29.11  ? 228 TRP A N     1 
ATOM   1529  C CA    . TRP A  1 228 ? 10.931  39.865  183.427 1.00 33.10  ? 228 TRP A CA    1 
ATOM   1530  C C     . TRP A  1 228 ? 9.667   40.137  182.627 1.00 35.79  ? 228 TRP A C     1 
ATOM   1531  O O     . TRP A  1 228 ? 8.958   41.110  182.875 1.00 34.82  ? 228 TRP A O     1 
ATOM   1532  C CB    . TRP A  1 228 ? 12.011  40.879  183.057 1.00 32.17  ? 228 TRP A CB    1 
ATOM   1533  C CG    . TRP A  1 228 ? 13.338  40.426  183.535 1.00 31.84  ? 228 TRP A CG    1 
ATOM   1534  C CD1   . TRP A  1 228 ? 14.304  39.799  182.806 1.00 33.35  ? 228 TRP A CD1   1 
ATOM   1535  C CD2   . TRP A  1 228 ? 13.834  40.517  184.871 1.00 35.20  ? 228 TRP A CD2   1 
ATOM   1536  N NE1   . TRP A  1 228 ? 15.384  39.509  183.606 1.00 32.25  ? 228 TRP A NE1   1 
ATOM   1537  C CE2   . TRP A  1 228 ? 15.120  39.942  184.879 1.00 31.92  ? 228 TRP A CE2   1 
ATOM   1538  C CE3   . TRP A  1 228 ? 13.321  41.041  186.061 1.00 34.89  ? 228 TRP A CE3   1 
ATOM   1539  C CZ2   . TRP A  1 228 ? 15.898  39.874  186.030 1.00 34.05  ? 228 TRP A CZ2   1 
ATOM   1540  C CZ3   . TRP A  1 228 ? 14.094  40.974  187.201 1.00 37.32  ? 228 TRP A CZ3   1 
ATOM   1541  C CH2   . TRP A  1 228 ? 15.370  40.395  187.179 1.00 37.27  ? 228 TRP A CH2   1 
ATOM   1542  N N     . GLY A  1 229 ? 9.389   39.257  181.676 1.00 31.44  ? 229 GLY A N     1 
ATOM   1543  C CA    . GLY A  1 229 ? 8.332   39.473  180.711 1.00 30.74  ? 229 GLY A CA    1 
ATOM   1544  C C     . GLY A  1 229 ? 8.895   39.101  179.358 1.00 34.23  ? 229 GLY A C     1 
ATOM   1545  O O     . GLY A  1 229 ? 9.991   38.548  179.273 1.00 27.76  ? 229 GLY A O     1 
ATOM   1546  N N     . ALA A  1 230 ? 8.159   39.406  178.299 1.00 26.35  ? 230 ALA A N     1 
ATOM   1547  C CA    . ALA A  1 230 ? 8.629   39.097  176.958 1.00 28.29  ? 230 ALA A CA    1 
ATOM   1548  C C     . ALA A  1 230 ? 9.176   40.342  176.281 1.00 30.25  ? 230 ALA A C     1 
ATOM   1549  O O     . ALA A  1 230 ? 8.438   41.292  176.031 1.00 28.76  ? 230 ALA A O     1 
ATOM   1550  C CB    . ALA A  1 230 ? 7.509   38.486  176.127 1.00 29.62  ? 230 ALA A CB    1 
ATOM   1551  N N     . ILE A  1 231 ? 10.477  40.345  176.006 1.00 29.35  ? 231 ILE A N     1 
ATOM   1552  C CA    . ILE A  1 231 ? 11.072  41.416  175.218 1.00 28.71  ? 231 ILE A CA    1 
ATOM   1553  C C     . ILE A  1 231 ? 10.516  41.340  173.808 1.00 31.26  ? 231 ILE A C     1 
ATOM   1554  O O     . ILE A  1 231 ? 10.663  40.317  173.145 1.00 26.16  ? 231 ILE A O     1 
ATOM   1555  C CB    . ILE A  1 231 ? 12.610  41.318  175.158 1.00 26.96  ? 231 ILE A CB    1 
ATOM   1556  C CG1   . ILE A  1 231 ? 13.219  41.412  176.560 1.00 31.26  ? 231 ILE A CG1   1 
ATOM   1557  C CG2   . ILE A  1 231 ? 13.169  42.412  174.263 1.00 26.31  ? 231 ILE A CG2   1 
ATOM   1558  C CD1   . ILE A  1 231 ? 13.207  42.811  177.137 1.00 29.25  ? 231 ILE A CD1   1 
ATOM   1559  N N     . TYR A  1 232 ? 9.863   42.404  173.352 1.00 29.57  ? 232 TYR A N     1 
ATOM   1560  C CA    . TYR A  1 232 ? 9.406   42.440  171.969 1.00 30.97  ? 232 TYR A CA    1 
ATOM   1561  C C     . TYR A  1 232 ? 10.541  42.900  171.064 1.00 28.87  ? 232 TYR A C     1 
ATOM   1562  O O     . TYR A  1 232 ? 10.782  42.306  170.014 1.00 30.75  ? 232 TYR A O     1 
ATOM   1563  C CB    . TYR A  1 232 ? 8.194   43.358  171.786 1.00 25.22  ? 232 TYR A CB    1 
ATOM   1564  C CG    . TYR A  1 232 ? 8.047   43.817  170.350 1.00 27.37  ? 232 TYR A CG    1 
ATOM   1565  C CD1   . TYR A  1 232 ? 7.723   42.916  169.342 1.00 30.96  ? 232 TYR A CD1   1 
ATOM   1566  C CD2   . TYR A  1 232 ? 8.263   45.144  169.999 1.00 33.30  ? 232 TYR A CD2   1 
ATOM   1567  C CE1   . TYR A  1 232 ? 7.607   43.325  168.028 1.00 30.61  ? 232 TYR A CE1   1 
ATOM   1568  C CE2   . TYR A  1 232 ? 8.151   45.562  168.687 1.00 33.17  ? 232 TYR A CE2   1 
ATOM   1569  C CZ    . TYR A  1 232 ? 7.822   44.649  167.707 1.00 31.09  ? 232 TYR A CZ    1 
ATOM   1570  O OH    . TYR A  1 232 ? 7.711   45.062  166.400 1.00 31.35  ? 232 TYR A OH    1 
ATOM   1571  N N     . ALA A  1 233 ? 11.238  43.956  171.473 1.00 28.39  ? 233 ALA A N     1 
ATOM   1572  C CA    . ALA A  1 233 ? 12.312  44.509  170.657 1.00 30.42  ? 233 ALA A CA    1 
ATOM   1573  C C     . ALA A  1 233 ? 13.401  45.191  171.481 1.00 27.73  ? 233 ALA A C     1 
ATOM   1574  O O     . ALA A  1 233 ? 13.146  45.706  172.569 1.00 31.75  ? 233 ALA A O     1 
ATOM   1575  C CB    . ALA A  1 233 ? 11.742  45.489  169.640 1.00 27.01  ? 233 ALA A CB    1 
ATOM   1576  N N     . TRP A  1 234 ? 14.617  45.188  170.944 1.00 30.99  ? 234 TRP A N     1 
ATOM   1577  C CA    . TRP A  1 234 ? 15.728  45.928  171.529 1.00 27.97  ? 234 TRP A CA    1 
ATOM   1578  C C     . TRP A  1 234 ? 16.022  47.166  170.700 1.00 29.26  ? 234 TRP A C     1 
ATOM   1579  O O     . TRP A  1 234 ? 15.999  47.112  169.469 1.00 29.03  ? 234 TRP A O     1 
ATOM   1580  C CB    . TRP A  1 234 ? 16.999  45.074  171.605 1.00 31.63  ? 234 TRP A CB    1 
ATOM   1581  C CG    . TRP A  1 234 ? 16.870  43.774  172.331 1.00 28.46  ? 234 TRP A CG    1 
ATOM   1582  C CD1   . TRP A  1 234 ? 16.727  42.535  171.774 1.00 30.67  ? 234 TRP A CD1   1 
ATOM   1583  C CD2   . TRP A  1 234 ? 16.905  43.575  173.749 1.00 29.57  ? 234 TRP A CD2   1 
ATOM   1584  N NE1   . TRP A  1 234 ? 16.658  41.579  172.759 1.00 29.72  ? 234 TRP A NE1   1 
ATOM   1585  C CE2   . TRP A  1 234 ? 16.764  42.192  173.981 1.00 28.72  ? 234 TRP A CE2   1 
ATOM   1586  C CE3   . TRP A  1 234 ? 17.036  44.432  174.845 1.00 27.42  ? 234 TRP A CE3   1 
ATOM   1587  C CZ2   . TRP A  1 234 ? 16.750  41.647  175.264 1.00 28.90  ? 234 TRP A CZ2   1 
ATOM   1588  C CZ3   . TRP A  1 234 ? 17.020  43.890  176.119 1.00 24.99  ? 234 TRP A CZ3   1 
ATOM   1589  C CH2   . TRP A  1 234 ? 16.876  42.511  176.317 1.00 29.68  ? 234 TRP A CH2   1 
ATOM   1590  N N     . LYS A  1 235 ? 16.304  48.279  171.367 1.00 28.41  ? 235 LYS A N     1 
ATOM   1591  C CA    . LYS A  1 235 ? 16.894  49.418  170.682 1.00 28.63  ? 235 LYS A CA    1 
ATOM   1592  C C     . LYS A  1 235 ? 18.378  49.475  171.026 1.00 31.15  ? 235 LYS A C     1 
ATOM   1593  O O     . LYS A  1 235 ? 18.753  49.749  172.168 1.00 29.78  ? 235 LYS A O     1 
ATOM   1594  C CB    . LYS A  1 235 ? 16.202  50.729  171.057 1.00 30.67  ? 235 LYS A CB    1 
ATOM   1595  C CG    . LYS A  1 235 ? 16.603  51.882  170.147 1.00 31.80  ? 235 LYS A CG    1 
ATOM   1596  C CD    . LYS A  1 235 ? 15.940  53.188  170.542 1.00 36.38  ? 235 LYS A CD    1 
ATOM   1597  C CE    . LYS A  1 235 ? 16.354  54.304  169.602 1.00 37.68  ? 235 LYS A CE    1 
ATOM   1598  N NZ    . LYS A  1 235 ? 15.840  55.619  170.063 1.00 36.76  ? 235 LYS A NZ    1 
ATOM   1599  N N     . ILE A  1 236 ? 19.219  49.200  170.037 1.00 30.37  ? 236 ILE A N     1 
ATOM   1600  C CA    . ILE A  1 236 ? 20.656  49.131  170.262 1.00 31.32  ? 236 ILE A CA    1 
ATOM   1601  C C     . ILE A  1 236 ? 21.396  50.301  169.631 1.00 37.26  ? 236 ILE A C     1 
ATOM   1602  O O     . ILE A  1 236 ? 20.931  50.898  168.658 1.00 36.57  ? 236 ILE A O     1 
ATOM   1603  C CB    . ILE A  1 236 ? 21.251  47.821  169.706 1.00 37.61  ? 236 ILE A CB    1 
ATOM   1604  C CG1   . ILE A  1 236 ? 20.982  47.712  168.203 1.00 33.35  ? 236 ILE A CG1   1 
ATOM   1605  C CG2   . ILE A  1 236 ? 20.689  46.618  170.449 1.00 29.94  ? 236 ILE A CG2   1 
ATOM   1606  C CD1   . ILE A  1 236 ? 21.665  46.537  167.546 1.00 26.42  ? 236 ILE A CD1   1 
ATOM   1607  N N     . LYS A  1 237 ? 22.548  50.630  170.201 1.00 36.12  ? 237 LYS A N     1 
ATOM   1608  C CA    . LYS A  1 237 ? 23.445  51.596  169.586 1.00 38.41  ? 237 LYS A CA    1 
ATOM   1609  C C     . LYS A  1 237 ? 24.339  50.879  168.586 1.00 35.66  ? 237 LYS A C     1 
ATOM   1610  O O     . LYS A  1 237 ? 24.985  49.888  168.925 1.00 33.64  ? 237 LYS A O     1 
ATOM   1611  C CB    . LYS A  1 237 ? 24.288  52.308  170.644 1.00 33.90  ? 237 LYS A CB    1 
ATOM   1612  C CG    . LYS A  1 237 ? 25.236  53.358  170.077 1.00 44.35  ? 237 LYS A CG    1 
ATOM   1613  C CD    . LYS A  1 237 ? 24.476  54.563  169.540 1.00 43.88  ? 237 LYS A CD    1 
ATOM   1614  C CE    . LYS A  1 237 ? 25.409  55.535  168.832 1.00 44.82  ? 237 LYS A CE    1 
ATOM   1615  N NZ    . LYS A  1 237 ? 24.708  56.789  168.453 1.00 47.09  ? 237 LYS A NZ    1 
ATOM   1616  N N     . LEU A  1 238 ? 24.362  51.360  167.349 1.00 37.08  ? 238 LEU A N     1 
ATOM   1617  C CA    . LEU A  1 238 ? 25.271  50.803  166.357 1.00 35.28  ? 238 LEU A CA    1 
ATOM   1618  C C     . LEU A  1 238 ? 26.659  51.398  166.577 1.00 39.25  ? 238 LEU A C     1 
ATOM   1619  O O     . LEU A  1 238 ? 26.791  52.569  166.937 1.00 38.90  ? 238 LEU A O     1 
ATOM   1620  C CB    . LEU A  1 238 ? 24.766  51.070  164.937 1.00 32.20  ? 238 LEU A CB    1 
ATOM   1621  C CG    . LEU A  1 238 ? 23.415  50.425  164.600 1.00 37.29  ? 238 LEU A CG    1 
ATOM   1622  C CD1   . LEU A  1 238 ? 23.001  50.732  163.169 1.00 34.61  ? 238 LEU A CD1   1 
ATOM   1623  C CD2   . LEU A  1 238 ? 23.451  48.920  164.842 1.00 35.74  ? 238 LEU A CD2   1 
ATOM   1624  N N     . LEU A  1 239 ? 27.691  50.588  166.376 1.00 38.33  ? 239 LEU A N     1 
ATOM   1625  C CA    . LEU A  1 239 ? 29.038  50.969  166.784 1.00 43.58  ? 239 LEU A CA    1 
ATOM   1626  C C     . LEU A  1 239 ? 29.973  51.147  165.596 1.00 42.81  ? 239 LEU A C     1 
ATOM   1627  O O     . LEU A  1 239 ? 29.968  50.334  164.670 1.00 40.48  ? 239 LEU A O     1 
ATOM   1628  C CB    . LEU A  1 239 ? 29.602  49.921  167.741 1.00 42.96  ? 239 LEU A CB    1 
ATOM   1629  C CG    . LEU A  1 239 ? 28.617  49.496  168.833 1.00 41.22  ? 239 LEU A CG    1 
ATOM   1630  C CD1   . LEU A  1 239 ? 29.077  48.215  169.492 1.00 39.59  ? 239 LEU A CD1   1 
ATOM   1631  C CD2   . LEU A  1 239 ? 28.441  50.606  169.860 1.00 38.91  ? 239 LEU A CD2   1 
ATOM   1632  N N     . PRO A  1 240 ? 30.785  52.217  165.624 1.00 42.73  ? 240 PRO A N     1 
ATOM   1633  C CA    . PRO A  1 240 ? 31.761  52.509  164.569 1.00 47.38  ? 240 PRO A CA    1 
ATOM   1634  C C     . PRO A  1 240 ? 32.732  51.356  164.337 1.00 41.54  ? 240 PRO A C     1 
ATOM   1635  O O     . PRO A  1 240 ? 33.287  50.810  165.291 1.00 41.39  ? 240 PRO A O     1 
ATOM   1636  C CB    . PRO A  1 240 ? 32.500  53.740  165.104 1.00 47.97  ? 240 PRO A CB    1 
ATOM   1637  C CG    . PRO A  1 240 ? 31.528  54.388  166.024 1.00 43.79  ? 240 PRO A CG    1 
ATOM   1638  C CD    . PRO A  1 240 ? 30.776  53.259  166.665 1.00 42.46  ? 240 PRO A CD    1 
ATOM   1639  N N     . VAL A  1 241 ? 32.909  50.981  163.075 1.00 42.15  ? 241 VAL A N     1 
ATOM   1640  C CA    . VAL A  1 241 ? 33.888  49.974  162.689 1.00 42.87  ? 241 VAL A CA    1 
ATOM   1641  C C     . VAL A  1 241 ? 34.619  50.455  161.443 1.00 47.21  ? 241 VAL A C     1 
ATOM   1642  O O     . VAL A  1 241 ? 34.041  51.171  160.626 1.00 47.47  ? 241 VAL A O     1 
ATOM   1643  C CB    . VAL A  1 241 ? 33.236  48.597  162.418 1.00 46.14  ? 241 VAL A CB    1 
ATOM   1644  C CG1   . VAL A  1 241 ? 32.640  48.025  163.695 1.00 41.77  ? 241 VAL A CG1   1 
ATOM   1645  C CG2   . VAL A  1 241 ? 32.183  48.696  161.321 1.00 44.53  ? 241 VAL A CG2   1 
ATOM   1646  N N     . PRO A  1 242 ? 35.898  50.076  161.296 1.00 45.64  ? 242 PRO A N     1 
ATOM   1647  C CA    . PRO A  1 242 ? 36.653  50.498  160.114 1.00 50.03  ? 242 PRO A CA    1 
ATOM   1648  C C     . PRO A  1 242 ? 36.078  49.859  158.857 1.00 47.20  ? 242 PRO A C     1 
ATOM   1649  O O     . PRO A  1 242 ? 35.395  48.842  158.961 1.00 50.61  ? 242 PRO A O     1 
ATOM   1650  C CB    . PRO A  1 242 ? 38.074  49.988  160.398 1.00 45.66  ? 242 PRO A CB    1 
ATOM   1651  C CG    . PRO A  1 242 ? 38.104  49.717  161.879 1.00 45.80  ? 242 PRO A CG    1 
ATOM   1652  C CD    . PRO A  1 242 ? 36.721  49.256  162.200 1.00 42.70  ? 242 PRO A CD    1 
ATOM   1653  N N     . GLU A  1 243 ? 36.347  50.449  157.696 1.00 49.39  ? 243 GLU A N     1 
ATOM   1654  C CA    . GLU A  1 243 ? 35.899  49.890  156.425 1.00 50.99  ? 243 GLU A CA    1 
ATOM   1655  C C     . GLU A  1 243 ? 36.543  48.531  156.201 1.00 51.39  ? 243 GLU A C     1 
ATOM   1656  O O     . GLU A  1 243 ? 35.960  47.643  155.578 1.00 54.11  ? 243 GLU A O     1 
ATOM   1657  C CB    . GLU A  1 243 ? 36.235  50.837  155.275 1.00 50.55  ? 243 GLU A CB    1 
ATOM   1658  C CG    . GLU A  1 243 ? 35.584  52.204  155.385 1.00 62.94  ? 243 GLU A CG    1 
ATOM   1659  C CD    . GLU A  1 243 ? 34.251  52.272  154.669 1.00 69.64  ? 243 GLU A CD    1 
ATOM   1660  O OE1   . GLU A  1 243 ? 33.773  51.220  154.194 1.00 70.18  ? 243 GLU A OE1   1 
ATOM   1661  O OE2   . GLU A  1 243 ? 33.684  53.380  154.571 1.00 78.63  ? 243 GLU A OE2   1 
ATOM   1662  N N     . LYS A  1 244 ? 37.753  48.383  156.726 1.00 48.25  ? 244 LYS A N     1 
ATOM   1663  C CA    . LYS A  1 244 ? 38.472  47.121  156.667 1.00 51.73  ? 244 LYS A CA    1 
ATOM   1664  C C     . LYS A  1 244 ? 38.994  46.743  158.048 1.00 45.48  ? 244 LYS A C     1 
ATOM   1665  O O     . LYS A  1 244 ? 39.634  47.552  158.717 1.00 45.80  ? 244 LYS A O     1 
ATOM   1666  C CB    . LYS A  1 244 ? 39.627  47.211  155.668 1.00 54.02  ? 244 LYS A CB    1 
ATOM   1667  C CG    . LYS A  1 244 ? 39.533  46.217  154.524 1.00 58.24  ? 244 LYS A CG    1 
ATOM   1668  C CD    . LYS A  1 244 ? 38.208  46.364  153.791 1.00 66.55  ? 244 LYS A CD    1 
ATOM   1669  C CE    . LYS A  1 244 ? 38.021  45.294  152.727 1.00 73.13  ? 244 LYS A CE    1 
ATOM   1670  N NZ    . LYS A  1 244 ? 36.604  45.230  152.259 1.00 83.99  ? 244 LYS A NZ    1 
ATOM   1671  N N     . VAL A  1 245 ? 38.704  45.521  158.482 1.00 47.44  ? 245 VAL A N     1 
ATOM   1672  C CA    . VAL A  1 245 ? 39.255  45.012  159.734 1.00 43.08  ? 245 VAL A CA    1 
ATOM   1673  C C     . VAL A  1 245 ? 40.122  43.800  159.434 1.00 40.68  ? 245 VAL A C     1 
ATOM   1674  O O     . VAL A  1 245 ? 40.158  43.329  158.299 1.00 42.42  ? 245 VAL A O     1 
ATOM   1675  C CB    . VAL A  1 245 ? 38.158  44.626  160.752 1.00 43.53  ? 245 VAL A CB    1 
ATOM   1676  C CG1   . VAL A  1 245 ? 37.318  45.834  161.110 1.00 39.17  ? 245 VAL A CG1   1 
ATOM   1677  C CG2   . VAL A  1 245 ? 37.286  43.500  160.215 1.00 44.52  ? 245 VAL A CG2   1 
ATOM   1678  N N     . THR A  1 246 ? 40.816  43.289  160.444 1.00 39.58  ? 246 THR A N     1 
ATOM   1679  C CA    . THR A  1 246 ? 41.708  42.157  160.218 1.00 38.26  ? 246 THR A CA    1 
ATOM   1680  C C     . THR A  1 246 ? 41.408  40.971  161.133 1.00 40.07  ? 246 THR A C     1 
ATOM   1681  O O     . THR A  1 246 ? 41.251  41.124  162.345 1.00 40.57  ? 246 THR A O     1 
ATOM   1682  C CB    . THR A  1 246 ? 43.188  42.558  160.401 1.00 42.84  ? 246 THR A CB    1 
ATOM   1683  O OG1   . THR A  1 246 ? 43.469  43.735  159.632 1.00 40.10  ? 246 THR A OG1   1 
ATOM   1684  C CG2   . THR A  1 246 ? 44.103  41.430  159.945 1.00 39.36  ? 246 THR A CG2   1 
ATOM   1685  N N     . VAL A  1 247 ? 41.331  39.786  160.535 1.00 41.10  ? 247 VAL A N     1 
ATOM   1686  C CA    . VAL A  1 247 ? 41.149  38.552  161.287 1.00 39.29  ? 247 VAL A CA    1 
ATOM   1687  C C     . VAL A  1 247 ? 42.174  37.515  160.854 1.00 46.42  ? 247 VAL A C     1 
ATOM   1688  O O     . VAL A  1 247 ? 42.743  37.609  159.766 1.00 52.52  ? 247 VAL A O     1 
ATOM   1689  C CB    . VAL A  1 247 ? 39.732  37.968  161.102 1.00 46.19  ? 247 VAL A CB    1 
ATOM   1690  C CG1   . VAL A  1 247 ? 38.680  38.930  161.633 1.00 44.73  ? 247 VAL A CG1   1 
ATOM   1691  C CG2   . VAL A  1 247 ? 39.475  37.648  159.642 1.00 44.53  ? 247 VAL A CG2   1 
ATOM   1692  N N     . PHE A  1 248 ? 42.415  36.534  161.717 1.00 44.52  ? 248 PHE A N     1 
ATOM   1693  C CA    . PHE A  1 248 ? 43.213  35.376  161.345 1.00 50.16  ? 248 PHE A CA    1 
ATOM   1694  C C     . PHE A  1 248 ? 42.783  34.155  162.150 1.00 53.14  ? 248 PHE A C     1 
ATOM   1695  O O     . PHE A  1 248 ? 42.351  34.275  163.296 1.00 55.59  ? 248 PHE A O     1 
ATOM   1696  C CB    . PHE A  1 248 ? 44.715  35.643  161.525 1.00 51.59  ? 248 PHE A CB    1 
ATOM   1697  C CG    . PHE A  1 248 ? 45.120  36.016  162.929 1.00 44.63  ? 248 PHE A CG    1 
ATOM   1698  C CD1   . PHE A  1 248 ? 45.300  35.044  163.902 1.00 49.45  ? 248 PHE A CD1   1 
ATOM   1699  C CD2   . PHE A  1 248 ? 45.360  37.340  163.261 1.00 46.48  ? 248 PHE A CD2   1 
ATOM   1700  C CE1   . PHE A  1 248 ? 45.679  35.387  165.184 1.00 47.65  ? 248 PHE A CE1   1 
ATOM   1701  C CE2   . PHE A  1 248 ? 45.744  37.690  164.543 1.00 47.55  ? 248 PHE A CE2   1 
ATOM   1702  C CZ    . PHE A  1 248 ? 45.904  36.712  165.505 1.00 43.08  ? 248 PHE A CZ    1 
ATOM   1703  N N     . ARG A  1 249 ? 42.892  32.982  161.535 1.00 58.59  ? 249 ARG A N     1 
ATOM   1704  C CA    . ARG A  1 249 ? 42.557  31.724  162.194 1.00 55.18  ? 249 ARG A CA    1 
ATOM   1705  C C     . ARG A  1 249 ? 43.669  30.716  161.961 1.00 64.72  ? 249 ARG A C     1 
ATOM   1706  O O     . ARG A  1 249 ? 43.786  30.151  160.875 1.00 67.06  ? 249 ARG A O     1 
ATOM   1707  C CB    . ARG A  1 249 ? 41.222  31.176  161.683 1.00 64.22  ? 249 ARG A CB    1 
ATOM   1708  C CG    . ARG A  1 249 ? 40.905  29.774  162.189 1.00 64.17  ? 249 ARG A CG    1 
ATOM   1709  C CD    . ARG A  1 249 ? 39.422  29.438  162.063 1.00 69.14  ? 249 ARG A CD    1 
ATOM   1710  N NE    . ARG A  1 249 ? 38.950  29.425  160.682 1.00 73.10  ? 249 ARG A NE    1 
ATOM   1711  C CZ    . ARG A  1 249 ? 37.780  29.920  160.290 1.00 76.47  ? 249 ARG A CZ    1 
ATOM   1712  N NH1   . ARG A  1 249 ? 37.425  29.863  159.014 1.00 75.68  ? 249 ARG A NH1   1 
ATOM   1713  N NH2   . ARG A  1 249 ? 36.964  30.478  161.175 1.00 68.30  ? 249 ARG A NH2   1 
ATOM   1714  N N     . VAL A  1 250 ? 44.490  30.496  162.980 1.00 58.61  ? 250 VAL A N     1 
ATOM   1715  C CA    . VAL A  1 250 ? 45.640  29.613  162.837 1.00 61.16  ? 250 VAL A CA    1 
ATOM   1716  C C     . VAL A  1 250 ? 45.604  28.484  163.858 1.00 59.30  ? 250 VAL A C     1 
ATOM   1717  O O     . VAL A  1 250 ? 45.468  28.716  165.058 1.00 55.50  ? 250 VAL A O     1 
ATOM   1718  C CB    . VAL A  1 250 ? 46.961  30.392  162.963 1.00 57.14  ? 250 VAL A CB    1 
ATOM   1719  C CG1   . VAL A  1 250 ? 48.132  29.447  163.181 1.00 59.75  ? 250 VAL A CG1   1 
ATOM   1720  C CG2   . VAL A  1 250 ? 47.180  31.227  161.717 1.00 63.34  ? 250 VAL A CG2   1 
ATOM   1721  N N     . THR A  1 251 ? 45.721  27.257  163.362 1.00 56.26  ? 251 THR A N     1 
ATOM   1722  C CA    . THR A  1 251 ? 45.620  26.073  164.202 1.00 57.10  ? 251 THR A CA    1 
ATOM   1723  C C     . THR A  1 251 ? 46.992  25.475  164.486 1.00 60.01  ? 251 THR A C     1 
ATOM   1724  O O     . THR A  1 251 ? 47.777  25.239  163.567 1.00 56.78  ? 251 THR A O     1 
ATOM   1725  C CB    . THR A  1 251 ? 44.725  25.007  163.549 1.00 54.54  ? 251 THR A CB    1 
ATOM   1726  O OG1   . THR A  1 251 ? 43.501  25.611  163.110 1.00 59.83  ? 251 THR A OG1   1 
ATOM   1727  C CG2   . THR A  1 251 ? 44.418  23.891  164.540 1.00 55.87  ? 251 THR A CG2   1 
ATOM   1728  N N     . LYS A  1 252 ? 47.282  25.237  165.760 1.00 55.01  ? 252 LYS A N     1 
ATOM   1729  C CA    . LYS A  1 252 ? 48.547  24.625  166.133 1.00 56.50  ? 252 LYS A CA    1 
ATOM   1730  C C     . LYS A  1 252 ? 48.345  23.219  166.669 1.00 62.28  ? 252 LYS A C     1 
ATOM   1731  O O     . LYS A  1 252 ? 47.727  23.019  167.713 1.00 58.51  ? 252 LYS A O     1 
ATOM   1732  C CB    . LYS A  1 252 ? 49.282  25.480  167.166 1.00 55.15  ? 252 LYS A CB    1 
ATOM   1733  C CG    . LYS A  1 252 ? 50.101  26.597  166.547 1.00 58.29  ? 252 LYS A CG    1 
ATOM   1734  C CD    . LYS A  1 252 ? 51.326  26.909  167.382 1.00 60.09  ? 252 LYS A CD    1 
ATOM   1735  C CE    . LYS A  1 252 ? 52.519  27.219  166.496 1.00 66.07  ? 252 LYS A CE    1 
ATOM   1736  N NZ    . LYS A  1 252 ? 52.188  28.265  165.490 1.00 68.98  ? 252 LYS A NZ    1 
ATOM   1737  N N     . ASN A  1 253 ? 48.864  22.243  165.934 1.00 63.00  ? 253 ASN A N     1 
ATOM   1738  C CA    . ASN A  1 253 ? 48.831  20.857  166.375 1.00 62.32  ? 253 ASN A CA    1 
ATOM   1739  C C     . ASN A  1 253 ? 50.137  20.489  167.070 1.00 62.07  ? 253 ASN A C     1 
ATOM   1740  O O     . ASN A  1 253 ? 51.139  20.203  166.416 1.00 60.06  ? 253 ASN A O     1 
ATOM   1741  C CB    . ASN A  1 253 ? 48.573  19.925  165.193 1.00 60.11  ? 253 ASN A CB    1 
ATOM   1742  C CG    . ASN A  1 253 ? 47.256  20.215  164.500 1.00 66.18  ? 253 ASN A CG    1 
ATOM   1743  O OD1   . ASN A  1 253 ? 46.207  19.710  164.901 1.00 65.81  ? 253 ASN A OD1   1 
ATOM   1744  N ND2   . ASN A  1 253 ? 47.305  21.024  163.448 1.00 63.32  ? 253 ASN A ND2   1 
ATOM   1745  N N     . VAL A  1 254 ? 50.122  20.508  168.399 1.00 59.19  ? 254 VAL A N     1 
ATOM   1746  C CA    . VAL A  1 254 ? 51.329  20.292  169.189 1.00 61.58  ? 254 VAL A CA    1 
ATOM   1747  C C     . VAL A  1 254 ? 51.087  19.319  170.337 1.00 67.04  ? 254 VAL A C     1 
ATOM   1748  O O     . VAL A  1 254 ? 49.973  18.827  170.519 1.00 68.66  ? 254 VAL A O     1 
ATOM   1749  C CB    . VAL A  1 254 ? 51.859  21.614  169.776 1.00 62.86  ? 254 VAL A CB    1 
ATOM   1750  C CG1   . VAL A  1 254 ? 52.124  22.626  168.665 1.00 64.51  ? 254 VAL A CG1   1 
ATOM   1751  C CG2   . VAL A  1 254 ? 50.873  22.168  170.794 1.00 58.86  ? 254 VAL A CG2   1 
ATOM   1752  N N     . ALA A  1 255 ? 52.136  19.051  171.111 1.00 64.22  ? 255 ALA A N     1 
ATOM   1753  C CA    . ALA A  1 255 ? 52.031  18.190  172.287 1.00 66.03  ? 255 ALA A CA    1 
ATOM   1754  C C     . ALA A  1 255 ? 51.538  18.967  173.501 1.00 60.26  ? 255 ALA A C     1 
ATOM   1755  O O     . ALA A  1 255 ? 51.594  20.198  173.521 1.00 65.43  ? 255 ALA A O     1 
ATOM   1756  C CB    . ALA A  1 255 ? 53.366  17.545  172.593 1.00 72.72  ? 255 ALA A CB    1 
ATOM   1757  N N     . ILE A  1 256 ? 51.077  18.225  174.507 1.00 63.04  ? 256 ILE A N     1 
ATOM   1758  C CA    . ILE A  1 256 ? 50.584  18.775  175.767 1.00 60.67  ? 256 ILE A CA    1 
ATOM   1759  C C     . ILE A  1 256 ? 51.567  19.771  176.395 1.00 61.41  ? 256 ILE A C     1 
ATOM   1760  O O     . ILE A  1 256 ? 51.159  20.791  176.954 1.00 60.37  ? 256 ILE A O     1 
ATOM   1761  C CB    . ILE A  1 256 ? 50.287  17.634  176.784 1.00 63.58  ? 256 ILE A CB    1 
ATOM   1762  C CG1   . ILE A  1 256 ? 49.256  16.660  176.202 1.00 72.35  ? 256 ILE A CG1   1 
ATOM   1763  C CG2   . ILE A  1 256 ? 49.806  18.199  178.119 1.00 68.31  ? 256 ILE A CG2   1 
ATOM   1764  C CD1   . ILE A  1 256 ? 48.933  15.476  177.095 1.00 75.60  ? 256 ILE A CD1   1 
ATOM   1765  N N     . ASP A  1 257 ? 52.861  19.492  176.268 1.00 62.36  ? 257 ASP A N     1 
ATOM   1766  C CA    . ASP A  1 257 ? 53.889  20.335  176.869 1.00 59.67  ? 257 ASP A CA    1 
ATOM   1767  C C     . ASP A  1 257 ? 54.004  21.708  176.205 1.00 57.81  ? 257 ASP A C     1 
ATOM   1768  O O     . ASP A  1 257 ? 54.086  22.726  176.892 1.00 53.00  ? 257 ASP A O     1 
ATOM   1769  C CB    . ASP A  1 257 ? 55.234  19.614  176.827 1.00 63.75  ? 257 ASP A CB    1 
ATOM   1770  C CG    . ASP A  1 257 ? 55.159  18.219  177.415 1.00 72.73  ? 257 ASP A CG    1 
ATOM   1771  O OD1   . ASP A  1 257 ? 55.323  18.082  178.647 1.00 74.53  ? 257 ASP A OD1   1 
ATOM   1772  O OD2   . ASP A  1 257 ? 54.935  17.258  176.649 1.00 70.32  ? 257 ASP A OD2   1 
ATOM   1773  N N     . GLU A  1 258 ? 54.026  21.741  174.876 1.00 55.47  ? 258 GLU A N     1 
ATOM   1774  C CA    . GLU A  1 258 ? 54.091  23.013  174.164 1.00 53.49  ? 258 GLU A CA    1 
ATOM   1775  C C     . GLU A  1 258 ? 52.764  23.753  174.292 1.00 57.11  ? 258 GLU A C     1 
ATOM   1776  O O     . GLU A  1 258 ? 52.735  24.965  174.521 1.00 56.25  ? 258 GLU A O     1 
ATOM   1777  C CB    . GLU A  1 258 ? 54.442  22.803  172.693 1.00 51.70  ? 258 GLU A CB    1 
ATOM   1778  C CG    . GLU A  1 258 ? 54.588  24.094  171.910 1.00 56.10  ? 258 GLU A CG    1 
ATOM   1779  C CD    . GLU A  1 258 ? 54.883  23.855  170.446 1.00 61.04  ? 258 GLU A CD    1 
ATOM   1780  O OE1   . GLU A  1 258 ? 55.049  22.680  170.060 1.00 63.62  ? 258 GLU A OE1   1 
ATOM   1781  O OE2   . GLU A  1 258 ? 54.946  24.840  169.680 1.00 62.95  ? 258 GLU A OE2   1 
ATOM   1782  N N     . ALA A  1 259 ? 51.671  23.010  174.147 1.00 52.65  ? 259 ALA A N     1 
ATOM   1783  C CA    . ALA A  1 259 ? 50.323  23.549  174.295 1.00 53.62  ? 259 ALA A CA    1 
ATOM   1784  C C     . ALA A  1 259 ? 50.136  24.263  175.622 1.00 53.89  ? 259 ALA A C     1 
ATOM   1785  O O     . ALA A  1 259 ? 49.547  25.341  175.684 1.00 54.03  ? 259 ALA A O     1 
ATOM   1786  C CB    . ALA A  1 259 ? 49.322  22.448  174.173 1.00 52.73  ? 259 ALA A CB    1 
ATOM   1787  N N     . THR A  1 260 ? 50.643  23.641  176.680 1.00 48.97  ? 260 THR A N     1 
ATOM   1788  C CA    . THR A  1 260 ? 50.550  24.188  178.024 1.00 46.73  ? 260 THR A CA    1 
ATOM   1789  C C     . THR A  1 260 ? 51.268  25.530  178.113 1.00 54.05  ? 260 THR A C     1 
ATOM   1790  O O     . THR A  1 260 ? 50.786  26.461  178.758 1.00 54.95  ? 260 THR A O     1 
ATOM   1791  C CB    . THR A  1 260 ? 51.142  23.213  179.059 1.00 49.86  ? 260 THR A CB    1 
ATOM   1792  O OG1   . THR A  1 260 ? 50.471  21.951  178.957 1.00 51.23  ? 260 THR A OG1   1 
ATOM   1793  C CG2   . THR A  1 260 ? 50.983  23.756  180.467 1.00 52.25  ? 260 THR A CG2   1 
ATOM   1794  N N     . SER A  1 261 ? 52.410  25.631  177.440 1.00 54.51  ? 261 SER A N     1 
ATOM   1795  C CA    . SER A  1 261 ? 53.202  26.855  177.461 1.00 50.10  ? 261 SER A CA    1 
ATOM   1796  C C     . SER A  1 261 ? 52.572  27.936  176.586 1.00 46.62  ? 261 SER A C     1 
ATOM   1797  O O     . SER A  1 261 ? 52.631  29.118  176.919 1.00 44.04  ? 261 SER A O     1 
ATOM   1798  C CB    . SER A  1 261 ? 54.640  26.581  177.007 1.00 50.19  ? 261 SER A CB    1 
ATOM   1799  O OG    . SER A  1 261 ? 54.791  26.784  175.612 1.00 51.70  ? 261 SER A OG    1 
ATOM   1800  N N     . LEU A  1 262 ? 51.987  27.529  175.463 1.00 49.31  ? 262 LEU A N     1 
ATOM   1801  C CA    . LEU A  1 262 ? 51.258  28.455  174.600 1.00 50.38  ? 262 LEU A CA    1 
ATOM   1802  C C     . LEU A  1 262 ? 50.075  29.071  175.342 1.00 46.14  ? 262 LEU A C     1 
ATOM   1803  O O     . LEU A  1 262 ? 49.868  30.284  175.305 1.00 46.68  ? 262 LEU A O     1 
ATOM   1804  C CB    . LEU A  1 262 ? 50.773  27.745  173.334 1.00 50.41  ? 262 LEU A CB    1 
ATOM   1805  C CG    . LEU A  1 262 ? 51.804  27.512  172.230 1.00 55.35  ? 262 LEU A CG    1 
ATOM   1806  C CD1   . LEU A  1 262 ? 51.238  26.600  171.153 1.00 52.48  ? 262 LEU A CD1   1 
ATOM   1807  C CD2   . LEU A  1 262 ? 52.244  28.839  171.634 1.00 47.30  ? 262 LEU A CD2   1 
ATOM   1808  N N     . LEU A  1 263 ? 49.306  28.224  176.020 1.00 49.57  ? 263 LEU A N     1 
ATOM   1809  C CA    . LEU A  1 263 ? 48.148  28.680  176.778 1.00 49.27  ? 263 LEU A CA    1 
ATOM   1810  C C     . LEU A  1 263 ? 48.540  29.517  177.991 1.00 53.33  ? 263 LEU A C     1 
ATOM   1811  O O     . LEU A  1 263 ? 47.857  30.488  178.324 1.00 49.22  ? 263 LEU A O     1 
ATOM   1812  C CB    . LEU A  1 263 ? 47.298  27.487  177.221 1.00 50.04  ? 263 LEU A CB    1 
ATOM   1813  C CG    . LEU A  1 263 ? 46.529  26.779  176.104 1.00 49.88  ? 263 LEU A CG    1 
ATOM   1814  C CD1   . LEU A  1 263 ? 45.601  25.716  176.670 1.00 47.33  ? 263 LEU A CD1   1 
ATOM   1815  C CD2   . LEU A  1 263 ? 45.751  27.794  175.280 1.00 48.23  ? 263 LEU A CD2   1 
ATOM   1816  N N     . HIS A  1 264 ? 49.640  29.153  178.646 1.00 51.16  ? 264 HIS A N     1 
ATOM   1817  C CA    . HIS A  1 264 ? 50.085  29.895  179.822 1.00 50.52  ? 264 HIS A CA    1 
ATOM   1818  C C     . HIS A  1 264 ? 50.497  31.311  179.440 1.00 48.28  ? 264 HIS A C     1 
ATOM   1819  O O     . HIS A  1 264 ? 50.371  32.238  180.238 1.00 44.54  ? 264 HIS A O     1 
ATOM   1820  C CB    . HIS A  1 264 ? 51.246  29.192  180.528 1.00 47.29  ? 264 HIS A CB    1 
ATOM   1821  C CG    . HIS A  1 264 ? 51.674  29.874  181.791 1.00 43.52  ? 264 HIS A CG    1 
ATOM   1822  N ND1   . HIS A  1 264 ? 52.692  30.802  181.828 1.00 45.11  ? 264 HIS A ND1   1 
ATOM   1823  C CD2   . HIS A  1 264 ? 51.202  29.784  183.058 1.00 42.32  ? 264 HIS A CD2   1 
ATOM   1824  C CE1   . HIS A  1 264 ? 52.836  31.246  183.064 1.00 47.94  ? 264 HIS A CE1   1 
ATOM   1825  N NE2   . HIS A  1 264 ? 51.944  30.644  183.830 1.00 47.42  ? 264 HIS A NE2   1 
ATOM   1826  N N     . LYS A  1 265 ? 50.986  31.483  178.217 1.00 46.39  ? 265 LYS A N     1 
ATOM   1827  C CA    . LYS A  1 265 ? 51.343  32.816  177.756 1.00 47.08  ? 265 LYS A CA    1 
ATOM   1828  C C     . LYS A  1 265 ? 50.125  33.532  177.182 1.00 40.29  ? 265 LYS A C     1 
ATOM   1829  O O     . LYS A  1 265 ? 49.963  34.739  177.370 1.00 41.14  ? 265 LYS A O     1 
ATOM   1830  C CB    . LYS A  1 265 ? 52.458  32.765  176.713 1.00 42.40  ? 265 LYS A CB    1 
ATOM   1831  C CG    . LYS A  1 265 ? 52.929  34.150  176.313 1.00 42.45  ? 265 LYS A CG    1 
ATOM   1832  C CD    . LYS A  1 265 ? 53.960  34.127  175.203 1.00 49.05  ? 265 LYS A CD    1 
ATOM   1833  C CE    . LYS A  1 265 ? 54.359  35.551  174.831 1.00 44.41  ? 265 LYS A CE    1 
ATOM   1834  N NZ    . LYS A  1 265 ? 55.514  35.597  173.893 1.00 46.79  ? 265 LYS A NZ    1 
ATOM   1835  N N     . TRP A  1 266 ? 49.277  32.779  176.483 1.00 43.12  ? 266 TRP A N     1 
ATOM   1836  C CA    . TRP A  1 266 ? 48.083  33.336  175.858 1.00 49.30  ? 266 TRP A CA    1 
ATOM   1837  C C     . TRP A  1 266 ? 47.250  34.162  176.832 1.00 40.97  ? 266 TRP A C     1 
ATOM   1838  O O     . TRP A  1 266 ? 46.748  35.230  176.475 1.00 44.76  ? 266 TRP A O     1 
ATOM   1839  C CB    . TRP A  1 266 ? 47.204  32.232  175.264 1.00 47.34  ? 266 TRP A CB    1 
ATOM   1840  C CG    . TRP A  1 266 ? 45.819  32.730  174.973 1.00 46.40  ? 266 TRP A CG    1 
ATOM   1841  C CD1   . TRP A  1 266 ? 45.399  33.368  173.843 1.00 45.24  ? 266 TRP A CD1   1 
ATOM   1842  C CD2   . TRP A  1 266 ? 44.680  32.667  175.843 1.00 42.29  ? 266 TRP A CD2   1 
ATOM   1843  N NE1   . TRP A  1 266 ? 44.070  33.698  173.950 1.00 45.18  ? 266 TRP A NE1   1 
ATOM   1844  C CE2   . TRP A  1 266 ? 43.605  33.279  175.169 1.00 45.83  ? 266 TRP A CE2   1 
ATOM   1845  C CE3   . TRP A  1 266 ? 44.466  32.150  177.124 1.00 43.92  ? 266 TRP A CE3   1 
ATOM   1846  C CZ2   . TRP A  1 266 ? 42.336  33.386  175.731 1.00 39.46  ? 266 TRP A CZ2   1 
ATOM   1847  C CZ3   . TRP A  1 266 ? 43.209  32.263  177.682 1.00 45.84  ? 266 TRP A CZ3   1 
ATOM   1848  C CH2   . TRP A  1 266 ? 42.161  32.879  176.988 1.00 41.24  ? 266 TRP A CH2   1 
ATOM   1849  N N     . GLN A  1 267 ? 47.108  33.662  178.058 1.00 45.90  ? 267 GLN A N     1 
ATOM   1850  C CA    . GLN A  1 267 ? 46.237  34.288  179.050 1.00 43.44  ? 267 GLN A CA    1 
ATOM   1851  C C     . GLN A  1 267 ? 46.664  35.714  179.366 1.00 45.16  ? 267 GLN A C     1 
ATOM   1852  O O     . GLN A  1 267 ? 45.833  36.558  179.698 1.00 44.36  ? 267 GLN A O     1 
ATOM   1853  C CB    . GLN A  1 267 ? 46.198  33.456  180.336 1.00 48.33  ? 267 GLN A CB    1 
ATOM   1854  C CG    . GLN A  1 267 ? 47.430  33.590  181.220 1.00 47.38  ? 267 GLN A CG    1 
ATOM   1855  C CD    . GLN A  1 267 ? 47.390  32.672  182.421 1.00 51.13  ? 267 GLN A CD    1 
ATOM   1856  O OE1   . GLN A  1 267 ? 46.419  32.661  183.178 1.00 50.70  ? 267 GLN A OE1   1 
ATOM   1857  N NE2   . GLN A  1 267 ? 48.445  31.887  182.597 1.00 48.26  ? 267 GLN A NE2   1 
ATOM   1858  N N     . PHE A  1 268 ? 47.962  35.979  179.257 1.00 46.00  ? 268 PHE A N     1 
ATOM   1859  C CA    . PHE A  1 268 ? 48.487  37.305  179.535 1.00 43.19  ? 268 PHE A CA    1 
ATOM   1860  C C     . PHE A  1 268 ? 48.307  38.195  178.316 1.00 39.65  ? 268 PHE A C     1 
ATOM   1861  O O     . PHE A  1 268 ? 47.905  39.345  178.441 1.00 47.98  ? 268 PHE A O     1 
ATOM   1862  C CB    . PHE A  1 268 ? 49.960  37.232  179.947 1.00 50.03  ? 268 PHE A CB    1 
ATOM   1863  C CG    . PHE A  1 268 ? 50.198  36.424  181.191 1.00 47.90  ? 268 PHE A CG    1 
ATOM   1864  C CD1   . PHE A  1 268 ? 49.811  36.905  182.431 1.00 47.16  ? 268 PHE A CD1   1 
ATOM   1865  C CD2   . PHE A  1 268 ? 50.808  35.182  181.121 1.00 47.62  ? 268 PHE A CD2   1 
ATOM   1866  C CE1   . PHE A  1 268 ? 50.026  36.162  183.578 1.00 48.33  ? 268 PHE A CE1   1 
ATOM   1867  C CE2   . PHE A  1 268 ? 51.027  34.436  182.264 1.00 47.34  ? 268 PHE A CE2   1 
ATOM   1868  C CZ    . PHE A  1 268 ? 50.635  34.926  183.493 1.00 44.68  ? 268 PHE A CZ    1 
ATOM   1869  N N     . VAL A  1 269 ? 48.591  37.650  177.137 1.00 39.27  ? 269 VAL A N     1 
ATOM   1870  C CA    . VAL A  1 269 ? 48.400  38.382  175.890 1.00 39.19  ? 269 VAL A CA    1 
ATOM   1871  C C     . VAL A  1 269 ? 46.938  38.786  175.717 1.00 42.44  ? 269 VAL A C     1 
ATOM   1872  O O     . VAL A  1 269 ? 46.633  39.955  175.483 1.00 38.24  ? 269 VAL A O     1 
ATOM   1873  C CB    . VAL A  1 269 ? 48.838  37.552  174.668 1.00 37.86  ? 269 VAL A CB    1 
ATOM   1874  C CG1   . VAL A  1 269 ? 48.576  38.325  173.381 1.00 39.88  ? 269 VAL A CG1   1 
ATOM   1875  C CG2   . VAL A  1 269 ? 50.308  37.161  174.784 1.00 43.64  ? 269 VAL A CG2   1 
ATOM   1876  N N     . ALA A  1 270 ? 46.046  37.809  175.849 1.00 40.71  ? 270 ALA A N     1 
ATOM   1877  C CA    . ALA A  1 270 ? 44.612  38.018  175.666 1.00 38.11  ? 270 ALA A CA    1 
ATOM   1878  C C     . ALA A  1 270 ? 44.063  39.157  176.524 1.00 36.43  ? 270 ALA A C     1 
ATOM   1879  O O     . ALA A  1 270 ? 43.271  39.967  176.049 1.00 40.88  ? 270 ALA A O     1 
ATOM   1880  C CB    . ALA A  1 270 ? 43.856  36.728  175.962 1.00 37.41  ? 270 ALA A CB    1 
ATOM   1881  N N     . GLU A  1 271 ? 44.483  39.218  177.782 1.00 43.24  ? 271 GLU A N     1 
ATOM   1882  C CA    . GLU A  1 271 ? 43.974  40.236  178.695 1.00 47.10  ? 271 GLU A CA    1 
ATOM   1883  C C     . GLU A  1 271 ? 44.689  41.578  178.528 1.00 42.91  ? 271 GLU A C     1 
ATOM   1884  O O     . GLU A  1 271 ? 44.091  42.636  178.720 1.00 43.15  ? 271 GLU A O     1 
ATOM   1885  C CB    . GLU A  1 271 ? 44.098  39.765  180.145 1.00 47.34  ? 271 GLU A CB    1 
ATOM   1886  C CG    . GLU A  1 271 ? 43.498  40.728  181.158 1.00 49.08  ? 271 GLU A CG    1 
ATOM   1887  C CD    . GLU A  1 271 ? 43.939  40.438  182.577 1.00 56.40  ? 271 GLU A CD    1 
ATOM   1888  O OE1   . GLU A  1 271 ? 44.588  39.395  182.800 1.00 56.30  ? 271 GLU A OE1   1 
ATOM   1889  O OE2   . GLU A  1 271 ? 43.640  41.259  183.470 1.00 57.02  ? 271 GLU A OE2   1 
ATOM   1890  N N     . GLU A  1 272 ? 45.966  41.530  178.165 1.00 42.94  ? 272 GLU A N     1 
ATOM   1891  C CA    . GLU A  1 272 ? 46.786  42.739  178.116 1.00 45.06  ? 272 GLU A CA    1 
ATOM   1892  C C     . GLU A  1 272 ? 46.742  43.456  176.772 1.00 38.06  ? 272 GLU A C     1 
ATOM   1893  O O     . GLU A  1 272 ? 47.156  44.613  176.677 1.00 40.52  ? 272 GLU A O     1 
ATOM   1894  C CB    . GLU A  1 272 ? 48.233  42.406  178.468 1.00 44.93  ? 272 GLU A CB    1 
ATOM   1895  C CG    . GLU A  1 272 ? 48.429  42.082  179.932 1.00 49.47  ? 272 GLU A CG    1 
ATOM   1896  C CD    . GLU A  1 272 ? 49.675  41.262  180.186 1.00 61.91  ? 272 GLU A CD    1 
ATOM   1897  O OE1   . GLU A  1 272 ? 50.583  41.269  179.326 1.00 59.36  ? 272 GLU A OE1   1 
ATOM   1898  O OE2   . GLU A  1 272 ? 49.744  40.605  181.246 1.00 61.22  ? 272 GLU A OE2   1 
ATOM   1899  N N     . LEU A  1 273 ? 46.263  42.768  175.738 1.00 37.55  ? 273 LEU A N     1 
ATOM   1900  C CA    . LEU A  1 273 ? 46.108  43.373  174.417 1.00 41.42  ? 273 LEU A CA    1 
ATOM   1901  C C     . LEU A  1 273 ? 45.313  44.673  174.487 1.00 41.00  ? 273 LEU A C     1 
ATOM   1902  O O     . LEU A  1 273 ? 44.399  44.805  175.303 1.00 42.95  ? 273 LEU A O     1 
ATOM   1903  C CB    . LEU A  1 273 ? 45.415  42.399  173.458 1.00 40.87  ? 273 LEU A CB    1 
ATOM   1904  C CG    . LEU A  1 273 ? 46.269  41.360  172.723 1.00 39.62  ? 273 LEU A CG    1 
ATOM   1905  C CD1   . LEU A  1 273 ? 45.397  40.271  172.120 1.00 38.13  ? 273 LEU A CD1   1 
ATOM   1906  C CD2   . LEU A  1 273 ? 47.117  42.028  171.647 1.00 39.58  ? 273 LEU A CD2   1 
ATOM   1907  N N     . GLU A  1 274 ? 45.669  45.634  173.638 1.00 36.99  ? 274 GLU A N     1 
ATOM   1908  C CA    . GLU A  1 274 ? 44.881  46.855  173.503 1.00 43.26  ? 274 GLU A CA    1 
ATOM   1909  C C     . GLU A  1 274 ? 43.452  46.488  173.113 1.00 37.75  ? 274 GLU A C     1 
ATOM   1910  O O     . GLU A  1 274 ? 43.219  45.440  172.509 1.00 35.00  ? 274 GLU A O     1 
ATOM   1911  C CB    . GLU A  1 274 ? 45.500  47.802  172.470 1.00 37.67  ? 274 GLU A CB    1 
ATOM   1912  C CG    . GLU A  1 274 ? 46.814  48.433  172.907 1.00 47.04  ? 274 GLU A CG    1 
ATOM   1913  C CD    . GLU A  1 274 ? 46.655  49.296  174.145 1.00 48.65  ? 274 GLU A CD    1 
ATOM   1914  O OE1   . GLU A  1 274 ? 46.064  50.393  174.035 1.00 45.19  ? 274 GLU A OE1   1 
ATOM   1915  O OE2   . GLU A  1 274 ? 47.127  48.882  175.225 1.00 55.31  ? 274 GLU A OE2   1 
ATOM   1916  N N     . GLU A  1 275 ? 42.498  47.348  173.456 1.00 37.53  ? 275 GLU A N     1 
ATOM   1917  C CA    . GLU A  1 275 ? 41.085  47.009  173.304 1.00 44.47  ? 275 GLU A CA    1 
ATOM   1918  C C     . GLU A  1 275 ? 40.680  46.819  171.841 1.00 42.86  ? 275 GLU A C     1 
ATOM   1919  O O     . GLU A  1 275 ? 39.633  46.239  171.551 1.00 39.41  ? 275 GLU A O     1 
ATOM   1920  C CB    . GLU A  1 275 ? 40.208  48.078  173.967 1.00 39.23  ? 275 GLU A CB    1 
ATOM   1921  C CG    . GLU A  1 275 ? 40.369  49.473  173.396 1.00 41.37  ? 275 GLU A CG    1 
ATOM   1922  C CD    . GLU A  1 275 ? 39.494  50.495  174.101 1.00 53.39  ? 275 GLU A CD    1 
ATOM   1923  O OE1   . GLU A  1 275 ? 39.364  50.424  175.343 1.00 56.20  ? 275 GLU A OE1   1 
ATOM   1924  O OE2   . GLU A  1 275 ? 38.933  51.369  173.405 1.00 52.52  ? 275 GLU A OE2   1 
ATOM   1925  N N     . ASP A  1 276 ? 41.524  47.282  170.922 1.00 39.68  ? 276 ASP A N     1 
ATOM   1926  C CA    . ASP A  1 276 ? 41.288  47.078  169.495 1.00 41.42  ? 276 ASP A CA    1 
ATOM   1927  C C     . ASP A  1 276 ? 41.677  45.671  169.043 1.00 39.58  ? 276 ASP A C     1 
ATOM   1928  O O     . ASP A  1 276 ? 41.647  45.366  167.851 1.00 41.29  ? 276 ASP A O     1 
ATOM   1929  C CB    . ASP A  1 276 ? 42.054  48.113  168.669 1.00 47.29  ? 276 ASP A CB    1 
ATOM   1930  C CG    . ASP A  1 276 ? 41.397  49.475  168.689 1.00 53.06  ? 276 ASP A CG    1 
ATOM   1931  O OD1   . ASP A  1 276 ? 40.261  49.577  169.194 1.00 55.19  ? 276 ASP A OD1   1 
ATOM   1932  O OD2   . ASP A  1 276 ? 42.004  50.443  168.184 1.00 64.25  ? 276 ASP A OD2   1 
ATOM   1933  N N     . PHE A  1 277 ? 42.033  44.817  169.996 1.00 39.28  ? 277 PHE A N     1 
ATOM   1934  C CA    . PHE A  1 277 ? 42.431  43.450  169.685 1.00 40.23  ? 277 PHE A CA    1 
ATOM   1935  C C     . PHE A  1 277 ? 41.632  42.422  170.475 1.00 41.86  ? 277 PHE A C     1 
ATOM   1936  O O     . PHE A  1 277 ? 41.196  42.685  171.595 1.00 43.63  ? 277 PHE A O     1 
ATOM   1937  C CB    . PHE A  1 277 ? 43.925  43.250  169.965 1.00 40.51  ? 277 PHE A CB    1 
ATOM   1938  C CG    . PHE A  1 277 ? 44.832  43.947  168.992 1.00 41.79  ? 277 PHE A CG    1 
ATOM   1939  C CD1   . PHE A  1 277 ? 45.275  43.296  167.853 1.00 39.95  ? 277 PHE A CD1   1 
ATOM   1940  C CD2   . PHE A  1 277 ? 45.254  45.247  169.222 1.00 45.38  ? 277 PHE A CD2   1 
ATOM   1941  C CE1   . PHE A  1 277 ? 46.115  43.929  166.957 1.00 45.62  ? 277 PHE A CE1   1 
ATOM   1942  C CE2   . PHE A  1 277 ? 46.096  45.886  168.328 1.00 41.34  ? 277 PHE A CE2   1 
ATOM   1943  C CZ    . PHE A  1 277 ? 46.528  45.225  167.194 1.00 40.59  ? 277 PHE A CZ    1 
ATOM   1944  N N     . THR A  1 278 ? 41.451  41.248  169.883 1.00 39.92  ? 278 THR A N     1 
ATOM   1945  C CA    . THR A  1 278 ? 40.901  40.105  170.597 1.00 36.80  ? 278 THR A CA    1 
ATOM   1946  C C     . THR A  1 278 ? 41.595  38.835  170.136 1.00 36.48  ? 278 THR A C     1 
ATOM   1947  O O     . THR A  1 278 ? 41.709  38.584  168.937 1.00 38.73  ? 278 THR A O     1 
ATOM   1948  C CB    . THR A  1 278 ? 39.385  39.958  170.386 1.00 37.14  ? 278 THR A CB    1 
ATOM   1949  O OG1   . THR A  1 278 ? 38.722  41.144  170.837 1.00 46.15  ? 278 THR A OG1   1 
ATOM   1950  C CG2   . THR A  1 278 ? 38.853  38.762  171.163 1.00 36.20  ? 278 THR A CG2   1 
ATOM   1951  N N     . LEU A  1 279 ? 42.075  38.043  171.087 1.00 33.67  ? 279 LEU A N     1 
ATOM   1952  C CA    . LEU A  1 279 ? 42.673  36.754  170.769 1.00 33.39  ? 279 LEU A CA    1 
ATOM   1953  C C     . LEU A  1 279 ? 41.990  35.657  171.570 1.00 35.75  ? 279 LEU A C     1 
ATOM   1954  O O     . LEU A  1 279 ? 42.119  35.603  172.791 1.00 37.72  ? 279 LEU A O     1 
ATOM   1955  C CB    . LEU A  1 279 ? 44.175  36.758  171.054 1.00 33.17  ? 279 LEU A CB    1 
ATOM   1956  C CG    . LEU A  1 279 ? 44.906  35.445  170.762 1.00 38.80  ? 279 LEU A CG    1 
ATOM   1957  C CD1   . LEU A  1 279 ? 44.797  35.074  169.290 1.00 37.53  ? 279 LEU A CD1   1 
ATOM   1958  C CD2   . LEU A  1 279 ? 46.363  35.540  171.193 1.00 42.66  ? 279 LEU A CD2   1 
ATOM   1959  N N     . SER A  1 280 ? 41.264  34.786  170.878 1.00 37.42  ? 280 SER A N     1 
ATOM   1960  C CA    . SER A  1 280 ? 40.517  33.723  171.537 1.00 42.00  ? 280 SER A CA    1 
ATOM   1961  C C     . SER A  1 280 ? 41.068  32.355  171.146 1.00 44.59  ? 280 SER A C     1 
ATOM   1962  O O     . SER A  1 280 ? 41.728  32.220  170.118 1.00 45.43  ? 280 SER A O     1 
ATOM   1963  C CB    . SER A  1 280 ? 39.031  33.825  171.189 1.00 36.56  ? 280 SER A CB    1 
ATOM   1964  O OG    . SER A  1 280 ? 38.513  35.086  171.571 1.00 47.95  ? 280 SER A OG    1 
ATOM   1965  N N     . VAL A  1 281 ? 40.802  31.345  171.971 1.00 42.61  ? 281 VAL A N     1 
ATOM   1966  C CA    . VAL A  1 281 ? 41.321  30.003  171.721 1.00 46.85  ? 281 VAL A CA    1 
ATOM   1967  C C     . VAL A  1 281 ? 40.227  28.948  171.769 1.00 39.20  ? 281 VAL A C     1 
ATOM   1968  O O     . VAL A  1 281 ? 39.435  28.908  172.707 1.00 38.69  ? 281 VAL A O     1 
ATOM   1969  C CB    . VAL A  1 281 ? 42.409  29.605  172.747 1.00 42.00  ? 281 VAL A CB    1 
ATOM   1970  C CG1   . VAL A  1 281 ? 43.030  28.269  172.371 1.00 50.77  ? 281 VAL A CG1   1 
ATOM   1971  C CG2   . VAL A  1 281 ? 43.480  30.671  172.836 1.00 47.68  ? 281 VAL A CG2   1 
ATOM   1972  N N     . LEU A  1 282 ? 40.188  28.102  170.745 1.00 44.37  ? 282 LEU A N     1 
ATOM   1973  C CA    . LEU A  1 282 ? 39.384  26.889  170.777 1.00 49.05  ? 282 LEU A CA    1 
ATOM   1974  C C     . LEU A  1 282 ? 40.336  25.712  170.912 1.00 54.42  ? 282 LEU A C     1 
ATOM   1975  O O     . LEU A  1 282 ? 41.245  25.539  170.100 1.00 53.99  ? 282 LEU A O     1 
ATOM   1976  C CB    . LEU A  1 282 ? 38.519  26.754  169.521 1.00 48.41  ? 282 LEU A CB    1 
ATOM   1977  C CG    . LEU A  1 282 ? 37.535  27.900  169.253 1.00 58.57  ? 282 LEU A CG    1 
ATOM   1978  C CD1   . LEU A  1 282 ? 36.757  27.657  167.967 1.00 64.68  ? 282 LEU A CD1   1 
ATOM   1979  C CD2   . LEU A  1 282 ? 36.592  28.120  170.432 1.00 61.80  ? 282 LEU A CD2   1 
ATOM   1980  N N     . GLY A  1 283 ? 40.139  24.913  171.953 1.00 51.94  ? 283 GLY A N     1 
ATOM   1981  C CA    . GLY A  1 283 ? 41.032  23.805  172.222 1.00 50.79  ? 283 GLY A CA    1 
ATOM   1982  C C     . GLY A  1 283 ? 40.328  22.467  172.199 1.00 58.88  ? 283 GLY A C     1 
ATOM   1983  O O     . GLY A  1 283 ? 39.204  22.330  172.676 1.00 53.31  ? 283 GLY A O     1 
ATOM   1984  N N     . GLY A  1 284 ? 40.994  21.473  171.629 1.00 58.30  ? 284 GLY A N     1 
ATOM   1985  C CA    . GLY A  1 284 ? 40.473  20.123  171.619 1.00 59.62  ? 284 GLY A CA    1 
ATOM   1986  C C     . GLY A  1 284 ? 41.624  19.146  171.586 1.00 66.71  ? 284 GLY A C     1 
ATOM   1987  O O     . GLY A  1 284 ? 42.753  19.513  171.261 1.00 59.19  ? 284 GLY A O     1 
ATOM   1988  N N     . ALA A  1 285 ? 41.347  17.900  171.940 1.00 69.65  ? 285 ALA A N     1 
ATOM   1989  C CA    . ALA A  1 285 ? 42.330  16.849  171.758 1.00 75.95  ? 285 ALA A CA    1 
ATOM   1990  C C     . ALA A  1 285 ? 41.665  15.664  171.075 1.00 86.93  ? 285 ALA A C     1 
ATOM   1991  O O     . ALA A  1 285 ? 41.307  14.673  171.719 1.00 80.87  ? 285 ALA A O     1 
ATOM   1992  C CB    . ALA A  1 285 ? 42.942  16.447  173.077 1.00 70.81  ? 285 ALA A CB    1 
ATOM   1993  N N     . ASP A  1 286 ? 41.499  15.793  169.759 1.00 94.91  ? 286 ASP A N     1 
ATOM   1994  C CA    . ASP A  1 286 ? 40.874  14.774  168.919 1.00 104.53 ? 286 ASP A CA    1 
ATOM   1995  C C     . ASP A  1 286 ? 41.630  13.452  168.980 1.00 111.41 ? 286 ASP A C     1 
ATOM   1996  O O     . ASP A  1 286 ? 41.107  12.405  168.598 1.00 108.54 ? 286 ASP A O     1 
ATOM   1997  C CB    . ASP A  1 286 ? 40.798  15.254  167.465 1.00 107.37 ? 286 ASP A CB    1 
ATOM   1998  C CG    . ASP A  1 286 ? 39.834  16.410  167.281 1.00 115.68 ? 286 ASP A CG    1 
ATOM   1999  O OD1   . ASP A  1 286 ? 39.042  16.674  168.212 1.00 121.98 ? 286 ASP A OD1   1 
ATOM   2000  O OD2   . ASP A  1 286 ? 39.861  17.044  166.205 1.00 114.02 ? 286 ASP A OD2   1 
ATOM   2001  N N     . GLU A  1 287 ? 42.874  13.521  169.445 1.00 102.57 ? 287 GLU A N     1 
ATOM   2002  C CA    . GLU A  1 287 ? 43.693  12.342  169.694 1.00 99.12  ? 287 GLU A CA    1 
ATOM   2003  C C     . GLU A  1 287 ? 44.185  12.364  171.144 1.00 92.19  ? 287 GLU A C     1 
ATOM   2004  O O     . GLU A  1 287 ? 43.382  12.393  172.081 1.00 93.59  ? 287 GLU A O     1 
ATOM   2005  C CB    . GLU A  1 287 ? 44.875  12.289  168.717 1.00 99.86  ? 287 GLU A CB    1 
ATOM   2006  C CG    . GLU A  1 287 ? 44.508  12.335  167.222 1.00 107.36 ? 287 GLU A CG    1 
ATOM   2007  C CD    . GLU A  1 287 ? 44.012  10.998  166.684 1.00 116.78 ? 287 GLU A CD    1 
ATOM   2008  O OE1   . GLU A  1 287 ? 44.076  10.782  165.456 1.00 123.37 ? 287 GLU A OE1   1 
ATOM   2009  O OE2   . GLU A  1 287 ? 43.553  10.164  167.489 1.00 125.20 ? 287 GLU A OE2   1 
ATOM   2010  N N     . LYS A  1 288 ? 45.503  12.342  171.318 1.00 88.51  ? 288 LYS A N     1 
ATOM   2011  C CA    . LYS A  1 288 ? 46.126  12.522  172.623 1.00 88.79  ? 288 LYS A CA    1 
ATOM   2012  C C     . LYS A  1 288 ? 47.306  13.472  172.452 1.00 89.03  ? 288 LYS A C     1 
ATOM   2013  O O     . LYS A  1 288 ? 48.140  13.651  173.342 1.00 101.95 ? 288 LYS A O     1 
ATOM   2014  C CB    . LYS A  1 288 ? 46.536  11.176  173.227 1.00 93.19  ? 288 LYS A CB    1 
ATOM   2015  C CG    . LYS A  1 288 ? 45.317  10.409  173.711 1.00 92.09  ? 288 LYS A CG    1 
ATOM   2016  C CD    . LYS A  1 288 ? 45.636  9.137   174.472 1.00 95.02  ? 288 LYS A CD    1 
ATOM   2017  C CE    . LYS A  1 288 ? 44.327  8.477   174.900 1.00 88.76  ? 288 LYS A CE    1 
ATOM   2018  N NZ    . LYS A  1 288 ? 44.449  7.039   175.266 1.00 84.61  ? 288 LYS A NZ    1 
ATOM   2019  N N     . GLN A  1 289 ? 47.357  14.064  171.264 1.00 85.84  ? 289 GLN A N     1 
ATOM   2020  C CA    . GLN A  1 289 ? 48.009  15.346  171.059 1.00 86.95  ? 289 GLN A CA    1 
ATOM   2021  C C     . GLN A  1 289 ? 46.864  16.348  171.049 1.00 79.30  ? 289 GLN A C     1 
ATOM   2022  O O     . GLN A  1 289 ? 45.719  15.966  170.794 1.00 81.28  ? 289 GLN A O     1 
ATOM   2023  C CB    . GLN A  1 289 ? 48.813  15.386  169.757 1.00 90.47  ? 289 GLN A CB    1 
ATOM   2024  C CG    . GLN A  1 289 ? 47.982  15.160  168.485 1.00 94.62  ? 289 GLN A CG    1 
ATOM   2025  C CD    . GLN A  1 289 ? 47.889  16.402  167.606 1.00 99.18  ? 289 GLN A CD    1 
ATOM   2026  O OE1   . GLN A  1 289 ? 48.652  17.355  167.772 1.00 103.08 ? 289 GLN A OE1   1 
ATOM   2027  N NE2   . GLN A  1 289 ? 46.950  16.392  166.664 1.00 104.66 ? 289 GLN A NE2   1 
ATOM   2028  N N     . VAL A  1 290 ? 47.141  17.612  171.342 1.00 74.27  ? 290 VAL A N     1 
ATOM   2029  C CA    . VAL A  1 290 ? 46.069  18.597  171.323 1.00 67.26  ? 290 VAL A CA    1 
ATOM   2030  C C     . VAL A  1 290 ? 46.194  19.522  170.127 1.00 64.75  ? 290 VAL A C     1 
ATOM   2031  O O     . VAL A  1 290 ? 47.273  19.684  169.557 1.00 65.31  ? 290 VAL A O     1 
ATOM   2032  C CB    . VAL A  1 290 ? 46.047  19.447  172.597 1.00 63.57  ? 290 VAL A CB    1 
ATOM   2033  C CG1   . VAL A  1 290 ? 46.068  18.567  173.828 1.00 66.31  ? 290 VAL A CG1   1 
ATOM   2034  C CG2   . VAL A  1 290 ? 47.213  20.389  172.605 1.00 64.84  ? 290 VAL A CG2   1 
ATOM   2035  N N     . TRP A  1 291 ? 45.073  20.115  169.741 1.00 62.08  ? 291 TRP A N     1 
ATOM   2036  C CA    . TRP A  1 291 ? 45.084  21.164  168.739 1.00 56.90  ? 291 TRP A CA    1 
ATOM   2037  C C     . TRP A  1 291 ? 44.597  22.459  169.367 1.00 56.82  ? 291 TRP A C     1 
ATOM   2038  O O     . TRP A  1 291 ? 43.681  22.456  170.185 1.00 56.66  ? 291 TRP A O     1 
ATOM   2039  C CB    . TRP A  1 291 ? 44.219  20.787  167.535 1.00 49.66  ? 291 TRP A CB    1 
ATOM   2040  C CG    . TRP A  1 291 ? 42.792  20.478  167.874 1.00 65.40  ? 291 TRP A CG    1 
ATOM   2041  C CD1   . TRP A  1 291 ? 42.280  19.266  168.233 1.00 65.82  ? 291 TRP A CD1   1 
ATOM   2042  C CD2   . TRP A  1 291 ? 41.692  21.396  167.877 1.00 61.38  ? 291 TRP A CD2   1 
ATOM   2043  N NE1   . TRP A  1 291 ? 40.929  19.373  168.462 1.00 70.37  ? 291 TRP A NE1   1 
ATOM   2044  C CE2   . TRP A  1 291 ? 40.544  20.670  168.249 1.00 64.88  ? 291 TRP A CE2   1 
ATOM   2045  C CE3   . TRP A  1 291 ? 41.566  22.762  167.602 1.00 57.61  ? 291 TRP A CE3   1 
ATOM   2046  C CZ2   . TRP A  1 291 ? 39.288  21.263  168.355 1.00 65.35  ? 291 TRP A CZ2   1 
ATOM   2047  C CZ3   . TRP A  1 291 ? 40.318  23.348  167.706 1.00 53.95  ? 291 TRP A CZ3   1 
ATOM   2048  C CH2   . TRP A  1 291 ? 39.196  22.599  168.080 1.00 57.42  ? 291 TRP A CH2   1 
ATOM   2049  N N     . LEU A  1 292 ? 45.228  23.564  168.996 1.00 53.32  ? 292 LEU A N     1 
ATOM   2050  C CA    . LEU A  1 292 ? 44.797  24.871  169.467 1.00 50.42  ? 292 LEU A CA    1 
ATOM   2051  C C     . LEU A  1 292 ? 44.538  25.790  168.287 1.00 55.30  ? 292 LEU A C     1 
ATOM   2052  O O     . LEU A  1 292 ? 45.444  26.083  167.508 1.00 56.50  ? 292 LEU A O     1 
ATOM   2053  C CB    . LEU A  1 292 ? 45.841  25.493  170.396 1.00 52.23  ? 292 LEU A CB    1 
ATOM   2054  C CG    . LEU A  1 292 ? 46.229  24.707  171.649 1.00 49.83  ? 292 LEU A CG    1 
ATOM   2055  C CD1   . LEU A  1 292 ? 47.316  25.449  172.423 1.00 41.22  ? 292 LEU A CD1   1 
ATOM   2056  C CD2   . LEU A  1 292 ? 45.016  24.447  172.526 1.00 47.45  ? 292 LEU A CD2   1 
ATOM   2057  N N     . THR A  1 293 ? 43.298  26.238  168.146 1.00 49.36  ? 293 THR A N     1 
ATOM   2058  C CA    . THR A  1 293 ? 42.974  27.199  167.104 1.00 52.56  ? 293 THR A CA    1 
ATOM   2059  C C     . THR A  1 293 ? 42.916  28.600  167.695 1.00 52.74  ? 293 THR A C     1 
ATOM   2060  O O     . THR A  1 293 ? 42.061  28.900  168.527 1.00 51.47  ? 293 THR A O     1 
ATOM   2061  C CB    . THR A  1 293 ? 41.642  26.868  166.411 1.00 53.58  ? 293 THR A CB    1 
ATOM   2062  O OG1   . THR A  1 293 ? 41.700  25.541  165.873 1.00 53.50  ? 293 THR A OG1   1 
ATOM   2063  C CG2   . THR A  1 293 ? 41.383  27.844  165.281 1.00 53.73  ? 293 THR A CG2   1 
ATOM   2064  N N     . MET A  1 294 ? 43.845  29.449  167.270 1.00 54.84  ? 294 MET A N     1 
ATOM   2065  C CA    . MET A  1 294 ? 43.900  30.822  167.750 1.00 49.44  ? 294 MET A CA    1 
ATOM   2066  C C     . MET A  1 294 ? 43.084  31.729  166.841 1.00 48.07  ? 294 MET A C     1 
ATOM   2067  O O     . MET A  1 294 ? 43.333  31.801  165.637 1.00 51.12  ? 294 MET A O     1 
ATOM   2068  C CB    . MET A  1 294 ? 45.346  31.307  167.822 1.00 49.51  ? 294 MET A CB    1 
ATOM   2069  C CG    . MET A  1 294 ? 46.284  30.332  168.504 1.00 51.10  ? 294 MET A CG    1 
ATOM   2070  S SD    . MET A  1 294 ? 45.985  30.207  170.275 1.00 62.51  ? 294 MET A SD    1 
ATOM   2071  C CE    . MET A  1 294 ? 46.196  31.917  170.752 1.00 44.49  ? 294 MET A CE    1 
ATOM   2072  N N     . LEU A  1 295 ? 42.108  32.419  167.419 1.00 47.47  ? 295 LEU A N     1 
ATOM   2073  C CA    . LEU A  1 295 ? 41.257  33.313  166.648 1.00 44.01  ? 295 LEU A CA    1 
ATOM   2074  C C     . LEU A  1 295 ? 41.525  34.759  167.030 1.00 41.44  ? 295 LEU A C     1 
ATOM   2075  O O     . LEU A  1 295 ? 41.419  35.132  168.199 1.00 38.65  ? 295 LEU A O     1 
ATOM   2076  C CB    . LEU A  1 295 ? 39.788  32.958  166.861 1.00 44.53  ? 295 LEU A CB    1 
ATOM   2077  C CG    . LEU A  1 295 ? 39.500  31.492  166.539 1.00 50.27  ? 295 LEU A CG    1 
ATOM   2078  C CD1   . LEU A  1 295 ? 38.462  30.914  167.489 1.00 51.39  ? 295 LEU A CD1   1 
ATOM   2079  C CD2   . LEU A  1 295 ? 39.064  31.329  165.091 1.00 58.74  ? 295 LEU A CD2   1 
ATOM   2080  N N     . GLY A  1 296 ? 41.876  35.567  166.035 1.00 37.24  ? 296 GLY A N     1 
ATOM   2081  C CA    . GLY A  1 296 ? 42.246  36.950  166.266 1.00 42.87  ? 296 GLY A CA    1 
ATOM   2082  C C     . GLY A  1 296 ? 41.378  37.938  165.514 1.00 37.64  ? 296 GLY A C     1 
ATOM   2083  O O     . GLY A  1 296 ? 40.896  37.655  164.416 1.00 36.05  ? 296 GLY A O     1 
ATOM   2084  N N     . PHE A  1 297 ? 41.184  39.107  166.115 1.00 38.47  ? 297 PHE A N     1 
ATOM   2085  C CA    . PHE A  1 297 ? 40.415  40.183  165.501 1.00 41.69  ? 297 PHE A CA    1 
ATOM   2086  C C     . PHE A  1 297 ? 41.065  41.520  165.831 1.00 39.40  ? 297 PHE A C     1 
ATOM   2087  O O     . PHE A  1 297 ? 41.483  41.750  166.966 1.00 41.37  ? 297 PHE A O     1 
ATOM   2088  C CB    . PHE A  1 297 ? 38.960  40.160  165.985 1.00 39.44  ? 297 PHE A CB    1 
ATOM   2089  C CG    . PHE A  1 297 ? 38.098  41.250  165.395 1.00 42.07  ? 297 PHE A CG    1 
ATOM   2090  C CD1   . PHE A  1 297 ? 37.346  41.018  164.254 1.00 45.36  ? 297 PHE A CD1   1 
ATOM   2091  C CD2   . PHE A  1 297 ? 38.031  42.503  165.990 1.00 38.05  ? 297 PHE A CD2   1 
ATOM   2092  C CE1   . PHE A  1 297 ? 36.555  42.016  163.713 1.00 43.51  ? 297 PHE A CE1   1 
ATOM   2093  C CE2   . PHE A  1 297 ? 37.243  43.502  165.451 1.00 44.47  ? 297 PHE A CE2   1 
ATOM   2094  C CZ    . PHE A  1 297 ? 36.503  43.258  164.313 1.00 45.95  ? 297 PHE A CZ    1 
ATOM   2095  N N     . HIS A  1 298 ? 41.148  42.399  164.839 1.00 39.35  ? 298 HIS A N     1 
ATOM   2096  C CA    . HIS A  1 298 ? 41.706  43.729  165.046 1.00 43.35  ? 298 HIS A CA    1 
ATOM   2097  C C     . HIS A  1 298 ? 40.886  44.808  164.342 1.00 40.99  ? 298 HIS A C     1 
ATOM   2098  O O     . HIS A  1 298 ? 40.609  44.710  163.144 1.00 43.79  ? 298 HIS A O     1 
ATOM   2099  C CB    . HIS A  1 298 ? 43.157  43.787  164.563 1.00 44.19  ? 298 HIS A CB    1 
ATOM   2100  C CG    . HIS A  1 298 ? 43.743  45.164  164.590 1.00 40.59  ? 298 HIS A CG    1 
ATOM   2101  N ND1   . HIS A  1 298 ? 43.767  45.937  165.730 1.00 42.16  ? 298 HIS A ND1   1 
ATOM   2102  C CD2   . HIS A  1 298 ? 44.312  45.912  163.616 1.00 45.03  ? 298 HIS A CD2   1 
ATOM   2103  C CE1   . HIS A  1 298 ? 44.331  47.101  165.459 1.00 44.91  ? 298 HIS A CE1   1 
ATOM   2104  N NE2   . HIS A  1 298 ? 44.672  47.111  164.183 1.00 42.92  ? 298 HIS A NE2   1 
ATOM   2105  N N     . PHE A  1 299 ? 40.496  45.832  165.094 1.00 40.44  ? 299 PHE A N     1 
ATOM   2106  C CA    . PHE A  1 299 ? 39.832  46.999  164.523 1.00 45.16  ? 299 PHE A CA    1 
ATOM   2107  C C     . PHE A  1 299 ? 40.821  47.841  163.729 1.00 46.04  ? 299 PHE A C     1 
ATOM   2108  O O     . PHE A  1 299 ? 41.205  48.925  164.165 1.00 50.61  ? 299 PHE A O     1 
ATOM   2109  C CB    . PHE A  1 299 ? 39.199  47.864  165.617 1.00 44.57  ? 299 PHE A CB    1 
ATOM   2110  C CG    . PHE A  1 299 ? 38.062  47.205  166.338 1.00 49.07  ? 299 PHE A CG    1 
ATOM   2111  C CD1   . PHE A  1 299 ? 36.752  47.518  166.016 1.00 47.85  ? 299 PHE A CD1   1 
ATOM   2112  C CD2   . PHE A  1 299 ? 38.299  46.285  167.347 1.00 50.93  ? 299 PHE A CD2   1 
ATOM   2113  C CE1   . PHE A  1 299 ? 35.700  46.919  166.680 1.00 51.89  ? 299 PHE A CE1   1 
ATOM   2114  C CE2   . PHE A  1 299 ? 37.248  45.683  168.015 1.00 54.85  ? 299 PHE A CE2   1 
ATOM   2115  C CZ    . PHE A  1 299 ? 35.949  46.001  167.682 1.00 50.76  ? 299 PHE A CZ    1 
ATOM   2116  N N     . GLY A  1 300 ? 41.236  47.345  162.570 1.00 44.80  ? 300 GLY A N     1 
ATOM   2117  C CA    . GLY A  1 300 ? 42.217  48.049  161.771 1.00 46.83  ? 300 GLY A CA    1 
ATOM   2118  C C     . GLY A  1 300 ? 42.852  47.162  160.727 1.00 50.28  ? 300 GLY A C     1 
ATOM   2119  O O     . GLY A  1 300 ? 42.416  46.031  160.499 1.00 43.35  ? 300 GLY A O     1 
ATOM   2120  N N     . LEU A  1 301 ? 43.899  47.672  160.092 1.00 49.96  ? 301 LEU A N     1 
ATOM   2121  C CA    . LEU A  1 301 ? 44.524  46.958  158.986 1.00 48.56  ? 301 LEU A CA    1 
ATOM   2122  C C     . LEU A  1 301 ? 45.629  46.022  159.470 1.00 45.29  ? 301 LEU A C     1 
ATOM   2123  O O     . LEU A  1 301 ? 46.034  46.075  160.637 1.00 48.77  ? 301 LEU A O     1 
ATOM   2124  C CB    . LEU A  1 301 ? 45.062  47.959  157.959 1.00 51.38  ? 301 LEU A CB    1 
ATOM   2125  C CG    . LEU A  1 301 ? 43.967  48.832  157.335 1.00 57.81  ? 301 LEU A CG    1 
ATOM   2126  C CD1   . LEU A  1 301 ? 44.523  50.123  156.730 1.00 57.97  ? 301 LEU A CD1   1 
ATOM   2127  C CD2   . LEU A  1 301 ? 43.159  48.033  156.298 1.00 60.70  ? 301 LEU A CD2   1 
ATOM   2128  N N     . LYS A  1 302 ? 46.110  45.166  158.569 1.00 45.00  ? 302 LYS A N     1 
ATOM   2129  C CA    . LYS A  1 302 ? 46.966  44.035  158.929 1.00 48.52  ? 302 LYS A CA    1 
ATOM   2130  C C     . LYS A  1 302 ? 48.332  44.420  159.499 1.00 48.21  ? 302 LYS A C     1 
ATOM   2131  O O     . LYS A  1 302 ? 48.893  43.686  160.316 1.00 48.91  ? 302 LYS A O     1 
ATOM   2132  C CB    . LYS A  1 302 ? 47.164  43.140  157.702 1.00 49.31  ? 302 LYS A CB    1 
ATOM   2133  C CG    . LYS A  1 302 ? 47.849  43.817  156.522 1.00 58.25  ? 302 LYS A CG    1 
ATOM   2134  C CD    . LYS A  1 302 ? 47.577  43.066  155.232 1.00 58.65  ? 302 LYS A CD    1 
ATOM   2135  C CE    . LYS A  1 302 ? 47.942  41.601  155.391 1.00 64.45  ? 302 LYS A CE    1 
ATOM   2136  N NZ    . LYS A  1 302 ? 47.686  40.776  154.179 1.00 69.34  ? 302 LYS A NZ    1 
ATOM   2137  N N     . THR A  1 303 ? 48.864  45.560  159.061 1.00 45.66  ? 303 THR A N     1 
ATOM   2138  C CA    . THR A  1 303 ? 50.200  46.002  159.465 1.00 54.68  ? 303 THR A CA    1 
ATOM   2139  C C     . THR A  1 303 ? 50.286  46.266  160.966 1.00 50.38  ? 303 THR A C     1 
ATOM   2140  O O     . THR A  1 303 ? 51.252  45.863  161.615 1.00 48.38  ? 303 THR A O     1 
ATOM   2141  C CB    . THR A  1 303 ? 50.641  47.278  158.697 1.00 55.98  ? 303 THR A CB    1 
ATOM   2142  O OG1   . THR A  1 303 ? 49.766  48.367  159.013 1.00 59.48  ? 303 THR A OG1   1 
ATOM   2143  C CG2   . THR A  1 303 ? 50.632  47.042  157.198 1.00 52.74  ? 303 THR A CG2   1 
ATOM   2144  N N     . VAL A  1 304 ? 49.283  46.944  161.518 1.00 47.80  ? 304 VAL A N     1 
ATOM   2145  C CA    . VAL A  1 304 ? 49.235  47.188  162.963 1.00 48.16  ? 304 VAL A CA    1 
ATOM   2146  C C     . VAL A  1 304 ? 48.954  45.875  163.705 1.00 50.51  ? 304 VAL A C     1 
ATOM   2147  O O     . VAL A  1 304 ? 49.495  45.627  164.787 1.00 48.81  ? 304 VAL A O     1 
ATOM   2148  C CB    . VAL A  1 304 ? 48.165  48.252  163.338 1.00 50.27  ? 304 VAL A CB    1 
ATOM   2149  C CG1   . VAL A  1 304 ? 48.042  48.397  164.852 1.00 49.06  ? 304 VAL A CG1   1 
ATOM   2150  C CG2   . VAL A  1 304 ? 48.511  49.598  162.712 1.00 57.91  ? 304 VAL A CG2   1 
ATOM   2151  N N     . ALA A  1 305 ? 48.132  45.020  163.100 1.00 45.90  ? 305 ALA A N     1 
ATOM   2152  C CA    . ALA A  1 305 ? 47.811  43.713  163.671 1.00 49.72  ? 305 ALA A CA    1 
ATOM   2153  C C     . ALA A  1 305 ? 49.037  42.795  163.745 1.00 44.38  ? 305 ALA A C     1 
ATOM   2154  O O     . ALA A  1 305 ? 49.288  42.175  164.779 1.00 43.79  ? 305 ALA A O     1 
ATOM   2155  C CB    . ALA A  1 305 ? 46.703  43.046  162.861 1.00 40.11  ? 305 ALA A CB    1 
ATOM   2156  N N     . LYS A  1 306 ? 49.780  42.692  162.646 1.00 44.15  ? 306 LYS A N     1 
ATOM   2157  C CA    . LYS A  1 306 ? 50.965  41.834  162.589 1.00 49.13  ? 306 LYS A CA    1 
ATOM   2158  C C     . LYS A  1 306 ? 52.102  42.342  163.481 1.00 45.17  ? 306 LYS A C     1 
ATOM   2159  O O     . LYS A  1 306 ? 52.732  41.559  164.201 1.00 40.59  ? 306 LYS A O     1 
ATOM   2160  C CB    . LYS A  1 306 ? 51.460  41.703  161.142 1.00 49.19  ? 306 LYS A CB    1 
ATOM   2161  C CG    . LYS A  1 306 ? 52.738  40.880  161.010 1.00 51.84  ? 306 LYS A CG    1 
ATOM   2162  C CD    . LYS A  1 306 ? 53.029  40.489  159.570 1.00 54.05  ? 306 LYS A CD    1 
ATOM   2163  C CE    . LYS A  1 306 ? 54.234  39.561  159.496 1.00 53.93  ? 306 LYS A CE    1 
ATOM   2164  N NZ    . LYS A  1 306 ? 55.475  40.199  160.027 1.00 55.40  ? 306 LYS A NZ    1 
ATOM   2165  N N     . SER A  1 307 ? 52.359  43.648  163.418 1.00 42.07  ? 307 SER A N     1 
ATOM   2166  C CA    . SER A  1 307 ? 53.356  44.299  164.267 1.00 45.45  ? 307 SER A CA    1 
ATOM   2167  C C     . SER A  1 307 ? 53.129  43.996  165.740 1.00 46.91  ? 307 SER A C     1 
ATOM   2168  O O     . SER A  1 307 ? 54.076  43.793  166.501 1.00 41.72  ? 307 SER A O     1 
ATOM   2169  C CB    . SER A  1 307 ? 53.328  45.811  164.048 1.00 46.25  ? 307 SER A CB    1 
ATOM   2170  O OG    . SER A  1 307 ? 53.990  46.492  165.096 1.00 56.61  ? 307 SER A OG    1 
ATOM   2171  N N     . THR A  1 308 ? 51.860  43.962  166.128 1.00 41.94  ? 308 THR A N     1 
ATOM   2172  C CA    . THR A  1 308 ? 51.482  43.716  167.508 1.00 38.73  ? 308 THR A CA    1 
ATOM   2173  C C     . THR A  1 308 ? 51.768  42.277  167.929 1.00 39.95  ? 308 THR A C     1 
ATOM   2174  O O     . THR A  1 308 ? 52.298  42.039  169.014 1.00 40.19  ? 308 THR A O     1 
ATOM   2175  C CB    . THR A  1 308 ? 49.991  44.026  167.737 1.00 40.39  ? 308 THR A CB    1 
ATOM   2176  O OG1   . THR A  1 308 ? 49.738  45.401  167.429 1.00 38.05  ? 308 THR A OG1   1 
ATOM   2177  C CG2   . THR A  1 308 ? 49.609  43.762  169.182 1.00 31.89  ? 308 THR A CG2   1 
ATOM   2178  N N     . PHE A  1 309 ? 51.432  41.317  167.071 1.00 38.56  ? 309 PHE A N     1 
ATOM   2179  C CA    . PHE A  1 309 ? 51.577  39.910  167.436 1.00 41.06  ? 309 PHE A CA    1 
ATOM   2180  C C     . PHE A  1 309 ? 52.983  39.366  167.177 1.00 42.37  ? 309 PHE A C     1 
ATOM   2181  O O     . PHE A  1 309 ? 53.396  38.401  167.813 1.00 41.97  ? 309 PHE A O     1 
ATOM   2182  C CB    . PHE A  1 309 ? 50.538  39.058  166.707 1.00 40.68  ? 309 PHE A CB    1 
ATOM   2183  C CG    . PHE A  1 309 ? 49.158  39.161  167.296 1.00 48.65  ? 309 PHE A CG    1 
ATOM   2184  C CD1   . PHE A  1 309 ? 48.831  38.470  168.453 1.00 45.12  ? 309 PHE A CD1   1 
ATOM   2185  C CD2   . PHE A  1 309 ? 48.192  39.951  166.698 1.00 47.19  ? 309 PHE A CD2   1 
ATOM   2186  C CE1   . PHE A  1 309 ? 47.564  38.565  169.000 1.00 45.29  ? 309 PHE A CE1   1 
ATOM   2187  C CE2   . PHE A  1 309 ? 46.924  40.050  167.238 1.00 44.46  ? 309 PHE A CE2   1 
ATOM   2188  C CZ    . PHE A  1 309 ? 46.610  39.357  168.390 1.00 44.32  ? 309 PHE A CZ    1 
ATOM   2189  N N     . ASP A  1 310 ? 53.707  39.975  166.244 1.00 41.69  ? 310 ASP A N     1 
ATOM   2190  C CA    . ASP A  1 310 ? 55.139  39.718  166.121 1.00 42.85  ? 310 ASP A CA    1 
ATOM   2191  C C     . ASP A  1 310 ? 55.802  39.988  167.468 1.00 38.24  ? 310 ASP A C     1 
ATOM   2192  O O     . ASP A  1 310 ? 56.591  39.189  167.972 1.00 40.98  ? 310 ASP A O     1 
ATOM   2193  C CB    . ASP A  1 310 ? 55.774  40.602  165.046 1.00 35.93  ? 310 ASP A CB    1 
ATOM   2194  C CG    . ASP A  1 310 ? 55.512  40.106  163.638 1.00 42.39  ? 310 ASP A CG    1 
ATOM   2195  O OD1   . ASP A  1 310 ? 55.057  38.956  163.475 1.00 38.43  ? 310 ASP A OD1   1 
ATOM   2196  O OD2   . ASP A  1 310 ? 55.784  40.871  162.687 1.00 46.69  ? 310 ASP A OD2   1 
ATOM   2197  N N     . LEU A  1 311 ? 55.441  41.127  168.043 1.00 43.27  ? 311 LEU A N     1 
ATOM   2198  C CA    . LEU A  1 311 ? 55.978  41.591  169.313 1.00 40.22  ? 311 LEU A CA    1 
ATOM   2199  C C     . LEU A  1 311 ? 55.482  40.764  170.497 1.00 42.26  ? 311 LEU A C     1 
ATOM   2200  O O     . LEU A  1 311 ? 56.272  40.181  171.244 1.00 40.22  ? 311 LEU A O     1 
ATOM   2201  C CB    . LEU A  1 311 ? 55.600  43.060  169.502 1.00 40.75  ? 311 LEU A CB    1 
ATOM   2202  C CG    . LEU A  1 311 ? 56.618  44.037  170.076 1.00 46.16  ? 311 LEU A CG    1 
ATOM   2203  C CD1   . LEU A  1 311 ? 58.031  43.593  169.737 1.00 41.40  ? 311 LEU A CD1   1 
ATOM   2204  C CD2   . LEU A  1 311 ? 56.344  45.434  169.525 1.00 42.17  ? 311 LEU A CD2   1 
ATOM   2205  N N     . LEU A  1 312 ? 54.163  40.718  170.656 1.00 42.97  ? 312 LEU A N     1 
ATOM   2206  C CA    . LEU A  1 312 ? 53.537  40.105  171.826 1.00 42.34  ? 312 LEU A CA    1 
ATOM   2207  C C     . LEU A  1 312 ? 53.456  38.583  171.792 1.00 39.11  ? 312 LEU A C     1 
ATOM   2208  O O     . LEU A  1 312 ? 53.546  37.936  172.836 1.00 37.64  ? 312 LEU A O     1 
ATOM   2209  C CB    . LEU A  1 312 ? 52.126  40.678  172.012 1.00 44.75  ? 312 LEU A CB    1 
ATOM   2210  C CG    . LEU A  1 312 ? 52.064  42.158  172.412 1.00 44.87  ? 312 LEU A CG    1 
ATOM   2211  C CD1   . LEU A  1 312 ? 50.623  42.604  172.615 1.00 40.73  ? 312 LEU A CD1   1 
ATOM   2212  C CD2   . LEU A  1 312 ? 52.887  42.394  173.663 1.00 42.93  ? 312 LEU A CD2   1 
ATOM   2213  N N     . PHE A  1 313 ? 53.271  38.004  170.608 1.00 34.91  ? 313 PHE A N     1 
ATOM   2214  C CA    . PHE A  1 313 ? 53.123  36.539  170.501 1.00 38.31  ? 313 PHE A CA    1 
ATOM   2215  C C     . PHE A  1 313 ? 53.812  35.958  169.261 1.00 46.39  ? 313 PHE A C     1 
ATOM   2216  O O     . PHE A  1 313 ? 53.143  35.436  168.371 1.00 39.98  ? 313 PHE A O     1 
ATOM   2217  C CB    . PHE A  1 313 ? 51.643  36.174  170.479 1.00 45.83  ? 313 PHE A CB    1 
ATOM   2218  C CG    . PHE A  1 313 ? 51.295  34.959  171.288 1.00 46.24  ? 313 PHE A CG    1 
ATOM   2219  C CD1   . PHE A  1 313 ? 52.245  33.986  171.560 1.00 42.16  ? 313 PHE A CD1   1 
ATOM   2220  C CD2   . PHE A  1 313 ? 50.008  34.793  171.781 1.00 42.90  ? 313 PHE A CD2   1 
ATOM   2221  C CE1   . PHE A  1 313 ? 51.920  32.863  172.312 1.00 37.55  ? 313 PHE A CE1   1 
ATOM   2222  C CE2   . PHE A  1 313 ? 49.672  33.682  172.527 1.00 41.91  ? 313 PHE A CE2   1 
ATOM   2223  C CZ    . PHE A  1 313 ? 50.628  32.716  172.795 1.00 48.91  ? 313 PHE A CZ    1 
ATOM   2224  N N     . PRO A  1 314 ? 55.153  36.042  169.202 1.00 47.23  ? 314 PRO A N     1 
ATOM   2225  C CA    . PRO A  1 314 ? 55.889  35.515  168.049 1.00 41.79  ? 314 PRO A CA    1 
ATOM   2226  C C     . PRO A  1 314 ? 55.769  33.997  167.953 1.00 37.48  ? 314 PRO A C     1 
ATOM   2227  O O     . PRO A  1 314 ? 55.890  33.451  166.858 1.00 41.60  ? 314 PRO A O     1 
ATOM   2228  C CB    . PRO A  1 314 ? 57.335  35.947  168.320 1.00 47.99  ? 314 PRO A CB    1 
ATOM   2229  C CG    . PRO A  1 314 ? 57.395  36.160  169.787 1.00 42.99  ? 314 PRO A CG    1 
ATOM   2230  C CD    . PRO A  1 314 ? 56.050  36.621  170.214 1.00 45.05  ? 314 PRO A CD    1 
ATOM   2231  N N     . GLU A  1 315 ? 55.513  33.340  169.083 1.00 41.87  ? 315 GLU A N     1 
ATOM   2232  C CA    . GLU A  1 315 ? 55.407  31.881  169.151 1.00 45.79  ? 315 GLU A CA    1 
ATOM   2233  C C     . GLU A  1 315 ? 54.313  31.289  168.252 1.00 46.20  ? 315 GLU A C     1 
ATOM   2234  O O     . GLU A  1 315 ? 54.320  30.088  167.968 1.00 48.32  ? 315 GLU A O     1 
ATOM   2235  C CB    . GLU A  1 315 ? 55.153  31.435  170.598 1.00 43.25  ? 315 GLU A CB    1 
ATOM   2236  C CG    . GLU A  1 315 ? 56.320  31.636  171.564 1.00 44.08  ? 315 GLU A CG    1 
ATOM   2237  C CD    . GLU A  1 315 ? 56.229  32.942  172.336 1.00 54.46  ? 315 GLU A CD    1 
ATOM   2238  O OE1   . GLU A  1 315 ? 55.607  33.890  171.818 1.00 46.47  ? 315 GLU A OE1   1 
ATOM   2239  O OE2   . GLU A  1 315 ? 56.775  33.020  173.458 1.00 54.81  ? 315 GLU A OE2   1 
ATOM   2240  N N     . LEU A  1 316 ? 53.369  32.123  167.824 1.00 48.16  ? 316 LEU A N     1 
ATOM   2241  C CA    . LEU A  1 316 ? 52.261  31.654  167.002 1.00 52.17  ? 316 LEU A CA    1 
ATOM   2242  C C     . LEU A  1 316 ? 52.706  31.411  165.561 1.00 53.39  ? 316 LEU A C     1 
ATOM   2243  O O     . LEU A  1 316 ? 52.051  30.672  164.822 1.00 54.15  ? 316 LEU A O     1 
ATOM   2244  C CB    . LEU A  1 316 ? 51.094  32.654  167.042 1.00 45.15  ? 316 LEU A CB    1 
ATOM   2245  C CG    . LEU A  1 316 ? 50.386  32.800  168.393 1.00 43.20  ? 316 LEU A CG    1 
ATOM   2246  C CD1   . LEU A  1 316 ? 49.083  33.577  168.272 1.00 48.72  ? 316 LEU A CD1   1 
ATOM   2247  C CD2   . LEU A  1 316 ? 50.138  31.439  169.026 1.00 46.51  ? 316 LEU A CD2   1 
ATOM   2248  N N     . GLY A  1 317 ? 53.826  32.014  165.175 1.00 50.79  ? 317 GLY A N     1 
ATOM   2249  C CA    . GLY A  1 317 ? 54.347  31.836  163.833 1.00 47.41  ? 317 GLY A CA    1 
ATOM   2250  C C     . GLY A  1 317 ? 53.427  32.422  162.780 1.00 54.35  ? 317 GLY A C     1 
ATOM   2251  O O     . GLY A  1 317 ? 53.307  31.895  161.674 1.00 55.23  ? 317 GLY A O     1 
ATOM   2252  N N     . LEU A  1 318 ? 52.764  33.516  163.137 1.00 55.46  ? 318 LEU A N     1 
ATOM   2253  C CA    . LEU A  1 318 ? 51.891  34.217  162.209 1.00 54.96  ? 318 LEU A CA    1 
ATOM   2254  C C     . LEU A  1 318 ? 52.702  34.932  161.141 1.00 58.43  ? 318 LEU A C     1 
ATOM   2255  O O     . LEU A  1 318 ? 53.666  35.632  161.449 1.00 61.49  ? 318 LEU A O     1 
ATOM   2256  C CB    . LEU A  1 318 ? 51.005  35.217  162.953 1.00 54.37  ? 318 LEU A CB    1 
ATOM   2257  C CG    . LEU A  1 318 ? 49.799  34.650  163.700 1.00 54.79  ? 318 LEU A CG    1 
ATOM   2258  C CD1   . LEU A  1 318 ? 49.220  35.687  164.646 1.00 53.21  ? 318 LEU A CD1   1 
ATOM   2259  C CD2   . LEU A  1 318 ? 48.760  34.199  162.699 1.00 54.24  ? 318 LEU A CD2   1 
ATOM   2260  N N     . VAL A  1 319 ? 52.308  34.751  159.885 1.00 55.52  ? 319 VAL A N     1 
ATOM   2261  C CA    . VAL A  1 319 ? 52.965  35.428  158.775 1.00 59.76  ? 319 VAL A CA    1 
ATOM   2262  C C     . VAL A  1 319 ? 51.990  36.399  158.119 1.00 62.16  ? 319 VAL A C     1 
ATOM   2263  O O     . VAL A  1 319 ? 50.814  36.433  158.474 1.00 57.89  ? 319 VAL A O     1 
ATOM   2264  C CB    . VAL A  1 319 ? 53.494  34.426  157.735 1.00 63.74  ? 319 VAL A CB    1 
ATOM   2265  C CG1   . VAL A  1 319 ? 54.609  33.585  158.342 1.00 58.62  ? 319 VAL A CG1   1 
ATOM   2266  C CG2   . VAL A  1 319 ? 52.367  33.543  157.227 1.00 63.02  ? 319 VAL A CG2   1 
ATOM   2267  N N     . GLU A  1 320 ? 52.483  37.183  157.164 1.00 54.99  ? 320 GLU A N     1 
ATOM   2268  C CA    . GLU A  1 320 ? 51.673  38.213  156.518 1.00 66.81  ? 320 GLU A CA    1 
ATOM   2269  C C     . GLU A  1 320 ? 50.460  37.636  155.791 1.00 68.64  ? 320 GLU A C     1 
ATOM   2270  O O     . GLU A  1 320 ? 49.440  38.309  155.633 1.00 68.20  ? 320 GLU A O     1 
ATOM   2271  C CB    . GLU A  1 320 ? 52.520  39.024  155.535 1.00 69.77  ? 320 GLU A CB    1 
ATOM   2272  C CG    . GLU A  1 320 ? 52.381  40.525  155.706 1.00 72.66  ? 320 GLU A CG    1 
ATOM   2273  C CD    . GLU A  1 320 ? 52.806  41.297  154.473 1.00 89.36  ? 320 GLU A CD    1 
ATOM   2274  O OE1   . GLU A  1 320 ? 54.024  41.384  154.206 1.00 90.03  ? 320 GLU A OE1   1 
ATOM   2275  O OE2   . GLU A  1 320 ? 51.917  41.819  153.767 1.00 90.70  ? 320 GLU A OE2   1 
ATOM   2276  N N     . GLU A  1 321 ? 50.577  36.389  155.352 1.00 71.05  ? 321 GLU A N     1 
ATOM   2277  C CA    . GLU A  1 321 ? 49.514  35.736  154.599 1.00 70.06  ? 321 GLU A CA    1 
ATOM   2278  C C     . GLU A  1 321 ? 48.331  35.369  155.490 1.00 64.43  ? 321 GLU A C     1 
ATOM   2279  O O     . GLU A  1 321 ? 47.210  35.205  155.010 1.00 61.20  ? 321 GLU A O     1 
ATOM   2280  C CB    . GLU A  1 321 ? 50.052  34.481  153.902 1.00 76.33  ? 321 GLU A CB    1 
ATOM   2281  C CG    . GLU A  1 321 ? 51.090  34.743  152.809 1.00 96.37  ? 321 GLU A CG    1 
ATOM   2282  C CD    . GLU A  1 321 ? 52.470  35.099  153.350 1.00 108.17 ? 321 GLU A CD    1 
ATOM   2283  O OE1   . GLU A  1 321 ? 52.602  35.344  154.568 1.00 95.48  ? 321 GLU A OE1   1 
ATOM   2284  O OE2   . GLU A  1 321 ? 53.429  35.135  152.551 1.00 112.37 ? 321 GLU A OE2   1 
ATOM   2285  N N     . ASP A  1 322 ? 48.586  35.237  156.788 1.00 62.69  ? 322 ASP A N     1 
ATOM   2286  C CA    . ASP A  1 322 ? 47.554  34.826  157.733 1.00 59.60  ? 322 ASP A CA    1 
ATOM   2287  C C     . ASP A  1 322 ? 46.587  35.958  158.051 1.00 57.23  ? 322 ASP A C     1 
ATOM   2288  O O     . ASP A  1 322 ? 45.409  35.721  158.316 1.00 54.31  ? 322 ASP A O     1 
ATOM   2289  C CB    . ASP A  1 322 ? 48.193  34.305  159.020 1.00 58.35  ? 322 ASP A CB    1 
ATOM   2290  C CG    . ASP A  1 322 ? 48.938  33.005  158.811 1.00 59.11  ? 322 ASP A CG    1 
ATOM   2291  O OD1   . ASP A  1 322 ? 48.525  32.226  157.926 1.00 62.49  ? 322 ASP A OD1   1 
ATOM   2292  O OD2   . ASP A  1 322 ? 49.931  32.759  159.528 1.00 56.10  ? 322 ASP A OD2   1 
ATOM   2293  N N     . TYR A  1 323 ? 47.088  37.188  158.022 1.00 54.03  ? 323 TYR A N     1 
ATOM   2294  C CA    . TYR A  1 323 ? 46.262  38.350  158.320 1.00 57.20  ? 323 TYR A CA    1 
ATOM   2295  C C     . TYR A  1 323 ? 45.376  38.698  157.135 1.00 55.07  ? 323 TYR A C     1 
ATOM   2296  O O     . TYR A  1 323 ? 45.855  39.129  156.086 1.00 56.37  ? 323 TYR A O     1 
ATOM   2297  C CB    . TYR A  1 323 ? 47.136  39.539  158.712 1.00 56.51  ? 323 TYR A CB    1 
ATOM   2298  C CG    . TYR A  1 323 ? 47.969  39.264  159.940 1.00 53.09  ? 323 TYR A CG    1 
ATOM   2299  C CD1   . TYR A  1 323 ? 47.491  39.563  161.208 1.00 51.59  ? 323 TYR A CD1   1 
ATOM   2300  C CD2   . TYR A  1 323 ? 49.223  38.682  159.832 1.00 52.41  ? 323 TYR A CD2   1 
ATOM   2301  C CE1   . TYR A  1 323 ? 48.247  39.302  162.334 1.00 51.02  ? 323 TYR A CE1   1 
ATOM   2302  C CE2   . TYR A  1 323 ? 49.987  38.416  160.951 1.00 49.07  ? 323 TYR A CE2   1 
ATOM   2303  C CZ    . TYR A  1 323 ? 49.495  38.727  162.199 1.00 49.12  ? 323 TYR A CZ    1 
ATOM   2304  O OH    . TYR A  1 323 ? 50.255  38.465  163.317 1.00 45.38  ? 323 TYR A OH    1 
ATOM   2305  N N     . LEU A  1 324 ? 44.077  38.498  157.316 1.00 52.54  ? 324 LEU A N     1 
ATOM   2306  C CA    . LEU A  1 324 ? 43.106  38.716  156.255 1.00 46.80  ? 324 LEU A CA    1 
ATOM   2307  C C     . LEU A  1 324 ? 42.317  39.993  156.497 1.00 48.11  ? 324 LEU A C     1 
ATOM   2308  O O     . LEU A  1 324 ? 41.703  40.164  157.548 1.00 49.36  ? 324 LEU A O     1 
ATOM   2309  C CB    . LEU A  1 324 ? 42.161  37.519  156.152 1.00 52.92  ? 324 LEU A CB    1 
ATOM   2310  C CG    . LEU A  1 324 ? 42.852  36.163  156.008 1.00 54.30  ? 324 LEU A CG    1 
ATOM   2311  C CD1   . LEU A  1 324 ? 41.882  35.018  156.267 1.00 49.16  ? 324 LEU A CD1   1 
ATOM   2312  C CD2   . LEU A  1 324 ? 43.489  36.035  154.631 1.00 56.87  ? 324 LEU A CD2   1 
ATOM   2313  N N     . GLU A  1 325 ? 42.348  40.896  155.525 1.00 46.47  ? 325 GLU A N     1 
ATOM   2314  C CA    . GLU A  1 325 ? 41.567  42.119  155.613 1.00 47.30  ? 325 GLU A CA    1 
ATOM   2315  C C     . GLU A  1 325 ? 40.223  41.941  154.923 1.00 48.41  ? 325 GLU A C     1 
ATOM   2316  O O     . GLU A  1 325 ? 40.136  41.346  153.849 1.00 51.45  ? 325 GLU A O     1 
ATOM   2317  C CB    . GLU A  1 325 ? 42.320  43.295  154.995 1.00 48.92  ? 325 GLU A CB    1 
ATOM   2318  C CG    . GLU A  1 325 ? 43.573  43.700  155.739 1.00 54.44  ? 325 GLU A CG    1 
ATOM   2319  C CD    . GLU A  1 325 ? 44.296  44.838  155.050 1.00 58.80  ? 325 GLU A CD    1 
ATOM   2320  O OE1   . GLU A  1 325 ? 43.811  45.302  153.999 1.00 67.73  ? 325 GLU A OE1   1 
ATOM   2321  O OE2   . GLU A  1 325 ? 45.341  45.268  155.568 1.00 60.46  ? 325 GLU A OE2   1 
ATOM   2322  N N     . MET A  1 326 ? 39.181  42.467  155.554 1.00 47.74  ? 326 MET A N     1 
ATOM   2323  C CA    . MET A  1 326 ? 37.825  42.374  155.033 1.00 47.73  ? 326 MET A CA    1 
ATOM   2324  C C     . MET A  1 326 ? 36.926  43.344  155.788 1.00 51.93  ? 326 MET A C     1 
ATOM   2325  O O     . MET A  1 326 ? 37.356  43.984  156.749 1.00 46.25  ? 326 MET A O     1 
ATOM   2326  C CB    . MET A  1 326 ? 37.292  40.942  155.146 1.00 46.88  ? 326 MET A CB    1 
ATOM   2327  C CG    . MET A  1 326 ? 37.359  40.348  156.547 1.00 45.31  ? 326 MET A CG    1 
ATOM   2328  S SD    . MET A  1 326 ? 36.977  38.584  156.581 1.00 46.06  ? 326 MET A SD    1 
ATOM   2329  C CE    . MET A  1 326 ? 38.499  37.873  155.963 1.00 45.71  ? 326 MET A CE    1 
ATOM   2330  N N     . SER A  1 327 ? 35.681  43.457  155.343 1.00 51.13  ? 327 SER A N     1 
ATOM   2331  C CA    . SER A  1 327 ? 34.712  44.306  156.017 1.00 49.96  ? 327 SER A CA    1 
ATOM   2332  C C     . SER A  1 327 ? 34.325  43.670  157.347 1.00 47.19  ? 327 SER A C     1 
ATOM   2333  O O     . SER A  1 327 ? 34.608  42.494  157.580 1.00 45.56  ? 327 SER A O     1 
ATOM   2334  C CB    . SER A  1 327 ? 33.474  44.523  155.143 1.00 51.27  ? 327 SER A CB    1 
ATOM   2335  O OG    . SER A  1 327 ? 32.761  43.314  154.958 1.00 47.65  ? 327 SER A OG    1 
ATOM   2336  N N     . TRP A  1 328 ? 33.687  44.448  158.217 1.00 45.30  ? 328 TRP A N     1 
ATOM   2337  C CA    . TRP A  1 328 ? 33.272  43.945  159.522 1.00 45.20  ? 328 TRP A CA    1 
ATOM   2338  C C     . TRP A  1 328 ? 32.328  42.760  159.379 1.00 43.10  ? 328 TRP A C     1 
ATOM   2339  O O     . TRP A  1 328 ? 32.486  41.745  160.059 1.00 43.39  ? 328 TRP A O     1 
ATOM   2340  C CB    . TRP A  1 328 ? 32.594  45.037  160.347 1.00 42.42  ? 328 TRP A CB    1 
ATOM   2341  C CG    . TRP A  1 328 ? 31.870  44.476  161.533 1.00 46.00  ? 328 TRP A CG    1 
ATOM   2342  C CD1   . TRP A  1 328 ? 32.423  44.072  162.712 1.00 47.60  ? 328 TRP A CD1   1 
ATOM   2343  C CD2   . TRP A  1 328 ? 30.461  44.238  161.647 1.00 44.77  ? 328 TRP A CD2   1 
ATOM   2344  N NE1   . TRP A  1 328 ? 31.445  43.604  163.558 1.00 46.01  ? 328 TRP A NE1   1 
ATOM   2345  C CE2   . TRP A  1 328 ? 30.232  43.695  162.927 1.00 45.22  ? 328 TRP A CE2   1 
ATOM   2346  C CE3   . TRP A  1 328 ? 29.372  44.434  160.793 1.00 40.87  ? 328 TRP A CE3   1 
ATOM   2347  C CZ2   . TRP A  1 328 ? 28.959  43.348  163.374 1.00 41.28  ? 328 TRP A CZ2   1 
ATOM   2348  C CZ3   . TRP A  1 328 ? 28.108  44.089  161.237 1.00 42.86  ? 328 TRP A CZ3   1 
ATOM   2349  C CH2   . TRP A  1 328 ? 27.913  43.552  162.516 1.00 44.50  ? 328 TRP A CH2   1 
ATOM   2350  N N     . GLY A  1 329 ? 31.346  42.904  158.494 1.00 44.64  ? 329 GLY A N     1 
ATOM   2351  C CA    . GLY A  1 329 ? 30.388  41.848  158.233 1.00 45.84  ? 329 GLY A CA    1 
ATOM   2352  C C     . GLY A  1 329 ? 31.062  40.598  157.706 1.00 44.64  ? 329 GLY A C     1 
ATOM   2353  O O     . GLY A  1 329 ? 30.760  39.488  158.143 1.00 46.33  ? 329 GLY A O     1 
ATOM   2354  N N     . GLU A  1 330 ? 31.987  40.781  156.769 1.00 46.66  ? 330 GLU A N     1 
ATOM   2355  C CA    . GLU A  1 330 ? 32.730  39.664  156.200 1.00 46.44  ? 330 GLU A CA    1 
ATOM   2356  C C     . GLU A  1 330 ? 33.567  38.956  157.261 1.00 41.46  ? 330 GLU A C     1 
ATOM   2357  O O     . GLU A  1 330 ? 33.745  37.739  157.209 1.00 42.50  ? 330 GLU A O     1 
ATOM   2358  C CB    . GLU A  1 330 ? 33.624  40.141  155.052 1.00 46.78  ? 330 GLU A CB    1 
ATOM   2359  C CG    . GLU A  1 330 ? 32.879  40.350  153.741 1.00 52.37  ? 330 GLU A CG    1 
ATOM   2360  C CD    . GLU A  1 330 ? 33.685  41.137  152.725 1.00 57.44  ? 330 GLU A CD    1 
ATOM   2361  O OE1   . GLU A  1 330 ? 34.851  41.476  153.015 1.00 56.73  ? 330 GLU A OE1   1 
ATOM   2362  O OE2   . GLU A  1 330 ? 33.145  41.424  151.636 1.00 64.48  ? 330 GLU A OE2   1 
ATOM   2363  N N     . SER A  1 331 ? 34.068  39.721  158.226 1.00 45.69  ? 331 SER A N     1 
ATOM   2364  C CA    . SER A  1 331 ? 34.874  39.158  159.302 1.00 46.89  ? 331 SER A CA    1 
ATOM   2365  C C     . SER A  1 331 ? 34.035  38.269  160.214 1.00 44.74  ? 331 SER A C     1 
ATOM   2366  O O     . SER A  1 331 ? 34.471  37.187  160.600 1.00 48.17  ? 331 SER A O     1 
ATOM   2367  C CB    . SER A  1 331 ? 35.544  40.266  160.116 1.00 39.83  ? 331 SER A CB    1 
ATOM   2368  O OG    . SER A  1 331 ? 34.587  41.139  160.687 1.00 48.13  ? 331 SER A OG    1 
ATOM   2369  N N     . PHE A  1 332 ? 32.832  38.722  160.554 1.00 47.86  ? 332 PHE A N     1 
ATOM   2370  C CA    . PHE A  1 332 ? 31.953  37.946  161.424 1.00 44.10  ? 332 PHE A CA    1 
ATOM   2371  C C     . PHE A  1 332 ? 31.419  36.703  160.720 1.00 46.22  ? 332 PHE A C     1 
ATOM   2372  O O     . PHE A  1 332 ? 31.196  35.673  161.358 1.00 48.61  ? 332 PHE A O     1 
ATOM   2373  C CB    . PHE A  1 332 ? 30.796  38.804  161.934 1.00 47.34  ? 332 PHE A CB    1 
ATOM   2374  C CG    . PHE A  1 332 ? 31.115  39.542  163.203 1.00 47.59  ? 332 PHE A CG    1 
ATOM   2375  C CD1   . PHE A  1 332 ? 32.428  39.840  163.529 1.00 47.18  ? 332 PHE A CD1   1 
ATOM   2376  C CD2   . PHE A  1 332 ? 30.112  39.913  164.083 1.00 50.24  ? 332 PHE A CD2   1 
ATOM   2377  C CE1   . PHE A  1 332 ? 32.735  40.509  164.695 1.00 48.36  ? 332 PHE A CE1   1 
ATOM   2378  C CE2   . PHE A  1 332 ? 30.413  40.582  165.256 1.00 49.18  ? 332 PHE A CE2   1 
ATOM   2379  C CZ    . PHE A  1 332 ? 31.728  40.880  165.561 1.00 53.66  ? 332 PHE A CZ    1 
ATOM   2380  N N     . ALA A  1 333 ? 31.216  36.798  159.410 1.00 41.26  ? 333 ALA A N     1 
ATOM   2381  C CA    . ALA A  1 333 ? 30.867  35.627  158.619 1.00 49.10  ? 333 ALA A CA    1 
ATOM   2382  C C     . ALA A  1 333 ? 32.020  34.628  158.648 1.00 49.18  ? 333 ALA A C     1 
ATOM   2383  O O     . ALA A  1 333 ? 31.815  33.427  158.828 1.00 48.99  ? 333 ALA A O     1 
ATOM   2384  C CB    . ALA A  1 333 ? 30.536  36.023  157.193 1.00 48.02  ? 333 ALA A CB    1 
ATOM   2385  N N     . TYR A  1 334 ? 33.232  35.148  158.474 1.00 47.94  ? 334 TYR A N     1 
ATOM   2386  C CA    . TYR A  1 334 ? 34.448  34.345  158.522 1.00 47.47  ? 334 TYR A CA    1 
ATOM   2387  C C     . TYR A  1 334 ? 34.606  33.657  159.875 1.00 50.94  ? 334 TYR A C     1 
ATOM   2388  O O     . TYR A  1 334 ? 34.829  32.448  159.940 1.00 51.75  ? 334 TYR A O     1 
ATOM   2389  C CB    . TYR A  1 334 ? 35.669  35.220  158.231 1.00 51.78  ? 334 TYR A CB    1 
ATOM   2390  C CG    . TYR A  1 334 ? 36.991  34.486  158.276 1.00 54.80  ? 334 TYR A CG    1 
ATOM   2391  C CD1   . TYR A  1 334 ? 37.429  33.737  157.192 1.00 59.03  ? 334 TYR A CD1   1 
ATOM   2392  C CD2   . TYR A  1 334 ? 37.800  34.542  159.403 1.00 54.10  ? 334 TYR A CD2   1 
ATOM   2393  C CE1   . TYR A  1 334 ? 38.634  33.066  157.229 1.00 58.82  ? 334 TYR A CE1   1 
ATOM   2394  C CE2   . TYR A  1 334 ? 39.008  33.874  159.450 1.00 55.80  ? 334 TYR A CE2   1 
ATOM   2395  C CZ    . TYR A  1 334 ? 39.419  33.137  158.360 1.00 56.41  ? 334 TYR A CZ    1 
ATOM   2396  O OH    . TYR A  1 334 ? 40.621  32.471  158.403 1.00 63.11  ? 334 TYR A OH    1 
ATOM   2397  N N     . LEU A  1 335 ? 34.479  34.427  160.952 1.00 51.94  ? 335 LEU A N     1 
ATOM   2398  C CA    . LEU A  1 335 ? 34.657  33.898  162.302 1.00 49.90  ? 335 LEU A CA    1 
ATOM   2399  C C     . LEU A  1 335 ? 33.587  32.875  162.665 1.00 54.88  ? 335 LEU A C     1 
ATOM   2400  O O     . LEU A  1 335 ? 33.799  32.024  163.529 1.00 57.31  ? 335 LEU A O     1 
ATOM   2401  C CB    . LEU A  1 335 ? 34.653  35.036  163.320 1.00 47.91  ? 335 LEU A CB    1 
ATOM   2402  C CG    . LEU A  1 335 ? 35.835  36.005  163.225 1.00 52.31  ? 335 LEU A CG    1 
ATOM   2403  C CD1   . LEU A  1 335 ? 35.577  37.254  164.052 1.00 46.67  ? 335 LEU A CD1   1 
ATOM   2404  C CD2   . LEU A  1 335 ? 37.118  35.326  163.663 1.00 46.48  ? 335 LEU A CD2   1 
ATOM   2405  N N     . ALA A  1 336 ? 32.437  32.966  162.005 1.00 52.58  ? 336 ALA A N     1 
ATOM   2406  C CA    . ALA A  1 336 ? 31.339  32.038  162.240 1.00 53.80  ? 336 ALA A CA    1 
ATOM   2407  C C     . ALA A  1 336 ? 31.535  30.749  161.451 1.00 56.59  ? 336 ALA A C     1 
ATOM   2408  O O     . ALA A  1 336 ? 30.747  29.813  161.569 1.00 55.17  ? 336 ALA A O     1 
ATOM   2409  C CB    . ALA A  1 336 ? 30.022  32.684  161.875 1.00 46.96  ? 336 ALA A CB    1 
ATOM   2410  N N     . GLY A  1 337 ? 32.589  30.711  160.645 1.00 59.07  ? 337 GLY A N     1 
ATOM   2411  C CA    . GLY A  1 337 ? 32.867  29.554  159.818 1.00 54.70  ? 337 GLY A CA    1 
ATOM   2412  C C     . GLY A  1 337 ? 31.991  29.502  158.582 1.00 56.06  ? 337 GLY A C     1 
ATOM   2413  O O     . GLY A  1 337 ? 31.751  28.431  158.027 1.00 60.75  ? 337 GLY A O     1 
ATOM   2414  N N     . LEU A  1 338 ? 31.506  30.663  158.152 1.00 56.38  ? 338 LEU A N     1 
ATOM   2415  C CA    . LEU A  1 338 ? 30.659  30.747  156.966 1.00 56.41  ? 338 LEU A CA    1 
ATOM   2416  C C     . LEU A  1 338 ? 31.460  31.221  155.761 1.00 57.88  ? 338 LEU A C     1 
ATOM   2417  O O     . LEU A  1 338 ? 32.585  31.700  155.902 1.00 57.77  ? 338 LEU A O     1 
ATOM   2418  C CB    . LEU A  1 338 ? 29.473  31.686  157.205 1.00 52.53  ? 338 LEU A CB    1 
ATOM   2419  C CG    . LEU A  1 338 ? 28.573  31.388  158.407 1.00 57.21  ? 338 LEU A CG    1 
ATOM   2420  C CD1   . LEU A  1 338 ? 27.469  32.425  158.516 1.00 50.90  ? 338 LEU A CD1   1 
ATOM   2421  C CD2   . LEU A  1 338 ? 27.984  29.989  158.326 1.00 54.82  ? 338 LEU A CD2   1 
ATOM   2422  N N     . GLU A  1 339 ? 30.872  31.092  154.576 1.00 60.43  ? 339 GLU A N     1 
ATOM   2423  C CA    . GLU A  1 339 ? 31.531  31.513  153.345 1.00 66.87  ? 339 GLU A CA    1 
ATOM   2424  C C     . GLU A  1 339 ? 31.170  32.945  152.966 1.00 65.43  ? 339 GLU A C     1 
ATOM   2425  O O     . GLU A  1 339 ? 32.041  33.741  152.619 1.00 66.29  ? 339 GLU A O     1 
ATOM   2426  C CB    . GLU A  1 339 ? 31.167  30.575  152.193 1.00 71.54  ? 339 GLU A CB    1 
ATOM   2427  C CG    . GLU A  1 339 ? 31.641  29.145  152.371 1.00 77.16  ? 339 GLU A CG    1 
ATOM   2428  C CD    . GLU A  1 339 ? 31.188  28.242  151.241 1.00 86.66  ? 339 GLU A CD    1 
ATOM   2429  O OE1   . GLU A  1 339 ? 30.405  28.706  150.386 1.00 85.25  ? 339 GLU A OE1   1 
ATOM   2430  O OE2   . GLU A  1 339 ? 31.608  27.067  151.214 1.00 93.12  ? 339 GLU A OE2   1 
ATOM   2431  N N     . THR A  1 340 ? 29.882  33.268  153.029 1.00 62.55  ? 340 THR A N     1 
ATOM   2432  C CA    . THR A  1 340 ? 29.403  34.576  152.590 1.00 59.05  ? 340 THR A CA    1 
ATOM   2433  C C     . THR A  1 340 ? 28.620  35.321  153.671 1.00 59.01  ? 340 THR A C     1 
ATOM   2434  O O     . THR A  1 340 ? 28.117  34.720  154.622 1.00 57.38  ? 340 THR A O     1 
ATOM   2435  C CB    . THR A  1 340 ? 28.507  34.449  151.341 1.00 62.24  ? 340 THR A CB    1 
ATOM   2436  O OG1   . THR A  1 340 ? 27.337  33.689  151.666 1.00 60.15  ? 340 THR A OG1   1 
ATOM   2437  C CG2   . THR A  1 340 ? 29.256  33.757  150.210 1.00 62.57  ? 340 THR A CG2   1 
ATOM   2438  N N     . VAL A  1 341 ? 28.525  36.637  153.510 1.00 55.77  ? 341 VAL A N     1 
ATOM   2439  C CA    . VAL A  1 341 ? 27.752  37.487  154.410 1.00 52.81  ? 341 VAL A CA    1 
ATOM   2440  C C     . VAL A  1 341 ? 26.265  37.107  154.369 1.00 56.09  ? 341 VAL A C     1 
ATOM   2441  O O     . VAL A  1 341 ? 25.555  37.217  155.370 1.00 50.62  ? 341 VAL A O     1 
ATOM   2442  C CB    . VAL A  1 341 ? 27.941  38.985  154.049 1.00 50.00  ? 341 VAL A CB    1 
ATOM   2443  C CG1   . VAL A  1 341 ? 26.939  39.864  154.779 1.00 47.38  ? 341 VAL A CG1   1 
ATOM   2444  C CG2   . VAL A  1 341 ? 29.369  39.429  154.355 1.00 48.84  ? 341 VAL A CG2   1 
ATOM   2445  N N     . SER A  1 342 ? 25.809  36.632  153.213 1.00 56.28  ? 342 SER A N     1 
ATOM   2446  C CA    . SER A  1 342 ? 24.408  36.247  153.028 1.00 56.82  ? 342 SER A CA    1 
ATOM   2447  C C     . SER A  1 342 ? 23.978  35.094  153.929 1.00 53.94  ? 342 SER A C     1 
ATOM   2448  O O     . SER A  1 342 ? 22.807  34.985  154.289 1.00 55.90  ? 342 SER A O     1 
ATOM   2449  C CB    . SER A  1 342 ? 24.147  35.872  151.568 1.00 55.59  ? 342 SER A CB    1 
ATOM   2450  O OG    . SER A  1 342 ? 24.171  37.013  150.730 1.00 59.04  ? 342 SER A OG    1 
ATOM   2451  N N     . GLN A  1 343 ? 24.929  34.237  154.289 1.00 54.19  ? 343 GLN A N     1 
ATOM   2452  C CA    . GLN A  1 343 ? 24.646  33.076  155.127 1.00 56.14  ? 343 GLN A CA    1 
ATOM   2453  C C     . GLN A  1 343 ? 24.335  33.470  156.566 1.00 56.23  ? 343 GLN A C     1 
ATOM   2454  O O     . GLN A  1 343 ? 23.745  32.692  157.317 1.00 53.42  ? 343 GLN A O     1 
ATOM   2455  C CB    . GLN A  1 343 ? 25.823  32.103  155.099 1.00 57.34  ? 343 GLN A CB    1 
ATOM   2456  C CG    . GLN A  1 343 ? 26.101  31.520  153.726 1.00 63.15  ? 343 GLN A CG    1 
ATOM   2457  C CD    . GLN A  1 343 ? 27.274  30.564  153.728 1.00 64.10  ? 343 GLN A CD    1 
ATOM   2458  O OE1   . GLN A  1 343 ? 28.421  30.975  153.897 1.00 65.67  ? 343 GLN A OE1   1 
ATOM   2459  N NE2   . GLN A  1 343 ? 26.993  29.280  153.548 1.00 68.05  ? 343 GLN A NE2   1 
ATOM   2460  N N     . LEU A  1 344 ? 24.742  34.676  156.949 1.00 52.06  ? 344 LEU A N     1 
ATOM   2461  C CA    . LEU A  1 344 ? 24.386  35.228  158.251 1.00 48.66  ? 344 LEU A CA    1 
ATOM   2462  C C     . LEU A  1 344 ? 22.867  35.349  158.380 1.00 47.88  ? 344 LEU A C     1 
ATOM   2463  O O     . LEU A  1 344 ? 22.304  35.157  159.458 1.00 43.20  ? 344 LEU A O     1 
ATOM   2464  C CB    . LEU A  1 344 ? 25.045  36.594  158.455 1.00 46.63  ? 344 LEU A CB    1 
ATOM   2465  C CG    . LEU A  1 344 ? 26.574  36.641  158.524 1.00 45.84  ? 344 LEU A CG    1 
ATOM   2466  C CD1   . LEU A  1 344 ? 27.061  38.080  158.500 1.00 44.02  ? 344 LEU A CD1   1 
ATOM   2467  C CD2   . LEU A  1 344 ? 27.073  35.928  159.767 1.00 39.25  ? 344 LEU A CD2   1 
ATOM   2468  N N     . ASN A  1 345 ? 22.208  35.654  157.265 1.00 42.48  ? 345 ASN A N     1 
ATOM   2469  C CA    . ASN A  1 345 ? 20.768  35.898  157.259 1.00 50.34  ? 345 ASN A CA    1 
ATOM   2470  C C     . ASN A  1 345 ? 19.936  34.617  157.166 1.00 50.25  ? 345 ASN A C     1 
ATOM   2471  O O     . ASN A  1 345 ? 18.774  34.656  156.766 1.00 52.80  ? 345 ASN A O     1 
ATOM   2472  C CB    . ASN A  1 345 ? 20.407  36.833  156.102 1.00 48.96  ? 345 ASN A CB    1 
ATOM   2473  C CG    . ASN A  1 345 ? 19.107  37.583  156.336 1.00 51.14  ? 345 ASN A CG    1 
ATOM   2474  O OD1   . ASN A  1 345 ? 18.831  38.042  157.444 1.00 51.72  ? 345 ASN A OD1   1 
ATOM   2475  N ND2   . ASN A  1 345 ? 18.300  37.706  155.289 1.00 53.23  ? 345 ASN A ND2   1 
ATOM   2476  N N     . ASN A  1 346 ? 20.527  33.485  157.534 1.00 49.22  ? 346 ASN A N     1 
ATOM   2477  C CA    . ASN A  1 346 ? 19.797  32.221  157.546 1.00 53.63  ? 346 ASN A CA    1 
ATOM   2478  C C     . ASN A  1 346 ? 19.801  31.597  158.938 1.00 52.19  ? 346 ASN A C     1 
ATOM   2479  O O     . ASN A  1 346 ? 20.796  31.010  159.364 1.00 49.95  ? 346 ASN A O     1 
ATOM   2480  C CB    . ASN A  1 346 ? 20.391  31.245  156.528 1.00 53.07  ? 346 ASN A CB    1 
ATOM   2481  C CG    . ASN A  1 346 ? 19.668  29.910  156.509 1.00 58.06  ? 346 ASN A CG    1 
ATOM   2482  O OD1   . ASN A  1 346 ? 18.489  29.820  156.853 1.00 57.63  ? 346 ASN A OD1   1 
ATOM   2483  N ND2   . ASN A  1 346 ? 20.379  28.861  156.113 1.00 61.97  ? 346 ASN A ND2   1 
ATOM   2484  N N     . ARG A  1 347 ? 18.676  31.718  159.633 1.00 49.85  ? 347 ARG A N     1 
ATOM   2485  C CA    . ARG A  1 347 ? 18.585  31.324  161.033 1.00 49.14  ? 347 ARG A CA    1 
ATOM   2486  C C     . ARG A  1 347 ? 18.548  29.810  161.240 1.00 48.50  ? 347 ARG A C     1 
ATOM   2487  O O     . ARG A  1 347 ? 18.802  29.329  162.344 1.00 43.10  ? 347 ARG A O     1 
ATOM   2488  C CB    . ARG A  1 347 ? 17.345  31.956  161.671 1.00 48.43  ? 347 ARG A CB    1 
ATOM   2489  C CG    . ARG A  1 347 ? 16.038  31.456  161.079 1.00 47.00  ? 347 ARG A CG    1 
ATOM   2490  C CD    . ARG A  1 347 ? 14.827  32.232  161.589 1.00 45.25  ? 347 ARG A CD    1 
ATOM   2491  N NE    . ARG A  1 347 ? 14.675  32.171  163.042 1.00 43.88  ? 347 ARG A NE    1 
ATOM   2492  C CZ    . ARG A  1 347 ? 14.696  33.233  163.842 1.00 42.92  ? 347 ARG A CZ    1 
ATOM   2493  N NH1   . ARG A  1 347 ? 14.863  34.447  163.334 1.00 40.45  ? 347 ARG A NH1   1 
ATOM   2494  N NH2   . ARG A  1 347 ? 14.548  33.086  165.150 1.00 43.11  ? 347 ARG A NH2   1 
ATOM   2495  N N     . PHE A  1 348 ? 18.233  29.059  160.189 1.00 52.18  ? 348 PHE A N     1 
ATOM   2496  C CA    . PHE A  1 348 ? 18.057  27.615  160.330 1.00 58.38  ? 348 PHE A CA    1 
ATOM   2497  C C     . PHE A  1 348 ? 19.266  26.824  159.845 1.00 61.72  ? 348 PHE A C     1 
ATOM   2498  O O     . PHE A  1 348 ? 19.207  25.601  159.727 1.00 59.42  ? 348 PHE A O     1 
ATOM   2499  C CB    . PHE A  1 348 ? 16.805  27.153  159.582 1.00 50.95  ? 348 PHE A CB    1 
ATOM   2500  C CG    . PHE A  1 348 ? 15.547  27.827  160.041 1.00 51.43  ? 348 PHE A CG    1 
ATOM   2501  C CD1   . PHE A  1 348 ? 15.132  27.723  161.359 1.00 49.23  ? 348 PHE A CD1   1 
ATOM   2502  C CD2   . PHE A  1 348 ? 14.778  28.562  159.157 1.00 46.46  ? 348 PHE A CD2   1 
ATOM   2503  C CE1   . PHE A  1 348 ? 13.977  28.347  161.788 1.00 50.66  ? 348 PHE A CE1   1 
ATOM   2504  C CE2   . PHE A  1 348 ? 13.619  29.186  159.578 1.00 51.28  ? 348 PHE A CE2   1 
ATOM   2505  C CZ    . PHE A  1 348 ? 13.218  29.077  160.895 1.00 47.10  ? 348 PHE A CZ    1 
ATOM   2506  N N     . LEU A  1 349 ? 20.360  27.524  159.572 1.00 60.00  ? 349 LEU A N     1 
ATOM   2507  C CA    . LEU A  1 349 ? 21.585  26.873  159.129 1.00 64.02  ? 349 LEU A CA    1 
ATOM   2508  C C     . LEU A  1 349 ? 22.302  26.219  160.307 1.00 70.46  ? 349 LEU A C     1 
ATOM   2509  O O     . LEU A  1 349 ? 22.873  26.909  161.150 1.00 66.01  ? 349 LEU A O     1 
ATOM   2510  C CB    . LEU A  1 349 ? 22.509  27.883  158.440 1.00 63.24  ? 349 LEU A CB    1 
ATOM   2511  C CG    . LEU A  1 349 ? 23.702  27.328  157.659 1.00 73.54  ? 349 LEU A CG    1 
ATOM   2512  C CD1   . LEU A  1 349 ? 23.232  26.322  156.619 1.00 75.35  ? 349 LEU A CD1   1 
ATOM   2513  C CD2   . LEU A  1 349 ? 24.489  28.453  156.999 1.00 65.93  ? 349 LEU A CD2   1 
ATOM   2514  N N     . LYS A  1 350 ? 22.268  24.891  160.372 1.00 70.64  ? 350 LYS A N     1 
ATOM   2515  C CA    . LYS A  1 350 ? 22.987  24.178  161.423 1.00 78.07  ? 350 LYS A CA    1 
ATOM   2516  C C     . LYS A  1 350 ? 24.252  23.527  160.876 1.00 87.88  ? 350 LYS A C     1 
ATOM   2517  O O     . LYS A  1 350 ? 24.187  22.561  160.117 1.00 91.35  ? 350 LYS A O     1 
ATOM   2518  C CB    . LYS A  1 350 ? 22.101  23.113  162.076 1.00 82.56  ? 350 LYS A CB    1 
ATOM   2519  C CG    . LYS A  1 350 ? 20.754  23.611  162.566 1.00 77.19  ? 350 LYS A CG    1 
ATOM   2520  C CD    . LYS A  1 350 ? 20.399  22.997  163.912 1.00 73.36  ? 350 LYS A CD    1 
ATOM   2521  C CE    . LYS A  1 350 ? 18.893  22.886  164.093 1.00 72.46  ? 350 LYS A CE    1 
ATOM   2522  N NZ    . LYS A  1 350 ? 18.196  24.184  163.872 1.00 64.40  ? 350 LYS A NZ    1 
ATOM   2523  N N     . PHE A  1 351 ? 25.402  24.064  161.269 1.00 94.14  ? 351 PHE A N     1 
ATOM   2524  C CA    . PHE A  1 351 ? 26.691  23.516  160.865 1.00 102.51 ? 351 PHE A CA    1 
ATOM   2525  C C     . PHE A  1 351 ? 27.063  22.345  161.774 1.00 100.98 ? 351 PHE A C     1 
ATOM   2526  O O     . PHE A  1 351 ? 27.819  21.452  161.386 1.00 102.46 ? 351 PHE A O     1 
ATOM   2527  C CB    . PHE A  1 351 ? 27.767  24.604  160.902 1.00 107.43 ? 351 PHE A CB    1 
ATOM   2528  C CG    . PHE A  1 351 ? 29.121  24.142  160.442 1.00 115.55 ? 351 PHE A CG    1 
ATOM   2529  C CD1   . PHE A  1 351 ? 29.277  23.506  159.223 1.00 118.09 ? 351 PHE A CD1   1 
ATOM   2530  C CD2   . PHE A  1 351 ? 30.244  24.365  161.225 1.00 118.44 ? 351 PHE A CD2   1 
ATOM   2531  C CE1   . PHE A  1 351 ? 30.524  23.084  158.799 1.00 120.18 ? 351 PHE A CE1   1 
ATOM   2532  C CE2   . PHE A  1 351 ? 31.494  23.947  160.805 1.00 122.50 ? 351 PHE A CE2   1 
ATOM   2533  C CZ    . PHE A  1 351 ? 31.634  23.306  159.590 1.00 121.78 ? 351 PHE A CZ    1 
ATOM   2534  N N     . ASP A  1 352 ? 26.517  22.361  162.987 1.00 95.57  ? 352 ASP A N     1 
ATOM   2535  C CA    . ASP A  1 352 ? 26.695  21.273  163.944 1.00 91.96  ? 352 ASP A CA    1 
ATOM   2536  C C     . ASP A  1 352 ? 25.342  20.857  164.517 1.00 93.00  ? 352 ASP A C     1 
ATOM   2537  O O     . ASP A  1 352 ? 24.477  21.697  164.761 1.00 94.24  ? 352 ASP A O     1 
ATOM   2538  C CB    . ASP A  1 352 ? 27.642  21.688  165.074 1.00 90.29  ? 352 ASP A CB    1 
ATOM   2539  C CG    . ASP A  1 352 ? 28.044  20.520  165.967 1.00 85.76  ? 352 ASP A CG    1 
ATOM   2540  O OD1   . ASP A  1 352 ? 27.274  19.541  166.081 1.00 81.19  ? 352 ASP A OD1   1 
ATOM   2541  O OD2   . ASP A  1 352 ? 29.140  20.578  166.562 1.00 88.47  ? 352 ASP A OD2   1 
ATOM   2542  N N     . GLU A  1 353 ? 25.166  19.556  164.733 1.00 86.45  ? 353 GLU A N     1 
ATOM   2543  C CA    . GLU A  1 353 ? 23.925  19.039  165.302 1.00 79.73  ? 353 GLU A CA    1 
ATOM   2544  C C     . GLU A  1 353 ? 24.170  17.948  166.331 1.00 72.05  ? 353 GLU A C     1 
ATOM   2545  O O     . GLU A  1 353 ? 23.570  16.874  166.260 1.00 73.31  ? 353 GLU A O     1 
ATOM   2546  C CB    . GLU A  1 353 ? 23.013  18.498  164.201 1.00 85.87  ? 353 GLU A CB    1 
ATOM   2547  C CG    . GLU A  1 353 ? 22.435  19.561  163.286 1.00 93.61  ? 353 GLU A CG    1 
ATOM   2548  C CD    . GLU A  1 353 ? 23.253  19.763  162.024 1.00 99.51  ? 353 GLU A CD    1 
ATOM   2549  O OE1   . GLU A  1 353 ? 24.476  19.500  162.040 1.00 98.50  ? 353 GLU A OE1   1 
ATOM   2550  O OE2   . GLU A  1 353 ? 22.666  20.178  161.003 1.00 101.58 ? 353 GLU A OE2   1 
ATOM   2551  N N     . ARG A  1 354 ? 25.044  18.223  167.291 1.00 65.25  ? 354 ARG A N     1 
ATOM   2552  C CA    . ARG A  1 354 ? 25.350  17.254  168.335 1.00 64.20  ? 354 ARG A CA    1 
ATOM   2553  C C     . ARG A  1 354 ? 24.765  17.675  169.678 1.00 54.43  ? 354 ARG A C     1 
ATOM   2554  O O     . ARG A  1 354 ? 24.663  18.866  169.976 1.00 50.12  ? 354 ARG A O     1 
ATOM   2555  C CB    . ARG A  1 354 ? 26.863  17.071  168.464 1.00 65.14  ? 354 ARG A CB    1 
ATOM   2556  C CG    . ARG A  1 354 ? 27.541  16.581  167.197 1.00 69.80  ? 354 ARG A CG    1 
ATOM   2557  C CD    . ARG A  1 354 ? 29.024  16.326  167.429 1.00 75.04  ? 354 ARG A CD    1 
ATOM   2558  N NE    . ARG A  1 354 ? 29.776  17.567  167.605 1.00 75.14  ? 354 ARG A NE    1 
ATOM   2559  C CZ    . ARG A  1 354 ? 31.053  17.630  167.976 1.00 86.13  ? 354 ARG A CZ    1 
ATOM   2560  N NH1   . ARG A  1 354 ? 31.734  16.518  168.222 1.00 75.00  ? 354 ARG A NH1   1 
ATOM   2561  N NH2   . ARG A  1 354 ? 31.651  18.808  168.105 1.00 83.44  ? 354 ARG A NH2   1 
ATOM   2562  N N     . ALA A  1 355 ? 24.372  16.694  170.484 1.00 50.63  ? 355 ALA A N     1 
ATOM   2563  C CA    . ALA A  1 355 ? 24.000  16.961  171.865 1.00 50.90  ? 355 ALA A CA    1 
ATOM   2564  C C     . ALA A  1 355 ? 25.221  17.499  172.591 1.00 54.49  ? 355 ALA A C     1 
ATOM   2565  O O     . ALA A  1 355 ? 26.348  17.181  172.221 1.00 56.45  ? 355 ALA A O     1 
ATOM   2566  C CB    . ALA A  1 355 ? 23.480  15.702  172.544 1.00 50.26  ? 355 ALA A CB    1 
ATOM   2567  N N     . PHE A  1 356 ? 25.011  18.318  173.614 1.00 51.66  ? 356 PHE A N     1 
ATOM   2568  C CA    . PHE A  1 356 ? 26.137  18.802  174.400 1.00 48.65  ? 356 PHE A CA    1 
ATOM   2569  C C     . PHE A  1 356 ? 25.731  19.199  175.808 1.00 46.34  ? 356 PHE A C     1 
ATOM   2570  O O     . PHE A  1 356 ? 24.556  19.419  176.100 1.00 45.31  ? 356 PHE A O     1 
ATOM   2571  C CB    . PHE A  1 356 ? 26.817  19.988  173.699 1.00 50.21  ? 356 PHE A CB    1 
ATOM   2572  C CG    . PHE A  1 356 ? 25.971  21.231  173.637 1.00 50.01  ? 356 PHE A CG    1 
ATOM   2573  C CD1   . PHE A  1 356 ? 26.026  22.180  174.648 1.00 44.93  ? 356 PHE A CD1   1 
ATOM   2574  C CD2   . PHE A  1 356 ? 25.126  21.454  172.563 1.00 46.42  ? 356 PHE A CD2   1 
ATOM   2575  C CE1   . PHE A  1 356 ? 25.248  23.321  174.593 1.00 47.69  ? 356 PHE A CE1   1 
ATOM   2576  C CE2   . PHE A  1 356 ? 24.348  22.597  172.499 1.00 38.65  ? 356 PHE A CE2   1 
ATOM   2577  C CZ    . PHE A  1 356 ? 24.408  23.529  173.517 1.00 41.44  ? 356 PHE A CZ    1 
ATOM   2578  N N     . LYS A  1 357 ? 26.729  19.263  176.677 1.00 46.65  ? 357 LYS A N     1 
ATOM   2579  C CA    . LYS A  1 357 ? 26.595  19.872  177.988 1.00 46.51  ? 357 LYS A CA    1 
ATOM   2580  C C     . LYS A  1 357 ? 27.841  20.725  178.163 1.00 49.36  ? 357 LYS A C     1 
ATOM   2581  O O     . LYS A  1 357 ? 28.918  20.357  177.695 1.00 49.89  ? 357 LYS A O     1 
ATOM   2582  C CB    . LYS A  1 357 ? 26.460  18.812  179.087 1.00 50.38  ? 357 LYS A CB    1 
ATOM   2583  C CG    . LYS A  1 357 ? 26.704  19.311  180.507 1.00 50.57  ? 357 LYS A CG    1 
ATOM   2584  C CD    . LYS A  1 357 ? 25.604  20.216  181.034 1.00 58.59  ? 357 LYS A CD    1 
ATOM   2585  C CE    . LYS A  1 357 ? 26.032  20.867  182.346 1.00 56.30  ? 357 LYS A CE    1 
ATOM   2586  N NZ    . LYS A  1 357 ? 24.944  21.648  183.002 1.00 57.65  ? 357 LYS A NZ    1 
ATOM   2587  N N     . THR A  1 358 ? 27.703  21.882  178.795 1.00 43.87  ? 358 THR A N     1 
ATOM   2588  C CA    . THR A  1 358 ? 28.842  22.775  178.925 1.00 44.97  ? 358 THR A CA    1 
ATOM   2589  C C     . THR A  1 358 ? 28.867  23.446  180.281 1.00 47.34  ? 358 THR A C     1 
ATOM   2590  O O     . THR A  1 358 ? 27.838  23.581  180.939 1.00 49.32  ? 358 THR A O     1 
ATOM   2591  C CB    . THR A  1 358 ? 28.842  23.860  177.830 1.00 42.87  ? 358 THR A CB    1 
ATOM   2592  O OG1   . THR A  1 358 ? 29.864  24.821  178.115 1.00 52.92  ? 358 THR A OG1   1 
ATOM   2593  C CG2   . THR A  1 358 ? 27.505  24.563  177.782 1.00 41.39  ? 358 THR A CG2   1 
ATOM   2594  N N     . LYS A  1 359 ? 30.059  23.849  180.702 1.00 41.84  ? 359 LYS A N     1 
ATOM   2595  C CA    . LYS A  1 359 ? 30.217  24.600  181.939 1.00 42.08  ? 359 LYS A CA    1 
ATOM   2596  C C     . LYS A  1 359 ? 31.190  25.743  181.690 1.00 40.93  ? 359 LYS A C     1 
ATOM   2597  O O     . LYS A  1 359 ? 31.839  25.794  180.646 1.00 39.11  ? 359 LYS A O     1 
ATOM   2598  C CB    . LYS A  1 359 ? 30.709  23.702  183.075 1.00 45.88  ? 359 LYS A CB    1 
ATOM   2599  C CG    . LYS A  1 359 ? 29.850  22.465  183.308 1.00 47.84  ? 359 LYS A CG    1 
ATOM   2600  C CD    . LYS A  1 359 ? 30.305  21.684  184.528 1.00 49.82  ? 359 LYS A CD    1 
ATOM   2601  C CE    . LYS A  1 359 ? 29.910  22.384  185.818 1.00 45.08  ? 359 LYS A CE    1 
ATOM   2602  N NZ    . LYS A  1 359 ? 28.474  22.180  186.147 1.00 57.42  ? 359 LYS A NZ    1 
ATOM   2603  N N     . VAL A  1 360 ? 31.295  26.662  182.639 1.00 35.32  ? 360 VAL A N     1 
ATOM   2604  C CA    . VAL A  1 360 ? 32.164  27.808  182.443 1.00 38.45  ? 360 VAL A CA    1 
ATOM   2605  C C     . VAL A  1 360 ? 32.775  28.275  183.760 1.00 42.47  ? 360 VAL A C     1 
ATOM   2606  O O     . VAL A  1 360 ? 32.193  28.096  184.830 1.00 43.04  ? 360 VAL A O     1 
ATOM   2607  C CB    . VAL A  1 360 ? 31.398  28.979  181.768 1.00 40.09  ? 360 VAL A CB    1 
ATOM   2608  C CG1   . VAL A  1 360 ? 30.437  29.637  182.746 1.00 38.18  ? 360 VAL A CG1   1 
ATOM   2609  C CG2   . VAL A  1 360 ? 32.369  29.994  181.192 1.00 39.19  ? 360 VAL A CG2   1 
ATOM   2610  N N     . ASP A  1 361 ? 33.974  28.837  183.674 1.00 37.38  ? 361 ASP A N     1 
ATOM   2611  C CA    . ASP A  1 361 ? 34.617  29.459  184.819 1.00 39.92  ? 361 ASP A CA    1 
ATOM   2612  C C     . ASP A  1 361 ? 35.011  30.887  184.475 1.00 35.19  ? 361 ASP A C     1 
ATOM   2613  O O     . ASP A  1 361 ? 35.280  31.201  183.317 1.00 33.99  ? 361 ASP A O     1 
ATOM   2614  C CB    . ASP A  1 361 ? 35.852  28.661  185.253 1.00 44.64  ? 361 ASP A CB    1 
ATOM   2615  C CG    . ASP A  1 361 ? 35.524  27.569  186.252 1.00 45.33  ? 361 ASP A CG    1 
ATOM   2616  O OD1   . ASP A  1 361 ? 34.818  27.856  187.240 1.00 45.14  ? 361 ASP A OD1   1 
ATOM   2617  O OD2   . ASP A  1 361 ? 35.975  26.422  186.047 1.00 48.32  ? 361 ASP A OD2   1 
ATOM   2618  N N     . LEU A  1 362 ? 35.027  31.755  185.478 1.00 36.78  ? 362 LEU A N     1 
ATOM   2619  C CA    . LEU A  1 362 ? 35.654  33.057  185.329 1.00 41.29  ? 362 LEU A CA    1 
ATOM   2620  C C     . LEU A  1 362 ? 36.773  33.147  186.356 1.00 47.01  ? 362 LEU A C     1 
ATOM   2621  O O     . LEU A  1 362 ? 36.621  32.688  187.485 1.00 46.79  ? 362 LEU A O     1 
ATOM   2622  C CB    . LEU A  1 362 ? 34.640  34.188  185.495 1.00 39.01  ? 362 LEU A CB    1 
ATOM   2623  C CG    . LEU A  1 362 ? 33.580  34.214  184.385 1.00 37.53  ? 362 LEU A CG    1 
ATOM   2624  C CD1   . LEU A  1 362 ? 32.254  33.678  184.895 1.00 38.46  ? 362 LEU A CD1   1 
ATOM   2625  C CD2   . LEU A  1 362 ? 33.418  35.605  183.796 1.00 39.48  ? 362 LEU A CD2   1 
ATOM   2626  N N     . THR A  1 363 ? 37.906  33.713  185.959 1.00 47.72  ? 363 THR A N     1 
ATOM   2627  C CA    . THR A  1 363 ? 39.092  33.692  186.805 1.00 42.98  ? 363 THR A CA    1 
ATOM   2628  C C     . THR A  1 363 ? 39.423  35.077  187.353 1.00 50.23  ? 363 THR A C     1 
ATOM   2629  O O     . THR A  1 363 ? 39.107  36.093  186.736 1.00 50.55  ? 363 THR A O     1 
ATOM   2630  C CB    . THR A  1 363 ? 40.307  33.148  186.033 1.00 43.75  ? 363 THR A CB    1 
ATOM   2631  O OG1   . THR A  1 363 ? 40.667  34.068  184.994 1.00 42.92  ? 363 THR A OG1   1 
ATOM   2632  C CG2   . THR A  1 363 ? 39.980  31.799  185.412 1.00 40.70  ? 363 THR A CG2   1 
ATOM   2633  N N     . LYS A  1 364 ? 40.052  35.108  188.523 1.00 48.37  ? 364 LYS A N     1 
ATOM   2634  C CA    . LYS A  1 364 ? 40.526  36.359  189.105 1.00 51.67  ? 364 LYS A CA    1 
ATOM   2635  C C     . LYS A  1 364 ? 42.051  36.372  189.145 1.00 53.84  ? 364 LYS A C     1 
ATOM   2636  O O     . LYS A  1 364 ? 42.679  37.411  188.942 1.00 55.59  ? 364 LYS A O     1 
ATOM   2637  C CB    . LYS A  1 364 ? 39.956  36.559  190.507 1.00 52.29  ? 364 LYS A CB    1 
ATOM   2638  C CG    . LYS A  1 364 ? 38.441  36.463  190.564 1.00 58.54  ? 364 LYS A CG    1 
ATOM   2639  C CD    . LYS A  1 364 ? 37.775  37.555  189.737 1.00 58.90  ? 364 LYS A CD    1 
ATOM   2640  C CE    . LYS A  1 364 ? 37.358  38.734  190.606 1.00 61.26  ? 364 LYS A CE    1 
ATOM   2641  N NZ    . LYS A  1 364 ? 36.509  39.724  189.876 1.00 60.10  ? 364 LYS A NZ    1 
ATOM   2642  N N     . GLU A  1 365 ? 42.640  35.211  189.410 1.00 50.57  ? 365 GLU A N     1 
ATOM   2643  C CA    . GLU A  1 365 ? 44.091  35.081  189.436 1.00 55.65  ? 365 GLU A CA    1 
ATOM   2644  C C     . GLU A  1 365 ? 44.577  34.324  188.206 1.00 51.98  ? 365 GLU A C     1 
ATOM   2645  O O     . GLU A  1 365 ? 43.845  33.498  187.659 1.00 48.70  ? 365 GLU A O     1 
ATOM   2646  C CB    . GLU A  1 365 ? 44.550  34.372  190.716 1.00 55.46  ? 365 GLU A CB    1 
ATOM   2647  C CG    . GLU A  1 365 ? 44.085  35.033  192.008 1.00 55.74  ? 365 GLU A CG    1 
ATOM   2648  C CD    . GLU A  1 365 ? 44.672  36.420  192.214 1.00 69.86  ? 365 GLU A CD    1 
ATOM   2649  O OE1   . GLU A  1 365 ? 45.650  36.773  191.520 1.00 75.07  ? 365 GLU A OE1   1 
ATOM   2650  O OE2   . GLU A  1 365 ? 44.154  37.160  193.077 1.00 68.79  ? 365 GLU A OE2   1 
ATOM   2651  N N     . PRO A  1 366 ? 45.811  34.613  187.761 1.00 51.09  ? 366 PRO A N     1 
ATOM   2652  C CA    . PRO A  1 366 ? 46.386  33.893  186.620 1.00 48.87  ? 366 PRO A CA    1 
ATOM   2653  C C     . PRO A  1 366 ? 46.403  32.389  186.864 1.00 52.86  ? 366 PRO A C     1 
ATOM   2654  O O     . PRO A  1 366 ? 46.546  31.959  188.009 1.00 53.99  ? 366 PRO A O     1 
ATOM   2655  C CB    . PRO A  1 366 ? 47.811  34.448  186.535 1.00 51.94  ? 366 PRO A CB    1 
ATOM   2656  C CG    . PRO A  1 366 ? 47.725  35.799  187.153 1.00 52.06  ? 366 PRO A CG    1 
ATOM   2657  C CD    . PRO A  1 366 ? 46.711  35.671  188.254 1.00 53.86  ? 366 PRO A CD    1 
ATOM   2658  N N     . LEU A  1 367 ? 46.236  31.601  185.808 1.00 48.26  ? 367 LEU A N     1 
ATOM   2659  C CA    . LEU A  1 367 ? 46.285  30.152  185.939 1.00 47.31  ? 367 LEU A CA    1 
ATOM   2660  C C     . LEU A  1 367 ? 47.726  29.665  185.939 1.00 57.33  ? 367 LEU A C     1 
ATOM   2661  O O     . LEU A  1 367 ? 48.482  29.963  185.011 1.00 56.80  ? 367 LEU A O     1 
ATOM   2662  C CB    . LEU A  1 367 ? 45.505  29.478  184.808 1.00 50.68  ? 367 LEU A CB    1 
ATOM   2663  C CG    . LEU A  1 367 ? 44.007  29.792  184.739 1.00 48.86  ? 367 LEU A CG    1 
ATOM   2664  C CD1   . LEU A  1 367 ? 43.370  29.100  183.551 1.00 37.96  ? 367 LEU A CD1   1 
ATOM   2665  C CD2   . LEU A  1 367 ? 43.323  29.376  186.024 1.00 49.05  ? 367 LEU A CD2   1 
ATOM   2666  N N     . PRO A  1 368 ? 48.119  28.915  186.980 1.00 56.21  ? 368 PRO A N     1 
ATOM   2667  C CA    . PRO A  1 368 ? 49.463  28.331  186.983 1.00 59.49  ? 368 PRO A CA    1 
ATOM   2668  C C     . PRO A  1 368 ? 49.629  27.348  185.830 1.00 58.82  ? 368 PRO A C     1 
ATOM   2669  O O     . PRO A  1 368 ? 48.631  26.850  185.308 1.00 58.74  ? 368 PRO A O     1 
ATOM   2670  C CB    . PRO A  1 368 ? 49.541  27.624  188.340 1.00 59.90  ? 368 PRO A CB    1 
ATOM   2671  C CG    . PRO A  1 368 ? 48.125  27.386  188.730 1.00 58.62  ? 368 PRO A CG    1 
ATOM   2672  C CD    . PRO A  1 368 ? 47.355  28.551  188.184 1.00 58.63  ? 368 PRO A CD    1 
ATOM   2673  N N     . SER A  1 369 ? 50.869  27.085  185.437 1.00 58.35  ? 369 SER A N     1 
ATOM   2674  C CA    . SER A  1 369 ? 51.145  26.246  184.277 1.00 57.03  ? 369 SER A CA    1 
ATOM   2675  C C     . SER A  1 369 ? 50.559  24.842  184.437 1.00 59.49  ? 369 SER A C     1 
ATOM   2676  O O     . SER A  1 369 ? 50.188  24.202  183.456 1.00 62.10  ? 369 SER A O     1 
ATOM   2677  C CB    . SER A  1 369 ? 52.655  26.166  184.031 1.00 57.40  ? 369 SER A CB    1 
ATOM   2678  O OG    . SER A  1 369 ? 52.939  25.696  182.726 1.00 62.97  ? 369 SER A OG    1 
ATOM   2679  N N     . LYS A  1 370 ? 50.456  24.377  185.678 1.00 55.54  ? 370 LYS A N     1 
ATOM   2680  C CA    . LYS A  1 370 ? 49.935  23.042  185.948 1.00 60.57  ? 370 LYS A CA    1 
ATOM   2681  C C     . LYS A  1 370 ? 48.420  22.946  185.731 1.00 62.93  ? 370 LYS A C     1 
ATOM   2682  O O     . LYS A  1 370 ? 47.891  21.864  185.469 1.00 63.27  ? 370 LYS A O     1 
ATOM   2683  C CB    . LYS A  1 370 ? 50.290  22.615  187.374 1.00 60.06  ? 370 LYS A CB    1 
ATOM   2684  C CG    . LYS A  1 370 ? 49.876  23.600  188.455 1.00 60.54  ? 370 LYS A CG    1 
ATOM   2685  C CD    . LYS A  1 370 ? 50.129  23.005  189.831 1.00 62.22  ? 370 LYS A CD    1 
ATOM   2686  C CE    . LYS A  1 370 ? 49.336  23.728  190.906 1.00 69.91  ? 370 LYS A CE    1 
ATOM   2687  N NZ    . LYS A  1 370 ? 50.208  24.546  191.791 1.00 74.97  ? 370 LYS A NZ    1 
ATOM   2688  N N     . ALA A  1 371 ? 47.733  24.081  185.842 1.00 58.66  ? 371 ALA A N     1 
ATOM   2689  C CA    . ALA A  1 371 ? 46.294  24.145  185.586 1.00 57.81  ? 371 ALA A CA    1 
ATOM   2690  C C     . ALA A  1 371 ? 45.986  23.785  184.138 1.00 51.99  ? 371 ALA A C     1 
ATOM   2691  O O     . ALA A  1 371 ? 45.157  22.916  183.861 1.00 54.93  ? 371 ALA A O     1 
ATOM   2692  C CB    . ALA A  1 371 ? 45.754  25.529  185.911 1.00 55.11  ? 371 ALA A CB    1 
ATOM   2693  N N     . PHE A  1 372 ? 46.657  24.471  183.219 1.00 50.54  ? 372 PHE A N     1 
ATOM   2694  C CA    . PHE A  1 372 ? 46.509  24.197  181.798 1.00 50.36  ? 372 PHE A CA    1 
ATOM   2695  C C     . PHE A  1 372 ? 46.938  22.774  181.464 1.00 57.87  ? 372 PHE A C     1 
ATOM   2696  O O     . PHE A  1 372 ? 46.283  22.097  180.674 1.00 57.42  ? 372 PHE A O     1 
ATOM   2697  C CB    . PHE A  1 372 ? 47.316  25.195  180.968 1.00 54.44  ? 372 PHE A CB    1 
ATOM   2698  C CG    . PHE A  1 372 ? 46.670  26.545  180.845 1.00 54.83  ? 372 PHE A CG    1 
ATOM   2699  C CD1   . PHE A  1 372 ? 45.498  26.699  180.126 1.00 54.42  ? 372 PHE A CD1   1 
ATOM   2700  C CD2   . PHE A  1 372 ? 47.242  27.661  181.436 1.00 52.49  ? 372 PHE A CD2   1 
ATOM   2701  C CE1   . PHE A  1 372 ? 44.900  27.939  180.004 1.00 52.70  ? 372 PHE A CE1   1 
ATOM   2702  C CE2   . PHE A  1 372 ? 46.649  28.904  181.318 1.00 51.17  ? 372 PHE A CE2   1 
ATOM   2703  C CZ    . PHE A  1 372 ? 45.477  29.043  180.599 1.00 53.81  ? 372 PHE A CZ    1 
ATOM   2704  N N     . TYR A  1 373 ? 48.037  22.329  182.069 1.00 60.70  ? 373 TYR A N     1 
ATOM   2705  C CA    . TYR A  1 373 ? 48.549  20.985  181.824 1.00 57.51  ? 373 TYR A CA    1 
ATOM   2706  C C     . TYR A  1 373 ? 47.485  19.941  182.121 1.00 53.89  ? 373 TYR A C     1 
ATOM   2707  O O     . TYR A  1 373 ? 47.195  19.089  181.282 1.00 59.50  ? 373 TYR A O     1 
ATOM   2708  C CB    . TYR A  1 373 ? 49.796  20.693  182.663 1.00 66.98  ? 373 TYR A CB    1 
ATOM   2709  C CG    . TYR A  1 373 ? 50.363  19.316  182.383 1.00 65.89  ? 373 TYR A CG    1 
ATOM   2710  C CD1   . TYR A  1 373 ? 51.302  19.127  181.380 1.00 67.72  ? 373 TYR A CD1   1 
ATOM   2711  C CD2   . TYR A  1 373 ? 49.943  18.202  183.109 1.00 69.13  ? 373 TYR A CD2   1 
ATOM   2712  C CE1   . TYR A  1 373 ? 51.814  17.877  181.110 1.00 67.41  ? 373 TYR A CE1   1 
ATOM   2713  C CE2   . TYR A  1 373 ? 50.446  16.950  182.844 1.00 75.65  ? 373 TYR A CE2   1 
ATOM   2714  C CZ    . TYR A  1 373 ? 51.383  16.793  181.845 1.00 77.71  ? 373 TYR A CZ    1 
ATOM   2715  O OH    . TYR A  1 373 ? 51.888  15.542  181.583 1.00 84.07  ? 373 TYR A OH    1 
ATOM   2716  N N     . GLY A  1 374 ? 46.912  20.003  183.319 1.00 51.36  ? 374 GLY A N     1 
ATOM   2717  C CA    . GLY A  1 374 ? 45.886  19.051  183.713 1.00 60.86  ? 374 GLY A CA    1 
ATOM   2718  C C     . GLY A  1 374 ? 44.649  19.113  182.832 1.00 60.18  ? 374 GLY A C     1 
ATOM   2719  O O     . GLY A  1 374 ? 44.047  18.083  182.509 1.00 61.20  ? 374 GLY A O     1 
ATOM   2720  N N     . LEU A  1 375 ? 44.277  20.329  182.439 1.00 58.81  ? 375 LEU A N     1 
ATOM   2721  C CA    . LEU A  1 375 ? 43.115  20.556  181.578 1.00 57.19  ? 375 LEU A CA    1 
ATOM   2722  C C     . LEU A  1 375 ? 43.295  19.866  180.225 1.00 58.32  ? 375 LEU A C     1 
ATOM   2723  O O     . LEU A  1 375 ? 42.387  19.193  179.731 1.00 58.39  ? 375 LEU A O     1 
ATOM   2724  C CB    . LEU A  1 375 ? 42.883  22.061  181.393 1.00 53.22  ? 375 LEU A CB    1 
ATOM   2725  C CG    . LEU A  1 375 ? 41.584  22.505  180.727 1.00 57.55  ? 375 LEU A CG    1 
ATOM   2726  C CD1   . LEU A  1 375 ? 40.386  21.902  181.440 1.00 44.88  ? 375 LEU A CD1   1 
ATOM   2727  C CD2   . LEU A  1 375 ? 41.474  24.025  180.696 1.00 43.95  ? 375 LEU A CD2   1 
ATOM   2728  N N     . LEU A  1 376 ? 44.473  20.041  179.635 1.00 57.32  ? 376 LEU A N     1 
ATOM   2729  C CA    . LEU A  1 376 ? 44.805  19.403  178.366 1.00 63.38  ? 376 LEU A CA    1 
ATOM   2730  C C     . LEU A  1 376 ? 44.971  17.894  178.520 1.00 64.96  ? 376 LEU A C     1 
ATOM   2731  O O     . LEU A  1 376 ? 44.698  17.133  177.593 1.00 66.72  ? 376 LEU A O     1 
ATOM   2732  C CB    . LEU A  1 376 ? 46.083  20.013  177.790 1.00 60.56  ? 376 LEU A CB    1 
ATOM   2733  C CG    . LEU A  1 376 ? 46.044  21.531  177.597 1.00 56.77  ? 376 LEU A CG    1 
ATOM   2734  C CD1   . LEU A  1 376 ? 47.420  22.088  177.250 1.00 56.37  ? 376 LEU A CD1   1 
ATOM   2735  C CD2   . LEU A  1 376 ? 45.014  21.909  176.545 1.00 58.87  ? 376 LEU A CD2   1 
ATOM   2736  N N     . GLU A  1 377 ? 45.420  17.474  179.698 1.00 63.20  ? 377 GLU A N     1 
ATOM   2737  C CA    . GLU A  1 377 ? 45.610  16.060  179.999 1.00 67.86  ? 377 GLU A CA    1 
ATOM   2738  C C     . GLU A  1 377 ? 44.285  15.304  179.921 1.00 71.33  ? 377 GLU A C     1 
ATOM   2739  O O     . GLU A  1 377 ? 44.189  14.262  179.274 1.00 76.50  ? 377 GLU A O     1 
ATOM   2740  C CB    . GLU A  1 377 ? 46.235  15.896  181.384 1.00 67.59  ? 377 GLU A CB    1 
ATOM   2741  C CG    . GLU A  1 377 ? 47.220  14.751  181.495 1.00 76.80  ? 377 GLU A CG    1 
ATOM   2742  C CD    . GLU A  1 377 ? 47.821  14.639  182.881 1.00 76.84  ? 377 GLU A CD    1 
ATOM   2743  O OE1   . GLU A  1 377 ? 47.254  15.224  183.828 1.00 77.40  ? 377 GLU A OE1   1 
ATOM   2744  O OE2   . GLU A  1 377 ? 48.864  13.968  183.022 1.00 83.06  ? 377 GLU A OE2   1 
ATOM   2745  N N     . ARG A  1 378 ? 43.264  15.839  180.580 1.00 67.83  ? 378 ARG A N     1 
ATOM   2746  C CA    . ARG A  1 378 ? 41.934  15.240  180.558 1.00 68.91  ? 378 ARG A CA    1 
ATOM   2747  C C     . ARG A  1 378 ? 41.278  15.381  179.193 1.00 64.98  ? 378 ARG A C     1 
ATOM   2748  O O     . ARG A  1 378 ? 40.504  14.518  178.773 1.00 66.00  ? 378 ARG A O     1 
ATOM   2749  C CB    . ARG A  1 378 ? 41.054  15.877  181.629 1.00 62.50  ? 378 ARG A CB    1 
ATOM   2750  C CG    . ARG A  1 378 ? 41.396  15.450  183.035 1.00 67.77  ? 378 ARG A CG    1 
ATOM   2751  C CD    . ARG A  1 378 ? 41.384  16.640  183.976 1.00 66.46  ? 378 ARG A CD    1 
ATOM   2752  N NE    . ARG A  1 378 ? 41.379  16.226  185.375 1.00 69.19  ? 378 ARG A NE    1 
ATOM   2753  C CZ    . ARG A  1 378 ? 42.451  16.205  186.160 1.00 72.27  ? 378 ARG A CZ    1 
ATOM   2754  N NH1   . ARG A  1 378 ? 43.634  16.579  185.691 1.00 67.33  ? 378 ARG A NH1   1 
ATOM   2755  N NH2   . ARG A  1 378 ? 42.336  15.815  187.422 1.00 78.60  ? 378 ARG A NH2   1 
ATOM   2756  N N     . LEU A  1 379 ? 41.594  16.477  178.509 1.00 63.05  ? 379 LEU A N     1 
ATOM   2757  C CA    . LEU A  1 379 ? 41.102  16.720  177.157 1.00 63.85  ? 379 LEU A CA    1 
ATOM   2758  C C     . LEU A  1 379 ? 41.555  15.598  176.214 1.00 69.75  ? 379 LEU A C     1 
ATOM   2759  O O     . LEU A  1 379 ? 40.785  15.129  175.372 1.00 63.93  ? 379 LEU A O     1 
ATOM   2760  C CB    . LEU A  1 379 ? 41.585  18.090  176.652 1.00 60.52  ? 379 LEU A CB    1 
ATOM   2761  C CG    . LEU A  1 379 ? 40.708  18.832  175.641 1.00 63.51  ? 379 LEU A CG    1 
ATOM   2762  C CD1   . LEU A  1 379 ? 39.252  18.741  176.063 1.00 56.02  ? 379 LEU A CD1   1 
ATOM   2763  C CD2   . LEU A  1 379 ? 41.130  20.294  175.497 1.00 57.39  ? 379 LEU A CD2   1 
ATOM   2764  N N     . SER A  1 380 ? 42.806  15.170  176.373 1.00 73.22  ? 380 SER A N     1 
ATOM   2765  C CA    . SER A  1 380 ? 43.362  14.077  175.580 1.00 74.05  ? 380 SER A CA    1 
ATOM   2766  C C     . SER A  1 380 ? 42.654  12.760  175.866 1.00 77.56  ? 380 SER A C     1 
ATOM   2767  O O     . SER A  1 380 ? 42.537  11.903  174.992 1.00 83.24  ? 380 SER A O     1 
ATOM   2768  C CB    . SER A  1 380 ? 44.862  13.936  175.843 1.00 79.75  ? 380 SER A CB    1 
ATOM   2769  O OG    . SER A  1 380 ? 45.143  13.959  177.232 1.00 78.39  ? 380 SER A OG    1 
ATOM   2770  N N     . LYS A  1 381 ? 42.175  12.609  177.096 1.00 76.84  ? 381 LYS A N     1 
ATOM   2771  C CA    . LYS A  1 381 ? 41.453  11.408  177.490 1.00 76.32  ? 381 LYS A CA    1 
ATOM   2772  C C     . LYS A  1 381 ? 40.011  11.406  176.985 1.00 75.10  ? 381 LYS A C     1 
ATOM   2773  O O     . LYS A  1 381 ? 39.254  10.482  177.276 1.00 74.54  ? 381 LYS A O     1 
ATOM   2774  C CB    . LYS A  1 381 ? 41.462  11.255  179.011 1.00 82.92  ? 381 LYS A CB    1 
ATOM   2775  C CG    . LYS A  1 381 ? 42.805  10.850  179.590 1.00 88.04  ? 381 LYS A CG    1 
ATOM   2776  C CD    . LYS A  1 381 ? 42.690  10.584  181.081 1.00 89.71  ? 381 LYS A CD    1 
ATOM   2777  C CE    . LYS A  1 381 ? 42.147  11.800  181.811 1.00 83.44  ? 381 LYS A CE    1 
ATOM   2778  N NZ    . LYS A  1 381 ? 41.921  11.538  183.257 1.00 87.01  ? 381 LYS A NZ    1 
ATOM   2779  N N     . GLU A  1 382 ? 39.631  12.435  176.230 1.00 72.30  ? 382 GLU A N     1 
ATOM   2780  C CA    . GLU A  1 382 ? 38.252  12.558  175.764 1.00 66.65  ? 382 GLU A CA    1 
ATOM   2781  C C     . GLU A  1 382 ? 38.139  13.371  174.472 1.00 62.23  ? 382 GLU A C     1 
ATOM   2782  O O     . GLU A  1 382 ? 38.123  14.602  174.503 1.00 55.21  ? 382 GLU A O     1 
ATOM   2783  C CB    . GLU A  1 382 ? 37.385  13.181  176.861 1.00 63.64  ? 382 GLU A CB    1 
ATOM   2784  C CG    . GLU A  1 382 ? 35.925  13.360  176.479 1.00 64.72  ? 382 GLU A CG    1 
ATOM   2785  C CD    . GLU A  1 382 ? 35.345  12.142  175.788 1.00 65.08  ? 382 GLU A CD    1 
ATOM   2786  O OE1   . GLU A  1 382 ? 35.038  11.147  176.479 1.00 69.87  ? 382 GLU A OE1   1 
ATOM   2787  O OE2   . GLU A  1 382 ? 35.197  12.180  174.550 1.00 63.21  ? 382 GLU A OE2   1 
ATOM   2788  N N     . PRO A  1 383 ? 38.045  12.671  173.331 1.00 61.13  ? 383 PRO A N     1 
ATOM   2789  C CA    . PRO A  1 383 ? 38.020  13.267  171.990 1.00 63.78  ? 383 PRO A CA    1 
ATOM   2790  C C     . PRO A  1 383 ? 36.768  14.098  171.721 1.00 60.72  ? 383 PRO A C     1 
ATOM   2791  O O     . PRO A  1 383 ? 36.766  14.905  170.794 1.00 65.15  ? 383 PRO A O     1 
ATOM   2792  C CB    . PRO A  1 383 ? 38.066  12.045  171.061 1.00 61.78  ? 383 PRO A CB    1 
ATOM   2793  C CG    . PRO A  1 383 ? 38.546  10.913  171.922 1.00 64.55  ? 383 PRO A CG    1 
ATOM   2794  C CD    . PRO A  1 383 ? 37.985  11.202  173.270 1.00 62.80  ? 383 PRO A CD    1 
ATOM   2795  N N     . ASN A  1 384 ? 35.721  13.899  172.514 1.00 58.58  ? 384 ASN A N     1 
ATOM   2796  C CA    . ASN A  1 384 ? 34.498  14.680  172.361 1.00 60.04  ? 384 ASN A CA    1 
ATOM   2797  C C     . ASN A  1 384 ? 34.497  15.906  173.265 1.00 61.64  ? 384 ASN A C     1 
ATOM   2798  O O     . ASN A  1 384 ? 33.502  16.626  173.358 1.00 52.46  ? 384 ASN A O     1 
ATOM   2799  C CB    . ASN A  1 384 ? 33.272  13.816  172.643 1.00 58.90  ? 384 ASN A CB    1 
ATOM   2800  C CG    . ASN A  1 384 ? 33.025  12.794  171.554 1.00 64.68  ? 384 ASN A CG    1 
ATOM   2801  O OD1   . ASN A  1 384 ? 32.198  13.003  170.666 1.00 63.97  ? 384 ASN A OD1   1 
ATOM   2802  N ND2   . ASN A  1 384 ? 33.751  11.682  171.610 1.00 67.48  ? 384 ASN A ND2   1 
ATOM   2803  N N     . GLY A  1 385 ? 35.627  16.140  173.925 1.00 58.27  ? 385 GLY A N     1 
ATOM   2804  C CA    . GLY A  1 385 ? 35.775  17.279  174.811 1.00 57.16  ? 385 GLY A CA    1 
ATOM   2805  C C     . GLY A  1 385 ? 36.400  18.463  174.102 1.00 54.64  ? 385 GLY A C     1 
ATOM   2806  O O     . GLY A  1 385 ? 37.238  18.301  173.216 1.00 51.93  ? 385 GLY A O     1 
ATOM   2807  N N     . PHE A  1 386 ? 35.979  19.662  174.488 1.00 50.36  ? 386 PHE A N     1 
ATOM   2808  C CA    . PHE A  1 386 ? 36.529  20.889  173.929 1.00 45.24  ? 386 PHE A CA    1 
ATOM   2809  C C     . PHE A  1 386 ? 36.694  21.933  175.019 1.00 47.18  ? 386 PHE A C     1 
ATOM   2810  O O     . PHE A  1 386 ? 36.069  21.843  176.074 1.00 47.29  ? 386 PHE A O     1 
ATOM   2811  C CB    . PHE A  1 386 ? 35.627  21.446  172.822 1.00 52.15  ? 386 PHE A CB    1 
ATOM   2812  C CG    . PHE A  1 386 ? 35.437  20.515  171.659 1.00 60.22  ? 386 PHE A CG    1 
ATOM   2813  C CD1   . PHE A  1 386 ? 36.178  20.675  170.500 1.00 61.19  ? 386 PHE A CD1   1 
ATOM   2814  C CD2   . PHE A  1 386 ? 34.503  19.492  171.717 1.00 63.75  ? 386 PHE A CD2   1 
ATOM   2815  C CE1   . PHE A  1 386 ? 36.000  19.823  169.425 1.00 67.34  ? 386 PHE A CE1   1 
ATOM   2816  C CE2   . PHE A  1 386 ? 34.323  18.636  170.648 1.00 63.27  ? 386 PHE A CE2   1 
ATOM   2817  C CZ    . PHE A  1 386 ? 35.071  18.802  169.500 1.00 64.00  ? 386 PHE A CZ    1 
ATOM   2818  N N     . ILE A  1 387 ? 37.544  22.920  174.768 1.00 48.25  ? 387 ILE A N     1 
ATOM   2819  C CA    . ILE A  1 387 ? 37.571  24.110  175.604 1.00 43.59  ? 387 ILE A CA    1 
ATOM   2820  C C     . ILE A  1 387 ? 37.510  25.353  174.731 1.00 44.62  ? 387 ILE A C     1 
ATOM   2821  O O     . ILE A  1 387 ? 37.917  25.329  173.568 1.00 45.28  ? 387 ILE A O     1 
ATOM   2822  C CB    . ILE A  1 387 ? 38.828  24.181  176.497 1.00 47.88  ? 387 ILE A CB    1 
ATOM   2823  C CG1   . ILE A  1 387 ? 40.100  24.028  175.663 1.00 48.37  ? 387 ILE A CG1   1 
ATOM   2824  C CG2   . ILE A  1 387 ? 38.769  23.133  177.598 1.00 47.27  ? 387 ILE A CG2   1 
ATOM   2825  C CD1   . ILE A  1 387 ? 41.371  24.193  176.472 1.00 49.35  ? 387 ILE A CD1   1 
ATOM   2826  N N     . ALA A  1 388 ? 36.974  26.431  175.288 1.00 47.19  ? 388 ALA A N     1 
ATOM   2827  C CA    . ALA A  1 388 ? 37.020  27.730  174.636 1.00 41.77  ? 388 ALA A CA    1 
ATOM   2828  C C     . ALA A  1 388 ? 37.473  28.759  175.650 1.00 34.64  ? 388 ALA A C     1 
ATOM   2829  O O     . ALA A  1 388 ? 36.985  28.787  176.780 1.00 40.41  ? 388 ALA A O     1 
ATOM   2830  C CB    . ALA A  1 388 ? 35.671  28.100  174.053 1.00 41.25  ? 388 ALA A CB    1 
ATOM   2831  N N     . LEU A  1 389 ? 38.416  29.600  175.248 1.00 39.46  ? 389 LEU A N     1 
ATOM   2832  C CA    . LEU A  1 389 ? 39.032  30.524  176.183 1.00 36.72  ? 389 LEU A CA    1 
ATOM   2833  C C     . LEU A  1 389 ? 38.975  31.965  175.675 1.00 38.18  ? 389 LEU A C     1 
ATOM   2834  O O     . LEU A  1 389 ? 39.250  32.240  174.506 1.00 40.48  ? 389 LEU A O     1 
ATOM   2835  C CB    . LEU A  1 389 ? 40.480  30.108  176.442 1.00 42.34  ? 389 LEU A CB    1 
ATOM   2836  C CG    . LEU A  1 389 ? 40.779  28.651  176.814 1.00 43.81  ? 389 LEU A CG    1 
ATOM   2837  C CD1   . LEU A  1 389 ? 42.219  28.307  176.479 1.00 49.15  ? 389 LEU A CD1   1 
ATOM   2838  C CD2   . LEU A  1 389 ? 40.523  28.396  178.283 1.00 48.93  ? 389 LEU A CD2   1 
ATOM   2839  N N     . ASN A  1 390 ? 38.611  32.882  176.563 1.00 34.65  ? 390 ASN A N     1 
ATOM   2840  C CA    . ASN A  1 390 ? 38.590  34.297  176.224 1.00 35.94  ? 390 ASN A CA    1 
ATOM   2841  C C     . ASN A  1 390 ? 39.157  35.154  177.344 1.00 33.31  ? 390 ASN A C     1 
ATOM   2842  O O     . ASN A  1 390 ? 38.887  34.921  178.522 1.00 37.62  ? 390 ASN A O     1 
ATOM   2843  C CB    . ASN A  1 390 ? 37.169  34.758  175.894 1.00 33.65  ? 390 ASN A CB    1 
ATOM   2844  C CG    . ASN A  1 390 ? 36.775  34.459  174.458 1.00 43.49  ? 390 ASN A CG    1 
ATOM   2845  O OD1   . ASN A  1 390 ? 37.197  35.148  173.529 1.00 44.66  ? 390 ASN A OD1   1 
ATOM   2846  N ND2   . ASN A  1 390 ? 35.949  33.435  174.271 1.00 37.59  ? 390 ASN A ND2   1 
ATOM   2847  N N     . GLY A  1 391 ? 39.954  36.147  176.971 1.00 29.25  ? 391 GLY A N     1 
ATOM   2848  C CA    . GLY A  1 391 ? 40.461  37.098  177.939 1.00 37.90  ? 391 GLY A CA    1 
ATOM   2849  C C     . GLY A  1 391 ? 39.498  38.258  178.049 1.00 38.68  ? 391 GLY A C     1 
ATOM   2850  O O     . GLY A  1 391 ? 38.874  38.646  177.064 1.00 38.42  ? 391 GLY A O     1 
ATOM   2851  N N     . PHE A  1 392 ? 39.347  38.799  179.250 1.00 37.76  ? 392 PHE A N     1 
ATOM   2852  C CA    . PHE A  1 392 ? 38.589  40.030  179.406 1.00 37.84  ? 392 PHE A CA    1 
ATOM   2853  C C     . PHE A  1 392 ? 39.552  41.206  179.320 1.00 35.42  ? 392 PHE A C     1 
ATOM   2854  O O     . PHE A  1 392 ? 40.339  41.303  178.377 1.00 40.86  ? 392 PHE A O     1 
ATOM   2855  C CB    . PHE A  1 392 ? 37.808  40.051  180.724 1.00 40.20  ? 392 PHE A CB    1 
ATOM   2856  C CG    . PHE A  1 392 ? 36.520  39.267  180.681 1.00 36.54  ? 392 PHE A CG    1 
ATOM   2857  C CD1   . PHE A  1 392 ? 36.286  38.343  179.676 1.00 33.13  ? 392 PHE A CD1   1 
ATOM   2858  C CD2   . PHE A  1 392 ? 35.538  39.470  181.638 1.00 34.64  ? 392 PHE A CD2   1 
ATOM   2859  C CE1   . PHE A  1 392 ? 35.105  37.626  179.631 1.00 43.11  ? 392 PHE A CE1   1 
ATOM   2860  C CE2   . PHE A  1 392 ? 34.351  38.754  181.598 1.00 40.81  ? 392 PHE A CE2   1 
ATOM   2861  C CZ    . PHE A  1 392 ? 34.134  37.832  180.590 1.00 36.70  ? 392 PHE A CZ    1 
ATOM   2862  N N     . GLY A  1 393 ? 39.501  42.096  180.303 1.00 38.56  ? 393 GLY A N     1 
ATOM   2863  C CA    . GLY A  1 393 ? 40.331  43.284  180.258 1.00 37.94  ? 393 GLY A CA    1 
ATOM   2864  C C     . GLY A  1 393 ? 39.784  44.245  179.224 1.00 41.95  ? 393 GLY A C     1 
ATOM   2865  O O     . GLY A  1 393 ? 38.668  44.068  178.735 1.00 36.08  ? 393 GLY A O     1 
ATOM   2866  N N     . GLY A  1 394 ? 40.566  45.258  178.877 1.00 32.45  ? 394 GLY A N     1 
ATOM   2867  C CA    . GLY A  1 394 ? 40.098  46.270  177.952 1.00 34.53  ? 394 GLY A CA    1 
ATOM   2868  C C     . GLY A  1 394 ? 38.918  47.013  178.544 1.00 35.33  ? 394 GLY A C     1 
ATOM   2869  O O     . GLY A  1 394 ? 38.957  47.430  179.702 1.00 38.55  ? 394 GLY A O     1 
ATOM   2870  N N     . GLN A  1 395 ? 37.859  47.167  177.757 1.00 38.36  ? 395 GLN A N     1 
ATOM   2871  C CA    . GLN A  1 395 ? 36.692  47.925  178.197 1.00 41.75  ? 395 GLN A CA    1 
ATOM   2872  C C     . GLN A  1 395 ? 35.857  47.157  179.220 1.00 39.90  ? 395 GLN A C     1 
ATOM   2873  O O     . GLN A  1 395 ? 35.050  47.747  179.937 1.00 43.81  ? 395 GLN A O     1 
ATOM   2874  C CB    . GLN A  1 395 ? 35.819  48.307  177.001 1.00 46.88  ? 395 GLN A CB    1 
ATOM   2875  C CG    . GLN A  1 395 ? 34.888  49.478  177.271 1.00 51.33  ? 395 GLN A CG    1 
ATOM   2876  C CD    . GLN A  1 395 ? 35.640  50.772  177.509 1.00 51.58  ? 395 GLN A CD    1 
ATOM   2877  O OE1   . GLN A  1 395 ? 36.723  50.981  176.962 1.00 52.31  ? 395 GLN A OE1   1 
ATOM   2878  N NE2   . GLN A  1 395 ? 35.071  51.648  178.331 1.00 60.89  ? 395 GLN A NE2   1 
ATOM   2879  N N     . MET A  1 396 ? 36.049  45.842  179.289 1.00 36.63  ? 396 MET A N     1 
ATOM   2880  C CA    . MET A  1 396 ? 35.346  45.036  180.280 1.00 39.03  ? 396 MET A CA    1 
ATOM   2881  C C     . MET A  1 396 ? 35.820  45.405  181.680 1.00 45.40  ? 396 MET A C     1 
ATOM   2882  O O     . MET A  1 396 ? 35.105  45.195  182.651 1.00 42.26  ? 396 MET A O     1 
ATOM   2883  C CB    . MET A  1 396 ? 35.544  43.538  180.027 1.00 25.71  ? 396 MET A CB    1 
ATOM   2884  C CG    . MET A  1 396 ? 34.822  42.999  178.792 1.00 28.75  ? 396 MET A CG    1 
ATOM   2885  S SD    . MET A  1 396 ? 33.019  43.025  178.905 1.00 34.52  ? 396 MET A SD    1 
ATOM   2886  C CE    . MET A  1 396 ? 32.723  41.727  180.103 1.00 28.18  ? 396 MET A CE    1 
ATOM   2887  N N     . SER A  1 397 ? 37.021  45.967  181.781 1.00 36.56  ? 397 SER A N     1 
ATOM   2888  C CA    . SER A  1 397 ? 37.546  46.404  183.072 1.00 37.69  ? 397 SER A CA    1 
ATOM   2889  C C     . SER A  1 397 ? 37.142  47.835  183.414 1.00 40.13  ? 397 SER A C     1 
ATOM   2890  O O     . SER A  1 397 ? 37.277  48.261  184.560 1.00 48.75  ? 397 SER A O     1 
ATOM   2891  C CB    . SER A  1 397 ? 39.073  46.286  183.101 1.00 40.16  ? 397 SER A CB    1 
ATOM   2892  O OG    . SER A  1 397 ? 39.475  44.938  183.239 1.00 40.92  ? 397 SER A OG    1 
ATOM   2893  N N     . LYS A  1 398 ? 36.659  48.577  182.423 1.00 40.44  ? 398 LYS A N     1 
ATOM   2894  C CA    . LYS A  1 398 ? 36.315  49.981  182.622 1.00 41.72  ? 398 LYS A CA    1 
ATOM   2895  C C     . LYS A  1 398 ? 34.822  50.190  182.858 1.00 43.79  ? 398 LYS A C     1 
ATOM   2896  O O     . LYS A  1 398 ? 34.396  51.266  183.277 1.00 41.98  ? 398 LYS A O     1 
ATOM   2897  C CB    . LYS A  1 398 ? 36.775  50.813  181.426 1.00 45.88  ? 398 LYS A CB    1 
ATOM   2898  C CG    . LYS A  1 398 ? 38.285  50.948  181.339 1.00 46.75  ? 398 LYS A CG    1 
ATOM   2899  C CD    . LYS A  1 398 ? 38.717  51.625  180.054 1.00 51.01  ? 398 LYS A CD    1 
ATOM   2900  C CE    . LYS A  1 398 ? 40.228  51.777  180.010 1.00 58.80  ? 398 LYS A CE    1 
ATOM   2901  N NZ    . LYS A  1 398 ? 40.732  51.946  178.620 1.00 73.17  ? 398 LYS A NZ    1 
ATOM   2902  N N     . ILE A  1 399 ? 34.034  49.157  182.588 1.00 42.15  ? 399 ILE A N     1 
ATOM   2903  C CA    . ILE A  1 399 ? 32.604  49.198  182.847 1.00 37.58  ? 399 ILE A CA    1 
ATOM   2904  C C     . ILE A  1 399 ? 32.334  48.784  184.290 1.00 37.23  ? 399 ILE A C     1 
ATOM   2905  O O     . ILE A  1 399 ? 32.800  47.737  184.732 1.00 37.48  ? 399 ILE A O     1 
ATOM   2906  C CB    . ILE A  1 399 ? 31.840  48.280  181.875 1.00 36.19  ? 399 ILE A CB    1 
ATOM   2907  C CG1   . ILE A  1 399 ? 32.030  48.769  180.437 1.00 35.98  ? 399 ILE A CG1   1 
ATOM   2908  C CG2   . ILE A  1 399 ? 30.365  48.229  182.237 1.00 38.01  ? 399 ILE A CG2   1 
ATOM   2909  C CD1   . ILE A  1 399 ? 31.602  47.772  179.384 1.00 35.95  ? 399 ILE A CD1   1 
ATOM   2910  N N     . SER A  1 400 ? 31.603  49.618  185.024 1.00 37.04  ? 400 SER A N     1 
ATOM   2911  C CA    . SER A  1 400 ? 31.289  49.336  186.422 1.00 37.40  ? 400 SER A CA    1 
ATOM   2912  C C     . SER A  1 400 ? 30.526  48.019  186.564 1.00 42.61  ? 400 SER A C     1 
ATOM   2913  O O     . SER A  1 400 ? 29.771  47.628  185.674 1.00 36.01  ? 400 SER A O     1 
ATOM   2914  C CB    . SER A  1 400 ? 30.485  50.486  187.029 1.00 42.79  ? 400 SER A CB    1 
ATOM   2915  O OG    . SER A  1 400 ? 30.129  50.209  188.372 1.00 54.93  ? 400 SER A OG    1 
ATOM   2916  N N     . SER A  1 401 ? 30.726  47.342  187.690 1.00 37.52  ? 401 SER A N     1 
ATOM   2917  C CA    . SER A  1 401 ? 30.157  46.015  187.895 1.00 41.59  ? 401 SER A CA    1 
ATOM   2918  C C     . SER A  1 401 ? 28.633  46.043  188.013 1.00 40.75  ? 401 SER A C     1 
ATOM   2919  O O     . SER A  1 401 ? 27.976  45.014  187.849 1.00 43.59  ? 401 SER A O     1 
ATOM   2920  C CB    . SER A  1 401 ? 30.759  45.367  189.143 1.00 41.25  ? 401 SER A CB    1 
ATOM   2921  O OG    . SER A  1 401 ? 30.361  46.055  190.315 1.00 47.18  ? 401 SER A OG    1 
ATOM   2922  N N     . ASP A  1 402 ? 28.074  47.216  188.291 1.00 38.42  ? 402 ASP A N     1 
ATOM   2923  C CA    . ASP A  1 402 ? 26.631  47.338  188.439 1.00 39.77  ? 402 ASP A CA    1 
ATOM   2924  C C     . ASP A  1 402 ? 26.016  48.213  187.346 1.00 40.36  ? 402 ASP A C     1 
ATOM   2925  O O     . ASP A  1 402 ? 24.860  48.632  187.453 1.00 44.92  ? 402 ASP A O     1 
ATOM   2926  C CB    . ASP A  1 402 ? 26.281  47.898  189.819 1.00 44.13  ? 402 ASP A CB    1 
ATOM   2927  C CG    . ASP A  1 402 ? 26.610  49.370  189.956 1.00 45.31  ? 402 ASP A CG    1 
ATOM   2928  O OD1   . ASP A  1 402 ? 27.567  49.836  189.305 1.00 47.00  ? 402 ASP A OD1   1 
ATOM   2929  O OD2   . ASP A  1 402 ? 25.899  50.064  190.715 1.00 51.20  ? 402 ASP A OD2   1 
ATOM   2930  N N     . PHE A  1 403 ? 26.790  48.488  186.299 1.00 35.23  ? 403 PHE A N     1 
ATOM   2931  C CA    . PHE A  1 403 ? 26.272  49.213  185.140 1.00 37.39  ? 403 PHE A CA    1 
ATOM   2932  C C     . PHE A  1 403 ? 25.093  48.443  184.553 1.00 37.16  ? 403 PHE A C     1 
ATOM   2933  O O     . PHE A  1 403 ? 24.039  49.016  184.273 1.00 35.86  ? 403 PHE A O     1 
ATOM   2934  C CB    . PHE A  1 403 ? 27.363  49.423  184.086 1.00 34.20  ? 403 PHE A CB    1 
ATOM   2935  C CG    . PHE A  1 403 ? 26.859  50.037  182.807 1.00 36.72  ? 403 PHE A CG    1 
ATOM   2936  C CD1   . PHE A  1 403 ? 26.382  51.338  182.786 1.00 37.75  ? 403 PHE A CD1   1 
ATOM   2937  C CD2   . PHE A  1 403 ? 26.864  49.314  181.625 1.00 33.62  ? 403 PHE A CD2   1 
ATOM   2938  C CE1   . PHE A  1 403 ? 25.916  51.905  181.610 1.00 36.90  ? 403 PHE A CE1   1 
ATOM   2939  C CE2   . PHE A  1 403 ? 26.401  49.876  180.446 1.00 33.57  ? 403 PHE A CE2   1 
ATOM   2940  C CZ    . PHE A  1 403 ? 25.925  51.172  180.440 1.00 37.93  ? 403 PHE A CZ    1 
ATOM   2941  N N     . THR A  1 404 ? 25.291  47.141  184.368 1.00 38.16  ? 404 THR A N     1 
ATOM   2942  C CA    . THR A  1 404 ? 24.224  46.208  184.020 1.00 36.95  ? 404 THR A CA    1 
ATOM   2943  C C     . THR A  1 404 ? 24.404  44.989  184.942 1.00 36.48  ? 404 THR A C     1 
ATOM   2944  O O     . THR A  1 404 ? 25.419  44.899  185.630 1.00 37.91  ? 404 THR A O     1 
ATOM   2945  C CB    . THR A  1 404 ? 24.267  45.825  182.517 1.00 37.75  ? 404 THR A CB    1 
ATOM   2946  O OG1   . THR A  1 404 ? 25.531  45.233  182.196 1.00 32.32  ? 404 THR A OG1   1 
ATOM   2947  C CG2   . THR A  1 404 ? 24.046  47.056  181.638 1.00 34.13  ? 404 THR A CG2   1 
ATOM   2948  N N     . PRO A  1 405 ? 23.417  44.072  185.000 1.00 37.27  ? 405 PRO A N     1 
ATOM   2949  C CA    . PRO A  1 405 ? 23.532  42.926  185.918 1.00 33.74  ? 405 PRO A CA    1 
ATOM   2950  C C     . PRO A  1 405 ? 24.809  42.072  185.805 1.00 37.58  ? 405 PRO A C     1 
ATOM   2951  O O     . PRO A  1 405 ? 25.196  41.467  186.804 1.00 39.82  ? 405 PRO A O     1 
ATOM   2952  C CB    . PRO A  1 405 ? 22.307  42.085  185.556 1.00 32.81  ? 405 PRO A CB    1 
ATOM   2953  C CG    . PRO A  1 405 ? 21.290  43.096  185.173 1.00 36.23  ? 405 PRO A CG    1 
ATOM   2954  C CD    . PRO A  1 405 ? 22.053  44.178  184.446 1.00 32.08  ? 405 PRO A CD    1 
ATOM   2955  N N     . PHE A  1 406 ? 25.442  42.016  184.635 1.00 35.55  ? 406 PHE A N     1 
ATOM   2956  C CA    . PHE A  1 406 ? 26.676  41.243  184.484 1.00 36.19  ? 406 PHE A CA    1 
ATOM   2957  C C     . PHE A  1 406 ? 27.787  41.890  185.298 1.00 36.93  ? 406 PHE A C     1 
ATOM   2958  O O     . PHE A  1 406 ? 28.257  42.975  184.959 1.00 38.76  ? 406 PHE A O     1 
ATOM   2959  C CB    . PHE A  1 406 ? 27.085  41.132  183.015 1.00 34.34  ? 406 PHE A CB    1 
ATOM   2960  C CG    . PHE A  1 406 ? 28.266  40.224  182.776 1.00 35.62  ? 406 PHE A CG    1 
ATOM   2961  C CD1   . PHE A  1 406 ? 28.081  38.864  182.580 1.00 36.86  ? 406 PHE A CD1   1 
ATOM   2962  C CD2   . PHE A  1 406 ? 29.556  40.732  182.737 1.00 34.58  ? 406 PHE A CD2   1 
ATOM   2963  C CE1   . PHE A  1 406 ? 29.160  38.026  182.355 1.00 36.89  ? 406 PHE A CE1   1 
ATOM   2964  C CE2   . PHE A  1 406 ? 30.640  39.899  182.513 1.00 33.54  ? 406 PHE A CE2   1 
ATOM   2965  C CZ    . PHE A  1 406 ? 30.439  38.544  182.321 1.00 35.43  ? 406 PHE A CZ    1 
ATOM   2966  N N     . PRO A  1 407 ? 28.214  41.216  186.374 1.00 35.49  ? 407 PRO A N     1 
ATOM   2967  C CA    . PRO A  1 407 ? 29.084  41.801  187.395 1.00 37.41  ? 407 PRO A CA    1 
ATOM   2968  C C     . PRO A  1 407 ? 30.578  41.586  187.162 1.00 37.44  ? 407 PRO A C     1 
ATOM   2969  O O     . PRO A  1 407 ? 31.388  42.207  187.848 1.00 37.55  ? 407 PRO A O     1 
ATOM   2970  C CB    . PRO A  1 407 ? 28.646  41.062  188.654 1.00 39.11  ? 407 PRO A CB    1 
ATOM   2971  C CG    . PRO A  1 407 ? 28.349  39.676  188.141 1.00 36.07  ? 407 PRO A CG    1 
ATOM   2972  C CD    . PRO A  1 407 ? 27.838  39.833  186.717 1.00 37.04  ? 407 PRO A CD    1 
ATOM   2973  N N     . HIS A  1 408 ? 30.937  40.719  186.223 1.00 36.51  ? 408 HIS A N     1 
ATOM   2974  C CA    . HIS A  1 408 ? 32.323  40.289  186.094 1.00 38.01  ? 408 HIS A CA    1 
ATOM   2975  C C     . HIS A  1 408 ? 33.120  41.222  185.196 1.00 32.36  ? 408 HIS A C     1 
ATOM   2976  O O     . HIS A  1 408 ? 33.375  40.930  184.026 1.00 35.49  ? 408 HIS A O     1 
ATOM   2977  C CB    . HIS A  1 408 ? 32.362  38.856  185.586 1.00 37.40  ? 408 HIS A CB    1 
ATOM   2978  C CG    . HIS A  1 408 ? 31.479  37.937  186.368 1.00 35.33  ? 408 HIS A CG    1 
ATOM   2979  N ND1   . HIS A  1 408 ? 30.504  37.159  185.782 1.00 44.59  ? 408 HIS A ND1   1 
ATOM   2980  C CD2   . HIS A  1 408 ? 31.398  37.703  187.699 1.00 33.94  ? 408 HIS A CD2   1 
ATOM   2981  C CE1   . HIS A  1 408 ? 29.873  36.473  186.718 1.00 41.42  ? 408 HIS A CE1   1 
ATOM   2982  N NE2   . HIS A  1 408 ? 30.399  36.781  187.890 1.00 46.66  ? 408 HIS A NE2   1 
ATOM   2983  N N     . ARG A  1 409 ? 33.506  42.353  185.773 1.00 37.38  ? 409 ARG A N     1 
ATOM   2984  C CA    . ARG A  1 409 ? 34.218  43.395  185.056 1.00 38.51  ? 409 ARG A CA    1 
ATOM   2985  C C     . ARG A  1 409 ? 35.669  43.467  185.532 1.00 39.69  ? 409 ARG A C     1 
ATOM   2986  O O     . ARG A  1 409 ? 36.421  42.511  185.355 1.00 41.24  ? 409 ARG A O     1 
ATOM   2987  C CB    . ARG A  1 409 ? 33.506  44.735  185.243 1.00 34.31  ? 409 ARG A CB    1 
ATOM   2988  C CG    . ARG A  1 409 ? 31.998  44.686  184.969 1.00 39.71  ? 409 ARG A CG    1 
ATOM   2989  C CD    . ARG A  1 409 ? 31.675  44.397  183.504 1.00 29.90  ? 409 ARG A CD    1 
ATOM   2990  N NE    . ARG A  1 409 ? 30.241  44.506  183.230 1.00 37.71  ? 409 ARG A NE    1 
ATOM   2991  C CZ    . ARG A  1 409 ? 29.713  44.598  182.013 1.00 35.62  ? 409 ARG A CZ    1 
ATOM   2992  N NH1   . ARG A  1 409 ? 30.498  44.599  180.943 1.00 32.21  ? 409 ARG A NH1   1 
ATOM   2993  N NH2   . ARG A  1 409 ? 28.398  44.695  181.863 1.00 36.80  ? 409 ARG A NH2   1 
ATOM   2994  N N     . SER A  1 410 ? 36.056  44.589  186.139 1.00 43.25  ? 410 SER A N     1 
ATOM   2995  C CA    . SER A  1 410 ? 37.430  44.774  186.613 1.00 44.62  ? 410 SER A CA    1 
ATOM   2996  C C     . SER A  1 410 ? 37.816  43.675  187.598 1.00 46.67  ? 410 SER A C     1 
ATOM   2997  O O     . SER A  1 410 ? 37.038  43.327  188.486 1.00 44.06  ? 410 SER A O     1 
ATOM   2998  C CB    . SER A  1 410 ? 37.601  46.150  187.264 1.00 43.77  ? 410 SER A CB    1 
ATOM   2999  O OG    . SER A  1 410 ? 38.897  46.305  187.819 1.00 53.87  ? 410 SER A OG    1 
ATOM   3000  N N     . GLY A  1 411 ? 39.014  43.125  187.430 1.00 45.90  ? 411 GLY A N     1 
ATOM   3001  C CA    . GLY A  1 411 ? 39.466  42.025  188.261 1.00 42.21  ? 411 GLY A CA    1 
ATOM   3002  C C     . GLY A  1 411 ? 39.239  40.670  187.615 1.00 52.07  ? 411 GLY A C     1 
ATOM   3003  O O     . GLY A  1 411 ? 39.844  39.673  188.011 1.00 56.95  ? 411 GLY A O     1 
ATOM   3004  N N     . THR A  1 412 ? 38.361  40.632  186.618 1.00 48.02  ? 412 THR A N     1 
ATOM   3005  C CA    . THR A  1 412 ? 38.085  39.399  185.891 1.00 44.18  ? 412 THR A CA    1 
ATOM   3006  C C     . THR A  1 412 ? 39.058  39.266  184.728 1.00 39.62  ? 412 THR A C     1 
ATOM   3007  O O     . THR A  1 412 ? 39.173  40.169  183.901 1.00 38.69  ? 412 THR A O     1 
ATOM   3008  C CB    . THR A  1 412 ? 36.634  39.356  185.371 1.00 38.96  ? 412 THR A CB    1 
ATOM   3009  O OG1   . THR A  1 412 ? 35.737  39.709  186.432 1.00 43.70  ? 412 THR A OG1   1 
ATOM   3010  C CG2   . THR A  1 412 ? 36.288  37.967  184.863 1.00 37.85  ? 412 THR A CG2   1 
ATOM   3011  N N     . ARG A  1 413 ? 39.765  38.142  184.676 1.00 43.22  ? 413 ARG A N     1 
ATOM   3012  C CA    . ARG A  1 413 ? 40.812  37.945  183.680 1.00 36.89  ? 413 ARG A CA    1 
ATOM   3013  C C     . ARG A  1 413 ? 40.359  37.110  182.490 1.00 36.24  ? 413 ARG A C     1 
ATOM   3014  O O     . ARG A  1 413 ? 40.493  37.528  181.340 1.00 38.06  ? 413 ARG A O     1 
ATOM   3015  C CB    . ARG A  1 413 ? 42.034  37.282  184.319 1.00 43.75  ? 413 ARG A CB    1 
ATOM   3016  C CG    . ARG A  1 413 ? 42.682  38.081  185.428 1.00 48.66  ? 413 ARG A CG    1 
ATOM   3017  C CD    . ARG A  1 413 ? 43.919  37.368  185.948 1.00 54.51  ? 413 ARG A CD    1 
ATOM   3018  N NE    . ARG A  1 413 ? 44.574  38.103  187.026 1.00 60.70  ? 413 ARG A NE    1 
ATOM   3019  C CZ    . ARG A  1 413 ? 45.598  38.932  186.855 1.00 60.78  ? 413 ARG A CZ    1 
ATOM   3020  N NH1   . ARG A  1 413 ? 46.126  39.553  187.900 1.00 63.19  ? 413 ARG A NH1   1 
ATOM   3021  N NH2   . ARG A  1 413 ? 46.097  39.140  185.644 1.00 54.42  ? 413 ARG A NH2   1 
ATOM   3022  N N     . LEU A  1 414 ? 39.836  35.921  182.768 1.00 36.43  ? 414 LEU A N     1 
ATOM   3023  C CA    . LEU A  1 414 ? 39.512  34.972  181.708 1.00 40.54  ? 414 LEU A CA    1 
ATOM   3024  C C     . LEU A  1 414 ? 38.102  34.411  181.832 1.00 39.29  ? 414 LEU A C     1 
ATOM   3025  O O     . LEU A  1 414 ? 37.544  34.334  182.927 1.00 35.23  ? 414 LEU A O     1 
ATOM   3026  C CB    . LEU A  1 414 ? 40.505  33.807  181.714 1.00 39.51  ? 414 LEU A CB    1 
ATOM   3027  C CG    . LEU A  1 414 ? 42.010  34.095  181.779 1.00 38.74  ? 414 LEU A CG    1 
ATOM   3028  C CD1   . LEU A  1 414 ? 42.782  32.791  181.923 1.00 41.30  ? 414 LEU A CD1   1 
ATOM   3029  C CD2   . LEU A  1 414 ? 42.488  34.865  180.560 1.00 38.29  ? 414 LEU A CD2   1 
ATOM   3030  N N     . MET A  1 415 ? 37.533  34.017  180.698 1.00 36.70  ? 415 MET A N     1 
ATOM   3031  C CA    . MET A  1 415 ? 36.348  33.173  180.696 1.00 39.68  ? 415 MET A CA    1 
ATOM   3032  C C     . MET A  1 415 ? 36.732  31.840  180.076 1.00 38.96  ? 415 MET A C     1 
ATOM   3033  O O     . MET A  1 415 ? 37.195  31.787  178.937 1.00 40.64  ? 415 MET A O     1 
ATOM   3034  C CB    . MET A  1 415 ? 35.186  33.814  179.929 1.00 33.72  ? 415 MET A CB    1 
ATOM   3035  C CG    . MET A  1 415 ? 33.906  32.981  179.988 1.00 42.27  ? 415 MET A CG    1 
ATOM   3036  S SD    . MET A  1 415 ? 32.393  33.851  179.532 1.00 41.75  ? 415 MET A SD    1 
ATOM   3037  C CE    . MET A  1 415 ? 32.672  34.096  177.782 1.00 43.86  ? 415 MET A CE    1 
ATOM   3038  N N     . VAL A  1 416 ? 36.557  30.765  180.836 1.00 37.05  ? 416 VAL A N     1 
ATOM   3039  C CA    . VAL A  1 416 ? 36.952  29.438  180.381 1.00 37.95  ? 416 VAL A CA    1 
ATOM   3040  C C     . VAL A  1 416 ? 35.747  28.515  180.232 1.00 40.04  ? 416 VAL A C     1 
ATOM   3041  O O     . VAL A  1 416 ? 35.074  28.202  181.211 1.00 36.32  ? 416 VAL A O     1 
ATOM   3042  C CB    . VAL A  1 416 ? 37.959  28.797  181.349 1.00 37.96  ? 416 VAL A CB    1 
ATOM   3043  C CG1   . VAL A  1 416 ? 38.346  27.414  180.869 1.00 41.65  ? 416 VAL A CG1   1 
ATOM   3044  C CG2   . VAL A  1 416 ? 39.189  29.681  181.495 1.00 37.69  ? 416 VAL A CG2   1 
ATOM   3045  N N     . GLU A  1 417 ? 35.481  28.075  179.006 1.00 38.48  ? 417 GLU A N     1 
ATOM   3046  C CA    . GLU A  1 417 ? 34.331  27.217  178.744 1.00 39.68  ? 417 GLU A CA    1 
ATOM   3047  C C     . GLU A  1 417 ? 34.755  25.763  178.570 1.00 44.56  ? 417 GLU A C     1 
ATOM   3048  O O     . GLU A  1 417 ? 35.673  25.468  177.808 1.00 40.40  ? 417 GLU A O     1 
ATOM   3049  C CB    . GLU A  1 417 ? 33.582  27.699  177.499 1.00 43.48  ? 417 GLU A CB    1 
ATOM   3050  C CG    . GLU A  1 417 ? 33.228  29.179  177.528 1.00 49.70  ? 417 GLU A CG    1 
ATOM   3051  C CD    . GLU A  1 417 ? 32.718  29.686  176.191 1.00 50.17  ? 417 GLU A CD    1 
ATOM   3052  O OE1   . GLU A  1 417 ? 31.785  29.069  175.634 1.00 46.11  ? 417 GLU A OE1   1 
ATOM   3053  O OE2   . GLU A  1 417 ? 33.255  30.696  175.691 1.00 44.15  ? 417 GLU A OE2   1 
ATOM   3054  N N     . TYR A  1 418 ? 34.093  24.857  179.284 1.00 43.98  ? 418 TYR A N     1 
ATOM   3055  C CA    . TYR A  1 418 ? 34.344  23.430  179.113 1.00 44.87  ? 418 TYR A CA    1 
ATOM   3056  C C     . TYR A  1 418 ? 33.141  22.770  178.454 1.00 45.05  ? 418 TYR A C     1 
ATOM   3057  O O     . TYR A  1 418 ? 32.035  22.810  178.986 1.00 47.04  ? 418 TYR A O     1 
ATOM   3058  C CB    . TYR A  1 418 ? 34.639  22.750  180.450 1.00 43.34  ? 418 TYR A CB    1 
ATOM   3059  C CG    . TYR A  1 418 ? 35.427  23.590  181.424 1.00 42.83  ? 418 TYR A CG    1 
ATOM   3060  C CD1   . TYR A  1 418 ? 36.812  23.654  181.359 1.00 44.33  ? 418 TYR A CD1   1 
ATOM   3061  C CD2   . TYR A  1 418 ? 34.783  24.310  182.421 1.00 42.54  ? 418 TYR A CD2   1 
ATOM   3062  C CE1   . TYR A  1 418 ? 37.533  24.418  182.257 1.00 44.11  ? 418 TYR A CE1   1 
ATOM   3063  C CE2   . TYR A  1 418 ? 35.493  25.077  183.322 1.00 45.18  ? 418 TYR A CE2   1 
ATOM   3064  C CZ    . TYR A  1 418 ? 36.869  25.130  183.236 1.00 42.79  ? 418 TYR A CZ    1 
ATOM   3065  O OH    . TYR A  1 418 ? 37.574  25.896  184.136 1.00 45.49  ? 418 TYR A OH    1 
ATOM   3066  N N     . ILE A  1 419 ? 33.362  22.162  177.295 1.00 48.20  ? 419 ILE A N     1 
ATOM   3067  C CA    . ILE A  1 419 ? 32.273  21.584  176.520 1.00 47.26  ? 419 ILE A CA    1 
ATOM   3068  C C     . ILE A  1 419 ? 32.545  20.124  176.167 1.00 54.17  ? 419 ILE A C     1 
ATOM   3069  O O     . ILE A  1 419 ? 33.673  19.759  175.835 1.00 48.69  ? 419 ILE A O     1 
ATOM   3070  C CB    . ILE A  1 419 ? 32.037  22.377  175.222 1.00 45.54  ? 419 ILE A CB    1 
ATOM   3071  C CG1   . ILE A  1 419 ? 31.886  23.871  175.527 1.00 53.09  ? 419 ILE A CG1   1 
ATOM   3072  C CG2   . ILE A  1 419 ? 30.814  21.854  174.489 1.00 50.07  ? 419 ILE A CG2   1 
ATOM   3073  C CD1   . ILE A  1 419 ? 32.643  24.773  174.576 1.00 48.89  ? 419 ILE A CD1   1 
ATOM   3074  N N     . VAL A  1 420 ? 31.515  19.286  176.261 1.00 53.38  ? 420 VAL A N     1 
ATOM   3075  C CA    . VAL A  1 420 ? 31.579  17.945  175.689 1.00 54.77  ? 420 VAL A CA    1 
ATOM   3076  C C     . VAL A  1 420 ? 30.342  17.728  174.812 1.00 53.04  ? 420 VAL A C     1 
ATOM   3077  O O     . VAL A  1 420 ? 29.217  17.995  175.229 1.00 55.25  ? 420 VAL A O     1 
ATOM   3078  C CB    . VAL A  1 420 ? 31.696  16.843  176.780 1.00 53.80  ? 420 VAL A CB    1 
ATOM   3079  C CG1   . VAL A  1 420 ? 30.465  16.803  177.682 1.00 52.80  ? 420 VAL A CG1   1 
ATOM   3080  C CG2   . VAL A  1 420 ? 31.950  15.485  176.139 1.00 59.92  ? 420 VAL A CG2   1 
ATOM   3081  N N     . ALA A  1 421 ? 30.563  17.281  173.579 1.00 53.53  ? 421 ALA A N     1 
ATOM   3082  C CA    . ALA A  1 421 ? 29.483  17.134  172.607 1.00 53.64  ? 421 ALA A CA    1 
ATOM   3083  C C     . ALA A  1 421 ? 29.567  15.793  171.890 1.00 60.34  ? 421 ALA A C     1 
ATOM   3084  O O     . ALA A  1 421 ? 30.659  15.287  171.639 1.00 60.95  ? 421 ALA A O     1 
ATOM   3085  C CB    . ALA A  1 421 ? 29.519  18.270  171.601 1.00 53.93  ? 421 ALA A CB    1 
ATOM   3086  N N     . TRP A  1 422 ? 28.415  15.223  171.547 1.00 60.50  ? 422 TRP A N     1 
ATOM   3087  C CA    . TRP A  1 422 ? 28.390  13.893  170.947 1.00 65.00  ? 422 TRP A CA    1 
ATOM   3088  C C     . TRP A  1 422 ? 27.209  13.695  170.000 1.00 68.22  ? 422 TRP A C     1 
ATOM   3089  O O     . TRP A  1 422 ? 26.128  14.237  170.225 1.00 63.88  ? 422 TRP A O     1 
ATOM   3090  C CB    . TRP A  1 422 ? 28.363  12.828  172.041 1.00 63.64  ? 422 TRP A CB    1 
ATOM   3091  C CG    . TRP A  1 422 ? 27.099  12.806  172.847 1.00 63.65  ? 422 TRP A CG    1 
ATOM   3092  C CD1   . TRP A  1 422 ? 26.004  12.024  172.625 1.00 66.87  ? 422 TRP A CD1   1 
ATOM   3093  C CD2   . TRP A  1 422 ? 26.800  13.594  174.008 1.00 58.75  ? 422 TRP A CD2   1 
ATOM   3094  N NE1   . TRP A  1 422 ? 25.042  12.276  173.572 1.00 61.51  ? 422 TRP A NE1   1 
ATOM   3095  C CE2   . TRP A  1 422 ? 25.505  13.236  174.432 1.00 56.43  ? 422 TRP A CE2   1 
ATOM   3096  C CE3   . TRP A  1 422 ? 27.500  14.568  174.727 1.00 55.80  ? 422 TRP A CE3   1 
ATOM   3097  C CZ2   . TRP A  1 422 ? 24.897  13.815  175.543 1.00 53.74  ? 422 TRP A CZ2   1 
ATOM   3098  C CZ3   . TRP A  1 422 ? 26.893  15.143  175.831 1.00 55.21  ? 422 TRP A CZ3   1 
ATOM   3099  C CH2   . TRP A  1 422 ? 25.605  14.764  176.227 1.00 54.89  ? 422 TRP A CH2   1 
ATOM   3100  N N     . ASN A  1 423 ? 27.416  12.912  168.945 1.00 70.50  ? 423 ASN A N     1 
ATOM   3101  C CA    . ASN A  1 423 ? 26.358  12.680  167.971 1.00 73.01  ? 423 ASN A CA    1 
ATOM   3102  C C     . ASN A  1 423 ? 25.465  11.505  168.360 1.00 74.15  ? 423 ASN A C     1 
ATOM   3103  O O     . ASN A  1 423 ? 25.593  10.943  169.446 1.00 69.88  ? 423 ASN A O     1 
ATOM   3104  C CB    . ASN A  1 423 ? 26.944  12.462  166.568 1.00 75.75  ? 423 ASN A CB    1 
ATOM   3105  C CG    . ASN A  1 423 ? 27.895  11.274  166.493 1.00 83.18  ? 423 ASN A CG    1 
ATOM   3106  O OD1   . ASN A  1 423 ? 27.734  10.281  167.198 1.00 83.28  ? 423 ASN A OD1   1 
ATOM   3107  N ND2   . ASN A  1 423 ? 28.897  11.377  165.624 1.00 90.35  ? 423 ASN A ND2   1 
ATOM   3108  N N     . GLN A  1 424 ? 24.575  11.130  167.448 1.00 80.08  ? 424 GLN A N     1 
ATOM   3109  C CA    . GLN A  1 424 ? 23.565  10.115  167.721 1.00 85.35  ? 424 GLN A CA    1 
ATOM   3110  C C     . GLN A  1 424 ? 24.124  8.694   167.762 1.00 82.02  ? 424 GLN A C     1 
ATOM   3111  O O     . GLN A  1 424 ? 23.395  7.748   168.056 1.00 85.40  ? 424 GLN A O     1 
ATOM   3112  C CB    . GLN A  1 424 ? 22.455  10.204  166.679 1.00 86.62  ? 424 GLN A CB    1 
ATOM   3113  C CG    . GLN A  1 424 ? 21.762  11.552  166.651 1.00 100.16 ? 424 GLN A CG    1 
ATOM   3114  C CD    . GLN A  1 424 ? 20.930  11.746  165.404 1.00 105.90 ? 424 GLN A CD    1 
ATOM   3115  O OE1   . GLN A  1 424 ? 21.286  11.267  164.327 1.00 110.09 ? 424 GLN A OE1   1 
ATOM   3116  N NE2   . GLN A  1 424 ? 19.812  12.450  165.541 1.00 98.69  ? 424 GLN A NE2   1 
ATOM   3117  N N     . SER A  1 425 ? 25.410  8.545   167.463 1.00 80.57  ? 425 SER A N     1 
ATOM   3118  C CA    . SER A  1 425 ? 26.055  7.238   167.517 1.00 81.00  ? 425 SER A CA    1 
ATOM   3119  C C     . SER A  1 425 ? 26.510  6.922   168.938 1.00 81.22  ? 425 SER A C     1 
ATOM   3120  O O     . SER A  1 425 ? 26.448  5.776   169.383 1.00 78.79  ? 425 SER A O     1 
ATOM   3121  C CB    . SER A  1 425 ? 27.250  7.187   166.566 1.00 81.16  ? 425 SER A CB    1 
ATOM   3122  O OG    . SER A  1 425 ? 26.990  7.888   165.362 1.00 77.25  ? 425 SER A OG    1 
ATOM   3123  N N     . GLU A  1 426 ? 26.958  7.953   169.645 1.00 77.95  ? 426 GLU A N     1 
ATOM   3124  C CA    . GLU A  1 426 ? 27.625  7.780   170.929 1.00 74.64  ? 426 GLU A CA    1 
ATOM   3125  C C     . GLU A  1 426 ? 26.670  7.934   172.110 1.00 73.81  ? 426 GLU A C     1 
ATOM   3126  O O     . GLU A  1 426 ? 27.106  8.088   173.250 1.00 73.49  ? 426 GLU A O     1 
ATOM   3127  C CB    . GLU A  1 426 ? 28.766  8.789   171.052 1.00 72.59  ? 426 GLU A CB    1 
ATOM   3128  C CG    . GLU A  1 426 ? 29.389  9.166   169.716 1.00 77.46  ? 426 GLU A CG    1 
ATOM   3129  C CD    . GLU A  1 426 ? 30.363  10.321  169.828 1.00 80.18  ? 426 GLU A CD    1 
ATOM   3130  O OE1   . GLU A  1 426 ? 30.886  10.550  170.937 1.00 78.08  ? 426 GLU A OE1   1 
ATOM   3131  O OE2   . GLU A  1 426 ? 30.603  11.003  168.809 1.00 80.10  ? 426 GLU A OE2   1 
ATOM   3132  N N     . GLN A  1 427 ? 25.372  7.877   171.820 1.00 76.21  ? 427 GLN A N     1 
ATOM   3133  C CA    . GLN A  1 427 ? 24.315  8.167   172.793 1.00 77.76  ? 427 GLN A CA    1 
ATOM   3134  C C     . GLN A  1 427 ? 24.474  7.460   174.145 1.00 79.74  ? 427 GLN A C     1 
ATOM   3135  O O     . GLN A  1 427 ? 24.248  8.069   175.194 1.00 75.86  ? 427 GLN A O     1 
ATOM   3136  C CB    . GLN A  1 427 ? 22.950  7.817   172.194 1.00 84.29  ? 427 GLN A CB    1 
ATOM   3137  C CG    . GLN A  1 427 ? 21.777  8.044   173.139 1.00 91.51  ? 427 GLN A CG    1 
ATOM   3138  C CD    . GLN A  1 427 ? 20.443  7.665   172.524 1.00 99.16  ? 427 GLN A CD    1 
ATOM   3139  O OE1   . GLN A  1 427 ? 20.377  7.224   171.377 1.00 110.97 ? 427 GLN A OE1   1 
ATOM   3140  N NE2   . GLN A  1 427 ? 19.370  7.831   173.289 1.00 101.35 ? 427 GLN A NE2   1 
ATOM   3141  N N     . LYS A  1 428 ? 24.860  6.188   174.123 1.00 81.48  ? 428 LYS A N     1 
ATOM   3142  C CA    . LYS A  1 428 ? 25.002  5.407   175.353 1.00 81.75  ? 428 LYS A CA    1 
ATOM   3143  C C     . LYS A  1 428 ? 26.157  5.890   176.229 1.00 79.98  ? 428 LYS A C     1 
ATOM   3144  O O     . LYS A  1 428 ? 26.163  5.663   177.439 1.00 76.64  ? 428 LYS A O     1 
ATOM   3145  C CB    . LYS A  1 428 ? 25.197  3.925   175.024 1.00 87.13  ? 428 LYS A CB    1 
ATOM   3146  C CG    . LYS A  1 428 ? 23.965  3.235   174.459 1.00 94.36  ? 428 LYS A CG    1 
ATOM   3147  C CD    . LYS A  1 428 ? 22.850  3.160   175.490 1.00 96.61  ? 428 LYS A CD    1 
ATOM   3148  C CE    . LYS A  1 428 ? 21.553  2.689   174.857 1.00 101.46 ? 428 LYS A CE    1 
ATOM   3149  N NZ    . LYS A  1 428 ? 21.679  1.309   174.315 1.00 102.24 ? 428 LYS A NZ    1 
ATOM   3150  N N     . LYS A  1 429 ? 27.133  6.555   175.615 1.00 80.37  ? 429 LYS A N     1 
ATOM   3151  C CA    . LYS A  1 429 ? 28.282  7.091   176.344 1.00 77.81  ? 429 LYS A CA    1 
ATOM   3152  C C     . LYS A  1 429 ? 27.976  8.399   177.078 1.00 75.17  ? 429 LYS A C     1 
ATOM   3153  O O     . LYS A  1 429 ? 28.894  9.065   177.557 1.00 74.75  ? 429 LYS A O     1 
ATOM   3154  C CB    . LYS A  1 429 ? 29.462  7.325   175.392 1.00 77.82  ? 429 LYS A CB    1 
ATOM   3155  C CG    . LYS A  1 429 ? 30.235  6.088   174.981 1.00 78.27  ? 429 LYS A CG    1 
ATOM   3156  C CD    . LYS A  1 429 ? 31.494  6.493   174.222 1.00 82.19  ? 429 LYS A CD    1 
ATOM   3157  C CE    . LYS A  1 429 ? 31.376  6.227   172.728 1.00 82.95  ? 429 LYS A CE    1 
ATOM   3158  N NZ    . LYS A  1 429 ? 32.322  7.075   171.942 1.00 81.11  ? 429 LYS A NZ    1 
ATOM   3159  N N     . LYS A  1 430 ? 26.700  8.768   177.155 1.00 72.16  ? 430 LYS A N     1 
ATOM   3160  C CA    . LYS A  1 430 ? 26.294  10.035  177.768 1.00 70.71  ? 430 LYS A CA    1 
ATOM   3161  C C     . LYS A  1 430 ? 26.851  10.223  179.188 1.00 72.29  ? 430 LYS A C     1 
ATOM   3162  O O     . LYS A  1 430 ? 27.607  11.165  179.439 1.00 70.96  ? 430 LYS A O     1 
ATOM   3163  C CB    . LYS A  1 430 ? 24.766  10.149  177.790 1.00 70.62  ? 430 LYS A CB    1 
ATOM   3164  C CG    . LYS A  1 430 ? 24.245  11.220  178.736 1.00 66.36  ? 430 LYS A CG    1 
ATOM   3165  C CD    . LYS A  1 430 ? 22.731  11.268  178.733 1.00 68.20  ? 430 LYS A CD    1 
ATOM   3166  C CE    . LYS A  1 430 ? 22.202  11.860  180.026 1.00 61.67  ? 430 LYS A CE    1 
ATOM   3167  N NZ    . LYS A  1 430 ? 20.722  12.006  179.995 1.00 76.87  ? 430 LYS A NZ    1 
ATOM   3168  N N     . THR A  1 431 ? 26.492  9.315   180.099 1.00 71.68  ? 431 THR A N     1 
ATOM   3169  C CA    . THR A  1 431 ? 26.911  9.384   181.505 1.00 73.20  ? 431 THR A CA    1 
ATOM   3170  C C     . THR A  1 431 ? 28.432  9.376   181.678 1.00 73.32  ? 431 THR A C     1 
ATOM   3171  O O     . THR A  1 431 ? 28.956  9.849   182.687 1.00 72.22  ? 431 THR A O     1 
ATOM   3172  C CB    . THR A  1 431 ? 26.312  8.217   182.324 1.00 71.02  ? 431 THR A CB    1 
ATOM   3173  O OG1   . THR A  1 431 ? 26.946  6.987   181.956 1.00 81.48  ? 431 THR A OG1   1 
ATOM   3174  C CG2   . THR A  1 431 ? 24.819  8.103   182.080 1.00 73.83  ? 431 THR A CG2   1 
ATOM   3175  N N     . GLU A  1 432 ? 29.125  8.822   180.690 1.00 72.57  ? 432 GLU A N     1 
ATOM   3176  C CA    . GLU A  1 432 ? 30.577  8.898   180.602 1.00 72.65  ? 432 GLU A CA    1 
ATOM   3177  C C     . GLU A  1 432 ? 31.014  10.345  180.354 1.00 71.23  ? 432 GLU A C     1 
ATOM   3178  O O     . GLU A  1 432 ? 31.768  10.921  181.141 1.00 70.28  ? 432 GLU A O     1 
ATOM   3179  C CB    . GLU A  1 432 ? 31.073  7.974   179.483 1.00 75.08  ? 432 GLU A CB    1 
ATOM   3180  C CG    . GLU A  1 432 ? 32.533  7.562   179.535 1.00 83.40  ? 432 GLU A CG    1 
ATOM   3181  C CD    . GLU A  1 432 ? 32.862  6.536   178.463 1.00 81.94  ? 432 GLU A CD    1 
ATOM   3182  O OE1   . GLU A  1 432 ? 32.481  5.359   178.627 1.00 83.90  ? 432 GLU A OE1   1 
ATOM   3183  O OE2   . GLU A  1 432 ? 33.484  6.912   177.448 1.00 83.48  ? 432 GLU A OE2   1 
ATOM   3184  N N     . PHE A  1 433 ? 30.521  10.920  179.258 1.00 70.46  ? 433 PHE A N     1 
ATOM   3185  C CA    . PHE A  1 433 ? 30.815  12.302  178.872 1.00 66.14  ? 433 PHE A CA    1 
ATOM   3186  C C     . PHE A  1 433 ? 30.557  13.299  179.999 1.00 60.92  ? 433 PHE A C     1 
ATOM   3187  O O     . PHE A  1 433 ? 31.346  14.217  180.226 1.00 60.52  ? 433 PHE A O     1 
ATOM   3188  C CB    . PHE A  1 433 ? 29.977  12.702  177.655 1.00 63.78  ? 433 PHE A CB    1 
ATOM   3189  C CG    . PHE A  1 433 ? 30.295  11.922  176.412 1.00 64.77  ? 433 PHE A CG    1 
ATOM   3190  C CD1   . PHE A  1 433 ? 31.607  11.641  176.070 1.00 66.70  ? 433 PHE A CD1   1 
ATOM   3191  C CD2   . PHE A  1 433 ? 29.280  11.467  175.586 1.00 65.53  ? 433 PHE A CD2   1 
ATOM   3192  C CE1   . PHE A  1 433 ? 31.900  10.925  174.926 1.00 65.12  ? 433 PHE A CE1   1 
ATOM   3193  C CE2   . PHE A  1 433 ? 29.567  10.747  174.445 1.00 68.72  ? 433 PHE A CE2   1 
ATOM   3194  C CZ    . PHE A  1 433 ? 30.879  10.478  174.113 1.00 68.72  ? 433 PHE A CZ    1 
ATOM   3195  N N     . LEU A  1 434 ? 29.444  13.106  180.698 1.00 59.36  ? 434 LEU A N     1 
ATOM   3196  C CA    . LEU A  1 434 ? 29.038  13.997  181.778 1.00 62.16  ? 434 LEU A CA    1 
ATOM   3197  C C     . LEU A  1 434 ? 29.969  13.870  182.983 1.00 61.40  ? 434 LEU A C     1 
ATOM   3198  O O     . LEU A  1 434 ? 30.283  14.861  183.646 1.00 59.30  ? 434 LEU A O     1 
ATOM   3199  C CB    . LEU A  1 434 ? 27.595  13.703  182.195 1.00 59.80  ? 434 LEU A CB    1 
ATOM   3200  C CG    . LEU A  1 434 ? 26.461  14.427  181.459 1.00 60.32  ? 434 LEU A CG    1 
ATOM   3201  C CD1   . LEU A  1 434 ? 26.495  14.196  179.951 1.00 59.36  ? 434 LEU A CD1   1 
ATOM   3202  C CD2   . LEU A  1 434 ? 25.106  14.023  182.035 1.00 57.04  ? 434 LEU A CD2   1 
ATOM   3203  N N     . ASP A  1 435 ? 30.402  12.643  183.256 1.00 69.47  ? 435 ASP A N     1 
ATOM   3204  C CA    . ASP A  1 435 ? 31.350  12.374  184.330 1.00 67.23  ? 435 ASP A CA    1 
ATOM   3205  C C     . ASP A  1 435 ? 32.693  13.041  184.055 1.00 62.72  ? 435 ASP A C     1 
ATOM   3206  O O     . ASP A  1 435 ? 33.350  13.532  184.973 1.00 65.93  ? 435 ASP A O     1 
ATOM   3207  C CB    . ASP A  1 435 ? 31.539  10.866  184.512 1.00 75.40  ? 435 ASP A CB    1 
ATOM   3208  C CG    . ASP A  1 435 ? 32.401  10.528  185.711 1.00 87.67  ? 435 ASP A CG    1 
ATOM   3209  O OD1   . ASP A  1 435 ? 32.098  11.018  186.820 1.00 90.75  ? 435 ASP A OD1   1 
ATOM   3210  O OD2   . ASP A  1 435 ? 33.385  9.777   185.544 1.00 90.01  ? 435 ASP A OD2   1 
ATOM   3211  N N     . TRP A  1 436 ? 33.096  13.047  182.788 1.00 57.73  ? 436 TRP A N     1 
ATOM   3212  C CA    . TRP A  1 436 ? 34.327  13.714  182.379 1.00 61.15  ? 436 TRP A CA    1 
ATOM   3213  C C     . TRP A  1 436 ? 34.261  15.205  182.678 1.00 60.55  ? 436 TRP A C     1 
ATOM   3214  O O     . TRP A  1 436 ? 35.152  15.763  183.318 1.00 54.40  ? 436 TRP A O     1 
ATOM   3215  C CB    . TRP A  1 436 ? 34.598  13.504  180.886 1.00 59.96  ? 436 TRP A CB    1 
ATOM   3216  C CG    . TRP A  1 436 ? 35.805  14.256  180.395 1.00 64.98  ? 436 TRP A CG    1 
ATOM   3217  C CD1   . TRP A  1 436 ? 37.112  13.890  180.543 1.00 59.79  ? 436 TRP A CD1   1 
ATOM   3218  C CD2   . TRP A  1 436 ? 35.818  15.505  179.688 1.00 66.45  ? 436 TRP A CD2   1 
ATOM   3219  N NE1   . TRP A  1 436 ? 37.935  14.828  179.971 1.00 66.70  ? 436 TRP A NE1   1 
ATOM   3220  C CE2   . TRP A  1 436 ? 37.167  15.830  179.438 1.00 67.82  ? 436 TRP A CE2   1 
ATOM   3221  C CE3   . TRP A  1 436 ? 34.821  16.378  179.239 1.00 63.18  ? 436 TRP A CE3   1 
ATOM   3222  C CZ2   . TRP A  1 436 ? 37.544  16.991  178.762 1.00 65.46  ? 436 TRP A CZ2   1 
ATOM   3223  C CZ3   . TRP A  1 436 ? 35.199  17.531  178.566 1.00 60.00  ? 436 TRP A CZ3   1 
ATOM   3224  C CH2   . TRP A  1 436 ? 36.548  17.825  178.336 1.00 61.04  ? 436 TRP A CH2   1 
ATOM   3225  N N     . LEU A  1 437 ? 33.190  15.836  182.208 1.00 59.84  ? 437 LEU A N     1 
ATOM   3226  C CA    . LEU A  1 437 ? 32.997  17.269  182.369 1.00 54.68  ? 437 LEU A CA    1 
ATOM   3227  C C     . LEU A  1 437 ? 32.977  17.658  183.838 1.00 53.67  ? 437 LEU A C     1 
ATOM   3228  O O     . LEU A  1 437 ? 33.580  18.657  184.235 1.00 54.95  ? 437 LEU A O     1 
ATOM   3229  C CB    . LEU A  1 437 ? 31.699  17.706  181.691 1.00 54.47  ? 437 LEU A CB    1 
ATOM   3230  C CG    . LEU A  1 437 ? 31.481  19.211  181.560 1.00 52.82  ? 437 LEU A CG    1 
ATOM   3231  C CD1   . LEU A  1 437 ? 32.534  19.813  180.653 1.00 50.01  ? 437 LEU A CD1   1 
ATOM   3232  C CD2   . LEU A  1 437 ? 30.096  19.480  181.021 1.00 47.14  ? 437 LEU A CD2   1 
ATOM   3233  N N     . GLU A  1 438 ? 32.290  16.855  184.644 1.00 53.40  ? 438 GLU A N     1 
ATOM   3234  C CA    . GLU A  1 438 ? 32.190  17.111  186.075 1.00 57.33  ? 438 GLU A CA    1 
ATOM   3235  C C     . GLU A  1 438 ? 33.558  17.048  186.752 1.00 61.82  ? 438 GLU A C     1 
ATOM   3236  O O     . GLU A  1 438 ? 33.819  17.779  187.707 1.00 58.47  ? 438 GLU A O     1 
ATOM   3237  C CB    . GLU A  1 438 ? 31.235  16.112  186.735 1.00 55.92  ? 438 GLU A CB    1 
ATOM   3238  C CG    . GLU A  1 438 ? 30.972  16.395  188.207 1.00 62.25  ? 438 GLU A CG    1 
ATOM   3239  C CD    . GLU A  1 438 ? 30.101  15.345  188.876 1.00 75.15  ? 438 GLU A CD    1 
ATOM   3240  O OE1   . GLU A  1 438 ? 29.520  14.500  188.164 1.00 73.79  ? 438 GLU A OE1   1 
ATOM   3241  O OE2   . GLU A  1 438 ? 30.000  15.366  190.120 1.00 82.20  ? 438 GLU A OE2   1 
ATOM   3242  N N     . LYS A  1 439 ? 34.431  16.180  186.252 1.00 59.93  ? 439 LYS A N     1 
ATOM   3243  C CA    . LYS A  1 439 ? 35.751  16.011  186.848 1.00 63.87  ? 439 LYS A CA    1 
ATOM   3244  C C     . LYS A  1 439 ? 36.725  17.084  186.369 1.00 61.74  ? 439 LYS A C     1 
ATOM   3245  O O     . LYS A  1 439 ? 37.608  17.505  187.116 1.00 61.00  ? 439 LYS A O     1 
ATOM   3246  C CB    . LYS A  1 439 ? 36.300  14.616  186.543 1.00 72.12  ? 439 LYS A CB    1 
ATOM   3247  C CG    . LYS A  1 439 ? 35.586  13.512  187.312 1.00 88.73  ? 439 LYS A CG    1 
ATOM   3248  C CD    . LYS A  1 439 ? 36.352  12.204  187.247 1.00 113.97 ? 439 LYS A CD    1 
ATOM   3249  C CE    . LYS A  1 439 ? 36.057  11.445  185.965 1.00 85.14  ? 439 LYS A CE    1 
ATOM   3250  N NZ    . LYS A  1 439 ? 37.275  10.783  185.426 1.00 81.88  ? 439 LYS A NZ    1 
ATOM   3251  N N     . VAL A  1 440 ? 36.561  17.517  185.123 1.00 59.32  ? 440 VAL A N     1 
ATOM   3252  C CA    . VAL A  1 440 ? 37.295  18.664  184.602 1.00 57.69  ? 440 VAL A CA    1 
ATOM   3253  C C     . VAL A  1 440 ? 37.002  19.886  185.463 1.00 54.58  ? 440 VAL A C     1 
ATOM   3254  O O     . VAL A  1 440 ? 37.906  20.631  185.848 1.00 56.67  ? 440 VAL A O     1 
ATOM   3255  C CB    . VAL A  1 440 ? 36.914  18.963  183.137 1.00 54.24  ? 440 VAL A CB    1 
ATOM   3256  C CG1   . VAL A  1 440 ? 37.432  20.329  182.714 1.00 53.37  ? 440 VAL A CG1   1 
ATOM   3257  C CG2   . VAL A  1 440 ? 37.435  17.874  182.220 1.00 56.57  ? 440 VAL A CG2   1 
ATOM   3258  N N     . TYR A  1 441 ? 35.722  20.062  185.771 1.00 58.03  ? 441 TYR A N     1 
ATOM   3259  C CA    . TYR A  1 441 ? 35.240  21.172  186.581 1.00 56.44  ? 441 TYR A CA    1 
ATOM   3260  C C     . TYR A  1 441 ? 35.750  21.085  188.016 1.00 56.64  ? 441 TYR A C     1 
ATOM   3261  O O     . TYR A  1 441 ? 36.071  22.100  188.632 1.00 57.23  ? 441 TYR A O     1 
ATOM   3262  C CB    . TYR A  1 441 ? 33.710  21.197  186.562 1.00 48.53  ? 441 TYR A CB    1 
ATOM   3263  C CG    . TYR A  1 441 ? 33.096  22.482  187.061 1.00 48.07  ? 441 TYR A CG    1 
ATOM   3264  C CD1   . TYR A  1 441 ? 33.143  23.638  186.293 1.00 44.92  ? 441 TYR A CD1   1 
ATOM   3265  C CD2   . TYR A  1 441 ? 32.451  22.536  188.289 1.00 50.28  ? 441 TYR A CD2   1 
ATOM   3266  C CE1   . TYR A  1 441 ? 32.576  24.816  186.739 1.00 47.94  ? 441 TYR A CE1   1 
ATOM   3267  C CE2   . TYR A  1 441 ? 31.878  23.709  188.744 1.00 50.73  ? 441 TYR A CE2   1 
ATOM   3268  C CZ    . TYR A  1 441 ? 31.944  24.846  187.964 1.00 51.14  ? 441 TYR A CZ    1 
ATOM   3269  O OH    . TYR A  1 441 ? 31.378  26.018  188.411 1.00 52.53  ? 441 TYR A OH    1 
ATOM   3270  N N     . GLU A  1 442 ? 35.817  19.868  188.544 1.00 60.63  ? 442 GLU A N     1 
ATOM   3271  C CA    . GLU A  1 442 ? 36.341  19.648  189.886 1.00 61.62  ? 442 GLU A CA    1 
ATOM   3272  C C     . GLU A  1 442 ? 37.839  19.932  189.933 1.00 57.32  ? 442 GLU A C     1 
ATOM   3273  O O     . GLU A  1 442 ? 38.344  20.485  190.909 1.00 57.90  ? 442 GLU A O     1 
ATOM   3274  C CB    . GLU A  1 442 ? 36.056  18.218  190.356 1.00 66.65  ? 442 GLU A CB    1 
ATOM   3275  C CG    . GLU A  1 442 ? 36.693  17.853  191.693 1.00 65.68  ? 442 GLU A CG    1 
ATOM   3276  C CD    . GLU A  1 442 ? 36.148  18.664  192.856 1.00 71.55  ? 442 GLU A CD    1 
ATOM   3277  O OE1   . GLU A  1 442 ? 35.015  19.182  192.752 1.00 77.23  ? 442 GLU A OE1   1 
ATOM   3278  O OE2   . GLU A  1 442 ? 36.855  18.784  193.879 1.00 69.55  ? 442 GLU A OE2   1 
ATOM   3279  N N     . PHE A  1 443 ? 38.544  19.558  188.870 1.00 55.29  ? 443 PHE A N     1 
ATOM   3280  C CA    . PHE A  1 443 ? 39.982  19.799  188.788 1.00 58.01  ? 443 PHE A CA    1 
ATOM   3281  C C     . PHE A  1 443 ? 40.318  21.289  188.792 1.00 57.77  ? 443 PHE A C     1 
ATOM   3282  O O     . PHE A  1 443 ? 41.252  21.719  189.468 1.00 57.83  ? 443 PHE A O     1 
ATOM   3283  C CB    . PHE A  1 443 ? 40.571  19.145  187.535 1.00 60.55  ? 443 PHE A CB    1 
ATOM   3284  C CG    . PHE A  1 443 ? 41.947  19.640  187.190 1.00 65.66  ? 443 PHE A CG    1 
ATOM   3285  C CD1   . PHE A  1 443 ? 42.994  19.483  188.082 1.00 68.44  ? 443 PHE A CD1   1 
ATOM   3286  C CD2   . PHE A  1 443 ? 42.192  20.267  185.979 1.00 65.05  ? 443 PHE A CD2   1 
ATOM   3287  C CE1   . PHE A  1 443 ? 44.259  19.943  187.777 1.00 63.88  ? 443 PHE A CE1   1 
ATOM   3288  C CE2   . PHE A  1 443 ? 43.457  20.728  185.667 1.00 63.77  ? 443 PHE A CE2   1 
ATOM   3289  C CZ    . PHE A  1 443 ? 44.490  20.565  186.568 1.00 63.19  ? 443 PHE A CZ    1 
ATOM   3290  N N     . MET A  1 444 ? 39.552  22.071  188.038 1.00 58.49  ? 444 MET A N     1 
ATOM   3291  C CA    . MET A  1 444 ? 39.821  23.498  187.878 1.00 57.59  ? 444 MET A CA    1 
ATOM   3292  C C     . MET A  1 444 ? 39.446  24.320  189.112 1.00 51.80  ? 444 MET A C     1 
ATOM   3293  O O     . MET A  1 444 ? 39.819  25.489  189.217 1.00 53.53  ? 444 MET A O     1 
ATOM   3294  C CB    . MET A  1 444 ? 39.077  24.034  186.652 1.00 55.43  ? 444 MET A CB    1 
ATOM   3295  C CG    . MET A  1 444 ? 39.586  23.485  185.325 1.00 55.63  ? 444 MET A CG    1 
ATOM   3296  S SD    . MET A  1 444 ? 41.303  23.935  185.007 1.00 59.13  ? 444 MET A SD    1 
ATOM   3297  C CE    . MET A  1 444 ? 41.181  25.723  184.967 1.00 49.81  ? 444 MET A CE    1 
ATOM   3298  N N     . LYS A  1 445 ? 38.722  23.702  190.044 1.00 47.77  ? 445 LYS A N     1 
ATOM   3299  C CA    . LYS A  1 445 ? 38.196  24.396  191.225 1.00 54.47  ? 445 LYS A CA    1 
ATOM   3300  C C     . LYS A  1 445 ? 39.205  25.268  191.996 1.00 55.44  ? 445 LYS A C     1 
ATOM   3301  O O     . LYS A  1 445 ? 38.882  26.399  192.358 1.00 51.96  ? 445 LYS A O     1 
ATOM   3302  C CB    . LYS A  1 445 ? 37.569  23.379  192.190 1.00 57.68  ? 445 LYS A CB    1 
ATOM   3303  C CG    . LYS A  1 445 ? 36.902  24.008  193.407 1.00 61.41  ? 445 LYS A CG    1 
ATOM   3304  C CD    . LYS A  1 445 ? 35.824  23.102  193.986 1.00 68.66  ? 445 LYS A CD    1 
ATOM   3305  C CE    . LYS A  1 445 ? 36.417  21.872  194.654 1.00 79.75  ? 445 LYS A CE    1 
ATOM   3306  N NZ    . LYS A  1 445 ? 35.375  20.861  195.004 1.00 80.70  ? 445 LYS A NZ    1 
ATOM   3307  N N     . PRO A  1 446 ? 40.425  24.759  192.256 1.00 57.57  ? 446 PRO A N     1 
ATOM   3308  C CA    . PRO A  1 446 ? 41.325  25.621  193.029 1.00 54.92  ? 446 PRO A CA    1 
ATOM   3309  C C     . PRO A  1 446 ? 41.960  26.772  192.249 1.00 56.46  ? 446 PRO A C     1 
ATOM   3310  O O     . PRO A  1 446 ? 42.529  27.662  192.878 1.00 60.50  ? 446 PRO A O     1 
ATOM   3311  C CB    . PRO A  1 446 ? 42.415  24.651  193.489 1.00 61.81  ? 446 PRO A CB    1 
ATOM   3312  C CG    . PRO A  1 446 ? 42.448  23.623  192.419 1.00 54.92  ? 446 PRO A CG    1 
ATOM   3313  C CD    . PRO A  1 446 ? 41.000  23.413  192.086 1.00 55.78  ? 446 PRO A CD    1 
ATOM   3314  N N     . PHE A  1 447 ? 41.887  26.763  190.923 1.00 56.09  ? 447 PHE A N     1 
ATOM   3315  C CA    . PHE A  1 447 ? 42.583  27.787  190.146 1.00 55.24  ? 447 PHE A CA    1 
ATOM   3316  C C     . PHE A  1 447 ? 41.664  28.931  189.726 1.00 57.77  ? 447 PHE A C     1 
ATOM   3317  O O     . PHE A  1 447 ? 42.131  30.017  189.377 1.00 54.85  ? 447 PHE A O     1 
ATOM   3318  C CB    . PHE A  1 447 ? 43.232  27.170  188.909 1.00 55.07  ? 447 PHE A CB    1 
ATOM   3319  C CG    . PHE A  1 447 ? 44.070  25.961  189.205 1.00 59.68  ? 447 PHE A CG    1 
ATOM   3320  C CD1   . PHE A  1 447 ? 45.215  26.062  189.975 1.00 57.91  ? 447 PHE A CD1   1 
ATOM   3321  C CD2   . PHE A  1 447 ? 43.711  24.720  188.708 1.00 59.77  ? 447 PHE A CD2   1 
ATOM   3322  C CE1   . PHE A  1 447 ? 45.985  24.948  190.246 1.00 61.18  ? 447 PHE A CE1   1 
ATOM   3323  C CE2   . PHE A  1 447 ? 44.475  23.605  188.975 1.00 64.10  ? 447 PHE A CE2   1 
ATOM   3324  C CZ    . PHE A  1 447 ? 45.614  23.718  189.744 1.00 62.16  ? 447 PHE A CZ    1 
ATOM   3325  N N     . VAL A  1 448 ? 40.358  28.684  189.766 1.00 57.43  ? 448 VAL A N     1 
ATOM   3326  C CA    . VAL A  1 448 ? 39.382  29.659  189.296 1.00 51.54  ? 448 VAL A CA    1 
ATOM   3327  C C     . VAL A  1 448 ? 38.749  30.427  190.453 1.00 54.87  ? 448 VAL A C     1 
ATOM   3328  O O     . VAL A  1 448 ? 39.184  30.300  191.598 1.00 54.90  ? 448 VAL A O     1 
ATOM   3329  C CB    . VAL A  1 448 ? 38.279  28.979  188.465 1.00 49.32  ? 448 VAL A CB    1 
ATOM   3330  C CG1   . VAL A  1 448 ? 38.900  28.206  187.313 1.00 45.28  ? 448 VAL A CG1   1 
ATOM   3331  C CG2   . VAL A  1 448 ? 37.438  28.058  189.338 1.00 50.68  ? 448 VAL A CG2   1 
ATOM   3332  N N     . SER A  1 449 ? 37.730  31.227  190.144 1.00 53.32  ? 449 SER A N     1 
ATOM   3333  C CA    . SER A  1 449 ? 37.067  32.064  191.140 1.00 50.17  ? 449 SER A CA    1 
ATOM   3334  C C     . SER A  1 449 ? 36.490  31.240  192.287 1.00 52.46  ? 449 SER A C     1 
ATOM   3335  O O     . SER A  1 449 ? 36.119  30.078  192.111 1.00 52.57  ? 449 SER A O     1 
ATOM   3336  C CB    . SER A  1 449 ? 35.956  32.895  190.494 1.00 53.33  ? 449 SER A CB    1 
ATOM   3337  O OG    . SER A  1 449 ? 35.007  32.067  189.843 1.00 51.97  ? 449 SER A OG    1 
ATOM   3338  N N     . LYS A  1 450 ? 36.438  31.851  193.469 1.00 55.75  ? 450 LYS A N     1 
ATOM   3339  C CA    . LYS A  1 450 ? 35.958  31.180  194.675 1.00 57.13  ? 450 LYS A CA    1 
ATOM   3340  C C     . LYS A  1 450 ? 35.162  32.132  195.561 1.00 57.98  ? 450 LYS A C     1 
ATOM   3341  O O     . LYS A  1 450 ? 35.354  33.349  195.508 1.00 60.25  ? 450 LYS A O     1 
ATOM   3342  C CB    . LYS A  1 450 ? 37.124  30.601  195.481 1.00 66.10  ? 450 LYS A CB    1 
ATOM   3343  C CG    . LYS A  1 450 ? 38.287  30.084  194.651 1.00 58.30  ? 450 LYS A CG    1 
ATOM   3344  C CD    . LYS A  1 450 ? 39.546  29.944  195.490 1.00 63.13  ? 450 LYS A CD    1 
ATOM   3345  C CE    . LYS A  1 450 ? 40.748  29.539  194.644 1.00 63.06  ? 450 LYS A CE    1 
ATOM   3346  N NZ    . LYS A  1 450 ? 41.521  30.709  194.135 1.00 62.57  ? 450 LYS A NZ    1 
ATOM   3347  N N     . ASN A  1 451 ? 34.288  31.557  196.385 1.00 59.60  ? 451 ASN A N     1 
ATOM   3348  C CA    . ASN A  1 451 ? 33.475  32.301  197.352 1.00 65.24  ? 451 ASN A CA    1 
ATOM   3349  C C     . ASN A  1 451 ? 32.804  33.557  196.793 1.00 65.16  ? 451 ASN A C     1 
ATOM   3350  O O     . ASN A  1 451 ? 33.113  34.669  197.223 1.00 69.93  ? 451 ASN A O     1 
ATOM   3351  C CB    . ASN A  1 451 ? 34.330  32.684  198.563 1.00 72.94  ? 451 ASN A CB    1 
ATOM   3352  C CG    . ASN A  1 451 ? 34.994  31.483  199.212 1.00 74.92  ? 451 ASN A CG    1 
ATOM   3353  O OD1   . ASN A  1 451 ? 34.400  30.409  199.313 1.00 77.91  ? 451 ASN A OD1   1 
ATOM   3354  N ND2   . ASN A  1 451 ? 36.235  31.659  199.652 1.00 77.80  ? 451 ASN A ND2   1 
ATOM   3355  N N     . PRO A  1 452 ? 31.868  33.385  195.844 1.00 62.78  ? 452 PRO A N     1 
ATOM   3356  C CA    . PRO A  1 452 ? 31.427  32.114  195.262 1.00 58.11  ? 452 PRO A CA    1 
ATOM   3357  C C     . PRO A  1 452 ? 32.180  31.773  193.985 1.00 52.79  ? 452 PRO A C     1 
ATOM   3358  O O     . PRO A  1 452 ? 32.893  32.626  193.460 1.00 54.72  ? 452 PRO A O     1 
ATOM   3359  C CB    . PRO A  1 452 ? 29.958  32.378  194.954 1.00 53.17  ? 452 PRO A CB    1 
ATOM   3360  C CG    . PRO A  1 452 ? 29.953  33.816  194.552 1.00 57.40  ? 452 PRO A CG    1 
ATOM   3361  C CD    . PRO A  1 452 ? 31.030  34.503  195.374 1.00 59.72  ? 452 PRO A CD    1 
ATOM   3362  N N     . ARG A  1 453 ? 32.020  30.549  193.491 1.00 51.74  ? 453 ARG A N     1 
ATOM   3363  C CA    . ARG A  1 453 ? 32.536  30.197  192.174 1.00 50.74  ? 453 ARG A CA    1 
ATOM   3364  C C     . ARG A  1 453 ? 31.618  30.804  191.119 1.00 56.78  ? 453 ARG A C     1 
ATOM   3365  O O     . ARG A  1 453 ? 30.421  30.522  191.093 1.00 51.59  ? 453 ARG A O     1 
ATOM   3366  C CB    . ARG A  1 453 ? 32.642  28.680  192.006 1.00 49.90  ? 453 ARG A CB    1 
ATOM   3367  C CG    . ARG A  1 453 ? 33.360  28.254  190.732 1.00 49.09  ? 453 ARG A CG    1 
ATOM   3368  C CD    . ARG A  1 453 ? 33.598  26.754  190.698 1.00 41.54  ? 453 ARG A CD    1 
ATOM   3369  N NE    . ARG A  1 453 ? 34.417  26.361  189.555 1.00 44.60  ? 453 ARG A NE    1 
ATOM   3370  C CZ    . ARG A  1 453 ? 34.915  25.141  189.374 1.00 48.93  ? 453 ARG A CZ    1 
ATOM   3371  N NH1   . ARG A  1 453 ? 34.679  24.187  190.263 1.00 46.97  ? 453 ARG A NH1   1 
ATOM   3372  N NH2   . ARG A  1 453 ? 35.654  24.877  188.304 1.00 50.61  ? 453 ARG A NH2   1 
ATOM   3373  N N     . LEU A  1 454 ? 32.184  31.634  190.250 1.00 57.25  ? 454 LEU A N     1 
ATOM   3374  C CA    . LEU A  1 454 ? 31.386  32.477  189.366 1.00 49.68  ? 454 LEU A CA    1 
ATOM   3375  C C     . LEU A  1 454 ? 30.869  31.756  188.127 1.00 47.56  ? 454 LEU A C     1 
ATOM   3376  O O     . LEU A  1 454 ? 31.467  30.790  187.654 1.00 43.42  ? 454 LEU A O     1 
ATOM   3377  C CB    . LEU A  1 454 ? 32.199  33.701  188.943 1.00 47.89  ? 454 LEU A CB    1 
ATOM   3378  C CG    . LEU A  1 454 ? 32.773  34.517  190.102 1.00 47.98  ? 454 LEU A CG    1 
ATOM   3379  C CD1   . LEU A  1 454 ? 33.598  35.684  189.589 1.00 48.00  ? 454 LEU A CD1   1 
ATOM   3380  C CD2   . LEU A  1 454 ? 31.665  35.002  191.015 1.00 48.04  ? 454 LEU A CD2   1 
ATOM   3381  N N     . GLY A  1 455 ? 29.748  32.248  187.610 1.00 44.30  ? 455 GLY A N     1 
ATOM   3382  C CA    . GLY A  1 455 ? 29.166  31.737  186.384 1.00 42.14  ? 455 GLY A CA    1 
ATOM   3383  C C     . GLY A  1 455 ? 28.614  32.864  185.531 1.00 40.65  ? 455 GLY A C     1 
ATOM   3384  O O     . GLY A  1 455 ? 28.708  34.031  185.893 1.00 41.80  ? 455 GLY A O     1 
ATOM   3385  N N     . TYR A  1 456 ? 28.016  32.504  184.403 1.00 37.16  ? 456 TYR A N     1 
ATOM   3386  C CA    . TYR A  1 456 ? 27.515  33.468  183.431 1.00 37.48  ? 456 TYR A CA    1 
ATOM   3387  C C     . TYR A  1 456 ? 26.120  33.018  183.002 1.00 33.17  ? 456 TYR A C     1 
ATOM   3388  O O     . TYR A  1 456 ? 25.949  31.890  182.553 1.00 33.66  ? 456 TYR A O     1 
ATOM   3389  C CB    . TYR A  1 456 ? 28.487  33.554  182.251 1.00 35.36  ? 456 TYR A CB    1 
ATOM   3390  C CG    . TYR A  1 456 ? 28.050  34.356  181.045 1.00 37.49  ? 456 TYR A CG    1 
ATOM   3391  C CD1   . TYR A  1 456 ? 27.191  35.441  181.159 1.00 34.92  ? 456 TYR A CD1   1 
ATOM   3392  C CD2   . TYR A  1 456 ? 28.519  34.022  179.781 1.00 37.26  ? 456 TYR A CD2   1 
ATOM   3393  C CE1   . TYR A  1 456 ? 26.806  36.165  180.040 1.00 32.79  ? 456 TYR A CE1   1 
ATOM   3394  C CE2   . TYR A  1 456 ? 28.144  34.734  178.666 1.00 36.46  ? 456 TYR A CE2   1 
ATOM   3395  C CZ    . TYR A  1 456 ? 27.288  35.803  178.798 1.00 36.87  ? 456 TYR A CZ    1 
ATOM   3396  O OH    . TYR A  1 456 ? 26.916  36.508  177.677 1.00 33.57  ? 456 TYR A OH    1 
ATOM   3397  N N     . VAL A  1 457 ? 25.125  33.890  183.153 1.00 35.14  ? 457 VAL A N     1 
ATOM   3398  C CA    . VAL A  1 457 ? 23.726  33.466  183.029 1.00 33.86  ? 457 VAL A CA    1 
ATOM   3399  C C     . VAL A  1 457 ? 23.381  32.957  181.622 1.00 34.79  ? 457 VAL A C     1 
ATOM   3400  O O     . VAL A  1 457 ? 22.507  32.107  181.472 1.00 34.23  ? 457 VAL A O     1 
ATOM   3401  C CB    . VAL A  1 457 ? 22.754  34.603  183.429 1.00 32.26  ? 457 VAL A CB    1 
ATOM   3402  C CG1   . VAL A  1 457 ? 22.721  35.686  182.374 1.00 31.05  ? 457 VAL A CG1   1 
ATOM   3403  C CG2   . VAL A  1 457 ? 21.355  34.050  183.677 1.00 37.05  ? 457 VAL A CG2   1 
ATOM   3404  N N     . ASN A  1 458 ? 24.079  33.450  180.600 1.00 31.68  ? 458 ASN A N     1 
ATOM   3405  C CA    . ASN A  1 458 ? 23.901  32.925  179.249 1.00 31.60  ? 458 ASN A CA    1 
ATOM   3406  C C     . ASN A  1 458 ? 24.529  31.543  179.118 1.00 35.01  ? 458 ASN A C     1 
ATOM   3407  O O     . ASN A  1 458 ? 24.226  30.791  178.190 1.00 34.59  ? 458 ASN A O     1 
ATOM   3408  C CB    . ASN A  1 458 ? 24.489  33.874  178.207 1.00 30.05  ? 458 ASN A CB    1 
ATOM   3409  C CG    . ASN A  1 458 ? 23.464  34.859  177.680 1.00 35.21  ? 458 ASN A CG    1 
ATOM   3410  O OD1   . ASN A  1 458 ? 22.266  34.572  177.656 1.00 31.13  ? 458 ASN A OD1   1 
ATOM   3411  N ND2   . ASN A  1 458 ? 23.928  36.031  177.264 1.00 32.28  ? 458 ASN A ND2   1 
ATOM   3412  N N     . HIS A  1 459 ? 25.417  31.222  180.051 1.00 38.42  ? 459 HIS A N     1 
ATOM   3413  C CA    . HIS A  1 459 ? 25.914  29.865  180.197 1.00 40.81  ? 459 HIS A CA    1 
ATOM   3414  C C     . HIS A  1 459 ? 25.163  29.184  181.331 1.00 38.36  ? 459 HIS A C     1 
ATOM   3415  O O     . HIS A  1 459 ? 25.778  28.652  182.257 1.00 40.70  ? 459 HIS A O     1 
ATOM   3416  C CB    . HIS A  1 459 ? 27.418  29.864  180.471 1.00 44.96  ? 459 HIS A CB    1 
ATOM   3417  C CG    . HIS A  1 459 ? 28.255  29.827  179.232 1.00 47.80  ? 459 HIS A CG    1 
ATOM   3418  N ND1   . HIS A  1 459 ? 29.083  28.768  178.927 1.00 56.38  ? 459 HIS A ND1   1 
ATOM   3419  C CD2   . HIS A  1 459 ? 28.378  30.709  178.213 1.00 53.13  ? 459 HIS A CD2   1 
ATOM   3420  C CE1   . HIS A  1 459 ? 29.689  29.005  177.778 1.00 61.92  ? 459 HIS A CE1   1 
ATOM   3421  N NE2   . HIS A  1 459 ? 29.279  30.176  177.323 1.00 61.04  ? 459 HIS A NE2   1 
ATOM   3422  N N     . ILE A  1 460 ? 23.834  29.220  181.253 1.00 41.29  ? 460 ILE A N     1 
ATOM   3423  C CA    . ILE A  1 460 ? 22.970  28.688  182.302 1.00 41.69  ? 460 ILE A CA    1 
ATOM   3424  C C     . ILE A  1 460 ? 23.355  27.239  182.634 1.00 39.59  ? 460 ILE A C     1 
ATOM   3425  O O     . ILE A  1 460 ? 23.571  26.412  181.742 1.00 40.15  ? 460 ILE A O     1 
ATOM   3426  C CB    . ILE A  1 460 ? 21.463  28.794  181.899 1.00 41.67  ? 460 ILE A CB    1 
ATOM   3427  C CG1   . ILE A  1 460 ? 20.551  28.673  183.122 1.00 43.45  ? 460 ILE A CG1   1 
ATOM   3428  C CG2   . ILE A  1 460 ? 21.093  27.811  180.785 1.00 38.04  ? 460 ILE A CG2   1 
ATOM   3429  C CD1   . ILE A  1 460 ? 20.344  29.985  183.850 1.00 44.57  ? 460 ILE A CD1   1 
ATOM   3430  N N     . ASP A  1 461 ? 23.488  26.960  183.928 1.00 41.84  ? 461 ASP A N     1 
ATOM   3431  C CA    . ASP A  1 461 ? 23.989  25.672  184.402 1.00 42.74  ? 461 ASP A CA    1 
ATOM   3432  C C     . ASP A  1 461 ? 23.165  25.184  185.594 1.00 41.36  ? 461 ASP A C     1 
ATOM   3433  O O     . ASP A  1 461 ? 23.213  25.770  186.677 1.00 43.63  ? 461 ASP A O     1 
ATOM   3434  C CB    . ASP A  1 461 ? 25.469  25.787  184.785 1.00 44.41  ? 461 ASP A CB    1 
ATOM   3435  C CG    . ASP A  1 461 ? 26.134  24.434  184.991 1.00 48.08  ? 461 ASP A CG    1 
ATOM   3436  O OD1   . ASP A  1 461 ? 25.433  23.400  184.975 1.00 48.16  ? 461 ASP A OD1   1 
ATOM   3437  O OD2   . ASP A  1 461 ? 27.371  24.408  185.172 1.00 49.79  ? 461 ASP A OD2   1 
ATOM   3438  N N     . LEU A  1 462 ? 22.417  24.105  185.387 1.00 42.40  ? 462 LEU A N     1 
ATOM   3439  C CA    . LEU A  1 462 ? 21.485  23.616  186.396 1.00 49.46  ? 462 LEU A CA    1 
ATOM   3440  C C     . LEU A  1 462 ? 22.131  22.680  187.415 1.00 50.37  ? 462 LEU A C     1 
ATOM   3441  O O     . LEU A  1 462 ? 21.502  22.320  188.413 1.00 49.23  ? 462 LEU A O     1 
ATOM   3442  C CB    . LEU A  1 462 ? 20.307  22.915  185.723 1.00 40.88  ? 462 LEU A CB    1 
ATOM   3443  C CG    . LEU A  1 462 ? 19.353  23.844  184.972 1.00 44.02  ? 462 LEU A CG    1 
ATOM   3444  C CD1   . LEU A  1 462 ? 18.139  23.072  184.475 1.00 38.60  ? 462 LEU A CD1   1 
ATOM   3445  C CD2   . LEU A  1 462 ? 18.936  25.011  185.858 1.00 44.47  ? 462 LEU A CD2   1 
ATOM   3446  N N     . ASP A  1 463 ? 23.380  22.291  187.165 1.00 45.65  ? 463 ASP A N     1 
ATOM   3447  C CA    . ASP A  1 463 ? 24.152  21.517  188.138 1.00 50.34  ? 463 ASP A CA    1 
ATOM   3448  C C     . ASP A  1 463 ? 24.259  22.296  189.438 1.00 54.71  ? 463 ASP A C     1 
ATOM   3449  O O     . ASP A  1 463 ? 24.372  21.724  190.523 1.00 59.86  ? 463 ASP A O     1 
ATOM   3450  C CB    . ASP A  1 463 ? 25.554  21.201  187.613 1.00 51.77  ? 463 ASP A CB    1 
ATOM   3451  C CG    . ASP A  1 463 ? 25.539  20.257  186.432 1.00 55.50  ? 463 ASP A CG    1 
ATOM   3452  O OD1   . ASP A  1 463 ? 24.463  19.710  186.116 1.00 55.71  ? 463 ASP A OD1   1 
ATOM   3453  O OD2   . ASP A  1 463 ? 26.613  20.052  185.827 1.00 58.83  ? 463 ASP A OD2   1 
ATOM   3454  N N     . LEU A  1 464 ? 24.213  23.617  189.303 1.00 55.90  ? 464 LEU A N     1 
ATOM   3455  C CA    . LEU A  1 464 ? 24.338  24.546  190.415 1.00 54.53  ? 464 LEU A CA    1 
ATOM   3456  C C     . LEU A  1 464 ? 23.068  24.565  191.269 1.00 56.49  ? 464 LEU A C     1 
ATOM   3457  O O     . LEU A  1 464 ? 23.027  25.205  192.320 1.00 60.69  ? 464 LEU A O     1 
ATOM   3458  C CB    . LEU A  1 464 ? 24.646  25.955  189.889 1.00 57.69  ? 464 LEU A CB    1 
ATOM   3459  C CG    . LEU A  1 464 ? 26.038  26.344  189.363 1.00 59.00  ? 464 LEU A CG    1 
ATOM   3460  C CD1   . LEU A  1 464 ? 26.665  25.304  188.436 1.00 57.79  ? 464 LEU A CD1   1 
ATOM   3461  C CD2   . LEU A  1 464 ? 25.959  27.693  188.650 1.00 53.99  ? 464 LEU A CD2   1 
ATOM   3462  N N     . GLY A  1 465 ? 22.035  23.864  190.803 1.00 57.16  ? 465 GLY A N     1 
ATOM   3463  C CA    . GLY A  1 465 ? 20.780  23.751  191.527 1.00 51.98  ? 465 GLY A CA    1 
ATOM   3464  C C     . GLY A  1 465 ? 19.593  24.307  190.759 1.00 56.39  ? 465 GLY A C     1 
ATOM   3465  O O     . GLY A  1 465 ? 19.744  24.783  189.633 1.00 57.18  ? 465 GLY A O     1 
ATOM   3466  N N     . GLY A  1 466 ? 18.411  24.252  191.370 1.00 55.67  ? 466 GLY A N     1 
ATOM   3467  C CA    . GLY A  1 466 ? 17.204  24.775  190.750 1.00 55.74  ? 466 GLY A CA    1 
ATOM   3468  C C     . GLY A  1 466 ? 15.997  24.859  191.672 1.00 55.30  ? 466 GLY A C     1 
ATOM   3469  O O     . GLY A  1 466 ? 15.928  24.164  192.686 1.00 56.82  ? 466 GLY A O     1 
ATOM   3470  N N     . ILE A  1 467 ? 15.044  25.716  191.312 1.00 54.23  ? 467 ILE A N     1 
ATOM   3471  C CA    . ILE A  1 467 ? 13.809  25.883  192.075 1.00 51.19  ? 467 ILE A CA    1 
ATOM   3472  C C     . ILE A  1 467 ? 12.668  25.057  191.484 1.00 54.23  ? 467 ILE A C     1 
ATOM   3473  O O     . ILE A  1 467 ? 12.472  25.043  190.269 1.00 55.70  ? 467 ILE A O     1 
ATOM   3474  C CB    . ILE A  1 467 ? 13.359  27.369  192.123 1.00 49.74  ? 467 ILE A CB    1 
ATOM   3475  C CG1   . ILE A  1 467 ? 14.367  28.225  192.891 1.00 54.52  ? 467 ILE A CG1   1 
ATOM   3476  C CG2   . ILE A  1 467 ? 11.975  27.496  192.753 1.00 53.41  ? 467 ILE A CG2   1 
ATOM   3477  C CD1   . ILE A  1 467 ? 14.176  28.212  194.393 1.00 55.77  ? 467 ILE A CD1   1 
ATOM   3478  N N     . ASP A  1 468 ? 11.932  24.360  192.347 1.00 57.90  ? 468 ASP A N     1 
ATOM   3479  C CA    . ASP A  1 468 ? 10.643  23.784  191.974 1.00 56.05  ? 468 ASP A CA    1 
ATOM   3480  C C     . ASP A  1 468 ? 9.555   24.763  192.397 1.00 52.60  ? 468 ASP A C     1 
ATOM   3481  O O     . ASP A  1 468 ? 9.205   24.835  193.576 1.00 55.95  ? 468 ASP A O     1 
ATOM   3482  C CB    . ASP A  1 468 ? 10.427  22.415  192.636 1.00 57.13  ? 468 ASP A CB    1 
ATOM   3483  C CG    . ASP A  1 468 ? 9.149   21.717  192.162 1.00 62.78  ? 468 ASP A CG    1 
ATOM   3484  O OD1   . ASP A  1 468 ? 8.264   22.377  191.577 1.00 61.30  ? 468 ASP A OD1   1 
ATOM   3485  O OD2   . ASP A  1 468 ? 9.028   20.492  192.382 1.00 66.34  ? 468 ASP A OD2   1 
ATOM   3486  N N     . TRP A  1 469 ? 9.019   25.513  191.438 1.00 50.46  ? 469 TRP A N     1 
ATOM   3487  C CA    . TRP A  1 469 ? 8.013   26.527  191.737 1.00 52.33  ? 469 TRP A CA    1 
ATOM   3488  C C     . TRP A  1 469 ? 6.655   25.910  192.074 1.00 53.30  ? 469 TRP A C     1 
ATOM   3489  O O     . TRP A  1 469 ? 5.717   26.622  192.432 1.00 53.29  ? 469 TRP A O     1 
ATOM   3490  C CB    . TRP A  1 469 ? 7.868   27.502  190.565 1.00 49.45  ? 469 TRP A CB    1 
ATOM   3491  C CG    . TRP A  1 469 ? 9.085   28.347  190.335 1.00 46.04  ? 469 TRP A CG    1 
ATOM   3492  C CD1   . TRP A  1 469 ? 9.989   28.226  189.321 1.00 40.61  ? 469 TRP A CD1   1 
ATOM   3493  C CD2   . TRP A  1 469 ? 9.536   29.441  191.145 1.00 45.23  ? 469 TRP A CD2   1 
ATOM   3494  N NE1   . TRP A  1 469 ? 10.973  29.179  189.447 1.00 44.36  ? 469 TRP A NE1   1 
ATOM   3495  C CE2   . TRP A  1 469 ? 10.718  29.937  190.560 1.00 43.26  ? 469 TRP A CE2   1 
ATOM   3496  C CE3   . TRP A  1 469 ? 9.054   30.050  192.309 1.00 47.70  ? 469 TRP A CE3   1 
ATOM   3497  C CZ2   . TRP A  1 469 ? 11.424  31.011  191.096 1.00 42.39  ? 469 TRP A CZ2   1 
ATOM   3498  C CZ3   . TRP A  1 469 ? 9.757   31.116  192.840 1.00 49.34  ? 469 TRP A CZ3   1 
ATOM   3499  C CH2   . TRP A  1 469 ? 10.929  31.586  192.234 1.00 42.33  ? 469 TRP A CH2   1 
ATOM   3500  N N     . GLY A  1 470 ? 6.560   24.587  191.963 1.00 57.80  ? 470 GLY A N     1 
ATOM   3501  C CA    . GLY A  1 470 ? 5.353   23.868  192.332 1.00 59.43  ? 470 GLY A CA    1 
ATOM   3502  C C     . GLY A  1 470 ? 5.401   23.342  193.757 1.00 62.14  ? 470 GLY A C     1 
ATOM   3503  O O     . GLY A  1 470 ? 4.390   22.904  194.305 1.00 62.05  ? 470 GLY A O     1 
ATOM   3504  N N     . ASN A  1 471 ? 6.591   23.381  194.349 1.00 60.67  ? 471 ASN A N     1 
ATOM   3505  C CA    . ASN A  1 471 ? 6.795   23.003  195.745 1.00 65.39  ? 471 ASN A CA    1 
ATOM   3506  C C     . ASN A  1 471 ? 6.704   24.241  196.634 1.00 67.83  ? 471 ASN A C     1 
ATOM   3507  O O     . ASN A  1 471 ? 7.624   25.056  196.651 1.00 70.80  ? 471 ASN A O     1 
ATOM   3508  C CB    . ASN A  1 471 ? 8.155   22.307  195.907 1.00 66.11  ? 471 ASN A CB    1 
ATOM   3509  C CG    . ASN A  1 471 ? 8.414   21.810  197.325 1.00 74.94  ? 471 ASN A CG    1 
ATOM   3510  O OD1   . ASN A  1 471 ? 8.050   22.453  198.307 1.00 77.43  ? 471 ASN A OD1   1 
ATOM   3511  N ND2   . ASN A  1 471 ? 9.066   20.658  197.429 1.00 75.70  ? 471 ASN A ND2   1 
ATOM   3512  N N     . LYS A  1 472 ? 5.609   24.372  197.382 1.00 68.45  ? 472 LYS A N     1 
ATOM   3513  C CA    . LYS A  1 472 ? 5.370   25.578  198.175 1.00 66.98  ? 472 LYS A CA    1 
ATOM   3514  C C     . LYS A  1 472 ? 6.426   25.810  199.260 1.00 71.14  ? 472 LYS A C     1 
ATOM   3515  O O     . LYS A  1 472 ? 6.666   26.948  199.660 1.00 70.05  ? 472 LYS A O     1 
ATOM   3516  C CB    . LYS A  1 472 ? 3.983   25.534  198.823 1.00 72.24  ? 472 LYS A CB    1 
ATOM   3517  C CG    . LYS A  1 472 ? 3.517   26.890  199.340 1.00 79.36  ? 472 LYS A CG    1 
ATOM   3518  C CD    . LYS A  1 472 ? 2.176   26.811  200.045 1.00 83.89  ? 472 LYS A CD    1 
ATOM   3519  C CE    . LYS A  1 472 ? 1.611   28.200  200.300 1.00 85.32  ? 472 LYS A CE    1 
ATOM   3520  N NZ    . LYS A  1 472 ? 1.205   28.877  199.033 1.00 86.34  ? 472 LYS A NZ    1 
ATOM   3521  N N     . THR A  1 473 ? 7.052   24.738  199.736 1.00 72.13  ? 473 THR A N     1 
ATOM   3522  C CA    . THR A  1 473 ? 8.108   24.873  200.735 1.00 72.45  ? 473 THR A CA    1 
ATOM   3523  C C     . THR A  1 473 ? 9.277   25.660  200.155 1.00 71.06  ? 473 THR A C     1 
ATOM   3524  O O     . THR A  1 473 ? 9.758   26.621  200.754 1.00 70.01  ? 473 THR A O     1 
ATOM   3525  C CB    . THR A  1 473 ? 8.619   23.506  201.236 1.00 77.02  ? 473 THR A CB    1 
ATOM   3526  O OG1   . THR A  1 473 ? 7.514   22.697  201.652 1.00 78.10  ? 473 THR A OG1   1 
ATOM   3527  C CG2   . THR A  1 473 ? 9.580   23.692  202.398 1.00 76.17  ? 473 THR A CG2   1 
ATOM   3528  N N     . VAL A  1 474 ? 9.714   25.239  198.974 1.00 70.49  ? 474 VAL A N     1 
ATOM   3529  C CA    . VAL A  1 474 ? 10.805  25.889  198.259 1.00 65.03  ? 474 VAL A CA    1 
ATOM   3530  C C     . VAL A  1 474 ? 10.477  27.341  197.912 1.00 64.76  ? 474 VAL A C     1 
ATOM   3531  O O     . VAL A  1 474 ? 11.285  28.240  198.151 1.00 66.78  ? 474 VAL A O     1 
ATOM   3532  C CB    . VAL A  1 474 ? 11.141  25.123  196.963 1.00 63.73  ? 474 VAL A CB    1 
ATOM   3533  C CG1   . VAL A  1 474 ? 12.300  25.778  196.240 1.00 61.53  ? 474 VAL A CG1   1 
ATOM   3534  C CG2   . VAL A  1 474 ? 11.454  23.668  197.272 1.00 66.24  ? 474 VAL A CG2   1 
ATOM   3535  N N     . VAL A  1 475 ? 9.286   27.557  197.359 1.00 65.38  ? 475 VAL A N     1 
ATOM   3536  C CA    . VAL A  1 475 ? 8.876   28.865  196.844 1.00 63.58  ? 475 VAL A CA    1 
ATOM   3537  C C     . VAL A  1 475 ? 8.888   29.966  197.907 1.00 67.59  ? 475 VAL A C     1 
ATOM   3538  O O     . VAL A  1 475 ? 9.298   31.094  197.633 1.00 68.71  ? 475 VAL A O     1 
ATOM   3539  C CB    . VAL A  1 475 ? 7.464   28.792  196.217 1.00 61.35  ? 475 VAL A CB    1 
ATOM   3540  C CG1   . VAL A  1 475 ? 7.033   30.155  195.687 1.00 58.92  ? 475 VAL A CG1   1 
ATOM   3541  C CG2   . VAL A  1 475 ? 7.437   27.763  195.103 1.00 61.39  ? 475 VAL A CG2   1 
ATOM   3542  N N     . ASN A  1 476 ? 8.446   29.638  199.117 1.00 67.70  ? 476 ASN A N     1 
ATOM   3543  C CA    . ASN A  1 476 ? 8.404   30.620  200.197 1.00 70.66  ? 476 ASN A CA    1 
ATOM   3544  C C     . ASN A  1 476 ? 9.792   31.028  200.681 1.00 69.79  ? 476 ASN A C     1 
ATOM   3545  O O     . ASN A  1 476 ? 9.955   32.076  201.305 1.00 70.30  ? 476 ASN A O     1 
ATOM   3546  C CB    . ASN A  1 476 ? 7.586   30.087  201.375 1.00 71.83  ? 476 ASN A CB    1 
ATOM   3547  C CG    . ASN A  1 476 ? 6.095   30.131  201.116 1.00 76.26  ? 476 ASN A CG    1 
ATOM   3548  O OD1   . ASN A  1 476 ? 5.488   31.201  201.098 1.00 77.58  ? 476 ASN A OD1   1 
ATOM   3549  N ND2   . ASN A  1 476 ? 5.494   28.964  200.920 1.00 75.94  ? 476 ASN A ND2   1 
ATOM   3550  N N     . ASN A  1 477 ? 10.787  30.196  200.396 1.00 64.61  ? 477 ASN A N     1 
ATOM   3551  C CA    . ASN A  1 477 ? 12.167  30.504  200.750 1.00 66.94  ? 477 ASN A CA    1 
ATOM   3552  C C     . ASN A  1 477 ? 13.024  30.637  199.494 1.00 63.93  ? 477 ASN A C     1 
ATOM   3553  O O     . ASN A  1 477 ? 14.222  30.355  199.509 1.00 62.12  ? 477 ASN A O     1 
ATOM   3554  C CB    . ASN A  1 477 ? 12.736  29.424  201.673 1.00 66.44  ? 477 ASN A CB    1 
ATOM   3555  C CG    . ASN A  1 477 ? 13.963  29.891  202.433 1.00 70.29  ? 477 ASN A CG    1 
ATOM   3556  O OD1   . ASN A  1 477 ? 14.066  31.057  202.814 1.00 70.70  ? 477 ASN A OD1   1 
ATOM   3557  N ND2   . ASN A  1 477 ? 14.907  28.979  202.649 1.00 68.46  ? 477 ASN A ND2   1 
ATOM   3558  N N     . ALA A  1 478 ? 12.393  31.083  198.411 1.00 63.85  ? 478 ALA A N     1 
ATOM   3559  C CA    . ALA A  1 478 ? 13.011  31.093  197.088 1.00 60.16  ? 478 ALA A CA    1 
ATOM   3560  C C     . ALA A  1 478 ? 14.248  31.982  196.998 1.00 56.14  ? 478 ALA A C     1 
ATOM   3561  O O     . ALA A  1 478 ? 15.213  31.633  196.323 1.00 56.16  ? 478 ALA A O     1 
ATOM   3562  C CB    . ALA A  1 478 ? 11.992  31.523  196.045 1.00 57.09  ? 478 ALA A CB    1 
ATOM   3563  N N     . ILE A  1 479 ? 14.214  33.128  197.669 1.00 54.69  ? 479 ILE A N     1 
ATOM   3564  C CA    . ILE A  1 479 ? 15.321  34.078  197.604 1.00 56.95  ? 479 ILE A CA    1 
ATOM   3565  C C     . ILE A  1 479 ? 16.624  33.481  198.139 1.00 56.92  ? 479 ILE A C     1 
ATOM   3566  O O     . ILE A  1 479 ? 17.660  33.542  197.477 1.00 60.13  ? 479 ILE A O     1 
ATOM   3567  C CB    . ILE A  1 479 ? 15.003  35.368  198.386 1.00 51.90  ? 479 ILE A CB    1 
ATOM   3568  C CG1   . ILE A  1 479 ? 13.850  36.126  197.727 1.00 49.19  ? 479 ILE A CG1   1 
ATOM   3569  C CG2   . ILE A  1 479 ? 16.228  36.259  198.459 1.00 53.79  ? 479 ILE A CG2   1 
ATOM   3570  C CD1   . ILE A  1 479 ? 13.559  37.466  198.370 1.00 48.36  ? 479 ILE A CD1   1 
ATOM   3571  N N     . GLU A  1 480 ? 16.566  32.896  199.331 1.00 57.88  ? 480 GLU A N     1 
ATOM   3572  C CA    . GLU A  1 480 ? 17.756  32.337  199.965 1.00 56.48  ? 480 GLU A CA    1 
ATOM   3573  C C     . GLU A  1 480 ? 18.214  31.036  199.306 1.00 58.27  ? 480 GLU A C     1 
ATOM   3574  O O     . GLU A  1 480 ? 19.405  30.723  199.302 1.00 60.73  ? 480 GLU A O     1 
ATOM   3575  C CB    . GLU A  1 480 ? 17.506  32.107  201.457 1.00 58.80  ? 480 GLU A CB    1 
ATOM   3576  C CG    . GLU A  1 480 ? 17.312  33.391  202.244 1.00 57.57  ? 480 GLU A CG    1 
ATOM   3577  C CD    . GLU A  1 480 ? 18.495  34.333  202.108 1.00 59.52  ? 480 GLU A CD    1 
ATOM   3578  O OE1   . GLU A  1 480 ? 19.648  33.849  202.098 1.00 59.62  ? 480 GLU A OE1   1 
ATOM   3579  O OE2   . GLU A  1 480 ? 18.273  35.558  202.001 1.00 57.54  ? 480 GLU A OE2   1 
ATOM   3580  N N     . ILE A  1 481 ? 17.269  30.279  198.757 1.00 59.42  ? 481 ILE A N     1 
ATOM   3581  C CA    . ILE A  1 481 ? 17.609  29.072  198.013 1.00 55.40  ? 481 ILE A CA    1 
ATOM   3582  C C     . ILE A  1 481 ? 18.282  29.447  196.692 1.00 55.94  ? 481 ILE A C     1 
ATOM   3583  O O     . ILE A  1 481 ? 19.293  28.858  196.313 1.00 58.20  ? 481 ILE A O     1 
ATOM   3584  C CB    . ILE A  1 481 ? 16.368  28.192  197.736 1.00 58.68  ? 481 ILE A CB    1 
ATOM   3585  C CG1   . ILE A  1 481 ? 15.783  27.654  199.045 1.00 63.08  ? 481 ILE A CG1   1 
ATOM   3586  C CG2   . ILE A  1 481 ? 16.726  27.031  196.825 1.00 56.39  ? 481 ILE A CG2   1 
ATOM   3587  C CD1   . ILE A  1 481 ? 14.530  26.825  198.858 1.00 60.83  ? 481 ILE A CD1   1 
ATOM   3588  N N     . SER A  1 482 ? 17.728  30.444  196.005 1.00 56.94  ? 482 SER A N     1 
ATOM   3589  C CA    . SER A  1 482 ? 18.264  30.882  194.716 1.00 58.39  ? 482 SER A CA    1 
ATOM   3590  C C     . SER A  1 482 ? 19.532  31.725  194.851 1.00 56.16  ? 482 SER A C     1 
ATOM   3591  O O     . SER A  1 482 ? 20.209  31.992  193.856 1.00 55.53  ? 482 SER A O     1 
ATOM   3592  C CB    . SER A  1 482 ? 17.210  31.671  193.934 1.00 54.84  ? 482 SER A CB    1 
ATOM   3593  O OG    . SER A  1 482 ? 16.101  30.857  193.593 1.00 53.20  ? 482 SER A OG    1 
ATOM   3594  N N     . ARG A  1 483 ? 19.854  32.141  196.074 1.00 57.83  ? 483 ARG A N     1 
ATOM   3595  C CA    . ARG A  1 483 ? 21.036  32.969  196.307 1.00 57.57  ? 483 ARG A CA    1 
ATOM   3596  C C     . ARG A  1 483 ? 22.309  32.246  195.861 1.00 56.86  ? 483 ARG A C     1 
ATOM   3597  O O     . ARG A  1 483 ? 23.310  32.879  195.522 1.00 57.33  ? 483 ARG A O     1 
ATOM   3598  C CB    . ARG A  1 483 ? 21.137  33.366  197.783 1.00 55.20  ? 483 ARG A CB    1 
ATOM   3599  C CG    . ARG A  1 483 ? 22.218  34.396  198.057 1.00 59.38  ? 483 ARG A CG    1 
ATOM   3600  C CD    . ARG A  1 483 ? 22.337  34.734  199.530 1.00 56.81  ? 483 ARG A CD    1 
ATOM   3601  N NE    . ARG A  1 483 ? 21.186  35.484  200.018 1.00 56.08  ? 483 ARG A NE    1 
ATOM   3602  C CZ    . ARG A  1 483 ? 21.012  36.789  199.835 1.00 57.09  ? 483 ARG A CZ    1 
ATOM   3603  N NH1   . ARG A  1 483 ? 21.910  37.495  199.163 1.00 56.85  ? 483 ARG A NH1   1 
ATOM   3604  N NH2   . ARG A  1 483 ? 19.935  37.388  200.320 1.00 55.53  ? 483 ARG A NH2   1 
ATOM   3605  N N     . SER A  1 484 ? 22.249  30.917  195.846 1.00 55.34  ? 484 SER A N     1 
ATOM   3606  C CA    . SER A  1 484 ? 23.352  30.078  195.386 1.00 54.14  ? 484 SER A CA    1 
ATOM   3607  C C     . SER A  1 484 ? 23.820  30.419  193.971 1.00 54.06  ? 484 SER A C     1 
ATOM   3608  O O     . SER A  1 484 ? 24.955  30.850  193.775 1.00 51.90  ? 484 SER A O     1 
ATOM   3609  C CB    . SER A  1 484 ? 22.948  28.603  195.442 1.00 57.63  ? 484 SER A CB    1 
ATOM   3610  O OG    . SER A  1 484 ? 23.799  27.817  194.625 1.00 55.40  ? 484 SER A OG    1 
ATOM   3611  N N     . TRP A  1 485 ? 22.953  30.208  192.986 1.00 54.91  ? 485 TRP A N     1 
ATOM   3612  C CA    . TRP A  1 485 ? 23.306  30.501  191.601 1.00 50.43  ? 485 TRP A CA    1 
ATOM   3613  C C     . TRP A  1 485 ? 23.157  31.983  191.290 1.00 51.28  ? 485 TRP A C     1 
ATOM   3614  O O     . TRP A  1 485 ? 23.821  32.508  190.397 1.00 49.85  ? 485 TRP A O     1 
ATOM   3615  C CB    . TRP A  1 485 ? 22.456  29.674  190.632 1.00 47.98  ? 485 TRP A CB    1 
ATOM   3616  C CG    . TRP A  1 485 ? 20.989  29.679  190.941 1.00 52.13  ? 485 TRP A CG    1 
ATOM   3617  C CD1   . TRP A  1 485 ? 20.068  30.611  190.554 1.00 49.77  ? 485 TRP A CD1   1 
ATOM   3618  C CD2   . TRP A  1 485 ? 20.269  28.692  191.691 1.00 52.78  ? 485 TRP A CD2   1 
ATOM   3619  N NE1   . TRP A  1 485 ? 18.822  30.268  191.024 1.00 48.60  ? 485 TRP A NE1   1 
ATOM   3620  C CE2   . TRP A  1 485 ? 18.918  29.094  191.723 1.00 53.79  ? 485 TRP A CE2   1 
ATOM   3621  C CE3   . TRP A  1 485 ? 20.637  27.510  192.339 1.00 54.05  ? 485 TRP A CE3   1 
ATOM   3622  C CZ2   . TRP A  1 485 ? 17.936  28.355  192.378 1.00 51.26  ? 485 TRP A CZ2   1 
ATOM   3623  C CZ3   . TRP A  1 485 ? 19.661  26.780  192.990 1.00 56.18  ? 485 TRP A CZ3   1 
ATOM   3624  C CH2   . TRP A  1 485 ? 18.327  27.206  193.005 1.00 52.44  ? 485 TRP A CH2   1 
ATOM   3625  N N     . GLY A  1 486 ? 22.281  32.652  192.033 1.00 46.89  ? 486 GLY A N     1 
ATOM   3626  C CA    . GLY A  1 486 ? 22.033  34.068  191.833 1.00 46.38  ? 486 GLY A CA    1 
ATOM   3627  C C     . GLY A  1 486 ? 23.286  34.908  191.989 1.00 47.91  ? 486 GLY A C     1 
ATOM   3628  O O     . GLY A  1 486 ? 23.617  35.714  191.121 1.00 49.62  ? 486 GLY A O     1 
ATOM   3629  N N     . GLU A  1 487 ? 23.996  34.713  193.095 1.00 47.79  ? 487 GLU A N     1 
ATOM   3630  C CA    . GLU A  1 487 ? 25.220  35.463  193.353 1.00 46.21  ? 487 GLU A CA    1 
ATOM   3631  C C     . GLU A  1 487 ? 26.377  34.962  192.488 1.00 46.83  ? 487 GLU A C     1 
ATOM   3632  O O     . GLU A  1 487 ? 27.352  35.676  192.270 1.00 50.99  ? 487 GLU A O     1 
ATOM   3633  C CB    . GLU A  1 487 ? 25.585  35.389  194.836 1.00 47.57  ? 487 GLU A CB    1 
ATOM   3634  C CG    . GLU A  1 487 ? 24.504  35.947  195.756 1.00 52.09  ? 487 GLU A CG    1 
ATOM   3635  C CD    . GLU A  1 487 ? 25.023  36.266  197.142 1.00 53.39  ? 487 GLU A CD    1 
ATOM   3636  O OE1   . GLU A  1 487 ? 25.989  35.607  197.582 1.00 56.55  ? 487 GLU A OE1   1 
ATOM   3637  O OE2   . GLU A  1 487 ? 24.469  37.180  197.789 1.00 56.22  ? 487 GLU A OE2   1 
ATOM   3638  N N     . SER A  1 488 ? 26.266  33.734  191.992 1.00 46.71  ? 488 SER A N     1 
ATOM   3639  C CA    . SER A  1 488 ? 27.266  33.205  191.071 1.00 45.94  ? 488 SER A CA    1 
ATOM   3640  C C     . SER A  1 488 ? 27.184  33.932  189.732 1.00 44.25  ? 488 SER A C     1 
ATOM   3641  O O     . SER A  1 488 ? 28.203  34.261  189.122 1.00 45.05  ? 488 SER A O     1 
ATOM   3642  C CB    . SER A  1 488 ? 27.078  31.702  190.869 1.00 46.52  ? 488 SER A CB    1 
ATOM   3643  O OG    . SER A  1 488 ? 28.127  31.160  190.084 1.00 53.78  ? 488 SER A OG    1 
ATOM   3644  N N     . TYR A  1 489 ? 25.957  34.184  189.287 1.00 42.84  ? 489 TYR A N     1 
ATOM   3645  C CA    . TYR A  1 489 ? 25.721  34.890  188.035 1.00 38.32  ? 489 TYR A CA    1 
ATOM   3646  C C     . TYR A  1 489 ? 25.867  36.399  188.173 1.00 35.81  ? 489 TYR A C     1 
ATOM   3647  O O     . TYR A  1 489 ? 26.379  37.057  187.271 1.00 36.25  ? 489 TYR A O     1 
ATOM   3648  C CB    . TYR A  1 489 ? 24.321  34.592  187.496 1.00 38.80  ? 489 TYR A CB    1 
ATOM   3649  C CG    . TYR A  1 489 ? 24.072  33.163  187.083 1.00 39.24  ? 489 TYR A CG    1 
ATOM   3650  C CD1   . TYR A  1 489 ? 25.088  32.375  186.559 1.00 38.72  ? 489 TYR A CD1   1 
ATOM   3651  C CD2   . TYR A  1 489 ? 22.806  32.604  187.210 1.00 37.94  ? 489 TYR A CD2   1 
ATOM   3652  C CE1   . TYR A  1 489 ? 24.848  31.063  186.177 1.00 34.30  ? 489 TYR A CE1   1 
ATOM   3653  C CE2   . TYR A  1 489 ? 22.558  31.300  186.835 1.00 39.02  ? 489 TYR A CE2   1 
ATOM   3654  C CZ    . TYR A  1 489 ? 23.581  30.532  186.320 1.00 41.32  ? 489 TYR A CZ    1 
ATOM   3655  O OH    . TYR A  1 489 ? 23.331  29.231  185.945 1.00 43.33  ? 489 TYR A OH    1 
ATOM   3656  N N     . PHE A  1 490 ? 25.395  36.950  189.289 1.00 38.87  ? 490 PHE A N     1 
ATOM   3657  C CA    . PHE A  1 490 ? 25.210  38.394  189.383 1.00 35.55  ? 490 PHE A CA    1 
ATOM   3658  C C     . PHE A  1 490 ? 25.910  39.045  190.572 1.00 40.22  ? 490 PHE A C     1 
ATOM   3659  O O     . PHE A  1 490 ? 25.921  40.271  190.677 1.00 40.20  ? 490 PHE A O     1 
ATOM   3660  C CB    . PHE A  1 490 ? 23.714  38.723  189.438 1.00 38.74  ? 490 PHE A CB    1 
ATOM   3661  C CG    . PHE A  1 490 ? 22.903  38.016  188.391 1.00 36.37  ? 490 PHE A CG    1 
ATOM   3662  C CD1   . PHE A  1 490 ? 23.011  38.371  187.057 1.00 37.09  ? 490 PHE A CD1   1 
ATOM   3663  C CD2   . PHE A  1 490 ? 22.033  36.995  188.741 1.00 35.47  ? 490 PHE A CD2   1 
ATOM   3664  C CE1   . PHE A  1 490 ? 22.270  37.721  186.089 1.00 38.21  ? 490 PHE A CE1   1 
ATOM   3665  C CE2   . PHE A  1 490 ? 21.287  36.341  187.776 1.00 35.05  ? 490 PHE A CE2   1 
ATOM   3666  C CZ    . PHE A  1 490 ? 21.407  36.703  186.448 1.00 34.45  ? 490 PHE A CZ    1 
ATOM   3667  N N     . LEU A  1 491 ? 26.495  38.234  191.451 1.00 41.41  ? 491 LEU A N     1 
ATOM   3668  C CA    . LEU A  1 491 ? 27.124  38.730  192.678 1.00 41.86  ? 491 LEU A CA    1 
ATOM   3669  C C     . LEU A  1 491 ? 26.185  39.649  193.461 1.00 44.05  ? 491 LEU A C     1 
ATOM   3670  O O     . LEU A  1 491 ? 25.059  39.265  193.780 1.00 50.26  ? 491 LEU A O     1 
ATOM   3671  C CB    . LEU A  1 491 ? 28.441  39.443  192.359 1.00 40.49  ? 491 LEU A CB    1 
ATOM   3672  C CG    . LEU A  1 491 ? 29.570  38.506  191.914 1.00 45.12  ? 491 LEU A CG    1 
ATOM   3673  C CD1   . LEU A  1 491 ? 30.812  39.280  191.492 1.00 35.16  ? 491 LEU A CD1   1 
ATOM   3674  C CD2   . LEU A  1 491 ? 29.908  37.516  193.019 1.00 42.71  ? 491 LEU A CD2   1 
ATOM   3675  N N     . SER A  1 492 ? 26.642  40.862  193.758 1.00 39.42  ? 492 SER A N     1 
ATOM   3676  C CA    . SER A  1 492 ? 25.863  41.796  194.568 1.00 47.63  ? 492 SER A CA    1 
ATOM   3677  C C     . SER A  1 492 ? 24.680  42.405  193.807 1.00 43.27  ? 492 SER A C     1 
ATOM   3678  O O     . SER A  1 492 ? 23.815  43.043  194.406 1.00 42.73  ? 492 SER A O     1 
ATOM   3679  C CB    . SER A  1 492 ? 26.760  42.916  195.097 1.00 47.28  ? 492 SER A CB    1 
ATOM   3680  O OG    . SER A  1 492 ? 27.242  43.728  194.042 1.00 60.43  ? 492 SER A OG    1 
ATOM   3681  N N     . ASN A  1 493 ? 24.646  42.209  192.491 1.00 39.62  ? 493 ASN A N     1 
ATOM   3682  C CA    . ASN A  1 493 ? 23.538  42.702  191.677 1.00 42.06  ? 493 ASN A CA    1 
ATOM   3683  C C     . ASN A  1 493 ? 22.267  41.882  191.888 1.00 39.71  ? 493 ASN A C     1 
ATOM   3684  O O     . ASN A  1 493 ? 21.183  42.275  191.454 1.00 40.28  ? 493 ASN A O     1 
ATOM   3685  C CB    . ASN A  1 493 ? 23.916  42.700  190.194 1.00 39.79  ? 493 ASN A CB    1 
ATOM   3686  C CG    . ASN A  1 493 ? 24.945  43.759  189.852 1.00 41.56  ? 493 ASN A CG    1 
ATOM   3687  O OD1   . ASN A  1 493 ? 24.996  44.817  190.480 1.00 38.89  ? 493 ASN A OD1   1 
ATOM   3688  N ND2   . ASN A  1 493 ? 25.770  43.482  188.848 1.00 38.55  ? 493 ASN A ND2   1 
ATOM   3689  N N     . TYR A  1 494 ? 22.417  40.742  192.558 1.00 38.11  ? 494 TYR A N     1 
ATOM   3690  C CA    . TYR A  1 494 ? 21.310  39.828  192.831 1.00 43.52  ? 494 TYR A CA    1 
ATOM   3691  C C     . TYR A  1 494 ? 20.169  40.499  193.594 1.00 43.37  ? 494 TYR A C     1 
ATOM   3692  O O     . TYR A  1 494 ? 18.994  40.242  193.326 1.00 46.06  ? 494 TYR A O     1 
ATOM   3693  C CB    . TYR A  1 494 ? 21.826  38.616  193.611 1.00 42.15  ? 494 TYR A CB    1 
ATOM   3694  C CG    . TYR A  1 494 ? 20.769  37.597  193.978 1.00 48.37  ? 494 TYR A CG    1 
ATOM   3695  C CD1   . TYR A  1 494 ? 20.104  36.873  192.998 1.00 46.82  ? 494 TYR A CD1   1 
ATOM   3696  C CD2   . TYR A  1 494 ? 20.457  37.340  195.307 1.00 49.07  ? 494 TYR A CD2   1 
ATOM   3697  C CE1   . TYR A  1 494 ? 19.146  35.934  193.328 1.00 48.33  ? 494 TYR A CE1   1 
ATOM   3698  C CE2   . TYR A  1 494 ? 19.503  36.401  195.648 1.00 52.45  ? 494 TYR A CE2   1 
ATOM   3699  C CZ    . TYR A  1 494 ? 18.851  35.702  194.656 1.00 52.35  ? 494 TYR A CZ    1 
ATOM   3700  O OH    . TYR A  1 494 ? 17.897  34.769  194.988 1.00 51.46  ? 494 TYR A OH    1 
ATOM   3701  N N     . GLU A  1 495 ? 20.524  41.364  194.538 1.00 41.84  ? 495 GLU A N     1 
ATOM   3702  C CA    . GLU A  1 495 ? 19.538  42.041  195.375 1.00 41.61  ? 495 GLU A CA    1 
ATOM   3703  C C     . GLU A  1 495 ? 18.671  43.026  194.585 1.00 45.42  ? 495 GLU A C     1 
ATOM   3704  O O     . GLU A  1 495 ? 17.456  43.083  194.778 1.00 47.23  ? 495 GLU A O     1 
ATOM   3705  C CB    . GLU A  1 495 ? 20.232  42.770  196.527 1.00 44.11  ? 495 GLU A CB    1 
ATOM   3706  C CG    . GLU A  1 495 ? 21.147  41.892  197.373 1.00 46.79  ? 495 GLU A CG    1 
ATOM   3707  C CD    . GLU A  1 495 ? 20.386  40.941  198.281 1.00 51.65  ? 495 GLU A CD    1 
ATOM   3708  O OE1   . GLU A  1 495 ? 19.143  41.050  198.363 1.00 46.81  ? 495 GLU A OE1   1 
ATOM   3709  O OE2   . GLU A  1 495 ? 21.033  40.084  198.920 1.00 55.57  ? 495 GLU A OE2   1 
ATOM   3710  N N     . ARG A  1 496 ? 19.294  43.802  193.702 1.00 40.83  ? 496 ARG A N     1 
ATOM   3711  C CA    . ARG A  1 496 ? 18.557  44.781  192.905 1.00 44.22  ? 496 ARG A CA    1 
ATOM   3712  C C     . ARG A  1 496 ? 17.652  44.084  191.895 1.00 40.42  ? 496 ARG A C     1 
ATOM   3713  O O     . ARG A  1 496 ? 16.568  44.574  191.572 1.00 39.33  ? 496 ARG A O     1 
ATOM   3714  C CB    . ARG A  1 496 ? 19.513  45.734  192.186 1.00 41.26  ? 496 ARG A CB    1 
ATOM   3715  C CG    . ARG A  1 496 ? 18.807  46.893  191.491 1.00 39.50  ? 496 ARG A CG    1 
ATOM   3716  C CD    . ARG A  1 496 ? 19.788  47.821  190.786 1.00 40.39  ? 496 ARG A CD    1 
ATOM   3717  N NE    . ARG A  1 496 ? 19.103  48.861  190.021 1.00 41.76  ? 496 ARG A NE    1 
ATOM   3718  C CZ    . ARG A  1 496 ? 19.713  49.709  189.199 1.00 40.29  ? 496 ARG A CZ    1 
ATOM   3719  N NH1   . ARG A  1 496 ? 21.026  49.640  189.028 1.00 40.12  ? 496 ARG A NH1   1 
ATOM   3720  N NH2   . ARG A  1 496 ? 19.010  50.621  188.542 1.00 41.51  ? 496 ARG A NH2   1 
ATOM   3721  N N     . LEU A  1 497 ? 18.108  42.937  191.403 1.00 36.96  ? 497 LEU A N     1 
ATOM   3722  C CA    . LEU A  1 497 ? 17.339  42.141  190.453 1.00 41.33  ? 497 LEU A CA    1 
ATOM   3723  C C     . LEU A  1 497 ? 16.022  41.662  191.052 1.00 42.34  ? 497 LEU A C     1 
ATOM   3724  O O     . LEU A  1 497 ? 15.004  41.597  190.361 1.00 42.51  ? 497 LEU A O     1 
ATOM   3725  C CB    . LEU A  1 497 ? 18.157  40.941  189.977 1.00 38.54  ? 497 LEU A CB    1 
ATOM   3726  C CG    . LEU A  1 497 ? 19.297  41.247  189.004 1.00 40.58  ? 497 LEU A CG    1 
ATOM   3727  C CD1   . LEU A  1 497 ? 20.182  40.029  188.813 1.00 32.72  ? 497 LEU A CD1   1 
ATOM   3728  C CD2   . LEU A  1 497 ? 18.739  41.716  187.674 1.00 36.33  ? 497 LEU A CD2   1 
ATOM   3729  N N     . ILE A  1 498 ? 16.050  41.321  192.336 1.00 44.04  ? 498 ILE A N     1 
ATOM   3730  C CA    . ILE A  1 498 ? 14.856  40.862  193.036 1.00 44.12  ? 498 ILE A CA    1 
ATOM   3731  C C     . ILE A  1 498 ? 13.822  41.983  193.130 1.00 45.45  ? 498 ILE A C     1 
ATOM   3732  O O     . ILE A  1 498 ? 12.622  41.748  192.982 1.00 46.84  ? 498 ILE A O     1 
ATOM   3733  C CB    . ILE A  1 498 ? 15.202  40.341  194.449 1.00 42.32  ? 498 ILE A CB    1 
ATOM   3734  C CG1   . ILE A  1 498 ? 16.084  39.097  194.351 1.00 42.37  ? 498 ILE A CG1   1 
ATOM   3735  C CG2   . ILE A  1 498 ? 13.938  40.020  195.234 1.00 47.13  ? 498 ILE A CG2   1 
ATOM   3736  C CD1   . ILE A  1 498 ? 16.599  38.607  195.680 1.00 46.28  ? 498 ILE A CD1   1 
ATOM   3737  N N     . ARG A  1 499 ? 14.293  43.205  193.356 1.00 43.72  ? 499 ARG A N     1 
ATOM   3738  C CA    . ARG A  1 499 ? 13.407  44.362  193.393 1.00 43.63  ? 499 ARG A CA    1 
ATOM   3739  C C     . ARG A  1 499 ? 12.788  44.627  192.025 1.00 45.44  ? 499 ARG A C     1 
ATOM   3740  O O     . ARG A  1 499 ? 11.591  44.907  191.915 1.00 46.66  ? 499 ARG A O     1 
ATOM   3741  C CB    . ARG A  1 499 ? 14.158  45.606  193.878 1.00 39.02  ? 499 ARG A CB    1 
ATOM   3742  C CG    . ARG A  1 499 ? 13.309  46.868  193.881 1.00 41.48  ? 499 ARG A CG    1 
ATOM   3743  C CD    . ARG A  1 499 ? 13.824  47.907  194.868 1.00 45.67  ? 499 ARG A CD    1 
ATOM   3744  N NE    . ARG A  1 499 ? 15.184  48.337  194.560 1.00 46.45  ? 499 ARG A NE    1 
ATOM   3745  C CZ    . ARG A  1 499 ? 15.493  49.403  193.827 1.00 50.60  ? 499 ARG A CZ    1 
ATOM   3746  N NH1   . ARG A  1 499 ? 14.540  50.173  193.315 1.00 44.69  ? 499 ARG A NH1   1 
ATOM   3747  N NH2   . ARG A  1 499 ? 16.766  49.702  193.608 1.00 50.89  ? 499 ARG A NH2   1 
ATOM   3748  N N     . ALA A  1 500 ? 13.611  44.532  190.985 1.00 36.32  ? 500 ALA A N     1 
ATOM   3749  C CA    . ALA A  1 500 ? 13.153  44.739  189.617 1.00 38.61  ? 500 ALA A CA    1 
ATOM   3750  C C     . ALA A  1 500 ? 12.144  43.668  189.222 1.00 42.92  ? 500 ALA A C     1 
ATOM   3751  O O     . ALA A  1 500 ? 11.177  43.941  188.511 1.00 37.76  ? 500 ALA A O     1 
ATOM   3752  C CB    . ALA A  1 500 ? 14.331  44.739  188.660 1.00 33.70  ? 500 ALA A CB    1 
ATOM   3753  N N     . LYS A  1 501 ? 12.382  42.447  189.690 1.00 40.85  ? 501 LYS A N     1 
ATOM   3754  C CA    . LYS A  1 501 ? 11.458  41.336  189.481 1.00 39.94  ? 501 LYS A CA    1 
ATOM   3755  C C     . LYS A  1 501 ? 10.102  41.620  190.121 1.00 46.49  ? 501 LYS A C     1 
ATOM   3756  O O     . LYS A  1 501 ? 9.054   41.304  189.556 1.00 42.49  ? 501 LYS A O     1 
ATOM   3757  C CB    . LYS A  1 501 ? 12.054  40.046  190.052 1.00 38.38  ? 501 LYS A CB    1 
ATOM   3758  C CG    . LYS A  1 501 ? 11.107  38.854  190.081 1.00 44.11  ? 501 LYS A CG    1 
ATOM   3759  C CD    . LYS A  1 501 ? 10.787  38.338  188.684 1.00 40.20  ? 501 LYS A CD    1 
ATOM   3760  C CE    . LYS A  1 501 ? 9.853   37.131  188.742 1.00 37.99  ? 501 LYS A CE    1 
ATOM   3761  N NZ    . LYS A  1 501 ? 9.593   36.545  187.394 1.00 35.53  ? 501 LYS A NZ    1 
ATOM   3762  N N     . THR A  1 502 ? 10.136  42.225  191.304 1.00 44.39  ? 502 THR A N     1 
ATOM   3763  C CA    . THR A  1 502 ? 8.925   42.524  192.059 1.00 41.97  ? 502 THR A CA    1 
ATOM   3764  C C     . THR A  1 502 ? 8.149   43.678  191.421 1.00 45.42  ? 502 THR A C     1 
ATOM   3765  O O     . THR A  1 502 ? 6.925   43.741  191.513 1.00 42.81  ? 502 THR A O     1 
ATOM   3766  C CB    . THR A  1 502 ? 9.261   42.861  193.527 1.00 45.40  ? 502 THR A CB    1 
ATOM   3767  O OG1   . THR A  1 502 ? 10.050  41.805  194.089 1.00 46.00  ? 502 THR A OG1   1 
ATOM   3768  C CG2   . THR A  1 502 ? 7.994   43.020  194.351 1.00 46.11  ? 502 THR A CG2   1 
ATOM   3769  N N     . LEU A  1 503 ? 8.869   44.581  190.761 1.00 44.29  ? 503 LEU A N     1 
ATOM   3770  C CA    . LEU A  1 503 ? 8.242   45.699  190.063 1.00 41.43  ? 503 LEU A CA    1 
ATOM   3771  C C     . LEU A  1 503 ? 7.479   45.248  188.819 1.00 40.11  ? 503 LEU A C     1 
ATOM   3772  O O     . LEU A  1 503 ? 6.395   45.756  188.530 1.00 46.34  ? 503 LEU A O     1 
ATOM   3773  C CB    . LEU A  1 503 ? 9.290   46.746  189.664 1.00 38.10  ? 503 LEU A CB    1 
ATOM   3774  C CG    . LEU A  1 503 ? 9.755   47.788  190.690 1.00 44.36  ? 503 LEU A CG    1 
ATOM   3775  C CD1   . LEU A  1 503 ? 10.972  48.545  190.177 1.00 44.55  ? 503 LEU A CD1   1 
ATOM   3776  C CD2   . LEU A  1 503 ? 8.633   48.761  191.022 1.00 46.92  ? 503 LEU A CD2   1 
ATOM   3777  N N     . ILE A  1 504 ? 8.048   44.294  188.087 1.00 43.61  ? 504 ILE A N     1 
ATOM   3778  C CA    . ILE A  1 504 ? 7.541   43.951  186.761 1.00 41.25  ? 504 ILE A CA    1 
ATOM   3779  C C     . ILE A  1 504 ? 6.788   42.617  186.712 1.00 32.57  ? 504 ILE A C     1 
ATOM   3780  O O     . ILE A  1 504 ? 5.929   42.420  185.852 1.00 42.33  ? 504 ILE A O     1 
ATOM   3781  C CB    . ILE A  1 504 ? 8.697   43.920  185.726 1.00 34.01  ? 504 ILE A CB    1 
ATOM   3782  C CG1   . ILE A  1 504 ? 8.156   44.084  184.303 1.00 37.89  ? 504 ILE A CG1   1 
ATOM   3783  C CG2   . ILE A  1 504 ? 9.544   42.662  185.872 1.00 31.80  ? 504 ILE A CG2   1 
ATOM   3784  C CD1   . ILE A  1 504 ? 7.477   45.414  184.070 1.00 28.81  ? 504 ILE A CD1   1 
ATOM   3785  N N     . ASP A  1 505 ? 7.093   41.709  187.635 1.00 38.98  ? 505 ASP A N     1 
ATOM   3786  C CA    . ASP A  1 505 ? 6.443   40.398  187.651 1.00 37.89  ? 505 ASP A CA    1 
ATOM   3787  C C     . ASP A  1 505 ? 6.289   39.848  189.072 1.00 36.92  ? 505 ASP A C     1 
ATOM   3788  O O     . ASP A  1 505 ? 6.826   38.788  189.390 1.00 40.65  ? 505 ASP A O     1 
ATOM   3789  C CB    . ASP A  1 505 ? 7.235   39.411  186.785 1.00 36.00  ? 505 ASP A CB    1 
ATOM   3790  C CG    . ASP A  1 505 ? 6.510   38.092  186.574 1.00 42.26  ? 505 ASP A CG    1 
ATOM   3791  O OD1   . ASP A  1 505 ? 5.260   38.067  186.622 1.00 39.21  ? 505 ASP A OD1   1 
ATOM   3792  O OD2   . ASP A  1 505 ? 7.200   37.074  186.351 1.00 34.86  ? 505 ASP A OD2   1 
ATOM   3793  N N     . PRO A  1 506 ? 5.543   40.563  189.931 1.00 39.74  ? 506 PRO A N     1 
ATOM   3794  C CA    . PRO A  1 506 ? 5.429   40.140  191.333 1.00 43.57  ? 506 PRO A CA    1 
ATOM   3795  C C     . PRO A  1 506 ? 4.770   38.773  191.522 1.00 45.97  ? 506 PRO A C     1 
ATOM   3796  O O     . PRO A  1 506 ? 5.062   38.094  192.506 1.00 46.06  ? 506 PRO A O     1 
ATOM   3797  C CB    . PRO A  1 506 ? 4.565   41.240  191.959 1.00 45.32  ? 506 PRO A CB    1 
ATOM   3798  C CG    . PRO A  1 506 ? 3.820   41.838  190.821 1.00 45.47  ? 506 PRO A CG    1 
ATOM   3799  C CD    . PRO A  1 506 ? 4.758   41.780  189.659 1.00 41.88  ? 506 PRO A CD    1 
ATOM   3800  N N     . ASN A  1 507 ? 3.897   38.379  190.600 1.00 41.02  ? 507 ASN A N     1 
ATOM   3801  C CA    . ASN A  1 507 ? 3.209   37.095  190.711 1.00 40.56  ? 507 ASN A CA    1 
ATOM   3802  C C     . ASN A  1 507 ? 3.984   35.962  190.043 1.00 41.96  ? 507 ASN A C     1 
ATOM   3803  O O     . ASN A  1 507 ? 3.506   34.830  189.981 1.00 44.94  ? 507 ASN A O     1 
ATOM   3804  C CB    . ASN A  1 507 ? 1.802   37.191  190.119 1.00 43.78  ? 507 ASN A CB    1 
ATOM   3805  C CG    . ASN A  1 507 ? 0.927   38.185  190.860 1.00 46.15  ? 507 ASN A CG    1 
ATOM   3806  O OD1   . ASN A  1 507 ? 0.407   39.133  190.272 1.00 49.34  ? 507 ASN A OD1   1 
ATOM   3807  N ND2   . ASN A  1 507 ? 0.766   37.974  192.161 1.00 53.02  ? 507 ASN A ND2   1 
ATOM   3808  N N     . ASN A  1 508 ? 5.176   36.284  189.542 1.00 43.36  ? 508 ASN A N     1 
ATOM   3809  C CA    . ASN A  1 508 ? 6.101   35.297  188.983 1.00 42.87  ? 508 ASN A CA    1 
ATOM   3810  C C     . ASN A  1 508 ? 5.508   34.494  187.825 1.00 41.95  ? 508 ASN A C     1 
ATOM   3811  O O     . ASN A  1 508 ? 5.623   33.269  187.783 1.00 38.97  ? 508 ASN A O     1 
ATOM   3812  C CB    . ASN A  1 508 ? 6.577   34.346  190.084 1.00 40.83  ? 508 ASN A CB    1 
ATOM   3813  C CG    . ASN A  1 508 ? 7.902   33.687  189.758 1.00 43.35  ? 508 ASN A CG    1 
ATOM   3814  O OD1   . ASN A  1 508 ? 8.695   34.213  188.979 1.00 42.85  ? 508 ASN A OD1   1 
ATOM   3815  N ND2   . ASN A  1 508 ? 8.150   32.530  190.359 1.00 46.30  ? 508 ASN A ND2   1 
ATOM   3816  N N     . VAL A  1 509 ? 4.874   35.192  186.889 1.00 38.35  ? 509 VAL A N     1 
ATOM   3817  C CA    . VAL A  1 509 ? 4.319   34.558  185.698 1.00 34.58  ? 509 VAL A CA    1 
ATOM   3818  C C     . VAL A  1 509 ? 5.449   34.019  184.822 1.00 40.73  ? 509 VAL A C     1 
ATOM   3819  O O     . VAL A  1 509 ? 5.312   32.977  184.179 1.00 39.94  ? 509 VAL A O     1 
ATOM   3820  C CB    . VAL A  1 509 ? 3.434   35.547  184.901 1.00 33.86  ? 509 VAL A CB    1 
ATOM   3821  C CG1   . VAL A  1 509 ? 3.032   34.970  183.552 1.00 38.19  ? 509 VAL A CG1   1 
ATOM   3822  C CG2   . VAL A  1 509 ? 2.198   35.910  185.714 1.00 37.34  ? 509 VAL A CG2   1 
ATOM   3823  N N     . PHE A  1 510 ? 6.576   34.726  184.822 1.00 33.57  ? 510 PHE A N     1 
ATOM   3824  C CA    . PHE A  1 510 ? 7.737   34.312  184.045 1.00 33.98  ? 510 PHE A CA    1 
ATOM   3825  C C     . PHE A  1 510 ? 8.785   33.677  184.949 1.00 37.74  ? 510 PHE A C     1 
ATOM   3826  O O     . PHE A  1 510 ? 9.509   34.371  185.665 1.00 38.02  ? 510 PHE A O     1 
ATOM   3827  C CB    . PHE A  1 510 ? 8.325   35.502  183.287 1.00 31.29  ? 510 PHE A CB    1 
ATOM   3828  C CG    . PHE A  1 510 ? 7.369   36.118  182.310 1.00 33.96  ? 510 PHE A CG    1 
ATOM   3829  C CD1   . PHE A  1 510 ? 7.312   35.670  180.999 1.00 30.59  ? 510 PHE A CD1   1 
ATOM   3830  C CD2   . PHE A  1 510 ? 6.511   37.131  182.706 1.00 33.38  ? 510 PHE A CD2   1 
ATOM   3831  C CE1   . PHE A  1 510 ? 6.423   36.227  180.101 1.00 36.85  ? 510 PHE A CE1   1 
ATOM   3832  C CE2   . PHE A  1 510 ? 5.620   37.691  181.813 1.00 36.02  ? 510 PHE A CE2   1 
ATOM   3833  C CZ    . PHE A  1 510 ? 5.576   37.240  180.507 1.00 32.35  ? 510 PHE A CZ    1 
ATOM   3834  N N     . ASN A  1 511 ? 8.856   32.350  184.911 1.00 36.82  ? 511 ASN A N     1 
ATOM   3835  C CA    . ASN A  1 511 ? 9.736   31.602  185.800 1.00 37.20  ? 511 ASN A CA    1 
ATOM   3836  C C     . ASN A  1 511 ? 10.363  30.376  185.140 1.00 35.66  ? 511 ASN A C     1 
ATOM   3837  O O     . ASN A  1 511 ? 9.868   29.876  184.129 1.00 38.44  ? 511 ASN A O     1 
ATOM   3838  C CB    . ASN A  1 511 ? 8.967   31.165  187.045 1.00 38.17  ? 511 ASN A CB    1 
ATOM   3839  C CG    . ASN A  1 511 ? 7.787   30.271  186.711 1.00 41.55  ? 511 ASN A CG    1 
ATOM   3840  O OD1   . ASN A  1 511 ? 7.937   29.057  186.570 1.00 43.06  ? 511 ASN A OD1   1 
ATOM   3841  N ND2   . ASN A  1 511 ? 6.609   30.869  186.572 1.00 38.47  ? 511 ASN A ND2   1 
ATOM   3842  N N     . HIS A  1 512 ? 11.456  29.904  185.730 1.00 36.10  ? 512 HIS A N     1 
ATOM   3843  C CA    . HIS A  1 512 ? 12.126  28.678  185.304 1.00 36.11  ? 512 HIS A CA    1 
ATOM   3844  C C     . HIS A  1 512 ? 13.060  28.269  186.459 1.00 39.32  ? 512 HIS A C     1 
ATOM   3845  O O     . HIS A  1 512 ? 13.140  29.000  187.445 1.00 38.97  ? 512 HIS A O     1 
ATOM   3846  C CB    . HIS A  1 512 ? 12.852  28.889  183.959 1.00 34.05  ? 512 HIS A CB    1 
ATOM   3847  C CG    . HIS A  1 512 ? 13.976  29.875  184.008 1.00 42.52  ? 512 HIS A CG    1 
ATOM   3848  N ND1   . HIS A  1 512 ? 15.174  29.610  184.638 1.00 35.58  ? 512 HIS A ND1   1 
ATOM   3849  C CD2   . HIS A  1 512 ? 14.100  31.111  183.471 1.00 38.88  ? 512 HIS A CD2   1 
ATOM   3850  C CE1   . HIS A  1 512 ? 15.980  30.647  184.501 1.00 37.44  ? 512 HIS A CE1   1 
ATOM   3851  N NE2   . HIS A  1 512 ? 15.353  31.571  183.796 1.00 37.84  ? 512 HIS A NE2   1 
ATOM   3852  N N     . PRO A  1 513 ? 13.735  27.100  186.376 1.00 35.59  ? 513 PRO A N     1 
ATOM   3853  C CA    . PRO A  1 513 ? 14.497  26.638  187.550 1.00 40.88  ? 513 PRO A CA    1 
ATOM   3854  C C     . PRO A  1 513 ? 15.477  27.622  188.210 1.00 45.37  ? 513 PRO A C     1 
ATOM   3855  O O     . PRO A  1 513 ? 15.814  27.418  189.376 1.00 45.86  ? 513 PRO A O     1 
ATOM   3856  C CB    . PRO A  1 513 ? 15.279  25.446  186.993 1.00 41.11  ? 513 PRO A CB    1 
ATOM   3857  C CG    . PRO A  1 513 ? 14.384  24.882  185.974 1.00 42.67  ? 513 PRO A CG    1 
ATOM   3858  C CD    . PRO A  1 513 ? 13.693  26.056  185.332 1.00 37.37  ? 513 PRO A CD    1 
ATOM   3859  N N     . GLN A  1 514 ? 15.930  28.653  187.505 1.00 40.45  ? 514 GLN A N     1 
ATOM   3860  C CA    . GLN A  1 514 ? 16.894  29.577  188.098 1.00 44.03  ? 514 GLN A CA    1 
ATOM   3861  C C     . GLN A  1 514 ? 16.513  31.043  187.915 1.00 44.53  ? 514 GLN A C     1 
ATOM   3862  O O     . GLN A  1 514 ? 17.356  31.929  188.044 1.00 44.23  ? 514 GLN A O     1 
ATOM   3863  C CB    . GLN A  1 514 ? 18.289  29.324  187.523 1.00 42.37  ? 514 GLN A CB    1 
ATOM   3864  C CG    . GLN A  1 514 ? 18.930  28.037  188.018 1.00 47.11  ? 514 GLN A CG    1 
ATOM   3865  C CD    . GLN A  1 514 ? 20.330  27.845  187.477 1.00 47.78  ? 514 GLN A CD    1 
ATOM   3866  O OE1   . GLN A  1 514 ? 20.776  28.593  186.612 1.00 47.45  ? 514 GLN A OE1   1 
ATOM   3867  N NE2   . GLN A  1 514 ? 21.034  26.844  187.988 1.00 49.28  ? 514 GLN A NE2   1 
ATOM   3868  N N     . SER A  1 515 ? 15.239  31.296  187.630 1.00 38.95  ? 515 SER A N     1 
ATOM   3869  C CA    . SER A  1 515 ? 14.758  32.663  187.457 1.00 39.91  ? 515 SER A CA    1 
ATOM   3870  C C     . SER A  1 515 ? 14.820  33.443  188.766 1.00 41.65  ? 515 SER A C     1 
ATOM   3871  O O     . SER A  1 515 ? 14.693  32.866  189.846 1.00 48.48  ? 515 SER A O     1 
ATOM   3872  C CB    . SER A  1 515 ? 13.329  32.667  186.913 1.00 40.40  ? 515 SER A CB    1 
ATOM   3873  O OG    . SER A  1 515 ? 12.427  32.076  187.834 1.00 39.73  ? 515 SER A OG    1 
ATOM   3874  N N     . ILE A  1 516 ? 15.021  34.756  188.659 1.00 38.07  ? 516 ILE A N     1 
ATOM   3875  C CA    . ILE A  1 516 ? 15.065  35.638  189.824 1.00 36.43  ? 516 ILE A CA    1 
ATOM   3876  C C     . ILE A  1 516 ? 13.726  35.658  190.554 1.00 45.23  ? 516 ILE A C     1 
ATOM   3877  O O     . ILE A  1 516 ? 12.691  35.948  189.953 1.00 41.67  ? 516 ILE A O     1 
ATOM   3878  C CB    . ILE A  1 516 ? 15.444  37.083  189.424 1.00 36.29  ? 516 ILE A CB    1 
ATOM   3879  C CG1   . ILE A  1 516 ? 16.835  37.118  188.781 1.00 41.62  ? 516 ILE A CG1   1 
ATOM   3880  C CG2   . ILE A  1 516 ? 15.390  38.006  190.633 1.00 33.65  ? 516 ILE A CG2   1 
ATOM   3881  C CD1   . ILE A  1 516 ? 17.962  36.802  189.743 1.00 37.52  ? 516 ILE A CD1   1 
ATOM   3882  N N     . PRO A  1 517 ? 13.740  35.339  191.855 1.00 46.46  ? 517 PRO A N     1 
ATOM   3883  C CA    . PRO A  1 517 ? 12.511  35.321  192.653 1.00 44.33  ? 517 PRO A CA    1 
ATOM   3884  C C     . PRO A  1 517 ? 12.061  36.732  193.010 1.00 45.85  ? 517 PRO A C     1 
ATOM   3885  O O     . PRO A  1 517 ? 12.906  37.617  193.134 1.00 48.66  ? 517 PRO A O     1 
ATOM   3886  C CB    . PRO A  1 517 ? 12.915  34.542  193.916 1.00 41.90  ? 517 PRO A CB    1 
ATOM   3887  C CG    . PRO A  1 517 ? 14.289  33.974  193.624 1.00 47.87  ? 517 PRO A CG    1 
ATOM   3888  C CD    . PRO A  1 517 ? 14.905  34.904  192.639 1.00 43.69  ? 517 PRO A CD    1 
ATOM   3889  N N     . PRO A  1 518 ? 10.745  36.945  193.169 1.00 41.05  ? 518 PRO A N     1 
ATOM   3890  C CA    . PRO A  1 518 ? 10.245  38.241  193.639 1.00 45.04  ? 518 PRO A CA    1 
ATOM   3891  C C     . PRO A  1 518 ? 10.530  38.414  195.127 1.00 50.64  ? 518 PRO A C     1 
ATOM   3892  O O     . PRO A  1 518 ? 11.008  37.465  195.747 1.00 54.18  ? 518 PRO A O     1 
ATOM   3893  C CB    . PRO A  1 518 ? 8.744   38.154  193.366 1.00 44.26  ? 518 PRO A CB    1 
ATOM   3894  C CG    . PRO A  1 518 ? 8.443   36.700  193.490 1.00 43.89  ? 518 PRO A CG    1 
ATOM   3895  C CD    . PRO A  1 518 ? 9.651   35.984  192.938 1.00 44.04  ? 518 PRO A CD    1 
ATOM   3896  N N     . MET A  1 519 ? 10.237  39.586  195.687 1.00 49.44  ? 519 MET A N     1 
ATOM   3897  C CA    . MET A  1 519 ? 10.552  39.870  197.089 1.00 55.82  ? 519 MET A CA    1 
ATOM   3898  C C     . MET A  1 519 ? 9.947   38.842  198.047 1.00 57.05  ? 519 MET A C     1 
ATOM   3899  O O     . MET A  1 519 ? 10.520  38.551  199.099 1.00 60.68  ? 519 MET A O     1 
ATOM   3900  C CB    . MET A  1 519 ? 10.086  41.277  197.471 1.00 56.14  ? 519 MET A CB    1 
ATOM   3901  C CG    . MET A  1 519 ? 11.029  42.377  197.013 1.00 51.60  ? 519 MET A CG    1 
ATOM   3902  S SD    . MET A  1 519 ? 10.539  44.025  197.549 1.00 57.95  ? 519 MET A SD    1 
ATOM   3903  C CE    . MET A  1 519 ? 11.798  45.014  196.744 1.00 50.53  ? 519 MET A CE    1 
ATOM   3904  N N     . ALA A  1 520 ? 8.797   38.294  197.669 1.00 58.86  ? 520 ALA A N     1 
ATOM   3905  C CA    . ALA A  1 520 ? 8.142   37.242  198.437 1.00 61.08  ? 520 ALA A CA    1 
ATOM   3906  C C     . ALA A  1 520 ? 7.159   36.476  197.554 1.00 63.72  ? 520 ALA A C     1 
ATOM   3907  O O     . ALA A  1 520 ? 7.002   36.791  196.375 1.00 62.15  ? 520 ALA A O     1 
ATOM   3908  C CB    . ALA A  1 520 ? 7.430   37.825  199.650 1.00 58.93  ? 520 ALA A CB    1 
ATOM   3909  N N     . ASN A  1 521 ? 6.508   35.466  198.124 1.00 71.36  ? 521 ASN A N     1 
ATOM   3910  C CA    . ASN A  1 521 ? 5.451   34.739  197.428 1.00 72.05  ? 521 ASN A CA    1 
ATOM   3911  C C     . ASN A  1 521 ? 4.139   35.517  197.527 1.00 73.64  ? 521 ASN A C     1 
ATOM   3912  O O     . ASN A  1 521 ? 3.558   35.630  198.606 1.00 75.01  ? 521 ASN A O     1 
ATOM   3913  C CB    . ASN A  1 521 ? 5.296   33.330  198.013 1.00 71.25  ? 521 ASN A CB    1 
ATOM   3914  C CG    . ASN A  1 521 ? 4.341   32.454  197.212 1.00 79.24  ? 521 ASN A CG    1 
ATOM   3915  O OD1   . ASN A  1 521 ? 3.534   32.942  196.420 1.00 81.63  ? 521 ASN A OD1   1 
ATOM   3916  N ND2   . ASN A  1 521 ? 4.428   31.145  197.426 1.00 77.90  ? 521 ASN A ND2   1 
ATOM   3917  N N     . PHE A  1 522 ? 3.673   36.043  196.399 1.00 72.26  ? 522 PHE A N     1 
ATOM   3918  C CA    . PHE A  1 522 ? 2.539   36.962  196.393 1.00 73.09  ? 522 PHE A CA    1 
ATOM   3919  C C     . PHE A  1 522 ? 1.232   36.351  195.889 1.00 82.72  ? 522 PHE A C     1 
ATOM   3920  O O     . PHE A  1 522 ? 0.170   36.957  196.046 1.00 83.20  ? 522 PHE A O     1 
ATOM   3921  C CB    . PHE A  1 522 ? 2.859   38.184  195.529 1.00 65.41  ? 522 PHE A CB    1 
ATOM   3922  C CG    . PHE A  1 522 ? 3.872   39.118  196.127 1.00 67.65  ? 522 PHE A CG    1 
ATOM   3923  C CD1   . PHE A  1 522 ? 3.505   40.013  197.118 1.00 66.14  ? 522 PHE A CD1   1 
ATOM   3924  C CD2   . PHE A  1 522 ? 5.181   39.129  195.672 1.00 62.65  ? 522 PHE A CD2   1 
ATOM   3925  C CE1   . PHE A  1 522 ? 4.429   40.886  197.661 1.00 66.68  ? 522 PHE A CE1   1 
ATOM   3926  C CE2   . PHE A  1 522 ? 6.111   40.001  196.212 1.00 61.98  ? 522 PHE A CE2   1 
ATOM   3927  C CZ    . PHE A  1 522 ? 5.733   40.880  197.208 1.00 62.94  ? 522 PHE A CZ    1 
ATOM   3928  N N     . ASP A  1 523 ? 1.328   35.166  195.288 1.00 94.82  ? 523 ASP A N     1 
ATOM   3929  C CA    . ASP A  1 523 ? 0.242   34.540  194.522 1.00 104.11 ? 523 ASP A CA    1 
ATOM   3930  C C     . ASP A  1 523 ? -1.165  34.767  195.075 1.00 97.49  ? 523 ASP A C     1 
ATOM   3931  O O     . ASP A  1 523 ? -1.899  35.628  194.586 1.00 87.80  ? 523 ASP A O     1 
ATOM   3932  C CB    . ASP A  1 523 ? 0.491   33.035  194.412 1.00 103.61 ? 523 ASP A CB    1 
ATOM   3933  C CG    . ASP A  1 523 ? 0.317   32.320  195.735 1.00 101.80 ? 523 ASP A CG    1 
ATOM   3934  O OD1   . ASP A  1 523 ? -0.224  31.195  195.737 1.00 102.66 ? 523 ASP A OD1   1 
ATOM   3935  O OD2   . ASP A  1 523 ? 0.716   32.886  196.775 1.00 98.26  ? 523 ASP A OD2   1 
ATOM   3936  N N     . ASN B  1 25  ? -20.126 47.452  230.243 1.00 74.10  ? 25  ASN B N     1 
ATOM   3937  C CA    . ASN B  1 25  ? -20.091 48.648  229.400 1.00 68.79  ? 25  ASN B CA    1 
ATOM   3938  C C     . ASN B  1 25  ? -20.416 48.379  227.924 1.00 56.34  ? 25  ASN B C     1 
ATOM   3939  O O     . ASN B  1 25  ? -21.275 47.548  227.610 1.00 61.18  ? 25  ASN B O     1 
ATOM   3940  C CB    . ASN B  1 25  ? -18.720 49.322  229.514 1.00 67.64  ? 25  ASN B CB    1 
ATOM   3941  C CG    . ASN B  1 25  ? -17.587 48.323  229.708 1.00 74.50  ? 25  ASN B CG    1 
ATOM   3942  O OD1   . ASN B  1 25  ? -17.778 47.240  230.264 1.00 70.90  ? 25  ASN B OD1   1 
ATOM   3943  N ND2   . ASN B  1 25  ? -16.394 48.692  229.254 1.00 76.13  ? 25  ASN B ND2   1 
ATOM   3944  N N     . ASP B  1 26  ? -19.729 49.099  227.034 1.00 55.24  ? 26  ASP B N     1 
ATOM   3945  C CA    . ASP B  1 26  ? -19.955 49.010  225.591 1.00 51.42  ? 26  ASP B CA    1 
ATOM   3946  C C     . ASP B  1 26  ? -19.032 47.972  224.956 1.00 46.23  ? 26  ASP B C     1 
ATOM   3947  O O     . ASP B  1 26  ? -18.020 48.319  224.341 1.00 41.76  ? 26  ASP B O     1 
ATOM   3948  C CB    . ASP B  1 26  ? -19.744 50.376  224.922 1.00 41.40  ? 26  ASP B CB    1 
ATOM   3949  C CG    . ASP B  1 26  ? -20.335 50.446  223.522 1.00 40.85  ? 26  ASP B CG    1 
ATOM   3950  O OD1   . ASP B  1 26  ? -20.597 49.381  222.921 1.00 47.83  ? 26  ASP B OD1   1 
ATOM   3951  O OD2   . ASP B  1 26  ? -20.533 51.573  223.026 1.00 50.77  ? 26  ASP B OD2   1 
ATOM   3952  N N     . LEU B  1 27  ? -19.403 46.702  225.090 1.00 41.80  ? 27  LEU B N     1 
ATOM   3953  C CA    . LEU B  1 27  ? -18.604 45.602  224.562 1.00 42.56  ? 27  LEU B CA    1 
ATOM   3954  C C     . LEU B  1 27  ? -18.429 45.685  223.046 1.00 45.01  ? 27  LEU B C     1 
ATOM   3955  O O     . LEU B  1 27  ? -17.344 45.424  222.523 1.00 38.74  ? 27  LEU B O     1 
ATOM   3956  C CB    . LEU B  1 27  ? -19.240 44.262  224.936 1.00 41.68  ? 27  LEU B CB    1 
ATOM   3957  C CG    . LEU B  1 27  ? -18.536 43.032  224.357 1.00 45.26  ? 27  LEU B CG    1 
ATOM   3958  C CD1   . LEU B  1 27  ? -17.132 42.894  224.929 1.00 40.41  ? 27  LEU B CD1   1 
ATOM   3959  C CD2   . LEU B  1 27  ? -19.350 41.775  224.601 1.00 42.78  ? 27  LEU B CD2   1 
ATOM   3960  N N     . LEU B  1 28  ? -19.491 46.066  222.342 1.00 36.16  ? 28  LEU B N     1 
ATOM   3961  C CA    . LEU B  1 28  ? -19.446 46.129  220.884 1.00 38.72  ? 28  LEU B CA    1 
ATOM   3962  C C     . LEU B  1 28  ? -18.513 47.229  220.377 1.00 39.81  ? 28  LEU B C     1 
ATOM   3963  O O     . LEU B  1 28  ? -17.865 47.064  219.341 1.00 38.74  ? 28  LEU B O     1 
ATOM   3964  C CB    . LEU B  1 28  ? -20.852 46.330  220.314 1.00 37.56  ? 28  LEU B CB    1 
ATOM   3965  C CG    . LEU B  1 28  ? -21.831 45.173  220.546 1.00 42.31  ? 28  LEU B CG    1 
ATOM   3966  C CD1   . LEU B  1 28  ? -23.089 45.334  219.697 1.00 38.69  ? 28  LEU B CD1   1 
ATOM   3967  C CD2   . LEU B  1 28  ? -21.164 43.833  220.273 1.00 39.61  ? 28  LEU B CD2   1 
ATOM   3968  N N     . SER B  1 29  ? -18.440 48.346  221.094 1.00 36.62  ? 29  SER B N     1 
ATOM   3969  C CA    . SER B  1 29  ? -17.524 49.411  220.704 1.00 42.94  ? 29  SER B CA    1 
ATOM   3970  C C     . SER B  1 29  ? -16.100 49.061  221.117 1.00 40.25  ? 29  SER B C     1 
ATOM   3971  O O     . SER B  1 29  ? -15.146 49.421  220.433 1.00 40.39  ? 29  SER B O     1 
ATOM   3972  C CB    . SER B  1 29  ? -17.938 50.745  221.319 1.00 43.21  ? 29  SER B CB    1 
ATOM   3973  O OG    . SER B  1 29  ? -17.345 51.833  220.628 1.00 54.16  ? 29  SER B OG    1 
ATOM   3974  N N     . CYS B  1 30  ? -15.963 48.367  222.244 1.00 38.07  ? 30  CYS B N     1 
ATOM   3975  C CA    . CYS B  1 30  ? -14.654 47.916  222.705 1.00 43.41  ? 30  CYS B CA    1 
ATOM   3976  C C     . CYS B  1 30  ? -14.018 47.027  221.650 1.00 40.26  ? 30  CYS B C     1 
ATOM   3977  O O     . CYS B  1 30  ? -12.861 47.220  221.279 1.00 36.22  ? 30  CYS B O     1 
ATOM   3978  C CB    . CYS B  1 30  ? -14.760 47.164  224.035 1.00 41.85  ? 30  CYS B CB    1 
ATOM   3979  S SG    . CYS B  1 30  ? -13.158 46.617  224.692 1.00 38.91  ? 30  CYS B SG    1 
ATOM   3980  N N     . LEU B  1 31  ? -14.793 46.063  221.162 1.00 36.52  ? 31  LEU B N     1 
ATOM   3981  C CA    . LEU B  1 31  ? -14.341 45.158  220.110 1.00 40.16  ? 31  LEU B CA    1 
ATOM   3982  C C     . LEU B  1 31  ? -13.953 45.899  218.838 1.00 37.45  ? 31  LEU B C     1 
ATOM   3983  O O     . LEU B  1 31  ? -12.917 45.610  218.241 1.00 42.06  ? 31  LEU B O     1 
ATOM   3984  C CB    . LEU B  1 31  ? -15.424 44.130  219.792 1.00 37.09  ? 31  LEU B CB    1 
ATOM   3985  C CG    . LEU B  1 31  ? -15.738 43.137  220.904 1.00 40.85  ? 31  LEU B CG    1 
ATOM   3986  C CD1   . LEU B  1 31  ? -16.902 42.268  220.483 1.00 42.29  ? 31  LEU B CD1   1 
ATOM   3987  C CD2   . LEU B  1 31  ? -14.512 42.294  221.236 1.00 35.25  ? 31  LEU B CD2   1 
ATOM   3988  N N     . THR B  1 32  ? -14.788 46.850  218.429 1.00 36.37  ? 32  THR B N     1 
ATOM   3989  C CA    . THR B  1 32  ? -14.542 47.621  217.216 1.00 40.40  ? 32  THR B CA    1 
ATOM   3990  C C     . THR B  1 32  ? -13.264 48.452  217.325 1.00 41.39  ? 32  THR B C     1 
ATOM   3991  O O     . THR B  1 32  ? -12.464 48.496  216.390 1.00 39.33  ? 32  THR B O     1 
ATOM   3992  C CB    . THR B  1 32  ? -15.726 48.554  216.890 1.00 42.34  ? 32  THR B CB    1 
ATOM   3993  O OG1   . THR B  1 32  ? -16.910 47.771  216.693 1.00 40.93  ? 32  THR B OG1   1 
ATOM   3994  C CG2   . THR B  1 32  ? -15.440 49.368  215.628 1.00 35.94  ? 32  THR B CG2   1 
ATOM   3995  N N     . PHE B  1 33  ? -13.075 49.110  218.466 1.00 37.61  ? 33  PHE B N     1 
ATOM   3996  C CA    . PHE B  1 33  ? -11.851 49.869  218.705 1.00 42.15  ? 33  PHE B CA    1 
ATOM   3997  C C     . PHE B  1 33  ? -10.640 48.943  218.790 1.00 42.19  ? 33  PHE B C     1 
ATOM   3998  O O     . PHE B  1 33  ? -9.523  49.341  218.464 1.00 42.69  ? 33  PHE B O     1 
ATOM   3999  C CB    . PHE B  1 33  ? -11.959 50.700  219.988 1.00 40.83  ? 33  PHE B CB    1 
ATOM   4000  C CG    . PHE B  1 33  ? -12.582 52.052  219.786 1.00 47.63  ? 33  PHE B CG    1 
ATOM   4001  C CD1   . PHE B  1 33  ? -11.867 53.077  219.189 1.00 46.84  ? 33  PHE B CD1   1 
ATOM   4002  C CD2   . PHE B  1 33  ? -13.878 52.301  220.201 1.00 47.11  ? 33  PHE B CD2   1 
ATOM   4003  C CE1   . PHE B  1 33  ? -12.437 54.327  219.006 1.00 51.09  ? 33  PHE B CE1   1 
ATOM   4004  C CE2   . PHE B  1 33  ? -14.455 53.547  220.022 1.00 48.71  ? 33  PHE B CE2   1 
ATOM   4005  C CZ    . PHE B  1 33  ? -13.734 54.561  219.423 1.00 47.58  ? 33  PHE B CZ    1 
ATOM   4006  N N     . ASN B  1 34  ? -10.867 47.708  219.231 1.00 40.08  ? 34  ASN B N     1 
ATOM   4007  C CA    . ASN B  1 34  ? -9.792  46.726  219.360 1.00 43.17  ? 34  ASN B CA    1 
ATOM   4008  C C     . ASN B  1 34  ? -9.551  45.946  218.073 1.00 38.72  ? 34  ASN B C     1 
ATOM   4009  O O     . ASN B  1 34  ? -8.746  45.012  218.044 1.00 43.92  ? 34  ASN B O     1 
ATOM   4010  C CB    . ASN B  1 34  ? -10.089 45.756  220.503 1.00 35.18  ? 34  ASN B CB    1 
ATOM   4011  C CG    . ASN B  1 34  ? -9.682  46.309  221.853 1.00 40.47  ? 34  ASN B CG    1 
ATOM   4012  O OD1   . ASN B  1 34  ? -8.683  45.884  222.434 1.00 42.64  ? 34  ASN B OD1   1 
ATOM   4013  N ND2   . ASN B  1 34  ? -10.448 47.267  222.357 1.00 39.19  ? 34  ASN B ND2   1 
ATOM   4014  N N     . GLY B  1 35  ? -10.244 46.333  217.007 1.00 37.73  ? 35  GLY B N     1 
ATOM   4015  C CA    . GLY B  1 35  ? -10.043 45.717  215.707 1.00 37.23  ? 35  GLY B CA    1 
ATOM   4016  C C     . GLY B  1 35  ? -10.644 44.332  215.571 1.00 44.30  ? 35  GLY B C     1 
ATOM   4017  O O     . GLY B  1 35  ? -10.248 43.552  214.704 1.00 37.92  ? 35  GLY B O     1 
ATOM   4018  N N     . VAL B  1 36  ? -11.610 44.026  216.429 1.00 32.97  ? 36  VAL B N     1 
ATOM   4019  C CA    . VAL B  1 36  ? -12.310 42.751  216.358 1.00 39.44  ? 36  VAL B CA    1 
ATOM   4020  C C     . VAL B  1 36  ? -13.712 42.972  215.798 1.00 40.85  ? 36  VAL B C     1 
ATOM   4021  O O     . VAL B  1 36  ? -14.647 43.282  216.536 1.00 34.52  ? 36  VAL B O     1 
ATOM   4022  C CB    . VAL B  1 36  ? -12.392 42.076  217.735 1.00 32.81  ? 36  VAL B CB    1 
ATOM   4023  C CG1   . VAL B  1 36  ? -12.996 40.696  217.597 1.00 32.39  ? 36  VAL B CG1   1 
ATOM   4024  C CG2   . VAL B  1 36  ? -11.005 41.999  218.372 1.00 37.05  ? 36  VAL B CG2   1 
ATOM   4025  N N     . ARG B  1 37  ? -13.848 42.810  214.486 1.00 37.75  ? 37  ARG B N     1 
ATOM   4026  C CA    . ARG B  1 37  ? -15.052 43.238  213.781 1.00 43.15  ? 37  ARG B CA    1 
ATOM   4027  C C     . ARG B  1 37  ? -16.066 42.127  213.530 1.00 42.20  ? 37  ARG B C     1 
ATOM   4028  O O     . ARG B  1 37  ? -17.256 42.401  213.373 1.00 46.06  ? 37  ARG B O     1 
ATOM   4029  C CB    . ARG B  1 37  ? -14.660 43.886  212.453 1.00 41.33  ? 37  ARG B CB    1 
ATOM   4030  C CG    . ARG B  1 37  ? -13.968 45.219  212.643 1.00 51.78  ? 37  ARG B CG    1 
ATOM   4031  C CD    . ARG B  1 37  ? -12.983 45.509  211.532 1.00 58.90  ? 37  ARG B CD    1 
ATOM   4032  N NE    . ARG B  1 37  ? -12.149 46.662  211.857 1.00 63.94  ? 37  ARG B NE    1 
ATOM   4033  C CZ    . ARG B  1 37  ? -10.825 46.624  211.980 1.00 65.54  ? 37  ARG B CZ    1 
ATOM   4034  N NH1   . ARG B  1 37  ? -10.161 47.731  212.285 1.00 63.83  ? 37  ARG B NH1   1 
ATOM   4035  N NH2   . ARG B  1 37  ? -10.164 45.489  211.791 1.00 67.85  ? 37  ARG B NH2   1 
ATOM   4036  N N     . ASN B  1 38  ? -15.611 40.879  213.492 1.00 43.33  ? 38  ASN B N     1 
ATOM   4037  C CA    . ASN B  1 38  ? -16.536 39.770  213.286 1.00 46.44  ? 38  ASN B CA    1 
ATOM   4038  C C     . ASN B  1 38  ? -17.213 39.368  214.595 1.00 41.84  ? 38  ASN B C     1 
ATOM   4039  O O     . ASN B  1 38  ? -16.777 38.442  215.280 1.00 41.45  ? 38  ASN B O     1 
ATOM   4040  C CB    . ASN B  1 38  ? -15.818 38.567  212.661 1.00 44.18  ? 38  ASN B CB    1 
ATOM   4041  C CG    . ASN B  1 38  ? -16.785 37.548  212.068 1.00 50.06  ? 38  ASN B CG    1 
ATOM   4042  O OD1   . ASN B  1 38  ? -17.849 37.284  212.629 1.00 52.11  ? 38  ASN B OD1   1 
ATOM   4043  N ND2   . ASN B  1 38  ? -16.419 36.976  210.924 1.00 51.76  ? 38  ASN B ND2   1 
ATOM   4044  N N     . HIS B  1 39  ? -18.286 40.079  214.931 1.00 38.41  ? 39  HIS B N     1 
ATOM   4045  C CA    . HIS B  1 39  ? -19.081 39.779  216.115 1.00 39.74  ? 39  HIS B CA    1 
ATOM   4046  C C     . HIS B  1 39  ? -20.563 39.988  215.818 1.00 43.36  ? 39  HIS B C     1 
ATOM   4047  O O     . HIS B  1 39  ? -20.928 40.880  215.053 1.00 46.19  ? 39  HIS B O     1 
ATOM   4048  C CB    . HIS B  1 39  ? -18.644 40.650  217.295 1.00 37.26  ? 39  HIS B CB    1 
ATOM   4049  C CG    . HIS B  1 39  ? -18.621 42.115  216.987 1.00 42.29  ? 39  HIS B CG    1 
ATOM   4050  N ND1   . HIS B  1 39  ? -17.462 42.793  216.679 1.00 45.05  ? 39  HIS B ND1   1 
ATOM   4051  C CD2   . HIS B  1 39  ? -19.618 43.030  216.933 1.00 36.08  ? 39  HIS B CD2   1 
ATOM   4052  C CE1   . HIS B  1 39  ? -17.744 44.064  216.453 1.00 41.71  ? 39  HIS B CE1   1 
ATOM   4053  N NE2   . HIS B  1 39  ? -19.046 44.233  216.599 1.00 45.52  ? 39  HIS B NE2   1 
ATOM   4054  N N     . THR B  1 40  ? -21.413 39.148  216.408 1.00 46.70  ? 40  THR B N     1 
ATOM   4055  C CA    . THR B  1 40  ? -22.864 39.237  216.221 1.00 44.64  ? 40  THR B CA    1 
ATOM   4056  C C     . THR B  1 40  ? -23.601 39.029  217.544 1.00 44.32  ? 40  THR B C     1 
ATOM   4057  O O     . THR B  1 40  ? -23.259 38.129  218.309 1.00 44.13  ? 40  THR B O     1 
ATOM   4058  C CB    . THR B  1 40  ? -23.384 38.191  215.213 1.00 46.69  ? 40  THR B CB    1 
ATOM   4059  O OG1   . THR B  1 40  ? -23.329 36.889  215.807 1.00 54.29  ? 40  THR B OG1   1 
ATOM   4060  C CG2   . THR B  1 40  ? -22.562 38.197  213.933 1.00 45.15  ? 40  THR B CG2   1 
ATOM   4061  N N     . VAL B  1 41  ? -24.620 39.844  217.805 1.00 35.83  ? 41  VAL B N     1 
ATOM   4062  C CA    . VAL B  1 41  ? -25.407 39.700  219.030 1.00 41.01  ? 41  VAL B CA    1 
ATOM   4063  C C     . VAL B  1 41  ? -26.474 38.617  218.887 1.00 42.25  ? 41  VAL B C     1 
ATOM   4064  O O     . VAL B  1 41  ? -26.779 38.180  217.776 1.00 46.66  ? 41  VAL B O     1 
ATOM   4065  C CB    . VAL B  1 41  ? -26.087 41.022  219.433 1.00 49.92  ? 41  VAL B CB    1 
ATOM   4066  C CG1   . VAL B  1 41  ? -25.057 42.131  219.544 1.00 49.10  ? 41  VAL B CG1   1 
ATOM   4067  C CG2   . VAL B  1 41  ? -27.177 41.391  218.436 1.00 46.08  ? 41  VAL B CG2   1 
ATOM   4068  N N     . PHE B  1 42  ? -27.032 38.192  220.019 1.00 41.03  ? 42  PHE B N     1 
ATOM   4069  C CA    . PHE B  1 42  ? -28.052 37.143  220.044 1.00 47.70  ? 42  PHE B CA    1 
ATOM   4070  C C     . PHE B  1 42  ? -29.258 37.476  219.170 1.00 51.03  ? 42  PHE B C     1 
ATOM   4071  O O     . PHE B  1 42  ? -29.652 38.636  219.046 1.00 48.01  ? 42  PHE B O     1 
ATOM   4072  C CB    . PHE B  1 42  ? -28.514 36.884  221.487 1.00 45.42  ? 42  PHE B CB    1 
ATOM   4073  C CG    . PHE B  1 42  ? -29.684 35.931  221.599 1.00 48.75  ? 42  PHE B CG    1 
ATOM   4074  C CD1   . PHE B  1 42  ? -29.476 34.566  221.714 1.00 47.38  ? 42  PHE B CD1   1 
ATOM   4075  C CD2   . PHE B  1 42  ? -30.990 36.402  221.600 1.00 52.99  ? 42  PHE B CD2   1 
ATOM   4076  C CE1   . PHE B  1 42  ? -30.545 33.690  221.816 1.00 49.81  ? 42  PHE B CE1   1 
ATOM   4077  C CE2   . PHE B  1 42  ? -32.062 35.531  221.700 1.00 54.58  ? 42  PHE B CE2   1 
ATOM   4078  C CZ    . PHE B  1 42  ? -31.838 34.175  221.811 1.00 59.17  ? 42  PHE B CZ    1 
ATOM   4079  N N     . SER B  1 43  ? -29.832 36.438  218.572 1.00 53.97  ? 43  SER B N     1 
ATOM   4080  C CA    . SER B  1 43  ? -31.082 36.543  217.829 1.00 49.39  ? 43  SER B CA    1 
ATOM   4081  C C     . SER B  1 43  ? -31.715 35.163  217.722 1.00 52.15  ? 43  SER B C     1 
ATOM   4082  O O     . SER B  1 43  ? -31.046 34.194  217.363 1.00 50.63  ? 43  SER B O     1 
ATOM   4083  C CB    . SER B  1 43  ? -30.855 37.136  216.438 1.00 48.49  ? 43  SER B CB    1 
ATOM   4084  O OG    . SER B  1 43  ? -32.022 37.020  215.643 1.00 58.13  ? 43  SER B OG    1 
ATOM   4085  N N     . ALA B  1 44  ? -33.004 35.073  218.034 1.00 56.61  ? 44  ALA B N     1 
ATOM   4086  C CA    . ALA B  1 44  ? -33.691 33.785  218.043 1.00 54.70  ? 44  ALA B CA    1 
ATOM   4087  C C     . ALA B  1 44  ? -34.132 33.367  216.643 1.00 53.54  ? 44  ALA B C     1 
ATOM   4088  O O     . ALA B  1 44  ? -34.630 32.257  216.448 1.00 65.11  ? 44  ALA B O     1 
ATOM   4089  C CB    . ALA B  1 44  ? -34.884 33.830  218.981 1.00 47.02  ? 44  ALA B CB    1 
ATOM   4090  N N     . ASP B  1 45  ? -33.951 34.259  215.674 1.00 54.01  ? 45  ASP B N     1 
ATOM   4091  C CA    . ASP B  1 45  ? -34.304 33.964  214.289 1.00 59.02  ? 45  ASP B CA    1 
ATOM   4092  C C     . ASP B  1 45  ? -33.474 32.804  213.751 1.00 59.68  ? 45  ASP B C     1 
ATOM   4093  O O     . ASP B  1 45  ? -32.244 32.851  213.773 1.00 57.55  ? 45  ASP B O     1 
ATOM   4094  C CB    . ASP B  1 45  ? -34.115 35.200  213.405 1.00 57.96  ? 45  ASP B CB    1 
ATOM   4095  C CG    . ASP B  1 45  ? -35.112 36.299  213.719 1.00 72.37  ? 45  ASP B CG    1 
ATOM   4096  O OD1   . ASP B  1 45  ? -36.106 36.017  214.421 1.00 70.48  ? 45  ASP B OD1   1 
ATOM   4097  O OD2   . ASP B  1 45  ? -34.907 37.441  213.255 1.00 81.83  ? 45  ASP B OD2   1 
ATOM   4098  N N     . SER B  1 46  ? -34.156 31.768  213.266 1.00 58.65  ? 46  SER B N     1 
ATOM   4099  C CA    . SER B  1 46  ? -33.499 30.578  212.731 1.00 60.15  ? 46  SER B CA    1 
ATOM   4100  C C     . SER B  1 46  ? -32.548 30.900  211.579 1.00 57.49  ? 46  SER B C     1 
ATOM   4101  O O     . SER B  1 46  ? -31.637 30.127  211.284 1.00 62.35  ? 46  SER B O     1 
ATOM   4102  C CB    . SER B  1 46  ? -34.543 29.561  212.262 1.00 62.59  ? 46  SER B CB    1 
ATOM   4103  O OG    . SER B  1 46  ? -35.251 28.999  213.353 1.00 68.00  ? 46  SER B OG    1 
ATOM   4104  N N     . ASP B  1 47  ? -32.764 32.045  210.941 1.00 62.04  ? 47  ASP B N     1 
ATOM   4105  C CA    . ASP B  1 47  ? -32.026 32.418  209.740 1.00 67.24  ? 47  ASP B CA    1 
ATOM   4106  C C     . ASP B  1 47  ? -30.908 33.430  210.020 1.00 64.66  ? 47  ASP B C     1 
ATOM   4107  O O     . ASP B  1 47  ? -30.109 33.747  209.137 1.00 64.49  ? 47  ASP B O     1 
ATOM   4108  C CB    . ASP B  1 47  ? -33.005 32.974  208.696 1.00 79.31  ? 47  ASP B CB    1 
ATOM   4109  C CG    . ASP B  1 47  ? -32.319 33.416  207.419 1.00 99.79  ? 47  ASP B CG    1 
ATOM   4110  O OD1   . ASP B  1 47  ? -31.939 32.544  206.609 1.00 105.37 ? 47  ASP B OD1   1 
ATOM   4111  O OD2   . ASP B  1 47  ? -32.158 34.640  207.228 1.00 119.22 ? 47  ASP B OD2   1 
ATOM   4112  N N     . SER B  1 48  ? -30.839 33.923  211.252 1.00 59.43  ? 48  SER B N     1 
ATOM   4113  C CA    . SER B  1 48  ? -29.823 34.911  211.614 1.00 53.72  ? 48  SER B CA    1 
ATOM   4114  C C     . SER B  1 48  ? -28.406 34.351  211.495 1.00 55.60  ? 48  SER B C     1 
ATOM   4115  O O     . SER B  1 48  ? -28.182 33.157  211.704 1.00 52.62  ? 48  SER B O     1 
ATOM   4116  C CB    . SER B  1 48  ? -30.058 35.426  213.036 1.00 52.24  ? 48  SER B CB    1 
ATOM   4117  O OG    . SER B  1 48  ? -29.938 34.384  213.989 1.00 49.14  ? 48  SER B OG    1 
ATOM   4118  N N     . ASP B  1 49  ? -27.462 35.222  211.144 1.00 59.20  ? 49  ASP B N     1 
ATOM   4119  C CA    . ASP B  1 49  ? -26.045 34.876  211.128 1.00 49.97  ? 49  ASP B CA    1 
ATOM   4120  C C     . ASP B  1 49  ? -25.619 34.334  212.485 1.00 48.70  ? 49  ASP B C     1 
ATOM   4121  O O     . ASP B  1 49  ? -24.822 33.401  212.572 1.00 49.97  ? 49  ASP B O     1 
ATOM   4122  C CB    . ASP B  1 49  ? -25.191 36.094  210.761 1.00 53.42  ? 49  ASP B CB    1 
ATOM   4123  C CG    . ASP B  1 49  ? -25.062 36.292  209.265 1.00 61.09  ? 49  ASP B CG    1 
ATOM   4124  O OD1   . ASP B  1 49  ? -25.735 35.567  208.502 1.00 65.89  ? 49  ASP B OD1   1 
ATOM   4125  O OD2   . ASP B  1 49  ? -24.286 37.180  208.852 1.00 61.92  ? 49  ASP B OD2   1 
ATOM   4126  N N     . PHE B  1 50  ? -26.166 34.933  213.539 1.00 42.25  ? 50  PHE B N     1 
ATOM   4127  C CA    . PHE B  1 50  ? -25.911 34.493  214.905 1.00 45.83  ? 50  PHE B CA    1 
ATOM   4128  C C     . PHE B  1 50  ? -26.287 33.029  215.106 1.00 47.49  ? 50  PHE B C     1 
ATOM   4129  O O     . PHE B  1 50  ? -25.438 32.202  215.437 1.00 43.28  ? 50  PHE B O     1 
ATOM   4130  C CB    . PHE B  1 50  ? -26.682 35.362  215.905 1.00 43.17  ? 50  PHE B CB    1 
ATOM   4131  C CG    . PHE B  1 50  ? -26.623 34.854  217.322 1.00 46.79  ? 50  PHE B CG    1 
ATOM   4132  C CD1   . PHE B  1 50  ? -25.578 35.215  218.157 1.00 44.56  ? 50  PHE B CD1   1 
ATOM   4133  C CD2   . PHE B  1 50  ? -27.609 34.014  217.819 1.00 46.32  ? 50  PHE B CD2   1 
ATOM   4134  C CE1   . PHE B  1 50  ? -25.520 34.748  219.460 1.00 39.64  ? 50  PHE B CE1   1 
ATOM   4135  C CE2   . PHE B  1 50  ? -27.551 33.541  219.117 1.00 45.81  ? 50  PHE B CE2   1 
ATOM   4136  C CZ    . PHE B  1 50  ? -26.507 33.909  219.937 1.00 45.42  ? 50  PHE B CZ    1 
ATOM   4137  N N     . ASN B  1 51  ? -27.567 32.723  214.917 1.00 46.48  ? 51  ASN B N     1 
ATOM   4138  C CA    . ASN B  1 51  ? -28.082 31.382  215.169 1.00 46.69  ? 51  ASN B CA    1 
ATOM   4139  C C     . ASN B  1 51  ? -27.384 30.338  214.304 1.00 40.09  ? 51  ASN B C     1 
ATOM   4140  O O     . ASN B  1 51  ? -27.147 29.215  214.744 1.00 41.67  ? 51  ASN B O     1 
ATOM   4141  C CB    . ASN B  1 51  ? -29.595 31.336  214.937 1.00 45.58  ? 51  ASN B CB    1 
ATOM   4142  C CG    . ASN B  1 51  ? -30.208 30.012  215.345 1.00 46.13  ? 51  ASN B CG    1 
ATOM   4143  O OD1   . ASN B  1 51  ? -30.491 29.781  216.521 1.00 50.24  ? 51  ASN B OD1   1 
ATOM   4144  N ND2   . ASN B  1 51  ? -30.417 29.131  214.372 1.00 46.87  ? 51  ASN B ND2   1 
ATOM   4145  N N     . ARG B  1 52  ? -27.049 30.722  213.076 1.00 42.32  ? 52  ARG B N     1 
ATOM   4146  C CA    . ARG B  1 52  ? -26.303 29.848  212.177 1.00 40.64  ? 52  ARG B CA    1 
ATOM   4147  C C     . ARG B  1 52  ? -24.921 29.523  212.744 1.00 48.02  ? 52  ARG B C     1 
ATOM   4148  O O     . ARG B  1 52  ? -24.539 28.355  212.837 1.00 46.17  ? 52  ARG B O     1 
ATOM   4149  C CB    . ARG B  1 52  ? -26.168 30.489  210.796 1.00 45.24  ? 52  ARG B CB    1 
ATOM   4150  C CG    . ARG B  1 52  ? -25.251 29.726  209.852 1.00 54.28  ? 52  ARG B CG    1 
ATOM   4151  C CD    . ARG B  1 52  ? -25.511 30.092  208.400 1.00 59.59  ? 52  ARG B CD    1 
ATOM   4152  N NE    . ARG B  1 52  ? -25.209 31.493  208.130 1.00 65.23  ? 52  ARG B NE    1 
ATOM   4153  C CZ    . ARG B  1 52  ? -24.026 31.933  207.718 1.00 72.61  ? 52  ARG B CZ    1 
ATOM   4154  N NH1   . ARG B  1 52  ? -23.031 31.079  207.527 1.00 71.51  ? 52  ARG B NH1   1 
ATOM   4155  N NH2   . ARG B  1 52  ? -23.838 33.226  207.495 1.00 67.91  ? 52  ARG B NH2   1 
ATOM   4156  N N     . PHE B  1 53  ? -24.180 30.564  213.118 1.00 46.27  ? 53  PHE B N     1 
ATOM   4157  C CA    . PHE B  1 53  ? -22.859 30.408  213.724 1.00 42.04  ? 53  PHE B CA    1 
ATOM   4158  C C     . PHE B  1 53  ? -22.919 29.533  214.971 1.00 40.47  ? 53  PHE B C     1 
ATOM   4159  O O     . PHE B  1 53  ? -22.083 28.651  215.164 1.00 46.08  ? 53  PHE B O     1 
ATOM   4160  C CB    . PHE B  1 53  ? -22.265 31.771  214.089 1.00 38.39  ? 53  PHE B CB    1 
ATOM   4161  C CG    . PHE B  1 53  ? -21.882 32.608  212.905 1.00 41.62  ? 53  PHE B CG    1 
ATOM   4162  C CD1   . PHE B  1 53  ? -21.576 32.021  211.689 1.00 47.27  ? 53  PHE B CD1   1 
ATOM   4163  C CD2   . PHE B  1 53  ? -21.823 33.987  213.013 1.00 50.47  ? 53  PHE B CD2   1 
ATOM   4164  C CE1   . PHE B  1 53  ? -21.221 32.796  210.600 1.00 50.44  ? 53  PHE B CE1   1 
ATOM   4165  C CE2   . PHE B  1 53  ? -21.470 34.767  211.930 1.00 46.02  ? 53  PHE B CE2   1 
ATOM   4166  C CZ    . PHE B  1 53  ? -21.169 34.171  210.721 1.00 51.68  ? 53  PHE B CZ    1 
ATOM   4167  N N     . LEU B  1 54  ? -23.919 29.792  215.808 1.00 41.75  ? 54  LEU B N     1 
ATOM   4168  C CA    . LEU B  1 54  ? -24.086 29.080  217.070 1.00 42.23  ? 54  LEU B CA    1 
ATOM   4169  C C     . LEU B  1 54  ? -24.231 27.575  216.871 1.00 46.73  ? 54  LEU B C     1 
ATOM   4170  O O     . LEU B  1 54  ? -23.579 26.789  217.561 1.00 41.70  ? 54  LEU B O     1 
ATOM   4171  C CB    . LEU B  1 54  ? -25.301 29.619  217.829 1.00 43.57  ? 54  LEU B CB    1 
ATOM   4172  C CG    . LEU B  1 54  ? -25.679 28.908  219.133 1.00 44.29  ? 54  LEU B CG    1 
ATOM   4173  C CD1   . LEU B  1 54  ? -24.501 28.891  220.091 1.00 42.37  ? 54  LEU B CD1   1 
ATOM   4174  C CD2   . LEU B  1 54  ? -26.887 29.563  219.791 1.00 43.93  ? 54  LEU B CD2   1 
ATOM   4175  N N     . HIS B  1 55  ? -25.076 27.182  215.923 1.00 45.28  ? 55  HIS B N     1 
ATOM   4176  C CA    . HIS B  1 55  ? -25.426 25.777  215.730 1.00 44.22  ? 55  HIS B CA    1 
ATOM   4177  C C     . HIS B  1 55  ? -24.462 25.035  214.807 1.00 42.87  ? 55  HIS B C     1 
ATOM   4178  O O     . HIS B  1 55  ? -24.400 23.806  214.828 1.00 50.22  ? 55  HIS B O     1 
ATOM   4179  C CB    . HIS B  1 55  ? -26.854 25.661  215.183 1.00 41.64  ? 55  HIS B CB    1 
ATOM   4180  C CG    . HIS B  1 55  ? -27.914 25.909  216.210 1.00 38.78  ? 55  HIS B CG    1 
ATOM   4181  N ND1   . HIS B  1 55  ? -28.295 24.957  217.130 1.00 39.41  ? 55  HIS B ND1   1 
ATOM   4182  C CD2   . HIS B  1 55  ? -28.669 27.004  216.466 1.00 40.80  ? 55  HIS B CD2   1 
ATOM   4183  C CE1   . HIS B  1 55  ? -29.241 25.453  217.907 1.00 44.84  ? 55  HIS B CE1   1 
ATOM   4184  N NE2   . HIS B  1 55  ? -29.485 26.694  217.526 1.00 41.79  ? 55  HIS B NE2   1 
ATOM   4185  N N     . LEU B  1 56  ? -23.712 25.786  214.007 1.00 44.37  ? 56  LEU B N     1 
ATOM   4186  C CA    . LEU B  1 56  ? -22.772 25.210  213.048 1.00 47.72  ? 56  LEU B CA    1 
ATOM   4187  C C     . LEU B  1 56  ? -21.775 24.266  213.721 1.00 50.66  ? 56  LEU B C     1 
ATOM   4188  O O     . LEU B  1 56  ? -21.333 23.281  213.125 1.00 49.72  ? 56  LEU B O     1 
ATOM   4189  C CB    . LEU B  1 56  ? -22.033 26.330  212.314 1.00 50.94  ? 56  LEU B CB    1 
ATOM   4190  C CG    . LEU B  1 56  ? -21.619 26.113  210.859 1.00 58.12  ? 56  LEU B CG    1 
ATOM   4191  C CD1   . LEU B  1 56  ? -22.699 25.375  210.091 1.00 54.27  ? 56  LEU B CD1   1 
ATOM   4192  C CD2   . LEU B  1 56  ? -21.330 27.450  210.198 1.00 58.24  ? 56  LEU B CD2   1 
ATOM   4193  N N     . SER B  1 57  ? -21.437 24.564  214.970 1.00 43.22  ? 57  SER B N     1 
ATOM   4194  C CA    . SER B  1 57  ? -20.472 23.756  215.704 1.00 48.63  ? 57  SER B CA    1 
ATOM   4195  C C     . SER B  1 57  ? -21.029 23.241  217.027 1.00 46.78  ? 57  SER B C     1 
ATOM   4196  O O     . SER B  1 57  ? -20.304 23.150  218.015 1.00 47.12  ? 57  SER B O     1 
ATOM   4197  C CB    . SER B  1 57  ? -19.190 24.555  215.954 1.00 43.68  ? 57  SER B CB    1 
ATOM   4198  O OG    . SER B  1 57  ? -18.514 24.814  214.737 1.00 48.83  ? 57  SER B OG    1 
ATOM   4199  N N     . ILE B  1 58  ? -22.317 22.917  217.049 1.00 46.80  ? 58  ILE B N     1 
ATOM   4200  C CA    . ILE B  1 58  ? -22.891 22.191  218.175 1.00 44.52  ? 58  ILE B CA    1 
ATOM   4201  C C     . ILE B  1 58  ? -22.916 20.714  217.798 1.00 46.51  ? 58  ILE B C     1 
ATOM   4202  O O     . ILE B  1 58  ? -23.626 20.316  216.875 1.00 54.94  ? 58  ILE B O     1 
ATOM   4203  C CB    . ILE B  1 58  ? -24.307 22.688  218.537 1.00 47.31  ? 58  ILE B CB    1 
ATOM   4204  C CG1   . ILE B  1 58  ? -24.238 24.099  219.124 1.00 42.68  ? 58  ILE B CG1   1 
ATOM   4205  C CG2   . ILE B  1 58  ? -24.968 21.746  219.535 1.00 46.07  ? 58  ILE B CG2   1 
ATOM   4206  C CD1   . ILE B  1 58  ? -25.575 24.648  219.564 1.00 49.07  ? 58  ILE B CD1   1 
ATOM   4207  N N     . GLN B  1 59  ? -22.130 19.903  218.499 1.00 44.61  ? 59  GLN B N     1 
ATOM   4208  C CA    . GLN B  1 59  ? -21.901 18.525  218.069 1.00 48.15  ? 59  GLN B CA    1 
ATOM   4209  C C     . GLN B  1 59  ? -22.609 17.506  218.955 1.00 45.96  ? 59  GLN B C     1 
ATOM   4210  O O     . GLN B  1 59  ? -22.531 16.300  218.720 1.00 56.08  ? 59  GLN B O     1 
ATOM   4211  C CB    . GLN B  1 59  ? -20.400 18.232  218.028 1.00 47.02  ? 59  GLN B CB    1 
ATOM   4212  C CG    . GLN B  1 59  ? -19.599 19.153  217.101 1.00 41.91  ? 59  GLN B CG    1 
ATOM   4213  C CD    . GLN B  1 59  ? -19.840 18.879  215.623 1.00 46.91  ? 59  GLN B CD    1 
ATOM   4214  O OE1   . GLN B  1 59  ? -20.693 18.071  215.255 1.00 53.92  ? 59  GLN B OE1   1 
ATOM   4215  N NE2   . GLN B  1 59  ? -19.077 19.549  214.769 1.00 46.85  ? 59  GLN B NE2   1 
ATOM   4216  N N     . ASN B  1 60  ? -23.295 18.001  219.979 1.00 48.43  ? 60  ASN B N     1 
ATOM   4217  C CA    . ASN B  1 60  ? -24.185 17.170  220.775 1.00 49.74  ? 60  ASN B CA    1 
ATOM   4218  C C     . ASN B  1 60  ? -25.559 17.823  220.818 1.00 50.31  ? 60  ASN B C     1 
ATOM   4219  O O     . ASN B  1 60  ? -25.809 18.694  221.651 1.00 47.08  ? 60  ASN B O     1 
ATOM   4220  C CB    . ASN B  1 60  ? -23.640 16.961  222.191 1.00 48.33  ? 60  ASN B CB    1 
ATOM   4221  C CG    . ASN B  1 60  ? -24.434 15.926  222.977 1.00 51.09  ? 60  ASN B CG    1 
ATOM   4222  O OD1   . ASN B  1 60  ? -25.489 15.475  222.539 1.00 50.65  ? 60  ASN B OD1   1 
ATOM   4223  N ND2   . ASN B  1 60  ? -23.925 15.547  224.144 1.00 48.84  ? 60  ASN B ND2   1 
ATOM   4224  N N     . PRO B  1 61  ? -26.454 17.403  219.908 1.00 55.60  ? 61  PRO B N     1 
ATOM   4225  C CA    . PRO B  1 61  ? -27.836 17.885  219.781 1.00 55.19  ? 61  PRO B CA    1 
ATOM   4226  C C     . PRO B  1 61  ? -28.608 17.943  221.103 1.00 51.42  ? 61  PRO B C     1 
ATOM   4227  O O     . PRO B  1 61  ? -29.646 18.601  221.163 1.00 51.49  ? 61  PRO B O     1 
ATOM   4228  C CB    . PRO B  1 61  ? -28.463 16.862  218.834 1.00 56.93  ? 61  PRO B CB    1 
ATOM   4229  C CG    . PRO B  1 61  ? -27.335 16.473  217.945 1.00 54.34  ? 61  PRO B CG    1 
ATOM   4230  C CD    . PRO B  1 61  ? -26.106 16.468  218.823 1.00 53.19  ? 61  PRO B CD    1 
ATOM   4231  N N     . LEU B  1 62  ? -28.104 17.278  222.140 1.00 45.96  ? 62  LEU B N     1 
ATOM   4232  C CA    . LEU B  1 62  ? -28.708 17.335  223.470 1.00 47.91  ? 62  LEU B CA    1 
ATOM   4233  C C     . LEU B  1 62  ? -28.758 18.764  224.013 1.00 53.60  ? 62  LEU B C     1 
ATOM   4234  O O     . LEU B  1 62  ? -29.550 19.072  224.904 1.00 56.45  ? 62  LEU B O     1 
ATOM   4235  C CB    . LEU B  1 62  ? -27.940 16.431  224.444 1.00 41.19  ? 62  LEU B CB    1 
ATOM   4236  C CG    . LEU B  1 62  ? -28.408 16.345  225.904 1.00 50.83  ? 62  LEU B CG    1 
ATOM   4237  C CD1   . LEU B  1 62  ? -29.849 15.853  225.986 1.00 48.89  ? 62  LEU B CD1   1 
ATOM   4238  C CD2   . LEU B  1 62  ? -27.492 15.451  226.730 1.00 48.47  ? 62  LEU B CD2   1 
ATOM   4239  N N     . PHE B  1 63  ? -27.918 19.638  223.468 1.00 49.82  ? 63  PHE B N     1 
ATOM   4240  C CA    . PHE B  1 63  ? -27.811 20.997  223.982 1.00 49.79  ? 63  PHE B CA    1 
ATOM   4241  C C     . PHE B  1 63  ? -28.150 22.062  222.945 1.00 55.33  ? 63  PHE B C     1 
ATOM   4242  O O     . PHE B  1 63  ? -27.683 23.195  223.049 1.00 56.10  ? 63  PHE B O     1 
ATOM   4243  C CB    . PHE B  1 63  ? -26.397 21.243  224.517 1.00 50.69  ? 63  PHE B CB    1 
ATOM   4244  C CG    . PHE B  1 63  ? -25.989 20.293  225.604 1.00 47.93  ? 63  PHE B CG    1 
ATOM   4245  C CD1   . PHE B  1 63  ? -26.405 20.496  226.909 1.00 45.98  ? 63  PHE B CD1   1 
ATOM   4246  C CD2   . PHE B  1 63  ? -25.190 19.195  225.322 1.00 43.47  ? 63  PHE B CD2   1 
ATOM   4247  C CE1   . PHE B  1 63  ? -26.035 19.622  227.914 1.00 44.95  ? 63  PHE B CE1   1 
ATOM   4248  C CE2   . PHE B  1 63  ? -24.818 18.317  226.322 1.00 42.89  ? 63  PHE B CE2   1 
ATOM   4249  C CZ    . PHE B  1 63  ? -25.239 18.532  227.620 1.00 42.99  ? 63  PHE B CZ    1 
ATOM   4250  N N     . GLN B  1 64  ? -28.969 21.720  221.956 1.00 54.92  ? 64  GLN B N     1 
ATOM   4251  C CA    . GLN B  1 64  ? -29.232 22.653  220.862 1.00 54.04  ? 64  GLN B CA    1 
ATOM   4252  C C     . GLN B  1 64  ? -30.563 23.395  220.987 1.00 57.10  ? 64  GLN B C     1 
ATOM   4253  O O     . GLN B  1 64  ? -30.739 24.450  220.380 1.00 53.65  ? 64  GLN B O     1 
ATOM   4254  C CB    . GLN B  1 64  ? -29.193 21.918  219.517 1.00 55.87  ? 64  GLN B CB    1 
ATOM   4255  C CG    . GLN B  1 64  ? -30.399 21.030  219.267 1.00 61.35  ? 64  GLN B CG    1 
ATOM   4256  C CD    . GLN B  1 64  ? -30.298 20.253  217.971 1.00 65.41  ? 64  GLN B CD    1 
ATOM   4257  O OE1   . GLN B  1 64  ? -29.263 20.264  217.303 1.00 72.01  ? 64  GLN B OE1   1 
ATOM   4258  N NE2   . GLN B  1 64  ? -31.375 19.564  217.611 1.00 72.34  ? 64  GLN B NE2   1 
ATOM   4259  N N     . ASN B  1 65  ? -31.492 22.855  221.771 1.00 57.15  ? 65  ASN B N     1 
ATOM   4260  C CA    . ASN B  1 65  ? -32.854 23.387  221.794 1.00 61.57  ? 65  ASN B CA    1 
ATOM   4261  C C     . ASN B  1 65  ? -32.949 24.783  222.408 1.00 61.61  ? 65  ASN B C     1 
ATOM   4262  O O     . ASN B  1 65  ? -32.081 25.202  223.174 1.00 56.20  ? 65  ASN B O     1 
ATOM   4263  C CB    . ASN B  1 65  ? -33.788 22.426  222.533 1.00 59.64  ? 65  ASN B CB    1 
ATOM   4264  C CG    . ASN B  1 65  ? -33.497 22.353  224.016 1.00 64.50  ? 65  ASN B CG    1 
ATOM   4265  O OD1   . ASN B  1 65  ? -33.960 23.189  224.792 1.00 61.97  ? 65  ASN B OD1   1 
ATOM   4266  N ND2   . ASN B  1 65  ? -32.732 21.345  224.420 1.00 73.36  ? 65  ASN B ND2   1 
ATOM   4267  N N     . SER B  1 66  ? -34.028 25.484  222.072 1.00 59.63  ? 66  SER B N     1 
ATOM   4268  C CA    . SER B  1 66  ? -34.173 26.908  222.365 1.00 63.10  ? 66  SER B CA    1 
ATOM   4269  C C     . SER B  1 66  ? -34.144 27.251  223.856 1.00 63.57  ? 66  SER B C     1 
ATOM   4270  O O     . SER B  1 66  ? -33.959 28.411  224.231 1.00 63.42  ? 66  SER B O     1 
ATOM   4271  C CB    . SER B  1 66  ? -35.474 27.426  221.750 1.00 70.75  ? 66  SER B CB    1 
ATOM   4272  O OG    . SER B  1 66  ? -35.644 28.806  222.012 1.00 80.80  ? 66  SER B OG    1 
ATOM   4273  N N     . LEU B  1 67  ? -34.319 26.234  224.696 1.00 59.58  ? 67  LEU B N     1 
ATOM   4274  C CA    . LEU B  1 67  ? -34.431 26.415  226.141 1.00 57.55  ? 67  LEU B CA    1 
ATOM   4275  C C     . LEU B  1 67  ? -33.071 26.278  226.838 1.00 61.96  ? 67  LEU B C     1 
ATOM   4276  O O     . LEU B  1 67  ? -32.965 26.436  228.059 1.00 64.97  ? 67  LEU B O     1 
ATOM   4277  C CB    . LEU B  1 67  ? -35.438 25.411  226.721 1.00 68.25  ? 67  LEU B CB    1 
ATOM   4278  C CG    . LEU B  1 67  ? -36.945 25.738  226.676 1.00 60.85  ? 67  LEU B CG    1 
ATOM   4279  C CD1   . LEU B  1 67  ? -37.392 26.325  225.338 1.00 52.17  ? 67  LEU B CD1   1 
ATOM   4280  C CD2   . LEU B  1 67  ? -37.773 24.503  227.011 1.00 58.44  ? 67  LEU B CD2   1 
ATOM   4281  N N     . ILE B  1 68  ? -32.039 25.984  226.051 1.00 56.40  ? 68  ILE B N     1 
ATOM   4282  C CA    . ILE B  1 68  ? -30.658 25.974  226.526 1.00 55.54  ? 68  ILE B CA    1 
ATOM   4283  C C     . ILE B  1 68  ? -30.159 27.409  226.652 1.00 53.38  ? 68  ILE B C     1 
ATOM   4284  O O     . ILE B  1 68  ? -30.618 28.293  225.926 1.00 47.56  ? 68  ILE B O     1 
ATOM   4285  C CB    . ILE B  1 68  ? -29.743 25.175  225.566 1.00 56.40  ? 68  ILE B CB    1 
ATOM   4286  C CG1   . ILE B  1 68  ? -30.299 23.767  225.356 1.00 62.43  ? 68  ILE B CG1   1 
ATOM   4287  C CG2   . ILE B  1 68  ? -28.322 25.075  226.098 1.00 57.77  ? 68  ILE B CG2   1 
ATOM   4288  C CD1   . ILE B  1 68  ? -30.275 22.922  226.606 1.00 58.73  ? 68  ILE B CD1   1 
ATOM   4289  N N     . SER B  1 69  ? -29.247 27.646  227.590 1.00 54.84  ? 69  SER B N     1 
ATOM   4290  C CA    . SER B  1 69  ? -28.573 28.933  227.686 1.00 50.60  ? 69  SER B CA    1 
ATOM   4291  C C     . SER B  1 69  ? -27.931 29.293  226.351 1.00 45.31  ? 69  SER B C     1 
ATOM   4292  O O     . SER B  1 69  ? -27.342 28.442  225.686 1.00 46.18  ? 69  SER B O     1 
ATOM   4293  C CB    . SER B  1 69  ? -27.516 28.906  228.790 1.00 47.90  ? 69  SER B CB    1 
ATOM   4294  O OG    . SER B  1 69  ? -26.564 27.888  228.547 1.00 49.45  ? 69  SER B OG    1 
ATOM   4295  N N     . LYS B  1 70  ? -28.064 30.554  225.961 1.00 44.59  ? 70  LYS B N     1 
ATOM   4296  C CA    . LYS B  1 70  ? -27.518 31.034  224.699 1.00 45.70  ? 70  LYS B CA    1 
ATOM   4297  C C     . LYS B  1 70  ? -26.542 32.170  224.961 1.00 44.19  ? 70  LYS B C     1 
ATOM   4298  O O     . LYS B  1 70  ? -26.745 32.958  225.885 1.00 35.88  ? 70  LYS B O     1 
ATOM   4299  C CB    . LYS B  1 70  ? -28.642 31.502  223.774 1.00 47.85  ? 70  LYS B CB    1 
ATOM   4300  C CG    . LYS B  1 70  ? -29.774 30.501  223.613 1.00 45.96  ? 70  LYS B CG    1 
ATOM   4301  C CD    . LYS B  1 70  ? -29.402 29.395  222.642 1.00 51.38  ? 70  LYS B CD    1 
ATOM   4302  C CE    . LYS B  1 70  ? -30.451 28.293  222.638 1.00 49.79  ? 70  LYS B CE    1 
ATOM   4303  N NZ    . LYS B  1 70  ? -30.200 27.286  221.571 1.00 46.55  ? 70  LYS B NZ    1 
ATOM   4304  N N     . PRO B  1 71  ? -25.471 32.257  224.157 1.00 41.02  ? 71  PRO B N     1 
ATOM   4305  C CA    . PRO B  1 71  ? -24.537 33.373  224.336 1.00 43.86  ? 71  PRO B CA    1 
ATOM   4306  C C     . PRO B  1 71  ? -25.176 34.685  223.900 1.00 43.34  ? 71  PRO B C     1 
ATOM   4307  O O     . PRO B  1 71  ? -25.925 34.702  222.923 1.00 45.74  ? 71  PRO B O     1 
ATOM   4308  C CB    . PRO B  1 71  ? -23.355 32.993  223.440 1.00 36.64  ? 71  PRO B CB    1 
ATOM   4309  C CG    . PRO B  1 71  ? -23.939 32.097  222.404 1.00 41.22  ? 71  PRO B CG    1 
ATOM   4310  C CD    . PRO B  1 71  ? -25.040 31.336  223.091 1.00 42.50  ? 71  PRO B CD    1 
ATOM   4311  N N     . SER B  1 72  ? -24.893 35.762  224.626 1.00 40.29  ? 72  SER B N     1 
ATOM   4312  C CA    . SER B  1 72  ? -25.466 37.068  224.319 1.00 36.67  ? 72  SER B CA    1 
ATOM   4313  C C     . SER B  1 72  ? -24.834 37.649  223.056 1.00 38.81  ? 72  SER B C     1 
ATOM   4314  O O     . SER B  1 72  ? -25.379 38.562  222.435 1.00 37.66  ? 72  SER B O     1 
ATOM   4315  C CB    . SER B  1 72  ? -25.280 38.023  225.499 1.00 35.27  ? 72  SER B CB    1 
ATOM   4316  O OG    . SER B  1 72  ? -25.772 37.442  226.699 1.00 37.49  ? 72  SER B OG    1 
ATOM   4317  N N     . ALA B  1 73  ? -23.680 37.104  222.680 1.00 36.49  ? 73  ALA B N     1 
ATOM   4318  C CA    . ALA B  1 73  ? -22.989 37.508  221.461 1.00 37.64  ? 73  ALA B CA    1 
ATOM   4319  C C     . ALA B  1 73  ? -21.981 36.447  221.051 1.00 33.98  ? 73  ALA B C     1 
ATOM   4320  O O     . ALA B  1 73  ? -21.477 35.699  221.889 1.00 34.21  ? 73  ALA B O     1 
ATOM   4321  C CB    . ALA B  1 73  ? -22.299 38.850  221.651 1.00 30.49  ? 73  ALA B CB    1 
ATOM   4322  N N     . ILE B  1 74  ? -21.695 36.381  219.757 1.00 35.18  ? 74  ILE B N     1 
ATOM   4323  C CA    . ILE B  1 74  ? -20.681 35.473  219.243 1.00 35.14  ? 74  ILE B CA    1 
ATOM   4324  C C     . ILE B  1 74  ? -19.583 36.274  218.563 1.00 38.25  ? 74  ILE B C     1 
ATOM   4325  O O     . ILE B  1 74  ? -19.860 37.160  217.757 1.00 33.72  ? 74  ILE B O     1 
ATOM   4326  C CB    . ILE B  1 74  ? -21.272 34.455  218.251 1.00 37.47  ? 74  ILE B CB    1 
ATOM   4327  C CG1   . ILE B  1 74  ? -22.326 33.593  218.940 1.00 45.36  ? 74  ILE B CG1   1 
ATOM   4328  C CG2   . ILE B  1 74  ? -20.183 33.563  217.692 1.00 35.88  ? 74  ILE B CG2   1 
ATOM   4329  C CD1   . ILE B  1 74  ? -22.945 32.545  218.041 1.00 42.38  ? 74  ILE B CD1   1 
ATOM   4330  N N     . ILE B  1 75  ? -18.335 35.968  218.899 1.00 37.24  ? 75  ILE B N     1 
ATOM   4331  C CA    . ILE B  1 75  ? -17.199 36.683  218.333 1.00 34.65  ? 75  ILE B CA    1 
ATOM   4332  C C     . ILE B  1 75  ? -16.247 35.717  217.635 1.00 32.13  ? 75  ILE B C     1 
ATOM   4333  O O     . ILE B  1 75  ? -15.899 34.674  218.185 1.00 31.13  ? 75  ILE B O     1 
ATOM   4334  C CB    . ILE B  1 75  ? -16.433 37.467  219.414 1.00 33.74  ? 75  ILE B CB    1 
ATOM   4335  C CG1   . ILE B  1 75  ? -17.385 38.362  220.211 1.00 37.56  ? 75  ILE B CG1   1 
ATOM   4336  C CG2   . ILE B  1 75  ? -15.325 38.294  218.786 1.00 31.47  ? 75  ILE B CG2   1 
ATOM   4337  C CD1   . ILE B  1 75  ? -16.748 38.953  221.444 1.00 44.27  ? 75  ILE B CD1   1 
ATOM   4338  N N     . LEU B  1 76  ? -15.840 36.065  216.419 1.00 33.27  ? 76  LEU B N     1 
ATOM   4339  C CA    . LEU B  1 76  ? -14.926 35.231  215.651 1.00 37.15  ? 76  LEU B CA    1 
ATOM   4340  C C     . LEU B  1 76  ? -13.590 35.937  215.418 1.00 37.46  ? 76  LEU B C     1 
ATOM   4341  O O     . LEU B  1 76  ? -13.389 36.563  214.375 1.00 39.37  ? 76  LEU B O     1 
ATOM   4342  C CB    . LEU B  1 76  ? -15.551 34.841  214.306 1.00 37.02  ? 76  LEU B CB    1 
ATOM   4343  C CG    . LEU B  1 76  ? -16.507 33.643  214.218 1.00 44.76  ? 76  LEU B CG    1 
ATOM   4344  C CD1   . LEU B  1 76  ? -17.718 33.830  215.102 1.00 39.94  ? 76  LEU B CD1   1 
ATOM   4345  C CD2   . LEU B  1 76  ? -16.944 33.439  212.782 1.00 50.01  ? 76  LEU B CD2   1 
ATOM   4346  N N     . PRO B  1 77  ? -12.670 35.841  216.390 1.00 32.67  ? 77  PRO B N     1 
ATOM   4347  C CA    . PRO B  1 77  ? -11.346 36.458  216.231 1.00 36.61  ? 77  PRO B CA    1 
ATOM   4348  C C     . PRO B  1 77  ? -10.586 35.853  215.058 1.00 33.32  ? 77  PRO B C     1 
ATOM   4349  O O     . PRO B  1 77  ? -10.688 34.650  214.824 1.00 33.20  ? 77  PRO B O     1 
ATOM   4350  C CB    . PRO B  1 77  ? -10.648 36.152  217.560 1.00 31.56  ? 77  PRO B CB    1 
ATOM   4351  C CG    . PRO B  1 77  ? -11.352 34.952  218.089 1.00 36.22  ? 77  PRO B CG    1 
ATOM   4352  C CD    . PRO B  1 77  ? -12.786 35.110  217.663 1.00 30.28  ? 77  PRO B CD    1 
ATOM   4353  N N     . GLY B  1 78  ? -9.847  36.684  214.328 1.00 34.77  ? 78  GLY B N     1 
ATOM   4354  C CA    . GLY B  1 78  ? -9.154  36.239  213.132 1.00 36.89  ? 78  GLY B CA    1 
ATOM   4355  C C     . GLY B  1 78  ? -7.644  36.275  213.261 1.00 37.37  ? 78  GLY B C     1 
ATOM   4356  O O     . GLY B  1 78  ? -6.922  36.040  212.293 1.00 37.09  ? 78  GLY B O     1 
ATOM   4357  N N     . SER B  1 79  ? -7.166  36.573  214.464 1.00 35.44  ? 79  SER B N     1 
ATOM   4358  C CA    . SER B  1 79  ? -5.734  36.602  214.744 1.00 34.42  ? 79  SER B CA    1 
ATOM   4359  C C     . SER B  1 79  ? -5.501  36.439  216.241 1.00 36.64  ? 79  SER B C     1 
ATOM   4360  O O     . SER B  1 79  ? -6.440  36.537  217.031 1.00 31.79  ? 79  SER B O     1 
ATOM   4361  C CB    . SER B  1 79  ? -5.106  37.907  214.244 1.00 29.58  ? 79  SER B CB    1 
ATOM   4362  O OG    . SER B  1 79  ? -5.437  38.993  215.091 1.00 34.99  ? 79  SER B OG    1 
ATOM   4363  N N     . LYS B  1 80  ? -4.255  36.192  216.635 1.00 35.50  ? 80  LYS B N     1 
ATOM   4364  C CA    . LYS B  1 80  ? -3.952  36.024  218.051 1.00 29.77  ? 80  LYS B CA    1 
ATOM   4365  C C     . LYS B  1 80  ? -4.117  37.359  218.775 1.00 28.32  ? 80  LYS B C     1 
ATOM   4366  O O     . LYS B  1 80  ? -4.490  37.397  219.949 1.00 31.88  ? 80  LYS B O     1 
ATOM   4367  C CB    . LYS B  1 80  ? -2.541  35.454  218.258 1.00 36.00  ? 80  LYS B CB    1 
ATOM   4368  C CG    . LYS B  1 80  ? -1.388  36.382  217.897 1.00 29.54  ? 80  LYS B CG    1 
ATOM   4369  C CD    . LYS B  1 80  ? -0.047  35.704  218.178 1.00 33.79  ? 80  LYS B CD    1 
ATOM   4370  C CE    . LYS B  1 80  ? 1.127   36.666  218.023 1.00 31.73  ? 80  LYS B CE    1 
ATOM   4371  N NZ    . LYS B  1 80  ? 1.313   37.113  216.617 1.00 29.29  ? 80  LYS B NZ    1 
ATOM   4372  N N     . GLU B  1 81  ? -3.857  38.451  218.062 1.00 29.59  ? 81  GLU B N     1 
ATOM   4373  C CA    . GLU B  1 81  ? -4.053  39.783  218.620 1.00 32.92  ? 81  GLU B CA    1 
ATOM   4374  C C     . GLU B  1 81  ? -5.536  40.055  218.861 1.00 31.75  ? 81  GLU B C     1 
ATOM   4375  O O     . GLU B  1 81  ? -5.912  40.622  219.887 1.00 33.84  ? 81  GLU B O     1 
ATOM   4376  C CB    . GLU B  1 81  ? -3.470  40.860  217.700 1.00 30.11  ? 81  GLU B CB    1 
ATOM   4377  C CG    . GLU B  1 81  ? -1.951  40.854  217.597 1.00 31.96  ? 81  GLU B CG    1 
ATOM   4378  C CD    . GLU B  1 81  ? -1.434  39.807  216.632 1.00 36.59  ? 81  GLU B CD    1 
ATOM   4379  O OE1   . GLU B  1 81  ? -2.235  39.305  215.813 1.00 34.69  ? 81  GLU B OE1   1 
ATOM   4380  O OE2   . GLU B  1 81  ? -0.226  39.486  216.686 1.00 34.39  ? 81  GLU B OE2   1 
ATOM   4381  N N     . GLU B  1 82  ? -6.375  39.649  217.912 1.00 31.97  ? 82  GLU B N     1 
ATOM   4382  C CA    . GLU B  1 82  ? -7.819  39.810  218.064 1.00 31.02  ? 82  GLU B CA    1 
ATOM   4383  C C     . GLU B  1 82  ? -8.345  38.931  219.193 1.00 31.10  ? 82  GLU B C     1 
ATOM   4384  O O     . GLU B  1 82  ? -9.259  39.323  219.915 1.00 31.68  ? 82  GLU B O     1 
ATOM   4385  C CB    . GLU B  1 82  ? -8.551  39.487  216.759 1.00 35.11  ? 82  GLU B CB    1 
ATOM   4386  C CG    . GLU B  1 82  ? -8.383  40.539  215.672 1.00 35.19  ? 82  GLU B CG    1 
ATOM   4387  C CD    . GLU B  1 82  ? -9.189  40.222  214.429 1.00 42.36  ? 82  GLU B CD    1 
ATOM   4388  O OE1   . GLU B  1 82  ? -10.111 39.381  214.510 1.00 39.15  ? 82  GLU B OE1   1 
ATOM   4389  O OE2   . GLU B  1 82  ? -8.901  40.814  213.366 1.00 42.12  ? 82  GLU B OE2   1 
ATOM   4390  N N     . LEU B  1 83  ? -7.757  37.747  219.345 1.00 31.65  ? 83  LEU B N     1 
ATOM   4391  C CA    . LEU B  1 83  ? -8.139  36.843  220.425 1.00 28.80  ? 83  LEU B CA    1 
ATOM   4392  C C     . LEU B  1 83  ? -7.780  37.450  221.773 1.00 33.20  ? 83  LEU B C     1 
ATOM   4393  O O     . LEU B  1 83  ? -8.566  37.391  222.721 1.00 34.33  ? 83  LEU B O     1 
ATOM   4394  C CB    . LEU B  1 83  ? -7.467  35.477  220.263 1.00 30.71  ? 83  LEU B CB    1 
ATOM   4395  C CG    . LEU B  1 83  ? -7.769  34.435  221.342 1.00 26.53  ? 83  LEU B CG    1 
ATOM   4396  C CD1   . LEU B  1 83  ? -9.275  34.249  221.499 1.00 29.53  ? 83  LEU B CD1   1 
ATOM   4397  C CD2   . LEU B  1 83  ? -7.096  33.110  221.015 1.00 29.45  ? 83  LEU B CD2   1 
ATOM   4398  N N     . SER B  1 84  ? -6.586  38.033  221.845 1.00 31.01  ? 84  SER B N     1 
ATOM   4399  C CA    . SER B  1 84  ? -6.109  38.678  223.062 1.00 29.79  ? 84  SER B CA    1 
ATOM   4400  C C     . SER B  1 84  ? -7.000  39.852  223.454 1.00 24.50  ? 84  SER B C     1 
ATOM   4401  O O     . SER B  1 84  ? -7.402  39.976  224.608 1.00 31.59  ? 84  SER B O     1 
ATOM   4402  C CB    . SER B  1 84  ? -4.660  39.153  222.888 1.00 28.24  ? 84  SER B CB    1 
ATOM   4403  O OG    . SER B  1 84  ? -4.262  39.979  223.968 1.00 27.15  ? 84  SER B OG    1 
ATOM   4404  N N     . ASN B  1 85  ? -7.305  40.710  222.485 1.00 27.10  ? 85  ASN B N     1 
ATOM   4405  C CA    . ASN B  1 85  ? -8.157  41.876  222.722 1.00 30.33  ? 85  ASN B CA    1 
ATOM   4406  C C     . ASN B  1 85  ? -9.603  41.497  223.036 1.00 34.75  ? 85  ASN B C     1 
ATOM   4407  O O     . ASN B  1 85  ? -10.257 42.153  223.851 1.00 34.57  ? 85  ASN B O     1 
ATOM   4408  C CB    . ASN B  1 85  ? -8.119  42.817  221.521 1.00 29.37  ? 85  ASN B CB    1 
ATOM   4409  C CG    . ASN B  1 85  ? -6.781  43.524  221.388 1.00 40.05  ? 85  ASN B CG    1 
ATOM   4410  O OD1   . ASN B  1 85  ? -6.007  43.587  222.345 1.00 37.18  ? 85  ASN B OD1   1 
ATOM   4411  N ND2   . ASN B  1 85  ? -6.508  44.070  220.210 1.00 35.82  ? 85  ASN B ND2   1 
ATOM   4412  N N     . THR B  1 86  ? -10.100 40.445  222.390 1.00 35.11  ? 86  THR B N     1 
ATOM   4413  C CA    . THR B  1 86  ? -11.451 39.955  222.649 1.00 32.63  ? 86  THR B CA    1 
ATOM   4414  C C     . THR B  1 86  ? -11.606 39.572  224.117 1.00 36.75  ? 86  THR B C     1 
ATOM   4415  O O     . THR B  1 86  ? -12.592 39.931  224.762 1.00 34.23  ? 86  THR B O     1 
ATOM   4416  C CB    . THR B  1 86  ? -11.794 38.740  221.763 1.00 28.51  ? 86  THR B CB    1 
ATOM   4417  O OG1   . THR B  1 86  ? -11.820 39.132  220.384 1.00 30.44  ? 86  THR B OG1   1 
ATOM   4418  C CG2   . THR B  1 86  ? -13.149 38.174  222.140 1.00 32.46  ? 86  THR B CG2   1 
ATOM   4419  N N     . ILE B  1 87  ? -10.613 38.857  224.638 1.00 30.97  ? 87  ILE B N     1 
ATOM   4420  C CA    . ILE B  1 87  ? -10.618 38.404  226.023 1.00 30.04  ? 87  ILE B CA    1 
ATOM   4421  C C     . ILE B  1 87  ? -10.612 39.576  227.003 1.00 32.89  ? 87  ILE B C     1 
ATOM   4422  O O     . ILE B  1 87  ? -11.309 39.550  228.019 1.00 38.73  ? 87  ILE B O     1 
ATOM   4423  C CB    . ILE B  1 87  ? -9.407  37.487  226.299 1.00 36.24  ? 87  ILE B CB    1 
ATOM   4424  C CG1   . ILE B  1 87  ? -9.602  36.145  225.594 1.00 36.33  ? 87  ILE B CG1   1 
ATOM   4425  C CG2   . ILE B  1 87  ? -9.202  37.281  227.794 1.00 33.02  ? 87  ILE B CG2   1 
ATOM   4426  C CD1   . ILE B  1 87  ? -8.376  35.270  225.610 1.00 34.97  ? 87  ILE B CD1   1 
ATOM   4427  N N     . ARG B  1 88  ? -9.837  40.608  226.684 1.00 32.59  ? 88  ARG B N     1 
ATOM   4428  C CA    . ARG B  1 88  ? -9.771  41.807  227.514 1.00 38.23  ? 88  ARG B CA    1 
ATOM   4429  C C     . ARG B  1 88  ? -11.088 42.578  227.523 1.00 37.42  ? 88  ARG B C     1 
ATOM   4430  O O     . ARG B  1 88  ? -11.547 43.025  228.575 1.00 43.35  ? 88  ARG B O     1 
ATOM   4431  C CB    . ARG B  1 88  ? -8.662  42.737  227.031 1.00 32.32  ? 88  ARG B CB    1 
ATOM   4432  C CG    . ARG B  1 88  ? -7.268  42.440  227.550 1.00 39.92  ? 88  ARG B CG    1 
ATOM   4433  C CD    . ARG B  1 88  ? -6.340  43.635  227.315 1.00 48.26  ? 88  ARG B CD    1 
ATOM   4434  N NE    . ARG B  1 88  ? -6.398  44.118  225.935 1.00 53.08  ? 88  ARG B NE    1 
ATOM   4435  C CZ    . ARG B  1 88  ? -7.139  45.143  225.519 1.00 48.42  ? 88  ARG B CZ    1 
ATOM   4436  N NH1   . ARG B  1 88  ? -7.901  45.813  226.374 1.00 44.86  ? 88  ARG B NH1   1 
ATOM   4437  N NH2   . ARG B  1 88  ? -7.123  45.493  224.241 1.00 45.25  ? 88  ARG B NH2   1 
ATOM   4438  N N     . CYS B  1 89  ? -11.671 42.750  226.340 1.00 32.75  ? 89  CYS B N     1 
ATOM   4439  C CA    . CYS B  1 89  ? -12.921 43.492  226.176 1.00 39.21  ? 89  CYS B CA    1 
ATOM   4440  C C     . CYS B  1 89  ? -14.080 42.848  226.925 1.00 38.60  ? 89  CYS B C     1 
ATOM   4441  O O     . CYS B  1 89  ? -14.772 43.517  227.698 1.00 40.04  ? 89  CYS B O     1 
ATOM   4442  C CB    . CYS B  1 89  ? -13.282 43.613  224.695 1.00 36.25  ? 89  CYS B CB    1 
ATOM   4443  S SG    . CYS B  1 89  ? -12.425 44.921  223.805 1.00 39.84  ? 89  CYS B SG    1 
ATOM   4444  N N     . ILE B  1 90  ? -14.293 41.558  226.679 1.00 38.83  ? 90  ILE B N     1 
ATOM   4445  C CA    . ILE B  1 90  ? -15.320 40.782  227.361 1.00 45.44  ? 90  ILE B CA    1 
ATOM   4446  C C     . ILE B  1 90  ? -15.198 40.904  228.878 1.00 49.53  ? 90  ILE B C     1 
ATOM   4447  O O     . ILE B  1 90  ? -16.202 41.050  229.587 1.00 47.58  ? 90  ILE B O     1 
ATOM   4448  C CB    . ILE B  1 90  ? -15.238 39.282  226.972 1.00 41.89  ? 90  ILE B CB    1 
ATOM   4449  C CG1   . ILE B  1 90  ? -15.576 39.087  225.494 1.00 33.78  ? 90  ILE B CG1   1 
ATOM   4450  C CG2   . ILE B  1 90  ? -16.169 38.450  227.832 1.00 39.27  ? 90  ILE B CG2   1 
ATOM   4451  C CD1   . ILE B  1 90  ? -15.327 37.678  225.004 1.00 30.75  ? 90  ILE B CD1   1 
ATOM   4452  N N     . ARG B  1 91  ? -13.963 40.875  229.369 1.00 47.11  ? 91  ARG B N     1 
ATOM   4453  C CA    . ARG B  1 91  ? -13.710 40.854  230.802 1.00 47.43  ? 91  ARG B CA    1 
ATOM   4454  C C     . ARG B  1 91  ? -14.022 42.179  231.501 1.00 50.64  ? 91  ARG B C     1 
ATOM   4455  O O     . ARG B  1 91  ? -14.422 42.194  232.664 1.00 53.24  ? 91  ARG B O     1 
ATOM   4456  C CB    . ARG B  1 91  ? -12.262 40.466  231.057 1.00 55.59  ? 91  ARG B CB    1 
ATOM   4457  C CG    . ARG B  1 91  ? -11.880 40.486  232.508 1.00 59.21  ? 91  ARG B CG    1 
ATOM   4458  C CD    . ARG B  1 91  ? -10.444 40.109  232.676 1.00 55.61  ? 91  ARG B CD    1 
ATOM   4459  N NE    . ARG B  1 91  ? -10.081 40.044  234.083 1.00 60.38  ? 91  ARG B NE    1 
ATOM   4460  C CZ    . ARG B  1 91  ? -8.918  39.580  234.525 1.00 59.64  ? 91  ARG B CZ    1 
ATOM   4461  N NH1   . ARG B  1 91  ? -8.664  39.550  235.824 1.00 61.98  ? 91  ARG B NH1   1 
ATOM   4462  N NH2   . ARG B  1 91  ? -8.007  39.139  233.668 1.00 63.99  ? 91  ARG B NH2   1 
ATOM   4463  N N     . LYS B  1 92  ? -13.848 43.287  230.783 1.00 50.61  ? 92  LYS B N     1 
ATOM   4464  C CA    . LYS B  1 92  ? -14.238 44.609  231.282 1.00 54.78  ? 92  LYS B CA    1 
ATOM   4465  C C     . LYS B  1 92  ? -15.697 44.621  231.729 1.00 55.24  ? 92  LYS B C     1 
ATOM   4466  O O     . LYS B  1 92  ? -16.081 45.387  232.611 1.00 58.94  ? 92  LYS B O     1 
ATOM   4467  C CB    . LYS B  1 92  ? -14.033 45.694  230.215 1.00 54.97  ? 92  LYS B CB    1 
ATOM   4468  C CG    . LYS B  1 92  ? -12.587 46.082  229.949 1.00 50.39  ? 92  LYS B CG    1 
ATOM   4469  C CD    . LYS B  1 92  ? -12.514 47.440  229.249 1.00 54.40  ? 92  LYS B CD    1 
ATOM   4470  C CE    . LYS B  1 92  ? -11.169 47.651  228.565 1.00 53.83  ? 92  LYS B CE    1 
ATOM   4471  N NZ    . LYS B  1 92  ? -10.024 47.572  229.514 1.00 68.82  ? 92  LYS B NZ    1 
ATOM   4472  N N     . GLY B  1 93  ? -16.509 43.772  231.108 1.00 54.11  ? 93  GLY B N     1 
ATOM   4473  C CA    . GLY B  1 93  ? -17.899 43.629  231.488 1.00 54.37  ? 93  GLY B CA    1 
ATOM   4474  C C     . GLY B  1 93  ? -18.116 42.549  232.535 1.00 55.09  ? 93  GLY B C     1 
ATOM   4475  O O     . GLY B  1 93  ? -17.179 42.100  233.196 1.00 54.41  ? 93  GLY B O     1 
ATOM   4476  N N     . SER B  1 94  ? -19.369 42.134  232.683 1.00 61.31  ? 94  SER B N     1 
ATOM   4477  C CA    . SER B  1 94  ? -19.748 41.112  233.649 1.00 63.90  ? 94  SER B CA    1 
ATOM   4478  C C     . SER B  1 94  ? -19.607 39.708  233.064 1.00 61.97  ? 94  SER B C     1 
ATOM   4479  O O     . SER B  1 94  ? -19.653 38.709  233.784 1.00 60.67  ? 94  SER B O     1 
ATOM   4480  C CB    . SER B  1 94  ? -21.188 41.340  234.104 1.00 75.50  ? 94  SER B CB    1 
ATOM   4481  O OG    . SER B  1 94  ? -22.074 41.301  232.996 1.00 74.41  ? 94  SER B OG    1 
ATOM   4482  N N     . TRP B  1 95  ? -19.419 39.656  231.750 1.00 55.53  ? 95  TRP B N     1 
ATOM   4483  C CA    . TRP B  1 95  ? -19.562 38.434  230.969 1.00 50.64  ? 95  TRP B CA    1 
ATOM   4484  C C     . TRP B  1 95  ? -18.656 37.277  231.376 1.00 50.89  ? 95  TRP B C     1 
ATOM   4485  O O     . TRP B  1 95  ? -17.480 37.463  231.694 1.00 51.39  ? 95  TRP B O     1 
ATOM   4486  C CB    . TRP B  1 95  ? -19.322 38.746  229.492 1.00 47.96  ? 95  TRP B CB    1 
ATOM   4487  C CG    . TRP B  1 95  ? -19.975 40.004  229.031 1.00 54.85  ? 95  TRP B CG    1 
ATOM   4488  C CD1   . TRP B  1 95  ? -19.386 41.224  228.879 1.00 50.47  ? 95  TRP B CD1   1 
ATOM   4489  C CD2   . TRP B  1 95  ? -21.349 40.172  228.659 1.00 52.32  ? 95  TRP B CD2   1 
ATOM   4490  N NE1   . TRP B  1 95  ? -20.306 42.142  228.433 1.00 54.75  ? 95  TRP B NE1   1 
ATOM   4491  C CE2   . TRP B  1 95  ? -21.519 41.521  228.290 1.00 53.59  ? 95  TRP B CE2   1 
ATOM   4492  C CE3   . TRP B  1 95  ? -22.450 39.311  228.600 1.00 49.68  ? 95  TRP B CE3   1 
ATOM   4493  C CZ2   . TRP B  1 95  ? -22.746 42.030  227.869 1.00 56.36  ? 95  TRP B CZ2   1 
ATOM   4494  C CZ3   . TRP B  1 95  ? -23.668 39.818  228.181 1.00 51.19  ? 95  TRP B CZ3   1 
ATOM   4495  C CH2   . TRP B  1 95  ? -23.806 41.166  227.821 1.00 52.61  ? 95  TRP B CH2   1 
ATOM   4496  N N     . THR B  1 96  ? -19.233 36.079  231.358 1.00 43.94  ? 96  THR B N     1 
ATOM   4497  C CA    . THR B  1 96  ? -18.480 34.836  231.442 1.00 40.94  ? 96  THR B CA    1 
ATOM   4498  C C     . THR B  1 96  ? -17.925 34.517  230.059 1.00 43.15  ? 96  THR B C     1 
ATOM   4499  O O     . THR B  1 96  ? -18.628 34.653  229.060 1.00 38.81  ? 96  THR B O     1 
ATOM   4500  C CB    . THR B  1 96  ? -19.361 33.667  231.941 1.00 44.77  ? 96  THR B CB    1 
ATOM   4501  O OG1   . THR B  1 96  ? -19.646 33.844  233.333 1.00 48.38  ? 96  THR B OG1   1 
ATOM   4502  C CG2   . THR B  1 96  ? -18.664 32.329  231.740 1.00 42.93  ? 96  THR B CG2   1 
ATOM   4503  N N     . ILE B  1 97  ? -16.662 34.116  229.998 1.00 42.31  ? 97  ILE B N     1 
ATOM   4504  C CA    . ILE B  1 97  ? -16.045 33.761  228.728 1.00 37.13  ? 97  ILE B CA    1 
ATOM   4505  C C     . ILE B  1 97  ? -16.305 32.297  228.381 1.00 33.35  ? 97  ILE B C     1 
ATOM   4506  O O     . ILE B  1 97  ? -16.217 31.423  229.243 1.00 34.54  ? 97  ILE B O     1 
ATOM   4507  C CB    . ILE B  1 97  ? -14.525 34.018  228.755 1.00 40.00  ? 97  ILE B CB    1 
ATOM   4508  C CG1   . ILE B  1 97  ? -14.247 35.520  228.817 1.00 37.47  ? 97  ILE B CG1   1 
ATOM   4509  C CG2   . ILE B  1 97  ? -13.851 33.413  227.538 1.00 32.14  ? 97  ILE B CG2   1 
ATOM   4510  C CD1   . ILE B  1 97  ? -12.782 35.874  228.962 1.00 39.65  ? 97  ILE B CD1   1 
ATOM   4511  N N     . ARG B  1 98  ? -16.644 32.038  227.122 1.00 33.03  ? 98  ARG B N     1 
ATOM   4512  C CA    . ARG B  1 98  ? -16.726 30.671  226.624 1.00 35.37  ? 98  ARG B CA    1 
ATOM   4513  C C     . ARG B  1 98  ? -15.930 30.536  225.336 1.00 35.51  ? 98  ARG B C     1 
ATOM   4514  O O     . ARG B  1 98  ? -16.079 31.335  224.411 1.00 35.69  ? 98  ARG B O     1 
ATOM   4515  C CB    . ARG B  1 98  ? -18.181 30.250  226.402 1.00 35.76  ? 98  ARG B CB    1 
ATOM   4516  C CG    . ARG B  1 98  ? -18.904 29.837  227.672 1.00 32.97  ? 98  ARG B CG    1 
ATOM   4517  C CD    . ARG B  1 98  ? -18.363 28.521  228.206 1.00 35.12  ? 98  ARG B CD    1 
ATOM   4518  N NE    . ARG B  1 98  ? -18.951 28.159  229.492 1.00 33.10  ? 98  ARG B NE    1 
ATOM   4519  C CZ    . ARG B  1 98  ? -18.432 28.480  230.673 1.00 42.12  ? 98  ARG B CZ    1 
ATOM   4520  N NH1   . ARG B  1 98  ? -17.304 29.177  230.742 1.00 36.17  ? 98  ARG B NH1   1 
ATOM   4521  N NH2   . ARG B  1 98  ? -19.042 28.105  231.790 1.00 40.02  ? 98  ARG B NH2   1 
ATOM   4522  N N     . LEU B  1 99  ? -15.073 29.522  225.289 1.00 29.00  ? 99  LEU B N     1 
ATOM   4523  C CA    . LEU B  1 99  ? -14.267 29.256  224.107 1.00 29.87  ? 99  LEU B CA    1 
ATOM   4524  C C     . LEU B  1 99  ? -14.797 28.031  223.389 1.00 31.91  ? 99  LEU B C     1 
ATOM   4525  O O     . LEU B  1 99  ? -15.170 27.050  224.027 1.00 31.30  ? 99  LEU B O     1 
ATOM   4526  C CB    . LEU B  1 99  ? -12.800 29.044  224.485 1.00 29.77  ? 99  LEU B CB    1 
ATOM   4527  C CG    . LEU B  1 99  ? -12.074 30.166  225.227 1.00 32.80  ? 99  LEU B CG    1 
ATOM   4528  C CD1   . LEU B  1 99  ? -10.716 29.672  225.718 1.00 36.34  ? 99  LEU B CD1   1 
ATOM   4529  C CD2   . LEU B  1 99  ? -11.917 31.392  224.339 1.00 36.59  ? 99  LEU B CD2   1 
ATOM   4530  N N     . ARG B  1 100 ? -14.831 28.083  222.063 1.00 31.11  ? 100 ARG B N     1 
ATOM   4531  C CA    . ARG B  1 100 ? -15.218 26.917  221.279 1.00 32.00  ? 100 ARG B CA    1 
ATOM   4532  C C     . ARG B  1 100 ? -14.307 26.720  220.075 1.00 33.86  ? 100 ARG B C     1 
ATOM   4533  O O     . ARG B  1 100 ? -14.041 27.656  219.320 1.00 32.91  ? 100 ARG B O     1 
ATOM   4534  C CB    . ARG B  1 100 ? -16.672 27.031  220.816 1.00 33.91  ? 100 ARG B CB    1 
ATOM   4535  C CG    . ARG B  1 100 ? -17.153 25.813  220.035 1.00 36.88  ? 100 ARG B CG    1 
ATOM   4536  C CD    . ARG B  1 100 ? -18.656 25.848  219.785 1.00 40.23  ? 100 ARG B CD    1 
ATOM   4537  N NE    . ARG B  1 100 ? -19.041 26.840  218.784 1.00 46.17  ? 100 ARG B NE    1 
ATOM   4538  C CZ    . ARG B  1 100 ? -20.296 27.072  218.411 1.00 44.08  ? 100 ARG B CZ    1 
ATOM   4539  N NH1   . ARG B  1 100 ? -20.559 27.990  217.492 1.00 39.81  ? 100 ARG B NH1   1 
ATOM   4540  N NH2   . ARG B  1 100 ? -21.290 26.384  218.958 1.00 37.64  ? 100 ARG B NH2   1 
ATOM   4541  N N     . SER B  1 101 ? -13.831 25.493  219.903 1.00 32.50  ? 101 SER B N     1 
ATOM   4542  C CA    . SER B  1 101 ? -13.073 25.133  218.715 1.00 33.67  ? 101 SER B CA    1 
ATOM   4543  C C     . SER B  1 101 ? -13.928 24.246  217.820 1.00 36.09  ? 101 SER B C     1 
ATOM   4544  O O     . SER B  1 101 ? -14.486 24.705  216.824 1.00 42.19  ? 101 SER B O     1 
ATOM   4545  C CB    . SER B  1 101 ? -11.771 24.421  219.089 1.00 35.89  ? 101 SER B CB    1 
ATOM   4546  O OG    . SER B  1 101 ? -11.082 23.980  217.933 1.00 36.20  ? 101 SER B OG    1 
ATOM   4547  N N     . GLY B  1 102 ? -14.038 22.974  218.191 1.00 37.43  ? 102 GLY B N     1 
ATOM   4548  C CA    . GLY B  1 102 ? -14.817 22.020  217.422 1.00 34.02  ? 102 GLY B CA    1 
ATOM   4549  C C     . GLY B  1 102 ? -16.215 21.817  217.976 1.00 39.68  ? 102 GLY B C     1 
ATOM   4550  O O     . GLY B  1 102 ? -17.076 21.241  217.310 1.00 40.02  ? 102 GLY B O     1 
ATOM   4551  N N     . GLY B  1 103 ? -16.436 22.280  219.203 1.00 36.44  ? 103 GLY B N     1 
ATOM   4552  C CA    . GLY B  1 103 ? -17.740 22.190  219.837 1.00 36.45  ? 103 GLY B CA    1 
ATOM   4553  C C     . GLY B  1 103 ? -18.185 20.774  220.149 1.00 38.99  ? 103 GLY B C     1 
ATOM   4554  O O     . GLY B  1 103 ? -19.382 20.486  220.168 1.00 34.19  ? 103 GLY B O     1 
ATOM   4555  N N     . HIS B  1 104 ? -17.225 19.890  220.403 1.00 35.34  ? 104 HIS B N     1 
ATOM   4556  C CA    . HIS B  1 104 ? -17.531 18.478  220.634 1.00 36.77  ? 104 HIS B CA    1 
ATOM   4557  C C     . HIS B  1 104 ? -17.688 18.133  222.104 1.00 35.85  ? 104 HIS B C     1 
ATOM   4558  O O     . HIS B  1 104 ? -17.805 16.958  222.454 1.00 35.53  ? 104 HIS B O     1 
ATOM   4559  C CB    . HIS B  1 104 ? -16.448 17.586  220.021 1.00 33.08  ? 104 HIS B CB    1 
ATOM   4560  C CG    . HIS B  1 104 ? -16.779 17.100  218.646 1.00 37.13  ? 104 HIS B CG    1 
ATOM   4561  N ND1   . HIS B  1 104 ? -17.500 15.946  218.419 1.00 38.71  ? 104 HIS B ND1   1 
ATOM   4562  C CD2   . HIS B  1 104 ? -16.499 17.618  217.428 1.00 35.22  ? 104 HIS B CD2   1 
ATOM   4563  C CE1   . HIS B  1 104 ? -17.650 15.777  217.117 1.00 37.41  ? 104 HIS B CE1   1 
ATOM   4564  N NE2   . HIS B  1 104 ? -17.051 16.774  216.493 1.00 37.37  ? 104 HIS B NE2   1 
ATOM   4565  N N     . SER B  1 105 ? -17.690 19.155  222.956 1.00 34.17  ? 105 SER B N     1 
ATOM   4566  C CA    . SER B  1 105 ? -17.874 18.967  224.392 1.00 34.10  ? 105 SER B CA    1 
ATOM   4567  C C     . SER B  1 105 ? -19.077 18.078  224.672 1.00 42.19  ? 105 SER B C     1 
ATOM   4568  O O     . SER B  1 105 ? -20.198 18.395  224.272 1.00 36.81  ? 105 SER B O     1 
ATOM   4569  C CB    . SER B  1 105 ? -18.044 20.312  225.097 1.00 37.06  ? 105 SER B CB    1 
ATOM   4570  O OG    . SER B  1 105 ? -18.409 20.129  226.454 1.00 39.67  ? 105 SER B OG    1 
ATOM   4571  N N     . TYR B  1 106 ? -18.827 16.958  225.342 1.00 38.72  ? 106 TYR B N     1 
ATOM   4572  C CA    . TYR B  1 106 ? -19.870 15.989  225.649 1.00 43.53  ? 106 TYR B CA    1 
ATOM   4573  C C     . TYR B  1 106 ? -20.989 16.613  226.478 1.00 46.68  ? 106 TYR B C     1 
ATOM   4574  O O     . TYR B  1 106 ? -22.139 16.177  226.411 1.00 45.94  ? 106 TYR B O     1 
ATOM   4575  C CB    . TYR B  1 106 ? -19.279 14.788  226.387 1.00 42.35  ? 106 TYR B CB    1 
ATOM   4576  C CG    . TYR B  1 106 ? -18.477 13.853  225.511 1.00 41.22  ? 106 TYR B CG    1 
ATOM   4577  C CD1   . TYR B  1 106 ? -18.479 13.988  224.129 1.00 41.79  ? 106 TYR B CD1   1 
ATOM   4578  C CD2   . TYR B  1 106 ? -17.728 12.829  226.067 1.00 41.53  ? 106 TYR B CD2   1 
ATOM   4579  C CE1   . TYR B  1 106 ? -17.752 13.130  223.326 1.00 41.75  ? 106 TYR B CE1   1 
ATOM   4580  C CE2   . TYR B  1 106 ? -17.002 11.965  225.276 1.00 45.19  ? 106 TYR B CE2   1 
ATOM   4581  C CZ    . TYR B  1 106 ? -17.016 12.119  223.910 1.00 45.95  ? 106 TYR B CZ    1 
ATOM   4582  O OH    . TYR B  1 106 ? -16.289 11.259  223.124 1.00 44.24  ? 106 TYR B OH    1 
ATOM   4583  N N     . GLU B  1 107 ? -20.645 17.642  227.247 1.00 47.18  ? 107 GLU B N     1 
ATOM   4584  C CA    . GLU B  1 107 ? -21.612 18.342  228.084 1.00 42.63  ? 107 GLU B CA    1 
ATOM   4585  C C     . GLU B  1 107 ? -21.930 19.742  227.559 1.00 36.24  ? 107 GLU B C     1 
ATOM   4586  O O     . GLU B  1 107 ? -22.516 20.559  228.272 1.00 36.75  ? 107 GLU B O     1 
ATOM   4587  C CB    . GLU B  1 107 ? -21.095 18.437  229.521 1.00 38.07  ? 107 GLU B CB    1 
ATOM   4588  C CG    . GLU B  1 107 ? -20.868 17.097  230.207 1.00 45.03  ? 107 GLU B CG    1 
ATOM   4589  C CD    . GLU B  1 107 ? -22.150 16.469  230.730 1.00 55.13  ? 107 GLU B CD    1 
ATOM   4590  O OE1   . GLU B  1 107 ? -23.247 16.915  230.334 1.00 48.84  ? 107 GLU B OE1   1 
ATOM   4591  O OE2   . GLU B  1 107 ? -22.060 15.526  231.543 1.00 53.97  ? 107 GLU B OE2   1 
ATOM   4592  N N     . GLY B  1 108 ? -21.538 20.019  226.319 1.00 37.16  ? 108 GLY B N     1 
ATOM   4593  C CA    . GLY B  1 108 ? -21.795 21.311  225.707 1.00 40.57  ? 108 GLY B CA    1 
ATOM   4594  C C     . GLY B  1 108 ? -21.223 22.479  226.491 1.00 43.68  ? 108 GLY B C     1 
ATOM   4595  O O     . GLY B  1 108 ? -21.789 23.570  226.497 1.00 39.68  ? 108 GLY B O     1 
ATOM   4596  N N     . LEU B  1 109 ? -20.090 22.246  227.146 1.00 35.67  ? 109 LEU B N     1 
ATOM   4597  C CA    . LEU B  1 109 ? -19.493 23.232  228.044 1.00 39.96  ? 109 LEU B CA    1 
ATOM   4598  C C     . LEU B  1 109 ? -18.811 24.380  227.305 1.00 37.97  ? 109 LEU B C     1 
ATOM   4599  O O     . LEU B  1 109 ? -18.384 25.357  227.923 1.00 41.33  ? 109 LEU B O     1 
ATOM   4600  C CB    . LEU B  1 109 ? -18.484 22.557  228.977 1.00 42.00  ? 109 LEU B CB    1 
ATOM   4601  C CG    . LEU B  1 109 ? -19.037 21.468  229.903 1.00 41.20  ? 109 LEU B CG    1 
ATOM   4602  C CD1   . LEU B  1 109 ? -17.974 20.990  230.890 1.00 45.89  ? 109 LEU B CD1   1 
ATOM   4603  C CD2   . LEU B  1 109 ? -20.274 21.961  230.638 1.00 39.77  ? 109 LEU B CD2   1 
ATOM   4604  N N     . SER B  1 110 ? -18.704 24.266  225.985 1.00 38.69  ? 110 SER B N     1 
ATOM   4605  C CA    . SER B  1 110 ? -18.030 25.291  225.197 1.00 42.47  ? 110 SER B CA    1 
ATOM   4606  C C     . SER B  1 110 ? -19.003 26.340  224.675 1.00 39.46  ? 110 SER B C     1 
ATOM   4607  O O     . SER B  1 110 ? -18.585 27.371  224.154 1.00 36.85  ? 110 SER B O     1 
ATOM   4608  C CB    . SER B  1 110 ? -17.273 24.664  224.026 1.00 34.99  ? 110 SER B CB    1 
ATOM   4609  O OG    . SER B  1 110 ? -18.119 23.842  223.240 1.00 37.32  ? 110 SER B OG    1 
ATOM   4610  N N     . TYR B  1 111 ? -20.298 26.078  224.814 1.00 39.79  ? 111 TYR B N     1 
ATOM   4611  C CA    . TYR B  1 111 ? -21.299 27.016  224.322 1.00 39.68  ? 111 TYR B CA    1 
ATOM   4612  C C     . TYR B  1 111 ? -22.508 27.138  225.250 1.00 38.14  ? 111 TYR B C     1 
ATOM   4613  O O     . TYR B  1 111 ? -23.579 27.565  224.821 1.00 40.16  ? 111 TYR B O     1 
ATOM   4614  C CB    . TYR B  1 111 ? -21.751 26.615  222.911 1.00 37.65  ? 111 TYR B CB    1 
ATOM   4615  C CG    . TYR B  1 111 ? -22.132 25.156  222.760 1.00 39.33  ? 111 TYR B CG    1 
ATOM   4616  C CD1   . TYR B  1 111 ? -23.445 24.739  222.937 1.00 44.44  ? 111 TYR B CD1   1 
ATOM   4617  C CD2   . TYR B  1 111 ? -21.179 24.196  222.432 1.00 37.67  ? 111 TYR B CD2   1 
ATOM   4618  C CE1   . TYR B  1 111 ? -23.799 23.407  222.798 1.00 39.73  ? 111 TYR B CE1   1 
ATOM   4619  C CE2   . TYR B  1 111 ? -21.525 22.858  222.292 1.00 41.53  ? 111 TYR B CE2   1 
ATOM   4620  C CZ    . TYR B  1 111 ? -22.841 22.473  222.476 1.00 40.37  ? 111 TYR B CZ    1 
ATOM   4621  O OH    . TYR B  1 111 ? -23.194 21.148  222.339 1.00 35.32  ? 111 TYR B OH    1 
ATOM   4622  N N     . THR B  1 112 ? -22.341 26.760  226.515 1.00 38.99  ? 112 THR B N     1 
ATOM   4623  C CA    . THR B  1 112 ? -23.391 26.950  227.513 1.00 38.44  ? 112 THR B CA    1 
ATOM   4624  C C     . THR B  1 112 ? -22.806 27.475  228.817 1.00 43.62  ? 112 THR B C     1 
ATOM   4625  O O     . THR B  1 112 ? -21.643 27.217  229.134 1.00 38.74  ? 112 THR B O     1 
ATOM   4626  C CB    . THR B  1 112 ? -24.163 25.640  227.813 1.00 42.57  ? 112 THR B CB    1 
ATOM   4627  O OG1   . THR B  1 112 ? -23.288 24.695  228.444 1.00 41.64  ? 112 THR B OG1   1 
ATOM   4628  C CG2   . THR B  1 112 ? -24.730 25.040  226.541 1.00 41.24  ? 112 THR B CG2   1 
ATOM   4629  N N     . SER B  1 113 ? -23.618 28.208  229.573 1.00 37.76  ? 113 SER B N     1 
ATOM   4630  C CA    . SER B  1 113 ? -23.204 28.743  230.866 1.00 46.58  ? 113 SER B CA    1 
ATOM   4631  C C     . SER B  1 113 ? -24.418 29.207  231.673 1.00 51.84  ? 113 SER B C     1 
ATOM   4632  O O     . SER B  1 113 ? -25.348 29.801  231.125 1.00 49.27  ? 113 SER B O     1 
ATOM   4633  C CB    . SER B  1 113 ? -22.216 29.898  230.681 1.00 42.35  ? 113 SER B CB    1 
ATOM   4634  O OG    . SER B  1 113 ? -22.004 30.588  231.899 1.00 44.50  ? 113 SER B OG    1 
ATOM   4635  N N     . ASP B  1 114 ? -24.406 28.936  232.975 1.00 55.64  ? 114 ASP B N     1 
ATOM   4636  C CA    . ASP B  1 114 ? -25.520 29.304  233.842 1.00 57.10  ? 114 ASP B CA    1 
ATOM   4637  C C     . ASP B  1 114 ? -25.509 30.796  234.173 1.00 59.10  ? 114 ASP B C     1 
ATOM   4638  O O     . ASP B  1 114 ? -26.343 31.279  234.937 1.00 62.52  ? 114 ASP B O     1 
ATOM   4639  C CB    . ASP B  1 114 ? -25.495 28.477  235.130 1.00 60.24  ? 114 ASP B CB    1 
ATOM   4640  C CG    . ASP B  1 114 ? -24.203 28.640  235.907 1.00 76.90  ? 114 ASP B CG    1 
ATOM   4641  O OD1   . ASP B  1 114 ? -23.200 29.082  235.309 1.00 68.64  ? 114 ASP B OD1   1 
ATOM   4642  O OD2   . ASP B  1 114 ? -24.189 28.319  237.115 1.00 91.15  ? 114 ASP B OD2   1 
ATOM   4643  N N     . THR B  1 115 ? -24.555 31.517  233.594 1.00 50.05  ? 115 THR B N     1 
ATOM   4644  C CA    . THR B  1 115 ? -24.484 32.968  233.722 1.00 52.86  ? 115 THR B CA    1 
ATOM   4645  C C     . THR B  1 115 ? -24.411 33.578  232.325 1.00 50.22  ? 115 THR B C     1 
ATOM   4646  O O     . THR B  1 115 ? -24.055 32.881  231.374 1.00 51.10  ? 115 THR B O     1 
ATOM   4647  C CB    . THR B  1 115 ? -23.261 33.407  234.565 1.00 55.91  ? 115 THR B CB    1 
ATOM   4648  O OG1   . THR B  1 115 ? -22.063 32.853  234.005 1.00 54.33  ? 115 THR B OG1   1 
ATOM   4649  C CG2   . THR B  1 115 ? -23.407 32.928  236.001 1.00 54.29  ? 115 THR B CG2   1 
ATOM   4650  N N     . PRO B  1 116 ? -24.781 34.867  232.186 1.00 47.56  ? 116 PRO B N     1 
ATOM   4651  C CA    . PRO B  1 116 ? -24.635 35.535  230.886 1.00 49.98  ? 116 PRO B CA    1 
ATOM   4652  C C     . PRO B  1 116 ? -23.224 35.383  230.346 1.00 47.61  ? 116 PRO B C     1 
ATOM   4653  O O     . PRO B  1 116 ? -22.268 35.578  231.095 1.00 43.64  ? 116 PRO B O     1 
ATOM   4654  C CB    . PRO B  1 116 ? -24.937 37.000  231.205 1.00 43.13  ? 116 PRO B CB    1 
ATOM   4655  C CG    . PRO B  1 116 ? -25.853 36.940  232.363 1.00 46.70  ? 116 PRO B CG    1 
ATOM   4656  C CD    . PRO B  1 116 ? -25.428 35.744  233.178 1.00 48.78  ? 116 PRO B CD    1 
ATOM   4657  N N     . PHE B  1 117 ? -23.083 35.028  229.076 1.00 45.39  ? 117 PHE B N     1 
ATOM   4658  C CA    . PHE B  1 117 ? -21.750 34.768  228.556 1.00 41.49  ? 117 PHE B CA    1 
ATOM   4659  C C     . PHE B  1 117 ? -21.566 35.211  227.115 1.00 41.83  ? 117 PHE B C     1 
ATOM   4660  O O     . PHE B  1 117 ? -22.529 35.394  226.371 1.00 39.27  ? 117 PHE B O     1 
ATOM   4661  C CB    . PHE B  1 117 ? -21.405 33.277  228.695 1.00 36.31  ? 117 PHE B CB    1 
ATOM   4662  C CG    . PHE B  1 117 ? -22.275 32.356  227.883 1.00 40.97  ? 117 PHE B CG    1 
ATOM   4663  C CD1   . PHE B  1 117 ? -21.759 31.685  226.785 1.00 37.39  ? 117 PHE B CD1   1 
ATOM   4664  C CD2   . PHE B  1 117 ? -23.597 32.138  228.231 1.00 43.28  ? 117 PHE B CD2   1 
ATOM   4665  C CE1   . PHE B  1 117 ? -22.547 30.827  226.047 1.00 40.21  ? 117 PHE B CE1   1 
ATOM   4666  C CE2   . PHE B  1 117 ? -24.389 31.286  227.492 1.00 41.12  ? 117 PHE B CE2   1 
ATOM   4667  C CZ    . PHE B  1 117 ? -23.864 30.627  226.400 1.00 41.57  ? 117 PHE B CZ    1 
ATOM   4668  N N     . ILE B  1 118 ? -20.306 35.399  226.744 1.00 40.94  ? 118 ILE B N     1 
ATOM   4669  C CA    . ILE B  1 118 ? -19.937 35.702  225.374 1.00 35.14  ? 118 ILE B CA    1 
ATOM   4670  C C     . ILE B  1 118 ? -19.216 34.502  224.784 1.00 39.03  ? 118 ILE B C     1 
ATOM   4671  O O     . ILE B  1 118 ? -18.367 33.892  225.438 1.00 39.85  ? 118 ILE B O     1 
ATOM   4672  C CB    . ILE B  1 118 ? -19.043 36.952  225.287 1.00 37.00  ? 118 ILE B CB    1 
ATOM   4673  C CG1   . ILE B  1 118 ? -19.752 38.148  225.917 1.00 39.18  ? 118 ILE B CG1   1 
ATOM   4674  C CG2   . ILE B  1 118 ? -18.708 37.261  223.843 1.00 31.22  ? 118 ILE B CG2   1 
ATOM   4675  C CD1   . ILE B  1 118 ? -20.998 38.562  225.171 1.00 35.77  ? 118 ILE B CD1   1 
ATOM   4676  N N     . LEU B  1 119 ? -19.563 34.149  223.553 1.00 37.51  ? 119 LEU B N     1 
ATOM   4677  C CA    . LEU B  1 119 ? -18.947 33.001  222.905 1.00 36.52  ? 119 LEU B CA    1 
ATOM   4678  C C     . LEU B  1 119 ? -17.850 33.423  221.945 1.00 36.30  ? 119 LEU B C     1 
ATOM   4679  O O     . LEU B  1 119 ? -18.106 34.119  220.963 1.00 34.67  ? 119 LEU B O     1 
ATOM   4680  C CB    . LEU B  1 119 ? -19.996 32.176  222.157 1.00 36.72  ? 119 LEU B CB    1 
ATOM   4681  C CG    . LEU B  1 119 ? -19.483 30.968  221.367 1.00 42.56  ? 119 LEU B CG    1 
ATOM   4682  C CD1   . LEU B  1 119 ? -18.602 30.074  222.229 1.00 35.06  ? 119 LEU B CD1   1 
ATOM   4683  C CD2   . LEU B  1 119 ? -20.656 30.173  220.787 1.00 38.73  ? 119 LEU B CD2   1 
ATOM   4684  N N     . ILE B  1 120 ? -16.626 33.001  222.240 1.00 37.17  ? 120 ILE B N     1 
ATOM   4685  C CA    . ILE B  1 120 ? -15.513 33.182  221.322 1.00 34.80  ? 120 ILE B CA    1 
ATOM   4686  C C     . ILE B  1 120 ? -15.376 31.929  220.468 1.00 33.57  ? 120 ILE B C     1 
ATOM   4687  O O     . ILE B  1 120 ? -14.993 30.872  220.965 1.00 37.53  ? 120 ILE B O     1 
ATOM   4688  C CB    . ILE B  1 120 ? -14.189 33.454  222.066 1.00 32.39  ? 120 ILE B CB    1 
ATOM   4689  C CG1   . ILE B  1 120 ? -14.347 34.628  223.033 1.00 38.12  ? 120 ILE B CG1   1 
ATOM   4690  C CG2   . ILE B  1 120 ? -13.064 33.727  221.077 1.00 28.06  ? 120 ILE B CG2   1 
ATOM   4691  C CD1   . ILE B  1 120 ? -13.092 34.939  223.824 1.00 35.88  ? 120 ILE B CD1   1 
ATOM   4692  N N     . ASP B  1 121 ? -15.708 32.042  219.187 1.00 36.43  ? 121 ASP B N     1 
ATOM   4693  C CA    . ASP B  1 121 ? -15.597 30.908  218.282 1.00 39.39  ? 121 ASP B CA    1 
ATOM   4694  C C     . ASP B  1 121 ? -14.326 31.025  217.449 1.00 36.25  ? 121 ASP B C     1 
ATOM   4695  O O     . ASP B  1 121 ? -14.062 32.064  216.843 1.00 37.62  ? 121 ASP B O     1 
ATOM   4696  C CB    . ASP B  1 121 ? -16.826 30.812  217.377 1.00 39.41  ? 121 ASP B CB    1 
ATOM   4697  C CG    . ASP B  1 121 ? -16.932 29.468  216.683 1.00 41.12  ? 121 ASP B CG    1 
ATOM   4698  O OD1   . ASP B  1 121 ? -17.863 28.700  217.006 1.00 52.46  ? 121 ASP B OD1   1 
ATOM   4699  O OD2   . ASP B  1 121 ? -16.076 29.172  215.824 1.00 47.39  ? 121 ASP B OD2   1 
ATOM   4700  N N     . LEU B  1 122 ? -13.551 29.946  217.410 1.00 38.23  ? 122 LEU B N     1 
ATOM   4701  C CA    . LEU B  1 122 ? -12.207 29.982  216.842 1.00 36.75  ? 122 LEU B CA    1 
ATOM   4702  C C     . LEU B  1 122 ? -12.122 29.423  215.425 1.00 36.80  ? 122 LEU B C     1 
ATOM   4703  O O     . LEU B  1 122 ? -11.026 29.156  214.931 1.00 41.73  ? 122 LEU B O     1 
ATOM   4704  C CB    . LEU B  1 122 ? -11.248 29.212  217.751 1.00 32.08  ? 122 LEU B CB    1 
ATOM   4705  C CG    . LEU B  1 122 ? -11.225 29.699  219.199 1.00 35.16  ? 122 LEU B CG    1 
ATOM   4706  C CD1   . LEU B  1 122 ? -10.515 28.701  220.082 1.00 31.57  ? 122 LEU B CD1   1 
ATOM   4707  C CD2   . LEU B  1 122 ? -10.557 31.062  219.289 1.00 37.32  ? 122 LEU B CD2   1 
ATOM   4708  N N     . MET B  1 123 ? -13.269 29.261  214.770 1.00 40.37  ? 123 MET B N     1 
ATOM   4709  C CA    . MET B  1 123 ? -13.322 28.611  213.460 1.00 43.57  ? 123 MET B CA    1 
ATOM   4710  C C     . MET B  1 123 ? -12.526 29.354  212.384 1.00 38.41  ? 123 MET B C     1 
ATOM   4711  O O     . MET B  1 123 ? -12.143 28.767  211.375 1.00 42.14  ? 123 MET B O     1 
ATOM   4712  C CB    . MET B  1 123 ? -14.775 28.452  213.000 1.00 43.89  ? 123 MET B CB    1 
ATOM   4713  C CG    . MET B  1 123 ? -15.449 29.754  212.595 1.00 46.75  ? 123 MET B CG    1 
ATOM   4714  S SD    . MET B  1 123 ? -17.088 29.507  211.886 1.00 55.03  ? 123 MET B SD    1 
ATOM   4715  C CE    . MET B  1 123 ? -17.969 28.828  213.288 1.00 48.35  ? 123 MET B CE    1 
ATOM   4716  N N     . ASN B  1 124 ? -12.286 30.644  212.595 1.00 42.46  ? 124 ASN B N     1 
ATOM   4717  C CA    . ASN B  1 124 ? -11.497 31.428  211.652 1.00 42.20  ? 124 ASN B CA    1 
ATOM   4718  C C     . ASN B  1 124 ? -10.005 31.310  211.931 1.00 40.46  ? 124 ASN B C     1 
ATOM   4719  O O     . ASN B  1 124 ? -9.174  31.768  211.145 1.00 44.19  ? 124 ASN B O     1 
ATOM   4720  C CB    . ASN B  1 124 ? -11.923 32.892  211.682 1.00 38.16  ? 124 ASN B CB    1 
ATOM   4721  C CG    . ASN B  1 124 ? -13.307 33.097  211.105 1.00 49.26  ? 124 ASN B CG    1 
ATOM   4722  O OD1   . ASN B  1 124 ? -13.846 32.213  210.440 1.00 41.60  ? 124 ASN B OD1   1 
ATOM   4723  N ND2   . ASN B  1 124 ? -13.887 34.266  211.349 1.00 44.45  ? 124 ASN B ND2   1 
ATOM   4724  N N     . LEU B  1 125 ? -9.677  30.697  213.062 1.00 38.21  ? 125 LEU B N     1 
ATOM   4725  C CA    . LEU B  1 125 ? -8.295  30.391  213.401 1.00 43.36  ? 125 LEU B CA    1 
ATOM   4726  C C     . LEU B  1 125 ? -8.023  28.918  213.117 1.00 40.66  ? 125 LEU B C     1 
ATOM   4727  O O     . LEU B  1 125 ? -7.814  28.129  214.034 1.00 36.53  ? 125 LEU B O     1 
ATOM   4728  C CB    . LEU B  1 125 ? -8.012  30.726  214.866 1.00 38.70  ? 125 LEU B CB    1 
ATOM   4729  C CG    . LEU B  1 125 ? -8.194  32.196  215.242 1.00 41.34  ? 125 LEU B CG    1 
ATOM   4730  C CD1   . LEU B  1 125 ? -7.969  32.405  216.724 1.00 39.78  ? 125 LEU B CD1   1 
ATOM   4731  C CD2   . LEU B  1 125 ? -7.246  33.060  214.432 1.00 41.60  ? 125 LEU B CD2   1 
ATOM   4732  N N     . ASN B  1 126 ? -8.042  28.547  211.841 1.00 41.49  ? 126 ASN B N     1 
ATOM   4733  C CA    . ASN B  1 126 ? -7.853  27.152  211.462 1.00 40.00  ? 126 ASN B CA    1 
ATOM   4734  C C     . ASN B  1 126 ? -6.687  26.947  210.507 1.00 47.48  ? 126 ASN B C     1 
ATOM   4735  O O     . ASN B  1 126 ? -6.743  26.086  209.631 1.00 49.58  ? 126 ASN B O     1 
ATOM   4736  C CB    . ASN B  1 126 ? -9.132  26.594  210.835 1.00 49.21  ? 126 ASN B CB    1 
ATOM   4737  C CG    . ASN B  1 126 ? -9.544  27.341  209.578 1.00 50.74  ? 126 ASN B CG    1 
ATOM   4738  O OD1   . ASN B  1 126 ? -9.051  28.434  209.297 1.00 49.74  ? 126 ASN B OD1   1 
ATOM   4739  N ND2   . ASN B  1 126 ? -10.456 26.750  208.814 1.00 52.26  ? 126 ASN B ND2   1 
ATOM   4740  N N     . ARG B  1 127 ? -5.633  27.738  210.678 1.00 41.80  ? 127 ARG B N     1 
ATOM   4741  C CA    . ARG B  1 127 ? -4.463  27.644  209.813 1.00 41.55  ? 127 ARG B CA    1 
ATOM   4742  C C     . ARG B  1 127 ? -3.475  26.605  210.320 1.00 47.28  ? 127 ARG B C     1 
ATOM   4743  O O     . ARG B  1 127 ? -3.242  26.495  211.522 1.00 43.44  ? 127 ARG B O     1 
ATOM   4744  C CB    . ARG B  1 127 ? -3.762  28.995  209.704 1.00 47.32  ? 127 ARG B CB    1 
ATOM   4745  C CG    . ARG B  1 127 ? -4.613  30.097  209.121 1.00 52.11  ? 127 ARG B CG    1 
ATOM   4746  C CD    . ARG B  1 127 ? -3.957  31.443  209.353 1.00 53.58  ? 127 ARG B CD    1 
ATOM   4747  N NE    . ARG B  1 127 ? -4.821  32.549  208.958 1.00 62.28  ? 127 ARG B NE    1 
ATOM   4748  C CZ    . ARG B  1 127 ? -5.839  33.001  209.685 1.00 65.68  ? 127 ARG B CZ    1 
ATOM   4749  N NH1   . ARG B  1 127 ? -6.138  32.438  210.849 1.00 55.34  ? 127 ARG B NH1   1 
ATOM   4750  N NH2   . ARG B  1 127 ? -6.566  34.018  209.241 1.00 74.58  ? 127 ARG B NH2   1 
ATOM   4751  N N     . VAL B  1 128 ? -2.887  25.853  209.396 1.00 45.71  ? 128 VAL B N     1 
ATOM   4752  C CA    . VAL B  1 128 ? -1.863  24.879  209.745 1.00 45.64  ? 128 VAL B CA    1 
ATOM   4753  C C     . VAL B  1 128 ? -0.574  25.194  208.997 1.00 48.17  ? 128 VAL B C     1 
ATOM   4754  O O     . VAL B  1 128 ? -0.578  25.346  207.777 1.00 51.80  ? 128 VAL B O     1 
ATOM   4755  C CB    . VAL B  1 128 ? -2.310  23.439  209.422 1.00 48.76  ? 128 VAL B CB    1 
ATOM   4756  C CG1   . VAL B  1 128 ? -1.184  22.454  209.700 1.00 48.22  ? 128 VAL B CG1   1 
ATOM   4757  C CG2   . VAL B  1 128 ? -3.546  23.077  210.227 1.00 45.60  ? 128 VAL B CG2   1 
ATOM   4758  N N     . SER B  1 129 ? 0.524   25.308  209.736 1.00 48.24  ? 129 SER B N     1 
ATOM   4759  C CA    . SER B  1 129 ? 1.819   25.601  209.138 1.00 47.04  ? 129 SER B CA    1 
ATOM   4760  C C     . SER B  1 129 ? 2.802   24.478  209.432 1.00 52.44  ? 129 SER B C     1 
ATOM   4761  O O     . SER B  1 129 ? 3.178   24.259  210.582 1.00 51.94  ? 129 SER B O     1 
ATOM   4762  C CB    . SER B  1 129 ? 2.365   26.933  209.653 1.00 45.35  ? 129 SER B CB    1 
ATOM   4763  O OG    . SER B  1 129 ? 3.632   27.215  209.086 1.00 56.98  ? 129 SER B OG    1 
ATOM   4764  N N     . ILE B  1 130 ? 3.220   23.771  208.388 1.00 52.91  ? 130 ILE B N     1 
ATOM   4765  C CA    . ILE B  1 130 ? 4.055   22.588  208.553 1.00 52.24  ? 130 ILE B CA    1 
ATOM   4766  C C     . ILE B  1 130 ? 5.521   22.855  208.222 1.00 61.13  ? 130 ILE B C     1 
ATOM   4767  O O     . ILE B  1 130 ? 5.840   23.501  207.223 1.00 60.91  ? 130 ILE B O     1 
ATOM   4768  C CB    . ILE B  1 130 ? 3.530   21.432  207.677 1.00 56.96  ? 130 ILE B CB    1 
ATOM   4769  C CG1   . ILE B  1 130 ? 2.154   20.988  208.168 1.00 55.23  ? 130 ILE B CG1   1 
ATOM   4770  C CG2   . ILE B  1 130 ? 4.491   20.256  207.689 1.00 55.29  ? 130 ILE B CG2   1 
ATOM   4771  C CD1   . ILE B  1 130 ? 1.553   19.883  207.350 1.00 55.68  ? 130 ILE B CD1   1 
ATOM   4772  N N     . ASP B  1 131 ? 6.407   22.364  209.082 1.00 59.36  ? 131 ASP B N     1 
ATOM   4773  C CA    . ASP B  1 131 ? 7.843   22.439  208.851 1.00 57.89  ? 131 ASP B CA    1 
ATOM   4774  C C     . ASP B  1 131 ? 8.385   21.031  208.609 1.00 60.72  ? 131 ASP B C     1 
ATOM   4775  O O     . ASP B  1 131 ? 8.521   20.241  209.540 1.00 59.55  ? 131 ASP B O     1 
ATOM   4776  C CB    . ASP B  1 131 ? 8.540   23.105  210.041 1.00 58.38  ? 131 ASP B CB    1 
ATOM   4777  C CG    . ASP B  1 131 ? 10.040  23.245  209.847 1.00 66.47  ? 131 ASP B CG    1 
ATOM   4778  O OD1   . ASP B  1 131 ? 10.546  22.951  208.742 1.00 67.05  ? 131 ASP B OD1   1 
ATOM   4779  O OD2   . ASP B  1 131 ? 10.717  23.667  210.809 1.00 69.42  ? 131 ASP B OD2   1 
ATOM   4780  N N     . LEU B  1 132 ? 8.686   20.723  207.352 1.00 66.01  ? 132 LEU B N     1 
ATOM   4781  C CA    . LEU B  1 132 ? 9.117   19.381  206.969 1.00 62.01  ? 132 LEU B CA    1 
ATOM   4782  C C     . LEU B  1 132 ? 10.550  19.064  207.395 1.00 65.49  ? 132 LEU B C     1 
ATOM   4783  O O     . LEU B  1 132 ? 10.962  17.905  207.382 1.00 69.15  ? 132 LEU B O     1 
ATOM   4784  C CB    . LEU B  1 132 ? 8.978   19.196  205.456 1.00 60.99  ? 132 LEU B CB    1 
ATOM   4785  C CG    . LEU B  1 132 ? 7.551   19.130  204.905 1.00 63.22  ? 132 LEU B CG    1 
ATOM   4786  C CD1   . LEU B  1 132 ? 7.554   19.312  203.399 1.00 69.23  ? 132 LEU B CD1   1 
ATOM   4787  C CD2   . LEU B  1 132 ? 6.893   17.811  205.275 1.00 59.53  ? 132 LEU B CD2   1 
ATOM   4788  N N     . GLU B  1 133 ? 11.309  20.088  207.773 1.00 67.17  ? 133 GLU B N     1 
ATOM   4789  C CA    . GLU B  1 133 ? 12.710  19.887  208.136 1.00 70.13  ? 133 GLU B CA    1 
ATOM   4790  C C     . GLU B  1 133 ? 12.899  19.516  209.606 1.00 66.91  ? 133 GLU B C     1 
ATOM   4791  O O     . GLU B  1 133 ? 13.658  18.600  209.924 1.00 62.37  ? 133 GLU B O     1 
ATOM   4792  C CB    . GLU B  1 133 ? 13.530  21.132  207.795 1.00 75.02  ? 133 GLU B CB    1 
ATOM   4793  C CG    . GLU B  1 133 ? 14.123  21.088  206.400 1.00 86.76  ? 133 GLU B CG    1 
ATOM   4794  C CD    . GLU B  1 133 ? 14.709  22.410  205.959 1.00 100.13 ? 133 GLU B CD    1 
ATOM   4795  O OE1   . GLU B  1 133 ? 15.237  23.147  206.818 1.00 104.41 ? 133 GLU B OE1   1 
ATOM   4796  O OE2   . GLU B  1 133 ? 14.634  22.714  204.750 1.00 101.45 ? 133 GLU B OE2   1 
ATOM   4797  N N     . SER B  1 134 ? 12.211  20.218  210.499 1.00 67.42  ? 134 SER B N     1 
ATOM   4798  C CA    . SER B  1 134 ? 12.270  19.886  211.916 1.00 61.85  ? 134 SER B CA    1 
ATOM   4799  C C     . SER B  1 134 ? 11.159  18.898  212.251 1.00 61.27  ? 134 SER B C     1 
ATOM   4800  O O     . SER B  1 134 ? 11.074  18.390  213.372 1.00 60.72  ? 134 SER B O     1 
ATOM   4801  C CB    . SER B  1 134 ? 12.163  21.149  212.774 1.00 60.03  ? 134 SER B CB    1 
ATOM   4802  O OG    . SER B  1 134 ? 11.026  21.917  212.420 1.00 62.82  ? 134 SER B OG    1 
ATOM   4803  N N     . GLU B  1 135 ? 10.327  18.625  211.248 1.00 54.79  ? 135 GLU B N     1 
ATOM   4804  C CA    . GLU B  1 135 ? 9.170   17.741  211.371 1.00 61.80  ? 135 GLU B CA    1 
ATOM   4805  C C     . GLU B  1 135 ? 8.261   18.164  212.519 1.00 56.34  ? 135 GLU B C     1 
ATOM   4806  O O     . GLU B  1 135 ? 7.924   17.374  213.399 1.00 50.50  ? 135 GLU B O     1 
ATOM   4807  C CB    . GLU B  1 135 ? 9.623   16.289  211.527 1.00 57.28  ? 135 GLU B CB    1 
ATOM   4808  C CG    . GLU B  1 135 ? 10.050  15.668  210.201 1.00 64.30  ? 135 GLU B CG    1 
ATOM   4809  C CD    . GLU B  1 135 ? 10.849  14.396  210.373 1.00 64.45  ? 135 GLU B CD    1 
ATOM   4810  O OE1   . GLU B  1 135 ? 11.336  14.148  211.495 1.00 66.70  ? 135 GLU B OE1   1 
ATOM   4811  O OE2   . GLU B  1 135 ? 10.989  13.647  209.384 1.00 71.36  ? 135 GLU B OE2   1 
ATOM   4812  N N     . THR B  1 136 ? 7.876   19.434  212.488 1.00 56.85  ? 136 THR B N     1 
ATOM   4813  C CA    . THR B  1 136 ? 6.906   19.980  213.421 1.00 52.36  ? 136 THR B CA    1 
ATOM   4814  C C     . THR B  1 136 ? 5.814   20.693  212.641 1.00 53.12  ? 136 THR B C     1 
ATOM   4815  O O     . THR B  1 136 ? 5.892   20.812  211.419 1.00 55.12  ? 136 THR B O     1 
ATOM   4816  C CB    . THR B  1 136 ? 7.542   20.967  214.410 1.00 48.66  ? 136 THR B CB    1 
ATOM   4817  O OG1   . THR B  1 136 ? 8.118   22.063  213.688 1.00 57.54  ? 136 THR B OG1   1 
ATOM   4818  C CG2   . THR B  1 136 ? 8.621   20.282  215.229 1.00 51.65  ? 136 THR B CG2   1 
ATOM   4819  N N     . ALA B  1 137 ? 4.800   21.170  213.350 1.00 52.37  ? 137 ALA B N     1 
ATOM   4820  C CA    . ALA B  1 137 ? 3.754   21.969  212.731 1.00 47.03  ? 137 ALA B CA    1 
ATOM   4821  C C     . ALA B  1 137 ? 3.139   22.910  213.751 1.00 42.01  ? 137 ALA B C     1 
ATOM   4822  O O     . ALA B  1 137 ? 2.938   22.535  214.906 1.00 40.70  ? 137 ALA B O     1 
ATOM   4823  C CB    . ALA B  1 137 ? 2.686   21.077  212.121 1.00 48.21  ? 137 ALA B CB    1 
ATOM   4824  N N     . TRP B  1 138 ? 2.858   24.137  213.328 1.00 43.84  ? 138 TRP B N     1 
ATOM   4825  C CA    . TRP B  1 138 ? 2.061   25.049  214.135 1.00 42.14  ? 138 TRP B CA    1 
ATOM   4826  C C     . TRP B  1 138 ? 0.603   24.920  213.721 1.00 41.61  ? 138 TRP B C     1 
ATOM   4827  O O     . TRP B  1 138 ? 0.277   24.999  212.538 1.00 45.45  ? 138 TRP B O     1 
ATOM   4828  C CB    . TRP B  1 138 ? 2.536   26.495  213.984 1.00 43.38  ? 138 TRP B CB    1 
ATOM   4829  C CG    . TRP B  1 138 ? 3.691   26.850  214.871 1.00 42.91  ? 138 TRP B CG    1 
ATOM   4830  C CD1   . TRP B  1 138 ? 4.997   26.982  214.501 1.00 42.71  ? 138 TRP B CD1   1 
ATOM   4831  C CD2   . TRP B  1 138 ? 3.642   27.120  216.278 1.00 39.95  ? 138 TRP B CD2   1 
ATOM   4832  N NE1   . TRP B  1 138 ? 5.765   27.317  215.589 1.00 41.51  ? 138 TRP B NE1   1 
ATOM   4833  C CE2   . TRP B  1 138 ? 4.957   27.408  216.692 1.00 45.08  ? 138 TRP B CE2   1 
ATOM   4834  C CE3   . TRP B  1 138 ? 2.615   27.146  217.228 1.00 42.66  ? 138 TRP B CE3   1 
ATOM   4835  C CZ2   . TRP B  1 138 ? 5.273   27.718  218.014 1.00 45.03  ? 138 TRP B CZ2   1 
ATOM   4836  C CZ3   . TRP B  1 138 ? 2.931   27.454  218.539 1.00 39.11  ? 138 TRP B CZ3   1 
ATOM   4837  C CH2   . TRP B  1 138 ? 4.249   27.735  218.920 1.00 42.38  ? 138 TRP B CH2   1 
ATOM   4838  N N     . VAL B  1 139 ? -0.269  24.707  214.701 1.00 37.27  ? 139 VAL B N     1 
ATOM   4839  C CA    . VAL B  1 139 ? -1.684  24.488  214.431 1.00 31.62  ? 139 VAL B CA    1 
ATOM   4840  C C     . VAL B  1 139 ? -2.558  25.449  215.224 1.00 31.79  ? 139 VAL B C     1 
ATOM   4841  O O     . VAL B  1 139 ? -2.647  25.345  216.447 1.00 32.52  ? 139 VAL B O     1 
ATOM   4842  C CB    . VAL B  1 139 ? -2.104  23.047  214.772 1.00 33.91  ? 139 VAL B CB    1 
ATOM   4843  C CG1   . VAL B  1 139 ? -3.518  22.780  214.286 1.00 35.35  ? 139 VAL B CG1   1 
ATOM   4844  C CG2   . VAL B  1 139 ? -1.129  22.044  214.174 1.00 36.39  ? 139 VAL B CG2   1 
ATOM   4845  N N     . GLU B  1 140 ? -3.202  26.383  214.530 1.00 32.78  ? 140 GLU B N     1 
ATOM   4846  C CA    . GLU B  1 140 ? -4.136  27.290  215.186 1.00 34.97  ? 140 GLU B CA    1 
ATOM   4847  C C     . GLU B  1 140 ? -5.268  26.479  215.806 1.00 35.57  ? 140 GLU B C     1 
ATOM   4848  O O     . GLU B  1 140 ? -5.726  25.497  215.225 1.00 31.50  ? 140 GLU B O     1 
ATOM   4849  C CB    . GLU B  1 140 ? -4.672  28.328  214.200 1.00 39.68  ? 140 GLU B CB    1 
ATOM   4850  C CG    . GLU B  1 140 ? -3.620  29.345  213.766 1.00 38.06  ? 140 GLU B CG    1 
ATOM   4851  C CD    . GLU B  1 140 ? -4.196  30.488  212.952 1.00 41.63  ? 140 GLU B CD    1 
ATOM   4852  O OE1   . GLU B  1 140 ? -5.238  30.290  212.294 1.00 45.50  ? 140 GLU B OE1   1 
ATOM   4853  O OE2   . GLU B  1 140 ? -3.605  31.585  212.979 1.00 49.30  ? 140 GLU B OE2   1 
ATOM   4854  N N     . SER B  1 141 ? -5.709  26.889  216.990 1.00 35.27  ? 141 SER B N     1 
ATOM   4855  C CA    . SER B  1 141 ? -6.539  26.038  217.840 1.00 35.55  ? 141 SER B CA    1 
ATOM   4856  C C     . SER B  1 141 ? -7.970  25.836  217.350 1.00 39.19  ? 141 SER B C     1 
ATOM   4857  O O     . SER B  1 141 ? -8.717  25.051  217.934 1.00 38.62  ? 141 SER B O     1 
ATOM   4858  C CB    . SER B  1 141 ? -6.576  26.601  219.258 1.00 32.18  ? 141 SER B CB    1 
ATOM   4859  O OG    . SER B  1 141 ? -7.151  27.895  219.285 1.00 34.52  ? 141 SER B OG    1 
ATOM   4860  N N     . GLY B  1 142 ? -8.354  26.542  216.293 1.00 37.32  ? 142 GLY B N     1 
ATOM   4861  C CA    . GLY B  1 142 ? -9.674  26.366  215.712 1.00 40.14  ? 142 GLY B CA    1 
ATOM   4862  C C     . GLY B  1 142 ? -9.655  25.289  214.647 1.00 39.53  ? 142 GLY B C     1 
ATOM   4863  O O     . GLY B  1 142 ? -10.699 24.904  214.118 1.00 35.51  ? 142 GLY B O     1 
ATOM   4864  N N     . SER B  1 143 ? -8.457  24.805  214.330 1.00 38.99  ? 143 SER B N     1 
ATOM   4865  C CA    . SER B  1 143 ? -8.298  23.730  213.359 1.00 36.79  ? 143 SER B CA    1 
ATOM   4866  C C     . SER B  1 143 ? -8.902  22.441  213.890 1.00 38.88  ? 143 SER B C     1 
ATOM   4867  O O     . SER B  1 143 ? -8.765  22.121  215.070 1.00 38.06  ? 143 SER B O     1 
ATOM   4868  C CB    . SER B  1 143 ? -6.824  23.505  213.027 1.00 40.42  ? 143 SER B CB    1 
ATOM   4869  O OG    . SER B  1 143 ? -6.197  24.701  212.595 1.00 40.22  ? 143 SER B OG    1 
ATOM   4870  N N     . THR B  1 144 ? -9.581  21.708  213.017 1.00 40.55  ? 144 THR B N     1 
ATOM   4871  C CA    . THR B  1 144 ? -10.091 20.393  213.372 1.00 41.83  ? 144 THR B CA    1 
ATOM   4872  C C     . THR B  1 144 ? -9.009  19.350  213.121 1.00 41.26  ? 144 THR B C     1 
ATOM   4873  O O     . THR B  1 144 ? -8.003  19.635  212.471 1.00 41.64  ? 144 THR B O     1 
ATOM   4874  C CB    . THR B  1 144 ? -11.358 20.033  212.578 1.00 42.71  ? 144 THR B CB    1 
ATOM   4875  O OG1   . THR B  1 144 ? -11.073 20.080  211.176 1.00 47.08  ? 144 THR B OG1   1 
ATOM   4876  C CG2   . THR B  1 144 ? -12.490 21.007  212.901 1.00 41.97  ? 144 THR B CG2   1 
ATOM   4877  N N     . LEU B  1 145 ? -9.217  18.146  213.647 1.00 41.57  ? 145 LEU B N     1 
ATOM   4878  C CA    . LEU B  1 145 ? -8.277  17.049  213.448 1.00 43.28  ? 145 LEU B CA    1 
ATOM   4879  C C     . LEU B  1 145 ? -8.188  16.699  211.972 1.00 44.24  ? 145 LEU B C     1 
ATOM   4880  O O     . LEU B  1 145 ? -7.106  16.444  211.447 1.00 44.10  ? 145 LEU B O     1 
ATOM   4881  C CB    . LEU B  1 145 ? -8.695  15.823  214.259 1.00 42.22  ? 145 LEU B CB    1 
ATOM   4882  C CG    . LEU B  1 145 ? -8.647  15.995  215.775 1.00 40.84  ? 145 LEU B CG    1 
ATOM   4883  C CD1   . LEU B  1 145 ? -9.137  14.740  216.453 1.00 38.69  ? 145 LEU B CD1   1 
ATOM   4884  C CD2   . LEU B  1 145 ? -7.234  16.325  216.229 1.00 38.77  ? 145 LEU B CD2   1 
ATOM   4885  N N     . GLY B  1 146 ? -9.341  16.707  211.311 1.00 42.39  ? 146 GLY B N     1 
ATOM   4886  C CA    . GLY B  1 146 ? -9.417  16.429  209.890 1.00 47.14  ? 146 GLY B CA    1 
ATOM   4887  C C     . GLY B  1 146 ? -8.627  17.428  209.067 1.00 49.68  ? 146 GLY B C     1 
ATOM   4888  O O     . GLY B  1 146 ? -7.878  17.048  208.167 1.00 56.30  ? 146 GLY B O     1 
ATOM   4889  N N     . GLU B  1 147 ? -8.796  18.710  209.378 1.00 48.04  ? 147 GLU B N     1 
ATOM   4890  C CA    . GLU B  1 147 ? -8.039  19.769  208.723 1.00 52.78  ? 147 GLU B CA    1 
ATOM   4891  C C     . GLU B  1 147 ? -6.539  19.605  208.966 1.00 49.94  ? 147 GLU B C     1 
ATOM   4892  O O     . GLU B  1 147 ? -5.722  19.906  208.095 1.00 52.91  ? 147 GLU B O     1 
ATOM   4893  C CB    . GLU B  1 147 ? -8.507  21.143  209.212 1.00 49.78  ? 147 GLU B CB    1 
ATOM   4894  C CG    . GLU B  1 147 ? -9.845  21.591  208.636 1.00 49.64  ? 147 GLU B CG    1 
ATOM   4895  C CD    . GLU B  1 147 ? -10.366 22.860  209.285 1.00 50.90  ? 147 GLU B CD    1 
ATOM   4896  O OE1   . GLU B  1 147 ? -10.033 23.108  210.464 1.00 48.05  ? 147 GLU B OE1   1 
ATOM   4897  O OE2   . GLU B  1 147 ? -11.106 23.613  208.618 1.00 58.33  ? 147 GLU B OE2   1 
ATOM   4898  N N     . LEU B  1 148 ? -6.188  19.129  210.156 1.00 45.67  ? 148 LEU B N     1 
ATOM   4899  C CA    . LEU B  1 148 ? -4.796  18.876  210.502 1.00 48.53  ? 148 LEU B CA    1 
ATOM   4900  C C     . LEU B  1 148 ? -4.248  17.677  209.733 1.00 53.29  ? 148 LEU B C     1 
ATOM   4901  O O     . LEU B  1 148 ? -3.182  17.763  209.122 1.00 52.53  ? 148 LEU B O     1 
ATOM   4902  C CB    . LEU B  1 148 ? -4.644  18.649  212.008 1.00 40.12  ? 148 LEU B CB    1 
ATOM   4903  C CG    . LEU B  1 148 ? -3.248  18.213  212.464 1.00 44.58  ? 148 LEU B CG    1 
ATOM   4904  C CD1   . LEU B  1 148 ? -2.189  19.202  211.996 1.00 42.79  ? 148 LEU B CD1   1 
ATOM   4905  C CD2   . LEU B  1 148 ? -3.195  18.042  213.973 1.00 39.83  ? 148 LEU B CD2   1 
ATOM   4906  N N     . TYR B  1 149 ? -4.979  16.565  209.775 1.00 51.38  ? 149 TYR B N     1 
ATOM   4907  C CA    . TYR B  1 149 ? -4.599  15.354  209.050 1.00 53.30  ? 149 TYR B CA    1 
ATOM   4908  C C     . TYR B  1 149 ? -4.419  15.641  207.569 1.00 57.37  ? 149 TYR B C     1 
ATOM   4909  O O     . TYR B  1 149 ? -3.423  15.241  206.963 1.00 62.56  ? 149 TYR B O     1 
ATOM   4910  C CB    . TYR B  1 149 ? -5.649  14.255  209.226 1.00 52.00  ? 149 TYR B CB    1 
ATOM   4911  C CG    . TYR B  1 149 ? -5.837  13.774  210.644 1.00 51.54  ? 149 TYR B CG    1 
ATOM   4912  C CD1   . TYR B  1 149 ? -4.805  13.850  211.568 1.00 51.17  ? 149 TYR B CD1   1 
ATOM   4913  C CD2   . TYR B  1 149 ? -7.052  13.241  211.056 1.00 50.24  ? 149 TYR B CD2   1 
ATOM   4914  C CE1   . TYR B  1 149 ? -4.978  13.407  212.865 1.00 50.81  ? 149 TYR B CE1   1 
ATOM   4915  C CE2   . TYR B  1 149 ? -7.234  12.799  212.346 1.00 52.50  ? 149 TYR B CE2   1 
ATOM   4916  C CZ    . TYR B  1 149 ? -6.197  12.883  213.246 1.00 50.27  ? 149 TYR B CZ    1 
ATOM   4917  O OH    . TYR B  1 149 ? -6.386  12.438  214.530 1.00 54.06  ? 149 TYR B OH    1 
ATOM   4918  N N     . TYR B  1 150 ? -5.397  16.336  206.994 1.00 57.24  ? 150 TYR B N     1 
ATOM   4919  C CA    . TYR B  1 150 ? -5.385  16.668  205.576 1.00 62.47  ? 150 TYR B CA    1 
ATOM   4920  C C     . TYR B  1 150 ? -4.151  17.472  205.203 1.00 62.07  ? 150 TYR B C     1 
ATOM   4921  O O     . TYR B  1 150 ? -3.481  17.175  204.214 1.00 65.60  ? 150 TYR B O     1 
ATOM   4922  C CB    . TYR B  1 150 ? -6.646  17.448  205.192 1.00 61.66  ? 150 TYR B CB    1 
ATOM   4923  C CG    . TYR B  1 150 ? -6.629  17.960  203.768 1.00 65.27  ? 150 TYR B CG    1 
ATOM   4924  C CD1   . TYR B  1 150 ? -7.110  17.181  202.725 1.00 68.83  ? 150 TYR B CD1   1 
ATOM   4925  C CD2   . TYR B  1 150 ? -6.126  19.222  203.465 1.00 64.62  ? 150 TYR B CD2   1 
ATOM   4926  C CE1   . TYR B  1 150 ? -7.092  17.642  201.422 1.00 71.26  ? 150 TYR B CE1   1 
ATOM   4927  C CE2   . TYR B  1 150 ? -6.101  19.689  202.166 1.00 69.90  ? 150 TYR B CE2   1 
ATOM   4928  C CZ    . TYR B  1 150 ? -6.586  18.896  201.149 1.00 71.59  ? 150 TYR B CZ    1 
ATOM   4929  O OH    . TYR B  1 150 ? -6.565  19.362  199.854 1.00 76.52  ? 150 TYR B OH    1 
ATOM   4930  N N     . ALA B  1 151 ? -3.862  18.497  205.997 1.00 61.27  ? 151 ALA B N     1 
ATOM   4931  C CA    . ALA B  1 151 ? -2.742  19.386  205.725 1.00 59.41  ? 151 ALA B CA    1 
ATOM   4932  C C     . ALA B  1 151 ? -1.417  18.640  205.762 1.00 63.23  ? 151 ALA B C     1 
ATOM   4933  O O     . ALA B  1 151 ? -0.476  19.004  205.061 1.00 66.00  ? 151 ALA B O     1 
ATOM   4934  C CB    . ALA B  1 151 ? -2.726  20.532  206.720 1.00 49.62  ? 151 ALA B CB    1 
ATOM   4935  N N     . ILE B  1 152 ? -1.355  17.590  206.576 1.00 61.51  ? 152 ILE B N     1 
ATOM   4936  C CA    . ILE B  1 152 ? -0.143  16.788  206.713 1.00 65.86  ? 152 ILE B CA    1 
ATOM   4937  C C     . ILE B  1 152 ? 0.099   15.925  205.478 1.00 66.47  ? 152 ILE B C     1 
ATOM   4938  O O     . ILE B  1 152 ? 1.227   15.829  204.992 1.00 68.55  ? 152 ILE B O     1 
ATOM   4939  C CB    . ILE B  1 152 ? -0.202  15.891  207.965 1.00 62.14  ? 152 ILE B CB    1 
ATOM   4940  C CG1   . ILE B  1 152 ? -0.196  16.754  209.228 1.00 53.97  ? 152 ILE B CG1   1 
ATOM   4941  C CG2   . ILE B  1 152 ? 0.970   14.921  207.992 1.00 61.56  ? 152 ILE B CG2   1 
ATOM   4942  C CD1   . ILE B  1 152 ? -0.382  15.968  210.503 1.00 48.63  ? 152 ILE B CD1   1 
ATOM   4943  N N     . THR B  1 153 ? -0.966  15.306  204.974 1.00 65.87  ? 153 THR B N     1 
ATOM   4944  C CA    . THR B  1 153 ? -0.894  14.480  203.770 1.00 70.56  ? 153 THR B CA    1 
ATOM   4945  C C     . THR B  1 153 ? -0.369  15.282  202.582 1.00 73.72  ? 153 THR B C     1 
ATOM   4946  O O     . THR B  1 153 ? 0.512   14.829  201.849 1.00 73.04  ? 153 THR B O     1 
ATOM   4947  C CB    . THR B  1 153 ? -2.271  13.893  203.398 1.00 68.69  ? 153 THR B CB    1 
ATOM   4948  O OG1   . THR B  1 153 ? -3.170  14.957  203.062 1.00 68.92  ? 153 THR B OG1   1 
ATOM   4949  C CG2   . THR B  1 153 ? -2.851  13.090  204.554 1.00 63.59  ? 153 THR B CG2   1 
ATOM   4950  N N     . GLU B  1 154 ? -0.911  16.485  202.416 1.00 70.58  ? 154 GLU B N     1 
ATOM   4951  C CA    . GLU B  1 154 ? -0.573  17.361  201.295 1.00 72.97  ? 154 GLU B CA    1 
ATOM   4952  C C     . GLU B  1 154 ? 0.850   17.924  201.363 1.00 72.57  ? 154 GLU B C     1 
ATOM   4953  O O     . GLU B  1 154 ? 1.256   18.703  200.499 1.00 79.38  ? 154 GLU B O     1 
ATOM   4954  C CB    . GLU B  1 154 ? -1.581  18.514  201.217 1.00 72.21  ? 154 GLU B CB    1 
ATOM   4955  C CG    . GLU B  1 154 ? -2.992  18.099  200.802 1.00 76.48  ? 154 GLU B CG    1 
ATOM   4956  C CD    . GLU B  1 154 ? -3.129  17.909  199.302 1.00 82.72  ? 154 GLU B CD    1 
ATOM   4957  O OE1   . GLU B  1 154 ? -3.607  16.835  198.878 1.00 87.06  ? 154 GLU B OE1   1 
ATOM   4958  O OE2   . GLU B  1 154 ? -2.777  18.842  198.547 1.00 88.86  ? 154 GLU B OE2   1 
ATOM   4959  N N     . SER B  1 155 ? 1.599   17.537  202.393 1.00 67.51  ? 155 SER B N     1 
ATOM   4960  C CA    . SER B  1 155 ? 2.985   17.974  202.554 1.00 68.46  ? 155 SER B CA    1 
ATOM   4961  C C     . SER B  1 155 ? 3.942   16.780  202.619 1.00 68.24  ? 155 SER B C     1 
ATOM   4962  O O     . SER B  1 155 ? 5.138   16.912  202.334 1.00 66.63  ? 155 SER B O     1 
ATOM   4963  C CB    . SER B  1 155 ? 3.139   18.833  203.813 1.00 67.67  ? 155 SER B CB    1 
ATOM   4964  O OG    . SER B  1 155 ? 3.055   18.043  204.989 1.00 70.62  ? 155 SER B OG    1 
ATOM   4965  N N     . SER B  1 156 ? 3.408   15.618  202.993 1.00 70.09  ? 156 SER B N     1 
ATOM   4966  C CA    . SER B  1 156 ? 4.215   14.411  203.160 1.00 63.54  ? 156 SER B CA    1 
ATOM   4967  C C     . SER B  1 156 ? 3.384   13.126  203.162 1.00 71.34  ? 156 SER B C     1 
ATOM   4968  O O     . SER B  1 156 ? 2.221   13.123  203.563 1.00 72.97  ? 156 SER B O     1 
ATOM   4969  C CB    . SER B  1 156 ? 5.021   14.485  204.459 1.00 64.80  ? 156 SER B CB    1 
ATOM   4970  O OG    . SER B  1 156 ? 5.758   13.291  204.659 1.00 68.96  ? 156 SER B OG    1 
ATOM   4971  N N     . SER B  1 157 ? 4.007   12.037  202.720 1.00 71.92  ? 157 SER B N     1 
ATOM   4972  C CA    . SER B  1 157 ? 3.400   10.710  202.764 1.00 71.09  ? 157 SER B CA    1 
ATOM   4973  C C     . SER B  1 157 ? 4.056   9.876   203.856 1.00 71.45  ? 157 SER B C     1 
ATOM   4974  O O     . SER B  1 157 ? 3.632   8.755   204.142 1.00 73.87  ? 157 SER B O     1 
ATOM   4975  C CB    . SER B  1 157 ? 3.530   10.008  201.412 1.00 78.06  ? 157 SER B CB    1 
ATOM   4976  O OG    . SER B  1 157 ? 3.197   8.632   201.512 1.00 88.28  ? 157 SER B OG    1 
ATOM   4977  N N     . LYS B  1 158 ? 5.097   10.436  204.462 1.00 67.38  ? 158 LYS B N     1 
ATOM   4978  C CA    . LYS B  1 158 ? 5.876   9.726   205.468 1.00 69.29  ? 158 LYS B CA    1 
ATOM   4979  C C     . LYS B  1 158 ? 5.662   10.295  206.862 1.00 66.16  ? 158 LYS B C     1 
ATOM   4980  O O     . LYS B  1 158 ? 6.409   9.984   207.791 1.00 65.00  ? 158 LYS B O     1 
ATOM   4981  C CB    . LYS B  1 158 ? 7.362   9.777   205.112 1.00 71.64  ? 158 LYS B CB    1 
ATOM   4982  C CG    . LYS B  1 158 ? 7.683   9.143   203.775 1.00 75.94  ? 158 LYS B CG    1 
ATOM   4983  C CD    . LYS B  1 158 ? 9.174   9.130   203.503 1.00 86.16  ? 158 LYS B CD    1 
ATOM   4984  C CE    . LYS B  1 158 ? 9.500   8.194   202.353 1.00 87.70  ? 158 LYS B CE    1 
ATOM   4985  N NZ    . LYS B  1 158 ? 10.714  8.627   201.614 1.00 89.11  ? 158 LYS B NZ    1 
ATOM   4986  N N     . LEU B  1 159 ? 4.642   11.132  207.007 1.00 66.45  ? 159 LEU B N     1 
ATOM   4987  C CA    . LEU B  1 159 ? 4.380   11.779  208.283 1.00 61.76  ? 159 LEU B CA    1 
ATOM   4988  C C     . LEU B  1 159 ? 2.899   11.773  208.636 1.00 61.20  ? 159 LEU B C     1 
ATOM   4989  O O     . LEU B  1 159 ? 2.035   11.822  207.760 1.00 63.76  ? 159 LEU B O     1 
ATOM   4990  C CB    . LEU B  1 159 ? 4.911   13.214  208.268 1.00 59.71  ? 159 LEU B CB    1 
ATOM   4991  C CG    . LEU B  1 159 ? 6.436   13.344  208.292 1.00 57.13  ? 159 LEU B CG    1 
ATOM   4992  C CD1   . LEU B  1 159 ? 6.856   14.792  208.119 1.00 59.07  ? 159 LEU B CD1   1 
ATOM   4993  C CD2   . LEU B  1 159 ? 6.999   12.772  209.584 1.00 53.21  ? 159 LEU B CD2   1 
ATOM   4994  N N     . GLY B  1 160 ? 2.618   11.702  209.932 1.00 60.53  ? 160 GLY B N     1 
ATOM   4995  C CA    . GLY B  1 160 ? 1.259   11.729  210.431 1.00 55.49  ? 160 GLY B CA    1 
ATOM   4996  C C     . GLY B  1 160 ? 1.231   12.302  211.832 1.00 52.70  ? 160 GLY B C     1 
ATOM   4997  O O     . GLY B  1 160 ? 2.222   12.863  212.298 1.00 50.35  ? 160 GLY B O     1 
ATOM   4998  N N     . PHE B  1 161 ? 0.097   12.162  212.507 1.00 54.50  ? 161 PHE B N     1 
ATOM   4999  C CA    . PHE B  1 161 ? -0.026  12.639  213.878 1.00 51.49  ? 161 PHE B CA    1 
ATOM   5000  C C     . PHE B  1 161 ? -1.039  11.796  214.642 1.00 49.54  ? 161 PHE B C     1 
ATOM   5001  O O     . PHE B  1 161 ? -1.993  11.282  214.057 1.00 54.53  ? 161 PHE B O     1 
ATOM   5002  C CB    . PHE B  1 161 ? -0.426  14.114  213.899 1.00 47.97  ? 161 PHE B CB    1 
ATOM   5003  C CG    . PHE B  1 161 ? -0.352  14.739  215.261 1.00 46.12  ? 161 PHE B CG    1 
ATOM   5004  C CD1   . PHE B  1 161 ? 0.874   15.012  215.844 1.00 45.22  ? 161 PHE B CD1   1 
ATOM   5005  C CD2   . PHE B  1 161 ? -1.506  15.060  215.954 1.00 45.95  ? 161 PHE B CD2   1 
ATOM   5006  C CE1   . PHE B  1 161 ? 0.948   15.588  217.098 1.00 43.69  ? 161 PHE B CE1   1 
ATOM   5007  C CE2   . PHE B  1 161 ? -1.440  15.639  217.208 1.00 43.43  ? 161 PHE B CE2   1 
ATOM   5008  C CZ    . PHE B  1 161 ? -0.211  15.902  217.780 1.00 40.72  ? 161 PHE B CZ    1 
ATOM   5009  N N     . THR B  1 162 ? -0.827  11.646  215.946 1.00 48.22  ? 162 THR B N     1 
ATOM   5010  C CA    . THR B  1 162 ? -1.699  10.795  216.748 1.00 51.07  ? 162 THR B CA    1 
ATOM   5011  C C     . THR B  1 162 ? -2.804  11.597  217.427 1.00 53.36  ? 162 THR B C     1 
ATOM   5012  O O     . THR B  1 162 ? -2.542  12.503  218.218 1.00 51.08  ? 162 THR B O     1 
ATOM   5013  C CB    . THR B  1 162 ? -0.900  9.999   217.813 1.00 51.58  ? 162 THR B CB    1 
ATOM   5014  O OG1   . THR B  1 162 ? -1.807  9.333   218.701 1.00 50.14  ? 162 THR B OG1   1 
ATOM   5015  C CG2   . THR B  1 162 ? 0.012   10.912  218.618 1.00 44.64  ? 162 THR B CG2   1 
ATOM   5016  N N     . ALA B  1 163 ? -4.045  11.257  217.086 1.00 50.70  ? 163 ALA B N     1 
ATOM   5017  C CA    . ALA B  1 163 ? -5.227  11.837  217.714 1.00 49.08  ? 163 ALA B CA    1 
ATOM   5018  C C     . ALA B  1 163 ? -6.474  11.045  217.329 1.00 52.31  ? 163 ALA B C     1 
ATOM   5019  O O     . ALA B  1 163 ? -6.385  10.018  216.653 1.00 52.63  ? 163 ALA B O     1 
ATOM   5020  C CB    . ALA B  1 163 ? -5.385  13.302  217.328 1.00 47.59  ? 163 ALA B CB    1 
ATOM   5021  N N     . ALA B  1 164 ? -7.628  11.543  217.764 1.00 53.00  ? 164 ALA B N     1 
ATOM   5022  C CA    . ALA B  1 164 ? -8.925  10.898  217.556 1.00 47.10  ? 164 ALA B CA    1 
ATOM   5023  C C     . ALA B  1 164 ? -9.212  10.549  216.101 1.00 49.37  ? 164 ALA B C     1 
ATOM   5024  O O     . ALA B  1 164 ? -8.593  11.087  215.183 1.00 55.27  ? 164 ALA B O     1 
ATOM   5025  C CB    . ALA B  1 164 ? -10.032 11.789  218.091 1.00 46.65  ? 164 ALA B CB    1 
ATOM   5026  N N     . TRP B  1 165 ? -10.167 9.647   215.902 1.00 50.29  ? 165 TRP B N     1 
ATOM   5027  C CA    . TRP B  1 165 ? -10.614 9.293   214.563 1.00 54.77  ? 165 TRP B CA    1 
ATOM   5028  C C     . TRP B  1 165 ? -11.653 10.295  214.068 1.00 57.15  ? 165 TRP B C     1 
ATOM   5029  O O     . TRP B  1 165 ? -11.802 10.494  212.865 1.00 57.10  ? 165 TRP B O     1 
ATOM   5030  C CB    . TRP B  1 165 ? -11.189 7.871   214.537 1.00 58.32  ? 165 TRP B CB    1 
ATOM   5031  C CG    . TRP B  1 165 ? -12.415 7.672   215.391 1.00 60.64  ? 165 TRP B CG    1 
ATOM   5032  C CD1   . TRP B  1 165 ? -12.454 7.188   216.668 1.00 58.61  ? 165 TRP B CD1   1 
ATOM   5033  C CD2   . TRP B  1 165 ? -13.776 7.942   215.025 1.00 64.47  ? 165 TRP B CD2   1 
ATOM   5034  N NE1   . TRP B  1 165 ? -13.751 7.144   217.120 1.00 65.87  ? 165 TRP B NE1   1 
ATOM   5035  C CE2   . TRP B  1 165 ? -14.582 7.601   216.131 1.00 67.91  ? 165 TRP B CE2   1 
ATOM   5036  C CE3   . TRP B  1 165 ? -14.392 8.439   213.870 1.00 62.18  ? 165 TRP B CE3   1 
ATOM   5037  C CZ2   . TRP B  1 165 ? -15.971 7.741   216.116 1.00 65.95  ? 165 TRP B CZ2   1 
ATOM   5038  C CZ3   . TRP B  1 165 ? -15.770 8.579   213.859 1.00 61.22  ? 165 TRP B CZ3   1 
ATOM   5039  C CH2   . TRP B  1 165 ? -16.544 8.231   214.974 1.00 63.42  ? 165 TRP B CH2   1 
ATOM   5040  N N     . CYS B  1 166 ? -12.365 10.918  215.004 1.00 57.76  ? 166 CYS B N     1 
ATOM   5041  C CA    . CYS B  1 166 ? -13.386 11.915  214.681 1.00 47.14  ? 166 CYS B CA    1 
ATOM   5042  C C     . CYS B  1 166 ? -12.760 13.163  214.064 1.00 46.28  ? 166 CYS B C     1 
ATOM   5043  O O     . CYS B  1 166 ? -12.086 13.924  214.754 1.00 44.32  ? 166 CYS B O     1 
ATOM   5044  C CB    . CYS B  1 166 ? -14.175 12.304  215.933 1.00 48.09  ? 166 CYS B CB    1 
ATOM   5045  S SG    . CYS B  1 166 ? -14.842 10.936  216.907 1.00 53.54  ? 166 CYS B SG    1 
ATOM   5046  N N     . PRO B  1 167 ? -12.992 13.385  212.761 1.00 48.65  ? 167 PRO B N     1 
ATOM   5047  C CA    . PRO B  1 167 ? -12.295 14.483  212.078 1.00 45.08  ? 167 PRO B CA    1 
ATOM   5048  C C     . PRO B  1 167 ? -12.869 15.885  212.324 1.00 42.96  ? 167 PRO B C     1 
ATOM   5049  O O     . PRO B  1 167 ? -12.206 16.858  211.964 1.00 44.95  ? 167 PRO B O     1 
ATOM   5050  C CB    . PRO B  1 167 ? -12.431 14.105  210.602 1.00 45.74  ? 167 PRO B CB    1 
ATOM   5051  C CG    . PRO B  1 167 ? -13.705 13.341  210.534 1.00 49.16  ? 167 PRO B CG    1 
ATOM   5052  C CD    . PRO B  1 167 ? -13.812 12.585  211.831 1.00 46.19  ? 167 PRO B CD    1 
ATOM   5053  N N     . THR B  1 168 ? -14.058 15.999  212.910 1.00 43.91  ? 168 THR B N     1 
ATOM   5054  C CA    . THR B  1 168 ? -14.613 17.324  213.195 1.00 42.88  ? 168 THR B CA    1 
ATOM   5055  C C     . THR B  1 168 ? -14.304 17.774  214.621 1.00 37.23  ? 168 THR B C     1 
ATOM   5056  O O     . THR B  1 168 ? -14.743 18.838  215.050 1.00 40.86  ? 168 THR B O     1 
ATOM   5057  C CB    . THR B  1 168 ? -16.138 17.378  212.978 1.00 42.88  ? 168 THR B CB    1 
ATOM   5058  O OG1   . THR B  1 168 ? -16.792 16.506  213.906 1.00 44.03  ? 168 THR B OG1   1 
ATOM   5059  C CG2   . THR B  1 168 ? -16.496 16.981  211.556 1.00 48.11  ? 168 THR B CG2   1 
ATOM   5060  N N     . VAL B  1 169 ? -13.555 16.959  215.356 1.00 37.52  ? 169 VAL B N     1 
ATOM   5061  C CA    . VAL B  1 169 ? -13.078 17.359  216.676 1.00 37.25  ? 169 VAL B CA    1 
ATOM   5062  C C     . VAL B  1 169 ? -12.021 18.449  216.514 1.00 34.25  ? 169 VAL B C     1 
ATOM   5063  O O     . VAL B  1 169 ? -11.146 18.345  215.657 1.00 39.73  ? 169 VAL B O     1 
ATOM   5064  C CB    . VAL B  1 169 ? -12.498 16.159  217.463 1.00 40.70  ? 169 VAL B CB    1 
ATOM   5065  C CG1   . VAL B  1 169 ? -11.699 16.629  218.662 1.00 34.10  ? 169 VAL B CG1   1 
ATOM   5066  C CG2   . VAL B  1 169 ? -13.614 15.220  217.899 1.00 35.52  ? 169 VAL B CG2   1 
ATOM   5067  N N     . GLY B  1 170 ? -12.117 19.504  217.319 1.00 37.41  ? 170 GLY B N     1 
ATOM   5068  C CA    . GLY B  1 170 ? -11.175 20.605  217.232 1.00 36.46  ? 170 GLY B CA    1 
ATOM   5069  C C     . GLY B  1 170 ? -9.917  20.352  218.042 1.00 35.51  ? 170 GLY B C     1 
ATOM   5070  O O     . GLY B  1 170 ? -9.965  19.680  219.068 1.00 36.42  ? 170 GLY B O     1 
ATOM   5071  N N     . THR B  1 171 ? -8.790  20.887  217.580 1.00 33.51  ? 171 THR B N     1 
ATOM   5072  C CA    . THR B  1 171 ? -7.525  20.751  218.297 1.00 33.47  ? 171 THR B CA    1 
ATOM   5073  C C     . THR B  1 171 ? -7.571  21.475  219.637 1.00 34.25  ? 171 THR B C     1 
ATOM   5074  O O     . THR B  1 171 ? -6.917  21.069  220.598 1.00 35.24  ? 171 THR B O     1 
ATOM   5075  C CB    . THR B  1 171 ? -6.344  21.306  217.473 1.00 34.55  ? 171 THR B CB    1 
ATOM   5076  O OG1   . THR B  1 171 ? -6.659  22.629  217.018 1.00 35.54  ? 171 THR B OG1   1 
ATOM   5077  C CG2   . THR B  1 171 ? -6.070  20.421  216.271 1.00 39.32  ? 171 THR B CG2   1 
ATOM   5078  N N     . GLY B  1 172 ? -8.358  22.547  219.685 1.00 35.77  ? 172 GLY B N     1 
ATOM   5079  C CA    . GLY B  1 172 ? -8.490  23.371  220.873 1.00 31.49  ? 172 GLY B CA    1 
ATOM   5080  C C     . GLY B  1 172 ? -8.825  22.590  222.127 1.00 37.67  ? 172 GLY B C     1 
ATOM   5081  O O     . GLY B  1 172 ? -8.053  22.585  223.082 1.00 36.50  ? 172 GLY B O     1 
ATOM   5082  N N     . GLY B  1 173 ? -9.972  21.921  222.126 1.00 34.13  ? 173 GLY B N     1 
ATOM   5083  C CA    . GLY B  1 173 ? -10.381 21.135  223.274 1.00 32.85  ? 173 GLY B CA    1 
ATOM   5084  C C     . GLY B  1 173 ? -9.716  19.772  223.345 1.00 33.14  ? 173 GLY B C     1 
ATOM   5085  O O     . GLY B  1 173 ? -9.402  19.286  224.431 1.00 35.88  ? 173 GLY B O     1 
ATOM   5086  N N     . HIS B  1 174 ? -9.499  19.156  222.186 1.00 29.85  ? 174 HIS B N     1 
ATOM   5087  C CA    . HIS B  1 174 ? -8.962  17.796  222.110 1.00 34.48  ? 174 HIS B CA    1 
ATOM   5088  C C     . HIS B  1 174 ? -7.568  17.663  222.711 1.00 37.84  ? 174 HIS B C     1 
ATOM   5089  O O     . HIS B  1 174 ? -7.334  16.834  223.592 1.00 34.31  ? 174 HIS B O     1 
ATOM   5090  C CB    . HIS B  1 174 ? -8.925  17.332  220.655 1.00 33.94  ? 174 HIS B CB    1 
ATOM   5091  C CG    . HIS B  1 174 ? -8.556  15.893  220.482 1.00 35.61  ? 174 HIS B CG    1 
ATOM   5092  N ND1   . HIS B  1 174 ? -9.334  14.863  220.965 1.00 35.24  ? 174 HIS B ND1   1 
ATOM   5093  C CD2   . HIS B  1 174 ? -7.496  15.311  219.872 1.00 38.82  ? 174 HIS B CD2   1 
ATOM   5094  C CE1   . HIS B  1 174 ? -8.768  13.708  220.662 1.00 40.56  ? 174 HIS B CE1   1 
ATOM   5095  N NE2   . HIS B  1 174 ? -7.653  13.952  219.998 1.00 39.46  ? 174 HIS B NE2   1 
ATOM   5096  N N     . ILE B  1 175 ? -6.641  18.474  222.216 1.00 36.58  ? 175 ILE B N     1 
ATOM   5097  C CA    . ILE B  1 175 ? -5.259  18.427  222.681 1.00 31.64  ? 175 ILE B CA    1 
ATOM   5098  C C     . ILE B  1 175 ? -5.177  18.928  224.124 1.00 31.86  ? 175 ILE B C     1 
ATOM   5099  O O     . ILE B  1 175 ? -4.357  18.456  224.910 1.00 32.94  ? 175 ILE B O     1 
ATOM   5100  C CB    . ILE B  1 175 ? -4.332  19.254  221.765 1.00 33.30  ? 175 ILE B CB    1 
ATOM   5101  C CG1   . ILE B  1 175 ? -4.357  18.699  220.335 1.00 31.83  ? 175 ILE B CG1   1 
ATOM   5102  C CG2   . ILE B  1 175 ? -2.906  19.256  222.289 1.00 33.52  ? 175 ILE B CG2   1 
ATOM   5103  C CD1   . ILE B  1 175 ? -3.303  19.304  219.427 1.00 38.57  ? 175 ILE B CD1   1 
ATOM   5104  N N     . SER B  1 176 ? -6.056  19.865  224.473 1.00 34.97  ? 176 SER B N     1 
ATOM   5105  C CA    . SER B  1 176 ? -6.125  20.402  225.832 1.00 33.26  ? 176 SER B CA    1 
ATOM   5106  C C     . SER B  1 176 ? -6.497  19.332  226.856 1.00 37.17  ? 176 SER B C     1 
ATOM   5107  O O     . SER B  1 176 ? -6.178  19.452  228.039 1.00 36.66  ? 176 SER B O     1 
ATOM   5108  C CB    . SER B  1 176 ? -7.134  21.549  225.902 1.00 36.54  ? 176 SER B CB    1 
ATOM   5109  O OG    . SER B  1 176 ? -6.681  22.676  225.168 1.00 33.11  ? 176 SER B OG    1 
ATOM   5110  N N     . GLY B  1 177 ? -7.177  18.288  226.399 1.00 34.97  ? 177 GLY B N     1 
ATOM   5111  C CA    . GLY B  1 177 ? -7.613  17.231  227.289 1.00 34.15  ? 177 GLY B CA    1 
ATOM   5112  C C     . GLY B  1 177 ? -6.792  15.966  227.158 1.00 34.78  ? 177 GLY B C     1 
ATOM   5113  O O     . GLY B  1 177 ? -7.043  14.983  227.852 1.00 41.79  ? 177 GLY B O     1 
ATOM   5114  N N     . GLY B  1 178 ? -5.813  15.985  226.260 1.00 35.67  ? 178 GLY B N     1 
ATOM   5115  C CA    . GLY B  1 178 ? -4.992  14.815  226.006 1.00 34.95  ? 178 GLY B CA    1 
ATOM   5116  C C     . GLY B  1 178 ? -5.083  14.373  224.559 1.00 36.96  ? 178 GLY B C     1 
ATOM   5117  O O     . GLY B  1 178 ? -4.256  14.753  223.732 1.00 35.17  ? 178 GLY B O     1 
ATOM   5118  N N     . GLY B  1 179 ? -6.093  13.565  224.252 1.00 36.56  ? 179 GLY B N     1 
ATOM   5119  C CA    . GLY B  1 179 ? -6.328  13.133  222.888 1.00 37.33  ? 179 GLY B CA    1 
ATOM   5120  C C     . GLY B  1 179 ? -5.843  11.729  222.595 1.00 38.94  ? 179 GLY B C     1 
ATOM   5121  O O     . GLY B  1 179 ? -4.671  11.522  222.284 1.00 41.19  ? 179 GLY B O     1 
ATOM   5122  N N     . PHE B  1 180 ? -6.751  10.764  222.682 1.00 41.37  ? 180 PHE B N     1 
ATOM   5123  C CA    . PHE B  1 180 ? -6.409  9.357   222.485 1.00 38.66  ? 180 PHE B CA    1 
ATOM   5124  C C     . PHE B  1 180 ? -6.917  8.844   221.136 1.00 47.70  ? 180 PHE B C     1 
ATOM   5125  O O     . PHE B  1 180 ? -8.046  9.137   220.732 1.00 47.40  ? 180 PHE B O     1 
ATOM   5126  C CB    . PHE B  1 180 ? -6.985  8.516   223.630 1.00 42.83  ? 180 PHE B CB    1 
ATOM   5127  C CG    . PHE B  1 180 ? -6.657  7.051   223.546 1.00 49.75  ? 180 PHE B CG    1 
ATOM   5128  C CD1   . PHE B  1 180 ? -5.482  6.557   224.091 1.00 44.54  ? 180 PHE B CD1   1 
ATOM   5129  C CD2   . PHE B  1 180 ? -7.534  6.166   222.941 1.00 48.64  ? 180 PHE B CD2   1 
ATOM   5130  C CE1   . PHE B  1 180 ? -5.183  5.208   224.020 1.00 50.20  ? 180 PHE B CE1   1 
ATOM   5131  C CE2   . PHE B  1 180 ? -7.240  4.817   222.866 1.00 52.50  ? 180 PHE B CE2   1 
ATOM   5132  C CZ    . PHE B  1 180 ? -6.063  4.337   223.406 1.00 53.58  ? 180 PHE B CZ    1 
ATOM   5133  N N     . GLY B  1 181 ? -6.080  8.079   220.441 1.00 47.69  ? 181 GLY B N     1 
ATOM   5134  C CA    . GLY B  1 181 ? -6.436  7.541   219.139 1.00 51.56  ? 181 GLY B CA    1 
ATOM   5135  C C     . GLY B  1 181 ? -5.811  6.190   218.832 1.00 53.25  ? 181 GLY B C     1 
ATOM   5136  O O     . GLY B  1 181 ? -5.160  5.586   219.684 1.00 52.39  ? 181 GLY B O     1 
ATOM   5137  N N     . MET B  1 182 ? -6.002  5.728   217.599 1.00 55.66  ? 182 MET B N     1 
ATOM   5138  C CA    . MET B  1 182 ? -5.516  4.422   217.159 1.00 57.35  ? 182 MET B CA    1 
ATOM   5139  C C     . MET B  1 182 ? -3.990  4.318   217.155 1.00 55.16  ? 182 MET B C     1 
ATOM   5140  O O     . MET B  1 182 ? -3.439  3.218   217.115 1.00 57.90  ? 182 MET B O     1 
ATOM   5141  C CB    . MET B  1 182 ? -6.050  4.107   215.759 1.00 59.59  ? 182 MET B CB    1 
ATOM   5142  C CG    . MET B  1 182 ? -7.570  4.046   215.660 1.00 64.69  ? 182 MET B CG    1 
ATOM   5143  S SD    . MET B  1 182 ? -8.277  2.585   216.441 1.00 68.24  ? 182 MET B SD    1 
ATOM   5144  C CE    . MET B  1 182 ? -7.680  1.292   215.352 1.00 60.96  ? 182 MET B CE    1 
ATOM   5145  N N     . MET B  1 183 ? -3.311  5.460   217.197 1.00 49.35  ? 183 MET B N     1 
ATOM   5146  C CA    . MET B  1 183 ? -1.851  5.480   217.157 1.00 46.02  ? 183 MET B CA    1 
ATOM   5147  C C     . MET B  1 183 ? -1.237  5.782   218.523 1.00 47.05  ? 183 MET B C     1 
ATOM   5148  O O     . MET B  1 183 ? -0.019  5.925   218.644 1.00 47.28  ? 183 MET B O     1 
ATOM   5149  C CB    . MET B  1 183 ? -1.355  6.508   216.139 1.00 47.90  ? 183 MET B CB    1 
ATOM   5150  C CG    . MET B  1 183 ? -1.969  6.369   214.758 1.00 53.74  ? 183 MET B CG    1 
ATOM   5151  S SD    . MET B  1 183 ? -0.880  6.955   213.442 1.00 60.42  ? 183 MET B SD    1 
ATOM   5152  C CE    . MET B  1 183 ? -0.253  8.469   214.159 1.00 63.81  ? 183 MET B CE    1 
ATOM   5153  N N     . SER B  1 184 ? -2.082  5.873   219.546 1.00 38.80  ? 184 SER B N     1 
ATOM   5154  C CA    . SER B  1 184 ? -1.626  6.209   220.893 1.00 41.44  ? 184 SER B CA    1 
ATOM   5155  C C     . SER B  1 184 ? -0.762  5.117   221.518 1.00 47.56  ? 184 SER B C     1 
ATOM   5156  O O     . SER B  1 184 ? 0.098   5.398   222.354 1.00 44.73  ? 184 SER B O     1 
ATOM   5157  C CB    . SER B  1 184 ? -2.819  6.501   221.800 1.00 42.80  ? 184 SER B CB    1 
ATOM   5158  O OG    . SER B  1 184 ? -3.423  7.740   221.468 1.00 45.31  ? 184 SER B OG    1 
ATOM   5159  N N     . ARG B  1 185 ? -1.000  3.871   221.122 1.00 45.27  ? 185 ARG B N     1 
ATOM   5160  C CA    . ARG B  1 185 ? -0.186  2.759   221.600 1.00 51.44  ? 185 ARG B CA    1 
ATOM   5161  C C     . ARG B  1 185 ? 1.232   2.874   221.049 1.00 46.63  ? 185 ARG B C     1 
ATOM   5162  O O     . ARG B  1 185 ? 2.176   2.321   221.612 1.00 49.77  ? 185 ARG B O     1 
ATOM   5163  C CB    . ARG B  1 185 ? -0.809  1.418   221.204 1.00 47.60  ? 185 ARG B CB    1 
ATOM   5164  C CG    . ARG B  1 185 ? -2.226  1.217   221.723 1.00 50.41  ? 185 ARG B CG    1 
ATOM   5165  C CD    . ARG B  1 185 ? -2.705  -0.222  221.559 1.00 51.29  ? 185 ARG B CD    1 
ATOM   5166  N NE    . ARG B  1 185 ? -1.980  -1.160  222.415 1.00 54.25  ? 185 ARG B NE    1 
ATOM   5167  C CZ    . ARG B  1 185 ? -1.016  -1.971  221.990 1.00 53.88  ? 185 ARG B CZ    1 
ATOM   5168  N NH1   . ARG B  1 185 ? -0.657  -1.969  220.714 1.00 47.76  ? 185 ARG B NH1   1 
ATOM   5169  N NH2   . ARG B  1 185 ? -0.414  -2.790  222.841 1.00 57.18  ? 185 ARG B NH2   1 
ATOM   5170  N N     . LYS B  1 186 ? 1.371   3.607   219.949 1.00 49.73  ? 186 LYS B N     1 
ATOM   5171  C CA    . LYS B  1 186 ? 2.664   3.795   219.302 1.00 48.29  ? 186 LYS B CA    1 
ATOM   5172  C C     . LYS B  1 186 ? 3.283   5.153   219.636 1.00 49.86  ? 186 LYS B C     1 
ATOM   5173  O O     . LYS B  1 186 ? 4.502   5.272   219.754 1.00 42.74  ? 186 LYS B O     1 
ATOM   5174  C CB    . LYS B  1 186 ? 2.515   3.647   217.783 1.00 49.21  ? 186 LYS B CB    1 
ATOM   5175  C CG    . LYS B  1 186 ? 3.738   4.055   216.967 1.00 51.53  ? 186 LYS B CG    1 
ATOM   5176  C CD    . LYS B  1 186 ? 4.815   2.984   216.956 1.00 53.60  ? 186 LYS B CD    1 
ATOM   5177  C CE    . LYS B  1 186 ? 5.882   3.299   215.911 1.00 57.56  ? 186 LYS B CE    1 
ATOM   5178  N NZ    . LYS B  1 186 ? 6.977   2.288   215.887 1.00 59.47  ? 186 LYS B NZ    1 
ATOM   5179  N N     . TYR B  1 187 ? 2.446   6.174   219.796 1.00 47.59  ? 187 TYR B N     1 
ATOM   5180  C CA    . TYR B  1 187 ? 2.950   7.537   219.955 1.00 43.53  ? 187 TYR B CA    1 
ATOM   5181  C C     . TYR B  1 187 ? 2.348   8.322   221.120 1.00 39.49  ? 187 TYR B C     1 
ATOM   5182  O O     . TYR B  1 187 ? 2.595   9.523   221.248 1.00 46.32  ? 187 TYR B O     1 
ATOM   5183  C CB    . TYR B  1 187 ? 2.722   8.326   218.664 1.00 44.98  ? 187 TYR B CB    1 
ATOM   5184  C CG    . TYR B  1 187 ? 3.616   7.916   217.517 1.00 46.88  ? 187 TYR B CG    1 
ATOM   5185  C CD1   . TYR B  1 187 ? 4.999   7.998   217.625 1.00 46.72  ? 187 TYR B CD1   1 
ATOM   5186  C CD2   . TYR B  1 187 ? 3.078   7.472   216.316 1.00 47.08  ? 187 TYR B CD2   1 
ATOM   5187  C CE1   . TYR B  1 187 ? 5.821   7.634   216.574 1.00 49.07  ? 187 TYR B CE1   1 
ATOM   5188  C CE2   . TYR B  1 187 ? 3.892   7.108   215.258 1.00 51.64  ? 187 TYR B CE2   1 
ATOM   5189  C CZ    . TYR B  1 187 ? 5.263   7.190   215.394 1.00 53.18  ? 187 TYR B CZ    1 
ATOM   5190  O OH    . TYR B  1 187 ? 6.075   6.828   214.344 1.00 54.28  ? 187 TYR B OH    1 
ATOM   5191  N N     . GLY B  1 188 ? 1.567   7.659   221.966 1.00 41.62  ? 188 GLY B N     1 
ATOM   5192  C CA    . GLY B  1 188 ? 0.936   8.334   223.086 1.00 37.70  ? 188 GLY B CA    1 
ATOM   5193  C C     . GLY B  1 188 ? -0.187  9.256   222.648 1.00 40.33  ? 188 GLY B C     1 
ATOM   5194  O O     . GLY B  1 188 ? -0.691  9.154   221.530 1.00 40.28  ? 188 GLY B O     1 
ATOM   5195  N N     . LEU B  1 189 ? -0.578  10.167  223.532 1.00 39.37  ? 189 LEU B N     1 
ATOM   5196  C CA    . LEU B  1 189 ? -1.651  11.105  223.226 1.00 40.11  ? 189 LEU B CA    1 
ATOM   5197  C C     . LEU B  1 189 ? -1.182  12.227  222.308 1.00 38.96  ? 189 LEU B C     1 
ATOM   5198  O O     . LEU B  1 189 ? 0.016   12.411  222.091 1.00 36.66  ? 189 LEU B O     1 
ATOM   5199  C CB    . LEU B  1 189 ? -2.221  11.701  224.514 1.00 39.92  ? 189 LEU B CB    1 
ATOM   5200  C CG    . LEU B  1 189 ? -2.629  10.716  225.615 1.00 42.96  ? 189 LEU B CG    1 
ATOM   5201  C CD1   . LEU B  1 189 ? -3.055  11.471  226.858 1.00 39.32  ? 189 LEU B CD1   1 
ATOM   5202  C CD2   . LEU B  1 189 ? -3.736  9.786   225.140 1.00 38.21  ? 189 LEU B CD2   1 
ATOM   5203  N N     . ALA B  1 190 ? -2.139  12.975  221.771 1.00 39.13  ? 190 ALA B N     1 
ATOM   5204  C CA    . ALA B  1 190 ? -1.831  14.159  220.982 1.00 37.46  ? 190 ALA B CA    1 
ATOM   5205  C C     . ALA B  1 190 ? -1.036  15.152  221.819 1.00 32.37  ? 190 ALA B C     1 
ATOM   5206  O O     . ALA B  1 190 ? -0.065  15.747  221.351 1.00 32.19  ? 190 ALA B O     1 
ATOM   5207  C CB    . ALA B  1 190 ? -3.106  14.796  220.469 1.00 38.93  ? 190 ALA B CB    1 
ATOM   5208  N N     . ALA B  1 191 ? -1.454  15.309  223.070 1.00 29.25  ? 191 ALA B N     1 
ATOM   5209  C CA    . ALA B  1 191 ? -0.809  16.221  224.003 1.00 35.99  ? 191 ALA B CA    1 
ATOM   5210  C C     . ALA B  1 191 ? 0.612   15.785  224.359 1.00 39.33  ? 191 ALA B C     1 
ATOM   5211  O O     . ALA B  1 191 ? 1.441   16.612  224.742 1.00 37.19  ? 191 ALA B O     1 
ATOM   5212  C CB    . ALA B  1 191 ? -1.646  16.347  225.256 1.00 34.08  ? 191 ALA B CB    1 
ATOM   5213  N N     . ASP B  1 192 ? 0.893   14.491  224.234 1.00 40.93  ? 192 ASP B N     1 
ATOM   5214  C CA    . ASP B  1 192 ? 2.226   13.968  224.528 1.00 40.66  ? 192 ASP B CA    1 
ATOM   5215  C C     . ASP B  1 192 ? 3.235   14.368  223.459 1.00 40.24  ? 192 ASP B C     1 
ATOM   5216  O O     . ASP B  1 192 ? 4.436   14.169  223.625 1.00 36.49  ? 192 ASP B O     1 
ATOM   5217  C CB    . ASP B  1 192 ? 2.198   12.442  224.654 1.00 36.56  ? 192 ASP B CB    1 
ATOM   5218  C CG    . ASP B  1 192 ? 1.432   11.970  225.867 1.00 40.92  ? 192 ASP B CG    1 
ATOM   5219  O OD1   . ASP B  1 192 ? 1.431   12.690  226.888 1.00 40.09  ? 192 ASP B OD1   1 
ATOM   5220  O OD2   . ASP B  1 192 ? 0.826   10.880  225.797 1.00 40.75  ? 192 ASP B OD2   1 
ATOM   5221  N N     . ASN B  1 193 ? 2.738   14.926  222.361 1.00 41.27  ? 193 ASN B N     1 
ATOM   5222  C CA    . ASN B  1 193 ? 3.589   15.298  221.240 1.00 38.46  ? 193 ASN B CA    1 
ATOM   5223  C C     . ASN B  1 193 ? 3.530   16.795  220.942 1.00 37.44  ? 193 ASN B C     1 
ATOM   5224  O O     . ASN B  1 193 ? 3.782   17.227  219.818 1.00 35.48  ? 193 ASN B O     1 
ATOM   5225  C CB    . ASN B  1 193 ? 3.206   14.492  219.998 1.00 38.05  ? 193 ASN B CB    1 
ATOM   5226  C CG    . ASN B  1 193 ? 3.501   13.009  220.156 1.00 42.57  ? 193 ASN B CG    1 
ATOM   5227  O OD1   . ASN B  1 193 ? 4.627   12.564  219.935 1.00 37.50  ? 193 ASN B OD1   1 
ATOM   5228  N ND2   . ASN B  1 193 ? 2.491   12.240  220.542 1.00 36.10  ? 193 ASN B ND2   1 
ATOM   5229  N N     . VAL B  1 194 ? 3.193   17.576  221.963 1.00 38.12  ? 194 VAL B N     1 
ATOM   5230  C CA    . VAL B  1 194 ? 3.215   19.032  221.876 1.00 38.33  ? 194 VAL B CA    1 
ATOM   5231  C C     . VAL B  1 194 ? 4.546   19.549  222.411 1.00 35.09  ? 194 VAL B C     1 
ATOM   5232  O O     . VAL B  1 194 ? 4.940   19.208  223.524 1.00 37.83  ? 194 VAL B O     1 
ATOM   5233  C CB    . VAL B  1 194 ? 2.055   19.661  222.671 1.00 35.38  ? 194 VAL B CB    1 
ATOM   5234  C CG1   . VAL B  1 194 ? 2.257   21.165  222.829 1.00 31.97  ? 194 VAL B CG1   1 
ATOM   5235  C CG2   . VAL B  1 194 ? 0.722   19.348  222.001 1.00 33.13  ? 194 VAL B CG2   1 
ATOM   5236  N N     . VAL B  1 195 ? 5.239   20.366  221.622 1.00 34.74  ? 195 VAL B N     1 
ATOM   5237  C CA    . VAL B  1 195 ? 6.569   20.834  222.006 1.00 36.98  ? 195 VAL B CA    1 
ATOM   5238  C C     . VAL B  1 195 ? 6.583   22.321  222.341 1.00 40.98  ? 195 VAL B C     1 
ATOM   5239  O O     . VAL B  1 195 ? 7.514   22.818  222.976 1.00 39.65  ? 195 VAL B O     1 
ATOM   5240  C CB    . VAL B  1 195 ? 7.595   20.562  220.897 1.00 39.43  ? 195 VAL B CB    1 
ATOM   5241  C CG1   . VAL B  1 195 ? 7.833   19.066  220.762 1.00 33.17  ? 195 VAL B CG1   1 
ATOM   5242  C CG2   . VAL B  1 195 ? 7.123   21.159  219.581 1.00 38.95  ? 195 VAL B CG2   1 
ATOM   5243  N N     . ASP B  1 196 ? 5.545   23.023  221.904 1.00 37.31  ? 196 ASP B N     1 
ATOM   5244  C CA    . ASP B  1 196 ? 5.368   24.428  222.239 1.00 37.44  ? 196 ASP B CA    1 
ATOM   5245  C C     . ASP B  1 196 ? 3.901   24.798  222.050 1.00 35.67  ? 196 ASP B C     1 
ATOM   5246  O O     . ASP B  1 196 ? 3.128   24.032  221.474 1.00 33.14  ? 196 ASP B O     1 
ATOM   5247  C CB    . ASP B  1 196 ? 6.267   25.317  221.376 1.00 37.60  ? 196 ASP B CB    1 
ATOM   5248  C CG    . ASP B  1 196 ? 6.576   26.650  222.034 1.00 40.69  ? 196 ASP B CG    1 
ATOM   5249  O OD1   . ASP B  1 196 ? 5.735   27.146  222.813 1.00 38.02  ? 196 ASP B OD1   1 
ATOM   5250  O OD2   . ASP B  1 196 ? 7.665   27.200  221.773 1.00 46.66  ? 196 ASP B OD2   1 
ATOM   5251  N N     . ALA B  1 197 ? 3.517   25.969  222.541 1.00 36.10  ? 197 ALA B N     1 
ATOM   5252  C CA    . ALA B  1 197 ? 2.150   26.435  222.377 1.00 37.40  ? 197 ALA B CA    1 
ATOM   5253  C C     . ALA B  1 197 ? 2.066   27.935  222.583 1.00 39.78  ? 197 ALA B C     1 
ATOM   5254  O O     . ALA B  1 197 ? 2.912   28.527  223.249 1.00 38.67  ? 197 ALA B O     1 
ATOM   5255  C CB    . ALA B  1 197 ? 1.216   25.714  223.346 1.00 33.92  ? 197 ALA B CB    1 
ATOM   5256  N N     . ILE B  1 198 ? 1.042   28.551  222.007 1.00 30.30  ? 198 ILE B N     1 
ATOM   5257  C CA    . ILE B  1 198 ? 0.759   29.950  222.293 1.00 28.60  ? 198 ILE B CA    1 
ATOM   5258  C C     . ILE B  1 198 ? -0.491  30.047  223.158 1.00 33.84  ? 198 ILE B C     1 
ATOM   5259  O O     . ILE B  1 198 ? -1.599  29.773  222.698 1.00 35.60  ? 198 ILE B O     1 
ATOM   5260  C CB    . ILE B  1 198 ? 0.570   30.776  221.012 1.00 35.25  ? 198 ILE B CB    1 
ATOM   5261  C CG1   . ILE B  1 198 ? 1.832   30.701  220.148 1.00 34.73  ? 198 ILE B CG1   1 
ATOM   5262  C CG2   . ILE B  1 198 ? 0.252   32.218  221.360 1.00 32.99  ? 198 ILE B CG2   1 
ATOM   5263  C CD1   . ILE B  1 198 ? 3.102   31.032  220.898 1.00 35.75  ? 198 ILE B CD1   1 
ATOM   5264  N N     . LEU B  1 199 ? -0.304  30.414  224.421 1.00 30.49  ? 199 LEU B N     1 
ATOM   5265  C CA    . LEU B  1 199 ? -1.416  30.557  225.348 1.00 30.84  ? 199 LEU B CA    1 
ATOM   5266  C C     . LEU B  1 199 ? -1.678  32.024  225.656 1.00 36.25  ? 199 LEU B C     1 
ATOM   5267  O O     . LEU B  1 199 ? -0.753  32.783  225.953 1.00 35.57  ? 199 LEU B O     1 
ATOM   5268  C CB    . LEU B  1 199 ? -1.142  29.790  226.644 1.00 33.13  ? 199 LEU B CB    1 
ATOM   5269  C CG    . LEU B  1 199 ? -2.228  29.887  227.721 1.00 35.79  ? 199 LEU B CG    1 
ATOM   5270  C CD1   . LEU B  1 199 ? -3.505  29.185  227.273 1.00 30.70  ? 199 LEU B CD1   1 
ATOM   5271  C CD2   . LEU B  1 199 ? -1.734  29.322  229.044 1.00 31.17  ? 199 LEU B CD2   1 
ATOM   5272  N N     . ILE B  1 200 ? -2.942  32.423  225.574 1.00 32.51  ? 200 ILE B N     1 
ATOM   5273  C CA    . ILE B  1 200 ? -3.335  33.787  225.896 1.00 29.75  ? 200 ILE B CA    1 
ATOM   5274  C C     . ILE B  1 200 ? -4.083  33.786  227.224 1.00 34.11  ? 200 ILE B C     1 
ATOM   5275  O O     . ILE B  1 200 ? -5.139  33.168  227.347 1.00 39.87  ? 200 ILE B O     1 
ATOM   5276  C CB    . ILE B  1 200 ? -4.206  34.398  224.784 1.00 34.74  ? 200 ILE B CB    1 
ATOM   5277  C CG1   . ILE B  1 200 ? -3.463  34.343  223.447 1.00 34.41  ? 200 ILE B CG1   1 
ATOM   5278  C CG2   . ILE B  1 200 ? -4.579  35.828  225.124 1.00 36.25  ? 200 ILE B CG2   1 
ATOM   5279  C CD1   . ILE B  1 200 ? -4.173  35.046  222.309 1.00 32.42  ? 200 ILE B CD1   1 
ATOM   5280  N N     . ASP B  1 201 ? -3.532  34.471  228.222 1.00 33.49  ? 201 ASP B N     1 
ATOM   5281  C CA    . ASP B  1 201 ? -4.080  34.390  229.574 1.00 34.69  ? 201 ASP B CA    1 
ATOM   5282  C C     . ASP B  1 201 ? -5.218  35.383  229.800 1.00 36.32  ? 201 ASP B C     1 
ATOM   5283  O O     . ASP B  1 201 ? -5.661  36.053  228.868 1.00 35.35  ? 201 ASP B O     1 
ATOM   5284  C CB    . ASP B  1 201 ? -2.971  34.590  230.617 1.00 36.15  ? 201 ASP B CB    1 
ATOM   5285  C CG    . ASP B  1 201 ? -2.503  36.036  230.739 1.00 40.52  ? 201 ASP B CG    1 
ATOM   5286  O OD1   . ASP B  1 201 ? -2.874  36.894  229.908 1.00 40.45  ? 201 ASP B OD1   1 
ATOM   5287  O OD2   . ASP B  1 201 ? -1.735  36.312  231.686 1.00 47.70  ? 201 ASP B OD2   1 
ATOM   5288  N N     . ALA B  1 202 ? -5.669  35.482  231.046 1.00 37.36  ? 202 ALA B N     1 
ATOM   5289  C CA    . ALA B  1 202 ? -6.846  36.274  231.388 1.00 39.79  ? 202 ALA B CA    1 
ATOM   5290  C C     . ALA B  1 202 ? -6.651  37.775  231.171 1.00 42.79  ? 202 ALA B C     1 
ATOM   5291  O O     . ALA B  1 202 ? -7.625  38.521  231.053 1.00 41.33  ? 202 ALA B O     1 
ATOM   5292  C CB    . ALA B  1 202 ? -7.241  36.007  232.830 1.00 47.21  ? 202 ALA B CB    1 
ATOM   5293  N N     . ASN B  1 203 ? -5.396  38.213  231.127 1.00 44.10  ? 203 ASN B N     1 
ATOM   5294  C CA    . ASN B  1 203 ? -5.082  39.621  230.905 1.00 39.39  ? 203 ASN B CA    1 
ATOM   5295  C C     . ASN B  1 203 ? -4.840  39.926  229.432 1.00 37.10  ? 203 ASN B C     1 
ATOM   5296  O O     . ASN B  1 203 ? -4.567  41.067  229.062 1.00 40.74  ? 203 ASN B O     1 
ATOM   5297  C CB    . ASN B  1 203 ? -3.854  40.032  231.722 1.00 42.62  ? 203 ASN B CB    1 
ATOM   5298  C CG    . ASN B  1 203 ? -4.049  39.826  233.209 1.00 47.80  ? 203 ASN B CG    1 
ATOM   5299  O OD1   . ASN B  1 203 ? -3.185  39.273  233.889 1.00 53.48  ? 203 ASN B OD1   1 
ATOM   5300  N ND2   . ASN B  1 203 ? -5.193  40.265  233.723 1.00 50.85  ? 203 ASN B ND2   1 
ATOM   5301  N N     . GLY B  1 204 ? -4.939  38.900  228.594 1.00 34.11  ? 204 GLY B N     1 
ATOM   5302  C CA    . GLY B  1 204 ? -4.684  39.055  227.175 1.00 35.62  ? 204 GLY B CA    1 
ATOM   5303  C C     . GLY B  1 204 ? -3.212  38.914  226.826 1.00 35.31  ? 204 GLY B C     1 
ATOM   5304  O O     . GLY B  1 204 ? -2.809  39.145  225.685 1.00 32.77  ? 204 GLY B O     1 
ATOM   5305  N N     . ALA B  1 205 ? -2.405  38.540  227.814 1.00 28.38  ? 205 ALA B N     1 
ATOM   5306  C CA    . ALA B  1 205 ? -0.976  38.339  227.594 1.00 35.77  ? 205 ALA B CA    1 
ATOM   5307  C C     . ALA B  1 205 ? -0.736  37.130  226.704 1.00 32.75  ? 205 ALA B C     1 
ATOM   5308  O O     . ALA B  1 205 ? -1.210  36.030  226.988 1.00 35.76  ? 205 ALA B O     1 
ATOM   5309  C CB    . ALA B  1 205 ? -0.246  38.175  228.915 1.00 27.46  ? 205 ALA B CB    1 
ATOM   5310  N N     . ILE B  1 206 ? -0.001  37.346  225.620 1.00 29.29  ? 206 ILE B N     1 
ATOM   5311  C CA    . ILE B  1 206 ? 0.298   36.283  224.672 1.00 31.03  ? 206 ILE B CA    1 
ATOM   5312  C C     . ILE B  1 206 ? 1.592   35.575  225.061 1.00 33.89  ? 206 ILE B C     1 
ATOM   5313  O O     . ILE B  1 206 ? 2.669   36.166  225.029 1.00 39.24  ? 206 ILE B O     1 
ATOM   5314  C CB    . ILE B  1 206 ? 0.397   36.838  223.243 1.00 32.58  ? 206 ILE B CB    1 
ATOM   5315  C CG1   . ILE B  1 206 ? -0.911  37.539  222.870 1.00 32.47  ? 206 ILE B CG1   1 
ATOM   5316  C CG2   . ILE B  1 206 ? 0.718   35.726  222.261 1.00 31.89  ? 206 ILE B CG2   1 
ATOM   5317  C CD1   . ILE B  1 206 ? -0.890  38.221  221.519 1.00 30.32  ? 206 ILE B CD1   1 
ATOM   5318  N N     . LEU B  1 207 ? 1.476   34.304  225.430 1.00 35.32  ? 207 LEU B N     1 
ATOM   5319  C CA    . LEU B  1 207 ? 2.586   33.573  226.026 1.00 33.79  ? 207 LEU B CA    1 
ATOM   5320  C C     . LEU B  1 207 ? 2.948   32.333  225.225 1.00 36.38  ? 207 LEU B C     1 
ATOM   5321  O O     . LEU B  1 207 ? 2.068   31.612  224.760 1.00 32.46  ? 207 LEU B O     1 
ATOM   5322  C CB    . LEU B  1 207 ? 2.234   33.167  227.462 1.00 35.41  ? 207 LEU B CB    1 
ATOM   5323  C CG    . LEU B  1 207 ? 1.631   34.239  228.373 1.00 39.80  ? 207 LEU B CG    1 
ATOM   5324  C CD1   . LEU B  1 207 ? 0.979   33.600  229.590 1.00 36.90  ? 207 LEU B CD1   1 
ATOM   5325  C CD2   . LEU B  1 207 ? 2.693   35.255  228.800 1.00 38.19  ? 207 LEU B CD2   1 
ATOM   5326  N N     . ASP B  1 208 ? 4.243   32.081  225.060 1.00 35.22  ? 208 ASP B N     1 
ATOM   5327  C CA    . ASP B  1 208 ? 4.690   30.803  224.518 1.00 27.23  ? 208 ASP B CA    1 
ATOM   5328  C C     . ASP B  1 208 ? 5.223   29.952  225.661 1.00 32.42  ? 208 ASP B C     1 
ATOM   5329  O O     . ASP B  1 208 ? 5.113   30.347  226.819 1.00 31.02  ? 208 ASP B O     1 
ATOM   5330  C CB    . ASP B  1 208 ? 5.745   30.996  223.422 1.00 35.21  ? 208 ASP B CB    1 
ATOM   5331  C CG    . ASP B  1 208 ? 7.020   31.658  223.927 1.00 40.52  ? 208 ASP B CG    1 
ATOM   5332  O OD1   . ASP B  1 208 ? 7.086   32.084  225.101 1.00 35.26  ? 208 ASP B OD1   1 
ATOM   5333  O OD2   . ASP B  1 208 ? 7.965   31.765  223.119 1.00 41.08  ? 208 ASP B OD2   1 
ATOM   5334  N N     . ARG B  1 209 ? 5.790   28.793  225.340 1.00 35.87  ? 209 ARG B N     1 
ATOM   5335  C CA    . ARG B  1 209 ? 6.259   27.861  226.364 1.00 34.21  ? 209 ARG B CA    1 
ATOM   5336  C C     . ARG B  1 209 ? 7.261   28.503  227.320 1.00 38.10  ? 209 ARG B C     1 
ATOM   5337  O O     . ARG B  1 209 ? 7.167   28.333  228.538 1.00 42.22  ? 209 ARG B O     1 
ATOM   5338  C CB    . ARG B  1 209 ? 6.892   26.624  225.725 1.00 39.89  ? 209 ARG B CB    1 
ATOM   5339  C CG    . ARG B  1 209 ? 7.461   25.649  226.735 1.00 34.14  ? 209 ARG B CG    1 
ATOM   5340  C CD    . ARG B  1 209 ? 8.076   24.439  226.061 1.00 38.26  ? 209 ARG B CD    1 
ATOM   5341  N NE    . ARG B  1 209 ? 8.458   23.426  227.040 1.00 38.97  ? 209 ARG B NE    1 
ATOM   5342  C CZ    . ARG B  1 209 ? 8.876   22.204  226.727 1.00 41.77  ? 209 ARG B CZ    1 
ATOM   5343  N NH1   . ARG B  1 209 ? 8.968   21.841  225.457 1.00 36.64  ? 209 ARG B NH1   1 
ATOM   5344  N NH2   . ARG B  1 209 ? 9.195   21.344  227.685 1.00 44.63  ? 209 ARG B NH2   1 
ATOM   5345  N N     . GLN B  1 210 ? 8.215   29.241  226.763 1.00 37.02  ? 210 GLN B N     1 
ATOM   5346  C CA    . GLN B  1 210 ? 9.212   29.936  227.569 1.00 45.70  ? 210 GLN B CA    1 
ATOM   5347  C C     . GLN B  1 210 ? 8.558   30.939  228.515 1.00 41.90  ? 210 GLN B C     1 
ATOM   5348  O O     . GLN B  1 210 ? 8.933   31.043  229.683 1.00 47.34  ? 210 GLN B O     1 
ATOM   5349  C CB    . GLN B  1 210 ? 10.223  30.647  226.666 1.00 44.93  ? 210 GLN B CB    1 
ATOM   5350  C CG    . GLN B  1 210 ? 11.401  31.255  227.406 1.00 61.20  ? 210 GLN B CG    1 
ATOM   5351  C CD    . GLN B  1 210 ? 12.449  31.828  226.472 1.00 62.78  ? 210 GLN B CD    1 
ATOM   5352  O OE1   . GLN B  1 210 ? 12.177  32.092  225.301 1.00 63.78  ? 210 GLN B OE1   1 
ATOM   5353  N NE2   . GLN B  1 210 ? 13.658  32.023  226.989 1.00 60.41  ? 210 GLN B NE2   1 
ATOM   5354  N N     . ALA B  1 211 ? 7.568   31.663  228.007 1.00 41.10  ? 211 ALA B N     1 
ATOM   5355  C CA    . ALA B  1 211 ? 6.941   32.735  228.767 1.00 34.87  ? 211 ALA B CA    1 
ATOM   5356  C C     . ALA B  1 211 ? 5.958   32.225  229.819 1.00 40.37  ? 211 ALA B C     1 
ATOM   5357  O O     . ALA B  1 211 ? 5.802   32.838  230.874 1.00 41.45  ? 211 ALA B O     1 
ATOM   5358  C CB    . ALA B  1 211 ? 6.239   33.695  227.821 1.00 38.61  ? 211 ALA B CB    1 
ATOM   5359  N N     . MET B  1 212 ? 5.299   31.106  229.539 1.00 38.97  ? 212 MET B N     1 
ATOM   5360  C CA    . MET B  1 212 ? 4.280   30.596  230.450 1.00 40.70  ? 212 MET B CA    1 
ATOM   5361  C C     . MET B  1 212 ? 4.887   29.729  231.549 1.00 40.32  ? 212 MET B C     1 
ATOM   5362  O O     . MET B  1 212 ? 4.244   29.456  232.560 1.00 41.16  ? 212 MET B O     1 
ATOM   5363  C CB    . MET B  1 212 ? 3.210   29.802  229.685 1.00 38.46  ? 212 MET B CB    1 
ATOM   5364  C CG    . MET B  1 212 ? 3.681   28.470  229.120 1.00 34.47  ? 212 MET B CG    1 
ATOM   5365  S SD    . MET B  1 212 ? 2.358   27.583  228.264 1.00 39.08  ? 212 MET B SD    1 
ATOM   5366  C CE    . MET B  1 212 ? 2.336   28.423  226.684 1.00 30.32  ? 212 MET B CE    1 
ATOM   5367  N N     . GLY B  1 213 ? 6.127   29.300  231.350 1.00 44.71  ? 213 GLY B N     1 
ATOM   5368  C CA    . GLY B  1 213 ? 6.781   28.427  232.305 1.00 44.24  ? 213 GLY B CA    1 
ATOM   5369  C C     . GLY B  1 213 ? 6.367   26.980  232.113 1.00 45.44  ? 213 GLY B C     1 
ATOM   5370  O O     . GLY B  1 213 ? 5.378   26.692  231.436 1.00 41.82  ? 213 GLY B O     1 
ATOM   5371  N N     . GLU B  1 214 ? 7.119   26.069  232.723 1.00 46.15  ? 214 GLU B N     1 
ATOM   5372  C CA    . GLU B  1 214 ? 6.932   24.643  232.485 1.00 45.72  ? 214 GLU B CA    1 
ATOM   5373  C C     . GLU B  1 214 ? 5.719   24.047  233.199 1.00 43.63  ? 214 GLU B C     1 
ATOM   5374  O O     . GLU B  1 214 ? 5.147   23.069  232.729 1.00 46.64  ? 214 GLU B O     1 
ATOM   5375  C CB    . GLU B  1 214 ? 8.195   23.875  232.885 1.00 45.43  ? 214 GLU B CB    1 
ATOM   5376  C CG    . GLU B  1 214 ? 9.344   24.028  231.894 1.00 46.53  ? 214 GLU B CG    1 
ATOM   5377  C CD    . GLU B  1 214 ? 8.992   23.512  230.513 1.00 43.09  ? 214 GLU B CD    1 
ATOM   5378  O OE1   . GLU B  1 214 ? 8.821   22.285  230.364 1.00 46.68  ? 214 GLU B OE1   1 
ATOM   5379  O OE2   . GLU B  1 214 ? 8.887   24.331  229.577 1.00 46.84  ? 214 GLU B OE2   1 
ATOM   5380  N N     . ASP B  1 215 ? 5.324   24.626  234.328 1.00 39.28  ? 215 ASP B N     1 
ATOM   5381  C CA    . ASP B  1 215 ? 4.145   24.143  235.045 1.00 45.12  ? 215 ASP B CA    1 
ATOM   5382  C C     . ASP B  1 215 ? 2.870   24.369  234.231 1.00 48.05  ? 215 ASP B C     1 
ATOM   5383  O O     . ASP B  1 215 ? 2.017   23.483  234.131 1.00 44.71  ? 215 ASP B O     1 
ATOM   5384  C CB    . ASP B  1 215 ? 4.025   24.822  236.413 1.00 47.32  ? 215 ASP B CB    1 
ATOM   5385  C CG    . ASP B  1 215 ? 5.030   24.292  237.418 1.00 53.51  ? 215 ASP B CG    1 
ATOM   5386  O OD1   . ASP B  1 215 ? 5.360   23.088  237.355 1.00 56.57  ? 215 ASP B OD1   1 
ATOM   5387  O OD2   . ASP B  1 215 ? 5.484   25.076  238.277 1.00 55.28  ? 215 ASP B OD2   1 
ATOM   5388  N N     . VAL B  1 216 ? 2.749   25.563  233.658 1.00 45.12  ? 216 VAL B N     1 
ATOM   5389  C CA    . VAL B  1 216 ? 1.603   25.907  232.825 1.00 40.86  ? 216 VAL B CA    1 
ATOM   5390  C C     . VAL B  1 216 ? 1.650   25.160  231.493 1.00 41.40  ? 216 VAL B C     1 
ATOM   5391  O O     . VAL B  1 216 ? 0.627   24.664  231.017 1.00 39.63  ? 216 VAL B O     1 
ATOM   5392  C CB    . VAL B  1 216 ? 1.527   27.425  232.559 1.00 38.15  ? 216 VAL B CB    1 
ATOM   5393  C CG1   . VAL B  1 216 ? 0.376   27.747  231.613 1.00 38.28  ? 216 VAL B CG1   1 
ATOM   5394  C CG2   . VAL B  1 216 ? 1.375   28.187  233.870 1.00 37.56  ? 216 VAL B CG2   1 
ATOM   5395  N N     . PHE B  1 217 ? 2.837   25.068  230.898 1.00 38.46  ? 217 PHE B N     1 
ATOM   5396  C CA    . PHE B  1 217 ? 2.997   24.339  229.639 1.00 37.66  ? 217 PHE B CA    1 
ATOM   5397  C C     . PHE B  1 217 ? 2.672   22.865  229.818 1.00 39.59  ? 217 PHE B C     1 
ATOM   5398  O O     . PHE B  1 217 ? 2.219   22.198  228.887 1.00 35.84  ? 217 PHE B O     1 
ATOM   5399  C CB    . PHE B  1 217 ? 4.415   24.485  229.082 1.00 37.99  ? 217 PHE B CB    1 
ATOM   5400  C CG    . PHE B  1 217 ? 4.646   23.702  227.818 1.00 40.06  ? 217 PHE B CG    1 
ATOM   5401  C CD1   . PHE B  1 217 ? 4.087   24.120  226.621 1.00 37.09  ? 217 PHE B CD1   1 
ATOM   5402  C CD2   . PHE B  1 217 ? 5.405   22.543  227.826 1.00 32.44  ? 217 PHE B CD2   1 
ATOM   5403  C CE1   . PHE B  1 217 ? 4.286   23.403  225.456 1.00 35.77  ? 217 PHE B CE1   1 
ATOM   5404  C CE2   . PHE B  1 217 ? 5.609   21.823  226.660 1.00 31.81  ? 217 PHE B CE2   1 
ATOM   5405  C CZ    . PHE B  1 217 ? 5.049   22.256  225.474 1.00 36.99  ? 217 PHE B CZ    1 
ATOM   5406  N N     . TRP B  1 218 ? 2.922   22.362  231.021 1.00 38.76  ? 218 TRP B N     1 
ATOM   5407  C CA    . TRP B  1 218 ? 2.577   20.993  231.369 1.00 41.94  ? 218 TRP B CA    1 
ATOM   5408  C C     . TRP B  1 218 ? 1.067   20.860  231.519 1.00 40.66  ? 218 TRP B C     1 
ATOM   5409  O O     . TRP B  1 218 ? 0.465   19.935  230.983 1.00 38.39  ? 218 TRP B O     1 
ATOM   5410  C CB    . TRP B  1 218 ? 3.293   20.578  232.658 1.00 41.74  ? 218 TRP B CB    1 
ATOM   5411  C CG    . TRP B  1 218 ? 2.872   19.261  233.233 1.00 39.91  ? 218 TRP B CG    1 
ATOM   5412  C CD1   . TRP B  1 218 ? 3.335   18.026  232.883 1.00 42.31  ? 218 TRP B CD1   1 
ATOM   5413  C CD2   . TRP B  1 218 ? 1.922   19.050  234.284 1.00 42.62  ? 218 TRP B CD2   1 
ATOM   5414  N NE1   . TRP B  1 218 ? 2.722   17.058  233.642 1.00 41.06  ? 218 TRP B NE1   1 
ATOM   5415  C CE2   . TRP B  1 218 ? 1.850   17.661  234.510 1.00 40.21  ? 218 TRP B CE2   1 
ATOM   5416  C CE3   . TRP B  1 218 ? 1.118   19.901  235.050 1.00 42.98  ? 218 TRP B CE3   1 
ATOM   5417  C CZ2   . TRP B  1 218 ? 1.008   17.104  235.471 1.00 42.17  ? 218 TRP B CZ2   1 
ATOM   5418  C CZ3   . TRP B  1 218 ? 0.284   19.347  236.003 1.00 45.89  ? 218 TRP B CZ3   1 
ATOM   5419  C CH2   . TRP B  1 218 ? 0.234   17.962  236.205 1.00 46.28  ? 218 TRP B CH2   1 
ATOM   5420  N N     . ALA B  1 219 ? 0.462   21.809  232.225 1.00 39.13  ? 219 ALA B N     1 
ATOM   5421  C CA    . ALA B  1 219 ? -0.959  21.753  232.554 1.00 38.48  ? 219 ALA B CA    1 
ATOM   5422  C C     . ALA B  1 219 ? -1.870  21.784  231.328 1.00 38.47  ? 219 ALA B C     1 
ATOM   5423  O O     . ALA B  1 219 ? -2.901  21.119  231.304 1.00 40.34  ? 219 ALA B O     1 
ATOM   5424  C CB    . ALA B  1 219 ? -1.314  22.894  233.483 1.00 41.37  ? 219 ALA B CB    1 
ATOM   5425  N N     . ILE B  1 220 ? -1.497  22.558  230.314 1.00 38.30  ? 220 ILE B N     1 
ATOM   5426  C CA    . ILE B  1 220 ? -2.335  22.694  229.125 1.00 40.60  ? 220 ILE B CA    1 
ATOM   5427  C C     . ILE B  1 220 ? -2.277  21.457  228.228 1.00 36.81  ? 220 ILE B C     1 
ATOM   5428  O O     . ILE B  1 220 ? -3.094  21.300  227.323 1.00 33.87  ? 220 ILE B O     1 
ATOM   5429  C CB    . ILE B  1 220 ? -1.937  23.924  228.289 1.00 33.42  ? 220 ILE B CB    1 
ATOM   5430  C CG1   . ILE B  1 220 ? -0.492  23.794  227.802 1.00 35.23  ? 220 ILE B CG1   1 
ATOM   5431  C CG2   . ILE B  1 220 ? -2.141  25.201  229.092 1.00 35.22  ? 220 ILE B CG2   1 
ATOM   5432  C CD1   . ILE B  1 220 ? -0.076  24.878  226.828 1.00 33.62  ? 220 ILE B CD1   1 
ATOM   5433  N N     . ARG B  1 221 ? -1.307  20.585  228.483 1.00 36.85  ? 221 ARG B N     1 
ATOM   5434  C CA    . ARG B  1 221 ? -1.132  19.380  227.681 1.00 39.61  ? 221 ARG B CA    1 
ATOM   5435  C C     . ARG B  1 221 ? -1.896  18.199  228.267 1.00 36.36  ? 221 ARG B C     1 
ATOM   5436  O O     . ARG B  1 221 ? -1.350  17.105  228.409 1.00 36.76  ? 221 ARG B O     1 
ATOM   5437  C CB    . ARG B  1 221 ? 0.353   19.034  227.554 1.00 36.27  ? 221 ARG B CB    1 
ATOM   5438  C CG    . ARG B  1 221 ? 1.136   19.979  226.658 1.00 37.48  ? 221 ARG B CG    1 
ATOM   5439  C CD    . ARG B  1 221 ? 2.598   19.578  226.594 1.00 37.91  ? 221 ARG B CD    1 
ATOM   5440  N NE    . ARG B  1 221 ? 3.292   19.838  227.850 1.00 37.21  ? 221 ARG B NE    1 
ATOM   5441  C CZ    . ARG B  1 221 ? 4.312   19.116  228.301 1.00 41.57  ? 221 ARG B CZ    1 
ATOM   5442  N NH1   . ARG B  1 221 ? 4.747   18.077  227.600 1.00 41.08  ? 221 ARG B NH1   1 
ATOM   5443  N NH2   . ARG B  1 221 ? 4.888   19.426  229.456 1.00 39.92  ? 221 ARG B NH2   1 
ATOM   5444  N N     . GLY B  1 222 ? -3.161  18.426  228.609 1.00 38.15  ? 222 GLY B N     1 
ATOM   5445  C CA    . GLY B  1 222 ? -4.001  17.365  229.132 1.00 40.48  ? 222 GLY B CA    1 
ATOM   5446  C C     . GLY B  1 222 ? -4.860  17.776  230.313 1.00 38.51  ? 222 GLY B C     1 
ATOM   5447  O O     . GLY B  1 222 ? -5.736  17.025  230.738 1.00 39.37  ? 222 GLY B O     1 
ATOM   5448  N N     . GLY B  1 223 ? -4.619  18.971  230.843 1.00 38.18  ? 223 GLY B N     1 
ATOM   5449  C CA    . GLY B  1 223 ? -5.342  19.437  232.014 1.00 42.08  ? 223 GLY B CA    1 
ATOM   5450  C C     . GLY B  1 223 ? -6.765  19.888  231.743 1.00 40.61  ? 223 GLY B C     1 
ATOM   5451  O O     . GLY B  1 223 ? -7.470  20.309  232.660 1.00 41.96  ? 223 GLY B O     1 
ATOM   5452  N N     . GLY B  1 224 ? -7.186  19.810  230.485 1.00 38.01  ? 224 GLY B N     1 
ATOM   5453  C CA    . GLY B  1 224 ? -8.551  20.141  230.113 1.00 36.06  ? 224 GLY B CA    1 
ATOM   5454  C C     . GLY B  1 224 ? -8.720  21.557  229.595 1.00 35.10  ? 224 GLY B C     1 
ATOM   5455  O O     . GLY B  1 224 ? -8.123  22.497  230.121 1.00 37.53  ? 224 GLY B O     1 
ATOM   5456  N N     . GLY B  1 225 ? -9.549  21.712  228.567 1.00 34.90  ? 225 GLY B N     1 
ATOM   5457  C CA    . GLY B  1 225 ? -9.795  23.016  227.982 1.00 35.17  ? 225 GLY B CA    1 
ATOM   5458  C C     . GLY B  1 225 ? -10.671 23.902  228.846 1.00 35.56  ? 225 GLY B C     1 
ATOM   5459  O O     . GLY B  1 225 ? -11.300 23.431  229.795 1.00 36.13  ? 225 GLY B O     1 
ATOM   5460  N N     . GLY B  1 226 ? -10.699 25.191  228.518 1.00 32.83  ? 226 GLY B N     1 
ATOM   5461  C CA    . GLY B  1 226 ? -11.541 26.155  229.206 1.00 34.67  ? 226 GLY B CA    1 
ATOM   5462  C C     . GLY B  1 226 ? -11.126 26.456  230.634 1.00 39.65  ? 226 GLY B C     1 
ATOM   5463  O O     . GLY B  1 226 ? -11.963 26.819  231.461 1.00 35.29  ? 226 GLY B O     1 
ATOM   5464  N N     . VAL B  1 227 ? -9.836  26.321  230.928 1.00 37.13  ? 227 VAL B N     1 
ATOM   5465  C CA    . VAL B  1 227 ? -9.366  26.416  232.305 1.00 38.69  ? 227 VAL B CA    1 
ATOM   5466  C C     . VAL B  1 227 ? -8.152  27.338  232.472 1.00 36.51  ? 227 VAL B C     1 
ATOM   5467  O O     . VAL B  1 227 ? -8.031  28.049  233.473 1.00 38.58  ? 227 VAL B O     1 
ATOM   5468  C CB    . VAL B  1 227 ? -9.022  25.005  232.849 1.00 39.68  ? 227 VAL B CB    1 
ATOM   5469  C CG1   . VAL B  1 227 ? -8.337  25.082  234.203 1.00 41.21  ? 227 VAL B CG1   1 
ATOM   5470  C CG2   . VAL B  1 227 ? -10.283 24.154  232.937 1.00 40.92  ? 227 VAL B CG2   1 
ATOM   5471  N N     . TRP B  1 228 ? -7.273  27.348  231.476 1.00 37.55  ? 228 TRP B N     1 
ATOM   5472  C CA    . TRP B  1 228 ? -5.963  27.982  231.617 1.00 34.81  ? 228 TRP B CA    1 
ATOM   5473  C C     . TRP B  1 228 ? -5.854  29.307  230.883 1.00 42.29  ? 228 TRP B C     1 
ATOM   5474  O O     . TRP B  1 228 ? -4.931  30.086  231.117 1.00 43.04  ? 228 TRP B O     1 
ATOM   5475  C CB    . TRP B  1 228 ? -4.882  27.028  231.116 1.00 37.54  ? 228 TRP B CB    1 
ATOM   5476  C CG    . TRP B  1 228 ? -5.157  25.635  231.541 1.00 39.83  ? 228 TRP B CG    1 
ATOM   5477  C CD1   . TRP B  1 228 ? -5.733  24.648  230.797 1.00 37.27  ? 228 TRP B CD1   1 
ATOM   5478  C CD2   . TRP B  1 228 ? -4.909  25.075  232.831 1.00 39.56  ? 228 TRP B CD2   1 
ATOM   5479  N NE1   . TRP B  1 228 ? -5.846  23.502  231.542 1.00 41.15  ? 228 TRP B NE1   1 
ATOM   5480  C CE2   . TRP B  1 228 ? -5.346  23.738  232.796 1.00 40.62  ? 228 TRP B CE2   1 
ATOM   5481  C CE3   . TRP B  1 228 ? -4.351  25.573  234.012 1.00 41.28  ? 228 TRP B CE3   1 
ATOM   5482  C CZ2   . TRP B  1 228 ? -5.242  22.891  233.897 1.00 43.11  ? 228 TRP B CZ2   1 
ATOM   5483  C CZ3   . TRP B  1 228 ? -4.250  24.732  235.102 1.00 42.70  ? 228 TRP B CZ3   1 
ATOM   5484  C CH2   . TRP B  1 228 ? -4.692  23.406  235.038 1.00 41.26  ? 228 TRP B CH2   1 
ATOM   5485  N N     . GLY B  1 229 ? -6.811  29.561  230.003 1.00 34.34  ? 229 GLY B N     1 
ATOM   5486  C CA    . GLY B  1 229 ? -6.736  30.685  229.095 1.00 28.91  ? 229 GLY B CA    1 
ATOM   5487  C C     . GLY B  1 229 ? -7.105  30.174  227.720 1.00 33.48  ? 229 GLY B C     1 
ATOM   5488  O O     . GLY B  1 229 ? -7.593  29.054  227.586 1.00 37.69  ? 229 GLY B O     1 
ATOM   5489  N N     . ALA B  1 230 ? -6.874  30.983  226.695 1.00 33.63  ? 230 ALA B N     1 
ATOM   5490  C CA    . ALA B  1 230 ? -7.204  30.572  225.339 1.00 30.53  ? 230 ALA B CA    1 
ATOM   5491  C C     . ALA B  1 230 ? -5.962  30.125  224.587 1.00 37.26  ? 230 ALA B C     1 
ATOM   5492  O O     . ALA B  1 230 ? -5.048  30.918  224.363 1.00 35.76  ? 230 ALA B O     1 
ATOM   5493  C CB    . ALA B  1 230 ? -7.894  31.703  224.594 1.00 30.57  ? 230 ALA B CB    1 
ATOM   5494  N N     . ILE B  1 231 ? -5.925  28.851  224.206 1.00 29.03  ? 231 ILE B N     1 
ATOM   5495  C CA    . ILE B  1 231 ? -4.861  28.361  223.344 1.00 31.72  ? 231 ILE B CA    1 
ATOM   5496  C C     . ILE B  1 231 ? -5.037  28.981  221.970 1.00 35.03  ? 231 ILE B C     1 
ATOM   5497  O O     . ILE B  1 231 ? -6.092  28.835  221.360 1.00 34.35  ? 231 ILE B O     1 
ATOM   5498  C CB    . ILE B  1 231 ? -4.870  26.825  223.211 1.00 35.33  ? 231 ILE B CB    1 
ATOM   5499  C CG1   . ILE B  1 231 ? -4.694  26.159  224.574 1.00 38.29  ? 231 ILE B CG1   1 
ATOM   5500  C CG2   . ILE B  1 231 ? -3.773  26.372  222.258 1.00 31.91  ? 231 ILE B CG2   1 
ATOM   5501  C CD1   . ILE B  1 231 ? -3.269  26.170  225.083 1.00 33.03  ? 231 ILE B CD1   1 
ATOM   5502  N N     . TYR B  1 232 ? -4.023  29.691  221.489 1.00 31.93  ? 232 TYR B N     1 
ATOM   5503  C CA    . TYR B  1 232 ? -4.089  30.239  220.142 1.00 31.53  ? 232 TYR B CA    1 
ATOM   5504  C C     . TYR B  1 232 ? -3.600  29.207  219.134 1.00 35.15  ? 232 TYR B C     1 
ATOM   5505  O O     . TYR B  1 232 ? -4.208  29.019  218.080 1.00 37.44  ? 232 TYR B O     1 
ATOM   5506  C CB    . TYR B  1 232 ? -3.269  31.528  220.020 1.00 29.17  ? 232 TYR B CB    1 
ATOM   5507  C CG    . TYR B  1 232 ? -2.859  31.825  218.595 1.00 32.36  ? 232 TYR B CG    1 
ATOM   5508  C CD1   . TYR B  1 232 ? -3.809  32.113  217.622 1.00 32.37  ? 232 TYR B CD1   1 
ATOM   5509  C CD2   . TYR B  1 232 ? -1.522  31.798  218.218 1.00 34.64  ? 232 TYR B CD2   1 
ATOM   5510  C CE1   . TYR B  1 232 ? -3.439  32.367  216.314 1.00 32.25  ? 232 TYR B CE1   1 
ATOM   5511  C CE2   . TYR B  1 232 ? -1.142  32.054  216.914 1.00 34.85  ? 232 TYR B CE2   1 
ATOM   5512  C CZ    . TYR B  1 232 ? -2.105  32.338  215.967 1.00 35.90  ? 232 TYR B CZ    1 
ATOM   5513  O OH    . TYR B  1 232 ? -1.732  32.592  214.667 1.00 38.50  ? 232 TYR B OH    1 
ATOM   5514  N N     . ALA B  1 233 ? -2.502  28.534  219.464 1.00 32.52  ? 233 ALA B N     1 
ATOM   5515  C CA    . ALA B  1 233 ? -1.917  27.555  218.556 1.00 33.31  ? 233 ALA B CA    1 
ATOM   5516  C C     . ALA B  1 233 ? -1.107  26.487  219.287 1.00 33.67  ? 233 ALA B C     1 
ATOM   5517  O O     . ALA B  1 233 ? -0.557  26.732  220.361 1.00 32.15  ? 233 ALA B O     1 
ATOM   5518  C CB    . ALA B  1 233 ? -1.045  28.258  217.521 1.00 30.88  ? 233 ALA B CB    1 
ATOM   5519  N N     . TRP B  1 234 ? -1.049  25.299  218.693 1.00 33.21  ? 234 TRP B N     1 
ATOM   5520  C CA    . TRP B  1 234 ? -0.209  24.219  219.191 1.00 35.77  ? 234 TRP B CA    1 
ATOM   5521  C C     . TRP B  1 234 ? 0.994   24.033  218.274 1.00 35.63  ? 234 TRP B C     1 
ATOM   5522  O O     . TRP B  1 234 ? 0.859   24.099  217.051 1.00 36.64  ? 234 TRP B O     1 
ATOM   5523  C CB    . TRP B  1 234 ? -0.983  22.898  219.272 1.00 32.07  ? 234 TRP B CB    1 
ATOM   5524  C CG    . TRP B  1 234 ? -2.211  22.915  220.130 1.00 36.04  ? 234 TRP B CG    1 
ATOM   5525  C CD1   . TRP B  1 234 ? -3.509  22.993  219.707 1.00 33.95  ? 234 TRP B CD1   1 
ATOM   5526  C CD2   . TRP B  1 234 ? -2.259  22.825  221.557 1.00 33.10  ? 234 TRP B CD2   1 
ATOM   5527  N NE1   . TRP B  1 234 ? -4.360  22.966  220.786 1.00 30.75  ? 234 TRP B NE1   1 
ATOM   5528  C CE2   . TRP B  1 234 ? -3.619  22.862  221.934 1.00 30.53  ? 234 TRP B CE2   1 
ATOM   5529  C CE3   . TRP B  1 234 ? -1.285  22.719  222.555 1.00 31.78  ? 234 TRP B CE3   1 
ATOM   5530  C CZ2   . TRP B  1 234 ? -4.027  22.799  223.265 1.00 28.89  ? 234 TRP B CZ2   1 
ATOM   5531  C CZ3   . TRP B  1 234 ? -1.692  22.658  223.876 1.00 36.68  ? 234 TRP B CZ3   1 
ATOM   5532  C CH2   . TRP B  1 234 ? -3.052  22.699  224.219 1.00 33.17  ? 234 TRP B CH2   1 
ATOM   5533  N N     . LYS B  1 235 ? 2.167   23.808  218.856 1.00 34.14  ? 235 LYS B N     1 
ATOM   5534  C CA    . LYS B  1 235 ? 3.296   23.327  218.069 1.00 38.69  ? 235 LYS B CA    1 
ATOM   5535  C C     . LYS B  1 235 ? 3.492   21.845  218.357 1.00 35.70  ? 235 LYS B C     1 
ATOM   5536  O O     . LYS B  1 235 ? 3.836   21.457  219.474 1.00 35.71  ? 235 LYS B O     1 
ATOM   5537  C CB    . LYS B  1 235 ? 4.576   24.103  218.365 1.00 35.43  ? 235 LYS B CB    1 
ATOM   5538  C CG    . LYS B  1 235 ? 5.700   23.738  217.409 1.00 40.67  ? 235 LYS B CG    1 
ATOM   5539  C CD    . LYS B  1 235 ? 7.002   24.442  217.735 1.00 38.86  ? 235 LYS B CD    1 
ATOM   5540  C CE    . LYS B  1 235 ? 8.084   24.029  216.748 1.00 42.21  ? 235 LYS B CE    1 
ATOM   5541  N NZ    . LYS B  1 235 ? 9.423   24.568  217.118 1.00 43.79  ? 235 LYS B NZ    1 
ATOM   5542  N N     . ILE B  1 236 ? 3.257   21.017  217.346 1.00 41.62  ? 236 ILE B N     1 
ATOM   5543  C CA    . ILE B  1 236 ? 3.262   19.572  217.528 1.00 39.11  ? 236 ILE B CA    1 
ATOM   5544  C C     . ILE B  1 236 ? 4.399   18.894  216.779 1.00 43.95  ? 236 ILE B C     1 
ATOM   5545  O O     . ILE B  1 236 ? 4.868   19.392  215.759 1.00 45.88  ? 236 ILE B O     1 
ATOM   5546  C CB    . ILE B  1 236 ? 1.936   18.947  217.063 1.00 38.19  ? 236 ILE B CB    1 
ATOM   5547  C CG1   . ILE B  1 236 ? 1.663   19.307  215.601 1.00 38.85  ? 236 ILE B CG1   1 
ATOM   5548  C CG2   . ILE B  1 236 ? 0.787   19.395  217.952 1.00 36.68  ? 236 ILE B CG2   1 
ATOM   5549  C CD1   . ILE B  1 236 ? 0.442   18.631  215.020 1.00 40.80  ? 236 ILE B CD1   1 
ATOM   5550  N N     . LYS B  1 237 ? 4.832   17.751  217.300 1.00 39.45  ? 237 LYS B N     1 
ATOM   5551  C CA    . LYS B  1 237 ? 5.791   16.908  216.607 1.00 48.31  ? 237 LYS B CA    1 
ATOM   5552  C C     . LYS B  1 237 ? 5.075   16.052  215.571 1.00 48.87  ? 237 LYS B C     1 
ATOM   5553  O O     . LYS B  1 237 ? 4.141   15.324  215.903 1.00 47.43  ? 237 LYS B O     1 
ATOM   5554  C CB    . LYS B  1 237 ? 6.539   16.012  217.597 1.00 46.50  ? 237 LYS B CB    1 
ATOM   5555  C CG    . LYS B  1 237 ? 7.659   15.201  216.972 1.00 53.65  ? 237 LYS B CG    1 
ATOM   5556  C CD    . LYS B  1 237 ? 8.963   15.976  217.016 1.00 61.07  ? 237 LYS B CD    1 
ATOM   5557  C CE    . LYS B  1 237 ? 9.815   15.702  215.791 1.00 56.47  ? 237 LYS B CE    1 
ATOM   5558  N NZ    . LYS B  1 237 ? 11.018  16.578  215.757 1.00 66.55  ? 237 LYS B NZ    1 
ATOM   5559  N N     . LEU B  1 238 ? 5.501   16.145  214.315 1.00 49.93  ? 238 LEU B N     1 
ATOM   5560  C CA    . LEU B  1 238 ? 4.962   15.266  213.284 1.00 49.71  ? 238 LEU B CA    1 
ATOM   5561  C C     . LEU B  1 238 ? 5.663   13.915  213.380 1.00 54.44  ? 238 LEU B C     1 
ATOM   5562  O O     . LEU B  1 238 ? 6.854   13.845  213.681 1.00 44.37  ? 238 LEU B O     1 
ATOM   5563  C CB    . LEU B  1 238 ? 5.121   15.883  211.894 1.00 53.48  ? 238 LEU B CB    1 
ATOM   5564  C CG    . LEU B  1 238 ? 4.331   17.178  211.670 1.00 52.62  ? 238 LEU B CG    1 
ATOM   5565  C CD1   . LEU B  1 238 ? 4.510   17.694  210.253 1.00 52.42  ? 238 LEU B CD1   1 
ATOM   5566  C CD2   . LEU B  1 238 ? 2.855   16.984  211.988 1.00 49.96  ? 238 LEU B CD2   1 
ATOM   5567  N N     . LEU B  1 239 ? 4.919   12.844  213.136 1.00 52.25  ? 239 LEU B N     1 
ATOM   5568  C CA    . LEU B  1 239 ? 5.393   11.506  213.464 1.00 49.74  ? 239 LEU B CA    1 
ATOM   5569  C C     . LEU B  1 239 ? 5.543   10.608  212.239 1.00 55.75  ? 239 LEU B C     1 
ATOM   5570  O O     . LEU B  1 239 ? 4.666   10.576  211.375 1.00 53.34  ? 239 LEU B O     1 
ATOM   5571  C CB    . LEU B  1 239 ? 4.441   10.865  214.477 1.00 54.22  ? 239 LEU B CB    1 
ATOM   5572  C CG    . LEU B  1 239 ? 4.161   11.752  215.694 1.00 51.35  ? 239 LEU B CG    1 
ATOM   5573  C CD1   . LEU B  1 239 ? 2.924   11.285  216.445 1.00 45.57  ? 239 LEU B CD1   1 
ATOM   5574  C CD2   . LEU B  1 239 ? 5.374   11.798  216.616 1.00 43.62  ? 239 LEU B CD2   1 
ATOM   5575  N N     . PRO B  1 240 ? 6.666   9.873   212.167 1.00 55.23  ? 240 PRO B N     1 
ATOM   5576  C CA    . PRO B  1 240 ? 6.971   8.980   211.044 1.00 53.32  ? 240 PRO B CA    1 
ATOM   5577  C C     . PRO B  1 240 ? 5.925   7.886   210.865 1.00 55.80  ? 240 PRO B C     1 
ATOM   5578  O O     . PRO B  1 240 ? 5.561   7.206   211.824 1.00 55.67  ? 240 PRO B O     1 
ATOM   5579  C CB    . PRO B  1 240 ? 8.326   8.375   211.431 1.00 54.82  ? 240 PRO B CB    1 
ATOM   5580  C CG    . PRO B  1 240 ? 8.916   9.342   212.396 1.00 52.04  ? 240 PRO B CG    1 
ATOM   5581  C CD    . PRO B  1 240 ? 7.754   9.895   213.161 1.00 55.14  ? 240 PRO B CD    1 
ATOM   5582  N N     . VAL B  1 241 ? 5.441   7.736   209.638 1.00 59.35  ? 241 VAL B N     1 
ATOM   5583  C CA    . VAL B  1 241 ? 4.521   6.663   209.292 1.00 60.98  ? 241 VAL B CA    1 
ATOM   5584  C C     . VAL B  1 241 ? 4.994   6.032   207.986 1.00 61.11  ? 241 VAL B C     1 
ATOM   5585  O O     . VAL B  1 241 ? 5.601   6.711   207.158 1.00 66.29  ? 241 VAL B O     1 
ATOM   5586  C CB    . VAL B  1 241 ? 3.067   7.173   209.146 1.00 60.46  ? 241 VAL B CB    1 
ATOM   5587  C CG1   . VAL B  1 241 ? 2.519   7.620   210.495 1.00 59.80  ? 241 VAL B CG1   1 
ATOM   5588  C CG2   . VAL B  1 241 ? 2.989   8.302   208.127 1.00 60.80  ? 241 VAL B CG2   1 
ATOM   5589  N N     . PRO B  1 242 ? 4.734   4.728   207.797 1.00 62.75  ? 242 PRO B N     1 
ATOM   5590  C CA    . PRO B  1 242 ? 5.133   4.136   206.518 1.00 64.19  ? 242 PRO B CA    1 
ATOM   5591  C C     . PRO B  1 242 ? 4.234   4.644   205.396 1.00 65.69  ? 242 PRO B C     1 
ATOM   5592  O O     . PRO B  1 242 ? 3.144   5.145   205.672 1.00 65.50  ? 242 PRO B O     1 
ATOM   5593  C CB    . PRO B  1 242 ? 4.950   2.627   206.740 1.00 64.06  ? 242 PRO B CB    1 
ATOM   5594  C CG    . PRO B  1 242 ? 4.437   2.462   208.158 1.00 66.11  ? 242 PRO B CG    1 
ATOM   5595  C CD    . PRO B  1 242 ? 3.945   3.794   208.615 1.00 63.33  ? 242 PRO B CD    1 
ATOM   5596  N N     . GLU B  1 243 ? 4.682   4.524   204.151 1.00 66.87  ? 243 GLU B N     1 
ATOM   5597  C CA    . GLU B  1 243 ? 3.898   5.012   203.022 1.00 71.40  ? 243 GLU B CA    1 
ATOM   5598  C C     . GLU B  1 243 ? 2.689   4.115   202.773 1.00 73.05  ? 243 GLU B C     1 
ATOM   5599  O O     . GLU B  1 243 ? 1.742   4.508   202.094 1.00 76.12  ? 243 GLU B O     1 
ATOM   5600  C CB    . GLU B  1 243 ? 4.766   5.114   201.768 1.00 75.56  ? 243 GLU B CB    1 
ATOM   5601  C CG    . GLU B  1 243 ? 5.961   6.039   201.938 1.00 77.06  ? 243 GLU B CG    1 
ATOM   5602  C CD    . GLU B  1 243 ? 6.561   6.473   200.616 1.00 90.43  ? 243 GLU B CD    1 
ATOM   5603  O OE1   . GLU B  1 243 ? 6.916   5.595   199.801 1.00 99.85  ? 243 GLU B OE1   1 
ATOM   5604  O OE2   . GLU B  1 243 ? 6.675   7.697   200.391 1.00 90.28  ? 243 GLU B OE2   1 
ATOM   5605  N N     . LYS B  1 244 ? 2.726   2.909   203.330 1.00 69.75  ? 244 LYS B N     1 
ATOM   5606  C CA    . LYS B  1 244 ? 1.557   2.039   203.333 1.00 72.89  ? 244 LYS B CA    1 
ATOM   5607  C C     . LYS B  1 244 ? 1.291   1.470   204.718 1.00 69.72  ? 244 LYS B C     1 
ATOM   5608  O O     . LYS B  1 244 ? 2.192   0.942   205.367 1.00 68.45  ? 244 LYS B O     1 
ATOM   5609  C CB    . LYS B  1 244 ? 1.720   0.896   202.335 1.00 78.92  ? 244 LYS B CB    1 
ATOM   5610  C CG    . LYS B  1 244 ? 1.462   1.289   200.898 1.00 84.06  ? 244 LYS B CG    1 
ATOM   5611  C CD    . LYS B  1 244 ? 1.092   0.069   200.076 1.00 98.58  ? 244 LYS B CD    1 
ATOM   5612  C CE    . LYS B  1 244 ? 2.240   -0.922  200.001 1.00 97.05  ? 244 LYS B CE    1 
ATOM   5613  N NZ    . LYS B  1 244 ? 3.195   -0.561  198.922 1.00 95.93  ? 244 LYS B NZ    1 
ATOM   5614  N N     . VAL B  1 245 ? 0.045   1.583   205.165 1.00 67.84  ? 245 VAL B N     1 
ATOM   5615  C CA    . VAL B  1 245 ? -0.371  0.991   206.428 1.00 62.72  ? 245 VAL B CA    1 
ATOM   5616  C C     . VAL B  1 245 ? -1.508  0.013   206.178 1.00 64.42  ? 245 VAL B C     1 
ATOM   5617  O O     . VAL B  1 245 ? -2.069  -0.027  205.084 1.00 65.68  ? 245 VAL B O     1 
ATOM   5618  C CB    . VAL B  1 245 ? -0.820  2.056   207.441 1.00 63.77  ? 245 VAL B CB    1 
ATOM   5619  C CG1   . VAL B  1 245 ? 0.294   3.062   207.674 1.00 59.76  ? 245 VAL B CG1   1 
ATOM   5620  C CG2   . VAL B  1 245 ? -2.077  2.752   206.955 1.00 60.30  ? 245 VAL B CG2   1 
ATOM   5621  N N     . THR B  1 246 ? -1.845  -0.780  207.189 1.00 62.26  ? 246 THR B N     1 
ATOM   5622  C CA    . THR B  1 246 ? -2.896  -1.777  207.043 1.00 62.81  ? 246 THR B CA    1 
ATOM   5623  C C     . THR B  1 246 ? -3.981  -1.597  208.091 1.00 64.98  ? 246 THR B C     1 
ATOM   5624  O O     . THR B  1 246 ? -3.692  -1.457  209.278 1.00 66.22  ? 246 THR B O     1 
ATOM   5625  C CB    . THR B  1 246 ? -2.338  -3.205  207.152 1.00 68.00  ? 246 THR B CB    1 
ATOM   5626  O OG1   . THR B  1 246 ? -1.244  -3.360  206.240 1.00 66.21  ? 246 THR B OG1   1 
ATOM   5627  C CG2   . THR B  1 246 ? -3.421  -4.231  206.831 1.00 69.87  ? 246 THR B CG2   1 
ATOM   5628  N N     . VAL B  1 247 ? -5.233  -1.587  207.643 1.00 63.32  ? 247 VAL B N     1 
ATOM   5629  C CA    . VAL B  1 247 ? -6.371  -1.546  208.552 1.00 65.00  ? 247 VAL B CA    1 
ATOM   5630  C C     . VAL B  1 247 ? -7.407  -2.586  208.154 1.00 67.69  ? 247 VAL B C     1 
ATOM   5631  O O     . VAL B  1 247 ? -7.359  -3.137  207.054 1.00 69.00  ? 247 VAL B O     1 
ATOM   5632  C CB    . VAL B  1 247 ? -7.056  -0.165  208.578 1.00 68.18  ? 247 VAL B CB    1 
ATOM   5633  C CG1   . VAL B  1 247 ? -6.038  0.942   208.792 1.00 69.35  ? 247 VAL B CG1   1 
ATOM   5634  C CG2   . VAL B  1 247 ? -7.832  0.064   207.299 1.00 63.53  ? 247 VAL B CG2   1 
ATOM   5635  N N     . PHE B  1 248 ? -8.337  -2.858  209.061 1.00 64.66  ? 248 PHE B N     1 
ATOM   5636  C CA    . PHE B  1 248 ? -9.517  -3.635  208.722 1.00 66.79  ? 248 PHE B CA    1 
ATOM   5637  C C     . PHE B  1 248 ? -10.687 -3.264  209.619 1.00 72.45  ? 248 PHE B C     1 
ATOM   5638  O O     . PHE B  1 248 ? -10.520 -3.000  210.808 1.00 69.23  ? 248 PHE B O     1 
ATOM   5639  C CB    . PHE B  1 248 ? -9.241  -5.141  208.808 1.00 70.29  ? 248 PHE B CB    1 
ATOM   5640  C CG    . PHE B  1 248 ? -8.631  -5.586  210.108 1.00 69.02  ? 248 PHE B CG    1 
ATOM   5641  C CD1   . PHE B  1 248 ? -9.425  -5.859  211.212 1.00 68.05  ? 248 PHE B CD1   1 
ATOM   5642  C CD2   . PHE B  1 248 ? -7.261  -5.758  210.217 1.00 67.07  ? 248 PHE B CD2   1 
ATOM   5643  C CE1   . PHE B  1 248 ? -8.862  -6.276  212.404 1.00 67.82  ? 248 PHE B CE1   1 
ATOM   5644  C CE2   . PHE B  1 248 ? -6.693  -6.177  211.406 1.00 64.91  ? 248 PHE B CE2   1 
ATOM   5645  C CZ    . PHE B  1 248 ? -7.494  -6.436  212.500 1.00 64.28  ? 248 PHE B CZ    1 
ATOM   5646  N N     . ARG B  1 249 ? -11.874 -3.235  209.028 1.00 75.59  ? 249 ARG B N     1 
ATOM   5647  C CA    . ARG B  1 249 ? -13.105 -3.043  209.776 1.00 76.74  ? 249 ARG B CA    1 
ATOM   5648  C C     . ARG B  1 249 ? -14.003 -4.249  209.542 1.00 80.77  ? 249 ARG B C     1 
ATOM   5649  O O     . ARG B  1 249 ? -14.647 -4.362  208.500 1.00 86.77  ? 249 ARG B O     1 
ATOM   5650  C CB    . ARG B  1 249 ? -13.801 -1.751  209.356 1.00 75.01  ? 249 ARG B CB    1 
ATOM   5651  C CG    . ARG B  1 249 ? -15.208 -1.586  209.893 1.00 79.62  ? 249 ARG B CG    1 
ATOM   5652  C CD    . ARG B  1 249 ? -15.891 -0.420  209.206 1.00 87.67  ? 249 ARG B CD    1 
ATOM   5653  N NE    . ARG B  1 249 ? -15.248 0.850   209.528 1.00 88.32  ? 249 ARG B NE    1 
ATOM   5654  C CZ    . ARG B  1 249 ? -15.180 1.887   208.699 1.00 89.62  ? 249 ARG B CZ    1 
ATOM   5655  N NH1   . ARG B  1 249 ? -14.578 3.007   209.080 1.00 83.20  ? 249 ARG B NH1   1 
ATOM   5656  N NH2   . ARG B  1 249 ? -15.709 1.804   207.486 1.00 105.63 ? 249 ARG B NH2   1 
ATOM   5657  N N     . VAL B  1 250 ? -14.026 -5.159  210.508 1.00 78.80  ? 250 VAL B N     1 
ATOM   5658  C CA    . VAL B  1 250 ? -14.765 -6.404  210.359 1.00 73.24  ? 250 VAL B CA    1 
ATOM   5659  C C     . VAL B  1 250 ? -15.804 -6.560  211.456 1.00 74.29  ? 250 VAL B C     1 
ATOM   5660  O O     . VAL B  1 250 ? -15.473 -6.628  212.640 1.00 74.14  ? 250 VAL B O     1 
ATOM   5661  C CB    . VAL B  1 250 ? -13.818 -7.616  210.362 1.00 72.44  ? 250 VAL B CB    1 
ATOM   5662  C CG1   . VAL B  1 250 ? -14.609 -8.912  210.451 1.00 77.59  ? 250 VAL B CG1   1 
ATOM   5663  C CG2   . VAL B  1 250 ? -12.962 -7.594  209.112 1.00 75.26  ? 250 VAL B CG2   1 
ATOM   5664  N N     . THR B  1 251 ? -17.066 -6.613  211.050 1.00 73.84  ? 251 THR B N     1 
ATOM   5665  C CA    . THR B  1 251 ? -18.162 -6.705  212.000 1.00 73.76  ? 251 THR B CA    1 
ATOM   5666  C C     . THR B  1 251 ? -18.639 -8.138  212.159 1.00 73.68  ? 251 THR B C     1 
ATOM   5667  O O     . THR B  1 251 ? -18.794 -8.865  211.179 1.00 78.39  ? 251 THR B O     1 
ATOM   5668  C CB    . THR B  1 251 ? -19.352 -5.830  211.577 1.00 72.03  ? 251 THR B CB    1 
ATOM   5669  O OG1   . THR B  1 251 ? -18.868 -4.615  210.994 1.00 75.97  ? 251 THR B OG1   1 
ATOM   5670  C CG2   . THR B  1 251 ? -20.229 -5.506  212.781 1.00 67.73  ? 251 THR B CG2   1 
ATOM   5671  N N     . LYS B  1 252 ? -18.867 -8.538  213.405 1.00 71.11  ? 252 LYS B N     1 
ATOM   5672  C CA    . LYS B  1 252 ? -19.382 -9.867  213.695 1.00 72.59  ? 252 LYS B CA    1 
ATOM   5673  C C     . LYS B  1 252 ? -20.718 -9.831  214.403 1.00 71.19  ? 252 LYS B C     1 
ATOM   5674  O O     . LYS B  1 252 ? -20.807 -9.457  215.571 1.00 68.47  ? 252 LYS B O     1 
ATOM   5675  C CB    . LYS B  1 252 ? -18.403 -10.655 214.551 1.00 70.11  ? 252 LYS B CB    1 
ATOM   5676  C CG    . LYS B  1 252 ? -17.152 -11.029 213.835 1.00 79.09  ? 252 LYS B CG    1 
ATOM   5677  C CD    . LYS B  1 252 ? -16.463 -12.150 214.550 1.00 72.59  ? 252 LYS B CD    1 
ATOM   5678  C CE    . LYS B  1 252 ? -15.383 -12.694 213.677 1.00 84.46  ? 252 LYS B CE    1 
ATOM   5679  N NZ    . LYS B  1 252 ? -14.476 -11.589 213.268 1.00 89.53  ? 252 LYS B NZ    1 
ATOM   5680  N N     . ASN B  1 253 ? -21.756 -10.242 213.694 1.00 70.53  ? 253 ASN B N     1 
ATOM   5681  C CA    . ASN B  1 253 ? -23.051 -10.436 214.312 1.00 67.85  ? 253 ASN B CA    1 
ATOM   5682  C C     . ASN B  1 253 ? -23.130 -11.836 214.912 1.00 66.99  ? 253 ASN B C     1 
ATOM   5683  O O     . ASN B  1 253 ? -23.361 -12.812 214.198 1.00 70.53  ? 253 ASN B O     1 
ATOM   5684  C CB    . ASN B  1 253 ? -24.153 -10.199 213.286 1.00 62.67  ? 253 ASN B CB    1 
ATOM   5685  C CG    . ASN B  1 253 ? -24.061 -8.824  212.658 1.00 67.72  ? 253 ASN B CG    1 
ATOM   5686  O OD1   . ASN B  1 253 ? -23.438 -8.643  211.611 1.00 70.98  ? 253 ASN B OD1   1 
ATOM   5687  N ND2   . ASN B  1 253 ? -24.668 -7.841  213.308 1.00 71.96  ? 253 ASN B ND2   1 
ATOM   5688  N N     . VAL B  1 254 ? -22.898 -11.930 216.221 1.00 67.14  ? 254 VAL B N     1 
ATOM   5689  C CA    . VAL B  1 254 ? -22.846 -13.218 216.920 1.00 65.53  ? 254 VAL B CA    1 
ATOM   5690  C C     . VAL B  1 254 ? -23.673 -13.195 218.208 1.00 69.28  ? 254 VAL B C     1 
ATOM   5691  O O     . VAL B  1 254 ? -24.230 -12.164 218.575 1.00 72.94  ? 254 VAL B O     1 
ATOM   5692  C CB    . VAL B  1 254 ? -21.394 -13.620 217.276 1.00 69.46  ? 254 VAL B CB    1 
ATOM   5693  C CG1   . VAL B  1 254 ? -20.475 -13.434 216.081 1.00 69.15  ? 254 VAL B CG1   1 
ATOM   5694  C CG2   . VAL B  1 254 ? -20.883 -12.820 218.463 1.00 70.46  ? 254 VAL B CG2   1 
ATOM   5695  N N     . ALA B  1 255 ? -23.748 -14.340 218.884 1.00 72.82  ? 255 ALA B N     1 
ATOM   5696  C CA    . ALA B  1 255 ? -24.439 -14.439 220.169 1.00 76.42  ? 255 ALA B CA    1 
ATOM   5697  C C     . ALA B  1 255 ? -23.614 -13.838 221.297 1.00 78.91  ? 255 ALA B C     1 
ATOM   5698  O O     . ALA B  1 255 ? -22.390 -13.762 221.202 1.00 77.56  ? 255 ALA B O     1 
ATOM   5699  C CB    . ALA B  1 255 ? -24.763 -15.885 220.486 1.00 83.51  ? 255 ALA B CB    1 
ATOM   5700  N N     . ILE B  1 256 ? -24.290 -13.441 222.374 1.00 80.46  ? 256 ILE B N     1 
ATOM   5701  C CA    . ILE B  1 256 ? -23.633 -12.949 223.585 1.00 83.33  ? 256 ILE B CA    1 
ATOM   5702  C C     . ILE B  1 256 ? -22.613 -13.956 224.112 1.00 84.81  ? 256 ILE B C     1 
ATOM   5703  O O     . ILE B  1 256 ? -21.611 -13.579 224.717 1.00 80.35  ? 256 ILE B O     1 
ATOM   5704  C CB    . ILE B  1 256 ? -24.656 -12.646 224.701 1.00 82.50  ? 256 ILE B CB    1 
ATOM   5705  C CG1   . ILE B  1 256 ? -23.997 -11.854 225.832 1.00 86.86  ? 256 ILE B CG1   1 
ATOM   5706  C CG2   . ILE B  1 256 ? -25.266 -13.926 225.262 1.00 89.25  ? 256 ILE B CG2   1 
ATOM   5707  C CD1   . ILE B  1 256 ? -24.919 -11.623 226.998 1.00 86.99  ? 256 ILE B CD1   1 
ATOM   5708  N N     . ASP B  1 257 ? -22.879 -15.236 223.864 1.00 87.78  ? 257 ASP B N     1 
ATOM   5709  C CA    . ASP B  1 257 ? -22.045 -16.307 224.378 1.00 87.40  ? 257 ASP B CA    1 
ATOM   5710  C C     . ASP B  1 257 ? -20.721 -16.337 223.630 1.00 82.27  ? 257 ASP B C     1 
ATOM   5711  O O     . ASP B  1 257 ? -19.660 -16.488 224.232 1.00 78.05  ? 257 ASP B O     1 
ATOM   5712  C CB    . ASP B  1 257 ? -22.769 -17.650 224.264 1.00 92.25  ? 257 ASP B CB    1 
ATOM   5713  C CG    . ASP B  1 257 ? -24.166 -17.611 224.863 1.00 102.82 ? 257 ASP B CG    1 
ATOM   5714  O OD1   . ASP B  1 257 ? -24.289 -17.786 226.094 1.00 108.93 ? 257 ASP B OD1   1 
ATOM   5715  O OD2   . ASP B  1 257 ? -25.141 -17.411 224.108 1.00 120.30 ? 257 ASP B OD2   1 
ATOM   5716  N N     . GLU B  1 258 ? -20.787 -16.188 222.311 1.00 78.42  ? 258 GLU B N     1 
ATOM   5717  C CA    . GLU B  1 258 ? -19.570 -16.088 221.520 1.00 75.26  ? 258 GLU B CA    1 
ATOM   5718  C C     . GLU B  1 258 ? -18.918 -14.729 221.750 1.00 77.91  ? 258 GLU B C     1 
ATOM   5719  O O     . GLU B  1 258 ? -17.699 -14.636 221.884 1.00 74.78  ? 258 GLU B O     1 
ATOM   5720  C CB    . GLU B  1 258 ? -19.852 -16.298 220.033 1.00 74.42  ? 258 GLU B CB    1 
ATOM   5721  C CG    . GLU B  1 258 ? -18.591 -16.406 219.184 1.00 76.75  ? 258 GLU B CG    1 
ATOM   5722  C CD    . GLU B  1 258 ? -18.886 -16.608 217.710 1.00 77.85  ? 258 GLU B CD    1 
ATOM   5723  O OE1   . GLU B  1 258 ? -20.077 -16.697 217.349 1.00 78.49  ? 258 GLU B OE1   1 
ATOM   5724  O OE2   . GLU B  1 258 ? -17.927 -16.681 216.911 1.00 73.18  ? 258 GLU B OE2   1 
ATOM   5725  N N     . ALA B  1 259 ? -19.740 -13.684 221.806 1.00 75.18  ? 259 ALA B N     1 
ATOM   5726  C CA    . ALA B  1 259 ? -19.255 -12.318 221.999 1.00 74.52  ? 259 ALA B CA    1 
ATOM   5727  C C     . ALA B  1 259 ? -18.422 -12.191 223.267 1.00 74.11  ? 259 ALA B C     1 
ATOM   5728  O O     . ALA B  1 259 ? -17.330 -11.624 223.255 1.00 71.58  ? 259 ALA B O     1 
ATOM   5729  C CB    . ALA B  1 259 ? -20.422 -11.344 222.044 1.00 68.75  ? 259 ALA B CB    1 
ATOM   5730  N N     . THR B  1 260 ? -18.954 -12.735 224.354 1.00 73.69  ? 260 THR B N     1 
ATOM   5731  C CA    . THR B  1 260 ? -18.324 -12.663 225.665 1.00 72.91  ? 260 THR B CA    1 
ATOM   5732  C C     . THR B  1 260 ? -16.931 -13.284 225.683 1.00 75.81  ? 260 THR B C     1 
ATOM   5733  O O     . THR B  1 260 ? -15.991 -12.700 226.226 1.00 72.98  ? 260 THR B O     1 
ATOM   5734  C CB    . THR B  1 260 ? -19.206 -13.351 226.715 1.00 76.16  ? 260 THR B CB    1 
ATOM   5735  O OG1   . THR B  1 260 ? -20.407 -12.589 226.895 1.00 74.47  ? 260 THR B OG1   1 
ATOM   5736  C CG2   . THR B  1 260 ? -18.481 -13.468 228.027 1.00 72.62  ? 260 THR B CG2   1 
ATOM   5737  N N     . SER B  1 261 ? -16.800 -14.464 225.083 1.00 75.19  ? 261 SER B N     1 
ATOM   5738  C CA    . SER B  1 261 ? -15.508 -15.140 225.012 1.00 79.24  ? 261 SER B CA    1 
ATOM   5739  C C     . SER B  1 261 ? -14.569 -14.401 224.064 1.00 74.66  ? 261 SER B C     1 
ATOM   5740  O O     . SER B  1 261 ? -13.350 -14.477 224.206 1.00 74.21  ? 261 SER B O     1 
ATOM   5741  C CB    . SER B  1 261 ? -15.669 -16.595 224.562 1.00 78.56  ? 261 SER B CB    1 
ATOM   5742  O OG    . SER B  1 261 ? -15.480 -16.721 223.163 1.00 79.17  ? 261 SER B OG    1 
ATOM   5743  N N     . LEU B  1 262 ? -15.143 -13.691 223.096 1.00 70.24  ? 262 LEU B N     1 
ATOM   5744  C CA    . LEU B  1 262 ? -14.355 -12.888 222.164 1.00 72.27  ? 262 LEU B CA    1 
ATOM   5745  C C     . LEU B  1 262 ? -13.728 -11.688 222.860 1.00 69.11  ? 262 LEU B C     1 
ATOM   5746  O O     . LEU B  1 262 ? -12.540 -11.416 222.691 1.00 67.82  ? 262 LEU B O     1 
ATOM   5747  C CB    . LEU B  1 262 ? -15.216 -12.416 220.992 1.00 69.51  ? 262 LEU B CB    1 
ATOM   5748  C CG    . LEU B  1 262 ? -15.346 -13.345 219.786 1.00 70.56  ? 262 LEU B CG    1 
ATOM   5749  C CD1   . LEU B  1 262 ? -16.360 -12.789 218.799 1.00 65.65  ? 262 LEU B CD1   1 
ATOM   5750  C CD2   . LEU B  1 262 ? -13.996 -13.537 219.115 1.00 64.61  ? 262 LEU B CD2   1 
ATOM   5751  N N     . LEU B  1 263 ? -14.537 -10.971 223.636 1.00 69.97  ? 263 LEU B N     1 
ATOM   5752  C CA    . LEU B  1 263 ? -14.059 -9.818  224.392 1.00 69.15  ? 263 LEU B CA    1 
ATOM   5753  C C     . LEU B  1 263 ? -12.999 -10.222 225.412 1.00 71.96  ? 263 LEU B C     1 
ATOM   5754  O O     . LEU B  1 263 ? -12.013 -9.508  225.606 1.00 66.45  ? 263 LEU B O     1 
ATOM   5755  C CB    . LEU B  1 263 ? -15.220 -9.113  225.103 1.00 71.79  ? 263 LEU B CB    1 
ATOM   5756  C CG    . LEU B  1 263 ? -16.296 -8.473  224.219 1.00 68.66  ? 263 LEU B CG    1 
ATOM   5757  C CD1   . LEU B  1 263 ? -17.234 -7.591  225.042 1.00 71.57  ? 263 LEU B CD1   1 
ATOM   5758  C CD2   . LEU B  1 263 ? -15.660 -7.687  223.083 1.00 66.79  ? 263 LEU B CD2   1 
ATOM   5759  N N     . HIS B  1 264 ? -13.200 -11.371 226.053 1.00 71.46  ? 264 HIS B N     1 
ATOM   5760  C CA    . HIS B  1 264 ? -12.296 -11.818 227.109 1.00 68.13  ? 264 HIS B CA    1 
ATOM   5761  C C     . HIS B  1 264 ? -10.908 -12.135 226.568 1.00 69.06  ? 264 HIS B C     1 
ATOM   5762  O O     . HIS B  1 264 ? -9.913  -11.928 227.256 1.00 66.62  ? 264 HIS B O     1 
ATOM   5763  C CB    . HIS B  1 264 ? -12.856 -13.041 227.835 1.00 71.97  ? 264 HIS B CB    1 
ATOM   5764  C CG    . HIS B  1 264 ? -12.154 -13.341 229.124 1.00 73.05  ? 264 HIS B CG    1 
ATOM   5765  N ND1   . HIS B  1 264 ? -11.046 -14.158 229.200 1.00 69.03  ? 264 HIS B ND1   1 
ATOM   5766  C CD2   . HIS B  1 264 ? -12.393 -12.917 230.388 1.00 74.03  ? 264 HIS B CD2   1 
ATOM   5767  C CE1   . HIS B  1 264 ? -10.638 -14.230 230.454 1.00 70.58  ? 264 HIS B CE1   1 
ATOM   5768  N NE2   . HIS B  1 264 ? -11.439 -13.486 231.196 1.00 72.76  ? 264 HIS B NE2   1 
ATOM   5769  N N     . LYS B  1 265 ? -10.834 -12.636 225.340 1.00 65.92  ? 265 LYS B N     1 
ATOM   5770  C CA    . LYS B  1 265 ? -9.531  -12.868 224.732 1.00 68.46  ? 265 LYS B CA    1 
ATOM   5771  C C     . LYS B  1 265 ? -8.974  -11.563 224.181 1.00 65.08  ? 265 LYS B C     1 
ATOM   5772  O O     . LYS B  1 265 ? -7.778  -11.293 224.304 1.00 66.50  ? 265 LYS B O     1 
ATOM   5773  C CB    . LYS B  1 265 ? -9.597  -13.916 223.621 1.00 68.67  ? 265 LYS B CB    1 
ATOM   5774  C CG    . LYS B  1 265 ? -8.216  -14.428 223.244 1.00 67.24  ? 265 LYS B CG    1 
ATOM   5775  C CD    . LYS B  1 265 ? -8.203  -15.224 221.955 1.00 70.69  ? 265 LYS B CD    1 
ATOM   5776  C CE    . LYS B  1 265 ? -6.779  -15.653 221.629 1.00 72.06  ? 265 LYS B CE    1 
ATOM   5777  N NZ    . LYS B  1 265 ? -6.682  -16.514 220.420 1.00 74.96  ? 265 LYS B NZ    1 
ATOM   5778  N N     . TRP B  1 266 ? -9.846  -10.756 223.581 1.00 64.24  ? 266 TRP B N     1 
ATOM   5779  C CA    . TRP B  1 266 ? -9.434  -9.502  222.955 1.00 64.31  ? 266 TRP B CA    1 
ATOM   5780  C C     . TRP B  1 266 ? -8.674  -8.577  223.902 1.00 57.95  ? 266 TRP B C     1 
ATOM   5781  O O     . TRP B  1 266 ? -7.709  -7.931  223.494 1.00 58.62  ? 266 TRP B O     1 
ATOM   5782  C CB    . TRP B  1 266 ? -10.647 -8.753  222.394 1.00 64.98  ? 266 TRP B CB    1 
ATOM   5783  C CG    . TRP B  1 266 ? -10.323 -7.327  222.057 1.00 63.69  ? 266 TRP B CG    1 
ATOM   5784  C CD1   . TRP B  1 266 ? -9.806  -6.859  220.886 1.00 60.14  ? 266 TRP B CD1   1 
ATOM   5785  C CD2   . TRP B  1 266 ? -10.472 -6.187  222.914 1.00 58.32  ? 266 TRP B CD2   1 
ATOM   5786  N NE1   . TRP B  1 266 ? -9.629  -5.499  220.956 1.00 56.63  ? 266 TRP B NE1   1 
ATOM   5787  C CE2   . TRP B  1 266 ? -10.030 -5.062  222.191 1.00 56.67  ? 266 TRP B CE2   1 
ATOM   5788  C CE3   . TRP B  1 266 ? -10.938 -6.009  224.220 1.00 58.70  ? 266 TRP B CE3   1 
ATOM   5789  C CZ2   . TRP B  1 266 ? -10.042 -3.778  222.729 1.00 53.65  ? 266 TRP B CZ2   1 
ATOM   5790  C CZ3   . TRP B  1 266 ? -10.946 -4.734  224.754 1.00 56.07  ? 266 TRP B CZ3   1 
ATOM   5791  C CH2   . TRP B  1 266 ? -10.498 -3.636  224.010 1.00 54.36  ? 266 TRP B CH2   1 
ATOM   5792  N N     . GLN B  1 267 ? -9.112  -8.511  225.157 1.00 59.45  ? 267 GLN B N     1 
ATOM   5793  C CA    . GLN B  1 267 ? -8.514  -7.596  226.125 1.00 61.26  ? 267 GLN B CA    1 
ATOM   5794  C C     . GLN B  1 267 ? -7.034  -7.903  226.344 1.00 63.74  ? 267 GLN B C     1 
ATOM   5795  O O     . GLN B  1 267 ? -6.256  -7.025  226.718 1.00 60.99  ? 267 GLN B O     1 
ATOM   5796  C CB    . GLN B  1 267 ? -9.269  -7.648  227.459 1.00 63.43  ? 267 GLN B CB    1 
ATOM   5797  C CG    . GLN B  1 267 ? -8.972  -8.870  228.313 1.00 63.12  ? 267 GLN B CG    1 
ATOM   5798  C CD    . GLN B  1 267 ? -9.708  -8.853  229.638 1.00 65.90  ? 267 GLN B CD    1 
ATOM   5799  O OE1   . GLN B  1 267 ? -9.701  -7.853  230.355 1.00 68.23  ? 267 GLN B OE1   1 
ATOM   5800  N NE2   . GLN B  1 267 ? -10.356 -9.965  229.967 1.00 70.82  ? 267 GLN B NE2   1 
ATOM   5801  N N     . PHE B  1 268 ? -6.650  -9.152  226.097 1.00 64.44  ? 268 PHE B N     1 
ATOM   5802  C CA    . PHE B  1 268 ? -5.257  -9.555  226.213 1.00 61.80  ? 268 PHE B CA    1 
ATOM   5803  C C     . PHE B  1 268 ? -4.521  -9.322  224.899 1.00 62.30  ? 268 PHE B C     1 
ATOM   5804  O O     . PHE B  1 268 ? -3.363  -8.908  224.895 1.00 64.91  ? 268 PHE B O     1 
ATOM   5805  C CB    . PHE B  1 268 ? -5.151  -11.023 226.629 1.00 62.18  ? 268 PHE B CB    1 
ATOM   5806  C CG    . PHE B  1 268 ? -5.816  -11.332 227.940 1.00 59.84  ? 268 PHE B CG    1 
ATOM   5807  C CD1   . PHE B  1 268 ? -5.263  -10.897 229.134 1.00 59.91  ? 268 PHE B CD1   1 
ATOM   5808  C CD2   . PHE B  1 268 ? -6.987  -12.067 227.980 1.00 60.16  ? 268 PHE B CD2   1 
ATOM   5809  C CE1   . PHE B  1 268 ? -5.873  -11.184 230.342 1.00 58.63  ? 268 PHE B CE1   1 
ATOM   5810  C CE2   . PHE B  1 268 ? -7.601  -12.358 229.184 1.00 60.28  ? 268 PHE B CE2   1 
ATOM   5811  C CZ    . PHE B  1 268 ? -7.044  -11.916 230.365 1.00 60.01  ? 268 PHE B CZ    1 
ATOM   5812  N N     . VAL B  1 269 ? -5.201  -9.585  223.787 1.00 55.07  ? 269 VAL B N     1 
ATOM   5813  C CA    . VAL B  1 269 ? -4.634  -9.338  222.466 1.00 56.45  ? 269 VAL B CA    1 
ATOM   5814  C C     . VAL B  1 269 ? -4.258  -7.869  222.301 1.00 61.44  ? 269 VAL B C     1 
ATOM   5815  O O     . VAL B  1 269 ? -3.143  -7.545  221.894 1.00 63.65  ? 269 VAL B O     1 
ATOM   5816  C CB    . VAL B  1 269 ? -5.614  -9.736  221.340 1.00 59.88  ? 269 VAL B CB    1 
ATOM   5817  C CG1   . VAL B  1 269 ? -4.990  -9.468  219.977 1.00 56.34  ? 269 VAL B CG1   1 
ATOM   5818  C CG2   . VAL B  1 269 ? -6.032  -11.199 221.476 1.00 60.35  ? 269 VAL B CG2   1 
ATOM   5819  N N     . ALA B  1 270 ? -5.194  -6.987  222.638 1.00 59.06  ? 270 ALA B N     1 
ATOM   5820  C CA    . ALA B  1 270 ? -5.014  -5.549  222.470 1.00 61.76  ? 270 ALA B CA    1 
ATOM   5821  C C     . ALA B  1 270 ? -3.807  -5.014  223.236 1.00 61.63  ? 270 ALA B C     1 
ATOM   5822  O O     . ALA B  1 270 ? -3.109  -4.121  222.759 1.00 60.26  ? 270 ALA B O     1 
ATOM   5823  C CB    . ALA B  1 270 ? -6.276  -4.813  222.903 1.00 55.35  ? 270 ALA B CB    1 
ATOM   5824  N N     . GLU B  1 271 ? -3.562  -5.570  224.417 1.00 62.18  ? 271 GLU B N     1 
ATOM   5825  C CA    . GLU B  1 271 ? -2.503  -5.077  225.290 1.00 69.34  ? 271 GLU B CA    1 
ATOM   5826  C C     . GLU B  1 271 ? -1.146  -5.699  224.970 1.00 68.52  ? 271 GLU B C     1 
ATOM   5827  O O     . GLU B  1 271 ? -0.106  -5.058  225.132 1.00 71.49  ? 271 GLU B O     1 
ATOM   5828  C CB    . GLU B  1 271 ? -2.860  -5.346  226.755 1.00 75.66  ? 271 GLU B CB    1 
ATOM   5829  C CG    . GLU B  1 271 ? -1.881  -4.756  227.758 1.00 85.62  ? 271 GLU B CG    1 
ATOM   5830  C CD    . GLU B  1 271 ? -2.219  -5.130  229.187 1.00 96.07  ? 271 GLU B CD    1 
ATOM   5831  O OE1   . GLU B  1 271 ? -3.267  -5.777  229.398 1.00 92.23  ? 271 GLU B OE1   1 
ATOM   5832  O OE2   . GLU B  1 271 ? -1.442  -4.777  230.099 1.00 103.77 ? 271 GLU B OE2   1 
ATOM   5833  N N     . GLU B  1 272 ? -1.161  -6.947  224.516 1.00 68.12  ? 272 GLU B N     1 
ATOM   5834  C CA    . GLU B  1 272 ? 0.079   -7.679  224.276 1.00 68.43  ? 272 GLU B CA    1 
ATOM   5835  C C     . GLU B  1 272 ? 0.564   -7.554  222.836 1.00 65.80  ? 272 GLU B C     1 
ATOM   5836  O O     . GLU B  1 272 ? 1.645   -8.034  222.498 1.00 68.99  ? 272 GLU B O     1 
ATOM   5837  C CB    . GLU B  1 272 ? -0.094  -9.153  224.647 1.00 68.75  ? 272 GLU B CB    1 
ATOM   5838  C CG    . GLU B  1 272 ? -0.120  -9.397  226.147 1.00 73.43  ? 272 GLU B CG    1 
ATOM   5839  C CD    . GLU B  1 272 ? -1.241  -10.323 226.568 1.00 78.54  ? 272 GLU B CD    1 
ATOM   5840  O OE1   . GLU B  1 272 ? -1.667  -11.157 225.742 1.00 77.92  ? 272 GLU B OE1   1 
ATOM   5841  O OE2   . GLU B  1 272 ? -1.704  -10.206 227.722 1.00 76.90  ? 272 GLU B OE2   1 
ATOM   5842  N N     . LEU B  1 273 ? -0.234  -6.911  221.989 1.00 62.93  ? 273 LEU B N     1 
ATOM   5843  C CA    . LEU B  1 273 ? 0.213   -6.575  220.643 1.00 60.66  ? 273 LEU B CA    1 
ATOM   5844  C C     . LEU B  1 273 ? 1.417   -5.645  220.717 1.00 61.23  ? 273 LEU B C     1 
ATOM   5845  O O     . LEU B  1 273 ? 1.522   -4.832  221.637 1.00 62.47  ? 273 LEU B O     1 
ATOM   5846  C CB    . LEU B  1 273 ? -0.910  -5.915  219.839 1.00 59.22  ? 273 LEU B CB    1 
ATOM   5847  C CG    . LEU B  1 273 ? -1.906  -6.813  219.103 1.00 59.94  ? 273 LEU B CG    1 
ATOM   5848  C CD1   . LEU B  1 273 ? -3.163  -6.038  218.738 1.00 59.13  ? 273 LEU B CD1   1 
ATOM   5849  C CD2   . LEU B  1 273 ? -1.270  -7.409  217.858 1.00 57.09  ? 273 LEU B CD2   1 
ATOM   5850  N N     . GLU B  1 274 ? 2.326   -5.763  219.754 1.00 62.07  ? 274 GLU B N     1 
ATOM   5851  C CA    . GLU B  1 274 ? 3.416   -4.802  219.636 1.00 67.03  ? 274 GLU B CA    1 
ATOM   5852  C C     . GLU B  1 274 ? 2.832   -3.415  219.381 1.00 63.93  ? 274 GLU B C     1 
ATOM   5853  O O     . GLU B  1 274 ? 1.705   -3.292  218.901 1.00 60.41  ? 274 GLU B O     1 
ATOM   5854  C CB    . GLU B  1 274 ? 4.383   -5.199  218.519 1.00 66.35  ? 274 GLU B CB    1 
ATOM   5855  C CG    . GLU B  1 274 ? 5.325   -6.336  218.888 1.00 76.08  ? 274 GLU B CG    1 
ATOM   5856  C CD    . GLU B  1 274 ? 6.206   -6.763  217.730 1.00 89.62  ? 274 GLU B CD    1 
ATOM   5857  O OE1   . GLU B  1 274 ? 6.044   -6.208  216.623 1.00 82.54  ? 274 GLU B OE1   1 
ATOM   5858  O OE2   . GLU B  1 274 ? 7.060   -7.655  217.927 1.00 97.77  ? 274 GLU B OE2   1 
ATOM   5859  N N     . GLU B  1 275 ? 3.597   -2.376  219.702 1.00 62.31  ? 275 GLU B N     1 
ATOM   5860  C CA    . GLU B  1 275 ? 3.105   -1.003  219.614 1.00 59.05  ? 275 GLU B CA    1 
ATOM   5861  C C     . GLU B  1 275 ? 2.736   -0.601  218.185 1.00 56.71  ? 275 GLU B C     1 
ATOM   5862  O O     . GLU B  1 275 ? 2.030   0.382   217.972 1.00 53.31  ? 275 GLU B O     1 
ATOM   5863  C CB    . GLU B  1 275 ? 4.145   -0.035  220.175 1.00 51.51  ? 275 GLU B CB    1 
ATOM   5864  C CG    . GLU B  1 275 ? 5.471   -0.078  219.450 1.00 54.92  ? 275 GLU B CG    1 
ATOM   5865  C CD    . GLU B  1 275 ? 6.494   0.862   220.052 1.00 58.25  ? 275 GLU B CD    1 
ATOM   5866  O OE1   . GLU B  1 275 ? 6.506   1.021   221.292 1.00 57.13  ? 275 GLU B OE1   1 
ATOM   5867  O OE2   . GLU B  1 275 ? 7.285   1.444   219.282 1.00 60.98  ? 275 GLU B OE2   1 
ATOM   5868  N N     . ASP B  1 276 ? 3.217   -1.369  217.213 1.00 58.13  ? 276 ASP B N     1 
ATOM   5869  C CA    . ASP B  1 276 ? 2.899   -1.126  215.810 1.00 55.23  ? 276 ASP B CA    1 
ATOM   5870  C C     . ASP B  1 276 ? 1.501   -1.621  215.449 1.00 56.70  ? 276 ASP B C     1 
ATOM   5871  O O     . ASP B  1 276 ? 1.061   -1.482  214.308 1.00 55.25  ? 276 ASP B O     1 
ATOM   5872  C CB    . ASP B  1 276 ? 3.935   -1.793  214.903 1.00 56.92  ? 276 ASP B CB    1 
ATOM   5873  C CG    . ASP B  1 276 ? 5.261   -1.064  214.903 1.00 63.97  ? 276 ASP B CG    1 
ATOM   5874  O OD1   . ASP B  1 276 ? 5.291   0.106   215.337 1.00 65.55  ? 276 ASP B OD1   1 
ATOM   5875  O OD2   . ASP B  1 276 ? 6.269   -1.650  214.458 1.00 69.58  ? 276 ASP B OD2   1 
ATOM   5876  N N     . PHE B  1 277 ? 0.806   -2.201  216.421 1.00 53.91  ? 277 PHE B N     1 
ATOM   5877  C CA    . PHE B  1 277 ? -0.537  -2.722  216.193 1.00 56.40  ? 277 PHE B CA    1 
ATOM   5878  C C     . PHE B  1 277 ? -1.557  -2.091  217.131 1.00 55.62  ? 277 PHE B C     1 
ATOM   5879  O O     . PHE B  1 277 ? -1.249  -1.774  218.280 1.00 58.28  ? 277 PHE B O     1 
ATOM   5880  C CB    . PHE B  1 277 ? -0.566  -4.241  216.369 1.00 56.64  ? 277 PHE B CB    1 
ATOM   5881  C CG    . PHE B  1 277 ? 0.218   -4.998  215.334 1.00 58.65  ? 277 PHE B CG    1 
ATOM   5882  C CD1   . PHE B  1 277 ? -0.401  -5.486  214.193 1.00 60.88  ? 277 PHE B CD1   1 
ATOM   5883  C CD2   . PHE B  1 277 ? 1.570   -5.237  215.512 1.00 61.45  ? 277 PHE B CD2   1 
ATOM   5884  C CE1   . PHE B  1 277 ? 0.320   -6.191  213.243 1.00 62.03  ? 277 PHE B CE1   1 
ATOM   5885  C CE2   . PHE B  1 277 ? 2.295   -5.939  214.569 1.00 62.54  ? 277 PHE B CE2   1 
ATOM   5886  C CZ    . PHE B  1 277 ? 1.670   -6.417  213.433 1.00 61.52  ? 277 PHE B CZ    1 
ATOM   5887  N N     . THR B  1 278 ? -2.775  -1.914  216.631 1.00 51.41  ? 278 THR B N     1 
ATOM   5888  C CA    . THR B  1 278 ? -3.893  -1.496  217.465 1.00 55.08  ? 278 THR B CA    1 
ATOM   5889  C C     . THR B  1 278 ? -5.139  -2.291  217.087 1.00 52.40  ? 278 THR B C     1 
ATOM   5890  O O     . THR B  1 278 ? -5.475  -2.414  215.909 1.00 49.34  ? 278 THR B O     1 
ATOM   5891  C CB    . THR B  1 278 ? -4.183  0.015   217.336 1.00 52.92  ? 278 THR B CB    1 
ATOM   5892  O OG1   . THR B  1 278 ? -3.047  0.761   217.787 1.00 53.89  ? 278 THR B OG1   1 
ATOM   5893  C CG2   . THR B  1 278 ? -5.394  0.401   218.175 1.00 49.53  ? 278 THR B CG2   1 
ATOM   5894  N N     . LEU B  1 279 ? -5.808  -2.845  218.092 1.00 52.77  ? 279 LEU B N     1 
ATOM   5895  C CA    . LEU B  1 279 ? -7.063  -3.555  217.881 1.00 54.64  ? 279 LEU B CA    1 
ATOM   5896  C C     . LEU B  1 279 ? -8.120  -3.034  218.850 1.00 53.17  ? 279 LEU B C     1 
ATOM   5897  O O     . LEU B  1 279 ? -8.027  -3.257  220.057 1.00 56.16  ? 279 LEU B O     1 
ATOM   5898  C CB    . LEU B  1 279 ? -6.872  -5.064  218.057 1.00 58.23  ? 279 LEU B CB    1 
ATOM   5899  C CG    . LEU B  1 279 ? -8.101  -5.947  217.822 1.00 57.35  ? 279 LEU B CG    1 
ATOM   5900  C CD1   . LEU B  1 279 ? -8.604  -5.809  216.393 1.00 54.50  ? 279 LEU B CD1   1 
ATOM   5901  C CD2   . LEU B  1 279 ? -7.793  -7.404  218.146 1.00 62.50  ? 279 LEU B CD2   1 
ATOM   5902  N N     . SER B  1 280 ? -9.119  -2.333  218.324 1.00 50.27  ? 280 SER B N     1 
ATOM   5903  C CA    . SER B  1 280 ? -10.164 -1.742  219.159 1.00 57.72  ? 280 SER B CA    1 
ATOM   5904  C C     . SER B  1 280 ? -11.546 -2.259  218.742 1.00 55.21  ? 280 SER B C     1 
ATOM   5905  O O     . SER B  1 280 ? -11.713 -2.745  217.626 1.00 55.04  ? 280 SER B O     1 
ATOM   5906  C CB    . SER B  1 280 ? -10.114 -0.215  219.073 1.00 51.51  ? 280 SER B CB    1 
ATOM   5907  O OG    . SER B  1 280 ? -10.439 0.248   217.772 1.00 56.93  ? 280 SER B OG    1 
ATOM   5908  N N     . VAL B  1 281 ? -12.536 -2.154  219.628 1.00 54.61  ? 281 VAL B N     1 
ATOM   5909  C CA    . VAL B  1 281 ? -13.855 -2.748  219.375 1.00 58.37  ? 281 VAL B CA    1 
ATOM   5910  C C     . VAL B  1 281 ? -14.991 -1.720  219.492 1.00 60.44  ? 281 VAL B C     1 
ATOM   5911  O O     . VAL B  1 281 ? -14.966 -0.867  220.391 1.00 58.87  ? 281 VAL B O     1 
ATOM   5912  C CB    . VAL B  1 281 ? -14.105 -3.921  220.353 1.00 57.41  ? 281 VAL B CB    1 
ATOM   5913  C CG1   . VAL B  1 281 ? -15.433 -4.590  220.075 1.00 63.40  ? 281 VAL B CG1   1 
ATOM   5914  C CG2   . VAL B  1 281 ? -12.965 -4.942  220.274 1.00 59.41  ? 281 VAL B CG2   1 
ATOM   5915  N N     . LEU B  1 282 ? -15.986 -1.780  218.610 1.00 67.99  ? 282 LEU B N     1 
ATOM   5916  C CA    . LEU B  1 282 ? -17.134 -0.894  218.777 1.00 64.77  ? 282 LEU B CA    1 
ATOM   5917  C C     . LEU B  1 282 ? -18.185 -1.590  219.663 1.00 72.00  ? 282 LEU B C     1 
ATOM   5918  O O     . LEU B  1 282 ? -18.142 -1.524  220.849 1.00 76.41  ? 282 LEU B O     1 
ATOM   5919  C CB    . LEU B  1 282 ? -17.762 -0.531  217.425 1.00 70.24  ? 282 LEU B CB    1 
ATOM   5920  C CG    . LEU B  1 282 ? -18.074 0.945   217.162 1.00 72.13  ? 282 LEU B CG    1 
ATOM   5921  C CD1   . LEU B  1 282 ? -19.163 1.343   218.114 1.00 71.53  ? 282 LEU B CD1   1 
ATOM   5922  C CD2   . LEU B  1 282 ? -16.850 1.860   217.298 1.00 69.28  ? 282 LEU B CD2   1 
ATOM   5923  N N     . GLY B  1 283 ? -19.133 -2.264  219.024 1.00 64.46  ? 283 GLY B N     1 
ATOM   5924  C CA    . GLY B  1 283 ? -20.122 -3.109  219.663 1.00 68.02  ? 283 GLY B CA    1 
ATOM   5925  C C     . GLY B  1 283 ? -21.395 -2.362  220.013 1.00 65.08  ? 283 GLY B C     1 
ATOM   5926  O O     . GLY B  1 283 ? -21.330 -1.260  220.548 1.00 65.13  ? 283 GLY B O     1 
ATOM   5927  N N     . GLY B  1 284 ? -22.541 -2.962  219.702 1.00 67.83  ? 284 GLY B N     1 
ATOM   5928  C CA    . GLY B  1 284 ? -23.855 -2.441  220.039 1.00 66.83  ? 284 GLY B CA    1 
ATOM   5929  C C     . GLY B  1 284 ? -24.755 -3.662  219.953 1.00 71.56  ? 284 GLY B C     1 
ATOM   5930  O O     . GLY B  1 284 ? -24.252 -4.739  219.623 1.00 67.92  ? 284 GLY B O     1 
ATOM   5931  N N     . ALA B  1 285 ? -26.055 -3.524  220.218 1.00 75.11  ? 285 ALA B N     1 
ATOM   5932  C CA    . ALA B  1 285 ? -26.915 -4.703  220.287 1.00 81.50  ? 285 ALA B CA    1 
ATOM   5933  C C     . ALA B  1 285 ? -28.410 -4.403  220.340 1.00 86.95  ? 285 ALA B C     1 
ATOM   5934  O O     . ALA B  1 285 ? -28.831 -3.282  220.635 1.00 86.42  ? 285 ALA B O     1 
ATOM   5935  C CB    . ALA B  1 285 ? -26.523 -5.538  221.489 1.00 85.27  ? 285 ALA B CB    1 
ATOM   5936  N N     . ASP B  1 286 ? -29.196 -5.438  220.050 1.00 94.63  ? 286 ASP B N     1 
ATOM   5937  C CA    . ASP B  1 286 ? -30.652 -5.395  220.153 1.00 94.25  ? 286 ASP B CA    1 
ATOM   5938  C C     . ASP B  1 286 ? -31.219 -6.815  220.311 1.00 97.55  ? 286 ASP B C     1 
ATOM   5939  O O     . ASP B  1 286 ? -31.354 -7.551  219.334 1.00 94.59  ? 286 ASP B O     1 
ATOM   5940  C CB    . ASP B  1 286 ? -31.266 -4.713  218.929 1.00 94.23  ? 286 ASP B CB    1 
ATOM   5941  C CG    . ASP B  1 286 ? -32.745 -4.425  219.107 1.00 105.88 ? 286 ASP B CG    1 
ATOM   5942  O OD1   . ASP B  1 286 ? -33.219 -4.488  220.259 1.00 105.50 ? 286 ASP B OD1   1 
ATOM   5943  O OD2   . ASP B  1 286 ? -33.433 -4.135  218.101 1.00 107.37 ? 286 ASP B OD2   1 
ATOM   5944  N N     . GLU B  1 287 ? -31.548 -7.180  221.550 1.00 98.65  ? 287 GLU B N     1 
ATOM   5945  C CA    . GLU B  1 287 ? -32.106 -8.494  221.882 1.00 95.36  ? 287 GLU B CA    1 
ATOM   5946  C C     . GLU B  1 287 ? -31.196 -9.638  221.415 1.00 94.05  ? 287 GLU B C     1 
ATOM   5947  O O     . GLU B  1 287 ? -31.487 -10.320 220.429 1.00 96.67  ? 287 GLU B O     1 
ATOM   5948  C CB    . GLU B  1 287 ? -33.503 -8.645  221.275 1.00 95.48  ? 287 GLU B CB    1 
ATOM   5949  C CG    . GLU B  1 287 ? -34.358 -7.393  221.373 1.00 98.89  ? 287 GLU B CG    1 
ATOM   5950  C CD    . GLU B  1 287 ? -35.721 -7.584  220.750 1.00 90.30  ? 287 GLU B CD    1 
ATOM   5951  O OE1   . GLU B  1 287 ? -35.973 -7.011  219.671 1.00 85.14  ? 287 GLU B OE1   1 
ATOM   5952  O OE2   . GLU B  1 287 ? -36.542 -8.320  221.341 1.00 86.68  ? 287 GLU B OE2   1 
ATOM   5953  N N     . LYS B  1 288 ? -30.086 -9.816  222.127 1.00 94.84  ? 288 LYS B N     1 
ATOM   5954  C CA    . LYS B  1 288 ? -29.066 -10.835 221.850 1.00 90.28  ? 288 LYS B CA    1 
ATOM   5955  C C     . LYS B  1 288 ? -28.555 -10.909 220.404 1.00 89.82  ? 288 LYS B C     1 
ATOM   5956  O O     . LYS B  1 288 ? -27.629 -11.672 220.109 1.00 88.25  ? 288 LYS B O     1 
ATOM   5957  C CB    . LYS B  1 288 ? -29.580 -12.211 222.286 1.00 99.21  ? 288 LYS B CB    1 
ATOM   5958  C CG    . LYS B  1 288 ? -29.198 -12.536 223.723 1.00 102.34 ? 288 LYS B CG    1 
ATOM   5959  C CD    . LYS B  1 288 ? -29.712 -13.894 224.165 1.00 114.20 ? 288 LYS B CD    1 
ATOM   5960  C CE    . LYS B  1 288 ? -28.632 -14.693 224.880 1.00 112.99 ? 288 LYS B CE    1 
ATOM   5961  N NZ    . LYS B  1 288 ? -29.121 -15.258 226.167 1.00 103.33 ? 288 LYS B NZ    1 
ATOM   5962  N N     . GLN B  1 289 ? -29.140 -10.122 219.509 1.00 88.35  ? 289 GLN B N     1 
ATOM   5963  C CA    . GLN B  1 289 ? -28.591 -9.948  218.175 1.00 92.16  ? 289 GLN B CA    1 
ATOM   5964  C C     . GLN B  1 289 ? -27.492 -8.895  218.269 1.00 91.07  ? 289 GLN B C     1 
ATOM   5965  O O     . GLN B  1 289 ? -27.706 -7.726  217.949 1.00 89.47  ? 289 GLN B O     1 
ATOM   5966  C CB    . GLN B  1 289 ? -29.683 -9.531  217.183 1.00 91.95  ? 289 GLN B CB    1 
ATOM   5967  C CG    . GLN B  1 289 ? -30.875 -10.479 217.132 1.00 98.13  ? 289 GLN B CG    1 
ATOM   5968  C CD    . GLN B  1 289 ? -30.715 -11.570 216.089 1.00 95.81  ? 289 GLN B CD    1 
ATOM   5969  O OE1   . GLN B  1 289 ? -30.209 -11.326 214.993 1.00 103.28 ? 289 GLN B OE1   1 
ATOM   5970  N NE2   . GLN B  1 289 ? -31.153 -12.779 216.424 1.00 93.15  ? 289 GLN B NE2   1 
ATOM   5971  N N     . VAL B  1 290 ? -26.319 -9.326  218.720 1.00 84.50  ? 290 VAL B N     1 
ATOM   5972  C CA    . VAL B  1 290 ? -25.227 -8.421  219.068 1.00 79.76  ? 290 VAL B CA    1 
ATOM   5973  C C     . VAL B  1 290 ? -24.182 -8.323  217.961 1.00 72.72  ? 290 VAL B C     1 
ATOM   5974  O O     . VAL B  1 290 ? -23.861 -9.318  217.318 1.00 72.23  ? 290 VAL B O     1 
ATOM   5975  C CB    . VAL B  1 290 ? -24.532 -8.874  220.370 1.00 76.48  ? 290 VAL B CB    1 
ATOM   5976  C CG1   . VAL B  1 290 ? -23.599 -7.796  220.886 1.00 70.16  ? 290 VAL B CG1   1 
ATOM   5977  C CG2   . VAL B  1 290 ? -25.567 -9.214  221.420 1.00 82.24  ? 290 VAL B CG2   1 
ATOM   5978  N N     . TRP B  1 291 ? -23.653 -7.123  217.742 1.00 69.33  ? 291 TRP B N     1 
ATOM   5979  C CA    . TRP B  1 291 ? -22.595 -6.939  216.756 1.00 67.93  ? 291 TRP B CA    1 
ATOM   5980  C C     . TRP B  1 291 ? -21.316 -6.428  217.401 1.00 67.56  ? 291 TRP B C     1 
ATOM   5981  O O     . TRP B  1 291 ? -21.356 -5.587  218.293 1.00 67.01  ? 291 TRP B O     1 
ATOM   5982  C CB    . TRP B  1 291 ? -23.041 -5.982  215.648 1.00 67.93  ? 291 TRP B CB    1 
ATOM   5983  C CG    . TRP B  1 291 ? -23.480 -4.628  216.131 1.00 69.87  ? 291 TRP B CG    1 
ATOM   5984  C CD1   . TRP B  1 291 ? -24.726 -4.274  216.558 1.00 72.59  ? 291 TRP B CD1   1 
ATOM   5985  C CD2   . TRP B  1 291 ? -22.677 -3.442  216.213 1.00 72.79  ? 291 TRP B CD2   1 
ATOM   5986  N NE1   . TRP B  1 291 ? -24.749 -2.945  216.907 1.00 72.71  ? 291 TRP B NE1   1 
ATOM   5987  C CE2   . TRP B  1 291 ? -23.503 -2.411  216.703 1.00 73.04  ? 291 TRP B CE2   1 
ATOM   5988  C CE3   . TRP B  1 291 ? -21.340 -3.153  215.921 1.00 69.09  ? 291 TRP B CE3   1 
ATOM   5989  C CZ2   . TRP B  1 291 ? -23.037 -1.116  216.912 1.00 70.08  ? 291 TRP B CZ2   1 
ATOM   5990  C CZ3   . TRP B  1 291 ? -20.879 -1.864  216.128 1.00 67.40  ? 291 TRP B CZ3   1 
ATOM   5991  C CH2   . TRP B  1 291 ? -21.726 -0.863  216.619 1.00 70.20  ? 291 TRP B CH2   1 
ATOM   5992  N N     . LEU B  1 292 ? -20.183 -6.953  216.950 1.00 68.35  ? 292 LEU B N     1 
ATOM   5993  C CA    . LEU B  1 292 ? -18.884 -6.473  217.399 1.00 62.38  ? 292 LEU B CA    1 
ATOM   5994  C C     . LEU B  1 292 ? -18.034 -6.086  216.200 1.00 65.21  ? 292 LEU B C     1 
ATOM   5995  O O     . LEU B  1 292 ? -17.690 -6.934  215.379 1.00 70.43  ? 292 LEU B O     1 
ATOM   5996  C CB    . LEU B  1 292 ? -18.163 -7.534  218.234 1.00 58.23  ? 292 LEU B CB    1 
ATOM   5997  C CG    . LEU B  1 292 ? -18.796 -7.929  219.570 1.00 61.18  ? 292 LEU B CG    1 
ATOM   5998  C CD1   . LEU B  1 292 ? -17.886 -8.894  220.320 1.00 54.96  ? 292 LEU B CD1   1 
ATOM   5999  C CD2   . LEU B  1 292 ? -19.098 -6.706  220.419 1.00 59.54  ? 292 LEU B CD2   1 
ATOM   6000  N N     . THR B  1 293 ? -17.705 -4.805  216.090 1.00 68.35  ? 293 THR B N     1 
ATOM   6001  C CA    . THR B  1 293 ? -16.832 -4.352  215.016 1.00 66.83  ? 293 THR B CA    1 
ATOM   6002  C C     . THR B  1 293 ? -15.387 -4.305  215.497 1.00 69.51  ? 293 THR B C     1 
ATOM   6003  O O     . THR B  1 293 ? -15.043 -3.511  216.371 1.00 66.72  ? 293 THR B O     1 
ATOM   6004  C CB    . THR B  1 293 ? -17.238 -2.965  214.487 1.00 65.35  ? 293 THR B CB    1 
ATOM   6005  O OG1   . THR B  1 293 ? -18.634 -2.960  214.164 1.00 67.21  ? 293 THR B OG1   1 
ATOM   6006  C CG2   . THR B  1 293 ? -16.435 -2.619  213.241 1.00 68.83  ? 293 THR B CG2   1 
ATOM   6007  N N     . MET B  1 294 ? -14.552 -5.172  214.932 1.00 68.25  ? 294 MET B N     1 
ATOM   6008  C CA    . MET B  1 294 ? -13.129 -5.179  215.241 1.00 65.93  ? 294 MET B CA    1 
ATOM   6009  C C     . MET B  1 294 ? -12.402 -4.191  214.343 1.00 69.12  ? 294 MET B C     1 
ATOM   6010  O O     . MET B  1 294 ? -12.457 -4.300  213.119 1.00 72.09  ? 294 MET B O     1 
ATOM   6011  C CB    . MET B  1 294 ? -12.537 -6.578  215.067 1.00 67.11  ? 294 MET B CB    1 
ATOM   6012  C CG    . MET B  1 294 ? -13.352 -7.684  215.711 1.00 71.19  ? 294 MET B CG    1 
ATOM   6013  S SD    . MET B  1 294 ? -13.470 -7.526  217.501 1.00 77.76  ? 294 MET B SD    1 
ATOM   6014  C CE    . MET B  1 294 ? -11.740 -7.595  217.960 1.00 62.05  ? 294 MET B CE    1 
ATOM   6015  N N     . LEU B  1 295 ? -11.724 -3.227  214.952 1.00 63.40  ? 295 LEU B N     1 
ATOM   6016  C CA    . LEU B  1 295 ? -10.977 -2.235  214.193 1.00 62.53  ? 295 LEU B CA    1 
ATOM   6017  C C     . LEU B  1 295 ? -9.482  -2.425  214.405 1.00 58.14  ? 295 LEU B C     1 
ATOM   6018  O O     . LEU B  1 295 ? -8.980  -2.306  215.523 1.00 54.70  ? 295 LEU B O     1 
ATOM   6019  C CB    . LEU B  1 295 ? -11.409 -0.823  214.592 1.00 59.94  ? 295 LEU B CB    1 
ATOM   6020  C CG    . LEU B  1 295 ? -12.886 -0.526  214.312 1.00 64.83  ? 295 LEU B CG    1 
ATOM   6021  C CD1   . LEU B  1 295 ? -13.518 0.276   215.441 1.00 58.52  ? 295 LEU B CD1   1 
ATOM   6022  C CD2   . LEU B  1 295 ? -13.049 0.199   212.983 1.00 66.18  ? 295 LEU B CD2   1 
ATOM   6023  N N     . GLY B  1 296 ? -8.777  -2.730  213.322 1.00 59.17  ? 296 GLY B N     1 
ATOM   6024  C CA    . GLY B  1 296 ? -7.354  -2.990  213.392 1.00 59.29  ? 296 GLY B CA    1 
ATOM   6025  C C     . GLY B  1 296 ? -6.526  -1.970  212.639 1.00 59.79  ? 296 GLY B C     1 
ATOM   6026  O O     . GLY B  1 296 ? -6.982  -1.379  211.663 1.00 61.27  ? 296 GLY B O     1 
ATOM   6027  N N     . PHE B  1 297 ? -5.300  -1.762  213.105 1.00 56.74  ? 297 PHE B N     1 
ATOM   6028  C CA    . PHE B  1 297 ? -4.358  -0.877  212.436 1.00 59.90  ? 297 PHE B CA    1 
ATOM   6029  C C     . PHE B  1 297 ? -2.948  -1.411  212.625 1.00 58.40  ? 297 PHE B C     1 
ATOM   6030  O O     . PHE B  1 297 ? -2.575  -1.824  213.721 1.00 58.57  ? 297 PHE B O     1 
ATOM   6031  C CB    . PHE B  1 297 ? -4.468  0.556   212.973 1.00 55.73  ? 297 PHE B CB    1 
ATOM   6032  C CG    . PHE B  1 297 ? -3.471  1.516   212.367 1.00 60.30  ? 297 PHE B CG    1 
ATOM   6033  C CD1   . PHE B  1 297 ? -3.813  2.294   211.272 1.00 60.40  ? 297 PHE B CD1   1 
ATOM   6034  C CD2   . PHE B  1 297 ? -2.196  1.650   212.900 1.00 55.84  ? 297 PHE B CD2   1 
ATOM   6035  C CE1   . PHE B  1 297 ? -2.901  3.177   210.716 1.00 60.26  ? 297 PHE B CE1   1 
ATOM   6036  C CE2   . PHE B  1 297 ? -1.283  2.528   212.346 1.00 59.08  ? 297 PHE B CE2   1 
ATOM   6037  C CZ    . PHE B  1 297 ? -1.636  3.293   211.256 1.00 59.35  ? 297 PHE B CZ    1 
ATOM   6038  N N     . HIS B  1 298 ? -2.165  -1.400  211.554 1.00 60.93  ? 298 HIS B N     1 
ATOM   6039  C CA    . HIS B  1 298 ? -0.769  -1.796  211.645 1.00 58.00  ? 298 HIS B CA    1 
ATOM   6040  C C     . HIS B  1 298 ? 0.134   -0.830  210.895 1.00 58.65  ? 298 HIS B C     1 
ATOM   6041  O O     . HIS B  1 298 ? -0.109  -0.520  209.729 1.00 60.37  ? 298 HIS B O     1 
ATOM   6042  C CB    . HIS B  1 298 ? -0.566  -3.211  211.104 1.00 61.13  ? 298 HIS B CB    1 
ATOM   6043  C CG    . HIS B  1 298 ? 0.873   -3.610  210.999 1.00 62.42  ? 298 HIS B CG    1 
ATOM   6044  N ND1   . HIS B  1 298 ? 1.754   -3.498  212.053 1.00 61.14  ? 298 HIS B ND1   1 
ATOM   6045  C CD2   . HIS B  1 298 ? 1.588   -4.109  209.963 1.00 67.81  ? 298 HIS B CD2   1 
ATOM   6046  C CE1   . HIS B  1 298 ? 2.949   -3.913  211.673 1.00 61.42  ? 298 HIS B CE1   1 
ATOM   6047  N NE2   . HIS B  1 298 ? 2.876   -4.291  210.409 1.00 64.53  ? 298 HIS B NE2   1 
ATOM   6048  N N     . PHE B  1 299 ? 1.176   -0.357  211.572 1.00 60.97  ? 299 PHE B N     1 
ATOM   6049  C CA    . PHE B  1 299 ? 2.207   0.447   210.928 1.00 59.89  ? 299 PHE B CA    1 
ATOM   6050  C C     . PHE B  1 299 ? 3.054   -0.424  210.013 1.00 63.19  ? 299 PHE B C     1 
ATOM   6051  O O     . PHE B  1 299 ? 4.232   -0.657  210.281 1.00 64.85  ? 299 PHE B O     1 
ATOM   6052  C CB    . PHE B  1 299 ? 3.101   1.129   211.964 1.00 59.37  ? 299 PHE B CB    1 
ATOM   6053  C CG    . PHE B  1 299 ? 2.412   2.206   212.747 1.00 59.71  ? 299 PHE B CG    1 
ATOM   6054  C CD1   . PHE B  1 299 ? 2.442   3.522   212.316 1.00 61.82  ? 299 PHE B CD1   1 
ATOM   6055  C CD2   . PHE B  1 299 ? 1.744   1.905   213.921 1.00 57.01  ? 299 PHE B CD2   1 
ATOM   6056  C CE1   . PHE B  1 299 ? 1.811   4.518   213.040 1.00 61.28  ? 299 PHE B CE1   1 
ATOM   6057  C CE2   . PHE B  1 299 ? 1.112   2.894   214.649 1.00 58.64  ? 299 PHE B CE2   1 
ATOM   6058  C CZ    . PHE B  1 299 ? 1.145   4.202   214.208 1.00 58.48  ? 299 PHE B CZ    1 
ATOM   6059  N N     . GLY B  1 300 ? 2.450   -0.910  208.936 1.00 65.47  ? 300 GLY B N     1 
ATOM   6060  C CA    . GLY B  1 300 ? 3.149   -1.780  208.014 1.00 67.60  ? 300 GLY B CA    1 
ATOM   6061  C C     . GLY B  1 300 ? 2.227   -2.468  207.031 1.00 68.90  ? 300 GLY B C     1 
ATOM   6062  O O     . GLY B  1 300 ? 1.131   -1.991  206.745 1.00 64.15  ? 300 GLY B O     1 
ATOM   6063  N N     . LEU B  1 301 ? 2.670   -3.616  206.533 1.00 74.11  ? 301 LEU B N     1 
ATOM   6064  C CA    . LEU B  1 301 ? 2.034   -4.242  205.384 1.00 72.11  ? 301 LEU B CA    1 
ATOM   6065  C C     . LEU B  1 301 ? 0.981   -5.291  205.729 1.00 70.69  ? 301 LEU B C     1 
ATOM   6066  O O     . LEU B  1 301 ? 0.887   -5.767  206.860 1.00 71.85  ? 301 LEU B O     1 
ATOM   6067  C CB    . LEU B  1 301 ? 3.103   -4.867  204.491 1.00 73.18  ? 301 LEU B CB    1 
ATOM   6068  C CG    . LEU B  1 301 ? 4.194   -3.880  204.070 1.00 75.22  ? 301 LEU B CG    1 
ATOM   6069  C CD1   . LEU B  1 301 ? 5.303   -4.581  203.299 1.00 72.58  ? 301 LEU B CD1   1 
ATOM   6070  C CD2   . LEU B  1 301 ? 3.597   -2.736  203.259 1.00 76.48  ? 301 LEU B CD2   1 
ATOM   6071  N N     . LYS B  1 302 ? 0.194   -5.632  204.716 1.00 70.53  ? 302 LYS B N     1 
ATOM   6072  C CA    . LYS B  1 302 ? -0.879  -6.612  204.810 1.00 74.39  ? 302 LYS B CA    1 
ATOM   6073  C C     . LYS B  1 302 ? -0.392  -7.975  205.296 1.00 73.39  ? 302 LYS B C     1 
ATOM   6074  O O     . LYS B  1 302 ? -1.074  -8.653  206.066 1.00 74.36  ? 302 LYS B O     1 
ATOM   6075  C CB    . LYS B  1 302 ? -1.537  -6.744  203.440 1.00 77.58  ? 302 LYS B CB    1 
ATOM   6076  C CG    . LYS B  1 302 ? -2.772  -7.591  203.377 1.00 81.34  ? 302 LYS B CG    1 
ATOM   6077  C CD    . LYS B  1 302 ? -3.369  -7.459  201.994 1.00 81.32  ? 302 LYS B CD    1 
ATOM   6078  C CE    . LYS B  1 302 ? -4.557  -8.356  201.819 1.00 84.72  ? 302 LYS B CE    1 
ATOM   6079  N NZ    . LYS B  1 302 ? -5.100  -8.294  200.436 1.00 86.26  ? 302 LYS B NZ    1 
ATOM   6080  N N     . THR B  1 303 ? 0.796   -8.363  204.843 1.00 72.91  ? 303 THR B N     1 
ATOM   6081  C CA    . THR B  1 303 ? 1.357   -9.675  205.142 1.00 74.62  ? 303 THR B CA    1 
ATOM   6082  C C     . THR B  1 303 ? 1.604   -9.879  206.637 1.00 75.08  ? 303 THR B C     1 
ATOM   6083  O O     . THR B  1 303 ? 1.133   -10.852 207.222 1.00 71.94  ? 303 THR B O     1 
ATOM   6084  C CB    . THR B  1 303 ? 2.678   -9.895  204.381 1.00 73.61  ? 303 THR B CB    1 
ATOM   6085  O OG1   . THR B  1 303 ? 3.647   -8.932  204.813 1.00 76.40  ? 303 THR B OG1   1 
ATOM   6086  C CG2   . THR B  1 303 ? 2.457   -9.746  202.879 1.00 70.29  ? 303 THR B CG2   1 
ATOM   6087  N N     . VAL B  1 304 ? 2.342   -8.956  207.247 1.00 72.27  ? 304 VAL B N     1 
ATOM   6088  C CA    . VAL B  1 304 ? 2.652   -9.036  208.670 1.00 67.93  ? 304 VAL B CA    1 
ATOM   6089  C C     . VAL B  1 304 ? 1.382   -8.931  209.512 1.00 69.75  ? 304 VAL B C     1 
ATOM   6090  O O     . VAL B  1 304 ? 1.251   -9.596  210.541 1.00 68.95  ? 304 VAL B O     1 
ATOM   6091  C CB    . VAL B  1 304 ? 3.645   -7.929  209.089 1.00 71.22  ? 304 VAL B CB    1 
ATOM   6092  C CG1   . VAL B  1 304 ? 3.969   -8.029  210.573 1.00 68.16  ? 304 VAL B CG1   1 
ATOM   6093  C CG2   . VAL B  1 304 ? 4.916   -8.010  208.254 1.00 62.45  ? 304 VAL B CG2   1 
ATOM   6094  N N     . ALA B  1 305 ? 0.443   -8.107  209.055 1.00 70.73  ? 305 ALA B N     1 
ATOM   6095  C CA    . ALA B  1 305 ? -0.817  -7.888  209.762 1.00 71.37  ? 305 ALA B CA    1 
ATOM   6096  C C     . ALA B  1 305 ? -1.605  -9.183  209.973 1.00 69.34  ? 305 ALA B C     1 
ATOM   6097  O O     . ALA B  1 305 ? -1.905  -9.549  211.108 1.00 68.04  ? 305 ALA B O     1 
ATOM   6098  C CB    . ALA B  1 305 ? -1.667  -6.873  209.012 1.00 68.96  ? 305 ALA B CB    1 
ATOM   6099  N N     . LYS B  1 306 ? -1.942  -9.873  208.886 1.00 70.52  ? 306 LYS B N     1 
ATOM   6100  C CA    . LYS B  1 306 ? -2.683  -11.126 208.997 1.00 75.40  ? 306 LYS B CA    1 
ATOM   6101  C C     . LYS B  1 306 ? -1.852  -12.193 209.701 1.00 69.83  ? 306 LYS B C     1 
ATOM   6102  O O     . LYS B  1 306 ? -2.361  -12.924 210.550 1.00 65.69  ? 306 LYS B O     1 
ATOM   6103  C CB    . LYS B  1 306 ? -3.124  -11.635 207.624 1.00 77.88  ? 306 LYS B CB    1 
ATOM   6104  C CG    . LYS B  1 306 ? -3.983  -12.889 207.705 1.00 83.49  ? 306 LYS B CG    1 
ATOM   6105  C CD    . LYS B  1 306 ? -4.672  -13.217 206.393 1.00 82.76  ? 306 LYS B CD    1 
ATOM   6106  C CE    . LYS B  1 306 ? -5.755  -14.269 206.600 1.00 87.31  ? 306 LYS B CE    1 
ATOM   6107  N NZ    . LYS B  1 306 ? -5.225  -15.510 207.232 1.00 85.34  ? 306 LYS B NZ    1 
ATOM   6108  N N     . SER B  1 307 ? -0.575  -12.273 209.336 1.00 68.16  ? 307 SER B N     1 
ATOM   6109  C CA    . SER B  1 307 ? 0.365   -13.193 209.970 1.00 71.58  ? 307 SER B CA    1 
ATOM   6110  C C     . SER B  1 307 ? 0.333   -13.070 211.486 1.00 71.46  ? 307 SER B C     1 
ATOM   6111  O O     . SER B  1 307 ? 0.321   -14.070 212.204 1.00 67.18  ? 307 SER B O     1 
ATOM   6112  C CB    . SER B  1 307 ? 1.784   -12.937 209.468 1.00 68.23  ? 307 SER B CB    1 
ATOM   6113  O OG    . SER B  1 307 ? 2.741   -13.496 210.351 1.00 74.33  ? 307 SER B OG    1 
ATOM   6114  N N     . THR B  1 308 ? 0.314   -11.830 211.960 1.00 71.65  ? 308 THR B N     1 
ATOM   6115  C CA    . THR B  1 308 ? 0.282   -11.552 213.386 1.00 67.47  ? 308 THR B CA    1 
ATOM   6116  C C     . THR B  1 308 ? -1.061  -11.942 213.997 1.00 64.83  ? 308 THR B C     1 
ATOM   6117  O O     . THR B  1 308 ? -1.104  -12.568 215.052 1.00 61.69  ? 308 THR B O     1 
ATOM   6118  C CB    . THR B  1 308 ? 0.554   -10.067 213.679 1.00 63.79  ? 308 THR B CB    1 
ATOM   6119  O OG1   . THR B  1 308 ? 1.742   -9.653  212.992 1.00 67.88  ? 308 THR B OG1   1 
ATOM   6120  C CG2   . THR B  1 308 ? 0.729   -9.843  215.173 1.00 60.06  ? 308 THR B CG2   1 
ATOM   6121  N N     . PHE B  1 309 ? -2.157  -11.584 213.336 1.00 66.33  ? 309 PHE B N     1 
ATOM   6122  C CA    . PHE B  1 309 ? -3.478  -11.831 213.907 1.00 64.28  ? 309 PHE B CA    1 
ATOM   6123  C C     . PHE B  1 309 ? -3.942  -13.276 213.733 1.00 64.86  ? 309 PHE B C     1 
ATOM   6124  O O     . PHE B  1 309 ? -4.719  -13.772 214.547 1.00 61.35  ? 309 PHE B O     1 
ATOM   6125  C CB    . PHE B  1 309 ? -4.511  -10.870 213.314 1.00 64.61  ? 309 PHE B CB    1 
ATOM   6126  C CG    . PHE B  1 309 ? -4.429  -9.478  213.876 1.00 69.11  ? 309 PHE B CG    1 
ATOM   6127  C CD1   . PHE B  1 309 ? -4.944  -9.187  215.131 1.00 65.51  ? 309 PHE B CD1   1 
ATOM   6128  C CD2   . PHE B  1 309 ? -3.828  -8.462  213.155 1.00 66.10  ? 309 PHE B CD2   1 
ATOM   6129  C CE1   . PHE B  1 309 ? -4.861  -7.907  215.651 1.00 62.34  ? 309 PHE B CE1   1 
ATOM   6130  C CE2   . PHE B  1 309 ? -3.742  -7.183  213.668 1.00 65.13  ? 309 PHE B CE2   1 
ATOM   6131  C CZ    . PHE B  1 309 ? -4.259  -6.904  214.916 1.00 58.43  ? 309 PHE B CZ    1 
ATOM   6132  N N     . ASP B  1 310 ? -3.477  -13.945 212.680 1.00 64.87  ? 310 ASP B N     1 
ATOM   6133  C CA    . ASP B  1 310 ? -3.717  -15.380 212.531 1.00 68.53  ? 310 ASP B CA    1 
ATOM   6134  C C     . ASP B  1 310 ? -3.196  -16.108 213.759 1.00 61.79  ? 310 ASP B C     1 
ATOM   6135  O O     . ASP B  1 310 ? -3.853  -16.990 214.309 1.00 66.65  ? 310 ASP B O     1 
ATOM   6136  C CB    . ASP B  1 310 ? -3.036  -15.938 211.278 1.00 68.91  ? 310 ASP B CB    1 
ATOM   6137  C CG    . ASP B  1 310 ? -3.776  -15.598 210.006 1.00 70.79  ? 310 ASP B CG    1 
ATOM   6138  O OD1   . ASP B  1 310 ? -4.979  -15.270 210.080 1.00 74.36  ? 310 ASP B OD1   1 
ATOM   6139  O OD2   . ASP B  1 310 ? -3.151  -15.671 208.927 1.00 73.97  ? 310 ASP B OD2   1 
ATOM   6140  N N     . LEU B  1 311 ? -1.999  -15.716 214.174 1.00 59.44  ? 311 LEU B N     1 
ATOM   6141  C CA    . LEU B  1 311 ? -1.352  -16.261 215.356 1.00 60.72  ? 311 LEU B CA    1 
ATOM   6142  C C     . LEU B  1 311 ? -2.079  -15.864 216.637 1.00 60.99  ? 311 LEU B C     1 
ATOM   6143  O O     . LEU B  1 311 ? -2.367  -16.706 217.490 1.00 62.29  ? 311 LEU B O     1 
ATOM   6144  C CB    . LEU B  1 311 ? 0.100   -15.782 215.409 1.00 55.55  ? 311 LEU B CB    1 
ATOM   6145  C CG    . LEU B  1 311 ? 1.158   -16.731 215.967 1.00 57.86  ? 311 LEU B CG    1 
ATOM   6146  C CD1   . LEU B  1 311 ? 0.963   -18.127 215.406 1.00 53.04  ? 311 LEU B CD1   1 
ATOM   6147  C CD2   . LEU B  1 311 ? 2.546   -16.212 215.630 1.00 48.77  ? 311 LEU B CD2   1 
ATOM   6148  N N     . LEU B  1 312 ? -2.381  -14.575 216.764 1.00 63.86  ? 312 LEU B N     1 
ATOM   6149  C CA    . LEU B  1 312 ? -2.871  -14.026 218.030 1.00 59.98  ? 312 LEU B CA    1 
ATOM   6150  C C     . LEU B  1 312 ? -4.386  -14.088 218.201 1.00 59.57  ? 312 LEU B C     1 
ATOM   6151  O O     . LEU B  1 312 ? -4.882  -14.172 219.326 1.00 62.08  ? 312 LEU B O     1 
ATOM   6152  C CB    . LEU B  1 312 ? -2.401  -12.566 218.191 1.00 60.11  ? 312 LEU B CB    1 
ATOM   6153  C CG    . LEU B  1 312 ? -1.015  -12.296 218.792 1.00 61.96  ? 312 LEU B CG    1 
ATOM   6154  C CD1   . LEU B  1 312 ? 0.090   -12.792 217.879 1.00 67.61  ? 312 LEU B CD1   1 
ATOM   6155  C CD2   . LEU B  1 312 ? -0.812  -10.816 219.108 1.00 67.14  ? 312 LEU B CD2   1 
ATOM   6156  N N     . PHE B  1 313 ? -5.118  -14.048 217.090 1.00 58.40  ? 313 PHE B N     1 
ATOM   6157  C CA    . PHE B  1 313 ? -6.588  -13.991 217.139 1.00 66.16  ? 313 PHE B CA    1 
ATOM   6158  C C     . PHE B  1 313 ? -7.241  -14.628 215.905 1.00 68.94  ? 313 PHE B C     1 
ATOM   6159  O O     . PHE B  1 313 ? -7.913  -13.936 215.137 1.00 70.97  ? 313 PHE B O     1 
ATOM   6160  C CB    . PHE B  1 313 ? -7.040  -12.540 217.264 1.00 66.23  ? 313 PHE B CB    1 
ATOM   6161  C CG    . PHE B  1 313 ? -8.213  -12.333 218.179 1.00 67.16  ? 313 PHE B CG    1 
ATOM   6162  C CD1   . PHE B  1 313 ? -8.850  -13.403 218.779 1.00 67.64  ? 313 PHE B CD1   1 
ATOM   6163  C CD2   . PHE B  1 313 ? -8.678  -11.050 218.436 1.00 65.77  ? 313 PHE B CD2   1 
ATOM   6164  C CE1   . PHE B  1 313 ? -9.930  -13.206 219.627 1.00 67.72  ? 313 PHE B CE1   1 
ATOM   6165  C CE2   . PHE B  1 313 ? -9.754  -10.844 219.278 1.00 62.08  ? 313 PHE B CE2   1 
ATOM   6166  C CZ    . PHE B  1 313 ? -10.380 -11.920 219.874 1.00 67.78  ? 313 PHE B CZ    1 
ATOM   6167  N N     . PRO B  1 314 ? -7.048  -15.945 215.710 1.00 70.59  ? 314 PRO B N     1 
ATOM   6168  C CA    . PRO B  1 314 ? -7.696  -16.606 214.576 1.00 71.32  ? 314 PRO B CA    1 
ATOM   6169  C C     . PRO B  1 314 ? -9.220  -16.612 214.707 1.00 71.20  ? 314 PRO B C     1 
ATOM   6170  O O     . PRO B  1 314 ? -9.903  -16.568 213.684 1.00 69.20  ? 314 PRO B O     1 
ATOM   6171  C CB    . PRO B  1 314 ? -7.128  -18.031 214.619 1.00 72.89  ? 314 PRO B CB    1 
ATOM   6172  C CG    . PRO B  1 314 ? -6.649  -18.208 216.019 1.00 72.79  ? 314 PRO B CG    1 
ATOM   6173  C CD    . PRO B  1 314 ? -6.201  -16.869 216.478 1.00 73.36  ? 314 PRO B CD    1 
ATOM   6174  N N     . GLU B  1 315 ? -9.733  -16.625 215.938 1.00 73.79  ? 315 GLU B N     1 
ATOM   6175  C CA    . GLU B  1 315 ? -11.172 -16.709 216.201 1.00 74.05  ? 315 GLU B CA    1 
ATOM   6176  C C     . GLU B  1 315 ? -12.002 -15.643 215.473 1.00 75.72  ? 315 GLU B C     1 
ATOM   6177  O O     . GLU B  1 315 ? -13.223 -15.779 215.343 1.00 77.92  ? 315 GLU B O     1 
ATOM   6178  C CB    . GLU B  1 315 ? -11.449 -16.607 217.706 1.00 71.88  ? 315 GLU B CB    1 
ATOM   6179  C CG    . GLU B  1 315 ? -10.760 -17.656 218.573 1.00 77.99  ? 315 GLU B CG    1 
ATOM   6180  C CD    . GLU B  1 315 ? -9.359  -17.245 219.003 1.00 87.00  ? 315 GLU B CD    1 
ATOM   6181  O OE1   . GLU B  1 315 ? -8.859  -17.790 220.012 1.00 85.79  ? 315 GLU B OE1   1 
ATOM   6182  O OE2   . GLU B  1 315 ? -8.754  -16.382 218.338 1.00 92.10  ? 315 GLU B OE2   1 
ATOM   6183  N N     . LEU B  1 316 ? -11.338 -14.585 215.013 1.00 78.60  ? 316 LEU B N     1 
ATOM   6184  C CA    . LEU B  1 316 ? -12.003 -13.506 214.291 1.00 81.62  ? 316 LEU B CA    1 
ATOM   6185  C C     . LEU B  1 316 ? -12.295 -13.851 212.837 1.00 79.80  ? 316 LEU B C     1 
ATOM   6186  O O     . LEU B  1 316 ? -12.779 -12.997 212.094 1.00 82.95  ? 316 LEU B O     1 
ATOM   6187  C CB    . LEU B  1 316 ? -11.163 -12.227 214.331 1.00 76.27  ? 316 LEU B CB    1 
ATOM   6188  C CG    . LEU B  1 316 ? -11.093 -11.464 215.650 1.00 72.07  ? 316 LEU B CG    1 
ATOM   6189  C CD1   . LEU B  1 316 ? -10.351 -10.145 215.481 1.00 70.55  ? 316 LEU B CD1   1 
ATOM   6190  C CD2   . LEU B  1 316 ? -12.491 -11.237 216.205 1.00 74.29  ? 316 LEU B CD2   1 
ATOM   6191  N N     . GLY B  1 317 ? -11.993 -15.086 212.437 1.00 81.31  ? 317 GLY B N     1 
ATOM   6192  C CA    . GLY B  1 317 ? -12.160 -15.523 211.060 1.00 83.60  ? 317 GLY B CA    1 
ATOM   6193  C C     . GLY B  1 317 ? -11.768 -14.449 210.063 1.00 83.65  ? 317 GLY B C     1 
ATOM   6194  O O     . GLY B  1 317 ? -12.462 -14.211 209.072 1.00 86.18  ? 317 GLY B O     1 
ATOM   6195  N N     . LEU B  1 318 ? -10.673 -13.759 210.366 1.00 80.72  ? 318 LEU B N     1 
ATOM   6196  C CA    . LEU B  1 318 ? -10.200 -12.680 209.522 1.00 82.64  ? 318 LEU B CA    1 
ATOM   6197  C C     . LEU B  1 318 ? -9.540  -13.290 208.307 1.00 83.05  ? 318 LEU B C     1 
ATOM   6198  O O     . LEU B  1 318 ? -8.712  -14.193 208.423 1.00 84.87  ? 318 LEU B O     1 
ATOM   6199  C CB    . LEU B  1 318 ? -9.233  -11.765 210.279 1.00 84.51  ? 318 LEU B CB    1 
ATOM   6200  C CG    . LEU B  1 318 ? -9.866  -10.552 210.961 1.00 80.94  ? 318 LEU B CG    1 
ATOM   6201  C CD1   . LEU B  1 318 ? -9.002  -10.055 212.103 1.00 76.06  ? 318 LEU B CD1   1 
ATOM   6202  C CD2   . LEU B  1 318 ? -10.061 -9.448  209.943 1.00 78.38  ? 318 LEU B CD2   1 
ATOM   6203  N N     . VAL B  1 319 ? -9.931  -12.807 207.137 1.00 83.88  ? 319 VAL B N     1 
ATOM   6204  C CA    . VAL B  1 319 ? -9.431  -13.349 205.889 1.00 83.48  ? 319 VAL B CA    1 
ATOM   6205  C C     . VAL B  1 319 ? -8.547  -12.315 205.209 1.00 86.41  ? 319 VAL B C     1 
ATOM   6206  O O     . VAL B  1 319 ? -8.451  -11.181 205.672 1.00 87.36  ? 319 VAL B O     1 
ATOM   6207  C CB    . VAL B  1 319 ? -10.585 -13.768 204.969 1.00 86.17  ? 319 VAL B CB    1 
ATOM   6208  C CG1   . VAL B  1 319 ? -11.340 -14.941 205.581 1.00 82.41  ? 319 VAL B CG1   1 
ATOM   6209  C CG2   . VAL B  1 319 ? -11.526 -12.597 204.734 1.00 85.89  ? 319 VAL B CG2   1 
ATOM   6210  N N     . GLU B  1 320 ? -7.892  -12.707 204.121 1.00 86.28  ? 320 GLU B N     1 
ATOM   6211  C CA    . GLU B  1 320 ? -6.976  -11.804 203.433 1.00 85.39  ? 320 GLU B CA    1 
ATOM   6212  C C     . GLU B  1 320 ? -7.707  -10.590 202.850 1.00 87.61  ? 320 GLU B C     1 
ATOM   6213  O O     . GLU B  1 320 ? -7.166  -9.489  202.822 1.00 85.22  ? 320 GLU B O     1 
ATOM   6214  C CB    . GLU B  1 320 ? -6.210  -12.551 202.333 1.00 86.95  ? 320 GLU B CB    1 
ATOM   6215  C CG    . GLU B  1 320 ? -5.457  -11.647 201.365 1.00 88.69  ? 320 GLU B CG    1 
ATOM   6216  C CD    . GLU B  1 320 ? -4.324  -12.350 200.635 1.00 94.51  ? 320 GLU B CD    1 
ATOM   6217  O OE1   . GLU B  1 320 ? -3.791  -13.341 201.174 1.00 93.43  ? 320 GLU B OE1   1 
ATOM   6218  O OE2   . GLU B  1 320 ? -3.967  -11.906 199.522 1.00 95.67  ? 320 GLU B OE2   1 
ATOM   6219  N N     . GLU B  1 321 ? -8.946  -10.788 202.416 1.00 91.80  ? 321 GLU B N     1 
ATOM   6220  C CA    . GLU B  1 321 ? -9.719  -9.721  201.784 1.00 90.10  ? 321 GLU B CA    1 
ATOM   6221  C C     . GLU B  1 321 ? -10.007 -8.572  202.753 1.00 87.94  ? 321 GLU B C     1 
ATOM   6222  O O     . GLU B  1 321 ? -10.204 -7.431  202.334 1.00 85.62  ? 321 GLU B O     1 
ATOM   6223  C CB    . GLU B  1 321 ? -11.031 -10.277 201.222 1.00 90.90  ? 321 GLU B CB    1 
ATOM   6224  C CG    . GLU B  1 321 ? -10.858 -11.349 200.144 1.00 98.29  ? 321 GLU B CG    1 
ATOM   6225  C CD    . GLU B  1 321 ? -10.438 -12.702 200.700 1.00 108.38 ? 321 GLU B CD    1 
ATOM   6226  O OE1   . GLU B  1 321 ? -10.125 -12.786 201.906 1.00 104.41 ? 321 GLU B OE1   1 
ATOM   6227  O OE2   . GLU B  1 321 ? -10.421 -13.684 199.930 1.00 116.85 ? 321 GLU B OE2   1 
ATOM   6228  N N     . ASP B  1 322 ? -10.019 -8.877  204.047 1.00 86.10  ? 322 ASP B N     1 
ATOM   6229  C CA    . ASP B  1 322 ? -10.311 -7.878  205.074 1.00 82.76  ? 322 ASP B CA    1 
ATOM   6230  C C     . ASP B  1 322 ? -9.195  -6.851  205.242 1.00 80.87  ? 322 ASP B C     1 
ATOM   6231  O O     . ASP B  1 322 ? -9.460  -5.679  205.511 1.00 77.63  ? 322 ASP B O     1 
ATOM   6232  C CB    . ASP B  1 322 ? -10.579 -8.560  206.417 1.00 82.42  ? 322 ASP B CB    1 
ATOM   6233  C CG    . ASP B  1 322 ? -11.792 -9.462  206.377 1.00 85.67  ? 322 ASP B CG    1 
ATOM   6234  O OD1   . ASP B  1 322 ? -12.738 -9.154  205.623 1.00 88.65  ? 322 ASP B OD1   1 
ATOM   6235  O OD2   . ASP B  1 322 ? -11.802 -10.479 207.104 1.00 84.08  ? 322 ASP B OD2   1 
ATOM   6236  N N     . TYR B  1 323 ? -7.949  -7.293  205.101 1.00 80.41  ? 323 TYR B N     1 
ATOM   6237  C CA    . TYR B  1 323 ? -6.806  -6.412  205.312 1.00 74.61  ? 323 TYR B CA    1 
ATOM   6238  C C     . TYR B  1 323 ? -6.610  -5.476  204.130 1.00 77.32  ? 323 TYR B C     1 
ATOM   6239  O O     . TYR B  1 323 ? -6.346  -5.916  203.012 1.00 78.73  ? 323 TYR B O     1 
ATOM   6240  C CB    . TYR B  1 323 ? -5.537  -7.227  205.557 1.00 78.50  ? 323 TYR B CB    1 
ATOM   6241  C CG    . TYR B  1 323 ? -5.629  -8.108  206.777 1.00 78.15  ? 323 TYR B CG    1 
ATOM   6242  C CD1   . TYR B  1 323 ? -5.216  -7.650  208.019 1.00 76.16  ? 323 TYR B CD1   1 
ATOM   6243  C CD2   . TYR B  1 323 ? -6.145  -9.393  206.690 1.00 78.29  ? 323 TYR B CD2   1 
ATOM   6244  C CE1   . TYR B  1 323 ? -5.308  -8.450  209.140 1.00 74.34  ? 323 TYR B CE1   1 
ATOM   6245  C CE2   . TYR B  1 323 ? -6.244  -10.200 207.803 1.00 78.75  ? 323 TYR B CE2   1 
ATOM   6246  C CZ    . TYR B  1 323 ? -5.822  -9.724  209.027 1.00 76.23  ? 323 TYR B CZ    1 
ATOM   6247  O OH    . TYR B  1 323 ? -5.913  -10.524 210.142 1.00 75.10  ? 323 TYR B OH    1 
ATOM   6248  N N     . LEU B  1 324 ? -6.743  -4.180  204.387 1.00 75.85  ? 324 LEU B N     1 
ATOM   6249  C CA    . LEU B  1 324 ? -6.664  -3.179  203.333 1.00 72.86  ? 324 LEU B CA    1 
ATOM   6250  C C     . LEU B  1 324 ? -5.424  -2.303  203.489 1.00 70.59  ? 324 LEU B C     1 
ATOM   6251  O O     . LEU B  1 324 ? -5.215  -1.689  204.534 1.00 69.17  ? 324 LEU B O     1 
ATOM   6252  C CB    . LEU B  1 324 ? -7.927  -2.315  203.336 1.00 72.19  ? 324 LEU B CB    1 
ATOM   6253  C CG    . LEU B  1 324 ? -9.249  -3.086  203.288 1.00 71.12  ? 324 LEU B CG    1 
ATOM   6254  C CD1   . LEU B  1 324 ? -10.411 -2.208  203.727 1.00 73.28  ? 324 LEU B CD1   1 
ATOM   6255  C CD2   . LEU B  1 324 ? -9.498  -3.642  201.895 1.00 70.48  ? 324 LEU B CD2   1 
ATOM   6256  N N     . GLU B  1 325 ? -4.598  -2.254  202.449 1.00 70.17  ? 325 GLU B N     1 
ATOM   6257  C CA    . GLU B  1 325 ? -3.427  -1.386  202.461 1.00 68.99  ? 325 GLU B CA    1 
ATOM   6258  C C     . GLU B  1 325 ? -3.732  -0.038  201.829 1.00 76.61  ? 325 GLU B C     1 
ATOM   6259  O O     . GLU B  1 325 ? -4.415  0.044   200.808 1.00 78.42  ? 325 GLU B O     1 
ATOM   6260  C CB    . GLU B  1 325 ? -2.250  -2.042  201.738 1.00 72.25  ? 325 GLU B CB    1 
ATOM   6261  C CG    . GLU B  1 325 ? -1.275  -2.744  202.666 1.00 77.17  ? 325 GLU B CG    1 
ATOM   6262  C CD    . GLU B  1 325 ? -0.189  -3.481  201.912 1.00 79.57  ? 325 GLU B CD    1 
ATOM   6263  O OE1   . GLU B  1 325 ? 0.076   -3.119  200.747 1.00 85.20  ? 325 GLU B OE1   1 
ATOM   6264  O OE2   . GLU B  1 325 ? 0.391   -4.428  202.481 1.00 76.75  ? 325 GLU B OE2   1 
ATOM   6265  N N     . MET B  1 326 ? -3.215  1.016   202.452 1.00 72.29  ? 326 MET B N     1 
ATOM   6266  C CA    . MET B  1 326 ? -3.371  2.375   201.956 1.00 66.58  ? 326 MET B CA    1 
ATOM   6267  C C     . MET B  1 326 ? -2.427  3.309   202.701 1.00 68.84  ? 326 MET B C     1 
ATOM   6268  O O     . MET B  1 326 ? -1.729  2.888   203.625 1.00 68.87  ? 326 MET B O     1 
ATOM   6269  C CB    . MET B  1 326 ? -4.820  2.847   202.102 1.00 67.13  ? 326 MET B CB    1 
ATOM   6270  C CG    . MET B  1 326 ? -5.450  2.564   203.453 1.00 65.81  ? 326 MET B CG    1 
ATOM   6271  S SD    . MET B  1 326 ? -7.160  3.131   203.526 1.00 74.78  ? 326 MET B SD    1 
ATOM   6272  C CE    . MET B  1 326 ? -7.996  1.660   204.106 1.00 66.64  ? 326 MET B CE    1 
ATOM   6273  N N     . SER B  1 327 ? -2.401  4.575   202.297 1.00 69.06  ? 327 SER B N     1 
ATOM   6274  C CA    . SER B  1 327 ? -1.565  5.563   202.967 1.00 69.53  ? 327 SER B CA    1 
ATOM   6275  C C     . SER B  1 327 ? -2.116  5.840   204.359 1.00 66.84  ? 327 SER B C     1 
ATOM   6276  O O     . SER B  1 327 ? -3.229  5.422   204.685 1.00 66.59  ? 327 SER B O     1 
ATOM   6277  C CB    . SER B  1 327 ? -1.489  6.856   202.152 1.00 70.20  ? 327 SER B CB    1 
ATOM   6278  O OG    . SER B  1 327 ? -2.722  7.552   202.179 1.00 69.92  ? 327 SER B OG    1 
ATOM   6279  N N     . TRP B  1 328 ? -1.333  6.533   205.181 1.00 61.55  ? 328 TRP B N     1 
ATOM   6280  C CA    . TRP B  1 328 ? -1.774  6.887   206.525 1.00 64.84  ? 328 TRP B CA    1 
ATOM   6281  C C     . TRP B  1 328 ? -3.019  7.762   206.478 1.00 66.42  ? 328 TRP B C     1 
ATOM   6282  O O     . TRP B  1 328 ? -3.993  7.512   207.189 1.00 63.99  ? 328 TRP B O     1 
ATOM   6283  C CB    . TRP B  1 328 ? -0.673  7.612   207.296 1.00 64.73  ? 328 TRP B CB    1 
ATOM   6284  C CG    . TRP B  1 328 ? -1.198  8.280   208.526 1.00 65.34  ? 328 TRP B CG    1 
ATOM   6285  C CD1   . TRP B  1 328 ? -1.541  7.679   209.701 1.00 65.85  ? 328 TRP B CD1   1 
ATOM   6286  C CD2   . TRP B  1 328 ? -1.462  9.678   208.699 1.00 62.28  ? 328 TRP B CD2   1 
ATOM   6287  N NE1   . TRP B  1 328 ? -1.996  8.614   210.597 1.00 64.06  ? 328 TRP B NE1   1 
ATOM   6288  C CE2   . TRP B  1 328 ? -1.957  9.850   210.006 1.00 63.84  ? 328 TRP B CE2   1 
ATOM   6289  C CE3   . TRP B  1 328 ? -1.323  10.800  207.877 1.00 62.04  ? 328 TRP B CE3   1 
ATOM   6290  C CZ2   . TRP B  1 328 ? -2.314  11.098  210.511 1.00 62.21  ? 328 TRP B CZ2   1 
ATOM   6291  C CZ3   . TRP B  1 328 ? -1.678  12.039  208.380 1.00 59.93  ? 328 TRP B CZ3   1 
ATOM   6292  C CH2   . TRP B  1 328 ? -2.168  12.178  209.685 1.00 60.03  ? 328 TRP B CH2   1 
ATOM   6293  N N     . GLY B  1 329 ? -2.968  8.790   205.637 1.00 66.38  ? 329 GLY B N     1 
ATOM   6294  C CA    . GLY B  1 329 ? -4.091  9.688   205.447 1.00 65.06  ? 329 GLY B CA    1 
ATOM   6295  C C     . GLY B  1 329 ? -5.348  8.951   205.030 1.00 64.64  ? 329 GLY B C     1 
ATOM   6296  O O     . GLY B  1 329 ? -6.425  9.191   205.571 1.00 66.61  ? 329 GLY B O     1 
ATOM   6297  N N     . GLU B  1 330 ? -5.207  8.042   204.071 1.00 65.07  ? 330 GLU B N     1 
ATOM   6298  C CA    . GLU B  1 330 ? -6.339  7.262   203.583 1.00 66.92  ? 330 GLU B CA    1 
ATOM   6299  C C     . GLU B  1 330 ? -6.916  6.368   204.677 1.00 65.45  ? 330 GLU B C     1 
ATOM   6300  O O     . GLU B  1 330 ? -8.123  6.134   204.723 1.00 66.32  ? 330 GLU B O     1 
ATOM   6301  C CB    . GLU B  1 330 ? -5.926  6.416   202.374 1.00 70.15  ? 330 GLU B CB    1 
ATOM   6302  C CG    . GLU B  1 330 ? -5.730  7.218   201.093 1.00 72.15  ? 330 GLU B CG    1 
ATOM   6303  C CD    . GLU B  1 330 ? -4.911  6.475   200.051 1.00 76.71  ? 330 GLU B CD    1 
ATOM   6304  O OE1   . GLU B  1 330 ? -4.725  5.249   200.193 1.00 76.64  ? 330 GLU B OE1   1 
ATOM   6305  O OE2   . GLU B  1 330 ? -4.440  7.121   199.091 1.00 77.76  ? 330 GLU B OE2   1 
ATOM   6306  N N     . SER B  1 331 ? -6.048  5.876   205.557 1.00 65.32  ? 331 SER B N     1 
ATOM   6307  C CA    . SER B  1 331 ? -6.476  5.004   206.645 1.00 65.48  ? 331 SER B CA    1 
ATOM   6308  C C     . SER B  1 331 ? -7.354  5.745   207.650 1.00 65.39  ? 331 SER B C     1 
ATOM   6309  O O     . SER B  1 331 ? -8.391  5.231   208.064 1.00 67.34  ? 331 SER B O     1 
ATOM   6310  C CB    . SER B  1 331 ? -5.267  4.394   207.356 1.00 61.07  ? 331 SER B CB    1 
ATOM   6311  O OG    . SER B  1 331 ? -4.426  5.402   207.889 1.00 65.39  ? 331 SER B OG    1 
ATOM   6312  N N     . PHE B  1 332 ? -6.942  6.948   208.039 1.00 65.75  ? 332 PHE B N     1 
ATOM   6313  C CA    . PHE B  1 332 ? -7.726  7.740   208.984 1.00 65.39  ? 332 PHE B CA    1 
ATOM   6314  C C     . PHE B  1 332 ? -9.030  8.220   208.363 1.00 65.53  ? 332 PHE B C     1 
ATOM   6315  O O     . PHE B  1 332 ? -10.040 8.352   209.053 1.00 61.88  ? 332 PHE B O     1 
ATOM   6316  C CB    . PHE B  1 332 ? -6.923  8.935   209.501 1.00 62.50  ? 332 PHE B CB    1 
ATOM   6317  C CG    . PHE B  1 332 ? -6.117  8.633   210.730 1.00 68.24  ? 332 PHE B CG    1 
ATOM   6318  C CD1   . PHE B  1 332 ? -5.777  7.328   211.043 1.00 66.08  ? 332 PHE B CD1   1 
ATOM   6319  C CD2   . PHE B  1 332 ? -5.716  9.649   211.583 1.00 61.84  ? 332 PHE B CD2   1 
ATOM   6320  C CE1   . PHE B  1 332 ? -5.040  7.040   212.174 1.00 62.06  ? 332 PHE B CE1   1 
ATOM   6321  C CE2   . PHE B  1 332 ? -4.978  9.367   212.719 1.00 58.73  ? 332 PHE B CE2   1 
ATOM   6322  C CZ    . PHE B  1 332 ? -4.641  8.060   213.014 1.00 62.54  ? 332 PHE B CZ    1 
ATOM   6323  N N     . ALA B  1 333 ? -9.007  8.485   207.062 1.00 64.52  ? 333 ALA B N     1 
ATOM   6324  C CA    . ALA B  1 333 ? -10.227 8.828   206.348 1.00 66.10  ? 333 ALA B CA    1 
ATOM   6325  C C     . ALA B  1 333 ? -11.160 7.623   206.335 1.00 69.18  ? 333 ALA B C     1 
ATOM   6326  O O     . ALA B  1 333 ? -12.369 7.757   206.518 1.00 68.99  ? 333 ALA B O     1 
ATOM   6327  C CB    . ALA B  1 333 ? -9.912  9.284   204.934 1.00 64.61  ? 333 ALA B CB    1 
ATOM   6328  N N     . TYR B  1 334 ? -10.580 6.444   206.133 1.00 67.98  ? 334 TYR B N     1 
ATOM   6329  C CA    . TYR B  1 334 ? -11.338 5.200   206.098 1.00 69.78  ? 334 TYR B CA    1 
ATOM   6330  C C     . TYR B  1 334 ? -11.967 4.876   207.452 1.00 71.08  ? 334 TYR B C     1 
ATOM   6331  O O     . TYR B  1 334 ? -13.153 4.555   207.532 1.00 70.58  ? 334 TYR B O     1 
ATOM   6332  C CB    . TYR B  1 334 ? -10.437 4.047   205.649 1.00 70.07  ? 334 TYR B CB    1 
ATOM   6333  C CG    . TYR B  1 334 ? -11.080 2.685   205.751 1.00 71.03  ? 334 TYR B CG    1 
ATOM   6334  C CD1   . TYR B  1 334 ? -12.037 2.276   204.833 1.00 76.52  ? 334 TYR B CD1   1 
ATOM   6335  C CD2   . TYR B  1 334 ? -10.731 1.806   206.766 1.00 73.05  ? 334 TYR B CD2   1 
ATOM   6336  C CE1   . TYR B  1 334 ? -12.629 1.028   204.924 1.00 76.23  ? 334 TYR B CE1   1 
ATOM   6337  C CE2   . TYR B  1 334 ? -11.314 0.556   206.866 1.00 76.78  ? 334 TYR B CE2   1 
ATOM   6338  C CZ    . TYR B  1 334 ? -12.264 0.172   205.942 1.00 81.45  ? 334 TYR B CZ    1 
ATOM   6339  O OH    . TYR B  1 334 ? -12.849 -1.072  206.038 1.00 77.99  ? 334 TYR B OH    1 
ATOM   6340  N N     . LEU B  1 335 ? -11.165 4.963   208.511 1.00 69.69  ? 335 LEU B N     1 
ATOM   6341  C CA    . LEU B  1 335 ? -11.638 4.688   209.865 1.00 69.06  ? 335 LEU B CA    1 
ATOM   6342  C C     . LEU B  1 335 ? -12.712 5.681   210.304 1.00 69.18  ? 335 LEU B C     1 
ATOM   6343  O O     . LEU B  1 335 ? -13.537 5.372   211.162 1.00 69.94  ? 335 LEU B O     1 
ATOM   6344  C CB    . LEU B  1 335 ? -10.470 4.716   210.855 1.00 63.49  ? 335 LEU B CB    1 
ATOM   6345  C CG    . LEU B  1 335 ? -9.367  3.667   210.681 1.00 67.62  ? 335 LEU B CG    1 
ATOM   6346  C CD1   . LEU B  1 335 ? -8.189  3.966   211.599 1.00 69.17  ? 335 LEU B CD1   1 
ATOM   6347  C CD2   . LEU B  1 335 ? -9.896  2.264   210.928 1.00 65.18  ? 335 LEU B CD2   1 
ATOM   6348  N N     . ALA B  1 336 ? -12.698 6.872   209.711 1.00 68.78  ? 336 ALA B N     1 
ATOM   6349  C CA    . ALA B  1 336 ? -13.651 7.918   210.071 1.00 71.47  ? 336 ALA B CA    1 
ATOM   6350  C C     . ALA B  1 336 ? -14.999 7.714   209.388 1.00 70.58  ? 336 ALA B C     1 
ATOM   6351  O O     . ALA B  1 336 ? -15.947 8.461   209.632 1.00 73.17  ? 336 ALA B O     1 
ATOM   6352  C CB    . ALA B  1 336 ? -13.088 9.288   209.724 1.00 65.90  ? 336 ALA B CB    1 
ATOM   6353  N N     . GLY B  1 337 ? -15.079 6.700   208.533 1.00 73.51  ? 337 GLY B N     1 
ATOM   6354  C CA    . GLY B  1 337 ? -16.296 6.417   207.796 1.00 72.23  ? 337 GLY B CA    1 
ATOM   6355  C C     . GLY B  1 337 ? -16.443 7.300   206.573 1.00 72.36  ? 337 GLY B C     1 
ATOM   6356  O O     . GLY B  1 337 ? -17.557 7.585   206.134 1.00 75.38  ? 337 GLY B O     1 
ATOM   6357  N N     . LEU B  1 338 ? -15.315 7.735   206.021 1.00 71.21  ? 338 LEU B N     1 
ATOM   6358  C CA    . LEU B  1 338 ? -15.321 8.611   204.854 1.00 75.78  ? 338 LEU B CA    1 
ATOM   6359  C C     . LEU B  1 338 ? -14.917 7.866   203.584 1.00 76.97  ? 338 LEU B C     1 
ATOM   6360  O O     . LEU B  1 338 ? -14.502 6.708   203.633 1.00 79.63  ? 338 LEU B O     1 
ATOM   6361  C CB    . LEU B  1 338 ? -14.387 9.805   205.069 1.00 73.73  ? 338 LEU B CB    1 
ATOM   6362  C CG    . LEU B  1 338 ? -14.681 10.742  206.242 1.00 71.57  ? 338 LEU B CG    1 
ATOM   6363  C CD1   . LEU B  1 338 ? -13.689 11.891  206.257 1.00 71.34  ? 338 LEU B CD1   1 
ATOM   6364  C CD2   . LEU B  1 338 ? -16.103 11.269  206.180 1.00 73.59  ? 338 LEU B CD2   1 
ATOM   6365  N N     . GLU B  1 339 ? -15.042 8.546   202.448 1.00 77.23  ? 339 GLU B N     1 
ATOM   6366  C CA    . GLU B  1 339 ? -14.638 7.988   201.162 1.00 79.43  ? 339 GLU B CA    1 
ATOM   6367  C C     . GLU B  1 339 ? -13.242 8.453   200.774 1.00 82.70  ? 339 GLU B C     1 
ATOM   6368  O O     . GLU B  1 339 ? -12.378 7.647   200.431 1.00 83.72  ? 339 GLU B O     1 
ATOM   6369  C CB    . GLU B  1 339 ? -15.627 8.383   200.063 1.00 84.31  ? 339 GLU B CB    1 
ATOM   6370  C CG    . GLU B  1 339 ? -17.031 7.837   200.235 1.00 89.44  ? 339 GLU B CG    1 
ATOM   6371  C CD    . GLU B  1 339 ? -17.993 8.421   199.220 1.00 97.89  ? 339 GLU B CD    1 
ATOM   6372  O OE1   . GLU B  1 339 ? -17.917 9.643   198.967 1.00 95.96  ? 339 GLU B OE1   1 
ATOM   6373  O OE2   . GLU B  1 339 ? -18.818 7.660   198.670 1.00 105.89 ? 339 GLU B OE2   1 
ATOM   6374  N N     . THR B  1 340 ? -13.031 9.765   200.823 1.00 82.13  ? 340 THR B N     1 
ATOM   6375  C CA    . THR B  1 340 ? -11.780 10.356  200.365 1.00 79.77  ? 340 THR B CA    1 
ATOM   6376  C C     . THR B  1 340 ? -11.075 11.145  201.463 1.00 77.73  ? 340 THR B C     1 
ATOM   6377  O O     . THR B  1 340 ? -11.666 11.463  202.495 1.00 78.20  ? 340 THR B O     1 
ATOM   6378  C CB    . THR B  1 340 ? -12.012 11.286  199.155 1.00 82.08  ? 340 THR B CB    1 
ATOM   6379  O OG1   . THR B  1 340 ? -12.811 12.407  199.552 1.00 87.13  ? 340 THR B OG1   1 
ATOM   6380  C CG2   . THR B  1 340 ? -12.716 10.537  198.034 1.00 85.83  ? 340 THR B CG2   1 
ATOM   6381  N N     . VAL B  1 341 ? -9.803  11.454  201.224 1.00 77.78  ? 341 VAL B N     1 
ATOM   6382  C CA    . VAL B  1 341 ? -8.996  12.240  202.150 1.00 74.96  ? 341 VAL B CA    1 
ATOM   6383  C C     . VAL B  1 341 ? -9.495  13.685  202.213 1.00 78.85  ? 341 VAL B C     1 
ATOM   6384  O O     . VAL B  1 341 ? -9.465  14.317  203.269 1.00 76.93  ? 341 VAL B O     1 
ATOM   6385  C CB    . VAL B  1 341 ? -7.499  12.203  201.743 1.00 72.62  ? 341 VAL B CB    1 
ATOM   6386  C CG1   . VAL B  1 341 ? -6.707  13.318  202.417 1.00 72.76  ? 341 VAL B CG1   1 
ATOM   6387  C CG2   . VAL B  1 341 ? -6.896  10.838  202.062 1.00 74.69  ? 341 VAL B CG2   1 
ATOM   6388  N N     . SER B  1 342 ? -9.982  14.192  201.084 1.00 79.99  ? 342 SER B N     1 
ATOM   6389  C CA    . SER B  1 342 ? -10.439 15.578  200.985 1.00 77.71  ? 342 SER B CA    1 
ATOM   6390  C C     . SER B  1 342 ? -11.595 15.907  201.934 1.00 73.23  ? 342 SER B C     1 
ATOM   6391  O O     . SER B  1 342 ? -11.754 17.054  202.350 1.00 75.87  ? 342 SER B O     1 
ATOM   6392  C CB    . SER B  1 342 ? -10.844 15.893  199.542 1.00 79.50  ? 342 SER B CB    1 
ATOM   6393  O OG    . SER B  1 342 ? -11.475 14.781  198.931 1.00 87.01  ? 342 SER B OG    1 
ATOM   6394  N N     . GLN B  1 343 ? -12.392 14.899  202.277 1.00 74.37  ? 343 GLN B N     1 
ATOM   6395  C CA    . GLN B  1 343 ? -13.522 15.083  203.187 1.00 75.90  ? 343 GLN B CA    1 
ATOM   6396  C C     . GLN B  1 343 ? -13.067 15.339  204.622 1.00 71.03  ? 343 GLN B C     1 
ATOM   6397  O O     . GLN B  1 343 ? -13.844 15.810  205.455 1.00 70.16  ? 343 GLN B O     1 
ATOM   6398  C CB    . GLN B  1 343 ? -14.442 13.864  203.143 1.00 75.68  ? 343 GLN B CB    1 
ATOM   6399  C CG    . GLN B  1 343 ? -15.124 13.654  201.803 1.00 79.70  ? 343 GLN B CG    1 
ATOM   6400  C CD    . GLN B  1 343 ? -15.907 12.358  201.746 1.00 84.91  ? 343 GLN B CD    1 
ATOM   6401  O OE1   . GLN B  1 343 ? -15.335 11.281  201.582 1.00 85.24  ? 343 GLN B OE1   1 
ATOM   6402  N NE2   . GLN B  1 343 ? -17.225 12.456  201.883 1.00 81.14  ? 343 GLN B NE2   1 
ATOM   6403  N N     . LEU B  1 344 ? -11.809 15.015  204.908 1.00 69.71  ? 344 LEU B N     1 
ATOM   6404  C CA    . LEU B  1 344 ? -11.223 15.299  206.212 1.00 63.66  ? 344 LEU B CA    1 
ATOM   6405  C C     . LEU B  1 344 ? -11.129 16.806  206.416 1.00 63.00  ? 344 LEU B C     1 
ATOM   6406  O O     . LEU B  1 344 ? -11.288 17.303  207.529 1.00 60.36  ? 344 LEU B O     1 
ATOM   6407  C CB    . LEU B  1 344 ? -9.838  14.655  206.343 1.00 66.37  ? 344 LEU B CB    1 
ATOM   6408  C CG    . LEU B  1 344 ? -9.771  13.125  206.395 1.00 66.85  ? 344 LEU B CG    1 
ATOM   6409  C CD1   . LEU B  1 344 ? -8.337  12.629  206.279 1.00 57.18  ? 344 LEU B CD1   1 
ATOM   6410  C CD2   . LEU B  1 344 ? -10.408 12.607  207.672 1.00 61.98  ? 344 LEU B CD2   1 
ATOM   6411  N N     . ASN B  1 345 ? -10.891 17.530  205.325 1.00 63.11  ? 345 ASN B N     1 
ATOM   6412  C CA    . ASN B  1 345 ? -10.729 18.979  205.377 1.00 61.63  ? 345 ASN B CA    1 
ATOM   6413  C C     . ASN B  1 345 ? -12.072 19.715  205.400 1.00 63.77  ? 345 ASN B C     1 
ATOM   6414  O O     . ASN B  1 345 ? -12.138 20.918  205.148 1.00 62.56  ? 345 ASN B O     1 
ATOM   6415  C CB    . ASN B  1 345 ? -9.892  19.457  204.187 1.00 60.68  ? 345 ASN B CB    1 
ATOM   6416  C CG    . ASN B  1 345 ? -9.248  20.810  204.429 1.00 65.24  ? 345 ASN B CG    1 
ATOM   6417  O OD1   . ASN B  1 345 ? -8.762  21.095  205.523 1.00 65.41  ? 345 ASN B OD1   1 
ATOM   6418  N ND2   . ASN B  1 345 ? -9.248  21.655  203.403 1.00 67.13  ? 345 ASN B ND2   1 
ATOM   6419  N N     . ASN B  1 346 ? -13.139 18.984  205.708 1.00 64.74  ? 346 ASN B N     1 
ATOM   6420  C CA    . ASN B  1 346 ? -14.472 19.566  205.819 1.00 60.45  ? 346 ASN B CA    1 
ATOM   6421  C C     . ASN B  1 346 ? -14.970 19.505  207.259 1.00 62.85  ? 346 ASN B C     1 
ATOM   6422  O O     . ASN B  1 346 ? -15.472 18.475  207.706 1.00 66.43  ? 346 ASN B O     1 
ATOM   6423  C CB    . ASN B  1 346 ? -15.446 18.845  204.883 1.00 66.08  ? 346 ASN B CB    1 
ATOM   6424  C CG    . ASN B  1 346 ? -16.786 19.554  204.758 1.00 73.02  ? 346 ASN B CG    1 
ATOM   6425  O OD1   . ASN B  1 346 ? -17.363 20.018  205.744 1.00 71.67  ? 346 ASN B OD1   1 
ATOM   6426  N ND2   . ASN B  1 346 ? -17.291 19.634  203.534 1.00 73.54  ? 346 ASN B ND2   1 
ATOM   6427  N N     . ARG B  1 347 ? -14.838 20.619  207.971 1.00 61.46  ? 347 ARG B N     1 
ATOM   6428  C CA    . ARG B  1 347 ? -15.168 20.682  209.393 1.00 62.48  ? 347 ARG B CA    1 
ATOM   6429  C C     . ARG B  1 347 ? -16.671 20.660  209.661 1.00 64.90  ? 347 ARG B C     1 
ATOM   6430  O O     . ARG B  1 347 ? -17.108 20.302  210.755 1.00 67.45  ? 347 ARG B O     1 
ATOM   6431  C CB    . ARG B  1 347 ? -14.559 21.941  210.016 1.00 57.30  ? 347 ARG B CB    1 
ATOM   6432  C CG    . ARG B  1 347 ? -15.188 23.234  209.516 1.00 55.13  ? 347 ARG B CG    1 
ATOM   6433  C CD    . ARG B  1 347 ? -14.422 24.466  209.986 1.00 53.48  ? 347 ARG B CD    1 
ATOM   6434  N NE    . ARG B  1 347 ? -14.467 24.649  211.435 1.00 46.01  ? 347 ARG B NE    1 
ATOM   6435  C CZ    . ARG B  1 347 ? -13.392 24.744  212.213 1.00 46.90  ? 347 ARG B CZ    1 
ATOM   6436  N NH1   . ARG B  1 347 ? -12.178 24.670  211.686 1.00 45.03  ? 347 ARG B NH1   1 
ATOM   6437  N NH2   . ARG B  1 347 ? -13.530 24.915  213.521 1.00 41.91  ? 347 ARG B NH2   1 
ATOM   6438  N N     . PHE B  1 348 ? -17.460 21.043  208.664 1.00 64.53  ? 348 PHE B N     1 
ATOM   6439  C CA    . PHE B  1 348 ? -18.902 21.170  208.840 1.00 68.60  ? 348 PHE B CA    1 
ATOM   6440  C C     . PHE B  1 348 ? -19.652 19.933  208.354 1.00 72.83  ? 348 PHE B C     1 
ATOM   6441  O O     . PHE B  1 348 ? -20.874 19.954  208.202 1.00 73.16  ? 348 PHE B O     1 
ATOM   6442  C CB    . PHE B  1 348 ? -19.400 22.420  208.115 1.00 66.48  ? 348 PHE B CB    1 
ATOM   6443  C CG    . PHE B  1 348 ? -18.803 23.691  208.641 1.00 64.03  ? 348 PHE B CG    1 
ATOM   6444  C CD1   . PHE B  1 348 ? -18.841 23.976  209.994 1.00 62.68  ? 348 PHE B CD1   1 
ATOM   6445  C CD2   . PHE B  1 348 ? -18.176 24.586  207.789 1.00 63.86  ? 348 PHE B CD2   1 
ATOM   6446  C CE1   . PHE B  1 348 ? -18.282 25.139  210.488 1.00 60.40  ? 348 PHE B CE1   1 
ATOM   6447  C CE2   . PHE B  1 348 ? -17.614 25.751  208.278 1.00 65.33  ? 348 PHE B CE2   1 
ATOM   6448  C CZ    . PHE B  1 348 ? -17.669 26.028  209.629 1.00 64.25  ? 348 PHE B CZ    1 
ATOM   6449  N N     . LEU B  1 349 ? -18.910 18.855  208.124 1.00 75.39  ? 349 LEU B N     1 
ATOM   6450  C CA    . LEU B  1 349 ? -19.494 17.596  207.682 1.00 77.90  ? 349 LEU B CA    1 
ATOM   6451  C C     . LEU B  1 349 ? -19.991 16.784  208.873 1.00 83.38  ? 349 LEU B C     1 
ATOM   6452  O O     . LEU B  1 349 ? -19.205 16.390  209.733 1.00 82.44  ? 349 LEU B O     1 
ATOM   6453  C CB    . LEU B  1 349 ? -18.470 16.789  206.880 1.00 78.54  ? 349 LEU B CB    1 
ATOM   6454  C CG    . LEU B  1 349 ? -18.991 15.593  206.084 1.00 88.80  ? 349 LEU B CG    1 
ATOM   6455  C CD1   . LEU B  1 349 ? -20.010 16.049  205.052 1.00 90.33  ? 349 LEU B CD1   1 
ATOM   6456  C CD2   . LEU B  1 349 ? -17.839 14.857  205.415 1.00 85.78  ? 349 LEU B CD2   1 
ATOM   6457  N N     . LYS B  1 350 ? -21.296 16.540  208.928 1.00 87.96  ? 350 LYS B N     1 
ATOM   6458  C CA    . LYS B  1 350 ? -21.867 15.750  210.012 1.00 93.03  ? 350 LYS B CA    1 
ATOM   6459  C C     . LYS B  1 350 ? -22.286 14.370  209.524 1.00 99.90  ? 350 LYS B C     1 
ATOM   6460  O O     . LYS B  1 350 ? -23.309 14.219  208.858 1.00 99.90  ? 350 LYS B O     1 
ATOM   6461  C CB    . LYS B  1 350 ? -23.064 16.468  210.642 1.00 89.38  ? 350 LYS B CB    1 
ATOM   6462  C CG    . LYS B  1 350 ? -22.776 17.887  211.105 1.00 84.75  ? 350 LYS B CG    1 
ATOM   6463  C CD    . LYS B  1 350 ? -23.470 18.182  212.426 1.00 77.55  ? 350 LYS B CD    1 
ATOM   6464  C CE    . LYS B  1 350 ? -23.625 19.679  212.661 1.00 74.41  ? 350 LYS B CE    1 
ATOM   6465  N NZ    . LYS B  1 350 ? -22.345 20.421  212.507 1.00 62.10  ? 350 LYS B NZ    1 
ATOM   6466  N N     . PHE B  1 351 ? -21.483 13.365  209.858 1.00 103.94 ? 351 PHE B N     1 
ATOM   6467  C CA    . PHE B  1 351 ? -21.796 11.985  209.508 1.00 108.72 ? 351 PHE B CA    1 
ATOM   6468  C C     . PHE B  1 351 ? -22.832 11.439  210.482 1.00 107.27 ? 351 PHE B C     1 
ATOM   6469  O O     . PHE B  1 351 ? -23.534 10.470  210.186 1.00 109.55 ? 351 PHE B O     1 
ATOM   6470  C CB    . PHE B  1 351 ? -20.530 11.126  209.513 1.00 114.20 ? 351 PHE B CB    1 
ATOM   6471  C CG    . PHE B  1 351 ? -20.784 9.664   209.275 1.00 123.79 ? 351 PHE B CG    1 
ATOM   6472  C CD1   . PHE B  1 351 ? -21.203 9.210   208.033 1.00 120.79 ? 351 PHE B CD1   1 
ATOM   6473  C CD2   . PHE B  1 351 ? -20.596 8.741   210.290 1.00 119.45 ? 351 PHE B CD2   1 
ATOM   6474  C CE1   . PHE B  1 351 ? -21.434 7.865   207.812 1.00 118.02 ? 351 PHE B CE1   1 
ATOM   6475  C CE2   . PHE B  1 351 ? -20.825 7.396   210.074 1.00 117.13 ? 351 PHE B CE2   1 
ATOM   6476  C CZ    . PHE B  1 351 ? -21.244 6.958   208.834 1.00 115.88 ? 351 PHE B CZ    1 
ATOM   6477  N N     . ASP B  1 352 ? -22.930 12.074  211.645 1.00 102.82 ? 352 ASP B N     1 
ATOM   6478  C CA    . ASP B  1 352 ? -23.963 11.720  212.606 1.00 97.76  ? 352 ASP B CA    1 
ATOM   6479  C C     . ASP B  1 352 ? -24.689 12.953  213.139 1.00 96.38  ? 352 ASP B C     1 
ATOM   6480  O O     . ASP B  1 352 ? -24.114 14.037  213.244 1.00 99.60  ? 352 ASP B O     1 
ATOM   6481  C CB    . ASP B  1 352 ? -23.374 10.929  213.768 1.00 95.00  ? 352 ASP B CB    1 
ATOM   6482  C CG    . ASP B  1 352 ? -24.425 10.536  214.782 1.00 91.56  ? 352 ASP B CG    1 
ATOM   6483  O OD1   . ASP B  1 352 ? -25.333 9.759   214.413 1.00 93.99  ? 352 ASP B OD1   1 
ATOM   6484  O OD2   . ASP B  1 352 ? -24.355 11.005  215.936 1.00 90.02  ? 352 ASP B OD2   1 
ATOM   6485  N N     . GLU B  1 353 ? -25.961 12.768  213.479 1.00 86.97  ? 353 GLU B N     1 
ATOM   6486  C CA    . GLU B  1 353 ? -26.806 13.867  213.915 1.00 83.05  ? 353 GLU B CA    1 
ATOM   6487  C C     . GLU B  1 353 ? -27.688 13.497  215.115 1.00 76.95  ? 353 GLU B C     1 
ATOM   6488  O O     . GLU B  1 353 ? -28.831 13.943  215.202 1.00 76.12  ? 353 GLU B O     1 
ATOM   6489  C CB    . GLU B  1 353 ? -27.692 14.345  212.759 1.00 87.81  ? 353 GLU B CB    1 
ATOM   6490  C CG    . GLU B  1 353 ? -26.948 14.725  211.471 1.00 94.94  ? 353 GLU B CG    1 
ATOM   6491  C CD    . GLU B  1 353 ? -26.599 13.522  210.602 1.00 100.48 ? 353 GLU B CD    1 
ATOM   6492  O OE1   . GLU B  1 353 ? -26.835 12.376  211.041 1.00 101.01 ? 353 GLU B OE1   1 
ATOM   6493  O OE2   . GLU B  1 353 ? -26.086 13.724  209.481 1.00 99.78  ? 353 GLU B OE2   1 
ATOM   6494  N N     . ARG B  1 354 ? -27.163 12.693  216.039 1.00 72.30  ? 354 ARG B N     1 
ATOM   6495  C CA    . ARG B  1 354 ? -27.929 12.284  217.223 1.00 70.60  ? 354 ARG B CA    1 
ATOM   6496  C C     . ARG B  1 354 ? -27.499 13.014  218.485 1.00 62.99  ? 354 ARG B C     1 
ATOM   6497  O O     . ARG B  1 354 ? -26.330 13.357  218.644 1.00 64.79  ? 354 ARG B O     1 
ATOM   6498  C CB    . ARG B  1 354 ? -27.796 10.779  217.462 1.00 75.42  ? 354 ARG B CB    1 
ATOM   6499  C CG    . ARG B  1 354 ? -28.576 9.896   216.506 1.00 73.54  ? 354 ARG B CG    1 
ATOM   6500  C CD    . ARG B  1 354 ? -27.997 8.490   216.510 1.00 75.10  ? 354 ARG B CD    1 
ATOM   6501  N NE    . ARG B  1 354 ? -26.593 8.520   216.112 1.00 82.09  ? 354 ARG B NE    1 
ATOM   6502  C CZ    . ARG B  1 354 ? -25.685 7.617   216.470 1.00 83.27  ? 354 ARG B CZ    1 
ATOM   6503  N NH1   . ARG B  1 354 ? -26.025 6.597   217.245 1.00 83.31  ? 354 ARG B NH1   1 
ATOM   6504  N NH2   . ARG B  1 354 ? -24.432 7.739   216.056 1.00 88.79  ? 354 ARG B NH2   1 
ATOM   6505  N N     . ALA B  1 355 ? -28.448 13.243  219.386 1.00 59.59  ? 355 ALA B N     1 
ATOM   6506  C CA    . ALA B  1 355 ? -28.107 13.607  220.755 1.00 56.84  ? 355 ALA B CA    1 
ATOM   6507  C C     . ALA B  1 355 ? -27.476 12.385  221.405 1.00 65.07  ? 355 ALA B C     1 
ATOM   6508  O O     . ALA B  1 355 ? -27.706 11.260  220.954 1.00 67.72  ? 355 ALA B O     1 
ATOM   6509  C CB    . ALA B  1 355 ? -29.335 14.059  221.526 1.00 55.73  ? 355 ALA B CB    1 
ATOM   6510  N N     . PHE B  1 356 ? -26.676 12.591  222.446 1.00 62.43  ? 356 PHE B N     1 
ATOM   6511  C CA    . PHE B  1 356 ? -26.040 11.466  223.131 1.00 60.36  ? 356 PHE B CA    1 
ATOM   6512  C C     . PHE B  1 356 ? -25.593 11.828  224.536 1.00 57.90  ? 356 PHE B C     1 
ATOM   6513  O O     . PHE B  1 356 ? -25.401 13.001  224.859 1.00 57.48  ? 356 PHE B O     1 
ATOM   6514  C CB    . PHE B  1 356 ? -24.831 10.950  222.333 1.00 51.98  ? 356 PHE B CB    1 
ATOM   6515  C CG    . PHE B  1 356 ? -23.686 11.923  222.258 1.00 59.54  ? 356 PHE B CG    1 
ATOM   6516  C CD1   . PHE B  1 356 ? -22.651 11.882  223.187 1.00 52.87  ? 356 PHE B CD1   1 
ATOM   6517  C CD2   . PHE B  1 356 ? -23.636 12.867  221.246 1.00 56.64  ? 356 PHE B CD2   1 
ATOM   6518  C CE1   . PHE B  1 356 ? -21.601 12.775  223.112 1.00 55.22  ? 356 PHE B CE1   1 
ATOM   6519  C CE2   . PHE B  1 356 ? -22.588 13.760  221.164 1.00 54.40  ? 356 PHE B CE2   1 
ATOM   6520  C CZ    . PHE B  1 356 ? -21.570 13.715  222.098 1.00 50.10  ? 356 PHE B CZ    1 
ATOM   6521  N N     . LYS B  1 357 ? -25.445 10.807  225.371 1.00 57.13  ? 357 LYS B N     1 
ATOM   6522  C CA    . LYS B  1 357 ? -24.725 10.945  226.626 1.00 56.40  ? 357 LYS B CA    1 
ATOM   6523  C C     . LYS B  1 357 ? -23.786 9.758   226.744 1.00 57.52  ? 357 LYS B C     1 
ATOM   6524  O O     . LYS B  1 357 ? -24.067 8.682   226.206 1.00 61.16  ? 357 LYS B O     1 
ATOM   6525  C CB    . LYS B  1 357 ? -25.669 11.011  227.824 1.00 59.44  ? 357 LYS B CB    1 
ATOM   6526  C CG    . LYS B  1 357 ? -24.959 11.361  229.118 1.00 65.67  ? 357 LYS B CG    1 
ATOM   6527  C CD    . LYS B  1 357 ? -25.847 11.112  230.310 1.00 85.75  ? 357 LYS B CD    1 
ATOM   6528  C CE    . LYS B  1 357 ? -25.069 11.244  231.599 1.00 85.09  ? 357 LYS B CE    1 
ATOM   6529  N NZ    . LYS B  1 357 ? -25.978 11.324  232.773 1.00 84.27  ? 357 LYS B NZ    1 
ATOM   6530  N N     . THR B  1 358 ? -22.666 9.949   227.428 1.00 54.76  ? 358 THR B N     1 
ATOM   6531  C CA    . THR B  1 358 ? -21.673 8.893   227.511 1.00 52.89  ? 358 THR B CA    1 
ATOM   6532  C C     . THR B  1 358 ? -20.956 8.886   228.847 1.00 53.57  ? 358 THR B C     1 
ATOM   6533  O O     . THR B  1 358 ? -20.911 9.893   229.553 1.00 57.54  ? 358 THR B O     1 
ATOM   6534  C CB    . THR B  1 358 ? -20.631 9.021   226.389 1.00 51.01  ? 358 THR B CB    1 
ATOM   6535  O OG1   . THR B  1 358 ? -19.597 8.052   226.588 1.00 59.66  ? 358 THR B OG1   1 
ATOM   6536  C CG2   . THR B  1 358 ? -20.020 10.404  226.403 1.00 51.89  ? 358 THR B CG2   1 
ATOM   6537  N N     . LYS B  1 359 ? -20.403 7.729   229.187 1.00 50.98  ? 359 LYS B N     1 
ATOM   6538  C CA    . LYS B  1 359 ? -19.569 7.590   230.369 1.00 50.91  ? 359 LYS B CA    1 
ATOM   6539  C C     . LYS B  1 359 ? -18.365 6.740   229.994 1.00 54.58  ? 359 LYS B C     1 
ATOM   6540  O O     . LYS B  1 359 ? -18.316 6.181   228.900 1.00 54.85  ? 359 LYS B O     1 
ATOM   6541  C CB    . LYS B  1 359 ? -20.345 6.962   231.527 1.00 57.47  ? 359 LYS B CB    1 
ATOM   6542  C CG    . LYS B  1 359 ? -21.581 7.752   231.944 1.00 60.10  ? 359 LYS B CG    1 
ATOM   6543  C CD    . LYS B  1 359 ? -22.180 7.211   233.227 1.00 63.89  ? 359 LYS B CD    1 
ATOM   6544  C CE    . LYS B  1 359 ? -21.336 7.589   234.431 1.00 65.55  ? 359 LYS B CE    1 
ATOM   6545  N NZ    . LYS B  1 359 ? -21.601 8.971   234.906 1.00 63.31  ? 359 LYS B NZ    1 
ATOM   6546  N N     . VAL B  1 360 ? -17.391 6.644   230.891 1.00 54.32  ? 360 VAL B N     1 
ATOM   6547  C CA    . VAL B  1 360 ? -16.173 5.915   230.576 1.00 49.16  ? 360 VAL B CA    1 
ATOM   6548  C C     . VAL B  1 360 ? -15.560 5.286   231.822 1.00 50.36  ? 360 VAL B C     1 
ATOM   6549  O O     . VAL B  1 360 ? -15.674 5.816   232.928 1.00 52.42  ? 360 VAL B O     1 
ATOM   6550  C CB    . VAL B  1 360 ? -15.135 6.838   229.881 1.00 50.64  ? 360 VAL B CB    1 
ATOM   6551  C CG1   . VAL B  1 360 ? -14.589 7.867   230.855 1.00 50.28  ? 360 VAL B CG1   1 
ATOM   6552  C CG2   . VAL B  1 360 ? -14.009 6.022   229.261 1.00 49.16  ? 360 VAL B CG2   1 
ATOM   6553  N N     . ASP B  1 361 ? -14.937 4.129   231.633 1.00 50.01  ? 361 ASP B N     1 
ATOM   6554  C CA    . ASP B  1 361 ? -14.189 3.479   232.695 1.00 55.75  ? 361 ASP B CA    1 
ATOM   6555  C C     . ASP B  1 361 ? -12.767 3.204   232.231 1.00 53.77  ? 361 ASP B C     1 
ATOM   6556  O O     . ASP B  1 361 ? -12.505 3.077   231.035 1.00 51.86  ? 361 ASP B O     1 
ATOM   6557  C CB    . ASP B  1 361 ? -14.868 2.178   233.124 1.00 54.85  ? 361 ASP B CB    1 
ATOM   6558  C CG    . ASP B  1 361 ? -15.903 2.391   234.212 1.00 62.81  ? 361 ASP B CG    1 
ATOM   6559  O OD1   . ASP B  1 361 ? -15.630 3.170   235.150 1.00 63.96  ? 361 ASP B OD1   1 
ATOM   6560  O OD2   . ASP B  1 361 ? -16.993 1.785   234.132 1.00 59.12  ? 361 ASP B OD2   1 
ATOM   6561  N N     . LEU B  1 362 ? -11.847 3.133   233.182 1.00 56.24  ? 362 LEU B N     1 
ATOM   6562  C CA    . LEU B  1 362 ? -10.492 2.698   232.890 1.00 55.61  ? 362 LEU B CA    1 
ATOM   6563  C C     . LEU B  1 362 ? -10.164 1.538   233.818 1.00 58.87  ? 362 LEU B C     1 
ATOM   6564  O O     . LEU B  1 362 ? -10.489 1.572   235.001 1.00 62.02  ? 362 LEU B O     1 
ATOM   6565  C CB    . LEU B  1 362 ? -9.500  3.851   233.046 1.00 54.44  ? 362 LEU B CB    1 
ATOM   6566  C CG    . LEU B  1 362 ? -9.718  4.979   232.031 1.00 53.49  ? 362 LEU B CG    1 
ATOM   6567  C CD1   . LEU B  1 362 ? -9.863  6.318   232.732 1.00 55.96  ? 362 LEU B CD1   1 
ATOM   6568  C CD2   . LEU B  1 362 ? -8.595  5.022   231.000 1.00 50.07  ? 362 LEU B CD2   1 
ATOM   6569  N N     . THR B  1 363 ? -9.547  0.499   233.271 1.00 57.44  ? 363 THR B N     1 
ATOM   6570  C CA    . THR B  1 363 ? -9.317  -0.724  234.029 1.00 60.03  ? 363 THR B CA    1 
ATOM   6571  C C     . THR B  1 363 ? -7.852  -0.895  234.403 1.00 65.59  ? 363 THR B C     1 
ATOM   6572  O O     . THR B  1 363 ? -6.960  -0.458  233.676 1.00 59.39  ? 363 THR B O     1 
ATOM   6573  C CB    . THR B  1 363 ? -9.771  -1.961  233.237 1.00 60.71  ? 363 THR B CB    1 
ATOM   6574  O OG1   . THR B  1 363 ? -8.919  -2.136  232.097 1.00 56.04  ? 363 THR B OG1   1 
ATOM   6575  C CG2   . THR B  1 363 ? -11.212 -1.797  232.770 1.00 56.19  ? 363 THR B CG2   1 
ATOM   6576  N N     . LYS B  1 364 ? -7.612  -1.531  235.545 1.00 68.31  ? 364 LYS B N     1 
ATOM   6577  C CA    . LYS B  1 364 ? -6.260  -1.889  235.956 1.00 68.21  ? 364 LYS B CA    1 
ATOM   6578  C C     . LYS B  1 364 ? -6.118  -3.405  235.966 1.00 69.89  ? 364 LYS B C     1 
ATOM   6579  O O     . LYS B  1 364 ? -5.055  -3.942  235.652 1.00 74.58  ? 364 LYS B O     1 
ATOM   6580  C CB    . LYS B  1 364 ? -5.932  -1.314  237.337 1.00 71.92  ? 364 LYS B CB    1 
ATOM   6581  C CG    . LYS B  1 364 ? -6.061  0.199   237.423 1.00 71.37  ? 364 LYS B CG    1 
ATOM   6582  C CD    . LYS B  1 364 ? -5.151  0.905   236.426 1.00 74.76  ? 364 LYS B CD    1 
ATOM   6583  C CE    . LYS B  1 364 ? -3.706  0.920   236.897 1.00 80.88  ? 364 LYS B CE    1 
ATOM   6584  N NZ    . LYS B  1 364 ? -2.830  1.788   236.058 1.00 81.99  ? 364 LYS B NZ    1 
ATOM   6585  N N     . GLU B  1 365 ? -7.198  -4.091  236.327 1.00 70.17  ? 365 GLU B N     1 
ATOM   6586  C CA    . GLU B  1 365 ? -7.210  -5.549  236.339 1.00 72.67  ? 365 GLU B CA    1 
ATOM   6587  C C     . GLU B  1 365 ? -8.053  -6.092  235.190 1.00 70.65  ? 365 GLU B C     1 
ATOM   6588  O O     . GLU B  1 365 ? -9.013  -5.444  234.768 1.00 65.39  ? 365 GLU B O     1 
ATOM   6589  C CB    . GLU B  1 365 ? -7.735  -6.073  237.682 1.00 71.55  ? 365 GLU B CB    1 
ATOM   6590  C CG    . GLU B  1 365 ? -6.892  -5.672  238.886 1.00 77.51  ? 365 GLU B CG    1 
ATOM   6591  C CD    . GLU B  1 365 ? -5.475  -6.221  238.829 1.00 79.35  ? 365 GLU B CD    1 
ATOM   6592  O OE1   . GLU B  1 365 ? -5.216  -7.149  238.031 1.00 84.07  ? 365 GLU B OE1   1 
ATOM   6593  O OE2   . GLU B  1 365 ? -4.616  -5.725  239.588 1.00 83.83  ? 365 GLU B OE2   1 
ATOM   6594  N N     . PRO B  1 366 ? -7.691  -7.280  234.673 1.00 68.03  ? 366 PRO B N     1 
ATOM   6595  C CA    . PRO B  1 366 ? -8.436  -7.912  233.577 1.00 70.08  ? 366 PRO B CA    1 
ATOM   6596  C C     . PRO B  1 366 ? -9.925  -8.044  233.889 1.00 67.63  ? 366 PRO B C     1 
ATOM   6597  O O     . PRO B  1 366 ? -10.284 -8.223  235.052 1.00 69.15  ? 366 PRO B O     1 
ATOM   6598  C CB    . PRO B  1 366 ? -7.783  -9.291  233.463 1.00 69.55  ? 366 PRO B CB    1 
ATOM   6599  C CG    . PRO B  1 366 ? -6.397  -9.089  233.965 1.00 67.43  ? 366 PRO B CG    1 
ATOM   6600  C CD    . PRO B  1 366 ? -6.516  -8.077  235.071 1.00 71.84  ? 366 PRO B CD    1 
ATOM   6601  N N     . LEU B  1 367 ? -10.779 -7.942  232.876 1.00 68.23  ? 367 LEU B N     1 
ATOM   6602  C CA    . LEU B  1 367 ? -12.212 -8.120  233.090 1.00 74.14  ? 367 LEU B CA    1 
ATOM   6603  C C     . LEU B  1 367 ? -12.575 -9.602  233.067 1.00 75.71  ? 367 LEU B C     1 
ATOM   6604  O O     . LEU B  1 367 ? -12.164 -10.333 232.167 1.00 73.13  ? 367 LEU B O     1 
ATOM   6605  C CB    . LEU B  1 367 ? -13.025 -7.342  232.045 1.00 71.56  ? 367 LEU B CB    1 
ATOM   6606  C CG    . LEU B  1 367 ? -12.945 -5.819  232.216 1.00 70.33  ? 367 LEU B CG    1 
ATOM   6607  C CD1   . LEU B  1 367 ? -13.924 -5.063  231.322 1.00 62.75  ? 367 LEU B CD1   1 
ATOM   6608  C CD2   . LEU B  1 367 ? -13.156 -5.452  233.675 1.00 72.57  ? 367 LEU B CD2   1 
ATOM   6609  N N     . PRO B  1 368 ? -13.345 -10.049 234.070 1.00 79.48  ? 368 PRO B N     1 
ATOM   6610  C CA    . PRO B  1 368 ? -13.765 -11.452 234.119 1.00 80.85  ? 368 PRO B CA    1 
ATOM   6611  C C     . PRO B  1 368 ? -14.847 -11.748 233.090 1.00 82.67  ? 368 PRO B C     1 
ATOM   6612  O O     . PRO B  1 368 ? -15.748 -10.926 232.906 1.00 81.86  ? 368 PRO B O     1 
ATOM   6613  C CB    . PRO B  1 368 ? -14.297 -11.606 235.546 1.00 84.62  ? 368 PRO B CB    1 
ATOM   6614  C CG    . PRO B  1 368 ? -14.802 -10.258 235.896 1.00 83.01  ? 368 PRO B CG    1 
ATOM   6615  C CD    . PRO B  1 368 ? -13.950 -9.251  235.153 1.00 80.46  ? 368 PRO B CD    1 
ATOM   6616  N N     . SER B  1 369 ? -14.746 -12.906 232.441 1.00 86.92  ? 369 SER B N     1 
ATOM   6617  C CA    . SER B  1 369 ? -15.713 -13.364 231.439 1.00 80.66  ? 369 SER B CA    1 
ATOM   6618  C C     . SER B  1 369 ? -17.167 -12.974 231.739 1.00 76.16  ? 369 SER B C     1 
ATOM   6619  O O     . SER B  1 369 ? -17.927 -12.653 230.835 1.00 73.80  ? 369 SER B O     1 
ATOM   6620  C CB    . SER B  1 369 ? -15.610 -14.884 231.297 1.00 76.93  ? 369 SER B CB    1 
ATOM   6621  O OG    . SER B  1 369 ? -15.870 -15.522 232.536 1.00 82.03  ? 369 SER B OG    1 
ATOM   6622  N N     . LYS B  1 370 ? -17.541 -12.976 233.014 1.00 78.42  ? 370 LYS B N     1 
ATOM   6623  C CA    . LYS B  1 370 ? -18.892 -12.584 233.418 1.00 80.00  ? 370 LYS B CA    1 
ATOM   6624  C C     . LYS B  1 370 ? -19.174 -11.081 233.265 1.00 80.10  ? 370 LYS B C     1 
ATOM   6625  O O     . LYS B  1 370 ? -20.309 -10.692 232.996 1.00 76.97  ? 370 LYS B O     1 
ATOM   6626  C CB    . LYS B  1 370 ? -19.145 -13.006 234.867 1.00 79.35  ? 370 LYS B CB    1 
ATOM   6627  C CG    . LYS B  1 370 ? -18.008 -12.655 235.803 1.00 78.42  ? 370 LYS B CG    1 
ATOM   6628  C CD    . LYS B  1 370 ? -18.408 -12.858 237.247 1.00 77.35  ? 370 LYS B CD    1 
ATOM   6629  C CE    . LYS B  1 370 ? -17.197 -12.746 238.149 1.00 88.12  ? 370 LYS B CE    1 
ATOM   6630  N NZ    . LYS B  1 370 ? -17.538 -12.077 239.430 1.00 96.26  ? 370 LYS B NZ    1 
ATOM   6631  N N     . ALA B  1 371 ? -18.154 -10.242 233.440 1.00 77.15  ? 371 ALA B N     1 
ATOM   6632  C CA    . ALA B  1 371 ? -18.320 -8.790  233.306 1.00 75.90  ? 371 ALA B CA    1 
ATOM   6633  C C     . ALA B  1 371 ? -18.777 -8.394  231.900 1.00 74.06  ? 371 ALA B C     1 
ATOM   6634  O O     . ALA B  1 371 ? -19.734 -7.631  231.739 1.00 74.98  ? 371 ALA B O     1 
ATOM   6635  C CB    . ALA B  1 371 ? -17.024 -8.072  233.654 1.00 76.78  ? 371 ALA B CB    1 
ATOM   6636  N N     . PHE B  1 372 ? -18.068 -8.898  230.893 1.00 73.51  ? 372 PHE B N     1 
ATOM   6637  C CA    . PHE B  1 372 ? -18.460 -8.735  229.497 1.00 73.06  ? 372 PHE B CA    1 
ATOM   6638  C C     . PHE B  1 372 ? -19.856 -9.303  229.266 1.00 74.91  ? 372 PHE B C     1 
ATOM   6639  O O     . PHE B  1 372 ? -20.694 -8.679  228.610 1.00 76.12  ? 372 PHE B O     1 
ATOM   6640  C CB    . PHE B  1 372 ? -17.458 -9.427  228.567 1.00 74.82  ? 372 PHE B CB    1 
ATOM   6641  C CG    . PHE B  1 372 ? -16.082 -8.825  228.591 1.00 74.91  ? 372 PHE B CG    1 
ATOM   6642  C CD1   . PHE B  1 372 ? -15.895 -7.484  228.289 1.00 70.75  ? 372 PHE B CD1   1 
ATOM   6643  C CD2   . PHE B  1 372 ? -14.971 -9.605  228.880 1.00 74.77  ? 372 PHE B CD2   1 
ATOM   6644  C CE1   . PHE B  1 372 ? -14.631 -6.925  228.298 1.00 69.94  ? 372 PHE B CE1   1 
ATOM   6645  C CE2   . PHE B  1 372 ? -13.702 -9.053  228.889 1.00 72.21  ? 372 PHE B CE2   1 
ATOM   6646  C CZ    . PHE B  1 372 ? -13.533 -7.711  228.596 1.00 72.52  ? 372 PHE B CZ    1 
ATOM   6647  N N     . TYR B  1 373 ? -20.085 -10.498 229.804 1.00 76.89  ? 373 TYR B N     1 
ATOM   6648  C CA    . TYR B  1 373 ? -21.374 -11.172 229.712 1.00 78.63  ? 373 TYR B CA    1 
ATOM   6649  C C     . TYR B  1 373 ? -22.516 -10.261 230.148 1.00 75.42  ? 373 TYR B C     1 
ATOM   6650  O O     . TYR B  1 373 ? -23.448 -10.011 229.386 1.00 77.67  ? 373 TYR B O     1 
ATOM   6651  C CB    . TYR B  1 373 ? -21.366 -12.444 230.562 1.00 82.24  ? 373 TYR B CB    1 
ATOM   6652  C CG    . TYR B  1 373 ? -22.501 -13.386 230.250 1.00 85.23  ? 373 TYR B CG    1 
ATOM   6653  C CD1   . TYR B  1 373 ? -22.404 -14.290 229.202 1.00 87.34  ? 373 TYR B CD1   1 
ATOM   6654  C CD2   . TYR B  1 373 ? -23.673 -13.367 230.995 1.00 87.18  ? 373 TYR B CD2   1 
ATOM   6655  C CE1   . TYR B  1 373 ? -23.439 -15.153 228.904 1.00 93.74  ? 373 TYR B CE1   1 
ATOM   6656  C CE2   . TYR B  1 373 ? -24.716 -14.227 230.704 1.00 92.81  ? 373 TYR B CE2   1 
ATOM   6657  C CZ    . TYR B  1 373 ? -24.593 -15.118 229.657 1.00 96.98  ? 373 TYR B CZ    1 
ATOM   6658  O OH    . TYR B  1 373 ? -25.624 -15.980 229.359 1.00 98.63  ? 373 TYR B OH    1 
ATOM   6659  N N     . GLY B  1 374 ? -22.425 -9.761  231.376 1.00 73.79  ? 374 GLY B N     1 
ATOM   6660  C CA    . GLY B  1 374 ? -23.406 -8.830  231.897 1.00 74.85  ? 374 GLY B CA    1 
ATOM   6661  C C     . GLY B  1 374 ? -23.535 -7.578  231.047 1.00 77.29  ? 374 GLY B C     1 
ATOM   6662  O O     . GLY B  1 374 ? -24.647 -7.129  230.761 1.00 80.28  ? 374 GLY B O     1 
ATOM   6663  N N     . LEU B  1 375 ? -22.396 -7.015  230.650 1.00 76.30  ? 375 LEU B N     1 
ATOM   6664  C CA    . LEU B  1 375 ? -22.366 -5.827  229.802 1.00 76.41  ? 375 LEU B CA    1 
ATOM   6665  C C     . LEU B  1 375 ? -23.108 -6.054  228.495 1.00 72.96  ? 375 LEU B C     1 
ATOM   6666  O O     . LEU B  1 375 ? -24.005 -5.293  228.128 1.00 68.24  ? 375 LEU B O     1 
ATOM   6667  C CB    . LEU B  1 375 ? -20.926 -5.417  229.498 1.00 74.54  ? 375 LEU B CB    1 
ATOM   6668  C CG    . LEU B  1 375 ? -20.816 -4.200  228.574 1.00 70.07  ? 375 LEU B CG    1 
ATOM   6669  C CD1   . LEU B  1 375 ? -21.391 -2.978  229.263 1.00 60.13  ? 375 LEU B CD1   1 
ATOM   6670  C CD2   . LEU B  1 375 ? -19.385 -3.947  228.115 1.00 68.87  ? 375 LEU B CD2   1 
ATOM   6671  N N     . LEU B  1 376 ? -22.712 -7.112  227.797 1.00 76.10  ? 376 LEU B N     1 
ATOM   6672  C CA    . LEU B  1 376 ? -23.301 -7.460  226.514 1.00 77.33  ? 376 LEU B CA    1 
ATOM   6673  C C     . LEU B  1 376 ? -24.785 -7.789  226.650 1.00 76.74  ? 376 LEU B C     1 
ATOM   6674  O O     . LEU B  1 376 ? -25.557 -7.578  225.717 1.00 83.15  ? 376 LEU B O     1 
ATOM   6675  C CB    . LEU B  1 376 ? -22.546 -8.637  225.895 1.00 77.16  ? 376 LEU B CB    1 
ATOM   6676  C CG    . LEU B  1 376 ? -21.111 -8.327  225.465 1.00 73.58  ? 376 LEU B CG    1 
ATOM   6677  C CD1   . LEU B  1 376 ? -20.301 -9.601  225.267 1.00 72.73  ? 376 LEU B CD1   1 
ATOM   6678  C CD2   . LEU B  1 376 ? -21.118 -7.486  224.199 1.00 71.68  ? 376 LEU B CD2   1 
ATOM   6679  N N     . GLU B  1 377 ? -25.182 -8.291  227.814 1.00 77.75  ? 377 GLU B N     1 
ATOM   6680  C CA    . GLU B  1 377 ? -26.581 -8.622  228.056 1.00 83.58  ? 377 GLU B CA    1 
ATOM   6681  C C     . GLU B  1 377 ? -27.442 -7.367  228.096 1.00 82.05  ? 377 GLU B C     1 
ATOM   6682  O O     . GLU B  1 377 ? -28.509 -7.312  227.485 1.00 82.52  ? 377 GLU B O     1 
ATOM   6683  C CB    . GLU B  1 377 ? -26.730 -9.401  229.365 1.00 89.00  ? 377 GLU B CB    1 
ATOM   6684  C CG    . GLU B  1 377 ? -28.063 -10.114 229.515 1.00 93.49  ? 377 GLU B CG    1 
ATOM   6685  C CD    . GLU B  1 377 ? -28.121 -10.976 230.760 1.00 96.92  ? 377 GLU B CD    1 
ATOM   6686  O OE1   . GLU B  1 377 ? -27.994 -10.425 231.873 1.00 99.15  ? 377 GLU B OE1   1 
ATOM   6687  O OE2   . GLU B  1 377 ? -28.288 -12.207 230.626 1.00 98.46  ? 377 GLU B OE2   1 
ATOM   6688  N N     . ARG B  1 378 ? -26.963 -6.358  228.813 1.00 79.03  ? 378 ARG B N     1 
ATOM   6689  C CA    . ARG B  1 378 ? -27.710 -5.121  229.001 1.00 80.78  ? 378 ARG B CA    1 
ATOM   6690  C C     . ARG B  1 378 ? -27.689 -4.260  227.751 1.00 78.10  ? 378 ARG B C     1 
ATOM   6691  O O     . ARG B  1 378 ? -28.563 -3.420  227.550 1.00 79.08  ? 378 ARG B O     1 
ATOM   6692  C CB    . ARG B  1 378 ? -27.147 -4.346  230.191 1.00 76.11  ? 378 ARG B CB    1 
ATOM   6693  C CG    . ARG B  1 378 ? -27.223 -5.140  231.472 1.00 79.83  ? 378 ARG B CG    1 
ATOM   6694  C CD    . ARG B  1 378 ? -26.690 -4.392  232.677 1.00 79.53  ? 378 ARG B CD    1 
ATOM   6695  N NE    . ARG B  1 378 ? -26.851 -5.191  233.889 1.00 83.56  ? 378 ARG B NE    1 
ATOM   6696  C CZ    . ARG B  1 378 ? -26.089 -6.233  234.200 1.00 79.32  ? 378 ARG B CZ    1 
ATOM   6697  N NH1   . ARG B  1 378 ? -25.113 -6.598  233.391 1.00 80.35  ? 378 ARG B NH1   1 
ATOM   6698  N NH2   . ARG B  1 378 ? -26.305 -6.914  235.316 1.00 79.67  ? 378 ARG B NH2   1 
ATOM   6699  N N     . LEU B  1 379 ? -26.686 -4.477  226.910 1.00 80.11  ? 379 LEU B N     1 
ATOM   6700  C CA    . LEU B  1 379 ? -26.576 -3.742  225.658 1.00 79.38  ? 379 LEU B CA    1 
ATOM   6701  C C     . LEU B  1 379 ? -27.717 -4.120  224.724 1.00 82.51  ? 379 LEU B C     1 
ATOM   6702  O O     . LEU B  1 379 ? -28.305 -3.264  224.066 1.00 84.04  ? 379 LEU B O     1 
ATOM   6703  C CB    . LEU B  1 379 ? -25.229 -4.021  224.993 1.00 73.10  ? 379 LEU B CB    1 
ATOM   6704  C CG    . LEU B  1 379 ? -24.750 -3.065  223.906 1.00 74.70  ? 379 LEU B CG    1 
ATOM   6705  C CD1   . LEU B  1 379 ? -24.565 -1.662  224.471 1.00 69.67  ? 379 LEU B CD1   1 
ATOM   6706  C CD2   . LEU B  1 379 ? -23.451 -3.597  223.329 1.00 71.25  ? 379 LEU B CD2   1 
ATOM   6707  N N     . SER B  1 380 ? -28.022 -5.412  224.678 1.00 86.07  ? 380 SER B N     1 
ATOM   6708  C CA    . SER B  1 380 ? -29.080 -5.924  223.818 1.00 88.29  ? 380 SER B CA    1 
ATOM   6709  C C     . SER B  1 380 ? -30.454 -5.420  224.219 1.00 86.95  ? 380 SER B C     1 
ATOM   6710  O O     . SER B  1 380 ? -31.339 -5.264  223.379 1.00 90.58  ? 380 SER B O     1 
ATOM   6711  C CB    . SER B  1 380 ? -29.068 -7.444  223.829 1.00 89.97  ? 380 SER B CB    1 
ATOM   6712  O OG    . SER B  1 380 ? -28.021 -7.949  223.017 1.00 88.88  ? 380 SER B OG    1 
ATOM   6713  N N     . LYS B  1 381 ? -30.625 -5.157  225.509 1.00 86.36  ? 381 LYS B N     1 
ATOM   6714  C CA    . LYS B  1 381 ? -31.897 -4.676  226.031 1.00 88.24  ? 381 LYS B CA    1 
ATOM   6715  C C     . LYS B  1 381 ? -32.076 -3.180  225.746 1.00 87.12  ? 381 LYS B C     1 
ATOM   6716  O O     . LYS B  1 381 ? -32.962 -2.529  226.302 1.00 82.58  ? 381 LYS B O     1 
ATOM   6717  C CB    . LYS B  1 381 ? -31.982 -4.981  227.529 1.00 91.78  ? 381 LYS B CB    1 
ATOM   6718  C CG    . LYS B  1 381 ? -31.695 -6.453  227.826 1.00 88.52  ? 381 LYS B CG    1 
ATOM   6719  C CD    . LYS B  1 381 ? -31.534 -6.767  229.305 1.00 91.29  ? 381 LYS B CD    1 
ATOM   6720  C CE    . LYS B  1 381 ? -31.338 -8.267  229.509 1.00 91.92  ? 381 LYS B CE    1 
ATOM   6721  N NZ    . LYS B  1 381 ? -31.028 -8.644  230.917 1.00 91.90  ? 381 LYS B NZ    1 
ATOM   6722  N N     . GLU B  1 382 ? -31.241 -2.653  224.853 1.00 90.03  ? 382 GLU B N     1 
ATOM   6723  C CA    . GLU B  1 382 ? -31.279 -1.243  224.480 1.00 84.54  ? 382 GLU B CA    1 
ATOM   6724  C C     . GLU B  1 382 ? -30.571 -0.999  223.144 1.00 80.25  ? 382 GLU B C     1 
ATOM   6725  O O     . GLU B  1 382 ? -29.342 -0.933  223.089 1.00 78.08  ? 382 GLU B O     1 
ATOM   6726  C CB    . GLU B  1 382 ? -30.647 -0.389  225.582 1.00 83.41  ? 382 GLU B CB    1 
ATOM   6727  C CG    . GLU B  1 382 ? -30.557 1.089   225.252 1.00 80.90  ? 382 GLU B CG    1 
ATOM   6728  C CD    . GLU B  1 382 ? -31.847 1.632   224.670 1.00 80.90  ? 382 GLU B CD    1 
ATOM   6729  O OE1   . GLU B  1 382 ? -32.820 1.816   225.431 1.00 88.07  ? 382 GLU B OE1   1 
ATOM   6730  O OE2   . GLU B  1 382 ? -31.888 1.868   223.446 1.00 79.02  ? 382 GLU B OE2   1 
ATOM   6731  N N     . PRO B  1 383 ? -31.352 -0.854  222.062 1.00 78.69  ? 383 PRO B N     1 
ATOM   6732  C CA    . PRO B  1 383 ? -30.818 -0.687  220.705 1.00 77.98  ? 383 PRO B CA    1 
ATOM   6733  C C     . PRO B  1 383 ? -30.062 0.625   220.509 1.00 72.54  ? 383 PRO B C     1 
ATOM   6734  O O     . PRO B  1 383 ? -29.277 0.736   219.569 1.00 68.78  ? 383 PRO B O     1 
ATOM   6735  C CB    . PRO B  1 383 ? -32.074 -0.718  219.823 1.00 79.30  ? 383 PRO B CB    1 
ATOM   6736  C CG    . PRO B  1 383 ? -33.150 -1.305  220.681 1.00 82.39  ? 383 PRO B CG    1 
ATOM   6737  C CD    . PRO B  1 383 ? -32.824 -0.877  222.071 1.00 79.03  ? 383 PRO B CD    1 
ATOM   6738  N N     . ASN B  1 384 ? -30.300 1.605   221.374 1.00 71.35  ? 384 ASN B N     1 
ATOM   6739  C CA    . ASN B  1 384 ? -29.616 2.888   221.255 1.00 81.39  ? 384 ASN B CA    1 
ATOM   6740  C C     . ASN B  1 384 ? -28.331 2.959   222.076 1.00 72.38  ? 384 ASN B C     1 
ATOM   6741  O O     . ASN B  1 384 ? -27.671 3.999   222.122 1.00 68.30  ? 384 ASN B O     1 
ATOM   6742  C CB    . ASN B  1 384 ? -30.554 4.029   221.656 1.00 75.69  ? 384 ASN B CB    1 
ATOM   6743  C CG    . ASN B  1 384 ? -31.582 4.338   220.584 1.00 77.36  ? 384 ASN B CG    1 
ATOM   6744  O OD1   . ASN B  1 384 ? -31.499 3.827   219.467 1.00 78.23  ? 384 ASN B OD1   1 
ATOM   6745  N ND2   . ASN B  1 384 ? -32.547 5.189   220.911 1.00 78.96  ? 384 ASN B ND2   1 
ATOM   6746  N N     . GLY B  1 385 ? -27.977 1.848   222.712 1.00 71.30  ? 385 GLY B N     1 
ATOM   6747  C CA    . GLY B  1 385 ? -26.756 1.771   223.486 1.00 66.07  ? 385 GLY B CA    1 
ATOM   6748  C C     . GLY B  1 385 ? -25.592 1.279   222.653 1.00 65.53  ? 385 GLY B C     1 
ATOM   6749  O O     . GLY B  1 385 ? -25.753 0.537   221.682 1.00 62.94  ? 385 GLY B O     1 
ATOM   6750  N N     . PHE B  1 386 ? -24.404 1.723   223.031 1.00 68.02  ? 386 PHE B N     1 
ATOM   6751  C CA    . PHE B  1 386 ? -23.178 1.275   222.396 1.00 62.89  ? 386 PHE B CA    1 
ATOM   6752  C C     . PHE B  1 386 ? -22.101 1.159   223.455 1.00 62.95  ? 386 PHE B C     1 
ATOM   6753  O O     . PHE B  1 386 ? -22.241 1.673   224.554 1.00 63.31  ? 386 PHE B O     1 
ATOM   6754  C CB    . PHE B  1 386 ? -22.729 2.245   221.296 1.00 65.70  ? 386 PHE B CB    1 
ATOM   6755  C CG    . PHE B  1 386 ? -23.719 2.407   220.180 1.00 67.25  ? 386 PHE B CG    1 
ATOM   6756  C CD1   . PHE B  1 386 ? -23.624 1.645   219.028 1.00 69.24  ? 386 PHE B CD1   1 
ATOM   6757  C CD2   . PHE B  1 386 ? -24.739 3.337   220.279 1.00 65.87  ? 386 PHE B CD2   1 
ATOM   6758  C CE1   . PHE B  1 386 ? -24.539 1.802   217.997 1.00 67.35  ? 386 PHE B CE1   1 
ATOM   6759  C CE2   . PHE B  1 386 ? -25.657 3.499   219.259 1.00 70.01  ? 386 PHE B CE2   1 
ATOM   6760  C CZ    . PHE B  1 386 ? -25.557 2.732   218.115 1.00 71.23  ? 386 PHE B CZ    1 
ATOM   6761  N N     . ILE B  1 387 ? -21.024 0.480   223.111 1.00 62.45  ? 387 ILE B N     1 
ATOM   6762  C CA    . ILE B  1 387 ? -19.826 0.540   223.896 1.00 62.47  ? 387 ILE B CA    1 
ATOM   6763  C C     . ILE B  1 387 ? -18.716 1.001   222.959 1.00 62.96  ? 387 ILE B C     1 
ATOM   6764  O O     . ILE B  1 387 ? -18.951 1.299   221.800 1.00 70.38  ? 387 ILE B O     1 
ATOM   6765  C CB    . ILE B  1 387 ? -19.482 -0.824  224.553 1.00 61.06  ? 387 ILE B CB    1 
ATOM   6766  C CG1   . ILE B  1 387 ? -19.554 -1.974  223.534 1.00 62.38  ? 387 ILE B CG1   1 
ATOM   6767  C CG2   . ILE B  1 387 ? -20.435 -1.127  225.697 1.00 60.18  ? 387 ILE B CG2   1 
ATOM   6768  C CD1   . ILE B  1 387 ? -19.279 -3.333  224.150 1.00 57.50  ? 387 ILE B CD1   1 
ATOM   6769  N N     . ALA B  1 388 ? -17.510 1.073   223.499 1.00 58.56  ? 388 ALA B N     1 
ATOM   6770  C CA    . ALA B  1 388 ? -16.280 1.278   222.728 1.00 54.43  ? 388 ALA B CA    1 
ATOM   6771  C C     . ALA B  1 388 ? -15.092 0.911   223.596 1.00 53.00  ? 388 ALA B C     1 
ATOM   6772  O O     . ALA B  1 388 ? -14.946 1.411   224.711 1.00 54.49  ? 388 ALA B O     1 
ATOM   6773  C CB    . ALA B  1 388 ? -16.144 2.697   222.219 1.00 55.24  ? 388 ALA B CB    1 
ATOM   6774  N N     . LEU B  1 389 ? -14.253 0.021   223.084 1.00 53.27  ? 389 LEU B N     1 
ATOM   6775  C CA    . LEU B  1 389 ? -13.182 -0.532  223.883 1.00 52.26  ? 389 LEU B CA    1 
ATOM   6776  C C     . LEU B  1 389 ? -11.829 -0.282  223.233 1.00 54.19  ? 389 LEU B C     1 
ATOM   6777  O O     . LEU B  1 389 ? -11.653 -0.470  222.030 1.00 54.67  ? 389 LEU B O     1 
ATOM   6778  C CB    . LEU B  1 389 ? -13.417 -2.028  224.091 1.00 52.47  ? 389 LEU B CB    1 
ATOM   6779  C CG    . LEU B  1 389 ? -14.815 -2.449  224.557 1.00 55.56  ? 389 LEU B CG    1 
ATOM   6780  C CD1   . LEU B  1 389 ? -15.055 -3.908  224.232 1.00 61.90  ? 389 LEU B CD1   1 
ATOM   6781  C CD2   . LEU B  1 389 ? -14.995 -2.209  226.042 1.00 55.59  ? 389 LEU B CD2   1 
ATOM   6782  N N     . ASN B  1 390 ? -10.875 0.155   224.041 1.00 47.32  ? 390 ASN B N     1 
ATOM   6783  C CA    . ASN B  1 390 ? -9.513  0.358   223.572 1.00 52.57  ? 390 ASN B CA    1 
ATOM   6784  C C     . ASN B  1 390 ? -8.497  -0.203  224.554 1.00 47.62  ? 390 ASN B C     1 
ATOM   6785  O O     . ASN B  1 390 ? -8.639  -0.052  225.766 1.00 48.99  ? 390 ASN B O     1 
ATOM   6786  C CB    . ASN B  1 390 ? -9.240  1.843   223.327 1.00 53.70  ? 390 ASN B CB    1 
ATOM   6787  C CG    . ASN B  1 390 ? -9.887  2.351   222.054 1.00 51.11  ? 390 ASN B CG    1 
ATOM   6788  O OD1   . ASN B  1 390 ? -9.313  2.247   220.970 1.00 59.14  ? 390 ASN B OD1   1 
ATOM   6789  N ND2   . ASN B  1 390 ? -11.084 2.912   222.180 1.00 49.74  ? 390 ASN B ND2   1 
ATOM   6790  N N     . GLY B  1 391 ? -7.479  -0.864  224.022 1.00 47.16  ? 391 GLY B N     1 
ATOM   6791  C CA    . GLY B  1 391 ? -6.400  -1.355  224.850 1.00 52.08  ? 391 GLY B CA    1 
ATOM   6792  C C     . GLY B  1 391 ? -5.320  -0.302  224.976 1.00 51.77  ? 391 GLY B C     1 
ATOM   6793  O O     . GLY B  1 391 ? -5.016  0.399   224.013 1.00 52.25  ? 391 GLY B O     1 
ATOM   6794  N N     . PHE B  1 392 ? -4.752  -0.168  226.167 1.00 56.18  ? 392 PHE B N     1 
ATOM   6795  C CA    . PHE B  1 392 ? -3.591  0.690   226.328 1.00 53.69  ? 392 PHE B CA    1 
ATOM   6796  C C     . PHE B  1 392 ? -2.342  -0.149  226.100 1.00 52.78  ? 392 PHE B C     1 
ATOM   6797  O O     . PHE B  1 392 ? -2.252  -0.878  225.110 1.00 54.51  ? 392 PHE B O     1 
ATOM   6798  C CB    . PHE B  1 392 ? -3.568  1.356   227.705 1.00 56.54  ? 392 PHE B CB    1 
ATOM   6799  C CG    . PHE B  1 392 ? -4.502  2.530   227.830 1.00 54.53  ? 392 PHE B CG    1 
ATOM   6800  C CD1   . PHE B  1 392 ? -5.470  2.773   226.869 1.00 55.94  ? 392 PHE B CD1   1 
ATOM   6801  C CD2   . PHE B  1 392 ? -4.401  3.400   228.902 1.00 53.44  ? 392 PHE B CD2   1 
ATOM   6802  C CE1   . PHE B  1 392 ? -6.327  3.852   226.982 1.00 53.59  ? 392 PHE B CE1   1 
ATOM   6803  C CE2   . PHE B  1 392 ? -5.255  4.483   229.022 1.00 52.17  ? 392 PHE B CE2   1 
ATOM   6804  C CZ    . PHE B  1 392 ? -6.220  4.709   228.060 1.00 53.52  ? 392 PHE B CZ    1 
ATOM   6805  N N     . GLY B  1 393 ? -1.388  -0.062  227.019 1.00 56.64  ? 393 GLY B N     1 
ATOM   6806  C CA    . GLY B  1 393 ? -0.125  -0.749  226.842 1.00 53.69  ? 393 GLY B CA    1 
ATOM   6807  C C     . GLY B  1 393 ? 0.691   -0.028  225.791 1.00 53.95  ? 393 GLY B C     1 
ATOM   6808  O O     . GLY B  1 393 ? 0.372   1.103   225.425 1.00 51.16  ? 393 GLY B O     1 
ATOM   6809  N N     . GLY B  1 394 ? 1.735   -0.682  225.294 1.00 49.51  ? 394 GLY B N     1 
ATOM   6810  C CA    . GLY B  1 394 ? 2.629   -0.056  224.337 1.00 52.24  ? 394 GLY B CA    1 
ATOM   6811  C C     . GLY B  1 394 ? 3.279   1.175   224.938 1.00 53.66  ? 394 GLY B C     1 
ATOM   6812  O O     . GLY B  1 394 ? 3.738   1.145   226.081 1.00 55.96  ? 394 GLY B O     1 
ATOM   6813  N N     . GLN B  1 395 ? 3.297   2.266   224.178 1.00 51.35  ? 395 GLN B N     1 
ATOM   6814  C CA    . GLN B  1 395 ? 3.897   3.515   224.639 1.00 54.80  ? 395 GLN B CA    1 
ATOM   6815  C C     . GLN B  1 395 ? 3.142   4.116   225.816 1.00 51.10  ? 395 GLN B C     1 
ATOM   6816  O O     . GLN B  1 395 ? 3.704   4.890   226.590 1.00 55.58  ? 395 GLN B O     1 
ATOM   6817  C CB    . GLN B  1 395 ? 3.965   4.530   223.498 1.00 49.57  ? 395 GLN B CB    1 
ATOM   6818  C CG    . GLN B  1 395 ? 5.220   4.419   222.665 1.00 55.30  ? 395 GLN B CG    1 
ATOM   6819  C CD    . GLN B  1 395 ? 6.477   4.577   223.494 1.00 57.04  ? 395 GLN B CD    1 
ATOM   6820  O OE1   . GLN B  1 395 ? 6.653   5.572   224.198 1.00 57.92  ? 395 GLN B OE1   1 
ATOM   6821  N NE2   . GLN B  1 395 ? 7.359   3.589   223.418 1.00 55.67  ? 395 GLN B NE2   1 
ATOM   6822  N N     . MET B  1 396 ? 1.870   3.759   225.948 1.00 50.55  ? 396 MET B N     1 
ATOM   6823  C CA    . MET B  1 396 ? 1.069   4.242   227.063 1.00 52.21  ? 396 MET B CA    1 
ATOM   6824  C C     . MET B  1 396 ? 1.584   3.689   228.390 1.00 54.72  ? 396 MET B C     1 
ATOM   6825  O O     . MET B  1 396 ? 1.339   4.270   229.434 1.00 52.91  ? 396 MET B O     1 
ATOM   6826  C CB    . MET B  1 396 ? -0.405  3.881   226.871 1.00 47.81  ? 396 MET B CB    1 
ATOM   6827  C CG    . MET B  1 396 ? -1.063  4.577   225.685 1.00 54.52  ? 396 MET B CG    1 
ATOM   6828  S SD    . MET B  1 396 ? -1.085  6.379   225.806 1.00 46.26  ? 396 MET B SD    1 
ATOM   6829  C CE    . MET B  1 396 ? -2.236  6.624   227.158 1.00 41.34  ? 396 MET B CE    1 
ATOM   6830  N N     . SER B  1 397 ? 2.306   2.573   228.347 1.00 55.40  ? 397 SER B N     1 
ATOM   6831  C CA    . SER B  1 397 ? 2.913   2.018   229.555 1.00 51.49  ? 397 SER B CA    1 
ATOM   6832  C C     . SER B  1 397 ? 4.309   2.588   229.802 1.00 52.66  ? 397 SER B C     1 
ATOM   6833  O O     . SER B  1 397 ? 4.786   2.603   230.935 1.00 54.92  ? 397 SER B O     1 
ATOM   6834  C CB    . SER B  1 397 ? 2.985   0.492   229.472 1.00 54.55  ? 397 SER B CB    1 
ATOM   6835  O OG    . SER B  1 397 ? 1.700   -0.091  229.581 1.00 56.21  ? 397 SER B OG    1 
ATOM   6836  N N     . LYS B  1 398 ? 4.957   3.057   228.740 1.00 50.25  ? 398 LYS B N     1 
ATOM   6837  C CA    . LYS B  1 398 ? 6.325   3.561   228.835 1.00 53.78  ? 398 LYS B CA    1 
ATOM   6838  C C     . LYS B  1 398 ? 6.387   5.050   229.169 1.00 50.67  ? 398 LYS B C     1 
ATOM   6839  O O     . LYS B  1 398 ? 7.441   5.565   229.552 1.00 53.85  ? 398 LYS B O     1 
ATOM   6840  C CB    . LYS B  1 398 ? 7.076   3.297   227.533 1.00 56.85  ? 398 LYS B CB    1 
ATOM   6841  C CG    . LYS B  1 398 ? 7.424   1.836   227.317 1.00 58.22  ? 398 LYS B CG    1 
ATOM   6842  C CD    . LYS B  1 398 ? 8.017   1.607   225.942 1.00 61.89  ? 398 LYS B CD    1 
ATOM   6843  C CE    . LYS B  1 398 ? 8.464   0.165   225.783 1.00 64.23  ? 398 LYS B CE    1 
ATOM   6844  N NZ    . LYS B  1 398 ? 8.730   -0.182  224.361 1.00 70.65  ? 398 LYS B NZ    1 
ATOM   6845  N N     . ILE B  1 399 ? 5.261   5.738   229.017 1.00 53.30  ? 399 ILE B N     1 
ATOM   6846  C CA    . ILE B  1 399 ? 5.177   7.149   229.362 1.00 48.79  ? 399 ILE B CA    1 
ATOM   6847  C C     . ILE B  1 399 ? 4.824   7.285   230.841 1.00 46.10  ? 399 ILE B C     1 
ATOM   6848  O O     . ILE B  1 399 ? 3.852   6.682   231.303 1.00 49.29  ? 399 ILE B O     1 
ATOM   6849  C CB    . ILE B  1 399 ? 4.133   7.885   228.490 1.00 49.48  ? 399 ILE B CB    1 
ATOM   6850  C CG1   . ILE B  1 399 ? 4.586   7.905   227.031 1.00 46.99  ? 399 ILE B CG1   1 
ATOM   6851  C CG2   . ILE B  1 399 ? 3.920   9.301   228.998 1.00 42.81  ? 399 ILE B CG2   1 
ATOM   6852  C CD1   . ILE B  1 399 ? 3.479   8.208   226.033 1.00 39.81  ? 399 ILE B CD1   1 
ATOM   6853  N N     . SER B  1 400 ? 5.625   8.050   231.583 1.00 45.66  ? 400 SER B N     1 
ATOM   6854  C CA    . SER B  1 400 ? 5.370   8.270   233.008 1.00 47.62  ? 400 SER B CA    1 
ATOM   6855  C C     . SER B  1 400 ? 4.023   8.965   233.214 1.00 51.26  ? 400 SER B C     1 
ATOM   6856  O O     . SER B  1 400 ? 3.578   9.735   232.357 1.00 51.82  ? 400 SER B O     1 
ATOM   6857  C CB    . SER B  1 400 ? 6.495   9.091   233.645 1.00 49.77  ? 400 SER B CB    1 
ATOM   6858  O OG    . SER B  1 400 ? 6.554   10.403  233.111 1.00 57.01  ? 400 SER B OG    1 
ATOM   6859  N N     . SER B  1 401 ? 3.370   8.688   234.340 1.00 52.07  ? 401 SER B N     1 
ATOM   6860  C CA    . SER B  1 401 ? 2.032   9.214   234.602 1.00 51.37  ? 401 SER B CA    1 
ATOM   6861  C C     . SER B  1 401 ? 2.045   10.716  234.886 1.00 51.75  ? 401 SER B C     1 
ATOM   6862  O O     . SER B  1 401 ? 0.986   11.350  234.952 1.00 56.29  ? 401 SER B O     1 
ATOM   6863  C CB    . SER B  1 401 ? 1.385   8.475   235.781 1.00 55.95  ? 401 SER B CB    1 
ATOM   6864  O OG    . SER B  1 401 ? 1.926   8.901   237.021 1.00 65.85  ? 401 SER B OG    1 
ATOM   6865  N N     . ASP B  1 402 ? 3.240   11.277  235.056 1.00 51.15  ? 402 ASP B N     1 
ATOM   6866  C CA    . ASP B  1 402 ? 3.382   12.692  235.369 1.00 52.45  ? 402 ASP B CA    1 
ATOM   6867  C C     . ASP B  1 402 ? 4.031   13.470  234.223 1.00 47.09  ? 402 ASP B C     1 
ATOM   6868  O O     . ASP B  1 402 ? 4.291   14.666  234.353 1.00 49.49  ? 402 ASP B O     1 
ATOM   6869  C CB    . ASP B  1 402 ? 4.190   12.873  236.659 1.00 56.20  ? 402 ASP B CB    1 
ATOM   6870  C CG    . ASP B  1 402 ? 5.644   12.453  236.508 1.00 56.29  ? 402 ASP B CG    1 
ATOM   6871  O OD1   . ASP B  1 402 ? 5.936   11.588  235.654 1.00 62.08  ? 402 ASP B OD1   1 
ATOM   6872  O OD2   . ASP B  1 402 ? 6.492   12.982  237.257 1.00 62.39  ? 402 ASP B OD2   1 
ATOM   6873  N N     . PHE B  1 403 ? 4.288   12.792  233.106 1.00 46.87  ? 403 PHE B N     1 
ATOM   6874  C CA    . PHE B  1 403 ? 4.837   13.458  231.926 1.00 46.15  ? 403 PHE B CA    1 
ATOM   6875  C C     . PHE B  1 403 ? 3.891   14.564  231.464 1.00 46.31  ? 403 PHE B C     1 
ATOM   6876  O O     . PHE B  1 403 ? 4.318   15.681  231.168 1.00 46.87  ? 403 PHE B O     1 
ATOM   6877  C CB    . PHE B  1 403 ? 5.085   12.451  230.796 1.00 47.14  ? 403 PHE B CB    1 
ATOM   6878  C CG    . PHE B  1 403 ? 5.596   13.078  229.527 1.00 49.79  ? 403 PHE B CG    1 
ATOM   6879  C CD1   . PHE B  1 403 ? 6.887   13.577  229.458 1.00 44.71  ? 403 PHE B CD1   1 
ATOM   6880  C CD2   . PHE B  1 403 ? 4.786   13.171  228.406 1.00 46.23  ? 403 PHE B CD2   1 
ATOM   6881  C CE1   . PHE B  1 403 ? 7.361   14.158  228.297 1.00 45.35  ? 403 PHE B CE1   1 
ATOM   6882  C CE2   . PHE B  1 403 ? 5.256   13.753  227.242 1.00 45.19  ? 403 PHE B CE2   1 
ATOM   6883  C CZ    . PHE B  1 403 ? 6.544   14.246  227.188 1.00 46.77  ? 403 PHE B CZ    1 
ATOM   6884  N N     . THR B  1 404 ? 2.603   14.236  231.404 1.00 45.91  ? 404 THR B N     1 
ATOM   6885  C CA    . THR B  1 404 ? 1.541   15.206  231.152 1.00 44.00  ? 404 THR B CA    1 
ATOM   6886  C C     . THR B  1 404 ? 0.416   14.904  232.154 1.00 46.61  ? 404 THR B C     1 
ATOM   6887  O O     . THR B  1 404 ? 0.446   13.851  232.791 1.00 49.15  ? 404 THR B O     1 
ATOM   6888  C CB    . THR B  1 404 ? 1.042   15.141  229.684 1.00 42.34  ? 404 THR B CB    1 
ATOM   6889  O OG1   . THR B  1 404 ? 0.639   13.804  229.356 1.00 46.62  ? 404 THR B OG1   1 
ATOM   6890  C CG2   . THR B  1 404 ? 2.138   15.581  228.727 1.00 44.13  ? 404 THR B CG2   1 
ATOM   6891  N N     . PRO B  1 405 ? -0.551  15.827  232.334 1.00 42.37  ? 405 PRO B N     1 
ATOM   6892  C CA    . PRO B  1 405 ? -1.614  15.618  233.331 1.00 43.30  ? 405 PRO B CA    1 
ATOM   6893  C C     . PRO B  1 405 ? -2.397  14.303  233.215 1.00 45.57  ? 405 PRO B C     1 
ATOM   6894  O O     . PRO B  1 405 ? -2.898  13.823  234.231 1.00 47.76  ? 405 PRO B O     1 
ATOM   6895  C CB    . PRO B  1 405 ? -2.545  16.807  233.088 1.00 37.32  ? 405 PRO B CB    1 
ATOM   6896  C CG    . PRO B  1 405 ? -1.638  17.882  232.642 1.00 40.31  ? 405 PRO B CG    1 
ATOM   6897  C CD    . PRO B  1 405 ? -0.589  17.199  231.796 1.00 38.97  ? 405 PRO B CD    1 
ATOM   6898  N N     . PHE B  1 406 ? -2.510  13.745  232.012 1.00 43.61  ? 406 PHE B N     1 
ATOM   6899  C CA    . PHE B  1 406 ? -3.195  12.464  231.829 1.00 43.89  ? 406 PHE B CA    1 
ATOM   6900  C C     . PHE B  1 406 ? -2.400  11.351  232.506 1.00 46.82  ? 406 PHE B C     1 
ATOM   6901  O O     . PHE B  1 406 ? -1.292  11.028  232.079 1.00 48.96  ? 406 PHE B O     1 
ATOM   6902  C CB    . PHE B  1 406 ? -3.391  12.158  230.341 1.00 40.81  ? 406 PHE B CB    1 
ATOM   6903  C CG    . PHE B  1 406 ? -4.189  10.908  230.071 1.00 41.37  ? 406 PHE B CG    1 
ATOM   6904  C CD1   . PHE B  1 406 ? -5.568  10.965  229.949 1.00 41.55  ? 406 PHE B CD1   1 
ATOM   6905  C CD2   . PHE B  1 406 ? -3.560  9.679   229.927 1.00 42.02  ? 406 PHE B CD2   1 
ATOM   6906  C CE1   . PHE B  1 406 ? -6.307  9.820   229.695 1.00 44.58  ? 406 PHE B CE1   1 
ATOM   6907  C CE2   . PHE B  1 406 ? -4.294  8.531   229.675 1.00 41.32  ? 406 PHE B CE2   1 
ATOM   6908  C CZ    . PHE B  1 406 ? -5.669  8.603   229.558 1.00 46.04  ? 406 PHE B CZ    1 
ATOM   6909  N N     . PRO B  1 407 ? -2.972  10.758  233.565 1.00 50.12  ? 407 PRO B N     1 
ATOM   6910  C CA    . PRO B  1 407 ? -2.239  9.890   234.488 1.00 49.21  ? 407 PRO B CA    1 
ATOM   6911  C C     . PRO B  1 407 ? -2.340  8.395   234.208 1.00 54.34  ? 407 PRO B C     1 
ATOM   6912  O O     . PRO B  1 407 ? -1.628  7.619   234.843 1.00 56.98  ? 407 PRO B O     1 
ATOM   6913  C CB    . PRO B  1 407 ? -2.906  10.204  235.822 1.00 51.67  ? 407 PRO B CB    1 
ATOM   6914  C CG    . PRO B  1 407 ? -4.344  10.398  235.436 1.00 49.45  ? 407 PRO B CG    1 
ATOM   6915  C CD    . PRO B  1 407 ? -4.345  11.006  234.042 1.00 49.76  ? 407 PRO B CD    1 
ATOM   6916  N N     . HIS B  1 408 ? -3.210  7.993   233.291 1.00 51.53  ? 408 HIS B N     1 
ATOM   6917  C CA    . HIS B  1 408 ? -3.510  6.577   233.127 1.00 50.38  ? 408 HIS B CA    1 
ATOM   6918  C C     . HIS B  1 408 ? -2.555  5.907   232.155 1.00 51.10  ? 408 HIS B C     1 
ATOM   6919  O O     . HIS B  1 408 ? -2.857  5.710   230.978 1.00 47.76  ? 408 HIS B O     1 
ATOM   6920  C CB    . HIS B  1 408 ? -4.957  6.417   232.693 1.00 50.83  ? 408 HIS B CB    1 
ATOM   6921  C CG    . HIS B  1 408 ? -5.909  7.158   233.575 1.00 49.65  ? 408 HIS B CG    1 
ATOM   6922  N ND1   . HIS B  1 408 ? -6.859  8.027   233.086 1.00 54.03  ? 408 HIS B ND1   1 
ATOM   6923  C CD2   . HIS B  1 408 ? -6.027  7.188   234.923 1.00 51.86  ? 408 HIS B CD2   1 
ATOM   6924  C CE1   . HIS B  1 408 ? -7.533  8.547   234.096 1.00 54.37  ? 408 HIS B CE1   1 
ATOM   6925  N NE2   . HIS B  1 408 ? -7.052  8.052   235.221 1.00 56.82  ? 408 HIS B NE2   1 
ATOM   6926  N N     . ARG B  1 409 ? -1.393  5.550   232.687 1.00 49.71  ? 409 ARG B N     1 
ATOM   6927  C CA    . ARG B  1 409 ? -0.321  4.983   231.895 1.00 49.73  ? 409 ARG B CA    1 
ATOM   6928  C C     . ARG B  1 409 ? -0.056  3.530   232.289 1.00 55.22  ? 409 ARG B C     1 
ATOM   6929  O O     . ARG B  1 409 ? -0.889  2.656   232.046 1.00 50.63  ? 409 ARG B O     1 
ATOM   6930  C CB    . ARG B  1 409 ? 0.943   5.827   232.052 1.00 50.47  ? 409 ARG B CB    1 
ATOM   6931  C CG    . ARG B  1 409 ? 0.731   7.325   231.819 1.00 51.45  ? 409 ARG B CG    1 
ATOM   6932  C CD    . ARG B  1 409 ? 0.372   7.660   230.372 1.00 46.35  ? 409 ARG B CD    1 
ATOM   6933  N NE    . ARG B  1 409 ? 0.281   9.105   230.162 1.00 49.88  ? 409 ARG B NE    1 
ATOM   6934  C CZ    . ARG B  1 409 ? 0.256   9.691   228.968 1.00 43.11  ? 409 ARG B CZ    1 
ATOM   6935  N NH1   . ARG B  1 409 ? 0.321   8.958   227.866 1.00 39.80  ? 409 ARG B NH1   1 
ATOM   6936  N NH2   . ARG B  1 409 ? 0.176   11.013  228.877 1.00 41.62  ? 409 ARG B NH2   1 
ATOM   6937  N N     . SER B  1 410 ? 1.099   3.279   232.900 1.00 56.89  ? 410 SER B N     1 
ATOM   6938  C CA    . SER B  1 410 ? 1.496   1.923   233.274 1.00 54.65  ? 410 SER B CA    1 
ATOM   6939  C C     . SER B  1 410 ? 0.469   1.269   234.195 1.00 54.83  ? 410 SER B C     1 
ATOM   6940  O O     . SER B  1 410 ? 0.005   1.880   235.158 1.00 54.10  ? 410 SER B O     1 
ATOM   6941  C CB    . SER B  1 410 ? 2.871   1.932   233.944 1.00 57.94  ? 410 SER B CB    1 
ATOM   6942  O OG    . SER B  1 410 ? 3.255   0.625   234.338 1.00 58.85  ? 410 SER B OG    1 
ATOM   6943  N N     . GLY B  1 411 ? 0.111   0.027   233.885 1.00 58.80  ? 411 GLY B N     1 
ATOM   6944  C CA    . GLY B  1 411 ? -0.854  -0.702  234.685 1.00 58.92  ? 411 GLY B CA    1 
ATOM   6945  C C     . GLY B  1 411 ? -2.269  -0.583  234.155 1.00 62.96  ? 411 GLY B C     1 
ATOM   6946  O O     . GLY B  1 411 ? -3.125  -1.410  234.469 1.00 68.33  ? 411 GLY B O     1 
ATOM   6947  N N     . THR B  1 412 ? -2.521  0.450   233.357 1.00 58.98  ? 412 THR B N     1 
ATOM   6948  C CA    . THR B  1 412 ? -3.839  0.644   232.766 1.00 56.94  ? 412 THR B CA    1 
ATOM   6949  C C     . THR B  1 412 ? -3.984  -0.257  231.546 1.00 55.66  ? 412 THR B C     1 
ATOM   6950  O O     . THR B  1 412 ? -3.140  -0.240  230.651 1.00 55.71  ? 412 THR B O     1 
ATOM   6951  C CB    . THR B  1 412 ? -4.076  2.106   232.363 1.00 56.52  ? 412 THR B CB    1 
ATOM   6952  O OG1   . THR B  1 412 ? -3.730  2.966   233.457 1.00 53.36  ? 412 THR B OG1   1 
ATOM   6953  C CG2   . THR B  1 412 ? -5.536  2.321   231.996 1.00 52.67  ? 412 THR B CG2   1 
ATOM   6954  N N     . ARG B  1 413 ? -5.053  -1.046  231.521 1.00 56.27  ? 413 ARG B N     1 
ATOM   6955  C CA    . ARG B  1 413 ? -5.260  -2.024  230.459 1.00 58.36  ? 413 ARG B CA    1 
ATOM   6956  C C     . ARG B  1 413 ? -6.232  -1.533  229.397 1.00 55.30  ? 413 ARG B C     1 
ATOM   6957  O O     . ARG B  1 413 ? -5.895  -1.466  228.214 1.00 56.93  ? 413 ARG B O     1 
ATOM   6958  C CB    . ARG B  1 413 ? -5.771  -3.345  231.039 1.00 61.12  ? 413 ARG B CB    1 
ATOM   6959  C CG    . ARG B  1 413 ? -4.871  -3.959  232.094 1.00 67.96  ? 413 ARG B CG    1 
ATOM   6960  C CD    . ARG B  1 413 ? -5.396  -5.317  232.529 1.00 71.47  ? 413 ARG B CD    1 
ATOM   6961  N NE    . ARG B  1 413 ? -4.589  -5.905  233.595 1.00 74.85  ? 413 ARG B NE    1 
ATOM   6962  C CZ    . ARG B  1 413 ? -3.605  -6.778  233.404 1.00 76.74  ? 413 ARG B CZ    1 
ATOM   6963  N NH1   . ARG B  1 413 ? -2.934  -7.255  234.443 1.00 79.15  ? 413 ARG B NH1   1 
ATOM   6964  N NH2   . ARG B  1 413 ? -3.289  -7.176  232.178 1.00 76.40  ? 413 ARG B NH2   1 
ATOM   6965  N N     . LEU B  1 414 ? -7.444  -1.199  229.821 1.00 50.51  ? 414 LEU B N     1 
ATOM   6966  C CA    . LEU B  1 414 ? -8.503  -0.861  228.881 1.00 54.90  ? 414 LEU B CA    1 
ATOM   6967  C C     . LEU B  1 414 ? -9.169  0.471   229.192 1.00 54.30  ? 414 LEU B C     1 
ATOM   6968  O O     . LEU B  1 414 ? -9.266  0.876   230.350 1.00 54.91  ? 414 LEU B O     1 
ATOM   6969  C CB    . LEU B  1 414 ? -9.571  -1.959  228.868 1.00 54.93  ? 414 LEU B CB    1 
ATOM   6970  C CG    . LEU B  1 414 ? -9.117  -3.403  228.653 1.00 53.77  ? 414 LEU B CG    1 
ATOM   6971  C CD1   . LEU B  1 414 ? -10.296 -4.354  228.773 1.00 55.40  ? 414 LEU B CD1   1 
ATOM   6972  C CD2   . LEU B  1 414 ? -8.429  -3.565  227.308 1.00 55.33  ? 414 LEU B CD2   1 
ATOM   6973  N N     . MET B  1 415 ? -9.623  1.147   228.142 1.00 53.54  ? 415 MET B N     1 
ATOM   6974  C CA    . MET B  1 415 ? -10.575 2.235   228.291 1.00 55.32  ? 415 MET B CA    1 
ATOM   6975  C C     . MET B  1 415 ? -11.914 1.735   227.772 1.00 51.39  ? 415 MET B C     1 
ATOM   6976  O O     . MET B  1 415 ? -12.001 1.232   226.652 1.00 51.88  ? 415 MET B O     1 
ATOM   6977  C CB    . MET B  1 415 ? -10.130 3.487   227.536 1.00 53.67  ? 415 MET B CB    1 
ATOM   6978  C CG    . MET B  1 415 ? -11.039 4.689   227.761 1.00 50.38  ? 415 MET B CG    1 
ATOM   6979  S SD    . MET B  1 415 ? -10.357 6.241   227.149 1.00 55.64  ? 415 MET B SD    1 
ATOM   6980  C CE    . MET B  1 415 ? -10.383 5.941   225.385 1.00 52.39  ? 415 MET B CE    1 
ATOM   6981  N N     . VAL B  1 416 ? -12.950 1.849   228.594 1.00 54.28  ? 416 VAL B N     1 
ATOM   6982  C CA    . VAL B  1 416 ? -14.269 1.360   228.215 1.00 52.82  ? 416 VAL B CA    1 
ATOM   6983  C C     . VAL B  1 416 ? -15.288 2.493   228.188 1.00 50.62  ? 416 VAL B C     1 
ATOM   6984  O O     . VAL B  1 416 ? -15.572 3.102   229.216 1.00 52.65  ? 416 VAL B O     1 
ATOM   6985  C CB    . VAL B  1 416 ? -14.761 0.263   229.178 1.00 53.19  ? 416 VAL B CB    1 
ATOM   6986  C CG1   . VAL B  1 416 ? -16.123 -0.240  228.747 1.00 51.56  ? 416 VAL B CG1   1 
ATOM   6987  C CG2   . VAL B  1 416 ? -13.762 -0.883  229.241 1.00 52.86  ? 416 VAL B CG2   1 
ATOM   6988  N N     . GLU B  1 417 ? -15.836 2.773   227.010 1.00 46.03  ? 417 GLU B N     1 
ATOM   6989  C CA    . GLU B  1 417 ? -16.811 3.849   226.862 1.00 51.38  ? 417 GLU B CA    1 
ATOM   6990  C C     . GLU B  1 417 ? -18.227 3.299   226.744 1.00 53.60  ? 417 GLU B C     1 
ATOM   6991  O O     . GLU B  1 417 ? -18.481 2.417   225.934 1.00 53.03  ? 417 GLU B O     1 
ATOM   6992  C CB    . GLU B  1 417 ? -16.493 4.701   225.631 1.00 51.51  ? 417 GLU B CB    1 
ATOM   6993  C CG    . GLU B  1 417 ? -15.064 5.202   225.559 1.00 53.80  ? 417 GLU B CG    1 
ATOM   6994  C CD    . GLU B  1 417 ? -14.747 5.848   224.224 1.00 55.23  ? 417 GLU B CD    1 
ATOM   6995  O OE1   . GLU B  1 417 ? -15.495 6.755   223.804 1.00 60.40  ? 417 GLU B OE1   1 
ATOM   6996  O OE2   . GLU B  1 417 ? -13.754 5.440   223.588 1.00 56.85  ? 417 GLU B OE2   1 
ATOM   6997  N N     . TYR B  1 418 ? -19.146 3.820   227.551 1.00 53.83  ? 418 TYR B N     1 
ATOM   6998  C CA    . TYR B  1 418 ? -20.556 3.458   227.430 1.00 54.95  ? 418 TYR B CA    1 
ATOM   6999  C C     . TYR B  1 418 ? -21.343 4.634   226.863 1.00 56.11  ? 418 TYR B C     1 
ATOM   7000  O O     . TYR B  1 418 ? -21.394 5.702   227.468 1.00 52.99  ? 418 TYR B O     1 
ATOM   7001  C CB    . TYR B  1 418 ? -21.140 3.037   228.781 1.00 53.31  ? 418 TYR B CB    1 
ATOM   7002  C CG    . TYR B  1 418 ? -20.160 2.342   229.700 1.00 60.14  ? 418 TYR B CG    1 
ATOM   7003  C CD1   . TYR B  1 418 ? -19.901 0.985   229.576 1.00 59.79  ? 418 TYR B CD1   1 
ATOM   7004  C CD2   . TYR B  1 418 ? -19.501 3.047   230.698 1.00 60.68  ? 418 TYR B CD2   1 
ATOM   7005  C CE1   . TYR B  1 418 ? -19.009 0.348   230.420 1.00 57.69  ? 418 TYR B CE1   1 
ATOM   7006  C CE2   . TYR B  1 418 ? -18.606 2.422   231.544 1.00 58.11  ? 418 TYR B CE2   1 
ATOM   7007  C CZ    . TYR B  1 418 ? -18.361 1.072   231.401 1.00 62.01  ? 418 TYR B CZ    1 
ATOM   7008  O OH    . TYR B  1 418 ? -17.470 0.445   232.243 1.00 60.49  ? 418 TYR B OH    1 
ATOM   7009  N N     . ILE B  1 419 ? -21.957 4.434   225.701 1.00 59.86  ? 419 ILE B N     1 
ATOM   7010  C CA    . ILE B  1 419 ? -22.644 5.515   224.998 1.00 55.69  ? 419 ILE B CA    1 
ATOM   7011  C C     . ILE B  1 419 ? -24.099 5.161   224.701 1.00 61.59  ? 419 ILE B C     1 
ATOM   7012  O O     . ILE B  1 419 ? -24.408 4.016   224.378 1.00 63.44  ? 419 ILE B O     1 
ATOM   7013  C CB    . ILE B  1 419 ? -21.926 5.852   223.673 1.00 55.21  ? 419 ILE B CB    1 
ATOM   7014  C CG1   . ILE B  1 419 ? -20.430 6.080   223.919 1.00 53.61  ? 419 ILE B CG1   1 
ATOM   7015  C CG2   . ILE B  1 419 ? -22.555 7.067   223.008 1.00 49.38  ? 419 ILE B CG2   1 
ATOM   7016  C CD1   . ILE B  1 419 ? -19.572 5.936   222.680 1.00 57.08  ? 419 ILE B CD1   1 
ATOM   7017  N N     . VAL B  1 420 ? -24.993 6.137   224.824 1.00 61.28  ? 420 VAL B N     1 
ATOM   7018  C CA    . VAL B  1 420 ? -26.364 5.961   224.358 1.00 64.91  ? 420 VAL B CA    1 
ATOM   7019  C C     . VAL B  1 420 ? -26.764 7.179   223.520 1.00 66.03  ? 420 VAL B C     1 
ATOM   7020  O O     . VAL B  1 420 ? -26.603 8.323   223.944 1.00 62.88  ? 420 VAL B O     1 
ATOM   7021  C CB    . VAL B  1 420 ? -27.357 5.730   225.533 1.00 65.01  ? 420 VAL B CB    1 
ATOM   7022  C CG1   . VAL B  1 420 ? -27.405 6.925   226.483 1.00 65.96  ? 420 VAL B CG1   1 
ATOM   7023  C CG2   . VAL B  1 420 ? -28.741 5.390   225.000 1.00 72.44  ? 420 VAL B CG2   1 
ATOM   7024  N N     . ALA B  1 421 ? -27.248 6.926   222.309 1.00 68.60  ? 421 ALA B N     1 
ATOM   7025  C CA    . ALA B  1 421 ? -27.557 8.001   221.372 1.00 68.72  ? 421 ALA B CA    1 
ATOM   7026  C C     . ALA B  1 421 ? -28.949 7.839   220.782 1.00 73.40  ? 421 ALA B C     1 
ATOM   7027  O O     . ALA B  1 421 ? -29.439 6.722   220.642 1.00 72.85  ? 421 ALA B O     1 
ATOM   7028  C CB    . ALA B  1 421 ? -26.521 8.050   220.262 1.00 68.75  ? 421 ALA B CB    1 
ATOM   7029  N N     . TRP B  1 422 ? -29.578 8.955   220.423 1.00 73.97  ? 422 TRP B N     1 
ATOM   7030  C CA    . TRP B  1 422 ? -30.927 8.923   219.868 1.00 77.51  ? 422 TRP B CA    1 
ATOM   7031  C C     . TRP B  1 422 ? -31.220 10.147  219.004 1.00 78.05  ? 422 TRP B C     1 
ATOM   7032  O O     . TRP B  1 422 ? -30.780 11.251  219.324 1.00 74.60  ? 422 TRP B O     1 
ATOM   7033  C CB    . TRP B  1 422 ? -31.959 8.825   220.997 1.00 76.19  ? 422 TRP B CB    1 
ATOM   7034  C CG    . TRP B  1 422 ? -32.053 10.059  221.860 1.00 76.97  ? 422 TRP B CG    1 
ATOM   7035  C CD1   . TRP B  1 422 ? -32.919 11.103  221.707 1.00 81.46  ? 422 TRP B CD1   1 
ATOM   7036  C CD2   . TRP B  1 422 ? -31.255 10.370  223.011 1.00 75.01  ? 422 TRP B CD2   1 
ATOM   7037  N NE1   . TRP B  1 422 ? -32.710 12.044  222.685 1.00 79.36  ? 422 TRP B NE1   1 
ATOM   7038  C CE2   . TRP B  1 422 ? -31.694 11.618  223.500 1.00 74.39  ? 422 TRP B CE2   1 
ATOM   7039  C CE3   . TRP B  1 422 ? -30.211 9.716   223.674 1.00 73.54  ? 422 TRP B CE3   1 
ATOM   7040  C CZ2   . TRP B  1 422 ? -31.127 12.224  224.619 1.00 75.84  ? 422 TRP B CZ2   1 
ATOM   7041  C CZ3   . TRP B  1 422 ? -29.649 10.320  224.787 1.00 71.74  ? 422 TRP B CZ3   1 
ATOM   7042  C CH2   . TRP B  1 422 ? -30.108 11.561  225.247 1.00 71.88  ? 422 TRP B CH2   1 
ATOM   7043  N N     . ASN B  1 423 ? -31.958 9.959   217.910 1.00 80.82  ? 423 ASN B N     1 
ATOM   7044  C CA    . ASN B  1 423 ? -32.455 11.109  217.155 1.00 84.12  ? 423 ASN B CA    1 
ATOM   7045  C C     . ASN B  1 423 ? -33.652 11.688  217.900 1.00 82.79  ? 423 ASN B C     1 
ATOM   7046  O O     . ASN B  1 423 ? -34.022 11.178  218.956 1.00 79.80  ? 423 ASN B O     1 
ATOM   7047  C CB    . ASN B  1 423 ? -32.812 10.739  215.697 1.00 86.79  ? 423 ASN B CB    1 
ATOM   7048  C CG    . ASN B  1 423 ? -33.971 9.742   215.579 1.00 91.88  ? 423 ASN B CG    1 
ATOM   7049  O OD1   . ASN B  1 423 ? -34.960 9.811   216.307 1.00 94.08  ? 423 ASN B OD1   1 
ATOM   7050  N ND2   . ASN B  1 423 ? -33.851 8.818   214.627 1.00 92.88  ? 423 ASN B ND2   1 
ATOM   7051  N N     . GLN B  1 424 ? -34.262 12.740  217.365 1.00 84.41  ? 424 GLN B N     1 
ATOM   7052  C CA    . GLN B  1 424 ? -35.314 13.437  218.099 1.00 90.97  ? 424 GLN B CA    1 
ATOM   7053  C C     . GLN B  1 424 ? -36.647 12.675  218.122 1.00 91.56  ? 424 GLN B C     1 
ATOM   7054  O O     . GLN B  1 424 ? -37.452 12.861  219.034 1.00 92.71  ? 424 GLN B O     1 
ATOM   7055  C CB    . GLN B  1 424 ? -35.518 14.840  217.523 1.00 95.23  ? 424 GLN B CB    1 
ATOM   7056  C CG    . GLN B  1 424 ? -36.484 15.695  218.333 1.00 103.15 ? 424 GLN B CG    1 
ATOM   7057  C CD    . GLN B  1 424 ? -36.283 17.179  218.114 1.00 112.31 ? 424 GLN B CD    1 
ATOM   7058  O OE1   . GLN B  1 424 ? -35.182 17.702  218.296 1.00 111.64 ? 424 GLN B OE1   1 
ATOM   7059  N NE2   . GLN B  1 424 ? -37.348 17.868  217.724 1.00 115.63 ? 424 GLN B NE2   1 
ATOM   7060  N N     . SER B  1 425 ? -36.878 11.817  217.132 1.00 86.98  ? 425 SER B N     1 
ATOM   7061  C CA    . SER B  1 425 ? -38.085 10.991  217.111 1.00 87.10  ? 425 SER B CA    1 
ATOM   7062  C C     . SER B  1 425 ? -38.224 10.153  218.386 1.00 89.07  ? 425 SER B C     1 
ATOM   7063  O O     . SER B  1 425 ? -39.333 9.874   218.841 1.00 83.86  ? 425 SER B O     1 
ATOM   7064  C CB    . SER B  1 425 ? -38.080 10.079  215.881 1.00 88.97  ? 425 SER B CB    1 
ATOM   7065  O OG    . SER B  1 425 ? -37.196 10.570  214.888 1.00 89.15  ? 425 SER B OG    1 
ATOM   7066  N N     . GLU B  1 426 ? -37.086 9.770   218.959 1.00 89.02  ? 426 GLU B N     1 
ATOM   7067  C CA    . GLU B  1 426 ? -37.037 8.963   220.178 1.00 85.05  ? 426 GLU B CA    1 
ATOM   7068  C C     . GLU B  1 426 ? -36.871 9.804   221.454 1.00 86.30  ? 426 GLU B C     1 
ATOM   7069  O O     . GLU B  1 426 ? -36.510 9.270   222.506 1.00 84.90  ? 426 GLU B O     1 
ATOM   7070  C CB    . GLU B  1 426 ? -35.888 7.945   220.074 1.00 82.08  ? 426 GLU B CB    1 
ATOM   7071  C CG    . GLU B  1 426 ? -35.370 7.767   218.649 1.00 81.18  ? 426 GLU B CG    1 
ATOM   7072  C CD    . GLU B  1 426 ? -34.314 6.685   218.511 1.00 84.72  ? 426 GLU B CD    1 
ATOM   7073  O OE1   . GLU B  1 426 ? -33.113 7.001   218.617 1.00 81.42  ? 426 GLU B OE1   1 
ATOM   7074  O OE2   . GLU B  1 426 ? -34.690 5.520   218.275 1.00 84.63  ? 426 GLU B OE2   1 
ATOM   7075  N N     . GLN B  1 427 ? -37.144 11.106  221.370 1.00 89.25  ? 427 GLN B N     1 
ATOM   7076  C CA    . GLN B  1 427 ? -36.833 12.033  222.467 1.00 92.66  ? 427 GLN B CA    1 
ATOM   7077  C C     . GLN B  1 427 ? -37.572 11.743  223.778 1.00 94.37  ? 427 GLN B C     1 
ATOM   7078  O O     . GLN B  1 427 ? -37.021 11.954  224.861 1.00 96.17  ? 427 GLN B O     1 
ATOM   7079  C CB    . GLN B  1 427 ? -37.131 13.476  222.045 1.00 95.87  ? 427 GLN B CB    1 
ATOM   7080  C CG    . GLN B  1 427 ? -36.602 14.524  223.019 1.00 103.17 ? 427 GLN B CG    1 
ATOM   7081  C CD    . GLN B  1 427 ? -37.512 15.731  223.135 1.00 109.20 ? 427 GLN B CD    1 
ATOM   7082  O OE1   . GLN B  1 427 ? -38.402 15.932  222.309 1.00 108.40 ? 427 GLN B OE1   1 
ATOM   7083  N NE2   . GLN B  1 427 ? -37.299 16.536  224.170 1.00 105.52 ? 427 GLN B NE2   1 
ATOM   7084  N N     . LYS B  1 428 ? -38.815 11.279  223.677 1.00 96.22  ? 428 LYS B N     1 
ATOM   7085  C CA    . LYS B  1 428 ? -39.651 11.031  224.853 1.00 99.88  ? 428 LYS B CA    1 
ATOM   7086  C C     . LYS B  1 428 ? -39.019 10.034  225.824 1.00 97.66  ? 428 LYS B C     1 
ATOM   7087  O O     . LYS B  1 428 ? -39.155 10.170  227.042 1.00 97.23  ? 428 LYS B O     1 
ATOM   7088  C CB    . LYS B  1 428 ? -41.032 10.519  224.429 1.00 105.75 ? 428 LYS B CB    1 
ATOM   7089  C CG    . LYS B  1 428 ? -41.648 11.266  223.259 1.00 110.72 ? 428 LYS B CG    1 
ATOM   7090  C CD    . LYS B  1 428 ? -41.979 12.710  223.604 1.00 117.87 ? 428 LYS B CD    1 
ATOM   7091  C CE    . LYS B  1 428 ? -42.277 13.504  222.342 1.00 114.19 ? 428 LYS B CE    1 
ATOM   7092  N NZ    . LYS B  1 428 ? -43.064 12.693  221.370 1.00 113.45 ? 428 LYS B NZ    1 
ATOM   7093  N N     . LYS B  1 429 ? -38.325 9.038   225.281 1.00 97.61  ? 429 LYS B N     1 
ATOM   7094  C CA    . LYS B  1 429 ? -37.680 8.012   226.098 1.00 99.73  ? 429 LYS B CA    1 
ATOM   7095  C C     . LYS B  1 429 ? -36.358 8.481   226.712 1.00 94.35  ? 429 LYS B C     1 
ATOM   7096  O O     . LYS B  1 429 ? -35.568 7.656   227.161 1.00 92.15  ? 429 LYS B O     1 
ATOM   7097  C CB    . LYS B  1 429 ? -37.426 6.745   225.266 1.00 98.51  ? 429 LYS B CB    1 
ATOM   7098  C CG    . LYS B  1 429 ? -38.670 5.941   224.902 1.00 97.02  ? 429 LYS B CG    1 
ATOM   7099  C CD    . LYS B  1 429 ? -38.388 4.930   223.787 1.00 96.39  ? 429 LYS B CD    1 
ATOM   7100  C CE    . LYS B  1 429 ? -37.287 3.935   224.149 1.00 96.06  ? 429 LYS B CE    1 
ATOM   7101  N NZ    . LYS B  1 429 ? -37.233 2.833   223.141 1.00 92.17  ? 429 LYS B NZ    1 
ATOM   7102  N N     . LYS B  1 430 ? -36.125 9.793   226.733 1.00 96.32  ? 430 LYS B N     1 
ATOM   7103  C CA    . LYS B  1 430 ? -34.858 10.366  227.205 1.00 95.36  ? 430 LYS B CA    1 
ATOM   7104  C C     . LYS B  1 430 ? -34.375 9.769   228.524 1.00 95.68  ? 430 LYS B C     1 
ATOM   7105  O O     . LYS B  1 430 ? -33.225 9.341   228.634 1.00 90.63  ? 430 LYS B O     1 
ATOM   7106  C CB    . LYS B  1 430 ? -34.982 11.886  227.352 1.00 95.94  ? 430 LYS B CB    1 
ATOM   7107  C CG    . LYS B  1 430 ? -33.918 12.523  228.244 1.00 98.30  ? 430 LYS B CG    1 
ATOM   7108  C CD    . LYS B  1 430 ? -33.491 13.885  227.712 1.00 101.91 ? 430 LYS B CD    1 
ATOM   7109  C CE    . LYS B  1 430 ? -32.522 14.590  228.653 1.00 99.30  ? 430 LYS B CE    1 
ATOM   7110  N NZ    . LYS B  1 430 ? -33.215 15.572  229.533 1.00 91.49  ? 430 LYS B NZ    1 
ATOM   7111  N N     . THR B  1 431 ? -35.266 9.730   229.512 1.00 94.49  ? 431 THR B N     1 
ATOM   7112  C CA    . THR B  1 431 ? -34.930 9.206   230.832 1.00 93.58  ? 431 THR B CA    1 
ATOM   7113  C C     . THR B  1 431 ? -34.783 7.684   230.837 1.00 93.04  ? 431 THR B C     1 
ATOM   7114  O O     . THR B  1 431 ? -34.185 7.123   231.751 1.00 91.47  ? 431 THR B O     1 
ATOM   7115  C CB    . THR B  1 431 ? -35.981 9.615   231.889 1.00 94.23  ? 431 THR B CB    1 
ATOM   7116  O OG1   . THR B  1 431 ? -37.298 9.422   231.362 1.00 97.90  ? 431 THR B OG1   1 
ATOM   7117  C CG2   . THR B  1 431 ? -35.806 11.075  232.280 1.00 91.30  ? 431 THR B CG2   1 
ATOM   7118  N N     . GLU B  1 432 ? -35.325 7.014   229.826 1.00 92.62  ? 432 GLU B N     1 
ATOM   7119  C CA    . GLU B  1 432 ? -35.089 5.582   229.687 1.00 94.46  ? 432 GLU B CA    1 
ATOM   7120  C C     . GLU B  1 432 ? -33.613 5.341   229.378 1.00 88.75  ? 432 GLU B C     1 
ATOM   7121  O O     . GLU B  1 432 ? -32.951 4.547   230.047 1.00 86.71  ? 432 GLU B O     1 
ATOM   7122  C CB    . GLU B  1 432 ? -35.971 4.980   228.591 1.00 105.57 ? 432 GLU B CB    1 
ATOM   7123  C CG    . GLU B  1 432 ? -36.677 3.693   228.985 1.00 105.05 ? 432 GLU B CG    1 
ATOM   7124  C CD    . GLU B  1 432 ? -37.485 3.113   227.843 1.00 102.90 ? 432 GLU B CD    1 
ATOM   7125  O OE1   . GLU B  1 432 ? -36.894 2.404   227.003 1.00 101.14 ? 432 GLU B OE1   1 
ATOM   7126  O OE2   . GLU B  1 432 ? -38.708 3.372   227.777 1.00 102.77 ? 432 GLU B OE2   1 
ATOM   7127  N N     . PHE B  1 433 ? -33.110 6.045   228.367 1.00 87.74  ? 433 PHE B N     1 
ATOM   7128  C CA    . PHE B  1 433 ? -31.711 5.948   227.960 1.00 85.62  ? 433 PHE B CA    1 
ATOM   7129  C C     . PHE B  1 433 ? -30.747 6.276   229.103 1.00 78.87  ? 433 PHE B C     1 
ATOM   7130  O O     . PHE B  1 433 ? -29.748 5.582   229.299 1.00 78.23  ? 433 PHE B O     1 
ATOM   7131  C CB    . PHE B  1 433 ? -31.436 6.875   226.776 1.00 83.52  ? 433 PHE B CB    1 
ATOM   7132  C CG    . PHE B  1 433 ? -32.428 6.737   225.652 1.00 83.82  ? 433 PHE B CG    1 
ATOM   7133  C CD1   . PHE B  1 433 ? -32.525 5.557   224.934 1.00 82.84  ? 433 PHE B CD1   1 
ATOM   7134  C CD2   . PHE B  1 433 ? -33.244 7.797   225.298 1.00 86.20  ? 433 PHE B CD2   1 
ATOM   7135  C CE1   . PHE B  1 433 ? -33.431 5.431   223.897 1.00 80.94  ? 433 PHE B CE1   1 
ATOM   7136  C CE2   . PHE B  1 433 ? -34.152 7.678   224.263 1.00 87.42  ? 433 PHE B CE2   1 
ATOM   7137  C CZ    . PHE B  1 433 ? -34.245 6.494   223.560 1.00 85.20  ? 433 PHE B CZ    1 
ATOM   7138  N N     . LEU B  1 434 ? -31.047 7.334   229.853 1.00 78.00  ? 434 LEU B N     1 
ATOM   7139  C CA    . LEU B  1 434 ? -30.190 7.765   230.957 1.00 80.18  ? 434 LEU B CA    1 
ATOM   7140  C C     . LEU B  1 434 ? -30.139 6.740   232.083 1.00 82.83  ? 434 LEU B C     1 
ATOM   7141  O O     . LEU B  1 434 ? -29.085 6.513   232.682 1.00 76.80  ? 434 LEU B O     1 
ATOM   7142  C CB    . LEU B  1 434 ? -30.659 9.113   231.503 1.00 77.84  ? 434 LEU B CB    1 
ATOM   7143  C CG    . LEU B  1 434 ? -30.532 10.282  230.523 1.00 80.25  ? 434 LEU B CG    1 
ATOM   7144  C CD1   . LEU B  1 434 ? -30.600 11.610  231.257 1.00 71.90  ? 434 LEU B CD1   1 
ATOM   7145  C CD2   . LEU B  1 434 ? -29.247 10.177  229.706 1.00 73.02  ? 434 LEU B CD2   1 
ATOM   7146  N N     . ASP B  1 435 ? -31.282 6.127   232.372 1.00 84.33  ? 435 ASP B N     1 
ATOM   7147  C CA    . ASP B  1 435 ? -31.349 5.089   233.390 1.00 78.81  ? 435 ASP B CA    1 
ATOM   7148  C C     . ASP B  1 435 ? -30.577 3.854   232.945 1.00 77.87  ? 435 ASP B C     1 
ATOM   7149  O O     . ASP B  1 435 ? -29.903 3.215   233.755 1.00 76.54  ? 435 ASP B O     1 
ATOM   7150  C CB    . ASP B  1 435 ? -32.802 4.733   233.704 1.00 86.11  ? 435 ASP B CB    1 
ATOM   7151  C CG    . ASP B  1 435 ? -33.404 5.637   234.762 1.00 89.55  ? 435 ASP B CG    1 
ATOM   7152  O OD1   . ASP B  1 435 ? -33.435 5.230   235.942 1.00 91.20  ? 435 ASP B OD1   1 
ATOM   7153  O OD2   . ASP B  1 435 ? -33.837 6.756   234.421 1.00 96.87  ? 435 ASP B OD2   1 
ATOM   7154  N N     . TRP B  1 436 ? -30.672 3.526   231.659 1.00 77.17  ? 436 TRP B N     1 
ATOM   7155  C CA    . TRP B  1 436 ? -29.893 2.428   231.101 1.00 73.19  ? 436 TRP B CA    1 
ATOM   7156  C C     . TRP B  1 436 ? -28.409 2.684   231.305 1.00 78.20  ? 436 TRP B C     1 
ATOM   7157  O O     . TRP B  1 436 ? -27.679 1.828   231.803 1.00 75.88  ? 436 TRP B O     1 
ATOM   7158  C CB    . TRP B  1 436 ? -30.182 2.239   229.613 1.00 73.71  ? 436 TRP B CB    1 
ATOM   7159  C CG    . TRP B  1 436 ? -29.328 1.172   228.992 1.00 80.74  ? 436 TRP B CG    1 
ATOM   7160  C CD1   . TRP B  1 436 ? -29.598 -0.164  228.941 1.00 81.40  ? 436 TRP B CD1   1 
ATOM   7161  C CD2   . TRP B  1 436 ? -28.056 1.349   228.352 1.00 78.71  ? 436 TRP B CD2   1 
ATOM   7162  N NE1   . TRP B  1 436 ? -28.579 -0.829  228.304 1.00 80.19  ? 436 TRP B NE1   1 
ATOM   7163  C CE2   . TRP B  1 436 ? -27.620 0.077   227.933 1.00 76.74  ? 436 TRP B CE2   1 
ATOM   7164  C CE3   . TRP B  1 436 ? -27.247 2.459   228.091 1.00 78.70  ? 436 TRP B CE3   1 
ATOM   7165  C CZ2   . TRP B  1 436 ? -26.412 -0.116  227.265 1.00 74.29  ? 436 TRP B CZ2   1 
ATOM   7166  C CZ3   . TRP B  1 436 ? -26.046 2.265   227.429 1.00 75.58  ? 436 TRP B CZ3   1 
ATOM   7167  C CH2   . TRP B  1 436 ? -25.641 0.987   227.024 1.00 75.25  ? 436 TRP B CH2   1 
ATOM   7168  N N     . LEU B  1 437 ? -27.978 3.878   230.911 1.00 77.25  ? 437 LEU B N     1 
ATOM   7169  C CA    . LEU B  1 437 ? -26.589 4.289   231.042 1.00 74.27  ? 437 LEU B CA    1 
ATOM   7170  C C     . LEU B  1 437 ? -26.138 4.227   232.496 1.00 72.92  ? 437 LEU B C     1 
ATOM   7171  O O     . LEU B  1 437 ? -25.039 3.764   232.799 1.00 72.72  ? 437 LEU B O     1 
ATOM   7172  C CB    . LEU B  1 437 ? -26.408 5.700   230.491 1.00 72.00  ? 437 LEU B CB    1 
ATOM   7173  C CG    . LEU B  1 437 ? -24.975 6.124   230.171 1.00 67.00  ? 437 LEU B CG    1 
ATOM   7174  C CD1   . LEU B  1 437 ? -24.450 5.330   228.988 1.00 64.54  ? 437 LEU B CD1   1 
ATOM   7175  C CD2   . LEU B  1 437 ? -24.912 7.617   229.900 1.00 65.08  ? 437 LEU B CD2   1 
ATOM   7176  N N     . GLU B  1 438 ? -27.004 4.691   233.390 1.00 74.87  ? 438 GLU B N     1 
ATOM   7177  C CA    . GLU B  1 438 ? -26.718 4.689   234.818 1.00 76.47  ? 438 GLU B CA    1 
ATOM   7178  C C     . GLU B  1 438 ? -26.559 3.267   235.354 1.00 79.96  ? 438 GLU B C     1 
ATOM   7179  O O     . GLU B  1 438 ? -25.737 3.011   236.232 1.00 78.40  ? 438 GLU B O     1 
ATOM   7180  C CB    . GLU B  1 438 ? -27.829 5.417   235.575 1.00 77.03  ? 438 GLU B CB    1 
ATOM   7181  C CG    . GLU B  1 438 ? -27.504 5.739   237.018 1.00 83.09  ? 438 GLU B CG    1 
ATOM   7182  C CD    . GLU B  1 438 ? -28.692 6.321   237.756 1.00 92.19  ? 438 GLU B CD    1 
ATOM   7183  O OE1   . GLU B  1 438 ? -29.709 6.624   237.098 1.00 89.12  ? 438 GLU B OE1   1 
ATOM   7184  O OE2   . GLU B  1 438 ? -28.609 6.472   238.993 1.00 99.98  ? 438 GLU B OE2   1 
ATOM   7185  N N     . LYS B  1 439 ? -27.349 2.349   234.808 1.00 78.48  ? 439 LYS B N     1 
ATOM   7186  C CA    . LYS B  1 439 ? -27.361 0.960   235.256 1.00 79.53  ? 439 LYS B CA    1 
ATOM   7187  C C     . LYS B  1 439 ? -26.106 0.204   234.826 1.00 79.53  ? 439 LYS B C     1 
ATOM   7188  O O     . LYS B  1 439 ? -25.473 -0.474  235.638 1.00 77.19  ? 439 LYS B O     1 
ATOM   7189  C CB    . LYS B  1 439 ? -28.610 0.259   234.728 1.00 80.97  ? 439 LYS B CB    1 
ATOM   7190  C CG    . LYS B  1 439 ? -28.601 -1.247  234.872 1.00 83.49  ? 439 LYS B CG    1 
ATOM   7191  C CD    . LYS B  1 439 ? -29.816 -1.843  234.184 1.00 92.27  ? 439 LYS B CD    1 
ATOM   7192  C CE    . LYS B  1 439 ? -29.920 -3.335  234.434 1.00 88.09  ? 439 LYS B CE    1 
ATOM   7193  N NZ    . LYS B  1 439 ? -31.183 -3.895  233.876 1.00 93.15  ? 439 LYS B NZ    1 
ATOM   7194  N N     . VAL B  1 440 ? -25.764 0.318   233.545 1.00 78.36  ? 440 VAL B N     1 
ATOM   7195  C CA    . VAL B  1 440 ? -24.537 -0.254  232.998 1.00 76.51  ? 440 VAL B CA    1 
ATOM   7196  C C     . VAL B  1 440 ? -23.320 0.192   233.799 1.00 73.41  ? 440 VAL B C     1 
ATOM   7197  O O     . VAL B  1 440 ? -22.429 -0.602  234.104 1.00 73.24  ? 440 VAL B O     1 
ATOM   7198  C CB    . VAL B  1 440 ? -24.349 0.153   231.523 1.00 75.52  ? 440 VAL B CB    1 
ATOM   7199  C CG1   . VAL B  1 440 ? -22.999 -0.311  231.002 1.00 72.30  ? 440 VAL B CG1   1 
ATOM   7200  C CG2   . VAL B  1 440 ? -25.480 -0.397  230.674 1.00 76.16  ? 440 VAL B CG2   1 
ATOM   7201  N N     . TYR B  1 441 ? -23.309 1.473   234.145 1.00 73.93  ? 441 TYR B N     1 
ATOM   7202  C CA    . TYR B  1 441 ? -22.213 2.069   234.892 1.00 72.65  ? 441 TYR B CA    1 
ATOM   7203  C C     . TYR B  1 441 ? -22.138 1.544   236.323 1.00 71.79  ? 441 TYR B C     1 
ATOM   7204  O O     . TYR B  1 441 ? -21.053 1.258   236.834 1.00 71.65  ? 441 TYR B O     1 
ATOM   7205  C CB    . TYR B  1 441 ? -22.355 3.589   234.903 1.00 68.89  ? 441 TYR B CB    1 
ATOM   7206  C CG    . TYR B  1 441 ? -21.094 4.299   235.314 1.00 66.76  ? 441 TYR B CG    1 
ATOM   7207  C CD1   . TYR B  1 441 ? -20.009 4.370   234.452 1.00 64.71  ? 441 TYR B CD1   1 
ATOM   7208  C CD2   . TYR B  1 441 ? -20.985 4.896   236.561 1.00 68.54  ? 441 TYR B CD2   1 
ATOM   7209  C CE1   . TYR B  1 441 ? -18.848 5.017   234.818 1.00 68.08  ? 441 TYR B CE1   1 
ATOM   7210  C CE2   . TYR B  1 441 ? -19.827 5.551   236.937 1.00 71.41  ? 441 TYR B CE2   1 
ATOM   7211  C CZ    . TYR B  1 441 ? -18.762 5.607   236.061 1.00 68.50  ? 441 TYR B CZ    1 
ATOM   7212  O OH    . TYR B  1 441 ? -17.603 6.252   236.425 1.00 69.35  ? 441 TYR B OH    1 
ATOM   7213  N N     . GLU B  1 442 ? -23.293 1.428   236.970 1.00 75.62  ? 442 GLU B N     1 
ATOM   7214  C CA    . GLU B  1 442 ? -23.352 0.889   238.322 1.00 77.90  ? 442 GLU B CA    1 
ATOM   7215  C C     . GLU B  1 442 ? -22.931 -0.575  238.333 1.00 74.40  ? 442 GLU B C     1 
ATOM   7216  O O     . GLU B  1 442 ? -22.252 -1.027  239.256 1.00 74.52  ? 442 GLU B O     1 
ATOM   7217  C CB    . GLU B  1 442 ? -24.758 1.039   238.909 1.00 83.46  ? 442 GLU B CB    1 
ATOM   7218  C CG    . GLU B  1 442 ? -24.919 0.433   240.300 1.00 88.40  ? 442 GLU B CG    1 
ATOM   7219  C CD    . GLU B  1 442 ? -24.114 1.163   241.361 1.00 95.98  ? 442 GLU B CD    1 
ATOM   7220  O OE1   . GLU B  1 442 ? -23.853 0.567   242.427 1.00 101.72 ? 442 GLU B OE1   1 
ATOM   7221  O OE2   . GLU B  1 442 ? -23.748 2.336   241.132 1.00 97.61  ? 442 GLU B OE2   1 
ATOM   7222  N N     . PHE B  1 443 ? -23.331 -1.311  237.300 1.00 73.39  ? 443 PHE B N     1 
ATOM   7223  C CA    . PHE B  1 443 ? -22.996 -2.727  237.193 1.00 74.34  ? 443 PHE B CA    1 
ATOM   7224  C C     . PHE B  1 443 ? -21.492 -2.956  237.103 1.00 73.73  ? 443 PHE B C     1 
ATOM   7225  O O     . PHE B  1 443 ? -20.968 -3.924  237.653 1.00 74.19  ? 443 PHE B O     1 
ATOM   7226  C CB    . PHE B  1 443 ? -23.678 -3.354  235.974 1.00 74.43  ? 443 PHE B CB    1 
ATOM   7227  C CG    . PHE B  1 443 ? -23.131 -4.708  235.607 1.00 75.92  ? 443 PHE B CG    1 
ATOM   7228  C CD1   . PHE B  1 443 ? -23.230 -5.771  236.489 1.00 77.49  ? 443 PHE B CD1   1 
ATOM   7229  C CD2   . PHE B  1 443 ? -22.517 -4.917  234.381 1.00 76.82  ? 443 PHE B CD2   1 
ATOM   7230  C CE1   . PHE B  1 443 ? -22.727 -7.015  236.160 1.00 78.77  ? 443 PHE B CE1   1 
ATOM   7231  C CE2   . PHE B  1 443 ? -22.012 -6.161  234.046 1.00 80.25  ? 443 PHE B CE2   1 
ATOM   7232  C CZ    . PHE B  1 443 ? -22.118 -7.212  234.936 1.00 81.10  ? 443 PHE B CZ    1 
ATOM   7233  N N     . MET B  1 444 ? -20.805 -2.053  236.412 1.00 73.17  ? 444 MET B N     1 
ATOM   7234  C CA    . MET B  1 444 ? -19.390 -2.223  236.104 1.00 70.81  ? 444 MET B CA    1 
ATOM   7235  C C     . MET B  1 444 ? -18.455 -1.859  237.254 1.00 70.75  ? 444 MET B C     1 
ATOM   7236  O O     . MET B  1 444 ? -17.264 -2.166  237.208 1.00 74.16  ? 444 MET B O     1 
ATOM   7237  C CB    . MET B  1 444 ? -19.029 -1.392  234.874 1.00 69.39  ? 444 MET B CB    1 
ATOM   7238  C CG    . MET B  1 444 ? -19.385 -2.064  233.561 1.00 66.29  ? 444 MET B CG    1 
ATOM   7239  S SD    . MET B  1 444 ? -18.672 -3.717  233.454 1.00 80.05  ? 444 MET B SD    1 
ATOM   7240  C CE    . MET B  1 444 ? -18.573 -3.937  231.683 1.00 72.29  ? 444 MET B CE    1 
ATOM   7241  N N     . LYS B  1 445 ? -19.003 -1.214  238.279 1.00 69.97  ? 445 LYS B N     1 
ATOM   7242  C CA    . LYS B  1 445 ? -18.222 -0.753  239.430 1.00 71.23  ? 445 LYS B CA    1 
ATOM   7243  C C     . LYS B  1 445 ? -17.236 -1.779  240.027 1.00 73.80  ? 445 LYS B C     1 
ATOM   7244  O O     . LYS B  1 445 ? -16.096 -1.423  240.323 1.00 74.58  ? 445 LYS B O     1 
ATOM   7245  C CB    . LYS B  1 445 ? -19.173 -0.264  240.528 1.00 69.36  ? 445 LYS B CB    1 
ATOM   7246  C CG    . LYS B  1 445 ? -18.476 0.352   241.722 1.00 75.33  ? 445 LYS B CG    1 
ATOM   7247  C CD    . LYS B  1 445 ? -19.458 0.613   242.851 1.00 78.66  ? 445 LYS B CD    1 
ATOM   7248  C CE    . LYS B  1 445 ? -20.652 1.418   242.363 1.00 84.77  ? 445 LYS B CE    1 
ATOM   7249  N NZ    . LYS B  1 445 ? -21.374 2.092   243.480 1.00 90.49  ? 445 LYS B NZ    1 
ATOM   7250  N N     . PRO B  1 446 ? -17.657 -3.048  240.213 1.00 75.07  ? 446 PRO B N     1 
ATOM   7251  C CA    . PRO B  1 446 ? -16.703 -3.972  240.845 1.00 74.27  ? 446 PRO B CA    1 
ATOM   7252  C C     . PRO B  1 446 ? -15.507 -4.366  239.977 1.00 72.97  ? 446 PRO B C     1 
ATOM   7253  O O     . PRO B  1 446 ? -14.463 -4.733  240.519 1.00 75.60  ? 446 PRO B O     1 
ATOM   7254  C CB    . PRO B  1 446 ? -17.553 -5.216  241.136 1.00 73.86  ? 446 PRO B CB    1 
ATOM   7255  C CG    . PRO B  1 446 ? -18.958 -4.761  241.078 1.00 74.71  ? 446 PRO B CG    1 
ATOM   7256  C CD    . PRO B  1 446 ? -18.988 -3.664  240.071 1.00 72.93  ? 446 PRO B CD    1 
ATOM   7257  N N     . PHE B  1 447 ? -15.657 -4.296  238.659 1.00 72.14  ? 447 PHE B N     1 
ATOM   7258  C CA    . PHE B  1 447 ? -14.650 -4.839  237.751 1.00 74.47  ? 447 PHE B CA    1 
ATOM   7259  C C     . PHE B  1 447 ? -13.606 -3.810  237.329 1.00 73.23  ? 447 PHE B C     1 
ATOM   7260  O O     . PHE B  1 447 ? -12.517 -4.167  236.873 1.00 70.83  ? 447 PHE B O     1 
ATOM   7261  C CB    . PHE B  1 447 ? -15.318 -5.409  236.500 1.00 75.59  ? 447 PHE B CB    1 
ATOM   7262  C CG    . PHE B  1 447 ? -16.553 -6.213  236.784 1.00 75.49  ? 447 PHE B CG    1 
ATOM   7263  C CD1   . PHE B  1 447 ? -16.468 -7.564  237.066 1.00 77.32  ? 447 PHE B CD1   1 
ATOM   7264  C CD2   . PHE B  1 447 ? -17.801 -5.617  236.764 1.00 77.86  ? 447 PHE B CD2   1 
ATOM   7265  C CE1   . PHE B  1 447 ? -17.602 -8.308  237.323 1.00 81.08  ? 447 PHE B CE1   1 
ATOM   7266  C CE2   . PHE B  1 447 ? -18.938 -6.352  237.022 1.00 77.90  ? 447 PHE B CE2   1 
ATOM   7267  C CZ    . PHE B  1 447 ? -18.840 -7.701  237.302 1.00 77.22  ? 447 PHE B CZ    1 
ATOM   7268  N N     . VAL B  1 448 ? -13.946 -2.535  237.476 1.00 72.60  ? 448 VAL B N     1 
ATOM   7269  C CA    . VAL B  1 448 ? -13.109 -1.457  236.963 1.00 69.97  ? 448 VAL B CA    1 
ATOM   7270  C C     . VAL B  1 448 ? -12.242 -0.844  238.052 1.00 72.33  ? 448 VAL B C     1 
ATOM   7271  O O     . VAL B  1 448 ? -12.180 -1.357  239.170 1.00 75.71  ? 448 VAL B O     1 
ATOM   7272  C CB    . VAL B  1 448 ? -13.962 -0.352  236.327 1.00 67.41  ? 448 VAL B CB    1 
ATOM   7273  C CG1   . VAL B  1 448 ? -14.786 -0.917  235.182 1.00 65.88  ? 448 VAL B CG1   1 
ATOM   7274  C CG2   . VAL B  1 448 ? -14.862 0.282   237.371 1.00 68.29  ? 448 VAL B CG2   1 
ATOM   7275  N N     . SER B  1 449 ? -11.570 0.251   237.705 1.00 70.90  ? 449 SER B N     1 
ATOM   7276  C CA    . SER B  1 449 ? -10.789 1.021   238.666 1.00 68.70  ? 449 SER B CA    1 
ATOM   7277  C C     . SER B  1 449 ? -11.665 1.438   239.837 1.00 68.15  ? 449 SER B C     1 
ATOM   7278  O O     . SER B  1 449 ? -12.848 1.739   239.666 1.00 69.81  ? 449 SER B O     1 
ATOM   7279  C CB    . SER B  1 449 ? -10.170 2.259   238.014 1.00 70.05  ? 449 SER B CB    1 
ATOM   7280  O OG    . SER B  1 449 ? -11.172 3.164   237.577 1.00 61.81  ? 449 SER B OG    1 
ATOM   7281  N N     . LYS B  1 450 ? -11.077 1.433   241.029 1.00 70.66  ? 450 LYS B N     1 
ATOM   7282  C CA    . LYS B  1 450 ? -11.789 1.791   242.249 1.00 75.22  ? 450 LYS B CA    1 
ATOM   7283  C C     . LYS B  1 450 ? -10.916 2.692   243.114 1.00 78.55  ? 450 LYS B C     1 
ATOM   7284  O O     . LYS B  1 450 ? -9.696  2.700   242.962 1.00 78.63  ? 450 LYS B O     1 
ATOM   7285  C CB    . LYS B  1 450 ? -12.186 0.542   243.033 1.00 84.99  ? 450 LYS B CB    1 
ATOM   7286  C CG    . LYS B  1 450 ? -12.976 -0.490  242.246 1.00 87.99  ? 450 LYS B CG    1 
ATOM   7287  C CD    . LYS B  1 450 ? -12.906 -1.854  242.919 1.00 91.08  ? 450 LYS B CD    1 
ATOM   7288  C CE    . LYS B  1 450 ? -11.526 -2.476  242.776 1.00 99.84  ? 450 LYS B CE    1 
ATOM   7289  N NZ    . LYS B  1 450 ? -11.435 -3.340  241.566 1.00 82.97  ? 450 LYS B NZ    1 
ATOM   7290  N N     . ASN B  1 451 ? -11.553 3.436   244.016 1.00 78.68  ? 451 ASN B N     1 
ATOM   7291  C CA    . ASN B  1 451 ? -10.869 4.252   245.023 1.00 82.09  ? 451 ASN B CA    1 
ATOM   7292  C C     . ASN B  1 451 ? -9.630  5.009   244.528 1.00 81.94  ? 451 ASN B C     1 
ATOM   7293  O O     . ASN B  1 451 ? -8.500  4.685   244.905 1.00 81.86  ? 451 ASN B O     1 
ATOM   7294  C CB    . ASN B  1 451 ? -10.500 3.361   246.212 1.00 87.46  ? 451 ASN B CB    1 
ATOM   7295  C CG    . ASN B  1 451 ? -11.679 2.536   246.701 1.00 87.34  ? 451 ASN B CG    1 
ATOM   7296  O OD1   . ASN B  1 451 ? -11.720 1.320   246.515 1.00 86.70  ? 451 ASN B OD1   1 
ATOM   7297  N ND2   . ASN B  1 451 ? -12.652 3.199   247.314 1.00 88.27  ? 451 ASN B ND2   1 
ATOM   7298  N N     . PRO B  1 452 ? -9.841  6.018   243.668 1.00 78.77  ? 452 PRO B N     1 
ATOM   7299  C CA    . PRO B  1 452 ? -11.135 6.433   243.115 1.00 75.82  ? 452 PRO B CA    1 
ATOM   7300  C C     . PRO B  1 452 ? -11.426 5.802   241.752 1.00 70.75  ? 452 PRO B C     1 
ATOM   7301  O O     . PRO B  1 452 ? -10.514 5.296   241.099 1.00 70.92  ? 452 PRO B O     1 
ATOM   7302  C CB    . PRO B  1 452 ? -10.986 7.951   242.990 1.00 77.48  ? 452 PRO B CB    1 
ATOM   7303  C CG    . PRO B  1 452 ? -9.478  8.206   242.948 1.00 72.40  ? 452 PRO B CG    1 
ATOM   7304  C CD    . PRO B  1 452 ? -8.760  6.910   243.224 1.00 78.83  ? 452 PRO B CD    1 
ATOM   7305  N N     . ARG B  1 453 ? -12.690 5.824   241.336 1.00 70.59  ? 453 ARG B N     1 
ATOM   7306  C CA    . ARG B  1 453 ? -13.062 5.354   240.006 1.00 67.00  ? 453 ARG B CA    1 
ATOM   7307  C C     . ARG B  1 453 ? -12.577 6.360   238.967 1.00 66.61  ? 453 ARG B C     1 
ATOM   7308  O O     . ARG B  1 453 ? -12.911 7.542   239.038 1.00 66.70  ? 453 ARG B O     1 
ATOM   7309  C CB    . ARG B  1 453 ? -14.574 5.150   239.903 1.00 66.45  ? 453 ARG B CB    1 
ATOM   7310  C CG    . ARG B  1 453 ? -15.026 4.411   238.656 1.00 66.20  ? 453 ARG B CG    1 
ATOM   7311  C CD    . ARG B  1 453 ? -16.512 4.107   238.722 1.00 63.21  ? 453 ARG B CD    1 
ATOM   7312  N NE    . ARG B  1 453 ? -16.950 3.239   237.633 1.00 66.85  ? 453 ARG B NE    1 
ATOM   7313  C CZ    . ARG B  1 453 ? -18.151 2.675   237.569 1.00 65.42  ? 453 ARG B CZ    1 
ATOM   7314  N NH1   . ARG B  1 453 ? -19.037 2.886   238.533 1.00 66.46  ? 453 ARG B NH1   1 
ATOM   7315  N NH2   . ARG B  1 453 ? -18.467 1.898   236.543 1.00 63.83  ? 453 ARG B NH2   1 
ATOM   7316  N N     . LEU B  1 454 ? -11.793 5.886   238.004 1.00 62.60  ? 454 LEU B N     1 
ATOM   7317  C CA    . LEU B  1 454 ? -11.075 6.773   237.094 1.00 60.26  ? 454 LEU B CA    1 
ATOM   7318  C C     . LEU B  1 454 ? -11.929 7.278   235.936 1.00 60.07  ? 454 LEU B C     1 
ATOM   7319  O O     . LEU B  1 454 ? -12.871 6.614   235.505 1.00 60.82  ? 454 LEU B O     1 
ATOM   7320  C CB    . LEU B  1 454 ? -9.834  6.062   236.549 1.00 56.90  ? 454 LEU B CB    1 
ATOM   7321  C CG    . LEU B  1 454 ? -8.865  5.591   237.635 1.00 57.46  ? 454 LEU B CG    1 
ATOM   7322  C CD1   . LEU B  1 454 ? -7.699  4.811   237.048 1.00 56.04  ? 454 LEU B CD1   1 
ATOM   7323  C CD2   . LEU B  1 454 ? -8.368  6.775   238.448 1.00 60.79  ? 454 LEU B CD2   1 
ATOM   7324  N N     . GLY B  1 455 ? -11.584 8.465   235.442 1.00 55.88  ? 455 GLY B N     1 
ATOM   7325  C CA    . GLY B  1 455 ? -12.267 9.070   234.313 1.00 56.90  ? 455 GLY B CA    1 
ATOM   7326  C C     . GLY B  1 455 ? -11.290 9.716   233.347 1.00 54.46  ? 455 GLY B C     1 
ATOM   7327  O O     . GLY B  1 455 ? -10.082 9.568   233.487 1.00 51.15  ? 455 GLY B O     1 
ATOM   7328  N N     . TYR B  1 456 ? -11.819 10.444  232.372 1.00 54.23  ? 456 TYR B N     1 
ATOM   7329  C CA    . TYR B  1 456 ? -11.015 11.032  231.307 1.00 48.43  ? 456 TYR B CA    1 
ATOM   7330  C C     . TYR B  1 456 ? -11.592 12.401  230.965 1.00 45.90  ? 456 TYR B C     1 
ATOM   7331  O O     . TYR B  1 456 ? -12.756 12.506  230.590 1.00 43.18  ? 456 TYR B O     1 
ATOM   7332  C CB    . TYR B  1 456 ? -11.004 10.102  230.089 1.00 43.76  ? 456 TYR B CB    1 
ATOM   7333  C CG    . TYR B  1 456 ? -10.320 10.626  228.846 1.00 40.97  ? 456 TYR B CG    1 
ATOM   7334  C CD1   . TYR B  1 456 ? -9.222  11.473  228.922 1.00 40.65  ? 456 TYR B CD1   1 
ATOM   7335  C CD2   . TYR B  1 456 ? -10.780 10.262  227.587 1.00 39.50  ? 456 TYR B CD2   1 
ATOM   7336  C CE1   . TYR B  1 456 ? -8.604  11.942  227.775 1.00 34.39  ? 456 TYR B CE1   1 
ATOM   7337  C CE2   . TYR B  1 456 ? -10.172 10.723  226.441 1.00 41.81  ? 456 TYR B CE2   1 
ATOM   7338  C CZ    . TYR B  1 456 ? -9.084  11.561  226.540 1.00 40.30  ? 456 TYR B CZ    1 
ATOM   7339  O OH    . TYR B  1 456 ? -8.483  12.022  225.391 1.00 37.40  ? 456 TYR B OH    1 
ATOM   7340  N N     . VAL B  1 457 ? -10.781 13.447  231.103 1.00 40.70  ? 457 VAL B N     1 
ATOM   7341  C CA    . VAL B  1 457 ? -11.288 14.817  231.038 1.00 38.44  ? 457 VAL B CA    1 
ATOM   7342  C C     . VAL B  1 457 ? -11.915 15.159  229.680 1.00 44.04  ? 457 VAL B C     1 
ATOM   7343  O O     . VAL B  1 457 ? -12.866 15.940  229.610 1.00 40.03  ? 457 VAL B O     1 
ATOM   7344  C CB    . VAL B  1 457 ? -10.173 15.843  231.373 1.00 45.33  ? 457 VAL B CB    1 
ATOM   7345  C CG1   . VAL B  1 457 ? -9.082  15.861  230.306 1.00 37.03  ? 457 VAL B CG1   1 
ATOM   7346  C CG2   . VAL B  1 457 ? -10.766 17.232  231.588 1.00 39.98  ? 457 VAL B CG2   1 
ATOM   7347  N N     . ASN B  1 458 ? -11.412 14.555  228.607 1.00 39.41  ? 458 ASN B N     1 
ATOM   7348  C CA    . ASN B  1 458 ? -12.001 14.770  227.289 1.00 40.53  ? 458 ASN B CA    1 
ATOM   7349  C C     . ASN B  1 458 ? -13.351 14.078  227.170 1.00 45.11  ? 458 ASN B C     1 
ATOM   7350  O O     . ASN B  1 458 ? -14.160 14.417  226.308 1.00 42.60  ? 458 ASN B O     1 
ATOM   7351  C CB    . ASN B  1 458 ? -11.063 14.290  226.184 1.00 36.54  ? 458 ASN B CB    1 
ATOM   7352  C CG    . ASN B  1 458 ? -10.185 15.402  225.651 1.00 40.20  ? 458 ASN B CG    1 
ATOM   7353  O OD1   . ASN B  1 458 ? -10.565 16.575  225.674 1.00 38.06  ? 458 ASN B OD1   1 
ATOM   7354  N ND2   . ASN B  1 458 ? -9.006  15.040  225.162 1.00 37.47  ? 458 ASN B ND2   1 
ATOM   7355  N N     . HIS B  1 459 ? -13.579 13.093  228.034 1.00 41.16  ? 459 HIS B N     1 
ATOM   7356  C CA    . HIS B  1 459 ? -14.897 12.492  228.179 1.00 46.43  ? 459 HIS B CA    1 
ATOM   7357  C C     . HIS B  1 459 ? -15.560 13.065  229.422 1.00 47.01  ? 459 HIS B C     1 
ATOM   7358  O O     . HIS B  1 459 ? -15.980 12.326  230.310 1.00 47.49  ? 459 HIS B O     1 
ATOM   7359  C CB    . HIS B  1 459 ? -14.805 10.970  228.272 1.00 48.21  ? 459 HIS B CB    1 
ATOM   7360  C CG    . HIS B  1 459 ? -14.353 10.317  227.004 1.00 50.45  ? 459 HIS B CG    1 
ATOM   7361  N ND1   . HIS B  1 459 ? -14.403 8.953   226.812 1.00 58.42  ? 459 HIS B ND1   1 
ATOM   7362  C CD2   . HIS B  1 459 ? -13.839 10.838  225.865 1.00 49.51  ? 459 HIS B CD2   1 
ATOM   7363  C CE1   . HIS B  1 459 ? -13.939 8.662   225.610 1.00 64.57  ? 459 HIS B CE1   1 
ATOM   7364  N NE2   . HIS B  1 459 ? -13.591 9.789   225.014 1.00 53.12  ? 459 HIS B NE2   1 
ATOM   7365  N N     . ILE B  1 460 ? -15.628 14.393  229.475 1.00 42.66  ? 460 ILE B N     1 
ATOM   7366  C CA    . ILE B  1 460 ? -16.161 15.118  230.622 1.00 47.68  ? 460 ILE B CA    1 
ATOM   7367  C C     . ILE B  1 460 ? -17.544 14.600  231.021 1.00 49.86  ? 460 ILE B C     1 
ATOM   7368  O O     . ILE B  1 460 ? -18.399 14.349  230.170 1.00 45.61  ? 460 ILE B O     1 
ATOM   7369  C CB    . ILE B  1 460 ? -16.218 16.639  230.323 1.00 41.32  ? 460 ILE B CB    1 
ATOM   7370  C CG1   . ILE B  1 460 ? -16.683 17.428  231.554 1.00 49.48  ? 460 ILE B CG1   1 
ATOM   7371  C CG2   . ILE B  1 460 ? -17.072 16.927  229.084 1.00 45.76  ? 460 ILE B CG2   1 
ATOM   7372  C CD1   . ILE B  1 460 ? -15.585 17.657  232.577 1.00 53.06  ? 460 ILE B CD1   1 
ATOM   7373  N N     . ASP B  1 461 ? -17.744 14.418  232.322 1.00 51.82  ? 461 ASP B N     1 
ATOM   7374  C CA    . ASP B  1 461 ? -18.966 13.814  232.837 1.00 55.47  ? 461 ASP B CA    1 
ATOM   7375  C C     . ASP B  1 461 ? -19.415 14.544  234.097 1.00 56.38  ? 461 ASP B C     1 
ATOM   7376  O O     . ASP B  1 461 ? -18.765 14.463  235.140 1.00 60.93  ? 461 ASP B O     1 
ATOM   7377  C CB    . ASP B  1 461 ? -18.737 12.325  233.111 1.00 54.08  ? 461 ASP B CB    1 
ATOM   7378  C CG    . ASP B  1 461 ? -19.987 11.610  233.592 1.00 62.59  ? 461 ASP B CG    1 
ATOM   7379  O OD1   . ASP B  1 461 ? -21.085 12.206  233.570 1.00 59.08  ? 461 ASP B OD1   1 
ATOM   7380  O OD2   . ASP B  1 461 ? -19.864 10.430  233.986 1.00 61.80  ? 461 ASP B OD2   1 
ATOM   7381  N N     . LEU B  1 462 ? -20.531 15.259  233.989 1.00 56.48  ? 462 LEU B N     1 
ATOM   7382  C CA    . LEU B  1 462 ? -21.014 16.092  235.084 1.00 61.66  ? 462 LEU B CA    1 
ATOM   7383  C C     . LEU B  1 462 ? -21.822 15.300  236.110 1.00 61.99  ? 462 LEU B C     1 
ATOM   7384  O O     . LEU B  1 462 ? -22.280 15.858  237.106 1.00 58.73  ? 462 LEU B O     1 
ATOM   7385  C CB    . LEU B  1 462 ? -21.851 17.251  234.539 1.00 61.30  ? 462 LEU B CB    1 
ATOM   7386  C CG    . LEU B  1 462 ? -21.053 18.361  233.848 1.00 57.05  ? 462 LEU B CG    1 
ATOM   7387  C CD1   . LEU B  1 462 ? -21.972 19.482  233.391 1.00 52.95  ? 462 LEU B CD1   1 
ATOM   7388  C CD2   . LEU B  1 462 ? -19.976 18.901  234.773 1.00 57.12  ? 462 LEU B CD2   1 
ATOM   7389  N N     . ASP B  1 463 ? -21.991 14.002  235.868 1.00 63.34  ? 463 ASP B N     1 
ATOM   7390  C CA    . ASP B  1 463 ? -22.593 13.120  236.863 1.00 68.72  ? 463 ASP B CA    1 
ATOM   7391  C C     . ASP B  1 463 ? -21.689 13.063  238.086 1.00 67.65  ? 463 ASP B C     1 
ATOM   7392  O O     . ASP B  1 463 ? -22.148 12.863  239.211 1.00 72.55  ? 463 ASP B O     1 
ATOM   7393  C CB    . ASP B  1 463 ? -22.812 11.712  236.308 1.00 64.04  ? 463 ASP B CB    1 
ATOM   7394  C CG    . ASP B  1 463 ? -23.847 11.670  235.204 1.00 68.02  ? 463 ASP B CG    1 
ATOM   7395  O OD1   . ASP B  1 463 ? -24.577 12.669  235.028 1.00 68.77  ? 463 ASP B OD1   1 
ATOM   7396  O OD2   . ASP B  1 463 ? -23.939 10.630  234.520 1.00 72.88  ? 463 ASP B OD2   1 
ATOM   7397  N N     . LEU B  1 464 ? -20.394 13.248  237.843 1.00 66.05  ? 464 LEU B N     1 
ATOM   7398  C CA    . LEU B  1 464 ? -19.387 13.279  238.898 1.00 66.54  ? 464 LEU B CA    1 
ATOM   7399  C C     . LEU B  1 464 ? -19.577 14.465  239.838 1.00 69.65  ? 464 LEU B C     1 
ATOM   7400  O O     . LEU B  1 464 ? -18.981 14.512  240.911 1.00 71.69  ? 464 LEU B O     1 
ATOM   7401  C CB    . LEU B  1 464 ? -17.984 13.322  238.288 1.00 65.48  ? 464 LEU B CB    1 
ATOM   7402  C CG    . LEU B  1 464 ? -17.561 12.156  237.386 1.00 70.93  ? 464 LEU B CG    1 
ATOM   7403  C CD1   . LEU B  1 464 ? -16.281 12.490  236.636 1.00 64.47  ? 464 LEU B CD1   1 
ATOM   7404  C CD2   . LEU B  1 464 ? -17.383 10.883  238.199 1.00 69.71  ? 464 LEU B CD2   1 
ATOM   7405  N N     . GLY B  1 465 ? -20.399 15.425  239.425 1.00 65.83  ? 465 GLY B N     1 
ATOM   7406  C CA    . GLY B  1 465 ? -20.654 16.616  240.217 1.00 68.94  ? 465 GLY B CA    1 
ATOM   7407  C C     . GLY B  1 465 ? -20.207 17.874  239.497 1.00 70.25  ? 465 GLY B C     1 
ATOM   7408  O O     . GLY B  1 465 ? -19.759 17.814  238.353 1.00 66.68  ? 465 GLY B O     1 
ATOM   7409  N N     . GLY B  1 466 ? -20.323 19.016  240.168 1.00 65.51  ? 466 GLY B N     1 
ATOM   7410  C CA    . GLY B  1 466 ? -19.945 20.287  239.577 1.00 62.99  ? 466 GLY B CA    1 
ATOM   7411  C C     . GLY B  1 466 ? -19.911 21.431  240.572 1.00 63.83  ? 466 GLY B C     1 
ATOM   7412  O O     . GLY B  1 466 ? -20.644 21.431  241.561 1.00 64.37  ? 466 GLY B O     1 
ATOM   7413  N N     . ILE B  1 467 ? -19.053 22.411  240.302 1.00 62.26  ? 467 ILE B N     1 
ATOM   7414  C CA    . ILE B  1 467 ? -18.921 23.590  241.151 1.00 62.29  ? 467 ILE B CA    1 
ATOM   7415  C C     . ILE B  1 467 ? -19.868 24.709  240.715 1.00 66.31  ? 467 ILE B C     1 
ATOM   7416  O O     . ILE B  1 467 ? -19.954 25.027  239.529 1.00 64.88  ? 467 ILE B O     1 
ATOM   7417  C CB    . ILE B  1 467 ? -17.475 24.137  241.136 1.00 62.67  ? 467 ILE B CB    1 
ATOM   7418  C CG1   . ILE B  1 467 ? -16.509 23.150  241.798 1.00 62.58  ? 467 ILE B CG1   1 
ATOM   7419  C CG2   . ILE B  1 467 ? -17.405 25.485  241.836 1.00 60.84  ? 467 ILE B CG2   1 
ATOM   7420  C CD1   . ILE B  1 467 ? -16.476 23.247  243.312 1.00 61.31  ? 467 ILE B CD1   1 
ATOM   7421  N N     . ASP B  1 468 ? -20.586 25.291  241.673 1.00 67.44  ? 468 ASP B N     1 
ATOM   7422  C CA    . ASP B  1 468 ? -21.282 26.554  241.447 1.00 67.71  ? 468 ASP B CA    1 
ATOM   7423  C C     . ASP B  1 468 ? -20.352 27.686  241.870 1.00 66.48  ? 468 ASP B C     1 
ATOM   7424  O O     . ASP B  1 468 ? -20.146 27.915  243.061 1.00 71.72  ? 468 ASP B O     1 
ATOM   7425  C CB    . ASP B  1 468 ? -22.602 26.615  242.227 1.00 68.34  ? 468 ASP B CB    1 
ATOM   7426  C CG    . ASP B  1 468 ? -23.422 27.866  241.914 1.00 68.72  ? 468 ASP B CG    1 
ATOM   7427  O OD1   . ASP B  1 468 ? -22.899 28.797  241.265 1.00 65.89  ? 468 ASP B OD1   1 
ATOM   7428  O OD2   . ASP B  1 468 ? -24.599 27.922  242.329 1.00 65.29  ? 468 ASP B OD2   1 
ATOM   7429  N N     . TRP B  1 469 ? -19.795 28.392  240.892 1.00 62.72  ? 469 TRP B N     1 
ATOM   7430  C CA    . TRP B  1 469 ? -18.855 29.471  241.171 1.00 63.06  ? 469 TRP B CA    1 
ATOM   7431  C C     . TRP B  1 469 ? -19.563 30.722  241.689 1.00 63.97  ? 469 TRP B C     1 
ATOM   7432  O O     . TRP B  1 469 ? -18.916 31.703  242.056 1.00 68.17  ? 469 TRP B O     1 
ATOM   7433  C CB    . TRP B  1 469 ? -18.039 29.799  239.918 1.00 59.66  ? 469 TRP B CB    1 
ATOM   7434  C CG    . TRP B  1 469 ? -17.170 28.661  239.468 1.00 57.53  ? 469 TRP B CG    1 
ATOM   7435  C CD1   . TRP B  1 469 ? -17.389 27.829  238.408 1.00 54.79  ? 469 TRP B CD1   1 
ATOM   7436  C CD2   . TRP B  1 469 ? -15.948 28.220  240.076 1.00 57.35  ? 469 TRP B CD2   1 
ATOM   7437  N NE1   . TRP B  1 469 ? -16.378 26.904  238.314 1.00 52.24  ? 469 TRP B NE1   1 
ATOM   7438  C CE2   . TRP B  1 469 ? -15.480 27.122  239.327 1.00 50.91  ? 469 TRP B CE2   1 
ATOM   7439  C CE3   . TRP B  1 469 ? -15.202 28.650  241.179 1.00 59.19  ? 469 TRP B CE3   1 
ATOM   7440  C CZ2   . TRP B  1 469 ? -14.301 26.447  239.645 1.00 53.21  ? 469 TRP B CZ2   1 
ATOM   7441  C CZ3   . TRP B  1 469 ? -14.032 27.979  241.494 1.00 56.72  ? 469 TRP B CZ3   1 
ATOM   7442  C CH2   . TRP B  1 469 ? -13.593 26.891  240.729 1.00 54.34  ? 469 TRP B CH2   1 
ATOM   7443  N N     . GLY B  1 470 ? -20.892 30.676  241.724 1.00 67.66  ? 470 GLY B N     1 
ATOM   7444  C CA    . GLY B  1 470 ? -21.692 31.773  242.239 1.00 68.22  ? 470 GLY B CA    1 
ATOM   7445  C C     . GLY B  1 470 ? -22.075 31.606  243.699 1.00 71.17  ? 470 GLY B C     1 
ATOM   7446  O O     . GLY B  1 470 ? -22.598 32.529  244.321 1.00 72.43  ? 470 GLY B O     1 
ATOM   7447  N N     . ASN B  1 471 ? -21.827 30.417  244.241 1.00 72.65  ? 471 ASN B N     1 
ATOM   7448  C CA    . ASN B  1 471 ? -22.030 30.144  245.662 1.00 74.39  ? 471 ASN B CA    1 
ATOM   7449  C C     . ASN B  1 471 ? -20.707 30.328  246.405 1.00 77.49  ? 471 ASN B C     1 
ATOM   7450  O O     . ASN B  1 471 ? -19.820 29.478  246.323 1.00 77.55  ? 471 ASN B O     1 
ATOM   7451  C CB    . ASN B  1 471 ? -22.581 28.725  245.867 1.00 78.92  ? 471 ASN B CB    1 
ATOM   7452  C CG    . ASN B  1 471 ? -22.930 28.422  247.325 1.00 86.99  ? 471 ASN B CG    1 
ATOM   7453  O OD1   . ASN B  1 471 ? -22.151 28.697  248.239 1.00 87.70  ? 471 ASN B OD1   1 
ATOM   7454  N ND2   . ASN B  1 471 ? -24.108 27.843  247.542 1.00 91.52  ? 471 ASN B ND2   1 
ATOM   7455  N N     . LYS B  1 472 ? -20.586 31.429  247.141 1.00 81.81  ? 472 LYS B N     1 
ATOM   7456  C CA    . LYS B  1 472 ? -19.309 31.819  247.731 1.00 81.61  ? 472 LYS B CA    1 
ATOM   7457  C C     . LYS B  1 472 ? -18.795 30.838  248.790 1.00 82.95  ? 472 LYS B C     1 
ATOM   7458  O O     . LYS B  1 472 ? -17.583 30.686  248.959 1.00 82.21  ? 472 LYS B O     1 
ATOM   7459  C CB    . LYS B  1 472 ? -19.414 33.221  248.333 1.00 84.98  ? 472 LYS B CB    1 
ATOM   7460  C CG    . LYS B  1 472 ? -18.088 33.960  248.335 1.00 89.08  ? 472 LYS B CG    1 
ATOM   7461  C CD    . LYS B  1 472 ? -18.089 35.146  249.276 1.00 90.03  ? 472 LYS B CD    1 
ATOM   7462  C CE    . LYS B  1 472 ? -16.688 35.389  249.812 1.00 89.92  ? 472 LYS B CE    1 
ATOM   7463  N NZ    . LYS B  1 472 ? -16.566 36.699  250.502 1.00 81.31  ? 472 LYS B NZ    1 
ATOM   7464  N N     . THR B  1 473 ? -19.709 30.184  249.502 1.00 84.35  ? 473 THR B N     1 
ATOM   7465  C CA    . THR B  1 473 ? -19.327 29.182  250.494 1.00 84.05  ? 473 THR B CA    1 
ATOM   7466  C C     . THR B  1 473 ? -18.608 28.015  249.827 1.00 83.67  ? 473 THR B C     1 
ATOM   7467  O O     . THR B  1 473 ? -17.606 27.511  250.336 1.00 84.92  ? 473 THR B O     1 
ATOM   7468  C CB    . THR B  1 473 ? -20.549 28.641  251.260 1.00 83.15  ? 473 THR B CB    1 
ATOM   7469  O OG1   . THR B  1 473 ? -21.471 29.707  251.519 1.00 88.85  ? 473 THR B OG1   1 
ATOM   7470  C CG2   . THR B  1 473 ? -20.118 28.004  252.577 1.00 78.07  ? 473 THR B CG2   1 
ATOM   7471  N N     . VAL B  1 474 ? -19.132 27.598  248.680 1.00 83.67  ? 474 VAL B N     1 
ATOM   7472  C CA    . VAL B  1 474 ? -18.563 26.499  247.909 1.00 80.85  ? 474 VAL B CA    1 
ATOM   7473  C C     . VAL B  1 474 ? -17.181 26.847  247.362 1.00 79.23  ? 474 VAL B C     1 
ATOM   7474  O O     . VAL B  1 474 ? -16.241 26.056  247.470 1.00 78.64  ? 474 VAL B O     1 
ATOM   7475  C CB    . VAL B  1 474 ? -19.489 26.112  246.737 1.00 78.04  ? 474 VAL B CB    1 
ATOM   7476  C CG1   . VAL B  1 474 ? -18.814 25.101  245.831 1.00 73.98  ? 474 VAL B CG1   1 
ATOM   7477  C CG2   . VAL B  1 474 ? -20.811 25.574  247.261 1.00 76.09  ? 474 VAL B CG2   1 
ATOM   7478  N N     . VAL B  1 475 ? -17.073 28.040  246.781 1.00 77.30  ? 475 VAL B N     1 
ATOM   7479  C CA    . VAL B  1 475 ? -15.836 28.522  246.172 1.00 78.59  ? 475 VAL B CA    1 
ATOM   7480  C C     . VAL B  1 475 ? -14.650 28.474  247.133 1.00 80.66  ? 475 VAL B C     1 
ATOM   7481  O O     . VAL B  1 475 ? -13.535 28.126  246.741 1.00 82.55  ? 475 VAL B O     1 
ATOM   7482  C CB    . VAL B  1 475 ? -16.004 29.970  245.655 1.00 74.74  ? 475 VAL B CB    1 
ATOM   7483  C CG1   . VAL B  1 475 ? -14.713 30.477  245.035 1.00 76.50  ? 475 VAL B CG1   1 
ATOM   7484  C CG2   . VAL B  1 475 ? -17.137 30.042  244.649 1.00 70.59  ? 475 VAL B CG2   1 
ATOM   7485  N N     . ASN B  1 476 ? -14.897 28.806  248.397 1.00 80.25  ? 476 ASN B N     1 
ATOM   7486  C CA    . ASN B  1 476 ? -13.829 28.858  249.392 1.00 83.53  ? 476 ASN B CA    1 
ATOM   7487  C C     . ASN B  1 476 ? -13.278 27.483  249.767 1.00 84.25  ? 476 ASN B C     1 
ATOM   7488  O O     . ASN B  1 476 ? -12.208 27.384  250.366 1.00 89.60  ? 476 ASN B O     1 
ATOM   7489  C CB    . ASN B  1 476 ? -14.311 29.584  250.648 1.00 83.80  ? 476 ASN B CB    1 
ATOM   7490  C CG    . ASN B  1 476 ? -14.370 31.089  250.462 1.00 88.87  ? 476 ASN B CG    1 
ATOM   7491  O OD1   . ASN B  1 476 ? -13.825 31.628  249.498 1.00 89.02  ? 476 ASN B OD1   1 
ATOM   7492  N ND2   . ASN B  1 476 ? -15.026 31.777  251.389 1.00 90.61  ? 476 ASN B ND2   1 
ATOM   7493  N N     . ASN B  1 477 ? -14.002 26.424  249.417 1.00 81.51  ? 477 ASN B N     1 
ATOM   7494  C CA    . ASN B  1 477 ? -13.479 25.070  249.576 1.00 84.74  ? 477 ASN B CA    1 
ATOM   7495  C C     . ASN B  1 477 ? -13.614 24.293  248.270 1.00 80.92  ? 477 ASN B C     1 
ATOM   7496  O O     . ASN B  1 477 ? -13.950 23.109  248.265 1.00 79.01  ? 477 ASN B O     1 
ATOM   7497  C CB    . ASN B  1 477 ? -14.195 24.330  250.711 1.00 86.34  ? 477 ASN B CB    1 
ATOM   7498  C CG    . ASN B  1 477 ? -13.421 23.113  251.194 1.00 90.10  ? 477 ASN B CG    1 
ATOM   7499  O OD1   . ASN B  1 477 ? -12.194 23.148  251.307 1.00 92.38  ? 477 ASN B OD1   1 
ATOM   7500  N ND2   . ASN B  1 477 ? -14.134 22.026  251.466 1.00 90.70  ? 477 ASN B ND2   1 
ATOM   7501  N N     . ALA B  1 478 ? -13.340 24.976  247.163 1.00 79.72  ? 478 ALA B N     1 
ATOM   7502  C CA    . ALA B  1 478 ? -13.493 24.398  245.834 1.00 71.07  ? 478 ALA B CA    1 
ATOM   7503  C C     . ALA B  1 478 ? -12.555 23.217  245.596 1.00 69.87  ? 478 ALA B C     1 
ATOM   7504  O O     . ALA B  1 478 ? -12.920 22.259  244.917 1.00 69.24  ? 478 ALA B O     1 
ATOM   7505  C CB    . ALA B  1 478 ? -13.272 25.467  244.773 1.00 67.95  ? 478 ALA B CB    1 
ATOM   7506  N N     . ILE B  1 479 ? -11.353 23.289  246.161 1.00 70.66  ? 479 ILE B N     1 
ATOM   7507  C CA    . ILE B  1 479 ? -10.329 22.266  245.945 1.00 72.05  ? 479 ILE B CA    1 
ATOM   7508  C C     . ILE B  1 479 ? -10.764 20.883  246.441 1.00 73.54  ? 479 ILE B C     1 
ATOM   7509  O O     . ILE B  1 479 ? -10.602 19.884  245.737 1.00 74.47  ? 479 ILE B O     1 
ATOM   7510  C CB    . ILE B  1 479 ? -9.000  22.654  246.631 1.00 66.47  ? 479 ILE B CB    1 
ATOM   7511  C CG1   . ILE B  1 479 ? -8.408  23.910  245.985 1.00 65.09  ? 479 ILE B CG1   1 
ATOM   7512  C CG2   . ILE B  1 479 ? -8.001  21.514  246.551 1.00 67.17  ? 479 ILE B CG2   1 
ATOM   7513  C CD1   . ILE B  1 479 ? -7.014  24.254  246.483 1.00 65.06  ? 479 ILE B CD1   1 
ATOM   7514  N N     . GLU B  1 480 ? -11.325 20.834  247.646 1.00 76.56  ? 480 GLU B N     1 
ATOM   7515  C CA    . GLU B  1 480 ? -11.795 19.582  248.235 1.00 75.99  ? 480 GLU B CA    1 
ATOM   7516  C C     . GLU B  1 480 ? -13.029 19.039  247.521 1.00 70.83  ? 480 GLU B C     1 
ATOM   7517  O O     . GLU B  1 480 ? -13.189 17.826  247.372 1.00 76.83  ? 480 GLU B O     1 
ATOM   7518  C CB    . GLU B  1 480 ? -12.106 19.771  249.723 1.00 77.45  ? 480 GLU B CB    1 
ATOM   7519  C CG    . GLU B  1 480 ? -10.883 20.026  250.580 1.00 76.48  ? 480 GLU B CG    1 
ATOM   7520  C CD    . GLU B  1 480 ? -9.833  18.935  250.438 1.00 79.59  ? 480 GLU B CD    1 
ATOM   7521  O OE1   . GLU B  1 480 ? -10.203 17.745  250.370 1.00 77.41  ? 480 GLU B OE1   1 
ATOM   7522  O OE2   . GLU B  1 480 ? -8.635  19.271  250.372 1.00 81.62  ? 480 GLU B OE2   1 
ATOM   7523  N N     . ILE B  1 481 ? -13.904 19.941  247.091 1.00 71.30  ? 481 ILE B N     1 
ATOM   7524  C CA    . ILE B  1 481 ? -15.120 19.552  246.389 1.00 68.78  ? 481 ILE B CA    1 
ATOM   7525  C C     . ILE B  1 481 ? -14.794 19.046  244.984 1.00 69.28  ? 481 ILE B C     1 
ATOM   7526  O O     . ILE B  1 481 ? -15.365 18.057  244.523 1.00 69.96  ? 481 ILE B O     1 
ATOM   7527  C CB    . ILE B  1 481 ? -16.118 20.726  246.301 1.00 69.01  ? 481 ILE B CB    1 
ATOM   7528  C CG1   . ILE B  1 481 ? -16.463 21.242  247.701 1.00 71.04  ? 481 ILE B CG1   1 
ATOM   7529  C CG2   . ILE B  1 481 ? -17.386 20.306  245.573 1.00 65.84  ? 481 ILE B CG2   1 
ATOM   7530  C CD1   . ILE B  1 481 ? -17.412 22.415  247.695 1.00 68.40  ? 481 ILE B CD1   1 
ATOM   7531  N N     . SER B  1 482 ? -13.862 19.720  244.317 1.00 68.22  ? 482 SER B N     1 
ATOM   7532  C CA    . SER B  1 482 ? -13.457 19.347  242.964 1.00 66.68  ? 482 SER B CA    1 
ATOM   7533  C C     . SER B  1 482 ? -12.576 18.101  242.955 1.00 68.41  ? 482 SER B C     1 
ATOM   7534  O O     . SER B  1 482 ? -12.318 17.527  241.895 1.00 64.59  ? 482 SER B O     1 
ATOM   7535  C CB    . SER B  1 482 ? -12.725 20.507  242.282 1.00 63.65  ? 482 SER B CB    1 
ATOM   7536  O OG    . SER B  1 482 ? -13.579 21.625  242.106 1.00 63.35  ? 482 SER B OG    1 
ATOM   7537  N N     . ARG B  1 483 ? -12.118 17.682  244.133 1.00 69.68  ? 483 ARG B N     1 
ATOM   7538  C CA    . ARG B  1 483 ? -11.212 16.538  244.239 1.00 67.97  ? 483 ARG B CA    1 
ATOM   7539  C C     . ARG B  1 483 ? -11.887 15.245  243.766 1.00 67.23  ? 483 ARG B C     1 
ATOM   7540  O O     . ARG B  1 483 ? -11.210 14.310  243.331 1.00 68.04  ? 483 ARG B O     1 
ATOM   7541  C CB    . ARG B  1 483 ? -10.690 16.377  245.681 1.00 71.39  ? 483 ARG B CB    1 
ATOM   7542  C CG    . ARG B  1 483 ? -9.823  15.129  245.878 1.00 77.94  ? 483 ARG B CG    1 
ATOM   7543  C CD    . ARG B  1 483 ? -9.068  15.086  247.210 1.00 78.64  ? 483 ARG B CD    1 
ATOM   7544  N NE    . ARG B  1 483 ? -7.773  15.763  247.148 1.00 75.82  ? 483 ARG B NE    1 
ATOM   7545  C CZ    . ARG B  1 483 ? -7.551  17.003  247.567 1.00 76.71  ? 483 ARG B CZ    1 
ATOM   7546  N NH1   . ARG B  1 483 ? -8.536  17.711  248.084 1.00 79.53  ? 483 ARG B NH1   1 
ATOM   7547  N NH2   . ARG B  1 483 ? -6.343  17.537  247.473 1.00 79.38  ? 483 ARG B NH2   1 
ATOM   7548  N N     . SER B  1 484 ? -13.217 15.209  243.833 1.00 66.77  ? 484 SER B N     1 
ATOM   7549  C CA    . SER B  1 484 ? -13.997 14.064  243.356 1.00 67.14  ? 484 SER B CA    1 
ATOM   7550  C C     . SER B  1 484 ? -13.715 13.702  241.895 1.00 66.60  ? 484 SER B C     1 
ATOM   7551  O O     . SER B  1 484 ? -13.286 12.588  241.589 1.00 65.88  ? 484 SER B O     1 
ATOM   7552  C CB    . SER B  1 484 ? -15.493 14.340  243.521 1.00 65.41  ? 484 SER B CB    1 
ATOM   7553  O OG    . SER B  1 484 ? -16.266 13.406  242.792 1.00 67.87  ? 484 SER B OG    1 
ATOM   7554  N N     . TRP B  1 485 ? -13.975 14.643  240.994 1.00 66.13  ? 485 TRP B N     1 
ATOM   7555  C CA    . TRP B  1 485 ? -13.729 14.418  239.575 1.00 62.73  ? 485 TRP B CA    1 
ATOM   7556  C C     . TRP B  1 485 ? -12.278 14.714  239.218 1.00 59.65  ? 485 TRP B C     1 
ATOM   7557  O O     . TRP B  1 485 ? -11.733 14.135  238.279 1.00 57.36  ? 485 TRP B O     1 
ATOM   7558  C CB    . TRP B  1 485 ? -14.669 15.267  238.717 1.00 62.53  ? 485 TRP B CB    1 
ATOM   7559  C CG    . TRP B  1 485 ? -14.719 16.719  239.094 1.00 62.51  ? 485 TRP B CG    1 
ATOM   7560  C CD1   . TRP B  1 485 ? -13.880 17.708  238.671 1.00 58.07  ? 485 TRP B CD1   1 
ATOM   7561  C CD2   . TRP B  1 485 ? -15.676 17.346  239.957 1.00 60.81  ? 485 TRP B CD2   1 
ATOM   7562  N NE1   . TRP B  1 485 ? -14.250 18.911  239.223 1.00 58.72  ? 485 TRP B NE1   1 
ATOM   7563  C CE2   . TRP B  1 485 ? -15.349 18.716  240.016 1.00 62.04  ? 485 TRP B CE2   1 
ATOM   7564  C CE3   . TRP B  1 485 ? -16.773 16.882  240.688 1.00 63.47  ? 485 TRP B CE3   1 
ATOM   7565  C CZ2   . TRP B  1 485 ? -16.083 19.626  240.776 1.00 63.88  ? 485 TRP B CZ2   1 
ATOM   7566  C CZ3   . TRP B  1 485 ? -17.497 17.786  241.444 1.00 67.89  ? 485 TRP B CZ3   1 
ATOM   7567  C CH2   . TRP B  1 485 ? -17.149 19.141  241.482 1.00 65.64  ? 485 TRP B CH2   1 
ATOM   7568  N N     . GLY B  1 486 ? -11.656 15.607  239.979 1.00 58.80  ? 486 GLY B N     1 
ATOM   7569  C CA    . GLY B  1 486 ? -10.289 16.015  239.714 1.00 57.10  ? 486 GLY B CA    1 
ATOM   7570  C C     . GLY B  1 486 ? -9.289  14.880  239.816 1.00 61.24  ? 486 GLY B C     1 
ATOM   7571  O O     . GLY B  1 486 ? -8.458  14.692  238.928 1.00 55.61  ? 486 GLY B O     1 
ATOM   7572  N N     . GLU B  1 487 ? -9.368  14.119  240.903 1.00 64.19  ? 487 GLU B N     1 
ATOM   7573  C CA    . GLU B  1 487 ? -8.487  12.973  241.094 1.00 65.43  ? 487 GLU B CA    1 
ATOM   7574  C C     . GLU B  1 487 ? -8.940  11.792  240.239 1.00 60.04  ? 487 GLU B C     1 
ATOM   7575  O O     . GLU B  1 487 ? -8.155  10.895  239.935 1.00 63.08  ? 487 GLU B O     1 
ATOM   7576  C CB    . GLU B  1 487 ? -8.432  12.577  242.570 1.00 67.26  ? 487 GLU B CB    1 
ATOM   7577  C CG    . GLU B  1 487 ? -7.808  13.639  243.458 1.00 77.01  ? 487 GLU B CG    1 
ATOM   7578  C CD    . GLU B  1 487 ? -7.402  13.103  244.819 1.00 80.67  ? 487 GLU B CD    1 
ATOM   7579  O OE1   . GLU B  1 487 ? -7.885  12.016  245.201 1.00 83.07  ? 487 GLU B OE1   1 
ATOM   7580  O OE2   . GLU B  1 487 ? -6.597  13.768  245.506 1.00 81.46  ? 487 GLU B OE2   1 
ATOM   7581  N N     . SER B  1 488 ? -10.212 11.797  239.856 1.00 58.26  ? 488 SER B N     1 
ATOM   7582  C CA    . SER B  1 488 ? -10.726 10.805  238.923 1.00 61.24  ? 488 SER B CA    1 
ATOM   7583  C C     . SER B  1 488 ? -10.096 11.027  237.552 1.00 59.90  ? 488 SER B C     1 
ATOM   7584  O O     . SER B  1 488 ? -9.745  10.079  236.846 1.00 56.70  ? 488 SER B O     1 
ATOM   7585  C CB    . SER B  1 488 ? -12.250 10.886  238.836 1.00 59.97  ? 488 SER B CB    1 
ATOM   7586  O OG    . SER B  1 488 ? -12.778 9.838   238.044 1.00 66.79  ? 488 SER B OG    1 
ATOM   7587  N N     . TYR B  1 489 ? -9.945  12.296  237.190 1.00 59.14  ? 489 TYR B N     1 
ATOM   7588  C CA    . TYR B  1 489 ? -9.369  12.661  235.905 1.00 54.02  ? 489 TYR B CA    1 
ATOM   7589  C C     . TYR B  1 489 ? -7.846  12.603  235.901 1.00 54.87  ? 489 TYR B C     1 
ATOM   7590  O O     . TYR B  1 489 ? -7.243  12.189  234.913 1.00 51.36  ? 489 TYR B O     1 
ATOM   7591  C CB    . TYR B  1 489 ? -9.813  14.066  235.502 1.00 52.89  ? 489 TYR B CB    1 
ATOM   7592  C CG    . TYR B  1 489 ? -11.279 14.191  235.169 1.00 51.81  ? 489 TYR B CG    1 
ATOM   7593  C CD1   . TYR B  1 489 ? -11.979 13.131  234.608 1.00 50.06  ? 489 TYR B CD1   1 
ATOM   7594  C CD2   . TYR B  1 489 ? -11.962 15.374  235.410 1.00 50.70  ? 489 TYR B CD2   1 
ATOM   7595  C CE1   . TYR B  1 489 ? -13.318 13.245  234.300 1.00 50.52  ? 489 TYR B CE1   1 
ATOM   7596  C CE2   . TYR B  1 489 ? -13.299 15.497  235.106 1.00 51.50  ? 489 TYR B CE2   1 
ATOM   7597  C CZ    . TYR B  1 489 ? -13.973 14.433  234.552 1.00 53.36  ? 489 TYR B CZ    1 
ATOM   7598  O OH    . TYR B  1 489 ? -15.309 14.553  234.248 1.00 55.57  ? 489 TYR B OH    1 
ATOM   7599  N N     . PHE B  1 490 ? -7.222  13.021  236.999 1.00 56.89  ? 490 PHE B N     1 
ATOM   7600  C CA    . PHE B  1 490 ? -5.788  13.287  236.968 1.00 52.73  ? 490 PHE B CA    1 
ATOM   7601  C C     . PHE B  1 490 ? -4.973  12.589  238.058 1.00 56.50  ? 490 PHE B C     1 
ATOM   7602  O O     . PHE B  1 490 ? -3.742  12.577  237.993 1.00 56.38  ? 490 PHE B O     1 
ATOM   7603  C CB    . PHE B  1 490 ? -5.551  14.798  237.041 1.00 52.32  ? 490 PHE B CB    1 
ATOM   7604  C CG    . PHE B  1 490 ? -6.350  15.582  236.039 1.00 52.28  ? 490 PHE B CG    1 
ATOM   7605  C CD1   . PHE B  1 490 ? -6.085  15.475  234.683 1.00 48.90  ? 490 PHE B CD1   1 
ATOM   7606  C CD2   . PHE B  1 490 ? -7.367  16.428  236.454 1.00 50.98  ? 490 PHE B CD2   1 
ATOM   7607  C CE1   . PHE B  1 490 ? -6.820  16.193  233.760 1.00 43.39  ? 490 PHE B CE1   1 
ATOM   7608  C CE2   . PHE B  1 490 ? -8.102  17.153  235.535 1.00 49.97  ? 490 PHE B CE2   1 
ATOM   7609  C CZ    . PHE B  1 490 ? -7.830  17.034  234.188 1.00 49.22  ? 490 PHE B CZ    1 
ATOM   7610  N N     . LEU B  1 491 ? -5.656  12.012  239.044 1.00 59.10  ? 491 LEU B N     1 
ATOM   7611  C CA    . LEU B  1 491 ? -5.005  11.293  240.143 1.00 61.72  ? 491 LEU B CA    1 
ATOM   7612  C C     . LEU B  1 491 ? -3.915  12.120  240.825 1.00 63.56  ? 491 LEU B C     1 
ATOM   7613  O O     . LEU B  1 491 ? -4.186  13.173  241.399 1.00 67.39  ? 491 LEU B O     1 
ATOM   7614  C CB    . LEU B  1 491 ? -4.409  9.971   239.646 1.00 56.44  ? 491 LEU B CB    1 
ATOM   7615  C CG    . LEU B  1 491 ? -5.336  8.764   239.497 1.00 56.03  ? 491 LEU B CG    1 
ATOM   7616  C CD1   . LEU B  1 491 ? -4.548  7.552   239.029 1.00 55.10  ? 491 LEU B CD1   1 
ATOM   7617  C CD2   . LEU B  1 491 ? -6.056  8.463   240.804 1.00 58.84  ? 491 LEU B CD2   1 
ATOM   7618  N N     . SER B  1 492 ? -2.682  11.629  240.742 1.00 62.19  ? 492 SER B N     1 
ATOM   7619  C CA    . SER B  1 492 ? -1.529  12.286  241.353 1.00 66.91  ? 492 SER B CA    1 
ATOM   7620  C C     . SER B  1 492 ? -1.257  13.672  240.770 1.00 65.06  ? 492 SER B C     1 
ATOM   7621  O O     . SER B  1 492 ? -0.581  14.491  241.392 1.00 65.55  ? 492 SER B O     1 
ATOM   7622  C CB    . SER B  1 492 ? -0.282  11.414  241.195 1.00 66.19  ? 492 SER B CB    1 
ATOM   7623  O OG    . SER B  1 492 ? 0.111   11.349  239.833 1.00 70.07  ? 492 SER B OG    1 
ATOM   7624  N N     . ASN B  1 493 ? -1.774  13.931  239.575 1.00 61.38  ? 493 ASN B N     1 
ATOM   7625  C CA    . ASN B  1 493 ? -1.472  15.174  238.874 1.00 60.12  ? 493 ASN B CA    1 
ATOM   7626  C C     . ASN B  1 493 ? -2.439  16.313  239.196 1.00 57.39  ? 493 ASN B C     1 
ATOM   7627  O O     . ASN B  1 493 ? -2.231  17.446  238.763 1.00 57.40  ? 493 ASN B O     1 
ATOM   7628  C CB    . ASN B  1 493 ? -1.455  14.931  237.362 1.00 53.86  ? 493 ASN B CB    1 
ATOM   7629  C CG    . ASN B  1 493 ? -0.399  13.925  236.943 1.00 53.52  ? 493 ASN B CG    1 
ATOM   7630  O OD1   . ASN B  1 493 ? 0.656   13.813  237.568 1.00 56.68  ? 493 ASN B OD1   1 
ATOM   7631  N ND2   . ASN B  1 493 ? -0.680  13.187  235.875 1.00 42.64  ? 493 ASN B ND2   1 
ATOM   7632  N N     . TYR B  1 494 ? -3.485  16.013  239.960 1.00 59.53  ? 494 TYR B N     1 
ATOM   7633  C CA    . TYR B  1 494 ? -4.525  16.995  240.263 1.00 62.08  ? 494 TYR B CA    1 
ATOM   7634  C C     . TYR B  1 494 ? -4.005  18.193  241.046 1.00 66.95  ? 494 TYR B C     1 
ATOM   7635  O O     . TYR B  1 494 ? -4.409  19.328  240.789 1.00 68.38  ? 494 TYR B O     1 
ATOM   7636  C CB    . TYR B  1 494 ? -5.667  16.344  241.045 1.00 65.78  ? 494 TYR B CB    1 
ATOM   7637  C CG    . TYR B  1 494 ? -6.698  17.329  241.561 1.00 69.03  ? 494 TYR B CG    1 
ATOM   7638  C CD1   . TYR B  1 494 ? -7.654  17.868  240.713 1.00 67.64  ? 494 TYR B CD1   1 
ATOM   7639  C CD2   . TYR B  1 494 ? -6.713  17.723  242.896 1.00 71.39  ? 494 TYR B CD2   1 
ATOM   7640  C CE1   . TYR B  1 494 ? -8.601  18.767  241.176 1.00 67.80  ? 494 TYR B CE1   1 
ATOM   7641  C CE2   . TYR B  1 494 ? -7.655  18.624  243.368 1.00 75.25  ? 494 TYR B CE2   1 
ATOM   7642  C CZ    . TYR B  1 494 ? -8.596  19.141  242.502 1.00 70.05  ? 494 TYR B CZ    1 
ATOM   7643  O OH    . TYR B  1 494 ? -9.534  20.035  242.967 1.00 66.38  ? 494 TYR B OH    1 
ATOM   7644  N N     . GLU B  1 495 ? -3.114  17.948  242.001 1.00 68.91  ? 495 GLU B N     1 
ATOM   7645  C CA    . GLU B  1 495 ? -2.673  19.007  242.897 1.00 67.19  ? 495 GLU B CA    1 
ATOM   7646  C C     . GLU B  1 495 ? -1.566  19.869  242.316 1.00 66.00  ? 495 GLU B C     1 
ATOM   7647  O O     . GLU B  1 495 ? -1.248  20.921  242.861 1.00 66.89  ? 495 GLU B O     1 
ATOM   7648  C CB    . GLU B  1 495 ? -2.207  18.408  244.217 1.00 75.31  ? 495 GLU B CB    1 
ATOM   7649  C CG    . GLU B  1 495 ? -3.295  17.664  244.948 1.00 80.37  ? 495 GLU B CG    1 
ATOM   7650  C CD    . GLU B  1 495 ? -3.251  17.911  246.436 1.00 74.35  ? 495 GLU B CD    1 
ATOM   7651  O OE1   . GLU B  1 495 ? -2.140  18.027  246.990 1.00 76.49  ? 495 GLU B OE1   1 
ATOM   7652  O OE2   . GLU B  1 495 ? -4.326  18.007  247.053 1.00 77.35  ? 495 GLU B OE2   1 
ATOM   7653  N N     . ARG B  1 496 ? -0.966  19.419  241.221 1.00 65.30  ? 496 ARG B N     1 
ATOM   7654  C CA    . ARG B  1 496 ? -0.019  20.266  240.506 1.00 57.51  ? 496 ARG B CA    1 
ATOM   7655  C C     . ARG B  1 496 ? -0.788  21.179  239.555 1.00 57.84  ? 496 ARG B C     1 
ATOM   7656  O O     . ARG B  1 496 ? -0.370  22.303  239.281 1.00 58.17  ? 496 ARG B O     1 
ATOM   7657  C CB    . ARG B  1 496 ? 1.025   19.449  239.731 1.00 56.76  ? 496 ARG B CB    1 
ATOM   7658  C CG    . ARG B  1 496 ? 2.042   20.334  239.004 1.00 50.46  ? 496 ARG B CG    1 
ATOM   7659  C CD    . ARG B  1 496 ? 3.046   19.568  238.145 1.00 49.87  ? 496 ARG B CD    1 
ATOM   7660  N NE    . ARG B  1 496 ? 3.980   20.477  237.476 1.00 52.94  ? 496 ARG B NE    1 
ATOM   7661  C CZ    . ARG B  1 496 ? 4.864   20.108  236.553 1.00 49.09  ? 496 ARG B CZ    1 
ATOM   7662  N NH1   . ARG B  1 496 ? 4.942   18.841  236.173 1.00 53.33  ? 496 ARG B NH1   1 
ATOM   7663  N NH2   . ARG B  1 496 ? 5.669   21.010  236.006 1.00 45.62  ? 496 ARG B NH2   1 
ATOM   7664  N N     . LEU B  1 497 ? -1.923  20.693  239.064 1.00 57.14  ? 497 LEU B N     1 
ATOM   7665  C CA    . LEU B  1 497 ? -2.767  21.479  238.169 1.00 57.17  ? 497 LEU B CA    1 
ATOM   7666  C C     . LEU B  1 497 ? -3.284  22.734  238.863 1.00 53.97  ? 497 LEU B C     1 
ATOM   7667  O O     . LEU B  1 497 ? -3.456  23.776  238.231 1.00 54.47  ? 497 LEU B O     1 
ATOM   7668  C CB    . LEU B  1 497 ? -3.934  20.637  237.660 1.00 50.10  ? 497 LEU B CB    1 
ATOM   7669  C CG    . LEU B  1 497 ? -3.538  19.520  236.698 1.00 47.70  ? 497 LEU B CG    1 
ATOM   7670  C CD1   . LEU B  1 497 ? -4.693  18.569  236.490 1.00 49.52  ? 497 LEU B CD1   1 
ATOM   7671  C CD2   . LEU B  1 497 ? -3.081  20.093  235.371 1.00 42.66  ? 497 LEU B CD2   1 
ATOM   7672  N N     . ILE B  1 498 ? -3.533  22.620  240.164 1.00 56.19  ? 498 ILE B N     1 
ATOM   7673  C CA    . ILE B  1 498 ? -3.957  23.752  240.978 1.00 53.57  ? 498 ILE B CA    1 
ATOM   7674  C C     . ILE B  1 498 ? -2.853  24.803  241.040 1.00 57.57  ? 498 ILE B C     1 
ATOM   7675  O O     . ILE B  1 498 ? -3.125  26.004  240.977 1.00 61.17  ? 498 ILE B O     1 
ATOM   7676  C CB    . ILE B  1 498 ? -4.333  23.302  242.404 1.00 56.08  ? 498 ILE B CB    1 
ATOM   7677  C CG1   . ILE B  1 498 ? -5.451  22.260  242.353 1.00 56.67  ? 498 ILE B CG1   1 
ATOM   7678  C CG2   . ILE B  1 498 ? -4.748  24.488  243.258 1.00 59.30  ? 498 ILE B CG2   1 
ATOM   7679  C CD1   . ILE B  1 498 ? -5.789  21.670  243.700 1.00 66.35  ? 498 ILE B CD1   1 
ATOM   7680  N N     . ARG B  1 499 ? -1.608  24.343  241.159 1.00 55.53  ? 499 ARG B N     1 
ATOM   7681  C CA    . ARG B  1 499 ? -0.448  25.231  241.122 1.00 59.35  ? 499 ARG B CA    1 
ATOM   7682  C C     . ARG B  1 499 ? -0.405  26.014  239.814 1.00 57.50  ? 499 ARG B C     1 
ATOM   7683  O O     . ARG B  1 499 ? -0.242  27.233  239.816 1.00 59.83  ? 499 ARG B O     1 
ATOM   7684  C CB    . ARG B  1 499 ? 0.858   24.444  241.305 1.00 57.75  ? 499 ARG B CB    1 
ATOM   7685  C CG    . ARG B  1 499 ? 1.444   24.495  242.709 1.00 57.85  ? 499 ARG B CG    1 
ATOM   7686  C CD    . ARG B  1 499 ? 2.911   24.073  242.726 1.00 57.39  ? 499 ARG B CD    1 
ATOM   7687  N NE    . ARG B  1 499 ? 3.066   22.631  242.575 1.00 53.78  ? 499 ARG B NE    1 
ATOM   7688  C CZ    . ARG B  1 499 ? 3.922   22.057  241.735 1.00 56.54  ? 499 ARG B CZ    1 
ATOM   7689  N NH1   . ARG B  1 499 ? 4.707   22.800  240.967 1.00 56.23  ? 499 ARG B NH1   1 
ATOM   7690  N NH2   . ARG B  1 499 ? 3.997   20.735  241.658 1.00 64.08  ? 499 ARG B NH2   1 
ATOM   7691  N N     . ALA B  1 500 ? -0.561  25.303  238.702 1.00 56.41  ? 500 ALA B N     1 
ATOM   7692  C CA    . ALA B  1 500 ? -0.560  25.915  237.377 1.00 54.12  ? 500 ALA B CA    1 
ATOM   7693  C C     . ALA B  1 500 ? -1.718  26.891  237.200 1.00 47.13  ? 500 ALA B C     1 
ATOM   7694  O O     . ALA B  1 500 ? -1.552  27.967  236.626 1.00 49.53  ? 500 ALA B O     1 
ATOM   7695  C CB    . ALA B  1 500 ? -0.617  24.842  236.313 1.00 52.00  ? 500 ALA B CB    1 
ATOM   7696  N N     . LYS B  1 501 ? -2.889  26.496  237.689 1.00 51.79  ? 501 LYS B N     1 
ATOM   7697  C CA    . LYS B  1 501 ? -4.076  27.340  237.653 1.00 48.27  ? 501 LYS B CA    1 
ATOM   7698  C C     . LYS B  1 501 ? -3.840  28.665  238.377 1.00 54.94  ? 501 LYS B C     1 
ATOM   7699  O O     . LYS B  1 501 ? -4.266  29.723  237.914 1.00 52.03  ? 501 LYS B O     1 
ATOM   7700  C CB    . LYS B  1 501 ? -5.260  26.600  238.277 1.00 52.40  ? 501 LYS B CB    1 
ATOM   7701  C CG    . LYS B  1 501 ? -6.542  27.410  238.351 1.00 55.01  ? 501 LYS B CG    1 
ATOM   7702  C CD    . LYS B  1 501 ? -7.080  27.739  236.969 1.00 48.21  ? 501 LYS B CD    1 
ATOM   7703  C CE    . LYS B  1 501 ? -8.390  28.501  237.068 1.00 49.19  ? 501 LYS B CE    1 
ATOM   7704  N NZ    . LYS B  1 501 ? -9.004  28.766  235.737 1.00 42.66  ? 501 LYS B NZ    1 
ATOM   7705  N N     . THR B  1 502 ? -3.145  28.594  239.508 1.00 54.50  ? 502 THR B N     1 
ATOM   7706  C CA    . THR B  1 502 ? -2.874  29.764  240.333 1.00 56.74  ? 502 THR B CA    1 
ATOM   7707  C C     . THR B  1 502 ? -1.884  30.710  239.659 1.00 54.52  ? 502 THR B C     1 
ATOM   7708  O O     . THR B  1 502 ? -1.985  31.930  239.791 1.00 56.93  ? 502 THR B O     1 
ATOM   7709  C CB    . THR B  1 502 ? -2.334  29.342  241.711 1.00 60.98  ? 502 THR B CB    1 
ATOM   7710  O OG1   . THR B  1 502 ? -3.249  28.418  242.307 1.00 59.14  ? 502 THR B OG1   1 
ATOM   7711  C CG2   . THR B  1 502 ? -2.168  30.548  242.626 1.00 66.11  ? 502 THR B CG2   1 
ATOM   7712  N N     . LEU B  1 503 ? -0.936  30.139  238.924 1.00 54.09  ? 503 LEU B N     1 
ATOM   7713  C CA    . LEU B  1 503 ? 0.059   30.929  238.205 1.00 54.07  ? 503 LEU B CA    1 
ATOM   7714  C C     . LEU B  1 503 ? -0.550  31.695  237.037 1.00 48.12  ? 503 LEU B C     1 
ATOM   7715  O O     . LEU B  1 503 ? -0.216  32.857  236.806 1.00 54.09  ? 503 LEU B O     1 
ATOM   7716  C CB    . LEU B  1 503 ? 1.185   30.031  237.689 1.00 52.65  ? 503 LEU B CB    1 
ATOM   7717  C CG    . LEU B  1 503 ? 2.096   29.384  238.732 1.00 60.09  ? 503 LEU B CG    1 
ATOM   7718  C CD1   . LEU B  1 503 ? 3.073   28.414  238.079 1.00 50.91  ? 503 LEU B CD1   1 
ATOM   7719  C CD2   . LEU B  1 503 ? 2.839   30.456  239.509 1.00 59.28  ? 503 LEU B CD2   1 
ATOM   7720  N N     . ILE B  1 504 ? -1.443  31.037  236.304 1.00 46.91  ? 504 ILE B N     1 
ATOM   7721  C CA    . ILE B  1 504 ? -1.901  31.555  235.018 1.00 45.48  ? 504 ILE B CA    1 
ATOM   7722  C C     . ILE B  1 504 ? -3.297  32.183  235.066 1.00 42.25  ? 504 ILE B C     1 
ATOM   7723  O O     . ILE B  1 504 ? -3.608  33.073  234.275 1.00 41.20  ? 504 ILE B O     1 
ATOM   7724  C CB    . ILE B  1 504 ? -1.878  30.435  233.943 1.00 38.57  ? 504 ILE B CB    1 
ATOM   7725  C CG1   . ILE B  1 504 ? -1.855  31.038  232.539 1.00 34.91  ? 504 ILE B CG1   1 
ATOM   7726  C CG2   . ILE B  1 504 ? -3.030  29.451  234.135 1.00 40.10  ? 504 ILE B CG2   1 
ATOM   7727  C CD1   . ILE B  1 504 ? -0.596  31.814  232.254 1.00 36.57  ? 504 ILE B CD1   1 
ATOM   7728  N N     . ASP B  1 505 ? -4.130  31.729  235.996 1.00 46.69  ? 505 ASP B N     1 
ATOM   7729  C CA    . ASP B  1 505 ? -5.489  32.251  236.122 1.00 48.71  ? 505 ASP B CA    1 
ATOM   7730  C C     . ASP B  1 505 ? -5.923  32.306  237.583 1.00 46.96  ? 505 ASP B C     1 
ATOM   7731  O O     . ASP B  1 505 ? -6.880  31.639  237.971 1.00 47.63  ? 505 ASP B O     1 
ATOM   7732  C CB    . ASP B  1 505 ? -6.469  31.391  235.312 1.00 43.38  ? 505 ASP B CB    1 
ATOM   7733  C CG    . ASP B  1 505 ? -7.846  32.024  235.186 1.00 47.44  ? 505 ASP B CG    1 
ATOM   7734  O OD1   . ASP B  1 505 ? -7.949  33.261  235.314 1.00 45.06  ? 505 ASP B OD1   1 
ATOM   7735  O OD2   . ASP B  1 505 ? -8.826  31.283  234.955 1.00 43.85  ? 505 ASP B OD2   1 
ATOM   7736  N N     . PRO B  1 506 ? -5.220  33.104  238.406 1.00 51.06  ? 506 PRO B N     1 
ATOM   7737  C CA    . PRO B  1 506 ? -5.543  33.153  239.837 1.00 53.26  ? 506 PRO B CA    1 
ATOM   7738  C C     . PRO B  1 506 ? -6.959  33.655  240.124 1.00 57.33  ? 506 PRO B C     1 
ATOM   7739  O O     . PRO B  1 506 ? -7.582  33.213  241.092 1.00 60.02  ? 506 PRO B O     1 
ATOM   7740  C CB    . PRO B  1 506 ? -4.502  34.129  240.398 1.00 58.80  ? 506 PRO B CB    1 
ATOM   7741  C CG    . PRO B  1 506 ? -4.086  34.955  239.232 1.00 55.58  ? 506 PRO B CG    1 
ATOM   7742  C CD    . PRO B  1 506 ? -4.119  34.022  238.065 1.00 48.32  ? 506 PRO B CD    1 
ATOM   7743  N N     . ASN B  1 507 ? -7.456  34.561  239.288 1.00 47.38  ? 507 ASN B N     1 
ATOM   7744  C CA    . ASN B  1 507 ? -8.786  35.131  239.479 1.00 55.31  ? 507 ASN B CA    1 
ATOM   7745  C C     . ASN B  1 507 ? -9.878  34.281  238.834 1.00 52.48  ? 507 ASN B C     1 
ATOM   7746  O O     . ASN B  1 507 ? -11.048 34.665  238.830 1.00 53.19  ? 507 ASN B O     1 
ATOM   7747  C CB    . ASN B  1 507 ? -8.838  36.557  238.929 1.00 53.63  ? 507 ASN B CB    1 
ATOM   7748  C CG    . ASN B  1 507 ? -7.846  37.481  239.610 1.00 56.75  ? 507 ASN B CG    1 
ATOM   7749  O OD1   . ASN B  1 507 ? -7.029  38.128  238.953 1.00 58.54  ? 507 ASN B OD1   1 
ATOM   7750  N ND2   . ASN B  1 507 ? -7.908  37.543  240.934 1.00 62.55  ? 507 ASN B ND2   1 
ATOM   7751  N N     . ASN B  1 508 ? -9.480  33.134  238.286 1.00 49.42  ? 508 ASN B N     1 
ATOM   7752  C CA    . ASN B  1 508 ? -10.411 32.144  237.746 1.00 51.30  ? 508 ASN B CA    1 
ATOM   7753  C C     . ASN B  1 508 ? -11.354 32.720  236.688 1.00 46.36  ? 508 ASN B C     1 
ATOM   7754  O O     . ASN B  1 508 ? -12.566 32.512  236.742 1.00 47.66  ? 508 ASN B O     1 
ATOM   7755  C CB    . ASN B  1 508 ? -11.218 31.510  238.884 1.00 50.05  ? 508 ASN B CB    1 
ATOM   7756  C CG    . ASN B  1 508 ? -11.810 30.167  238.505 1.00 51.35  ? 508 ASN B CG    1 
ATOM   7757  O OD1   . ASN B  1 508 ? -11.306 29.483  237.618 1.00 50.83  ? 508 ASN B OD1   1 
ATOM   7758  N ND2   . ASN B  1 508 ? -12.887 29.783  239.180 1.00 51.93  ? 508 ASN B ND2   1 
ATOM   7759  N N     . VAL B  1 509 ? -10.785 33.448  235.731 1.00 44.50  ? 509 VAL B N     1 
ATOM   7760  C CA    . VAL B  1 509 ? -11.554 34.014  234.628 1.00 45.29  ? 509 VAL B CA    1 
ATOM   7761  C C     . VAL B  1 509 ? -12.071 32.897  233.726 1.00 45.35  ? 509 VAL B C     1 
ATOM   7762  O O     . VAL B  1 509 ? -13.179 32.976  233.192 1.00 45.29  ? 509 VAL B O     1 
ATOM   7763  C CB    . VAL B  1 509 ? -10.705 35.014  233.806 1.00 38.10  ? 509 VAL B CB    1 
ATOM   7764  C CG1   . VAL B  1 509 ? -11.418 35.427  232.526 1.00 39.76  ? 509 VAL B CG1   1 
ATOM   7765  C CG2   . VAL B  1 509 ? -10.383 36.234  234.647 1.00 46.83  ? 509 VAL B CG2   1 
ATOM   7766  N N     . PHE B  1 510 ? -11.271 31.846  233.582 1.00 38.47  ? 510 PHE B N     1 
ATOM   7767  C CA    . PHE B  1 510 ? -11.647 30.703  232.759 1.00 39.36  ? 510 PHE B CA    1 
ATOM   7768  C C     . PHE B  1 510 ? -12.141 29.555  233.632 1.00 41.30  ? 510 PHE B C     1 
ATOM   7769  O O     . PHE B  1 510 ? -11.348 28.830  234.232 1.00 43.36  ? 510 PHE B O     1 
ATOM   7770  C CB    . PHE B  1 510 ? -10.465 30.262  231.890 1.00 37.03  ? 510 PHE B CB    1 
ATOM   7771  C CG    . PHE B  1 510 ? -10.014 31.313  230.921 1.00 37.71  ? 510 PHE B CG    1 
ATOM   7772  C CD1   . PHE B  1 510 ? -10.566 31.389  229.653 1.00 35.58  ? 510 PHE B CD1   1 
ATOM   7773  C CD2   . PHE B  1 510 ? -9.059  32.245  231.289 1.00 36.97  ? 510 PHE B CD2   1 
ATOM   7774  C CE1   . PHE B  1 510 ? -10.160 32.368  228.763 1.00 40.97  ? 510 PHE B CE1   1 
ATOM   7775  C CE2   . PHE B  1 510 ? -8.652  33.227  230.407 1.00 34.99  ? 510 PHE B CE2   1 
ATOM   7776  C CZ    . PHE B  1 510 ? -9.200  33.288  229.139 1.00 35.35  ? 510 PHE B CZ    1 
ATOM   7777  N N     . ASN B  1 511 ? -13.459 29.399  233.693 1.00 39.87  ? 511 ASN B N     1 
ATOM   7778  C CA    . ASN B  1 511 ? -14.072 28.442  234.602 1.00 44.03  ? 511 ASN B CA    1 
ATOM   7779  C C     . ASN B  1 511 ? -15.293 27.740  234.014 1.00 44.40  ? 511 ASN B C     1 
ATOM   7780  O O     . ASN B  1 511 ? -15.924 28.241  233.082 1.00 41.42  ? 511 ASN B O     1 
ATOM   7781  C CB    . ASN B  1 511 ? -14.472 29.142  235.904 1.00 47.08  ? 511 ASN B CB    1 
ATOM   7782  C CG    . ASN B  1 511 ? -15.569 30.170  235.699 1.00 46.40  ? 511 ASN B CG    1 
ATOM   7783  O OD1   . ASN B  1 511 ? -16.751 29.833  235.659 1.00 47.17  ? 511 ASN B OD1   1 
ATOM   7784  N ND2   . ASN B  1 511 ? -15.180 31.432  235.564 1.00 44.25  ? 511 ASN B ND2   1 
ATOM   7785  N N     . HIS B  1 512 ? -15.610 26.577  234.575 1.00 45.50  ? 512 HIS B N     1 
ATOM   7786  C CA    . HIS B  1 512 ? -16.796 25.805  234.215 1.00 44.36  ? 512 HIS B CA    1 
ATOM   7787  C C     . HIS B  1 512 ? -17.033 24.808  235.370 1.00 48.62  ? 512 HIS B C     1 
ATOM   7788  O O     . HIS B  1 512 ? -16.225 24.769  236.296 1.00 50.35  ? 512 HIS B O     1 
ATOM   7789  C CB    . HIS B  1 512 ? -16.614 25.136  232.838 1.00 44.66  ? 512 HIS B CB    1 
ATOM   7790  C CG    . HIS B  1 512 ? -15.478 24.168  232.766 1.00 44.89  ? 512 HIS B CG    1 
ATOM   7791  N ND1   . HIS B  1 512 ? -15.485 22.958  233.425 1.00 46.83  ? 512 HIS B ND1   1 
ATOM   7792  C CD2   . HIS B  1 512 ? -14.308 24.218  232.086 1.00 43.97  ? 512 HIS B CD2   1 
ATOM   7793  C CE1   . HIS B  1 512 ? -14.364 22.310  233.165 1.00 49.89  ? 512 HIS B CE1   1 
ATOM   7794  N NE2   . HIS B  1 512 ? -13.632 23.054  232.356 1.00 48.21  ? 512 HIS B NE2   1 
ATOM   7795  N N     . PRO B  1 513 ? -18.143 24.034  235.354 1.00 48.63  ? 513 PRO B N     1 
ATOM   7796  C CA    . PRO B  1 513 ? -18.463 23.222  236.542 1.00 53.88  ? 513 PRO B CA    1 
ATOM   7797  C C     . PRO B  1 513 ? -17.354 22.317  237.094 1.00 55.11  ? 513 PRO B C     1 
ATOM   7798  O O     . PRO B  1 513 ? -17.374 22.022  238.289 1.00 57.20  ? 513 PRO B O     1 
ATOM   7799  C CB    . PRO B  1 513 ? -19.631 22.360  236.059 1.00 50.40  ? 513 PRO B CB    1 
ATOM   7800  C CG    . PRO B  1 513 ? -20.322 23.215  235.085 1.00 49.41  ? 513 PRO B CG    1 
ATOM   7801  C CD    . PRO B  1 513 ? -19.243 23.985  234.371 1.00 50.50  ? 513 PRO B CD    1 
ATOM   7802  N N     . GLN B  1 514 ? -16.414 21.882  236.263 1.00 51.26  ? 514 GLN B N     1 
ATOM   7803  C CA    . GLN B  1 514 ? -15.364 20.990  236.744 1.00 52.72  ? 514 GLN B CA    1 
ATOM   7804  C C     . GLN B  1 514 ? -13.966 21.515  236.434 1.00 53.69  ? 514 GLN B C     1 
ATOM   7805  O O     . GLN B  1 514 ? -12.991 20.763  236.451 1.00 52.95  ? 514 GLN B O     1 
ATOM   7806  C CB    . GLN B  1 514 ? -15.545 19.589  236.157 1.00 51.95  ? 514 GLN B CB    1 
ATOM   7807  C CG    . GLN B  1 514 ? -16.807 18.887  236.637 1.00 54.79  ? 514 GLN B CG    1 
ATOM   7808  C CD    . GLN B  1 514 ? -16.831 17.416  236.280 1.00 57.60  ? 514 GLN B CD    1 
ATOM   7809  O OE1   . GLN B  1 514 ? -15.921 16.912  235.628 1.00 57.54  ? 514 GLN B OE1   1 
ATOM   7810  N NE2   . GLN B  1 514 ? -17.873 16.716  236.714 1.00 61.73  ? 514 GLN B NE2   1 
ATOM   7811  N N     . SER B  1 515 ? -13.878 22.812  236.160 1.00 50.37  ? 515 SER B N     1 
ATOM   7812  C CA    . SER B  1 515 ? -12.595 23.464  235.939 1.00 49.37  ? 515 SER B CA    1 
ATOM   7813  C C     . SER B  1 515 ? -11.724 23.386  237.190 1.00 50.95  ? 515 SER B C     1 
ATOM   7814  O O     . SER B  1 515 ? -12.233 23.416  238.312 1.00 49.59  ? 515 SER B O     1 
ATOM   7815  C CB    . SER B  1 515 ? -12.806 24.920  235.530 1.00 50.57  ? 515 SER B CB    1 
ATOM   7816  O OG    . SER B  1 515 ? -13.576 25.611  236.500 1.00 47.81  ? 515 SER B OG    1 
ATOM   7817  N N     . ILE B  1 516 ? -10.414 23.272  236.990 1.00 50.69  ? 516 ILE B N     1 
ATOM   7818  C CA    . ILE B  1 516 ? -9.468  23.256  238.099 1.00 49.81  ? 516 ILE B CA    1 
ATOM   7819  C C     . ILE B  1 516 ? -9.550  24.566  238.876 1.00 49.98  ? 516 ILE B C     1 
ATOM   7820  O O     . ILE B  1 516 ? -9.374  25.638  238.303 1.00 52.91  ? 516 ILE B O     1 
ATOM   7821  C CB    . ILE B  1 516 ? -8.021  23.036  237.610 1.00 50.59  ? 516 ILE B CB    1 
ATOM   7822  C CG1   . ILE B  1 516 ? -7.910  21.725  236.828 1.00 48.29  ? 516 ILE B CG1   1 
ATOM   7823  C CG2   . ILE B  1 516 ? -7.057  23.031  238.784 1.00 49.52  ? 516 ILE B CG2   1 
ATOM   7824  C CD1   . ILE B  1 516 ? -8.025  20.490  237.693 1.00 52.03  ? 516 ILE B CD1   1 
ATOM   7825  N N     . PRO B  1 517 ? -9.843  24.486  240.182 1.00 51.42  ? 517 PRO B N     1 
ATOM   7826  C CA    . PRO B  1 517 ? -9.898  25.702  240.997 1.00 53.92  ? 517 PRO B CA    1 
ATOM   7827  C C     . PRO B  1 517 ? -8.500  26.200  241.353 1.00 56.96  ? 517 PRO B C     1 
ATOM   7828  O O     . PRO B  1 517 ? -7.571  25.396  241.403 1.00 56.24  ? 517 PRO B O     1 
ATOM   7829  C CB    . PRO B  1 517 ? -10.652 25.246  242.245 1.00 54.26  ? 517 PRO B CB    1 
ATOM   7830  C CG    . PRO B  1 517 ? -10.301 23.805  242.369 1.00 55.42  ? 517 PRO B CG    1 
ATOM   7831  C CD    . PRO B  1 517 ? -10.211 23.287  240.957 1.00 51.93  ? 517 PRO B CD    1 
ATOM   7832  N N     . PRO B  1 518 ? -8.349  27.511  241.590 1.00 61.96  ? 518 PRO B N     1 
ATOM   7833  C CA    . PRO B  1 518 ? -7.043  28.053  241.983 1.00 58.37  ? 518 PRO B CA    1 
ATOM   7834  C C     . PRO B  1 518 ? -6.687  27.732  243.435 1.00 62.96  ? 518 PRO B C     1 
ATOM   7835  O O     . PRO B  1 518 ? -7.548  27.265  244.181 1.00 63.73  ? 518 PRO B O     1 
ATOM   7836  C CB    . PRO B  1 518 ? -7.220  29.560  241.787 1.00 57.46  ? 518 PRO B CB    1 
ATOM   7837  C CG    . PRO B  1 518 ? -8.679  29.786  241.986 1.00 58.70  ? 518 PRO B CG    1 
ATOM   7838  C CD    . PRO B  1 518 ? -9.358  28.571  241.416 1.00 54.79  ? 518 PRO B CD    1 
ATOM   7839  N N     . MET B  1 519 ? -5.436  27.986  243.817 1.00 65.83  ? 519 MET B N     1 
ATOM   7840  C CA    . MET B  1 519 ? -4.945  27.724  245.172 1.00 69.48  ? 519 MET B CA    1 
ATOM   7841  C C     . MET B  1 519 ? -5.838  28.361  246.232 1.00 76.93  ? 519 MET B C     1 
ATOM   7842  O O     . MET B  1 519 ? -6.461  27.670  247.038 1.00 85.78  ? 519 MET B O     1 
ATOM   7843  C CB    . MET B  1 519 ? -3.514  28.245  245.314 1.00 68.63  ? 519 MET B CB    1 
ATOM   7844  C CG    . MET B  1 519 ? -2.749  27.746  246.517 1.00 66.58  ? 519 MET B CG    1 
ATOM   7845  S SD    . MET B  1 519 ? -1.086  28.429  246.477 1.00 73.22  ? 519 MET B SD    1 
ATOM   7846  C CE    . MET B  1 519 ? -1.464  30.177  246.566 1.00 74.64  ? 519 MET B CE    1 
ATOM   7847  N N     . ALA B  1 520 ? -5.888  29.687  246.227 1.00 79.53  ? 520 ALA B N     1 
ATOM   7848  C CA    . ALA B  1 520 ? -6.828  30.421  247.058 1.00 83.37  ? 520 ALA B CA    1 
ATOM   7849  C C     . ALA B  1 520 ? -7.730  31.238  246.149 1.00 82.04  ? 520 ALA B C     1 
ATOM   7850  O O     . ALA B  1 520 ? -7.845  30.946  244.957 1.00 77.82  ? 520 ALA B O     1 
ATOM   7851  C CB    . ALA B  1 520 ? -6.098  31.316  248.047 1.00 82.92  ? 520 ALA B CB    1 
ATOM   7852  N N     . ASN B  1 521 ? -8.357  32.275  246.692 1.00 89.50  ? 521 ASN B N     1 
ATOM   7853  C CA    . ASN B  1 521 ? -9.131  33.186  245.859 1.00 84.82  ? 521 ASN B CA    1 
ATOM   7854  C C     . ASN B  1 521 ? -8.209  34.190  245.168 1.00 86.38  ? 521 ASN B C     1 
ATOM   7855  O O     . ASN B  1 521 ? -8.630  35.275  244.765 1.00 88.62  ? 521 ASN B O     1 
ATOM   7856  C CB    . ASN B  1 521 ? -10.207 33.893  246.685 1.00 85.40  ? 521 ASN B CB    1 
ATOM   7857  C CG    . ASN B  1 521 ? -11.353 32.965  247.056 1.00 93.73  ? 521 ASN B CG    1 
ATOM   7858  O OD1   . ASN B  1 521 ? -11.595 31.961  246.382 1.00 94.15  ? 521 ASN B OD1   1 
ATOM   7859  N ND2   . ASN B  1 521 ? -12.065 33.298  248.125 1.00 93.11  ? 521 ASN B ND2   1 
ATOM   7860  N N     . PHE B  1 522 ? -6.939  33.808  245.060 1.00 88.75  ? 522 PHE B N     1 
ATOM   7861  C CA    . PHE B  1 522 ? -6.001  34.432  244.142 1.00 85.49  ? 522 PHE B CA    1 
ATOM   7862  C C     . PHE B  1 522 ? -4.993  33.391  243.664 1.00 81.72  ? 522 PHE B C     1 
ATOM   7863  O O     . PHE B  1 522 ? -4.639  32.467  244.398 1.00 79.50  ? 522 PHE B O     1 
ATOM   7864  C CB    . PHE B  1 522 ? -5.275  35.613  244.785 1.00 87.70  ? 522 PHE B CB    1 
ATOM   7865  C CG    . PHE B  1 522 ? -4.428  36.389  243.815 1.00 93.95  ? 522 PHE B CG    1 
ATOM   7866  C CD1   . PHE B  1 522 ? -5.020  37.118  242.797 1.00 92.56  ? 522 PHE B CD1   1 
ATOM   7867  C CD2   . PHE B  1 522 ? -3.045  36.386  243.912 1.00 94.74  ? 522 PHE B CD2   1 
ATOM   7868  C CE1   . PHE B  1 522 ? -4.252  37.832  241.895 1.00 89.33  ? 522 PHE B CE1   1 
ATOM   7869  C CE2   . PHE B  1 522 ? -2.270  37.100  243.012 1.00 91.78  ? 522 PHE B CE2   1 
ATOM   7870  C CZ    . PHE B  1 522 ? -2.876  37.823  242.003 1.00 91.11  ? 522 PHE B CZ    1 
ATOM   7871  N N     . ASN C  1 25  ? -17.999 37.427  164.745 1.00 74.13  ? 25  ASN C N     1 
ATOM   7872  C CA    . ASN C  1 25  ? -19.455 37.491  164.685 1.00 63.04  ? 25  ASN C CA    1 
ATOM   7873  C C     . ASN C  1 25  ? -20.081 37.706  166.060 1.00 50.90  ? 25  ASN C C     1 
ATOM   7874  O O     . ASN C  1 25  ? -21.265 38.028  166.167 1.00 62.93  ? 25  ASN C O     1 
ATOM   7875  C CB    . ASN C  1 25  ? -20.024 36.215  164.059 1.00 63.49  ? 25  ASN C CB    1 
ATOM   7876  C CG    . ASN C  1 25  ? -20.362 36.381  162.590 1.00 72.09  ? 25  ASN C CG    1 
ATOM   7877  O OD1   . ASN C  1 25  ? -19.985 35.553  161.760 1.00 78.78  ? 25  ASN C OD1   1 
ATOM   7878  N ND2   . ASN C  1 25  ? -21.080 37.451  162.261 1.00 78.47  ? 25  ASN C ND2   1 
ATOM   7879  N N     . ASP C  1 26  ? -19.281 37.508  167.103 1.00 49.72  ? 26  ASP C N     1 
ATOM   7880  C CA    . ASP C  1 26  ? -19.713 37.730  168.476 1.00 42.76  ? 26  ASP C CA    1 
ATOM   7881  C C     . ASP C  1 26  ? -18.864 38.839  169.092 1.00 43.88  ? 26  ASP C C     1 
ATOM   7882  O O     . ASP C  1 26  ? -17.827 38.579  169.710 1.00 39.58  ? 26  ASP C O     1 
ATOM   7883  C CB    . ASP C  1 26  ? -19.600 36.437  169.287 1.00 37.87  ? 26  ASP C CB    1 
ATOM   7884  C CG    . ASP C  1 26  ? -20.211 36.551  170.671 1.00 38.77  ? 26  ASP C CG    1 
ATOM   7885  O OD1   . ASP C  1 26  ? -20.531 37.675  171.114 1.00 42.82  ? 26  ASP C OD1   1 
ATOM   7886  O OD2   . ASP C  1 26  ? -20.366 35.498  171.325 1.00 48.02  ? 26  ASP C OD2   1 
ATOM   7887  N N     . LEU C  1 27  ? -19.317 40.076  168.925 1.00 38.12  ? 27  LEU C N     1 
ATOM   7888  C CA    . LEU C  1 27  ? -18.525 41.233  169.315 1.00 38.51  ? 27  LEU C CA    1 
ATOM   7889  C C     . LEU C  1 27  ? -18.315 41.319  170.827 1.00 41.40  ? 27  LEU C C     1 
ATOM   7890  O O     . LEU C  1 27  ? -17.203 41.580  171.292 1.00 35.56  ? 27  LEU C O     1 
ATOM   7891  C CB    . LEU C  1 27  ? -19.179 42.518  168.805 1.00 39.19  ? 27  LEU C CB    1 
ATOM   7892  C CG    . LEU C  1 27  ? -18.441 43.796  169.204 1.00 35.62  ? 27  LEU C CG    1 
ATOM   7893  C CD1   . LEU C  1 27  ? -17.031 43.804  168.631 1.00 40.11  ? 27  LEU C CD1   1 
ATOM   7894  C CD2   . LEU C  1 27  ? -19.210 45.023  168.755 1.00 36.03  ? 27  LEU C CD2   1 
ATOM   7895  N N     . LEU C  1 28  ? -19.376 41.088  171.593 1.00 34.57  ? 28  LEU C N     1 
ATOM   7896  C CA    . LEU C  1 28  ? -19.295 41.211  173.047 1.00 38.85  ? 28  LEU C CA    1 
ATOM   7897  C C     . LEU C  1 28  ? -18.376 40.162  173.667 1.00 38.52  ? 28  LEU C C     1 
ATOM   7898  O O     . LEU C  1 28  ? -17.730 40.421  174.680 1.00 39.99  ? 28  LEU C O     1 
ATOM   7899  C CB    . LEU C  1 28  ? -20.690 41.120  173.676 1.00 35.21  ? 28  LEU C CB    1 
ATOM   7900  C CG    . LEU C  1 28  ? -21.671 42.222  173.270 1.00 42.13  ? 28  LEU C CG    1 
ATOM   7901  C CD1   . LEU C  1 28  ? -22.937 42.178  174.122 1.00 34.91  ? 28  LEU C CD1   1 
ATOM   7902  C CD2   . LEU C  1 28  ? -21.012 43.587  173.354 1.00 33.46  ? 28  LEU C CD2   1 
ATOM   7903  N N     . SER C  1 29  ? -18.320 38.981  173.060 1.00 37.94  ? 29  SER C N     1 
ATOM   7904  C CA    . SER C  1 29  ? -17.431 37.935  173.549 1.00 40.31  ? 29  SER C CA    1 
ATOM   7905  C C     . SER C  1 29  ? -15.991 38.233  173.142 1.00 38.64  ? 29  SER C C     1 
ATOM   7906  O O     . SER C  1 29  ? -15.058 37.962  173.894 1.00 40.15  ? 29  SER C O     1 
ATOM   7907  C CB    . SER C  1 29  ? -17.861 36.565  173.026 1.00 38.71  ? 29  SER C CB    1 
ATOM   7908  O OG    . SER C  1 29  ? -17.213 35.521  173.730 1.00 50.81  ? 29  SER C OG    1 
ATOM   7909  N N     . CYS C  1 30  ? -15.821 38.790  171.947 1.00 32.69  ? 30  CYS C N     1 
ATOM   7910  C CA    . CYS C  1 30  ? -14.505 39.210  171.477 1.00 38.45  ? 30  CYS C CA    1 
ATOM   7911  C C     . CYS C  1 30  ? -13.884 40.204  172.451 1.00 39.99  ? 30  CYS C C     1 
ATOM   7912  O O     . CYS C  1 30  ? -12.745 40.031  172.887 1.00 35.63  ? 30  CYS C O     1 
ATOM   7913  C CB    . CYS C  1 30  ? -14.599 39.827  170.081 1.00 38.31  ? 30  CYS C CB    1 
ATOM   7914  S SG    . CYS C  1 30  ? -13.013 40.349  169.394 1.00 36.50  ? 30  CYS C SG    1 
ATOM   7915  N N     . LEU C  1 31  ? -14.652 41.234  172.792 1.00 34.52  ? 31  LEU C N     1 
ATOM   7916  C CA    . LEU C  1 31  ? -14.221 42.252  173.745 1.00 35.46  ? 31  LEU C CA    1 
ATOM   7917  C C     . LEU C  1 31  ? -13.857 41.656  175.101 1.00 40.83  ? 31  LEU C C     1 
ATOM   7918  O O     . LEU C  1 31  ? -12.865 42.052  175.712 1.00 44.08  ? 31  LEU C O     1 
ATOM   7919  C CB    . LEU C  1 31  ? -15.311 43.309  173.916 1.00 38.66  ? 31  LEU C CB    1 
ATOM   7920  C CG    . LEU C  1 31  ? -15.634 44.107  172.655 1.00 35.64  ? 31  LEU C CG    1 
ATOM   7921  C CD1   . LEU C  1 31  ? -16.883 44.949  172.868 1.00 38.16  ? 31  LEU C CD1   1 
ATOM   7922  C CD2   . LEU C  1 31  ? -14.445 44.973  172.268 1.00 35.71  ? 31  LEU C CD2   1 
ATOM   7923  N N     . THR C  1 32  ? -14.663 40.706  175.565 1.00 41.46  ? 32  THR C N     1 
ATOM   7924  C CA    . THR C  1 32  ? -14.417 40.047  176.842 1.00 41.53  ? 32  THR C CA    1 
ATOM   7925  C C     . THR C  1 32  ? -13.118 39.247  176.808 1.00 39.92  ? 32  THR C C     1 
ATOM   7926  O O     . THR C  1 32  ? -12.311 39.319  177.734 1.00 39.96  ? 32  THR C O     1 
ATOM   7927  C CB    . THR C  1 32  ? -15.580 39.112  177.228 1.00 39.85  ? 32  THR C CB    1 
ATOM   7928  O OG1   . THR C  1 32  ? -16.795 39.868  177.305 1.00 39.38  ? 32  THR C OG1   1 
ATOM   7929  C CG2   . THR C  1 32  ? -15.312 38.441  178.573 1.00 36.08  ? 32  THR C CG2   1 
ATOM   7930  N N     . PHE C  1 33  ? -12.916 38.489  175.736 1.00 38.01  ? 33  PHE C N     1 
ATOM   7931  C CA    . PHE C  1 33  ? -11.681 37.730  175.565 1.00 36.33  ? 33  PHE C CA    1 
ATOM   7932  C C     . PHE C  1 33  ? -10.480 38.657  175.384 1.00 39.96  ? 33  PHE C C     1 
ATOM   7933  O O     . PHE C  1 33  ? -9.355  38.301  175.731 1.00 40.03  ? 33  PHE C O     1 
ATOM   7934  C CB    . PHE C  1 33  ? -11.785 36.780  174.371 1.00 34.60  ? 33  PHE C CB    1 
ATOM   7935  C CG    . PHE C  1 33  ? -12.372 35.439  174.709 1.00 40.91  ? 33  PHE C CG    1 
ATOM   7936  C CD1   . PHE C  1 33  ? -11.594 34.460  175.305 1.00 38.21  ? 33  PHE C CD1   1 
ATOM   7937  C CD2   . PHE C  1 33  ? -13.697 35.153  174.425 1.00 42.17  ? 33  PHE C CD2   1 
ATOM   7938  C CE1   . PHE C  1 33  ? -12.126 33.220  175.612 1.00 41.07  ? 33  PHE C CE1   1 
ATOM   7939  C CE2   . PHE C  1 33  ? -14.236 33.916  174.731 1.00 43.68  ? 33  PHE C CE2   1 
ATOM   7940  C CZ    . PHE C  1 33  ? -13.452 32.950  175.326 1.00 47.13  ? 33  PHE C CZ    1 
ATOM   7941  N N     . ASN C  1 34  ? -10.724 39.844  174.834 1.00 38.56  ? 34  ASN C N     1 
ATOM   7942  C CA    . ASN C  1 34  ? -9.661  40.820  174.620 1.00 37.95  ? 34  ASN C CA    1 
ATOM   7943  C C     . ASN C  1 34  ? -9.418  41.691  175.844 1.00 39.60  ? 34  ASN C C     1 
ATOM   7944  O O     . ASN C  1 34  ? -8.580  42.593  175.820 1.00 40.74  ? 34  ASN C O     1 
ATOM   7945  C CB    . ASN C  1 34  ? -9.975  41.699  173.408 1.00 34.08  ? 34  ASN C CB    1 
ATOM   7946  C CG    . ASN C  1 34  ? -9.603  41.033  172.099 1.00 33.25  ? 34  ASN C CG    1 
ATOM   7947  O OD1   . ASN C  1 34  ? -8.618  41.404  171.459 1.00 35.43  ? 34  ASN C OD1   1 
ATOM   7948  N ND2   . ASN C  1 34  ? -10.376 40.033  171.702 1.00 34.31  ? 34  ASN C ND2   1 
ATOM   7949  N N     . GLY C  1 35  ? -10.143 41.409  176.920 1.00 36.24  ? 35  GLY C N     1 
ATOM   7950  C CA    . GLY C  1 35  ? -9.948  42.123  178.168 1.00 44.11  ? 35  GLY C CA    1 
ATOM   7951  C C     . GLY C  1 35  ? -10.530 43.522  178.172 1.00 45.28  ? 35  GLY C C     1 
ATOM   7952  O O     . GLY C  1 35  ? -10.131 44.370  178.971 1.00 43.22  ? 35  GLY C O     1 
ATOM   7953  N N     . VAL C  1 36  ? -11.475 43.768  177.274 1.00 37.72  ? 36  VAL C N     1 
ATOM   7954  C CA    . VAL C  1 36  ? -12.177 45.044  177.243 1.00 42.14  ? 36  VAL C CA    1 
ATOM   7955  C C     . VAL C  1 36  ? -13.576 44.855  177.816 1.00 45.60  ? 36  VAL C C     1 
ATOM   7956  O O     . VAL C  1 36  ? -14.485 44.418  177.116 1.00 37.62  ? 36  VAL C O     1 
ATOM   7957  C CB    . VAL C  1 36  ? -12.267 45.613  175.819 1.00 36.78  ? 36  VAL C CB    1 
ATOM   7958  C CG1   . VAL C  1 36  ? -12.867 47.001  175.856 1.00 38.61  ? 36  VAL C CG1   1 
ATOM   7959  C CG2   . VAL C  1 36  ? -10.892 45.649  175.173 1.00 34.38  ? 36  VAL C CG2   1 
ATOM   7960  N N     . ARG C  1 37  ? -13.740 45.184  179.092 1.00 46.18  ? 37  ARG C N     1 
ATOM   7961  C CA    . ARG C  1 37  ? -14.967 44.850  179.809 1.00 49.23  ? 37  ARG C CA    1 
ATOM   7962  C C     . ARG C  1 37  ? -15.983 45.988  179.888 1.00 50.35  ? 37  ARG C C     1 
ATOM   7963  O O     . ARG C  1 37  ? -17.185 45.739  179.990 1.00 48.81  ? 37  ARG C O     1 
ATOM   7964  C CB    . ARG C  1 37  ? -14.614 44.367  181.214 1.00 55.09  ? 37  ARG C CB    1 
ATOM   7965  C CG    . ARG C  1 37  ? -13.947 43.005  181.200 1.00 54.48  ? 37  ARG C CG    1 
ATOM   7966  C CD    . ARG C  1 37  ? -13.058 42.796  182.404 1.00 60.82  ? 37  ARG C CD    1 
ATOM   7967  N NE    . ARG C  1 37  ? -12.207 41.624  182.222 1.00 68.21  ? 37  ARG C NE    1 
ATOM   7968  C CZ    . ARG C  1 37  ? -10.879 41.649  182.236 1.00 72.00  ? 37  ARG C CZ    1 
ATOM   7969  N NH1   . ARG C  1 37  ? -10.195 40.527  182.056 1.00 63.65  ? 37  ARG C NH1   1 
ATOM   7970  N NH2   . ARG C  1 37  ? -10.232 42.791  182.434 1.00 62.64  ? 37  ARG C NH2   1 
ATOM   7971  N N     . ASN C  1 38  ? -15.519 47.232  179.831 1.00 42.98  ? 38  ASN C N     1 
ATOM   7972  C CA    . ASN C  1 38  ? -16.446 48.357  179.871 1.00 47.71  ? 38  ASN C CA    1 
ATOM   7973  C C     . ASN C  1 38  ? -17.124 48.564  178.517 1.00 43.59  ? 38  ASN C C     1 
ATOM   7974  O O     . ASN C  1 38  ? -16.654 49.337  177.683 1.00 39.59  ? 38  ASN C O     1 
ATOM   7975  C CB    . ASN C  1 38  ? -15.732 49.639  180.312 1.00 48.20  ? 38  ASN C CB    1 
ATOM   7976  C CG    . ASN C  1 38  ? -16.699 50.703  180.813 1.00 53.29  ? 38  ASN C CG    1 
ATOM   7977  O OD1   . ASN C  1 38  ? -17.797 50.864  180.277 1.00 52.76  ? 38  ASN C OD1   1 
ATOM   7978  N ND2   . ASN C  1 38  ? -16.298 51.429  181.854 1.00 56.41  ? 38  ASN C ND2   1 
ATOM   7979  N N     . HIS C  1 39  ? -18.230 47.856  178.311 1.00 43.50  ? 39  HIS C N     1 
ATOM   7980  C CA    . HIS C  1 39  ? -19.035 47.994  177.102 1.00 41.83  ? 39  HIS C CA    1 
ATOM   7981  C C     . HIS C  1 39  ? -20.507 47.759  177.430 1.00 46.11  ? 39  HIS C C     1 
ATOM   7982  O O     . HIS C  1 39  ? -20.830 46.927  178.278 1.00 47.24  ? 39  HIS C O     1 
ATOM   7983  C CB    . HIS C  1 39  ? -18.559 47.021  176.019 1.00 41.31  ? 39  HIS C CB    1 
ATOM   7984  C CG    . HIS C  1 39  ? -18.464 45.600  176.480 1.00 43.69  ? 39  HIS C CG    1 
ATOM   7985  N ND1   . HIS C  1 39  ? -19.554 44.757  176.523 1.00 42.19  ? 39  HIS C ND1   1 
ATOM   7986  C CD2   . HIS C  1 39  ? -17.410 44.874  176.919 1.00 42.33  ? 39  HIS C CD2   1 
ATOM   7987  C CE1   . HIS C  1 39  ? -19.175 43.573  176.968 1.00 38.95  ? 39  HIS C CE1   1 
ATOM   7988  N NE2   . HIS C  1 39  ? -17.878 43.617  177.216 1.00 49.59  ? 39  HIS C NE2   1 
ATOM   7989  N N     . THR C  1 40  ? -21.389 48.515  176.776 1.00 46.19  ? 40  THR C N     1 
ATOM   7990  C CA    . THR C  1 40  ? -22.837 48.431  176.992 1.00 41.67  ? 40  THR C CA    1 
ATOM   7991  C C     . THR C  1 40  ? -23.591 48.556  175.665 1.00 42.64  ? 40  THR C C     1 
ATOM   7992  O O     . THR C  1 40  ? -23.264 49.414  174.848 1.00 41.37  ? 40  THR C O     1 
ATOM   7993  C CB    . THR C  1 40  ? -23.348 49.538  177.946 1.00 52.82  ? 40  THR C CB    1 
ATOM   7994  O OG1   . THR C  1 40  ? -23.228 50.814  177.305 1.00 52.45  ? 40  THR C OG1   1 
ATOM   7995  C CG2   . THR C  1 40  ? -22.564 49.556  179.248 1.00 49.86  ? 40  THR C CG2   1 
ATOM   7996  N N     . VAL C  1 41  ? -24.605 47.719  175.457 1.00 37.36  ? 41  VAL C N     1 
ATOM   7997  C CA    . VAL C  1 41  ? -25.376 47.759  174.212 1.00 40.04  ? 41  VAL C CA    1 
ATOM   7998  C C     . VAL C  1 41  ? -26.461 48.837  174.239 1.00 40.10  ? 41  VAL C C     1 
ATOM   7999  O O     . VAL C  1 41  ? -26.769 49.388  175.295 1.00 39.46  ? 41  VAL C O     1 
ATOM   8000  C CB    . VAL C  1 41  ? -26.035 46.403  173.910 1.00 47.63  ? 41  VAL C CB    1 
ATOM   8001  C CG1   . VAL C  1 41  ? -24.977 45.326  173.751 1.00 44.06  ? 41  VAL C CG1   1 
ATOM   8002  C CG2   . VAL C  1 41  ? -27.036 46.036  175.004 1.00 38.78  ? 41  VAL C CG2   1 
ATOM   8003  N N     . PHE C  1 42  ? -27.036 49.127  173.073 1.00 37.17  ? 42  PHE C N     1 
ATOM   8004  C CA    . PHE C  1 42  ? -28.041 50.182  172.950 1.00 49.17  ? 42  PHE C CA    1 
ATOM   8005  C C     . PHE C  1 42  ? -29.260 49.936  173.830 1.00 48.66  ? 42  PHE C C     1 
ATOM   8006  O O     . PHE C  1 42  ? -29.664 48.794  174.056 1.00 47.08  ? 42  PHE C O     1 
ATOM   8007  C CB    . PHE C  1 42  ? -28.488 50.344  171.488 1.00 45.78  ? 42  PHE C CB    1 
ATOM   8008  C CG    . PHE C  1 42  ? -29.615 51.334  171.302 1.00 50.72  ? 42  PHE C CG    1 
ATOM   8009  C CD1   . PHE C  1 42  ? -29.351 52.684  171.142 1.00 46.05  ? 42  PHE C CD1   1 
ATOM   8010  C CD2   . PHE C  1 42  ? -30.937 50.915  171.287 1.00 49.58  ? 42  PHE C CD2   1 
ATOM   8011  C CE1   . PHE C  1 42  ? -30.379 53.596  170.982 1.00 55.91  ? 42  PHE C CE1   1 
ATOM   8012  C CE2   . PHE C  1 42  ? -31.968 51.825  171.124 1.00 50.58  ? 42  PHE C CE2   1 
ATOM   8013  C CZ    . PHE C  1 42  ? -31.687 53.165  170.969 1.00 52.67  ? 42  PHE C CZ    1 
ATOM   8014  N N     . SER C  1 43  ? -29.830 51.031  174.321 1.00 50.26  ? 43  SER C N     1 
ATOM   8015  C CA    . SER C  1 43  ? -31.089 51.012  175.054 1.00 51.49  ? 43  SER C CA    1 
ATOM   8016  C C     . SER C  1 43  ? -31.684 52.412  175.030 1.00 52.42  ? 43  SER C C     1 
ATOM   8017  O O     . SER C  1 43  ? -30.979 53.391  175.266 1.00 46.58  ? 43  SER C O     1 
ATOM   8018  C CB    . SER C  1 43  ? -30.889 50.541  176.494 1.00 48.71  ? 43  SER C CB    1 
ATOM   8019  O OG    . SER C  1 43  ? -32.089 50.675  177.238 1.00 54.66  ? 43  SER C OG    1 
ATOM   8020  N N     . ALA C  1 44  ? -32.975 52.510  174.736 1.00 55.13  ? 44  ALA C N     1 
ATOM   8021  C CA    . ALA C  1 44  ? -33.623 53.809  174.632 1.00 50.85  ? 44  ALA C CA    1 
ATOM   8022  C C     . ALA C  1 44  ? -34.038 54.329  176.003 1.00 54.40  ? 44  ALA C C     1 
ATOM   8023  O O     . ALA C  1 44  ? -34.439 55.486  176.142 1.00 58.74  ? 44  ALA C O     1 
ATOM   8024  C CB    . ALA C  1 44  ? -34.828 53.730  173.705 1.00 52.82  ? 44  ALA C CB    1 
ATOM   8025  N N     . ASP C  1 45  ? -33.938 53.468  177.012 1.00 55.35  ? 45  ASP C N     1 
ATOM   8026  C CA    . ASP C  1 45  ? -34.308 53.832  178.377 1.00 58.55  ? 45  ASP C CA    1 
ATOM   8027  C C     . ASP C  1 45  ? -33.508 55.033  178.866 1.00 62.08  ? 45  ASP C C     1 
ATOM   8028  O O     . ASP C  1 45  ? -32.279 54.992  178.942 1.00 60.34  ? 45  ASP C O     1 
ATOM   8029  C CB    . ASP C  1 45  ? -34.115 52.643  179.319 1.00 58.12  ? 45  ASP C CB    1 
ATOM   8030  C CG    . ASP C  1 45  ? -35.109 51.532  179.056 1.00 74.55  ? 45  ASP C CG    1 
ATOM   8031  O OD1   . ASP C  1 45  ? -36.124 51.798  178.375 1.00 74.62  ? 45  ASP C OD1   1 
ATOM   8032  O OD2   . ASP C  1 45  ? -34.883 50.398  179.528 1.00 71.76  ? 45  ASP C OD2   1 
ATOM   8033  N N     . SER C  1 46  ? -34.233 56.098  179.198 1.00 62.30  ? 46  SER C N     1 
ATOM   8034  C CA    . SER C  1 46  ? -33.652 57.388  179.552 1.00 65.18  ? 46  SER C CA    1 
ATOM   8035  C C     . SER C  1 46  ? -32.591 57.303  180.653 1.00 66.27  ? 46  SER C C     1 
ATOM   8036  O O     . SER C  1 46  ? -31.667 58.119  180.691 1.00 73.20  ? 46  SER C O     1 
ATOM   8037  C CB    . SER C  1 46  ? -34.766 58.353  179.975 1.00 66.41  ? 46  SER C CB    1 
ATOM   8038  O OG    . SER C  1 46  ? -34.374 59.704  179.804 1.00 72.93  ? 46  SER C OG    1 
ATOM   8039  N N     . ASP C  1 47  ? -32.716 56.319  181.539 1.00 68.78  ? 47  ASP C N     1 
ATOM   8040  C CA    . ASP C  1 47  ? -31.809 56.208  182.682 1.00 70.35  ? 47  ASP C CA    1 
ATOM   8041  C C     . ASP C  1 47  ? -30.781 55.090  182.548 1.00 70.43  ? 47  ASP C C     1 
ATOM   8042  O O     . ASP C  1 47  ? -30.029 54.824  183.485 1.00 71.96  ? 47  ASP C O     1 
ATOM   8043  C CB    . ASP C  1 47  ? -32.601 55.997  183.972 1.00 76.74  ? 47  ASP C CB    1 
ATOM   8044  C CG    . ASP C  1 47  ? -33.378 57.226  184.383 1.00 98.74  ? 47  ASP C CG    1 
ATOM   8045  O OD1   . ASP C  1 47  ? -33.096 58.313  183.835 1.00 91.46  ? 47  ASP C OD1   1 
ATOM   8046  O OD2   . ASP C  1 47  ? -34.266 57.106  185.253 1.00 111.10 ? 47  ASP C OD2   1 
ATOM   8047  N N     . SER C  1 48  ? -30.746 54.436  181.393 1.00 63.39  ? 48  SER C N     1 
ATOM   8048  C CA    . SER C  1 48  ? -29.777 53.370  181.163 1.00 60.11  ? 48  SER C CA    1 
ATOM   8049  C C     . SER C  1 48  ? -28.355 53.924  181.151 1.00 58.32  ? 48  SER C C     1 
ATOM   8050  O O     . SER C  1 48  ? -28.133 55.073  180.766 1.00 53.25  ? 48  SER C O     1 
ATOM   8051  C CB    . SER C  1 48  ? -30.071 52.647  179.849 1.00 54.99  ? 48  SER C CB    1 
ATOM   8052  O OG    . SER C  1 48  ? -29.929 53.520  178.741 1.00 50.77  ? 48  SER C OG    1 
ATOM   8053  N N     . ASP C  1 49  ? -27.402 53.101  181.581 1.00 58.57  ? 49  ASP C N     1 
ATOM   8054  C CA    . ASP C  1 49  ? -25.984 53.442  181.503 1.00 54.71  ? 49  ASP C CA    1 
ATOM   8055  C C     . ASP C  1 49  ? -25.615 53.854  180.086 1.00 53.23  ? 49  ASP C C     1 
ATOM   8056  O O     . ASP C  1 49  ? -24.840 54.789  179.881 1.00 51.19  ? 49  ASP C O     1 
ATOM   8057  C CB    . ASP C  1 49  ? -25.114 52.262  181.948 1.00 58.19  ? 49  ASP C CB    1 
ATOM   8058  C CG    . ASP C  1 49  ? -24.921 52.211  183.450 1.00 60.73  ? 49  ASP C CG    1 
ATOM   8059  O OD1   . ASP C  1 49  ? -25.584 52.992  184.166 1.00 72.64  ? 49  ASP C OD1   1 
ATOM   8060  O OD2   . ASP C  1 49  ? -24.108 51.384  183.915 1.00 59.33  ? 49  ASP C OD2   1 
ATOM   8061  N N     . PHE C  1 50  ? -26.183 53.147  179.112 1.00 44.59  ? 50  PHE C N     1 
ATOM   8062  C CA    . PHE C  1 50  ? -25.949 53.447  177.705 1.00 46.55  ? 50  PHE C CA    1 
ATOM   8063  C C     . PHE C  1 50  ? -26.348 54.875  177.353 1.00 48.48  ? 50  PHE C C     1 
ATOM   8064  O O     . PHE C  1 50  ? -25.515 55.667  176.913 1.00 44.66  ? 50  PHE C O     1 
ATOM   8065  C CB    . PHE C  1 50  ? -26.711 52.472  176.806 1.00 43.60  ? 50  PHE C CB    1 
ATOM   8066  C CG    . PHE C  1 50  ? -26.574 52.777  175.344 1.00 42.62  ? 50  PHE C CG    1 
ATOM   8067  C CD1   . PHE C  1 50  ? -25.531 52.244  174.609 1.00 39.67  ? 50  PHE C CD1   1 
ATOM   8068  C CD2   . PHE C  1 50  ? -27.479 53.612  174.706 1.00 41.17  ? 50  PHE C CD2   1 
ATOM   8069  C CE1   . PHE C  1 50  ? -25.398 52.529  173.263 1.00 39.79  ? 50  PHE C CE1   1 
ATOM   8070  C CE2   . PHE C  1 50  ? -27.346 53.907  173.369 1.00 43.59  ? 50  PHE C CE2   1 
ATOM   8071  C CZ    . PHE C  1 50  ? -26.306 53.363  172.643 1.00 39.25  ? 50  PHE C CZ    1 
ATOM   8072  N N     . ASN C  1 51  ? -27.629 55.189  177.528 1.00 48.13  ? 51  ASN C N     1 
ATOM   8073  C CA    . ASN C  1 51  ? -28.149 56.501  177.163 1.00 45.82  ? 51  ASN C CA    1 
ATOM   8074  C C     . ASN C  1 51  ? -27.435 57.612  177.924 1.00 42.02  ? 51  ASN C C     1 
ATOM   8075  O O     . ASN C  1 51  ? -27.236 58.707  177.401 1.00 44.40  ? 51  ASN C O     1 
ATOM   8076  C CB    . ASN C  1 51  ? -29.658 56.572  177.413 1.00 48.34  ? 51  ASN C CB    1 
ATOM   8077  C CG    . ASN C  1 51  ? -30.257 57.899  176.989 1.00 48.02  ? 51  ASN C CG    1 
ATOM   8078  O OD1   . ASN C  1 51  ? -30.548 58.112  175.812 1.00 47.52  ? 51  ASN C OD1   1 
ATOM   8079  N ND2   . ASN C  1 51  ? -30.447 58.798  177.949 1.00 52.06  ? 51  ASN C ND2   1 
ATOM   8080  N N     . ARG C  1 52  ? -27.045 57.313  179.159 1.00 41.92  ? 52  ARG C N     1 
ATOM   8081  C CA    . ARG C  1 52  ? -26.295 58.253  179.984 1.00 46.09  ? 52  ARG C CA    1 
ATOM   8082  C C     . ARG C  1 52  ? -24.913 58.525  179.391 1.00 51.07  ? 52  ARG C C     1 
ATOM   8083  O O     . ARG C  1 52  ? -24.518 59.678  179.223 1.00 51.75  ? 52  ARG C O     1 
ATOM   8084  C CB    . ARG C  1 52  ? -26.162 57.717  181.410 1.00 51.18  ? 52  ARG C CB    1 
ATOM   8085  C CG    . ARG C  1 52  ? -25.635 58.730  182.412 1.00 56.93  ? 52  ARG C CG    1 
ATOM   8086  C CD    . ARG C  1 52  ? -25.824 58.239  183.837 1.00 57.44  ? 52  ARG C CD    1 
ATOM   8087  N NE    . ARG C  1 52  ? -25.172 56.953  184.057 1.00 64.15  ? 52  ARG C NE    1 
ATOM   8088  C CZ    . ARG C  1 52  ? -23.931 56.807  184.513 1.00 74.31  ? 52  ARG C CZ    1 
ATOM   8089  N NH1   . ARG C  1 52  ? -23.198 57.873  184.803 1.00 66.82  ? 52  ARG C NH1   1 
ATOM   8090  N NH2   . ARG C  1 52  ? -23.424 55.593  184.679 1.00 71.77  ? 52  ARG C NH2   1 
ATOM   8091  N N     . PHE C  1 53  ? -24.188 57.452  179.081 1.00 46.83  ? 53  PHE C N     1 
ATOM   8092  C CA    . PHE C  1 53  ? -22.869 57.553  178.461 1.00 42.10  ? 53  PHE C CA    1 
ATOM   8093  C C     . PHE C  1 53  ? -22.935 58.307  177.138 1.00 45.37  ? 53  PHE C C     1 
ATOM   8094  O O     . PHE C  1 53  ? -22.116 59.185  176.869 1.00 48.51  ? 53  PHE C O     1 
ATOM   8095  C CB    . PHE C  1 53  ? -22.272 56.161  178.227 1.00 47.48  ? 53  PHE C CB    1 
ATOM   8096  C CG    . PHE C  1 53  ? -21.867 55.451  179.484 1.00 44.35  ? 53  PHE C CG    1 
ATOM   8097  C CD1   . PHE C  1 53  ? -21.548 56.163  180.627 1.00 50.05  ? 53  PHE C CD1   1 
ATOM   8098  C CD2   . PHE C  1 53  ? -21.801 54.067  179.521 1.00 46.01  ? 53  PHE C CD2   1 
ATOM   8099  C CE1   . PHE C  1 53  ? -21.172 55.509  181.786 1.00 53.33  ? 53  PHE C CE1   1 
ATOM   8100  C CE2   . PHE C  1 53  ? -21.426 53.407  180.675 1.00 51.86  ? 53  PHE C CE2   1 
ATOM   8101  C CZ    . PHE C  1 53  ? -21.110 54.129  181.808 1.00 54.00  ? 53  PHE C CZ    1 
ATOM   8102  N N     . LEU C  1 54  ? -23.926 57.957  176.324 1.00 45.14  ? 54  LEU C N     1 
ATOM   8103  C CA    . LEU C  1 54  ? -24.082 58.520  174.987 1.00 45.35  ? 54  LEU C CA    1 
ATOM   8104  C C     . LEU C  1 54  ? -24.278 60.037  175.000 1.00 49.71  ? 54  LEU C C     1 
ATOM   8105  O O     . LEU C  1 54  ? -23.625 60.759  174.242 1.00 47.83  ? 54  LEU C O     1 
ATOM   8106  C CB    . LEU C  1 54  ? -25.260 57.852  174.275 1.00 45.07  ? 54  LEU C CB    1 
ATOM   8107  C CG    . LEU C  1 54  ? -25.726 58.460  172.949 1.00 45.14  ? 54  LEU C CG    1 
ATOM   8108  C CD1   . LEU C  1 54  ? -24.602 58.444  171.920 1.00 41.18  ? 54  LEU C CD1   1 
ATOM   8109  C CD2   . LEU C  1 54  ? -26.958 57.734  172.416 1.00 39.82  ? 54  LEU C CD2   1 
ATOM   8110  N N     . HIS C  1 55  ? -25.178 60.510  175.858 1.00 46.27  ? 55  HIS C N     1 
ATOM   8111  C CA    . HIS C  1 55  ? -25.553 61.921  175.892 1.00 48.49  ? 55  HIS C CA    1 
ATOM   8112  C C     . HIS C  1 55  ? -24.581 62.770  176.700 1.00 44.89  ? 55  HIS C C     1 
ATOM   8113  O O     . HIS C  1 55  ? -24.489 63.978  176.491 1.00 46.87  ? 55  HIS C O     1 
ATOM   8114  C CB    . HIS C  1 55  ? -26.968 62.082  176.454 1.00 43.88  ? 55  HIS C CB    1 
ATOM   8115  C CG    . HIS C  1 55  ? -28.041 61.658  175.503 1.00 44.02  ? 55  HIS C CG    1 
ATOM   8116  N ND1   . HIS C  1 55  ? -28.428 62.429  174.428 1.00 48.72  ? 55  HIS C ND1   1 
ATOM   8117  C CD2   . HIS C  1 55  ? -28.799 60.537  175.455 1.00 41.33  ? 55  HIS C CD2   1 
ATOM   8118  C CE1   . HIS C  1 55  ? -29.382 61.803  173.762 1.00 44.90  ? 55  HIS C CE1   1 
ATOM   8119  N NE2   . HIS C  1 55  ? -29.624 60.652  174.363 1.00 49.67  ? 55  HIS C NE2   1 
ATOM   8120  N N     . LEU C  1 56  ? -23.855 62.131  177.612 1.00 46.82  ? 56  LEU C N     1 
ATOM   8121  C CA    . LEU C  1 56  ? -22.872 62.811  178.450 1.00 52.07  ? 56  LEU C CA    1 
ATOM   8122  C C     . LEU C  1 56  ? -21.902 63.670  177.634 1.00 53.18  ? 56  LEU C C     1 
ATOM   8123  O O     . LEU C  1 56  ? -21.411 64.693  178.113 1.00 56.70  ? 56  LEU C O     1 
ATOM   8124  C CB    . LEU C  1 56  ? -22.096 61.782  179.273 1.00 51.68  ? 56  LEU C CB    1 
ATOM   8125  C CG    . LEU C  1 56  ? -21.735 62.111  180.722 1.00 55.50  ? 56  LEU C CG    1 
ATOM   8126  C CD1   . LEU C  1 56  ? -22.894 62.784  181.434 1.00 54.58  ? 56  LEU C CD1   1 
ATOM   8127  C CD2   . LEU C  1 56  ? -21.337 60.839  181.448 1.00 53.89  ? 56  LEU C CD2   1 
ATOM   8128  N N     . SER C  1 57  ? -21.641 63.258  176.396 1.00 50.92  ? 57  SER C N     1 
ATOM   8129  C CA    . SER C  1 57  ? -20.697 63.971  175.543 1.00 50.02  ? 57  SER C CA    1 
ATOM   8130  C C     . SER C  1 57  ? -21.275 64.361  174.183 1.00 49.29  ? 57  SER C C     1 
ATOM   8131  O O     . SER C  1 57  ? -20.552 64.401  173.189 1.00 50.87  ? 57  SER C O     1 
ATOM   8132  C CB    . SER C  1 57  ? -19.434 63.131  175.338 1.00 43.09  ? 57  SER C CB    1 
ATOM   8133  O OG    . SER C  1 57  ? -18.788 62.880  176.574 1.00 46.58  ? 57  SER C OG    1 
ATOM   8134  N N     . ILE C  1 58  ? -22.574 64.638  174.134 1.00 50.40  ? 58  ILE C N     1 
ATOM   8135  C CA    . ILE C  1 58  ? -23.157 65.262  172.951 1.00 49.81  ? 58  ILE C CA    1 
ATOM   8136  C C     . ILE C  1 58  ? -23.196 66.766  173.183 1.00 49.82  ? 58  ILE C C     1 
ATOM   8137  O O     . ILE C  1 58  ? -23.953 67.252  174.023 1.00 60.33  ? 58  ILE C O     1 
ATOM   8138  C CB    . ILE C  1 58  ? -24.571 64.736  172.637 1.00 51.49  ? 58  ILE C CB    1 
ATOM   8139  C CG1   . ILE C  1 58  ? -24.518 63.251  172.277 1.00 48.85  ? 58  ILE C CG1   1 
ATOM   8140  C CG2   . ILE C  1 58  ? -25.183 65.516  171.483 1.00 47.74  ? 58  ILE C CG2   1 
ATOM   8141  C CD1   . ILE C  1 58  ? -25.848 62.684  171.826 1.00 54.43  ? 58  ILE C CD1   1 
ATOM   8142  N N     . GLN C  1 59  ? -22.370 67.500  172.445 1.00 45.38  ? 59  GLN C N     1 
ATOM   8143  C CA    . GLN C  1 59  ? -22.172 68.921  172.717 1.00 50.56  ? 59  GLN C CA    1 
ATOM   8144  C C     . GLN C  1 59  ? -22.929 69.819  171.741 1.00 50.95  ? 59  GLN C C     1 
ATOM   8145  O O     . GLN C  1 59  ? -22.905 71.044  171.861 1.00 52.17  ? 59  GLN C O     1 
ATOM   8146  C CB    . GLN C  1 59  ? -20.677 69.252  172.694 1.00 46.74  ? 59  GLN C CB    1 
ATOM   8147  C CG    . GLN C  1 59  ? -19.842 68.426  173.674 1.00 46.46  ? 59  GLN C CG    1 
ATOM   8148  C CD    . GLN C  1 59  ? -20.061 68.824  175.124 1.00 52.99  ? 59  GLN C CD    1 
ATOM   8149  O OE1   . GLN C  1 59  ? -20.823 69.742  175.422 1.00 60.82  ? 59  GLN C OE1   1 
ATOM   8150  N NE2   . GLN C  1 59  ? -19.388 68.130  176.034 1.00 47.42  ? 59  GLN C NE2   1 
ATOM   8151  N N     . ASN C  1 60  ? -23.590 69.200  170.770 1.00 50.92  ? 60  ASN C N     1 
ATOM   8152  C CA    . ASN C  1 60  ? -24.516 69.913  169.901 1.00 52.31  ? 60  ASN C CA    1 
ATOM   8153  C C     . ASN C  1 60  ? -25.861 69.200  169.909 1.00 53.76  ? 60  ASN C C     1 
ATOM   8154  O O     . ASN C  1 60  ? -26.062 68.247  169.156 1.00 52.33  ? 60  ASN C O     1 
ATOM   8155  C CB    . ASN C  1 60  ? -23.975 70.017  168.471 1.00 48.83  ? 60  ASN C CB    1 
ATOM   8156  C CG    . ASN C  1 60  ? -24.814 70.933  167.590 1.00 50.19  ? 60  ASN C CG    1 
ATOM   8157  O OD1   . ASN C  1 60  ? -25.877 71.400  167.996 1.00 53.82  ? 60  ASN C OD1   1 
ATOM   8158  N ND2   . ASN C  1 60  ? -24.339 71.187  166.375 1.00 49.16  ? 60  ASN C ND2   1 
ATOM   8159  N N     . PRO C  1 61  ? -26.787 69.662  170.769 1.00 58.62  ? 61  PRO C N     1 
ATOM   8160  C CA    . PRO C  1 61  ? -28.153 69.142  170.925 1.00 52.51  ? 61  PRO C CA    1 
ATOM   8161  C C     . PRO C  1 61  ? -28.906 68.928  169.608 1.00 51.13  ? 61  PRO C C     1 
ATOM   8162  O O     . PRO C  1 61  ? -29.916 68.224  169.601 1.00 59.02  ? 61  PRO C O     1 
ATOM   8163  C CB    . PRO C  1 61  ? -28.831 70.224  171.766 1.00 58.17  ? 61  PRO C CB    1 
ATOM   8164  C CG    . PRO C  1 61  ? -27.730 70.733  172.630 1.00 60.16  ? 61  PRO C CG    1 
ATOM   8165  C CD    . PRO C  1 61  ? -26.491 70.709  171.765 1.00 56.51  ? 61  PRO C CD    1 
ATOM   8166  N N     . LEU C  1 62  ? -28.418 69.513  168.516 1.00 52.09  ? 62  LEU C N     1 
ATOM   8167  C CA    . LEU C  1 62  ? -28.992 69.294  167.188 1.00 54.45  ? 62  LEU C CA    1 
ATOM   8168  C C     . LEU C  1 62  ? -29.009 67.807  166.812 1.00 54.50  ? 62  LEU C C     1 
ATOM   8169  O O     . LEU C  1 62  ? -29.761 67.386  165.933 1.00 52.49  ? 62  LEU C O     1 
ATOM   8170  C CB    . LEU C  1 62  ? -28.215 70.101  166.138 1.00 48.22  ? 62  LEU C CB    1 
ATOM   8171  C CG    . LEU C  1 62  ? -28.629 70.037  164.660 1.00 50.80  ? 62  LEU C CG    1 
ATOM   8172  C CD1   . LEU C  1 62  ? -30.083 70.446  164.476 1.00 55.09  ? 62  LEU C CD1   1 
ATOM   8173  C CD2   . LEU C  1 62  ? -27.720 70.901  163.789 1.00 49.92  ? 62  LEU C CD2   1 
ATOM   8174  N N     . PHE C  1 63  ? -28.189 67.012  167.493 1.00 53.13  ? 63  PHE C N     1 
ATOM   8175  C CA    . PHE C  1 63  ? -28.065 65.596  167.168 1.00 53.74  ? 63  PHE C CA    1 
ATOM   8176  C C     . PHE C  1 63  ? -28.391 64.676  168.342 1.00 54.02  ? 63  PHE C C     1 
ATOM   8177  O O     . PHE C  1 63  ? -27.936 63.533  168.372 1.00 52.11  ? 63  PHE C O     1 
ATOM   8178  C CB    . PHE C  1 63  ? -26.649 65.292  166.674 1.00 47.27  ? 63  PHE C CB    1 
ATOM   8179  C CG    . PHE C  1 63  ? -26.196 66.173  165.544 1.00 44.82  ? 63  PHE C CG    1 
ATOM   8180  C CD1   . PHE C  1 63  ? -26.623 65.933  164.248 1.00 44.11  ? 63  PHE C CD1   1 
ATOM   8181  C CD2   . PHE C  1 63  ? -25.336 67.234  165.776 1.00 44.54  ? 63  PHE C CD2   1 
ATOM   8182  C CE1   . PHE C  1 63  ? -26.208 66.740  163.206 1.00 44.00  ? 63  PHE C CE1   1 
ATOM   8183  C CE2   . PHE C  1 63  ? -24.917 68.043  164.738 1.00 41.44  ? 63  PHE C CE2   1 
ATOM   8184  C CZ    . PHE C  1 63  ? -25.354 67.795  163.451 1.00 43.74  ? 63  PHE C CZ    1 
ATOM   8185  N N     . GLN C  1 64  ? -29.179 65.149  169.301 1.00 52.25  ? 64  GLN C N     1 
ATOM   8186  C CA    . GLN C  1 64  ? -29.447 64.340  170.487 1.00 56.43  ? 64  GLN C CA    1 
ATOM   8187  C C     . GLN C  1 64  ? -30.763 63.571  170.413 1.00 57.49  ? 64  GLN C C     1 
ATOM   8188  O O     . GLN C  1 64  ? -30.949 62.595  171.140 1.00 56.24  ? 64  GLN C O     1 
ATOM   8189  C CB    . GLN C  1 64  ? -29.451 65.214  171.742 1.00 59.16  ? 64  GLN C CB    1 
ATOM   8190  C CG    . GLN C  1 64  ? -30.667 66.112  171.864 1.00 63.70  ? 64  GLN C CG    1 
ATOM   8191  C CD    . GLN C  1 64  ? -30.733 66.830  173.196 1.00 67.08  ? 64  GLN C CD    1 
ATOM   8192  O OE1   . GLN C  1 64  ? -29.768 66.838  173.960 1.00 70.78  ? 64  GLN C OE1   1 
ATOM   8193  N NE2   . GLN C  1 64  ? -31.880 67.435  173.484 1.00 72.52  ? 64  GLN C NE2   1 
ATOM   8194  N N     . ASN C  1 65  ? -31.670 64.002  169.539 1.00 60.11  ? 65  ASN C N     1 
ATOM   8195  C CA    . ASN C  1 65  ? -33.030 63.469  169.543 1.00 57.50  ? 65  ASN C CA    1 
ATOM   8196  C C     . ASN C  1 65  ? -33.107 62.013  169.099 1.00 59.28  ? 65  ASN C C     1 
ATOM   8197  O O     . ASN C  1 65  ? -32.171 61.478  168.503 1.00 52.69  ? 65  ASN C O     1 
ATOM   8198  C CB    . ASN C  1 65  ? -33.951 64.333  168.672 1.00 59.91  ? 65  ASN C CB    1 
ATOM   8199  C CG    . ASN C  1 65  ? -33.763 64.093  167.184 1.00 61.50  ? 65  ASN C CG    1 
ATOM   8200  O OD1   . ASN C  1 65  ? -34.135 63.047  166.660 1.00 61.50  ? 65  ASN C OD1   1 
ATOM   8201  N ND2   . ASN C  1 65  ? -33.221 65.085  166.489 1.00 59.55  ? 65  ASN C ND2   1 
ATOM   8202  N N     . SER C  1 66  ? -34.247 61.391  169.385 1.00 58.70  ? 66  SER C N     1 
ATOM   8203  C CA    . SER C  1 66  ? -34.438 59.960  169.177 1.00 59.12  ? 66  SER C CA    1 
ATOM   8204  C C     . SER C  1 66  ? -34.335 59.531  167.711 1.00 57.75  ? 66  SER C C     1 
ATOM   8205  O O     . SER C  1 66  ? -33.980 58.388  167.423 1.00 63.03  ? 66  SER C O     1 
ATOM   8206  C CB    . SER C  1 66  ? -35.795 59.532  169.746 1.00 65.92  ? 66  SER C CB    1 
ATOM   8207  O OG    . SER C  1 66  ? -36.860 60.095  168.996 1.00 63.67  ? 66  SER C OG    1 
ATOM   8208  N N     . LEU C  1 67  ? -34.651 60.442  166.795 1.00 56.87  ? 67  LEU C N     1 
ATOM   8209  C CA    . LEU C  1 67  ? -34.631 60.140  165.361 1.00 54.70  ? 67  LEU C CA    1 
ATOM   8210  C C     . LEU C  1 67  ? -33.215 59.955  164.812 1.00 57.41  ? 67  LEU C C     1 
ATOM   8211  O O     . LEU C  1 67  ? -33.027 59.336  163.763 1.00 57.76  ? 67  LEU C O     1 
ATOM   8212  C CB    . LEU C  1 67  ? -35.336 61.246  164.565 1.00 59.51  ? 67  LEU C CB    1 
ATOM   8213  C CG    . LEU C  1 67  ? -36.835 61.177  164.256 1.00 69.52  ? 67  LEU C CG    1 
ATOM   8214  C CD1   . LEU C  1 67  ? -37.617 60.543  165.393 1.00 61.38  ? 67  LEU C CD1   1 
ATOM   8215  C CD2   . LEU C  1 67  ? -37.370 62.574  163.959 1.00 65.77  ? 67  LEU C CD2   1 
ATOM   8216  N N     . ILE C  1 68  ? -32.226 60.504  165.510 1.00 51.28  ? 68  ILE C N     1 
ATOM   8217  C CA    . ILE C  1 68  ? -30.836 60.423  165.069 1.00 55.09  ? 68  ILE C CA    1 
ATOM   8218  C C     . ILE C  1 68  ? -30.302 58.996  165.193 1.00 51.93  ? 68  ILE C C     1 
ATOM   8219  O O     . ILE C  1 68  ? -30.742 58.231  166.054 1.00 45.12  ? 68  ILE C O     1 
ATOM   8220  C CB    . ILE C  1 68  ? -29.939 61.389  165.875 1.00 52.63  ? 68  ILE C CB    1 
ATOM   8221  C CG1   . ILE C  1 68  ? -30.487 62.813  165.784 1.00 56.24  ? 68  ILE C CG1   1 
ATOM   8222  C CG2   . ILE C  1 68  ? -28.514 61.388  165.352 1.00 51.27  ? 68  ILE C CG2   1 
ATOM   8223  C CD1   . ILE C  1 68  ? -30.418 63.390  164.387 1.00 47.91  ? 68  ILE C CD1   1 
ATOM   8224  N N     . SER C  1 69  ? -29.377 58.634  164.308 1.00 56.87  ? 69  SER C N     1 
ATOM   8225  C CA    . SER C  1 69  ? -28.684 57.354  164.395 1.00 48.57  ? 69  SER C CA    1 
ATOM   8226  C C     . SER C  1 69  ? -28.031 57.174  165.762 1.00 44.99  ? 69  SER C C     1 
ATOM   8227  O O     . SER C  1 69  ? -27.463 58.112  166.320 1.00 47.89  ? 69  SER C O     1 
ATOM   8228  C CB    . SER C  1 69  ? -27.630 57.245  163.294 1.00 44.07  ? 69  SER C CB    1 
ATOM   8229  O OG    . SER C  1 69  ? -26.671 58.280  163.407 1.00 41.72  ? 69  SER C OG    1 
ATOM   8230  N N     . LYS C  1 70  ? -28.125 55.963  166.297 1.00 49.02  ? 70  LYS C N     1 
ATOM   8231  C CA    . LYS C  1 70  ? -27.567 55.645  167.605 1.00 43.54  ? 70  LYS C CA    1 
ATOM   8232  C C     . LYS C  1 70  ? -26.609 54.468  167.485 1.00 43.93  ? 70  LYS C C     1 
ATOM   8233  O O     . LYS C  1 70  ? -26.833 53.567  166.676 1.00 41.54  ? 70  LYS C O     1 
ATOM   8234  C CB    . LYS C  1 70  ? -28.682 55.321  168.598 1.00 45.22  ? 70  LYS C CB    1 
ATOM   8235  C CG    . LYS C  1 70  ? -29.812 56.339  168.622 1.00 48.34  ? 70  LYS C CG    1 
ATOM   8236  C CD    . LYS C  1 70  ? -29.406 57.611  169.347 1.00 48.39  ? 70  LYS C CD    1 
ATOM   8237  C CE    . LYS C  1 70  ? -30.457 58.698  169.172 1.00 45.83  ? 70  LYS C CE    1 
ATOM   8238  N NZ    . LYS C  1 70  ? -30.179 59.894  170.012 1.00 45.61  ? 70  LYS C NZ    1 
ATOM   8239  N N     . PRO C  1 71  ? -25.530 54.471  168.284 1.00 45.91  ? 71  PRO C N     1 
ATOM   8240  C CA    . PRO C  1 71  ? -24.600 53.340  168.223 1.00 37.36  ? 71  PRO C CA    1 
ATOM   8241  C C     . PRO C  1 71  ? -25.240 52.078  168.780 1.00 40.43  ? 71  PRO C C     1 
ATOM   8242  O O     . PRO C  1 71  ? -26.025 52.161  169.724 1.00 43.38  ? 71  PRO C O     1 
ATOM   8243  C CB    . PRO C  1 71  ? -23.424 53.800  169.089 1.00 39.87  ? 71  PRO C CB    1 
ATOM   8244  C CG    . PRO C  1 71  ? -24.015 54.789  170.032 1.00 39.42  ? 71  PRO C CG    1 
ATOM   8245  C CD    . PRO C  1 71  ? -25.113 55.482  169.272 1.00 43.84  ? 71  PRO C CD    1 
ATOM   8246  N N     . SER C  1 72  ? -24.913 50.930  168.196 1.00 41.88  ? 72  SER C N     1 
ATOM   8247  C CA    . SER C  1 72  ? -25.461 49.660  168.654 1.00 34.92  ? 72  SER C CA    1 
ATOM   8248  C C     . SER C  1 72  ? -24.836 49.268  169.989 1.00 37.83  ? 72  SER C C     1 
ATOM   8249  O O     . SER C  1 72  ? -25.375 48.440  170.722 1.00 33.73  ? 72  SER C O     1 
ATOM   8250  C CB    . SER C  1 72  ? -25.229 48.568  167.608 1.00 33.52  ? 72  SER C CB    1 
ATOM   8251  O OG    . SER C  1 72  ? -25.738 48.967  166.344 1.00 37.58  ? 72  SER C OG    1 
ATOM   8252  N N     . ALA C  1 73  ? -23.698 49.883  170.301 1.00 36.93  ? 73  ALA C N     1 
ATOM   8253  C CA    . ALA C  1 73  ? -23.013 49.653  171.567 1.00 36.53  ? 73  ALA C CA    1 
ATOM   8254  C C     . ALA C  1 73  ? -22.008 50.763  171.845 1.00 34.71  ? 73  ALA C C     1 
ATOM   8255  O O     . ALA C  1 73  ? -21.549 51.439  170.924 1.00 35.98  ? 73  ALA C O     1 
ATOM   8256  C CB    . ALA C  1 73  ? -22.318 48.301  171.561 1.00 31.96  ? 73  ALA C CB    1 
ATOM   8257  N N     . ILE C  1 74  ? -21.675 50.953  173.118 1.00 36.35  ? 74  ILE C N     1 
ATOM   8258  C CA    . ILE C  1 74  ? -20.659 51.919  173.509 1.00 35.84  ? 74  ILE C CA    1 
ATOM   8259  C C     . ILE C  1 74  ? -19.559 51.228  174.299 1.00 37.09  ? 74  ILE C C     1 
ATOM   8260  O O     . ILE C  1 74  ? -19.833 50.491  175.244 1.00 35.10  ? 74  ILE C O     1 
ATOM   8261  C CB    . ILE C  1 74  ? -21.246 53.065  174.354 1.00 36.50  ? 74  ILE C CB    1 
ATOM   8262  C CG1   . ILE C  1 74  ? -22.257 53.861  173.537 1.00 39.92  ? 74  ILE C CG1   1 
ATOM   8263  C CG2   . ILE C  1 74  ? -20.146 53.999  174.818 1.00 35.52  ? 74  ILE C CG2   1 
ATOM   8264  C CD1   . ILE C  1 74  ? -22.871 55.019  174.290 1.00 40.41  ? 74  ILE C CD1   1 
ATOM   8265  N N     . ILE C  1 75  ? -18.314 51.464  173.899 1.00 34.21  ? 75  ILE C N     1 
ATOM   8266  C CA    . ILE C  1 75  ? -17.168 50.850  174.551 1.00 35.44  ? 75  ILE C CA    1 
ATOM   8267  C C     . ILE C  1 75  ? -16.237 51.914  175.121 1.00 34.44  ? 75  ILE C C     1 
ATOM   8268  O O     . ILE C  1 75  ? -15.919 52.895  174.452 1.00 30.55  ? 75  ILE C O     1 
ATOM   8269  C CB    . ILE C  1 75  ? -16.379 49.952  173.574 1.00 32.46  ? 75  ILE C CB    1 
ATOM   8270  C CG1   . ILE C  1 75  ? -17.312 48.935  172.915 1.00 36.76  ? 75  ILE C CG1   1 
ATOM   8271  C CG2   . ILE C  1 75  ? -15.235 49.250  174.292 1.00 35.71  ? 75  ILE C CG2   1 
ATOM   8272  C CD1   . ILE C  1 75  ? -16.703 48.250  171.718 1.00 43.80  ? 75  ILE C CD1   1 
ATOM   8273  N N     . LEU C  1 76  ? -15.811 51.721  176.364 1.00 36.39  ? 76  LEU C N     1 
ATOM   8274  C CA    . LEU C  1 76  ? -14.893 52.657  177.000 1.00 35.62  ? 76  LEU C CA    1 
ATOM   8275  C C     . LEU C  1 76  ? -13.570 51.980  177.355 1.00 36.96  ? 76  LEU C C     1 
ATOM   8276  O O     . LEU C  1 76  ? -13.384 51.529  178.488 1.00 37.79  ? 76  LEU C O     1 
ATOM   8277  C CB    . LEU C  1 76  ? -15.523 53.265  178.260 1.00 42.06  ? 76  LEU C CB    1 
ATOM   8278  C CG    . LEU C  1 76  ? -16.577 54.375  178.141 1.00 43.79  ? 76  LEU C CG    1 
ATOM   8279  C CD1   . LEU C  1 76  ? -17.865 53.854  177.549 1.00 41.68  ? 76  LEU C CD1   1 
ATOM   8280  C CD2   . LEU C  1 76  ? -16.836 54.984  179.507 1.00 50.44  ? 76  LEU C CD2   1 
ATOM   8281  N N     . PRO C  1 77  ? -12.645 51.907  176.384 1.00 33.12  ? 77  PRO C N     1 
ATOM   8282  C CA    . PRO C  1 77  ? -11.327 51.301  176.615 1.00 35.29  ? 77  PRO C CA    1 
ATOM   8283  C C     . PRO C  1 77  ? -10.549 52.052  177.683 1.00 36.39  ? 77  PRO C C     1 
ATOM   8284  O O     . PRO C  1 77  ? -10.627 53.278  177.738 1.00 31.91  ? 77  PRO C O     1 
ATOM   8285  C CB    . PRO C  1 77  ? -10.639 51.416  175.252 1.00 32.27  ? 77  PRO C CB    1 
ATOM   8286  C CG    . PRO C  1 77  ? -11.330 52.541  174.573 1.00 31.39  ? 77  PRO C CG    1 
ATOM   8287  C CD    . PRO C  1 77  ? -12.763 52.462  175.025 1.00 34.44  ? 77  PRO C CD    1 
ATOM   8288  N N     . GLY C  1 78  ? -9.814  51.321  178.516 1.00 33.33  ? 78  GLY C N     1 
ATOM   8289  C CA    . GLY C  1 78  ? -9.118  51.913  179.644 1.00 35.73  ? 78  GLY C CA    1 
ATOM   8290  C C     . GLY C  1 78  ? -7.606  51.930  179.511 1.00 39.68  ? 78  GLY C C     1 
ATOM   8291  O O     . GLY C  1 78  ? -6.902  52.371  180.419 1.00 41.25  ? 78  GLY C O     1 
ATOM   8292  N N     . SER C  1 79  ? -7.107  51.451  178.376 1.00 38.50  ? 79  SER C N     1 
ATOM   8293  C CA    . SER C  1 79  ? -5.674  51.461  178.095 1.00 36.57  ? 79  SER C CA    1 
ATOM   8294  C C     . SER C  1 79  ? -5.436  51.484  176.591 1.00 37.64  ? 79  SER C C     1 
ATOM   8295  O O     . SER C  1 79  ? -6.370  51.296  175.811 1.00 33.32  ? 79  SER C O     1 
ATOM   8296  C CB    . SER C  1 79  ? -4.988  50.243  178.723 1.00 33.79  ? 79  SER C CB    1 
ATOM   8297  O OG    . SER C  1 79  ? -5.299  49.057  178.011 1.00 38.26  ? 79  SER C OG    1 
ATOM   8298  N N     . LYS C  1 80  ? -4.189  51.707  176.182 1.00 32.98  ? 80  LYS C N     1 
ATOM   8299  C CA    . LYS C  1 80  ? -3.864  51.706  174.759 1.00 28.29  ? 80  LYS C CA    1 
ATOM   8300  C C     . LYS C  1 80  ? -4.007  50.293  174.209 1.00 25.73  ? 80  LYS C C     1 
ATOM   8301  O O     . LYS C  1 80  ? -4.326  50.104  173.036 1.00 30.01  ? 80  LYS C O     1 
ATOM   8302  C CB    . LYS C  1 80  ? -2.452  52.258  174.502 1.00 32.91  ? 80  LYS C CB    1 
ATOM   8303  C CG    . LYS C  1 80  ? -1.306  51.394  175.008 1.00 30.73  ? 80  LYS C CG    1 
ATOM   8304  C CD    . LYS C  1 80  ? 0.036   52.047  174.696 1.00 32.41  ? 80  LYS C CD    1 
ATOM   8305  C CE    . LYS C  1 80  ? 1.202   51.126  175.029 1.00 33.34  ? 80  LYS C CE    1 
ATOM   8306  N NZ    . LYS C  1 80  ? 1.276   50.776  176.474 1.00 30.44  ? 80  LYS C NZ    1 
ATOM   8307  N N     . GLU C  1 81  ? -3.787  49.302  175.068 1.00 30.40  ? 81  GLU C N     1 
ATOM   8308  C CA    . GLU C  1 81  ? -3.949  47.910  174.672 1.00 30.89  ? 81  GLU C CA    1 
ATOM   8309  C C     . GLU C  1 81  ? -5.426  47.569  174.461 1.00 33.82  ? 81  GLU C C     1 
ATOM   8310  O O     . GLU C  1 81  ? -5.778  46.863  173.518 1.00 33.49  ? 81  GLU C O     1 
ATOM   8311  C CB    . GLU C  1 81  ? -3.340  46.968  175.715 1.00 30.40  ? 81  GLU C CB    1 
ATOM   8312  C CG    . GLU C  1 81  ? -1.819  46.978  175.768 1.00 33.13  ? 81  GLU C CG    1 
ATOM   8313  C CD    . GLU C  1 81  ? -1.269  48.123  176.598 1.00 39.09  ? 81  GLU C CD    1 
ATOM   8314  O OE1   . GLU C  1 81  ? -2.050  48.736  177.358 1.00 35.43  ? 81  GLU C OE1   1 
ATOM   8315  O OE2   . GLU C  1 81  ? -0.056  48.408  176.496 1.00 36.19  ? 81  GLU C OE2   1 
ATOM   8316  N N     . GLU C  1 82  ? -6.283  48.066  175.347 1.00 31.21  ? 82  GLU C N     1 
ATOM   8317  C CA    . GLU C  1 82  ? -7.721  47.859  175.210 1.00 32.50  ? 82  GLU C CA    1 
ATOM   8318  C C     . GLU C  1 82  ? -8.254  48.597  173.987 1.00 29.96  ? 82  GLU C C     1 
ATOM   8319  O O     . GLU C  1 82  ? -9.144  48.103  173.295 1.00 32.21  ? 82  GLU C O     1 
ATOM   8320  C CB    . GLU C  1 82  ? -8.465  48.314  176.470 1.00 33.22  ? 82  GLU C CB    1 
ATOM   8321  C CG    . GLU C  1 82  ? -8.332  47.367  177.656 1.00 37.60  ? 82  GLU C CG    1 
ATOM   8322  C CD    . GLU C  1 82  ? -9.170  47.801  178.845 1.00 42.12  ? 82  GLU C CD    1 
ATOM   8323  O OE1   . GLU C  1 82  ? -10.052 48.670  178.670 1.00 46.01  ? 82  GLU C OE1   1 
ATOM   8324  O OE2   . GLU C  1 82  ? -8.947  47.270  179.955 1.00 44.04  ? 82  GLU C OE2   1 
ATOM   8325  N N     . LEU C  1 83  ? -7.701  49.778  173.724 1.00 30.88  ? 83  LEU C N     1 
ATOM   8326  C CA    . LEU C  1 83  ? -8.079  50.552  172.545 1.00 30.49  ? 83  LEU C CA    1 
ATOM   8327  C C     . LEU C  1 83  ? -7.703  49.809  171.270 1.00 33.39  ? 83  LEU C C     1 
ATOM   8328  O O     . LEU C  1 83  ? -8.480  49.763  170.316 1.00 31.83  ? 83  LEU C O     1 
ATOM   8329  C CB    . LEU C  1 83  ? -7.421  51.933  172.567 1.00 33.47  ? 83  LEU C CB    1 
ATOM   8330  C CG    . LEU C  1 83  ? -7.725  52.847  171.377 1.00 33.48  ? 83  LEU C CG    1 
ATOM   8331  C CD1   . LEU C  1 83  ? -9.232  52.985  171.164 1.00 27.07  ? 83  LEU C CD1   1 
ATOM   8332  C CD2   . LEU C  1 83  ? -7.092  54.213  171.575 1.00 30.63  ? 83  LEU C CD2   1 
ATOM   8333  N N     . SER C  1 84  ? -6.505  49.232  171.263 1.00 35.89  ? 84  SER C N     1 
ATOM   8334  C CA    . SER C  1 84  ? -6.029  48.452  170.127 1.00 33.65  ? 84  SER C CA    1 
ATOM   8335  C C     . SER C  1 84  ? -6.937  47.260  169.863 1.00 28.38  ? 84  SER C C     1 
ATOM   8336  O O     . SER C  1 84  ? -7.381  47.043  168.737 1.00 32.70  ? 84  SER C O     1 
ATOM   8337  C CB    . SER C  1 84  ? -4.595  47.969  170.364 1.00 27.80  ? 84  SER C CB    1 
ATOM   8338  O OG    . SER C  1 84  ? -4.204  47.048  169.362 1.00 25.74  ? 84  SER C OG    1 
ATOM   8339  N N     . ASN C  1 85  ? -7.212  46.493  170.912 1.00 28.61  ? 85  ASN C N     1 
ATOM   8340  C CA    . ASN C  1 85  ? -8.056  45.309  170.802 1.00 28.25  ? 85  ASN C CA    1 
ATOM   8341  C C     . ASN C  1 85  ? -9.512  45.636  170.473 1.00 31.77  ? 85  ASN C C     1 
ATOM   8342  O O     . ASN C  1 85  ? -10.194 44.849  169.811 1.00 29.00  ? 85  ASN C O     1 
ATOM   8343  C CB    . ASN C  1 85  ? -7.986  44.494  172.092 1.00 26.58  ? 85  ASN C CB    1 
ATOM   8344  C CG    . ASN C  1 85  ? -6.642  43.808  172.269 1.00 35.33  ? 85  ASN C CG    1 
ATOM   8345  O OD1   . ASN C  1 85  ? -5.875  43.669  171.316 1.00 31.47  ? 85  ASN C OD1   1 
ATOM   8346  N ND2   . ASN C  1 85  ? -6.358  43.365  173.486 1.00 32.05  ? 85  ASN C ND2   1 
ATOM   8347  N N     . THR C  1 86  ? -9.988  46.791  170.931 1.00 29.61  ? 86  THR C N     1 
ATOM   8348  C CA    . THR C  1 86  ? -11.349 47.225  170.625 1.00 30.36  ? 86  THR C CA    1 
ATOM   8349  C C     . THR C  1 86  ? -11.522 47.405  169.123 1.00 34.97  ? 86  THR C C     1 
ATOM   8350  O O     . THR C  1 86  ? -12.517 46.967  168.543 1.00 34.84  ? 86  THR C O     1 
ATOM   8351  C CB    . THR C  1 86  ? -11.701 48.543  171.345 1.00 30.59  ? 86  THR C CB    1 
ATOM   8352  O OG1   . THR C  1 86  ? -11.722 48.324  172.761 1.00 28.15  ? 86  THR C OG1   1 
ATOM   8353  C CG2   . THR C  1 86  ? -13.064 49.049  170.897 1.00 29.67  ? 86  THR C CG2   1 
ATOM   8354  N N     . ILE C  1 87  ? -10.534 48.040  168.500 1.00 28.78  ? 87  ILE C N     1 
ATOM   8355  C CA    . ILE C  1 87  ? -10.560 48.300  167.067 1.00 27.38  ? 87  ILE C CA    1 
ATOM   8356  C C     . ILE C  1 87  ? -10.530 46.998  166.264 1.00 35.20  ? 87  ILE C C     1 
ATOM   8357  O O     . ILE C  1 87  ? -11.230 46.864  165.261 1.00 39.57  ? 87  ILE C O     1 
ATOM   8358  C CB    . ILE C  1 87  ? -9.380  49.208  166.654 1.00 27.27  ? 87  ILE C CB    1 
ATOM   8359  C CG1   . ILE C  1 87  ? -9.603  50.628  167.189 1.00 27.34  ? 87  ILE C CG1   1 
ATOM   8360  C CG2   . ILE C  1 87  ? -9.210  49.240  165.147 1.00 26.83  ? 87  ILE C CG2   1 
ATOM   8361  C CD1   . ILE C  1 87  ? -8.417  51.547  167.001 1.00 35.10  ? 87  ILE C CD1   1 
ATOM   8362  N N     . ARG C  1 88  ? -9.741  46.029  166.720 1.00 31.59  ? 88  ARG C N     1 
ATOM   8363  C CA    . ARG C  1 88  ? -9.655  44.744  166.030 1.00 34.32  ? 88  ARG C CA    1 
ATOM   8364  C C     . ARG C  1 88  ? -10.960 43.954  166.146 1.00 38.30  ? 88  ARG C C     1 
ATOM   8365  O O     . ARG C  1 88  ? -11.419 43.364  165.168 1.00 39.93  ? 88  ARG C O     1 
ATOM   8366  C CB    . ARG C  1 88  ? -8.484  43.919  166.568 1.00 32.39  ? 88  ARG C CB    1 
ATOM   8367  C CG    . ARG C  1 88  ? -7.122  44.458  166.147 1.00 40.99  ? 88  ARG C CG    1 
ATOM   8368  C CD    . ARG C  1 88  ? -5.970  43.566  166.600 1.00 43.45  ? 88  ARG C CD    1 
ATOM   8369  N NE    . ARG C  1 88  ? -5.993  42.240  165.984 1.00 53.73  ? 88  ARG C NE    1 
ATOM   8370  C CZ    . ARG C  1 88  ? -5.729  42.001  164.703 1.00 62.39  ? 88  ARG C CZ    1 
ATOM   8371  N NH1   . ARG C  1 88  ? -5.767  40.760  164.232 1.00 48.26  ? 88  ARG C NH1   1 
ATOM   8372  N NH2   . ARG C  1 88  ? -5.435  43.004  163.888 1.00 65.34  ? 88  ARG C NH2   1 
ATOM   8373  N N     . CYS C  1 89  ? -11.547 43.946  167.341 1.00 33.62  ? 89  CYS C N     1 
ATOM   8374  C CA    . CYS C  1 89  ? -12.797 43.226  167.594 1.00 39.59  ? 89  CYS C CA    1 
ATOM   8375  C C     . CYS C  1 89  ? -13.963 43.759  166.765 1.00 34.92  ? 89  CYS C C     1 
ATOM   8376  O O     . CYS C  1 89  ? -14.683 42.983  166.132 1.00 39.88  ? 89  CYS C O     1 
ATOM   8377  C CB    . CYS C  1 89  ? -13.160 43.293  169.076 1.00 37.01  ? 89  CYS C CB    1 
ATOM   8378  S SG    . CYS C  1 89  ? -12.290 42.118  170.125 1.00 40.49  ? 89  CYS C SG    1 
ATOM   8379  N N     . ILE C  1 90  ? -14.155 45.076  166.794 1.00 36.82  ? 90  ILE C N     1 
ATOM   8380  C CA    . ILE C  1 90  ? -15.195 45.743  166.024 1.00 40.68  ? 90  ILE C CA    1 
ATOM   8381  C C     . ILE C  1 90  ? -15.077 45.420  164.533 1.00 43.91  ? 90  ILE C C     1 
ATOM   8382  O O     . ILE C  1 90  ? -16.073 45.118  163.865 1.00 47.10  ? 90  ILE C O     1 
ATOM   8383  C CB    . ILE C  1 90  ? -15.132 47.284  166.216 1.00 36.45  ? 90  ILE C CB    1 
ATOM   8384  C CG1   . ILE C  1 90  ? -15.499 47.672  167.649 1.00 31.63  ? 90  ILE C CG1   1 
ATOM   8385  C CG2   . ILE C  1 90  ? -16.052 47.990  165.242 1.00 38.04  ? 90  ILE C CG2   1 
ATOM   8386  C CD1   . ILE C  1 90  ? -15.361 49.159  167.930 1.00 29.43  ? 90  ILE C CD1   1 
ATOM   8387  N N     . ARG C  1 91  ? -13.849 45.453  164.028 1.00 42.58  ? 91  ARG C N     1 
ATOM   8388  C CA    . ARG C  1 91  ? -13.586 45.251  162.612 1.00 46.05  ? 91  ARG C CA    1 
ATOM   8389  C C     . ARG C  1 91  ? -13.889 43.836  162.125 1.00 48.77  ? 91  ARG C C     1 
ATOM   8390  O O     . ARG C  1 91  ? -14.276 43.636  160.973 1.00 53.44  ? 91  ARG C O     1 
ATOM   8391  C CB    . ARG C  1 91  ? -12.136 45.592  162.314 1.00 53.45  ? 91  ARG C CB    1 
ATOM   8392  C CG    . ARG C  1 91  ? -11.766 45.455  160.868 1.00 59.20  ? 91  ARG C CG    1 
ATOM   8393  C CD    . ARG C  1 91  ? -10.355 45.902  160.651 1.00 48.80  ? 91  ARG C CD    1 
ATOM   8394  N NE    . ARG C  1 91  ? -9.977  45.814  159.251 1.00 49.13  ? 91  ARG C NE    1 
ATOM   8395  C CZ    . ARG C  1 91  ? -8.796  46.197  158.779 1.00 51.98  ? 91  ARG C CZ    1 
ATOM   8396  N NH1   . ARG C  1 91  ? -8.526  46.086  157.486 1.00 55.39  ? 91  ARG C NH1   1 
ATOM   8397  N NH2   . ARG C  1 91  ? -7.882  46.696  159.598 1.00 59.64  ? 91  ARG C NH2   1 
ATOM   8398  N N     . LYS C  1 92  ? -13.716 42.857  163.009 1.00 45.59  ? 92  LYS C N     1 
ATOM   8399  C CA    . LYS C  1 92  ? -14.064 41.472  162.701 1.00 54.10  ? 92  LYS C CA    1 
ATOM   8400  C C     . LYS C  1 92  ? -15.546 41.351  162.350 1.00 52.03  ? 92  LYS C C     1 
ATOM   8401  O O     . LYS C  1 92  ? -15.959 40.406  161.678 1.00 58.78  ? 92  LYS C O     1 
ATOM   8402  C CB    . LYS C  1 92  ? -13.736 40.547  163.879 1.00 53.11  ? 92  LYS C CB    1 
ATOM   8403  C CG    . LYS C  1 92  ? -12.254 40.347  164.142 1.00 54.99  ? 92  LYS C CG    1 
ATOM   8404  C CD    . LYS C  1 92  ? -12.040 39.245  165.175 1.00 71.64  ? 92  LYS C CD    1 
ATOM   8405  C CE    . LYS C  1 92  ? -10.587 39.154  165.615 1.00 76.40  ? 92  LYS C CE    1 
ATOM   8406  N NZ    . LYS C  1 92  ? -9.660  38.951  164.469 1.00 73.43  ? 92  LYS C NZ    1 
ATOM   8407  N N     . GLY C  1 93  ? -16.341 42.308  162.816 1.00 50.29  ? 93  GLY C N     1 
ATOM   8408  C CA    . GLY C  1 93  ? -17.745 42.378  162.465 1.00 47.10  ? 93  GLY C CA    1 
ATOM   8409  C C     . GLY C  1 93  ? -17.979 43.311  161.290 1.00 51.49  ? 93  GLY C C     1 
ATOM   8410  O O     . GLY C  1 93  ? -17.042 43.702  160.593 1.00 53.90  ? 93  GLY C O     1 
ATOM   8411  N N     . SER C  1 94  ? -19.237 43.675  161.075 1.00 55.65  ? 94  SER C N     1 
ATOM   8412  C CA    . SER C  1 94  ? -19.608 44.550  159.970 1.00 62.12  ? 94  SER C CA    1 
ATOM   8413  C C     . SER C  1 94  ? -19.498 46.024  160.353 1.00 54.77  ? 94  SER C C     1 
ATOM   8414  O O     . SER C  1 94  ? -19.675 46.909  159.518 1.00 59.98  ? 94  SER C O     1 
ATOM   8415  C CB    . SER C  1 94  ? -21.035 44.243  159.519 1.00 61.12  ? 94  SER C CB    1 
ATOM   8416  O OG    . SER C  1 94  ? -21.951 44.451  160.582 1.00 61.20  ? 94  SER C OG    1 
ATOM   8417  N N     . TRP C  1 95  ? -19.182 46.272  161.619 1.00 48.93  ? 95  TRP C N     1 
ATOM   8418  C CA    . TRP C  1 95  ? -19.403 47.574  162.239 1.00 40.78  ? 95  TRP C CA    1 
ATOM   8419  C C     . TRP C  1 95  ? -18.546 48.722  161.713 1.00 39.71  ? 95  TRP C C     1 
ATOM   8420  O O     . TRP C  1 95  ? -17.360 48.562  161.418 1.00 40.57  ? 95  TRP C O     1 
ATOM   8421  C CB    . TRP C  1 95  ? -19.192 47.455  163.747 1.00 39.67  ? 95  TRP C CB    1 
ATOM   8422  C CG    . TRP C  1 95  ? -19.888 46.285  164.346 1.00 47.49  ? 95  TRP C CG    1 
ATOM   8423  C CD1   . TRP C  1 95  ? -19.334 45.084  164.678 1.00 44.48  ? 95  TRP C CD1   1 
ATOM   8424  C CD2   . TRP C  1 95  ? -21.275 46.194  164.680 1.00 39.16  ? 95  TRP C CD2   1 
ATOM   8425  N NE1   . TRP C  1 95  ? -20.291 44.251  165.204 1.00 42.00  ? 95  TRP C NE1   1 
ATOM   8426  C CE2   . TRP C  1 95  ? -21.493 44.910  165.217 1.00 42.24  ? 95  TRP C CE2   1 
ATOM   8427  C CE3   . TRP C  1 95  ? -22.355 47.076  164.582 1.00 41.60  ? 95  TRP C CE3   1 
ATOM   8428  C CZ2   . TRP C  1 95  ? -22.749 44.485  165.651 1.00 46.29  ? 95  TRP C CZ2   1 
ATOM   8429  C CZ3   . TRP C  1 95  ? -23.600 46.655  165.014 1.00 41.02  ? 95  TRP C CZ3   1 
ATOM   8430  C CH2   . TRP C  1 95  ? -23.787 45.371  165.542 1.00 43.46  ? 95  TRP C CH2   1 
ATOM   8431  N N     . THR C  1 96  ? -19.179 49.887  161.609 1.00 39.18  ? 96  THR C N     1 
ATOM   8432  C CA    . THR C  1 96  ? -18.488 51.144  161.365 1.00 41.39  ? 96  THR C CA    1 
ATOM   8433  C C     . THR C  1 96  ? -17.942 51.683  162.682 1.00 38.23  ? 96  THR C C     1 
ATOM   8434  O O     . THR C  1 96  ? -18.660 51.744  163.678 1.00 35.03  ? 96  THR C O     1 
ATOM   8435  C CB    . THR C  1 96  ? -19.423 52.189  160.726 1.00 39.99  ? 96  THR C CB    1 
ATOM   8436  O OG1   . THR C  1 96  ? -19.694 51.819  159.370 1.00 43.94  ? 96  THR C OG1   1 
ATOM   8437  C CG2   . THR C  1 96  ? -18.790 53.572  160.750 1.00 38.28  ? 96  THR C CG2   1 
ATOM   8438  N N     . ILE C  1 97  ? -16.670 52.063  162.689 1.00 38.87  ? 97  ILE C N     1 
ATOM   8439  C CA    . ILE C  1 97  ? -16.037 52.576  163.896 1.00 35.12  ? 97  ILE C CA    1 
ATOM   8440  C C     . ILE C  1 97  ? -16.294 54.069  164.087 1.00 30.15  ? 97  ILE C C     1 
ATOM   8441  O O     . ILE C  1 97  ? -16.136 54.858  163.158 1.00 30.57  ? 97  ILE C O     1 
ATOM   8442  C CB    . ILE C  1 97  ? -14.519 52.334  163.870 1.00 33.53  ? 97  ILE C CB    1 
ATOM   8443  C CG1   . ILE C  1 97  ? -14.222 50.838  163.941 1.00 33.68  ? 97  ILE C CG1   1 
ATOM   8444  C CG2   . ILE C  1 97  ? -13.846 53.063  165.015 1.00 26.43  ? 97  ILE C CG2   1 
ATOM   8445  C CD1   . ILE C  1 97  ? -12.756 50.500  163.816 1.00 34.20  ? 97  ILE C CD1   1 
ATOM   8446  N N     . ARG C  1 98  ? -16.703 54.447  165.293 1.00 30.96  ? 98  ARG C N     1 
ATOM   8447  C CA    . ARG C  1 98  ? -16.820 55.853  165.650 1.00 30.27  ? 98  ARG C CA    1 
ATOM   8448  C C     . ARG C  1 98  ? -16.014 56.140  166.907 1.00 32.93  ? 98  ARG C C     1 
ATOM   8449  O O     . ARG C  1 98  ? -16.175 55.471  167.929 1.00 34.67  ? 98  ARG C O     1 
ATOM   8450  C CB    . ARG C  1 98  ? -18.287 56.252  165.846 1.00 31.52  ? 98  ARG C CB    1 
ATOM   8451  C CG    . ARG C  1 98  ? -19.019 56.527  164.546 1.00 29.33  ? 98  ARG C CG    1 
ATOM   8452  C CD    . ARG C  1 98  ? -18.435 57.739  163.836 1.00 33.85  ? 98  ARG C CD    1 
ATOM   8453  N NE    . ARG C  1 98  ? -19.039 57.958  162.523 1.00 33.61  ? 98  ARG C NE    1 
ATOM   8454  C CZ    . ARG C  1 98  ? -18.555 57.485  161.377 1.00 38.25  ? 98  ARG C CZ    1 
ATOM   8455  N NH1   . ARG C  1 98  ? -17.449 56.750  161.364 1.00 30.22  ? 98  ARG C NH1   1 
ATOM   8456  N NH2   . ARG C  1 98  ? -19.184 57.746  160.239 1.00 34.12  ? 98  ARG C NH2   1 
ATOM   8457  N N     . LEU C  1 99  ? -15.139 57.135  166.820 1.00 31.27  ? 99  LEU C N     1 
ATOM   8458  C CA    . LEU C  1 99  ? -14.320 57.541  167.955 1.00 34.12  ? 99  LEU C CA    1 
ATOM   8459  C C     . LEU C  1 99  ? -14.851 58.842  168.543 1.00 37.27  ? 99  LEU C C     1 
ATOM   8460  O O     . LEU C  1 99  ? -15.241 59.746  167.807 1.00 32.91  ? 99  LEU C O     1 
ATOM   8461  C CB    . LEU C  1 99  ? -12.859 57.712  167.532 1.00 32.21  ? 99  LEU C CB    1 
ATOM   8462  C CG    . LEU C  1 99  ? -12.141 56.498  166.930 1.00 34.45  ? 99  LEU C CG    1 
ATOM   8463  C CD1   . LEU C  1 99  ? -10.856 56.933  166.237 1.00 30.51  ? 99  LEU C CD1   1 
ATOM   8464  C CD2   . LEU C  1 99  ? -11.842 55.461  168.003 1.00 34.60  ? 99  LEU C CD2   1 
ATOM   8465  N N     . ARG C  1 100 ? -14.871 58.939  169.867 1.00 32.84  ? 100 ARG C N     1 
ATOM   8466  C CA    . ARG C  1 100 ? -15.303 60.172  170.513 1.00 34.27  ? 100 ARG C CA    1 
ATOM   8467  C C     . ARG C  1 100 ? -14.426 60.533  171.704 1.00 34.57  ? 100 ARG C C     1 
ATOM   8468  O O     . ARG C  1 100 ? -14.192 59.714  172.592 1.00 28.75  ? 100 ARG C O     1 
ATOM   8469  C CB    . ARG C  1 100 ? -16.764 60.071  170.964 1.00 34.80  ? 100 ARG C CB    1 
ATOM   8470  C CG    . ARG C  1 100 ? -17.304 61.372  171.546 1.00 40.51  ? 100 ARG C CG    1 
ATOM   8471  C CD    . ARG C  1 100 ? -18.809 61.320  171.776 1.00 35.05  ? 100 ARG C CD    1 
ATOM   8472  N NE    . ARG C  1 100 ? -19.179 60.502  172.926 1.00 37.79  ? 100 ARG C NE    1 
ATOM   8473  C CZ    . ARG C  1 100 ? -20.431 60.326  173.342 1.00 44.79  ? 100 ARG C CZ    1 
ATOM   8474  N NH1   . ARG C  1 100 ? -20.683 59.569  174.401 1.00 44.41  ? 100 ARG C NH1   1 
ATOM   8475  N NH2   . ARG C  1 100 ? -21.433 60.910  172.700 1.00 38.97  ? 100 ARG C NH2   1 
ATOM   8476  N N     . SER C  1 101 ? -13.950 61.772  171.713 1.00 38.01  ? 101 SER C N     1 
ATOM   8477  C CA    . SER C  1 101 ? -13.169 62.289  172.825 1.00 38.76  ? 101 SER C CA    1 
ATOM   8478  C C     . SER C  1 101 ? -14.011 63.263  173.644 1.00 39.50  ? 101 SER C C     1 
ATOM   8479  O O     . SER C  1 101 ? -14.431 62.952  174.759 1.00 43.74  ? 101 SER C O     1 
ATOM   8480  C CB    . SER C  1 101 ? -11.898 62.976  172.321 1.00 35.83  ? 101 SER C CB    1 
ATOM   8481  O OG    . SER C  1 101 ? -11.199 63.598  173.383 1.00 38.60  ? 101 SER C OG    1 
ATOM   8482  N N     . GLY C  1 102 ? -14.255 64.443  173.080 1.00 41.19  ? 102 GLY C N     1 
ATOM   8483  C CA    . GLY C  1 102 ? -15.035 65.471  173.747 1.00 42.98  ? 102 GLY C CA    1 
ATOM   8484  C C     . GLY C  1 102 ? -16.425 65.606  173.156 1.00 44.25  ? 102 GLY C C     1 
ATOM   8485  O O     . GLY C  1 102 ? -17.319 66.197  173.764 1.00 48.27  ? 102 GLY C O     1 
ATOM   8486  N N     . GLY C  1 103 ? -16.605 65.059  171.958 1.00 43.72  ? 103 GLY C N     1 
ATOM   8487  C CA    . GLY C  1 103 ? -17.896 65.065  171.296 1.00 43.26  ? 103 GLY C CA    1 
ATOM   8488  C C     . GLY C  1 103 ? -18.354 66.432  170.821 1.00 43.18  ? 103 GLY C C     1 
ATOM   8489  O O     . GLY C  1 103 ? -19.555 66.694  170.752 1.00 43.87  ? 103 GLY C O     1 
ATOM   8490  N N     . HIS C  1 104 ? -17.405 67.299  170.477 1.00 37.39  ? 104 HIS C N     1 
ATOM   8491  C CA    . HIS C  1 104 ? -17.732 68.671  170.092 1.00 40.53  ? 104 HIS C CA    1 
ATOM   8492  C C     . HIS C  1 104 ? -17.908 68.843  168.591 1.00 40.48  ? 104 HIS C C     1 
ATOM   8493  O O     . HIS C  1 104 ? -18.021 69.968  168.103 1.00 38.70  ? 104 HIS C O     1 
ATOM   8494  C CB    . HIS C  1 104 ? -16.658 69.641  170.591 1.00 39.08  ? 104 HIS C CB    1 
ATOM   8495  C CG    . HIS C  1 104 ? -17.003 70.302  171.889 1.00 43.12  ? 104 HIS C CG    1 
ATOM   8496  N ND1   . HIS C  1 104 ? -17.692 71.496  171.957 1.00 41.52  ? 104 HIS C ND1   1 
ATOM   8497  C CD2   . HIS C  1 104 ? -16.764 69.929  173.168 1.00 41.80  ? 104 HIS C CD2   1 
ATOM   8498  C CE1   . HIS C  1 104 ? -17.858 71.829  173.226 1.00 40.95  ? 104 HIS C CE1   1 
ATOM   8499  N NE2   . HIS C  1 104 ? -17.305 70.898  173.980 1.00 40.88  ? 104 HIS C NE2   1 
ATOM   8500  N N     . SER C  1 105 ? -17.929 67.727  167.869 1.00 40.51  ? 105 SER C N     1 
ATOM   8501  C CA    . SER C  1 105 ? -18.169 67.751  166.433 1.00 38.54  ? 105 SER C CA    1 
ATOM   8502  C C     . SER C  1 105 ? -19.393 68.598  166.106 1.00 41.41  ? 105 SER C C     1 
ATOM   8503  O O     . SER C  1 105 ? -20.502 68.305  166.553 1.00 33.62  ? 105 SER C O     1 
ATOM   8504  C CB    . SER C  1 105 ? -18.349 66.334  165.891 1.00 37.63  ? 105 SER C CB    1 
ATOM   8505  O OG    . SER C  1 105 ? -18.732 66.364  164.528 1.00 39.68  ? 105 SER C OG    1 
ATOM   8506  N N     . TYR C  1 106 ? -19.173 69.661  165.341 1.00 38.69  ? 106 TYR C N     1 
ATOM   8507  C CA    . TYR C  1 106 ? -20.251 70.560  164.951 1.00 41.55  ? 106 TYR C CA    1 
ATOM   8508  C C     . TYR C  1 106 ? -21.343 69.813  164.194 1.00 43.37  ? 106 TYR C C     1 
ATOM   8509  O O     . TYR C  1 106 ? -22.505 70.219  164.206 1.00 43.60  ? 106 TYR C O     1 
ATOM   8510  C CB    . TYR C  1 106 ? -19.711 71.704  164.094 1.00 35.78  ? 106 TYR C CB    1 
ATOM   8511  C CG    . TYR C  1 106 ? -18.889 72.720  164.852 1.00 42.73  ? 106 TYR C CG    1 
ATOM   8512  C CD1   . TYR C  1 106 ? -18.869 72.741  166.242 1.00 42.71  ? 106 TYR C CD1   1 
ATOM   8513  C CD2   . TYR C  1 106 ? -18.138 73.665  164.174 1.00 40.98  ? 106 TYR C CD2   1 
ATOM   8514  C CE1   . TYR C  1 106 ? -18.118 73.679  166.930 1.00 42.33  ? 106 TYR C CE1   1 
ATOM   8515  C CE2   . TYR C  1 106 ? -17.395 74.607  164.848 1.00 42.47  ? 106 TYR C CE2   1 
ATOM   8516  C CZ    . TYR C  1 106 ? -17.384 74.611  166.224 1.00 42.70  ? 106 TYR C CZ    1 
ATOM   8517  O OH    . TYR C  1 106 ? -16.633 75.550  166.891 1.00 46.10  ? 106 TYR C OH    1 
ATOM   8518  N N     . GLU C  1 107 ? -20.962 68.719  163.540 1.00 43.81  ? 107 GLU C N     1 
ATOM   8519  C CA    . GLU C  1 107 ? -21.892 67.927  162.743 1.00 38.06  ? 107 GLU C CA    1 
ATOM   8520  C C     . GLU C  1 107 ? -22.184 66.560  163.367 1.00 37.79  ? 107 GLU C C     1 
ATOM   8521  O O     . GLU C  1 107 ? -22.739 65.678  162.706 1.00 40.69  ? 107 GLU C O     1 
ATOM   8522  C CB    . GLU C  1 107 ? -21.340 67.741  161.326 1.00 40.20  ? 107 GLU C CB    1 
ATOM   8523  C CG    . GLU C  1 107 ? -21.185 69.028  160.528 1.00 42.96  ? 107 GLU C CG    1 
ATOM   8524  C CD    . GLU C  1 107 ? -22.476 69.470  159.855 1.00 49.97  ? 107 GLU C CD    1 
ATOM   8525  O OE1   . GLU C  1 107 ? -23.560 68.991  160.252 1.00 44.99  ? 107 GLU C OE1   1 
ATOM   8526  O OE2   . GLU C  1 107 ? -22.403 70.296  158.920 1.00 45.27  ? 107 GLU C OE2   1 
ATOM   8527  N N     . GLY C  1 108 ? -21.809 66.389  164.633 1.00 42.45  ? 108 GLY C N     1 
ATOM   8528  C CA    . GLY C  1 108 ? -22.076 65.158  165.360 1.00 41.12  ? 108 GLY C CA    1 
ATOM   8529  C C     . GLY C  1 108 ? -21.448 63.917  164.756 1.00 42.45  ? 108 GLY C C     1 
ATOM   8530  O O     . GLY C  1 108 ? -21.975 62.814  164.892 1.00 41.12  ? 108 GLY C O     1 
ATOM   8531  N N     . LEU C  1 109 ? -20.306 64.094  164.101 1.00 38.41  ? 109 LEU C N     1 
ATOM   8532  C CA    . LEU C  1 109 ? -19.680 63.017  163.341 1.00 37.40  ? 109 LEU C CA    1 
ATOM   8533  C C     . LEU C  1 109 ? -18.936 61.999  164.207 1.00 38.70  ? 109 LEU C C     1 
ATOM   8534  O O     . LEU C  1 109 ? -18.422 61.005  163.694 1.00 38.63  ? 109 LEU C O     1 
ATOM   8535  C CB    . LEU C  1 109 ? -18.714 63.601  162.307 1.00 39.76  ? 109 LEU C CB    1 
ATOM   8536  C CG    . LEU C  1 109 ? -19.346 64.468  161.218 1.00 40.79  ? 109 LEU C CG    1 
ATOM   8537  C CD1   . LEU C  1 109 ? -18.298 64.912  160.208 1.00 40.99  ? 109 LEU C CD1   1 
ATOM   8538  C CD2   . LEU C  1 109 ? -20.475 63.723  160.527 1.00 39.73  ? 109 LEU C CD2   1 
ATOM   8539  N N     . SER C  1 110 ? -18.869 62.240  165.512 1.00 37.55  ? 110 SER C N     1 
ATOM   8540  C CA    . SER C  1 110 ? -18.158 61.324  166.395 1.00 31.33  ? 110 SER C CA    1 
ATOM   8541  C C     . SER C  1 110 ? -19.107 60.320  167.039 1.00 39.65  ? 110 SER C C     1 
ATOM   8542  O O     . SER C  1 110 ? -18.667 59.375  167.690 1.00 37.64  ? 110 SER C O     1 
ATOM   8543  C CB    . SER C  1 110 ? -17.401 62.092  167.480 1.00 36.68  ? 110 SER C CB    1 
ATOM   8544  O OG    . SER C  1 110 ? -18.260 62.978  168.181 1.00 39.05  ? 110 SER C OG    1 
ATOM   8545  N N     . TYR C  1 111 ? -20.406 60.521  166.849 1.00 36.24  ? 111 TYR C N     1 
ATOM   8546  C CA    . TYR C  1 111 ? -21.392 59.653  167.476 1.00 37.22  ? 111 TYR C CA    1 
ATOM   8547  C C     . TYR C  1 111 ? -22.604 59.385  166.582 1.00 42.48  ? 111 TYR C C     1 
ATOM   8548  O O     . TYR C  1 111 ? -23.645 58.943  167.065 1.00 36.62  ? 111 TYR C O     1 
ATOM   8549  C CB    . TYR C  1 111 ? -21.845 60.252  168.813 1.00 40.24  ? 111 TYR C CB    1 
ATOM   8550  C CG    . TYR C  1 111 ? -22.247 61.713  168.742 1.00 42.80  ? 111 TYR C CG    1 
ATOM   8551  C CD1   . TYR C  1 111 ? -23.562 62.081  168.491 1.00 42.49  ? 111 TYR C CD1   1 
ATOM   8552  C CD2   . TYR C  1 111 ? -21.310 62.723  168.932 1.00 40.82  ? 111 TYR C CD2   1 
ATOM   8553  C CE1   . TYR C  1 111 ? -23.933 63.416  168.425 1.00 44.62  ? 111 TYR C CE1   1 
ATOM   8554  C CE2   . TYR C  1 111 ? -21.670 64.061  168.866 1.00 44.49  ? 111 TYR C CE2   1 
ATOM   8555  C CZ    . TYR C  1 111 ? -22.986 64.400  168.614 1.00 46.14  ? 111 TYR C CZ    1 
ATOM   8556  O OH    . TYR C  1 111 ? -23.345 65.727  168.548 1.00 43.20  ? 111 TYR C OH    1 
ATOM   8557  N N     . THR C  1 112 ? -22.470 59.651  165.285 1.00 40.45  ? 112 THR C N     1 
ATOM   8558  C CA    . THR C  1 112 ? -23.525 59.325  164.326 1.00 37.81  ? 112 THR C CA    1 
ATOM   8559  C C     . THR C  1 112 ? -22.945 58.664  163.079 1.00 43.72  ? 112 THR C C     1 
ATOM   8560  O O     . THR C  1 112 ? -21.787 58.890  162.722 1.00 42.06  ? 112 THR C O     1 
ATOM   8561  C CB    . THR C  1 112 ? -24.331 60.573  163.892 1.00 39.72  ? 112 THR C CB    1 
ATOM   8562  O OG1   . THR C  1 112 ? -23.503 61.435  163.099 1.00 38.14  ? 112 THR C OG1   1 
ATOM   8563  C CG2   . THR C  1 112 ? -24.854 61.335  165.100 1.00 38.74  ? 112 THR C CG2   1 
ATOM   8564  N N     . SER C  1 113 ? -23.765 57.853  162.419 1.00 38.51  ? 113 SER C N     1 
ATOM   8565  C CA    . SER C  1 113 ? -23.366 57.157  161.199 1.00 43.51  ? 113 SER C CA    1 
ATOM   8566  C C     . SER C  1 113 ? -24.604 56.615  160.487 1.00 42.75  ? 113 SER C C     1 
ATOM   8567  O O     . SER C  1 113 ? -25.542 56.164  161.140 1.00 40.94  ? 113 SER C O     1 
ATOM   8568  C CB    . SER C  1 113 ? -22.391 56.021  161.517 1.00 37.35  ? 113 SER C CB    1 
ATOM   8569  O OG    . SER C  1 113 ? -22.132 55.231  160.370 1.00 38.99  ? 113 SER C OG    1 
ATOM   8570  N N     . ASP C  1 114 ? -24.618 56.660  159.158 1.00 45.80  ? 114 ASP C N     1 
ATOM   8571  C CA    . ASP C  1 114 ? -25.772 56.158  158.418 1.00 51.29  ? 114 ASP C CA    1 
ATOM   8572  C C     . ASP C  1 114 ? -25.700 54.641  158.243 1.00 55.55  ? 114 ASP C C     1 
ATOM   8573  O O     . ASP C  1 114 ? -26.564 54.031  157.612 1.00 52.40  ? 114 ASP C O     1 
ATOM   8574  C CB    . ASP C  1 114 ? -25.900 56.854  157.057 1.00 54.85  ? 114 ASP C CB    1 
ATOM   8575  C CG    . ASP C  1 114 ? -24.618 56.814  156.246 1.00 73.68  ? 114 ASP C CG    1 
ATOM   8576  O OD1   . ASP C  1 114 ? -23.713 56.018  156.573 1.00 69.78  ? 114 ASP C OD1   1 
ATOM   8577  O OD2   . ASP C  1 114 ? -24.520 57.586  155.266 1.00 86.76  ? 114 ASP C OD2   1 
ATOM   8578  N N     . THR C  1 115 ? -24.660 54.041  158.810 1.00 48.81  ? 115 THR C N     1 
ATOM   8579  C CA    . THR C  1 115 ? -24.546 52.592  158.877 1.00 46.32  ? 115 THR C CA    1 
ATOM   8580  C C     . THR C  1 115 ? -24.490 52.177  160.343 1.00 43.18  ? 115 THR C C     1 
ATOM   8581  O O     . THR C  1 115 ? -24.168 53.001  161.200 1.00 45.04  ? 115 THR C O     1 
ATOM   8582  C CB    . THR C  1 115 ? -23.292 52.084  158.136 1.00 50.22  ? 115 THR C CB    1 
ATOM   8583  O OG1   . THR C  1 115 ? -22.122 52.714  158.676 1.00 50.37  ? 115 THR C OG1   1 
ATOM   8584  C CG2   . THR C  1 115 ? -23.393 52.390  156.649 1.00 49.49  ? 115 THR C CG2   1 
ATOM   8585  N N     . PRO C  1 116 ? -24.831 50.911  160.646 1.00 42.13  ? 116 PRO C N     1 
ATOM   8586  C CA    . PRO C  1 116 ? -24.690 50.439  162.029 1.00 42.69  ? 116 PRO C CA    1 
ATOM   8587  C C     . PRO C  1 116 ? -23.278 50.672  162.543 1.00 43.41  ? 116 PRO C C     1 
ATOM   8588  O O     . PRO C  1 116 ? -22.320 50.316  161.861 1.00 39.94  ? 116 PRO C O     1 
ATOM   8589  C CB    . PRO C  1 116 ? -24.990 48.944  161.923 1.00 41.06  ? 116 PRO C CB    1 
ATOM   8590  C CG    . PRO C  1 116 ? -25.894 48.834  160.755 1.00 44.02  ? 116 PRO C CG    1 
ATOM   8591  C CD    . PRO C  1 116 ? -25.442 49.887  159.778 1.00 45.00  ? 116 PRO C CD    1 
ATOM   8592  N N     . PHE C  1 117 ? -23.141 51.272  163.718 1.00 41.79  ? 117 PHE C N     1 
ATOM   8593  C CA    . PHE C  1 117 ? -21.812 51.621  164.196 1.00 39.27  ? 117 PHE C CA    1 
ATOM   8594  C C     . PHE C  1 117 ? -21.622 51.354  165.679 1.00 41.10  ? 117 PHE C C     1 
ATOM   8595  O O     . PHE C  1 117 ? -22.581 51.300  166.446 1.00 39.28  ? 117 PHE C O     1 
ATOM   8596  C CB    . PHE C  1 117 ? -21.503 53.092  163.883 1.00 32.95  ? 117 PHE C CB    1 
ATOM   8597  C CG    . PHE C  1 117 ? -22.366 54.080  164.623 1.00 39.09  ? 117 PHE C CG    1 
ATOM   8598  C CD1   . PHE C  1 117 ? -21.842 54.838  165.659 1.00 37.98  ? 117 PHE C CD1   1 
ATOM   8599  C CD2   . PHE C  1 117 ? -23.692 54.269  164.269 1.00 43.82  ? 117 PHE C CD2   1 
ATOM   8600  C CE1   . PHE C  1 117 ? -22.628 55.760  166.331 1.00 42.67  ? 117 PHE C CE1   1 
ATOM   8601  C CE2   . PHE C  1 117 ? -24.480 55.185  164.941 1.00 42.63  ? 117 PHE C CE2   1 
ATOM   8602  C CZ    . PHE C  1 117 ? -23.946 55.931  165.971 1.00 41.37  ? 117 PHE C CZ    1 
ATOM   8603  N N     . ILE C  1 118 ? -20.364 51.168  166.063 1.00 36.24  ? 118 ILE C N     1 
ATOM   8604  C CA    . ILE C  1 118 ? -19.988 51.023  167.458 1.00 36.20  ? 118 ILE C CA    1 
ATOM   8605  C C     . ILE C  1 118 ? -19.242 52.270  167.900 1.00 35.60  ? 118 ILE C C     1 
ATOM   8606  O O     . ILE C  1 118 ? -18.356 52.755  167.196 1.00 35.74  ? 118 ILE C O     1 
ATOM   8607  C CB    . ILE C  1 118 ? -19.109 49.781  167.682 1.00 39.52  ? 118 ILE C CB    1 
ATOM   8608  C CG1   . ILE C  1 118 ? -19.839 48.528  167.200 1.00 38.86  ? 118 ILE C CG1   1 
ATOM   8609  C CG2   . ILE C  1 118 ? -18.746 49.645  169.147 1.00 33.72  ? 118 ILE C CG2   1 
ATOM   8610  C CD1   . ILE C  1 118 ? -21.092 48.219  167.990 1.00 35.67  ? 118 ILE C CD1   1 
ATOM   8611  N N     . LEU C  1 119 ? -19.611 52.800  169.059 1.00 36.90  ? 119 LEU C N     1 
ATOM   8612  C CA    . LEU C  1 119 ? -18.962 53.997  169.570 1.00 36.57  ? 119 LEU C CA    1 
ATOM   8613  C C     . LEU C  1 119 ? -17.854 53.670  170.561 1.00 33.45  ? 119 LEU C C     1 
ATOM   8614  O O     . LEU C  1 119 ? -18.099 53.078  171.613 1.00 36.25  ? 119 LEU C O     1 
ATOM   8615  C CB    . LEU C  1 119 ? -19.986 54.923  170.226 1.00 34.00  ? 119 LEU C CB    1 
ATOM   8616  C CG    . LEU C  1 119 ? -19.402 56.198  170.841 1.00 39.42  ? 119 LEU C CG    1 
ATOM   8617  C CD1   . LEU C  1 119 ? -18.610 56.988  169.811 1.00 35.58  ? 119 LEU C CD1   1 
ATOM   8618  C CD2   . LEU C  1 119 ? -20.507 57.059  171.449 1.00 43.13  ? 119 LEU C CD2   1 
ATOM   8619  N N     . ILE C  1 120 ? -16.635 54.059  170.210 1.00 33.93  ? 120 ILE C N     1 
ATOM   8620  C CA    . ILE C  1 120 ? -15.516 53.981  171.135 1.00 34.50  ? 120 ILE C CA    1 
ATOM   8621  C C     . ILE C  1 120 ? -15.364 55.326  171.831 1.00 33.90  ? 120 ILE C C     1 
ATOM   8622  O O     . ILE C  1 120 ? -14.962 56.309  171.212 1.00 36.05  ? 120 ILE C O     1 
ATOM   8623  C CB    . ILE C  1 120 ? -14.200 53.615  170.424 1.00 32.58  ? 120 ILE C CB    1 
ATOM   8624  C CG1   . ILE C  1 120 ? -14.383 52.364  169.562 1.00 29.58  ? 120 ILE C CG1   1 
ATOM   8625  C CG2   . ILE C  1 120 ? -13.083 53.414  171.441 1.00 30.66  ? 120 ILE C CG2   1 
ATOM   8626  C CD1   . ILE C  1 120 ? -13.172 52.022  168.724 1.00 34.23  ? 120 ILE C CD1   1 
ATOM   8627  N N     . ASP C  1 121 ? -15.702 55.373  173.115 1.00 35.87  ? 121 ASP C N     1 
ATOM   8628  C CA    . ASP C  1 121 ? -15.610 56.616  173.868 1.00 40.05  ? 121 ASP C CA    1 
ATOM   8629  C C     . ASP C  1 121 ? -14.359 56.610  174.738 1.00 36.03  ? 121 ASP C C     1 
ATOM   8630  O O     . ASP C  1 121 ? -14.146 55.694  175.531 1.00 37.87  ? 121 ASP C O     1 
ATOM   8631  C CB    . ASP C  1 121 ? -16.854 56.831  174.730 1.00 37.77  ? 121 ASP C CB    1 
ATOM   8632  C CG    . ASP C  1 121 ? -16.988 58.265  175.203 1.00 46.38  ? 121 ASP C CG    1 
ATOM   8633  O OD1   . ASP C  1 121 ? -17.886 58.975  174.704 1.00 52.53  ? 121 ASP C OD1   1 
ATOM   8634  O OD2   . ASP C  1 121 ? -16.187 58.691  176.062 1.00 44.41  ? 121 ASP C OD2   1 
ATOM   8635  N N     . LEU C  1 122 ? -13.547 57.651  174.594 1.00 39.48  ? 122 LEU C N     1 
ATOM   8636  C CA    . LEU C  1 122 ? -12.210 57.674  175.175 1.00 40.79  ? 122 LEU C CA    1 
ATOM   8637  C C     . LEU C  1 122 ? -12.121 58.404  176.511 1.00 43.29  ? 122 LEU C C     1 
ATOM   8638  O O     . LEU C  1 122 ? -11.025 58.735  176.961 1.00 41.83  ? 122 LEU C O     1 
ATOM   8639  C CB    . LEU C  1 122 ? -11.240 58.313  174.184 1.00 33.29  ? 122 LEU C CB    1 
ATOM   8640  C CG    . LEU C  1 122 ? -11.261 57.644  172.811 1.00 37.88  ? 122 LEU C CG    1 
ATOM   8641  C CD1   . LEU C  1 122 ? -10.652 58.543  171.770 1.00 33.42  ? 122 LEU C CD1   1 
ATOM   8642  C CD2   . LEU C  1 122 ? -10.532 56.307  172.856 1.00 37.70  ? 122 LEU C CD2   1 
ATOM   8643  N N     . MET C  1 123 ? -13.266 58.637  177.145 1.00 40.36  ? 123 MET C N     1 
ATOM   8644  C CA    . MET C  1 123 ? -13.316 59.446  178.360 1.00 45.62  ? 123 MET C CA    1 
ATOM   8645  C C     . MET C  1 123 ? -12.478 58.863  179.499 1.00 40.04  ? 123 MET C C     1 
ATOM   8646  O O     . MET C  1 123 ? -12.025 59.599  180.376 1.00 47.06  ? 123 MET C O     1 
ATOM   8647  C CB    . MET C  1 123 ? -14.765 59.630  178.822 1.00 42.41  ? 123 MET C CB    1 
ATOM   8648  C CG    . MET C  1 123 ? -15.400 58.394  179.442 1.00 43.80  ? 123 MET C CG    1 
ATOM   8649  S SD    . MET C  1 123 ? -17.015 58.742  180.163 1.00 56.86  ? 123 MET C SD    1 
ATOM   8650  C CE    . MET C  1 123 ? -17.961 59.155  178.699 1.00 43.30  ? 123 MET C CE    1 
ATOM   8651  N N     . ASN C  1 124 ? -12.270 57.551  179.488 1.00 35.59  ? 124 ASN C N     1 
ATOM   8652  C CA    . ASN C  1 124 ? -11.454 56.910  180.515 1.00 41.05  ? 124 ASN C CA    1 
ATOM   8653  C C     . ASN C  1 124 ? -9.967  56.997  180.207 1.00 41.55  ? 124 ASN C C     1 
ATOM   8654  O O     . ASN C  1 124 ? -9.129  56.597  181.018 1.00 48.66  ? 124 ASN C O     1 
ATOM   8655  C CB    . ASN C  1 124 ? -11.861 55.451  180.694 1.00 39.03  ? 124 ASN C CB    1 
ATOM   8656  C CG    . ASN C  1 124 ? -13.199 55.309  181.375 1.00 48.18  ? 124 ASN C CG    1 
ATOM   8657  O OD1   . ASN C  1 124 ? -13.748 56.287  181.880 1.00 50.60  ? 124 ASN C OD1   1 
ATOM   8658  N ND2   . ASN C  1 124 ? -13.731 54.092  181.404 1.00 45.62  ? 124 ASN C ND2   1 
ATOM   8659  N N     . LEU C  1 125 ? -9.649  57.519  179.028 1.00 40.11  ? 125 LEU C N     1 
ATOM   8660  C CA    . LEU C  1 125 ? -8.268  57.788  178.655 1.00 44.39  ? 125 LEU C CA    1 
ATOM   8661  C C     . LEU C  1 125 ? -7.998  59.280  178.795 1.00 44.93  ? 125 LEU C C     1 
ATOM   8662  O O     . LEU C  1 125 ? -7.835  59.982  177.803 1.00 37.04  ? 125 LEU C O     1 
ATOM   8663  C CB    . LEU C  1 125 ? -7.990  57.322  177.225 1.00 36.43  ? 125 LEU C CB    1 
ATOM   8664  C CG    . LEU C  1 125 ? -8.163  55.828  176.954 1.00 41.72  ? 125 LEU C CG    1 
ATOM   8665  C CD1   . LEU C  1 125 ? -7.873  55.520  175.500 1.00 41.65  ? 125 LEU C CD1   1 
ATOM   8666  C CD2   . LEU C  1 125 ? -7.262  55.014  177.866 1.00 37.40  ? 125 LEU C CD2   1 
ATOM   8667  N N     . ASN C  1 126 ? -7.966  59.763  180.032 1.00 44.59  ? 126 ASN C N     1 
ATOM   8668  C CA    . ASN C  1 126 ? -7.826  61.192  180.275 1.00 44.82  ? 126 ASN C CA    1 
ATOM   8669  C C     . ASN C  1 126 ? -6.656  61.539  181.188 1.00 51.27  ? 126 ASN C C     1 
ATOM   8670  O O     . ASN C  1 126 ? -6.709  62.519  181.930 1.00 49.87  ? 126 ASN C O     1 
ATOM   8671  C CB    . ASN C  1 126 ? -9.120  61.751  180.868 1.00 50.84  ? 126 ASN C CB    1 
ATOM   8672  C CG    . ASN C  1 126 ? -9.474  61.117  182.200 1.00 54.16  ? 126 ASN C CG    1 
ATOM   8673  O OD1   . ASN C  1 126 ? -8.881  60.116  182.605 1.00 54.08  ? 126 ASN C OD1   1 
ATOM   8674  N ND2   . ASN C  1 126 ? -10.453 61.694  182.885 1.00 55.46  ? 126 ASN C ND2   1 
ATOM   8675  N N     . ARG C  1 127 ? -5.600  60.738  181.130 1.00 44.08  ? 127 ARG C N     1 
ATOM   8676  C CA    . ARG C  1 127 ? -4.425  60.974  181.959 1.00 48.03  ? 127 ARG C CA    1 
ATOM   8677  C C     . ARG C  1 127 ? -3.481  61.980  181.322 1.00 47.50  ? 127 ARG C C     1 
ATOM   8678  O O     . ARG C  1 127 ? -3.237  61.938  180.117 1.00 41.31  ? 127 ARG C O     1 
ATOM   8679  C CB    . ARG C  1 127 ? -3.676  59.669  182.218 1.00 48.67  ? 127 ARG C CB    1 
ATOM   8680  C CG    . ARG C  1 127 ? -4.453  58.673  183.046 1.00 55.83  ? 127 ARG C CG    1 
ATOM   8681  C CD    . ARG C  1 127 ? -3.853  57.287  182.916 1.00 67.04  ? 127 ARG C CD    1 
ATOM   8682  N NE    . ARG C  1 127 ? -4.790  56.243  183.319 1.00 63.92  ? 127 ARG C NE    1 
ATOM   8683  C CZ    . ARG C  1 127 ? -5.823  55.845  182.584 1.00 65.18  ? 127 ARG C CZ    1 
ATOM   8684  N NH1   . ARG C  1 127 ? -6.061  56.412  181.409 1.00 55.03  ? 127 ARG C NH1   1 
ATOM   8685  N NH2   . ARG C  1 127 ? -6.626  54.887  183.025 1.00 71.55  ? 127 ARG C NH2   1 
ATOM   8686  N N     . VAL C  1 128 ? -2.949  62.879  182.142 1.00 51.46  ? 128 VAL C N     1 
ATOM   8687  C CA    . VAL C  1 128 ? -1.942  63.830  181.691 1.00 49.21  ? 128 VAL C CA    1 
ATOM   8688  C C     . VAL C  1 128 ? -0.646  63.612  182.463 1.00 46.28  ? 128 VAL C C     1 
ATOM   8689  O O     . VAL C  1 128 ? -0.647  63.584  183.692 1.00 47.40  ? 128 VAL C O     1 
ATOM   8690  C CB    . VAL C  1 128 ? -2.409  65.288  181.866 1.00 47.64  ? 128 VAL C CB    1 
ATOM   8691  C CG1   . VAL C  1 128 ? -1.347  66.253  181.355 1.00 45.50  ? 128 VAL C CG1   1 
ATOM   8692  C CG2   . VAL C  1 128 ? -3.725  65.512  181.147 1.00 41.86  ? 128 VAL C CG2   1 
ATOM   8693  N N     . SER C  1 129 ? 0.453   63.444  181.738 1.00 48.77  ? 129 SER C N     1 
ATOM   8694  C CA    . SER C  1 129 ? 1.754   63.244  182.362 1.00 45.56  ? 129 SER C CA    1 
ATOM   8695  C C     . SER C  1 129 ? 2.709   64.363  181.968 1.00 50.97  ? 129 SER C C     1 
ATOM   8696  O O     . SER C  1 129 ? 3.146   64.440  180.821 1.00 49.93  ? 129 SER C O     1 
ATOM   8697  C CB    . SER C  1 129 ? 2.334   61.886  181.967 1.00 49.12  ? 129 SER C CB    1 
ATOM   8698  O OG    . SER C  1 129 ? 1.380   60.856  182.159 1.00 64.42  ? 129 SER C OG    1 
ATOM   8699  N N     . ILE C  1 130 ? 3.032   65.225  182.924 1.00 52.18  ? 130 ILE C N     1 
ATOM   8700  C CA    . ILE C  1 130 ? 3.871   66.382  182.650 1.00 50.93  ? 130 ILE C CA    1 
ATOM   8701  C C     . ILE C  1 130 ? 5.320   66.144  183.059 1.00 49.13  ? 130 ILE C C     1 
ATOM   8702  O O     . ILE C  1 130 ? 5.596   65.694  184.171 1.00 53.06  ? 130 ILE C O     1 
ATOM   8703  C CB    . ILE C  1 130 ? 3.337   67.632  183.367 1.00 46.62  ? 130 ILE C CB    1 
ATOM   8704  C CG1   . ILE C  1 130 ? 1.968   68.006  182.800 1.00 50.26  ? 130 ILE C CG1   1 
ATOM   8705  C CG2   . ILE C  1 130 ? 4.308   68.790  183.218 1.00 48.77  ? 130 ILE C CG2   1 
ATOM   8706  C CD1   . ILE C  1 130 ? 1.212   69.001  183.630 1.00 49.16  ? 130 ILE C CD1   1 
ATOM   8707  N N     . ASP C  1 131 ? 6.239   66.437  182.143 1.00 53.03  ? 131 ASP C N     1 
ATOM   8708  C CA    . ASP C  1 131 ? 7.667   66.349  182.420 1.00 51.95  ? 131 ASP C CA    1 
ATOM   8709  C C     . ASP C  1 131 ? 8.264   67.755  182.443 1.00 52.28  ? 131 ASP C C     1 
ATOM   8710  O O     . ASP C  1 131 ? 8.416   68.390  181.402 1.00 51.01  ? 131 ASP C O     1 
ATOM   8711  C CB    . ASP C  1 131 ? 8.363   65.473  181.374 1.00 52.03  ? 131 ASP C CB    1 
ATOM   8712  C CG    . ASP C  1 131 ? 9.850   65.313  181.635 1.00 61.71  ? 131 ASP C CG    1 
ATOM   8713  O OD1   . ASP C  1 131 ? 10.314  65.687  182.734 1.00 63.55  ? 131 ASP C OD1   1 
ATOM   8714  O OD2   . ASP C  1 131 ? 10.558  64.800  180.742 1.00 63.49  ? 131 ASP C OD2   1 
ATOM   8715  N N     . LEU C  1 132 ? 8.598   68.233  183.639 1.00 54.71  ? 132 LEU C N     1 
ATOM   8716  C CA    . LEU C  1 132 ? 9.024   69.617  183.830 1.00 60.52  ? 132 LEU C CA    1 
ATOM   8717  C C     . LEU C  1 132 ? 10.440  69.897  183.328 1.00 63.10  ? 132 LEU C C     1 
ATOM   8718  O O     . LEU C  1 132 ? 10.814  71.054  183.131 1.00 66.26  ? 132 LEU C O     1 
ATOM   8719  C CB    . LEU C  1 132 ? 8.921   69.996  185.310 1.00 61.49  ? 132 LEU C CB    1 
ATOM   8720  C CG    . LEU C  1 132 ? 7.508   70.103  185.892 1.00 61.81  ? 132 LEU C CG    1 
ATOM   8721  C CD1   . LEU C  1 132 ? 7.550   70.370  187.390 1.00 59.55  ? 132 LEU C CD1   1 
ATOM   8722  C CD2   . LEU C  1 132 ? 6.718   71.185  185.175 1.00 59.15  ? 132 LEU C CD2   1 
ATOM   8723  N N     . GLU C  1 133 ? 11.221  68.841  183.119 1.00 61.61  ? 133 GLU C N     1 
ATOM   8724  C CA    . GLU C  1 133 ? 12.610  68.993  182.690 1.00 66.70  ? 133 GLU C CA    1 
ATOM   8725  C C     . GLU C  1 133 ? 12.729  69.223  181.185 1.00 64.43  ? 133 GLU C C     1 
ATOM   8726  O O     . GLU C  1 133 ? 13.456  70.112  180.743 1.00 65.60  ? 133 GLU C O     1 
ATOM   8727  C CB    . GLU C  1 133 ? 13.427  67.770  183.102 1.00 71.10  ? 133 GLU C CB    1 
ATOM   8728  C CG    . GLU C  1 133 ? 13.732  67.717  184.588 1.00 85.42  ? 133 GLU C CG    1 
ATOM   8729  C CD    . GLU C  1 133 ? 14.633  68.852  185.034 1.00 98.80  ? 133 GLU C CD    1 
ATOM   8730  O OE1   . GLU C  1 133 ? 15.658  69.091  184.361 1.00 93.81  ? 133 GLU C OE1   1 
ATOM   8731  O OE2   . GLU C  1 133 ? 14.315  69.510  186.049 1.00 107.24 ? 133 GLU C OE2   1 
ATOM   8732  N N     . SER C  1 134 ? 12.017  68.421  180.400 1.00 60.98  ? 134 SER C N     1 
ATOM   8733  C CA    . SER C  1 134 ? 12.003  68.600  178.952 1.00 55.88  ? 134 SER C CA    1 
ATOM   8734  C C     . SER C  1 134 ? 10.906  69.585  178.557 1.00 57.53  ? 134 SER C C     1 
ATOM   8735  O O     . SER C  1 134 ? 10.810  69.998  177.399 1.00 55.55  ? 134 SER C O     1 
ATOM   8736  C CB    . SER C  1 134 ? 11.810  67.258  178.242 1.00 56.59  ? 134 SER C CB    1 
ATOM   8737  O OG    . SER C  1 134 ? 10.685  66.560  178.749 1.00 65.77  ? 134 SER C OG    1 
ATOM   8738  N N     . GLU C  1 135 ? 10.101  69.967  179.547 1.00 54.14  ? 135 GLU C N     1 
ATOM   8739  C CA    . GLU C  1 135 ? 8.944   70.841  179.358 1.00 57.49  ? 135 GLU C CA    1 
ATOM   8740  C C     . GLU C  1 135 ? 8.028   70.305  178.262 1.00 51.63  ? 135 GLU C C     1 
ATOM   8741  O O     . GLU C  1 135 ? 7.649   71.019  177.333 1.00 49.12  ? 135 GLU C O     1 
ATOM   8742  C CB    . GLU C  1 135 ? 9.390   72.270  179.051 1.00 51.92  ? 135 GLU C CB    1 
ATOM   8743  C CG    . GLU C  1 135 ? 10.107  72.927  180.220 1.00 61.21  ? 135 GLU C CG    1 
ATOM   8744  C CD    . GLU C  1 135 ? 10.427  74.384  179.971 1.00 59.95  ? 135 GLU C CD    1 
ATOM   8745  O OE1   . GLU C  1 135 ? 10.333  74.824  178.807 1.00 62.70  ? 135 GLU C OE1   1 
ATOM   8746  O OE2   . GLU C  1 135 ? 10.766  75.091  180.943 1.00 62.25  ? 135 GLU C OE2   1 
ATOM   8747  N N     . THR C  1 136 ? 7.689   69.027  178.388 1.00 48.06  ? 136 THR C N     1 
ATOM   8748  C CA    . THR C  1 136 ? 6.736   68.376  177.501 1.00 46.95  ? 136 THR C CA    1 
ATOM   8749  C C     . THR C  1 136 ? 5.656   67.693  178.327 1.00 48.91  ? 136 THR C C     1 
ATOM   8750  O O     . THR C  1 136 ? 5.745   67.634  179.554 1.00 47.61  ? 136 THR C O     1 
ATOM   8751  C CB    . THR C  1 136 ? 7.413   67.334  176.590 1.00 43.88  ? 136 THR C CB    1 
ATOM   8752  O OG1   . THR C  1 136 ? 7.988   66.295  177.392 1.00 45.57  ? 136 THR C OG1   1 
ATOM   8753  C CG2   . THR C  1 136 ? 8.498   67.980  175.745 1.00 44.08  ? 136 THR C CG2   1 
ATOM   8754  N N     . ALA C  1 137 ? 4.638   67.175  177.653 1.00 43.77  ? 137 ALA C N     1 
ATOM   8755  C CA    . ALA C  1 137 ? 3.585   66.434  178.332 1.00 41.32  ? 137 ALA C CA    1 
ATOM   8756  C C     . ALA C  1 137 ? 3.006   65.365  177.421 1.00 40.33  ? 137 ALA C C     1 
ATOM   8757  O O     . ALA C  1 137 ? 2.870   65.575  176.215 1.00 36.12  ? 137 ALA C O     1 
ATOM   8758  C CB    . ALA C  1 137 ? 2.488   67.374  178.805 1.00 46.86  ? 137 ALA C CB    1 
ATOM   8759  N N     . TRP C  1 138 ? 2.684   64.214  178.000 1.00 40.13  ? 138 TRP C N     1 
ATOM   8760  C CA    . TRP C  1 138 ? 1.926   63.195  177.290 1.00 40.59  ? 138 TRP C CA    1 
ATOM   8761  C C     . TRP C  1 138 ? 0.461   63.319  177.675 1.00 41.82  ? 138 TRP C C     1 
ATOM   8762  O O     . TRP C  1 138 ? 0.123   63.363  178.856 1.00 43.37  ? 138 TRP C O     1 
ATOM   8763  C CB    . TRP C  1 138 ? 2.447   61.792  177.600 1.00 39.98  ? 138 TRP C CB    1 
ATOM   8764  C CG    . TRP C  1 138 ? 3.573   61.364  176.710 1.00 41.54  ? 138 TRP C CG    1 
ATOM   8765  C CD1   . TRP C  1 138 ? 4.905   61.375  177.008 1.00 40.58  ? 138 TRP C CD1   1 
ATOM   8766  C CD2   . TRP C  1 138 ? 3.465   60.868  175.369 1.00 41.97  ? 138 TRP C CD2   1 
ATOM   8767  N NE1   . TRP C  1 138 ? 5.633   60.913  175.937 1.00 39.99  ? 138 TRP C NE1   1 
ATOM   8768  C CE2   . TRP C  1 138 ? 4.773   60.596  174.918 1.00 42.41  ? 138 TRP C CE2   1 
ATOM   8769  C CE3   . TRP C  1 138 ? 2.389   60.626  174.507 1.00 40.54  ? 138 TRP C CE3   1 
ATOM   8770  C CZ2   . TRP C  1 138 ? 5.036   60.094  173.646 1.00 37.07  ? 138 TRP C CZ2   1 
ATOM   8771  C CZ3   . TRP C  1 138 ? 2.652   60.128  173.242 1.00 37.14  ? 138 TRP C CZ3   1 
ATOM   8772  C CH2   . TRP C  1 138 ? 3.966   59.866  172.824 1.00 40.25  ? 138 TRP C CH2   1 
ATOM   8773  N N     . VAL C  1 139 ? -0.406  63.389  176.672 1.00 34.21  ? 139 VAL C N     1 
ATOM   8774  C CA    . VAL C  1 139 ? -1.828  63.591  176.913 1.00 33.49  ? 139 VAL C CA    1 
ATOM   8775  C C     . VAL C  1 139 ? -2.669  62.512  176.243 1.00 35.90  ? 139 VAL C C     1 
ATOM   8776  O O     . VAL C  1 139 ? -2.763  62.470  175.018 1.00 33.80  ? 139 VAL C O     1 
ATOM   8777  C CB    . VAL C  1 139 ? -2.296  64.968  176.401 1.00 31.48  ? 139 VAL C CB    1 
ATOM   8778  C CG1   . VAL C  1 139 ? -3.742  65.209  176.785 1.00 37.55  ? 139 VAL C CG1   1 
ATOM   8779  C CG2   . VAL C  1 139 ? -1.408  66.074  176.946 1.00 38.63  ? 139 VAL C CG2   1 
ATOM   8780  N N     . GLU C  1 140 ? -3.272  61.639  177.046 1.00 35.70  ? 140 GLU C N     1 
ATOM   8781  C CA    . GLU C  1 140 ? -4.216  60.660  176.521 1.00 33.67  ? 140 GLU C CA    1 
ATOM   8782  C C     . GLU C  1 140 ? -5.373  61.397  175.846 1.00 38.69  ? 140 GLU C C     1 
ATOM   8783  O O     . GLU C  1 140 ? -5.849  62.414  176.350 1.00 40.23  ? 140 GLU C O     1 
ATOM   8784  C CB    . GLU C  1 140 ? -4.720  59.732  177.629 1.00 40.73  ? 140 GLU C CB    1 
ATOM   8785  C CG    . GLU C  1 140 ? -3.660  58.769  178.155 1.00 39.72  ? 140 GLU C CG    1 
ATOM   8786  C CD    . GLU C  1 140 ? -4.201  57.785  179.177 1.00 43.65  ? 140 GLU C CD    1 
ATOM   8787  O OE1   . GLU C  1 140 ? -5.258  58.063  179.778 1.00 47.55  ? 140 GLU C OE1   1 
ATOM   8788  O OE2   . GLU C  1 140 ? -3.564  56.729  179.379 1.00 45.87  ? 140 GLU C OE2   1 
ATOM   8789  N N     . SER C  1 141 ? -5.814  60.883  174.703 1.00 37.33  ? 141 SER C N     1 
ATOM   8790  C CA    . SER C  1 141 ? -6.674  61.639  173.793 1.00 38.15  ? 141 SER C CA    1 
ATOM   8791  C C     . SER C  1 141 ? -8.112  61.846  174.271 1.00 34.92  ? 141 SER C C     1 
ATOM   8792  O O     . SER C  1 141 ? -8.896  62.526  173.607 1.00 35.22  ? 141 SER C O     1 
ATOM   8793  C CB    . SER C  1 141 ? -6.695  60.955  172.428 1.00 31.23  ? 141 SER C CB    1 
ATOM   8794  O OG    . SER C  1 141 ? -7.158  59.621  172.536 1.00 41.22  ? 141 SER C OG    1 
ATOM   8795  N N     . GLY C  1 142 ? -8.463  61.266  175.412 1.00 36.46  ? 142 GLY C N     1 
ATOM   8796  C CA    . GLY C  1 142 ? -9.781  61.484  175.977 1.00 41.84  ? 142 GLY C CA    1 
ATOM   8797  C C     . GLY C  1 142 ? -9.790  62.724  176.849 1.00 41.45  ? 142 GLY C C     1 
ATOM   8798  O O     . GLY C  1 142 ? -10.841 63.168  177.312 1.00 42.69  ? 142 GLY C O     1 
ATOM   8799  N N     . SER C  1 143 ? -8.604  63.282  177.073 1.00 43.92  ? 143 SER C N     1 
ATOM   8800  C CA    . SER C  1 143 ? -8.462  64.479  177.890 1.00 40.79  ? 143 SER C CA    1 
ATOM   8801  C C     . SER C  1 143 ? -9.078  65.687  177.201 1.00 40.48  ? 143 SER C C     1 
ATOM   8802  O O     . SER C  1 143 ? -8.922  65.873  175.993 1.00 41.76  ? 143 SER C O     1 
ATOM   8803  C CB    . SER C  1 143 ? -6.989  64.754  178.192 1.00 37.80  ? 143 SER C CB    1 
ATOM   8804  O OG    . SER C  1 143 ? -6.384  63.658  178.855 1.00 46.52  ? 143 SER C OG    1 
ATOM   8805  N N     . THR C  1 144 ? -9.785  66.505  177.971 1.00 41.36  ? 144 THR C N     1 
ATOM   8806  C CA    . THR C  1 144 ? -10.306 67.760  177.452 1.00 42.88  ? 144 THR C CA    1 
ATOM   8807  C C     . THR C  1 144 ? -9.247  68.847  177.602 1.00 43.30  ? 144 THR C C     1 
ATOM   8808  O O     . THR C  1 144 ? -8.283  68.684  178.350 1.00 42.80  ? 144 THR C O     1 
ATOM   8809  C CB    . THR C  1 144 ? -11.599 68.189  178.170 1.00 42.83  ? 144 THR C CB    1 
ATOM   8810  O OG1   . THR C  1 144 ? -11.349 68.319  179.575 1.00 43.59  ? 144 THR C OG1   1 
ATOM   8811  C CG2   . THR C  1 144 ? -12.708 67.166  177.945 1.00 42.59  ? 144 THR C CG2   1 
ATOM   8812  N N     . LEU C  1 145 ? -9.427  69.949  176.880 1.00 43.75  ? 145 LEU C N     1 
ATOM   8813  C CA    . LEU C  1 145 ? -8.508  71.077  176.964 1.00 47.07  ? 145 LEU C CA    1 
ATOM   8814  C C     . LEU C  1 145 ? -8.446  71.605  178.391 1.00 47.93  ? 145 LEU C C     1 
ATOM   8815  O O     . LEU C  1 145 ? -7.376  71.949  178.891 1.00 45.61  ? 145 LEU C O     1 
ATOM   8816  C CB    . LEU C  1 145 ? -8.929  72.189  176.003 1.00 44.05  ? 145 LEU C CB    1 
ATOM   8817  C CG    . LEU C  1 145 ? -8.907  71.815  174.521 1.00 43.76  ? 145 LEU C CG    1 
ATOM   8818  C CD1   . LEU C  1 145 ? -9.383  72.973  173.676 1.00 42.58  ? 145 LEU C CD1   1 
ATOM   8819  C CD2   . LEU C  1 145 ? -7.512  71.386  174.095 1.00 42.74  ? 145 LEU C CD2   1 
ATOM   8820  N N     . GLY C  1 146 ? -9.604  71.644  179.043 1.00 48.11  ? 146 GLY C N     1 
ATOM   8821  C CA    . GLY C  1 146 ? -9.698  72.090  180.419 1.00 51.35  ? 146 GLY C CA    1 
ATOM   8822  C C     . GLY C  1 146 ? -8.952  71.184  181.380 1.00 49.46  ? 146 GLY C C     1 
ATOM   8823  O O     . GLY C  1 146 ? -8.270  71.660  182.286 1.00 48.34  ? 146 GLY C O     1 
ATOM   8824  N N     . GLU C  1 147 ? -9.091  69.875  181.190 1.00 50.37  ? 147 GLU C N     1 
ATOM   8825  C CA    . GLU C  1 147 ? -8.349  68.903  181.984 1.00 52.31  ? 147 GLU C CA    1 
ATOM   8826  C C     . GLU C  1 147 ? -6.851  69.080  181.765 1.00 50.93  ? 147 GLU C C     1 
ATOM   8827  O O     . GLU C  1 147 ? -6.055  68.923  182.691 1.00 52.00  ? 147 GLU C O     1 
ATOM   8828  C CB    . GLU C  1 147 ? -8.768  67.474  181.631 1.00 48.63  ? 147 GLU C CB    1 
ATOM   8829  C CG    . GLU C  1 147 ? -10.104 67.034  182.215 1.00 53.65  ? 147 GLU C CG    1 
ATOM   8830  C CD    . GLU C  1 147 ? -10.573 65.708  181.645 1.00 52.66  ? 147 GLU C CD    1 
ATOM   8831  O OE1   . GLU C  1 147 ? -10.052 65.302  180.586 1.00 49.34  ? 147 GLU C OE1   1 
ATOM   8832  O OE2   . GLU C  1 147 ? -11.461 65.073  182.251 1.00 58.09  ? 147 GLU C OE2   1 
ATOM   8833  N N     . LEU C  1 148 ? -6.476  69.415  180.534 1.00 48.81  ? 148 LEU C N     1 
ATOM   8834  C CA    . LEU C  1 148 ? -5.080  69.639  180.185 1.00 50.81  ? 148 LEU C CA    1 
ATOM   8835  C C     . LEU C  1 148 ? -4.558  70.939  180.789 1.00 53.90  ? 148 LEU C C     1 
ATOM   8836  O O     . LEU C  1 148 ? -3.501  70.951  181.423 1.00 49.23  ? 148 LEU C O     1 
ATOM   8837  C CB    . LEU C  1 148 ? -4.906  69.660  178.665 1.00 47.67  ? 148 LEU C CB    1 
ATOM   8838  C CG    . LEU C  1 148 ? -3.516  70.051  178.152 1.00 44.50  ? 148 LEU C CG    1 
ATOM   8839  C CD1   . LEU C  1 148 ? -2.445  69.144  178.737 1.00 41.43  ? 148 LEU C CD1   1 
ATOM   8840  C CD2   . LEU C  1 148 ? -3.479  70.013  176.634 1.00 38.20  ? 148 LEU C CD2   1 
ATOM   8841  N N     . TYR C  1 149 ? -5.298  72.026  180.579 1.00 52.74  ? 149 TYR C N     1 
ATOM   8842  C CA    . TYR C  1 149 ? -4.945  73.329  181.137 1.00 45.68  ? 149 TYR C CA    1 
ATOM   8843  C C     . TYR C  1 149 ? -4.784  73.245  182.649 1.00 49.46  ? 149 TYR C C     1 
ATOM   8844  O O     . TYR C  1 149 ? -3.825  73.773  183.212 1.00 50.22  ? 149 TYR C O     1 
ATOM   8845  C CB    . TYR C  1 149 ? -6.007  74.379  180.798 1.00 51.99  ? 149 TYR C CB    1 
ATOM   8846  C CG    . TYR C  1 149 ? -6.173  74.669  179.324 1.00 48.26  ? 149 TYR C CG    1 
ATOM   8847  C CD1   . TYR C  1 149 ? -5.145  74.424  178.424 1.00 50.92  ? 149 TYR C CD1   1 
ATOM   8848  C CD2   . TYR C  1 149 ? -7.364  75.188  178.836 1.00 50.81  ? 149 TYR C CD2   1 
ATOM   8849  C CE1   . TYR C  1 149 ? -5.301  74.690  177.076 1.00 51.73  ? 149 TYR C CE1   1 
ATOM   8850  C CE2   . TYR C  1 149 ? -7.531  75.456  177.495 1.00 49.14  ? 149 TYR C CE2   1 
ATOM   8851  C CZ    . TYR C  1 149 ? -6.496  75.205  176.620 1.00 50.80  ? 149 TYR C CZ    1 
ATOM   8852  O OH    . TYR C  1 149 ? -6.666  75.476  175.286 1.00 52.12  ? 149 TYR C OH    1 
ATOM   8853  N N     . TYR C  1 150 ? -5.734  72.578  183.298 1.00 55.50  ? 150 TYR C N     1 
ATOM   8854  C CA    . TYR C  1 150 ? -5.714  72.428  184.747 1.00 58.12  ? 150 TYR C CA    1 
ATOM   8855  C C     . TYR C  1 150 ? -4.471  71.686  185.217 1.00 57.76  ? 150 TYR C C     1 
ATOM   8856  O O     . TYR C  1 150 ? -3.816  72.098  186.174 1.00 58.52  ? 150 TYR C O     1 
ATOM   8857  C CB    . TYR C  1 150 ? -6.964  71.689  185.233 1.00 58.18  ? 150 TYR C CB    1 
ATOM   8858  C CG    . TYR C  1 150 ? -6.955  71.423  186.721 1.00 62.73  ? 150 TYR C CG    1 
ATOM   8859  C CD1   . TYR C  1 150 ? -7.438  72.368  187.616 1.00 64.88  ? 150 TYR C CD1   1 
ATOM   8860  C CD2   . TYR C  1 150 ? -6.450  70.232  187.235 1.00 60.73  ? 150 TYR C CD2   1 
ATOM   8861  C CE1   . TYR C  1 150 ? -7.424  72.134  188.980 1.00 67.17  ? 150 TYR C CE1   1 
ATOM   8862  C CE2   . TYR C  1 150 ? -6.431  69.991  188.594 1.00 66.66  ? 150 TYR C CE2   1 
ATOM   8863  C CZ    . TYR C  1 150 ? -6.919  70.944  189.463 1.00 71.13  ? 150 TYR C CZ    1 
ATOM   8864  O OH    . TYR C  1 150 ? -6.903  70.704  190.818 1.00 76.80  ? 150 TYR C OH    1 
ATOM   8865  N N     . ALA C  1 151 ? -4.165  70.583  184.543 1.00 56.05  ? 151 ALA C N     1 
ATOM   8866  C CA    . ALA C  1 151 ? -3.036  69.742  184.913 1.00 55.38  ? 151 ALA C CA    1 
ATOM   8867  C C     . ALA C  1 151 ? -1.725  70.514  184.845 1.00 55.78  ? 151 ALA C C     1 
ATOM   8868  O O     . ALA C  1 151 ? -0.835  70.311  185.668 1.00 58.52  ? 151 ALA C O     1 
ATOM   8869  C CB    . ALA C  1 151 ? -2.975  68.517  184.019 1.00 54.74  ? 151 ALA C CB    1 
ATOM   8870  N N     . ILE C  1 152 ? -1.619  71.408  183.867 1.00 51.09  ? 152 ILE C N     1 
ATOM   8871  C CA    . ILE C  1 152 ? -0.418  72.219  183.695 1.00 56.70  ? 152 ILE C CA    1 
ATOM   8872  C C     . ILE C  1 152 ? -0.230  73.219  184.835 1.00 58.23  ? 152 ILE C C     1 
ATOM   8873  O O     . ILE C  1 152 ? 0.856   73.321  185.402 1.00 55.85  ? 152 ILE C O     1 
ATOM   8874  C CB    . ILE C  1 152 ? -0.445  72.981  182.356 1.00 55.90  ? 152 ILE C CB    1 
ATOM   8875  C CG1   . ILE C  1 152 ? -0.484  71.995  181.186 1.00 52.79  ? 152 ILE C CG1   1 
ATOM   8876  C CG2   . ILE C  1 152 ? 0.769   73.883  182.238 1.00 52.49  ? 152 ILE C CG2   1 
ATOM   8877  C CD1   . ILE C  1 152 ? -0.650  72.659  179.837 1.00 47.37  ? 152 ILE C CD1   1 
ATOM   8878  N N     . THR C  1 153 ? -1.292  73.950  185.164 1.00 56.82  ? 153 THR C N     1 
ATOM   8879  C CA    . THR C  1 153 ? -1.255  74.924  186.256 1.00 56.01  ? 153 THR C CA    1 
ATOM   8880  C C     . THR C  1 153 ? -0.835  74.274  187.572 1.00 63.00  ? 153 THR C C     1 
ATOM   8881  O O     . THR C  1 153 ? -0.128  74.879  188.378 1.00 67.95  ? 153 THR C O     1 
ATOM   8882  C CB    . THR C  1 153 ? -2.617  75.605  186.459 1.00 59.26  ? 153 THR C CB    1 
ATOM   8883  O OG1   . THR C  1 153 ? -3.571  74.640  186.910 1.00 65.06  ? 153 THR C OG1   1 
ATOM   8884  C CG2   . THR C  1 153 ? -3.106  76.231  185.161 1.00 57.29  ? 153 THR C CG2   1 
ATOM   8885  N N     . GLU C  1 154 ? -1.279  73.036  187.773 1.00 60.27  ? 154 GLU C N     1 
ATOM   8886  C CA    . GLU C  1 154 ? -1.005  72.281  188.995 1.00 61.86  ? 154 GLU C CA    1 
ATOM   8887  C C     . GLU C  1 154 ? 0.442   71.788  189.096 1.00 63.14  ? 154 GLU C C     1 
ATOM   8888  O O     . GLU C  1 154 ? 0.826   71.194  190.105 1.00 69.32  ? 154 GLU C O     1 
ATOM   8889  C CB    . GLU C  1 154 ? -1.963  71.086  189.100 1.00 64.12  ? 154 GLU C CB    1 
ATOM   8890  C CG    . GLU C  1 154 ? -3.373  71.424  189.579 1.00 69.60  ? 154 GLU C CG    1 
ATOM   8891  C CD    . GLU C  1 154 ? -3.429  71.821  191.047 1.00 73.97  ? 154 GLU C CD    1 
ATOM   8892  O OE1   . GLU C  1 154 ? -2.772  71.152  191.876 1.00 78.71  ? 154 GLU C OE1   1 
ATOM   8893  O OE2   . GLU C  1 154 ? -4.136  72.799  191.371 1.00 74.60  ? 154 GLU C OE2   1 
ATOM   8894  N N     . SER C  1 155 ? 1.239   72.027  188.057 1.00 58.15  ? 155 SER C N     1 
ATOM   8895  C CA    . SER C  1 155 ? 2.639   71.593  188.046 1.00 63.15  ? 155 SER C CA    1 
ATOM   8896  C C     . SER C  1 155 ? 3.623   72.739  187.767 1.00 62.86  ? 155 SER C C     1 
ATOM   8897  O O     . SER C  1 155 ? 4.814   72.631  188.072 1.00 60.74  ? 155 SER C O     1 
ATOM   8898  C CB    . SER C  1 155 ? 2.846   70.486  187.005 1.00 60.69  ? 155 SER C CB    1 
ATOM   8899  O OG    . SER C  1 155 ? 3.093   71.031  185.720 1.00 64.10  ? 155 SER C OG    1 
ATOM   8900  N N     . SER C  1 156 ? 3.123   73.826  187.181 1.00 63.30  ? 156 SER C N     1 
ATOM   8901  C CA    . SER C  1 156 ? 3.950   74.995  186.868 1.00 58.59  ? 156 SER C CA    1 
ATOM   8902  C C     . SER C  1 156 ? 3.108   76.257  186.642 1.00 61.22  ? 156 SER C C     1 
ATOM   8903  O O     . SER C  1 156 ? 1.947   76.179  186.235 1.00 59.11  ? 156 SER C O     1 
ATOM   8904  C CB    . SER C  1 156 ? 4.820   74.727  185.631 1.00 56.90  ? 156 SER C CB    1 
ATOM   8905  O OG    . SER C  1 156 ? 5.506   75.901  185.220 1.00 61.40  ? 156 SER C OG    1 
ATOM   8906  N N     . SER C  1 157 ? 3.709   77.416  186.908 1.00 62.15  ? 157 SER C N     1 
ATOM   8907  C CA    . SER C  1 157 ? 3.062   78.705  186.678 1.00 65.27  ? 157 SER C CA    1 
ATOM   8908  C C     . SER C  1 157 ? 3.723   79.448  185.515 1.00 63.86  ? 157 SER C C     1 
ATOM   8909  O O     . SER C  1 157 ? 3.259   80.515  185.104 1.00 65.54  ? 157 SER C O     1 
ATOM   8910  C CB    . SER C  1 157 ? 3.098   79.563  187.950 1.00 67.22  ? 157 SER C CB    1 
ATOM   8911  O OG    . SER C  1 157 ? 2.424   80.801  187.760 1.00 79.08  ? 157 SER C OG    1 
ATOM   8912  N N     . LYS C  1 158 ? 4.802   78.876  184.983 1.00 64.08  ? 158 LYS C N     1 
ATOM   8913  C CA    . LYS C  1 158 ? 5.520   79.482  183.865 1.00 65.76  ? 158 LYS C CA    1 
ATOM   8914  C C     . LYS C  1 158 ? 5.259   78.726  182.569 1.00 62.65  ? 158 LYS C C     1 
ATOM   8915  O O     . LYS C  1 158 ? 5.915   78.962  181.555 1.00 59.72  ? 158 LYS C O     1 
ATOM   8916  C CB    . LYS C  1 158 ? 7.023   79.516  184.149 1.00 67.19  ? 158 LYS C CB    1 
ATOM   8917  C CG    . LYS C  1 158 ? 7.362   79.432  185.623 1.00 69.66  ? 158 LYS C CG    1 
ATOM   8918  C CD    . LYS C  1 158 ? 8.796   79.846  185.902 1.00 86.74  ? 158 LYS C CD    1 
ATOM   8919  C CE    . LYS C  1 158 ? 9.019   81.316  185.585 1.00 98.66  ? 158 LYS C CE    1 
ATOM   8920  N NZ    . LYS C  1 158 ? 10.359  81.768  186.049 1.00 101.89 ? 158 LYS C NZ    1 
ATOM   8921  N N     . LEU C  1 159 ? 4.295   77.815  182.611 1.00 63.71  ? 159 LEU C N     1 
ATOM   8922  C CA    . LEU C  1 159 ? 3.996   76.971  181.464 1.00 58.83  ? 159 LEU C CA    1 
ATOM   8923  C C     . LEU C  1 159 ? 2.509   76.960  181.135 1.00 59.02  ? 159 LEU C C     1 
ATOM   8924  O O     . LEU C  1 159 ? 1.657   76.996  182.024 1.00 57.73  ? 159 LEU C O     1 
ATOM   8925  C CB    . LEU C  1 159 ? 4.491   75.545  181.713 1.00 52.92  ? 159 LEU C CB    1 
ATOM   8926  C CG    . LEU C  1 159 ? 6.010   75.369  181.778 1.00 55.72  ? 159 LEU C CG    1 
ATOM   8927  C CD1   . LEU C  1 159 ? 6.367   73.953  182.190 1.00 54.65  ? 159 LEU C CD1   1 
ATOM   8928  C CD2   . LEU C  1 159 ? 6.644   75.718  180.440 1.00 53.09  ? 159 LEU C CD2   1 
ATOM   8929  N N     . GLY C  1 160 ? 2.212   76.918  179.841 1.00 56.68  ? 160 GLY C N     1 
ATOM   8930  C CA    . GLY C  1 160 ? 0.851   76.793  179.360 1.00 54.44  ? 160 GLY C CA    1 
ATOM   8931  C C     . GLY C  1 160 ? 0.839   76.041  178.045 1.00 55.40  ? 160 GLY C C     1 
ATOM   8932  O O     . GLY C  1 160 ? 1.829   75.411  177.675 1.00 50.18  ? 160 GLY C O     1 
ATOM   8933  N N     . PHE C  1 161 ? -0.282  76.105  177.336 1.00 50.67  ? 161 PHE C N     1 
ATOM   8934  C CA    . PHE C  1 161 ? -0.391  75.472  176.027 1.00 51.37  ? 161 PHE C CA    1 
ATOM   8935  C C     . PHE C  1 161 ? -1.399  76.216  175.162 1.00 47.09  ? 161 PHE C C     1 
ATOM   8936  O O     . PHE C  1 161 ? -2.365  76.782  175.673 1.00 53.57  ? 161 PHE C O     1 
ATOM   8937  C CB    . PHE C  1 161 ? -0.784  74.000  176.167 1.00 49.53  ? 161 PHE C CB    1 
ATOM   8938  C CG    . PHE C  1 161 ? -0.696  73.225  174.883 1.00 49.27  ? 161 PHE C CG    1 
ATOM   8939  C CD1   . PHE C  1 161 ? 0.534   72.952  174.307 1.00 42.07  ? 161 PHE C CD1   1 
ATOM   8940  C CD2   . PHE C  1 161 ? -1.842  72.761  174.258 1.00 45.37  ? 161 PHE C CD2   1 
ATOM   8941  C CE1   . PHE C  1 161 ? 0.620   72.239  173.126 1.00 43.69  ? 161 PHE C CE1   1 
ATOM   8942  C CE2   . PHE C  1 161 ? -1.761  72.044  173.077 1.00 44.69  ? 161 PHE C CE2   1 
ATOM   8943  C CZ    . PHE C  1 161 ? -0.528  71.784  172.512 1.00 43.33  ? 161 PHE C CZ    1 
ATOM   8944  N N     . THR C  1 162 ? -1.171  76.221  173.853 1.00 47.55  ? 162 THR C N     1 
ATOM   8945  C CA    . THR C  1 162 ? -2.049  76.954  172.950 1.00 48.96  ? 162 THR C CA    1 
ATOM   8946  C C     . THR C  1 162 ? -3.134  76.056  172.362 1.00 52.21  ? 162 THR C C     1 
ATOM   8947  O O     . THR C  1 162 ? -2.849  75.074  171.677 1.00 51.53  ? 162 THR C O     1 
ATOM   8948  C CB    . THR C  1 162 ? -1.257  77.631  171.804 1.00 48.60  ? 162 THR C CB    1 
ATOM   8949  O OG1   . THR C  1 162 ? -2.169  78.139  170.822 1.00 50.69  ? 162 THR C OG1   1 
ATOM   8950  C CG2   . THR C  1 162 ? -0.294  76.654  171.142 1.00 47.87  ? 162 THR C CG2   1 
ATOM   8951  N N     . ALA C  1 163 ? -4.382  76.404  172.658 1.00 51.67  ? 163 ALA C N     1 
ATOM   8952  C CA    . ALA C  1 163 ? -5.543  75.742  172.080 1.00 52.60  ? 163 ALA C CA    1 
ATOM   8953  C C     . ALA C  1 163 ? -6.802  76.556  172.368 1.00 55.54  ? 163 ALA C C     1 
ATOM   8954  O O     . ALA C  1 163 ? -6.724  77.678  172.876 1.00 52.69  ? 163 ALA C O     1 
ATOM   8955  C CB    . ALA C  1 163 ? -5.683  74.317  172.613 1.00 46.70  ? 163 ALA C CB    1 
ATOM   8956  N N     . ALA C  1 164 ? -7.956  75.977  172.044 1.00 51.20  ? 164 ALA C N     1 
ATOM   8957  C CA    . ALA C  1 164 ? -9.252  76.647  172.163 1.00 51.80  ? 164 ALA C CA    1 
ATOM   8958  C C     . ALA C  1 164 ? -9.561  77.114  173.581 1.00 54.63  ? 164 ALA C C     1 
ATOM   8959  O O     . ALA C  1 164 ? -8.961  76.649  174.550 1.00 54.52  ? 164 ALA C O     1 
ATOM   8960  C CB    . ALA C  1 164 ? -10.356 75.722  171.679 1.00 52.29  ? 164 ALA C CB    1 
ATOM   8961  N N     . TRP C  1 165 ? -10.509 78.040  173.688 1.00 53.65  ? 165 TRP C N     1 
ATOM   8962  C CA    . TRP C  1 165 ? -10.952 78.529  174.985 1.00 54.83  ? 165 TRP C CA    1 
ATOM   8963  C C     . TRP C  1 165 ? -11.952 77.564  175.617 1.00 56.44  ? 165 TRP C C     1 
ATOM   8964  O O     . TRP C  1 165 ? -12.021 77.452  176.839 1.00 56.73  ? 165 TRP C O     1 
ATOM   8965  C CB    . TRP C  1 165 ? -11.570 79.924  174.858 1.00 56.34  ? 165 TRP C CB    1 
ATOM   8966  C CG    . TRP C  1 165 ? -12.855 79.967  174.072 1.00 63.60  ? 165 TRP C CG    1 
ATOM   8967  C CD1   . TRP C  1 165 ? -12.991 80.212  172.736 1.00 64.49  ? 165 TRP C CD1   1 
ATOM   8968  C CD2   . TRP C  1 165 ? -14.184 79.769  174.580 1.00 66.12  ? 165 TRP C CD2   1 
ATOM   8969  N NE1   . TRP C  1 165 ? -14.318 80.174  172.379 1.00 71.59  ? 165 TRP C NE1   1 
ATOM   8970  C CE2   . TRP C  1 165 ? -15.071 79.905  173.492 1.00 69.04  ? 165 TRP C CE2   1 
ATOM   8971  C CE3   . TRP C  1 165 ? -14.708 79.488  175.846 1.00 66.93  ? 165 TRP C CE3   1 
ATOM   8972  C CZ2   . TRP C  1 165 ? -16.452 79.769  173.631 1.00 66.11  ? 165 TRP C CZ2   1 
ATOM   8973  C CZ3   . TRP C  1 165 ? -16.082 79.353  175.983 1.00 67.47  ? 165 TRP C CZ3   1 
ATOM   8974  C CH2   . TRP C  1 165 ? -16.937 79.494  174.880 1.00 65.42  ? 165 TRP C CH2   1 
ATOM   8975  N N     . CYS C  1 166 ? -12.724 76.876  174.777 1.00 57.60  ? 166 CYS C N     1 
ATOM   8976  C CA    . CYS C  1 166 ? -13.719 75.906  175.238 1.00 48.96  ? 166 CYS C CA    1 
ATOM   8977  C C     . CYS C  1 166 ? -13.058 74.749  175.978 1.00 48.23  ? 166 CYS C C     1 
ATOM   8978  O O     . CYS C  1 166 ? -12.375 73.932  175.363 1.00 47.49  ? 166 CYS C O     1 
ATOM   8979  C CB    . CYS C  1 166 ? -14.526 75.356  174.061 1.00 52.25  ? 166 CYS C CB    1 
ATOM   8980  S SG    . CYS C  1 166 ? -15.248 76.581  172.946 1.00 54.42  ? 166 CYS C SG    1 
ATOM   8981  N N     . PRO C  1 167 ? -13.269 74.663  177.299 1.00 50.30  ? 167 PRO C N     1 
ATOM   8982  C CA    . PRO C  1 167 ? -12.542 73.654  178.079 1.00 43.34  ? 167 PRO C CA    1 
ATOM   8983  C C     . PRO C  1 167 ? -13.131 72.241  178.042 1.00 47.32  ? 167 PRO C C     1 
ATOM   8984  O O     . PRO C  1 167 ? -12.505 71.334  178.588 1.00 45.75  ? 167 PRO C O     1 
ATOM   8985  C CB    . PRO C  1 167 ? -12.600 74.216  179.501 1.00 45.74  ? 167 PRO C CB    1 
ATOM   8986  C CG    . PRO C  1 167 ? -13.866 74.993  179.540 1.00 50.55  ? 167 PRO C CG    1 
ATOM   8987  C CD    . PRO C  1 167 ? -14.075 75.555  178.155 1.00 46.11  ? 167 PRO C CD    1 
ATOM   8988  N N     . THR C  1 168 ? -14.295 72.049  177.426 1.00 47.70  ? 168 THR C N     1 
ATOM   8989  C CA    . THR C  1 168 ? -14.862 70.705  177.317 1.00 45.30  ? 168 THR C CA    1 
ATOM   8990  C C     . THR C  1 168 ? -14.544 70.071  175.967 1.00 44.42  ? 168 THR C C     1 
ATOM   8991  O O     . THR C  1 168 ? -14.913 68.926  175.705 1.00 43.08  ? 168 THR C O     1 
ATOM   8992  C CB    . THR C  1 168 ? -16.391 70.697  177.520 1.00 44.61  ? 168 THR C CB    1 
ATOM   8993  O OG1   . THR C  1 168 ? -17.019 71.507  176.518 1.00 43.42  ? 168 THR C OG1   1 
ATOM   8994  C CG2   . THR C  1 168 ? -16.749 71.223  178.897 1.00 53.02  ? 168 THR C CG2   1 
ATOM   8995  N N     . VAL C  1 169 ? -13.872 70.827  175.107 1.00 43.76  ? 169 VAL C N     1 
ATOM   8996  C CA    . VAL C  1 169 ? -13.372 70.294  173.847 1.00 40.33  ? 169 VAL C CA    1 
ATOM   8997  C C     . VAL C  1 169 ? -12.315 69.230  174.131 1.00 40.63  ? 169 VAL C C     1 
ATOM   8998  O O     . VAL C  1 169 ? -11.448 69.430  174.979 1.00 41.51  ? 169 VAL C O     1 
ATOM   8999  C CB    . VAL C  1 169 ? -12.778 71.409  172.960 1.00 43.94  ? 169 VAL C CB    1 
ATOM   9000  C CG1   . VAL C  1 169 ? -11.917 70.826  171.857 1.00 41.59  ? 169 VAL C CG1   1 
ATOM   9001  C CG2   . VAL C  1 169 ? -13.887 72.276  172.384 1.00 44.42  ? 169 VAL C CG2   1 
ATOM   9002  N N     . GLY C  1 170 ? -12.399 68.098  173.438 1.00 43.07  ? 170 GLY C N     1 
ATOM   9003  C CA    . GLY C  1 170 ? -11.458 67.010  173.641 1.00 39.87  ? 170 GLY C CA    1 
ATOM   9004  C C     . GLY C  1 170 ? -10.201 67.140  172.800 1.00 36.45  ? 170 GLY C C     1 
ATOM   9005  O O     . GLY C  1 170 ? -10.262 67.583  171.654 1.00 36.43  ? 170 GLY C O     1 
ATOM   9006  N N     . THR C  1 171 ? -9.063  66.747  173.367 1.00 36.93  ? 171 THR C N     1 
ATOM   9007  C CA    . THR C  1 171 ? -7.787  66.807  172.660 1.00 38.04  ? 171 THR C CA    1 
ATOM   9008  C C     . THR C  1 171 ? -7.771  65.901  171.432 1.00 32.31  ? 171 THR C C     1 
ATOM   9009  O O     . THR C  1 171 ? -7.093  66.192  170.442 1.00 38.17  ? 171 THR C O     1 
ATOM   9010  C CB    . THR C  1 171 ? -6.610  66.407  173.579 1.00 39.24  ? 171 THR C CB    1 
ATOM   9011  O OG1   . THR C  1 171 ? -6.890  65.141  174.194 1.00 38.44  ? 171 THR C OG1   1 
ATOM   9012  C CG2   . THR C  1 171 ? -6.399  67.453  174.659 1.00 37.18  ? 171 THR C CG2   1 
ATOM   9013  N N     . GLY C  1 172 ? -8.528  64.809  171.506 1.00 36.80  ? 172 GLY C N     1 
ATOM   9014  C CA    . GLY C  1 172 ? -8.583  63.831  170.434 1.00 34.83  ? 172 GLY C CA    1 
ATOM   9015  C C     . GLY C  1 172 ? -8.975  64.416  169.092 1.00 32.27  ? 172 GLY C C     1 
ATOM   9016  O O     . GLY C  1 172 ? -8.273  64.227  168.102 1.00 34.84  ? 172 GLY C O     1 
ATOM   9017  N N     . GLY C  1 173 ? -10.094 65.131  169.059 1.00 40.20  ? 173 GLY C N     1 
ATOM   9018  C CA    . GLY C  1 173 ? -10.545 65.769  167.837 1.00 35.90  ? 173 GLY C CA    1 
ATOM   9019  C C     . GLY C  1 173 ? -9.904  67.123  167.593 1.00 31.48  ? 173 GLY C C     1 
ATOM   9020  O O     . GLY C  1 173 ? -9.595  67.472  166.452 1.00 37.83  ? 173 GLY C O     1 
ATOM   9021  N N     . HIS C  1 174 ? -9.697  67.883  168.666 1.00 32.58  ? 174 HIS C N     1 
ATOM   9022  C CA    . HIS C  1 174 ? -9.177  69.249  168.574 1.00 38.64  ? 174 HIS C CA    1 
ATOM   9023  C C     . HIS C  1 174 ? -7.782  69.333  167.966 1.00 32.61  ? 174 HIS C C     1 
ATOM   9024  O O     . HIS C  1 174 ? -7.549  70.074  167.009 1.00 34.12  ? 174 HIS C O     1 
ATOM   9025  C CB    . HIS C  1 174 ? -9.152  69.892  169.961 1.00 36.52  ? 174 HIS C CB    1 
ATOM   9026  C CG    . HIS C  1 174 ? -8.867  71.359  169.943 1.00 41.04  ? 174 HIS C CG    1 
ATOM   9027  N ND1   . HIS C  1 174 ? -9.669  72.262  169.281 1.00 38.87  ? 174 HIS C ND1   1 
ATOM   9028  C CD2   . HIS C  1 174 ? -7.868  72.083  170.505 1.00 42.31  ? 174 HIS C CD2   1 
ATOM   9029  C CE1   . HIS C  1 174 ? -9.180  73.479  169.438 1.00 41.20  ? 174 HIS C CE1   1 
ATOM   9030  N NE2   . HIS C  1 174 ? -8.089  73.397  170.178 1.00 37.89  ? 174 HIS C NE2   1 
ATOM   9031  N N     . ILE C  1 175 ? -6.851  68.584  168.544 1.00 37.85  ? 175 ILE C N     1 
ATOM   9032  C CA    . ILE C  1 175 ? -5.466  68.608  168.092 1.00 35.24  ? 175 ILE C CA    1 
ATOM   9033  C C     . ILE C  1 175 ? -5.368  67.930  166.724 1.00 32.27  ? 175 ILE C C     1 
ATOM   9034  O O     . ILE C  1 175 ? -4.555  68.319  165.884 1.00 34.56  ? 175 ILE C O     1 
ATOM   9035  C CB    . ILE C  1 175 ? -4.528  67.927  169.112 1.00 29.85  ? 175 ILE C CB    1 
ATOM   9036  C CG1   . ILE C  1 175 ? -4.584  68.659  170.463 1.00 29.48  ? 175 ILE C CG1   1 
ATOM   9037  C CG2   . ILE C  1 175 ? -3.100  67.895  168.605 1.00 36.85  ? 175 ILE C CG2   1 
ATOM   9038  C CD1   . ILE C  1 175 ? -3.578  68.148  171.480 1.00 39.19  ? 175 ILE C CD1   1 
ATOM   9039  N N     . SER C  1 176 ? -6.225  66.936  166.497 1.00 30.64  ? 176 SER C N     1 
ATOM   9040  C CA    . SER C  1 176 ? -6.301  66.252  165.207 1.00 30.44  ? 176 SER C CA    1 
ATOM   9041  C C     . SER C  1 176 ? -6.696  67.201  164.080 1.00 34.94  ? 176 SER C C     1 
ATOM   9042  O O     . SER C  1 176 ? -6.307  67.007  162.931 1.00 38.07  ? 176 SER C O     1 
ATOM   9043  C CB    . SER C  1 176 ? -7.301  65.093  165.261 1.00 33.57  ? 176 SER C CB    1 
ATOM   9044  O OG    . SER C  1 176 ? -6.840  64.033  166.079 1.00 34.67  ? 176 SER C OG    1 
ATOM   9045  N N     . GLY C  1 177 ? -7.483  68.218  164.410 1.00 37.09  ? 177 GLY C N     1 
ATOM   9046  C CA    . GLY C  1 177 ? -7.939  69.171  163.417 1.00 32.72  ? 177 GLY C CA    1 
ATOM   9047  C C     . GLY C  1 177 ? -7.120  70.448  163.388 1.00 36.91  ? 177 GLY C C     1 
ATOM   9048  O O     . GLY C  1 177 ? -7.366  71.335  162.572 1.00 37.26  ? 177 GLY C O     1 
ATOM   9049  N N     . GLY C  1 178 ? -6.139  70.537  164.279 1.00 34.85  ? 178 GLY C N     1 
ATOM   9050  C CA    . GLY C  1 178 ? -5.308  71.723  164.383 1.00 32.94  ? 178 GLY C CA    1 
ATOM   9051  C C     . GLY C  1 178 ? -5.375  72.342  165.766 1.00 36.66  ? 178 GLY C C     1 
ATOM   9052  O O     . GLY C  1 178 ? -4.523  72.080  166.616 1.00 36.09  ? 178 GLY C O     1 
ATOM   9053  N N     . GLY C  1 179 ? -6.390  73.171  165.990 1.00 34.35  ? 179 GLY C N     1 
ATOM   9054  C CA    . GLY C  1 179 ? -6.604  73.777  167.291 1.00 38.12  ? 179 GLY C CA    1 
ATOM   9055  C C     . GLY C  1 179 ? -6.143  75.218  167.380 1.00 40.90  ? 179 GLY C C     1 
ATOM   9056  O O     . GLY C  1 179 ? -4.967  75.488  167.611 1.00 40.46  ? 179 GLY C O     1 
ATOM   9057  N N     . PHE C  1 180 ? -7.077  76.146  167.208 1.00 43.94  ? 180 PHE C N     1 
ATOM   9058  C CA    . PHE C  1 180 ? -6.752  77.568  167.217 1.00 39.16  ? 180 PHE C CA    1 
ATOM   9059  C C     . PHE C  1 180 ? -7.253  78.242  168.493 1.00 49.80  ? 180 PHE C C     1 
ATOM   9060  O O     . PHE C  1 180 ? -8.345  77.942  168.979 1.00 46.10  ? 180 PHE C O     1 
ATOM   9061  C CB    . PHE C  1 180 ? -7.344  78.246  165.977 1.00 41.62  ? 180 PHE C CB    1 
ATOM   9062  C CG    . PHE C  1 180 ? -7.051  79.716  165.883 1.00 51.63  ? 180 PHE C CG    1 
ATOM   9063  C CD1   . PHE C  1 180 ? -5.886  80.171  165.285 1.00 44.33  ? 180 PHE C CD1   1 
ATOM   9064  C CD2   . PHE C  1 180 ? -7.951  80.646  166.374 1.00 47.40  ? 180 PHE C CD2   1 
ATOM   9065  C CE1   . PHE C  1 180 ? -5.621  81.527  165.193 1.00 47.59  ? 180 PHE C CE1   1 
ATOM   9066  C CE2   . PHE C  1 180 ? -7.691  82.000  166.286 1.00 47.04  ? 180 PHE C CE2   1 
ATOM   9067  C CZ    . PHE C  1 180 ? -6.525  82.441  165.695 1.00 52.27  ? 180 PHE C CZ    1 
ATOM   9068  N N     . GLY C  1 181 ? -6.445  79.150  169.034 1.00 48.86  ? 181 GLY C N     1 
ATOM   9069  C CA    . GLY C  1 181 ? -6.796  79.847  170.258 1.00 50.08  ? 181 GLY C CA    1 
ATOM   9070  C C     . GLY C  1 181 ? -6.204  81.242  170.367 1.00 50.53  ? 181 GLY C C     1 
ATOM   9071  O O     . GLY C  1 181 ? -5.618  81.757  169.415 1.00 47.56  ? 181 GLY C O     1 
ATOM   9072  N N     . MET C  1 182 ? -6.352  81.844  171.546 1.00 54.21  ? 182 MET C N     1 
ATOM   9073  C CA    . MET C  1 182 ? -5.893  83.207  171.803 1.00 57.53  ? 182 MET C CA    1 
ATOM   9074  C C     . MET C  1 182 ? -4.370  83.344  171.751 1.00 54.54  ? 182 MET C C     1 
ATOM   9075  O O     . MET C  1 182 ? -3.844  84.455  171.702 1.00 53.73  ? 182 MET C O     1 
ATOM   9076  C CB    . MET C  1 182 ? -6.402  83.686  173.166 1.00 55.67  ? 182 MET C CB    1 
ATOM   9077  C CG    . MET C  1 182 ? -7.916  83.736  173.293 1.00 61.85  ? 182 MET C CG    1 
ATOM   9078  S SD    . MET C  1 182 ? -8.628  85.225  172.574 1.00 66.08  ? 182 MET C SD    1 
ATOM   9079  C CE    . MET C  1 182 ? -8.008  86.474  173.699 1.00 55.81  ? 182 MET C CE    1 
ATOM   9080  N N     . MET C  1 183 ? -3.668  82.214  171.764 1.00 50.47  ? 183 MET C N     1 
ATOM   9081  C CA    . MET C  1 183 ? -2.208  82.216  171.759 1.00 49.66  ? 183 MET C CA    1 
ATOM   9082  C C     . MET C  1 183 ? -1.604  81.794  170.432 1.00 48.42  ? 183 MET C C     1 
ATOM   9083  O O     . MET C  1 183 ? -0.381  81.730  170.299 1.00 43.47  ? 183 MET C O     1 
ATOM   9084  C CB    . MET C  1 183 ? -1.671  81.293  172.844 1.00 49.13  ? 183 MET C CB    1 
ATOM   9085  C CG    . MET C  1 183 ? -2.175  81.632  174.210 1.00 45.94  ? 183 MET C CG    1 
ATOM   9086  S SD    . MET C  1 183 ? -1.208  80.829  175.492 1.00 60.24  ? 183 MET C SD    1 
ATOM   9087  C CE    . MET C  1 183 ? -1.520  81.963  176.826 1.00 57.93  ? 183 MET C CE    1 
ATOM   9088  N N     . SER C  1 184 ? -2.451  81.492  169.457 1.00 44.03  ? 184 SER C N     1 
ATOM   9089  C CA    . SER C  1 184 ? -1.957  80.987  168.184 1.00 48.93  ? 184 SER C CA    1 
ATOM   9090  C C     . SER C  1 184 ? -1.142  82.047  167.447 1.00 47.04  ? 184 SER C C     1 
ATOM   9091  O O     . SER C  1 184 ? -0.277  81.718  166.637 1.00 45.40  ? 184 SER C O     1 
ATOM   9092  C CB    . SER C  1 184 ? -3.114  80.495  167.318 1.00 44.24  ? 184 SER C CB    1 
ATOM   9093  O OG    . SER C  1 184 ? -3.781  79.414  167.942 1.00 44.73  ? 184 SER C OG    1 
ATOM   9094  N N     . ARG C  1 185 ? -1.414  83.317  167.737 1.00 47.63  ? 185 ARG C N     1 
ATOM   9095  C CA    . ARG C  1 185 ? -0.625  84.409  167.178 1.00 47.49  ? 185 ARG C CA    1 
ATOM   9096  C C     . ARG C  1 185 ? 0.786   84.380  167.752 1.00 45.01  ? 185 ARG C C     1 
ATOM   9097  O O     . ARG C  1 185 ? 1.722   84.911  167.157 1.00 41.35  ? 185 ARG C O     1 
ATOM   9098  C CB    . ARG C  1 185 ? -1.281  85.765  167.456 1.00 43.43  ? 185 ARG C CB    1 
ATOM   9099  C CG    . ARG C  1 185 ? -2.716  85.869  166.972 1.00 47.93  ? 185 ARG C CG    1 
ATOM   9100  C CD    . ARG C  1 185 ? -3.222  87.305  166.970 1.00 50.65  ? 185 ARG C CD    1 
ATOM   9101  N NE    . ARG C  1 185 ? -2.581  88.122  165.941 1.00 54.45  ? 185 ARG C NE    1 
ATOM   9102  C CZ    . ARG C  1 185 ? -1.596  88.984  166.175 1.00 49.73  ? 185 ARG C CZ    1 
ATOM   9103  N NH1   . ARG C  1 185 ? -1.135  89.151  167.408 1.00 50.83  ? 185 ARG C NH1   1 
ATOM   9104  N NH2   . ARG C  1 185 ? -1.073  89.682  165.177 1.00 55.79  ? 185 ARG C NH2   1 
ATOM   9105  N N     . LYS C  1 186 ? 0.924   83.750  168.914 1.00 47.40  ? 186 LYS C N     1 
ATOM   9106  C CA    . LYS C  1 186 ? 2.213   83.610  169.581 1.00 51.21  ? 186 LYS C CA    1 
ATOM   9107  C C     . LYS C  1 186 ? 2.861   82.256  169.291 1.00 47.59  ? 186 LYS C C     1 
ATOM   9108  O O     . LYS C  1 186 ? 4.050   82.187  168.976 1.00 49.54  ? 186 LYS C O     1 
ATOM   9109  C CB    . LYS C  1 186 ? 2.049   83.796  171.091 1.00 51.58  ? 186 LYS C CB    1 
ATOM   9110  C CG    . LYS C  1 186 ? 3.299   83.504  171.913 1.00 53.61  ? 186 LYS C CG    1 
ATOM   9111  C CD    . LYS C  1 186 ? 4.262   84.681  171.949 1.00 50.03  ? 186 LYS C CD    1 
ATOM   9112  C CE    . LYS C  1 186 ? 5.309   84.490  173.040 1.00 48.55  ? 186 LYS C CE    1 
ATOM   9113  N NZ    . LYS C  1 186 ? 6.387   85.518  172.990 1.00 56.35  ? 186 LYS C NZ    1 
ATOM   9114  N N     . TYR C  1 187 ? 2.080   81.182  169.386 1.00 47.89  ? 187 TYR C N     1 
ATOM   9115  C CA    . TYR C  1 187 ? 2.637   79.832  169.315 1.00 45.73  ? 187 TYR C CA    1 
ATOM   9116  C C     . TYR C  1 187 ? 2.047   78.926  168.232 1.00 42.61  ? 187 TYR C C     1 
ATOM   9117  O O     . TYR C  1 187 ? 2.348   77.732  168.198 1.00 46.75  ? 187 TYR C O     1 
ATOM   9118  C CB    . TYR C  1 187 ? 2.468   79.131  170.665 1.00 45.06  ? 187 TYR C CB    1 
ATOM   9119  C CG    . TYR C  1 187 ? 3.305   79.700  171.786 1.00 50.72  ? 187 TYR C CG    1 
ATOM   9120  C CD1   . TYR C  1 187 ? 4.692   79.707  171.710 1.00 47.29  ? 187 TYR C CD1   1 
ATOM   9121  C CD2   . TYR C  1 187 ? 2.709   80.206  172.934 1.00 47.60  ? 187 TYR C CD2   1 
ATOM   9122  C CE1   . TYR C  1 187 ? 5.462   80.217  172.740 1.00 47.57  ? 187 TYR C CE1   1 
ATOM   9123  C CE2   . TYR C  1 187 ? 3.471   80.717  173.970 1.00 49.88  ? 187 TYR C CE2   1 
ATOM   9124  C CZ    . TYR C  1 187 ? 4.846   80.722  173.866 1.00 51.12  ? 187 TYR C CZ    1 
ATOM   9125  O OH    . TYR C  1 187 ? 5.607   81.230  174.896 1.00 49.91  ? 187 TYR C OH    1 
ATOM   9126  N N     . GLY C  1 188 ? 1.213   79.472  167.354 1.00 37.57  ? 188 GLY C N     1 
ATOM   9127  C CA    . GLY C  1 188 ? 0.564   78.660  166.338 1.00 45.44  ? 188 GLY C CA    1 
ATOM   9128  C C     . GLY C  1 188 ? -0.504  77.751  166.927 1.00 42.83  ? 188 GLY C C     1 
ATOM   9129  O O     . GLY C  1 188 ? -0.949  77.959  168.055 1.00 42.15  ? 188 GLY C O     1 
ATOM   9130  N N     . LEU C  1 189 ? -0.907  76.734  166.170 1.00 41.28  ? 189 LEU C N     1 
ATOM   9131  C CA    . LEU C  1 189 ? -1.975  75.831  166.600 1.00 41.84  ? 189 LEU C CA    1 
ATOM   9132  C C     . LEU C  1 189 ? -1.495  74.825  167.641 1.00 37.17  ? 189 LEU C C     1 
ATOM   9133  O O     . LEU C  1 189 ? -0.296  74.676  167.864 1.00 40.36  ? 189 LEU C O     1 
ATOM   9134  C CB    . LEU C  1 189 ? -2.560  75.082  165.402 1.00 33.88  ? 189 LEU C CB    1 
ATOM   9135  C CG    . LEU C  1 189 ? -3.028  75.927  164.217 1.00 42.15  ? 189 LEU C CG    1 
ATOM   9136  C CD1   . LEU C  1 189 ? -3.382  75.027  163.059 1.00 35.38  ? 189 LEU C CD1   1 
ATOM   9137  C CD2   . LEU C  1 189 ? -4.215  76.806  164.599 1.00 37.81  ? 189 LEU C CD2   1 
ATOM   9138  N N     . ALA C  1 190 ? -2.443  74.139  168.270 1.00 36.23  ? 190 ALA C N     1 
ATOM   9139  C CA    . ALA C  1 190 ? -2.127  73.070  169.208 1.00 39.31  ? 190 ALA C CA    1 
ATOM   9140  C C     . ALA C  1 190 ? -1.324  71.977  168.512 1.00 37.94  ? 190 ALA C C     1 
ATOM   9141  O O     . ALA C  1 190 ? -0.349  71.453  169.060 1.00 35.58  ? 190 ALA C O     1 
ATOM   9142  C CB    . ALA C  1 190 ? -3.406  72.497  169.809 1.00 38.96  ? 190 ALA C CB    1 
ATOM   9143  N N     . ALA C  1 191 ? -1.736  71.654  167.290 1.00 35.24  ? 191 ALA C N     1 
ATOM   9144  C CA    . ALA C  1 191 ? -1.077  70.625  166.498 1.00 36.09  ? 191 ALA C CA    1 
ATOM   9145  C C     . ALA C  1 191 ? 0.319   71.059  166.065 1.00 37.08  ? 191 ALA C C     1 
ATOM   9146  O O     . ALA C  1 191 ? 1.161   70.217  165.755 1.00 35.24  ? 191 ALA C O     1 
ATOM   9147  C CB    . ALA C  1 191 ? -1.921  70.274  165.287 1.00 32.57  ? 191 ALA C CB    1 
ATOM   9148  N N     . ASP C  1 192 ? 0.563   72.367  166.051 1.00 39.39  ? 192 ASP C N     1 
ATOM   9149  C CA    . ASP C  1 192 ? 1.875   72.898  165.686 1.00 37.53  ? 192 ASP C CA    1 
ATOM   9150  C C     . ASP C  1 192 ? 2.914   72.629  166.765 1.00 36.67  ? 192 ASP C C     1 
ATOM   9151  O O     . ASP C  1 192 ? 4.108   72.832  166.548 1.00 38.69  ? 192 ASP C O     1 
ATOM   9152  C CB    . ASP C  1 192 ? 1.801   74.406  165.419 1.00 37.89  ? 192 ASP C CB    1 
ATOM   9153  C CG    . ASP C  1 192 ? 1.041   74.739  164.159 1.00 41.73  ? 192 ASP C CG    1 
ATOM   9154  O OD1   . ASP C  1 192 ? 0.959   73.868  163.270 1.00 43.69  ? 192 ASP C OD1   1 
ATOM   9155  O OD2   . ASP C  1 192 ? 0.526   75.873  164.053 1.00 46.62  ? 192 ASP C OD2   1 
ATOM   9156  N N     . ASN C  1 193 ? 2.456   72.175  167.927 1.00 37.12  ? 193 ASN C N     1 
ATOM   9157  C CA    . ASN C  1 193 ? 3.343   71.948  169.059 1.00 35.57  ? 193 ASN C CA    1 
ATOM   9158  C C     . ASN C  1 193 ? 3.328   70.497  169.529 1.00 36.66  ? 193 ASN C C     1 
ATOM   9159  O O     . ASN C  1 193 ? 3.635   70.199  170.683 1.00 38.63  ? 193 ASN C O     1 
ATOM   9160  C CB    . ASN C  1 193 ? 2.973   72.886  170.211 1.00 39.56  ? 193 ASN C CB    1 
ATOM   9161  C CG    . ASN C  1 193 ? 3.216   74.346  169.870 1.00 41.86  ? 193 ASN C CG    1 
ATOM   9162  O OD1   . ASN C  1 193 ? 4.328   74.853  170.017 1.00 44.26  ? 193 ASN C OD1   1 
ATOM   9163  N ND2   . ASN C  1 193 ? 2.177   75.026  169.403 1.00 43.00  ? 193 ASN C ND2   1 
ATOM   9164  N N     . VAL C  1 194 ? 2.969   69.601  168.616 1.00 35.73  ? 194 VAL C N     1 
ATOM   9165  C CA    . VAL C  1 194 ? 3.031   68.169  168.866 1.00 37.14  ? 194 VAL C CA    1 
ATOM   9166  C C     . VAL C  1 194 ? 4.383   67.633  168.394 1.00 30.95  ? 194 VAL C C     1 
ATOM   9167  O O     . VAL C  1 194 ? 4.782   67.875  167.254 1.00 29.70  ? 194 VAL C O     1 
ATOM   9168  C CB    . VAL C  1 194 ? 1.887   67.421  168.150 1.00 32.11  ? 194 VAL C CB    1 
ATOM   9169  C CG1   . VAL C  1 194 ? 2.064   65.924  168.286 1.00 32.26  ? 194 VAL C CG1   1 
ATOM   9170  C CG2   . VAL C  1 194 ? 0.538   67.854  168.710 1.00 34.70  ? 194 VAL C CG2   1 
ATOM   9171  N N     . VAL C  1 195 ? 5.090   66.920  169.266 1.00 32.38  ? 195 VAL C N     1 
ATOM   9172  C CA    . VAL C  1 195 ? 6.424   66.423  168.928 1.00 35.27  ? 195 VAL C CA    1 
ATOM   9173  C C     . VAL C  1 195 ? 6.447   64.903  168.790 1.00 32.50  ? 195 VAL C C     1 
ATOM   9174  O O     . VAL C  1 195 ? 7.388   64.335  168.236 1.00 33.23  ? 195 VAL C O     1 
ATOM   9175  C CB    . VAL C  1 195 ? 7.459   66.850  169.978 1.00 34.90  ? 195 VAL C CB    1 
ATOM   9176  C CG1   . VAL C  1 195 ? 7.590   68.370  169.999 1.00 27.60  ? 195 VAL C CG1   1 
ATOM   9177  C CG2   . VAL C  1 195 ? 7.081   66.310  171.352 1.00 37.30  ? 195 VAL C CG2   1 
ATOM   9178  N N     . ASP C  1 196 ? 5.405   64.254  169.296 1.00 35.86  ? 196 ASP C N     1 
ATOM   9179  C CA    . ASP C  1 196 ? 5.243   62.813  169.139 1.00 34.47  ? 196 ASP C CA    1 
ATOM   9180  C C     . ASP C  1 196 ? 3.782   62.441  169.376 1.00 34.52  ? 196 ASP C C     1 
ATOM   9181  O O     . ASP C  1 196 ? 3.002   63.252  169.874 1.00 33.43  ? 196 ASP C O     1 
ATOM   9182  C CB    . ASP C  1 196 ? 6.156   62.051  170.102 1.00 33.25  ? 196 ASP C CB    1 
ATOM   9183  C CG    . ASP C  1 196 ? 6.487   60.653  169.609 1.00 38.96  ? 196 ASP C CG    1 
ATOM   9184  O OD1   . ASP C  1 196 ? 5.681   60.071  168.854 1.00 34.48  ? 196 ASP C OD1   1 
ATOM   9185  O OD2   . ASP C  1 196 ? 7.561   60.137  169.977 1.00 48.70  ? 196 ASP C OD2   1 
ATOM   9186  N N     . ALA C  1 197 ? 3.413   61.218  169.019 1.00 31.57  ? 197 ALA C N     1 
ATOM   9187  C CA    . ALA C  1 197 ? 2.052   60.753  169.236 1.00 35.44  ? 197 ALA C CA    1 
ATOM   9188  C C     . ALA C  1 197 ? 1.993   59.238  169.222 1.00 34.48  ? 197 ALA C C     1 
ATOM   9189  O O     . ALA C  1 197 ? 2.834   58.579  168.616 1.00 36.87  ? 197 ALA C O     1 
ATOM   9190  C CB    . ALA C  1 197 ? 1.109   61.328  168.178 1.00 29.06  ? 197 ALA C CB    1 
ATOM   9191  N N     . ILE C  1 198 ? 1.003   58.684  169.906 1.00 27.11  ? 198 ILE C N     1 
ATOM   9192  C CA    . ILE C  1 198 ? 0.715   57.263  169.781 1.00 27.42  ? 198 ILE C CA    1 
ATOM   9193  C C     . ILE C  1 198 ? -0.535  57.084  168.928 1.00 32.62  ? 198 ILE C C     1 
ATOM   9194  O O     . ILE C  1 198 ? -1.629  57.479  169.324 1.00 31.06  ? 198 ILE C O     1 
ATOM   9195  C CB    . ILE C  1 198 ? 0.520   56.591  171.145 1.00 30.11  ? 198 ILE C CB    1 
ATOM   9196  C CG1   . ILE C  1 198 ? 1.771   56.769  172.008 1.00 31.99  ? 198 ILE C CG1   1 
ATOM   9197  C CG2   . ILE C  1 198 ? 0.204   55.120  170.961 1.00 29.85  ? 198 ILE C CG2   1 
ATOM   9198  C CD1   . ILE C  1 198 ? 3.034   56.240  171.363 1.00 35.94  ? 198 ILE C CD1   1 
ATOM   9199  N N     . LEU C  1 199 ? -0.360  56.509  167.744 1.00 27.69  ? 199 LEU C N     1 
ATOM   9200  C CA    . LEU C  1 199 ? -1.472  56.277  166.837 1.00 30.59  ? 199 LEU C CA    1 
ATOM   9201  C C     . LEU C  1 199 ? -1.733  54.786  166.690 1.00 37.61  ? 199 LEU C C     1 
ATOM   9202  O O     . LEU C  1 199 ? -0.809  54.005  166.464 1.00 30.38  ? 199 LEU C O     1 
ATOM   9203  C CB    . LEU C  1 199 ? -1.192  56.902  165.466 1.00 25.13  ? 199 LEU C CB    1 
ATOM   9204  C CG    . LEU C  1 199 ? -2.219  56.601  164.364 1.00 27.99  ? 199 LEU C CG    1 
ATOM   9205  C CD1   . LEU C  1 199 ? -3.562  57.267  164.636 1.00 30.89  ? 199 LEU C CD1   1 
ATOM   9206  C CD2   . LEU C  1 199 ? -1.674  57.012  163.009 1.00 30.91  ? 199 LEU C CD2   1 
ATOM   9207  N N     . ILE C  1 200 ? -2.991  54.389  166.830 1.00 28.83  ? 200 ILE C N     1 
ATOM   9208  C CA    . ILE C  1 200 ? -3.366  52.989  166.680 1.00 29.52  ? 200 ILE C CA    1 
ATOM   9209  C C     . ILE C  1 200 ? -4.133  52.813  165.374 1.00 34.34  ? 200 ILE C C     1 
ATOM   9210  O O     . ILE C  1 200 ? -5.227  53.353  165.216 1.00 33.60  ? 200 ILE C O     1 
ATOM   9211  C CB    . ILE C  1 200 ? -4.213  52.504  167.873 1.00 32.52  ? 200 ILE C CB    1 
ATOM   9212  C CG1   . ILE C  1 200 ? -3.453  52.733  169.185 1.00 27.41  ? 200 ILE C CG1   1 
ATOM   9213  C CG2   . ILE C  1 200 ? -4.573  51.035  167.717 1.00 33.43  ? 200 ILE C CG2   1 
ATOM   9214  C CD1   . ILE C  1 200 ? -4.182  52.230  170.416 1.00 30.39  ? 200 ILE C CD1   1 
ATOM   9215  N N     . ASP C  1 201 ? -3.558  52.065  164.436 1.00 33.76  ? 201 ASP C N     1 
ATOM   9216  C CA    . ASP C  1 201 ? -4.143  51.988  163.099 1.00 29.14  ? 201 ASP C CA    1 
ATOM   9217  C C     . ASP C  1 201 ? -5.247  50.940  162.992 1.00 30.64  ? 201 ASP C C     1 
ATOM   9218  O O     . ASP C  1 201 ? -5.670  50.354  163.988 1.00 26.81  ? 201 ASP C O     1 
ATOM   9219  C CB    . ASP C  1 201 ? -3.057  51.728  162.039 1.00 30.21  ? 201 ASP C CB    1 
ATOM   9220  C CG    . ASP C  1 201 ? -2.432  50.339  162.138 1.00 38.39  ? 201 ASP C CG    1 
ATOM   9221  O OD1   . ASP C  1 201 ? -2.858  49.513  162.976 1.00 37.12  ? 201 ASP C OD1   1 
ATOM   9222  O OD2   . ASP C  1 201 ? -1.501  50.067  161.350 1.00 37.08  ? 201 ASP C OD2   1 
ATOM   9223  N N     . ALA C  1 202 ? -5.692  50.706  161.763 1.00 29.72  ? 202 ALA C N     1 
ATOM   9224  C CA    . ALA C  1 202 ? -6.817  49.820  161.488 1.00 35.15  ? 202 ALA C CA    1 
ATOM   9225  C C     . ALA C  1 202 ? -6.568  48.375  161.926 1.00 36.55  ? 202 ALA C C     1 
ATOM   9226  O O     . ALA C  1 202 ? -7.516  47.639  162.212 1.00 40.07  ? 202 ALA C O     1 
ATOM   9227  C CB    . ALA C  1 202 ? -7.151  49.866  160.014 1.00 40.15  ? 202 ALA C CB    1 
ATOM   9228  N N     . ASN C  1 203 ? -5.302  47.969  161.960 1.00 34.51  ? 203 ASN C N     1 
ATOM   9229  C CA    . ASN C  1 203 ? -4.944  46.607  162.343 1.00 36.42  ? 203 ASN C CA    1 
ATOM   9230  C C     . ASN C  1 203 ? -4.682  46.469  163.839 1.00 35.44  ? 203 ASN C C     1 
ATOM   9231  O O     . ASN C  1 203 ? -4.359  45.379  164.322 1.00 35.02  ? 203 ASN C O     1 
ATOM   9232  C CB    . ASN C  1 203 ? -3.709  46.141  161.559 1.00 37.04  ? 203 ASN C CB    1 
ATOM   9233  C CG    . ASN C  1 203 ? -3.930  46.141  160.060 1.00 43.06  ? 203 ASN C CG    1 
ATOM   9234  O OD1   . ASN C  1 203 ? -3.104  46.644  159.300 1.00 48.29  ? 203 ASN C OD1   1 
ATOM   9235  N ND2   . ASN C  1 203 ? -5.051  45.580  159.627 1.00 39.70  ? 203 ASN C ND2   1 
ATOM   9236  N N     . GLY C  1 204 ? -4.818  47.577  164.564 1.00 31.32  ? 204 GLY C N     1 
ATOM   9237  C CA    . GLY C  1 204 ? -4.565  47.590  165.993 1.00 30.54  ? 204 GLY C CA    1 
ATOM   9238  C C     . GLY C  1 204 ? -3.103  47.804  166.332 1.00 33.66  ? 204 GLY C C     1 
ATOM   9239  O O     . GLY C  1 204 ? -2.708  47.739  167.497 1.00 34.12  ? 204 GLY C O     1 
ATOM   9240  N N     . ALA C  1 205 ? -2.293  48.049  165.308 1.00 30.56  ? 205 ALA C N     1 
ATOM   9241  C CA    . ALA C  1 205 ? -0.869  48.289  165.506 1.00 35.49  ? 205 ALA C CA    1 
ATOM   9242  C C     . ALA C  1 205 ? -0.650  49.601  166.247 1.00 33.57  ? 205 ALA C C     1 
ATOM   9243  O O     . ALA C  1 205 ? -1.150  50.647  165.841 1.00 32.89  ? 205 ALA C O     1 
ATOM   9244  C CB    . ALA C  1 205 ? -0.139  48.300  164.172 1.00 28.02  ? 205 ALA C CB    1 
ATOM   9245  N N     . ILE C  1 206 ? 0.098   49.536  167.342 1.00 30.29  ? 206 ILE C N     1 
ATOM   9246  C CA    . ILE C  1 206 ? 0.365   50.710  168.165 1.00 30.46  ? 206 ILE C CA    1 
ATOM   9247  C C     . ILE C  1 206 ? 1.637   51.422  167.701 1.00 35.09  ? 206 ILE C C     1 
ATOM   9248  O O     . ILE C  1 206 ? 2.744   50.919  167.879 1.00 35.59  ? 206 ILE C O     1 
ATOM   9249  C CB    . ILE C  1 206 ? 0.481   50.318  169.646 1.00 30.11  ? 206 ILE C CB    1 
ATOM   9250  C CG1   . ILE C  1 206 ? -0.798  49.608  170.099 1.00 33.75  ? 206 ILE C CG1   1 
ATOM   9251  C CG2   . ILE C  1 206 ? 0.748   51.541  170.502 1.00 35.64  ? 206 ILE C CG2   1 
ATOM   9252  C CD1   . ILE C  1 206 ? -0.746  49.080  171.513 1.00 30.69  ? 206 ILE C CD1   1 
ATOM   9253  N N     . LEU C  1 207 ? 1.466   52.598  167.107 1.00 29.01  ? 207 LEU C N     1 
ATOM   9254  C CA    . LEU C  1 207 ? 2.563   53.287  166.438 1.00 32.16  ? 207 LEU C CA    1 
ATOM   9255  C C     . LEU C  1 207 ? 2.919   54.607  167.108 1.00 33.35  ? 207 LEU C C     1 
ATOM   9256  O O     . LEU C  1 207 ? 2.034   55.368  167.496 1.00 32.49  ? 207 LEU C O     1 
ATOM   9257  C CB    . LEU C  1 207 ? 2.203   53.541  164.967 1.00 32.14  ? 207 LEU C CB    1 
ATOM   9258  C CG    . LEU C  1 207 ? 1.637   52.353  164.187 1.00 34.15  ? 207 LEU C CG    1 
ATOM   9259  C CD1   . LEU C  1 207 ? 1.096   52.805  162.842 1.00 33.53  ? 207 LEU C CD1   1 
ATOM   9260  C CD2   . LEU C  1 207 ? 2.691   51.266  164.004 1.00 34.51  ? 207 LEU C CD2   1 
ATOM   9261  N N     . ASP C  1 208 ? 4.215   54.876  167.250 1.00 25.06  ? 208 ASP C N     1 
ATOM   9262  C CA    . ASP C  1 208 ? 4.666   56.217  167.617 1.00 28.03  ? 208 ASP C CA    1 
ATOM   9263  C C     . ASP C  1 208 ? 5.181   56.931  166.370 1.00 25.58  ? 208 ASP C C     1 
ATOM   9264  O O     . ASP C  1 208 ? 5.068   56.399  165.265 1.00 31.80  ? 208 ASP C O     1 
ATOM   9265  C CB    . ASP C  1 208 ? 5.735   56.167  168.715 1.00 33.09  ? 208 ASP C CB    1 
ATOM   9266  C CG    . ASP C  1 208 ? 7.007   55.449  168.283 1.00 34.13  ? 208 ASP C CG    1 
ATOM   9267  O OD1   . ASP C  1 208 ? 7.057   54.876  167.174 1.00 29.36  ? 208 ASP C OD1   1 
ATOM   9268  O OD2   . ASP C  1 208 ? 7.965   55.453  169.082 1.00 33.78  ? 208 ASP C OD2   1 
ATOM   9269  N N     . ARG C  1 209 ? 5.738   58.126  166.543 1.00 26.78  ? 209 ARG C N     1 
ATOM   9270  C CA    . ARG C  1 209 ? 6.181   58.929  165.407 1.00 32.44  ? 209 ARG C CA    1 
ATOM   9271  C C     . ARG C  1 209 ? 7.192   58.190  164.533 1.00 31.41  ? 209 ARG C C     1 
ATOM   9272  O O     . ARG C  1 209 ? 7.083   58.186  163.305 1.00 33.89  ? 209 ARG C O     1 
ATOM   9273  C CB    . ARG C  1 209 ? 6.784   60.250  165.887 1.00 35.30  ? 209 ARG C CB    1 
ATOM   9274  C CG    . ARG C  1 209 ? 7.285   61.130  164.762 1.00 36.00  ? 209 ARG C CG    1 
ATOM   9275  C CD    . ARG C  1 209 ? 7.897   62.419  165.281 1.00 34.33  ? 209 ARG C CD    1 
ATOM   9276  N NE    . ARG C  1 209 ? 8.314   63.293  164.189 1.00 31.60  ? 209 ARG C NE    1 
ATOM   9277  C CZ    . ARG C  1 209 ? 8.703   64.554  164.348 1.00 37.92  ? 209 ARG C CZ    1 
ATOM   9278  N NH1   . ARG C  1 209 ? 8.723   65.093  165.559 1.00 33.89  ? 209 ARG C NH1   1 
ATOM   9279  N NH2   . ARG C  1 209 ? 9.063   65.279  163.297 1.00 34.96  ? 209 ARG C NH2   1 
ATOM   9280  N N     . GLN C  1 210 ? 8.172   57.564  165.174 1.00 31.92  ? 210 GLN C N     1 
ATOM   9281  C CA    . GLN C  1 210 ? 9.187   56.803  164.458 1.00 35.59  ? 210 GLN C CA    1 
ATOM   9282  C C     . GLN C  1 210 ? 8.546   55.674  163.655 1.00 34.82  ? 210 GLN C C     1 
ATOM   9283  O O     . GLN C  1 210 ? 8.892   55.448  162.498 1.00 38.35  ? 210 GLN C O     1 
ATOM   9284  C CB    . GLN C  1 210 ? 10.225  56.242  165.434 1.00 30.99  ? 210 GLN C CB    1 
ATOM   9285  C CG    . GLN C  1 210 ? 11.389  55.535  164.759 1.00 49.84  ? 210 GLN C CG    1 
ATOM   9286  C CD    . GLN C  1 210 ? 12.503  55.175  165.726 1.00 62.34  ? 210 GLN C CD    1 
ATOM   9287  O OE1   . GLN C  1 210 ? 12.269  54.976  166.920 1.00 59.95  ? 210 GLN C OE1   1 
ATOM   9288  N NE2   . GLN C  1 210 ? 13.726  55.097  165.213 1.00 56.04  ? 210 GLN C NE2   1 
ATOM   9289  N N     . ALA C  1 211 ? 7.588   54.991  164.271 1.00 29.59  ? 211 ALA C N     1 
ATOM   9290  C CA    . ALA C  1 211 ? 6.956   53.834  163.651 1.00 33.66  ? 211 ALA C CA    1 
ATOM   9291  C C     . ALA C  1 211 ? 5.972   54.209  162.542 1.00 36.96  ? 211 ALA C C     1 
ATOM   9292  O O     . ALA C  1 211 ? 5.849   53.490  161.551 1.00 36.49  ? 211 ALA C O     1 
ATOM   9293  C CB    . ALA C  1 211 ? 6.248   52.997  164.707 1.00 35.89  ? 211 ALA C CB    1 
ATOM   9294  N N     . MET C  1 212 ? 5.269   55.326  162.704 1.00 36.16  ? 212 MET C N     1 
ATOM   9295  C CA    . MET C  1 212 ? 4.244   55.705  161.735 1.00 32.23  ? 212 MET C CA    1 
ATOM   9296  C C     . MET C  1 212 ? 4.848   56.444  160.545 1.00 34.01  ? 212 MET C C     1 
ATOM   9297  O O     . MET C  1 212 ? 4.235   56.533  159.482 1.00 35.67  ? 212 MET C O     1 
ATOM   9298  C CB    . MET C  1 212 ? 3.153   56.558  162.397 1.00 34.67  ? 212 MET C CB    1 
ATOM   9299  C CG    . MET C  1 212 ? 3.569   57.975  162.763 1.00 29.84  ? 212 MET C CG    1 
ATOM   9300  S SD    . MET C  1 212 ? 2.197   58.928  163.461 1.00 34.77  ? 212 MET C SD    1 
ATOM   9301  C CE    . MET C  1 212 ? 2.194   58.360  165.158 1.00 22.12  ? 212 MET C CE    1 
ATOM   9302  N N     . GLY C  1 213 ? 6.057   56.964  160.719 1.00 32.95  ? 213 GLY C N     1 
ATOM   9303  C CA    . GLY C  1 213 ? 6.714   57.709  159.661 1.00 36.33  ? 213 GLY C CA    1 
ATOM   9304  C C     . GLY C  1 213 ? 6.222   59.144  159.609 1.00 39.07  ? 213 GLY C C     1 
ATOM   9305  O O     . GLY C  1 213 ? 5.191   59.478  160.193 1.00 34.60  ? 213 GLY C O     1 
ATOM   9306  N N     . GLU C  1 214 ? 6.956   59.990  158.894 1.00 38.48  ? 214 GLU C N     1 
ATOM   9307  C CA    . GLU C  1 214 ? 6.711   61.428  158.923 1.00 40.57  ? 214 GLU C CA    1 
ATOM   9308  C C     . GLU C  1 214 ? 5.481   61.869  158.133 1.00 39.90  ? 214 GLU C C     1 
ATOM   9309  O O     . GLU C  1 214 ? 4.890   62.896  158.447 1.00 45.04  ? 214 GLU C O     1 
ATOM   9310  C CB    . GLU C  1 214 ? 7.946   62.180  158.417 1.00 41.88  ? 214 GLU C CB    1 
ATOM   9311  C CG    . GLU C  1 214 ? 9.106   62.187  159.400 1.00 38.82  ? 214 GLU C CG    1 
ATOM   9312  C CD    . GLU C  1 214 ? 8.725   62.784  160.742 1.00 41.52  ? 214 GLU C CD    1 
ATOM   9313  O OE1   . GLU C  1 214 ? 8.488   64.009  160.800 1.00 46.09  ? 214 GLU C OE1   1 
ATOM   9314  O OE2   . GLU C  1 214 ? 8.662   62.033  161.738 1.00 40.56  ? 214 GLU C OE2   1 
ATOM   9315  N N     . ASP C  1 215 ? 5.095   61.108  157.114 1.00 43.46  ? 215 ASP C N     1 
ATOM   9316  C CA    . ASP C  1 215 ? 3.909   61.455  156.331 1.00 43.49  ? 215 ASP C CA    1 
ATOM   9317  C C     . ASP C  1 215 ? 2.636   61.314  157.159 1.00 43.67  ? 215 ASP C C     1 
ATOM   9318  O O     . ASP C  1 215 ? 1.734   62.154  157.084 1.00 40.14  ? 215 ASP C O     1 
ATOM   9319  C CB    . ASP C  1 215 ? 3.810   60.585  155.076 1.00 42.28  ? 215 ASP C CB    1 
ATOM   9320  C CG    . ASP C  1 215 ? 4.683   61.093  153.947 1.00 54.98  ? 215 ASP C CG    1 
ATOM   9321  O OD1   . ASP C  1 215 ? 4.994   62.304  153.935 1.00 51.00  ? 215 ASP C OD1   1 
ATOM   9322  O OD2   . ASP C  1 215 ? 5.053   60.285  153.069 1.00 60.49  ? 215 ASP C OD2   1 
ATOM   9323  N N     . VAL C  1 216 ? 2.570   60.248  157.950 1.00 42.14  ? 216 VAL C N     1 
ATOM   9324  C CA    . VAL C  1 216 ? 1.422   60.007  158.812 1.00 36.67  ? 216 VAL C CA    1 
ATOM   9325  C C     . VAL C  1 216 ? 1.457   60.934  160.025 1.00 34.08  ? 216 VAL C C     1 
ATOM   9326  O O     . VAL C  1 216 ? 0.425   61.470  160.430 1.00 40.36  ? 216 VAL C O     1 
ATOM   9327  C CB    . VAL C  1 216 ? 1.367   58.541  159.278 1.00 36.42  ? 216 VAL C CB    1 
ATOM   9328  C CG1   . VAL C  1 216 ? 0.232   58.337  160.272 1.00 32.97  ? 216 VAL C CG1   1 
ATOM   9329  C CG2   . VAL C  1 216 ? 1.206   57.617  158.082 1.00 32.37  ? 216 VAL C CG2   1 
ATOM   9330  N N     . PHE C  1 217 ? 2.645   61.132  160.592 1.00 35.88  ? 217 PHE C N     1 
ATOM   9331  C CA    . PHE C  1 217 ? 2.796   62.019  161.743 1.00 35.40  ? 217 PHE C CA    1 
ATOM   9332  C C     . PHE C  1 217 ? 2.503   63.467  161.370 1.00 34.71  ? 217 PHE C C     1 
ATOM   9333  O O     . PHE C  1 217 ? 2.083   64.264  162.209 1.00 33.93  ? 217 PHE C O     1 
ATOM   9334  C CB    . PHE C  1 217 ? 4.200   61.912  162.341 1.00 34.75  ? 217 PHE C CB    1 
ATOM   9335  C CG    . PHE C  1 217 ? 4.436   62.852  163.488 1.00 30.58  ? 217 PHE C CG    1 
ATOM   9336  C CD1   . PHE C  1 217 ? 3.858   62.610  164.724 1.00 27.32  ? 217 PHE C CD1   1 
ATOM   9337  C CD2   . PHE C  1 217 ? 5.219   63.983  163.329 1.00 34.90  ? 217 PHE C CD2   1 
ATOM   9338  C CE1   . PHE C  1 217 ? 4.062   63.476  165.782 1.00 34.79  ? 217 PHE C CE1   1 
ATOM   9339  C CE2   . PHE C  1 217 ? 5.426   64.852  164.384 1.00 32.25  ? 217 PHE C CE2   1 
ATOM   9340  C CZ    . PHE C  1 217 ? 4.848   64.597  165.613 1.00 32.17  ? 217 PHE C CZ    1 
ATOM   9341  N N     . TRP C  1 218 ? 2.740   63.801  160.107 1.00 32.40  ? 218 TRP C N     1 
ATOM   9342  C CA    . TRP C  1 218 ? 2.379   65.107  159.574 1.00 35.08  ? 218 TRP C CA    1 
ATOM   9343  C C     . TRP C  1 218 ? 0.861   65.211  159.462 1.00 38.33  ? 218 TRP C C     1 
ATOM   9344  O O     . TRP C  1 218 ? 0.258   66.182  159.917 1.00 35.46  ? 218 TRP C O     1 
ATOM   9345  C CB    . TRP C  1 218 ? 3.050   65.323  158.214 1.00 35.42  ? 218 TRP C CB    1 
ATOM   9346  C CG    . TRP C  1 218 ? 2.637   66.557  157.473 1.00 39.83  ? 218 TRP C CG    1 
ATOM   9347  C CD1   . TRP C  1 218 ? 3.160   67.810  157.607 1.00 40.00  ? 218 TRP C CD1   1 
ATOM   9348  C CD2   . TRP C  1 218 ? 1.630   66.650  156.456 1.00 40.95  ? 218 TRP C CD2   1 
ATOM   9349  N NE1   . TRP C  1 218 ? 2.533   68.680  156.746 1.00 42.42  ? 218 TRP C NE1   1 
ATOM   9350  C CE2   . TRP C  1 218 ? 1.589   67.992  156.029 1.00 42.15  ? 218 TRP C CE2   1 
ATOM   9351  C CE3   . TRP C  1 218 ? 0.755   65.728  155.870 1.00 39.27  ? 218 TRP C CE3   1 
ATOM   9352  C CZ2   . TRP C  1 218 ? 0.710   68.436  155.044 1.00 39.03  ? 218 TRP C CZ2   1 
ATOM   9353  C CZ3   . TRP C  1 218 ? -0.118  66.172  154.893 1.00 39.63  ? 218 TRP C CZ3   1 
ATOM   9354  C CH2   . TRP C  1 218 ? -0.134  67.514  154.490 1.00 42.74  ? 218 TRP C CH2   1 
ATOM   9355  N N     . ALA C  1 219 ? 0.250   64.180  158.888 1.00 36.57  ? 219 ALA C N     1 
ATOM   9356  C CA    . ALA C  1 219 ? -1.180  64.179  158.598 1.00 33.84  ? 219 ALA C CA    1 
ATOM   9357  C C     . ALA C  1 219 ? -2.056  64.273  159.843 1.00 37.09  ? 219 ALA C C     1 
ATOM   9358  O O     . ALA C  1 219 ? -3.099  64.918  159.815 1.00 40.00  ? 219 ALA C O     1 
ATOM   9359  C CB    . ALA C  1 219 ? -1.544  62.939  157.812 1.00 40.70  ? 219 ALA C CB    1 
ATOM   9360  N N     . ILE C  1 220 ? -1.649  63.628  160.931 1.00 34.35  ? 220 ILE C N     1 
ATOM   9361  C CA    . ILE C  1 220 ? -2.479  63.612  162.133 1.00 33.88  ? 220 ILE C CA    1 
ATOM   9362  C C     . ILE C  1 220 ? -2.463  64.953  162.863 1.00 34.47  ? 220 ILE C C     1 
ATOM   9363  O O     . ILE C  1 220 ? -3.309  65.210  163.720 1.00 34.41  ? 220 ILE C O     1 
ATOM   9364  C CB    . ILE C  1 220 ? -2.042  62.511  163.122 1.00 33.71  ? 220 ILE C CB    1 
ATOM   9365  C CG1   . ILE C  1 220 ? -0.579  62.707  163.529 1.00 34.50  ? 220 ILE C CG1   1 
ATOM   9366  C CG2   . ILE C  1 220 ? -2.265  61.130  162.518 1.00 32.83  ? 220 ILE C CG2   1 
ATOM   9367  C CD1   . ILE C  1 220 ? -0.124  61.763  164.623 1.00 33.84  ? 220 ILE C CD1   1 
ATOM   9368  N N     . ARG C  1 221 ? -1.504  65.805  162.517 1.00 31.13  ? 221 ARG C N     1 
ATOM   9369  C CA    . ARG C  1 221 ? -1.369  67.105  163.164 1.00 37.20  ? 221 ARG C CA    1 
ATOM   9370  C C     . ARG C  1 221 ? -2.156  68.193  162.440 1.00 35.91  ? 221 ARG C C     1 
ATOM   9371  O O     . ARG C  1 221 ? -1.621  69.260  162.144 1.00 31.53  ? 221 ARG C O     1 
ATOM   9372  C CB    . ARG C  1 221 ? 0.105   67.509  163.253 1.00 29.92  ? 221 ARG C CB    1 
ATOM   9373  C CG    . ARG C  1 221 ? 0.910   66.713  164.262 1.00 33.89  ? 221 ARG C CG    1 
ATOM   9374  C CD    . ARG C  1 221 ? 2.356   67.174  164.284 1.00 32.19  ? 221 ARG C CD    1 
ATOM   9375  N NE    . ARG C  1 221 ? 3.060   66.812  163.058 1.00 30.40  ? 221 ARG C NE    1 
ATOM   9376  C CZ    . ARG C  1 221 ? 4.113   67.466  162.582 1.00 36.39  ? 221 ARG C CZ    1 
ATOM   9377  N NH1   . ARG C  1 221 ? 4.581   68.525  163.228 1.00 36.94  ? 221 ARG C NH1   1 
ATOM   9378  N NH2   . ARG C  1 221 ? 4.695   67.064  161.459 1.00 36.31  ? 221 ARG C NH2   1 
ATOM   9379  N N     . GLY C  1 222 ? -3.426  67.923  162.156 1.00 35.48  ? 222 GLY C N     1 
ATOM   9380  C CA    . GLY C  1 222 ? -4.274  68.906  161.506 1.00 38.61  ? 222 GLY C CA    1 
ATOM   9381  C C     . GLY C  1 222 ? -5.100  68.354  160.358 1.00 38.20  ? 222 GLY C C     1 
ATOM   9382  O O     . GLY C  1 222 ? -5.914  69.067  159.771 1.00 33.89  ? 222 GLY C O     1 
ATOM   9383  N N     . GLY C  1 223 ? -4.895  67.081  160.036 1.00 35.18  ? 223 GLY C N     1 
ATOM   9384  C CA    . GLY C  1 223 ? -5.581  66.468  158.913 1.00 31.11  ? 223 GLY C CA    1 
ATOM   9385  C C     . GLY C  1 223 ? -6.998  66.027  159.215 1.00 33.26  ? 223 GLY C C     1 
ATOM   9386  O O     . GLY C  1 223 ? -7.679  65.480  158.347 1.00 35.31  ? 223 GLY C O     1 
ATOM   9387  N N     . GLY C  1 224 ? -7.443  66.252  160.447 1.00 34.00  ? 224 GLY C N     1 
ATOM   9388  C CA    . GLY C  1 224 ? -8.803  65.921  160.838 1.00 31.29  ? 224 GLY C CA    1 
ATOM   9389  C C     . GLY C  1 224 ? -8.909  64.588  161.552 1.00 35.57  ? 224 GLY C C     1 
ATOM   9390  O O     . GLY C  1 224 ? -8.231  63.626  161.189 1.00 34.59  ? 224 GLY C O     1 
ATOM   9391  N N     . GLY C  1 225 ? -9.766  64.528  162.566 1.00 34.01  ? 225 GLY C N     1 
ATOM   9392  C CA    . GLY C  1 225 ? -9.965  63.308  163.325 1.00 36.72  ? 225 GLY C CA    1 
ATOM   9393  C C     . GLY C  1 225 ? -10.811 62.286  162.587 1.00 35.55  ? 225 GLY C C     1 
ATOM   9394  O O     . GLY C  1 225 ? -11.466 62.613  161.596 1.00 34.11  ? 225 GLY C O     1 
ATOM   9395  N N     . GLY C  1 226 ? -10.781 61.044  163.065 1.00 35.79  ? 226 GLY C N     1 
ATOM   9396  C CA    . GLY C  1 226 ? -11.605 59.974  162.521 1.00 31.99  ? 226 GLY C CA    1 
ATOM   9397  C C     . GLY C  1 226 ? -11.195 59.493  161.142 1.00 38.05  ? 226 GLY C C     1 
ATOM   9398  O O     . GLY C  1 226 ? -12.011 58.952  160.397 1.00 36.80  ? 226 GLY C O     1 
ATOM   9399  N N     . VAL C  1 227 ? -9.925  59.679  160.799 1.00 34.88  ? 227 VAL C N     1 
ATOM   9400  C CA    . VAL C  1 227 ? -9.470  59.401  159.442 1.00 37.12  ? 227 VAL C CA    1 
ATOM   9401  C C     . VAL C  1 227 ? -8.242  58.488  159.404 1.00 33.09  ? 227 VAL C C     1 
ATOM   9402  O O     . VAL C  1 227 ? -8.102  57.661  158.502 1.00 35.90  ? 227 VAL C O     1 
ATOM   9403  C CB    . VAL C  1 227 ? -9.154  60.722  158.694 1.00 32.76  ? 227 VAL C CB    1 
ATOM   9404  C CG1   . VAL C  1 227 ? -8.591  60.450  157.309 1.00 32.17  ? 227 VAL C CG1   1 
ATOM   9405  C CG2   . VAL C  1 227 ? -10.407 61.585  158.597 1.00 36.54  ? 227 VAL C CG2   1 
ATOM   9406  N N     . TRP C  1 228 ? -7.371  58.618  160.398 1.00 30.82  ? 228 TRP C N     1 
ATOM   9407  C CA    . TRP C  1 228 ? -6.050  57.999  160.335 1.00 31.42  ? 228 TRP C CA    1 
ATOM   9408  C C     . TRP C  1 228 ? -5.906  56.807  161.267 1.00 31.15  ? 228 TRP C C     1 
ATOM   9409  O O     . TRP C  1 228 ? -4.969  56.019  161.144 1.00 36.63  ? 228 TRP C O     1 
ATOM   9410  C CB    . TRP C  1 228 ? -4.987  59.045  160.660 1.00 27.53  ? 228 TRP C CB    1 
ATOM   9411  C CG    . TRP C  1 228 ? -5.324  60.356  160.051 1.00 33.91  ? 228 TRP C CG    1 
ATOM   9412  C CD1   . TRP C  1 228 ? -5.948  61.408  160.655 1.00 36.08  ? 228 TRP C CD1   1 
ATOM   9413  C CD2   . TRP C  1 228 ? -5.100  60.744  158.697 1.00 35.06  ? 228 TRP C CD2   1 
ATOM   9414  N NE1   . TRP C  1 228 ? -6.110  62.439  159.761 1.00 32.97  ? 228 TRP C NE1   1 
ATOM   9415  C CE2   . TRP C  1 228 ? -5.599  62.054  158.549 1.00 30.95  ? 228 TRP C CE2   1 
ATOM   9416  C CE3   . TRP C  1 228 ? -4.517  60.113  157.594 1.00 32.16  ? 228 TRP C CE3   1 
ATOM   9417  C CZ2   . TRP C  1 228 ? -5.532  62.744  157.342 1.00 29.92  ? 228 TRP C CZ2   1 
ATOM   9418  C CZ3   . TRP C  1 228 ? -4.451  60.798  156.399 1.00 37.00  ? 228 TRP C CZ3   1 
ATOM   9419  C CH2   . TRP C  1 228 ? -4.954  62.102  156.281 1.00 36.45  ? 228 TRP C CH2   1 
ATOM   9420  N N     . GLY C  1 229 ? -6.849  56.672  162.188 1.00 32.63  ? 229 GLY C N     1 
ATOM   9421  C CA    . GLY C  1 229 ? -6.760  55.672  163.230 1.00 31.11  ? 229 GLY C CA    1 
ATOM   9422  C C     . GLY C  1 229 ? -7.146  56.327  164.536 1.00 32.38  ? 229 GLY C C     1 
ATOM   9423  O O     . GLY C  1 229 ? -7.575  57.481  164.548 1.00 31.84  ? 229 GLY C O     1 
ATOM   9424  N N     . ALA C  1 230 ? -6.992  55.608  165.639 1.00 32.29  ? 230 ALA C N     1 
ATOM   9425  C CA    . ALA C  1 230 ? -7.314  56.177  166.938 1.00 32.64  ? 230 ALA C CA    1 
ATOM   9426  C C     . ALA C  1 230 ? -6.065  56.707  167.620 1.00 34.98  ? 230 ALA C C     1 
ATOM   9427  O O     . ALA C  1 230 ? -5.151  55.944  167.925 1.00 33.77  ? 230 ALA C O     1 
ATOM   9428  C CB    . ALA C  1 230 ? -7.997  55.145  167.816 1.00 34.63  ? 230 ALA C CB    1 
ATOM   9429  N N     . ILE C  1 231 ? -6.027  58.015  167.854 1.00 32.33  ? 231 ILE C N     1 
ATOM   9430  C CA    . ILE C  1 231 ? -4.964  58.605  168.655 1.00 31.48  ? 231 ILE C CA    1 
ATOM   9431  C C     . ILE C  1 231 ? -5.125  58.139  170.090 1.00 34.13  ? 231 ILE C C     1 
ATOM   9432  O O     . ILE C  1 231 ? -6.171  58.360  170.699 1.00 32.70  ? 231 ILE C O     1 
ATOM   9433  C CB    . ILE C  1 231 ? -4.986  60.149  168.620 1.00 31.57  ? 231 ILE C CB    1 
ATOM   9434  C CG1   . ILE C  1 231 ? -4.794  60.665  167.196 1.00 33.51  ? 231 ILE C CG1   1 
ATOM   9435  C CG2   . ILE C  1 231 ? -3.902  60.720  169.530 1.00 33.68  ? 231 ILE C CG2   1 
ATOM   9436  C CD1   . ILE C  1 231 ? -3.392  60.470  166.662 1.00 36.83  ? 231 ILE C CD1   1 
ATOM   9437  N N     . TYR C  1 232 ? -4.105  57.480  170.628 1.00 31.87  ? 232 TYR C N     1 
ATOM   9438  C CA    . TYR C  1 232 ? -4.139  57.110  172.034 1.00 31.44  ? 232 TYR C CA    1 
ATOM   9439  C C     . TYR C  1 232 ? -3.659  58.276  172.888 1.00 33.51  ? 232 TYR C C     1 
ATOM   9440  O O     . TYR C  1 232 ? -4.233  58.562  173.938 1.00 36.18  ? 232 TYR C O     1 
ATOM   9441  C CB    . TYR C  1 232 ? -3.285  55.871  172.315 1.00 29.17  ? 232 TYR C CB    1 
ATOM   9442  C CG    . TYR C  1 232 ? -2.845  55.796  173.761 1.00 30.07  ? 232 TYR C CG    1 
ATOM   9443  C CD1   . TYR C  1 232 ? -3.769  55.585  174.779 1.00 33.28  ? 232 TYR C CD1   1 
ATOM   9444  C CD2   . TYR C  1 232 ? -1.512  55.963  174.111 1.00 33.96  ? 232 TYR C CD2   1 
ATOM   9445  C CE1   . TYR C  1 232 ? -3.373  55.531  176.103 1.00 36.60  ? 232 TYR C CE1   1 
ATOM   9446  C CE2   . TYR C  1 232 ? -1.107  55.911  175.430 1.00 30.27  ? 232 TYR C CE2   1 
ATOM   9447  C CZ    . TYR C  1 232 ? -2.039  55.696  176.421 1.00 38.49  ? 232 TYR C CZ    1 
ATOM   9448  O OH    . TYR C  1 232 ? -1.639  55.643  177.737 1.00 40.77  ? 232 TYR C OH    1 
ATOM   9449  N N     . ALA C  1 233 ? -2.607  58.948  172.432 1.00 30.92  ? 233 ALA C N     1 
ATOM   9450  C CA    . ALA C  1 233 ? -2.016  60.034  173.206 1.00 38.13  ? 233 ALA C CA    1 
ATOM   9451  C C     . ALA C  1 233 ? -1.220  61.012  172.344 1.00 33.81  ? 233 ALA C C     1 
ATOM   9452  O O     . ALA C  1 233 ? -0.678  60.642  171.302 1.00 31.29  ? 233 ALA C O     1 
ATOM   9453  C CB    . ALA C  1 233 ? -1.127  59.470  174.304 1.00 28.94  ? 233 ALA C CB    1 
ATOM   9454  N N     . TRP C  1 234 ? -1.160  62.263  172.792 1.00 31.25  ? 234 TRP C N     1 
ATOM   9455  C CA    . TRP C  1 234 ? -0.333  63.281  172.154 1.00 35.60  ? 234 TRP C CA    1 
ATOM   9456  C C     . TRP C  1 234 ? 0.873   63.595  173.029 1.00 34.41  ? 234 TRP C C     1 
ATOM   9457  O O     . TRP C  1 234 ? 0.754   63.646  174.254 1.00 36.82  ? 234 TRP C O     1 
ATOM   9458  C CB    . TRP C  1 234 ? -1.117  64.577  171.913 1.00 33.04  ? 234 TRP C CB    1 
ATOM   9459  C CG    . TRP C  1 234 ? -2.340  64.461  171.054 1.00 33.78  ? 234 TRP C CG    1 
ATOM   9460  C CD1   . TRP C  1 234 ? -3.635  64.387  171.478 1.00 33.38  ? 234 TRP C CD1   1 
ATOM   9461  C CD2   . TRP C  1 234 ? -2.385  64.444  169.622 1.00 35.92  ? 234 TRP C CD2   1 
ATOM   9462  N NE1   . TRP C  1 234 ? -4.483  64.312  170.398 1.00 31.51  ? 234 TRP C NE1   1 
ATOM   9463  C CE2   . TRP C  1 234 ? -3.741  64.346  169.247 1.00 31.27  ? 234 TRP C CE2   1 
ATOM   9464  C CE3   . TRP C  1 234 ? -1.410  64.498  168.621 1.00 34.25  ? 234 TRP C CE3   1 
ATOM   9465  C CZ2   . TRP C  1 234 ? -4.147  64.297  167.915 1.00 30.95  ? 234 TRP C CZ2   1 
ATOM   9466  C CZ3   . TRP C  1 234 ? -1.814  64.447  167.298 1.00 34.07  ? 234 TRP C CZ3   1 
ATOM   9467  C CH2   . TRP C  1 234 ? -3.171  64.347  166.957 1.00 36.94  ? 234 TRP C CH2   1 
ATOM   9468  N N     . LYS C  1 235 ? 2.029   63.809  172.412 1.00 34.67  ? 235 LYS C N     1 
ATOM   9469  C CA    . LYS C  1 235 ? 3.146   64.401  173.138 1.00 37.79  ? 235 LYS C CA    1 
ATOM   9470  C C     . LYS C  1 235 ? 3.287   65.851  172.698 1.00 33.55  ? 235 LYS C C     1 
ATOM   9471  O O     . LYS C  1 235 ? 3.538   66.132  171.526 1.00 36.69  ? 235 LYS C O     1 
ATOM   9472  C CB    . LYS C  1 235 ? 4.452   63.641  172.910 1.00 33.92  ? 235 LYS C CB    1 
ATOM   9473  C CG    . LYS C  1 235 ? 5.555   64.082  173.865 1.00 35.31  ? 235 LYS C CG    1 
ATOM   9474  C CD    . LYS C  1 235 ? 6.874   63.373  173.609 1.00 33.00  ? 235 LYS C CD    1 
ATOM   9475  C CE    . LYS C  1 235 ? 7.948   63.881  174.562 1.00 36.37  ? 235 LYS C CE    1 
ATOM   9476  N NZ    . LYS C  1 235 ? 9.280   63.275  174.289 1.00 39.02  ? 235 LYS C NZ    1 
ATOM   9477  N N     . ILE C  1 236 ? 3.105   66.770  173.638 1.00 35.28  ? 236 ILE C N     1 
ATOM   9478  C CA    . ILE C  1 236 ? 3.101   68.188  173.316 1.00 37.13  ? 236 ILE C CA    1 
ATOM   9479  C C     . ILE C  1 236 ? 4.243   68.934  173.989 1.00 38.45  ? 236 ILE C C     1 
ATOM   9480  O O     . ILE C  1 236 ? 4.708   68.545  175.058 1.00 42.70  ? 236 ILE C O     1 
ATOM   9481  C CB    . ILE C  1 236 ? 1.772   68.851  173.728 1.00 38.02  ? 236 ILE C CB    1 
ATOM   9482  C CG1   . ILE C  1 236 ? 1.503   68.626  175.220 1.00 40.29  ? 236 ILE C CG1   1 
ATOM   9483  C CG2   . ILE C  1 236 ? 0.630   68.297  172.899 1.00 37.88  ? 236 ILE C CG2   1 
ATOM   9484  C CD1   . ILE C  1 236 ? 0.324   69.415  175.759 1.00 37.50  ? 236 ILE C CD1   1 
ATOM   9485  N N     . LYS C  1 237 ? 4.694   70.005  173.347 1.00 42.78  ? 237 LYS C N     1 
ATOM   9486  C CA    . LYS C  1 237 ? 5.654   70.911  173.958 1.00 43.91  ? 237 LYS C CA    1 
ATOM   9487  C C     . LYS C  1 237 ? 4.923   71.936  174.819 1.00 48.53  ? 237 LYS C C     1 
ATOM   9488  O O     . LYS C  1 237 ? 4.057   72.659  174.330 1.00 49.83  ? 237 LYS C O     1 
ATOM   9489  C CB    . LYS C  1 237 ? 6.491   71.620  172.891 1.00 47.89  ? 237 LYS C CB    1 
ATOM   9490  C CG    . LYS C  1 237 ? 7.563   72.534  173.458 1.00 59.30  ? 237 LYS C CG    1 
ATOM   9491  C CD    . LYS C  1 237 ? 8.615   71.732  174.209 1.00 57.70  ? 237 LYS C CD    1 
ATOM   9492  C CE    . LYS C  1 237 ? 9.598   72.640  174.931 1.00 56.54  ? 237 LYS C CE    1 
ATOM   9493  N NZ    . LYS C  1 237 ? 10.701  71.869  175.571 1.00 61.25  ? 237 LYS C NZ    1 
ATOM   9494  N N     . LEU C  1 238 ? 5.257   71.987  176.103 1.00 48.56  ? 238 LEU C N     1 
ATOM   9495  C CA    . LEU C  1 238 ? 4.692   73.009  176.977 1.00 48.26  ? 238 LEU C CA    1 
ATOM   9496  C C     . LEU C  1 238 ? 5.371   74.342  176.680 1.00 52.80  ? 238 LEU C C     1 
ATOM   9497  O O     . LEU C  1 238 ? 6.570   74.388  176.403 1.00 48.45  ? 238 LEU C O     1 
ATOM   9498  C CB    . LEU C  1 238 ? 4.845   72.618  178.446 1.00 48.69  ? 238 LEU C CB    1 
ATOM   9499  C CG    . LEU C  1 238 ? 4.135   71.315  178.824 1.00 50.68  ? 238 LEU C CG    1 
ATOM   9500  C CD1   . LEU C  1 238 ? 4.347   70.985  180.291 1.00 49.70  ? 238 LEU C CD1   1 
ATOM   9501  C CD2   . LEU C  1 238 ? 2.648   71.399  178.496 1.00 43.89  ? 238 LEU C CD2   1 
ATOM   9502  N N     . LEU C  1 239 ? 4.601   75.424  176.731 1.00 51.91  ? 239 LEU C N     1 
ATOM   9503  C CA    . LEU C  1 239 ? 5.067   76.712  176.233 1.00 51.65  ? 239 LEU C CA    1 
ATOM   9504  C C     . LEU C  1 239 ? 5.186   77.763  177.333 1.00 53.80  ? 239 LEU C C     1 
ATOM   9505  O O     . LEU C  1 239 ? 4.300   77.888  178.177 1.00 57.41  ? 239 LEU C O     1 
ATOM   9506  C CB    . LEU C  1 239 ? 4.126   77.205  175.130 1.00 51.63  ? 239 LEU C CB    1 
ATOM   9507  C CG    . LEU C  1 239 ? 3.843   76.156  174.050 1.00 50.58  ? 239 LEU C CG    1 
ATOM   9508  C CD1   . LEU C  1 239 ? 2.592   76.496  173.272 1.00 44.93  ? 239 LEU C CD1   1 
ATOM   9509  C CD2   . LEU C  1 239 ? 5.033   76.008  173.109 1.00 48.20  ? 239 LEU C CD2   1 
ATOM   9510  N N     . PRO C  1 240 ? 6.295   78.521  177.325 1.00 53.84  ? 240 PRO C N     1 
ATOM   9511  C CA    . PRO C  1 240 ? 6.560   79.563  178.323 1.00 53.70  ? 240 PRO C CA    1 
ATOM   9512  C C     . PRO C  1 240 ? 5.487   80.649  178.364 1.00 55.12  ? 240 PRO C C     1 
ATOM   9513  O O     . PRO C  1 240 ? 5.147   81.235  177.336 1.00 51.50  ? 240 PRO C O     1 
ATOM   9514  C CB    . PRO C  1 240 ? 7.899   80.148  177.866 1.00 52.77  ? 240 PRO C CB    1 
ATOM   9515  C CG    . PRO C  1 240 ? 8.551   79.042  177.115 1.00 53.48  ? 240 PRO C CG    1 
ATOM   9516  C CD    . PRO C  1 240 ? 7.429   78.351  176.401 1.00 53.66  ? 240 PRO C CD    1 
ATOM   9517  N N     . VAL C  1 241 ? 4.959   80.902  179.555 1.00 56.30  ? 241 VAL C N     1 
ATOM   9518  C CA    . VAL C  1 241 ? 4.020   81.994  179.773 1.00 59.62  ? 241 VAL C CA    1 
ATOM   9519  C C     . VAL C  1 241 ? 4.496   82.793  180.984 1.00 57.50  ? 241 VAL C C     1 
ATOM   9520  O O     . VAL C  1 241 ? 5.113   82.231  181.887 1.00 61.66  ? 241 VAL C O     1 
ATOM   9521  C CB    . VAL C  1 241 ? 2.574   81.479  179.988 1.00 57.63  ? 241 VAL C CB    1 
ATOM   9522  C CG1   . VAL C  1 241 ? 2.039   80.844  178.713 1.00 57.93  ? 241 VAL C CG1   1 
ATOM   9523  C CG2   . VAL C  1 241 ? 2.513   80.494  181.146 1.00 56.18  ? 241 VAL C CG2   1 
ATOM   9524  N N     . PRO C  1 242 ? 4.230   84.109  181.008 1.00 61.73  ? 242 PRO C N     1 
ATOM   9525  C CA    . PRO C  1 242 ? 4.681   84.869  182.179 1.00 63.89  ? 242 PRO C CA    1 
ATOM   9526  C C     . PRO C  1 242 ? 3.865   84.516  183.419 1.00 64.98  ? 242 PRO C C     1 
ATOM   9527  O O     . PRO C  1 242 ? 2.756   83.999  183.286 1.00 65.66  ? 242 PRO C O     1 
ATOM   9528  C CB    . PRO C  1 242 ? 4.453   86.334  181.775 1.00 64.67  ? 242 PRO C CB    1 
ATOM   9529  C CG    . PRO C  1 242 ? 3.825   86.309  180.401 1.00 67.46  ? 242 PRO C CG    1 
ATOM   9530  C CD    . PRO C  1 242 ? 3.376   84.914  180.120 1.00 62.93  ? 242 PRO C CD    1 
ATOM   9531  N N     . GLU C  1 243 ? 4.404   84.796  184.602 1.00 62.70  ? 243 GLU C N     1 
ATOM   9532  C CA    . GLU C  1 243 ? 3.694   84.522  185.848 1.00 65.30  ? 243 GLU C CA    1 
ATOM   9533  C C     . GLU C  1 243 ? 2.451   85.402  185.971 1.00 64.79  ? 243 GLU C C     1 
ATOM   9534  O O     . GLU C  1 243 ? 1.536   85.096  186.735 1.00 69.38  ? 243 GLU C O     1 
ATOM   9535  C CB    . GLU C  1 243 ? 4.614   84.730  187.050 1.00 67.08  ? 243 GLU C CB    1 
ATOM   9536  C CG    . GLU C  1 243 ? 5.823   83.803  187.078 1.00 65.50  ? 243 GLU C CG    1 
ATOM   9537  C CD    . GLU C  1 243 ? 5.626   82.613  187.996 1.00 72.58  ? 243 GLU C CD    1 
ATOM   9538  O OE1   . GLU C  1 243 ? 4.536   82.492  188.593 1.00 75.26  ? 243 GLU C OE1   1 
ATOM   9539  O OE2   . GLU C  1 243 ? 6.567   81.801  188.127 1.00 78.02  ? 243 GLU C OE2   1 
ATOM   9540  N N     . LYS C  1 244 ? 2.428   86.499  185.218 1.00 61.45  ? 244 LYS C N     1 
ATOM   9541  C CA    . LYS C  1 244 ? 1.246   87.353  185.133 1.00 66.84  ? 244 LYS C CA    1 
ATOM   9542  C C     . LYS C  1 244 ? 0.929   87.730  183.692 1.00 63.85  ? 244 LYS C C     1 
ATOM   9543  O O     . LYS C  1 244 ? 1.801   88.172  182.943 1.00 64.09  ? 244 LYS C O     1 
ATOM   9544  C CB    . LYS C  1 244 ? 1.420   88.624  185.965 1.00 70.20  ? 244 LYS C CB    1 
ATOM   9545  C CG    . LYS C  1 244 ? 1.459   88.388  187.460 1.00 77.94  ? 244 LYS C CG    1 
ATOM   9546  C CD    . LYS C  1 244 ? 1.231   89.673  188.244 1.00 87.28  ? 244 LYS C CD    1 
ATOM   9547  C CE    . LYS C  1 244 ? -0.216  89.801  188.700 1.00 97.35  ? 244 LYS C CE    1 
ATOM   9548  N NZ    . LYS C  1 244 ? -0.314  90.460  190.034 1.00 98.76  ? 244 LYS C NZ    1 
ATOM   9549  N N     . VAL C  1 245 ? -0.333  87.554  183.316 1.00 61.43  ? 245 VAL C N     1 
ATOM   9550  C CA    . VAL C  1 245 ? -0.813  87.959  182.003 1.00 63.67  ? 245 VAL C CA    1 
ATOM   9551  C C     . VAL C  1 245 ? -1.980  88.921  182.173 1.00 60.80  ? 245 VAL C C     1 
ATOM   9552  O O     . VAL C  1 245 ? -2.496  89.085  183.278 1.00 61.07  ? 245 VAL C O     1 
ATOM   9553  C CB    . VAL C  1 245 ? -1.257  86.753  181.157 1.00 64.26  ? 245 VAL C CB    1 
ATOM   9554  C CG1   . VAL C  1 245 ? -0.121  85.756  181.025 1.00 58.09  ? 245 VAL C CG1   1 
ATOM   9555  C CG2   . VAL C  1 245 ? -2.472  86.091  181.777 1.00 59.07  ? 245 VAL C CG2   1 
ATOM   9556  N N     . THR C  1 246 ? -2.396  89.553  181.082 1.00 57.75  ? 246 THR C N     1 
ATOM   9557  C CA    . THR C  1 246 ? -3.471  90.533  181.144 1.00 61.55  ? 246 THR C CA    1 
ATOM   9558  C C     . THR C  1 246 ? -4.593  90.181  180.177 1.00 60.44  ? 246 THR C C     1 
ATOM   9559  O O     . THR C  1 246 ? -4.350  89.900  179.004 1.00 59.74  ? 246 THR C O     1 
ATOM   9560  C CB    . THR C  1 246 ? -2.962  91.955  180.828 1.00 62.88  ? 246 THR C CB    1 
ATOM   9561  O OG1   . THR C  1 246 ? -1.848  92.267  181.673 1.00 61.74  ? 246 THR C OG1   1 
ATOM   9562  C CG2   . THR C  1 246 ? -4.065  92.979  181.050 1.00 61.54  ? 246 THR C CG2   1 
ATOM   9563  N N     . VAL C  1 247 ? -5.821  90.190  180.680 1.00 59.80  ? 247 VAL C N     1 
ATOM   9564  C CA    . VAL C  1 247 ? -6.983  89.994  179.828 1.00 66.41  ? 247 VAL C CA    1 
ATOM   9565  C C     . VAL C  1 247 ? -8.029  91.070  180.076 1.00 65.97  ? 247 VAL C C     1 
ATOM   9566  O O     . VAL C  1 247 ? -7.996  91.767  181.092 1.00 66.60  ? 247 VAL C O     1 
ATOM   9567  C CB    . VAL C  1 247 ? -7.632  88.613  180.047 1.00 64.71  ? 247 VAL C CB    1 
ATOM   9568  C CG1   . VAL C  1 247 ? -6.799  87.521  179.399 1.00 66.07  ? 247 VAL C CG1   1 
ATOM   9569  C CG2   . VAL C  1 247 ? -7.834  88.347  181.534 1.00 61.98  ? 247 VAL C CG2   1 
ATOM   9570  N N     . PHE C  1 248 ? -8.947  91.212  179.127 1.00 65.84  ? 248 PHE C N     1 
ATOM   9571  C CA    . PHE C  1 248 ? -10.141 92.013  179.339 1.00 69.14  ? 248 PHE C CA    1 
ATOM   9572  C C     . PHE C  1 248 ? -11.277 91.518  178.458 1.00 72.89  ? 248 PHE C C     1 
ATOM   9573  O O     . PHE C  1 248 ? -11.069 91.134  177.306 1.00 69.61  ? 248 PHE C O     1 
ATOM   9574  C CB    . PHE C  1 248 ? -9.879  93.500  179.078 1.00 69.75  ? 248 PHE C CB    1 
ATOM   9575  C CG    . PHE C  1 248 ? -9.290  93.799  177.727 1.00 64.60  ? 248 PHE C CG    1 
ATOM   9576  C CD1   . PHE C  1 248 ? -10.102 93.948  176.613 1.00 64.78  ? 248 PHE C CD1   1 
ATOM   9577  C CD2   . PHE C  1 248 ? -7.924  93.964  177.580 1.00 62.66  ? 248 PHE C CD2   1 
ATOM   9578  C CE1   . PHE C  1 248 ? -9.559  94.233  175.374 1.00 61.29  ? 248 PHE C CE1   1 
ATOM   9579  C CE2   . PHE C  1 248 ? -7.376  94.252  176.346 1.00 61.38  ? 248 PHE C CE2   1 
ATOM   9580  C CZ    . PHE C  1 248 ? -8.195  94.387  175.242 1.00 63.86  ? 248 PHE C CZ    1 
ATOM   9581  N N     . ARG C  1 249 ? -12.477 91.513  179.022 1.00 73.61  ? 249 ARG C N     1 
ATOM   9582  C CA    . ARG C  1 249 ? -13.684 91.217  178.269 1.00 74.55  ? 249 ARG C CA    1 
ATOM   9583  C C     . ARG C  1 249 ? -14.625 92.407  178.391 1.00 72.63  ? 249 ARG C C     1 
ATOM   9584  O O     . ARG C  1 249 ? -15.294 92.579  179.408 1.00 75.16  ? 249 ARG C O     1 
ATOM   9585  C CB    . ARG C  1 249 ? -14.349 89.935  178.773 1.00 81.50  ? 249 ARG C CB    1 
ATOM   9586  C CG    . ARG C  1 249 ? -15.647 89.596  178.068 1.00 75.41  ? 249 ARG C CG    1 
ATOM   9587  C CD    . ARG C  1 249 ? -16.098 88.180  178.375 1.00 81.90  ? 249 ARG C CD    1 
ATOM   9588  N NE    . ARG C  1 249 ? -16.322 87.967  179.801 1.00 86.28  ? 249 ARG C NE    1 
ATOM   9589  C CZ    . ARG C  1 249 ? -15.942 86.875  180.455 1.00 86.83  ? 249 ARG C CZ    1 
ATOM   9590  N NH1   . ARG C  1 249 ? -16.185 86.755  181.753 1.00 83.38  ? 249 ARG C NH1   1 
ATOM   9591  N NH2   . ARG C  1 249 ? -15.314 85.904  179.808 1.00 99.64  ? 249 ARG C NH2   1 
ATOM   9592  N N     . VAL C  1 250 ? -14.656 93.235  177.354 1.00 69.21  ? 250 VAL C N     1 
ATOM   9593  C CA    . VAL C  1 250 ? -15.402 94.486  177.389 1.00 68.97  ? 250 VAL C CA    1 
ATOM   9594  C C     . VAL C  1 250 ? -16.421 94.562  176.258 1.00 68.74  ? 250 VAL C C     1 
ATOM   9595  O O     . VAL C  1 250 ? -16.060 94.553  175.083 1.00 69.26  ? 250 VAL C O     1 
ATOM   9596  C CB    . VAL C  1 250 ? -14.454 95.700  177.307 1.00 72.07  ? 250 VAL C CB    1 
ATOM   9597  C CG1   . VAL C  1 250 ? -15.241 96.983  177.077 1.00 73.48  ? 250 VAL C CG1   1 
ATOM   9598  C CG2   . VAL C  1 250 ? -13.607 95.792  178.572 1.00 70.29  ? 250 VAL C CG2   1 
ATOM   9599  N N     . THR C  1 251 ? -17.697 94.637  176.620 1.00 68.36  ? 251 THR C N     1 
ATOM   9600  C CA    . THR C  1 251 ? -18.764 94.675  175.628 1.00 66.24  ? 251 THR C CA    1 
ATOM   9601  C C     . THR C  1 251 ? -19.231 96.107  175.373 1.00 70.43  ? 251 THR C C     1 
ATOM   9602  O O     . THR C  1 251 ? -19.468 96.860  176.315 1.00 70.15  ? 251 THR C O     1 
ATOM   9603  C CB    . THR C  1 251 ? -19.964 93.814  176.072 1.00 66.40  ? 251 THR C CB    1 
ATOM   9604  O OG1   . THR C  1 251 ? -19.523 92.474  176.327 1.00 71.29  ? 251 THR C OG1   1 
ATOM   9605  C CG2   . THR C  1 251 ? -21.037 93.791  174.995 1.00 71.16  ? 251 THR C CG2   1 
ATOM   9606  N N     . LYS C  1 252 ? -19.354 96.484  174.103 1.00 70.32  ? 252 LYS C N     1 
ATOM   9607  C CA    . LYS C  1 252 ? -19.851 97.814  173.754 1.00 70.98  ? 252 LYS C CA    1 
ATOM   9608  C C     . LYS C  1 252 ? -21.243 97.749  173.126 1.00 75.20  ? 252 LYS C C     1 
ATOM   9609  O O     . LYS C  1 252 ? -21.425 97.164  172.057 1.00 72.02  ? 252 LYS C O     1 
ATOM   9610  C CB    . LYS C  1 252 ? -18.884 98.529  172.803 1.00 72.42  ? 252 LYS C CB    1 
ATOM   9611  C CG    . LYS C  1 252 ? -17.491 98.754  173.368 1.00 72.00  ? 252 LYS C CG    1 
ATOM   9612  C CD    . LYS C  1 252 ? -16.830 99.964  172.733 1.00 69.91  ? 252 LYS C CD    1 
ATOM   9613  C CE    . LYS C  1 252 ? -17.024 101.204 173.590 1.00 76.41  ? 252 LYS C CE    1 
ATOM   9614  N NZ    . LYS C  1 252 ? -16.200 101.144 174.831 1.00 77.53  ? 252 LYS C NZ    1 
ATOM   9615  N N     . ASN C  1 253 ? -22.219 98.351  173.804 1.00 77.37  ? 253 ASN C N     1 
ATOM   9616  C CA    . ASN C  1 253 ? -23.586 98.444  173.293 1.00 71.98  ? 253 ASN C CA    1 
ATOM   9617  C C     . ASN C  1 253 ? -23.760 99.725  172.482 1.00 70.74  ? 253 ASN C C     1 
ATOM   9618  O O     . ASN C  1 253 ? -23.680 100.830 173.020 1.00 71.41  ? 253 ASN C O     1 
ATOM   9619  C CB    . ASN C  1 253 ? -24.590 98.380  174.442 1.00 78.99  ? 253 ASN C CB    1 
ATOM   9620  C CG    . ASN C  1 253 ? -24.566 97.043  175.158 1.00 83.09  ? 253 ASN C CG    1 
ATOM   9621  O OD1   . ASN C  1 253 ? -25.267 96.106  174.774 1.00 89.62  ? 253 ASN C OD1   1 
ATOM   9622  N ND2   . ASN C  1 253 ? -23.750 96.945  176.202 1.00 72.97  ? 253 ASN C ND2   1 
ATOM   9623  N N     . VAL C  1 254 ? -23.997 99.561  171.182 1.00 69.91  ? 254 VAL C N     1 
ATOM   9624  C CA    . VAL C  1 254 ? -23.704 100.588 170.182 1.00 71.81  ? 254 VAL C CA    1 
ATOM   9625  C C     . VAL C  1 254 ? -24.671 100.472 168.983 1.00 76.28  ? 254 VAL C C     1 
ATOM   9626  O O     . VAL C  1 254 ? -25.361 99.463  168.852 1.00 80.61  ? 254 VAL C O     1 
ATOM   9627  C CB    . VAL C  1 254 ? -22.204 100.451 169.734 1.00 73.70  ? 254 VAL C CB    1 
ATOM   9628  C CG1   . VAL C  1 254 ? -21.878 101.247 168.498 1.00 71.52  ? 254 VAL C CG1   1 
ATOM   9629  C CG2   . VAL C  1 254 ? -21.250 100.832 170.873 1.00 72.87  ? 254 VAL C CG2   1 
ATOM   9630  N N     . ALA C  1 255 ? -24.761 101.508 168.146 1.00 73.79  ? 255 ALA C N     1 
ATOM   9631  C CA    . ALA C  1 255 ? -25.489 101.427 166.878 1.00 74.82  ? 255 ALA C CA    1 
ATOM   9632  C C     . ALA C  1 255 ? -24.618 100.877 165.740 1.00 70.47  ? 255 ALA C C     1 
ATOM   9633  O O     . ALA C  1 255 ? -23.393 100.831 165.848 1.00 73.90  ? 255 ALA C O     1 
ATOM   9634  C CB    . ALA C  1 255 ? -26.040 102.791 166.503 1.00 70.82  ? 255 ALA C CB    1 
ATOM   9635  N N     . ILE C  1 256 ? -25.269 100.484 164.646 1.00 69.89  ? 256 ILE C N     1 
ATOM   9636  C CA    . ILE C  1 256 ? -24.620 99.801  163.524 1.00 71.56  ? 256 ILE C CA    1 
ATOM   9637  C C     . ILE C  1 256 ? -23.493 100.611 162.875 1.00 72.41  ? 256 ILE C C     1 
ATOM   9638  O O     . ILE C  1 256 ? -22.511 100.044 162.395 1.00 71.84  ? 256 ILE C O     1 
ATOM   9639  C CB    . ILE C  1 256 ? -25.668 99.420  162.431 1.00 74.11  ? 256 ILE C CB    1 
ATOM   9640  C CG1   . ILE C  1 256 ? -25.021 98.643  161.275 1.00 69.08  ? 256 ILE C CG1   1 
ATOM   9641  C CG2   . ILE C  1 256 ? -26.390 100.657 161.914 1.00 74.02  ? 256 ILE C CG2   1 
ATOM   9642  C CD1   . ILE C  1 256 ? -26.021 98.009  160.314 1.00 72.96  ? 256 ILE C CD1   1 
ATOM   9643  N N     . ASP C  1 257 ? -23.621 101.934 162.883 1.00 68.84  ? 257 ASP C N     1 
ATOM   9644  C CA    . ASP C  1 257 ? -22.649 102.797 162.218 1.00 73.18  ? 257 ASP C CA    1 
ATOM   9645  C C     . ASP C  1 257 ? -21.316 102.858 162.962 1.00 67.83  ? 257 ASP C C     1 
ATOM   9646  O O     . ASP C  1 257 ? -20.254 102.808 162.342 1.00 61.60  ? 257 ASP C O     1 
ATOM   9647  C CB    . ASP C  1 257 ? -23.220 104.206 162.049 1.00 74.08  ? 257 ASP C CB    1 
ATOM   9648  C CG    . ASP C  1 257 ? -24.441 104.231 161.151 1.00 78.40  ? 257 ASP C CG    1 
ATOM   9649  O OD1   . ASP C  1 257 ? -24.269 104.252 159.913 1.00 74.30  ? 257 ASP C OD1   1 
ATOM   9650  O OD2   . ASP C  1 257 ? -25.571 104.228 161.682 1.00 75.50  ? 257 ASP C OD2   1 
ATOM   9651  N N     . GLU C  1 258 ? -21.369 102.973 164.284 1.00 68.98  ? 258 GLU C N     1 
ATOM   9652  C CA    . GLU C  1 258 ? -20.148 102.973 165.080 1.00 69.10  ? 258 GLU C CA    1 
ATOM   9653  C C     . GLU C  1 258 ? -19.602 101.547 165.145 1.00 67.94  ? 258 GLU C C     1 
ATOM   9654  O O     . GLU C  1 258 ? -18.389 101.339 165.119 1.00 61.44  ? 258 GLU C O     1 
ATOM   9655  C CB    . GLU C  1 258 ? -20.411 103.549 166.476 1.00 68.51  ? 258 GLU C CB    1 
ATOM   9656  C CG    . GLU C  1 258 ? -19.250 103.475 167.468 1.00 70.63  ? 258 GLU C CG    1 
ATOM   9657  C CD    . GLU C  1 258 ? -19.667 103.900 168.869 1.00 75.93  ? 258 GLU C CD    1 
ATOM   9658  O OE1   . GLU C  1 258 ? -20.817 104.363 169.027 1.00 76.87  ? 258 GLU C OE1   1 
ATOM   9659  O OE2   . GLU C  1 258 ? -18.857 103.770 169.811 1.00 69.91  ? 258 GLU C OE2   1 
ATOM   9660  N N     . ALA C  1 259 ? -20.507 100.571 165.198 1.00 69.11  ? 259 ALA C N     1 
ATOM   9661  C CA    . ALA C  1 259 ? -20.138 99.157  165.144 1.00 64.47  ? 259 ALA C CA    1 
ATOM   9662  C C     . ALA C  1 259 ? -19.326 98.846  163.890 1.00 62.27  ? 259 ALA C C     1 
ATOM   9663  O O     . ALA C  1 259 ? -18.276 98.208  163.960 1.00 65.24  ? 259 ALA C O     1 
ATOM   9664  C CB    . ALA C  1 259 ? -21.382 98.279  165.196 1.00 67.45  ? 259 ALA C CB    1 
ATOM   9665  N N     . THR C  1 260 ? -19.823 99.312  162.748 1.00 60.33  ? 260 THR C N     1 
ATOM   9666  C CA    . THR C  1 260 ? -19.162 99.114  161.462 1.00 63.60  ? 260 THR C CA    1 
ATOM   9667  C C     . THR C  1 260 ? -17.764 99.737  161.427 1.00 67.55  ? 260 THR C C     1 
ATOM   9668  O O     . THR C  1 260 ? -16.818 99.127  160.931 1.00 66.45  ? 260 THR C O     1 
ATOM   9669  C CB    . THR C  1 260 ? -20.005 99.700  160.314 1.00 64.63  ? 260 THR C CB    1 
ATOM   9670  O OG1   . THR C  1 260 ? -21.290 99.065  160.292 1.00 69.62  ? 260 THR C OG1   1 
ATOM   9671  C CG2   . THR C  1 260 ? -19.316 99.494  158.977 1.00 64.90  ? 260 THR C CG2   1 
ATOM   9672  N N     . SER C  1 261 ? -17.638 100.949 161.960 1.00 62.62  ? 261 SER C N     1 
ATOM   9673  C CA    . SER C  1 261 ? -16.350 101.638 161.985 1.00 67.77  ? 261 SER C CA    1 
ATOM   9674  C C     . SER C  1 261 ? -15.377 100.964 162.949 1.00 59.61  ? 261 SER C C     1 
ATOM   9675  O O     . SER C  1 261 ? -14.170 100.935 162.711 1.00 58.55  ? 261 SER C O     1 
ATOM   9676  C CB    . SER C  1 261 ? -16.530 103.106 162.375 1.00 62.83  ? 261 SER C CB    1 
ATOM   9677  O OG    . SER C  1 261 ? -16.631 103.245 163.782 1.00 62.34  ? 261 SER C OG    1 
ATOM   9678  N N     . LEU C  1 262 ? -15.911 100.435 164.045 1.00 59.60  ? 262 LEU C N     1 
ATOM   9679  C CA    . LEU C  1 262 ? -15.103 99.737  165.040 1.00 62.94  ? 262 LEU C CA    1 
ATOM   9680  C C     . LEU C  1 262 ? -14.484 98.469  164.466 1.00 62.59  ? 262 LEU C C     1 
ATOM   9681  O O     . LEU C  1 262 ? -13.280 98.238  164.591 1.00 62.15  ? 262 LEU C O     1 
ATOM   9682  C CB    . LEU C  1 262 ? -15.948 99.396  166.268 1.00 61.28  ? 262 LEU C CB    1 
ATOM   9683  C CG    . LEU C  1 262 ? -16.168 100.517 167.282 1.00 59.17  ? 262 LEU C CG    1 
ATOM   9684  C CD1   . LEU C  1 262 ? -17.313 100.168 168.213 1.00 59.30  ? 262 LEU C CD1   1 
ATOM   9685  C CD2   . LEU C  1 262 ? -14.891 100.769 168.069 1.00 57.33  ? 262 LEU C CD2   1 
ATOM   9686  N N     . LEU C  1 263 ? -15.320 97.653  163.835 1.00 62.17  ? 263 LEU C N     1 
ATOM   9687  C CA    . LEU C  1 263 ? -14.877 96.388  163.269 1.00 62.46  ? 263 LEU C CA    1 
ATOM   9688  C C     . LEU C  1 263 ? -13.968 96.599  162.063 1.00 63.05  ? 263 LEU C C     1 
ATOM   9689  O O     . LEU C  1 263 ? -13.030 95.832  161.849 1.00 59.00  ? 263 LEU C O     1 
ATOM   9690  C CB    . LEU C  1 263 ? -16.079 95.528  162.877 1.00 59.05  ? 263 LEU C CB    1 
ATOM   9691  C CG    . LEU C  1 263 ? -16.949 94.998  164.020 1.00 60.81  ? 263 LEU C CG    1 
ATOM   9692  C CD1   . LEU C  1 263 ? -17.992 94.030  163.489 1.00 55.69  ? 263 LEU C CD1   1 
ATOM   9693  C CD2   . LEU C  1 263 ? -16.097 94.334  165.091 1.00 62.40  ? 263 LEU C CD2   1 
ATOM   9694  N N     . HIS C  1 264 ? -14.240 97.640  161.280 1.00 58.73  ? 264 HIS C N     1 
ATOM   9695  C CA    . HIS C  1 264 ? -13.397 97.948  160.130 1.00 65.54  ? 264 HIS C CA    1 
ATOM   9696  C C     . HIS C  1 264 ? -12.014 98.383  160.589 1.00 60.51  ? 264 HIS C C     1 
ATOM   9697  O O     . HIS C  1 264 ? -11.036 98.247  159.855 1.00 59.23  ? 264 HIS C O     1 
ATOM   9698  C CB    . HIS C  1 264 ? -14.021 99.035  159.254 1.00 62.68  ? 264 HIS C CB    1 
ATOM   9699  C CG    . HIS C  1 264 ? -13.271 99.281  157.980 1.00 60.96  ? 264 HIS C CG    1 
ATOM   9700  N ND1   . HIS C  1 264 ? -12.228 100.179 157.890 1.00 64.93  ? 264 HIS C ND1   1 
ATOM   9701  C CD2   . HIS C  1 264 ? -13.407 98.739  156.747 1.00 63.42  ? 264 HIS C CD2   1 
ATOM   9702  C CE1   . HIS C  1 264 ? -11.758 100.183 156.656 1.00 63.03  ? 264 HIS C CE1   1 
ATOM   9703  N NE2   . HIS C  1 264 ? -12.455 99.317  155.942 1.00 61.82  ? 264 HIS C NE2   1 
ATOM   9704  N N     . LYS C  1 265 ? -11.934 98.911  161.805 1.00 59.46  ? 265 LYS C N     1 
ATOM   9705  C CA    . LYS C  1 265 ? -10.643 99.229  162.391 1.00 64.02  ? 265 LYS C CA    1 
ATOM   9706  C C     . LYS C  1 265 ? -10.053 97.991  163.059 1.00 60.78  ? 265 LYS C C     1 
ATOM   9707  O O     . LYS C  1 265 ? -8.851  97.739  162.949 1.00 57.49  ? 265 LYS C O     1 
ATOM   9708  C CB    . LYS C  1 265 ? -10.753 100.373 163.401 1.00 57.75  ? 265 LYS C CB    1 
ATOM   9709  C CG    . LYS C  1 265 ? -9.401  100.798 163.947 1.00 61.32  ? 265 LYS C CG    1 
ATOM   9710  C CD    . LYS C  1 265 ? -9.498  101.808 165.074 1.00 69.69  ? 265 LYS C CD    1 
ATOM   9711  C CE    . LYS C  1 265 ? -8.111  102.063 165.645 1.00 70.68  ? 265 LYS C CE    1 
ATOM   9712  N NZ    . LYS C  1 265 ? -8.054  103.164 166.642 1.00 72.10  ? 265 LYS C NZ    1 
ATOM   9713  N N     . TRP C  1 266 ? -10.903 97.213  163.731 1.00 65.27  ? 266 TRP C N     1 
ATOM   9714  C CA    . TRP C  1 266 ? -10.450 96.026  164.457 1.00 64.97  ? 266 TRP C CA    1 
ATOM   9715  C C     . TRP C  1 266 ? -9.768  94.989  163.556 1.00 62.92  ? 266 TRP C C     1 
ATOM   9716  O O     . TRP C  1 266 ? -9.009  94.156  164.042 1.00 67.39  ? 266 TRP C O     1 
ATOM   9717  C CB    . TRP C  1 266 ? -11.617 95.347  165.207 1.00 60.60  ? 266 TRP C CB    1 
ATOM   9718  C CG    . TRP C  1 266 ? -11.219 93.981  165.708 1.00 60.91  ? 266 TRP C CG    1 
ATOM   9719  C CD1   . TRP C  1 266 ? -10.684 93.674  166.926 1.00 58.84  ? 266 TRP C CD1   1 
ATOM   9720  C CD2   . TRP C  1 266 ? -11.255 92.753  164.967 1.00 58.99  ? 266 TRP C CD2   1 
ATOM   9721  N NE1   . TRP C  1 266 ? -10.404 92.329  166.995 1.00 56.59  ? 266 TRP C NE1   1 
ATOM   9722  C CE2   . TRP C  1 266 ? -10.739 91.744  165.803 1.00 59.14  ? 266 TRP C CE2   1 
ATOM   9723  C CE3   . TRP C  1 266 ? -11.665 92.414  163.673 1.00 60.25  ? 266 TRP C CE3   1 
ATOM   9724  C CZ2   . TRP C  1 266 ? -10.642 90.416  165.394 1.00 51.67  ? 266 TRP C CZ2   1 
ATOM   9725  C CZ3   . TRP C  1 266 ? -11.564 91.099  163.269 1.00 59.49  ? 266 TRP C CZ3   1 
ATOM   9726  C CH2   . TRP C  1 266 ? -11.051 90.117  164.125 1.00 47.67  ? 266 TRP C CH2   1 
ATOM   9727  N N     . GLN C  1 267 ? -10.035 95.017  162.254 1.00 58.84  ? 267 GLN C N     1 
ATOM   9728  C CA    . GLN C  1 267 ? -9.484  93.994  161.362 1.00 60.12  ? 267 GLN C CA    1 
ATOM   9729  C C     . GLN C  1 267 ? -7.989  94.250  161.135 1.00 62.65  ? 267 GLN C C     1 
ATOM   9730  O O     . GLN C  1 267 ? -7.176  93.321  161.116 1.00 61.79  ? 267 GLN C O     1 
ATOM   9731  C CB    . GLN C  1 267 ? -10.249 93.955  160.040 1.00 57.64  ? 267 GLN C CB    1 
ATOM   9732  C CG    . GLN C  1 267 ? -9.986  95.125  159.128 1.00 57.58  ? 267 GLN C CG    1 
ATOM   9733  C CD    . GLN C  1 267 ? -10.704 95.017  157.808 1.00 64.61  ? 267 GLN C CD    1 
ATOM   9734  O OE1   . GLN C  1 267 ? -10.605 94.006  157.111 1.00 58.10  ? 267 GLN C OE1   1 
ATOM   9735  N NE2   . GLN C  1 267 ? -11.442 96.062  157.455 1.00 61.39  ? 267 GLN C NE2   1 
ATOM   9736  N N     . PHE C  1 268 ? -7.636  95.526  160.993 1.00 59.04  ? 268 PHE C N     1 
ATOM   9737  C CA    . PHE C  1 268 ? -6.278  95.994  161.224 1.00 62.66  ? 268 PHE C CA    1 
ATOM   9738  C C     . PHE C  1 268 ? -6.093  95.936  162.743 1.00 63.86  ? 268 PHE C C     1 
ATOM   9739  O O     . PHE C  1 268 ? -6.941  95.364  163.420 1.00 70.76  ? 268 PHE C O     1 
ATOM   9740  C CB    . PHE C  1 268 ? -6.096  97.389  160.644 1.00 60.66  ? 268 PHE C CB    1 
ATOM   9741  C CG    . PHE C  1 268 ? -6.690  97.541  159.259 1.00 62.69  ? 268 PHE C CG    1 
ATOM   9742  C CD1   . PHE C  1 268 ? -6.052  97.009  158.145 1.00 62.98  ? 268 PHE C CD1   1 
ATOM   9743  C CD2   . PHE C  1 268 ? -7.899  98.191  159.077 1.00 59.13  ? 268 PHE C CD2   1 
ATOM   9744  C CE1   . PHE C  1 268 ? -6.607  97.137  156.875 1.00 64.59  ? 268 PHE C CE1   1 
ATOM   9745  C CE2   . PHE C  1 268 ? -8.457  98.323  157.815 1.00 61.07  ? 268 PHE C CE2   1 
ATOM   9746  C CZ    . PHE C  1 268 ? -7.811  97.796  156.711 1.00 58.26  ? 268 PHE C CZ    1 
ATOM   9747  N N     . VAL C  1 269 ? -5.023  96.485  163.301 1.00 62.11  ? 269 VAL C N     1 
ATOM   9748  C CA    . VAL C  1 269 ? -4.742  96.214  164.711 1.00 65.25  ? 269 VAL C CA    1 
ATOM   9749  C C     . VAL C  1 269 ? -4.622  94.689  164.920 1.00 64.00  ? 269 VAL C C     1 
ATOM   9750  O O     . VAL C  1 269 ? -3.520  94.156  164.858 1.00 64.74  ? 269 VAL C O     1 
ATOM   9751  C CB    . VAL C  1 269 ? -5.820  96.831  165.658 1.00 56.07  ? 269 VAL C CB    1 
ATOM   9752  C CG1   . VAL C  1 269 ? -5.404  96.722  167.094 1.00 56.67  ? 269 VAL C CG1   1 
ATOM   9753  C CG2   . VAL C  1 269 ? -6.055  98.277  165.288 1.00 65.97  ? 269 VAL C CG2   1 
ATOM   9754  N N     . ALA C  1 270 ? -5.749  93.996  165.109 1.00 66.23  ? 270 ALA C N     1 
ATOM   9755  C CA    . ALA C  1 270 ? -5.780  92.552  165.441 1.00 63.99  ? 270 ALA C CA    1 
ATOM   9756  C C     . ALA C  1 270 ? -4.810  91.674  164.656 1.00 66.14  ? 270 ALA C C     1 
ATOM   9757  O O     . ALA C  1 270 ? -4.128  90.814  165.227 1.00 61.22  ? 270 ALA C O     1 
ATOM   9758  C CB    . ALA C  1 270 ? -7.178  92.014  165.275 1.00 60.66  ? 270 ALA C CB    1 
ATOM   9759  N N     . GLU C  1 271 ? -4.774  91.884  163.348 1.00 65.10  ? 271 GLU C N     1 
ATOM   9760  C CA    . GLU C  1 271 ? -3.845  91.185  162.483 1.00 68.20  ? 271 GLU C CA    1 
ATOM   9761  C C     . GLU C  1 271 ? -2.428  91.741  162.637 1.00 71.12  ? 271 GLU C C     1 
ATOM   9762  O O     . GLU C  1 271 ? -1.449  91.038  162.385 1.00 66.30  ? 271 GLU C O     1 
ATOM   9763  C CB    . GLU C  1 271 ? -4.302  91.295  161.032 1.00 70.08  ? 271 GLU C CB    1 
ATOM   9764  C CG    . GLU C  1 271 ? -3.563  90.379  160.081 1.00 68.32  ? 271 GLU C CG    1 
ATOM   9765  C CD    . GLU C  1 271 ? -3.619  90.873  158.656 1.00 82.78  ? 271 GLU C CD    1 
ATOM   9766  O OE1   . GLU C  1 271 ? -4.495  91.710  158.345 1.00 89.88  ? 271 GLU C OE1   1 
ATOM   9767  O OE2   . GLU C  1 271 ? -2.771  90.438  157.850 1.00 79.00  ? 271 GLU C OE2   1 
ATOM   9768  N N     . GLU C  1 272 ? -2.317  92.998  163.060 1.00 69.22  ? 272 GLU C N     1 
ATOM   9769  C CA    . GLU C  1 272 ? -1.020  93.672  163.083 1.00 66.31  ? 272 GLU C CA    1 
ATOM   9770  C C     . GLU C  1 272 ? -0.401  93.830  164.472 1.00 68.52  ? 272 GLU C C     1 
ATOM   9771  O O     . GLU C  1 272 ? 0.742   94.277  164.579 1.00 75.04  ? 272 GLU C O     1 
ATOM   9772  C CB    . GLU C  1 272 ? -1.138  95.053  162.435 1.00 66.28  ? 272 GLU C CB    1 
ATOM   9773  C CG    . GLU C  1 272 ? -1.268  95.016  160.925 1.00 69.18  ? 272 GLU C CG    1 
ATOM   9774  C CD    . GLU C  1 272 ? -1.890  96.280  160.365 1.00 82.37  ? 272 GLU C CD    1 
ATOM   9775  O OE1   . GLU C  1 272 ? -1.925  97.300  161.087 1.00 82.13  ? 272 GLU C OE1   1 
ATOM   9776  O OE2   . GLU C  1 272 ? -2.355  96.252  159.206 1.00 83.25  ? 272 GLU C OE2   1 
ATOM   9777  N N     . LEU C  1 273 ? -1.133  93.486  165.530 1.00 65.54  ? 273 LEU C N     1 
ATOM   9778  C CA    . LEU C  1 273 ? -0.536  93.507  166.864 1.00 66.13  ? 273 LEU C CA    1 
ATOM   9779  C C     . LEU C  1 273 ? 0.632   92.534  166.886 1.00 68.16  ? 273 LEU C C     1 
ATOM   9780  O O     . LEU C  1 273 ? 0.624   91.526  166.173 1.00 66.29  ? 273 LEU C O     1 
ATOM   9781  C CB    . LEU C  1 273 ? -1.552  93.143  167.961 1.00 65.69  ? 273 LEU C CB    1 
ATOM   9782  C CG    . LEU C  1 273 ? -2.603  94.166  168.432 1.00 64.61  ? 273 LEU C CG    1 
ATOM   9783  C CD1   . LEU C  1 273 ? -3.962  93.723  167.996 1.00 59.83  ? 273 LEU C CD1   1 
ATOM   9784  C CD2   . LEU C  1 273 ? -2.622  94.378  169.936 1.00 58.66  ? 273 LEU C CD2   1 
ATOM   9785  N N     . GLU C  1 274 ? 1.645   92.844  167.687 1.00 68.33  ? 274 GLU C N     1 
ATOM   9786  C CA    . GLU C  1 274 ? 2.765   91.932  167.877 1.00 69.46  ? 274 GLU C CA    1 
ATOM   9787  C C     . GLU C  1 274 ? 2.264   90.638  168.511 1.00 64.26  ? 274 GLU C C     1 
ATOM   9788  O O     . GLU C  1 274 ? 1.188   90.609  169.107 1.00 61.06  ? 274 GLU C O     1 
ATOM   9789  C CB    . GLU C  1 274 ? 3.854   92.582  168.731 1.00 67.70  ? 274 GLU C CB    1 
ATOM   9790  C CG    . GLU C  1 274 ? 4.646   93.637  167.979 1.00 79.00  ? 274 GLU C CG    1 
ATOM   9791  C CD    . GLU C  1 274 ? 5.142   93.123  166.642 1.00 90.08  ? 274 GLU C CD    1 
ATOM   9792  O OE1   . GLU C  1 274 ? 5.925   92.150  166.637 1.00 90.78  ? 274 GLU C OE1   1 
ATOM   9793  O OE2   . GLU C  1 274 ? 4.739   93.679  165.598 1.00 89.44  ? 274 GLU C OE2   1 
ATOM   9794  N N     . GLU C  1 275 ? 3.046   89.574  168.379 1.00 59.54  ? 275 GLU C N     1 
ATOM   9795  C CA    . GLU C  1 275 ? 2.601   88.229  168.739 1.00 56.57  ? 275 GLU C CA    1 
ATOM   9796  C C     . GLU C  1 275 ? 2.226   88.062  170.212 1.00 56.78  ? 275 GLU C C     1 
ATOM   9797  O O     . GLU C  1 275 ? 1.565   87.091  170.580 1.00 56.87  ? 275 GLU C O     1 
ATOM   9798  C CB    . GLU C  1 275 ? 3.684   87.218  168.377 1.00 55.36  ? 275 GLU C CB    1 
ATOM   9799  C CG    . GLU C  1 275 ? 5.012   87.480  169.052 1.00 60.22  ? 275 GLU C CG    1 
ATOM   9800  C CD    . GLU C  1 275 ? 6.041   86.422  168.724 1.00 57.51  ? 275 GLU C CD    1 
ATOM   9801  O OE1   . GLU C  1 275 ? 6.073   85.963  167.563 1.00 59.01  ? 275 GLU C OE1   1 
ATOM   9802  O OE2   . GLU C  1 275 ? 6.811   86.043  169.630 1.00 60.48  ? 275 GLU C OE2   1 
ATOM   9803  N N     . ASP C  1 276 ? 2.647   89.006  171.049 1.00 56.06  ? 276 ASP C N     1 
ATOM   9804  C CA    . ASP C  1 276 ? 2.359   88.956  172.481 1.00 58.41  ? 276 ASP C CA    1 
ATOM   9805  C C     . ASP C  1 276 ? 0.958   89.470  172.797 1.00 59.52  ? 276 ASP C C     1 
ATOM   9806  O O     . ASP C  1 276 ? 0.553   89.529  173.958 1.00 55.82  ? 276 ASP C O     1 
ATOM   9807  C CB    . ASP C  1 276 ? 3.397   89.768  173.261 1.00 61.05  ? 276 ASP C CB    1 
ATOM   9808  C CG    . ASP C  1 276 ? 4.732   89.060  173.367 1.00 66.53  ? 276 ASP C CG    1 
ATOM   9809  O OD1   . ASP C  1 276 ? 4.735   87.831  173.586 1.00 64.35  ? 276 ASP C OD1   1 
ATOM   9810  O OD2   . ASP C  1 276 ? 5.777   89.730  173.239 1.00 76.05  ? 276 ASP C OD2   1 
ATOM   9811  N N     . PHE C  1 277 ? 0.224   89.842  171.756 1.00 55.01  ? 277 PHE C N     1 
ATOM   9812  C CA    . PHE C  1 277 ? -1.100  90.424  171.919 1.00 58.00  ? 277 PHE C CA    1 
ATOM   9813  C C     . PHE C  1 277 ? -2.156  89.713  171.073 1.00 54.52  ? 277 PHE C C     1 
ATOM   9814  O O     . PHE C  1 277 ? -1.875  89.268  169.960 1.00 54.47  ? 277 PHE C O     1 
ATOM   9815  C CB    . PHE C  1 277 ? -1.081  91.899  171.536 1.00 58.73  ? 277 PHE C CB    1 
ATOM   9816  C CG    . PHE C  1 277 ? -0.384  92.796  172.522 1.00 61.02  ? 277 PHE C CG    1 
ATOM   9817  C CD1   . PHE C  1 277 ? -1.057  93.297  173.626 1.00 59.47  ? 277 PHE C CD1   1 
ATOM   9818  C CD2   . PHE C  1 277 ? 0.933   93.178  172.318 1.00 60.95  ? 277 PHE C CD2   1 
ATOM   9819  C CE1   . PHE C  1 277 ? -0.422  94.141  174.522 1.00 61.22  ? 277 PHE C CE1   1 
ATOM   9820  C CE2   . PHE C  1 277 ? 1.573   94.021  173.209 1.00 61.53  ? 277 PHE C CE2   1 
ATOM   9821  C CZ    . PHE C  1 277 ? 0.895   94.504  174.313 1.00 61.97  ? 277 PHE C CZ    1 
ATOM   9822  N N     . THR C  1 278 ? -3.374  89.629  171.599 1.00 57.01  ? 278 THR C N     1 
ATOM   9823  C CA    . THR C  1 278 ? -4.500  89.098  170.840 1.00 55.59  ? 278 THR C CA    1 
ATOM   9824  C C     . THR C  1 278 ? -5.765  89.890  171.148 1.00 54.23  ? 278 THR C C     1 
ATOM   9825  O O     . THR C  1 278 ? -6.103  90.101  172.312 1.00 52.86  ? 278 THR C O     1 
ATOM   9826  C CB    . THR C  1 278 ? -4.750  87.608  171.141 1.00 51.56  ? 278 THR C CB    1 
ATOM   9827  O OG1   . THR C  1 278 ? -3.589  86.846  170.791 1.00 53.67  ? 278 THR C OG1   1 
ATOM   9828  C CG2   . THR C  1 278 ? -5.949  87.093  170.348 1.00 51.70  ? 278 THR C CG2   1 
ATOM   9829  N N     . LEU C  1 279 ? -6.455  90.336  170.104 1.00 56.99  ? 279 LEU C N     1 
ATOM   9830  C CA    . LEU C  1 279 ? -7.723  91.032  170.271 1.00 56.86  ? 279 LEU C CA    1 
ATOM   9831  C C     . LEU C  1 279 ? -8.808  90.375  169.425 1.00 52.15  ? 279 LEU C C     1 
ATOM   9832  O O     . LEU C  1 279 ? -8.777  90.452  168.199 1.00 53.59  ? 279 LEU C O     1 
ATOM   9833  C CB    . LEU C  1 279 ? -7.588  92.509  169.898 1.00 56.20  ? 279 LEU C CB    1 
ATOM   9834  C CG    . LEU C  1 279 ? -8.856  93.357  170.038 1.00 57.65  ? 279 LEU C CG    1 
ATOM   9835  C CD1   . LEU C  1 279 ? -9.329  93.392  171.484 1.00 53.88  ? 279 LEU C CD1   1 
ATOM   9836  C CD2   . LEU C  1 279 ? -8.628  94.766  169.507 1.00 59.44  ? 279 LEU C CD2   1 
ATOM   9837  N N     . SER C  1 280 ? -9.767  89.734  170.087 1.00 51.74  ? 280 SER C N     1 
ATOM   9838  C CA    . SER C  1 280 ? -10.829 89.015  169.391 1.00 58.78  ? 280 SER C CA    1 
ATOM   9839  C C     . SER C  1 280 ? -12.194 89.645  169.659 1.00 56.71  ? 280 SER C C     1 
ATOM   9840  O O     . SER C  1 280 ? -12.362 90.386  170.627 1.00 58.44  ? 280 SER C O     1 
ATOM   9841  C CB    . SER C  1 280 ? -10.836 87.543  169.806 1.00 52.15  ? 280 SER C CB    1 
ATOM   9842  O OG    . SER C  1 280 ? -9.568  86.947  169.596 1.00 58.88  ? 280 SER C OG    1 
ATOM   9843  N N     . VAL C  1 281 ? -13.166 89.352  168.798 1.00 55.22  ? 281 VAL C N     1 
ATOM   9844  C CA    . VAL C  1 281 ? -14.495 89.944  168.924 1.00 61.71  ? 281 VAL C CA    1 
ATOM   9845  C C     . VAL C  1 281 ? -15.617 88.913  168.868 1.00 64.69  ? 281 VAL C C     1 
ATOM   9846  O O     . VAL C  1 281 ? -15.614 88.021  168.020 1.00 62.52  ? 281 VAL C O     1 
ATOM   9847  C CB    . VAL C  1 281 ? -14.759 90.985  167.814 1.00 58.67  ? 281 VAL C CB    1 
ATOM   9848  C CG1   . VAL C  1 281 ? -16.070 91.713  168.067 1.00 65.50  ? 281 VAL C CG1   1 
ATOM   9849  C CG2   . VAL C  1 281 ? -13.618 91.975  167.723 1.00 59.41  ? 281 VAL C CG2   1 
ATOM   9850  N N     . LEU C  1 282 ? -16.570 89.044  169.785 1.00 71.94  ? 282 LEU C N     1 
ATOM   9851  C CA    . LEU C  1 282 ? -17.850 88.358  169.680 1.00 67.29  ? 282 LEU C CA    1 
ATOM   9852  C C     . LEU C  1 282 ? -18.919 89.414  169.450 1.00 69.48  ? 282 LEU C C     1 
ATOM   9853  O O     . LEU C  1 282 ? -19.048 90.351  170.236 1.00 66.78  ? 282 LEU C O     1 
ATOM   9854  C CB    . LEU C  1 282 ? -18.154 87.543  170.937 1.00 69.29  ? 282 LEU C CB    1 
ATOM   9855  C CG    . LEU C  1 282 ? -17.378 86.239  171.132 1.00 77.93  ? 282 LEU C CG    1 
ATOM   9856  C CD1   . LEU C  1 282 ? -17.673 85.644  172.500 1.00 82.86  ? 282 LEU C CD1   1 
ATOM   9857  C CD2   . LEU C  1 282 ? -17.718 85.243  170.032 1.00 73.88  ? 282 LEU C CD2   1 
ATOM   9858  N N     . GLY C  1 283 ? -19.673 89.278  168.366 1.00 68.38  ? 283 GLY C N     1 
ATOM   9859  C CA    . GLY C  1 283 ? -20.664 90.279  168.023 1.00 71.24  ? 283 GLY C CA    1 
ATOM   9860  C C     . GLY C  1 283 ? -22.006 89.702  167.630 1.00 70.26  ? 283 GLY C C     1 
ATOM   9861  O O     . GLY C  1 283 ? -22.090 88.614  167.065 1.00 64.70  ? 283 GLY C O     1 
ATOM   9862  N N     . GLY C  1 284 ? -23.062 90.441  167.943 1.00 73.91  ? 284 GLY C N     1 
ATOM   9863  C CA    . GLY C  1 284 ? -24.408 90.072  167.553 1.00 68.76  ? 284 GLY C CA    1 
ATOM   9864  C C     . GLY C  1 284 ? -25.284 91.294  167.696 1.00 78.43  ? 284 GLY C C     1 
ATOM   9865  O O     . GLY C  1 284 ? -24.825 92.336  168.163 1.00 76.94  ? 284 GLY C O     1 
ATOM   9866  N N     . ALA C  1 285 ? -26.547 91.177  167.310 1.00 77.87  ? 285 ALA C N     1 
ATOM   9867  C CA    . ALA C  1 285 ? -27.444 92.319  167.404 1.00 81.18  ? 285 ALA C CA    1 
ATOM   9868  C C     . ALA C  1 285 ? -28.796 91.930  167.985 1.00 84.99  ? 285 ALA C C     1 
ATOM   9869  O O     . ALA C  1 285 ? -29.096 90.747  168.157 1.00 80.45  ? 285 ALA C O     1 
ATOM   9870  C CB    . ALA C  1 285 ? -27.619 92.962  166.041 1.00 77.00  ? 285 ALA C CB    1 
ATOM   9871  N N     . ASP C  1 286 ? -29.594 92.945  168.299 1.00 91.68  ? 286 ASP C N     1 
ATOM   9872  C CA    . ASP C  1 286 ? -30.969 92.775  168.751 1.00 99.39  ? 286 ASP C CA    1 
ATOM   9873  C C     . ASP C  1 286 ? -31.731 94.031  168.327 1.00 98.84  ? 286 ASP C C     1 
ATOM   9874  O O     . ASP C  1 286 ? -32.035 94.898  169.149 1.00 98.68  ? 286 ASP C O     1 
ATOM   9875  C CB    . ASP C  1 286 ? -31.024 92.552  170.267 1.00 102.54 ? 286 ASP C CB    1 
ATOM   9876  C CG    . ASP C  1 286 ? -32.443 92.542  170.818 1.00 103.56 ? 286 ASP C CG    1 
ATOM   9877  O OD1   . ASP C  1 286 ? -33.385 92.194  170.075 1.00 96.09  ? 286 ASP C OD1   1 
ATOM   9878  O OD2   . ASP C  1 286 ? -32.607 92.889  172.007 1.00 104.90 ? 286 ASP C OD2   1 
ATOM   9879  N N     . GLU C  1 287 ? -32.016 94.117  167.027 1.00 95.80  ? 287 GLU C N     1 
ATOM   9880  C CA    . GLU C  1 287 ? -32.568 95.320  166.387 1.00 96.36  ? 287 GLU C CA    1 
ATOM   9881  C C     . GLU C  1 287 ? -31.724 96.579  166.630 1.00 98.73  ? 287 GLU C C     1 
ATOM   9882  O O     . GLU C  1 287 ? -31.788 97.169  167.707 1.00 108.84 ? 287 GLU C O     1 
ATOM   9883  C CB    . GLU C  1 287 ? -34.000 95.600  166.859 1.00 99.43  ? 287 GLU C CB    1 
ATOM   9884  C CG    . GLU C  1 287 ? -34.905 94.390  167.048 1.00 95.76  ? 287 GLU C CG    1 
ATOM   9885  C CD    . GLU C  1 287 ? -36.329 94.802  167.394 1.00 92.74  ? 287 GLU C CD    1 
ATOM   9886  O OE1   . GLU C  1 287 ? -36.716 94.706  168.578 1.00 89.64  ? 287 GLU C OE1   1 
ATOM   9887  O OE2   . GLU C  1 287 ? -37.060 95.227  166.476 1.00 91.86  ? 287 GLU C OE2   1 
ATOM   9888  N N     . LYS C  1 288 ? -30.943 96.989  165.628 1.00 97.68  ? 288 LYS C N     1 
ATOM   9889  C CA    . LYS C  1 288 ? -30.123 98.218  165.668 1.00 94.35  ? 288 LYS C CA    1 
ATOM   9890  C C     . LYS C  1 288 ? -29.302 98.441  166.945 1.00 90.06  ? 288 LYS C C     1 
ATOM   9891  O O     . LYS C  1 288 ? -28.398 99.275  166.962 1.00 88.58  ? 288 LYS C O     1 
ATOM   9892  C CB    . LYS C  1 288 ? -31.004 99.449  165.429 1.00 96.67  ? 288 LYS C CB    1 
ATOM   9893  C CG    . LYS C  1 288 ? -31.462 99.593  163.989 1.00 93.50  ? 288 LYS C CG    1 
ATOM   9894  C CD    . LYS C  1 288 ? -31.973 100.990 163.691 1.00 90.87  ? 288 LYS C CD    1 
ATOM   9895  C CE    . LYS C  1 288 ? -32.706 101.019 162.359 1.00 91.02  ? 288 LYS C CE    1 
ATOM   9896  N NZ    . LYS C  1 288 ? -32.542 102.316 161.649 1.00 89.41  ? 288 LYS C NZ    1 
ATOM   9897  N N     . GLN C  1 289 ? -29.631 97.717  168.010 1.00 90.19  ? 289 GLN C N     1 
ATOM   9898  C CA    . GLN C  1 289 ? -28.785 97.648  169.185 1.00 97.30  ? 289 GLN C CA    1 
ATOM   9899  C C     . GLN C  1 289 ? -27.738 96.579  168.947 1.00 91.90  ? 289 GLN C C     1 
ATOM   9900  O O     . GLN C  1 289 ? -28.052 95.391  168.865 1.00 86.43  ? 289 GLN C O     1 
ATOM   9901  C CB    . GLN C  1 289 ? -29.591 97.322  170.441 1.00 100.15 ? 289 GLN C CB    1 
ATOM   9902  C CG    . GLN C  1 289 ? -28.855 97.624  171.730 1.00 103.86 ? 289 GLN C CG    1 
ATOM   9903  C CD    . GLN C  1 289 ? -29.050 99.058  172.172 1.00 110.87 ? 289 GLN C CD    1 
ATOM   9904  O OE1   . GLN C  1 289 ? -30.045 99.390  172.813 1.00 115.82 ? 289 GLN C OE1   1 
ATOM   9905  N NE2   . GLN C  1 289 ? -28.100 99.921  171.825 1.00 105.82 ? 289 GLN C NE2   1 
ATOM   9906  N N     . VAL C  1 290 ? -26.491 97.006  168.834 1.00 89.22  ? 290 VAL C N     1 
ATOM   9907  C CA    . VAL C  1 290 ? -25.407 96.076  168.588 1.00 81.90  ? 290 VAL C CA    1 
ATOM   9908  C C     . VAL C  1 290 ? -24.562 95.909  169.837 1.00 78.24  ? 290 VAL C C     1 
ATOM   9909  O O     . VAL C  1 290 ? -24.284 96.878  170.540 1.00 78.75  ? 290 VAL C O     1 
ATOM   9910  C CB    . VAL C  1 290 ? -24.525 96.547  167.428 1.00 74.72  ? 290 VAL C CB    1 
ATOM   9911  C CG1   . VAL C  1 290 ? -23.505 95.482  167.082 1.00 73.82  ? 290 VAL C CG1   1 
ATOM   9912  C CG2   . VAL C  1 290 ? -25.387 96.881  166.222 1.00 76.84  ? 290 VAL C CG2   1 
ATOM   9913  N N     . TRP C  1 291 ? -24.175 94.673  170.124 1.00 73.67  ? 291 TRP C N     1 
ATOM   9914  C CA    . TRP C  1 291 ? -23.203 94.421  171.173 1.00 73.22  ? 291 TRP C CA    1 
ATOM   9915  C C     . TRP C  1 291 ? -21.930 93.863  170.559 1.00 76.01  ? 291 TRP C C     1 
ATOM   9916  O O     . TRP C  1 291 ? -21.970 92.934  169.752 1.00 76.50  ? 291 TRP C O     1 
ATOM   9917  C CB    . TRP C  1 291 ? -23.759 93.462  172.228 1.00 74.86  ? 291 TRP C CB    1 
ATOM   9918  C CG    . TRP C  1 291 ? -24.282 92.175  171.669 1.00 78.98  ? 291 TRP C CG    1 
ATOM   9919  C CD1   . TRP C  1 291 ? -25.537 91.944  171.187 1.00 81.73  ? 291 TRP C CD1   1 
ATOM   9920  C CD2   . TRP C  1 291 ? -23.569 90.937  171.543 1.00 76.46  ? 291 TRP C CD2   1 
ATOM   9921  N NE1   . TRP C  1 291 ? -25.650 90.641  170.766 1.00 78.65  ? 291 TRP C NE1   1 
ATOM   9922  C CE2   . TRP C  1 291 ? -24.457 90.001  170.974 1.00 77.74  ? 291 TRP C CE2   1 
ATOM   9923  C CE3   . TRP C  1 291 ? -22.267 90.529  171.854 1.00 76.06  ? 291 TRP C CE3   1 
ATOM   9924  C CZ2   . TRP C  1 291 ? -24.085 88.683  170.709 1.00 75.29  ? 291 TRP C CZ2   1 
ATOM   9925  C CZ3   . TRP C  1 291 ? -21.900 89.219  171.589 1.00 75.83  ? 291 TRP C CZ3   1 
ATOM   9926  C CH2   . TRP C  1 291 ? -22.805 88.313  171.023 1.00 76.38  ? 291 TRP C CH2   1 
ATOM   9927  N N     . LEU C  1 292 ? -20.802 94.456  170.927 1.00 71.22  ? 292 LEU C N     1 
ATOM   9928  C CA    . LEU C  1 292 ? -19.504 93.948  170.516 1.00 65.25  ? 292 LEU C CA    1 
ATOM   9929  C C     . LEU C  1 292 ? -18.671 93.633  171.744 1.00 64.56  ? 292 LEU C C     1 
ATOM   9930  O O     . LEU C  1 292 ? -18.257 94.538  172.464 1.00 65.61  ? 292 LEU C O     1 
ATOM   9931  C CB    . LEU C  1 292 ? -18.771 94.957  169.629 1.00 63.64  ? 292 LEU C CB    1 
ATOM   9932  C CG    . LEU C  1 292 ? -19.382 95.277  168.265 1.00 61.82  ? 292 LEU C CG    1 
ATOM   9933  C CD1   . LEU C  1 292 ? -18.423 96.129  167.446 1.00 61.39  ? 292 LEU C CD1   1 
ATOM   9934  C CD2   . LEU C  1 292 ? -19.755 94.013  167.507 1.00 66.19  ? 292 LEU C CD2   1 
ATOM   9935  N N     . THR C  1 293 ? -18.431 92.351  171.989 1.00 62.70  ? 293 THR C N     1 
ATOM   9936  C CA    . THR C  1 293 ? -17.592 91.960  173.111 1.00 68.02  ? 293 THR C CA    1 
ATOM   9937  C C     . THR C  1 293 ? -16.150 91.813  172.650 1.00 66.49  ? 293 THR C C     1 
ATOM   9938  O O     . THR C  1 293 ? -15.820 90.895  171.900 1.00 64.39  ? 293 THR C O     1 
ATOM   9939  C CB    . THR C  1 293 ? -18.062 90.649  173.755 1.00 66.78  ? 293 THR C CB    1 
ATOM   9940  O OG1   . THR C  1 293 ? -19.461 90.734  174.054 1.00 72.21  ? 293 THR C OG1   1 
ATOM   9941  C CG2   . THR C  1 293 ? -17.290 90.391  175.037 1.00 64.87  ? 293 THR C CG2   1 
ATOM   9942  N N     . MET C  1 294 ? -15.300 92.733  173.093 1.00 68.66  ? 294 MET C N     1 
ATOM   9943  C CA    . MET C  1 294 ? -13.890 92.709  172.733 1.00 61.34  ? 294 MET C CA    1 
ATOM   9944  C C     . MET C  1 294 ? -13.104 91.873  173.728 1.00 63.28  ? 294 MET C C     1 
ATOM   9945  O O     . MET C  1 294 ? -13.134 92.132  174.930 1.00 64.60  ? 294 MET C O     1 
ATOM   9946  C CB    . MET C  1 294 ? -13.323 94.128  172.674 1.00 65.08  ? 294 MET C CB    1 
ATOM   9947  C CG    . MET C  1 294 ? -13.978 95.012  171.626 1.00 66.52  ? 294 MET C CG    1 
ATOM   9948  S SD    . MET C  1 294 ? -13.419 94.680  169.944 1.00 74.77  ? 294 MET C SD    1 
ATOM   9949  C CE    . MET C  1 294 ? -14.618 95.614  168.996 1.00 62.64  ? 294 MET C CE    1 
ATOM   9950  N N     . LEU C  1 295 ? -12.406 90.864  173.224 1.00 63.63  ? 295 LEU C N     1 
ATOM   9951  C CA    . LEU C  1 295 ? -11.622 89.988  174.080 1.00 59.36  ? 295 LEU C CA    1 
ATOM   9952  C C     . LEU C  1 295 ? -10.132 90.193  173.839 1.00 58.86  ? 295 LEU C C     1 
ATOM   9953  O O     . LEU C  1 295 ? -9.627  89.946  172.744 1.00 56.36  ? 295 LEU C O     1 
ATOM   9954  C CB    . LEU C  1 295 ? -12.013 88.529  173.846 1.00 61.89  ? 295 LEU C CB    1 
ATOM   9955  C CG    . LEU C  1 295 ? -13.478 88.202  174.155 1.00 67.40  ? 295 LEU C CG    1 
ATOM   9956  C CD1   . LEU C  1 295 ? -14.037 87.192  173.163 1.00 67.04  ? 295 LEU C CD1   1 
ATOM   9957  C CD2   . LEU C  1 295 ? -13.635 87.697  175.583 1.00 68.18  ? 295 LEU C CD2   1 
ATOM   9958  N N     . GLY C  1 296 ? -9.433  90.651  174.871 1.00 60.47  ? 296 GLY C N     1 
ATOM   9959  C CA    . GLY C  1 296 ? -8.013  90.918  174.765 1.00 56.70  ? 296 GLY C CA    1 
ATOM   9960  C C     . GLY C  1 296 ? -7.162  90.014  175.633 1.00 58.15  ? 296 GLY C C     1 
ATOM   9961  O O     . GLY C  1 296 ? -7.589  89.574  176.699 1.00 58.51  ? 296 GLY C O     1 
ATOM   9962  N N     . PHE C  1 297 ? -5.951  89.734  175.164 1.00 55.54  ? 297 PHE C N     1 
ATOM   9963  C CA    . PHE C  1 297 ? -4.976  88.967  175.932 1.00 55.05  ? 297 PHE C CA    1 
ATOM   9964  C C     . PHE C  1 297 ? -3.580  89.512  175.661 1.00 53.07  ? 297 PHE C C     1 
ATOM   9965  O O     . PHE C  1 297 ? -3.247  89.839  174.523 1.00 53.24  ? 297 PHE C O     1 
ATOM   9966  C CB    . PHE C  1 297 ? -5.046  87.473  175.583 1.00 51.18  ? 297 PHE C CB    1 
ATOM   9967  C CG    . PHE C  1 297 ? -3.999  86.634  176.275 1.00 55.04  ? 297 PHE C CG    1 
ATOM   9968  C CD1   . PHE C  1 297 ? -4.281  85.995  177.472 1.00 56.53  ? 297 PHE C CD1   1 
ATOM   9969  C CD2   . PHE C  1 297 ? -2.732  86.485  175.728 1.00 53.40  ? 297 PHE C CD2   1 
ATOM   9970  C CE1   . PHE C  1 297 ? -3.322  85.231  178.109 1.00 61.82  ? 297 PHE C CE1   1 
ATOM   9971  C CE2   . PHE C  1 297 ? -1.773  85.726  176.364 1.00 54.47  ? 297 PHE C CE2   1 
ATOM   9972  C CZ    . PHE C  1 297 ? -2.068  85.105  177.556 1.00 56.33  ? 297 PHE C CZ    1 
ATOM   9973  N N     . HIS C  1 298 ? -2.763  89.608  176.703 1.00 55.51  ? 298 HIS C N     1 
ATOM   9974  C CA    . HIS C  1 298 ? -1.380  90.031  176.528 1.00 58.43  ? 298 HIS C CA    1 
ATOM   9975  C C     . HIS C  1 298 ? -0.427  89.194  177.367 1.00 59.02  ? 298 HIS C C     1 
ATOM   9976  O O     . HIS C  1 298 ? -0.656  88.980  178.556 1.00 59.26  ? 298 HIS C O     1 
ATOM   9977  C CB    . HIS C  1 298 ? -1.208  91.508  176.882 1.00 58.37  ? 298 HIS C CB    1 
ATOM   9978  C CG    . HIS C  1 298 ? 0.224   91.936  176.976 1.00 62.36  ? 298 HIS C CG    1 
ATOM   9979  N ND1   . HIS C  1 298 ? 1.128   91.738  175.954 1.00 59.30  ? 298 HIS C ND1   1 
ATOM   9980  C CD2   . HIS C  1 298 ? 0.911   92.539  177.974 1.00 64.44  ? 298 HIS C CD2   1 
ATOM   9981  C CE1   . HIS C  1 298 ? 2.309   92.206  176.317 1.00 64.18  ? 298 HIS C CE1   1 
ATOM   9982  N NE2   . HIS C  1 298 ? 2.205   92.697  177.538 1.00 64.29  ? 298 HIS C NE2   1 
ATOM   9983  N N     . PHE C  1 299 ? 0.645   88.726  176.737 1.00 60.44  ? 299 PHE C N     1 
ATOM   9984  C CA    . PHE C  1 299 ? 1.708   88.033  177.451 1.00 59.47  ? 299 PHE C CA    1 
ATOM   9985  C C     . PHE C  1 299 ? 2.551   89.024  178.239 1.00 65.60  ? 299 PHE C C     1 
ATOM   9986  O O     . PHE C  1 299 ? 3.697   89.294  177.883 1.00 68.48  ? 299 PHE C O     1 
ATOM   9987  C CB    . PHE C  1 299 ? 2.595   87.254  176.483 1.00 57.00  ? 299 PHE C CB    1 
ATOM   9988  C CG    . PHE C  1 299 ? 1.952   86.018  175.934 1.00 62.25  ? 299 PHE C CG    1 
ATOM   9989  C CD1   . PHE C  1 299 ? 2.027   84.821  176.624 1.00 58.49  ? 299 PHE C CD1   1 
ATOM   9990  C CD2   . PHE C  1 299 ? 1.277   86.051  174.725 1.00 59.04  ? 299 PHE C CD2   1 
ATOM   9991  C CE1   . PHE C  1 299 ? 1.439   83.680  176.118 1.00 55.70  ? 299 PHE C CE1   1 
ATOM   9992  C CE2   . PHE C  1 299 ? 0.688   84.913  174.215 1.00 58.76  ? 299 PHE C CE2   1 
ATOM   9993  C CZ    . PHE C  1 299 ? 0.768   83.727  174.912 1.00 57.84  ? 299 PHE C CZ    1 
ATOM   9994  N N     . GLY C  1 300 ? 1.983   89.569  179.307 1.00 64.91  ? 300 GLY C N     1 
ATOM   9995  C CA    . GLY C  1 300 ? 2.696   90.536  180.116 1.00 66.04  ? 300 GLY C CA    1 
ATOM   9996  C C     . GLY C  1 300 ? 1.781   91.311  181.039 1.00 66.66  ? 300 GLY C C     1 
ATOM   9997  O O     . GLY C  1 300 ? 0.716   90.833  181.424 1.00 64.68  ? 300 GLY C O     1 
ATOM   9998  N N     . LEU C  1 301 ? 2.189   92.525  181.382 1.00 67.82  ? 301 LEU C N     1 
ATOM   9999  C CA    . LEU C  1 301 ? 1.521   93.256  182.446 1.00 63.81  ? 301 LEU C CA    1 
ATOM   10000 C C     . LEU C  1 301 ? 0.511   94.302  181.967 1.00 64.58  ? 301 LEU C C     1 
ATOM   10001 O O     . LEU C  1 301 ? 0.498   94.708  180.803 1.00 65.62  ? 301 LEU C O     1 
ATOM   10002 C CB    . LEU C  1 301 ? 2.570   93.912  183.347 1.00 68.07  ? 301 LEU C CB    1 
ATOM   10003 C CG    . LEU C  1 301 ? 3.463   92.901  184.077 1.00 64.32  ? 301 LEU C CG    1 
ATOM   10004 C CD1   . LEU C  1 301 ? 4.850   93.467  184.324 1.00 64.44  ? 301 LEU C CD1   1 
ATOM   10005 C CD2   . LEU C  1 301 ? 2.829   92.460  185.393 1.00 67.19  ? 301 LEU C CD2   1 
ATOM   10006 N N     . LYS C  1 302 ? -0.342  94.706  182.902 1.00 65.65  ? 302 LYS C N     1 
ATOM   10007 C CA    . LYS C  1 302 ? -1.406  95.679  182.688 1.00 68.39  ? 302 LYS C CA    1 
ATOM   10008 C C     . LYS C  1 302 ? -0.930  96.977  182.039 1.00 66.66  ? 302 LYS C C     1 
ATOM   10009 O O     . LYS C  1 302 ? -1.570  97.502  181.126 1.00 64.23  ? 302 LYS C O     1 
ATOM   10010 C CB    . LYS C  1 302 ? -2.066  95.984  184.035 1.00 72.37  ? 302 LYS C CB    1 
ATOM   10011 C CG    . LYS C  1 302 ? -3.391  96.695  183.959 1.00 76.49  ? 302 LYS C CG    1 
ATOM   10012 C CD    . LYS C  1 302 ? -4.244  96.331  185.162 1.00 76.83  ? 302 LYS C CD    1 
ATOM   10013 C CE    . LYS C  1 302 ? -4.508  97.532  186.051 1.00 79.39  ? 302 LYS C CE    1 
ATOM   10014 N NZ    . LYS C  1 302 ? -4.942  97.127  187.417 1.00 81.35  ? 302 LYS C NZ    1 
ATOM   10015 N N     . THR C  1 303 ? 0.199   97.484  182.524 1.00 68.88  ? 303 THR C N     1 
ATOM   10016 C CA    . THR C  1 303 ? 0.754   98.750  182.060 1.00 66.35  ? 303 THR C CA    1 
ATOM   10017 C C     . THR C  1 303 ? 1.034   98.737  180.559 1.00 65.89  ? 303 THR C C     1 
ATOM   10018 O O     . THR C  1 303 ? 0.605   99.631  179.838 1.00 64.90  ? 303 THR C O     1 
ATOM   10019 C CB    . THR C  1 303 ? 2.051   99.092  182.807 1.00 68.57  ? 303 THR C CB    1 
ATOM   10020 O OG1   . THR C  1 303 ? 3.098   98.216  182.373 1.00 72.85  ? 303 THR C OG1   1 
ATOM   10021 C CG2   . THR C  1 303 ? 1.852   98.937  184.309 1.00 63.12  ? 303 THR C CG2   1 
ATOM   10022 N N     . VAL C  1 304 ? 1.750   97.716  180.100 1.00 66.01  ? 304 VAL C N     1 
ATOM   10023 C CA    . VAL C  1 304 ? 2.087   97.585  178.686 1.00 63.87  ? 304 VAL C CA    1 
ATOM   10024 C C     . VAL C  1 304 ? 0.834   97.361  177.840 1.00 62.78  ? 304 VAL C C     1 
ATOM   10025 O O     . VAL C  1 304 ? 0.740   97.843  176.710 1.00 56.52  ? 304 VAL C O     1 
ATOM   10026 C CB    . VAL C  1 304 ? 3.082   96.428  178.456 1.00 65.18  ? 304 VAL C CB    1 
ATOM   10027 C CG1   . VAL C  1 304 ? 3.531   96.383  177.006 1.00 59.93  ? 304 VAL C CG1   1 
ATOM   10028 C CG2   . VAL C  1 304 ? 4.281   96.575  179.377 1.00 62.09  ? 304 VAL C CG2   1 
ATOM   10029 N N     . ALA C  1 305 ? -0.132  96.641  178.405 1.00 63.12  ? 305 ALA C N     1 
ATOM   10030 C CA    . ALA C  1 305 ? -1.379  96.326  177.712 1.00 64.40  ? 305 ALA C CA    1 
ATOM   10031 C C     . ALA C  1 305 ? -2.176  97.581  177.373 1.00 64.71  ? 305 ALA C C     1 
ATOM   10032 O O     . ALA C  1 305 ? -2.440  97.855  176.199 1.00 61.97  ? 305 ALA C O     1 
ATOM   10033 C CB    . ALA C  1 305 ? -2.224  95.380  178.554 1.00 65.51  ? 305 ALA C CB    1 
ATOM   10034 N N     . LYS C  1 306 ? -2.559  98.341  178.396 1.00 70.12  ? 306 LYS C N     1 
ATOM   10035 C CA    . LYS C  1 306 ? -3.337  99.556  178.170 1.00 69.25  ? 306 LYS C CA    1 
ATOM   10036 C C     . LYS C  1 306 ? -2.540  100.564 177.359 1.00 63.83  ? 306 LYS C C     1 
ATOM   10037 O O     . LYS C  1 306 ? -3.079  101.188 176.450 1.00 62.63  ? 306 LYS C O     1 
ATOM   10038 C CB    . LYS C  1 306 ? -3.794  100.184 179.487 1.00 72.51  ? 306 LYS C CB    1 
ATOM   10039 C CG    . LYS C  1 306 ? -4.696  101.398 179.276 1.00 73.99  ? 306 LYS C CG    1 
ATOM   10040 C CD    . LYS C  1 306 ? -5.330  101.889 180.565 1.00 80.20  ? 306 LYS C CD    1 
ATOM   10041 C CE    . LYS C  1 306 ? -6.359  102.976 180.288 1.00 80.99  ? 306 LYS C CE    1 
ATOM   10042 N NZ    . LYS C  1 306 ? -5.742  104.185 179.675 1.00 85.13  ? 306 LYS C NZ    1 
ATOM   10043 N N     . SER C  1 307 ? -1.258  100.707 177.681 1.00 61.37  ? 307 SER C N     1 
ATOM   10044 C CA    . SER C  1 307 ? -0.370  101.570 176.912 1.00 61.40  ? 307 SER C CA    1 
ATOM   10045 C C     . SER C  1 307 ? -0.431  101.241 175.426 1.00 61.60  ? 307 SER C C     1 
ATOM   10046 O O     . SER C  1 307 ? -0.535  102.131 174.590 1.00 63.23  ? 307 SER C O     1 
ATOM   10047 C CB    . SER C  1 307 ? 1.069   101.439 177.409 1.00 61.69  ? 307 SER C CB    1 
ATOM   10048 O OG    . SER C  1 307 ? 1.985   102.033 176.508 1.00 68.10  ? 307 SER C OG    1 
ATOM   10049 N N     . THR C  1 308 ? -0.384  99.954  175.102 1.00 62.24  ? 308 THR C N     1 
ATOM   10050 C CA    . THR C  1 308 ? -0.384  99.535  173.709 1.00 57.41  ? 308 THR C CA    1 
ATOM   10051 C C     . THR C  1 308 ? -1.751  99.776  173.067 1.00 60.52  ? 308 THR C C     1 
ATOM   10052 O O     . THR C  1 308 ? -1.829  100.229 171.926 1.00 60.06  ? 308 THR C O     1 
ATOM   10053 C CB    . THR C  1 308 ? -0.000  98.048  173.550 1.00 59.14  ? 308 THR C CB    1 
ATOM   10054 O OG1   . THR C  1 308 ? 1.232   97.782  174.234 1.00 58.39  ? 308 THR C OG1   1 
ATOM   10055 C CG2   . THR C  1 308 ? 0.179   97.716  172.082 1.00 60.88  ? 308 THR C CG2   1 
ATOM   10056 N N     . PHE C  1 309 ? -2.826  99.482  173.796 1.00 55.66  ? 309 PHE C N     1 
ATOM   10057 C CA    . PHE C  1 309 ? -4.176  99.616  173.243 1.00 62.56  ? 309 PHE C CA    1 
ATOM   10058 C C     . PHE C  1 309 ? -4.683  101.061 173.241 1.00 59.38  ? 309 PHE C C     1 
ATOM   10059 O O     . PHE C  1 309 ? -5.487  101.436 172.385 1.00 61.10  ? 309 PHE C O     1 
ATOM   10060 C CB    . PHE C  1 309 ? -5.157  98.716  174.001 1.00 63.02  ? 309 PHE C CB    1 
ATOM   10061 C CG    . PHE C  1 309 ? -5.042  97.263  173.642 1.00 65.30  ? 309 PHE C CG    1 
ATOM   10062 C CD1   . PHE C  1 309 ? -5.377  96.827  172.368 1.00 65.20  ? 309 PHE C CD1   1 
ATOM   10063 C CD2   . PHE C  1 309 ? -4.600  96.335  174.572 1.00 61.17  ? 309 PHE C CD2   1 
ATOM   10064 C CE1   . PHE C  1 309 ? -5.271  95.492  172.027 1.00 62.04  ? 309 PHE C CE1   1 
ATOM   10065 C CE2   . PHE C  1 309 ? -4.492  94.996  174.240 1.00 60.29  ? 309 PHE C CE2   1 
ATOM   10066 C CZ    . PHE C  1 309 ? -4.829  94.576  172.966 1.00 58.07  ? 309 PHE C CZ    1 
ATOM   10067 N N     . ASP C  1 310 ? -4.223  101.862 174.200 1.00 61.75  ? 310 ASP C N     1 
ATOM   10068 C CA    . ASP C  1 310 ? -4.467  103.305 174.179 1.00 65.87  ? 310 ASP C CA    1 
ATOM   10069 C C     . ASP C  1 310 ? -3.962  103.880 172.859 1.00 62.35  ? 310 ASP C C     1 
ATOM   10070 O O     . ASP C  1 310 ? -4.630  104.683 172.208 1.00 61.44  ? 310 ASP C O     1 
ATOM   10071 C CB    . ASP C  1 310 ? -3.769  104.004 175.354 1.00 59.69  ? 310 ASP C CB    1 
ATOM   10072 C CG    . ASP C  1 310 ? -4.516  103.847 176.663 1.00 69.38  ? 310 ASP C CG    1 
ATOM   10073 O OD1   . ASP C  1 310 ? -5.511  103.092 176.698 1.00 76.84  ? 310 ASP C OD1   1 
ATOM   10074 O OD2   . ASP C  1 310 ? -4.099  104.475 177.660 1.00 70.84  ? 310 ASP C OD2   1 
ATOM   10075 N N     . LEU C  1 311 ? -2.770  103.442 172.471 1.00 56.55  ? 311 LEU C N     1 
ATOM   10076 C CA    . LEU C  1 311 ? -2.137  103.894 171.240 1.00 58.08  ? 311 LEU C CA    1 
ATOM   10077 C C     . LEU C  1 311 ? -2.817  103.328 169.986 1.00 63.10  ? 311 LEU C C     1 
ATOM   10078 O O     . LEU C  1 311 ? -3.185  104.081 169.087 1.00 60.78  ? 311 LEU C O     1 
ATOM   10079 C CB    . LEU C  1 311 ? -0.650  103.519 171.247 1.00 61.34  ? 311 LEU C CB    1 
ATOM   10080 C CG    . LEU C  1 311 ? 0.375   104.550 171.737 1.00 64.62  ? 311 LEU C CG    1 
ATOM   10081 C CD1   . LEU C  1 311 ? 0.098   105.002 173.174 1.00 65.10  ? 311 LEU C CD1   1 
ATOM   10082 C CD2   . LEU C  1 311 ? 1.796   104.002 171.597 1.00 65.24  ? 311 LEU C CD2   1 
ATOM   10083 N N     . LEU C  1 312 ? -2.991  102.008 169.932 1.00 63.31  ? 312 LEU C N     1 
ATOM   10084 C CA    . LEU C  1 312 ? -3.525  101.345 168.738 1.00 58.67  ? 312 LEU C CA    1 
ATOM   10085 C C     . LEU C  1 312 ? -5.047  101.400 168.595 1.00 59.99  ? 312 LEU C C     1 
ATOM   10086 O O     . LEU C  1 312 ? -5.565  101.424 167.479 1.00 60.68  ? 312 LEU C O     1 
ATOM   10087 C CB    . LEU C  1 312 ? -3.073  99.882  168.711 1.00 59.89  ? 312 LEU C CB    1 
ATOM   10088 C CG    . LEU C  1 312 ? -1.607  99.677  168.330 1.00 57.78  ? 312 LEU C CG    1 
ATOM   10089 C CD1   . LEU C  1 312 ? -1.180  98.233  168.538 1.00 50.80  ? 312 LEU C CD1   1 
ATOM   10090 C CD2   . LEU C  1 312 ? -1.388  100.102 166.887 1.00 53.25  ? 312 LEU C CD2   1 
ATOM   10091 N N     . PHE C  1 313 ? -5.765  101.413 169.712 1.00 61.57  ? 313 PHE C N     1 
ATOM   10092 C CA    . PHE C  1 313 ? -7.224  101.343 169.651 1.00 68.81  ? 313 PHE C CA    1 
ATOM   10093 C C     . PHE C  1 313 ? -7.925  102.174 170.731 1.00 66.87  ? 313 PHE C C     1 
ATOM   10094 O O     . PHE C  1 313 ? -8.605  101.618 171.592 1.00 64.08  ? 313 PHE C O     1 
ATOM   10095 C CB    . PHE C  1 313 ? -7.667  99.882  169.759 1.00 69.66  ? 313 PHE C CB    1 
ATOM   10096 C CG    . PHE C  1 313 ? -8.851  99.538  168.902 1.00 72.81  ? 313 PHE C CG    1 
ATOM   10097 C CD1   . PHE C  1 313 ? -9.883  100.443 168.720 1.00 66.19  ? 313 PHE C CD1   1 
ATOM   10098 C CD2   . PHE C  1 313 ? -8.926  98.307  168.270 1.00 70.37  ? 313 PHE C CD2   1 
ATOM   10099 C CE1   . PHE C  1 313 ? -10.973 100.125 167.934 1.00 69.38  ? 313 PHE C CE1   1 
ATOM   10100 C CE2   . PHE C  1 313 ? -10.011 97.984  167.479 1.00 69.52  ? 313 PHE C CE2   1 
ATOM   10101 C CZ    . PHE C  1 313 ? -11.037 98.894  167.310 1.00 69.04  ? 313 PHE C CZ    1 
ATOM   10102 N N     . PRO C  1 314 ? -7.770  103.509 170.688 1.00 67.99  ? 314 PRO C N     1 
ATOM   10103 C CA    . PRO C  1 314 ? -8.413  104.335 171.718 1.00 64.78  ? 314 PRO C CA    1 
ATOM   10104 C C     . PRO C  1 314 ? -9.940  104.361 171.616 1.00 63.16  ? 314 PRO C C     1 
ATOM   10105 O O     . PRO C  1 314 ? -10.607 104.485 172.644 1.00 65.00  ? 314 PRO C O     1 
ATOM   10106 C CB    . PRO C  1 314 ? -7.831  105.727 171.460 1.00 63.83  ? 314 PRO C CB    1 
ATOM   10107 C CG    . PRO C  1 314 ? -7.474  105.713 170.013 1.00 62.56  ? 314 PRO C CG    1 
ATOM   10108 C CD    . PRO C  1 314 ? -6.962  104.326 169.765 1.00 65.47  ? 314 PRO C CD    1 
ATOM   10109 N N     . GLU C  1 315 ? -10.471 104.246 170.400 1.00 62.50  ? 315 GLU C N     1 
ATOM   10110 C CA    . GLU C  1 315 ? -11.917 104.250 170.166 1.00 63.58  ? 315 GLU C CA    1 
ATOM   10111 C C     . GLU C  1 315 ? -12.665 103.268 171.052 1.00 67.34  ? 315 GLU C C     1 
ATOM   10112 O O     . GLU C  1 315 ? -13.866 103.407 171.301 1.00 74.04  ? 315 GLU C O     1 
ATOM   10113 C CB    . GLU C  1 315 ? -12.223 103.921 168.700 1.00 59.26  ? 315 GLU C CB    1 
ATOM   10114 C CG    . GLU C  1 315 ? -11.889 105.014 167.718 1.00 58.96  ? 315 GLU C CG    1 
ATOM   10115 C CD    . GLU C  1 315 ? -10.469 104.924 167.193 1.00 67.25  ? 315 GLU C CD    1 
ATOM   10116 O OE1   . GLU C  1 315 ? -9.582  104.455 167.937 1.00 63.92  ? 315 GLU C OE1   1 
ATOM   10117 O OE2   . GLU C  1 315 ? -10.237 105.313 166.027 1.00 66.29  ? 315 GLU C OE2   1 
ATOM   10118 N N     . LEU C  1 316 ? -11.937 102.255 171.493 1.00 68.94  ? 316 LEU C N     1 
ATOM   10119 C CA    . LEU C  1 316 ? -12.490 101.246 172.366 1.00 72.39  ? 316 LEU C CA    1 
ATOM   10120 C C     . LEU C  1 316 ? -12.916 101.843 173.706 1.00 71.84  ? 316 LEU C C     1 
ATOM   10121 O O     . LEU C  1 316 ? -13.850 101.357 174.350 1.00 76.95  ? 316 LEU C O     1 
ATOM   10122 C CB    . LEU C  1 316 ? -11.480 100.143 172.573 1.00 78.67  ? 316 LEU C CB    1 
ATOM   10123 C CG    . LEU C  1 316 ? -11.428 99.060  171.491 1.00 74.35  ? 316 LEU C CG    1 
ATOM   10124 C CD1   . LEU C  1 316 ? -10.303 98.072  171.741 1.00 71.59  ? 316 LEU C CD1   1 
ATOM   10125 C CD2   . LEU C  1 316 ? -12.765 98.340  171.399 1.00 71.49  ? 316 LEU C CD2   1 
ATOM   10126 N N     . GLY C  1 317 ? -12.231 102.898 174.128 1.00 68.49  ? 317 GLY C N     1 
ATOM   10127 C CA    . GLY C  1 317 ? -12.552 103.533 175.392 1.00 71.82  ? 317 GLY C CA    1 
ATOM   10128 C C     . GLY C  1 317 ? -12.359 102.623 176.587 1.00 74.74  ? 317 GLY C C     1 
ATOM   10129 O O     . GLY C  1 317 ? -13.151 102.646 177.528 1.00 75.88  ? 317 GLY C O     1 
ATOM   10130 N N     . LEU C  1 318 ? -11.309 101.811 176.549 1.00 74.38  ? 318 LEU C N     1 
ATOM   10131 C CA    . LEU C  1 318 ? -10.981 100.989 177.702 1.00 73.45  ? 318 LEU C CA    1 
ATOM   10132 C C     . LEU C  1 318 ? -10.359 101.810 178.798 1.00 75.29  ? 318 LEU C C     1 
ATOM   10133 O O     . LEU C  1 318 ? -9.555  102.711 178.550 1.00 74.67  ? 318 LEU C O     1 
ATOM   10134 C CB    . LEU C  1 318 ? -10.030 99.857  177.346 1.00 78.88  ? 318 LEU C CB    1 
ATOM   10135 C CG    . LEU C  1 318 ? -10.706 98.538  176.950 1.00 76.72  ? 318 LEU C CG    1 
ATOM   10136 C CD1   . LEU C  1 318 ? -10.817 98.403  175.414 1.00 69.14  ? 318 LEU C CD1   1 
ATOM   10137 C CD2   . LEU C  1 318 ? -10.022 97.341  177.585 1.00 74.20  ? 318 LEU C CD2   1 
ATOM   10138 N N     . VAL C  1 319 ? -10.726 101.462 180.020 1.00 77.44  ? 319 VAL C N     1 
ATOM   10139 C CA    . VAL C  1 319 ? -10.190 102.108 181.190 1.00 80.77  ? 319 VAL C CA    1 
ATOM   10140 C C     . VAL C  1 319 ? -9.247  101.155 181.900 1.00 79.68  ? 319 VAL C C     1 
ATOM   10141 O O     . VAL C  1 319 ? -9.074  100.005 181.487 1.00 79.29  ? 319 VAL C O     1 
ATOM   10142 C CB    . VAL C  1 319 ? -11.314 102.547 182.121 1.00 82.22  ? 319 VAL C CB    1 
ATOM   10143 C CG1   . VAL C  1 319 ? -12.297 103.412 181.349 1.00 79.56  ? 319 VAL C CG1   1 
ATOM   10144 C CG2   . VAL C  1 319 ? -12.020 101.334 182.691 1.00 80.60  ? 319 VAL C CG2   1 
ATOM   10145 N N     . GLU C  1 320 ? -8.630  101.653 182.963 1.00 82.54  ? 320 GLU C N     1 
ATOM   10146 C CA    . GLU C  1 320 ? -7.644  100.902 183.721 1.00 84.68  ? 320 GLU C CA    1 
ATOM   10147 C C     . GLU C  1 320 ? -8.272  99.717  184.449 1.00 85.75  ? 320 GLU C C     1 
ATOM   10148 O O     . GLU C  1 320 ? -7.627  98.686  184.642 1.00 83.78  ? 320 GLU C O     1 
ATOM   10149 C CB    . GLU C  1 320 ? -6.940  101.831 184.710 1.00 86.01  ? 320 GLU C CB    1 
ATOM   10150 C CG    . GLU C  1 320 ? -5.993  101.122 185.661 1.00 88.18  ? 320 GLU C CG    1 
ATOM   10151 C CD    . GLU C  1 320 ? -5.061  102.076 186.380 1.00 99.46  ? 320 GLU C CD    1 
ATOM   10152 O OE1   . GLU C  1 320 ? -5.516  103.161 186.801 1.00 100.37 ? 320 GLU C OE1   1 
ATOM   10153 O OE2   . GLU C  1 320 ? -3.866  101.738 186.516 1.00 100.33 ? 320 GLU C OE2   1 
ATOM   10154 N N     . GLU C  1 321 ? -9.533  99.860  184.843 1.00 88.11  ? 321 GLU C N     1 
ATOM   10155 C CA    . GLU C  1 321 ? -10.236 98.805  185.566 1.00 88.11  ? 321 GLU C CA    1 
ATOM   10156 C C     . GLU C  1 321 ? -10.589 97.629  184.662 1.00 82.72  ? 321 GLU C C     1 
ATOM   10157 O O     . GLU C  1 321 ? -10.797 96.511  185.134 1.00 79.70  ? 321 GLU C O     1 
ATOM   10158 C CB    . GLU C  1 321 ? -11.503 99.364  186.210 1.00 91.56  ? 321 GLU C CB    1 
ATOM   10159 C CG    . GLU C  1 321 ? -11.229 100.326 187.348 1.00 102.17 ? 321 GLU C CG    1 
ATOM   10160 C CD    . GLU C  1 321 ? -12.484 101.000 187.862 1.00 111.49 ? 321 GLU C CD    1 
ATOM   10161 O OE1   . GLU C  1 321 ? -13.521 100.317 187.995 1.00 107.66 ? 321 GLU C OE1   1 
ATOM   10162 O OE2   . GLU C  1 321 ? -12.436 102.220 188.126 1.00 109.37 ? 321 GLU C OE2   1 
ATOM   10163 N N     . ASP C  1 322 ? -10.650 97.886  183.360 1.00 79.38  ? 322 ASP C N     1 
ATOM   10164 C CA    . ASP C  1 322 ? -10.992 96.851  182.392 1.00 76.19  ? 322 ASP C CA    1 
ATOM   10165 C C     . ASP C  1 322 ? -9.868  95.817  182.261 1.00 77.48  ? 322 ASP C C     1 
ATOM   10166 O O     . ASP C  1 322 ? -10.121 94.644  181.984 1.00 76.32  ? 322 ASP C O     1 
ATOM   10167 C CB    . ASP C  1 322 ? -11.318 97.485  181.033 1.00 76.93  ? 322 ASP C CB    1 
ATOM   10168 C CG    . ASP C  1 322 ? -12.653 98.218  181.038 1.00 79.56  ? 322 ASP C CG    1 
ATOM   10169 O OD1   . ASP C  1 322 ? -13.480 97.938  181.931 1.00 80.57  ? 322 ASP C OD1   1 
ATOM   10170 O OD2   . ASP C  1 322 ? -12.881 99.064  180.147 1.00 79.47  ? 322 ASP C OD2   1 
ATOM   10171 N N     . TYR C  1 323 ? -8.632  96.251  182.484 1.00 75.77  ? 323 TYR C N     1 
ATOM   10172 C CA    . TYR C  1 323 ? -7.474  95.365  182.369 1.00 71.74  ? 323 TYR C CA    1 
ATOM   10173 C C     . TYR C  1 323 ? -7.284  94.547  183.646 1.00 73.37  ? 323 TYR C C     1 
ATOM   10174 O O     . TYR C  1 323 ? -7.051  95.099  184.725 1.00 75.91  ? 323 TYR C O     1 
ATOM   10175 C CB    . TYR C  1 323 ? -6.212  96.174  182.046 1.00 70.00  ? 323 TYR C CB    1 
ATOM   10176 C CG    . TYR C  1 323 ? -6.259  96.851  180.690 1.00 71.27  ? 323 TYR C CG    1 
ATOM   10177 C CD1   . TYR C  1 323 ? -5.538  96.352  179.612 1.00 66.06  ? 323 TYR C CD1   1 
ATOM   10178 C CD2   . TYR C  1 323 ? -7.036  97.986  180.488 1.00 74.13  ? 323 TYR C CD2   1 
ATOM   10179 C CE1   . TYR C  1 323 ? -5.591  96.968  178.371 1.00 65.48  ? 323 TYR C CE1   1 
ATOM   10180 C CE2   . TYR C  1 323 ? -7.096  98.608  179.258 1.00 71.97  ? 323 TYR C CE2   1 
ATOM   10181 C CZ    . TYR C  1 323 ? -6.372  98.095  178.200 1.00 70.54  ? 323 TYR C CZ    1 
ATOM   10182 O OH    . TYR C  1 323 ? -6.431  98.718  176.974 1.00 70.72  ? 323 TYR C OH    1 
ATOM   10183 N N     . LEU C  1 324 ? -7.408  93.227  183.524 1.00 70.72  ? 324 LEU C N     1 
ATOM   10184 C CA    . LEU C  1 324 ? -7.244  92.337  184.673 1.00 68.99  ? 324 LEU C CA    1 
ATOM   10185 C C     . LEU C  1 324 ? -5.982  91.495  184.563 1.00 69.92  ? 324 LEU C C     1 
ATOM   10186 O O     . LEU C  1 324 ? -5.798  90.746  183.598 1.00 70.65  ? 324 LEU C O     1 
ATOM   10187 C CB    . LEU C  1 324 ? -8.465  91.429  184.829 1.00 69.83  ? 324 LEU C CB    1 
ATOM   10188 C CG    . LEU C  1 324 ? -9.767  92.174  185.104 1.00 71.41  ? 324 LEU C CG    1 
ATOM   10189 C CD1   . LEU C  1 324 ? -10.963 91.242  185.080 1.00 73.10  ? 324 LEU C CD1   1 
ATOM   10190 C CD2   . LEU C  1 324 ? -9.692  92.911  186.432 1.00 73.79  ? 324 LEU C CD2   1 
ATOM   10191 N N     . GLU C  1 325 ? -5.111  91.634  185.557 1.00 70.24  ? 325 GLU C N     1 
ATOM   10192 C CA    . GLU C  1 325 ? -3.923  90.809  185.637 1.00 68.21  ? 325 GLU C CA    1 
ATOM   10193 C C     . GLU C  1 325 ? -4.214  89.564  186.447 1.00 72.04  ? 325 GLU C C     1 
ATOM   10194 O O     . GLU C  1 325 ? -4.895  89.620  187.471 1.00 73.55  ? 325 GLU C O     1 
ATOM   10195 C CB    . GLU C  1 325 ? -2.759  91.579  186.255 1.00 73.13  ? 325 GLU C CB    1 
ATOM   10196 C CG    . GLU C  1 325 ? -1.967  92.397  185.262 1.00 69.82  ? 325 GLU C CG    1 
ATOM   10197 C CD    . GLU C  1 325 ? -0.738  93.028  185.879 1.00 74.59  ? 325 GLU C CD    1 
ATOM   10198 O OE1   . GLU C  1 325 ? -0.414  92.698  187.038 1.00 72.27  ? 325 GLU C OE1   1 
ATOM   10199 O OE2   . GLU C  1 325 ? -0.096  93.857  185.203 1.00 71.46  ? 325 GLU C OE2   1 
ATOM   10200 N N     . MET C  1 326 ? -3.694  88.440  185.971 1.00 71.90  ? 326 MET C N     1 
ATOM   10201 C CA    . MET C  1 326 ? -3.882  87.153  186.620 1.00 68.38  ? 326 MET C CA    1 
ATOM   10202 C C     . MET C  1 326 ? -2.891  86.162  186.027 1.00 67.32  ? 326 MET C C     1 
ATOM   10203 O O     . MET C  1 326 ? -2.190  86.481  185.065 1.00 67.11  ? 326 MET C O     1 
ATOM   10204 C CB    . MET C  1 326 ? -5.322  86.661  186.453 1.00 67.95  ? 326 MET C CB    1 
ATOM   10205 C CG    . MET C  1 326 ? -5.841  86.683  185.023 1.00 68.65  ? 326 MET C CG    1 
ATOM   10206 S SD    . MET C  1 326 ? -7.592  86.257  184.917 1.00 62.09  ? 326 MET C SD    1 
ATOM   10207 C CE    . MET C  1 326 ? -8.363  87.828  185.292 1.00 65.85  ? 326 MET C CE    1 
ATOM   10208 N N     . SER C  1 327 ? -2.819  84.966  186.597 1.00 66.81  ? 327 SER C N     1 
ATOM   10209 C CA    . SER C  1 327 ? -1.910  83.956  186.075 1.00 64.74  ? 327 SER C CA    1 
ATOM   10210 C C     . SER C  1 327 ? -2.450  83.421  184.757 1.00 64.86  ? 327 SER C C     1 
ATOM   10211 O O     . SER C  1 327 ? -3.562  83.764  184.349 1.00 65.10  ? 327 SER C O     1 
ATOM   10212 C CB    . SER C  1 327 ? -1.713  82.818  187.078 1.00 65.14  ? 327 SER C CB    1 
ATOM   10213 O OG    . SER C  1 327 ? -2.880  82.028  187.200 1.00 67.46  ? 327 SER C OG    1 
ATOM   10214 N N     . TRP C  1 328 ? -1.660  82.585  184.092 1.00 66.04  ? 328 TRP C N     1 
ATOM   10215 C CA    . TRP C  1 328 ? -2.057  82.031  182.804 1.00 62.76  ? 328 TRP C CA    1 
ATOM   10216 C C     . TRP C  1 328 ? -3.334  81.212  182.909 1.00 58.95  ? 328 TRP C C     1 
ATOM   10217 O O     . TRP C  1 328 ? -4.258  81.375  182.110 1.00 59.23  ? 328 TRP C O     1 
ATOM   10218 C CB    . TRP C  1 328 ? -0.956  81.152  182.218 1.00 56.84  ? 328 TRP C CB    1 
ATOM   10219 C CG    . TRP C  1 328 ? -1.473  80.355  181.069 1.00 59.88  ? 328 TRP C CG    1 
ATOM   10220 C CD1   . TRP C  1 328 ? -1.798  80.829  179.841 1.00 57.79  ? 328 TRP C CD1   1 
ATOM   10221 C CD2   . TRP C  1 328 ? -1.759  78.950  181.046 1.00 55.25  ? 328 TRP C CD2   1 
ATOM   10222 N NE1   . TRP C  1 328 ? -2.256  79.812  179.042 1.00 58.36  ? 328 TRP C NE1   1 
ATOM   10223 C CE2   . TRP C  1 328 ? -2.242  78.647  179.758 1.00 58.74  ? 328 TRP C CE2   1 
ATOM   10224 C CE3   . TRP C  1 328 ? -1.647  77.921  181.985 1.00 55.96  ? 328 TRP C CE3   1 
ATOM   10225 C CZ2   . TRP C  1 328 ? -2.616  77.357  179.385 1.00 56.65  ? 328 TRP C CZ2   1 
ATOM   10226 C CZ3   . TRP C  1 328 ? -2.018  76.639  181.612 1.00 57.77  ? 328 TRP C CZ3   1 
ATOM   10227 C CH2   . TRP C  1 328 ? -2.496  76.369  180.323 1.00 57.76  ? 328 TRP C CH2   1 
ATOM   10228 N N     . GLY C  1 329 ? -3.363  80.321  183.893 1.00 57.07  ? 329 GLY C N     1 
ATOM   10229 C CA    . GLY C  1 329 ? -4.498  79.444  184.100 1.00 59.09  ? 329 GLY C CA    1 
ATOM   10230 C C     . GLY C  1 329 ? -5.767  80.206  184.419 1.00 63.80  ? 329 GLY C C     1 
ATOM   10231 O O     . GLY C  1 329 ? -6.831  79.908  183.879 1.00 62.93  ? 329 GLY C O     1 
ATOM   10232 N N     . GLU C  1 330 ? -5.648  81.199  185.295 1.00 63.99  ? 330 GLU C N     1 
ATOM   10233 C CA    . GLU C  1 330 ? -6.790  82.011  185.701 1.00 64.49  ? 330 GLU C CA    1 
ATOM   10234 C C     . GLU C  1 330 ? -7.390  82.757  184.514 1.00 61.40  ? 330 GLU C C     1 
ATOM   10235 O O     . GLU C  1 330 ? -8.606  82.929  184.432 1.00 65.49  ? 330 GLU C O     1 
ATOM   10236 C CB    . GLU C  1 330 ? -6.382  83.000  186.793 1.00 66.31  ? 330 GLU C CB    1 
ATOM   10237 C CG    . GLU C  1 330 ? -5.938  82.335  188.087 1.00 71.30  ? 330 GLU C CG    1 
ATOM   10238 C CD    . GLU C  1 330 ? -5.259  83.301  189.039 1.00 71.81  ? 330 GLU C CD    1 
ATOM   10239 O OE1   . GLU C  1 330 ? -5.334  84.524  188.800 1.00 71.49  ? 330 GLU C OE1   1 
ATOM   10240 O OE2   . GLU C  1 330 ? -4.643  82.835  190.020 1.00 74.46  ? 330 GLU C OE2   1 
ATOM   10241 N N     . SER C  1 331 ? -6.533  83.194  183.597 1.00 60.17  ? 331 SER C N     1 
ATOM   10242 C CA    . SER C  1 331 ? -6.986  83.908  182.409 1.00 61.88  ? 331 SER C CA    1 
ATOM   10243 C C     . SER C  1 331 ? -7.818  83.006  181.504 1.00 63.92  ? 331 SER C C     1 
ATOM   10244 O O     . SER C  1 331 ? -8.842  83.429  180.972 1.00 66.18  ? 331 SER C O     1 
ATOM   10245 C CB    . SER C  1 331 ? -5.796  84.479  181.639 1.00 60.17  ? 331 SER C CB    1 
ATOM   10246 O OG    . SER C  1 331 ? -4.853  83.471  181.331 1.00 61.90  ? 331 SER C OG    1 
ATOM   10247 N N     . PHE C  1 332 ? -7.380  81.763  181.332 1.00 62.97  ? 332 PHE C N     1 
ATOM   10248 C CA    . PHE C  1 332 ? -8.123  80.811  180.514 1.00 61.89  ? 332 PHE C CA    1 
ATOM   10249 C C     . PHE C  1 332 ? -9.403  80.372  181.210 1.00 62.11  ? 332 PHE C C     1 
ATOM   10250 O O     . PHE C  1 332 ? -10.404 80.086  180.554 1.00 64.95  ? 332 PHE C O     1 
ATOM   10251 C CB    . PHE C  1 332 ? -7.265  79.595  180.171 1.00 59.10  ? 332 PHE C CB    1 
ATOM   10252 C CG    . PHE C  1 332 ? -6.460  79.765  178.917 1.00 64.40  ? 332 PHE C CG    1 
ATOM   10253 C CD1   . PHE C  1 332 ? -6.156  81.030  178.444 1.00 66.41  ? 332 PHE C CD1   1 
ATOM   10254 C CD2   . PHE C  1 332 ? -6.028  78.663  178.198 1.00 62.25  ? 332 PHE C CD2   1 
ATOM   10255 C CE1   . PHE C  1 332 ? -5.422  81.194  177.286 1.00 61.14  ? 332 PHE C CE1   1 
ATOM   10256 C CE2   . PHE C  1 332 ? -5.295  78.821  177.037 1.00 62.13  ? 332 PHE C CE2   1 
ATOM   10257 C CZ    . PHE C  1 332 ? -4.992  80.089  176.581 1.00 63.90  ? 332 PHE C CZ    1 
ATOM   10258 N N     . ALA C  1 333 ? -9.367  80.317  182.538 1.00 61.00  ? 333 ALA C N     1 
ATOM   10259 C CA    . ALA C  1 333 ? -10.572 80.064  183.314 1.00 65.17  ? 333 ALA C CA    1 
ATOM   10260 C C     . ALA C  1 333 ? -11.538 81.228  183.127 1.00 67.28  ? 333 ALA C C     1 
ATOM   10261 O O     . ALA C  1 333 ? -12.728 81.033  182.878 1.00 66.87  ? 333 ALA C O     1 
ATOM   10262 C CB    . ALA C  1 333 ? -10.236 79.867  184.785 1.00 64.68  ? 333 ALA C CB    1 
ATOM   10263 N N     . TYR C  1 334 ? -11.001 82.440  183.234 1.00 67.46  ? 334 TYR C N     1 
ATOM   10264 C CA    . TYR C  1 334 ? -11.772 83.665  183.052 1.00 68.71  ? 334 TYR C CA    1 
ATOM   10265 C C     . TYR C  1 334 ? -12.386 83.753  181.658 1.00 71.32  ? 334 TYR C C     1 
ATOM   10266 O O     . TYR C  1 334 ? -13.593 83.965  181.513 1.00 68.65  ? 334 TYR C O     1 
ATOM   10267 C CB    . TYR C  1 334 ? -10.886 84.885  183.308 1.00 70.02  ? 334 TYR C CB    1 
ATOM   10268 C CG    . TYR C  1 334 ? -11.514 86.198  182.904 1.00 72.12  ? 334 TYR C CG    1 
ATOM   10269 C CD1   . TYR C  1 334 ? -12.555 86.744  183.641 1.00 74.87  ? 334 TYR C CD1   1 
ATOM   10270 C CD2   . TYR C  1 334 ? -11.068 86.892  181.785 1.00 70.61  ? 334 TYR C CD2   1 
ATOM   10271 C CE1   . TYR C  1 334 ? -13.138 87.942  183.277 1.00 73.46  ? 334 TYR C CE1   1 
ATOM   10272 C CE2   . TYR C  1 334 ? -11.644 88.093  181.414 1.00 73.42  ? 334 TYR C CE2   1 
ATOM   10273 C CZ    . TYR C  1 334 ? -12.679 88.612  182.164 1.00 74.35  ? 334 TYR C CZ    1 
ATOM   10274 O OH    . TYR C  1 334 ? -13.258 89.806  181.803 1.00 75.84  ? 334 TYR C OH    1 
ATOM   10275 N N     . LEU C  1 335 ? -11.551 83.586  180.636 1.00 68.76  ? 335 LEU C N     1 
ATOM   10276 C CA    . LEU C  1 335 ? -11.989 83.713  179.249 1.00 70.43  ? 335 LEU C CA    1 
ATOM   10277 C C     . LEU C  1 335 ? -13.016 82.649  178.862 1.00 71.29  ? 335 LEU C C     1 
ATOM   10278 O O     . LEU C  1 335 ? -13.803 82.850  177.938 1.00 72.35  ? 335 LEU C O     1 
ATOM   10279 C CB    . LEU C  1 335 ? -10.783 83.646  178.308 1.00 68.91  ? 335 LEU C CB    1 
ATOM   10280 C CG    . LEU C  1 335 ? -9.867  84.872  178.320 1.00 66.06  ? 335 LEU C CG    1 
ATOM   10281 C CD1   . LEU C  1 335 ? -8.555  84.585  177.612 1.00 70.75  ? 335 LEU C CD1   1 
ATOM   10282 C CD2   . LEU C  1 335 ? -10.563 86.063  177.683 1.00 68.57  ? 335 LEU C CD2   1 
ATOM   10283 N N     . ALA C  1 336 ? -13.009 81.524  179.571 1.00 68.47  ? 336 ALA C N     1 
ATOM   10284 C CA    . ALA C  1 336 ? -13.971 80.459  179.312 1.00 71.44  ? 336 ALA C CA    1 
ATOM   10285 C C     . ALA C  1 336 ? -15.311 80.756  179.977 1.00 73.75  ? 336 ALA C C     1 
ATOM   10286 O O     . ALA C  1 336 ? -16.263 79.987  179.844 1.00 72.28  ? 336 ALA C O     1 
ATOM   10287 C CB    . ALA C  1 336 ? -13.430 79.124  179.791 1.00 63.27  ? 336 ALA C CB    1 
ATOM   10288 N N     . GLY C  1 337 ? -15.378 81.873  180.695 1.00 73.53  ? 337 GLY C N     1 
ATOM   10289 C CA    . GLY C  1 337 ? -16.592 82.268  181.382 1.00 73.59  ? 337 GLY C CA    1 
ATOM   10290 C C     . GLY C  1 337 ? -16.765 81.544  182.703 1.00 72.60  ? 337 GLY C C     1 
ATOM   10291 O O     . GLY C  1 337 ? -17.884 81.366  183.183 1.00 69.21  ? 337 GLY C O     1 
ATOM   10292 N N     . LEU C  1 338 ? -15.650 81.124  183.291 1.00 72.39  ? 338 LEU C N     1 
ATOM   10293 C CA    . LEU C  1 338 ? -15.683 80.393  184.552 1.00 76.87  ? 338 LEU C CA    1 
ATOM   10294 C C     . LEU C  1 338 ? -15.185 81.256  185.706 1.00 79.58  ? 338 LEU C C     1 
ATOM   10295 O O     . LEU C  1 338 ? -14.646 82.342  185.494 1.00 78.56  ? 338 LEU C O     1 
ATOM   10296 C CB    . LEU C  1 338 ? -14.849 79.115  184.453 1.00 75.47  ? 338 LEU C CB    1 
ATOM   10297 C CG    . LEU C  1 338 ? -15.276 78.145  183.353 1.00 76.34  ? 338 LEU C CG    1 
ATOM   10298 C CD1   . LEU C  1 338 ? -14.377 76.918  183.337 1.00 71.30  ? 338 LEU C CD1   1 
ATOM   10299 C CD2   . LEU C  1 338 ? -16.736 77.748  183.523 1.00 75.55  ? 338 LEU C CD2   1 
ATOM   10300 N N     . GLU C  1 339 ? -15.370 80.766  186.926 1.00 82.08  ? 339 GLU C N     1 
ATOM   10301 C CA    . GLU C  1 339 ? -14.960 81.504  188.114 1.00 83.66  ? 339 GLU C CA    1 
ATOM   10302 C C     . GLU C  1 339 ? -13.597 81.049  188.628 1.00 79.72  ? 339 GLU C C     1 
ATOM   10303 O O     . GLU C  1 339 ? -12.731 81.873  188.919 1.00 81.56  ? 339 GLU C O     1 
ATOM   10304 C CB    . GLU C  1 339 ? -16.008 81.359  189.220 1.00 86.32  ? 339 GLU C CB    1 
ATOM   10305 C CG    . GLU C  1 339 ? -17.318 82.073  188.930 1.00 89.34  ? 339 GLU C CG    1 
ATOM   10306 C CD    . GLU C  1 339 ? -18.353 81.843  190.012 1.00 97.53  ? 339 GLU C CD    1 
ATOM   10307 O OE1   . GLU C  1 339 ? -18.252 80.817  190.718 1.00 94.39  ? 339 GLU C OE1   1 
ATOM   10308 O OE2   . GLU C  1 339 ? -19.262 82.686  190.160 1.00 100.30 ? 339 GLU C OE2   1 
ATOM   10309 N N     . THR C  1 340 ? -13.408 79.738  188.744 1.00 81.50  ? 340 THR C N     1 
ATOM   10310 C CA    . THR C  1 340 ? -12.147 79.208  189.255 1.00 82.06  ? 340 THR C CA    1 
ATOM   10311 C C     . THR C  1 340 ? -11.452 78.284  188.256 1.00 79.01  ? 340 THR C C     1 
ATOM   10312 O O     . THR C  1 340 ? -12.065 77.805  187.302 1.00 76.78  ? 340 THR C O     1 
ATOM   10313 C CB    . THR C  1 340 ? -12.354 78.444  190.580 1.00 84.02  ? 340 THR C CB    1 
ATOM   10314 O OG1   . THR C  1 340 ? -11.090 77.972  191.065 1.00 81.62  ? 340 THR C OG1   1 
ATOM   10315 C CG2   . THR C  1 340 ? -13.290 77.265  190.379 1.00 79.53  ? 340 THR C CG2   1 
ATOM   10316 N N     . VAL C  1 341 ? -10.165 78.042  188.492 1.00 78.28  ? 341 VAL C N     1 
ATOM   10317 C CA    . VAL C  1 341 ? -9.342  77.215  187.613 1.00 74.59  ? 341 VAL C CA    1 
ATOM   10318 C C     . VAL C  1 341 ? -9.756  75.743  187.696 1.00 73.95  ? 341 VAL C C     1 
ATOM   10319 O O     . VAL C  1 341 ? -9.640  74.997  186.721 1.00 73.64  ? 341 VAL C O     1 
ATOM   10320 C CB    . VAL C  1 341 ? -7.837  77.377  187.961 1.00 66.49  ? 341 VAL C CB    1 
ATOM   10321 C CG1   . VAL C  1 341 ? -6.986  76.303  187.297 1.00 67.35  ? 341 VAL C CG1   1 
ATOM   10322 C CG2   . VAL C  1 341 ? -7.351  78.761  187.560 1.00 69.78  ? 341 VAL C CG2   1 
ATOM   10323 N N     . SER C  1 342 ? -10.269 75.338  188.854 1.00 73.43  ? 342 SER C N     1 
ATOM   10324 C CA    . SER C  1 342 ? -10.698 73.957  189.064 1.00 73.79  ? 342 SER C CA    1 
ATOM   10325 C C     . SER C  1 342 ? -11.877 73.565  188.174 1.00 74.42  ? 342 SER C C     1 
ATOM   10326 O O     . SER C  1 342 ? -12.107 72.383  187.924 1.00 73.58  ? 342 SER C O     1 
ATOM   10327 C CB    . SER C  1 342 ? -11.064 73.730  190.533 1.00 77.07  ? 342 SER C CB    1 
ATOM   10328 O OG    . SER C  1 342 ? -9.901  73.644  191.339 1.00 79.02  ? 342 SER C OG    1 
ATOM   10329 N N     . GLN C  1 343 ? -12.618 74.561  187.699 1.00 72.18  ? 343 GLN C N     1 
ATOM   10330 C CA    . GLN C  1 343 ? -13.750 74.326  186.811 1.00 75.28  ? 343 GLN C CA    1 
ATOM   10331 C C     . GLN C  1 343 ? -13.302 73.872  185.426 1.00 70.30  ? 343 GLN C C     1 
ATOM   10332 O O     . GLN C  1 343 ? -14.085 73.291  184.672 1.00 67.87  ? 343 GLN C O     1 
ATOM   10333 C CB    . GLN C  1 343 ? -14.602 75.588  186.694 1.00 74.75  ? 343 GLN C CB    1 
ATOM   10334 C CG    . GLN C  1 343 ? -15.456 75.870  187.912 1.00 79.69  ? 343 GLN C CG    1 
ATOM   10335 C CD    . GLN C  1 343 ? -16.169 77.202  187.821 1.00 83.84  ? 343 GLN C CD    1 
ATOM   10336 O OE1   . GLN C  1 343 ? -15.534 78.257  187.810 1.00 84.85  ? 343 GLN C OE1   1 
ATOM   10337 N NE2   . GLN C  1 343 ? -17.494 77.162  187.744 1.00 83.06  ? 343 GLN C NE2   1 
ATOM   10338 N N     . LEU C  1 344 ? -12.045 74.153  185.093 1.00 66.90  ? 344 LEU C N     1 
ATOM   10339 C CA    . LEU C  1 344 ? -11.446 73.656  183.862 1.00 61.29  ? 344 LEU C CA    1 
ATOM   10340 C C     . LEU C  1 344 ? -11.408 72.131  183.889 1.00 59.50  ? 344 LEU C C     1 
ATOM   10341 O O     . LEU C  1 344 ? -11.577 71.477  182.863 1.00 55.31  ? 344 LEU C O     1 
ATOM   10342 C CB    . LEU C  1 344 ? -10.031 74.218  183.674 1.00 60.43  ? 344 LEU C CB    1 
ATOM   10343 C CG    . LEU C  1 344 ? -9.870  75.732  183.503 1.00 62.95  ? 344 LEU C CG    1 
ATOM   10344 C CD1   . LEU C  1 344 ? -8.400  76.134  183.535 1.00 60.08  ? 344 LEU C CD1   1 
ATOM   10345 C CD2   . LEU C  1 344 ? -10.526 76.196  182.213 1.00 55.34  ? 344 LEU C CD2   1 
ATOM   10346 N N     . ASN C  1 345 ? -11.206 71.574  185.080 1.00 60.54  ? 345 ASN C N     1 
ATOM   10347 C CA    . ASN C  1 345 ? -11.029 70.134  185.249 1.00 58.44  ? 345 ASN C CA    1 
ATOM   10348 C C     . ASN C  1 345 ? -12.351 69.358  185.297 1.00 62.64  ? 345 ASN C C     1 
ATOM   10349 O O     . ASN C  1 345 ? -12.372 68.172  185.628 1.00 64.95  ? 345 ASN C O     1 
ATOM   10350 C CB    . ASN C  1 345 ? -10.220 69.860  186.518 1.00 59.43  ? 345 ASN C CB    1 
ATOM   10351 C CG    . ASN C  1 345 ? -9.586  68.482  186.525 1.00 64.25  ? 345 ASN C CG    1 
ATOM   10352 O OD1   . ASN C  1 345 ? -9.122  67.993  185.496 1.00 64.90  ? 345 ASN C OD1   1 
ATOM   10353 N ND2   . ASN C  1 345 ? -9.571  67.845  187.691 1.00 66.24  ? 345 ASN C ND2   1 
ATOM   10354 N N     . ASN C  1 346 ? -13.452 70.026  184.967 1.00 64.28  ? 346 ASN C N     1 
ATOM   10355 C CA    . ASN C  1 346 ? -14.749 69.362  184.887 1.00 64.82  ? 346 ASN C CA    1 
ATOM   10356 C C     . ASN C  1 346 ? -15.216 69.260  183.437 1.00 65.24  ? 346 ASN C C     1 
ATOM   10357 O O     . ASN C  1 346 ? -15.699 70.233  182.863 1.00 68.92  ? 346 ASN C O     1 
ATOM   10358 C CB    . ASN C  1 346 ? -15.783 70.106  185.737 1.00 72.58  ? 346 ASN C CB    1 
ATOM   10359 C CG    . ASN C  1 346 ? -17.136 69.408  185.766 1.00 74.07  ? 346 ASN C CG    1 
ATOM   10360 O OD1   . ASN C  1 346 ? -17.317 68.339  185.181 1.00 72.54  ? 346 ASN C OD1   1 
ATOM   10361 N ND2   . ASN C  1 346 ? -18.091 70.010  186.462 1.00 73.01  ? 346 ASN C ND2   1 
ATOM   10362 N N     . ARG C  1 347 ? -15.079 68.073  182.855 1.00 62.61  ? 347 ARG C N     1 
ATOM   10363 C CA    . ARG C  1 347 ? -15.378 67.863  181.440 1.00 63.69  ? 347 ARG C CA    1 
ATOM   10364 C C     . ARG C  1 347 ? -16.875 67.900  181.116 1.00 65.40  ? 347 ARG C C     1 
ATOM   10365 O O     . ARG C  1 347 ? -17.260 68.133  179.969 1.00 62.33  ? 347 ARG C O     1 
ATOM   10366 C CB    . ARG C  1 347 ? -14.789 66.527  180.978 1.00 62.72  ? 347 ARG C CB    1 
ATOM   10367 C CG    . ARG C  1 347 ? -15.355 65.317  181.709 1.00 60.40  ? 347 ARG C CG    1 
ATOM   10368 C CD    . ARG C  1 347 ? -14.610 64.033  181.360 1.00 57.07  ? 347 ARG C CD    1 
ATOM   10369 N NE    . ARG C  1 347 ? -14.671 63.707  179.936 1.00 56.42  ? 347 ARG C NE    1 
ATOM   10370 C CZ    . ARG C  1 347 ? -13.605 63.479  179.174 1.00 56.67  ? 347 ARG C CZ    1 
ATOM   10371 N NH1   . ARG C  1 347 ? -12.388 63.545  179.697 1.00 51.10  ? 347 ARG C NH1   1 
ATOM   10372 N NH2   . ARG C  1 347 ? -13.754 63.183  177.889 1.00 51.39  ? 347 ARG C NH2   1 
ATOM   10373 N N     . PHE C  1 348 ? -17.715 67.667  182.119 1.00 65.93  ? 348 PHE C N     1 
ATOM   10374 C CA    . PHE C  1 348 ? -19.158 67.596  181.896 1.00 70.07  ? 348 PHE C CA    1 
ATOM   10375 C C     . PHE C  1 348 ? -19.863 68.882  182.320 1.00 78.75  ? 348 PHE C C     1 
ATOM   10376 O O     . PHE C  1 348 ? -21.090 68.919  182.452 1.00 77.65  ? 348 PHE C O     1 
ATOM   10377 C CB    . PHE C  1 348 ? -19.752 66.399  182.644 1.00 65.70  ? 348 PHE C CB    1 
ATOM   10378 C CG    . PHE C  1 348 ? -19.122 65.086  182.280 1.00 64.70  ? 348 PHE C CG    1 
ATOM   10379 C CD1   . PHE C  1 348 ? -19.110 64.652  180.963 1.00 62.16  ? 348 PHE C CD1   1 
ATOM   10380 C CD2   . PHE C  1 348 ? -18.555 64.280  183.255 1.00 64.75  ? 348 PHE C CD2   1 
ATOM   10381 C CE1   . PHE C  1 348 ? -18.531 63.440  180.620 1.00 62.07  ? 348 PHE C CE1   1 
ATOM   10382 C CE2   . PHE C  1 348 ? -17.977 63.064  182.922 1.00 64.01  ? 348 PHE C CE2   1 
ATOM   10383 C CZ    . PHE C  1 348 ? -17.967 62.646  181.603 1.00 61.12  ? 348 PHE C CZ    1 
ATOM   10384 N N     . LEU C  1 349 ? -19.080 69.937  182.523 1.00 79.41  ? 349 LEU C N     1 
ATOM   10385 C CA    . LEU C  1 349 ? -19.621 71.211  182.981 1.00 81.82  ? 349 LEU C CA    1 
ATOM   10386 C C     . LEU C  1 349 ? -20.101 72.070  181.810 1.00 88.79  ? 349 LEU C C     1 
ATOM   10387 O O     . LEU C  1 349 ? -19.331 72.842  181.240 1.00 90.90  ? 349 LEU C O     1 
ATOM   10388 C CB    . LEU C  1 349 ? -18.571 71.970  183.802 1.00 81.96  ? 349 LEU C CB    1 
ATOM   10389 C CG    . LEU C  1 349 ? -19.037 73.183  184.611 1.00 90.31  ? 349 LEU C CG    1 
ATOM   10390 C CD1   . LEU C  1 349 ? -20.305 72.858  185.386 1.00 86.26  ? 349 LEU C CD1   1 
ATOM   10391 C CD2   . LEU C  1 349 ? -17.934 73.635  185.559 1.00 86.48  ? 349 LEU C CD2   1 
ATOM   10392 N N     . LYS C  1 350 ? -21.379 71.943  181.466 1.00 93.79  ? 350 LYS C N     1 
ATOM   10393 C CA    . LYS C  1 350 ? -21.945 72.675  180.337 1.00 96.43  ? 350 LYS C CA    1 
ATOM   10394 C C     . LYS C  1 350 ? -22.819 73.847  180.783 1.00 98.62  ? 350 LYS C C     1 
ATOM   10395 O O     . LYS C  1 350 ? -23.859 73.628  181.417 1.00 102.51 ? 350 LYS C O     1 
ATOM   10396 C CB    . LYS C  1 350 ? -22.764 71.726  179.461 1.00 94.26  ? 350 LYS C CB    1 
ATOM   10397 C CG    . LYS C  1 350 ? -21.936 70.634  178.781 1.00 95.20  ? 350 LYS C CG    1 
ATOM   10398 C CD    . LYS C  1 350 ? -22.799 69.653  177.989 1.00 84.20  ? 350 LYS C CD    1 
ATOM   10399 C CE    . LYS C  1 350 ? -23.636 70.366  176.941 1.00 82.07  ? 350 LYS C CE    1 
ATOM   10400 N NZ    . LYS C  1 350 ? -24.423 69.416  176.107 1.00 74.88  ? 350 LYS C NZ    1 
ATOM   10401 N N     . PHE C  1 351 ? -22.431 75.083  180.454 1.00 102.05 ? 351 PHE C N     1 
ATOM   10402 C CA    . PHE C  1 351 ? -23.325 76.214  180.743 1.00 105.57 ? 351 PHE C CA    1 
ATOM   10403 C C     . PHE C  1 351 ? -24.358 76.408  179.608 1.00 105.44 ? 351 PHE C C     1 
ATOM   10404 O O     . PHE C  1 351 ? -25.544 76.457  179.858 1.00 108.43 ? 351 PHE C O     1 
ATOM   10405 C CB    . PHE C  1 351 ? -22.557 77.523  180.977 1.00 105.45 ? 351 PHE C CB    1 
ATOM   10406 C CG    . PHE C  1 351 ? -23.450 78.643  181.413 1.00 111.60 ? 351 PHE C CG    1 
ATOM   10407 C CD1   . PHE C  1 351 ? -24.595 78.335  182.118 1.00 110.87 ? 351 PHE C CD1   1 
ATOM   10408 C CD2   . PHE C  1 351 ? -23.203 79.967  181.080 1.00 108.24 ? 351 PHE C CD2   1 
ATOM   10409 C CE1   . PHE C  1 351 ? -25.465 79.304  182.509 1.00 106.71 ? 351 PHE C CE1   1 
ATOM   10410 C CE2   . PHE C  1 351 ? -24.078 80.957  181.478 1.00 104.49 ? 351 PHE C CE2   1 
ATOM   10411 C CZ    . PHE C  1 351 ? -25.212 80.621  182.194 1.00 106.29 ? 351 PHE C CZ    1 
ATOM   10412 N N     . ASP C  1 352 ? -23.898 76.494  178.365 1.00 101.81 ? 352 ASP C N     1 
ATOM   10413 C CA    . ASP C  1 352 ? -24.809 76.645  177.239 1.00 97.78  ? 352 ASP C CA    1 
ATOM   10414 C C     . ASP C  1 352 ? -25.190 75.241  176.765 1.00 94.74  ? 352 ASP C C     1 
ATOM   10415 O O     . ASP C  1 352 ? -24.324 74.380  176.630 1.00 99.25  ? 352 ASP C O     1 
ATOM   10416 C CB    . ASP C  1 352 ? -24.183 77.469  176.100 1.00 98.15  ? 352 ASP C CB    1 
ATOM   10417 C CG    . ASP C  1 352 ? -25.224 78.236  175.302 1.00 96.43  ? 352 ASP C CG    1 
ATOM   10418 O OD1   . ASP C  1 352 ? -26.429 78.019  175.551 1.00 92.09  ? 352 ASP C OD1   1 
ATOM   10419 O OD2   . ASP C  1 352 ? -24.842 79.043  174.418 1.00 95.18  ? 352 ASP C OD2   1 
ATOM   10420 N N     . GLU C  1 353 ? -26.481 75.000  176.543 1.00 83.68  ? 353 GLU C N     1 
ATOM   10421 C CA    . GLU C  1 353 ? -26.916 73.744  175.937 1.00 80.62  ? 353 GLU C CA    1 
ATOM   10422 C C     . GLU C  1 353 ? -27.909 73.969  174.806 1.00 72.79  ? 353 GLU C C     1 
ATOM   10423 O O     . GLU C  1 353 ? -29.021 73.444  174.841 1.00 72.09  ? 353 GLU C O     1 
ATOM   10424 C CB    . GLU C  1 353 ? -27.556 72.815  176.971 1.00 85.32  ? 353 GLU C CB    1 
ATOM   10425 C CG    . GLU C  1 353 ? -26.790 72.667  178.271 1.00 91.73  ? 353 GLU C CG    1 
ATOM   10426 C CD    . GLU C  1 353 ? -27.130 73.730  179.298 1.00 99.70  ? 353 GLU C CD    1 
ATOM   10427 O OE1   . GLU C  1 353 ? -27.854 74.702  178.963 1.00 102.20 ? 353 GLU C OE1   1 
ATOM   10428 O OE2   . GLU C  1 353 ? -26.673 73.586  180.448 1.00 101.74 ? 353 GLU C OE2   1 
ATOM   10429 N N     . ARG C  1 354 ? -27.512 74.740  173.804 1.00 70.27  ? 354 ARG C N     1 
ATOM   10430 C CA    . ARG C  1 354 ? -28.387 75.011  172.678 1.00 69.93  ? 354 ARG C CA    1 
ATOM   10431 C C     . ARG C  1 354 ? -27.931 74.252  171.442 1.00 64.04  ? 354 ARG C C     1 
ATOM   10432 O O     . ARG C  1 354 ? -26.741 73.993  171.267 1.00 61.69  ? 354 ARG C O     1 
ATOM   10433 C CB    . ARG C  1 354 ? -28.432 76.511  172.394 1.00 73.20  ? 354 ARG C CB    1 
ATOM   10434 C CG    . ARG C  1 354 ? -28.993 77.336  173.542 1.00 77.12  ? 354 ARG C CG    1 
ATOM   10435 C CD    . ARG C  1 354 ? -29.139 78.792  173.136 1.00 76.43  ? 354 ARG C CD    1 
ATOM   10436 N NE    . ARG C  1 354 ? -27.844 79.412  172.872 1.00 79.84  ? 354 ARG C NE    1 
ATOM   10437 C CZ    . ARG C  1 354 ? -27.677 80.550  172.205 1.00 86.41  ? 354 ARG C CZ    1 
ATOM   10438 N NH1   . ARG C  1 354 ? -28.726 81.200  171.720 1.00 82.76  ? 354 ARG C NH1   1 
ATOM   10439 N NH2   . ARG C  1 354 ? -26.456 81.036  172.017 1.00 82.65  ? 354 ARG C NH2   1 
ATOM   10440 N N     . ALA C  1 355 ? -28.885 73.874  170.600 1.00 65.42  ? 355 ALA C N     1 
ATOM   10441 C CA    . ALA C  1 355 ? -28.559 73.347  169.287 1.00 62.62  ? 355 ALA C CA    1 
ATOM   10442 C C     . ALA C  1 355 ? -27.965 74.481  168.473 1.00 62.61  ? 355 ALA C C     1 
ATOM   10443 O O     . ALA C  1 355 ? -28.353 75.637  168.642 1.00 61.30  ? 355 ALA C O     1 
ATOM   10444 C CB    . ALA C  1 355 ? -29.788 72.777  168.609 1.00 57.43  ? 355 ALA C CB    1 
ATOM   10445 N N     . PHE C  1 356 ? -27.016 74.164  167.603 1.00 56.65  ? 356 PHE C N     1 
ATOM   10446 C CA    . PHE C  1 356 ? -26.436 75.195  166.759 1.00 56.80  ? 356 PHE C CA    1 
ATOM   10447 C C     . PHE C  1 356 ? -25.960 74.646  165.426 1.00 56.03  ? 356 PHE C C     1 
ATOM   10448 O O     . PHE C  1 356 ? -25.737 73.446  165.267 1.00 60.68  ? 356 PHE C O     1 
ATOM   10449 C CB    . PHE C  1 356 ? -25.275 75.893  167.478 1.00 50.80  ? 356 PHE C CB    1 
ATOM   10450 C CG    . PHE C  1 356 ? -24.100 74.995  167.754 1.00 56.20  ? 356 PHE C CG    1 
ATOM   10451 C CD1   . PHE C  1 356 ? -23.045 74.915  166.858 1.00 49.71  ? 356 PHE C CD1   1 
ATOM   10452 C CD2   . PHE C  1 356 ? -24.047 74.236  168.911 1.00 55.65  ? 356 PHE C CD2   1 
ATOM   10453 C CE1   . PHE C  1 356 ? -21.964 74.090  167.108 1.00 54.00  ? 356 PHE C CE1   1 
ATOM   10454 C CE2   . PHE C  1 356 ? -22.966 73.411  169.167 1.00 55.48  ? 356 PHE C CE2   1 
ATOM   10455 C CZ    . PHE C  1 356 ? -21.924 73.338  168.264 1.00 51.69  ? 356 PHE C CZ    1 
ATOM   10456 N N     . LYS C  1 357 ? -25.827 75.551  164.467 1.00 52.74  ? 357 LYS C N     1 
ATOM   10457 C CA    . LYS C  1 357 ? -25.185 75.277  163.194 1.00 54.27  ? 357 LYS C CA    1 
ATOM   10458 C C     . LYS C  1 357 ? -24.294 76.475  162.924 1.00 57.36  ? 357 LYS C C     1 
ATOM   10459 O O     . LYS C  1 357 ? -24.679 77.615  163.191 1.00 57.88  ? 357 LYS C O     1 
ATOM   10460 C CB    . LYS C  1 357 ? -26.216 75.061  162.080 1.00 58.07  ? 357 LYS C CB    1 
ATOM   10461 C CG    . LYS C  1 357 ? -25.681 75.201  160.659 1.00 58.90  ? 357 LYS C CG    1 
ATOM   10462 C CD    . LYS C  1 357 ? -24.645 74.149  160.298 1.00 71.46  ? 357 LYS C CD    1 
ATOM   10463 C CE    . LYS C  1 357 ? -24.117 74.391  158.889 1.00 73.56  ? 357 LYS C CE    1 
ATOM   10464 N NZ    . LYS C  1 357 ? -23.050 73.432  158.489 1.00 76.87  ? 357 LYS C NZ    1 
ATOM   10465 N N     . THR C  1 358 ? -23.090 76.221  162.435 1.00 57.20  ? 358 THR C N     1 
ATOM   10466 C CA    . THR C  1 358 ? -22.135 77.295  162.231 1.00 53.88  ? 358 THR C CA    1 
ATOM   10467 C C     . THR C  1 358 ? -21.415 77.149  160.906 1.00 56.95  ? 358 THR C C     1 
ATOM   10468 O O     . THR C  1 358 ? -21.362 76.063  160.330 1.00 58.96  ? 358 THR C O     1 
ATOM   10469 C CB    . THR C  1 358 ? -21.094 77.340  163.357 1.00 52.20  ? 358 THR C CB    1 
ATOM   10470 O OG1   . THR C  1 358 ? -20.126 78.358  163.075 1.00 53.32  ? 358 THR C OG1   1 
ATOM   10471 C CG2   . THR C  1 358 ? -20.397 76.007  163.464 1.00 49.34  ? 358 THR C CG2   1 
ATOM   10472 N N     . LYS C  1 359 ? -20.871 78.258  160.422 1.00 52.04  ? 359 LYS C N     1 
ATOM   10473 C CA    . LYS C  1 359 ? -20.071 78.254  159.209 1.00 49.50  ? 359 LYS C CA    1 
ATOM   10474 C C     . LYS C  1 359 ? -18.885 79.183  159.434 1.00 53.68  ? 359 LYS C C     1 
ATOM   10475 O O     . LYS C  1 359 ? -18.833 79.899  160.435 1.00 51.08  ? 359 LYS C O     1 
ATOM   10476 C CB    . LYS C  1 359 ? -20.902 78.684  157.999 1.00 55.75  ? 359 LYS C CB    1 
ATOM   10477 C CG    . LYS C  1 359 ? -22.135 77.814  157.745 1.00 59.87  ? 359 LYS C CG    1 
ATOM   10478 C CD    . LYS C  1 359 ? -22.914 78.280  156.530 1.00 57.18  ? 359 LYS C CD    1 
ATOM   10479 C CE    . LYS C  1 359 ? -22.222 77.872  155.242 1.00 59.11  ? 359 LYS C CE    1 
ATOM   10480 N NZ    . LYS C  1 359 ? -22.236 76.405  155.027 1.00 58.88  ? 359 LYS C NZ    1 
ATOM   10481 N N     . VAL C  1 360 ? -17.924 79.169  158.522 1.00 47.31  ? 360 VAL C N     1 
ATOM   10482 C CA    . VAL C  1 360 ? -16.716 79.950  158.726 1.00 46.31  ? 360 VAL C CA    1 
ATOM   10483 C C     . VAL C  1 360 ? -16.159 80.459  157.407 1.00 46.58  ? 360 VAL C C     1 
ATOM   10484 O O     . VAL C  1 360 ? -16.394 79.870  156.353 1.00 43.67  ? 360 VAL C O     1 
ATOM   10485 C CB    . VAL C  1 360 ? -15.637 79.117  159.466 1.00 50.41  ? 360 VAL C CB    1 
ATOM   10486 C CG1   . VAL C  1 360 ? -15.044 78.056  158.542 1.00 41.51  ? 360 VAL C CG1   1 
ATOM   10487 C CG2   . VAL C  1 360 ? -14.546 80.018  160.035 1.00 48.73  ? 360 VAL C CG2   1 
ATOM   10488 N N     . ASP C  1 361 ? -15.443 81.574  157.473 1.00 45.01  ? 361 ASP C N     1 
ATOM   10489 C CA    . ASP C  1 361 ? -14.728 82.103  156.325 1.00 47.86  ? 361 ASP C CA    1 
ATOM   10490 C C     . ASP C  1 361 ? -13.305 82.451  156.737 1.00 50.06  ? 361 ASP C C     1 
ATOM   10491 O O     . ASP C  1 361 ? -13.048 82.775  157.895 1.00 46.34  ? 361 ASP C O     1 
ATOM   10492 C CB    . ASP C  1 361 ? -15.436 83.337  155.760 1.00 55.13  ? 361 ASP C CB    1 
ATOM   10493 C CG    . ASP C  1 361 ? -16.439 82.990  154.676 1.00 55.29  ? 361 ASP C CG    1 
ATOM   10494 O OD1   . ASP C  1 361 ? -16.094 82.186  153.785 1.00 59.50  ? 361 ASP C OD1   1 
ATOM   10495 O OD2   . ASP C  1 361 ? -17.571 83.518  154.715 1.00 61.04  ? 361 ASP C OD2   1 
ATOM   10496 N N     . LEU C  1 362 ? -12.376 82.358  155.797 1.00 45.96  ? 362 LEU C N     1 
ATOM   10497 C CA    . LEU C  1 362 ? -11.046 82.896  156.025 1.00 51.10  ? 362 LEU C CA    1 
ATOM   10498 C C     . LEU C  1 362 ? -10.780 83.941  154.959 1.00 56.46  ? 362 LEU C C     1 
ATOM   10499 O O     . LEU C  1 362 ? -11.137 83.757  153.795 1.00 56.69  ? 362 LEU C O     1 
ATOM   10500 C CB    . LEU C  1 362 ? -9.985  81.795  156.015 1.00 50.93  ? 362 LEU C CB    1 
ATOM   10501 C CG    . LEU C  1 362 ? -10.117 80.818  157.187 1.00 49.81  ? 362 LEU C CG    1 
ATOM   10502 C CD1   . LEU C  1 362 ? -10.733 79.504  156.729 1.00 52.57  ? 362 LEU C CD1   1 
ATOM   10503 C CD2   . LEU C  1 362 ? -8.780  80.585  157.879 1.00 47.73  ? 362 LEU C CD2   1 
ATOM   10504 N N     . THR C  1 363 ? -10.174 85.050  155.362 1.00 55.47  ? 363 THR C N     1 
ATOM   10505 C CA    . THR C  1 363 ? -10.034 86.190  154.471 1.00 55.10  ? 363 THR C CA    1 
ATOM   10506 C C     . THR C  1 363 ? -8.611  86.359  153.960 1.00 57.25  ? 363 THR C C     1 
ATOM   10507 O O     . THR C  1 363 ? -7.642  86.039  154.648 1.00 57.15  ? 363 THR C O     1 
ATOM   10508 C CB    . THR C  1 363 ? -10.475 87.493  155.164 1.00 53.96  ? 363 THR C CB    1 
ATOM   10509 O OG1   . THR C  1 363 ? -9.615  87.761  156.278 1.00 50.16  ? 363 THR C OG1   1 
ATOM   10510 C CG2   . THR C  1 363 ? -11.910 87.374  155.654 1.00 50.04  ? 363 THR C CG2   1 
ATOM   10511 N N     . LYS C  1 364 ? -8.503  86.860  152.736 1.00 60.98  ? 364 LYS C N     1 
ATOM   10512 C CA    . LYS C  1 364 ? -7.216  87.157  152.131 1.00 65.44  ? 364 LYS C CA    1 
ATOM   10513 C C     . LYS C  1 364 ? -7.007  88.662  152.094 1.00 67.11  ? 364 LYS C C     1 
ATOM   10514 O O     . LYS C  1 364 ? -5.905  89.162  152.326 1.00 65.84  ? 364 LYS C O     1 
ATOM   10515 C CB    . LYS C  1 364 ? -7.139  86.579  150.720 1.00 67.08  ? 364 LYS C CB    1 
ATOM   10516 C CG    . LYS C  1 364 ? -5.775  86.700  150.073 1.00 73.61  ? 364 LYS C CG    1 
ATOM   10517 C CD    . LYS C  1 364 ? -5.882  86.582  148.564 1.00 78.39  ? 364 LYS C CD    1 
ATOM   10518 C CE    . LYS C  1 364 ? -4.618  85.991  147.969 1.00 86.82  ? 364 LYS C CE    1 
ATOM   10519 N NZ    . LYS C  1 364 ? -4.377  86.496  146.590 1.00 89.20  ? 364 LYS C NZ    1 
ATOM   10520 N N     . GLU C  1 365 ? -8.088  89.376  151.801 1.00 66.57  ? 365 GLU C N     1 
ATOM   10521 C CA    . GLU C  1 365 ? -8.058  90.825  151.683 1.00 67.85  ? 365 GLU C CA    1 
ATOM   10522 C C     . GLU C  1 365 ? -8.800  91.475  152.844 1.00 65.51  ? 365 GLU C C     1 
ATOM   10523 O O     . GLU C  1 365 ? -9.632  90.831  153.486 1.00 63.60  ? 365 GLU C O     1 
ATOM   10524 C CB    . GLU C  1 365 ? -8.672  91.257  150.346 1.00 65.03  ? 365 GLU C CB    1 
ATOM   10525 C CG    . GLU C  1 365 ? -7.964  90.692  149.124 1.00 65.38  ? 365 GLU C CG    1 
ATOM   10526 C CD    . GLU C  1 365 ? -6.529  91.175  148.993 1.00 78.02  ? 365 GLU C CD    1 
ATOM   10527 O OE1   . GLU C  1 365 ? -6.159  92.166  149.660 1.00 81.86  ? 365 GLU C OE1   1 
ATOM   10528 O OE2   . GLU C  1 365 ? -5.766  90.562  148.217 1.00 82.23  ? 365 GLU C OE2   1 
ATOM   10529 N N     . PRO C  1 366 ? -8.495  92.753  153.129 1.00 63.89  ? 366 PRO C N     1 
ATOM   10530 C CA    . PRO C  1 366 ? -9.252  93.453  154.170 1.00 60.59  ? 366 PRO C CA    1 
ATOM   10531 C C     . PRO C  1 366 ? -10.722 93.524  153.786 1.00 59.72  ? 366 PRO C C     1 
ATOM   10532 O O     . PRO C  1 366 ? -11.029 93.534  152.594 1.00 60.06  ? 366 PRO C O     1 
ATOM   10533 C CB    . PRO C  1 366 ? -8.620  94.852  154.201 1.00 60.36  ? 366 PRO C CB    1 
ATOM   10534 C CG    . PRO C  1 366 ? -7.296  94.703  153.527 1.00 64.66  ? 366 PRO C CG    1 
ATOM   10535 C CD    . PRO C  1 366 ? -7.457  93.607  152.525 1.00 65.72  ? 366 PRO C CD    1 
ATOM   10536 N N     . LEU C  1 367 ? -11.616 93.547  154.766 1.00 57.62  ? 367 LEU C N     1 
ATOM   10537 C CA    . LEU C  1 367 ? -13.035 93.661  154.465 1.00 62.91  ? 367 LEU C CA    1 
ATOM   10538 C C     . LEU C  1 367 ? -13.457 95.123  154.443 1.00 66.79  ? 367 LEU C C     1 
ATOM   10539 O O     . LEU C  1 367 ? -13.220 95.858  155.404 1.00 64.54  ? 367 LEU C O     1 
ATOM   10540 C CB    . LEU C  1 367 ? -13.877 92.887  155.480 1.00 66.18  ? 367 LEU C CB    1 
ATOM   10541 C CG    . LEU C  1 367 ? -13.631 91.384  155.635 1.00 62.03  ? 367 LEU C CG    1 
ATOM   10542 C CD1   . LEU C  1 367 ? -14.550 90.817  156.705 1.00 56.21  ? 367 LEU C CD1   1 
ATOM   10543 C CD2   . LEU C  1 367 ? -13.827 90.655  154.316 1.00 64.12  ? 367 LEU C CD2   1 
ATOM   10544 N N     . PRO C  1 368 ? -14.083 95.550  153.338 1.00 67.48  ? 368 PRO C N     1 
ATOM   10545 C CA    . PRO C  1 368 ? -14.590 96.919  153.219 1.00 67.14  ? 368 PRO C CA    1 
ATOM   10546 C C     . PRO C  1 368 ? -15.686 97.185  154.244 1.00 69.56  ? 368 PRO C C     1 
ATOM   10547 O O     . PRO C  1 368 ? -16.290 96.239  154.752 1.00 66.03  ? 368 PRO C O     1 
ATOM   10548 C CB    . PRO C  1 368 ? -15.135 96.971  151.788 1.00 66.63  ? 368 PRO C CB    1 
ATOM   10549 C CG    . PRO C  1 368 ? -15.451 95.554  151.455 1.00 70.01  ? 368 PRO C CG    1 
ATOM   10550 C CD    . PRO C  1 368 ? -14.414 94.731  152.160 1.00 65.46  ? 368 PRO C CD    1 
ATOM   10551 N N     . SER C  1 369 ? -15.926 98.459  154.540 1.00 68.89  ? 369 SER C N     1 
ATOM   10552 C CA    . SER C  1 369 ? -16.876 98.857  155.573 1.00 69.83  ? 369 SER C CA    1 
ATOM   10553 C C     . SER C  1 369 ? -18.264 98.260  155.354 1.00 64.46  ? 369 SER C C     1 
ATOM   10554 O O     . SER C  1 369 ? -18.949 97.894  156.308 1.00 66.27  ? 369 SER C O     1 
ATOM   10555 C CB    . SER C  1 369 ? -16.970 100.381 155.641 1.00 67.91  ? 369 SER C CB    1 
ATOM   10556 O OG    . SER C  1 369 ? -15.724 100.948 156.010 1.00 67.11  ? 369 SER C OG    1 
ATOM   10557 N N     . LYS C  1 370 ? -18.668 98.145  154.094 1.00 63.77  ? 370 LYS C N     1 
ATOM   10558 C CA    . LYS C  1 370 ? -20.003 97.658  153.772 1.00 68.52  ? 370 LYS C CA    1 
ATOM   10559 C C     . LYS C  1 370 ? -20.184 96.172  154.089 1.00 72.87  ? 370 LYS C C     1 
ATOM   10560 O O     . LYS C  1 370 ? -21.305 95.717  154.313 1.00 72.06  ? 370 LYS C O     1 
ATOM   10561 C CB    . LYS C  1 370 ? -20.320 97.920  152.300 1.00 65.39  ? 370 LYS C CB    1 
ATOM   10562 C CG    . LYS C  1 370 ? -19.219 97.506  151.345 1.00 70.72  ? 370 LYS C CG    1 
ATOM   10563 C CD    . LYS C  1 370 ? -19.715 97.501  149.912 1.00 72.27  ? 370 LYS C CD    1 
ATOM   10564 C CE    . LYS C  1 370 ? -18.599 97.147  148.946 1.00 74.05  ? 370 LYS C CE    1 
ATOM   10565 N NZ    . LYS C  1 370 ? -19.126 96.862  147.585 1.00 75.55  ? 370 LYS C NZ    1 
ATOM   10566 N N     . ALA C  1 371 ? -19.085 95.421  154.108 1.00 67.94  ? 371 ALA C N     1 
ATOM   10567 C CA    . ALA C  1 371 ? -19.135 93.989  154.405 1.00 67.78  ? 371 ALA C CA    1 
ATOM   10568 C C     . ALA C  1 371 ? -19.566 93.744  155.851 1.00 65.02  ? 371 ALA C C     1 
ATOM   10569 O O     . ALA C  1 371 ? -20.491 92.972  156.108 1.00 69.45  ? 371 ALA C O     1 
ATOM   10570 C CB    . ALA C  1 371 ? -17.786 93.337  154.129 1.00 66.55  ? 371 ALA C CB    1 
ATOM   10571 N N     . PHE C  1 372 ? -18.890 94.401  156.789 1.00 62.41  ? 372 PHE C N     1 
ATOM   10572 C CA    . PHE C  1 372 ? -19.296 94.374  158.188 1.00 63.30  ? 372 PHE C CA    1 
ATOM   10573 C C     . PHE C  1 372 ? -20.708 94.932  158.332 1.00 66.92  ? 372 PHE C C     1 
ATOM   10574 O O     . PHE C  1 372 ? -21.553 94.340  159.002 1.00 64.46  ? 372 PHE C O     1 
ATOM   10575 C CB    . PHE C  1 372 ? -18.319 95.179  159.049 1.00 66.01  ? 372 PHE C CB    1 
ATOM   10576 C CG    . PHE C  1 372 ? -16.948 94.579  159.138 1.00 65.07  ? 372 PHE C CG    1 
ATOM   10577 C CD1   . PHE C  1 372 ? -16.653 93.657  160.127 1.00 65.15  ? 372 PHE C CD1   1 
ATOM   10578 C CD2   . PHE C  1 372 ? -15.954 94.940  158.241 1.00 66.21  ? 372 PHE C CD2   1 
ATOM   10579 C CE1   . PHE C  1 372 ? -15.389 93.103  160.228 1.00 63.94  ? 372 PHE C CE1   1 
ATOM   10580 C CE2   . PHE C  1 372 ? -14.688 94.390  158.335 1.00 63.15  ? 372 PHE C CE2   1 
ATOM   10581 C CZ    . PHE C  1 372 ? -14.408 93.468  159.328 1.00 59.81  ? 372 PHE C CZ    1 
ATOM   10582 N N     . TYR C  1 373 ? -20.941 96.072  157.684 1.00 66.55  ? 373 TYR C N     1 
ATOM   10583 C CA    . TYR C  1 373 ? -22.229 96.761  157.692 1.00 68.05  ? 373 TYR C CA    1 
ATOM   10584 C C     . TYR C  1 373 ? -23.391 95.822  157.382 1.00 67.14  ? 373 TYR C C     1 
ATOM   10585 O O     . TYR C  1 373 ? -24.278 95.634  158.214 1.00 62.44  ? 373 TYR C O     1 
ATOM   10586 C CB    . TYR C  1 373 ? -22.210 97.919  156.690 1.00 69.80  ? 373 TYR C CB    1 
ATOM   10587 C CG    . TYR C  1 373 ? -23.433 98.806  156.748 1.00 76.59  ? 373 TYR C CG    1 
ATOM   10588 C CD1   . TYR C  1 373 ? -23.685 99.595  157.863 1.00 78.29  ? 373 TYR C CD1   1 
ATOM   10589 C CD2   . TYR C  1 373 ? -24.329 98.864  155.686 1.00 78.61  ? 373 TYR C CD2   1 
ATOM   10590 C CE1   . TYR C  1 373 ? -24.797 100.409 157.924 1.00 81.57  ? 373 TYR C CE1   1 
ATOM   10591 C CE2   . TYR C  1 373 ? -25.444 99.677  155.737 1.00 80.03  ? 373 TYR C CE2   1 
ATOM   10592 C CZ    . TYR C  1 373 ? -25.674 100.448 156.858 1.00 84.05  ? 373 TYR C CZ    1 
ATOM   10593 O OH    . TYR C  1 373 ? -26.784 101.260 156.916 1.00 93.19  ? 373 TYR C OH    1 
ATOM   10594 N N     . GLY C  1 374 ? -23.380 95.228  156.191 1.00 66.02  ? 374 GLY C N     1 
ATOM   10595 C CA    . GLY C  1 374 ? -24.413 94.281  155.802 1.00 72.98  ? 374 GLY C CA    1 
ATOM   10596 C C     . GLY C  1 374 ? -24.460 93.051  156.695 1.00 71.75  ? 374 GLY C C     1 
ATOM   10597 O O     . GLY C  1 374 ? -25.517 92.441  156.875 1.00 69.75  ? 374 GLY C O     1 
ATOM   10598 N N     . LEU C  1 375 ? -23.308 92.687  157.254 1.00 65.34  ? 375 LEU C N     1 
ATOM   10599 C CA    . LEU C  1 375 ? -23.214 91.567  158.188 1.00 63.44  ? 375 LEU C CA    1 
ATOM   10600 C C     . LEU C  1 375 ? -23.946 91.894  159.490 1.00 63.11  ? 375 LEU C C     1 
ATOM   10601 O O     . LEU C  1 375 ? -24.765 91.108  159.974 1.00 64.21  ? 375 LEU C O     1 
ATOM   10602 C CB    . LEU C  1 375 ? -21.743 91.230  158.463 1.00 64.88  ? 375 LEU C CB    1 
ATOM   10603 C CG    . LEU C  1 375 ? -21.428 90.163  159.515 1.00 57.78  ? 375 LEU C CG    1 
ATOM   10604 C CD1   . LEU C  1 375 ? -21.951 88.805  159.077 1.00 62.48  ? 375 LEU C CD1   1 
ATOM   10605 C CD2   . LEU C  1 375 ? -19.934 90.098  159.797 1.00 63.92  ? 375 LEU C CD2   1 
ATOM   10606 N N     . LEU C  1 376 ? -23.636 93.059  160.051 1.00 61.46  ? 376 LEU C N     1 
ATOM   10607 C CA    . LEU C  1 376 ? -24.337 93.582  161.222 1.00 64.42  ? 376 LEU C CA    1 
ATOM   10608 C C     . LEU C  1 376 ? -25.828 93.786  160.942 1.00 66.91  ? 376 LEU C C     1 
ATOM   10609 O O     . LEU C  1 376 ? -26.661 93.620  161.835 1.00 63.55  ? 376 LEU C O     1 
ATOM   10610 C CB    . LEU C  1 376 ? -23.705 94.903  161.676 1.00 64.62  ? 376 LEU C CB    1 
ATOM   10611 C CG    . LEU C  1 376 ? -22.303 94.866  162.297 1.00 63.72  ? 376 LEU C CG    1 
ATOM   10612 C CD1   . LEU C  1 376 ? -21.459 96.053  161.838 1.00 64.76  ? 376 LEU C CD1   1 
ATOM   10613 C CD2   . LEU C  1 376 ? -22.391 94.822  163.813 1.00 60.94  ? 376 LEU C CD2   1 
ATOM   10614 N N     . GLU C  1 377 ? -26.152 94.153  159.704 1.00 63.00  ? 377 GLU C N     1 
ATOM   10615 C CA    . GLU C  1 377 ? -27.539 94.306  159.266 1.00 74.56  ? 377 GLU C CA    1 
ATOM   10616 C C     . GLU C  1 377 ? -28.335 93.016  159.451 1.00 71.26  ? 377 GLU C C     1 
ATOM   10617 O O     . GLU C  1 377 ? -29.441 93.023  159.989 1.00 65.84  ? 377 GLU C O     1 
ATOM   10618 C CB    . GLU C  1 377 ? -27.582 94.725  157.798 1.00 75.65  ? 377 GLU C CB    1 
ATOM   10619 C CG    . GLU C  1 377 ? -28.375 95.986  157.507 1.00 80.10  ? 377 GLU C CG    1 
ATOM   10620 C CD    . GLU C  1 377 ? -28.393 96.325  156.028 1.00 87.80  ? 377 GLU C CD    1 
ATOM   10621 O OE1   . GLU C  1 377 ? -28.575 95.403  155.205 1.00 95.28  ? 377 GLU C OE1   1 
ATOM   10622 O OE2   . GLU C  1 377 ? -28.214 97.512  155.686 1.00 87.79  ? 377 GLU C OE2   1 
ATOM   10623 N N     . ARG C  1 378 ? -27.753 91.911  158.995 1.00 68.21  ? 378 ARG C N     1 
ATOM   10624 C CA    . ARG C  1 378 ? -28.392 90.603  159.044 1.00 69.55  ? 378 ARG C CA    1 
ATOM   10625 C C     . ARG C  1 378 ? -28.414 90.053  160.465 1.00 68.53  ? 378 ARG C C     1 
ATOM   10626 O O     . ARG C  1 378 ? -29.340 89.336  160.852 1.00 71.73  ? 378 ARG C O     1 
ATOM   10627 C CB    . ARG C  1 378 ? -27.674 89.642  158.094 1.00 67.06  ? 378 ARG C CB    1 
ATOM   10628 C CG    . ARG C  1 378 ? -27.868 90.001  156.634 1.00 66.72  ? 378 ARG C CG    1 
ATOM   10629 C CD    . ARG C  1 378 ? -26.779 89.438  155.743 1.00 71.25  ? 378 ARG C CD    1 
ATOM   10630 N NE    . ARG C  1 378 ? -27.082 89.669  154.332 1.00 72.64  ? 378 ARG C NE    1 
ATOM   10631 C CZ    . ARG C  1 378 ? -26.882 90.823  153.703 1.00 75.17  ? 378 ARG C CZ    1 
ATOM   10632 N NH1   . ARG C  1 378 ? -26.378 91.857  154.360 1.00 75.36  ? 378 ARG C NH1   1 
ATOM   10633 N NH2   . ARG C  1 378 ? -27.190 90.943  152.419 1.00 75.45  ? 378 ARG C NH2   1 
ATOM   10634 N N     . LEU C  1 379 ? -27.389 90.401  161.235 1.00 65.46  ? 379 LEU C N     1 
ATOM   10635 C CA    . LEU C  1 379 ? -27.358 90.103  162.661 1.00 67.00  ? 379 LEU C CA    1 
ATOM   10636 C C     . LEU C  1 379 ? -28.538 90.768  163.363 1.00 68.81  ? 379 LEU C C     1 
ATOM   10637 O O     . LEU C  1 379 ? -29.127 90.203  164.288 1.00 69.01  ? 379 LEU C O     1 
ATOM   10638 C CB    . LEU C  1 379 ? -26.033 90.566  163.280 1.00 67.72  ? 379 LEU C CB    1 
ATOM   10639 C CG    . LEU C  1 379 ? -24.888 89.557  163.186 1.00 69.38  ? 379 LEU C CG    1 
ATOM   10640 C CD1   . LEU C  1 379 ? -23.526 90.193  163.431 1.00 64.80  ? 379 LEU C CD1   1 
ATOM   10641 C CD2   . LEU C  1 379 ? -25.139 88.440  164.174 1.00 67.06  ? 379 LEU C CD2   1 
ATOM   10642 N N     . SER C  1 380 ? -28.877 91.974  162.915 1.00 72.83  ? 380 SER C N     1 
ATOM   10643 C CA    . SER C  1 380 ? -30.035 92.689  163.437 1.00 77.70  ? 380 SER C CA    1 
ATOM   10644 C C     . SER C  1 380 ? -31.331 91.991  163.045 1.00 73.70  ? 380 SER C C     1 
ATOM   10645 O O     . SER C  1 380 ? -32.343 92.118  163.730 1.00 75.37  ? 380 SER C O     1 
ATOM   10646 C CB    . SER C  1 380 ? -30.047 94.135  162.938 1.00 77.80  ? 380 SER C CB    1 
ATOM   10647 O OG    . SER C  1 380 ? -29.076 94.918  163.613 1.00 81.25  ? 380 SER C OG    1 
ATOM   10648 N N     . LYS C  1 381 ? -31.292 91.249  161.943 1.00 74.56  ? 381 LYS C N     1 
ATOM   10649 C CA    . LYS C  1 381 ? -32.465 90.524  161.467 1.00 75.63  ? 381 LYS C CA    1 
ATOM   10650 C C     . LYS C  1 381 ? -32.663 89.195  162.196 1.00 74.77  ? 381 LYS C C     1 
ATOM   10651 O O     . LYS C  1 381 ? -33.624 88.476  161.925 1.00 77.19  ? 381 LYS C O     1 
ATOM   10652 C CB    . LYS C  1 381 ? -32.362 90.275  159.963 1.00 76.97  ? 381 LYS C CB    1 
ATOM   10653 C CG    . LYS C  1 381 ? -32.406 91.535  159.119 1.00 77.96  ? 381 LYS C CG    1 
ATOM   10654 C CD    . LYS C  1 381 ? -32.534 91.190  157.645 1.00 78.70  ? 381 LYS C CD    1 
ATOM   10655 C CE    . LYS C  1 381 ? -31.420 90.251  157.208 1.00 83.80  ? 381 LYS C CE    1 
ATOM   10656 N NZ    . LYS C  1 381 ? -31.501 89.873  155.769 1.00 84.33  ? 381 LYS C NZ    1 
ATOM   10657 N N     . GLU C  1 382 ? -31.760 88.872  163.118 1.00 73.56  ? 382 GLU C N     1 
ATOM   10658 C CA    . GLU C  1 382 ? -31.817 87.587  163.812 1.00 70.23  ? 382 GLU C CA    1 
ATOM   10659 C C     . GLU C  1 382 ? -31.069 87.593  165.147 1.00 70.67  ? 382 GLU C C     1 
ATOM   10660 O O     . GLU C  1 382 ? -29.851 87.412  165.183 1.00 70.62  ? 382 GLU C O     1 
ATOM   10661 C CB    . GLU C  1 382 ? -31.261 86.482  162.910 1.00 70.90  ? 382 GLU C CB    1 
ATOM   10662 C CG    . GLU C  1 382 ? -31.333 85.094  163.519 1.00 69.89  ? 382 GLU C CG    1 
ATOM   10663 C CD    . GLU C  1 382 ? -32.729 84.740  163.989 1.00 68.78  ? 382 GLU C CD    1 
ATOM   10664 O OE1   . GLU C  1 382 ? -33.604 84.489  163.134 1.00 67.45  ? 382 GLU C OE1   1 
ATOM   10665 O OE2   . GLU C  1 382 ? -32.951 84.719  165.218 1.00 66.82  ? 382 GLU C OE2   1 
ATOM   10666 N N     . PRO C  1 383 ? -31.810 87.784  166.252 1.00 70.78  ? 383 PRO C N     1 
ATOM   10667 C CA    . PRO C  1 383 ? -31.273 87.848  167.617 1.00 64.54  ? 383 PRO C CA    1 
ATOM   10668 C C     . PRO C  1 383 ? -30.575 86.562  168.059 1.00 67.80  ? 383 PRO C C     1 
ATOM   10669 O O     . PRO C  1 383 ? -29.808 86.586  169.021 1.00 63.55  ? 383 PRO C O     1 
ATOM   10670 C CB    . PRO C  1 383 ? -32.520 88.094  168.472 1.00 65.14  ? 383 PRO C CB    1 
ATOM   10671 C CG    . PRO C  1 383 ? -33.497 88.722  167.539 1.00 74.44  ? 383 PRO C CG    1 
ATOM   10672 C CD    . PRO C  1 383 ? -33.260 88.033  166.231 1.00 71.04  ? 383 PRO C CD    1 
ATOM   10673 N N     . ASN C  1 384 ? -30.840 85.457  167.369 1.00 67.89  ? 384 ASN C N     1 
ATOM   10674 C CA    . ASN C  1 384 ? -30.257 84.171  167.737 1.00 69.44  ? 384 ASN C CA    1 
ATOM   10675 C C     . ASN C  1 384 ? -28.935 83.892  167.040 1.00 67.59  ? 384 ASN C C     1 
ATOM   10676 O O     . ASN C  1 384 ? -28.256 82.912  167.347 1.00 63.95  ? 384 ASN C O     1 
ATOM   10677 C CB    . ASN C  1 384 ? -31.245 83.047  167.440 1.00 69.64  ? 384 ASN C CB    1 
ATOM   10678 C CG    . ASN C  1 384 ? -32.411 83.045  168.395 1.00 74.85  ? 384 ASN C CG    1 
ATOM   10679 O OD1   . ASN C  1 384 ? -32.406 82.320  169.390 1.00 70.49  ? 384 ASN C OD1   1 
ATOM   10680 N ND2   . ASN C  1 384 ? -33.412 83.867  168.111 1.00 73.59  ? 384 ASN C ND2   1 
ATOM   10681 N N     . GLY C  1 385 ? -28.582 84.751  166.094 1.00 65.86  ? 385 GLY C N     1 
ATOM   10682 C CA    . GLY C  1 385 ? -27.318 84.628  165.401 1.00 64.44  ? 385 GLY C CA    1 
ATOM   10683 C C     . GLY C  1 385 ? -26.270 85.526  166.024 1.00 63.42  ? 385 GLY C C     1 
ATOM   10684 O O     . GLY C  1 385 ? -26.596 86.561  166.607 1.00 65.66  ? 385 GLY C O     1 
ATOM   10685 N N     . PHE C  1 386 ? -25.009 85.120  165.924 1.00 65.59  ? 386 PHE C N     1 
ATOM   10686 C CA    . PHE C  1 386 ? -23.901 85.974  166.334 1.00 64.58  ? 386 PHE C CA    1 
ATOM   10687 C C     . PHE C  1 386 ? -22.645 85.612  165.554 1.00 63.39  ? 386 PHE C C     1 
ATOM   10688 O O     . PHE C  1 386 ? -22.631 84.640  164.798 1.00 62.65  ? 386 PHE C O     1 
ATOM   10689 C CB    . PHE C  1 386 ? -23.648 85.877  167.846 1.00 65.53  ? 386 PHE C CB    1 
ATOM   10690 C CG    . PHE C  1 386 ? -23.352 84.488  168.335 1.00 68.46  ? 386 PHE C CG    1 
ATOM   10691 C CD1   . PHE C  1 386 ? -22.047 84.075  168.548 1.00 68.89  ? 386 PHE C CD1   1 
ATOM   10692 C CD2   . PHE C  1 386 ? -24.381 83.602  168.607 1.00 64.68  ? 386 PHE C CD2   1 
ATOM   10693 C CE1   . PHE C  1 386 ? -21.777 82.802  169.009 1.00 67.22  ? 386 PHE C CE1   1 
ATOM   10694 C CE2   . PHE C  1 386 ? -24.116 82.328  169.066 1.00 67.86  ? 386 PHE C CE2   1 
ATOM   10695 C CZ    . PHE C  1 386 ? -22.812 81.925  169.269 1.00 63.79  ? 386 PHE C CZ    1 
ATOM   10696 N N     . ILE C  1 387 ? -21.596 86.409  165.723 1.00 67.00  ? 387 ILE C N     1 
ATOM   10697 C CA    . ILE C  1 387 ? -20.347 86.164  165.018 1.00 59.26  ? 387 ILE C CA    1 
ATOM   10698 C C     . ILE C  1 387 ? -19.151 86.142  165.959 1.00 62.08  ? 387 ILE C C     1 
ATOM   10699 O O     . ILE C  1 387 ? -19.202 86.674  167.069 1.00 61.01  ? 387 ILE C O     1 
ATOM   10700 C CB    . ILE C  1 387 ? -20.095 87.221  163.921 1.00 61.87  ? 387 ILE C CB    1 
ATOM   10701 C CG1   . ILE C  1 387 ? -20.061 88.629  164.521 1.00 60.61  ? 387 ILE C CG1   1 
ATOM   10702 C CG2   . ILE C  1 387 ? -21.155 87.125  162.837 1.00 62.96  ? 387 ILE C CG2   1 
ATOM   10703 C CD1   . ILE C  1 387 ? -19.803 89.709  163.493 1.00 53.18  ? 387 ILE C CD1   1 
ATOM   10704 N N     . ALA C  1 388 ? -18.079 85.505  165.501 1.00 58.68  ? 388 ALA C N     1 
ATOM   10705 C CA    . ALA C  1 388 ? -16.813 85.485  166.219 1.00 55.71  ? 388 ALA C CA    1 
ATOM   10706 C C     . ALA C  1 388 ? -15.701 85.854  165.249 1.00 53.16  ? 388 ALA C C     1 
ATOM   10707 O O     . ALA C  1 388 ? -15.627 85.314  164.145 1.00 51.98  ? 388 ALA C O     1 
ATOM   10708 C CB    . ALA C  1 388 ? -16.562 84.121  166.841 1.00 53.51  ? 388 ALA C CB    1 
ATOM   10709 N N     . LEU C  1 389 ? -14.847 86.785  165.649 1.00 50.08  ? 389 LEU C N     1 
ATOM   10710 C CA    . LEU C  1 389 ? -13.796 87.253  164.760 1.00 55.38  ? 389 LEU C CA    1 
ATOM   10711 C C     . LEU C  1 389 ? -12.419 87.059  165.387 1.00 52.40  ? 389 LEU C C     1 
ATOM   10712 O O     . LEU C  1 389 ? -12.237 87.261  166.587 1.00 50.41  ? 389 LEU C O     1 
ATOM   10713 C CB    . LEU C  1 389 ? -14.025 88.723  164.409 1.00 54.43  ? 389 LEU C CB    1 
ATOM   10714 C CG    . LEU C  1 389 ? -15.443 89.156  164.020 1.00 56.45  ? 389 LEU C CG    1 
ATOM   10715 C CD1   . LEU C  1 389 ? -15.569 90.660  164.133 1.00 58.59  ? 389 LEU C CD1   1 
ATOM   10716 C CD2   . LEU C  1 389 ? -15.799 88.708  162.616 1.00 56.02  ? 389 LEU C CD2   1 
ATOM   10717 N N     . ASN C  1 390 ? -11.454 86.652  164.571 1.00 49.81  ? 390 ASN C N     1 
ATOM   10718 C CA    . ASN C  1 390 ? -10.089 86.459  165.037 1.00 48.21  ? 390 ASN C CA    1 
ATOM   10719 C C     . ASN C  1 390 ? -9.074  86.861  163.977 1.00 49.00  ? 390 ASN C C     1 
ATOM   10720 O O     . ASN C  1 390 ? -9.237  86.553  162.798 1.00 48.21  ? 390 ASN C O     1 
ATOM   10721 C CB    . ASN C  1 390 ? -9.862  85.004  165.450 1.00 46.35  ? 390 ASN C CB    1 
ATOM   10722 C CG    . ASN C  1 390 ? -10.358 84.710  166.855 1.00 48.51  ? 390 ASN C CG    1 
ATOM   10723 O OD1   . ASN C  1 390 ? -9.653  84.948  167.836 1.00 51.60  ? 390 ASN C OD1   1 
ATOM   10724 N ND2   . ASN C  1 390 ? -11.572 84.180  166.957 1.00 47.51  ? 390 ASN C ND2   1 
ATOM   10725 N N     . GLY C  1 391 ? -8.027  87.559  164.400 1.00 47.04  ? 391 GLY C N     1 
ATOM   10726 C CA    . GLY C  1 391 ? -6.966  87.936  163.491 1.00 49.11  ? 391 GLY C CA    1 
ATOM   10727 C C     . GLY C  1 391 ? -5.864  86.896  163.486 1.00 45.86  ? 391 GLY C C     1 
ATOM   10728 O O     . GLY C  1 391 ? -5.508  86.355  164.533 1.00 43.81  ? 391 GLY C O     1 
ATOM   10729 N N     . PHE C  1 392 ? -5.331  86.594  162.308 1.00 44.04  ? 392 PHE C N     1 
ATOM   10730 C CA    . PHE C  1 392 ? -4.157  85.738  162.233 1.00 46.52  ? 392 PHE C CA    1 
ATOM   10731 C C     . PHE C  1 392 ? -2.916  86.619  162.292 1.00 49.37  ? 392 PHE C C     1 
ATOM   10732 O O     . PHE C  1 392 ? -2.812  87.490  163.157 1.00 52.13  ? 392 PHE C O     1 
ATOM   10733 C CB    . PHE C  1 392 ? -4.167  84.875  160.967 1.00 45.12  ? 392 PHE C CB    1 
ATOM   10734 C CG    . PHE C  1 392 ? -5.077  83.677  161.056 1.00 46.70  ? 392 PHE C CG    1 
ATOM   10735 C CD1   . PHE C  1 392 ? -6.046  83.597  162.044 1.00 47.19  ? 392 PHE C CD1   1 
ATOM   10736 C CD2   . PHE C  1 392 ? -4.952  82.622  160.166 1.00 46.98  ? 392 PHE C CD2   1 
ATOM   10737 C CE1   . PHE C  1 392 ? -6.884  82.502  162.133 1.00 52.03  ? 392 PHE C CE1   1 
ATOM   10738 C CE2   . PHE C  1 392 ? -5.785  81.519  160.252 1.00 47.78  ? 392 PHE C CE2   1 
ATOM   10739 C CZ    . PHE C  1 392 ? -6.752  81.460  161.239 1.00 42.34  ? 392 PHE C CZ    1 
ATOM   10740 N N     . GLY C  1 393 ? -1.982  86.407  161.373 1.00 51.40  ? 393 GLY C N     1 
ATOM   10741 C CA    . GLY C  1 393 ? -0.724  87.125  161.418 1.00 48.21  ? 393 GLY C CA    1 
ATOM   10742 C C     . GLY C  1 393 ? 0.096   86.633  162.593 1.00 46.19  ? 393 GLY C C     1 
ATOM   10743 O O     . GLY C  1 393 ? -0.181  85.566  163.138 1.00 42.80  ? 393 GLY C O     1 
ATOM   10744 N N     . GLY C  1 394 ? 1.094   87.410  163.000 1.00 43.53  ? 394 GLY C N     1 
ATOM   10745 C CA    . GLY C  1 394 ? 1.976   86.990  164.073 1.00 46.14  ? 394 GLY C CA    1 
ATOM   10746 C C     . GLY C  1 394 ? 2.707   85.712  163.705 1.00 42.71  ? 394 GLY C C     1 
ATOM   10747 O O     . GLY C  1 394 ? 3.265   85.603  162.613 1.00 45.89  ? 394 GLY C O     1 
ATOM   10748 N N     . GLN C  1 395 ? 2.690   84.736  164.608 1.00 41.64  ? 395 GLN C N     1 
ATOM   10749 C CA    . GLN C  1 395 ? 3.371   83.467  164.369 1.00 51.18  ? 395 GLN C CA    1 
ATOM   10750 C C     . GLN C  1 395 ? 2.668   82.653  163.288 1.00 50.89  ? 395 GLN C C     1 
ATOM   10751 O O     . GLN C  1 395 ? 3.282   81.810  162.633 1.00 49.61  ? 395 GLN C O     1 
ATOM   10752 C CB    . GLN C  1 395 ? 3.463   82.655  165.661 1.00 47.67  ? 395 GLN C CB    1 
ATOM   10753 C CG    . GLN C  1 395 ? 4.497   81.543  165.618 1.00 53.71  ? 395 GLN C CG    1 
ATOM   10754 C CD    . GLN C  1 395 ? 5.891   82.067  165.322 1.00 59.28  ? 395 GLN C CD    1 
ATOM   10755 O OE1   . GLN C  1 395 ? 6.297   83.112  165.835 1.00 62.05  ? 395 GLN C OE1   1 
ATOM   10756 N NE2   . GLN C  1 395 ? 6.627   81.347  164.484 1.00 55.72  ? 395 GLN C NE2   1 
ATOM   10757 N N     . MET C  1 396 ? 1.378   82.916  163.101 1.00 44.01  ? 396 MET C N     1 
ATOM   10758 C CA    . MET C  1 396 ? 0.596   82.211  162.093 1.00 46.88  ? 396 MET C CA    1 
ATOM   10759 C C     . MET C  1 396 ? 1.061   82.560  160.682 1.00 49.87  ? 396 MET C C     1 
ATOM   10760 O O     . MET C  1 396 ? 0.785   81.827  159.740 1.00 52.60  ? 396 MET C O     1 
ATOM   10761 C CB    . MET C  1 396 ? -0.894  82.523  162.251 1.00 42.44  ? 396 MET C CB    1 
ATOM   10762 C CG    . MET C  1 396 ? -1.531  81.907  163.489 1.00 45.54  ? 396 MET C CG    1 
ATOM   10763 S SD    . MET C  1 396 ? -1.591  80.103  163.453 1.00 44.29  ? 396 MET C SD    1 
ATOM   10764 C CE    . MET C  1 396 ? -2.772  79.825  162.136 1.00 40.81  ? 396 MET C CE    1 
ATOM   10765 N N     . SER C  1 397 ? 1.774   83.673  160.538 1.00 46.49  ? 397 SER C N     1 
ATOM   10766 C CA    . SER C  1 397 ? 2.303   84.071  159.236 1.00 47.64  ? 397 SER C CA    1 
ATOM   10767 C C     . SER C  1 397 ? 3.726   83.567  159.013 1.00 48.33  ? 397 SER C C     1 
ATOM   10768 O O     . SER C  1 397 ? 4.227   83.581  157.890 1.00 45.23  ? 397 SER C O     1 
ATOM   10769 C CB    . SER C  1 397 ? 2.268   85.595  159.085 1.00 46.78  ? 397 SER C CB    1 
ATOM   10770 O OG    . SER C  1 397 ? 0.949   86.056  158.858 1.00 57.87  ? 397 SER C OG    1 
ATOM   10771 N N     . LYS C  1 398 ? 4.371   83.123  160.087 1.00 46.31  ? 398 LYS C N     1 
ATOM   10772 C CA    . LYS C  1 398 ? 5.755   82.665  160.019 1.00 51.70  ? 398 LYS C CA    1 
ATOM   10773 C C     . LYS C  1 398 ? 5.839   81.155  159.841 1.00 50.64  ? 398 LYS C C     1 
ATOM   10774 O O     . LYS C  1 398 ? 6.883   80.621  159.463 1.00 52.09  ? 398 LYS C O     1 
ATOM   10775 C CB    . LYS C  1 398 ? 6.517   83.092  161.272 1.00 46.47  ? 398 LYS C CB    1 
ATOM   10776 C CG    . LYS C  1 398 ? 6.659   84.598  161.400 1.00 55.56  ? 398 LYS C CG    1 
ATOM   10777 C CD    . LYS C  1 398 ? 7.367   84.993  162.682 1.00 66.54  ? 398 LYS C CD    1 
ATOM   10778 C CE    . LYS C  1 398 ? 7.484   86.504  162.781 1.00 64.43  ? 398 LYS C CE    1 
ATOM   10779 N NZ    . LYS C  1 398 ? 7.767   86.950  164.171 1.00 67.24  ? 398 LYS C NZ    1 
ATOM   10780 N N     . ILE C  1 399 ? 4.738   80.468  160.119 1.00 45.93  ? 399 ILE C N     1 
ATOM   10781 C CA    . ILE C  1 399 ? 4.673   79.026  159.935 1.00 46.20  ? 399 ILE C CA    1 
ATOM   10782 C C     . ILE C  1 399 ? 4.294   78.709  158.492 1.00 45.61  ? 399 ILE C C     1 
ATOM   10783 O O     . ILE C  1 399 ? 3.326   79.257  157.966 1.00 45.07  ? 399 ILE C O     1 
ATOM   10784 C CB    . ILE C  1 399 ? 3.658   78.388  160.904 1.00 47.28  ? 399 ILE C CB    1 
ATOM   10785 C CG1   . ILE C  1 399 ? 4.052   78.692  162.352 1.00 44.36  ? 399 ILE C CG1   1 
ATOM   10786 C CG2   . ILE C  1 399 ? 3.560   76.884  160.671 1.00 41.66  ? 399 ILE C CG2   1 
ATOM   10787 C CD1   . ILE C  1 399 ? 2.947   78.448  163.353 1.00 40.44  ? 399 ILE C CD1   1 
ATOM   10788 N N     . SER C  1 400 ? 5.074   77.841  157.853 1.00 42.12  ? 400 SER C N     1 
ATOM   10789 C CA    . SER C  1 400 ? 4.829   77.440  156.468 1.00 44.45  ? 400 SER C CA    1 
ATOM   10790 C C     . SER C  1 400 ? 3.433   76.846  156.302 1.00 43.35  ? 400 SER C C     1 
ATOM   10791 O O     . SER C  1 400 ? 2.876   76.286  157.246 1.00 38.12  ? 400 SER C O     1 
ATOM   10792 C CB    . SER C  1 400 ? 5.888   76.436  156.011 1.00 42.88  ? 400 SER C CB    1 
ATOM   10793 O OG    . SER C  1 400 ? 7.190   76.857  156.398 1.00 58.14  ? 400 SER C OG    1 
ATOM   10794 N N     . SER C  1 401 ? 2.866   76.973  155.107 1.00 43.98  ? 401 SER C N     1 
ATOM   10795 C CA    . SER C  1 401 ? 1.520   76.469  154.860 1.00 47.33  ? 401 SER C CA    1 
ATOM   10796 C C     . SER C  1 401 ? 1.494   74.941  154.841 1.00 42.17  ? 401 SER C C     1 
ATOM   10797 O O     . SER C  1 401 ? 0.435   74.333  154.992 1.00 39.54  ? 401 SER C O     1 
ATOM   10798 C CB    . SER C  1 401 ? 0.968   77.020  153.542 1.00 45.95  ? 401 SER C CB    1 
ATOM   10799 O OG    . SER C  1 401 ? 1.684   76.513  152.432 1.00 53.51  ? 401 SER C OG    1 
ATOM   10800 N N     . ASP C  1 402 ? 2.659   74.322  154.661 1.00 44.66  ? 402 ASP C N     1 
ATOM   10801 C CA    . ASP C  1 402 ? 2.731   72.865  154.633 1.00 44.23  ? 402 ASP C CA    1 
ATOM   10802 C C     . ASP C  1 402 ? 3.469   72.277  155.836 1.00 44.78  ? 402 ASP C C     1 
ATOM   10803 O O     . ASP C  1 402 ? 3.801   71.091  155.840 1.00 45.46  ? 402 ASP C O     1 
ATOM   10804 C CB    . ASP C  1 402 ? 3.387   72.378  153.330 1.00 48.56  ? 402 ASP C CB    1 
ATOM   10805 C CG    . ASP C  1 402 ? 4.850   72.794  153.196 1.00 51.89  ? 402 ASP C CG    1 
ATOM   10806 O OD1   . ASP C  1 402 ? 5.441   73.331  154.156 1.00 50.63  ? 402 ASP C OD1   1 
ATOM   10807 O OD2   . ASP C  1 402 ? 5.423   72.564  152.109 1.00 57.25  ? 402 ASP C OD2   1 
ATOM   10808 N N     . PHE C  1 403 ? 3.735   73.099  156.847 1.00 45.25  ? 403 PHE C N     1 
ATOM   10809 C CA    . PHE C  1 403 ? 4.359   72.596  158.067 1.00 41.08  ? 403 PHE C CA    1 
ATOM   10810 C C     . PHE C  1 403 ? 3.475   71.522  158.688 1.00 40.84  ? 403 PHE C C     1 
ATOM   10811 O O     . PHE C  1 403 ? 3.962   70.482  159.135 1.00 37.18  ? 403 PHE C O     1 
ATOM   10812 C CB    . PHE C  1 403 ? 4.610   73.721  159.071 1.00 36.80  ? 403 PHE C CB    1 
ATOM   10813 C CG    . PHE C  1 403 ? 5.170   73.243  160.382 1.00 37.73  ? 403 PHE C CG    1 
ATOM   10814 C CD1   . PHE C  1 403 ? 6.460   72.740  160.459 1.00 39.41  ? 403 PHE C CD1   1 
ATOM   10815 C CD2   . PHE C  1 403 ? 4.405   73.289  161.537 1.00 33.25  ? 403 PHE C CD2   1 
ATOM   10816 C CE1   . PHE C  1 403 ? 6.976   72.294  161.665 1.00 34.28  ? 403 PHE C CE1   1 
ATOM   10817 C CE2   . PHE C  1 403 ? 4.917   72.845  162.745 1.00 37.16  ? 403 PHE C CE2   1 
ATOM   10818 C CZ    . PHE C  1 403 ? 6.203   72.346  162.807 1.00 40.18  ? 403 PHE C CZ    1 
ATOM   10819 N N     . THR C  1 404 ? 2.173   71.796  158.711 1.00 40.34  ? 404 THR C N     1 
ATOM   10820 C CA    . THR C  1 404 ? 1.151   70.838  159.117 1.00 37.80  ? 404 THR C CA    1 
ATOM   10821 C C     . THR C  1 404 ? 0.011   70.955  158.094 1.00 37.75  ? 404 THR C C     1 
ATOM   10822 O O     . THR C  1 404 ? 0.049   71.850  157.250 1.00 41.10  ? 404 THR C O     1 
ATOM   10823 C CB    . THR C  1 404 ? 0.659   71.106  160.560 1.00 40.59  ? 404 THR C CB    1 
ATOM   10824 O OG1   . THR C  1 404 ? 0.265   72.478  160.693 1.00 39.32  ? 404 THR C OG1   1 
ATOM   10825 C CG2   . THR C  1 404 ? 1.756   70.797  161.564 1.00 36.83  ? 404 THR C CG2   1 
ATOM   10826 N N     . PRO C  1 405 ? -0.983  70.044  158.129 1.00 34.48  ? 405 PRO C N     1 
ATOM   10827 C CA    . PRO C  1 405 ? -2.071  70.124  157.143 1.00 36.03  ? 405 PRO C CA    1 
ATOM   10828 C C     . PRO C  1 405 ? -2.862  71.438  157.122 1.00 39.25  ? 405 PRO C C     1 
ATOM   10829 O O     . PRO C  1 405 ? -3.412  71.766  156.073 1.00 43.17  ? 405 PRO C O     1 
ATOM   10830 C CB    . PRO C  1 405 ? -2.986  68.967  157.552 1.00 41.39  ? 405 PRO C CB    1 
ATOM   10831 C CG    . PRO C  1 405 ? -2.060  67.965  158.109 1.00 39.50  ? 405 PRO C CG    1 
ATOM   10832 C CD    . PRO C  1 405 ? -1.013  68.758  158.850 1.00 35.99  ? 405 PRO C CD    1 
ATOM   10833 N N     . PHE C  1 406 ? -2.930  72.162  158.237 1.00 36.34  ? 406 PHE C N     1 
ATOM   10834 C CA    . PHE C  1 406 ? -3.618  73.456  158.255 1.00 38.94  ? 406 PHE C CA    1 
ATOM   10835 C C     . PHE C  1 406 ? -2.859  74.450  157.381 1.00 40.89  ? 406 PHE C C     1 
ATOM   10836 O O     . PHE C  1 406 ? -1.735  74.834  157.701 1.00 38.48  ? 406 PHE C O     1 
ATOM   10837 C CB    . PHE C  1 406 ? -3.752  73.985  159.684 1.00 38.07  ? 406 PHE C CB    1 
ATOM   10838 C CG    . PHE C  1 406 ? -4.568  75.246  159.798 1.00 41.27  ? 406 PHE C CG    1 
ATOM   10839 C CD1   . PHE C  1 406 ? -5.936  75.186  160.018 1.00 38.75  ? 406 PHE C CD1   1 
ATOM   10840 C CD2   . PHE C  1 406 ? -3.965  76.491  159.704 1.00 36.79  ? 406 PHE C CD2   1 
ATOM   10841 C CE1   . PHE C  1 406 ? -6.685  76.345  160.130 1.00 45.53  ? 406 PHE C CE1   1 
ATOM   10842 C CE2   . PHE C  1 406 ? -4.712  77.650  159.816 1.00 41.92  ? 406 PHE C CE2   1 
ATOM   10843 C CZ    . PHE C  1 406 ? -6.073  77.577  160.029 1.00 43.32  ? 406 PHE C CZ    1 
ATOM   10844 N N     . PRO C  1 407 ? -3.480  74.870  156.269 1.00 36.07  ? 407 PRO C N     1 
ATOM   10845 C CA    . PRO C  1 407 ? -2.800  75.611  155.205 1.00 42.65  ? 407 PRO C CA    1 
ATOM   10846 C C     . PRO C  1 407 ? -2.903  77.133  155.305 1.00 42.41  ? 407 PRO C C     1 
ATOM   10847 O O     . PRO C  1 407 ? -2.190  77.832  154.589 1.00 39.93  ? 407 PRO C O     1 
ATOM   10848 C CB    . PRO C  1 407 ? -3.526  75.122  153.956 1.00 40.88  ? 407 PRO C CB    1 
ATOM   10849 C CG    . PRO C  1 407 ? -4.947  74.973  154.438 1.00 43.25  ? 407 PRO C CG    1 
ATOM   10850 C CD    . PRO C  1 407 ? -4.873  74.561  155.901 1.00 42.22  ? 407 PRO C CD    1 
ATOM   10851 N N     . HIS C  1 408 ? -3.775  77.639  156.166 1.00 40.66  ? 408 HIS C N     1 
ATOM   10852 C CA    . HIS C  1 408 ? -4.072  79.066  156.174 1.00 41.35  ? 408 HIS C CA    1 
ATOM   10853 C C     . HIS C  1 408 ? -3.124  79.827  157.082 1.00 39.56  ? 408 HIS C C     1 
ATOM   10854 O O     . HIS C  1 408 ? -3.437  80.108  158.239 1.00 40.16  ? 408 HIS C O     1 
ATOM   10855 C CB    . HIS C  1 408 ? -5.519  79.288  156.591 1.00 43.13  ? 408 HIS C CB    1 
ATOM   10856 C CG    . HIS C  1 408 ? -6.477  78.403  155.862 1.00 41.78  ? 408 HIS C CG    1 
ATOM   10857 N ND1   . HIS C  1 408 ? -7.337  77.543  156.508 1.00 48.87  ? 408 HIS C ND1   1 
ATOM   10858 C CD2   . HIS C  1 408 ? -6.684  78.220  154.537 1.00 43.06  ? 408 HIS C CD2   1 
ATOM   10859 C CE1   . HIS C  1 408 ? -8.042  76.877  155.612 1.00 48.15  ? 408 HIS C CE1   1 
ATOM   10860 N NE2   . HIS C  1 408 ? -7.668  77.271  154.408 1.00 49.60  ? 408 HIS C NE2   1 
ATOM   10861 N N     . ARG C  1 409 ? -1.961  80.161  156.536 1.00 39.33  ? 409 ARG C N     1 
ATOM   10862 C CA    . ARG C  1 409 ? -0.921  80.840  157.288 1.00 45.59  ? 409 ARG C CA    1 
ATOM   10863 C C     . ARG C  1 409 ? -0.701  82.252  156.737 1.00 45.32  ? 409 ARG C C     1 
ATOM   10864 O O     . ARG C  1 409 ? -1.592  83.096  156.824 1.00 49.64  ? 409 ARG C O     1 
ATOM   10865 C CB    . ARG C  1 409 ? 0.371   80.024  157.247 1.00 43.07  ? 409 ARG C CB    1 
ATOM   10866 C CG    . ARG C  1 409 ? 0.199   78.545  157.609 1.00 43.42  ? 409 ARG C CG    1 
ATOM   10867 C CD    . ARG C  1 409 ? -0.120  78.339  159.089 1.00 42.10  ? 409 ARG C CD    1 
ATOM   10868 N NE    . ARG C  1 409 ? -0.087  76.926  159.462 1.00 42.24  ? 409 ARG C NE    1 
ATOM   10869 C CZ    . ARG C  1 409 ? -0.138  76.474  160.712 1.00 39.93  ? 409 ARG C CZ    1 
ATOM   10870 N NH1   . ARG C  1 409 ? -0.227  77.319  161.729 1.00 39.74  ? 409 ARG C NH1   1 
ATOM   10871 N NH2   . ARG C  1 409 ? -0.094  75.171  160.946 1.00 39.67  ? 409 ARG C NH2   1 
ATOM   10872 N N     . SER C  1 410 ? 0.474   82.505  156.166 1.00 48.51  ? 410 SER C N     1 
ATOM   10873 C CA    . SER C  1 410 ? 0.768   83.815  155.586 1.00 48.43  ? 410 SER C CA    1 
ATOM   10874 C C     . SER C  1 410 ? -0.255  84.184  154.515 1.00 54.40  ? 410 SER C C     1 
ATOM   10875 O O     . SER C  1 410 ? -0.672  83.338  153.725 1.00 53.15  ? 410 SER C O     1 
ATOM   10876 C CB    . SER C  1 410 ? 2.178   83.842  154.994 1.00 49.10  ? 410 SER C CB    1 
ATOM   10877 O OG    . SER C  1 410 ? 2.470   85.105  154.423 1.00 56.78  ? 410 SER C OG    1 
ATOM   10878 N N     . GLY C  1 411 ? -0.665  85.448  154.500 1.00 54.41  ? 411 GLY C N     1 
ATOM   10879 C CA    . GLY C  1 411 ? -1.661  85.908  153.550 1.00 47.81  ? 411 GLY C CA    1 
ATOM   10880 C C     . GLY C  1 411 ? -3.078  85.779  154.076 1.00 55.79  ? 411 GLY C C     1 
ATOM   10881 O O     . GLY C  1 411 ? -4.021  86.277  153.464 1.00 64.33  ? 411 GLY C O     1 
ATOM   10882 N N     . THR C  1 412 ? -3.235  85.100  155.208 1.00 54.67  ? 412 THR C N     1 
ATOM   10883 C CA    . THR C  1 412 ? -4.547  84.964  155.834 1.00 52.80  ? 412 THR C CA    1 
ATOM   10884 C C     . THR C  1 412 ? -4.707  86.009  156.935 1.00 51.29  ? 412 THR C C     1 
ATOM   10885 O O     . THR C  1 412 ? -3.885  86.088  157.844 1.00 49.18  ? 412 THR C O     1 
ATOM   10886 C CB    . THR C  1 412 ? -4.760  83.553  156.420 1.00 48.06  ? 412 THR C CB    1 
ATOM   10887 O OG1   . THR C  1 412 ? -4.439  82.568  155.428 1.00 47.82  ? 412 THR C OG1   1 
ATOM   10888 C CG2   . THR C  1 412 ? -6.207  83.370  156.867 1.00 47.75  ? 412 THR C CG2   1 
ATOM   10889 N N     . ARG C  1 413 ? -5.763  86.813  156.846 1.00 55.68  ? 413 ARG C N     1 
ATOM   10890 C CA    . ARG C  1 413 ? -5.951  87.923  157.774 1.00 51.56  ? 413 ARG C CA    1 
ATOM   10891 C C     . ARG C  1 413 ? -6.895  87.584  158.918 1.00 46.55  ? 413 ARG C C     1 
ATOM   10892 O O     . ARG C  1 413 ? -6.573  87.796  160.087 1.00 48.69  ? 413 ARG C O     1 
ATOM   10893 C CB    . ARG C  1 413 ? -6.483  89.155  157.036 1.00 56.63  ? 413 ARG C CB    1 
ATOM   10894 C CG    . ARG C  1 413 ? -5.602  89.644  155.900 1.00 58.85  ? 413 ARG C CG    1 
ATOM   10895 C CD    . ARG C  1 413 ? -6.185  90.898  155.265 1.00 65.36  ? 413 ARG C CD    1 
ATOM   10896 N NE    . ARG C  1 413 ? -5.391  91.370  154.133 1.00 70.75  ? 413 ARG C NE    1 
ATOM   10897 C CZ    . ARG C  1 413 ? -4.453  92.308  154.214 1.00 68.64  ? 413 ARG C CZ    1 
ATOM   10898 N NH1   . ARG C  1 413 ? -3.783  92.674  153.129 1.00 77.03  ? 413 ARG C NH1   1 
ATOM   10899 N NH2   . ARG C  1 413 ? -4.182  92.882  155.379 1.00 63.47  ? 413 ARG C NH2   1 
ATOM   10900 N N     . LEU C  1 414 ? -8.071  87.069  158.579 1.00 49.86  ? 414 LEU C N     1 
ATOM   10901 C CA    . LEU C  1 414 ? -9.116  86.877  159.574 1.00 48.19  ? 414 LEU C CA    1 
ATOM   10902 C C     . LEU C  1 414 ? -9.771  85.504  159.496 1.00 48.50  ? 414 LEU C C     1 
ATOM   10903 O O     . LEU C  1 414 ? -9.901  84.923  158.420 1.00 44.53  ? 414 LEU C O     1 
ATOM   10904 C CB    . LEU C  1 414 ? -10.196 87.952  159.419 1.00 47.19  ? 414 LEU C CB    1 
ATOM   10905 C CG    . LEU C  1 414 ? -9.778  89.424  159.415 1.00 55.57  ? 414 LEU C CG    1 
ATOM   10906 C CD1   . LEU C  1 414 ? -10.936 90.299  158.946 1.00 47.90  ? 414 LEU C CD1   1 
ATOM   10907 C CD2   . LEU C  1 414 ? -9.306  89.850  160.796 1.00 47.44  ? 414 LEU C CD2   1 
ATOM   10908 N N     . MET C  1 415 ? -10.186 84.990  160.647 1.00 41.28  ? 415 MET C N     1 
ATOM   10909 C CA    . MET C  1 415 ? -11.115 83.873  160.674 1.00 48.42  ? 415 MET C CA    1 
ATOM   10910 C C     . MET C  1 415 ? -12.462 84.398  161.145 1.00 51.19  ? 415 MET C C     1 
ATOM   10911 O O     . MET C  1 415 ? -12.582 84.889  162.266 1.00 45.47  ? 415 MET C O     1 
ATOM   10912 C CB    . MET C  1 415 ? -10.629 82.744  161.587 1.00 45.50  ? 415 MET C CB    1 
ATOM   10913 C CG    . MET C  1 415 ? -11.524 81.509  161.531 1.00 50.81  ? 415 MET C CG    1 
ATOM   10914 S SD    . MET C  1 415 ? -10.808 80.037  162.282 1.00 49.05  ? 415 MET C SD    1 
ATOM   10915 C CE    . MET C  1 415 ? -10.980 80.416  164.025 1.00 45.55  ? 415 MET C CE    1 
ATOM   10916 N N     . VAL C  1 416 ? -13.473 84.308  160.289 1.00 49.19  ? 416 VAL C N     1 
ATOM   10917 C CA    . VAL C  1 416 ? -14.797 84.807  160.640 1.00 48.84  ? 416 VAL C CA    1 
ATOM   10918 C C     . VAL C  1 416 ? -15.785 83.662  160.812 1.00 47.02  ? 416 VAL C C     1 
ATOM   10919 O O     . VAL C  1 416 ? -16.074 82.943  159.862 1.00 44.49  ? 416 VAL C O     1 
ATOM   10920 C CB    . VAL C  1 416 ? -15.333 85.780  159.578 1.00 44.58  ? 416 VAL C CB    1 
ATOM   10921 C CG1   . VAL C  1 416 ? -16.692 86.323  159.998 1.00 51.06  ? 416 VAL C CG1   1 
ATOM   10922 C CG2   . VAL C  1 416 ? -14.346 86.911  159.349 1.00 44.81  ? 416 VAL C CG2   1 
ATOM   10923 N N     . GLU C  1 417 ? -16.293 83.495  162.029 1.00 47.90  ? 417 GLU C N     1 
ATOM   10924 C CA    . GLU C  1 417 ? -17.265 82.444  162.315 1.00 48.26  ? 417 GLU C CA    1 
ATOM   10925 C C     . GLU C  1 417 ? -18.689 82.999  162.327 1.00 53.37  ? 417 GLU C C     1 
ATOM   10926 O O     . GLU C  1 417 ? -18.958 84.006  162.978 1.00 50.28  ? 417 GLU C O     1 
ATOM   10927 C CB    . GLU C  1 417 ? -16.951 81.779  163.656 1.00 48.65  ? 417 GLU C CB    1 
ATOM   10928 C CG    . GLU C  1 417 ? -15.504 81.340  163.802 1.00 55.35  ? 417 GLU C CG    1 
ATOM   10929 C CD    . GLU C  1 417 ? -15.146 80.959  165.226 1.00 55.46  ? 417 GLU C CD    1 
ATOM   10930 O OE1   . GLU C  1 417 ? -15.908 80.191  165.851 1.00 58.88  ? 417 GLU C OE1   1 
ATOM   10931 O OE2   . GLU C  1 417 ? -14.103 81.432  165.722 1.00 58.09  ? 417 GLU C OE2   1 
ATOM   10932 N N     . TYR C  1 418 ? -19.594 82.349  161.599 1.00 45.66  ? 418 TYR C N     1 
ATOM   10933 C CA    . TYR C  1 418 ? -21.008 82.715  161.637 1.00 49.23  ? 418 TYR C CA    1 
ATOM   10934 C C     . TYR C  1 418 ? -21.804 81.638  162.354 1.00 51.41  ? 418 TYR C C     1 
ATOM   10935 O O     . TYR C  1 418 ? -21.855 80.494  161.907 1.00 50.03  ? 418 TYR C O     1 
ATOM   10936 C CB    . TYR C  1 418 ? -21.575 82.915  160.230 1.00 49.19  ? 418 TYR C CB    1 
ATOM   10937 C CG    . TYR C  1 418 ? -20.628 83.550  159.243 1.00 53.74  ? 418 TYR C CG    1 
ATOM   10938 C CD1   . TYR C  1 418 ? -20.457 84.928  159.197 1.00 54.61  ? 418 TYR C CD1   1 
ATOM   10939 C CD2   . TYR C  1 418 ? -19.916 82.771  158.341 1.00 54.83  ? 418 TYR C CD2   1 
ATOM   10940 C CE1   . TYR C  1 418 ? -19.591 85.512  158.282 1.00 55.95  ? 418 TYR C CE1   1 
ATOM   10941 C CE2   . TYR C  1 418 ? -19.050 83.343  157.427 1.00 54.44  ? 418 TYR C CE2   1 
ATOM   10942 C CZ    . TYR C  1 418 ? -18.889 84.712  157.399 1.00 52.29  ? 418 TYR C CZ    1 
ATOM   10943 O OH    . TYR C  1 418 ? -18.025 85.279  156.485 1.00 49.24  ? 418 TYR C OH    1 
ATOM   10944 N N     . ILE C  1 419 ? -22.438 82.005  163.459 1.00 51.70  ? 419 ILE C N     1 
ATOM   10945 C CA    . ILE C  1 419 ? -23.157 81.031  164.269 1.00 52.46  ? 419 ILE C CA    1 
ATOM   10946 C C     . ILE C  1 419 ? -24.624 81.419  164.448 1.00 61.30  ? 419 ILE C C     1 
ATOM   10947 O O     . ILE C  1 419 ? -24.954 82.599  164.564 1.00 59.97  ? 419 ILE C O     1 
ATOM   10948 C CB    . ILE C  1 419 ? -22.482 80.873  165.646 1.00 51.74  ? 419 ILE C CB    1 
ATOM   10949 C CG1   . ILE C  1 419 ? -20.996 80.543  165.464 1.00 56.06  ? 419 ILE C CG1   1 
ATOM   10950 C CG2   . ILE C  1 419 ? -23.171 79.795  166.468 1.00 57.67  ? 419 ILE C CG2   1 
ATOM   10951 C CD1   . ILE C  1 419 ? -20.141 80.825  166.677 1.00 57.30  ? 419 ILE C CD1   1 
ATOM   10952 N N     . VAL C  1 420 ? -25.505 80.423  164.436 1.00 57.18  ? 420 VAL C N     1 
ATOM   10953 C CA    . VAL C  1 420 ? -26.891 80.628  164.835 1.00 60.23  ? 420 VAL C CA    1 
ATOM   10954 C C     . VAL C  1 420 ? -27.284 79.507  165.803 1.00 59.61  ? 420 VAL C C     1 
ATOM   10955 O O     . VAL C  1 420 ? -27.075 78.326  165.527 1.00 61.09  ? 420 VAL C O     1 
ATOM   10956 C CB    . VAL C  1 420 ? -27.850 80.696  163.611 1.00 64.39  ? 420 VAL C CB    1 
ATOM   10957 C CG1   . VAL C  1 420 ? -27.864 79.388  162.827 1.00 63.29  ? 420 VAL C CG1   1 
ATOM   10958 C CG2   . VAL C  1 420 ? -29.253 81.088  164.051 1.00 69.72  ? 420 VAL C CG2   1 
ATOM   10959 N N     . ALA C  1 421 ? -27.810 79.887  166.962 1.00 60.96  ? 421 ALA C N     1 
ATOM   10960 C CA    . ALA C  1 421 ? -28.111 78.921  168.013 1.00 64.61  ? 421 ALA C CA    1 
ATOM   10961 C C     . ALA C  1 421 ? -29.514 79.125  168.574 1.00 68.66  ? 421 ALA C C     1 
ATOM   10962 O O     . ALA C  1 421 ? -30.035 80.236  168.566 1.00 70.72  ? 421 ALA C O     1 
ATOM   10963 C CB    . ALA C  1 421 ? -27.080 79.014  169.125 1.00 56.90  ? 421 ALA C CB    1 
ATOM   10964 N N     . TRP C  1 422 ? -30.114 78.049  169.072 1.00 67.98  ? 422 TRP C N     1 
ATOM   10965 C CA    . TRP C  1 422 ? -31.481 78.101  169.569 1.00 73.08  ? 422 TRP C CA    1 
ATOM   10966 C C     . TRP C  1 422 ? -31.745 77.003  170.594 1.00 73.63  ? 422 TRP C C     1 
ATOM   10967 O O     . TRP C  1 422 ? -31.186 75.911  170.499 1.00 72.35  ? 422 TRP C O     1 
ATOM   10968 C CB    . TRP C  1 422 ? -32.465 77.978  168.404 1.00 71.39  ? 422 TRP C CB    1 
ATOM   10969 C CG    . TRP C  1 422 ? -32.452 76.621  167.746 1.00 74.19  ? 422 TRP C CG    1 
ATOM   10970 C CD1   . TRP C  1 422 ? -33.166 75.521  168.129 1.00 74.91  ? 422 TRP C CD1   1 
ATOM   10971 C CD2   . TRP C  1 422 ? -31.692 76.223  166.594 1.00 71.79  ? 422 TRP C CD2   1 
ATOM   10972 N NE1   . TRP C  1 422 ? -32.897 74.466  167.291 1.00 73.77  ? 422 TRP C NE1   1 
ATOM   10973 C CE2   . TRP C  1 422 ? -31.997 74.869  166.340 1.00 70.89  ? 422 TRP C CE2   1 
ATOM   10974 C CE3   . TRP C  1 422 ? -30.784 76.878  165.753 1.00 69.15  ? 422 TRP C CE3   1 
ATOM   10975 C CZ2   . TRP C  1 422 ? -31.428 74.159  165.283 1.00 67.99  ? 422 TRP C CZ2   1 
ATOM   10976 C CZ3   . TRP C  1 422 ? -30.219 76.169  164.702 1.00 68.10  ? 422 TRP C CZ3   1 
ATOM   10977 C CH2   . TRP C  1 422 ? -30.544 74.824  164.477 1.00 66.62  ? 422 TRP C CH2   1 
ATOM   10978 N N     . ASN C  1 423 ? -32.595 77.291  171.573 1.00 75.72  ? 423 ASN C N     1 
ATOM   10979 C CA    . ASN C  1 423 ? -33.009 76.269  172.529 1.00 83.85  ? 423 ASN C CA    1 
ATOM   10980 C C     . ASN C  1 423 ? -34.179 75.482  171.954 1.00 80.36  ? 423 ASN C C     1 
ATOM   10981 O O     . ASN C  1 423 ? -34.700 75.838  170.898 1.00 77.00  ? 423 ASN C O     1 
ATOM   10982 C CB    . ASN C  1 423 ? -33.388 76.902  173.873 1.00 85.63  ? 423 ASN C CB    1 
ATOM   10983 C CG    . ASN C  1 423 ? -33.368 75.904  175.020 1.00 90.39  ? 423 ASN C CG    1 
ATOM   10984 O OD1   . ASN C  1 423 ? -33.866 74.784  174.895 1.00 88.56  ? 423 ASN C OD1   1 
ATOM   10985 N ND2   . ASN C  1 423 ? -32.785 76.306  176.141 1.00 88.87  ? 423 ASN C ND2   1 
ATOM   10986 N N     . GLN C  1 424 ? -34.584 74.418  172.641 1.00 83.52  ? 424 GLN C N     1 
ATOM   10987 C CA    . GLN C  1 424 ? -35.704 73.589  172.202 1.00 87.86  ? 424 GLN C CA    1 
ATOM   10988 C C     . GLN C  1 424 ? -36.981 74.400  171.957 1.00 86.53  ? 424 GLN C C     1 
ATOM   10989 O O     . GLN C  1 424 ? -37.670 74.182  170.963 1.00 85.30  ? 424 GLN C O     1 
ATOM   10990 C CB    . GLN C  1 424 ? -35.976 72.487  173.230 1.00 90.19  ? 424 GLN C CB    1 
ATOM   10991 C CG    . GLN C  1 424 ? -36.806 71.326  172.700 1.00 96.36  ? 424 GLN C CG    1 
ATOM   10992 C CD    . GLN C  1 424 ? -38.071 71.087  173.504 1.00 103.71 ? 424 GLN C CD    1 
ATOM   10993 O OE1   . GLN C  1 424 ? -38.930 71.964  173.606 1.00 103.14 ? 424 GLN C OE1   1 
ATOM   10994 N NE2   . GLN C  1 424 ? -38.189 69.897  174.083 1.00 103.37 ? 424 GLN C NE2   1 
ATOM   10995 N N     . SER C  1 425 ? -37.286 75.343  172.849 1.00 84.70  ? 425 SER C N     1 
ATOM   10996 C CA    . SER C  1 425 ? -38.488 76.180  172.725 1.00 85.76  ? 425 SER C CA    1 
ATOM   10997 C C     . SER C  1 425 ? -38.638 76.833  171.349 1.00 82.50  ? 425 SER C C     1 
ATOM   10998 O O     . SER C  1 425 ? -39.738 77.219  170.954 1.00 80.37  ? 425 SER C O     1 
ATOM   10999 C CB    . SER C  1 425 ? -38.487 77.274  173.796 1.00 87.24  ? 425 SER C CB    1 
ATOM   11000 O OG    . SER C  1 425 ? -38.376 76.726  175.096 1.00 94.50  ? 425 SER C OG    1 
ATOM   11001 N N     . GLU C  1 426 ? -37.525 76.949  170.630 1.00 78.91  ? 426 GLU C N     1 
ATOM   11002 C CA    . GLU C  1 426 ? -37.494 77.587  169.320 1.00 78.62  ? 426 GLU C CA    1 
ATOM   11003 C C     . GLU C  1 426 ? -37.394 76.570  168.181 1.00 81.91  ? 426 GLU C C     1 
ATOM   11004 O O     . GLU C  1 426 ? -37.223 76.951  167.022 1.00 81.01  ? 426 GLU C O     1 
ATOM   11005 C CB    . GLU C  1 426 ? -36.317 78.562  169.251 1.00 77.71  ? 426 GLU C CB    1 
ATOM   11006 C CG    . GLU C  1 426 ? -36.109 79.351  170.533 1.00 80.43  ? 426 GLU C CG    1 
ATOM   11007 C CD    . GLU C  1 426 ? -34.906 80.265  170.456 1.00 82.88  ? 426 GLU C CD    1 
ATOM   11008 O OE1   . GLU C  1 426 ? -34.399 80.471  169.336 1.00 80.71  ? 426 GLU C OE1   1 
ATOM   11009 O OE2   . GLU C  1 426 ? -34.472 80.770  171.512 1.00 85.90  ? 426 GLU C OE2   1 
ATOM   11010 N N     . GLN C  1 427 ? -37.501 75.289  168.536 1.00 84.18  ? 427 GLN C N     1 
ATOM   11011 C CA    . GLN C  1 427 ? -37.363 74.147  167.620 1.00 84.80  ? 427 GLN C CA    1 
ATOM   11012 C C     . GLN C  1 427 ? -37.991 74.341  166.244 1.00 85.93  ? 427 GLN C C     1 
ATOM   11013 O O     . GLN C  1 427 ? -37.373 74.049  165.218 1.00 84.00  ? 427 GLN C O     1 
ATOM   11014 C CB    . GLN C  1 427 ? -37.980 72.905  168.272 1.00 90.40  ? 427 GLN C CB    1 
ATOM   11015 C CG    . GLN C  1 427 ? -37.581 71.579  167.659 1.00 98.58  ? 427 GLN C CG    1 
ATOM   11016 C CD    . GLN C  1 427 ? -37.491 70.476  168.697 1.00 99.38  ? 427 GLN C CD    1 
ATOM   11017 O OE1   . GLN C  1 427 ? -38.088 70.566  169.771 1.00 93.73  ? 427 GLN C OE1   1 
ATOM   11018 N NE2   . GLN C  1 427 ? -36.730 69.434  168.387 1.00 106.86 ? 427 GLN C NE2   1 
ATOM   11019 N N     . LYS C  1 428 ? -39.228 74.824  166.240 1.00 84.83  ? 428 LYS C N     1 
ATOM   11020 C CA    . LYS C  1 428 ? -40.003 74.996  165.018 1.00 85.35  ? 428 LYS C CA    1 
ATOM   11021 C C     . LYS C  1 428 ? -39.345 75.963  164.030 1.00 82.28  ? 428 LYS C C     1 
ATOM   11022 O O     . LYS C  1 428 ? -39.372 75.733  162.821 1.00 79.86  ? 428 LYS C O     1 
ATOM   11023 C CB    . LYS C  1 428 ? -41.417 75.475  165.368 1.00 89.39  ? 428 LYS C CB    1 
ATOM   11024 C CG    . LYS C  1 428 ? -42.212 74.495  166.232 1.00 92.14  ? 428 LYS C CG    1 
ATOM   11025 C CD    . LYS C  1 428 ? -42.624 73.262  165.433 1.00 101.09 ? 428 LYS C CD    1 
ATOM   11026 C CE    . LYS C  1 428 ? -42.886 72.051  166.327 1.00 105.50 ? 428 LYS C CE    1 
ATOM   11027 N NZ    . LYS C  1 428 ? -44.325 71.856  166.667 1.00 105.50 ? 428 LYS C NZ    1 
ATOM   11028 N N     . LYS C  1 429 ? -38.746 77.032  164.549 1.00 82.37  ? 429 LYS C N     1 
ATOM   11029 C CA    . LYS C  1 429 ? -38.092 78.033  163.705 1.00 78.23  ? 429 LYS C CA    1 
ATOM   11030 C C     . LYS C  1 429 ? -36.735 77.580  163.158 1.00 78.66  ? 429 LYS C C     1 
ATOM   11031 O O     . LYS C  1 429 ? -36.072 78.340  162.452 1.00 72.96  ? 429 LYS C O     1 
ATOM   11032 C CB    . LYS C  1 429 ? -37.906 79.348  164.474 1.00 82.51  ? 429 LYS C CB    1 
ATOM   11033 C CG    . LYS C  1 429 ? -39.182 80.159  164.670 1.00 80.89  ? 429 LYS C CG    1 
ATOM   11034 C CD    . LYS C  1 429 ? -38.872 81.635  164.883 1.00 78.24  ? 429 LYS C CD    1 
ATOM   11035 C CE    . LYS C  1 429 ? -38.233 82.254  163.648 1.00 81.23  ? 429 LYS C CE    1 
ATOM   11036 N NZ    . LYS C  1 429 ? -37.729 83.628  163.929 1.00 84.83  ? 429 LYS C NZ    1 
ATOM   11037 N N     . LYS C  1 430 ? -36.329 76.352  163.481 1.00 78.93  ? 430 LYS C N     1 
ATOM   11038 C CA    . LYS C  1 430 ? -35.023 75.821  163.078 1.00 75.76  ? 430 LYS C CA    1 
ATOM   11039 C C     . LYS C  1 430 ? -34.697 76.064  161.602 1.00 75.82  ? 430 LYS C C     1 
ATOM   11040 O O     . LYS C  1 430 ? -33.610 76.543  161.269 1.00 74.65  ? 430 LYS C O     1 
ATOM   11041 C CB    . LYS C  1 430 ? -34.949 74.321  163.377 1.00 76.75  ? 430 LYS C CB    1 
ATOM   11042 C CG    . LYS C  1 430 ? -33.877 73.580  162.598 1.00 78.56  ? 430 LYS C CG    1 
ATOM   11043 C CD    . LYS C  1 430 ? -33.902 72.087  162.888 1.00 79.66  ? 430 LYS C CD    1 
ATOM   11044 C CE    . LYS C  1 430 ? -33.095 71.326  161.851 1.00 81.25  ? 430 LYS C CE    1 
ATOM   11045 N NZ    . LYS C  1 430 ? -33.657 71.527  160.486 1.00 83.67  ? 430 LYS C NZ    1 
ATOM   11046 N N     . THR C  1 431 ? -35.653 75.752  160.731 1.00 73.39  ? 431 THR C N     1 
ATOM   11047 C CA    . THR C  1 431 ? -35.462 75.851  159.285 1.00 74.28  ? 431 THR C CA    1 
ATOM   11048 C C     . THR C  1 431 ? -35.170 77.282  158.813 1.00 72.70  ? 431 THR C C     1 
ATOM   11049 O O     . THR C  1 431 ? -34.476 77.482  157.812 1.00 69.44  ? 431 THR C O     1 
ATOM   11050 C CB    . THR C  1 431 ? -36.696 75.318  158.532 1.00 73.85  ? 431 THR C CB    1 
ATOM   11051 O OG1   . THR C  1 431 ? -37.302 74.260  159.286 1.00 75.73  ? 431 THR C OG1   1 
ATOM   11052 C CG2   . THR C  1 431 ? -36.299 74.791  157.159 1.00 66.63  ? 431 THR C CG2   1 
ATOM   11053 N N     . GLU C  1 432 ? -35.688 78.271  159.537 1.00 71.18  ? 432 GLU C N     1 
ATOM   11054 C CA    . GLU C  1 432 ? -35.481 79.669  159.174 1.00 78.94  ? 432 GLU C CA    1 
ATOM   11055 C C     . GLU C  1 432 ? -34.098 80.150  159.623 1.00 73.78  ? 432 GLU C C     1 
ATOM   11056 O O     . GLU C  1 432 ? -33.447 80.920  158.916 1.00 72.47  ? 432 GLU C O     1 
ATOM   11057 C CB    . GLU C  1 432 ? -36.587 80.542  159.779 1.00 82.62  ? 432 GLU C CB    1 
ATOM   11058 C CG    . GLU C  1 432 ? -37.102 81.644  158.859 1.00 91.80  ? 432 GLU C CG    1 
ATOM   11059 C CD    . GLU C  1 432 ? -36.222 82.876  158.867 1.00 104.67 ? 432 GLU C CD    1 
ATOM   11060 O OE1   . GLU C  1 432 ? -35.367 83.001  157.966 1.00 106.20 ? 432 GLU C OE1   1 
ATOM   11061 O OE2   . GLU C  1 432 ? -36.388 83.718  159.777 1.00 108.42 ? 432 GLU C OE2   1 
ATOM   11062 N N     . PHE C  1 433 ? -33.665 79.691  160.797 1.00 72.19  ? 433 PHE C N     1 
ATOM   11063 C CA    . PHE C  1 433 ? -32.322 79.971  161.304 1.00 72.54  ? 433 PHE C CA    1 
ATOM   11064 C C     . PHE C  1 433 ? -31.260 79.551  160.291 1.00 65.34  ? 433 PHE C C     1 
ATOM   11065 O O     . PHE C  1 433 ? -30.315 80.292  160.013 1.00 64.23  ? 433 PHE C O     1 
ATOM   11066 C CB    . PHE C  1 433 ? -32.089 79.246  162.632 1.00 71.82  ? 433 PHE C CB    1 
ATOM   11067 C CG    . PHE C  1 433 ? -32.942 79.751  163.764 1.00 72.25  ? 433 PHE C CG    1 
ATOM   11068 C CD1   . PHE C  1 433 ? -33.167 81.107  163.928 1.00 71.38  ? 433 PHE C CD1   1 
ATOM   11069 C CD2   . PHE C  1 433 ? -33.516 78.867  164.666 1.00 73.20  ? 433 PHE C CD2   1 
ATOM   11070 C CE1   . PHE C  1 433 ? -33.948 81.575  164.972 1.00 73.99  ? 433 PHE C CE1   1 
ATOM   11071 C CE2   . PHE C  1 433 ? -34.301 79.329  165.711 1.00 76.13  ? 433 PHE C CE2   1 
ATOM   11072 C CZ    . PHE C  1 433 ? -34.515 80.686  165.863 1.00 76.03  ? 433 PHE C CZ    1 
ATOM   11073 N N     . LEU C  1 434 ? -31.434 78.351  159.743 1.00 65.59  ? 434 LEU C N     1 
ATOM   11074 C CA    . LEU C  1 434 ? -30.544 77.818  158.715 1.00 68.20  ? 434 LEU C CA    1 
ATOM   11075 C C     . LEU C  1 434 ? -30.588 78.661  157.443 1.00 66.63  ? 434 LEU C C     1 
ATOM   11076 O O     . LEU C  1 434 ? -29.552 78.925  156.830 1.00 61.83  ? 434 LEU C O     1 
ATOM   11077 C CB    . LEU C  1 434 ? -30.906 76.366  158.382 1.00 64.71  ? 434 LEU C CB    1 
ATOM   11078 C CG    . LEU C  1 434 ? -30.830 75.305  159.483 1.00 66.11  ? 434 LEU C CG    1 
ATOM   11079 C CD1   . LEU C  1 434 ? -30.666 73.922  158.874 1.00 66.56  ? 434 LEU C CD1   1 
ATOM   11080 C CD2   . LEU C  1 434 ? -29.711 75.590  160.472 1.00 64.53  ? 434 LEU C CD2   1 
ATOM   11081 N N     . ASP C  1 435 ? -31.792 79.068  157.047 1.00 67.56  ? 435 ASP C N     1 
ATOM   11082 C CA    . ASP C  1 435 ? -31.981 79.917  155.874 1.00 68.96  ? 435 ASP C CA    1 
ATOM   11083 C C     . ASP C  1 435 ? -31.266 81.254  156.058 1.00 66.82  ? 435 ASP C C     1 
ATOM   11084 O O     . ASP C  1 435 ? -30.635 81.764  155.129 1.00 61.24  ? 435 ASP C O     1 
ATOM   11085 C CB    . ASP C  1 435 ? -33.475 80.140  155.608 1.00 74.44  ? 435 ASP C CB    1 
ATOM   11086 C CG    . ASP C  1 435 ? -33.746 80.708  154.225 1.00 84.39  ? 435 ASP C CG    1 
ATOM   11087 O OD1   . ASP C  1 435 ? -33.499 79.990  153.231 1.00 85.74  ? 435 ASP C OD1   1 
ATOM   11088 O OD2   . ASP C  1 435 ? -34.220 81.861  154.132 1.00 92.64  ? 435 ASP C OD2   1 
ATOM   11089 N N     . TRP C  1 436 ? -31.374 81.811  157.263 1.00 64.13  ? 436 TRP C N     1 
ATOM   11090 C CA    . TRP C  1 436 ? -30.649 83.025  157.628 1.00 67.91  ? 436 TRP C CA    1 
ATOM   11091 C C     . TRP C  1 436 ? -29.148 82.836  157.450 1.00 66.80  ? 436 TRP C C     1 
ATOM   11092 O O     . TRP C  1 436 ? -28.512 83.558  156.682 1.00 64.35  ? 436 TRP C O     1 
ATOM   11093 C CB    . TRP C  1 436 ? -30.952 83.426  159.075 1.00 68.47  ? 436 TRP C CB    1 
ATOM   11094 C CG    . TRP C  1 436 ? -30.137 84.598  159.542 1.00 72.01  ? 436 TRP C CG    1 
ATOM   11095 C CD1   . TRP C  1 436 ? -30.363 85.917  159.264 1.00 69.21  ? 436 TRP C CD1   1 
ATOM   11096 C CD2   . TRP C  1 436 ? -28.962 84.557  160.365 1.00 74.10  ? 436 TRP C CD2   1 
ATOM   11097 N NE1   . TRP C  1 436 ? -29.401 86.697  159.863 1.00 71.43  ? 436 TRP C NE1   1 
ATOM   11098 C CE2   . TRP C  1 436 ? -28.531 85.887  160.546 1.00 74.94  ? 436 TRP C CE2   1 
ATOM   11099 C CE3   . TRP C  1 436 ? -28.236 83.525  160.968 1.00 71.81  ? 436 TRP C CE3   1 
ATOM   11100 C CZ2   . TRP C  1 436 ? -27.403 86.211  161.304 1.00 69.61  ? 436 TRP C CZ2   1 
ATOM   11101 C CZ3   . TRP C  1 436 ? -27.118 83.850  161.720 1.00 72.28  ? 436 TRP C CZ3   1 
ATOM   11102 C CH2   . TRP C  1 436 ? -26.713 85.180  161.881 1.00 71.55  ? 436 TRP C CH2   1 
ATOM   11103 N N     . LEU C  1 437 ? -28.601 81.859  158.168 1.00 65.10  ? 437 LEU C N     1 
ATOM   11104 C CA    . LEU C  1 437 ? -27.182 81.525  158.108 1.00 64.37  ? 437 LEU C CA    1 
ATOM   11105 C C     . LEU C  1 437 ? -26.701 81.320  156.676 1.00 63.67  ? 437 LEU C C     1 
ATOM   11106 O O     . LEU C  1 437 ? -25.628 81.791  156.294 1.00 62.84  ? 437 LEU C O     1 
ATOM   11107 C CB    . LEU C  1 437 ? -26.909 80.269  158.932 1.00 64.04  ? 437 LEU C CB    1 
ATOM   11108 C CG    . LEU C  1 437 ? -25.448 79.901  159.186 1.00 62.43  ? 437 LEU C CG    1 
ATOM   11109 C CD1   . LEU C  1 437 ? -24.764 80.991  159.988 1.00 56.60  ? 437 LEU C CD1   1 
ATOM   11110 C CD2   . LEU C  1 437 ? -25.362 78.579  159.914 1.00 55.48  ? 437 LEU C CD2   1 
ATOM   11111 N N     . GLU C  1 438 ? -27.510 80.616  155.891 1.00 62.91  ? 438 GLU C N     1 
ATOM   11112 C CA    . GLU C  1 438 ? -27.203 80.381  154.488 1.00 68.78  ? 438 GLU C CA    1 
ATOM   11113 C C     . GLU C  1 438 ? -27.089 81.697  153.717 1.00 68.78  ? 438 GLU C C     1 
ATOM   11114 O O     . GLU C  1 438 ? -26.225 81.839  152.851 1.00 68.39  ? 438 GLU C O     1 
ATOM   11115 C CB    . GLU C  1 438 ? -28.265 79.486  153.851 1.00 68.15  ? 438 GLU C CB    1 
ATOM   11116 C CG    . GLU C  1 438 ? -27.910 79.017  152.450 1.00 76.04  ? 438 GLU C CG    1 
ATOM   11117 C CD    . GLU C  1 438 ? -29.030 78.240  151.785 1.00 91.37  ? 438 GLU C CD    1 
ATOM   11118 O OE1   . GLU C  1 438 ? -29.973 77.817  152.488 1.00 88.89  ? 438 GLU C OE1   1 
ATOM   11119 O OE2   . GLU C  1 438 ? -28.968 78.057  150.551 1.00 91.57  ? 438 GLU C OE2   1 
ATOM   11120 N N     . LYS C  1 439 ? -27.952 82.659  154.035 1.00 70.41  ? 439 LYS C N     1 
ATOM   11121 C CA    . LYS C  1 439 ? -27.926 83.946  153.343 1.00 71.91  ? 439 LYS C CA    1 
ATOM   11122 C C     . LYS C  1 439 ? -26.739 84.803  153.780 1.00 66.16  ? 439 LYS C C     1 
ATOM   11123 O O     . LYS C  1 439 ? -26.109 85.461  152.952 1.00 64.46  ? 439 LYS C O     1 
ATOM   11124 C CB    . LYS C  1 439 ? -29.235 84.713  153.562 1.00 75.31  ? 439 LYS C CB    1 
ATOM   11125 C CG    . LYS C  1 439 ? -29.161 86.168  153.114 1.00 85.29  ? 439 LYS C CG    1 
ATOM   11126 C CD    . LYS C  1 439 ? -30.494 86.688  152.607 1.00 83.73  ? 439 LYS C CD    1 
ATOM   11127 C CE    . LYS C  1 439 ? -30.372 88.141  152.174 1.00 81.87  ? 439 LYS C CE    1 
ATOM   11128 N NZ    . LYS C  1 439 ? -31.452 88.537  151.231 1.00 67.90  ? 439 LYS C NZ    1 
ATOM   11129 N N     . VAL C  1 440 ? -26.441 84.794  155.078 1.00 65.69  ? 440 VAL C N     1 
ATOM   11130 C CA    . VAL C  1 440 ? -25.280 85.509  155.608 1.00 64.23  ? 440 VAL C CA    1 
ATOM   11131 C C     . VAL C  1 440 ? -24.012 85.062  154.889 1.00 61.51  ? 440 VAL C C     1 
ATOM   11132 O O     . VAL C  1 440 ? -23.192 85.880  154.471 1.00 61.60  ? 440 VAL C O     1 
ATOM   11133 C CB    . VAL C  1 440 ? -25.111 85.280  157.124 1.00 65.28  ? 440 VAL C CB    1 
ATOM   11134 C CG1   . VAL C  1 440 ? -23.831 85.935  157.627 1.00 59.76  ? 440 VAL C CG1   1 
ATOM   11135 C CG2   . VAL C  1 440 ? -26.320 85.805  157.877 1.00 59.58  ? 440 VAL C CG2   1 
ATOM   11136 N N     . TYR C  1 441 ? -23.879 83.749  154.745 1.00 62.81  ? 441 TYR C N     1 
ATOM   11137 C CA    . TYR C  1 441 ? -22.771 83.132  154.030 1.00 61.01  ? 441 TYR C CA    1 
ATOM   11138 C C     . TYR C  1 441 ? -22.753 83.557  152.564 1.00 59.78  ? 441 TYR C C     1 
ATOM   11139 O O     . TYR C  1 441 ? -21.691 83.826  151.997 1.00 59.17  ? 441 TYR C O     1 
ATOM   11140 C CB    . TYR C  1 441 ? -22.877 81.612  154.145 1.00 62.02  ? 441 TYR C CB    1 
ATOM   11141 C CG    . TYR C  1 441 ? -21.617 80.854  153.803 1.00 60.39  ? 441 TYR C CG    1 
ATOM   11142 C CD1   . TYR C  1 441 ? -20.562 80.783  154.702 1.00 63.03  ? 441 TYR C CD1   1 
ATOM   11143 C CD2   . TYR C  1 441 ? -21.496 80.183  152.593 1.00 61.31  ? 441 TYR C CD2   1 
ATOM   11144 C CE1   . TYR C  1 441 ? -19.415 80.077  154.401 1.00 60.11  ? 441 TYR C CE1   1 
ATOM   11145 C CE2   . TYR C  1 441 ? -20.352 79.475  152.282 1.00 60.93  ? 441 TYR C CE2   1 
ATOM   11146 C CZ    . TYR C  1 441 ? -19.315 79.427  153.190 1.00 58.80  ? 441 TYR C CZ    1 
ATOM   11147 O OH    . TYR C  1 441 ? -18.173 78.726  152.885 1.00 60.83  ? 441 TYR C OH    1 
ATOM   11148 N N     . GLU C  1 442 ? -23.935 83.618  151.957 1.00 63.83  ? 442 GLU C N     1 
ATOM   11149 C CA    . GLU C  1 442 ? -24.065 84.023  150.563 1.00 65.79  ? 442 GLU C CA    1 
ATOM   11150 C C     . GLU C  1 442 ? -23.668 85.485  150.370 1.00 64.24  ? 442 GLU C C     1 
ATOM   11151 O O     . GLU C  1 442 ? -23.081 85.845  149.350 1.00 62.01  ? 442 GLU C O     1 
ATOM   11152 C CB    . GLU C  1 442 ? -25.497 83.794  150.069 1.00 68.08  ? 442 GLU C CB    1 
ATOM   11153 C CG    . GLU C  1 442 ? -25.742 84.222  148.622 1.00 65.87  ? 442 GLU C CG    1 
ATOM   11154 C CD    . GLU C  1 442 ? -24.945 83.401  147.625 1.00 72.84  ? 442 GLU C CD    1 
ATOM   11155 O OE1   . GLU C  1 442 ? -24.617 82.237  147.939 1.00 78.25  ? 442 GLU C OE1   1 
ATOM   11156 O OE2   . GLU C  1 442 ? -24.646 83.919  146.527 1.00 70.18  ? 442 GLU C OE2   1 
ATOM   11157 N N     . PHE C  1 443 ? -23.982 86.325  151.353 1.00 60.39  ? 443 PHE C N     1 
ATOM   11158 C CA    . PHE C  1 443 ? -23.640 87.743  151.272 1.00 61.84  ? 443 PHE C CA    1 
ATOM   11159 C C     . PHE C  1 443 ? -22.131 87.969  151.328 1.00 64.54  ? 443 PHE C C     1 
ATOM   11160 O O     . PHE C  1 443 ? -21.591 88.783  150.580 1.00 63.49  ? 443 PHE C O     1 
ATOM   11161 C CB    . PHE C  1 443 ? -24.322 88.534  152.393 1.00 65.45  ? 443 PHE C CB    1 
ATOM   11162 C CG    . PHE C  1 443 ? -23.760 89.918  152.583 1.00 69.66  ? 443 PHE C CG    1 
ATOM   11163 C CD1   . PHE C  1 443 ? -23.788 90.838  151.547 1.00 69.40  ? 443 PHE C CD1   1 
ATOM   11164 C CD2   . PHE C  1 443 ? -23.202 90.298  153.794 1.00 69.40  ? 443 PHE C CD2   1 
ATOM   11165 C CE1   . PHE C  1 443 ? -23.267 92.109  151.711 1.00 73.23  ? 443 PHE C CE1   1 
ATOM   11166 C CE2   . PHE C  1 443 ? -22.681 91.571  153.965 1.00 73.53  ? 443 PHE C CE2   1 
ATOM   11167 C CZ    . PHE C  1 443 ? -22.715 92.476  152.922 1.00 71.72  ? 443 PHE C CZ    1 
ATOM   11168 N N     . MET C  1 444 ? -21.457 87.243  152.213 1.00 63.34  ? 444 MET C N     1 
ATOM   11169 C CA    . MET C  1 444 ? -20.030 87.441  152.453 1.00 62.15  ? 444 MET C CA    1 
ATOM   11170 C C     . MET C  1 444 ? -19.143 86.885  151.337 1.00 61.17  ? 444 MET C C     1 
ATOM   11171 O O     . MET C  1 444 ? -17.962 87.223  151.264 1.00 66.02  ? 444 MET C O     1 
ATOM   11172 C CB    . MET C  1 444 ? -19.635 86.807  153.789 1.00 57.46  ? 444 MET C CB    1 
ATOM   11173 C CG    . MET C  1 444 ? -20.227 87.503  155.000 1.00 58.49  ? 444 MET C CG    1 
ATOM   11174 S SD    . MET C  1 444 ? -19.620 89.191  155.205 1.00 62.16  ? 444 MET C SD    1 
ATOM   11175 C CE    . MET C  1 444 ? -17.861 88.896  155.393 1.00 60.32  ? 444 MET C CE    1 
ATOM   11176 N N     . LYS C  1 445 ? -19.720 86.052  150.473 1.00 64.35  ? 445 LYS C N     1 
ATOM   11177 C CA    . LYS C  1 445 ? -18.975 85.360  149.416 1.00 69.32  ? 445 LYS C CA    1 
ATOM   11178 C C     . LYS C  1 445 ? -17.967 86.218  148.612 1.00 68.94  ? 445 LYS C C     1 
ATOM   11179 O O     . LYS C  1 445 ? -16.834 85.782  148.385 1.00 70.36  ? 445 LYS C O     1 
ATOM   11180 C CB    . LYS C  1 445 ? -19.965 84.699  148.445 1.00 69.82  ? 445 LYS C CB    1 
ATOM   11181 C CG    . LYS C  1 445 ? -19.305 83.990  147.264 1.00 73.13  ? 445 LYS C CG    1 
ATOM   11182 C CD    . LYS C  1 445 ? -20.323 83.400  146.294 1.00 77.22  ? 445 LYS C CD    1 
ATOM   11183 C CE    . LYS C  1 445 ? -19.625 82.636  145.175 1.00 78.61  ? 445 LYS C CE    1 
ATOM   11184 N NZ    . LYS C  1 445 ? -20.567 82.022  144.194 1.00 86.99  ? 445 LYS C NZ    1 
ATOM   11185 N N     . PRO C  1 446 ? -18.356 87.435  148.183 1.00 73.21  ? 446 PRO C N     1 
ATOM   11186 C CA    . PRO C  1 446 ? -17.370 88.167  147.374 1.00 66.75  ? 446 PRO C CA    1 
ATOM   11187 C C     . PRO C  1 446 ? -16.214 88.790  148.165 1.00 67.81  ? 446 PRO C C     1 
ATOM   11188 O O     . PRO C  1 446 ? -15.204 89.144  147.556 1.00 68.97  ? 446 PRO C O     1 
ATOM   11189 C CB    . PRO C  1 446 ? -18.204 89.275  146.712 1.00 69.42  ? 446 PRO C CB    1 
ATOM   11190 C CG    . PRO C  1 446 ? -19.626 88.902  146.914 1.00 68.96  ? 446 PRO C CG    1 
ATOM   11191 C CD    . PRO C  1 446 ? -19.668 88.105  148.177 1.00 69.29  ? 446 PRO C CD    1 
ATOM   11192 N N     . PHE C  1 447 ? -16.349 88.922  149.482 1.00 65.19  ? 447 PHE C N     1 
ATOM   11193 C CA    . PHE C  1 447 ? -15.344 89.628  150.278 1.00 67.30  ? 447 PHE C CA    1 
ATOM   11194 C C     . PHE C  1 447 ? -14.337 88.693  150.951 1.00 67.41  ? 447 PHE C C     1 
ATOM   11195 O O     . PHE C  1 447 ? -13.343 89.144  151.526 1.00 57.64  ? 447 PHE C O     1 
ATOM   11196 C CB    . PHE C  1 447 ? -16.031 90.494  151.339 1.00 66.10  ? 447 PHE C CB    1 
ATOM   11197 C CG    . PHE C  1 447 ? -17.199 91.281  150.816 1.00 73.08  ? 447 PHE C CG    1 
ATOM   11198 C CD1   . PHE C  1 447 ? -17.003 92.354  149.960 1.00 74.64  ? 447 PHE C CD1   1 
ATOM   11199 C CD2   . PHE C  1 447 ? -18.493 90.954  151.192 1.00 69.76  ? 447 PHE C CD2   1 
ATOM   11200 C CE1   . PHE C  1 447 ? -18.080 93.084  149.481 1.00 73.57  ? 447 PHE C CE1   1 
ATOM   11201 C CE2   . PHE C  1 447 ? -19.574 91.679  150.718 1.00 72.24  ? 447 PHE C CE2   1 
ATOM   11202 C CZ    . PHE C  1 447 ? -19.366 92.745  149.862 1.00 72.23  ? 447 PHE C CZ    1 
ATOM   11203 N N     . VAL C  1 448 ? -14.591 87.392  150.873 1.00 67.28  ? 448 VAL C N     1 
ATOM   11204 C CA    . VAL C  1 448 ? -13.722 86.417  151.515 1.00 62.81  ? 448 VAL C CA    1 
ATOM   11205 C C     . VAL C  1 448 ? -12.892 85.656  150.486 1.00 64.19  ? 448 VAL C C     1 
ATOM   11206 O O     . VAL C  1 448 ? -12.784 86.072  149.331 1.00 66.17  ? 448 VAL C O     1 
ATOM   11207 C CB    . VAL C  1 448 ? -14.533 85.421  152.363 1.00 62.25  ? 448 VAL C CB    1 
ATOM   11208 C CG1   . VAL C  1 448 ? -15.327 86.173  153.421 1.00 60.23  ? 448 VAL C CG1   1 
ATOM   11209 C CG2   . VAL C  1 448 ? -15.465 84.587  151.485 1.00 62.30  ? 448 VAL C CG2   1 
ATOM   11210 N N     . SER C  1 449 ? -12.295 84.550  150.919 1.00 63.47  ? 449 SER C N     1 
ATOM   11211 C CA    . SER C  1 449 ? -11.457 83.730  150.055 1.00 63.44  ? 449 SER C CA    1 
ATOM   11212 C C     . SER C  1 449 ? -12.252 83.160  148.887 1.00 64.35  ? 449 SER C C     1 
ATOM   11213 O O     . SER C  1 449 ? -13.441 82.865  149.014 1.00 61.08  ? 449 SER C O     1 
ATOM   11214 C CB    . SER C  1 449 ? -10.820 82.593  150.851 1.00 59.02  ? 449 SER C CB    1 
ATOM   11215 O OG    . SER C  1 449 ? -11.811 81.736  151.391 1.00 58.49  ? 449 SER C OG    1 
ATOM   11216 N N     . LYS C  1 450 ? -11.588 83.019  147.743 1.00 67.49  ? 450 LYS C N     1 
ATOM   11217 C CA    . LYS C  1 450 ? -12.236 82.550  146.521 1.00 70.57  ? 450 LYS C CA    1 
ATOM   11218 C C     . LYS C  1 450 ? -11.337 81.581  145.752 1.00 71.85  ? 450 LYS C C     1 
ATOM   11219 O O     . LYS C  1 450 ? -10.114 81.685  145.813 1.00 72.02  ? 450 LYS C O     1 
ATOM   11220 C CB    . LYS C  1 450 ? -12.610 83.732  145.620 1.00 72.66  ? 450 LYS C CB    1 
ATOM   11221 C CG    . LYS C  1 450 ? -13.057 84.988  146.357 1.00 74.18  ? 450 LYS C CG    1 
ATOM   11222 C CD    . LYS C  1 450 ? -13.440 86.109  145.406 1.00 74.74  ? 450 LYS C CD    1 
ATOM   11223 C CE    . LYS C  1 450 ? -12.526 87.319  145.562 1.00 80.32  ? 450 LYS C CE    1 
ATOM   11224 N NZ    . LYS C  1 450 ? -12.596 87.921  146.923 1.00 76.23  ? 450 LYS C NZ    1 
ATOM   11225 N N     . ASN C  1 451 ? -11.961 80.658  145.024 1.00 67.62  ? 451 ASN C N     1 
ATOM   11226 C CA    . ASN C  1 451 ? -11.258 79.678  144.191 1.00 74.16  ? 451 ASN C CA    1 
ATOM   11227 C C     . ASN C  1 451 ? -10.082 78.966  144.860 1.00 71.61  ? 451 ASN C C     1 
ATOM   11228 O O     . ASN C  1 451 ? -8.929  79.182  144.483 1.00 73.52  ? 451 ASN C O     1 
ATOM   11229 C CB    . ASN C  1 451 ? -10.753 80.347  142.910 1.00 78.88  ? 451 ASN C CB    1 
ATOM   11230 C CG    . ASN C  1 451 ? -11.877 80.834  142.023 1.00 86.79  ? 451 ASN C CG    1 
ATOM   11231 O OD1   . ASN C  1 451 ? -12.921 80.191  141.914 1.00 86.87  ? 451 ASN C OD1   1 
ATOM   11232 N ND2   . ASN C  1 451 ? -11.672 81.983  141.387 1.00 89.79  ? 451 ASN C ND2   1 
ATOM   11233 N N     . PRO C  1 452 ? -10.370 78.100  145.845 1.00 67.72  ? 452 PRO C N     1 
ATOM   11234 C CA    . PRO C  1 452 ? -11.709 77.829  146.374 1.00 64.19  ? 452 PRO C CA    1 
ATOM   11235 C C     . PRO C  1 452 ? -12.016 78.659  147.615 1.00 63.50  ? 452 PRO C C     1 
ATOM   11236 O O     . PRO C  1 452 ? -11.122 79.319  148.146 1.00 61.56  ? 452 PRO C O     1 
ATOM   11237 C CB    . PRO C  1 452 ? -11.639 76.348  146.724 1.00 61.90  ? 452 PRO C CB    1 
ATOM   11238 C CG    . PRO C  1 452 ? -10.227 76.177  147.187 1.00 62.15  ? 452 PRO C CG    1 
ATOM   11239 C CD    . PRO C  1 452 ? -9.383  77.139  146.369 1.00 67.78  ? 452 PRO C CD    1 
ATOM   11240 N N     . ARG C  1 453 ? -13.265 78.622  148.069 1.00 61.96  ? 453 ARG C N     1 
ATOM   11241 C CA    . ARG C  1 453 ? -13.650 79.283  149.312 1.00 57.87  ? 453 ARG C CA    1 
ATOM   11242 C C     . ARG C  1 453 ? -13.194 78.438  150.497 1.00 58.63  ? 453 ARG C C     1 
ATOM   11243 O O     . ARG C  1 453 ? -13.562 77.271  150.611 1.00 56.00  ? 453 ARG C O     1 
ATOM   11244 C CB    . ARG C  1 453 ? -15.163 79.511  149.357 1.00 54.57  ? 453 ARG C CB    1 
ATOM   11245 C CG    . ARG C  1 453 ? -15.646 80.263  150.587 1.00 55.42  ? 453 ARG C CG    1 
ATOM   11246 C CD    . ARG C  1 453 ? -17.094 80.700  150.422 1.00 60.42  ? 453 ARG C CD    1 
ATOM   11247 N NE    . ARG C  1 453 ? -17.539 81.561  151.514 1.00 61.58  ? 453 ARG C NE    1 
ATOM   11248 C CZ    . ARG C  1 453 ? -18.689 82.228  151.518 1.00 62.39  ? 453 ARG C CZ    1 
ATOM   11249 N NH1   . ARG C  1 453 ? -19.514 82.135  150.485 1.00 62.29  ? 453 ARG C NH1   1 
ATOM   11250 N NH2   . ARG C  1 453 ? -19.014 82.988  152.555 1.00 60.13  ? 453 ARG C NH2   1 
ATOM   11251 N N     . LEU C  1 454 ? -12.398 79.034  151.379 1.00 56.47  ? 454 LEU C N     1 
ATOM   11252 C CA    . LEU C  1 454 ? -11.685 78.272  152.403 1.00 55.10  ? 454 LEU C CA    1 
ATOM   11253 C C     . LEU C  1 454 ? -12.540 77.922  153.617 1.00 53.42  ? 454 LEU C C     1 
ATOM   11254 O O     . LEU C  1 454 ? -13.514 78.605  153.925 1.00 47.63  ? 454 LEU C O     1 
ATOM   11255 C CB    . LEU C  1 454 ? -10.445 79.047  152.855 1.00 51.80  ? 454 LEU C CB    1 
ATOM   11256 C CG    . LEU C  1 454 ? -9.494  79.433  151.720 1.00 53.57  ? 454 LEU C CG    1 
ATOM   11257 C CD1   . LEU C  1 454 ? -8.348  80.291  152.227 1.00 52.17  ? 454 LEU C CD1   1 
ATOM   11258 C CD2   . LEU C  1 454 ? -8.972  78.194  151.021 1.00 55.66  ? 454 LEU C CD2   1 
ATOM   11259 N N     . GLY C  1 455 ? -12.156 76.844  154.296 1.00 50.02  ? 455 GLY C N     1 
ATOM   11260 C CA    . GLY C  1 455 ? -12.812 76.406  155.514 1.00 44.87  ? 455 GLY C CA    1 
ATOM   11261 C C     . GLY C  1 455 ? -11.798 75.849  156.497 1.00 44.11  ? 455 GLY C C     1 
ATOM   11262 O O     . GLY C  1 455 ? -10.602 75.850  156.227 1.00 46.69  ? 455 GLY C O     1 
ATOM   11263 N N     . TYR C  1 456 ? -12.279 75.357  157.632 1.00 46.02  ? 456 TYR C N     1 
ATOM   11264 C CA    . TYR C  1 456 ? -11.410 74.868  158.697 1.00 39.58  ? 456 TYR C CA    1 
ATOM   11265 C C     . TYR C  1 456 ? -11.968 73.551  159.226 1.00 43.44  ? 456 TYR C C     1 
ATOM   11266 O O     . TYR C  1 456 ? -13.115 73.491  159.664 1.00 36.33  ? 456 TYR C O     1 
ATOM   11267 C CB    . TYR C  1 456 ? -11.298 75.926  159.797 1.00 40.63  ? 456 TYR C CB    1 
ATOM   11268 C CG    . TYR C  1 456 ? -10.601 75.506  161.071 1.00 40.65  ? 456 TYR C CG    1 
ATOM   11269 C CD1   . TYR C  1 456 ? -9.489  74.675  161.048 1.00 36.98  ? 456 TYR C CD1   1 
ATOM   11270 C CD2   . TYR C  1 456 ? -11.043 75.975  162.302 1.00 39.79  ? 456 TYR C CD2   1 
ATOM   11271 C CE1   . TYR C  1 456 ? -8.854  74.305  162.220 1.00 32.36  ? 456 TYR C CE1   1 
ATOM   11272 C CE2   . TYR C  1 456 ? -10.418 75.614  163.470 1.00 41.97  ? 456 TYR C CE2   1 
ATOM   11273 C CZ    . TYR C  1 456 ? -9.322  74.781  163.425 1.00 37.72  ? 456 TYR C CZ    1 
ATOM   11274 O OH    . TYR C  1 456 ? -8.702  74.422  164.599 1.00 32.92  ? 456 TYR C OH    1 
ATOM   11275 N N     . VAL C  1 457 ? -11.153 72.499  159.181 1.00 38.31  ? 457 VAL C N     1 
ATOM   11276 C CA    . VAL C  1 457 ? -11.641 71.137  159.399 1.00 39.95  ? 457 VAL C CA    1 
ATOM   11277 C C     . VAL C  1 457 ? -12.212 70.919  160.805 1.00 38.11  ? 457 VAL C C     1 
ATOM   11278 O O     . VAL C  1 457 ? -13.075 70.063  160.998 1.00 35.47  ? 457 VAL C O     1 
ATOM   11279 C CB    . VAL C  1 457 ? -10.526 70.092  159.123 1.00 37.35  ? 457 VAL C CB    1 
ATOM   11280 C CG1   . VAL C  1 457 ? -9.499  70.069  160.247 1.00 35.10  ? 457 VAL C CG1   1 
ATOM   11281 C CG2   . VAL C  1 457 ? -11.132 68.711  158.904 1.00 36.35  ? 457 VAL C CG2   1 
ATOM   11282 N N     . ASN C  1 458 ? -11.753 71.698  161.780 1.00 35.36  ? 458 ASN C N     1 
ATOM   11283 C CA    . ASN C  1 458 ? -12.321 71.610  163.121 1.00 36.36  ? 458 ASN C CA    1 
ATOM   11284 C C     . ASN C  1 458 ? -13.662 72.327  163.197 1.00 38.36  ? 458 ASN C C     1 
ATOM   11285 O O     . ASN C  1 458 ? -14.450 72.102  164.115 1.00 37.02  ? 458 ASN C O     1 
ATOM   11286 C CB    . ASN C  1 458 ? -11.358 72.174  164.160 1.00 37.32  ? 458 ASN C CB    1 
ATOM   11287 C CG    . ASN C  1 458 ? -10.532 71.094  164.826 1.00 40.55  ? 458 ASN C CG    1 
ATOM   11288 O OD1   . ASN C  1 458 ? -10.934 69.929  164.868 1.00 32.36  ? 458 ASN C OD1   1 
ATOM   11289 N ND2   . ASN C  1 458 ? -9.372  71.472  165.353 1.00 35.89  ? 458 ASN C ND2   1 
ATOM   11290 N N     . HIS C  1 459 ? -13.908 73.195  162.223 1.00 36.84  ? 459 HIS C N     1 
ATOM   11291 C CA    . HIS C  1 459 ? -15.231 73.769  162.023 1.00 46.54  ? 459 HIS C CA    1 
ATOM   11292 C C     . HIS C  1 459 ? -15.901 73.029  160.876 1.00 46.04  ? 459 HIS C C     1 
ATOM   11293 O O     . HIS C  1 459 ? -16.283 73.632  159.872 1.00 38.93  ? 459 HIS C O     1 
ATOM   11294 C CB    . HIS C  1 459 ? -15.147 75.265  161.731 1.00 41.40  ? 459 HIS C CB    1 
ATOM   11295 C CG    . HIS C  1 459 ? -14.762 76.085  162.921 1.00 52.18  ? 459 HIS C CG    1 
ATOM   11296 N ND1   . HIS C  1 459 ? -14.711 77.463  162.895 1.00 60.24  ? 459 HIS C ND1   1 
ATOM   11297 C CD2   . HIS C  1 459 ? -14.410 75.720  164.176 1.00 55.97  ? 459 HIS C CD2   1 
ATOM   11298 C CE1   . HIS C  1 459 ? -14.341 77.909  164.082 1.00 56.58  ? 459 HIS C CE1   1 
ATOM   11299 N NE2   . HIS C  1 459 ? -14.155 76.872  164.879 1.00 55.24  ? 459 HIS C NE2   1 
ATOM   11300 N N     . ILE C  1 460 ? -16.013 71.712  161.036 1.00 43.37  ? 460 ILE C N     1 
ATOM   11301 C CA    . ILE C  1 460 ? -16.559 70.827  160.014 1.00 44.77  ? 460 ILE C CA    1 
ATOM   11302 C C     . ILE C  1 460 ? -17.947 71.285  159.564 1.00 40.87  ? 460 ILE C C     1 
ATOM   11303 O O     . ILE C  1 460 ? -18.815 71.595  160.381 1.00 37.29  ? 460 ILE C O     1 
ATOM   11304 C CB    . ILE C  1 460 ? -16.614 69.364  160.526 1.00 41.11  ? 460 ILE C CB    1 
ATOM   11305 C CG1   . ILE C  1 460 ? -17.109 68.419  159.426 1.00 45.19  ? 460 ILE C CG1   1 
ATOM   11306 C CG2   . ILE C  1 460 ? -17.444 69.255  161.805 1.00 40.62  ? 460 ILE C CG2   1 
ATOM   11307 C CD1   . ILE C  1 460 ? -15.999 67.914  158.533 1.00 52.54  ? 460 ILE C CD1   1 
ATOM   11308 N N     . ASP C  1 461 ? -18.135 71.341  158.252 1.00 40.69  ? 461 ASP C N     1 
ATOM   11309 C CA    . ASP C  1 461 ? -19.366 71.861  157.676 1.00 51.63  ? 461 ASP C CA    1 
ATOM   11310 C C     . ASP C  1 461 ? -19.782 70.984  156.497 1.00 46.88  ? 461 ASP C C     1 
ATOM   11311 O O     . ASP C  1 461 ? -19.116 70.958  155.462 1.00 48.23  ? 461 ASP C O     1 
ATOM   11312 C CB    . ASP C  1 461 ? -19.162 73.318  157.254 1.00 52.64  ? 461 ASP C CB    1 
ATOM   11313 C CG    . ASP C  1 461 ? -20.401 73.945  156.647 1.00 55.19  ? 461 ASP C CG    1 
ATOM   11314 O OD1   . ASP C  1 461 ? -21.497 73.349  156.712 1.00 56.11  ? 461 ASP C OD1   1 
ATOM   11315 O OD2   . ASP C  1 461 ? -20.265 75.062  156.105 1.00 57.15  ? 461 ASP C OD2   1 
ATOM   11316 N N     . LEU C  1 462 ? -20.882 70.258  156.671 1.00 51.30  ? 462 LEU C N     1 
ATOM   11317 C CA    . LEU C  1 462 ? -21.333 69.292  155.675 1.00 53.53  ? 462 LEU C CA    1 
ATOM   11318 C C     . LEU C  1 462 ? -22.046 69.956  154.498 1.00 55.90  ? 462 LEU C C     1 
ATOM   11319 O O     . LEU C  1 462 ? -22.381 69.293  153.514 1.00 55.03  ? 462 LEU C O     1 
ATOM   11320 C CB    . LEU C  1 462 ? -22.247 68.252  156.327 1.00 51.18  ? 462 LEU C CB    1 
ATOM   11321 C CG    . LEU C  1 462 ? -21.566 67.226  157.239 1.00 47.36  ? 462 LEU C CG    1 
ATOM   11322 C CD1   . LEU C  1 462 ? -22.585 66.250  157.818 1.00 51.24  ? 462 LEU C CD1   1 
ATOM   11323 C CD2   . LEU C  1 462 ? -20.481 66.489  156.475 1.00 43.83  ? 462 LEU C CD2   1 
ATOM   11324 N N     . ASP C  1 463 ? -22.271 71.263  154.598 1.00 55.83  ? 463 ASP C N     1 
ATOM   11325 C CA    . ASP C  1 463 ? -22.895 72.013  153.511 1.00 58.51  ? 463 ASP C CA    1 
ATOM   11326 C C     . ASP C  1 463 ? -22.028 71.979  152.261 1.00 59.33  ? 463 ASP C C     1 
ATOM   11327 O O     . ASP C  1 463 ? -22.533 72.072  151.142 1.00 61.48  ? 463 ASP C O     1 
ATOM   11328 C CB    . ASP C  1 463 ? -23.150 73.464  153.922 1.00 60.49  ? 463 ASP C CB    1 
ATOM   11329 C CG    . ASP C  1 463 ? -24.177 73.587  155.027 1.00 61.91  ? 463 ASP C CG    1 
ATOM   11330 O OD1   . ASP C  1 463 ? -24.864 72.585  155.317 1.00 59.59  ? 463 ASP C OD1   1 
ATOM   11331 O OD2   . ASP C  1 463 ? -24.300 74.688  155.604 1.00 61.15  ? 463 ASP C OD2   1 
ATOM   11332 N N     . LEU C  1 464 ? -20.722 71.835  152.462 1.00 55.31  ? 464 LEU C N     1 
ATOM   11333 C CA    . LEU C  1 464 ? -19.764 71.800  151.363 1.00 56.73  ? 464 LEU C CA    1 
ATOM   11334 C C     . LEU C  1 464 ? -19.833 70.485  150.593 1.00 59.19  ? 464 LEU C C     1 
ATOM   11335 O O     . LEU C  1 464 ? -19.218 70.345  149.536 1.00 63.49  ? 464 LEU C O     1 
ATOM   11336 C CB    . LEU C  1 464 ? -18.339 72.014  151.883 1.00 58.75  ? 464 LEU C CB    1 
ATOM   11337 C CG    . LEU C  1 464 ? -17.926 73.397  152.401 1.00 61.91  ? 464 LEU C CG    1 
ATOM   11338 C CD1   . LEU C  1 464 ? -18.440 73.664  153.813 1.00 64.47  ? 464 LEU C CD1   1 
ATOM   11339 C CD2   . LEU C  1 464 ? -16.411 73.571  152.330 1.00 58.93  ? 464 LEU C CD2   1 
ATOM   11340 N N     . GLY C  1 465 ? -20.572 69.522  151.137 1.00 56.97  ? 465 GLY C N     1 
ATOM   11341 C CA    . GLY C  1 465 ? -20.766 68.239  150.485 1.00 58.87  ? 465 GLY C CA    1 
ATOM   11342 C C     . GLY C  1 465 ? -20.325 67.062  151.334 1.00 60.33  ? 465 GLY C C     1 
ATOM   11343 O O     . GLY C  1 465 ? -19.883 67.236  152.470 1.00 55.79  ? 465 GLY C O     1 
ATOM   11344 N N     . GLY C  1 466 ? -20.443 65.858  150.780 1.00 60.64  ? 466 GLY C N     1 
ATOM   11345 C CA    . GLY C  1 466 ? -20.043 64.649  151.482 1.00 55.96  ? 466 GLY C CA    1 
ATOM   11346 C C     . GLY C  1 466 ? -20.014 63.412  150.598 1.00 57.00  ? 466 GLY C C     1 
ATOM   11347 O O     . GLY C  1 466 ? -20.671 63.365  149.557 1.00 60.38  ? 466 GLY C O     1 
ATOM   11348 N N     . ILE C  1 467 ? -19.251 62.406  151.020 1.00 51.70  ? 467 ILE C N     1 
ATOM   11349 C CA    . ILE C  1 467 ? -19.133 61.150  150.284 1.00 52.21  ? 467 ILE C CA    1 
ATOM   11350 C C     . ILE C  1 467 ? -20.091 60.084  150.815 1.00 54.91  ? 467 ILE C C     1 
ATOM   11351 O O     . ILE C  1 467 ? -20.285 59.963  152.025 1.00 54.94  ? 467 ILE C O     1 
ATOM   11352 C CB    . ILE C  1 467 ? -17.687 60.590  150.352 1.00 55.98  ? 467 ILE C CB    1 
ATOM   11353 C CG1   . ILE C  1 467 ? -16.687 61.576  149.753 1.00 58.85  ? 467 ILE C CG1   1 
ATOM   11354 C CG2   . ILE C  1 467 ? -17.579 59.271  149.606 1.00 56.34  ? 467 ILE C CG2   1 
ATOM   11355 C CD1   . ILE C  1 467 ? -16.626 61.542  148.242 1.00 63.19  ? 467 ILE C CD1   1 
ATOM   11356 N N     . ASP C  1 468 ? -20.695 59.325  149.903 1.00 58.86  ? 468 ASP C N     1 
ATOM   11357 C CA    . ASP C  1 468 ? -21.405 58.100  150.258 1.00 56.69  ? 468 ASP C CA    1 
ATOM   11358 C C     . ASP C  1 468 ? -20.455 56.922  150.065 1.00 51.30  ? 468 ASP C C     1 
ATOM   11359 O O     . ASP C  1 468 ? -20.231 56.479  148.939 1.00 50.41  ? 468 ASP C O     1 
ATOM   11360 C CB    . ASP C  1 468 ? -22.668 57.919  149.405 1.00 55.64  ? 468 ASP C CB    1 
ATOM   11361 C CG    . ASP C  1 468 ? -23.543 56.758  149.878 1.00 61.91  ? 468 ASP C CG    1 
ATOM   11362 O OD1   . ASP C  1 468 ? -23.068 55.914  150.667 1.00 53.22  ? 468 ASP C OD1   1 
ATOM   11363 O OD2   . ASP C  1 468 ? -24.717 56.684  149.453 1.00 71.67  ? 468 ASP C OD2   1 
ATOM   11364 N N     . TRP C  1 469 ? -19.903 56.418  151.165 1.00 49.05  ? 469 TRP C N     1 
ATOM   11365 C CA    . TRP C  1 469 ? -18.913 55.344  151.103 1.00 51.58  ? 469 TRP C CA    1 
ATOM   11366 C C     . TRP C  1 469 ? -19.542 53.994  150.769 1.00 56.97  ? 469 TRP C C     1 
ATOM   11367 O O     . TRP C  1 469 ? -18.837 53.043  150.425 1.00 59.98  ? 469 TRP C O     1 
ATOM   11368 C CB    . TRP C  1 469 ? -18.145 55.248  152.423 1.00 47.55  ? 469 TRP C CB    1 
ATOM   11369 C CG    . TRP C  1 469 ? -17.233 56.416  152.672 1.00 48.58  ? 469 TRP C CG    1 
ATOM   11370 C CD1   . TRP C  1 469 ? -17.388 57.395  153.611 1.00 42.57  ? 469 TRP C CD1   1 
ATOM   11371 C CD2   . TRP C  1 469 ? -16.030 56.730  151.959 1.00 42.79  ? 469 TRP C CD2   1 
ATOM   11372 N NE1   . TRP C  1 469 ? -16.351 58.295  153.531 1.00 49.26  ? 469 TRP C NE1   1 
ATOM   11373 C CE2   . TRP C  1 469 ? -15.506 57.910  152.524 1.00 41.90  ? 469 TRP C CE2   1 
ATOM   11374 C CE3   . TRP C  1 469 ? -15.345 56.127  150.900 1.00 43.13  ? 469 TRP C CE3   1 
ATOM   11375 C CZ2   . TRP C  1 469 ? -14.331 58.499  152.065 1.00 40.27  ? 469 TRP C CZ2   1 
ATOM   11376 C CZ3   . TRP C  1 469 ? -14.176 56.713  150.446 1.00 45.37  ? 469 TRP C CZ3   1 
ATOM   11377 C CH2   . TRP C  1 469 ? -13.681 57.888  151.029 1.00 40.63  ? 469 TRP C CH2   1 
ATOM   11378 N N     . GLY C  1 470 ? -20.865 53.915  150.872 1.00 53.78  ? 470 GLY C N     1 
ATOM   11379 C CA    . GLY C  1 470 ? -21.592 52.699  150.545 1.00 64.74  ? 470 GLY C CA    1 
ATOM   11380 C C     . GLY C  1 470 ? -22.018 52.630  149.090 1.00 69.44  ? 470 GLY C C     1 
ATOM   11381 O O     . GLY C  1 470 ? -22.452 51.584  148.606 1.00 74.85  ? 470 GLY C O     1 
ATOM   11382 N N     . ASN C  1 471 ? -21.904 53.758  148.395 1.00 67.68  ? 471 ASN C N     1 
ATOM   11383 C CA    . ASN C  1 471 ? -22.187 53.820  146.965 1.00 70.00  ? 471 ASN C CA    1 
ATOM   11384 C C     . ASN C  1 471 ? -20.884 53.714  146.180 1.00 70.33  ? 471 ASN C C     1 
ATOM   11385 O O     . ASN C  1 471 ? -20.072 54.638  146.186 1.00 74.77  ? 471 ASN C O     1 
ATOM   11386 C CB    . ASN C  1 471 ? -22.930 55.114  146.618 1.00 74.90  ? 471 ASN C CB    1 
ATOM   11387 C CG    . ASN C  1 471 ? -23.399 55.152  145.175 1.00 81.66  ? 471 ASN C CG    1 
ATOM   11388 O OD1   . ASN C  1 471 ? -23.281 54.168  144.445 1.00 85.58  ? 471 ASN C OD1   1 
ATOM   11389 N ND2   . ASN C  1 471 ? -23.949 56.289  144.761 1.00 84.54  ? 471 ASN C ND2   1 
ATOM   11390 N N     . LYS C  1 472 ? -20.690 52.585  145.504 1.00 71.81  ? 472 LYS C N     1 
ATOM   11391 C CA    . LYS C  1 472 ? -19.398 52.261  144.906 1.00 73.77  ? 472 LYS C CA    1 
ATOM   11392 C C     . LYS C  1 472 ? -18.990 53.175  143.746 1.00 78.41  ? 472 LYS C C     1 
ATOM   11393 O O     . LYS C  1 472 ? -17.798 53.376  143.509 1.00 76.51  ? 472 LYS C O     1 
ATOM   11394 C CB    . LYS C  1 472 ? -19.387 50.809  144.427 1.00 79.63  ? 472 LYS C CB    1 
ATOM   11395 C CG    . LYS C  1 472 ? -17.999 50.322  144.048 1.00 86.25  ? 472 LYS C CG    1 
ATOM   11396 C CD    . LYS C  1 472 ? -18.049 49.060  143.212 1.00 96.81  ? 472 LYS C CD    1 
ATOM   11397 C CE    . LYS C  1 472 ? -17.281 49.230  141.910 1.00 98.43  ? 472 LYS C CE    1 
ATOM   11398 N NZ    . LYS C  1 472 ? -18.199 49.169  140.740 1.00 97.44  ? 472 LYS C NZ    1 
ATOM   11399 N N     . THR C  1 473 ? -19.959 53.725  143.020 1.00 74.96  ? 473 THR C N     1 
ATOM   11400 C CA    . THR C  1 473 ? -19.624 54.618  141.915 1.00 77.57  ? 473 THR C CA    1 
ATOM   11401 C C     . THR C  1 473 ? -18.877 55.856  142.416 1.00 74.90  ? 473 THR C C     1 
ATOM   11402 O O     . THR C  1 473 ? -17.945 56.331  141.767 1.00 73.29  ? 473 THR C O     1 
ATOM   11403 C CB    . THR C  1 473 ? -20.871 55.064  141.117 1.00 80.69  ? 473 THR C CB    1 
ATOM   11404 O OG1   . THR C  1 473 ? -20.474 56.003  140.110 1.00 85.26  ? 473 THR C OG1   1 
ATOM   11405 C CG2   . THR C  1 473 ? -21.902 55.716  142.015 1.00 81.08  ? 473 THR C CG2   1 
ATOM   11406 N N     . VAL C  1 474 ? -19.281 56.358  143.579 1.00 74.09  ? 474 VAL C N     1 
ATOM   11407 C CA    . VAL C  1 474 ? -18.641 57.514  144.193 1.00 68.86  ? 474 VAL C CA    1 
ATOM   11408 C C     . VAL C  1 474 ? -17.233 57.164  144.658 1.00 65.88  ? 474 VAL C C     1 
ATOM   11409 O O     . VAL C  1 474 ? -16.274 57.870  144.351 1.00 67.08  ? 474 VAL C O     1 
ATOM   11410 C CB    . VAL C  1 474 ? -19.455 58.036  145.397 1.00 68.24  ? 474 VAL C CB    1 
ATOM   11411 C CG1   . VAL C  1 474 ? -18.706 59.154  146.097 1.00 65.52  ? 474 VAL C CG1   1 
ATOM   11412 C CG2   . VAL C  1 474 ? -20.840 58.498  144.957 1.00 72.93  ? 474 VAL C CG2   1 
ATOM   11413 N N     . VAL C  1 475 ? -17.131 56.057  145.390 1.00 62.17  ? 475 VAL C N     1 
ATOM   11414 C CA    . VAL C  1 475 ? -15.884 55.599  146.002 1.00 61.03  ? 475 VAL C CA    1 
ATOM   11415 C C     . VAL C  1 475 ? -14.724 55.491  145.007 1.00 63.49  ? 475 VAL C C     1 
ATOM   11416 O O     . VAL C  1 475 ? -13.583 55.828  145.335 1.00 66.86  ? 475 VAL C O     1 
ATOM   11417 C CB    . VAL C  1 475 ? -16.090 54.229  146.687 1.00 62.42  ? 475 VAL C CB    1 
ATOM   11418 C CG1   . VAL C  1 475 ? -14.764 53.629  147.138 1.00 55.41  ? 475 VAL C CG1   1 
ATOM   11419 C CG2   . VAL C  1 475 ? -17.050 54.369  147.863 1.00 61.36  ? 475 VAL C CG2   1 
ATOM   11420 N N     . ASN C  1 476 ? -15.018 55.031  143.794 1.00 64.64  ? 476 ASN C N     1 
ATOM   11421 C CA    . ASN C  1 476 ? -13.996 54.900  142.759 1.00 69.97  ? 476 ASN C CA    1 
ATOM   11422 C C     . ASN C  1 476 ? -13.459 56.254  142.298 1.00 68.76  ? 476 ASN C C     1 
ATOM   11423 O O     . ASN C  1 476 ? -12.340 56.345  141.798 1.00 71.68  ? 476 ASN C O     1 
ATOM   11424 C CB    . ASN C  1 476 ? -14.546 54.123  141.554 1.00 73.38  ? 476 ASN C CB    1 
ATOM   11425 C CG    . ASN C  1 476 ? -14.924 52.692  141.897 1.00 81.68  ? 476 ASN C CG    1 
ATOM   11426 O OD1   . ASN C  1 476 ? -14.066 51.812  141.977 1.00 84.74  ? 476 ASN C OD1   1 
ATOM   11427 N ND2   . ASN C  1 476 ? -16.218 52.451  142.082 1.00 78.95  ? 476 ASN C ND2   1 
ATOM   11428 N N     . ASN C  1 477 ? -14.267 57.297  142.457 1.00 68.07  ? 477 ASN C N     1 
ATOM   11429 C CA    . ASN C  1 477 ? -13.876 58.651  142.073 1.00 68.14  ? 477 ASN C CA    1 
ATOM   11430 C C     . ASN C  1 477 ? -13.824 59.554  143.302 1.00 63.37  ? 477 ASN C C     1 
ATOM   11431 O O     . ASN C  1 477 ? -14.063 60.761  143.218 1.00 63.14  ? 477 ASN C O     1 
ATOM   11432 C CB    . ASN C  1 477 ? -14.848 59.213  141.032 1.00 67.39  ? 477 ASN C CB    1 
ATOM   11433 C CG    . ASN C  1 477 ? -14.274 60.391  140.264 1.00 70.33  ? 477 ASN C CG    1 
ATOM   11434 O OD1   . ASN C  1 477 ? -13.077 60.445  139.984 1.00 68.68  ? 477 ASN C OD1   1 
ATOM   11435 N ND2   . ASN C  1 477 ? -15.134 61.344  139.918 1.00 75.09  ? 477 ASN C ND2   1 
ATOM   11436 N N     . ALA C  1 478 ? -13.504 58.950  144.442 1.00 60.17  ? 478 ALA C N     1 
ATOM   11437 C CA    . ALA C  1 478 ? -13.574 59.621  145.735 1.00 60.17  ? 478 ALA C CA    1 
ATOM   11438 C C     . ALA C  1 478 ? -12.607 60.793  145.846 1.00 54.62  ? 478 ALA C C     1 
ATOM   11439 O O     . ALA C  1 478 ? -12.919 61.794  146.485 1.00 52.17  ? 478 ALA C O     1 
ATOM   11440 C CB    . ALA C  1 478 ? -13.313 58.623  146.854 1.00 55.92  ? 478 ALA C CB    1 
ATOM   11441 N N     . ILE C  1 479 ? -11.438 60.666  145.226 1.00 49.74  ? 479 ILE C N     1 
ATOM   11442 C CA    . ILE C  1 479 ? -10.421 61.711  145.292 1.00 53.24  ? 479 ILE C CA    1 
ATOM   11443 C C     . ILE C  1 479 ? -10.912 63.017  144.674 1.00 58.44  ? 479 ILE C C     1 
ATOM   11444 O O     . ILE C  1 479 ? -10.790 64.083  145.277 1.00 54.75  ? 479 ILE C O     1 
ATOM   11445 C CB    . ILE C  1 479 ? -9.117  61.280  144.588 1.00 48.67  ? 479 ILE C CB    1 
ATOM   11446 C CG1   . ILE C  1 479 ? -8.460  60.122  145.340 1.00 42.48  ? 479 ILE C CG1   1 
ATOM   11447 C CG2   . ILE C  1 479 ? -8.151  62.452  144.484 1.00 51.11  ? 479 ILE C CG2   1 
ATOM   11448 C CD1   . ILE C  1 479 ? -7.131  59.691  144.751 1.00 46.30  ? 479 ILE C CD1   1 
ATOM   11449 N N     . GLU C  1 480 ? -11.477 62.925  143.474 1.00 59.30  ? 480 GLU C N     1 
ATOM   11450 C CA    . GLU C  1 480 ? -11.966 64.107  142.769 1.00 58.29  ? 480 GLU C CA    1 
ATOM   11451 C C     . GLU C  1 480 ? -13.247 64.664  143.382 1.00 57.96  ? 480 GLU C C     1 
ATOM   11452 O O     . GLU C  1 480 ? -13.460 65.877  143.375 1.00 60.02  ? 480 GLU C O     1 
ATOM   11453 C CB    . GLU C  1 480 ? -12.191 63.790  141.288 1.00 60.44  ? 480 GLU C CB    1 
ATOM   11454 C CG    . GLU C  1 480 ? -10.908 63.537  140.519 1.00 60.82  ? 480 GLU C CG    1 
ATOM   11455 C CD    . GLU C  1 480 ? -9.932  64.692  140.628 1.00 65.81  ? 480 GLU C CD    1 
ATOM   11456 O OE1   . GLU C  1 480 ? -10.385 65.857  140.632 1.00 62.51  ? 480 GLU C OE1   1 
ATOM   11457 O OE2   . GLU C  1 480 ? -8.713  64.439  140.724 1.00 68.36  ? 480 GLU C OE2   1 
ATOM   11458 N N     . ILE C  1 481 ? -14.100 63.788  143.907 1.00 55.44  ? 481 ILE C N     1 
ATOM   11459 C CA    . ILE C  1 481 ? -15.340 64.240  144.533 1.00 55.01  ? 481 ILE C CA    1 
ATOM   11460 C C     . ILE C  1 481 ? -15.052 64.905  145.884 1.00 55.91  ? 481 ILE C C     1 
ATOM   11461 O O     . ILE C  1 481 ? -15.676 65.907  146.232 1.00 57.70  ? 481 ILE C O     1 
ATOM   11462 C CB    . ILE C  1 481 ? -16.350 63.084  144.723 1.00 57.08  ? 481 ILE C CB    1 
ATOM   11463 C CG1   . ILE C  1 481 ? -16.721 62.466  143.371 1.00 60.93  ? 481 ILE C CG1   1 
ATOM   11464 C CG2   . ILE C  1 481 ? -17.613 63.580  145.413 1.00 57.13  ? 481 ILE C CG2   1 
ATOM   11465 C CD1   . ILE C  1 481 ? -17.769 61.378  143.456 1.00 61.72  ? 481 ILE C CD1   1 
ATOM   11466 N N     . SER C  1 482 ? -14.089 64.366  146.629 1.00 55.90  ? 482 SER C N     1 
ATOM   11467 C CA    . SER C  1 482 ? -13.737 64.922  147.937 1.00 55.17  ? 482 SER C CA    1 
ATOM   11468 C C     . SER C  1 482 ? -12.902 66.197  147.828 1.00 50.74  ? 482 SER C C     1 
ATOM   11469 O O     . SER C  1 482 ? -12.660 66.870  148.830 1.00 51.56  ? 482 SER C O     1 
ATOM   11470 C CB    . SER C  1 482 ? -12.981 63.891  148.781 1.00 48.93  ? 482 SER C CB    1 
ATOM   11471 O OG    . SER C  1 482 ? -13.777 62.751  149.049 1.00 49.99  ? 482 SER C OG    1 
ATOM   11472 N N     . ARG C  1 483 ? -12.469 66.524  146.614 1.00 52.46  ? 483 ARG C N     1 
ATOM   11473 C CA    . ARG C  1 483 ? -11.580 67.662  146.386 1.00 51.93  ? 483 ARG C CA    1 
ATOM   11474 C C     . ARG C  1 483 ? -12.216 68.991  146.790 1.00 53.51  ? 483 ARG C C     1 
ATOM   11475 O O     . ARG C  1 483 ? -11.518 69.939  147.155 1.00 53.90  ? 483 ARG C O     1 
ATOM   11476 C CB    . ARG C  1 483 ? -11.153 67.713  144.915 1.00 51.79  ? 483 ARG C CB    1 
ATOM   11477 C CG    . ARG C  1 483 ? -10.097 68.762  144.618 1.00 56.26  ? 483 ARG C CG    1 
ATOM   11478 C CD    . ARG C  1 483 ? -9.616  68.716  143.177 1.00 56.52  ? 483 ARG C CD    1 
ATOM   11479 N NE    . ARG C  1 483 ? -8.919  67.474  142.861 1.00 55.98  ? 483 ARG C NE    1 
ATOM   11480 C CZ    . ARG C  1 483 ? -7.660  67.213  143.200 1.00 59.48  ? 483 ARG C CZ    1 
ATOM   11481 N NH1   . ARG C  1 483 ? -6.954  68.106  143.880 1.00 57.24  ? 483 ARG C NH1   1 
ATOM   11482 N NH2   . ARG C  1 483 ? -7.107  66.055  142.865 1.00 55.00  ? 483 ARG C NH2   1 
ATOM   11483 N N     . SER C  1 484 ? -13.542 69.047  146.726 1.00 54.57  ? 484 SER C N     1 
ATOM   11484 C CA    . SER C  1 484 ? -14.296 70.253  147.056 1.00 53.90  ? 484 SER C CA    1 
ATOM   11485 C C     . SER C  1 484 ? -14.006 70.751  148.471 1.00 50.84  ? 484 SER C C     1 
ATOM   11486 O O     . SER C  1 484 ? -13.494 71.855  148.654 1.00 52.36  ? 484 SER C O     1 
ATOM   11487 C CB    . SER C  1 484 ? -15.794 69.992  146.898 1.00 50.59  ? 484 SER C CB    1 
ATOM   11488 O OG    . SER C  1 484 ? -16.047 69.211  145.743 1.00 62.87  ? 484 SER C OG    1 
ATOM   11489 N N     . TRP C  1 485 ? -14.338 69.935  149.466 1.00 50.74  ? 485 TRP C N     1 
ATOM   11490 C CA    . TRP C  1 485 ? -14.109 70.302  150.859 1.00 52.25  ? 485 TRP C CA    1 
ATOM   11491 C C     . TRP C  1 485 ? -12.662 70.047  151.272 1.00 49.96  ? 485 TRP C C     1 
ATOM   11492 O O     . TRP C  1 485 ? -12.151 70.682  152.196 1.00 46.31  ? 485 TRP C O     1 
ATOM   11493 C CB    . TRP C  1 485 ? -15.065 69.539  151.781 1.00 51.61  ? 485 TRP C CB    1 
ATOM   11494 C CG    . TRP C  1 485 ? -15.098 68.055  151.553 1.00 55.26  ? 485 TRP C CG    1 
ATOM   11495 C CD1   . TRP C  1 485 ? -14.278 67.118  152.113 1.00 52.41  ? 485 TRP C CD1   1 
ATOM   11496 C CD2   . TRP C  1 485 ? -16.012 67.337  150.715 1.00 54.53  ? 485 TRP C CD2   1 
ATOM   11497 N NE1   . TRP C  1 485 ? -14.622 65.862  151.671 1.00 50.36  ? 485 TRP C NE1   1 
ATOM   11498 C CE2   . TRP C  1 485 ? -15.684 65.970  150.811 1.00 52.98  ? 485 TRP C CE2   1 
ATOM   11499 C CE3   . TRP C  1 485 ? -17.074 67.718  149.888 1.00 52.64  ? 485 TRP C CE3   1 
ATOM   11500 C CZ2   . TRP C  1 485 ? -16.379 64.985  150.116 1.00 51.00  ? 485 TRP C CZ2   1 
ATOM   11501 C CZ3   . TRP C  1 485 ? -17.762 66.738  149.195 1.00 56.76  ? 485 TRP C CZ3   1 
ATOM   11502 C CH2   . TRP C  1 485 ? -17.411 65.387  149.313 1.00 54.64  ? 485 TRP C CH2   1 
ATOM   11503 N N     . GLY C  1 486 ? -12.009 69.116  150.584 1.00 50.15  ? 486 GLY C N     1 
ATOM   11504 C CA    . GLY C  1 486 ? -10.617 68.804  150.848 1.00 48.45  ? 486 GLY C CA    1 
ATOM   11505 C C     . GLY C  1 486 ? -9.705  69.991  150.607 1.00 49.24  ? 486 GLY C C     1 
ATOM   11506 O O     . GLY C  1 486 ? -8.898  70.344  151.466 1.00 49.99  ? 486 GLY C O     1 
ATOM   11507 N N     . GLU C  1 487 ? -9.834  70.614  149.440 1.00 50.49  ? 487 GLU C N     1 
ATOM   11508 C CA    . GLU C  1 487 ? -9.029  71.786  149.111 1.00 52.56  ? 487 GLU C CA    1 
ATOM   11509 C C     . GLU C  1 487 ? -9.526  73.028  149.845 1.00 49.86  ? 487 GLU C C     1 
ATOM   11510 O O     . GLU C  1 487 ? -8.808  74.017  149.971 1.00 50.38  ? 487 GLU C O     1 
ATOM   11511 C CB    . GLU C  1 487 ? -9.027  72.031  147.601 1.00 50.90  ? 487 GLU C CB    1 
ATOM   11512 C CG    . GLU C  1 487 ? -8.288  70.963  146.815 1.00 55.51  ? 487 GLU C CG    1 
ATOM   11513 C CD    . GLU C  1 487 ? -8.093  71.334  145.359 1.00 59.67  ? 487 GLU C CD    1 
ATOM   11514 O OE1   . GLU C  1 487 ? -8.817  72.224  144.867 1.00 65.13  ? 487 GLU C OE1   1 
ATOM   11515 O OE2   . GLU C  1 487 ? -7.217  70.729  144.705 1.00 58.89  ? 487 GLU C OE2   1 
ATOM   11516 N N     . SER C  1 488 ? -10.760 72.976  150.329 1.00 46.73  ? 488 SER C N     1 
ATOM   11517 C CA    . SER C  1 488 ? -11.284 74.065  151.137 1.00 51.46  ? 488 SER C CA    1 
ATOM   11518 C C     . SER C  1 488 ? -10.643 74.038  152.521 1.00 50.81  ? 488 SER C C     1 
ATOM   11519 O O     . SER C  1 488 ? -10.309 75.078  153.089 1.00 51.91  ? 488 SER C O     1 
ATOM   11520 C CB    . SER C  1 488 ? -12.804 73.970  151.245 1.00 51.72  ? 488 SER C CB    1 
ATOM   11521 O OG    . SER C  1 488 ? -13.325 75.064  151.977 1.00 59.76  ? 488 SER C OG    1 
ATOM   11522 N N     . TYR C  1 489 ? -10.471 72.833  153.054 1.00 50.15  ? 489 TYR C N     1 
ATOM   11523 C CA    . TYR C  1 489 ? -9.874  72.644  154.370 1.00 44.04  ? 489 TYR C CA    1 
ATOM   11524 C C     . TYR C  1 489 ? -8.353  72.704  154.347 1.00 43.29  ? 489 TYR C C     1 
ATOM   11525 O O     . TYR C  1 489 ? -7.736  73.252  155.258 1.00 39.64  ? 489 TYR C O     1 
ATOM   11526 C CB    . TYR C  1 489 ? -10.284 71.297  154.960 1.00 40.63  ? 489 TYR C CB    1 
ATOM   11527 C CG    . TYR C  1 489 ? -11.744 71.163  155.311 1.00 47.15  ? 489 TYR C CG    1 
ATOM   11528 C CD1   . TYR C  1 489 ? -12.474 72.245  155.785 1.00 46.02  ? 489 TYR C CD1   1 
ATOM   11529 C CD2   . TYR C  1 489 ? -12.390 69.943  155.178 1.00 42.55  ? 489 TYR C CD2   1 
ATOM   11530 C CE1   . TYR C  1 489 ? -13.813 72.111  156.112 1.00 43.82  ? 489 TYR C CE1   1 
ATOM   11531 C CE2   . TYR C  1 489 ? -13.719 69.800  155.498 1.00 44.00  ? 489 TYR C CE2   1 
ATOM   11532 C CZ    . TYR C  1 489 ? -14.430 70.884  155.965 1.00 45.25  ? 489 TYR C CZ    1 
ATOM   11533 O OH    . TYR C  1 489 ? -15.760 70.733  156.283 1.00 43.37  ? 489 TYR C OH    1 
ATOM   11534 N N     . PHE C  1 490 ? -7.755  72.120  153.314 1.00 43.34  ? 490 PHE C N     1 
ATOM   11535 C CA    . PHE C  1 490 ? -6.326  71.845  153.334 1.00 41.37  ? 490 PHE C CA    1 
ATOM   11536 C C     . PHE C  1 490 ? -5.578  72.423  152.141 1.00 45.39  ? 490 PHE C C     1 
ATOM   11537 O O     . PHE C  1 490 ? -4.348  72.370  152.098 1.00 41.77  ? 490 PHE C O     1 
ATOM   11538 C CB    . PHE C  1 490 ? -6.097  70.332  153.403 1.00 39.65  ? 490 PHE C CB    1 
ATOM   11539 C CG    . PHE C  1 490 ? -6.897  69.650  154.474 1.00 34.93  ? 490 PHE C CG    1 
ATOM   11540 C CD1   . PHE C  1 490 ? -6.646  69.910  155.809 1.00 38.72  ? 490 PHE C CD1   1 
ATOM   11541 C CD2   . PHE C  1 490 ? -7.896  68.746  154.145 1.00 33.86  ? 490 PHE C CD2   1 
ATOM   11542 C CE1   . PHE C  1 490 ? -7.377  69.287  156.801 1.00 33.61  ? 490 PHE C CE1   1 
ATOM   11543 C CE2   . PHE C  1 490 ? -8.631  68.116  155.133 1.00 34.14  ? 490 PHE C CE2   1 
ATOM   11544 C CZ    . PHE C  1 490 ? -8.370  68.389  156.461 1.00 35.65  ? 490 PHE C CZ    1 
ATOM   11545 N N     . LEU C  1 491 ? -6.325  72.980  151.189 1.00 43.45  ? 491 LEU C N     1 
ATOM   11546 C CA    . LEU C  1 491 ? -5.753  73.488  149.940 1.00 45.45  ? 491 LEU C CA    1 
ATOM   11547 C C     . LEU C  1 491 ? -4.864  72.439  149.276 1.00 46.19  ? 491 LEU C C     1 
ATOM   11548 O O     . LEU C  1 491 ? -5.302  71.312  149.037 1.00 49.21  ? 491 LEU C O     1 
ATOM   11549 C CB    . LEU C  1 491 ? -4.976  74.789  150.193 1.00 47.96  ? 491 LEU C CB    1 
ATOM   11550 C CG    . LEU C  1 491 ? -5.889  75.995  150.399 1.00 47.46  ? 491 LEU C CG    1 
ATOM   11551 C CD1   . LEU C  1 491 ? -5.151  77.196  150.973 1.00 47.56  ? 491 LEU C CD1   1 
ATOM   11552 C CD2   . LEU C  1 491 ? -6.559  76.362  149.084 1.00 45.86  ? 491 LEU C CD2   1 
ATOM   11553 N N     . SER C  1 492 ? -3.615  72.800  149.001 1.00 47.51  ? 492 SER C N     1 
ATOM   11554 C CA    . SER C  1 492 ? -2.690  71.902  148.318 1.00 45.68  ? 492 SER C CA    1 
ATOM   11555 C C     . SER C  1 492 ? -2.098  70.816  149.224 1.00 43.38  ? 492 SER C C     1 
ATOM   11556 O O     . SER C  1 492 ? -1.359  69.946  148.755 1.00 52.96  ? 492 SER C O     1 
ATOM   11557 C CB    . SER C  1 492 ? -1.567  72.720  147.674 1.00 52.80  ? 492 SER C CB    1 
ATOM   11558 O OG    . SER C  1 492 ? -1.221  73.836  148.472 1.00 57.50  ? 492 SER C OG    1 
ATOM   11559 N N     . ASN C  1 493 ? -2.419  70.862  150.514 1.00 43.16  ? 493 ASN C N     1 
ATOM   11560 C CA    . ASN C  1 493 ? -2.002  69.807  151.437 1.00 41.50  ? 493 ASN C CA    1 
ATOM   11561 C C     . ASN C  1 493 ? -2.870  68.557  151.288 1.00 48.39  ? 493 ASN C C     1 
ATOM   11562 O O     . ASN C  1 493 ? -2.575  67.505  151.860 1.00 46.19  ? 493 ASN C O     1 
ATOM   11563 C CB    . ASN C  1 493 ? -2.044  70.307  152.890 1.00 40.45  ? 493 ASN C CB    1 
ATOM   11564 C CG    . ASN C  1 493 ? -1.022  71.400  153.170 1.00 40.02  ? 493 ASN C CG    1 
ATOM   11565 O OD1   . ASN C  1 493 ? 0.024   71.474  152.526 1.00 43.66  ? 493 ASN C OD1   1 
ATOM   11566 N ND2   . ASN C  1 493 ? -1.319  72.245  154.148 1.00 34.25  ? 493 ASN C ND2   1 
ATOM   11567 N N     . TYR C  1 494 ? -3.944  68.693  150.517 1.00 44.69  ? 494 TYR C N     1 
ATOM   11568 C CA    . TYR C  1 494 ? -4.907  67.622  150.278 1.00 47.69  ? 494 TYR C CA    1 
ATOM   11569 C C     . TYR C  1 494 ? -4.270  66.393  149.639 1.00 47.08  ? 494 TYR C C     1 
ATOM   11570 O O     . TYR C  1 494 ? -4.608  65.258  149.974 1.00 46.81  ? 494 TYR C O     1 
ATOM   11571 C CB    . TYR C  1 494 ? -6.040  68.155  149.395 1.00 45.11  ? 494 TYR C CB    1 
ATOM   11572 C CG    . TYR C  1 494 ? -7.069  67.129  148.986 1.00 48.26  ? 494 TYR C CG    1 
ATOM   11573 C CD1   . TYR C  1 494 ? -7.891  66.528  149.931 1.00 52.09  ? 494 TYR C CD1   1 
ATOM   11574 C CD2   . TYR C  1 494 ? -7.238  66.777  147.652 1.00 52.51  ? 494 TYR C CD2   1 
ATOM   11575 C CE1   . TYR C  1 494 ? -8.844  65.590  149.559 1.00 45.59  ? 494 TYR C CE1   1 
ATOM   11576 C CE2   . TYR C  1 494 ? -8.189  65.842  147.271 1.00 51.59  ? 494 TYR C CE2   1 
ATOM   11577 C CZ    . TYR C  1 494 ? -8.988  65.252  148.230 1.00 46.22  ? 494 TYR C CZ    1 
ATOM   11578 O OH    . TYR C  1 494 ? -9.934  64.323  147.859 1.00 53.67  ? 494 TYR C OH    1 
ATOM   11579 N N     . GLU C  1 495 ? -3.344  66.634  148.717 1.00 43.71  ? 495 GLU C N     1 
ATOM   11580 C CA    . GLU C  1 495 ? -2.674  65.567  147.984 1.00 46.06  ? 495 GLU C CA    1 
ATOM   11581 C C     . GLU C  1 495 ? -1.772  64.714  148.878 1.00 48.37  ? 495 GLU C C     1 
ATOM   11582 O O     . GLU C  1 495 ? -1.765  63.486  148.766 1.00 46.41  ? 495 GLU C O     1 
ATOM   11583 C CB    . GLU C  1 495 ? -1.856  66.155  146.825 1.00 45.50  ? 495 GLU C CB    1 
ATOM   11584 C CG    . GLU C  1 495 ? -2.687  66.813  145.726 1.00 51.32  ? 495 GLU C CG    1 
ATOM   11585 C CD    . GLU C  1 495 ? -3.456  65.810  144.884 1.00 52.98  ? 495 GLU C CD    1 
ATOM   11586 O OE1   . GLU C  1 495 ? -3.223  64.599  145.047 1.00 49.34  ? 495 GLU C OE1   1 
ATOM   11587 O OE2   . GLU C  1 495 ? -4.290  66.237  144.057 1.00 61.14  ? 495 GLU C OE2   1 
ATOM   11588 N N     . ARG C  1 496 ? -1.015  65.361  149.760 1.00 40.40  ? 496 ARG C N     1 
ATOM   11589 C CA    . ARG C  1 496 ? -0.133  64.635  150.672 1.00 44.45  ? 496 ARG C CA    1 
ATOM   11590 C C     . ARG C  1 496 ? -0.937  63.862  151.715 1.00 40.50  ? 496 ARG C C     1 
ATOM   11591 O O     . ARG C  1 496 ? -0.533  62.783  152.155 1.00 43.81  ? 496 ARG C O     1 
ATOM   11592 C CB    . ARG C  1 496 ? 0.842   65.590  151.366 1.00 41.49  ? 496 ARG C CB    1 
ATOM   11593 C CG    . ARG C  1 496 ? 1.888   64.874  152.212 1.00 43.68  ? 496 ARG C CG    1 
ATOM   11594 C CD    . ARG C  1 496 ? 2.881   65.833  152.846 1.00 45.41  ? 496 ARG C CD    1 
ATOM   11595 N NE    . ARG C  1 496 ? 3.844   65.125  153.685 1.00 41.60  ? 496 ARG C NE    1 
ATOM   11596 C CZ    . ARG C  1 496 ? 4.733   65.723  154.471 1.00 44.54  ? 496 ARG C CZ    1 
ATOM   11597 N NH1   . ARG C  1 496 ? 4.785   67.046  154.531 1.00 45.50  ? 496 ARG C NH1   1 
ATOM   11598 N NH2   . ARG C  1 496 ? 5.568   64.997  155.201 1.00 44.04  ? 496 ARG C NH2   1 
ATOM   11599 N N     . LEU C  1 497 ? -2.073  64.425  152.111 1.00 39.33  ? 497 LEU C N     1 
ATOM   11600 C CA    . LEU C  1 497 ? -2.979  63.755  153.034 1.00 42.27  ? 497 LEU C CA    1 
ATOM   11601 C C     . LEU C  1 497 ? -3.469  62.436  152.457 1.00 43.83  ? 497 LEU C C     1 
ATOM   11602 O O     . LEU C  1 497 ? -3.620  61.452  153.180 1.00 42.31  ? 497 LEU C O     1 
ATOM   11603 C CB    . LEU C  1 497 ? -4.169  64.650  153.363 1.00 40.77  ? 497 LEU C CB    1 
ATOM   11604 C CG    . LEU C  1 497 ? -3.881  65.853  154.258 1.00 43.60  ? 497 LEU C CG    1 
ATOM   11605 C CD1   . LEU C  1 497 ? -5.070  66.793  154.241 1.00 39.87  ? 497 LEU C CD1   1 
ATOM   11606 C CD2   . LEU C  1 497 ? -3.575  65.392  155.671 1.00 33.96  ? 497 LEU C CD2   1 
ATOM   11607 N N     . ILE C  1 498 ? -3.726  62.429  151.154 1.00 44.93  ? 498 ILE C N     1 
ATOM   11608 C CA    . ILE C  1 498 ? -4.152  61.219  150.460 1.00 42.47  ? 498 ILE C CA    1 
ATOM   11609 C C     . ILE C  1 498 ? -3.066  60.146  150.508 1.00 47.36  ? 498 ILE C C     1 
ATOM   11610 O O     . ILE C  1 498 ? -3.363  58.970  150.727 1.00 47.98  ? 498 ILE C O     1 
ATOM   11611 C CB    . ILE C  1 498 ? -4.526  61.517  148.994 1.00 42.58  ? 498 ILE C CB    1 
ATOM   11612 C CG1   . ILE C  1 498 ? -5.783  62.385  148.938 1.00 43.61  ? 498 ILE C CG1   1 
ATOM   11613 C CG2   . ILE C  1 498 ? -4.759  60.229  148.224 1.00 44.88  ? 498 ILE C CG2   1 
ATOM   11614 C CD1   . ILE C  1 498 ? -6.157  62.828  147.546 1.00 43.58  ? 498 ILE C CD1   1 
ATOM   11615 N N     . ARG C  1 499 ? -1.810  60.549  150.320 1.00 41.93  ? 499 ARG C N     1 
ATOM   11616 C CA    . ARG C  1 499 ? -0.702  59.600  150.403 1.00 46.33  ? 499 ARG C CA    1 
ATOM   11617 C C     . ARG C  1 499 ? -0.595  59.039  151.818 1.00 45.88  ? 499 ARG C C     1 
ATOM   11618 O O     . ARG C  1 499 ? -0.376  57.842  152.003 1.00 43.83  ? 499 ARG C O     1 
ATOM   11619 C CB    . ARG C  1 499 ? 0.629   60.240  149.991 1.00 41.15  ? 499 ARG C CB    1 
ATOM   11620 C CG    . ARG C  1 499 ? 1.814   59.278  150.137 1.00 45.02  ? 499 ARG C CG    1 
ATOM   11621 C CD    . ARG C  1 499 ? 3.059   59.719  149.380 1.00 44.73  ? 499 ARG C CD    1 
ATOM   11622 N NE    . ARG C  1 499 ? 3.881   60.652  150.147 1.00 48.85  ? 499 ARG C NE    1 
ATOM   11623 C CZ    . ARG C  1 499 ? 3.786   61.974  150.056 1.00 49.38  ? 499 ARG C CZ    1 
ATOM   11624 N NH1   . ARG C  1 499 ? 2.899   62.517  149.232 1.00 44.07  ? 499 ARG C NH1   1 
ATOM   11625 N NH2   . ARG C  1 499 ? 4.572   62.755  150.789 1.00 51.07  ? 499 ARG C NH2   1 
ATOM   11626 N N     . ALA C  1 500 ? -0.762  59.908  152.810 1.00 43.56  ? 500 ALA C N     1 
ATOM   11627 C CA    . ALA C  1 500 ? -0.716  59.495  154.208 1.00 41.15  ? 500 ALA C CA    1 
ATOM   11628 C C     . ALA C  1 500 ? -1.847  58.522  154.530 1.00 38.51  ? 500 ALA C C     1 
ATOM   11629 O O     . ALA C  1 500 ? -1.649  57.539  155.242 1.00 39.25  ? 500 ALA C O     1 
ATOM   11630 C CB    . ALA C  1 500 ? -0.783  60.708  155.116 1.00 36.61  ? 500 ALA C CB    1 
ATOM   11631 N N     . LYS C  1 501 ? -3.031  58.807  153.999 1.00 37.30  ? 501 LYS C N     1 
ATOM   11632 C CA    . LYS C  1 501 ? -4.187  57.934  154.165 1.00 42.71  ? 501 LYS C CA    1 
ATOM   11633 C C     . LYS C  1 501 ? -3.915  56.554  153.567 1.00 41.72  ? 501 LYS C C     1 
ATOM   11634 O O     . LYS C  1 501 ? -4.240  55.530  154.169 1.00 38.42  ? 501 LYS C O     1 
ATOM   11635 C CB    . LYS C  1 501 ? -5.421  58.561  153.516 1.00 38.27  ? 501 LYS C CB    1 
ATOM   11636 C CG    . LYS C  1 501 ? -6.654  57.674  153.522 1.00 42.83  ? 501 LYS C CG    1 
ATOM   11637 C CD    . LYS C  1 501 ? -7.280  57.585  154.904 1.00 39.16  ? 501 LYS C CD    1 
ATOM   11638 C CE    . LYS C  1 501 ? -8.562  56.776  154.858 1.00 39.17  ? 501 LYS C CE    1 
ATOM   11639 N NZ    . LYS C  1 501 ? -9.268  56.717  156.172 1.00 37.07  ? 501 LYS C NZ    1 
ATOM   11640 N N     . THR C  1 502 ? -3.309  56.542  152.384 1.00 42.48  ? 502 THR C N     1 
ATOM   11641 C CA    . THR C  1 502 ? -2.956  55.302  151.702 1.00 43.95  ? 502 THR C CA    1 
ATOM   11642 C C     . THR C  1 502 ? -1.957  54.482  152.520 1.00 41.42  ? 502 THR C C     1 
ATOM   11643 O O     . THR C  1 502 ? -2.012  53.252  152.529 1.00 43.11  ? 502 THR C O     1 
ATOM   11644 C CB    . THR C  1 502 ? -2.367  55.585  150.301 1.00 46.39  ? 502 THR C CB    1 
ATOM   11645 O OG1   . THR C  1 502 ? -3.282  56.393  149.550 1.00 46.76  ? 502 THR C OG1   1 
ATOM   11646 C CG2   . THR C  1 502 ? -2.108  54.287  149.547 1.00 47.36  ? 502 THR C CG2   1 
ATOM   11647 N N     . LEU C  1 503 ? -1.059  55.170  153.220 1.00 42.10  ? 503 LEU C N     1 
ATOM   11648 C CA    . LEU C  1 503 ? -0.032  54.509  154.022 1.00 39.85  ? 503 LEU C CA    1 
ATOM   11649 C C     . LEU C  1 503 ? -0.588  53.897  155.308 1.00 37.82  ? 503 LEU C C     1 
ATOM   11650 O O     . LEU C  1 503 ? -0.181  52.806  155.706 1.00 41.28  ? 503 LEU C O     1 
ATOM   11651 C CB    . LEU C  1 503 ? 1.090   55.497  154.367 1.00 41.33  ? 503 LEU C CB    1 
ATOM   11652 C CG    . LEU C  1 503 ? 2.023   55.933  153.234 1.00 40.90  ? 503 LEU C CG    1 
ATOM   11653 C CD1   . LEU C  1 503 ? 2.903   57.091  153.672 1.00 43.48  ? 503 LEU C CD1   1 
ATOM   11654 C CD2   . LEU C  1 503 ? 2.882   54.765  152.767 1.00 46.64  ? 503 LEU C CD2   1 
ATOM   11655 N N     . ILE C  1 504 ? -1.519  54.597  155.952 1.00 39.29  ? 504 ILE C N     1 
ATOM   11656 C CA    . ILE C  1 504 ? -1.964  54.207  157.287 1.00 32.56  ? 504 ILE C CA    1 
ATOM   11657 C C     . ILE C  1 504 ? -3.350  53.550  157.320 1.00 36.08  ? 504 ILE C C     1 
ATOM   11658 O O     . ILE C  1 504 ? -3.651  52.775  158.228 1.00 32.28  ? 504 ILE C O     1 
ATOM   11659 C CB    . ILE C  1 504 ? -1.959  55.429  158.242 1.00 31.51  ? 504 ILE C CB    1 
ATOM   11660 C CG1   . ILE C  1 504 ? -1.971  54.971  159.705 1.00 31.76  ? 504 ILE C CG1   1 
ATOM   11661 C CG2   . ILE C  1 504 ? -3.113  56.376  157.940 1.00 32.68  ? 504 ILE C CG2   1 
ATOM   11662 C CD1   . ILE C  1 504 ? -0.739  54.193  160.096 1.00 37.19  ? 504 ILE C CD1   1 
ATOM   11663 N N     . ASP C  1 505 ? -4.189  53.849  156.333 1.00 36.38  ? 505 ASP C N     1 
ATOM   11664 C CA    . ASP C  1 505 ? -5.532  53.272  156.291 1.00 38.46  ? 505 ASP C CA    1 
ATOM   11665 C C     . ASP C  1 505 ? -5.998  53.005  154.860 1.00 39.03  ? 505 ASP C C     1 
ATOM   11666 O O     . ASP C  1 505 ? -6.996  53.574  154.421 1.00 38.52  ? 505 ASP C O     1 
ATOM   11667 C CB    . ASP C  1 505 ? -6.531  54.199  157.001 1.00 33.94  ? 505 ASP C CB    1 
ATOM   11668 C CG    . ASP C  1 505 ? -7.883  53.544  157.233 1.00 40.27  ? 505 ASP C CG    1 
ATOM   11669 O OD1   . ASP C  1 505 ? -7.954  52.298  157.250 1.00 37.13  ? 505 ASP C OD1   1 
ATOM   11670 O OD2   . ASP C  1 505 ? -8.881  54.279  157.410 1.00 33.57  ? 505 ASP C OD2   1 
ATOM   11671 N N     . PRO C  1 506 ? -5.286  52.129  154.128 1.00 36.23  ? 506 PRO C N     1 
ATOM   11672 C CA    . PRO C  1 506 ? -5.659  51.866  152.731 1.00 38.67  ? 506 PRO C CA    1 
ATOM   11673 C C     . PRO C  1 506 ? -7.051  51.248  152.575 1.00 42.51  ? 506 PRO C C     1 
ATOM   11674 O O     . PRO C  1 506 ? -7.724  51.507  151.576 1.00 44.13  ? 506 PRO C O     1 
ATOM   11675 C CB    . PRO C  1 506 ? -4.578  50.888  152.257 1.00 44.00  ? 506 PRO C CB    1 
ATOM   11676 C CG    . PRO C  1 506 ? -4.069  50.248  153.503 1.00 39.84  ? 506 PRO C CG    1 
ATOM   11677 C CD    . PRO C  1 506 ? -4.129  51.318  154.547 1.00 39.78  ? 506 PRO C CD    1 
ATOM   11678 N N     . ASN C  1 507 ? -7.474  50.453  153.552 1.00 37.10  ? 507 ASN C N     1 
ATOM   11679 C CA    . ASN C  1 507 ? -8.782  49.806  153.494 1.00 41.73  ? 507 ASN C CA    1 
ATOM   11680 C C     . ASN C  1 507 ? -9.899  50.715  154.010 1.00 42.45  ? 507 ASN C C     1 
ATOM   11681 O O     . ASN C  1 507 ? -11.058 50.305  154.080 1.00 40.60  ? 507 ASN C O     1 
ATOM   11682 C CB    . ASN C  1 507 ? -8.759  48.492  154.279 1.00 45.05  ? 507 ASN C CB    1 
ATOM   11683 C CG    . ASN C  1 507 ? -7.759  47.494  153.717 1.00 47.99  ? 507 ASN C CG    1 
ATOM   11684 O OD1   . ASN C  1 507 ? -6.892  46.992  154.436 1.00 50.56  ? 507 ASN C OD1   1 
ATOM   11685 N ND2   . ASN C  1 507 ? -7.868  47.213  152.424 1.00 49.50  ? 507 ASN C ND2   1 
ATOM   11686 N N     . ASN C  1 508 ? -9.534  51.945  154.369 1.00 41.80  ? 508 ASN C N     1 
ATOM   11687 C CA    . ASN C  1 508 ? -10.493 52.985  154.738 1.00 35.00  ? 508 ASN C CA    1 
ATOM   11688 C C     . ASN C  1 508 ? -11.420 52.583  155.888 1.00 35.20  ? 508 ASN C C     1 
ATOM   11689 O O     . ASN C  1 508 ? -12.635 52.761  155.808 1.00 39.04  ? 508 ASN C O     1 
ATOM   11690 C CB    . ASN C  1 508 ? -11.324 53.380  153.512 1.00 40.44  ? 508 ASN C CB    1 
ATOM   11691 C CG    . ASN C  1 508 ? -11.936 54.761  153.635 1.00 42.80  ? 508 ASN C CG    1 
ATOM   11692 O OD1   . ASN C  1 508 ? -11.423 55.619  154.350 1.00 41.22  ? 508 ASN C OD1   1 
ATOM   11693 N ND2   . ASN C  1 508 ? -13.041 54.982  152.928 1.00 39.58  ? 508 ASN C ND2   1 
ATOM   11694 N N     . VAL C  1 509 ? -10.838 52.042  156.954 1.00 35.15  ? 509 VAL C N     1 
ATOM   11695 C CA    . VAL C  1 509 ? -11.602 51.633  158.127 1.00 31.67  ? 509 VAL C CA    1 
ATOM   11696 C C     . VAL C  1 509 ? -12.129 52.855  158.876 1.00 40.85  ? 509 VAL C C     1 
ATOM   11697 O O     . VAL C  1 509 ? -13.239 52.842  159.413 1.00 36.09  ? 509 VAL C O     1 
ATOM   11698 C CB    . VAL C  1 509 ? -10.746 50.757  159.075 1.00 33.41  ? 509 VAL C CB    1 
ATOM   11699 C CG1   . VAL C  1 509 ? -11.478 50.484  160.379 1.00 35.54  ? 509 VAL C CG1   1 
ATOM   11700 C CG2   . VAL C  1 509 ? -10.384 49.453  158.389 1.00 38.61  ? 509 VAL C CG2   1 
ATOM   11701 N N     . PHE C  1 510 ? -11.334 53.919  158.889 1.00 31.79  ? 510 PHE C N     1 
ATOM   11702 C CA    . PHE C  1 510 ? -11.729 55.153  159.555 1.00 37.43  ? 510 PHE C CA    1 
ATOM   11703 C C     . PHE C  1 510 ? -12.229 56.165  158.534 1.00 33.75  ? 510 PHE C C     1 
ATOM   11704 O O     . PHE C  1 510 ? -11.440 56.782  157.819 1.00 37.93  ? 510 PHE C O     1 
ATOM   11705 C CB    . PHE C  1 510 ? -10.561 55.723  160.359 1.00 33.42  ? 510 PHE C CB    1 
ATOM   11706 C CG    . PHE C  1 510 ? -10.055 54.788  161.414 1.00 37.22  ? 510 PHE C CG    1 
ATOM   11707 C CD1   . PHE C  1 510 ? -10.575 54.828  162.697 1.00 35.61  ? 510 PHE C CD1   1 
ATOM   11708 C CD2   . PHE C  1 510 ? -9.078  53.850  161.118 1.00 32.89  ? 510 PHE C CD2   1 
ATOM   11709 C CE1   . PHE C  1 510 ? -10.121 53.961  163.669 1.00 36.98  ? 510 PHE C CE1   1 
ATOM   11710 C CE2   . PHE C  1 510 ? -8.623  52.978  162.087 1.00 28.79  ? 510 PHE C CE2   1 
ATOM   11711 C CZ    . PHE C  1 510 ? -9.143  53.036  163.367 1.00 28.28  ? 510 PHE C CZ    1 
ATOM   11712 N N     . ASN C  1 511 ? -13.547 56.318  158.468 1.00 34.70  ? 511 ASN C N     1 
ATOM   11713 C CA    . ASN C  1 511 ? -14.167 57.178  157.473 1.00 36.12  ? 511 ASN C CA    1 
ATOM   11714 C C     . ASN C  1 511 ? -15.387 57.919  158.006 1.00 39.27  ? 511 ASN C C     1 
ATOM   11715 O O     . ASN C  1 511 ? -15.987 57.518  159.004 1.00 36.46  ? 511 ASN C O     1 
ATOM   11716 C CB    . ASN C  1 511 ? -14.573 56.355  156.252 1.00 40.05  ? 511 ASN C CB    1 
ATOM   11717 C CG    . ASN C  1 511 ? -15.572 55.267  156.594 1.00 42.57  ? 511 ASN C CG    1 
ATOM   11718 O OD1   . ASN C  1 511 ? -16.772 55.521  156.697 1.00 37.33  ? 511 ASN C OD1   1 
ATOM   11719 N ND2   . ASN C  1 511 ? -15.081 54.050  156.780 1.00 43.15  ? 511 ASN C ND2   1 
ATOM   11720 N N     . HIS C  1 512 ? -15.744 59.003  157.326 1.00 35.89  ? 512 HIS C N     1 
ATOM   11721 C CA    . HIS C  1 512 ? -16.956 59.760  157.618 1.00 32.86  ? 512 HIS C CA    1 
ATOM   11722 C C     . HIS C  1 512 ? -17.296 60.539  156.336 1.00 40.42  ? 512 HIS C C     1 
ATOM   11723 O O     . HIS C  1 512 ? -16.545 60.439  155.367 1.00 36.87  ? 512 HIS C O     1 
ATOM   11724 C CB    . HIS C  1 512 ? -16.759 60.654  158.857 1.00 36.90  ? 512 HIS C CB    1 
ATOM   11725 C CG    . HIS C  1 512 ? -15.687 61.688  158.713 1.00 37.20  ? 512 HIS C CG    1 
ATOM   11726 N ND1   . HIS C  1 512 ? -15.787 62.754  157.846 1.00 43.31  ? 512 HIS C ND1   1 
ATOM   11727 C CD2   . HIS C  1 512 ? -14.505 61.837  159.358 1.00 41.76  ? 512 HIS C CD2   1 
ATOM   11728 C CE1   . HIS C  1 512 ? -14.706 63.507  157.951 1.00 44.12  ? 512 HIS C CE1   1 
ATOM   11729 N NE2   . HIS C  1 512 ? -13.912 62.972  158.861 1.00 37.75  ? 512 HIS C NE2   1 
ATOM   11730 N N     . PRO C  1 513 ? -18.429 61.279  156.296 1.00 39.30  ? 513 PRO C N     1 
ATOM   11731 C CA    . PRO C  1 513 ? -18.797 61.908  155.015 1.00 41.24  ? 513 PRO C CA    1 
ATOM   11732 C C     . PRO C  1 513 ? -17.721 62.759  154.325 1.00 42.18  ? 513 PRO C C     1 
ATOM   11733 O O     . PRO C  1 513 ? -17.796 62.921  153.109 1.00 43.64  ? 513 PRO C O     1 
ATOM   11734 C CB    . PRO C  1 513 ? -19.982 62.795  155.401 1.00 44.44  ? 513 PRO C CB    1 
ATOM   11735 C CG    . PRO C  1 513 ? -20.634 62.063  156.497 1.00 35.78  ? 513 PRO C CG    1 
ATOM   11736 C CD    . PRO C  1 513 ? -19.522 61.409  157.282 1.00 40.72  ? 513 PRO C CD    1 
ATOM   11737 N N     . GLN C  1 514 ? -16.748 63.283  155.064 1.00 42.29  ? 514 GLN C N     1 
ATOM   11738 C CA    . GLN C  1 514 ? -15.722 64.121  154.450 1.00 46.26  ? 514 GLN C CA    1 
ATOM   11739 C C     . GLN C  1 514 ? -14.300 63.651  154.747 1.00 46.32  ? 514 GLN C C     1 
ATOM   11740 O O     . GLN C  1 514 ? -13.346 64.420  154.616 1.00 38.95  ? 514 GLN C O     1 
ATOM   11741 C CB    . GLN C  1 514 ? -15.885 65.571  154.900 1.00 43.66  ? 514 GLN C CB    1 
ATOM   11742 C CG    . GLN C  1 514 ? -17.100 66.261  154.310 1.00 47.92  ? 514 GLN C CG    1 
ATOM   11743 C CD    . GLN C  1 514 ? -17.131 67.735  154.633 1.00 48.41  ? 514 GLN C CD    1 
ATOM   11744 O OE1   . GLN C  1 514 ? -16.315 68.222  155.410 1.00 46.91  ? 514 GLN C OE1   1 
ATOM   11745 N NE2   . GLN C  1 514 ? -18.068 68.457  154.033 1.00 53.15  ? 514 GLN C NE2   1 
ATOM   11746 N N     . SER C  1 515 ? -14.154 62.388  155.134 1.00 45.16  ? 515 SER C N     1 
ATOM   11747 C CA    . SER C  1 515 ? -12.836 61.850  155.455 1.00 39.54  ? 515 SER C CA    1 
ATOM   11748 C C     . SER C  1 515 ? -11.976 61.747  154.203 1.00 39.21  ? 515 SER C C     1 
ATOM   11749 O O     . SER C  1 515 ? -12.482 61.448  153.119 1.00 45.49  ? 515 SER C O     1 
ATOM   11750 C CB    . SER C  1 515 ? -12.957 60.481  156.123 1.00 41.51  ? 515 SER C CB    1 
ATOM   11751 O OG    . SER C  1 515 ? -13.542 59.537  155.243 1.00 44.59  ? 515 SER C OG    1 
ATOM   11752 N N     . ILE C  1 516 ? -10.679 62.006  154.358 1.00 36.08  ? 516 ILE C N     1 
ATOM   11753 C CA    . ILE C  1 516 ? -9.735  61.923  153.249 1.00 37.68  ? 516 ILE C CA    1 
ATOM   11754 C C     . ILE C  1 516 ? -9.770  60.539  152.613 1.00 44.81  ? 516 ILE C C     1 
ATOM   11755 O O     . ILE C  1 516 ? -9.687  59.531  153.312 1.00 38.86  ? 516 ILE C O     1 
ATOM   11756 C CB    . ILE C  1 516 ? -8.288  62.229  153.704 1.00 37.53  ? 516 ILE C CB    1 
ATOM   11757 C CG1   . ILE C  1 516 ? -8.205  63.605  154.366 1.00 41.06  ? 516 ILE C CG1   1 
ATOM   11758 C CG2   . ILE C  1 516 ? -7.330  62.159  152.523 1.00 37.02  ? 516 ILE C CG2   1 
ATOM   11759 C CD1   . ILE C  1 516 ? -8.361  64.754  153.395 1.00 35.97  ? 516 ILE C CD1   1 
ATOM   11760 N N     . PRO C  1 517 ? -9.918  60.483  151.282 1.00 47.66  ? 517 PRO C N     1 
ATOM   11761 C CA    . PRO C  1 517 ? -9.910  59.178  150.622 1.00 45.24  ? 517 PRO C CA    1 
ATOM   11762 C C     . PRO C  1 517 ? -8.501  58.659  150.391 1.00 47.89  ? 517 PRO C C     1 
ATOM   11763 O O     . PRO C  1 517 ? -7.575  59.453  150.227 1.00 49.94  ? 517 PRO C O     1 
ATOM   11764 C CB    . PRO C  1 517 ? -10.604 59.461  149.291 1.00 49.19  ? 517 PRO C CB    1 
ATOM   11765 C CG    . PRO C  1 517 ? -10.239 60.876  149.000 1.00 49.39  ? 517 PRO C CG    1 
ATOM   11766 C CD    . PRO C  1 517 ? -10.246 61.569  150.342 1.00 45.92  ? 517 PRO C CD    1 
ATOM   11767 N N     . PRO C  1 518 ? -8.338  57.332  150.388 1.00 43.53  ? 518 PRO C N     1 
ATOM   11768 C CA    . PRO C  1 518 ? -7.085  56.727  149.945 1.00 51.73  ? 518 PRO C CA    1 
ATOM   11769 C C     . PRO C  1 518 ? -7.086  56.651  148.432 1.00 54.15  ? 518 PRO C C     1 
ATOM   11770 O O     . PRO C  1 518 ? -8.097  56.990  147.822 1.00 56.53  ? 518 PRO C O     1 
ATOM   11771 C CB    . PRO C  1 518 ? -7.138  55.335  150.562 1.00 51.08  ? 518 PRO C CB    1 
ATOM   11772 C CG    . PRO C  1 518 ? -8.600  55.007  150.536 1.00 44.27  ? 518 PRO C CG    1 
ATOM   11773 C CD    . PRO C  1 518 ? -9.317  56.314  150.810 1.00 43.32  ? 518 PRO C CD    1 
ATOM   11774 N N     . MET C  1 519 ? -5.991  56.211  147.828 1.00 53.92  ? 519 MET C N     1 
ATOM   11775 C CA    . MET C  1 519 ? -6.055  55.856  146.421 1.00 62.84  ? 519 MET C CA    1 
ATOM   11776 C C     . MET C  1 519 ? -6.887  54.579  146.323 1.00 71.52  ? 519 MET C C     1 
ATOM   11777 O O     . MET C  1 519 ? -6.953  53.800  147.280 1.00 75.60  ? 519 MET C O     1 
ATOM   11778 C CB    . MET C  1 519 ? -4.664  55.655  145.823 1.00 59.63  ? 519 MET C CB    1 
ATOM   11779 C CG    . MET C  1 519 ? -3.602  56.611  146.341 1.00 56.05  ? 519 MET C CG    1 
ATOM   11780 S SD    . MET C  1 519 ? -1.994  56.347  145.557 1.00 64.99  ? 519 MET C SD    1 
ATOM   11781 C CE    . MET C  1 519 ? -1.969  54.560  145.432 1.00 68.20  ? 519 MET C CE    1 
ATOM   11782 N N     . ALA C  1 520 ? -7.531  54.372  145.179 1.00 78.23  ? 520 ALA C N     1 
ATOM   11783 C CA    . ALA C  1 520 ? -8.418  53.225  144.995 1.00 70.85  ? 520 ALA C CA    1 
ATOM   11784 C C     . ALA C  1 520 ? -7.707  51.891  145.221 1.00 80.99  ? 520 ALA C C     1 
ATOM   11785 O O     . ALA C  1 520 ? -6.485  51.810  145.165 1.00 81.18  ? 520 ALA C O     1 
ATOM   11786 C CB    . ALA C  1 520 ? -9.034  53.262  143.609 1.00 69.29  ? 520 ALA C CB    1 
ATOM   11787 N N     . ASP D  1 26  ? -11.342 58.933  218.128 1.00 55.31  ? 26  ASP D N     1 
ATOM   11788 C CA    . ASP D  1 26  ? -10.711 59.667  219.221 1.00 52.15  ? 26  ASP D CA    1 
ATOM   11789 C C     . ASP D  1 26  ? -9.629  58.816  219.889 1.00 49.86  ? 26  ASP D C     1 
ATOM   11790 O O     . ASP D  1 26  ? -9.901  57.714  220.369 1.00 46.50  ? 26  ASP D O     1 
ATOM   11791 C CB    . ASP D  1 26  ? -11.766 60.106  220.239 1.00 47.93  ? 26  ASP D CB    1 
ATOM   11792 C CG    . ASP D  1 26  ? -11.167 60.768  221.460 1.00 49.12  ? 26  ASP D CG    1 
ATOM   11793 O OD1   . ASP D  1 26  ? -10.655 61.902  221.338 1.00 60.85  ? 26  ASP D OD1   1 
ATOM   11794 O OD2   . ASP D  1 26  ? -11.221 60.159  222.550 1.00 49.03  ? 26  ASP D OD2   1 
ATOM   11795 N N     . LEU D  1 27  ? -8.404  59.337  219.905 1.00 47.16  ? 27  LEU D N     1 
ATOM   11796 C CA    . LEU D  1 27  ? -7.245  58.607  220.415 1.00 47.65  ? 27  LEU D CA    1 
ATOM   11797 C C     . LEU D  1 27  ? -7.424  58.149  221.862 1.00 47.29  ? 27  LEU D C     1 
ATOM   11798 O O     . LEU D  1 27  ? -7.086  57.016  222.204 1.00 43.47  ? 27  LEU D O     1 
ATOM   11799 C CB    . LEU D  1 27  ? -5.982  59.467  220.305 1.00 47.48  ? 27  LEU D CB    1 
ATOM   11800 C CG    . LEU D  1 27  ? -4.682  58.769  220.718 1.00 49.56  ? 27  LEU D CG    1 
ATOM   11801 C CD1   . LEU D  1 27  ? -4.400  57.601  219.788 1.00 48.37  ? 27  LEU D CD1   1 
ATOM   11802 C CD2   . LEU D  1 27  ? -3.517  59.741  220.738 1.00 46.71  ? 27  LEU D CD2   1 
ATOM   11803 N N     . LEU D  1 28  ? -7.961  59.029  222.703 1.00 46.27  ? 28  LEU D N     1 
ATOM   11804 C CA    . LEU D  1 28  ? -8.148  58.722  224.118 1.00 46.18  ? 28  LEU D CA    1 
ATOM   11805 C C     . LEU D  1 28  ? -9.177  57.615  224.340 1.00 50.50  ? 28  LEU D C     1 
ATOM   11806 O O     . LEU D  1 28  ? -8.987  56.746  225.194 1.00 48.11  ? 28  LEU D O     1 
ATOM   11807 C CB    . LEU D  1 28  ? -8.561  59.976  224.890 1.00 48.24  ? 28  LEU D CB    1 
ATOM   11808 C CG    . LEU D  1 28  ? -7.493  61.064  225.074 1.00 54.11  ? 28  LEU D CG    1 
ATOM   11809 C CD1   . LEU D  1 28  ? -7.834  61.963  226.258 1.00 59.99  ? 28  LEU D CD1   1 
ATOM   11810 C CD2   . LEU D  1 28  ? -6.104  60.461  225.236 1.00 50.49  ? 28  LEU D CD2   1 
ATOM   11811 N N     . SER D  1 29  ? -10.267 57.652  223.578 1.00 50.00  ? 29  SER D N     1 
ATOM   11812 C CA    . SER D  1 29  ? -11.274 56.597  223.638 1.00 49.15  ? 29  SER D CA    1 
ATOM   11813 C C     . SER D  1 29  ? -10.678 55.281  223.155 1.00 41.04  ? 29  SER D C     1 
ATOM   11814 O O     . SER D  1 29  ? -10.895 54.231  223.761 1.00 43.22  ? 29  SER D O     1 
ATOM   11815 C CB    . SER D  1 29  ? -12.506 56.963  222.803 1.00 41.86  ? 29  SER D CB    1 
ATOM   11816 O OG    . SER D  1 29  ? -13.222 58.038  223.382 1.00 53.95  ? 29  SER D OG    1 
ATOM   11817 N N     . CYS D  1 30  ? -9.921  55.346  222.064 1.00 41.37  ? 30  CYS D N     1 
ATOM   11818 C CA    . CYS D  1 30  ? -9.280  54.162  221.496 1.00 46.33  ? 30  CYS D CA    1 
ATOM   11819 C C     . CYS D  1 30  ? -8.319  53.516  222.488 1.00 39.32  ? 30  CYS D C     1 
ATOM   11820 O O     . CYS D  1 30  ? -8.366  52.305  222.716 1.00 37.02  ? 30  CYS D O     1 
ATOM   11821 C CB    . CYS D  1 30  ? -8.538  54.525  220.208 1.00 39.00  ? 30  CYS D CB    1 
ATOM   11822 S SG    . CYS D  1 30  ? -7.836  53.121  219.324 1.00 47.15  ? 30  CYS D SG    1 
ATOM   11823 N N     . LEU D  1 31  ? -7.451  54.335  223.074 1.00 43.00  ? 31  LEU D N     1 
ATOM   11824 C CA    . LEU D  1 31  ? -6.474  53.859  224.045 1.00 44.68  ? 31  LEU D CA    1 
ATOM   11825 C C     . LEU D  1 31  ? -7.154  53.277  225.278 1.00 38.79  ? 31  LEU D C     1 
ATOM   11826 O O     . LEU D  1 31  ? -6.721  52.255  225.807 1.00 40.32  ? 31  LEU D O     1 
ATOM   11827 C CB    . LEU D  1 31  ? -5.530  54.990  224.462 1.00 38.33  ? 31  LEU D CB    1 
ATOM   11828 C CG    . LEU D  1 31  ? -4.561  55.524  223.407 1.00 43.90  ? 31  LEU D CG    1 
ATOM   11829 C CD1   . LEU D  1 31  ? -3.750  56.681  223.973 1.00 43.08  ? 31  LEU D CD1   1 
ATOM   11830 C CD2   . LEU D  1 31  ? -3.645  54.424  222.883 1.00 37.20  ? 31  LEU D CD2   1 
ATOM   11831 N N     . THR D  1 32  ? -8.216  53.936  225.733 1.00 47.44  ? 32  THR D N     1 
ATOM   11832 C CA    . THR D  1 32  ? -8.956  53.482  226.907 1.00 46.18  ? 32  THR D CA    1 
ATOM   11833 C C     . THR D  1 32  ? -9.619  52.130  226.657 1.00 43.40  ? 32  THR D C     1 
ATOM   11834 O O     . THR D  1 32  ? -9.556  51.232  227.497 1.00 40.49  ? 32  THR D O     1 
ATOM   11835 C CB    . THR D  1 32  ? -10.035 54.500  227.325 1.00 48.35  ? 32  THR D CB    1 
ATOM   11836 O OG1   . THR D  1 32  ? -9.439  55.794  227.481 1.00 49.79  ? 32  THR D OG1   1 
ATOM   11837 C CG2   . THR D  1 32  ? -10.691 54.078  228.637 1.00 47.38  ? 32  THR D CG2   1 
ATOM   11838 N N     . PHE D  1 33  ? -10.251 51.990  225.496 1.00 41.34  ? 33  PHE D N     1 
ATOM   11839 C CA    . PHE D  1 33  ? -10.873 50.728  225.110 1.00 40.59  ? 33  PHE D CA    1 
ATOM   11840 C C     . PHE D  1 33  ? -9.839  49.623  224.919 1.00 45.13  ? 33  PHE D C     1 
ATOM   11841 O O     . PHE D  1 33  ? -10.106 48.457  225.214 1.00 39.41  ? 33  PHE D O     1 
ATOM   11842 C CB    . PHE D  1 33  ? -11.688 50.899  223.830 1.00 40.84  ? 33  PHE D CB    1 
ATOM   11843 C CG    . PHE D  1 33  ? -13.092 51.383  224.065 1.00 45.82  ? 33  PHE D CG    1 
ATOM   11844 C CD1   . PHE D  1 33  ? -13.988 50.619  224.791 1.00 41.74  ? 33  PHE D CD1   1 
ATOM   11845 C CD2   . PHE D  1 33  ? -13.519 52.595  223.547 1.00 41.77  ? 33  PHE D CD2   1 
ATOM   11846 C CE1   . PHE D  1 33  ? -15.282 51.055  225.005 1.00 43.80  ? 33  PHE D CE1   1 
ATOM   11847 C CE2   . PHE D  1 33  ? -14.812 53.038  223.754 1.00 47.47  ? 33  PHE D CE2   1 
ATOM   11848 C CZ    . PHE D  1 33  ? -15.695 52.267  224.485 1.00 39.51  ? 33  PHE D CZ    1 
ATOM   11849 N N     . ASN D  1 34  ? -8.660  49.991  224.425 1.00 41.16  ? 34  ASN D N     1 
ATOM   11850 C CA    . ASN D  1 34  ? -7.612  49.012  224.150 1.00 40.21  ? 34  ASN D CA    1 
ATOM   11851 C C     . ASN D  1 34  ? -6.771  48.671  225.374 1.00 38.87  ? 34  ASN D C     1 
ATOM   11852 O O     . ASN D  1 34  ? -5.815  47.900  225.280 1.00 44.23  ? 34  ASN D O     1 
ATOM   11853 C CB    . ASN D  1 34  ? -6.702  49.511  223.029 1.00 36.64  ? 34  ASN D CB    1 
ATOM   11854 C CG    . ASN D  1 34  ? -7.304  49.299  221.656 1.00 40.39  ? 34  ASN D CG    1 
ATOM   11855 O OD1   . ASN D  1 34  ? -6.952  48.352  220.951 1.00 41.70  ? 34  ASN D OD1   1 
ATOM   11856 N ND2   . ASN D  1 34  ? -8.227  50.172  221.274 1.00 35.89  ? 34  ASN D ND2   1 
ATOM   11857 N N     . GLY D  1 35  ? -7.122  49.247  226.519 1.00 36.28  ? 35  GLY D N     1 
ATOM   11858 C CA    . GLY D  1 35  ? -6.453  48.920  227.767 1.00 42.07  ? 35  GLY D CA    1 
ATOM   11859 C C     . GLY D  1 35  ? -5.083  49.552  227.954 1.00 42.64  ? 35  GLY D C     1 
ATOM   11860 O O     . GLY D  1 35  ? -4.246  49.026  228.688 1.00 39.81  ? 35  GLY D O     1 
ATOM   11861 N N     . VAL D  1 36  ? -4.853  50.682  227.294 1.00 39.90  ? 36  VAL D N     1 
ATOM   11862 C CA    . VAL D  1 36  ? -3.594  51.406  227.436 1.00 41.72  ? 36  VAL D CA    1 
ATOM   11863 C C     . VAL D  1 36  ? -3.825  52.677  228.251 1.00 46.68  ? 36  VAL D C     1 
ATOM   11864 O O     . VAL D  1 36  ? -4.220  53.707  227.704 1.00 42.81  ? 36  VAL D O     1 
ATOM   11865 C CB    . VAL D  1 36  ? -2.989  51.758  226.061 1.00 38.78  ? 36  VAL D CB    1 
ATOM   11866 C CG1   . VAL D  1 36  ? -1.662  52.484  226.229 1.00 40.27  ? 36  VAL D CG1   1 
ATOM   11867 C CG2   . VAL D  1 36  ? -2.810  50.496  225.224 1.00 30.97  ? 36  VAL D CG2   1 
ATOM   11868 N N     . ARG D  1 37  ? -3.579  52.603  229.558 1.00 50.61  ? 37  ARG D N     1 
ATOM   11869 C CA    . ARG D  1 37  ? -3.991  53.675  230.466 1.00 50.54  ? 37  ARG D CA    1 
ATOM   11870 C C     . ARG D  1 37  ? -2.909  54.696  230.826 1.00 54.48  ? 37  ARG D C     1 
ATOM   11871 O O     . ARG D  1 37  ? -3.235  55.825  231.190 1.00 54.54  ? 37  ARG D O     1 
ATOM   11872 C CB    . ARG D  1 37  ? -4.550  53.078  231.762 1.00 57.09  ? 37  ARG D CB    1 
ATOM   11873 C CG    . ARG D  1 37  ? -5.847  52.294  231.589 1.00 65.24  ? 37  ARG D CG    1 
ATOM   11874 C CD    . ARG D  1 37  ? -6.954  53.129  230.949 1.00 77.57  ? 37  ARG D CD    1 
ATOM   11875 N NE    . ARG D  1 37  ? -7.312  54.310  231.736 1.00 91.43  ? 37  ARG D NE    1 
ATOM   11876 C CZ    . ARG D  1 37  ? -8.305  54.353  232.620 1.00 90.38  ? 37  ARG D CZ    1 
ATOM   11877 N NH1   . ARG D  1 37  ? -8.551  55.472  233.289 1.00 94.00  ? 37  ARG D NH1   1 
ATOM   11878 N NH2   . ARG D  1 37  ? -9.053  53.281  232.836 1.00 83.95  ? 37  ARG D NH2   1 
ATOM   11879 N N     . ASN D  1 38  ? -1.635  54.319  230.750 1.00 49.32  ? 38  ASN D N     1 
ATOM   11880 C CA    . ASN D  1 38  ? -0.580  55.285  231.047 1.00 50.00  ? 38  ASN D CA    1 
ATOM   11881 C C     . ASN D  1 38  ? -0.311  56.171  229.833 1.00 48.11  ? 38  ASN D C     1 
ATOM   11882 O O     . ASN D  1 38  ? 0.553   55.879  229.007 1.00 40.01  ? 38  ASN D O     1 
ATOM   11883 C CB    . ASN D  1 38  ? 0.711   54.597  231.505 1.00 53.68  ? 38  ASN D CB    1 
ATOM   11884 C CG    . ASN D  1 38  ? 1.681   55.567  232.178 1.00 51.86  ? 38  ASN D CG    1 
ATOM   11885 O OD1   . ASN D  1 38  ? 1.816   56.716  231.758 1.00 50.21  ? 38  ASN D OD1   1 
ATOM   11886 N ND2   . ASN D  1 38  ? 2.350   55.108  233.232 1.00 58.20  ? 38  ASN D ND2   1 
ATOM   11887 N N     . HIS D  1 39  ? -1.069  57.257  229.743 1.00 45.63  ? 39  HIS D N     1 
ATOM   11888 C CA    . HIS D  1 39  ? -0.943  58.216  228.658 1.00 43.44  ? 39  HIS D CA    1 
ATOM   11889 C C     . HIS D  1 39  ? -1.195  59.621  229.193 1.00 53.72  ? 39  HIS D C     1 
ATOM   11890 O O     . HIS D  1 39  ? -2.007  59.805  230.097 1.00 56.82  ? 39  HIS D O     1 
ATOM   11891 C CB    . HIS D  1 39  ? -1.931  57.886  227.543 1.00 47.46  ? 39  HIS D CB    1 
ATOM   11892 C CG    . HIS D  1 39  ? -3.343  57.750  228.020 1.00 54.77  ? 39  HIS D CG    1 
ATOM   11893 N ND1   . HIS D  1 39  ? -4.176  58.832  228.197 1.00 58.39  ? 39  HIS D ND1   1 
ATOM   11894 C CD2   . HIS D  1 39  ? -4.060  56.659  228.381 1.00 52.04  ? 39  HIS D CD2   1 
ATOM   11895 C CE1   . HIS D  1 39  ? -5.351  58.414  228.635 1.00 51.95  ? 39  HIS D CE1   1 
ATOM   11896 N NE2   . HIS D  1 39  ? -5.306  57.100  228.756 1.00 55.56  ? 39  HIS D NE2   1 
ATOM   11897 N N     . THR D  1 40  ? -0.487  60.608  228.651 1.00 47.46  ? 40  THR D N     1 
ATOM   11898 C CA    . THR D  1 40  ? -0.718  62.005  229.013 1.00 47.47  ? 40  THR D CA    1 
ATOM   11899 C C     . THR D  1 40  ? -0.797  62.870  227.759 1.00 46.84  ? 40  THR D C     1 
ATOM   11900 O O     . THR D  1 40  ? 0.099   62.831  226.915 1.00 45.29  ? 40  THR D O     1 
ATOM   11901 C CB    . THR D  1 40  ? 0.393   62.570  229.932 1.00 51.30  ? 40  THR D CB    1 
ATOM   11902 O OG1   . THR D  1 40  ? 1.568   62.847  229.161 1.00 55.80  ? 40  THR D OG1   1 
ATOM   11903 C CG2   . THR D  1 40  ? 0.734   61.597  231.052 1.00 51.21  ? 40  THR D CG2   1 
ATOM   11904 N N     . VAL D  1 41  ? -1.867  63.648  227.635 1.00 49.75  ? 41  VAL D N     1 
ATOM   11905 C CA    . VAL D  1 41  ? -2.010  64.564  226.507 1.00 45.83  ? 41  VAL D CA    1 
ATOM   11906 C C     . VAL D  1 41  ? -1.173  65.812  226.753 1.00 48.86  ? 41  VAL D C     1 
ATOM   11907 O O     . VAL D  1 41  ? -0.631  65.987  227.845 1.00 52.26  ? 41  VAL D O     1 
ATOM   11908 C CB    . VAL D  1 41  ? -3.473  64.964  226.278 1.00 51.00  ? 41  VAL D CB    1 
ATOM   11909 C CG1   . VAL D  1 41  ? -4.325  63.728  226.046 1.00 46.06  ? 41  VAL D CG1   1 
ATOM   11910 C CG2   . VAL D  1 41  ? -3.995  65.762  227.462 1.00 47.97  ? 41  VAL D CG2   1 
ATOM   11911 N N     . PHE D  1 42  ? -1.068  66.676  225.744 1.00 51.67  ? 42  PHE D N     1 
ATOM   11912 C CA    . PHE D  1 42  ? -0.253  67.887  225.852 1.00 51.89  ? 42  PHE D CA    1 
ATOM   11913 C C     . PHE D  1 42  ? -0.672  68.755  227.034 1.00 60.62  ? 42  PHE D C     1 
ATOM   11914 O O     . PHE D  1 42  ? -1.830  68.750  227.445 1.00 63.96  ? 42  PHE D O     1 
ATOM   11915 C CB    . PHE D  1 42  ? -0.326  68.711  224.555 1.00 56.58  ? 42  PHE D CB    1 
ATOM   11916 C CG    . PHE D  1 42  ? 0.531   69.960  224.565 1.00 65.01  ? 42  PHE D CG    1 
ATOM   11917 C CD1   . PHE D  1 42  ? 1.851   69.913  224.149 1.00 66.20  ? 42  PHE D CD1   1 
ATOM   11918 C CD2   . PHE D  1 42  ? 0.013   71.180  224.983 1.00 63.50  ? 42  PHE D CD2   1 
ATOM   11919 C CE1   . PHE D  1 42  ? 2.643   71.053  224.157 1.00 71.79  ? 42  PHE D CE1   1 
ATOM   11920 C CE2   . PHE D  1 42  ? 0.801   72.324  224.994 1.00 71.04  ? 42  PHE D CE2   1 
ATOM   11921 C CZ    . PHE D  1 42  ? 2.116   72.257  224.579 1.00 72.32  ? 42  PHE D CZ    1 
ATOM   11922 N N     . SER D  1 43  ? 0.294   69.486  227.577 1.00 64.87  ? 43  SER D N     1 
ATOM   11923 C CA    . SER D  1 43  ? 0.049   70.510  228.582 1.00 62.10  ? 43  SER D CA    1 
ATOM   11924 C C     . SER D  1 43  ? 1.169   71.534  228.494 1.00 72.26  ? 43  SER D C     1 
ATOM   11925 O O     . SER D  1 43  ? 2.344   71.180  228.578 1.00 70.84  ? 43  SER D O     1 
ATOM   11926 C CB    . SER D  1 43  ? -0.024  69.911  229.987 1.00 65.32  ? 43  SER D CB    1 
ATOM   11927 O OG    . SER D  1 43  ? -0.053  70.928  230.973 1.00 75.75  ? 43  SER D OG    1 
ATOM   11928 N N     . ALA D  1 44  ? 0.806   72.800  228.311 1.00 74.99  ? 44  ALA D N     1 
ATOM   11929 C CA    . ALA D  1 44  ? 1.798   73.863  228.182 1.00 81.70  ? 44  ALA D CA    1 
ATOM   11930 C C     . ALA D  1 44  ? 2.420   74.193  229.535 1.00 78.25  ? 44  ALA D C     1 
ATOM   11931 O O     . ALA D  1 44  ? 3.407   74.921  229.616 1.00 75.26  ? 44  ALA D O     1 
ATOM   11932 C CB    . ALA D  1 44  ? 1.174   75.102  227.565 1.00 77.14  ? 44  ALA D CB    1 
ATOM   11933 N N     . ASP D  1 45  ? 1.826   73.651  230.593 1.00 80.56  ? 45  ASP D N     1 
ATOM   11934 C CA    . ASP D  1 45  ? 2.344   73.802  231.947 1.00 83.55  ? 45  ASP D CA    1 
ATOM   11935 C C     . ASP D  1 45  ? 3.658   73.037  232.102 1.00 81.82  ? 45  ASP D C     1 
ATOM   11936 O O     . ASP D  1 45  ? 3.693   71.814  231.973 1.00 80.72  ? 45  ASP D O     1 
ATOM   11937 C CB    . ASP D  1 45  ? 1.298   73.321  232.961 1.00 84.95  ? 45  ASP D CB    1 
ATOM   11938 C CG    . ASP D  1 45  ? 1.756   73.464  234.403 1.00 93.41  ? 45  ASP D CG    1 
ATOM   11939 O OD1   . ASP D  1 45  ? 2.809   74.085  234.652 1.00 101.62 ? 45  ASP D OD1   1 
ATOM   11940 O OD2   . ASP D  1 45  ? 1.043   72.957  235.296 1.00 93.58  ? 45  ASP D OD2   1 
ATOM   11941 N N     . SER D  1 46  ? 4.736   73.765  232.386 1.00 82.69  ? 46  SER D N     1 
ATOM   11942 C CA    . SER D  1 46  ? 6.060   73.163  232.527 1.00 81.16  ? 46  SER D CA    1 
ATOM   11943 C C     . SER D  1 46  ? 6.146   72.209  233.718 1.00 83.51  ? 46  SER D C     1 
ATOM   11944 O O     . SER D  1 46  ? 7.088   71.424  233.824 1.00 86.23  ? 46  SER D O     1 
ATOM   11945 C CB    . SER D  1 46  ? 7.129   74.252  232.666 1.00 81.04  ? 46  SER D CB    1 
ATOM   11946 O OG    . SER D  1 46  ? 7.334   74.928  231.438 1.00 83.07  ? 46  SER D OG    1 
ATOM   11947 N N     . ASP D  1 47  ? 5.165   72.277  234.612 1.00 84.86  ? 47  ASP D N     1 
ATOM   11948 C CA    . ASP D  1 47  ? 5.152   71.416  235.788 1.00 88.49  ? 47  ASP D CA    1 
ATOM   11949 C C     . ASP D  1 47  ? 4.277   70.184  235.599 1.00 87.06  ? 47  ASP D C     1 
ATOM   11950 O O     . ASP D  1 47  ? 4.110   69.390  236.523 1.00 82.15  ? 47  ASP D O     1 
ATOM   11951 C CB    . ASP D  1 47  ? 4.680   72.193  237.018 1.00 97.80  ? 47  ASP D CB    1 
ATOM   11952 C CG    . ASP D  1 47  ? 5.734   73.141  237.543 1.00 112.21 ? 47  ASP D CG    1 
ATOM   11953 O OD1   . ASP D  1 47  ? 6.893   73.046  237.086 1.00 115.35 ? 47  ASP D OD1   1 
ATOM   11954 O OD2   . ASP D  1 47  ? 5.412   73.973  238.417 1.00 120.61 ? 47  ASP D OD2   1 
ATOM   11955 N N     . SER D  1 48  ? 3.724   70.022  234.402 1.00 81.36  ? 48  SER D N     1 
ATOM   11956 C CA    . SER D  1 48  ? 2.813   68.916  234.134 1.00 73.46  ? 48  SER D CA    1 
ATOM   11957 C C     . SER D  1 48  ? 3.542   67.584  233.989 1.00 71.15  ? 48  SER D C     1 
ATOM   11958 O O     . SER D  1 48  ? 4.735   67.548  233.686 1.00 70.17  ? 48  SER D O     1 
ATOM   11959 C CB    . SER D  1 48  ? 2.000   69.196  232.871 1.00 72.63  ? 48  SER D CB    1 
ATOM   11960 O OG    . SER D  1 48  ? 2.842   69.362  231.744 1.00 68.93  ? 48  SER D OG    1 
ATOM   11961 N N     . ASP D  1 49  ? 2.813   66.493  234.215 1.00 70.11  ? 49  ASP D N     1 
ATOM   11962 C CA    . ASP D  1 49  ? 3.328   65.148  233.980 1.00 67.21  ? 49  ASP D CA    1 
ATOM   11963 C C     . ASP D  1 49  ? 3.762   64.997  232.530 1.00 64.24  ? 49  ASP D C     1 
ATOM   11964 O O     . ASP D  1 49  ? 4.725   64.293  232.226 1.00 63.06  ? 49  ASP D O     1 
ATOM   11965 C CB    . ASP D  1 49  ? 2.273   64.091  234.321 1.00 70.72  ? 49  ASP D CB    1 
ATOM   11966 C CG    . ASP D  1 49  ? 2.309   63.673  235.778 1.00 77.25  ? 49  ASP D CG    1 
ATOM   11967 O OD1   . ASP D  1 49  ? 3.130   64.224  236.542 1.00 80.13  ? 49  ASP D OD1   1 
ATOM   11968 O OD2   . ASP D  1 49  ? 1.507   62.795  236.161 1.00 77.02  ? 49  ASP D OD2   1 
ATOM   11969 N N     . PHE D  1 50  ? 3.036   65.666  231.638 1.00 59.64  ? 50  PHE D N     1 
ATOM   11970 C CA    . PHE D  1 50  ? 3.357   65.654  230.217 1.00 58.04  ? 50  PHE D CA    1 
ATOM   11971 C C     . PHE D  1 50  ? 4.760   66.178  229.946 1.00 58.37  ? 50  PHE D C     1 
ATOM   11972 O O     . PHE D  1 50  ? 5.618   65.446  229.454 1.00 57.33  ? 50  PHE D O     1 
ATOM   11973 C CB    . PHE D  1 50  ? 2.347   66.484  229.427 1.00 52.14  ? 50  PHE D CB    1 
ATOM   11974 C CG    . PHE D  1 50  ? 2.737   66.696  227.994 1.00 51.67  ? 50  PHE D CG    1 
ATOM   11975 C CD1   . PHE D  1 50  ? 2.524   65.703  227.053 1.00 48.05  ? 50  PHE D CD1   1 
ATOM   11976 C CD2   . PHE D  1 50  ? 3.326   67.884  227.587 1.00 51.89  ? 50  PHE D CD2   1 
ATOM   11977 C CE1   . PHE D  1 50  ? 2.886   65.890  225.734 1.00 44.41  ? 50  PHE D CE1   1 
ATOM   11978 C CE2   . PHE D  1 50  ? 3.693   68.075  226.272 1.00 49.24  ? 50  PHE D CE2   1 
ATOM   11979 C CZ    . PHE D  1 50  ? 3.471   67.078  225.343 1.00 45.84  ? 50  PHE D CZ    1 
ATOM   11980 N N     . ASN D  1 51  ? 4.975   67.455  230.253 1.00 61.23  ? 51  ASN D N     1 
ATOM   11981 C CA    . ASN D  1 51  ? 6.267   68.105  230.049 1.00 55.97  ? 51  ASN D CA    1 
ATOM   11982 C C     . ASN D  1 51  ? 7.393   67.344  230.740 1.00 57.84  ? 51  ASN D C     1 
ATOM   11983 O O     . ASN D  1 51  ? 8.487   67.201  230.197 1.00 58.98  ? 51  ASN D O     1 
ATOM   11984 C CB    . ASN D  1 51  ? 6.215   69.549  230.554 1.00 64.58  ? 51  ASN D CB    1 
ATOM   11985 C CG    . ASN D  1 51  ? 7.486   70.322  230.256 1.00 67.40  ? 51  ASN D CG    1 
ATOM   11986 O OD1   . ASN D  1 51  ? 7.674   70.822  229.147 1.00 69.38  ? 51  ASN D OD1   1 
ATOM   11987 N ND2   . ASN D  1 51  ? 8.363   70.429  231.249 1.00 71.84  ? 51  ASN D ND2   1 
ATOM   11988 N N     . ARG D  1 52  ? 7.104   66.845  231.937 1.00 58.16  ? 52  ARG D N     1 
ATOM   11989 C CA    . ARG D  1 52  ? 8.067   66.070  232.707 1.00 55.27  ? 52  ARG D CA    1 
ATOM   11990 C C     . ARG D  1 52  ? 8.495   64.800  231.971 1.00 62.31  ? 52  ARG D C     1 
ATOM   11991 O O     . ARG D  1 52  ? 9.690   64.524  231.833 1.00 55.84  ? 52  ARG D O     1 
ATOM   11992 C CB    . ARG D  1 52  ? 7.474   65.717  234.067 1.00 56.05  ? 52  ARG D CB    1 
ATOM   11993 C CG    . ARG D  1 52  ? 8.490   65.297  235.106 1.00 63.21  ? 52  ARG D CG    1 
ATOM   11994 C CD    . ARG D  1 52  ? 7.783   64.802  236.347 1.00 67.77  ? 52  ARG D CD    1 
ATOM   11995 N NE    . ARG D  1 52  ? 8.135   63.426  236.681 1.00 70.76  ? 52  ARG D NE    1 
ATOM   11996 C CZ    . ARG D  1 52  ? 7.291   62.561  237.230 1.00 78.64  ? 52  ARG D CZ    1 
ATOM   11997 N NH1   . ARG D  1 52  ? 6.044   62.929  237.490 1.00 79.81  ? 52  ARG D NH1   1 
ATOM   11998 N NH2   . ARG D  1 52  ? 7.687   61.329  237.513 1.00 75.88  ? 52  ARG D NH2   1 
ATOM   11999 N N     . PHE D  1 53  ? 7.516   64.026  231.509 1.00 55.70  ? 53  PHE D N     1 
ATOM   12000 C CA    . PHE D  1 53  ? 7.790   62.812  230.748 1.00 53.49  ? 53  PHE D CA    1 
ATOM   12001 C C     . PHE D  1 53  ? 8.533   63.129  229.457 1.00 51.71  ? 53  PHE D C     1 
ATOM   12002 O O     . PHE D  1 53  ? 9.455   62.411  229.071 1.00 50.43  ? 53  PHE D O     1 
ATOM   12003 C CB    . PHE D  1 53  ? 6.491   62.068  230.428 1.00 55.77  ? 53  PHE D CB    1 
ATOM   12004 C CG    . PHE D  1 53  ? 5.938   61.286  231.581 1.00 57.25  ? 53  PHE D CG    1 
ATOM   12005 C CD1   . PHE D  1 53  ? 6.773   60.808  232.574 1.00 59.12  ? 53  PHE D CD1   1 
ATOM   12006 C CD2   . PHE D  1 53  ? 4.579   61.027  231.671 1.00 63.83  ? 53  PHE D CD2   1 
ATOM   12007 C CE1   . PHE D  1 53  ? 6.267   60.086  233.639 1.00 64.21  ? 53  PHE D CE1   1 
ATOM   12008 C CE2   . PHE D  1 53  ? 4.066   60.305  232.733 1.00 64.09  ? 53  PHE D CE2   1 
ATOM   12009 C CZ    . PHE D  1 53  ? 4.911   59.834  233.718 1.00 69.62  ? 53  PHE D CZ    1 
ATOM   12010 N N     . LEU D  1 54  ? 8.132   64.215  228.802 1.00 47.38  ? 54  LEU D N     1 
ATOM   12011 C CA    . LEU D  1 54  ? 8.734   64.618  227.534 1.00 51.33  ? 54  LEU D CA    1 
ATOM   12012 C C     . LEU D  1 54  ? 10.234  64.879  227.645 1.00 53.42  ? 54  LEU D C     1 
ATOM   12013 O O     . LEU D  1 54  ? 10.998  64.548  226.740 1.00 51.26  ? 54  LEU D O     1 
ATOM   12014 C CB    . LEU D  1 54  ? 8.037   65.874  226.989 1.00 45.13  ? 54  LEU D CB    1 
ATOM   12015 C CG    . LEU D  1 54  ? 8.697   66.560  225.784 1.00 51.29  ? 54  LEU D CG    1 
ATOM   12016 C CD1   . LEU D  1 54  ? 8.736   65.627  224.581 1.00 35.75  ? 54  LEU D CD1   1 
ATOM   12017 C CD2   . LEU D  1 54  ? 8.014   67.883  225.430 1.00 50.59  ? 54  LEU D CD2   1 
ATOM   12018 N N     . HIS D  1 55  ? 10.648  65.474  228.758 1.00 48.47  ? 55  HIS D N     1 
ATOM   12019 C CA    . HIS D  1 55  ? 12.018  65.950  228.904 1.00 58.54  ? 55  HIS D CA    1 
ATOM   12020 C C     . HIS D  1 55  ? 12.911  64.964  229.634 1.00 54.31  ? 55  HIS D C     1 
ATOM   12021 O O     . HIS D  1 55  ? 14.136  65.080  229.592 1.00 61.80  ? 55  HIS D O     1 
ATOM   12022 C CB    . HIS D  1 55  ? 12.031  67.290  229.639 1.00 54.49  ? 55  HIS D CB    1 
ATOM   12023 C CG    . HIS D  1 55  ? 11.460  68.416  228.841 1.00 62.07  ? 55  HIS D CG    1 
ATOM   12024 N ND1   . HIS D  1 55  ? 12.096  68.930  227.732 1.00 62.68  ? 55  HIS D ND1   1 
ATOM   12025 C CD2   . HIS D  1 55  ? 10.308  69.117  228.976 1.00 58.29  ? 55  HIS D CD2   1 
ATOM   12026 C CE1   . HIS D  1 55  ? 11.360  69.901  227.221 1.00 65.81  ? 55  HIS D CE1   1 
ATOM   12027 N NE2   . HIS D  1 55  ? 10.272  70.037  227.959 1.00 62.83  ? 55  HIS D NE2   1 
ATOM   12028 N N     . LEU D  1 56  ? 12.295  63.987  230.288 1.00 56.56  ? 56  LEU D N     1 
ATOM   12029 C CA    . LEU D  1 56  ? 13.019  63.044  231.130 1.00 56.17  ? 56  LEU D CA    1 
ATOM   12030 C C     . LEU D  1 56  ? 14.044  62.217  230.354 1.00 60.73  ? 56  LEU D C     1 
ATOM   12031 O O     . LEU D  1 56  ? 15.051  61.779  230.912 1.00 61.60  ? 56  LEU D O     1 
ATOM   12032 C CB    . LEU D  1 56  ? 12.026  62.120  231.832 1.00 58.60  ? 56  LEU D CB    1 
ATOM   12033 C CG    . LEU D  1 56  ? 12.496  61.429  233.111 1.00 62.99  ? 56  LEU D CG    1 
ATOM   12034 C CD1   . LEU D  1 56  ? 13.021  62.438  234.120 1.00 56.14  ? 56  LEU D CD1   1 
ATOM   12035 C CD2   . LEU D  1 56  ? 11.353  60.624  233.695 1.00 62.96  ? 56  LEU D CD2   1 
ATOM   12036 N N     . SER D  1 57  ? 13.789  62.009  229.066 1.00 56.34  ? 57  SER D N     1 
ATOM   12037 C CA    . SER D  1 57  ? 14.706  61.241  228.232 1.00 54.24  ? 57  SER D CA    1 
ATOM   12038 C C     . SER D  1 57  ? 15.167  62.012  226.999 1.00 51.65  ? 57  SER D C     1 
ATOM   12039 O O     . SER D  1 57  ? 15.443  61.418  225.956 1.00 54.63  ? 57  SER D O     1 
ATOM   12040 C CB    . SER D  1 57  ? 14.058  59.922  227.809 1.00 48.01  ? 57  SER D CB    1 
ATOM   12041 O OG    . SER D  1 57  ? 13.970  59.036  228.907 1.00 56.64  ? 57  SER D OG    1 
ATOM   12042 N N     . ILE D  1 58  ? 15.243  63.333  227.114 1.00 53.77  ? 58  ILE D N     1 
ATOM   12043 C CA    . ILE D  1 58  ? 15.908  64.135  226.097 1.00 54.81  ? 58  ILE D CA    1 
ATOM   12044 C C     . ILE D  1 58  ? 17.386  64.204  226.456 1.00 53.69  ? 58  ILE D C     1 
ATOM   12045 O O     . ILE D  1 58  ? 17.752  64.738  227.502 1.00 57.18  ? 58  ILE D O     1 
ATOM   12046 C CB    . ILE D  1 58  ? 15.310  65.553  225.986 1.00 53.64  ? 58  ILE D CB    1 
ATOM   12047 C CG1   . ILE D  1 58  ? 13.851  65.478  225.533 1.00 54.65  ? 58  ILE D CG1   1 
ATOM   12048 C CG2   . ILE D  1 58  ? 16.114  66.401  225.011 1.00 51.64  ? 58  ILE D CG2   1 
ATOM   12049 C CD1   . ILE D  1 58  ? 13.235  66.823  225.222 1.00 52.45  ? 58  ILE D CD1   1 
ATOM   12050 N N     . GLN D  1 59  ? 18.232  63.642  225.598 1.00 48.65  ? 59  GLN D N     1 
ATOM   12051 C CA    . GLN D  1 59  ? 19.649  63.504  225.916 1.00 51.11  ? 59  GLN D CA    1 
ATOM   12052 C C     . GLN D  1 59  ? 20.501  64.493  225.127 1.00 45.55  ? 59  GLN D C     1 
ATOM   12053 O O     . GLN D  1 59  ? 21.711  64.589  225.332 1.00 48.42  ? 59  GLN D O     1 
ATOM   12054 C CB    . GLN D  1 59  ? 20.113  62.068  225.656 1.00 43.75  ? 59  GLN D CB    1 
ATOM   12055 C CG    . GLN D  1 59  ? 19.294  60.993  226.384 1.00 49.20  ? 59  GLN D CG    1 
ATOM   12056 C CD    . GLN D  1 59  ? 19.506  60.988  227.890 1.00 54.25  ? 59  GLN D CD    1 
ATOM   12057 O OE1   . GLN D  1 59  ? 20.221  61.829  228.435 1.00 61.28  ? 59  GLN D OE1   1 
ATOM   12058 N NE2   . GLN D  1 59  ? 18.885  60.031  228.569 1.00 54.79  ? 59  GLN D NE2   1 
ATOM   12059 N N     . ASN D  1 60  ? 19.860  65.223  224.222 1.00 45.48  ? 60  ASN D N     1 
ATOM   12060 C CA    . ASN D  1 60  ? 20.510  66.318  223.513 1.00 53.60  ? 60  ASN D CA    1 
ATOM   12061 C C     . ASN D  1 60  ? 19.655  67.576  223.599 1.00 55.87  ? 60  ASN D C     1 
ATOM   12062 O O     . ASN D  1 60  ? 18.779  67.792  222.761 1.00 54.34  ? 60  ASN D O     1 
ATOM   12063 C CB    . ASN D  1 60  ? 20.768  65.949  222.051 1.00 48.23  ? 60  ASN D CB    1 
ATOM   12064 C CG    . ASN D  1 60  ? 21.680  66.942  221.345 1.00 50.71  ? 60  ASN D CG    1 
ATOM   12065 O OD1   . ASN D  1 60  ? 22.003  68.001  221.884 1.00 51.03  ? 60  ASN D OD1   1 
ATOM   12066 N ND2   . ASN D  1 60  ? 22.094  66.602  220.128 1.00 50.07  ? 60  ASN D ND2   1 
ATOM   12067 N N     . PRO D  1 61  ? 19.911  68.411  224.622 1.00 60.26  ? 61  PRO D N     1 
ATOM   12068 C CA    . PRO D  1 61  ? 19.249  69.696  224.883 1.00 60.89  ? 61  PRO D CA    1 
ATOM   12069 C C     . PRO D  1 61  ? 19.122  70.609  223.659 1.00 59.14  ? 61  PRO D C     1 
ATOM   12070 O O     . PRO D  1 61  ? 18.299  71.524  223.680 1.00 57.56  ? 61  PRO D O     1 
ATOM   12071 C CB    . PRO D  1 61  ? 20.154  70.333  225.937 1.00 61.63  ? 61  PRO D CB    1 
ATOM   12072 C CG    . PRO D  1 61  ? 20.655  69.166  226.714 1.00 63.00  ? 61  PRO D CG    1 
ATOM   12073 C CD    . PRO D  1 61  ? 20.838  68.052  225.710 1.00 56.60  ? 61  PRO D CD    1 
ATOM   12074 N N     . LEU D  1 62  ? 19.911  70.361  222.616 1.00 53.62  ? 62  LEU D N     1 
ATOM   12075 C CA    . LEU D  1 62  ? 19.815  71.125  221.373 1.00 52.25  ? 62  LEU D CA    1 
ATOM   12076 C C     . LEU D  1 62  ? 18.395  71.076  220.795 1.00 58.50  ? 62  LEU D C     1 
ATOM   12077 O O     . LEU D  1 62  ? 17.977  71.978  220.062 1.00 54.52  ? 62  LEU D O     1 
ATOM   12078 C CB    . LEU D  1 62  ? 20.822  70.600  220.345 1.00 52.36  ? 62  LEU D CB    1 
ATOM   12079 C CG    . LEU D  1 62  ? 20.823  71.245  218.954 1.00 57.01  ? 62  LEU D CG    1 
ATOM   12080 C CD1   . LEU D  1 62  ? 21.227  72.714  219.035 1.00 60.50  ? 62  LEU D CD1   1 
ATOM   12081 C CD2   . LEU D  1 62  ? 21.721  70.485  217.980 1.00 53.78  ? 62  LEU D CD2   1 
ATOM   12082 N N     . PHE D  1 63  ? 17.653  70.028  221.140 1.00 61.49  ? 63  PHE D N     1 
ATOM   12083 C CA    . PHE D  1 63  ? 16.302  69.825  220.627 1.00 59.75  ? 63  PHE D CA    1 
ATOM   12084 C C     . PHE D  1 63  ? 15.227  69.942  221.698 1.00 65.35  ? 63  PHE D C     1 
ATOM   12085 O O     . PHE D  1 63  ? 14.139  69.387  221.548 1.00 69.02  ? 63  PHE D O     1 
ATOM   12086 C CB    . PHE D  1 63  ? 16.189  68.443  219.983 1.00 47.00  ? 63  PHE D CB    1 
ATOM   12087 C CG    . PHE D  1 63  ? 17.141  68.220  218.861 1.00 47.10  ? 63  PHE D CG    1 
ATOM   12088 C CD1   . PHE D  1 63  ? 16.858  68.717  217.600 1.00 44.30  ? 63  PHE D CD1   1 
ATOM   12089 C CD2   . PHE D  1 63  ? 18.315  67.507  219.061 1.00 45.02  ? 63  PHE D CD2   1 
ATOM   12090 C CE1   . PHE D  1 63  ? 17.730  68.515  216.553 1.00 46.14  ? 63  PHE D CE1   1 
ATOM   12091 C CE2   . PHE D  1 63  ? 19.195  67.299  218.018 1.00 43.33  ? 63  PHE D CE2   1 
ATOM   12092 C CZ    . PHE D  1 63  ? 18.900  67.806  216.763 1.00 41.69  ? 63  PHE D CZ    1 
ATOM   12093 N N     . GLN D  1 64  ? 15.513  70.651  222.780 1.00 69.75  ? 64  GLN D N     1 
ATOM   12094 C CA    . GLN D  1 64  ? 14.634  70.582  223.938 1.00 84.46  ? 64  GLN D CA    1 
ATOM   12095 C C     . GLN D  1 64  ? 13.567  71.671  223.966 1.00 93.38  ? 64  GLN D C     1 
ATOM   12096 O O     . GLN D  1 64  ? 12.372  71.383  223.865 1.00 88.11  ? 64  GLN D O     1 
ATOM   12097 C CB    . GLN D  1 64  ? 15.468  70.638  225.225 1.00 76.76  ? 64  GLN D CB    1 
ATOM   12098 C CG    . GLN D  1 64  ? 14.758  70.051  226.434 1.00 81.04  ? 64  GLN D CG    1 
ATOM   12099 C CD    . GLN D  1 64  ? 15.714  69.515  227.480 1.00 81.00  ? 64  GLN D CD    1 
ATOM   12100 O OE1   . GLN D  1 64  ? 16.928  69.677  227.369 1.00 86.52  ? 64  GLN D OE1   1 
ATOM   12101 N NE2   . GLN D  1 64  ? 15.170  68.865  228.501 1.00 81.11  ? 64  GLN D NE2   1 
ATOM   12102 N N     . ASN D  1 65  ? 14.017  72.918  224.069 1.00 100.41 ? 65  ASN D N     1 
ATOM   12103 C CA    . ASN D  1 65  ? 13.182  74.036  224.496 1.00 109.78 ? 65  ASN D CA    1 
ATOM   12104 C C     . ASN D  1 65  ? 12.124  74.544  223.503 1.00 111.66 ? 65  ASN D C     1 
ATOM   12105 O O     . ASN D  1 65  ? 12.415  75.337  222.603 1.00 110.98 ? 65  ASN D O     1 
ATOM   12106 C CB    . ASN D  1 65  ? 14.106  75.193  224.909 1.00 111.25 ? 65  ASN D CB    1 
ATOM   12107 C CG    . ASN D  1 65  ? 14.973  74.847  226.122 1.00 121.73 ? 65  ASN D CG    1 
ATOM   12108 O OD1   . ASN D  1 65  ? 15.834  73.968  226.056 1.00 120.85 ? 65  ASN D OD1   1 
ATOM   12109 N ND2   . ASN D  1 65  ? 14.742  75.541  227.233 1.00 123.28 ? 65  ASN D ND2   1 
ATOM   12110 N N     . SER D  1 66  ? 10.901  74.043  223.676 1.00 109.25 ? 66  SER D N     1 
ATOM   12111 C CA    . SER D  1 66  ? 9.660   74.651  223.162 1.00 110.88 ? 66  SER D CA    1 
ATOM   12112 C C     . SER D  1 66  ? 9.640   75.144  221.715 1.00 109.57 ? 66  SER D C     1 
ATOM   12113 O O     . SER D  1 66  ? 8.694   74.853  220.982 1.00 107.06 ? 66  SER D O     1 
ATOM   12114 C CB    . SER D  1 66  ? 9.263   75.805  224.082 1.00 116.22 ? 66  SER D CB    1 
ATOM   12115 O OG    . SER D  1 66  ? 8.899   75.315  225.366 1.00 120.64 ? 66  SER D OG    1 
ATOM   12116 N N     . LEU D  1 67  ? 10.659  75.898  221.314 1.00 111.95 ? 67  LEU D N     1 
ATOM   12117 C CA    . LEU D  1 67  ? 10.779  76.396  219.944 1.00 112.72 ? 67  LEU D CA    1 
ATOM   12118 C C     . LEU D  1 67  ? 10.724  75.284  218.896 1.00 105.89 ? 67  LEU D C     1 
ATOM   12119 O O     . LEU D  1 67  ? 10.364  75.527  217.738 1.00 104.04 ? 67  LEU D O     1 
ATOM   12120 C CB    . LEU D  1 67  ? 12.082  77.180  219.795 1.00 120.12 ? 67  LEU D CB    1 
ATOM   12121 C CG    . LEU D  1 67  ? 12.122  78.425  220.680 1.00 117.25 ? 67  LEU D CG    1 
ATOM   12122 C CD1   . LEU D  1 67  ? 13.385  79.238  220.449 1.00 105.34 ? 67  LEU D CD1   1 
ATOM   12123 C CD2   . LEU D  1 67  ? 10.884  79.262  220.411 1.00 111.68 ? 67  LEU D CD2   1 
ATOM   12124 N N     . ILE D  1 68  ? 11.083  74.066  219.304 1.00 102.01 ? 68  ILE D N     1 
ATOM   12125 C CA    . ILE D  1 68  ? 11.031  72.906  218.415 1.00 94.44  ? 68  ILE D CA    1 
ATOM   12126 C C     . ILE D  1 68  ? 9.879   71.961  218.779 1.00 91.97  ? 68  ILE D C     1 
ATOM   12127 O O     . ILE D  1 68  ? 9.414   71.935  219.921 1.00 91.97  ? 68  ILE D O     1 
ATOM   12128 C CB    . ILE D  1 68  ? 12.353  72.117  218.424 1.00 89.58  ? 68  ILE D CB    1 
ATOM   12129 C CG1   . ILE D  1 68  ? 12.537  71.378  217.091 1.00 88.97  ? 68  ILE D CG1   1 
ATOM   12130 C CG2   . ILE D  1 68  ? 12.398  71.141  219.592 1.00 84.55  ? 68  ILE D CG2   1 
ATOM   12131 C CD1   . ILE D  1 68  ? 12.532  72.295  215.872 1.00 88.57  ? 68  ILE D CD1   1 
ATOM   12132 N N     . SER D  1 69  ? 9.459   71.171  217.794 1.00 82.77  ? 69  SER D N     1 
ATOM   12133 C CA    . SER D  1 69  ? 8.213   70.405  217.829 1.00 84.76  ? 69  SER D CA    1 
ATOM   12134 C C     . SER D  1 69  ? 7.959   69.550  219.079 1.00 73.63  ? 69  SER D C     1 
ATOM   12135 O O     . SER D  1 69  ? 8.862   68.888  219.592 1.00 75.08  ? 69  SER D O     1 
ATOM   12136 C CB    . SER D  1 69  ? 8.145   69.494  216.603 1.00 78.45  ? 69  SER D CB    1 
ATOM   12137 O OG    . SER D  1 69  ? 9.076   68.429  216.705 1.00 57.74  ? 69  SER D OG    1 
ATOM   12138 N N     . LYS D  1 70  ? 6.710   69.562  219.545 1.00 61.71  ? 70  LYS D N     1 
ATOM   12139 C CA    . LYS D  1 70  ? 6.301   68.781  220.711 1.00 61.55  ? 70  LYS D CA    1 
ATOM   12140 C C     . LYS D  1 70  ? 5.156   67.822  220.381 1.00 59.67  ? 70  LYS D C     1 
ATOM   12141 O O     . LYS D  1 70  ? 4.316   68.129  219.533 1.00 53.79  ? 70  LYS D O     1 
ATOM   12142 C CB    . LYS D  1 70  ? 5.864   69.701  221.848 1.00 64.68  ? 70  LYS D CB    1 
ATOM   12143 C CG    . LYS D  1 70  ? 6.884   70.709  222.312 1.00 76.30  ? 70  LYS D CG    1 
ATOM   12144 C CD    . LYS D  1 70  ? 6.342   71.425  223.534 1.00 84.25  ? 70  LYS D CD    1 
ATOM   12145 C CE    . LYS D  1 70  ? 7.392   72.292  224.181 1.00 94.50  ? 70  LYS D CE    1 
ATOM   12146 N NZ    . LYS D  1 70  ? 8.717   71.611  224.227 1.00 92.14  ? 70  LYS D NZ    1 
ATOM   12147 N N     . PRO D  1 71  ? 5.099   66.667  221.070 1.00 50.95  ? 71  PRO D N     1 
ATOM   12148 C CA    . PRO D  1 71  ? 4.054   65.673  220.790 1.00 52.21  ? 71  PRO D CA    1 
ATOM   12149 C C     . PRO D  1 71  ? 2.684   66.080  221.316 1.00 48.87  ? 71  PRO D C     1 
ATOM   12150 O O     . PRO D  1 71  ? 2.593   66.744  222.348 1.00 50.76  ? 71  PRO D O     1 
ATOM   12151 C CB    . PRO D  1 71  ? 4.554   64.424  221.519 1.00 40.48  ? 71  PRO D CB    1 
ATOM   12152 C CG    . PRO D  1 71  ? 5.348   64.961  222.655 1.00 48.42  ? 71  PRO D CG    1 
ATOM   12153 C CD    . PRO D  1 71  ? 6.008   66.217  222.142 1.00 51.31  ? 71  PRO D CD    1 
ATOM   12154 N N     . SER D  1 72  ? 1.634   65.670  220.614 1.00 47.03  ? 72  SER D N     1 
ATOM   12155 C CA    . SER D  1 72  ? 0.269   65.962  221.035 1.00 43.23  ? 72  SER D CA    1 
ATOM   12156 C C     . SER D  1 72  ? -0.111  65.109  222.239 1.00 47.50  ? 72  SER D C     1 
ATOM   12157 O O     . SER D  1 72  ? -1.046  65.434  222.972 1.00 45.51  ? 72  SER D O     1 
ATOM   12158 C CB    . SER D  1 72  ? -0.709  65.729  219.883 1.00 44.07  ? 72  SER D CB    1 
ATOM   12159 O OG    . SER D  1 72  ? -0.244  66.350  218.693 1.00 51.79  ? 72  SER D OG    1 
ATOM   12160 N N     . ALA D  1 73  ? 0.626   64.017  222.436 1.00 40.08  ? 73  ALA D N     1 
ATOM   12161 C CA    . ALA D  1 73  ? 0.427   63.134  223.584 1.00 39.42  ? 73  ALA D CA    1 
ATOM   12162 C C     . ALA D  1 73  ? 1.617   62.199  223.788 1.00 42.00  ? 73  ALA D C     1 
ATOM   12163 O O     . ALA D  1 73  ? 2.330   61.871  222.841 1.00 37.68  ? 73  ALA D O     1 
ATOM   12164 C CB    . ALA D  1 73  ? -0.846  62.324  223.413 1.00 40.69  ? 73  ALA D CB    1 
ATOM   12165 N N     . ILE D  1 74  ? 1.820   61.771  225.030 1.00 40.30  ? 74  ILE D N     1 
ATOM   12166 C CA    . ILE D  1 74  ? 2.857   60.801  225.349 1.00 43.20  ? 74  ILE D CA    1 
ATOM   12167 C C     . ILE D  1 74  ? 2.232   59.546  225.942 1.00 40.73  ? 74  ILE D C     1 
ATOM   12168 O O     . ILE D  1 74  ? 1.454   59.625  226.890 1.00 42.10  ? 74  ILE D O     1 
ATOM   12169 C CB    . ILE D  1 74  ? 3.887   61.372  226.341 1.00 39.09  ? 74  ILE D CB    1 
ATOM   12170 C CG1   . ILE D  1 74  ? 4.546   62.622  225.763 1.00 42.78  ? 74  ILE D CG1   1 
ATOM   12171 C CG2   . ILE D  1 74  ? 4.941   60.328  226.677 1.00 38.19  ? 74  ILE D CG2   1 
ATOM   12172 C CD1   . ILE D  1 74  ? 5.499   63.288  226.716 1.00 45.68  ? 74  ILE D CD1   1 
ATOM   12173 N N     . ILE D  1 75  ? 2.568   58.390  225.381 1.00 41.34  ? 75  ILE D N     1 
ATOM   12174 C CA    . ILE D  1 75  ? 1.997   57.127  225.844 1.00 36.65  ? 75  ILE D CA    1 
ATOM   12175 C C     . ILE D  1 75  ? 3.095   56.180  226.316 1.00 39.99  ? 75  ILE D C     1 
ATOM   12176 O O     . ILE D  1 75  ? 4.094   55.990  225.628 1.00 39.28  ? 75  ILE D O     1 
ATOM   12177 C CB    . ILE D  1 75  ? 1.169   56.449  224.740 1.00 35.94  ? 75  ILE D CB    1 
ATOM   12178 C CG1   . ILE D  1 75  ? 0.034   57.372  224.291 1.00 38.98  ? 75  ILE D CG1   1 
ATOM   12179 C CG2   . ILE D  1 75  ? 0.609   55.123  225.228 1.00 40.70  ? 75  ILE D CG2   1 
ATOM   12180 C CD1   . ILE D  1 75  ? -0.430  57.128  222.874 1.00 40.28  ? 75  ILE D CD1   1 
ATOM   12181 N N     . LEU D  1 76  ? 2.909   55.601  227.498 1.00 41.49  ? 76  LEU D N     1 
ATOM   12182 C CA    . LEU D  1 76  ? 3.865   54.647  228.044 1.00 37.20  ? 76  LEU D CA    1 
ATOM   12183 C C     . LEU D  1 76  ? 3.246   53.257  228.169 1.00 42.35  ? 76  LEU D C     1 
ATOM   12184 O O     . LEU D  1 76  ? 2.728   52.899  229.229 1.00 45.99  ? 76  LEU D O     1 
ATOM   12185 C CB    . LEU D  1 76  ? 4.379   55.111  229.413 1.00 46.51  ? 76  LEU D CB    1 
ATOM   12186 C CG    . LEU D  1 76  ? 5.467   56.192  229.507 1.00 45.67  ? 76  LEU D CG    1 
ATOM   12187 C CD1   . LEU D  1 76  ? 4.998   57.520  228.945 1.00 41.64  ? 76  LEU D CD1   1 
ATOM   12188 C CD2   . LEU D  1 76  ? 5.908   56.362  230.951 1.00 49.46  ? 76  LEU D CD2   1 
ATOM   12189 N N     . PRO D  1 77  ? 3.298   52.468  227.085 1.00 40.59  ? 77  PRO D N     1 
ATOM   12190 C CA    . PRO D  1 77  ? 2.776   51.097  227.112 1.00 33.18  ? 77  PRO D CA    1 
ATOM   12191 C C     . PRO D  1 77  ? 3.529   50.228  228.112 1.00 40.22  ? 77  PRO D C     1 
ATOM   12192 O O     . PRO D  1 77  ? 4.735   50.403  228.289 1.00 37.67  ? 77  PRO D O     1 
ATOM   12193 C CB    . PRO D  1 77  ? 2.995   50.605  225.677 1.00 31.64  ? 77  PRO D CB    1 
ATOM   12194 C CG    . PRO D  1 77  ? 4.062   51.488  225.124 1.00 36.71  ? 77  PRO D CG    1 
ATOM   12195 C CD    . PRO D  1 77  ? 3.854   52.821  225.769 1.00 36.00  ? 77  PRO D CD    1 
ATOM   12196 N N     . GLY D  1 78  ? 2.817   49.312  228.761 1.00 39.11  ? 78  GLY D N     1 
ATOM   12197 C CA    . GLY D  1 78  ? 3.402   48.485  229.799 1.00 33.75  ? 78  GLY D CA    1 
ATOM   12198 C C     . GLY D  1 78  ? 3.500   47.022  229.413 1.00 38.07  ? 78  GLY D C     1 
ATOM   12199 O O     . GLY D  1 78  ? 3.867   46.179  230.230 1.00 36.07  ? 78  GLY D O     1 
ATOM   12200 N N     . SER D  1 79  ? 3.177   46.722  228.160 1.00 35.37  ? 79  SER D N     1 
ATOM   12201 C CA    . SER D  1 79  ? 3.238   45.356  227.652 1.00 31.53  ? 79  SER D CA    1 
ATOM   12202 C C     . SER D  1 79  ? 3.372   45.369  226.136 1.00 29.89  ? 79  SER D C     1 
ATOM   12203 O O     . SER D  1 79  ? 3.163   46.403  225.502 1.00 32.82  ? 79  SER D O     1 
ATOM   12204 C CB    . SER D  1 79  ? 1.996   44.566  228.069 1.00 31.04  ? 79  SER D CB    1 
ATOM   12205 O OG    . SER D  1 79  ? 0.882   44.922  227.267 1.00 33.08  ? 79  SER D OG    1 
ATOM   12206 N N     . LYS D  1 80  ? 3.714   44.227  225.549 1.00 31.91  ? 80  LYS D N     1 
ATOM   12207 C CA    . LYS D  1 80  ? 3.817   44.150  224.096 1.00 33.07  ? 80  LYS D CA    1 
ATOM   12208 C C     . LYS D  1 80  ? 2.431   44.277  223.461 1.00 35.14  ? 80  LYS D C     1 
ATOM   12209 O O     . LYS D  1 80  ? 2.293   44.783  222.348 1.00 36.12  ? 80  LYS D O     1 
ATOM   12210 C CB    . LYS D  1 80  ? 4.501   42.849  223.657 1.00 32.39  ? 80  LYS D CB    1 
ATOM   12211 C CG    . LYS D  1 80  ? 3.754   41.568  224.003 1.00 35.29  ? 80  LYS D CG    1 
ATOM   12212 C CD    . LYS D  1 80  ? 4.531   40.346  223.521 1.00 35.42  ? 80  LYS D CD    1 
ATOM   12213 C CE    . LYS D  1 80  ? 3.721   39.064  223.652 1.00 30.41  ? 80  LYS D CE    1 
ATOM   12214 N NZ    . LYS D  1 80  ? 3.434   38.727  225.073 1.00 34.81  ? 80  LYS D NZ    1 
ATOM   12215 N N     . GLU D  1 81  ? 1.406   43.835  224.184 1.00 36.87  ? 81  GLU D N     1 
ATOM   12216 C CA    . GLU D  1 81  ? 0.030   43.971  223.716 1.00 35.93  ? 81  GLU D CA    1 
ATOM   12217 C C     . GLU D  1 81  ? -0.403  45.434  223.723 1.00 31.10  ? 81  GLU D C     1 
ATOM   12218 O O     . GLU D  1 81  ? -1.016  45.912  222.767 1.00 32.21  ? 81  GLU D O     1 
ATOM   12219 C CB    . GLU D  1 81  ? -0.926  43.137  224.571 1.00 29.57  ? 81  GLU D CB    1 
ATOM   12220 C CG    . GLU D  1 81  ? -0.796  41.636  224.367 1.00 32.22  ? 81  GLU D CG    1 
ATOM   12221 C CD    . GLU D  1 81  ? 0.350   41.038  225.154 1.00 32.68  ? 81  GLU D CD    1 
ATOM   12222 O OE1   . GLU D  1 81  ? 0.832   41.700  226.096 1.00 38.27  ? 81  GLU D OE1   1 
ATOM   12223 O OE2   . GLU D  1 81  ? 0.768   39.904  224.835 1.00 32.35  ? 81  GLU D OE2   1 
ATOM   12224 N N     . GLU D  1 82  ? -0.082  46.140  224.803 1.00 28.17  ? 82  GLU D N     1 
ATOM   12225 C CA    . GLU D  1 82  ? -0.387  47.566  224.898 1.00 29.26  ? 82  GLU D CA    1 
ATOM   12226 C C     . GLU D  1 82  ? 0.365   48.353  223.830 1.00 35.05  ? 82  GLU D C     1 
ATOM   12227 O O     . GLU D  1 82  ? -0.156  49.327  223.283 1.00 32.48  ? 82  GLU D O     1 
ATOM   12228 C CB    . GLU D  1 82  ? -0.044  48.111  226.285 1.00 36.05  ? 82  GLU D CB    1 
ATOM   12229 C CG    . GLU D  1 82  ? -1.043  47.749  227.377 1.00 38.30  ? 82  GLU D CG    1 
ATOM   12230 C CD    . GLU D  1 82  ? -0.779  48.489  228.678 1.00 42.89  ? 82  GLU D CD    1 
ATOM   12231 O OE1   . GLU D  1 82  ? -0.063  49.513  228.651 1.00 39.21  ? 82  GLU D OE1   1 
ATOM   12232 O OE2   . GLU D  1 82  ? -1.284  48.043  229.730 1.00 49.87  ? 82  GLU D OE2   1 
ATOM   12233 N N     . LEU D  1 83  ? 1.589   47.921  223.538 1.00 32.24  ? 83  LEU D N     1 
ATOM   12234 C CA    . LEU D  1 83  ? 2.404   48.550  222.505 1.00 34.03  ? 83  LEU D CA    1 
ATOM   12235 C C     . LEU D  1 83  ? 1.792   48.326  221.128 1.00 32.74  ? 83  LEU D C     1 
ATOM   12236 O O     . LEU D  1 83  ? 1.741   49.241  220.305 1.00 32.96  ? 83  LEU D O     1 
ATOM   12237 C CB    . LEU D  1 83  ? 3.838   48.010  222.554 1.00 31.66  ? 83  LEU D CB    1 
ATOM   12238 C CG    . LEU D  1 83  ? 4.827   48.459  221.475 1.00 31.51  ? 83  LEU D CG    1 
ATOM   12239 C CD1   . LEU D  1 83  ? 4.893   49.975  221.371 1.00 25.03  ? 83  LEU D CD1   1 
ATOM   12240 C CD2   . LEU D  1 83  ? 6.204   47.881  221.761 1.00 28.52  ? 83  LEU D CD2   1 
ATOM   12241 N N     . SER D  1 84  ? 1.323   47.103  220.893 1.00 32.56  ? 84  SER D N     1 
ATOM   12242 C CA    . SER D  1 84  ? 0.655   46.755  219.643 1.00 32.66  ? 84  SER D CA    1 
ATOM   12243 C C     . SER D  1 84  ? -0.594  47.607  219.420 1.00 28.22  ? 84  SER D C     1 
ATOM   12244 O O     . SER D  1 84  ? -0.800  48.149  218.335 1.00 27.91  ? 84  SER D O     1 
ATOM   12245 C CB    . SER D  1 84  ? 0.282   45.268  219.630 1.00 28.35  ? 84  SER D CB    1 
ATOM   12246 O OG    . SER D  1 84  ? -0.605  44.974  218.570 1.00 33.53  ? 84  SER D OG    1 
ATOM   12247 N N     . ASN D  1 85  ? -1.422  47.722  220.454 1.00 30.98  ? 85  ASN D N     1 
ATOM   12248 C CA    . ASN D  1 85  ? -2.658  48.498  220.373 1.00 32.92  ? 85  ASN D CA    1 
ATOM   12249 C C     . ASN D  1 85  ? -2.408  50.004  220.311 1.00 34.77  ? 85  ASN D C     1 
ATOM   12250 O O     . ASN D  1 85  ? -3.164  50.741  219.675 1.00 34.48  ? 85  ASN D O     1 
ATOM   12251 C CB    . ASN D  1 85  ? -3.567  48.168  221.558 1.00 29.85  ? 85  ASN D CB    1 
ATOM   12252 C CG    . ASN D  1 85  ? -4.178  46.780  221.452 1.00 37.52  ? 85  ASN D CG    1 
ATOM   12253 O OD1   . ASN D  1 85  ? -4.358  46.253  220.356 1.00 33.04  ? 85  ASN D OD1   1 
ATOM   12254 N ND2   . ASN D  1 85  ? -4.505  46.185  222.592 1.00 34.68  ? 85  ASN D ND2   1 
ATOM   12255 N N     . THR D  1 86  ? -1.351  50.458  220.977 1.00 36.22  ? 86  THR D N     1 
ATOM   12256 C CA    . THR D  1 86  ? -0.980  51.868  220.941 1.00 33.24  ? 86  THR D CA    1 
ATOM   12257 C C     . THR D  1 86  ? -0.680  52.298  219.509 1.00 34.51  ? 86  THR D C     1 
ATOM   12258 O O     . THR D  1 86  ? -1.146  53.340  219.054 1.00 35.31  ? 86  THR D O     1 
ATOM   12259 C CB    . THR D  1 86  ? 0.243   52.156  221.829 1.00 34.47  ? 86  THR D CB    1 
ATOM   12260 O OG1   . THR D  1 86  ? -0.089  51.897  223.199 1.00 31.65  ? 86  THR D OG1   1 
ATOM   12261 C CG2   . THR D  1 86  ? 0.679   53.609  221.682 1.00 32.14  ? 86  THR D CG2   1 
ATOM   12262 N N     . ILE D  1 87  ? 0.094   51.475  218.808 1.00 29.08  ? 87  ILE D N     1 
ATOM   12263 C CA    . ILE D  1 87  ? 0.404   51.713  217.405 1.00 29.46  ? 87  ILE D CA    1 
ATOM   12264 C C     . ILE D  1 87  ? -0.868  51.769  216.561 1.00 37.86  ? 87  ILE D C     1 
ATOM   12265 O O     . ILE D  1 87  ? -1.023  52.640  215.704 1.00 37.19  ? 87  ILE D O     1 
ATOM   12266 C CB    . ILE D  1 87  ? 1.342   50.621  216.849 1.00 28.60  ? 87  ILE D CB    1 
ATOM   12267 C CG1   . ILE D  1 87  ? 2.745   50.766  217.440 1.00 30.45  ? 87  ILE D CG1   1 
ATOM   12268 C CG2   . ILE D  1 87  ? 1.401   50.690  215.332 1.00 32.71  ? 87  ILE D CG2   1 
ATOM   12269 C CD1   . ILE D  1 87  ? 3.648   49.576  217.175 1.00 30.54  ? 87  ILE D CD1   1 
ATOM   12270 N N     . ARG D  1 88  ? -1.779  50.837  216.816 1.00 31.26  ? 88  ARG D N     1 
ATOM   12271 C CA    . ARG D  1 88  ? -3.048  50.783  216.099 1.00 35.33  ? 88  ARG D CA    1 
ATOM   12272 C C     . ARG D  1 88  ? -3.864  52.064  216.282 1.00 35.22  ? 88  ARG D C     1 
ATOM   12273 O O     . ARG D  1 88  ? -4.345  52.645  215.307 1.00 39.75  ? 88  ARG D O     1 
ATOM   12274 C CB    . ARG D  1 88  ? -3.865  49.573  216.555 1.00 34.62  ? 88  ARG D CB    1 
ATOM   12275 C CG    . ARG D  1 88  ? -3.297  48.225  216.123 1.00 34.34  ? 88  ARG D CG    1 
ATOM   12276 C CD    . ARG D  1 88  ? -4.225  47.065  216.488 1.00 42.26  ? 88  ARG D CD    1 
ATOM   12277 N NE    . ARG D  1 88  ? -5.622  47.360  216.173 1.00 44.97  ? 88  ARG D NE    1 
ATOM   12278 C CZ    . ARG D  1 88  ? -6.536  47.701  217.076 1.00 45.84  ? 88  ARG D CZ    1 
ATOM   12279 N NH1   . ARG D  1 88  ? -6.211  47.784  218.358 1.00 37.99  ? 88  ARG D NH1   1 
ATOM   12280 N NH2   . ARG D  1 88  ? -7.775  47.961  216.693 1.00 46.28  ? 88  ARG D NH2   1 
ATOM   12281 N N     . CYS D  1 89  ? -4.009  52.500  217.531 1.00 31.36  ? 89  CYS D N     1 
ATOM   12282 C CA    . CYS D  1 89  ? -4.825  53.671  217.859 1.00 36.80  ? 89  CYS D CA    1 
ATOM   12283 C C     . CYS D  1 89  ? -4.269  54.972  217.288 1.00 42.98  ? 89  CYS D C     1 
ATOM   12284 O O     . CYS D  1 89  ? -5.010  55.733  216.657 1.00 41.26  ? 89  CYS D O     1 
ATOM   12285 C CB    . CYS D  1 89  ? -4.976  53.810  219.375 1.00 35.84  ? 89  CYS D CB    1 
ATOM   12286 S SG    . CYS D  1 89  ? -6.042  52.588  220.148 1.00 43.32  ? 89  CYS D SG    1 
ATOM   12287 N N     . ILE D  1 90  ? -2.985  55.238  217.530 1.00 37.02  ? 90  ILE D N     1 
ATOM   12288 C CA    . ILE D  1 90  ? -2.306  56.412  216.982 1.00 40.34  ? 90  ILE D CA    1 
ATOM   12289 C C     . ILE D  1 90  ? -2.545  56.540  215.477 1.00 44.43  ? 90  ILE D C     1 
ATOM   12290 O O     . ILE D  1 90  ? -2.828  57.631  214.966 1.00 45.33  ? 90  ILE D O     1 
ATOM   12291 C CB    . ILE D  1 90  ? -0.778  56.354  217.226 1.00 38.68  ? 90  ILE D CB    1 
ATOM   12292 C CG1   . ILE D  1 90  ? -0.446  56.401  218.717 1.00 35.09  ? 90  ILE D CG1   1 
ATOM   12293 C CG2   . ILE D  1 90  ? -0.082  57.497  216.505 1.00 39.30  ? 90  ILE D CG2   1 
ATOM   12294 C CD1   . ILE D  1 90  ? 1.026   56.177  219.002 1.00 35.98  ? 90  ILE D CD1   1 
ATOM   12295 N N     . ARG D  1 91  ? -2.475  55.412  214.780 1.00 42.75  ? 91  ARG D N     1 
ATOM   12296 C CA    . ARG D  1 91  ? -2.566  55.403  213.336 1.00 48.68  ? 91  ARG D CA    1 
ATOM   12297 C C     . ARG D  1 91  ? -3.979  55.667  212.796 1.00 53.01  ? 91  ARG D C     1 
ATOM   12298 O O     . ARG D  1 91  ? -4.132  56.203  211.700 1.00 57.07  ? 91  ARG D O     1 
ATOM   12299 C CB    . ARG D  1 91  ? -2.046  54.065  212.831 1.00 51.36  ? 91  ARG D CB    1 
ATOM   12300 C CG    . ARG D  1 91  ? -2.203  53.871  211.364 1.00 61.60  ? 91  ARG D CG    1 
ATOM   12301 C CD    . ARG D  1 91  ? -1.649  52.532  210.978 1.00 51.13  ? 91  ARG D CD    1 
ATOM   12302 N NE    . ARG D  1 91  ? -1.671  52.351  209.535 1.00 50.66  ? 91  ARG D NE    1 
ATOM   12303 C CZ    . ARG D  1 91  ? -1.175  51.288  208.912 1.00 40.53  ? 91  ARG D CZ    1 
ATOM   12304 N NH1   . ARG D  1 91  ? -1.231  51.200  207.590 1.00 53.57  ? 91  ARG D NH1   1 
ATOM   12305 N NH2   . ARG D  1 91  ? -0.616  50.309  209.608 1.00 52.66  ? 91  ARG D NH2   1 
ATOM   12306 N N     . LYS D  1 92  ? -5.001  55.297  213.567 1.00 50.13  ? 92  LYS D N     1 
ATOM   12307 C CA    . LYS D  1 92  ? -6.391  55.578  213.194 1.00 54.26  ? 92  LYS D CA    1 
ATOM   12308 C C     . LYS D  1 92  ? -6.638  57.079  213.058 1.00 50.05  ? 92  LYS D C     1 
ATOM   12309 O O     . LYS D  1 92  ? -7.572  57.505  212.384 1.00 58.51  ? 92  LYS D O     1 
ATOM   12310 C CB    . LYS D  1 92  ? -7.369  54.996  214.218 1.00 52.83  ? 92  LYS D CB    1 
ATOM   12311 C CG    . LYS D  1 92  ? -7.578  53.484  214.120 1.00 55.68  ? 92  LYS D CG    1 
ATOM   12312 C CD    . LYS D  1 92  ? -8.788  53.045  214.944 1.00 59.48  ? 92  LYS D CD    1 
ATOM   12313 C CE    . LYS D  1 92  ? -8.891  51.529  215.066 1.00 62.82  ? 92  LYS D CE    1 
ATOM   12314 N NZ    . LYS D  1 92  ? -9.497  51.131  216.372 1.00 66.99  ? 92  LYS D NZ    1 
ATOM   12315 N N     . GLY D  1 93  ? -5.795  57.868  213.719 1.00 51.69  ? 93  GLY D N     1 
ATOM   12316 C CA    . GLY D  1 93  ? -5.793  59.309  213.572 1.00 50.53  ? 93  GLY D CA    1 
ATOM   12317 C C     . GLY D  1 93  ? -4.826  59.738  212.484 1.00 54.44  ? 93  GLY D C     1 
ATOM   12318 O O     . GLY D  1 93  ? -4.479  58.954  211.603 1.00 52.62  ? 93  GLY D O     1 
ATOM   12319 N N     . SER D  1 94  ? -4.379  60.986  212.554 1.00 56.53  ? 94  SER D N     1 
ATOM   12320 C CA    . SER D  1 94  ? -3.530  61.558  211.517 1.00 63.49  ? 94  SER D CA    1 
ATOM   12321 C C     . SER D  1 94  ? -2.050  61.485  211.874 1.00 55.98  ? 94  SER D C     1 
ATOM   12322 O O     . SER D  1 94  ? -1.187  61.804  211.054 1.00 62.53  ? 94  SER D O     1 
ATOM   12323 C CB    . SER D  1 94  ? -3.928  63.013  211.269 1.00 67.03  ? 94  SER D CB    1 
ATOM   12324 O OG    . SER D  1 94  ? -3.904  63.748  212.483 1.00 62.64  ? 94  SER D OG    1 
ATOM   12325 N N     . TRP D  1 95  ? -1.764  61.046  213.093 1.00 50.86  ? 95  TRP D N     1 
ATOM   12326 C CA    . TRP D  1 95  ? -0.449  61.247  213.692 1.00 49.18  ? 95  TRP D CA    1 
ATOM   12327 C C     . TRP D  1 95  ? 0.679   60.378  213.160 1.00 48.45  ? 95  TRP D C     1 
ATOM   12328 O O     . TRP D  1 95  ? 0.499   59.207  212.821 1.00 47.37  ? 95  TRP D O     1 
ATOM   12329 C CB    . TRP D  1 95  ? -0.535  61.036  215.201 1.00 49.35  ? 95  TRP D CB    1 
ATOM   12330 C CG    . TRP D  1 95  ? -1.414  62.011  215.880 1.00 52.24  ? 95  TRP D CG    1 
ATOM   12331 C CD1   . TRP D  1 95  ? -1.123  63.309  216.179 1.00 51.36  ? 95  TRP D CD1   1 
ATOM   12332 C CD2   . TRP D  1 95  ? -2.739  61.773  216.359 1.00 52.44  ? 95  TRP D CD2   1 
ATOM   12333 N NE1   . TRP D  1 95  ? -2.189  63.896  216.815 1.00 57.72  ? 95  TRP D NE1   1 
ATOM   12334 C CE2   . TRP D  1 95  ? -3.194  62.973  216.938 1.00 57.08  ? 95  TRP D CE2   1 
ATOM   12335 C CE3   . TRP D  1 95  ? -3.586  60.660  216.355 1.00 45.72  ? 95  TRP D CE3   1 
ATOM   12336 C CZ2   . TRP D  1 95  ? -4.460  63.093  217.508 1.00 55.16  ? 95  TRP D CZ2   1 
ATOM   12337 C CZ3   . TRP D  1 95  ? -4.841  60.780  216.920 1.00 57.09  ? 95  TRP D CZ3   1 
ATOM   12338 C CH2   . TRP D  1 95  ? -5.267  61.988  217.489 1.00 64.61  ? 95  TRP D CH2   1 
ATOM   12339 N N     . THR D  1 96  ? 1.854   60.994  213.104 1.00 41.82  ? 96  THR D N     1 
ATOM   12340 C CA    . THR D  1 96  ? 3.113   60.304  212.896 1.00 45.20  ? 96  THR D CA    1 
ATOM   12341 C C     . THR D  1 96  ? 3.538   59.606  214.182 1.00 40.10  ? 96  THR D C     1 
ATOM   12342 O O     . THR D  1 96  ? 3.450   60.187  215.262 1.00 43.12  ? 96  THR D O     1 
ATOM   12343 C CB    . THR D  1 96  ? 4.219   61.286  212.463 1.00 48.19  ? 96  THR D CB    1 
ATOM   12344 O OG1   . THR D  1 96  ? 3.905   61.825  211.173 1.00 46.74  ? 96  THR D OG1   1 
ATOM   12345 C CG2   . THR D  1 96  ? 5.576   60.599  212.415 1.00 43.23  ? 96  THR D CG2   1 
ATOM   12346 N N     . ILE D  1 97  ? 3.996   58.365  214.076 1.00 35.24  ? 97  ILE D N     1 
ATOM   12347 C CA    . ILE D  1 97  ? 4.469   57.639  215.249 1.00 33.73  ? 97  ILE D CA    1 
ATOM   12348 C C     . ILE D  1 97  ? 5.936   57.947  215.532 1.00 35.61  ? 97  ILE D C     1 
ATOM   12349 O O     . ILE D  1 97  ? 6.760   57.977  214.619 1.00 33.91  ? 97  ILE D O     1 
ATOM   12350 C CB    . ILE D  1 97  ? 4.295   56.120  215.076 1.00 35.09  ? 97  ILE D CB    1 
ATOM   12351 C CG1   . ILE D  1 97  ? 2.810   55.759  215.058 1.00 32.63  ? 97  ILE D CG1   1 
ATOM   12352 C CG2   . ILE D  1 97  ? 5.010   55.361  216.184 1.00 28.33  ? 97  ILE D CG2   1 
ATOM   12353 C CD1   . ILE D  1 97  ? 2.537   54.292  214.835 1.00 37.33  ? 97  ILE D CD1   1 
ATOM   12354 N N     . ARG D  1 98  ? 6.254   58.194  216.798 1.00 32.70  ? 98  ARG D N     1 
ATOM   12355 C CA    . ARG D  1 98  ? 7.641   58.298  217.231 1.00 34.34  ? 98  ARG D CA    1 
ATOM   12356 C C     . ARG D  1 98  ? 7.882   57.350  218.395 1.00 34.43  ? 98  ARG D C     1 
ATOM   12357 O O     . ARG D  1 98  ? 7.134   57.353  219.370 1.00 35.41  ? 98  ARG D O     1 
ATOM   12358 C CB    . ARG D  1 98  ? 7.992   59.733  217.631 1.00 36.91  ? 98  ARG D CB    1 
ATOM   12359 C CG    . ARG D  1 98  ? 8.280   60.658  216.459 1.00 38.90  ? 98  ARG D CG    1 
ATOM   12360 C CD    . ARG D  1 98  ? 9.561   60.256  215.742 1.00 33.97  ? 98  ARG D CD    1 
ATOM   12361 N NE    . ARG D  1 98  ? 9.790   61.052  214.538 1.00 38.46  ? 98  ARG D NE    1 
ATOM   12362 C CZ    . ARG D  1 98  ? 9.393   60.703  213.318 1.00 43.24  ? 98  ARG D CZ    1 
ATOM   12363 N NH1   . ARG D  1 98  ? 8.745   59.562  213.129 1.00 40.67  ? 98  ARG D NH1   1 
ATOM   12364 N NH2   . ARG D  1 98  ? 9.647   61.495  212.286 1.00 40.74  ? 98  ARG D NH2   1 
ATOM   12365 N N     . LEU D  1 99  ? 8.921   56.529  218.280 1.00 29.41  ? 99  LEU D N     1 
ATOM   12366 C CA    . LEU D  1 99  ? 9.312   55.632  219.360 1.00 32.37  ? 99  LEU D CA    1 
ATOM   12367 C C     . LEU D  1 99  ? 10.526  56.199  220.076 1.00 31.70  ? 99  LEU D C     1 
ATOM   12368 O O     . LEU D  1 99  ? 11.438  56.717  219.439 1.00 32.80  ? 99  LEU D O     1 
ATOM   12369 C CB    . LEU D  1 99  ? 9.628   54.232  218.824 1.00 36.20  ? 99  LEU D CB    1 
ATOM   12370 C CG    . LEU D  1 99  ? 8.566   53.514  217.986 1.00 35.37  ? 99  LEU D CG    1 
ATOM   12371 C CD1   . LEU D  1 99  ? 9.214   52.388  217.197 1.00 33.87  ? 99  LEU D CD1   1 
ATOM   12372 C CD2   . LEU D  1 99  ? 7.427   52.987  218.855 1.00 31.38  ? 99  LEU D CD2   1 
ATOM   12373 N N     . ARG D  1 100 ? 10.538  56.112  221.401 1.00 30.56  ? 100 ARG D N     1 
ATOM   12374 C CA    . ARG D  1 100 ? 11.706  56.524  222.170 1.00 37.43  ? 100 ARG D CA    1 
ATOM   12375 C C     . ARG D  1 100 ? 12.046  55.498  223.234 1.00 39.49  ? 100 ARG D C     1 
ATOM   12376 O O     . ARG D  1 100 ? 11.185  55.084  224.009 1.00 34.35  ? 100 ARG D O     1 
ATOM   12377 C CB    . ARG D  1 100 ? 11.484  57.893  222.821 1.00 41.79  ? 100 ARG D CB    1 
ATOM   12378 C CG    . ARG D  1 100 ? 12.722  58.427  223.533 1.00 34.92  ? 100 ARG D CG    1 
ATOM   12379 C CD    . ARG D  1 100 ? 12.544  59.871  223.981 1.00 39.11  ? 100 ARG D CD    1 
ATOM   12380 N NE    . ARG D  1 100 ? 11.626  60.001  225.109 1.00 48.10  ? 100 ARG D NE    1 
ATOM   12381 C CZ    . ARG D  1 100 ? 11.223  61.166  225.606 1.00 48.11  ? 100 ARG D CZ    1 
ATOM   12382 N NH1   . ARG D  1 100 ? 10.389  61.200  226.636 1.00 50.43  ? 100 ARG D NH1   1 
ATOM   12383 N NH2   . ARG D  1 100 ? 11.652  62.299  225.068 1.00 48.01  ? 100 ARG D NH2   1 
ATOM   12384 N N     . SER D  1 101 ? 13.307  55.084  223.260 1.00 32.56  ? 101 SER D N     1 
ATOM   12385 C CA    . SER D  1 101 ? 13.788  54.162  224.281 1.00 33.51  ? 101 SER D CA    1 
ATOM   12386 C C     . SER D  1 101 ? 14.644  54.906  225.299 1.00 39.16  ? 101 SER D C     1 
ATOM   12387 O O     . SER D  1 101 ? 14.208  55.169  226.420 1.00 41.67  ? 101 SER D O     1 
ATOM   12388 C CB    . SER D  1 101 ? 14.584  53.021  223.649 1.00 31.17  ? 101 SER D CB    1 
ATOM   12389 O OG    . SER D  1 101 ? 15.062  52.128  224.636 1.00 33.53  ? 101 SER D OG    1 
ATOM   12390 N N     . GLY D  1 102 ? 15.865  55.245  224.898 1.00 39.27  ? 102 GLY D N     1 
ATOM   12391 C CA    . GLY D  1 102 ? 16.772  55.981  225.759 1.00 34.86  ? 102 GLY D CA    1 
ATOM   12392 C C     . GLY D  1 102 ? 16.843  57.450  225.390 1.00 38.07  ? 102 GLY D C     1 
ATOM   12393 O O     . GLY D  1 102 ? 17.317  58.273  226.174 1.00 40.06  ? 102 GLY D O     1 
ATOM   12394 N N     . GLY D  1 103 ? 16.377  57.774  224.187 1.00 37.82  ? 103 GLY D N     1 
ATOM   12395 C CA    . GLY D  1 103 ? 16.333  59.148  223.716 1.00 33.99  ? 103 GLY D CA    1 
ATOM   12396 C C     . GLY D  1 103 ? 17.691  59.742  223.389 1.00 41.00  ? 103 GLY D C     1 
ATOM   12397 O O     . GLY D  1 103 ? 17.875  60.957  223.455 1.00 35.98  ? 103 GLY D O     1 
ATOM   12398 N N     . HIS D  1 104 ? 18.640  58.889  223.018 1.00 33.30  ? 104 HIS D N     1 
ATOM   12399 C CA    . HIS D  1 104 ? 20.009  59.333  222.773 1.00 32.68  ? 104 HIS D CA    1 
ATOM   12400 C C     . HIS D  1 104 ? 20.280  59.705  221.324 1.00 34.33  ? 104 HIS D C     1 
ATOM   12401 O O     . HIS D  1 104 ? 21.431  59.930  220.952 1.00 37.84  ? 104 HIS D O     1 
ATOM   12402 C CB    . HIS D  1 104 ? 21.003  58.255  223.205 1.00 35.32  ? 104 HIS D CB    1 
ATOM   12403 C CG    . HIS D  1 104 ? 21.537  58.451  224.589 1.00 37.08  ? 104 HIS D CG    1 
ATOM   12404 N ND1   . HIS D  1 104 ? 22.637  59.241  224.855 1.00 40.94  ? 104 HIS D ND1   1 
ATOM   12405 C CD2   . HIS D  1 104 ? 21.122  57.966  225.782 1.00 37.73  ? 104 HIS D CD2   1 
ATOM   12406 C CE1   . HIS D  1 104 ? 22.870  59.236  226.156 1.00 39.25  ? 104 HIS D CE1   1 
ATOM   12407 N NE2   . HIS D  1 104 ? 21.971  58.466  226.741 1.00 44.51  ? 104 HIS D NE2   1 
ATOM   12408 N N     . SER D  1 105 ? 19.226  59.762  220.515 1.00 36.44  ? 105 SER D N     1 
ATOM   12409 C CA    . SER D  1 105 ? 19.348  60.186  219.125 1.00 35.90  ? 105 SER D CA    1 
ATOM   12410 C C     . SER D  1 105 ? 20.119  61.496  219.028 1.00 38.87  ? 105 SER D C     1 
ATOM   12411 O O     . SER D  1 105 ? 19.711  62.512  219.596 1.00 39.93  ? 105 SER D O     1 
ATOM   12412 C CB    . SER D  1 105 ? 17.969  60.340  218.483 1.00 34.96  ? 105 SER D CB    1 
ATOM   12413 O OG    . SER D  1 105 ? 18.076  60.908  217.189 1.00 34.83  ? 105 SER D OG    1 
ATOM   12414 N N     . TYR D  1 106 ? 21.247  61.456  218.324 1.00 36.95  ? 106 TYR D N     1 
ATOM   12415 C CA    . TYR D  1 106 ? 22.089  62.632  218.142 1.00 37.17  ? 106 TYR D CA    1 
ATOM   12416 C C     . TYR D  1 106 ? 21.313  63.768  217.482 1.00 43.58  ? 106 TYR D C     1 
ATOM   12417 O O     . TYR D  1 106 ? 21.619  64.944  217.683 1.00 42.20  ? 106 TYR D O     1 
ATOM   12418 C CB    . TYR D  1 106 ? 23.318  62.280  217.306 1.00 38.68  ? 106 TYR D CB    1 
ATOM   12419 C CG    . TYR D  1 106 ? 24.330  61.406  218.017 1.00 31.37  ? 106 TYR D CG    1 
ATOM   12420 C CD1   . TYR D  1 106 ? 24.253  61.186  219.387 1.00 32.92  ? 106 TYR D CD1   1 
ATOM   12421 C CD2   . TYR D  1 106 ? 25.365  60.803  217.317 1.00 43.12  ? 106 TYR D CD2   1 
ATOM   12422 C CE1   . TYR D  1 106 ? 25.184  60.392  220.040 1.00 38.47  ? 106 TYR D CE1   1 
ATOM   12423 C CE2   . TYR D  1 106 ? 26.302  60.015  217.958 1.00 40.70  ? 106 TYR D CE2   1 
ATOM   12424 C CZ    . TYR D  1 106 ? 26.206  59.809  219.320 1.00 38.27  ? 106 TYR D CZ    1 
ATOM   12425 O OH    . TYR D  1 106 ? 27.133  59.020  219.963 1.00 41.32  ? 106 TYR D OH    1 
ATOM   12426 N N     . GLU D  1 107 ? 20.300  63.404  216.701 1.00 40.67  ? 107 GLU D N     1 
ATOM   12427 C CA    . GLU D  1 107 ? 19.486  64.381  215.994 1.00 40.90  ? 107 GLU D CA    1 
ATOM   12428 C C     . GLU D  1 107 ? 18.065  64.472  216.552 1.00 34.50  ? 107 GLU D C     1 
ATOM   12429 O O     . GLU D  1 107 ? 17.178  65.031  215.902 1.00 40.59  ? 107 GLU D O     1 
ATOM   12430 C CB    . GLU D  1 107 ? 19.437  64.042  214.501 1.00 35.79  ? 107 GLU D CB    1 
ATOM   12431 C CG    . GLU D  1 107 ? 20.785  64.100  213.794 1.00 43.00  ? 107 GLU D CG    1 
ATOM   12432 C CD    . GLU D  1 107 ? 21.159  65.504  213.341 1.00 45.90  ? 107 GLU D CD    1 
ATOM   12433 O OE1   . GLU D  1 107 ? 20.660  66.484  213.935 1.00 46.17  ? 107 GLU D OE1   1 
ATOM   12434 O OE2   . GLU D  1 107 ? 21.949  65.624  212.382 1.00 47.34  ? 107 GLU D OE2   1 
ATOM   12435 N N     . GLY D  1 108 ? 17.851  63.919  217.745 1.00 36.20  ? 108 GLY D N     1 
ATOM   12436 C CA    . GLY D  1 108 ? 16.566  64.011  218.423 1.00 41.48  ? 108 GLY D CA    1 
ATOM   12437 C C     . GLY D  1 108 ? 15.398  63.379  217.688 1.00 42.45  ? 108 GLY D C     1 
ATOM   12438 O O     . GLY D  1 108 ? 14.247  63.769  217.880 1.00 38.78  ? 108 GLY D O     1 
ATOM   12439 N N     . LEU D  1 109 ? 15.696  62.380  216.865 1.00 37.93  ? 109 LEU D N     1 
ATOM   12440 C CA    . LEU D  1 109 ? 14.696  61.776  215.985 1.00 39.40  ? 109 LEU D CA    1 
ATOM   12441 C C     . LEU D  1 109 ? 13.670  60.903  216.710 1.00 38.37  ? 109 LEU D C     1 
ATOM   12442 O O     . LEU D  1 109 ? 12.718  60.424  216.093 1.00 42.31  ? 109 LEU D O     1 
ATOM   12443 C CB    . LEU D  1 109 ? 15.390  60.949  214.896 1.00 38.75  ? 109 LEU D CB    1 
ATOM   12444 C CG    . LEU D  1 109 ? 16.300  61.756  213.964 1.00 39.26  ? 109 LEU D CG    1 
ATOM   12445 C CD1   . LEU D  1 109 ? 16.796  60.923  212.796 1.00 34.65  ? 109 LEU D CD1   1 
ATOM   12446 C CD2   . LEU D  1 109 ? 15.582  63.001  213.464 1.00 37.01  ? 109 LEU D CD2   1 
ATOM   12447 N N     . SER D  1 110 ? 13.851  60.695  218.010 1.00 34.32  ? 110 SER D N     1 
ATOM   12448 C CA    . SER D  1 110 ? 12.922  59.861  218.767 1.00 35.64  ? 110 SER D CA    1 
ATOM   12449 C C     . SER D  1 110 ? 11.836  60.674  219.470 1.00 37.76  ? 110 SER D C     1 
ATOM   12450 O O     . SER D  1 110 ? 10.891  60.108  220.021 1.00 34.83  ? 110 SER D O     1 
ATOM   12451 C CB    . SER D  1 110 ? 13.677  59.021  219.797 1.00 32.81  ? 110 SER D CB    1 
ATOM   12452 O OG    . SER D  1 110 ? 14.516  59.833  220.600 1.00 36.90  ? 110 SER D OG    1 
ATOM   12453 N N     . TYR D  1 111 ? 11.967  61.996  219.450 1.00 37.49  ? 111 TYR D N     1 
ATOM   12454 C CA    . TYR D  1 111 ? 11.009  62.848  220.143 1.00 36.52  ? 111 TYR D CA    1 
ATOM   12455 C C     . TYR D  1 111 ? 10.722  64.147  219.392 1.00 33.42  ? 111 TYR D C     1 
ATOM   12456 O O     . TYR D  1 111 ? 10.174  65.089  219.962 1.00 39.23  ? 111 TYR D O     1 
ATOM   12457 C CB    . TYR D  1 111 ? 11.505  63.152  221.561 1.00 40.51  ? 111 TYR D CB    1 
ATOM   12458 C CG    . TYR D  1 111 ? 12.941  63.632  221.627 1.00 39.76  ? 111 TYR D CG    1 
ATOM   12459 C CD1   . TYR D  1 111 ? 13.258  64.963  221.394 1.00 45.60  ? 111 TYR D CD1   1 
ATOM   12460 C CD2   . TYR D  1 111 ? 13.976  62.755  221.931 1.00 41.30  ? 111 TYR D CD2   1 
ATOM   12461 C CE1   . TYR D  1 111 ? 14.565  65.409  221.454 1.00 43.73  ? 111 TYR D CE1   1 
ATOM   12462 C CE2   . TYR D  1 111 ? 15.290  63.192  221.993 1.00 42.40  ? 111 TYR D CE2   1 
ATOM   12463 C CZ    . TYR D  1 111 ? 15.576  64.520  221.754 1.00 45.13  ? 111 TYR D CZ    1 
ATOM   12464 O OH    . TYR D  1 111 ? 16.877  64.957  221.816 1.00 43.00  ? 111 TYR D OH    1 
ATOM   12465 N N     . THR D  1 112 ? 11.093  64.203  218.116 1.00 35.92  ? 112 THR D N     1 
ATOM   12466 C CA    . THR D  1 112 ? 10.735  65.341  217.272 1.00 38.48  ? 112 THR D CA    1 
ATOM   12467 C C     . THR D  1 112 ? 10.209  64.861  215.926 1.00 44.27  ? 112 THR D C     1 
ATOM   12468 O O     . THR D  1 112 ? 10.536  63.761  215.479 1.00 42.38  ? 112 THR D O     1 
ATOM   12469 C CB    . THR D  1 112 ? 11.927  66.298  217.022 1.00 42.02  ? 112 THR D CB    1 
ATOM   12470 O OG1   . THR D  1 112 ? 12.898  65.657  216.184 1.00 40.65  ? 112 THR D OG1   1 
ATOM   12471 C CG2   . THR D  1 112 ? 12.574  66.723  218.326 1.00 43.16  ? 112 THR D CG2   1 
ATOM   12472 N N     . SER D  1 113 ? 9.401   65.701  215.288 1.00 40.71  ? 113 SER D N     1 
ATOM   12473 C CA    . SER D  1 113 ? 8.828   65.401  213.980 1.00 42.74  ? 113 SER D CA    1 
ATOM   12474 C C     . SER D  1 113 ? 8.323   66.693  213.347 1.00 51.20  ? 113 SER D C     1 
ATOM   12475 O O     . SER D  1 113 ? 7.820   67.572  214.046 1.00 53.82  ? 113 SER D O     1 
ATOM   12476 C CB    . SER D  1 113 ? 7.697   64.377  214.105 1.00 46.65  ? 113 SER D CB    1 
ATOM   12477 O OG    . SER D  1 113 ? 6.980   64.233  212.890 1.00 41.89  ? 113 SER D OG    1 
ATOM   12478 N N     . ASP D  1 114 ? 8.459   66.823  212.030 1.00 45.30  ? 114 ASP D N     1 
ATOM   12479 C CA    . ASP D  1 114 ? 7.993   68.037  211.362 1.00 58.27  ? 114 ASP D CA    1 
ATOM   12480 C C     . ASP D  1 114 ? 6.510   67.945  211.009 1.00 56.38  ? 114 ASP D C     1 
ATOM   12481 O O     . ASP D  1 114 ? 5.966   68.816  210.330 1.00 58.59  ? 114 ASP D O     1 
ATOM   12482 C CB    . ASP D  1 114 ? 8.828   68.331  210.110 1.00 65.20  ? 114 ASP D CB    1 
ATOM   12483 C CG    . ASP D  1 114 ? 9.019   67.114  209.227 1.00 62.97  ? 114 ASP D CG    1 
ATOM   12484 O OD1   . ASP D  1 114 ? 8.026   66.411  208.942 1.00 63.72  ? 114 ASP D OD1   1 
ATOM   12485 O OD2   . ASP D  1 114 ? 10.170  66.863  208.808 1.00 74.55  ? 114 ASP D OD2   1 
ATOM   12486 N N     . THR D  1 115 ? 5.864   66.884  211.481 1.00 54.46  ? 115 THR D N     1 
ATOM   12487 C CA    . THR D  1 115 ? 4.418   66.729  211.365 1.00 51.49  ? 115 THR D CA    1 
ATOM   12488 C C     . THR D  1 115 ? 3.858   66.431  212.754 1.00 51.58  ? 115 THR D C     1 
ATOM   12489 O O     . THR D  1 115 ? 4.613   66.029  213.641 1.00 51.34  ? 115 THR D O     1 
ATOM   12490 C CB    . THR D  1 115 ? 4.041   65.603  210.379 1.00 52.21  ? 115 THR D CB    1 
ATOM   12491 O OG1   . THR D  1 115 ? 4.631   64.368  210.803 1.00 57.38  ? 115 THR D OG1   1 
ATOM   12492 C CG2   . THR D  1 115 ? 4.524   65.938  208.974 1.00 54.14  ? 115 THR D CG2   1 
ATOM   12493 N N     . PRO D  1 116 ? 2.547   66.658  212.963 1.00 50.79  ? 116 PRO D N     1 
ATOM   12494 C CA    . PRO D  1 116 ? 1.950   66.310  214.259 1.00 51.82  ? 116 PRO D CA    1 
ATOM   12495 C C     . PRO D  1 116 ? 2.193   64.850  214.607 1.00 46.25  ? 116 PRO D C     1 
ATOM   12496 O O     . PRO D  1 116 ? 1.996   63.988  213.754 1.00 44.15  ? 116 PRO D O     1 
ATOM   12497 C CB    . PRO D  1 116 ? 0.461   66.576  214.044 1.00 46.80  ? 116 PRO D CB    1 
ATOM   12498 C CG    . PRO D  1 116 ? 0.420   67.621  212.994 1.00 48.52  ? 116 PRO D CG    1 
ATOM   12499 C CD    . PRO D  1 116 ? 1.584   67.346  212.082 1.00 47.01  ? 116 PRO D CD    1 
ATOM   12500 N N     . PHE D  1 117 ? 2.613   64.571  215.835 1.00 42.49  ? 117 PHE D N     1 
ATOM   12501 C CA    . PHE D  1 117 ? 3.034   63.218  216.166 1.00 43.49  ? 117 PHE D CA    1 
ATOM   12502 C C     . PHE D  1 117 ? 2.676   62.803  217.583 1.00 39.91  ? 117 PHE D C     1 
ATOM   12503 O O     . PHE D  1 117 ? 2.452   63.644  218.451 1.00 38.48  ? 117 PHE D O     1 
ATOM   12504 C CB    . PHE D  1 117 ? 4.545   63.077  215.951 1.00 41.09  ? 117 PHE D CB    1 
ATOM   12505 C CG    . PHE D  1 117 ? 5.383   63.820  216.960 1.00 43.54  ? 117 PHE D CG    1 
ATOM   12506 C CD1   . PHE D  1 117 ? 6.053   63.134  217.959 1.00 39.82  ? 117 PHE D CD1   1 
ATOM   12507 C CD2   . PHE D  1 117 ? 5.512   65.201  216.903 1.00 44.06  ? 117 PHE D CD2   1 
ATOM   12508 C CE1   . PHE D  1 117 ? 6.834   63.806  218.882 1.00 45.68  ? 117 PHE D CE1   1 
ATOM   12509 C CE2   . PHE D  1 117 ? 6.290   65.880  217.830 1.00 47.02  ? 117 PHE D CE2   1 
ATOM   12510 C CZ    . PHE D  1 117 ? 6.951   65.179  218.819 1.00 48.49  ? 117 PHE D CZ    1 
ATOM   12511 N N     . ILE D  1 118 ? 2.615   61.492  217.800 1.00 37.74  ? 118 ILE D N     1 
ATOM   12512 C CA    . ILE D  1 118 ? 2.423   60.934  219.130 1.00 36.89  ? 118 ILE D CA    1 
ATOM   12513 C C     . ILE D  1 118 ? 3.699   60.229  219.560 1.00 39.55  ? 118 ILE D C     1 
ATOM   12514 O O     . ILE D  1 118 ? 4.283   59.465  218.790 1.00 36.93  ? 118 ILE D O     1 
ATOM   12515 C CB    . ILE D  1 118 ? 1.246   59.942  219.181 1.00 34.36  ? 118 ILE D CB    1 
ATOM   12516 C CG1   . ILE D  1 118 ? -0.039  60.604  218.694 1.00 41.13  ? 118 ILE D CG1   1 
ATOM   12517 C CG2   . ILE D  1 118 ? 1.048   59.441  220.596 1.00 32.95  ? 118 ILE D CG2   1 
ATOM   12518 C CD1   . ILE D  1 118 ? -0.540  61.701  219.606 1.00 42.64  ? 118 ILE D CD1   1 
ATOM   12519 N N     . LEU D  1 119 ? 4.133   60.489  220.787 1.00 39.09  ? 119 LEU D N     1 
ATOM   12520 C CA    . LEU D  1 119 ? 5.369   59.908  221.292 1.00 39.32  ? 119 LEU D CA    1 
ATOM   12521 C C     . LEU D  1 119 ? 5.100   58.666  222.134 1.00 38.10  ? 119 LEU D C     1 
ATOM   12522 O O     . LEU D  1 119 ? 4.420   58.732  223.157 1.00 37.30  ? 119 LEU D O     1 
ATOM   12523 C CB    . LEU D  1 119 ? 6.148   60.941  222.110 1.00 39.66  ? 119 LEU D CB    1 
ATOM   12524 C CG    . LEU D  1 119 ? 7.362   60.459  222.913 1.00 37.40  ? 119 LEU D CG    1 
ATOM   12525 C CD1   . LEU D  1 119 ? 8.358   59.713  222.035 1.00 38.61  ? 119 LEU D CD1   1 
ATOM   12526 C CD2   . LEU D  1 119 ? 8.035   61.639  223.604 1.00 41.55  ? 119 LEU D CD2   1 
ATOM   12527 N N     . ILE D  1 120 ? 5.633   57.533  221.686 1.00 38.78  ? 120 ILE D N     1 
ATOM   12528 C CA    . ILE D  1 120 ? 5.567   56.293  222.449 1.00 33.06  ? 120 ILE D CA    1 
ATOM   12529 C C     . ILE D  1 120 ? 6.853   56.122  223.243 1.00 38.55  ? 120 ILE D C     1 
ATOM   12530 O O     . ILE D  1 120 ? 7.908   55.849  222.671 1.00 38.00  ? 120 ILE D O     1 
ATOM   12531 C CB    . ILE D  1 120 ? 5.367   55.061  221.542 1.00 36.11  ? 120 ILE D CB    1 
ATOM   12532 C CG1   . ILE D  1 120 ? 4.127   55.234  220.662 1.00 35.99  ? 120 ILE D CG1   1 
ATOM   12533 C CG2   . ILE D  1 120 ? 5.253   53.793  222.375 1.00 30.45  ? 120 ILE D CG2   1 
ATOM   12534 C CD1   . ILE D  1 120 ? 3.927   54.111  219.663 1.00 28.06  ? 120 ILE D CD1   1 
ATOM   12535 N N     . ASP D  1 121 ? 6.774   56.292  224.559 1.00 38.06  ? 121 ASP D N     1 
ATOM   12536 C CA    . ASP D  1 121 ? 7.952   56.116  225.402 1.00 44.06  ? 121 ASP D CA    1 
ATOM   12537 C C     . ASP D  1 121 ? 7.957   54.726  226.031 1.00 42.13  ? 121 ASP D C     1 
ATOM   12538 O O     . ASP D  1 121 ? 6.991   54.319  226.675 1.00 36.89  ? 121 ASP D O     1 
ATOM   12539 C CB    . ASP D  1 121 ? 8.016   57.186  226.492 1.00 42.76  ? 121 ASP D CB    1 
ATOM   12540 C CG    . ASP D  1 121 ? 9.418   57.366  227.042 1.00 44.04  ? 121 ASP D CG    1 
ATOM   12541 O OD1   . ASP D  1 121 ? 9.887   56.470  227.774 1.00 48.12  ? 121 ASP D OD1   1 
ATOM   12542 O OD2   . ASP D  1 121 ? 10.055  58.396  226.736 1.00 47.91  ? 121 ASP D OD2   1 
ATOM   12543 N N     . LEU D  1 122 ? 9.062   54.011  225.851 1.00 33.79  ? 122 LEU D N     1 
ATOM   12544 C CA    . LEU D  1 122 ? 9.139   52.599  226.213 1.00 35.81  ? 122 LEU D CA    1 
ATOM   12545 C C     . LEU D  1 122 ? 9.788   52.351  227.569 1.00 37.19  ? 122 LEU D C     1 
ATOM   12546 O O     . LEU D  1 122 ? 10.155  51.219  227.880 1.00 38.21  ? 122 LEU D O     1 
ATOM   12547 C CB    . LEU D  1 122 ? 9.913   51.835  225.138 1.00 37.79  ? 122 LEU D CB    1 
ATOM   12548 C CG    . LEU D  1 122 ? 9.374   52.038  223.721 1.00 41.44  ? 122 LEU D CG    1 
ATOM   12549 C CD1   . LEU D  1 122 ? 10.374  51.570  222.685 1.00 31.60  ? 122 LEU D CD1   1 
ATOM   12550 C CD2   . LEU D  1 122 ? 8.044   51.313  223.552 1.00 36.75  ? 122 LEU D CD2   1 
ATOM   12551 N N     . MET D  1 123 ? 9.911   53.401  228.378 1.00 36.47  ? 123 MET D N     1 
ATOM   12552 C CA    . MET D  1 123 ? 10.651  53.324  229.636 1.00 42.38  ? 123 MET D CA    1 
ATOM   12553 C C     . MET D  1 123 ? 10.092  52.287  230.611 1.00 45.01  ? 123 MET D C     1 
ATOM   12554 O O     . MET D  1 123 ? 10.815  51.790  231.474 1.00 47.67  ? 123 MET D O     1 
ATOM   12555 C CB    . MET D  1 123 ? 10.687  54.691  230.323 1.00 48.84  ? 123 MET D CB    1 
ATOM   12556 C CG    . MET D  1 123 ? 9.377   55.110  230.968 1.00 47.10  ? 123 MET D CG    1 
ATOM   12557 S SD    . MET D  1 123 ? 9.539   56.611  231.954 1.00 54.10  ? 123 MET D SD    1 
ATOM   12558 C CE    . MET D  1 123 ? 9.827   57.835  230.678 1.00 49.70  ? 123 MET D CE    1 
ATOM   12559 N N     . ASN D  1 124 ? 8.811   51.960  230.473 1.00 46.85  ? 124 ASN D N     1 
ATOM   12560 C CA    . ASN D  1 124 ? 8.188   50.967  231.342 1.00 41.13  ? 124 ASN D CA    1 
ATOM   12561 C C     . ASN D  1 124 ? 8.396   49.548  230.836 1.00 40.54  ? 124 ASN D C     1 
ATOM   12562 O O     . ASN D  1 124 ? 8.094   48.579  231.532 1.00 45.82  ? 124 ASN D O     1 
ATOM   12563 C CB    . ASN D  1 124 ? 6.696   51.254  231.498 1.00 47.02  ? 124 ASN D CB    1 
ATOM   12564 C CG    . ASN D  1 124 ? 6.435   52.490  232.327 1.00 52.50  ? 124 ASN D CG    1 
ATOM   12565 O OD1   . ASN D  1 124 ? 7.320   52.964  233.035 1.00 55.48  ? 124 ASN D OD1   1 
ATOM   12566 N ND2   . ASN D  1 124 ? 5.218   53.017  232.250 1.00 53.14  ? 124 ASN D ND2   1 
ATOM   12567 N N     . LEU D  1 125 ? 8.902   49.433  229.615 1.00 41.30  ? 125 LEU D N     1 
ATOM   12568 C CA    . LEU D  1 125 ? 9.284   48.140  229.071 1.00 42.70  ? 125 LEU D CA    1 
ATOM   12569 C C     . LEU D  1 125 ? 10.774  47.927  229.283 1.00 47.46  ? 125 LEU D C     1 
ATOM   12570 O O     . LEU D  1 125 ? 11.557  47.978  228.338 1.00 41.04  ? 125 LEU D O     1 
ATOM   12571 C CB    . LEU D  1 125 ? 8.927   48.048  227.589 1.00 38.50  ? 125 LEU D CB    1 
ATOM   12572 C CG    . LEU D  1 125 ? 7.438   48.236  227.288 1.00 41.42  ? 125 LEU D CG    1 
ATOM   12573 C CD1   . LEU D  1 125 ? 7.177   48.184  225.797 1.00 37.28  ? 125 LEU D CD1   1 
ATOM   12574 C CD2   . LEU D  1 125 ? 6.624   47.182  228.020 1.00 39.62  ? 125 LEU D CD2   1 
ATOM   12575 N N     . ASN D  1 126 ? 11.168  47.705  230.533 1.00 48.81  ? 126 ASN D N     1 
ATOM   12576 C CA    . ASN D  1 126 ? 12.588  47.589  230.862 1.00 45.77  ? 126 ASN D CA    1 
ATOM   12577 C C     . ASN D  1 126 ? 12.914  46.334  231.655 1.00 46.09  ? 126 ASN D C     1 
ATOM   12578 O O     . ASN D  1 126 ? 13.735  46.368  232.568 1.00 49.75  ? 126 ASN D O     1 
ATOM   12579 C CB    . ASN D  1 126 ? 13.053  48.826  231.638 1.00 43.05  ? 126 ASN D CB    1 
ATOM   12580 C CG    . ASN D  1 126 ? 12.290  49.028  232.933 1.00 53.88  ? 126 ASN D CG    1 
ATOM   12581 O OD1   . ASN D  1 126 ? 11.301  48.343  233.204 1.00 52.41  ? 126 ASN D OD1   1 
ATOM   12582 N ND2   . ASN D  1 126 ? 12.737  49.986  233.735 1.00 52.93  ? 126 ASN D ND2   1 
ATOM   12583 N N     . ARG D  1 127 ? 12.269  45.228  231.304 1.00 45.79  ? 127 ARG D N     1 
ATOM   12584 C CA    . ARG D  1 127 ? 12.483  43.973  232.009 1.00 47.31  ? 127 ARG D CA    1 
ATOM   12585 C C     . ARG D  1 127 ? 13.516  43.099  231.313 1.00 47.13  ? 127 ARG D C     1 
ATOM   12586 O O     . ARG D  1 127 ? 13.500  42.957  230.090 1.00 44.12  ? 127 ARG D O     1 
ATOM   12587 C CB    . ARG D  1 127 ? 11.173  43.201  232.138 1.00 49.21  ? 127 ARG D CB    1 
ATOM   12588 C CG    . ARG D  1 127 ? 10.137  43.884  233.002 1.00 54.58  ? 127 ARG D CG    1 
ATOM   12589 C CD    . ARG D  1 127 ? 8.791   43.203  232.853 1.00 63.68  ? 127 ARG D CD    1 
ATOM   12590 N NE    . ARG D  1 127 ? 7.682   44.077  233.222 1.00 63.50  ? 127 ARG D NE    1 
ATOM   12591 C CZ    . ARG D  1 127 ? 7.209   45.047  232.446 1.00 68.04  ? 127 ARG D CZ    1 
ATOM   12592 N NH1   . ARG D  1 127 ? 7.759   45.277  231.262 1.00 66.10  ? 127 ARG D NH1   1 
ATOM   12593 N NH2   . ARG D  1 127 ? 6.194   45.795  232.856 1.00 72.38  ? 127 ARG D NH2   1 
ATOM   12594 N N     . VAL D  1 128 ? 14.404  42.504  232.102 1.00 49.86  ? 128 VAL D N     1 
ATOM   12595 C CA    . VAL D  1 128 ? 15.390  41.573  231.574 1.00 41.33  ? 128 VAL D CA    1 
ATOM   12596 C C     . VAL D  1 128 ? 15.177  40.191  232.179 1.00 38.77  ? 128 VAL D C     1 
ATOM   12597 O O     . VAL D  1 128 ? 15.083  40.047  233.398 1.00 45.96  ? 128 VAL D O     1 
ATOM   12598 C CB    . VAL D  1 128 ? 16.835  42.039  231.857 1.00 44.90  ? 128 VAL D CB    1 
ATOM   12599 C CG1   . VAL D  1 128 ? 17.834  41.111  231.183 1.00 38.49  ? 128 VAL D CG1   1 
ATOM   12600 C CG2   . VAL D  1 128 ? 17.037  43.466  231.380 1.00 44.64  ? 128 VAL D CG2   1 
ATOM   12601 N N     . SER D  1 129 ? 15.092  39.178  231.324 1.00 45.37  ? 129 SER D N     1 
ATOM   12602 C CA    . SER D  1 129 ? 14.899  37.807  231.778 1.00 51.13  ? 129 SER D CA    1 
ATOM   12603 C C     . SER D  1 129 ? 16.037  36.918  231.288 1.00 50.16  ? 129 SER D C     1 
ATOM   12604 O O     . SER D  1 129 ? 16.130  36.616  230.099 1.00 51.75  ? 129 SER D O     1 
ATOM   12605 C CB    . SER D  1 129 ? 13.554  37.271  231.287 1.00 50.78  ? 129 SER D CB    1 
ATOM   12606 O OG    . SER D  1 129 ? 12.510  38.184  231.590 1.00 64.54  ? 129 SER D OG    1 
ATOM   12607 N N     . ILE D  1 130 ? 16.893  36.492  232.210 1.00 51.72  ? 130 ILE D N     1 
ATOM   12608 C CA    . ILE D  1 130 ? 18.091  35.734  231.856 1.00 55.69  ? 130 ILE D CA    1 
ATOM   12609 C C     . ILE D  1 130 ? 17.904  34.227  232.016 1.00 57.11  ? 130 ILE D C     1 
ATOM   12610 O O     . ILE D  1 130 ? 17.422  33.756  233.045 1.00 61.24  ? 130 ILE D O     1 
ATOM   12611 C CB    . ILE D  1 130 ? 19.298  36.183  232.702 1.00 57.47  ? 130 ILE D CB    1 
ATOM   12612 C CG1   . ILE D  1 130 ? 19.624  37.649  232.409 1.00 52.60  ? 130 ILE D CG1   1 
ATOM   12613 C CG2   . ILE D  1 130 ? 20.509  35.305  232.422 1.00 58.33  ? 130 ILE D CG2   1 
ATOM   12614 C CD1   . ILE D  1 130 ? 20.353  38.350  233.523 1.00 60.35  ? 130 ILE D CD1   1 
ATOM   12615 N N     . ASP D  1 131 ? 18.274  33.481  230.978 1.00 58.42  ? 131 ASP D N     1 
ATOM   12616 C CA    . ASP D  1 131 ? 18.313  32.026  231.041 1.00 61.68  ? 131 ASP D CA    1 
ATOM   12617 C C     . ASP D  1 131 ? 19.768  31.571  231.022 1.00 66.38  ? 131 ASP D C     1 
ATOM   12618 O O     . ASP D  1 131 ? 20.404  31.538  229.969 1.00 63.64  ? 131 ASP D O     1 
ATOM   12619 C CB    . ASP D  1 131 ? 17.530  31.407  229.878 1.00 62.18  ? 131 ASP D CB    1 
ATOM   12620 C CG    . ASP D  1 131 ? 17.475  29.888  229.950 1.00 69.94  ? 131 ASP D CG    1 
ATOM   12621 O OD1   . ASP D  1 131 ? 17.857  29.324  230.996 1.00 72.89  ? 131 ASP D OD1   1 
ATOM   12622 O OD2   . ASP D  1 131 ? 17.037  29.261  228.962 1.00 70.69  ? 131 ASP D OD2   1 
ATOM   12623 N N     . LEU D  1 132 ? 20.286  31.220  232.195 1.00 69.33  ? 132 LEU D N     1 
ATOM   12624 C CA    . LEU D  1 132 ? 21.703  30.894  232.362 1.00 68.91  ? 132 LEU D CA    1 
ATOM   12625 C C     . LEU D  1 132 ? 22.093  29.554  231.748 1.00 71.67  ? 132 LEU D C     1 
ATOM   12626 O O     . LEU D  1 132 ? 23.279  29.236  231.635 1.00 78.31  ? 132 LEU D O     1 
ATOM   12627 C CB    . LEU D  1 132 ? 22.063  30.887  233.848 1.00 66.42  ? 132 LEU D CB    1 
ATOM   12628 C CG    . LEU D  1 132 ? 22.098  32.237  234.557 1.00 69.88  ? 132 LEU D CG    1 
ATOM   12629 C CD1   . LEU D  1 132 ? 22.402  32.046  236.030 1.00 73.36  ? 132 LEU D CD1   1 
ATOM   12630 C CD2   . LEU D  1 132 ? 23.130  33.142  233.914 1.00 70.67  ? 132 LEU D CD2   1 
ATOM   12631 N N     . GLU D  1 133 ? 21.096  28.774  231.351 1.00 70.50  ? 133 GLU D N     1 
ATOM   12632 C CA    . GLU D  1 133 ? 21.330  27.421  230.870 1.00 75.30  ? 133 GLU D CA    1 
ATOM   12633 C C     . GLU D  1 133 ? 21.508  27.398  229.356 1.00 74.19  ? 133 GLU D C     1 
ATOM   12634 O O     . GLU D  1 133 ? 22.239  26.571  228.812 1.00 77.40  ? 133 GLU D O     1 
ATOM   12635 C CB    . GLU D  1 133 ? 20.172  26.519  231.295 1.00 72.86  ? 133 GLU D CB    1 
ATOM   12636 C CG    . GLU D  1 133 ? 19.715  26.813  232.715 1.00 78.23  ? 133 GLU D CG    1 
ATOM   12637 C CD    . GLU D  1 133 ? 18.656  25.853  233.208 1.00 91.38  ? 133 GLU D CD    1 
ATOM   12638 O OE1   . GLU D  1 133 ? 17.475  26.255  233.284 1.00 90.37  ? 133 GLU D OE1   1 
ATOM   12639 O OE2   . GLU D  1 133 ? 19.006  24.700  233.531 1.00 90.32  ? 133 GLU D OE2   1 
ATOM   12640 N N     . SER D  1 134 ? 20.828  28.318  228.683 1.00 71.91  ? 134 SER D N     1 
ATOM   12641 C CA    . SER D  1 134 ? 21.019  28.519  227.256 1.00 67.27  ? 134 SER D CA    1 
ATOM   12642 C C     . SER D  1 134 ? 21.959  29.701  227.056 1.00 64.03  ? 134 SER D C     1 
ATOM   12643 O O     . SER D  1 134 ? 22.399  29.982  225.939 1.00 63.15  ? 134 SER D O     1 
ATOM   12644 C CB    . SER D  1 134 ? 19.680  28.756  226.554 1.00 66.23  ? 134 SER D CB    1 
ATOM   12645 O OG    . SER D  1 134 ? 18.988  29.855  227.124 1.00 62.35  ? 134 SER D OG    1 
ATOM   12646 N N     . GLU D  1 135 ? 22.267  30.373  228.165 1.00 62.53  ? 135 GLU D N     1 
ATOM   12647 C CA    . GLU D  1 135 ? 23.096  31.575  228.182 1.00 61.63  ? 135 GLU D CA    1 
ATOM   12648 C C     . GLU D  1 135 ? 22.563  32.623  227.216 1.00 59.51  ? 135 GLU D C     1 
ATOM   12649 O O     . GLU D  1 135 ? 23.306  33.203  226.423 1.00 60.59  ? 135 GLU D O     1 
ATOM   12650 C CB    . GLU D  1 135 ? 24.550  31.233  227.870 1.00 62.75  ? 135 GLU D CB    1 
ATOM   12651 C CG    . GLU D  1 135 ? 25.266  30.577  229.037 1.00 64.24  ? 135 GLU D CG    1 
ATOM   12652 C CD    . GLU D  1 135 ? 26.641  30.064  228.671 1.00 73.13  ? 135 GLU D CD    1 
ATOM   12653 O OE1   . GLU D  1 135 ? 26.963  30.028  227.465 1.00 68.40  ? 135 GLU D OE1   1 
ATOM   12654 O OE2   . GLU D  1 135 ? 27.401  29.694  229.592 1.00 72.55  ? 135 GLU D OE2   1 
ATOM   12655 N N     . THR D  1 136 ? 21.257  32.848  227.297 1.00 58.63  ? 136 THR D N     1 
ATOM   12656 C CA    . THR D  1 136 ? 20.589  33.889  226.533 1.00 53.77  ? 136 THR D CA    1 
ATOM   12657 C C     . THR D  1 136 ? 19.784  34.774  227.473 1.00 55.60  ? 136 THR D C     1 
ATOM   12658 O O     . THR D  1 136 ? 19.618  34.455  228.652 1.00 59.19  ? 136 THR D O     1 
ATOM   12659 C CB    . THR D  1 136 ? 19.652  33.304  225.463 1.00 54.14  ? 136 THR D CB    1 
ATOM   12660 O OG1   . THR D  1 136 ? 18.654  32.491  226.094 1.00 54.88  ? 136 THR D OG1   1 
ATOM   12661 C CG2   . THR D  1 136 ? 20.435  32.460  224.472 1.00 52.23  ? 136 THR D CG2   1 
ATOM   12662 N N     . ALA D  1 137 ? 19.284  35.888  226.952 1.00 48.72  ? 137 ALA D N     1 
ATOM   12663 C CA    . ALA D  1 137 ? 18.460  36.788  227.745 1.00 48.19  ? 137 ALA D CA    1 
ATOM   12664 C C     . ALA D  1 137 ? 17.449  37.524  226.876 1.00 44.10  ? 137 ALA D C     1 
ATOM   12665 O O     . ALA D  1 137 ? 17.752  37.914  225.748 1.00 43.81  ? 137 ALA D O     1 
ATOM   12666 C CB    . ALA D  1 137 ? 19.333  37.783  228.496 1.00 45.68  ? 137 ALA D CB    1 
ATOM   12667 N N     . TRP D  1 138 ? 16.243  37.705  227.402 1.00 43.41  ? 138 TRP D N     1 
ATOM   12668 C CA    . TRP D  1 138 ? 15.251  38.546  226.746 1.00 37.65  ? 138 TRP D CA    1 
ATOM   12669 C C     . TRP D  1 138 ? 15.295  39.942  227.353 1.00 38.64  ? 138 TRP D C     1 
ATOM   12670 O O     . TRP D  1 138 ? 15.208  40.102  228.572 1.00 43.29  ? 138 TRP D O     1 
ATOM   12671 C CB    . TRP D  1 138 ? 13.850  37.950  226.872 1.00 40.26  ? 138 TRP D CB    1 
ATOM   12672 C CG    . TRP D  1 138 ? 13.548  36.909  225.840 1.00 35.76  ? 138 TRP D CG    1 
ATOM   12673 C CD1   . TRP D  1 138 ? 13.576  35.556  226.008 1.00 39.03  ? 138 TRP D CD1   1 
ATOM   12674 C CD2   . TRP D  1 138 ? 13.174  37.136  224.476 1.00 38.62  ? 138 TRP D CD2   1 
ATOM   12675 N NE1   . TRP D  1 138 ? 13.243  34.925  224.833 1.00 40.37  ? 138 TRP D NE1   1 
ATOM   12676 C CE2   . TRP D  1 138 ? 12.991  35.874  223.877 1.00 40.76  ? 138 TRP D CE2   1 
ATOM   12677 C CE3   . TRP D  1 138 ? 12.976  38.285  223.703 1.00 34.73  ? 138 TRP D CE3   1 
ATOM   12678 C CZ2   . TRP D  1 138 ? 12.617  35.729  222.541 1.00 40.48  ? 138 TRP D CZ2   1 
ATOM   12679 C CZ3   . TRP D  1 138 ? 12.608  38.138  222.378 1.00 34.93  ? 138 TRP D CZ3   1 
ATOM   12680 C CH2   . TRP D  1 138 ? 12.430  36.871  221.811 1.00 31.92  ? 138 TRP D CH2   1 
ATOM   12681 N N     . VAL D  1 139 ? 15.437  40.949  226.501 1.00 34.94  ? 139 VAL D N     1 
ATOM   12682 C CA    . VAL D  1 139 ? 15.582  42.321  226.961 1.00 34.59  ? 139 VAL D CA    1 
ATOM   12683 C C     . VAL D  1 139 ? 14.542  43.228  226.325 1.00 35.77  ? 139 VAL D C     1 
ATOM   12684 O O     . VAL D  1 139 ? 14.592  43.478  225.121 1.00 34.39  ? 139 VAL D O     1 
ATOM   12685 C CB    . VAL D  1 139 ? 16.976  42.872  226.633 1.00 33.49  ? 139 VAL D CB    1 
ATOM   12686 C CG1   . VAL D  1 139 ? 17.132  44.283  227.179 1.00 34.15  ? 139 VAL D CG1   1 
ATOM   12687 C CG2   . VAL D  1 139 ? 18.052  41.948  227.182 1.00 34.37  ? 139 VAL D CG2   1 
ATOM   12688 N N     . GLU D  1 140 ? 13.605  43.722  227.129 1.00 38.09  ? 140 GLU D N     1 
ATOM   12689 C CA    . GLU D  1 140 ? 12.596  44.648  226.629 1.00 37.17  ? 140 GLU D CA    1 
ATOM   12690 C C     . GLU D  1 140 ? 13.283  45.927  226.165 1.00 39.42  ? 140 GLU D C     1 
ATOM   12691 O O     . GLU D  1 140 ? 14.264  46.363  226.760 1.00 40.01  ? 140 GLU D O     1 
ATOM   12692 C CB    . GLU D  1 140 ? 11.541  44.930  227.698 1.00 39.73  ? 140 GLU D CB    1 
ATOM   12693 C CG    . GLU D  1 140 ? 10.678  43.721  228.022 1.00 38.70  ? 140 GLU D CG    1 
ATOM   12694 C CD    . GLU D  1 140 ? 9.548   44.038  228.977 1.00 47.12  ? 140 GLU D CD    1 
ATOM   12695 O OE1   . GLU D  1 140 ? 9.635   45.058  229.688 1.00 46.58  ? 140 GLU D OE1   1 
ATOM   12696 O OE2   . GLU D  1 140 ? 8.568   43.264  229.017 1.00 37.57  ? 140 GLU D OE2   1 
ATOM   12697 N N     . SER D  1 141 ? 12.769  46.517  225.091 1.00 33.29  ? 141 SER D N     1 
ATOM   12698 C CA    . SER D  1 141 ? 13.503  47.539  224.347 1.00 30.62  ? 141 SER D CA    1 
ATOM   12699 C C     . SER D  1 141 ? 13.598  48.900  225.031 1.00 38.55  ? 141 SER D C     1 
ATOM   12700 O O     . SER D  1 141 ? 14.245  49.807  224.511 1.00 36.26  ? 141 SER D O     1 
ATOM   12701 C CB    . SER D  1 141 ? 12.878  47.719  222.964 1.00 34.29  ? 141 SER D CB    1 
ATOM   12702 O OG    . SER D  1 141 ? 11.517  48.106  223.054 1.00 31.84  ? 141 SER D OG    1 
ATOM   12703 N N     . GLY D  1 142 ? 12.958  49.047  226.186 1.00 39.40  ? 142 GLY D N     1 
ATOM   12704 C CA    . GLY D  1 142 ? 13.052  50.281  226.948 1.00 39.68  ? 142 GLY D CA    1 
ATOM   12705 C C     . GLY D  1 142 ? 14.217  50.227  227.917 1.00 40.41  ? 142 GLY D C     1 
ATOM   12706 O O     . GLY D  1 142 ? 14.605  51.234  228.510 1.00 41.45  ? 142 GLY D O     1 
ATOM   12707 N N     . SER D  1 143 ? 14.775  49.032  228.075 1.00 36.87  ? 143 SER D N     1 
ATOM   12708 C CA    . SER D  1 143 ? 15.942  48.832  228.921 1.00 45.61  ? 143 SER D CA    1 
ATOM   12709 C C     . SER D  1 143 ? 17.131  49.635  228.423 1.00 42.34  ? 143 SER D C     1 
ATOM   12710 O O     . SER D  1 143 ? 17.408  49.672  227.225 1.00 38.93  ? 143 SER D O     1 
ATOM   12711 C CB    . SER D  1 143 ? 16.321  47.351  228.978 1.00 42.08  ? 143 SER D CB    1 
ATOM   12712 O OG    . SER D  1 143 ? 15.249  46.551  229.442 1.00 44.87  ? 143 SER D OG    1 
ATOM   12713 N N     . THR D  1 144 ? 17.832  50.281  229.347 1.00 43.54  ? 144 THR D N     1 
ATOM   12714 C CA    . THR D  1 144 ? 19.092  50.920  229.004 1.00 44.85  ? 144 THR D CA    1 
ATOM   12715 C C     . THR D  1 144 ? 20.196  49.874  229.053 1.00 38.88  ? 144 THR D C     1 
ATOM   12716 O O     . THR D  1 144 ? 20.011  48.796  229.621 1.00 42.46  ? 144 THR D O     1 
ATOM   12717 C CB    . THR D  1 144 ? 19.428  52.087  229.948 1.00 42.13  ? 144 THR D CB    1 
ATOM   12718 O OG1   . THR D  1 144 ? 19.528  51.611  231.295 1.00 46.77  ? 144 THR D OG1   1 
ATOM   12719 C CG2   . THR D  1 144 ? 18.356  53.151  229.868 1.00 45.18  ? 144 THR D CG2   1 
ATOM   12720 N N     . LEU D  1 145 ? 21.334  50.188  228.443 1.00 46.42  ? 145 LEU D N     1 
ATOM   12721 C CA    . LEU D  1 145 ? 22.491  49.304  228.488 1.00 43.60  ? 145 LEU D CA    1 
ATOM   12722 C C     . LEU D  1 145 ? 22.904  49.050  229.933 1.00 42.27  ? 145 LEU D C     1 
ATOM   12723 O O     . LEU D  1 145 ? 23.228  47.924  230.312 1.00 40.13  ? 145 LEU D O     1 
ATOM   12724 C CB    . LEU D  1 145 ? 23.652  49.905  227.697 1.00 47.12  ? 145 LEU D CB    1 
ATOM   12725 C CG    . LEU D  1 145 ? 23.402  50.172  226.211 1.00 44.00  ? 145 LEU D CG    1 
ATOM   12726 C CD1   . LEU D  1 145 ? 24.639  50.766  225.573 1.00 39.57  ? 145 LEU D CD1   1 
ATOM   12727 C CD2   . LEU D  1 145 ? 22.996  48.895  225.499 1.00 36.49  ? 145 LEU D CD2   1 
ATOM   12728 N N     . GLY D  1 146 ? 22.879  50.111  230.733 1.00 42.42  ? 146 GLY D N     1 
ATOM   12729 C CA    . GLY D  1 146 ? 23.218  50.025  232.141 1.00 47.23  ? 146 GLY D CA    1 
ATOM   12730 C C     . GLY D  1 146 ? 22.297  49.090  232.898 1.00 52.10  ? 146 GLY D C     1 
ATOM   12731 O O     . GLY D  1 146 ? 22.755  48.265  233.685 1.00 57.96  ? 146 GLY D O     1 
ATOM   12732 N N     . GLU D  1 147 ? 20.995  49.213  232.653 1.00 51.71  ? 147 GLU D N     1 
ATOM   12733 C CA    . GLU D  1 147 ? 20.019  48.323  233.271 1.00 50.31  ? 147 GLU D CA    1 
ATOM   12734 C C     . GLU D  1 147 ? 20.263  46.871  232.865 1.00 44.06  ? 147 GLU D C     1 
ATOM   12735 O O     . GLU D  1 147 ? 20.061  45.956  233.661 1.00 51.98  ? 147 GLU D O     1 
ATOM   12736 C CB    . GLU D  1 147 ? 18.595  48.744  232.898 1.00 47.78  ? 147 GLU D CB    1 
ATOM   12737 C CG    . GLU D  1 147 ? 18.107  49.987  233.616 1.00 51.22  ? 147 GLU D CG    1 
ATOM   12738 C CD    . GLU D  1 147 ? 16.783  50.490  233.077 1.00 53.98  ? 147 GLU D CD    1 
ATOM   12739 O OE1   . GLU D  1 147 ? 16.408  50.093  231.954 1.00 49.55  ? 147 GLU D OE1   1 
ATOM   12740 O OE2   . GLU D  1 147 ? 16.115  51.282  233.776 1.00 57.06  ? 147 GLU D OE2   1 
ATOM   12741 N N     . LEU D  1 148 ? 20.703  46.670  231.626 1.00 43.32  ? 148 LEU D N     1 
ATOM   12742 C CA    . LEU D  1 148 ? 21.001  45.333  231.117 1.00 43.49  ? 148 LEU D CA    1 
ATOM   12743 C C     . LEU D  1 148 ? 22.281  44.757  231.727 1.00 45.51  ? 148 LEU D C     1 
ATOM   12744 O O     . LEU D  1 148 ? 22.303  43.602  232.152 1.00 50.07  ? 148 LEU D O     1 
ATOM   12745 C CB    . LEU D  1 148 ? 21.117  45.352  229.590 1.00 38.53  ? 148 LEU D CB    1 
ATOM   12746 C CG    . LEU D  1 148 ? 21.683  44.083  228.945 1.00 37.83  ? 148 LEU D CG    1 
ATOM   12747 C CD1   . LEU D  1 148 ? 20.833  42.865  229.282 1.00 38.53  ? 148 LEU D CD1   1 
ATOM   12748 C CD2   . LEU D  1 148 ? 21.823  44.244  227.436 1.00 34.36  ? 148 LEU D CD2   1 
ATOM   12749 N N     . TYR D  1 149 ? 23.343  45.558  231.746 1.00 48.50  ? 149 TYR D N     1 
ATOM   12750 C CA    . TYR D  1 149 ? 24.622  45.147  232.325 1.00 53.44  ? 149 TYR D CA    1 
ATOM   12751 C C     . TYR D  1 149 ? 24.446  44.695  233.768 1.00 55.66  ? 149 TYR D C     1 
ATOM   12752 O O     . TYR D  1 149 ? 24.873  43.605  234.148 1.00 57.51  ? 149 TYR D O     1 
ATOM   12753 C CB    . TYR D  1 149 ? 25.635  46.290  232.270 1.00 47.74  ? 149 TYR D CB    1 
ATOM   12754 C CG    . TYR D  1 149 ? 25.987  46.756  230.879 1.00 43.99  ? 149 TYR D CG    1 
ATOM   12755 C CD1   . TYR D  1 149 ? 25.903  45.895  229.794 1.00 46.78  ? 149 TYR D CD1   1 
ATOM   12756 C CD2   . TYR D  1 149 ? 26.409  48.060  230.653 1.00 45.37  ? 149 TYR D CD2   1 
ATOM   12757 C CE1   . TYR D  1 149 ? 26.228  46.320  228.524 1.00 48.20  ? 149 TYR D CE1   1 
ATOM   12758 C CE2   . TYR D  1 149 ? 26.732  48.493  229.390 1.00 46.83  ? 149 TYR D CE2   1 
ATOM   12759 C CZ    . TYR D  1 149 ? 26.642  47.621  228.331 1.00 43.05  ? 149 TYR D CZ    1 
ATOM   12760 O OH    . TYR D  1 149 ? 26.967  48.059  227.073 1.00 43.90  ? 149 TYR D OH    1 
ATOM   12761 N N     . TYR D  1 150 ? 23.810  45.557  234.556 1.00 58.89  ? 150 TYR D N     1 
ATOM   12762 C CA    . TYR D  1 150 ? 23.492  45.288  235.954 1.00 60.75  ? 150 TYR D CA    1 
ATOM   12763 C C     . TYR D  1 150 ? 22.813  43.933  236.133 1.00 62.54  ? 150 TYR D C     1 
ATOM   12764 O O     . TYR D  1 150 ? 23.229  43.123  236.962 1.00 67.72  ? 150 TYR D O     1 
ATOM   12765 C CB    . TYR D  1 150 ? 22.597  46.406  236.503 1.00 63.75  ? 150 TYR D CB    1 
ATOM   12766 C CG    . TYR D  1 150 ? 22.140  46.220  237.937 1.00 72.99  ? 150 TYR D CG    1 
ATOM   12767 C CD1   . TYR D  1 150 ? 22.787  46.867  238.981 1.00 72.67  ? 150 TYR D CD1   1 
ATOM   12768 C CD2   . TYR D  1 150 ? 21.047  45.415  238.243 1.00 71.97  ? 150 TYR D CD2   1 
ATOM   12769 C CE1   . TYR D  1 150 ? 22.368  46.705  240.290 1.00 73.87  ? 150 TYR D CE1   1 
ATOM   12770 C CE2   . TYR D  1 150 ? 20.626  45.245  239.543 1.00 73.79  ? 150 TYR D CE2   1 
ATOM   12771 C CZ    . TYR D  1 150 ? 21.288  45.892  240.563 1.00 77.61  ? 150 TYR D CZ    1 
ATOM   12772 O OH    . TYR D  1 150 ? 20.864  45.724  241.861 1.00 81.92  ? 150 TYR D OH    1 
ATOM   12773 N N     . ALA D  1 151 ? 21.764  43.700  235.349 1.00 60.93  ? 151 ALA D N     1 
ATOM   12774 C CA    . ALA D  1 151 ? 20.954  42.494  235.471 1.00 63.46  ? 151 ALA D CA    1 
ATOM   12775 C C     . ALA D  1 151 ? 21.765  41.233  235.201 1.00 60.63  ? 151 ALA D C     1 
ATOM   12776 O O     . ALA D  1 151 ? 21.561  40.207  235.850 1.00 64.22  ? 151 ALA D O     1 
ATOM   12777 C CB    . ALA D  1 151 ? 19.761  42.566  234.528 1.00 60.71  ? 151 ALA D CB    1 
ATOM   12778 N N     . ILE D  1 152 ? 22.683  41.318  234.243 1.00 61.56  ? 152 ILE D N     1 
ATOM   12779 C CA    . ILE D  1 152 ? 23.547  40.193  233.899 1.00 64.98  ? 152 ILE D CA    1 
ATOM   12780 C C     . ILE D  1 152 ? 24.503  39.860  235.041 1.00 66.16  ? 152 ILE D C     1 
ATOM   12781 O O     . ILE D  1 152 ? 24.694  38.689  235.375 1.00 69.31  ? 152 ILE D O     1 
ATOM   12782 C CB    . ILE D  1 152 ? 24.359  40.475  232.623 1.00 62.58  ? 152 ILE D CB    1 
ATOM   12783 C CG1   . ILE D  1 152 ? 23.422  40.685  231.431 1.00 54.75  ? 152 ILE D CG1   1 
ATOM   12784 C CG2   . ILE D  1 152 ? 25.320  39.332  232.333 1.00 59.45  ? 152 ILE D CG2   1 
ATOM   12785 C CD1   . ILE D  1 152 ? 24.132  41.140  230.179 1.00 50.70  ? 152 ILE D CD1   1 
ATOM   12786 N N     . THR D  1 153 ? 25.099  40.891  235.634 1.00 63.87  ? 153 THR D N     1 
ATOM   12787 C CA    . THR D  1 153 ? 25.992  40.718  236.777 1.00 69.61  ? 153 THR D CA    1 
ATOM   12788 C C     . THR D  1 153 ? 25.290  40.009  237.931 1.00 71.91  ? 153 THR D C     1 
ATOM   12789 O O     . THR D  1 153 ? 25.821  39.058  238.506 1.00 72.20  ? 153 THR D O     1 
ATOM   12790 C CB    . THR D  1 153 ? 26.529  42.067  237.295 1.00 67.07  ? 153 THR D CB    1 
ATOM   12791 O OG1   . THR D  1 153 ? 25.445  42.849  237.815 1.00 63.81  ? 153 THR D OG1   1 
ATOM   12792 C CG2   . THR D  1 153 ? 27.216  42.837  236.180 1.00 64.92  ? 153 THR D CG2   1 
ATOM   12793 N N     . GLU D  1 154 ? 24.083  40.471  238.247 1.00 70.94  ? 154 GLU D N     1 
ATOM   12794 C CA    . GLU D  1 154 ? 23.293  39.923  239.347 1.00 68.74  ? 154 GLU D CA    1 
ATOM   12795 C C     . GLU D  1 154 ? 22.833  38.487  239.092 1.00 71.48  ? 154 GLU D C     1 
ATOM   12796 O O     . GLU D  1 154 ? 22.192  37.876  239.945 1.00 85.99  ? 154 GLU D O     1 
ATOM   12797 C CB    . GLU D  1 154 ? 22.073  40.806  239.608 1.00 72.27  ? 154 GLU D CB    1 
ATOM   12798 C CG    . GLU D  1 154 ? 22.397  42.195  240.132 1.00 74.41  ? 154 GLU D CG    1 
ATOM   12799 C CD    . GLU D  1 154 ? 22.331  42.275  241.645 1.00 84.92  ? 154 GLU D CD    1 
ATOM   12800 O OE1   . GLU D  1 154 ? 21.930  43.337  242.165 1.00 85.80  ? 154 GLU D OE1   1 
ATOM   12801 O OE2   . GLU D  1 154 ? 22.680  41.279  242.315 1.00 90.53  ? 154 GLU D OE2   1 
ATOM   12802 N N     . SER D  1 155 ? 23.159  37.957  237.919 1.00 66.59  ? 155 SER D N     1 
ATOM   12803 C CA    . SER D  1 155 ? 22.755  36.609  237.546 1.00 69.88  ? 155 SER D CA    1 
ATOM   12804 C C     . SER D  1 155 ? 23.961  35.694  237.359 1.00 70.63  ? 155 SER D C     1 
ATOM   12805 O O     . SER D  1 155 ? 23.868  34.480  237.543 1.00 70.75  ? 155 SER D O     1 
ATOM   12806 C CB    . SER D  1 155 ? 21.921  36.643  236.266 1.00 70.90  ? 155 SER D CB    1 
ATOM   12807 O OG    . SER D  1 155 ? 21.708  35.338  235.753 1.00 74.06  ? 155 SER D OG    1 
ATOM   12808 N N     . SER D  1 156 ? 25.090  36.291  236.992 1.00 71.94  ? 156 SER D N     1 
ATOM   12809 C CA    . SER D  1 156 ? 26.310  35.541  236.732 1.00 70.16  ? 156 SER D CA    1 
ATOM   12810 C C     . SER D  1 156 ? 27.523  36.459  236.703 1.00 75.57  ? 156 SER D C     1 
ATOM   12811 O O     . SER D  1 156 ? 27.408  37.649  236.408 1.00 73.20  ? 156 SER D O     1 
ATOM   12812 C CB    . SER D  1 156 ? 26.203  34.783  235.409 1.00 71.73  ? 156 SER D CB    1 
ATOM   12813 O OG    . SER D  1 156 ? 27.426  34.140  235.090 1.00 76.23  ? 156 SER D OG    1 
ATOM   12814 N N     . SER D  1 157 ? 28.687  35.899  237.010 1.00 76.49  ? 157 SER D N     1 
ATOM   12815 C CA    . SER D  1 157 ? 29.934  36.648  236.945 1.00 77.77  ? 157 SER D CA    1 
ATOM   12816 C C     . SER D  1 157 ? 30.828  36.076  235.852 1.00 77.23  ? 157 SER D C     1 
ATOM   12817 O O     . SER D  1 157 ? 31.934  36.558  235.618 1.00 79.09  ? 157 SER D O     1 
ATOM   12818 C CB    . SER D  1 157 ? 30.652  36.620  238.296 1.00 79.98  ? 157 SER D CB    1 
ATOM   12819 O OG    . SER D  1 157 ? 30.818  35.291  238.758 1.00 85.69  ? 157 SER D OG    1 
ATOM   12820 N N     . LYS D  1 158 ? 30.332  35.037  235.190 1.00 76.91  ? 158 LYS D N     1 
ATOM   12821 C CA    . LYS D  1 158 ? 31.064  34.392  234.111 1.00 73.74  ? 158 LYS D CA    1 
ATOM   12822 C C     . LYS D  1 158 ? 30.483  34.813  232.768 1.00 70.09  ? 158 LYS D C     1 
ATOM   12823 O O     . LYS D  1 158 ? 30.820  34.243  231.732 1.00 65.69  ? 158 LYS D O     1 
ATOM   12824 C CB    . LYS D  1 158 ? 31.014  32.874  234.268 1.00 80.73  ? 158 LYS D CB    1 
ATOM   12825 C CG    . LYS D  1 158 ? 30.993  32.428  235.722 1.00 84.78  ? 158 LYS D CG    1 
ATOM   12826 C CD    . LYS D  1 158 ? 30.614  30.965  235.869 1.00 87.69  ? 158 LYS D CD    1 
ATOM   12827 C CE    . LYS D  1 158 ? 30.125  30.667  237.280 1.00 93.22  ? 158 LYS D CE    1 
ATOM   12828 N NZ    . LYS D  1 158 ? 28.939  31.495  237.646 1.00 88.39  ? 158 LYS D NZ    1 
ATOM   12829 N N     . LEU D  1 159 ? 29.613  35.819  232.794 1.00 73.68  ? 159 LEU D N     1 
ATOM   12830 C CA    . LEU D  1 159 ? 28.890  36.240  231.599 1.00 64.43  ? 159 LEU D CA    1 
ATOM   12831 C C     . LEU D  1 159 ? 28.804  37.760  231.469 1.00 60.89  ? 159 LEU D C     1 
ATOM   12832 O O     . LEU D  1 159 ? 28.716  38.480  232.463 1.00 61.24  ? 159 LEU D O     1 
ATOM   12833 C CB    . LEU D  1 159 ? 27.482  35.641  231.602 1.00 63.90  ? 159 LEU D CB    1 
ATOM   12834 C CG    . LEU D  1 159 ? 27.356  34.133  231.376 1.00 67.46  ? 159 LEU D CG    1 
ATOM   12835 C CD1   . LEU D  1 159 ? 25.957  33.653  231.736 1.00 69.09  ? 159 LEU D CD1   1 
ATOM   12836 C CD2   . LEU D  1 159 ? 27.686  33.777  229.933 1.00 60.58  ? 159 LEU D CD2   1 
ATOM   12837 N N     . GLY D  1 160 ? 28.831  38.236  230.228 1.00 59.86  ? 160 GLY D N     1 
ATOM   12838 C CA    . GLY D  1 160 ? 28.693  39.651  229.936 1.00 59.06  ? 160 GLY D CA    1 
ATOM   12839 C C     . GLY D  1 160 ? 28.067  39.856  228.570 1.00 55.07  ? 160 GLY D C     1 
ATOM   12840 O O     . GLY D  1 160 ? 27.559  38.908  227.971 1.00 52.42  ? 160 GLY D O     1 
ATOM   12841 N N     . PHE D  1 161 ? 28.104  41.089  228.072 1.00 53.63  ? 161 PHE D N     1 
ATOM   12842 C CA    . PHE D  1 161 ? 27.536  41.400  226.764 1.00 52.66  ? 161 PHE D CA    1 
ATOM   12843 C C     . PHE D  1 161 ? 28.213  42.626  226.157 1.00 51.31  ? 161 PHE D C     1 
ATOM   12844 O O     . PHE D  1 161 ? 28.633  43.533  226.879 1.00 53.88  ? 161 PHE D O     1 
ATOM   12845 C CB    . PHE D  1 161 ? 26.027  41.620  226.879 1.00 46.58  ? 161 PHE D CB    1 
ATOM   12846 C CG    . PHE D  1 161 ? 25.346  41.839  225.561 1.00 34.51  ? 161 PHE D CG    1 
ATOM   12847 C CD1   . PHE D  1 161 ? 25.124  40.779  224.697 1.00 41.58  ? 161 PHE D CD1   1 
ATOM   12848 C CD2   . PHE D  1 161 ? 24.921  43.103  225.190 1.00 40.03  ? 161 PHE D CD2   1 
ATOM   12849 C CE1   . PHE D  1 161 ? 24.494  40.976  223.484 1.00 40.37  ? 161 PHE D CE1   1 
ATOM   12850 C CE2   . PHE D  1 161 ? 24.291  43.310  223.979 1.00 36.69  ? 161 PHE D CE2   1 
ATOM   12851 C CZ    . PHE D  1 161 ? 24.077  42.245  223.125 1.00 35.94  ? 161 PHE D CZ    1 
ATOM   12852 N N     . THR D  1 162 ? 28.324  42.650  224.832 1.00 46.93  ? 162 THR D N     1 
ATOM   12853 C CA    . THR D  1 162 ? 29.058  43.716  224.158 1.00 48.40  ? 162 THR D CA    1 
ATOM   12854 C C     . THR D  1 162 ? 28.154  44.848  223.673 1.00 51.27  ? 162 THR D C     1 
ATOM   12855 O O     . THR D  1 162 ? 27.260  44.645  222.853 1.00 50.20  ? 162 THR D O     1 
ATOM   12856 C CB    . THR D  1 162 ? 29.876  43.170  222.960 1.00 47.79  ? 162 THR D CB    1 
ATOM   12857 O OG1   . THR D  1 162 ? 30.389  44.264  222.191 1.00 56.42  ? 162 THR D OG1   1 
ATOM   12858 C CG2   . THR D  1 162 ? 29.023  42.288  222.064 1.00 41.00  ? 162 THR D CG2   1 
ATOM   12859 N N     . ALA D  1 163 ? 28.398  46.043  224.204 1.00 50.63  ? 163 ALA D N     1 
ATOM   12860 C CA    . ALA D  1 163 ? 27.736  47.260  223.749 1.00 49.65  ? 163 ALA D CA    1 
ATOM   12861 C C     . ALA D  1 163 ? 28.457  48.491  224.298 1.00 56.01  ? 163 ALA D C     1 
ATOM   12862 O O     . ALA D  1 163 ? 29.514  48.378  224.921 1.00 51.96  ? 163 ALA D O     1 
ATOM   12863 C CB    . ALA D  1 163 ? 26.262  47.269  224.159 1.00 43.90  ? 163 ALA D CB    1 
ATOM   12864 N N     . ALA D  1 164 ? 27.865  49.658  224.060 1.00 55.58  ? 164 ALA D N     1 
ATOM   12865 C CA    . ALA D  1 164 ? 28.455  50.952  224.405 1.00 54.32  ? 164 ALA D CA    1 
ATOM   12866 C C     . ALA D  1 164 ? 28.833  51.095  225.877 1.00 60.65  ? 164 ALA D C     1 
ATOM   12867 O O     . ALA D  1 164 ? 28.415  50.303  226.722 1.00 60.75  ? 164 ALA D O     1 
ATOM   12868 C CB    . ALA D  1 164 ? 27.496  52.065  224.017 1.00 65.91  ? 164 ALA D CB    1 
ATOM   12869 N N     . TRP D  1 165 ? 29.626  52.121  226.172 1.00 59.27  ? 165 TRP D N     1 
ATOM   12870 C CA    . TRP D  1 165 ? 29.999  52.437  227.545 1.00 63.65  ? 165 TRP D CA    1 
ATOM   12871 C C     . TRP D  1 165 ? 28.947  53.334  228.188 1.00 63.74  ? 165 TRP D C     1 
ATOM   12872 O O     . TRP D  1 165 ? 28.766  53.312  229.405 1.00 67.70  ? 165 TRP D O     1 
ATOM   12873 C CB    . TRP D  1 165 ? 31.374  53.111  227.595 1.00 61.67  ? 165 TRP D CB    1 
ATOM   12874 C CG    . TRP D  1 165 ? 31.473  54.365  226.772 1.00 67.01  ? 165 TRP D CG    1 
ATOM   12875 C CD1   . TRP D  1 165 ? 31.904  54.465  225.481 1.00 67.38  ? 165 TRP D CD1   1 
ATOM   12876 C CD2   . TRP D  1 165 ? 31.141  55.697  227.187 1.00 72.89  ? 165 TRP D CD2   1 
ATOM   12877 N NE1   . TRP D  1 165 ? 31.860  55.773  225.065 1.00 66.26  ? 165 TRP D NE1   1 
ATOM   12878 C CE2   . TRP D  1 165 ? 31.396  56.551  226.093 1.00 72.67  ? 165 TRP D CE2   1 
ATOM   12879 C CE3   . TRP D  1 165 ? 30.655  56.252  228.376 1.00 67.57  ? 165 TRP D CE3   1 
ATOM   12880 C CZ2   . TRP D  1 165 ? 31.180  57.928  226.152 1.00 69.58  ? 165 TRP D CZ2   1 
ATOM   12881 C CZ3   . TRP D  1 165 ? 30.441  57.619  228.433 1.00 69.68  ? 165 TRP D CZ3   1 
ATOM   12882 C CH2   . TRP D  1 165 ? 30.703  58.441  227.328 1.00 67.28  ? 165 TRP D CH2   1 
ATOM   12883 N N     . CYS D  1 166 ? 28.263  54.122  227.361 1.00 58.73  ? 166 CYS D N     1 
ATOM   12884 C CA    . CYS D  1 166 ? 27.194  55.004  227.824 1.00 55.51  ? 166 CYS D CA    1 
ATOM   12885 C C     . CYS D  1 166 ? 26.038  54.198  228.407 1.00 55.71  ? 166 CYS D C     1 
ATOM   12886 O O     . CYS D  1 166 ? 25.299  53.544  227.671 1.00 53.93  ? 166 CYS D O     1 
ATOM   12887 C CB    . CYS D  1 166 ? 26.687  55.882  226.678 1.00 55.22  ? 166 CYS D CB    1 
ATOM   12888 S SG    . CYS D  1 166 ? 27.949  56.821  225.788 1.00 59.53  ? 166 CYS D SG    1 
ATOM   12889 N N     . PRO D  1 167 ? 25.864  54.255  229.734 1.00 54.73  ? 167 PRO D N     1 
ATOM   12890 C CA    . PRO D  1 167 ? 24.914  53.358  230.401 1.00 52.51  ? 167 PRO D CA    1 
ATOM   12891 C C     . PRO D  1 167 ? 23.444  53.762  230.263 1.00 51.09  ? 167 PRO D C     1 
ATOM   12892 O O     . PRO D  1 167 ? 22.574  52.925  230.512 1.00 50.41  ? 167 PRO D O     1 
ATOM   12893 C CB    . PRO D  1 167 ? 25.350  53.429  231.863 1.00 57.62  ? 167 PRO D CB    1 
ATOM   12894 C CG    . PRO D  1 167 ? 25.908  54.802  232.008 1.00 58.34  ? 167 PRO D CG    1 
ATOM   12895 C CD    . PRO D  1 167 ? 26.572  55.121  230.694 1.00 58.84  ? 167 PRO D CD    1 
ATOM   12896 N N     . THR D  1 168 ? 23.165  55.004  229.879 1.00 48.57  ? 168 THR D N     1 
ATOM   12897 C CA    . THR D  1 168 ? 21.779  55.450  229.757 1.00 49.64  ? 168 THR D CA    1 
ATOM   12898 C C     . THR D  1 168 ? 21.244  55.293  228.336 1.00 46.89  ? 168 THR D C     1 
ATOM   12899 O O     . THR D  1 168 ? 20.090  55.618  228.063 1.00 45.48  ? 168 THR D O     1 
ATOM   12900 C CB    . THR D  1 168 ? 21.612  56.918  230.187 1.00 46.77  ? 168 THR D CB    1 
ATOM   12901 O OG1   . THR D  1 168 ? 22.343  57.771  229.296 1.00 44.58  ? 168 THR D OG1   1 
ATOM   12902 C CG2   . THR D  1 168 ? 22.106  57.116  231.608 1.00 54.49  ? 168 THR D CG2   1 
ATOM   12903 N N     . VAL D  1 169 ? 22.088  54.801  227.435 1.00 46.56  ? 169 VAL D N     1 
ATOM   12904 C CA    . VAL D  1 169 ? 21.660  54.505  226.071 1.00 39.36  ? 169 VAL D CA    1 
ATOM   12905 C C     . VAL D  1 169 ? 20.642  53.368  226.074 1.00 37.79  ? 169 VAL D C     1 
ATOM   12906 O O     . VAL D  1 169 ? 20.850  52.350  226.731 1.00 37.02  ? 169 VAL D O     1 
ATOM   12907 C CB    . VAL D  1 169 ? 22.858  54.129  225.171 1.00 42.70  ? 169 VAL D CB    1 
ATOM   12908 C CG1   . VAL D  1 169 ? 22.386  53.466  223.891 1.00 34.61  ? 169 VAL D CG1   1 
ATOM   12909 C CG2   . VAL D  1 169 ? 23.692  55.361  224.860 1.00 39.40  ? 169 VAL D CG2   1 
ATOM   12910 N N     . GLY D  1 170 ? 19.539  53.548  225.354 1.00 41.60  ? 170 GLY D N     1 
ATOM   12911 C CA    . GLY D  1 170 ? 18.510  52.527  225.278 1.00 38.16  ? 170 GLY D CA    1 
ATOM   12912 C C     . GLY D  1 170 ? 18.850  51.419  224.298 1.00 36.12  ? 170 GLY D C     1 
ATOM   12913 O O     . GLY D  1 170 ? 19.443  51.667  223.251 1.00 33.95  ? 170 GLY D O     1 
ATOM   12914 N N     . THR D  1 171 ? 18.475  50.190  224.641 1.00 37.57  ? 171 THR D N     1 
ATOM   12915 C CA    . THR D  1 171 ? 18.703  49.042  223.768 1.00 35.27  ? 171 THR D CA    1 
ATOM   12916 C C     . THR D  1 171 ? 17.881  49.152  222.486 1.00 33.17  ? 171 THR D C     1 
ATOM   12917 O O     . THR D  1 171 ? 18.260  48.609  221.447 1.00 30.76  ? 171 THR D O     1 
ATOM   12918 C CB    . THR D  1 171 ? 18.354  47.717  224.469 1.00 35.63  ? 171 THR D CB    1 
ATOM   12919 O OG1   . THR D  1 171 ? 17.033  47.802  225.017 1.00 36.59  ? 171 THR D OG1   1 
ATOM   12920 C CG2   . THR D  1 171 ? 19.348  47.415  225.587 1.00 31.83  ? 171 THR D CG2   1 
ATOM   12921 N N     . GLY D  1 172 ? 16.758  49.860  222.575 1.00 34.70  ? 172 GLY D N     1 
ATOM   12922 C CA    . GLY D  1 172 ? 15.863  50.039  221.447 1.00 32.09  ? 172 GLY D CA    1 
ATOM   12923 C C     . GLY D  1 172 ? 16.535  50.636  220.227 1.00 34.30  ? 172 GLY D C     1 
ATOM   12924 O O     . GLY D  1 172 ? 16.481  50.064  219.140 1.00 34.18  ? 172 GLY D O     1 
ATOM   12925 N N     . GLY D  1 173 ? 17.172  51.787  220.403 1.00 30.07  ? 173 GLY D N     1 
ATOM   12926 C CA    . GLY D  1 173 ? 17.841  52.449  219.302 1.00 32.50  ? 173 GLY D CA    1 
ATOM   12927 C C     . GLY D  1 173 ? 19.238  51.909  219.064 1.00 28.91  ? 173 GLY D C     1 
ATOM   12928 O O     . GLY D  1 173 ? 19.669  51.765  217.920 1.00 32.80  ? 173 GLY D O     1 
ATOM   12929 N N     . HIS D  1 174 ? 19.943  51.601  220.148 1.00 28.92  ? 174 HIS D N     1 
ATOM   12930 C CA    . HIS D  1 174 ? 21.338  51.156  220.077 1.00 31.92  ? 174 HIS D CA    1 
ATOM   12931 C C     . HIS D  1 174 ? 21.519  49.871  219.271 1.00 32.57  ? 174 HIS D C     1 
ATOM   12932 O O     . HIS D  1 174 ? 22.283  49.832  218.307 1.00 30.87  ? 174 HIS D O     1 
ATOM   12933 C CB    . HIS D  1 174 ? 21.889  50.949  221.488 1.00 31.19  ? 174 HIS D CB    1 
ATOM   12934 C CG    . HIS D  1 174 ? 23.367  50.727  221.539 1.00 35.37  ? 174 HIS D CG    1 
ATOM   12935 N ND1   . HIS D  1 174 ? 24.276  51.687  221.152 1.00 37.83  ? 174 HIS D ND1   1 
ATOM   12936 C CD2   . HIS D  1 174 ? 24.096  49.658  221.938 1.00 35.35  ? 174 HIS D CD2   1 
ATOM   12937 C CE1   . HIS D  1 174 ? 25.501  51.219  221.308 1.00 37.94  ? 174 HIS D CE1   1 
ATOM   12938 N NE2   . HIS D  1 174 ? 25.420  49.991  221.786 1.00 34.90  ? 174 HIS D NE2   1 
ATOM   12939 N N     . ILE D  1 175 ? 20.818  48.817  219.680 1.00 32.34  ? 175 ILE D N     1 
ATOM   12940 C CA    . ILE D  1 175 ? 20.911  47.527  219.006 1.00 31.38  ? 175 ILE D CA    1 
ATOM   12941 C C     . ILE D  1 175 ? 20.346  47.620  217.589 1.00 30.23  ? 175 ILE D C     1 
ATOM   12942 O O     . ILE D  1 175 ? 20.840  46.968  216.668 1.00 29.03  ? 175 ILE D O     1 
ATOM   12943 C CB    . ILE D  1 175 ? 20.177  46.426  219.802 1.00 30.45  ? 175 ILE D CB    1 
ATOM   12944 C CG1   . ILE D  1 175 ? 20.834  46.227  221.172 1.00 26.38  ? 175 ILE D CG1   1 
ATOM   12945 C CG2   . ILE D  1 175 ? 20.170  45.112  219.041 1.00 24.22  ? 175 ILE D CG2   1 
ATOM   12946 C CD1   . ILE D  1 175 ? 20.234  45.095  221.984 1.00 34.82  ? 175 ILE D CD1   1 
ATOM   12947 N N     . SER D  1 176 ? 19.327  48.458  217.419 1.00 29.11  ? 176 SER D N     1 
ATOM   12948 C CA    . SER D  1 176 ? 18.711  48.678  216.111 1.00 25.54  ? 176 SER D CA    1 
ATOM   12949 C C     . SER D  1 176 ? 19.688  49.255  215.091 1.00 27.69  ? 176 SER D C     1 
ATOM   12950 O O     . SER D  1 176 ? 19.535  49.048  213.888 1.00 29.58  ? 176 SER D O     1 
ATOM   12951 C CB    . SER D  1 176 ? 17.509  49.615  216.235 1.00 27.85  ? 176 SER D CB    1 
ATOM   12952 O OG    . SER D  1 176 ? 16.427  48.986  216.899 1.00 30.91  ? 176 SER D OG    1 
ATOM   12953 N N     . GLY D  1 177 ? 20.683  49.992  215.573 1.00 26.18  ? 177 GLY D N     1 
ATOM   12954 C CA    . GLY D  1 177 ? 21.639  50.629  214.687 1.00 26.74  ? 177 GLY D CA    1 
ATOM   12955 C C     . GLY D  1 177 ? 22.989  49.936  214.633 1.00 32.59  ? 177 GLY D C     1 
ATOM   12956 O O     . GLY D  1 177 ? 23.898  50.388  213.938 1.00 30.64  ? 177 GLY D O     1 
ATOM   12957 N N     . GLY D  1 178 ? 23.122  48.838  215.368 1.00 31.31  ? 178 GLY D N     1 
ATOM   12958 C CA    . GLY D  1 178 ? 24.383  48.122  215.443 1.00 31.34  ? 178 GLY D CA    1 
ATOM   12959 C C     . GLY D  1 178 ? 24.863  47.988  216.875 1.00 32.20  ? 178 GLY D C     1 
ATOM   12960 O O     . GLY D  1 178 ? 24.565  47.000  217.545 1.00 33.68  ? 178 GLY D O     1 
ATOM   12961 N N     . GLY D  1 179 ? 25.602  48.985  217.350 1.00 28.26  ? 179 GLY D N     1 
ATOM   12962 C CA    . GLY D  1 179 ? 26.048  48.997  218.729 1.00 33.35  ? 179 GLY D CA    1 
ATOM   12963 C C     . GLY D  1 179 ? 27.503  48.619  218.919 1.00 35.84  ? 179 GLY D C     1 
ATOM   12964 O O     . GLY D  1 179 ? 27.829  47.448  219.120 1.00 35.19  ? 179 GLY D O     1 
ATOM   12965 N N     . PHE D  1 180 ? 28.380  49.615  218.876 1.00 37.64  ? 180 PHE D N     1 
ATOM   12966 C CA    . PHE D  1 180 ? 29.816  49.377  218.997 1.00 41.34  ? 180 PHE D CA    1 
ATOM   12967 C C     . PHE D  1 180 ? 30.325  49.685  220.404 1.00 43.17  ? 180 PHE D C     1 
ATOM   12968 O O     . PHE D  1 180 ? 29.913  50.673  221.017 1.00 51.76  ? 180 PHE D O     1 
ATOM   12969 C CB    . PHE D  1 180 ? 30.573  50.215  217.966 1.00 39.47  ? 180 PHE D CB    1 
ATOM   12970 C CG    . PHE D  1 180 ? 32.038  49.900  217.887 1.00 40.66  ? 180 PHE D CG    1 
ATOM   12971 C CD1   . PHE D  1 180 ? 32.491  48.843  217.116 1.00 34.55  ? 180 PHE D CD1   1 
ATOM   12972 C CD2   . PHE D  1 180 ? 32.960  50.661  218.583 1.00 41.90  ? 180 PHE D CD2   1 
ATOM   12973 C CE1   . PHE D  1 180 ? 33.839  48.548  217.042 1.00 42.89  ? 180 PHE D CE1   1 
ATOM   12974 C CE2   . PHE D  1 180 ? 34.311  50.373  218.516 1.00 41.26  ? 180 PHE D CE2   1 
ATOM   12975 C CZ    . PHE D  1 180 ? 34.749  49.315  217.744 1.00 36.35  ? 180 PHE D CZ    1 
ATOM   12976 N N     . GLY D  1 181 ? 31.219  48.839  220.912 1.00 45.70  ? 181 GLY D N     1 
ATOM   12977 C CA    . GLY D  1 181 ? 31.745  49.001  222.258 1.00 48.32  ? 181 GLY D CA    1 
ATOM   12978 C C     . GLY D  1 181 ? 33.154  48.465  222.468 1.00 41.40  ? 181 GLY D C     1 
ATOM   12979 O O     . GLY D  1 181 ? 33.807  48.015  221.528 1.00 38.55  ? 181 GLY D O     1 
ATOM   12980 N N     . MET D  1 182 ? 33.610  48.501  223.718 1.00 44.84  ? 182 MET D N     1 
ATOM   12981 C CA    . MET D  1 182 ? 34.975  48.113  224.074 1.00 50.69  ? 182 MET D CA    1 
ATOM   12982 C C     . MET D  1 182 ? 35.251  46.621  223.878 1.00 50.06  ? 182 MET D C     1 
ATOM   12983 O O     . MET D  1 182 ? 36.407  46.195  223.861 1.00 48.03  ? 182 MET D O     1 
ATOM   12984 C CB    . MET D  1 182 ? 35.269  48.501  225.526 1.00 54.00  ? 182 MET D CB    1 
ATOM   12985 C CG    . MET D  1 182 ? 35.169  49.995  225.811 1.00 51.10  ? 182 MET D CG    1 
ATOM   12986 S SD    . MET D  1 182 ? 36.605  50.925  225.243 1.00 55.28  ? 182 MET D SD    1 
ATOM   12987 C CE    . MET D  1 182 ? 37.890  50.245  226.291 1.00 55.14  ? 182 MET D CE    1 
ATOM   12988 N N     . MET D  1 183 ? 34.196  45.826  223.734 1.00 39.57  ? 183 MET D N     1 
ATOM   12989 C CA    . MET D  1 183 ? 34.362  44.388  223.546 1.00 42.07  ? 183 MET D CA    1 
ATOM   12990 C C     . MET D  1 183 ? 34.042  43.961  222.117 1.00 41.13  ? 183 MET D C     1 
ATOM   12991 O O     . MET D  1 183 ? 34.014  42.769  221.813 1.00 44.40  ? 183 MET D O     1 
ATOM   12992 C CB    . MET D  1 183 ? 33.480  43.607  224.523 1.00 51.91  ? 183 MET D CB    1 
ATOM   12993 C CG    . MET D  1 183 ? 33.632  44.027  225.976 1.00 57.85  ? 183 MET D CG    1 
ATOM   12994 S SD    . MET D  1 183 ? 33.145  42.741  227.146 1.00 67.68  ? 183 MET D SD    1 
ATOM   12995 C CE    . MET D  1 183 ? 31.615  42.160  226.420 1.00 60.81  ? 183 MET D CE    1 
ATOM   12996 N N     . SER D  1 184 ? 33.810  44.935  221.242 1.00 36.62  ? 184 SER D N     1 
ATOM   12997 C CA    . SER D  1 184 ? 33.404  44.643  219.870 1.00 38.73  ? 184 SER D CA    1 
ATOM   12998 C C     . SER D  1 184 ? 34.521  44.007  219.048 1.00 37.15  ? 184 SER D C     1 
ATOM   12999 O O     . SER D  1 184 ? 34.257  43.272  218.099 1.00 38.72  ? 184 SER D O     1 
ATOM   13000 C CB    . SER D  1 184 ? 32.912  45.913  219.177 1.00 36.92  ? 184 SER D CB    1 
ATOM   13001 O OG    . SER D  1 184 ? 31.676  46.340  219.721 1.00 44.04  ? 184 SER D OG    1 
ATOM   13002 N N     . ARG D  1 185 ? 35.768  44.289  219.409 1.00 35.05  ? 185 ARG D N     1 
ATOM   13003 C CA    . ARG D  1 185 ? 36.897  43.665  218.730 1.00 38.09  ? 185 ARG D CA    1 
ATOM   13004 C C     . ARG D  1 185 ? 36.938  42.175  219.065 1.00 33.46  ? 185 ARG D C     1 
ATOM   13005 O O     . ARG D  1 185 ? 37.507  41.374  218.320 1.00 39.35  ? 185 ARG D O     1 
ATOM   13006 C CB    . ARG D  1 185 ? 38.212  44.350  219.112 1.00 33.95  ? 185 ARG D CB    1 
ATOM   13007 C CG    . ARG D  1 185 ? 38.201  45.857  218.875 1.00 38.55  ? 185 ARG D CG    1 
ATOM   13008 C CD    . ARG D  1 185 ? 39.570  46.499  219.065 1.00 32.82  ? 185 ARG D CD    1 
ATOM   13009 N NE    . ARG D  1 185 ? 40.546  46.030  218.080 1.00 38.14  ? 185 ARG D NE    1 
ATOM   13010 C CZ    . ARG D  1 185 ? 41.464  45.101  218.325 1.00 31.94  ? 185 ARG D CZ    1 
ATOM   13011 N NH1   . ARG D  1 185 ? 41.534  44.536  219.524 1.00 37.44  ? 185 ARG D NH1   1 
ATOM   13012 N NH2   . ARG D  1 185 ? 42.307  44.733  217.373 1.00 36.54  ? 185 ARG D NH2   1 
ATOM   13013 N N     . LYS D  1 186 ? 36.324  41.813  220.188 1.00 33.68  ? 186 LYS D N     1 
ATOM   13014 C CA    . LYS D  1 186 ? 36.215  40.414  220.587 1.00 43.84  ? 186 LYS D CA    1 
ATOM   13015 C C     . LYS D  1 186 ? 34.902  39.783  220.129 1.00 41.11  ? 186 LYS D C     1 
ATOM   13016 O O     . LYS D  1 186 ? 34.882  38.630  219.711 1.00 41.91  ? 186 LYS D O     1 
ATOM   13017 C CB    . LYS D  1 186 ? 36.344  40.271  222.105 1.00 47.61  ? 186 LYS D CB    1 
ATOM   13018 C CG    . LYS D  1 186 ? 37.209  39.090  222.554 1.00 53.64  ? 186 LYS D CG    1 
ATOM   13019 C CD    . LYS D  1 186 ? 36.674  37.759  222.039 1.00 54.01  ? 186 LYS D CD    1 
ATOM   13020 C CE    . LYS D  1 186 ? 37.571  36.594  222.404 1.00 57.74  ? 186 LYS D CE    1 
ATOM   13021 N NZ    . LYS D  1 186 ? 37.546  36.322  223.864 1.00 60.21  ? 186 LYS D NZ    1 
ATOM   13022 N N     . TYR D  1 187 ? 33.801  40.518  220.222 1.00 43.17  ? 187 TYR D N     1 
ATOM   13023 C CA    . TYR D  1 187 ? 32.501  39.895  219.994 1.00 39.51  ? 187 TYR D CA    1 
ATOM   13024 C C     . TYR D  1 187 ? 31.646  40.572  218.927 1.00 42.81  ? 187 TYR D C     1 
ATOM   13025 O O     . TYR D  1 187 ? 30.528  40.133  218.657 1.00 40.38  ? 187 TYR D O     1 
ATOM   13026 C CB    . TYR D  1 187 ? 31.720  39.841  221.306 1.00 38.84  ? 187 TYR D CB    1 
ATOM   13027 C CG    . TYR D  1 187 ? 32.253  38.838  222.307 1.00 44.02  ? 187 TYR D CG    1 
ATOM   13028 C CD1   . TYR D  1 187 ? 32.366  37.492  221.980 1.00 41.69  ? 187 TYR D CD1   1 
ATOM   13029 C CD2   . TYR D  1 187 ? 32.621  39.233  223.587 1.00 46.56  ? 187 TYR D CD2   1 
ATOM   13030 C CE1   . TYR D  1 187 ? 32.846  36.571  222.893 1.00 50.39  ? 187 TYR D CE1   1 
ATOM   13031 C CE2   . TYR D  1 187 ? 33.099  38.318  224.509 1.00 50.04  ? 187 TYR D CE2   1 
ATOM   13032 C CZ    . TYR D  1 187 ? 33.209  36.990  224.156 1.00 51.26  ? 187 TYR D CZ    1 
ATOM   13033 O OH    . TYR D  1 187 ? 33.680  36.079  225.070 1.00 48.43  ? 187 TYR D OH    1 
ATOM   13034 N N     . GLY D  1 188 ? 32.165  41.633  218.320 1.00 37.42  ? 188 GLY D N     1 
ATOM   13035 C CA    . GLY D  1 188 ? 31.409  42.366  217.323 1.00 38.41  ? 188 GLY D CA    1 
ATOM   13036 C C     . GLY D  1 188 ? 30.368  43.266  217.961 1.00 33.78  ? 188 GLY D C     1 
ATOM   13037 O O     . GLY D  1 188 ? 30.405  43.522  219.164 1.00 37.22  ? 188 GLY D O     1 
ATOM   13038 N N     . LEU D  1 189 ? 29.429  43.740  217.150 1.00 31.62  ? 189 LEU D N     1 
ATOM   13039 C CA    . LEU D  1 189 ? 28.407  44.663  217.623 1.00 32.76  ? 189 LEU D CA    1 
ATOM   13040 C C     . LEU D  1 189 ? 27.372  43.971  218.501 1.00 34.24  ? 189 LEU D C     1 
ATOM   13041 O O     . LEU D  1 189 ? 27.244  42.745  218.481 1.00 32.60  ? 189 LEU D O     1 
ATOM   13042 C CB    . LEU D  1 189 ? 27.713  45.338  216.437 1.00 28.42  ? 189 LEU D CB    1 
ATOM   13043 C CG    . LEU D  1 189 ? 28.652  45.958  215.402 1.00 32.46  ? 189 LEU D CG    1 
ATOM   13044 C CD1   . LEU D  1 189 ? 27.867  46.528  214.249 1.00 23.74  ? 189 LEU D CD1   1 
ATOM   13045 C CD2   . LEU D  1 189 ? 29.523  47.028  216.040 1.00 32.33  ? 189 LEU D CD2   1 
ATOM   13046 N N     . ALA D  1 190 ? 26.634  44.767  219.270 1.00 35.77  ? 190 ALA D N     1 
ATOM   13047 C CA    . ALA D  1 190 ? 25.526  44.259  220.070 1.00 34.09  ? 190 ALA D CA    1 
ATOM   13048 C C     . ALA D  1 190 ? 24.520  43.529  219.189 1.00 30.35  ? 190 ALA D C     1 
ATOM   13049 O O     . ALA D  1 190 ? 23.975  42.496  219.572 1.00 37.72  ? 190 ALA D O     1 
ATOM   13050 C CB    . ALA D  1 190 ? 24.847  45.396  220.813 1.00 32.83  ? 190 ALA D CB    1 
ATOM   13051 N N     . ALA D  1 191 ? 24.288  44.085  218.004 1.00 29.22  ? 191 ALA D N     1 
ATOM   13052 C CA    . ALA D  1 191 ? 23.342  43.529  217.048 1.00 33.31  ? 191 ALA D CA    1 
ATOM   13053 C C     . ALA D  1 191 ? 23.844  42.225  216.435 1.00 34.47  ? 191 ALA D C     1 
ATOM   13054 O O     . ALA D  1 191 ? 23.052  41.420  215.947 1.00 32.53  ? 191 ALA D O     1 
ATOM   13055 C CB    . ALA D  1 191 ? 23.051  44.541  215.955 1.00 30.06  ? 191 ALA D CB    1 
ATOM   13056 N N     . ASP D  1 192 ? 25.160  42.026  216.452 1.00 34.34  ? 192 ASP D N     1 
ATOM   13057 C CA    . ASP D  1 192 ? 25.760  40.796  215.939 1.00 30.36  ? 192 ASP D CA    1 
ATOM   13058 C C     . ASP D  1 192 ? 25.460  39.616  216.851 1.00 30.35  ? 192 ASP D C     1 
ATOM   13059 O O     . ASP D  1 192 ? 25.613  38.462  216.455 1.00 36.03  ? 192 ASP D O     1 
ATOM   13060 C CB    . ASP D  1 192 ? 27.280  40.946  215.787 1.00 33.87  ? 192 ASP D CB    1 
ATOM   13061 C CG    . ASP D  1 192 ? 27.668  41.918  214.689 1.00 37.22  ? 192 ASP D CG    1 
ATOM   13062 O OD1   . ASP D  1 192 ? 26.921  42.025  213.696 1.00 34.84  ? 192 ASP D OD1   1 
ATOM   13063 O OD2   . ASP D  1 192 ? 28.725  42.572  214.819 1.00 39.50  ? 192 ASP D OD2   1 
ATOM   13064 N N     . ASN D  1 193 ? 25.055  39.913  218.081 1.00 28.20  ? 193 ASN D N     1 
ATOM   13065 C CA    . ASN D  1 193 ? 24.799  38.874  219.073 1.00 29.88  ? 193 ASN D CA    1 
ATOM   13066 C C     . ASN D  1 193 ? 23.318  38.742  219.429 1.00 38.68  ? 193 ASN D C     1 
ATOM   13067 O O     . ASN D  1 193 ? 22.970  38.322  220.533 1.00 38.22  ? 193 ASN D O     1 
ATOM   13068 C CB    . ASN D  1 193 ? 25.620  39.139  220.333 1.00 31.49  ? 193 ASN D CB    1 
ATOM   13069 C CG    . ASN D  1 193 ? 27.116  39.080  220.070 1.00 38.05  ? 193 ASN D CG    1 
ATOM   13070 O OD1   . ASN D  1 193 ? 27.732  38.021  220.170 1.00 37.72  ? 193 ASN D OD1   1 
ATOM   13071 N ND2   . ASN D  1 193 ? 27.703  40.218  219.725 1.00 35.15  ? 193 ASN D ND2   1 
ATOM   13072 N N     . VAL D  1 194 ? 22.451  39.100  218.486 1.00 35.22  ? 194 VAL D N     1 
ATOM   13073 C CA    . VAL D  1 194 ? 21.008  38.969  218.666 1.00 30.87  ? 194 VAL D CA    1 
ATOM   13074 C C     . VAL D  1 194 ? 20.496  37.729  217.939 1.00 35.28  ? 194 VAL D C     1 
ATOM   13075 O O     . VAL D  1 194 ? 20.712  37.579  216.740 1.00 36.50  ? 194 VAL D O     1 
ATOM   13076 C CB    . VAL D  1 194 ? 20.258  40.215  218.151 1.00 29.74  ? 194 VAL D CB    1 
ATOM   13077 C CG1   . VAL D  1 194 ? 18.752  39.961  218.118 1.00 28.41  ? 194 VAL D CG1   1 
ATOM   13078 C CG2   . VAL D  1 194 ? 20.585  41.425  219.011 1.00 30.29  ? 194 VAL D CG2   1 
ATOM   13079 N N     . VAL D  1 195 ? 19.813  36.845  218.659 1.00 33.67  ? 195 VAL D N     1 
ATOM   13080 C CA    . VAL D  1 195 ? 19.378  35.578  218.072 1.00 33.85  ? 195 VAL D CA    1 
ATOM   13081 C C     . VAL D  1 195 ? 17.873  35.515  217.820 1.00 35.24  ? 195 VAL D C     1 
ATOM   13082 O O     . VAL D  1 195 ? 17.400  34.690  217.038 1.00 37.81  ? 195 VAL D O     1 
ATOM   13083 C CB    . VAL D  1 195 ? 19.782  34.390  218.960 1.00 37.98  ? 195 VAL D CB    1 
ATOM   13084 C CG1   . VAL D  1 195 ? 21.300  34.295  219.052 1.00 31.30  ? 195 VAL D CG1   1 
ATOM   13085 C CG2   . VAL D  1 195 ? 19.154  34.521  220.345 1.00 36.43  ? 195 VAL D CG2   1 
ATOM   13086 N N     . ASP D  1 196 ? 17.126  36.387  218.485 1.00 35.63  ? 196 ASP D N     1 
ATOM   13087 C CA    . ASP D  1 196 ? 15.689  36.480  218.270 1.00 36.66  ? 196 ASP D CA    1 
ATOM   13088 C C     . ASP D  1 196 ? 15.208  37.863  218.692 1.00 37.02  ? 196 ASP D C     1 
ATOM   13089 O O     . ASP D  1 196 ? 15.938  38.605  219.348 1.00 36.33  ? 196 ASP D O     1 
ATOM   13090 C CB    . ASP D  1 196 ? 14.951  35.387  219.045 1.00 37.18  ? 196 ASP D CB    1 
ATOM   13091 C CG    . ASP D  1 196 ? 13.632  35.005  218.407 1.00 37.85  ? 196 ASP D CG    1 
ATOM   13092 O OD1   . ASP D  1 196 ? 13.023  35.851  217.716 1.00 44.95  ? 196 ASP D OD1   1 
ATOM   13093 O OD2   . ASP D  1 196 ? 13.201  33.847  218.596 1.00 47.49  ? 196 ASP D OD2   1 
ATOM   13094 N N     . ALA D  1 197 ? 13.984  38.209  218.311 1.00 32.66  ? 197 ALA D N     1 
ATOM   13095 C CA    . ALA D  1 197 ? 13.424  39.503  218.666 1.00 34.95  ? 197 ALA D CA    1 
ATOM   13096 C C     . ALA D  1 197 ? 11.917  39.507  218.506 1.00 33.79  ? 197 ALA D C     1 
ATOM   13097 O O     . ALA D  1 197 ? 11.367  38.782  217.678 1.00 29.70  ? 197 ALA D O     1 
ATOM   13098 C CB    . ALA D  1 197 ? 14.040  40.606  217.818 1.00 29.76  ? 197 ALA D CB    1 
ATOM   13099 N N     . ILE D  1 198 ? 11.248  40.328  219.303 1.00 32.55  ? 198 ILE D N     1 
ATOM   13100 C CA    . ILE D  1 198 ? 9.831   40.563  219.085 1.00 31.06  ? 198 ILE D CA    1 
ATOM   13101 C C     . ILE D  1 198 ? 9.665   41.903  218.386 1.00 31.62  ? 198 ILE D C     1 
ATOM   13102 O O     . ILE D  1 198 ? 9.998   42.949  218.940 1.00 34.04  ? 198 ILE D O     1 
ATOM   13103 C CB    . ILE D  1 198 ? 9.032   40.550  220.393 1.00 32.45  ? 198 ILE D CB    1 
ATOM   13104 C CG1   . ILE D  1 198 ? 9.250   39.227  221.129 1.00 30.77  ? 198 ILE D CG1   1 
ATOM   13105 C CG2   . ILE D  1 198 ? 7.553   40.756  220.105 1.00 32.43  ? 198 ILE D CG2   1 
ATOM   13106 C CD1   . ILE D  1 198 ? 8.943   38.016  220.285 1.00 34.49  ? 198 ILE D CD1   1 
ATOM   13107 N N     . LEU D  1 199 ? 9.172   41.856  217.154 1.00 30.24  ? 199 LEU D N     1 
ATOM   13108 C CA    . LEU D  1 199 ? 8.908   43.059  216.380 1.00 27.74  ? 199 LEU D CA    1 
ATOM   13109 C C     . LEU D  1 199 ? 7.405   43.250  216.216 1.00 34.27  ? 199 LEU D C     1 
ATOM   13110 O O     . LEU D  1 199 ? 6.680   42.312  215.885 1.00 29.93  ? 199 LEU D O     1 
ATOM   13111 C CB    . LEU D  1 199 ? 9.591   42.981  215.015 1.00 30.44  ? 199 LEU D CB    1 
ATOM   13112 C CG    . LEU D  1 199 ? 9.356   44.151  214.059 1.00 32.53  ? 199 LEU D CG    1 
ATOM   13113 C CD1   . LEU D  1 199 ? 10.025  45.430  214.559 1.00 29.35  ? 199 LEU D CD1   1 
ATOM   13114 C CD2   . LEU D  1 199 ? 9.842   43.788  212.672 1.00 30.06  ? 199 LEU D CD2   1 
ATOM   13115 N N     . ILE D  1 200 ? 6.938   44.467  216.466 1.00 32.75  ? 200 ILE D N     1 
ATOM   13116 C CA    . ILE D  1 200 ? 5.526   44.786  216.308 1.00 30.90  ? 200 ILE D CA    1 
ATOM   13117 C C     . ILE D  1 200 ? 5.350   45.697  215.100 1.00 31.60  ? 200 ILE D C     1 
ATOM   13118 O O     . ILE D  1 200 ? 5.851   46.822  215.091 1.00 27.82  ? 200 ILE D O     1 
ATOM   13119 C CB    . ILE D  1 200 ? 4.961   45.450  217.574 1.00 29.82  ? 200 ILE D CB    1 
ATOM   13120 C CG1   . ILE D  1 200 ? 5.137   44.515  218.773 1.00 31.55  ? 200 ILE D CG1   1 
ATOM   13121 C CG2   . ILE D  1 200 ? 3.497   45.795  217.384 1.00 32.12  ? 200 ILE D CG2   1 
ATOM   13122 C CD1   . ILE D  1 200 ? 4.571   45.054  220.065 1.00 35.62  ? 200 ILE D CD1   1 
ATOM   13123 N N     . ASP D  1 201 ? 4.652   45.214  214.074 1.00 30.60  ? 201 ASP D N     1 
ATOM   13124 C CA    . ASP D  1 201 ? 4.599   45.945  212.809 1.00 29.08  ? 201 ASP D CA    1 
ATOM   13125 C C     . ASP D  1 201 ? 3.473   46.965  212.779 1.00 30.67  ? 201 ASP D C     1 
ATOM   13126 O O     . ASP D  1 201 ? 2.778   47.160  213.775 1.00 30.53  ? 201 ASP D O     1 
ATOM   13127 C CB    . ASP D  1 201 ? 4.484   44.980  211.612 1.00 32.33  ? 201 ASP D CB    1 
ATOM   13128 C CG    . ASP D  1 201 ? 3.117   44.295  211.500 1.00 36.61  ? 201 ASP D CG    1 
ATOM   13129 O OD1   . ASP D  1 201 ? 2.178   44.597  212.269 1.00 32.64  ? 201 ASP D OD1   1 
ATOM   13130 O OD2   . ASP D  1 201 ? 2.987   43.437  210.600 1.00 34.26  ? 201 ASP D OD2   1 
ATOM   13131 N N     . ALA D  1 202 ? 3.296   47.598  211.624 1.00 33.82  ? 202 ALA D N     1 
ATOM   13132 C CA    . ALA D  1 202 ? 2.370   48.714  211.483 1.00 36.59  ? 202 ALA D CA    1 
ATOM   13133 C C     . ALA D  1 202 ? 0.913   48.340  211.752 1.00 37.11  ? 202 ALA D C     1 
ATOM   13134 O O     . ALA D  1 202 ? 0.093   49.207  212.057 1.00 34.05  ? 202 ALA D O     1 
ATOM   13135 C CB    . ALA D  1 202 ? 2.497   49.320  210.094 1.00 39.38  ? 202 ALA D CB    1 
ATOM   13136 N N     . ASN D  1 203 ? 0.590   47.056  211.642 1.00 36.78  ? 203 ASN D N     1 
ATOM   13137 C CA    . ASN D  1 203 ? -0.775  46.596  211.896 1.00 32.48  ? 203 ASN D CA    1 
ATOM   13138 C C     . ASN D  1 203 ? -0.962  46.110  213.331 1.00 31.90  ? 203 ASN D C     1 
ATOM   13139 O O     . ASN D  1 203 ? -2.053  45.687  213.715 1.00 32.99  ? 203 ASN D O     1 
ATOM   13140 C CB    . ASN D  1 203 ? -1.159  45.483  210.922 1.00 33.05  ? 203 ASN D CB    1 
ATOM   13141 C CG    . ASN D  1 203 ? -1.079  45.924  209.472 1.00 36.60  ? 203 ASN D CG    1 
ATOM   13142 O OD1   . ASN D  1 203 ? -0.473  45.250  208.640 1.00 44.59  ? 203 ASN D OD1   1 
ATOM   13143 N ND2   . ASN D  1 203 ? -1.686  47.065  209.165 1.00 41.49  ? 203 ASN D ND2   1 
ATOM   13144 N N     . GLY D  1 204 ? 0.102   46.177  214.124 1.00 28.19  ? 204 GLY D N     1 
ATOM   13145 C CA    . GLY D  1 204 ? 0.052   45.726  215.502 1.00 31.39  ? 204 GLY D CA    1 
ATOM   13146 C C     . GLY D  1 204 ? 0.340   44.242  215.637 1.00 30.45  ? 204 GLY D C     1 
ATOM   13147 O O     . GLY D  1 204 ? 0.232   43.673  216.724 1.00 29.33  ? 204 GLY D O     1 
ATOM   13148 N N     . ALA D  1 205 ? 0.704   43.611  214.526 1.00 29.21  ? 205 ALA D N     1 
ATOM   13149 C CA    . ALA D  1 205 ? 1.045   42.192  214.535 1.00 35.20  ? 205 ALA D CA    1 
ATOM   13150 C C     . ALA D  1 205 ? 2.319   41.953  215.340 1.00 33.96  ? 205 ALA D C     1 
ATOM   13151 O O     . ALA D  1 205 ? 3.330   42.621  215.133 1.00 31.92  ? 205 ALA D O     1 
ATOM   13152 C CB    . ALA D  1 205 ? 1.202   41.671  213.111 1.00 31.22  ? 205 ALA D CB    1 
ATOM   13153 N N     . ILE D  1 206 ? 2.255   41.003  216.266 1.00 32.37  ? 206 ILE D N     1 
ATOM   13154 C CA    . ILE D  1 206 ? 3.378   40.702  217.141 1.00 31.42  ? 206 ILE D CA    1 
ATOM   13155 C C     . ILE D  1 206 ? 4.191   39.548  216.563 1.00 38.41  ? 206 ILE D C     1 
ATOM   13156 O O     . ILE D  1 206 ? 3.743   38.403  216.568 1.00 29.99  ? 206 ILE D O     1 
ATOM   13157 C CB    . ILE D  1 206 ? 2.892   40.353  218.559 1.00 35.41  ? 206 ILE D CB    1 
ATOM   13158 C CG1   . ILE D  1 206 ? 2.059   41.506  219.120 1.00 30.94  ? 206 ILE D CG1   1 
ATOM   13159 C CG2   . ILE D  1 206 ? 4.067   40.039  219.468 1.00 31.64  ? 206 ILE D CG2   1 
ATOM   13160 C CD1   . ILE D  1 206 ? 1.410   41.210  220.454 1.00 37.12  ? 206 ILE D CD1   1 
ATOM   13161 N N     . LEU D  1 207 ? 5.386   39.859  216.066 1.00 32.39  ? 207 LEU D N     1 
ATOM   13162 C CA    . LEU D  1 207 ? 6.186   38.901  215.305 1.00 32.19  ? 207 LEU D CA    1 
ATOM   13163 C C     . LEU D  1 207 ? 7.505   38.537  215.989 1.00 35.06  ? 207 LEU D C     1 
ATOM   13164 O O     . LEU D  1 207 ? 8.195   39.405  216.526 1.00 35.05  ? 207 LEU D O     1 
ATOM   13165 C CB    . LEU D  1 207 ? 6.487   39.466  213.909 1.00 33.61  ? 207 LEU D CB    1 
ATOM   13166 C CG    . LEU D  1 207 ? 5.325   40.069  213.109 1.00 33.17  ? 207 LEU D CG    1 
ATOM   13167 C CD1   . LEU D  1 207 ? 5.852   40.832  211.905 1.00 31.72  ? 207 LEU D CD1   1 
ATOM   13168 C CD2   . LEU D  1 207 ? 4.338   38.994  212.667 1.00 31.56  ? 207 LEU D CD2   1 
ATOM   13169 N N     . ASP D  1 208 ? 7.861   37.256  215.960 1.00 33.26  ? 208 ASP D N     1 
ATOM   13170 C CA    . ASP D  1 208 ? 9.210   36.850  216.344 1.00 30.99  ? 208 ASP D CA    1 
ATOM   13171 C C     . ASP D  1 208 ? 10.039  36.609  215.087 1.00 27.16  ? 208 ASP D C     1 
ATOM   13172 O O     . ASP D  1 208 ? 9.582   36.896  213.983 1.00 30.31  ? 208 ASP D O     1 
ATOM   13173 C CB    . ASP D  1 208 ? 9.195   35.605  217.241 1.00 39.85  ? 208 ASP D CB    1 
ATOM   13174 C CG    . ASP D  1 208 ? 8.571   34.389  216.569 1.00 36.16  ? 208 ASP D CG    1 
ATOM   13175 O OD1   . ASP D  1 208 ? 8.199   34.455  215.375 1.00 32.46  ? 208 ASP D OD1   1 
ATOM   13176 O OD2   . ASP D  1 208 ? 8.465   33.351  217.251 1.00 40.74  ? 208 ASP D OD2   1 
ATOM   13177 N N     . ARG D  1 209 ? 11.248  36.083  215.259 1.00 35.78  ? 209 ARG D N     1 
ATOM   13178 C CA    . ARG D  1 209 ? 12.140  35.843  214.129 1.00 34.40  ? 209 ARG D CA    1 
ATOM   13179 C C     . ARG D  1 209 ? 11.492  34.955  213.068 1.00 34.73  ? 209 ARG D C     1 
ATOM   13180 O O     . ARG D  1 209 ? 11.531  35.269  211.879 1.00 35.15  ? 209 ARG D O     1 
ATOM   13181 C CB    . ARG D  1 209 ? 13.450  35.211  214.601 1.00 32.74  ? 209 ARG D CB    1 
ATOM   13182 C CG    . ARG D  1 209 ? 14.424  34.919  213.476 1.00 34.47  ? 209 ARG D CG    1 
ATOM   13183 C CD    . ARG D  1 209 ? 15.762  34.416  213.999 1.00 37.35  ? 209 ARG D CD    1 
ATOM   13184 N NE    . ARG D  1 209 ? 16.718  34.214  212.912 1.00 39.50  ? 209 ARG D NE    1 
ATOM   13185 C CZ    . ARG D  1 209 ? 17.999  33.908  213.086 1.00 40.74  ? 209 ARG D CZ    1 
ATOM   13186 N NH1   . ARG D  1 209 ? 18.488  33.770  214.311 1.00 33.31  ? 209 ARG D NH1   1 
ATOM   13187 N NH2   . ARG D  1 209 ? 18.793  33.745  212.037 1.00 38.20  ? 209 ARG D NH2   1 
ATOM   13188 N N     . GLN D  1 210 ? 10.893  33.853  213.510 1.00 36.98  ? 210 GLN D N     1 
ATOM   13189 C CA    . GLN D  1 210 ? 10.202  32.935  212.610 1.00 37.55  ? 210 GLN D CA    1 
ATOM   13190 C C     . GLN D  1 210 ? 9.120   33.650  211.806 1.00 35.34  ? 210 GLN D C     1 
ATOM   13191 O O     . GLN D  1 210 ? 9.012   33.477  210.591 1.00 36.85  ? 210 GLN D O     1 
ATOM   13192 C CB    . GLN D  1 210 ? 9.585   31.775  213.396 1.00 44.31  ? 210 GLN D CB    1 
ATOM   13193 C CG    . GLN D  1 210 ? 8.905   30.733  212.520 1.00 55.18  ? 210 GLN D CG    1 
ATOM   13194 C CD    . GLN D  1 210 ? 8.486   29.493  213.292 1.00 59.65  ? 210 GLN D CD    1 
ATOM   13195 O OE1   . GLN D  1 210 ? 8.263   29.544  214.502 1.00 62.69  ? 210 GLN D OE1   1 
ATOM   13196 N NE2   . GLN D  1 210 ? 8.384   28.369  212.592 1.00 57.15  ? 210 GLN D NE2   1 
ATOM   13197 N N     . ALA D  1 211 ? 8.334   34.467  212.497 1.00 31.75  ? 211 ALA D N     1 
ATOM   13198 C CA    . ALA D  1 211 ? 7.196   35.143  211.887 1.00 30.33  ? 211 ALA D CA    1 
ATOM   13199 C C     . ALA D  1 211 ? 7.599   36.262  210.929 1.00 39.37  ? 211 ALA D C     1 
ATOM   13200 O O     . ALA D  1 211 ? 6.992   36.425  209.870 1.00 33.70  ? 211 ALA D O     1 
ATOM   13201 C CB    . ALA D  1 211 ? 6.281   35.692  212.966 1.00 32.51  ? 211 ALA D CB    1 
ATOM   13202 N N     . MET D  1 212 ? 8.613   37.038  211.301 1.00 36.60  ? 212 MET D N     1 
ATOM   13203 C CA    . MET D  1 212 ? 8.998   38.196  210.498 1.00 35.83  ? 212 MET D CA    1 
ATOM   13204 C C     . MET D  1 212 ? 9.848   37.804  209.289 1.00 33.64  ? 212 MET D C     1 
ATOM   13205 O O     . MET D  1 212 ? 9.933   38.555  208.319 1.00 37.67  ? 212 MET D O     1 
ATOM   13206 C CB    . MET D  1 212 ? 9.745   39.227  211.354 1.00 35.64  ? 212 MET D CB    1 
ATOM   13207 C CG    . MET D  1 212 ? 11.157  38.823  211.755 1.00 36.04  ? 212 MET D CG    1 
ATOM   13208 S SD    . MET D  1 212 ? 11.999  40.115  212.699 1.00 36.89  ? 212 MET D SD    1 
ATOM   13209 C CE    . MET D  1 212 ? 11.405  39.782  214.354 1.00 28.26  ? 212 MET D CE    1 
ATOM   13210 N N     . GLY D  1 213 ? 10.470  36.632  209.342 1.00 36.34  ? 213 GLY D N     1 
ATOM   13211 C CA    . GLY D  1 213 ? 11.325  36.185  208.256 1.00 37.62  ? 213 GLY D CA    1 
ATOM   13212 C C     . GLY D  1 213 ? 12.747  36.691  208.414 1.00 44.20  ? 213 GLY D C     1 
ATOM   13213 O O     . GLY D  1 213 ? 13.004  37.614  209.187 1.00 36.59  ? 213 GLY D O     1 
ATOM   13214 N N     . GLU D  1 214 ? 13.674  36.096  207.668 1.00 43.78  ? 214 GLU D N     1 
ATOM   13215 C CA    . GLU D  1 214 ? 15.096  36.375  207.854 1.00 39.03  ? 214 GLU D CA    1 
ATOM   13216 C C     . GLU D  1 214 ? 15.539  37.710  207.276 1.00 32.06  ? 214 GLU D C     1 
ATOM   13217 O O     . GLU D  1 214 ? 16.505  38.295  207.756 1.00 42.48  ? 214 GLU D O     1 
ATOM   13218 C CB    . GLU D  1 214 ? 15.940  35.252  207.251 1.00 41.14  ? 214 GLU D CB    1 
ATOM   13219 C CG    . GLU D  1 214 ? 15.915  33.969  208.059 1.00 34.10  ? 214 GLU D CG    1 
ATOM   13220 C CD    . GLU D  1 214 ? 16.499  34.140  209.448 1.00 38.89  ? 214 GLU D CD    1 
ATOM   13221 O OE1   . GLU D  1 214 ? 17.689  34.499  209.557 1.00 44.65  ? 214 GLU D OE1   1 
ATOM   13222 O OE2   . GLU D  1 214 ? 15.766  33.917  210.436 1.00 39.77  ? 214 GLU D OE2   1 
ATOM   13223 N N     . ASP D  1 215 ? 14.848  38.188  206.246 1.00 37.26  ? 215 ASP D N     1 
ATOM   13224 C CA    . ASP D  1 215 ? 15.147  39.505  205.682 1.00 41.81  ? 215 ASP D CA    1 
ATOM   13225 C C     . ASP D  1 215 ? 14.905  40.612  206.703 1.00 42.14  ? 215 ASP D C     1 
ATOM   13226 O O     . ASP D  1 215 ? 15.723  41.521  206.859 1.00 37.21  ? 215 ASP D O     1 
ATOM   13227 C CB    . ASP D  1 215 ? 14.315  39.768  204.427 1.00 40.77  ? 215 ASP D CB    1 
ATOM   13228 C CG    . ASP D  1 215 ? 14.989  39.262  203.167 1.00 50.28  ? 215 ASP D CG    1 
ATOM   13229 O OD1   . ASP D  1 215 ? 16.211  39.000  203.214 1.00 51.72  ? 215 ASP D OD1   1 
ATOM   13230 O OD2   . ASP D  1 215 ? 14.308  39.142  202.125 1.00 53.26  ? 215 ASP D OD2   1 
ATOM   13231 N N     . VAL D  1 216 ? 13.778  40.524  207.400 1.00 38.28  ? 216 VAL D N     1 
ATOM   13232 C CA    . VAL D  1 216 ? 13.404  41.523  208.393 1.00 34.84  ? 216 VAL D CA    1 
ATOM   13233 C C     . VAL D  1 216 ? 14.215  41.367  209.679 1.00 35.47  ? 216 VAL D C     1 
ATOM   13234 O O     . VAL D  1 216 ? 14.638  42.361  210.273 1.00 31.37  ? 216 VAL D O     1 
ATOM   13235 C CB    . VAL D  1 216 ? 11.898  41.446  208.712 1.00 37.57  ? 216 VAL D CB    1 
ATOM   13236 C CG1   . VAL D  1 216 ? 11.552  42.357  209.874 1.00 35.65  ? 216 VAL D CG1   1 
ATOM   13237 C CG2   . VAL D  1 216 ? 11.084  41.820  207.482 1.00 36.07  ? 216 VAL D CG2   1 
ATOM   13238 N N     . PHE D  1 217 ? 14.441  40.125  210.103 1.00 31.44  ? 217 PHE D N     1 
ATOM   13239 C CA    . PHE D  1 217 ? 15.253  39.875  211.291 1.00 34.78  ? 217 PHE D CA    1 
ATOM   13240 C C     . PHE D  1 217 ? 16.687  40.339  211.066 1.00 35.53  ? 217 PHE D C     1 
ATOM   13241 O O     . PHE D  1 217 ? 17.408  40.666  212.009 1.00 31.74  ? 217 PHE D O     1 
ATOM   13242 C CB    . PHE D  1 217 ? 15.235  38.395  211.675 1.00 32.59  ? 217 PHE D CB    1 
ATOM   13243 C CG    . PHE D  1 217 ? 16.102  38.074  212.856 1.00 32.28  ? 217 PHE D CG    1 
ATOM   13244 C CD1   . PHE D  1 217 ? 15.716  38.448  214.131 1.00 33.03  ? 217 PHE D CD1   1 
ATOM   13245 C CD2   . PHE D  1 217 ? 17.310  37.412  212.692 1.00 32.98  ? 217 PHE D CD2   1 
ATOM   13246 C CE1   . PHE D  1 217 ? 16.511  38.164  215.222 1.00 33.61  ? 217 PHE D CE1   1 
ATOM   13247 C CE2   . PHE D  1 217 ? 18.110  37.125  213.780 1.00 33.31  ? 217 PHE D CE2   1 
ATOM   13248 C CZ    . PHE D  1 217 ? 17.710  37.501  215.047 1.00 31.13  ? 217 PHE D CZ    1 
ATOM   13249 N N     . TRP D  1 218 ? 17.089  40.355  209.803 1.00 33.72  ? 218 TRP D N     1 
ATOM   13250 C CA    . TRP D  1 218 ? 18.390  40.866  209.410 1.00 34.87  ? 218 TRP D CA    1 
ATOM   13251 C C     . TRP D  1 218 ? 18.406  42.388  209.508 1.00 38.18  ? 218 TRP D C     1 
ATOM   13252 O O     . TRP D  1 218 ? 19.306  42.972  210.109 1.00 37.06  ? 218 TRP D O     1 
ATOM   13253 C CB    . TRP D  1 218 ? 18.724  40.402  207.989 1.00 33.20  ? 218 TRP D CB    1 
ATOM   13254 C CG    . TRP D  1 218 ? 19.973  40.972  207.410 1.00 44.05  ? 218 TRP D CG    1 
ATOM   13255 C CD1   . TRP D  1 218 ? 21.247  40.521  207.601 1.00 36.74  ? 218 TRP D CD1   1 
ATOM   13256 C CD2   . TRP D  1 218 ? 20.072  42.088  206.520 1.00 37.38  ? 218 TRP D CD2   1 
ATOM   13257 N NE1   . TRP D  1 218 ? 22.133  41.294  206.893 1.00 38.09  ? 218 TRP D NE1   1 
ATOM   13258 C CE2   . TRP D  1 218 ? 21.436  42.264  206.221 1.00 36.73  ? 218 TRP D CE2   1 
ATOM   13259 C CE3   . TRP D  1 218 ? 19.138  42.962  205.952 1.00 37.94  ? 218 TRP D CE3   1 
ATOM   13260 C CZ2   . TRP D  1 218 ? 21.891  43.278  205.377 1.00 41.21  ? 218 TRP D CZ2   1 
ATOM   13261 C CZ3   . TRP D  1 218 ? 19.591  43.965  205.115 1.00 40.12  ? 218 TRP D CZ3   1 
ATOM   13262 C CH2   . TRP D  1 218 ? 20.955  44.116  204.836 1.00 37.12  ? 218 TRP D CH2   1 
ATOM   13263 N N     . ALA D  1 219 ? 17.383  43.020  208.942 1.00 33.26  ? 219 ALA D N     1 
ATOM   13264 C CA    . ALA D  1 219 ? 17.304  44.477  208.862 1.00 33.24  ? 219 ALA D CA    1 
ATOM   13265 C C     . ALA D  1 219 ? 17.308  45.166  210.224 1.00 31.61  ? 219 ALA D C     1 
ATOM   13266 O O     . ALA D  1 219 ? 17.926  46.212  210.390 1.00 33.30  ? 219 ALA D O     1 
ATOM   13267 C CB    . ALA D  1 219 ? 16.064  44.883  208.091 1.00 33.70  ? 219 ALA D CB    1 
ATOM   13268 N N     . ILE D  1 220 ? 16.616  44.583  211.198 1.00 34.27  ? 220 ILE D N     1 
ATOM   13269 C CA    . ILE D  1 220 ? 16.501  45.208  212.515 1.00 30.15  ? 220 ILE D CA    1 
ATOM   13270 C C     . ILE D  1 220 ? 17.791  45.107  213.328 1.00 31.33  ? 220 ILE D C     1 
ATOM   13271 O O     . ILE D  1 220 ? 17.941  45.786  214.342 1.00 29.85  ? 220 ILE D O     1 
ATOM   13272 C CB    . ILE D  1 220 ? 15.354  44.593  213.341 1.00 25.19  ? 220 ILE D CB    1 
ATOM   13273 C CG1   . ILE D  1 220 ? 15.618  43.110  213.622 1.00 28.34  ? 220 ILE D CG1   1 
ATOM   13274 C CG2   . ILE D  1 220 ? 14.017  44.789  212.634 1.00 27.40  ? 220 ILE D CG2   1 
ATOM   13275 C CD1   . ILE D  1 220 ? 14.579  42.465  214.523 1.00 30.80  ? 220 ILE D CD1   1 
ATOM   13276 N N     . ARG D  1 221 ? 18.715  44.260  212.885 1.00 31.06  ? 221 ARG D N     1 
ATOM   13277 C CA    . ARG D  1 221 ? 19.984  44.086  213.584 1.00 32.87  ? 221 ARG D CA    1 
ATOM   13278 C C     . ARG D  1 221 ? 21.070  45.011  213.044 1.00 32.25  ? 221 ARG D C     1 
ATOM   13279 O O     . ARG D  1 221 ? 22.179  44.564  212.750 1.00 33.38  ? 221 ARG D O     1 
ATOM   13280 C CB    . ARG D  1 221 ? 20.460  42.635  213.489 1.00 32.45  ? 221 ARG D CB    1 
ATOM   13281 C CG    . ARG D  1 221 ? 19.744  41.668  214.420 1.00 37.40  ? 221 ARG D CG    1 
ATOM   13282 C CD    . ARG D  1 221 ? 20.285  40.255  214.248 1.00 31.46  ? 221 ARG D CD    1 
ATOM   13283 N NE    . ARG D  1 221 ? 20.011  39.726  212.913 1.00 31.04  ? 221 ARG D NE    1 
ATOM   13284 C CZ    . ARG D  1 221 ? 20.724  38.772  212.324 1.00 36.76  ? 221 ARG D CZ    1 
ATOM   13285 N NH1   . ARG D  1 221 ? 21.768  38.238  212.946 1.00 37.26  ? 221 ARG D NH1   1 
ATOM   13286 N NH2   . ARG D  1 221 ? 20.396  38.355  211.108 1.00 37.80  ? 221 ARG D NH2   1 
ATOM   13287 N N     . GLY D  1 222 ? 20.751  46.295  212.912 1.00 35.46  ? 222 GLY D N     1 
ATOM   13288 C CA    . GLY D  1 222 ? 21.722  47.269  212.449 1.00 31.18  ? 222 GLY D CA    1 
ATOM   13289 C C     . GLY D  1 222 ? 21.187  48.255  211.427 1.00 34.96  ? 222 GLY D C     1 
ATOM   13290 O O     . GLY D  1 222 ? 21.830  49.261  211.134 1.00 28.10  ? 222 GLY D O     1 
ATOM   13291 N N     . GLY D  1 223 ? 20.002  47.977  210.893 1.00 32.05  ? 223 GLY D N     1 
ATOM   13292 C CA    . GLY D  1 223 ? 19.419  48.808  209.856 1.00 32.23  ? 223 GLY D CA    1 
ATOM   13293 C C     . GLY D  1 223 ? 18.867  50.136  210.339 1.00 32.64  ? 223 GLY D C     1 
ATOM   13294 O O     . GLY D  1 223 ? 18.407  50.947  209.536 1.00 32.10  ? 223 GLY D O     1 
ATOM   13295 N N     . GLY D  1 224 ? 18.899  50.361  211.648 1.00 33.60  ? 224 GLY D N     1 
ATOM   13296 C CA    . GLY D  1 224 ? 18.463  51.628  212.208 1.00 27.60  ? 224 GLY D CA    1 
ATOM   13297 C C     . GLY D  1 224 ? 17.079  51.581  212.826 1.00 29.61  ? 224 GLY D C     1 
ATOM   13298 O O     . GLY D  1 224 ? 16.172  50.939  212.296 1.00 33.97  ? 224 GLY D O     1 
ATOM   13299 N N     . GLY D  1 225 ? 16.915  52.270  213.951 1.00 30.35  ? 225 GLY D N     1 
ATOM   13300 C CA    . GLY D  1 225 ? 15.638  52.309  214.636 1.00 30.78  ? 225 GLY D CA    1 
ATOM   13301 C C     . GLY D  1 225 ? 14.618  53.200  213.953 1.00 30.88  ? 225 GLY D C     1 
ATOM   13302 O O     . GLY D  1 225 ? 14.974  54.046  213.130 1.00 36.03  ? 225 GLY D O     1 
ATOM   13303 N N     . GLY D  1 226 ? 13.346  52.998  214.292 1.00 35.63  ? 226 GLY D N     1 
ATOM   13304 C CA    . GLY D  1 226 ? 12.261  53.832  213.799 1.00 31.71  ? 226 GLY D CA    1 
ATOM   13305 C C     . GLY D  1 226 ? 11.897  53.609  212.343 1.00 37.43  ? 226 GLY D C     1 
ATOM   13306 O O     . GLY D  1 226 ? 11.353  54.497  211.689 1.00 34.11  ? 226 GLY D O     1 
ATOM   13307 N N     . VAL D  1 227 ? 12.181  52.415  211.834 1.00 29.94  ? 227 VAL D N     1 
ATOM   13308 C CA    . VAL D  1 227 ? 12.047  52.157  210.403 1.00 31.24  ? 227 VAL D CA    1 
ATOM   13309 C C     . VAL D  1 227 ? 11.189  50.928  210.092 1.00 35.02  ? 227 VAL D C     1 
ATOM   13310 O O     . VAL D  1 227 ? 10.454  50.906  209.104 1.00 36.64  ? 227 VAL D O     1 
ATOM   13311 C CB    . VAL D  1 227 ? 13.444  51.982  209.750 1.00 34.80  ? 227 VAL D CB    1 
ATOM   13312 C CG1   . VAL D  1 227 ? 13.327  51.637  208.275 1.00 31.83  ? 227 VAL D CG1   1 
ATOM   13313 C CG2   . VAL D  1 227 ? 14.281  53.242  209.936 1.00 32.76  ? 227 VAL D CG2   1 
ATOM   13314 N N     . TRP D  1 228 ? 11.270  49.916  210.949 1.00 30.43  ? 228 TRP D N     1 
ATOM   13315 C CA    . TRP D  1 228 ? 10.730  48.597  210.629 1.00 32.23  ? 228 TRP D CA    1 
ATOM   13316 C C     . TRP D  1 228 ? 9.482   48.283  211.431 1.00 34.95  ? 228 TRP D C     1 
ATOM   13317 O O     . TRP D  1 228 ? 8.749   47.348  211.120 1.00 34.84  ? 228 TRP D O     1 
ATOM   13318 C CB    . TRP D  1 228 ? 11.797  47.527  210.879 1.00 28.78  ? 228 TRP D CB    1 
ATOM   13319 C CG    . TRP D  1 228 ? 13.146  48.002  210.481 1.00 32.52  ? 228 TRP D CG    1 
ATOM   13320 C CD1   . TRP D  1 228 ? 14.120  48.485  211.302 1.00 30.18  ? 228 TRP D CD1   1 
ATOM   13321 C CD2   . TRP D  1 228 ? 13.664  48.083  209.149 1.00 36.09  ? 228 TRP D CD2   1 
ATOM   13322 N NE1   . TRP D  1 228 ? 15.220  48.853  210.565 1.00 34.89  ? 228 TRP D NE1   1 
ATOM   13323 C CE2   . TRP D  1 228 ? 14.965  48.616  209.240 1.00 31.62  ? 228 TRP D CE2   1 
ATOM   13324 C CE3   . TRP D  1 228 ? 13.157  47.749  207.890 1.00 33.25  ? 228 TRP D CE3   1 
ATOM   13325 C CZ2   . TRP D  1 228 ? 15.768  48.820  208.120 1.00 30.76  ? 228 TRP D CZ2   1 
ATOM   13326 C CZ3   . TRP D  1 228 ? 13.954  47.953  206.780 1.00 36.29  ? 228 TRP D CZ3   1 
ATOM   13327 C CH2   . TRP D  1 228 ? 15.245  48.485  206.901 1.00 37.84  ? 228 TRP D CH2   1 
ATOM   13328 N N     . GLY D  1 229 ? 9.242   49.082  212.460 1.00 29.66  ? 229 GLY D N     1 
ATOM   13329 C CA    . GLY D  1 229 ? 8.195   48.797  213.417 1.00 27.13  ? 229 GLY D CA    1 
ATOM   13330 C C     . GLY D  1 229 ? 8.761   49.042  214.794 1.00 32.84  ? 229 GLY D C     1 
ATOM   13331 O O     . GLY D  1 229 ? 9.835   49.622  214.928 1.00 31.02  ? 229 GLY D O     1 
ATOM   13332 N N     . ALA D  1 230 ? 8.049   48.599  215.821 1.00 28.32  ? 230 ALA D N     1 
ATOM   13333 C CA    . ALA D  1 230 ? 8.505   48.798  217.187 1.00 26.97  ? 230 ALA D CA    1 
ATOM   13334 C C     . ALA D  1 230 ? 9.063   47.508  217.770 1.00 31.02  ? 230 ALA D C     1 
ATOM   13335 O O     . ALA D  1 230 ? 8.327   46.542  217.985 1.00 26.42  ? 230 ALA D O     1 
ATOM   13336 C CB    . ALA D  1 230 ? 7.370   49.329  218.052 1.00 28.20  ? 230 ALA D CB    1 
ATOM   13337 N N     . ILE D  1 231 ? 10.370  47.485  218.010 1.00 28.28  ? 231 ILE D N     1 
ATOM   13338 C CA    . ILE D  1 231 ? 10.975  46.370  218.715 1.00 28.02  ? 231 ILE D CA    1 
ATOM   13339 C C     . ILE D  1 231 ? 10.417  46.331  220.128 1.00 32.74  ? 231 ILE D C     1 
ATOM   13340 O O     . ILE D  1 231 ? 10.520  47.316  220.857 1.00 30.42  ? 231 ILE D O     1 
ATOM   13341 C CB    . ILE D  1 231 ? 12.514  46.482  218.787 1.00 30.27  ? 231 ILE D CB    1 
ATOM   13342 C CG1   . ILE D  1 231 ? 13.122  46.537  217.386 1.00 30.72  ? 231 ILE D CG1   1 
ATOM   13343 C CG2   . ILE D  1 231 ? 13.087  45.314  219.577 1.00 28.38  ? 231 ILE D CG2   1 
ATOM   13344 C CD1   . ILE D  1 231 ? 13.112  45.210  216.670 1.00 33.68  ? 231 ILE D CD1   1 
ATOM   13345 N N     . TYR D  1 232 ? 9.811   45.213  220.514 1.00 31.79  ? 232 TYR D N     1 
ATOM   13346 C CA    . TYR D  1 232 ? 9.352   45.062  221.886 1.00 29.76  ? 232 TYR D CA    1 
ATOM   13347 C C     . TYR D  1 232 ? 10.490  44.543  222.755 1.00 28.81  ? 232 TYR D C     1 
ATOM   13348 O O     . TYR D  1 232 ? 10.715  45.043  223.855 1.00 36.86  ? 232 TYR D O     1 
ATOM   13349 C CB    . TYR D  1 232 ? 8.144   44.121  221.983 1.00 26.71  ? 232 TYR D CB    1 
ATOM   13350 C CG    . TYR D  1 232 ? 7.990   43.537  223.371 1.00 30.99  ? 232 TYR D CG    1 
ATOM   13351 C CD1   . TYR D  1 232 ? 7.657   44.346  224.453 1.00 36.02  ? 232 TYR D CD1   1 
ATOM   13352 C CD2   . TYR D  1 232 ? 8.208   42.186  223.606 1.00 33.27  ? 232 TYR D CD2   1 
ATOM   13353 C CE1   . TYR D  1 232 ? 7.536   43.820  225.729 1.00 37.41  ? 232 TYR D CE1   1 
ATOM   13354 C CE2   . TYR D  1 232 ? 8.091   41.653  224.877 1.00 32.89  ? 232 TYR D CE2   1 
ATOM   13355 C CZ    . TYR D  1 232 ? 7.755   42.472  225.933 1.00 37.34  ? 232 TYR D CZ    1 
ATOM   13356 O OH    . TYR D  1 232 ? 7.638   41.938  227.197 1.00 37.96  ? 232 TYR D OH    1 
ATOM   13357 N N     . ALA D  1 233 ? 11.211  43.545  222.255 1.00 28.50  ? 233 ALA D N     1 
ATOM   13358 C CA    . ALA D  1 233 ? 12.283  42.929  223.025 1.00 34.25  ? 233 ALA D CA    1 
ATOM   13359 C C     . ALA D  1 233 ? 13.351  42.290  222.140 1.00 32.99  ? 233 ALA D C     1 
ATOM   13360 O O     . ALA D  1 233 ? 13.062  41.805  221.045 1.00 33.23  ? 233 ALA D O     1 
ATOM   13361 C CB    . ALA D  1 233 ? 11.712  41.890  223.978 1.00 36.47  ? 233 ALA D CB    1 
ATOM   13362 N N     . TRP D  1 234 ? 14.585  42.294  222.634 1.00 29.43  ? 234 TRP D N     1 
ATOM   13363 C CA    . TRP D  1 234 ? 15.688  41.600  221.982 1.00 29.68  ? 234 TRP D CA    1 
ATOM   13364 C C     . TRP D  1 234 ? 15.997  40.300  222.712 1.00 30.82  ? 234 TRP D C     1 
ATOM   13365 O O     . TRP D  1 234 ? 15.995  40.260  223.941 1.00 33.62  ? 234 TRP D O     1 
ATOM   13366 C CB    . TRP D  1 234 ? 16.953  42.465  221.952 1.00 30.34  ? 234 TRP D CB    1 
ATOM   13367 C CG    . TRP D  1 234 ? 16.810  43.799  221.285 1.00 28.89  ? 234 TRP D CG    1 
ATOM   13368 C CD1   . TRP D  1 234 ? 16.651  45.008  221.898 1.00 30.50  ? 234 TRP D CD1   1 
ATOM   13369 C CD2   . TRP D  1 234 ? 16.843  44.063  219.878 1.00 31.98  ? 234 TRP D CD2   1 
ATOM   13370 N NE1   . TRP D  1 234 ? 16.572  46.009  220.958 1.00 29.38  ? 234 TRP D NE1   1 
ATOM   13371 C CE2   . TRP D  1 234 ? 16.688  45.454  219.710 1.00 29.84  ? 234 TRP D CE2   1 
ATOM   13372 C CE3   . TRP D  1 234 ? 16.982  43.258  218.743 1.00 31.26  ? 234 TRP D CE3   1 
ATOM   13373 C CZ2   . TRP D  1 234 ? 16.667  46.057  218.455 1.00 30.87  ? 234 TRP D CZ2   1 
ATOM   13374 C CZ3   . TRP D  1 234 ? 16.963  43.860  217.496 1.00 29.65  ? 234 TRP D CZ3   1 
ATOM   13375 C CH2   . TRP D  1 234 ? 16.806  45.245  217.363 1.00 32.01  ? 234 TRP D CH2   1 
ATOM   13376 N N     . LYS D  1 235 ? 16.264  39.239  221.960 1.00 29.61  ? 235 LYS D N     1 
ATOM   13377 C CA    . LYS D  1 235 ? 16.830  38.038  222.557 1.00 36.44  ? 235 LYS D CA    1 
ATOM   13378 C C     . LYS D  1 235 ? 18.307  37.969  222.198 1.00 33.31  ? 235 LYS D C     1 
ATOM   13379 O O     . LYS D  1 235 ? 18.667  37.733  221.045 1.00 35.05  ? 235 LYS D O     1 
ATOM   13380 C CB    . LYS D  1 235 ? 16.107  36.774  222.094 1.00 37.21  ? 235 LYS D CB    1 
ATOM   13381 C CG    . LYS D  1 235 ? 16.525  35.531  222.871 1.00 37.87  ? 235 LYS D CG    1 
ATOM   13382 C CD    . LYS D  1 235 ? 15.890  34.264  222.322 1.00 41.42  ? 235 LYS D CD    1 
ATOM   13383 C CE    . LYS D  1 235 ? 16.297  33.050  223.145 1.00 38.58  ? 235 LYS D CE    1 
ATOM   13384 N NZ    . LYS D  1 235 ? 15.848  31.774  222.528 1.00 44.12  ? 235 LYS D NZ    1 
ATOM   13385 N N     . ILE D  1 236 ? 19.156  38.188  223.195 1.00 33.33  ? 236 ILE D N     1 
ATOM   13386 C CA    . ILE D  1 236 ? 20.592  38.268  222.973 1.00 41.36  ? 236 ILE D CA    1 
ATOM   13387 C C     . ILE D  1 236 ? 21.320  37.031  223.480 1.00 45.27  ? 236 ILE D C     1 
ATOM   13388 O O     . ILE D  1 236 ? 20.874  36.371  224.420 1.00 47.08  ? 236 ILE D O     1 
ATOM   13389 C CB    . ILE D  1 236 ? 21.197  39.511  223.655 1.00 39.90  ? 236 ILE D CB    1 
ATOM   13390 C CG1   . ILE D  1 236 ? 20.917  39.492  225.158 1.00 40.85  ? 236 ILE D CG1   1 
ATOM   13391 C CG2   . ILE D  1 236 ? 20.644  40.782  223.029 1.00 34.30  ? 236 ILE D CG2   1 
ATOM   13392 C CD1   . ILE D  1 236 ? 21.603  40.608  225.923 1.00 37.23  ? 236 ILE D CD1   1 
ATOM   13393 N N     . LYS D  1 237 ? 22.440  36.719  222.840 1.00 43.83  ? 237 LYS D N     1 
ATOM   13394 C CA    . LYS D  1 237 ? 23.331  35.674  223.321 1.00 45.80  ? 237 LYS D CA    1 
ATOM   13395 C C     . LYS D  1 237 ? 24.298  36.265  224.337 1.00 46.85  ? 237 LYS D C     1 
ATOM   13396 O O     . LYS D  1 237 ? 25.057  37.179  224.015 1.00 48.40  ? 237 LYS D O     1 
ATOM   13397 C CB    . LYS D  1 237 ? 24.104  35.040  222.166 1.00 47.69  ? 237 LYS D CB    1 
ATOM   13398 C CG    . LYS D  1 237 ? 25.045  33.933  222.597 1.00 59.67  ? 237 LYS D CG    1 
ATOM   13399 C CD    . LYS D  1 237 ? 24.277  32.773  223.206 1.00 63.11  ? 237 LYS D CD    1 
ATOM   13400 C CE    . LYS D  1 237 ? 25.223  31.712  223.739 1.00 61.13  ? 237 LYS D CE    1 
ATOM   13401 N NZ    . LYS D  1 237 ? 24.494  30.570  224.355 1.00 68.51  ? 237 LYS D NZ    1 
ATOM   13402 N N     . LEU D  1 238 ? 24.261  35.762  225.566 1.00 47.23  ? 238 LEU D N     1 
ATOM   13403 C CA    . LEU D  1 238 ? 25.195  36.216  226.590 1.00 54.15  ? 238 LEU D CA    1 
ATOM   13404 C C     . LEU D  1 238 ? 26.580  35.635  226.311 1.00 53.91  ? 238 LEU D C     1 
ATOM   13405 O O     . LEU D  1 238 ? 26.705  34.496  225.863 1.00 49.01  ? 238 LEU D O     1 
ATOM   13406 C CB    . LEU D  1 238 ? 24.704  35.830  227.985 1.00 55.39  ? 238 LEU D CB    1 
ATOM   13407 C CG    . LEU D  1 238 ? 23.403  36.518  228.409 1.00 55.72  ? 238 LEU D CG    1 
ATOM   13408 C CD1   . LEU D  1 238 ? 23.013  36.132  229.828 1.00 52.98  ? 238 LEU D CD1   1 
ATOM   13409 C CD2   . LEU D  1 238 ? 23.529  38.029  228.278 1.00 51.30  ? 238 LEU D CD2   1 
ATOM   13410 N N     . LEU D  1 239 ? 27.616  36.425  226.571 1.00 55.10  ? 239 LEU D N     1 
ATOM   13411 C CA    . LEU D  1 239 ? 28.962  36.090  226.120 1.00 58.87  ? 239 LEU D CA    1 
ATOM   13412 C C     . LEU D  1 239 ? 29.899  35.745  227.270 1.00 55.76  ? 239 LEU D C     1 
ATOM   13413 O O     . LEU D  1 239 ? 29.894  36.420  228.301 1.00 55.23  ? 239 LEU D O     1 
ATOM   13414 C CB    . LEU D  1 239 ? 29.537  37.255  225.313 1.00 54.83  ? 239 LEU D CB    1 
ATOM   13415 C CG    . LEU D  1 239 ? 28.563  37.834  224.283 1.00 53.21  ? 239 LEU D CG    1 
ATOM   13416 C CD1   . LEU D  1 239 ? 29.034  39.192  223.801 1.00 48.22  ? 239 LEU D CD1   1 
ATOM   13417 C CD2   . LEU D  1 239 ? 28.372  36.878  223.112 1.00 52.22  ? 239 LEU D CD2   1 
ATOM   13418 N N     . PRO D  1 240 ? 30.719  34.695  227.088 1.00 60.46  ? 240 PRO D N     1 
ATOM   13419 C CA    . PRO D  1 240 ? 31.691  34.274  228.102 1.00 59.94  ? 240 PRO D CA    1 
ATOM   13420 C C     . PRO D  1 240 ? 32.690  35.379  228.420 1.00 57.47  ? 240 PRO D C     1 
ATOM   13421 O O     . PRO D  1 240 ? 33.267  35.963  227.503 1.00 56.18  ? 240 PRO D O     1 
ATOM   13422 C CB    . PRO D  1 240 ? 32.396  33.075  227.449 1.00 66.81  ? 240 PRO D CB    1 
ATOM   13423 C CG    . PRO D  1 240 ? 31.493  32.633  226.348 1.00 59.13  ? 240 PRO D CG    1 
ATOM   13424 C CD    . PRO D  1 240 ? 30.795  33.866  225.873 1.00 60.06  ? 240 PRO D CD    1 
ATOM   13425 N N     . VAL D  1 241 ? 32.859  35.678  229.705 1.00 60.81  ? 241 VAL D N     1 
ATOM   13426 C CA    . VAL D  1 241 ? 33.884  36.610  230.161 1.00 70.19  ? 241 VAL D CA    1 
ATOM   13427 C C     . VAL D  1 241 ? 34.589  36.037  231.384 1.00 78.32  ? 241 VAL D C     1 
ATOM   13428 O O     . VAL D  1 241 ? 33.983  35.306  232.171 1.00 72.15  ? 241 VAL D O     1 
ATOM   13429 C CB    . VAL D  1 241 ? 33.304  38.006  230.514 1.00 68.50  ? 241 VAL D CB    1 
ATOM   13430 C CG1   . VAL D  1 241 ? 32.546  38.590  229.336 1.00 68.68  ? 241 VAL D CG1   1 
ATOM   13431 C CG2   . VAL D  1 241 ? 32.414  37.939  231.751 1.00 72.62  ? 241 VAL D CG2   1 
ATOM   13432 N N     . PRO D  1 242 ? 35.886  36.349  231.538 1.00 78.47  ? 242 PRO D N     1 
ATOM   13433 C CA    . PRO D  1 242 ? 36.638  35.986  232.741 1.00 76.63  ? 242 PRO D CA    1 
ATOM   13434 C C     . PRO D  1 242 ? 36.006  36.553  234.012 1.00 76.27  ? 242 PRO D C     1 
ATOM   13435 O O     . PRO D  1 242 ? 35.262  37.531  233.944 1.00 79.28  ? 242 PRO D O     1 
ATOM   13436 C CB    . PRO D  1 242 ? 38.011  36.610  232.483 1.00 76.10  ? 242 PRO D CB    1 
ATOM   13437 C CG    . PRO D  1 242 ? 38.135  36.582  230.997 1.00 71.50  ? 242 PRO D CG    1 
ATOM   13438 C CD    . PRO D  1 242 ? 36.761  36.958  230.521 1.00 72.93  ? 242 PRO D CD    1 
ATOM   13439 N N     . GLU D  1 243 ? 36.303  35.934  235.151 1.00 75.72  ? 243 GLU D N     1 
ATOM   13440 C CA    . GLU D  1 243 ? 35.850  36.418  236.453 1.00 77.86  ? 243 GLU D CA    1 
ATOM   13441 C C     . GLU D  1 243 ? 36.551  37.725  236.796 1.00 76.46  ? 243 GLU D C     1 
ATOM   13442 O O     . GLU D  1 243 ? 36.034  38.546  237.559 1.00 74.59  ? 243 GLU D O     1 
ATOM   13443 C CB    . GLU D  1 243 ? 36.116  35.374  237.541 1.00 80.70  ? 243 GLU D CB    1 
ATOM   13444 C CG    . GLU D  1 243 ? 35.685  33.963  237.178 1.00 85.03  ? 243 GLU D CG    1 
ATOM   13445 C CD    . GLU D  1 243 ? 34.333  33.587  237.758 1.00 87.36  ? 243 GLU D CD    1 
ATOM   13446 O OE1   . GLU D  1 243 ? 33.748  32.586  237.297 1.00 90.17  ? 243 GLU D OE1   1 
ATOM   13447 O OE2   . GLU D  1 243 ? 33.864  34.283  238.682 1.00 94.22  ? 243 GLU D OE2   1 
ATOM   13448 N N     . LYS D  1 244 ? 37.742  37.898  236.233 1.00 79.37  ? 244 LYS D N     1 
ATOM   13449 C CA    . LYS D  1 244 ? 38.490  39.130  236.394 1.00 77.70  ? 244 LYS D CA    1 
ATOM   13450 C C     . LYS D  1 244 ? 39.033  39.612  235.061 1.00 73.79  ? 244 LYS D C     1 
ATOM   13451 O O     . LYS D  1 244 ? 39.614  38.844  234.292 1.00 74.12  ? 244 LYS D O     1 
ATOM   13452 C CB    . LYS D  1 244 ? 39.626  38.941  237.394 1.00 84.41  ? 244 LYS D CB    1 
ATOM   13453 C CG    . LYS D  1 244 ? 39.269  39.378  238.798 1.00 84.95  ? 244 LYS D CG    1 
ATOM   13454 C CD    . LYS D  1 244 ? 40.204  38.757  239.812 1.00 92.34  ? 244 LYS D CD    1 
ATOM   13455 C CE    . LYS D  1 244 ? 40.742  39.796  240.773 1.00 96.09  ? 244 LYS D CE    1 
ATOM   13456 N NZ    . LYS D  1 244 ? 42.169  39.525  241.091 1.00 92.58  ? 244 LYS D NZ    1 
ATOM   13457 N N     . VAL D  1 245 ? 38.822  40.892  234.791 1.00 73.12  ? 245 VAL D N     1 
ATOM   13458 C CA    . VAL D  1 245 ? 39.329  41.518  233.584 1.00 67.55  ? 245 VAL D CA    1 
ATOM   13459 C C     . VAL D  1 245 ? 40.169  42.710  234.003 1.00 61.18  ? 245 VAL D C     1 
ATOM   13460 O O     . VAL D  1 245 ? 40.165  43.090  235.173 1.00 66.73  ? 245 VAL D O     1 
ATOM   13461 C CB    . VAL D  1 245 ? 38.189  41.959  232.648 1.00 64.76  ? 245 VAL D CB    1 
ATOM   13462 C CG1   . VAL D  1 245 ? 37.379  40.750  232.205 1.00 62.26  ? 245 VAL D CG1   1 
ATOM   13463 C CG2   . VAL D  1 245 ? 37.297  42.973  233.342 1.00 60.99  ? 245 VAL D CG2   1 
ATOM   13464 N N     . THR D  1 246 ? 40.896  43.302  233.065 1.00 55.60  ? 246 THR D N     1 
ATOM   13465 C CA    . THR D  1 246 ? 41.762  44.416  233.421 1.00 57.01  ? 246 THR D CA    1 
ATOM   13466 C C     . THR D  1 246 ? 41.467  45.650  232.585 1.00 49.91  ? 246 THR D C     1 
ATOM   13467 O O     . THR D  1 246 ? 41.324  45.571  231.366 1.00 55.73  ? 246 THR D O     1 
ATOM   13468 C CB    . THR D  1 246 ? 43.244  44.042  233.271 1.00 61.50  ? 246 THR D CB    1 
ATOM   13469 O OG1   . THR D  1 246 ? 43.464  42.746  233.837 1.00 62.56  ? 246 THR D OG1   1 
ATOM   13470 C CG2   . THR D  1 246 ? 44.126  45.061  233.984 1.00 56.42  ? 246 THR D CG2   1 
ATOM   13471 N N     . VAL D  1 247 ? 41.365  46.789  233.262 1.00 46.84  ? 247 VAL D N     1 
ATOM   13472 C CA    . VAL D  1 247 ? 41.148  48.068  232.606 1.00 53.68  ? 247 VAL D CA    1 
ATOM   13473 C C     . VAL D  1 247 ? 42.095  49.116  233.168 1.00 61.30  ? 247 VAL D C     1 
ATOM   13474 O O     . VAL D  1 247 ? 42.681  48.930  234.235 1.00 67.88  ? 247 VAL D O     1 
ATOM   13475 C CB    . VAL D  1 247 ? 39.700  48.567  232.780 1.00 59.37  ? 247 VAL D CB    1 
ATOM   13476 C CG1   . VAL D  1 247 ? 38.718  47.608  232.136 1.00 54.55  ? 247 VAL D CG1   1 
ATOM   13477 C CG2   . VAL D  1 247 ? 39.382  48.741  234.249 1.00 62.39  ? 247 VAL D CG2   1 
ATOM   13478 N N     . PHE D  1 248 ? 42.247  50.214  232.436 1.00 56.07  ? 248 PHE D N     1 
ATOM   13479 C CA    . PHE D  1 248 ? 42.997  51.367  232.919 1.00 61.73  ? 248 PHE D CA    1 
ATOM   13480 C C     . PHE D  1 248 ? 42.550  52.632  232.196 1.00 66.84  ? 248 PHE D C     1 
ATOM   13481 O O     . PHE D  1 248 ? 42.302  52.615  230.991 1.00 65.37  ? 248 PHE D O     1 
ATOM   13482 C CB    . PHE D  1 248 ? 44.509  51.157  232.753 1.00 65.24  ? 248 PHE D CB    1 
ATOM   13483 C CG    . PHE D  1 248 ? 44.950  50.884  231.335 1.00 53.90  ? 248 PHE D CG    1 
ATOM   13484 C CD1   . PHE D  1 248 ? 45.242  51.928  230.468 1.00 57.66  ? 248 PHE D CD1   1 
ATOM   13485 C CD2   . PHE D  1 248 ? 45.107  49.583  230.881 1.00 58.51  ? 248 PHE D CD2   1 
ATOM   13486 C CE1   . PHE D  1 248 ? 45.659  51.680  229.170 1.00 57.25  ? 248 PHE D CE1   1 
ATOM   13487 C CE2   . PHE D  1 248 ? 45.525  49.329  229.583 1.00 53.61  ? 248 PHE D CE2   1 
ATOM   13488 C CZ    . PHE D  1 248 ? 45.801  50.380  228.728 1.00 52.88  ? 248 PHE D CZ    1 
ATOM   13489 N N     . ARG D  1 249 ? 42.432  53.722  232.947 1.00 73.65  ? 249 ARG D N     1 
ATOM   13490 C CA    . ARG D  1 249 ? 42.120  55.023  232.371 1.00 76.74  ? 249 ARG D CA    1 
ATOM   13491 C C     . ARG D  1 249 ? 43.253  55.996  232.667 1.00 81.65  ? 249 ARG D C     1 
ATOM   13492 O O     . ARG D  1 249 ? 43.353  56.528  233.773 1.00 91.09  ? 249 ARG D O     1 
ATOM   13493 C CB    . ARG D  1 249 ? 40.797  55.567  232.913 1.00 83.88  ? 249 ARG D CB    1 
ATOM   13494 C CG    . ARG D  1 249 ? 40.486  56.973  232.424 1.00 81.30  ? 249 ARG D CG    1 
ATOM   13495 C CD    . ARG D  1 249 ? 39.003  57.301  232.507 1.00 88.52  ? 249 ARG D CD    1 
ATOM   13496 N NE    . ARG D  1 249 ? 38.561  57.580  233.870 1.00 101.34 ? 249 ARG D NE    1 
ATOM   13497 C CZ    . ARG D  1 249 ? 37.684  56.843  234.546 1.00 99.95  ? 249 ARG D CZ    1 
ATOM   13498 N NH1   . ARG D  1 249 ? 37.348  57.187  235.782 1.00 96.45  ? 249 ARG D NH1   1 
ATOM   13499 N NH2   . ARG D  1 249 ? 37.138  55.768  233.992 1.00 98.95  ? 249 ARG D NH2   1 
ATOM   13500 N N     . VAL D  1 250 ? 44.110  56.223  231.676 1.00 75.73  ? 250 VAL D N     1 
ATOM   13501 C CA    . VAL D  1 250 ? 45.270  57.089  231.854 1.00 76.28  ? 250 VAL D CA    1 
ATOM   13502 C C     . VAL D  1 250 ? 45.214  58.292  230.918 1.00 74.79  ? 250 VAL D C     1 
ATOM   13503 O O     . VAL D  1 250 ? 45.049  58.144  229.708 1.00 73.04  ? 250 VAL D O     1 
ATOM   13504 C CB    . VAL D  1 250 ? 46.584  56.311  231.625 1.00 75.46  ? 250 VAL D CB    1 
ATOM   13505 C CG1   . VAL D  1 250 ? 47.740  57.263  231.334 1.00 73.01  ? 250 VAL D CG1   1 
ATOM   13506 C CG2   . VAL D  1 250 ? 46.890  55.427  232.828 1.00 78.53  ? 250 VAL D CG2   1 
ATOM   13507 N N     . THR D  1 251 ? 45.348  59.485  231.490 1.00 77.66  ? 251 THR D N     1 
ATOM   13508 C CA    . THR D  1 251 ? 45.278  60.717  230.714 1.00 72.24  ? 251 THR D CA    1 
ATOM   13509 C C     . THR D  1 251 ? 46.668  61.309  230.498 1.00 77.49  ? 251 THR D C     1 
ATOM   13510 O O     . THR D  1 251 ? 47.501  61.310  231.404 1.00 80.07  ? 251 THR D O     1 
ATOM   13511 C CB    . THR D  1 251 ? 44.379  61.763  231.404 1.00 72.57  ? 251 THR D CB    1 
ATOM   13512 O OG1   . THR D  1 251 ? 43.111  61.176  231.718 1.00 68.80  ? 251 THR D OG1   1 
ATOM   13513 C CG2   . THR D  1 251 ? 44.163  62.970  230.504 1.00 68.50  ? 251 THR D CG2   1 
ATOM   13514 N N     . LYS D  1 252 ? 46.917  61.810  229.292 1.00 75.95  ? 252 LYS D N     1 
ATOM   13515 C CA    . LYS D  1 252 ? 48.200  62.422  228.977 1.00 73.51  ? 252 LYS D CA    1 
ATOM   13516 C C     . LYS D  1 252 ? 48.046  63.870  228.525 1.00 74.88  ? 252 LYS D C     1 
ATOM   13517 O O     . LYS D  1 252 ? 47.513  64.148  227.452 1.00 70.14  ? 252 LYS D O     1 
ATOM   13518 C CB    . LYS D  1 252 ? 48.932  61.614  227.905 1.00 72.49  ? 252 LYS D CB    1 
ATOM   13519 C CG    . LYS D  1 252 ? 49.408  60.254  228.389 1.00 68.55  ? 252 LYS D CG    1 
ATOM   13520 C CD    . LYS D  1 252 ? 50.848  60.001  227.980 1.00 71.07  ? 252 LYS D CD    1 
ATOM   13521 C CE    . LYS D  1 252 ? 51.595  59.194  229.030 1.00 71.79  ? 252 LYS D CE    1 
ATOM   13522 N NZ    . LYS D  1 252 ? 52.893  58.687  228.502 1.00 70.86  ? 252 LYS D NZ    1 
ATOM   13523 N N     . ASN D  1 253 ? 48.521  64.787  229.360 1.00 79.98  ? 253 ASN D N     1 
ATOM   13524 C CA    . ASN D  1 253 ? 48.562  66.200  229.012 1.00 78.67  ? 253 ASN D CA    1 
ATOM   13525 C C     . ASN D  1 253 ? 49.900  66.549  228.364 1.00 79.18  ? 253 ASN D C     1 
ATOM   13526 O O     . ASN D  1 253 ? 50.909  66.711  229.053 1.00 78.44  ? 253 ASN D O     1 
ATOM   13527 C CB    . ASN D  1 253 ? 48.324  67.061  230.252 1.00 81.08  ? 253 ASN D CB    1 
ATOM   13528 C CG    . ASN D  1 253 ? 47.074  66.654  231.009 1.00 81.67  ? 253 ASN D CG    1 
ATOM   13529 O OD1   . ASN D  1 253 ? 47.112  65.774  231.869 1.00 81.16  ? 253 ASN D OD1   1 
ATOM   13530 N ND2   . ASN D  1 253 ? 45.955  67.296  230.692 1.00 74.18  ? 253 ASN D ND2   1 
ATOM   13531 N N     . VAL D  1 254 ? 49.906  66.644  227.034 1.00 76.92  ? 254 VAL D N     1 
ATOM   13532 C CA    . VAL D  1 254 ? 51.139  66.837  226.263 1.00 77.09  ? 254 VAL D CA    1 
ATOM   13533 C C     . VAL D  1 254 ? 50.973  67.831  225.117 1.00 72.50  ? 254 VAL D C     1 
ATOM   13534 O O     . VAL D  1 254 ? 49.855  68.156  224.726 1.00 75.92  ? 254 VAL D O     1 
ATOM   13535 C CB    . VAL D  1 254 ? 51.641  65.514  225.650 1.00 73.18  ? 254 VAL D CB    1 
ATOM   13536 C CG1   . VAL D  1 254 ? 51.804  64.444  226.718 1.00 73.19  ? 254 VAL D CG1   1 
ATOM   13537 C CG2   . VAL D  1 254 ? 50.698  65.052  224.552 1.00 67.30  ? 254 VAL D CG2   1 
ATOM   13538 N N     . ALA D  1 255 ? 52.097  68.285  224.566 1.00 71.91  ? 255 ALA D N     1 
ATOM   13539 C CA    . ALA D  1 255 ? 52.098  69.185  223.413 1.00 71.78  ? 255 ALA D CA    1 
ATOM   13540 C C     . ALA D  1 255 ? 51.573  68.505  222.145 1.00 63.94  ? 255 ALA D C     1 
ATOM   13541 O O     . ALA D  1 255 ? 51.573  67.278  222.048 1.00 60.03  ? 255 ALA D O     1 
ATOM   13542 C CB    . ALA D  1 255 ? 53.501  69.727  223.173 1.00 64.47  ? 255 ALA D CB    1 
ATOM   13543 N N     . ILE D  1 256 ? 51.148  69.318  221.177 1.00 62.48  ? 256 ILE D N     1 
ATOM   13544 C CA    . ILE D  1 256 ? 50.567  68.830  219.923 1.00 64.29  ? 256 ILE D CA    1 
ATOM   13545 C C     . ILE D  1 256 ? 51.504  67.881  219.172 1.00 63.56  ? 256 ILE D C     1 
ATOM   13546 O O     . ILE D  1 256 ? 51.053  66.953  218.496 1.00 59.24  ? 256 ILE D O     1 
ATOM   13547 C CB    . ILE D  1 256 ? 50.180  70.014  218.986 1.00 66.77  ? 256 ILE D CB    1 
ATOM   13548 C CG1   . ILE D  1 256 ? 49.587  69.511  217.665 1.00 65.24  ? 256 ILE D CG1   1 
ATOM   13549 C CG2   . ILE D  1 256 ? 51.378  70.915  218.724 1.00 74.67  ? 256 ILE D CG2   1 
ATOM   13550 C CD1   . ILE D  1 256 ? 49.285  70.614  216.665 1.00 68.07  ? 256 ILE D CD1   1 
ATOM   13551 N N     . ASP D  1 257 ? 52.808  68.100  219.312 1.00 64.59  ? 257 ASP D N     1 
ATOM   13552 C CA    . ASP D  1 257 ? 53.796  67.286  218.616 1.00 60.02  ? 257 ASP D CA    1 
ATOM   13553 C C     . ASP D  1 257 ? 53.928  65.889  219.221 1.00 51.77  ? 257 ASP D C     1 
ATOM   13554 O O     . ASP D  1 257 ? 54.041  64.907  218.490 1.00 50.17  ? 257 ASP D O     1 
ATOM   13555 C CB    . ASP D  1 257 ? 55.154  67.990  218.610 1.00 61.64  ? 257 ASP D CB    1 
ATOM   13556 C CG    . ASP D  1 257 ? 55.153  69.244  217.758 1.00 72.46  ? 257 ASP D CG    1 
ATOM   13557 O OD1   . ASP D  1 257 ? 55.279  69.126  216.520 1.00 69.55  ? 257 ASP D OD1   1 
ATOM   13558 O OD2   . ASP D  1 257 ? 55.026  70.350  218.327 1.00 84.35  ? 257 ASP D OD2   1 
ATOM   13559 N N     . GLU D  1 258 ? 53.920  65.790  220.548 1.00 46.87  ? 258 GLU D N     1 
ATOM   13560 C CA    . GLU D  1 258 ? 53.973  64.475  221.180 1.00 47.21  ? 258 GLU D CA    1 
ATOM   13561 C C     . GLU D  1 258 ? 52.651  63.753  220.957 1.00 55.31  ? 258 GLU D C     1 
ATOM   13562 O O     . GLU D  1 258 ? 52.624  62.561  220.648 1.00 53.73  ? 258 GLU D O     1 
ATOM   13563 C CB    . GLU D  1 258 ? 54.277  64.576  222.676 1.00 48.36  ? 258 GLU D CB    1 
ATOM   13564 C CG    . GLU D  1 258 ? 54.506  63.218  223.331 1.00 59.08  ? 258 GLU D CG    1 
ATOM   13565 C CD    . GLU D  1 258 ? 54.839  63.312  224.806 1.00 61.65  ? 258 GLU D CD    1 
ATOM   13566 O OE1   . GLU D  1 258 ? 55.060  64.437  225.301 1.00 63.50  ? 258 GLU D OE1   1 
ATOM   13567 O OE2   . GLU D  1 258 ? 54.876  62.256  225.474 1.00 56.87  ? 258 GLU D OE2   1 
ATOM   13568 N N     . ALA D  1 259 ? 51.560  64.497  221.115 1.00 50.69  ? 259 ALA D N     1 
ATOM   13569 C CA    . ALA D  1 259 ? 50.214  63.980  220.912 1.00 52.74  ? 259 ALA D CA    1 
ATOM   13570 C C     . ALA D  1 259 ? 50.058  63.395  219.521 1.00 49.43  ? 259 ALA D C     1 
ATOM   13571 O O     . ALA D  1 259 ? 49.518  62.303  219.355 1.00 50.48  ? 259 ALA D O     1 
ATOM   13572 C CB    . ALA D  1 259 ? 49.207  65.067  221.128 1.00 52.33  ? 259 ALA D CB    1 
ATOM   13573 N N     . THR D  1 260 ? 50.537  64.136  218.528 1.00 49.15  ? 260 THR D N     1 
ATOM   13574 C CA    . THR D  1 260 ? 50.504  63.686  217.144 1.00 49.90  ? 260 THR D CA    1 
ATOM   13575 C C     . THR D  1 260 ? 51.244  62.361  216.983 1.00 52.04  ? 260 THR D C     1 
ATOM   13576 O O     . THR D  1 260 ? 50.772  61.457  216.294 1.00 50.46  ? 260 THR D O     1 
ATOM   13577 C CB    . THR D  1 260 ? 51.120  64.738  216.198 1.00 50.54  ? 260 THR D CB    1 
ATOM   13578 O OG1   . THR D  1 260 ? 50.429  65.982  216.359 1.00 56.11  ? 260 THR D OG1   1 
ATOM   13579 C CG2   . THR D  1 260 ? 51.022  64.287  214.750 1.00 48.65  ? 260 THR D CG2   1 
ATOM   13580 N N     . SER D  1 261 ? 52.393  62.244  217.643 1.00 49.88  ? 261 SER D N     1 
ATOM   13581 C CA    . SER D  1 261 ? 53.212  61.039  217.547 1.00 46.64  ? 261 SER D CA    1 
ATOM   13582 C C     . SER D  1 261 ? 52.571  59.873  218.290 1.00 43.86  ? 261 SER D C     1 
ATOM   13583 O O     . SER D  1 261 ? 52.663  58.729  217.847 1.00 45.90  ? 261 SER D O     1 
ATOM   13584 C CB    . SER D  1 261 ? 54.624  61.295  218.088 1.00 46.67  ? 261 SER D CB    1 
ATOM   13585 O OG    . SER D  1 261 ? 54.693  61.056  219.485 1.00 49.71  ? 261 SER D OG    1 
ATOM   13586 N N     . LEU D  1 262 ? 51.938  60.165  219.423 1.00 45.26  ? 262 LEU D N     1 
ATOM   13587 C CA    . LEU D  1 262 ? 51.207  59.149  220.176 1.00 48.22  ? 262 LEU D CA    1 
ATOM   13588 C C     . LEU D  1 262 ? 50.039  58.605  219.362 1.00 46.85  ? 262 LEU D C     1 
ATOM   13589 O O     . LEU D  1 262 ? 49.904  57.393  219.190 1.00 44.37  ? 262 LEU D O     1 
ATOM   13590 C CB    . LEU D  1 262 ? 50.696  59.711  221.505 1.00 47.77  ? 262 LEU D CB    1 
ATOM   13591 C CG    . LEU D  1 262 ? 51.646  59.677  222.704 1.00 54.56  ? 262 LEU D CG    1 
ATOM   13592 C CD1   . LEU D  1 262 ? 50.984  60.277  223.937 1.00 58.53  ? 262 LEU D CD1   1 
ATOM   13593 C CD2   . LEU D  1 262 ? 52.099  58.255  222.979 1.00 45.46  ? 262 LEU D CD2   1 
ATOM   13594 N N     . LEU D  1 263 ? 49.203  59.511  218.864 1.00 45.25  ? 263 LEU D N     1 
ATOM   13595 C CA    . LEU D  1 263 ? 48.044  59.139  218.057 1.00 45.07  ? 263 LEU D CA    1 
ATOM   13596 C C     . LEU D  1 263 ? 48.435  58.414  216.772 1.00 46.41  ? 263 LEU D C     1 
ATOM   13597 O O     . LEU D  1 263 ? 47.764  57.464  216.366 1.00 42.12  ? 263 LEU D O     1 
ATOM   13598 C CB    . LEU D  1 263 ? 47.205  60.377  217.717 1.00 44.10  ? 263 LEU D CB    1 
ATOM   13599 C CG    . LEU D  1 263 ? 46.380  60.989  218.855 1.00 49.09  ? 263 LEU D CG    1 
ATOM   13600 C CD1   . LEU D  1 263 ? 45.433  62.061  218.332 1.00 40.02  ? 263 LEU D CD1   1 
ATOM   13601 C CD2   . LEU D  1 263 ? 45.608  59.910  219.592 1.00 45.17  ? 263 LEU D CD2   1 
ATOM   13602 N N     . HIS D  1 264 ? 49.520  58.851  216.136 1.00 44.07  ? 264 HIS D N     1 
ATOM   13603 C CA    . HIS D  1 264 ? 49.963  58.223  214.891 1.00 45.82  ? 264 HIS D CA    1 
ATOM   13604 C C     . HIS D  1 264 ? 50.411  56.785  215.129 1.00 44.34  ? 264 HIS D C     1 
ATOM   13605 O O     . HIS D  1 264 ? 50.333  55.945  214.230 1.00 40.60  ? 264 HIS D O     1 
ATOM   13606 C CB    . HIS D  1 264 ? 51.102  59.013  214.244 1.00 45.79  ? 264 HIS D CB    1 
ATOM   13607 C CG    . HIS D  1 264 ? 51.527  58.473  212.912 1.00 43.11  ? 264 HIS D CG    1 
ATOM   13608 N ND1   . HIS D  1 264 ? 52.562  57.574  212.769 1.00 40.97  ? 264 HIS D ND1   1 
ATOM   13609 C CD2   . HIS D  1 264 ? 51.041  58.686  211.666 1.00 40.73  ? 264 HIS D CD2   1 
ATOM   13610 C CE1   . HIS D  1 264 ? 52.703  57.266  211.492 1.00 41.78  ? 264 HIS D CE1   1 
ATOM   13611 N NE2   . HIS D  1 264 ? 51.792  57.925  210.801 1.00 48.65  ? 264 HIS D NE2   1 
ATOM   13612 N N     . LYS D  1 265 ? 50.882  56.494  216.336 1.00 37.20  ? 265 LYS D N     1 
ATOM   13613 C CA    . LYS D  1 265 ? 51.256  55.127  216.659 1.00 40.82  ? 265 LYS D CA    1 
ATOM   13614 C C     . LYS D  1 265 ? 50.060  54.353  217.204 1.00 42.90  ? 265 LYS D C     1 
ATOM   13615 O O     . LYS D  1 265 ? 49.928  53.156  216.956 1.00 37.02  ? 265 LYS D O     1 
ATOM   13616 C CB    . LYS D  1 265 ? 52.403  55.084  217.667 1.00 38.34  ? 265 LYS D CB    1 
ATOM   13617 C CG    . LYS D  1 265 ? 52.826  53.657  217.971 1.00 45.46  ? 265 LYS D CG    1 
ATOM   13618 C CD    . LYS D  1 265 ? 53.900  53.550  219.031 1.00 46.51  ? 265 LYS D CD    1 
ATOM   13619 C CE    . LYS D  1 265 ? 54.129  52.085  219.375 1.00 47.94  ? 265 LYS D CE    1 
ATOM   13620 N NZ    . LYS D  1 265 ? 55.378  51.846  220.146 1.00 46.71  ? 265 LYS D NZ    1 
ATOM   13621 N N     . TRP D  1 266 ? 49.197  55.045  217.945 1.00 42.30  ? 266 TRP D N     1 
ATOM   13622 C CA    . TRP D  1 266 ? 48.023  54.418  218.546 1.00 41.38  ? 266 TRP D CA    1 
ATOM   13623 C C     . TRP D  1 266 ? 47.188  53.667  217.512 1.00 36.91  ? 266 TRP D C     1 
ATOM   13624 O O     . TRP D  1 266 ? 46.706  52.567  217.777 1.00 37.87  ? 266 TRP D O     1 
ATOM   13625 C CB    . TRP D  1 266 ? 47.140  55.456  219.254 1.00 41.32  ? 266 TRP D CB    1 
ATOM   13626 C CG    . TRP D  1 266 ? 45.750  54.934  219.480 1.00 39.53  ? 266 TRP D CG    1 
ATOM   13627 C CD1   . TRP D  1 266 ? 45.314  54.188  220.537 1.00 40.28  ? 266 TRP D CD1   1 
ATOM   13628 C CD2   . TRP D  1 266 ? 44.625  55.085  218.606 1.00 34.62  ? 266 TRP D CD2   1 
ATOM   13629 N NE1   . TRP D  1 266 ? 43.985  53.873  220.379 1.00 42.72  ? 266 TRP D NE1   1 
ATOM   13630 C CE2   . TRP D  1 266 ? 43.540  54.410  219.201 1.00 41.38  ? 266 TRP D CE2   1 
ATOM   13631 C CE3   . TRP D  1 266 ? 44.430  55.726  217.380 1.00 35.44  ? 266 TRP D CE3   1 
ATOM   13632 C CZ2   . TRP D  1 266 ? 42.279  54.364  218.613 1.00 37.66  ? 266 TRP D CZ2   1 
ATOM   13633 C CZ3   . TRP D  1 266 ? 43.182  55.674  216.797 1.00 41.65  ? 266 TRP D CZ3   1 
ATOM   13634 C CH2   . TRP D  1 266 ? 42.124  54.992  217.411 1.00 36.01  ? 266 TRP D CH2   1 
ATOM   13635 N N     . GLN D  1 267 ? 47.031  54.267  216.333 1.00 38.17  ? 267 GLN D N     1 
ATOM   13636 C CA    . GLN D  1 267 ? 46.166  53.717  215.289 1.00 36.42  ? 267 GLN D CA    1 
ATOM   13637 C C     . GLN D  1 267 ? 46.575  52.305  214.885 1.00 44.14  ? 267 GLN D C     1 
ATOM   13638 O O     . GLN D  1 267 ? 45.731  51.474  214.537 1.00 43.82  ? 267 GLN D O     1 
ATOM   13639 C CB    . GLN D  1 267 ? 46.163  54.634  214.060 1.00 40.75  ? 267 GLN D CB    1 
ATOM   13640 C CG    . GLN D  1 267 ? 47.469  54.659  213.278 1.00 40.97  ? 267 GLN D CG    1 
ATOM   13641 C CD    . GLN D  1 267 ? 47.440  55.607  212.097 1.00 42.12  ? 267 GLN D CD    1 
ATOM   13642 O OE1   . GLN D  1 267 ? 46.507  55.593  211.292 1.00 44.12  ? 267 GLN D OE1   1 
ATOM   13643 N NE2   . GLN D  1 267 ? 48.466  56.444  211.990 1.00 43.30  ? 267 GLN D NE2   1 
ATOM   13644 N N     . PHE D  1 268 ? 47.874  52.037  214.946 1.00 38.69  ? 268 PHE D N     1 
ATOM   13645 C CA    . PHE D  1 268 ? 48.395  50.740  214.557 1.00 39.39  ? 268 PHE D CA    1 
ATOM   13646 C C     . PHE D  1 268 ? 48.245  49.762  215.711 1.00 43.61  ? 268 PHE D C     1 
ATOM   13647 O O     . PHE D  1 268 ? 47.822  48.627  215.515 1.00 43.48  ? 268 PHE D O     1 
ATOM   13648 C CB    . PHE D  1 268 ? 49.855  50.854  214.113 1.00 41.06  ? 268 PHE D CB    1 
ATOM   13649 C CG    . PHE D  1 268 ? 50.050  51.727  212.902 1.00 39.83  ? 268 PHE D CG    1 
ATOM   13650 C CD1   . PHE D  1 268 ? 49.606  51.315  211.656 1.00 39.47  ? 268 PHE D CD1   1 
ATOM   13651 C CD2   . PHE D  1 268 ? 50.681  52.955  213.010 1.00 42.52  ? 268 PHE D CD2   1 
ATOM   13652 C CE1   . PHE D  1 268 ? 49.781  52.112  210.540 1.00 44.33  ? 268 PHE D CE1   1 
ATOM   13653 C CE2   . PHE D  1 268 ? 50.862  53.759  211.897 1.00 45.04  ? 268 PHE D CE2   1 
ATOM   13654 C CZ    . PHE D  1 268 ? 50.410  53.336  210.660 1.00 38.91  ? 268 PHE D CZ    1 
ATOM   13655 N N     . VAL D  1 269 ? 48.569  50.218  216.917 1.00 33.89  ? 269 VAL D N     1 
ATOM   13656 C CA    . VAL D  1 269 ? 48.400  49.406  218.118 1.00 37.19  ? 269 VAL D CA    1 
ATOM   13657 C C     . VAL D  1 269 ? 46.939  48.996  218.294 1.00 41.06  ? 269 VAL D C     1 
ATOM   13658 O O     . VAL D  1 269 ? 46.637  47.823  218.500 1.00 35.09  ? 269 VAL D O     1 
ATOM   13659 C CB    . VAL D  1 269 ? 48.876  50.153  219.381 1.00 37.31  ? 269 VAL D CB    1 
ATOM   13660 C CG1   . VAL D  1 269 ? 48.574  49.331  220.632 1.00 38.83  ? 269 VAL D CG1   1 
ATOM   13661 C CG2   . VAL D  1 269 ? 50.365  50.486  219.281 1.00 42.85  ? 269 VAL D CG2   1 
ATOM   13662 N N     . ALA D  1 270 ? 46.041  49.972  218.193 1.00 36.87  ? 270 ALA D N     1 
ATOM   13663 C CA    . ALA D  1 270 ? 44.612  49.740  218.385 1.00 35.46  ? 270 ALA D CA    1 
ATOM   13664 C C     . ALA D  1 270 ? 44.065  48.664  217.447 1.00 38.02  ? 270 ALA D C     1 
ATOM   13665 O O     . ALA D  1 270 ? 43.312  47.789  217.871 1.00 39.53  ? 270 ALA D O     1 
ATOM   13666 C CB    . ALA D  1 270 ? 43.842  51.043  218.200 1.00 35.96  ? 270 ALA D CB    1 
ATOM   13667 N N     . GLU D  1 271 ? 44.453  48.725  216.178 1.00 41.35  ? 271 GLU D N     1 
ATOM   13668 C CA    . GLU D  1 271 ? 43.933  47.794  215.183 1.00 40.76  ? 271 GLU D CA    1 
ATOM   13669 C C     . GLU D  1 271 ? 44.631  46.433  215.225 1.00 40.87  ? 271 GLU D C     1 
ATOM   13670 O O     . GLU D  1 271 ? 44.021  45.405  214.932 1.00 44.56  ? 271 GLU D O     1 
ATOM   13671 C CB    . GLU D  1 271 ? 44.060  48.394  213.781 1.00 44.05  ? 271 GLU D CB    1 
ATOM   13672 C CG    . GLU D  1 271 ? 43.411  47.559  212.691 1.00 47.81  ? 271 GLU D CG    1 
ATOM   13673 C CD    . GLU D  1 271 ? 43.811  48.007  211.303 1.00 55.76  ? 271 GLU D CD    1 
ATOM   13674 O OE1   . GLU D  1 271 ? 44.453  49.072  211.184 1.00 55.53  ? 271 GLU D OE1   1 
ATOM   13675 O OE2   . GLU D  1 271 ? 43.492  47.290  210.332 1.00 59.82  ? 271 GLU D OE2   1 
ATOM   13676 N N     . GLU D  1 272 ? 45.907  46.430  215.598 1.00 44.68  ? 272 GLU D N     1 
ATOM   13677 C CA    . GLU D  1 272 ? 46.717  45.215  215.534 1.00 43.21  ? 272 GLU D CA    1 
ATOM   13678 C C     . GLU D  1 272 ? 46.682  44.380  216.810 1.00 40.27  ? 272 GLU D C     1 
ATOM   13679 O O     . GLU D  1 272 ? 47.100  43.220  216.800 1.00 48.20  ? 272 GLU D O     1 
ATOM   13680 C CB    . GLU D  1 272 ? 48.163  45.569  215.196 1.00 43.70  ? 272 GLU D CB    1 
ATOM   13681 C CG    . GLU D  1 272 ? 48.353  46.012  213.760 1.00 45.45  ? 272 GLU D CG    1 
ATOM   13682 C CD    . GLU D  1 272 ? 49.584  46.871  213.574 1.00 59.99  ? 272 GLU D CD    1 
ATOM   13683 O OE1   . GLU D  1 272 ? 50.466  46.853  214.458 1.00 65.72  ? 272 GLU D OE1   1 
ATOM   13684 O OE2   . GLU D  1 272 ? 49.670  47.569  212.540 1.00 57.78  ? 272 GLU D OE2   1 
ATOM   13685 N N     . LEU D  1 273 ? 46.204  44.971  217.902 1.00 37.50  ? 273 LEU D N     1 
ATOM   13686 C CA    . LEU D  1 273 ? 46.050  44.248  219.161 1.00 39.97  ? 273 LEU D CA    1 
ATOM   13687 C C     . LEU D  1 273 ? 45.247  42.966  218.961 1.00 46.39  ? 273 LEU D C     1 
ATOM   13688 O O     . LEU D  1 273 ? 44.338  42.920  218.130 1.00 44.31  ? 273 LEU D O     1 
ATOM   13689 C CB    . LEU D  1 273 ? 45.366  45.130  220.212 1.00 41.75  ? 273 LEU D CB    1 
ATOM   13690 C CG    . LEU D  1 273 ? 46.222  46.108  221.022 1.00 38.81  ? 273 LEU D CG    1 
ATOM   13691 C CD1   . LEU D  1 273 ? 45.352  47.180  221.677 1.00 41.93  ? 273 LEU D CD1   1 
ATOM   13692 C CD2   . LEU D  1 273 ? 47.041  45.363  222.065 1.00 35.71  ? 273 LEU D CD2   1 
ATOM   13693 N N     . GLU D  1 274 ? 45.592  41.925  219.715 1.00 44.00  ? 274 GLU D N     1 
ATOM   13694 C CA    . GLU D  1 274 ? 44.787  40.706  219.733 1.00 45.64  ? 274 GLU D CA    1 
ATOM   13695 C C     . GLU D  1 274 ? 43.363  41.052  220.157 1.00 46.86  ? 274 GLU D C     1 
ATOM   13696 O O     . GLU D  1 274 ? 43.141  42.044  220.855 1.00 46.30  ? 274 GLU D O     1 
ATOM   13697 C CB    . GLU D  1 274 ? 45.392  39.658  220.670 1.00 46.89  ? 274 GLU D CB    1 
ATOM   13698 C CG    . GLU D  1 274 ? 46.692  39.041  220.165 1.00 43.88  ? 274 GLU D CG    1 
ATOM   13699 C CD    . GLU D  1 274 ? 46.491  38.211  218.913 1.00 50.06  ? 274 GLU D CD    1 
ATOM   13700 O OE1   . GLU D  1 274 ? 45.766  37.196  218.980 1.00 61.31  ? 274 GLU D OE1   1 
ATOM   13701 O OE2   . GLU D  1 274 ? 47.059  38.572  217.860 1.00 52.38  ? 274 GLU D OE2   1 
ATOM   13702 N N     . GLU D  1 275 ? 42.400  40.237  219.739 1.00 44.75  ? 275 GLU D N     1 
ATOM   13703 C CA    . GLU D  1 275 ? 40.990  40.546  219.954 1.00 47.49  ? 275 GLU D CA    1 
ATOM   13704 C C     . GLU D  1 275 ? 40.617  40.604  221.439 1.00 47.25  ? 275 GLU D C     1 
ATOM   13705 O O     . GLU D  1 275 ? 39.560  41.122  221.798 1.00 49.50  ? 275 GLU D O     1 
ATOM   13706 C CB    . GLU D  1 275 ? 40.109  39.525  219.228 1.00 45.75  ? 275 GLU D CB    1 
ATOM   13707 C CG    . GLU D  1 275 ? 40.317  38.085  219.662 1.00 51.41  ? 275 GLU D CG    1 
ATOM   13708 C CD    . GLU D  1 275 ? 39.428  37.116  218.901 1.00 60.97  ? 275 GLU D CD    1 
ATOM   13709 O OE1   . GLU D  1 275 ? 39.224  37.317  217.684 1.00 61.60  ? 275 GLU D OE1   1 
ATOM   13710 O OE2   . GLU D  1 275 ? 38.928  36.154  219.521 1.00 63.98  ? 275 GLU D OE2   1 
ATOM   13711 N N     . ASP D  1 276 ? 41.493  40.091  222.298 1.00 45.22  ? 276 ASP D N     1 
ATOM   13712 C CA    . ASP D  1 276 ? 41.272  40.144  223.740 1.00 45.67  ? 276 ASP D CA    1 
ATOM   13713 C C     . ASP D  1 276 ? 41.694  41.490  224.329 1.00 47.53  ? 276 ASP D C     1 
ATOM   13714 O O     . ASP D  1 276 ? 41.701  41.666  225.546 1.00 49.09  ? 276 ASP D O     1 
ATOM   13715 C CB    . ASP D  1 276 ? 42.025  39.008  224.441 1.00 55.09  ? 276 ASP D CB    1 
ATOM   13716 C CG    . ASP D  1 276 ? 41.375  37.654  224.225 1.00 58.58  ? 276 ASP D CG    1 
ATOM   13717 O OD1   . ASP D  1 276 ? 40.155  37.614  223.963 1.00 54.88  ? 276 ASP D OD1   1 
ATOM   13718 O OD2   . ASP D  1 276 ? 42.084  36.629  224.320 1.00 64.26  ? 276 ASP D OD2   1 
ATOM   13719 N N     . PHE D  1 277 ? 42.042  42.436  223.462 1.00 48.27  ? 277 PHE D N     1 
ATOM   13720 C CA    . PHE D  1 277 ? 42.464  43.763  223.898 1.00 41.21  ? 277 PHE D CA    1 
ATOM   13721 C C     . PHE D  1 277 ? 41.676  44.872  223.202 1.00 41.97  ? 277 PHE D C     1 
ATOM   13722 O O     . PHE D  1 277 ? 41.261  44.719  222.054 1.00 42.12  ? 277 PHE D O     1 
ATOM   13723 C CB    . PHE D  1 277 ? 43.961  43.961  223.633 1.00 44.47  ? 277 PHE D CB    1 
ATOM   13724 C CG    . PHE D  1 277 ? 44.859  43.235  224.596 1.00 44.67  ? 277 PHE D CG    1 
ATOM   13725 C CD1   . PHE D  1 277 ? 45.349  43.876  225.722 1.00 52.03  ? 277 PHE D CD1   1 
ATOM   13726 C CD2   . PHE D  1 277 ? 45.229  41.919  224.367 1.00 49.94  ? 277 PHE D CD2   1 
ATOM   13727 C CE1   . PHE D  1 277 ? 46.184  43.218  226.608 1.00 55.40  ? 277 PHE D CE1   1 
ATOM   13728 C CE2   . PHE D  1 277 ? 46.064  41.253  225.250 1.00 52.46  ? 277 PHE D CE2   1 
ATOM   13729 C CZ    . PHE D  1 277 ? 46.542  41.905  226.372 1.00 50.25  ? 277 PHE D CZ    1 
ATOM   13730 N N     . THR D  1 278 ? 41.479  45.986  223.901 1.00 38.55  ? 278 THR D N     1 
ATOM   13731 C CA    . THR D  1 278 ? 40.911  47.182  223.291 1.00 39.76  ? 278 THR D CA    1 
ATOM   13732 C C     . THR D  1 278 ? 41.591  48.422  223.856 1.00 39.19  ? 278 THR D C     1 
ATOM   13733 O O     . THR D  1 278 ? 41.715  48.571  225.073 1.00 46.07  ? 278 THR D O     1 
ATOM   13734 C CB    . THR D  1 278 ? 39.391  47.290  223.517 1.00 37.86  ? 278 THR D CB    1 
ATOM   13735 O OG1   . THR D  1 278 ? 38.736  46.175  222.902 1.00 37.86  ? 278 THR D OG1   1 
ATOM   13736 C CG2   . THR D  1 278 ? 38.850  48.585  222.914 1.00 35.01  ? 278 THR D CG2   1 
ATOM   13737 N N     . LEU D  1 279 ? 42.045  49.303  222.971 1.00 35.89  ? 279 LEU D N     1 
ATOM   13738 C CA    . LEU D  1 279 ? 42.638  50.567  223.387 1.00 38.00  ? 279 LEU D CA    1 
ATOM   13739 C C     . LEU D  1 279 ? 41.958  51.736  222.685 1.00 38.69  ? 279 LEU D C     1 
ATOM   13740 O O     . LEU D  1 279 ? 42.083  51.893  221.472 1.00 41.43  ? 279 LEU D O     1 
ATOM   13741 C CB    . LEU D  1 279 ? 44.140  50.587  223.099 1.00 38.09  ? 279 LEU D CB    1 
ATOM   13742 C CG    . LEU D  1 279 ? 44.850  51.878  223.512 1.00 43.39  ? 279 LEU D CG    1 
ATOM   13743 C CD1   . LEU D  1 279 ? 44.746  52.089  225.014 1.00 43.17  ? 279 LEU D CD1   1 
ATOM   13744 C CD2   . LEU D  1 279 ? 46.305  51.873  223.065 1.00 44.01  ? 279 LEU D CD2   1 
ATOM   13745 N N     . SER D  1 280 ? 41.251  52.559  223.452 1.00 41.54  ? 280 SER D N     1 
ATOM   13746 C CA    . SER D  1 280 ? 40.477  53.657  222.884 1.00 44.50  ? 280 SER D CA    1 
ATOM   13747 C C     . SER D  1 280 ? 41.010  55.005  223.350 1.00 45.07  ? 280 SER D C     1 
ATOM   13748 O O     . SER D  1 280 ? 41.695  55.085  224.365 1.00 44.93  ? 280 SER D O     1 
ATOM   13749 C CB    . SER D  1 280 ? 39.002  53.517  223.258 1.00 36.14  ? 280 SER D CB    1 
ATOM   13750 O OG    . SER D  1 280 ? 38.495  52.263  222.843 1.00 51.72  ? 280 SER D OG    1 
ATOM   13751 N N     . VAL D  1 281 ? 40.692  56.061  222.606 1.00 38.76  ? 281 VAL D N     1 
ATOM   13752 C CA    . VAL D  1 281 ? 41.201  57.394  222.919 1.00 41.13  ? 281 VAL D CA    1 
ATOM   13753 C C     . VAL D  1 281 ? 40.102  58.446  222.985 1.00 46.44  ? 281 VAL D C     1 
ATOM   13754 O O     . VAL D  1 281 ? 39.279  58.555  222.077 1.00 43.27  ? 281 VAL D O     1 
ATOM   13755 C CB    . VAL D  1 281 ? 42.245  57.866  221.877 1.00 46.17  ? 281 VAL D CB    1 
ATOM   13756 C CG1   . VAL D  1 281 ? 42.843  59.206  222.286 1.00 44.37  ? 281 VAL D CG1   1 
ATOM   13757 C CG2   . VAL D  1 281 ? 43.338  56.830  221.708 1.00 40.08  ? 281 VAL D CG2   1 
ATOM   13758 N N     . LEU D  1 282 ? 40.094  59.217  224.066 1.00 53.35  ? 282 LEU D N     1 
ATOM   13759 C CA    . LEU D  1 282 ? 39.289  60.430  224.138 1.00 53.17  ? 282 LEU D CA    1 
ATOM   13760 C C     . LEU D  1 282 ? 40.237  61.624  224.155 1.00 55.66  ? 282 LEU D C     1 
ATOM   13761 O O     . LEU D  1 282 ? 41.139  61.694  224.989 1.00 57.98  ? 282 LEU D O     1 
ATOM   13762 C CB    . LEU D  1 282 ? 38.391  60.432  225.378 1.00 51.83  ? 282 LEU D CB    1 
ATOM   13763 C CG    . LEU D  1 282 ? 37.294  59.370  225.463 1.00 61.41  ? 282 LEU D CG    1 
ATOM   13764 C CD1   . LEU D  1 282 ? 36.685  59.358  226.855 1.00 61.90  ? 282 LEU D CD1   1 
ATOM   13765 C CD2   . LEU D  1 282 ? 36.213  59.608  224.419 1.00 53.34  ? 282 LEU D CD2   1 
ATOM   13766 N N     . GLY D  1 283 ? 40.041  62.555  223.228 1.00 54.26  ? 283 GLY D N     1 
ATOM   13767 C CA    . GLY D  1 283 ? 40.922  63.704  223.118 1.00 50.25  ? 283 GLY D CA    1 
ATOM   13768 C C     . GLY D  1 283 ? 40.179  65.020  223.217 1.00 57.54  ? 283 GLY D C     1 
ATOM   13769 O O     . GLY D  1 283 ? 39.015  65.114  222.830 1.00 55.93  ? 283 GLY D O     1 
ATOM   13770 N N     . GLY D  1 284 ? 40.849  66.042  223.738 1.00 58.25  ? 284 GLY D N     1 
ATOM   13771 C CA    . GLY D  1 284 ? 40.229  67.343  223.892 1.00 60.85  ? 284 GLY D CA    1 
ATOM   13772 C C     . GLY D  1 284 ? 41.225  68.476  224.014 1.00 69.37  ? 284 GLY D C     1 
ATOM   13773 O O     . GLY D  1 284 ? 42.430  68.256  224.147 1.00 68.45  ? 284 GLY D O     1 
ATOM   13774 N N     . ALA D  1 285 ? 40.712  69.698  223.976 1.00 70.85  ? 285 ALA D N     1 
ATOM   13775 C CA    . ALA D  1 285 ? 41.558  70.879  224.032 1.00 71.91  ? 285 ALA D CA    1 
ATOM   13776 C C     . ALA D  1 285 ? 41.709  71.418  225.446 1.00 79.28  ? 285 ALA D C     1 
ATOM   13777 O O     . ALA D  1 285 ? 40.752  71.440  226.218 1.00 83.04  ? 285 ALA D O     1 
ATOM   13778 C CB    . ALA D  1 285 ? 40.995  71.962  223.138 1.00 63.58  ? 285 ALA D CB    1 
ATOM   13779 N N     . ASP D  1 286 ? 42.921  71.839  225.785 1.00 89.24  ? 286 ASP D N     1 
ATOM   13780 C CA    . ASP D  1 286 ? 43.080  72.864  226.802 1.00 96.55  ? 286 ASP D CA    1 
ATOM   13781 C C     . ASP D  1 286 ? 44.076  73.883  226.253 1.00 94.05  ? 286 ASP D C     1 
ATOM   13782 O O     . ASP D  1 286 ? 45.082  73.514  225.645 1.00 95.03  ? 286 ASP D O     1 
ATOM   13783 C CB    . ASP D  1 286 ? 43.501  72.282  228.168 1.00 99.43  ? 286 ASP D CB    1 
ATOM   13784 C CG    . ASP D  1 286 ? 44.810  71.515  228.127 1.00 99.16  ? 286 ASP D CG    1 
ATOM   13785 O OD1   . ASP D  1 286 ? 45.819  72.079  227.676 1.00 99.77  ? 286 ASP D OD1   1 
ATOM   13786 O OD2   . ASP D  1 286 ? 44.837  70.350  228.581 1.00 97.21  ? 286 ASP D OD2   1 
ATOM   13787 N N     . GLU D  1 287 ? 43.747  75.162  226.417 1.00 94.61  ? 287 GLU D N     1 
ATOM   13788 C CA    . GLU D  1 287 ? 44.570  76.272  225.929 1.00 94.48  ? 287 GLU D CA    1 
ATOM   13789 C C     . GLU D  1 287 ? 45.065  76.058  224.491 1.00 93.45  ? 287 GLU D C     1 
ATOM   13790 O O     . GLU D  1 287 ? 44.390  76.434  223.531 1.00 94.26  ? 287 GLU D O     1 
ATOM   13791 C CB    . GLU D  1 287 ? 45.749  76.489  226.873 1.00 97.01  ? 287 GLU D CB    1 
ATOM   13792 C CG    . GLU D  1 287 ? 45.371  76.445  228.354 1.00 99.41  ? 287 GLU D CG    1 
ATOM   13793 C CD    . GLU D  1 287 ? 44.443  77.574  228.772 1.00 102.73 ? 287 GLU D CD    1 
ATOM   13794 O OE1   . GLU D  1 287 ? 44.399  78.608  228.072 1.00 106.60 ? 287 GLU D OE1   1 
ATOM   13795 O OE2   . GLU D  1 287 ? 43.759  77.429  229.808 1.00 101.26 ? 287 GLU D OE2   1 
ATOM   13796 N N     . LYS D  1 288 ? 46.247  75.460  224.357 1.00 95.86  ? 288 LYS D N     1 
ATOM   13797 C CA    . LYS D  1 288 ? 46.739  74.982  223.065 1.00 94.86  ? 288 LYS D CA    1 
ATOM   13798 C C     . LYS D  1 288 ? 47.559  73.702  223.276 1.00 94.85  ? 288 LYS D C     1 
ATOM   13799 O O     . LYS D  1 288 ? 48.221  73.213  222.363 1.00 94.57  ? 288 LYS D O     1 
ATOM   13800 C CB    . LYS D  1 288 ? 47.567  76.058  222.342 1.00 101.40 ? 288 LYS D CB    1 
ATOM   13801 C CG    . LYS D  1 288 ? 47.327  76.158  220.826 1.00 106.27 ? 288 LYS D CG    1 
ATOM   13802 C CD    . LYS D  1 288 ? 47.929  74.973  220.089 1.00 112.92 ? 288 LYS D CD    1 
ATOM   13803 C CE    . LYS D  1 288 ? 47.791  75.028  218.587 1.00 107.24 ? 288 LYS D CE    1 
ATOM   13804 N NZ    . LYS D  1 288 ? 48.910  74.250  217.982 1.00 116.60 ? 288 LYS D NZ    1 
ATOM   13805 N N     . GLN D  1 289 ? 47.518  73.159  224.489 1.00 94.29  ? 289 GLN D N     1 
ATOM   13806 C CA    . GLN D  1 289 ? 47.949  71.785  224.691 1.00 95.75  ? 289 GLN D CA    1 
ATOM   13807 C C     . GLN D  1 289 ? 46.804  70.909  224.228 1.00 91.35  ? 289 GLN D C     1 
ATOM   13808 O O     . GLN D  1 289 ? 45.757  71.418  223.836 1.00 87.01  ? 289 GLN D O     1 
ATOM   13809 C CB    . GLN D  1 289 ? 48.274  71.505  226.157 1.00 94.44  ? 289 GLN D CB    1 
ATOM   13810 C CG    . GLN D  1 289 ? 49.471  70.614  226.404 1.00 92.97  ? 289 GLN D CG    1 
ATOM   13811 C CD    . GLN D  1 289 ? 50.761  71.401  226.491 1.00 90.08  ? 289 GLN D CD    1 
ATOM   13812 O OE1   . GLN D  1 289 ? 51.083  72.193  225.604 1.00 89.86  ? 289 GLN D OE1   1 
ATOM   13813 N NE2   . GLN D  1 289 ? 51.506  71.191  227.569 1.00 87.57  ? 289 GLN D NE2   1 
ATOM   13814 N N     . VAL D  1 290 ? 46.987  69.597  224.268 1.00 85.29  ? 290 VAL D N     1 
ATOM   13815 C CA    . VAL D  1 290 ? 45.849  68.696  224.157 1.00 77.34  ? 290 VAL D CA    1 
ATOM   13816 C C     . VAL D  1 290 ? 45.957  67.651  225.246 1.00 74.97  ? 290 VAL D C     1 
ATOM   13817 O O     . VAL D  1 290 ? 47.053  67.337  225.710 1.00 74.08  ? 290 VAL D O     1 
ATOM   13818 C CB    . VAL D  1 290 ? 45.765  67.993  222.789 1.00 73.06  ? 290 VAL D CB    1 
ATOM   13819 C CG1   . VAL D  1 290 ? 45.651  69.002  221.659 1.00 69.49  ? 290 VAL D CG1   1 
ATOM   13820 C CG2   . VAL D  1 290 ? 46.953  67.091  222.594 1.00 64.59  ? 290 VAL D CG2   1 
ATOM   13821 N N     . TRP D  1 291 ? 44.822  67.117  225.667 1.00 67.49  ? 291 TRP D N     1 
ATOM   13822 C CA    . TRP D  1 291 ? 44.851  65.994  226.583 1.00 65.50  ? 291 TRP D CA    1 
ATOM   13823 C C     . TRP D  1 291 ? 44.356  64.748  225.868 1.00 64.59  ? 291 TRP D C     1 
ATOM   13824 O O     . TRP D  1 291 ? 43.414  64.803  225.078 1.00 63.87  ? 291 TRP D O     1 
ATOM   13825 C CB    . TRP D  1 291 ? 44.016  66.277  227.832 1.00 66.44  ? 291 TRP D CB    1 
ATOM   13826 C CG    . TRP D  1 291 ? 42.605  66.654  227.546 1.00 70.35  ? 291 TRP D CG    1 
ATOM   13827 C CD1   . TRP D  1 291 ? 42.124  67.908  227.310 1.00 71.05  ? 291 TRP D CD1   1 
ATOM   13828 C CD2   . TRP D  1 291 ? 41.481  65.771  227.471 1.00 63.26  ? 291 TRP D CD2   1 
ATOM   13829 N NE1   . TRP D  1 291 ? 40.770  67.861  227.091 1.00 67.15  ? 291 TRP D NE1   1 
ATOM   13830 C CE2   . TRP D  1 291 ? 40.350  66.560  227.184 1.00 65.29  ? 291 TRP D CE2   1 
ATOM   13831 C CE3   . TRP D  1 291 ? 41.321  64.390  227.618 1.00 63.79  ? 291 TRP D CE3   1 
ATOM   13832 C CZ2   . TRP D  1 291 ? 39.077  66.014  227.039 1.00 63.76  ? 291 TRP D CZ2   1 
ATOM   13833 C CZ3   . TRP D  1 291 ? 40.056  63.850  227.474 1.00 60.54  ? 291 TRP D CZ3   1 
ATOM   13834 C CH2   . TRP D  1 291 ? 38.951  64.660  227.188 1.00 59.23  ? 291 TRP D CH2   1 
ATOM   13835 N N     . LEU D  1 292 ? 45.015  63.628  226.126 1.00 63.10  ? 292 LEU D N     1 
ATOM   13836 C CA    . LEU D  1 292 ? 44.600  62.362  225.547 1.00 59.30  ? 292 LEU D CA    1 
ATOM   13837 C C     . LEU D  1 292 ? 44.349  61.356  226.655 1.00 64.50  ? 292 LEU D C     1 
ATOM   13838 O O     . LEU D  1 292 ? 45.245  61.055  227.440 1.00 62.61  ? 292 LEU D O     1 
ATOM   13839 C CB    . LEU D  1 292 ? 45.655  61.830  224.576 1.00 58.28  ? 292 LEU D CB    1 
ATOM   13840 C CG    . LEU D  1 292 ? 46.019  62.703  223.371 1.00 57.34  ? 292 LEU D CG    1 
ATOM   13841 C CD1   . LEU D  1 292 ? 47.118  62.044  222.548 1.00 55.62  ? 292 LEU D CD1   1 
ATOM   13842 C CD2   . LEU D  1 292 ? 44.801  62.998  222.502 1.00 51.11  ? 292 LEU D CD2   1 
ATOM   13843 N N     . THR D  1 293 ? 43.127  60.846  226.729 1.00 55.19  ? 293 THR D N     1 
ATOM   13844 C CA    . THR D  1 293 ? 42.824  59.806  227.697 1.00 60.49  ? 293 THR D CA    1 
ATOM   13845 C C     . THR D  1 293 ? 42.835  58.448  227.014 1.00 56.69  ? 293 THR D C     1 
ATOM   13846 O O     . THR D  1 293 ? 41.996  58.159  226.160 1.00 53.53  ? 293 THR D O     1 
ATOM   13847 C CB    . THR D  1 293 ? 41.464  60.031  228.376 1.00 60.06  ? 293 THR D CB    1 
ATOM   13848 O OG1   . THR D  1 293 ? 41.420  61.352  228.927 1.00 60.03  ? 293 THR D OG1   1 
ATOM   13849 C CG2   . THR D  1 293 ? 41.256  59.015  229.488 1.00 58.71  ? 293 THR D CG2   1 
ATOM   13850 N N     . MET D  1 294 ? 43.805  57.621  227.384 1.00 61.51  ? 294 MET D N     1 
ATOM   13851 C CA    . MET D  1 294 ? 43.899  56.275  226.848 1.00 53.57  ? 294 MET D CA    1 
ATOM   13852 C C     . MET D  1 294 ? 43.053  55.339  227.695 1.00 54.98  ? 294 MET D C     1 
ATOM   13853 O O     . MET D  1 294 ? 43.243  55.254  228.907 1.00 60.39  ? 294 MET D O     1 
ATOM   13854 C CB    . MET D  1 294 ? 45.354  55.806  226.820 1.00 55.16  ? 294 MET D CB    1 
ATOM   13855 C CG    . MET D  1 294 ? 46.302  56.776  226.137 1.00 57.67  ? 294 MET D CG    1 
ATOM   13856 S SD    . MET D  1 294 ? 45.888  57.072  224.410 1.00 60.29  ? 294 MET D SD    1 
ATOM   13857 C CE    . MET D  1 294 ? 45.964  55.407  223.756 1.00 46.39  ? 294 MET D CE    1 
ATOM   13858 N N     . LEU D  1 295 ? 42.109  54.650  227.063 1.00 48.19  ? 295 LEU D N     1 
ATOM   13859 C CA    . LEU D  1 295 ? 41.259  53.714  227.784 1.00 48.54  ? 295 LEU D CA    1 
ATOM   13860 C C     . LEU D  1 295 ? 41.534  52.289  227.326 1.00 47.16  ? 295 LEU D C     1 
ATOM   13861 O O     . LEU D  1 295 ? 41.430  51.973  226.140 1.00 45.15  ? 295 LEU D O     1 
ATOM   13862 C CB    . LEU D  1 295 ? 39.785  54.075  227.597 1.00 51.62  ? 295 LEU D CB    1 
ATOM   13863 C CG    . LEU D  1 295 ? 39.453  55.494  228.071 1.00 54.52  ? 295 LEU D CG    1 
ATOM   13864 C CD1   . LEU D  1 295 ? 38.827  56.315  226.953 1.00 55.19  ? 295 LEU D CD1   1 
ATOM   13865 C CD2   . LEU D  1 295 ? 38.552  55.482  229.300 1.00 60.86  ? 295 LEU D CD2   1 
ATOM   13866 N N     . GLY D  1 296 ? 41.897  51.435  228.277 1.00 50.59  ? 296 GLY D N     1 
ATOM   13867 C CA    . GLY D  1 296 ? 42.271  50.069  227.967 1.00 52.52  ? 296 GLY D CA    1 
ATOM   13868 C C     . GLY D  1 296 ? 41.362  49.044  228.611 1.00 47.40  ? 296 GLY D C     1 
ATOM   13869 O O     . GLY D  1 296 ? 40.813  49.274  229.686 1.00 51.71  ? 296 GLY D O     1 
ATOM   13870 N N     . PHE D  1 297 ? 41.202  47.910  227.938 1.00 40.45  ? 297 PHE D N     1 
ATOM   13871 C CA    . PHE D  1 297 ? 40.429  46.791  228.458 1.00 50.50  ? 297 PHE D CA    1 
ATOM   13872 C C     . PHE D  1 297 ? 41.051  45.498  227.956 1.00 42.69  ? 297 PHE D C     1 
ATOM   13873 O O     . PHE D  1 297 ? 41.446  45.405  226.793 1.00 50.01  ? 297 PHE D O     1 
ATOM   13874 C CB    . PHE D  1 297 ? 38.957  46.885  228.033 1.00 47.84  ? 297 PHE D CB    1 
ATOM   13875 C CG    . PHE D  1 297 ? 38.128  45.676  228.412 1.00 49.83  ? 297 PHE D CG    1 
ATOM   13876 C CD1   . PHE D  1 297 ? 37.391  45.662  229.587 1.00 54.41  ? 297 PHE D CD1   1 
ATOM   13877 C CD2   . PHE D  1 297 ? 38.072  44.563  227.585 1.00 48.45  ? 297 PHE D CD2   1 
ATOM   13878 C CE1   . PHE D  1 297 ? 36.628  44.560  229.934 1.00 53.12  ? 297 PHE D CE1   1 
ATOM   13879 C CE2   . PHE D  1 297 ? 37.316  43.459  227.931 1.00 52.34  ? 297 PHE D CE2   1 
ATOM   13880 C CZ    . PHE D  1 297 ? 36.592  43.458  229.104 1.00 55.53  ? 297 PHE D CZ    1 
ATOM   13881 N N     . HIS D  1 298 ? 41.136  44.502  228.829 1.00 48.66  ? 298 HIS D N     1 
ATOM   13882 C CA    . HIS D  1 298 ? 41.679  43.208  228.442 1.00 50.92  ? 298 HIS D CA    1 
ATOM   13883 C C     . HIS D  1 298 ? 40.869  42.066  229.043 1.00 51.03  ? 298 HIS D C     1 
ATOM   13884 O O     . HIS D  1 298 ? 40.514  42.094  230.221 1.00 52.43  ? 298 HIS D O     1 
ATOM   13885 C CB    . HIS D  1 298 ? 43.145  43.090  228.863 1.00 53.26  ? 298 HIS D CB    1 
ATOM   13886 C CG    . HIS D  1 298 ? 43.694  41.704  228.733 1.00 51.52  ? 298 HIS D CG    1 
ATOM   13887 N ND1   . HIS D  1 298 ? 43.698  41.015  227.540 1.00 47.80  ? 298 HIS D ND1   1 
ATOM   13888 C CD2   . HIS D  1 298 ? 44.244  40.873  229.650 1.00 54.88  ? 298 HIS D CD2   1 
ATOM   13889 C CE1   . HIS D  1 298 ? 44.229  39.819  227.726 1.00 51.15  ? 298 HIS D CE1   1 
ATOM   13890 N NE2   . HIS D  1 298 ? 44.569  39.709  228.998 1.00 55.80  ? 298 HIS D NE2   1 
ATOM   13891 N N     . PHE D  1 299 ? 40.575  41.063  228.221 1.00 53.67  ? 299 PHE D N     1 
ATOM   13892 C CA    . PHE D  1 299 ? 39.882  39.867  228.688 1.00 57.73  ? 299 PHE D CA    1 
ATOM   13893 C C     . PHE D  1 299 ? 40.845  38.942  229.421 1.00 60.49  ? 299 PHE D C     1 
ATOM   13894 O O     . PHE D  1 299 ? 41.160  37.854  228.943 1.00 62.62  ? 299 PHE D O     1 
ATOM   13895 C CB    . PHE D  1 299 ? 39.232  39.124  227.520 1.00 57.23  ? 299 PHE D CB    1 
ATOM   13896 C CG    . PHE D  1 299 ? 38.069  39.849  226.912 1.00 64.66  ? 299 PHE D CG    1 
ATOM   13897 C CD1   . PHE D  1 299 ? 36.786  39.660  227.400 1.00 65.81  ? 299 PHE D CD1   1 
ATOM   13898 C CD2   . PHE D  1 299 ? 38.255  40.715  225.848 1.00 64.00  ? 299 PHE D CD2   1 
ATOM   13899 C CE1   . PHE D  1 299 ? 35.712  40.325  226.839 1.00 67.23  ? 299 PHE D CE1   1 
ATOM   13900 C CE2   . PHE D  1 299 ? 37.185  41.381  225.283 1.00 66.50  ? 299 PHE D CE2   1 
ATOM   13901 C CZ    . PHE D  1 299 ? 35.912  41.186  225.779 1.00 66.13  ? 299 PHE D CZ    1 
ATOM   13902 N N     . GLY D  1 300 ? 41.307  39.384  230.584 1.00 59.00  ? 300 GLY D N     1 
ATOM   13903 C CA    . GLY D  1 300 ? 42.262  38.627  231.370 1.00 61.97  ? 300 GLY D CA    1 
ATOM   13904 C C     . GLY D  1 300 ? 42.882  39.514  232.429 1.00 66.49  ? 300 GLY D C     1 
ATOM   13905 O O     . GLY D  1 300 ? 42.421  40.634  232.649 1.00 64.74  ? 300 GLY D O     1 
ATOM   13906 N N     . LEU D  1 301 ? 43.936  39.027  233.076 1.00 77.22  ? 301 LEU D N     1 
ATOM   13907 C CA    . LEU D  1 301 ? 44.557  39.772  234.166 1.00 79.32  ? 301 LEU D CA    1 
ATOM   13908 C C     . LEU D  1 301 ? 45.732  40.624  233.689 1.00 73.59  ? 301 LEU D C     1 
ATOM   13909 O O     . LEU D  1 301 ? 46.127  40.567  232.526 1.00 72.63  ? 301 LEU D O     1 
ATOM   13910 C CB    . LEU D  1 301 ? 45.015  38.820  235.272 1.00 78.98  ? 301 LEU D CB    1 
ATOM   13911 C CG    . LEU D  1 301 ? 43.950  37.878  235.844 1.00 74.50  ? 301 LEU D CG    1 
ATOM   13912 C CD1   . LEU D  1 301 ? 44.135  36.466  235.302 1.00 76.85  ? 301 LEU D CD1   1 
ATOM   13913 C CD2   . LEU D  1 301 ? 43.973  37.893  237.365 1.00 72.40  ? 301 LEU D CD2   1 
ATOM   13914 N N     . LYS D  1 302 ? 46.281  41.408  234.611 1.00 77.15  ? 302 LYS D N     1 
ATOM   13915 C CA    . LYS D  1 302 ? 47.333  42.378  234.314 1.00 82.55  ? 302 LYS D CA    1 
ATOM   13916 C C     . LYS D  1 302 ? 48.598  41.772  233.708 1.00 78.48  ? 302 LYS D C     1 
ATOM   13917 O O     . LYS D  1 302 ? 49.219  42.382  232.833 1.00 79.98  ? 302 LYS D O     1 
ATOM   13918 C CB    . LYS D  1 302 ? 47.693  43.145  235.587 1.00 85.70  ? 302 LYS D CB    1 
ATOM   13919 C CG    . LYS D  1 302 ? 49.119  43.666  235.644 1.00 91.83  ? 302 LYS D CG    1 
ATOM   13920 C CD    . LYS D  1 302 ? 49.215  44.819  236.622 1.00 98.50  ? 302 LYS D CD    1 
ATOM   13921 C CE    . LYS D  1 302 ? 48.404  44.535  237.878 1.00 95.71  ? 302 LYS D CE    1 
ATOM   13922 N NZ    . LYS D  1 302 ? 48.275  45.726  238.759 1.00 95.58  ? 302 LYS D NZ    1 
ATOM   13923 N N     . THR D  1 303 ? 48.974  40.583  234.171 1.00 78.83  ? 303 THR D N     1 
ATOM   13924 C CA    . THR D  1 303 ? 50.200  39.929  233.717 1.00 81.71  ? 303 THR D CA    1 
ATOM   13925 C C     . THR D  1 303 ? 50.303  39.867  232.195 1.00 76.97  ? 303 THR D C     1 
ATOM   13926 O O     . THR D  1 303 ? 51.283  40.336  231.615 1.00 75.55  ? 303 THR D O     1 
ATOM   13927 C CB    . THR D  1 303 ? 50.315  38.499  234.272 1.00 81.47  ? 303 THR D CB    1 
ATOM   13928 O OG1   . THR D  1 303 ? 50.283  38.532  235.705 1.00 94.47  ? 303 THR D OG1   1 
ATOM   13929 C CG2   . THR D  1 303 ? 51.621  37.866  233.812 1.00 71.17  ? 303 THR D CG2   1 
ATOM   13930 N N     . VAL D  1 304 ? 49.287  39.294  231.556 1.00 73.14  ? 304 VAL D N     1 
ATOM   13931 C CA    . VAL D  1 304 ? 49.227  39.245  230.098 1.00 70.78  ? 304 VAL D CA    1 
ATOM   13932 C C     . VAL D  1 304 ? 49.006  40.648  229.531 1.00 71.02  ? 304 VAL D C     1 
ATOM   13933 O O     . VAL D  1 304 ? 49.420  40.949  228.412 1.00 67.64  ? 304 VAL D O     1 
ATOM   13934 C CB    . VAL D  1 304 ? 48.104  38.299  229.606 1.00 69.95  ? 304 VAL D CB    1 
ATOM   13935 C CG1   . VAL D  1 304 ? 48.146  38.149  228.089 1.00 68.70  ? 304 VAL D CG1   1 
ATOM   13936 C CG2   . VAL D  1 304 ? 48.225  36.939  230.276 1.00 67.65  ? 304 VAL D CG2   1 
ATOM   13937 N N     . ALA D  1 305 ? 48.364  41.507  230.318 1.00 69.69  ? 305 ALA D N     1 
ATOM   13938 C CA    . ALA D  1 305 ? 48.056  42.863  229.874 1.00 66.12  ? 305 ALA D CA    1 
ATOM   13939 C C     . ALA D  1 305 ? 49.294  43.757  229.852 1.00 65.36  ? 305 ALA D C     1 
ATOM   13940 O O     . ALA D  1 305 ? 49.552  44.436  228.859 1.00 61.90  ? 305 ALA D O     1 
ATOM   13941 C CB    . ALA D  1 305 ? 46.981  43.478  230.756 1.00 62.20  ? 305 ALA D CB    1 
ATOM   13942 N N     . LYS D  1 306 ? 50.052  43.762  230.946 1.00 72.05  ? 306 LYS D N     1 
ATOM   13943 C CA    . LYS D  1 306 ? 51.245  44.604  231.040 1.00 71.20  ? 306 LYS D CA    1 
ATOM   13944 C C     . LYS D  1 306 ? 52.300  44.178  230.033 1.00 63.51  ? 306 LYS D C     1 
ATOM   13945 O O     . LYS D  1 306 ? 52.874  45.013  229.331 1.00 63.72  ? 306 LYS D O     1 
ATOM   13946 C CB    . LYS D  1 306 ? 51.826  44.573  232.455 1.00 73.14  ? 306 LYS D CB    1 
ATOM   13947 C CG    . LYS D  1 306 ? 53.022  45.496  232.643 1.00 80.32  ? 306 LYS D CG    1 
ATOM   13948 C CD    . LYS D  1 306 ? 53.583  45.415  234.052 1.00 85.62  ? 306 LYS D CD    1 
ATOM   13949 C CE    . LYS D  1 306 ? 54.814  46.295  234.208 1.00 85.58  ? 306 LYS D CE    1 
ATOM   13950 N NZ    . LYS D  1 306 ? 55.983  45.770  233.450 1.00 76.70  ? 306 LYS D NZ    1 
ATOM   13951 N N     . SER D  1 307 ? 52.544  42.872  229.976 1.00 63.56  ? 307 SER D N     1 
ATOM   13952 C CA    . SER D  1 307 ? 53.448  42.273  229.002 1.00 63.76  ? 307 SER D CA    1 
ATOM   13953 C C     . SER D  1 307 ? 53.180  42.758  227.582 1.00 60.49  ? 307 SER D C     1 
ATOM   13954 O O     . SER D  1 307 ? 54.108  43.056  226.829 1.00 56.76  ? 307 SER D O     1 
ATOM   13955 C CB    . SER D  1 307 ? 53.330  40.750  229.053 1.00 65.06  ? 307 SER D CB    1 
ATOM   13956 O OG    . SER D  1 307 ? 53.885  40.160  227.889 1.00 62.61  ? 307 SER D OG    1 
ATOM   13957 N N     . THR D  1 308 ? 51.902  42.840  227.232 1.00 60.38  ? 308 THR D N     1 
ATOM   13958 C CA    . THR D  1 308 ? 51.489  43.214  225.887 1.00 55.46  ? 308 THR D CA    1 
ATOM   13959 C C     . THR D  1 308 ? 51.718  44.696  225.601 1.00 51.03  ? 308 THR D C     1 
ATOM   13960 O O     . THR D  1 308 ? 52.221  45.055  224.539 1.00 51.28  ? 308 THR D O     1 
ATOM   13961 C CB    . THR D  1 308 ? 50.003  42.884  225.652 1.00 55.20  ? 308 THR D CB    1 
ATOM   13962 O OG1   . THR D  1 308 ? 49.778  41.491  225.900 1.00 52.78  ? 308 THR D OG1   1 
ATOM   13963 C CG2   . THR D  1 308 ? 49.602  43.213  224.222 1.00 49.13  ? 308 THR D CG2   1 
ATOM   13964 N N     . PHE D  1 309 ? 51.356  45.555  226.549 1.00 51.81  ? 309 PHE D N     1 
ATOM   13965 C CA    . PHE D  1 309 ? 51.464  46.995  226.333 1.00 52.79  ? 309 PHE D CA    1 
ATOM   13966 C C     . PHE D  1 309 ? 52.869  47.530  226.608 1.00 53.61  ? 309 PHE D C     1 
ATOM   13967 O O     . PHE D  1 309 ? 53.245  48.582  226.093 1.00 47.28  ? 309 PHE D O     1 
ATOM   13968 C CB    . PHE D  1 309 ? 50.444  47.745  227.186 1.00 49.34  ? 309 PHE D CB    1 
ATOM   13969 C CG    . PHE D  1 309 ? 49.047  47.694  226.632 1.00 61.40  ? 309 PHE D CG    1 
ATOM   13970 C CD1   . PHE D  1 309 ? 48.695  48.462  225.533 1.00 58.06  ? 309 PHE D CD1   1 
ATOM   13971 C CD2   . PHE D  1 309 ? 48.086  46.879  227.209 1.00 57.59  ? 309 PHE D CD2   1 
ATOM   13972 C CE1   . PHE D  1 309 ? 47.411  48.419  225.021 1.00 57.71  ? 309 PHE D CE1   1 
ATOM   13973 C CE2   . PHE D  1 309 ? 46.802  46.832  226.702 1.00 57.33  ? 309 PHE D CE2   1 
ATOM   13974 C CZ    . PHE D  1 309 ? 46.464  47.603  225.606 1.00 53.66  ? 309 PHE D CZ    1 
ATOM   13975 N N     . ASP D  1 310 ? 53.640  46.816  227.422 1.00 55.44  ? 310 ASP D N     1 
ATOM   13976 C CA    . ASP D  1 310 ? 55.057  47.133  227.571 1.00 58.24  ? 310 ASP D CA    1 
ATOM   13977 C C     . ASP D  1 310 ? 55.739  46.976  226.217 1.00 47.44  ? 310 ASP D C     1 
ATOM   13978 O O     . ASP D  1 310 ? 56.509  47.834  225.789 1.00 50.64  ? 310 ASP D O     1 
ATOM   13979 C CB    . ASP D  1 310 ? 55.728  46.227  228.609 1.00 57.34  ? 310 ASP D CB    1 
ATOM   13980 C CG    . ASP D  1 310 ? 55.472  46.673  230.036 1.00 61.08  ? 310 ASP D CG    1 
ATOM   13981 O OD1   . ASP D  1 310 ? 55.112  47.850  230.244 1.00 57.38  ? 310 ASP D OD1   1 
ATOM   13982 O OD2   . ASP D  1 310 ? 55.651  45.842  230.952 1.00 65.07  ? 310 ASP D OD2   1 
ATOM   13983 N N     . LEU D  1 311 ? 55.436  45.867  225.551 1.00 49.98  ? 311 LEU D N     1 
ATOM   13984 C CA    . LEU D  1 311 ? 55.989  45.570  224.236 1.00 44.40  ? 311 LEU D CA    1 
ATOM   13985 C C     . LEU D  1 311 ? 55.459  46.495  223.143 1.00 47.34  ? 311 LEU D C     1 
ATOM   13986 O O     . LEU D  1 311 ? 56.230  47.124  222.420 1.00 41.98  ? 311 LEU D O     1 
ATOM   13987 C CB    . LEU D  1 311 ? 55.693  44.119  223.851 1.00 46.78  ? 311 LEU D CB    1 
ATOM   13988 C CG    . LEU D  1 311 ? 56.589  43.015  224.416 1.00 47.46  ? 311 LEU D CG    1 
ATOM   13989 C CD1   . LEU D  1 311 ? 56.143  41.662  223.891 1.00 41.20  ? 311 LEU D CD1   1 
ATOM   13990 C CD2   . LEU D  1 311 ? 58.039  43.275  224.057 1.00 50.36  ? 311 LEU D CD2   1 
ATOM   13991 N N     . LEU D  1 312 ? 54.136  46.568  223.031 1.00 45.57  ? 312 LEU D N     1 
ATOM   13992 C CA    . LEU D  1 312 ? 53.488  47.220  221.896 1.00 42.83  ? 312 LEU D CA    1 
ATOM   13993 C C     . LEU D  1 312 ? 53.394  48.737  222.007 1.00 42.70  ? 312 LEU D C     1 
ATOM   13994 O O     . LEU D  1 312 ? 53.465  49.435  220.998 1.00 40.99  ? 312 LEU D O     1 
ATOM   13995 C CB    . LEU D  1 312 ? 52.084  46.648  221.696 1.00 45.75  ? 312 LEU D CB    1 
ATOM   13996 C CG    . LEU D  1 312 ? 52.020  45.206  221.190 1.00 51.46  ? 312 LEU D CG    1 
ATOM   13997 C CD1   . LEU D  1 312 ? 50.578  44.767  220.984 1.00 46.23  ? 312 LEU D CD1   1 
ATOM   13998 C CD2   . LEU D  1 312 ? 52.818  45.059  219.906 1.00 53.59  ? 312 LEU D CD2   1 
ATOM   13999 N N     . PHE D  1 313 ? 53.216  49.245  223.221 1.00 38.99  ? 313 PHE D N     1 
ATOM   14000 C CA    . PHE D  1 313 ? 53.046  50.682  223.415 1.00 43.91  ? 313 PHE D CA    1 
ATOM   14001 C C     . PHE D  1 313 ? 53.735  51.182  224.683 1.00 47.59  ? 313 PHE D C     1 
ATOM   14002 O O     . PHE D  1 313 ? 53.071  51.688  225.584 1.00 45.39  ? 313 PHE D O     1 
ATOM   14003 C CB    . PHE D  1 313 ? 51.556  51.031  223.475 1.00 48.01  ? 313 PHE D CB    1 
ATOM   14004 C CG    . PHE D  1 313 ? 51.213  52.355  222.849 1.00 48.57  ? 313 PHE D CG    1 
ATOM   14005 C CD1   . PHE D  1 313 ? 52.192  53.303  222.604 1.00 50.26  ? 313 PHE D CD1   1 
ATOM   14006 C CD2   . PHE D  1 313 ? 49.904  52.646  222.502 1.00 47.10  ? 313 PHE D CD2   1 
ATOM   14007 C CE1   . PHE D  1 313 ? 51.870  54.519  222.023 1.00 46.37  ? 313 PHE D CE1   1 
ATOM   14008 C CE2   . PHE D  1 313 ? 49.575  53.857  221.923 1.00 46.45  ? 313 PHE D CE2   1 
ATOM   14009 C CZ    . PHE D  1 313 ? 50.561  54.795  221.683 1.00 49.95  ? 313 PHE D CZ    1 
ATOM   14010 N N     . PRO D  1 314 ? 55.069  51.051  224.759 1.00 53.84  ? 314 PRO D N     1 
ATOM   14011 C CA    . PRO D  1 314 ? 55.767  51.510  225.963 1.00 48.30  ? 314 PRO D CA    1 
ATOM   14012 C C     . PRO D  1 314 ? 55.699  53.020  226.149 1.00 40.43  ? 314 PRO D C     1 
ATOM   14013 O O     . PRO D  1 314 ? 55.855  53.501  227.272 1.00 44.82  ? 314 PRO D O     1 
ATOM   14014 C CB    . PRO D  1 314 ? 57.209  51.065  225.718 1.00 51.14  ? 314 PRO D CB    1 
ATOM   14015 C CG    . PRO D  1 314 ? 57.327  51.025  224.240 1.00 47.61  ? 314 PRO D CG    1 
ATOM   14016 C CD    . PRO D  1 314 ? 56.007  50.506  223.764 1.00 49.18  ? 314 PRO D CD    1 
ATOM   14017 N N     . GLU D  1 315 ? 55.472  53.750  225.060 1.00 41.61  ? 315 GLU D N     1 
ATOM   14018 C CA    . GLU D  1 315 ? 55.402  55.210  225.102 1.00 40.60  ? 315 GLU D CA    1 
ATOM   14019 C C     . GLU D  1 315 ? 54.282  55.730  226.002 1.00 52.85  ? 315 GLU D C     1 
ATOM   14020 O O     . GLU D  1 315 ? 54.301  56.890  226.412 1.00 56.84  ? 315 GLU D O     1 
ATOM   14021 C CB    . GLU D  1 315 ? 55.213  55.781  223.693 1.00 38.60  ? 315 GLU D CB    1 
ATOM   14022 C CG    . GLU D  1 315 ? 56.392  55.576  222.757 1.00 47.15  ? 315 GLU D CG    1 
ATOM   14023 C CD    . GLU D  1 315 ? 56.267  54.320  221.914 1.00 49.20  ? 315 GLU D CD    1 
ATOM   14024 O OE1   . GLU D  1 315 ? 55.645  53.340  222.379 1.00 46.34  ? 315 GLU D OE1   1 
ATOM   14025 O OE2   . GLU D  1 315 ? 56.790  54.315  220.780 1.00 48.60  ? 315 GLU D OE2   1 
ATOM   14026 N N     . LEU D  1 316 ? 53.304  54.880  226.302 1.00 52.69  ? 316 LEU D N     1 
ATOM   14027 C CA    . LEU D  1 316 ? 52.198  55.272  227.169 1.00 59.48  ? 316 LEU D CA    1 
ATOM   14028 C C     . LEU D  1 316 ? 52.659  55.506  228.601 1.00 62.79  ? 316 LEU D C     1 
ATOM   14029 O O     . LEU D  1 316 ? 51.956  56.139  229.386 1.00 64.36  ? 316 LEU D O     1 
ATOM   14030 C CB    . LEU D  1 316 ? 51.091  54.216  227.151 1.00 53.90  ? 316 LEU D CB    1 
ATOM   14031 C CG    . LEU D  1 316 ? 50.221  54.129  225.896 1.00 53.07  ? 316 LEU D CG    1 
ATOM   14032 C CD1   . LEU D  1 316 ? 49.054  53.185  226.134 1.00 53.58  ? 316 LEU D CD1   1 
ATOM   14033 C CD2   . LEU D  1 316 ? 49.726  55.504  225.482 1.00 52.48  ? 316 LEU D CD2   1 
ATOM   14034 N N     . GLY D  1 317 ? 53.835  54.987  228.940 1.00 63.76  ? 317 GLY D N     1 
ATOM   14035 C CA    . GLY D  1 317 ? 54.368  55.128  230.281 1.00 65.31  ? 317 GLY D CA    1 
ATOM   14036 C C     . GLY D  1 317 ? 53.443  54.523  231.318 1.00 70.33  ? 317 GLY D C     1 
ATOM   14037 O O     . GLY D  1 317 ? 53.333  55.025  232.438 1.00 73.91  ? 317 GLY D O     1 
ATOM   14038 N N     . LEU D  1 318 ? 52.764  53.445  230.936 1.00 71.40  ? 318 LEU D N     1 
ATOM   14039 C CA    . LEU D  1 318 ? 51.864  52.745  231.843 1.00 78.37  ? 318 LEU D CA    1 
ATOM   14040 C C     . LEU D  1 318 ? 52.631  52.103  232.989 1.00 85.36  ? 318 LEU D C     1 
ATOM   14041 O O     . LEU D  1 318 ? 53.633  51.424  232.773 1.00 84.99  ? 318 LEU D O     1 
ATOM   14042 C CB    . LEU D  1 318 ? 51.064  51.676  231.092 1.00 76.25  ? 318 LEU D CB    1 
ATOM   14043 C CG    . LEU D  1 318 ? 49.932  52.163  230.181 1.00 74.41  ? 318 LEU D CG    1 
ATOM   14044 C CD1   . LEU D  1 318 ? 49.316  51.006  229.400 1.00 67.44  ? 318 LEU D CD1   1 
ATOM   14045 C CD2   . LEU D  1 318 ? 48.875  52.894  230.994 1.00 70.84  ? 318 LEU D CD2   1 
ATOM   14046 N N     . VAL D  1 319 ? 52.152  52.322  234.207 1.00 87.03  ? 319 VAL D N     1 
ATOM   14047 C CA    . VAL D  1 319 ? 52.728  51.678  235.378 1.00 85.41  ? 319 VAL D CA    1 
ATOM   14048 C C     . VAL D  1 319 ? 51.847  50.499  235.780 1.00 90.74  ? 319 VAL D C     1 
ATOM   14049 O O     . VAL D  1 319 ? 50.792  50.283  235.182 1.00 92.42  ? 319 VAL D O     1 
ATOM   14050 C CB    . VAL D  1 319 ? 52.870  52.660  236.558 1.00 88.37  ? 319 VAL D CB    1 
ATOM   14051 C CG1   . VAL D  1 319 ? 53.713  53.856  236.149 1.00 79.56  ? 319 VAL D CG1   1 
ATOM   14052 C CG2   . VAL D  1 319 ? 51.503  53.120  237.032 1.00 91.34  ? 319 VAL D CG2   1 
ATOM   14053 N N     . GLU D  1 320 ? 52.280  49.732  236.776 1.00 89.66  ? 320 GLU D N     1 
ATOM   14054 C CA    . GLU D  1 320 ? 51.477  48.619  237.278 1.00 92.58  ? 320 GLU D CA    1 
ATOM   14055 C C     . GLU D  1 320 ? 50.304  49.139  238.108 1.00 91.21  ? 320 GLU D C     1 
ATOM   14056 O O     . GLU D  1 320 ? 49.263  48.493  238.205 1.00 91.31  ? 320 GLU D O     1 
ATOM   14057 C CB    . GLU D  1 320 ? 52.339  47.652  238.105 1.00 90.55  ? 320 GLU D CB    1 
ATOM   14058 C CG    . GLU D  1 320 ? 51.556  46.510  238.753 1.00 99.13  ? 320 GLU D CG    1 
ATOM   14059 C CD    . GLU D  1 320 ? 52.414  45.297  239.075 1.00 105.88 ? 320 GLU D CD    1 
ATOM   14060 O OE1   . GLU D  1 320 ? 53.370  45.431  239.868 1.00 114.93 ? 320 GLU D OE1   1 
ATOM   14061 O OE2   . GLU D  1 320 ? 52.128  44.208  238.532 1.00 106.24 ? 320 GLU D OE2   1 
ATOM   14062 N N     . GLU D  1 321 ? 50.476  50.318  238.698 1.00 92.20  ? 321 GLU D N     1 
ATOM   14063 C CA    . GLU D  1 321 ? 49.422  50.928  239.503 1.00 93.83  ? 321 GLU D CA    1 
ATOM   14064 C C     . GLU D  1 321 ? 48.192  51.256  238.661 1.00 92.29  ? 321 GLU D C     1 
ATOM   14065 O O     . GLU D  1 321 ? 47.066  51.219  239.157 1.00 89.49  ? 321 GLU D O     1 
ATOM   14066 C CB    . GLU D  1 321 ? 49.936  52.193  240.189 1.00 94.57  ? 321 GLU D CB    1 
ATOM   14067 C CG    . GLU D  1 321 ? 51.220  51.996  240.973 1.00 97.02  ? 321 GLU D CG    1 
ATOM   14068 C CD    . GLU D  1 321 ? 51.977  53.291  241.170 1.00 95.21  ? 321 GLU D CD    1 
ATOM   14069 O OE1   . GLU D  1 321 ? 51.326  54.328  241.422 1.00 97.85  ? 321 GLU D OE1   1 
ATOM   14070 O OE2   . GLU D  1 321 ? 53.221  53.275  241.062 1.00 96.65  ? 321 GLU D OE2   1 
ATOM   14071 N N     . ASP D  1 322 ? 48.406  51.572  237.388 1.00 90.93  ? 322 ASP D N     1 
ATOM   14072 C CA    . ASP D  1 322 ? 47.310  51.986  236.519 1.00 87.46  ? 322 ASP D CA    1 
ATOM   14073 C C     . ASP D  1 322 ? 46.409  50.821  236.136 1.00 86.41  ? 322 ASP D C     1 
ATOM   14074 O O     . ASP D  1 322 ? 45.228  51.007  235.851 1.00 84.08  ? 322 ASP D O     1 
ATOM   14075 C CB    . ASP D  1 322 ? 47.855  52.656  235.260 1.00 85.66  ? 322 ASP D CB    1 
ATOM   14076 C CG    . ASP D  1 322 ? 48.470  54.005  235.547 1.00 85.65  ? 322 ASP D CG    1 
ATOM   14077 O OD1   . ASP D  1 322 ? 48.037  54.652  236.523 1.00 90.08  ? 322 ASP D OD1   1 
ATOM   14078 O OD2   . ASP D  1 322 ? 49.382  54.419  234.800 1.00 85.88  ? 322 ASP D OD2   1 
ATOM   14079 N N     . TYR D  1 323 ? 46.968  49.618  236.147 1.00 83.22  ? 323 TYR D N     1 
ATOM   14080 C CA    . TYR D  1 323 ? 46.227  48.432  235.742 1.00 82.05  ? 323 TYR D CA    1 
ATOM   14081 C C     . TYR D  1 323 ? 45.306  47.970  236.858 1.00 81.72  ? 323 TYR D C     1 
ATOM   14082 O O     . TYR D  1 323 ? 45.767  47.510  237.903 1.00 83.58  ? 323 TYR D O     1 
ATOM   14083 C CB    . TYR D  1 323 ? 47.182  47.307  235.355 1.00 82.14  ? 323 TYR D CB    1 
ATOM   14084 C CG    . TYR D  1 323 ? 47.956  47.532  234.075 1.00 85.20  ? 323 TYR D CG    1 
ATOM   14085 C CD1   . TYR D  1 323 ? 48.173  46.489  233.192 1.00 83.21  ? 323 TYR D CD1   1 
ATOM   14086 C CD2   . TYR D  1 323 ? 48.469  48.782  233.747 1.00 87.85  ? 323 TYR D CD2   1 
ATOM   14087 C CE1   . TYR D  1 323 ? 48.875  46.680  232.024 1.00 81.83  ? 323 TYR D CE1   1 
ATOM   14088 C CE2   . TYR D  1 323 ? 49.178  48.982  232.578 1.00 85.05  ? 323 TYR D CE2   1 
ATOM   14089 C CZ    . TYR D  1 323 ? 49.380  47.925  231.719 1.00 81.83  ? 323 TYR D CZ    1 
ATOM   14090 O OH    . TYR D  1 323 ? 50.085  48.109  230.551 1.00 74.31  ? 323 TYR D OH    1 
ATOM   14091 N N     . LEU D  1 324 ? 44.004  48.088  236.634 1.00 79.96  ? 324 LEU D N     1 
ATOM   14092 C CA    . LEU D  1 324 ? 43.022  47.716  237.643 1.00 73.00  ? 324 LEU D CA    1 
ATOM   14093 C C     . LEU D  1 324 ? 42.325  46.418  237.262 1.00 68.63  ? 324 LEU D C     1 
ATOM   14094 O O     . LEU D  1 324 ? 41.808  46.285  236.153 1.00 71.64  ? 324 LEU D O     1 
ATOM   14095 C CB    . LEU D  1 324 ? 42.004  48.839  237.823 1.00 71.23  ? 324 LEU D CB    1 
ATOM   14096 C CG    . LEU D  1 324 ? 42.635  50.221  238.016 1.00 72.64  ? 324 LEU D CG    1 
ATOM   14097 C CD1   . LEU D  1 324 ? 41.639  51.322  237.706 1.00 72.35  ? 324 LEU D CD1   1 
ATOM   14098 C CD2   . LEU D  1 324 ? 43.182  50.372  239.428 1.00 80.53  ? 324 LEU D CD2   1 
ATOM   14099 N N     . GLU D  1 325 ? 42.332  45.455  238.176 1.00 68.79  ? 325 GLU D N     1 
ATOM   14100 C CA    . GLU D  1 325 ? 41.633  44.196  237.957 1.00 73.24  ? 325 GLU D CA    1 
ATOM   14101 C C     . GLU D  1 325 ? 40.275  44.231  238.643 1.00 75.96  ? 325 GLU D C     1 
ATOM   14102 O O     . GLU D  1 325 ? 40.148  44.722  239.766 1.00 80.23  ? 325 GLU D O     1 
ATOM   14103 C CB    . GLU D  1 325 ? 42.454  43.015  238.474 1.00 76.22  ? 325 GLU D CB    1 
ATOM   14104 C CG    . GLU D  1 325 ? 43.809  42.850  237.804 1.00 83.06  ? 325 GLU D CG    1 
ATOM   14105 C CD    . GLU D  1 325 ? 44.536  41.605  238.276 1.00 87.76  ? 325 GLU D CD    1 
ATOM   14106 O OE1   . GLU D  1 325 ? 43.962  40.861  239.099 1.00 91.35  ? 325 GLU D OE1   1 
ATOM   14107 O OE2   . GLU D  1 325 ? 45.674  41.368  237.821 1.00 96.22  ? 325 GLU D OE2   1 
ATOM   14108 N N     . MET D  1 326 ? 39.263  43.711  237.958 1.00 79.07  ? 326 MET D N     1 
ATOM   14109 C CA    . MET D  1 326 ? 37.905  43.673  238.484 1.00 73.87  ? 326 MET D CA    1 
ATOM   14110 C C     . MET D  1 326 ? 37.039  42.753  237.635 1.00 73.11  ? 326 MET D C     1 
ATOM   14111 O O     . MET D  1 326 ? 37.477  42.263  236.596 1.00 72.36  ? 326 MET D O     1 
ATOM   14112 C CB    . MET D  1 326 ? 37.306  45.082  238.532 1.00 68.95  ? 326 MET D CB    1 
ATOM   14113 C CG    . MET D  1 326 ? 37.570  45.914  237.285 1.00 68.34  ? 326 MET D CG    1 
ATOM   14114 S SD    . MET D  1 326 ? 37.012  47.626  237.452 1.00 65.75  ? 326 MET D SD    1 
ATOM   14115 C CE    . MET D  1 326 ? 38.261  48.327  238.530 1.00 69.51  ? 326 MET D CE    1 
ATOM   14116 N N     . SER D  1 327 ? 35.811  42.515  238.085 1.00 76.46  ? 327 SER D N     1 
ATOM   14117 C CA    . SER D  1 327 ? 34.871  41.708  237.321 1.00 73.52  ? 327 SER D CA    1 
ATOM   14118 C C     . SER D  1 327 ? 34.403  42.491  236.101 1.00 70.31  ? 327 SER D C     1 
ATOM   14119 O O     . SER D  1 327 ? 34.654  43.693  235.997 1.00 68.74  ? 327 SER D O     1 
ATOM   14120 C CB    . SER D  1 327 ? 33.674  41.297  238.183 1.00 75.42  ? 327 SER D CB    1 
ATOM   14121 O OG    . SER D  1 327 ? 32.833  42.404  238.452 1.00 81.13  ? 327 SER D OG    1 
ATOM   14122 N N     . TRP D  1 328 ? 33.727  41.808  235.180 1.00 70.30  ? 328 TRP D N     1 
ATOM   14123 C CA    . TRP D  1 328 ? 33.238  42.444  233.962 1.00 67.01  ? 328 TRP D CA    1 
ATOM   14124 C C     . TRP D  1 328 ? 32.342  43.635  234.271 1.00 65.01  ? 328 TRP D C     1 
ATOM   14125 O O     . TRP D  1 328 ? 32.465  44.692  233.652 1.00 61.76  ? 328 TRP D O     1 
ATOM   14126 C CB    . TRP D  1 328 ? 32.474  41.441  233.095 1.00 67.34  ? 328 TRP D CB    1 
ATOM   14127 C CG    . TRP D  1 328 ? 31.735  42.094  231.969 1.00 69.00  ? 328 TRP D CG    1 
ATOM   14128 C CD1   . TRP D  1 328 ? 32.253  42.494  230.772 1.00 68.14  ? 328 TRP D CD1   1 
ATOM   14129 C CD2   . TRP D  1 328 ? 30.342  42.431  231.937 1.00 69.39  ? 328 TRP D CD2   1 
ATOM   14130 N NE1   . TRP D  1 328 ? 31.269  43.056  229.995 1.00 68.18  ? 328 TRP D NE1   1 
ATOM   14131 C CE2   . TRP D  1 328 ? 30.087  43.030  230.687 1.00 67.20  ? 328 TRP D CE2   1 
ATOM   14132 C CE3   . TRP D  1 328 ? 29.287  42.284  232.843 1.00 69.90  ? 328 TRP D CE3   1 
ATOM   14133 C CZ2   . TRP D  1 328 ? 28.822  43.481  230.320 1.00 62.29  ? 328 TRP D CZ2   1 
ATOM   14134 C CZ3   . TRP D  1 328 ? 28.031  42.732  232.477 1.00 65.85  ? 328 TRP D CZ3   1 
ATOM   14135 C CH2   . TRP D  1 328 ? 27.809  43.323  231.226 1.00 64.59  ? 328 TRP D CH2   1 
ATOM   14136 N N     . GLY D  1 329 ? 31.447  43.458  235.238 1.00 67.17  ? 329 GLY D N     1 
ATOM   14137 C CA    . GLY D  1 329 ? 30.502  44.495  235.608 1.00 64.65  ? 329 GLY D CA    1 
ATOM   14138 C C     . GLY D  1 329 ? 31.158  45.755  236.139 1.00 65.34  ? 329 GLY D C     1 
ATOM   14139 O O     . GLY D  1 329 ? 30.808  46.865  235.735 1.00 66.50  ? 329 GLY D O     1 
ATOM   14140 N N     . GLU D  1 330 ? 32.114  45.581  237.046 1.00 71.26  ? 330 GLU D N     1 
ATOM   14141 C CA    . GLU D  1 330 ? 32.799  46.709  237.665 1.00 68.98  ? 330 GLU D CA    1 
ATOM   14142 C C     . GLU D  1 330 ? 33.564  47.529  236.634 1.00 64.50  ? 330 GLU D C     1 
ATOM   14143 O O     . GLU D  1 330 ? 33.621  48.756  236.722 1.00 60.60  ? 330 GLU D O     1 
ATOM   14144 C CB    . GLU D  1 330 ? 33.752  46.222  238.756 1.00 75.62  ? 330 GLU D CB    1 
ATOM   14145 C CG    . GLU D  1 330 ? 33.093  45.310  239.775 1.00 73.65  ? 330 GLU D CG    1 
ATOM   14146 C CD    . GLU D  1 330 ? 33.836  45.285  241.094 1.00 89.07  ? 330 GLU D CD    1 
ATOM   14147 O OE1   . GLU D  1 330 ? 34.589  46.243  241.371 1.00 82.56  ? 330 GLU D OE1   1 
ATOM   14148 O OE2   . GLU D  1 330 ? 33.670  44.308  241.854 1.00 88.91  ? 330 GLU D OE2   1 
ATOM   14149 N N     . SER D  1 331 ? 34.139  46.840  235.653 1.00 63.70  ? 331 SER D N     1 
ATOM   14150 C CA    . SER D  1 331 ? 34.911  47.492  234.602 1.00 64.32  ? 331 SER D CA    1 
ATOM   14151 C C     . SER D  1 331 ? 34.040  48.407  233.743 1.00 64.66  ? 331 SER D C     1 
ATOM   14152 O O     . SER D  1 331 ? 34.394  49.562  233.511 1.00 66.08  ? 331 SER D O     1 
ATOM   14153 C CB    . SER D  1 331 ? 35.606  46.450  233.727 1.00 62.68  ? 331 SER D CB    1 
ATOM   14154 O OG    . SER D  1 331 ? 34.671  45.540  233.176 1.00 64.33  ? 331 SER D OG    1 
ATOM   14155 N N     . PHE D  1 332 ? 32.903  47.895  233.278 1.00 65.66  ? 332 PHE D N     1 
ATOM   14156 C CA    . PHE D  1 332 ? 31.978  48.708  232.493 1.00 62.98  ? 332 PHE D CA    1 
ATOM   14157 C C     . PHE D  1 332 ? 31.390  49.835  233.329 1.00 63.47  ? 332 PHE D C     1 
ATOM   14158 O O     . PHE D  1 332 ? 31.123  50.922  232.819 1.00 63.98  ? 332 PHE D O     1 
ATOM   14159 C CB    . PHE D  1 332 ? 30.859  47.852  231.902 1.00 63.35  ? 332 PHE D CB    1 
ATOM   14160 C CG    . PHE D  1 332 ? 31.204  47.251  230.574 1.00 64.99  ? 332 PHE D CG    1 
ATOM   14161 C CD1   . PHE D  1 332 ? 32.525  47.152  230.175 1.00 62.30  ? 332 PHE D CD1   1 
ATOM   14162 C CD2   . PHE D  1 332 ? 30.213  46.806  229.715 1.00 68.16  ? 332 PHE D CD2   1 
ATOM   14163 C CE1   . PHE D  1 332 ? 32.856  46.608  228.954 1.00 65.09  ? 332 PHE D CE1   1 
ATOM   14164 C CE2   . PHE D  1 332 ? 30.539  46.260  228.488 1.00 67.82  ? 332 PHE D CE2   1 
ATOM   14165 C CZ    . PHE D  1 332 ? 31.863  46.162  228.109 1.00 67.23  ? 332 PHE D CZ    1 
ATOM   14166 N N     . ALA D  1 333 ? 31.188  49.569  234.614 1.00 66.36  ? 333 ALA D N     1 
ATOM   14167 C CA    . ALA D  1 333 ? 30.807  50.619  235.542 1.00 62.80  ? 333 ALA D CA    1 
ATOM   14168 C C     . ALA D  1 333 ? 31.926  51.654  235.607 1.00 66.97  ? 333 ALA D C     1 
ATOM   14169 O O     . ALA D  1 333 ? 31.684  52.852  235.479 1.00 70.20  ? 333 ALA D O     1 
ATOM   14170 C CB    . ALA D  1 333 ? 30.515  50.046  236.919 1.00 63.37  ? 333 ALA D CB    1 
ATOM   14171 N N     . TYR D  1 334 ? 33.155  51.178  235.780 1.00 68.45  ? 334 TYR D N     1 
ATOM   14172 C CA    . TYR D  1 334 ? 34.318  52.057  235.838 1.00 69.67  ? 334 TYR D CA    1 
ATOM   14173 C C     . TYR D  1 334 ? 34.534  52.811  234.526 1.00 70.95  ? 334 TYR D C     1 
ATOM   14174 O O     . TYR D  1 334 ? 34.727  54.027  234.528 1.00 70.16  ? 334 TYR D O     1 
ATOM   14175 C CB    . TYR D  1 334 ? 35.573  51.258  236.197 1.00 74.56  ? 334 TYR D CB    1 
ATOM   14176 C CG    . TYR D  1 334 ? 36.849  52.063  236.115 1.00 80.40  ? 334 TYR D CG    1 
ATOM   14177 C CD1   . TYR D  1 334 ? 36.946  53.310  236.714 1.00 86.10  ? 334 TYR D CD1   1 
ATOM   14178 C CD2   . TYR D  1 334 ? 37.961  51.569  235.451 1.00 81.85  ? 334 TYR D CD2   1 
ATOM   14179 C CE1   . TYR D  1 334 ? 38.111  54.049  236.643 1.00 88.65  ? 334 TYR D CE1   1 
ATOM   14180 C CE2   . TYR D  1 334 ? 39.133  52.297  235.375 1.00 82.62  ? 334 TYR D CE2   1 
ATOM   14181 C CZ    . TYR D  1 334 ? 39.202  53.537  235.974 1.00 86.24  ? 334 TYR D CZ    1 
ATOM   14182 O OH    . TYR D  1 334 ? 40.366  54.267  235.903 1.00 87.31  ? 334 TYR D OH    1 
ATOM   14183 N N     . LEU D  1 335 ? 34.502  52.083  233.414 1.00 69.07  ? 335 LEU D N     1 
ATOM   14184 C CA    . LEU D  1 335 ? 34.689  52.680  232.094 1.00 70.69  ? 335 LEU D CA    1 
ATOM   14185 C C     . LEU D  1 335 ? 33.633  53.742  231.793 1.00 72.09  ? 335 LEU D C     1 
ATOM   14186 O O     . LEU D  1 335 ? 33.908  54.721  231.099 1.00 76.26  ? 335 LEU D O     1 
ATOM   14187 C CB    . LEU D  1 335 ? 34.669  51.601  231.008 1.00 69.15  ? 335 LEU D CB    1 
ATOM   14188 C CG    . LEU D  1 335 ? 35.910  50.710  230.910 1.00 64.19  ? 335 LEU D CG    1 
ATOM   14189 C CD1   . LEU D  1 335 ? 35.660  49.523  229.992 1.00 61.34  ? 335 LEU D CD1   1 
ATOM   14190 C CD2   . LEU D  1 335 ? 37.103  51.521  230.426 1.00 70.73  ? 335 LEU D CD2   1 
ATOM   14191 N N     . ALA D  1 336 ? 32.430  53.553  232.327 1.00 74.53  ? 336 ALA D N     1 
ATOM   14192 C CA    . ALA D  1 336 ? 31.356  54.527  232.155 1.00 72.01  ? 336 ALA D CA    1 
ATOM   14193 C C     . ALA D  1 336 ? 31.593  55.780  232.993 1.00 72.59  ? 336 ALA D C     1 
ATOM   14194 O O     . ALA D  1 336 ? 30.840  56.750  232.904 1.00 72.18  ? 336 ALA D O     1 
ATOM   14195 C CB    . ALA D  1 336 ? 30.010  53.907  232.508 1.00 68.81  ? 336 ALA D CB    1 
ATOM   14196 N N     . GLY D  1 337 ? 32.640  55.754  233.810 1.00 75.58  ? 337 GLY D N     1 
ATOM   14197 C CA    . GLY D  1 337 ? 32.944  56.866  234.690 1.00 82.86  ? 337 GLY D CA    1 
ATOM   14198 C C     . GLY D  1 337 ? 32.095  56.825  235.944 1.00 80.05  ? 337 GLY D C     1 
ATOM   14199 O O     . GLY D  1 337 ? 31.794  57.862  236.535 1.00 84.84  ? 337 GLY D O     1 
ATOM   14200 N N     . LEU D  1 338 ? 31.708  55.620  236.351 1.00 76.67  ? 338 LEU D N     1 
ATOM   14201 C CA    . LEU D  1 338 ? 30.868  55.449  237.530 1.00 83.09  ? 338 LEU D CA    1 
ATOM   14202 C C     . LEU D  1 338 ? 31.678  54.993  238.737 1.00 84.04  ? 338 LEU D C     1 
ATOM   14203 O O     . LEU D  1 338 ? 32.864  54.687  238.627 1.00 87.88  ? 338 LEU D O     1 
ATOM   14204 C CB    . LEU D  1 338 ? 29.745  54.448  237.254 1.00 80.32  ? 338 LEU D CB    1 
ATOM   14205 C CG    . LEU D  1 338 ? 28.768  54.803  236.133 1.00 77.56  ? 338 LEU D CG    1 
ATOM   14206 C CD1   . LEU D  1 338 ? 27.645  53.783  236.076 1.00 73.80  ? 338 LEU D CD1   1 
ATOM   14207 C CD2   . LEU D  1 338 ? 28.215  56.204  236.331 1.00 75.04  ? 338 LEU D CD2   1 
ATOM   14208 N N     . GLU D  1 339 ? 31.018  54.946  239.889 1.00 85.18  ? 339 GLU D N     1 
ATOM   14209 C CA    . GLU D  1 339 ? 31.660  54.560  241.138 1.00 84.86  ? 339 GLU D CA    1 
ATOM   14210 C C     . GLU D  1 339 ? 31.288  53.130  241.519 1.00 85.35  ? 339 GLU D C     1 
ATOM   14211 O O     . GLU D  1 339 ? 32.156  52.325  241.859 1.00 79.11  ? 339 GLU D O     1 
ATOM   14212 C CB    . GLU D  1 339 ? 31.272  55.535  242.251 1.00 88.16  ? 339 GLU D CB    1 
ATOM   14213 C CG    . GLU D  1 339 ? 31.451  56.994  241.861 1.00 91.19  ? 339 GLU D CG    1 
ATOM   14214 C CD    . GLU D  1 339 ? 30.851  57.958  242.864 1.00 99.72  ? 339 GLU D CD    1 
ATOM   14215 O OE1   . GLU D  1 339 ? 30.013  57.525  243.683 1.00 100.36 ? 339 GLU D OE1   1 
ATOM   14216 O OE2   . GLU D  1 339 ? 31.214  59.153  242.828 1.00 100.60 ? 339 GLU D OE2   1 
ATOM   14217 N N     . THR D  1 340 ? 29.997  52.815  241.452 1.00 85.73  ? 340 THR D N     1 
ATOM   14218 C CA    . THR D  1 340 ? 29.530  51.471  241.774 1.00 81.57  ? 340 THR D CA    1 
ATOM   14219 C C     . THR D  1 340 ? 28.723  50.864  240.627 1.00 77.72  ? 340 THR D C     1 
ATOM   14220 O O     . THR D  1 340 ? 28.283  51.571  239.718 1.00 78.12  ? 340 THR D O     1 
ATOM   14221 C CB    . THR D  1 340 ? 28.674  51.463  243.054 1.00 83.94  ? 340 THR D CB    1 
ATOM   14222 O OG1   . THR D  1 340 ? 28.528  50.118  243.524 1.00 85.98  ? 340 THR D OG1   1 
ATOM   14223 C CG2   . THR D  1 340 ? 27.297  52.058  242.791 1.00 77.30  ? 340 THR D CG2   1 
ATOM   14224 N N     . VAL D  1 341 ? 28.541  49.547  240.676 1.00 73.82  ? 341 VAL D N     1 
ATOM   14225 C CA    . VAL D  1 341 ? 27.773  48.824  239.666 1.00 71.64  ? 341 VAL D CA    1 
ATOM   14226 C C     . VAL D  1 341 ? 26.298  49.228  239.719 1.00 76.71  ? 341 VAL D C     1 
ATOM   14227 O O     . VAL D  1 341 ? 25.618  49.279  238.693 1.00 71.53  ? 341 VAL D O     1 
ATOM   14228 C CB    . VAL D  1 341 ? 27.908  47.289  239.851 1.00 71.03  ? 341 VAL D CB    1 
ATOM   14229 C CG1   . VAL D  1 341 ? 26.888  46.540  239.007 1.00 70.26  ? 341 VAL D CG1   1 
ATOM   14230 C CG2   . VAL D  1 341 ? 29.321  46.832  239.510 1.00 71.60  ? 341 VAL D CG2   1 
ATOM   14231 N N     . SER D  1 342 ? 25.817  49.541  240.918 1.00 77.64  ? 342 SER D N     1 
ATOM   14232 C CA    . SER D  1 342 ? 24.415  49.900  241.119 1.00 76.84  ? 342 SER D CA    1 
ATOM   14233 C C     . SER D  1 342 ? 23.992  51.146  240.338 1.00 75.62  ? 342 SER D C     1 
ATOM   14234 O O     . SER D  1 342 ? 22.811  51.326  240.047 1.00 72.52  ? 342 SER D O     1 
ATOM   14235 C CB    . SER D  1 342 ? 24.131  50.108  242.607 1.00 77.06  ? 342 SER D CB    1 
ATOM   14236 O OG    . SER D  1 342 ? 24.158  48.876  243.309 1.00 76.30  ? 342 SER D OG    1 
ATOM   14237 N N     . GLN D  1 343 ? 24.953  52.003  240.003 1.00 73.84  ? 343 GLN D N     1 
ATOM   14238 C CA    . GLN D  1 343 ? 24.666  53.223  239.251 1.00 74.94  ? 343 GLN D CA    1 
ATOM   14239 C C     . GLN D  1 343 ? 24.344  52.925  237.789 1.00 71.93  ? 343 GLN D C     1 
ATOM   14240 O O     . GLN D  1 343 ? 23.767  53.757  237.087 1.00 70.75  ? 343 GLN D O     1 
ATOM   14241 C CB    . GLN D  1 343 ? 25.844  54.193  239.337 1.00 75.50  ? 343 GLN D CB    1 
ATOM   14242 C CG    . GLN D  1 343 ? 26.087  54.761  240.722 1.00 81.48  ? 343 GLN D CG    1 
ATOM   14243 C CD    . GLN D  1 343 ? 27.496  55.288  240.883 1.00 85.71  ? 343 GLN D CD    1 
ATOM   14244 O OE1   . GLN D  1 343 ? 28.443  54.519  241.032 1.00 86.63  ? 343 GLN D OE1   1 
ATOM   14245 N NE2   . GLN D  1 343 ? 27.644  56.607  240.841 1.00 84.54  ? 343 GLN D NE2   1 
ATOM   14246 N N     . LEU D  1 344 ? 24.732  51.737  237.335 1.00 67.39  ? 344 LEU D N     1 
ATOM   14247 C CA    . LEU D  1 344 ? 24.383  51.276  235.997 1.00 66.02  ? 344 LEU D CA    1 
ATOM   14248 C C     . LEU D  1 344 ? 22.870  51.146  235.871 1.00 66.21  ? 344 LEU D C     1 
ATOM   14249 O O     . LEU D  1 344 ? 22.290  51.478  234.839 1.00 64.01  ? 344 LEU D O     1 
ATOM   14250 C CB    . LEU D  1 344 ? 25.056  49.937  235.689 1.00 62.53  ? 344 LEU D CB    1 
ATOM   14251 C CG    . LEU D  1 344 ? 26.579  49.915  235.537 1.00 62.97  ? 344 LEU D CG    1 
ATOM   14252 C CD1   . LEU D  1 344 ? 27.083  48.485  235.455 1.00 60.30  ? 344 LEU D CD1   1 
ATOM   14253 C CD2   . LEU D  1 344 ? 26.992  50.694  234.304 1.00 60.61  ? 344 LEU D CD2   1 
ATOM   14254 N N     . ASN D  1 345 ? 22.234  50.676  236.940 1.00 68.81  ? 345 ASN D N     1 
ATOM   14255 C CA    . ASN D  1 345 ? 20.798  50.419  236.932 1.00 65.53  ? 345 ASN D CA    1 
ATOM   14256 C C     . ASN D  1 345 ? 19.956  51.683  237.151 1.00 68.73  ? 345 ASN D C     1 
ATOM   14257 O O     . ASN D  1 345 ? 18.776  51.598  237.484 1.00 71.16  ? 345 ASN D O     1 
ATOM   14258 C CB    . ASN D  1 345 ? 20.454  49.366  237.993 1.00 65.59  ? 345 ASN D CB    1 
ATOM   14259 C CG    . ASN D  1 345 ? 19.098  48.714  237.761 1.00 69.07  ? 345 ASN D CG    1 
ATOM   14260 O OD1   . ASN D  1 345 ? 18.108  49.068  238.401 1.00 70.46  ? 345 ASN D OD1   1 
ATOM   14261 N ND2   . ASN D  1 345 ? 19.051  47.755  236.844 1.00 61.58  ? 345 ASN D ND2   1 
ATOM   14262 N N     . ASN D  1 346 ? 20.555  52.856  236.966 1.00 69.58  ? 346 ASN D N     1 
ATOM   14263 C CA    . ASN D  1 346 ? 19.786  54.097  237.012 1.00 69.16  ? 346 ASN D CA    1 
ATOM   14264 C C     . ASN D  1 346 ? 19.801  54.798  235.657 1.00 70.69  ? 346 ASN D C     1 
ATOM   14265 O O     . ASN D  1 346 ? 20.797  55.410  235.272 1.00 73.08  ? 346 ASN D O     1 
ATOM   14266 C CB    . ASN D  1 346 ? 20.313  55.033  238.102 1.00 72.97  ? 346 ASN D CB    1 
ATOM   14267 C CG    . ASN D  1 346 ? 19.477  56.294  238.242 1.00 78.18  ? 346 ASN D CG    1 
ATOM   14268 O OD1   . ASN D  1 346 ? 19.937  57.394  237.933 1.00 80.61  ? 346 ASN D OD1   1 
ATOM   14269 N ND2   . ASN D  1 346 ? 18.238  56.138  238.696 1.00 77.69  ? 346 ASN D ND2   1 
ATOM   14270 N N     . ARG D  1 347 ? 18.682  54.703  234.945 1.00 63.44  ? 347 ARG D N     1 
ATOM   14271 C CA    . ARG D  1 347 ? 18.578  55.193  233.575 1.00 59.91  ? 347 ARG D CA    1 
ATOM   14272 C C     . ARG D  1 347 ? 18.584  56.719  233.477 1.00 60.10  ? 347 ARG D C     1 
ATOM   14273 O O     . ARG D  1 347 ? 18.834  57.275  232.408 1.00 60.21  ? 347 ARG D O     1 
ATOM   14274 C CB    . ARG D  1 347 ? 17.307  54.644  232.921 1.00 61.10  ? 347 ARG D CB    1 
ATOM   14275 C CG    . ARG D  1 347 ? 16.022  55.113  233.586 1.00 60.34  ? 347 ARG D CG    1 
ATOM   14276 C CD    . ARG D  1 347 ? 14.792  54.401  233.033 1.00 56.52  ? 347 ARG D CD    1 
ATOM   14277 N NE    . ARG D  1 347 ? 14.590  54.636  231.605 1.00 50.87  ? 347 ARG D NE    1 
ATOM   14278 C CZ    . ARG D  1 347 ? 14.606  53.679  230.681 1.00 46.45  ? 347 ARG D CZ    1 
ATOM   14279 N NH1   . ARG D  1 347 ? 14.813  52.418  231.034 1.00 43.24  ? 347 ARG D NH1   1 
ATOM   14280 N NH2   . ARG D  1 347 ? 14.412  53.981  229.405 1.00 48.76  ? 347 ARG D NH2   1 
ATOM   14281 N N     . PHE D  1 348 ? 18.311  57.393  234.589 1.00 67.62  ? 348 PHE D N     1 
ATOM   14282 C CA    . PHE D  1 348 ? 18.167  58.844  234.568 1.00 71.88  ? 348 PHE D CA    1 
ATOM   14283 C C     . PHE D  1 348 ? 19.401  59.589  235.063 1.00 80.84  ? 348 PHE D C     1 
ATOM   14284 O O     . PHE D  1 348 ? 19.370  60.810  235.216 1.00 83.08  ? 348 PHE D O     1 
ATOM   14285 C CB    . PHE D  1 348 ? 16.955  59.269  235.400 1.00 73.23  ? 348 PHE D CB    1 
ATOM   14286 C CG    . PHE D  1 348 ? 15.664  58.674  234.930 1.00 69.49  ? 348 PHE D CG    1 
ATOM   14287 C CD1   . PHE D  1 348 ? 15.233  58.870  233.628 1.00 65.55  ? 348 PHE D CD1   1 
ATOM   14288 C CD2   . PHE D  1 348 ? 14.878  57.922  235.787 1.00 67.54  ? 348 PHE D CD2   1 
ATOM   14289 C CE1   . PHE D  1 348 ? 14.045  58.319  233.188 1.00 67.34  ? 348 PHE D CE1   1 
ATOM   14290 C CE2   . PHE D  1 348 ? 13.686  57.373  235.352 1.00 69.99  ? 348 PHE D CE2   1 
ATOM   14291 C CZ    . PHE D  1 348 ? 13.270  57.573  234.052 1.00 66.62  ? 348 PHE D CZ    1 
ATOM   14292 N N     . LEU D  1 349 ? 20.485  58.864  235.313 1.00 82.68  ? 349 LEU D N     1 
ATOM   14293 C CA    . LEU D  1 349 ? 21.706  59.510  235.777 1.00 84.57  ? 349 LEU D CA    1 
ATOM   14294 C C     . LEU D  1 349 ? 22.451  60.175  234.627 1.00 89.12  ? 349 LEU D C     1 
ATOM   14295 O O     . LEU D  1 349 ? 23.208  59.522  233.910 1.00 92.57  ? 349 LEU D O     1 
ATOM   14296 C CB    . LEU D  1 349 ? 22.626  58.512  236.479 1.00 84.28  ? 349 LEU D CB    1 
ATOM   14297 C CG    . LEU D  1 349 ? 23.696  59.164  237.362 1.00 92.09  ? 349 LEU D CG    1 
ATOM   14298 C CD1   . LEU D  1 349 ? 23.032  59.950  238.485 1.00 93.20  ? 349 LEU D CD1   1 
ATOM   14299 C CD2   . LEU D  1 349 ? 24.662  58.128  237.917 1.00 89.47  ? 349 LEU D CD2   1 
ATOM   14300 N N     . LYS D  1 350 ? 22.229  61.473  234.448 1.00 92.24  ? 350 LYS D N     1 
ATOM   14301 C CA    . LYS D  1 350 ? 22.991  62.239  233.468 1.00 97.57  ? 350 LYS D CA    1 
ATOM   14302 C C     . LYS D  1 350 ? 23.974  63.173  234.168 1.00 103.66 ? 350 LYS D C     1 
ATOM   14303 O O     . LYS D  1 350 ? 23.585  64.236  234.650 1.00 105.27 ? 350 LYS D O     1 
ATOM   14304 C CB    . LYS D  1 350 ? 22.066  63.056  232.559 1.00 98.48  ? 350 LYS D CB    1 
ATOM   14305 C CG    . LYS D  1 350 ? 20.667  62.494  232.375 1.00 95.55  ? 350 LYS D CG    1 
ATOM   14306 C CD    . LYS D  1 350 ? 19.897  63.348  231.374 1.00 98.80  ? 350 LYS D CD    1 
ATOM   14307 C CE    . LYS D  1 350 ? 18.403  63.075  231.392 1.00 106.45 ? 350 LYS D CE    1 
ATOM   14308 N NZ    . LYS D  1 350 ? 17.692  64.068  230.536 1.00 94.35  ? 350 LYS D NZ    1 
ATOM   14309 N N     . PHE D  1 351 ? 25.244  62.781  234.218 1.00 109.61 ? 351 PHE D N     1 
ATOM   14310 C CA    . PHE D  1 351 ? 26.286  63.633  234.790 1.00 113.12 ? 351 PHE D CA    1 
ATOM   14311 C C     . PHE D  1 351 ? 26.723  64.717  233.800 1.00 112.90 ? 351 PHE D C     1 
ATOM   14312 O O     . PHE D  1 351 ? 27.666  65.474  234.057 1.00 113.87 ? 351 PHE D O     1 
ATOM   14313 C CB    . PHE D  1 351 ? 27.487  62.790  235.236 1.00 113.19 ? 351 PHE D CB    1 
ATOM   14314 C CG    . PHE D  1 351 ? 27.364  62.268  236.641 1.00 113.61 ? 351 PHE D CG    1 
ATOM   14315 C CD1   . PHE D  1 351 ? 26.338  62.713  237.461 1.00 113.99 ? 351 PHE D CD1   1 
ATOM   14316 C CD2   . PHE D  1 351 ? 28.270  61.347  237.148 1.00 112.97 ? 351 PHE D CD2   1 
ATOM   14317 C CE1   . PHE D  1 351 ? 26.211  62.247  238.756 1.00 112.16 ? 351 PHE D CE1   1 
ATOM   14318 C CE2   . PHE D  1 351 ? 28.148  60.876  238.449 1.00 110.95 ? 351 PHE D CE2   1 
ATOM   14319 C CZ    . PHE D  1 351 ? 27.114  61.329  239.251 1.00 110.77 ? 351 PHE D CZ    1 
ATOM   14320 N N     . ASP D  1 352 ? 26.017  64.777  232.674 1.00 108.47 ? 352 ASP D N     1 
ATOM   14321 C CA    . ASP D  1 352 ? 26.181  65.825  231.673 1.00 103.58 ? 352 ASP D CA    1 
ATOM   14322 C C     . ASP D  1 352 ? 24.828  66.518  231.477 1.00 102.87 ? 352 ASP D C     1 
ATOM   14323 O O     . ASP D  1 352 ? 23.806  66.026  231.955 1.00 107.74 ? 352 ASP D O     1 
ATOM   14324 C CB    . ASP D  1 352 ? 26.699  65.235  230.356 1.00 101.75 ? 352 ASP D CB    1 
ATOM   14325 C CG    . ASP D  1 352 ? 27.171  66.296  229.373 1.00 98.73  ? 352 ASP D CG    1 
ATOM   14326 O OD1   . ASP D  1 352 ? 26.407  67.237  229.084 1.00 95.03  ? 352 ASP D OD1   1 
ATOM   14327 O OD2   . ASP D  1 352 ? 28.320  66.186  228.894 1.00 111.54 ? 352 ASP D OD2   1 
ATOM   14328 N N     . GLU D  1 353 ? 24.834  67.661  230.793 1.00 97.75  ? 353 GLU D N     1 
ATOM   14329 C CA    . GLU D  1 353 ? 23.620  68.432  230.512 1.00 89.64  ? 353 GLU D CA    1 
ATOM   14330 C C     . GLU D  1 353 ? 23.841  69.314  229.288 1.00 84.43  ? 353 GLU D C     1 
ATOM   14331 O O     . GLU D  1 353 ? 23.089  70.259  229.044 1.00 83.98  ? 353 GLU D O     1 
ATOM   14332 C CB    . GLU D  1 353 ? 23.224  69.296  231.712 1.00 97.02  ? 353 GLU D CB    1 
ATOM   14333 C CG    . GLU D  1 353 ? 24.184  70.455  231.988 1.00 103.23 ? 353 GLU D CG    1 
ATOM   14334 C CD    . GLU D  1 353 ? 24.447  70.659  233.471 1.00 109.25 ? 353 GLU D CD    1 
ATOM   14335 O OE1   . GLU D  1 353 ? 24.920  69.703  234.120 1.00 109.56 ? 353 GLU D OE1   1 
ATOM   14336 O OE2   . GLU D  1 353 ? 24.183  71.767  233.985 1.00 110.24 ? 353 GLU D OE2   1 
ATOM   14337 N N     . ARG D  1 354 ? 24.893  69.010  228.534 1.00 80.67  ? 354 ARG D N     1 
ATOM   14338 C CA    . ARG D  1 354 ? 25.265  69.811  227.370 1.00 75.44  ? 354 ARG D CA    1 
ATOM   14339 C C     . ARG D  1 354 ? 24.506  69.422  226.111 1.00 63.25  ? 354 ARG D C     1 
ATOM   14340 O O     . ARG D  1 354 ? 24.274  68.241  225.848 1.00 62.41  ? 354 ARG D O     1 
ATOM   14341 C CB    . ARG D  1 354 ? 26.766  69.696  227.103 1.00 74.58  ? 354 ARG D CB    1 
ATOM   14342 C CG    . ARG D  1 354 ? 27.626  70.491  228.064 1.00 79.85  ? 354 ARG D CG    1 
ATOM   14343 C CD    . ARG D  1 354 ? 29.093  70.127  227.925 1.00 79.95  ? 354 ARG D CD    1 
ATOM   14344 N NE    . ARG D  1 354 ? 29.338  68.736  228.294 1.00 92.90  ? 354 ARG D NE    1 
ATOM   14345 C CZ    . ARG D  1 354 ? 30.498  68.109  228.127 1.00 90.91  ? 354 ARG D CZ    1 
ATOM   14346 N NH1   . ARG D  1 354 ? 31.530  68.745  227.592 1.00 82.62  ? 354 ARG D NH1   1 
ATOM   14347 N NH2   . ARG D  1 354 ? 30.626  66.840  228.494 1.00 92.06  ? 354 ARG D NH2   1 
ATOM   14348 N N     . ALA D  1 355 ? 24.117  70.432  225.341 1.00 59.89  ? 355 ALA D N     1 
ATOM   14349 C CA    . ALA D  1 355 ? 23.704  70.213  223.965 1.00 57.17  ? 355 ALA D CA    1 
ATOM   14350 C C     . ALA D  1 355 ? 24.945  69.831  223.188 1.00 61.37  ? 355 ALA D C     1 
ATOM   14351 O O     . ALA D  1 355 ? 26.047  70.238  223.557 1.00 63.79  ? 355 ALA D O     1 
ATOM   14352 C CB    . ALA D  1 355 ? 23.066  71.456  223.379 1.00 59.36  ? 355 ALA D CB    1 
ATOM   14353 N N     . PHE D  1 356 ? 24.787  69.056  222.122 1.00 56.43  ? 356 PHE D N     1 
ATOM   14354 C CA    . PHE D  1 356 ? 25.937  68.704  221.300 1.00 55.04  ? 356 PHE D CA    1 
ATOM   14355 C C     . PHE D  1 356 ? 25.560  68.468  219.848 1.00 52.65  ? 356 PHE D C     1 
ATOM   14356 O O     . PHE D  1 356 ? 24.393  68.298  219.503 1.00 52.88  ? 356 PHE D O     1 
ATOM   14357 C CB    . PHE D  1 356 ? 26.649  67.463  221.860 1.00 52.76  ? 356 PHE D CB    1 
ATOM   14358 C CG    . PHE D  1 356 ? 25.815  66.210  221.825 1.00 54.56  ? 356 PHE D CG    1 
ATOM   14359 C CD1   . PHE D  1 356 ? 25.797  65.396  220.699 1.00 50.61  ? 356 PHE D CD1   1 
ATOM   14360 C CD2   . PHE D  1 356 ? 25.064  65.836  222.925 1.00 49.88  ? 356 PHE D CD2   1 
ATOM   14361 C CE1   . PHE D  1 356 ? 25.033  64.249  220.670 1.00 47.99  ? 356 PHE D CE1   1 
ATOM   14362 C CE2   . PHE D  1 356 ? 24.299  64.683  222.900 1.00 50.56  ? 356 PHE D CE2   1 
ATOM   14363 C CZ    . PHE D  1 356 ? 24.285  63.890  221.771 1.00 44.07  ? 356 PHE D CZ    1 
ATOM   14364 N N     . LYS D  1 357 ? 26.583  68.467  219.009 1.00 46.60  ? 357 LYS D N     1 
ATOM   14365 C CA    . LYS D  1 357 ? 26.467  68.131  217.604 1.00 46.52  ? 357 LYS D CA    1 
ATOM   14366 C C     . LYS D  1 357 ? 27.720  67.329  217.301 1.00 55.20  ? 357 LYS D C     1 
ATOM   14367 O O     . LYS D  1 357 ? 28.794  67.630  217.824 1.00 56.75  ? 357 LYS D O     1 
ATOM   14368 C CB    . LYS D  1 357 ? 26.347  69.389  216.736 1.00 57.42  ? 357 LYS D CB    1 
ATOM   14369 C CG    . LYS D  1 357 ? 26.537  69.181  215.246 1.00 57.72  ? 357 LYS D CG    1 
ATOM   14370 C CD    . LYS D  1 357 ? 25.544  68.199  214.655 1.00 57.03  ? 357 LYS D CD    1 
ATOM   14371 C CE    . LYS D  1 357 ? 25.982  67.777  213.258 1.00 60.97  ? 357 LYS D CE    1 
ATOM   14372 N NZ    . LYS D  1 357 ? 25.019  66.851  212.600 1.00 58.65  ? 357 LYS D NZ    1 
ATOM   14373 N N     . THR D  1 358 ? 27.585  66.281  216.501 1.00 47.48  ? 358 THR D N     1 
ATOM   14374 C CA    . THR D  1 358 ? 28.706  65.385  216.280 1.00 48.35  ? 358 THR D CA    1 
ATOM   14375 C C     . THR D  1 358 ? 28.724  64.829  214.871 1.00 45.79  ? 358 THR D C     1 
ATOM   14376 O O     . THR D  1 358 ? 27.706  64.809  214.183 1.00 50.04  ? 358 THR D O     1 
ATOM   14377 C CB    . THR D  1 358 ? 28.683  64.212  217.266 1.00 47.14  ? 358 THR D CB    1 
ATOM   14378 O OG1   . THR D  1 358 ? 29.768  63.325  216.971 1.00 51.67  ? 358 THR D OG1   1 
ATOM   14379 C CG2   . THR D  1 358 ? 27.376  63.459  217.143 1.00 45.15  ? 358 THR D CG2   1 
ATOM   14380 N N     . LYS D  1 359 ? 29.901  64.386  214.449 1.00 42.81  ? 359 LYS D N     1 
ATOM   14381 C CA    . LYS D  1 359 ? 30.064  63.729  213.164 1.00 44.27  ? 359 LYS D CA    1 
ATOM   14382 C C     . LYS D  1 359 ? 31.025  62.567  213.347 1.00 44.03  ? 359 LYS D C     1 
ATOM   14383 O O     . LYS D  1 359 ? 31.651  62.432  214.398 1.00 37.97  ? 359 LYS D O     1 
ATOM   14384 C CB    . LYS D  1 359 ? 30.581  64.701  212.100 1.00 45.56  ? 359 LYS D CB    1 
ATOM   14385 C CG    . LYS D  1 359 ? 29.701  65.927  211.891 1.00 48.94  ? 359 LYS D CG    1 
ATOM   14386 C CD    . LYS D  1 359 ? 30.177  66.779  210.725 1.00 46.53  ? 359 LYS D CD    1 
ATOM   14387 C CE    . LYS D  1 359 ? 29.627  66.274  209.405 1.00 48.93  ? 359 LYS D CE    1 
ATOM   14388 N NZ    . LYS D  1 359 ? 28.157  66.489  209.320 1.00 50.68  ? 359 LYS D NZ    1 
ATOM   14389 N N     . VAL D  1 360 ? 31.146  61.726  212.329 1.00 40.72  ? 360 VAL D N     1 
ATOM   14390 C CA    . VAL D  1 360 ? 31.996  60.555  212.442 1.00 36.75  ? 360 VAL D CA    1 
ATOM   14391 C C     . VAL D  1 360 ? 32.623  60.185  211.102 1.00 37.54  ? 360 VAL D C     1 
ATOM   14392 O O     . VAL D  1 360 ? 32.062  60.457  210.040 1.00 41.46  ? 360 VAL D O     1 
ATOM   14393 C CB    . VAL D  1 360 ? 31.202  59.350  213.004 1.00 40.23  ? 360 VAL D CB    1 
ATOM   14394 C CG1   . VAL D  1 360 ? 30.247  58.802  211.959 1.00 34.62  ? 360 VAL D CG1   1 
ATOM   14395 C CG2   . VAL D  1 360 ? 32.146  58.266  213.499 1.00 34.83  ? 360 VAL D CG2   1 
ATOM   14396 N N     . ASP D  1 361 ? 33.808  59.592  211.163 1.00 35.57  ? 361 ASP D N     1 
ATOM   14397 C CA    . ASP D  1 361 ? 34.460  59.048  209.983 1.00 38.12  ? 361 ASP D CA    1 
ATOM   14398 C C     . ASP D  1 361 ? 34.848  57.600  210.230 1.00 38.67  ? 361 ASP D C     1 
ATOM   14399 O O     . ASP D  1 361 ? 35.074  57.197  211.369 1.00 35.67  ? 361 ASP D O     1 
ATOM   14400 C CB    . ASP D  1 361 ? 35.701  59.868  209.618 1.00 44.46  ? 361 ASP D CB    1 
ATOM   14401 C CG    . ASP D  1 361 ? 35.376  61.065  208.752 1.00 46.71  ? 361 ASP D CG    1 
ATOM   14402 O OD1   . ASP D  1 361 ? 34.603  60.909  207.785 1.00 43.35  ? 361 ASP D OD1   1 
ATOM   14403 O OD2   . ASP D  1 361 ? 35.896  62.164  209.036 1.00 49.89  ? 361 ASP D OD2   1 
ATOM   14404 N N     . LEU D  1 362 ? 34.906  56.813  209.164 1.00 33.54  ? 362 LEU D N     1 
ATOM   14405 C CA    . LEU D  1 362 ? 35.538  55.506  209.232 1.00 37.80  ? 362 LEU D CA    1 
ATOM   14406 C C     . LEU D  1 362 ? 36.663  55.506  208.212 1.00 42.76  ? 362 LEU D C     1 
ATOM   14407 O O     . LEU D  1 362 ? 36.522  56.078  207.137 1.00 42.82  ? 362 LEU D O     1 
ATOM   14408 C CB    . LEU D  1 362 ? 34.535  54.379  208.976 1.00 40.68  ? 362 LEU D CB    1 
ATOM   14409 C CG    . LEU D  1 362 ? 33.483  54.254  210.081 1.00 39.00  ? 362 LEU D CG    1 
ATOM   14410 C CD1   . LEU D  1 362 ? 32.135  54.775  209.614 1.00 39.34  ? 362 LEU D CD1   1 
ATOM   14411 C CD2   . LEU D  1 362 ? 33.372  52.827  210.587 1.00 39.65  ? 362 LEU D CD2   1 
ATOM   14412 N N     . THR D  1 363 ? 37.789  54.896  208.558 1.00 43.56  ? 363 THR D N     1 
ATOM   14413 C CA    . THR D  1 363 ? 38.975  55.001  207.721 1.00 42.11  ? 363 THR D CA    1 
ATOM   14414 C C     . THR D  1 363 ? 39.333  53.674  207.062 1.00 44.55  ? 363 THR D C     1 
ATOM   14415 O O     . THR D  1 363 ? 39.045  52.604  207.597 1.00 40.79  ? 363 THR D O     1 
ATOM   14416 C CB    . THR D  1 363 ? 40.180  55.501  208.536 1.00 40.79  ? 363 THR D CB    1 
ATOM   14417 O OG1   . THR D  1 363 ? 40.525  54.527  209.528 1.00 40.15  ? 363 THR D OG1   1 
ATOM   14418 C CG2   . THR D  1 363 ? 39.847  56.821  209.224 1.00 39.99  ? 363 THR D CG2   1 
ATOM   14419 N N     . LYS D  1 364 ? 39.953  53.754  205.891 1.00 48.10  ? 364 LYS D N     1 
ATOM   14420 C CA    . LYS D  1 364 ? 40.432  52.570  205.190 1.00 45.83  ? 364 LYS D CA    1 
ATOM   14421 C C     . LYS D  1 364 ? 41.954  52.574  205.163 1.00 51.12  ? 364 LYS D C     1 
ATOM   14422 O O     . LYS D  1 364 ? 42.592  51.524  205.214 1.00 49.74  ? 364 LYS D O     1 
ATOM   14423 C CB    . LYS D  1 364 ? 39.876  52.516  203.767 1.00 47.80  ? 364 LYS D CB    1 
ATOM   14424 C CG    . LYS D  1 364 ? 38.361  52.413  203.691 1.00 53.02  ? 364 LYS D CG    1 
ATOM   14425 C CD    . LYS D  1 364 ? 37.876  51.015  204.027 1.00 54.93  ? 364 LYS D CD    1 
ATOM   14426 C CE    . LYS D  1 364 ? 36.358  50.957  204.056 1.00 61.84  ? 364 LYS D CE    1 
ATOM   14427 N NZ    . LYS D  1 364 ? 35.876  49.929  205.020 1.00 62.06  ? 364 LYS D NZ    1 
ATOM   14428 N N     . GLU D  1 365 ? 42.527  53.769  205.084 1.00 51.45  ? 365 GLU D N     1 
ATOM   14429 C CA    . GLU D  1 365 ? 43.975  53.923  205.056 1.00 53.57  ? 365 GLU D CA    1 
ATOM   14430 C C     . GLU D  1 365 ? 44.482  54.465  206.386 1.00 52.86  ? 365 GLU D C     1 
ATOM   14431 O O     . GLU D  1 365 ? 43.746  55.148  207.099 1.00 46.23  ? 365 GLU D O     1 
ATOM   14432 C CB    . GLU D  1 365 ? 44.395  54.851  203.912 1.00 56.28  ? 365 GLU D CB    1 
ATOM   14433 C CG    . GLU D  1 365 ? 43.930  54.401  202.535 1.00 59.38  ? 365 GLU D CG    1 
ATOM   14434 C CD    . GLU D  1 365 ? 44.664  53.168  202.043 1.00 63.95  ? 365 GLU D CD    1 
ATOM   14435 O OE1   . GLU D  1 365 ? 45.691  52.798  202.652 1.00 66.88  ? 365 GLU D OE1   1 
ATOM   14436 O OE2   . GLU D  1 365 ? 44.216  52.569  201.043 1.00 68.80  ? 365 GLU D OE2   1 
ATOM   14437 N N     . PRO D  1 366 ? 45.742  54.151  206.730 1.00 49.08  ? 366 PRO D N     1 
ATOM   14438 C CA    . PRO D  1 366 ? 46.351  54.749  207.922 1.00 41.80  ? 366 PRO D CA    1 
ATOM   14439 C C     . PRO D  1 366 ? 46.356  56.268  207.814 1.00 42.70  ? 366 PRO D C     1 
ATOM   14440 O O     . PRO D  1 366 ? 46.497  56.793  206.710 1.00 44.00  ? 366 PRO D O     1 
ATOM   14441 C CB    . PRO D  1 366 ? 47.779  54.194  207.910 1.00 45.36  ? 366 PRO D CB    1 
ATOM   14442 C CG    . PRO D  1 366 ? 47.699  52.948  207.104 1.00 44.55  ? 366 PRO D CG    1 
ATOM   14443 C CD    . PRO D  1 366 ? 46.641  53.188  206.070 1.00 48.14  ? 366 PRO D CD    1 
ATOM   14444 N N     . LEU D  1 367 ? 46.190  56.964  208.933 1.00 42.53  ? 367 LEU D N     1 
ATOM   14445 C CA    . LEU D  1 367 ? 46.241  58.419  208.923 1.00 46.07  ? 367 LEU D CA    1 
ATOM   14446 C C     . LEU D  1 367 ? 47.684  58.896  208.977 1.00 46.56  ? 367 LEU D C     1 
ATOM   14447 O O     . LEU D  1 367 ? 48.440  58.481  209.853 1.00 47.23  ? 367 LEU D O     1 
ATOM   14448 C CB    . LEU D  1 367 ? 45.451  59.002  210.097 1.00 45.85  ? 367 LEU D CB    1 
ATOM   14449 C CG    . LEU D  1 367 ? 43.962  58.653  210.175 1.00 43.56  ? 367 LEU D CG    1 
ATOM   14450 C CD1   . LEU D  1 367 ? 43.289  59.437  211.296 1.00 41.19  ? 367 LEU D CD1   1 
ATOM   14451 C CD2   . LEU D  1 367 ? 43.279  58.901  208.841 1.00 46.84  ? 367 LEU D CD2   1 
ATOM   14452 N N     . PRO D  1 368 ? 48.073  59.766  208.033 1.00 50.15  ? 368 PRO D N     1 
ATOM   14453 C CA    . PRO D  1 368 ? 49.425  60.333  208.045 1.00 47.46  ? 368 PRO D CA    1 
ATOM   14454 C C     . PRO D  1 368 ? 49.611  61.252  209.245 1.00 50.17  ? 368 PRO D C     1 
ATOM   14455 O O     . PRO D  1 368 ? 48.623  61.674  209.844 1.00 50.11  ? 368 PRO D O     1 
ATOM   14456 C CB    . PRO D  1 368 ? 49.496  61.111  206.728 1.00 46.45  ? 368 PRO D CB    1 
ATOM   14457 C CG    . PRO D  1 368 ? 48.080  61.458  206.426 1.00 53.13  ? 368 PRO D CG    1 
ATOM   14458 C CD    . PRO D  1 368 ? 47.262  60.295  206.922 1.00 51.54  ? 368 PRO D CD    1 
ATOM   14459 N N     . SER D  1 369 ? 50.862  61.547  209.587 1.00 51.92  ? 369 SER D N     1 
ATOM   14460 C CA    . SER D  1 369 ? 51.175  62.342  210.769 1.00 52.69  ? 369 SER D CA    1 
ATOM   14461 C C     . SER D  1 369 ? 50.499  63.711  210.729 1.00 50.45  ? 369 SER D C     1 
ATOM   14462 O O     . SER D  1 369 ? 50.073  64.231  211.760 1.00 50.09  ? 369 SER D O     1 
ATOM   14463 C CB    . SER D  1 369 ? 52.688  62.508  210.912 1.00 49.43  ? 369 SER D CB    1 
ATOM   14464 O OG    . SER D  1 369 ? 53.318  61.249  211.079 1.00 56.50  ? 369 SER D OG    1 
ATOM   14465 N N     . LYS D  1 370 ? 50.384  64.282  209.535 1.00 45.68  ? 370 LYS D N     1 
ATOM   14466 C CA    . LYS D  1 370 ? 49.806  65.613  209.390 1.00 55.57  ? 370 LYS D CA    1 
ATOM   14467 C C     . LYS D  1 370 ? 48.293  65.618  209.596 1.00 55.18  ? 370 LYS D C     1 
ATOM   14468 O O     . LYS D  1 370 ? 47.724  66.641  209.984 1.00 54.42  ? 370 LYS D O     1 
ATOM   14469 C CB    . LYS D  1 370 ? 50.141  66.193  208.019 1.00 57.01  ? 370 LYS D CB    1 
ATOM   14470 C CG    . LYS D  1 370 ? 49.833  65.269  206.860 1.00 54.14  ? 370 LYS D CG    1 
ATOM   14471 C CD    . LYS D  1 370 ? 49.587  66.054  205.585 1.00 56.14  ? 370 LYS D CD    1 
ATOM   14472 C CE    . LYS D  1 370 ? 50.153  65.326  204.383 1.00 65.54  ? 370 LYS D CE    1 
ATOM   14473 N NZ    . LYS D  1 370 ? 49.685  65.917  203.102 1.00 72.08  ? 370 LYS D NZ    1 
ATOM   14474 N N     . ALA D  1 371 ? 47.643  64.487  209.322 1.00 53.36  ? 371 ALA D N     1 
ATOM   14475 C CA    . ALA D  1 371 ? 46.210  64.343  209.573 1.00 50.86  ? 371 ALA D CA    1 
ATOM   14476 C C     . ALA D  1 371 ? 45.912  64.524  211.055 1.00 48.58  ? 371 ALA D C     1 
ATOM   14477 O O     . ALA D  1 371 ? 45.039  65.303  211.434 1.00 50.98  ? 371 ALA D O     1 
ATOM   14478 C CB    . ALA D  1 371 ? 45.716  62.986  209.093 1.00 48.56  ? 371 ALA D CB    1 
ATOM   14479 N N     . PHE D  1 372 ? 46.647  63.794  211.886 1.00 50.60  ? 372 PHE D N     1 
ATOM   14480 C CA    . PHE D  1 372 ? 46.529  63.928  213.330 1.00 51.05  ? 372 PHE D CA    1 
ATOM   14481 C C     . PHE D  1 372 ? 46.983  65.308  213.790 1.00 54.43  ? 372 PHE D C     1 
ATOM   14482 O O     . PHE D  1 372 ? 46.401  65.884  214.707 1.00 54.07  ? 372 PHE D O     1 
ATOM   14483 C CB    . PHE D  1 372 ? 47.340  62.845  214.043 1.00 44.99  ? 372 PHE D CB    1 
ATOM   14484 C CG    . PHE D  1 372 ? 46.649  61.512  214.103 1.00 50.83  ? 372 PHE D CG    1 
ATOM   14485 C CD1   . PHE D  1 372 ? 45.489  61.355  214.844 1.00 47.46  ? 372 PHE D CD1   1 
ATOM   14486 C CD2   . PHE D  1 372 ? 47.161  60.415  213.429 1.00 46.60  ? 372 PHE D CD2   1 
ATOM   14487 C CE1   . PHE D  1 372 ? 44.850  60.132  214.908 1.00 48.81  ? 372 PHE D CE1   1 
ATOM   14488 C CE2   . PHE D  1 372 ? 46.523  59.189  213.489 1.00 44.69  ? 372 PHE D CE2   1 
ATOM   14489 C CZ    . PHE D  1 372 ? 45.366  59.046  214.231 1.00 43.14  ? 372 PHE D CZ    1 
ATOM   14490 N N     . TYR D  1 373 ? 48.022  65.835  213.147 1.00 53.44  ? 373 TYR D N     1 
ATOM   14491 C CA    . TYR D  1 373 ? 48.544  67.150  213.500 1.00 56.84  ? 373 TYR D CA    1 
ATOM   14492 C C     . TYR D  1 373 ? 47.480  68.224  213.310 1.00 54.28  ? 373 TYR D C     1 
ATOM   14493 O O     . TYR D  1 373 ? 47.162  68.962  214.242 1.00 53.66  ? 373 TYR D O     1 
ATOM   14494 C CB    . TYR D  1 373 ? 49.786  67.493  212.673 1.00 62.48  ? 373 TYR D CB    1 
ATOM   14495 C CG    . TYR D  1 373 ? 50.511  68.725  213.172 1.00 63.67  ? 373 TYR D CG    1 
ATOM   14496 C CD1   . TYR D  1 373 ? 51.489  68.626  214.152 1.00 67.00  ? 373 TYR D CD1   1 
ATOM   14497 C CD2   . TYR D  1 373 ? 50.209  69.987  212.674 1.00 65.03  ? 373 TYR D CD2   1 
ATOM   14498 C CE1   . TYR D  1 373 ? 52.151  69.745  214.618 1.00 70.59  ? 373 TYR D CE1   1 
ATOM   14499 C CE2   . TYR D  1 373 ? 50.865  71.113  213.135 1.00 71.65  ? 373 TYR D CE2   1 
ATOM   14500 C CZ    . TYR D  1 373 ? 51.836  70.986  214.107 1.00 74.41  ? 373 TYR D CZ    1 
ATOM   14501 O OH    . TYR D  1 373 ? 52.495  72.102  214.570 1.00 83.95  ? 373 TYR D OH    1 
ATOM   14502 N N     . GLY D  1 374 ? 46.932  68.304  212.102 1.00 50.84  ? 374 GLY D N     1 
ATOM   14503 C CA    . GLY D  1 374 ? 45.911  69.289  211.794 1.00 58.95  ? 374 GLY D CA    1 
ATOM   14504 C C     . GLY D  1 374 ? 44.676  69.142  212.660 1.00 57.98  ? 374 GLY D C     1 
ATOM   14505 O O     . GLY D  1 374 ? 44.080  70.136  213.078 1.00 59.37  ? 374 GLY D O     1 
ATOM   14506 N N     . LEU D  1 375 ? 44.299  67.896  212.931 1.00 53.12  ? 375 LEU D N     1 
ATOM   14507 C CA    . LEU D  1 375 ? 43.146  67.595  213.771 1.00 54.31  ? 375 LEU D CA    1 
ATOM   14508 C C     . LEU D  1 375 ? 43.333  68.132  215.186 1.00 54.99  ? 375 LEU D C     1 
ATOM   14509 O O     . LEU D  1 375 ? 42.453  68.802  215.730 1.00 57.12  ? 375 LEU D O     1 
ATOM   14510 C CB    . LEU D  1 375 ? 42.901  66.084  213.817 1.00 56.10  ? 375 LEU D CB    1 
ATOM   14511 C CG    . LEU D  1 375 ? 41.617  65.633  214.515 1.00 49.44  ? 375 LEU D CG    1 
ATOM   14512 C CD1   . LEU D  1 375 ? 40.406  66.208  213.802 1.00 48.63  ? 375 LEU D CD1   1 
ATOM   14513 C CD2   . LEU D  1 375 ? 41.535  64.116  214.580 1.00 49.02  ? 375 LEU D CD2   1 
ATOM   14514 N N     . LEU D  1 376 ? 44.485  67.830  215.773 1.00 52.01  ? 376 LEU D N     1 
ATOM   14515 C CA    . LEU D  1 376 ? 44.811  68.274  217.124 1.00 59.08  ? 376 LEU D CA    1 
ATOM   14516 C C     . LEU D  1 376 ? 45.001  69.784  217.180 1.00 60.38  ? 376 LEU D C     1 
ATOM   14517 O O     . LEU D  1 376 ? 44.727  70.417  218.200 1.00 60.63  ? 376 LEU D O     1 
ATOM   14518 C CB    . LEU D  1 376 ? 46.071  67.565  217.623 1.00 55.59  ? 376 LEU D CB    1 
ATOM   14519 C CG    . LEU D  1 376 ? 45.934  66.054  217.827 1.00 56.44  ? 376 LEU D CG    1 
ATOM   14520 C CD1   . LEU D  1 376 ? 47.298  65.378  217.848 1.00 50.46  ? 376 LEU D CD1   1 
ATOM   14521 C CD2   . LEU D  1 376 ? 45.173  65.759  219.109 1.00 50.80  ? 376 LEU D CD2   1 
ATOM   14522 N N     . GLU D  1 377 ? 45.471  70.352  216.074 1.00 60.15  ? 377 GLU D N     1 
ATOM   14523 C CA    . GLU D  1 377 ? 45.696  71.789  215.986 1.00 65.34  ? 377 GLU D CA    1 
ATOM   14524 C C     . GLU D  1 377 ? 44.367  72.536  216.075 1.00 63.79  ? 377 GLU D C     1 
ATOM   14525 O O     . GLU D  1 377 ? 44.234  73.492  216.837 1.00 65.07  ? 377 GLU D O     1 
ATOM   14526 C CB    . GLU D  1 377 ? 46.430  72.140  214.689 1.00 64.97  ? 377 GLU D CB    1 
ATOM   14527 C CG    . GLU D  1 377 ? 46.974  73.561  214.638 1.00 72.80  ? 377 GLU D CG    1 
ATOM   14528 C CD    . GLU D  1 377 ? 47.532  73.922  213.274 1.00 75.29  ? 377 GLU D CD    1 
ATOM   14529 O OE1   . GLU D  1 377 ? 48.468  73.235  212.809 1.00 71.45  ? 377 GLU D OE1   1 
ATOM   14530 O OE2   . GLU D  1 377 ? 47.030  74.888  212.663 1.00 82.94  ? 377 GLU D OE2   1 
ATOM   14531 N N     . ARG D  1 378 ? 43.386  72.084  215.297 1.00 61.34  ? 378 ARG D N     1 
ATOM   14532 C CA    . ARG D  1 378 ? 42.036  72.645  215.322 1.00 59.09  ? 378 ARG D CA    1 
ATOM   14533 C C     . ARG D  1 378 ? 41.320  72.315  216.621 1.00 55.68  ? 378 ARG D C     1 
ATOM   14534 O O     . ARG D  1 378 ? 40.519  73.110  217.117 1.00 60.61  ? 378 ARG D O     1 
ATOM   14535 C CB    . ARG D  1 378 ? 41.224  72.125  214.136 1.00 53.56  ? 378 ARG D CB    1 
ATOM   14536 C CG    . ARG D  1 378 ? 41.718  72.627  212.801 1.00 56.48  ? 378 ARG D CG    1 
ATOM   14537 C CD    . ARG D  1 378 ? 41.281  71.735  211.656 1.00 55.69  ? 378 ARG D CD    1 
ATOM   14538 N NE    . ARG D  1 378 ? 41.685  72.299  210.373 1.00 57.15  ? 378 ARG D NE    1 
ATOM   14539 C CZ    . ARG D  1 378 ? 42.914  72.221  209.877 1.00 66.16  ? 378 ARG D CZ    1 
ATOM   14540 N NH1   . ARG D  1 378 ? 43.865  71.599  210.557 1.00 64.80  ? 378 ARG D NH1   1 
ATOM   14541 N NH2   . ARG D  1 378 ? 43.194  72.769  208.703 1.00 60.95  ? 378 ARG D NH2   1 
ATOM   14542 N N     . LEU D  1 379 ? 41.605  71.131  217.158 1.00 58.96  ? 379 LEU D N     1 
ATOM   14543 C CA    . LEU D  1 379 ? 41.059  70.723  218.447 1.00 61.04  ? 379 LEU D CA    1 
ATOM   14544 C C     . LEU D  1 379 ? 41.483  71.734  219.507 1.00 62.32  ? 379 LEU D C     1 
ATOM   14545 O O     . LEU D  1 379 ? 40.641  72.340  220.169 1.00 57.99  ? 379 LEU D O     1 
ATOM   14546 C CB    . LEU D  1 379 ? 41.526  69.307  218.819 1.00 51.41  ? 379 LEU D CB    1 
ATOM   14547 C CG    . LEU D  1 379 ? 40.843  68.627  220.009 1.00 59.15  ? 379 LEU D CG    1 
ATOM   14548 C CD1   . LEU D  1 379 ? 39.343  68.814  219.907 1.00 52.13  ? 379 LEU D CD1   1 
ATOM   14549 C CD2   . LEU D  1 379 ? 41.183  67.136  220.102 1.00 52.24  ? 379 LEU D CD2   1 
ATOM   14550 N N     . SER D  1 380 ? 42.794  71.927  219.627 1.00 57.55  ? 380 SER D N     1 
ATOM   14551 C CA    . SER D  1 380 ? 43.377  72.847  220.599 1.00 65.68  ? 380 SER D CA    1 
ATOM   14552 C C     . SER D  1 380 ? 42.800  74.265  220.533 1.00 65.39  ? 380 SER D C     1 
ATOM   14553 O O     . SER D  1 380 ? 42.805  74.978  221.531 1.00 67.63  ? 380 SER D O     1 
ATOM   14554 C CB    . SER D  1 380 ? 44.896  72.904  220.413 1.00 72.94  ? 380 SER D CB    1 
ATOM   14555 O OG    . SER D  1 380 ? 45.229  73.262  219.083 1.00 72.55  ? 380 SER D OG    1 
ATOM   14556 N N     . LYS D  1 381 ? 42.298  74.668  219.368 1.00 62.31  ? 381 LYS D N     1 
ATOM   14557 C CA    . LYS D  1 381 ? 41.743  76.011  219.195 1.00 60.26  ? 381 LYS D CA    1 
ATOM   14558 C C     . LYS D  1 381 ? 40.287  76.117  219.651 1.00 63.91  ? 381 LYS D C     1 
ATOM   14559 O O     . LYS D  1 381 ? 39.652  77.157  219.478 1.00 66.01  ? 381 LYS D O     1 
ATOM   14560 C CB    . LYS D  1 381 ? 41.838  76.446  217.731 1.00 60.68  ? 381 LYS D CB    1 
ATOM   14561 C CG    . LYS D  1 381 ? 43.241  76.738  217.230 1.00 67.28  ? 381 LYS D CG    1 
ATOM   14562 C CD    . LYS D  1 381 ? 43.240  76.911  215.716 1.00 75.06  ? 381 LYS D CD    1 
ATOM   14563 C CE    . LYS D  1 381 ? 44.533  77.537  215.235 1.00 76.29  ? 381 LYS D CE    1 
ATOM   14564 N NZ    . LYS D  1 381 ? 45.665  77.131  216.107 1.00 81.56  ? 381 LYS D NZ    1 
ATOM   14565 N N     . GLU D  1 382 ? 39.758  75.042  220.225 1.00 64.68  ? 382 GLU D N     1 
ATOM   14566 C CA    . GLU D  1 382 ? 38.346  75.001  220.588 1.00 57.34  ? 382 GLU D CA    1 
ATOM   14567 C C     . GLU D  1 382 ? 38.113  74.175  221.849 1.00 58.33  ? 382 GLU D C     1 
ATOM   14568 O O     . GLU D  1 382 ? 38.054  72.947  221.790 1.00 61.07  ? 382 GLU D O     1 
ATOM   14569 C CB    . GLU D  1 382 ? 37.521  74.444  219.427 1.00 58.06  ? 382 GLU D CB    1 
ATOM   14570 C CG    . GLU D  1 382 ? 36.032  74.340  219.709 1.00 62.87  ? 382 GLU D CG    1 
ATOM   14571 C CD    . GLU D  1 382 ? 35.451  75.632  220.248 1.00 60.32  ? 382 GLU D CD    1 
ATOM   14572 O OE1   . GLU D  1 382 ? 35.269  76.585  219.460 1.00 55.13  ? 382 GLU D OE1   1 
ATOM   14573 O OE2   . GLU D  1 382 ? 35.174  75.691  221.465 1.00 59.24  ? 382 GLU D OE2   1 
ATOM   14574 N N     . PRO D  1 383 ? 37.972  74.857  222.997 1.00 60.70  ? 383 PRO D N     1 
ATOM   14575 C CA    . PRO D  1 383 ? 37.802  74.221  224.308 1.00 65.38  ? 383 PRO D CA    1 
ATOM   14576 C C     . PRO D  1 383 ? 36.557  73.342  224.373 1.00 62.22  ? 383 PRO D C     1 
ATOM   14577 O O     . PRO D  1 383 ? 36.496  72.419  225.187 1.00 58.75  ? 383 PRO D O     1 
ATOM   14578 C CB    . PRO D  1 383 ? 37.676  75.412  225.265 1.00 61.13  ? 383 PRO D CB    1 
ATOM   14579 C CG    . PRO D  1 383 ? 38.294  76.559  224.534 1.00 63.06  ? 383 PRO D CG    1 
ATOM   14580 C CD    . PRO D  1 383 ? 37.953  76.325  223.098 1.00 59.79  ? 383 PRO D CD    1 
ATOM   14581 N N     . ASN D  1 384 ? 35.579  73.629  223.521 1.00 60.72  ? 384 ASN D N     1 
ATOM   14582 C CA    . ASN D  1 384 ? 34.352  72.842  223.476 1.00 64.01  ? 384 ASN D CA    1 
ATOM   14583 C C     . ASN D  1 384 ? 34.402  71.728  222.438 1.00 65.34  ? 384 ASN D C     1 
ATOM   14584 O O     . ASN D  1 384 ? 33.399  71.059  222.186 1.00 61.91  ? 384 ASN D O     1 
ATOM   14585 C CB    . ASN D  1 384 ? 33.152  73.746  223.202 1.00 63.21  ? 384 ASN D CB    1 
ATOM   14586 C CG    . ASN D  1 384 ? 32.811  74.628  224.383 1.00 68.28  ? 384 ASN D CG    1 
ATOM   14587 O OD1   . ASN D  1 384 ? 33.224  75.786  224.448 1.00 74.21  ? 384 ASN D OD1   1 
ATOM   14588 N ND2   . ASN D  1 384 ? 32.057  74.082  225.329 1.00 65.16  ? 384 ASN D ND2   1 
ATOM   14589 N N     . GLY D  1 385 ? 35.570  71.537  221.835 1.00 60.78  ? 385 GLY D N     1 
ATOM   14590 C CA    . GLY D  1 385 ? 35.759  70.478  220.862 1.00 57.21  ? 385 GLY D CA    1 
ATOM   14591 C C     . GLY D  1 385 ? 36.344  69.239  221.509 1.00 57.93  ? 385 GLY D C     1 
ATOM   14592 O O     . GLY D  1 385 ? 37.103  69.328  222.473 1.00 57.97  ? 385 GLY D O     1 
ATOM   14593 N N     . PHE D  1 386 ? 35.978  68.076  220.980 1.00 54.09  ? 386 PHE D N     1 
ATOM   14594 C CA    . PHE D  1 386 ? 36.461  66.801  221.497 1.00 49.11  ? 386 PHE D CA    1 
ATOM   14595 C C     . PHE D  1 386 ? 36.605  65.793  220.362 1.00 51.16  ? 386 PHE D C     1 
ATOM   14596 O O     . PHE D  1 386 ? 36.037  65.979  219.288 1.00 48.81  ? 386 PHE D O     1 
ATOM   14597 C CB    . PHE D  1 386 ? 35.509  66.236  222.559 1.00 53.85  ? 386 PHE D CB    1 
ATOM   14598 C CG    . PHE D  1 386 ? 35.149  67.208  223.648 1.00 60.34  ? 386 PHE D CG    1 
ATOM   14599 C CD1   . PHE D  1 386 ? 35.877  67.243  224.824 1.00 65.27  ? 386 PHE D CD1   1 
ATOM   14600 C CD2   . PHE D  1 386 ? 34.071  68.069  223.508 1.00 63.05  ? 386 PHE D CD2   1 
ATOM   14601 C CE1   . PHE D  1 386 ? 35.549  68.127  225.833 1.00 70.83  ? 386 PHE D CE1   1 
ATOM   14602 C CE2   . PHE D  1 386 ? 33.738  68.957  224.514 1.00 64.60  ? 386 PHE D CE2   1 
ATOM   14603 C CZ    . PHE D  1 386 ? 34.479  68.985  225.679 1.00 64.67  ? 386 PHE D CZ    1 
ATOM   14604 N N     . ILE D  1 387 ? 37.362  64.726  220.600 1.00 51.47  ? 387 ILE D N     1 
ATOM   14605 C CA    . ILE D  1 387 ? 37.394  63.599  219.672 1.00 43.36  ? 387 ILE D CA    1 
ATOM   14606 C C     . ILE D  1 387 ? 37.376  62.272  220.414 1.00 46.88  ? 387 ILE D C     1 
ATOM   14607 O O     . ILE D  1 387 ? 37.809  62.186  221.563 1.00 47.02  ? 387 ILE D O     1 
ATOM   14608 C CB    . ILE D  1 387 ? 38.635  63.623  218.749 1.00 47.61  ? 387 ILE D CB    1 
ATOM   14609 C CG1   . ILE D  1 387 ? 39.931  63.648  219.561 1.00 45.69  ? 387 ILE D CG1   1 
ATOM   14610 C CG2   . ILE D  1 387 ? 38.563  64.785  217.768 1.00 44.07  ? 387 ILE D CG2   1 
ATOM   14611 C CD1   . ILE D  1 387 ? 41.177  63.572  218.703 1.00 45.69  ? 387 ILE D CD1   1 
ATOM   14612 N N     . ALA D  1 388 ? 36.857  61.245  219.753 1.00 47.97  ? 388 ALA D N     1 
ATOM   14613 C CA    . ALA D  1 388 ? 36.928  59.885  220.263 1.00 41.26  ? 388 ALA D CA    1 
ATOM   14614 C C     . ALA D  1 388 ? 37.378  58.970  219.142 1.00 40.23  ? 388 ALA D C     1 
ATOM   14615 O O     . ALA D  1 388 ? 36.879  59.056  218.022 1.00 42.07  ? 388 ALA D O     1 
ATOM   14616 C CB    . ALA D  1 388 ? 35.587  59.435  220.820 1.00 36.86  ? 388 ALA D CB    1 
ATOM   14617 N N     . LEU D  1 389 ? 38.331  58.099  219.444 1.00 41.16  ? 389 LEU D N     1 
ATOM   14618 C CA    . LEU D  1 389 ? 38.905  57.237  218.424 1.00 37.50  ? 389 LEU D CA    1 
ATOM   14619 C C     . LEU D  1 389 ? 38.825  55.772  218.835 1.00 35.16  ? 389 LEU D C     1 
ATOM   14620 O O     . LEU D  1 389 ? 39.112  55.420  219.981 1.00 37.30  ? 389 LEU D O     1 
ATOM   14621 C CB    . LEU D  1 389 ? 40.359  57.625  218.160 1.00 40.40  ? 389 LEU D CB    1 
ATOM   14622 C CG    . LEU D  1 389 ? 40.763  59.100  218.114 1.00 42.19  ? 389 LEU D CG    1 
ATOM   14623 C CD1   . LEU D  1 389 ? 42.280  59.212  218.101 1.00 45.28  ? 389 LEU D CD1   1 
ATOM   14624 C CD2   . LEU D  1 389 ? 40.175  59.797  216.911 1.00 42.66  ? 389 LEU D CD2   1 
ATOM   14625 N N     . ASN D  1 390 ? 38.431  54.920  217.896 1.00 33.67  ? 390 ASN D N     1 
ATOM   14626 C CA    . ASN D  1 390 ? 38.424  53.481  218.126 1.00 36.92  ? 390 ASN D CA    1 
ATOM   14627 C C     . ASN D  1 390 ? 39.068  52.739  216.967 1.00 32.65  ? 390 ASN D C     1 
ATOM   14628 O O     . ASN D  1 390 ? 38.937  53.140  215.811 1.00 36.80  ? 390 ASN D O     1 
ATOM   14629 C CB    . ASN D  1 390 ? 36.999  52.969  218.343 1.00 37.79  ? 390 ASN D CB    1 
ATOM   14630 C CG    . ASN D  1 390 ? 36.495  53.222  219.753 1.00 45.75  ? 390 ASN D CG    1 
ATOM   14631 O OD1   . ASN D  1 390 ? 36.782  52.455  220.674 1.00 45.33  ? 390 ASN D OD1   1 
ATOM   14632 N ND2   . ASN D  1 390 ? 35.727  54.294  219.925 1.00 39.38  ? 390 ASN D ND2   1 
ATOM   14633 N N     . GLY D  1 391 ? 39.772  51.660  217.281 1.00 32.36  ? 391 GLY D N     1 
ATOM   14634 C CA    . GLY D  1 391 ? 40.320  50.808  216.249 1.00 36.96  ? 391 GLY D CA    1 
ATOM   14635 C C     . GLY D  1 391 ? 39.394  49.632  216.040 1.00 34.25  ? 391 GLY D C     1 
ATOM   14636 O O     . GLY D  1 391 ? 38.818  49.116  216.998 1.00 37.03  ? 391 GLY D O     1 
ATOM   14637 N N     . PHE D  1 392 ? 39.225  49.213  214.793 1.00 35.90  ? 392 PHE D N     1 
ATOM   14638 C CA    . PHE D  1 392 ? 38.479  47.991  214.531 1.00 36.16  ? 392 PHE D CA    1 
ATOM   14639 C C     . PHE D  1 392 ? 39.443  46.810  214.560 1.00 32.66  ? 392 PHE D C     1 
ATOM   14640 O O     . PHE D  1 392 ? 40.143  46.601  215.553 1.00 32.46  ? 392 PHE D O     1 
ATOM   14641 C CB    . PHE D  1 392 ? 37.733  48.065  213.196 1.00 33.34  ? 392 PHE D CB    1 
ATOM   14642 C CG    . PHE D  1 392 ? 36.441  48.840  213.260 1.00 36.51  ? 392 PHE D CG    1 
ATOM   14643 C CD1   . PHE D  1 392 ? 36.167  49.672  214.331 1.00 38.60  ? 392 PHE D CD1   1 
ATOM   14644 C CD2   . PHE D  1 392 ? 35.493  48.720  212.254 1.00 35.08  ? 392 PHE D CD2   1 
ATOM   14645 C CE1   . PHE D  1 392 ? 34.982  50.384  214.397 1.00 39.76  ? 392 PHE D CE1   1 
ATOM   14646 C CE2   . PHE D  1 392 ? 34.302  49.428  212.313 1.00 35.32  ? 392 PHE D CE2   1 
ATOM   14647 C CZ    . PHE D  1 392 ? 34.047  50.261  213.386 1.00 35.44  ? 392 PHE D CZ    1 
ATOM   14648 N N     . GLY D  1 393 ? 39.496  46.048  213.474 1.00 35.86  ? 393 GLY D N     1 
ATOM   14649 C CA    . GLY D  1 393 ? 40.310  44.848  213.455 1.00 37.14  ? 393 GLY D CA    1 
ATOM   14650 C C     . GLY D  1 393 ? 39.669  43.796  214.330 1.00 40.31  ? 393 GLY D C     1 
ATOM   14651 O O     . GLY D  1 393 ? 38.498  43.926  214.697 1.00 37.54  ? 393 GLY D O     1 
ATOM   14652 N N     . GLY D  1 394 ? 40.431  42.764  214.680 1.00 30.96  ? 394 GLY D N     1 
ATOM   14653 C CA    . GLY D  1 394 ? 39.902  41.671  215.479 1.00 38.80  ? 394 GLY D CA    1 
ATOM   14654 C C     . GLY D  1 394 ? 38.703  41.021  214.817 1.00 38.11  ? 394 GLY D C     1 
ATOM   14655 O O     . GLY D  1 394 ? 38.738  40.728  213.619 1.00 41.31  ? 394 GLY D O     1 
ATOM   14656 N N     . GLN D  1 395 ? 37.636  40.815  215.585 1.00 44.62  ? 395 GLN D N     1 
ATOM   14657 C CA    . GLN D  1 395 ? 36.422  40.183  215.068 1.00 46.55  ? 395 GLN D CA    1 
ATOM   14658 C C     . GLN D  1 395 ? 35.694  41.042  214.047 1.00 44.77  ? 395 GLN D C     1 
ATOM   14659 O O     . GLN D  1 395 ? 35.012  40.516  213.164 1.00 47.37  ? 395 GLN D O     1 
ATOM   14660 C CB    . GLN D  1 395 ? 35.470  39.848  216.214 1.00 44.88  ? 395 GLN D CB    1 
ATOM   14661 C CG    . GLN D  1 395 ? 35.782  38.539  216.883 1.00 59.55  ? 395 GLN D CG    1 
ATOM   14662 C CD    . GLN D  1 395 ? 35.638  37.361  215.950 1.00 70.82  ? 395 GLN D CD    1 
ATOM   14663 O OE1   . GLN D  1 395 ? 34.643  37.235  215.237 1.00 62.63  ? 395 GLN D OE1   1 
ATOM   14664 N NE2   . GLN D  1 395 ? 36.637  36.490  215.945 1.00 88.35  ? 395 GLN D NE2   1 
ATOM   14665 N N     . MET D  1 396 ? 35.830  42.359  214.174 1.00 42.95  ? 396 MET D N     1 
ATOM   14666 C CA    . MET D  1 396 ? 35.223  43.276  213.225 1.00 39.24  ? 396 MET D CA    1 
ATOM   14667 C C     . MET D  1 396 ? 35.762  43.049  211.812 1.00 46.04  ? 396 MET D C     1 
ATOM   14668 O O     . MET D  1 396 ? 35.101  43.389  210.844 1.00 47.05  ? 396 MET D O     1 
ATOM   14669 C CB    . MET D  1 396 ? 35.450  44.725  213.665 1.00 34.36  ? 396 MET D CB    1 
ATOM   14670 C CG    . MET D  1 396 ? 34.734  45.090  214.953 1.00 30.62  ? 396 MET D CG    1 
ATOM   14671 S SD    . MET D  1 396 ? 32.933  45.019  214.816 1.00 35.77  ? 396 MET D SD    1 
ATOM   14672 C CE    . MET D  1 396 ? 32.634  46.357  213.658 1.00 26.62  ? 396 MET D CE    1 
ATOM   14673 N N     . SER D  1 397 ? 36.948  42.453  211.693 1.00 41.22  ? 397 SER D N     1 
ATOM   14674 C CA    . SER D  1 397 ? 37.485  42.071  210.386 1.00 43.85  ? 397 SER D CA    1 
ATOM   14675 C C     . SER D  1 397 ? 37.043  40.673  209.951 1.00 44.47  ? 397 SER D C     1 
ATOM   14676 O O     . SER D  1 397 ? 37.083  40.354  208.765 1.00 46.48  ? 397 SER D O     1 
ATOM   14677 C CB    . SER D  1 397 ? 39.016  42.141  210.392 1.00 42.88  ? 397 SER D CB    1 
ATOM   14678 O OG    . SER D  1 397 ? 39.470  43.478  210.363 1.00 46.52  ? 397 SER D OG    1 
ATOM   14679 N N     . LYS D  1 398 ? 36.630  39.843  210.906 1.00 44.40  ? 398 LYS D N     1 
ATOM   14680 C CA    . LYS D  1 398 ? 36.241  38.463  210.610 1.00 43.29  ? 398 LYS D CA    1 
ATOM   14681 C C     . LYS D  1 398 ? 34.752  38.288  210.311 1.00 50.50  ? 398 LYS D C     1 
ATOM   14682 O O     . LYS D  1 398 ? 34.337  37.251  209.779 1.00 55.14  ? 398 LYS D O     1 
ATOM   14683 C CB    . LYS D  1 398 ? 36.637  37.548  211.769 1.00 49.32  ? 398 LYS D CB    1 
ATOM   14684 C CG    . LYS D  1 398 ? 38.134  37.317  211.845 1.00 52.57  ? 398 LYS D CG    1 
ATOM   14685 C CD    . LYS D  1 398 ? 38.568  36.862  213.220 1.00 59.16  ? 398 LYS D CD    1 
ATOM   14686 C CE    . LYS D  1 398 ? 40.083  36.786  213.289 1.00 63.99  ? 398 LYS D CE    1 
ATOM   14687 N NZ    . LYS D  1 398 ? 40.560  36.224  214.581 1.00 66.80  ? 398 LYS D NZ    1 
ATOM   14688 N N     . ILE D  1 399 ? 33.953  39.292  210.652 1.00 46.39  ? 399 ILE D N     1 
ATOM   14689 C CA    . ILE D  1 399 ? 32.531  39.262  210.353 1.00 40.67  ? 399 ILE D CA    1 
ATOM   14690 C C     . ILE D  1 399 ? 32.303  39.781  208.934 1.00 40.29  ? 399 ILE D C     1 
ATOM   14691 O O     . ILE D  1 399 ? 32.824  40.839  208.572 1.00 45.01  ? 399 ILE D O     1 
ATOM   14692 C CB    . ILE D  1 399 ? 31.730  40.102  211.373 1.00 43.15  ? 399 ILE D CB    1 
ATOM   14693 C CG1   . ILE D  1 399 ? 31.938  39.552  212.784 1.00 43.17  ? 399 ILE D CG1   1 
ATOM   14694 C CG2   . ILE D  1 399 ? 30.255  40.112  211.008 1.00 38.93  ? 399 ILE D CG2   1 
ATOM   14695 C CD1   . ILE D  1 399 ? 31.520  40.497  213.901 1.00 43.70  ? 399 ILE D CD1   1 
ATOM   14696 N N     . SER D  1 400 ? 31.562  39.022  208.124 1.00 42.84  ? 400 SER D N     1 
ATOM   14697 C CA    . SER D  1 400 ? 31.262  39.430  206.749 1.00 44.42  ? 400 SER D CA    1 
ATOM   14698 C C     . SER D  1 400 ? 30.477  40.742  206.736 1.00 46.38  ? 400 SER D C     1 
ATOM   14699 O O     . SER D  1 400 ? 29.738  41.037  207.681 1.00 47.32  ? 400 SER D O     1 
ATOM   14700 C CB    . SER D  1 400 ? 30.481  38.335  206.015 1.00 47.16  ? 400 SER D CB    1 
ATOM   14701 O OG    . SER D  1 400 ? 29.191  38.149  206.576 1.00 58.23  ? 400 SER D OG    1 
ATOM   14702 N N     . SER D  1 401 ? 30.640  41.531  205.676 1.00 44.35  ? 401 SER D N     1 
ATOM   14703 C CA    . SER D  1 401 ? 30.013  42.849  205.596 1.00 47.33  ? 401 SER D CA    1 
ATOM   14704 C C     . SER D  1 401 ? 28.487  42.767  205.502 1.00 46.55  ? 401 SER D C     1 
ATOM   14705 O O     . SER D  1 401 ? 27.789  43.737  205.818 1.00 43.61  ? 401 SER D O     1 
ATOM   14706 C CB    . SER D  1 401 ? 30.562  43.630  204.397 1.00 48.53  ? 401 SER D CB    1 
ATOM   14707 O OG    . SER D  1 401 ? 30.036  43.130  203.178 1.00 57.02  ? 401 SER D OG    1 
ATOM   14708 N N     . ASP D  1 402 ? 27.974  41.617  205.068 1.00 42.67  ? 402 ASP D N     1 
ATOM   14709 C CA    . ASP D  1 402 ? 26.534  41.454  204.891 1.00 48.98  ? 402 ASP D CA    1 
ATOM   14710 C C     . ASP D  1 402 ? 25.890  40.586  205.974 1.00 41.22  ? 402 ASP D C     1 
ATOM   14711 O O     . ASP D  1 402 ? 24.714  40.240  205.867 1.00 45.16  ? 402 ASP D O     1 
ATOM   14712 C CB    . ASP D  1 402 ? 26.229  40.867  203.504 1.00 52.57  ? 402 ASP D CB    1 
ATOM   14713 C CG    . ASP D  1 402 ? 26.814  39.473  203.304 1.00 52.69  ? 402 ASP D CG    1 
ATOM   14714 O OD1   . ASP D  1 402 ? 27.320  38.865  204.275 1.00 55.21  ? 402 ASP D OD1   1 
ATOM   14715 O OD2   . ASP D  1 402 ? 26.759  38.976  202.161 1.00 58.58  ? 402 ASP D OD2   1 
ATOM   14716 N N     . PHE D  1 403 ? 26.662  40.222  206.997 1.00 41.40  ? 403 PHE D N     1 
ATOM   14717 C CA    . PHE D  1 403 ? 26.128  39.443  208.113 1.00 40.35  ? 403 PHE D CA    1 
ATOM   14718 C C     . PHE D  1 403 ? 24.948  40.173  208.746 1.00 42.77  ? 403 PHE D C     1 
ATOM   14719 O O     . PHE D  1 403 ? 23.893  39.585  208.988 1.00 39.62  ? 403 PHE D O     1 
ATOM   14720 C CB    . PHE D  1 403 ? 27.212  39.166  209.164 1.00 39.07  ? 403 PHE D CB    1 
ATOM   14721 C CG    . PHE D  1 403 ? 26.711  38.408  210.366 1.00 41.58  ? 403 PHE D CG    1 
ATOM   14722 C CD1   . PHE D  1 403 ? 26.204  37.125  210.229 1.00 41.05  ? 403 PHE D CD1   1 
ATOM   14723 C CD2   . PHE D  1 403 ? 26.746  38.977  211.632 1.00 37.50  ? 403 PHE D CD2   1 
ATOM   14724 C CE1   . PHE D  1 403 ? 25.738  36.425  211.329 1.00 45.07  ? 403 PHE D CE1   1 
ATOM   14725 C CE2   . PHE D  1 403 ? 26.281  38.281  212.735 1.00 39.26  ? 403 PHE D CE2   1 
ATOM   14726 C CZ    . PHE D  1 403 ? 25.777  37.004  212.582 1.00 46.98  ? 403 PHE D CZ    1 
ATOM   14727 N N     . THR D  1 404 ? 25.146  41.461  209.009 1.00 40.24  ? 404 THR D N     1 
ATOM   14728 C CA    . THR D  1 404 ? 24.085  42.361  209.450 1.00 38.22  ? 404 THR D CA    1 
ATOM   14729 C C     . THR D  1 404 ? 24.244  43.665  208.652 1.00 39.35  ? 404 THR D C     1 
ATOM   14730 O O     . THR D  1 404 ? 25.258  43.838  207.979 1.00 45.62  ? 404 THR D O     1 
ATOM   14731 C CB    . THR D  1 404 ? 24.145  42.613  210.978 1.00 38.56  ? 404 THR D CB    1 
ATOM   14732 O OG1   . THR D  1 404 ? 25.480  42.960  211.363 1.00 40.72  ? 404 THR D OG1   1 
ATOM   14733 C CG2   . THR D  1 404 ? 23.714  41.370  211.746 1.00 38.88  ? 404 THR D CG2   1 
ATOM   14734 N N     . PRO D  1 405 ? 23.246  44.571  208.694 1.00 35.68  ? 405 PRO D N     1 
ATOM   14735 C CA    . PRO D  1 405 ? 23.338  45.797  207.887 1.00 33.88  ? 405 PRO D CA    1 
ATOM   14736 C C     . PRO D  1 405 ? 24.598  46.654  208.077 1.00 38.09  ? 405 PRO D C     1 
ATOM   14737 O O     . PRO D  1 405 ? 24.964  47.365  207.141 1.00 36.72  ? 405 PRO D O     1 
ATOM   14738 C CB    . PRO D  1 405 ? 22.103  46.581  208.328 1.00 35.24  ? 405 PRO D CB    1 
ATOM   14739 C CG    . PRO D  1 405 ? 21.108  45.525  208.617 1.00 34.04  ? 405 PRO D CG    1 
ATOM   14740 C CD    . PRO D  1 405 ? 21.895  44.413  209.264 1.00 35.47  ? 405 PRO D CD    1 
ATOM   14741 N N     . PHE D  1 406 ? 25.237  46.604  209.242 1.00 38.61  ? 406 PHE D N     1 
ATOM   14742 C CA    . PHE D  1 406 ? 26.478  47.351  209.454 1.00 36.86  ? 406 PHE D CA    1 
ATOM   14743 C C     . PHE D  1 406 ? 27.594  46.751  208.607 1.00 36.97  ? 406 PHE D C     1 
ATOM   14744 O O     . PHE D  1 406 ? 28.038  45.633  208.865 1.00 33.67  ? 406 PHE D O     1 
ATOM   14745 C CB    . PHE D  1 406 ? 26.862  47.354  210.935 1.00 32.87  ? 406 PHE D CB    1 
ATOM   14746 C CG    . PHE D  1 406 ? 28.082  48.179  211.254 1.00 37.18  ? 406 PHE D CG    1 
ATOM   14747 C CD1   . PHE D  1 406 ? 27.961  49.516  211.597 1.00 35.92  ? 406 PHE D CD1   1 
ATOM   14748 C CD2   . PHE D  1 406 ? 29.347  47.611  211.235 1.00 33.59  ? 406 PHE D CD2   1 
ATOM   14749 C CE1   . PHE D  1 406 ? 29.080  50.274  211.901 1.00 34.87  ? 406 PHE D CE1   1 
ATOM   14750 C CE2   . PHE D  1 406 ? 30.468  48.362  211.537 1.00 34.25  ? 406 PHE D CE2   1 
ATOM   14751 C CZ    . PHE D  1 406 ? 30.334  49.696  211.870 1.00 32.58  ? 406 PHE D CZ    1 
ATOM   14752 N N     . PRO D  1 407 ? 28.053  47.502  207.594 1.00 36.40  ? 407 PRO D N     1 
ATOM   14753 C CA    . PRO D  1 407 ? 28.924  46.972  206.543 1.00 35.93  ? 407 PRO D CA    1 
ATOM   14754 C C     . PRO D  1 407 ? 30.418  47.186  206.765 1.00 35.34  ? 407 PRO D C     1 
ATOM   14755 O O     . PRO D  1 407 ? 31.213  46.649  205.999 1.00 41.11  ? 407 PRO D O     1 
ATOM   14756 C CB    . PRO D  1 407 ? 28.469  47.759  205.319 1.00 39.37  ? 407 PRO D CB    1 
ATOM   14757 C CG    . PRO D  1 407 ? 28.155  49.114  205.889 1.00 37.70  ? 407 PRO D CG    1 
ATOM   14758 C CD    . PRO D  1 407 ? 27.666  48.896  207.314 1.00 37.31  ? 407 PRO D CD    1 
ATOM   14759 N N     . HIS D  1 408 ? 30.794  47.956  207.778 1.00 38.43  ? 408 HIS D N     1 
ATOM   14760 C CA    . HIS D  1 408 ? 32.190  48.355  207.926 1.00 37.25  ? 408 HIS D CA    1 
ATOM   14761 C C     . HIS D  1 408 ? 32.987  47.343  208.728 1.00 32.84  ? 408 HIS D C     1 
ATOM   14762 O O     . HIS D  1 408 ? 33.221  47.503  209.927 1.00 36.47  ? 408 HIS D O     1 
ATOM   14763 C CB    . HIS D  1 408 ? 32.261  49.736  208.555 1.00 31.27  ? 408 HIS D CB    1 
ATOM   14764 C CG    . HIS D  1 408 ? 31.389  50.731  207.862 1.00 34.19  ? 408 HIS D CG    1 
ATOM   14765 N ND1   . HIS D  1 408 ? 30.448  51.489  208.523 1.00 43.24  ? 408 HIS D ND1   1 
ATOM   14766 C CD2   . HIS D  1 408 ? 31.289  51.064  206.552 1.00 33.77  ? 408 HIS D CD2   1 
ATOM   14767 C CE1   . HIS D  1 408 ? 29.816  52.257  207.653 1.00 35.54  ? 408 HIS D CE1   1 
ATOM   14768 N NE2   . HIS D  1 408 ? 30.312  52.022  206.452 1.00 40.83  ? 408 HIS D NE2   1 
ATOM   14769 N N     . ARG D  1 409 ? 33.407  46.294  208.032 1.00 31.26  ? 409 ARG D N     1 
ATOM   14770 C CA    . ARG D  1 409 ? 34.109  45.196  208.657 1.00 35.69  ? 409 ARG D CA    1 
ATOM   14771 C C     . ARG D  1 409 ? 35.558  45.146  208.166 1.00 39.22  ? 409 ARG D C     1 
ATOM   14772 O O     . ARG D  1 409 ? 36.346  46.039  208.477 1.00 40.13  ? 409 ARG D O     1 
ATOM   14773 C CB    . ARG D  1 409 ? 33.377  43.883  208.374 1.00 36.33  ? 409 ARG D CB    1 
ATOM   14774 C CG    . ARG D  1 409 ? 31.872  43.913  208.693 1.00 40.25  ? 409 ARG D CG    1 
ATOM   14775 C CD    . ARG D  1 409 ? 31.582  44.082  210.188 1.00 35.95  ? 409 ARG D CD    1 
ATOM   14776 N NE    . ARG D  1 409 ? 30.155  43.952  210.483 1.00 37.53  ? 409 ARG D NE    1 
ATOM   14777 C CZ    . ARG D  1 409 ? 29.647  43.754  211.697 1.00 37.10  ? 409 ARG D CZ    1 
ATOM   14778 N NH1   . ARG D  1 409 ? 30.445  43.661  212.753 1.00 33.92  ? 409 ARG D NH1   1 
ATOM   14779 N NH2   . ARG D  1 409 ? 28.336  43.639  211.856 1.00 36.36  ? 409 ARG D NH2   1 
ATOM   14780 N N     . SER D  1 410 ? 35.906  44.114  207.402 1.00 42.46  ? 410 SER D N     1 
ATOM   14781 C CA    . SER D  1 410 ? 37.263  43.977  206.875 1.00 40.78  ? 410 SER D CA    1 
ATOM   14782 C C     . SER D  1 410 ? 37.634  45.186  206.025 1.00 37.43  ? 410 SER D C     1 
ATOM   14783 O O     . SER D  1 410 ? 36.836  45.650  205.211 1.00 42.19  ? 410 SER D O     1 
ATOM   14784 C CB    . SER D  1 410 ? 37.403  42.692  206.055 1.00 44.66  ? 410 SER D CB    1 
ATOM   14785 O OG    . SER D  1 410 ? 38.697  42.591  205.483 1.00 54.12  ? 410 SER D OG    1 
ATOM   14786 N N     . GLY D  1 411 ? 38.841  45.704  206.227 1.00 40.83  ? 411 GLY D N     1 
ATOM   14787 C CA    . GLY D  1 411 ? 39.289  46.875  205.498 1.00 39.33  ? 411 GLY D CA    1 
ATOM   14788 C C     . GLY D  1 411 ? 39.084  48.165  206.269 1.00 45.46  ? 411 GLY D C     1 
ATOM   14789 O O     . GLY D  1 411 ? 39.672  49.194  205.941 1.00 50.05  ? 411 GLY D O     1 
ATOM   14790 N N     . THR D  1 412 ? 38.247  48.110  207.300 1.00 41.94  ? 412 THR D N     1 
ATOM   14791 C CA    . THR D  1 412 ? 37.994  49.271  208.142 1.00 38.43  ? 412 THR D CA    1 
ATOM   14792 C C     . THR D  1 412 ? 38.990  49.287  209.293 1.00 41.02  ? 412 THR D C     1 
ATOM   14793 O O     . THR D  1 412 ? 39.141  48.293  209.998 1.00 35.21  ? 412 THR D O     1 
ATOM   14794 C CB    . THR D  1 412 ? 36.559  49.270  208.701 1.00 37.33  ? 412 THR D CB    1 
ATOM   14795 O OG1   . THR D  1 412 ? 35.628  49.012  207.642 1.00 40.36  ? 412 THR D OG1   1 
ATOM   14796 C CG2   . THR D  1 412 ? 36.237  50.608  209.335 1.00 36.86  ? 412 THR D CG2   1 
ATOM   14797 N N     . ARG D  1 413 ? 39.672  50.413  209.477 1.00 36.42  ? 413 ARG D N     1 
ATOM   14798 C CA    . ARG D  1 413 ? 40.713  50.510  210.493 1.00 34.54  ? 413 ARG D CA    1 
ATOM   14799 C C     . ARG D  1 413 ? 40.247  51.257  211.731 1.00 33.08  ? 413 ARG D C     1 
ATOM   14800 O O     . ARG D  1 413 ? 40.374  50.761  212.851 1.00 33.03  ? 413 ARG D O     1 
ATOM   14801 C CB    . ARG D  1 413 ? 41.955  51.202  209.928 1.00 43.17  ? 413 ARG D CB    1 
ATOM   14802 C CG    . ARG D  1 413 ? 42.590  50.495  208.752 1.00 46.07  ? 413 ARG D CG    1 
ATOM   14803 C CD    . ARG D  1 413 ? 43.864  51.206  208.340 1.00 50.13  ? 413 ARG D CD    1 
ATOM   14804 N NE    . ARG D  1 413 ? 44.414  50.691  207.090 1.00 48.75  ? 413 ARG D NE    1 
ATOM   14805 C CZ    . ARG D  1 413 ? 45.359  49.759  207.016 1.00 53.74  ? 413 ARG D CZ    1 
ATOM   14806 N NH1   . ARG D  1 413 ? 45.799  49.354  205.832 1.00 53.93  ? 413 ARG D NH1   1 
ATOM   14807 N NH2   . ARG D  1 413 ? 45.865  49.232  208.123 1.00 51.81  ? 413 ARG D NH2   1 
ATOM   14808 N N     . LEU D  1 414 ? 39.720  52.459  211.529 1.00 32.72  ? 414 LEU D N     1 
ATOM   14809 C CA    . LEU D  1 414 ? 39.374  53.325  212.648 1.00 34.71  ? 414 LEU D CA    1 
ATOM   14810 C C     . LEU D  1 414 ? 37.976  53.911  212.531 1.00 37.35  ? 414 LEU D C     1 
ATOM   14811 O O     . LEU D  1 414 ? 37.460  54.114  211.432 1.00 31.57  ? 414 LEU D O     1 
ATOM   14812 C CB    . LEU D  1 414 ? 40.377  54.477  212.768 1.00 34.81  ? 414 LEU D CB    1 
ATOM   14813 C CG    . LEU D  1 414 ? 41.879  54.196  212.681 1.00 35.65  ? 414 LEU D CG    1 
ATOM   14814 C CD1   . LEU D  1 414 ? 42.642  55.513  212.628 1.00 41.06  ? 414 LEU D CD1   1 
ATOM   14815 C CD2   . LEU D  1 414 ? 42.352  53.350  213.847 1.00 30.50  ? 414 LEU D CD2   1 
ATOM   14816 N N     . MET D  1 415 ? 37.372  54.191  213.678 1.00 32.29  ? 415 MET D N     1 
ATOM   14817 C CA    . MET D  1 415 ? 36.200  55.047  213.730 1.00 34.57  ? 415 MET D CA    1 
ATOM   14818 C C     . MET D  1 415 ? 36.598  56.316  214.463 1.00 35.29  ? 415 MET D C     1 
ATOM   14819 O O     . MET D  1 415 ? 37.107  56.258  215.581 1.00 38.61  ? 415 MET D O     1 
ATOM   14820 C CB    . MET D  1 415 ? 35.023  54.359  214.426 1.00 31.80  ? 415 MET D CB    1 
ATOM   14821 C CG    . MET D  1 415 ? 33.743  55.187  214.406 1.00 35.54  ? 415 MET D CG    1 
ATOM   14822 S SD    . MET D  1 415 ? 32.272  54.298  214.950 1.00 45.93  ? 415 MET D SD    1 
ATOM   14823 C CE    . MET D  1 415 ? 32.633  54.093  216.691 1.00 41.22  ? 415 MET D CE    1 
ATOM   14824 N N     . VAL D  1 416 ? 36.389  57.460  213.822 1.00 39.34  ? 416 VAL D N     1 
ATOM   14825 C CA    . VAL D  1 416 ? 36.796  58.738  214.393 1.00 35.41  ? 416 VAL D CA    1 
ATOM   14826 C C     . VAL D  1 416 ? 35.600  59.652  214.634 1.00 35.93  ? 416 VAL D C     1 
ATOM   14827 O O     . VAL D  1 416 ? 34.945  60.090  213.691 1.00 35.53  ? 416 VAL D O     1 
ATOM   14828 C CB    . VAL D  1 416 ? 37.804  59.458  213.482 1.00 39.96  ? 416 VAL D CB    1 
ATOM   14829 C CG1   . VAL D  1 416 ? 38.224  60.773  214.105 1.00 41.73  ? 416 VAL D CG1   1 
ATOM   14830 C CG2   . VAL D  1 416 ? 39.014  58.574  213.222 1.00 39.49  ? 416 VAL D CG2   1 
ATOM   14831 N N     . GLU D  1 417 ? 35.324  59.941  215.902 1.00 34.75  ? 417 GLU D N     1 
ATOM   14832 C CA    . GLU D  1 417 ? 34.206  60.807  216.260 1.00 36.32  ? 417 GLU D CA    1 
ATOM   14833 C C     . GLU D  1 417 ? 34.677  62.238  216.509 1.00 45.09  ? 417 GLU D C     1 
ATOM   14834 O O     . GLU D  1 417 ? 35.662  62.458  217.210 1.00 42.67  ? 417 GLU D O     1 
ATOM   14835 C CB    . GLU D  1 417 ? 33.489  60.270  217.500 1.00 40.60  ? 417 GLU D CB    1 
ATOM   14836 C CG    . GLU D  1 417 ? 33.044  58.819  217.381 1.00 44.17  ? 417 GLU D CG    1 
ATOM   14837 C CD    . GLU D  1 417 ? 32.479  58.276  218.679 1.00 45.05  ? 417 GLU D CD    1 
ATOM   14838 O OE1   . GLU D  1 417 ? 31.524  58.880  219.213 1.00 45.39  ? 417 GLU D OE1   1 
ATOM   14839 O OE2   . GLU D  1 417 ? 32.989  57.245  219.166 1.00 41.63  ? 417 GLU D OE2   1 
ATOM   14840 N N     . TYR D  1 418 ? 33.978  63.205  215.924 1.00 42.64  ? 418 TYR D N     1 
ATOM   14841 C CA    . TYR D  1 418 ? 34.241  64.613  216.200 1.00 43.74  ? 418 TYR D CA    1 
ATOM   14842 C C     . TYR D  1 418 ? 33.050  65.232  216.923 1.00 50.68  ? 418 TYR D C     1 
ATOM   14843 O O     . TYR D  1 418 ? 31.976  65.382  216.346 1.00 47.72  ? 418 TYR D O     1 
ATOM   14844 C CB    . TYR D  1 418 ? 34.525  65.389  214.912 1.00 43.35  ? 418 TYR D CB    1 
ATOM   14845 C CG    . TYR D  1 418 ? 35.338  64.643  213.879 1.00 43.94  ? 418 TYR D CG    1 
ATOM   14846 C CD1   . TYR D  1 418 ? 36.725  64.595  213.953 1.00 42.28  ? 418 TYR D CD1   1 
ATOM   14847 C CD2   . TYR D  1 418 ? 34.717  64.002  212.816 1.00 44.84  ? 418 TYR D CD2   1 
ATOM   14848 C CE1   . TYR D  1 418 ? 37.470  63.920  212.997 1.00 45.30  ? 418 TYR D CE1   1 
ATOM   14849 C CE2   . TYR D  1 418 ? 35.450  63.325  211.860 1.00 44.56  ? 418 TYR D CE2   1 
ATOM   14850 C CZ    . TYR D  1 418 ? 36.826  63.284  211.953 1.00 45.32  ? 418 TYR D CZ    1 
ATOM   14851 O OH    . TYR D  1 418 ? 37.555  62.607  210.997 1.00 44.36  ? 418 TYR D OH    1 
ATOM   14852 N N     . ILE D  1 419 ? 33.241  65.596  218.185 1.00 55.02  ? 419 ILE D N     1 
ATOM   14853 C CA    . ILE D  1 419 ? 32.143  66.117  218.990 1.00 54.72  ? 419 ILE D CA    1 
ATOM   14854 C C     . ILE D  1 419 ? 32.385  67.556  219.429 1.00 57.51  ? 419 ILE D C     1 
ATOM   14855 O O     . ILE D  1 419 ? 33.504  67.923  219.787 1.00 49.80  ? 419 ILE D O     1 
ATOM   14856 C CB    . ILE D  1 419 ? 31.918  65.249  220.241 1.00 53.41  ? 419 ILE D CB    1 
ATOM   14857 C CG1   . ILE D  1 419 ? 31.960  63.765  219.866 1.00 56.50  ? 419 ILE D CG1   1 
ATOM   14858 C CG2   . ILE D  1 419 ? 30.601  65.613  220.919 1.00 52.41  ? 419 ILE D CG2   1 
ATOM   14859 C CD1   . ILE D  1 419 ? 32.116  62.835  221.051 1.00 52.91  ? 419 ILE D CD1   1 
ATOM   14860 N N     . VAL D  1 420 ? 31.339  68.374  219.380 1.00 58.15  ? 420 VAL D N     1 
ATOM   14861 C CA    . VAL D  1 420 ? 31.376  69.676  220.029 1.00 59.57  ? 420 VAL D CA    1 
ATOM   14862 C C     . VAL D  1 420 ? 30.159  69.785  220.950 1.00 60.39  ? 420 VAL D C     1 
ATOM   14863 O O     . VAL D  1 420 ? 29.021  69.575  220.531 1.00 58.98  ? 420 VAL D O     1 
ATOM   14864 C CB    . VAL D  1 420 ? 31.427  70.848  219.006 1.00 60.38  ? 420 VAL D CB    1 
ATOM   14865 C CG1   . VAL D  1 420 ? 30.202  70.862  218.095 1.00 57.93  ? 420 VAL D CG1   1 
ATOM   14866 C CG2   . VAL D  1 420 ? 31.591  72.177  219.729 1.00 65.48  ? 420 VAL D CG2   1 
ATOM   14867 N N     . ALA D  1 421 ? 30.415  70.061  222.223 1.00 62.21  ? 421 ALA D N     1 
ATOM   14868 C CA    . ALA D  1 421 ? 29.351  70.140  223.214 1.00 59.54  ? 421 ALA D CA    1 
ATOM   14869 C C     . ALA D  1 421 ? 29.419  71.463  223.953 1.00 67.66  ? 421 ALA D C     1 
ATOM   14870 O O     . ALA D  1 421 ? 30.492  72.052  224.096 1.00 70.06  ? 421 ALA D O     1 
ATOM   14871 C CB    . ALA D  1 421 ? 29.441  68.977  224.194 1.00 61.99  ? 421 ALA D CB    1 
ATOM   14872 N N     . TRP D  1 422 ? 28.270  71.927  224.428 1.00 70.65  ? 422 TRP D N     1 
ATOM   14873 C CA    . TRP D  1 422 ? 28.226  73.174  225.170 1.00 77.07  ? 422 TRP D CA    1 
ATOM   14874 C C     . TRP D  1 422 ? 27.015  73.232  226.084 1.00 77.34  ? 422 TRP D C     1 
ATOM   14875 O O     . TRP D  1 422 ? 25.902  72.888  225.677 1.00 75.43  ? 422 TRP D O     1 
ATOM   14876 C CB    . TRP D  1 422 ? 28.226  74.365  224.209 1.00 76.38  ? 422 TRP D CB    1 
ATOM   14877 C CG    . TRP D  1 422 ? 26.995  74.494  223.357 1.00 75.15  ? 422 TRP D CG    1 
ATOM   14878 C CD1   . TRP D  1 422 ? 25.889  75.244  223.629 1.00 79.85  ? 422 TRP D CD1   1 
ATOM   14879 C CD2   . TRP D  1 422 ? 26.757  73.879  222.081 1.00 74.47  ? 422 TRP D CD2   1 
ATOM   14880 N NE1   . TRP D  1 422 ? 24.975  75.129  222.609 1.00 78.57  ? 422 TRP D NE1   1 
ATOM   14881 C CE2   . TRP D  1 422 ? 25.483  74.296  221.647 1.00 76.69  ? 422 TRP D CE2   1 
ATOM   14882 C CE3   . TRP D  1 422 ? 27.494  73.011  221.270 1.00 68.94  ? 422 TRP D CE3   1 
ATOM   14883 C CZ2   . TRP D  1 422 ? 24.930  73.876  220.437 1.00 70.98  ? 422 TRP D CZ2   1 
ATOM   14884 C CZ3   . TRP D  1 422 ? 26.941  72.595  220.066 1.00 66.10  ? 422 TRP D CZ3   1 
ATOM   14885 C CH2   . TRP D  1 422 ? 25.672  73.028  219.663 1.00 67.87  ? 422 TRP D CH2   1 
ATOM   14886 N N     . ASN D  1 423 ? 27.235  73.651  227.329 1.00 82.29  ? 423 ASN D N     1 
ATOM   14887 C CA    . ASN D  1 423 ? 26.121  74.012  228.196 1.00 87.43  ? 423 ASN D CA    1 
ATOM   14888 C C     . ASN D  1 423 ? 25.466  75.262  227.629 1.00 85.61  ? 423 ASN D C     1 
ATOM   14889 O O     . ASN D  1 423 ? 25.875  75.755  226.578 1.00 83.95  ? 423 ASN D O     1 
ATOM   14890 C CB    . ASN D  1 423 ? 26.580  74.241  229.649 1.00 89.91  ? 423 ASN D CB    1 
ATOM   14891 C CG    . ASN D  1 423 ? 27.778  75.188  229.760 1.00 96.12  ? 423 ASN D CG    1 
ATOM   14892 O OD1   . ASN D  1 423 ? 27.855  76.206  229.074 1.00 95.03  ? 423 ASN D OD1   1 
ATOM   14893 N ND2   . ASN D  1 423 ? 28.723  74.842  230.631 1.00 97.23  ? 423 ASN D ND2   1 
ATOM   14894 N N     . GLN D  1 424 ? 24.463  75.782  228.325 1.00 89.97  ? 424 GLN D N     1 
ATOM   14895 C CA    . GLN D  1 424 ? 23.890  77.087  228.001 1.00 94.46  ? 424 GLN D CA    1 
ATOM   14896 C C     . GLN D  1 424 ? 24.953  78.208  228.081 1.00 94.52  ? 424 GLN D C     1 
ATOM   14897 O O     . GLN D  1 424 ? 26.141  77.946  227.910 1.00 100.72 ? 424 GLN D O     1 
ATOM   14898 C CB    . GLN D  1 424 ? 22.706  77.384  228.929 1.00 93.70  ? 424 GLN D CB    1 
ATOM   14899 C CG    . GLN D  1 424 ? 23.044  77.624  230.405 1.00 97.53  ? 424 GLN D CG    1 
ATOM   14900 C CD    . GLN D  1 424 ? 23.915  76.540  231.023 1.00 100.28 ? 424 GLN D CD    1 
ATOM   14901 O OE1   . GLN D  1 424 ? 23.822  75.363  230.667 1.00 100.69 ? 424 GLN D OE1   1 
ATOM   14902 N NE2   . GLN D  1 424 ? 24.779  76.941  231.949 1.00 105.90 ? 424 GLN D NE2   1 
ATOM   14903 N N     . SER D  1 425 ? 24.551  79.455  228.326 1.00 92.32  ? 425 SER D N     1 
ATOM   14904 C CA    . SER D  1 425 ? 25.503  80.582  228.361 1.00 89.95  ? 425 SER D CA    1 
ATOM   14905 C C     . SER D  1 425 ? 26.343  80.684  227.072 1.00 87.60  ? 425 SER D C     1 
ATOM   14906 O O     . SER D  1 425 ? 26.304  81.700  226.379 1.00 85.53  ? 425 SER D O     1 
ATOM   14907 C CB    . SER D  1 425 ? 26.426  80.484  229.585 1.00 84.96  ? 425 SER D CB    1 
ATOM   14908 O OG    . SER D  1 425 ? 26.074  79.398  230.425 1.00 84.66  ? 425 SER D OG    1 
ATOM   14909 N N     . GLU D  1 426 ? 27.087  79.624  226.758 1.00 87.93  ? 426 GLU D N     1 
ATOM   14910 C CA    . GLU D  1 426 ? 27.819  79.486  225.499 1.00 82.87  ? 426 GLU D CA    1 
ATOM   14911 C C     . GLU D  1 426 ? 26.894  79.308  224.280 1.00 83.18  ? 426 GLU D C     1 
ATOM   14912 O O     . GLU D  1 426 ? 27.369  79.205  223.144 1.00 80.46  ? 426 GLU D O     1 
ATOM   14913 C CB    . GLU D  1 426 ? 28.781  78.293  225.598 1.00 80.58  ? 426 GLU D CB    1 
ATOM   14914 C CG    . GLU D  1 426 ? 29.364  78.097  226.994 1.00 87.08  ? 426 GLU D CG    1 
ATOM   14915 C CD    . GLU D  1 426 ? 30.228  76.852  227.119 1.00 86.33  ? 426 GLU D CD    1 
ATOM   14916 O OE1   . GLU D  1 426 ? 29.739  75.740  226.831 1.00 84.88  ? 426 GLU D OE1   1 
ATOM   14917 O OE2   . GLU D  1 426 ? 31.402  76.990  227.516 1.00 85.43  ? 426 GLU D OE2   1 
ATOM   14918 N N     . GLN D  1 427 ? 25.583  79.273  224.520 1.00 85.28  ? 427 GLN D N     1 
ATOM   14919 C CA    . GLN D  1 427 ? 24.593  79.008  223.471 1.00 87.33  ? 427 GLN D CA    1 
ATOM   14920 C C     . GLN D  1 427 ? 24.554  80.072  222.360 1.00 84.54  ? 427 GLN D C     1 
ATOM   14921 O O     . GLN D  1 427 ? 24.061  79.809  221.261 1.00 85.43  ? 427 GLN D O     1 
ATOM   14922 C CB    . GLN D  1 427 ? 23.201  78.861  224.102 1.00 91.42  ? 427 GLN D CB    1 
ATOM   14923 C CG    . GLN D  1 427 ? 22.136  78.264  223.180 1.00 98.51  ? 427 GLN D CG    1 
ATOM   14924 C CD    . GLN D  1 427 ? 21.381  77.114  223.822 1.00 111.21 ? 427 GLN D CD    1 
ATOM   14925 O OE1   . GLN D  1 427 ? 21.457  75.976  223.358 1.00 124.45 ? 427 GLN D OE1   1 
ATOM   14926 N NE2   . GLN D  1 427 ? 20.647  77.406  224.891 1.00 108.60 ? 427 GLN D NE2   1 
ATOM   14927 N N     . LYS D  1 428 ? 25.065  81.268  222.639 1.00 85.76  ? 428 LYS D N     1 
ATOM   14928 C CA    . LYS D  1 428 ? 25.187  82.285  221.593 1.00 87.69  ? 428 LYS D CA    1 
ATOM   14929 C C     . LYS D  1 428 ? 26.231  81.867  220.559 1.00 87.49  ? 428 LYS D C     1 
ATOM   14930 O O     . LYS D  1 428 ? 26.036  82.050  219.358 1.00 86.54  ? 428 LYS D O     1 
ATOM   14931 C CB    . LYS D  1 428 ? 25.559  83.651  222.175 1.00 92.80  ? 428 LYS D CB    1 
ATOM   14932 C CG    . LYS D  1 428 ? 25.709  84.739  221.116 1.00 101.86 ? 428 LYS D CG    1 
ATOM   14933 C CD    . LYS D  1 428 ? 26.635  85.846  221.584 1.00 109.65 ? 428 LYS D CD    1 
ATOM   14934 C CE    . LYS D  1 428 ? 27.886  85.916  220.724 1.00 108.71 ? 428 LYS D CE    1 
ATOM   14935 N NZ    . LYS D  1 428 ? 28.772  87.048  221.113 1.00 102.10 ? 428 LYS D NZ    1 
ATOM   14936 N N     . LYS D  1 429 ? 27.331  81.289  221.034 1.00 85.83  ? 429 LYS D N     1 
ATOM   14937 C CA    . LYS D  1 429 ? 28.409  80.841  220.155 1.00 80.85  ? 429 LYS D CA    1 
ATOM   14938 C C     . LYS D  1 429 ? 28.031  79.620  219.301 1.00 77.80  ? 429 LYS D C     1 
ATOM   14939 O O     . LYS D  1 429 ? 28.839  79.167  218.504 1.00 72.33  ? 429 LYS D O     1 
ATOM   14940 C CB    . LYS D  1 429 ? 29.668  80.524  220.975 1.00 79.55  ? 429 LYS D CB    1 
ATOM   14941 C CG    . LYS D  1 429 ? 30.385  81.745  221.546 1.00 79.54  ? 429 LYS D CG    1 
ATOM   14942 C CD    . LYS D  1 429 ? 31.775  81.383  222.068 1.00 80.14  ? 429 LYS D CD    1 
ATOM   14943 C CE    . LYS D  1 429 ? 31.708  80.581  223.360 1.00 79.61  ? 429 LYS D CE    1 
ATOM   14944 N NZ    . LYS D  1 429 ? 32.999  79.884  223.633 1.00 72.86  ? 429 LYS D NZ    1 
ATOM   14945 N N     . LYS D  1 430 ? 26.813  79.103  219.461 1.00 78.04  ? 430 LYS D N     1 
ATOM   14946 C CA    . LYS D  1 430 ? 26.352  77.905  218.743 1.00 73.18  ? 430 LYS D CA    1 
ATOM   14947 C C     . LYS D  1 430 ? 26.812  77.803  217.277 1.00 69.93  ? 430 LYS D C     1 
ATOM   14948 O O     . LYS D  1 430 ? 27.340  76.771  216.857 1.00 67.06  ? 430 LYS D O     1 
ATOM   14949 C CB    . LYS D  1 430 ? 24.827  77.834  218.796 1.00 77.78  ? 430 LYS D CB    1 
ATOM   14950 C CG    . LYS D  1 430 ? 24.246  76.712  217.964 1.00 76.14  ? 430 LYS D CG    1 
ATOM   14951 C CD    . LYS D  1 430 ? 22.824  76.392  218.380 1.00 81.97  ? 430 LYS D CD    1 
ATOM   14952 C CE    . LYS D  1 430 ? 21.858  76.643  217.240 1.00 81.93  ? 430 LYS D CE    1 
ATOM   14953 N NZ    . LYS D  1 430 ? 22.290  75.920  216.015 1.00 79.91  ? 430 LYS D NZ    1 
ATOM   14954 N N     . THR D  1 431 ? 26.620  78.879  216.517 1.00 68.48  ? 431 THR D N     1 
ATOM   14955 C CA    . THR D  1 431 ? 27.054  78.951  215.119 1.00 67.14  ? 431 THR D CA    1 
ATOM   14956 C C     . THR D  1 431 ? 28.576  78.788  214.979 1.00 68.27  ? 431 THR D C     1 
ATOM   14957 O O     . THR D  1 431 ? 29.063  78.199  214.014 1.00 65.66  ? 431 THR D O     1 
ATOM   14958 C CB    . THR D  1 431 ? 26.613  80.288  214.473 1.00 66.44  ? 431 THR D CB    1 
ATOM   14959 O OG1   . THR D  1 431 ? 25.234  80.531  214.779 1.00 74.92  ? 431 THR D OG1   1 
ATOM   14960 C CG2   . THR D  1 431 ? 26.799  80.255  212.960 1.00 59.32  ? 431 THR D CG2   1 
ATOM   14961 N N     . GLU D  1 432 ? 29.319  79.297  215.956 1.00 68.17  ? 432 GLU D N     1 
ATOM   14962 C CA    . GLU D  1 432 ? 30.774  79.131  216.026 1.00 71.70  ? 432 GLU D CA    1 
ATOM   14963 C C     . GLU D  1 432 ? 31.160  77.660  216.197 1.00 67.17  ? 432 GLU D C     1 
ATOM   14964 O O     . GLU D  1 432 ? 31.924  77.118  215.397 1.00 63.65  ? 432 GLU D O     1 
ATOM   14965 C CB    . GLU D  1 432 ? 31.324  79.972  217.183 1.00 76.30  ? 432 GLU D CB    1 
ATOM   14966 C CG    . GLU D  1 432 ? 32.806  80.274  217.203 1.00 85.07  ? 432 GLU D CG    1 
ATOM   14967 C CD    . GLU D  1 432 ? 33.139  81.237  218.331 1.00 87.43  ? 432 GLU D CD    1 
ATOM   14968 O OE1   . GLU D  1 432 ? 32.907  82.453  218.161 1.00 91.94  ? 432 GLU D OE1   1 
ATOM   14969 O OE2   . GLU D  1 432 ? 33.593  80.775  219.398 1.00 100.67 ? 432 GLU D OE2   1 
ATOM   14970 N N     . PHE D  1 433 ? 30.634  77.031  217.248 1.00 64.99  ? 433 PHE D N     1 
ATOM   14971 C CA    . PHE D  1 433 ? 30.855  75.610  217.524 1.00 65.34  ? 433 PHE D CA    1 
ATOM   14972 C C     . PHE D  1 433 ? 30.622  74.718  216.309 1.00 63.48  ? 433 PHE D C     1 
ATOM   14973 O O     . PHE D  1 433 ? 31.435  73.846  215.995 1.00 60.36  ? 433 PHE D O     1 
ATOM   14974 C CB    . PHE D  1 433 ? 29.942  75.152  218.660 1.00 65.88  ? 433 PHE D CB    1 
ATOM   14975 C CG    . PHE D  1 433 ? 30.284  75.753  219.988 1.00 69.86  ? 433 PHE D CG    1 
ATOM   14976 C CD1   . PHE D  1 433 ? 31.602  75.998  220.328 1.00 68.42  ? 433 PHE D CD1   1 
ATOM   14977 C CD2   . PHE D  1 433 ? 29.289  76.082  220.894 1.00 72.65  ? 433 PHE D CD2   1 
ATOM   14978 C CE1   . PHE D  1 433 ? 31.924  76.554  221.547 1.00 67.74  ? 433 PHE D CE1   1 
ATOM   14979 C CE2   . PHE D  1 433 ? 29.604  76.643  222.114 1.00 74.75  ? 433 PHE D CE2   1 
ATOM   14980 C CZ    . PHE D  1 433 ? 30.925  76.876  222.443 1.00 70.89  ? 433 PHE D CZ    1 
ATOM   14981 N N     . LEU D  1 434 ? 29.502  74.950  215.632 1.00 58.38  ? 434 LEU D N     1 
ATOM   14982 C CA    . LEU D  1 434 ? 29.119  74.163  214.466 1.00 60.32  ? 434 LEU D CA    1 
ATOM   14983 C C     . LEU D  1 434 ? 30.051  74.435  213.290 1.00 60.35  ? 434 LEU D C     1 
ATOM   14984 O O     . LEU D  1 434 ? 30.359  73.532  212.511 1.00 59.77  ? 434 LEU D O     1 
ATOM   14985 C CB    . LEU D  1 434 ? 27.664  74.459  214.075 1.00 61.28  ? 434 LEU D CB    1 
ATOM   14986 C CG    . LEU D  1 434 ? 26.559  73.598  214.697 1.00 56.13  ? 434 LEU D CG    1 
ATOM   14987 C CD1   . LEU D  1 434 ? 26.690  73.502  216.209 1.00 59.91  ? 434 LEU D CD1   1 
ATOM   14988 C CD2   . LEU D  1 434 ? 25.187  74.140  214.323 1.00 63.99  ? 434 LEU D CD2   1 
ATOM   14989 N N     . ASP D  1 435 ? 30.497  75.683  213.171 1.00 60.23  ? 435 ASP D N     1 
ATOM   14990 C CA    . ASP D  1 435 ? 31.447  76.060  212.129 1.00 62.58  ? 435 ASP D CA    1 
ATOM   14991 C C     . ASP D  1 435 ? 32.775  75.336  212.318 1.00 57.93  ? 435 ASP D C     1 
ATOM   14992 O O     . ASP D  1 435 ? 33.396  74.901  211.346 1.00 53.67  ? 435 ASP D O     1 
ATOM   14993 C CB    . ASP D  1 435 ? 31.674  77.573  212.119 1.00 67.12  ? 435 ASP D CB    1 
ATOM   14994 C CG    . ASP D  1 435 ? 32.737  77.994  211.118 1.00 75.46  ? 435 ASP D CG    1 
ATOM   14995 O OD1   . ASP D  1 435 ? 32.497  77.841  209.902 1.00 81.35  ? 435 ASP D OD1   1 
ATOM   14996 O OD2   . ASP D  1 435 ? 33.808  78.475  211.546 1.00 75.11  ? 435 ASP D OD2   1 
ATOM   14997 N N     . TRP D  1 436 ? 33.208  75.220  213.572 1.00 55.22  ? 436 TRP D N     1 
ATOM   14998 C CA    . TRP D  1 436 ? 34.418  74.472  213.904 1.00 60.23  ? 436 TRP D CA    1 
ATOM   14999 C C     . TRP D  1 436 ? 34.283  73.032  213.448 1.00 58.74  ? 436 TRP D C     1 
ATOM   15000 O O     . TRP D  1 436 ? 35.148  72.505  212.747 1.00 53.87  ? 436 TRP D O     1 
ATOM   15001 C CB    . TRP D  1 436 ? 34.698  74.508  215.407 1.00 56.49  ? 436 TRP D CB    1 
ATOM   15002 C CG    . TRP D  1 436 ? 35.845  73.620  215.823 1.00 63.32  ? 436 TRP D CG    1 
ATOM   15003 C CD1   . TRP D  1 436 ? 37.174  73.925  215.770 1.00 59.60  ? 436 TRP D CD1   1 
ATOM   15004 C CD2   . TRP D  1 436 ? 35.762  72.285  216.348 1.00 64.26  ? 436 TRP D CD2   1 
ATOM   15005 N NE1   . TRP D  1 436 ? 37.922  72.868  216.229 1.00 60.92  ? 436 TRP D NE1   1 
ATOM   15006 C CE2   . TRP D  1 436 ? 37.080  71.850  216.592 1.00 64.22  ? 436 TRP D CE2   1 
ATOM   15007 C CE3   . TRP D  1 436 ? 34.702  71.418  216.639 1.00 60.59  ? 436 TRP D CE3   1 
ATOM   15008 C CZ2   . TRP D  1 436 ? 37.368  70.587  217.107 1.00 61.05  ? 436 TRP D CZ2   1 
ATOM   15009 C CZ3   . TRP D  1 436 ? 34.991  70.163  217.152 1.00 58.99  ? 436 TRP D CZ3   1 
ATOM   15010 C CH2   . TRP D  1 436 ? 36.313  69.760  217.380 1.00 57.86  ? 436 TRP D CH2   1 
ATOM   15011 N N     . LEU D  1 437 ? 33.182  72.408  213.854 1.00 58.94  ? 437 LEU D N     1 
ATOM   15012 C CA    . LEU D  1 437 ? 32.922  71.012  213.544 1.00 54.88  ? 437 LEU D CA    1 
ATOM   15013 C C     . LEU D  1 437 ? 32.969  70.745  212.043 1.00 54.95  ? 437 LEU D C     1 
ATOM   15014 O O     . LEU D  1 437 ? 33.537  69.745  211.606 1.00 54.26  ? 437 LEU D O     1 
ATOM   15015 C CB    . LEU D  1 437 ? 31.567  70.585  214.104 1.00 56.20  ? 437 LEU D CB    1 
ATOM   15016 C CG    . LEU D  1 437 ? 31.247  69.115  213.827 1.00 53.65  ? 437 LEU D CG    1 
ATOM   15017 C CD1   . LEU D  1 437 ? 32.167  68.206  214.630 1.00 48.66  ? 437 LEU D CD1   1 
ATOM   15018 C CD2   . LEU D  1 437 ? 29.792  68.810  214.109 1.00 51.90  ? 437 LEU D CD2   1 
ATOM   15019 N N     . GLU D  1 438 ? 32.379  71.642  211.258 1.00 54.89  ? 438 GLU D N     1 
ATOM   15020 C CA    . GLU D  1 438 ? 32.380  71.478  209.808 1.00 58.27  ? 438 GLU D CA    1 
ATOM   15021 C C     . GLU D  1 438 ? 33.793  71.612  209.241 1.00 58.89  ? 438 GLU D C     1 
ATOM   15022 O O     . GLU D  1 438 ? 34.168  70.890  208.318 1.00 59.64  ? 438 GLU D O     1 
ATOM   15023 C CB    . GLU D  1 438 ? 31.448  72.492  209.134 1.00 59.10  ? 438 GLU D CB    1 
ATOM   15024 C CG    . GLU D  1 438 ? 31.322  72.275  207.629 1.00 67.87  ? 438 GLU D CG    1 
ATOM   15025 C CD    . GLU D  1 438 ? 30.581  73.390  206.912 1.00 82.54  ? 438 GLU D CD    1 
ATOM   15026 O OE1   . GLU D  1 438 ? 29.973  74.245  207.590 1.00 86.65  ? 438 GLU D OE1   1 
ATOM   15027 O OE2   . GLU D  1 438 ? 30.610  73.409  205.663 1.00 84.67  ? 438 GLU D OE2   1 
ATOM   15028 N N     . LYS D  1 439 ? 34.571  72.534  209.803 1.00 59.38  ? 439 LYS D N     1 
ATOM   15029 C CA    . LYS D  1 439 ? 35.955  72.740  209.384 1.00 57.61  ? 439 LYS D CA    1 
ATOM   15030 C C     . LYS D  1 439 ? 36.801  71.490  209.626 1.00 57.35  ? 439 LYS D C     1 
ATOM   15031 O O     . LYS D  1 439 ? 37.532  71.037  208.742 1.00 57.08  ? 439 LYS D O     1 
ATOM   15032 C CB    . LYS D  1 439 ? 36.563  73.936  210.116 1.00 58.53  ? 439 LYS D CB    1 
ATOM   15033 C CG    . LYS D  1 439 ? 37.975  74.271  209.677 1.00 65.31  ? 439 LYS D CG    1 
ATOM   15034 C CD    . LYS D  1 439 ? 38.454  75.571  210.294 1.00 80.65  ? 439 LYS D CD    1 
ATOM   15035 C CE    . LYS D  1 439 ? 39.803  75.970  209.728 1.00 70.53  ? 439 LYS D CE    1 
ATOM   15036 N NZ    . LYS D  1 439 ? 40.136  77.384  210.045 1.00 71.33  ? 439 LYS D NZ    1 
ATOM   15037 N N     . VAL D  1 440 ? 36.697  70.953  210.838 1.00 53.96  ? 440 VAL D N     1 
ATOM   15038 C CA    . VAL D  1 440 ? 37.341  69.700  211.215 1.00 54.85  ? 440 VAL D CA    1 
ATOM   15039 C C     . VAL D  1 440 ? 37.007  68.583  210.236 1.00 53.52  ? 440 VAL D C     1 
ATOM   15040 O O     . VAL D  1 440 ? 37.891  67.880  209.743 1.00 49.88  ? 440 VAL D O     1 
ATOM   15041 C CB    . VAL D  1 440 ? 36.909  69.273  212.629 1.00 55.62  ? 440 VAL D CB    1 
ATOM   15042 C CG1   . VAL D  1 440 ? 37.428  67.889  212.955 1.00 47.14  ? 440 VAL D CG1   1 
ATOM   15043 C CG2   . VAL D  1 440 ? 37.374  70.291  213.647 1.00 57.22  ? 440 VAL D CG2   1 
ATOM   15044 N N     . TYR D  1 441 ? 35.715  68.442  209.962 1.00 57.09  ? 441 TYR D N     1 
ATOM   15045 C CA    . TYR D  1 441 ? 35.207  67.436  209.040 1.00 55.14  ? 441 TYR D CA    1 
ATOM   15046 C C     . TYR D  1 441 ? 35.735  67.660  207.624 1.00 52.64  ? 441 TYR D C     1 
ATOM   15047 O O     . TYR D  1 441 ? 36.126  66.712  206.941 1.00 50.63  ? 441 TYR D O     1 
ATOM   15048 C CB    . TYR D  1 441 ? 33.677  67.448  209.049 1.00 53.94  ? 441 TYR D CB    1 
ATOM   15049 C CG    . TYR D  1 441 ? 33.042  66.205  208.473 1.00 51.43  ? 441 TYR D CG    1 
ATOM   15050 C CD1   . TYR D  1 441 ? 33.047  65.009  209.179 1.00 52.01  ? 441 TYR D CD1   1 
ATOM   15051 C CD2   . TYR D  1 441 ? 32.422  66.230  207.230 1.00 52.79  ? 441 TYR D CD2   1 
ATOM   15052 C CE1   . TYR D  1 441 ? 32.465  63.871  208.661 1.00 51.15  ? 441 TYR D CE1   1 
ATOM   15053 C CE2   . TYR D  1 441 ? 31.834  65.097  206.704 1.00 54.80  ? 441 TYR D CE2   1 
ATOM   15054 C CZ    . TYR D  1 441 ? 31.859  63.920  207.424 1.00 52.60  ? 441 TYR D CZ    1 
ATOM   15055 O OH    . TYR D  1 441 ? 31.277  62.786  206.907 1.00 55.96  ? 441 TYR D OH    1 
ATOM   15056 N N     . GLU D  1 442 ? 35.746  68.916  207.185 1.00 56.48  ? 442 GLU D N     1 
ATOM   15057 C CA    . GLU D  1 442 ? 36.261  69.248  205.862 1.00 59.87  ? 442 GLU D CA    1 
ATOM   15058 C C     . GLU D  1 442 ? 37.763  69.000  205.781 1.00 54.01  ? 442 GLU D C     1 
ATOM   15059 O O     . GLU D  1 442 ? 38.274  68.574  204.744 1.00 58.00  ? 442 GLU D O     1 
ATOM   15060 C CB    . GLU D  1 442 ? 35.946  70.703  205.501 1.00 60.51  ? 442 GLU D CB    1 
ATOM   15061 C CG    . GLU D  1 442 ? 36.508  71.159  204.150 1.00 59.40  ? 442 GLU D CG    1 
ATOM   15062 C CD    . GLU D  1 442 ? 35.929  70.391  202.971 1.00 74.09  ? 442 GLU D CD    1 
ATOM   15063 O OE1   . GLU D  1 442 ? 34.837  69.799  203.115 1.00 79.51  ? 442 GLU D OE1   1 
ATOM   15064 O OE2   . GLU D  1 442 ? 36.565  70.381  201.895 1.00 76.07  ? 442 GLU D OE2   1 
ATOM   15065 N N     . PHE D  1 443 ? 38.471  69.263  206.876 1.00 50.94  ? 443 PHE D N     1 
ATOM   15066 C CA    . PHE D  1 443 ? 39.913  69.028  206.906 1.00 55.56  ? 443 PHE D CA    1 
ATOM   15067 C C     . PHE D  1 443 ? 40.244  67.548  206.749 1.00 55.23  ? 443 PHE D C     1 
ATOM   15068 O O     . PHE D  1 443 ? 41.191  67.191  206.053 1.00 51.97  ? 443 PHE D O     1 
ATOM   15069 C CB    . PHE D  1 443 ? 40.533  69.546  208.204 1.00 56.69  ? 443 PHE D CB    1 
ATOM   15070 C CG    . PHE D  1 443 ? 41.946  69.080  208.416 1.00 57.40  ? 443 PHE D CG    1 
ATOM   15071 C CD1   . PHE D  1 443 ? 42.955  69.494  207.562 1.00 57.68  ? 443 PHE D CD1   1 
ATOM   15072 C CD2   . PHE D  1 443 ? 42.264  68.211  209.448 1.00 56.64  ? 443 PHE D CD2   1 
ATOM   15073 C CE1   . PHE D  1 443 ? 44.255  69.062  207.737 1.00 54.48  ? 443 PHE D CE1   1 
ATOM   15074 C CE2   . PHE D  1 443 ? 43.565  67.775  209.628 1.00 59.31  ? 443 PHE D CE2   1 
ATOM   15075 C CZ    . PHE D  1 443 ? 44.560  68.201  208.771 1.00 57.04  ? 443 PHE D CZ    1 
ATOM   15076 N N     . MET D  1 444 ? 39.456  66.694  207.396 1.00 55.39  ? 444 MET D N     1 
ATOM   15077 C CA    . MET D  1 444 ? 39.735  65.261  207.432 1.00 50.36  ? 444 MET D CA    1 
ATOM   15078 C C     . MET D  1 444 ? 39.358  64.546  206.134 1.00 50.21  ? 444 MET D C     1 
ATOM   15079 O O     . MET D  1 444 ? 39.770  63.407  205.913 1.00 51.28  ? 444 MET D O     1 
ATOM   15080 C CB    . MET D  1 444 ? 39.000  64.620  208.609 1.00 51.15  ? 444 MET D CB    1 
ATOM   15081 C CG    . MET D  1 444 ? 39.533  65.028  209.974 1.00 49.79  ? 444 MET D CG    1 
ATOM   15082 S SD    . MET D  1 444 ? 41.226  64.471  210.247 1.00 55.15  ? 444 MET D SD    1 
ATOM   15083 C CE    . MET D  1 444 ? 41.040  62.698  210.068 1.00 46.86  ? 444 MET D CE    1 
ATOM   15084 N N     . LYS D  1 445 ? 38.593  65.224  205.279 1.00 51.54  ? 445 LYS D N     1 
ATOM   15085 C CA    . LYS D  1 445 ? 38.052  64.623  204.055 1.00 48.51  ? 445 LYS D CA    1 
ATOM   15086 C C     . LYS D  1 445 ? 39.055  63.840  203.186 1.00 48.47  ? 445 LYS D C     1 
ATOM   15087 O O     . LYS D  1 445 ? 38.728  62.754  202.711 1.00 53.08  ? 445 LYS D O     1 
ATOM   15088 C CB    . LYS D  1 445 ? 37.385  65.701  203.193 1.00 52.06  ? 445 LYS D CB    1 
ATOM   15089 C CG    . LYS D  1 445 ? 36.752  65.166  201.912 1.00 56.85  ? 445 LYS D CG    1 
ATOM   15090 C CD    . LYS D  1 445 ? 35.758  66.155  201.319 1.00 61.53  ? 445 LYS D CD    1 
ATOM   15091 C CE    . LYS D  1 445 ? 36.449  67.317  200.617 1.00 72.65  ? 445 LYS D CE    1 
ATOM   15092 N NZ    . LYS D  1 445 ? 35.493  68.415  200.280 1.00 76.49  ? 445 LYS D NZ    1 
ATOM   15093 N N     . PRO D  1 446 ? 40.272  64.377  202.966 1.00 52.69  ? 446 PRO D N     1 
ATOM   15094 C CA    . PRO D  1 446 ? 41.153  63.576  202.107 1.00 52.15  ? 446 PRO D CA    1 
ATOM   15095 C C     . PRO D  1 446 ? 41.782  62.357  202.780 1.00 49.61  ? 446 PRO D C     1 
ATOM   15096 O O     . PRO D  1 446 ? 42.308  61.499  202.073 1.00 54.09  ? 446 PRO D O     1 
ATOM   15097 C CB    . PRO D  1 446 ? 42.247  64.573  201.714 1.00 55.55  ? 446 PRO D CB    1 
ATOM   15098 C CG    . PRO D  1 446 ? 42.301  65.517  202.856 1.00 54.26  ? 446 PRO D CG    1 
ATOM   15099 C CD    . PRO D  1 446 ? 40.862  65.697  203.257 1.00 47.82  ? 446 PRO D CD    1 
ATOM   15100 N N     . PHE D  1 447 ? 41.742  62.276  204.107 1.00 53.25  ? 447 PHE D N     1 
ATOM   15101 C CA    . PHE D  1 447 ? 42.440  61.200  204.812 1.00 48.21  ? 447 PHE D CA    1 
ATOM   15102 C C     . PHE D  1 447 ? 41.542  60.012  205.136 1.00 52.76  ? 447 PHE D C     1 
ATOM   15103 O O     . PHE D  1 447 ? 42.027  58.920  205.436 1.00 46.65  ? 447 PHE D O     1 
ATOM   15104 C CB    . PHE D  1 447 ? 43.062  61.724  206.105 1.00 50.11  ? 447 PHE D CB    1 
ATOM   15105 C CG    . PHE D  1 447 ? 43.874  62.973  205.923 1.00 54.98  ? 447 PHE D CG    1 
ATOM   15106 C CD1   . PHE D  1 447 ? 45.054  62.952  205.198 1.00 56.80  ? 447 PHE D CD1   1 
ATOM   15107 C CD2   . PHE D  1 447 ? 43.462  64.167  206.491 1.00 53.70  ? 447 PHE D CD2   1 
ATOM   15108 C CE1   . PHE D  1 447 ? 45.802  64.101  205.033 1.00 52.52  ? 447 PHE D CE1   1 
ATOM   15109 C CE2   . PHE D  1 447 ? 44.205  65.319  206.332 1.00 54.73  ? 447 PHE D CE2   1 
ATOM   15110 C CZ    . PHE D  1 447 ? 45.377  65.287  205.603 1.00 50.19  ? 447 PHE D CZ    1 
ATOM   15111 N N     . VAL D  1 448 ? 40.233  60.227  205.080 1.00 54.07  ? 448 VAL D N     1 
ATOM   15112 C CA    . VAL D  1 448 ? 39.279  59.210  205.505 1.00 50.20  ? 448 VAL D CA    1 
ATOM   15113 C C     . VAL D  1 448 ? 38.668  58.473  204.320 1.00 54.66  ? 448 VAL D C     1 
ATOM   15114 O O     . VAL D  1 448 ? 39.070  58.685  203.174 1.00 57.89  ? 448 VAL D O     1 
ATOM   15115 C CB    . VAL D  1 448 ? 38.158  59.830  206.350 1.00 51.37  ? 448 VAL D CB    1 
ATOM   15116 C CG1   . VAL D  1 448 ? 38.741  60.439  207.618 1.00 49.07  ? 448 VAL D CG1   1 
ATOM   15117 C CG2   . VAL D  1 448 ? 37.396  60.873  205.537 1.00 52.76  ? 448 VAL D CG2   1 
ATOM   15118 N N     . SER D  1 449 ? 37.704  57.601  204.609 1.00 56.05  ? 449 SER D N     1 
ATOM   15119 C CA    . SER D  1 449 ? 37.002  56.854  203.571 1.00 51.65  ? 449 SER D CA    1 
ATOM   15120 C C     . SER D  1 449 ? 36.396  57.792  202.543 1.00 48.69  ? 449 SER D C     1 
ATOM   15121 O O     . SER D  1 449 ? 35.991  58.913  202.864 1.00 46.57  ? 449 SER D O     1 
ATOM   15122 C CB    . SER D  1 449 ? 35.906  55.974  204.170 1.00 50.86  ? 449 SER D CB    1 
ATOM   15123 O OG    . SER D  1 449 ? 34.891  56.766  204.765 1.00 47.01  ? 449 SER D OG    1 
ATOM   15124 N N     . LYS D  1 450 ? 36.333  57.318  201.304 1.00 55.45  ? 450 LYS D N     1 
ATOM   15125 C CA    . LYS D  1 450 ? 35.864  58.134  200.195 1.00 59.36  ? 450 LYS D CA    1 
ATOM   15126 C C     . LYS D  1 450 ? 35.122  57.288  199.175 1.00 59.18  ? 450 LYS D C     1 
ATOM   15127 O O     . LYS D  1 450 ? 35.307  56.073  199.096 1.00 56.70  ? 450 LYS D O     1 
ATOM   15128 C CB    . LYS D  1 450 ? 37.041  58.854  199.536 1.00 66.37  ? 450 LYS D CB    1 
ATOM   15129 C CG    . LYS D  1 450 ? 38.187  57.933  199.144 1.00 64.41  ? 450 LYS D CG    1 
ATOM   15130 C CD    . LYS D  1 450 ? 39.381  58.726  198.624 1.00 71.73  ? 450 LYS D CD    1 
ATOM   15131 C CE    . LYS D  1 450 ? 40.109  59.460  199.742 1.00 64.49  ? 450 LYS D CE    1 
ATOM   15132 N NZ    . LYS D  1 450 ? 41.272  58.681  200.257 1.00 71.76  ? 450 LYS D NZ    1 
ATOM   15133 N N     . ASN D  1 451 ? 34.277  57.956  198.401 1.00 60.51  ? 451 ASN D N     1 
ATOM   15134 C CA    . ASN D  1 451 ? 33.487  57.328  197.340 1.00 62.97  ? 451 ASN D CA    1 
ATOM   15135 C C     . ASN D  1 451 ? 32.734  56.072  197.785 1.00 63.29  ? 451 ASN D C     1 
ATOM   15136 O O     . ASN D  1 451 ? 33.038  54.976  197.316 1.00 63.94  ? 451 ASN D O     1 
ATOM   15137 C CB    . ASN D  1 451 ? 34.385  57.009  196.170 1.00 65.21  ? 451 ASN D CB    1 
ATOM   15138 C CG    . ASN D  1 451 ? 35.272  58.179  195.813 1.00 73.19  ? 451 ASN D CG    1 
ATOM   15139 O OD1   . ASN D  1 451 ? 34.783  59.289  195.607 1.00 77.38  ? 451 ASN D OD1   1 
ATOM   15140 N ND2   . ASN D  1 451 ? 36.582  57.954  195.781 1.00 74.10  ? 451 ASN D ND2   1 
ATOM   15141 N N     . PRO D  1 452 ? 31.733  56.240  198.676 1.00 58.44  ? 452 PRO D N     1 
ATOM   15142 C CA    . PRO D  1 452 ? 31.355  57.506  199.315 1.00 59.68  ? 452 PRO D CA    1 
ATOM   15143 C C     . PRO D  1 452 ? 32.056  57.699  200.655 1.00 54.65  ? 452 PRO D C     1 
ATOM   15144 O O     . PRO D  1 452 ? 32.733  56.782  201.116 1.00 53.61  ? 452 PRO D O     1 
ATOM   15145 C CB    . PRO D  1 452 ? 29.850  57.356  199.513 1.00 57.90  ? 452 PRO D CB    1 
ATOM   15146 C CG    . PRO D  1 452 ? 29.685  55.896  199.782 1.00 54.61  ? 452 PRO D CG    1 
ATOM   15147 C CD    . PRO D  1 452 ? 30.767  55.178  198.992 1.00 59.02  ? 452 PRO D CD    1 
ATOM   15148 N N     . ARG D  1 453 ? 31.892  58.866  201.270 1.00 57.26  ? 453 ARG D N     1 
ATOM   15149 C CA    . ARG D  1 453 ? 32.383  59.074  202.624 1.00 54.27  ? 453 ARG D CA    1 
ATOM   15150 C C     . ARG D  1 453 ? 31.444  58.372  203.600 1.00 52.28  ? 453 ARG D C     1 
ATOM   15151 O O     . ARG D  1 453 ? 30.253  58.682  203.653 1.00 51.26  ? 453 ARG D O     1 
ATOM   15152 C CB    . ARG D  1 453 ? 32.489  60.565  202.947 1.00 53.02  ? 453 ARG D CB    1 
ATOM   15153 C CG    . ARG D  1 453 ? 33.137  60.861  204.282 1.00 53.41  ? 453 ARG D CG    1 
ATOM   15154 C CD    . ARG D  1 453 ? 33.448  62.332  204.414 1.00 50.70  ? 453 ARG D CD    1 
ATOM   15155 N NE    . ARG D  1 453 ? 34.239  62.594  205.608 1.00 51.20  ? 453 ARG D NE    1 
ATOM   15156 C CZ    . ARG D  1 453 ? 34.786  63.767  205.902 1.00 53.81  ? 453 ARG D CZ    1 
ATOM   15157 N NH1   . ARG D  1 453 ? 34.626  64.802  205.086 1.00 50.51  ? 453 ARG D NH1   1 
ATOM   15158 N NH2   . ARG D  1 453 ? 35.493  63.905  207.014 1.00 50.06  ? 453 ARG D NH2   1 
ATOM   15159 N N     . LEU D  1 454 ? 31.980  57.428  204.369 1.00 52.44  ? 454 LEU D N     1 
ATOM   15160 C CA    . LEU D  1 454 ? 31.157  56.523  205.168 1.00 48.86  ? 454 LEU D CA    1 
ATOM   15161 C C     . LEU D  1 454 ? 30.643  57.140  206.464 1.00 46.61  ? 454 LEU D C     1 
ATOM   15162 O O     . LEU D  1 454 ? 31.223  58.087  206.992 1.00 41.92  ? 454 LEU D O     1 
ATOM   15163 C CB    . LEU D  1 454 ? 31.943  55.252  205.491 1.00 44.26  ? 454 LEU D CB    1 
ATOM   15164 C CG    . LEU D  1 454 ? 32.546  54.540  204.282 1.00 44.38  ? 454 LEU D CG    1 
ATOM   15165 C CD1   . LEU D  1 454 ? 33.312  53.303  204.711 1.00 40.14  ? 454 LEU D CD1   1 
ATOM   15166 C CD2   . LEU D  1 454 ? 31.467  54.183  203.279 1.00 49.22  ? 454 LEU D CD2   1 
ATOM   15167 N N     . GLY D  1 455 ? 29.547  56.581  206.967 1.00 43.48  ? 455 GLY D N     1 
ATOM   15168 C CA    . GLY D  1 455 ? 28.966  56.993  208.231 1.00 41.15  ? 455 GLY D CA    1 
ATOM   15169 C C     . GLY D  1 455 ? 28.473  55.788  209.011 1.00 41.31  ? 455 GLY D C     1 
ATOM   15170 O O     . GLY D  1 455 ? 28.685  54.651  208.607 1.00 37.38  ? 455 GLY D O     1 
ATOM   15171 N N     . TYR D  1 456 ? 27.799  56.043  210.124 1.00 41.28  ? 456 TYR D N     1 
ATOM   15172 C CA    . TYR D  1 456 ? 27.340  54.993  211.024 1.00 32.79  ? 456 TYR D CA    1 
ATOM   15173 C C     . TYR D  1 456 ? 25.955  55.385  211.521 1.00 35.10  ? 456 TYR D C     1 
ATOM   15174 O O     . TYR D  1 456 ? 25.793  56.430  212.141 1.00 33.79  ? 456 TYR D O     1 
ATOM   15175 C CB    . TYR D  1 456 ? 28.348  54.816  212.167 1.00 33.77  ? 456 TYR D CB    1 
ATOM   15176 C CG    . TYR D  1 456 ? 27.922  53.966  213.343 1.00 35.70  ? 456 TYR D CG    1 
ATOM   15177 C CD1   . TYR D  1 456 ? 27.166  52.813  213.170 1.00 32.23  ? 456 TYR D CD1   1 
ATOM   15178 C CD2   . TYR D  1 456 ? 28.318  54.302  214.633 1.00 37.02  ? 456 TYR D CD2   1 
ATOM   15179 C CE1   . TYR D  1 456 ? 26.793  52.036  214.258 1.00 28.23  ? 456 TYR D CE1   1 
ATOM   15180 C CE2   . TYR D  1 456 ? 27.955  53.536  215.717 1.00 37.86  ? 456 TYR D CE2   1 
ATOM   15181 C CZ    . TYR D  1 456 ? 27.197  52.402  215.525 1.00 32.74  ? 456 TYR D CZ    1 
ATOM   15182 O OH    . TYR D  1 456 ? 26.835  51.642  216.613 1.00 34.07  ? 456 TYR D OH    1 
ATOM   15183 N N     . VAL D  1 457 ? 24.957  54.553  211.231 1.00 30.72  ? 457 VAL D N     1 
ATOM   15184 C CA    . VAL D  1 457 ? 23.557  54.952  211.398 1.00 26.85  ? 457 VAL D CA    1 
ATOM   15185 C C     . VAL D  1 457 ? 23.217  55.309  212.846 1.00 30.34  ? 457 VAL D C     1 
ATOM   15186 O O     . VAL D  1 457 ? 22.327  56.120  213.090 1.00 30.98  ? 457 VAL D O     1 
ATOM   15187 C CB    . VAL D  1 457 ? 22.587  53.853  210.888 1.00 33.17  ? 457 VAL D CB    1 
ATOM   15188 C CG1   . VAL D  1 457 ? 22.552  52.664  211.840 1.00 27.65  ? 457 VAL D CG1   1 
ATOM   15189 C CG2   . VAL D  1 457 ? 21.184  54.426  210.670 1.00 29.93  ? 457 VAL D CG2   1 
ATOM   15190 N N     . ASN D  1 458 ? 23.934  54.726  213.803 1.00 31.55  ? 458 ASN D N     1 
ATOM   15191 C CA    . ASN D  1 458 ? 23.744  55.095  215.202 1.00 33.42  ? 458 ASN D CA    1 
ATOM   15192 C C     . ASN D  1 458 ? 24.336  56.465  215.495 1.00 37.62  ? 458 ASN D C     1 
ATOM   15193 O O     . ASN D  1 458 ? 24.001  57.099  216.493 1.00 34.54  ? 458 ASN D O     1 
ATOM   15194 C CB    . ASN D  1 458 ? 24.351  54.048  216.133 1.00 30.17  ? 458 ASN D CB    1 
ATOM   15195 C CG    . ASN D  1 458 ? 23.310  53.102  216.694 1.00 32.51  ? 458 ASN D CG    1 
ATOM   15196 O OD1   . ASN D  1 458 ? 22.141  53.464  216.839 1.00 29.24  ? 458 ASN D OD1   1 
ATOM   15197 N ND2   . ASN D  1 458 ? 23.729  51.884  217.017 1.00 32.73  ? 458 ASN D ND2   1 
ATOM   15198 N N     . HIS D  1 459 ? 25.227  56.912  214.619 1.00 35.21  ? 459 HIS D N     1 
ATOM   15199 C CA    . HIS D  1 459 ? 25.711  58.283  214.661 1.00 39.80  ? 459 HIS D CA    1 
ATOM   15200 C C     . HIS D  1 459 ? 25.026  59.069  213.557 1.00 41.36  ? 459 HIS D C     1 
ATOM   15201 O O     . HIS D  1 459 ? 25.679  59.653  212.693 1.00 37.47  ? 459 HIS D O     1 
ATOM   15202 C CB    . HIS D  1 459 ? 27.229  58.335  214.515 1.00 39.59  ? 459 HIS D CB    1 
ATOM   15203 C CG    . HIS D  1 459 ? 27.960  57.867  215.732 1.00 43.71  ? 459 HIS D CG    1 
ATOM   15204 N ND1   . HIS D  1 459 ? 29.304  58.096  215.930 1.00 51.25  ? 459 HIS D ND1   1 
ATOM   15205 C CD2   . HIS D  1 459 ? 27.531  57.184  216.820 1.00 43.88  ? 459 HIS D CD2   1 
ATOM   15206 C CE1   . HIS D  1 459 ? 29.673  57.573  217.086 1.00 57.22  ? 459 HIS D CE1   1 
ATOM   15207 N NE2   . HIS D  1 459 ? 28.615  57.014  217.646 1.00 48.84  ? 459 HIS D NE2   1 
ATOM   15208 N N     . ILE D  1 460 ? 23.695  59.049  213.602 1.00 41.47  ? 460 ILE D N     1 
ATOM   15209 C CA    . ILE D  1 460 ? 22.849  59.675  212.595 1.00 40.71  ? 460 ILE D CA    1 
ATOM   15210 C C     . ILE D  1 460 ? 23.231  61.142  212.384 1.00 38.75  ? 460 ILE D C     1 
ATOM   15211 O O     . ILE D  1 460 ? 23.392  61.907  213.338 1.00 38.96  ? 460 ILE D O     1 
ATOM   15212 C CB    . ILE D  1 460 ? 21.345  59.545  212.982 1.00 40.15  ? 460 ILE D CB    1 
ATOM   15213 C CG1   . ILE D  1 460 ? 20.443  59.931  211.806 1.00 45.41  ? 460 ILE D CG1   1 
ATOM   15214 C CG2   . ILE D  1 460 ? 21.017  60.310  214.272 1.00 38.81  ? 460 ILE D CG2   1 
ATOM   15215 C CD1   . ILE D  1 460 ? 20.087  58.753  210.921 1.00 52.49  ? 460 ILE D CD1   1 
ATOM   15216 N N     . ASP D  1 461 ? 23.412  61.509  211.119 1.00 39.99  ? 461 ASP D N     1 
ATOM   15217 C CA    . ASP D  1 461 ? 23.889  62.839  210.753 1.00 43.97  ? 461 ASP D CA    1 
ATOM   15218 C C     . ASP D  1 461 ? 23.040  63.405  209.617 1.00 42.61  ? 461 ASP D C     1 
ATOM   15219 O O     . ASP D  1 461 ? 23.164  62.981  208.467 1.00 44.03  ? 461 ASP D O     1 
ATOM   15220 C CB    . ASP D  1 461 ? 25.364  62.781  210.338 1.00 43.87  ? 461 ASP D CB    1 
ATOM   15221 C CG    . ASP D  1 461 ? 25.981  64.157  210.156 1.00 49.33  ? 461 ASP D CG    1 
ATOM   15222 O OD1   . ASP D  1 461 ? 25.262  65.170  210.286 1.00 48.33  ? 461 ASP D OD1   1 
ATOM   15223 O OD2   . ASP D  1 461 ? 27.197  64.226  209.876 1.00 50.82  ? 461 ASP D OD2   1 
ATOM   15224 N N     . LEU D  1 462 ? 22.187  64.370  209.942 1.00 44.72  ? 462 LEU D N     1 
ATOM   15225 C CA    . LEU D  1 462 ? 21.257  64.924  208.965 1.00 47.69  ? 462 LEU D CA    1 
ATOM   15226 C C     . LEU D  1 462 ? 21.922  65.898  207.995 1.00 50.81  ? 462 LEU D C     1 
ATOM   15227 O O     . LEU D  1 462 ? 21.308  66.317  207.012 1.00 50.62  ? 462 LEU D O     1 
ATOM   15228 C CB    . LEU D  1 462 ? 20.092  65.607  209.677 1.00 47.64  ? 462 LEU D CB    1 
ATOM   15229 C CG    . LEU D  1 462 ? 19.117  64.645  210.363 1.00 51.54  ? 462 LEU D CG    1 
ATOM   15230 C CD1   . LEU D  1 462 ? 18.005  65.407  211.043 1.00 37.59  ? 462 LEU D CD1   1 
ATOM   15231 C CD2   . LEU D  1 462 ? 18.549  63.664  209.353 1.00 46.97  ? 462 LEU D CD2   1 
ATOM   15232 N N     . ASP D  1 463 ? 23.176  66.253  208.269 1.00 50.07  ? 463 ASP D N     1 
ATOM   15233 C CA    . ASP D  1 463 ? 23.954  67.074  207.343 1.00 53.18  ? 463 ASP D CA    1 
ATOM   15234 C C     . ASP D  1 463 ? 24.093  66.356  206.005 1.00 56.57  ? 463 ASP D C     1 
ATOM   15235 O O     . ASP D  1 463 ? 24.200  66.989  204.953 1.00 58.90  ? 463 ASP D O     1 
ATOM   15236 C CB    . ASP D  1 463 ? 25.340  67.390  207.908 1.00 54.53  ? 463 ASP D CB    1 
ATOM   15237 C CG    . ASP D  1 463 ? 25.289  68.276  209.141 1.00 54.83  ? 463 ASP D CG    1 
ATOM   15238 O OD1   . ASP D  1 463 ? 24.219  68.853  209.426 1.00 57.80  ? 463 ASP D OD1   1 
ATOM   15239 O OD2   . ASP D  1 463 ? 26.332  68.403  209.818 1.00 56.82  ? 463 ASP D OD2   1 
ATOM   15240 N N     . LEU D  1 464 ? 24.081  65.026  206.060 1.00 55.23  ? 464 LEU D N     1 
ATOM   15241 C CA    . LEU D  1 464 ? 24.167  64.187  204.868 1.00 54.01  ? 464 LEU D CA    1 
ATOM   15242 C C     . LEU D  1 464 ? 22.925  64.309  203.987 1.00 54.83  ? 464 LEU D C     1 
ATOM   15243 O O     . LEU D  1 464 ? 22.903  63.798  202.868 1.00 59.59  ? 464 LEU D O     1 
ATOM   15244 C CB    . LEU D  1 464 ? 24.373  62.720  205.260 1.00 57.27  ? 464 LEU D CB    1 
ATOM   15245 C CG    . LEU D  1 464 ? 25.571  62.366  206.149 1.00 59.18  ? 464 LEU D CG    1 
ATOM   15246 C CD1   . LEU D  1 464 ? 25.531  60.894  206.552 1.00 51.20  ? 464 LEU D CD1   1 
ATOM   15247 C CD2   . LEU D  1 464 ? 26.889  62.707  205.464 1.00 53.56  ? 464 LEU D CD2   1 
ATOM   15248 N N     . GLY D  1 465 ? 21.892  64.975  204.499 1.00 54.13  ? 465 GLY D N     1 
ATOM   15249 C CA    . GLY D  1 465 ? 20.652  65.168  203.762 1.00 57.60  ? 465 GLY D CA    1 
ATOM   15250 C C     . GLY D  1 465 ? 19.457  64.530  204.450 1.00 56.79  ? 465 GLY D C     1 
ATOM   15251 O O     . GLY D  1 465 ? 19.603  63.907  205.502 1.00 53.89  ? 465 GLY D O     1 
ATOM   15252 N N     . GLY D  1 466 ? 18.273  64.673  203.856 1.00 55.83  ? 466 GLY D N     1 
ATOM   15253 C CA    . GLY D  1 466 ? 17.061  64.107  204.427 1.00 51.80  ? 466 GLY D CA    1 
ATOM   15254 C C     . GLY D  1 466 ? 15.836  64.152  203.526 1.00 61.19  ? 466 GLY D C     1 
ATOM   15255 O O     . GLY D  1 466 ? 15.743  64.988  202.628 1.00 58.61  ? 466 GLY D O     1 
ATOM   15256 N N     . ILE D  1 467 ? 14.890  63.252  203.784 1.00 56.99  ? 467 ILE D N     1 
ATOM   15257 C CA    . ILE D  1 467 ? 13.659  63.153  203.000 1.00 50.82  ? 467 ILE D CA    1 
ATOM   15258 C C     . ILE D  1 467 ? 12.512  63.954  203.623 1.00 57.71  ? 467 ILE D C     1 
ATOM   15259 O O     . ILE D  1 467 ? 12.308  63.916  204.837 1.00 56.33  ? 467 ILE D O     1 
ATOM   15260 C CB    . ILE D  1 467 ? 13.210  61.675  202.849 1.00 50.97  ? 467 ILE D CB    1 
ATOM   15261 C CG1   . ILE D  1 467 ? 14.162  60.908  201.928 1.00 57.56  ? 467 ILE D CG1   1 
ATOM   15262 C CG2   . ILE D  1 467 ? 11.790  61.590  202.311 1.00 56.10  ? 467 ILE D CG2   1 
ATOM   15263 C CD1   . ILE D  1 467 ? 13.868  61.083  200.451 1.00 59.73  ? 467 ILE D CD1   1 
ATOM   15264 N N     . ASP D  1 468 ? 11.784  64.691  202.786 1.00 58.88  ? 468 ASP D N     1 
ATOM   15265 C CA    . ASP D  1 468 ? 10.515  65.302  203.175 1.00 60.65  ? 468 ASP D CA    1 
ATOM   15266 C C     . ASP D  1 468 ? 9.375   64.394  202.718 1.00 61.92  ? 468 ASP D C     1 
ATOM   15267 O O     . ASP D  1 468 ? 8.999   64.407  201.547 1.00 64.70  ? 468 ASP D O     1 
ATOM   15268 C CB    . ASP D  1 468 ? 10.366  66.701  202.563 1.00 61.41  ? 468 ASP D CB    1 
ATOM   15269 C CG    . ASP D  1 468 ? 9.142   67.452  203.080 1.00 66.23  ? 468 ASP D CG    1 
ATOM   15270 O OD1   . ASP D  1 468 ? 8.274   66.838  203.735 1.00 66.09  ? 468 ASP D OD1   1 
ATOM   15271 O OD2   . ASP D  1 468 ? 9.045   68.671  202.820 1.00 67.73  ? 468 ASP D OD2   1 
ATOM   15272 N N     . TRP D  1 469 ? 8.825   63.614  203.645 1.00 56.13  ? 469 TRP D N     1 
ATOM   15273 C CA    . TRP D  1 469 ? 7.802   62.627  203.301 1.00 60.19  ? 469 TRP D CA    1 
ATOM   15274 C C     . TRP D  1 469 ? 6.447   63.262  202.987 1.00 61.63  ? 469 TRP D C     1 
ATOM   15275 O O     . TRP D  1 469 ? 5.513   62.568  202.586 1.00 63.13  ? 469 TRP D O     1 
ATOM   15276 C CB    . TRP D  1 469 ? 7.643   61.604  204.431 1.00 51.96  ? 469 TRP D CB    1 
ATOM   15277 C CG    . TRP D  1 469 ? 8.850   60.734  204.644 1.00 48.82  ? 469 TRP D CG    1 
ATOM   15278 C CD1   . TRP D  1 469 ? 9.730   60.792  205.686 1.00 47.40  ? 469 TRP D CD1   1 
ATOM   15279 C CD2   . TRP D  1 469 ? 9.309   59.676  203.792 1.00 48.13  ? 469 TRP D CD2   1 
ATOM   15280 N NE1   . TRP D  1 469 ? 10.707  59.837  205.535 1.00 44.22  ? 469 TRP D NE1   1 
ATOM   15281 C CE2   . TRP D  1 469 ? 10.471  59.137  204.381 1.00 41.07  ? 469 TRP D CE2   1 
ATOM   15282 C CE3   . TRP D  1 469 ? 8.850   59.132  202.588 1.00 47.97  ? 469 TRP D CE3   1 
ATOM   15283 C CZ2   . TRP D  1 469 ? 11.180  58.084  203.807 1.00 41.49  ? 469 TRP D CZ2   1 
ATOM   15284 C CZ3   . TRP D  1 469 ? 9.554   58.086  202.020 1.00 50.10  ? 469 TRP D CZ3   1 
ATOM   15285 C CH2   . TRP D  1 469 ? 10.707  57.574  202.629 1.00 44.15  ? 469 TRP D CH2   1 
ATOM   15286 N N     . GLY D  1 470 ? 6.342   64.575  203.171 1.00 63.82  ? 470 GLY D N     1 
ATOM   15287 C CA    . GLY D  1 470 ? 5.122   65.300  202.855 1.00 66.24  ? 470 GLY D CA    1 
ATOM   15288 C C     . GLY D  1 470 ? 5.127   65.861  201.444 1.00 70.68  ? 470 GLY D C     1 
ATOM   15289 O O     . GLY D  1 470 ? 4.100   66.310  200.933 1.00 73.00  ? 470 GLY D O     1 
ATOM   15290 N N     . ASN D  1 471 ? 6.300   65.840  200.820 1.00 71.03  ? 471 ASN D N     1 
ATOM   15291 C CA    . ASN D  1 471 ? 6.465   66.246  199.427 1.00 72.19  ? 471 ASN D CA    1 
ATOM   15292 C C     . ASN D  1 471 ? 6.390   65.011  198.530 1.00 73.50  ? 471 ASN D C     1 
ATOM   15293 O O     . ASN D  1 471 ? 7.310   64.194  198.516 1.00 71.92  ? 471 ASN D O     1 
ATOM   15294 C CB    . ASN D  1 471 ? 7.798   66.991  199.249 1.00 73.48  ? 471 ASN D CB    1 
ATOM   15295 C CG    . ASN D  1 471 ? 8.039   67.465  197.817 1.00 80.46  ? 471 ASN D CG    1 
ATOM   15296 O OD1   . ASN D  1 471 ? 7.808   66.735  196.852 1.00 81.73  ? 471 ASN D OD1   1 
ATOM   15297 N ND2   . ASN D  1 471 ? 8.532   68.691  197.680 1.00 89.99  ? 471 ASN D ND2   1 
ATOM   15298 N N     . LYS D  1 472 ? 5.300   64.884  197.775 1.00 73.34  ? 472 LYS D N     1 
ATOM   15299 C CA    . LYS D  1 472 ? 5.036   63.676  196.991 1.00 74.88  ? 472 LYS D CA    1 
ATOM   15300 C C     . LYS D  1 472 ? 6.074   63.413  195.891 1.00 74.17  ? 472 LYS D C     1 
ATOM   15301 O O     . LYS D  1 472 ? 6.432   62.261  195.641 1.00 72.12  ? 472 LYS D O     1 
ATOM   15302 C CB    . LYS D  1 472 ? 3.629   63.746  196.379 1.00 75.79  ? 472 LYS D CB    1 
ATOM   15303 C CG    . LYS D  1 472 ? 3.255   62.536  195.517 1.00 78.60  ? 472 LYS D CG    1 
ATOM   15304 C CD    . LYS D  1 472 ? 1.787   62.576  195.100 1.00 84.13  ? 472 LYS D CD    1 
ATOM   15305 C CE    . LYS D  1 472 ? 1.507   61.672  193.901 1.00 81.54  ? 472 LYS D CE    1 
ATOM   15306 N NZ    . LYS D  1 472 ? 1.054   60.301  194.274 1.00 81.50  ? 472 LYS D NZ    1 
ATOM   15307 N N     . THR D  1 473 ? 6.559   64.472  195.244 1.00 75.03  ? 473 THR D N     1 
ATOM   15308 C CA    . THR D  1 473 ? 7.573   64.329  194.194 1.00 77.75  ? 473 THR D CA    1 
ATOM   15309 C C     . THR D  1 473 ? 8.874   63.726  194.734 1.00 75.13  ? 473 THR D C     1 
ATOM   15310 O O     . THR D  1 473 ? 9.533   62.944  194.047 1.00 73.56  ? 473 THR D O     1 
ATOM   15311 C CB    . THR D  1 473 ? 7.889   65.681  193.504 1.00 79.93  ? 473 THR D CB    1 
ATOM   15312 O OG1   . THR D  1 473 ? 8.481   66.582  194.446 1.00 86.95  ? 473 THR D OG1   1 
ATOM   15313 C CG2   . THR D  1 473 ? 6.630   66.303  192.931 1.00 79.75  ? 473 THR D CG2   1 
ATOM   15314 N N     . VAL D  1 474 ? 9.238   64.098  195.960 1.00 75.21  ? 474 VAL D N     1 
ATOM   15315 C CA    . VAL D  1 474 ? 10.379  63.493  196.651 1.00 72.83  ? 474 VAL D CA    1 
ATOM   15316 C C     . VAL D  1 474 ? 10.131  62.004  196.919 1.00 69.84  ? 474 VAL D C     1 
ATOM   15317 O O     . VAL D  1 474 ? 10.925  61.149  196.513 1.00 71.59  ? 474 VAL D O     1 
ATOM   15318 C CB    . VAL D  1 474 ? 10.676  64.205  198.000 1.00 70.91  ? 474 VAL D CB    1 
ATOM   15319 C CG1   . VAL D  1 474 ? 11.807  63.506  198.743 1.00 70.27  ? 474 VAL D CG1   1 
ATOM   15320 C CG2   . VAL D  1 474 ? 11.011  65.675  197.774 1.00 77.02  ? 474 VAL D CG2   1 
ATOM   15321 N N     . VAL D  1 475 ? 9.016   61.716  197.590 1.00 70.17  ? 475 VAL D N     1 
ATOM   15322 C CA    . VAL D  1 475 ? 8.628   60.359  197.983 1.00 68.69  ? 475 VAL D CA    1 
ATOM   15323 C C     . VAL D  1 475 ? 8.645   59.367  196.814 1.00 69.70  ? 475 VAL D C     1 
ATOM   15324 O O     . VAL D  1 475 ? 9.013   58.202  196.984 1.00 69.84  ? 475 VAL D O     1 
ATOM   15325 C CB    . VAL D  1 475 ? 7.218   60.362  198.624 1.00 63.51  ? 475 VAL D CB    1 
ATOM   15326 C CG1   . VAL D  1 475 ? 6.836   58.974  199.104 1.00 57.79  ? 475 VAL D CG1   1 
ATOM   15327 C CG2   . VAL D  1 475 ? 7.163   61.343  199.787 1.00 60.41  ? 475 VAL D CG2   1 
ATOM   15328 N N     . ASN D  1 476 ? 8.261   59.837  195.631 1.00 71.32  ? 476 ASN D N     1 
ATOM   15329 C CA    . ASN D  1 476 ? 8.231   58.987  194.447 1.00 72.91  ? 476 ASN D CA    1 
ATOM   15330 C C     . ASN D  1 476 ? 9.624   58.597  193.953 1.00 73.38  ? 476 ASN D C     1 
ATOM   15331 O O     . ASN D  1 476 ? 9.782   57.592  193.260 1.00 74.88  ? 476 ASN D O     1 
ATOM   15332 C CB    . ASN D  1 476 ? 7.453   59.675  193.324 1.00 76.95  ? 476 ASN D CB    1 
ATOM   15333 C CG    . ASN D  1 476 ? 5.953   59.586  193.519 1.00 73.15  ? 476 ASN D CG    1 
ATOM   15334 O OD1   . ASN D  1 476 ? 5.266   60.601  193.634 1.00 76.62  ? 476 ASN D OD1   1 
ATOM   15335 N ND2   . ASN D  1 476 ? 5.437   58.365  193.561 1.00 68.90  ? 476 ASN D ND2   1 
ATOM   15336 N N     . ASN D  1 477 ? 10.630  59.391  194.308 1.00 71.45  ? 477 ASN D N     1 
ATOM   15337 C CA    . ASN D  1 477 ? 12.013  59.061  193.973 1.00 74.23  ? 477 ASN D CA    1 
ATOM   15338 C C     . ASN D  1 477 ? 12.851  58.886  195.237 1.00 69.94  ? 477 ASN D C     1 
ATOM   15339 O O     . ASN D  1 477 ? 14.057  59.138  195.240 1.00 69.50  ? 477 ASN D O     1 
ATOM   15340 C CB    . ASN D  1 477 ? 12.627  60.139  193.075 1.00 73.95  ? 477 ASN D CB    1 
ATOM   15341 C CG    . ASN D  1 477 ? 13.786  59.616  192.244 1.00 71.80  ? 477 ASN D CG    1 
ATOM   15342 O OD1   . ASN D  1 477 ? 13.791  58.459  191.826 1.00 72.75  ? 477 ASN D OD1   1 
ATOM   15343 N ND2   . ASN D  1 477 ? 14.779  60.468  192.006 1.00 79.60  ? 477 ASN D ND2   1 
ATOM   15344 N N     . ALA D  1 478 ? 12.199  58.435  196.304 1.00 65.15  ? 478 ALA D N     1 
ATOM   15345 C CA    . ALA D  1 478 ? 12.816  58.351  197.624 1.00 62.29  ? 478 ALA D CA    1 
ATOM   15346 C C     . ALA D  1 478 ? 14.036  57.437  197.669 1.00 58.76  ? 478 ALA D C     1 
ATOM   15347 O O     . ALA D  1 478 ? 14.970  57.689  198.426 1.00 57.85  ? 478 ALA D O     1 
ATOM   15348 C CB    . ALA D  1 478 ? 11.786  57.889  198.644 1.00 57.26  ? 478 ALA D CB    1 
ATOM   15349 N N     . ILE D  1 479 ? 14.027  56.382  196.859 1.00 57.32  ? 479 ILE D N     1 
ATOM   15350 C CA    . ILE D  1 479 ? 15.116  55.405  196.864 1.00 53.67  ? 479 ILE D CA    1 
ATOM   15351 C C     . ILE D  1 479 ? 16.430  56.016  196.376 1.00 55.87  ? 479 ILE D C     1 
ATOM   15352 O O     . ILE D  1 479 ? 17.483  55.812  196.980 1.00 57.11  ? 479 ILE D O     1 
ATOM   15353 C CB    . ILE D  1 479 ? 14.773  54.175  195.998 1.00 50.91  ? 479 ILE D CB    1 
ATOM   15354 C CG1   . ILE D  1 479 ? 13.625  53.380  196.628 1.00 54.04  ? 479 ILE D CG1   1 
ATOM   15355 C CG2   . ILE D  1 479 ? 15.989  53.279  195.828 1.00 43.98  ? 479 ILE D CG2   1 
ATOM   15356 C CD1   . ILE D  1 479 ? 13.345  52.057  195.940 1.00 46.40  ? 479 ILE D CD1   1 
ATOM   15357 N N     . GLU D  1 480 ? 16.357  56.775  195.288 1.00 57.47  ? 480 GLU D N     1 
ATOM   15358 C CA    . GLU D  1 480 ? 17.540  57.407  194.716 1.00 62.54  ? 480 GLU D CA    1 
ATOM   15359 C C     . GLU D  1 480 ? 18.007  58.593  195.550 1.00 56.21  ? 480 GLU D C     1 
ATOM   15360 O O     . GLU D  1 480 ? 19.206  58.848  195.660 1.00 61.30  ? 480 GLU D O     1 
ATOM   15361 C CB    . GLU D  1 480 ? 17.266  57.852  193.278 1.00 64.10  ? 480 GLU D CB    1 
ATOM   15362 C CG    . GLU D  1 480 ? 17.024  56.699  192.322 1.00 66.33  ? 480 GLU D CG    1 
ATOM   15363 C CD    . GLU D  1 480 ? 18.121  55.656  192.386 1.00 64.23  ? 480 GLU D CD    1 
ATOM   15364 O OE1   . GLU D  1 480 ? 19.308  56.038  192.469 1.00 69.63  ? 480 GLU D OE1   1 
ATOM   15365 O OE2   . GLU D  1 480 ? 17.797  54.450  192.365 1.00 68.08  ? 480 GLU D OE2   1 
ATOM   15366 N N     . ILE D  1 481 ? 17.057  59.313  196.138 1.00 57.85  ? 481 ILE D N     1 
ATOM   15367 C CA    . ILE D  1 481 ? 17.378  60.457  196.985 1.00 60.13  ? 481 ILE D CA    1 
ATOM   15368 C C     . ILE D  1 481 ? 18.027  60.003  198.294 1.00 59.72  ? 481 ILE D C     1 
ATOM   15369 O O     . ILE D  1 481 ? 18.995  60.608  198.757 1.00 59.16  ? 481 ILE D O     1 
ATOM   15370 C CB    . ILE D  1 481 ? 16.121  61.303  197.290 1.00 60.76  ? 481 ILE D CB    1 
ATOM   15371 C CG1   . ILE D  1 481 ? 15.519  61.848  195.992 1.00 61.58  ? 481 ILE D CG1   1 
ATOM   15372 C CG2   . ILE D  1 481 ? 16.456  62.452  198.233 1.00 57.71  ? 481 ILE D CG2   1 
ATOM   15373 C CD1   . ILE D  1 481 ? 14.146  62.460  196.159 1.00 66.20  ? 481 ILE D CD1   1 
ATOM   15374 N N     . SER D  1 482 ? 17.505  58.927  198.878 1.00 58.08  ? 482 SER D N     1 
ATOM   15375 C CA    . SER D  1 482 ? 18.022  58.417  200.146 1.00 54.70  ? 482 SER D CA    1 
ATOM   15376 C C     . SER D  1 482 ? 19.343  57.671  199.987 1.00 53.25  ? 482 SER D C     1 
ATOM   15377 O O     . SER D  1 482 ? 19.979  57.304  200.975 1.00 51.62  ? 482 SER D O     1 
ATOM   15378 C CB    . SER D  1 482 ? 16.995  57.498  200.815 1.00 51.07  ? 482 SER D CB    1 
ATOM   15379 O OG    . SER D  1 482 ? 15.866  58.227  201.262 1.00 55.73  ? 482 SER D OG    1 
ATOM   15380 N N     . ARG D  1 483 ? 19.752  57.457  198.741 1.00 54.42  ? 483 ARG D N     1 
ATOM   15381 C CA    . ARG D  1 483 ? 20.937  56.662  198.436 1.00 55.58  ? 483 ARG D CA    1 
ATOM   15382 C C     . ARG D  1 483 ? 22.224  57.297  198.970 1.00 53.67  ? 483 ARG D C     1 
ATOM   15383 O O     . ARG D  1 483 ? 23.213  56.606  199.217 1.00 52.43  ? 483 ARG D O     1 
ATOM   15384 C CB    . ARG D  1 483 ? 21.044  56.446  196.922 1.00 58.83  ? 483 ARG D CB    1 
ATOM   15385 C CG    . ARG D  1 483 ? 22.182  55.540  196.496 1.00 57.80  ? 483 ARG D CG    1 
ATOM   15386 C CD    . ARG D  1 483 ? 22.177  55.288  194.998 1.00 61.44  ? 483 ARG D CD    1 
ATOM   15387 N NE    . ARG D  1 483 ? 20.955  54.619  194.562 1.00 64.51  ? 483 ARG D NE    1 
ATOM   15388 C CZ    . ARG D  1 483 ? 20.751  53.308  194.641 1.00 63.15  ? 483 ARG D CZ    1 
ATOM   15389 N NH1   . ARG D  1 483 ? 21.687  52.516  195.147 1.00 61.40  ? 483 ARG D NH1   1 
ATOM   15390 N NH2   . ARG D  1 483 ? 19.608  52.789  194.216 1.00 67.53  ? 483 ARG D NH2   1 
ATOM   15391 N N     . SER D  1 484 ? 22.197  58.614  199.153 1.00 54.37  ? 484 SER D N     1 
ATOM   15392 C CA    . SER D  1 484 ? 23.348  59.355  199.663 1.00 53.69  ? 484 SER D CA    1 
ATOM   15393 C C     . SER D  1 484 ? 23.782  58.847  201.038 1.00 54.14  ? 484 SER D C     1 
ATOM   15394 O O     . SER D  1 484 ? 24.870  58.292  201.187 1.00 48.60  ? 484 SER D O     1 
ATOM   15395 C CB    . SER D  1 484 ? 23.026  60.849  199.731 1.00 53.91  ? 484 SER D CB    1 
ATOM   15396 O OG    . SER D  1 484 ? 22.543  61.319  198.482 1.00 64.16  ? 484 SER D OG    1 
ATOM   15397 N N     . TRP D  1 485 ? 22.923  59.032  202.035 1.00 50.89  ? 485 TRP D N     1 
ATOM   15398 C CA    . TRP D  1 485 ? 23.214  58.570  203.387 1.00 48.85  ? 485 TRP D CA    1 
ATOM   15399 C C     . TRP D  1 485 ? 23.028  57.060  203.511 1.00 47.93  ? 485 TRP D C     1 
ATOM   15400 O O     . TRP D  1 485 ? 23.676  56.413  204.335 1.00 43.10  ? 485 TRP D O     1 
ATOM   15401 C CB    . TRP D  1 485 ? 22.335  59.297  204.406 1.00 43.75  ? 485 TRP D CB    1 
ATOM   15402 C CG    . TRP D  1 485 ? 20.868  59.308  204.075 1.00 51.95  ? 485 TRP D CG    1 
ATOM   15403 C CD1   . TRP D  1 485 ? 19.939  58.376  204.433 1.00 44.77  ? 485 TRP D CD1   1 
ATOM   15404 C CD2   . TRP D  1 485 ? 20.163  60.311  203.332 1.00 49.80  ? 485 TRP D CD2   1 
ATOM   15405 N NE1   . TRP D  1 485 ? 18.700  58.733  203.957 1.00 47.15  ? 485 TRP D NE1   1 
ATOM   15406 C CE2   . TRP D  1 485 ? 18.811  59.917  203.277 1.00 51.36  ? 485 TRP D CE2   1 
ATOM   15407 C CE3   . TRP D  1 485 ? 20.544  61.502  202.706 1.00 51.01  ? 485 TRP D CE3   1 
ATOM   15408 C CZ2   . TRP D  1 485 ? 17.839  60.672  202.625 1.00 51.23  ? 485 TRP D CZ2   1 
ATOM   15409 C CZ3   . TRP D  1 485 ? 19.578  62.247  202.054 1.00 55.43  ? 485 TRP D CZ3   1 
ATOM   15410 C CH2   . TRP D  1 485 ? 18.242  61.828  202.017 1.00 55.30  ? 485 TRP D CH2   1 
ATOM   15411 N N     . GLY D  1 486 ? 22.146  56.507  202.684 1.00 48.78  ? 486 GLY D N     1 
ATOM   15412 C CA    . GLY D  1 486 ? 21.881  55.079  202.685 1.00 44.93  ? 486 GLY D CA    1 
ATOM   15413 C C     . GLY D  1 486 ? 23.122  54.249  202.417 1.00 43.15  ? 486 GLY D C     1 
ATOM   15414 O O     . GLY D  1 486 ? 23.442  53.333  203.175 1.00 47.71  ? 486 GLY D O     1 
ATOM   15415 N N     . GLU D  1 487 ? 23.828  54.575  201.338 1.00 45.93  ? 487 GLU D N     1 
ATOM   15416 C CA    . GLU D  1 487 ? 25.065  53.882  200.997 1.00 51.68  ? 487 GLU D CA    1 
ATOM   15417 C C     . GLU D  1 487 ? 26.201  54.305  201.923 1.00 46.09  ? 487 GLU D C     1 
ATOM   15418 O O     . GLU D  1 487 ? 27.169  53.571  202.109 1.00 44.72  ? 487 GLU D O     1 
ATOM   15419 C CB    . GLU D  1 487 ? 25.441  54.139  199.538 1.00 55.13  ? 487 GLU D CB    1 
ATOM   15420 C CG    . GLU D  1 487 ? 24.412  53.616  198.554 1.00 60.96  ? 487 GLU D CG    1 
ATOM   15421 C CD    . GLU D  1 487 ? 24.916  53.603  197.127 1.00 63.08  ? 487 GLU D CD    1 
ATOM   15422 O OE1   . GLU D  1 487 ? 25.906  54.304  196.835 1.00 71.97  ? 487 GLU D OE1   1 
ATOM   15423 O OE2   . GLU D  1 487 ? 24.319  52.886  196.297 1.00 65.62  ? 487 GLU D OE2   1 
ATOM   15424 N N     . SER D  1 488 ? 26.078  55.492  202.504 1.00 48.33  ? 488 SER D N     1 
ATOM   15425 C CA    . SER D  1 488 ? 27.062  55.961  203.472 1.00 47.46  ? 488 SER D CA    1 
ATOM   15426 C C     . SER D  1 488 ? 26.996  55.111  204.734 1.00 47.63  ? 488 SER D C     1 
ATOM   15427 O O     . SER D  1 488 ? 28.023  54.724  205.298 1.00 40.61  ? 488 SER D O     1 
ATOM   15428 C CB    . SER D  1 488 ? 26.832  57.432  203.808 1.00 47.19  ? 488 SER D CB    1 
ATOM   15429 O OG    . SER D  1 488 ? 27.864  57.936  204.635 1.00 54.61  ? 488 SER D OG    1 
ATOM   15430 N N     . TYR D  1 489 ? 25.773  54.819  205.164 1.00 44.28  ? 489 TYR D N     1 
ATOM   15431 C CA    . TYR D  1 489 ? 25.548  54.005  206.349 1.00 39.21  ? 489 TYR D CA    1 
ATOM   15432 C C     . TYR D  1 489 ? 25.733  52.517  206.076 1.00 39.66  ? 489 TYR D C     1 
ATOM   15433 O O     . TYR D  1 489 ? 26.297  51.801  206.901 1.00 37.44  ? 489 TYR D O     1 
ATOM   15434 C CB    . TYR D  1 489 ? 24.141  54.234  206.904 1.00 41.56  ? 489 TYR D CB    1 
ATOM   15435 C CG    . TYR D  1 489 ? 23.885  55.616  207.457 1.00 41.96  ? 489 TYR D CG    1 
ATOM   15436 C CD1   . TYR D  1 489 ? 24.884  56.323  208.109 1.00 39.79  ? 489 TYR D CD1   1 
ATOM   15437 C CD2   . TYR D  1 489 ? 22.637  56.212  207.326 1.00 34.23  ? 489 TYR D CD2   1 
ATOM   15438 C CE1   . TYR D  1 489 ? 24.649  57.587  208.617 1.00 34.34  ? 489 TYR D CE1   1 
ATOM   15439 C CE2   . TYR D  1 489 ? 22.391  57.473  207.828 1.00 43.01  ? 489 TYR D CE2   1 
ATOM   15440 C CZ    . TYR D  1 489 ? 23.401  58.158  208.472 1.00 43.26  ? 489 TYR D CZ    1 
ATOM   15441 O OH    . TYR D  1 489 ? 23.161  59.416  208.975 1.00 41.45  ? 489 TYR D OH    1 
ATOM   15442 N N     . PHE D  1 490 ? 25.252  52.051  204.926 1.00 37.76  ? 490 PHE D N     1 
ATOM   15443 C CA    . PHE D  1 490 ? 25.078  50.616  204.719 1.00 41.77  ? 490 PHE D CA    1 
ATOM   15444 C C     . PHE D  1 490 ? 25.756  50.058  203.469 1.00 42.20  ? 490 PHE D C     1 
ATOM   15445 O O     . PHE D  1 490 ? 25.839  48.839  203.306 1.00 42.13  ? 490 PHE D O     1 
ATOM   15446 C CB    . PHE D  1 490 ? 23.583  50.284  204.670 1.00 37.94  ? 490 PHE D CB    1 
ATOM   15447 C CG    . PHE D  1 490 ? 22.803  50.827  205.834 1.00 32.46  ? 490 PHE D CG    1 
ATOM   15448 C CD1   . PHE D  1 490 ? 22.991  50.317  207.107 1.00 34.94  ? 490 PHE D CD1   1 
ATOM   15449 C CD2   . PHE D  1 490 ? 21.874  51.841  205.654 1.00 36.92  ? 490 PHE D CD2   1 
ATOM   15450 C CE1   . PHE D  1 490 ? 22.275  50.810  208.184 1.00 29.45  ? 490 PHE D CE1   1 
ATOM   15451 C CE2   . PHE D  1 490 ? 21.152  52.341  206.727 1.00 30.57  ? 490 PHE D CE2   1 
ATOM   15452 C CZ    . PHE D  1 490 ? 21.355  51.825  207.992 1.00 28.60  ? 490 PHE D CZ    1 
ATOM   15453 N N     . LEU D  1 491 ? 26.228  50.943  202.595 1.00 43.07  ? 491 LEU D N     1 
ATOM   15454 C CA    . LEU D  1 491 ? 26.875  50.543  201.344 1.00 47.01  ? 491 LEU D CA    1 
ATOM   15455 C C     . LEU D  1 491 ? 26.041  49.557  200.527 1.00 45.82  ? 491 LEU D C     1 
ATOM   15456 O O     . LEU D  1 491 ? 24.918  49.856  200.120 1.00 43.82  ? 491 LEU D O     1 
ATOM   15457 C CB    . LEU D  1 491 ? 28.256  49.942  201.625 1.00 39.43  ? 491 LEU D CB    1 
ATOM   15458 C CG    . LEU D  1 491 ? 29.365  50.931  201.988 1.00 48.21  ? 491 LEU D CG    1 
ATOM   15459 C CD1   . LEU D  1 491 ? 30.627  50.193  202.395 1.00 41.81  ? 491 LEU D CD1   1 
ATOM   15460 C CD2   . LEU D  1 491 ? 29.652  51.866  200.825 1.00 45.31  ? 491 LEU D CD2   1 
ATOM   15461 N N     . SER D  1 492 ? 26.603  48.375  200.301 1.00 48.42  ? 492 SER D N     1 
ATOM   15462 C CA    . SER D  1 492 ? 25.968  47.359  199.470 1.00 47.21  ? 492 SER D CA    1 
ATOM   15463 C C     . SER D  1 492 ? 24.770  46.683  200.137 1.00 51.78  ? 492 SER D C     1 
ATOM   15464 O O     . SER D  1 492 ? 24.014  45.966  199.481 1.00 54.27  ? 492 SER D O     1 
ATOM   15465 C CB    . SER D  1 492 ? 26.993  46.296  199.076 1.00 47.74  ? 492 SER D CB    1 
ATOM   15466 O OG    . SER D  1 492 ? 26.360  45.050  198.846 1.00 67.79  ? 492 SER D OG    1 
ATOM   15467 N N     . ASN D  1 493 ? 24.602  46.902  201.438 1.00 49.49  ? 493 ASN D N     1 
ATOM   15468 C CA    . ASN D  1 493 ? 23.477  46.322  202.169 1.00 45.03  ? 493 ASN D CA    1 
ATOM   15469 C C     . ASN D  1 493 ? 22.193  47.112  201.953 1.00 48.05  ? 493 ASN D C     1 
ATOM   15470 O O     . ASN D  1 493 ? 21.115  46.686  202.365 1.00 48.22  ? 493 ASN D O     1 
ATOM   15471 C CB    . ASN D  1 493 ? 23.790  46.243  203.667 1.00 40.76  ? 493 ASN D CB    1 
ATOM   15472 C CG    . ASN D  1 493 ? 24.847  45.203  203.990 1.00 42.53  ? 493 ASN D CG    1 
ATOM   15473 O OD1   . ASN D  1 493 ? 24.940  44.169  203.328 1.00 46.18  ? 493 ASN D OD1   1 
ATOM   15474 N ND2   . ASN D  1 493 ? 25.645  45.468  205.020 1.00 41.01  ? 493 ASN D ND2   1 
ATOM   15475 N N     . TYR D  1 494 ? 22.320  48.261  201.295 1.00 45.39  ? 494 TYR D N     1 
ATOM   15476 C CA    . TYR D  1 494 ? 21.209  49.195  201.121 1.00 44.01  ? 494 TYR D CA    1 
ATOM   15477 C C     . TYR D  1 494 ? 20.031  48.617  200.332 1.00 47.86  ? 494 TYR D C     1 
ATOM   15478 O O     . TYR D  1 494 ? 18.874  48.925  200.622 1.00 46.19  ? 494 TYR D O     1 
ATOM   15479 C CB    . TYR D  1 494 ? 21.712  50.471  200.441 1.00 44.74  ? 494 TYR D CB    1 
ATOM   15480 C CG    . TYR D  1 494 ? 20.637  51.495  200.172 1.00 47.05  ? 494 TYR D CG    1 
ATOM   15481 C CD1   . TYR D  1 494 ? 19.914  52.063  201.214 1.00 46.15  ? 494 TYR D CD1   1 
ATOM   15482 C CD2   . TYR D  1 494 ? 20.358  51.911  198.878 1.00 45.90  ? 494 TYR D CD2   1 
ATOM   15483 C CE1   . TYR D  1 494 ? 18.933  53.007  200.973 1.00 40.62  ? 494 TYR D CE1   1 
ATOM   15484 C CE2   . TYR D  1 494 ? 19.378  52.857  198.626 1.00 45.10  ? 494 TYR D CE2   1 
ATOM   15485 C CZ    . TYR D  1 494 ? 18.669  53.400  199.677 1.00 42.24  ? 494 TYR D CZ    1 
ATOM   15486 O OH    . TYR D  1 494 ? 17.695  54.341  199.435 1.00 47.92  ? 494 TYR D OH    1 
ATOM   15487 N N     . GLU D  1 495 ? 20.322  47.786  199.337 1.00 44.51  ? 495 GLU D N     1 
ATOM   15488 C CA    . GLU D  1 495 ? 19.272  47.158  198.540 1.00 47.27  ? 495 GLU D CA    1 
ATOM   15489 C C     . GLU D  1 495 ? 18.397  46.220  199.369 1.00 45.32  ? 495 GLU D C     1 
ATOM   15490 O O     . GLU D  1 495 ? 17.170  46.270  199.282 1.00 49.38  ? 495 GLU D O     1 
ATOM   15491 C CB    . GLU D  1 495 ? 19.883  46.399  197.360 1.00 48.01  ? 495 GLU D CB    1 
ATOM   15492 C CG    . GLU D  1 495 ? 20.107  47.260  196.135 1.00 55.36  ? 495 GLU D CG    1 
ATOM   15493 C CD    . GLU D  1 495 ? 18.804  47.720  195.523 1.00 51.72  ? 495 GLU D CD    1 
ATOM   15494 O OE1   . GLU D  1 495 ? 18.799  48.788  194.879 1.00 55.14  ? 495 GLU D OE1   1 
ATOM   15495 O OE2   . GLU D  1 495 ? 17.792  47.008  195.685 1.00 53.47  ? 495 GLU D OE2   1 
ATOM   15496 N N     . ARG D  1 496 ? 19.031  45.373  200.174 1.00 47.72  ? 496 ARG D N     1 
ATOM   15497 C CA    . ARG D  1 496 ? 18.304  44.382  200.961 1.00 44.25  ? 496 ARG D CA    1 
ATOM   15498 C C     . ARG D  1 496 ? 17.477  45.022  202.074 1.00 48.13  ? 496 ARG D C     1 
ATOM   15499 O O     . ARG D  1 496 ? 16.453  44.481  202.493 1.00 46.00  ? 496 ARG D O     1 
ATOM   15500 C CB    . ARG D  1 496 ? 19.274  43.362  201.557 1.00 44.38  ? 496 ARG D CB    1 
ATOM   15501 C CG    . ARG D  1 496 ? 18.592  42.146  202.153 1.00 42.09  ? 496 ARG D CG    1 
ATOM   15502 C CD    . ARG D  1 496 ? 19.591  41.188  202.760 1.00 41.69  ? 496 ARG D CD    1 
ATOM   15503 N NE    . ARG D  1 496 ? 18.916  40.105  203.467 1.00 40.78  ? 496 ARG D NE    1 
ATOM   15504 C CZ    . ARG D  1 496 ? 19.533  39.202  204.220 1.00 40.46  ? 496 ARG D CZ    1 
ATOM   15505 N NH1   . ARG D  1 496 ? 20.851  39.244  204.369 1.00 46.18  ? 496 ARG D NH1   1 
ATOM   15506 N NH2   . ARG D  1 496 ? 18.832  38.255  204.827 1.00 43.38  ? 496 ARG D NH2   1 
ATOM   15507 N N     . LEU D  1 497 ? 17.934  46.173  202.555 1.00 42.79  ? 497 LEU D N     1 
ATOM   15508 C CA    . LEU D  1 497 ? 17.186  46.928  203.549 1.00 40.14  ? 497 LEU D CA    1 
ATOM   15509 C C     . LEU D  1 497 ? 15.895  47.452  202.939 1.00 48.14  ? 497 LEU D C     1 
ATOM   15510 O O     . LEU D  1 497 ? 14.868  47.523  203.611 1.00 47.79  ? 497 LEU D O     1 
ATOM   15511 C CB    . LEU D  1 497 ? 18.025  48.079  204.096 1.00 37.47  ? 497 LEU D CB    1 
ATOM   15512 C CG    . LEU D  1 497 ? 19.189  47.657  204.990 1.00 44.03  ? 497 LEU D CG    1 
ATOM   15513 C CD1   . LEU D  1 497 ? 20.122  48.835  205.208 1.00 36.48  ? 497 LEU D CD1   1 
ATOM   15514 C CD2   . LEU D  1 497 ? 18.665  47.131  206.316 1.00 36.65  ? 497 LEU D CD2   1 
ATOM   15515 N N     . ILE D  1 498 ? 15.956  47.814  201.661 1.00 47.30  ? 498 ILE D N     1 
ATOM   15516 C CA    . ILE D  1 498 ? 14.779  48.274  200.933 1.00 47.62  ? 498 ILE D CA    1 
ATOM   15517 C C     . ILE D  1 498 ? 13.753  47.147  200.801 1.00 46.86  ? 498 ILE D C     1 
ATOM   15518 O O     . ILE D  1 498 ? 12.547  47.378  200.910 1.00 49.93  ? 498 ILE D O     1 
ATOM   15519 C CB    . ILE D  1 498 ? 15.161  48.811  199.535 1.00 47.24  ? 498 ILE D CB    1 
ATOM   15520 C CG1   . ILE D  1 498 ? 15.974  50.098  199.673 1.00 49.26  ? 498 ILE D CG1   1 
ATOM   15521 C CG2   . ILE D  1 498 ? 13.919  49.068  198.692 1.00 43.16  ? 498 ILE D CG2   1 
ATOM   15522 C CD1   . ILE D  1 498 ? 16.526  50.623  198.367 1.00 47.60  ? 498 ILE D CD1   1 
ATOM   15523 N N     . ARG D  1 499 ? 14.236  45.926  200.586 1.00 46.44  ? 499 ARG D N     1 
ATOM   15524 C CA    . ARG D  1 499 ? 13.352  44.768  200.488 1.00 48.47  ? 499 ARG D CA    1 
ATOM   15525 C C     . ARG D  1 499 ? 12.659  44.498  201.820 1.00 50.90  ? 499 ARG D C     1 
ATOM   15526 O O     . ARG D  1 499 ? 11.445  44.292  201.868 1.00 47.47  ? 499 ARG D O     1 
ATOM   15527 C CB    . ARG D  1 499 ? 14.119  43.521  200.033 1.00 48.76  ? 499 ARG D CB    1 
ATOM   15528 C CG    . ARG D  1 499 ? 13.248  42.269  199.991 1.00 49.07  ? 499 ARG D CG    1 
ATOM   15529 C CD    . ARG D  1 499 ? 13.809  41.178  199.088 1.00 42.47  ? 499 ARG D CD    1 
ATOM   15530 N NE    . ARG D  1 499 ? 14.912  40.444  199.701 1.00 49.98  ? 499 ARG D NE    1 
ATOM   15531 C CZ    . ARG D  1 499 ? 16.197  40.690  199.466 1.00 48.06  ? 499 ARG D CZ    1 
ATOM   15532 N NH1   . ARG D  1 499 ? 16.547  41.660  198.630 1.00 47.50  ? 499 ARG D NH1   1 
ATOM   15533 N NH2   . ARG D  1 499 ? 17.135  39.969  200.068 1.00 49.39  ? 499 ARG D NH2   1 
ATOM   15534 N N     . ALA D  1 500 ? 13.436  44.513  202.898 1.00 46.69  ? 500 ALA D N     1 
ATOM   15535 C CA    . ALA D  1 500 ? 12.903  44.266  204.232 1.00 44.18  ? 500 ALA D CA    1 
ATOM   15536 C C     . ALA D  1 500 ? 11.888  45.331  204.631 1.00 44.98  ? 500 ALA D C     1 
ATOM   15537 O O     . ALA D  1 500 ? 10.891  45.031  205.283 1.00 43.22  ? 500 ALA D O     1 
ATOM   15538 C CB    . ALA D  1 500 ? 14.030  44.206  205.245 1.00 35.36  ? 500 ALA D CB    1 
ATOM   15539 N N     . LYS D  1 501 ? 12.149  46.572  204.231 1.00 42.14  ? 501 LYS D N     1 
ATOM   15540 C CA    . LYS D  1 501 ? 11.232  47.678  204.486 1.00 43.49  ? 501 LYS D CA    1 
ATOM   15541 C C     . LYS D  1 501 ? 9.905   47.468  203.758 1.00 49.35  ? 501 LYS D C     1 
ATOM   15542 O O     . LYS D  1 501 ? 8.834   47.745  204.301 1.00 43.33  ? 501 LYS D O     1 
ATOM   15543 C CB    . LYS D  1 501 ? 11.867  49.004  204.059 1.00 40.71  ? 501 LYS D CB    1 
ATOM   15544 C CG    . LYS D  1 501 ? 10.952  50.214  204.171 1.00 41.75  ? 501 LYS D CG    1 
ATOM   15545 C CD    . LYS D  1 501 ? 10.626  50.552  205.619 1.00 42.13  ? 501 LYS D CD    1 
ATOM   15546 C CE    . LYS D  1 501 ? 9.719   51.776  205.708 1.00 37.68  ? 501 LYS D CE    1 
ATOM   15547 N NZ    . LYS D  1 501 ? 9.450   52.192  207.115 1.00 34.83  ? 501 LYS D NZ    1 
ATOM   15548 N N     . THR D  1 502 ? 9.987   46.973  202.526 1.00 49.49  ? 502 THR D N     1 
ATOM   15549 C CA    . THR D  1 502 ? 8.806   46.715  201.713 1.00 48.95  ? 502 THR D CA    1 
ATOM   15550 C C     . THR D  1 502 ? 7.973   45.574  202.298 1.00 47.19  ? 502 THR D C     1 
ATOM   15551 O O     . THR D  1 502 ? 6.743   45.596  202.240 1.00 48.40  ? 502 THR D O     1 
ATOM   15552 C CB    . THR D  1 502 ? 9.197   46.379  200.259 1.00 49.62  ? 502 THR D CB    1 
ATOM   15553 O OG1   . THR D  1 502 ? 10.002  47.436  199.720 1.00 50.47  ? 502 THR D OG1   1 
ATOM   15554 C CG2   . THR D  1 502 ? 7.960   46.212  199.397 1.00 53.86  ? 502 THR D CG2   1 
ATOM   15555 N N     . LEU D  1 503 ? 8.649   44.586  202.875 1.00 47.56  ? 503 LEU D N     1 
ATOM   15556 C CA    . LEU D  1 503 ? 7.980   43.425  203.456 1.00 45.22  ? 503 LEU D CA    1 
ATOM   15557 C C     . LEU D  1 503 ? 7.293   43.738  204.784 1.00 45.40  ? 503 LEU D C     1 
ATOM   15558 O O     . LEU D  1 503 ? 6.224   43.203  205.078 1.00 44.40  ? 503 LEU D O     1 
ATOM   15559 C CB    . LEU D  1 503 ? 8.980   42.283  203.661 1.00 42.80  ? 503 LEU D CB    1 
ATOM   15560 C CG    . LEU D  1 503 ? 9.567   41.632  202.405 1.00 51.21  ? 503 LEU D CG    1 
ATOM   15561 C CD1   . LEU D  1 503 ? 10.609  40.578  202.767 1.00 44.32  ? 503 LEU D CD1   1 
ATOM   15562 C CD2   . LEU D  1 503 ? 8.462   41.034  201.549 1.00 47.62  ? 503 LEU D CD2   1 
ATOM   15563 N N     . ILE D  1 504 ? 7.910   44.601  205.585 1.00 45.23  ? 504 ILE D N     1 
ATOM   15564 C CA    . ILE D  1 504 ? 7.442   44.828  206.947 1.00 40.32  ? 504 ILE D CA    1 
ATOM   15565 C C     . ILE D  1 504 ? 6.699   46.155  207.128 1.00 36.12  ? 504 ILE D C     1 
ATOM   15566 O O     . ILE D  1 504 ? 5.880   46.284  208.037 1.00 42.51  ? 504 ILE D O     1 
ATOM   15567 C CB    . ILE D  1 504 ? 8.622   44.762  207.954 1.00 33.98  ? 504 ILE D CB    1 
ATOM   15568 C CG1   . ILE D  1 504 ? 8.115   44.419  209.358 1.00 35.99  ? 504 ILE D CG1   1 
ATOM   15569 C CG2   . ILE D  1 504 ? 9.435   46.058  207.948 1.00 35.39  ? 504 ILE D CG2   1 
ATOM   15570 C CD1   . ILE D  1 504 ? 7.544   43.026  209.469 1.00 38.35  ? 504 ILE D CD1   1 
ATOM   15571 N N     . ASP D  1 505 ? 6.964   47.132  206.265 1.00 42.52  ? 505 ASP D N     1 
ATOM   15572 C CA    . ASP D  1 505 ? 6.304   48.435  206.380 1.00 40.28  ? 505 ASP D CA    1 
ATOM   15573 C C     . ASP D  1 505 ? 6.130   49.116  205.018 1.00 43.43  ? 505 ASP D C     1 
ATOM   15574 O O     . ASP D  1 505 ? 6.670   50.198  204.793 1.00 44.65  ? 505 ASP D O     1 
ATOM   15575 C CB    . ASP D  1 505 ? 7.102   49.342  207.329 1.00 36.22  ? 505 ASP D CB    1 
ATOM   15576 C CG    . ASP D  1 505 ? 6.389   50.648  207.646 1.00 41.40  ? 505 ASP D CG    1 
ATOM   15577 O OD1   . ASP D  1 505 ? 5.141   50.672  207.656 1.00 37.31  ? 505 ASP D OD1   1 
ATOM   15578 O OD2   . ASP D  1 505 ? 7.087   51.658  207.892 1.00 40.75  ? 505 ASP D OD2   1 
ATOM   15579 N N     . PRO D  1 506 ? 5.369   48.491  204.103 1.00 46.58  ? 506 PRO D N     1 
ATOM   15580 C CA    . PRO D  1 506 ? 5.213   49.071  202.762 1.00 46.12  ? 506 PRO D CA    1 
ATOM   15581 C C     . PRO D  1 506 ? 4.500   50.425  202.744 1.00 49.32  ? 506 PRO D C     1 
ATOM   15582 O O     . PRO D  1 506 ? 4.747   51.226  201.841 1.00 50.60  ? 506 PRO D O     1 
ATOM   15583 C CB    . PRO D  1 506 ? 4.384   48.016  202.019 1.00 51.99  ? 506 PRO D CB    1 
ATOM   15584 C CG    . PRO D  1 506 ? 3.694   47.242  203.086 1.00 48.42  ? 506 PRO D CG    1 
ATOM   15585 C CD    . PRO D  1 506 ? 4.645   47.214  204.239 1.00 48.06  ? 506 PRO D CD    1 
ATOM   15586 N N     . ASN D  1 507 ? 3.636   50.678  203.721 1.00 47.85  ? 507 ASN D N     1 
ATOM   15587 C CA    . ASN D  1 507 ? 2.924   51.950  203.784 1.00 43.42  ? 507 ASN D CA    1 
ATOM   15588 C C     . ASN D  1 507 ? 3.715   53.022  204.533 1.00 41.58  ? 507 ASN D C     1 
ATOM   15589 O O     . ASN D  1 507 ? 3.206   54.116  204.778 1.00 39.10  ? 507 ASN D O     1 
ATOM   15590 C CB    . ASN D  1 507 ? 1.552   51.764  204.433 1.00 48.84  ? 507 ASN D CB    1 
ATOM   15591 C CG    . ASN D  1 507 ? 0.627   50.898  203.600 1.00 51.96  ? 507 ASN D CG    1 
ATOM   15592 O OD1   . ASN D  1 507 ? 0.061   49.924  204.094 1.00 59.49  ? 507 ASN D OD1   1 
ATOM   15593 N ND2   . ASN D  1 507 ? 0.476   51.244  202.326 1.00 54.85  ? 507 ASN D ND2   1 
ATOM   15594 N N     . ASN D  1 508 ? 4.955   52.692  204.894 1.00 41.94  ? 508 ASN D N     1 
ATOM   15595 C CA    . ASN D  1 508 ? 5.894   53.640  205.497 1.00 39.10  ? 508 ASN D CA    1 
ATOM   15596 C C     . ASN D  1 508 ? 5.353   54.332  206.745 1.00 38.09  ? 508 ASN D C     1 
ATOM   15597 O O     . ASN D  1 508 ? 5.504   55.543  206.902 1.00 44.62  ? 508 ASN D O     1 
ATOM   15598 C CB    . ASN D  1 508 ? 6.306   54.697  204.468 1.00 38.88  ? 508 ASN D CB    1 
ATOM   15599 C CG    . ASN D  1 508 ? 7.650   55.333  204.784 1.00 44.13  ? 508 ASN D CG    1 
ATOM   15600 O OD1   . ASN D  1 508 ? 8.520   54.709  205.387 1.00 40.88  ? 508 ASN D OD1   1 
ATOM   15601 N ND2   . ASN D  1 508 ? 7.822   56.585  204.373 1.00 40.87  ? 508 ASN D ND2   1 
ATOM   15602 N N     . VAL D  1 509 ? 4.717   53.562  207.622 1.00 39.62  ? 509 VAL D N     1 
ATOM   15603 C CA    . VAL D  1 509 ? 4.179   54.097  208.869 1.00 33.16  ? 509 VAL D CA    1 
ATOM   15604 C C     . VAL D  1 509 ? 5.314   54.554  209.783 1.00 42.33  ? 509 VAL D C     1 
ATOM   15605 O O     . VAL D  1 509 ? 5.188   55.548  210.503 1.00 40.14  ? 509 VAL D O     1 
ATOM   15606 C CB    . VAL D  1 509 ? 3.297   53.052  209.592 1.00 35.63  ? 509 VAL D CB    1 
ATOM   15607 C CG1   . VAL D  1 509 ? 2.868   53.549  210.966 1.00 36.34  ? 509 VAL D CG1   1 
ATOM   15608 C CG2   . VAL D  1 509 ? 2.077   52.722  208.740 1.00 39.61  ? 509 VAL D CG2   1 
ATOM   15609 N N     . PHE D  1 510 ? 6.430   53.834  209.738 1.00 35.06  ? 510 PHE D N     1 
ATOM   15610 C CA    . PHE D  1 510 ? 7.597   54.195  210.531 1.00 36.96  ? 510 PHE D CA    1 
ATOM   15611 C C     . PHE D  1 510 ? 8.634   54.877  209.653 1.00 37.57  ? 510 PHE D C     1 
ATOM   15612 O O     . PHE D  1 510 ? 9.337   54.231  208.878 1.00 38.70  ? 510 PHE D O     1 
ATOM   15613 C CB    . PHE D  1 510 ? 8.182   52.962  211.220 1.00 33.42  ? 510 PHE D CB    1 
ATOM   15614 C CG    . PHE D  1 510 ? 7.236   52.321  212.190 1.00 34.16  ? 510 PHE D CG    1 
ATOM   15615 C CD1   . PHE D  1 510 ? 7.203   52.723  213.517 1.00 26.95  ? 510 PHE D CD1   1 
ATOM   15616 C CD2   . PHE D  1 510 ? 6.356   51.340  211.770 1.00 33.49  ? 510 PHE D CD2   1 
ATOM   15617 C CE1   . PHE D  1 510 ? 6.318   52.143  214.408 1.00 32.53  ? 510 PHE D CE1   1 
ATOM   15618 C CE2   . PHE D  1 510 ? 5.469   50.760  212.654 1.00 31.08  ? 510 PHE D CE2   1 
ATOM   15619 C CZ    . PHE D  1 510 ? 5.452   51.160  213.977 1.00 28.29  ? 510 PHE D CZ    1 
ATOM   15620 N N     . ASN D  1 511 ? 8.704   56.198  209.776 1.00 34.51  ? 511 ASN D N     1 
ATOM   15621 C CA    . ASN D  1 511 ? 9.562   57.011  208.929 1.00 42.07  ? 511 ASN D CA    1 
ATOM   15622 C C     . ASN D  1 511 ? 10.237  58.143  209.695 1.00 36.75  ? 511 ASN D C     1 
ATOM   15623 O O     . ASN D  1 511 ? 9.753   58.573  210.743 1.00 39.06  ? 511 ASN D O     1 
ATOM   15624 C CB    . ASN D  1 511 ? 8.751   57.595  207.771 1.00 41.88  ? 511 ASN D CB    1 
ATOM   15625 C CG    . ASN D  1 511 ? 7.640   58.515  208.245 1.00 45.11  ? 511 ASN D CG    1 
ATOM   15626 O OD1   . ASN D  1 511 ? 7.875   59.684  208.551 1.00 45.23  ? 511 ASN D OD1   1 
ATOM   15627 N ND2   . ASN D  1 511 ? 6.423   57.988  208.314 1.00 42.48  ? 511 ASN D ND2   1 
ATOM   15628 N N     . HIS D  1 512 ? 11.357  58.620  209.163 1.00 41.80  ? 512 HIS D N     1 
ATOM   15629 C CA    . HIS D  1 512 ? 12.027  59.807  209.685 1.00 31.09  ? 512 HIS D CA    1 
ATOM   15630 C C     . HIS D  1 512 ? 12.899  60.358  208.545 1.00 40.20  ? 512 HIS D C     1 
ATOM   15631 O O     . HIS D  1 512 ? 12.938  59.740  207.481 1.00 42.65  ? 512 HIS D O     1 
ATOM   15632 C CB    . HIS D  1 512 ? 12.815  59.470  210.966 1.00 34.68  ? 512 HIS D CB    1 
ATOM   15633 C CG    . HIS D  1 512 ? 13.905  58.463  210.781 1.00 39.14  ? 512 HIS D CG    1 
ATOM   15634 N ND1   . HIS D  1 512 ? 15.008  58.690  209.987 1.00 39.12  ? 512 HIS D ND1   1 
ATOM   15635 C CD2   . HIS D  1 512 ? 14.079  57.235  211.323 1.00 40.76  ? 512 HIS D CD2   1 
ATOM   15636 C CE1   . HIS D  1 512 ? 15.807  57.639  210.035 1.00 39.24  ? 512 HIS D CE1   1 
ATOM   15637 N NE2   . HIS D  1 512 ? 15.266  56.742  210.840 1.00 37.99  ? 512 HIS D NE2   1 
ATOM   15638 N N     . PRO D  1 513 ? 13.565  61.523  208.731 1.00 39.87  ? 513 PRO D N     1 
ATOM   15639 C CA    . PRO D  1 513 ? 14.295  62.119  207.600 1.00 42.63  ? 513 PRO D CA    1 
ATOM   15640 C C     . PRO D  1 513 ? 15.251  61.202  206.827 1.00 44.57  ? 513 PRO D C     1 
ATOM   15641 O O     . PRO D  1 513 ? 15.527  61.489  205.663 1.00 49.16  ? 513 PRO D O     1 
ATOM   15642 C CB    . PRO D  1 513 ? 15.089  63.244  208.267 1.00 44.19  ? 513 PRO D CB    1 
ATOM   15643 C CG    . PRO D  1 513 ? 14.217  63.693  209.360 1.00 40.72  ? 513 PRO D CG    1 
ATOM   15644 C CD    . PRO D  1 513 ? 13.519  62.455  209.876 1.00 39.36  ? 513 PRO D CD    1 
ATOM   15645 N N     . GLN D  1 514 ? 15.748  60.133  207.440 1.00 41.53  ? 514 GLN D N     1 
ATOM   15646 C CA    . GLN D  1 514 ? 16.683  59.256  206.738 1.00 41.31  ? 514 GLN D CA    1 
ATOM   15647 C C     . GLN D  1 514 ? 16.293  57.782  206.812 1.00 42.05  ? 514 GLN D C     1 
ATOM   15648 O O     . GLN D  1 514 ? 17.134  56.905  206.628 1.00 45.10  ? 514 GLN D O     1 
ATOM   15649 C CB    . GLN D  1 514 ? 18.100  59.445  207.284 1.00 43.76  ? 514 GLN D CB    1 
ATOM   15650 C CG    . GLN D  1 514 ? 18.736  60.770  206.894 1.00 46.93  ? 514 GLN D CG    1 
ATOM   15651 C CD    . GLN D  1 514 ? 20.182  60.871  207.335 1.00 51.64  ? 514 GLN D CD    1 
ATOM   15652 O OE1   . GLN D  1 514 ? 20.654  60.065  208.134 1.00 46.22  ? 514 GLN D OE1   1 
ATOM   15653 N NE2   . GLN D  1 514 ? 20.898  61.857  206.806 1.00 50.35  ? 514 GLN D NE2   1 
ATOM   15654 N N     . SER D  1 515 ? 15.018  57.513  207.065 1.00 39.02  ? 515 SER D N     1 
ATOM   15655 C CA    . SER D  1 515 ? 14.540  56.137  207.148 1.00 41.80  ? 515 SER D CA    1 
ATOM   15656 C C     . SER D  1 515 ? 14.566  55.450  205.782 1.00 40.74  ? 515 SER D C     1 
ATOM   15657 O O     . SER D  1 515 ? 14.328  56.088  204.753 1.00 46.39  ? 515 SER D O     1 
ATOM   15658 C CB    . SER D  1 515 ? 13.126  56.095  207.733 1.00 37.77  ? 515 SER D CB    1 
ATOM   15659 O OG    . SER D  1 515 ? 12.221  56.848  206.943 1.00 40.26  ? 515 SER D OG    1 
ATOM   15660 N N     . ILE D  1 516 ? 14.872  54.154  205.783 1.00 40.26  ? 516 ILE D N     1 
ATOM   15661 C CA    . ILE D  1 516 ? 14.882  53.353  204.561 1.00 40.19  ? 516 ILE D CA    1 
ATOM   15662 C C     . ILE D  1 516 ? 13.526  53.396  203.867 1.00 48.49  ? 516 ILE D C     1 
ATOM   15663 O O     . ILE D  1 516 ? 12.503  53.098  204.482 1.00 44.06  ? 516 ILE D O     1 
ATOM   15664 C CB    . ILE D  1 516 ? 15.245  51.881  204.848 1.00 38.04  ? 516 ILE D CB    1 
ATOM   15665 C CG1   . ILE D  1 516 ? 16.584  51.783  205.582 1.00 40.81  ? 516 ILE D CG1   1 
ATOM   15666 C CG2   . ILE D  1 516 ? 15.296  51.080  203.555 1.00 43.44  ? 516 ILE D CG2   1 
ATOM   15667 C CD1   . ILE D  1 516 ? 17.775  52.150  204.726 1.00 35.67  ? 516 ILE D CD1   1 
ATOM   15668 N N     . PRO D  1 517 ? 13.510  53.780  202.583 1.00 51.58  ? 517 PRO D N     1 
ATOM   15669 C CA    . PRO D  1 517 ? 12.241  53.816  201.855 1.00 45.49  ? 517 PRO D CA    1 
ATOM   15670 C C     . PRO D  1 517 ? 11.851  52.440  201.327 1.00 46.00  ? 517 PRO D C     1 
ATOM   15671 O O     . PRO D  1 517 ? 12.729  51.614  201.079 1.00 45.64  ? 517 PRO D O     1 
ATOM   15672 C CB    . PRO D  1 517 ? 12.534  54.777  200.705 1.00 46.84  ? 517 PRO D CB    1 
ATOM   15673 C CG    . PRO D  1 517 ? 13.981  54.542  200.418 1.00 51.04  ? 517 PRO D CG    1 
ATOM   15674 C CD    . PRO D  1 517 ? 14.633  54.257  201.755 1.00 45.28  ? 517 PRO D CD    1 
ATOM   15675 N N     . PRO D  1 518 ? 10.544  52.190  201.167 1.00 48.68  ? 518 PRO D N     1 
ATOM   15676 C CA    . PRO D  1 518 ? 10.095  50.963  200.508 1.00 48.34  ? 518 PRO D CA    1 
ATOM   15677 C C     . PRO D  1 518 ? 10.246  51.098  198.998 1.00 54.13  ? 518 PRO D C     1 
ATOM   15678 O O     . PRO D  1 518 ? 10.541  52.194  198.522 1.00 54.80  ? 518 PRO D O     1 
ATOM   15679 C CB    . PRO D  1 518 ? 8.629   50.862  200.922 1.00 50.28  ? 518 PRO D CB    1 
ATOM   15680 C CG    . PRO D  1 518 ? 8.208   52.279  201.089 1.00 47.61  ? 518 PRO D CG    1 
ATOM   15681 C CD    . PRO D  1 518 ? 9.412   53.015  201.627 1.00 42.10  ? 518 PRO D CD    1 
ATOM   15682 N N     . MET D  1 519 ? 10.036  50.014  198.258 1.00 54.39  ? 519 MET D N     1 
ATOM   15683 C CA    . MET D  1 519 ? 10.349  49.994  196.832 1.00 56.05  ? 519 MET D CA    1 
ATOM   15684 C C     . MET D  1 519 ? 9.496   50.962  196.009 1.00 58.58  ? 519 MET D C     1 
ATOM   15685 O O     . MET D  1 519 ? 9.837   51.270  194.867 1.00 62.96  ? 519 MET D O     1 
ATOM   15686 C CB    . MET D  1 519 ? 10.195  48.576  196.279 1.00 58.89  ? 519 MET D CB    1 
ATOM   15687 C CG    . MET D  1 519 ? 8.779   48.037  196.372 1.00 57.37  ? 519 MET D CG    1 
ATOM   15688 S SD    . MET D  1 519 ? 8.587   46.362  195.732 1.00 70.98  ? 519 MET D SD    1 
ATOM   15689 C CE    . MET D  1 519 ? 9.181   46.545  194.058 1.00 50.65  ? 519 MET D CE    1 
ATOM   15690 N N     . ALA D  1 520 ? 8.398   51.443  196.588 1.00 62.04  ? 520 ALA D N     1 
ATOM   15691 C CA    . ALA D  1 520 ? 7.510   52.367  195.888 1.00 61.43  ? 520 ALA D CA    1 
ATOM   15692 C C     . ALA D  1 520 ? 6.628   53.167  196.843 1.00 64.87  ? 520 ALA D C     1 
ATOM   15693 O O     . ALA D  1 520 ? 6.554   52.871  198.036 1.00 66.06  ? 520 ALA D O     1 
ATOM   15694 C CB    . ALA D  1 520 ? 6.644   51.613  194.897 1.00 68.21  ? 520 ALA D CB    1 
ATOM   15695 N N     . ASN D  1 521 ? 5.960   54.182  196.299 1.00 67.65  ? 521 ASN D N     1 
ATOM   15696 C CA    . ASN D  1 521 ? 5.029   55.004  197.065 1.00 69.51  ? 521 ASN D CA    1 
ATOM   15697 C C     . ASN D  1 521 ? 3.647   54.358  197.099 1.00 74.11  ? 521 ASN D C     1 
ATOM   15698 O O     . ASN D  1 521 ? 2.718   54.816  196.432 1.00 78.66  ? 521 ASN D O     1 
ATOM   15699 C CB    . ASN D  1 521 ? 4.949   56.417  196.471 1.00 69.05  ? 521 ASN D CB    1 
ATOM   15700 C CG    . ASN D  1 521 ? 4.163   57.388  197.345 1.00 71.66  ? 521 ASN D CG    1 
ATOM   15701 O OD1   . ASN D  1 521 ? 3.481   56.988  198.289 1.00 74.37  ? 521 ASN D OD1   1 
ATOM   15702 N ND2   . ASN D  1 521 ? 4.249   58.674  197.020 1.00 71.26  ? 521 ASN D ND2   1 
ATOM   15703 N N     . PHE D  1 522 ? 3.527   53.287  197.878 1.00 72.56  ? 522 PHE D N     1 
ATOM   15704 C CA    . PHE D  1 522 ? 2.265   52.567  198.020 1.00 68.87  ? 522 PHE D CA    1 
ATOM   15705 C C     . PHE D  1 522 ? 1.159   53.470  198.559 1.00 78.75  ? 522 PHE D C     1 
ATOM   15706 O O     . PHE D  1 522 ? 0.885   53.480  199.758 1.00 78.86  ? 522 PHE D O     1 
ATOM   15707 C CB    . PHE D  1 522 ? 2.435   51.359  198.942 1.00 66.71  ? 522 PHE D CB    1 
ATOM   15708 C CG    . PHE D  1 522 ? 3.345   50.297  198.398 1.00 66.44  ? 522 PHE D CG    1 
ATOM   15709 C CD1   . PHE D  1 522 ? 2.846   49.285  197.594 1.00 64.57  ? 522 PHE D CD1   1 
ATOM   15710 C CD2   . PHE D  1 522 ? 4.697   50.297  198.704 1.00 64.52  ? 522 PHE D CD2   1 
ATOM   15711 C CE1   . PHE D  1 522 ? 3.678   48.299  197.098 1.00 66.04  ? 522 PHE D CE1   1 
ATOM   15712 C CE2   . PHE D  1 522 ? 5.534   49.315  198.211 1.00 61.88  ? 522 PHE D CE2   1 
ATOM   15713 C CZ    . PHE D  1 522 ? 5.024   48.315  197.406 1.00 63.60  ? 522 PHE D CZ    1 
HETATM 15714 P PA    . FAD E  2 .   ? 16.594  30.728  173.742 1.00 36.63  ? 601 FAD A PA    1 
HETATM 15715 O O1A   . FAD E  2 .   ? 16.713  29.298  174.196 1.00 29.79  ? 601 FAD A O1A   1 
HETATM 15716 O O2A   . FAD E  2 .   ? 15.668  31.099  172.609 1.00 31.99  ? 601 FAD A O2A   1 
HETATM 15717 O O5B   . FAD E  2 .   ? 16.284  31.635  175.035 1.00 28.48  ? 601 FAD A O5B   1 
HETATM 15718 C C5B   . FAD E  2 .   ? 17.090  31.524  176.211 1.00 28.87  ? 601 FAD A C5B   1 
HETATM 15719 C C4B   . FAD E  2 .   ? 16.352  32.113  177.404 1.00 26.49  ? 601 FAD A C4B   1 
HETATM 15720 O O4B   . FAD E  2 .   ? 15.942  33.451  177.101 1.00 31.03  ? 601 FAD A O4B   1 
HETATM 15721 C C3B   . FAD E  2 .   ? 15.093  31.317  177.696 1.00 27.94  ? 601 FAD A C3B   1 
HETATM 15722 O O3B   . FAD E  2 .   ? 14.862  31.312  179.102 1.00 32.21  ? 601 FAD A O3B   1 
HETATM 15723 C C2B   . FAD E  2 .   ? 13.994  32.113  177.031 1.00 30.09  ? 601 FAD A C2B   1 
HETATM 15724 O O2B   . FAD E  2 .   ? 12.747  31.918  177.699 1.00 31.92  ? 601 FAD A O2B   1 
HETATM 15725 C C1B   . FAD E  2 .   ? 14.510  33.538  177.149 1.00 30.87  ? 601 FAD A C1B   1 
HETATM 15726 N N9A   . FAD E  2 .   ? 14.035  34.406  176.045 1.00 28.90  ? 601 FAD A N9A   1 
HETATM 15727 C C8A   . FAD E  2 .   ? 14.177  34.182  174.725 1.00 31.51  ? 601 FAD A C8A   1 
HETATM 15728 N N7A   . FAD E  2 .   ? 13.629  35.191  174.000 1.00 33.17  ? 601 FAD A N7A   1 
HETATM 15729 C C5A   . FAD E  2 .   ? 13.121  36.087  174.870 1.00 29.19  ? 601 FAD A C5A   1 
HETATM 15730 C C6A   . FAD E  2 .   ? 12.402  37.379  174.781 1.00 24.26  ? 601 FAD A C6A   1 
HETATM 15731 N N6A   . FAD E  2 .   ? 12.104  37.940  173.587 1.00 27.87  ? 601 FAD A N6A   1 
HETATM 15732 N N1A   . FAD E  2 .   ? 12.052  37.987  175.934 1.00 28.24  ? 601 FAD A N1A   1 
HETATM 15733 C C2A   . FAD E  2 .   ? 12.337  37.446  177.131 1.00 29.47  ? 601 FAD A C2A   1 
HETATM 15734 N N3A   . FAD E  2 .   ? 12.986  36.278  177.289 1.00 29.30  ? 601 FAD A N3A   1 
HETATM 15735 C C4A   . FAD E  2 .   ? 13.394  35.560  176.215 1.00 26.08  ? 601 FAD A C4A   1 
HETATM 15736 N N1    . FAD E  2 .   ? 26.893  33.378  174.531 1.00 31.00  ? 601 FAD A N1    1 
HETATM 15737 C C2    . FAD E  2 .   ? 27.786  34.383  174.569 1.00 41.95  ? 601 FAD A C2    1 
HETATM 15738 O O2    . FAD E  2 .   ? 27.679  35.249  175.467 1.00 31.50  ? 601 FAD A O2    1 
HETATM 15739 N N3    . FAD E  2 .   ? 28.796  34.498  173.685 1.00 40.84  ? 601 FAD A N3    1 
HETATM 15740 C C4    . FAD E  2 .   ? 28.985  33.612  172.697 1.00 35.95  ? 601 FAD A C4    1 
HETATM 15741 O O4    . FAD E  2 .   ? 29.922  33.742  171.880 1.00 43.41  ? 601 FAD A O4    1 
HETATM 15742 C C4X   . FAD E  2 .   ? 28.035  32.481  172.587 1.00 34.63  ? 601 FAD A C4X   1 
HETATM 15743 N N5    . FAD E  2 .   ? 28.141  31.551  171.633 1.00 36.87  ? 601 FAD A N5    1 
HETATM 15744 C C5X   . FAD E  2 .   ? 27.175  30.644  171.450 1.00 37.26  ? 601 FAD A C5X   1 
HETATM 15745 C C6    . FAD E  2 .   ? 27.219  29.819  170.337 1.00 42.49  ? 601 FAD A C6    1 
HETATM 15746 C C7    . FAD E  2 .   ? 26.219  28.876  170.145 1.00 37.76  ? 601 FAD A C7    1 
HETATM 15747 C C7M   . FAD E  2 .   ? 26.286  27.982  168.938 1.00 44.42  ? 601 FAD A C7M   1 
HETATM 15748 C C8    . FAD E  2 .   ? 25.097  28.736  171.114 1.00 40.38  ? 601 FAD A C8    1 
HETATM 15749 C C8M   . FAD E  2 .   ? 24.019  27.704  170.870 1.00 33.09  ? 601 FAD A C8M   1 
HETATM 15750 C C9    . FAD E  2 .   ? 25.052  29.564  172.231 1.00 33.13  ? 601 FAD A C9    1 
HETATM 15751 C C9A   . FAD E  2 .   ? 26.055  30.511  172.427 1.00 37.60  ? 601 FAD A C9A   1 
HETATM 15752 N N10   . FAD E  2 .   ? 26.030  31.365  173.546 1.00 37.63  ? 601 FAD A N10   1 
HETATM 15753 C C10   . FAD E  2 .   ? 26.955  32.423  173.597 1.00 35.41  ? 601 FAD A C10   1 
HETATM 15754 C "C1'" . FAD E  2 .   ? 24.955  31.262  174.531 1.00 33.23  ? 601 FAD A "C1'" 1 
HETATM 15755 C "C2'" . FAD E  2 .   ? 23.844  32.255  174.236 1.00 33.54  ? 601 FAD A "C2'" 1 
HETATM 15756 O "O2'" . FAD E  2 .   ? 24.267  33.583  174.550 1.00 26.91  ? 601 FAD A "O2'" 1 
HETATM 15757 C "C3'" . FAD E  2 .   ? 22.652  31.921  175.106 1.00 29.80  ? 601 FAD A "C3'" 1 
HETATM 15758 O "O3'" . FAD E  2 .   ? 22.287  30.561  174.848 1.00 31.20  ? 601 FAD A "O3'" 1 
HETATM 15759 C "C4'" . FAD E  2 .   ? 21.502  32.848  174.755 1.00 34.16  ? 601 FAD A "C4'" 1 
HETATM 15760 O "O4'" . FAD E  2 .   ? 20.683  33.047  175.912 1.00 30.49  ? 601 FAD A "O4'" 1 
HETATM 15761 C "C5'" . FAD E  2 .   ? 20.706  32.237  173.611 1.00 30.10  ? 601 FAD A "C5'" 1 
HETATM 15762 O "O5'" . FAD E  2 .   ? 19.625  33.086  173.248 1.00 33.93  ? 601 FAD A "O5'" 1 
HETATM 15763 P P     . FAD E  2 .   ? 18.443  32.425  172.393 1.00 35.98  ? 601 FAD A P     1 
HETATM 15764 O O1P   . FAD E  2 .   ? 17.308  33.411  172.302 1.00 35.48  ? 601 FAD A O1P   1 
HETATM 15765 O O2P   . FAD E  2 .   ? 19.026  31.777  171.163 1.00 34.35  ? 601 FAD A O2P   1 
HETATM 15766 O O3P   . FAD E  2 .   ? 18.077  31.254  173.429 1.00 33.17  ? 601 FAD A O3P   1 
HETATM 15767 C C1    . NAG F  3 .   ? 3.113   30.408  160.716 1.00 55.51  ? 602 NAG A C1    1 
HETATM 15768 C C2    . NAG F  3 .   ? 2.489   30.343  159.319 1.00 57.11  ? 602 NAG A C2    1 
HETATM 15769 C C3    . NAG F  3 .   ? 3.388   29.570  158.358 1.00 58.57  ? 602 NAG A C3    1 
HETATM 15770 C C4    . NAG F  3 .   ? 4.806   30.135  158.385 1.00 58.81  ? 602 NAG A C4    1 
HETATM 15771 C C5    . NAG F  3 .   ? 5.318   30.164  159.821 1.00 52.11  ? 602 NAG A C5    1 
HETATM 15772 C C6    . NAG F  3 .   ? 6.696   30.771  159.956 1.00 50.86  ? 602 NAG A C6    1 
HETATM 15773 C C7    . NAG F  3 .   ? 0.040   30.445  159.426 1.00 56.36  ? 602 NAG A C7    1 
HETATM 15774 C C8    . NAG F  3 .   ? -1.235  29.656  159.485 1.00 51.18  ? 602 NAG A C8    1 
HETATM 15775 N N2    . NAG F  3 .   ? 1.164   29.733  159.375 1.00 55.70  ? 602 NAG A N2    1 
HETATM 15776 O O3    . NAG F  3 .   ? 2.858   29.651  157.042 1.00 65.28  ? 602 NAG A O3    1 
HETATM 15777 O O4    . NAG F  3 .   ? 5.666   29.339  157.581 1.00 60.74  ? 602 NAG A O4    1 
HETATM 15778 O O5    . NAG F  3 .   ? 4.433   30.956  160.623 1.00 52.87  ? 602 NAG A O5    1 
HETATM 15779 O O6    . NAG F  3 .   ? 6.793   32.017  159.281 1.00 53.03  ? 602 NAG A O6    1 
HETATM 15780 O O7    . NAG F  3 .   ? 0.043   31.672  159.423 1.00 57.61  ? 602 NAG A O7    1 
HETATM 15781 C C1    . NAG G  3 .   ? 6.287   29.912  156.435 1.00 65.93  ? 603 NAG A C1    1 
HETATM 15782 C C2    . NAG G  3 .   ? 7.463   28.973  156.208 1.00 64.60  ? 603 NAG A C2    1 
HETATM 15783 C C3    . NAG G  3 .   ? 8.286   29.461  155.015 1.00 69.95  ? 603 NAG A C3    1 
HETATM 15784 C C4    . NAG G  3 .   ? 7.398   29.638  153.794 1.00 74.17  ? 603 NAG A C4    1 
HETATM 15785 C C5    . NAG G  3 .   ? 6.217   30.544  154.134 1.00 74.80  ? 603 NAG A C5    1 
HETATM 15786 C C6    . NAG G  3 .   ? 5.220   30.666  153.006 1.00 79.87  ? 603 NAG A C6    1 
HETATM 15787 C C7    . NAG G  3 .   ? 8.471   27.699  158.036 1.00 58.44  ? 603 NAG A C7    1 
HETATM 15788 C C8    . NAG G  3 .   ? 9.348   27.757  159.243 1.00 50.64  ? 603 NAG A C8    1 
HETATM 15789 N N2    . NAG G  3 .   ? 8.283   28.853  157.385 1.00 60.20  ? 603 NAG A N2    1 
HETATM 15790 O O3    . NAG G  3 .   ? 9.325   28.524  154.739 1.00 70.65  ? 603 NAG A O3    1 
HETATM 15791 O O4    . NAG G  3 .   ? 8.139   30.210  152.722 1.00 76.10  ? 603 NAG A O4    1 
HETATM 15792 O O5    . NAG G  3 .   ? 5.497   30.010  155.259 1.00 72.53  ? 603 NAG A O5    1 
HETATM 15793 O O6    . NAG G  3 .   ? 3.918   30.275  153.422 1.00 80.12  ? 603 NAG A O6    1 
HETATM 15794 O O7    . NAG G  3 .   ? 7.949   26.653  157.658 1.00 58.87  ? 603 NAG A O7    1 
HETATM 15795 C C1    . NAG H  3 .   ? 9.211   20.213  198.771 1.00 79.16  ? 604 NAG A C1    1 
HETATM 15796 C C2    . NAG H  3 .   ? 9.248   18.697  198.883 1.00 82.94  ? 604 NAG A C2    1 
HETATM 15797 C C3    . NAG H  3 .   ? 9.781   18.291  200.253 1.00 82.80  ? 604 NAG A C3    1 
HETATM 15798 C C4    . NAG H  3 .   ? 11.134  18.940  200.506 1.00 83.40  ? 604 NAG A C4    1 
HETATM 15799 C C5    . NAG H  3 .   ? 11.047  20.452  200.300 1.00 81.56  ? 604 NAG A C5    1 
HETATM 15800 C C6    . NAG H  3 .   ? 12.393  21.136  200.381 1.00 81.97  ? 604 NAG A C6    1 
HETATM 15801 C C7    . NAG H  3 .   ? 7.726   17.154  197.741 1.00 85.24  ? 604 NAG A C7    1 
HETATM 15802 C C8    . NAG H  3 .   ? 6.315   16.665  197.621 1.00 87.82  ? 604 NAG A C8    1 
HETATM 15803 N N2    . NAG H  3 .   ? 7.940   18.116  198.646 1.00 83.74  ? 604 NAG A N2    1 
HETATM 15804 O O3    . NAG H  3 .   ? 9.894   16.873  200.314 1.00 87.88  ? 604 NAG A O3    1 
HETATM 15805 O O4    . NAG H  3 .   ? 11.564  18.675  201.837 1.00 82.35  ? 604 NAG A O4    1 
HETATM 15806 O O5    . NAG H  3 .   ? 10.515  20.746  198.998 1.00 82.78  ? 604 NAG A O5    1 
HETATM 15807 O O6    . NAG H  3 .   ? 13.080  21.084  199.138 1.00 78.34  ? 604 NAG A O6    1 
HETATM 15808 O O7    . NAG H  3 .   ? 8.634   16.699  197.052 1.00 86.32  ? 604 NAG A O7    1 
HETATM 15809 P PA    . FAD I  2 .   ? -15.085 22.155  222.306 1.00 38.53  ? 601 FAD B PA    1 
HETATM 15810 O O1A   . FAD I  2 .   ? -16.451 21.958  222.906 1.00 34.92  ? 601 FAD B O1A   1 
HETATM 15811 O O2A   . FAD I  2 .   ? -14.858 23.202  221.241 1.00 36.60  ? 601 FAD B O2A   1 
HETATM 15812 O O5B   . FAD I  2 .   ? -14.029 22.350  223.508 1.00 36.13  ? 601 FAD B O5B   1 
HETATM 15813 C C5B   . FAD I  2 .   ? -14.079 21.521  224.669 1.00 30.47  ? 601 FAD B C5B   1 
HETATM 15814 C C4B   . FAD I  2 .   ? -13.532 22.287  225.861 1.00 36.31  ? 601 FAD B C4B   1 
HETATM 15815 O O4B   . FAD I  2 .   ? -12.259 22.844  225.516 1.00 34.49  ? 601 FAD B O4B   1 
HETATM 15816 C C3B   . FAD I  2 .   ? -14.450 23.446  226.211 1.00 37.89  ? 601 FAD B C3B   1 
HETATM 15817 O O3B   . FAD I  2 .   ? -14.472 23.621  227.629 1.00 41.97  ? 601 FAD B O3B   1 
HETATM 15818 C C2B   . FAD I  2 .   ? -13.797 24.650  225.578 1.00 32.76  ? 601 FAD B C2B   1 
HETATM 15819 O O2B   . FAD I  2 .   ? -14.054 25.830  226.345 1.00 34.92  ? 601 FAD B O2B   1 
HETATM 15820 C C1B   . FAD I  2 .   ? -12.327 24.271  225.586 1.00 31.66  ? 601 FAD B C1B   1 
HETATM 15821 N N9A   . FAD I  2 .   ? -11.595 24.849  224.434 1.00 33.42  ? 601 FAD B N9A   1 
HETATM 15822 C C8A   . FAD I  2 .   ? -11.914 24.760  223.128 1.00 31.41  ? 601 FAD B C8A   1 
HETATM 15823 N N7A   . FAD I  2 .   ? -11.003 25.415  222.364 1.00 34.99  ? 601 FAD B N7A   1 
HETATM 15824 C C5A   . FAD I  2 .   ? -10.079 25.938  223.198 1.00 34.36  ? 601 FAD B C5A   1 
HETATM 15825 C C6A   . FAD I  2 .   ? -8.845  26.752  223.073 1.00 28.95  ? 601 FAD B C6A   1 
HETATM 15826 N N6A   . FAD I  2 .   ? -8.381  27.155  221.869 1.00 30.21  ? 601 FAD B N6A   1 
HETATM 15827 N N1A   . FAD I  2 .   ? -8.189  27.076  224.205 1.00 31.57  ? 601 FAD B N1A   1 
HETATM 15828 C C2A   . FAD I  2 .   ? -8.619  26.688  225.419 1.00 34.19  ? 601 FAD B C2A   1 
HETATM 15829 N N3A   . FAD I  2 .   ? -9.727  25.952  225.610 1.00 32.65  ? 601 FAD B N3A   1 
HETATM 15830 C C4A   . FAD I  2 .   ? -10.482 25.560  224.558 1.00 35.32  ? 601 FAD B C4A   1 
HETATM 15831 N N1    . FAD I  2 .   ? -11.699 12.065  222.397 1.00 42.82  ? 601 FAD B N1    1 
HETATM 15832 C C2    . FAD I  2 .   ? -10.643 11.234  222.338 1.00 47.92  ? 601 FAD B C2    1 
HETATM 15833 O O2    . FAD I  2 .   ? -9.730  11.359  223.185 1.00 41.61  ? 601 FAD B O2    1 
HETATM 15834 N N3    . FAD I  2 .   ? -10.520 10.270  221.407 1.00 48.70  ? 601 FAD B N3    1 
HETATM 15835 C C4    . FAD I  2 .   ? -11.450 10.064  220.468 1.00 43.83  ? 601 FAD B C4    1 
HETATM 15836 O O4    . FAD I  2 .   ? -11.314 9.167   219.607 1.00 44.07  ? 601 FAD B O4    1 
HETATM 15837 C C4X   . FAD I  2 .   ? -12.640 10.948  220.464 1.00 43.69  ? 601 FAD B C4X   1 
HETATM 15838 N N5    . FAD I  2 .   ? -13.618 10.818  219.562 1.00 49.21  ? 601 FAD B N5    1 
HETATM 15839 C C5X   . FAD I  2 .   ? -14.601 11.723  219.482 1.00 43.41  ? 601 FAD B C5X   1 
HETATM 15840 C C6    . FAD I  2 .   ? -15.500 11.662  218.427 1.00 45.47  ? 601 FAD B C6    1 
HETATM 15841 C C7    . FAD I  2 .   ? -16.521 12.597  218.337 1.00 41.52  ? 601 FAD B C7    1 
HETATM 15842 C C7M   . FAD I  2 .   ? -17.496 12.518  217.194 1.00 42.80  ? 601 FAD B C7M   1 
HETATM 15843 C C8    . FAD I  2 .   ? -16.664 13.666  219.361 1.00 42.81  ? 601 FAD B C8    1 
HETATM 15844 C C8M   . FAD I  2 .   ? -17.779 14.676  219.239 1.00 35.59  ? 601 FAD B C8M   1 
HETATM 15845 C C9    . FAD I  2 .   ? -15.765 13.731  220.419 1.00 39.68  ? 601 FAD B C9    1 
HETATM 15846 C C9A   . FAD I  2 .   ? -14.740 12.794  220.511 1.00 44.89  ? 601 FAD B C9A   1 
HETATM 15847 N N10   . FAD I  2 .   ? -13.816 12.848  221.573 1.00 38.51  ? 601 FAD B N10   1 
HETATM 15848 C C10   . FAD I  2 .   ? -12.704 11.986  221.520 1.00 43.80  ? 601 FAD B C10   1 
HETATM 15849 C "C1'" . FAD I  2 .   ? -13.937 13.882  222.604 1.00 41.41  ? 601 FAD B "C1'" 1 
HETATM 15850 C "C2'" . FAD I  2 .   ? -13.033 15.075  222.342 1.00 34.18  ? 601 FAD B "C2'" 1 
HETATM 15851 O "O2'" . FAD I  2 .   ? -11.664 14.690  222.478 1.00 34.21  ? 601 FAD B "O2'" 1 
HETATM 15852 C "C3'" . FAD I  2 .   ? -13.350 16.164  223.350 1.00 39.08  ? 601 FAD B "C3'" 1 
HETATM 15853 O "O3'" . FAD I  2 .   ? -14.750 16.462  223.241 1.00 39.76  ? 601 FAD B "O3'" 1 
HETATM 15854 C "C4'" . FAD I  2 .   ? -12.551 17.422  223.040 1.00 35.96  ? 601 FAD B "C4'" 1 
HETATM 15855 O "O4'" . FAD I  2 .   ? -12.506 18.254  224.200 1.00 38.24  ? 601 FAD B "O4'" 1 
HETATM 15856 C "C5'" . FAD I  2 .   ? -13.215 18.144  221.876 1.00 34.43  ? 601 FAD B "C5'" 1 
HETATM 15857 O "O5'" . FAD I  2 .   ? -12.614 19.407  221.629 1.00 32.17  ? 601 FAD B "O5'" 1 
HETATM 15858 P P     . FAD I  2 .   ? -13.436 20.464  220.736 1.00 39.09  ? 601 FAD B P     1 
HETATM 15859 O O1P   . FAD I  2 .   ? -12.615 21.716  220.577 1.00 36.27  ? 601 FAD B O1P   1 
HETATM 15860 O O2P   . FAD I  2 .   ? -14.036 19.771  219.537 1.00 42.15  ? 601 FAD B O2P   1 
HETATM 15861 O O3P   . FAD I  2 .   ? -14.621 20.715  221.783 1.00 37.37  ? 601 FAD B O3P   1 
HETATM 15862 C C1    . NAG J  3 .   ? -17.292 36.155  210.141 1.00 58.22  ? 602 NAG B C1    1 
HETATM 15863 C C2    . NAG J  3 .   ? -17.504 36.885  208.809 1.00 68.23  ? 602 NAG B C2    1 
HETATM 15864 C C3    . NAG J  3 .   ? -18.213 35.972  207.807 1.00 66.86  ? 602 NAG B C3    1 
HETATM 15865 C C4    . NAG J  3 .   ? -17.475 34.647  207.679 1.00 69.21  ? 602 NAG B C4    1 
HETATM 15866 C C5    . NAG J  3 .   ? -17.328 34.017  209.058 1.00 63.20  ? 602 NAG B C5    1 
HETATM 15867 C C6    . NAG J  3 .   ? -16.567 32.712  209.043 1.00 56.36  ? 602 NAG B C6    1 
HETATM 15868 C C7    . NAG J  3 .   ? -17.690 39.315  209.106 1.00 63.36  ? 602 NAG B C7    1 
HETATM 15869 C C8    . NAG J  3 .   ? -18.625 40.470  209.300 1.00 59.65  ? 602 NAG B C8    1 
HETATM 15870 N N2    . NAG J  3 .   ? -18.260 38.110  209.002 1.00 65.51  ? 602 NAG B N2    1 
HETATM 15871 O O3    . NAG J  3 .   ? -18.287 36.618  206.541 1.00 70.07  ? 602 NAG B O3    1 
HETATM 15872 O O4    . NAG J  3 .   ? -18.189 33.764  206.821 1.00 68.56  ? 602 NAG B O4    1 
HETATM 15873 O O5    . NAG J  3 .   ? -16.604 34.916  209.912 1.00 56.38  ? 602 NAG B O5    1 
HETATM 15874 O O6    . NAG J  3 .   ? -15.342 32.828  208.331 1.00 61.20  ? 602 NAG B O6    1 
HETATM 15875 O O7    . NAG J  3 .   ? -16.474 39.465  209.047 1.00 63.16  ? 602 NAG B O7    1 
HETATM 15876 C C1    . NAG K  3 .   ? -17.570 33.372  205.606 1.00 69.82  ? 603 NAG B C1    1 
HETATM 15877 C C2    . NAG K  3 .   ? -18.507 32.188  205.372 1.00 71.92  ? 603 NAG B C2    1 
HETATM 15878 C C3    . NAG K  3 .   ? -18.133 31.462  204.084 1.00 78.06  ? 603 NAG B C3    1 
HETATM 15879 C C4    . NAG K  3 .   ? -18.085 32.445  202.919 1.00 76.82  ? 603 NAG B C4    1 
HETATM 15880 C C5    . NAG K  3 .   ? -17.162 33.611  203.259 1.00 77.58  ? 603 NAG B C5    1 
HETATM 15881 C C6    . NAG K  3 .   ? -17.140 34.681  202.192 1.00 81.04  ? 603 NAG B C6    1 
HETATM 15882 C C7    . NAG K  3 .   ? -19.564 30.933  207.200 1.00 69.51  ? 603 NAG B C7    1 
HETATM 15883 C C8    . NAG K  3 .   ? -19.349 29.969  208.330 1.00 68.19  ? 603 NAG B C8    1 
HETATM 15884 N N2    . NAG K  3 .   ? -18.476 31.266  206.503 1.00 69.64  ? 603 NAG B N2    1 
HETATM 15885 O O3    . NAG K  3 .   ? -19.082 30.437  203.821 1.00 84.06  ? 603 NAG B O3    1 
HETATM 15886 O O4    . NAG K  3 .   ? -17.613 31.793  201.746 1.00 80.26  ? 603 NAG B O4    1 
HETATM 15887 O O5    . NAG K  3 .   ? -17.608 34.240  204.469 1.00 73.76  ? 603 NAG B O5    1 
HETATM 15888 O O6    . NAG K  3 .   ? -17.840 35.846  202.606 1.00 78.57  ? 603 NAG B O6    1 
HETATM 15889 O O7    . NAG K  3 .   ? -20.675 31.386  206.936 1.00 68.90  ? 603 NAG B O7    1 
HETATM 15890 C C1    . NAG L  3 .   ? -24.429 27.349  248.852 1.00 95.12  ? 604 NAG B C1    1 
HETATM 15891 C C2    . NAG L  3 .   ? -25.957 27.296  248.929 1.00 95.27  ? 604 NAG B C2    1 
HETATM 15892 C C3    . NAG L  3 .   ? -26.401 26.468  250.137 1.00 100.06 ? 604 NAG B C3    1 
HETATM 15893 C C4    . NAG L  3 .   ? -25.723 25.105  250.132 1.00 102.70 ? 604 NAG B C4    1 
HETATM 15894 C C5    . NAG L  3 .   ? -24.212 25.286  250.042 1.00 100.71 ? 604 NAG B C5    1 
HETATM 15895 C C6    . NAG L  3 .   ? -23.454 23.981  249.969 1.00 97.25  ? 604 NAG B C6    1 
HETATM 15896 C C7    . NAG L  3 .   ? -27.645 28.983  248.360 1.00 94.29  ? 604 NAG B C7    1 
HETATM 15897 C C8    . NAG L  3 .   ? -28.080 30.407  248.535 1.00 93.13  ? 604 NAG B C8    1 
HETATM 15898 N N2    . NAG L  3 .   ? -26.521 28.631  248.992 1.00 96.94  ? 604 NAG B N2    1 
HETATM 15899 O O3    . NAG L  3 .   ? -27.815 26.310  250.106 1.00 99.58  ? 604 NAG B O3    1 
HETATM 15900 O O4    . NAG L  3 .   ? -26.045 24.387  251.318 1.00 106.45 ? 604 NAG B O4    1 
HETATM 15901 O O5    . NAG L  3 .   ? -23.895 26.022  248.851 1.00 95.48  ? 604 NAG B O5    1 
HETATM 15902 O O6    . NAG L  3 .   ? -23.971 23.129  248.956 1.00 99.49  ? 604 NAG B O6    1 
HETATM 15903 O O7    . NAG L  3 .   ? -28.282 28.187  247.678 1.00 97.81  ? 604 NAG B O7    1 
HETATM 15904 S S     . SO4 M  4 .   ? -7.555  47.373  212.985 1.00 73.81  ? 605 SO4 B S     1 
HETATM 15905 O O1    . SO4 M  4 .   ? -8.018  45.989  212.918 1.00 66.37  ? 605 SO4 B O1    1 
HETATM 15906 O O2    . SO4 M  4 .   ? -7.511  47.934  211.638 1.00 72.81  ? 605 SO4 B O2    1 
HETATM 15907 O O3    . SO4 M  4 .   ? -6.215  47.409  213.567 1.00 68.52  ? 605 SO4 B O3    1 
HETATM 15908 O O4    . SO4 M  4 .   ? -8.470  48.156  213.813 1.00 60.01  ? 605 SO4 B O4    1 
HETATM 15909 P PA    . FAD N  2 .   ? -15.267 64.845  168.885 1.00 39.07  ? 601 FAD C PA    1 
HETATM 15910 O O1A   . FAD N  2 .   ? -16.639 64.958  168.278 1.00 40.60  ? 601 FAD C O1A   1 
HETATM 15911 O O2A   . FAD N  2 .   ? -15.030 63.955  170.085 1.00 34.46  ? 601 FAD C O2A   1 
HETATM 15912 O O5B   . FAD N  2 .   ? -14.219 64.464  167.724 1.00 34.42  ? 601 FAD C O5B   1 
HETATM 15913 C C5B   . FAD N  2 .   ? -14.167 65.208  166.506 1.00 28.24  ? 601 FAD C C5B   1 
HETATM 15914 C C4B   . FAD N  2 .   ? -13.637 64.311  165.400 1.00 29.88  ? 601 FAD C C4B   1 
HETATM 15915 O O4B   . FAD N  2 .   ? -12.365 63.779  165.788 1.00 35.15  ? 601 FAD C O4B   1 
HETATM 15916 C C3B   . FAD N  2 .   ? -14.568 63.130  165.190 1.00 29.93  ? 601 FAD C C3B   1 
HETATM 15917 O O3B   . FAD N  2 .   ? -14.607 62.803  163.800 1.00 33.97  ? 601 FAD C O3B   1 
HETATM 15918 C C2B   . FAD N  2 .   ? -13.917 61.992  165.941 1.00 30.90  ? 601 FAD C C2B   1 
HETATM 15919 O O2B   . FAD N  2 .   ? -14.201 60.749  165.296 1.00 34.40  ? 601 FAD C O2B   1 
HETATM 15920 C C1B   . FAD N  2 .   ? -12.440 62.353  165.897 1.00 33.14  ? 601 FAD C C1B   1 
HETATM 15921 N N9A   . FAD N  2 .   ? -11.705 61.924  167.113 1.00 37.52  ? 601 FAD C N9A   1 
HETATM 15922 C C8A   . FAD N  2 .   ? -12.030 62.167  168.397 1.00 37.99  ? 601 FAD C C8A   1 
HETATM 15923 N N7A   . FAD N  2 .   ? -11.115 61.620  169.242 1.00 33.33  ? 601 FAD C N7A   1 
HETATM 15924 C C5A   . FAD N  2 .   ? -10.177 61.010  168.489 1.00 34.32  ? 601 FAD C C5A   1 
HETATM 15925 C C6A   . FAD N  2 .   ? -8.934  60.236  168.721 1.00 28.45  ? 601 FAD C C6A   1 
HETATM 15926 N N6A   . FAD N  2 .   ? -8.467  59.983  169.966 1.00 30.13  ? 601 FAD C N6A   1 
HETATM 15927 N N1A   . FAD N  2 .   ? -8.265  59.784  167.640 1.00 28.89  ? 601 FAD C N1A   1 
HETATM 15928 C C2A   . FAD N  2 .   ? -8.694  60.017  166.388 1.00 33.50  ? 601 FAD C C2A   1 
HETATM 15929 N N3A   . FAD N  2 .   ? -9.809  60.709  166.101 1.00 33.46  ? 601 FAD C N3A   1 
HETATM 15930 C C4A   . FAD N  2 .   ? -10.579 61.217  167.089 1.00 31.86  ? 601 FAD C C4A   1 
HETATM 15931 N N1    . FAD N  2 .   ? -12.018 74.950  167.486 1.00 41.32  ? 601 FAD C N1    1 
HETATM 15932 C C2    . FAD N  2 .   ? -10.985 75.806  167.410 1.00 53.01  ? 601 FAD C C2    1 
HETATM 15933 O O2    . FAD N  2 .   ? -10.087 75.589  166.568 1.00 48.36  ? 601 FAD C O2    1 
HETATM 15934 N N3    . FAD N  2 .   ? -10.871 76.889  168.202 1.00 48.01  ? 601 FAD C N3    1 
HETATM 15935 C C4    . FAD N  2 .   ? -11.786 77.193  169.128 1.00 49.30  ? 601 FAD C C4    1 
HETATM 15936 O O4    . FAD N  2 .   ? -11.659 78.201  169.858 1.00 52.64  ? 601 FAD C O4    1 
HETATM 15937 C C4X   . FAD N  2 .   ? -12.953 76.292  169.274 1.00 50.32  ? 601 FAD C C4X   1 
HETATM 15938 N N5    . FAD N  2 .   ? -13.916 76.521  170.174 1.00 49.64  ? 601 FAD C N5    1 
HETATM 15939 C C5X   . FAD N  2 .   ? -14.886 75.620  170.377 1.00 49.94  ? 601 FAD C C5X   1 
HETATM 15940 C C6    . FAD N  2 .   ? -15.791 75.804  171.415 1.00 51.69  ? 601 FAD C C6    1 
HETATM 15941 C C7    . FAD N  2 .   ? -16.797 74.869  171.632 1.00 50.34  ? 601 FAD C C7    1 
HETATM 15942 C C7M   . FAD N  2 .   ? -17.779 75.072  172.752 1.00 46.47  ? 601 FAD C C7M   1 
HETATM 15943 C C8    . FAD N  2 .   ? -16.916 73.672  170.758 1.00 48.26  ? 601 FAD C C8    1 
HETATM 15944 C C8M   . FAD N  2 .   ? -18.008 72.660  171.004 1.00 41.00  ? 601 FAD C C8M   1 
HETATM 15945 C C9    . FAD N  2 .   ? -16.014 73.486  169.719 1.00 49.19  ? 601 FAD C C9    1 
HETATM 15946 C C9A   . FAD N  2 .   ? -15.008 74.419  169.502 1.00 45.65  ? 601 FAD C C9A   1 
HETATM 15947 N N10   . FAD N  2 .   ? -14.090 74.232  168.454 1.00 46.84  ? 601 FAD C N10   1 
HETATM 15948 C C10   . FAD N  2 .   ? -13.005 75.122  168.367 1.00 44.46  ? 601 FAD C C10   1 
HETATM 15949 C "C1'" . FAD N  2 .   ? -14.198 73.063  167.574 1.00 43.16  ? 601 FAD C "C1'" 1 
HETATM 15950 C "C2'" . FAD N  2 .   ? -13.300 71.912  168.001 1.00 38.65  ? 601 FAD C "C2'" 1 
HETATM 15951 O "O2'" . FAD N  2 .   ? -11.929 72.280  167.857 1.00 38.33  ? 601 FAD C "O2'" 1 
HETATM 15952 C "C3'" . FAD N  2 .   ? -13.586 70.717  167.111 1.00 40.31  ? 601 FAD C "C3'" 1 
HETATM 15953 O "O3'" . FAD N  2 .   ? -14.989 70.426  167.191 1.00 41.81  ? 601 FAD C "O3'" 1 
HETATM 15954 C "C4'" . FAD N  2 .   ? -12.797 69.508  167.583 1.00 38.33  ? 601 FAD C "C4'" 1 
HETATM 15955 O "O4'" . FAD N  2 .   ? -12.791 68.511  166.557 1.00 40.56  ? 601 FAD C "O4'" 1 
HETATM 15956 C "C5'" . FAD N  2 .   ? -13.437 68.964  168.851 1.00 37.08  ? 601 FAD C "C5'" 1 
HETATM 15957 O "O5'" . FAD N  2 .   ? -12.810 67.750  169.249 1.00 31.78  ? 601 FAD C "O5'" 1 
HETATM 15958 P P     . FAD N  2 .   ? -13.626 66.749  170.209 1.00 38.93  ? 601 FAD C P     1 
HETATM 15959 O O1P   . FAD N  2 .   ? -12.769 65.547  170.507 1.00 37.05  ? 601 FAD C O1P   1 
HETATM 15960 O O2P   . FAD N  2 .   ? -14.291 67.518  171.324 1.00 43.37  ? 601 FAD C O2P   1 
HETATM 15961 O O3P   . FAD N  2 .   ? -14.777 66.347  169.165 1.00 39.64  ? 601 FAD C O3P   1 
HETATM 15962 C C1    . NAG O  3 .   ? -17.174 52.125  182.755 1.00 58.39  ? 602 NAG C C1    1 
HETATM 15963 C C2    . NAG O  3 .   ? -17.451 51.681  184.199 1.00 64.70  ? 602 NAG C C2    1 
HETATM 15964 C C3    . NAG O  3 .   ? -18.200 52.772  184.963 1.00 63.09  ? 602 NAG C C3    1 
HETATM 15965 C C4    . NAG O  3 .   ? -17.459 54.098  184.856 1.00 65.99  ? 602 NAG C C4    1 
HETATM 15966 C C5    . NAG O  3 .   ? -17.263 54.441  183.385 1.00 60.38  ? 602 NAG C C5    1 
HETATM 15967 C C6    . NAG O  3 .   ? -16.511 55.732  183.167 1.00 54.87  ? 602 NAG C C6    1 
HETATM 15968 C C7    . NAG O  3 .   ? -17.645 49.232  184.109 1.00 67.11  ? 602 NAG C C7    1 
HETATM 15969 C C8    . NAG O  3 .   ? -18.584 48.064  184.150 1.00 62.88  ? 602 NAG C C8    1 
HETATM 15970 N N2    . NAG O  3 .   ? -18.210 50.438  184.220 1.00 67.54  ? 602 NAG C N2    1 
HETATM 15971 O O3    . NAG O  3 .   ? -18.340 52.397  186.327 1.00 68.11  ? 602 NAG C O3    1 
HETATM 15972 O O4    . NAG O  3 .   ? -18.193 55.131  185.502 1.00 64.58  ? 602 NAG C O4    1 
HETATM 15973 O O5    . NAG O  3 .   ? -16.502 53.398  182.761 1.00 56.07  ? 602 NAG C O5    1 
HETATM 15974 O O6    . NAG O  3 .   ? -15.398 55.843  184.044 1.00 55.81  ? 602 NAG C O6    1 
HETATM 15975 O O7    . NAG O  3 .   ? -16.434 49.089  183.982 1.00 67.55  ? 602 NAG C O7    1 
HETATM 15976 C C1    . NAG P  3 .   ? -17.570 55.583  186.704 1.00 67.32  ? 603 NAG C C1    1 
HETATM 15977 C C2    . NAG P  3 .   ? -18.513 56.784  186.731 1.00 70.19  ? 603 NAG C C2    1 
HETATM 15978 C C3    . NAG P  3 .   ? -18.171 57.699  187.908 1.00 78.49  ? 603 NAG C C3    1 
HETATM 15979 C C4    . NAG P  3 .   ? -18.114 56.909  189.207 1.00 78.74  ? 603 NAG C C4    1 
HETATM 15980 C C5    . NAG P  3 .   ? -17.180 55.713  189.054 1.00 76.55  ? 603 NAG C C5    1 
HETATM 15981 C C6    . NAG P  3 .   ? -17.156 54.820  190.273 1.00 78.23  ? 603 NAG C C6    1 
HETATM 15982 C C7    . NAG P  3 .   ? -19.535 57.937  184.819 1.00 65.49  ? 603 NAG C C7    1 
HETATM 15983 C C8    . NAG P  3 .   ? -19.277 58.679  183.542 1.00 63.19  ? 603 NAG C C8    1 
HETATM 15984 N N2    . NAG P  3 .   ? -18.451 57.518  185.481 1.00 67.23  ? 603 NAG C N2    1 
HETATM 15985 O O3    . NAG P  3 .   ? -19.155 58.724  188.005 1.00 72.85  ? 603 NAG C O3    1 
HETATM 15986 O O4    . NAG P  3 .   ? -17.646 57.737  190.266 1.00 80.78  ? 603 NAG C O4    1 
HETATM 15987 O O5    . NAG P  3 .   ? -17.618 54.902  187.953 1.00 70.33  ? 603 NAG C O5    1 
HETATM 15988 O O6    . NAG P  3 .   ? -16.658 53.525  189.963 1.00 75.54  ? 603 NAG C O6    1 
HETATM 15989 O O7    . NAG P  3 .   ? -20.672 57.726  185.232 1.00 69.51  ? 603 NAG C O7    1 
HETATM 15990 C C1    . NAG Q  3 .   ? -24.793 56.595  143.660 1.00 93.21  ? 604 NAG C C1    1 
HETATM 15991 C C2    . NAG Q  3 .   ? -26.323 56.742  143.704 1.00 93.00  ? 604 NAG C C2    1 
HETATM 15992 C C3    . NAG Q  3 .   ? -26.841 57.465  142.455 1.00 95.24  ? 604 NAG C C3    1 
HETATM 15993 C C4    . NAG Q  3 .   ? -26.063 58.748  142.200 1.00 99.35  ? 604 NAG C C4    1 
HETATM 15994 C C5    . NAG Q  3 .   ? -24.580 58.421  142.138 1.00 99.48  ? 604 NAG C C5    1 
HETATM 15995 C C6    . NAG Q  3 .   ? -23.702 59.623  141.872 1.00 94.03  ? 604 NAG C C6    1 
HETATM 15996 C C7    . NAG Q  3 .   ? -27.560 55.007  144.932 1.00 88.28  ? 604 NAG C C7    1 
HETATM 15997 C C8    . NAG Q  3 .   ? -28.142 53.627  144.869 1.00 83.85  ? 604 NAG C C8    1 
HETATM 15998 N N2    . NAG Q  3 .   ? -26.948 55.435  143.823 1.00 89.25  ? 604 NAG C N2    1 
HETATM 15999 O O3    . NAG Q  3 .   ? -28.224 57.760  142.617 1.00 96.30  ? 604 NAG C O3    1 
HETATM 16000 O O4    . NAG Q  3 .   ? -26.472 59.341  140.973 1.00 103.61 ? 604 NAG C O4    1 
HETATM 16001 O O5    . NAG Q  3 .   ? -24.187 57.870  143.400 1.00 98.59  ? 604 NAG C O5    1 
HETATM 16002 O O6    . NAG Q  3 .   ? -23.356 60.305  143.070 1.00 91.66  ? 604 NAG C O6    1 
HETATM 16003 O O7    . NAG Q  3 .   ? -27.645 55.703  145.938 1.00 88.10  ? 604 NAG C O7    1 
HETATM 16004 O O37   . 12P R  5 .   ? 11.567  46.530  163.421 1.00 52.31  ? 605 12P C O37   1 
HETATM 16005 C C36   . 12P R  5 .   ? 11.051  46.594  164.749 1.00 43.51  ? 605 12P C C36   1 
HETATM 16006 C C35   . 12P R  5 .   ? 10.735  48.041  165.091 1.00 49.47  ? 605 12P C C35   1 
HETATM 16007 O O34   . 12P R  5 .   ? 10.362  48.138  166.463 1.00 52.33  ? 605 12P C O34   1 
HETATM 16008 C C33   . 12P R  5 .   ? 10.147  49.503  166.815 1.00 48.58  ? 605 12P C C33   1 
HETATM 16009 C C32   . 12P R  5 .   ? 9.406   49.593  168.136 1.00 44.07  ? 605 12P C C32   1 
HETATM 16010 O O31   . 12P R  5 .   ? 8.798   50.879  168.203 1.00 60.25  ? 605 12P C O31   1 
HETATM 16011 C C30   . 12P R  5 .   ? 7.761   50.876  169.170 1.00 45.52  ? 605 12P C C30   1 
HETATM 16012 C C29   . 12P R  5 .   ? 6.601   51.710  168.653 1.00 45.70  ? 605 12P C C29   1 
HETATM 16013 O O28   . 12P R  5 .   ? 5.466   51.285  169.394 1.00 46.82  ? 605 12P C O28   1 
HETATM 16014 C C27   . 12P R  5 .   ? 5.159   52.238  170.402 1.00 36.34  ? 605 12P C C27   1 
HETATM 16015 C C26   . 12P R  5 .   ? 4.465   51.530  171.555 1.00 42.32  ? 605 12P C C26   1 
HETATM 16016 O O25   . 12P R  5 .   ? 5.257   51.696  172.727 1.00 50.37  ? 605 12P C O25   1 
HETATM 16017 C C24   . 12P R  5 .   ? 4.428   51.852  173.869 1.00 40.09  ? 605 12P C C24   1 
HETATM 16018 C C23   . 12P R  5 .   ? 5.273   52.354  175.027 1.00 40.22  ? 605 12P C C23   1 
HETATM 16019 O O22   . 12P R  5 .   ? 4.447   53.199  175.820 1.00 51.68  ? 605 12P C O22   1 
HETATM 16020 C C21   . 12P R  5 .   ? 4.933   54.529  175.747 1.00 49.30  ? 605 12P C C21   1 
HETATM 16021 C C20   . 12P R  5 .   ? 3.753   55.461  175.535 1.00 50.65  ? 605 12P C C20   1 
HETATM 16022 O O19   . 12P R  5 .   ? 3.496   56.108  176.775 1.00 55.83  ? 605 12P C O19   1 
HETATM 16023 C C18   . 12P R  5 .   ? 3.920   57.462  176.676 1.00 49.97  ? 605 12P C C18   1 
HETATM 16024 C C17   . 12P R  5 .   ? 3.695   58.183  177.995 1.00 51.47  ? 605 12P C C17   1 
HETATM 16025 O O16   . 12P R  5 .   ? 2.687   57.551  178.781 1.00 65.13  ? 605 12P C O16   1 
HETATM 16026 C C15   . 12P R  5 .   ? 2.706   58.133  180.083 1.00 57.43  ? 605 12P C C15   1 
HETATM 16027 C C14   . 12P R  5 .   ? 1.366   57.961  180.780 1.00 57.99  ? 605 12P C C14   1 
HETATM 16028 O O13   . 12P R  5 .   ? 0.681   56.841  180.231 1.00 68.41  ? 605 12P C O13   1 
HETATM 16029 C C12   . 12P R  5 .   ? 0.783   55.732  181.116 1.00 60.38  ? 605 12P C C12   1 
HETATM 16030 C C11   . 12P R  5 .   ? -0.529  54.968  181.178 1.00 54.64  ? 605 12P C C11   1 
HETATM 16031 O O10   . 12P R  5 .   ? -0.289  53.766  181.916 1.00 60.97  ? 605 12P C O10   1 
HETATM 16032 S S     . SO4 S  4 .   ? -7.402  40.688  181.074 1.00 68.89  ? 606 SO4 C S     1 
HETATM 16033 O O1    . SO4 S  4 .   ? -6.191  40.986  180.315 1.00 73.79  ? 606 SO4 C O1    1 
HETATM 16034 O O2    . SO4 S  4 .   ? -8.300  39.872  180.259 1.00 60.70  ? 606 SO4 C O2    1 
HETATM 16035 O O3    . SO4 S  4 .   ? -7.051  39.953  182.285 1.00 73.57  ? 606 SO4 C O3    1 
HETATM 16036 O O4    . SO4 S  4 .   ? -8.063  41.937  181.437 1.00 62.30  ? 606 SO4 C O4    1 
HETATM 16037 S S     . SO4 T  4 .   ? 4.168   79.400  152.884 0.65 69.30  ? 607 SO4 C S     1 
HETATM 16038 O O1    . SO4 T  4 .   ? 5.508   79.693  152.380 0.65 63.28  ? 607 SO4 C O1    1 
HETATM 16039 O O2    . SO4 T  4 .   ? 3.172   79.794  151.891 0.65 56.26  ? 607 SO4 C O2    1 
HETATM 16040 O O3    . SO4 T  4 .   ? 4.059   77.968  153.144 0.65 57.44  ? 607 SO4 C O3    1 
HETATM 16041 O O4    . SO4 T  4 .   ? 3.939   80.139  154.122 0.65 59.36  ? 607 SO4 C O4    1 
HETATM 16042 P PA    . FAD U  2 .   ? 16.450  56.859  220.960 1.00 37.11  ? 601 FAD D PA    1 
HETATM 16043 O O1A   . FAD U  2 .   ? 16.544  58.305  220.554 1.00 30.73  ? 601 FAD D O1A   1 
HETATM 16044 O O2A   . FAD U  2 .   ? 15.448  56.401  221.994 1.00 30.99  ? 601 FAD D O2A   1 
HETATM 16045 O O5B   . FAD U  2 .   ? 16.269  55.981  219.622 1.00 33.39  ? 601 FAD D O5B   1 
HETATM 16046 C C5B   . FAD U  2 .   ? 16.998  56.298  218.437 1.00 32.68  ? 601 FAD D C5B   1 
HETATM 16047 C C4B   . FAD U  2 .   ? 16.226  55.832  217.213 1.00 29.24  ? 601 FAD D C4B   1 
HETATM 16048 O O4B   . FAD U  2 .   ? 15.795  54.480  217.400 1.00 33.25  ? 601 FAD D O4B   1 
HETATM 16049 C C3B   . FAD U  2 .   ? 14.977  56.676  217.035 1.00 30.91  ? 601 FAD D C3B   1 
HETATM 16050 O O3B   . FAD U  2 .   ? 14.721  56.843  215.641 1.00 38.05  ? 601 FAD D O3B   1 
HETATM 16051 C C2B   . FAD U  2 .   ? 13.875  55.841  217.649 1.00 30.35  ? 601 FAD D C2B   1 
HETATM 16052 O O2B   . FAD U  2 .   ? 12.622  56.105  217.016 1.00 32.60  ? 601 FAD D O2B   1 
HETATM 16053 C C1B   . FAD U  2 .   ? 14.363  54.423  217.400 1.00 31.67  ? 601 FAD D C1B   1 
HETATM 16054 N N9A   . FAD U  2 .   ? 13.911  53.466  218.440 1.00 31.28  ? 601 FAD D N9A   1 
HETATM 16055 C C8A   . FAD U  2 .   ? 14.063  53.578  219.774 1.00 29.87  ? 601 FAD D C8A   1 
HETATM 16056 N N7A   . FAD U  2 .   ? 13.533  52.503  220.414 1.00 32.18  ? 601 FAD D N7A   1 
HETATM 16057 C C5A   . FAD U  2 .   ? 13.026  51.678  219.473 1.00 29.05  ? 601 FAD D C5A   1 
HETATM 16058 C C6A   . FAD U  2 .   ? 12.321  50.373  219.452 1.00 28.66  ? 601 FAD D C6A   1 
HETATM 16059 N N6A   . FAD U  2 .   ? 12.040  49.703  220.592 1.00 28.24  ? 601 FAD D N6A   1 
HETATM 16060 N N1A   . FAD U  2 .   ? 11.970  49.868  218.252 1.00 29.71  ? 601 FAD D N1A   1 
HETATM 16061 C C2A   . FAD U  2 .   ? 12.239  50.516  217.103 1.00 31.54  ? 601 FAD D C2A   1 
HETATM 16062 N N3A   . FAD U  2 .   ? 12.873  51.701  217.047 1.00 27.21  ? 601 FAD D N3A   1 
HETATM 16063 C C4A   . FAD U  2 .   ? 13.281  52.325  218.178 1.00 26.84  ? 601 FAD D C4A   1 
HETATM 16064 N N1    . FAD U  2 .   ? 26.696  54.370  219.954 1.00 35.61  ? 601 FAD D N1    1 
HETATM 16065 C C2    . FAD U  2 .   ? 27.584  53.370  219.820 1.00 43.49  ? 601 FAD D C2    1 
HETATM 16066 O O2    . FAD U  2 .   ? 27.455  52.580  218.858 1.00 35.50  ? 601 FAD D O2    1 
HETATM 16067 N N3    . FAD U  2 .   ? 28.608  53.184  220.676 1.00 42.90  ? 601 FAD D N3    1 
HETATM 16068 C C4    . FAD U  2 .   ? 28.817  53.987  221.726 1.00 43.73  ? 601 FAD D C4    1 
HETATM 16069 O O4    . FAD U  2 .   ? 29.770  53.791  222.511 1.00 50.47  ? 601 FAD D O4    1 
HETATM 16070 C C4X   . FAD U  2 .   ? 27.874  55.110  221.945 1.00 43.00  ? 601 FAD D C4X   1 
HETATM 16071 N N5    . FAD U  2 .   ? 28.002  55.965  222.970 1.00 47.75  ? 601 FAD D N5    1 
HETATM 16072 C C5X   . FAD U  2 .   ? 27.037  56.856  223.245 1.00 47.13  ? 601 FAD D C5X   1 
HETATM 16073 C C6    . FAD U  2 .   ? 27.085  57.606  224.415 1.00 47.50  ? 601 FAD D C6    1 
HETATM 16074 C C7    . FAD U  2 .   ? 26.081  58.527  224.695 1.00 45.90  ? 601 FAD D C7    1 
HETATM 16075 C C7M   . FAD U  2 .   ? 26.139  59.338  225.961 1.00 42.22  ? 601 FAD D C7M   1 
HETATM 16076 C C8    . FAD U  2 .   ? 24.949  58.723  223.752 1.00 45.55  ? 601 FAD D C8    1 
HETATM 16077 C C8M   . FAD U  2 .   ? 23.866  59.723  224.074 1.00 37.57  ? 601 FAD D C8M   1 
HETATM 16078 C C9    . FAD U  2 .   ? 24.898  57.977  222.581 1.00 40.61  ? 601 FAD D C9    1 
HETATM 16079 C C9A   . FAD U  2 .   ? 25.901  57.055  222.298 1.00 42.25  ? 601 FAD D C9A   1 
HETATM 16080 N N10   . FAD U  2 .   ? 25.853  56.296  221.115 1.00 39.52  ? 601 FAD D N10   1 
HETATM 16081 C C10   . FAD U  2 .   ? 26.776  55.247  220.962 1.00 40.40  ? 601 FAD D C10   1 
HETATM 16082 C "C1'" . FAD U  2 .   ? 24.753  56.479  220.169 1.00 39.69  ? 601 FAD D "C1'" 1 
HETATM 16083 C "C2'" . FAD U  2 .   ? 23.649  55.456  220.373 1.00 33.38  ? 601 FAD D "C2'" 1 
HETATM 16084 O "O2'" . FAD U  2 .   ? 24.103  54.152  219.998 1.00 32.34  ? 601 FAD D "O2'" 1 
HETATM 16085 C "C3'" . FAD U  2 .   ? 22.478  55.846  219.494 1.00 35.06  ? 601 FAD D "C3'" 1 
HETATM 16086 O "O3'" . FAD U  2 .   ? 22.106  57.195  219.816 1.00 35.08  ? 601 FAD D "O3'" 1 
HETATM 16087 C "C4'" . FAD U  2 .   ? 21.309  54.911  219.752 1.00 34.86  ? 601 FAD D "C4'" 1 
HETATM 16088 O "O4'" . FAD U  2 .   ? 20.494  54.833  218.581 1.00 35.20  ? 601 FAD D "O4'" 1 
HETATM 16089 C "C5'" . FAD U  2 .   ? 20.513  55.446  220.929 1.00 34.26  ? 601 FAD D "C5'" 1 
HETATM 16090 O "O5'" . FAD U  2 .   ? 19.462  54.554  221.275 1.00 35.29  ? 601 FAD D "O5'" 1 
HETATM 16091 P P     . FAD U  2 .   ? 18.322  55.133  222.247 1.00 40.43  ? 601 FAD D P     1 
HETATM 16092 O O1P   . FAD U  2 .   ? 17.167  54.167  222.275 1.00 32.26  ? 601 FAD D O1P   1 
HETATM 16093 O O2P   . FAD U  2 .   ? 18.959  55.623  223.525 1.00 38.20  ? 601 FAD D O2P   1 
HETATM 16094 O O3P   . FAD U  2 .   ? 17.938  56.431  221.380 1.00 31.84  ? 601 FAD D O3P   1 
HETATM 16095 C C1    . NAG V  3 .   ? 3.229   55.974  233.985 1.00 65.53  ? 602 NAG D C1    1 
HETATM 16096 C C2    . NAG V  3 .   ? 2.579   55.978  235.378 1.00 79.44  ? 602 NAG D C2    1 
HETATM 16097 C C3    . NAG V  3 .   ? 3.517   56.613  236.411 1.00 76.80  ? 602 NAG D C3    1 
HETATM 16098 C C4    . NAG V  3 .   ? 4.901   55.983  236.347 1.00 76.78  ? 602 NAG D C4    1 
HETATM 16099 C C5    . NAG V  3 .   ? 5.428   56.079  234.923 1.00 68.85  ? 602 NAG D C5    1 
HETATM 16100 C C6    . NAG V  3 .   ? 6.795   55.460  234.748 1.00 63.66  ? 602 NAG D C6    1 
HETATM 16101 C C7    . NAG V  3 .   ? 0.124   56.070  235.392 1.00 76.02  ? 602 NAG D C7    1 
HETATM 16102 C C8    . NAG V  3 .   ? -1.078  56.963  235.346 1.00 73.08  ? 602 NAG D C8    1 
HETATM 16103 N N2    . NAG V  3 .   ? 1.312   56.683  235.349 1.00 80.83  ? 602 NAG D N2    1 
HETATM 16104 O O3    . NAG V  3 .   ? 2.970   56.445  237.714 1.00 76.30  ? 602 NAG D O3    1 
HETATM 16105 O O4    . NAG V  3 .   ? 5.790   56.650  237.237 1.00 79.23  ? 602 NAG D O4    1 
HETATM 16106 O O5    . NAG V  3 .   ? 4.531   55.374  234.052 1.00 66.63  ? 602 NAG D O5    1 
HETATM 16107 O O6    . NAG V  3 .   ? 6.938   54.282  235.530 1.00 65.79  ? 602 NAG D O6    1 
HETATM 16108 O O7    . NAG V  3 .   ? 0.026   54.849  235.466 1.00 68.16  ? 602 NAG D O7    1 
HETATM 16109 C C1    . NAG W  3 .   ? 6.472   56.060  238.339 1.00 85.40  ? 603 NAG D C1    1 
HETATM 16110 C C2    . NAG W  3 .   ? 7.590   57.056  238.631 1.00 85.23  ? 603 NAG D C2    1 
HETATM 16111 C C3    . NAG W  3 .   ? 8.470   56.548  239.769 1.00 92.00  ? 603 NAG D C3    1 
HETATM 16112 C C4    . NAG W  3 .   ? 7.619   56.199  240.985 1.00 97.97  ? 603 NAG D C4    1 
HETATM 16113 C C5    . NAG W  3 .   ? 6.491   55.251  240.587 1.00 95.57  ? 603 NAG D C5    1 
HETATM 16114 C C6    . NAG W  3 .   ? 5.530   54.965  241.717 1.00 97.31  ? 603 NAG D C6    1 
HETATM 16115 C C7    . NAG W  3 .   ? 8.232   58.388  236.673 1.00 77.32  ? 603 NAG D C7    1 
HETATM 16116 C C8    . NAG W  3 .   ? 9.139   58.488  235.485 1.00 72.23  ? 603 NAG D C8    1 
HETATM 16117 N N2    . NAG W  3 .   ? 8.390   57.307  237.440 1.00 80.11  ? 603 NAG D N2    1 
HETATM 16118 O O3    . NAG W  3 .   ? 9.418   57.552  240.111 1.00 90.67  ? 603 NAG D O3    1 
HETATM 16119 O O4    . NAG W  3 .   ? 8.427   55.580  241.980 1.00 94.87  ? 603 NAG D O4    1 
HETATM 16120 O O5    . NAG W  3 .   ? 5.719   55.831  239.526 1.00 86.83  ? 603 NAG D O5    1 
HETATM 16121 O O6    . NAG W  3 .   ? 4.334   54.363  241.241 1.00 100.37 ? 603 NAG D O6    1 
HETATM 16122 O O7    . NAG W  3 .   ? 7.391   59.246  236.923 1.00 79.72  ? 603 NAG D O7    1 
HETATM 16123 C C1    . NAG X  3 .   ? 9.226   69.025  196.471 1.00 93.94  ? 604 NAG D C1    1 
HETATM 16124 C C2    . NAG X  3 .   ? 9.143   70.548  196.561 1.00 94.28  ? 604 NAG D C2    1 
HETATM 16125 C C3    . NAG X  3 .   ? 9.690   71.192  195.291 1.00 95.24  ? 604 NAG D C3    1 
HETATM 16126 C C4    . NAG X  3 .   ? 11.085  70.662  194.981 1.00 96.38  ? 604 NAG D C4    1 
HETATM 16127 C C5    . NAG X  3 .   ? 11.077  69.136  194.958 1.00 95.27  ? 604 NAG D C5    1 
HETATM 16128 C C6    . NAG X  3 .   ? 12.452  68.539  194.768 1.00 91.21  ? 604 NAG D C6    1 
HETATM 16129 C C7    . NAG X  3 .   ? 7.401   71.671  197.876 1.00 96.02  ? 604 NAG D C7    1 
HETATM 16130 C C8    . NAG X  3 .   ? 5.947   72.029  197.961 1.00 91.89  ? 604 NAG D C8    1 
HETATM 16131 N N2    . NAG X  3 .   ? 7.768   70.977  196.798 1.00 95.07  ? 604 NAG D N2    1 
HETATM 16132 O O3    . NAG X  3 .   ? 9.736   72.603  195.462 1.00 95.09  ? 604 NAG D O3    1 
HETATM 16133 O O4    . NAG X  3 .   ? 11.519  71.147  193.716 1.00 98.24  ? 604 NAG D O4    1 
HETATM 16134 O O5    . NAG X  3 .   ? 10.577  68.639  196.207 1.00 95.57  ? 604 NAG D O5    1 
HETATM 16135 O O6    . NAG X  3 .   ? 13.190  68.524  195.982 1.00 90.10  ? 604 NAG D O6    1 
HETATM 16136 O O7    . NAG X  3 .   ? 8.202   71.998  198.746 1.00 94.27  ? 604 NAG D O7    1 
HETATM 16137 O O37   . 12P Y  5 .   ? 11.131  39.875  228.898 1.00 56.28  ? 605 12P D O37   1 
HETATM 16138 C C36   . 12P Y  5 .   ? 10.723  39.684  227.542 1.00 44.47  ? 605 12P D C36   1 
HETATM 16139 C C35   . 12P Y  5 .   ? 10.253  38.248  227.380 1.00 52.05  ? 605 12P D C35   1 
HETATM 16140 O O34   . 12P Y  5 .   ? 9.859   38.000  226.031 1.00 59.08  ? 605 12P D O34   1 
HETATM 16141 C C33   . 12P Y  5 .   ? 8.666   37.219  226.005 1.00 53.75  ? 605 12P D C33   1 
HETATM 16142 C C32   . 12P Y  5 .   ? 8.679   36.238  224.844 1.00 49.47  ? 605 12P D C32   1 
HETATM 16143 O O31   . 12P Y  5 .   ? 7.582   36.525  223.980 1.00 56.75  ? 605 12P D O31   1 
HETATM 16144 C C30   . 12P Y  5 .   ? 6.376   35.948  224.478 1.00 46.78  ? 605 12P D C30   1 
HETATM 16145 C C29   . 12P Y  5 .   ? 5.576   35.295  223.356 1.00 43.13  ? 605 12P D C29   1 
HETATM 16146 O O28   . 12P Y  5 .   ? 5.441   36.153  222.225 1.00 52.02  ? 605 12P D O28   1 
HETATM 16147 C C27   . 12P Y  5 .   ? 4.653   35.509  221.226 1.00 40.95  ? 605 12P D C27   1 
HETATM 16148 C C26   . 12P Y  5 .   ? 4.953   36.099  219.856 1.00 39.65  ? 605 12P D C26   1 
HETATM 16149 O O25   . 12P Y  5 .   ? 4.619   35.138  218.857 1.00 51.08  ? 605 12P D O25   1 
HETATM 16150 C C24   . 12P Y  5 .   ? 4.979   35.611  217.564 1.00 44.14  ? 605 12P D C24   1 
HETATM 16151 C C23   . 12P Y  5 .   ? 4.725   34.532  216.522 1.00 49.26  ? 605 12P D C23   1 
HETATM 16152 O O22   . 12P Y  5 .   ? 3.912   33.495  217.063 1.00 54.34  ? 605 12P D O22   1 
HETATM 16153 C C21   . 12P Y  5 .   ? 4.253   32.249  216.461 1.00 52.10  ? 605 12P D C21   1 
HETATM 16154 C C20   . 12P Y  5 .   ? 3.154   31.862  215.493 1.00 56.39  ? 605 12P D C20   1 
HETATM 16155 O O19   . 12P Y  5 .   ? 3.527   30.645  214.856 1.00 52.84  ? 605 12P D O19   1 
HETATM 16156 C C18   . 12P Y  5 .   ? 2.740   30.451  213.687 1.00 55.89  ? 605 12P D C18   1 
HETATM 16157 C C17   . 12P Y  5 .   ? 1.404   29.861  214.111 1.00 48.49  ? 605 12P D C17   1 
HETATM 16158 O O16   . 12P Y  5 .   ? 0.563   29.713  212.970 1.00 51.31  ? 605 12P D O16   1 
HETATM 16159 S S     . SO4 Z  4 .   ? 29.776  37.132  216.381 0.65 59.62  ? 606 SO4 D S     1 
HETATM 16160 O O1    . SO4 Z  4 .   ? 30.998  36.793  215.658 0.65 57.86  ? 606 SO4 D O1    1 
HETATM 16161 O O2    . SO4 Z  4 .   ? 28.611  36.652  215.640 0.65 48.46  ? 606 SO4 D O2    1 
HETATM 16162 O O3    . SO4 Z  4 .   ? 29.808  36.526  217.710 0.65 52.47  ? 606 SO4 D O3    1 
HETATM 16163 O O4    . SO4 Z  4 .   ? 29.695  38.582  216.517 0.65 57.89  ? 606 SO4 D O4    1 
HETATM 16164 S S     . SO4 AA 4 .   ? 22.353  34.290  212.512 0.66 64.25  ? 607 SO4 D S     1 
HETATM 16165 O O1    . SO4 AA 4 .   ? 23.652  33.778  212.084 0.66 55.26  ? 607 SO4 D O1    1 
HETATM 16166 O O2    . SO4 AA 4 .   ? 21.792  35.125  211.454 0.66 52.30  ? 607 SO4 D O2    1 
HETATM 16167 O O3    . SO4 AA 4 .   ? 21.454  33.168  212.780 0.66 50.25  ? 607 SO4 D O3    1 
HETATM 16168 O O4    . SO4 AA 4 .   ? 22.515  35.088  213.724 0.66 46.33  ? 607 SO4 D O4    1 
HETATM 16169 O O     . HOH BA 6 .   ? -2.675  36.339  163.588 1.00 38.41  ? 701 HOH A O     1 
HETATM 16170 O O     . HOH BA 6 .   ? -0.112  34.940  164.853 1.00 39.66  ? 702 HOH A O     1 
HETATM 16171 O O     . HOH BA 6 .   ? 1.346   26.930  160.409 1.00 52.52  ? 703 HOH A O     1 
HETATM 16172 O O     . HOH BA 6 .   ? 0.362   20.157  162.899 1.00 49.04  ? 704 HOH A O     1 
HETATM 16173 O O     . HOH BA 6 .   ? -0.143  18.767  160.365 1.00 57.77  ? 705 HOH A O     1 
HETATM 16174 O O     . HOH BA 6 .   ? 18.866  24.462  173.197 1.00 40.91  ? 706 HOH A O     1 
HETATM 16175 O O     . HOH BA 6 .   ? 18.221  29.735  166.015 1.00 41.95  ? 707 HOH A O     1 
HETATM 16176 O O     . HOH BA 6 .   ? 15.426  30.170  165.181 1.00 45.43  ? 708 HOH A O     1 
HETATM 16177 O O     . HOH BA 6 .   ? 11.532  33.664  160.331 1.00 47.65  ? 709 HOH A O     1 
HETATM 16178 O O     . HOH BA 6 .   ? 18.056  15.201  178.515 1.00 60.02  ? 710 HOH A O     1 
HETATM 16179 O O     . HOH BA 6 .   ? 2.491   20.771  178.090 1.00 43.42  ? 711 HOH A O     1 
HETATM 16180 O O     . HOH BA 6 .   ? 6.758   34.559  166.028 1.00 34.20  ? 712 HOH A O     1 
HETATM 16181 O O     . HOH BA 6 .   ? 3.668   42.769  162.475 1.00 42.76  ? 713 HOH A O     1 
HETATM 16182 O O     . HOH BA 6 .   ? 4.741   44.809  166.161 1.00 30.70  ? 714 HOH A O     1 
HETATM 16183 O O     . HOH BA 6 .   ? 2.649   46.335  165.777 1.00 36.14  ? 715 HOH A O     1 
HETATM 16184 O O     . HOH BA 6 .   ? -1.107  44.118  165.712 1.00 41.48  ? 716 HOH A O     1 
HETATM 16185 O O     . HOH BA 6 .   ? -2.960  43.503  174.640 1.00 37.41  ? 717 HOH A O     1 
HETATM 16186 O O     . HOH BA 6 .   ? -2.521  44.415  178.662 1.00 42.87  ? 718 HOH A O     1 
HETATM 16187 O O     . HOH BA 6 .   ? 0.801   45.916  183.882 1.00 45.54  ? 719 HOH A O     1 
HETATM 16188 O O     . HOH BA 6 .   ? -1.322  34.654  187.533 1.00 53.08  ? 720 HOH A O     1 
HETATM 16189 O O     . HOH BA 6 .   ? -4.380  23.317  181.396 1.00 59.62  ? 721 HOH A O     1 
HETATM 16190 O O     . HOH BA 6 .   ? 3.651   31.296  183.306 1.00 38.45  ? 722 HOH A O     1 
HETATM 16191 O O     . HOH BA 6 .   ? 7.014   31.264  182.569 1.00 33.30  ? 723 HOH A O     1 
HETATM 16192 O O     . HOH BA 6 .   ? 8.880   27.143  185.678 1.00 43.19  ? 724 HOH A O     1 
HETATM 16193 O O     . HOH BA 6 .   ? 10.363  31.447  179.233 1.00 33.58  ? 725 HOH A O     1 
HETATM 16194 O O     . HOH BA 6 .   ? 3.537   31.470  188.971 1.00 48.81  ? 726 HOH A O     1 
HETATM 16195 O O     . HOH BA 6 .   ? 3.390   39.254  187.986 1.00 40.56  ? 727 HOH A O     1 
HETATM 16196 O O     . HOH BA 6 .   ? 6.150   40.856  183.623 1.00 41.99  ? 728 HOH A O     1 
HETATM 16197 O O     . HOH BA 6 .   ? 22.251  29.176  177.430 1.00 33.84  ? 729 HOH A O     1 
HETATM 16198 O O     . HOH BA 6 .   ? 27.421  29.857  184.461 1.00 37.29  ? 730 HOH A O     1 
HETATM 16199 O O     . HOH BA 6 .   ? 31.166  28.456  187.206 1.00 49.24  ? 731 HOH A O     1 
HETATM 16200 O O     . HOH BA 6 .   ? 34.257  30.447  187.939 1.00 38.66  ? 732 HOH A O     1 
HETATM 16201 O O     . HOH BA 6 .   ? 38.207  34.250  193.644 1.00 59.12  ? 733 HOH A O     1 
HETATM 16202 O O     . HOH BA 6 .   ? 25.103  29.666  165.528 1.00 39.95  ? 734 HOH A O     1 
HETATM 16203 O O     . HOH BA 6 .   ? 26.874  28.523  164.175 1.00 51.91  ? 735 HOH A O     1 
HETATM 16204 O O     . HOH BA 6 .   ? 14.605  42.933  158.879 1.00 48.08  ? 736 HOH A O     1 
HETATM 16205 O O     . HOH BA 6 .   ? 15.276  52.339  163.884 1.00 40.66  ? 737 HOH A O     1 
HETATM 16206 O O     . HOH BA 6 .   ? 16.353  53.647  166.057 1.00 38.70  ? 738 HOH A O     1 
HETATM 16207 O O     . HOH BA 6 .   ? 18.051  40.417  158.409 1.00 40.35  ? 739 HOH A O     1 
HETATM 16208 O O     . HOH BA 6 .   ? 30.574  45.460  156.948 1.00 50.20  ? 740 HOH A O     1 
HETATM 16209 O O     . HOH BA 6 .   ? 33.439  47.552  158.021 1.00 45.90  ? 741 HOH A O     1 
HETATM 16210 O O     . HOH BA 6 .   ? 30.431  43.696  154.197 1.00 50.98  ? 742 HOH A O     1 
HETATM 16211 O O     . HOH BA 6 .   ? 28.562  53.234  153.956 1.00 53.58  ? 743 HOH A O     1 
HETATM 16212 O O     . HOH BA 6 .   ? 31.351  41.410  170.561 1.00 40.77  ? 744 HOH A O     1 
HETATM 16213 O O     . HOH BA 6 .   ? 34.654  31.267  171.696 1.00 58.56  ? 745 HOH A O     1 
HETATM 16214 O O     . HOH BA 6 .   ? 24.670  38.546  182.793 1.00 31.54  ? 746 HOH A O     1 
HETATM 16215 O O     . HOH BA 6 .   ? 25.812  36.593  184.407 1.00 34.37  ? 747 HOH A O     1 
HETATM 16216 O O     . HOH BA 6 .   ? 24.963  42.955  181.341 1.00 37.79  ? 748 HOH A O     1 
HETATM 16217 O O     . HOH BA 6 .   ? 27.958  45.676  184.613 1.00 35.02  ? 749 HOH A O     1 
HETATM 16218 O O     . HOH BA 6 .   ? 30.192  51.951  183.997 1.00 42.70  ? 750 HOH A O     1 
HETATM 16219 O O     . HOH BA 6 .   ? 38.571  43.915  170.675 1.00 43.20  ? 751 HOH A O     1 
HETATM 16220 O O     . HOH BA 6 .   ? 36.329  40.457  172.865 1.00 36.90  ? 752 HOH A O     1 
HETATM 16221 O O     . HOH BA 6 .   ? 13.222  54.801  182.374 1.00 39.72  ? 753 HOH A O     1 
HETATM 16222 O O     . HOH BA 6 .   ? 12.877  55.048  186.892 1.00 45.36  ? 754 HOH A O     1 
HETATM 16223 O O     . HOH BA 6 .   ? 3.595   44.027  185.674 1.00 45.14  ? 755 HOH A O     1 
HETATM 16224 O O     . HOH BA 6 .   ? 14.696  39.344  179.311 1.00 35.00  ? 756 HOH A O     1 
HETATM 16225 O O     . HOH BA 6 .   ? 12.440  38.148  180.496 1.00 33.22  ? 757 HOH A O     1 
HETATM 16226 O O     . HOH BA 6 .   ? 52.979  35.358  165.544 1.00 43.61  ? 758 HOH A O     1 
HETATM 16227 O O     . HOH BA 6 .   ? 23.603  31.785  159.818 1.00 50.72  ? 759 HOH A O     1 
HETATM 16228 O O     . HOH BA 6 .   ? 40.251  36.706  174.454 1.00 36.51  ? 760 HOH A O     1 
HETATM 16229 O O     . HOH BA 6 .   ? 41.976  38.903  173.749 1.00 34.20  ? 761 HOH A O     1 
HETATM 16230 O O     . HOH BA 6 .   ? 38.033  42.680  182.631 1.00 34.07  ? 762 HOH A O     1 
HETATM 16231 O O     . HOH BA 6 .   ? 22.977  48.939  191.155 1.00 42.30  ? 763 HOH A O     1 
HETATM 16232 O O     . HOH BA 6 .   ? 23.079  50.924  187.317 1.00 44.12  ? 764 HOH A O     1 
HETATM 16233 O O     . HOH BA 6 .   ? 20.483  51.552  186.153 1.00 41.18  ? 765 HOH A O     1 
HETATM 16234 O O     . HOH BA 6 .   ? 24.985  22.738  179.305 1.00 39.06  ? 766 HOH A O     1 
HETATM 16235 O O     . HOH BA 6 .   ? 11.245  33.733  189.113 1.00 41.83  ? 767 HOH A O     1 
HETATM 16236 O O     . HOH BA 6 .   ? 17.635  35.015  185.706 1.00 36.99  ? 768 HOH A O     1 
HETATM 16237 O O     . HOH BA 6 .   ? 4.652   45.498  193.234 1.00 52.52  ? 769 HOH A O     1 
HETATM 16238 O O     . HOH BA 6 .   ? 21.124  33.649  161.447 1.00 42.07  ? 770 HOH A O     1 
HETATM 16239 O O     . HOH BA 6 .   ? 16.107  44.598  157.404 1.00 44.59  ? 771 HOH A O     1 
HETATM 16240 O O     . HOH BA 6 .   ? 11.566  54.784  176.648 1.00 36.92  ? 772 HOH A O     1 
HETATM 16241 O O     . HOH BA 6 .   ? 12.016  50.083  186.931 1.00 41.85  ? 773 HOH A O     1 
HETATM 16242 O O     . HOH BA 6 .   ? 18.671  51.709  183.880 1.00 39.30  ? 774 HOH A O     1 
HETATM 16243 O O     . HOH BA 6 .   ? 51.542  23.326  164.016 1.00 61.53  ? 775 HOH A O     1 
HETATM 16244 O O     . HOH BA 6 .   ? 43.280  44.672  182.040 1.00 60.58  ? 776 HOH A O     1 
HETATM 16245 O O     . HOH BA 6 .   ? 51.174  40.517  176.848 1.00 43.83  ? 777 HOH A O     1 
HETATM 16246 O O     . HOH BA 6 .   ? 56.384  38.298  172.996 1.00 40.27  ? 778 HOH A O     1 
HETATM 16247 O O     . HOH BA 6 .   ? 56.952  31.583  175.345 1.00 48.48  ? 779 HOH A O     1 
HETATM 16248 O O     . HOH BA 6 .   ? 52.779  37.778  163.591 1.00 49.95  ? 780 HOH A O     1 
HETATM 16249 O O     . HOH BA 6 .   ? 46.179  31.099  158.173 1.00 65.09  ? 781 HOH A O     1 
HETATM 16250 O O     . HOH BA 6 .   ? 50.908  30.522  160.702 1.00 57.26  ? 782 HOH A O     1 
HETATM 16251 O O     . HOH BA 6 .   ? 46.238  38.392  153.036 1.00 65.58  ? 783 HOH A O     1 
HETATM 16252 O O     . HOH BA 6 .   ? 44.920  35.093  183.441 1.00 45.57  ? 784 HOH A O     1 
HETATM 16253 O O     . HOH BA 6 .   ? 35.246  31.674  176.668 1.00 46.57  ? 785 HOH A O     1 
HETATM 16254 O O     . HOH BA 6 .   ? 23.465  46.554  191.950 1.00 44.03  ? 786 HOH A O     1 
HETATM 16255 O O     . HOH BA 6 .   ? 22.087  45.005  194.129 1.00 47.80  ? 787 HOH A O     1 
HETATM 16256 O O     . HOH BA 6 .   ? 34.283  43.782  188.717 1.00 42.61  ? 788 HOH A O     1 
HETATM 16257 O O     . HOH BA 6 .   ? 45.537  37.058  182.058 1.00 48.98  ? 789 HOH A O     1 
HETATM 16258 O O     . HOH BA 6 .   ? -8.145  24.980  173.549 1.00 50.25  ? 790 HOH A O     1 
HETATM 16259 O O     . HOH BA 6 .   ? 20.328  31.030  178.119 1.00 29.47  ? 791 HOH A O     1 
HETATM 16260 O O     . HOH BA 6 .   ? 9.765   20.077  174.303 1.00 45.36  ? 792 HOH A O     1 
HETATM 16261 O O     . HOH BA 6 .   ? 10.849  31.242  181.631 1.00 38.87  ? 793 HOH A O     1 
HETATM 16262 O O     . HOH BA 6 .   ? 17.577  33.508  183.213 1.00 39.07  ? 794 HOH A O     1 
HETATM 16263 O O     . HOH BA 6 .   ? 20.300  32.571  180.078 1.00 31.12  ? 795 HOH A O     1 
HETATM 16264 O O     . HOH BA 6 .   ? 15.793  40.309  159.461 1.00 46.94  ? 796 HOH A O     1 
HETATM 16265 O O     . HOH BA 6 .   ? 19.376  34.780  178.913 1.00 34.27  ? 797 HOH A O     1 
HETATM 16266 O O     . HOH BA 6 .   ? 16.872  39.896  180.757 1.00 44.09  ? 798 HOH A O     1 
HETATM 16267 O O     . HOH BA 6 .   ? 50.459  26.151  162.382 1.00 59.23  ? 799 HOH A O     1 
HETATM 16268 O O     . HOH BA 6 .   ? 28.942  47.299  158.153 1.00 48.03  ? 800 HOH A O     1 
HETATM 16269 O O     . HOH BA 6 .   ? 24.947  24.256  181.121 1.00 43.91  ? 801 HOH A O     1 
HETATM 16270 O O     . HOH BA 6 .   ? 43.334  33.635  185.040 1.00 42.88  ? 802 HOH A O     1 
HETATM 16271 O O     . HOH BA 6 .   ? 41.232  32.664  189.968 1.00 46.38  ? 803 HOH A O     1 
HETATM 16272 O O     . HOH BA 6 .   ? 34.800  47.450  186.515 1.00 42.60  ? 804 HOH A O     1 
HETATM 16273 O O     . HOH BA 6 .   ? 12.460  30.145  167.081 1.00 43.00  ? 805 HOH A O     1 
HETATM 16274 O O     . HOH CA 6 .   ? -1.104  37.949  214.167 1.00 39.37  ? 701 HOH B O     1 
HETATM 16275 O O     . HOH CA 6 .   ? -2.577  35.315  214.480 1.00 36.63  ? 702 HOH B O     1 
HETATM 16276 O O     . HOH CA 6 .   ? -11.473 42.364  212.454 1.00 42.49  ? 703 HOH B O     1 
HETATM 16277 O O     . HOH CA 6 .   ? -30.231 31.587  218.768 1.00 52.45  ? 704 HOH B O     1 
HETATM 16278 O O     . HOH CA 6 .   ? -21.160 19.428  222.043 1.00 41.51  ? 705 HOH B O     1 
HETATM 16279 O O     . HOH CA 6 .   ? -29.917 19.406  227.738 1.00 48.45  ? 706 HOH B O     1 
HETATM 16280 O O     . HOH CA 6 .   ? -26.160 27.588  223.700 1.00 45.94  ? 707 HOH B O     1 
HETATM 16281 O O     . HOH CA 6 .   ? -27.240 25.978  230.267 1.00 57.33  ? 708 HOH B O     1 
HETATM 16282 O O     . HOH CA 6 .   ? -30.946 28.093  219.035 1.00 49.04  ? 709 HOH B O     1 
HETATM 16283 O O     . HOH CA 6 .   ? -29.441 32.013  227.911 1.00 48.71  ? 710 HOH B O     1 
HETATM 16284 O O     . HOH CA 6 .   ? -25.698 34.991  227.344 1.00 41.70  ? 711 HOH B O     1 
HETATM 16285 O O     . HOH CA 6 .   ? -12.719 32.636  214.875 1.00 38.63  ? 712 HOH B O     1 
HETATM 16286 O O     . HOH CA 6 .   ? -7.075  43.375  216.621 1.00 46.47  ? 713 HOH B O     1 
HETATM 16287 O O     . HOH CA 6 .   ? -15.142 34.648  232.563 1.00 39.35  ? 714 HOH B O     1 
HETATM 16288 O O     . HOH CA 6 .   ? -14.999 31.064  231.780 1.00 41.93  ? 715 HOH B O     1 
HETATM 16289 O O     . HOH CA 6 .   ? -11.580 27.104  237.485 1.00 48.12  ? 716 HOH B O     1 
HETATM 16290 O O     . HOH CA 6 .   ? -14.628 28.071  227.676 1.00 32.58  ? 717 HOH B O     1 
HETATM 16291 O O     . HOH CA 6 .   ? -7.741  26.446  228.774 1.00 37.88  ? 718 HOH B O     1 
HETATM 16292 O O     . HOH CA 6 .   ? -6.369  24.529  227.082 1.00 39.51  ? 719 HOH B O     1 
HETATM 16293 O O     . HOH CA 6 .   ? -10.616 19.309  226.830 1.00 33.90  ? 720 HOH B O     1 
HETATM 16294 O O     . HOH CA 6 .   ? -6.241  14.187  230.331 1.00 38.37  ? 721 HOH B O     1 
HETATM 16295 O O     . HOH CA 6 .   ? -7.907  12.994  232.203 1.00 44.72  ? 722 HOH B O     1 
HETATM 16296 O O     . HOH CA 6 .   ? -12.653 18.456  209.490 1.00 50.52  ? 723 HOH B O     1 
HETATM 16297 O O     . HOH CA 6 .   ? -15.851 14.111  213.809 1.00 45.29  ? 724 HOH B O     1 
HETATM 16298 O O     . HOH CA 6 .   ? -12.603 18.310  228.498 1.00 36.34  ? 725 HOH B O     1 
HETATM 16299 O O     . HOH CA 6 .   ? -11.688 21.049  231.057 1.00 41.62  ? 726 HOH B O     1 
HETATM 16300 O O     . HOH CA 6 .   ? -20.485 12.504  229.485 1.00 48.07  ? 727 HOH B O     1 
HETATM 16301 O O     . HOH CA 6 .   ? -12.078 8.482   223.251 1.00 54.12  ? 728 HOH B O     1 
HETATM 16302 O O     . HOH CA 6 .   ? -16.868 8.606   227.289 1.00 54.30  ? 729 HOH B O     1 
HETATM 16303 O O     . HOH CA 6 .   ? -12.676 3.857   235.737 1.00 58.64  ? 730 HOH B O     1 
HETATM 16304 O O     . HOH CA 6 .   ? -6.574  21.742  206.445 1.00 55.36  ? 731 HOH B O     1 
HETATM 16305 O O     . HOH CA 6 .   ? -8.975  24.873  205.492 1.00 59.95  ? 732 HOH B O     1 
HETATM 16306 O O     . HOH CA 6 .   ? -6.414  24.297  207.064 1.00 56.60  ? 733 HOH B O     1 
HETATM 16307 O O     . HOH CA 6 .   ? 6.676   11.456  223.895 1.00 59.16  ? 734 HOH B O     1 
HETATM 16308 O O     . HOH CA 6 .   ? 8.735   28.800  223.810 1.00 30.61  ? 735 HOH B O     1 
HETATM 16309 O O     . HOH CA 6 .   ? 7.288   31.203  220.383 1.00 46.10  ? 736 HOH B O     1 
HETATM 16310 O O     . HOH CA 6 .   ? -5.422  32.896  232.239 1.00 42.58  ? 737 HOH B O     1 
HETATM 16311 O O     . HOH CA 6 .   ? 8.982   27.087  230.180 1.00 40.11  ? 738 HOH B O     1 
HETATM 16312 O O     . HOH CA 6 .   ? 6.509   21.289  231.122 1.00 43.27  ? 739 HOH B O     1 
HETATM 16313 O O     . HOH CA 6 .   ? 9.574   27.138  234.239 1.00 50.29  ? 740 HOH B O     1 
HETATM 16314 O O     . HOH CA 6 .   ? -0.852  -2.220  229.918 1.00 58.74  ? 741 HOH B O     1 
HETATM 16315 O O     . HOH CA 6 .   ? -6.810  -1.229  221.600 1.00 52.04  ? 742 HOH B O     1 
HETATM 16316 O O     . HOH CA 6 .   ? -16.729 32.151  241.866 1.00 62.26  ? 743 HOH B O     1 
HETATM 16317 O O     . HOH CA 6 .   ? -22.102 47.355  223.316 1.00 34.54  ? 744 HOH B O     1 
HETATM 16318 O O     . HOH CA 6 .   ? -21.728 49.934  220.556 1.00 45.02  ? 745 HOH B O     1 
HETATM 16319 O O     . HOH CA 6 .   ? -25.274 41.802  215.863 1.00 50.56  ? 746 HOH B O     1 
HETATM 16320 O O     . HOH CA 6 .   ? 0.608   34.466  215.189 1.00 47.44  ? 747 HOH B O     1 
HETATM 16321 O O     . HOH CA 6 .   ? -16.224 16.071  225.889 1.00 43.96  ? 748 HOH B O     1 
HETATM 16322 O O     . HOH CA 6 .   ? 8.519   17.925  227.478 1.00 48.92  ? 749 HOH B O     1 
HETATM 16323 O O     . HOH CA 6 .   ? -1.972  14.623  228.809 1.00 40.93  ? 750 HOH B O     1 
HETATM 16324 O O     . HOH CA 6 .   ? 1.571   11.491  231.568 1.00 46.27  ? 751 HOH B O     1 
HETATM 16325 O O     . HOH CA 6 .   ? -4.691  -2.650  220.693 1.00 56.54  ? 752 HOH B O     1 
HETATM 16326 O O     . HOH CA 6 .   ? -6.228  1.423   221.648 1.00 56.35  ? 753 HOH B O     1 
HETATM 16327 O O     . HOH CA 6 .   ? -11.650 -7.030  236.492 1.00 67.43  ? 754 HOH B O     1 
HETATM 16328 O O     . HOH CA 6 .   ? -14.544 10.736  232.288 1.00 53.55  ? 755 HOH B O     1 
HETATM 16329 O O     . HOH CA 6 .   ? -15.982 25.742  229.098 1.00 40.05  ? 756 HOH B O     1 
HETATM 16330 O O     . HOH CA 6 .   ? -12.408 36.701  212.247 1.00 41.91  ? 757 HOH B O     1 
HETATM 16331 O O     . HOH CA 6 .   ? -13.088 39.558  213.957 1.00 42.88  ? 758 HOH B O     1 
HETATM 16332 O O     . HOH CA 6 .   ? -2.680  41.559  213.802 1.00 39.41  ? 759 HOH B O     1 
HETATM 16333 O O     . HOH CA 6 .   ? -3.838  8.361   217.472 1.00 53.64  ? 760 HOH B O     1 
HETATM 16334 O O     . HOH CA 6 .   ? -9.944  20.822  234.150 1.00 42.62  ? 761 HOH B O     1 
HETATM 16335 O O     . HOH CA 6 .   ? -14.563 27.491  230.280 1.00 40.92  ? 762 HOH B O     1 
HETATM 16336 O O     . HOH CA 6 .   ? -15.025 21.646  229.480 1.00 37.91  ? 763 HOH B O     1 
HETATM 16337 O O     . HOH CA 6 .   ? -15.989 20.281  227.544 1.00 43.83  ? 764 HOH B O     1 
HETATM 16338 O O     . HOH CA 6 .   ? 4.463   27.733  234.401 1.00 44.64  ? 765 HOH B O     1 
HETATM 16339 O O     . HOH CA 6 .   ? 1.155   6.950   204.530 1.00 67.93  ? 766 HOH B O     1 
HETATM 16340 O O     . HOH CA 6 .   ? -0.888  1.367   229.505 1.00 51.34  ? 767 HOH B O     1 
HETATM 16341 O O     . HOH CA 6 .   ? 0.903   -2.016  231.968 1.00 58.93  ? 768 HOH B O     1 
HETATM 16342 O O     . HOH CA 6 .   ? -13.838 5.179   221.117 1.00 54.45  ? 769 HOH B O     1 
HETATM 16343 O O     . HOH CA 6 .   ? -17.024 8.079   224.817 1.00 56.88  ? 770 HOH B O     1 
HETATM 16344 O O     . HOH CA 6 .   ? -6.843  35.212  236.599 1.00 47.84  ? 771 HOH B O     1 
HETATM 16345 O O     . HOH DA 6 .   ? -7.202  41.735  169.105 1.00 38.83  ? 701 HOH C O     1 
HETATM 16346 O O     . HOH DA 6 .   ? -11.304 46.086  180.986 1.00 42.26  ? 702 HOH C O     1 
HETATM 16347 O O     . HOH DA 6 .   ? -12.996 48.521  179.060 1.00 40.54  ? 703 HOH C O     1 
HETATM 16348 O O     . HOH DA 6 .   ? -12.682 55.383  177.528 1.00 39.44  ? 704 HOH C O     1 
HETATM 16349 O O     . HOH DA 6 .   ? -26.079 59.072  168.112 1.00 41.46  ? 705 HOH C O     1 
HETATM 16350 O O     . HOH DA 6 .   ? -21.297 67.430  168.631 1.00 40.59  ? 706 HOH C O     1 
HETATM 16351 O O     . HOH DA 6 .   ? -25.687 51.362  165.313 1.00 35.55  ? 707 HOH C O     1 
HETATM 16352 O O     . HOH DA 6 .   ? -2.523  52.563  178.115 1.00 40.04  ? 708 HOH C O     1 
HETATM 16353 O O     . HOH DA 6 .   ? -1.160  50.309  179.003 1.00 44.76  ? 709 HOH C O     1 
HETATM 16354 O O     . HOH DA 6 .   ? -15.138 54.617  160.884 1.00 37.77  ? 710 HOH C O     1 
HETATM 16355 O O     . HOH DA 6 .   ? -15.061 51.231  160.500 1.00 38.49  ? 711 HOH C O     1 
HETATM 16356 O O     . HOH DA 6 .   ? -14.634 58.214  164.302 1.00 28.16  ? 712 HOH C O     1 
HETATM 16357 O O     . HOH DA 6 .   ? -14.676 58.675  161.526 1.00 34.98  ? 713 HOH C O     1 
HETATM 16358 O O     . HOH DA 6 .   ? -16.155 66.123  163.574 1.00 41.95  ? 714 HOH C O     1 
HETATM 16359 O O     . HOH DA 6 .   ? -16.172 70.326  164.822 1.00 41.80  ? 715 HOH C O     1 
HETATM 16360 O O     . HOH DA 6 .   ? -14.690 68.002  164.269 1.00 38.68  ? 716 HOH C O     1 
HETATM 16361 O O     . HOH DA 6 .   ? -13.011 68.049  162.362 1.00 32.23  ? 717 HOH C O     1 
HETATM 16362 O O     . HOH DA 6 .   ? -10.717 66.971  163.818 1.00 29.30  ? 718 HOH C O     1 
HETATM 16363 O O     . HOH DA 6 .   ? -7.920  59.748  162.970 1.00 32.45  ? 719 HOH C O     1 
HETATM 16364 O O     . HOH DA 6 .   ? -6.272  61.890  164.049 1.00 40.01  ? 720 HOH C O     1 
HETATM 16365 O O     . HOH DA 6 .   ? -5.312  53.221  160.294 1.00 33.76  ? 721 HOH C O     1 
HETATM 16366 O O     . HOH DA 6 .   ? -6.940  50.114  156.449 1.00 35.01  ? 722 HOH C O     1 
HETATM 16367 O O     . HOH DA 6 .   ? -2.371  50.186  158.828 1.00 46.12  ? 723 HOH C O     1 
HETATM 16368 O O     . HOH DA 6 .   ? -22.002 48.929  159.728 1.00 45.15  ? 724 HOH C O     1 
HETATM 16369 O O     . HOH DA 6 .   ? -23.296 60.955  160.825 1.00 44.94  ? 725 HOH C O     1 
HETATM 16370 O O     . HOH DA 6 .   ? -26.908 59.564  160.797 1.00 53.04  ? 726 HOH C O     1 
HETATM 16371 O O     . HOH DA 6 .   ? -6.548  67.819  184.612 1.00 52.21  ? 727 HOH C O     1 
HETATM 16372 O O     . HOH DA 6 .   ? 5.548   63.451  180.120 1.00 46.62  ? 728 HOH C O     1 
HETATM 16373 O O     . HOH DA 6 .   ? 6.791   64.074  178.319 1.00 45.11  ? 729 HOH C O     1 
HETATM 16374 O O     . HOH DA 6 .   ? -12.924 70.224  180.647 1.00 49.61  ? 730 HOH C O     1 
HETATM 16375 O O     . HOH DA 6 .   ? -6.435  71.603  160.049 1.00 34.06  ? 731 HOH C O     1 
HETATM 16376 O O     . HOH DA 6 .   ? -8.348  72.926  157.970 1.00 37.78  ? 732 HOH C O     1 
HETATM 16377 O O     . HOH DA 6 .   ? -15.136 74.846  157.695 1.00 43.82  ? 733 HOH C O     1 
HETATM 16378 O O     . HOH DA 6 .   ? -11.701 64.683  159.460 1.00 32.44  ? 734 HOH C O     1 
HETATM 16379 O O     . HOH DA 6 .   ? 8.847   58.360  168.247 1.00 30.00  ? 735 HOH C O     1 
HETATM 16380 O O     . HOH DA 6 .   ? 4.442   58.033  157.365 1.00 40.91  ? 736 HOH C O     1 
HETATM 16381 O O     . HOH DA 6 .   ? 6.111   64.792  160.124 1.00 39.09  ? 737 HOH C O     1 
HETATM 16382 O O     . HOH DA 6 .   ? 9.037   59.580  161.939 1.00 44.40  ? 738 HOH C O     1 
HETATM 16383 O O     . HOH DA 6 .   ? -5.256  89.878  167.732 1.00 50.51  ? 739 HOH C O     1 
HETATM 16384 O O     . HOH DA 6 .   ? -13.474 81.431  153.360 1.00 52.74  ? 740 HOH C O     1 
HETATM 16385 O O     . HOH DA 6 .   ? -7.555  88.220  167.048 1.00 49.65  ? 741 HOH C O     1 
HETATM 16386 O O     . HOH DA 6 .   ? 3.101   81.034  156.074 1.00 49.09  ? 742 HOH C O     1 
HETATM 16387 O O     . HOH DA 6 .   ? 7.364   76.483  159.364 1.00 43.90  ? 743 HOH C O     1 
HETATM 16388 O O     . HOH DA 6 .   ? 0.972   74.504  158.051 1.00 36.92  ? 744 HOH C O     1 
HETATM 16389 O O     . HOH DA 6 .   ? 1.663   69.587  151.443 1.00 47.07  ? 745 HOH C O     1 
HETATM 16390 O O     . HOH DA 6 .   ? -17.505 77.792  162.463 1.00 51.49  ? 746 HOH C O     1 
HETATM 16391 O O     . HOH DA 6 .   ? -11.595 58.111  154.470 1.00 41.78  ? 747 HOH C O     1 
HETATM 16392 O O     . HOH DA 6 .   ? -2.714  46.886  179.837 1.00 50.46  ? 748 HOH C O     1 
HETATM 16393 O O     . HOH DA 6 .   ? 0.792   53.271  177.631 1.00 45.45  ? 749 HOH C O     1 
HETATM 16394 O O     . HOH DA 6 .   ? -21.716 37.468  173.436 1.00 43.75  ? 750 HOH C O     1 
HETATM 16395 O O     . HOH DA 6 .   ? -15.849 40.877  167.067 1.00 42.31  ? 751 HOH C O     1 
HETATM 16396 O O     . HOH DA 6 .   ? -6.865  44.164  177.241 1.00 44.29  ? 752 HOH C O     1 
HETATM 16397 O O     . HOH DA 6 .   ? -30.245 55.855  173.792 1.00 50.95  ? 753 HOH C O     1 
HETATM 16398 O O     . HOH DA 6 .   ? -32.318 56.682  172.110 1.00 46.33  ? 754 HOH C O     1 
HETATM 16399 O O     . HOH DA 6 .   ? -27.140 50.431  179.761 1.00 58.39  ? 755 HOH C O     1 
HETATM 16400 O O     . HOH DA 6 .   ? -30.460 67.113  163.777 1.00 53.34  ? 756 HOH C O     1 
HETATM 16401 O O     . HOH DA 6 .   ? -15.066 64.411  161.585 1.00 39.78  ? 757 HOH C O     1 
HETATM 16402 O O     . HOH DA 6 .   ? -10.024 64.777  156.984 1.00 40.56  ? 758 HOH C O     1 
HETATM 16403 O O     . HOH DA 6 .   ? -22.288 58.138  157.852 1.00 56.18  ? 759 HOH C O     1 
HETATM 16404 O O     . HOH DA 6 .   ? -18.917 56.871  157.473 1.00 47.58  ? 760 HOH C O     1 
HETATM 16405 O O     . HOH DA 6 .   ? -5.757  63.842  162.599 1.00 39.68  ? 761 HOH C O     1 
HETATM 16406 O O     . HOH DA 6 .   ? 5.670   75.920  165.200 1.00 50.85  ? 762 HOH C O     1 
HETATM 16407 O O     . HOH DA 6 .   ? -18.273 53.024  155.783 1.00 56.98  ? 763 HOH C O     1 
HETATM 16408 O O     . HOH DA 6 .   ? -4.566  44.054  176.799 1.00 41.75  ? 764 HOH C O     1 
HETATM 16409 O O     . HOH DA 6 .   ? -16.079 60.752  162.510 1.00 35.08  ? 765 HOH C O     1 
HETATM 16410 O O     . HOH DA 6 .   ? -7.253  44.432  179.914 1.00 52.16  ? 766 HOH C O     1 
HETATM 16411 O O     . HOH DA 6 .   ? -27.621 60.973  169.293 1.00 44.24  ? 767 HOH C O     1 
HETATM 16412 O O     . HOH DA 6 .   ? 1.231   82.221  184.444 1.00 61.95  ? 768 HOH C O     1 
HETATM 16413 O O     . HOH DA 6 .   ? -4.240  79.495  172.169 1.00 52.45  ? 769 HOH C O     1 
HETATM 16414 O O     . HOH DA 6 .   ? -2.235  71.908  161.602 1.00 42.10  ? 770 HOH C O     1 
HETATM 16415 O O     . HOH DA 6 .   ? -0.669  47.735  160.706 1.00 38.95  ? 771 HOH C O     1 
HETATM 16416 O O     . HOH DA 6 .   ? -14.347 62.894  151.615 1.00 45.37  ? 772 HOH C O     1 
HETATM 16417 O O     . HOH EA 6 .   ? 6.555   52.783  228.361 1.00 39.37  ? 701 HOH D O     1 
HETATM 16418 O O     . HOH EA 6 .   ? 4.655   42.027  227.403 1.00 37.37  ? 702 HOH D O     1 
HETATM 16419 O O     . HOH EA 6 .   ? 3.481   57.182  211.417 1.00 35.09  ? 703 HOH D O     1 
HETATM 16420 O O     . HOH EA 6 .   ? 6.818   57.290  212.196 1.00 35.27  ? 704 HOH D O     1 
HETATM 16421 O O     . HOH EA 6 .   ? 18.870  62.828  221.917 1.00 41.26  ? 705 HOH D O     1 
HETATM 16422 O O     . HOH EA 6 .   ? 20.946  53.043  232.862 1.00 49.40  ? 706 HOH D O     1 
HETATM 16423 O O     . HOH EA 6 .   ? 31.318  46.114  223.561 1.00 43.14  ? 707 HOH D O     1 
HETATM 16424 O O     . HOH EA 6 .   ? 14.569  48.586  214.988 1.00 38.46  ? 708 HOH D O     1 
HETATM 16425 O O     . HOH EA 6 .   ? 12.336  50.180  213.735 1.00 33.92  ? 709 HOH D O     1 
HETATM 16426 O O     . HOH EA 6 .   ? 19.189  53.046  215.355 1.00 30.84  ? 710 HOH D O     1 
HETATM 16427 O O     . HOH EA 6 .   ? 20.130  55.732  214.444 1.00 29.68  ? 711 HOH D O     1 
HETATM 16428 O O     . HOH EA 6 .   ? 20.066  56.937  216.583 1.00 34.06  ? 712 HOH D O     1 
HETATM 16429 O O     . HOH EA 6 .   ? 22.194  58.755  217.332 1.00 37.73  ? 713 HOH D O     1 
HETATM 16430 O O     . HOH EA 6 .   ? 24.413  49.834  211.283 1.00 28.88  ? 714 HOH D O     1 
HETATM 16431 O O     . HOH EA 6 .   ? 25.598  51.889  209.807 1.00 36.32  ? 715 HOH D O     1 
HETATM 16432 O O     . HOH EA 6 .   ? 27.328  58.710  210.682 1.00 39.38  ? 716 HOH D O     1 
HETATM 16433 O O     . HOH EA 6 .   ? 24.763  45.445  212.261 1.00 34.27  ? 717 HOH D O     1 
HETATM 16434 O O     . HOH EA 6 .   ? 27.883  42.794  209.199 1.00 37.00  ? 718 HOH D O     1 
HETATM 16435 O O     . HOH EA 6 .   ? 30.042  36.460  209.357 1.00 49.72  ? 719 HOH D O     1 
HETATM 16436 O O     . HOH EA 6 .   ? 3.693   44.298  208.051 1.00 38.04  ? 720 HOH D O     1 
HETATM 16437 O O     . HOH EA 6 .   ? 6.054   47.576  210.405 1.00 36.89  ? 721 HOH D O     1 
HETATM 16438 O O     . HOH EA 6 .   ? 11.661  32.945  216.152 1.00 40.12  ? 722 HOH D O     1 
HETATM 16439 O O     . HOH EA 6 .   ? 13.270  33.517  210.321 1.00 40.31  ? 723 HOH D O     1 
HETATM 16440 O O     . HOH EA 6 .   ? 12.845  34.518  205.569 1.00 45.76  ? 724 HOH D O     1 
HETATM 16441 O O     . HOH EA 6 .   ? 18.406  37.150  209.095 1.00 43.51  ? 725 HOH D O     1 
HETATM 16442 O O     . HOH EA 6 .   ? 24.925  63.911  214.055 1.00 42.53  ? 726 HOH D O     1 
HETATM 16443 O O     . HOH EA 6 .   ? 29.397  60.555  215.990 1.00 47.41  ? 727 HOH D O     1 
HETATM 16444 O O     . HOH EA 6 .   ? 40.952  56.356  204.378 1.00 50.18  ? 728 HOH D O     1 
HETATM 16445 O O     . HOH EA 6 .   ? 15.836  45.777  197.309 1.00 42.41  ? 729 HOH D O     1 
HETATM 16446 O O     . HOH EA 6 .   ? 21.936  44.355  199.999 1.00 46.42  ? 730 HOH D O     1 
HETATM 16447 O O     . HOH EA 6 .   ? 11.044  55.019  205.283 1.00 41.22  ? 731 HOH D O     1 
HETATM 16448 O O     . HOH EA 6 .   ? -0.182  67.202  235.560 1.00 64.44  ? 732 HOH D O     1 
HETATM 16449 O O     . HOH EA 6 .   ? 5.319   69.074  215.129 1.00 57.55  ? 733 HOH D O     1 
HETATM 16450 O O     . HOH EA 6 .   ? -2.610  49.971  230.913 1.00 47.31  ? 734 HOH D O     1 
HETATM 16451 O O     . HOH EA 6 .   ? -7.015  55.634  228.994 1.00 59.97  ? 735 HOH D O     1 
HETATM 16452 O O     . HOH EA 6 .   ? 2.468   40.589  227.840 1.00 39.20  ? 736 HOH D O     1 
HETATM 16453 O O     . HOH EA 6 .   ? 5.568   39.339  226.480 1.00 45.76  ? 737 HOH D O     1 
HETATM 16454 O O     . HOH EA 6 .   ? 18.007  58.415  215.937 1.00 30.55  ? 738 HOH D O     1 
HETATM 16455 O O     . HOH EA 6 .   ? 16.361  57.736  213.802 1.00 39.53  ? 739 HOH D O     1 
HETATM 16456 O O     . HOH EA 6 .   ? 10.607  56.868  213.099 1.00 33.71  ? 740 HOH D O     1 
HETATM 16457 O O     . HOH EA 6 .   ? 17.595  53.600  208.686 1.00 36.16  ? 741 HOH D O     1 
HETATM 16458 O O     . HOH EA 6 .   ? 43.145  54.826  209.491 1.00 45.81  ? 742 HOH D O     1 
HETATM 16459 O O     . HOH EA 6 .   ? 41.896  48.599  220.405 1.00 34.37  ? 743 HOH D O     1 
HETATM 16460 O O     . HOH EA 6 .   ? 40.183  50.880  219.627 1.00 37.02  ? 744 HOH D O     1 
HETATM 16461 O O     . HOH EA 6 .   ? 43.218  47.055  207.081 1.00 52.23  ? 745 HOH D O     1 
HETATM 16462 O O     . HOH EA 6 .   ? 51.113  47.024  217.055 1.00 47.96  ? 746 HOH D O     1 
HETATM 16463 O O     . HOH EA 6 .   ? 53.140  60.121  208.323 1.00 51.24  ? 747 HOH D O     1 
HETATM 16464 O O     . HOH EA 6 .   ? 38.625  73.009  227.283 1.00 61.84  ? 748 HOH D O     1 
HETATM 16465 O O     . HOH EA 6 .   ? 37.721  45.657  210.808 1.00 41.95  ? 749 HOH D O     1 
HETATM 16466 O O     . HOH EA 6 .   ? 9.251   55.513  198.435 1.00 55.38  ? 750 HOH D O     1 
HETATM 16467 O O     . HOH EA 6 .   ? 3.053   49.369  206.344 1.00 39.25  ? 751 HOH D O     1 
HETATM 16468 O O     . HOH EA 6 .   ? -2.788  43.828  214.940 1.00 40.78  ? 752 HOH D O     1 
HETATM 16469 O O     . HOH EA 6 .   ? 11.653  38.821  206.250 1.00 43.59  ? 753 HOH D O     1 
HETATM 16470 O O     . HOH EA 6 .   ? -3.212  44.081  219.309 1.00 37.64  ? 754 HOH D O     1 
HETATM 16471 O O     . HOH EA 6 .   ? -0.099  51.861  229.348 1.00 42.17  ? 755 HOH D O     1 
HETATM 16472 O O     . HOH EA 6 .   ? 12.410  57.043  227.605 1.00 43.89  ? 756 HOH D O     1 
HETATM 16473 O O     . HOH EA 6 .   ? 56.460  49.131  220.913 1.00 45.03  ? 757 HOH D O     1 
HETATM 16474 O O     . HOH EA 6 .   ? 28.849  61.680  210.090 1.00 43.30  ? 758 HOH D O     1 
HETATM 16475 O O     . HOH EA 6 .   ? 44.842  53.592  211.003 1.00 39.61  ? 759 HOH D O     1 
HETATM 16476 O O     . HOH EA 6 .   ? 33.984  58.259  206.837 1.00 43.09  ? 760 HOH D O     1 
# 
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   GLU 2   2   ?   ?   ?   A . n 
A 1 3   ASN 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   PRO 6   6   ?   ?   ?   A . n 
A 1 7   ILE 7   7   ?   ?   ?   A . n 
A 1 8   PHE 8   8   ?   ?   ?   A . n 
A 1 9   PHE 9   9   ?   ?   ?   A . n 
A 1 10  SER 10  10  ?   ?   ?   A . n 
A 1 11  LEU 11  11  ?   ?   ?   A . n 
A 1 12  SER 12  12  ?   ?   ?   A . n 
A 1 13  ILE 13  13  ?   ?   ?   A . n 
A 1 14  PHE 14  14  ?   ?   ?   A . n 
A 1 15  LEU 15  15  ?   ?   ?   A . n 
A 1 16  SER 16  16  ?   ?   ?   A . n 
A 1 17  LEU 17  17  ?   ?   ?   A . n 
A 1 18  LEU 18  18  ?   ?   ?   A . n 
A 1 19  ASN 19  19  ?   ?   ?   A . n 
A 1 20  CYS 20  20  ?   ?   ?   A . n 
A 1 21  ALA 21  21  ?   ?   ?   A . n 
A 1 22  GLU 22  22  ?   ?   ?   A . n 
A 1 23  ALA 23  23  ?   ?   ?   A . n 
A 1 24  GLY 24  24  ?   ?   ?   A . n 
A 1 25  ASN 25  25  ?   ?   ?   A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  CYS 30  30  30  CYS CYS A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  ASN 34  34  34  ASN ASN A . n 
A 1 35  GLY 35  35  35  GLY GLY A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  ASN 38  38  38  ASN ASN A . n 
A 1 39  HIS 39  39  39  HIS HIS A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  PHE 42  42  42  PHE PHE A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  ASP 49  49  49  ASP ASP A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  ARG 52  52  52  ARG ARG A . n 
A 1 53  PHE 53  53  53  PHE PHE A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  HIS 55  55  55  HIS HIS A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  GLN 59  59  59  GLN GLN A . n 
A 1 60  ASN 60  60  60  ASN ASN A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  PHE 63  63  63  PHE PHE A . n 
A 1 64  GLN 64  64  64  GLN GLN A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  PRO 77  77  77  PRO PRO A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  CYS 89  89  89  CYS CYS A . n 
A 1 90  ILE 90  90  90  ILE ILE A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  LYS 92  92  92  LYS LYS 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  TRP 95  95  95  TRP TRP A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 TYR 106 106 106 TYR TYR A . n 
A 1 107 GLU 107 107 107 GLU GLU A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 SER 110 110 110 SER SER A . n 
A 1 111 TYR 111 111 111 TYR TYR A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 ASP 114 114 114 ASP ASP A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 PRO 116 116 116 PRO PRO A . n 
A 1 117 PHE 117 117 117 PHE PHE A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ILE 120 120 120 ILE ILE A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 MET 123 123 123 MET MET A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 ARG 127 127 127 ARG ARG A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 VAL 139 139 139 VAL VAL A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 SER 141 141 141 SER SER A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 SER 143 143 143 SER SER A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 TYR 149 149 149 TYR TYR A . n 
A 1 150 TYR 150 150 150 TYR TYR A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 TRP 165 165 165 TRP TRP A . n 
A 1 166 CYS 166 166 166 CYS CYS A . n 
A 1 167 PRO 167 167 167 PRO PRO A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 THR 171 171 171 THR THR A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 HIS 174 174 174 HIS HIS A . n 
A 1 175 ILE 175 175 175 ILE ILE A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 PHE 180 180 180 PHE PHE A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 MET 182 182 182 MET MET A . n 
A 1 183 MET 183 183 183 MET MET A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 LYS 186 186 186 LYS LYS A . n 
A 1 187 TYR 187 187 187 TYR TYR A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 ALA 202 202 202 ALA ALA A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 GLN 210 210 210 GLN GLN A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 MET 212 212 212 MET MET A . n 
A 1 213 GLY 213 213 213 GLY GLY A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 GLY 223 223 223 GLY GLY A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 VAL 227 227 227 VAL VAL A . n 
A 1 228 TRP 228 228 228 TRP TRP A . n 
A 1 229 GLY 229 229 229 GLY GLY A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 ILE 231 231 231 ILE ILE A . n 
A 1 232 TYR 232 232 232 TYR TYR A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 TRP 234 234 234 TRP TRP A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 ILE 236 236 236 ILE ILE A . n 
A 1 237 LYS 237 237 237 LYS LYS A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 PRO 240 240 240 PRO PRO A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 VAL 245 245 245 VAL VAL A . n 
A 1 246 THR 246 246 246 THR THR A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 THR 251 251 251 THR THR A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 VAL 254 254 254 VAL VAL A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 ASP 257 257 257 ASP ASP A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 ALA 259 259 259 ALA ALA A . n 
A 1 260 THR 260 260 260 THR THR A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 LYS 265 265 265 LYS LYS A . n 
A 1 266 TRP 266 266 266 TRP TRP A . n 
A 1 267 GLN 267 267 267 GLN GLN A . n 
A 1 268 PHE 268 268 268 PHE PHE A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 GLU 272 272 272 GLU GLU A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 GLU 275 275 275 GLU GLU A . n 
A 1 276 ASP 276 276 276 ASP ASP A . n 
A 1 277 PHE 277 277 277 PHE PHE A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 LEU 279 279 279 LEU LEU A . n 
A 1 280 SER 280 280 280 SER SER A . n 
A 1 281 VAL 281 281 281 VAL VAL A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 GLY 284 284 284 GLY GLY A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 GLU 287 287 287 GLU GLU A . n 
A 1 288 LYS 288 288 288 LYS LYS A . n 
A 1 289 GLN 289 289 289 GLN GLN A . n 
A 1 290 VAL 290 290 290 VAL VAL A . n 
A 1 291 TRP 291 291 291 TRP TRP A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 THR 293 293 293 THR THR A . n 
A 1 294 MET 294 294 294 MET MET A . n 
A 1 295 LEU 295 295 295 LEU LEU A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 HIS 298 298 298 HIS HIS A . n 
A 1 299 PHE 299 299 299 PHE PHE A . n 
A 1 300 GLY 300 300 300 GLY GLY A . n 
A 1 301 LEU 301 301 301 LEU LEU A . n 
A 1 302 LYS 302 302 302 LYS LYS A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 VAL 304 304 304 VAL VAL A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 LYS 306 306 306 LYS LYS A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 THR 308 308 308 THR THR A . n 
A 1 309 PHE 309 309 309 PHE PHE A . n 
A 1 310 ASP 310 310 310 ASP ASP A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 PHE 313 313 313 PHE PHE A . n 
A 1 314 PRO 314 314 314 PRO PRO A . n 
A 1 315 GLU 315 315 315 GLU GLU A . n 
A 1 316 LEU 316 316 316 LEU LEU A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 VAL 319 319 319 VAL VAL A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 ASP 322 322 322 ASP ASP A . n 
A 1 323 TYR 323 323 323 TYR TYR A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 GLU 325 325 325 GLU GLU A . n 
A 1 326 MET 326 326 326 MET MET A . n 
A 1 327 SER 327 327 327 SER SER A . n 
A 1 328 TRP 328 328 328 TRP TRP A . n 
A 1 329 GLY 329 329 329 GLY GLY A . n 
A 1 330 GLU 330 330 330 GLU GLU A . n 
A 1 331 SER 331 331 331 SER SER A . n 
A 1 332 PHE 332 332 332 PHE PHE A . n 
A 1 333 ALA 333 333 333 ALA ALA A . n 
A 1 334 TYR 334 334 334 TYR TYR A . n 
A 1 335 LEU 335 335 335 LEU LEU A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 GLY 337 337 337 GLY GLY A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 THR 340 340 340 THR THR A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 GLN 343 343 343 GLN GLN A . n 
A 1 344 LEU 344 344 344 LEU LEU A . n 
A 1 345 ASN 345 345 345 ASN ASN A . n 
A 1 346 ASN 346 346 346 ASN ASN A . n 
A 1 347 ARG 347 347 347 ARG ARG A . n 
A 1 348 PHE 348 348 348 PHE PHE A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 LYS 350 350 350 LYS LYS A . n 
A 1 351 PHE 351 351 351 PHE PHE A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 ARG 354 354 354 ARG ARG A . n 
A 1 355 ALA 355 355 355 ALA ALA A . n 
A 1 356 PHE 356 356 356 PHE PHE A . n 
A 1 357 LYS 357 357 357 LYS LYS A . n 
A 1 358 THR 358 358 358 THR THR A . n 
A 1 359 LYS 359 359 359 LYS LYS A . n 
A 1 360 VAL 360 360 360 VAL VAL A . n 
A 1 361 ASP 361 361 361 ASP ASP A . n 
A 1 362 LEU 362 362 362 LEU LEU A . n 
A 1 363 THR 363 363 363 THR THR A . n 
A 1 364 LYS 364 364 364 LYS LYS A . n 
A 1 365 GLU 365 365 365 GLU GLU A . n 
A 1 366 PRO 366 366 366 PRO PRO A . n 
A 1 367 LEU 367 367 367 LEU LEU A . n 
A 1 368 PRO 368 368 368 PRO PRO A . n 
A 1 369 SER 369 369 369 SER SER A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 ALA 371 371 371 ALA ALA A . n 
A 1 372 PHE 372 372 372 PHE PHE A . n 
A 1 373 TYR 373 373 373 TYR TYR A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 GLU 377 377 377 GLU GLU A . n 
A 1 378 ARG 378 378 378 ARG ARG A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 SER 380 380 380 SER SER A . n 
A 1 381 LYS 381 381 381 LYS LYS A . n 
A 1 382 GLU 382 382 382 GLU GLU A . n 
A 1 383 PRO 383 383 383 PRO PRO A . n 
A 1 384 ASN 384 384 384 ASN ASN A . n 
A 1 385 GLY 385 385 385 GLY GLY A . n 
A 1 386 PHE 386 386 386 PHE PHE A . n 
A 1 387 ILE 387 387 387 ILE ILE A . n 
A 1 388 ALA 388 388 388 ALA ALA A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 ASN 390 390 390 ASN ASN A . n 
A 1 391 GLY 391 391 391 GLY GLY A . n 
A 1 392 PHE 392 392 392 PHE PHE A . n 
A 1 393 GLY 393 393 393 GLY GLY A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 GLN 395 395 395 GLN GLN A . n 
A 1 396 MET 396 396 396 MET MET A . n 
A 1 397 SER 397 397 397 SER SER A . n 
A 1 398 LYS 398 398 398 LYS LYS A . n 
A 1 399 ILE 399 399 399 ILE ILE A . n 
A 1 400 SER 400 400 400 SER SER A . n 
A 1 401 SER 401 401 401 SER SER A . n 
A 1 402 ASP 402 402 402 ASP ASP A . n 
A 1 403 PHE 403 403 403 PHE PHE A . n 
A 1 404 THR 404 404 404 THR THR A . n 
A 1 405 PRO 405 405 405 PRO PRO A . n 
A 1 406 PHE 406 406 406 PHE PHE A . n 
A 1 407 PRO 407 407 407 PRO PRO A . n 
A 1 408 HIS 408 408 408 HIS HIS A . n 
A 1 409 ARG 409 409 409 ARG ARG A . n 
A 1 410 SER 410 410 410 SER SER A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 THR 412 412 412 THR THR A . n 
A 1 413 ARG 413 413 413 ARG ARG A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 MET 415 415 415 MET MET A . n 
A 1 416 VAL 416 416 416 VAL VAL 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 ILE 419 419 419 ILE ILE A . n 
A 1 420 VAL 420 420 420 VAL VAL A . n 
A 1 421 ALA 421 421 421 ALA ALA A . n 
A 1 422 TRP 422 422 422 TRP TRP A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 GLN 424 424 424 GLN GLN A . n 
A 1 425 SER 425 425 425 SER SER A . n 
A 1 426 GLU 426 426 426 GLU GLU A . n 
A 1 427 GLN 427 427 427 GLN GLN A . n 
A 1 428 LYS 428 428 428 LYS LYS A . n 
A 1 429 LYS 429 429 429 LYS LYS A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 THR 431 431 431 THR THR A . n 
A 1 432 GLU 432 432 432 GLU GLU A . n 
A 1 433 PHE 433 433 433 PHE PHE A . n 
A 1 434 LEU 434 434 434 LEU LEU A . n 
A 1 435 ASP 435 435 435 ASP ASP A . n 
A 1 436 TRP 436 436 436 TRP TRP A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 GLU 438 438 438 GLU GLU A . n 
A 1 439 LYS 439 439 439 LYS LYS A . n 
A 1 440 VAL 440 440 440 VAL VAL A . n 
A 1 441 TYR 441 441 441 TYR TYR A . n 
A 1 442 GLU 442 442 442 GLU GLU A . n 
A 1 443 PHE 443 443 443 PHE PHE A . n 
A 1 444 MET 444 444 444 MET MET A . n 
A 1 445 LYS 445 445 445 LYS LYS A . n 
A 1 446 PRO 446 446 446 PRO PRO A . n 
A 1 447 PHE 447 447 447 PHE PHE A . n 
A 1 448 VAL 448 448 448 VAL VAL A . n 
A 1 449 SER 449 449 449 SER SER A . n 
A 1 450 LYS 450 450 450 LYS LYS A . n 
A 1 451 ASN 451 451 451 ASN ASN A . n 
A 1 452 PRO 452 452 452 PRO PRO A . n 
A 1 453 ARG 453 453 453 ARG ARG A . n 
A 1 454 LEU 454 454 454 LEU LEU A . n 
A 1 455 GLY 455 455 455 GLY GLY A . n 
A 1 456 TYR 456 456 456 TYR TYR A . n 
A 1 457 VAL 457 457 457 VAL VAL A . n 
A 1 458 ASN 458 458 458 ASN ASN A . n 
A 1 459 HIS 459 459 459 HIS HIS 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 LEU 462 462 462 LEU LEU A . n 
A 1 463 ASP 463 463 463 ASP ASP A . n 
A 1 464 LEU 464 464 464 LEU LEU A . n 
A 1 465 GLY 465 465 465 GLY GLY A . n 
A 1 466 GLY 466 466 466 GLY GLY A . n 
A 1 467 ILE 467 467 467 ILE ILE A . n 
A 1 468 ASP 468 468 468 ASP ASP A . n 
A 1 469 TRP 469 469 469 TRP TRP A . n 
A 1 470 GLY 470 470 470 GLY GLY A . n 
A 1 471 ASN 471 471 471 ASN ASN A . n 
A 1 472 LYS 472 472 472 LYS LYS A . n 
A 1 473 THR 473 473 473 THR THR A . n 
A 1 474 VAL 474 474 474 VAL VAL A . n 
A 1 475 VAL 475 475 475 VAL VAL A . n 
A 1 476 ASN 476 476 476 ASN ASN A . n 
A 1 477 ASN 477 477 477 ASN ASN A . n 
A 1 478 ALA 478 478 478 ALA ALA A . n 
A 1 479 ILE 479 479 479 ILE ILE A . n 
A 1 480 GLU 480 480 480 GLU GLU A . n 
A 1 481 ILE 481 481 481 ILE ILE A . n 
A 1 482 SER 482 482 482 SER SER A . n 
A 1 483 ARG 483 483 483 ARG ARG A . n 
A 1 484 SER 484 484 484 SER SER A . n 
A 1 485 TRP 485 485 485 TRP TRP A . n 
A 1 486 GLY 486 486 486 GLY GLY A . n 
A 1 487 GLU 487 487 487 GLU GLU A . n 
A 1 488 SER 488 488 488 SER SER A . n 
A 1 489 TYR 489 489 489 TYR TYR A . n 
A 1 490 PHE 490 490 490 PHE PHE A . n 
A 1 491 LEU 491 491 491 LEU LEU A . n 
A 1 492 SER 492 492 492 SER SER A . n 
A 1 493 ASN 493 493 493 ASN ASN A . n 
A 1 494 TYR 494 494 494 TYR TYR A . n 
A 1 495 GLU 495 495 495 GLU GLU A . n 
A 1 496 ARG 496 496 496 ARG ARG A . n 
A 1 497 LEU 497 497 497 LEU LEU A . n 
A 1 498 ILE 498 498 498 ILE ILE A . n 
A 1 499 ARG 499 499 499 ARG ARG A . n 
A 1 500 ALA 500 500 500 ALA ALA A . n 
A 1 501 LYS 501 501 501 LYS LYS A . n 
A 1 502 THR 502 502 502 THR THR A . n 
A 1 503 LEU 503 503 503 LEU LEU A . n 
A 1 504 ILE 504 504 504 ILE ILE A . n 
A 1 505 ASP 505 505 505 ASP ASP A . n 
A 1 506 PRO 506 506 506 PRO PRO A . n 
A 1 507 ASN 507 507 507 ASN ASN A . n 
A 1 508 ASN 508 508 508 ASN ASN A . n 
A 1 509 VAL 509 509 509 VAL VAL A . n 
A 1 510 PHE 510 510 510 PHE PHE A . n 
A 1 511 ASN 511 511 511 ASN ASN A . n 
A 1 512 HIS 512 512 512 HIS HIS A . n 
A 1 513 PRO 513 513 513 PRO PRO A . n 
A 1 514 GLN 514 514 514 GLN GLN A . n 
A 1 515 SER 515 515 515 SER SER A . n 
A 1 516 ILE 516 516 516 ILE ILE A . n 
A 1 517 PRO 517 517 517 PRO PRO A . n 
A 1 518 PRO 518 518 518 PRO PRO A . n 
A 1 519 MET 519 519 519 MET MET A . n 
A 1 520 ALA 520 520 520 ALA ALA A . n 
A 1 521 ASN 521 521 521 ASN ASN A . n 
A 1 522 PHE 522 522 522 PHE PHE A . n 
A 1 523 ASP 523 523 523 ASP ASP A . n 
A 1 524 TYR 524 524 ?   ?   ?   A . n 
A 1 525 LEU 525 525 ?   ?   ?   A . n 
A 1 526 GLU 526 526 ?   ?   ?   A . n 
A 1 527 LYS 527 527 ?   ?   ?   A . n 
A 1 528 THR 528 528 ?   ?   ?   A . n 
A 1 529 LEU 529 529 ?   ?   ?   A . n 
A 1 530 GLY 530 530 ?   ?   ?   A . n 
A 1 531 SER 531 531 ?   ?   ?   A . n 
A 1 532 ASP 532 532 ?   ?   ?   A . n 
A 1 533 GLY 533 533 ?   ?   ?   A . n 
A 1 534 GLY 534 534 ?   ?   ?   A . n 
A 1 535 GLU 535 535 ?   ?   ?   A . n 
A 1 536 VAL 536 536 ?   ?   ?   A . n 
A 1 537 VAL 537 537 ?   ?   ?   A . n 
A 1 538 ILE 538 538 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLU 2   2   ?   ?   ?   B . n 
B 1 3   ASN 3   3   ?   ?   ?   B . n 
B 1 4   LYS 4   4   ?   ?   ?   B . n 
B 1 5   THR 5   5   ?   ?   ?   B . n 
B 1 6   PRO 6   6   ?   ?   ?   B . n 
B 1 7   ILE 7   7   ?   ?   ?   B . n 
B 1 8   PHE 8   8   ?   ?   ?   B . n 
B 1 9   PHE 9   9   ?   ?   ?   B . n 
B 1 10  SER 10  10  ?   ?   ?   B . n 
B 1 11  LEU 11  11  ?   ?   ?   B . n 
B 1 12  SER 12  12  ?   ?   ?   B . n 
B 1 13  ILE 13  13  ?   ?   ?   B . n 
B 1 14  PHE 14  14  ?   ?   ?   B . n 
B 1 15  LEU 15  15  ?   ?   ?   B . n 
B 1 16  SER 16  16  ?   ?   ?   B . n 
B 1 17  LEU 17  17  ?   ?   ?   B . n 
B 1 18  LEU 18  18  ?   ?   ?   B . n 
B 1 19  ASN 19  19  ?   ?   ?   B . n 
B 1 20  CYS 20  20  ?   ?   ?   B . n 
B 1 21  ALA 21  21  ?   ?   ?   B . n 
B 1 22  GLU 22  22  ?   ?   ?   B . n 
B 1 23  ALA 23  23  ?   ?   ?   B . n 
B 1 24  GLY 24  24  ?   ?   ?   B . n 
B 1 25  ASN 25  25  25  ASN ASN B . n 
B 1 26  ASP 26  26  26  ASP ASP B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  LEU 28  28  28  LEU LEU B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  CYS 30  30  30  CYS CYS B . n 
B 1 31  LEU 31  31  31  LEU LEU B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  ASN 34  34  34  ASN ASN B . n 
B 1 35  GLY 35  35  35  GLY GLY B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ARG 37  37  37  ARG ARG B . n 
B 1 38  ASN 38  38  38  ASN ASN B . n 
B 1 39  HIS 39  39  39  HIS HIS B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  PHE 42  42  42  PHE PHE B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  ASP 45  45  45  ASP ASP B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  ASP 49  49  49  ASP ASP B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  ARG 52  52  52  ARG ARG B . n 
B 1 53  PHE 53  53  53  PHE PHE B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  HIS 55  55  55  HIS HIS B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  SER 57  57  57  SER SER B . n 
B 1 58  ILE 58  58  58  ILE ILE B . n 
B 1 59  GLN 59  59  59  GLN GLN B . n 
B 1 60  ASN 60  60  60  ASN ASN B . n 
B 1 61  PRO 61  61  61  PRO PRO B . n 
B 1 62  LEU 62  62  62  LEU LEU B . n 
B 1 63  PHE 63  63  63  PHE PHE B . n 
B 1 64  GLN 64  64  64  GLN GLN B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  SER 66  66  66  SER SER B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  ILE 68  68  68  ILE ILE B . n 
B 1 69  SER 69  69  69  SER SER B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  PRO 71  71  71  PRO PRO B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  ILE 74  74  74  ILE ILE B . n 
B 1 75  ILE 75  75  75  ILE ILE B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  PRO 77  77  77  PRO PRO B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  SER 79  79  79  SER SER B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  GLU 81  81  81  GLU GLU B . n 
B 1 82  GLU 82  82  82  GLU GLU B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  ASN 85  85  85  ASN ASN B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  ILE 87  87  87  ILE ILE B . n 
B 1 88  ARG 88  88  88  ARG ARG B . n 
B 1 89  CYS 89  89  89  CYS CYS B . n 
B 1 90  ILE 90  90  90  ILE ILE B . n 
B 1 91  ARG 91  91  91  ARG ARG B . n 
B 1 92  LYS 92  92  92  LYS LYS 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  TRP 95  95  95  TRP TRP B . n 
B 1 96  THR 96  96  96  THR THR B . n 
B 1 97  ILE 97  97  97  ILE ILE B . n 
B 1 98  ARG 98  98  98  ARG ARG B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 ARG 100 100 100 ARG ARG B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 HIS 104 104 104 HIS HIS B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 TYR 106 106 106 TYR TYR B . n 
B 1 107 GLU 107 107 107 GLU GLU B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 SER 110 110 110 SER SER B . n 
B 1 111 TYR 111 111 111 TYR TYR B . n 
B 1 112 THR 112 112 112 THR THR B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 ASP 114 114 114 ASP ASP B . n 
B 1 115 THR 115 115 115 THR THR B . n 
B 1 116 PRO 116 116 116 PRO PRO B . n 
B 1 117 PHE 117 117 117 PHE PHE B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 ILE 120 120 120 ILE ILE B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 MET 123 123 123 MET MET B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 ASN 126 126 126 ASN ASN B . n 
B 1 127 ARG 127 127 127 ARG ARG B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 SER 129 129 129 SER SER B . n 
B 1 130 ILE 130 130 130 ILE ILE B . n 
B 1 131 ASP 131 131 131 ASP ASP B . n 
B 1 132 LEU 132 132 132 LEU LEU B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 THR 136 136 136 THR THR B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 TRP 138 138 138 TRP TRP B . n 
B 1 139 VAL 139 139 139 VAL VAL B . n 
B 1 140 GLU 140 140 140 GLU GLU B . n 
B 1 141 SER 141 141 141 SER SER B . n 
B 1 142 GLY 142 142 142 GLY GLY B . n 
B 1 143 SER 143 143 143 SER SER B . n 
B 1 144 THR 144 144 144 THR THR B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 TYR 149 149 149 TYR TYR B . n 
B 1 150 TYR 150 150 150 TYR TYR B . n 
B 1 151 ALA 151 151 151 ALA ALA B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 THR 153 153 153 THR THR B . n 
B 1 154 GLU 154 154 154 GLU GLU B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 GLY 160 160 160 GLY GLY B . n 
B 1 161 PHE 161 161 161 PHE PHE B . n 
B 1 162 THR 162 162 162 THR THR B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 ALA 164 164 164 ALA ALA B . n 
B 1 165 TRP 165 165 165 TRP TRP B . n 
B 1 166 CYS 166 166 166 CYS CYS B . n 
B 1 167 PRO 167 167 167 PRO PRO B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 VAL 169 169 169 VAL VAL B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 THR 171 171 171 THR THR B . n 
B 1 172 GLY 172 172 172 GLY GLY B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 HIS 174 174 174 HIS HIS B . n 
B 1 175 ILE 175 175 175 ILE ILE B . n 
B 1 176 SER 176 176 176 SER SER B . n 
B 1 177 GLY 177 177 177 GLY GLY B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 PHE 180 180 180 PHE PHE B . n 
B 1 181 GLY 181 181 181 GLY GLY B . n 
B 1 182 MET 182 182 182 MET MET B . n 
B 1 183 MET 183 183 183 MET MET B . n 
B 1 184 SER 184 184 184 SER SER B . n 
B 1 185 ARG 185 185 185 ARG ARG B . n 
B 1 186 LYS 186 186 186 LYS LYS B . n 
B 1 187 TYR 187 187 187 TYR TYR B . n 
B 1 188 GLY 188 188 188 GLY GLY B . n 
B 1 189 LEU 189 189 189 LEU LEU B . n 
B 1 190 ALA 190 190 190 ALA ALA B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 ASN 193 193 193 ASN ASN B . n 
B 1 194 VAL 194 194 194 VAL VAL B . n 
B 1 195 VAL 195 195 195 VAL VAL B . n 
B 1 196 ASP 196 196 196 ASP ASP B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 ILE 198 198 198 ILE ILE B . n 
B 1 199 LEU 199 199 199 LEU LEU B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 ASP 201 201 201 ASP ASP B . n 
B 1 202 ALA 202 202 202 ALA ALA B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 GLY 204 204 204 GLY GLY B . n 
B 1 205 ALA 205 205 205 ALA ALA B . n 
B 1 206 ILE 206 206 206 ILE ILE B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 ASP 208 208 208 ASP ASP B . n 
B 1 209 ARG 209 209 209 ARG ARG B . n 
B 1 210 GLN 210 210 210 GLN GLN B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 MET 212 212 212 MET MET B . n 
B 1 213 GLY 213 213 213 GLY GLY B . n 
B 1 214 GLU 214 214 214 GLU GLU B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 PHE 217 217 217 PHE PHE B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 ARG 221 221 221 ARG ARG B . n 
B 1 222 GLY 222 222 222 GLY GLY B . n 
B 1 223 GLY 223 223 223 GLY GLY B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 GLY 225 225 225 GLY GLY B . n 
B 1 226 GLY 226 226 226 GLY GLY B . n 
B 1 227 VAL 227 227 227 VAL VAL B . n 
B 1 228 TRP 228 228 228 TRP TRP B . n 
B 1 229 GLY 229 229 229 GLY GLY B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 ILE 231 231 231 ILE ILE B . n 
B 1 232 TYR 232 232 232 TYR TYR B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 TRP 234 234 234 TRP TRP B . n 
B 1 235 LYS 235 235 235 LYS LYS B . n 
B 1 236 ILE 236 236 236 ILE ILE B . n 
B 1 237 LYS 237 237 237 LYS LYS B . n 
B 1 238 LEU 238 238 238 LEU LEU B . n 
B 1 239 LEU 239 239 239 LEU LEU B . n 
B 1 240 PRO 240 240 240 PRO PRO B . n 
B 1 241 VAL 241 241 241 VAL VAL B . n 
B 1 242 PRO 242 242 242 PRO PRO B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 LYS 244 244 244 LYS LYS B . n 
B 1 245 VAL 245 245 245 VAL VAL B . n 
B 1 246 THR 246 246 246 THR THR B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 PHE 248 248 248 PHE PHE B . n 
B 1 249 ARG 249 249 249 ARG ARG B . n 
B 1 250 VAL 250 250 250 VAL VAL B . n 
B 1 251 THR 251 251 251 THR THR B . n 
B 1 252 LYS 252 252 252 LYS LYS B . n 
B 1 253 ASN 253 253 253 ASN ASN B . n 
B 1 254 VAL 254 254 254 VAL VAL B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 ILE 256 256 256 ILE ILE B . n 
B 1 257 ASP 257 257 257 ASP ASP B . n 
B 1 258 GLU 258 258 258 GLU GLU B . n 
B 1 259 ALA 259 259 259 ALA ALA B . n 
B 1 260 THR 260 260 260 THR THR B . n 
B 1 261 SER 261 261 261 SER SER B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 LEU 263 263 263 LEU LEU B . n 
B 1 264 HIS 264 264 264 HIS HIS B . n 
B 1 265 LYS 265 265 265 LYS LYS B . n 
B 1 266 TRP 266 266 266 TRP TRP B . n 
B 1 267 GLN 267 267 267 GLN GLN B . n 
B 1 268 PHE 268 268 268 PHE PHE B . n 
B 1 269 VAL 269 269 269 VAL VAL B . n 
B 1 270 ALA 270 270 270 ALA ALA B . n 
B 1 271 GLU 271 271 271 GLU GLU B . n 
B 1 272 GLU 272 272 272 GLU GLU B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 GLU 274 274 274 GLU GLU B . n 
B 1 275 GLU 275 275 275 GLU GLU B . n 
B 1 276 ASP 276 276 276 ASP ASP B . n 
B 1 277 PHE 277 277 277 PHE PHE B . n 
B 1 278 THR 278 278 278 THR THR B . n 
B 1 279 LEU 279 279 279 LEU LEU B . n 
B 1 280 SER 280 280 280 SER SER B . n 
B 1 281 VAL 281 281 281 VAL VAL B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 GLY 284 284 284 GLY GLY B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 ASP 286 286 286 ASP ASP B . n 
B 1 287 GLU 287 287 287 GLU GLU B . n 
B 1 288 LYS 288 288 288 LYS LYS B . n 
B 1 289 GLN 289 289 289 GLN GLN B . n 
B 1 290 VAL 290 290 290 VAL VAL B . n 
B 1 291 TRP 291 291 291 TRP TRP B . n 
B 1 292 LEU 292 292 292 LEU LEU B . n 
B 1 293 THR 293 293 293 THR THR B . n 
B 1 294 MET 294 294 294 MET MET B . n 
B 1 295 LEU 295 295 295 LEU LEU B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 PHE 297 297 297 PHE PHE B . n 
B 1 298 HIS 298 298 298 HIS HIS B . n 
B 1 299 PHE 299 299 299 PHE PHE B . n 
B 1 300 GLY 300 300 300 GLY GLY B . n 
B 1 301 LEU 301 301 301 LEU LEU B . n 
B 1 302 LYS 302 302 302 LYS LYS B . n 
B 1 303 THR 303 303 303 THR THR B . n 
B 1 304 VAL 304 304 304 VAL VAL B . n 
B 1 305 ALA 305 305 305 ALA ALA B . n 
B 1 306 LYS 306 306 306 LYS LYS B . n 
B 1 307 SER 307 307 307 SER SER B . n 
B 1 308 THR 308 308 308 THR THR B . n 
B 1 309 PHE 309 309 309 PHE PHE B . n 
B 1 310 ASP 310 310 310 ASP ASP B . n 
B 1 311 LEU 311 311 311 LEU LEU B . n 
B 1 312 LEU 312 312 312 LEU LEU B . n 
B 1 313 PHE 313 313 313 PHE PHE B . n 
B 1 314 PRO 314 314 314 PRO PRO B . n 
B 1 315 GLU 315 315 315 GLU GLU B . n 
B 1 316 LEU 316 316 316 LEU LEU B . n 
B 1 317 GLY 317 317 317 GLY GLY B . n 
B 1 318 LEU 318 318 318 LEU LEU B . n 
B 1 319 VAL 319 319 319 VAL VAL B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 GLU 321 321 321 GLU GLU B . n 
B 1 322 ASP 322 322 322 ASP ASP B . n 
B 1 323 TYR 323 323 323 TYR TYR B . n 
B 1 324 LEU 324 324 324 LEU LEU B . n 
B 1 325 GLU 325 325 325 GLU GLU B . n 
B 1 326 MET 326 326 326 MET MET B . n 
B 1 327 SER 327 327 327 SER SER B . n 
B 1 328 TRP 328 328 328 TRP TRP B . n 
B 1 329 GLY 329 329 329 GLY GLY B . n 
B 1 330 GLU 330 330 330 GLU GLU B . n 
B 1 331 SER 331 331 331 SER SER B . n 
B 1 332 PHE 332 332 332 PHE PHE B . n 
B 1 333 ALA 333 333 333 ALA ALA B . n 
B 1 334 TYR 334 334 334 TYR TYR B . n 
B 1 335 LEU 335 335 335 LEU LEU B . n 
B 1 336 ALA 336 336 336 ALA ALA B . n 
B 1 337 GLY 337 337 337 GLY GLY B . n 
B 1 338 LEU 338 338 338 LEU LEU B . n 
B 1 339 GLU 339 339 339 GLU GLU B . n 
B 1 340 THR 340 340 340 THR THR B . n 
B 1 341 VAL 341 341 341 VAL VAL B . n 
B 1 342 SER 342 342 342 SER SER B . n 
B 1 343 GLN 343 343 343 GLN GLN B . n 
B 1 344 LEU 344 344 344 LEU LEU B . n 
B 1 345 ASN 345 345 345 ASN ASN B . n 
B 1 346 ASN 346 346 346 ASN ASN B . n 
B 1 347 ARG 347 347 347 ARG ARG B . n 
B 1 348 PHE 348 348 348 PHE PHE B . n 
B 1 349 LEU 349 349 349 LEU LEU B . n 
B 1 350 LYS 350 350 350 LYS LYS B . n 
B 1 351 PHE 351 351 351 PHE PHE B . n 
B 1 352 ASP 352 352 352 ASP ASP B . n 
B 1 353 GLU 353 353 353 GLU GLU B . n 
B 1 354 ARG 354 354 354 ARG ARG B . n 
B 1 355 ALA 355 355 355 ALA ALA B . n 
B 1 356 PHE 356 356 356 PHE PHE B . n 
B 1 357 LYS 357 357 357 LYS LYS B . n 
B 1 358 THR 358 358 358 THR THR B . n 
B 1 359 LYS 359 359 359 LYS LYS B . n 
B 1 360 VAL 360 360 360 VAL VAL B . n 
B 1 361 ASP 361 361 361 ASP ASP B . n 
B 1 362 LEU 362 362 362 LEU LEU B . n 
B 1 363 THR 363 363 363 THR THR B . n 
B 1 364 LYS 364 364 364 LYS LYS B . n 
B 1 365 GLU 365 365 365 GLU GLU B . n 
B 1 366 PRO 366 366 366 PRO PRO B . n 
B 1 367 LEU 367 367 367 LEU LEU B . n 
B 1 368 PRO 368 368 368 PRO PRO B . n 
B 1 369 SER 369 369 369 SER SER B . n 
B 1 370 LYS 370 370 370 LYS LYS B . n 
B 1 371 ALA 371 371 371 ALA ALA B . n 
B 1 372 PHE 372 372 372 PHE PHE B . n 
B 1 373 TYR 373 373 373 TYR TYR B . n 
B 1 374 GLY 374 374 374 GLY GLY B . n 
B 1 375 LEU 375 375 375 LEU LEU B . n 
B 1 376 LEU 376 376 376 LEU LEU B . n 
B 1 377 GLU 377 377 377 GLU GLU B . n 
B 1 378 ARG 378 378 378 ARG ARG B . n 
B 1 379 LEU 379 379 379 LEU LEU B . n 
B 1 380 SER 380 380 380 SER SER B . n 
B 1 381 LYS 381 381 381 LYS LYS B . n 
B 1 382 GLU 382 382 382 GLU GLU B . n 
B 1 383 PRO 383 383 383 PRO PRO B . n 
B 1 384 ASN 384 384 384 ASN ASN B . n 
B 1 385 GLY 385 385 385 GLY GLY B . n 
B 1 386 PHE 386 386 386 PHE PHE B . n 
B 1 387 ILE 387 387 387 ILE ILE B . n 
B 1 388 ALA 388 388 388 ALA ALA B . n 
B 1 389 LEU 389 389 389 LEU LEU B . n 
B 1 390 ASN 390 390 390 ASN ASN B . n 
B 1 391 GLY 391 391 391 GLY GLY B . n 
B 1 392 PHE 392 392 392 PHE PHE B . n 
B 1 393 GLY 393 393 393 GLY GLY B . n 
B 1 394 GLY 394 394 394 GLY GLY B . n 
B 1 395 GLN 395 395 395 GLN GLN B . n 
B 1 396 MET 396 396 396 MET MET B . n 
B 1 397 SER 397 397 397 SER SER B . n 
B 1 398 LYS 398 398 398 LYS LYS B . n 
B 1 399 ILE 399 399 399 ILE ILE B . n 
B 1 400 SER 400 400 400 SER SER B . n 
B 1 401 SER 401 401 401 SER SER B . n 
B 1 402 ASP 402 402 402 ASP ASP B . n 
B 1 403 PHE 403 403 403 PHE PHE B . n 
B 1 404 THR 404 404 404 THR THR B . n 
B 1 405 PRO 405 405 405 PRO PRO B . n 
B 1 406 PHE 406 406 406 PHE PHE B . n 
B 1 407 PRO 407 407 407 PRO PRO B . n 
B 1 408 HIS 408 408 408 HIS HIS B . n 
B 1 409 ARG 409 409 409 ARG ARG B . n 
B 1 410 SER 410 410 410 SER SER B . n 
B 1 411 GLY 411 411 411 GLY GLY B . n 
B 1 412 THR 412 412 412 THR THR B . n 
B 1 413 ARG 413 413 413 ARG ARG B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 MET 415 415 415 MET MET B . n 
B 1 416 VAL 416 416 416 VAL VAL 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 ILE 419 419 419 ILE ILE B . n 
B 1 420 VAL 420 420 420 VAL VAL B . n 
B 1 421 ALA 421 421 421 ALA ALA B . n 
B 1 422 TRP 422 422 422 TRP TRP B . n 
B 1 423 ASN 423 423 423 ASN ASN B . n 
B 1 424 GLN 424 424 424 GLN GLN B . n 
B 1 425 SER 425 425 425 SER SER B . n 
B 1 426 GLU 426 426 426 GLU GLU B . n 
B 1 427 GLN 427 427 427 GLN GLN B . n 
B 1 428 LYS 428 428 428 LYS LYS B . n 
B 1 429 LYS 429 429 429 LYS LYS B . n 
B 1 430 LYS 430 430 430 LYS LYS B . n 
B 1 431 THR 431 431 431 THR THR B . n 
B 1 432 GLU 432 432 432 GLU GLU B . n 
B 1 433 PHE 433 433 433 PHE PHE B . n 
B 1 434 LEU 434 434 434 LEU LEU B . n 
B 1 435 ASP 435 435 435 ASP ASP B . n 
B 1 436 TRP 436 436 436 TRP TRP B . n 
B 1 437 LEU 437 437 437 LEU LEU B . n 
B 1 438 GLU 438 438 438 GLU GLU B . n 
B 1 439 LYS 439 439 439 LYS LYS B . n 
B 1 440 VAL 440 440 440 VAL VAL B . n 
B 1 441 TYR 441 441 441 TYR TYR B . n 
B 1 442 GLU 442 442 442 GLU GLU B . n 
B 1 443 PHE 443 443 443 PHE PHE B . n 
B 1 444 MET 444 444 444 MET MET B . n 
B 1 445 LYS 445 445 445 LYS LYS B . n 
B 1 446 PRO 446 446 446 PRO PRO B . n 
B 1 447 PHE 447 447 447 PHE PHE B . n 
B 1 448 VAL 448 448 448 VAL VAL B . n 
B 1 449 SER 449 449 449 SER SER B . n 
B 1 450 LYS 450 450 450 LYS LYS B . n 
B 1 451 ASN 451 451 451 ASN ASN B . n 
B 1 452 PRO 452 452 452 PRO PRO B . n 
B 1 453 ARG 453 453 453 ARG ARG B . n 
B 1 454 LEU 454 454 454 LEU LEU B . n 
B 1 455 GLY 455 455 455 GLY GLY B . n 
B 1 456 TYR 456 456 456 TYR TYR B . n 
B 1 457 VAL 457 457 457 VAL VAL B . n 
B 1 458 ASN 458 458 458 ASN ASN B . n 
B 1 459 HIS 459 459 459 HIS HIS 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 LEU 462 462 462 LEU LEU B . n 
B 1 463 ASP 463 463 463 ASP ASP B . n 
B 1 464 LEU 464 464 464 LEU LEU B . n 
B 1 465 GLY 465 465 465 GLY GLY B . n 
B 1 466 GLY 466 466 466 GLY GLY B . n 
B 1 467 ILE 467 467 467 ILE ILE B . n 
B 1 468 ASP 468 468 468 ASP ASP B . n 
B 1 469 TRP 469 469 469 TRP TRP B . n 
B 1 470 GLY 470 470 470 GLY GLY B . n 
B 1 471 ASN 471 471 471 ASN ASN B . n 
B 1 472 LYS 472 472 472 LYS LYS B . n 
B 1 473 THR 473 473 473 THR THR B . n 
B 1 474 VAL 474 474 474 VAL VAL B . n 
B 1 475 VAL 475 475 475 VAL VAL B . n 
B 1 476 ASN 476 476 476 ASN ASN B . n 
B 1 477 ASN 477 477 477 ASN ASN B . n 
B 1 478 ALA 478 478 478 ALA ALA B . n 
B 1 479 ILE 479 479 479 ILE ILE B . n 
B 1 480 GLU 480 480 480 GLU GLU B . n 
B 1 481 ILE 481 481 481 ILE ILE B . n 
B 1 482 SER 482 482 482 SER SER B . n 
B 1 483 ARG 483 483 483 ARG ARG B . n 
B 1 484 SER 484 484 484 SER SER B . n 
B 1 485 TRP 485 485 485 TRP TRP B . n 
B 1 486 GLY 486 486 486 GLY GLY B . n 
B 1 487 GLU 487 487 487 GLU GLU B . n 
B 1 488 SER 488 488 488 SER SER B . n 
B 1 489 TYR 489 489 489 TYR TYR B . n 
B 1 490 PHE 490 490 490 PHE PHE B . n 
B 1 491 LEU 491 491 491 LEU LEU B . n 
B 1 492 SER 492 492 492 SER SER B . n 
B 1 493 ASN 493 493 493 ASN ASN B . n 
B 1 494 TYR 494 494 494 TYR TYR B . n 
B 1 495 GLU 495 495 495 GLU GLU B . n 
B 1 496 ARG 496 496 496 ARG ARG B . n 
B 1 497 LEU 497 497 497 LEU LEU B . n 
B 1 498 ILE 498 498 498 ILE ILE B . n 
B 1 499 ARG 499 499 499 ARG ARG B . n 
B 1 500 ALA 500 500 500 ALA ALA B . n 
B 1 501 LYS 501 501 501 LYS LYS B . n 
B 1 502 THR 502 502 502 THR THR B . n 
B 1 503 LEU 503 503 503 LEU LEU B . n 
B 1 504 ILE 504 504 504 ILE ILE B . n 
B 1 505 ASP 505 505 505 ASP ASP B . n 
B 1 506 PRO 506 506 506 PRO PRO B . n 
B 1 507 ASN 507 507 507 ASN ASN B . n 
B 1 508 ASN 508 508 508 ASN ASN B . n 
B 1 509 VAL 509 509 509 VAL VAL B . n 
B 1 510 PHE 510 510 510 PHE PHE B . n 
B 1 511 ASN 511 511 511 ASN ASN B . n 
B 1 512 HIS 512 512 512 HIS HIS B . n 
B 1 513 PRO 513 513 513 PRO PRO B . n 
B 1 514 GLN 514 514 514 GLN GLN B . n 
B 1 515 SER 515 515 515 SER SER B . n 
B 1 516 ILE 516 516 516 ILE ILE B . n 
B 1 517 PRO 517 517 517 PRO PRO B . n 
B 1 518 PRO 518 518 518 PRO PRO B . n 
B 1 519 MET 519 519 519 MET MET B . n 
B 1 520 ALA 520 520 520 ALA ALA B . n 
B 1 521 ASN 521 521 521 ASN ASN B . n 
B 1 522 PHE 522 522 522 PHE PHE B . n 
B 1 523 ASP 523 523 ?   ?   ?   B . n 
B 1 524 TYR 524 524 ?   ?   ?   B . n 
B 1 525 LEU 525 525 ?   ?   ?   B . n 
B 1 526 GLU 526 526 ?   ?   ?   B . n 
B 1 527 LYS 527 527 ?   ?   ?   B . n 
B 1 528 THR 528 528 ?   ?   ?   B . n 
B 1 529 LEU 529 529 ?   ?   ?   B . n 
B 1 530 GLY 530 530 ?   ?   ?   B . n 
B 1 531 SER 531 531 ?   ?   ?   B . n 
B 1 532 ASP 532 532 ?   ?   ?   B . n 
B 1 533 GLY 533 533 ?   ?   ?   B . n 
B 1 534 GLY 534 534 ?   ?   ?   B . n 
B 1 535 GLU 535 535 ?   ?   ?   B . n 
B 1 536 VAL 536 536 ?   ?   ?   B . n 
B 1 537 VAL 537 537 ?   ?   ?   B . n 
B 1 538 ILE 538 538 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   GLU 2   2   ?   ?   ?   C . n 
C 1 3   ASN 3   3   ?   ?   ?   C . n 
C 1 4   LYS 4   4   ?   ?   ?   C . n 
C 1 5   THR 5   5   ?   ?   ?   C . n 
C 1 6   PRO 6   6   ?   ?   ?   C . n 
C 1 7   ILE 7   7   ?   ?   ?   C . n 
C 1 8   PHE 8   8   ?   ?   ?   C . n 
C 1 9   PHE 9   9   ?   ?   ?   C . n 
C 1 10  SER 10  10  ?   ?   ?   C . n 
C 1 11  LEU 11  11  ?   ?   ?   C . n 
C 1 12  SER 12  12  ?   ?   ?   C . n 
C 1 13  ILE 13  13  ?   ?   ?   C . n 
C 1 14  PHE 14  14  ?   ?   ?   C . n 
C 1 15  LEU 15  15  ?   ?   ?   C . n 
C 1 16  SER 16  16  ?   ?   ?   C . n 
C 1 17  LEU 17  17  ?   ?   ?   C . n 
C 1 18  LEU 18  18  ?   ?   ?   C . n 
C 1 19  ASN 19  19  ?   ?   ?   C . n 
C 1 20  CYS 20  20  ?   ?   ?   C . n 
C 1 21  ALA 21  21  ?   ?   ?   C . n 
C 1 22  GLU 22  22  ?   ?   ?   C . n 
C 1 23  ALA 23  23  ?   ?   ?   C . n 
C 1 24  GLY 24  24  ?   ?   ?   C . n 
C 1 25  ASN 25  25  25  ASN ASN C . n 
C 1 26  ASP 26  26  26  ASP ASP C . n 
C 1 27  LEU 27  27  27  LEU LEU C . n 
C 1 28  LEU 28  28  28  LEU LEU C . n 
C 1 29  SER 29  29  29  SER SER C . n 
C 1 30  CYS 30  30  30  CYS CYS C . n 
C 1 31  LEU 31  31  31  LEU LEU C . n 
C 1 32  THR 32  32  32  THR THR C . n 
C 1 33  PHE 33  33  33  PHE PHE C . n 
C 1 34  ASN 34  34  34  ASN ASN C . n 
C 1 35  GLY 35  35  35  GLY GLY C . n 
C 1 36  VAL 36  36  36  VAL VAL C . n 
C 1 37  ARG 37  37  37  ARG ARG C . n 
C 1 38  ASN 38  38  38  ASN ASN C . n 
C 1 39  HIS 39  39  39  HIS HIS C . n 
C 1 40  THR 40  40  40  THR THR C . n 
C 1 41  VAL 41  41  41  VAL VAL C . n 
C 1 42  PHE 42  42  42  PHE PHE C . n 
C 1 43  SER 43  43  43  SER SER C . n 
C 1 44  ALA 44  44  44  ALA ALA C . n 
C 1 45  ASP 45  45  45  ASP ASP C . n 
C 1 46  SER 46  46  46  SER SER C . n 
C 1 47  ASP 47  47  47  ASP ASP C . n 
C 1 48  SER 48  48  48  SER SER C . n 
C 1 49  ASP 49  49  49  ASP ASP C . n 
C 1 50  PHE 50  50  50  PHE PHE C . n 
C 1 51  ASN 51  51  51  ASN ASN C . n 
C 1 52  ARG 52  52  52  ARG ARG C . n 
C 1 53  PHE 53  53  53  PHE PHE C . n 
C 1 54  LEU 54  54  54  LEU LEU C . n 
C 1 55  HIS 55  55  55  HIS HIS C . n 
C 1 56  LEU 56  56  56  LEU LEU C . n 
C 1 57  SER 57  57  57  SER SER C . n 
C 1 58  ILE 58  58  58  ILE ILE C . n 
C 1 59  GLN 59  59  59  GLN GLN C . n 
C 1 60  ASN 60  60  60  ASN ASN C . n 
C 1 61  PRO 61  61  61  PRO PRO C . n 
C 1 62  LEU 62  62  62  LEU LEU C . n 
C 1 63  PHE 63  63  63  PHE PHE C . n 
C 1 64  GLN 64  64  64  GLN GLN C . n 
C 1 65  ASN 65  65  65  ASN ASN C . n 
C 1 66  SER 66  66  66  SER SER C . n 
C 1 67  LEU 67  67  67  LEU LEU C . n 
C 1 68  ILE 68  68  68  ILE ILE C . n 
C 1 69  SER 69  69  69  SER SER C . n 
C 1 70  LYS 70  70  70  LYS LYS C . n 
C 1 71  PRO 71  71  71  PRO PRO C . n 
C 1 72  SER 72  72  72  SER SER C . n 
C 1 73  ALA 73  73  73  ALA ALA C . n 
C 1 74  ILE 74  74  74  ILE ILE C . n 
C 1 75  ILE 75  75  75  ILE ILE C . n 
C 1 76  LEU 76  76  76  LEU LEU C . n 
C 1 77  PRO 77  77  77  PRO PRO C . n 
C 1 78  GLY 78  78  78  GLY GLY C . n 
C 1 79  SER 79  79  79  SER SER C . n 
C 1 80  LYS 80  80  80  LYS LYS C . n 
C 1 81  GLU 81  81  81  GLU GLU C . n 
C 1 82  GLU 82  82  82  GLU GLU C . n 
C 1 83  LEU 83  83  83  LEU LEU C . n 
C 1 84  SER 84  84  84  SER SER C . n 
C 1 85  ASN 85  85  85  ASN ASN C . n 
C 1 86  THR 86  86  86  THR THR C . n 
C 1 87  ILE 87  87  87  ILE ILE C . n 
C 1 88  ARG 88  88  88  ARG ARG C . n 
C 1 89  CYS 89  89  89  CYS CYS C . n 
C 1 90  ILE 90  90  90  ILE ILE C . n 
C 1 91  ARG 91  91  91  ARG ARG C . n 
C 1 92  LYS 92  92  92  LYS LYS C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  SER 94  94  94  SER SER C . n 
C 1 95  TRP 95  95  95  TRP TRP C . n 
C 1 96  THR 96  96  96  THR THR C . n 
C 1 97  ILE 97  97  97  ILE ILE C . n 
C 1 98  ARG 98  98  98  ARG ARG C . n 
C 1 99  LEU 99  99  99  LEU LEU C . n 
C 1 100 ARG 100 100 100 ARG ARG C . n 
C 1 101 SER 101 101 101 SER SER C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 GLY 103 103 103 GLY GLY C . n 
C 1 104 HIS 104 104 104 HIS HIS C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 TYR 106 106 106 TYR TYR C . n 
C 1 107 GLU 107 107 107 GLU GLU C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 LEU 109 109 109 LEU LEU C . n 
C 1 110 SER 110 110 110 SER SER C . n 
C 1 111 TYR 111 111 111 TYR TYR C . n 
C 1 112 THR 112 112 112 THR THR C . n 
C 1 113 SER 113 113 113 SER SER C . n 
C 1 114 ASP 114 114 114 ASP ASP C . n 
C 1 115 THR 115 115 115 THR THR C . n 
C 1 116 PRO 116 116 116 PRO PRO C . n 
C 1 117 PHE 117 117 117 PHE PHE C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 LEU 119 119 119 LEU LEU C . n 
C 1 120 ILE 120 120 120 ILE ILE C . n 
C 1 121 ASP 121 121 121 ASP ASP C . n 
C 1 122 LEU 122 122 122 LEU LEU C . n 
C 1 123 MET 123 123 123 MET MET C . n 
C 1 124 ASN 124 124 124 ASN ASN C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 ASN 126 126 126 ASN ASN C . n 
C 1 127 ARG 127 127 127 ARG ARG C . n 
C 1 128 VAL 128 128 128 VAL VAL C . n 
C 1 129 SER 129 129 129 SER SER C . n 
C 1 130 ILE 130 130 130 ILE ILE C . n 
C 1 131 ASP 131 131 131 ASP ASP C . n 
C 1 132 LEU 132 132 132 LEU LEU C . n 
C 1 133 GLU 133 133 133 GLU GLU C . n 
C 1 134 SER 134 134 134 SER SER C . n 
C 1 135 GLU 135 135 135 GLU GLU C . n 
C 1 136 THR 136 136 136 THR THR C . n 
C 1 137 ALA 137 137 137 ALA ALA C . n 
C 1 138 TRP 138 138 138 TRP TRP C . n 
C 1 139 VAL 139 139 139 VAL VAL C . n 
C 1 140 GLU 140 140 140 GLU GLU C . n 
C 1 141 SER 141 141 141 SER SER C . n 
C 1 142 GLY 142 142 142 GLY GLY C . n 
C 1 143 SER 143 143 143 SER SER C . n 
C 1 144 THR 144 144 144 THR THR C . n 
C 1 145 LEU 145 145 145 LEU LEU C . n 
C 1 146 GLY 146 146 146 GLY GLY C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 LEU 148 148 148 LEU LEU C . n 
C 1 149 TYR 149 149 149 TYR TYR C . n 
C 1 150 TYR 150 150 150 TYR TYR C . n 
C 1 151 ALA 151 151 151 ALA ALA C . n 
C 1 152 ILE 152 152 152 ILE ILE C . n 
C 1 153 THR 153 153 153 THR THR C . n 
C 1 154 GLU 154 154 154 GLU GLU C . n 
C 1 155 SER 155 155 155 SER SER C . n 
C 1 156 SER 156 156 156 SER SER C . n 
C 1 157 SER 157 157 157 SER SER C . n 
C 1 158 LYS 158 158 158 LYS LYS C . n 
C 1 159 LEU 159 159 159 LEU LEU C . n 
C 1 160 GLY 160 160 160 GLY GLY C . n 
C 1 161 PHE 161 161 161 PHE PHE C . n 
C 1 162 THR 162 162 162 THR THR C . n 
C 1 163 ALA 163 163 163 ALA ALA C . n 
C 1 164 ALA 164 164 164 ALA ALA C . n 
C 1 165 TRP 165 165 165 TRP TRP C . n 
C 1 166 CYS 166 166 166 CYS CYS C . n 
C 1 167 PRO 167 167 167 PRO PRO C . n 
C 1 168 THR 168 168 168 THR THR C . n 
C 1 169 VAL 169 169 169 VAL VAL C . n 
C 1 170 GLY 170 170 170 GLY GLY C . n 
C 1 171 THR 171 171 171 THR THR C . n 
C 1 172 GLY 172 172 172 GLY GLY C . n 
C 1 173 GLY 173 173 173 GLY GLY C . n 
C 1 174 HIS 174 174 174 HIS HIS C . n 
C 1 175 ILE 175 175 175 ILE ILE C . n 
C 1 176 SER 176 176 176 SER SER C . n 
C 1 177 GLY 177 177 177 GLY GLY C . n 
C 1 178 GLY 178 178 178 GLY GLY C . n 
C 1 179 GLY 179 179 179 GLY GLY C . n 
C 1 180 PHE 180 180 180 PHE PHE C . n 
C 1 181 GLY 181 181 181 GLY GLY C . n 
C 1 182 MET 182 182 182 MET MET C . n 
C 1 183 MET 183 183 183 MET MET C . n 
C 1 184 SER 184 184 184 SER SER C . n 
C 1 185 ARG 185 185 185 ARG ARG C . n 
C 1 186 LYS 186 186 186 LYS LYS C . n 
C 1 187 TYR 187 187 187 TYR TYR C . n 
C 1 188 GLY 188 188 188 GLY GLY C . n 
C 1 189 LEU 189 189 189 LEU LEU C . n 
C 1 190 ALA 190 190 190 ALA ALA C . n 
C 1 191 ALA 191 191 191 ALA ALA C . n 
C 1 192 ASP 192 192 192 ASP ASP C . n 
C 1 193 ASN 193 193 193 ASN ASN C . n 
C 1 194 VAL 194 194 194 VAL VAL C . n 
C 1 195 VAL 195 195 195 VAL VAL C . n 
C 1 196 ASP 196 196 196 ASP ASP C . n 
C 1 197 ALA 197 197 197 ALA ALA C . n 
C 1 198 ILE 198 198 198 ILE ILE C . n 
C 1 199 LEU 199 199 199 LEU LEU C . n 
C 1 200 ILE 200 200 200 ILE ILE C . n 
C 1 201 ASP 201 201 201 ASP ASP C . n 
C 1 202 ALA 202 202 202 ALA ALA C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 GLY 204 204 204 GLY GLY C . n 
C 1 205 ALA 205 205 205 ALA ALA C . n 
C 1 206 ILE 206 206 206 ILE ILE C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 ASP 208 208 208 ASP ASP C . n 
C 1 209 ARG 209 209 209 ARG ARG C . n 
C 1 210 GLN 210 210 210 GLN GLN C . n 
C 1 211 ALA 211 211 211 ALA ALA C . n 
C 1 212 MET 212 212 212 MET MET C . n 
C 1 213 GLY 213 213 213 GLY GLY C . n 
C 1 214 GLU 214 214 214 GLU GLU C . n 
C 1 215 ASP 215 215 215 ASP ASP C . n 
C 1 216 VAL 216 216 216 VAL VAL C . n 
C 1 217 PHE 217 217 217 PHE PHE C . n 
C 1 218 TRP 218 218 218 TRP TRP C . n 
C 1 219 ALA 219 219 219 ALA ALA C . n 
C 1 220 ILE 220 220 220 ILE ILE C . n 
C 1 221 ARG 221 221 221 ARG ARG C . n 
C 1 222 GLY 222 222 222 GLY GLY C . n 
C 1 223 GLY 223 223 223 GLY GLY C . n 
C 1 224 GLY 224 224 224 GLY GLY C . n 
C 1 225 GLY 225 225 225 GLY GLY C . n 
C 1 226 GLY 226 226 226 GLY GLY C . n 
C 1 227 VAL 227 227 227 VAL VAL C . n 
C 1 228 TRP 228 228 228 TRP TRP C . n 
C 1 229 GLY 229 229 229 GLY GLY C . n 
C 1 230 ALA 230 230 230 ALA ALA C . n 
C 1 231 ILE 231 231 231 ILE ILE C . n 
C 1 232 TYR 232 232 232 TYR TYR C . n 
C 1 233 ALA 233 233 233 ALA ALA C . n 
C 1 234 TRP 234 234 234 TRP TRP C . n 
C 1 235 LYS 235 235 235 LYS LYS C . n 
C 1 236 ILE 236 236 236 ILE ILE C . n 
C 1 237 LYS 237 237 237 LYS LYS C . n 
C 1 238 LEU 238 238 238 LEU LEU C . n 
C 1 239 LEU 239 239 239 LEU LEU C . n 
C 1 240 PRO 240 240 240 PRO PRO C . n 
C 1 241 VAL 241 241 241 VAL VAL C . n 
C 1 242 PRO 242 242 242 PRO PRO C . n 
C 1 243 GLU 243 243 243 GLU GLU C . n 
C 1 244 LYS 244 244 244 LYS LYS C . n 
C 1 245 VAL 245 245 245 VAL VAL C . n 
C 1 246 THR 246 246 246 THR THR C . n 
C 1 247 VAL 247 247 247 VAL VAL C . n 
C 1 248 PHE 248 248 248 PHE PHE C . n 
C 1 249 ARG 249 249 249 ARG ARG C . n 
C 1 250 VAL 250 250 250 VAL VAL C . n 
C 1 251 THR 251 251 251 THR THR C . n 
C 1 252 LYS 252 252 252 LYS LYS C . n 
C 1 253 ASN 253 253 253 ASN ASN C . n 
C 1 254 VAL 254 254 254 VAL VAL C . n 
C 1 255 ALA 255 255 255 ALA ALA C . n 
C 1 256 ILE 256 256 256 ILE ILE C . n 
C 1 257 ASP 257 257 257 ASP ASP C . n 
C 1 258 GLU 258 258 258 GLU GLU C . n 
C 1 259 ALA 259 259 259 ALA ALA C . n 
C 1 260 THR 260 260 260 THR THR C . n 
C 1 261 SER 261 261 261 SER SER C . n 
C 1 262 LEU 262 262 262 LEU LEU C . n 
C 1 263 LEU 263 263 263 LEU LEU C . n 
C 1 264 HIS 264 264 264 HIS HIS C . n 
C 1 265 LYS 265 265 265 LYS LYS C . n 
C 1 266 TRP 266 266 266 TRP TRP C . n 
C 1 267 GLN 267 267 267 GLN GLN C . n 
C 1 268 PHE 268 268 268 PHE PHE C . n 
C 1 269 VAL 269 269 269 VAL VAL C . n 
C 1 270 ALA 270 270 270 ALA ALA C . n 
C 1 271 GLU 271 271 271 GLU GLU C . n 
C 1 272 GLU 272 272 272 GLU GLU C . n 
C 1 273 LEU 273 273 273 LEU LEU C . n 
C 1 274 GLU 274 274 274 GLU GLU C . n 
C 1 275 GLU 275 275 275 GLU GLU C . n 
C 1 276 ASP 276 276 276 ASP ASP C . n 
C 1 277 PHE 277 277 277 PHE PHE C . n 
C 1 278 THR 278 278 278 THR THR C . n 
C 1 279 LEU 279 279 279 LEU LEU C . n 
C 1 280 SER 280 280 280 SER SER C . n 
C 1 281 VAL 281 281 281 VAL VAL C . n 
C 1 282 LEU 282 282 282 LEU LEU C . n 
C 1 283 GLY 283 283 283 GLY GLY C . n 
C 1 284 GLY 284 284 284 GLY GLY C . n 
C 1 285 ALA 285 285 285 ALA ALA C . n 
C 1 286 ASP 286 286 286 ASP ASP C . n 
C 1 287 GLU 287 287 287 GLU GLU C . n 
C 1 288 LYS 288 288 288 LYS LYS C . n 
C 1 289 GLN 289 289 289 GLN GLN C . n 
C 1 290 VAL 290 290 290 VAL VAL C . n 
C 1 291 TRP 291 291 291 TRP TRP C . n 
C 1 292 LEU 292 292 292 LEU LEU C . n 
C 1 293 THR 293 293 293 THR THR C . n 
C 1 294 MET 294 294 294 MET MET C . n 
C 1 295 LEU 295 295 295 LEU LEU C . n 
C 1 296 GLY 296 296 296 GLY GLY C . n 
C 1 297 PHE 297 297 297 PHE PHE C . n 
C 1 298 HIS 298 298 298 HIS HIS C . n 
C 1 299 PHE 299 299 299 PHE PHE C . n 
C 1 300 GLY 300 300 300 GLY GLY C . n 
C 1 301 LEU 301 301 301 LEU LEU C . n 
C 1 302 LYS 302 302 302 LYS LYS C . n 
C 1 303 THR 303 303 303 THR THR C . n 
C 1 304 VAL 304 304 304 VAL VAL C . n 
C 1 305 ALA 305 305 305 ALA ALA C . n 
C 1 306 LYS 306 306 306 LYS LYS C . n 
C 1 307 SER 307 307 307 SER SER C . n 
C 1 308 THR 308 308 308 THR THR C . n 
C 1 309 PHE 309 309 309 PHE PHE C . n 
C 1 310 ASP 310 310 310 ASP ASP C . n 
C 1 311 LEU 311 311 311 LEU LEU C . n 
C 1 312 LEU 312 312 312 LEU LEU C . n 
C 1 313 PHE 313 313 313 PHE PHE C . n 
C 1 314 PRO 314 314 314 PRO PRO C . n 
C 1 315 GLU 315 315 315 GLU GLU C . n 
C 1 316 LEU 316 316 316 LEU LEU C . n 
C 1 317 GLY 317 317 317 GLY GLY C . n 
C 1 318 LEU 318 318 318 LEU LEU C . n 
C 1 319 VAL 319 319 319 VAL VAL C . n 
C 1 320 GLU 320 320 320 GLU GLU C . n 
C 1 321 GLU 321 321 321 GLU GLU C . n 
C 1 322 ASP 322 322 322 ASP ASP C . n 
C 1 323 TYR 323 323 323 TYR TYR C . n 
C 1 324 LEU 324 324 324 LEU LEU C . n 
C 1 325 GLU 325 325 325 GLU GLU C . n 
C 1 326 MET 326 326 326 MET MET C . n 
C 1 327 SER 327 327 327 SER SER C . n 
C 1 328 TRP 328 328 328 TRP TRP C . n 
C 1 329 GLY 329 329 329 GLY GLY C . n 
C 1 330 GLU 330 330 330 GLU GLU C . n 
C 1 331 SER 331 331 331 SER SER C . n 
C 1 332 PHE 332 332 332 PHE PHE C . n 
C 1 333 ALA 333 333 333 ALA ALA C . n 
C 1 334 TYR 334 334 334 TYR TYR C . n 
C 1 335 LEU 335 335 335 LEU LEU C . n 
C 1 336 ALA 336 336 336 ALA ALA C . n 
C 1 337 GLY 337 337 337 GLY GLY C . n 
C 1 338 LEU 338 338 338 LEU LEU C . n 
C 1 339 GLU 339 339 339 GLU GLU C . n 
C 1 340 THR 340 340 340 THR THR C . n 
C 1 341 VAL 341 341 341 VAL VAL C . n 
C 1 342 SER 342 342 342 SER SER C . n 
C 1 343 GLN 343 343 343 GLN GLN C . n 
C 1 344 LEU 344 344 344 LEU LEU C . n 
C 1 345 ASN 345 345 345 ASN ASN C . n 
C 1 346 ASN 346 346 346 ASN ASN C . n 
C 1 347 ARG 347 347 347 ARG ARG C . n 
C 1 348 PHE 348 348 348 PHE PHE C . n 
C 1 349 LEU 349 349 349 LEU LEU C . n 
C 1 350 LYS 350 350 350 LYS LYS C . n 
C 1 351 PHE 351 351 351 PHE PHE C . n 
C 1 352 ASP 352 352 352 ASP ASP C . n 
C 1 353 GLU 353 353 353 GLU GLU C . n 
C 1 354 ARG 354 354 354 ARG ARG C . n 
C 1 355 ALA 355 355 355 ALA ALA C . n 
C 1 356 PHE 356 356 356 PHE PHE C . n 
C 1 357 LYS 357 357 357 LYS LYS C . n 
C 1 358 THR 358 358 358 THR THR C . n 
C 1 359 LYS 359 359 359 LYS LYS C . n 
C 1 360 VAL 360 360 360 VAL VAL C . n 
C 1 361 ASP 361 361 361 ASP ASP C . n 
C 1 362 LEU 362 362 362 LEU LEU C . n 
C 1 363 THR 363 363 363 THR THR C . n 
C 1 364 LYS 364 364 364 LYS LYS C . n 
C 1 365 GLU 365 365 365 GLU GLU C . n 
C 1 366 PRO 366 366 366 PRO PRO C . n 
C 1 367 LEU 367 367 367 LEU LEU C . n 
C 1 368 PRO 368 368 368 PRO PRO C . n 
C 1 369 SER 369 369 369 SER SER C . n 
C 1 370 LYS 370 370 370 LYS LYS C . n 
C 1 371 ALA 371 371 371 ALA ALA C . n 
C 1 372 PHE 372 372 372 PHE PHE C . n 
C 1 373 TYR 373 373 373 TYR TYR C . n 
C 1 374 GLY 374 374 374 GLY GLY C . n 
C 1 375 LEU 375 375 375 LEU LEU C . n 
C 1 376 LEU 376 376 376 LEU LEU C . n 
C 1 377 GLU 377 377 377 GLU GLU C . n 
C 1 378 ARG 378 378 378 ARG ARG C . n 
C 1 379 LEU 379 379 379 LEU LEU C . n 
C 1 380 SER 380 380 380 SER SER C . n 
C 1 381 LYS 381 381 381 LYS LYS C . n 
C 1 382 GLU 382 382 382 GLU GLU C . n 
C 1 383 PRO 383 383 383 PRO PRO C . n 
C 1 384 ASN 384 384 384 ASN ASN C . n 
C 1 385 GLY 385 385 385 GLY GLY C . n 
C 1 386 PHE 386 386 386 PHE PHE C . n 
C 1 387 ILE 387 387 387 ILE ILE C . n 
C 1 388 ALA 388 388 388 ALA ALA C . n 
C 1 389 LEU 389 389 389 LEU LEU C . n 
C 1 390 ASN 390 390 390 ASN ASN C . n 
C 1 391 GLY 391 391 391 GLY GLY C . n 
C 1 392 PHE 392 392 392 PHE PHE C . n 
C 1 393 GLY 393 393 393 GLY GLY C . n 
C 1 394 GLY 394 394 394 GLY GLY C . n 
C 1 395 GLN 395 395 395 GLN GLN C . n 
C 1 396 MET 396 396 396 MET MET C . n 
C 1 397 SER 397 397 397 SER SER C . n 
C 1 398 LYS 398 398 398 LYS LYS C . n 
C 1 399 ILE 399 399 399 ILE ILE C . n 
C 1 400 SER 400 400 400 SER SER C . n 
C 1 401 SER 401 401 401 SER SER C . n 
C 1 402 ASP 402 402 402 ASP ASP C . n 
C 1 403 PHE 403 403 403 PHE PHE C . n 
C 1 404 THR 404 404 404 THR THR C . n 
C 1 405 PRO 405 405 405 PRO PRO C . n 
C 1 406 PHE 406 406 406 PHE PHE C . n 
C 1 407 PRO 407 407 407 PRO PRO C . n 
C 1 408 HIS 408 408 408 HIS HIS C . n 
C 1 409 ARG 409 409 409 ARG ARG C . n 
C 1 410 SER 410 410 410 SER SER C . n 
C 1 411 GLY 411 411 411 GLY GLY C . n 
C 1 412 THR 412 412 412 THR THR C . n 
C 1 413 ARG 413 413 413 ARG ARG C . n 
C 1 414 LEU 414 414 414 LEU LEU C . n 
C 1 415 MET 415 415 415 MET MET C . n 
C 1 416 VAL 416 416 416 VAL VAL C . n 
C 1 417 GLU 417 417 417 GLU GLU C . n 
C 1 418 TYR 418 418 418 TYR TYR C . n 
C 1 419 ILE 419 419 419 ILE ILE C . n 
C 1 420 VAL 420 420 420 VAL VAL C . n 
C 1 421 ALA 421 421 421 ALA ALA C . n 
C 1 422 TRP 422 422 422 TRP TRP C . n 
C 1 423 ASN 423 423 423 ASN ASN C . n 
C 1 424 GLN 424 424 424 GLN GLN C . n 
C 1 425 SER 425 425 425 SER SER C . n 
C 1 426 GLU 426 426 426 GLU GLU C . n 
C 1 427 GLN 427 427 427 GLN GLN C . n 
C 1 428 LYS 428 428 428 LYS LYS C . n 
C 1 429 LYS 429 429 429 LYS LYS C . n 
C 1 430 LYS 430 430 430 LYS LYS C . n 
C 1 431 THR 431 431 431 THR THR C . n 
C 1 432 GLU 432 432 432 GLU GLU C . n 
C 1 433 PHE 433 433 433 PHE PHE C . n 
C 1 434 LEU 434 434 434 LEU LEU C . n 
C 1 435 ASP 435 435 435 ASP ASP C . n 
C 1 436 TRP 436 436 436 TRP TRP C . n 
C 1 437 LEU 437 437 437 LEU LEU C . n 
C 1 438 GLU 438 438 438 GLU GLU C . n 
C 1 439 LYS 439 439 439 LYS LYS C . n 
C 1 440 VAL 440 440 440 VAL VAL C . n 
C 1 441 TYR 441 441 441 TYR TYR C . n 
C 1 442 GLU 442 442 442 GLU GLU C . n 
C 1 443 PHE 443 443 443 PHE PHE C . n 
C 1 444 MET 444 444 444 MET MET C . n 
C 1 445 LYS 445 445 445 LYS LYS C . n 
C 1 446 PRO 446 446 446 PRO PRO C . n 
C 1 447 PHE 447 447 447 PHE PHE C . n 
C 1 448 VAL 448 448 448 VAL VAL C . n 
C 1 449 SER 449 449 449 SER SER C . n 
C 1 450 LYS 450 450 450 LYS LYS C . n 
C 1 451 ASN 451 451 451 ASN ASN C . n 
C 1 452 PRO 452 452 452 PRO PRO C . n 
C 1 453 ARG 453 453 453 ARG ARG C . n 
C 1 454 LEU 454 454 454 LEU LEU C . n 
C 1 455 GLY 455 455 455 GLY GLY C . n 
C 1 456 TYR 456 456 456 TYR TYR C . n 
C 1 457 VAL 457 457 457 VAL VAL C . n 
C 1 458 ASN 458 458 458 ASN ASN C . n 
C 1 459 HIS 459 459 459 HIS HIS C . n 
C 1 460 ILE 460 460 460 ILE ILE C . n 
C 1 461 ASP 461 461 461 ASP ASP C . n 
C 1 462 LEU 462 462 462 LEU LEU C . n 
C 1 463 ASP 463 463 463 ASP ASP C . n 
C 1 464 LEU 464 464 464 LEU LEU C . n 
C 1 465 GLY 465 465 465 GLY GLY C . n 
C 1 466 GLY 466 466 466 GLY GLY C . n 
C 1 467 ILE 467 467 467 ILE ILE C . n 
C 1 468 ASP 468 468 468 ASP ASP C . n 
C 1 469 TRP 469 469 469 TRP TRP C . n 
C 1 470 GLY 470 470 470 GLY GLY C . n 
C 1 471 ASN 471 471 471 ASN ASN C . n 
C 1 472 LYS 472 472 472 LYS LYS C . n 
C 1 473 THR 473 473 473 THR THR C . n 
C 1 474 VAL 474 474 474 VAL VAL C . n 
C 1 475 VAL 475 475 475 VAL VAL C . n 
C 1 476 ASN 476 476 476 ASN ASN C . n 
C 1 477 ASN 477 477 477 ASN ASN C . n 
C 1 478 ALA 478 478 478 ALA ALA C . n 
C 1 479 ILE 479 479 479 ILE ILE C . n 
C 1 480 GLU 480 480 480 GLU GLU C . n 
C 1 481 ILE 481 481 481 ILE ILE C . n 
C 1 482 SER 482 482 482 SER SER C . n 
C 1 483 ARG 483 483 483 ARG ARG C . n 
C 1 484 SER 484 484 484 SER SER C . n 
C 1 485 TRP 485 485 485 TRP TRP C . n 
C 1 486 GLY 486 486 486 GLY GLY C . n 
C 1 487 GLU 487 487 487 GLU GLU C . n 
C 1 488 SER 488 488 488 SER SER C . n 
C 1 489 TYR 489 489 489 TYR TYR C . n 
C 1 490 PHE 490 490 490 PHE PHE C . n 
C 1 491 LEU 491 491 491 LEU LEU C . n 
C 1 492 SER 492 492 492 SER SER C . n 
C 1 493 ASN 493 493 493 ASN ASN C . n 
C 1 494 TYR 494 494 494 TYR TYR C . n 
C 1 495 GLU 495 495 495 GLU GLU C . n 
C 1 496 ARG 496 496 496 ARG ARG C . n 
C 1 497 LEU 497 497 497 LEU LEU C . n 
C 1 498 ILE 498 498 498 ILE ILE C . n 
C 1 499 ARG 499 499 499 ARG ARG C . n 
C 1 500 ALA 500 500 500 ALA ALA C . n 
C 1 501 LYS 501 501 501 LYS LYS C . n 
C 1 502 THR 502 502 502 THR THR C . n 
C 1 503 LEU 503 503 503 LEU LEU C . n 
C 1 504 ILE 504 504 504 ILE ILE C . n 
C 1 505 ASP 505 505 505 ASP ASP C . n 
C 1 506 PRO 506 506 506 PRO PRO C . n 
C 1 507 ASN 507 507 507 ASN ASN C . n 
C 1 508 ASN 508 508 508 ASN ASN C . n 
C 1 509 VAL 509 509 509 VAL VAL C . n 
C 1 510 PHE 510 510 510 PHE PHE C . n 
C 1 511 ASN 511 511 511 ASN ASN C . n 
C 1 512 HIS 512 512 512 HIS HIS C . n 
C 1 513 PRO 513 513 513 PRO PRO C . n 
C 1 514 GLN 514 514 514 GLN GLN C . n 
C 1 515 SER 515 515 515 SER SER C . n 
C 1 516 ILE 516 516 516 ILE ILE C . n 
C 1 517 PRO 517 517 517 PRO PRO C . n 
C 1 518 PRO 518 518 518 PRO PRO C . n 
C 1 519 MET 519 519 519 MET MET C . n 
C 1 520 ALA 520 520 520 ALA ALA C . n 
C 1 521 ASN 521 521 ?   ?   ?   C . n 
C 1 522 PHE 522 522 ?   ?   ?   C . n 
C 1 523 ASP 523 523 ?   ?   ?   C . n 
C 1 524 TYR 524 524 ?   ?   ?   C . n 
C 1 525 LEU 525 525 ?   ?   ?   C . n 
C 1 526 GLU 526 526 ?   ?   ?   C . n 
C 1 527 LYS 527 527 ?   ?   ?   C . n 
C 1 528 THR 528 528 ?   ?   ?   C . n 
C 1 529 LEU 529 529 ?   ?   ?   C . n 
C 1 530 GLY 530 530 ?   ?   ?   C . n 
C 1 531 SER 531 531 ?   ?   ?   C . n 
C 1 532 ASP 532 532 ?   ?   ?   C . n 
C 1 533 GLY 533 533 ?   ?   ?   C . n 
C 1 534 GLY 534 534 ?   ?   ?   C . n 
C 1 535 GLU 535 535 ?   ?   ?   C . n 
C 1 536 VAL 536 536 ?   ?   ?   C . n 
C 1 537 VAL 537 537 ?   ?   ?   C . n 
C 1 538 ILE 538 538 ?   ?   ?   C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   GLU 2   2   ?   ?   ?   D . n 
D 1 3   ASN 3   3   ?   ?   ?   D . n 
D 1 4   LYS 4   4   ?   ?   ?   D . n 
D 1 5   THR 5   5   ?   ?   ?   D . n 
D 1 6   PRO 6   6   ?   ?   ?   D . n 
D 1 7   ILE 7   7   ?   ?   ?   D . n 
D 1 8   PHE 8   8   ?   ?   ?   D . n 
D 1 9   PHE 9   9   ?   ?   ?   D . n 
D 1 10  SER 10  10  ?   ?   ?   D . n 
D 1 11  LEU 11  11  ?   ?   ?   D . n 
D 1 12  SER 12  12  ?   ?   ?   D . n 
D 1 13  ILE 13  13  ?   ?   ?   D . n 
D 1 14  PHE 14  14  ?   ?   ?   D . n 
D 1 15  LEU 15  15  ?   ?   ?   D . n 
D 1 16  SER 16  16  ?   ?   ?   D . n 
D 1 17  LEU 17  17  ?   ?   ?   D . n 
D 1 18  LEU 18  18  ?   ?   ?   D . n 
D 1 19  ASN 19  19  ?   ?   ?   D . n 
D 1 20  CYS 20  20  ?   ?   ?   D . n 
D 1 21  ALA 21  21  ?   ?   ?   D . n 
D 1 22  GLU 22  22  ?   ?   ?   D . n 
D 1 23  ALA 23  23  ?   ?   ?   D . n 
D 1 24  GLY 24  24  ?   ?   ?   D . n 
D 1 25  ASN 25  25  ?   ?   ?   D . n 
D 1 26  ASP 26  26  26  ASP ASP D . n 
D 1 27  LEU 27  27  27  LEU LEU D . n 
D 1 28  LEU 28  28  28  LEU LEU D . n 
D 1 29  SER 29  29  29  SER SER D . n 
D 1 30  CYS 30  30  30  CYS CYS D . n 
D 1 31  LEU 31  31  31  LEU LEU D . n 
D 1 32  THR 32  32  32  THR THR D . n 
D 1 33  PHE 33  33  33  PHE PHE D . n 
D 1 34  ASN 34  34  34  ASN ASN D . n 
D 1 35  GLY 35  35  35  GLY GLY D . n 
D 1 36  VAL 36  36  36  VAL VAL D . n 
D 1 37  ARG 37  37  37  ARG ARG D . n 
D 1 38  ASN 38  38  38  ASN ASN D . n 
D 1 39  HIS 39  39  39  HIS HIS D . n 
D 1 40  THR 40  40  40  THR THR D . n 
D 1 41  VAL 41  41  41  VAL VAL D . n 
D 1 42  PHE 42  42  42  PHE PHE D . n 
D 1 43  SER 43  43  43  SER SER D . n 
D 1 44  ALA 44  44  44  ALA ALA D . n 
D 1 45  ASP 45  45  45  ASP ASP D . n 
D 1 46  SER 46  46  46  SER SER D . n 
D 1 47  ASP 47  47  47  ASP ASP D . n 
D 1 48  SER 48  48  48  SER SER D . n 
D 1 49  ASP 49  49  49  ASP ASP D . n 
D 1 50  PHE 50  50  50  PHE PHE D . n 
D 1 51  ASN 51  51  51  ASN ASN D . n 
D 1 52  ARG 52  52  52  ARG ARG D . n 
D 1 53  PHE 53  53  53  PHE PHE D . n 
D 1 54  LEU 54  54  54  LEU LEU D . n 
D 1 55  HIS 55  55  55  HIS HIS D . n 
D 1 56  LEU 56  56  56  LEU LEU D . n 
D 1 57  SER 57  57  57  SER SER D . n 
D 1 58  ILE 58  58  58  ILE ILE D . n 
D 1 59  GLN 59  59  59  GLN GLN D . n 
D 1 60  ASN 60  60  60  ASN ASN D . n 
D 1 61  PRO 61  61  61  PRO PRO D . n 
D 1 62  LEU 62  62  62  LEU LEU D . n 
D 1 63  PHE 63  63  63  PHE PHE D . n 
D 1 64  GLN 64  64  64  GLN GLN D . n 
D 1 65  ASN 65  65  65  ASN ASN D . n 
D 1 66  SER 66  66  66  SER SER D . n 
D 1 67  LEU 67  67  67  LEU LEU D . n 
D 1 68  ILE 68  68  68  ILE ILE D . n 
D 1 69  SER 69  69  69  SER SER D . n 
D 1 70  LYS 70  70  70  LYS LYS D . n 
D 1 71  PRO 71  71  71  PRO PRO D . n 
D 1 72  SER 72  72  72  SER SER D . n 
D 1 73  ALA 73  73  73  ALA ALA D . n 
D 1 74  ILE 74  74  74  ILE ILE D . n 
D 1 75  ILE 75  75  75  ILE ILE D . n 
D 1 76  LEU 76  76  76  LEU LEU D . n 
D 1 77  PRO 77  77  77  PRO PRO D . n 
D 1 78  GLY 78  78  78  GLY GLY D . n 
D 1 79  SER 79  79  79  SER SER D . n 
D 1 80  LYS 80  80  80  LYS LYS D . n 
D 1 81  GLU 81  81  81  GLU GLU D . n 
D 1 82  GLU 82  82  82  GLU GLU D . n 
D 1 83  LEU 83  83  83  LEU LEU D . n 
D 1 84  SER 84  84  84  SER SER D . n 
D 1 85  ASN 85  85  85  ASN ASN D . n 
D 1 86  THR 86  86  86  THR THR D . n 
D 1 87  ILE 87  87  87  ILE ILE D . n 
D 1 88  ARG 88  88  88  ARG ARG D . n 
D 1 89  CYS 89  89  89  CYS CYS D . n 
D 1 90  ILE 90  90  90  ILE ILE D . n 
D 1 91  ARG 91  91  91  ARG ARG D . n 
D 1 92  LYS 92  92  92  LYS LYS D . n 
D 1 93  GLY 93  93  93  GLY GLY D . n 
D 1 94  SER 94  94  94  SER SER D . n 
D 1 95  TRP 95  95  95  TRP TRP D . n 
D 1 96  THR 96  96  96  THR THR D . n 
D 1 97  ILE 97  97  97  ILE ILE D . n 
D 1 98  ARG 98  98  98  ARG ARG D . n 
D 1 99  LEU 99  99  99  LEU LEU D . n 
D 1 100 ARG 100 100 100 ARG ARG D . n 
D 1 101 SER 101 101 101 SER SER D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 GLY 103 103 103 GLY GLY D . n 
D 1 104 HIS 104 104 104 HIS HIS D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 TYR 106 106 106 TYR TYR D . n 
D 1 107 GLU 107 107 107 GLU GLU D . n 
D 1 108 GLY 108 108 108 GLY GLY D . n 
D 1 109 LEU 109 109 109 LEU LEU D . n 
D 1 110 SER 110 110 110 SER SER D . n 
D 1 111 TYR 111 111 111 TYR TYR D . n 
D 1 112 THR 112 112 112 THR THR D . n 
D 1 113 SER 113 113 113 SER SER D . n 
D 1 114 ASP 114 114 114 ASP ASP D . n 
D 1 115 THR 115 115 115 THR THR D . n 
D 1 116 PRO 116 116 116 PRO PRO D . n 
D 1 117 PHE 117 117 117 PHE PHE D . n 
D 1 118 ILE 118 118 118 ILE ILE D . n 
D 1 119 LEU 119 119 119 LEU LEU D . n 
D 1 120 ILE 120 120 120 ILE ILE D . n 
D 1 121 ASP 121 121 121 ASP ASP D . n 
D 1 122 LEU 122 122 122 LEU LEU D . n 
D 1 123 MET 123 123 123 MET MET D . n 
D 1 124 ASN 124 124 124 ASN ASN D . n 
D 1 125 LEU 125 125 125 LEU LEU D . n 
D 1 126 ASN 126 126 126 ASN ASN D . n 
D 1 127 ARG 127 127 127 ARG ARG D . n 
D 1 128 VAL 128 128 128 VAL VAL D . n 
D 1 129 SER 129 129 129 SER SER D . n 
D 1 130 ILE 130 130 130 ILE ILE D . n 
D 1 131 ASP 131 131 131 ASP ASP D . n 
D 1 132 LEU 132 132 132 LEU LEU D . n 
D 1 133 GLU 133 133 133 GLU GLU D . n 
D 1 134 SER 134 134 134 SER SER D . n 
D 1 135 GLU 135 135 135 GLU GLU D . n 
D 1 136 THR 136 136 136 THR THR D . n 
D 1 137 ALA 137 137 137 ALA ALA D . n 
D 1 138 TRP 138 138 138 TRP TRP D . n 
D 1 139 VAL 139 139 139 VAL VAL D . n 
D 1 140 GLU 140 140 140 GLU GLU D . n 
D 1 141 SER 141 141 141 SER SER D . n 
D 1 142 GLY 142 142 142 GLY GLY D . n 
D 1 143 SER 143 143 143 SER SER D . n 
D 1 144 THR 144 144 144 THR THR D . n 
D 1 145 LEU 145 145 145 LEU LEU D . n 
D 1 146 GLY 146 146 146 GLY GLY D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 LEU 148 148 148 LEU LEU D . n 
D 1 149 TYR 149 149 149 TYR TYR D . n 
D 1 150 TYR 150 150 150 TYR TYR D . n 
D 1 151 ALA 151 151 151 ALA ALA D . n 
D 1 152 ILE 152 152 152 ILE ILE D . n 
D 1 153 THR 153 153 153 THR THR D . n 
D 1 154 GLU 154 154 154 GLU GLU D . n 
D 1 155 SER 155 155 155 SER SER D . n 
D 1 156 SER 156 156 156 SER SER D . n 
D 1 157 SER 157 157 157 SER SER D . n 
D 1 158 LYS 158 158 158 LYS LYS D . n 
D 1 159 LEU 159 159 159 LEU LEU D . n 
D 1 160 GLY 160 160 160 GLY GLY D . n 
D 1 161 PHE 161 161 161 PHE PHE D . n 
D 1 162 THR 162 162 162 THR THR D . n 
D 1 163 ALA 163 163 163 ALA ALA D . n 
D 1 164 ALA 164 164 164 ALA ALA D . n 
D 1 165 TRP 165 165 165 TRP TRP D . n 
D 1 166 CYS 166 166 166 CYS CYS D . n 
D 1 167 PRO 167 167 167 PRO PRO D . n 
D 1 168 THR 168 168 168 THR THR D . n 
D 1 169 VAL 169 169 169 VAL VAL D . n 
D 1 170 GLY 170 170 170 GLY GLY D . n 
D 1 171 THR 171 171 171 THR THR D . n 
D 1 172 GLY 172 172 172 GLY GLY D . n 
D 1 173 GLY 173 173 173 GLY GLY D . n 
D 1 174 HIS 174 174 174 HIS HIS D . n 
D 1 175 ILE 175 175 175 ILE ILE D . n 
D 1 176 SER 176 176 176 SER SER D . n 
D 1 177 GLY 177 177 177 GLY GLY D . n 
D 1 178 GLY 178 178 178 GLY GLY D . n 
D 1 179 GLY 179 179 179 GLY GLY D . n 
D 1 180 PHE 180 180 180 PHE PHE D . n 
D 1 181 GLY 181 181 181 GLY GLY D . n 
D 1 182 MET 182 182 182 MET MET D . n 
D 1 183 MET 183 183 183 MET MET D . n 
D 1 184 SER 184 184 184 SER SER D . n 
D 1 185 ARG 185 185 185 ARG ARG D . n 
D 1 186 LYS 186 186 186 LYS LYS D . n 
D 1 187 TYR 187 187 187 TYR TYR D . n 
D 1 188 GLY 188 188 188 GLY GLY D . n 
D 1 189 LEU 189 189 189 LEU LEU D . n 
D 1 190 ALA 190 190 190 ALA ALA D . n 
D 1 191 ALA 191 191 191 ALA ALA D . n 
D 1 192 ASP 192 192 192 ASP ASP D . n 
D 1 193 ASN 193 193 193 ASN ASN D . n 
D 1 194 VAL 194 194 194 VAL VAL D . n 
D 1 195 VAL 195 195 195 VAL VAL D . n 
D 1 196 ASP 196 196 196 ASP ASP D . n 
D 1 197 ALA 197 197 197 ALA ALA D . n 
D 1 198 ILE 198 198 198 ILE ILE D . n 
D 1 199 LEU 199 199 199 LEU LEU D . n 
D 1 200 ILE 200 200 200 ILE ILE D . n 
D 1 201 ASP 201 201 201 ASP ASP D . n 
D 1 202 ALA 202 202 202 ALA ALA D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 GLY 204 204 204 GLY GLY D . n 
D 1 205 ALA 205 205 205 ALA ALA D . n 
D 1 206 ILE 206 206 206 ILE ILE D . n 
D 1 207 LEU 207 207 207 LEU LEU D . n 
D 1 208 ASP 208 208 208 ASP ASP D . n 
D 1 209 ARG 209 209 209 ARG ARG D . n 
D 1 210 GLN 210 210 210 GLN GLN D . n 
D 1 211 ALA 211 211 211 ALA ALA D . n 
D 1 212 MET 212 212 212 MET MET D . n 
D 1 213 GLY 213 213 213 GLY GLY D . n 
D 1 214 GLU 214 214 214 GLU GLU D . n 
D 1 215 ASP 215 215 215 ASP ASP D . n 
D 1 216 VAL 216 216 216 VAL VAL D . n 
D 1 217 PHE 217 217 217 PHE PHE D . n 
D 1 218 TRP 218 218 218 TRP TRP D . n 
D 1 219 ALA 219 219 219 ALA ALA D . n 
D 1 220 ILE 220 220 220 ILE ILE D . n 
D 1 221 ARG 221 221 221 ARG ARG D . n 
D 1 222 GLY 222 222 222 GLY GLY D . n 
D 1 223 GLY 223 223 223 GLY GLY D . n 
D 1 224 GLY 224 224 224 GLY GLY D . n 
D 1 225 GLY 225 225 225 GLY GLY D . n 
D 1 226 GLY 226 226 226 GLY GLY D . n 
D 1 227 VAL 227 227 227 VAL VAL D . n 
D 1 228 TRP 228 228 228 TRP TRP D . n 
D 1 229 GLY 229 229 229 GLY GLY D . n 
D 1 230 ALA 230 230 230 ALA ALA D . n 
D 1 231 ILE 231 231 231 ILE ILE D . n 
D 1 232 TYR 232 232 232 TYR TYR D . n 
D 1 233 ALA 233 233 233 ALA ALA D . n 
D 1 234 TRP 234 234 234 TRP TRP D . n 
D 1 235 LYS 235 235 235 LYS LYS D . n 
D 1 236 ILE 236 236 236 ILE ILE D . n 
D 1 237 LYS 237 237 237 LYS LYS D . n 
D 1 238 LEU 238 238 238 LEU LEU D . n 
D 1 239 LEU 239 239 239 LEU LEU D . n 
D 1 240 PRO 240 240 240 PRO PRO D . n 
D 1 241 VAL 241 241 241 VAL VAL D . n 
D 1 242 PRO 242 242 242 PRO PRO D . n 
D 1 243 GLU 243 243 243 GLU GLU D . n 
D 1 244 LYS 244 244 244 LYS LYS D . n 
D 1 245 VAL 245 245 245 VAL VAL D . n 
D 1 246 THR 246 246 246 THR THR D . n 
D 1 247 VAL 247 247 247 VAL VAL D . n 
D 1 248 PHE 248 248 248 PHE PHE D . n 
D 1 249 ARG 249 249 249 ARG ARG D . n 
D 1 250 VAL 250 250 250 VAL VAL D . n 
D 1 251 THR 251 251 251 THR THR D . n 
D 1 252 LYS 252 252 252 LYS LYS D . n 
D 1 253 ASN 253 253 253 ASN ASN D . n 
D 1 254 VAL 254 254 254 VAL VAL D . n 
D 1 255 ALA 255 255 255 ALA ALA D . n 
D 1 256 ILE 256 256 256 ILE ILE D . n 
D 1 257 ASP 257 257 257 ASP ASP D . n 
D 1 258 GLU 258 258 258 GLU GLU D . n 
D 1 259 ALA 259 259 259 ALA ALA D . n 
D 1 260 THR 260 260 260 THR THR D . n 
D 1 261 SER 261 261 261 SER SER D . n 
D 1 262 LEU 262 262 262 LEU LEU D . n 
D 1 263 LEU 263 263 263 LEU LEU D . n 
D 1 264 HIS 264 264 264 HIS HIS D . n 
D 1 265 LYS 265 265 265 LYS LYS D . n 
D 1 266 TRP 266 266 266 TRP TRP D . n 
D 1 267 GLN 267 267 267 GLN GLN D . n 
D 1 268 PHE 268 268 268 PHE PHE D . n 
D 1 269 VAL 269 269 269 VAL VAL D . n 
D 1 270 ALA 270 270 270 ALA ALA D . n 
D 1 271 GLU 271 271 271 GLU GLU D . n 
D 1 272 GLU 272 272 272 GLU GLU D . n 
D 1 273 LEU 273 273 273 LEU LEU D . n 
D 1 274 GLU 274 274 274 GLU GLU D . n 
D 1 275 GLU 275 275 275 GLU GLU D . n 
D 1 276 ASP 276 276 276 ASP ASP D . n 
D 1 277 PHE 277 277 277 PHE PHE D . n 
D 1 278 THR 278 278 278 THR THR D . n 
D 1 279 LEU 279 279 279 LEU LEU D . n 
D 1 280 SER 280 280 280 SER SER D . n 
D 1 281 VAL 281 281 281 VAL VAL D . n 
D 1 282 LEU 282 282 282 LEU LEU D . n 
D 1 283 GLY 283 283 283 GLY GLY D . n 
D 1 284 GLY 284 284 284 GLY GLY D . n 
D 1 285 ALA 285 285 285 ALA ALA D . n 
D 1 286 ASP 286 286 286 ASP ASP D . n 
D 1 287 GLU 287 287 287 GLU GLU D . n 
D 1 288 LYS 288 288 288 LYS LYS D . n 
D 1 289 GLN 289 289 289 GLN GLN D . n 
D 1 290 VAL 290 290 290 VAL VAL D . n 
D 1 291 TRP 291 291 291 TRP TRP D . n 
D 1 292 LEU 292 292 292 LEU LEU D . n 
D 1 293 THR 293 293 293 THR THR D . n 
D 1 294 MET 294 294 294 MET MET D . n 
D 1 295 LEU 295 295 295 LEU LEU D . n 
D 1 296 GLY 296 296 296 GLY GLY D . n 
D 1 297 PHE 297 297 297 PHE PHE D . n 
D 1 298 HIS 298 298 298 HIS HIS D . n 
D 1 299 PHE 299 299 299 PHE PHE D . n 
D 1 300 GLY 300 300 300 GLY GLY D . n 
D 1 301 LEU 301 301 301 LEU LEU D . n 
D 1 302 LYS 302 302 302 LYS LYS D . n 
D 1 303 THR 303 303 303 THR THR D . n 
D 1 304 VAL 304 304 304 VAL VAL D . n 
D 1 305 ALA 305 305 305 ALA ALA D . n 
D 1 306 LYS 306 306 306 LYS LYS D . n 
D 1 307 SER 307 307 307 SER SER D . n 
D 1 308 THR 308 308 308 THR THR D . n 
D 1 309 PHE 309 309 309 PHE PHE D . n 
D 1 310 ASP 310 310 310 ASP ASP D . n 
D 1 311 LEU 311 311 311 LEU LEU D . n 
D 1 312 LEU 312 312 312 LEU LEU D . n 
D 1 313 PHE 313 313 313 PHE PHE D . n 
D 1 314 PRO 314 314 314 PRO PRO D . n 
D 1 315 GLU 315 315 315 GLU GLU D . n 
D 1 316 LEU 316 316 316 LEU LEU D . n 
D 1 317 GLY 317 317 317 GLY GLY D . n 
D 1 318 LEU 318 318 318 LEU LEU D . n 
D 1 319 VAL 319 319 319 VAL VAL D . n 
D 1 320 GLU 320 320 320 GLU GLU D . n 
D 1 321 GLU 321 321 321 GLU GLU D . n 
D 1 322 ASP 322 322 322 ASP ASP D . n 
D 1 323 TYR 323 323 323 TYR TYR D . n 
D 1 324 LEU 324 324 324 LEU LEU D . n 
D 1 325 GLU 325 325 325 GLU GLU D . n 
D 1 326 MET 326 326 326 MET MET D . n 
D 1 327 SER 327 327 327 SER SER D . n 
D 1 328 TRP 328 328 328 TRP TRP D . n 
D 1 329 GLY 329 329 329 GLY GLY D . n 
D 1 330 GLU 330 330 330 GLU GLU D . n 
D 1 331 SER 331 331 331 SER SER D . n 
D 1 332 PHE 332 332 332 PHE PHE D . n 
D 1 333 ALA 333 333 333 ALA ALA D . n 
D 1 334 TYR 334 334 334 TYR TYR D . n 
D 1 335 LEU 335 335 335 LEU LEU D . n 
D 1 336 ALA 336 336 336 ALA ALA D . n 
D 1 337 GLY 337 337 337 GLY GLY D . n 
D 1 338 LEU 338 338 338 LEU LEU D . n 
D 1 339 GLU 339 339 339 GLU GLU D . n 
D 1 340 THR 340 340 340 THR THR D . n 
D 1 341 VAL 341 341 341 VAL VAL D . n 
D 1 342 SER 342 342 342 SER SER D . n 
D 1 343 GLN 343 343 343 GLN GLN D . n 
D 1 344 LEU 344 344 344 LEU LEU D . n 
D 1 345 ASN 345 345 345 ASN ASN D . n 
D 1 346 ASN 346 346 346 ASN ASN D . n 
D 1 347 ARG 347 347 347 ARG ARG D . n 
D 1 348 PHE 348 348 348 PHE PHE D . n 
D 1 349 LEU 349 349 349 LEU LEU D . n 
D 1 350 LYS 350 350 350 LYS LYS D . n 
D 1 351 PHE 351 351 351 PHE PHE D . n 
D 1 352 ASP 352 352 352 ASP ASP D . n 
D 1 353 GLU 353 353 353 GLU GLU D . n 
D 1 354 ARG 354 354 354 ARG ARG D . n 
D 1 355 ALA 355 355 355 ALA ALA D . n 
D 1 356 PHE 356 356 356 PHE PHE D . n 
D 1 357 LYS 357 357 357 LYS LYS D . n 
D 1 358 THR 358 358 358 THR THR D . n 
D 1 359 LYS 359 359 359 LYS LYS D . n 
D 1 360 VAL 360 360 360 VAL VAL D . n 
D 1 361 ASP 361 361 361 ASP ASP D . n 
D 1 362 LEU 362 362 362 LEU LEU D . n 
D 1 363 THR 363 363 363 THR THR D . n 
D 1 364 LYS 364 364 364 LYS LYS D . n 
D 1 365 GLU 365 365 365 GLU GLU D . n 
D 1 366 PRO 366 366 366 PRO PRO D . n 
D 1 367 LEU 367 367 367 LEU LEU D . n 
D 1 368 PRO 368 368 368 PRO PRO D . n 
D 1 369 SER 369 369 369 SER SER D . n 
D 1 370 LYS 370 370 370 LYS LYS D . n 
D 1 371 ALA 371 371 371 ALA ALA D . n 
D 1 372 PHE 372 372 372 PHE PHE D . n 
D 1 373 TYR 373 373 373 TYR TYR D . n 
D 1 374 GLY 374 374 374 GLY GLY D . n 
D 1 375 LEU 375 375 375 LEU LEU D . n 
D 1 376 LEU 376 376 376 LEU LEU D . n 
D 1 377 GLU 377 377 377 GLU GLU D . n 
D 1 378 ARG 378 378 378 ARG ARG D . n 
D 1 379 LEU 379 379 379 LEU LEU D . n 
D 1 380 SER 380 380 380 SER SER D . n 
D 1 381 LYS 381 381 381 LYS LYS D . n 
D 1 382 GLU 382 382 382 GLU GLU D . n 
D 1 383 PRO 383 383 383 PRO PRO D . n 
D 1 384 ASN 384 384 384 ASN ASN D . n 
D 1 385 GLY 385 385 385 GLY GLY D . n 
D 1 386 PHE 386 386 386 PHE PHE D . n 
D 1 387 ILE 387 387 387 ILE ILE D . n 
D 1 388 ALA 388 388 388 ALA ALA D . n 
D 1 389 LEU 389 389 389 LEU LEU D . n 
D 1 390 ASN 390 390 390 ASN ASN D . n 
D 1 391 GLY 391 391 391 GLY GLY D . n 
D 1 392 PHE 392 392 392 PHE PHE D . n 
D 1 393 GLY 393 393 393 GLY GLY D . n 
D 1 394 GLY 394 394 394 GLY GLY D . n 
D 1 395 GLN 395 395 395 GLN GLN D . n 
D 1 396 MET 396 396 396 MET MET D . n 
D 1 397 SER 397 397 397 SER SER D . n 
D 1 398 LYS 398 398 398 LYS LYS D . n 
D 1 399 ILE 399 399 399 ILE ILE D . n 
D 1 400 SER 400 400 400 SER SER D . n 
D 1 401 SER 401 401 401 SER SER D . n 
D 1 402 ASP 402 402 402 ASP ASP D . n 
D 1 403 PHE 403 403 403 PHE PHE D . n 
D 1 404 THR 404 404 404 THR THR D . n 
D 1 405 PRO 405 405 405 PRO PRO D . n 
D 1 406 PHE 406 406 406 PHE PHE D . n 
D 1 407 PRO 407 407 407 PRO PRO D . n 
D 1 408 HIS 408 408 408 HIS HIS D . n 
D 1 409 ARG 409 409 409 ARG ARG D . n 
D 1 410 SER 410 410 410 SER SER D . n 
D 1 411 GLY 411 411 411 GLY GLY D . n 
D 1 412 THR 412 412 412 THR THR D . n 
D 1 413 ARG 413 413 413 ARG ARG D . n 
D 1 414 LEU 414 414 414 LEU LEU D . n 
D 1 415 MET 415 415 415 MET MET D . n 
D 1 416 VAL 416 416 416 VAL VAL D . n 
D 1 417 GLU 417 417 417 GLU GLU D . n 
D 1 418 TYR 418 418 418 TYR TYR D . n 
D 1 419 ILE 419 419 419 ILE ILE D . n 
D 1 420 VAL 420 420 420 VAL VAL D . n 
D 1 421 ALA 421 421 421 ALA ALA D . n 
D 1 422 TRP 422 422 422 TRP TRP D . n 
D 1 423 ASN 423 423 423 ASN ASN D . n 
D 1 424 GLN 424 424 424 GLN GLN D . n 
D 1 425 SER 425 425 425 SER SER D . n 
D 1 426 GLU 426 426 426 GLU GLU D . n 
D 1 427 GLN 427 427 427 GLN GLN D . n 
D 1 428 LYS 428 428 428 LYS LYS D . n 
D 1 429 LYS 429 429 429 LYS LYS D . n 
D 1 430 LYS 430 430 430 LYS LYS D . n 
D 1 431 THR 431 431 431 THR THR D . n 
D 1 432 GLU 432 432 432 GLU GLU D . n 
D 1 433 PHE 433 433 433 PHE PHE D . n 
D 1 434 LEU 434 434 434 LEU LEU D . n 
D 1 435 ASP 435 435 435 ASP ASP D . n 
D 1 436 TRP 436 436 436 TRP TRP D . n 
D 1 437 LEU 437 437 437 LEU LEU D . n 
D 1 438 GLU 438 438 438 GLU GLU D . n 
D 1 439 LYS 439 439 439 LYS LYS D . n 
D 1 440 VAL 440 440 440 VAL VAL D . n 
D 1 441 TYR 441 441 441 TYR TYR D . n 
D 1 442 GLU 442 442 442 GLU GLU D . n 
D 1 443 PHE 443 443 443 PHE PHE D . n 
D 1 444 MET 444 444 444 MET MET D . n 
D 1 445 LYS 445 445 445 LYS LYS D . n 
D 1 446 PRO 446 446 446 PRO PRO D . n 
D 1 447 PHE 447 447 447 PHE PHE D . n 
D 1 448 VAL 448 448 448 VAL VAL D . n 
D 1 449 SER 449 449 449 SER SER D . n 
D 1 450 LYS 450 450 450 LYS LYS D . n 
D 1 451 ASN 451 451 451 ASN ASN D . n 
D 1 452 PRO 452 452 452 PRO PRO D . n 
D 1 453 ARG 453 453 453 ARG ARG D . n 
D 1 454 LEU 454 454 454 LEU LEU D . n 
D 1 455 GLY 455 455 455 GLY GLY D . n 
D 1 456 TYR 456 456 456 TYR TYR D . n 
D 1 457 VAL 457 457 457 VAL VAL D . n 
D 1 458 ASN 458 458 458 ASN ASN D . n 
D 1 459 HIS 459 459 459 HIS HIS D . n 
D 1 460 ILE 460 460 460 ILE ILE D . n 
D 1 461 ASP 461 461 461 ASP ASP D . n 
D 1 462 LEU 462 462 462 LEU LEU D . n 
D 1 463 ASP 463 463 463 ASP ASP D . n 
D 1 464 LEU 464 464 464 LEU LEU D . n 
D 1 465 GLY 465 465 465 GLY GLY D . n 
D 1 466 GLY 466 466 466 GLY GLY D . n 
D 1 467 ILE 467 467 467 ILE ILE D . n 
D 1 468 ASP 468 468 468 ASP ASP D . n 
D 1 469 TRP 469 469 469 TRP TRP D . n 
D 1 470 GLY 470 470 470 GLY GLY D . n 
D 1 471 ASN 471 471 471 ASN ASN D . n 
D 1 472 LYS 472 472 472 LYS LYS D . n 
D 1 473 THR 473 473 473 THR THR D . n 
D 1 474 VAL 474 474 474 VAL VAL D . n 
D 1 475 VAL 475 475 475 VAL VAL D . n 
D 1 476 ASN 476 476 476 ASN ASN D . n 
D 1 477 ASN 477 477 477 ASN ASN D . n 
D 1 478 ALA 478 478 478 ALA ALA D . n 
D 1 479 ILE 479 479 479 ILE ILE D . n 
D 1 480 GLU 480 480 480 GLU GLU D . n 
D 1 481 ILE 481 481 481 ILE ILE D . n 
D 1 482 SER 482 482 482 SER SER D . n 
D 1 483 ARG 483 483 483 ARG ARG D . n 
D 1 484 SER 484 484 484 SER SER D . n 
D 1 485 TRP 485 485 485 TRP TRP D . n 
D 1 486 GLY 486 486 486 GLY GLY D . n 
D 1 487 GLU 487 487 487 GLU GLU D . n 
D 1 488 SER 488 488 488 SER SER D . n 
D 1 489 TYR 489 489 489 TYR TYR D . n 
D 1 490 PHE 490 490 490 PHE PHE D . n 
D 1 491 LEU 491 491 491 LEU LEU D . n 
D 1 492 SER 492 492 492 SER SER D . n 
D 1 493 ASN 493 493 493 ASN ASN D . n 
D 1 494 TYR 494 494 494 TYR TYR D . n 
D 1 495 GLU 495 495 495 GLU GLU D . n 
D 1 496 ARG 496 496 496 ARG ARG D . n 
D 1 497 LEU 497 497 497 LEU LEU D . n 
D 1 498 ILE 498 498 498 ILE ILE D . n 
D 1 499 ARG 499 499 499 ARG ARG D . n 
D 1 500 ALA 500 500 500 ALA ALA D . n 
D 1 501 LYS 501 501 501 LYS LYS D . n 
D 1 502 THR 502 502 502 THR THR D . n 
D 1 503 LEU 503 503 503 LEU LEU D . n 
D 1 504 ILE 504 504 504 ILE ILE D . n 
D 1 505 ASP 505 505 505 ASP ASP D . n 
D 1 506 PRO 506 506 506 PRO PRO D . n 
D 1 507 ASN 507 507 507 ASN ASN D . n 
D 1 508 ASN 508 508 508 ASN ASN D . n 
D 1 509 VAL 509 509 509 VAL VAL D . n 
D 1 510 PHE 510 510 510 PHE PHE D . n 
D 1 511 ASN 511 511 511 ASN ASN D . n 
D 1 512 HIS 512 512 512 HIS HIS D . n 
D 1 513 PRO 513 513 513 PRO PRO D . n 
D 1 514 GLN 514 514 514 GLN GLN D . n 
D 1 515 SER 515 515 515 SER SER D . n 
D 1 516 ILE 516 516 516 ILE ILE D . n 
D 1 517 PRO 517 517 517 PRO PRO D . n 
D 1 518 PRO 518 518 518 PRO PRO D . n 
D 1 519 MET 519 519 519 MET MET D . n 
D 1 520 ALA 520 520 520 ALA ALA D . n 
D 1 521 ASN 521 521 521 ASN ASN D . n 
D 1 522 PHE 522 522 522 PHE PHE D . n 
D 1 523 ASP 523 523 ?   ?   ?   D . n 
D 1 524 TYR 524 524 ?   ?   ?   D . n 
D 1 525 LEU 525 525 ?   ?   ?   D . n 
D 1 526 GLU 526 526 ?   ?   ?   D . n 
D 1 527 LYS 527 527 ?   ?   ?   D . n 
D 1 528 THR 528 528 ?   ?   ?   D . n 
D 1 529 LEU 529 529 ?   ?   ?   D . n 
D 1 530 GLY 530 530 ?   ?   ?   D . n 
D 1 531 SER 531 531 ?   ?   ?   D . n 
D 1 532 ASP 532 532 ?   ?   ?   D . n 
D 1 533 GLY 533 533 ?   ?   ?   D . n 
D 1 534 GLY 534 534 ?   ?   ?   D . n 
D 1 535 GLU 535 535 ?   ?   ?   D . n 
D 1 536 VAL 536 536 ?   ?   ?   D . n 
D 1 537 VAL 537 537 ?   ?   ?   D . n 
D 1 538 ILE 538 538 ?   ?   ?   D . n 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 C ASN 471 C ASN 471 ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 471 A ASN 471 ? ASN 'GLYCOSYLATION SITE' 
3 B ASN 38  B ASN 38  ? ASN 'GLYCOSYLATION SITE' 
4 D ASN 471 D ASN 471 ? ASN 'GLYCOSYLATION SITE' 
5 B ASN 471 B ASN 471 ? ASN 'GLYCOSYLATION SITE' 
6 C ASN 38  C ASN 38  ? ASN 'GLYCOSYLATION SITE' 
7 A ASN 38  A ASN 38  ? ASN 'GLYCOSYLATION SITE' 
8 D ASN 38  D ASN 38  ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly   ?    monomeric 1 
2 author_defined_assembly   ?    monomeric 1 
3 author_defined_assembly   ?    monomeric 1 
4 author_defined_assembly   ?    monomeric 1 
5 software_defined_assembly PISA dimeric   2 
6 software_defined_assembly PISA dimeric   2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,F,G,H,BA                       
2 1 B,I,J,K,L,M,CA                     
3 1 C,N,O,P,Q,R,S,T,DA                 
4 1 D,U,V,W,X,Y,Z,AA,EA                
5 1 A,C,E,F,G,H,N,O,P,Q,R,S,T,BA,DA    
6 1 B,D,I,J,K,L,M,U,V,W,X,Y,Z,AA,CA,EA 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
5 'ABSA (A^2)' 6930  ? 
5 MORE         -37   ? 
5 'SSA (A^2)'  37570 ? 
6 'ABSA (A^2)' 7000  ? 
6 MORE         -51   ? 
6 'SSA (A^2)'  37150 ? 
# 
_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_
_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 2014-04-23 
2 'Structure model' 1 1 2014-05-14 
3 'Structure model' 1 2 2015-03-04 
4 'Structure model' 1 3 2015-03-25 
5 'Structure model' 1 4 2015-04-01 
6 'Structure model' 1 5 2015-04-22 
7 'Structure model' 1 6 2015-09-02 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
3 4 'Structure model' 'Database references' 
4 5 'Structure model' 'Structure summary'   
5 6 'Structure model' Other                 
6 7 'Structure model' 'Database references' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
ProDC  'data collection' .                             ? 1 
PHASER phasing           mr                            ? 2 
PHENIX refinement        '(phenix.refine: 1.8.4_1496)' ? 3 
XDS    'data reduction'  .                             ? 4 
XSCALE 'data scaling'    .                             ? 5 
# 
_pdbx_entry_details.entry_id             4PZF 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     'CONFLICT MUTATIONS ARE CLEAVING SITES.' 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
# 
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 O4  C NAG 602 ? ? C2  C NAG 603 ? ? 2.08 
2 1 ND2 C ASN 471 ? ? O5  C NAG 604 ? ? 2.10 
3 1 NH2 B ARG 483 ? ? OE2 B GLU 495 ? ? 2.11 
4 1 ND2 A ASN 471 ? ? O5  A NAG 604 ? ? 2.14 
5 1 O4  B NAG 602 ? ? C2  B NAG 603 ? ? 2.16 
6 1 ND2 C ASN 38  ? ? O5  C NAG 602 ? ? 2.18 
7 1 NH2 D ARG 52  ? ? O7  D NAG 603 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE1 
_pdbx_validate_symm_contact.auth_asym_id_1    C 
_pdbx_validate_symm_contact.auth_comp_id_1    GLU 
_pdbx_validate_symm_contact.auth_seq_id_1     495 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    NH1 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    ARG 
_pdbx_validate_symm_contact.auth_seq_id_2     499 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_556 
_pdbx_validate_symm_contact.dist              2.18 
# 
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 LEU A 67  ? ? -66.53  -151.52 
2  1 ILE A 68  ? ? 63.45   143.72  
3  1 SER A 101 ? ? -102.72 -77.17  
4  1 TYR A 111 ? ? -141.48 21.12   
5  1 LEU A 125 ? ? -103.01 70.41   
6  1 ARG A 221 ? ? -88.15  49.30   
7  1 GLU A 287 ? ? -124.84 -121.85 
8  1 PHE A 392 ? ? -92.26  -128.25 
9  1 ARG A 409 ? ? -109.61 -115.84 
10 1 HIS A 459 ? ? -99.41  52.81   
11 1 LEU A 491 ? ? 50.92   -125.10 
12 1 PRO B 61  ? ? -47.49  -15.64  
13 1 SER B 101 ? ? -107.37 -77.73  
14 1 TYR B 111 ? ? -141.47 20.70   
15 1 LEU B 125 ? ? -101.31 67.36   
16 1 GLU B 154 ? ? -69.49  1.31    
17 1 ARG B 221 ? ? -91.66  47.74   
18 1 VAL B 227 ? ? -132.00 -35.11  
19 1 LEU B 282 ? ? -89.32  -93.66  
20 1 GLU B 287 ? ? 56.23   73.50   
21 1 LYS B 288 ? ? 50.05   -4.79   
22 1 PHE B 313 ? ? -151.59 63.75   
23 1 SER B 369 ? ? -35.56  -36.03  
24 1 GLU B 382 ? ? -160.93 101.17  
25 1 PHE B 392 ? ? -90.27  -130.32 
26 1 ARG B 409 ? ? -113.84 -111.38 
27 1 HIS B 459 ? ? -101.32 54.22   
28 1 LEU B 491 ? ? 51.97   -117.11 
29 1 ALA B 520 ? ? -119.46 -159.28 
30 1 PRO C 61  ? ? -47.07  -15.90  
31 1 SER C 101 ? ? -106.08 -72.25  
32 1 TYR C 111 ? ? -143.09 17.02   
33 1 LEU C 125 ? ? -102.52 69.67   
34 1 ARG C 221 ? ? -90.81  49.79   
35 1 VAL C 269 ? ? 57.16   -84.33  
36 1 ASP C 286 ? ? -151.51 74.42   
37 1 GLU C 287 ? ? 54.81   102.60  
38 1 LYS C 288 ? ? 46.38   -15.87  
39 1 PHE C 392 ? ? -90.17  -130.97 
40 1 ARG C 409 ? ? -113.83 -114.08 
41 1 VAL C 448 ? ? -107.32 -165.38 
42 1 HIS C 459 ? ? -100.88 57.33   
43 1 LEU C 491 ? ? 51.02   -124.82 
44 1 PRO D 61  ? ? -46.91  -18.37  
45 1 GLN D 64  ? ? -93.38  -63.92  
46 1 SER D 66  ? ? 45.84   -48.04  
47 1 SER D 101 ? ? -105.51 -74.83  
48 1 TYR D 111 ? ? -143.50 15.58   
49 1 ARG D 221 ? ? -92.17  49.14   
50 1 GLU D 287 ? ? 45.42   -91.41  
51 1 GLU D 353 ? ? -156.79 15.56   
52 1 PHE D 392 ? ? -88.94  -123.22 
53 1 ARG D 409 ? ? -112.98 -111.80 
54 1 ASN D 423 ? ? -67.06  -176.87 
55 1 GLN D 424 ? ? -59.35  -154.54 
56 1 SER D 425 ? ? 54.55   -59.09  
57 1 HIS D 459 ? ? -103.30 56.28   
58 1 LEU D 491 ? ? 51.64   -119.28 
# 
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 N 1 C 12P 605 ? C9  ? R 12P 1 C9  
2  1 N 1 C 12P 605 ? C8  ? R 12P 1 C8  
3  1 N 1 C 12P 605 ? O7  ? R 12P 1 O7  
4  1 N 1 C 12P 605 ? C6  ? R 12P 1 C6  
5  1 N 1 C 12P 605 ? C5  ? R 12P 1 C5  
6  1 N 1 C 12P 605 ? O4  ? R 12P 1 O4  
7  1 N 1 C 12P 605 ? C3  ? R 12P 1 C3  
8  1 N 1 C 12P 605 ? C2  ? R 12P 1 C2  
9  1 N 1 C 12P 605 ? O1  ? R 12P 1 O1  
10 1 N 1 D 12P 605 ? C15 ? Y 12P 1 C15 
11 1 N 1 D 12P 605 ? C14 ? Y 12P 1 C14 
12 1 N 1 D 12P 605 ? O13 ? Y 12P 1 O13 
13 1 N 1 D 12P 605 ? C12 ? Y 12P 1 C12 
14 1 N 1 D 12P 605 ? C11 ? Y 12P 1 C11 
15 1 N 1 D 12P 605 ? O10 ? Y 12P 1 O10 
16 1 N 1 D 12P 605 ? C9  ? Y 12P 1 C9  
17 1 N 1 D 12P 605 ? C8  ? Y 12P 1 C8  
18 1 N 1 D 12P 605 ? O7  ? Y 12P 1 O7  
19 1 N 1 D 12P 605 ? C6  ? Y 12P 1 C6  
20 1 N 1 D 12P 605 ? C5  ? Y 12P 1 C5  
21 1 N 1 D 12P 605 ? O4  ? Y 12P 1 O4  
22 1 N 1 D 12P 605 ? C3  ? Y 12P 1 C3  
23 1 N 1 D 12P 605 ? C2  ? Y 12P 1 C2  
24 1 N 1 D 12P 605 ? O1  ? Y 12P 1 O1  
# 
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 GLU 2   ? A GLU 2   
3   1 Y 1 A ASN 3   ? A ASN 3   
4   1 Y 1 A LYS 4   ? A LYS 4   
5   1 Y 1 A THR 5   ? A THR 5   
6   1 Y 1 A PRO 6   ? A PRO 6   
7   1 Y 1 A ILE 7   ? A ILE 7   
8   1 Y 1 A PHE 8   ? A PHE 8   
9   1 Y 1 A PHE 9   ? A PHE 9   
10  1 Y 1 A SER 10  ? A SER 10  
11  1 Y 1 A LEU 11  ? A LEU 11  
12  1 Y 1 A SER 12  ? A SER 12  
13  1 Y 1 A ILE 13  ? A ILE 13  
14  1 Y 1 A PHE 14  ? A PHE 14  
15  1 Y 1 A LEU 15  ? A LEU 15  
16  1 Y 1 A SER 16  ? A SER 16  
17  1 Y 1 A LEU 17  ? A LEU 17  
18  1 Y 1 A LEU 18  ? A LEU 18  
19  1 Y 1 A ASN 19  ? A ASN 19  
20  1 Y 1 A CYS 20  ? A CYS 20  
21  1 Y 1 A ALA 21  ? A ALA 21  
22  1 Y 1 A GLU 22  ? A GLU 22  
23  1 Y 1 A ALA 23  ? A ALA 23  
24  1 Y 1 A GLY 24  ? A GLY 24  
25  1 Y 1 A ASN 25  ? A ASN 25  
26  1 Y 1 A TYR 524 ? A TYR 524 
27  1 Y 1 A LEU 525 ? A LEU 525 
28  1 Y 1 A GLU 526 ? A GLU 526 
29  1 Y 1 A LYS 527 ? A LYS 527 
30  1 Y 1 A THR 528 ? A THR 528 
31  1 Y 1 A LEU 529 ? A LEU 529 
32  1 Y 1 A GLY 530 ? A GLY 530 
33  1 Y 1 A SER 531 ? A SER 531 
34  1 Y 1 A ASP 532 ? A ASP 532 
35  1 Y 1 A GLY 533 ? A GLY 533 
36  1 Y 1 A GLY 534 ? A GLY 534 
37  1 Y 1 A GLU 535 ? A GLU 535 
38  1 Y 1 A VAL 536 ? A VAL 536 
39  1 Y 1 A VAL 537 ? A VAL 537 
40  1 Y 1 A ILE 538 ? A ILE 538 
41  1 Y 1 B MET 1   ? B MET 1   
42  1 Y 1 B GLU 2   ? B GLU 2   
43  1 Y 1 B ASN 3   ? B ASN 3   
44  1 Y 1 B LYS 4   ? B LYS 4   
45  1 Y 1 B THR 5   ? B THR 5   
46  1 Y 1 B PRO 6   ? B PRO 6   
47  1 Y 1 B ILE 7   ? B ILE 7   
48  1 Y 1 B PHE 8   ? B PHE 8   
49  1 Y 1 B PHE 9   ? B PHE 9   
50  1 Y 1 B SER 10  ? B SER 10  
51  1 Y 1 B LEU 11  ? B LEU 11  
52  1 Y 1 B SER 12  ? B SER 12  
53  1 Y 1 B ILE 13  ? B ILE 13  
54  1 Y 1 B PHE 14  ? B PHE 14  
55  1 Y 1 B LEU 15  ? B LEU 15  
56  1 Y 1 B SER 16  ? B SER 16  
57  1 Y 1 B LEU 17  ? B LEU 17  
58  1 Y 1 B LEU 18  ? B LEU 18  
59  1 Y 1 B ASN 19  ? B ASN 19  
60  1 Y 1 B CYS 20  ? B CYS 20  
61  1 Y 1 B ALA 21  ? B ALA 21  
62  1 Y 1 B GLU 22  ? B GLU 22  
63  1 Y 1 B ALA 23  ? B ALA 23  
64  1 Y 1 B GLY 24  ? B GLY 24  
65  1 Y 1 B ASP 523 ? B ASP 523 
66  1 Y 1 B TYR 524 ? B TYR 524 
67  1 Y 1 B LEU 525 ? B LEU 525 
68  1 Y 1 B GLU 526 ? B GLU 526 
69  1 Y 1 B LYS 527 ? B LYS 527 
70  1 Y 1 B THR 528 ? B THR 528 
71  1 Y 1 B LEU 529 ? B LEU 529 
72  1 Y 1 B GLY 530 ? B GLY 530 
73  1 Y 1 B SER 531 ? B SER 531 
74  1 Y 1 B ASP 532 ? B ASP 532 
75  1 Y 1 B GLY 533 ? B GLY 533 
76  1 Y 1 B GLY 534 ? B GLY 534 
77  1 Y 1 B GLU 535 ? B GLU 535 
78  1 Y 1 B VAL 536 ? B VAL 536 
79  1 Y 1 B VAL 537 ? B VAL 537 
80  1 Y 1 B ILE 538 ? B ILE 538 
81  1 Y 1 C MET 1   ? C MET 1   
82  1 Y 1 C GLU 2   ? C GLU 2   
83  1 Y 1 C ASN 3   ? C ASN 3   
84  1 Y 1 C LYS 4   ? C LYS 4   
85  1 Y 1 C THR 5   ? C THR 5   
86  1 Y 1 C PRO 6   ? C PRO 6   
87  1 Y 1 C ILE 7   ? C ILE 7   
88  1 Y 1 C PHE 8   ? C PHE 8   
89  1 Y 1 C PHE 9   ? C PHE 9   
90  1 Y 1 C SER 10  ? C SER 10  
91  1 Y 1 C LEU 11  ? C LEU 11  
92  1 Y 1 C SER 12  ? C SER 12  
93  1 Y 1 C ILE 13  ? C ILE 13  
94  1 Y 1 C PHE 14  ? C PHE 14  
95  1 Y 1 C LEU 15  ? C LEU 15  
96  1 Y 1 C SER 16  ? C SER 16  
97  1 Y 1 C LEU 17  ? C LEU 17  
98  1 Y 1 C LEU 18  ? C LEU 18  
99  1 Y 1 C ASN 19  ? C ASN 19  
100 1 Y 1 C CYS 20  ? C CYS 20  
101 1 Y 1 C ALA 21  ? C ALA 21  
102 1 Y 1 C GLU 22  ? C GLU 22  
103 1 Y 1 C ALA 23  ? C ALA 23  
104 1 Y 1 C GLY 24  ? C GLY 24  
105 1 Y 1 C ASN 521 ? C ASN 521 
106 1 Y 1 C PHE 522 ? C PHE 522 
107 1 Y 1 C ASP 523 ? C ASP 523 
108 1 Y 1 C TYR 524 ? C TYR 524 
109 1 Y 1 C LEU 525 ? C LEU 525 
110 1 Y 1 C GLU 526 ? C GLU 526 
111 1 Y 1 C LYS 527 ? C LYS 527 
112 1 Y 1 C THR 528 ? C THR 528 
113 1 Y 1 C LEU 529 ? C LEU 529 
114 1 Y 1 C GLY 530 ? C GLY 530 
115 1 Y 1 C SER 531 ? C SER 531 
116 1 Y 1 C ASP 532 ? C ASP 532 
117 1 Y 1 C GLY 533 ? C GLY 533 
118 1 Y 1 C GLY 534 ? C GLY 534 
119 1 Y 1 C GLU 535 ? C GLU 535 
120 1 Y 1 C VAL 536 ? C VAL 536 
121 1 Y 1 C VAL 537 ? C VAL 537 
122 1 Y 1 C ILE 538 ? C ILE 538 
123 1 Y 1 D MET 1   ? D MET 1   
124 1 Y 1 D GLU 2   ? D GLU 2   
125 1 Y 1 D ASN 3   ? D ASN 3   
126 1 Y 1 D LYS 4   ? D LYS 4   
127 1 Y 1 D THR 5   ? D THR 5   
128 1 Y 1 D PRO 6   ? D PRO 6   
129 1 Y 1 D ILE 7   ? D ILE 7   
130 1 Y 1 D PHE 8   ? D PHE 8   
131 1 Y 1 D PHE 9   ? D PHE 9   
132 1 Y 1 D SER 10  ? D SER 10  
133 1 Y 1 D LEU 11  ? D LEU 11  
134 1 Y 1 D SER 12  ? D SER 12  
135 1 Y 1 D ILE 13  ? D ILE 13  
136 1 Y 1 D PHE 14  ? D PHE 14  
137 1 Y 1 D LEU 15  ? D LEU 15  
138 1 Y 1 D SER 16  ? D SER 16  
139 1 Y 1 D LEU 17  ? D LEU 17  
140 1 Y 1 D LEU 18  ? D LEU 18  
141 1 Y 1 D ASN 19  ? D ASN 19  
142 1 Y 1 D CYS 20  ? D CYS 20  
143 1 Y 1 D ALA 21  ? D ALA 21  
144 1 Y 1 D GLU 22  ? D GLU 22  
145 1 Y 1 D ALA 23  ? D ALA 23  
146 1 Y 1 D GLY 24  ? D GLY 24  
147 1 Y 1 D ASN 25  ? D ASN 25  
148 1 Y 1 D ASP 523 ? D ASP 523 
149 1 Y 1 D TYR 524 ? D TYR 524 
150 1 Y 1 D LEU 525 ? D LEU 525 
151 1 Y 1 D GLU 526 ? D GLU 526 
152 1 Y 1 D LYS 527 ? D LYS 527 
153 1 Y 1 D THR 528 ? D THR 528 
154 1 Y 1 D LEU 529 ? D LEU 529 
155 1 Y 1 D GLY 530 ? D GLY 530 
156 1 Y 1 D SER 531 ? D SER 531 
157 1 Y 1 D ASP 532 ? D ASP 532 
158 1 Y 1 D GLY 533 ? D GLY 533 
159 1 Y 1 D GLY 534 ? D GLY 534 
160 1 Y 1 D GLU 535 ? D GLU 535 
161 1 Y 1 D VAL 536 ? D VAL 536 
162 1 Y 1 D VAL 537 ? D VAL 537 
163 1 Y 1 D ILE 538 ? D ILE 538 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 N-ACETYL-D-GLUCOSAMINE        NAG 
4 'SULFATE ION'                 SO4 
5 'DODECAETHYLENE GLYCOL'       12P 
6 water                         HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 FAD 1   601 600 FAD FAD A . 
F  3 NAG 1   602 701 NAG NAG A . 
G  3 NAG 2   603 702 NAG NAG A . 
H  3 NAG 1   604 801 NAG NAG A . 
I  2 FAD 1   601 600 FAD FAD B . 
J  3 NAG 1   602 701 NAG NAG B . 
K  3 NAG 2   603 702 NAG NAG B . 
L  3 NAG 1   604 801 NAG NAG B . 
M  4 SO4 1   605 3   SO4 SO4 B . 
N  2 FAD 1   601 600 FAD FAD C . 
O  3 NAG 1   602 701 NAG NAG C . 
P  3 NAG 2   603 702 NAG NAG C . 
Q  3 NAG 1   604 801 NAG NAG C . 
R  5 12P 1   605 2   12P 12P C . 
S  4 SO4 1   606 4   SO4 SO4 C . 
T  4 SO4 1   607 7   SO4 SO4 C . 
U  2 FAD 1   601 600 FAD FAD D . 
V  3 NAG 1   602 701 NAG NAG D . 
W  3 NAG 2   603 702 NAG NAG D . 
X  3 NAG 1   604 801 NAG NAG D . 
Y  5 12P 1   605 1   12P 12P D . 
Z  4 SO4 1   606 5   SO4 SO4 D . 
AA 4 SO4 1   607 6   SO4 SO4 D . 
BA 6 HOH 1   701 37  HOH HOH A . 
BA 6 HOH 2   702 38  HOH HOH A . 
BA 6 HOH 3   703 39  HOH HOH A . 
BA 6 HOH 4   704 40  HOH HOH A . 
BA 6 HOH 5   705 41  HOH HOH A . 
BA 6 HOH 6   706 42  HOH HOH A . 
BA 6 HOH 7   707 43  HOH HOH A . 
BA 6 HOH 8   708 44  HOH HOH A . 
BA 6 HOH 9   709 45  HOH HOH A . 
BA 6 HOH 10  710 46  HOH HOH A . 
BA 6 HOH 11  711 47  HOH HOH A . 
BA 6 HOH 12  712 48  HOH HOH A . 
BA 6 HOH 13  713 49  HOH HOH A . 
BA 6 HOH 14  714 50  HOH HOH A . 
BA 6 HOH 15  715 51  HOH HOH A . 
BA 6 HOH 16  716 52  HOH HOH A . 
BA 6 HOH 17  717 54  HOH HOH A . 
BA 6 HOH 18  718 55  HOH HOH A . 
BA 6 HOH 19  719 56  HOH HOH A . 
BA 6 HOH 20  720 57  HOH HOH A . 
BA 6 HOH 21  721 58  HOH HOH A . 
BA 6 HOH 22  722 59  HOH HOH A . 
BA 6 HOH 23  723 60  HOH HOH A . 
BA 6 HOH 24  724 61  HOH HOH A . 
BA 6 HOH 25  725 62  HOH HOH A . 
BA 6 HOH 26  726 63  HOH HOH A . 
BA 6 HOH 27  727 64  HOH HOH A . 
BA 6 HOH 28  728 65  HOH HOH A . 
BA 6 HOH 29  729 66  HOH HOH A . 
BA 6 HOH 30  730 68  HOH HOH A . 
BA 6 HOH 31  731 69  HOH HOH A . 
BA 6 HOH 32  732 70  HOH HOH A . 
BA 6 HOH 33  733 71  HOH HOH A . 
BA 6 HOH 34  734 72  HOH HOH A . 
BA 6 HOH 35  735 73  HOH HOH A . 
BA 6 HOH 36  736 74  HOH HOH A . 
BA 6 HOH 37  737 75  HOH HOH A . 
BA 6 HOH 38  738 76  HOH HOH A . 
BA 6 HOH 39  739 77  HOH HOH A . 
BA 6 HOH 40  740 78  HOH HOH A . 
BA 6 HOH 41  741 79  HOH HOH A . 
BA 6 HOH 42  742 80  HOH HOH A . 
BA 6 HOH 43  743 81  HOH HOH A . 
BA 6 HOH 44  744 82  HOH HOH A . 
BA 6 HOH 45  745 83  HOH HOH A . 
BA 6 HOH 46  746 84  HOH HOH A . 
BA 6 HOH 47  747 85  HOH HOH A . 
BA 6 HOH 48  748 86  HOH HOH A . 
BA 6 HOH 49  749 87  HOH HOH A . 
BA 6 HOH 50  750 88  HOH HOH A . 
BA 6 HOH 51  751 89  HOH HOH A . 
BA 6 HOH 52  752 90  HOH HOH A . 
BA 6 HOH 53  753 92  HOH HOH A . 
BA 6 HOH 54  754 93  HOH HOH A . 
BA 6 HOH 55  755 94  HOH HOH A . 
BA 6 HOH 56  756 95  HOH HOH A . 
BA 6 HOH 57  757 96  HOH HOH A . 
BA 6 HOH 58  758 97  HOH HOH A . 
BA 6 HOH 59  759 98  HOH HOH A . 
BA 6 HOH 60  760 99  HOH HOH A . 
BA 6 HOH 61  761 100 HOH HOH A . 
BA 6 HOH 62  762 101 HOH HOH A . 
BA 6 HOH 63  763 102 HOH HOH A . 
BA 6 HOH 64  764 103 HOH HOH A . 
BA 6 HOH 65  765 104 HOH HOH A . 
BA 6 HOH 66  766 105 HOH HOH A . 
BA 6 HOH 67  767 106 HOH HOH A . 
BA 6 HOH 68  768 107 HOH HOH A . 
BA 6 HOH 69  769 108 HOH HOH A . 
BA 6 HOH 70  770 217 HOH HOH A . 
BA 6 HOH 71  771 218 HOH HOH A . 
BA 6 HOH 72  772 221 HOH HOH A . 
BA 6 HOH 73  773 222 HOH HOH A . 
BA 6 HOH 74  774 223 HOH HOH A . 
BA 6 HOH 75  775 224 HOH HOH A . 
BA 6 HOH 76  776 225 HOH HOH A . 
BA 6 HOH 77  777 226 HOH HOH A . 
BA 6 HOH 78  778 227 HOH HOH A . 
BA 6 HOH 79  779 228 HOH HOH A . 
BA 6 HOH 80  780 229 HOH HOH A . 
BA 6 HOH 81  781 230 HOH HOH A . 
BA 6 HOH 82  782 231 HOH HOH A . 
BA 6 HOH 83  783 232 HOH HOH A . 
BA 6 HOH 84  784 233 HOH HOH A . 
BA 6 HOH 85  785 234 HOH HOH A . 
BA 6 HOH 86  786 235 HOH HOH A . 
BA 6 HOH 87  787 236 HOH HOH A . 
BA 6 HOH 88  788 237 HOH HOH A . 
BA 6 HOH 89  789 272 HOH HOH A . 
BA 6 HOH 90  790 273 HOH HOH A . 
BA 6 HOH 91  791 279 HOH HOH A . 
BA 6 HOH 92  792 281 HOH HOH A . 
BA 6 HOH 93  793 282 HOH HOH A . 
BA 6 HOH 94  794 283 HOH HOH A . 
BA 6 HOH 95  795 284 HOH HOH A . 
BA 6 HOH 96  796 285 HOH HOH A . 
BA 6 HOH 97  797 286 HOH HOH A . 
BA 6 HOH 98  798 287 HOH HOH A . 
BA 6 HOH 99  799 288 HOH HOH A . 
BA 6 HOH 100 800 289 HOH HOH A . 
BA 6 HOH 101 801 290 HOH HOH A . 
BA 6 HOH 102 802 291 HOH HOH A . 
BA 6 HOH 103 803 292 HOH HOH A . 
BA 6 HOH 104 804 293 HOH HOH A . 
BA 6 HOH 105 805 294 HOH HOH A . 
CA 6 HOH 1   701 23  HOH HOH B . 
CA 6 HOH 2   702 24  HOH HOH B . 
CA 6 HOH 3   703 109 HOH HOH B . 
CA 6 HOH 4   704 110 HOH HOH B . 
CA 6 HOH 5   705 111 HOH HOH B . 
CA 6 HOH 6   706 112 HOH HOH B . 
CA 6 HOH 7   707 113 HOH HOH B . 
CA 6 HOH 8   708 114 HOH HOH B . 
CA 6 HOH 9   709 115 HOH HOH B . 
CA 6 HOH 10  710 116 HOH HOH B . 
CA 6 HOH 11  711 117 HOH HOH B . 
CA 6 HOH 12  712 118 HOH HOH B . 
CA 6 HOH 13  713 119 HOH HOH B . 
CA 6 HOH 14  714 120 HOH HOH B . 
CA 6 HOH 15  715 121 HOH HOH B . 
CA 6 HOH 16  716 122 HOH HOH B . 
CA 6 HOH 17  717 123 HOH HOH B . 
CA 6 HOH 18  718 124 HOH HOH B . 
CA 6 HOH 19  719 125 HOH HOH B . 
CA 6 HOH 20  720 126 HOH HOH B . 
CA 6 HOH 21  721 127 HOH HOH B . 
CA 6 HOH 22  722 128 HOH HOH B . 
CA 6 HOH 23  723 129 HOH HOH B . 
CA 6 HOH 24  724 130 HOH HOH B . 
CA 6 HOH 25  725 132 HOH HOH B . 
CA 6 HOH 26  726 133 HOH HOH B . 
CA 6 HOH 27  727 134 HOH HOH B . 
CA 6 HOH 28  728 135 HOH HOH B . 
CA 6 HOH 29  729 136 HOH HOH B . 
CA 6 HOH 30  730 137 HOH HOH B . 
CA 6 HOH 31  731 138 HOH HOH B . 
CA 6 HOH 32  732 139 HOH HOH B . 
CA 6 HOH 33  733 140 HOH HOH B . 
CA 6 HOH 34  734 141 HOH HOH B . 
CA 6 HOH 35  735 142 HOH HOH B . 
CA 6 HOH 36  736 143 HOH HOH B . 
CA 6 HOH 37  737 144 HOH HOH B . 
CA 6 HOH 38  738 145 HOH HOH B . 
CA 6 HOH 39  739 146 HOH HOH B . 
CA 6 HOH 40  740 147 HOH HOH B . 
CA 6 HOH 41  741 148 HOH HOH B . 
CA 6 HOH 42  742 149 HOH HOH B . 
CA 6 HOH 43  743 150 HOH HOH B . 
CA 6 HOH 44  744 238 HOH HOH B . 
CA 6 HOH 45  745 239 HOH HOH B . 
CA 6 HOH 46  746 240 HOH HOH B . 
CA 6 HOH 47  747 241 HOH HOH B . 
CA 6 HOH 48  748 243 HOH HOH B . 
CA 6 HOH 49  749 244 HOH HOH B . 
CA 6 HOH 50  750 245 HOH HOH B . 
CA 6 HOH 51  751 246 HOH HOH B . 
CA 6 HOH 52  752 247 HOH HOH B . 
CA 6 HOH 53  753 248 HOH HOH B . 
CA 6 HOH 54  754 249 HOH HOH B . 
CA 6 HOH 55  755 250 HOH HOH B . 
CA 6 HOH 56  756 275 HOH HOH B . 
CA 6 HOH 57  757 296 HOH HOH B . 
CA 6 HOH 58  758 298 HOH HOH B . 
CA 6 HOH 59  759 299 HOH HOH B . 
CA 6 HOH 60  760 301 HOH HOH B . 
CA 6 HOH 61  761 302 HOH HOH B . 
CA 6 HOH 62  762 303 HOH HOH B . 
CA 6 HOH 63  763 304 HOH HOH B . 
CA 6 HOH 64  764 305 HOH HOH B . 
CA 6 HOH 65  765 308 HOH HOH B . 
CA 6 HOH 66  766 309 HOH HOH B . 
CA 6 HOH 67  767 311 HOH HOH B . 
CA 6 HOH 68  768 312 HOH HOH B . 
CA 6 HOH 69  769 313 HOH HOH B . 
CA 6 HOH 70  770 314 HOH HOH B . 
CA 6 HOH 71  771 315 HOH HOH B . 
DA 6 HOH 1   701 53  HOH HOH C . 
DA 6 HOH 2   702 151 HOH HOH C . 
DA 6 HOH 3   703 152 HOH HOH C . 
DA 6 HOH 4   704 153 HOH HOH C . 
DA 6 HOH 5   705 154 HOH HOH C . 
DA 6 HOH 6   706 155 HOH HOH C . 
DA 6 HOH 7   707 156 HOH HOH C . 
DA 6 HOH 8   708 157 HOH HOH C . 
DA 6 HOH 9   709 158 HOH HOH C . 
DA 6 HOH 10  710 159 HOH HOH C . 
DA 6 HOH 11  711 160 HOH HOH C . 
DA 6 HOH 12  712 161 HOH HOH C . 
DA 6 HOH 13  713 162 HOH HOH C . 
DA 6 HOH 14  714 163 HOH HOH C . 
DA 6 HOH 15  715 164 HOH HOH C . 
DA 6 HOH 16  716 165 HOH HOH C . 
DA 6 HOH 17  717 166 HOH HOH C . 
DA 6 HOH 18  718 167 HOH HOH C . 
DA 6 HOH 19  719 168 HOH HOH C . 
DA 6 HOH 20  720 169 HOH HOH C . 
DA 6 HOH 21  721 170 HOH HOH C . 
DA 6 HOH 22  722 171 HOH HOH C . 
DA 6 HOH 23  723 172 HOH HOH C . 
DA 6 HOH 24  724 173 HOH HOH C . 
DA 6 HOH 25  725 174 HOH HOH C . 
DA 6 HOH 26  726 175 HOH HOH C . 
DA 6 HOH 27  727 176 HOH HOH C . 
DA 6 HOH 28  728 177 HOH HOH C . 
DA 6 HOH 29  729 178 HOH HOH C . 
DA 6 HOH 30  730 179 HOH HOH C . 
DA 6 HOH 31  731 180 HOH HOH C . 
DA 6 HOH 32  732 181 HOH HOH C . 
DA 6 HOH 33  733 182 HOH HOH C . 
DA 6 HOH 34  734 183 HOH HOH C . 
DA 6 HOH 35  735 184 HOH HOH C . 
DA 6 HOH 36  736 185 HOH HOH C . 
DA 6 HOH 37  737 186 HOH HOH C . 
DA 6 HOH 38  738 187 HOH HOH C . 
DA 6 HOH 39  739 188 HOH HOH C . 
DA 6 HOH 40  740 189 HOH HOH C . 
DA 6 HOH 41  741 190 HOH HOH C . 
DA 6 HOH 42  742 191 HOH HOH C . 
DA 6 HOH 43  743 192 HOH HOH C . 
DA 6 HOH 44  744 193 HOH HOH C . 
DA 6 HOH 45  745 194 HOH HOH C . 
DA 6 HOH 46  746 195 HOH HOH C . 
DA 6 HOH 47  747 196 HOH HOH C . 
DA 6 HOH 48  748 219 HOH HOH C . 
DA 6 HOH 49  749 220 HOH HOH C . 
DA 6 HOH 50  750 251 HOH HOH C . 
DA 6 HOH 51  751 252 HOH HOH C . 
DA 6 HOH 52  752 253 HOH HOH C . 
DA 6 HOH 53  753 254 HOH HOH C . 
DA 6 HOH 54  754 255 HOH HOH C . 
DA 6 HOH 55  755 256 HOH HOH C . 
DA 6 HOH 56  756 257 HOH HOH C . 
DA 6 HOH 57  757 258 HOH HOH C . 
DA 6 HOH 58  758 259 HOH HOH C . 
DA 6 HOH 59  759 260 HOH HOH C . 
DA 6 HOH 60  760 261 HOH HOH C . 
DA 6 HOH 61  761 263 HOH HOH C . 
DA 6 HOH 62  762 264 HOH HOH C . 
DA 6 HOH 63  763 265 HOH HOH C . 
DA 6 HOH 64  764 271 HOH HOH C . 
DA 6 HOH 65  765 276 HOH HOH C . 
DA 6 HOH 66  766 316 HOH HOH C . 
DA 6 HOH 67  767 317 HOH HOH C . 
DA 6 HOH 68  768 318 HOH HOH C . 
DA 6 HOH 69  769 319 HOH HOH C . 
DA 6 HOH 70  770 320 HOH HOH C . 
DA 6 HOH 71  771 321 HOH HOH C . 
DA 6 HOH 72  772 322 HOH HOH C . 
EA 6 HOH 1   701 1   HOH HOH D . 
EA 6 HOH 2   702 2   HOH HOH D . 
EA 6 HOH 3   703 4   HOH HOH D . 
EA 6 HOH 4   704 5   HOH HOH D . 
EA 6 HOH 5   705 6   HOH HOH D . 
EA 6 HOH 6   706 7   HOH HOH D . 
EA 6 HOH 7   707 8   HOH HOH D . 
EA 6 HOH 8   708 9   HOH HOH D . 
EA 6 HOH 9   709 10  HOH HOH D . 
EA 6 HOH 10  710 11  HOH HOH D . 
EA 6 HOH 11  711 12  HOH HOH D . 
EA 6 HOH 12  712 13  HOH HOH D . 
EA 6 HOH 13  713 14  HOH HOH D . 
EA 6 HOH 14  714 15  HOH HOH D . 
EA 6 HOH 15  715 16  HOH HOH D . 
EA 6 HOH 16  716 17  HOH HOH D . 
EA 6 HOH 17  717 18  HOH HOH D . 
EA 6 HOH 18  718 19  HOH HOH D . 
EA 6 HOH 19  719 20  HOH HOH D . 
EA 6 HOH 20  720 21  HOH HOH D . 
EA 6 HOH 21  721 22  HOH HOH D . 
EA 6 HOH 22  722 25  HOH HOH D . 
EA 6 HOH 23  723 26  HOH HOH D . 
EA 6 HOH 24  724 27  HOH HOH D . 
EA 6 HOH 25  725 28  HOH HOH D . 
EA 6 HOH 26  726 30  HOH HOH D . 
EA 6 HOH 27  727 31  HOH HOH D . 
EA 6 HOH 28  728 33  HOH HOH D . 
EA 6 HOH 29  729 34  HOH HOH D . 
EA 6 HOH 30  730 35  HOH HOH D . 
EA 6 HOH 31  731 36  HOH HOH D . 
EA 6 HOH 32  732 197 HOH HOH D . 
EA 6 HOH 33  733 198 HOH HOH D . 
EA 6 HOH 34  734 199 HOH HOH D . 
EA 6 HOH 35  735 200 HOH HOH D . 
EA 6 HOH 36  736 201 HOH HOH D . 
EA 6 HOH 37  737 202 HOH HOH D . 
EA 6 HOH 38  738 203 HOH HOH D . 
EA 6 HOH 39  739 204 HOH HOH D . 
EA 6 HOH 40  740 205 HOH HOH D . 
EA 6 HOH 41  741 206 HOH HOH D . 
EA 6 HOH 42  742 207 HOH HOH D . 
EA 6 HOH 43  743 208 HOH HOH D . 
EA 6 HOH 44  744 209 HOH HOH D . 
EA 6 HOH 45  745 210 HOH HOH D . 
EA 6 HOH 46  746 211 HOH HOH D . 
EA 6 HOH 47  747 212 HOH HOH D . 
EA 6 HOH 48  748 213 HOH HOH D . 
EA 6 HOH 49  749 214 HOH HOH D . 
EA 6 HOH 50  750 215 HOH HOH D . 
EA 6 HOH 51  751 216 HOH HOH D . 
EA 6 HOH 52  752 242 HOH HOH D . 
EA 6 HOH 53  753 280 HOH HOH D . 
EA 6 HOH 54  754 300 HOH HOH D . 
EA 6 HOH 55  755 324 HOH HOH D . 
EA 6 HOH 56  756 325 HOH HOH D . 
EA 6 HOH 57  757 329 HOH HOH D . 
EA 6 HOH 58  758 330 HOH HOH D . 
EA 6 HOH 59  759 331 HOH HOH D . 
EA 6 HOH 60  760 332 HOH HOH D . 
# 
