data_5IH7
# 
_entry.id   5IH7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5IH7         
WWPDB D_1000218728 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5IH7 
_pdbx_database_status.recvd_initial_deposition_date   2016-02-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pesaresi, A.' 1 ? 
'Lamba, D.'    2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Acetylcholinesterase of Torpedo californica in complex with the N-methyl-indoxylacetate  hydrolysis products' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Pesaresi, A.' 1 
primary 'Lamba, D.'    2 
# 
_cell.entry_id           5IH7 
_cell.length_a           111.990 
_cell.length_b           111.990 
_cell.length_c           137.050 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              6 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         5IH7 
_symmetry.space_group_name_H-M             'P 31 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
# 
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     nat Acetylcholinesterase                60447.211 1   3.1.1.7 ? ? ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE              221.208   3   ?       ? ? ? 
3 non-polymer syn 1-methyl-1,2-dihydro-3H-indol-3-one 147.174   1   ?       ? ? ? 
4 non-polymer syn 'TETRAETHYLENE GLYCOL'              194.226   1   ?       ? ? ? 
5 non-polymer syn 'ACETATE ION'                       59.044    1   ?       ? ? ? 
6 water       nat water                               18.015    303 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        AChE 
# 
_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       
;DHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGS
EMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGS
QEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEG
RRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILL
GVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVI
CPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGN
PNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNAT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;DHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGS
EMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGS
QEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEG
RRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILL
GVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVI
CPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGN
PNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNAT
;
_entity_poly.pdbx_strand_id                 A 
_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   ASP n 
1 2   HIS n 
1 3   SER n 
1 4   GLU n 
1 5   LEU n 
1 6   LEU n 
1 7   VAL n 
1 8   ASN n 
1 9   THR n 
1 10  LYS n 
1 11  SER n 
1 12  GLY n 
1 13  LYS n 
1 14  VAL n 
1 15  MET n 
1 16  GLY n 
1 17  THR n 
1 18  ARG n 
1 19  VAL n 
1 20  PRO n 
1 21  VAL n 
1 22  LEU n 
1 23  SER n 
1 24  SER n 
1 25  HIS n 
1 26  ILE n 
1 27  SER n 
1 28  ALA n 
1 29  PHE n 
1 30  LEU n 
1 31  GLY n 
1 32  ILE n 
1 33  PRO n 
1 34  PHE n 
1 35  ALA n 
1 36  GLU n 
1 37  PRO n 
1 38  PRO n 
1 39  VAL n 
1 40  GLY n 
1 41  ASN n 
1 42  MET n 
1 43  ARG n 
1 44  PHE n 
1 45  ARG n 
1 46  ARG n 
1 47  PRO n 
1 48  GLU n 
1 49  PRO n 
1 50  LYS n 
1 51  LYS n 
1 52  PRO n 
1 53  TRP n 
1 54  SER n 
1 55  GLY n 
1 56  VAL n 
1 57  TRP n 
1 58  ASN n 
1 59  ALA n 
1 60  SER n 
1 61  THR n 
1 62  TYR n 
1 63  PRO n 
1 64  ASN n 
1 65  ASN n 
1 66  CYS n 
1 67  GLN n 
1 68  GLN n 
1 69  TYR n 
1 70  VAL n 
1 71  ASP n 
1 72  GLU n 
1 73  GLN n 
1 74  PHE n 
1 75  PRO n 
1 76  GLY n 
1 77  PHE n 
1 78  SER n 
1 79  GLY n 
1 80  SER n 
1 81  GLU n 
1 82  MET n 
1 83  TRP n 
1 84  ASN n 
1 85  PRO n 
1 86  ASN n 
1 87  ARG n 
1 88  GLU n 
1 89  MET n 
1 90  SER n 
1 91  GLU n 
1 92  ASP n 
1 93  CYS n 
1 94  LEU n 
1 95  TYR n 
1 96  LEU n 
1 97  ASN n 
1 98  ILE n 
1 99  TRP n 
1 100 VAL n 
1 101 PRO n 
1 102 SER n 
1 103 PRO n 
1 104 ARG n 
1 105 PRO n 
1 106 LYS n 
1 107 SER n 
1 108 THR n 
1 109 THR n 
1 110 VAL n 
1 111 MET n 
1 112 VAL n 
1 113 TRP n 
1 114 ILE n 
1 115 TYR n 
1 116 GLY n 
1 117 GLY n 
1 118 GLY n 
1 119 PHE n 
1 120 TYR n 
1 121 SER n 
1 122 GLY n 
1 123 SER n 
1 124 SER n 
1 125 THR n 
1 126 LEU n 
1 127 ASP n 
1 128 VAL n 
1 129 TYR n 
1 130 ASN n 
1 131 GLY n 
1 132 LYS n 
1 133 TYR n 
1 134 LEU n 
1 135 ALA n 
1 136 TYR n 
1 137 THR n 
1 138 GLU n 
1 139 GLU n 
1 140 VAL n 
1 141 VAL n 
1 142 LEU n 
1 143 VAL n 
1 144 SER n 
1 145 LEU n 
1 146 SER n 
1 147 TYR n 
1 148 ARG n 
1 149 VAL n 
1 150 GLY n 
1 151 ALA n 
1 152 PHE n 
1 153 GLY n 
1 154 PHE n 
1 155 LEU n 
1 156 ALA n 
1 157 LEU n 
1 158 HIS n 
1 159 GLY n 
1 160 SER n 
1 161 GLN n 
1 162 GLU n 
1 163 ALA n 
1 164 PRO n 
1 165 GLY n 
1 166 ASN n 
1 167 VAL n 
1 168 GLY n 
1 169 LEU n 
1 170 LEU n 
1 171 ASP n 
1 172 GLN n 
1 173 ARG n 
1 174 MET n 
1 175 ALA n 
1 176 LEU n 
1 177 GLN n 
1 178 TRP n 
1 179 VAL n 
1 180 HIS n 
1 181 ASP n 
1 182 ASN n 
1 183 ILE n 
1 184 GLN n 
1 185 PHE n 
1 186 PHE n 
1 187 GLY n 
1 188 GLY n 
1 189 ASP n 
1 190 PRO n 
1 191 LYS n 
1 192 THR n 
1 193 VAL n 
1 194 THR n 
1 195 ILE n 
1 196 PHE n 
1 197 GLY n 
1 198 GLU n 
1 199 SER n 
1 200 ALA n 
1 201 GLY n 
1 202 GLY n 
1 203 ALA n 
1 204 SER n 
1 205 VAL n 
1 206 GLY n 
1 207 MET n 
1 208 HIS n 
1 209 ILE n 
1 210 LEU n 
1 211 SER n 
1 212 PRO n 
1 213 GLY n 
1 214 SER n 
1 215 ARG n 
1 216 ASP n 
1 217 LEU n 
1 218 PHE n 
1 219 ARG n 
1 220 ARG n 
1 221 ALA n 
1 222 ILE n 
1 223 LEU n 
1 224 GLN n 
1 225 SER n 
1 226 GLY n 
1 227 SER n 
1 228 PRO n 
1 229 ASN n 
1 230 CYS n 
1 231 PRO n 
1 232 TRP n 
1 233 ALA n 
1 234 SER n 
1 235 VAL n 
1 236 SER n 
1 237 VAL n 
1 238 ALA n 
1 239 GLU n 
1 240 GLY n 
1 241 ARG n 
1 242 ARG n 
1 243 ARG n 
1 244 ALA n 
1 245 VAL n 
1 246 GLU n 
1 247 LEU n 
1 248 GLY n 
1 249 ARG n 
1 250 ASN n 
1 251 LEU n 
1 252 ASN n 
1 253 CYS n 
1 254 ASN n 
1 255 LEU n 
1 256 ASN n 
1 257 SER n 
1 258 ASP n 
1 259 GLU n 
1 260 GLU n 
1 261 LEU n 
1 262 ILE n 
1 263 HIS n 
1 264 CYS n 
1 265 LEU n 
1 266 ARG n 
1 267 GLU n 
1 268 LYS n 
1 269 LYS n 
1 270 PRO n 
1 271 GLN n 
1 272 GLU n 
1 273 LEU n 
1 274 ILE n 
1 275 ASP n 
1 276 VAL n 
1 277 GLU n 
1 278 TRP n 
1 279 ASN n 
1 280 VAL n 
1 281 LEU n 
1 282 PRO n 
1 283 PHE n 
1 284 ASP n 
1 285 SER n 
1 286 ILE n 
1 287 PHE n 
1 288 ARG n 
1 289 PHE n 
1 290 SER n 
1 291 PHE n 
1 292 VAL n 
1 293 PRO n 
1 294 VAL n 
1 295 ILE n 
1 296 ASP n 
1 297 GLY n 
1 298 GLU n 
1 299 PHE n 
1 300 PHE n 
1 301 PRO n 
1 302 THR n 
1 303 SER n 
1 304 LEU n 
1 305 GLU n 
1 306 SER n 
1 307 MET n 
1 308 LEU n 
1 309 ASN n 
1 310 SER n 
1 311 GLY n 
1 312 ASN n 
1 313 PHE n 
1 314 LYS n 
1 315 LYS n 
1 316 THR n 
1 317 GLN n 
1 318 ILE n 
1 319 LEU n 
1 320 LEU n 
1 321 GLY n 
1 322 VAL n 
1 323 ASN n 
1 324 LYS n 
1 325 ASP n 
1 326 GLU n 
1 327 GLY n 
1 328 SER n 
1 329 PHE n 
1 330 PHE n 
1 331 LEU n 
1 332 LEU n 
1 333 TYR n 
1 334 GLY n 
1 335 ALA n 
1 336 PRO n 
1 337 GLY n 
1 338 PHE n 
1 339 SER n 
1 340 LYS n 
1 341 ASP n 
1 342 SER n 
1 343 GLU n 
1 344 SER n 
1 345 LYS n 
1 346 ILE n 
1 347 SER n 
1 348 ARG n 
1 349 GLU n 
1 350 ASP n 
1 351 PHE n 
1 352 MET n 
1 353 SER n 
1 354 GLY n 
1 355 VAL n 
1 356 LYS n 
1 357 LEU n 
1 358 SER n 
1 359 VAL n 
1 360 PRO n 
1 361 HIS n 
1 362 ALA n 
1 363 ASN n 
1 364 ASP n 
1 365 LEU n 
1 366 GLY n 
1 367 LEU n 
1 368 ASP n 
1 369 ALA n 
1 370 VAL n 
1 371 THR n 
1 372 LEU n 
1 373 GLN n 
1 374 TYR n 
1 375 THR n 
1 376 ASP n 
1 377 TRP n 
1 378 MET n 
1 379 ASP n 
1 380 ASP n 
1 381 ASN n 
1 382 ASN n 
1 383 GLY n 
1 384 ILE n 
1 385 LYS n 
1 386 ASN n 
1 387 ARG n 
1 388 ASP n 
1 389 GLY n 
1 390 LEU n 
1 391 ASP n 
1 392 ASP n 
1 393 ILE n 
1 394 VAL n 
1 395 GLY n 
1 396 ASP n 
1 397 HIS n 
1 398 ASN n 
1 399 VAL n 
1 400 ILE n 
1 401 CYS n 
1 402 PRO n 
1 403 LEU n 
1 404 MET n 
1 405 HIS n 
1 406 PHE n 
1 407 VAL n 
1 408 ASN n 
1 409 LYS n 
1 410 TYR n 
1 411 THR n 
1 412 LYS n 
1 413 PHE n 
1 414 GLY n 
1 415 ASN n 
1 416 GLY n 
1 417 THR n 
1 418 TYR n 
1 419 LEU n 
1 420 TYR n 
1 421 PHE n 
1 422 PHE n 
1 423 ASN n 
1 424 HIS n 
1 425 ARG n 
1 426 ALA n 
1 427 SER n 
1 428 ASN n 
1 429 LEU n 
1 430 VAL n 
1 431 TRP n 
1 432 PRO n 
1 433 GLU n 
1 434 TRP n 
1 435 MET n 
1 436 GLY n 
1 437 VAL n 
1 438 ILE n 
1 439 HIS n 
1 440 GLY n 
1 441 TYR n 
1 442 GLU n 
1 443 ILE n 
1 444 GLU n 
1 445 PHE n 
1 446 VAL n 
1 447 PHE n 
1 448 GLY n 
1 449 LEU n 
1 450 PRO n 
1 451 LEU n 
1 452 VAL n 
1 453 LYS n 
1 454 GLU n 
1 455 LEU n 
1 456 ASN n 
1 457 TYR n 
1 458 THR n 
1 459 ALA n 
1 460 GLU n 
1 461 GLU n 
1 462 GLU n 
1 463 ALA n 
1 464 LEU n 
1 465 SER n 
1 466 ARG n 
1 467 ARG n 
1 468 ILE n 
1 469 MET n 
1 470 HIS n 
1 471 TYR n 
1 472 TRP n 
1 473 ALA n 
1 474 THR n 
1 475 PHE n 
1 476 ALA n 
1 477 LYS n 
1 478 THR n 
1 479 GLY n 
1 480 ASN n 
1 481 PRO n 
1 482 ASN n 
1 483 GLU n 
1 484 PRO n 
1 485 HIS n 
1 486 SER n 
1 487 GLN n 
1 488 GLU n 
1 489 SER n 
1 490 LYS n 
1 491 TRP n 
1 492 PRO n 
1 493 LEU n 
1 494 PHE n 
1 495 THR n 
1 496 THR n 
1 497 LYS n 
1 498 GLU n 
1 499 GLN n 
1 500 LYS n 
1 501 PHE n 
1 502 ILE n 
1 503 ASP n 
1 504 LEU n 
1 505 ASN n 
1 506 THR n 
1 507 GLU n 
1 508 PRO n 
1 509 MET n 
1 510 LYS n 
1 511 VAL n 
1 512 HIS n 
1 513 GLN n 
1 514 ARG n 
1 515 LEU n 
1 516 ARG n 
1 517 VAL n 
1 518 GLN n 
1 519 MET n 
1 520 CYS n 
1 521 VAL n 
1 522 PHE n 
1 523 TRP n 
1 524 ASN n 
1 525 GLN n 
1 526 PHE n 
1 527 LEU n 
1 528 PRO n 
1 529 LYS n 
1 530 LEU n 
1 531 LEU n 
1 532 ASN n 
1 533 ALA n 
1 534 THR n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           534 
_entity_src_nat.common_name                'Pacific electric ray' 
_entity_src_nat.pdbx_organism_scientific   'Tetronarce californica' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      7787 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ACES_TETCF 
_struct_ref.pdbx_db_accession          P04058 
_struct_ref.pdbx_db_isoform            P04058-2 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGS
EMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGS
QEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEG
RRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILL
GVNKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHANDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVI
CPLMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYEIEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGN
PNEPHSQESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFLPKLLNAT
;
_struct_ref.pdbx_align_begin           23 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              5IH7 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 534 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P04058 
_struct_ref_seq.db_align_beg                  23 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  556 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       535 
# 
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 
ACT non-polymer         . 'ACETATE ION'                       ? 'C2 H3 O2 -1'    59.044  
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 
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 
OMI non-polymer         . 1-methyl-1,2-dihydro-3H-indol-3-one ? 'C9 H9 N O'      147.174 
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL'              ? 'C8 H18 O5'      194.226 
PHE 'L-peptide linking' y PHENYLALANINE                       ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                             ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                              ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                           ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                          ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                            ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                              ? 'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5IH7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            4.07 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         69.79 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'MES 100mM, pH 6.2, PEG200 30%' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-06-15 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ELETTRA BEAMLINE 5.2R' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.2R 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     5IH7 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             35.410 
_reflns.d_resolution_high            2.4 
_reflns.number_obs                   44595 
_reflns.number_all                   39320 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.078 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.9 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              4.500 
_reflns.pdbx_CC_half                 ? 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.40 
_reflns_shell.d_res_low              2.53 
_reflns_shell.percent_possible_all   99.7 
_reflns_shell.Rmerge_I_obs           0.2730 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    4.9 
_reflns_shell.pdbx_redundancy        4.30 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.pdbx_CC_half           ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 5IH7 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     37298 
_refine.ls_number_reflns_all                     39380 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             35.41 
_refine.ls_d_res_high                            2.40 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_R_factor_obs                          0.172 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.170 
_refine.ls_R_factor_R_free                       0.207 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  1978 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.936 
_refine.B_iso_mean                               37.16 
_refine.aniso_B[1][1]                            1.12000 
_refine.aniso_B[2][2]                            1.12000 
_refine.aniso_B[3][3]                            -3.63000 
_refine.aniso_B[1][2]                            1.12000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  
;HYDROGENS HAVE BEEN ADDED IN THE RIDING
 POSITIONS
;
_refine.pdbx_starting_model                      1EA5 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.206 
_refine.pdbx_overall_ESU_R_Free                  0.178 
_refine.overall_SU_ML                            0.112 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.769 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_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        4263 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         69 
_refine_hist.number_atoms_solvent             303 
_refine_hist.number_atoms_total               4635 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        35.41 
# 
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_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.020  0.019  ? 4452 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.020  ? 4106 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.947  1.958  ? 6045 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.946  3.004  ? 9431 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.561  5.000  ? 533  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       33.232 24.028 ? 211  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       16.786 15.000 ? 706  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       21.613 15.000 ? 24   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.129  0.200  ? 636  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.021  ? 5054 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 1078 'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.147  3.412  ? 2135 'X-RAY DIFFRACTION' ? 
r_mcbond_other               3.128  3.409  ? 2134 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.387  5.102  ? 2667 'X-RAY DIFFRACTION' ? 
r_mcangle_other              4.390  5.105  ? 2668 'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.464  3.915  ? 2317 'X-RAY DIFFRACTION' ? 
r_scbond_other               4.463  3.916  ? 2318 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              6.615  5.697  ? 3379 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       7.982  28.334 ? 5396 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         7.976  28.159 ? 5287 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.40 
_refine_ls_shell.d_res_low                        2.53 
_refine_ls_shell.number_reflns_R_work             2713 
_refine_ls_shell.R_factor_R_work                  0.2230 
_refine_ls_shell.percent_reflns_obs               99.79 
_refine_ls_shell.R_factor_R_free                  0.2820 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             135 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                     5IH7 
_struct.title                        
'Acetylcholinesterase of Torpedo californica in complex with the N-methyl-indoxylacetate hydrolysis products' 
_struct.pdbx_descriptor              'Acetylcholinesterase (E.C.3.1.1.7)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5IH7 
_struct_keywords.text            'Acetylcholinesterase NMIA, hydrolase' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 VAL A 39  ? ARG A 43  ? VAL A 40  ARG A 44  5 ? 5  
HELX_P HELX_P2  AA2 PHE A 77  ? MET A 82  ? PHE A 78  MET A 83  1 ? 6  
HELX_P HELX_P3  AA3 LEU A 126 ? ASN A 130 ? LEU A 127 ASN A 131 5 ? 5  
HELX_P HELX_P4  AA4 GLY A 131 ? GLU A 139 ? GLY A 132 GLU A 140 1 ? 9  
HELX_P HELX_P5  AA5 VAL A 149 ? LEU A 155 ? VAL A 150 LEU A 156 1 ? 7  
HELX_P HELX_P6  AA6 ASN A 166 ? ILE A 183 ? ASN A 167 ILE A 184 1 ? 18 
HELX_P HELX_P7  AA7 GLN A 184 ? PHE A 186 ? GLN A 185 PHE A 187 5 ? 3  
HELX_P HELX_P8  AA8 SER A 199 ? SER A 211 ? SER A 200 SER A 212 1 ? 13 
HELX_P HELX_P9  AA9 SER A 214 ? PHE A 218 ? SER A 215 PHE A 219 5 ? 5  
HELX_P HELX_P10 AB1 VAL A 237 ? LEU A 251 ? VAL A 238 LEU A 252 1 ? 15 
HELX_P HELX_P11 AB2 SER A 257 ? LYS A 268 ? SER A 258 LYS A 269 1 ? 12 
HELX_P HELX_P12 AB3 LYS A 269 ? GLU A 277 ? LYS A 270 GLU A 278 1 ? 9  
HELX_P HELX_P13 AB4 TRP A 278 ? LEU A 281 ? TRP A 279 LEU A 282 5 ? 4  
HELX_P HELX_P14 AB5 SER A 303 ? GLY A 311 ? SER A 304 GLY A 312 1 ? 9  
HELX_P HELX_P15 AB6 GLY A 327 ? ALA A 335 ? GLY A 328 ALA A 336 1 ? 9  
HELX_P HELX_P16 AB7 SER A 347 ? VAL A 359 ? SER A 348 VAL A 360 1 ? 13 
HELX_P HELX_P17 AB8 ASN A 363 ? THR A 375 ? ASN A 364 THR A 376 1 ? 13 
HELX_P HELX_P18 AB9 ASN A 382 ? VAL A 399 ? ASN A 383 VAL A 400 1 ? 18 
HELX_P HELX_P19 AC1 VAL A 399 ? LYS A 412 ? VAL A 400 LYS A 413 1 ? 14 
HELX_P HELX_P20 AC2 PRO A 432 ? GLY A 436 ? PRO A 433 GLY A 437 5 ? 5  
HELX_P HELX_P21 AC3 GLU A 442 ? PHE A 447 ? GLU A 443 PHE A 448 1 ? 6  
HELX_P HELX_P22 AC4 GLY A 448 ? ASN A 456 ? GLY A 449 ASN A 457 5 ? 9  
HELX_P HELX_P23 AC5 THR A 458 ? GLY A 479 ? THR A 459 GLY A 480 1 ? 22 
HELX_P HELX_P24 AC6 ARG A 516 ? GLN A 525 ? ARG A 517 GLN A 526 1 ? 10 
HELX_P HELX_P25 AC7 GLN A 525 ? THR A 534 ? GLN A 526 THR A 535 1 ? 10 
# 
_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 66  SG  ? ? ? 1_555 A CYS 93  SG ? ? A CYS 67  A CYS 94  1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf2 disulf ?    ? A CYS 253 SG  ? ? ? 1_555 A CYS 264 SG ? ? A CYS 254 A CYS 265 1_555 ? ? ? ? ? ? ? 2.020 ? 
disulf3 disulf ?    ? A CYS 401 SG  ? ? ? 1_555 A CYS 520 SG ? ? A CYS 402 A CYS 521 1_555 ? ? ? ? ? ? ? 2.054 ? 
covale1 covale one  ? A ASN 58  ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 59  A NAG 601 1_555 ? ? ? ? ? ? ? 1.316 ? 
covale2 covale one  ? A ASN 415 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 416 A NAG 602 1_555 ? ? ? ? ? ? ? 1.471 ? 
covale3 covale both ? C NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? A NAG 602 A NAG 603 1_555 ? ? ? ? ? ? ? 1.439 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           102 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            103 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    103 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     104 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       5.17 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3  ? 
AA2 ? 11 ? 
AA3 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? parallel      
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? parallel      
AA2 5  6  ? parallel      
AA2 6  7  ? parallel      
AA2 7  8  ? parallel      
AA2 8  9  ? parallel      
AA2 9  10 ? parallel      
AA2 10 11 ? anti-parallel 
AA3 1  2  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  LEU A 6   ? THR A 9   ? LEU A 7   THR A 10  
AA1 2  GLY A 12  ? MET A 15  ? GLY A 13  MET A 16  
AA1 3  VAL A 56  ? ASN A 58  ? VAL A 57  ASN A 59  
AA2 1  THR A 17  ? PRO A 20  ? THR A 18  PRO A 21  
AA2 2  HIS A 25  ? PRO A 33  ? HIS A 26  PRO A 34  
AA2 3  TYR A 95  ? VAL A 100 ? TYR A 96  VAL A 101 
AA2 4  VAL A 141 ? SER A 144 ? VAL A 142 SER A 145 
AA2 5  THR A 108 ? ILE A 114 ? THR A 109 ILE A 115 
AA2 6  GLY A 188 ? GLU A 198 ? GLY A 189 GLU A 199 
AA2 7  ARG A 220 ? GLN A 224 ? ARG A 221 GLN A 225 
AA2 8  ILE A 318 ? ASN A 323 ? ILE A 319 ASN A 324 
AA2 9  THR A 417 ? PHE A 422 ? THR A 418 PHE A 423 
AA2 10 LYS A 500 ? LEU A 504 ? LYS A 501 LEU A 505 
AA2 11 VAL A 511 ? GLN A 513 ? VAL A 512 GLN A 514 
AA3 1  VAL A 235 ? SER A 236 ? VAL A 236 SER A 237 
AA3 2  VAL A 294 ? ILE A 295 ? VAL A 295 ILE A 296 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N VAL A 7   ? N VAL A 8   O VAL A 14  ? O VAL A 15  
AA1 2  3  N MET A 15  ? N MET A 16  O TRP A 57  ? O TRP A 58  
AA2 1  2  N VAL A 19  ? N VAL A 20  O ILE A 26  ? O ILE A 27  
AA2 2  3  N SER A 27  ? N SER A 28  O VAL A 100 ? O VAL A 101 
AA2 3  4  N ASN A 97  ? N ASN A 98  O SER A 144 ? O SER A 145 
AA2 4  5  O VAL A 143 ? O VAL A 144 N MET A 111 ? N MET A 112 
AA2 5  6  N THR A 108 ? N THR A 109 O ASP A 189 ? O ASP A 190 
AA2 6  7  N ILE A 195 ? N ILE A 196 O ILE A 222 ? O ILE A 223 
AA2 7  8  N LEU A 223 ? N LEU A 224 O LEU A 319 ? O LEU A 320 
AA2 8  9  N VAL A 322 ? N VAL A 323 O PHE A 422 ? O PHE A 423 
AA2 9  10 N PHE A 421 ? N PHE A 422 O LEU A 504 ? O LEU A 505 
AA2 10 11 N PHE A 501 ? N PHE A 502 O HIS A 512 ? O HIS A 513 
AA3 1  2  N VAL A 235 ? N VAL A 236 O ILE A 295 ? O ILE A 296 
# 
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 A OMI 604 ? 8 'binding site for residue OMI A 604'                                                       
AC2 Software A PG4 605 ? 5 'binding site for residue PG4 A 605'                                                       
AC3 Software A ACT 606 ? 6 'binding site for residue ACT A 606'                                                       
AC4 Software A NAG 601 ? 3 'binding site for Mono-Saccharide NAG A 601 bound to ASN A 59'                             
AC5 Software A ASN 416 ? 1 'binding site for Poly-Saccharide residues NAG A 602 through NAG A 603 bound to ASN A 416' 
# 
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 8 TRP A 83  ? TRP A 84  . ? 1_555 ? 
2  AC1 8 GLY A 116 ? GLY A 117 . ? 1_555 ? 
3  AC1 8 GLY A 117 ? GLY A 118 . ? 1_555 ? 
4  AC1 8 GLU A 198 ? GLU A 199 . ? 1_555 ? 
5  AC1 8 HIS A 439 ? HIS A 440 . ? 1_555 ? 
6  AC1 8 PG4 F .   ? PG4 A 605 . ? 1_555 ? 
7  AC1 8 ACT G .   ? ACT A 606 . ? 1_555 ? 
8  AC1 8 HOH H .   ? HOH A 816 . ? 1_555 ? 
9  AC2 5 TYR A 69  ? TYR A 70  . ? 1_555 ? 
10 AC2 5 TYR A 120 ? TYR A 121 . ? 1_555 ? 
11 AC2 5 TRP A 278 ? TRP A 279 . ? 1_555 ? 
12 AC2 5 PHE A 329 ? PHE A 330 . ? 1_555 ? 
13 AC2 5 OMI E .   ? OMI A 604 . ? 1_555 ? 
14 AC3 6 GLY A 117 ? GLY A 118 . ? 1_555 ? 
15 AC3 6 GLY A 118 ? GLY A 119 . ? 1_555 ? 
16 AC3 6 SER A 199 ? SER A 200 . ? 1_555 ? 
17 AC3 6 ALA A 200 ? ALA A 201 . ? 1_555 ? 
18 AC3 6 HIS A 439 ? HIS A 440 . ? 1_555 ? 
19 AC3 6 OMI E .   ? OMI A 604 . ? 1_555 ? 
20 AC4 3 ASN A 58  ? ASN A 59  . ? 1_555 ? 
21 AC4 3 SER A 60  ? SER A 61  . ? 1_555 ? 
22 AC4 3 THR A 61  ? THR A 62  . ? 1_555 ? 
23 AC5 1 ASN A 415 ? ASN A 416 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5IH7 
_atom_sites.fract_transf_matrix[1][1]   0.008929 
_atom_sites.fract_transf_matrix[1][2]   0.005155 
_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]   0.010311 
_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]   0.007297 
_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 
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 1   ? -71.157 12.877 -6.300  0.50 47.71  ? 2    ASP A N   1 
ATOM   2    C CA  . ASP A 1 1   ? -70.329 12.573 -7.495  0.50 50.38  ? 2    ASP A CA  1 
ATOM   3    C C   . ASP A 1 1   ? -70.608 11.132 -7.792  0.50 55.57  ? 2    ASP A C   1 
ATOM   4    O O   . ASP A 1 1   ? -70.815 10.354 -6.861  0.50 56.01  ? 2    ASP A O   1 
ATOM   5    C CB  . ASP A 1 1   ? -68.835 12.778 -7.234  0.50 49.70  ? 2    ASP A CB  1 
ATOM   6    C CG  . ASP A 1 1   ? -67.636 13.529 -7.013  0.10 43.54  ? 2    ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 1   ? -67.758 14.346 -7.949  0.10 42.36  ? 2    ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 1   ? -67.007 13.786 -5.965  0.10 42.36  ? 2    ASP A OD2 1 
ATOM   9    N N   . HIS A 1 2   ? -70.660 10.796 -9.082  0.50 56.64  ? 3    HIS A N   1 
ATOM   10   C CA  . HIS A 1 2   ? -70.993 9.455  -9.514  0.50 55.18  ? 3    HIS A CA  1 
ATOM   11   C C   . HIS A 1 2   ? -69.847 8.731  -10.287 0.50 57.45  ? 3    HIS A C   1 
ATOM   12   O O   . HIS A 1 2   ? -69.573 7.579  -9.974  0.50 59.86  ? 3    HIS A O   1 
ATOM   13   C CB  . HIS A 1 2   ? -72.315 9.485  -10.293 0.50 51.02  ? 3    HIS A CB  1 
ATOM   14   C CG  . HIS A 1 2   ? -73.396 9.713  -9.809  0.10 41.92  ? 3    HIS A CG  1 
ATOM   15   N ND1 . HIS A 1 2   ? -74.042 8.605  -9.299  0.10 40.71  ? 3    HIS A ND1 1 
ATOM   16   C CD2 . HIS A 1 2   ? -74.209 10.767 -9.560  0.10 40.71  ? 3    HIS A CD2 1 
ATOM   17   C CE1 . HIS A 1 2   ? -75.184 8.978  -8.749  0.10 40.25  ? 3    HIS A CE1 1 
ATOM   18   N NE2 . HIS A 1 2   ? -75.307 10.285 -8.894  0.10 40.25  ? 3    HIS A NE2 1 
ATOM   19   N N   . SER A 1 3   ? -69.165 9.389  -11.246 1.00 63.85  ? 4    SER A N   1 
ATOM   20   C CA  . SER A 1 3   ? -68.120 8.728  -12.129 1.00 57.10  ? 4    SER A CA  1 
ATOM   21   C C   . SER A 1 3   ? -67.079 9.650  -12.821 1.00 51.08  ? 4    SER A C   1 
ATOM   22   O O   . SER A 1 3   ? -67.274 10.860 -12.903 1.00 46.19  ? 4    SER A O   1 
ATOM   23   C CB  . SER A 1 3   ? -68.802 7.941  -13.264 1.00 57.47  ? 4    SER A CB  1 
ATOM   24   O OG  . SER A 1 3   ? -69.054 8.780  -14.395 1.00 54.81  ? 4    SER A OG  1 
ATOM   25   N N   . GLU A 1 4   ? -66.043 9.041  -13.416 1.00 45.36  ? 5    GLU A N   1 
ATOM   26   C CA  . GLU A 1 4   ? -64.864 9.750  -13.967 1.00 43.68  ? 5    GLU A CA  1 
ATOM   27   C C   . GLU A 1 4   ? -65.097 10.807 -15.061 1.00 41.42  ? 5    GLU A C   1 
ATOM   28   O O   . GLU A 1 4   ? -64.282 11.689 -15.247 1.00 41.34  ? 5    GLU A O   1 
ATOM   29   C CB  . GLU A 1 4   ? -63.909 8.737  -14.564 1.00 45.63  ? 5    GLU A CB  1 
ATOM   30   C CG  . GLU A 1 4   ? -62.568 9.333  -15.007 1.00 47.97  ? 5    GLU A CG  1 
ATOM   31   C CD  . GLU A 1 4   ? -61.484 8.289  -15.075 1.00 45.87  ? 5    GLU A CD  1 
ATOM   32   O OE1 . GLU A 1 4   ? -61.853 7.118  -15.094 1.00 51.69  ? 5    GLU A OE1 1 
ATOM   33   O OE2 . GLU A 1 4   ? -60.283 8.616  -15.054 1.00 49.31  ? 5    GLU A OE2 1 
ATOM   34   N N   . LEU A 1 5   ? -66.187 10.650 -15.779 1.00 39.47  ? 6    LEU A N   1 
ATOM   35   C CA  . LEU A 1 5   ? -66.577 11.398 -16.924 1.00 40.70  ? 6    LEU A CA  1 
ATOM   36   C C   . LEU A 1 5   ? -67.642 12.416 -16.551 1.00 38.06  ? 6    LEU A C   1 
ATOM   37   O O   . LEU A 1 5   ? -68.127 13.194 -17.393 1.00 39.56  ? 6    LEU A O   1 
ATOM   38   C CB  . LEU A 1 5   ? -67.159 10.436 -17.990 1.00 37.24  ? 6    LEU A CB  1 
ATOM   39   C CG  . LEU A 1 5   ? -66.217 9.411  -18.640 1.00 40.96  ? 6    LEU A CG  1 
ATOM   40   C CD1 . LEU A 1 5   ? -67.005 8.514  -19.666 1.00 40.77  ? 6    LEU A CD1 1 
ATOM   41   C CD2 . LEU A 1 5   ? -65.018 10.063 -19.318 1.00 41.79  ? 6    LEU A CD2 1 
ATOM   42   N N   . LEU A 1 6   ? -68.038 12.423 -15.304 1.00 37.30  ? 7    LEU A N   1 
ATOM   43   C CA  . LEU A 1 6   ? -68.984 13.432 -14.861 1.00 40.38  ? 7    LEU A CA  1 
ATOM   44   C C   . LEU A 1 6   ? -68.236 14.457 -13.983 1.00 39.48  ? 7    LEU A C   1 
ATOM   45   O O   . LEU A 1 6   ? -67.493 14.101 -13.040 1.00 37.17  ? 7    LEU A O   1 
ATOM   46   C CB  . LEU A 1 6   ? -70.132 12.766 -14.137 1.00 48.36  ? 7    LEU A CB  1 
ATOM   47   C CG  . LEU A 1 6   ? -71.273 13.667 -13.639 1.00 57.88  ? 7    LEU A CG  1 
ATOM   48   C CD1 . LEU A 1 6   ? -71.941 14.413 -14.787 1.00 63.46  ? 7    LEU A CD1 1 
ATOM   49   C CD2 . LEU A 1 6   ? -72.308 12.815 -12.890 1.00 61.44  ? 7    LEU A CD2 1 
ATOM   50   N N   . VAL A 1 7   ? -68.327 15.733 -14.353 1.00 39.98  ? 8    VAL A N   1 
ATOM   51   C CA  . VAL A 1 7   ? -67.655 16.782 -13.557 1.00 35.03  ? 8    VAL A CA  1 
ATOM   52   C C   . VAL A 1 7   ? -68.693 17.823 -13.294 1.00 33.75  ? 8    VAL A C   1 
ATOM   53   O O   . VAL A 1 7   ? -69.483 18.169 -14.158 1.00 37.14  ? 8    VAL A O   1 
ATOM   54   C CB  . VAL A 1 7   ? -66.432 17.344 -14.267 1.00 35.48  ? 8    VAL A CB  1 
ATOM   55   C CG1 . VAL A 1 7   ? -65.869 18.569 -13.545 1.00 35.22  ? 8    VAL A CG1 1 
ATOM   56   C CG2 . VAL A 1 7   ? -65.384 16.264 -14.433 1.00 35.33  ? 8    VAL A CG2 1 
ATOM   57   N N   . ASN A 1 8   ? -68.754 18.252 -12.049 1.00 38.55  ? 9    ASN A N   1 
ATOM   58   C CA  . ASN A 1 8   ? -69.683 19.305 -11.664 1.00 38.96  ? 9    ASN A CA  1 
ATOM   59   C C   . ASN A 1 8   ? -68.874 20.586 -11.604 1.00 33.70  ? 9    ASN A C   1 
ATOM   60   O O   . ASN A 1 8   ? -67.812 20.596 -11.017 1.00 38.91  ? 9    ASN A O   1 
ATOM   61   C CB  . ASN A 1 8   ? -70.371 18.982 -10.330 1.00 43.25  ? 9    ASN A CB  1 
ATOM   62   C CG  . ASN A 1 8   ? -71.442 19.997 -9.987  1.00 54.90  ? 9    ASN A CG  1 
ATOM   63   O OD1 . ASN A 1 8   ? -72.083 20.617 -10.875 1.00 53.19  ? 9    ASN A OD1 1 
ATOM   64   N ND2 . ASN A 1 8   ? -71.619 20.219 -8.696  1.00 62.83  ? 9    ASN A ND2 1 
ATOM   65   N N   . THR A 1 9   ? -69.329 21.618 -12.310 1.00 31.12  ? 10   THR A N   1 
ATOM   66   C CA  . THR A 1 9   ? -68.647 22.860 -12.371 1.00 35.38  ? 10   THR A CA  1 
ATOM   67   C C   . THR A 1 9   ? -69.602 23.893 -11.856 1.00 33.31  ? 10   THR A C   1 
ATOM   68   O O   . THR A 1 9   ? -70.769 23.623 -11.752 1.00 31.47  ? 10   THR A O   1 
ATOM   69   C CB  . THR A 1 9   ? -68.211 23.262 -13.845 1.00 33.19  ? 10   THR A CB  1 
ATOM   70   O OG1 . THR A 1 9   ? -69.317 23.774 -14.576 1.00 29.38  ? 10   THR A OG1 1 
ATOM   71   C CG2 . THR A 1 9   ? -67.602 22.131 -14.582 1.00 34.20  ? 10   THR A CG2 1 
ATOM   72   N N   . LYS A 1 10  ? -69.099 25.115 -11.710 1.00 35.84  ? 11   LYS A N   1 
ATOM   73   C CA  . LYS A 1 10  ? -69.899 26.296 -11.331 1.00 34.39  ? 11   LYS A CA  1 
ATOM   74   C C   . LYS A 1 10  ? -70.911 26.661 -12.387 1.00 35.70  ? 11   LYS A C   1 
ATOM   75   O O   . LYS A 1 10  ? -71.851 27.414 -12.141 1.00 37.57  ? 11   LYS A O   1 
ATOM   76   C CB  . LYS A 1 10  ? -68.922 27.472 -11.077 1.00 35.05  ? 11   LYS A CB  1 
ATOM   77   C CG  . LYS A 1 10  ? -67.843 27.116 -9.994  1.00 34.05  ? 11   LYS A CG  1 
ATOM   78   C CD  . LYS A 1 10  ? -66.838 28.258 -9.715  1.00 34.29  ? 11   LYS A CD  1 
ATOM   79   C CE  . LYS A 1 10  ? -65.850 27.912 -8.596  1.00 33.60  ? 11   LYS A CE  1 
ATOM   80   N NZ  . LYS A 1 10  ? -64.738 28.909 -8.529  1.00 39.49  ? 11   LYS A NZ  1 
ATOM   81   N N   . SER A 1 11  ? -70.747 26.134 -13.595 1.00 37.89  ? 12   SER A N   1 
ATOM   82   C CA  . SER A 1 11  ? -71.706 26.464 -14.654 1.00 38.91  ? 12   SER A CA  1 
ATOM   83   C C   . SER A 1 11  ? -72.754 25.357 -14.771 1.00 36.17  ? 12   SER A C   1 
ATOM   84   O O   . SER A 1 11  ? -73.848 25.545 -15.385 1.00 35.16  ? 12   SER A O   1 
ATOM   85   C CB  . SER A 1 11  ? -70.954 26.731 -15.974 1.00 44.83  ? 12   SER A CB  1 
ATOM   86   O OG  . SER A 1 11  ? -70.065 27.839 -15.820 1.00 44.07  ? 12   SER A OG  1 
ATOM   87   N N   . GLY A 1 12  ? -72.440 24.223 -14.141 1.00 35.52  ? 13   GLY A N   1 
ATOM   88   C CA  . GLY A 1 12  ? -73.305 23.058 -14.163 1.00 34.47  ? 13   GLY A CA  1 
ATOM   89   C C   . GLY A 1 12  ? -72.513 21.801 -14.380 1.00 35.63  ? 13   GLY A C   1 
ATOM   90   O O   . GLY A 1 12  ? -71.267 21.840 -14.408 1.00 38.12  ? 13   GLY A O   1 
ATOM   91   N N   . LYS A 1 13  ? -73.230 20.681 -14.510 1.00 37.81  ? 14   LYS A N   1 
ATOM   92   C CA  . LYS A 1 13  ? -72.593 19.389 -14.675 1.00 41.77  ? 14   LYS A CA  1 
ATOM   93   C C   . LYS A 1 13  ? -72.245 19.161 -16.137 1.00 39.53  ? 14   LYS A C   1 
ATOM   94   O O   . LYS A 1 13  ? -72.910 19.646 -17.046 1.00 36.83  ? 14   LYS A O   1 
ATOM   95   C CB  . LYS A 1 13  ? -73.506 18.280 -14.173 1.00 47.03  ? 14   LYS A CB  1 
ATOM   96   C CG  . LYS A 1 13  ? -73.198 17.848 -12.727 1.00 57.79  ? 14   LYS A CG  1 
ATOM   97   C CD  . LYS A 1 13  ? -74.269 16.974 -12.050 1.00 59.22  ? 14   LYS A CD  1 
ATOM   98   C CE  . LYS A 1 13  ? -75.604 17.733 -11.975 1.00 66.66  ? 14   LYS A CE  1 
ATOM   99   N NZ  . LYS A 1 13  ? -76.452 17.439 -10.771 1.00 66.07  ? 14   LYS A NZ  1 
ATOM   100  N N   . VAL A 1 14  ? -71.247 18.355 -16.364 1.00 34.39  ? 15   VAL A N   1 
ATOM   101  C CA  . VAL A 1 14  ? -70.760 18.157 -17.690 1.00 38.02  ? 15   VAL A CA  1 
ATOM   102  C C   . VAL A 1 14  ? -70.432 16.698 -17.851 1.00 35.21  ? 15   VAL A C   1 
ATOM   103  O O   . VAL A 1 14  ? -69.840 16.113 -16.941 1.00 31.32  ? 15   VAL A O   1 
ATOM   104  C CB  . VAL A 1 14  ? -69.491 19.054 -17.810 1.00 42.20  ? 15   VAL A CB  1 
ATOM   105  C CG1 . VAL A 1 14  ? -68.273 18.311 -18.272 1.00 47.82  ? 15   VAL A CG1 1 
ATOM   106  C CG2 . VAL A 1 14  ? -69.782 20.274 -18.612 1.00 41.24  ? 15   VAL A CG2 1 
ATOM   107  N N   . MET A 1 15  ? -70.805 16.097 -18.984 1.00 35.32  ? 16   MET A N   1 
ATOM   108  C CA  . MET A 1 15  ? -70.472 14.674 -19.230 1.00 36.56  ? 16   MET A CA  1 
ATOM   109  C C   . MET A 1 15  ? -69.475 14.472 -20.364 1.00 34.61  ? 16   MET A C   1 
ATOM   110  O O   . MET A 1 15  ? -69.698 14.856 -21.524 1.00 35.59  ? 16   MET A O   1 
ATOM   111  C CB  . MET A 1 15  ? -71.743 13.839 -19.461 1.00 43.94  ? 16   MET A CB  1 
ATOM   112  C CG  . MET A 1 15  ? -71.521 12.334 -19.779 1.00 50.74  ? 16   MET A CG  1 
ATOM   113  S SD  . MET A 1 15  ? -70.963 11.296 -18.398 1.00 62.21  ? 16   MET A SD  1 
ATOM   114  C CE  . MET A 1 15  ? -72.602 11.071 -17.652 1.00 67.54  ? 16   MET A CE  1 
ATOM   115  N N   . GLY A 1 16  ? -68.362 13.859 -20.033 1.00 32.89  ? 17   GLY A N   1 
ATOM   116  C CA  . GLY A 1 16  ? -67.330 13.655 -21.023 1.00 37.59  ? 17   GLY A CA  1 
ATOM   117  C C   . GLY A 1 16  ? -67.496 12.362 -21.788 1.00 38.37  ? 17   GLY A C   1 
ATOM   118  O O   . GLY A 1 16  ? -68.552 11.759 -21.749 1.00 41.08  ? 17   GLY A O   1 
ATOM   119  N N   . THR A 1 17  ? -66.409 11.941 -22.436 1.00 39.95  ? 18   THR A N   1 
ATOM   120  C CA  . THR A 1 17  ? -66.342 10.730 -23.218 1.00 36.64  ? 18   THR A CA  1 
ATOM   121  C C   . THR A 1 17  ? -64.972 10.206 -23.065 1.00 35.67  ? 18   THR A C   1 
ATOM   122  O O   . THR A 1 17  ? -64.069 10.988 -22.901 1.00 38.49  ? 18   THR A O   1 
ATOM   123  C CB  . THR A 1 17  ? -66.595 10.957 -24.707 1.00 38.86  ? 18   THR A CB  1 
ATOM   124  O OG1 . THR A 1 17  ? -66.567 9.689  -25.335 1.00 39.19  ? 18   THR A OG1 1 
ATOM   125  C CG2 . THR A 1 17  ? -65.487 11.807 -25.399 1.00 39.78  ? 18   THR A CG2 1 
ATOM   126  N N   . ARG A 1 18  ? -64.838 8.887  -23.010 1.00 36.83  ? 19   ARG A N   1 
ATOM   127  C CA  . ARG A 1 18  ? -63.536 8.199  -22.833 1.00 39.85  ? 19   ARG A CA  1 
ATOM   128  C C   . ARG A 1 18  ? -62.957 8.014  -24.235 1.00 43.84  ? 19   ARG A C   1 
ATOM   129  O O   . ARG A 1 18  ? -63.694 7.734  -25.182 1.00 43.54  ? 19   ARG A O   1 
ATOM   130  C CB  . ARG A 1 18  ? -63.743 6.840  -22.183 1.00 38.35  ? 19   ARG A CB  1 
ATOM   131  C CG  . ARG A 1 18  ? -62.487 6.092  -21.848 1.00 43.76  ? 19   ARG A CG  1 
ATOM   132  C CD  . ARG A 1 18  ? -62.672 5.231  -20.559 1.00 48.57  ? 19   ARG A CD  1 
ATOM   133  N NE  . ARG A 1 18  ? -61.503 4.344  -20.287 1.00 52.80  ? 19   ARG A NE  1 
ATOM   134  C CZ  . ARG A 1 18  ? -60.407 4.646  -19.571 1.00 56.73  ? 19   ARG A CZ  1 
ATOM   135  N NH1 . ARG A 1 18  ? -60.240 5.847  -19.006 1.00 65.55  ? 19   ARG A NH1 1 
ATOM   136  N NH2 . ARG A 1 18  ? -59.434 3.743  -19.448 1.00 55.19  ? 19   ARG A NH2 1 
ATOM   137  N N   . VAL A 1 19  ? -61.659 8.217  -24.388 1.00 41.36  ? 20   VAL A N   1 
ATOM   138  C CA  . VAL A 1 19  ? -61.105 8.366  -25.680 1.00 38.10  ? 20   VAL A CA  1 
ATOM   139  C C   . VAL A 1 19  ? -59.852 7.578  -25.664 1.00 36.07  ? 20   VAL A C   1 
ATOM   140  O O   . VAL A 1 19  ? -59.154 7.643  -24.694 1.00 38.70  ? 20   VAL A O   1 
ATOM   141  C CB  . VAL A 1 19  ? -60.775 9.856  -25.921 1.00 45.98  ? 20   VAL A CB  1 
ATOM   142  C CG1 . VAL A 1 19  ? -59.713 10.050 -26.957 1.00 48.79  ? 20   VAL A CG1 1 
ATOM   143  C CG2 . VAL A 1 19  ? -62.012 10.585 -26.353 1.00 47.85  ? 20   VAL A CG2 1 
ATOM   144  N N   . PRO A 1 20  ? -59.558 6.844  -26.751 1.00 35.56  ? 21   PRO A N   1 
ATOM   145  C CA  . PRO A 1 20  ? -58.320 6.011  -26.814 1.00 38.91  ? 21   PRO A CA  1 
ATOM   146  C C   . PRO A 1 20  ? -57.217 6.862  -27.332 1.00 38.92  ? 21   PRO A C   1 
ATOM   147  O O   . PRO A 1 20  ? -57.524 7.818  -28.089 1.00 39.35  ? 21   PRO A O   1 
ATOM   148  C CB  . PRO A 1 20  ? -58.668 4.913  -27.868 1.00 39.65  ? 21   PRO A CB  1 
ATOM   149  C CG  . PRO A 1 20  ? -59.712 5.604  -28.738 1.00 40.66  ? 21   PRO A CG  1 
ATOM   150  C CD  . PRO A 1 20  ? -60.516 6.511  -27.832 1.00 35.40  ? 21   PRO A CD  1 
ATOM   151  N N   . VAL A 1 21  ? -55.984 6.513  -26.950 1.00 33.90  ? 22   VAL A N   1 
ATOM   152  C CA  . VAL A 1 21  ? -54.800 7.282  -27.203 1.00 40.18  ? 22   VAL A CA  1 
ATOM   153  C C   . VAL A 1 21  ? -53.609 6.365  -27.075 1.00 41.51  ? 22   VAL A C   1 
ATOM   154  O O   . VAL A 1 21  ? -53.357 5.902  -25.966 1.00 41.05  ? 22   VAL A O   1 
ATOM   155  C CB  . VAL A 1 21  ? -54.490 8.346  -26.084 1.00 41.98  ? 22   VAL A CB  1 
ATOM   156  C CG1 . VAL A 1 21  ? -53.351 9.253  -26.526 1.00 36.78  ? 22   VAL A CG1 1 
ATOM   157  C CG2 . VAL A 1 21  ? -55.702 9.128  -25.720 1.00 51.33  ? 22   VAL A CG2 1 
ATOM   158  N N   . LEU A 1 22  ? -52.841 6.143  -28.148 1.00 47.20  ? 23   LEU A N   1 
ATOM   159  C CA  . LEU A 1 22  ? -51.616 5.341  -28.027 1.00 45.09  ? 23   LEU A CA  1 
ATOM   160  C C   . LEU A 1 22  ? -51.723 4.025  -27.141 1.00 45.67  ? 23   LEU A C   1 
ATOM   161  O O   . LEU A 1 22  ? -50.883 3.788  -26.245 1.00 42.12  ? 23   LEU A O   1 
ATOM   162  C CB  . LEU A 1 22  ? -50.543 6.247  -27.447 1.00 46.50  ? 23   LEU A CB  1 
ATOM   163  C CG  . LEU A 1 22  ? -50.156 7.464  -28.262 1.00 48.43  ? 23   LEU A CG  1 
ATOM   164  C CD1 . LEU A 1 22  ? -49.045 8.190  -27.554 1.00 48.54  ? 23   LEU A CD1 1 
ATOM   165  C CD2 . LEU A 1 22  ? -49.673 7.044  -29.648 1.00 51.40  ? 23   LEU A CD2 1 
ATOM   166  N N   . SER A 1 23  ? -52.764 3.219  -27.378 1.00 45.03  ? 24   SER A N   1 
ATOM   167  C CA  . SER A 1 23  ? -52.984 1.943  -26.631 1.00 57.00  ? 24   SER A CA  1 
ATOM   168  C C   . SER A 1 23  ? -53.305 2.183  -25.169 1.00 54.37  ? 24   SER A C   1 
ATOM   169  O O   . SER A 1 23  ? -52.787 1.511  -24.294 1.00 63.12  ? 24   SER A O   1 
ATOM   170  C CB  . SER A 1 23  ? -51.737 1.036  -26.675 1.00 56.69  ? 24   SER A CB  1 
ATOM   171  O OG  . SER A 1 23  ? -51.288 0.845  -27.998 1.00 69.74  ? 24   SER A OG  1 
ATOM   172  N N   . SER A 1 24  ? -54.092 3.199  -24.905 1.00 51.47  ? 25   SER A N   1 
ATOM   173  C CA  . SER A 1 24  ? -54.493 3.526  -23.551 1.00 42.91  ? 25   SER A CA  1 
ATOM   174  C C   . SER A 1 24  ? -55.689 4.402  -23.750 1.00 39.16  ? 25   SER A C   1 
ATOM   175  O O   . SER A 1 24  ? -56.292 4.390  -24.862 1.00 38.35  ? 25   SER A O   1 
ATOM   176  C CB  . SER A 1 24  ? -53.354 4.177  -22.769 1.00 43.37  ? 25   SER A CB  1 
ATOM   177  O OG  . SER A 1 24  ? -53.703 4.371  -21.409 1.00 47.30  ? 25   SER A OG  1 
ATOM   178  N N   . HIS A 1 25  ? -56.111 5.127  -22.732 1.00 39.45  ? 26   HIS A N   1 
ATOM   179  C CA  . HIS A 1 25  ? -57.336 5.892  -22.801 1.00 36.25  ? 26   HIS A CA  1 
ATOM   180  C C   . HIS A 1 25  ? -57.257 7.082  -21.882 1.00 40.20  ? 26   HIS A C   1 
ATOM   181  O O   . HIS A 1 25  ? -56.564 7.031  -20.928 1.00 40.65  ? 26   HIS A O   1 
ATOM   182  C CB  . HIS A 1 25  ? -58.498 5.037  -22.338 1.00 46.96  ? 26   HIS A CB  1 
ATOM   183  C CG  . HIS A 1 25  ? -58.922 3.985  -23.311 1.00 58.07  ? 26   HIS A CG  1 
ATOM   184  N ND1 . HIS A 1 25  ? -58.283 2.774  -23.423 1.00 61.35  ? 26   HIS A ND1 1 
ATOM   185  C CD2 . HIS A 1 25  ? -59.941 3.949  -24.193 1.00 64.74  ? 26   HIS A CD2 1 
ATOM   186  C CE1 . HIS A 1 25  ? -58.869 2.051  -24.351 1.00 66.75  ? 26   HIS A CE1 1 
ATOM   187  N NE2 . HIS A 1 25  ? -59.882 2.740  -24.829 1.00 68.46  ? 26   HIS A NE2 1 
ATOM   188  N N   . ILE A 1 26  ? -57.990 8.148  -22.171 1.00 41.65  ? 27   ILE A N   1 
ATOM   189  C CA  . ILE A 1 26  ? -58.160 9.277  -21.256 1.00 38.35  ? 27   ILE A CA  1 
ATOM   190  C C   . ILE A 1 26  ? -59.535 9.839  -21.386 1.00 34.63  ? 27   ILE A C   1 
ATOM   191  O O   . ILE A 1 26  ? -60.335 9.292  -22.146 1.00 35.77  ? 27   ILE A O   1 
ATOM   192  C CB  . ILE A 1 26  ? -57.121 10.396 -21.433 1.00 42.14  ? 27   ILE A CB  1 
ATOM   193  C CG1 . ILE A 1 26  ? -57.255 11.057 -22.778 1.00 42.95  ? 27   ILE A CG1 1 
ATOM   194  C CG2 . ILE A 1 26  ? -55.690 9.873  -21.225 1.00 41.60  ? 27   ILE A CG2 1 
ATOM   195  C CD1 . ILE A 1 26  ? -56.450 12.319 -22.772 1.00 49.02  ? 27   ILE A CD1 1 
ATOM   196  N N   . SER A 1 27  ? -59.823 10.909 -20.653 1.00 32.48  ? 28   SER A N   1 
ATOM   197  C CA  . SER A 1 27  ? -61.140 11.531 -20.685 1.00 31.64  ? 28   SER A CA  1 
ATOM   198  C C   . SER A 1 27  ? -61.109 12.846 -21.455 1.00 33.48  ? 28   SER A C   1 
ATOM   199  O O   . SER A 1 27  ? -60.162 13.624 -21.339 1.00 35.03  ? 28   SER A O   1 
ATOM   200  C CB  . SER A 1 27  ? -61.656 11.766 -19.264 1.00 39.30  ? 28   SER A CB  1 
ATOM   201  O OG  . SER A 1 27  ? -61.337 10.675 -18.418 1.00 35.14  ? 28   SER A OG  1 
ATOM   202  N N   . ALA A 1 28  ? -62.152 13.085 -22.241 1.00 33.87  ? 29   ALA A N   1 
ATOM   203  C CA  . ALA A 1 28  ? -62.251 14.264 -23.012 1.00 35.81  ? 29   ALA A CA  1 
ATOM   204  C C   . ALA A 1 28  ? -63.593 14.922 -22.797 1.00 35.58  ? 29   ALA A C   1 
ATOM   205  O O   . ALA A 1 28  ? -64.629 14.266 -22.809 1.00 40.12  ? 29   ALA A O   1 
ATOM   206  C CB  . ALA A 1 28  ? -62.036 13.948 -24.495 1.00 39.59  ? 29   ALA A CB  1 
ATOM   207  N N   . PHE A 1 29  ? -63.558 16.233 -22.619 1.00 32.33  ? 30   PHE A N   1 
ATOM   208  C CA  . PHE A 1 29  ? -64.749 16.998 -22.404 1.00 34.80  ? 30   PHE A CA  1 
ATOM   209  C C   . PHE A 1 29  ? -64.735 18.056 -23.513 1.00 35.86  ? 30   PHE A C   1 
ATOM   210  O O   . PHE A 1 29  ? -64.000 19.048 -23.461 1.00 39.59  ? 30   PHE A O   1 
ATOM   211  C CB  . PHE A 1 29  ? -64.711 17.658 -21.001 1.00 33.43  ? 30   PHE A CB  1 
ATOM   212  C CG  . PHE A 1 29  ? -64.610 16.673 -19.860 1.00 31.47  ? 30   PHE A CG  1 
ATOM   213  C CD1 . PHE A 1 29  ? -63.394 16.153 -19.491 1.00 30.11  ? 30   PHE A CD1 1 
ATOM   214  C CD2 . PHE A 1 29  ? -65.759 16.270 -19.176 1.00 32.78  ? 30   PHE A CD2 1 
ATOM   215  C CE1 . PHE A 1 29  ? -63.299 15.242 -18.449 1.00 37.19  ? 30   PHE A CE1 1 
ATOM   216  C CE2 . PHE A 1 29  ? -65.683 15.374 -18.125 1.00 35.17  ? 30   PHE A CE2 1 
ATOM   217  C CZ  . PHE A 1 29  ? -64.450 14.832 -17.772 1.00 34.25  ? 30   PHE A CZ  1 
ATOM   218  N N   . LEU A 1 30  ? -65.541 17.827 -24.519 1.00 34.30  ? 31   LEU A N   1 
ATOM   219  C CA  . LEU A 1 30  ? -65.442 18.549 -25.743 1.00 35.21  ? 31   LEU A CA  1 
ATOM   220  C C   . LEU A 1 30  ? -66.631 19.419 -25.830 1.00 32.89  ? 31   LEU A C   1 
ATOM   221  O O   . LEU A 1 30  ? -67.734 18.998 -25.475 1.00 34.26  ? 31   LEU A O   1 
ATOM   222  C CB  . LEU A 1 30  ? -65.459 17.555 -26.910 1.00 38.27  ? 31   LEU A CB  1 
ATOM   223  C CG  . LEU A 1 30  ? -64.358 16.485 -26.896 1.00 37.12  ? 31   LEU A CG  1 
ATOM   224  C CD1 . LEU A 1 30  ? -64.518 15.606 -28.138 1.00 36.79  ? 31   LEU A CD1 1 
ATOM   225  C CD2 . LEU A 1 30  ? -62.954 17.061 -26.811 1.00 35.00  ? 31   LEU A CD2 1 
ATOM   226  N N   . GLY A 1 31  ? -66.428 20.650 -26.279 1.00 31.28  ? 32   GLY A N   1 
ATOM   227  C CA  . GLY A 1 31  ? -67.572 21.508 -26.591 1.00 30.39  ? 32   GLY A CA  1 
ATOM   228  C C   . GLY A 1 31  ? -68.273 22.033 -25.342 1.00 34.84  ? 32   GLY A C   1 
ATOM   229  O O   . GLY A 1 31  ? -69.488 22.175 -25.340 1.00 34.51  ? 32   GLY A O   1 
ATOM   230  N N   . ILE A 1 32  ? -67.502 22.395 -24.298 1.00 36.32  ? 33   ILE A N   1 
ATOM   231  C CA  . ILE A 1 32  ? -68.094 23.068 -23.115 1.00 35.34  ? 33   ILE A CA  1 
ATOM   232  C C   . ILE A 1 32  ? -68.269 24.548 -23.409 1.00 32.86  ? 33   ILE A C   1 
ATOM   233  O O   . ILE A 1 32  ? -67.332 25.200 -23.788 1.00 35.47  ? 33   ILE A O   1 
ATOM   234  C CB  . ILE A 1 32  ? -67.206 22.924 -21.852 1.00 33.94  ? 33   ILE A CB  1 
ATOM   235  C CG1 . ILE A 1 32  ? -67.047 21.467 -21.491 1.00 34.56  ? 33   ILE A CG1 1 
ATOM   236  C CG2 . ILE A 1 32  ? -67.848 23.654 -20.678 1.00 36.57  ? 33   ILE A CG2 1 
ATOM   237  C CD1 . ILE A 1 32  ? -65.975 21.198 -20.464 1.00 34.84  ? 33   ILE A CD1 1 
ATOM   238  N N   . PRO A 1 33  ? -69.444 25.107 -23.160 1.00 31.78  ? 34   PRO A N   1 
ATOM   239  C CA  . PRO A 1 33  ? -69.643 26.499 -23.450 1.00 30.41  ? 34   PRO A CA  1 
ATOM   240  C C   . PRO A 1 33  ? -69.129 27.418 -22.330 1.00 32.03  ? 34   PRO A C   1 
ATOM   241  O O   . PRO A 1 33  ? -69.300 27.101 -21.148 1.00 36.59  ? 34   PRO A O   1 
ATOM   242  C CB  . PRO A 1 33  ? -71.155 26.590 -23.564 1.00 31.28  ? 34   PRO A CB  1 
ATOM   243  C CG  . PRO A 1 33  ? -71.659 25.555 -22.663 1.00 28.48  ? 34   PRO A CG  1 
ATOM   244  C CD  . PRO A 1 33  ? -70.689 24.449 -22.740 1.00 31.43  ? 34   PRO A CD  1 
ATOM   245  N N   . PHE A 1 34  ? -68.482 28.521 -22.696 1.00 30.45  ? 35   PHE A N   1 
ATOM   246  C CA  . PHE A 1 34  ? -67.898 29.426 -21.699 1.00 27.47  ? 35   PHE A CA  1 
ATOM   247  C C   . PHE A 1 34  ? -68.438 30.814 -21.826 1.00 28.34  ? 35   PHE A C   1 
ATOM   248  O O   . PHE A 1 34  ? -68.115 31.670 -20.990 1.00 31.44  ? 35   PHE A O   1 
ATOM   249  C CB  . PHE A 1 34  ? -66.351 29.419 -21.719 1.00 32.32  ? 35   PHE A CB  1 
ATOM   250  C CG  . PHE A 1 34  ? -65.741 29.976 -22.994 1.00 31.23  ? 35   PHE A CG  1 
ATOM   251  C CD1 . PHE A 1 34  ? -65.744 31.347 -23.249 1.00 31.44  ? 35   PHE A CD1 1 
ATOM   252  C CD2 . PHE A 1 34  ? -65.266 29.127 -23.980 1.00 30.70  ? 35   PHE A CD2 1 
ATOM   253  C CE1 . PHE A 1 34  ? -65.226 31.856 -24.422 1.00 31.17  ? 35   PHE A CE1 1 
ATOM   254  C CE2 . PHE A 1 34  ? -64.775 29.643 -25.172 1.00 32.31  ? 35   PHE A CE2 1 
ATOM   255  C CZ  . PHE A 1 34  ? -64.731 30.999 -25.379 1.00 31.11  ? 35   PHE A CZ  1 
ATOM   256  N N   . ALA A 1 35  ? -69.324 31.065 -22.799 1.00 27.81  ? 36   ALA A N   1 
ATOM   257  C CA  . ALA A 1 35  ? -69.926 32.371 -22.937 1.00 26.50  ? 36   ALA A CA  1 
ATOM   258  C C   . ALA A 1 35  ? -71.301 32.179 -23.470 1.00 31.10  ? 36   ALA A C   1 
ATOM   259  O O   . ALA A 1 35  ? -71.576 31.156 -24.034 1.00 29.43  ? 36   ALA A O   1 
ATOM   260  C CB  . ALA A 1 35  ? -69.083 33.208 -23.931 1.00 28.12  ? 36   ALA A CB  1 
ATOM   261  N N   . GLU A 1 36  ? -72.173 33.170 -23.357 1.00 32.55  ? 37   GLU A N   1 
ATOM   262  C CA  . GLU A 1 36  ? -73.416 33.119 -24.137 1.00 33.88  ? 37   GLU A CA  1 
ATOM   263  C C   . GLU A 1 36  ? -73.104 33.195 -25.662 1.00 36.28  ? 37   GLU A C   1 
ATOM   264  O O   . GLU A 1 36  ? -72.187 33.914 -26.052 1.00 34.85  ? 37   GLU A O   1 
ATOM   265  C CB  . GLU A 1 36  ? -74.276 34.362 -23.767 1.00 35.36  ? 37   GLU A CB  1 
ATOM   266  C CG  . GLU A 1 36  ? -75.017 34.263 -22.406 1.00 39.37  ? 37   GLU A CG  1 
ATOM   267  C CD  . GLU A 1 36  ? -75.873 33.005 -22.322 1.00 40.60  ? 37   GLU A CD  1 
ATOM   268  O OE1 . GLU A 1 36  ? -76.789 32.944 -23.108 1.00 40.74  ? 37   GLU A OE1 1 
ATOM   269  O OE2 . GLU A 1 36  ? -75.605 32.043 -21.557 1.00 41.93  ? 37   GLU A OE2 1 
ATOM   270  N N   . PRO A 1 37  ? -73.903 32.541 -26.522 1.00 37.03  ? 38   PRO A N   1 
ATOM   271  C CA  . PRO A 1 37  ? -73.790 32.728 -27.971 1.00 34.43  ? 38   PRO A CA  1 
ATOM   272  C C   . PRO A 1 37  ? -73.834 34.182 -28.430 1.00 37.28  ? 38   PRO A C   1 
ATOM   273  O O   . PRO A 1 37  ? -74.811 34.870 -28.211 1.00 39.66  ? 38   PRO A O   1 
ATOM   274  C CB  . PRO A 1 37  ? -75.046 32.000 -28.516 1.00 37.85  ? 38   PRO A CB  1 
ATOM   275  C CG  . PRO A 1 37  ? -75.295 30.906 -27.515 1.00 37.36  ? 38   PRO A CG  1 
ATOM   276  C CD  . PRO A 1 37  ? -74.967 31.556 -26.188 1.00 37.73  ? 38   PRO A CD  1 
ATOM   277  N N   . PRO A 1 38  ? -72.785 34.659 -29.109 1.00 35.93  ? 39   PRO A N   1 
ATOM   278  C CA  . PRO A 1 38  ? -72.750 36.032 -29.481 1.00 35.59  ? 39   PRO A CA  1 
ATOM   279  C C   . PRO A 1 38  ? -73.475 36.312 -30.798 1.00 42.63  ? 39   PRO A C   1 
ATOM   280  O O   . PRO A 1 38  ? -72.862 36.733 -31.792 1.00 40.69  ? 39   PRO A O   1 
ATOM   281  C CB  . PRO A 1 38  ? -71.281 36.299 -29.563 1.00 37.27  ? 39   PRO A CB  1 
ATOM   282  C CG  . PRO A 1 38  ? -70.698 35.002 -29.983 1.00 36.37  ? 39   PRO A CG  1 
ATOM   283  C CD  . PRO A 1 38  ? -71.605 33.934 -29.564 1.00 34.76  ? 39   PRO A CD  1 
ATOM   284  N N   . VAL A 1 39  ? -74.795 36.116 -30.767 1.00 40.89  ? 40   VAL A N   1 
ATOM   285  C CA  . VAL A 1 39  ? -75.605 36.112 -31.962 1.00 36.33  ? 40   VAL A CA  1 
ATOM   286  C C   . VAL A 1 39  ? -76.595 37.256 -31.915 1.00 42.07  ? 40   VAL A C   1 
ATOM   287  O O   . VAL A 1 39  ? -76.764 37.930 -30.902 1.00 42.95  ? 40   VAL A O   1 
ATOM   288  C CB  . VAL A 1 39  ? -76.323 34.785 -32.157 1.00 40.07  ? 40   VAL A CB  1 
ATOM   289  C CG1 . VAL A 1 39  ? -75.311 33.654 -32.244 1.00 41.05  ? 40   VAL A CG1 1 
ATOM   290  C CG2 . VAL A 1 39  ? -77.290 34.506 -31.011 1.00 40.89  ? 40   VAL A CG2 1 
ATOM   291  N N   . GLY A 1 40  ? -77.213 37.496 -33.058 1.00 42.42  ? 41   GLY A N   1 
ATOM   292  C CA  . GLY A 1 40  ? -78.070 38.634 -33.257 1.00 39.80  ? 41   GLY A CA  1 
ATOM   293  C C   . GLY A 1 40  ? -77.443 39.936 -32.838 1.00 41.55  ? 41   GLY A C   1 
ATOM   294  O O   . GLY A 1 40  ? -76.378 40.349 -33.350 1.00 44.99  ? 41   GLY A O   1 
ATOM   295  N N   . ASN A 1 41  ? -78.121 40.593 -31.906 1.00 41.71  ? 42   ASN A N   1 
ATOM   296  C CA  . ASN A 1 41  ? -77.738 41.886 -31.408 1.00 40.31  ? 42   ASN A CA  1 
ATOM   297  C C   . ASN A 1 41  ? -76.470 41.871 -30.578 1.00 35.35  ? 42   ASN A C   1 
ATOM   298  O O   . ASN A 1 41  ? -75.907 42.920 -30.322 1.00 35.88  ? 42   ASN A O   1 
ATOM   299  C CB  . ASN A 1 41  ? -78.899 42.546 -30.679 1.00 53.06  ? 42   ASN A CB  1 
ATOM   300  C CG  . ASN A 1 41  ? -79.845 43.248 -31.662 1.00 74.46  ? 42   ASN A CG  1 
ATOM   301  O OD1 . ASN A 1 41  ? -79.796 43.012 -32.911 1.00 84.81  ? 42   ASN A OD1 1 
ATOM   302  N ND2 . ASN A 1 41  ? -80.683 44.143 -31.128 1.00 76.59  ? 42   ASN A ND2 1 
ATOM   303  N N   . MET A 1 42  ? -76.000 40.703 -30.211 1.00 30.01  ? 43   MET A N   1 
ATOM   304  C CA  . MET A 1 42  ? -74.670 40.576 -29.581 1.00 38.94  ? 43   MET A CA  1 
ATOM   305  C C   . MET A 1 42  ? -73.437 40.391 -30.552 1.00 36.26  ? 43   MET A C   1 
ATOM   306  O O   . MET A 1 42  ? -72.237 40.294 -30.111 1.00 35.04  ? 43   MET A O   1 
ATOM   307  C CB  . MET A 1 42  ? -74.704 39.400 -28.620 1.00 46.15  ? 43   MET A CB  1 
ATOM   308  C CG  . MET A 1 42  ? -75.879 39.451 -27.639 1.00 54.22  ? 43   MET A CG  1 
ATOM   309  S SD  . MET A 1 42  ? -75.424 38.402 -26.248 1.00 73.86  ? 43   MET A SD  1 
ATOM   310  C CE  . MET A 1 42  ? -74.584 39.757 -25.398 1.00 72.53  ? 43   MET A CE  1 
ATOM   311  N N   . ARG A 1 43  ? -73.719 40.356 -31.848 1.00 32.63  ? 44   ARG A N   1 
ATOM   312  C CA  . ARG A 1 43  ? -72.673 40.269 -32.861 1.00 31.81  ? 44   ARG A CA  1 
ATOM   313  C C   . ARG A 1 43  ? -71.859 41.561 -32.700 1.00 31.28  ? 44   ARG A C   1 
ATOM   314  O O   . ARG A 1 43  ? -72.412 42.622 -32.490 1.00 33.97  ? 44   ARG A O   1 
ATOM   315  C CB  . ARG A 1 43  ? -73.249 40.042 -34.288 1.00 33.44  ? 44   ARG A CB  1 
ATOM   316  C CG  . ARG A 1 43  ? -72.173 40.153 -35.363 1.00 37.91  ? 44   ARG A CG  1 
ATOM   317  C CD  . ARG A 1 43  ? -72.697 40.249 -36.779 1.00 33.43  ? 44   ARG A CD  1 
ATOM   318  N NE  . ARG A 1 43  ? -73.173 38.980 -37.274 1.00 32.35  ? 44   ARG A NE  1 
ATOM   319  C CZ  . ARG A 1 43  ? -73.842 38.865 -38.407 1.00 32.50  ? 44   ARG A CZ  1 
ATOM   320  N NH1 . ARG A 1 43  ? -74.069 39.936 -39.175 1.00 31.82  ? 44   ARG A NH1 1 
ATOM   321  N NH2 . ARG A 1 43  ? -74.273 37.667 -38.799 1.00 36.30  ? 44   ARG A NH2 1 
ATOM   322  N N   . PHE A 1 44  ? -70.545 41.403 -32.634 1.00 31.07  ? 45   PHE A N   1 
ATOM   323  C CA  . PHE A 1 44  ? -69.576 42.459 -32.398 1.00 32.33  ? 45   PHE A CA  1 
ATOM   324  C C   . PHE A 1 44  ? -69.443 42.927 -30.980 1.00 32.26  ? 45   PHE A C   1 
ATOM   325  O O   . PHE A 1 44  ? -68.482 43.647 -30.679 1.00 34.22  ? 45   PHE A O   1 
ATOM   326  C CB  . PHE A 1 44  ? -69.788 43.684 -33.294 1.00 34.17  ? 45   PHE A CB  1 
ATOM   327  C CG  . PHE A 1 44  ? -70.038 43.374 -34.746 1.00 38.12  ? 45   PHE A CG  1 
ATOM   328  C CD1 . PHE A 1 44  ? -69.129 42.635 -35.487 1.00 39.45  ? 45   PHE A CD1 1 
ATOM   329  C CD2 . PHE A 1 44  ? -71.180 43.897 -35.396 1.00 44.07  ? 45   PHE A CD2 1 
ATOM   330  C CE1 . PHE A 1 44  ? -69.355 42.394 -36.832 1.00 42.47  ? 45   PHE A CE1 1 
ATOM   331  C CE2 . PHE A 1 44  ? -71.409 43.672 -36.745 1.00 43.75  ? 45   PHE A CE2 1 
ATOM   332  C CZ  . PHE A 1 44  ? -70.491 42.920 -37.464 1.00 45.58  ? 45   PHE A CZ  1 
ATOM   333  N N   . ARG A 1 45  ? -70.346 42.503 -30.104 1.00 36.90  ? 46   ARG A N   1 
ATOM   334  C CA  . ARG A 1 45  ? -70.321 42.906 -28.685 1.00 40.84  ? 46   ARG A CA  1 
ATOM   335  C C   . ARG A 1 45  ? -69.312 42.094 -27.883 1.00 38.00  ? 46   ARG A C   1 
ATOM   336  O O   . ARG A 1 45  ? -68.905 40.985 -28.286 1.00 37.73  ? 46   ARG A O   1 
ATOM   337  C CB  . ARG A 1 45  ? -71.697 42.712 -28.017 1.00 46.56  ? 46   ARG A CB  1 
ATOM   338  C CG  . ARG A 1 45  ? -72.593 43.935 -28.079 1.00 53.78  ? 46   ARG A CG  1 
ATOM   339  C CD  . ARG A 1 45  ? -73.829 43.762 -27.215 1.00 54.93  ? 46   ARG A CD  1 
ATOM   340  N NE  . ARG A 1 45  ? -74.120 44.999 -26.488 1.00 67.64  ? 46   ARG A NE  1 
ATOM   341  C CZ  . ARG A 1 45  ? -73.559 45.361 -25.327 1.00 70.17  ? 46   ARG A CZ  1 
ATOM   342  N NH1 . ARG A 1 45  ? -72.657 44.587 -24.731 1.00 76.12  ? 46   ARG A NH1 1 
ATOM   343  N NH2 . ARG A 1 45  ? -73.891 46.514 -24.755 1.00 72.91  ? 46   ARG A NH2 1 
ATOM   344  N N   . ARG A 1 46  ? -68.910 42.630 -26.734 1.00 33.94  ? 47   ARG A N   1 
ATOM   345  C CA  . ARG A 1 46  ? -68.039 41.901 -25.821 1.00 37.13  ? 47   ARG A CA  1 
ATOM   346  C C   . ARG A 1 46  ? -68.824 40.739 -25.225 1.00 31.16  ? 47   ARG A C   1 
ATOM   347  O O   . ARG A 1 46  ? -69.979 40.904 -24.831 1.00 32.82  ? 47   ARG A O   1 
ATOM   348  C CB  . ARG A 1 46  ? -67.530 42.822 -24.711 1.00 45.63  ? 47   ARG A CB  1 
ATOM   349  C CG  . ARG A 1 46  ? -68.549 43.101 -23.619 1.00 63.23  ? 47   ARG A CG  1 
ATOM   350  C CD  . ARG A 1 46  ? -68.463 44.541 -23.138 1.00 71.23  ? 47   ARG A CD  1 
ATOM   351  N NE  . ARG A 1 46  ? -67.101 45.061 -23.209 1.00 77.51  ? 47   ARG A NE  1 
ATOM   352  C CZ  . ARG A 1 46  ? -66.754 46.161 -23.868 1.00 69.98  ? 47   ARG A CZ  1 
ATOM   353  N NH1 . ARG A 1 46  ? -67.672 46.864 -24.518 1.00 63.88  ? 47   ARG A NH1 1 
ATOM   354  N NH2 . ARG A 1 46  ? -65.490 46.560 -23.879 1.00 58.59  ? 47   ARG A NH2 1 
ATOM   355  N N   . PRO A 1 47  ? -68.208 39.563 -25.168 1.00 31.22  ? 48   PRO A N   1 
ATOM   356  C CA  . PRO A 1 47  ? -68.917 38.382 -24.731 1.00 32.01  ? 48   PRO A CA  1 
ATOM   357  C C   . PRO A 1 47  ? -69.585 38.512 -23.326 1.00 34.66  ? 48   PRO A C   1 
ATOM   358  O O   . PRO A 1 47  ? -69.068 39.231 -22.495 1.00 33.05  ? 48   PRO A O   1 
ATOM   359  C CB  . PRO A 1 47  ? -67.801 37.372 -24.666 1.00 27.51  ? 48   PRO A CB  1 
ATOM   360  C CG  . PRO A 1 47  ? -66.606 38.160 -24.290 1.00 26.76  ? 48   PRO A CG  1 
ATOM   361  C CD  . PRO A 1 47  ? -66.746 39.372 -25.136 1.00 28.50  ? 48   PRO A CD  1 
ATOM   362  N N   . GLU A 1 48  ? -70.713 37.825 -23.121 1.00 40.34  ? 49   GLU A N   1 
ATOM   363  C CA  . GLU A 1 48  ? -71.334 37.628 -21.796 1.00 43.66  ? 49   GLU A CA  1 
ATOM   364  C C   . GLU A 1 48  ? -71.011 36.212 -21.270 1.00 36.40  ? 49   GLU A C   1 
ATOM   365  O O   . GLU A 1 48  ? -70.981 35.254 -22.030 1.00 36.61  ? 49   GLU A O   1 
ATOM   366  C CB  . GLU A 1 48  ? -72.868 37.877 -21.835 1.00 45.76  ? 49   GLU A CB  1 
ATOM   367  C CG  . GLU A 1 48  ? -73.314 39.329 -22.196 1.00 54.89  ? 49   GLU A CG  1 
ATOM   368  C CD  . GLU A 1 48  ? -72.507 40.457 -21.521 1.00 65.56  ? 49   GLU A CD  1 
ATOM   369  O OE1 . GLU A 1 48  ? -72.352 40.442 -20.277 1.00 84.90  ? 49   GLU A OE1 1 
ATOM   370  O OE2 . GLU A 1 48  ? -72.029 41.385 -22.227 1.00 78.15  ? 49   GLU A OE2 1 
ATOM   371  N N   . PRO A 1 49  ? -70.810 36.061 -19.955 1.00 35.74  ? 50   PRO A N   1 
ATOM   372  C CA  . PRO A 1 49  ? -70.548 34.719 -19.419 1.00 36.69  ? 50   PRO A CA  1 
ATOM   373  C C   . PRO A 1 49  ? -71.718 33.789 -19.617 1.00 33.47  ? 50   PRO A C   1 
ATOM   374  O O   . PRO A 1 49  ? -72.861 34.237 -19.647 1.00 30.91  ? 50   PRO A O   1 
ATOM   375  C CB  . PRO A 1 49  ? -70.275 34.965 -17.916 1.00 39.19  ? 50   PRO A CB  1 
ATOM   376  C CG  . PRO A 1 49  ? -70.953 36.249 -17.608 1.00 40.38  ? 50   PRO A CG  1 
ATOM   377  C CD  . PRO A 1 49  ? -70.867 37.082 -18.888 1.00 41.38  ? 50   PRO A CD  1 
ATOM   378  N N   . LYS A 1 50  ? -71.426 32.511 -19.805 1.00 33.90  ? 51   LYS A N   1 
ATOM   379  C CA  . LYS A 1 50  ? -72.470 31.505 -19.995 1.00 39.10  ? 51   LYS A CA  1 
ATOM   380  C C   . LYS A 1 50  ? -73.356 31.290 -18.706 1.00 40.61  ? 51   LYS A C   1 
ATOM   381  O O   . LYS A 1 50  ? -72.838 31.005 -17.654 1.00 35.40  ? 51   LYS A O   1 
ATOM   382  C CB  . LYS A 1 50  ? -71.802 30.194 -20.356 1.00 40.64  ? 51   LYS A CB  1 
ATOM   383  C CG  . LYS A 1 50  ? -72.753 29.017 -20.536 1.00 40.81  ? 51   LYS A CG  1 
ATOM   384  C CD  . LYS A 1 50  ? -73.808 29.291 -21.594 1.00 35.93  ? 51   LYS A CD  1 
ATOM   385  C CE  . LYS A 1 50  ? -74.517 27.989 -21.910 1.00 38.25  ? 51   LYS A CE  1 
ATOM   386  N NZ  . LYS A 1 50  ? -75.541 28.202 -22.961 1.00 40.30  ? 51   LYS A NZ  1 
ATOM   387  N N   . LYS A 1 51  ? -74.663 31.480 -18.841 1.00 41.59  ? 52   LYS A N   1 
ATOM   388  C CA  . LYS A 1 51  ? -75.623 31.245 -17.786 1.00 44.33  ? 52   LYS A CA  1 
ATOM   389  C C   . LYS A 1 51  ? -75.596 29.785 -17.418 1.00 40.24  ? 52   LYS A C   1 
ATOM   390  O O   . LYS A 1 51  ? -75.628 28.914 -18.261 1.00 39.25  ? 52   LYS A O   1 
ATOM   391  C CB  . LYS A 1 51  ? -77.020 31.673 -18.198 1.00 51.79  ? 52   LYS A CB  1 
ATOM   392  C CG  . LYS A 1 51  ? -77.096 33.182 -18.430 1.00 66.43  ? 52   LYS A CG  1 
ATOM   393  C CD  . LYS A 1 51  ? -78.454 33.675 -18.928 1.00 78.59  ? 52   LYS A CD  1 
ATOM   394  C CE  . LYS A 1 51  ? -78.941 32.913 -20.162 1.00 80.44  ? 52   LYS A CE  1 
ATOM   395  N NZ  . LYS A 1 51  ? -79.870 33.754 -20.966 1.00 83.53  ? 52   LYS A NZ  1 
ATOM   396  N N   . PRO A 1 52  ? -75.478 29.513 -16.132 1.00 41.79  ? 53   PRO A N   1 
ATOM   397  C CA  . PRO A 1 52  ? -75.342 28.126 -15.714 1.00 42.42  ? 53   PRO A CA  1 
ATOM   398  C C   . PRO A 1 52  ? -76.554 27.332 -16.126 1.00 41.33  ? 53   PRO A C   1 
ATOM   399  O O   . PRO A 1 52  ? -77.635 27.890 -16.386 1.00 40.26  ? 53   PRO A O   1 
ATOM   400  C CB  . PRO A 1 52  ? -75.251 28.234 -14.202 1.00 44.04  ? 53   PRO A CB  1 
ATOM   401  C CG  . PRO A 1 52  ? -74.785 29.656 -13.954 1.00 44.12  ? 53   PRO A CG  1 
ATOM   402  C CD  . PRO A 1 52  ? -75.528 30.437 -14.987 1.00 38.97  ? 53   PRO A CD  1 
ATOM   403  N N   . TRP A 1 53  ? -76.360 26.046 -16.249 1.00 42.18  ? 54   TRP A N   1 
ATOM   404  C CA  . TRP A 1 53  ? -77.423 25.179 -16.799 1.00 44.88  ? 54   TRP A CA  1 
ATOM   405  C C   . TRP A 1 53  ? -77.823 24.094 -15.786 1.00 46.76  ? 54   TRP A C   1 
ATOM   406  O O   . TRP A 1 53  ? -76.999 23.658 -14.941 1.00 43.33  ? 54   TRP A O   1 
ATOM   407  C CB  . TRP A 1 53  ? -76.984 24.537 -18.153 1.00 38.57  ? 54   TRP A CB  1 
ATOM   408  C CG  . TRP A 1 53  ? -75.766 23.759 -18.042 1.00 32.41  ? 54   TRP A CG  1 
ATOM   409  C CD1 . TRP A 1 53  ? -75.667 22.495 -17.635 1.00 35.71  ? 54   TRP A CD1 1 
ATOM   410  C CD2 . TRP A 1 53  ? -74.437 24.213 -18.275 1.00 34.68  ? 54   TRP A CD2 1 
ATOM   411  N NE1 . TRP A 1 53  ? -74.344 22.102 -17.587 1.00 34.84  ? 54   TRP A NE1 1 
ATOM   412  C CE2 . TRP A 1 53  ? -73.578 23.157 -17.988 1.00 32.36  ? 54   TRP A CE2 1 
ATOM   413  C CE3 . TRP A 1 53  ? -73.891 25.423 -18.713 1.00 34.94  ? 54   TRP A CE3 1 
ATOM   414  C CZ2 . TRP A 1 53  ? -72.225 23.256 -18.143 1.00 37.06  ? 54   TRP A CZ2 1 
ATOM   415  C CZ3 . TRP A 1 53  ? -72.576 25.527 -18.870 1.00 33.32  ? 54   TRP A CZ3 1 
ATOM   416  C CH2 . TRP A 1 53  ? -71.735 24.458 -18.605 1.00 38.95  ? 54   TRP A CH2 1 
ATOM   417  N N   . SER A 1 54  ? -79.089 23.684 -15.888 1.00 54.16  ? 55   SER A N   1 
ATOM   418  C CA  . SER A 1 54  ? -79.621 22.512 -15.194 1.00 59.83  ? 55   SER A CA  1 
ATOM   419  C C   . SER A 1 54  ? -79.279 21.297 -16.018 1.00 59.52  ? 55   SER A C   1 
ATOM   420  O O   . SER A 1 54  ? -79.058 21.398 -17.235 1.00 57.39  ? 55   SER A O   1 
ATOM   421  C CB  . SER A 1 54  ? -81.149 22.574 -15.094 1.00 58.59  ? 55   SER A CB  1 
ATOM   422  O OG  . SER A 1 54  ? -81.537 23.606 -14.195 1.00 66.62  ? 55   SER A OG  1 
ATOM   423  N N   . GLY A 1 55  ? -79.265 20.145 -15.368 1.00 54.19  ? 56   GLY A N   1 
ATOM   424  C CA  . GLY A 1 55  ? -78.976 18.916 -16.081 1.00 50.57  ? 56   GLY A CA  1 
ATOM   425  C C   . GLY A 1 55  ? -77.497 18.813 -16.421 1.00 48.93  ? 56   GLY A C   1 
ATOM   426  O O   . GLY A 1 55  ? -76.658 19.555 -15.887 1.00 44.50  ? 56   GLY A O   1 
ATOM   427  N N   . VAL A 1 56  ? -77.227 17.878 -17.328 1.00 45.51  ? 57   VAL A N   1 
ATOM   428  C CA  . VAL A 1 56  ? -75.912 17.389 -17.705 1.00 41.81  ? 57   VAL A CA  1 
ATOM   429  C C   . VAL A 1 56  ? -75.598 17.776 -19.173 1.00 41.30  ? 57   VAL A C   1 
ATOM   430  O O   . VAL A 1 56  ? -76.324 17.426 -20.079 1.00 38.59  ? 57   VAL A O   1 
ATOM   431  C CB  . VAL A 1 56  ? -75.850 15.874 -17.506 1.00 41.36  ? 57   VAL A CB  1 
ATOM   432  C CG1 . VAL A 1 56  ? -74.522 15.332 -18.012 1.00 44.34  ? 57   VAL A CG1 1 
ATOM   433  C CG2 . VAL A 1 56  ? -76.041 15.540 -15.995 1.00 39.92  ? 57   VAL A CG2 1 
ATOM   434  N N   . TRP A 1 57  ? -74.532 18.557 -19.359 1.00 39.85  ? 58   TRP A N   1 
ATOM   435  C CA  . TRP A 1 57  ? -74.168 19.114 -20.636 1.00 38.12  ? 58   TRP A CA  1 
ATOM   436  C C   . TRP A 1 57  ? -73.401 17.990 -21.260 1.00 36.52  ? 58   TRP A C   1 
ATOM   437  O O   . TRP A 1 57  ? -72.411 17.523 -20.663 1.00 33.52  ? 58   TRP A O   1 
ATOM   438  C CB  . TRP A 1 57  ? -73.256 20.356 -20.505 1.00 41.41  ? 58   TRP A CB  1 
ATOM   439  C CG  . TRP A 1 57  ? -72.960 20.900 -21.842 1.00 39.07  ? 58   TRP A CG  1 
ATOM   440  C CD1 . TRP A 1 57  ? -72.031 20.417 -22.737 1.00 33.25  ? 58   TRP A CD1 1 
ATOM   441  C CD2 . TRP A 1 57  ? -73.645 21.950 -22.489 1.00 32.59  ? 58   TRP A CD2 1 
ATOM   442  N NE1 . TRP A 1 57  ? -72.117 21.097 -23.867 1.00 32.99  ? 58   TRP A NE1 1 
ATOM   443  C CE2 . TRP A 1 57  ? -73.105 22.046 -23.768 1.00 34.75  ? 58   TRP A CE2 1 
ATOM   444  C CE3 . TRP A 1 57  ? -74.662 22.834 -22.101 1.00 36.89  ? 58   TRP A CE3 1 
ATOM   445  C CZ2 . TRP A 1 57  ? -73.506 23.021 -24.676 1.00 32.74  ? 58   TRP A CZ2 1 
ATOM   446  C CZ3 . TRP A 1 57  ? -75.108 23.787 -22.992 1.00 34.67  ? 58   TRP A CZ3 1 
ATOM   447  C CH2 . TRP A 1 57  ? -74.525 23.877 -24.283 1.00 39.32  ? 58   TRP A CH2 1 
ATOM   448  N N   . ASN A 1 58  ? -73.889 17.531 -22.425 1.00 34.39  ? 59   ASN A N   1 
ATOM   449  C CA  . ASN A 1 58  ? -73.269 16.418 -23.159 1.00 36.90  ? 59   ASN A CA  1 
ATOM   450  C C   . ASN A 1 58  ? -71.974 17.001 -23.760 1.00 37.97  ? 59   ASN A C   1 
ATOM   451  O O   . ASN A 1 58  ? -72.048 17.902 -24.552 1.00 38.09  ? 59   ASN A O   1 
ATOM   452  C CB  . ASN A 1 58  ? -74.226 15.826 -24.270 1.00 33.91  ? 59   ASN A CB  1 
ATOM   453  C CG  . ASN A 1 58  ? -73.623 14.598 -25.009 1.00 45.01  ? 59   ASN A CG  1 
ATOM   454  O OD1 . ASN A 1 58  ? -72.418 14.301 -24.833 1.00 43.96  ? 59   ASN A OD1 1 
ATOM   455  N ND2 . ASN A 1 58  ? -74.471 13.867 -25.863 1.00 59.44  ? 59   ASN A ND2 1 
ATOM   456  N N   . ALA A 1 59  ? -70.812 16.514 -23.362 1.00 36.64  ? 60   ALA A N   1 
ATOM   457  C CA  . ALA A 1 59  ? -69.548 17.070 -23.845 1.00 33.59  ? 60   ALA A CA  1 
ATOM   458  C C   . ALA A 1 59  ? -68.772 15.967 -24.500 1.00 33.68  ? 60   ALA A C   1 
ATOM   459  O O   . ALA A 1 59  ? -67.571 15.809 -24.269 1.00 35.07  ? 60   ALA A O   1 
ATOM   460  C CB  . ALA A 1 59  ? -68.748 17.617 -22.702 1.00 30.79  ? 60   ALA A CB  1 
ATOM   461  N N   . SER A 1 60  ? -69.458 15.205 -25.342 1.00 35.91  ? 61   SER A N   1 
ATOM   462  C CA  . SER A 1 60  ? -68.826 14.052 -25.992 1.00 39.85  ? 61   SER A CA  1 
ATOM   463  C C   . SER A 1 60  ? -68.386 14.383 -27.417 1.00 35.20  ? 61   SER A C   1 
ATOM   464  O O   . SER A 1 60  ? -67.552 13.685 -27.958 1.00 32.39  ? 61   SER A O   1 
ATOM   465  C CB  . SER A 1 60  ? -69.753 12.848 -25.937 1.00 38.81  ? 61   SER A CB  1 
ATOM   466  O OG  . SER A 1 60  ? -70.969 13.265 -26.470 1.00 40.09  ? 61   SER A OG  1 
ATOM   467  N N   . THR A 1 61  ? -68.869 15.491 -27.980 1.00 38.79  ? 62   THR A N   1 
ATOM   468  C CA  . THR A 1 61  ? -68.449 15.846 -29.332 1.00 42.42  ? 62   THR A CA  1 
ATOM   469  C C   . THR A 1 61  ? -68.044 17.311 -29.490 1.00 38.65  ? 62   THR A C   1 
ATOM   470  O O   . THR A 1 61  ? -68.513 18.194 -28.804 1.00 39.49  ? 62   THR A O   1 
ATOM   471  C CB  . THR A 1 61  ? -69.519 15.507 -30.375 1.00 47.00  ? 62   THR A CB  1 
ATOM   472  O OG1 . THR A 1 61  ? -70.693 16.272 -30.101 1.00 43.32  ? 62   THR A OG1 1 
ATOM   473  C CG2 . THR A 1 61  ? -69.843 13.979 -30.341 1.00 53.91  ? 62   THR A CG2 1 
ATOM   474  N N   . TYR A 1 62  ? -67.132 17.507 -30.420 1.00 34.10  ? 63   TYR A N   1 
ATOM   475  C CA  . TYR A 1 62  ? -66.581 18.803 -30.764 1.00 33.47  ? 63   TYR A CA  1 
ATOM   476  C C   . TYR A 1 62  ? -67.662 19.798 -31.132 1.00 32.36  ? 63   TYR A C   1 
ATOM   477  O O   . TYR A 1 62  ? -68.684 19.467 -31.648 1.00 37.39  ? 63   TYR A O   1 
ATOM   478  C CB  . TYR A 1 62  ? -65.619 18.655 -31.929 1.00 29.37  ? 63   TYR A CB  1 
ATOM   479  C CG  . TYR A 1 62  ? -64.216 18.258 -31.635 1.00 28.91  ? 63   TYR A CG  1 
ATOM   480  C CD1 . TYR A 1 62  ? -63.515 18.825 -30.577 1.00 30.34  ? 63   TYR A CD1 1 
ATOM   481  C CD2 . TYR A 1 62  ? -63.514 17.379 -32.497 1.00 31.17  ? 63   TYR A CD2 1 
ATOM   482  C CE1 . TYR A 1 62  ? -62.145 18.560 -30.386 1.00 27.05  ? 63   TYR A CE1 1 
ATOM   483  C CE2 . TYR A 1 62  ? -62.115 17.078 -32.307 1.00 27.95  ? 63   TYR A CE2 1 
ATOM   484  C CZ  . TYR A 1 62  ? -61.446 17.711 -31.258 1.00 29.73  ? 63   TYR A CZ  1 
ATOM   485  O OH  . TYR A 1 62  ? -60.112 17.439 -30.996 1.00 31.22  ? 63   TYR A OH  1 
ATOM   486  N N   . PRO A 1 63  ? -67.471 21.034 -30.756 1.00 28.72  ? 64   PRO A N   1 
ATOM   487  C CA  . PRO A 1 63  ? -68.412 22.030 -31.076 1.00 27.88  ? 64   PRO A CA  1 
ATOM   488  C C   . PRO A 1 63  ? -68.218 22.518 -32.538 1.00 29.43  ? 64   PRO A C   1 
ATOM   489  O O   . PRO A 1 63  ? -67.293 22.101 -33.217 1.00 29.84  ? 64   PRO A O   1 
ATOM   490  C CB  . PRO A 1 63  ? -67.972 23.165 -30.146 1.00 27.99  ? 64   PRO A CB  1 
ATOM   491  C CG  . PRO A 1 63  ? -66.483 23.065 -30.121 1.00 26.25  ? 64   PRO A CG  1 
ATOM   492  C CD  . PRO A 1 63  ? -66.263 21.577 -30.108 1.00 29.82  ? 64   PRO A CD  1 
ATOM   493  N N   . ASN A 1 64  ? -69.074 23.426 -32.935 1.00 26.97  ? 65   ASN A N   1 
ATOM   494  C CA  . ASN A 1 64  ? -68.915 24.223 -34.096 1.00 34.32  ? 65   ASN A CA  1 
ATOM   495  C C   . ASN A 1 64  ? -67.659 25.124 -34.073 1.00 35.55  ? 65   ASN A C   1 
ATOM   496  O O   . ASN A 1 64  ? -67.182 25.571 -33.008 1.00 34.15  ? 65   ASN A O   1 
ATOM   497  C CB  . ASN A 1 64  ? -70.153 25.147 -34.263 1.00 35.64  ? 65   ASN A CB  1 
ATOM   498  C CG  . ASN A 1 64  ? -71.496 24.368 -34.415 1.00 41.35  ? 65   ASN A CG  1 
ATOM   499  O OD1 . ASN A 1 64  ? -71.596 23.337 -35.076 1.00 39.76  ? 65   ASN A OD1 1 
ATOM   500  N ND2 . ASN A 1 64  ? -72.535 24.929 -33.836 1.00 42.67  ? 65   ASN A ND2 1 
ATOM   501  N N   . ASN A 1 65  ? -67.189 25.432 -35.278 1.00 34.43  ? 66   ASN A N   1 
ATOM   502  C CA  . ASN A 1 65  ? -66.114 26.398 -35.481 1.00 34.69  ? 66   ASN A CA  1 
ATOM   503  C C   . ASN A 1 65  ? -66.739 27.734 -35.731 1.00 32.61  ? 66   ASN A C   1 
ATOM   504  O O   . ASN A 1 65  ? -67.885 27.798 -36.178 1.00 32.00  ? 66   ASN A O   1 
ATOM   505  C CB  . ASN A 1 65  ? -65.205 26.002 -36.643 1.00 34.46  ? 66   ASN A CB  1 
ATOM   506  C CG  . ASN A 1 65  ? -64.725 24.539 -36.561 1.00 36.64  ? 66   ASN A CG  1 
ATOM   507  O OD1 . ASN A 1 65  ? -64.775 23.797 -37.551 1.00 38.31  ? 66   ASN A OD1 1 
ATOM   508  N ND2 . ASN A 1 65  ? -64.268 24.131 -35.387 1.00 37.16  ? 66   ASN A ND2 1 
ATOM   509  N N   . CYS A 1 66  ? -66.004 28.809 -35.446 1.00 28.94  ? 67   CYS A N   1 
ATOM   510  C CA  . CYS A 1 66  ? -66.535 30.132 -35.705 1.00 29.29  ? 67   CYS A CA  1 
ATOM   511  C C   . CYS A 1 66  ? -66.594 30.410 -37.200 1.00 32.20  ? 67   CYS A C   1 
ATOM   512  O O   . CYS A 1 66  ? -65.895 29.759 -38.013 1.00 30.78  ? 67   CYS A O   1 
ATOM   513  C CB  . CYS A 1 66  ? -65.677 31.190 -34.957 1.00 35.23  ? 67   CYS A CB  1 
ATOM   514  S SG  . CYS A 1 66  ? -65.755 31.039 -33.134 1.00 37.72  ? 67   CYS A SG  1 
ATOM   515  N N   . GLN A 1 67  ? -67.445 31.355 -37.576 1.00 31.23  ? 68   GLN A N   1 
ATOM   516  C CA  . GLN A 1 67  ? -67.582 31.737 -38.943 1.00 29.84  ? 68   GLN A CA  1 
ATOM   517  C C   . GLN A 1 67  ? -66.272 32.343 -39.452 1.00 32.40  ? 68   GLN A C   1 
ATOM   518  O O   . GLN A 1 67  ? -65.756 33.220 -38.840 1.00 36.52  ? 68   GLN A O   1 
ATOM   519  C CB  . GLN A 1 67  ? -68.691 32.732 -39.144 1.00 29.52  ? 68   GLN A CB  1 
ATOM   520  C CG  . GLN A 1 67  ? -70.060 32.166 -38.996 1.00 32.81  ? 68   GLN A CG  1 
ATOM   521  C CD  . GLN A 1 67  ? -70.564 31.365 -40.219 1.00 34.13  ? 68   GLN A CD  1 
ATOM   522  O OE1 . GLN A 1 67  ? -69.837 31.089 -41.143 1.00 35.84  ? 68   GLN A OE1 1 
ATOM   523  N NE2 . GLN A 1 67  ? -71.789 30.906 -40.140 1.00 33.60  ? 68   GLN A NE2 1 
ATOM   524  N N   . GLN A 1 68  ? -65.793 31.880 -40.607 1.00 32.76  ? 69   GLN A N   1 
ATOM   525  C CA  . GLN A 1 68  ? -64.492 32.257 -41.135 1.00 35.50  ? 69   GLN A CA  1 
ATOM   526  C C   . GLN A 1 68  ? -64.320 31.978 -42.645 1.00 35.99  ? 69   GLN A C   1 
ATOM   527  O O   . GLN A 1 68  ? -64.882 31.019 -43.217 1.00 27.67  ? 69   GLN A O   1 
ATOM   528  C CB  . GLN A 1 68  ? -63.356 31.533 -40.378 1.00 32.03  ? 69   GLN A CB  1 
ATOM   529  C CG  . GLN A 1 68  ? -63.417 30.026 -40.412 1.00 29.11  ? 69   GLN A CG  1 
ATOM   530  C CD  . GLN A 1 68  ? -62.408 29.349 -39.458 1.00 33.34  ? 69   GLN A CD  1 
ATOM   531  O OE1 . GLN A 1 68  ? -61.271 28.988 -39.852 1.00 29.10  ? 69   GLN A OE1 1 
ATOM   532  N NE2 . GLN A 1 68  ? -62.850 29.141 -38.187 1.00 33.03  ? 69   GLN A NE2 1 
ATOM   533  N N   . TYR A 1 69  ? -63.498 32.827 -43.260 1.00 35.64  ? 70   TYR A N   1 
ATOM   534  C CA  . TYR A 1 69  ? -62.940 32.536 -44.569 1.00 33.26  ? 70   TYR A CA  1 
ATOM   535  C C   . TYR A 1 69  ? -62.437 31.121 -44.578 1.00 34.14  ? 70   TYR A C   1 
ATOM   536  O O   . TYR A 1 69  ? -61.777 30.691 -43.612 1.00 34.61  ? 70   TYR A O   1 
ATOM   537  C CB  . TYR A 1 69  ? -61.767 33.442 -44.850 1.00 35.69  ? 70   TYR A CB  1 
ATOM   538  C CG  . TYR A 1 69  ? -61.118 33.189 -46.175 1.00 34.37  ? 70   TYR A CG  1 
ATOM   539  C CD1 . TYR A 1 69  ? -61.685 33.685 -47.367 1.00 34.48  ? 70   TYR A CD1 1 
ATOM   540  C CD2 . TYR A 1 69  ? -59.920 32.506 -46.245 1.00 33.27  ? 70   TYR A CD2 1 
ATOM   541  C CE1 . TYR A 1 69  ? -61.073 33.468 -48.601 1.00 33.66  ? 70   TYR A CE1 1 
ATOM   542  C CE2 . TYR A 1 69  ? -59.294 32.265 -47.461 1.00 36.13  ? 70   TYR A CE2 1 
ATOM   543  C CZ  . TYR A 1 69  ? -59.862 32.742 -48.632 1.00 38.44  ? 70   TYR A CZ  1 
ATOM   544  O OH  . TYR A 1 69  ? -59.197 32.482 -49.799 1.00 36.63  ? 70   TYR A OH  1 
ATOM   545  N N   . VAL A 1 70  ? -62.744 30.408 -45.669 1.00 32.48  ? 71   VAL A N   1 
ATOM   546  C CA  . VAL A 1 70  ? -62.291 29.023 -45.897 1.00 30.35  ? 71   VAL A CA  1 
ATOM   547  C C   . VAL A 1 70  ? -61.351 28.942 -47.125 1.00 33.60  ? 71   VAL A C   1 
ATOM   548  O O   . VAL A 1 70  ? -61.698 29.416 -48.237 1.00 37.40  ? 71   VAL A O   1 
ATOM   549  C CB  . VAL A 1 70  ? -63.491 28.125 -46.081 1.00 30.89  ? 71   VAL A CB  1 
ATOM   550  C CG1 . VAL A 1 70  ? -63.079 26.718 -46.435 1.00 32.19  ? 71   VAL A CG1 1 
ATOM   551  C CG2 . VAL A 1 70  ? -64.327 28.098 -44.783 1.00 37.95  ? 71   VAL A CG2 1 
ATOM   552  N N   . ASP A 1 71  ? -60.150 28.396 -46.913 1.00 32.06  ? 72   ASP A N   1 
ATOM   553  C CA  . ASP A 1 71  ? -59.108 28.343 -47.935 1.00 31.35  ? 72   ASP A CA  1 
ATOM   554  C C   . ASP A 1 71  ? -59.534 27.253 -48.970 1.00 34.06  ? 72   ASP A C   1 
ATOM   555  O O   . ASP A 1 71  ? -59.625 26.098 -48.623 1.00 34.72  ? 72   ASP A O   1 
ATOM   556  C CB  . ASP A 1 71  ? -57.800 27.942 -47.293 1.00 31.68  ? 72   ASP A CB  1 
ATOM   557  C CG  . ASP A 1 71  ? -56.619 27.819 -48.305 1.00 34.93  ? 72   ASP A CG  1 
ATOM   558  O OD1 . ASP A 1 71  ? -56.797 28.082 -49.483 1.00 37.77  ? 72   ASP A OD1 1 
ATOM   559  O OD2 . ASP A 1 71  ? -55.495 27.512 -47.894 1.00 33.37  ? 72   ASP A OD2 1 
ATOM   560  N N   . GLU A 1 72  ? -59.790 27.643 -50.216 1.00 31.90  ? 73   GLU A N   1 
ATOM   561  C CA  . GLU A 1 72  ? -60.094 26.705 -51.300 1.00 35.90  ? 73   GLU A CA  1 
ATOM   562  C C   . GLU A 1 72  ? -59.026 26.839 -52.404 1.00 37.75  ? 73   GLU A C   1 
ATOM   563  O O   . GLU A 1 72  ? -59.264 26.597 -53.593 1.00 37.77  ? 73   GLU A O   1 
ATOM   564  C CB  . GLU A 1 72  ? -61.454 27.042 -51.858 1.00 35.27  ? 73   GLU A CB  1 
ATOM   565  C CG  . GLU A 1 72  ? -62.610 26.529 -51.058 1.00 44.10  ? 73   GLU A CG  1 
ATOM   566  C CD  . GLU A 1 72  ? -63.851 27.401 -51.280 1.00 56.31  ? 73   GLU A CD  1 
ATOM   567  O OE1 . GLU A 1 72  ? -64.273 27.652 -52.458 1.00 50.22  ? 73   GLU A OE1 1 
ATOM   568  O OE2 . GLU A 1 72  ? -64.389 27.863 -50.244 1.00 74.14  ? 73   GLU A OE2 1 
ATOM   569  N N   . GLN A 1 73  ? -57.847 27.280 -52.021 1.00 38.15  ? 74   GLN A N   1 
ATOM   570  C CA  . GLN A 1 73  ? -56.844 27.564 -53.010 1.00 41.78  ? 74   GLN A CA  1 
ATOM   571  C C   . GLN A 1 73  ? -56.352 26.233 -53.614 1.00 38.11  ? 74   GLN A C   1 
ATOM   572  O O   . GLN A 1 73  ? -55.951 26.199 -54.723 1.00 41.77  ? 74   GLN A O   1 
ATOM   573  C CB  . GLN A 1 73  ? -55.781 28.443 -52.366 1.00 39.43  ? 74   GLN A CB  1 
ATOM   574  C CG  . GLN A 1 73  ? -54.669 28.991 -53.228 1.00 50.99  ? 74   GLN A CG  1 
ATOM   575  C CD  . GLN A 1 73  ? -55.133 29.556 -54.554 1.00 54.57  ? 74   GLN A CD  1 
ATOM   576  O OE1 . GLN A 1 73  ? -55.952 30.465 -54.605 1.00 53.21  ? 74   GLN A OE1 1 
ATOM   577  N NE2 . GLN A 1 73  ? -54.575 29.037 -55.629 1.00 56.11  ? 74   GLN A NE2 1 
ATOM   578  N N   . PHE A 1 74  ? -56.460 25.129 -52.877 1.00 39.68  ? 75   PHE A N   1 
ATOM   579  C CA  . PHE A 1 74  ? -56.025 23.799 -53.332 1.00 35.64  ? 75   PHE A CA  1 
ATOM   580  C C   . PHE A 1 74  ? -56.990 22.695 -52.882 1.00 36.31  ? 75   PHE A C   1 
ATOM   581  O O   . PHE A 1 74  ? -56.702 21.912 -51.984 1.00 34.30  ? 75   PHE A O   1 
ATOM   582  C CB  . PHE A 1 74  ? -54.638 23.490 -52.797 1.00 32.63  ? 75   PHE A CB  1 
ATOM   583  C CG  . PHE A 1 74  ? -53.615 24.524 -53.147 1.00 33.86  ? 75   PHE A CG  1 
ATOM   584  C CD1 . PHE A 1 74  ? -53.108 24.598 -54.460 1.00 30.76  ? 75   PHE A CD1 1 
ATOM   585  C CD2 . PHE A 1 74  ? -53.105 25.404 -52.171 1.00 32.22  ? 75   PHE A CD2 1 
ATOM   586  C CE1 . PHE A 1 74  ? -52.156 25.541 -54.785 1.00 30.00  ? 75   PHE A CE1 1 
ATOM   587  C CE2 . PHE A 1 74  ? -52.123 26.339 -52.506 1.00 34.41  ? 75   PHE A CE2 1 
ATOM   588  C CZ  . PHE A 1 74  ? -51.658 26.406 -53.831 1.00 33.05  ? 75   PHE A CZ  1 
ATOM   589  N N   . PRO A 1 75  ? -58.150 22.635 -53.515 1.00 40.37  ? 76   PRO A N   1 
ATOM   590  C CA  . PRO A 1 75  ? -59.183 21.665 -53.198 1.00 40.43  ? 76   PRO A CA  1 
ATOM   591  C C   . PRO A 1 75  ? -58.703 20.258 -53.139 1.00 42.41  ? 76   PRO A C   1 
ATOM   592  O O   . PRO A 1 75  ? -57.949 19.793 -54.045 1.00 43.92  ? 76   PRO A O   1 
ATOM   593  C CB  . PRO A 1 75  ? -60.182 21.858 -54.317 1.00 35.21  ? 76   PRO A CB  1 
ATOM   594  C CG  . PRO A 1 75  ? -60.150 23.310 -54.521 1.00 37.66  ? 76   PRO A CG  1 
ATOM   595  C CD  . PRO A 1 75  ? -58.675 23.649 -54.442 1.00 44.78  ? 76   PRO A CD  1 
ATOM   596  N N   . GLY A 1 76  ? -59.108 19.615 -52.028 1.00 46.66  ? 77   GLY A N   1 
ATOM   597  C CA  . GLY A 1 76  ? -58.691 18.243 -51.659 1.00 44.75  ? 77   GLY A CA  1 
ATOM   598  C C   . GLY A 1 76  ? -57.255 18.047 -51.199 1.00 43.59  ? 77   GLY A C   1 
ATOM   599  O O   . GLY A 1 76  ? -56.841 16.925 -50.881 1.00 51.57  ? 77   GLY A O   1 
ATOM   600  N N   . PHE A 1 77  ? -56.467 19.120 -51.154 1.00 35.15  ? 78   PHE A N   1 
ATOM   601  C CA  . PHE A 1 77  ? -55.084 18.981 -50.798 1.00 31.75  ? 78   PHE A CA  1 
ATOM   602  C C   . PHE A 1 77  ? -54.946 19.013 -49.277 1.00 31.95  ? 78   PHE A C   1 
ATOM   603  O O   . PHE A 1 77  ? -55.435 19.897 -48.604 1.00 32.07  ? 78   PHE A O   1 
ATOM   604  C CB  . PHE A 1 77  ? -54.310 20.094 -51.441 1.00 31.30  ? 78   PHE A CB  1 
ATOM   605  C CG  . PHE A 1 77  ? -52.855 20.076 -51.117 1.00 33.10  ? 78   PHE A CG  1 
ATOM   606  C CD1 . PHE A 1 77  ? -52.044 19.009 -51.497 1.00 32.78  ? 78   PHE A CD1 1 
ATOM   607  C CD2 . PHE A 1 77  ? -52.286 21.153 -50.446 1.00 30.35  ? 78   PHE A CD2 1 
ATOM   608  C CE1 . PHE A 1 77  ? -50.686 19.018 -51.204 1.00 33.17  ? 78   PHE A CE1 1 
ATOM   609  C CE2 . PHE A 1 77  ? -50.944 21.191 -50.195 1.00 29.26  ? 78   PHE A CE2 1 
ATOM   610  C CZ  . PHE A 1 77  ? -50.144 20.107 -50.535 1.00 33.15  ? 78   PHE A CZ  1 
ATOM   611  N N   . SER A 1 78  ? -54.255 18.073 -48.707 1.00 32.78  ? 79   SER A N   1 
ATOM   612  C CA  . SER A 1 78  ? -54.360 17.979 -47.241 1.00 37.75  ? 79   SER A CA  1 
ATOM   613  C C   . SER A 1 78  ? -53.520 19.110 -46.600 1.00 38.44  ? 79   SER A C   1 
ATOM   614  O O   . SER A 1 78  ? -53.797 19.558 -45.475 1.00 33.38  ? 79   SER A O   1 
ATOM   615  C CB  . SER A 1 78  ? -53.898 16.616 -46.762 1.00 32.86  ? 79   SER A CB  1 
ATOM   616  O OG  . SER A 1 78  ? -52.502 16.549 -47.038 1.00 37.00  ? 79   SER A OG  1 
ATOM   617  N N   . GLY A 1 79  ? -52.513 19.591 -47.335 1.00 34.75  ? 80   GLY A N   1 
ATOM   618  C CA  . GLY A 1 79  ? -51.598 20.583 -46.775 1.00 32.91  ? 80   GLY A CA  1 
ATOM   619  C C   . GLY A 1 79  ? -52.288 21.865 -46.311 1.00 34.27  ? 80   GLY A C   1 
ATOM   620  O O   . GLY A 1 79  ? -51.848 22.479 -45.321 1.00 32.32  ? 80   GLY A O   1 
ATOM   621  N N   . SER A 1 80  ? -53.312 22.280 -47.068 1.00 30.36  ? 81   SER A N   1 
ATOM   622  C CA  . SER A 1 80  ? -54.059 23.475 -46.842 1.00 32.03  ? 81   SER A CA  1 
ATOM   623  C C   . SER A 1 80  ? -55.327 23.147 -46.079 1.00 35.25  ? 81   SER A C   1 
ATOM   624  O O   . SER A 1 80  ? -55.735 23.918 -45.196 1.00 35.36  ? 81   SER A O   1 
ATOM   625  C CB  . SER A 1 80  ? -54.456 24.202 -48.174 1.00 33.57  ? 81   SER A CB  1 
ATOM   626  O OG  . SER A 1 80  ? -55.151 23.386 -49.142 1.00 31.70  ? 81   SER A OG  1 
ATOM   627  N N   . GLU A 1 81  ? -55.961 22.036 -46.429 1.00 33.80  ? 82   GLU A N   1 
ATOM   628  C CA  . GLU A 1 81  ? -57.233 21.633 -45.798 1.00 36.68  ? 82   GLU A CA  1 
ATOM   629  C C   . GLU A 1 81  ? -57.120 21.183 -44.360 1.00 33.60  ? 82   GLU A C   1 
ATOM   630  O O   . GLU A 1 81  ? -58.081 21.261 -43.641 1.00 28.68  ? 82   GLU A O   1 
ATOM   631  C CB  . GLU A 1 81  ? -58.017 20.605 -46.655 1.00 41.16  ? 82   GLU A CB  1 
ATOM   632  C CG  . GLU A 1 81  ? -59.033 21.352 -47.520 1.00 47.07  ? 82   GLU A CG  1 
ATOM   633  C CD  . GLU A 1 81  ? -59.485 20.637 -48.751 1.00 52.71  ? 82   GLU A CD  1 
ATOM   634  O OE1 . GLU A 1 81  ? -59.411 19.403 -48.778 1.00 62.19  ? 82   GLU A OE1 1 
ATOM   635  O OE2 . GLU A 1 81  ? -59.965 21.324 -49.688 1.00 55.71  ? 82   GLU A OE2 1 
ATOM   636  N N   . MET A 1 82  ? -55.931 20.814 -43.905 1.00 30.05  ? 83   MET A N   1 
ATOM   637  C CA  . MET A 1 82  ? -55.780 20.508 -42.491 1.00 29.69  ? 83   MET A CA  1 
ATOM   638  C C   . MET A 1 82  ? -55.975 21.728 -41.557 1.00 34.47  ? 83   MET A C   1 
ATOM   639  O O   . MET A 1 82  ? -56.033 21.523 -40.344 1.00 32.81  ? 83   MET A O   1 
ATOM   640  C CB  . MET A 1 82  ? -54.423 19.902 -42.209 1.00 30.69  ? 83   MET A CB  1 
ATOM   641  C CG  . MET A 1 82  ? -53.307 20.878 -42.438 1.00 35.94  ? 83   MET A CG  1 
ATOM   642  S SD  . MET A 1 82  ? -51.764 20.105 -42.064 1.00 41.49  ? 83   MET A SD  1 
ATOM   643  C CE  . MET A 1 82  ? -51.598 20.388 -40.312 1.00 45.51  ? 83   MET A CE  1 
ATOM   644  N N   . TRP A 1 83  ? -56.052 22.950 -42.126 1.00 29.64  ? 84   TRP A N   1 
ATOM   645  C CA  . TRP A 1 83  ? -56.167 24.190 -41.396 1.00 31.99  ? 84   TRP A CA  1 
ATOM   646  C C   . TRP A 1 83  ? -57.580 24.712 -41.427 1.00 32.26  ? 84   TRP A C   1 
ATOM   647  O O   . TRP A 1 83  ? -57.929 25.636 -40.688 1.00 32.59  ? 84   TRP A O   1 
ATOM   648  C CB  . TRP A 1 83  ? -55.169 25.259 -41.949 1.00 30.20  ? 84   TRP A CB  1 
ATOM   649  C CG  . TRP A 1 83  ? -53.761 24.788 -41.879 1.00 31.95  ? 84   TRP A CG  1 
ATOM   650  C CD1 . TRP A 1 83  ? -52.964 24.387 -42.934 1.00 37.47  ? 84   TRP A CD1 1 
ATOM   651  C CD2 . TRP A 1 83  ? -52.975 24.577 -40.712 1.00 33.94  ? 84   TRP A CD2 1 
ATOM   652  N NE1 . TRP A 1 83  ? -51.730 23.991 -42.490 1.00 34.49  ? 84   TRP A NE1 1 
ATOM   653  C CE2 . TRP A 1 83  ? -51.713 24.093 -41.126 1.00 36.18  ? 84   TRP A CE2 1 
ATOM   654  C CE3 . TRP A 1 83  ? -53.205 24.736 -39.360 1.00 33.80  ? 84   TRP A CE3 1 
ATOM   655  C CZ2 . TRP A 1 83  ? -50.711 23.797 -40.230 1.00 36.06  ? 84   TRP A CZ2 1 
ATOM   656  C CZ3 . TRP A 1 83  ? -52.198 24.433 -38.478 1.00 33.47  ? 84   TRP A CZ3 1 
ATOM   657  C CH2 . TRP A 1 83  ? -50.982 23.956 -38.913 1.00 34.99  ? 84   TRP A CH2 1 
ATOM   658  N N   . ASN A 1 84  ? -58.407 24.148 -42.290 1.00 31.56  ? 85   ASN A N   1 
ATOM   659  C CA  . ASN A 1 84  ? -59.766 24.681 -42.436 1.00 31.30  ? 85   ASN A CA  1 
ATOM   660  C C   . ASN A 1 84  ? -60.661 24.098 -41.364 1.00 29.96  ? 85   ASN A C   1 
ATOM   661  O O   . ASN A 1 84  ? -60.377 23.020 -40.794 1.00 28.73  ? 85   ASN A O   1 
ATOM   662  C CB  . ASN A 1 84  ? -60.365 24.279 -43.809 1.00 35.58  ? 85   ASN A CB  1 
ATOM   663  C CG  . ASN A 1 84  ? -59.907 25.177 -44.981 1.00 41.32  ? 85   ASN A CG  1 
ATOM   664  O OD1 . ASN A 1 84  ? -59.593 26.397 -44.845 1.00 37.40  ? 85   ASN A OD1 1 
ATOM   665  N ND2 . ASN A 1 84  ? -59.854 24.550 -46.154 1.00 34.79  ? 85   ASN A ND2 1 
ATOM   666  N N   . PRO A 1 85  ? -61.807 24.737 -41.154 1.00 26.61  ? 86   PRO A N   1 
ATOM   667  C CA  . PRO A 1 85  ? -62.811 24.193 -40.255 1.00 26.38  ? 86   PRO A CA  1 
ATOM   668  C C   . PRO A 1 85  ? -63.188 22.777 -40.629 1.00 28.52  ? 86   PRO A C   1 
ATOM   669  O O   . PRO A 1 85  ? -63.517 22.541 -41.786 1.00 32.10  ? 86   PRO A O   1 
ATOM   670  C CB  . PRO A 1 85  ? -64.021 25.081 -40.454 1.00 24.65  ? 86   PRO A CB  1 
ATOM   671  C CG  . PRO A 1 85  ? -63.555 26.288 -41.216 1.00 26.40  ? 86   PRO A CG  1 
ATOM   672  C CD  . PRO A 1 85  ? -62.222 25.990 -41.811 1.00 26.27  ? 86   PRO A CD  1 
ATOM   673  N N   . ASN A 1 86  ? -63.125 21.846 -39.667 1.00 28.69  ? 87   ASN A N   1 
ATOM   674  C CA  . ASN A 1 86  ? -63.656 20.483 -39.865 1.00 27.66  ? 87   ASN A CA  1 
ATOM   675  C C   . ASN A 1 86  ? -65.015 20.298 -39.171 1.00 30.97  ? 87   ASN A C   1 
ATOM   676  O O   . ASN A 1 86  ? -65.519 19.199 -39.069 1.00 34.61  ? 87   ASN A O   1 
ATOM   677  C CB  . ASN A 1 86  ? -62.660 19.438 -39.372 1.00 27.61  ? 87   ASN A CB  1 
ATOM   678  C CG  . ASN A 1 86  ? -62.277 19.637 -37.866 1.00 32.56  ? 87   ASN A CG  1 
ATOM   679  O OD1 . ASN A 1 86  ? -62.700 20.611 -37.192 1.00 36.49  ? 87   ASN A OD1 1 
ATOM   680  N ND2 . ASN A 1 86  ? -61.512 18.735 -37.363 1.00 27.70  ? 87   ASN A ND2 1 
ATOM   681  N N   . ARG A 1 87  ? -65.626 21.347 -38.679 1.00 32.59  ? 88   ARG A N   1 
ATOM   682  C CA  . ARG A 1 87  ? -66.987 21.200 -38.173 1.00 36.23  ? 88   ARG A CA  1 
ATOM   683  C C   . ARG A 1 87  ? -67.862 22.184 -38.869 1.00 35.98  ? 88   ARG A C   1 
ATOM   684  O O   . ARG A 1 87  ? -67.381 23.041 -39.552 1.00 37.43  ? 88   ARG A O   1 
ATOM   685  C CB  . ARG A 1 87  ? -67.007 21.418 -36.616 1.00 36.73  ? 88   ARG A CB  1 
ATOM   686  C CG  . ARG A 1 87  ? -66.428 20.208 -35.828 1.00 40.06  ? 88   ARG A CG  1 
ATOM   687  C CD  . ARG A 1 87  ? -67.472 19.070 -35.839 1.00 45.48  ? 88   ARG A CD  1 
ATOM   688  N NE  . ARG A 1 87  ? -67.088 17.782 -35.272 1.00 53.31  ? 88   ARG A NE  1 
ATOM   689  C CZ  . ARG A 1 87  ? -66.083 17.002 -35.719 1.00 63.01  ? 88   ARG A CZ  1 
ATOM   690  N NH1 . ARG A 1 87  ? -65.309 17.342 -36.765 1.00 68.78  ? 88   ARG A NH1 1 
ATOM   691  N NH2 . ARG A 1 87  ? -65.806 15.862 -35.101 1.00 63.57  ? 88   ARG A NH2 1 
ATOM   692  N N   . GLU A 1 88  ? -69.157 22.132 -38.653 1.00 39.77  ? 89   GLU A N   1 
ATOM   693  C CA  . GLU A 1 88  ? -69.991 23.144 -39.232 1.00 43.64  ? 89   GLU A CA  1 
ATOM   694  C C   . GLU A 1 88  ? -69.579 24.494 -38.630 1.00 39.49  ? 89   GLU A C   1 
ATOM   695  O O   . GLU A 1 88  ? -69.233 24.542 -37.486 1.00 32.17  ? 89   GLU A O   1 
ATOM   696  C CB  . GLU A 1 88  ? -71.478 22.866 -39.013 1.00 52.77  ? 89   GLU A CB  1 
ATOM   697  C CG  . GLU A 1 88  ? -72.369 23.674 -39.953 1.00 67.79  ? 89   GLU A CG  1 
ATOM   698  C CD  . GLU A 1 88  ? -73.823 23.801 -39.489 1.00 76.02  ? 89   GLU A CD  1 
ATOM   699  O OE1 . GLU A 1 88  ? -74.676 23.173 -40.135 1.00 84.61  ? 89   GLU A OE1 1 
ATOM   700  O OE2 . GLU A 1 88  ? -74.125 24.533 -38.505 1.00 78.30  ? 89   GLU A OE2 1 
ATOM   701  N N   . MET A 1 89  ? -69.590 25.565 -39.423 1.00 35.27  ? 90   MET A N   1 
ATOM   702  C CA  . MET A 1 89  ? -69.351 26.893 -38.916 1.00 33.55  ? 90   MET A CA  1 
ATOM   703  C C   . MET A 1 89  ? -70.633 27.453 -38.337 1.00 33.12  ? 90   MET A C   1 
ATOM   704  O O   . MET A 1 89  ? -71.738 27.210 -38.879 1.00 34.39  ? 90   MET A O   1 
ATOM   705  C CB  . MET A 1 89  ? -68.783 27.823 -40.017 1.00 31.21  ? 90   MET A CB  1 
ATOM   706  C CG  . MET A 1 89  ? -67.350 27.443 -40.435 1.00 33.34  ? 90   MET A CG  1 
ATOM   707  S SD  . MET A 1 89  ? -66.594 28.681 -41.510 1.00 35.20  ? 90   MET A SD  1 
ATOM   708  C CE  . MET A 1 89  ? -67.679 28.563 -42.947 1.00 39.65  ? 90   MET A CE  1 
ATOM   709  N N   . SER A 1 90  ? -70.486 28.236 -37.266 1.00 32.18  ? 91   SER A N   1 
ATOM   710  C CA  . SER A 1 90  ? -71.618 28.985 -36.662 1.00 31.32  ? 91   SER A CA  1 
ATOM   711  C C   . SER A 1 90  ? -71.117 30.182 -35.871 1.00 30.14  ? 91   SER A C   1 
ATOM   712  O O   . SER A 1 90  ? -70.063 30.120 -35.264 1.00 28.45  ? 91   SER A O   1 
ATOM   713  C CB  . SER A 1 90  ? -72.384 28.057 -35.699 1.00 29.94  ? 91   SER A CB  1 
ATOM   714  O OG  . SER A 1 90  ? -73.493 28.691 -35.094 1.00 30.38  ? 91   SER A OG  1 
ATOM   715  N N   . GLU A 1 91  ? -71.917 31.242 -35.809 1.00 34.88  ? 92   GLU A N   1 
ATOM   716  C CA  . GLU A 1 91  ? -71.686 32.328 -34.834 1.00 32.66  ? 92   GLU A CA  1 
ATOM   717  C C   . GLU A 1 91  ? -71.713 31.837 -33.377 1.00 32.59  ? 92   GLU A C   1 
ATOM   718  O O   . GLU A 1 91  ? -71.122 32.452 -32.481 1.00 33.62  ? 92   GLU A O   1 
ATOM   719  C CB  . GLU A 1 91  ? -72.692 33.455 -35.042 1.00 30.21  ? 92   GLU A CB  1 
ATOM   720  C CG  . GLU A 1 91  ? -72.285 34.309 -36.219 1.00 30.34  ? 92   GLU A CG  1 
ATOM   721  C CD  . GLU A 1 91  ? -73.061 35.570 -36.370 1.00 33.31  ? 92   GLU A CD  1 
ATOM   722  O OE1 . GLU A 1 91  ? -72.557 36.621 -35.904 1.00 33.90  ? 92   GLU A OE1 1 
ATOM   723  O OE2 . GLU A 1 91  ? -74.167 35.502 -36.996 1.00 37.13  ? 92   GLU A OE2 1 
ATOM   724  N N   . ASP A 1 92  ? -72.395 30.725 -33.152 1.00 32.99  ? 93   ASP A N   1 
ATOM   725  C CA  . ASP A 1 92  ? -72.461 30.101 -31.844 1.00 35.89  ? 93   ASP A CA  1 
ATOM   726  C C   . ASP A 1 92  ? -71.331 29.145 -31.750 1.00 31.62  ? 93   ASP A C   1 
ATOM   727  O O   . ASP A 1 92  ? -71.460 27.954 -32.099 1.00 36.23  ? 93   ASP A O   1 
ATOM   728  C CB  . ASP A 1 92  ? -73.800 29.377 -31.690 1.00 38.53  ? 93   ASP A CB  1 
ATOM   729  C CG  . ASP A 1 92  ? -73.945 28.646 -30.354 1.00 36.21  ? 93   ASP A CG  1 
ATOM   730  O OD1 . ASP A 1 92  ? -73.033 28.546 -29.481 1.00 36.03  ? 93   ASP A OD1 1 
ATOM   731  O OD2 . ASP A 1 92  ? -75.039 28.129 -30.227 1.00 37.93  ? 93   ASP A OD2 1 
ATOM   732  N N   . CYS A 1 93  ? -70.208 29.668 -31.277 1.00 29.53  ? 94   CYS A N   1 
ATOM   733  C CA  . CYS A 1 93  ? -68.954 28.938 -31.342 1.00 30.51  ? 94   CYS A CA  1 
ATOM   734  C C   . CYS A 1 93  ? -68.055 29.123 -30.183 1.00 31.55  ? 94   CYS A C   1 
ATOM   735  O O   . CYS A 1 93  ? -66.871 28.674 -30.254 1.00 29.25  ? 94   CYS A O   1 
ATOM   736  C CB  . CYS A 1 93  ? -68.145 29.364 -32.590 1.00 31.42  ? 94   CYS A CB  1 
ATOM   737  S SG  . CYS A 1 93  ? -67.759 31.117 -32.703 1.00 33.01  ? 94   CYS A SG  1 
ATOM   738  N N   . LEU A 1 94  ? -68.554 29.755 -29.115 1.00 29.99  ? 95   LEU A N   1 
ATOM   739  C CA  . LEU A 1 94  ? -67.654 29.971 -27.977 1.00 29.45  ? 95   LEU A CA  1 
ATOM   740  C C   . LEU A 1 94  ? -67.680 28.817 -26.980 1.00 29.96  ? 95   LEU A C   1 
ATOM   741  O O   . LEU A 1 94  ? -68.453 28.843 -26.021 1.00 28.64  ? 95   LEU A O   1 
ATOM   742  C CB  . LEU A 1 94  ? -67.962 31.277 -27.350 1.00 31.28  ? 95   LEU A CB  1 
ATOM   743  C CG  . LEU A 1 94  ? -67.779 32.449 -28.304 1.00 32.23  ? 95   LEU A CG  1 
ATOM   744  C CD1 . LEU A 1 94  ? -68.049 33.748 -27.575 1.00 33.39  ? 95   LEU A CD1 1 
ATOM   745  C CD2 . LEU A 1 94  ? -66.372 32.497 -28.924 1.00 32.75  ? 95   LEU A CD2 1 
ATOM   746  N N   . TYR A 1 95  ? -66.794 27.838 -27.227 1.00 26.76  ? 96   TYR A N   1 
ATOM   747  C CA  . TYR A 1 95  ? -66.688 26.600 -26.485 1.00 25.12  ? 96   TYR A CA  1 
ATOM   748  C C   . TYR A 1 95  ? -65.241 26.286 -26.260 1.00 26.65  ? 96   TYR A C   1 
ATOM   749  O O   . TYR A 1 95  ? -64.353 26.809 -26.943 1.00 26.41  ? 96   TYR A O   1 
ATOM   750  C CB  . TYR A 1 95  ? -67.337 25.420 -27.277 1.00 29.36  ? 96   TYR A CB  1 
ATOM   751  C CG  . TYR A 1 95  ? -68.813 25.644 -27.538 1.00 29.27  ? 96   TYR A CG  1 
ATOM   752  C CD1 . TYR A 1 95  ? -69.231 26.452 -28.560 1.00 29.90  ? 96   TYR A CD1 1 
ATOM   753  C CD2 . TYR A 1 95  ? -69.767 25.118 -26.704 1.00 30.07  ? 96   TYR A CD2 1 
ATOM   754  C CE1 . TYR A 1 95  ? -70.582 26.720 -28.772 1.00 30.03  ? 96   TYR A CE1 1 
ATOM   755  C CE2 . TYR A 1 95  ? -71.118 25.372 -26.906 1.00 30.53  ? 96   TYR A CE2 1 
ATOM   756  C CZ  . TYR A 1 95  ? -71.505 26.172 -27.922 1.00 30.93  ? 96   TYR A CZ  1 
ATOM   757  O OH  . TYR A 1 95  ? -72.795 26.484 -28.049 1.00 30.04  ? 96   TYR A OH  1 
ATOM   758  N N   . LEU A 1 96  ? -64.977 25.421 -25.291 1.00 27.41  ? 97   LEU A N   1 
ATOM   759  C CA  . LEU A 1 96  ? -63.645 24.951 -25.086 1.00 27.00  ? 97   LEU A CA  1 
ATOM   760  C C   . LEU A 1 96  ? -63.657 23.435 -24.924 1.00 25.25  ? 97   LEU A C   1 
ATOM   761  O O   . LEU A 1 96  ? -64.722 22.859 -24.733 1.00 28.53  ? 97   LEU A O   1 
ATOM   762  C CB  . LEU A 1 96  ? -63.061 25.679 -23.893 1.00 30.25  ? 97   LEU A CB  1 
ATOM   763  C CG  . LEU A 1 96  ? -63.770 25.672 -22.519 1.00 33.78  ? 97   LEU A CG  1 
ATOM   764  C CD1 . LEU A 1 96  ? -63.552 24.369 -21.771 1.00 30.52  ? 97   LEU A CD1 1 
ATOM   765  C CD2 . LEU A 1 96  ? -63.173 26.812 -21.697 1.00 33.18  ? 97   LEU A CD2 1 
ATOM   766  N N   . ASN A 1 97  ? -62.474 22.833 -24.968 1.00 24.99  ? 98   ASN A N   1 
ATOM   767  C CA  . ASN A 1 97  ? -62.215 21.400 -24.936 1.00 26.76  ? 98   ASN A CA  1 
ATOM   768  C C   . ASN A 1 97  ? -61.142 21.076 -23.912 1.00 27.07  ? 98   ASN A C   1 
ATOM   769  O O   . ASN A 1 97  ? -60.179 21.815 -23.807 1.00 26.87  ? 98   ASN A O   1 
ATOM   770  C CB  . ASN A 1 97  ? -61.755 20.875 -26.326 1.00 28.23  ? 98   ASN A CB  1 
ATOM   771  C CG  . ASN A 1 97  ? -62.632 21.413 -27.459 1.00 29.26  ? 98   ASN A CG  1 
ATOM   772  O OD1 . ASN A 1 97  ? -63.832 21.149 -27.526 1.00 32.49  ? 98   ASN A OD1 1 
ATOM   773  N ND2 . ASN A 1 97  ? -62.054 22.253 -28.289 1.00 31.42  ? 98   ASN A ND2 1 
ATOM   774  N N   . ILE A 1 98  ? -61.308 19.953 -23.199 1.00 27.55  ? 99   ILE A N   1 
ATOM   775  C CA  . ILE A 1 98  ? -60.384 19.549 -22.113 1.00 32.80  ? 99   ILE A CA  1 
ATOM   776  C C   . ILE A 1 98  ? -60.071 18.077 -22.188 1.00 30.45  ? 99   ILE A C   1 
ATOM   777  O O   . ILE A 1 98  ? -60.966 17.275 -22.221 1.00 34.54  ? 99   ILE A O   1 
ATOM   778  C CB  . ILE A 1 98  ? -60.951 19.787 -20.674 1.00 31.58  ? 99   ILE A CB  1 
ATOM   779  C CG1 . ILE A 1 98  ? -61.615 21.183 -20.563 1.00 36.81  ? 99   ILE A CG1 1 
ATOM   780  C CG2 . ILE A 1 98  ? -59.788 19.743 -19.703 1.00 34.09  ? 99   ILE A CG2 1 
ATOM   781  C CD1 . ILE A 1 98  ? -62.275 21.575 -19.228 1.00 38.06  ? 99   ILE A CD1 1 
ATOM   782  N N   . TRP A 1 99  ? -58.809 17.754 -22.199 1.00 29.49  ? 100  TRP A N   1 
ATOM   783  C CA  . TRP A 1 99  ? -58.342 16.400 -22.160 1.00 35.47  ? 100  TRP A CA  1 
ATOM   784  C C   . TRP A 1 99  ? -57.702 16.232 -20.789 1.00 38.12  ? 100  TRP A C   1 
ATOM   785  O O   . TRP A 1 99  ? -56.872 17.052 -20.403 1.00 37.17  ? 100  TRP A O   1 
ATOM   786  C CB  . TRP A 1 99  ? -57.309 16.087 -23.241 1.00 36.24  ? 100  TRP A CB  1 
ATOM   787  C CG  . TRP A 1 99  ? -57.930 15.998 -24.628 1.00 37.25  ? 100  TRP A CG  1 
ATOM   788  C CD1 . TRP A 1 99  ? -58.361 14.880 -25.250 1.00 41.26  ? 100  TRP A CD1 1 
ATOM   789  C CD2 . TRP A 1 99  ? -58.169 17.075 -25.548 1.00 36.52  ? 100  TRP A CD2 1 
ATOM   790  N NE1 . TRP A 1 99  ? -58.909 15.181 -26.481 1.00 38.08  ? 100  TRP A NE1 1 
ATOM   791  C CE2 . TRP A 1 99  ? -58.751 16.512 -26.712 1.00 36.54  ? 100  TRP A CE2 1 
ATOM   792  C CE3 . TRP A 1 99  ? -57.930 18.451 -25.516 1.00 37.34  ? 100  TRP A CE3 1 
ATOM   793  C CZ2 . TRP A 1 99  ? -59.107 17.278 -27.831 1.00 37.63  ? 100  TRP A CZ2 1 
ATOM   794  C CZ3 . TRP A 1 99  ? -58.301 19.232 -26.669 1.00 37.23  ? 100  TRP A CZ3 1 
ATOM   795  C CH2 . TRP A 1 99  ? -58.869 18.631 -27.788 1.00 32.66  ? 100  TRP A CH2 1 
ATOM   796  N N   . VAL A 1 100 ? -58.165 15.197 -20.074 1.00 34.24  ? 101  VAL A N   1 
ATOM   797  C CA  . VAL A 1 100 ? -57.837 14.952 -18.666 1.00 37.85  ? 101  VAL A CA  1 
ATOM   798  C C   . VAL A 1 100 ? -57.328 13.499 -18.528 1.00 33.40  ? 101  VAL A C   1 
ATOM   799  O O   . VAL A 1 100 ? -58.052 12.558 -18.906 1.00 33.61  ? 101  VAL A O   1 
ATOM   800  C CB  . VAL A 1 100 ? -59.114 15.091 -17.797 1.00 37.39  ? 101  VAL A CB  1 
ATOM   801  C CG1 . VAL A 1 100 ? -58.827 14.800 -16.332 1.00 36.98  ? 101  VAL A CG1 1 
ATOM   802  C CG2 . VAL A 1 100 ? -59.783 16.451 -18.020 1.00 39.13  ? 101  VAL A CG2 1 
ATOM   803  N N   . PRO A 1 101 ? -56.114 13.327 -18.025 1.00 29.98  ? 102  PRO A N   1 
ATOM   804  C CA  . PRO A 1 101 ? -55.627 11.981 -17.734 1.00 33.64  ? 102  PRO A CA  1 
ATOM   805  C C   . PRO A 1 101 ? -56.598 11.087 -16.929 1.00 39.44  ? 102  PRO A C   1 
ATOM   806  O O   . PRO A 1 101 ? -57.536 11.583 -16.223 1.00 34.73  ? 102  PRO A O   1 
ATOM   807  C CB  . PRO A 1 101 ? -54.376 12.214 -16.916 1.00 29.82  ? 102  PRO A CB  1 
ATOM   808  C CG  . PRO A 1 101 ? -53.903 13.602 -17.349 1.00 30.77  ? 102  PRO A CG  1 
ATOM   809  C CD  . PRO A 1 101 ? -55.175 14.371 -17.553 1.00 30.88  ? 102  PRO A CD  1 
ATOM   810  N N   . SER A 1 102 ? -56.403 9.779  -17.103 1.00 41.50  ? 103  SER A N   1 
ATOM   811  C CA  . SER A 1 102 ? -57.202 8.750  -16.431 1.00 49.09  ? 103  SER A CA  1 
ATOM   812  C C   . SER A 1 102 ? -56.235 7.852  -15.745 1.00 47.11  ? 103  SER A C   1 
ATOM   813  O O   . SER A 1 102 ? -55.382 7.269  -16.380 1.00 48.67  ? 103  SER A O   1 
ATOM   814  C CB  . SER A 1 102 ? -58.032 7.942  -17.402 1.00 52.01  ? 103  SER A CB  1 
ATOM   815  O OG  . SER A 1 102 ? -59.151 7.393  -16.747 1.00 54.10  ? 103  SER A OG  1 
ATOM   816  N N   . PRO A 1 103 ? -56.346 7.733  -14.436 1.00 53.67  ? 104  PRO A N   1 
ATOM   817  C CA  . PRO A 1 103 ? -57.412 8.337  -13.663 1.00 54.85  ? 104  PRO A CA  1 
ATOM   818  C C   . PRO A 1 103 ? -57.213 9.863  -13.494 1.00 44.16  ? 104  PRO A C   1 
ATOM   819  O O   . PRO A 1 103 ? -56.078 10.371 -13.569 1.00 32.27  ? 104  PRO A O   1 
ATOM   820  C CB  . PRO A 1 103 ? -57.305 7.609  -12.295 1.00 54.18  ? 104  PRO A CB  1 
ATOM   821  C CG  . PRO A 1 103 ? -55.843 7.325  -12.173 1.00 57.78  ? 104  PRO A CG  1 
ATOM   822  C CD  . PRO A 1 103 ? -55.348 7.058  -13.581 1.00 57.38  ? 104  PRO A CD  1 
ATOM   823  N N   . ARG A 1 104 ? -58.325 10.551 -13.230 1.00 41.32  ? 105  ARG A N   1 
ATOM   824  C CA  . ARG A 1 104 ? -58.329 12.011 -12.985 1.00 42.63  ? 105  ARG A CA  1 
ATOM   825  C C   . ARG A 1 104 ? -57.302 12.428 -11.968 1.00 44.25  ? 105  ARG A C   1 
ATOM   826  O O   . ARG A 1 104 ? -57.267 11.889 -10.875 1.00 48.21  ? 105  ARG A O   1 
ATOM   827  C CB  . ARG A 1 104 ? -59.685 12.464 -12.524 1.00 37.11  ? 105  ARG A CB  1 
ATOM   828  C CG  . ARG A 1 104 ? -59.832 13.955 -12.586 1.00 38.14  ? 105  ARG A CG  1 
ATOM   829  C CD  . ARG A 1 104 ? -61.148 14.382 -11.981 1.00 33.52  ? 105  ARG A CD  1 
ATOM   830  N NE  . ARG A 1 104 ? -62.278 13.811 -12.670 1.00 36.28  ? 105  ARG A NE  1 
ATOM   831  C CZ  . ARG A 1 104 ? -63.534 13.980 -12.282 1.00 36.60  ? 105  ARG A CZ  1 
ATOM   832  N NH1 . ARG A 1 104 ? -63.758 14.631 -11.172 1.00 36.76  ? 105  ARG A NH1 1 
ATOM   833  N NH2 . ARG A 1 104 ? -64.584 13.461 -12.944 1.00 34.89  ? 105  ARG A NH2 1 
ATOM   834  N N   . PRO A 1 105 ? -56.421 13.356 -12.340 1.00 43.88  ? 106  PRO A N   1 
ATOM   835  C CA  . PRO A 1 105 ? -55.455 13.899 -11.389 1.00 40.50  ? 106  PRO A CA  1 
ATOM   836  C C   . PRO A 1 105 ? -56.131 14.761 -10.312 1.00 35.77  ? 106  PRO A C   1 
ATOM   837  O O   . PRO A 1 105 ? -57.326 15.006 -10.373 1.00 42.63  ? 106  PRO A O   1 
ATOM   838  C CB  . PRO A 1 105 ? -54.532 14.740 -12.274 1.00 43.39  ? 106  PRO A CB  1 
ATOM   839  C CG  . PRO A 1 105 ? -55.324 15.074 -13.455 1.00 45.93  ? 106  PRO A CG  1 
ATOM   840  C CD  . PRO A 1 105 ? -56.350 14.009 -13.656 1.00 47.98  ? 106  PRO A CD  1 
ATOM   841  N N   . LYS A 1 106 ? -55.385 15.277 -9.361  1.00 42.14  ? 107  LYS A N   1 
ATOM   842  C CA  . LYS A 1 106 ? -56.028 16.149 -8.349  1.00 47.23  ? 107  LYS A CA  1 
ATOM   843  C C   . LYS A 1 106 ? -55.699 17.595 -8.560  1.00 44.59  ? 107  LYS A C   1 
ATOM   844  O O   . LYS A 1 106 ? -56.536 18.471 -8.355  1.00 45.00  ? 107  LYS A O   1 
ATOM   845  C CB  . LYS A 1 106 ? -55.626 15.737 -6.921  1.00 50.22  ? 107  LYS A CB  1 
ATOM   846  C CG  . LYS A 1 106 ? -55.777 14.236 -6.610  1.00 52.95  ? 107  LYS A CG  1 
ATOM   847  C CD  . LYS A 1 106 ? -57.225 13.742 -6.748  1.00 61.03  ? 107  LYS A CD  1 
ATOM   848  C CE  . LYS A 1 106 ? -57.268 12.198 -6.771  1.00 63.86  ? 107  LYS A CE  1 
ATOM   849  N NZ  . LYS A 1 106 ? -58.625 11.645 -6.510  1.00 63.64  ? 107  LYS A NZ  1 
ATOM   850  N N   . SER A 1 107 ? -54.446 17.853 -8.885  1.00 41.53  ? 108  SER A N   1 
ATOM   851  C CA  . SER A 1 107 ? -54.029 19.235 -9.022  1.00 48.75  ? 108  SER A CA  1 
ATOM   852  C C   . SER A 1 107 ? -52.854 19.303 -9.957  1.00 41.15  ? 108  SER A C   1 
ATOM   853  O O   . SER A 1 107 ? -51.745 19.516 -9.531  1.00 44.62  ? 108  SER A O   1 
ATOM   854  C CB  . SER A 1 107 ? -53.643 19.827 -7.682  1.00 45.26  ? 108  SER A CB  1 
ATOM   855  O OG  . SER A 1 107 ? -53.717 21.220 -7.771  1.00 50.54  ? 108  SER A OG  1 
ATOM   856  N N   . THR A 1 108 ? -53.106 19.086 -11.235 1.00 36.07  ? 109  THR A N   1 
ATOM   857  C CA  . THR A 1 108 ? -51.994 19.010 -12.157 1.00 36.21  ? 109  THR A CA  1 
ATOM   858  C C   . THR A 1 108 ? -51.809 20.278 -13.077 1.00 32.52  ? 109  THR A C   1 
ATOM   859  O O   . THR A 1 108 ? -52.728 21.122 -13.270 1.00 27.58  ? 109  THR A O   1 
ATOM   860  C CB  . THR A 1 108 ? -51.974 17.685 -12.922 1.00 33.79  ? 109  THR A CB  1 
ATOM   861  O OG1 . THR A 1 108 ? -50.662 17.536 -13.488 1.00 45.32  ? 109  THR A OG1 1 
ATOM   862  C CG2 . THR A 1 108 ? -52.972 17.682 -14.012 1.00 35.79  ? 109  THR A CG2 1 
ATOM   863  N N   . THR A 1 109 ? -50.597 20.386 -13.599 1.00 30.75  ? 110  THR A N   1 
ATOM   864  C CA  . THR A 1 109 ? -50.263 21.397 -14.587 1.00 31.24  ? 110  THR A CA  1 
ATOM   865  C C   . THR A 1 109 ? -51.295 21.445 -15.705 1.00 28.74  ? 110  THR A C   1 
ATOM   866  O O   . THR A 1 109 ? -51.779 20.424 -16.189 1.00 33.03  ? 110  THR A O   1 
ATOM   867  C CB  . THR A 1 109 ? -48.890 21.172 -15.182 1.00 34.72  ? 110  THR A CB  1 
ATOM   868  O OG1 . THR A 1 109 ? -47.920 21.078 -14.143 1.00 35.32  ? 110  THR A OG1 1 
ATOM   869  C CG2 . THR A 1 109 ? -48.539 22.330 -16.094 1.00 37.25  ? 110  THR A CG2 1 
ATOM   870  N N   . VAL A 1 110 ? -51.690 22.657 -16.043 1.00 28.97  ? 111  VAL A N   1 
ATOM   871  C CA  . VAL A 1 110 ? -52.726 22.930 -17.059 1.00 30.33  ? 111  VAL A CA  1 
ATOM   872  C C   . VAL A 1 110 ? -52.058 23.738 -18.243 1.00 30.18  ? 111  VAL A C   1 
ATOM   873  O O   . VAL A 1 110 ? -51.313 24.710 -18.007 1.00 28.95  ? 111  VAL A O   1 
ATOM   874  C CB  . VAL A 1 110 ? -53.826 23.782 -16.429 1.00 29.81  ? 111  VAL A CB  1 
ATOM   875  C CG1 . VAL A 1 110 ? -54.947 24.103 -17.412 1.00 32.75  ? 111  VAL A CG1 1 
ATOM   876  C CG2 . VAL A 1 110 ? -54.372 23.135 -15.157 1.00 29.25  ? 111  VAL A CG2 1 
ATOM   877  N N   . MET A 1 111 ? -52.342 23.334 -19.481 1.00 29.18  ? 112  MET A N   1 
ATOM   878  C CA  . MET A 1 111 ? -51.876 24.045 -20.683 1.00 27.02  ? 112  MET A CA  1 
ATOM   879  C C   . MET A 1 111 ? -53.089 24.438 -21.484 1.00 29.10  ? 112  MET A C   1 
ATOM   880  O O   . MET A 1 111 ? -54.013 23.623 -21.650 1.00 31.91  ? 112  MET A O   1 
ATOM   881  C CB  . MET A 1 111 ? -50.962 23.169 -21.476 1.00 28.43  ? 112  MET A CB  1 
ATOM   882  C CG  . MET A 1 111 ? -49.634 22.931 -20.770 1.00 27.11  ? 112  MET A CG  1 
ATOM   883  S SD  . MET A 1 111 ? -48.452 21.880 -21.649 1.00 32.71  ? 112  MET A SD  1 
ATOM   884  C CE  . MET A 1 111 ? -47.872 23.137 -22.782 1.00 30.88  ? 112  MET A CE  1 
ATOM   885  N N   . VAL A 1 112 ? -53.163 25.714 -21.871 1.00 25.91  ? 113  VAL A N   1 
ATOM   886  C CA  . VAL A 1 112 ? -54.314 26.210 -22.571 1.00 25.62  ? 113  VAL A CA  1 
ATOM   887  C C   . VAL A 1 112 ? -53.827 26.726 -23.927 1.00 25.78  ? 113  VAL A C   1 
ATOM   888  O O   . VAL A 1 112 ? -53.061 27.658 -23.973 1.00 23.83  ? 113  VAL A O   1 
ATOM   889  C CB  . VAL A 1 112 ? -55.024 27.374 -21.846 1.00 23.67  ? 113  VAL A CB  1 
ATOM   890  C CG1 . VAL A 1 112 ? -56.266 27.839 -22.642 1.00 24.74  ? 113  VAL A CG1 1 
ATOM   891  C CG2 . VAL A 1 112 ? -55.474 26.936 -20.508 1.00 24.79  ? 113  VAL A CG2 1 
ATOM   892  N N   . TRP A 1 113 ? -54.358 26.130 -24.988 1.00 27.60  ? 114  TRP A N   1 
ATOM   893  C CA  . TRP A 1 113 ? -53.930 26.334 -26.377 1.00 26.38  ? 114  TRP A CA  1 
ATOM   894  C C   . TRP A 1 113 ? -54.811 27.390 -27.022 1.00 25.37  ? 114  TRP A C   1 
ATOM   895  O O   . TRP A 1 113 ? -56.033 27.328 -26.963 1.00 22.58  ? 114  TRP A O   1 
ATOM   896  C CB  . TRP A 1 113 ? -54.019 25.006 -27.160 1.00 27.71  ? 114  TRP A CB  1 
ATOM   897  C CG  . TRP A 1 113 ? -53.803 25.159 -28.642 1.00 27.24  ? 114  TRP A CG  1 
ATOM   898  C CD1 . TRP A 1 113 ? -54.731 25.023 -29.633 1.00 29.20  ? 114  TRP A CD1 1 
ATOM   899  C CD2 . TRP A 1 113 ? -52.586 25.504 -29.264 1.00 25.25  ? 114  TRP A CD2 1 
ATOM   900  N NE1 . TRP A 1 113 ? -54.132 25.237 -30.887 1.00 30.60  ? 114  TRP A NE1 1 
ATOM   901  C CE2 . TRP A 1 113 ? -52.823 25.567 -30.663 1.00 28.07  ? 114  TRP A CE2 1 
ATOM   902  C CE3 . TRP A 1 113 ? -51.299 25.741 -28.777 1.00 26.35  ? 114  TRP A CE3 1 
ATOM   903  C CZ2 . TRP A 1 113 ? -51.831 25.866 -31.560 1.00 28.58  ? 114  TRP A CZ2 1 
ATOM   904  C CZ3 . TRP A 1 113 ? -50.318 26.035 -29.644 1.00 28.98  ? 114  TRP A CZ3 1 
ATOM   905  C CH2 . TRP A 1 113 ? -50.566 26.100 -31.042 1.00 29.18  ? 114  TRP A CH2 1 
ATOM   906  N N   . ILE A 1 114 ? -54.176 28.402 -27.593 1.00 26.45  ? 115  ILE A N   1 
ATOM   907  C CA  . ILE A 1 114 ? -54.907 29.432 -28.364 1.00 23.48  ? 115  ILE A CA  1 
ATOM   908  C C   . ILE A 1 114 ? -54.537 29.329 -29.861 1.00 23.18  ? 115  ILE A C   1 
ATOM   909  O O   . ILE A 1 114 ? -53.424 29.593 -30.274 1.00 18.93  ? 115  ILE A O   1 
ATOM   910  C CB  . ILE A 1 114 ? -54.523 30.821 -27.853 1.00 25.05  ? 115  ILE A CB  1 
ATOM   911  C CG1 . ILE A 1 114 ? -54.831 30.912 -26.325 1.00 24.97  ? 115  ILE A CG1 1 
ATOM   912  C CG2 . ILE A 1 114 ? -55.303 31.872 -28.661 1.00 23.65  ? 115  ILE A CG2 1 
ATOM   913  C CD1 . ILE A 1 114 ? -54.423 32.222 -25.692 1.00 25.24  ? 115  ILE A CD1 1 
ATOM   914  N N   . TYR A 1 115 ? -55.500 28.936 -30.686 1.00 26.86  ? 116  TYR A N   1 
ATOM   915  C CA  . TYR A 1 115 ? -55.217 28.760 -32.106 1.00 25.79  ? 116  TYR A CA  1 
ATOM   916  C C   . TYR A 1 115 ? -54.803 30.031 -32.833 1.00 26.76  ? 116  TYR A C   1 
ATOM   917  O O   . TYR A 1 115 ? -55.236 31.141 -32.483 1.00 24.66  ? 116  TYR A O   1 
ATOM   918  C CB  . TYR A 1 115 ? -56.343 28.040 -32.814 1.00 23.52  ? 116  TYR A CB  1 
ATOM   919  C CG  . TYR A 1 115 ? -57.655 28.652 -32.796 1.00 22.51  ? 116  TYR A CG  1 
ATOM   920  C CD1 . TYR A 1 115 ? -57.919 29.793 -33.517 1.00 23.31  ? 116  TYR A CD1 1 
ATOM   921  C CD2 . TYR A 1 115 ? -58.697 28.061 -32.141 1.00 22.73  ? 116  TYR A CD2 1 
ATOM   922  C CE1 . TYR A 1 115 ? -59.172 30.325 -33.564 1.00 20.64  ? 116  TYR A CE1 1 
ATOM   923  C CE2 . TYR A 1 115 ? -59.985 28.624 -32.187 1.00 19.62  ? 116  TYR A CE2 1 
ATOM   924  C CZ  . TYR A 1 115 ? -60.201 29.742 -32.874 1.00 20.12  ? 116  TYR A CZ  1 
ATOM   925  O OH  . TYR A 1 115 ? -61.462 30.368 -32.869 1.00 20.81  ? 116  TYR A OH  1 
ATOM   926  N N   . GLY A 1 116 ? -53.918 29.824 -33.830 1.00 29.74  ? 117  GLY A N   1 
ATOM   927  C CA  . GLY A 1 116 ? -53.556 30.868 -34.811 1.00 26.28  ? 117  GLY A CA  1 
ATOM   928  C C   . GLY A 1 116 ? -54.529 30.882 -35.986 1.00 24.44  ? 117  GLY A C   1 
ATOM   929  O O   . GLY A 1 116 ? -55.602 30.216 -35.974 1.00 27.20  ? 117  GLY A O   1 
ATOM   930  N N   . GLY A 1 117 ? -54.164 31.625 -37.022 1.00 24.26  ? 118  GLY A N   1 
ATOM   931  C CA  . GLY A 1 117 ? -55.025 31.794 -38.226 1.00 23.27  ? 118  GLY A CA  1 
ATOM   932  C C   . GLY A 1 117 ? -55.227 33.265 -38.585 1.00 25.40  ? 118  GLY A C   1 
ATOM   933  O O   . GLY A 1 117 ? -56.272 33.640 -39.105 1.00 25.76  ? 118  GLY A O   1 
ATOM   934  N N   . GLY A 1 118 ? -54.259 34.119 -38.257 1.00 24.13  ? 119  GLY A N   1 
ATOM   935  C CA  . GLY A 1 118 ? -54.294 35.536 -38.677 1.00 25.31  ? 119  GLY A CA  1 
ATOM   936  C C   . GLY A 1 118 ? -55.397 36.406 -38.114 1.00 24.97  ? 119  GLY A C   1 
ATOM   937  O O   . GLY A 1 118 ? -55.640 37.518 -38.580 1.00 23.88  ? 119  GLY A O   1 
ATOM   938  N N   . PHE A 1 119 ? -56.087 35.868 -37.131 1.00 24.96  ? 120  PHE A N   1 
ATOM   939  C CA  . PHE A 1 119 ? -57.262 36.533 -36.513 1.00 24.33  ? 120  PHE A CA  1 
ATOM   940  C C   . PHE A 1 119 ? -58.437 36.566 -37.455 1.00 26.34  ? 120  PHE A C   1 
ATOM   941  O O   . PHE A 1 119 ? -59.486 37.153 -37.084 1.00 24.82  ? 120  PHE A O   1 
ATOM   942  C CB  . PHE A 1 119 ? -56.993 37.957 -36.069 1.00 23.39  ? 120  PHE A CB  1 
ATOM   943  C CG  . PHE A 1 119 ? -55.961 38.082 -35.014 1.00 22.83  ? 120  PHE A CG  1 
ATOM   944  C CD1 . PHE A 1 119 ? -56.221 37.640 -33.725 1.00 22.45  ? 120  PHE A CD1 1 
ATOM   945  C CD2 . PHE A 1 119 ? -54.766 38.702 -35.284 1.00 23.08  ? 120  PHE A CD2 1 
ATOM   946  C CE1 . PHE A 1 119 ? -55.300 37.808 -32.725 1.00 23.63  ? 120  PHE A CE1 1 
ATOM   947  C CE2 . PHE A 1 119 ? -53.802 38.831 -34.293 1.00 23.73  ? 120  PHE A CE2 1 
ATOM   948  C CZ  . PHE A 1 119 ? -54.093 38.417 -33.009 1.00 24.21  ? 120  PHE A CZ  1 
ATOM   949  N N   . TYR A 1 120 ? -58.285 35.935 -38.637 1.00 25.72  ? 121  TYR A N   1 
ATOM   950  C CA  . TYR A 1 120 ? -59.441 35.779 -39.592 1.00 26.48  ? 121  TYR A CA  1 
ATOM   951  C C   . TYR A 1 120 ? -59.959 34.366 -39.744 1.00 27.12  ? 121  TYR A C   1 
ATOM   952  O O   . TYR A 1 120 ? -61.022 34.146 -40.384 1.00 27.76  ? 121  TYR A O   1 
ATOM   953  C CB  . TYR A 1 120 ? -59.071 36.280 -40.997 1.00 23.38  ? 121  TYR A CB  1 
ATOM   954  C CG  . TYR A 1 120 ? -58.089 35.444 -41.714 1.00 21.18  ? 121  TYR A CG  1 
ATOM   955  C CD1 . TYR A 1 120 ? -58.495 34.348 -42.480 1.00 24.76  ? 121  TYR A CD1 1 
ATOM   956  C CD2 . TYR A 1 120 ? -56.722 35.701 -41.602 1.00 23.54  ? 121  TYR A CD2 1 
ATOM   957  C CE1 . TYR A 1 120 ? -57.555 33.528 -43.164 1.00 25.17  ? 121  TYR A CE1 1 
ATOM   958  C CE2 . TYR A 1 120 ? -55.768 34.929 -42.258 1.00 24.10  ? 121  TYR A CE2 1 
ATOM   959  C CZ  . TYR A 1 120 ? -56.195 33.814 -43.056 1.00 28.54  ? 121  TYR A CZ  1 
ATOM   960  O OH  . TYR A 1 120 ? -55.248 33.001 -43.723 1.00 29.88  ? 121  TYR A OH  1 
ATOM   961  N N   . SER A 1 121 ? -59.220 33.416 -39.171 1.00 23.77  ? 122  SER A N   1 
ATOM   962  C CA  . SER A 1 121 ? -59.567 32.028 -39.287 1.00 25.78  ? 122  SER A CA  1 
ATOM   963  C C   . SER A 1 121 ? -59.034 31.273 -38.062 1.00 25.42  ? 122  SER A C   1 
ATOM   964  O O   . SER A 1 121 ? -58.335 31.863 -37.224 1.00 24.75  ? 122  SER A O   1 
ATOM   965  C CB  . SER A 1 121 ? -58.906 31.451 -40.545 1.00 24.22  ? 122  SER A CB  1 
ATOM   966  O OG  . SER A 1 121 ? -57.506 31.529 -40.414 1.00 23.22  ? 122  SER A OG  1 
ATOM   967  N N   . GLY A 1 122 ? -59.310 29.971 -38.034 1.00 24.00  ? 123  GLY A N   1 
ATOM   968  C CA  . GLY A 1 122 ? -58.792 29.060 -37.008 1.00 28.52  ? 123  GLY A CA  1 
ATOM   969  C C   . GLY A 1 122 ? -59.885 28.289 -36.264 1.00 27.40  ? 123  GLY A C   1 
ATOM   970  O O   . GLY A 1 122 ? -61.018 28.744 -36.182 1.00 24.02  ? 123  GLY A O   1 
ATOM   971  N N   . SER A 1 123 ? -59.521 27.122 -35.727 1.00 26.33  ? 124  SER A N   1 
ATOM   972  C CA  . SER A 1 123 ? -60.448 26.198 -35.114 1.00 27.73  ? 124  SER A CA  1 
ATOM   973  C C   . SER A 1 123 ? -59.759 25.446 -33.985 1.00 27.00  ? 124  SER A C   1 
ATOM   974  O O   . SER A 1 123 ? -58.607 25.047 -34.094 1.00 28.63  ? 124  SER A O   1 
ATOM   975  C CB  . SER A 1 123 ? -60.934 25.174 -36.149 1.00 28.25  ? 124  SER A CB  1 
ATOM   976  O OG  . SER A 1 123 ? -61.761 25.820 -37.080 1.00 30.70  ? 124  SER A OG  1 
ATOM   977  N N   . SER A 1 124 ? -60.476 25.231 -32.897 1.00 29.36  ? 125  SER A N   1 
ATOM   978  C CA  . SER A 1 124 ? -59.950 24.461 -31.783 1.00 30.68  ? 125  SER A CA  1 
ATOM   979  C C   . SER A 1 124 ? -59.936 22.944 -32.028 1.00 30.09  ? 125  SER A C   1 
ATOM   980  O O   . SER A 1 124 ? -59.278 22.218 -31.290 1.00 32.82  ? 125  SER A O   1 
ATOM   981  C CB  . SER A 1 124 ? -60.765 24.736 -30.521 1.00 29.78  ? 125  SER A CB  1 
ATOM   982  O OG  . SER A 1 124 ? -62.030 24.111 -30.586 1.00 27.03  ? 125  SER A OG  1 
ATOM   983  N N   . THR A 1 125 ? -60.612 22.524 -33.080 1.00 30.04  ? 126  THR A N   1 
ATOM   984  C CA  . THR A 1 125 ? -61.027 21.133 -33.356 1.00 31.79  ? 126  THR A CA  1 
ATOM   985  C C   . THR A 1 125 ? -60.218 20.439 -34.424 1.00 31.91  ? 126  THR A C   1 
ATOM   986  O O   . THR A 1 125 ? -60.492 19.332 -34.783 1.00 33.01  ? 126  THR A O   1 
ATOM   987  C CB  . THR A 1 125 ? -62.484 21.109 -33.847 1.00 30.65  ? 126  THR A CB  1 
ATOM   988  O OG1 . THR A 1 125 ? -62.644 21.977 -34.970 1.00 26.99  ? 126  THR A OG1 1 
ATOM   989  C CG2 . THR A 1 125 ? -63.407 21.627 -32.783 1.00 33.08  ? 126  THR A CG2 1 
ATOM   990  N N   . LEU A 1 126 ? -59.163 21.073 -34.903 1.00 35.23  ? 127  LEU A N   1 
ATOM   991  C CA  . LEU A 1 126 ? -58.328 20.475 -35.911 1.00 31.73  ? 127  LEU A CA  1 
ATOM   992  C C   . LEU A 1 126 ? -57.589 19.236 -35.418 1.00 35.77  ? 127  LEU A C   1 
ATOM   993  O O   . LEU A 1 126 ? -57.202 19.117 -34.242 1.00 35.19  ? 127  LEU A O   1 
ATOM   994  C CB  . LEU A 1 126 ? -57.312 21.484 -36.421 1.00 30.57  ? 127  LEU A CB  1 
ATOM   995  C CG  . LEU A 1 126 ? -57.820 22.812 -36.970 1.00 31.40  ? 127  LEU A CG  1 
ATOM   996  C CD1 . LEU A 1 126 ? -56.620 23.609 -37.469 1.00 30.90  ? 127  LEU A CD1 1 
ATOM   997  C CD2 . LEU A 1 126 ? -58.869 22.595 -38.028 1.00 30.78  ? 127  LEU A CD2 1 
ATOM   998  N N   . ASP A 1 127 ? -57.311 18.351 -36.361 1.00 35.76  ? 128  ASP A N   1 
ATOM   999  C CA  . ASP A 1 127 ? -56.553 17.160 -36.048 1.00 36.27  ? 128  ASP A CA  1 
ATOM   1000 C C   . ASP A 1 127 ? -55.244 17.543 -35.414 1.00 33.58  ? 128  ASP A C   1 
ATOM   1001 O O   . ASP A 1 127 ? -54.859 16.921 -34.453 1.00 34.42  ? 128  ASP A O   1 
ATOM   1002 C CB  . ASP A 1 127 ? -56.376 16.255 -37.301 1.00 36.43  ? 128  ASP A CB  1 
ATOM   1003 C CG  . ASP A 1 127 ? -57.727 15.649 -37.808 1.00 43.79  ? 128  ASP A CG  1 
ATOM   1004 O OD1 . ASP A 1 127 ? -58.719 15.627 -37.054 1.00 43.32  ? 128  ASP A OD1 1 
ATOM   1005 O OD2 . ASP A 1 127 ? -57.825 15.212 -38.979 1.00 56.37  ? 128  ASP A OD2 1 
ATOM   1006 N N   . VAL A 1 128 ? -54.513 18.524 -35.949 1.00 33.92  ? 129  VAL A N   1 
ATOM   1007 C CA  . VAL A 1 128 ? -53.178 18.792 -35.384 1.00 32.21  ? 129  VAL A CA  1 
ATOM   1008 C C   . VAL A 1 128 ? -53.273 19.407 -33.980 1.00 29.64  ? 129  VAL A C   1 
ATOM   1009 O O   . VAL A 1 128 ? -52.255 19.620 -33.328 1.00 28.59  ? 129  VAL A O   1 
ATOM   1010 C CB  . VAL A 1 128 ? -52.350 19.863 -36.114 1.00 32.40  ? 129  VAL A CB  1 
ATOM   1011 C CG1 . VAL A 1 128 ? -51.310 19.272 -36.944 1.00 34.89  ? 129  VAL A CG1 1 
ATOM   1012 C CG2 . VAL A 1 128 ? -53.224 20.903 -36.814 1.00 35.06  ? 129  VAL A CG2 1 
ATOM   1013 N N   . TYR A 1 129 ? -54.452 19.842 -33.566 1.00 30.49  ? 130  TYR A N   1 
ATOM   1014 C CA  . TYR A 1 129 ? -54.583 20.420 -32.220 1.00 31.48  ? 130  TYR A CA  1 
ATOM   1015 C C   . TYR A 1 129 ? -55.212 19.433 -31.210 1.00 33.04  ? 130  TYR A C   1 
ATOM   1016 O O   . TYR A 1 129 ? -55.576 19.830 -30.104 1.00 38.04  ? 130  TYR A O   1 
ATOM   1017 C CB  . TYR A 1 129 ? -55.414 21.710 -32.237 1.00 30.03  ? 130  TYR A CB  1 
ATOM   1018 C CG  . TYR A 1 129 ? -54.962 22.851 -33.102 1.00 28.23  ? 130  TYR A CG  1 
ATOM   1019 C CD1 . TYR A 1 129 ? -53.661 23.045 -33.447 1.00 30.68  ? 130  TYR A CD1 1 
ATOM   1020 C CD2 . TYR A 1 129 ? -55.915 23.730 -33.610 1.00 30.77  ? 130  TYR A CD2 1 
ATOM   1021 C CE1 . TYR A 1 129 ? -53.296 24.096 -34.280 1.00 28.56  ? 130  TYR A CE1 1 
ATOM   1022 C CE2 . TYR A 1 129 ? -55.580 24.794 -34.376 1.00 27.85  ? 130  TYR A CE2 1 
ATOM   1023 C CZ  . TYR A 1 129 ? -54.284 24.974 -34.728 1.00 27.82  ? 130  TYR A CZ  1 
ATOM   1024 O OH  . TYR A 1 129 ? -54.006 26.063 -35.509 1.00 27.74  ? 130  TYR A OH  1 
ATOM   1025 N N   . ASN A 1 130 ? -55.309 18.153 -31.558 1.00 38.16  ? 131  ASN A N   1 
ATOM   1026 C CA  . ASN A 1 130 ? -55.863 17.134 -30.646 1.00 37.70  ? 131  ASN A CA  1 
ATOM   1027 C C   . ASN A 1 130 ? -55.019 17.002 -29.401 1.00 30.99  ? 131  ASN A C   1 
ATOM   1028 O O   . ASN A 1 130 ? -53.852 16.575 -29.434 1.00 28.00  ? 131  ASN A O   1 
ATOM   1029 C CB  . ASN A 1 130 ? -55.990 15.776 -31.339 1.00 41.01  ? 131  ASN A CB  1 
ATOM   1030 C CG  . ASN A 1 130 ? -56.851 14.799 -30.560 1.00 45.40  ? 131  ASN A CG  1 
ATOM   1031 O OD1 . ASN A 1 130 ? -56.968 14.837 -29.334 1.00 44.99  ? 131  ASN A OD1 1 
ATOM   1032 N ND2 . ASN A 1 130 ? -57.489 13.931 -31.287 1.00 51.57  ? 131  ASN A ND2 1 
ATOM   1033 N N   . GLY A 1 131 ? -55.602 17.394 -28.286 1.00 32.26  ? 132  GLY A N   1 
ATOM   1034 C CA  . GLY A 1 131 ? -54.811 17.421 -27.022 1.00 37.52  ? 132  GLY A CA  1 
ATOM   1035 C C   . GLY A 1 131 ? -54.461 16.092 -26.314 1.00 33.31  ? 132  GLY A C   1 
ATOM   1036 O O   . GLY A 1 131 ? -53.606 16.060 -25.397 1.00 33.57  ? 132  GLY A O   1 
ATOM   1037 N N   . LYS A 1 132 ? -55.059 15.009 -26.791 1.00 34.18  ? 133  LYS A N   1 
ATOM   1038 C CA  . LYS A 1 132 ? -54.955 13.716 -26.119 1.00 38.46  ? 133  LYS A CA  1 
ATOM   1039 C C   . LYS A 1 132 ? -53.572 13.190 -26.011 1.00 37.50  ? 133  LYS A C   1 
ATOM   1040 O O   . LYS A 1 132 ? -53.240 12.683 -24.942 1.00 40.16  ? 133  LYS A O   1 
ATOM   1041 C CB  . LYS A 1 132 ? -55.911 12.671 -26.693 1.00 36.86  ? 133  LYS A CB  1 
ATOM   1042 C CG  . LYS A 1 132 ? -55.402 11.914 -27.894 1.00 38.74  ? 133  LYS A CG  1 
ATOM   1043 C CD  . LYS A 1 132 ? -56.550 11.342 -28.682 1.00 36.19  ? 133  LYS A CD  1 
ATOM   1044 C CE  . LYS A 1 132 ? -56.002 10.364 -29.714 1.00 39.23  ? 133  LYS A CE  1 
ATOM   1045 N NZ  . LYS A 1 132 ? -57.181 9.682  -30.347 1.00 40.80  ? 133  LYS A NZ  1 
ATOM   1046 N N   . TYR A 1 133 ? -52.732 13.365 -27.036 1.00 38.56  ? 134  TYR A N   1 
ATOM   1047 C CA  . TYR A 1 133 ? -51.385 12.782 -26.971 1.00 38.12  ? 134  TYR A CA  1 
ATOM   1048 C C   . TYR A 1 133 ? -50.565 13.466 -25.925 1.00 37.42  ? 134  TYR A C   1 
ATOM   1049 O O   . TYR A 1 133 ? -49.729 12.848 -25.284 1.00 46.46  ? 134  TYR A O   1 
ATOM   1050 C CB  . TYR A 1 133 ? -50.637 12.850 -28.331 1.00 40.15  ? 134  TYR A CB  1 
ATOM   1051 C CG  . TYR A 1 133 ? -51.476 12.339 -29.471 1.00 43.10  ? 134  TYR A CG  1 
ATOM   1052 C CD1 . TYR A 1 133 ? -51.721 10.957 -29.630 1.00 46.00  ? 134  TYR A CD1 1 
ATOM   1053 C CD2 . TYR A 1 133 ? -52.066 13.215 -30.363 1.00 38.41  ? 134  TYR A CD2 1 
ATOM   1054 C CE1 . TYR A 1 133 ? -52.550 10.478 -30.647 1.00 43.28  ? 134  TYR A CE1 1 
ATOM   1055 C CE2 . TYR A 1 133 ? -52.892 12.746 -31.390 1.00 38.76  ? 134  TYR A CE2 1 
ATOM   1056 C CZ  . TYR A 1 133 ? -53.120 11.380 -31.518 1.00 43.96  ? 134  TYR A CZ  1 
ATOM   1057 O OH  . TYR A 1 133 ? -53.929 10.926 -32.531 1.00 55.00  ? 134  TYR A OH  1 
ATOM   1058 N N   . LEU A 1 134 ? -50.722 14.767 -25.814 1.00 36.24  ? 135  LEU A N   1 
ATOM   1059 C CA  . LEU A 1 134 ? -49.913 15.574 -24.854 1.00 38.56  ? 135  LEU A CA  1 
ATOM   1060 C C   . LEU A 1 134 ? -50.420 15.413 -23.426 1.00 35.26  ? 135  LEU A C   1 
ATOM   1061 O O   . LEU A 1 134 ? -49.653 15.265 -22.500 1.00 36.52  ? 135  LEU A O   1 
ATOM   1062 C CB  . LEU A 1 134 ? -49.990 17.077 -25.236 1.00 36.45  ? 135  LEU A CB  1 
ATOM   1063 C CG  . LEU A 1 134 ? -49.067 18.118 -24.623 1.00 35.55  ? 135  LEU A CG  1 
ATOM   1064 C CD1 . LEU A 1 134 ? -47.596 17.768 -24.576 1.00 35.62  ? 135  LEU A CD1 1 
ATOM   1065 C CD2 . LEU A 1 134 ? -49.223 19.409 -25.421 1.00 35.16  ? 135  LEU A CD2 1 
ATOM   1066 N N   . ALA A 1 135 ? -51.728 15.501 -23.266 1.00 34.24  ? 136  ALA A N   1 
ATOM   1067 C CA  . ALA A 1 135 ? -52.336 15.261 -21.987 1.00 39.94  ? 136  ALA A CA  1 
ATOM   1068 C C   . ALA A 1 135 ? -51.871 13.892 -21.446 1.00 42.12  ? 136  ALA A C   1 
ATOM   1069 O O   . ALA A 1 135 ? -51.373 13.782 -20.332 1.00 41.50  ? 136  ALA A O   1 
ATOM   1070 C CB  . ALA A 1 135 ? -53.837 15.293 -22.141 1.00 36.37  ? 136  ALA A CB  1 
ATOM   1071 N N   . TYR A 1 136 ? -52.003 12.866 -22.277 1.00 44.88  ? 137  TYR A N   1 
ATOM   1072 C CA  . TYR A 1 136 ? -51.631 11.517 -21.908 1.00 43.72  ? 137  TYR A CA  1 
ATOM   1073 C C   . TYR A 1 136 ? -50.150 11.386 -21.698 1.00 42.07  ? 137  TYR A C   1 
ATOM   1074 O O   . TYR A 1 136 ? -49.710 10.884 -20.673 1.00 42.43  ? 137  TYR A O   1 
ATOM   1075 C CB  . TYR A 1 136 ? -52.115 10.522 -22.961 1.00 45.05  ? 137  TYR A CB  1 
ATOM   1076 C CG  . TYR A 1 136 ? -51.592 9.158  -22.746 1.00 46.79  ? 137  TYR A CG  1 
ATOM   1077 C CD1 . TYR A 1 136 ? -52.148 8.311  -21.748 1.00 49.84  ? 137  TYR A CD1 1 
ATOM   1078 C CD2 . TYR A 1 136 ? -50.520 8.686  -23.494 1.00 47.60  ? 137  TYR A CD2 1 
ATOM   1079 C CE1 . TYR A 1 136 ? -51.626 7.027  -21.515 1.00 49.88  ? 137  TYR A CE1 1 
ATOM   1080 C CE2 . TYR A 1 136 ? -49.995 7.392  -23.284 1.00 52.87  ? 137  TYR A CE2 1 
ATOM   1081 C CZ  . TYR A 1 136 ? -50.550 6.565  -22.304 1.00 52.30  ? 137  TYR A CZ  1 
ATOM   1082 O OH  . TYR A 1 136 ? -50.030 5.316  -22.116 1.00 49.18  ? 137  TYR A OH  1 
ATOM   1083 N N   . THR A 1 137 ? -49.350 11.857 -22.640 1.00 40.40  ? 138  THR A N   1 
ATOM   1084 C CA  . THR A 1 137 ? -47.894 11.602 -22.541 1.00 39.16  ? 138  THR A CA  1 
ATOM   1085 C C   . THR A 1 137 ? -47.282 12.324 -21.370 1.00 38.33  ? 138  THR A C   1 
ATOM   1086 O O   . THR A 1 137 ? -46.421 11.783 -20.713 1.00 41.63  ? 138  THR A O   1 
ATOM   1087 C CB  . THR A 1 137 ? -47.131 11.959 -23.833 1.00 37.81  ? 138  THR A CB  1 
ATOM   1088 O OG1 . THR A 1 137 ? -47.609 11.132 -24.878 1.00 43.02  ? 138  THR A OG1 1 
ATOM   1089 C CG2 . THR A 1 137 ? -45.671 11.696 -23.708 1.00 37.65  ? 138  THR A CG2 1 
ATOM   1090 N N   . GLU A 1 138 ? -47.735 13.543 -21.090 1.00 39.50  ? 139  GLU A N   1 
ATOM   1091 C CA  . GLU A 1 138 ? -47.034 14.402 -20.146 1.00 37.28  ? 139  GLU A CA  1 
ATOM   1092 C C   . GLU A 1 138 ? -47.858 14.661 -18.911 1.00 35.09  ? 139  GLU A C   1 
ATOM   1093 O O   . GLU A 1 138 ? -47.365 15.342 -18.025 1.00 36.37  ? 139  GLU A O   1 
ATOM   1094 C CB  . GLU A 1 138 ? -46.670 15.768 -20.798 1.00 36.67  ? 139  GLU A CB  1 
ATOM   1095 C CG  . GLU A 1 138 ? -45.552 15.750 -21.803 1.00 34.88  ? 139  GLU A CG  1 
ATOM   1096 C CD  . GLU A 1 138 ? -44.230 15.328 -21.273 1.00 39.60  ? 139  GLU A CD  1 
ATOM   1097 O OE1 . GLU A 1 138 ? -43.802 15.813 -20.204 1.00 40.06  ? 139  GLU A OE1 1 
ATOM   1098 O OE2 . GLU A 1 138 ? -43.552 14.564 -22.003 1.00 42.67  ? 139  GLU A OE2 1 
ATOM   1099 N N   . GLU A 1 139 ? -49.097 14.154 -18.846 1.00 39.06  ? 140  GLU A N   1 
ATOM   1100 C CA  . GLU A 1 139 ? -49.910 14.200 -17.620 1.00 42.12  ? 140  GLU A CA  1 
ATOM   1101 C C   . GLU A 1 139 ? -50.214 15.658 -17.260 1.00 42.63  ? 140  GLU A C   1 
ATOM   1102 O O   . GLU A 1 139 ? -49.893 16.146 -16.170 1.00 46.91  ? 140  GLU A O   1 
ATOM   1103 C CB  . GLU A 1 139 ? -49.193 13.439 -16.461 1.00 50.03  ? 140  GLU A CB  1 
ATOM   1104 C CG  . GLU A 1 139 ? -49.668 11.982 -16.243 1.00 65.33  ? 140  GLU A CG  1 
ATOM   1105 C CD  . GLU A 1 139 ? -48.529 10.953 -16.019 1.00 76.88  ? 140  GLU A CD  1 
ATOM   1106 O OE1 . GLU A 1 139 ? -47.428 11.252 -15.453 1.00 74.81  ? 140  GLU A OE1 1 
ATOM   1107 O OE2 . GLU A 1 139 ? -48.744 9.795  -16.431 1.00 87.46  ? 140  GLU A OE2 1 
ATOM   1108 N N   . VAL A 1 140 ? -50.809 16.362 -18.221 1.00 36.85  ? 141  VAL A N   1 
ATOM   1109 C CA  . VAL A 1 140 ? -51.233 17.707 -18.022 1.00 30.70  ? 141  VAL A CA  1 
ATOM   1110 C C   . VAL A 1 140 ? -52.667 17.649 -18.385 1.00 30.83  ? 141  VAL A C   1 
ATOM   1111 O O   . VAL A 1 140 ? -53.114 16.774 -19.140 1.00 30.25  ? 141  VAL A O   1 
ATOM   1112 C CB  . VAL A 1 140 ? -50.457 18.732 -18.911 1.00 35.33  ? 141  VAL A CB  1 
ATOM   1113 C CG1 . VAL A 1 140 ? -48.963 18.753 -18.595 1.00 32.33  ? 141  VAL A CG1 1 
ATOM   1114 C CG2 . VAL A 1 140 ? -50.606 18.467 -20.402 1.00 34.74  ? 141  VAL A CG2 1 
ATOM   1115 N N   . VAL A 1 141 ? -53.422 18.556 -17.805 1.00 31.71  ? 142  VAL A N   1 
ATOM   1116 C CA  . VAL A 1 141 ? -54.750 18.836 -18.272 1.00 31.89  ? 142  VAL A CA  1 
ATOM   1117 C C   . VAL A 1 141 ? -54.646 19.881 -19.421 1.00 34.36  ? 142  VAL A C   1 
ATOM   1118 O O   . VAL A 1 141 ? -54.035 20.948 -19.246 1.00 33.03  ? 142  VAL A O   1 
ATOM   1119 C CB  . VAL A 1 141 ? -55.529 19.439 -17.139 1.00 29.28  ? 142  VAL A CB  1 
ATOM   1120 C CG1 . VAL A 1 141 ? -56.834 20.006 -17.597 1.00 30.76  ? 142  VAL A CG1 1 
ATOM   1121 C CG2 . VAL A 1 141 ? -55.736 18.376 -16.098 1.00 34.15  ? 142  VAL A CG2 1 
ATOM   1122 N N   . LEU A 1 142 ? -55.204 19.532 -20.584 1.00 31.63  ? 143  LEU A N   1 
ATOM   1123 C CA  . LEU A 1 142 ? -54.936 20.255 -21.832 1.00 29.70  ? 143  LEU A CA  1 
ATOM   1124 C C   . LEU A 1 142 ? -56.209 20.852 -22.241 1.00 27.73  ? 143  LEU A C   1 
ATOM   1125 O O   . LEU A 1 142 ? -57.154 20.131 -22.577 1.00 31.59  ? 143  LEU A O   1 
ATOM   1126 C CB  . LEU A 1 142 ? -54.422 19.324 -22.928 1.00 33.30  ? 143  LEU A CB  1 
ATOM   1127 C CG  . LEU A 1 142 ? -53.719 19.938 -24.171 1.00 37.03  ? 143  LEU A CG  1 
ATOM   1128 C CD1 . LEU A 1 142 ? -54.722 20.578 -25.117 1.00 39.88  ? 143  LEU A CD1 1 
ATOM   1129 C CD2 . LEU A 1 142 ? -52.648 20.978 -23.846 1.00 37.65  ? 143  LEU A CD2 1 
ATOM   1130 N N   . VAL A 1 143 ? -56.272 22.177 -22.190 1.00 26.59  ? 144  VAL A N   1 
ATOM   1131 C CA  . VAL A 1 143 ? -57.436 22.878 -22.696 1.00 26.21  ? 144  VAL A CA  1 
ATOM   1132 C C   . VAL A 1 143 ? -57.186 23.517 -24.072 1.00 25.06  ? 144  VAL A C   1 
ATOM   1133 O O   . VAL A 1 143 ? -56.106 24.082 -24.340 1.00 26.41  ? 144  VAL A O   1 
ATOM   1134 C CB  . VAL A 1 143 ? -57.839 23.987 -21.715 1.00 25.33  ? 144  VAL A CB  1 
ATOM   1135 C CG1 . VAL A 1 143 ? -59.066 24.744 -22.188 1.00 24.45  ? 144  VAL A CG1 1 
ATOM   1136 C CG2 . VAL A 1 143 ? -58.141 23.383 -20.357 1.00 28.69  ? 144  VAL A CG2 1 
ATOM   1137 N N   . SER A 1 144 ? -58.217 23.541 -24.902 1.00 22.41  ? 145  SER A N   1 
ATOM   1138 C CA  . SER A 1 144 ? -58.135 24.375 -26.064 1.00 24.00  ? 145  SER A CA  1 
ATOM   1139 C C   . SER A 1 144 ? -59.353 25.252 -26.089 1.00 24.99  ? 145  SER A C   1 
ATOM   1140 O O   . SER A 1 144 ? -60.477 24.763 -26.065 1.00 21.99  ? 145  SER A O   1 
ATOM   1141 C CB  . SER A 1 144 ? -57.979 23.528 -27.350 1.00 24.61  ? 145  SER A CB  1 
ATOM   1142 O OG  . SER A 1 144 ? -59.176 22.794 -27.661 1.00 25.66  ? 145  SER A OG  1 
ATOM   1143 N N   . LEU A 1 145 ? -59.153 26.560 -26.196 1.00 24.52  ? 146  LEU A N   1 
ATOM   1144 C CA  . LEU A 1 145 ? -60.296 27.457 -26.269 1.00 25.98  ? 146  LEU A CA  1 
ATOM   1145 C C   . LEU A 1 145 ? -60.684 27.853 -27.741 1.00 26.63  ? 146  LEU A C   1 
ATOM   1146 O O   . LEU A 1 145 ? -60.033 27.490 -28.716 1.00 24.87  ? 146  LEU A O   1 
ATOM   1147 C CB  . LEU A 1 145 ? -59.954 28.712 -25.440 1.00 28.81  ? 146  LEU A CB  1 
ATOM   1148 C CG  . LEU A 1 145 ? -58.675 29.494 -25.717 1.00 30.08  ? 146  LEU A CG  1 
ATOM   1149 C CD1 . LEU A 1 145 ? -58.773 30.366 -27.000 1.00 34.20  ? 146  LEU A CD1 1 
ATOM   1150 C CD2 . LEU A 1 145 ? -58.307 30.395 -24.566 1.00 30.97  ? 146  LEU A CD2 1 
ATOM   1151 N N   . SER A 1 146 ? -61.711 28.669 -27.877 1.00 27.82  ? 147  SER A N   1 
ATOM   1152 C CA  . SER A 1 146 ? -62.001 29.271 -29.128 1.00 26.74  ? 147  SER A CA  1 
ATOM   1153 C C   . SER A 1 146 ? -62.306 30.734 -28.935 1.00 27.73  ? 147  SER A C   1 
ATOM   1154 O O   . SER A 1 146 ? -62.499 31.223 -27.819 1.00 25.84  ? 147  SER A O   1 
ATOM   1155 C CB  . SER A 1 146 ? -63.159 28.550 -29.775 1.00 28.42  ? 147  SER A CB  1 
ATOM   1156 O OG  . SER A 1 146 ? -64.332 28.664 -29.028 1.00 32.80  ? 147  SER A OG  1 
ATOM   1157 N N   . TYR A 1 147 ? -62.300 31.453 -30.046 1.00 28.64  ? 148  TYR A N   1 
ATOM   1158 C CA  . TYR A 1 147 ? -62.566 32.881 -30.091 1.00 23.98  ? 148  TYR A CA  1 
ATOM   1159 C C   . TYR A 1 147 ? -63.006 33.363 -31.487 1.00 25.11  ? 148  TYR A C   1 
ATOM   1160 O O   . TYR A 1 147 ? -62.589 32.819 -32.521 1.00 27.02  ? 148  TYR A O   1 
ATOM   1161 C CB  . TYR A 1 147 ? -61.332 33.650 -29.626 1.00 24.08  ? 148  TYR A CB  1 
ATOM   1162 C CG  . TYR A 1 147 ? -60.067 33.492 -30.467 1.00 24.50  ? 148  TYR A CG  1 
ATOM   1163 C CD1 . TYR A 1 147 ? -59.192 32.468 -30.265 1.00 25.68  ? 148  TYR A CD1 1 
ATOM   1164 C CD2 . TYR A 1 147 ? -59.756 34.403 -31.433 1.00 24.61  ? 148  TYR A CD2 1 
ATOM   1165 C CE1 . TYR A 1 147 ? -58.073 32.335 -31.032 1.00 25.83  ? 148  TYR A CE1 1 
ATOM   1166 C CE2 . TYR A 1 147 ? -58.650 34.273 -32.219 1.00 22.94  ? 148  TYR A CE2 1 
ATOM   1167 C CZ  . TYR A 1 147 ? -57.813 33.253 -32.033 1.00 24.49  ? 148  TYR A CZ  1 
ATOM   1168 O OH  . TYR A 1 147 ? -56.650 33.215 -32.810 1.00 23.49  ? 148  TYR A OH  1 
ATOM   1169 N N   . ARG A 1 148 ? -63.870 34.357 -31.504 1.00 24.83  ? 149  ARG A N   1 
ATOM   1170 C CA  . ARG A 1 148 ? -64.368 34.901 -32.719 1.00 26.97  ? 149  ARG A CA  1 
ATOM   1171 C C   . ARG A 1 148 ? -63.218 35.516 -33.525 1.00 30.00  ? 149  ARG A C   1 
ATOM   1172 O O   . ARG A 1 148 ? -62.360 36.247 -32.947 1.00 26.54  ? 149  ARG A O   1 
ATOM   1173 C CB  . ARG A 1 148 ? -65.371 35.998 -32.434 1.00 25.34  ? 149  ARG A CB  1 
ATOM   1174 C CG  . ARG A 1 148 ? -66.695 35.451 -31.981 1.00 28.48  ? 149  ARG A CG  1 
ATOM   1175 C CD  . ARG A 1 148 ? -67.634 36.586 -31.589 1.00 29.21  ? 149  ARG A CD  1 
ATOM   1176 N NE  . ARG A 1 148 ? -67.297 37.037 -30.222 1.00 28.03  ? 149  ARG A NE  1 
ATOM   1177 C CZ  . ARG A 1 148 ? -67.911 38.009 -29.585 1.00 26.85  ? 149  ARG A CZ  1 
ATOM   1178 N NH1 . ARG A 1 148 ? -68.828 38.691 -30.193 1.00 28.04  ? 149  ARG A NH1 1 
ATOM   1179 N NH2 . ARG A 1 148 ? -67.552 38.351 -28.336 1.00 28.93  ? 149  ARG A NH2 1 
ATOM   1180 N N   . VAL A 1 149 ? -63.239 35.237 -34.837 1.00 26.47  ? 150  VAL A N   1 
ATOM   1181 C CA  . VAL A 1 149 ? -62.246 35.779 -35.750 1.00 26.94  ? 150  VAL A CA  1 
ATOM   1182 C C   . VAL A 1 149 ? -62.937 36.668 -36.763 1.00 27.70  ? 150  VAL A C   1 
ATOM   1183 O O   . VAL A 1 149 ? -64.173 36.758 -36.824 1.00 29.46  ? 150  VAL A O   1 
ATOM   1184 C CB  . VAL A 1 149 ? -61.462 34.650 -36.429 1.00 27.14  ? 150  VAL A CB  1 
ATOM   1185 C CG1 . VAL A 1 149 ? -60.698 33.807 -35.384 1.00 29.34  ? 150  VAL A CG1 1 
ATOM   1186 C CG2 . VAL A 1 149 ? -62.377 33.713 -37.195 1.00 25.49  ? 150  VAL A CG2 1 
ATOM   1187 N N   . GLY A 1 150 ? -62.140 37.325 -37.586 1.00 30.85  ? 151  GLY A N   1 
ATOM   1188 C CA  . GLY A 1 150 ? -62.668 38.127 -38.669 1.00 26.43  ? 151  GLY A CA  1 
ATOM   1189 C C   . GLY A 1 150 ? -63.383 39.313 -38.052 1.00 29.71  ? 151  GLY A C   1 
ATOM   1190 O O   . GLY A 1 150 ? -63.084 39.758 -36.947 1.00 31.25  ? 151  GLY A O   1 
ATOM   1191 N N   . ALA A 1 151 ? -64.337 39.828 -38.782 1.00 29.46  ? 152  ALA A N   1 
ATOM   1192 C CA  . ALA A 1 151 ? -65.067 40.983 -38.347 1.00 32.04  ? 152  ALA A CA  1 
ATOM   1193 C C   . ALA A 1 151 ? -65.880 40.677 -37.106 1.00 28.26  ? 152  ALA A C   1 
ATOM   1194 O O   . ALA A 1 151 ? -66.044 41.533 -36.291 1.00 25.86  ? 152  ALA A O   1 
ATOM   1195 C CB  . ALA A 1 151 ? -66.005 41.413 -39.436 1.00 35.60  ? 152  ALA A CB  1 
ATOM   1196 N N   . PHE A 1 152 ? -66.312 39.432 -36.967 1.00 28.33  ? 153  PHE A N   1 
ATOM   1197 C CA  . PHE A 1 152 ? -67.047 38.999 -35.811 1.00 30.93  ? 153  PHE A CA  1 
ATOM   1198 C C   . PHE A 1 152 ? -66.244 39.183 -34.530 1.00 29.70  ? 153  PHE A C   1 
ATOM   1199 O O   . PHE A 1 152 ? -66.822 39.480 -33.494 1.00 28.66  ? 153  PHE A O   1 
ATOM   1200 C CB  . PHE A 1 152 ? -67.471 37.543 -35.948 1.00 31.35  ? 153  PHE A CB  1 
ATOM   1201 C CG  . PHE A 1 152 ? -68.140 37.249 -37.237 1.00 35.53  ? 153  PHE A CG  1 
ATOM   1202 C CD1 . PHE A 1 152 ? -69.485 37.469 -37.398 1.00 40.27  ? 153  PHE A CD1 1 
ATOM   1203 C CD2 . PHE A 1 152 ? -67.412 36.776 -38.319 1.00 37.76  ? 153  PHE A CD2 1 
ATOM   1204 C CE1 . PHE A 1 152 ? -70.123 37.195 -38.602 1.00 38.36  ? 153  PHE A CE1 1 
ATOM   1205 C CE2 . PHE A 1 152 ? -68.036 36.509 -39.521 1.00 39.29  ? 153  PHE A CE2 1 
ATOM   1206 C CZ  . PHE A 1 152 ? -69.386 36.726 -39.664 1.00 39.98  ? 153  PHE A CZ  1 
ATOM   1207 N N   . GLY A 1 153 ? -64.923 39.035 -34.608 1.00 28.75  ? 154  GLY A N   1 
ATOM   1208 C CA  . GLY A 1 153 ? -64.081 39.099 -33.419 1.00 28.40  ? 154  GLY A CA  1 
ATOM   1209 C C   . GLY A 1 153 ? -63.373 40.425 -33.294 1.00 28.66  ? 154  GLY A C   1 
ATOM   1210 O O   . GLY A 1 153 ? -62.906 40.778 -32.228 1.00 29.12  ? 154  GLY A O   1 
ATOM   1211 N N   . PHE A 1 154 ? -63.259 41.168 -34.388 1.00 27.28  ? 155  PHE A N   1 
ATOM   1212 C CA  . PHE A 1 154 ? -62.363 42.276 -34.390 1.00 26.42  ? 155  PHE A CA  1 
ATOM   1213 C C   . PHE A 1 154 ? -62.801 43.546 -35.089 1.00 28.56  ? 155  PHE A C   1 
ATOM   1214 O O   . PHE A 1 154 ? -62.011 44.500 -35.152 1.00 27.37  ? 155  PHE A O   1 
ATOM   1215 C CB  . PHE A 1 154 ? -61.033 41.767 -34.896 1.00 26.55  ? 155  PHE A CB  1 
ATOM   1216 C CG  . PHE A 1 154 ? -60.425 40.791 -33.971 1.00 24.92  ? 155  PHE A CG  1 
ATOM   1217 C CD1 . PHE A 1 154 ? -59.859 41.213 -32.772 1.00 26.61  ? 155  PHE A CD1 1 
ATOM   1218 C CD2 . PHE A 1 154 ? -60.522 39.460 -34.226 1.00 25.90  ? 155  PHE A CD2 1 
ATOM   1219 C CE1 . PHE A 1 154 ? -59.349 40.286 -31.873 1.00 25.85  ? 155  PHE A CE1 1 
ATOM   1220 C CE2 . PHE A 1 154 ? -60.043 38.526 -33.342 1.00 24.70  ? 155  PHE A CE2 1 
ATOM   1221 C CZ  . PHE A 1 154 ? -59.471 38.946 -32.143 1.00 25.88  ? 155  PHE A CZ  1 
ATOM   1222 N N   . LEU A 1 155 ? -64.057 43.610 -35.544 1.00 28.05  ? 156  LEU A N   1 
ATOM   1223 C CA  . LEU A 1 155 ? -64.549 44.881 -36.083 1.00 29.24  ? 156  LEU A CA  1 
ATOM   1224 C C   . LEU A 1 155 ? -64.440 45.909 -34.989 1.00 28.27  ? 156  LEU A C   1 
ATOM   1225 O O   . LEU A 1 155 ? -64.907 45.660 -33.910 1.00 34.82  ? 156  LEU A O   1 
ATOM   1226 C CB  . LEU A 1 155 ? -66.017 44.783 -36.535 1.00 31.65  ? 156  LEU A CB  1 
ATOM   1227 C CG  . LEU A 1 155 ? -66.530 46.027 -37.306 1.00 35.71  ? 156  LEU A CG  1 
ATOM   1228 C CD1 . LEU A 1 155 ? -66.560 45.778 -38.821 1.00 36.96  ? 156  LEU A CD1 1 
ATOM   1229 C CD2 . LEU A 1 155 ? -67.931 46.370 -36.865 1.00 34.57  ? 156  LEU A CD2 1 
ATOM   1230 N N   . ALA A 1 156 ? -63.893 47.082 -35.268 1.00 30.83  ? 157  ALA A N   1 
ATOM   1231 C CA  . ALA A 1 156 ? -63.610 48.048 -34.251 1.00 30.62  ? 157  ALA A CA  1 
ATOM   1232 C C   . ALA A 1 156 ? -64.049 49.471 -34.605 1.00 38.26  ? 157  ALA A C   1 
ATOM   1233 O O   . ALA A 1 156 ? -63.360 50.168 -35.395 1.00 32.47  ? 157  ALA A O   1 
ATOM   1234 C CB  . ALA A 1 156 ? -62.134 48.076 -33.961 1.00 29.59  ? 157  ALA A CB  1 
ATOM   1235 N N   . LEU A 1 157 ? -65.134 49.903 -33.942 1.00 33.68  ? 158  LEU A N   1 
ATOM   1236 C CA  . LEU A 1 157 ? -65.600 51.296 -33.987 1.00 35.67  ? 158  LEU A CA  1 
ATOM   1237 C C   . LEU A 1 157 ? -65.412 51.935 -32.623 1.00 32.80  ? 158  LEU A C   1 
ATOM   1238 O O   . LEU A 1 157 ? -66.312 52.014 -31.809 1.00 37.03  ? 158  LEU A O   1 
ATOM   1239 C CB  . LEU A 1 157 ? -67.078 51.317 -34.429 1.00 38.91  ? 158  LEU A CB  1 
ATOM   1240 C CG  . LEU A 1 157 ? -67.213 50.891 -35.925 1.00 38.58  ? 158  LEU A CG  1 
ATOM   1241 C CD1 . LEU A 1 157 ? -68.602 50.378 -36.283 1.00 35.85  ? 158  LEU A CD1 1 
ATOM   1242 C CD2 . LEU A 1 157 ? -66.754 52.006 -36.871 1.00 39.06  ? 158  LEU A CD2 1 
ATOM   1243 N N   . HIS A 1 158 ? -64.204 52.325 -32.339 1.00 34.80  ? 159  HIS A N   1 
ATOM   1244 C CA  . HIS A 1 158 ? -63.853 52.796 -31.020 1.00 39.55  ? 159  HIS A CA  1 
ATOM   1245 C C   . HIS A 1 158 ? -64.725 53.957 -30.566 1.00 49.11  ? 159  HIS A C   1 
ATOM   1246 O O   . HIS A 1 158 ? -64.977 54.874 -31.365 1.00 42.77  ? 159  HIS A O   1 
ATOM   1247 C CB  . HIS A 1 158 ? -62.440 53.275 -31.018 1.00 37.23  ? 159  HIS A CB  1 
ATOM   1248 C CG  . HIS A 1 158 ? -61.964 53.693 -29.677 1.00 42.71  ? 159  HIS A CG  1 
ATOM   1249 N ND1 . HIS A 1 158 ? -61.902 52.817 -28.601 1.00 42.61  ? 159  HIS A ND1 1 
ATOM   1250 C CD2 . HIS A 1 158 ? -61.482 54.886 -29.239 1.00 40.43  ? 159  HIS A CD2 1 
ATOM   1251 C CE1 . HIS A 1 158 ? -61.405 53.462 -27.561 1.00 41.24  ? 159  HIS A CE1 1 
ATOM   1252 N NE2 . HIS A 1 158 ? -61.149 54.717 -27.919 1.00 41.48  ? 159  HIS A NE2 1 
ATOM   1253 N N   . GLY A 1 159 ? -65.163 53.924 -29.295 1.00 46.39  ? 160  GLY A N   1 
ATOM   1254 C CA  . GLY A 1 159 ? -66.178 54.867 -28.800 1.00 49.67  ? 160  GLY A CA  1 
ATOM   1255 C C   . GLY A 1 159 ? -67.570 54.238 -28.824 1.00 47.52  ? 160  GLY A C   1 
ATOM   1256 O O   . GLY A 1 159 ? -68.431 54.584 -28.072 1.00 45.91  ? 160  GLY A O   1 
ATOM   1257 N N   . SER A 1 160 ? -67.804 53.284 -29.692 1.00 48.22  ? 161  SER A N   1 
ATOM   1258 C CA  . SER A 1 160 ? -69.069 52.593 -29.630 1.00 48.28  ? 161  SER A CA  1 
ATOM   1259 C C   . SER A 1 160 ? -68.933 51.466 -28.609 1.00 49.65  ? 161  SER A C   1 
ATOM   1260 O O   . SER A 1 160 ? -67.845 50.931 -28.419 1.00 53.78  ? 161  SER A O   1 
ATOM   1261 C CB  . SER A 1 160 ? -69.416 52.022 -30.993 1.00 50.42  ? 161  SER A CB  1 
ATOM   1262 O OG  . SER A 1 160 ? -70.225 50.869 -30.826 1.00 58.29  ? 161  SER A OG  1 
ATOM   1263 N N   . GLN A 1 161 ? -70.021 51.102 -27.944 1.00 46.10  ? 162  GLN A N   1 
ATOM   1264 C CA  . GLN A 1 161 ? -69.999 49.961 -27.046 1.00 45.86  ? 162  GLN A CA  1 
ATOM   1265 C C   . GLN A 1 161 ? -70.617 48.748 -27.697 1.00 42.76  ? 162  GLN A C   1 
ATOM   1266 O O   . GLN A 1 161 ? -70.590 47.639 -27.139 1.00 41.38  ? 162  GLN A O   1 
ATOM   1267 C CB  . GLN A 1 161 ? -70.702 50.294 -25.702 1.00 53.52  ? 162  GLN A CB  1 
ATOM   1268 C CG  . GLN A 1 161 ? -69.912 51.270 -24.815 1.00 57.79  ? 162  GLN A CG  1 
ATOM   1269 C CD  . GLN A 1 161 ? -68.478 50.795 -24.475 1.00 64.78  ? 162  GLN A CD  1 
ATOM   1270 O OE1 . GLN A 1 161 ? -68.239 49.602 -24.218 1.00 63.77  ? 162  GLN A OE1 1 
ATOM   1271 N NE2 . GLN A 1 161 ? -67.518 51.738 -24.468 1.00 61.86  ? 162  GLN A NE2 1 
ATOM   1272 N N   . GLU A 1 162 ? -71.227 48.956 -28.855 1.00 40.07  ? 163  GLU A N   1 
ATOM   1273 C CA  . GLU A 1 162 ? -71.840 47.851 -29.581 1.00 44.25  ? 163  GLU A CA  1 
ATOM   1274 C C   . GLU A 1 162 ? -70.784 47.053 -30.399 1.00 39.59  ? 163  GLU A C   1 
ATOM   1275 O O   . GLU A 1 162 ? -70.948 45.861 -30.553 1.00 47.09  ? 163  GLU A O   1 
ATOM   1276 C CB  . GLU A 1 162 ? -72.992 48.356 -30.465 1.00 50.78  ? 163  GLU A CB  1 
ATOM   1277 C CG  . GLU A 1 162 ? -74.158 49.046 -29.720 1.00 52.98  ? 163  GLU A CG  1 
ATOM   1278 C CD  . GLU A 1 162 ? -74.848 48.123 -28.729 1.00 54.56  ? 163  GLU A CD  1 
ATOM   1279 O OE1 . GLU A 1 162 ? -75.111 46.935 -29.044 1.00 51.08  ? 163  GLU A OE1 1 
ATOM   1280 O OE2 . GLU A 1 162 ? -75.113 48.586 -27.602 1.00 61.78  ? 163  GLU A OE2 1 
ATOM   1281 N N   . ALA A 1 163 ? -69.713 47.702 -30.872 1.00 37.38  ? 164  ALA A N   1 
ATOM   1282 C CA  . ALA A 1 163 ? -68.604 47.040 -31.616 1.00 37.81  ? 164  ALA A CA  1 
ATOM   1283 C C   . ALA A 1 163 ? -67.306 47.736 -31.260 1.00 33.85  ? 164  ALA A C   1 
ATOM   1284 O O   . ALA A 1 163 ? -66.744 48.502 -32.081 1.00 37.73  ? 164  ALA A O   1 
ATOM   1285 C CB  . ALA A 1 163 ? -68.836 47.096 -33.127 1.00 35.00  ? 164  ALA A CB  1 
ATOM   1286 N N   . PRO A 1 164 ? -66.833 47.508 -30.022 1.00 32.85  ? 165  PRO A N   1 
ATOM   1287 C CA  . PRO A 1 164 ? -65.730 48.264 -29.490 1.00 31.65  ? 165  PRO A CA  1 
ATOM   1288 C C   . PRO A 1 164 ? -64.426 47.860 -30.055 1.00 32.40  ? 165  PRO A C   1 
ATOM   1289 O O   . PRO A 1 164 ? -63.435 48.575 -29.875 1.00 32.27  ? 165  PRO A O   1 
ATOM   1290 C CB  . PRO A 1 164 ? -65.763 47.922 -27.965 1.00 33.12  ? 165  PRO A CB  1 
ATOM   1291 C CG  . PRO A 1 164 ? -66.484 46.630 -27.850 1.00 32.38  ? 165  PRO A CG  1 
ATOM   1292 C CD  . PRO A 1 164 ? -67.454 46.630 -29.000 1.00 34.74  ? 165  PRO A CD  1 
ATOM   1293 N N   . GLY A 1 165 ? -64.377 46.676 -30.668 1.00 31.06  ? 166  GLY A N   1 
ATOM   1294 C CA  . GLY A 1 165 ? -63.076 46.091 -31.020 1.00 32.24  ? 166  GLY A CA  1 
ATOM   1295 C C   . GLY A 1 165 ? -62.601 45.119 -29.920 1.00 33.93  ? 166  GLY A C   1 
ATOM   1296 O O   . GLY A 1 165 ? -63.143 45.087 -28.808 1.00 31.75  ? 166  GLY A O   1 
ATOM   1297 N N   . ASN A 1 166 ? -61.644 44.288 -30.291 1.00 30.57  ? 167  ASN A N   1 
ATOM   1298 C CA  . ASN A 1 166 ? -61.016 43.349 -29.431 1.00 28.08  ? 167  ASN A CA  1 
ATOM   1299 C C   . ASN A 1 166 ? -61.875 42.257 -28.831 1.00 28.18  ? 167  ASN A C   1 
ATOM   1300 O O   . ASN A 1 166 ? -61.390 41.508 -27.999 1.00 26.01  ? 167  ASN A O   1 
ATOM   1301 C CB  . ASN A 1 166 ? -60.295 44.109 -28.361 1.00 27.99  ? 167  ASN A CB  1 
ATOM   1302 C CG  . ASN A 1 166 ? -59.108 44.858 -28.909 1.00 28.46  ? 167  ASN A CG  1 
ATOM   1303 O OD1 . ASN A 1 166 ? -58.561 44.511 -29.963 1.00 28.34  ? 167  ASN A OD1 1 
ATOM   1304 N ND2 . ASN A 1 166 ? -58.698 45.883 -28.213 1.00 27.97  ? 167  ASN A ND2 1 
ATOM   1305 N N   . VAL A 1 167 ? -63.092 42.065 -29.318 1.00 25.49  ? 168  VAL A N   1 
ATOM   1306 C CA  . VAL A 1 167 ? -63.957 41.153 -28.593 1.00 29.21  ? 168  VAL A CA  1 
ATOM   1307 C C   . VAL A 1 167 ? -63.489 39.729 -28.641 1.00 29.49  ? 168  VAL A C   1 
ATOM   1308 O O   . VAL A 1 167 ? -63.723 38.940 -27.669 1.00 31.39  ? 168  VAL A O   1 
ATOM   1309 C CB  . VAL A 1 167 ? -65.438 41.315 -28.968 1.00 33.41  ? 168  VAL A CB  1 
ATOM   1310 C CG1 . VAL A 1 167 ? -65.854 42.768 -28.701 1.00 34.52  ? 168  VAL A CG1 1 
ATOM   1311 C CG2 . VAL A 1 167 ? -65.710 40.916 -30.421 1.00 36.75  ? 168  VAL A CG2 1 
ATOM   1312 N N   . GLY A 1 168 ? -62.735 39.400 -29.702 1.00 26.69  ? 169  GLY A N   1 
ATOM   1313 C CA  . GLY A 1 168 ? -62.163 38.073 -29.824 1.00 23.62  ? 169  GLY A CA  1 
ATOM   1314 C C   . GLY A 1 168 ? -61.085 37.843 -28.792 1.00 24.00  ? 169  GLY A C   1 
ATOM   1315 O O   . GLY A 1 168 ? -60.873 36.713 -28.407 1.00 24.72  ? 169  GLY A O   1 
ATOM   1316 N N   . LEU A 1 169 ? -60.362 38.885 -28.378 1.00 23.27  ? 170  LEU A N   1 
ATOM   1317 C CA  . LEU A 1 169 ? -59.386 38.706 -27.321 1.00 26.91  ? 170  LEU A CA  1 
ATOM   1318 C C   . LEU A 1 169 ? -60.181 38.576 -25.984 1.00 28.82  ? 170  LEU A C   1 
ATOM   1319 O O   . LEU A 1 169 ? -59.795 37.801 -25.080 1.00 25.71  ? 170  LEU A O   1 
ATOM   1320 C CB  . LEU A 1 169 ? -58.462 39.888 -27.215 1.00 26.52  ? 170  LEU A CB  1 
ATOM   1321 C CG  . LEU A 1 169 ? -57.375 39.975 -28.264 1.00 26.75  ? 170  LEU A CG  1 
ATOM   1322 C CD1 . LEU A 1 169 ? -56.820 41.378 -28.298 1.00 26.59  ? 170  LEU A CD1 1 
ATOM   1323 C CD2 . LEU A 1 169 ? -56.234 38.984 -28.013 1.00 26.66  ? 170  LEU A CD2 1 
ATOM   1324 N N   . LEU A 1 170 ? -61.277 39.327 -25.867 1.00 25.75  ? 171  LEU A N   1 
ATOM   1325 C CA  . LEU A 1 170 ? -62.125 39.199 -24.672 1.00 27.50  ? 171  LEU A CA  1 
ATOM   1326 C C   . LEU A 1 170 ? -62.701 37.760 -24.584 1.00 30.15  ? 171  LEU A C   1 
ATOM   1327 O O   . LEU A 1 170 ? -62.778 37.258 -23.510 1.00 27.92  ? 171  LEU A O   1 
ATOM   1328 C CB  . LEU A 1 170 ? -63.209 40.271 -24.624 1.00 26.49  ? 171  LEU A CB  1 
ATOM   1329 C CG  . LEU A 1 170 ? -62.691 41.701 -24.348 1.00 30.38  ? 171  LEU A CG  1 
ATOM   1330 C CD1 . LEU A 1 170 ? -63.826 42.722 -24.305 1.00 29.47  ? 171  LEU A CD1 1 
ATOM   1331 C CD2 . LEU A 1 170 ? -61.890 41.844 -23.078 1.00 26.82  ? 171  LEU A CD2 1 
ATOM   1332 N N   . ASP A 1 171 ? -63.028 37.100 -25.723 1.00 30.48  ? 172  ASP A N   1 
ATOM   1333 C CA  . ASP A 1 171 ? -63.439 35.716 -25.723 1.00 25.70  ? 172  ASP A CA  1 
ATOM   1334 C C   . ASP A 1 171 ? -62.330 34.847 -25.138 1.00 27.09  ? 172  ASP A C   1 
ATOM   1335 O O   . ASP A 1 171 ? -62.571 33.884 -24.394 1.00 27.51  ? 172  ASP A O   1 
ATOM   1336 C CB  . ASP A 1 171 ? -63.766 35.138 -27.152 1.00 25.22  ? 172  ASP A CB  1 
ATOM   1337 C CG  . ASP A 1 171 ? -64.915 35.835 -27.876 1.00 28.86  ? 172  ASP A CG  1 
ATOM   1338 O OD1 . ASP A 1 171 ? -65.684 36.578 -27.258 1.00 26.87  ? 172  ASP A OD1 1 
ATOM   1339 O OD2 . ASP A 1 171 ? -65.052 35.656 -29.143 1.00 29.77  ? 172  ASP A OD2 1 
ATOM   1340 N N   . GLN A 1 172 ? -61.107 35.065 -25.565 1.00 25.43  ? 173  GLN A N   1 
ATOM   1341 C CA  . GLN A 1 172 ? -60.061 34.219 -25.064 1.00 26.16  ? 173  GLN A CA  1 
ATOM   1342 C C   . GLN A 1 172 ? -59.978 34.442 -23.544 1.00 27.13  ? 173  GLN A C   1 
ATOM   1343 O O   . GLN A 1 172 ? -59.896 33.516 -22.791 1.00 30.64  ? 173  GLN A O   1 
ATOM   1344 C CB  . GLN A 1 172 ? -58.718 34.539 -25.709 1.00 26.63  ? 173  GLN A CB  1 
ATOM   1345 C CG  . GLN A 1 172 ? -58.678 34.399 -27.230 1.00 27.14  ? 173  GLN A CG  1 
ATOM   1346 C CD  . GLN A 1 172 ? -57.421 34.954 -27.849 1.00 27.93  ? 173  GLN A CD  1 
ATOM   1347 O OE1 . GLN A 1 172 ? -56.409 35.207 -27.174 1.00 23.30  ? 173  GLN A OE1 1 
ATOM   1348 N NE2 . GLN A 1 172 ? -57.453 35.100 -29.180 1.00 33.08  ? 173  GLN A NE2 1 
ATOM   1349 N N   . ARG A 1 173 ? -60.000 35.691 -23.110 1.00 28.93  ? 174  ARG A N   1 
ATOM   1350 C CA  . ARG A 1 173 ? -59.910 36.029 -21.694 1.00 28.67  ? 174  ARG A CA  1 
ATOM   1351 C C   . ARG A 1 173 ? -60.996 35.360 -20.878 1.00 26.06  ? 174  ARG A C   1 
ATOM   1352 O O   . ARG A 1 173 ? -60.703 34.923 -19.776 1.00 22.58  ? 174  ARG A O   1 
ATOM   1353 C CB  . ARG A 1 173 ? -59.990 37.526 -21.469 1.00 26.90  ? 174  ARG A CB  1 
ATOM   1354 C CG  . ARG A 1 173 ? -59.959 37.948 -19.997 1.00 28.10  ? 174  ARG A CG  1 
ATOM   1355 C CD  . ARG A 1 173 ? -60.273 39.444 -19.844 1.00 27.83  ? 174  ARG A CD  1 
ATOM   1356 N NE  . ARG A 1 173 ? -59.146 40.217 -20.242 1.00 25.40  ? 174  ARG A NE  1 
ATOM   1357 C CZ  . ARG A 1 173 ? -59.096 41.543 -20.362 1.00 30.48  ? 174  ARG A CZ  1 
ATOM   1358 N NH1 . ARG A 1 173 ? -60.140 42.331 -20.197 1.00 30.90  ? 174  ARG A NH1 1 
ATOM   1359 N NH2 . ARG A 1 173 ? -57.928 42.101 -20.649 1.00 32.98  ? 174  ARG A NH2 1 
ATOM   1360 N N   . MET A 1 174 ? -62.212 35.277 -21.429 1.00 27.04  ? 175  MET A N   1 
ATOM   1361 C CA  . MET A 1 174 ? -63.337 34.679 -20.713 1.00 30.93  ? 175  MET A CA  1 
ATOM   1362 C C   . MET A 1 174 ? -63.156 33.188 -20.556 1.00 32.94  ? 175  MET A C   1 
ATOM   1363 O O   . MET A 1 174 ? -63.560 32.619 -19.528 1.00 34.53  ? 175  MET A O   1 
ATOM   1364 C CB  . MET A 1 174 ? -64.668 34.938 -21.395 1.00 33.45  ? 175  MET A CB  1 
ATOM   1365 C CG  . MET A 1 174 ? -65.861 34.515 -20.520 1.00 36.60  ? 175  MET A CG  1 
ATOM   1366 S SD  . MET A 1 174 ? -67.445 35.116 -21.177 1.00 40.51  ? 175  MET A SD  1 
ATOM   1367 C CE  . MET A 1 174 ? -67.357 36.727 -20.426 1.00 33.91  ? 175  MET A CE  1 
ATOM   1368 N N   . ALA A 1 175 ? -62.616 32.544 -21.583 1.00 30.96  ? 176  ALA A N   1 
ATOM   1369 C CA  . ALA A 1 175 ? -62.308 31.155 -21.474 1.00 32.72  ? 176  ALA A CA  1 
ATOM   1370 C C   . ALA A 1 175 ? -61.226 30.989 -20.406 1.00 27.84  ? 176  ALA A C   1 
ATOM   1371 O O   . ALA A 1 175 ? -61.204 30.029 -19.675 1.00 25.13  ? 176  ALA A O   1 
ATOM   1372 C CB  . ALA A 1 175 ? -61.813 30.595 -22.817 1.00 32.56  ? 176  ALA A CB  1 
ATOM   1373 N N   . LEU A 1 176 ? -60.280 31.897 -20.372 1.00 27.53  ? 177  LEU A N   1 
ATOM   1374 C CA  . LEU A 1 176 ? -59.191 31.787 -19.375 1.00 28.27  ? 177  LEU A CA  1 
ATOM   1375 C C   . LEU A 1 176 ? -59.773 32.042 -17.947 1.00 26.92  ? 177  LEU A C   1 
ATOM   1376 O O   . LEU A 1 176 ? -59.303 31.464 -17.010 1.00 23.15  ? 177  LEU A O   1 
ATOM   1377 C CB  . LEU A 1 176 ? -58.062 32.773 -19.636 1.00 27.11  ? 177  LEU A CB  1 
ATOM   1378 C CG  . LEU A 1 176 ? -57.193 32.644 -20.872 1.00 29.54  ? 177  LEU A CG  1 
ATOM   1379 C CD1 . LEU A 1 176 ? -56.162 33.758 -20.847 1.00 31.52  ? 177  LEU A CD1 1 
ATOM   1380 C CD2 . LEU A 1 176 ? -56.414 31.352 -20.932 1.00 34.83  ? 177  LEU A CD2 1 
ATOM   1381 N N   . GLN A 1 177 ? -60.788 32.897 -17.828 1.00 28.03  ? 178  GLN A N   1 
ATOM   1382 C CA  . GLN A 1 177 ? -61.510 33.095 -16.572 1.00 30.55  ? 178  GLN A CA  1 
ATOM   1383 C C   . GLN A 1 177 ? -62.190 31.806 -16.154 1.00 29.49  ? 178  GLN A C   1 
ATOM   1384 O O   . GLN A 1 177 ? -62.156 31.407 -14.982 1.00 31.87  ? 178  GLN A O   1 
ATOM   1385 C CB  . GLN A 1 177 ? -62.554 34.217 -16.706 1.00 33.05  ? 178  GLN A CB  1 
ATOM   1386 C CG  . GLN A 1 177 ? -63.335 34.635 -15.444 1.00 30.40  ? 178  GLN A CG  1 
ATOM   1387 C CD  . GLN A 1 177 ? -62.417 35.214 -14.398 1.00 31.70  ? 178  GLN A CD  1 
ATOM   1388 O OE1 . GLN A 1 177 ? -61.904 36.292 -14.581 1.00 32.91  ? 178  GLN A OE1 1 
ATOM   1389 N NE2 . GLN A 1 177 ? -62.120 34.438 -13.340 1.00 31.63  ? 178  GLN A NE2 1 
ATOM   1390 N N   . TRP A 1 178 ? -62.748 31.108 -17.110 1.00 26.14  ? 179  TRP A N   1 
ATOM   1391 C CA  . TRP A 1 178 ? -63.550 29.949 -16.775 1.00 24.75  ? 179  TRP A CA  1 
ATOM   1392 C C   . TRP A 1 178 ? -62.616 28.815 -16.394 1.00 25.56  ? 179  TRP A C   1 
ATOM   1393 O O   . TRP A 1 178 ? -62.914 28.063 -15.522 1.00 25.50  ? 179  TRP A O   1 
ATOM   1394 C CB  . TRP A 1 178 ? -64.368 29.554 -17.948 1.00 26.50  ? 179  TRP A CB  1 
ATOM   1395 C CG  . TRP A 1 178 ? -65.371 28.529 -17.720 1.00 29.75  ? 179  TRP A CG  1 
ATOM   1396 C CD1 . TRP A 1 178 ? -66.708 28.742 -17.495 1.00 30.75  ? 179  TRP A CD1 1 
ATOM   1397 C CD2 . TRP A 1 178 ? -65.171 27.110 -17.670 1.00 28.10  ? 179  TRP A CD2 1 
ATOM   1398 N NE1 . TRP A 1 178 ? -67.345 27.537 -17.331 1.00 28.40  ? 179  TRP A NE1 1 
ATOM   1399 C CE2 . TRP A 1 178 ? -66.438 26.526 -17.438 1.00 26.81  ? 179  TRP A CE2 1 
ATOM   1400 C CE3 . TRP A 1 178 ? -64.059 26.274 -17.851 1.00 29.89  ? 179  TRP A CE3 1 
ATOM   1401 C CZ2 . TRP A 1 178 ? -66.618 25.179 -17.332 1.00 26.13  ? 179  TRP A CZ2 1 
ATOM   1402 C CZ3 . TRP A 1 178 ? -64.241 24.932 -17.750 1.00 31.12  ? 179  TRP A CZ3 1 
ATOM   1403 C CH2 . TRP A 1 178 ? -65.512 24.391 -17.481 1.00 29.16  ? 179  TRP A CH2 1 
ATOM   1404 N N   . VAL A 1 179 ? -61.467 28.718 -17.009 1.00 26.63  ? 180  VAL A N   1 
ATOM   1405 C CA  . VAL A 1 179 ? -60.491 27.746 -16.600 1.00 27.82  ? 180  VAL A CA  1 
ATOM   1406 C C   . VAL A 1 179 ? -60.013 28.086 -15.173 1.00 29.27  ? 180  VAL A C   1 
ATOM   1407 O O   . VAL A 1 179 ? -59.894 27.249 -14.317 1.00 30.29  ? 180  VAL A O   1 
ATOM   1408 C CB  . VAL A 1 179 ? -59.268 27.813 -17.563 1.00 29.34  ? 180  VAL A CB  1 
ATOM   1409 C CG1 . VAL A 1 179 ? -58.042 27.106 -16.999 1.00 27.49  ? 180  VAL A CG1 1 
ATOM   1410 C CG2 . VAL A 1 179 ? -59.619 27.211 -18.905 1.00 30.68  ? 180  VAL A CG2 1 
ATOM   1411 N N   . HIS A 1 180 ? -59.639 29.319 -14.942 1.00 31.77  ? 181  HIS A N   1 
ATOM   1412 C CA  . HIS A 1 180 ? -59.253 29.730 -13.625 1.00 31.32  ? 181  HIS A CA  1 
ATOM   1413 C C   . HIS A 1 180 ? -60.294 29.275 -12.632 1.00 30.21  ? 181  HIS A C   1 
ATOM   1414 O O   . HIS A 1 180 ? -59.944 28.669 -11.671 1.00 25.67  ? 181  HIS A O   1 
ATOM   1415 C CB  . HIS A 1 180 ? -59.204 31.222 -13.539 1.00 35.21  ? 181  HIS A CB  1 
ATOM   1416 C CG  . HIS A 1 180 ? -58.818 31.721 -12.186 1.00 40.99  ? 181  HIS A CG  1 
ATOM   1417 N ND1 . HIS A 1 180 ? -59.751 32.145 -11.259 1.00 43.12  ? 181  HIS A ND1 1 
ATOM   1418 C CD2 . HIS A 1 180 ? -57.608 31.866 -11.599 1.00 43.09  ? 181  HIS A CD2 1 
ATOM   1419 C CE1 . HIS A 1 180 ? -59.130 32.563 -10.170 1.00 43.77  ? 181  HIS A CE1 1 
ATOM   1420 N NE2 . HIS A 1 180 ? -57.831 32.413 -10.354 1.00 46.09  ? 181  HIS A NE2 1 
ATOM   1421 N N   . ASP A 1 181 ? -61.559 29.534 -12.944 1.00 27.61  ? 182  ASP A N   1 
ATOM   1422 C CA  . ASP A 1 181 ? -62.645 29.310 -12.035 1.00 27.98  ? 182  ASP A CA  1 
ATOM   1423 C C   . ASP A 1 181 ? -63.080 27.812 -11.865 1.00 34.52  ? 182  ASP A C   1 
ATOM   1424 O O   . ASP A 1 181 ? -63.674 27.427 -10.821 1.00 34.94  ? 182  ASP A O   1 
ATOM   1425 C CB  . ASP A 1 181 ? -63.855 30.155 -12.413 1.00 24.65  ? 182  ASP A CB  1 
ATOM   1426 C CG  . ASP A 1 181 ? -63.677 31.649 -12.150 1.00 26.53  ? 182  ASP A CG  1 
ATOM   1427 O OD1 . ASP A 1 181 ? -62.790 32.071 -11.355 1.00 29.51  ? 182  ASP A OD1 1 
ATOM   1428 O OD2 . ASP A 1 181 ? -64.459 32.433 -12.751 1.00 31.81  ? 182  ASP A OD2 1 
ATOM   1429 N N   . ASN A 1 182 ? -62.808 26.975 -12.860 1.00 32.52  ? 183  ASN A N   1 
ATOM   1430 C CA  . ASN A 1 182 ? -63.361 25.629 -12.867 1.00 29.43  ? 183  ASN A CA  1 
ATOM   1431 C C   . ASN A 1 182 ? -62.383 24.508 -13.105 1.00 30.76  ? 183  ASN A C   1 
ATOM   1432 O O   . ASN A 1 182 ? -62.731 23.337 -12.903 1.00 35.58  ? 183  ASN A O   1 
ATOM   1433 C CB  . ASN A 1 182 ? -64.439 25.534 -13.917 1.00 30.64  ? 183  ASN A CB  1 
ATOM   1434 C CG  . ASN A 1 182 ? -65.610 26.410 -13.621 1.00 32.57  ? 183  ASN A CG  1 
ATOM   1435 O OD1 . ASN A 1 182 ? -66.519 26.055 -12.828 1.00 32.38  ? 183  ASN A OD1 1 
ATOM   1436 N ND2 . ASN A 1 182 ? -65.643 27.578 -14.294 1.00 34.14  ? 183  ASN A ND2 1 
ATOM   1437 N N   . ILE A 1 183 ? -61.161 24.773 -13.536 1.00 29.61  ? 184  ILE A N   1 
ATOM   1438 C CA  . ILE A 1 183 ? -60.339 23.641 -13.942 1.00 30.70  ? 184  ILE A CA  1 
ATOM   1439 C C   . ILE A 1 183 ? -60.033 22.722 -12.743 1.00 36.35  ? 184  ILE A C   1 
ATOM   1440 O O   . ILE A 1 183 ? -59.735 21.506 -12.934 1.00 37.08  ? 184  ILE A O   1 
ATOM   1441 C CB  . ILE A 1 183 ? -59.059 24.100 -14.654 1.00 30.63  ? 184  ILE A CB  1 
ATOM   1442 C CG1 . ILE A 1 183 ? -58.496 23.027 -15.581 1.00 33.58  ? 184  ILE A CG1 1 
ATOM   1443 C CG2 . ILE A 1 183 ? -58.005 24.577 -13.680 1.00 29.89  ? 184  ILE A CG2 1 
ATOM   1444 C CD1 . ILE A 1 183 ? -59.428 22.694 -16.774 1.00 35.82  ? 184  ILE A CD1 1 
ATOM   1445 N N   . GLN A 1 184 ? -60.072 23.277 -11.522 1.00 30.86  ? 185  GLN A N   1 
ATOM   1446 C CA  . GLN A 1 184 ? -59.848 22.449 -10.310 1.00 32.54  ? 185  GLN A CA  1 
ATOM   1447 C C   . GLN A 1 184 ? -60.758 21.219 -10.352 1.00 28.28  ? 185  GLN A C   1 
ATOM   1448 O O   . GLN A 1 184 ? -60.339 20.136 -9.989  1.00 26.80  ? 185  GLN A O   1 
ATOM   1449 C CB  . GLN A 1 184 ? -60.037 23.255 -8.971  1.00 32.04  ? 185  GLN A CB  1 
ATOM   1450 C CG  . GLN A 1 184 ? -61.457 23.604 -8.709  1.00 33.92  ? 185  GLN A CG  1 
ATOM   1451 C CD  . GLN A 1 184 ? -61.625 24.726 -7.739  1.00 37.48  ? 185  GLN A CD  1 
ATOM   1452 O OE1 . GLN A 1 184 ? -61.325 25.838 -8.078  1.00 37.66  ? 185  GLN A OE1 1 
ATOM   1453 N NE2 . GLN A 1 184 ? -62.175 24.449 -6.530  1.00 38.07  ? 185  GLN A NE2 1 
ATOM   1454 N N   . PHE A 1 185 ? -61.968 21.345 -10.876 1.00 29.20  ? 186  PHE A N   1 
ATOM   1455 C CA  . PHE A 1 185 ? -62.890 20.191 -10.836 1.00 31.24  ? 186  PHE A CA  1 
ATOM   1456 C C   . PHE A 1 185 ? -62.537 19.066 -11.809 1.00 36.16  ? 186  PHE A C   1 
ATOM   1457 O O   . PHE A 1 185 ? -63.103 17.933 -11.705 1.00 38.86  ? 186  PHE A O   1 
ATOM   1458 C CB  . PHE A 1 185 ? -64.312 20.641 -11.031 1.00 29.34  ? 186  PHE A CB  1 
ATOM   1459 C CG  . PHE A 1 185 ? -64.700 21.748 -10.102 1.00 32.94  ? 186  PHE A CG  1 
ATOM   1460 C CD1 . PHE A 1 185 ? -64.742 21.534 -8.713  1.00 37.82  ? 186  PHE A CD1 1 
ATOM   1461 C CD2 . PHE A 1 185 ? -64.988 23.004 -10.575 1.00 32.92  ? 186  PHE A CD2 1 
ATOM   1462 C CE1 . PHE A 1 185 ? -65.081 22.566 -7.817  1.00 36.39  ? 186  PHE A CE1 1 
ATOM   1463 C CE2 . PHE A 1 185 ? -65.296 24.042 -9.692  1.00 38.25  ? 186  PHE A CE2 1 
ATOM   1464 C CZ  . PHE A 1 185 ? -65.352 23.815 -8.302  1.00 34.60  ? 186  PHE A CZ  1 
ATOM   1465 N N   . PHE A 1 186 ? -61.625 19.368 -12.745 1.00 30.69  ? 187  PHE A N   1 
ATOM   1466 C CA  . PHE A 1 186 ? -61.188 18.379 -13.735 1.00 31.71  ? 187  PHE A CA  1 
ATOM   1467 C C   . PHE A 1 186 ? -59.832 17.893 -13.321 1.00 30.05  ? 187  PHE A C   1 
ATOM   1468 O O   . PHE A 1 186 ? -59.207 17.130 -14.008 1.00 27.19  ? 187  PHE A O   1 
ATOM   1469 C CB  . PHE A 1 186 ? -61.118 18.968 -15.148 1.00 31.29  ? 187  PHE A CB  1 
ATOM   1470 C CG  . PHE A 1 186 ? -62.444 19.484 -15.663 1.00 29.94  ? 187  PHE A CG  1 
ATOM   1471 C CD1 . PHE A 1 186 ? -62.914 20.692 -15.298 1.00 29.66  ? 187  PHE A CD1 1 
ATOM   1472 C CD2 . PHE A 1 186 ? -63.202 18.718 -16.545 1.00 35.16  ? 187  PHE A CD2 1 
ATOM   1473 C CE1 . PHE A 1 186 ? -64.116 21.159 -15.783 1.00 33.15  ? 187  PHE A CE1 1 
ATOM   1474 C CE2 . PHE A 1 186 ? -64.412 19.143 -17.011 1.00 31.93  ? 187  PHE A CE2 1 
ATOM   1475 C CZ  . PHE A 1 186 ? -64.872 20.387 -16.644 1.00 32.14  ? 187  PHE A CZ  1 
ATOM   1476 N N   . GLY A 1 187 ? -59.372 18.373 -12.178 1.00 32.51  ? 188  GLY A N   1 
ATOM   1477 C CA  . GLY A 1 187 ? -58.081 17.958 -11.624 1.00 32.06  ? 188  GLY A CA  1 
ATOM   1478 C C   . GLY A 1 187 ? -56.896 18.798 -11.999 1.00 31.97  ? 188  GLY A C   1 
ATOM   1479 O O   . GLY A 1 187 ? -55.713 18.410 -11.759 1.00 30.04  ? 188  GLY A O   1 
ATOM   1480 N N   . GLY A 1 188 ? -57.188 19.962 -12.568 1.00 34.65  ? 189  GLY A N   1 
ATOM   1481 C CA  . GLY A 1 188 ? -56.139 20.868 -12.938 1.00 33.95  ? 189  GLY A CA  1 
ATOM   1482 C C   . GLY A 1 188 ? -55.913 21.834 -11.810 1.00 31.59  ? 189  GLY A C   1 
ATOM   1483 O O   . GLY A 1 188 ? -56.841 22.226 -11.147 1.00 38.74  ? 189  GLY A O   1 
ATOM   1484 N N   . ASP A 1 189 ? -54.681 22.264 -11.691 1.00 29.23  ? 190  ASP A N   1 
ATOM   1485 C CA  . ASP A 1 189 ? -54.246 23.337 -10.792 1.00 28.97  ? 190  ASP A CA  1 
ATOM   1486 C C   . ASP A 1 189 ? -54.309 24.747 -11.448 1.00 30.16  ? 190  ASP A C   1 
ATOM   1487 O O   . ASP A 1 189 ? -53.425 25.105 -12.235 1.00 36.70  ? 190  ASP A O   1 
ATOM   1488 C CB  . ASP A 1 189 ? -52.809 22.989 -10.384 1.00 26.34  ? 190  ASP A CB  1 
ATOM   1489 C CG  . ASP A 1 189 ? -52.195 23.976 -9.441  1.00 28.54  ? 190  ASP A CG  1 
ATOM   1490 O OD1 . ASP A 1 189 ? -52.915 24.867 -8.986  1.00 28.79  ? 190  ASP A OD1 1 
ATOM   1491 O OD2 . ASP A 1 189 ? -50.961 23.868 -9.198  1.00 28.78  ? 190  ASP A OD2 1 
ATOM   1492 N N   . PRO A 1 190 ? -55.286 25.570 -11.076 1.00 27.93  ? 191  PRO A N   1 
ATOM   1493 C CA  . PRO A 1 190 ? -55.449 26.894 -11.585 1.00 27.19  ? 191  PRO A CA  1 
ATOM   1494 C C   . PRO A 1 190 ? -54.343 27.861 -11.287 1.00 29.85  ? 191  PRO A C   1 
ATOM   1495 O O   . PRO A 1 190 ? -54.322 28.953 -11.885 1.00 29.01  ? 191  PRO A O   1 
ATOM   1496 C CB  . PRO A 1 190 ? -56.733 27.374 -10.907 1.00 28.88  ? 191  PRO A CB  1 
ATOM   1497 C CG  . PRO A 1 190 ? -56.731 26.635 -9.568  1.00 28.43  ? 191  PRO A CG  1 
ATOM   1498 C CD  . PRO A 1 190 ? -56.210 25.304 -9.947  1.00 32.64  ? 191  PRO A CD  1 
ATOM   1499 N N   . LYS A 1 191 ? -53.465 27.504 -10.371 1.00 31.46  ? 192  LYS A N   1 
ATOM   1500 C CA  . LYS A 1 191 ? -52.296 28.318 -10.029 1.00 36.47  ? 192  LYS A CA  1 
ATOM   1501 C C   . LYS A 1 191 ? -51.132 27.983 -10.984 1.00 31.67  ? 192  LYS A C   1 
ATOM   1502 O O   . LYS A 1 191 ? -50.013 28.544 -10.883 1.00 27.56  ? 192  LYS A O   1 
ATOM   1503 C CB  . LYS A 1 191 ? -51.811 27.983 -8.578  1.00 37.73  ? 192  LYS A CB  1 
ATOM   1504 C CG  . LYS A 1 191 ? -52.850 27.975 -7.449  1.00 47.43  ? 192  LYS A CG  1 
ATOM   1505 C CD  . LYS A 1 191 ? -52.262 27.605 -6.020  1.00 48.21  ? 192  LYS A CD  1 
ATOM   1506 C CE  . LYS A 1 191 ? -51.688 26.180 -5.915  1.00 49.47  ? 192  LYS A CE  1 
ATOM   1507 N NZ  . LYS A 1 191 ? -52.804 25.198 -6.219  1.00 50.50  ? 192  LYS A NZ  1 
ATOM   1508 N N   . THR A 1 192 ? -51.330 26.989 -11.820 1.00 28.61  ? 193  THR A N   1 
ATOM   1509 C CA  . THR A 1 192 ? -50.226 26.579 -12.711 1.00 33.96  ? 193  THR A CA  1 
ATOM   1510 C C   . THR A 1 192 ? -50.765 26.428 -14.145 1.00 31.24  ? 193  THR A C   1 
ATOM   1511 O O   . THR A 1 192 ? -50.688 25.334 -14.750 1.00 28.83  ? 193  THR A O   1 
ATOM   1512 C CB  . THR A 1 192 ? -49.575 25.298 -12.201 1.00 35.03  ? 193  THR A CB  1 
ATOM   1513 O OG1 . THR A 1 192 ? -49.231 25.506 -10.842 1.00 42.49  ? 193  THR A OG1 1 
ATOM   1514 C CG2 . THR A 1 192 ? -48.324 25.029 -12.896 1.00 33.75  ? 193  THR A CG2 1 
ATOM   1515 N N   . VAL A 1 193 ? -51.392 27.504 -14.625 1.00 26.78  ? 194  VAL A N   1 
ATOM   1516 C CA  . VAL A 1 193 ? -51.825 27.554 -16.011 1.00 28.10  ? 194  VAL A CA  1 
ATOM   1517 C C   . VAL A 1 193 ? -50.800 28.169 -16.954 1.00 27.20  ? 194  VAL A C   1 
ATOM   1518 O O   . VAL A 1 193 ? -50.356 29.302 -16.764 1.00 32.24  ? 194  VAL A O   1 
ATOM   1519 C CB  . VAL A 1 193 ? -53.109 28.332 -16.098 1.00 29.37  ? 194  VAL A CB  1 
ATOM   1520 C CG1 . VAL A 1 193 ? -53.574 28.385 -17.551 1.00 32.64  ? 194  VAL A CG1 1 
ATOM   1521 C CG2 . VAL A 1 193 ? -54.153 27.621 -15.227 1.00 32.48  ? 194  VAL A CG2 1 
ATOM   1522 N N   . THR A 1 194 ? -50.386 27.421 -17.955 1.00 28.63  ? 195  THR A N   1 
ATOM   1523 C CA  . THR A 1 194 ? -49.588 27.973 -19.046 1.00 25.49  ? 195  THR A CA  1 
ATOM   1524 C C   . THR A 1 194 ? -50.482 28.266 -20.276 1.00 27.05  ? 195  THR A C   1 
ATOM   1525 O O   . THR A 1 194 ? -51.164 27.352 -20.753 1.00 28.57  ? 195  THR A O   1 
ATOM   1526 C CB  . THR A 1 194 ? -48.456 27.052 -19.405 1.00 26.98  ? 195  THR A CB  1 
ATOM   1527 O OG1 . THR A 1 194 ? -47.519 27.050 -18.330 1.00 29.30  ? 195  THR A OG1 1 
ATOM   1528 C CG2 . THR A 1 194 ? -47.685 27.607 -20.630 1.00 28.42  ? 195  THR A CG2 1 
ATOM   1529 N N   . ILE A 1 195 ? -50.561 29.534 -20.735 1.00 24.22  ? 196  ILE A N   1 
ATOM   1530 C CA  . ILE A 1 195 ? -51.127 29.781 -22.052 1.00 25.37  ? 196  ILE A CA  1 
ATOM   1531 C C   . ILE A 1 195 ? -50.095 29.562 -23.194 1.00 26.24  ? 196  ILE A C   1 
ATOM   1532 O O   . ILE A 1 195 ? -48.930 29.943 -23.089 1.00 23.77  ? 196  ILE A O   1 
ATOM   1533 C CB  . ILE A 1 195 ? -51.857 31.099 -22.171 1.00 26.37  ? 196  ILE A CB  1 
ATOM   1534 C CG1 . ILE A 1 195 ? -50.934 32.258 -21.962 1.00 27.49  ? 196  ILE A CG1 1 
ATOM   1535 C CG2 . ILE A 1 195 ? -53.000 31.113 -21.165 1.00 29.76  ? 196  ILE A CG2 1 
ATOM   1536 C CD1 . ILE A 1 195 ? -51.599 33.595 -22.140 1.00 28.02  ? 196  ILE A CD1 1 
ATOM   1537 N N   . PHE A 1 196 ? -50.513 28.854 -24.245 1.00 27.37  ? 197  PHE A N   1 
ATOM   1538 C CA  . PHE A 1 196 ? -49.621 28.644 -25.404 1.00 26.37  ? 197  PHE A CA  1 
ATOM   1539 C C   . PHE A 1 196 ? -50.350 28.779 -26.713 1.00 25.65  ? 197  PHE A C   1 
ATOM   1540 O O   . PHE A 1 196 ? -51.531 28.560 -26.763 1.00 26.05  ? 197  PHE A O   1 
ATOM   1541 C CB  . PHE A 1 196 ? -48.778 27.406 -25.280 1.00 26.05  ? 197  PHE A CB  1 
ATOM   1542 C CG  . PHE A 1 196 ? -49.469 26.109 -25.529 1.00 26.47  ? 197  PHE A CG  1 
ATOM   1543 C CD1 . PHE A 1 196 ? -50.613 25.760 -24.851 1.00 27.91  ? 197  PHE A CD1 1 
ATOM   1544 C CD2 . PHE A 1 196 ? -48.836 25.132 -26.341 1.00 25.09  ? 197  PHE A CD2 1 
ATOM   1545 C CE1 . PHE A 1 196 ? -51.190 24.494 -25.039 1.00 27.02  ? 197  PHE A CE1 1 
ATOM   1546 C CE2 . PHE A 1 196 ? -49.422 23.886 -26.573 1.00 26.62  ? 197  PHE A CE2 1 
ATOM   1547 C CZ  . PHE A 1 196 ? -50.603 23.562 -25.896 1.00 28.01  ? 197  PHE A CZ  1 
ATOM   1548 N N   . GLY A 1 197 ? -49.677 29.245 -27.754 1.00 27.16  ? 198  GLY A N   1 
ATOM   1549 C CA  . GLY A 1 197 ? -50.360 29.494 -29.033 1.00 26.42  ? 198  GLY A CA  1 
ATOM   1550 C C   . GLY A 1 197 ? -49.372 29.759 -30.152 1.00 26.89  ? 198  GLY A C   1 
ATOM   1551 O O   . GLY A 1 197 ? -48.209 30.110 -29.897 1.00 24.82  ? 198  GLY A O   1 
ATOM   1552 N N   . GLU A 1 198 ? -49.856 29.568 -31.378 1.00 25.91  ? 199  GLU A N   1 
ATOM   1553 C CA  . GLU A 1 198 ? -49.055 29.738 -32.587 1.00 26.96  ? 199  GLU A CA  1 
ATOM   1554 C C   . GLU A 1 198 ? -49.491 30.869 -33.468 1.00 23.83  ? 199  GLU A C   1 
ATOM   1555 O O   . GLU A 1 198 ? -50.664 31.082 -33.684 1.00 23.01  ? 199  GLU A O   1 
ATOM   1556 C CB  . GLU A 1 198 ? -48.922 28.436 -33.369 1.00 28.20  ? 199  GLU A CB  1 
ATOM   1557 C CG  . GLU A 1 198 ? -47.873 28.503 -34.478 1.00 26.91  ? 199  GLU A CG  1 
ATOM   1558 C CD  . GLU A 1 198 ? -48.515 28.855 -35.812 1.00 28.28  ? 199  GLU A CD  1 
ATOM   1559 O OE1 . GLU A 1 198 ? -49.782 28.879 -35.887 1.00 29.57  ? 199  GLU A OE1 1 
ATOM   1560 O OE2 . GLU A 1 198 ? -47.773 29.105 -36.798 1.00 31.63  ? 199  GLU A OE2 1 
ATOM   1561 N N   . SER A 1 199 ? -48.508 31.628 -33.932 1.00 25.24  ? 200  SER A N   1 
ATOM   1562 C CA  . SER A 1 199 ? -48.744 32.722 -34.847 1.00 25.88  ? 200  SER A CA  1 
ATOM   1563 C C   . SER A 1 199 ? -49.730 33.760 -34.214 1.00 23.71  ? 200  SER A C   1 
ATOM   1564 O O   . SER A 1 199 ? -49.412 34.340 -33.206 1.00 27.76  ? 200  SER A O   1 
ATOM   1565 C CB  . SER A 1 199 ? -49.209 32.163 -36.222 1.00 26.59  ? 200  SER A CB  1 
ATOM   1566 O OG  . SER A 1 199 ? -49.333 33.256 -37.163 1.00 31.94  ? 200  SER A OG  1 
ATOM   1567 N N   . ALA A 1 200 ? -50.909 34.005 -34.766 1.00 21.35  ? 201  ALA A N   1 
ATOM   1568 C CA  . ALA A 1 200 ? -51.849 34.917 -34.130 1.00 22.40  ? 201  ALA A CA  1 
ATOM   1569 C C   . ALA A 1 200 ? -52.197 34.465 -32.670 1.00 24.15  ? 201  ALA A C   1 
ATOM   1570 O O   . ALA A 1 200 ? -52.625 35.266 -31.854 1.00 25.80  ? 201  ALA A O   1 
ATOM   1571 C CB  . ALA A 1 200 ? -53.143 35.008 -34.952 1.00 20.21  ? 201  ALA A CB  1 
ATOM   1572 N N   . GLY A 1 201 ? -52.105 33.179 -32.414 1.00 25.42  ? 202  GLY A N   1 
ATOM   1573 C CA  . GLY A 1 201 ? -52.284 32.625 -31.077 1.00 27.15  ? 202  GLY A CA  1 
ATOM   1574 C C   . GLY A 1 201 ? -51.064 32.965 -30.252 1.00 27.11  ? 202  GLY A C   1 
ATOM   1575 O O   . GLY A 1 201 ? -51.191 33.279 -29.099 1.00 23.35  ? 202  GLY A O   1 
ATOM   1576 N N   . GLY A 1 202 ? -49.867 32.894 -30.838 1.00 25.85  ? 203  GLY A N   1 
ATOM   1577 C CA  . GLY A 1 202 ? -48.693 33.381 -30.148 1.00 25.26  ? 203  GLY A CA  1 
ATOM   1578 C C   . GLY A 1 202 ? -48.784 34.878 -29.807 1.00 27.14  ? 203  GLY A C   1 
ATOM   1579 O O   . GLY A 1 202 ? -48.370 35.315 -28.736 1.00 27.13  ? 203  GLY A O   1 
ATOM   1580 N N   . ALA A 1 203 ? -49.301 35.674 -30.746 1.00 24.41  ? 204  ALA A N   1 
ATOM   1581 C CA  . ALA A 1 203 ? -49.401 37.064 -30.497 1.00 25.73  ? 204  ALA A CA  1 
ATOM   1582 C C   . ALA A 1 203 ? -50.481 37.337 -29.383 1.00 23.83  ? 204  ALA A C   1 
ATOM   1583 O O   . ALA A 1 203 ? -50.386 38.282 -28.574 1.00 21.46  ? 204  ALA A O   1 
ATOM   1584 C CB  . ALA A 1 203 ? -49.676 37.855 -31.809 1.00 22.68  ? 204  ALA A CB  1 
ATOM   1585 N N   . SER A 1 204 ? -51.565 36.606 -29.478 1.00 22.99  ? 205  SER A N   1 
ATOM   1586 C CA  . SER A 1 204 ? -52.639 36.688 -28.495 1.00 24.53  ? 205  SER A CA  1 
ATOM   1587 C C   . SER A 1 204 ? -52.012 36.458 -27.077 1.00 24.53  ? 205  SER A C   1 
ATOM   1588 O O   . SER A 1 204 ? -52.300 37.199 -26.135 1.00 22.39  ? 205  SER A O   1 
ATOM   1589 C CB  . SER A 1 204 ? -53.684 35.583 -28.765 1.00 25.10  ? 205  SER A CB  1 
ATOM   1590 O OG  . SER A 1 204 ? -54.595 35.893 -29.840 1.00 24.57  ? 205  SER A OG  1 
ATOM   1591 N N   . VAL A 1 205 ? -51.201 35.407 -26.954 1.00 21.51  ? 206  VAL A N   1 
ATOM   1592 C CA  . VAL A 1 205 ? -50.540 35.067 -25.688 1.00 24.41  ? 206  VAL A CA  1 
ATOM   1593 C C   . VAL A 1 205 ? -49.788 36.304 -25.171 1.00 24.89  ? 206  VAL A C   1 
ATOM   1594 O O   . VAL A 1 205 ? -50.038 36.787 -24.061 1.00 28.55  ? 206  VAL A O   1 
ATOM   1595 C CB  . VAL A 1 205 ? -49.627 33.860 -25.852 1.00 22.73  ? 206  VAL A CB  1 
ATOM   1596 C CG1 . VAL A 1 205 ? -48.682 33.788 -24.702 1.00 24.75  ? 206  VAL A CG1 1 
ATOM   1597 C CG2 . VAL A 1 205 ? -50.442 32.554 -25.995 1.00 23.64  ? 206  VAL A CG2 1 
ATOM   1598 N N   . GLY A 1 206 ? -48.991 36.893 -26.031 1.00 22.00  ? 207  GLY A N   1 
ATOM   1599 C CA  . GLY A 1 206 ? -48.239 38.118 -25.700 1.00 23.54  ? 207  GLY A CA  1 
ATOM   1600 C C   . GLY A 1 206 ? -49.141 39.267 -25.336 1.00 21.38  ? 207  GLY A C   1 
ATOM   1601 O O   . GLY A 1 206 ? -48.773 40.112 -24.544 1.00 20.70  ? 207  GLY A O   1 
ATOM   1602 N N   . MET A 1 207 ? -50.323 39.267 -25.911 1.00 20.64  ? 208  MET A N   1 
ATOM   1603 C CA  . MET A 1 207 ? -51.273 40.275 -25.635 1.00 23.43  ? 208  MET A CA  1 
ATOM   1604 C C   . MET A 1 207 ? -51.914 40.122 -24.230 1.00 25.68  ? 208  MET A C   1 
ATOM   1605 O O   . MET A 1 207 ? -52.231 41.125 -23.604 1.00 29.09  ? 208  MET A O   1 
ATOM   1606 C CB  . MET A 1 207 ? -52.331 40.347 -26.723 1.00 23.19  ? 208  MET A CB  1 
ATOM   1607 C CG  . MET A 1 207 ? -51.829 41.026 -28.022 1.00 26.87  ? 208  MET A CG  1 
ATOM   1608 S SD  . MET A 1 207 ? -52.954 40.813 -29.464 1.00 25.27  ? 208  MET A SD  1 
ATOM   1609 C CE  . MET A 1 207 ? -52.004 41.760 -30.647 1.00 26.62  ? 208  MET A CE  1 
ATOM   1610 N N   . HIS A 1 208 ? -52.083 38.896 -23.764 1.00 23.83  ? 209  HIS A N   1 
ATOM   1611 C CA  . HIS A 1 208 ? -52.619 38.643 -22.461 1.00 25.80  ? 209  HIS A CA  1 
ATOM   1612 C C   . HIS A 1 208 ? -51.540 38.911 -21.403 1.00 26.93  ? 209  HIS A C   1 
ATOM   1613 O O   . HIS A 1 208 ? -51.872 39.336 -20.320 1.00 27.21  ? 209  HIS A O   1 
ATOM   1614 C CB  . HIS A 1 208 ? -53.148 37.243 -22.337 1.00 24.38  ? 209  HIS A CB  1 
ATOM   1615 C CG  . HIS A 1 208 ? -54.387 37.019 -23.156 1.00 26.07  ? 209  HIS A CG  1 
ATOM   1616 N ND1 . HIS A 1 208 ? -55.522 37.772 -22.988 1.00 25.43  ? 209  HIS A ND1 1 
ATOM   1617 C CD2 . HIS A 1 208 ? -54.644 36.175 -24.187 1.00 23.88  ? 209  HIS A CD2 1 
ATOM   1618 C CE1 . HIS A 1 208 ? -56.460 37.355 -23.811 1.00 25.32  ? 209  HIS A CE1 1 
ATOM   1619 N NE2 . HIS A 1 208 ? -55.946 36.400 -24.568 1.00 24.76  ? 209  HIS A NE2 1 
ATOM   1620 N N   . ILE A 1 209 ? -50.276 38.748 -21.766 1.00 26.50  ? 210  ILE A N   1 
ATOM   1621 C CA  . ILE A 1 209 ? -49.151 39.167 -20.918 1.00 25.89  ? 210  ILE A CA  1 
ATOM   1622 C C   . ILE A 1 209 ? -49.116 40.659 -20.714 1.00 27.64  ? 210  ILE A C   1 
ATOM   1623 O O   . ILE A 1 209 ? -48.727 41.111 -19.644 1.00 27.46  ? 210  ILE A O   1 
ATOM   1624 C CB  . ILE A 1 209 ? -47.838 38.759 -21.551 1.00 26.33  ? 210  ILE A CB  1 
ATOM   1625 C CG1 . ILE A 1 209 ? -47.721 37.263 -21.483 1.00 25.31  ? 210  ILE A CG1 1 
ATOM   1626 C CG2 . ILE A 1 209 ? -46.670 39.471 -20.891 1.00 30.46  ? 210  ILE A CG2 1 
ATOM   1627 C CD1 . ILE A 1 209 ? -46.487 36.702 -22.123 1.00 26.97  ? 210  ILE A CD1 1 
ATOM   1628 N N   . LEU A 1 210 ? -49.550 41.436 -21.712 1.00 26.63  ? 211  LEU A N   1 
ATOM   1629 C CA  . LEU A 1 210 ? -49.410 42.870 -21.597 1.00 26.00  ? 211  LEU A CA  1 
ATOM   1630 C C   . LEU A 1 210 ? -50.637 43.493 -20.951 1.00 27.03  ? 211  LEU A C   1 
ATOM   1631 O O   . LEU A 1 210 ? -50.532 44.459 -20.157 1.00 25.99  ? 211  LEU A O   1 
ATOM   1632 C CB  . LEU A 1 210 ? -49.228 43.482 -22.975 1.00 27.23  ? 211  LEU A CB  1 
ATOM   1633 C CG  . LEU A 1 210 ? -47.827 43.510 -23.592 1.00 32.78  ? 211  LEU A CG  1 
ATOM   1634 C CD1 . LEU A 1 210 ? -48.082 43.620 -25.065 1.00 35.69  ? 211  LEU A CD1 1 
ATOM   1635 C CD2 . LEU A 1 210 ? -47.014 44.723 -23.162 1.00 36.24  ? 211  LEU A CD2 1 
ATOM   1636 N N   . SER A 1 211 ? -51.808 43.003 -21.346 1.00 23.78  ? 212  SER A N   1 
ATOM   1637 C CA  . SER A 1 211 ? -53.069 43.515 -20.863 1.00 26.29  ? 212  SER A CA  1 
ATOM   1638 C C   . SER A 1 211 ? -53.360 43.234 -19.358 1.00 29.29  ? 212  SER A C   1 
ATOM   1639 O O   . SER A 1 211 ? -53.553 42.047 -18.982 1.00 29.49  ? 212  SER A O   1 
ATOM   1640 C CB  . SER A 1 211 ? -54.200 42.868 -21.626 1.00 26.19  ? 212  SER A CB  1 
ATOM   1641 O OG  . SER A 1 211 ? -55.423 43.458 -21.254 1.00 23.76  ? 212  SER A OG  1 
ATOM   1642 N N   . PRO A 1 212 ? -53.434 44.314 -18.533 1.00 32.98  ? 213  PRO A N   1 
ATOM   1643 C CA  . PRO A 1 212 ? -53.775 44.291 -17.080 1.00 31.70  ? 213  PRO A CA  1 
ATOM   1644 C C   . PRO A 1 212 ? -54.967 43.434 -16.792 1.00 29.30  ? 213  PRO A C   1 
ATOM   1645 O O   . PRO A 1 212 ? -54.912 42.585 -15.928 1.00 24.94  ? 213  PRO A O   1 
ATOM   1646 C CB  . PRO A 1 212 ? -54.072 45.777 -16.769 1.00 32.19  ? 213  PRO A CB  1 
ATOM   1647 C CG  . PRO A 1 212 ? -53.239 46.533 -17.754 1.00 33.15  ? 213  PRO A CG  1 
ATOM   1648 C CD  . PRO A 1 212 ? -53.311 45.716 -19.014 1.00 32.89  ? 213  PRO A CD  1 
ATOM   1649 N N   . GLY A 1 213 ? -56.008 43.523 -17.625 1.00 29.20  ? 214  GLY A N   1 
ATOM   1650 C CA  . GLY A 1 213 ? -57.190 42.664 -17.394 1.00 27.00  ? 214  GLY A CA  1 
ATOM   1651 C C   . GLY A 1 213 ? -57.037 41.160 -17.601 1.00 29.29  ? 214  GLY A C   1 
ATOM   1652 O O   . GLY A 1 213 ? -57.965 40.418 -17.225 1.00 32.67  ? 214  GLY A O   1 
ATOM   1653 N N   . SER A 1 214 ? -55.922 40.697 -18.214 1.00 25.65  ? 215  SER A N   1 
ATOM   1654 C CA  . SER A 1 214 ? -55.688 39.269 -18.453 1.00 25.66  ? 215  SER A CA  1 
ATOM   1655 C C   . SER A 1 214 ? -54.590 38.666 -17.605 1.00 25.03  ? 215  SER A C   1 
ATOM   1656 O O   . SER A 1 214 ? -54.570 37.457 -17.390 1.00 24.69  ? 215  SER A O   1 
ATOM   1657 C CB  . SER A 1 214 ? -55.324 38.981 -19.984 1.00 26.01  ? 215  SER A CB  1 
ATOM   1658 O OG  . SER A 1 214 ? -56.410 39.282 -20.868 1.00 24.38  ? 215  SER A OG  1 
ATOM   1659 N N   . ARG A 1 215 ? -53.625 39.471 -17.200 1.00 26.08  ? 216  ARG A N   1 
ATOM   1660 C CA  . ARG A 1 215 ? -52.430 38.920 -16.535 1.00 27.75  ? 216  ARG A CA  1 
ATOM   1661 C C   . ARG A 1 215 ? -52.674 37.954 -15.396 1.00 27.97  ? 216  ARG A C   1 
ATOM   1662 O O   . ARG A 1 215 ? -51.821 37.111 -15.129 1.00 26.05  ? 216  ARG A O   1 
ATOM   1663 C CB  . ARG A 1 215 ? -51.571 40.021 -15.873 1.00 30.00  ? 216  ARG A CB  1 
ATOM   1664 C CG  . ARG A 1 215 ? -51.324 41.226 -16.735 1.00 33.94  ? 216  ARG A CG  1 
ATOM   1665 C CD  . ARG A 1 215 ? -50.297 42.172 -16.173 1.00 33.45  ? 216  ARG A CD  1 
ATOM   1666 N NE  . ARG A 1 215 ? -50.179 43.294 -17.093 1.00 31.04  ? 216  ARG A NE  1 
ATOM   1667 C CZ  . ARG A 1 215 ? -49.670 44.463 -16.789 1.00 33.57  ? 216  ARG A CZ  1 
ATOM   1668 N NH1 . ARG A 1 215 ? -49.179 44.691 -15.555 1.00 33.45  ? 216  ARG A NH1 1 
ATOM   1669 N NH2 . ARG A 1 215 ? -49.622 45.405 -17.727 1.00 34.29  ? 216  ARG A NH2 1 
ATOM   1670 N N   . ASP A 1 216 ? -53.727 38.168 -14.613 1.00 28.00  ? 217  ASP A N   1 
ATOM   1671 C CA  . ASP A 1 216 ? -53.785 37.429 -13.339 1.00 31.18  ? 217  ASP A CA  1 
ATOM   1672 C C   . ASP A 1 216 ? -54.330 36.052 -13.574 1.00 34.07  ? 217  ASP A C   1 
ATOM   1673 O O   . ASP A 1 216 ? -54.396 35.287 -12.629 1.00 37.02  ? 217  ASP A O   1 
ATOM   1674 C CB  . ASP A 1 216 ? -54.719 38.113 -12.313 1.00 31.48  ? 217  ASP A CB  1 
ATOM   1675 C CG  . ASP A 1 216 ? -54.284 39.519 -11.948 1.00 30.38  ? 217  ASP A CG  1 
ATOM   1676 O OD1 . ASP A 1 216 ? -53.222 39.972 -12.380 1.00 33.28  ? 217  ASP A OD1 1 
ATOM   1677 O OD2 . ASP A 1 216 ? -55.062 40.221 -11.304 1.00 30.93  ? 217  ASP A OD2 1 
ATOM   1678 N N   . LEU A 1 217 ? -54.862 35.789 -14.782 1.00 28.44  ? 218  LEU A N   1 
ATOM   1679 C CA  . LEU A 1 217 ? -55.548 34.573 -15.058 1.00 25.75  ? 218  LEU A CA  1 
ATOM   1680 C C   . LEU A 1 217 ? -54.620 33.465 -15.529 1.00 26.41  ? 218  LEU A C   1 
ATOM   1681 O O   . LEU A 1 217 ? -55.088 32.405 -15.831 1.00 32.04  ? 218  LEU A O   1 
ATOM   1682 C CB  . LEU A 1 217 ? -56.603 34.774 -16.114 1.00 28.11  ? 218  LEU A CB  1 
ATOM   1683 C CG  . LEU A 1 217 ? -57.660 35.837 -15.844 1.00 29.49  ? 218  LEU A CG  1 
ATOM   1684 C CD1 . LEU A 1 217 ? -58.599 35.957 -17.033 1.00 30.39  ? 218  LEU A CD1 1 
ATOM   1685 C CD2 . LEU A 1 217 ? -58.460 35.552 -14.589 1.00 27.68  ? 218  LEU A CD2 1 
ATOM   1686 N N   . PHE A 1 218 ? -53.312 33.631 -15.536 1.00 24.30  ? 219  PHE A N   1 
ATOM   1687 C CA  . PHE A 1 218 ? -52.524 32.477 -15.941 1.00 26.06  ? 219  PHE A CA  1 
ATOM   1688 C C   . PHE A 1 218 ? -51.189 32.644 -15.302 1.00 25.00  ? 219  PHE A C   1 
ATOM   1689 O O   . PHE A 1 218 ? -50.887 33.696 -14.843 1.00 26.01  ? 219  PHE A O   1 
ATOM   1690 C CB  . PHE A 1 218 ? -52.415 32.398 -17.510 1.00 27.50  ? 219  PHE A CB  1 
ATOM   1691 C CG  . PHE A 1 218 ? -51.771 33.588 -18.123 1.00 24.68  ? 219  PHE A CG  1 
ATOM   1692 C CD1 . PHE A 1 218 ? -52.519 34.713 -18.415 1.00 28.62  ? 219  PHE A CD1 1 
ATOM   1693 C CD2 . PHE A 1 218 ? -50.450 33.611 -18.371 1.00 25.66  ? 219  PHE A CD2 1 
ATOM   1694 C CE1 . PHE A 1 218 ? -51.915 35.855 -18.946 1.00 27.62  ? 219  PHE A CE1 1 
ATOM   1695 C CE2 . PHE A 1 218 ? -49.834 34.755 -18.934 1.00 29.77  ? 219  PHE A CE2 1 
ATOM   1696 C CZ  . PHE A 1 218 ? -50.558 35.879 -19.190 1.00 25.44  ? 219  PHE A CZ  1 
ATOM   1697 N N   . ARG A 1 219 ? -50.345 31.626 -15.320 1.00 25.79  ? 220  ARG A N   1 
ATOM   1698 C CA  . ARG A 1 219 ? -49.101 31.709 -14.598 1.00 25.40  ? 220  ARG A CA  1 
ATOM   1699 C C   . ARG A 1 219 ? -47.941 32.010 -15.526 1.00 26.72  ? 220  ARG A C   1 
ATOM   1700 O O   . ARG A 1 219 ? -47.000 32.799 -15.212 1.00 26.21  ? 220  ARG A O   1 
ATOM   1701 C CB  . ARG A 1 219 ? -48.879 30.323 -13.942 1.00 28.58  ? 220  ARG A CB  1 
ATOM   1702 C CG  . ARG A 1 219 ? -47.521 30.062 -13.292 1.00 30.43  ? 220  ARG A CG  1 
ATOM   1703 C CD  . ARG A 1 219 ? -47.383 30.907 -12.055 1.00 37.52  ? 220  ARG A CD  1 
ATOM   1704 N NE  . ARG A 1 219 ? -46.315 30.439 -11.138 1.00 48.75  ? 220  ARG A NE  1 
ATOM   1705 C CZ  . ARG A 1 219 ? -46.463 29.539 -10.156 1.00 46.25  ? 220  ARG A CZ  1 
ATOM   1706 N NH1 . ARG A 1 219 ? -47.620 28.930 -9.919  1.00 48.95  ? 220  ARG A NH1 1 
ATOM   1707 N NH2 . ARG A 1 219 ? -45.438 29.265 -9.385  1.00 48.26  ? 220  ARG A NH2 1 
ATOM   1708 N N   . ARG A 1 220 ? -47.924 31.267 -16.625 1.00 26.85  ? 221  ARG A N   1 
ATOM   1709 C CA  . ARG A 1 220 ? -46.845 31.434 -17.601 1.00 27.80  ? 221  ARG A CA  1 
ATOM   1710 C C   . ARG A 1 220 ? -47.228 31.175 -19.065 1.00 25.18  ? 221  ARG A C   1 
ATOM   1711 O O   . ARG A 1 220 ? -48.401 30.952 -19.342 1.00 22.88  ? 221  ARG A O   1 
ATOM   1712 C CB  . ARG A 1 220 ? -45.583 30.777 -17.139 1.00 28.33  ? 221  ARG A CB  1 
ATOM   1713 C CG  . ARG A 1 220 ? -45.528 29.302 -16.948 1.00 28.72  ? 221  ARG A CG  1 
ATOM   1714 C CD  . ARG A 1 220 ? -44.217 28.978 -16.160 1.00 30.46  ? 221  ARG A CD  1 
ATOM   1715 N NE  . ARG A 1 220 ? -44.591 27.928 -15.277 1.00 44.13  ? 221  ARG A NE  1 
ATOM   1716 C CZ  . ARG A 1 220 ? -44.399 27.840 -13.980 1.00 40.88  ? 221  ARG A CZ  1 
ATOM   1717 N NH1 . ARG A 1 220 ? -43.656 28.670 -13.308 1.00 36.27  ? 221  ARG A NH1 1 
ATOM   1718 N NH2 . ARG A 1 220 ? -44.993 26.834 -13.380 1.00 46.88  ? 221  ARG A NH2 1 
ATOM   1719 N N   . ALA A 1 221 ? -46.296 31.410 -19.990 1.00 24.95  ? 222  ALA A N   1 
ATOM   1720 C CA  . ALA A 1 221 ? -46.638 31.551 -21.434 1.00 25.59  ? 222  ALA A CA  1 
ATOM   1721 C C   . ALA A 1 221 ? -45.608 31.025 -22.374 1.00 24.90  ? 222  ALA A C   1 
ATOM   1722 O O   . ALA A 1 221 ? -44.385 31.110 -22.128 1.00 24.18  ? 222  ALA A O   1 
ATOM   1723 C CB  . ALA A 1 221 ? -46.961 32.979 -21.806 1.00 25.07  ? 222  ALA A CB  1 
ATOM   1724 N N   . ILE A 1 222 ? -46.151 30.421 -23.427 1.00 26.62  ? 223  ILE A N   1 
ATOM   1725 C CA  . ILE A 1 222 ? -45.402 29.936 -24.582 1.00 27.32  ? 223  ILE A CA  1 
ATOM   1726 C C   . ILE A 1 222 ? -45.930 30.603 -25.879 1.00 24.38  ? 223  ILE A C   1 
ATOM   1727 O O   . ILE A 1 222 ? -47.136 30.545 -26.162 1.00 23.30  ? 223  ILE A O   1 
ATOM   1728 C CB  . ILE A 1 222 ? -45.529 28.437 -24.657 1.00 27.99  ? 223  ILE A CB  1 
ATOM   1729 C CG1 . ILE A 1 222 ? -44.901 27.781 -23.390 1.00 29.65  ? 223  ILE A CG1 1 
ATOM   1730 C CG2 . ILE A 1 222 ? -44.811 27.899 -25.904 1.00 27.37  ? 223  ILE A CG2 1 
ATOM   1731 C CD1 . ILE A 1 222 ? -45.059 26.255 -23.386 1.00 29.06  ? 223  ILE A CD1 1 
ATOM   1732 N N   . LEU A 1 223 ? -45.027 31.228 -26.615 1.00 21.06  ? 224  LEU A N   1 
ATOM   1733 C CA  . LEU A 1 223 ? -45.317 31.926 -27.878 1.00 22.90  ? 224  LEU A CA  1 
ATOM   1734 C C   . LEU A 1 223 ? -44.564 31.247 -29.038 1.00 23.76  ? 224  LEU A C   1 
ATOM   1735 O O   . LEU A 1 223 ? -43.349 31.242 -29.087 1.00 22.47  ? 224  LEU A O   1 
ATOM   1736 C CB  . LEU A 1 223 ? -44.870 33.385 -27.804 1.00 22.95  ? 224  LEU A CB  1 
ATOM   1737 C CG  . LEU A 1 223 ? -45.586 34.268 -26.780 1.00 24.96  ? 224  LEU A CG  1 
ATOM   1738 C CD1 . LEU A 1 223 ? -44.951 34.140 -25.391 1.00 25.41  ? 224  LEU A CD1 1 
ATOM   1739 C CD2 . LEU A 1 223 ? -45.576 35.717 -27.226 1.00 28.46  ? 224  LEU A CD2 1 
ATOM   1740 N N   . GLN A 1 224 ? -45.291 30.701 -29.989 1.00 25.30  ? 225  GLN A N   1 
ATOM   1741 C CA  . GLN A 1 224 ? -44.693 29.953 -31.132 1.00 25.12  ? 225  GLN A CA  1 
ATOM   1742 C C   . GLN A 1 224 ? -44.903 30.831 -32.400 1.00 24.48  ? 225  GLN A C   1 
ATOM   1743 O O   . GLN A 1 224 ? -46.038 31.036 -32.782 1.00 20.48  ? 225  GLN A O   1 
ATOM   1744 C CB  . GLN A 1 224 ? -45.468 28.646 -31.270 1.00 26.05  ? 225  GLN A CB  1 
ATOM   1745 C CG  . GLN A 1 224 ? -45.043 27.608 -30.213 1.00 29.63  ? 225  GLN A CG  1 
ATOM   1746 C CD  . GLN A 1 224 ? -45.983 26.407 -30.115 1.00 28.81  ? 225  GLN A CD  1 
ATOM   1747 O OE1 . GLN A 1 224 ? -46.414 26.026 -29.047 1.00 26.88  ? 225  GLN A OE1 1 
ATOM   1748 N NE2 . GLN A 1 224 ? -46.364 25.861 -31.252 1.00 31.44  ? 225  GLN A NE2 1 
ATOM   1749 N N   . SER A 1 225 ? -43.846 31.452 -32.949 1.00 23.05  ? 226  SER A N   1 
ATOM   1750 C CA  . SER A 1 225 ? -43.946 32.114 -34.247 1.00 24.30  ? 226  SER A CA  1 
ATOM   1751 C C   . SER A 1 225 ? -44.907 33.267 -34.179 1.00 24.70  ? 226  SER A C   1 
ATOM   1752 O O   . SER A 1 225 ? -45.745 33.450 -35.053 1.00 28.59  ? 226  SER A O   1 
ATOM   1753 C CB  . SER A 1 225 ? -44.426 31.094 -35.362 1.00 26.79  ? 226  SER A CB  1 
ATOM   1754 O OG  . SER A 1 225 ? -43.498 29.988 -35.566 1.00 22.25  ? 226  SER A OG  1 
ATOM   1755 N N   . GLY A 1 226 ? -44.854 34.033 -33.110 1.00 27.52  ? 227  GLY A N   1 
ATOM   1756 C CA  . GLY A 1 226 ? -45.844 35.113 -32.925 1.00 24.29  ? 227  GLY A CA  1 
ATOM   1757 C C   . GLY A 1 226 ? -45.469 35.946 -31.735 1.00 25.32  ? 227  GLY A C   1 
ATOM   1758 O O   . GLY A 1 226 ? -44.892 35.469 -30.790 1.00 27.90  ? 227  GLY A O   1 
ATOM   1759 N N   . SER A 1 227 ? -45.750 37.236 -31.857 1.00 29.12  ? 228  SER A N   1 
ATOM   1760 C CA  . SER A 1 227 ? -45.417 38.215 -30.844 1.00 26.64  ? 228  SER A CA  1 
ATOM   1761 C C   . SER A 1 227 ? -46.467 39.303 -30.934 1.00 27.92  ? 228  SER A C   1 
ATOM   1762 O O   . SER A 1 227 ? -47.044 39.536 -31.996 1.00 23.60  ? 228  SER A O   1 
ATOM   1763 C CB  . SER A 1 227 ? -44.026 38.797 -31.091 1.00 28.14  ? 228  SER A CB  1 
ATOM   1764 O OG  . SER A 1 227 ? -43.242 38.763 -29.912 1.00 36.48  ? 228  SER A OG  1 
ATOM   1765 N N   . PRO A 1 228 ? -46.722 39.962 -29.815 1.00 26.21  ? 229  PRO A N   1 
ATOM   1766 C CA  . PRO A 1 228 ? -47.802 40.935 -29.746 1.00 27.01  ? 229  PRO A CA  1 
ATOM   1767 C C   . PRO A 1 228 ? -47.539 42.132 -30.592 1.00 26.94  ? 229  PRO A C   1 
ATOM   1768 O O   . PRO A 1 228 ? -48.486 42.741 -31.128 1.00 25.03  ? 229  PRO A O   1 
ATOM   1769 C CB  . PRO A 1 228 ? -47.851 41.307 -28.248 1.00 27.32  ? 229  PRO A CB  1 
ATOM   1770 C CG  . PRO A 1 228 ? -46.502 40.915 -27.717 1.00 26.86  ? 229  PRO A CG  1 
ATOM   1771 C CD  . PRO A 1 228 ? -46.002 39.802 -28.542 1.00 25.91  ? 229  PRO A CD  1 
ATOM   1772 N N   . ASN A 1 229 ? -46.246 42.451 -30.734 1.00 27.50  ? 230  ASN A N   1 
ATOM   1773 C CA  . ASN A 1 229 ? -45.791 43.582 -31.565 1.00 30.39  ? 230  ASN A CA  1 
ATOM   1774 C C   . ASN A 1 229 ? -45.659 43.289 -33.080 1.00 30.06  ? 230  ASN A C   1 
ATOM   1775 O O   . ASN A 1 229 ? -45.255 44.134 -33.837 1.00 32.64  ? 230  ASN A O   1 
ATOM   1776 C CB  . ASN A 1 229 ? -44.437 44.080 -31.079 1.00 27.16  ? 230  ASN A CB  1 
ATOM   1777 C CG  . ASN A 1 229 ? -43.431 42.957 -30.976 1.00 29.79  ? 230  ASN A CG  1 
ATOM   1778 O OD1 . ASN A 1 229 ? -43.756 41.856 -30.471 1.00 32.63  ? 230  ASN A OD1 1 
ATOM   1779 N ND2 . ASN A 1 229 ? -42.230 43.184 -31.440 1.00 26.79  ? 230  ASN A ND2 1 
ATOM   1780 N N   . CYS A 1 230 ? -46.011 42.109 -33.543 1.00 32.45  ? 231  CYS A N   1 
ATOM   1781 C CA  . CYS A 1 230 ? -45.961 41.855 -34.997 1.00 28.37  ? 231  CYS A CA  1 
ATOM   1782 C C   . CYS A 1 230 ? -46.701 42.990 -35.794 1.00 31.30  ? 231  CYS A C   1 
ATOM   1783 O O   . CYS A 1 230 ? -47.789 43.499 -35.365 1.00 28.01  ? 231  CYS A O   1 
ATOM   1784 C CB  . CYS A 1 230 ? -46.586 40.499 -35.278 1.00 26.84  ? 231  CYS A CB  1 
ATOM   1785 S SG  . CYS A 1 230 ? -45.419 39.159 -34.830 1.00 26.26  ? 231  CYS A SG  1 
ATOM   1786 N N   . PRO A 1 231 ? -46.134 43.397 -36.948 1.00 27.36  ? 232  PRO A N   1 
ATOM   1787 C CA  . PRO A 1 231 ? -46.713 44.477 -37.783 1.00 24.20  ? 232  PRO A CA  1 
ATOM   1788 C C   . PRO A 1 231 ? -48.119 44.160 -38.280 1.00 25.16  ? 232  PRO A C   1 
ATOM   1789 O O   . PRO A 1 231 ? -48.900 45.023 -38.511 1.00 24.16  ? 232  PRO A O   1 
ATOM   1790 C CB  . PRO A 1 231 ? -45.697 44.606 -38.913 1.00 24.63  ? 232  PRO A CB  1 
ATOM   1791 C CG  . PRO A 1 231 ? -44.954 43.288 -38.956 1.00 26.93  ? 232  PRO A CG  1 
ATOM   1792 C CD  . PRO A 1 231 ? -44.922 42.810 -37.545 1.00 27.79  ? 232  PRO A CD  1 
ATOM   1793 N N   . TRP A 1 232 ? -48.475 42.876 -38.372 1.00 26.26  ? 233  TRP A N   1 
ATOM   1794 C CA  . TRP A 1 232 ? -49.795 42.462 -38.785 1.00 21.92  ? 233  TRP A CA  1 
ATOM   1795 C C   . TRP A 1 232 ? -50.818 42.237 -37.640 1.00 23.60  ? 233  TRP A C   1 
ATOM   1796 O O   . TRP A 1 232 ? -52.005 41.994 -37.917 1.00 22.87  ? 233  TRP A O   1 
ATOM   1797 C CB  . TRP A 1 232 ? -49.666 41.138 -39.540 1.00 21.58  ? 233  TRP A CB  1 
ATOM   1798 C CG  . TRP A 1 232 ? -48.858 40.078 -38.847 1.00 21.82  ? 233  TRP A CG  1 
ATOM   1799 C CD1 . TRP A 1 232 ? -47.524 39.834 -38.994 1.00 24.11  ? 233  TRP A CD1 1 
ATOM   1800 C CD2 . TRP A 1 232 ? -49.321 39.146 -37.869 1.00 23.35  ? 233  TRP A CD2 1 
ATOM   1801 N NE1 . TRP A 1 232 ? -47.130 38.815 -38.154 1.00 23.43  ? 233  TRP A NE1 1 
ATOM   1802 C CE2 . TRP A 1 232 ? -48.245 38.359 -37.492 1.00 23.99  ? 233  TRP A CE2 1 
ATOM   1803 C CE3 . TRP A 1 232 ? -50.576 38.863 -37.325 1.00 27.35  ? 233  TRP A CE3 1 
ATOM   1804 C CZ2 . TRP A 1 232 ? -48.379 37.307 -36.596 1.00 26.73  ? 233  TRP A CZ2 1 
ATOM   1805 C CZ3 . TRP A 1 232 ? -50.689 37.814 -36.424 1.00 25.78  ? 233  TRP A CZ3 1 
ATOM   1806 C CH2 . TRP A 1 232 ? -49.588 37.104 -36.035 1.00 25.87  ? 233  TRP A CH2 1 
ATOM   1807 N N   . ALA A 1 233 ? -50.377 42.204 -36.384 1.00 23.02  ? 234  ALA A N   1 
ATOM   1808 C CA  . ALA A 1 233 ? -51.268 41.748 -35.287 1.00 22.93  ? 234  ALA A CA  1 
ATOM   1809 C C   . ALA A 1 233 ? -52.140 42.828 -34.643 1.00 24.12  ? 234  ALA A C   1 
ATOM   1810 O O   . ALA A 1 233 ? -52.950 42.491 -33.832 1.00 25.31  ? 234  ALA A O   1 
ATOM   1811 C CB  . ALA A 1 233 ? -50.446 41.113 -34.212 1.00 22.78  ? 234  ALA A CB  1 
ATOM   1812 N N   . SER A 1 234 ? -51.975 44.103 -34.977 1.00 26.31  ? 235  SER A N   1 
ATOM   1813 C CA  . SER A 1 234 ? -52.799 45.194 -34.412 1.00 26.81  ? 235  SER A CA  1 
ATOM   1814 C C   . SER A 1 234 ? -52.858 46.367 -35.380 1.00 26.96  ? 235  SER A C   1 
ATOM   1815 O O   . SER A 1 234 ? -52.015 46.479 -36.237 1.00 25.68  ? 235  SER A O   1 
ATOM   1816 C CB  . SER A 1 234 ? -52.262 45.700 -33.081 1.00 26.76  ? 235  SER A CB  1 
ATOM   1817 O OG  . SER A 1 234 ? -50.954 46.246 -33.158 1.00 24.73  ? 235  SER A OG  1 
ATOM   1818 N N   . VAL A 1 235 ? -53.892 47.178 -35.251 1.00 25.51  ? 236  VAL A N   1 
ATOM   1819 C CA  . VAL A 1 235 ? -54.014 48.445 -35.963 1.00 27.20  ? 236  VAL A CA  1 
ATOM   1820 C C   . VAL A 1 235 ? -54.490 49.546 -34.971 1.00 29.24  ? 236  VAL A C   1 
ATOM   1821 O O   . VAL A 1 235 ? -55.087 49.269 -33.909 1.00 26.28  ? 236  VAL A O   1 
ATOM   1822 C CB  . VAL A 1 235 ? -55.130 48.335 -37.060 1.00 27.36  ? 236  VAL A CB  1 
ATOM   1823 C CG1 . VAL A 1 235 ? -54.725 47.286 -38.099 1.00 28.04  ? 236  VAL A CG1 1 
ATOM   1824 C CG2 . VAL A 1 235 ? -56.478 47.942 -36.443 1.00 25.68  ? 236  VAL A CG2 1 
ATOM   1825 N N   . SER A 1 236 ? -54.271 50.778 -35.354 1.00 27.44  ? 237  SER A N   1 
ATOM   1826 C CA  . SER A 1 236 ? -54.700 51.917 -34.575 1.00 29.23  ? 237  SER A CA  1 
ATOM   1827 C C   . SER A 1 236 ? -56.227 51.960 -34.568 1.00 28.39  ? 237  SER A C   1 
ATOM   1828 O O   . SER A 1 236 ? -56.855 51.315 -35.425 1.00 23.78  ? 237  SER A O   1 
ATOM   1829 C CB  . SER A 1 236 ? -54.154 53.213 -35.244 1.00 28.27  ? 237  SER A CB  1 
ATOM   1830 O OG  . SER A 1 236 ? -54.848 53.392 -36.490 1.00 31.53  ? 237  SER A OG  1 
ATOM   1831 N N   . VAL A 1 237 ? -56.826 52.762 -33.665 1.00 27.09  ? 238  VAL A N   1 
ATOM   1832 C CA  . VAL A 1 237 ? -58.292 52.881 -33.682 1.00 30.45  ? 238  VAL A CA  1 
ATOM   1833 C C   . VAL A 1 237 ? -58.772 53.540 -34.937 1.00 28.60  ? 238  VAL A C   1 
ATOM   1834 O O   . VAL A 1 237 ? -59.844 53.170 -35.451 1.00 26.14  ? 238  VAL A O   1 
ATOM   1835 C CB  . VAL A 1 237 ? -58.906 53.617 -32.460 1.00 35.57  ? 238  VAL A CB  1 
ATOM   1836 C CG1 . VAL A 1 237 ? -58.623 52.863 -31.163 1.00 40.31  ? 238  VAL A CG1 1 
ATOM   1837 C CG2 . VAL A 1 237 ? -58.335 54.987 -32.309 1.00 38.08  ? 238  VAL A CG2 1 
ATOM   1838 N N   . ALA A 1 238 ? -58.027 54.537 -35.412 1.00 27.86  ? 239  ALA A N   1 
ATOM   1839 C CA  . ALA A 1 238 ? -58.429 55.244 -36.652 1.00 30.82  ? 239  ALA A CA  1 
ATOM   1840 C C   . ALA A 1 238 ? -58.467 54.235 -37.831 1.00 30.65  ? 239  ALA A C   1 
ATOM   1841 O O   . ALA A 1 238 ? -59.445 54.161 -38.569 1.00 29.92  ? 239  ALA A O   1 
ATOM   1842 C CB  . ALA A 1 238 ? -57.441 56.385 -36.951 1.00 29.99  ? 239  ALA A CB  1 
ATOM   1843 N N   . GLU A 1 239 ? -57.436 53.378 -37.927 1.00 31.83  ? 240  GLU A N   1 
ATOM   1844 C CA  . GLU A 1 239 ? -57.402 52.383 -39.015 1.00 30.81  ? 240  GLU A CA  1 
ATOM   1845 C C   . GLU A 1 239 ? -58.511 51.345 -38.904 1.00 29.22  ? 240  GLU A C   1 
ATOM   1846 O O   . GLU A 1 239 ? -59.172 50.973 -39.918 1.00 27.46  ? 240  GLU A O   1 
ATOM   1847 C CB  . GLU A 1 239 ? -56.022 51.769 -39.129 1.00 30.06  ? 240  GLU A CB  1 
ATOM   1848 C CG  . GLU A 1 239 ? -55.922 50.688 -40.192 1.00 32.50  ? 240  GLU A CG  1 
ATOM   1849 C CD  . GLU A 1 239 ? -56.128 51.200 -41.620 1.00 33.62  ? 240  GLU A CD  1 
ATOM   1850 O OE1 . GLU A 1 239 ? -56.187 52.438 -41.857 1.00 31.39  ? 240  GLU A OE1 1 
ATOM   1851 O OE2 . GLU A 1 239 ? -56.286 50.322 -42.486 1.00 29.09  ? 240  GLU A OE2 1 
ATOM   1852 N N   . GLY A 1 240 ? -58.771 50.909 -37.667 1.00 31.31  ? 241  GLY A N   1 
ATOM   1853 C CA  . GLY A 1 240 ? -59.926 50.012 -37.355 1.00 29.30  ? 241  GLY A CA  1 
ATOM   1854 C C   . GLY A 1 240 ? -61.241 50.580 -37.832 1.00 27.64  ? 241  GLY A C   1 
ATOM   1855 O O   . GLY A 1 240 ? -62.065 49.925 -38.482 1.00 27.10  ? 241  GLY A O   1 
ATOM   1856 N N   . ARG A 1 241 ? -61.408 51.837 -37.530 1.00 29.40  ? 242  ARG A N   1 
ATOM   1857 C CA  . ARG A 1 241 ? -62.607 52.540 -37.892 1.00 34.18  ? 242  ARG A CA  1 
ATOM   1858 C C   . ARG A 1 241 ? -62.743 52.564 -39.411 1.00 30.57  ? 242  ARG A C   1 
ATOM   1859 O O   . ARG A 1 241 ? -63.778 52.177 -39.985 1.00 33.67  ? 242  ARG A O   1 
ATOM   1860 C CB  . ARG A 1 241 ? -62.531 53.976 -37.308 1.00 37.78  ? 242  ARG A CB  1 
ATOM   1861 C CG  . ARG A 1 241 ? -63.769 54.825 -37.580 1.00 42.20  ? 242  ARG A CG  1 
ATOM   1862 C CD  . ARG A 1 241 ? -63.960 56.068 -36.647 1.00 41.33  ? 242  ARG A CD  1 
ATOM   1863 N NE  . ARG A 1 241 ? -64.456 55.687 -35.322 1.00 36.99  ? 242  ARG A NE  1 
ATOM   1864 C CZ  . ARG A 1 241 ? -65.718 55.413 -35.048 1.00 40.10  ? 242  ARG A CZ  1 
ATOM   1865 N NH1 . ARG A 1 241 ? -66.663 55.502 -35.992 1.00 37.65  ? 242  ARG A NH1 1 
ATOM   1866 N NH2 . ARG A 1 241 ? -66.058 55.023 -33.824 1.00 43.22  ? 242  ARG A NH2 1 
ATOM   1867 N N   . ARG A 1 242 ? -61.683 52.995 -40.054 1.00 28.32  ? 243  ARG A N   1 
ATOM   1868 C CA  . ARG A 1 242 ? -61.672 53.099 -41.514 1.00 34.06  ? 243  ARG A CA  1 
ATOM   1869 C C   . ARG A 1 242 ? -62.096 51.792 -42.148 1.00 31.70  ? 243  ARG A C   1 
ATOM   1870 O O   . ARG A 1 242 ? -62.997 51.779 -43.009 1.00 32.32  ? 243  ARG A O   1 
ATOM   1871 C CB  . ARG A 1 242 ? -60.281 53.499 -41.969 1.00 38.00  ? 243  ARG A CB  1 
ATOM   1872 C CG  . ARG A 1 242 ? -60.091 54.210 -43.298 1.00 37.93  ? 243  ARG A CG  1 
ATOM   1873 C CD  . ARG A 1 242 ? -58.751 53.756 -43.975 1.00 41.35  ? 243  ARG A CD  1 
ATOM   1874 N NE  . ARG A 1 242 ? -59.177 52.773 -44.967 1.00 48.09  ? 243  ARG A NE  1 
ATOM   1875 C CZ  . ARG A 1 242 ? -58.766 51.546 -45.184 1.00 43.96  ? 243  ARG A CZ  1 
ATOM   1876 N NH1 . ARG A 1 242 ? -57.740 51.001 -44.584 1.00 45.12  ? 243  ARG A NH1 1 
ATOM   1877 N NH2 . ARG A 1 242 ? -59.381 50.896 -46.144 1.00 57.94  ? 243  ARG A NH2 1 
ATOM   1878 N N   . ARG A 1 243 ? -61.558 50.675 -41.642 1.00 29.81  ? 244  ARG A N   1 
ATOM   1879 C CA  . ARG A 1 243 ? -61.848 49.406 -42.269 1.00 27.69  ? 244  ARG A CA  1 
ATOM   1880 C C   . ARG A 1 243 ? -63.243 49.003 -42.013 1.00 29.13  ? 244  ARG A C   1 
ATOM   1881 O O   . ARG A 1 243 ? -63.828 48.278 -42.874 1.00 30.86  ? 244  ARG A O   1 
ATOM   1882 C CB  . ARG A 1 243 ? -60.892 48.238 -41.844 1.00 26.41  ? 244  ARG A CB  1 
ATOM   1883 C CG  . ARG A 1 243 ? -59.438 48.573 -42.086 1.00 24.29  ? 244  ARG A CG  1 
ATOM   1884 C CD  . ARG A 1 243 ? -58.516 47.472 -41.619 1.00 25.54  ? 244  ARG A CD  1 
ATOM   1885 N NE  . ARG A 1 243 ? -57.085 47.819 -41.824 1.00 24.43  ? 244  ARG A NE  1 
ATOM   1886 C CZ  . ARG A 1 243 ? -56.081 46.971 -41.641 1.00 23.98  ? 244  ARG A CZ  1 
ATOM   1887 N NH1 . ARG A 1 243 ? -56.290 45.690 -41.277 1.00 26.71  ? 244  ARG A NH1 1 
ATOM   1888 N NH2 . ARG A 1 243 ? -54.855 47.388 -41.804 1.00 25.18  ? 244  ARG A NH2 1 
ATOM   1889 N N   . ALA A 1 244 ? -63.787 49.374 -40.843 1.00 28.48  ? 245  ALA A N   1 
ATOM   1890 C CA  . ALA A 1 244 ? -65.198 49.011 -40.540 1.00 31.51  ? 245  ALA A CA  1 
ATOM   1891 C C   . ALA A 1 244 ? -66.163 49.773 -41.421 1.00 32.24  ? 245  ALA A C   1 
ATOM   1892 O O   . ALA A 1 244 ? -67.113 49.197 -41.885 1.00 32.04  ? 245  ALA A O   1 
ATOM   1893 C CB  . ALA A 1 244 ? -65.539 49.272 -39.086 1.00 38.01  ? 245  ALA A CB  1 
ATOM   1894 N N   . VAL A 1 245 ? -65.904 51.069 -41.637 1.00 33.70  ? 246  VAL A N   1 
ATOM   1895 C CA  . VAL A 1 245 ? -66.661 51.853 -42.601 1.00 35.69  ? 246  VAL A CA  1 
ATOM   1896 C C   . VAL A 1 245 ? -66.542 51.316 -44.056 1.00 35.32  ? 246  VAL A C   1 
ATOM   1897 O O   . VAL A 1 245 ? -67.538 51.182 -44.758 1.00 38.48  ? 246  VAL A O   1 
ATOM   1898 C CB  . VAL A 1 245 ? -66.220 53.318 -42.552 1.00 39.33  ? 246  VAL A CB  1 
ATOM   1899 C CG1 . VAL A 1 245 ? -66.943 54.149 -43.623 1.00 37.31  ? 246  VAL A CG1 1 
ATOM   1900 C CG2 . VAL A 1 245 ? -66.495 53.888 -41.152 1.00 37.25  ? 246  VAL A CG2 1 
ATOM   1901 N N   . GLU A 1 246 ? -65.336 50.966 -44.481 1.00 34.04  ? 247  GLU A N   1 
ATOM   1902 C CA  . GLU A 1 246 ? -65.145 50.384 -45.787 1.00 34.71  ? 247  GLU A CA  1 
ATOM   1903 C C   . GLU A 1 246 ? -65.911 49.083 -45.931 1.00 36.28  ? 247  GLU A C   1 
ATOM   1904 O O   . GLU A 1 246 ? -66.549 48.778 -47.015 1.00 33.82  ? 247  GLU A O   1 
ATOM   1905 C CB  . GLU A 1 246 ? -63.669 50.223 -46.064 1.00 35.74  ? 247  GLU A CB  1 
ATOM   1906 C CG  . GLU A 1 246 ? -63.324 49.835 -47.472 1.00 43.96  ? 247  GLU A CG  1 
ATOM   1907 C CD  . GLU A 1 246 ? -63.751 50.878 -48.544 1.00 46.82  ? 247  GLU A CD  1 
ATOM   1908 O OE1 . GLU A 1 246 ? -63.959 52.074 -48.252 1.00 42.87  ? 247  GLU A OE1 1 
ATOM   1909 O OE2 . GLU A 1 246 ? -63.913 50.447 -49.692 1.00 43.76  ? 247  GLU A OE2 1 
ATOM   1910 N N   . LEU A 1 247 ? -65.943 48.316 -44.844 1.00 32.87  ? 248  LEU A N   1 
ATOM   1911 C CA  . LEU A 1 247 ? -66.670 47.064 -44.886 1.00 28.49  ? 248  LEU A CA  1 
ATOM   1912 C C   . LEU A 1 247 ? -68.093 47.381 -45.108 1.00 31.73  ? 248  LEU A C   1 
ATOM   1913 O O   . LEU A 1 247 ? -68.757 46.722 -45.884 1.00 34.35  ? 248  LEU A O   1 
ATOM   1914 C CB  . LEU A 1 247 ? -66.537 46.287 -43.574 1.00 30.15  ? 248  LEU A CB  1 
ATOM   1915 C CG  . LEU A 1 247 ? -67.224 44.907 -43.578 1.00 31.48  ? 248  LEU A CG  1 
ATOM   1916 C CD1 . LEU A 1 247 ? -66.456 43.923 -44.463 1.00 34.51  ? 248  LEU A CD1 1 
ATOM   1917 C CD2 . LEU A 1 247 ? -67.422 44.300 -42.183 1.00 32.44  ? 248  LEU A CD2 1 
ATOM   1918 N N   . GLY A 1 248 ? -68.618 48.362 -44.390 1.00 32.75  ? 249  GLY A N   1 
ATOM   1919 C CA  . GLY A 1 248 ? -70.049 48.726 -44.597 1.00 36.73  ? 249  GLY A CA  1 
ATOM   1920 C C   . GLY A 1 248 ? -70.342 49.270 -46.004 1.00 33.40  ? 249  GLY A C   1 
ATOM   1921 O O   . GLY A 1 248 ? -71.382 49.003 -46.598 1.00 30.84  ? 249  GLY A O   1 
ATOM   1922 N N   . ARG A 1 249 ? -69.392 50.005 -46.535 1.00 32.88  ? 250  ARG A N   1 
ATOM   1923 C CA  . ARG A 1 249 ? -69.481 50.451 -47.875 1.00 35.85  ? 250  ARG A CA  1 
ATOM   1924 C C   . ARG A 1 249 ? -69.565 49.298 -48.892 1.00 38.71  ? 250  ARG A C   1 
ATOM   1925 O O   . ARG A 1 249 ? -70.280 49.386 -49.850 1.00 37.88  ? 250  ARG A O   1 
ATOM   1926 C CB  . ARG A 1 249 ? -68.315 51.349 -48.142 1.00 41.10  ? 250  ARG A CB  1 
ATOM   1927 C CG  . ARG A 1 249 ? -68.472 52.164 -49.426 1.00 48.22  ? 250  ARG A CG  1 
ATOM   1928 C CD  . ARG A 1 249 ? -67.213 52.984 -49.709 1.00 46.14  ? 250  ARG A CD  1 
ATOM   1929 N NE  . ARG A 1 249 ? -66.777 53.732 -48.519 1.00 55.91  ? 250  ARG A NE  1 
ATOM   1930 C CZ  . ARG A 1 249 ? -67.115 54.998 -48.229 1.00 62.58  ? 250  ARG A CZ  1 
ATOM   1931 N NH1 . ARG A 1 249 ? -67.924 55.686 -49.041 1.00 71.22  ? 250  ARG A NH1 1 
ATOM   1932 N NH2 . ARG A 1 249 ? -66.636 55.600 -47.123 1.00 57.63  ? 250  ARG A NH2 1 
ATOM   1933 N N   . ASN A 1 250 ? -68.871 48.191 -48.659 1.00 40.56  ? 251  ASN A N   1 
ATOM   1934 C CA  . ASN A 1 250 ? -68.936 47.055 -49.553 1.00 34.87  ? 251  ASN A CA  1 
ATOM   1935 C C   . ASN A 1 250 ? -70.233 46.329 -49.463 1.00 34.33  ? 251  ASN A C   1 
ATOM   1936 O O   . ASN A 1 250 ? -70.532 45.486 -50.339 1.00 38.62  ? 251  ASN A O   1 
ATOM   1937 C CB  . ASN A 1 250 ? -67.844 46.020 -49.228 1.00 37.73  ? 251  ASN A CB  1 
ATOM   1938 C CG  . ASN A 1 250 ? -66.479 46.377 -49.806 1.00 33.77  ? 251  ASN A CG  1 
ATOM   1939 O OD1 . ASN A 1 250 ? -66.056 45.764 -50.751 1.00 35.00  ? 251  ASN A OD1 1 
ATOM   1940 N ND2 . ASN A 1 250 ? -65.790 47.305 -49.213 1.00 35.03  ? 251  ASN A ND2 1 
ATOM   1941 N N   . LEU A 1 251 ? -70.999 46.578 -48.399 1.00 37.45  ? 252  LEU A N   1 
ATOM   1942 C CA  . LEU A 1 251 ? -72.320 45.934 -48.229 1.00 37.01  ? 252  LEU A CA  1 
ATOM   1943 C C   . LEU A 1 251 ? -73.502 46.918 -48.369 1.00 40.44  ? 252  LEU A C   1 
ATOM   1944 O O   . LEU A 1 251 ? -74.610 46.606 -47.966 1.00 41.23  ? 252  LEU A O   1 
ATOM   1945 C CB  . LEU A 1 251 ? -72.374 45.193 -46.904 1.00 36.67  ? 252  LEU A CB  1 
ATOM   1946 C CG  . LEU A 1 251 ? -71.345 44.079 -46.871 1.00 36.85  ? 252  LEU A CG  1 
ATOM   1947 C CD1 . LEU A 1 251 ? -70.903 43.653 -45.488 1.00 36.70  ? 252  LEU A CD1 1 
ATOM   1948 C CD2 . LEU A 1 251 ? -71.833 42.867 -47.629 1.00 37.20  ? 252  LEU A CD2 1 
ATOM   1949 N N   . ASN A 1 252 ? -73.262 48.081 -48.980 1.00 46.37  ? 253  ASN A N   1 
ATOM   1950 C CA  . ASN A 1 252 ? -74.328 49.082 -49.247 1.00 55.36  ? 253  ASN A CA  1 
ATOM   1951 C C   . ASN A 1 252 ? -75.038 49.497 -47.940 1.00 52.78  ? 253  ASN A C   1 
ATOM   1952 O O   . ASN A 1 252 ? -76.252 49.559 -47.913 1.00 47.01  ? 253  ASN A O   1 
ATOM   1953 C CB  . ASN A 1 252 ? -75.394 48.572 -50.258 1.00 56.72  ? 253  ASN A CB  1 
ATOM   1954 C CG  . ASN A 1 252 ? -74.811 47.679 -51.377 1.00 67.65  ? 253  ASN A CG  1 
ATOM   1955 O OD1 . ASN A 1 252 ? -75.145 46.472 -51.472 1.00 62.43  ? 253  ASN A OD1 1 
ATOM   1956 N ND2 . ASN A 1 252 ? -73.937 48.253 -52.216 1.00 64.52  ? 253  ASN A ND2 1 
ATOM   1957 N N   . CYS A 1 253 ? -74.263 49.708 -46.875 1.00 45.75  ? 254  CYS A N   1 
ATOM   1958 C CA  . CYS A 1 253 ? -74.779 50.162 -45.594 1.00 42.00  ? 254  CYS A CA  1 
ATOM   1959 C C   . CYS A 1 253 ? -74.950 51.650 -45.526 1.00 41.39  ? 254  CYS A C   1 
ATOM   1960 O O   . CYS A 1 253 ? -74.188 52.441 -46.113 1.00 37.63  ? 254  CYS A O   1 
ATOM   1961 C CB  . CYS A 1 253 ? -73.850 49.801 -44.423 1.00 41.37  ? 254  CYS A CB  1 
ATOM   1962 S SG  . CYS A 1 253 ? -73.773 48.040 -44.031 1.00 42.52  ? 254  CYS A SG  1 
ATOM   1963 N N   . ASN A 1 254 ? -75.935 52.036 -44.715 1.00 47.34  ? 255  ASN A N   1 
ATOM   1964 C CA  . ASN A 1 254 ? -75.980 53.388 -44.194 1.00 45.73  ? 255  ASN A CA  1 
ATOM   1965 C C   . ASN A 1 254 ? -74.745 53.699 -43.376 1.00 39.27  ? 255  ASN A C   1 
ATOM   1966 O O   . ASN A 1 254 ? -74.465 52.996 -42.409 1.00 43.97  ? 255  ASN A O   1 
ATOM   1967 C CB  . ASN A 1 254 ? -77.216 53.553 -43.324 1.00 51.12  ? 255  ASN A CB  1 
ATOM   1968 C CG  . ASN A 1 254 ? -77.545 55.019 -43.066 1.00 51.69  ? 255  ASN A CG  1 
ATOM   1969 O OD1 . ASN A 1 254 ? -76.723 55.817 -42.600 1.00 46.09  ? 255  ASN A OD1 1 
ATOM   1970 N ND2 . ASN A 1 254 ? -78.747 55.381 -43.429 1.00 59.26  ? 255  ASN A ND2 1 
ATOM   1971 N N   . LEU A 1 255 ? -74.039 54.767 -43.730 1.00 41.50  ? 256  LEU A N   1 
ATOM   1972 C CA  . LEU A 1 255 ? -72.784 55.164 -43.065 1.00 41.30  ? 256  LEU A CA  1 
ATOM   1973 C C   . LEU A 1 255 ? -72.858 56.454 -42.251 1.00 47.62  ? 256  LEU A C   1 
ATOM   1974 O O   . LEU A 1 255 ? -71.803 56.986 -41.843 1.00 41.59  ? 256  LEU A O   1 
ATOM   1975 C CB  . LEU A 1 255 ? -71.668 55.351 -44.101 1.00 39.15  ? 256  LEU A CB  1 
ATOM   1976 C CG  . LEU A 1 255 ? -71.490 54.164 -45.060 1.00 43.58  ? 256  LEU A CG  1 
ATOM   1977 C CD1 . LEU A 1 255 ? -70.301 54.485 -45.951 1.00 45.27  ? 256  LEU A CD1 1 
ATOM   1978 C CD2 . LEU A 1 255 ? -71.268 52.842 -44.329 1.00 41.44  ? 256  LEU A CD2 1 
ATOM   1979 N N   . ASN A 1 256 ? -74.071 56.937 -41.960 1.00 50.82  ? 257  ASN A N   1 
ATOM   1980 C CA  . ASN A 1 256 ? -74.207 58.211 -41.207 1.00 55.24  ? 257  ASN A CA  1 
ATOM   1981 C C   . ASN A 1 256 ? -73.757 58.168 -39.774 1.00 51.68  ? 257  ASN A C   1 
ATOM   1982 O O   . ASN A 1 256 ? -73.421 59.199 -39.215 1.00 54.87  ? 257  ASN A O   1 
ATOM   1983 C CB  . ASN A 1 256 ? -75.661 58.690 -41.171 1.00 64.54  ? 257  ASN A CB  1 
ATOM   1984 C CG  . ASN A 1 256 ? -76.102 59.323 -42.474 1.00 70.52  ? 257  ASN A CG  1 
ATOM   1985 O OD1 . ASN A 1 256 ? -75.272 59.776 -43.280 1.00 77.19  ? 257  ASN A OD1 1 
ATOM   1986 N ND2 . ASN A 1 256 ? -77.418 59.349 -42.697 1.00 76.80  ? 257  ASN A ND2 1 
ATOM   1987 N N   . SER A 1 257 ? -73.819 56.994 -39.158 1.00 45.67  ? 258  SER A N   1 
ATOM   1988 C CA  . SER A 1 257 ? -73.495 56.869 -37.755 1.00 42.07  ? 258  SER A CA  1 
ATOM   1989 C C   . SER A 1 257 ? -73.007 55.456 -37.509 1.00 39.86  ? 258  SER A C   1 
ATOM   1990 O O   . SER A 1 257 ? -73.304 54.528 -38.257 1.00 43.11  ? 258  SER A O   1 
ATOM   1991 C CB  . SER A 1 257 ? -74.750 57.163 -36.877 1.00 35.32  ? 258  SER A CB  1 
ATOM   1992 O OG  . SER A 1 257 ? -75.831 56.252 -37.196 1.00 36.84  ? 258  SER A OG  1 
ATOM   1993 N N   . ASP A 1 258 ? -72.312 55.303 -36.404 1.00 40.68  ? 259  ASP A N   1 
ATOM   1994 C CA  . ASP A 1 258 ? -71.913 54.007 -35.904 1.00 39.66  ? 259  ASP A CA  1 
ATOM   1995 C C   . ASP A 1 258 ? -73.089 53.108 -35.734 1.00 41.88  ? 259  ASP A C   1 
ATOM   1996 O O   . ASP A 1 258 ? -73.003 51.930 -36.056 1.00 41.61  ? 259  ASP A O   1 
ATOM   1997 C CB  . ASP A 1 258 ? -71.192 54.156 -34.551 1.00 38.32  ? 259  ASP A CB  1 
ATOM   1998 C CG  . ASP A 1 258 ? -69.769 54.698 -34.683 1.00 41.50  ? 259  ASP A CG  1 
ATOM   1999 O OD1 . ASP A 1 258 ? -69.329 54.997 -35.809 1.00 46.70  ? 259  ASP A OD1 1 
ATOM   2000 O OD2 . ASP A 1 258 ? -69.047 54.831 -33.658 1.00 48.49  ? 259  ASP A OD2 1 
ATOM   2001 N N   . GLU A 1 259 ? -74.190 53.665 -35.220 1.00 47.85  ? 260  GLU A N   1 
ATOM   2002 C CA  . GLU A 1 259 ? -75.400 52.885 -34.907 1.00 48.46  ? 260  GLU A CA  1 
ATOM   2003 C C   . GLU A 1 259 ? -75.958 52.374 -36.183 1.00 44.68  ? 260  GLU A C   1 
ATOM   2004 O O   . GLU A 1 259 ? -76.373 51.205 -36.259 1.00 48.70  ? 260  GLU A O   1 
ATOM   2005 C CB  . GLU A 1 259 ? -76.496 53.728 -34.222 1.00 60.08  ? 260  GLU A CB  1 
ATOM   2006 C CG  . GLU A 1 259 ? -76.144 54.361 -32.868 1.00 72.38  ? 260  GLU A CG  1 
ATOM   2007 C CD  . GLU A 1 259 ? -74.848 55.209 -32.863 1.00 85.27  ? 260  GLU A CD  1 
ATOM   2008 O OE1 . GLU A 1 259 ? -74.567 55.972 -33.830 1.00 74.41  ? 260  GLU A OE1 1 
ATOM   2009 O OE2 . GLU A 1 259 ? -74.080 55.106 -31.869 1.00 96.62  ? 260  GLU A OE2 1 
ATOM   2010 N N   . GLU A 1 260 ? -76.019 53.270 -37.175 1.00 46.58  ? 261  GLU A N   1 
ATOM   2011 C CA  . GLU A 1 260 ? -76.487 52.918 -38.530 1.00 49.85  ? 261  GLU A CA  1 
ATOM   2012 C C   . GLU A 1 260 ? -75.608 51.775 -39.165 1.00 44.73  ? 261  GLU A C   1 
ATOM   2013 O O   . GLU A 1 260 ? -76.134 50.752 -39.643 1.00 36.07  ? 261  GLU A O   1 
ATOM   2014 C CB  . GLU A 1 260 ? -76.479 54.169 -39.443 1.00 59.37  ? 261  GLU A CB  1 
ATOM   2015 C CG  . GLU A 1 260 ? -77.433 55.332 -39.072 1.00 68.35  ? 261  GLU A CG  1 
ATOM   2016 C CD  . GLU A 1 260 ? -78.825 55.193 -39.699 1.00 74.05  ? 261  GLU A CD  1 
ATOM   2017 O OE1 . GLU A 1 260 ? -79.209 54.078 -40.144 1.00 68.74  ? 261  GLU A OE1 1 
ATOM   2018 O OE2 . GLU A 1 260 ? -79.544 56.212 -39.747 1.00 73.63  ? 261  GLU A OE2 1 
ATOM   2019 N N   . LEU A 1 261 ? -74.283 51.926 -39.111 1.00 37.53  ? 262  LEU A N   1 
ATOM   2020 C CA  . LEU A 1 261 ? -73.374 50.934 -39.695 1.00 37.93  ? 262  LEU A CA  1 
ATOM   2021 C C   . LEU A 1 261 ? -73.540 49.576 -39.016 1.00 39.18  ? 262  LEU A C   1 
ATOM   2022 O O   . LEU A 1 261 ? -73.811 48.503 -39.669 1.00 34.78  ? 262  LEU A O   1 
ATOM   2023 C CB  . LEU A 1 261 ? -71.958 51.462 -39.593 1.00 38.42  ? 262  LEU A CB  1 
ATOM   2024 C CG  . LEU A 1 261 ? -70.800 50.569 -39.986 1.00 37.43  ? 262  LEU A CG  1 
ATOM   2025 C CD1 . LEU A 1 261 ? -70.935 50.060 -41.380 1.00 36.92  ? 262  LEU A CD1 1 
ATOM   2026 C CD2 . LEU A 1 261 ? -69.530 51.394 -39.857 1.00 39.25  ? 262  LEU A CD2 1 
ATOM   2027 N N   . ILE A 1 262 ? -73.505 49.643 -37.694 1.00 34.26  ? 263  ILE A N   1 
ATOM   2028 C CA  . ILE A 1 262 ? -73.536 48.431 -36.920 1.00 37.70  ? 263  ILE A CA  1 
ATOM   2029 C C   . ILE A 1 262 ? -74.856 47.735 -37.149 1.00 33.66  ? 263  ILE A C   1 
ATOM   2030 O O   . ILE A 1 262 ? -74.887 46.547 -37.383 1.00 39.66  ? 263  ILE A O   1 
ATOM   2031 C CB  . ILE A 1 262 ? -73.262 48.659 -35.406 1.00 35.85  ? 263  ILE A CB  1 
ATOM   2032 C CG1 . ILE A 1 262 ? -71.844 49.139 -35.188 1.00 39.93  ? 263  ILE A CG1 1 
ATOM   2033 C CG2 . ILE A 1 262 ? -73.482 47.361 -34.707 1.00 39.71  ? 263  ILE A CG2 1 
ATOM   2034 C CD1 . ILE A 1 262 ? -71.540 49.771 -33.848 1.00 40.81  ? 263  ILE A CD1 1 
ATOM   2035 N N   . HIS A 1 263 ? -75.952 48.453 -37.103 1.00 39.47  ? 264  HIS A N   1 
ATOM   2036 C CA  . HIS A 1 263 ? -77.244 47.802 -37.348 1.00 44.85  ? 264  HIS A CA  1 
ATOM   2037 C C   . HIS A 1 263 ? -77.225 47.124 -38.719 1.00 40.64  ? 264  HIS A C   1 
ATOM   2038 O O   . HIS A 1 263 ? -77.698 45.988 -38.861 1.00 43.17  ? 264  HIS A O   1 
ATOM   2039 C CB  . HIS A 1 263 ? -78.421 48.802 -37.250 1.00 51.16  ? 264  HIS A CB  1 
ATOM   2040 C CG  . HIS A 1 263 ? -79.754 48.196 -37.602 1.00 62.97  ? 264  HIS A CG  1 
ATOM   2041 N ND1 . HIS A 1 263 ? -80.263 48.193 -38.893 1.00 67.49  ? 264  HIS A ND1 1 
ATOM   2042 C CD2 . HIS A 1 263 ? -80.664 47.540 -36.840 1.00 66.03  ? 264  HIS A CD2 1 
ATOM   2043 C CE1 . HIS A 1 263 ? -81.425 47.563 -38.909 1.00 65.89  ? 264  HIS A CE1 1 
ATOM   2044 N NE2 . HIS A 1 263 ? -81.691 47.159 -37.677 1.00 69.71  ? 264  HIS A NE2 1 
ATOM   2045 N N   . CYS A 1 264 ? -76.689 47.822 -39.735 1.00 42.86  ? 265  CYS A N   1 
ATOM   2046 C CA  . CYS A 1 264 ? -76.659 47.264 -41.101 1.00 39.91  ? 265  CYS A CA  1 
ATOM   2047 C C   . CYS A 1 264 ? -75.800 45.996 -41.091 1.00 35.42  ? 265  CYS A C   1 
ATOM   2048 O O   . CYS A 1 264 ? -76.241 44.954 -41.591 1.00 30.38  ? 265  CYS A O   1 
ATOM   2049 C CB  . CYS A 1 264 ? -76.169 48.275 -42.170 1.00 42.90  ? 265  CYS A CB  1 
ATOM   2050 S SG  . CYS A 1 264 ? -75.671 47.425 -43.716 1.00 58.72  ? 265  CYS A SG  1 
ATOM   2051 N N   . LEU A 1 265 ? -74.608 46.051 -40.447 1.00 34.27  ? 266  LEU A N   1 
ATOM   2052 C CA  . LEU A 1 265 ? -73.737 44.838 -40.408 1.00 33.31  ? 266  LEU A CA  1 
ATOM   2053 C C   . LEU A 1 265 ? -74.382 43.701 -39.688 1.00 36.37  ? 266  LEU A C   1 
ATOM   2054 O O   . LEU A 1 265 ? -74.116 42.522 -39.983 1.00 37.74  ? 266  LEU A O   1 
ATOM   2055 C CB  . LEU A 1 265 ? -72.332 45.135 -39.868 1.00 31.81  ? 266  LEU A CB  1 
ATOM   2056 C CG  . LEU A 1 265 ? -71.570 46.182 -40.697 1.00 27.93  ? 266  LEU A CG  1 
ATOM   2057 C CD1 . LEU A 1 265 ? -70.368 46.647 -39.939 1.00 30.67  ? 266  LEU A CD1 1 
ATOM   2058 C CD2 . LEU A 1 265 ? -71.209 45.637 -42.069 1.00 30.96  ? 266  LEU A CD2 1 
ATOM   2059 N N   . ARG A 1 266 ? -75.254 44.018 -38.747 1.00 41.47  ? 267  ARG A N   1 
ATOM   2060 C CA  . ARG A 1 266 ? -75.820 42.956 -37.905 1.00 42.62  ? 267  ARG A CA  1 
ATOM   2061 C C   . ARG A 1 266 ? -76.909 42.249 -38.633 1.00 43.92  ? 267  ARG A C   1 
ATOM   2062 O O   . ARG A 1 266 ? -77.173 41.119 -38.291 1.00 43.78  ? 267  ARG A O   1 
ATOM   2063 C CB  . ARG A 1 266 ? -76.355 43.509 -36.605 1.00 45.39  ? 267  ARG A CB  1 
ATOM   2064 C CG  . ARG A 1 266 ? -75.272 43.872 -35.620 1.00 48.22  ? 267  ARG A CG  1 
ATOM   2065 C CD  . ARG A 1 266 ? -75.832 44.105 -34.251 1.00 45.88  ? 267  ARG A CD  1 
ATOM   2066 N NE  . ARG A 1 266 ? -74.746 44.221 -33.308 1.00 52.08  ? 267  ARG A NE  1 
ATOM   2067 C CZ  . ARG A 1 266 ? -74.784 44.970 -32.218 1.00 49.97  ? 267  ARG A CZ  1 
ATOM   2068 N NH1 . ARG A 1 266 ? -75.865 45.669 -31.955 1.00 54.07  ? 267  ARG A NH1 1 
ATOM   2069 N NH2 . ARG A 1 266 ? -73.739 45.025 -31.400 1.00 49.50  ? 267  ARG A NH2 1 
ATOM   2070 N N   . GLU A 1 267 ? -77.539 42.909 -39.615 1.00 44.66  ? 268  GLU A N   1 
ATOM   2071 C CA  . GLU A 1 267 ? -78.555 42.252 -40.491 1.00 47.62  ? 268  GLU A CA  1 
ATOM   2072 C C   . GLU A 1 267 ? -77.961 41.245 -41.498 1.00 44.90  ? 268  GLU A C   1 
ATOM   2073 O O   . GLU A 1 267 ? -78.671 40.405 -42.032 1.00 41.88  ? 268  GLU A O   1 
ATOM   2074 C CB  . GLU A 1 267 ? -79.388 43.319 -41.283 1.00 54.69  ? 268  GLU A CB  1 
ATOM   2075 C CG  . GLU A 1 267 ? -80.575 43.980 -40.523 1.00 65.32  ? 268  GLU A CG  1 
ATOM   2076 C CD  . GLU A 1 267 ? -81.275 43.022 -39.517 1.00 75.12  ? 268  GLU A CD  1 
ATOM   2077 O OE1 . GLU A 1 267 ? -81.956 42.048 -39.942 1.00 79.87  ? 268  GLU A OE1 1 
ATOM   2078 O OE2 . GLU A 1 267 ? -81.125 43.214 -38.281 1.00 74.40  ? 268  GLU A OE2 1 
ATOM   2079 N N   . LYS A 1 268 ? -76.664 41.354 -41.788 1.00 42.01  ? 269  LYS A N   1 
ATOM   2080 C CA  . LYS A 1 268 ? -76.073 40.597 -42.879 1.00 39.09  ? 269  LYS A CA  1 
ATOM   2081 C C   . LYS A 1 268 ? -75.803 39.175 -42.446 1.00 38.86  ? 269  LYS A C   1 
ATOM   2082 O O   . LYS A 1 268 ? -75.516 38.901 -41.291 1.00 40.37  ? 269  LYS A O   1 
ATOM   2083 C CB  . LYS A 1 268 ? -74.763 41.234 -43.284 1.00 40.74  ? 269  LYS A CB  1 
ATOM   2084 C CG  . LYS A 1 268 ? -74.887 42.648 -43.777 1.00 43.89  ? 269  LYS A CG  1 
ATOM   2085 C CD  . LYS A 1 268 ? -75.776 42.741 -45.025 1.00 44.89  ? 269  LYS A CD  1 
ATOM   2086 C CE  . LYS A 1 268 ? -76.112 44.198 -45.269 1.00 48.92  ? 269  LYS A CE  1 
ATOM   2087 N NZ  . LYS A 1 268 ? -76.712 44.438 -46.608 1.00 59.08  ? 269  LYS A NZ  1 
ATOM   2088 N N   . LYS A 1 269 ? -75.922 38.242 -43.364 1.00 39.93  ? 270  LYS A N   1 
ATOM   2089 C CA  . LYS A 1 269 ? -75.595 36.870 -43.023 1.00 41.68  ? 270  LYS A CA  1 
ATOM   2090 C C   . LYS A 1 269 ? -74.072 36.799 -42.850 1.00 39.22  ? 270  LYS A C   1 
ATOM   2091 O O   . LYS A 1 269 ? -73.321 37.617 -43.420 1.00 35.57  ? 270  LYS A O   1 
ATOM   2092 C CB  . LYS A 1 269 ? -76.090 35.891 -44.096 1.00 49.46  ? 270  LYS A CB  1 
ATOM   2093 C CG  . LYS A 1 269 ? -77.592 35.650 -44.032 1.00 58.81  ? 270  LYS A CG  1 
ATOM   2094 C CD  . LYS A 1 269 ? -78.242 35.448 -45.399 1.00 69.71  ? 270  LYS A CD  1 
ATOM   2095 C CE  . LYS A 1 269 ? -79.755 35.752 -45.318 1.00 83.72  ? 270  LYS A CE  1 
ATOM   2096 N NZ  . LYS A 1 269 ? -80.497 35.600 -46.615 1.00 85.60  ? 270  LYS A NZ  1 
ATOM   2097 N N   . PRO A 1 270 ? -73.604 35.816 -42.089 1.00 35.27  ? 271  PRO A N   1 
ATOM   2098 C CA  . PRO A 1 270 ? -72.156 35.725 -41.876 1.00 34.14  ? 271  PRO A CA  1 
ATOM   2099 C C   . PRO A 1 270 ? -71.376 35.741 -43.191 1.00 33.17  ? 271  PRO A C   1 
ATOM   2100 O O   . PRO A 1 270 ? -70.436 36.516 -43.359 1.00 31.80  ? 271  PRO A O   1 
ATOM   2101 C CB  . PRO A 1 270 ? -71.997 34.387 -41.132 1.00 36.72  ? 271  PRO A CB  1 
ATOM   2102 C CG  . PRO A 1 270 ? -73.346 34.186 -40.427 1.00 37.24  ? 271  PRO A CG  1 
ATOM   2103 C CD  . PRO A 1 270 ? -74.389 34.901 -41.233 1.00 32.57  ? 271  PRO A CD  1 
ATOM   2104 N N   . GLN A 1 271 ? -71.821 34.962 -44.158 1.00 38.30  ? 272  GLN A N   1 
ATOM   2105 C CA  . GLN A 1 271 ? -71.028 34.770 -45.364 1.00 42.24  ? 272  GLN A CA  1 
ATOM   2106 C C   . GLN A 1 271 ? -70.909 36.034 -46.219 1.00 39.09  ? 272  GLN A C   1 
ATOM   2107 O O   . GLN A 1 271 ? -69.934 36.206 -46.943 1.00 37.06  ? 272  GLN A O   1 
ATOM   2108 C CB  . GLN A 1 271 ? -71.534 33.581 -46.175 1.00 43.86  ? 272  GLN A CB  1 
ATOM   2109 C CG  . GLN A 1 271 ? -70.570 33.079 -47.267 1.00 42.86  ? 272  GLN A CG  1 
ATOM   2110 C CD  . GLN A 1 271 ? -69.179 32.756 -46.770 1.00 46.07  ? 272  GLN A CD  1 
ATOM   2111 O OE1 . GLN A 1 271 ? -69.022 32.073 -45.758 1.00 44.38  ? 272  GLN A OE1 1 
ATOM   2112 N NE2 . GLN A 1 271 ? -68.141 33.248 -47.497 1.00 44.88  ? 272  GLN A NE2 1 
ATOM   2113 N N   . GLU A 1 272 ? -71.837 36.956 -46.044 1.00 37.17  ? 273  GLU A N   1 
ATOM   2114 C CA  . GLU A 1 272 ? -71.797 38.252 -46.740 1.00 35.32  ? 273  GLU A CA  1 
ATOM   2115 C C   . GLU A 1 272 ? -70.671 39.071 -46.223 1.00 35.38  ? 273  GLU A C   1 
ATOM   2116 O O   . GLU A 1 272 ? -70.072 39.809 -46.979 1.00 41.78  ? 273  GLU A O   1 
ATOM   2117 C CB  . GLU A 1 272 ? -73.118 39.031 -46.530 1.00 35.65  ? 273  GLU A CB  1 
ATOM   2118 C CG  . GLU A 1 272 ? -74.336 38.203 -46.955 1.00 43.10  ? 273  GLU A CG  1 
ATOM   2119 C CD  . GLU A 1 272 ? -75.668 38.959 -46.861 1.00 44.64  ? 273  GLU A CD  1 
ATOM   2120 O OE1 . GLU A 1 272 ? -75.843 40.001 -47.492 1.00 41.00  ? 273  GLU A OE1 1 
ATOM   2121 O OE2 . GLU A 1 272 ? -76.550 38.469 -46.181 1.00 46.09  ? 273  GLU A OE2 1 
ATOM   2122 N N   . LEU A 1 273 ? -70.366 38.940 -44.926 1.00 32.32  ? 274  LEU A N   1 
ATOM   2123 C CA  . LEU A 1 273 ? -69.264 39.698 -44.360 1.00 32.93  ? 274  LEU A CA  1 
ATOM   2124 C C   . LEU A 1 273 ? -67.971 39.055 -44.808 1.00 28.97  ? 274  LEU A C   1 
ATOM   2125 O O   . LEU A 1 273 ? -67.055 39.731 -45.197 1.00 26.69  ? 274  LEU A O   1 
ATOM   2126 C CB  . LEU A 1 273 ? -69.331 39.785 -42.821 1.00 36.65  ? 274  LEU A CB  1 
ATOM   2127 C CG  . LEU A 1 273 ? -70.131 40.874 -42.067 1.00 37.45  ? 274  LEU A CG  1 
ATOM   2128 C CD1 . LEU A 1 273 ? -71.524 41.015 -42.535 1.00 38.54  ? 274  LEU A CD1 1 
ATOM   2129 C CD2 . LEU A 1 273 ? -70.203 40.572 -40.581 1.00 41.84  ? 274  LEU A CD2 1 
ATOM   2130 N N   . ILE A 1 274 ? -67.911 37.740 -44.744 1.00 29.59  ? 275  ILE A N   1 
ATOM   2131 C CA  . ILE A 1 274 ? -66.688 37.004 -45.102 1.00 32.17  ? 275  ILE A CA  1 
ATOM   2132 C C   . ILE A 1 274 ? -66.287 37.242 -46.586 1.00 34.00  ? 275  ILE A C   1 
ATOM   2133 O O   . ILE A 1 274 ? -65.136 37.515 -46.872 1.00 32.70  ? 275  ILE A O   1 
ATOM   2134 C CB  . ILE A 1 274 ? -66.847 35.519 -44.792 1.00 30.53  ? 275  ILE A CB  1 
ATOM   2135 C CG1 . ILE A 1 274 ? -66.897 35.343 -43.267 1.00 31.92  ? 275  ILE A CG1 1 
ATOM   2136 C CG2 . ILE A 1 274 ? -65.739 34.691 -45.485 1.00 31.64  ? 275  ILE A CG2 1 
ATOM   2137 C CD1 . ILE A 1 274 ? -67.508 34.050 -42.791 1.00 32.93  ? 275  ILE A CD1 1 
ATOM   2138 N N   . ASP A 1 275 ? -67.277 37.306 -47.471 1.00 34.38  ? 276  ASP A N   1 
ATOM   2139 C CA  . ASP A 1 275 ? -67.045 37.466 -48.911 1.00 30.56  ? 276  ASP A CA  1 
ATOM   2140 C C   . ASP A 1 275 ? -66.375 38.765 -49.283 1.00 31.36  ? 276  ASP A C   1 
ATOM   2141 O O   . ASP A 1 275 ? -65.697 38.774 -50.257 1.00 31.04  ? 276  ASP A O   1 
ATOM   2142 C CB  . ASP A 1 275 ? -68.386 37.407 -49.670 1.00 31.78  ? 276  ASP A CB  1 
ATOM   2143 C CG  . ASP A 1 275 ? -68.857 36.020 -49.902 1.00 31.29  ? 276  ASP A CG  1 
ATOM   2144 O OD1 . ASP A 1 275 ? -68.104 35.034 -49.674 1.00 39.30  ? 276  ASP A OD1 1 
ATOM   2145 O OD2 . ASP A 1 275 ? -70.009 35.896 -50.272 1.00 37.43  ? 276  ASP A OD2 1 
ATOM   2146 N N   . VAL A 1 276 ? -66.575 39.854 -48.537 1.00 30.67  ? 277  VAL A N   1 
ATOM   2147 C CA  . VAL A 1 276 ? -65.969 41.162 -48.859 1.00 27.89  ? 277  VAL A CA  1 
ATOM   2148 C C   . VAL A 1 276 ? -64.849 41.611 -47.928 1.00 27.23  ? 277  VAL A C   1 
ATOM   2149 O O   . VAL A 1 276 ? -64.260 42.729 -48.078 1.00 26.08  ? 277  VAL A O   1 
ATOM   2150 C CB  . VAL A 1 276 ? -67.060 42.262 -48.876 1.00 33.55  ? 277  VAL A CB  1 
ATOM   2151 C CG1 . VAL A 1 276 ? -68.011 42.019 -50.068 1.00 33.34  ? 277  VAL A CG1 1 
ATOM   2152 C CG2 . VAL A 1 276 ? -67.856 42.292 -47.559 1.00 32.43  ? 277  VAL A CG2 1 
ATOM   2153 N N   . GLU A 1 277 ? -64.482 40.725 -46.997 1.00 25.89  ? 278  GLU A N   1 
ATOM   2154 C CA  . GLU A 1 277 ? -63.531 41.073 -45.867 1.00 23.28  ? 278  GLU A CA  1 
ATOM   2155 C C   . GLU A 1 277 ? -62.135 41.525 -46.359 1.00 26.19  ? 278  GLU A C   1 
ATOM   2156 O O   . GLU A 1 277 ? -61.444 42.372 -45.765 1.00 25.32  ? 278  GLU A O   1 
ATOM   2157 C CB  . GLU A 1 277 ? -63.430 39.785 -45.016 1.00 25.74  ? 278  GLU A CB  1 
ATOM   2158 C CG  . GLU A 1 277 ? -62.414 39.781 -43.917 1.00 27.98  ? 278  GLU A CG  1 
ATOM   2159 C CD  . GLU A 1 277 ? -62.274 38.476 -43.153 1.00 28.82  ? 278  GLU A CD  1 
ATOM   2160 O OE1 . GLU A 1 277 ? -63.179 37.644 -43.081 1.00 31.21  ? 278  GLU A OE1 1 
ATOM   2161 O OE2 . GLU A 1 277 ? -61.163 38.278 -42.635 1.00 36.51  ? 278  GLU A OE2 1 
ATOM   2162 N N   . TRP A 1 278 ? -61.665 40.907 -47.441 1.00 26.27  ? 279  TRP A N   1 
ATOM   2163 C CA  . TRP A 1 278 ? -60.328 41.202 -47.948 1.00 24.35  ? 279  TRP A CA  1 
ATOM   2164 C C   . TRP A 1 278 ? -60.353 42.443 -48.710 1.00 25.28  ? 279  TRP A C   1 
ATOM   2165 O O   . TRP A 1 278 ? -59.314 43.012 -48.905 1.00 35.01  ? 279  TRP A O   1 
ATOM   2166 C CB  . TRP A 1 278 ? -59.813 40.071 -48.758 1.00 28.01  ? 279  TRP A CB  1 
ATOM   2167 C CG  . TRP A 1 278 ? -59.743 38.863 -47.959 1.00 32.03  ? 279  TRP A CG  1 
ATOM   2168 C CD1 . TRP A 1 278 ? -60.687 37.882 -47.879 1.00 33.95  ? 279  TRP A CD1 1 
ATOM   2169 C CD2 . TRP A 1 278 ? -58.720 38.531 -47.013 1.00 30.23  ? 279  TRP A CD2 1 
ATOM   2170 N NE1 . TRP A 1 278 ? -60.294 36.912 -46.962 1.00 38.02  ? 279  TRP A NE1 1 
ATOM   2171 C CE2 . TRP A 1 278 ? -59.078 37.288 -46.430 1.00 36.93  ? 279  TRP A CE2 1 
ATOM   2172 C CE3 . TRP A 1 278 ? -57.518 39.112 -46.668 1.00 38.01  ? 279  TRP A CE3 1 
ATOM   2173 C CZ2 . TRP A 1 278 ? -58.276 36.637 -45.504 1.00 39.58  ? 279  TRP A CZ2 1 
ATOM   2174 C CZ3 . TRP A 1 278 ? -56.677 38.437 -45.739 1.00 45.24  ? 279  TRP A CZ3 1 
ATOM   2175 C CH2 . TRP A 1 278 ? -57.073 37.209 -45.173 1.00 40.34  ? 279  TRP A CH2 1 
ATOM   2176 N N   . ASN A 1 279 ? -61.535 42.999 -48.987 1.00 28.59  ? 280  ASN A N   1 
ATOM   2177 C CA  . ASN A 1 279 ? -61.568 44.293 -49.732 1.00 28.56  ? 280  ASN A CA  1 
ATOM   2178 C C   . ASN A 1 279 ? -61.216 45.521 -48.973 1.00 27.90  ? 280  ASN A C   1 
ATOM   2179 O O   . ASN A 1 279 ? -61.099 46.581 -49.576 1.00 30.09  ? 280  ASN A O   1 
ATOM   2180 C CB  . ASN A 1 279 ? -62.923 44.515 -50.405 1.00 27.76  ? 280  ASN A CB  1 
ATOM   2181 C CG  . ASN A 1 279 ? -63.346 43.339 -51.294 1.00 30.85  ? 280  ASN A CG  1 
ATOM   2182 O OD1 . ASN A 1 279 ? -62.531 42.500 -51.692 1.00 32.11  ? 280  ASN A OD1 1 
ATOM   2183 N ND2 . ASN A 1 279 ? -64.621 43.268 -51.592 1.00 31.18  ? 280  ASN A ND2 1 
ATOM   2184 N N   . VAL A 1 280 ? -60.986 45.438 -47.674 1.00 29.61  ? 281  VAL A N   1 
ATOM   2185 C CA  . VAL A 1 280 ? -60.814 46.689 -46.873 1.00 28.99  ? 281  VAL A CA  1 
ATOM   2186 C C   . VAL A 1 280 ? -59.384 47.022 -46.548 1.00 27.82  ? 281  VAL A C   1 
ATOM   2187 O O   . VAL A 1 280 ? -59.094 47.991 -45.816 1.00 27.54  ? 281  VAL A O   1 
ATOM   2188 C CB  . VAL A 1 280 ? -61.638 46.663 -45.548 1.00 29.17  ? 281  VAL A CB  1 
ATOM   2189 C CG1 . VAL A 1 280 ? -63.115 46.295 -45.862 1.00 30.02  ? 281  VAL A CG1 1 
ATOM   2190 C CG2 . VAL A 1 280 ? -61.079 45.665 -44.520 1.00 29.32  ? 281  VAL A CG2 1 
ATOM   2191 N N   . LEU A 1 281 ? -58.477 46.180 -47.006 1.00 27.14  ? 282  LEU A N   1 
ATOM   2192 C CA  . LEU A 1 281 ? -57.044 46.358 -46.636 1.00 27.93  ? 282  LEU A CA  1 
ATOM   2193 C C   . LEU A 1 281 ? -56.549 47.581 -47.349 1.00 29.85  ? 282  LEU A C   1 
ATOM   2194 O O   . LEU A 1 281 ? -56.924 47.825 -48.501 1.00 31.56  ? 282  LEU A O   1 
ATOM   2195 C CB  . LEU A 1 281 ? -56.179 45.181 -47.088 1.00 29.35  ? 282  LEU A CB  1 
ATOM   2196 C CG  . LEU A 1 281 ? -56.376 43.921 -46.270 1.00 31.37  ? 282  LEU A CG  1 
ATOM   2197 C CD1 . LEU A 1 281 ? -55.624 42.812 -46.972 1.00 33.17  ? 282  LEU A CD1 1 
ATOM   2198 C CD2 . LEU A 1 281 ? -55.812 44.125 -44.856 1.00 30.76  ? 282  LEU A CD2 1 
ATOM   2199 N N   . PRO A 1 282 ? -55.694 48.338 -46.696 1.00 29.32  ? 283  PRO A N   1 
ATOM   2200 C CA  . PRO A 1 282 ? -55.386 49.639 -47.265 1.00 31.80  ? 283  PRO A CA  1 
ATOM   2201 C C   . PRO A 1 282 ? -54.349 49.559 -48.379 1.00 34.37  ? 283  PRO A C   1 
ATOM   2202 O O   . PRO A 1 282 ? -54.271 50.480 -49.179 1.00 34.13  ? 283  PRO A O   1 
ATOM   2203 C CB  . PRO A 1 282 ? -54.827 50.436 -46.045 1.00 30.57  ? 283  PRO A CB  1 
ATOM   2204 C CG  . PRO A 1 282 ? -54.309 49.373 -45.134 1.00 31.12  ? 283  PRO A CG  1 
ATOM   2205 C CD  . PRO A 1 282 ? -55.178 48.175 -45.328 1.00 29.43  ? 283  PRO A CD  1 
ATOM   2206 N N   . PHE A 1 283 ? -53.527 48.498 -48.370 1.00 36.02  ? 284  PHE A N   1 
ATOM   2207 C CA  . PHE A 1 283 ? -52.477 48.267 -49.355 1.00 34.82  ? 284  PHE A CA  1 
ATOM   2208 C C   . PHE A 1 283 ? -52.563 46.895 -50.019 1.00 34.02  ? 284  PHE A C   1 
ATOM   2209 O O   . PHE A 1 283 ? -53.162 45.928 -49.525 1.00 29.87  ? 284  PHE A O   1 
ATOM   2210 C CB  . PHE A 1 283 ? -51.081 48.369 -48.728 1.00 37.69  ? 284  PHE A CB  1 
ATOM   2211 C CG  . PHE A 1 283 ? -50.898 49.562 -47.851 1.00 44.10  ? 284  PHE A CG  1 
ATOM   2212 C CD1 . PHE A 1 283 ? -50.760 50.842 -48.404 1.00 46.11  ? 284  PHE A CD1 1 
ATOM   2213 C CD2 . PHE A 1 283 ? -50.896 49.419 -46.437 1.00 50.66  ? 284  PHE A CD2 1 
ATOM   2214 C CE1 . PHE A 1 283 ? -50.609 51.959 -47.570 1.00 50.70  ? 284  PHE A CE1 1 
ATOM   2215 C CE2 . PHE A 1 283 ? -50.734 50.521 -45.599 1.00 46.16  ? 284  PHE A CE2 1 
ATOM   2216 C CZ  . PHE A 1 283 ? -50.596 51.797 -46.164 1.00 49.58  ? 284  PHE A CZ  1 
ATOM   2217 N N   . ASP A 1 284 ? -51.873 46.820 -51.144 1.00 34.40  ? 285  ASP A N   1 
ATOM   2218 C CA  . ASP A 1 284 ? -51.618 45.571 -51.818 1.00 31.62  ? 285  ASP A CA  1 
ATOM   2219 C C   . ASP A 1 284 ? -50.443 44.943 -51.070 1.00 28.58  ? 285  ASP A C   1 
ATOM   2220 O O   . ASP A 1 284 ? -49.270 45.425 -51.091 1.00 30.61  ? 285  ASP A O   1 
ATOM   2221 C CB  . ASP A 1 284 ? -51.244 45.884 -53.269 1.00 33.19  ? 285  ASP A CB  1 
ATOM   2222 C CG  . ASP A 1 284 ? -51.119 44.668 -54.098 1.00 34.01  ? 285  ASP A CG  1 
ATOM   2223 O OD1 . ASP A 1 284 ? -51.532 43.579 -53.638 1.00 33.01  ? 285  ASP A OD1 1 
ATOM   2224 O OD2 . ASP A 1 284 ? -50.617 44.818 -55.227 1.00 37.52  ? 285  ASP A OD2 1 
ATOM   2225 N N   . SER A 1 285 ? -50.752 43.899 -50.360 1.00 25.51  ? 286  SER A N   1 
ATOM   2226 C CA  . SER A 1 285 ? -49.819 43.403 -49.360 1.00 26.38  ? 286  SER A CA  1 
ATOM   2227 C C   . SER A 1 285 ? -49.974 41.913 -49.233 1.00 26.12  ? 286  SER A C   1 
ATOM   2228 O O   . SER A 1 285 ? -50.961 41.341 -49.678 1.00 25.13  ? 286  SER A O   1 
ATOM   2229 C CB  . SER A 1 285 ? -50.163 44.076 -48.018 1.00 28.58  ? 286  SER A CB  1 
ATOM   2230 O OG  . SER A 1 285 ? -51.543 43.785 -47.673 1.00 29.46  ? 286  SER A OG  1 
ATOM   2231 N N   . ILE A 1 286 ? -48.984 41.279 -48.636 1.00 26.69  ? 287  ILE A N   1 
ATOM   2232 C CA  . ILE A 1 286 ? -49.178 39.995 -48.069 1.00 24.51  ? 287  ILE A CA  1 
ATOM   2233 C C   . ILE A 1 286 ? -48.849 40.027 -46.569 1.00 25.24  ? 287  ILE A C   1 
ATOM   2234 O O   . ILE A 1 286 ? -48.145 40.945 -46.064 1.00 25.76  ? 287  ILE A O   1 
ATOM   2235 C CB  . ILE A 1 286 ? -48.271 38.999 -48.739 1.00 26.08  ? 287  ILE A CB  1 
ATOM   2236 C CG1 . ILE A 1 286 ? -46.842 39.364 -48.523 1.00 25.87  ? 287  ILE A CG1 1 
ATOM   2237 C CG2 . ILE A 1 286 ? -48.569 38.904 -50.213 1.00 30.75  ? 287  ILE A CG2 1 
ATOM   2238 C CD1 . ILE A 1 286 ? -45.924 38.325 -49.115 1.00 27.79  ? 287  ILE A CD1 1 
ATOM   2239 N N   . PHE A 1 287 ? -49.279 38.985 -45.882 1.00 24.69  ? 288  PHE A N   1 
ATOM   2240 C CA  . PHE A 1 287 ? -49.178 38.910 -44.401 1.00 25.72  ? 288  PHE A CA  1 
ATOM   2241 C C   . PHE A 1 287 ? -49.866 40.073 -43.694 1.00 24.26  ? 288  PHE A C   1 
ATOM   2242 O O   . PHE A 1 287 ? -49.337 40.636 -42.746 1.00 25.55  ? 288  PHE A O   1 
ATOM   2243 C CB  . PHE A 1 287 ? -47.714 38.844 -43.966 1.00 25.13  ? 288  PHE A CB  1 
ATOM   2244 C CG  . PHE A 1 287 ? -47.435 37.813 -42.888 1.00 28.44  ? 288  PHE A CG  1 
ATOM   2245 C CD1 . PHE A 1 287 ? -48.211 37.744 -41.726 1.00 26.62  ? 288  PHE A CD1 1 
ATOM   2246 C CD2 . PHE A 1 287 ? -46.337 36.981 -42.992 1.00 26.90  ? 288  PHE A CD2 1 
ATOM   2247 C CE1 . PHE A 1 287 ? -47.903 36.848 -40.724 1.00 29.34  ? 288  PHE A CE1 1 
ATOM   2248 C CE2 . PHE A 1 287 ? -46.053 36.071 -42.001 1.00 27.96  ? 288  PHE A CE2 1 
ATOM   2249 C CZ  . PHE A 1 287 ? -46.849 35.996 -40.855 1.00 28.99  ? 288  PHE A CZ  1 
ATOM   2250 N N   . ARG A 1 288 ? -50.995 40.488 -44.225 1.00 27.44  ? 289  ARG A N   1 
ATOM   2251 C CA  . ARG A 1 288 ? -51.828 41.516 -43.612 1.00 27.00  ? 289  ARG A CA  1 
ATOM   2252 C C   . ARG A 1 288 ? -53.272 41.045 -43.644 1.00 28.51  ? 289  ARG A C   1 
ATOM   2253 O O   . ARG A 1 288 ? -53.739 40.475 -44.649 1.00 29.42  ? 289  ARG A O   1 
ATOM   2254 C CB  . ARG A 1 288 ? -51.688 42.872 -44.271 1.00 26.42  ? 289  ARG A CB  1 
ATOM   2255 C CG  . ARG A 1 288 ? -50.315 43.470 -44.170 1.00 27.95  ? 289  ARG A CG  1 
ATOM   2256 C CD  . ARG A 1 288 ? -49.916 43.814 -42.750 1.00 29.64  ? 289  ARG A CD  1 
ATOM   2257 N NE  . ARG A 1 288 ? -48.637 44.504 -42.690 1.00 28.66  ? 289  ARG A NE  1 
ATOM   2258 C CZ  . ARG A 1 288 ? -47.444 43.939 -42.660 1.00 29.41  ? 289  ARG A CZ  1 
ATOM   2259 N NH1 . ARG A 1 288 ? -47.333 42.623 -42.673 1.00 32.99  ? 289  ARG A NH1 1 
ATOM   2260 N NH2 . ARG A 1 288 ? -46.352 44.704 -42.587 1.00 30.22  ? 289  ARG A NH2 1 
ATOM   2261 N N   . PHE A 1 289 ? -53.950 41.245 -42.506 1.00 26.99  ? 290  PHE A N   1 
ATOM   2262 C CA  . PHE A 1 289 ? -55.296 40.778 -42.326 1.00 25.53  ? 290  PHE A CA  1 
ATOM   2263 C C   . PHE A 1 289 ? -56.186 41.963 -41.923 1.00 23.91  ? 290  PHE A C   1 
ATOM   2264 O O   . PHE A 1 289 ? -55.771 42.902 -41.286 1.00 28.27  ? 290  PHE A O   1 
ATOM   2265 C CB  . PHE A 1 289 ? -55.303 39.617 -41.295 1.00 25.81  ? 290  PHE A CB  1 
ATOM   2266 C CG  . PHE A 1 289 ? -54.102 38.698 -41.426 1.00 25.38  ? 290  PHE A CG  1 
ATOM   2267 C CD1 . PHE A 1 289 ? -53.944 37.881 -42.545 1.00 24.58  ? 290  PHE A CD1 1 
ATOM   2268 C CD2 . PHE A 1 289 ? -53.092 38.702 -40.489 1.00 25.36  ? 290  PHE A CD2 1 
ATOM   2269 C CE1 . PHE A 1 289 ? -52.794 37.073 -42.720 1.00 24.27  ? 290  PHE A CE1 1 
ATOM   2270 C CE2 . PHE A 1 289 ? -51.966 37.890 -40.627 1.00 25.26  ? 290  PHE A CE2 1 
ATOM   2271 C CZ  . PHE A 1 289 ? -51.828 37.054 -41.752 1.00 26.48  ? 290  PHE A CZ  1 
ATOM   2272 N N   . SER A 1 290 ? -57.424 41.862 -42.279 1.00 26.54  ? 291  SER A N   1 
ATOM   2273 C CA  . SER A 1 290 ? -58.357 42.955 -42.232 1.00 32.37  ? 291  SER A CA  1 
ATOM   2274 C C   . SER A 1 290 ? -58.764 43.333 -40.777 1.00 32.19  ? 291  SER A C   1 
ATOM   2275 O O   . SER A 1 290 ? -58.585 44.484 -40.387 1.00 25.34  ? 291  SER A O   1 
ATOM   2276 C CB  . SER A 1 290 ? -59.611 42.638 -43.079 1.00 30.11  ? 291  SER A CB  1 
ATOM   2277 O OG  . SER A 1 290 ? -59.251 42.383 -44.423 1.00 32.72  ? 291  SER A OG  1 
ATOM   2278 N N   . PHE A 1 291 ? -59.258 42.354 -40.018 1.00 28.92  ? 292  PHE A N   1 
ATOM   2279 C CA  . PHE A 1 291 ? -59.795 42.617 -38.647 1.00 27.32  ? 292  PHE A CA  1 
ATOM   2280 C C   . PHE A 1 291 ? -58.952 41.930 -37.577 1.00 25.02  ? 292  PHE A C   1 
ATOM   2281 O O   . PHE A 1 291 ? -59.044 40.736 -37.381 1.00 22.44  ? 292  PHE A O   1 
ATOM   2282 C CB  . PHE A 1 291 ? -61.255 42.159 -38.579 1.00 27.24  ? 292  PHE A CB  1 
ATOM   2283 C CG  . PHE A 1 291 ? -62.110 42.886 -39.570 1.00 26.64  ? 292  PHE A CG  1 
ATOM   2284 C CD1 . PHE A 1 291 ? -62.422 44.236 -39.381 1.00 28.14  ? 292  PHE A CD1 1 
ATOM   2285 C CD2 . PHE A 1 291 ? -62.446 42.281 -40.785 1.00 28.78  ? 292  PHE A CD2 1 
ATOM   2286 C CE1 . PHE A 1 291 ? -63.135 44.957 -40.351 1.00 26.21  ? 292  PHE A CE1 1 
ATOM   2287 C CE2 . PHE A 1 291 ? -63.130 42.999 -41.756 1.00 29.14  ? 292  PHE A CE2 1 
ATOM   2288 C CZ  . PHE A 1 291 ? -63.491 44.326 -41.519 1.00 29.21  ? 292  PHE A CZ  1 
ATOM   2289 N N   . VAL A 1 292 ? -58.103 42.739 -36.963 1.00 24.50  ? 293  VAL A N   1 
ATOM   2290 C CA  . VAL A 1 292 ? -57.179 42.380 -35.962 1.00 23.17  ? 293  VAL A CA  1 
ATOM   2291 C C   . VAL A 1 292 ? -57.335 43.273 -34.673 1.00 26.69  ? 293  VAL A C   1 
ATOM   2292 O O   . VAL A 1 292 ? -58.104 44.238 -34.660 1.00 25.60  ? 293  VAL A O   1 
ATOM   2293 C CB  . VAL A 1 292 ? -55.799 42.563 -36.530 1.00 22.29  ? 293  VAL A CB  1 
ATOM   2294 C CG1 . VAL A 1 292 ? -55.581 41.671 -37.718 1.00 23.43  ? 293  VAL A CG1 1 
ATOM   2295 C CG2 . VAL A 1 292 ? -55.523 43.998 -36.883 1.00 22.98  ? 293  VAL A CG2 1 
ATOM   2296 N N   . PRO A 1 293 ? -56.642 42.922 -33.566 1.00 25.14  ? 294  PRO A N   1 
ATOM   2297 C CA  . PRO A 1 293 ? -56.701 43.710 -32.364 1.00 25.46  ? 294  PRO A CA  1 
ATOM   2298 C C   . PRO A 1 293 ? -56.430 45.203 -32.624 1.00 27.19  ? 294  PRO A C   1 
ATOM   2299 O O   . PRO A 1 293 ? -55.639 45.512 -33.507 1.00 25.67  ? 294  PRO A O   1 
ATOM   2300 C CB  . PRO A 1 293 ? -55.585 43.116 -31.522 1.00 24.21  ? 294  PRO A CB  1 
ATOM   2301 C CG  . PRO A 1 293 ? -55.647 41.696 -31.844 1.00 26.05  ? 294  PRO A CG  1 
ATOM   2302 C CD  . PRO A 1 293 ? -55.999 41.634 -33.315 1.00 26.17  ? 294  PRO A CD  1 
ATOM   2303 N N   . VAL A 1 294 ? -57.071 46.072 -31.847 1.00 26.40  ? 295  VAL A N   1 
ATOM   2304 C CA  . VAL A 1 294 ? -56.875 47.511 -31.952 1.00 30.19  ? 295  VAL A CA  1 
ATOM   2305 C C   . VAL A 1 294 ? -56.350 48.088 -30.639 1.00 30.69  ? 295  VAL A C   1 
ATOM   2306 O O   . VAL A 1 294 ? -56.825 47.743 -29.557 1.00 26.58  ? 295  VAL A O   1 
ATOM   2307 C CB  . VAL A 1 294 ? -58.182 48.232 -32.333 1.00 35.69  ? 295  VAL A CB  1 
ATOM   2308 C CG1 . VAL A 1 294 ? -58.413 48.151 -33.834 1.00 44.71  ? 295  VAL A CG1 1 
ATOM   2309 C CG2 . VAL A 1 294 ? -59.357 47.638 -31.572 1.00 36.43  ? 295  VAL A CG2 1 
ATOM   2310 N N   . ILE A 1 295 ? -55.363 48.969 -30.753 1.00 26.58  ? 296  ILE A N   1 
ATOM   2311 C CA  . ILE A 1 295 ? -54.746 49.601 -29.631 1.00 28.15  ? 296  ILE A CA  1 
ATOM   2312 C C   . ILE A 1 295 ? -55.729 50.676 -29.168 1.00 31.61  ? 296  ILE A C   1 
ATOM   2313 O O   . ILE A 1 295 ? -55.751 51.828 -29.729 1.00 27.69  ? 296  ILE A O   1 
ATOM   2314 C CB  . ILE A 1 295 ? -53.413 50.192 -30.054 1.00 29.61  ? 296  ILE A CB  1 
ATOM   2315 C CG1 . ILE A 1 295 ? -52.535 49.084 -30.708 1.00 28.62  ? 296  ILE A CG1 1 
ATOM   2316 C CG2 . ILE A 1 295 ? -52.694 50.783 -28.859 1.00 30.96  ? 296  ILE A CG2 1 
ATOM   2317 C CD1 . ILE A 1 295 ? -52.332 47.805 -29.895 1.00 27.28  ? 296  ILE A CD1 1 
ATOM   2318 N N   . ASP A 1 296 ? -56.577 50.253 -28.200 1.00 27.08  ? 297  ASP A N   1 
ATOM   2319 C CA  . ASP A 1 296 ? -57.822 50.942 -27.839 1.00 29.86  ? 297  ASP A CA  1 
ATOM   2320 C C   . ASP A 1 296 ? -57.735 51.832 -26.589 1.00 32.48  ? 297  ASP A C   1 
ATOM   2321 O O   . ASP A 1 296 ? -58.670 52.569 -26.327 1.00 36.32  ? 297  ASP A O   1 
ATOM   2322 C CB  . ASP A 1 296 ? -58.992 49.957 -27.592 1.00 28.18  ? 297  ASP A CB  1 
ATOM   2323 C CG  . ASP A 1 296 ? -58.658 48.929 -26.540 1.00 29.95  ? 297  ASP A CG  1 
ATOM   2324 O OD1 . ASP A 1 296 ? -57.452 48.852 -26.153 1.00 29.02  ? 297  ASP A OD1 1 
ATOM   2325 O OD2 . ASP A 1 296 ? -59.554 48.189 -26.118 1.00 33.79  ? 297  ASP A OD2 1 
ATOM   2326 N N   . GLY A 1 297 ? -56.676 51.722 -25.807 1.00 36.46  ? 298  GLY A N   1 
ATOM   2327 C CA  . GLY A 1 297 ? -56.611 52.395 -24.509 1.00 39.78  ? 298  GLY A CA  1 
ATOM   2328 C C   . GLY A 1 297 ? -57.289 51.643 -23.348 1.00 42.83  ? 298  GLY A C   1 
ATOM   2329 O O   . GLY A 1 297 ? -57.361 52.166 -22.275 1.00 40.35  ? 298  GLY A O   1 
ATOM   2330 N N   . GLU A 1 298 ? -57.780 50.427 -23.559 1.00 37.05  ? 299  GLU A N   1 
ATOM   2331 C CA  . GLU A 1 298 ? -58.507 49.697 -22.543 1.00 39.29  ? 299  GLU A CA  1 
ATOM   2332 C C   . GLU A 1 298 ? -57.835 48.323 -22.354 1.00 33.40  ? 299  GLU A C   1 
ATOM   2333 O O   . GLU A 1 298 ? -57.084 48.096 -21.406 1.00 29.16  ? 299  GLU A O   1 
ATOM   2334 C CB  . GLU A 1 298 ? -59.985 49.552 -22.955 1.00 46.56  ? 299  GLU A CB  1 
ATOM   2335 C CG  . GLU A 1 298 ? -60.944 50.533 -22.280 1.00 62.96  ? 299  GLU A CG  1 
ATOM   2336 C CD  . GLU A 1 298 ? -61.928 51.238 -23.242 1.00 72.72  ? 299  GLU A CD  1 
ATOM   2337 O OE1 . GLU A 1 298 ? -62.366 50.661 -24.268 1.00 69.95  ? 299  GLU A OE1 1 
ATOM   2338 O OE2 . GLU A 1 298 ? -62.280 52.404 -22.956 1.00 84.27  ? 299  GLU A OE2 1 
ATOM   2339 N N   . PHE A 1 299 ? -58.052 47.432 -23.310 1.00 29.06  ? 300  PHE A N   1 
ATOM   2340 C CA  . PHE A 1 299 ? -57.348 46.195 -23.342 1.00 26.74  ? 300  PHE A CA  1 
ATOM   2341 C C   . PHE A 1 299 ? -55.841 46.459 -23.368 1.00 28.58  ? 300  PHE A C   1 
ATOM   2342 O O   . PHE A 1 299 ? -55.072 45.803 -22.623 1.00 25.91  ? 300  PHE A O   1 
ATOM   2343 C CB  . PHE A 1 299 ? -57.881 45.359 -24.512 1.00 27.93  ? 300  PHE A CB  1 
ATOM   2344 C CG  . PHE A 1 299 ? -57.454 43.952 -24.459 1.00 28.07  ? 300  PHE A CG  1 
ATOM   2345 C CD1 . PHE A 1 299 ? -56.123 43.618 -24.741 1.00 26.34  ? 300  PHE A CD1 1 
ATOM   2346 C CD2 . PHE A 1 299 ? -58.346 42.956 -24.063 1.00 27.61  ? 300  PHE A CD2 1 
ATOM   2347 C CE1 . PHE A 1 299 ? -55.717 42.319 -24.666 1.00 24.05  ? 300  PHE A CE1 1 
ATOM   2348 C CE2 . PHE A 1 299 ? -57.931 41.643 -23.993 1.00 22.77  ? 300  PHE A CE2 1 
ATOM   2349 C CZ  . PHE A 1 299 ? -56.619 41.348 -24.282 1.00 24.37  ? 300  PHE A CZ  1 
ATOM   2350 N N   . PHE A 1 300 ? -55.416 47.433 -24.193 1.00 30.19  ? 301  PHE A N   1 
ATOM   2351 C CA  . PHE A 1 300 ? -54.023 47.884 -24.225 1.00 27.96  ? 301  PHE A CA  1 
ATOM   2352 C C   . PHE A 1 300 ? -54.040 49.344 -23.815 1.00 32.07  ? 301  PHE A C   1 
ATOM   2353 O O   . PHE A 1 300 ? -54.672 50.158 -24.496 1.00 31.95  ? 301  PHE A O   1 
ATOM   2354 C CB  . PHE A 1 300 ? -53.450 47.804 -25.618 1.00 26.57  ? 301  PHE A CB  1 
ATOM   2355 C CG  . PHE A 1 300 ? -53.565 46.452 -26.265 1.00 25.58  ? 301  PHE A CG  1 
ATOM   2356 C CD1 . PHE A 1 300 ? -52.696 45.447 -25.945 1.00 24.82  ? 301  PHE A CD1 1 
ATOM   2357 C CD2 . PHE A 1 300 ? -54.501 46.211 -27.209 1.00 26.40  ? 301  PHE A CD2 1 
ATOM   2358 C CE1 . PHE A 1 300 ? -52.759 44.242 -26.553 1.00 26.06  ? 301  PHE A CE1 1 
ATOM   2359 C CE2 . PHE A 1 300 ? -54.586 44.977 -27.830 1.00 24.74  ? 301  PHE A CE2 1 
ATOM   2360 C CZ  . PHE A 1 300 ? -53.725 43.987 -27.487 1.00 23.80  ? 301  PHE A CZ  1 
ATOM   2361 N N   . PRO A 1 301 ? -53.417 49.677 -22.682 1.00 31.91  ? 302  PRO A N   1 
ATOM   2362 C CA  . PRO A 1 301 ? -53.685 51.008 -22.159 1.00 34.78  ? 302  PRO A CA  1 
ATOM   2363 C C   . PRO A 1 301 ? -52.889 52.088 -22.872 1.00 33.48  ? 302  PRO A C   1 
ATOM   2364 O O   . PRO A 1 301 ? -53.340 53.214 -22.928 1.00 36.83  ? 302  PRO A O   1 
ATOM   2365 C CB  . PRO A 1 301 ? -53.321 50.888 -20.656 1.00 31.86  ? 302  PRO A CB  1 
ATOM   2366 C CG  . PRO A 1 301 ? -52.480 49.666 -20.547 1.00 37.77  ? 302  PRO A CG  1 
ATOM   2367 C CD  . PRO A 1 301 ? -53.009 48.749 -21.611 1.00 37.01  ? 302  PRO A CD  1 
ATOM   2368 N N   . THR A 1 302 ? -51.701 51.749 -23.363 1.00 34.61  ? 303  THR A N   1 
ATOM   2369 C CA  . THR A 1 302 ? -50.913 52.563 -24.271 1.00 31.96  ? 303  THR A CA  1 
ATOM   2370 C C   . THR A 1 302 ? -50.309 51.724 -25.420 1.00 33.51  ? 303  THR A C   1 
ATOM   2371 O O   . THR A 1 302 ? -50.510 50.519 -25.535 1.00 30.38  ? 303  THR A O   1 
ATOM   2372 C CB  . THR A 1 302 ? -49.781 53.269 -23.510 1.00 36.14  ? 303  THR A CB  1 
ATOM   2373 O OG1 . THR A 1 302 ? -48.794 52.337 -23.025 1.00 35.22  ? 303  THR A OG1 1 
ATOM   2374 C CG2 . THR A 1 302 ? -50.365 54.009 -22.324 1.00 39.81  ? 303  THR A CG2 1 
ATOM   2375 N N   . SER A 1 303 ? -49.467 52.362 -26.213 1.00 32.87  ? 304  SER A N   1 
ATOM   2376 C CA  . SER A 1 303 ? -48.902 51.700 -27.345 1.00 31.01  ? 304  SER A CA  1 
ATOM   2377 C C   . SER A 1 303 ? -48.163 50.479 -26.851 1.00 32.03  ? 304  SER A C   1 
ATOM   2378 O O   . SER A 1 303 ? -47.640 50.486 -25.725 1.00 30.85  ? 304  SER A O   1 
ATOM   2379 C CB  . SER A 1 303 ? -47.922 52.611 -28.081 1.00 29.93  ? 304  SER A CB  1 
ATOM   2380 O OG  . SER A 1 303 ? -46.756 52.784 -27.298 1.00 31.58  ? 304  SER A OG  1 
ATOM   2381 N N   . LEU A 1 304 ? -48.070 49.457 -27.720 1.00 30.22  ? 305  LEU A N   1 
ATOM   2382 C CA  . LEU A 1 304 ? -47.414 48.233 -27.300 1.00 30.84  ? 305  LEU A CA  1 
ATOM   2383 C C   . LEU A 1 304 ? -45.969 48.511 -26.950 1.00 32.24  ? 305  LEU A C   1 
ATOM   2384 O O   . LEU A 1 304 ? -45.446 47.947 -26.000 1.00 31.45  ? 305  LEU A O   1 
ATOM   2385 C CB  . LEU A 1 304 ? -47.491 47.147 -28.327 1.00 26.44  ? 305  LEU A CB  1 
ATOM   2386 C CG  . LEU A 1 304 ? -48.892 46.743 -28.729 1.00 28.08  ? 305  LEU A CG  1 
ATOM   2387 C CD1 . LEU A 1 304 ? -48.835 45.618 -29.757 1.00 28.54  ? 305  LEU A CD1 1 
ATOM   2388 C CD2 . LEU A 1 304 ? -49.812 46.411 -27.574 1.00 31.42  ? 305  LEU A CD2 1 
ATOM   2389 N N   . GLU A 1 305 ? -45.328 49.383 -27.716 1.00 29.29  ? 306  GLU A N   1 
ATOM   2390 C CA  . GLU A 1 305 ? -43.909 49.634 -27.534 1.00 30.33  ? 306  GLU A CA  1 
ATOM   2391 C C   . GLU A 1 305 ? -43.674 50.396 -26.216 1.00 32.29  ? 306  GLU A C   1 
ATOM   2392 O O   . GLU A 1 305 ? -42.685 50.173 -25.555 1.00 28.89  ? 306  GLU A O   1 
ATOM   2393 C CB  . GLU A 1 305 ? -43.379 50.458 -28.722 1.00 31.12  ? 306  GLU A CB  1 
ATOM   2394 C CG  . GLU A 1 305 ? -41.913 50.908 -28.658 1.00 33.33  ? 306  GLU A CG  1 
ATOM   2395 C CD  . GLU A 1 305 ? -40.911 49.759 -28.694 1.00 38.54  ? 306  GLU A CD  1 
ATOM   2396 O OE1 . GLU A 1 305 ? -41.285 48.589 -28.979 1.00 39.17  ? 306  GLU A OE1 1 
ATOM   2397 O OE2 . GLU A 1 305 ? -39.720 50.026 -28.433 1.00 42.57  ? 306  GLU A OE2 1 
ATOM   2398 N N   . SER A 1 306 ? -44.569 51.333 -25.851 1.00 34.01  ? 307  SER A N   1 
ATOM   2399 C CA  . SER A 1 306 ? -44.362 52.049 -24.586 1.00 32.04  ? 307  SER A CA  1 
ATOM   2400 C C   . SER A 1 306 ? -44.566 51.061 -23.378 1.00 32.57  ? 307  SER A C   1 
ATOM   2401 O O   . SER A 1 306 ? -43.771 51.091 -22.423 1.00 31.82  ? 307  SER A O   1 
ATOM   2402 C CB  . SER A 1 306 ? -45.208 53.320 -24.498 1.00 28.01  ? 307  SER A CB  1 
ATOM   2403 O OG  . SER A 1 306 ? -46.554 53.027 -24.232 1.00 37.85  ? 307  SER A OG  1 
ATOM   2404 N N   . MET A 1 307 ? -45.555 50.147 -23.457 1.00 28.24  ? 308  MET A N   1 
ATOM   2405 C CA  . MET A 1 307 ? -45.687 49.097 -22.425 1.00 29.49  ? 308  MET A CA  1 
ATOM   2406 C C   . MET A 1 307 ? -44.437 48.251 -22.373 1.00 30.28  ? 308  MET A C   1 
ATOM   2407 O O   . MET A 1 307 ? -43.926 47.955 -21.308 1.00 31.54  ? 308  MET A O   1 
ATOM   2408 C CB  . MET A 1 307 ? -46.935 48.216 -22.639 1.00 29.62  ? 308  MET A CB  1 
ATOM   2409 C CG  . MET A 1 307 ? -48.221 48.984 -22.638 1.00 27.28  ? 308  MET A CG  1 
ATOM   2410 S SD  . MET A 1 307 ? -49.680 47.998 -23.066 1.00 32.61  ? 308  MET A SD  1 
ATOM   2411 C CE  . MET A 1 307 ? -49.651 46.920 -21.596 1.00 34.76  ? 308  MET A CE  1 
ATOM   2412 N N   . LEU A 1 308 ? -43.889 47.875 -23.514 1.00 31.23  ? 309  LEU A N   1 
ATOM   2413 C CA  . LEU A 1 308 ? -42.715 47.017 -23.474 1.00 33.81  ? 309  LEU A CA  1 
ATOM   2414 C C   . LEU A 1 308 ? -41.512 47.686 -22.845 1.00 36.72  ? 309  LEU A C   1 
ATOM   2415 O O   . LEU A 1 308 ? -40.719 47.064 -22.079 1.00 38.65  ? 309  LEU A O   1 
ATOM   2416 C CB  . LEU A 1 308 ? -42.357 46.501 -24.875 1.00 35.41  ? 309  LEU A CB  1 
ATOM   2417 C CG  . LEU A 1 308 ? -43.278 45.364 -25.346 1.00 38.23  ? 309  LEU A CG  1 
ATOM   2418 C CD1 . LEU A 1 308 ? -43.032 45.122 -26.809 1.00 38.49  ? 309  LEU A CD1 1 
ATOM   2419 C CD2 . LEU A 1 308 ? -43.142 44.033 -24.598 1.00 32.98  ? 309  LEU A CD2 1 
ATOM   2420 N N   . ASN A 1 309 ? -41.358 48.955 -23.197 1.00 37.78  ? 310  ASN A N   1 
ATOM   2421 C CA  . ASN A 1 309 ? -40.290 49.794 -22.655 1.00 38.34  ? 310  ASN A CA  1 
ATOM   2422 C C   . ASN A 1 309 ? -40.360 50.073 -21.174 1.00 34.67  ? 310  ASN A C   1 
ATOM   2423 O O   . ASN A 1 309 ? -39.339 50.063 -20.552 1.00 32.49  ? 310  ASN A O   1 
ATOM   2424 C CB  . ASN A 1 309 ? -40.219 51.143 -23.405 1.00 44.31  ? 310  ASN A CB  1 
ATOM   2425 C CG  . ASN A 1 309 ? -39.375 51.025 -24.646 1.00 50.37  ? 310  ASN A CG  1 
ATOM   2426 O OD1 . ASN A 1 309 ? -38.481 50.171 -24.719 1.00 53.79  ? 310  ASN A OD1 1 
ATOM   2427 N ND2 . ASN A 1 309 ? -39.662 51.834 -25.633 1.00 54.02  ? 310  ASN A ND2 1 
ATOM   2428 N N   . SER A 1 310 ? -41.549 50.346 -20.641 1.00 32.88  ? 311  SER A N   1 
ATOM   2429 C CA  . SER A 1 310 ? -41.703 50.714 -19.251 1.00 34.00  ? 311  SER A CA  1 
ATOM   2430 C C   . SER A 1 310 ? -41.865 49.468 -18.378 1.00 35.87  ? 311  SER A C   1 
ATOM   2431 O O   . SER A 1 310 ? -41.924 49.592 -17.189 1.00 37.12  ? 311  SER A O   1 
ATOM   2432 C CB  . SER A 1 310 ? -42.945 51.605 -19.093 1.00 35.03  ? 311  SER A CB  1 
ATOM   2433 O OG  . SER A 1 310 ? -44.101 50.849 -19.442 1.00 44.46  ? 311  SER A OG  1 
ATOM   2434 N N   . GLY A 1 311 ? -41.943 48.276 -18.960 1.00 34.95  ? 312  GLY A N   1 
ATOM   2435 C CA  . GLY A 1 311 ? -42.146 47.054 -18.178 1.00 31.82  ? 312  GLY A CA  1 
ATOM   2436 C C   . GLY A 1 311 ? -43.609 46.912 -17.727 1.00 34.14  ? 312  GLY A C   1 
ATOM   2437 O O   . GLY A 1 311 ? -43.932 46.223 -16.784 1.00 27.12  ? 312  GLY A O   1 
ATOM   2438 N N   . ASN A 1 312 ? -44.516 47.590 -18.393 1.00 30.99  ? 313  ASN A N   1 
ATOM   2439 C CA  . ASN A 1 312 ? -45.888 47.434 -18.086 1.00 28.52  ? 313  ASN A CA  1 
ATOM   2440 C C   . ASN A 1 312 ? -46.429 46.138 -18.706 1.00 30.49  ? 313  ASN A C   1 
ATOM   2441 O O   . ASN A 1 312 ? -47.063 46.145 -19.780 1.00 32.78  ? 313  ASN A O   1 
ATOM   2442 C CB  . ASN A 1 312 ? -46.693 48.673 -18.527 1.00 26.15  ? 313  ASN A CB  1 
ATOM   2443 C CG  . ASN A 1 312 ? -48.076 48.662 -17.945 1.00 30.37  ? 313  ASN A CG  1 
ATOM   2444 O OD1 . ASN A 1 312 ? -48.381 47.778 -17.134 1.00 35.37  ? 313  ASN A OD1 1 
ATOM   2445 N ND2 . ASN A 1 312 ? -48.950 49.573 -18.398 1.00 32.16  ? 313  ASN A ND2 1 
ATOM   2446 N N   . PHE A 1 313 ? -46.169 45.034 -18.011 1.00 29.68  ? 314  PHE A N   1 
ATOM   2447 C CA  . PHE A 1 313 ? -46.610 43.712 -18.417 1.00 30.78  ? 314  PHE A CA  1 
ATOM   2448 C C   . PHE A 1 313 ? -46.381 42.665 -17.332 1.00 31.01  ? 314  PHE A C   1 
ATOM   2449 O O   . PHE A 1 313 ? -45.654 42.909 -16.402 1.00 30.59  ? 314  PHE A O   1 
ATOM   2450 C CB  . PHE A 1 313 ? -45.921 43.265 -19.732 1.00 28.42  ? 314  PHE A CB  1 
ATOM   2451 C CG  . PHE A 1 313 ? -44.430 43.430 -19.758 1.00 26.12  ? 314  PHE A CG  1 
ATOM   2452 C CD1 . PHE A 1 313 ? -43.579 42.448 -19.239 1.00 25.46  ? 314  PHE A CD1 1 
ATOM   2453 C CD2 . PHE A 1 313 ? -43.862 44.523 -20.387 1.00 27.84  ? 314  PHE A CD2 1 
ATOM   2454 C CE1 . PHE A 1 313 ? -42.185 42.605 -19.280 1.00 22.65  ? 314  PHE A CE1 1 
ATOM   2455 C CE2 . PHE A 1 313 ? -42.448 44.640 -20.481 1.00 26.53  ? 314  PHE A CE2 1 
ATOM   2456 C CZ  . PHE A 1 313 ? -41.627 43.692 -19.914 1.00 24.07  ? 314  PHE A CZ  1 
ATOM   2457 N N   . LYS A 1 314 ? -46.970 41.481 -17.512 1.00 30.78  ? 315  LYS A N   1 
ATOM   2458 C CA  . LYS A 1 314 ? -46.817 40.407 -16.553 1.00 29.80  ? 315  LYS A CA  1 
ATOM   2459 C C   . LYS A 1 314 ? -45.397 39.930 -16.539 1.00 32.31  ? 315  LYS A C   1 
ATOM   2460 O O   . LYS A 1 314 ? -44.832 39.580 -17.595 1.00 29.93  ? 315  LYS A O   1 
ATOM   2461 C CB  . LYS A 1 314 ? -47.727 39.218 -16.918 1.00 29.69  ? 315  LYS A CB  1 
ATOM   2462 C CG  . LYS A 1 314 ? -47.916 38.186 -15.810 1.00 26.01  ? 315  LYS A CG  1 
ATOM   2463 C CD  . LYS A 1 314 ? -48.570 36.910 -16.284 1.00 29.96  ? 315  LYS A CD  1 
ATOM   2464 C CE  . LYS A 1 314 ? -48.610 35.926 -15.142 1.00 32.73  ? 315  LYS A CE  1 
ATOM   2465 N NZ  . LYS A 1 314 ? -49.743 36.219 -14.237 1.00 26.73  ? 315  LYS A NZ  1 
ATOM   2466 N N   . LYS A 1 315 ? -44.831 39.855 -15.342 1.00 30.66  ? 316  LYS A N   1 
ATOM   2467 C CA  . LYS A 1 315 ? -43.482 39.312 -15.190 1.00 30.97  ? 316  LYS A CA  1 
ATOM   2468 C C   . LYS A 1 315 ? -43.494 37.866 -14.771 1.00 32.41  ? 316  LYS A C   1 
ATOM   2469 O O   . LYS A 1 315 ? -43.895 37.566 -13.729 1.00 33.69  ? 316  LYS A O   1 
ATOM   2470 C CB  . LYS A 1 315 ? -42.728 40.163 -14.185 1.00 35.59  ? 316  LYS A CB  1 
ATOM   2471 C CG  . LYS A 1 315 ? -42.482 41.501 -14.860 1.00 41.08  ? 316  LYS A CG  1 
ATOM   2472 C CD  . LYS A 1 315 ? -42.285 42.666 -13.957 1.00 39.82  ? 316  LYS A CD  1 
ATOM   2473 C CE  . LYS A 1 315 ? -42.297 43.904 -14.821 1.00 42.64  ? 316  LYS A CE  1 
ATOM   2474 N NZ  . LYS A 1 315 ? -43.347 44.830 -14.385 1.00 47.02  ? 316  LYS A NZ  1 
ATOM   2475 N N   . THR A 1 316 ? -43.001 36.962 -15.601 1.00 33.15  ? 317  THR A N   1 
ATOM   2476 C CA  . THR A 1 316 ? -43.104 35.566 -15.322 1.00 30.27  ? 317  THR A CA  1 
ATOM   2477 C C   . THR A 1 316 ? -42.096 34.918 -16.214 1.00 30.47  ? 317  THR A C   1 
ATOM   2478 O O   . THR A 1 316 ? -41.135 35.593 -16.654 1.00 31.57  ? 317  THR A O   1 
ATOM   2479 C CB  . THR A 1 316 ? -44.529 35.081 -15.556 1.00 33.33  ? 317  THR A CB  1 
ATOM   2480 O OG1 . THR A 1 316 ? -44.588 33.704 -15.226 1.00 32.90  ? 317  THR A OG1 1 
ATOM   2481 C CG2 . THR A 1 316 ? -44.994 35.359 -17.064 1.00 33.49  ? 317  THR A CG2 1 
ATOM   2482 N N   . GLN A 1 317 ? -42.258 33.635 -16.480 1.00 28.65  ? 318  GLN A N   1 
ATOM   2483 C CA  . GLN A 1 317 ? -41.341 32.969 -17.398 1.00 30.02  ? 318  GLN A CA  1 
ATOM   2484 C C   . GLN A 1 317 ? -41.998 32.835 -18.755 1.00 29.25  ? 318  GLN A C   1 
ATOM   2485 O O   . GLN A 1 317 ? -43.219 32.746 -18.864 1.00 28.89  ? 318  GLN A O   1 
ATOM   2486 C CB  . GLN A 1 317 ? -40.933 31.568 -16.922 1.00 31.37  ? 318  GLN A CB  1 
ATOM   2487 C CG  . GLN A 1 317 ? -40.295 31.486 -15.523 1.00 35.41  ? 318  GLN A CG  1 
ATOM   2488 C CD  . GLN A 1 317 ? -41.337 31.497 -14.381 1.00 33.51  ? 318  GLN A CD  1 
ATOM   2489 O OE1 . GLN A 1 317 ? -42.470 31.016 -14.524 1.00 30.35  ? 318  GLN A OE1 1 
ATOM   2490 N NE2 . GLN A 1 317 ? -41.001 32.186 -13.307 1.00 35.24  ? 318  GLN A NE2 1 
ATOM   2491 N N   . ILE A 1 318 ? -41.185 32.766 -19.789 1.00 27.83  ? 319  ILE A N   1 
ATOM   2492 C CA  . ILE A 1 318 ? -41.738 32.559 -21.133 1.00 26.30  ? 319  ILE A CA  1 
ATOM   2493 C C   . ILE A 1 318 ? -40.782 31.708 -21.900 1.00 25.94  ? 319  ILE A C   1 
ATOM   2494 O O   . ILE A 1 318 ? -39.561 31.734 -21.664 1.00 23.19  ? 319  ILE A O   1 
ATOM   2495 C CB  . ILE A 1 318 ? -41.965 33.880 -21.927 1.00 25.62  ? 319  ILE A CB  1 
ATOM   2496 C CG1 . ILE A 1 318 ? -40.673 34.627 -22.146 1.00 25.35  ? 319  ILE A CG1 1 
ATOM   2497 C CG2 . ILE A 1 318 ? -42.913 34.825 -21.227 1.00 26.27  ? 319  ILE A CG2 1 
ATOM   2498 C CD1 . ILE A 1 318 ? -40.813 35.789 -23.095 1.00 25.98  ? 319  ILE A CD1 1 
ATOM   2499 N N   . LEU A 1 319 ? -41.381 30.953 -22.813 1.00 25.36  ? 320  LEU A N   1 
ATOM   2500 C CA  . LEU A 1 319 ? -40.699 30.111 -23.725 1.00 28.60  ? 320  LEU A CA  1 
ATOM   2501 C C   . LEU A 1 319 ? -41.331 30.362 -25.103 1.00 31.33  ? 320  LEU A C   1 
ATOM   2502 O O   . LEU A 1 319 ? -42.564 30.360 -25.275 1.00 28.42  ? 320  LEU A O   1 
ATOM   2503 C CB  . LEU A 1 319 ? -40.871 28.671 -23.311 1.00 29.19  ? 320  LEU A CB  1 
ATOM   2504 C CG  . LEU A 1 319 ? -40.167 27.579 -24.145 1.00 32.45  ? 320  LEU A CG  1 
ATOM   2505 C CD1 . LEU A 1 319 ? -40.101 26.299 -23.327 1.00 33.01  ? 320  LEU A CD1 1 
ATOM   2506 C CD2 . LEU A 1 319 ? -40.907 27.270 -25.433 1.00 32.05  ? 320  LEU A CD2 1 
ATOM   2507 N N   . LEU A 1 320 ? -40.457 30.570 -26.073 1.00 32.45  ? 321  LEU A N   1 
ATOM   2508 C CA  . LEU A 1 320 ? -40.854 31.118 -27.335 1.00 29.93  ? 321  LEU A CA  1 
ATOM   2509 C C   . LEU A 1 320 ? -39.776 30.907 -28.408 1.00 31.70  ? 321  LEU A C   1 
ATOM   2510 O O   . LEU A 1 320 ? -38.619 30.577 -28.154 1.00 27.44  ? 321  LEU A O   1 
ATOM   2511 C CB  . LEU A 1 320 ? -41.297 32.567 -27.211 1.00 26.84  ? 321  LEU A CB  1 
ATOM   2512 C CG  . LEU A 1 320 ? -40.228 33.665 -27.218 1.00 27.67  ? 321  LEU A CG  1 
ATOM   2513 C CD1 . LEU A 1 320 ? -40.917 34.992 -27.147 1.00 23.68  ? 321  LEU A CD1 1 
ATOM   2514 C CD2 . LEU A 1 320 ? -39.264 33.551 -26.103 1.00 28.66  ? 321  LEU A CD2 1 
ATOM   2515 N N   . GLY A 1 321 ? -40.240 30.981 -29.641 1.00 30.31  ? 322  GLY A N   1 
ATOM   2516 C CA  . GLY A 1 321 ? -39.353 30.798 -30.758 1.00 31.17  ? 322  GLY A CA  1 
ATOM   2517 C C   . GLY A 1 321 ? -40.019 30.892 -32.095 1.00 27.30  ? 322  GLY A C   1 
ATOM   2518 O O   . GLY A 1 321 ? -41.222 31.224 -32.212 1.00 22.64  ? 322  GLY A O   1 
ATOM   2519 N N   . VAL A 1 322 ? -39.200 30.564 -33.093 1.00 27.61  ? 323  VAL A N   1 
ATOM   2520 C CA  . VAL A 1 322 ? -39.577 30.643 -34.486 1.00 26.91  ? 323  VAL A CA  1 
ATOM   2521 C C   . VAL A 1 322 ? -39.173 29.425 -35.350 1.00 28.83  ? 323  VAL A C   1 
ATOM   2522 O O   . VAL A 1 322 ? -38.396 28.604 -34.937 1.00 29.44  ? 323  VAL A O   1 
ATOM   2523 C CB  . VAL A 1 322 ? -39.031 31.887 -35.094 1.00 25.31  ? 323  VAL A CB  1 
ATOM   2524 C CG1 . VAL A 1 322 ? -39.494 33.089 -34.327 1.00 27.37  ? 323  VAL A CG1 1 
ATOM   2525 C CG2 . VAL A 1 322 ? -37.531 31.837 -35.155 1.00 28.28  ? 323  VAL A CG2 1 
ATOM   2526 N N   . ASN A 1 323 ? -39.827 29.286 -36.508 1.00 28.53  ? 324  ASN A N   1 
ATOM   2527 C CA  . ASN A 1 323 ? -39.406 28.347 -37.556 1.00 27.08  ? 324  ASN A CA  1 
ATOM   2528 C C   . ASN A 1 323 ? -38.527 28.997 -38.600 1.00 24.55  ? 324  ASN A C   1 
ATOM   2529 O O   . ASN A 1 323 ? -38.566 30.181 -38.809 1.00 25.02  ? 324  ASN A O   1 
ATOM   2530 C CB  . ASN A 1 323 ? -40.638 27.730 -38.209 1.00 27.71  ? 324  ASN A CB  1 
ATOM   2531 C CG  . ASN A 1 323 ? -41.499 26.975 -37.217 1.00 28.62  ? 324  ASN A CG  1 
ATOM   2532 O OD1 . ASN A 1 323 ? -41.187 26.937 -36.041 1.00 28.82  ? 324  ASN A OD1 1 
ATOM   2533 N ND2 . ASN A 1 323 ? -42.583 26.348 -37.699 1.00 31.34  ? 324  ASN A ND2 1 
ATOM   2534 N N   . LYS A 1 324 ? -37.727 28.206 -39.274 1.00 26.97  ? 325  LYS A N   1 
ATOM   2535 C CA  . LYS A 1 324 ? -36.766 28.718 -40.201 1.00 26.99  ? 325  LYS A CA  1 
ATOM   2536 C C   . LYS A 1 324 ? -37.338 29.443 -41.404 1.00 28.94  ? 325  LYS A C   1 
ATOM   2537 O O   . LYS A 1 324 ? -36.739 30.418 -41.866 1.00 24.56  ? 325  LYS A O   1 
ATOM   2538 C CB  . LYS A 1 324 ? -35.939 27.582 -40.712 1.00 32.63  ? 325  LYS A CB  1 
ATOM   2539 C CG  . LYS A 1 324 ? -34.706 27.985 -41.532 1.00 33.38  ? 325  LYS A CG  1 
ATOM   2540 C CD  . LYS A 1 324 ? -34.152 26.666 -42.087 1.00 39.12  ? 325  LYS A CD  1 
ATOM   2541 C CE  . LYS A 1 324 ? -32.830 26.830 -42.816 1.00 46.55  ? 325  LYS A CE  1 
ATOM   2542 N NZ  . LYS A 1 324 ? -32.995 27.783 -43.936 1.00 53.85  ? 325  LYS A NZ  1 
ATOM   2543 N N   . ASP A 1 325 ? -38.506 29.009 -41.886 1.00 26.30  ? 326  ASP A N   1 
ATOM   2544 C CA  . ASP A 1 325 ? -39.069 29.567 -43.112 1.00 25.94  ? 326  ASP A CA  1 
ATOM   2545 C C   . ASP A 1 325 ? -40.522 30.000 -42.900 1.00 31.37  ? 326  ASP A C   1 
ATOM   2546 O O   . ASP A 1 325 ? -41.510 29.433 -43.517 1.00 32.04  ? 326  ASP A O   1 
ATOM   2547 C CB  . ASP A 1 325 ? -38.970 28.505 -44.244 1.00 24.12  ? 326  ASP A CB  1 
ATOM   2548 C CG  . ASP A 1 325 ? -37.531 28.040 -44.501 1.00 26.68  ? 326  ASP A CG  1 
ATOM   2549 O OD1 . ASP A 1 325 ? -36.695 28.864 -44.882 1.00 27.09  ? 326  ASP A OD1 1 
ATOM   2550 O OD2 . ASP A 1 325 ? -37.214 26.846 -44.260 1.00 28.55  ? 326  ASP A OD2 1 
ATOM   2551 N N   . GLU A 1 326 ? -40.657 30.987 -42.024 1.00 30.60  ? 327  GLU A N   1 
ATOM   2552 C CA  . GLU A 1 326 ? -41.924 31.569 -41.679 1.00 30.03  ? 327  GLU A CA  1 
ATOM   2553 C C   . GLU A 1 326 ? -42.626 32.199 -42.900 1.00 32.02  ? 327  GLU A C   1 
ATOM   2554 O O   . GLU A 1 326 ? -43.840 32.104 -42.992 1.00 34.17  ? 327  GLU A O   1 
ATOM   2555 C CB  . GLU A 1 326 ? -41.751 32.648 -40.576 1.00 31.80  ? 327  GLU A CB  1 
ATOM   2556 C CG  . GLU A 1 326 ? -41.296 32.181 -39.200 1.00 31.00  ? 327  GLU A CG  1 
ATOM   2557 C CD  . GLU A 1 326 ? -42.299 31.371 -38.406 1.00 29.75  ? 327  GLU A CD  1 
ATOM   2558 O OE1 . GLU A 1 326 ? -43.433 31.080 -38.851 1.00 32.06  ? 327  GLU A OE1 1 
ATOM   2559 O OE2 . GLU A 1 326 ? -41.951 30.995 -37.271 1.00 33.21  ? 327  GLU A OE2 1 
ATOM   2560 N N   . GLY A 1 327 ? -41.883 32.781 -43.864 1.00 30.30  ? 328  GLY A N   1 
ATOM   2561 C CA  . GLY A 1 327 ? -42.553 33.478 -44.980 1.00 30.40  ? 328  GLY A CA  1 
ATOM   2562 C C   . GLY A 1 327 ? -43.175 32.732 -46.159 1.00 28.10  ? 328  GLY A C   1 
ATOM   2563 O O   . GLY A 1 327 ? -43.947 33.308 -46.937 1.00 27.77  ? 328  GLY A O   1 
ATOM   2564 N N   . SER A 1 328 ? -42.908 31.448 -46.294 1.00 30.56  ? 329  SER A N   1 
ATOM   2565 C CA  . SER A 1 328 ? -43.117 30.792 -47.581 1.00 26.71  ? 329  SER A CA  1 
ATOM   2566 C C   . SER A 1 328 ? -44.562 30.694 -47.946 1.00 30.07  ? 329  SER A C   1 
ATOM   2567 O O   . SER A 1 328 ? -44.939 30.830 -49.152 1.00 30.62  ? 329  SER A O   1 
ATOM   2568 C CB  . SER A 1 328 ? -42.406 29.473 -47.632 1.00 25.04  ? 329  SER A CB  1 
ATOM   2569 O OG  . SER A 1 328 ? -42.858 28.598 -46.660 1.00 26.82  ? 329  SER A OG  1 
ATOM   2570 N N   . PHE A 1 329 ? -45.388 30.406 -46.953 1.00 29.75  ? 330  PHE A N   1 
ATOM   2571 C CA  . PHE A 1 329 ? -46.823 30.284 -47.158 1.00 31.43  ? 330  PHE A CA  1 
ATOM   2572 C C   . PHE A 1 329 ? -47.408 31.546 -47.800 1.00 30.46  ? 330  PHE A C   1 
ATOM   2573 O O   . PHE A 1 329 ? -48.292 31.492 -48.658 1.00 30.78  ? 330  PHE A O   1 
ATOM   2574 C CB  . PHE A 1 329 ? -47.503 30.140 -45.804 1.00 36.07  ? 330  PHE A CB  1 
ATOM   2575 C CG  . PHE A 1 329 ? -48.304 28.969 -45.687 1.00 40.21  ? 330  PHE A CG  1 
ATOM   2576 C CD1 . PHE A 1 329 ? -49.473 28.876 -46.383 1.00 47.72  ? 330  PHE A CD1 1 
ATOM   2577 C CD2 . PHE A 1 329 ? -47.910 27.946 -44.851 1.00 52.81  ? 330  PHE A CD2 1 
ATOM   2578 C CE1 . PHE A 1 329 ? -50.254 27.733 -46.300 1.00 55.84  ? 330  PHE A CE1 1 
ATOM   2579 C CE2 . PHE A 1 329 ? -48.667 26.788 -44.745 1.00 58.82  ? 330  PHE A CE2 1 
ATOM   2580 C CZ  . PHE A 1 329 ? -49.843 26.670 -45.490 1.00 60.01  ? 330  PHE A CZ  1 
ATOM   2581 N N   . PHE A 1 330 ? -46.951 32.696 -47.330 1.00 27.17  ? 331  PHE A N   1 
ATOM   2582 C CA  . PHE A 1 330 ? -47.600 33.929 -47.684 1.00 27.05  ? 331  PHE A CA  1 
ATOM   2583 C C   . PHE A 1 330 ? -47.143 34.302 -49.070 1.00 27.30  ? 331  PHE A C   1 
ATOM   2584 O O   . PHE A 1 330 ? -47.878 34.918 -49.774 1.00 30.82  ? 331  PHE A O   1 
ATOM   2585 C CB  . PHE A 1 330 ? -47.305 35.017 -46.644 1.00 28.66  ? 331  PHE A CB  1 
ATOM   2586 C CG  . PHE A 1 330 ? -47.768 34.630 -45.274 1.00 28.50  ? 331  PHE A CG  1 
ATOM   2587 C CD1 . PHE A 1 330 ? -46.957 33.839 -44.465 1.00 28.81  ? 331  PHE A CD1 1 
ATOM   2588 C CD2 . PHE A 1 330 ? -49.074 34.849 -44.912 1.00 29.41  ? 331  PHE A CD2 1 
ATOM   2589 C CE1 . PHE A 1 330 ? -47.420 33.365 -43.273 1.00 30.55  ? 331  PHE A CE1 1 
ATOM   2590 C CE2 . PHE A 1 330 ? -49.533 34.400 -43.709 1.00 30.37  ? 331  PHE A CE2 1 
ATOM   2591 C CZ  . PHE A 1 330 ? -48.704 33.664 -42.888 1.00 29.62  ? 331  PHE A CZ  1 
ATOM   2592 N N   . LEU A 1 331 ? -45.923 33.935 -49.445 1.00 25.46  ? 332  LEU A N   1 
ATOM   2593 C CA  . LEU A 1 331 ? -45.427 34.103 -50.790 1.00 27.09  ? 332  LEU A CA  1 
ATOM   2594 C C   . LEU A 1 331 ? -46.154 33.202 -51.818 1.00 28.23  ? 332  LEU A C   1 
ATOM   2595 O O   . LEU A 1 331 ? -46.653 33.687 -52.874 1.00 27.18  ? 332  LEU A O   1 
ATOM   2596 C CB  . LEU A 1 331 ? -43.937 33.867 -50.830 1.00 27.17  ? 332  LEU A CB  1 
ATOM   2597 C CG  . LEU A 1 331 ? -43.139 34.963 -50.163 1.00 25.91  ? 332  LEU A CG  1 
ATOM   2598 C CD1 . LEU A 1 331 ? -41.741 34.530 -49.903 1.00 26.50  ? 332  LEU A CD1 1 
ATOM   2599 C CD2 . LEU A 1 331 ? -43.127 36.164 -51.048 1.00 28.67  ? 332  LEU A CD2 1 
ATOM   2600 N N   . LEU A 1 332 ? -46.287 31.944 -51.455 1.00 25.65  ? 333  LEU A N   1 
ATOM   2601 C CA  . LEU A 1 332 ? -47.056 30.985 -52.244 1.00 28.31  ? 333  LEU A CA  1 
ATOM   2602 C C   . LEU A 1 332 ? -48.418 31.520 -52.556 1.00 31.48  ? 333  LEU A C   1 
ATOM   2603 O O   . LEU A 1 332 ? -48.813 31.580 -53.725 1.00 30.44  ? 333  LEU A O   1 
ATOM   2604 C CB  . LEU A 1 332 ? -47.217 29.678 -51.494 1.00 26.25  ? 333  LEU A CB  1 
ATOM   2605 C CG  . LEU A 1 332 ? -48.150 28.700 -52.166 1.00 30.62  ? 333  LEU A CG  1 
ATOM   2606 C CD1 . LEU A 1 332 ? -47.601 28.321 -53.573 1.00 31.13  ? 333  LEU A CD1 1 
ATOM   2607 C CD2 . LEU A 1 332 ? -48.285 27.450 -51.299 1.00 28.44  ? 333  LEU A CD2 1 
ATOM   2608 N N   . TYR A 1 333 ? -49.129 31.949 -51.514 1.00 30.91  ? 334  TYR A N   1 
ATOM   2609 C CA  . TYR A 1 333 ? -50.481 32.401 -51.722 1.00 29.51  ? 334  TYR A CA  1 
ATOM   2610 C C   . TYR A 1 333 ? -50.586 33.763 -52.370 1.00 29.44  ? 334  TYR A C   1 
ATOM   2611 O O   . TYR A 1 333 ? -51.514 34.007 -53.110 1.00 31.40  ? 334  TYR A O   1 
ATOM   2612 C CB  . TYR A 1 333 ? -51.297 32.408 -50.453 1.00 29.45  ? 334  TYR A CB  1 
ATOM   2613 C CG  . TYR A 1 333 ? -51.857 31.065 -50.122 1.00 28.50  ? 334  TYR A CG  1 
ATOM   2614 C CD1 . TYR A 1 333 ? -51.005 30.008 -49.830 1.00 30.01  ? 334  TYR A CD1 1 
ATOM   2615 C CD2 . TYR A 1 333 ? -53.232 30.838 -50.082 1.00 27.44  ? 334  TYR A CD2 1 
ATOM   2616 C CE1 . TYR A 1 333 ? -51.474 28.746 -49.547 1.00 26.67  ? 334  TYR A CE1 1 
ATOM   2617 C CE2 . TYR A 1 333 ? -53.728 29.562 -49.797 1.00 26.80  ? 334  TYR A CE2 1 
ATOM   2618 C CZ  . TYR A 1 333 ? -52.838 28.513 -49.539 1.00 27.71  ? 334  TYR A CZ  1 
ATOM   2619 O OH  . TYR A 1 333 ? -53.277 27.230 -49.221 1.00 26.59  ? 334  TYR A OH  1 
ATOM   2620 N N   . GLY A 1 334 ? -49.654 34.651 -52.133 1.00 28.41  ? 335  GLY A N   1 
ATOM   2621 C CA  . GLY A 1 334 ? -49.892 36.026 -52.543 1.00 27.55  ? 335  GLY A CA  1 
ATOM   2622 C C   . GLY A 1 334 ? -48.888 36.720 -53.457 1.00 30.65  ? 335  GLY A C   1 
ATOM   2623 O O   . GLY A 1 334 ? -49.095 37.850 -53.764 1.00 33.25  ? 335  GLY A O   1 
ATOM   2624 N N   . ALA A 1 335 ? -47.732 36.125 -53.732 1.00 27.12  ? 336  ALA A N   1 
ATOM   2625 C CA  . ALA A 1 335 ? -46.748 36.821 -54.441 1.00 29.32  ? 336  ALA A CA  1 
ATOM   2626 C C   . ALA A 1 335 ? -46.544 36.169 -55.839 1.00 30.73  ? 336  ALA A C   1 
ATOM   2627 O O   . ALA A 1 335 ? -46.581 34.928 -55.992 1.00 27.57  ? 336  ALA A O   1 
ATOM   2628 C CB  . ALA A 1 335 ? -45.434 36.845 -53.663 1.00 30.94  ? 336  ALA A CB  1 
ATOM   2629 N N   . PRO A 1 336 ? -46.360 37.014 -56.850 1.00 36.32  ? 337  PRO A N   1 
ATOM   2630 C CA  . PRO A 1 336 ? -46.199 36.503 -58.217 1.00 38.75  ? 337  PRO A CA  1 
ATOM   2631 C C   . PRO A 1 336 ? -44.920 35.696 -58.409 1.00 31.36  ? 337  PRO A C   1 
ATOM   2632 O O   . PRO A 1 336 ? -43.858 36.118 -57.985 1.00 30.48  ? 337  PRO A O   1 
ATOM   2633 C CB  . PRO A 1 336 ? -46.189 37.779 -59.066 1.00 40.34  ? 337  PRO A CB  1 
ATOM   2634 C CG  . PRO A 1 336 ? -45.618 38.838 -58.121 1.00 44.79  ? 337  PRO A CG  1 
ATOM   2635 C CD  . PRO A 1 336 ? -46.127 38.481 -56.765 1.00 39.81  ? 337  PRO A CD  1 
ATOM   2636 N N   . GLY A 1 337 ? -45.037 34.541 -59.078 1.00 33.25  ? 338  GLY A N   1 
ATOM   2637 C CA  . GLY A 1 337 ? -43.841 33.735 -59.473 1.00 30.60  ? 338  GLY A CA  1 
ATOM   2638 C C   . GLY A 1 337 ? -43.650 32.470 -58.587 1.00 32.08  ? 338  GLY A C   1 
ATOM   2639 O O   . GLY A 1 337 ? -42.793 31.610 -58.882 1.00 31.06  ? 338  GLY A O   1 
ATOM   2640 N N   . PHE A 1 338 ? -44.474 32.352 -57.540 1.00 26.17  ? 339  PHE A N   1 
ATOM   2641 C CA  . PHE A 1 338 ? -44.397 31.241 -56.590 1.00 27.51  ? 339  PHE A CA  1 
ATOM   2642 C C   . PHE A 1 338 ? -45.610 30.444 -56.850 1.00 26.61  ? 339  PHE A C   1 
ATOM   2643 O O   . PHE A 1 338 ? -46.706 31.011 -56.948 1.00 33.59  ? 339  PHE A O   1 
ATOM   2644 C CB  . PHE A 1 338 ? -44.498 31.713 -55.114 1.00 24.22  ? 339  PHE A CB  1 
ATOM   2645 C CG  . PHE A 1 338 ? -43.392 32.582 -54.684 1.00 22.07  ? 339  PHE A CG  1 
ATOM   2646 C CD1 . PHE A 1 338 ? -43.440 33.939 -54.903 1.00 24.88  ? 339  PHE A CD1 1 
ATOM   2647 C CD2 . PHE A 1 338 ? -42.286 32.061 -54.014 1.00 27.68  ? 339  PHE A CD2 1 
ATOM   2648 C CE1 . PHE A 1 338 ? -42.404 34.771 -54.482 1.00 24.28  ? 339  PHE A CE1 1 
ATOM   2649 C CE2 . PHE A 1 338 ? -41.241 32.903 -53.561 1.00 23.82  ? 339  PHE A CE2 1 
ATOM   2650 C CZ  . PHE A 1 338 ? -41.309 34.234 -53.819 1.00 23.59  ? 339  PHE A CZ  1 
ATOM   2651 N N   . SER A 1 339 ? -45.424 29.144 -56.911 1.00 27.32  ? 340  SER A N   1 
ATOM   2652 C CA  . SER A 1 339 ? -46.495 28.201 -57.164 1.00 28.89  ? 340  SER A CA  1 
ATOM   2653 C C   . SER A 1 339 ? -46.198 26.949 -56.372 1.00 27.00  ? 340  SER A C   1 
ATOM   2654 O O   . SER A 1 339 ? -45.036 26.640 -56.062 1.00 26.90  ? 340  SER A O   1 
ATOM   2655 C CB  . SER A 1 339 ? -46.508 27.792 -58.638 1.00 34.38  ? 340  SER A CB  1 
ATOM   2656 O OG  . SER A 1 339 ? -46.158 28.856 -59.501 1.00 45.01  ? 340  SER A OG  1 
ATOM   2657 N N   . LYS A 1 340 ? -47.249 26.199 -56.120 1.00 26.91  ? 341  LYS A N   1 
ATOM   2658 C CA  . LYS A 1 340 ? -47.130 25.029 -55.368 1.00 29.93  ? 341  LYS A CA  1 
ATOM   2659 C C   . LYS A 1 340 ? -46.334 23.903 -56.005 1.00 32.59  ? 341  LYS A C   1 
ATOM   2660 O O   . LYS A 1 340 ? -45.641 23.099 -55.275 1.00 30.81  ? 341  LYS A O   1 
ATOM   2661 C CB  . LYS A 1 340 ? -48.503 24.498 -55.037 1.00 29.92  ? 341  LYS A CB  1 
ATOM   2662 C CG  . LYS A 1 340 ? -48.421 23.446 -53.923 1.00 31.25  ? 341  LYS A CG  1 
ATOM   2663 C CD  . LYS A 1 340 ? -49.785 23.107 -53.361 1.00 31.79  ? 341  LYS A CD  1 
ATOM   2664 C CE  . LYS A 1 340 ? -50.527 22.108 -54.208 1.00 35.39  ? 341  LYS A CE  1 
ATOM   2665 N NZ  . LYS A 1 340 ? -49.723 20.929 -54.681 1.00 36.17  ? 341  LYS A NZ  1 
ATOM   2666 N N   . ASP A 1 341 ? -46.499 23.754 -57.318 1.00 28.45  ? 342  ASP A N   1 
ATOM   2667 C CA  . ASP A 1 341 ? -45.905 22.602 -58.007 1.00 27.97  ? 342  ASP A CA  1 
ATOM   2668 C C   . ASP A 1 341 ? -44.677 22.965 -58.842 1.00 28.56  ? 342  ASP A C   1 
ATOM   2669 O O   . ASP A 1 341 ? -44.262 22.176 -59.633 1.00 31.07  ? 342  ASP A O   1 
ATOM   2670 C CB  . ASP A 1 341 ? -46.929 21.896 -58.859 1.00 30.15  ? 342  ASP A CB  1 
ATOM   2671 C CG  . ASP A 1 341 ? -48.174 21.511 -58.102 1.00 32.10  ? 342  ASP A CG  1 
ATOM   2672 O OD1 . ASP A 1 341 ? -48.127 21.417 -56.847 1.00 36.02  ? 342  ASP A OD1 1 
ATOM   2673 O OD2 . ASP A 1 341 ? -49.235 21.348 -58.769 1.00 34.24  ? 342  ASP A OD2 1 
ATOM   2674 N N   . SER A 1 342 ? -44.066 24.142 -58.671 1.00 29.38  ? 343  SER A N   1 
ATOM   2675 C CA  . SER A 1 342 ? -42.696 24.361 -59.174 1.00 28.89  ? 343  SER A CA  1 
ATOM   2676 C C   . SER A 1 342 ? -41.801 24.712 -58.044 1.00 31.90  ? 343  SER A C   1 
ATOM   2677 O O   . SER A 1 342 ? -42.269 25.012 -56.968 1.00 33.60  ? 343  SER A O   1 
ATOM   2678 C CB  . SER A 1 342 ? -42.605 25.522 -60.158 1.00 29.41  ? 343  SER A CB  1 
ATOM   2679 O OG  . SER A 1 342 ? -43.154 26.700 -59.678 1.00 38.87  ? 343  SER A OG  1 
ATOM   2680 N N   . GLU A 1 343 ? -40.517 24.739 -58.360 1.00 33.53  ? 344  GLU A N   1 
ATOM   2681 C CA  . GLU A 1 343 ? -39.445 25.175 -57.522 1.00 36.13  ? 344  GLU A CA  1 
ATOM   2682 C C   . GLU A 1 343 ? -39.515 26.689 -57.228 1.00 31.68  ? 344  GLU A C   1 
ATOM   2683 O O   . GLU A 1 343 ? -38.776 27.194 -56.378 1.00 28.35  ? 344  GLU A O   1 
ATOM   2684 C CB  . GLU A 1 343 ? -38.100 24.915 -58.247 1.00 40.90  ? 344  GLU A CB  1 
ATOM   2685 C CG  . GLU A 1 343 ? -37.605 23.465 -58.216 1.00 57.23  ? 344  GLU A CG  1 
ATOM   2686 C CD  . GLU A 1 343 ? -36.103 23.328 -58.570 1.00 63.73  ? 344  GLU A CD  1 
ATOM   2687 O OE1 . GLU A 1 343 ? -35.522 24.148 -59.314 1.00 64.54  ? 344  GLU A OE1 1 
ATOM   2688 O OE2 . GLU A 1 343 ? -35.481 22.383 -58.073 1.00 84.14  ? 344  GLU A OE2 1 
ATOM   2689 N N   . SER A 1 344 ? -40.296 27.420 -58.003 1.00 26.86  ? 345  SER A N   1 
ATOM   2690 C CA  . SER A 1 344 ? -40.524 28.818 -57.749 1.00 29.70  ? 345  SER A CA  1 
ATOM   2691 C C   . SER A 1 344 ? -39.263 29.615 -57.767 1.00 31.23  ? 345  SER A C   1 
ATOM   2692 O O   . SER A 1 344 ? -39.014 30.467 -56.905 1.00 33.62  ? 345  SER A O   1 
ATOM   2693 C CB  . SER A 1 344 ? -41.290 29.031 -56.444 1.00 28.44  ? 345  SER A CB  1 
ATOM   2694 O OG  . SER A 1 344 ? -42.550 28.406 -56.596 1.00 37.07  ? 345  SER A OG  1 
ATOM   2695 N N   . LYS A 1 345 ? -38.481 29.406 -58.795 1.00 32.91  ? 346  LYS A N   1 
ATOM   2696 C CA  . LYS A 1 345 ? -37.336 30.282 -59.003 1.00 37.24  ? 346  LYS A CA  1 
ATOM   2697 C C   . LYS A 1 345 ? -37.817 31.633 -59.478 1.00 35.29  ? 346  LYS A C   1 
ATOM   2698 O O   . LYS A 1 345 ? -38.688 31.743 -60.296 1.00 43.72  ? 346  LYS A O   1 
ATOM   2699 C CB  . LYS A 1 345 ? -36.378 29.653 -59.965 1.00 41.34  ? 346  LYS A CB  1 
ATOM   2700 C CG  . LYS A 1 345 ? -35.734 28.367 -59.451 1.00 45.60  ? 346  LYS A CG  1 
ATOM   2701 C CD  . LYS A 1 345 ? -34.706 27.916 -60.494 1.00 59.76  ? 346  LYS A CD  1 
ATOM   2702 C CE  . LYS A 1 345 ? -34.606 26.397 -60.637 1.00 72.04  ? 346  LYS A CE  1 
ATOM   2703 N NZ  . LYS A 1 345 ? -33.754 25.955 -61.796 1.00 75.80  ? 346  LYS A NZ  1 
ATOM   2704 N N   . ILE A 1 346 ? -37.275 32.683 -58.924 1.00 34.55  ? 347  ILE A N   1 
ATOM   2705 C CA  . ILE A 1 346 ? -37.911 33.967 -58.971 1.00 33.61  ? 347  ILE A CA  1 
ATOM   2706 C C   . ILE A 1 346 ? -37.025 34.932 -59.798 1.00 33.30  ? 347  ILE A C   1 
ATOM   2707 O O   . ILE A 1 346 ? -35.841 35.163 -59.504 1.00 29.86  ? 347  ILE A O   1 
ATOM   2708 C CB  . ILE A 1 346 ? -38.152 34.475 -57.468 1.00 35.19  ? 347  ILE A CB  1 
ATOM   2709 C CG1 . ILE A 1 346 ? -39.351 33.774 -56.824 1.00 36.76  ? 347  ILE A CG1 1 
ATOM   2710 C CG2 . ILE A 1 346 ? -38.434 35.946 -57.370 1.00 35.42  ? 347  ILE A CG2 1 
ATOM   2711 C CD1 . ILE A 1 346 ? -40.557 33.791 -57.730 1.00 38.57  ? 347  ILE A CD1 1 
ATOM   2712 N N   . SER A 1 347 ? -37.628 35.532 -60.807 1.00 40.26  ? 348  SER A N   1 
ATOM   2713 C CA  . SER A 1 347 ? -36.942 36.513 -61.601 1.00 47.86  ? 348  SER A CA  1 
ATOM   2714 C C   . SER A 1 347 ? -36.752 37.744 -60.742 1.00 51.81  ? 348  SER A C   1 
ATOM   2715 O O   . SER A 1 347 ? -37.367 37.891 -59.680 1.00 49.74  ? 348  SER A O   1 
ATOM   2716 C CB  . SER A 1 347 ? -37.781 36.846 -62.809 1.00 45.91  ? 348  SER A CB  1 
ATOM   2717 O OG  . SER A 1 347 ? -38.954 37.480 -62.413 1.00 47.23  ? 348  SER A OG  1 
ATOM   2718 N N   . ARG A 1 348 ? -35.863 38.605 -61.197 1.00 51.61  ? 349  ARG A N   1 
ATOM   2719 C CA  . ARG A 1 348 ? -35.590 39.880 -60.562 1.00 48.03  ? 349  ARG A CA  1 
ATOM   2720 C C   . ARG A 1 348 ? -36.827 40.778 -60.504 1.00 42.59  ? 349  ARG A C   1 
ATOM   2721 O O   . ARG A 1 348 ? -36.978 41.554 -59.597 1.00 51.90  ? 349  ARG A O   1 
ATOM   2722 C CB  . ARG A 1 348 ? -34.504 40.581 -61.378 1.00 56.70  ? 349  ARG A CB  1 
ATOM   2723 C CG  . ARG A 1 348 ? -33.761 41.681 -60.672 1.00 54.57  ? 349  ARG A CG  1 
ATOM   2724 C CD  . ARG A 1 348 ? -32.757 41.056 -59.746 1.00 60.54  ? 349  ARG A CD  1 
ATOM   2725 N NE  . ARG A 1 348 ? -32.711 41.900 -58.578 1.00 65.50  ? 349  ARG A NE  1 
ATOM   2726 C CZ  . ARG A 1 348 ? -32.530 41.502 -57.319 1.00 55.23  ? 349  ARG A CZ  1 
ATOM   2727 N NH1 . ARG A 1 348 ? -32.305 40.246 -56.988 1.00 52.83  ? 349  ARG A NH1 1 
ATOM   2728 N NH2 . ARG A 1 348 ? -32.550 42.426 -56.380 1.00 59.08  ? 349  ARG A NH2 1 
ATOM   2729 N N   . GLU A 1 349 ? -37.728 40.648 -61.457 1.00 45.02  ? 350  GLU A N   1 
ATOM   2730 C CA  . GLU A 1 349 ? -38.885 41.510 -61.555 1.00 48.71  ? 350  GLU A CA  1 
ATOM   2731 C C   . GLU A 1 349 ? -39.896 41.036 -60.507 1.00 50.29  ? 350  GLU A C   1 
ATOM   2732 O O   . GLU A 1 349 ? -40.568 41.841 -59.874 1.00 47.20  ? 350  GLU A O   1 
ATOM   2733 C CB  . GLU A 1 349 ? -39.489 41.504 -63.001 1.00 56.99  ? 350  GLU A CB  1 
ATOM   2734 C CG  . GLU A 1 349 ? -38.495 41.963 -64.117 1.00 73.56  ? 350  GLU A CG  1 
ATOM   2735 C CD  . GLU A 1 349 ? -37.345 40.966 -64.428 1.00 82.11  ? 350  GLU A CD  1 
ATOM   2736 O OE1 . GLU A 1 349 ? -37.630 39.758 -64.664 1.00 80.75  ? 350  GLU A OE1 1 
ATOM   2737 O OE2 . GLU A 1 349 ? -36.145 41.379 -64.436 1.00 84.29  ? 350  GLU A OE2 1 
ATOM   2738 N N   . ASP A 1 350 ? -40.016 39.718 -60.359 1.00 43.58  ? 351  ASP A N   1 
ATOM   2739 C CA  . ASP A 1 350 ? -40.873 39.147 -59.350 1.00 42.71  ? 351  ASP A CA  1 
ATOM   2740 C C   . ASP A 1 350 ? -40.270 39.372 -57.946 1.00 40.22  ? 351  ASP A C   1 
ATOM   2741 O O   . ASP A 1 350 ? -40.980 39.655 -57.005 1.00 39.61  ? 351  ASP A O   1 
ATOM   2742 C CB  . ASP A 1 350 ? -41.134 37.680 -59.676 1.00 45.55  ? 351  ASP A CB  1 
ATOM   2743 C CG  . ASP A 1 350 ? -42.207 37.508 -60.726 1.00 43.71  ? 351  ASP A CG  1 
ATOM   2744 O OD1 . ASP A 1 350 ? -42.834 38.515 -61.094 1.00 46.87  ? 351  ASP A OD1 1 
ATOM   2745 O OD2 . ASP A 1 350 ? -42.488 36.360 -61.148 1.00 46.01  ? 351  ASP A OD2 1 
ATOM   2746 N N   . PHE A 1 351 ? -38.961 39.407 -57.836 1.00 35.75  ? 352  PHE A N   1 
ATOM   2747 C CA  . PHE A 1 351 ? -38.369 39.772 -56.576 1.00 37.23  ? 352  PHE A CA  1 
ATOM   2748 C C   . PHE A 1 351 ? -38.826 41.145 -56.142 1.00 41.67  ? 352  PHE A C   1 
ATOM   2749 O O   . PHE A 1 351 ? -39.311 41.317 -55.038 1.00 42.53  ? 352  PHE A O   1 
ATOM   2750 C CB  . PHE A 1 351 ? -36.877 39.837 -56.698 1.00 36.32  ? 352  PHE A CB  1 
ATOM   2751 C CG  . PHE A 1 351 ? -36.190 40.033 -55.409 1.00 31.06  ? 352  PHE A CG  1 
ATOM   2752 C CD1 . PHE A 1 351 ? -36.034 39.002 -54.553 1.00 30.82  ? 352  PHE A CD1 1 
ATOM   2753 C CD2 . PHE A 1 351 ? -35.685 41.241 -55.075 1.00 31.85  ? 352  PHE A CD2 1 
ATOM   2754 C CE1 . PHE A 1 351 ? -35.417 39.186 -53.345 1.00 28.94  ? 352  PHE A CE1 1 
ATOM   2755 C CE2 . PHE A 1 351 ? -35.034 41.426 -53.895 1.00 30.17  ? 352  PHE A CE2 1 
ATOM   2756 C CZ  . PHE A 1 351 ? -34.927 40.404 -53.016 1.00 26.34  ? 352  PHE A CZ  1 
ATOM   2757 N N   . MET A 1 352 ? -38.676 42.113 -57.034 1.00 41.95  ? 353  MET A N   1 
ATOM   2758 C CA  . MET A 1 352 ? -38.994 43.489 -56.726 1.00 40.22  ? 353  MET A CA  1 
ATOM   2759 C C   . MET A 1 352 ? -40.452 43.594 -56.396 1.00 38.13  ? 353  MET A C   1 
ATOM   2760 O O   . MET A 1 352 ? -40.800 44.328 -55.484 1.00 37.52  ? 353  MET A O   1 
ATOM   2761 C CB  . MET A 1 352 ? -38.615 44.442 -57.876 1.00 42.45  ? 353  MET A CB  1 
ATOM   2762 C CG  . MET A 1 352 ? -37.090 44.697 -57.980 1.00 57.42  ? 353  MET A CG  1 
ATOM   2763 S SD  . MET A 1 352 ? -36.478 45.527 -59.517 1.00 77.13  ? 353  MET A SD  1 
ATOM   2764 C CE  . MET A 1 352 ? -37.916 45.640 -60.627 1.00 62.07  ? 353  MET A CE  1 
ATOM   2765 N N   . SER A 1 353 ? -41.299 42.894 -57.139 1.00 33.49  ? 354  SER A N   1 
ATOM   2766 C CA  . SER A 1 353 ? -42.721 42.924 -56.865 1.00 37.97  ? 354  SER A CA  1 
ATOM   2767 C C   . SER A 1 353 ? -42.987 42.369 -55.451 1.00 39.87  ? 354  SER A C   1 
ATOM   2768 O O   . SER A 1 353 ? -43.842 42.879 -54.765 1.00 35.93  ? 354  SER A O   1 
ATOM   2769 C CB  . SER A 1 353 ? -43.498 42.015 -57.810 1.00 38.92  ? 354  SER A CB  1 
ATOM   2770 O OG  . SER A 1 353 ? -43.638 42.609 -59.052 1.00 48.06  ? 354  SER A OG  1 
ATOM   2771 N N   . GLY A 1 354 ? -42.271 41.299 -55.073 1.00 33.78  ? 355  GLY A N   1 
ATOM   2772 C CA  . GLY A 1 354 ? -42.462 40.656 -53.785 1.00 33.73  ? 355  GLY A CA  1 
ATOM   2773 C C   . GLY A 1 354 ? -42.091 41.581 -52.641 1.00 29.76  ? 355  GLY A C   1 
ATOM   2774 O O   . GLY A 1 354 ? -42.819 41.717 -51.669 1.00 29.99  ? 355  GLY A O   1 
ATOM   2775 N N   . VAL A 1 355 ? -40.979 42.267 -52.801 1.00 28.57  ? 356  VAL A N   1 
ATOM   2776 C CA  . VAL A 1 355 ? -40.535 43.219 -51.810 1.00 30.84  ? 356  VAL A CA  1 
ATOM   2777 C C   . VAL A 1 355 ? -41.602 44.243 -51.517 1.00 32.30  ? 356  VAL A C   1 
ATOM   2778 O O   . VAL A 1 355 ? -41.899 44.524 -50.342 1.00 33.38  ? 356  VAL A O   1 
ATOM   2779 C CB  . VAL A 1 355 ? -39.239 43.901 -52.238 1.00 31.33  ? 356  VAL A CB  1 
ATOM   2780 C CG1 . VAL A 1 355 ? -38.895 45.066 -51.336 1.00 32.43  ? 356  VAL A CG1 1 
ATOM   2781 C CG2 . VAL A 1 355 ? -38.126 42.885 -52.199 1.00 30.84  ? 356  VAL A CG2 1 
ATOM   2782 N N   . LYS A 1 356 ? -42.197 44.783 -52.576 1.00 36.95  ? 357  LYS A N   1 
ATOM   2783 C CA  . LYS A 1 356 ? -43.280 45.747 -52.449 1.00 40.33  ? 357  LYS A CA  1 
ATOM   2784 C C   . LYS A 1 356 ? -44.432 45.172 -51.632 1.00 34.21  ? 357  LYS A C   1 
ATOM   2785 O O   . LYS A 1 356 ? -44.884 45.790 -50.668 1.00 33.21  ? 357  LYS A O   1 
ATOM   2786 C CB  . LYS A 1 356 ? -43.778 46.179 -53.829 1.00 46.30  ? 357  LYS A CB  1 
ATOM   2787 C CG  . LYS A 1 356 ? -43.743 47.681 -54.060 1.00 55.54  ? 357  LYS A CG  1 
ATOM   2788 C CD  . LYS A 1 356 ? -45.026 48.343 -53.586 1.00 67.60  ? 357  LYS A CD  1 
ATOM   2789 C CE  . LYS A 1 356 ? -44.968 49.851 -53.765 1.00 70.30  ? 357  LYS A CE  1 
ATOM   2790 N NZ  . LYS A 1 356 ? -44.709 50.554 -52.478 1.00 70.82  ? 357  LYS A NZ  1 
ATOM   2791 N N   . LEU A 1 357 ? -44.905 43.989 -52.015 1.00 31.22  ? 358  LEU A N   1 
ATOM   2792 C CA  . LEU A 1 357 ? -46.006 43.356 -51.286 1.00 30.48  ? 358  LEU A CA  1 
ATOM   2793 C C   . LEU A 1 357 ? -45.610 43.110 -49.819 1.00 31.72  ? 358  LEU A C   1 
ATOM   2794 O O   . LEU A 1 357 ? -46.436 43.148 -48.946 1.00 31.40  ? 358  LEU A O   1 
ATOM   2795 C CB  . LEU A 1 357 ? -46.406 42.005 -51.919 1.00 30.80  ? 358  LEU A CB  1 
ATOM   2796 C CG  . LEU A 1 357 ? -46.920 42.037 -53.386 1.00 30.33  ? 358  LEU A CG  1 
ATOM   2797 C CD1 . LEU A 1 357 ? -47.020 40.623 -53.984 1.00 28.87  ? 358  LEU A CD1 1 
ATOM   2798 C CD2 . LEU A 1 357 ? -48.271 42.730 -53.423 1.00 30.61  ? 358  LEU A CD2 1 
ATOM   2799 N N   . SER A 1 358 ? -44.342 42.797 -49.580 1.00 31.20  ? 359  SER A N   1 
ATOM   2800 C CA  . SER A 1 358 ? -43.888 42.366 -48.272 1.00 28.70  ? 359  SER A CA  1 
ATOM   2801 C C   . SER A 1 358 ? -43.742 43.493 -47.290 1.00 31.33  ? 359  SER A C   1 
ATOM   2802 O O   . SER A 1 358 ? -43.835 43.261 -46.101 1.00 35.05  ? 359  SER A O   1 
ATOM   2803 C CB  . SER A 1 358 ? -42.545 41.690 -48.389 1.00 29.70  ? 359  SER A CB  1 
ATOM   2804 O OG  . SER A 1 358 ? -42.654 40.443 -49.021 1.00 33.11  ? 359  SER A OG  1 
ATOM   2805 N N   . VAL A 1 359 ? -43.544 44.714 -47.779 1.00 29.16  ? 360  VAL A N   1 
ATOM   2806 C CA  . VAL A 1 359 ? -43.279 45.850 -46.955 1.00 27.12  ? 360  VAL A CA  1 
ATOM   2807 C C   . VAL A 1 359 ? -44.163 46.967 -47.433 1.00 30.02  ? 360  VAL A C   1 
ATOM   2808 O O   . VAL A 1 359 ? -43.686 48.029 -47.897 1.00 30.87  ? 360  VAL A O   1 
ATOM   2809 C CB  . VAL A 1 359 ? -41.813 46.303 -47.058 1.00 30.47  ? 360  VAL A CB  1 
ATOM   2810 C CG1 . VAL A 1 359 ? -41.489 47.257 -45.928 1.00 28.32  ? 360  VAL A CG1 1 
ATOM   2811 C CG2 . VAL A 1 359 ? -40.896 45.093 -47.013 1.00 32.73  ? 360  VAL A CG2 1 
ATOM   2812 N N   . PRO A 1 360 ? -45.462 46.777 -47.265 1.00 32.84  ? 361  PRO A N   1 
ATOM   2813 C CA  . PRO A 1 360 ? -46.432 47.673 -47.860 1.00 36.76  ? 361  PRO A CA  1 
ATOM   2814 C C   . PRO A 1 360 ? -46.318 49.121 -47.385 1.00 39.22  ? 361  PRO A C   1 
ATOM   2815 O O   . PRO A 1 360 ? -46.634 50.060 -48.133 1.00 36.91  ? 361  PRO A O   1 
ATOM   2816 C CB  . PRO A 1 360 ? -47.783 47.050 -47.444 1.00 40.69  ? 361  PRO A CB  1 
ATOM   2817 C CG  . PRO A 1 360 ? -47.519 46.144 -46.314 1.00 39.21  ? 361  PRO A CG  1 
ATOM   2818 C CD  . PRO A 1 360 ? -46.079 45.737 -46.420 1.00 37.52  ? 361  PRO A CD  1 
ATOM   2819 N N   . HIS A 1 361 ? -45.842 49.296 -46.167 1.00 47.91  ? 362  HIS A N   1 
ATOM   2820 C CA  . HIS A 1 361 ? -45.771 50.625 -45.583 1.00 64.90  ? 362  HIS A CA  1 
ATOM   2821 C C   . HIS A 1 361 ? -44.496 51.394 -46.021 1.00 64.31  ? 362  HIS A C   1 
ATOM   2822 O O   . HIS A 1 361 ? -44.167 52.385 -45.380 1.00 55.94  ? 362  HIS A O   1 
ATOM   2823 C CB  . HIS A 1 361 ? -45.827 50.550 -44.021 1.00 73.96  ? 362  HIS A CB  1 
ATOM   2824 C CG  . HIS A 1 361 ? -47.052 49.863 -43.459 1.00 80.98  ? 362  HIS A CG  1 
ATOM   2825 N ND1 . HIS A 1 361 ? -48.157 50.557 -43.002 1.00 78.27  ? 362  HIS A ND1 1 
ATOM   2826 C CD2 . HIS A 1 361 ? -47.317 48.547 -43.225 1.00 91.25  ? 362  HIS A CD2 1 
ATOM   2827 C CE1 . HIS A 1 361 ? -49.050 49.701 -42.527 1.00 84.56  ? 362  HIS A CE1 1 
ATOM   2828 N NE2 . HIS A 1 361 ? -48.578 48.472 -42.675 1.00 83.30  ? 362  HIS A NE2 1 
ATOM   2829 N N   . ALA A 1 362 ? -43.788 50.980 -47.084 1.00 54.45  ? 363  ALA A N   1 
ATOM   2830 C CA  . ALA A 1 362 ? -42.478 51.577 -47.349 1.00 44.09  ? 363  ALA A CA  1 
ATOM   2831 C C   . ALA A 1 362 ? -42.408 52.499 -48.542 1.00 37.99  ? 363  ALA A C   1 
ATOM   2832 O O   . ALA A 1 362 ? -42.760 52.149 -49.632 1.00 42.06  ? 363  ALA A O   1 
ATOM   2833 C CB  . ALA A 1 362 ? -41.419 50.500 -47.509 1.00 42.88  ? 363  ALA A CB  1 
ATOM   2834 N N   . ASN A 1 363 ? -41.824 53.661 -48.350 1.00 37.68  ? 364  ASN A N   1 
ATOM   2835 C CA  . ASN A 1 363 ? -41.405 54.469 -49.488 1.00 38.45  ? 364  ASN A CA  1 
ATOM   2836 C C   . ASN A 1 363 ? -40.259 53.789 -50.295 1.00 37.98  ? 364  ASN A C   1 
ATOM   2837 O O   . ASN A 1 363 ? -39.629 52.811 -49.848 1.00 39.63  ? 364  ASN A O   1 
ATOM   2838 C CB  . ASN A 1 363 ? -41.001 55.857 -48.991 1.00 35.08  ? 364  ASN A CB  1 
ATOM   2839 C CG  . ASN A 1 363 ? -39.698 55.849 -48.200 1.00 37.69  ? 364  ASN A CG  1 
ATOM   2840 O OD1 . ASN A 1 363 ? -38.956 54.875 -48.204 1.00 38.85  ? 364  ASN A OD1 1 
ATOM   2841 N ND2 . ASN A 1 363 ? -39.435 56.924 -47.496 1.00 38.19  ? 364  ASN A ND2 1 
ATOM   2842 N N   . ASP A 1 364 ? -39.986 54.330 -51.467 1.00 39.13  ? 365  ASP A N   1 
ATOM   2843 C CA  . ASP A 1 364 ? -39.027 53.768 -52.403 1.00 42.50  ? 365  ASP A CA  1 
ATOM   2844 C C   . ASP A 1 364 ? -37.621 53.614 -51.833 1.00 35.63  ? 365  ASP A C   1 
ATOM   2845 O O   . ASP A 1 364 ? -36.911 52.662 -52.098 1.00 34.17  ? 365  ASP A O   1 
ATOM   2846 C CB  . ASP A 1 364 ? -38.963 54.649 -53.677 1.00 54.20  ? 365  ASP A CB  1 
ATOM   2847 C CG  . ASP A 1 364 ? -40.150 54.431 -54.623 1.00 60.85  ? 365  ASP A CG  1 
ATOM   2848 O OD1 . ASP A 1 364 ? -41.011 53.563 -54.349 1.00 61.74  ? 365  ASP A OD1 1 
ATOM   2849 O OD2 . ASP A 1 364 ? -40.201 55.117 -55.667 1.00 67.67  ? 365  ASP A OD2 1 
ATOM   2850 N N   . LEU A 1 365 ? -37.204 54.582 -51.024 1.00 33.39  ? 366  LEU A N   1 
ATOM   2851 C CA  . LEU A 1 365 ? -35.899 54.494 -50.374 1.00 33.73  ? 366  LEU A CA  1 
ATOM   2852 C C   . LEU A 1 365 ? -35.880 53.266 -49.469 1.00 30.99  ? 366  LEU A C   1 
ATOM   2853 O O   . LEU A 1 365 ? -34.896 52.529 -49.404 1.00 29.90  ? 366  LEU A O   1 
ATOM   2854 C CB  . LEU A 1 365 ? -35.615 55.757 -49.561 1.00 35.79  ? 366  LEU A CB  1 
ATOM   2855 C CG  . LEU A 1 365 ? -34.160 56.228 -49.525 1.00 42.59  ? 366  LEU A CG  1 
ATOM   2856 C CD1 . LEU A 1 365 ? -33.903 57.084 -48.294 1.00 38.63  ? 366  LEU A CD1 1 
ATOM   2857 C CD2 . LEU A 1 365 ? -33.210 55.041 -49.565 1.00 39.71  ? 366  LEU A CD2 1 
ATOM   2858 N N   . GLY A 1 366 ? -36.995 53.068 -48.778 1.00 31.81  ? 367  GLY A N   1 
ATOM   2859 C CA  . GLY A 1 366 ? -37.236 51.925 -47.919 1.00 28.83  ? 367  GLY A CA  1 
ATOM   2860 C C   . GLY A 1 366 ? -37.137 50.648 -48.703 1.00 28.11  ? 367  GLY A C   1 
ATOM   2861 O O   . GLY A 1 366 ? -36.386 49.755 -48.325 1.00 28.34  ? 367  GLY A O   1 
ATOM   2862 N N   . LEU A 1 367 ? -37.804 50.597 -49.846 1.00 28.17  ? 368  LEU A N   1 
ATOM   2863 C CA  . LEU A 1 367 ? -37.756 49.388 -50.659 1.00 29.12  ? 368  LEU A CA  1 
ATOM   2864 C C   . LEU A 1 367 ? -36.353 49.087 -51.134 1.00 31.02  ? 368  LEU A C   1 
ATOM   2865 O O   . LEU A 1 367 ? -35.924 47.886 -51.174 1.00 30.73  ? 368  LEU A O   1 
ATOM   2866 C CB  . LEU A 1 367 ? -38.682 49.482 -51.850 1.00 29.94  ? 368  LEU A CB  1 
ATOM   2867 C CG  . LEU A 1 367 ? -40.195 49.582 -51.475 1.00 36.45  ? 368  LEU A CG  1 
ATOM   2868 C CD1 . LEU A 1 367 ? -41.023 49.828 -52.732 1.00 32.20  ? 368  LEU A CD1 1 
ATOM   2869 C CD2 . LEU A 1 367 ? -40.713 48.324 -50.707 1.00 34.55  ? 368  LEU A CD2 1 
ATOM   2870 N N   . ASP A 1 368 ? -35.647 50.141 -51.518 1.00 27.49  ? 369  ASP A N   1 
ATOM   2871 C CA  . ASP A 1 368 ? -34.265 49.965 -51.956 1.00 33.68  ? 369  ASP A CA  1 
ATOM   2872 C C   . ASP A 1 368 ? -33.403 49.413 -50.799 1.00 31.74  ? 369  ASP A C   1 
ATOM   2873 O O   . ASP A 1 368 ? -32.542 48.573 -51.037 1.00 33.57  ? 369  ASP A O   1 
ATOM   2874 C CB  . ASP A 1 368 ? -33.611 51.278 -52.427 1.00 34.33  ? 369  ASP A CB  1 
ATOM   2875 C CG  . ASP A 1 368 ? -34.223 51.812 -53.721 1.00 38.14  ? 369  ASP A CG  1 
ATOM   2876 O OD1 . ASP A 1 368 ? -34.896 51.058 -54.423 1.00 37.10  ? 369  ASP A OD1 1 
ATOM   2877 O OD2 . ASP A 1 368 ? -34.029 52.996 -54.028 1.00 42.52  ? 369  ASP A OD2 1 
ATOM   2878 N N   . ALA A 1 369 ? -33.613 49.924 -49.593 1.00 26.84  ? 370  ALA A N   1 
ATOM   2879 C CA  . ALA A 1 369 ? -32.830 49.488 -48.423 1.00 28.89  ? 370  ALA A CA  1 
ATOM   2880 C C   . ALA A 1 369 ? -33.099 48.029 -48.192 1.00 24.37  ? 370  ALA A C   1 
ATOM   2881 O O   . ALA A 1 369 ? -32.184 47.268 -48.045 1.00 23.08  ? 370  ALA A O   1 
ATOM   2882 C CB  . ALA A 1 369 ? -33.154 50.327 -47.180 1.00 30.54  ? 370  ALA A CB  1 
ATOM   2883 N N   . VAL A 1 370 ? -34.322 47.581 -48.356 1.00 23.88  ? 371  VAL A N   1 
ATOM   2884 C CA  . VAL A 1 370 ? -34.584 46.125 -48.182 1.00 24.57  ? 371  VAL A CA  1 
ATOM   2885 C C   . VAL A 1 370 ? -33.857 45.307 -49.239 1.00 25.88  ? 371  VAL A C   1 
ATOM   2886 O O   . VAL A 1 370 ? -33.095 44.330 -48.962 1.00 31.94  ? 371  VAL A O   1 
ATOM   2887 C CB  . VAL A 1 370 ? -36.082 45.823 -48.249 1.00 24.79  ? 371  VAL A CB  1 
ATOM   2888 C CG1 . VAL A 1 370 ? -36.387 44.327 -48.173 1.00 24.75  ? 371  VAL A CG1 1 
ATOM   2889 C CG2 . VAL A 1 370 ? -36.825 46.577 -47.141 1.00 25.86  ? 371  VAL A CG2 1 
ATOM   2890 N N   . THR A 1 371 ? -34.082 45.694 -50.460 1.00 27.60  ? 372  THR A N   1 
ATOM   2891 C CA  . THR A 1 371 ? -33.542 44.995 -51.610 1.00 28.92  ? 372  THR A CA  1 
ATOM   2892 C C   . THR A 1 371 ? -32.042 44.900 -51.524 1.00 25.89  ? 372  THR A C   1 
ATOM   2893 O O   . THR A 1 371 ? -31.450 43.858 -51.687 1.00 25.09  ? 372  THR A O   1 
ATOM   2894 C CB  . THR A 1 371 ? -33.916 45.755 -52.896 1.00 35.06  ? 372  THR A CB  1 
ATOM   2895 O OG1 . THR A 1 371 ? -35.336 45.796 -53.009 1.00 33.16  ? 372  THR A OG1 1 
ATOM   2896 C CG2 . THR A 1 371 ? -33.341 45.077 -54.134 1.00 34.13  ? 372  THR A CG2 1 
ATOM   2897 N N   . LEU A 1 372 ? -31.401 45.976 -51.156 1.00 27.91  ? 373  LEU A N   1 
ATOM   2898 C CA  . LEU A 1 372 ? -29.932 45.906 -50.945 1.00 28.51  ? 373  LEU A CA  1 
ATOM   2899 C C   . LEU A 1 372 ? -29.501 44.946 -49.859 1.00 31.59  ? 373  LEU A C   1 
ATOM   2900 O O   . LEU A 1 372 ? -28.467 44.284 -49.935 1.00 34.51  ? 373  LEU A O   1 
ATOM   2901 C CB  . LEU A 1 372 ? -29.440 47.285 -50.579 1.00 29.69  ? 373  LEU A CB  1 
ATOM   2902 C CG  . LEU A 1 372 ? -27.978 47.321 -50.259 1.00 31.79  ? 373  LEU A CG  1 
ATOM   2903 C CD1 . LEU A 1 372 ? -27.138 46.831 -51.437 1.00 38.68  ? 373  LEU A CD1 1 
ATOM   2904 C CD2 . LEU A 1 372 ? -27.611 48.728 -49.950 1.00 34.62  ? 373  LEU A CD2 1 
ATOM   2905 N N   . GLN A 1 373 ? -30.286 44.910 -48.790 1.00 32.12  ? 374  GLN A N   1 
ATOM   2906 C CA  . GLN A 1 373 ? -29.903 44.168 -47.649 1.00 30.64  ? 374  GLN A CA  1 
ATOM   2907 C C   . GLN A 1 373 ? -30.001 42.703 -47.953 1.00 30.28  ? 374  GLN A C   1 
ATOM   2908 O O   . GLN A 1 373 ? -29.343 41.926 -47.348 1.00 34.08  ? 374  GLN A O   1 
ATOM   2909 C CB  . GLN A 1 373 ? -30.862 44.544 -46.522 1.00 35.69  ? 374  GLN A CB  1 
ATOM   2910 C CG  . GLN A 1 373 ? -30.545 43.923 -45.204 1.00 34.54  ? 374  GLN A CG  1 
ATOM   2911 C CD  . GLN A 1 373 ? -29.331 44.575 -44.598 1.00 37.34  ? 374  GLN A CD  1 
ATOM   2912 O OE1 . GLN A 1 373 ? -28.829 45.613 -45.074 1.00 39.94  ? 374  GLN A OE1 1 
ATOM   2913 N NE2 . GLN A 1 373 ? -28.806 43.932 -43.606 1.00 35.09  ? 374  GLN A NE2 1 
ATOM   2914 N N   . TYR A 1 374 ? -30.863 42.303 -48.869 1.00 31.60  ? 375  TYR A N   1 
ATOM   2915 C CA  . TYR A 1 374 ? -31.130 40.877 -49.105 1.00 28.69  ? 375  TYR A CA  1 
ATOM   2916 C C   . TYR A 1 374 ? -30.686 40.386 -50.517 1.00 32.95  ? 375  TYR A C   1 
ATOM   2917 O O   . TYR A 1 374 ? -30.995 39.298 -50.943 1.00 29.22  ? 375  TYR A O   1 
ATOM   2918 C CB  . TYR A 1 374 ? -32.645 40.632 -48.955 1.00 29.52  ? 375  TYR A CB  1 
ATOM   2919 C CG  . TYR A 1 374 ? -33.097 40.510 -47.499 1.00 29.29  ? 375  TYR A CG  1 
ATOM   2920 C CD1 . TYR A 1 374 ? -33.499 41.645 -46.764 1.00 26.96  ? 375  TYR A CD1 1 
ATOM   2921 C CD2 . TYR A 1 374 ? -33.104 39.259 -46.862 1.00 28.57  ? 375  TYR A CD2 1 
ATOM   2922 C CE1 . TYR A 1 374 ? -33.854 41.545 -45.453 1.00 27.22  ? 375  TYR A CE1 1 
ATOM   2923 C CE2 . TYR A 1 374 ? -33.451 39.149 -45.526 1.00 27.64  ? 375  TYR A CE2 1 
ATOM   2924 C CZ  . TYR A 1 374 ? -33.833 40.286 -44.834 1.00 29.08  ? 375  TYR A CZ  1 
ATOM   2925 O OH  . TYR A 1 374 ? -34.240 40.161 -43.546 1.00 26.52  ? 375  TYR A OH  1 
ATOM   2926 N N   . THR A 1 375 ? -29.969 41.188 -51.266 1.00 36.96  ? 376  THR A N   1 
ATOM   2927 C CA  . THR A 1 375 ? -29.605 40.778 -52.608 1.00 33.63  ? 376  THR A CA  1 
ATOM   2928 C C   . THR A 1 375 ? -28.130 40.534 -52.576 1.00 33.43  ? 376  THR A C   1 
ATOM   2929 O O   . THR A 1 375 ? -27.376 41.417 -52.182 1.00 33.18  ? 376  THR A O   1 
ATOM   2930 C CB  . THR A 1 375 ? -29.822 41.942 -53.597 1.00 33.61  ? 376  THR A CB  1 
ATOM   2931 O OG1 . THR A 1 375 ? -31.217 42.269 -53.634 1.00 32.24  ? 376  THR A OG1 1 
ATOM   2932 C CG2 . THR A 1 375 ? -29.339 41.584 -54.980 1.00 31.22  ? 376  THR A CG2 1 
ATOM   2933 N N   . ASP A 1 376 ? -27.729 39.371 -53.058 1.00 33.56  ? 377  ASP A N   1 
ATOM   2934 C CA  . ASP A 1 376 ? -26.330 39.087 -53.377 1.00 39.21  ? 377  ASP A CA  1 
ATOM   2935 C C   . ASP A 1 376 ? -25.988 39.701 -54.734 1.00 39.76  ? 377  ASP A C   1 
ATOM   2936 O O   . ASP A 1 376 ? -26.411 39.145 -55.752 1.00 38.21  ? 377  ASP A O   1 
ATOM   2937 C CB  . ASP A 1 376 ? -26.125 37.566 -53.453 1.00 39.17  ? 377  ASP A CB  1 
ATOM   2938 C CG  . ASP A 1 376 ? -24.692 37.207 -53.795 1.00 40.67  ? 377  ASP A CG  1 
ATOM   2939 O OD1 . ASP A 1 376 ? -23.936 38.131 -54.158 1.00 35.82  ? 377  ASP A OD1 1 
ATOM   2940 O OD2 . ASP A 1 376 ? -24.339 36.014 -53.695 1.00 36.15  ? 377  ASP A OD2 1 
ATOM   2941 N N   . TRP A 1 377 ? -25.273 40.832 -54.758 1.00 38.71  ? 378  TRP A N   1 
ATOM   2942 C CA  . TRP A 1 377 ? -24.932 41.540 -56.030 1.00 43.73  ? 378  TRP A CA  1 
ATOM   2943 C C   . TRP A 1 377 ? -23.858 40.870 -56.934 1.00 39.54  ? 378  TRP A C   1 
ATOM   2944 O O   . TRP A 1 377 ? -23.625 41.329 -58.021 1.00 42.39  ? 378  TRP A O   1 
ATOM   2945 C CB  . TRP A 1 377 ? -24.588 43.047 -55.790 1.00 45.17  ? 378  TRP A CB  1 
ATOM   2946 C CG  . TRP A 1 377 ? -25.834 43.817 -55.441 1.00 47.07  ? 378  TRP A CG  1 
ATOM   2947 C CD1 . TRP A 1 377 ? -26.137 44.304 -54.246 1.00 47.52  ? 378  TRP A CD1 1 
ATOM   2948 C CD2 . TRP A 1 377 ? -26.982 44.062 -56.285 1.00 47.17  ? 378  TRP A CD2 1 
ATOM   2949 N NE1 . TRP A 1 377 ? -27.388 44.856 -54.259 1.00 51.89  ? 378  TRP A NE1 1 
ATOM   2950 C CE2 . TRP A 1 377 ? -27.925 44.732 -55.506 1.00 47.69  ? 378  TRP A CE2 1 
ATOM   2951 C CE3 . TRP A 1 377 ? -27.300 43.751 -57.614 1.00 62.81  ? 378  TRP A CE3 1 
ATOM   2952 C CZ2 . TRP A 1 377 ? -29.189 45.135 -55.993 1.00 59.19  ? 378  TRP A CZ2 1 
ATOM   2953 C CZ3 . TRP A 1 377 ? -28.559 44.160 -58.125 1.00 68.52  ? 378  TRP A CZ3 1 
ATOM   2954 C CH2 . TRP A 1 377 ? -29.484 44.845 -57.304 1.00 62.22  ? 378  TRP A CH2 1 
ATOM   2955 N N   . MET A 1 378 ? -23.240 39.791 -56.500 1.00 40.95  ? 379  MET A N   1 
ATOM   2956 C CA  . MET A 1 378 ? -22.353 38.997 -57.354 1.00 42.54  ? 379  MET A CA  1 
ATOM   2957 C C   . MET A 1 378 ? -23.183 37.965 -58.130 1.00 48.25  ? 379  MET A C   1 
ATOM   2958 O O   . MET A 1 378 ? -22.659 37.248 -58.983 1.00 44.55  ? 379  MET A O   1 
ATOM   2959 C CB  . MET A 1 378 ? -21.324 38.210 -56.514 1.00 41.74  ? 379  MET A CB  1 
ATOM   2960 C CG  . MET A 1 378 ? -20.374 39.034 -55.640 1.00 52.67  ? 379  MET A CG  1 
ATOM   2961 S SD  . MET A 1 378 ? -19.230 38.035 -54.613 1.00 63.22  ? 379  MET A SD  1 
ATOM   2962 C CE  . MET A 1 378 ? -18.346 37.215 -55.970 1.00 63.68  ? 379  MET A CE  1 
ATOM   2963 N N   . ASP A 1 379 ? -24.451 37.825 -57.778 1.00 45.59  ? 380  ASP A N   1 
ATOM   2964 C CA  . ASP A 1 379 ? -25.281 36.795 -58.384 1.00 40.71  ? 380  ASP A CA  1 
ATOM   2965 C C   . ASP A 1 379 ? -26.725 37.194 -58.205 1.00 40.86  ? 380  ASP A C   1 
ATOM   2966 O O   . ASP A 1 379 ? -27.493 36.526 -57.512 1.00 43.61  ? 380  ASP A O   1 
ATOM   2967 C CB  . ASP A 1 379 ? -25.021 35.438 -57.728 1.00 42.42  ? 380  ASP A CB  1 
ATOM   2968 C CG  . ASP A 1 379 ? -25.499 34.278 -58.579 1.00 46.79  ? 380  ASP A CG  1 
ATOM   2969 O OD1 . ASP A 1 379 ? -25.840 34.506 -59.759 1.00 49.19  ? 380  ASP A OD1 1 
ATOM   2970 O OD2 . ASP A 1 379 ? -25.534 33.139 -58.069 1.00 45.75  ? 380  ASP A OD2 1 
ATOM   2971 N N   . ASP A 1 380 ? -27.084 38.306 -58.829 1.00 46.83  ? 381  ASP A N   1 
ATOM   2972 C CA  . ASP A 1 380 ? -28.413 38.920 -58.598 1.00 52.08  ? 381  ASP A CA  1 
ATOM   2973 C C   . ASP A 1 380 ? -29.544 38.308 -59.455 1.00 57.26  ? 381  ASP A C   1 
ATOM   2974 O O   . ASP A 1 380 ? -30.746 38.638 -59.259 1.00 59.49  ? 381  ASP A O   1 
ATOM   2975 C CB  . ASP A 1 380 ? -28.352 40.470 -58.788 1.00 53.28  ? 381  ASP A CB  1 
ATOM   2976 C CG  . ASP A 1 380 ? -28.043 40.878 -60.228 1.00 54.94  ? 381  ASP A CG  1 
ATOM   2977 O OD1 . ASP A 1 380 ? -26.881 40.708 -60.699 1.00 54.24  ? 381  ASP A OD1 1 
ATOM   2978 O OD2 . ASP A 1 380 ? -28.993 41.340 -60.876 1.00 66.97  ? 381  ASP A OD2 1 
ATOM   2979 N N   . ASN A 1 381 ? -29.164 37.423 -60.383 1.00 55.12  ? 382  ASN A N   1 
ATOM   2980 C CA  . ASN A 1 381 ? -30.135 36.646 -61.174 1.00 56.32  ? 382  ASN A CA  1 
ATOM   2981 C C   . ASN A 1 381 ? -30.289 35.187 -60.808 1.00 48.72  ? 382  ASN A C   1 
ATOM   2982 O O   . ASN A 1 381 ? -30.965 34.434 -61.502 1.00 52.78  ? 382  ASN A O   1 
ATOM   2983 C CB  . ASN A 1 381 ? -29.797 36.745 -62.661 1.00 58.92  ? 382  ASN A CB  1 
ATOM   2984 C CG  . ASN A 1 381 ? -30.380 37.976 -63.259 1.00 54.72  ? 382  ASN A CG  1 
ATOM   2985 O OD1 . ASN A 1 381 ? -31.585 38.217 -63.168 1.00 63.36  ? 382  ASN A OD1 1 
ATOM   2986 N ND2 . ASN A 1 381 ? -29.537 38.806 -63.770 1.00 55.72  ? 382  ASN A ND2 1 
ATOM   2987 N N   . ASN A 1 382 ? -29.677 34.772 -59.719 1.00 41.24  ? 383  ASN A N   1 
ATOM   2988 C CA  . ASN A 1 382 ? -29.949 33.455 -59.225 1.00 41.76  ? 383  ASN A CA  1 
ATOM   2989 C C   . ASN A 1 382 ? -31.403 33.375 -58.661 1.00 41.74  ? 383  ASN A C   1 
ATOM   2990 O O   . ASN A 1 382 ? -31.759 34.030 -57.667 1.00 41.78  ? 383  ASN A O   1 
ATOM   2991 C CB  . ASN A 1 382 ? -28.895 33.161 -58.196 1.00 47.28  ? 383  ASN A CB  1 
ATOM   2992 C CG  . ASN A 1 382 ? -29.039 31.815 -57.646 1.00 45.82  ? 383  ASN A CG  1 
ATOM   2993 O OD1 . ASN A 1 382 ? -30.137 31.311 -57.597 1.00 47.54  ? 383  ASN A OD1 1 
ATOM   2994 N ND2 . ASN A 1 382 ? -27.944 31.217 -57.222 1.00 45.04  ? 383  ASN A ND2 1 
ATOM   2995 N N   . GLY A 1 383 ? -32.244 32.604 -59.335 1.00 36.99  ? 384  GLY A N   1 
ATOM   2996 C CA  . GLY A 1 383 ? -33.666 32.501 -59.042 1.00 36.85  ? 384  GLY A CA  1 
ATOM   2997 C C   . GLY A 1 383 ? -33.970 31.848 -57.706 1.00 36.10  ? 384  GLY A C   1 
ATOM   2998 O O   . GLY A 1 383 ? -35.028 32.096 -57.089 1.00 34.18  ? 384  GLY A O   1 
ATOM   2999 N N   . ILE A 1 384 ? -33.050 31.026 -57.267 1.00 31.17  ? 385  ILE A N   1 
ATOM   3000 C CA  . ILE A 1 384 ? -33.149 30.401 -55.987 1.00 34.47  ? 385  ILE A CA  1 
ATOM   3001 C C   . ILE A 1 384 ? -32.819 31.394 -54.860 1.00 38.91  ? 385  ILE A C   1 
ATOM   3002 O O   . ILE A 1 384 ? -33.514 31.416 -53.849 1.00 34.89  ? 385  ILE A O   1 
ATOM   3003 C CB  . ILE A 1 384 ? -32.235 29.214 -55.932 1.00 35.40  ? 385  ILE A CB  1 
ATOM   3004 C CG1 . ILE A 1 384 ? -32.888 28.075 -56.752 1.00 42.76  ? 385  ILE A CG1 1 
ATOM   3005 C CG2 . ILE A 1 384 ? -31.985 28.752 -54.499 1.00 34.96  ? 385  ILE A CG2 1 
ATOM   3006 C CD1 . ILE A 1 384 ? -31.937 26.911 -57.004 1.00 42.11  ? 385  ILE A CD1 1 
ATOM   3007 N N   . LYS A 1 385 ? -31.806 32.234 -55.075 1.00 37.75  ? 386  LYS A N   1 
ATOM   3008 C CA  . LYS A 1 385 ? -31.381 33.222 -54.106 1.00 40.14  ? 386  LYS A CA  1 
ATOM   3009 C C   . LYS A 1 385 ? -32.432 34.300 -53.929 1.00 39.68  ? 386  LYS A C   1 
ATOM   3010 O O   . LYS A 1 385 ? -32.679 34.727 -52.810 1.00 41.03  ? 386  LYS A O   1 
ATOM   3011 C CB  . LYS A 1 385 ? -30.040 33.844 -54.484 1.00 39.67  ? 386  LYS A CB  1 
ATOM   3012 C CG  . LYS A 1 385 ? -28.863 33.072 -53.906 1.00 43.32  ? 386  LYS A CG  1 
ATOM   3013 C CD  . LYS A 1 385 ? -27.560 33.448 -54.569 1.00 45.75  ? 386  LYS A CD  1 
ATOM   3014 C CE  . LYS A 1 385 ? -26.345 32.701 -53.963 1.00 49.44  ? 386  LYS A CE  1 
ATOM   3015 N NZ  . LYS A 1 385 ? -25.096 33.294 -54.585 1.00 49.83  ? 386  LYS A NZ  1 
ATOM   3016 N N   . ASN A 1 386 ? -33.041 34.701 -55.033 1.00 34.10  ? 387  ASN A N   1 
ATOM   3017 C CA  . ASN A 1 386 ? -34.131 35.580 -55.008 1.00 34.53  ? 387  ASN A CA  1 
ATOM   3018 C C   . ASN A 1 386 ? -35.346 34.967 -54.280 1.00 33.26  ? 387  ASN A C   1 
ATOM   3019 O O   . ASN A 1 386 ? -36.021 35.640 -53.541 1.00 31.04  ? 387  ASN A O   1 
ATOM   3020 C CB  . ASN A 1 386 ? -34.526 35.999 -56.419 1.00 35.68  ? 387  ASN A CB  1 
ATOM   3021 C CG  . ASN A 1 386 ? -33.474 36.874 -57.138 1.00 40.51  ? 387  ASN A CG  1 
ATOM   3022 O OD1 . ASN A 1 386 ? -32.482 37.343 -56.593 1.00 36.74  ? 387  ASN A OD1 1 
ATOM   3023 N ND2 . ASN A 1 386 ? -33.711 37.062 -58.411 1.00 47.50  ? 387  ASN A ND2 1 
ATOM   3024 N N   . ARG A 1 387 ? -35.656 33.716 -54.546 1.00 29.61  ? 388  ARG A N   1 
ATOM   3025 C CA  . ARG A 1 387 ? -36.784 33.058 -53.907 1.00 28.92  ? 388  ARG A CA  1 
ATOM   3026 C C   . ARG A 1 387 ? -36.531 32.992 -52.384 1.00 29.47  ? 388  ARG A C   1 
ATOM   3027 O O   . ARG A 1 387 ? -37.288 33.595 -51.604 1.00 28.04  ? 388  ARG A O   1 
ATOM   3028 C CB  . ARG A 1 387 ? -36.974 31.704 -54.503 1.00 29.11  ? 388  ARG A CB  1 
ATOM   3029 C CG  . ARG A 1 387 ? -38.136 30.862 -54.015 1.00 31.10  ? 388  ARG A CG  1 
ATOM   3030 C CD  . ARG A 1 387 ? -37.579 29.627 -53.325 1.00 33.10  ? 388  ARG A CD  1 
ATOM   3031 N NE  . ARG A 1 387 ? -37.384 28.566 -54.197 1.00 35.16  ? 388  ARG A NE  1 
ATOM   3032 C CZ  . ARG A 1 387 ? -36.424 27.646 -54.115 1.00 33.07  ? 388  ARG A CZ  1 
ATOM   3033 N NH1 . ARG A 1 387 ? -35.465 27.654 -53.210 1.00 29.87  ? 388  ARG A NH1 1 
ATOM   3034 N NH2 . ARG A 1 387 ? -36.433 26.721 -55.040 1.00 34.03  ? 388  ARG A NH2 1 
ATOM   3035 N N   . ASP A 1 388 ? -35.416 32.396 -52.001 1.00 28.48  ? 389  ASP A N   1 
ATOM   3036 C CA  . ASP A 1 388 ? -35.022 32.272 -50.604 1.00 30.96  ? 389  ASP A CA  1 
ATOM   3037 C C   . ASP A 1 388 ? -34.893 33.600 -49.882 1.00 34.08  ? 389  ASP A C   1 
ATOM   3038 O O   . ASP A 1 388 ? -35.333 33.699 -48.691 1.00 31.91  ? 389  ASP A O   1 
ATOM   3039 C CB  . ASP A 1 388 ? -33.760 31.445 -50.452 1.00 29.20  ? 389  ASP A CB  1 
ATOM   3040 C CG  . ASP A 1 388 ? -33.979 30.002 -50.859 1.00 30.96  ? 389  ASP A CG  1 
ATOM   3041 O OD1 . ASP A 1 388 ? -35.150 29.594 -50.996 1.00 28.09  ? 389  ASP A OD1 1 
ATOM   3042 O OD2 . ASP A 1 388 ? -32.989 29.325 -51.095 1.00 33.90  ? 389  ASP A OD2 1 
ATOM   3043 N N   . GLY A 1 389 ? -34.414 34.616 -50.614 1.00 32.43  ? 390  GLY A N   1 
ATOM   3044 C CA  . GLY A 1 389 ? -34.174 35.927 -50.045 1.00 30.83  ? 390  GLY A CA  1 
ATOM   3045 C C   . GLY A 1 389 ? -35.527 36.579 -49.723 1.00 34.11  ? 390  GLY A C   1 
ATOM   3046 O O   . GLY A 1 389 ? -35.717 37.183 -48.673 1.00 32.74  ? 390  GLY A O   1 
ATOM   3047 N N   . LEU A 1 390 ? -36.500 36.391 -50.589 1.00 29.60  ? 391  LEU A N   1 
ATOM   3048 C CA  . LEU A 1 390 ? -37.821 36.925 -50.334 1.00 30.63  ? 391  LEU A CA  1 
ATOM   3049 C C   . LEU A 1 390 ? -38.514 36.130 -49.180 1.00 28.00  ? 391  LEU A C   1 
ATOM   3050 O O   . LEU A 1 390 ? -39.197 36.682 -48.335 1.00 29.48  ? 391  LEU A O   1 
ATOM   3051 C CB  . LEU A 1 390 ? -38.593 36.854 -51.616 1.00 30.47  ? 391  LEU A CB  1 
ATOM   3052 C CG  . LEU A 1 390 ? -39.672 37.801 -52.057 1.00 40.48  ? 391  LEU A CG  1 
ATOM   3053 C CD1 . LEU A 1 390 ? -39.585 39.244 -51.534 1.00 39.83  ? 391  LEU A CD1 1 
ATOM   3054 C CD2 . LEU A 1 390 ? -39.698 37.771 -53.587 1.00 38.49  ? 391  LEU A CD2 1 
ATOM   3055 N N   . ASP A 1 391 ? -38.325 34.842 -49.154 1.00 26.50  ? 392  ASP A N   1 
ATOM   3056 C CA  . ASP A 1 391 ? -38.771 34.041 -48.046 1.00 29.81  ? 392  ASP A CA  1 
ATOM   3057 C C   . ASP A 1 391 ? -38.220 34.600 -46.689 1.00 27.73  ? 392  ASP A C   1 
ATOM   3058 O O   . ASP A 1 391 ? -38.993 34.839 -45.786 1.00 28.54  ? 392  ASP A O   1 
ATOM   3059 C CB  . ASP A 1 391 ? -38.350 32.600 -48.288 1.00 31.35  ? 392  ASP A CB  1 
ATOM   3060 C CG  . ASP A 1 391 ? -39.102 31.618 -47.441 1.00 38.38  ? 392  ASP A CG  1 
ATOM   3061 O OD1 . ASP A 1 391 ? -39.815 32.024 -46.495 1.00 41.45  ? 392  ASP A OD1 1 
ATOM   3062 O OD2 . ASP A 1 391 ? -39.004 30.414 -47.771 1.00 41.88  ? 392  ASP A OD2 1 
ATOM   3063 N N   . ASP A 1 392 ? -36.931 34.890 -46.594 1.00 25.85  ? 393  ASP A N   1 
ATOM   3064 C CA  . ASP A 1 392 ? -36.339 35.547 -45.432 1.00 25.55  ? 393  ASP A CA  1 
ATOM   3065 C C   . ASP A 1 392 ? -36.903 36.937 -45.141 1.00 29.65  ? 393  ASP A C   1 
ATOM   3066 O O   . ASP A 1 392 ? -37.115 37.300 -43.964 1.00 27.80  ? 393  ASP A O   1 
ATOM   3067 C CB  . ASP A 1 392 ? -34.827 35.632 -45.607 1.00 27.72  ? 393  ASP A CB  1 
ATOM   3068 C CG  . ASP A 1 392 ? -34.142 34.260 -45.513 1.00 30.86  ? 393  ASP A CG  1 
ATOM   3069 O OD1 . ASP A 1 392 ? -34.705 33.403 -44.881 1.00 34.10  ? 393  ASP A OD1 1 
ATOM   3070 O OD2 . ASP A 1 392 ? -33.023 34.045 -46.014 1.00 37.31  ? 393  ASP A OD2 1 
ATOM   3071 N N   . ILE A 1 393 ? -37.155 37.733 -46.187 1.00 26.83  ? 394  ILE A N   1 
ATOM   3072 C CA  . ILE A 1 393 ? -37.731 39.047 -45.954 1.00 26.85  ? 394  ILE A CA  1 
ATOM   3073 C C   . ILE A 1 393 ? -39.107 38.922 -45.249 1.00 25.44  ? 394  ILE A C   1 
ATOM   3074 O O   . ILE A 1 393 ? -39.365 39.580 -44.286 1.00 26.48  ? 394  ILE A O   1 
ATOM   3075 C CB  . ILE A 1 393 ? -37.863 39.845 -47.248 1.00 26.87  ? 394  ILE A CB  1 
ATOM   3076 C CG1 . ILE A 1 393 ? -36.468 40.260 -47.789 1.00 32.03  ? 394  ILE A CG1 1 
ATOM   3077 C CG2 . ILE A 1 393 ? -38.812 41.020 -47.142 1.00 23.38  ? 394  ILE A CG2 1 
ATOM   3078 C CD1 . ILE A 1 393 ? -36.529 40.685 -49.270 1.00 32.79  ? 394  ILE A CD1 1 
ATOM   3079 N N   . VAL A 1 394 ? -39.974 38.078 -45.723 1.00 22.78  ? 395  VAL A N   1 
ATOM   3080 C CA  . VAL A 1 394 ? -41.301 38.006 -45.179 1.00 24.15  ? 395  VAL A CA  1 
ATOM   3081 C C   . VAL A 1 394 ? -41.298 37.505 -43.721 1.00 24.84  ? 395  VAL A C   1 
ATOM   3082 O O   . VAL A 1 394 ? -41.945 38.074 -42.857 1.00 22.35  ? 395  VAL A O   1 
ATOM   3083 C CB  . VAL A 1 394 ? -42.159 37.108 -46.082 1.00 26.01  ? 395  VAL A CB  1 
ATOM   3084 C CG1 . VAL A 1 394 ? -43.527 36.900 -45.506 1.00 26.07  ? 395  VAL A CG1 1 
ATOM   3085 C CG2 . VAL A 1 394 ? -42.331 37.743 -47.486 1.00 26.46  ? 395  VAL A CG2 1 
ATOM   3086 N N   . GLY A 1 395 ? -40.482 36.482 -43.464 1.00 26.75  ? 396  GLY A N   1 
ATOM   3087 C CA  . GLY A 1 395 ? -40.314 35.878 -42.170 1.00 24.63  ? 396  GLY A CA  1 
ATOM   3088 C C   . GLY A 1 395 ? -39.607 36.785 -41.191 1.00 25.54  ? 396  GLY A C   1 
ATOM   3089 O O   . GLY A 1 395 ? -40.079 36.958 -40.091 1.00 29.85  ? 396  GLY A O   1 
ATOM   3090 N N   . ASP A 1 396 ? -38.534 37.449 -41.605 1.00 26.60  ? 397  ASP A N   1 
ATOM   3091 C CA  . ASP A 1 396 ? -37.797 38.312 -40.725 1.00 22.49  ? 397  ASP A CA  1 
ATOM   3092 C C   . ASP A 1 396 ? -38.658 39.467 -40.299 1.00 24.50  ? 397  ASP A C   1 
ATOM   3093 O O   . ASP A 1 396 ? -38.752 39.779 -39.129 1.00 25.24  ? 397  ASP A O   1 
ATOM   3094 C CB  . ASP A 1 396 ? -36.588 38.846 -41.391 1.00 26.35  ? 397  ASP A CB  1 
ATOM   3095 C CG  . ASP A 1 396 ? -35.507 37.792 -41.602 1.00 27.98  ? 397  ASP A CG  1 
ATOM   3096 O OD1 . ASP A 1 396 ? -35.640 36.674 -41.053 1.00 24.55  ? 397  ASP A OD1 1 
ATOM   3097 O OD2 . ASP A 1 396 ? -34.531 38.114 -42.313 1.00 23.78  ? 397  ASP A OD2 1 
ATOM   3098 N N   . HIS A 1 397 ? -39.285 40.110 -41.253 1.00 22.77  ? 398  HIS A N   1 
ATOM   3099 C CA  . HIS A 1 397 ? -40.053 41.292 -40.999 1.00 23.72  ? 398  HIS A CA  1 
ATOM   3100 C C   . HIS A 1 397 ? -41.339 41.050 -40.186 1.00 27.65  ? 398  HIS A C   1 
ATOM   3101 O O   . HIS A 1 397 ? -41.705 41.910 -39.389 1.00 29.27  ? 398  HIS A O   1 
ATOM   3102 C CB  . HIS A 1 397 ? -40.461 41.902 -42.321 1.00 22.93  ? 398  HIS A CB  1 
ATOM   3103 C CG  . HIS A 1 397 ? -41.438 43.013 -42.215 1.00 24.16  ? 398  HIS A CG  1 
ATOM   3104 N ND1 . HIS A 1 397 ? -41.222 44.127 -41.441 1.00 25.69  ? 398  HIS A ND1 1 
ATOM   3105 C CD2 . HIS A 1 397 ? -42.572 43.258 -42.891 1.00 29.74  ? 398  HIS A CD2 1 
ATOM   3106 C CE1 . HIS A 1 397 ? -42.207 44.979 -41.578 1.00 25.03  ? 398  HIS A CE1 1 
ATOM   3107 N NE2 . HIS A 1 397 ? -43.041 44.479 -42.466 1.00 31.46  ? 398  HIS A NE2 1 
ATOM   3108 N N   . ASN A 1 398 ? -42.005 39.918 -40.425 1.00 25.29  ? 399  ASN A N   1 
ATOM   3109 C CA  . ASN A 1 398 ? -43.264 39.637 -39.850 1.00 24.83  ? 399  ASN A CA  1 
ATOM   3110 C C   . ASN A 1 398 ? -43.285 38.777 -38.580 1.00 25.81  ? 399  ASN A C   1 
ATOM   3111 O O   . ASN A 1 398 ? -44.244 38.859 -37.823 1.00 26.70  ? 399  ASN A O   1 
ATOM   3112 C CB  . ASN A 1 398 ? -44.149 38.969 -40.858 1.00 24.60  ? 399  ASN A CB  1 
ATOM   3113 C CG  . ASN A 1 398 ? -44.679 39.955 -41.907 1.00 25.59  ? 399  ASN A CG  1 
ATOM   3114 O OD1 . ASN A 1 398 ? -45.476 40.834 -41.589 1.00 25.93  ? 399  ASN A OD1 1 
ATOM   3115 N ND2 . ASN A 1 398 ? -44.275 39.774 -43.163 1.00 22.30  ? 399  ASN A ND2 1 
ATOM   3116 N N   . VAL A 1 399 ? -42.282 37.951 -38.386 1.00 23.00  ? 400  VAL A N   1 
ATOM   3117 C CA  . VAL A 1 399 ? -42.294 36.990 -37.342 1.00 22.42  ? 400  VAL A CA  1 
ATOM   3118 C C   . VAL A 1 399 ? -40.996 37.045 -36.508 1.00 23.51  ? 400  VAL A C   1 
ATOM   3119 O O   . VAL A 1 399 ? -40.986 37.446 -35.341 1.00 25.24  ? 400  VAL A O   1 
ATOM   3120 C CB  . VAL A 1 399 ? -42.501 35.596 -37.884 1.00 22.82  ? 400  VAL A CB  1 
ATOM   3121 C CG1 . VAL A 1 399 ? -42.511 34.615 -36.736 1.00 24.52  ? 400  VAL A CG1 1 
ATOM   3122 C CG2 . VAL A 1 399 ? -43.846 35.491 -38.641 1.00 24.84  ? 400  VAL A CG2 1 
ATOM   3123 N N   . ILE A 1 400 ? -39.876 36.857 -37.140 1.00 25.71  ? 401  ILE A N   1 
ATOM   3124 C CA  . ILE A 1 400 ? -38.646 36.694 -36.394 1.00 27.01  ? 401  ILE A CA  1 
ATOM   3125 C C   . ILE A 1 400 ? -38.155 37.938 -35.737 1.00 27.22  ? 401  ILE A C   1 
ATOM   3126 O O   . ILE A 1 400 ? -37.854 37.929 -34.538 1.00 27.61  ? 401  ILE A O   1 
ATOM   3127 C CB  . ILE A 1 400 ? -37.566 36.067 -37.236 1.00 26.22  ? 401  ILE A CB  1 
ATOM   3128 C CG1 . ILE A 1 400 ? -38.063 34.680 -37.752 1.00 28.10  ? 401  ILE A CG1 1 
ATOM   3129 C CG2 . ILE A 1 400 ? -36.312 35.913 -36.404 1.00 26.20  ? 401  ILE A CG2 1 
ATOM   3130 C CD1 . ILE A 1 400 ? -36.968 33.922 -38.546 1.00 29.66  ? 401  ILE A CD1 1 
ATOM   3131 N N   . CYS A 1 401 ? -38.085 39.032 -36.473 1.00 26.22  ? 402  CYS A N   1 
ATOM   3132 C CA  . CYS A 1 401 ? -37.523 40.247 -35.872 1.00 23.46  ? 402  CYS A CA  1 
ATOM   3133 C C   . CYS A 1 401 ? -38.513 40.919 -34.895 1.00 24.78  ? 402  CYS A C   1 
ATOM   3134 O O   . CYS A 1 401 ? -38.111 41.448 -33.904 1.00 23.03  ? 402  CYS A O   1 
ATOM   3135 C CB  . CYS A 1 401 ? -37.032 41.220 -36.955 1.00 24.17  ? 402  CYS A CB  1 
ATOM   3136 S SG  . CYS A 1 401 ? -35.654 40.455 -37.860 1.00 28.98  ? 402  CYS A SG  1 
ATOM   3137 N N   . PRO A 1 402 ? -39.812 40.939 -35.187 1.00 24.91  ? 403  PRO A N   1 
ATOM   3138 C CA  . PRO A 1 402 ? -40.690 41.386 -34.094 1.00 25.11  ? 403  PRO A CA  1 
ATOM   3139 C C   . PRO A 1 402 ? -40.506 40.512 -32.836 1.00 28.06  ? 403  PRO A C   1 
ATOM   3140 O O   . PRO A 1 402 ? -40.443 41.022 -31.713 1.00 25.99  ? 403  PRO A O   1 
ATOM   3141 C CB  . PRO A 1 402 ? -42.089 41.142 -34.664 1.00 25.02  ? 403  PRO A CB  1 
ATOM   3142 C CG  . PRO A 1 402 ? -41.898 41.396 -36.142 1.00 26.69  ? 403  PRO A CG  1 
ATOM   3143 C CD  . PRO A 1 402 ? -40.550 40.711 -36.435 1.00 24.67  ? 403  PRO A CD  1 
ATOM   3144 N N   . LEU A 1 403 ? -40.392 39.210 -33.016 1.00 25.86  ? 404  LEU A N   1 
ATOM   3145 C CA  . LEU A 1 403 ? -40.292 38.370 -31.866 1.00 27.09  ? 404  LEU A CA  1 
ATOM   3146 C C   . LEU A 1 403 ? -38.962 38.657 -31.127 1.00 31.11  ? 404  LEU A C   1 
ATOM   3147 O O   . LEU A 1 403 ? -38.930 38.629 -29.857 1.00 28.22  ? 404  LEU A O   1 
ATOM   3148 C CB  . LEU A 1 403 ? -40.412 36.895 -32.225 1.00 24.59  ? 404  LEU A CB  1 
ATOM   3149 C CG  . LEU A 1 403 ? -40.195 35.902 -31.047 1.00 28.11  ? 404  LEU A CG  1 
ATOM   3150 C CD1 . LEU A 1 403 ? -41.161 34.744 -31.100 1.00 29.16  ? 404  LEU A CD1 1 
ATOM   3151 C CD2 . LEU A 1 403 ? -38.777 35.359 -30.952 1.00 26.92  ? 404  LEU A CD2 1 
ATOM   3152 N N   . MET A 1 404 ? -37.885 38.884 -31.900 1.00 26.70  ? 405  MET A N   1 
ATOM   3153 C CA  . MET A 1 404 ? -36.622 39.085 -31.267 1.00 27.27  ? 405  MET A CA  1 
ATOM   3154 C C   . MET A 1 404 ? -36.692 40.410 -30.495 1.00 27.43  ? 405  MET A C   1 
ATOM   3155 O O   . MET A 1 404 ? -35.988 40.577 -29.503 1.00 20.29  ? 405  MET A O   1 
ATOM   3156 C CB  . MET A 1 404 ? -35.442 39.082 -32.230 1.00 27.48  ? 405  MET A CB  1 
ATOM   3157 C CG  . MET A 1 404 ? -35.114 37.724 -32.766 1.00 28.25  ? 405  MET A CG  1 
ATOM   3158 S SD  . MET A 1 404 ? -34.906 36.463 -31.455 1.00 30.57  ? 405  MET A SD  1 
ATOM   3159 C CE  . MET A 1 404 ? -33.537 37.308 -30.608 1.00 24.52  ? 405  MET A CE  1 
ATOM   3160 N N   . HIS A 1 405 ? -37.518 41.352 -30.959 1.00 27.05  ? 406  HIS A N   1 
ATOM   3161 C CA  . HIS A 1 405 ? -37.633 42.659 -30.281 1.00 28.20  ? 406  HIS A CA  1 
ATOM   3162 C C   . HIS A 1 405 ? -38.434 42.504 -28.973 1.00 28.84  ? 406  HIS A C   1 
ATOM   3163 O O   . HIS A 1 405 ? -38.103 43.107 -27.945 1.00 30.87  ? 406  HIS A O   1 
ATOM   3164 C CB  . HIS A 1 405 ? -38.330 43.660 -31.149 1.00 26.50  ? 406  HIS A CB  1 
ATOM   3165 C CG  . HIS A 1 405 ? -38.546 44.991 -30.506 1.00 27.72  ? 406  HIS A CG  1 
ATOM   3166 N ND1 . HIS A 1 405 ? -37.516 45.886 -30.295 1.00 28.79  ? 406  HIS A ND1 1 
ATOM   3167 C CD2 . HIS A 1 405 ? -39.680 45.638 -30.156 1.00 29.00  ? 406  HIS A CD2 1 
ATOM   3168 C CE1 . HIS A 1 405 ? -37.997 46.997 -29.770 1.00 27.04  ? 406  HIS A CE1 1 
ATOM   3169 N NE2 . HIS A 1 405 ? -39.310 46.892 -29.711 1.00 31.16  ? 406  HIS A NE2 1 
ATOM   3170 N N   . PHE A 1 406 ? -39.489 41.730 -29.048 1.00 27.43  ? 407  PHE A N   1 
ATOM   3171 C CA  . PHE A 1 406 ? -40.277 41.371 -27.900 1.00 29.34  ? 407  PHE A CA  1 
ATOM   3172 C C   . PHE A 1 406 ? -39.389 40.681 -26.853 1.00 32.14  ? 407  PHE A C   1 
ATOM   3173 O O   . PHE A 1 406 ? -39.471 41.014 -25.684 1.00 29.86  ? 407  PHE A O   1 
ATOM   3174 C CB  . PHE A 1 406 ? -41.426 40.433 -28.277 1.00 29.65  ? 407  PHE A CB  1 
ATOM   3175 C CG  . PHE A 1 406 ? -42.201 39.951 -27.095 1.00 27.89  ? 407  PHE A CG  1 
ATOM   3176 C CD1 . PHE A 1 406 ? -43.061 40.805 -26.434 1.00 29.15  ? 407  PHE A CD1 1 
ATOM   3177 C CD2 . PHE A 1 406 ? -42.061 38.683 -26.645 1.00 27.96  ? 407  PHE A CD2 1 
ATOM   3178 C CE1 . PHE A 1 406 ? -43.776 40.392 -25.344 1.00 29.23  ? 407  PHE A CE1 1 
ATOM   3179 C CE2 . PHE A 1 406 ? -42.755 38.263 -25.506 1.00 33.39  ? 407  PHE A CE2 1 
ATOM   3180 C CZ  . PHE A 1 406 ? -43.587 39.134 -24.844 1.00 30.18  ? 407  PHE A CZ  1 
ATOM   3181 N N   . VAL A 1 407 ? -38.551 39.749 -27.281 1.00 29.47  ? 408  VAL A N   1 
ATOM   3182 C CA  . VAL A 1 407 ? -37.744 38.972 -26.350 1.00 34.45  ? 408  VAL A CA  1 
ATOM   3183 C C   . VAL A 1 407 ? -36.770 39.848 -25.615 1.00 34.05  ? 408  VAL A C   1 
ATOM   3184 O O   . VAL A 1 407 ? -36.510 39.662 -24.439 1.00 36.03  ? 408  VAL A O   1 
ATOM   3185 C CB  . VAL A 1 407 ? -36.938 37.884 -27.079 1.00 39.19  ? 408  VAL A CB  1 
ATOM   3186 C CG1 . VAL A 1 407 ? -35.876 37.299 -26.219 1.00 49.14  ? 408  VAL A CG1 1 
ATOM   3187 C CG2 . VAL A 1 407 ? -37.850 36.775 -27.430 1.00 46.58  ? 408  VAL A CG2 1 
ATOM   3188 N N   . ASN A 1 408 ? -36.189 40.780 -26.330 1.00 37.50  ? 409  ASN A N   1 
ATOM   3189 C CA  . ASN A 1 408 ? -35.130 41.568 -25.770 1.00 36.76  ? 409  ASN A CA  1 
ATOM   3190 C C   . ASN A 1 408 ? -35.717 42.546 -24.751 1.00 33.88  ? 409  ASN A C   1 
ATOM   3191 O O   . ASN A 1 408 ? -35.160 42.721 -23.678 1.00 33.78  ? 409  ASN A O   1 
ATOM   3192 C CB  . ASN A 1 408 ? -34.241 42.168 -26.884 1.00 35.68  ? 409  ASN A CB  1 
ATOM   3193 C CG  . ASN A 1 408 ? -33.066 41.215 -27.243 1.00 38.82  ? 409  ASN A CG  1 
ATOM   3194 O OD1 . ASN A 1 408 ? -32.151 40.980 -26.414 1.00 47.63  ? 409  ASN A OD1 1 
ATOM   3195 N ND2 . ASN A 1 408 ? -33.124 40.598 -28.408 1.00 35.75  ? 409  ASN A ND2 1 
ATOM   3196 N N   . LYS A 1 409 ? -36.878 43.093 -25.053 1.00 27.02  ? 410  LYS A N   1 
ATOM   3197 C CA  . LYS A 1 409 ? -37.563 43.960 -24.129 1.00 30.84  ? 410  LYS A CA  1 
ATOM   3198 C C   . LYS A 1 409 ? -38.131 43.217 -22.900 1.00 30.12  ? 410  LYS A C   1 
ATOM   3199 O O   . LYS A 1 409 ? -38.126 43.776 -21.816 1.00 29.73  ? 410  LYS A O   1 
ATOM   3200 C CB  . LYS A 1 409 ? -38.764 44.589 -24.798 1.00 32.67  ? 410  LYS A CB  1 
ATOM   3201 C CG  . LYS A 1 409 ? -38.437 45.527 -25.928 1.00 37.13  ? 410  LYS A CG  1 
ATOM   3202 C CD  . LYS A 1 409 ? -37.394 46.529 -25.539 1.00 39.33  ? 410  LYS A CD  1 
ATOM   3203 C CE  . LYS A 1 409 ? -37.450 47.737 -26.449 1.00 38.83  ? 410  LYS A CE  1 
ATOM   3204 N NZ  . LYS A 1 409 ? -36.772 48.816 -25.713 1.00 42.02  ? 410  LYS A NZ  1 
ATOM   3205 N N   . TYR A 1 410 ? -38.668 42.014 -23.104 1.00 27.80  ? 411  TYR A N   1 
ATOM   3206 C CA  . TYR A 1 410 ? -39.352 41.279 -22.068 1.00 30.71  ? 411  TYR A CA  1 
ATOM   3207 C C   . TYR A 1 410 ? -38.293 40.849 -21.061 1.00 32.86  ? 411  TYR A C   1 
ATOM   3208 O O   . TYR A 1 410 ? -38.500 40.944 -19.857 1.00 33.05  ? 411  TYR A O   1 
ATOM   3209 C CB  . TYR A 1 410 ? -40.101 40.020 -22.572 1.00 29.56  ? 411  TYR A CB  1 
ATOM   3210 C CG  . TYR A 1 410 ? -40.890 39.367 -21.455 1.00 23.15  ? 411  TYR A CG  1 
ATOM   3211 C CD1 . TYR A 1 410 ? -42.129 39.814 -21.148 1.00 23.90  ? 411  TYR A CD1 1 
ATOM   3212 C CD2 . TYR A 1 410 ? -40.350 38.310 -20.696 1.00 20.98  ? 411  TYR A CD2 1 
ATOM   3213 C CE1 . TYR A 1 410 ? -42.868 39.279 -20.125 1.00 24.33  ? 411  TYR A CE1 1 
ATOM   3214 C CE2 . TYR A 1 410 ? -41.042 37.771 -19.636 1.00 20.57  ? 411  TYR A CE2 1 
ATOM   3215 C CZ  . TYR A 1 410 ? -42.298 38.291 -19.331 1.00 25.30  ? 411  TYR A CZ  1 
ATOM   3216 O OH  . TYR A 1 410 ? -43.088 37.767 -18.361 1.00 24.66  ? 411  TYR A OH  1 
ATOM   3217 N N   . THR A 1 411 ? -37.177 40.389 -21.582 1.00 31.78  ? 412  THR A N   1 
ATOM   3218 C CA  . THR A 1 411 ? -36.131 39.798 -20.776 1.00 30.60  ? 412  THR A CA  1 
ATOM   3219 C C   . THR A 1 411 ? -35.521 40.787 -19.795 1.00 33.28  ? 412  THR A C   1 
ATOM   3220 O O   . THR A 1 411 ? -35.042 40.366 -18.796 1.00 33.32  ? 412  THR A O   1 
ATOM   3221 C CB  . THR A 1 411 ? -35.091 39.099 -21.677 1.00 27.22  ? 412  THR A CB  1 
ATOM   3222 O OG1 . THR A 1 411 ? -35.681 37.905 -22.240 1.00 32.71  ? 412  THR A OG1 1 
ATOM   3223 C CG2 . THR A 1 411 ? -33.873 38.657 -20.948 1.00 26.62  ? 412  THR A CG2 1 
ATOM   3224 N N   . LYS A 1 412 ? -35.595 42.086 -20.048 1.00 34.01  ? 413  LYS A N   1 
ATOM   3225 C CA  . LYS A 1 412 ? -35.140 43.027 -19.066 1.00 40.11  ? 413  LYS A CA  1 
ATOM   3226 C C   . LYS A 1 412 ? -35.920 42.946 -17.753 1.00 42.77  ? 413  LYS A C   1 
ATOM   3227 O O   . LYS A 1 412 ? -35.311 43.186 -16.740 1.00 38.76  ? 413  LYS A O   1 
ATOM   3228 C CB  . LYS A 1 412 ? -35.216 44.484 -19.554 1.00 45.78  ? 413  LYS A CB  1 
ATOM   3229 C CG  . LYS A 1 412 ? -34.139 44.816 -20.577 1.00 62.15  ? 413  LYS A CG  1 
ATOM   3230 C CD  . LYS A 1 412 ? -34.294 46.232 -21.125 1.00 69.05  ? 413  LYS A CD  1 
ATOM   3231 C CE  . LYS A 1 412 ? -33.863 46.314 -22.589 1.00 73.80  ? 413  LYS A CE  1 
ATOM   3232 N NZ  . LYS A 1 412 ? -34.266 47.621 -23.206 1.00 74.55  ? 413  LYS A NZ  1 
ATOM   3233 N N   . PHE A 1 413 ? -37.249 42.714 -17.783 1.00 34.66  ? 414  PHE A N   1 
ATOM   3234 C CA  . PHE A 1 413 ? -38.093 42.729 -16.592 1.00 31.23  ? 414  PHE A CA  1 
ATOM   3235 C C   . PHE A 1 413 ? -38.625 41.362 -16.148 1.00 30.66  ? 414  PHE A C   1 
ATOM   3236 O O   . PHE A 1 413 ? -39.117 41.234 -15.043 1.00 32.80  ? 414  PHE A O   1 
ATOM   3237 C CB  . PHE A 1 413 ? -39.306 43.602 -16.815 1.00 32.47  ? 414  PHE A CB  1 
ATOM   3238 C CG  . PHE A 1 413 ? -38.981 45.032 -16.992 1.00 35.75  ? 414  PHE A CG  1 
ATOM   3239 C CD1 . PHE A 1 413 ? -38.865 45.873 -15.893 1.00 38.70  ? 414  PHE A CD1 1 
ATOM   3240 C CD2 . PHE A 1 413 ? -38.746 45.539 -18.244 1.00 34.74  ? 414  PHE A CD2 1 
ATOM   3241 C CE1 . PHE A 1 413 ? -38.570 47.200 -16.073 1.00 38.03  ? 414  PHE A CE1 1 
ATOM   3242 C CE2 . PHE A 1 413 ? -38.458 46.861 -18.442 1.00 36.03  ? 414  PHE A CE2 1 
ATOM   3243 C CZ  . PHE A 1 413 ? -38.358 47.689 -17.364 1.00 42.27  ? 414  PHE A CZ  1 
ATOM   3244 N N   . GLY A 1 414 ? -38.477 40.343 -16.976 1.00 30.26  ? 415  GLY A N   1 
ATOM   3245 C CA  . GLY A 1 414 ? -39.128 39.065 -16.754 1.00 28.43  ? 415  GLY A CA  1 
ATOM   3246 C C   . GLY A 1 414 ? -38.277 38.187 -15.875 1.00 27.27  ? 415  GLY A C   1 
ATOM   3247 O O   . GLY A 1 414 ? -37.182 38.570 -15.435 1.00 27.84  ? 415  GLY A O   1 
ATOM   3248 N N   . ASN A 1 415 ? -38.794 37.013 -15.631 1.00 28.15  ? 416  ASN A N   1 
ATOM   3249 C CA  . ASN A 1 415 ? -38.219 36.091 -14.699 1.00 35.21  ? 416  ASN A CA  1 
ATOM   3250 C C   . ASN A 1 415 ? -37.656 34.813 -15.309 1.00 36.00  ? 416  ASN A C   1 
ATOM   3251 O O   . ASN A 1 415 ? -37.427 33.841 -14.592 1.00 34.35  ? 416  ASN A O   1 
ATOM   3252 C CB  . ASN A 1 415 ? -39.277 35.765 -13.613 1.00 41.47  ? 416  ASN A CB  1 
ATOM   3253 C CG  . ASN A 1 415 ? -38.708 34.951 -12.447 1.00 41.59  ? 416  ASN A CG  1 
ATOM   3254 O OD1 . ASN A 1 415 ? -39.233 33.854 -12.157 1.00 41.67  ? 416  ASN A OD1 1 
ATOM   3255 N ND2 . ASN A 1 415 ? -37.618 35.440 -11.807 1.00 39.43  ? 416  ASN A ND2 1 
ATOM   3256 N N   . GLY A 1 416 ? -37.359 34.847 -16.612 1.00 38.79  ? 417  GLY A N   1 
ATOM   3257 C CA  . GLY A 1 416 ? -36.714 33.732 -17.294 1.00 35.93  ? 417  GLY A CA  1 
ATOM   3258 C C   . GLY A 1 416 ? -37.279 33.501 -18.683 1.00 36.49  ? 417  GLY A C   1 
ATOM   3259 O O   . GLY A 1 416 ? -38.483 33.355 -18.843 1.00 28.80  ? 417  GLY A O   1 
ATOM   3260 N N   . THR A 1 417 ? -36.378 33.437 -19.665 1.00 34.67  ? 418  THR A N   1 
ATOM   3261 C CA  . THR A 1 417 ? -36.720 33.401 -21.056 1.00 33.77  ? 418  THR A CA  1 
ATOM   3262 C C   . THR A 1 417 ? -36.004 32.231 -21.649 1.00 31.74  ? 418  THR A C   1 
ATOM   3263 O O   . THR A 1 417 ? -34.792 32.081 -21.395 1.00 28.83  ? 418  THR A O   1 
ATOM   3264 C CB  . THR A 1 417 ? -36.292 34.725 -21.771 1.00 37.59  ? 418  THR A CB  1 
ATOM   3265 O OG1 . THR A 1 417 ? -36.998 35.856 -21.195 1.00 29.23  ? 418  THR A OG1 1 
ATOM   3266 C CG2 . THR A 1 417 ? -36.594 34.635 -23.297 1.00 34.48  ? 418  THR A CG2 1 
ATOM   3267 N N   . TYR A 1 418 ? -36.752 31.349 -22.351 1.00 28.70  ? 419  TYR A N   1 
ATOM   3268 C CA  . TYR A 1 418 ? -36.140 30.249 -23.114 1.00 29.72  ? 419  TYR A CA  1 
ATOM   3269 C C   . TYR A 1 418 ? -36.469 30.381 -24.614 1.00 32.37  ? 419  TYR A C   1 
ATOM   3270 O O   . TYR A 1 418 ? -37.639 30.402 -24.966 1.00 29.33  ? 419  TYR A O   1 
ATOM   3271 C CB  . TYR A 1 418 ? -36.548 28.866 -22.580 1.00 33.02  ? 419  TYR A CB  1 
ATOM   3272 C CG  . TYR A 1 418 ? -36.078 28.625 -21.172 1.00 35.95  ? 419  TYR A CG  1 
ATOM   3273 C CD1 . TYR A 1 418 ? -36.844 29.051 -20.095 1.00 34.57  ? 419  TYR A CD1 1 
ATOM   3274 C CD2 . TYR A 1 418 ? -34.856 28.057 -20.920 1.00 37.95  ? 419  TYR A CD2 1 
ATOM   3275 C CE1 . TYR A 1 418 ? -36.418 28.890 -18.808 1.00 38.35  ? 419  TYR A CE1 1 
ATOM   3276 C CE2 . TYR A 1 418 ? -34.408 27.911 -19.620 1.00 38.91  ? 419  TYR A CE2 1 
ATOM   3277 C CZ  . TYR A 1 418 ? -35.218 28.309 -18.568 1.00 36.48  ? 419  TYR A CZ  1 
ATOM   3278 O OH  . TYR A 1 418 ? -34.815 28.190 -17.270 1.00 31.37  ? 419  TYR A OH  1 
ATOM   3279 N N   . LEU A 1 419 ? -35.442 30.499 -25.468 1.00 31.26  ? 420  LEU A N   1 
ATOM   3280 C CA  . LEU A 1 419 ? -35.621 30.782 -26.897 1.00 28.01  ? 420  LEU A CA  1 
ATOM   3281 C C   . LEU A 1 419 ? -35.207 29.614 -27.803 1.00 29.71  ? 420  LEU A C   1 
ATOM   3282 O O   . LEU A 1 419 ? -34.116 29.029 -27.661 1.00 26.33  ? 420  LEU A O   1 
ATOM   3283 C CB  . LEU A 1 419 ? -34.844 32.038 -27.306 1.00 28.39  ? 420  LEU A CB  1 
ATOM   3284 C CG  . LEU A 1 419 ? -34.941 32.535 -28.777 1.00 29.46  ? 420  LEU A CG  1 
ATOM   3285 C CD1 . LEU A 1 419 ? -36.397 32.813 -29.181 1.00 28.63  ? 420  LEU A CD1 1 
ATOM   3286 C CD2 . LEU A 1 419 ? -34.073 33.779 -29.018 1.00 27.91  ? 420  LEU A CD2 1 
ATOM   3287 N N   . TYR A 1 420 ? -36.084 29.275 -28.743 1.00 26.26  ? 421  TYR A N   1 
ATOM   3288 C CA  . TYR A 1 420 ? -35.761 28.246 -29.724 1.00 28.91  ? 421  TYR A CA  1 
ATOM   3289 C C   . TYR A 1 420 ? -35.863 28.671 -31.224 1.00 28.45  ? 421  TYR A C   1 
ATOM   3290 O O   . TYR A 1 420 ? -36.592 29.610 -31.584 1.00 28.00  ? 421  TYR A O   1 
ATOM   3291 C CB  . TYR A 1 420 ? -36.647 27.023 -29.522 1.00 26.51  ? 421  TYR A CB  1 
ATOM   3292 C CG  . TYR A 1 420 ? -38.065 27.223 -29.978 1.00 28.96  ? 421  TYR A CG  1 
ATOM   3293 C CD1 . TYR A 1 420 ? -38.440 27.062 -31.324 1.00 30.09  ? 421  TYR A CD1 1 
ATOM   3294 C CD2 . TYR A 1 420 ? -39.060 27.526 -29.069 1.00 29.71  ? 421  TYR A CD2 1 
ATOM   3295 C CE1 . TYR A 1 420 ? -39.786 27.211 -31.728 1.00 26.79  ? 421  TYR A CE1 1 
ATOM   3296 C CE2 . TYR A 1 420 ? -40.362 27.687 -29.461 1.00 28.69  ? 421  TYR A CE2 1 
ATOM   3297 C CZ  . TYR A 1 420 ? -40.715 27.548 -30.793 1.00 28.14  ? 421  TYR A CZ  1 
ATOM   3298 O OH  . TYR A 1 420 ? -42.019 27.746 -31.103 1.00 27.42  ? 421  TYR A OH  1 
ATOM   3299 N N   . PHE A 1 421 ? -35.223 27.862 -32.073 1.00 25.67  ? 422  PHE A N   1 
ATOM   3300 C CA  . PHE A 1 421 ? -35.261 28.010 -33.496 1.00 25.51  ? 422  PHE A CA  1 
ATOM   3301 C C   . PHE A 1 421 ? -35.541 26.635 -34.015 1.00 26.26  ? 422  PHE A C   1 
ATOM   3302 O O   . PHE A 1 421 ? -34.676 25.719 -33.926 1.00 28.44  ? 422  PHE A O   1 
ATOM   3303 C CB  . PHE A 1 421 ? -33.919 28.543 -33.992 1.00 29.80  ? 422  PHE A CB  1 
ATOM   3304 C CG  . PHE A 1 421 ? -33.871 28.898 -35.492 1.00 31.03  ? 422  PHE A CG  1 
ATOM   3305 C CD1 . PHE A 1 421 ? -34.484 30.055 -35.975 1.00 32.32  ? 422  PHE A CD1 1 
ATOM   3306 C CD2 . PHE A 1 421 ? -33.138 28.122 -36.387 1.00 28.54  ? 422  PHE A CD2 1 
ATOM   3307 C CE1 . PHE A 1 421 ? -34.449 30.382 -37.340 1.00 31.65  ? 422  PHE A CE1 1 
ATOM   3308 C CE2 . PHE A 1 421 ? -33.060 28.466 -37.736 1.00 31.94  ? 422  PHE A CE2 1 
ATOM   3309 C CZ  . PHE A 1 421 ? -33.716 29.591 -38.213 1.00 31.24  ? 422  PHE A CZ  1 
ATOM   3310 N N   . PHE A 1 422 ? -36.759 26.440 -34.488 1.00 24.07  ? 423  PHE A N   1 
ATOM   3311 C CA  . PHE A 1 422 ? -37.161 25.143 -34.975 1.00 27.19  ? 423  PHE A CA  1 
ATOM   3312 C C   . PHE A 1 422 ? -36.847 25.071 -36.474 1.00 32.94  ? 423  PHE A C   1 
ATOM   3313 O O   . PHE A 1 422 ? -37.394 25.889 -37.297 1.00 36.03  ? 423  PHE A O   1 
ATOM   3314 C CB  . PHE A 1 422 ? -38.638 24.971 -34.718 1.00 27.11  ? 423  PHE A CB  1 
ATOM   3315 C CG  . PHE A 1 422 ? -39.189 23.725 -35.260 1.00 30.48  ? 423  PHE A CG  1 
ATOM   3316 C CD1 . PHE A 1 422 ? -39.163 22.555 -34.520 1.00 31.11  ? 423  PHE A CD1 1 
ATOM   3317 C CD2 . PHE A 1 422 ? -39.773 23.708 -36.542 1.00 30.57  ? 423  PHE A CD2 1 
ATOM   3318 C CE1 . PHE A 1 422 ? -39.700 21.374 -35.044 1.00 30.30  ? 423  PHE A CE1 1 
ATOM   3319 C CE2 . PHE A 1 422 ? -40.319 22.543 -37.051 1.00 28.63  ? 423  PHE A CE2 1 
ATOM   3320 C CZ  . PHE A 1 422 ? -40.268 21.374 -36.311 1.00 29.04  ? 423  PHE A CZ  1 
ATOM   3321 N N   . ASN A 1 423 ? -35.969 24.134 -36.848 1.00 32.80  ? 424  ASN A N   1 
ATOM   3322 C CA  . ASN A 1 423 ? -35.563 24.035 -38.235 1.00 34.35  ? 424  ASN A CA  1 
ATOM   3323 C C   . ASN A 1 423 ? -35.491 22.614 -38.787 1.00 35.89  ? 424  ASN A C   1 
ATOM   3324 O O   . ASN A 1 423 ? -34.642 22.331 -39.609 1.00 40.96  ? 424  ASN A O   1 
ATOM   3325 C CB  . ASN A 1 423 ? -34.259 24.760 -38.432 1.00 33.00  ? 424  ASN A CB  1 
ATOM   3326 C CG  . ASN A 1 423 ? -33.113 24.120 -37.676 1.00 36.01  ? 424  ASN A CG  1 
ATOM   3327 O OD1 . ASN A 1 423 ? -33.303 23.251 -36.831 1.00 34.27  ? 424  ASN A OD1 1 
ATOM   3328 N ND2 . ASN A 1 423 ? -31.915 24.578 -37.962 1.00 36.25  ? 424  ASN A ND2 1 
ATOM   3329 N N   . HIS A 1 424 ? -36.405 21.768 -38.375 1.00 31.78  ? 425  HIS A N   1 
ATOM   3330 C CA  . HIS A 1 424 ? -36.532 20.447 -38.938 1.00 37.79  ? 425  HIS A CA  1 
ATOM   3331 C C   . HIS A 1 424 ? -37.688 20.398 -39.939 1.00 35.61  ? 425  HIS A C   1 
ATOM   3332 O O   . HIS A 1 424 ? -38.832 20.643 -39.545 1.00 40.51  ? 425  HIS A O   1 
ATOM   3333 C CB  . HIS A 1 424 ? -36.850 19.402 -37.836 1.00 35.59  ? 425  HIS A CB  1 
ATOM   3334 C CG  . HIS A 1 424 ? -37.107 18.021 -38.376 1.00 33.08  ? 425  HIS A CG  1 
ATOM   3335 N ND1 . HIS A 1 424 ? -36.110 17.239 -38.931 1.00 35.23  ? 425  HIS A ND1 1 
ATOM   3336 C CD2 . HIS A 1 424 ? -38.253 17.330 -38.542 1.00 32.50  ? 425  HIS A CD2 1 
ATOM   3337 C CE1 . HIS A 1 424 ? -36.628 16.106 -39.378 1.00 31.73  ? 425  HIS A CE1 1 
ATOM   3338 N NE2 . HIS A 1 424 ? -37.929 16.141 -39.166 1.00 32.13  ? 425  HIS A NE2 1 
ATOM   3339 N N   . ARG A 1 425 ? -37.447 20.012 -41.187 1.00 40.05  ? 426  ARG A N   1 
ATOM   3340 C CA  . ARG A 1 425 ? -38.580 19.861 -42.111 1.00 48.55  ? 426  ARG A CA  1 
ATOM   3341 C C   . ARG A 1 425 ? -39.030 18.423 -42.010 1.00 46.21  ? 426  ARG A C   1 
ATOM   3342 O O   . ARG A 1 425 ? -38.219 17.514 -42.085 1.00 42.01  ? 426  ARG A O   1 
ATOM   3343 C CB  . ARG A 1 425 ? -38.332 20.391 -43.561 1.00 59.09  ? 426  ARG A CB  1 
ATOM   3344 C CG  . ARG A 1 425 ? -37.995 19.445 -44.725 1.00 68.22  ? 426  ARG A CG  1 
ATOM   3345 C CD  . ARG A 1 425 ? -39.109 19.254 -45.818 1.00 64.23  ? 426  ARG A CD  1 
ATOM   3346 N NE  . ARG A 1 425 ? -39.716 20.480 -46.303 1.00 62.27  ? 426  ARG A NE  1 
ATOM   3347 C CZ  . ARG A 1 425 ? -40.591 20.640 -47.324 1.00 52.38  ? 426  ARG A CZ  1 
ATOM   3348 N NH1 . ARG A 1 425 ? -41.020 19.646 -48.096 1.00 47.01  ? 426  ARG A NH1 1 
ATOM   3349 N NH2 . ARG A 1 425 ? -41.054 21.885 -47.555 1.00 40.68  ? 426  ARG A NH2 1 
ATOM   3350 N N   . ALA A 1 426 ? -40.331 18.272 -41.746 1.00 44.73  ? 427  ALA A N   1 
ATOM   3351 C CA  . ALA A 1 426 ? -40.930 17.005 -41.479 1.00 47.38  ? 427  ALA A CA  1 
ATOM   3352 C C   . ALA A 1 426 ? -40.800 16.189 -42.754 1.00 48.71  ? 427  ALA A C   1 
ATOM   3353 O O   . ALA A 1 426 ? -41.001 16.723 -43.856 1.00 49.48  ? 427  ALA A O   1 
ATOM   3354 C CB  . ALA A 1 426 ? -42.395 17.162 -41.068 1.00 42.90  ? 427  ALA A CB  1 
ATOM   3355 N N   . SER A 1 427 ? -40.465 14.910 -42.580 1.00 49.01  ? 428  SER A N   1 
ATOM   3356 C CA  . SER A 1 427 ? -40.152 13.951 -43.672 1.00 50.25  ? 428  SER A CA  1 
ATOM   3357 C C   . SER A 1 427 ? -41.377 13.685 -44.544 1.00 47.79  ? 428  SER A C   1 
ATOM   3358 O O   . SER A 1 427 ? -41.209 13.334 -45.670 1.00 46.01  ? 428  SER A O   1 
ATOM   3359 C CB  . SER A 1 427 ? -39.657 12.597 -43.076 1.00 49.75  ? 428  SER A CB  1 
ATOM   3360 O OG  . SER A 1 427 ? -40.699 12.035 -42.232 1.00 47.75  ? 428  SER A OG  1 
ATOM   3361 N N   . ASN A 1 428 ? -42.590 13.847 -44.006 1.00 45.21  ? 429  ASN A N   1 
ATOM   3362 C CA  . ASN A 1 428 ? -43.832 13.593 -44.745 1.00 42.41  ? 429  ASN A CA  1 
ATOM   3363 C C   . ASN A 1 428 ? -44.583 14.893 -45.178 1.00 44.65  ? 429  ASN A C   1 
ATOM   3364 O O   . ASN A 1 428 ? -45.810 14.889 -45.385 1.00 41.11  ? 429  ASN A O   1 
ATOM   3365 C CB  . ASN A 1 428 ? -44.771 12.745 -43.868 1.00 42.59  ? 429  ASN A CB  1 
ATOM   3366 C CG  . ASN A 1 428 ? -45.093 13.419 -42.485 1.00 48.04  ? 429  ASN A CG  1 
ATOM   3367 O OD1 . ASN A 1 428 ? -44.578 14.509 -42.149 1.00 39.36  ? 429  ASN A OD1 1 
ATOM   3368 N ND2 . ASN A 1 428 ? -45.927 12.742 -41.671 1.00 42.83  ? 429  ASN A ND2 1 
ATOM   3369 N N   . LEU A 1 429 ? -43.886 16.018 -45.269 1.00 43.62  ? 430  LEU A N   1 
ATOM   3370 C CA  . LEU A 1 429 ? -44.578 17.274 -45.634 1.00 45.08  ? 430  LEU A CA  1 
ATOM   3371 C C   . LEU A 1 429 ? -45.083 17.168 -47.106 1.00 44.60  ? 430  LEU A C   1 
ATOM   3372 O O   . LEU A 1 429 ? -44.359 16.773 -48.018 1.00 40.40  ? 430  LEU A O   1 
ATOM   3373 C CB  . LEU A 1 429 ? -43.659 18.510 -45.474 1.00 51.79  ? 430  LEU A CB  1 
ATOM   3374 C CG  . LEU A 1 429 ? -44.210 19.762 -44.768 1.00 54.59  ? 430  LEU A CG  1 
ATOM   3375 C CD1 . LEU A 1 429 ? -44.845 19.409 -43.467 1.00 61.91  ? 430  LEU A CD1 1 
ATOM   3376 C CD2 . LEU A 1 429 ? -43.079 20.708 -44.452 1.00 60.32  ? 430  LEU A CD2 1 
ATOM   3377 N N   . VAL A 1 430 ? -46.349 17.478 -47.289 1.00 42.65  ? 431  VAL A N   1 
ATOM   3378 C CA  . VAL A 1 430 ? -46.980 17.392 -48.567 1.00 41.04  ? 431  VAL A CA  1 
ATOM   3379 C C   . VAL A 1 430 ? -46.655 18.640 -49.387 1.00 38.95  ? 431  VAL A C   1 
ATOM   3380 O O   . VAL A 1 430 ? -46.847 18.629 -50.582 1.00 37.88  ? 431  VAL A O   1 
ATOM   3381 C CB  . VAL A 1 430 ? -48.498 17.223 -48.380 1.00 44.13  ? 431  VAL A CB  1 
ATOM   3382 C CG1 . VAL A 1 430 ? -48.778 15.837 -47.797 1.00 42.30  ? 431  VAL A CG1 1 
ATOM   3383 C CG2 . VAL A 1 430 ? -49.060 18.326 -47.432 1.00 41.76  ? 431  VAL A CG2 1 
ATOM   3384 N N   . TRP A 1 431 ? -46.206 19.715 -48.741 1.00 36.52  ? 432  TRP A N   1 
ATOM   3385 C CA  . TRP A 1 431 ? -45.910 20.991 -49.428 1.00 31.77  ? 432  TRP A CA  1 
ATOM   3386 C C   . TRP A 1 431 ? -44.578 20.831 -50.098 1.00 27.50  ? 432  TRP A C   1 
ATOM   3387 O O   . TRP A 1 431 ? -43.802 20.017 -49.689 1.00 33.44  ? 432  TRP A O   1 
ATOM   3388 C CB  . TRP A 1 431 ? -45.859 22.190 -48.421 1.00 30.44  ? 432  TRP A CB  1 
ATOM   3389 C CG  . TRP A 1 431 ? -47.138 22.585 -47.837 1.00 28.96  ? 432  TRP A CG  1 
ATOM   3390 C CD1 . TRP A 1 431 ? -47.596 22.236 -46.602 1.00 28.51  ? 432  TRP A CD1 1 
ATOM   3391 C CD2 . TRP A 1 431 ? -48.192 23.324 -48.454 1.00 29.61  ? 432  TRP A CD2 1 
ATOM   3392 N NE1 . TRP A 1 431 ? -48.849 22.701 -46.413 1.00 29.98  ? 432  TRP A NE1 1 
ATOM   3393 C CE2 . TRP A 1 431 ? -49.241 23.412 -47.509 1.00 30.96  ? 432  TRP A CE2 1 
ATOM   3394 C CE3 . TRP A 1 431 ? -48.357 23.922 -49.690 1.00 32.36  ? 432  TRP A CE3 1 
ATOM   3395 C CZ2 . TRP A 1 431 ? -50.452 24.068 -47.771 1.00 33.84  ? 432  TRP A CZ2 1 
ATOM   3396 C CZ3 . TRP A 1 431 ? -49.569 24.635 -49.953 1.00 36.07  ? 432  TRP A CZ3 1 
ATOM   3397 C CH2 . TRP A 1 431 ? -50.591 24.691 -48.989 1.00 37.91  ? 432  TRP A CH2 1 
ATOM   3398 N N   . PRO A 1 432 ? -44.284 21.614 -51.129 1.00 28.96  ? 433  PRO A N   1 
ATOM   3399 C CA  . PRO A 1 432 ? -43.015 21.411 -51.846 1.00 26.89  ? 433  PRO A CA  1 
ATOM   3400 C C   . PRO A 1 432 ? -41.785 21.811 -51.019 1.00 29.50  ? 433  PRO A C   1 
ATOM   3401 O O   . PRO A 1 432 ? -41.866 22.636 -50.105 1.00 30.55  ? 433  PRO A O   1 
ATOM   3402 C CB  . PRO A 1 432 ? -43.173 22.373 -53.030 1.00 28.02  ? 433  PRO A CB  1 
ATOM   3403 C CG  . PRO A 1 432 ? -44.110 23.503 -52.517 1.00 25.98  ? 433  PRO A CG  1 
ATOM   3404 C CD  . PRO A 1 432 ? -45.088 22.714 -51.730 1.00 28.00  ? 433  PRO A CD  1 
ATOM   3405 N N   . GLU A 1 433 ? -40.630 21.346 -51.436 1.00 32.91  ? 434  GLU A N   1 
ATOM   3406 C CA  . GLU A 1 433 ? -39.378 21.576 -50.765 1.00 35.13  ? 434  GLU A CA  1 
ATOM   3407 C C   . GLU A 1 433 ? -39.019 23.034 -50.624 1.00 32.11  ? 434  GLU A C   1 
ATOM   3408 O O   . GLU A 1 433 ? -38.323 23.410 -49.693 1.00 28.32  ? 434  GLU A O   1 
ATOM   3409 C CB  . GLU A 1 433 ? -38.237 20.934 -51.548 1.00 42.07  ? 434  GLU A CB  1 
ATOM   3410 C CG  . GLU A 1 433 ? -38.279 19.412 -51.587 1.00 59.17  ? 434  GLU A CG  1 
ATOM   3411 C CD  . GLU A 1 433 ? -38.046 18.765 -50.221 1.00 74.26  ? 434  GLU A CD  1 
ATOM   3412 O OE1 . GLU A 1 433 ? -37.096 19.186 -49.507 1.00 82.45  ? 434  GLU A OE1 1 
ATOM   3413 O OE2 . GLU A 1 433 ? -38.818 17.835 -49.854 1.00 77.16  ? 434  GLU A OE2 1 
ATOM   3414 N N   . TRP A 1 434 ? -39.339 23.847 -51.624 1.00 31.98  ? 435  TRP A N   1 
ATOM   3415 C CA  . TRP A 1 434 ? -38.837 25.209 -51.577 1.00 30.24  ? 435  TRP A CA  1 
ATOM   3416 C C   . TRP A 1 434 ? -39.377 25.982 -50.326 1.00 27.83  ? 435  TRP A C   1 
ATOM   3417 O O   . TRP A 1 434 ? -38.767 26.902 -49.895 1.00 25.50  ? 435  TRP A O   1 
ATOM   3418 C CB  . TRP A 1 434 ? -39.093 25.967 -52.874 1.00 27.24  ? 435  TRP A CB  1 
ATOM   3419 C CG  . TRP A 1 434 ? -40.524 26.300 -53.164 1.00 30.37  ? 435  TRP A CG  1 
ATOM   3420 C CD1 . TRP A 1 434 ? -41.355 25.597 -53.966 1.00 32.06  ? 435  TRP A CD1 1 
ATOM   3421 C CD2 . TRP A 1 434 ? -41.290 27.429 -52.698 1.00 26.61  ? 435  TRP A CD2 1 
ATOM   3422 N NE1 . TRP A 1 434 ? -42.590 26.197 -54.028 1.00 31.60  ? 435  TRP A NE1 1 
ATOM   3423 C CE2 . TRP A 1 434 ? -42.580 27.314 -53.253 1.00 28.24  ? 435  TRP A CE2 1 
ATOM   3424 C CE3 . TRP A 1 434 ? -41.031 28.479 -51.832 1.00 30.01  ? 435  TRP A CE3 1 
ATOM   3425 C CZ2 . TRP A 1 434 ? -43.599 28.206 -52.993 1.00 31.19  ? 435  TRP A CZ2 1 
ATOM   3426 C CZ3 . TRP A 1 434 ? -42.073 29.420 -51.575 1.00 31.00  ? 435  TRP A CZ3 1 
ATOM   3427 C CH2 . TRP A 1 434 ? -43.334 29.257 -52.147 1.00 33.73  ? 435  TRP A CH2 1 
ATOM   3428 N N   . MET A 1 435 ? -40.540 25.589 -49.802 1.00 28.57  ? 436  MET A N   1 
ATOM   3429 C CA  . MET A 1 435 ? -41.185 26.265 -48.674 1.00 27.08  ? 436  MET A CA  1 
ATOM   3430 C C   . MET A 1 435 ? -40.450 26.026 -47.342 1.00 31.50  ? 436  MET A C   1 
ATOM   3431 O O   . MET A 1 435 ? -40.684 26.762 -46.378 1.00 31.80  ? 436  MET A O   1 
ATOM   3432 C CB  . MET A 1 435 ? -42.664 25.861 -48.587 1.00 26.61  ? 436  MET A CB  1 
ATOM   3433 C CG  . MET A 1 435 ? -43.453 26.340 -49.799 1.00 26.37  ? 436  MET A CG  1 
ATOM   3434 S SD  . MET A 1 435 ? -45.128 25.750 -49.904 1.00 28.70  ? 436  MET A SD  1 
ATOM   3435 C CE  . MET A 1 435 ? -45.934 26.925 -48.797 1.00 30.17  ? 436  MET A CE  1 
ATOM   3436 N N   . GLY A 1 436 ? -39.530 25.056 -47.330 1.00 30.38  ? 437  GLY A N   1 
ATOM   3437 C CA  . GLY A 1 436 ? -38.680 24.748 -46.194 1.00 30.10  ? 437  GLY A CA  1 
ATOM   3438 C C   . GLY A 1 436 ? -39.428 24.270 -44.939 1.00 29.58  ? 437  GLY A C   1 
ATOM   3439 O O   . GLY A 1 436 ? -40.289 23.407 -44.989 1.00 28.19  ? 437  GLY A O   1 
ATOM   3440 N N   . VAL A 1 437 ? -39.120 24.902 -43.819 1.00 29.72  ? 438  VAL A N   1 
ATOM   3441 C CA  . VAL A 1 437 ? -39.745 24.599 -42.531 1.00 28.73  ? 438  VAL A CA  1 
ATOM   3442 C C   . VAL A 1 437 ? -40.827 25.689 -42.362 1.00 29.48  ? 438  VAL A C   1 
ATOM   3443 O O   . VAL A 1 437 ? -40.601 26.823 -41.882 1.00 29.64  ? 438  VAL A O   1 
ATOM   3444 C CB  . VAL A 1 437 ? -38.702 24.679 -41.438 1.00 30.50  ? 438  VAL A CB  1 
ATOM   3445 C CG1 . VAL A 1 437 ? -39.268 24.256 -40.099 1.00 32.63  ? 438  VAL A CG1 1 
ATOM   3446 C CG2 . VAL A 1 437 ? -37.492 23.847 -41.809 1.00 32.85  ? 438  VAL A CG2 1 
ATOM   3447 N N   . ILE A 1 438 ? -42.010 25.304 -42.767 1.00 30.12  ? 439  ILE A N   1 
ATOM   3448 C CA  . ILE A 1 438 ? -43.138 26.179 -42.961 1.00 31.08  ? 439  ILE A CA  1 
ATOM   3449 C C   . ILE A 1 438 ? -43.852 26.605 -41.650 1.00 35.46  ? 439  ILE A C   1 
ATOM   3450 O O   . ILE A 1 438 ? -43.887 25.882 -40.639 1.00 34.49  ? 439  ILE A O   1 
ATOM   3451 C CB  . ILE A 1 438 ? -44.157 25.445 -43.810 1.00 31.77  ? 439  ILE A CB  1 
ATOM   3452 C CG1 . ILE A 1 438 ? -43.490 25.050 -45.133 1.00 36.30  ? 439  ILE A CG1 1 
ATOM   3453 C CG2 . ILE A 1 438 ? -45.428 26.262 -44.012 1.00 34.01  ? 439  ILE A CG2 1 
ATOM   3454 C CD1 . ILE A 1 438 ? -44.341 24.141 -45.986 1.00 35.21  ? 439  ILE A CD1 1 
ATOM   3455 N N   . HIS A 1 439 ? -44.404 27.810 -41.721 1.00 31.94  ? 440  HIS A N   1 
ATOM   3456 C CA  . HIS A 1 439 ? -45.192 28.403 -40.726 1.00 34.13  ? 440  HIS A CA  1 
ATOM   3457 C C   . HIS A 1 439 ? -46.149 27.328 -40.263 1.00 32.28  ? 440  HIS A C   1 
ATOM   3458 O O   . HIS A 1 439 ? -46.856 26.752 -41.053 1.00 32.20  ? 440  HIS A O   1 
ATOM   3459 C CB  . HIS A 1 439 ? -45.921 29.551 -41.384 1.00 37.54  ? 440  HIS A CB  1 
ATOM   3460 C CG  . HIS A 1 439 ? -46.685 30.427 -40.464 1.00 42.43  ? 440  HIS A CG  1 
ATOM   3461 N ND1 . HIS A 1 439 ? -46.065 31.254 -39.529 1.00 48.28  ? 440  HIS A ND1 1 
ATOM   3462 C CD2 . HIS A 1 439 ? -48.020 30.666 -40.376 1.00 40.40  ? 440  HIS A CD2 1 
ATOM   3463 C CE1 . HIS A 1 439 ? -46.997 31.965 -38.906 1.00 50.98  ? 440  HIS A CE1 1 
ATOM   3464 N NE2 . HIS A 1 439 ? -48.188 31.617 -39.393 1.00 49.02  ? 440  HIS A NE2 1 
ATOM   3465 N N   . GLY A 1 440 ? -46.160 27.037 -38.975 1.00 30.09  ? 441  GLY A N   1 
ATOM   3466 C CA  . GLY A 1 440 ? -47.166 26.093 -38.460 1.00 31.05  ? 441  GLY A CA  1 
ATOM   3467 C C   . GLY A 1 440 ? -46.777 24.638 -38.376 1.00 30.09  ? 441  GLY A C   1 
ATOM   3468 O O   . GLY A 1 440 ? -47.528 23.847 -37.831 1.00 28.28  ? 441  GLY A O   1 
ATOM   3469 N N   . TYR A 1 441 ? -45.581 24.269 -38.831 1.00 30.99  ? 442  TYR A N   1 
ATOM   3470 C CA  . TYR A 1 441 ? -45.274 22.838 -38.939 1.00 32.01  ? 442  TYR A CA  1 
ATOM   3471 C C   . TYR A 1 441 ? -44.451 22.347 -37.755 1.00 35.37  ? 442  TYR A C   1 
ATOM   3472 O O   . TYR A 1 441 ? -44.022 21.186 -37.707 1.00 38.00  ? 442  TYR A O   1 
ATOM   3473 C CB  . TYR A 1 441 ? -44.725 22.480 -40.376 1.00 34.25  ? 442  TYR A CB  1 
ATOM   3474 C CG  . TYR A 1 441 ? -45.935 22.364 -41.326 1.00 33.76  ? 442  TYR A CG  1 
ATOM   3475 C CD1 . TYR A 1 441 ? -46.541 23.503 -41.843 1.00 35.87  ? 442  TYR A CD1 1 
ATOM   3476 C CD2 . TYR A 1 441 ? -46.596 21.104 -41.550 1.00 37.25  ? 442  TYR A CD2 1 
ATOM   3477 C CE1 . TYR A 1 441 ? -47.703 23.421 -42.635 1.00 38.09  ? 442  TYR A CE1 1 
ATOM   3478 C CE2 . TYR A 1 441 ? -47.754 21.024 -42.313 1.00 34.07  ? 442  TYR A CE2 1 
ATOM   3479 C CZ  . TYR A 1 441 ? -48.298 22.191 -42.860 1.00 34.37  ? 442  TYR A CZ  1 
ATOM   3480 O OH  . TYR A 1 441 ? -49.430 22.157 -43.610 1.00 34.93  ? 442  TYR A OH  1 
ATOM   3481 N N   . GLU A 1 442 ? -44.286 23.211 -36.753 1.00 27.86  ? 443  GLU A N   1 
ATOM   3482 C CA  . GLU A 1 442 ? -43.819 22.739 -35.448 1.00 26.46  ? 443  GLU A CA  1 
ATOM   3483 C C   . GLU A 1 442 ? -45.033 22.267 -34.633 1.00 25.02  ? 443  GLU A C   1 
ATOM   3484 O O   . GLU A 1 442 ? -44.927 21.461 -33.738 1.00 27.49  ? 443  GLU A O   1 
ATOM   3485 C CB  . GLU A 1 442 ? -43.008 23.826 -34.719 1.00 27.34  ? 443  GLU A CB  1 
ATOM   3486 C CG  . GLU A 1 442 ? -43.819 24.810 -33.876 1.00 27.55  ? 443  GLU A CG  1 
ATOM   3487 C CD  . GLU A 1 442 ? -44.774 25.746 -34.653 1.00 30.74  ? 443  GLU A CD  1 
ATOM   3488 O OE1 . GLU A 1 442 ? -44.866 25.744 -35.927 1.00 30.45  ? 443  GLU A OE1 1 
ATOM   3489 O OE2 . GLU A 1 442 ? -45.494 26.492 -33.974 1.00 33.43  ? 443  GLU A OE2 1 
ATOM   3490 N N   . ILE A 1 443 ? -46.222 22.702 -34.996 1.00 26.10  ? 444  ILE A N   1 
ATOM   3491 C CA  . ILE A 1 443 ? -47.370 22.435 -34.140 1.00 27.96  ? 444  ILE A CA  1 
ATOM   3492 C C   . ILE A 1 443 ? -47.542 20.923 -33.970 1.00 31.36  ? 444  ILE A C   1 
ATOM   3493 O O   . ILE A 1 443 ? -47.813 20.435 -32.862 1.00 28.71  ? 444  ILE A O   1 
ATOM   3494 C CB  . ILE A 1 443 ? -48.653 23.069 -34.678 1.00 26.68  ? 444  ILE A CB  1 
ATOM   3495 C CG1 . ILE A 1 443 ? -48.558 24.586 -34.668 1.00 27.61  ? 444  ILE A CG1 1 
ATOM   3496 C CG2 . ILE A 1 443 ? -49.853 22.620 -33.894 1.00 29.77  ? 444  ILE A CG2 1 
ATOM   3497 C CD1 . ILE A 1 443 ? -49.718 25.245 -35.385 1.00 27.38  ? 444  ILE A CD1 1 
ATOM   3498 N N   . GLU A 1 444 ? -47.440 20.196 -35.084 1.00 31.27  ? 445  GLU A N   1 
ATOM   3499 C CA  . GLU A 1 444 ? -47.599 18.754 -35.039 1.00 32.28  ? 445  GLU A CA  1 
ATOM   3500 C C   . GLU A 1 444 ? -46.606 18.079 -34.099 1.00 29.54  ? 445  GLU A C   1 
ATOM   3501 O O   . GLU A 1 444 ? -46.931 17.019 -33.553 1.00 27.48  ? 445  GLU A O   1 
ATOM   3502 C CB  . GLU A 1 444 ? -47.560 18.144 -36.446 1.00 32.74  ? 445  GLU A CB  1 
ATOM   3503 C CG  . GLU A 1 444 ? -46.364 18.534 -37.280 1.00 34.04  ? 445  GLU A CG  1 
ATOM   3504 C CD  . GLU A 1 444 ? -46.658 18.359 -38.788 1.00 33.84  ? 445  GLU A CD  1 
ATOM   3505 O OE1 . GLU A 1 444 ? -47.611 18.977 -39.278 1.00 32.33  ? 445  GLU A OE1 1 
ATOM   3506 O OE2 . GLU A 1 444 ? -45.902 17.629 -39.456 1.00 32.86  ? 445  GLU A OE2 1 
ATOM   3507 N N   . PHE A 1 445 ? -45.441 18.686 -33.901 1.00 26.41  ? 446  PHE A N   1 
ATOM   3508 C CA  . PHE A 1 445 ? -44.456 18.131 -32.988 1.00 31.38  ? 446  PHE A CA  1 
ATOM   3509 C C   . PHE A 1 445 ? -44.809 18.429 -31.532 1.00 34.34  ? 446  PHE A C   1 
ATOM   3510 O O   . PHE A 1 445 ? -44.583 17.586 -30.660 1.00 32.87  ? 446  PHE A O   1 
ATOM   3511 C CB  . PHE A 1 445 ? -43.062 18.636 -33.311 1.00 31.22  ? 446  PHE A CB  1 
ATOM   3512 C CG  . PHE A 1 445 ? -42.493 17.983 -34.546 1.00 34.97  ? 446  PHE A CG  1 
ATOM   3513 C CD1 . PHE A 1 445 ? -42.824 18.465 -35.825 1.00 32.80  ? 446  PHE A CD1 1 
ATOM   3514 C CD2 . PHE A 1 445 ? -41.706 16.811 -34.452 1.00 35.71  ? 446  PHE A CD2 1 
ATOM   3515 C CE1 . PHE A 1 445 ? -42.343 17.847 -36.957 1.00 32.28  ? 446  PHE A CE1 1 
ATOM   3516 C CE2 . PHE A 1 445 ? -41.203 16.187 -35.604 1.00 34.71  ? 446  PHE A CE2 1 
ATOM   3517 C CZ  . PHE A 1 445 ? -41.543 16.692 -36.852 1.00 34.88  ? 446  PHE A CZ  1 
ATOM   3518 N N   . VAL A 1 446 ? -45.399 19.615 -31.310 1.00 32.48  ? 447  VAL A N   1 
ATOM   3519 C CA  . VAL A 1 446 ? -45.787 20.078 -29.990 1.00 31.71  ? 447  VAL A CA  1 
ATOM   3520 C C   . VAL A 1 446 ? -46.983 19.229 -29.540 1.00 33.90  ? 447  VAL A C   1 
ATOM   3521 O O   . VAL A 1 446 ? -47.114 18.887 -28.344 1.00 27.83  ? 447  VAL A O   1 
ATOM   3522 C CB  . VAL A 1 446 ? -46.084 21.606 -29.973 1.00 29.46  ? 447  VAL A CB  1 
ATOM   3523 C CG1 . VAL A 1 446 ? -46.852 22.034 -28.745 1.00 28.72  ? 447  VAL A CG1 1 
ATOM   3524 C CG2 . VAL A 1 446 ? -44.794 22.409 -30.053 1.00 31.06  ? 447  VAL A CG2 1 
ATOM   3525 N N   . PHE A 1 447 ? -47.840 18.843 -30.484 1.00 30.18  ? 448  PHE A N   1 
ATOM   3526 C CA  . PHE A 1 447 ? -49.000 18.082 -30.085 1.00 28.29  ? 448  PHE A CA  1 
ATOM   3527 C C   . PHE A 1 447 ? -48.796 16.537 -30.184 1.00 32.11  ? 448  PHE A C   1 
ATOM   3528 O O   . PHE A 1 447 ? -49.705 15.773 -29.921 1.00 29.88  ? 448  PHE A O   1 
ATOM   3529 C CB  . PHE A 1 447 ? -50.216 18.550 -30.837 1.00 29.37  ? 448  PHE A CB  1 
ATOM   3530 C CG  . PHE A 1 447 ? -50.843 19.784 -30.264 1.00 29.19  ? 448  PHE A CG  1 
ATOM   3531 C CD1 . PHE A 1 447 ? -50.354 21.041 -30.579 1.00 28.78  ? 448  PHE A CD1 1 
ATOM   3532 C CD2 . PHE A 1 447 ? -51.925 19.691 -29.446 1.00 30.21  ? 448  PHE A CD2 1 
ATOM   3533 C CE1 . PHE A 1 447 ? -50.971 22.173 -30.079 1.00 28.70  ? 448  PHE A CE1 1 
ATOM   3534 C CE2 . PHE A 1 447 ? -52.562 20.816 -28.946 1.00 31.44  ? 448  PHE A CE2 1 
ATOM   3535 C CZ  . PHE A 1 447 ? -52.076 22.057 -29.252 1.00 30.46  ? 448  PHE A CZ  1 
ATOM   3536 N N   . GLY A 1 448 ? -47.597 16.086 -30.531 1.00 32.85  ? 449  GLY A N   1 
ATOM   3537 C CA  . GLY A 1 448 ? -47.304 14.669 -30.472 1.00 36.39  ? 449  GLY A CA  1 
ATOM   3538 C C   . GLY A 1 448 ? -47.793 13.752 -31.602 1.00 35.98  ? 449  GLY A C   1 
ATOM   3539 O O   . GLY A 1 448 ? -47.762 12.529 -31.437 1.00 35.34  ? 449  GLY A O   1 
ATOM   3540 N N   . LEU A 1 449 ? -48.154 14.319 -32.754 1.00 33.24  ? 450  LEU A N   1 
ATOM   3541 C CA  . LEU A 1 449 ? -48.657 13.547 -33.913 1.00 36.63  ? 450  LEU A CA  1 
ATOM   3542 C C   . LEU A 1 449 ? -47.614 12.494 -34.408 1.00 36.48  ? 450  LEU A C   1 
ATOM   3543 O O   . LEU A 1 449 ? -47.964 11.423 -34.852 1.00 39.25  ? 450  LEU A O   1 
ATOM   3544 C CB  . LEU A 1 449 ? -49.140 14.474 -35.056 1.00 35.43  ? 450  LEU A CB  1 
ATOM   3545 C CG  . LEU A 1 449 ? -50.509 15.197 -34.839 1.00 36.96  ? 450  LEU A CG  1 
ATOM   3546 C CD1 . LEU A 1 449 ? -51.682 14.258 -34.851 1.00 42.36  ? 450  LEU A CD1 1 
ATOM   3547 C CD2 . LEU A 1 449 ? -50.595 15.874 -33.489 1.00 36.19  ? 450  LEU A CD2 1 
ATOM   3548 N N   . PRO A 1 450 ? -46.345 12.776 -34.283 1.00 33.89  ? 451  PRO A N   1 
ATOM   3549 C CA  . PRO A 1 450 ? -45.375 11.779 -34.666 1.00 40.79  ? 451  PRO A CA  1 
ATOM   3550 C C   . PRO A 1 450 ? -45.312 10.503 -33.846 1.00 42.90  ? 451  PRO A C   1 
ATOM   3551 O O   . PRO A 1 450 ? -44.518 9.626  -34.182 1.00 49.03  ? 451  PRO A O   1 
ATOM   3552 C CB  . PRO A 1 450 ? -44.042 12.512 -34.512 1.00 35.75  ? 451  PRO A CB  1 
ATOM   3553 C CG  . PRO A 1 450 ? -44.423 13.862 -34.856 1.00 37.47  ? 451  PRO A CG  1 
ATOM   3554 C CD  . PRO A 1 450 ? -45.700 14.067 -34.081 1.00 37.38  ? 451  PRO A CD  1 
ATOM   3555 N N   . LEU A 1 451 ? -46.078 10.397 -32.779 1.00 44.39  ? 452  LEU A N   1 
ATOM   3556 C CA  . LEU A 1 451 ? -46.074 9.155  -32.028 1.00 43.39  ? 452  LEU A CA  1 
ATOM   3557 C C   . LEU A 1 451 ? -47.097 8.200  -32.596 1.00 45.96  ? 452  LEU A C   1 
ATOM   3558 O O   . LEU A 1 451 ? -47.148 7.038  -32.162 1.00 51.83  ? 452  LEU A O   1 
ATOM   3559 C CB  . LEU A 1 451 ? -46.415 9.340  -30.550 1.00 42.11  ? 452  LEU A CB  1 
ATOM   3560 C CG  . LEU A 1 451 ? -45.950 10.419 -29.614 1.00 48.64  ? 452  LEU A CG  1 
ATOM   3561 C CD1 . LEU A 1 451 ? -46.188 9.979  -28.144 1.00 52.93  ? 452  LEU A CD1 1 
ATOM   3562 C CD2 . LEU A 1 451 ? -44.538 10.899 -29.868 1.00 49.84  ? 452  LEU A CD2 1 
ATOM   3563 N N   . VAL A 1 452 ? -47.964 8.707  -33.469 1.00 42.59  ? 453  VAL A N   1 
ATOM   3564 C CA  . VAL A 1 452 ? -48.977 7.920  -34.121 1.00 43.71  ? 453  VAL A CA  1 
ATOM   3565 C C   . VAL A 1 452 ? -48.337 7.251  -35.378 1.00 51.56  ? 453  VAL A C   1 
ATOM   3566 O O   . VAL A 1 452 ? -47.956 7.914  -36.366 1.00 50.55  ? 453  VAL A O   1 
ATOM   3567 C CB  . VAL A 1 452 ? -50.212 8.780  -34.465 1.00 49.21  ? 453  VAL A CB  1 
ATOM   3568 C CG1 . VAL A 1 452 ? -51.331 7.932  -35.056 1.00 44.69  ? 453  VAL A CG1 1 
ATOM   3569 C CG2 . VAL A 1 452 ? -50.759 9.505  -33.228 1.00 52.00  ? 453  VAL A CG2 1 
ATOM   3570 N N   . LYS A 1 453 ? -48.194 5.931  -35.319 1.00 52.81  ? 454  LYS A N   1 
ATOM   3571 C CA  . LYS A 1 453 ? -47.448 5.180  -36.327 1.00 61.80  ? 454  LYS A CA  1 
ATOM   3572 C C   . LYS A 1 453 ? -48.020 5.403  -37.749 1.00 54.53  ? 454  LYS A C   1 
ATOM   3573 O O   . LYS A 1 453 ? -47.294 5.651  -38.694 1.00 52.06  ? 454  LYS A O   1 
ATOM   3574 C CB  . LYS A 1 453 ? -47.441 3.703  -35.891 1.00 74.82  ? 454  LYS A CB  1 
ATOM   3575 C CG  . LYS A 1 453 ? -47.152 2.673  -36.971 1.00 89.27  ? 454  LYS A CG  1 
ATOM   3576 C CD  . LYS A 1 453 ? -47.802 1.341  -36.606 1.00 93.99  ? 454  LYS A CD  1 
ATOM   3577 C CE  . LYS A 1 453 ? -47.349 0.232  -37.543 1.00 91.54  ? 454  LYS A CE  1 
ATOM   3578 N NZ  . LYS A 1 453 ? -47.617 -1.081 -36.910 1.00 92.21  ? 454  LYS A NZ  1 
ATOM   3579 N N   . GLU A 1 454 ? -49.340 5.413  -37.847 1.00 51.41  ? 455  GLU A N   1 
ATOM   3580 C CA  . GLU A 1 454 ? -50.060 5.534  -39.101 1.00 54.96  ? 455  GLU A CA  1 
ATOM   3581 C C   . GLU A 1 454 ? -49.786 6.854  -39.829 1.00 59.79  ? 455  GLU A C   1 
ATOM   3582 O O   . GLU A 1 454 ? -49.982 6.944  -41.036 1.00 64.07  ? 455  GLU A O   1 
ATOM   3583 C CB  . GLU A 1 454 ? -51.579 5.424  -38.866 1.00 60.79  ? 455  GLU A CB  1 
ATOM   3584 C CG  . GLU A 1 454 ? -52.060 4.218  -38.021 1.00 75.05  ? 455  GLU A CG  1 
ATOM   3585 C CD  . GLU A 1 454 ? -51.783 4.350  -36.506 1.00 79.97  ? 455  GLU A CD  1 
ATOM   3586 O OE1 . GLU A 1 454 ? -52.716 4.638  -35.724 1.00 84.51  ? 455  GLU A OE1 1 
ATOM   3587 O OE2 . GLU A 1 454 ? -50.619 4.182  -36.084 1.00 80.23  ? 455  GLU A OE2 1 
ATOM   3588 N N   . LEU A 1 455 ? -49.386 7.898  -39.115 1.00 54.95  ? 456  LEU A N   1 
ATOM   3589 C CA  . LEU A 1 455 ? -49.156 9.168  -39.765 1.00 49.45  ? 456  LEU A CA  1 
ATOM   3590 C C   . LEU A 1 455 ? -47.779 9.240  -40.426 1.00 50.83  ? 456  LEU A C   1 
ATOM   3591 O O   . LEU A 1 455 ? -47.530 10.157 -41.171 1.00 51.11  ? 456  LEU A O   1 
ATOM   3592 C CB  . LEU A 1 455 ? -49.351 10.322 -38.810 1.00 47.43  ? 456  LEU A CB  1 
ATOM   3593 C CG  . LEU A 1 455 ? -50.722 10.441 -38.149 1.00 49.84  ? 456  LEU A CG  1 
ATOM   3594 C CD1 . LEU A 1 455 ? -50.725 11.665 -37.212 1.00 47.03  ? 456  LEU A CD1 1 
ATOM   3595 C CD2 . LEU A 1 455 ? -51.870 10.512 -39.177 1.00 46.36  ? 456  LEU A CD2 1 
ATOM   3596 N N   . ASN A 1 456 ? -46.962 8.212  -40.229 1.00 52.00  ? 457  ASN A N   1 
ATOM   3597 C CA  . ASN A 1 456 ? -45.784 7.986  -41.061 1.00 58.70  ? 457  ASN A CA  1 
ATOM   3598 C C   . ASN A 1 456 ? -44.648 8.987  -40.893 1.00 55.18  ? 457  ASN A C   1 
ATOM   3599 O O   . ASN A 1 456 ? -44.052 9.435  -41.872 1.00 60.62  ? 457  ASN A O   1 
ATOM   3600 C CB  . ASN A 1 456 ? -46.187 7.906  -42.536 1.00 65.24  ? 457  ASN A CB  1 
ATOM   3601 C CG  . ASN A 1 456 ? -47.187 6.800  -42.808 1.00 59.98  ? 457  ASN A CG  1 
ATOM   3602 O OD1 . ASN A 1 456 ? -47.164 5.753  -42.160 1.00 52.51  ? 457  ASN A OD1 1 
ATOM   3603 N ND2 . ASN A 1 456 ? -48.072 7.026  -43.772 1.00 63.92  ? 457  ASN A ND2 1 
ATOM   3604 N N   . TYR A 1 457 ? -44.346 9.323  -39.647 1.00 50.20  ? 458  TYR A N   1 
ATOM   3605 C CA  . TYR A 1 457 ? -43.171 10.142 -39.331 1.00 40.34  ? 458  TYR A CA  1 
ATOM   3606 C C   . TYR A 1 457 ? -42.064 9.142  -39.158 1.00 40.66  ? 458  TYR A C   1 
ATOM   3607 O O   . TYR A 1 457 ? -42.325 7.975  -39.032 1.00 40.26  ? 458  TYR A O   1 
ATOM   3608 C CB  . TYR A 1 457 ? -43.409 10.970 -38.038 1.00 39.62  ? 458  TYR A CB  1 
ATOM   3609 C CG  . TYR A 1 457 ? -44.426 12.136 -38.184 1.00 35.75  ? 458  TYR A CG  1 
ATOM   3610 C CD1 . TYR A 1 457 ? -45.771 11.951 -38.012 1.00 35.25  ? 458  TYR A CD1 1 
ATOM   3611 C CD2 . TYR A 1 457 ? -43.999 13.417 -38.504 1.00 33.76  ? 458  TYR A CD2 1 
ATOM   3612 C CE1 . TYR A 1 457 ? -46.679 12.987 -38.143 1.00 32.24  ? 458  TYR A CE1 1 
ATOM   3613 C CE2 . TYR A 1 457 ? -44.906 14.464 -38.632 1.00 32.05  ? 458  TYR A CE2 1 
ATOM   3614 C CZ  . TYR A 1 457 ? -46.240 14.255 -38.461 1.00 32.10  ? 458  TYR A CZ  1 
ATOM   3615 O OH  . TYR A 1 457 ? -47.136 15.340 -38.603 1.00 31.56  ? 458  TYR A OH  1 
ATOM   3616 N N   . THR A 1 458 ? -40.820 9.581  -39.157 1.00 42.61  ? 459  THR A N   1 
ATOM   3617 C CA  . THR A 1 458 ? -39.730 8.720  -38.774 1.00 40.98  ? 459  THR A CA  1 
ATOM   3618 C C   . THR A 1 458 ? -39.570 8.560  -37.249 1.00 48.74  ? 459  THR A C   1 
ATOM   3619 O O   . THR A 1 458 ? -40.033 9.362  -36.456 1.00 47.63  ? 459  THR A O   1 
ATOM   3620 C CB  . THR A 1 458 ? -38.448 9.336  -39.266 1.00 45.15  ? 459  THR A CB  1 
ATOM   3621 O OG1 . THR A 1 458 ? -38.211 10.589 -38.577 1.00 39.20  ? 459  THR A OG1 1 
ATOM   3622 C CG2 . THR A 1 458 ? -38.519 9.496  -40.842 1.00 40.80  ? 459  THR A CG2 1 
ATOM   3623 N N   . ALA A 1 459 ? -38.854 7.538  -36.844 1.00 49.24  ? 460  ALA A N   1 
ATOM   3624 C CA  . ALA A 1 459 ? -38.521 7.348  -35.436 1.00 47.98  ? 460  ALA A CA  1 
ATOM   3625 C C   . ALA A 1 459 ? -37.807 8.566  -34.830 1.00 39.83  ? 460  ALA A C   1 
ATOM   3626 O O   . ALA A 1 459 ? -38.007 8.892  -33.686 1.00 37.86  ? 460  ALA A O   1 
ATOM   3627 C CB  . ALA A 1 459 ? -37.638 6.094  -35.266 1.00 41.11  ? 460  ALA A CB  1 
ATOM   3628 N N   . GLU A 1 460 ? -36.930 9.208  -35.567 1.00 44.47  ? 461  GLU A N   1 
ATOM   3629 C CA  . GLU A 1 460 ? -36.202 10.371 -35.001 1.00 46.32  ? 461  GLU A CA  1 
ATOM   3630 C C   . GLU A 1 460 ? -37.143 11.623 -34.843 1.00 43.86  ? 461  GLU A C   1 
ATOM   3631 O O   . GLU A 1 460 ? -36.919 12.461 -33.934 1.00 36.36  ? 461  GLU A O   1 
ATOM   3632 C CB  . GLU A 1 460 ? -34.866 10.682 -35.743 1.00 52.68  ? 461  GLU A CB  1 
ATOM   3633 C CG  . GLU A 1 460 ? -34.857 10.383 -37.223 1.00 67.47  ? 461  GLU A CG  1 
ATOM   3634 C CD  . GLU A 1 460 ? -34.610 8.903  -37.517 1.00 66.41  ? 461  GLU A CD  1 
ATOM   3635 O OE1 . GLU A 1 460 ? -33.478 8.479  -37.278 1.00 72.39  ? 461  GLU A OE1 1 
ATOM   3636 O OE2 . GLU A 1 460 ? -35.542 8.168  -37.961 1.00 62.00  ? 461  GLU A OE2 1 
ATOM   3637 N N   . GLU A 1 461 ? -38.197 11.681 -35.667 1.00 34.77  ? 462  GLU A N   1 
ATOM   3638 C CA  . GLU A 1 461 ? -39.264 12.636 -35.523 1.00 39.30  ? 462  GLU A CA  1 
ATOM   3639 C C   . GLU A 1 461 ? -40.187 12.314 -34.342 1.00 45.38  ? 462  GLU A C   1 
ATOM   3640 O O   . GLU A 1 461 ? -40.788 13.220 -33.729 1.00 38.98  ? 462  GLU A O   1 
ATOM   3641 C CB  . GLU A 1 461 ? -40.110 12.684 -36.822 1.00 36.67  ? 462  GLU A CB  1 
ATOM   3642 C CG  . GLU A 1 461 ? -39.354 13.389 -37.908 1.00 33.95  ? 462  GLU A CG  1 
ATOM   3643 C CD  . GLU A 1 461 ? -39.989 13.425 -39.298 1.00 34.71  ? 462  GLU A CD  1 
ATOM   3644 O OE1 . GLU A 1 461 ? -40.879 12.611 -39.646 1.00 37.06  ? 462  GLU A OE1 1 
ATOM   3645 O OE2 . GLU A 1 461 ? -39.535 14.316 -40.058 1.00 31.07  ? 462  GLU A OE2 1 
ATOM   3646 N N   . GLU A 1 462 ? -40.333 11.027 -34.025 1.00 45.53  ? 463  GLU A N   1 
ATOM   3647 C CA  . GLU A 1 462 ? -41.073 10.654 -32.818 1.00 43.45  ? 463  GLU A CA  1 
ATOM   3648 C C   . GLU A 1 462 ? -40.266 11.139 -31.637 1.00 40.07  ? 463  GLU A C   1 
ATOM   3649 O O   . GLU A 1 462 ? -40.788 11.794 -30.736 1.00 40.50  ? 463  GLU A O   1 
ATOM   3650 C CB  . GLU A 1 462 ? -41.344 9.160  -32.710 1.00 48.61  ? 463  GLU A CB  1 
ATOM   3651 C CG  . GLU A 1 462 ? -41.873 8.761  -31.319 1.00 54.48  ? 463  GLU A CG  1 
ATOM   3652 C CD  . GLU A 1 462 ? -42.325 7.304  -31.189 1.00 53.48  ? 463  GLU A CD  1 
ATOM   3653 O OE1 . GLU A 1 462 ? -42.118 6.489  -32.110 1.00 54.75  ? 463  GLU A OE1 1 
ATOM   3654 O OE2 . GLU A 1 462 ? -42.895 6.971  -30.130 1.00 57.33  ? 463  GLU A OE2 1 
ATOM   3655 N N   . ALA A 1 463 ? -38.980 10.875 -31.670 1.00 32.60  ? 464  ALA A N   1 
ATOM   3656 C CA  . ALA A 1 463 ? -38.156 11.264 -30.564 1.00 37.71  ? 464  ALA A CA  1 
ATOM   3657 C C   . ALA A 1 463 ? -38.118 12.798 -30.418 1.00 43.78  ? 464  ALA A C   1 
ATOM   3658 O O   . ALA A 1 463 ? -37.935 13.325 -29.305 1.00 38.07  ? 464  ALA A O   1 
ATOM   3659 C CB  . ALA A 1 463 ? -36.722 10.706 -30.716 1.00 34.39  ? 464  ALA A CB  1 
ATOM   3660 N N   . LEU A 1 464 ? -38.235 13.524 -31.536 1.00 37.88  ? 465  LEU A N   1 
ATOM   3661 C CA  . LEU A 1 464 ? -38.093 14.981 -31.436 1.00 35.53  ? 465  LEU A CA  1 
ATOM   3662 C C   . LEU A 1 464 ? -39.365 15.552 -30.786 1.00 30.10  ? 465  LEU A C   1 
ATOM   3663 O O   . LEU A 1 464 ? -39.340 16.413 -29.888 1.00 31.53  ? 465  LEU A O   1 
ATOM   3664 C CB  . LEU A 1 464 ? -37.814 15.581 -32.841 1.00 34.82  ? 465  LEU A CB  1 
ATOM   3665 C CG  . LEU A 1 464 ? -38.067 17.049 -32.945 1.00 34.80  ? 465  LEU A CG  1 
ATOM   3666 C CD1 . LEU A 1 464 ? -37.107 17.814 -32.040 1.00 36.32  ? 465  LEU A CD1 1 
ATOM   3667 C CD2 . LEU A 1 464 ? -37.913 17.453 -34.393 1.00 40.40  ? 465  LEU A CD2 1 
ATOM   3668 N N   . SER A 1 465 ? -40.475 15.040 -31.254 1.00 25.79  ? 466  SER A N   1 
ATOM   3669 C CA  . SER A 1 465 ? -41.750 15.334 -30.682 1.00 27.64  ? 466  SER A CA  1 
ATOM   3670 C C   . SER A 1 465 ? -41.792 15.051 -29.187 1.00 33.40  ? 466  SER A C   1 
ATOM   3671 O O   . SER A 1 465 ? -42.196 15.936 -28.415 1.00 39.18  ? 466  SER A O   1 
ATOM   3672 C CB  . SER A 1 465 ? -42.826 14.582 -31.392 1.00 25.30  ? 466  SER A CB  1 
ATOM   3673 O OG  . SER A 1 465 ? -44.107 14.922 -30.924 1.00 27.71  ? 466  SER A OG  1 
ATOM   3674 N N   . ARG A 1 466 ? -41.362 13.874 -28.757 1.00 38.89  ? 467  ARG A N   1 
ATOM   3675 C CA  . ARG A 1 466 ? -41.388 13.533 -27.295 1.00 40.12  ? 467  ARG A CA  1 
ATOM   3676 C C   . ARG A 1 466 ? -40.552 14.536 -26.503 1.00 34.90  ? 467  ARG A C   1 
ATOM   3677 O O   . ARG A 1 466 ? -40.921 15.028 -25.464 1.00 39.14  ? 467  ARG A O   1 
ATOM   3678 C CB  . ARG A 1 466 ? -40.864 12.116 -27.044 1.00 39.76  ? 467  ARG A CB  1 
ATOM   3679 C CG  . ARG A 1 466 ? -41.815 11.018 -27.516 1.00 38.33  ? 467  ARG A CG  1 
ATOM   3680 C CD  . ARG A 1 466 ? -41.328 9.603  -27.118 1.00 37.86  ? 467  ARG A CD  1 
ATOM   3681 N NE  . ARG A 1 466 ? -42.337 8.600  -27.458 1.00 33.82  ? 467  ARG A NE  1 
ATOM   3682 C CZ  . ARG A 1 466 ? -43.418 8.370  -26.749 1.00 36.52  ? 467  ARG A CZ  1 
ATOM   3683 N NH1 . ARG A 1 466 ? -43.611 9.037  -25.625 1.00 34.28  ? 467  ARG A NH1 1 
ATOM   3684 N NH2 . ARG A 1 466 ? -44.357 7.513  -27.184 1.00 39.12  ? 467  ARG A NH2 1 
ATOM   3685 N N   . ARG A 1 467 ? -39.451 14.914 -27.070 1.00 32.32  ? 468  ARG A N   1 
ATOM   3686 C CA  . ARG A 1 467 ? -38.585 15.866 -26.432 1.00 35.14  ? 468  ARG A CA  1 
ATOM   3687 C C   . ARG A 1 467 ? -39.208 17.295 -26.393 1.00 34.94  ? 468  ARG A C   1 
ATOM   3688 O O   . ARG A 1 467 ? -39.088 18.020 -25.424 1.00 30.30  ? 468  ARG A O   1 
ATOM   3689 C CB  . ARG A 1 467 ? -37.331 15.880 -27.248 1.00 38.10  ? 468  ARG A CB  1 
ATOM   3690 C CG  . ARG A 1 467 ? -36.075 16.213 -26.526 1.00 45.87  ? 468  ARG A CG  1 
ATOM   3691 C CD  . ARG A 1 467 ? -34.928 15.973 -27.506 1.00 52.20  ? 468  ARG A CD  1 
ATOM   3692 N NE  . ARG A 1 467 ? -34.338 17.260 -27.847 1.00 62.77  ? 468  ARG A NE  1 
ATOM   3693 C CZ  . ARG A 1 467 ? -33.972 17.640 -29.058 1.00 62.70  ? 468  ARG A CZ  1 
ATOM   3694 N NH1 . ARG A 1 467 ? -34.142 16.808 -30.089 1.00 59.71  ? 468  ARG A NH1 1 
ATOM   3695 N NH2 . ARG A 1 467 ? -33.414 18.858 -29.211 1.00 63.34  ? 468  ARG A NH2 1 
ATOM   3696 N N   . ILE A 1 468 ? -39.894 17.687 -27.454 1.00 30.67  ? 469  ILE A N   1 
ATOM   3697 C CA  . ILE A 1 468 ? -40.540 18.989 -27.446 1.00 30.38  ? 469  ILE A CA  1 
ATOM   3698 C C   . ILE A 1 468 ? -41.678 18.995 -26.478 1.00 27.65  ? 469  ILE A C   1 
ATOM   3699 O O   . ILE A 1 468 ? -41.889 19.948 -25.710 1.00 29.97  ? 469  ILE A O   1 
ATOM   3700 C CB  . ILE A 1 468 ? -40.997 19.403 -28.890 1.00 28.36  ? 469  ILE A CB  1 
ATOM   3701 C CG1 . ILE A 1 468 ? -39.772 19.870 -29.670 1.00 27.49  ? 469  ILE A CG1 1 
ATOM   3702 C CG2 . ILE A 1 468 ? -42.034 20.481 -28.868 1.00 28.72  ? 469  ILE A CG2 1 
ATOM   3703 C CD1 . ILE A 1 468 ? -40.020 19.938 -31.166 1.00 29.89  ? 469  ILE A CD1 1 
ATOM   3704 N N   . MET A 1 469 ? -42.443 17.938 -26.495 1.00 30.68  ? 470  MET A N   1 
ATOM   3705 C CA  . MET A 1 469 ? -43.596 17.897 -25.600 1.00 32.51  ? 470  MET A CA  1 
ATOM   3706 C C   . MET A 1 469 ? -43.129 17.984 -24.136 1.00 35.65  ? 470  MET A C   1 
ATOM   3707 O O   . MET A 1 469 ? -43.821 18.548 -23.286 1.00 31.08  ? 470  MET A O   1 
ATOM   3708 C CB  . MET A 1 469 ? -44.390 16.616 -25.789 1.00 31.83  ? 470  MET A CB  1 
ATOM   3709 C CG  . MET A 1 469 ? -45.336 16.638 -26.918 1.00 31.24  ? 470  MET A CG  1 
ATOM   3710 S SD  . MET A 1 469 ? -46.526 15.273 -26.948 1.00 39.41  ? 470  MET A SD  1 
ATOM   3711 C CE  . MET A 1 469 ? -45.400 13.964 -27.288 1.00 32.69  ? 470  MET A CE  1 
ATOM   3712 N N   . HIS A 1 470 ? -41.996 17.356 -23.851 1.00 33.31  ? 471  HIS A N   1 
ATOM   3713 C CA  . HIS A 1 470 ? -41.538 17.275 -22.507 1.00 35.54  ? 471  HIS A CA  1 
ATOM   3714 C C   . HIS A 1 470 ? -40.893 18.613 -22.132 1.00 33.41  ? 471  HIS A C   1 
ATOM   3715 O O   . HIS A 1 470 ? -41.077 19.064 -21.019 1.00 31.02  ? 471  HIS A O   1 
ATOM   3716 C CB  . HIS A 1 470 ? -40.595 16.063 -22.307 1.00 39.71  ? 471  HIS A CB  1 
ATOM   3717 C CG  . HIS A 1 470 ? -40.264 15.797 -20.870 1.00 45.53  ? 471  HIS A CG  1 
ATOM   3718 N ND1 . HIS A 1 470 ? -41.242 15.519 -19.924 1.00 46.02  ? 471  HIS A ND1 1 
ATOM   3719 C CD2 . HIS A 1 470 ? -39.082 15.815 -20.199 1.00 40.83  ? 471  HIS A CD2 1 
ATOM   3720 C CE1 . HIS A 1 470 ? -40.672 15.361 -18.741 1.00 40.28  ? 471  HIS A CE1 1 
ATOM   3721 N NE2 . HIS A 1 470 ? -39.369 15.543 -18.874 1.00 39.67  ? 471  HIS A NE2 1 
ATOM   3722 N N   . TYR A 1 471 ? -40.149 19.254 -23.032 1.00 31.43  ? 472  TYR A N   1 
ATOM   3723 C CA  . TYR A 1 471 ? -39.755 20.656 -22.780 1.00 32.95  ? 472  TYR A CA  1 
ATOM   3724 C C   . TYR A 1 471 ? -40.982 21.565 -22.479 1.00 33.69  ? 472  TYR A C   1 
ATOM   3725 O O   . TYR A 1 471 ? -40.945 22.365 -21.557 1.00 35.13  ? 472  TYR A O   1 
ATOM   3726 C CB  . TYR A 1 471 ? -39.088 21.267 -23.950 1.00 32.79  ? 472  TYR A CB  1 
ATOM   3727 C CG  . TYR A 1 471 ? -37.681 20.813 -24.266 1.00 37.34  ? 472  TYR A CG  1 
ATOM   3728 C CD1 . TYR A 1 471 ? -36.741 20.549 -23.266 1.00 42.10  ? 472  TYR A CD1 1 
ATOM   3729 C CD2 . TYR A 1 471 ? -37.257 20.733 -25.602 1.00 40.08  ? 472  TYR A CD2 1 
ATOM   3730 C CE1 . TYR A 1 471 ? -35.428 20.177 -23.577 1.00 37.72  ? 472  TYR A CE1 1 
ATOM   3731 C CE2 . TYR A 1 471 ? -35.975 20.372 -25.918 1.00 39.98  ? 472  TYR A CE2 1 
ATOM   3732 C CZ  . TYR A 1 471 ? -35.076 20.090 -24.893 1.00 41.12  ? 472  TYR A CZ  1 
ATOM   3733 O OH  . TYR A 1 471 ? -33.838 19.705 -25.226 1.00 47.35  ? 472  TYR A OH  1 
ATOM   3734 N N   . TRP A 1 472 ? -42.029 21.445 -23.288 1.00 30.24  ? 473  TRP A N   1 
ATOM   3735 C CA  . TRP A 1 472 ? -43.198 22.311 -23.158 1.00 30.58  ? 473  TRP A CA  1 
ATOM   3736 C C   . TRP A 1 472 ? -43.929 22.096 -21.837 1.00 31.87  ? 473  TRP A C   1 
ATOM   3737 O O   . TRP A 1 472 ? -44.334 23.052 -21.174 1.00 29.06  ? 473  TRP A O   1 
ATOM   3738 C CB  . TRP A 1 472 ? -44.158 22.092 -24.330 1.00 28.13  ? 473  TRP A CB  1 
ATOM   3739 C CG  . TRP A 1 472 ? -44.046 23.133 -25.400 1.00 31.89  ? 473  TRP A CG  1 
ATOM   3740 C CD1 . TRP A 1 472 ? -45.039 23.950 -25.857 1.00 30.16  ? 473  TRP A CD1 1 
ATOM   3741 C CD2 . TRP A 1 472 ? -42.873 23.471 -26.151 1.00 26.62  ? 473  TRP A CD2 1 
ATOM   3742 N NE1 . TRP A 1 472 ? -44.558 24.775 -26.844 1.00 27.76  ? 473  TRP A NE1 1 
ATOM   3743 C CE2 . TRP A 1 472 ? -43.230 24.500 -27.044 1.00 28.03  ? 473  TRP A CE2 1 
ATOM   3744 C CE3 . TRP A 1 472 ? -41.556 23.002 -26.155 1.00 26.67  ? 473  TRP A CE3 1 
ATOM   3745 C CZ2 . TRP A 1 472 ? -42.319 25.069 -27.931 1.00 28.32  ? 473  TRP A CZ2 1 
ATOM   3746 C CZ3 . TRP A 1 472 ? -40.652 23.568 -27.036 1.00 26.05  ? 473  TRP A CZ3 1 
ATOM   3747 C CH2 . TRP A 1 472 ? -41.038 24.590 -27.911 1.00 28.58  ? 473  TRP A CH2 1 
ATOM   3748 N N   . ALA A 1 473 ? -44.095 20.833 -21.465 1.00 29.69  ? 474  ALA A N   1 
ATOM   3749 C CA  . ALA A 1 473 ? -44.809 20.463 -20.246 1.00 30.38  ? 474  ALA A CA  1 
ATOM   3750 C C   . ALA A 1 473 ? -43.985 20.687 -19.004 1.00 28.71  ? 474  ALA A C   1 
ATOM   3751 O O   . ALA A 1 473 ? -44.500 21.167 -18.056 1.00 27.59  ? 474  ALA A O   1 
ATOM   3752 C CB  . ALA A 1 473 ? -45.287 19.051 -20.285 1.00 31.99  ? 474  ALA A CB  1 
ATOM   3753 N N   . THR A 1 474 ? -42.698 20.413 -19.035 1.00 31.28  ? 475  THR A N   1 
ATOM   3754 C CA  . THR A 1 474 ? -41.860 20.685 -17.888 1.00 29.77  ? 475  THR A CA  1 
ATOM   3755 C C   . THR A 1 474 ? -41.761 22.172 -17.648 1.00 34.79  ? 475  THR A C   1 
ATOM   3756 O O   . THR A 1 474 ? -41.732 22.667 -16.485 1.00 37.60  ? 475  THR A O   1 
ATOM   3757 C CB  . THR A 1 474 ? -40.477 20.106 -18.102 1.00 29.99  ? 475  THR A CB  1 
ATOM   3758 O OG1 . THR A 1 474 ? -40.611 18.703 -18.410 1.00 28.17  ? 475  THR A OG1 1 
ATOM   3759 C CG2 . THR A 1 474 ? -39.601 20.322 -16.922 1.00 29.46  ? 475  THR A CG2 1 
ATOM   3760 N N   . PHE A 1 475 ? -41.695 22.922 -18.731 1.00 35.38  ? 476  PHE A N   1 
ATOM   3761 C CA  . PHE A 1 475 ? -41.730 24.370 -18.567 1.00 29.62  ? 476  PHE A CA  1 
ATOM   3762 C C   . PHE A 1 475 ? -43.076 24.806 -18.001 1.00 27.74  ? 476  PHE A C   1 
ATOM   3763 O O   . PHE A 1 475 ? -43.122 25.729 -17.185 1.00 26.73  ? 476  PHE A O   1 
ATOM   3764 C CB  . PHE A 1 475 ? -41.453 25.063 -19.888 1.00 33.11  ? 476  PHE A CB  1 
ATOM   3765 C CG  . PHE A 1 475 ? -41.740 26.518 -19.865 1.00 30.42  ? 476  PHE A CG  1 
ATOM   3766 C CD1 . PHE A 1 475 ? -40.800 27.388 -19.391 1.00 30.80  ? 476  PHE A CD1 1 
ATOM   3767 C CD2 . PHE A 1 475 ? -42.981 26.981 -20.236 1.00 29.04  ? 476  PHE A CD2 1 
ATOM   3768 C CE1 . PHE A 1 475 ? -41.065 28.728 -19.319 1.00 29.53  ? 476  PHE A CE1 1 
ATOM   3769 C CE2 . PHE A 1 475 ? -43.256 28.312 -20.144 1.00 31.31  ? 476  PHE A CE2 1 
ATOM   3770 C CZ  . PHE A 1 475 ? -42.291 29.187 -19.724 1.00 29.45  ? 476  PHE A CZ  1 
ATOM   3771 N N   . ALA A 1 476 ? -44.190 24.191 -18.405 1.00 25.32  ? 477  ALA A N   1 
ATOM   3772 C CA  . ALA A 1 476 ? -45.471 24.676 -17.895 1.00 29.05  ? 477  ALA A CA  1 
ATOM   3773 C C   . ALA A 1 476 ? -45.582 24.463 -16.361 1.00 36.58  ? 477  ALA A C   1 
ATOM   3774 O O   . ALA A 1 476 ? -46.154 25.288 -15.615 1.00 31.55  ? 477  ALA A O   1 
ATOM   3775 C CB  . ALA A 1 476 ? -46.651 24.033 -18.608 1.00 28.96  ? 477  ALA A CB  1 
ATOM   3776 N N   . LYS A 1 477 ? -44.987 23.353 -15.944 1.00 40.71  ? 478  LYS A N   1 
ATOM   3777 C CA  . LYS A 1 477 ? -45.083 22.855 -14.610 1.00 46.71  ? 478  LYS A CA  1 
ATOM   3778 C C   . LYS A 1 477 ? -44.127 23.617 -13.672 1.00 44.19  ? 478  LYS A C   1 
ATOM   3779 O O   . LYS A 1 477 ? -44.529 23.990 -12.556 1.00 36.42  ? 478  LYS A O   1 
ATOM   3780 C CB  . LYS A 1 477 ? -44.772 21.358 -14.637 1.00 54.63  ? 478  LYS A CB  1 
ATOM   3781 C CG  . LYS A 1 477 ? -44.793 20.667 -13.272 1.00 70.13  ? 478  LYS A CG  1 
ATOM   3782 C CD  . LYS A 1 477 ? -44.699 19.148 -13.426 1.00 76.71  ? 478  LYS A CD  1 
ATOM   3783 C CE  . LYS A 1 477 ? -43.263 18.627 -13.312 1.00 79.47  ? 478  LYS A CE  1 
ATOM   3784 N NZ  . LYS A 1 477 ? -42.942 18.222 -11.914 1.00 80.42  ? 478  LYS A NZ  1 
ATOM   3785 N N   . THR A 1 478 ? -42.889 23.836 -14.134 1.00 35.81  ? 479  THR A N   1 
ATOM   3786 C CA  . THR A 1 478 ? -41.872 24.408 -13.320 1.00 31.40  ? 479  THR A CA  1 
ATOM   3787 C C   . THR A 1 478 ? -41.350 25.775 -13.720 1.00 36.30  ? 479  THR A C   1 
ATOM   3788 O O   . THR A 1 478 ? -40.685 26.384 -12.929 1.00 36.09  ? 479  THR A O   1 
ATOM   3789 C CB  . THR A 1 478 ? -40.633 23.529 -13.288 1.00 32.19  ? 479  THR A CB  1 
ATOM   3790 O OG1 . THR A 1 478 ? -39.901 23.635 -14.508 1.00 31.39  ? 479  THR A OG1 1 
ATOM   3791 C CG2 . THR A 1 478 ? -40.979 22.041 -12.993 1.00 32.44  ? 479  THR A CG2 1 
ATOM   3792 N N   . GLY A 1 479 ? -41.541 26.237 -14.956 1.00 33.03  ? 480  GLY A N   1 
ATOM   3793 C CA  . GLY A 1 479 ? -40.936 27.491 -15.378 1.00 30.42  ? 480  GLY A CA  1 
ATOM   3794 C C   . GLY A 1 479 ? -39.598 27.327 -15.987 1.00 27.55  ? 480  GLY A C   1 
ATOM   3795 O O   . GLY A 1 479 ? -38.917 28.300 -16.334 1.00 28.00  ? 480  GLY A O   1 
ATOM   3796 N N   . ASN A 1 480 ? -39.235 26.068 -16.187 1.00 32.74  ? 481  ASN A N   1 
ATOM   3797 C CA  . ASN A 1 480 ? -37.964 25.698 -16.816 1.00 31.89  ? 481  ASN A CA  1 
ATOM   3798 C C   . ASN A 1 480 ? -38.147 24.422 -17.679 1.00 30.86  ? 481  ASN A C   1 
ATOM   3799 O O   . ASN A 1 480 ? -38.648 23.419 -17.176 1.00 35.26  ? 481  ASN A O   1 
ATOM   3800 C CB  . ASN A 1 480 ? -36.950 25.479 -15.696 1.00 35.82  ? 481  ASN A CB  1 
ATOM   3801 C CG  . ASN A 1 480 ? -35.592 25.115 -16.206 1.00 39.16  ? 481  ASN A CG  1 
ATOM   3802 O OD1 . ASN A 1 480 ? -35.427 24.591 -17.312 1.00 42.87  ? 481  ASN A OD1 1 
ATOM   3803 N ND2 . ASN A 1 480 ? -34.607 25.398 -15.414 1.00 40.35  ? 481  ASN A ND2 1 
ATOM   3804 N N   . PRO A 1 481 ? -37.803 24.461 -18.988 1.00 32.40  ? 482  PRO A N   1 
ATOM   3805 C CA  . PRO A 1 481 ? -38.040 23.261 -19.839 1.00 39.14  ? 482  PRO A CA  1 
ATOM   3806 C C   . PRO A 1 481 ? -37.143 22.045 -19.468 1.00 34.64  ? 482  PRO A C   1 
ATOM   3807 O O   . PRO A 1 481 ? -37.412 20.898 -19.866 1.00 34.00  ? 482  PRO A O   1 
ATOM   3808 C CB  . PRO A 1 481 ? -37.669 23.753 -21.254 1.00 35.32  ? 482  PRO A CB  1 
ATOM   3809 C CG  . PRO A 1 481 ? -36.614 24.778 -20.980 1.00 35.63  ? 482  PRO A CG  1 
ATOM   3810 C CD  . PRO A 1 481 ? -37.064 25.493 -19.731 1.00 32.62  ? 482  PRO A CD  1 
ATOM   3811 N N   . ASN A 1 482 ? -36.061 22.333 -18.764 1.00 32.84  ? 483  ASN A N   1 
ATOM   3812 C CA  . ASN A 1 482 ? -35.082 21.309 -18.382 1.00 36.94  ? 483  ASN A CA  1 
ATOM   3813 C C   . ASN A 1 482 ? -35.485 20.552 -17.099 1.00 36.31  ? 483  ASN A C   1 
ATOM   3814 O O   . ASN A 1 482 ? -35.986 21.137 -16.114 1.00 34.39  ? 483  ASN A O   1 
ATOM   3815 C CB  . ASN A 1 482 ? -33.760 21.968 -18.124 1.00 36.13  ? 483  ASN A CB  1 
ATOM   3816 C CG  . ASN A 1 482 ? -33.227 22.682 -19.335 1.00 38.03  ? 483  ASN A CG  1 
ATOM   3817 O OD1 . ASN A 1 482 ? -32.741 22.044 -20.294 1.00 38.68  ? 483  ASN A OD1 1 
ATOM   3818 N ND2 . ASN A 1 482 ? -33.237 24.013 -19.270 1.00 33.80  ? 483  ASN A ND2 1 
ATOM   3819 N N   . GLU A 1 483 ? -35.314 19.256 -17.102 1.00 45.76  ? 484  GLU A N   1 
ATOM   3820 C CA  . GLU A 1 483 ? -35.646 18.497 -15.865 1.00 58.64  ? 484  GLU A CA  1 
ATOM   3821 C C   . GLU A 1 483 ? -34.502 18.653 -14.864 1.00 52.75  ? 484  GLU A C   1 
ATOM   3822 O O   . GLU A 1 483 ? -33.317 18.505 -15.254 1.00 46.24  ? 484  GLU A O   1 
ATOM   3823 C CB  . GLU A 1 483 ? -35.957 17.035 -16.159 1.00 65.91  ? 484  GLU A CB  1 
ATOM   3824 C CG  . GLU A 1 483 ? -36.800 16.359 -15.084 1.00 72.07  ? 484  GLU A CG  1 
ATOM   3825 C CD  . GLU A 1 483 ? -37.892 15.539 -15.692 1.00 74.92  ? 484  GLU A CD  1 
ATOM   3826 O OE1 . GLU A 1 483 ? -39.016 15.570 -15.159 1.00 100.38 ? 484  GLU A OE1 1 
ATOM   3827 O OE2 . GLU A 1 483 ? -37.648 14.912 -16.739 1.00 71.13  ? 484  GLU A OE2 1 
ATOM   3828 N N   . PRO A 1 484 ? -34.843 19.018 -13.599 0.50 49.91  ? 485  PRO A N   1 
ATOM   3829 C CA  . PRO A 1 484 ? -33.805 19.252 -12.605 0.50 48.45  ? 485  PRO A CA  1 
ATOM   3830 C C   . PRO A 1 484 ? -32.973 17.989 -12.465 0.50 44.36  ? 485  PRO A C   1 
ATOM   3831 O O   . PRO A 1 484 ? -33.549 16.889 -12.353 0.50 41.40  ? 485  PRO A O   1 
ATOM   3832 C CB  . PRO A 1 484 ? -34.612 19.503 -11.324 0.50 48.30  ? 485  PRO A CB  1 
ATOM   3833 C CG  . PRO A 1 484 ? -35.845 18.684 -11.525 0.50 48.30  ? 485  PRO A CG  1 
ATOM   3834 C CD  . PRO A 1 484 ? -36.174 18.941 -12.963 0.50 49.05  ? 485  PRO A CD  1 
ATOM   3835 N N   . HIS A 1 485 ? -31.656 18.153 -12.555 0.50 42.29  ? 486  HIS A N   1 
ATOM   3836 C CA  . HIS A 1 485 ? -30.665 17.093 -12.318 0.50 44.78  ? 486  HIS A CA  1 
ATOM   3837 C C   . HIS A 1 485 ? -30.576 15.986 -13.370 0.50 44.26  ? 486  HIS A C   1 
ATOM   3838 O O   . HIS A 1 485 ? -29.769 15.078 -13.199 0.50 45.02  ? 486  HIS A O   1 
ATOM   3839 C CB  . HIS A 1 485 ? -30.816 16.410 -10.927 0.50 48.87  ? 486  HIS A CB  1 
ATOM   3840 C CG  . HIS A 1 485 ? -31.042 17.353 -9.776  0.50 52.89  ? 486  HIS A CG  1 
ATOM   3841 N ND1 . HIS A 1 485 ? -30.299 18.501 -9.583  0.50 57.73  ? 486  HIS A ND1 1 
ATOM   3842 C CD2 . HIS A 1 485 ? -31.929 17.303 -8.747  0.50 51.57  ? 486  HIS A CD2 1 
ATOM   3843 C CE1 . HIS A 1 485 ? -30.729 19.126 -8.497  0.50 57.50  ? 486  HIS A CE1 1 
ATOM   3844 N NE2 . HIS A 1 485 ? -31.717 18.419 -7.972  0.50 54.57  ? 486  HIS A NE2 1 
ATOM   3845 N N   . SER A 1 486 ? -31.367 16.017 -14.438 0.50 43.62  ? 487  SER A N   1 
ATOM   3846 C CA  . SER A 1 486 ? -31.210 15.016 -15.517 0.50 43.19  ? 487  SER A CA  1 
ATOM   3847 C C   . SER A 1 486 ? -29.853 15.088 -16.212 0.50 40.83  ? 487  SER A C   1 
ATOM   3848 O O   . SER A 1 486 ? -29.084 15.978 -15.946 0.50 41.26  ? 487  SER A O   1 
ATOM   3849 C CB  . SER A 1 486 ? -32.311 15.167 -16.556 0.50 43.49  ? 487  SER A CB  1 
ATOM   3850 O OG  . SER A 1 486 ? -31.766 15.427 -17.839 0.50 44.02  ? 487  SER A OG  1 
ATOM   3851 N N   . GLN A 1 487 ? -29.578 14.148 -17.110 0.50 46.51  ? 488  GLN A N   1 
ATOM   3852 C CA  . GLN A 1 487 ? -28.291 14.084 -17.857 0.50 49.59  ? 488  GLN A CA  1 
ATOM   3853 C C   . GLN A 1 487 ? -28.319 14.646 -19.290 0.50 46.21  ? 488  GLN A C   1 
ATOM   3854 O O   . GLN A 1 487 ? -27.283 14.715 -19.960 0.50 39.12  ? 488  GLN A O   1 
ATOM   3855 C CB  . GLN A 1 487 ? -27.807 12.631 -17.951 0.50 52.54  ? 488  GLN A CB  1 
ATOM   3856 C CG  . GLN A 1 487 ? -27.557 11.959 -16.606 0.50 55.79  ? 488  GLN A CG  1 
ATOM   3857 C CD  . GLN A 1 487 ? -26.253 12.400 -15.970 0.50 55.89  ? 488  GLN A CD  1 
ATOM   3858 O OE1 . GLN A 1 487 ? -25.181 12.062 -16.449 0.50 57.31  ? 488  GLN A OE1 1 
ATOM   3859 N NE2 . GLN A 1 487 ? -26.342 13.154 -14.883 0.50 55.23  ? 488  GLN A NE2 1 
ATOM   3860 N N   . GLU A 1 488 ? -29.502 15.030 -19.756 0.50 44.81  ? 489  GLU A N   1 
ATOM   3861 C CA  . GLU A 1 488 ? -29.654 15.579 -21.095 0.50 43.60  ? 489  GLU A CA  1 
ATOM   3862 C C   . GLU A 1 488 ? -28.925 16.882 -21.224 0.50 42.81  ? 489  GLU A C   1 
ATOM   3863 O O   . GLU A 1 488 ? -28.549 17.520 -20.254 0.50 35.70  ? 489  GLU A O   1 
ATOM   3864 C CB  . GLU A 1 488 ? -31.115 15.863 -21.402 0.50 46.46  ? 489  GLU A CB  1 
ATOM   3865 C CG  . GLU A 1 488 ? -32.054 14.750 -21.019 0.50 48.24  ? 489  GLU A CG  1 
ATOM   3866 C CD  . GLU A 1 488 ? -31.485 13.457 -21.492 0.50 51.20  ? 489  GLU A CD  1 
ATOM   3867 O OE1 . GLU A 1 488 ? -30.700 13.540 -22.450 0.50 50.95  ? 489  GLU A OE1 1 
ATOM   3868 O OE2 . GLU A 1 488 ? -31.780 12.399 -20.897 0.50 53.92  ? 489  GLU A OE2 1 
ATOM   3869 N N   . SER A 1 489 ? -28.769 17.308 -22.458 1.00 51.69  ? 490  SER A N   1 
ATOM   3870 C CA  . SER A 1 489 ? -28.178 18.641 -22.722 1.00 58.38  ? 490  SER A CA  1 
ATOM   3871 C C   . SER A 1 489 ? -29.202 19.698 -22.321 1.00 49.88  ? 490  SER A C   1 
ATOM   3872 O O   . SER A 1 489 ? -30.403 19.492 -22.507 1.00 46.99  ? 490  SER A O   1 
ATOM   3873 C CB  . SER A 1 489 ? -27.802 18.834 -24.190 1.00 55.88  ? 490  SER A CB  1 
ATOM   3874 O OG  . SER A 1 489 ? -27.164 17.681 -24.691 1.00 66.98  ? 490  SER A OG  1 
ATOM   3875 N N   . LYS A 1 490 ? -28.705 20.810 -21.790 1.00 43.42  ? 491  LYS A N   1 
ATOM   3876 C CA  . LYS A 1 490 ? -29.497 21.730 -21.056 1.00 49.63  ? 491  LYS A CA  1 
ATOM   3877 C C   . LYS A 1 490 ? -29.838 22.893 -21.982 1.00 52.23  ? 491  LYS A C   1 
ATOM   3878 O O   . LYS A 1 490 ? -28.919 23.457 -22.574 1.00 42.75  ? 491  LYS A O   1 
ATOM   3879 C CB  . LYS A 1 490 ? -28.729 22.227 -19.835 1.00 59.49  ? 491  LYS A CB  1 
ATOM   3880 C CG  . LYS A 1 490 ? -28.961 21.390 -18.567 1.00 70.87  ? 491  LYS A CG  1 
ATOM   3881 C CD  . LYS A 1 490 ? -29.270 22.264 -17.335 1.00 82.32  ? 491  LYS A CD  1 
ATOM   3882 C CE  . LYS A 1 490 ? -28.011 22.778 -16.634 1.00 89.15  ? 491  LYS A CE  1 
ATOM   3883 N NZ  . LYS A 1 490 ? -27.402 21.751 -15.727 1.00 85.42  ? 491  LYS A NZ  1 
ATOM   3884 N N   . TRP A 1 491 ? -31.144 23.225 -22.110 1.00 36.05  ? 492  TRP A N   1 
ATOM   3885 C CA  . TRP A 1 491 ? -31.545 24.414 -22.807 1.00 32.77  ? 492  TRP A CA  1 
ATOM   3886 C C   . TRP A 1 491 ? -31.209 25.609 -21.938 1.00 32.49  ? 492  TRP A C   1 
ATOM   3887 O O   . TRP A 1 491 ? -31.816 25.838 -20.944 1.00 34.11  ? 492  TRP A O   1 
ATOM   3888 C CB  . TRP A 1 491 ? -33.037 24.297 -23.124 1.00 30.91  ? 492  TRP A CB  1 
ATOM   3889 C CG  . TRP A 1 491 ? -33.686 25.346 -23.993 1.00 29.57  ? 492  TRP A CG  1 
ATOM   3890 C CD1 . TRP A 1 491 ? -33.227 26.640 -24.271 1.00 31.99  ? 492  TRP A CD1 1 
ATOM   3891 C CD2 . TRP A 1 491 ? -34.997 25.268 -24.536 1.00 27.37  ? 492  TRP A CD2 1 
ATOM   3892 N NE1 . TRP A 1 491 ? -34.163 27.313 -25.034 1.00 33.76  ? 492  TRP A NE1 1 
ATOM   3893 C CE2 . TRP A 1 491 ? -35.256 26.491 -25.203 1.00 31.91  ? 492  TRP A CE2 1 
ATOM   3894 C CE3 . TRP A 1 491 ? -35.956 24.268 -24.568 1.00 30.60  ? 492  TRP A CE3 1 
ATOM   3895 C CZ2 . TRP A 1 491 ? -36.453 26.737 -25.884 1.00 30.69  ? 492  TRP A CZ2 1 
ATOM   3896 C CZ3 . TRP A 1 491 ? -37.133 24.492 -25.256 1.00 32.62  ? 492  TRP A CZ3 1 
ATOM   3897 C CH2 . TRP A 1 491 ? -37.376 25.749 -25.917 1.00 29.22  ? 492  TRP A CH2 1 
ATOM   3898 N N   . PRO A 1 492 ? -30.209 26.397 -22.304 1.00 37.59  ? 493  PRO A N   1 
ATOM   3899 C CA  . PRO A 1 492 ? -29.871 27.531 -21.432 1.00 35.81  ? 493  PRO A CA  1 
ATOM   3900 C C   . PRO A 1 492 ? -30.878 28.699 -21.471 1.00 40.69  ? 493  PRO A C   1 
ATOM   3901 O O   . PRO A 1 492 ? -31.627 28.875 -22.431 1.00 38.86  ? 493  PRO A O   1 
ATOM   3902 C CB  . PRO A 1 492 ? -28.509 27.980 -21.956 1.00 37.57  ? 493  PRO A CB  1 
ATOM   3903 C CG  . PRO A 1 492 ? -28.558 27.628 -23.392 1.00 40.46  ? 493  PRO A CG  1 
ATOM   3904 C CD  . PRO A 1 492 ? -29.373 26.364 -23.511 1.00 40.07  ? 493  PRO A CD  1 
ATOM   3905 N N   . LEU A 1 493 ? -30.929 29.432 -20.370 1.00 39.29  ? 494  LEU A N   1 
ATOM   3906 C CA  . LEU A 1 493 ? -31.650 30.671 -20.289 1.00 39.38  ? 494  LEU A CA  1 
ATOM   3907 C C   . LEU A 1 493 ? -31.129 31.684 -21.326 1.00 39.36  ? 494  LEU A C   1 
ATOM   3908 O O   . LEU A 1 493 ? -29.930 31.847 -21.534 1.00 38.73  ? 494  LEU A O   1 
ATOM   3909 C CB  . LEU A 1 493 ? -31.466 31.279 -18.893 1.00 41.40  ? 494  LEU A CB  1 
ATOM   3910 C CG  . LEU A 1 493 ? -32.539 31.754 -17.905 1.00 46.58  ? 494  LEU A CG  1 
ATOM   3911 C CD1 . LEU A 1 493 ? -33.896 31.089 -17.966 1.00 42.86  ? 494  LEU A CD1 1 
ATOM   3912 C CD2 . LEU A 1 493 ? -31.951 31.566 -16.499 1.00 46.24  ? 494  LEU A CD2 1 
ATOM   3913 N N   . PHE A 1 494 ? -32.060 32.414 -21.926 1.00 37.10  ? 495  PHE A N   1 
ATOM   3914 C CA  . PHE A 1 494 ? -31.731 33.531 -22.756 1.00 32.79  ? 495  PHE A CA  1 
ATOM   3915 C C   . PHE A 1 494 ? -31.556 34.708 -21.814 1.00 32.44  ? 495  PHE A C   1 
ATOM   3916 O O   . PHE A 1 494 ? -32.440 35.016 -21.010 1.00 32.48  ? 495  PHE A O   1 
ATOM   3917 C CB  . PHE A 1 494 ? -32.900 33.775 -23.729 1.00 33.46  ? 495  PHE A CB  1 
ATOM   3918 C CG  . PHE A 1 494 ? -32.786 35.064 -24.499 1.00 33.44  ? 495  PHE A CG  1 
ATOM   3919 C CD1 . PHE A 1 494 ? -33.102 36.250 -23.908 1.00 30.68  ? 495  PHE A CD1 1 
ATOM   3920 C CD2 . PHE A 1 494 ? -32.322 35.078 -25.822 1.00 34.46  ? 495  PHE A CD2 1 
ATOM   3921 C CE1 . PHE A 1 494 ? -33.022 37.462 -24.599 1.00 34.86  ? 495  PHE A CE1 1 
ATOM   3922 C CE2 . PHE A 1 494 ? -32.238 36.276 -26.527 1.00 35.92  ? 495  PHE A CE2 1 
ATOM   3923 C CZ  . PHE A 1 494 ? -32.544 37.475 -25.908 1.00 36.62  ? 495  PHE A CZ  1 
ATOM   3924 N N   . THR A 1 495 ? -30.438 35.389 -21.915 1.00 32.01  ? 496  THR A N   1 
ATOM   3925 C CA  . THR A 1 495 ? -30.180 36.584 -21.091 1.00 33.92  ? 496  THR A CA  1 
ATOM   3926 C C   . THR A 1 495 ? -29.842 37.755 -21.979 1.00 34.63  ? 496  THR A C   1 
ATOM   3927 O O   . THR A 1 495 ? -29.351 37.597 -23.090 1.00 34.47  ? 496  THR A O   1 
ATOM   3928 C CB  . THR A 1 495 ? -28.987 36.351 -20.141 1.00 36.23  ? 496  THR A CB  1 
ATOM   3929 O OG1 . THR A 1 495 ? -27.756 36.166 -20.903 1.00 37.90  ? 496  THR A OG1 1 
ATOM   3930 C CG2 . THR A 1 495 ? -29.271 35.084 -19.298 1.00 33.23  ? 496  THR A CG2 1 
ATOM   3931 N N   . THR A 1 496 ? -30.131 38.930 -21.483 1.00 42.58  ? 497  THR A N   1 
ATOM   3932 C CA  . THR A 1 496 ? -29.802 40.167 -22.164 1.00 49.56  ? 497  THR A CA  1 
ATOM   3933 C C   . THR A 1 496 ? -28.381 40.163 -22.674 1.00 52.75  ? 497  THR A C   1 
ATOM   3934 O O   . THR A 1 496 ? -28.131 40.571 -23.794 1.00 52.50  ? 497  THR A O   1 
ATOM   3935 C CB  . THR A 1 496 ? -29.924 41.340 -21.179 1.00 51.95  ? 497  THR A CB  1 
ATOM   3936 O OG1 . THR A 1 496 ? -31.147 41.215 -20.443 1.00 57.81  ? 497  THR A OG1 1 
ATOM   3937 C CG2 . THR A 1 496 ? -29.900 42.630 -21.905 1.00 54.12  ? 497  THR A CG2 1 
ATOM   3938 N N   . LYS A 1 497 ? -27.454 39.668 -21.856 1.00 52.24  ? 498  LYS A N   1 
ATOM   3939 C CA  . LYS A 1 497 ? -26.057 39.737 -22.196 1.00 53.20  ? 498  LYS A CA  1 
ATOM   3940 C C   . LYS A 1 497 ? -25.707 38.738 -23.299 1.00 46.81  ? 498  LYS A C   1 
ATOM   3941 O O   . LYS A 1 497 ? -25.149 39.101 -24.342 1.00 44.97  ? 498  LYS A O   1 
ATOM   3942 C CB  . LYS A 1 497 ? -25.195 39.508 -20.941 1.00 58.71  ? 498  LYS A CB  1 
ATOM   3943 C CG  . LYS A 1 497 ? -23.694 39.648 -21.213 1.00 78.15  ? 498  LYS A CG  1 
ATOM   3944 C CD  . LYS A 1 497 ? -22.884 40.192 -20.032 1.00 90.25  ? 498  LYS A CD  1 
ATOM   3945 C CE  . LYS A 1 497 ? -23.118 41.698 -19.833 1.00 97.72  ? 498  LYS A CE  1 
ATOM   3946 N NZ  . LYS A 1 497 ? -22.190 42.333 -18.850 1.00 98.85  ? 498  LYS A NZ  1 
ATOM   3947 N N   . GLU A 1 498 ? -26.009 37.470 -23.064 1.00 41.84  ? 499  GLU A N   1 
ATOM   3948 C CA  . GLU A 1 498 ? -25.463 36.399 -23.916 1.00 42.01  ? 499  GLU A CA  1 
ATOM   3949 C C   . GLU A 1 498 ? -26.418 35.980 -25.018 1.00 38.25  ? 499  GLU A C   1 
ATOM   3950 O O   . GLU A 1 498 ? -26.010 35.384 -25.969 1.00 32.26  ? 499  GLU A O   1 
ATOM   3951 C CB  . GLU A 1 498 ? -25.106 35.189 -23.074 1.00 47.77  ? 499  GLU A CB  1 
ATOM   3952 C CG  . GLU A 1 498 ? -24.429 35.504 -21.730 1.00 59.83  ? 499  GLU A CG  1 
ATOM   3953 C CD  . GLU A 1 498 ? -22.970 35.265 -21.794 1.00 65.97  ? 499  GLU A CD  1 
ATOM   3954 O OE1 . GLU A 1 498 ? -22.272 36.212 -22.199 1.00 74.92  ? 499  GLU A OE1 1 
ATOM   3955 O OE2 . GLU A 1 498 ? -22.548 34.108 -21.498 1.00 83.78  ? 499  GLU A OE2 1 
ATOM   3956 N N   . GLN A 1 499 ? -27.718 36.218 -24.830 1.00 38.02  ? 500  GLN A N   1 
ATOM   3957 C CA  . GLN A 1 499 ? -28.709 35.967 -25.868 1.00 40.58  ? 500  GLN A CA  1 
ATOM   3958 C C   . GLN A 1 499 ? -28.727 34.566 -26.514 1.00 36.75  ? 500  GLN A C   1 
ATOM   3959 O O   . GLN A 1 499 ? -28.943 34.411 -27.702 1.00 33.27  ? 500  GLN A O   1 
ATOM   3960 C CB  . GLN A 1 499 ? -28.592 37.079 -26.897 1.00 46.44  ? 500  GLN A CB  1 
ATOM   3961 C CG  . GLN A 1 499 ? -28.976 38.429 -26.275 1.00 47.41  ? 500  GLN A CG  1 
ATOM   3962 C CD  . GLN A 1 499 ? -28.696 39.583 -27.203 1.00 46.98  ? 500  GLN A CD  1 
ATOM   3963 O OE1 . GLN A 1 499 ? -28.804 39.444 -28.381 1.00 46.84  ? 500  GLN A OE1 1 
ATOM   3964 N NE2 . GLN A 1 499 ? -28.270 40.701 -26.658 1.00 49.55  ? 500  GLN A NE2 1 
ATOM   3965 N N   . LYS A 1 500 ? -28.610 33.536 -25.688 1.00 36.68  ? 501  LYS A N   1 
ATOM   3966 C CA  . LYS A 1 500 ? -28.547 32.182 -26.193 1.00 34.54  ? 501  LYS A CA  1 
ATOM   3967 C C   . LYS A 1 500 ? -29.852 31.576 -26.603 1.00 33.38  ? 501  LYS A C   1 
ATOM   3968 O O   . LYS A 1 500 ? -30.912 31.879 -26.034 1.00 30.27  ? 501  LYS A O   1 
ATOM   3969 C CB  . LYS A 1 500 ? -27.943 31.274 -25.178 1.00 37.81  ? 501  LYS A CB  1 
ATOM   3970 C CG  . LYS A 1 500 ? -26.505 31.644 -24.881 1.00 43.02  ? 501  LYS A CG  1 
ATOM   3971 C CD  . LYS A 1 500 ? -25.985 30.847 -23.691 1.00 47.07  ? 501  LYS A CD  1 
ATOM   3972 C CE  . LYS A 1 500 ? -24.604 31.380 -23.295 1.00 50.19  ? 501  LYS A CE  1 
ATOM   3973 N NZ  . LYS A 1 500 ? -23.776 30.316 -22.685 1.00 48.67  ? 501  LYS A NZ  1 
ATOM   3974 N N   . PHE A 1 501 ? -29.756 30.629 -27.537 1.00 28.00  ? 502  PHE A N   1 
ATOM   3975 C CA  . PHE A 1 501 ? -30.919 29.917 -27.906 1.00 29.21  ? 502  PHE A CA  1 
ATOM   3976 C C   . PHE A 1 501 ? -30.481 28.584 -28.431 1.00 31.24  ? 502  PHE A C   1 
ATOM   3977 O O   . PHE A 1 501 ? -29.302 28.332 -28.614 1.00 32.75  ? 502  PHE A O   1 
ATOM   3978 C CB  . PHE A 1 501 ? -31.739 30.705 -28.973 1.00 30.16  ? 502  PHE A CB  1 
ATOM   3979 C CG  . PHE A 1 501 ? -31.069 30.813 -30.329 1.00 25.32  ? 502  PHE A CG  1 
ATOM   3980 C CD1 . PHE A 1 501 ? -30.206 31.827 -30.592 1.00 24.21  ? 502  PHE A CD1 1 
ATOM   3981 C CD2 . PHE A 1 501 ? -31.353 29.893 -31.330 1.00 27.47  ? 502  PHE A CD2 1 
ATOM   3982 C CE1 . PHE A 1 501 ? -29.573 31.919 -31.817 1.00 28.16  ? 502  PHE A CE1 1 
ATOM   3983 C CE2 . PHE A 1 501 ? -30.751 29.996 -32.595 1.00 28.87  ? 502  PHE A CE2 1 
ATOM   3984 C CZ  . PHE A 1 501 ? -29.869 31.024 -32.846 1.00 26.37  ? 502  PHE A CZ  1 
ATOM   3985 N N   . ILE A 1 502 ? -31.442 27.720 -28.642 1.00 29.27  ? 503  ILE A N   1 
ATOM   3986 C CA  . ILE A 1 502 ? -31.140 26.438 -29.179 1.00 34.63  ? 503  ILE A CA  1 
ATOM   3987 C C   . ILE A 1 502 ? -31.939 26.161 -30.449 1.00 35.10  ? 503  ILE A C   1 
ATOM   3988 O O   . ILE A 1 502 ? -33.019 26.740 -30.668 1.00 32.18  ? 503  ILE A O   1 
ATOM   3989 C CB  . ILE A 1 502 ? -31.469 25.296 -28.177 1.00 37.83  ? 503  ILE A CB  1 
ATOM   3990 C CG1 . ILE A 1 502 ? -32.959 25.275 -27.829 1.00 35.93  ? 503  ILE A CG1 1 
ATOM   3991 C CG2 . ILE A 1 502 ? -30.627 25.455 -26.925 1.00 35.71  ? 503  ILE A CG2 1 
ATOM   3992 C CD1 . ILE A 1 502 ? -33.489 23.932 -27.469 1.00 37.90  ? 503  ILE A CD1 1 
ATOM   3993 N N   . ASP A 1 503 ? -31.391 25.257 -31.249 1.00 34.17  ? 504  ASP A N   1 
ATOM   3994 C CA  . ASP A 1 503 ? -32.040 24.758 -32.416 1.00 38.07  ? 504  ASP A CA  1 
ATOM   3995 C C   . ASP A 1 503 ? -32.883 23.615 -31.866 1.00 36.02  ? 504  ASP A C   1 
ATOM   3996 O O   . ASP A 1 503 ? -32.517 22.990 -30.886 1.00 41.56  ? 504  ASP A O   1 
ATOM   3997 C CB  . ASP A 1 503 ? -31.058 24.201 -33.475 1.00 41.37  ? 504  ASP A CB  1 
ATOM   3998 C CG  . ASP A 1 503 ? -30.140 25.270 -34.119 1.00 44.49  ? 504  ASP A CG  1 
ATOM   3999 O OD1 . ASP A 1 503 ? -30.489 26.444 -34.269 1.00 49.96  ? 504  ASP A OD1 1 
ATOM   4000 O OD2 . ASP A 1 503 ? -29.009 24.927 -34.502 1.00 54.58  ? 504  ASP A OD2 1 
ATOM   4001 N N   . LEU A 1 504 ? -33.977 23.348 -32.555 1.00 34.02  ? 505  LEU A N   1 
ATOM   4002 C CA  . LEU A 1 504 ? -34.865 22.283 -32.285 1.00 36.53  ? 505  LEU A CA  1 
ATOM   4003 C C   . LEU A 1 504 ? -34.972 21.424 -33.563 1.00 40.16  ? 505  LEU A C   1 
ATOM   4004 O O   . LEU A 1 504 ? -35.652 21.761 -34.510 1.00 39.66  ? 505  LEU A O   1 
ATOM   4005 C CB  . LEU A 1 504 ? -36.199 22.906 -31.869 1.00 38.88  ? 505  LEU A CB  1 
ATOM   4006 C CG  . LEU A 1 504 ? -36.906 22.454 -30.587 1.00 42.29  ? 505  LEU A CG  1 
ATOM   4007 C CD1 . LEU A 1 504 ? -36.011 22.144 -29.393 1.00 39.04  ? 505  LEU A CD1 1 
ATOM   4008 C CD2 . LEU A 1 504 ? -37.923 23.513 -30.225 1.00 41.01  ? 505  LEU A CD2 1 
ATOM   4009 N N   . ASN A 1 505 ? -34.252 20.307 -33.595 1.00 44.57  ? 506  ASN A N   1 
ATOM   4010 C CA  . ASN A 1 505 ? -34.319 19.389 -34.699 1.00 43.04  ? 506  ASN A CA  1 
ATOM   4011 C C   . ASN A 1 505 ? -33.940 17.971 -34.236 1.00 44.61  ? 506  ASN A C   1 
ATOM   4012 O O   . ASN A 1 505 ? -33.859 17.721 -33.073 1.00 47.21  ? 506  ASN A O   1 
ATOM   4013 C CB  . ASN A 1 505 ? -33.414 19.904 -35.821 1.00 38.90  ? 506  ASN A CB  1 
ATOM   4014 C CG  . ASN A 1 505 ? -32.016 20.108 -35.358 1.00 37.86  ? 506  ASN A CG  1 
ATOM   4015 O OD1 . ASN A 1 505 ? -31.534 19.296 -34.618 1.00 42.13  ? 506  ASN A OD1 1 
ATOM   4016 N ND2 . ASN A 1 505 ? -31.371 21.227 -35.730 1.00 37.21  ? 506  ASN A ND2 1 
ATOM   4017 N N   . THR A 1 506 ? -33.736 17.056 -35.164 1.00 44.99  ? 507  THR A N   1 
ATOM   4018 C CA  . THR A 1 506 ? -33.398 15.671 -34.866 1.00 48.34  ? 507  THR A CA  1 
ATOM   4019 C C   . THR A 1 506 ? -31.927 15.433 -34.497 1.00 49.84  ? 507  THR A C   1 
ATOM   4020 O O   . THR A 1 506 ? -31.577 14.356 -34.054 1.00 55.76  ? 507  THR A O   1 
ATOM   4021 C CB  . THR A 1 506 ? -33.734 14.801 -36.081 1.00 44.73  ? 507  THR A CB  1 
ATOM   4022 O OG1 . THR A 1 506 ? -33.119 15.384 -37.253 1.00 47.13  ? 507  THR A OG1 1 
ATOM   4023 C CG2 . THR A 1 506 ? -35.206 14.747 -36.260 1.00 43.72  ? 507  THR A CG2 1 
ATOM   4024 N N   . GLU A 1 507 ? -31.086 16.437 -34.650 1.00 52.07  ? 508  GLU A N   1 
ATOM   4025 C CA  . GLU A 1 507 ? -29.663 16.344 -34.343 1.00 52.42  ? 508  GLU A CA  1 
ATOM   4026 C C   . GLU A 1 507 ? -29.388 16.779 -32.897 1.00 53.52  ? 508  GLU A C   1 
ATOM   4027 O O   . GLU A 1 507 ? -30.218 17.425 -32.288 1.00 49.75  ? 508  GLU A O   1 
ATOM   4028 C CB  . GLU A 1 507 ? -28.866 17.241 -35.317 1.00 53.35  ? 508  GLU A CB  1 
ATOM   4029 C CG  . GLU A 1 507 ? -28.999 16.862 -36.795 1.00 66.24  ? 508  GLU A CG  1 
ATOM   4030 C CD  . GLU A 1 507 ? -28.696 18.067 -37.696 1.00 92.74  ? 508  GLU A CD  1 
ATOM   4031 O OE1 . GLU A 1 507 ? -27.615 18.697 -37.527 1.00 102.32 ? 508  GLU A OE1 1 
ATOM   4032 O OE2 . GLU A 1 507 ? -29.546 18.416 -38.553 1.00 100.68 ? 508  GLU A OE2 1 
ATOM   4033 N N   . PRO A 1 508 ? -28.208 16.433 -32.345 1.00 61.96  ? 509  PRO A N   1 
ATOM   4034 C CA  . PRO A 1 508 ? -27.944 16.830 -30.961 1.00 67.01  ? 509  PRO A CA  1 
ATOM   4035 C C   . PRO A 1 508 ? -27.994 18.347 -30.750 1.00 62.95  ? 509  PRO A C   1 
ATOM   4036 O O   . PRO A 1 508 ? -27.457 19.109 -31.557 1.00 58.33  ? 509  PRO A O   1 
ATOM   4037 C CB  . PRO A 1 508 ? -26.523 16.274 -30.674 1.00 65.18  ? 509  PRO A CB  1 
ATOM   4038 C CG  . PRO A 1 508 ? -25.965 15.874 -32.005 1.00 66.16  ? 509  PRO A CG  1 
ATOM   4039 C CD  . PRO A 1 508 ? -27.154 15.548 -32.871 1.00 61.71  ? 509  PRO A CD  1 
ATOM   4040 N N   . MET A 1 509 ? -28.646 18.756 -29.658 1.00 61.72  ? 510  MET A N   1 
ATOM   4041 C CA  . MET A 1 509 ? -28.867 20.149 -29.346 1.00 60.53  ? 510  MET A CA  1 
ATOM   4042 C C   . MET A 1 509 ? -27.580 20.917 -29.577 1.00 60.46  ? 510  MET A C   1 
ATOM   4043 O O   . MET A 1 509 ? -26.481 20.443 -29.296 1.00 63.95  ? 510  MET A O   1 
ATOM   4044 C CB  . MET A 1 509 ? -29.345 20.315 -27.911 1.00 63.86  ? 510  MET A CB  1 
ATOM   4045 C CG  . MET A 1 509 ? -29.548 21.758 -27.468 1.00 67.09  ? 510  MET A CG  1 
ATOM   4046 S SD  . MET A 1 509 ? -29.517 21.937 -25.670 1.00 63.42  ? 510  MET A SD  1 
ATOM   4047 C CE  . MET A 1 509 ? -31.017 21.021 -25.291 1.00 60.77  ? 510  MET A CE  1 
ATOM   4048 N N   . LYS A 1 510 ? -27.736 22.082 -30.179 1.00 60.99  ? 511  LYS A N   1 
ATOM   4049 C CA  . LYS A 1 510 ? -26.652 23.008 -30.393 1.00 55.72  ? 511  LYS A CA  1 
ATOM   4050 C C   . LYS A 1 510 ? -27.226 24.352 -29.902 1.00 51.97  ? 511  LYS A C   1 
ATOM   4051 O O   . LYS A 1 510 ? -28.399 24.687 -30.169 1.00 49.26  ? 511  LYS A O   1 
ATOM   4052 C CB  . LYS A 1 510 ? -26.261 23.004 -31.873 1.00 61.72  ? 511  LYS A CB  1 
ATOM   4053 C CG  . LYS A 1 510 ? -24.785 23.255 -32.132 1.00 80.42  ? 511  LYS A CG  1 
ATOM   4054 C CD  . LYS A 1 510 ? -24.293 22.683 -33.472 1.00 91.47  ? 511  LYS A CD  1 
ATOM   4055 C CE  . LYS A 1 510 ? -22.773 22.467 -33.473 1.00 97.43  ? 511  LYS A CE  1 
ATOM   4056 N NZ  . LYS A 1 510 ? -22.143 22.810 -34.783 1.00 99.97  ? 511  LYS A NZ  1 
ATOM   4057 N N   . VAL A 1 511 ? -26.419 25.033 -29.106 1.00 41.23  ? 512  VAL A N   1 
ATOM   4058 C CA  . VAL A 1 511 ? -26.655 26.344 -28.585 1.00 40.83  ? 512  VAL A CA  1 
ATOM   4059 C C   . VAL A 1 511 ? -25.969 27.360 -29.456 1.00 41.85  ? 512  VAL A C   1 
ATOM   4060 O O   . VAL A 1 511 ? -24.796 27.184 -29.827 1.00 40.66  ? 512  VAL A O   1 
ATOM   4061 C CB  . VAL A 1 511 ? -26.030 26.485 -27.155 1.00 43.65  ? 512  VAL A CB  1 
ATOM   4062 C CG1 . VAL A 1 511 ? -26.169 27.918 -26.592 1.00 39.25  ? 512  VAL A CG1 1 
ATOM   4063 C CG2 . VAL A 1 511 ? -26.658 25.435 -26.204 1.00 43.75  ? 512  VAL A CG2 1 
ATOM   4064 N N   . HIS A 1 512 ? -26.682 28.455 -29.729 1.00 39.33  ? 513  HIS A N   1 
ATOM   4065 C CA  . HIS A 1 512 ? -26.146 29.593 -30.476 1.00 38.51  ? 513  HIS A CA  1 
ATOM   4066 C C   . HIS A 1 512 ? -26.455 30.912 -29.773 1.00 40.12  ? 513  HIS A C   1 
ATOM   4067 O O   . HIS A 1 512 ? -27.127 30.947 -28.729 1.00 37.05  ? 513  HIS A O   1 
ATOM   4068 C CB  . HIS A 1 512 ? -26.820 29.659 -31.852 1.00 40.02  ? 513  HIS A CB  1 
ATOM   4069 C CG  . HIS A 1 512 ? -26.792 28.387 -32.623 1.00 38.42  ? 513  HIS A CG  1 
ATOM   4070 N ND1 . HIS A 1 512 ? -25.674 27.964 -33.312 1.00 43.20  ? 513  HIS A ND1 1 
ATOM   4071 C CD2 . HIS A 1 512 ? -27.749 27.459 -32.846 1.00 41.24  ? 513  HIS A CD2 1 
ATOM   4072 C CE1 . HIS A 1 512 ? -25.942 26.825 -33.929 1.00 42.16  ? 513  HIS A CE1 1 
ATOM   4073 N NE2 . HIS A 1 512 ? -27.190 26.488 -33.655 1.00 42.57  ? 513  HIS A NE2 1 
ATOM   4074 N N   . GLN A 1 513 ? -26.057 32.013 -30.398 1.00 42.77  ? 514  GLN A N   1 
ATOM   4075 C CA  . GLN A 1 513 ? -26.344 33.332 -29.845 1.00 43.55  ? 514  GLN A CA  1 
ATOM   4076 C C   . GLN A 1 513 ? -26.850 34.309 -30.878 1.00 38.66  ? 514  GLN A C   1 
ATOM   4077 O O   . GLN A 1 513 ? -26.529 34.191 -32.012 1.00 35.94  ? 514  GLN A O   1 
ATOM   4078 C CB  . GLN A 1 513 ? -25.069 33.895 -29.204 1.00 43.54  ? 514  GLN A CB  1 
ATOM   4079 C CG  . GLN A 1 513 ? -24.638 33.032 -28.009 1.00 51.22  ? 514  GLN A CG  1 
ATOM   4080 C CD  . GLN A 1 513 ? -23.365 33.507 -27.363 1.00 43.90  ? 514  GLN A CD  1 
ATOM   4081 O OE1 . GLN A 1 513 ? -22.302 32.992 -27.644 1.00 51.75  ? 514  GLN A OE1 1 
ATOM   4082 N NE2 . GLN A 1 513 ? -23.467 34.540 -26.556 1.00 45.25  ? 514  GLN A NE2 1 
ATOM   4083 N N   . ARG A 1 514 ? -27.650 35.275 -30.445 1.00 38.61  ? 515  ARG A N   1 
ATOM   4084 C CA  . ARG A 1 514 ? -27.977 36.432 -31.246 1.00 41.66  ? 515  ARG A CA  1 
ATOM   4085 C C   . ARG A 1 514 ? -28.679 36.013 -32.559 1.00 39.30  ? 515  ARG A C   1 
ATOM   4086 O O   . ARG A 1 514 ? -28.157 36.186 -33.627 1.00 35.38  ? 515  ARG A O   1 
ATOM   4087 C CB  . ARG A 1 514 ? -26.694 37.227 -31.478 1.00 43.78  ? 515  ARG A CB  1 
ATOM   4088 C CG  . ARG A 1 514 ? -26.274 38.037 -30.261 1.00 50.08  ? 515  ARG A CG  1 
ATOM   4089 C CD  . ARG A 1 514 ? -24.930 38.707 -30.417 1.00 51.89  ? 515  ARG A CD  1 
ATOM   4090 N NE  . ARG A 1 514 ? -24.721 39.749 -29.423 1.00 58.26  ? 515  ARG A NE  1 
ATOM   4091 C CZ  . ARG A 1 514 ? -23.912 40.821 -29.564 1.00 77.39  ? 515  ARG A CZ  1 
ATOM   4092 N NH1 . ARG A 1 514 ? -23.192 41.063 -30.681 1.00 87.12  ? 515  ARG A NH1 1 
ATOM   4093 N NH2 . ARG A 1 514 ? -23.801 41.687 -28.564 1.00 77.01  ? 515  ARG A NH2 1 
ATOM   4094 N N   . LEU A 1 515 ? -29.854 35.416 -32.412 1.00 36.46  ? 516  LEU A N   1 
ATOM   4095 C CA  . LEU A 1 515 ? -30.673 34.897 -33.496 1.00 38.18  ? 516  LEU A CA  1 
ATOM   4096 C C   . LEU A 1 515 ? -31.025 36.006 -34.519 1.00 37.39  ? 516  LEU A C   1 
ATOM   4097 O O   . LEU A 1 515 ? -31.736 36.980 -34.184 1.00 30.12  ? 516  LEU A O   1 
ATOM   4098 C CB  . LEU A 1 515 ? -31.968 34.306 -32.885 1.00 40.34  ? 516  LEU A CB  1 
ATOM   4099 C CG  . LEU A 1 515 ? -33.174 33.884 -33.723 1.00 40.80  ? 516  LEU A CG  1 
ATOM   4100 C CD1 . LEU A 1 515 ? -32.698 33.151 -34.916 1.00 44.16  ? 516  LEU A CD1 1 
ATOM   4101 C CD2 . LEU A 1 515 ? -34.112 32.972 -32.908 1.00 42.32  ? 516  LEU A CD2 1 
ATOM   4102 N N   . ARG A 1 516 ? -30.507 35.853 -35.738 1.00 32.65  ? 517  ARG A N   1 
ATOM   4103 C CA  . ARG A 1 516 ? -30.720 36.796 -36.856 1.00 33.24  ? 517  ARG A CA  1 
ATOM   4104 C C   . ARG A 1 516 ? -30.449 38.201 -36.535 1.00 31.43  ? 517  ARG A C   1 
ATOM   4105 O O   . ARG A 1 516 ? -31.166 39.060 -36.991 1.00 34.92  ? 517  ARG A O   1 
ATOM   4106 C CB  . ARG A 1 516 ? -32.115 36.585 -37.522 1.00 37.64  ? 517  ARG A CB  1 
ATOM   4107 C CG  . ARG A 1 516 ? -31.955 35.283 -38.336 1.00 44.96  ? 517  ARG A CG  1 
ATOM   4108 C CD  . ARG A 1 516 ? -33.047 34.804 -39.283 1.00 49.08  ? 517  ARG A CD  1 
ATOM   4109 N NE  . ARG A 1 516 ? -33.115 35.521 -40.544 1.00 54.87  ? 517  ARG A NE  1 
ATOM   4110 C CZ  . ARG A 1 516 ? -32.281 35.386 -41.591 1.00 55.25  ? 517  ARG A CZ  1 
ATOM   4111 N NH1 . ARG A 1 516 ? -31.262 34.561 -41.530 1.00 55.69  ? 517  ARG A NH1 1 
ATOM   4112 N NH2 . ARG A 1 516 ? -32.454 36.094 -42.725 1.00 45.24  ? 517  ARG A NH2 1 
ATOM   4113 N N   . VAL A 1 517 ? -29.423 38.474 -35.716 1.00 33.06  ? 518  VAL A N   1 
ATOM   4114 C CA  . VAL A 1 517 ? -29.269 39.844 -35.243 1.00 30.37  ? 518  VAL A CA  1 
ATOM   4115 C C   . VAL A 1 517 ? -29.030 40.800 -36.429 1.00 29.07  ? 518  VAL A C   1 
ATOM   4116 O O   . VAL A 1 517 ? -29.329 41.966 -36.307 1.00 30.84  ? 518  VAL A O   1 
ATOM   4117 C CB  . VAL A 1 517 ? -27.950 40.127 -34.504 1.00 32.58  ? 518  VAL A CB  1 
ATOM   4118 C CG1 . VAL A 1 517 ? -28.069 41.069 -33.322 1.00 29.71  ? 518  VAL A CG1 1 
ATOM   4119 C CG2 . VAL A 1 517 ? -27.009 38.982 -34.496 1.00 29.03  ? 518  VAL A CG2 1 
ATOM   4120 N N   . GLN A 1 518 ? -28.216 40.371 -37.415 1.00 28.95  ? 519  GLN A N   1 
ATOM   4121 C CA  . GLN A 1 518 ? -27.810 41.262 -38.520 1.00 31.96  ? 519  GLN A CA  1 
ATOM   4122 C C   . GLN A 1 518 ? -29.120 41.781 -39.184 1.00 29.95  ? 519  GLN A C   1 
ATOM   4123 O O   . GLN A 1 518 ? -29.347 42.944 -39.227 1.00 29.18  ? 519  GLN A O   1 
ATOM   4124 C CB  . GLN A 1 518 ? -26.910 40.473 -39.548 1.00 32.66  ? 519  GLN A CB  1 
ATOM   4125 C CG  . GLN A 1 518 ? -26.041 41.392 -40.431 1.00 35.30  ? 519  GLN A CG  1 
ATOM   4126 C CD  . GLN A 1 518 ? -25.030 42.200 -39.619 1.00 40.01  ? 519  GLN A CD  1 
ATOM   4127 O OE1 . GLN A 1 518 ? -24.501 41.716 -38.604 1.00 45.12  ? 519  GLN A OE1 1 
ATOM   4128 N NE2 . GLN A 1 518 ? -24.822 43.456 -39.995 1.00 38.62  ? 519  GLN A NE2 1 
ATOM   4129 N N   . MET A 1 519 ? -30.019 40.876 -39.592 1.00 25.27  ? 520  MET A N   1 
ATOM   4130 C CA  . MET A 1 519 ? -31.250 41.277 -40.236 1.00 29.45  ? 520  MET A CA  1 
ATOM   4131 C C   . MET A 1 519 ? -32.178 42.012 -39.270 1.00 29.80  ? 520  MET A C   1 
ATOM   4132 O O   . MET A 1 519 ? -32.835 42.975 -39.664 1.00 30.96  ? 520  MET A O   1 
ATOM   4133 C CB  . MET A 1 519 ? -31.940 40.065 -40.894 1.00 31.34  ? 520  MET A CB  1 
ATOM   4134 C CG  . MET A 1 519 ? -31.185 39.472 -42.106 1.00 37.57  ? 520  MET A CG  1 
ATOM   4135 S SD  . MET A 1 519 ? -30.605 40.718 -43.347 1.00 44.43  ? 520  MET A SD  1 
ATOM   4136 C CE  . MET A 1 519 ? -28.842 40.818 -43.012 1.00 52.60  ? 520  MET A CE  1 
ATOM   4137 N N   . CYS A 1 520 ? -32.187 41.647 -37.984 1.00 26.66  ? 521  CYS A N   1 
ATOM   4138 C CA  . CYS A 1 520 ? -33.162 42.274 -37.083 1.00 25.40  ? 521  CYS A CA  1 
ATOM   4139 C C   . CYS A 1 520 ? -32.680 43.601 -36.673 1.00 23.64  ? 521  CYS A C   1 
ATOM   4140 O O   . CYS A 1 520 ? -33.527 44.463 -36.386 1.00 23.68  ? 521  CYS A O   1 
ATOM   4141 C CB  . CYS A 1 520 ? -33.540 41.423 -35.887 1.00 26.95  ? 521  CYS A CB  1 
ATOM   4142 S SG  . CYS A 1 520 ? -34.319 39.891 -36.405 1.00 29.11  ? 521  CYS A SG  1 
ATOM   4143 N N   . VAL A 1 521 ? -31.364 43.858 -36.680 1.00 23.58  ? 522  VAL A N   1 
ATOM   4144 C CA  . VAL A 1 521 ? -30.942 45.279 -36.478 1.00 24.93  ? 522  VAL A CA  1 
ATOM   4145 C C   . VAL A 1 521 ? -31.446 46.113 -37.679 1.00 27.91  ? 522  VAL A C   1 
ATOM   4146 O O   . VAL A 1 521 ? -31.861 47.245 -37.553 1.00 25.55  ? 522  VAL A O   1 
ATOM   4147 C CB  . VAL A 1 521 ? -29.411 45.458 -36.398 1.00 29.74  ? 522  VAL A CB  1 
ATOM   4148 C CG1 . VAL A 1 521 ? -28.996 46.963 -36.481 1.00 27.56  ? 522  VAL A CG1 1 
ATOM   4149 C CG2 . VAL A 1 521 ? -28.856 44.875 -35.107 1.00 29.17  ? 522  VAL A CG2 1 
ATOM   4150 N N   . PHE A 1 522 ? -31.429 45.530 -38.879 1.00 29.83  ? 523  PHE A N   1 
ATOM   4151 C CA  . PHE A 1 522 ? -32.047 46.230 -39.995 1.00 28.79  ? 523  PHE A CA  1 
ATOM   4152 C C   . PHE A 1 522 ? -33.546 46.520 -39.800 1.00 28.07  ? 523  PHE A C   1 
ATOM   4153 O O   . PHE A 1 522 ? -34.003 47.681 -39.936 1.00 26.40  ? 523  PHE A O   1 
ATOM   4154 C CB  . PHE A 1 522 ? -31.808 45.479 -41.305 1.00 26.97  ? 523  PHE A CB  1 
ATOM   4155 C CG  . PHE A 1 522 ? -32.513 46.075 -42.437 1.00 25.91  ? 523  PHE A CG  1 
ATOM   4156 C CD1 . PHE A 1 522 ? -32.004 47.197 -43.092 1.00 28.42  ? 523  PHE A CD1 1 
ATOM   4157 C CD2 . PHE A 1 522 ? -33.683 45.553 -42.843 1.00 24.32  ? 523  PHE A CD2 1 
ATOM   4158 C CE1 . PHE A 1 522 ? -32.651 47.744 -44.187 1.00 25.03  ? 523  PHE A CE1 1 
ATOM   4159 C CE2 . PHE A 1 522 ? -34.357 46.128 -43.876 1.00 26.12  ? 523  PHE A CE2 1 
ATOM   4160 C CZ  . PHE A 1 522 ? -33.815 47.191 -44.576 1.00 27.67  ? 523  PHE A CZ  1 
ATOM   4161 N N   . TRP A 1 523 ? -34.316 45.483 -39.527 1.00 27.11  ? 524  TRP A N   1 
ATOM   4162 C CA  . TRP A 1 523 ? -35.761 45.687 -39.364 1.00 28.63  ? 524  TRP A CA  1 
ATOM   4163 C C   . TRP A 1 523 ? -36.169 46.396 -38.104 1.00 28.49  ? 524  TRP A C   1 
ATOM   4164 O O   . TRP A 1 523 ? -37.082 47.175 -38.136 1.00 30.93  ? 524  TRP A O   1 
ATOM   4165 C CB  . TRP A 1 523 ? -36.516 44.382 -39.397 1.00 27.56  ? 524  TRP A CB  1 
ATOM   4166 C CG  . TRP A 1 523 ? -36.416 43.714 -40.695 1.00 26.06  ? 524  TRP A CG  1 
ATOM   4167 C CD1 . TRP A 1 523 ? -35.584 42.706 -41.015 1.00 26.80  ? 524  TRP A CD1 1 
ATOM   4168 C CD2 . TRP A 1 523 ? -37.164 44.005 -41.865 1.00 24.58  ? 524  TRP A CD2 1 
ATOM   4169 N NE1 . TRP A 1 523 ? -35.775 42.308 -42.291 1.00 26.43  ? 524  TRP A NE1 1 
ATOM   4170 C CE2 . TRP A 1 523 ? -36.713 43.125 -42.868 1.00 28.00  ? 524  TRP A CE2 1 
ATOM   4171 C CE3 . TRP A 1 523 ? -38.123 44.943 -42.186 1.00 24.56  ? 524  TRP A CE3 1 
ATOM   4172 C CZ2 . TRP A 1 523 ? -37.230 43.136 -44.171 1.00 24.65  ? 524  TRP A CZ2 1 
ATOM   4173 C CZ3 . TRP A 1 523 ? -38.660 44.955 -43.505 1.00 26.16  ? 524  TRP A CZ3 1 
ATOM   4174 C CH2 . TRP A 1 523 ? -38.207 44.053 -44.459 1.00 24.50  ? 524  TRP A CH2 1 
ATOM   4175 N N   . ASN A 1 524 ? -35.459 46.214 -37.013 1.00 32.25  ? 525  ASN A N   1 
ATOM   4176 C CA  . ASN A 1 524 ? -35.884 46.842 -35.716 1.00 30.97  ? 525  ASN A CA  1 
ATOM   4177 C C   . ASN A 1 524 ? -35.286 48.190 -35.447 1.00 31.39  ? 525  ASN A C   1 
ATOM   4178 O O   . ASN A 1 524 ? -35.827 48.918 -34.716 1.00 30.56  ? 525  ASN A O   1 
ATOM   4179 C CB  . ASN A 1 524 ? -35.622 45.913 -34.551 1.00 26.41  ? 525  ASN A CB  1 
ATOM   4180 C CG  . ASN A 1 524 ? -36.400 44.649 -34.699 1.00 29.41  ? 525  ASN A CG  1 
ATOM   4181 O OD1 . ASN A 1 524 ? -37.343 44.617 -35.444 1.00 34.07  ? 525  ASN A OD1 1 
ATOM   4182 N ND2 . ASN A 1 524 ? -35.972 43.600 -34.094 1.00 29.93  ? 525  ASN A ND2 1 
ATOM   4183 N N   . GLN A 1 525 ? -34.187 48.553 -36.051 1.00 35.33  ? 526  GLN A N   1 
ATOM   4184 C CA  . GLN A 1 525 ? -33.583 49.824 -35.748 1.00 33.40  ? 526  GLN A CA  1 
ATOM   4185 C C   . GLN A 1 525 ? -33.421 50.697 -36.997 1.00 34.71  ? 526  GLN A C   1 
ATOM   4186 O O   . GLN A 1 525 ? -33.850 51.839 -36.978 1.00 30.60  ? 526  GLN A O   1 
ATOM   4187 C CB  . GLN A 1 525 ? -32.242 49.577 -35.123 1.00 41.25  ? 526  GLN A CB  1 
ATOM   4188 C CG  . GLN A 1 525 ? -32.253 48.952 -33.716 1.00 55.23  ? 526  GLN A CG  1 
ATOM   4189 C CD  . GLN A 1 525 ? -30.828 48.982 -33.083 1.00 70.52  ? 526  GLN A CD  1 
ATOM   4190 O OE1 . GLN A 1 525 ? -30.112 50.012 -33.134 1.00 68.62  ? 526  GLN A OE1 1 
ATOM   4191 N NE2 . GLN A 1 525 ? -30.394 47.837 -32.533 1.00 70.29  ? 526  GLN A NE2 1 
ATOM   4192 N N   . PHE A 1 526 ? -32.809 50.175 -38.086 1.00 31.69  ? 527  PHE A N   1 
ATOM   4193 C CA  . PHE A 1 526 ? -32.468 51.035 -39.210 1.00 29.47  ? 527  PHE A CA  1 
ATOM   4194 C C   . PHE A 1 526 ? -33.686 51.411 -40.036 1.00 25.73  ? 527  PHE A C   1 
ATOM   4195 O O   . PHE A 1 526 ? -34.027 52.592 -40.215 1.00 29.06  ? 527  PHE A O   1 
ATOM   4196 C CB  . PHE A 1 526 ? -31.313 50.429 -40.074 1.00 28.99  ? 527  PHE A CB  1 
ATOM   4197 C CG  . PHE A 1 526 ? -30.975 51.272 -41.238 1.00 29.13  ? 527  PHE A CG  1 
ATOM   4198 C CD1 . PHE A 1 526 ? -30.277 52.452 -41.066 1.00 33.22  ? 527  PHE A CD1 1 
ATOM   4199 C CD2 . PHE A 1 526 ? -31.426 50.949 -42.508 1.00 31.49  ? 527  PHE A CD2 1 
ATOM   4200 C CE1 . PHE A 1 526 ? -30.030 53.315 -42.131 1.00 30.49  ? 527  PHE A CE1 1 
ATOM   4201 C CE2 . PHE A 1 526 ? -31.159 51.774 -43.583 1.00 33.05  ? 527  PHE A CE2 1 
ATOM   4202 C CZ  . PHE A 1 526 ? -30.453 52.961 -43.393 1.00 33.31  ? 527  PHE A CZ  1 
ATOM   4203 N N   . LEU A 1 527 ? -34.381 50.424 -40.554 1.00 26.99  ? 528  LEU A N   1 
ATOM   4204 C CA  . LEU A 1 527 ? -35.478 50.731 -41.479 1.00 26.60  ? 528  LEU A CA  1 
ATOM   4205 C C   . LEU A 1 527 ? -36.540 51.666 -40.857 1.00 30.59  ? 528  LEU A C   1 
ATOM   4206 O O   . LEU A 1 527 ? -37.079 52.551 -41.528 1.00 34.09  ? 528  LEU A O   1 
ATOM   4207 C CB  . LEU A 1 527 ? -36.135 49.440 -41.965 1.00 25.67  ? 528  LEU A CB  1 
ATOM   4208 C CG  . LEU A 1 527 ? -37.263 49.666 -42.945 1.00 28.82  ? 528  LEU A CG  1 
ATOM   4209 C CD1 . LEU A 1 527 ? -36.753 50.510 -44.175 1.00 30.80  ? 528  LEU A CD1 1 
ATOM   4210 C CD2 . LEU A 1 527 ? -37.883 48.333 -43.380 1.00 30.72  ? 528  LEU A CD2 1 
ATOM   4211 N N   . PRO A 1 528 ? -36.898 51.450 -39.586 1.00 31.97  ? 529  PRO A N   1 
ATOM   4212 C CA  . PRO A 1 528 ? -37.871 52.386 -39.041 1.00 35.65  ? 529  PRO A CA  1 
ATOM   4213 C C   . PRO A 1 528 ? -37.310 53.788 -38.839 1.00 33.90  ? 529  PRO A C   1 
ATOM   4214 O O   . PRO A 1 528 ? -38.031 54.772 -39.067 1.00 37.03  ? 529  PRO A O   1 
ATOM   4215 C CB  . PRO A 1 528 ? -38.287 51.728 -37.696 1.00 36.10  ? 529  PRO A CB  1 
ATOM   4216 C CG  . PRO A 1 528 ? -37.931 50.290 -37.853 1.00 37.35  ? 529  PRO A CG  1 
ATOM   4217 C CD  . PRO A 1 528 ? -36.609 50.374 -38.628 1.00 34.11  ? 529  PRO A CD  1 
ATOM   4218 N N   . LYS A 1 529 ? -36.026 53.908 -38.520 1.00 37.96  ? 530  LYS A N   1 
ATOM   4219 C CA  . LYS A 1 529 ? -35.378 55.240 -38.562 1.00 40.48  ? 530  LYS A CA  1 
ATOM   4220 C C   . LYS A 1 529 ? -35.439 55.830 -39.985 1.00 44.77  ? 530  LYS A C   1 
ATOM   4221 O O   . LYS A 1 529 ? -35.679 57.012 -40.166 1.00 42.12  ? 530  LYS A O   1 
ATOM   4222 C CB  . LYS A 1 529 ? -33.962 55.137 -38.120 1.00 48.36  ? 530  LYS A CB  1 
ATOM   4223 C CG  . LYS A 1 529 ? -33.630 56.099 -37.029 1.00 58.80  ? 530  LYS A CG  1 
ATOM   4224 C CD  . LYS A 1 529 ? -32.127 56.142 -36.726 1.00 69.88  ? 530  LYS A CD  1 
ATOM   4225 C CE  . LYS A 1 529 ? -31.642 57.608 -36.752 1.00 70.22  ? 530  LYS A CE  1 
ATOM   4226 N NZ  . LYS A 1 529 ? -30.363 57.829 -36.042 1.00 69.16  ? 530  LYS A NZ  1 
ATOM   4227 N N   . LEU A 1 530 ? -35.275 54.997 -41.010 1.00 42.11  ? 531  LEU A N   1 
ATOM   4228 C CA  . LEU A 1 530 ? -35.227 55.534 -42.368 1.00 39.49  ? 531  LEU A CA  1 
ATOM   4229 C C   . LEU A 1 530 ? -36.600 56.030 -42.780 1.00 42.90  ? 531  LEU A C   1 
ATOM   4230 O O   . LEU A 1 530 ? -36.743 57.144 -43.333 1.00 38.24  ? 531  LEU A O   1 
ATOM   4231 C CB  . LEU A 1 530 ? -34.644 54.488 -43.335 1.00 35.36  ? 531  LEU A CB  1 
ATOM   4232 C CG  . LEU A 1 530 ? -34.582 54.685 -44.853 1.00 34.99  ? 531  LEU A CG  1 
ATOM   4233 C CD1 . LEU A 1 530 ? -33.606 53.703 -45.504 1.00 34.09  ? 531  LEU A CD1 1 
ATOM   4234 C CD2 . LEU A 1 530 ? -35.976 54.478 -45.452 1.00 36.25  ? 531  LEU A CD2 1 
ATOM   4235 N N   . LEU A 1 531 ? -37.618 55.221 -42.521 1.00 40.68  ? 532  LEU A N   1 
ATOM   4236 C CA  . LEU A 1 531 ? -39.002 55.631 -42.869 1.00 43.76  ? 532  LEU A CA  1 
ATOM   4237 C C   . LEU A 1 531 ? -39.506 56.803 -41.999 1.00 40.77  ? 532  LEU A C   1 
ATOM   4238 O O   . LEU A 1 531 ? -40.242 57.603 -42.489 1.00 41.70  ? 532  LEU A O   1 
ATOM   4239 C CB  . LEU A 1 531 ? -40.021 54.461 -42.828 1.00 40.54  ? 532  LEU A CB  1 
ATOM   4240 C CG  . LEU A 1 531 ? -39.716 53.213 -43.657 1.00 41.70  ? 532  LEU A CG  1 
ATOM   4241 C CD1 . LEU A 1 531 ? -40.479 51.996 -43.125 1.00 43.34  ? 532  LEU A CD1 1 
ATOM   4242 C CD2 . LEU A 1 531 ? -39.957 53.439 -45.141 1.00 39.64  ? 532  LEU A CD2 1 
ATOM   4243 N N   . ASN A 1 532 ? -39.107 56.930 -40.740 1.00 47.83  ? 533  ASN A N   1 
ATOM   4244 C CA  . ASN A 1 532 ? -39.461 58.159 -39.982 1.00 56.31  ? 533  ASN A CA  1 
ATOM   4245 C C   . ASN A 1 532 ? -38.827 59.413 -40.580 1.00 53.16  ? 533  ASN A C   1 
ATOM   4246 O O   . ASN A 1 532 ? -39.387 60.470 -40.483 1.00 46.05  ? 533  ASN A O   1 
ATOM   4247 C CB  . ASN A 1 532 ? -39.042 58.104 -38.487 1.00 58.33  ? 533  ASN A CB  1 
ATOM   4248 C CG  . ASN A 1 532 ? -39.829 59.075 -37.611 1.00 61.56  ? 533  ASN A CG  1 
ATOM   4249 O OD1 . ASN A 1 532 ? -41.025 59.262 -37.796 1.00 70.75  ? 533  ASN A OD1 1 
ATOM   4250 N ND2 . ASN A 1 532 ? -39.169 59.667 -36.633 1.00 66.23  ? 533  ASN A ND2 1 
ATOM   4251 N N   . ALA A 1 533 ? -37.637 59.312 -41.139 1.00 51.62  ? 534  ALA A N   1 
ATOM   4252 C CA  . ALA A 1 533 ? -36.939 60.512 -41.526 1.00 58.74  ? 534  ALA A CA  1 
ATOM   4253 C C   . ALA A 1 533 ? -37.494 61.023 -42.860 1.00 72.96  ? 534  ALA A C   1 
ATOM   4254 O O   . ALA A 1 533 ? -37.529 62.246 -43.083 1.00 78.81  ? 534  ALA A O   1 
ATOM   4255 C CB  . ALA A 1 533 ? -35.440 60.271 -41.584 1.00 55.95  ? 534  ALA A CB  1 
ATOM   4256 N N   . THR A 1 534 ? -37.991 60.095 -43.693 1.00 81.52  ? 535  THR A N   1 
ATOM   4257 C CA  . THR A 1 534 ? -38.481 60.391 -45.058 1.00 81.05  ? 535  THR A CA  1 
ATOM   4258 C C   . THR A 1 534 ? -40.017 60.401 -45.178 1.00 91.91  ? 535  THR A C   1 
ATOM   4259 O O   . THR A 1 534 ? -40.697 61.386 -44.831 1.00 104.15 ? 535  THR A O   1 
ATOM   4260 C CB  . THR A 1 534 ? -37.868 59.413 -46.113 1.00 80.92  ? 535  THR A CB  1 
ATOM   4261 O OG1 . THR A 1 534 ? -37.627 58.115 -45.553 1.00 62.19  ? 535  THR A OG1 1 
ATOM   4262 C CG2 . THR A 1 534 ? -36.549 59.917 -46.593 1.00 79.09  ? 535  THR A CG2 1 
ATOM   4263 O OXT . THR A 1 534 ? -40.631 59.441 -45.647 1.00 90.14  ? 535  THR A OXT 1 
HETATM 4264 C C1  . NAG B 2 .   ? -74.449 12.835 -26.679 1.00 67.39  ? 601  NAG A C1  1 
HETATM 4265 C C2  . NAG B 2 .   ? -74.804 11.369 -26.458 1.00 77.42  ? 601  NAG A C2  1 
HETATM 4266 C C3  . NAG B 2 .   ? -74.105 10.479 -27.479 1.00 77.88  ? 601  NAG A C3  1 
HETATM 4267 C C4  . NAG B 2 .   ? -74.303 11.010 -28.893 1.00 82.97  ? 601  NAG A C4  1 
HETATM 4268 C C5  . NAG B 2 .   ? -73.979 12.497 -28.968 1.00 76.77  ? 601  NAG A C5  1 
HETATM 4269 C C6  . NAG B 2 .   ? -74.250 13.046 -30.364 1.00 74.97  ? 601  NAG A C6  1 
HETATM 4270 C C7  . NAG B 2 .   ? -75.333 10.912 -24.135 1.00 73.05  ? 601  NAG A C7  1 
HETATM 4271 C C8  . NAG B 2 .   ? -75.238 9.718  -23.232 1.00 74.36  ? 601  NAG A C8  1 
HETATM 4272 N N2  . NAG B 2 .   ? -74.435 10.967 -25.115 1.00 76.00  ? 601  NAG A N2  1 
HETATM 4273 O O3  . NAG B 2 .   ? -74.630 9.149  -27.391 1.00 83.15  ? 601  NAG A O3  1 
HETATM 4274 O O4  . NAG B 2 .   ? -73.457 10.291 -29.797 1.00 91.25  ? 601  NAG A O4  1 
HETATM 4275 O O5  . NAG B 2 .   ? -74.771 13.205 -28.018 1.00 88.04  ? 601  NAG A O5  1 
HETATM 4276 O O6  . NAG B 2 .   ? -73.269 14.039 -30.686 1.00 66.36  ? 601  NAG A O6  1 
HETATM 4277 O O7  . NAG B 2 .   ? -76.179 11.778 -23.980 1.00 65.14  ? 601  NAG A O7  1 
HETATM 4278 C C1  . NAG C 2 .   ? -37.008 34.761 -10.654 1.00 45.05  ? 602  NAG A C1  1 
HETATM 4279 C C2  . NAG C 2 .   ? -35.514 34.933 -10.703 1.00 49.60  ? 602  NAG A C2  1 
HETATM 4280 C C3  . NAG C 2 .   ? -34.798 34.375 -9.501  1.00 59.50  ? 602  NAG A C3  1 
HETATM 4281 C C4  . NAG C 2 .   ? -35.425 34.931 -8.204  1.00 63.80  ? 602  NAG A C4  1 
HETATM 4282 C C5  . NAG C 2 .   ? -36.964 35.014 -8.196  1.00 59.13  ? 602  NAG A C5  1 
HETATM 4283 C C6  . NAG C 2 .   ? -37.355 36.092 -7.152  1.00 51.72  ? 602  NAG A C6  1 
HETATM 4284 C C7  . NAG C 2 .   ? -34.588 34.940 -12.910 1.00 39.44  ? 602  NAG A C7  1 
HETATM 4285 C C8  . NAG C 2 .   ? -34.132 34.152 -14.086 1.00 41.86  ? 602  NAG A C8  1 
HETATM 4286 N N2  . NAG C 2 .   ? -35.007 34.258 -11.863 1.00 46.99  ? 602  NAG A N2  1 
HETATM 4287 O O3  . NAG C 2 .   ? -33.482 34.861 -9.694  1.00 52.22  ? 602  NAG A O3  1 
HETATM 4288 O O4  . NAG C 2 .   ? -34.924 34.263 -7.048  1.00 75.62  ? 602  NAG A O4  1 
HETATM 4289 O O5  . NAG C 2 .   ? -37.504 35.375 -9.483  1.00 51.17  ? 602  NAG A O5  1 
HETATM 4290 O O6  . NAG C 2 .   ? -38.734 36.278 -6.901  1.00 49.70  ? 602  NAG A O6  1 
HETATM 4291 O O7  . NAG C 2 .   ? -34.596 36.171 -12.949 1.00 43.31  ? 602  NAG A O7  1 
HETATM 4292 C C1  . NAG D 2 .   ? -34.333 35.239 -6.171  1.00 83.66  ? 603  NAG A C1  1 
HETATM 4293 C C2  . NAG D 2 .   ? -34.293 34.686 -4.751  1.00 90.05  ? 603  NAG A C2  1 
HETATM 4294 C C3  . NAG D 2 .   ? -33.658 35.687 -3.793  1.00 96.21  ? 603  NAG A C3  1 
HETATM 4295 C C4  . NAG D 2 .   ? -32.338 36.211 -4.346  1.00 96.60  ? 603  NAG A C4  1 
HETATM 4296 C C5  . NAG D 2 .   ? -32.496 36.673 -5.789  1.00 100.24 ? 603  NAG A C5  1 
HETATM 4297 C C6  . NAG D 2 .   ? -31.161 37.127 -6.367  1.00 88.87  ? 603  NAG A C6  1 
HETATM 4298 C C7  . NAG D 2 .   ? -36.089 33.109 -4.336  1.00 74.10  ? 603  NAG A C7  1 
HETATM 4299 C C8  . NAG D 2 .   ? -37.481 32.913 -3.812  1.00 66.29  ? 603  NAG A C8  1 
HETATM 4300 N N2  . NAG D 2 .   ? -35.634 34.358 -4.308  1.00 82.54  ? 603  NAG A N2  1 
HETATM 4301 O O3  . NAG D 2 .   ? -33.429 35.056 -2.527  1.00 91.59  ? 603  NAG A O3  1 
HETATM 4302 O O4  . NAG D 2 .   ? -31.884 37.305 -3.541  1.00 85.25  ? 603  NAG A O4  1 
HETATM 4303 O O5  . NAG D 2 .   ? -33.016 35.604 -6.576  1.00 93.82  ? 603  NAG A O5  1 
HETATM 4304 O O6  . NAG D 2 .   ? -30.430 35.986 -6.832  1.00 81.69  ? 603  NAG A O6  1 
HETATM 4305 O O7  . NAG D 2 .   ? -35.418 32.182 -4.759  1.00 62.31  ? 603  NAG A O7  1 
HETATM 4306 C CA  . OMI E 3 .   ? -50.879 27.725 -39.150 1.00 79.18  ? 604  OMI A CA  1 
HETATM 4307 C C   . OMI E 3 .   ? -51.948 28.531 -39.191 1.00 77.80  ? 604  OMI A C   1 
HETATM 4308 O O   . OMI E 3 .   ? -52.470 28.976 -38.187 1.00 58.08  ? 604  OMI A O   1 
HETATM 4309 C CAI . OMI E 3 .   ? -52.384 28.670 -40.440 1.00 85.64  ? 604  OMI A CAI 1 
HETATM 4310 C CAE . OMI E 3 .   ? -53.400 29.331 -40.964 1.00 85.54  ? 604  OMI A CAE 1 
HETATM 4311 C CAC . OMI E 3 .   ? -53.635 29.302 -42.324 1.00 90.55  ? 604  OMI A CAC 1 
HETATM 4312 C CAD . OMI E 3 .   ? -52.812 28.567 -43.151 1.00 89.98  ? 604  OMI A CAD 1 
HETATM 4313 C CAF . OMI E 3 .   ? -51.772 27.913 -42.538 1.00 89.32  ? 604  OMI A CAF 1 
HETATM 4314 C CAJ . OMI E 3 .   ? -51.584 27.973 -41.221 1.00 86.45  ? 604  OMI A CAJ 1 
HETATM 4315 N N   . OMI E 3 .   ? -50.630 27.432 -40.551 1.00 80.55  ? 604  OMI A N   1 
HETATM 4316 C CAA . OMI E 3 .   ? -49.467 28.233 -40.893 1.00 87.71  ? 604  OMI A CAA 1 
HETATM 4317 C C1  . PG4 F 4 .   ? -52.115 30.227 -45.953 1.00 58.65  ? 605  PG4 A C1  1 
HETATM 4318 C C2  . PG4 F 4 .   ? -51.776 31.718 -45.926 1.00 61.19  ? 605  PG4 A C2  1 
HETATM 4319 O O2  . PG4 F 4 .   ? -52.888 32.528 -46.462 1.00 66.29  ? 605  PG4 A O2  1 
HETATM 4320 C C3  . PG4 F 4 .   ? -52.505 33.903 -46.292 1.00 67.95  ? 605  PG4 A C3  1 
HETATM 4321 C C4  . PG4 F 4 .   ? -53.609 34.845 -46.677 1.00 64.77  ? 605  PG4 A C4  1 
HETATM 4322 O O3  . PG4 F 4 .   ? -54.659 34.101 -47.327 1.00 76.17  ? 605  PG4 A O3  1 
HETATM 4323 C C5  . PG4 F 4 .   ? -55.089 34.815 -48.516 1.00 73.75  ? 605  PG4 A C5  1 
HETATM 4324 C C6  . PG4 F 4 .   ? -56.544 34.533 -48.827 1.00 69.11  ? 605  PG4 A C6  1 
HETATM 4325 O O4  . PG4 F 4 .   ? -57.166 35.771 -49.154 1.00 67.64  ? 605  PG4 A O4  1 
HETATM 4326 C C7  . PG4 F 4 .   ? -56.701 36.282 -50.421 1.00 70.36  ? 605  PG4 A C7  1 
HETATM 4327 C C8  . PG4 F 4 .   ? -57.474 37.544 -50.745 1.00 73.94  ? 605  PG4 A C8  1 
HETATM 4328 O O5  . PG4 F 4 .   ? -58.552 37.135 -51.621 1.00 64.10  ? 605  PG4 A O5  1 
HETATM 4329 C C   . ACT G 5 .   ? -51.375 32.791 -38.614 1.00 51.70  ? 606  ACT A C   1 
HETATM 4330 O O   . ACT G 5 .   ? -51.357 31.573 -38.934 1.00 59.60  ? 606  ACT A O   1 
HETATM 4331 O OXT . ACT G 5 .   ? -51.863 33.282 -37.568 1.00 37.19  ? 606  ACT A OXT 1 
HETATM 4332 C CH3 . ACT G 5 .   ? -50.801 33.765 -39.634 1.00 52.83  ? 606  ACT A CH3 1 
HETATM 4333 O O   . HOH H 6 .   ? -53.891 9.960  -13.758 1.00 43.54  ? 701  HOH A O   1 
HETATM 4334 O O   . HOH H 6 .   ? -59.783 11.217 -16.229 1.00 34.24  ? 702  HOH A O   1 
HETATM 4335 O O   . HOH H 6 .   ? -34.812 12.792 -33.065 1.00 38.36  ? 703  HOH A O   1 
HETATM 4336 O O   . HOH H 6 .   ? -32.408 19.799 -31.116 1.00 53.89  ? 704  HOH A O   1 
HETATM 4337 O O   . HOH H 6 .   ? -76.333 45.012 -28.402 1.00 59.10  ? 705  HOH A O   1 
HETATM 4338 O O   . HOH H 6 .   ? -32.246 18.438 -23.560 1.00 44.51  ? 706  HOH A O   1 
HETATM 4339 O O   . HOH H 6 .   ? -48.947 4.206  -24.894 1.00 52.10  ? 707  HOH A O   1 
HETATM 4340 O O   . HOH H 6 .   ? -58.804 19.296 -8.184  1.00 49.06  ? 708  HOH A O   1 
HETATM 4341 O O   . HOH H 6 .   ? -36.311 16.132 -42.657 1.00 55.86  ? 709  HOH A O   1 
HETATM 4342 O O   . HOH H 6 .   ? -34.962 38.855 -14.491 1.00 22.96  ? 710  HOH A O   1 
HETATM 4343 O O   . HOH H 6 .   ? -55.877 27.379 -36.344 1.00 23.85  ? 711  HOH A O   1 
HETATM 4344 O O   . HOH H 6 .   ? -43.883 29.556 -60.027 1.00 30.38  ? 712  HOH A O   1 
HETATM 4345 O O   . HOH H 6 .   ? -38.172 46.214 -21.824 1.00 27.40  ? 713  HOH A O   1 
HETATM 4346 O O   . HOH H 6 .   ? -37.735 21.750 -14.509 1.00 37.08  ? 714  HOH A O   1 
HETATM 4347 O O   . HOH H 6 .   ? -76.197 21.256 -14.165 1.00 37.84  ? 715  HOH A O   1 
HETATM 4348 O O   . HOH H 6 .   ? -59.932 39.512 -40.883 1.00 29.61  ? 716  HOH A O   1 
HETATM 4349 O O   . HOH H 6 .   ? -63.900 25.323 -29.509 1.00 30.88  ? 717  HOH A O   1 
HETATM 4350 O O   . HOH H 6 .   ? -60.141 16.509 -35.226 1.00 44.90  ? 718  HOH A O   1 
HETATM 4351 O O   . HOH H 6 .   ? -61.837 51.772 -34.235 1.00 27.56  ? 719  HOH A O   1 
HETATM 4352 O O   . HOH H 6 .   ? -71.709 36.297 -25.441 1.00 29.91  ? 720  HOH A O   1 
HETATM 4353 O O   . HOH H 6 .   ? -30.767 30.455 -51.379 1.00 40.62  ? 721  HOH A O   1 
HETATM 4354 O O   . HOH H 6 .   ? -77.158 30.238 -22.373 1.00 50.62  ? 722  HOH A O   1 
HETATM 4355 O O   . HOH H 6 .   ? -44.552 10.074 -20.847 1.00 56.44  ? 723  HOH A O   1 
HETATM 4356 O O   . HOH H 6 .   ? -62.770 35.283 -41.829 1.00 24.60  ? 724  HOH A O   1 
HETATM 4357 O O   . HOH H 6 .   ? -50.708 39.629 -12.524 1.00 46.46  ? 725  HOH A O   1 
HETATM 4358 O O   . HOH H 6 .   ? -34.983 25.854 -44.994 1.00 41.60  ? 726  HOH A O   1 
HETATM 4359 O O   . HOH H 6 .   ? -71.361 30.215 -28.507 1.00 29.46  ? 727  HOH A O   1 
HETATM 4360 O O   . HOH H 6 .   ? -57.156 24.627 -50.132 1.00 37.36  ? 728  HOH A O   1 
HETATM 4361 O O   . HOH H 6 .   ? -34.693 14.353 -30.583 1.00 41.42  ? 729  HOH A O   1 
HETATM 4362 O O   . HOH H 6 .   ? -45.324 28.397 -36.509 1.00 23.08  ? 730  HOH A O   1 
HETATM 4363 O O   . HOH H 6 .   ? -59.805 27.981 -55.688 1.00 40.45  ? 731  HOH A O   1 
HETATM 4364 O O   . HOH H 6 .   ? -36.555 31.522 -13.893 1.00 47.50  ? 732  HOH A O   1 
HETATM 4365 O O   . HOH H 6 .   ? -44.239 41.076 -61.032 1.00 40.66  ? 733  HOH A O   1 
HETATM 4366 O O   . HOH H 6 .   ? -70.556 31.155 -43.902 1.00 48.31  ? 734  HOH A O   1 
HETATM 4367 O O   . HOH H 6 .   ? -41.210 31.967 -60.893 1.00 31.78  ? 735  HOH A O   1 
HETATM 4368 O O   . HOH H 6 .   ? -34.082 37.748 -63.642 1.00 38.19  ? 736  HOH A O   1 
HETATM 4369 O O   . HOH H 6 .   ? -48.375 33.066 -56.032 1.00 8.46   ? 737  HOH A O   1 
HETATM 4370 O O   . HOH H 6 .   ? -48.813 44.502 -33.204 1.00 24.25  ? 738  HOH A O   1 
HETATM 4371 O O   . HOH H 6 .   ? -34.857 31.837 -40.782 1.00 40.98  ? 739  HOH A O   1 
HETATM 4372 O O   . HOH H 6 .   ? -57.784 21.326 -29.300 1.00 35.39  ? 740  HOH A O   1 
HETATM 4373 O O   . HOH H 6 .   ? -48.538 26.271 -15.995 1.00 37.20  ? 741  HOH A O   1 
HETATM 4374 O O   . HOH H 6 .   ? -48.150 21.051 -37.785 1.00 33.62  ? 742  HOH A O   1 
HETATM 4375 O O   . HOH H 6 .   ? -51.616 16.276 -28.115 1.00 25.62  ? 743  HOH A O   1 
HETATM 4376 O O   . HOH H 6 .   ? -65.481 26.463 -31.235 1.00 31.15  ? 744  HOH A O   1 
HETATM 4377 O O   . HOH H 6 .   ? -70.848 36.702 -33.927 1.00 30.75  ? 745  HOH A O   1 
HETATM 4378 O O   . HOH H 6 .   ? -77.681 28.320 -19.772 1.00 53.04  ? 746  HOH A O   1 
HETATM 4379 O O   . HOH H 6 .   ? -68.456 32.003 -18.416 1.00 45.08  ? 747  HOH A O   1 
HETATM 4380 O O   . HOH H 6 .   ? -45.456 41.338 -45.364 1.00 25.23  ? 748  HOH A O   1 
HETATM 4381 O O   . HOH H 6 .   ? -61.926 12.784 -15.614 1.00 41.33  ? 749  HOH A O   1 
HETATM 4382 O O   . HOH H 6 .   ? -60.348 40.370 -16.127 1.00 37.29  ? 750  HOH A O   1 
HETATM 4383 O O   . HOH H 6 .   ? -59.465 30.117 -51.043 1.00 39.11  ? 751  HOH A O   1 
HETATM 4384 O O   . HOH H 6 .   ? -24.070 31.709 -32.095 1.00 49.28  ? 752  HOH A O   1 
HETATM 4385 O O   . HOH H 6 .   ? -24.360 38.342 -27.223 1.00 51.47  ? 753  HOH A O   1 
HETATM 4386 O O   . HOH H 6 .   ? -76.025 37.012 -35.888 1.00 29.11  ? 754  HOH A O   1 
HETATM 4387 O O   . HOH H 6 .   ? -44.543 26.512 -10.799 1.00 35.43  ? 755  HOH A O   1 
HETATM 4388 O O   . HOH H 6 .   ? -36.444 48.482 -21.981 1.00 49.01  ? 756  HOH A O   1 
HETATM 4389 O O   . HOH H 6 .   ? -30.932 34.797 -50.822 1.00 36.57  ? 757  HOH A O   1 
HETATM 4390 O O   . HOH H 6 .   ? -69.340 38.731 -33.165 1.00 29.64  ? 758  HOH A O   1 
HETATM 4391 O O   . HOH H 6 .   ? -45.839 16.935 -42.011 1.00 35.88  ? 759  HOH A O   1 
HETATM 4392 O O   . HOH H 6 .   ? -27.991 31.322 -19.808 1.00 34.46  ? 760  HOH A O   1 
HETATM 4393 O O   . HOH H 6 .   ? -55.464 26.552 -45.127 1.00 33.61  ? 761  HOH A O   1 
HETATM 4394 O O   . HOH H 6 .   ? -65.864 31.575 -14.830 1.00 33.62  ? 762  HOH A O   1 
HETATM 4395 O O   . HOH H 6 .   ? -77.178 34.883 -27.010 1.00 46.48  ? 763  HOH A O   1 
HETATM 4396 O O   . HOH H 6 .   ? -72.460 52.231 -31.279 1.00 52.17  ? 764  HOH A O   1 
HETATM 4397 O O   . HOH H 6 .   ? -30.969 38.251 -29.377 1.00 36.66  ? 765  HOH A O   1 
HETATM 4398 O O   . HOH H 6 .   ? -44.096 29.623 -44.152 1.00 35.81  ? 766  HOH A O   1 
HETATM 4399 O O   . HOH H 6 .   ? -69.820 45.270 -26.177 1.00 42.15  ? 767  HOH A O   1 
HETATM 4400 O O   . HOH H 6 .   ? -53.764 32.682 -53.670 1.00 48.09  ? 768  HOH A O   1 
HETATM 4401 O O   . HOH H 6 .   ? -48.361 18.757 -12.896 1.00 53.19  ? 769  HOH A O   1 
HETATM 4402 O O   . HOH H 6 .   ? -65.341 51.511 -27.686 1.00 41.10  ? 770  HOH A O   1 
HETATM 4403 O O   . HOH H 6 .   ? -62.644 34.285 -9.863  1.00 54.44  ? 771  HOH A O   1 
HETATM 4404 O O   . HOH H 6 .   ? -36.435 29.348 -15.478 1.00 36.40  ? 772  HOH A O   1 
HETATM 4405 O O   . HOH H 6 .   ? -38.866 33.009 -43.833 1.00 32.61  ? 773  HOH A O   1 
HETATM 4406 O O   . HOH H 6 .   ? -33.560 17.917 -38.459 1.00 39.78  ? 774  HOH A O   1 
HETATM 4407 O O   . HOH H 6 .   ? -59.312 20.591 -41.184 1.00 33.95  ? 775  HOH A O   1 
HETATM 4408 O O   . HOH H 6 .   ? -60.122 26.717 -39.010 1.00 25.14  ? 776  HOH A O   1 
HETATM 4409 O O   . HOH H 6 .   ? -42.151 10.697 -24.108 1.00 31.80  ? 777  HOH A O   1 
HETATM 4410 O O   . HOH H 6 .   ? -63.104 45.999 -26.287 1.00 42.87  ? 778  HOH A O   1 
HETATM 4411 O O   . HOH H 6 .   ? -36.412 12.355 -39.492 1.00 35.29  ? 779  HOH A O   1 
HETATM 4412 O O   . HOH H 6 .   ? -52.185 27.860 -34.702 1.00 24.64  ? 780  HOH A O   1 
HETATM 4413 O O   . HOH H 6 .   ? -56.788 30.464 -16.577 1.00 35.34  ? 781  HOH A O   1 
HETATM 4414 O O   . HOH H 6 .   ? -69.433 34.247 -33.553 1.00 31.78  ? 782  HOH A O   1 
HETATM 4415 O O   . HOH H 6 .   ? -63.095 28.735 -34.459 1.00 26.44  ? 783  HOH A O   1 
HETATM 4416 O O   . HOH H 6 .   ? -28.335 33.692 -22.690 1.00 38.72  ? 784  HOH A O   1 
HETATM 4417 O O   . HOH H 6 .   ? -59.890 45.736 -36.281 1.00 24.42  ? 785  HOH A O   1 
HETATM 4418 O O   . HOH H 6 .   ? -42.443 28.061 -33.929 1.00 29.14  ? 786  HOH A O   1 
HETATM 4419 O O   . HOH H 6 .   ? -66.123 44.690 -31.493 1.00 28.39  ? 787  HOH A O   1 
HETATM 4420 O O   . HOH H 6 .   ? -54.787 53.355 -31.746 1.00 26.92  ? 788  HOH A O   1 
HETATM 4421 O O   . HOH H 6 .   ? -49.733 48.628 -32.752 1.00 24.76  ? 789  HOH A O   1 
HETATM 4422 O O   . HOH H 6 .   ? -51.335 46.335 -38.857 1.00 28.06  ? 790  HOH A O   1 
HETATM 4423 O O   . HOH H 6 .   ? -50.302 35.649 -48.800 1.00 36.16  ? 791  HOH A O   1 
HETATM 4424 O O   . HOH H 6 .   ? -47.335 47.273 -51.540 1.00 48.59  ? 792  HOH A O   1 
HETATM 4425 O O   . HOH H 6 .   ? -57.909 39.141 -39.261 1.00 23.63  ? 793  HOH A O   1 
HETATM 4426 O O   . HOH H 6 .   ? -62.545 47.311 -37.919 1.00 23.42  ? 794  HOH A O   1 
HETATM 4427 O O   . HOH H 6 .   ? -56.430 55.025 -41.060 1.00 37.56  ? 795  HOH A O   1 
HETATM 4428 O O   . HOH H 6 .   ? -60.349 44.782 -33.019 1.00 26.52  ? 796  HOH A O   1 
HETATM 4429 O O   . HOH H 6 .   ? -37.712 29.632 -50.086 1.00 34.51  ? 797  HOH A O   1 
HETATM 4430 O O   . HOH H 6 .   ? -43.061 47.170 -30.472 1.00 48.22  ? 798  HOH A O   1 
HETATM 4431 O O   . HOH H 6 .   ? -51.821 41.201 -54.926 1.00 33.21  ? 799  HOH A O   1 
HETATM 4432 O O   . HOH H 6 .   ? -56.673 33.497 -35.822 1.00 20.62  ? 800  HOH A O   1 
HETATM 4433 O O   . HOH H 6 .   ? -56.200 27.107 -39.183 1.00 24.09  ? 801  HOH A O   1 
HETATM 4434 O O   . HOH H 6 .   ? -55.548 19.359 -38.748 1.00 32.07  ? 802  HOH A O   1 
HETATM 4435 O O   . HOH H 6 .   ? -40.314 34.715 -61.428 1.00 33.96  ? 803  HOH A O   1 
HETATM 4436 O O   . HOH H 6 .   ? -26.619 36.560 -61.400 1.00 50.29  ? 804  HOH A O   1 
HETATM 4437 O O   . HOH H 6 .   ? -36.954 21.935 -47.826 1.00 48.50  ? 805  HOH A O   1 
HETATM 4438 O O   . HOH H 6 .   ? -62.557 31.156 -8.777  1.00 53.62  ? 806  HOH A O   1 
HETATM 4439 O O   . HOH H 6 .   ? -52.901 42.857 -40.366 1.00 28.52  ? 807  HOH A O   1 
HETATM 4440 O O   . HOH H 6 .   ? -51.352 50.273 -17.264 1.00 34.58  ? 808  HOH A O   1 
HETATM 4441 O O   . HOH H 6 .   ? -52.114 29.836 -13.364 1.00 27.07  ? 809  HOH A O   1 
HETATM 4442 O O   . HOH H 6 .   ? -42.479 12.531 -20.495 1.00 58.14  ? 810  HOH A O   1 
HETATM 4443 O O   . HOH H 6 .   ? -66.507 30.838 -45.430 1.00 33.41  ? 811  HOH A O   1 
HETATM 4444 O O   . HOH H 6 .   ? -51.151 37.169 -46.769 1.00 33.18  ? 812  HOH A O   1 
HETATM 4445 O O   . HOH H 6 .   ? -34.845 19.398 -41.852 1.00 42.70  ? 813  HOH A O   1 
HETATM 4446 O O   . HOH H 6 .   ? -56.707 31.331 -49.501 1.00 47.22  ? 814  HOH A O   1 
HETATM 4447 O O   . HOH H 6 .   ? -57.394 27.084 -29.413 1.00 21.43  ? 815  HOH A O   1 
HETATM 4448 O O   . HOH H 6 .   ? -56.090 29.244 -41.040 1.00 29.81  ? 816  HOH A O   1 
HETATM 4449 O O   . HOH H 6 .   ? -47.561 20.059 -52.840 1.00 36.48  ? 817  HOH A O   1 
HETATM 4450 O O   . HOH H 6 .   ? -35.083 24.451 -55.867 1.00 42.96  ? 818  HOH A O   1 
HETATM 4451 O O   . HOH H 6 .   ? -55.929 30.433 -13.585 1.00 33.37  ? 819  HOH A O   1 
HETATM 4452 O O   . HOH H 6 .   ? -36.192 34.186 -42.138 1.00 37.46  ? 820  HOH A O   1 
HETATM 4453 O O   . HOH H 6 .   ? -50.921 43.195 -57.451 1.00 36.48  ? 821  HOH A O   1 
HETATM 4454 O O   . HOH H 6 .   ? -42.891 13.338 -24.488 1.00 33.53  ? 822  HOH A O   1 
HETATM 4455 O O   . HOH H 6 .   ? -32.198 27.374 -16.850 1.00 37.56  ? 823  HOH A O   1 
HETATM 4456 O O   . HOH H 6 .   ? -76.157 39.532 -35.997 1.00 32.90  ? 824  HOH A O   1 
HETATM 4457 O O   . HOH H 6 .   ? -65.719 34.490 -36.368 1.00 27.30  ? 825  HOH A O   1 
HETATM 4458 O O   . HOH H 6 .   ? -37.634 36.947 -18.718 1.00 26.56  ? 826  HOH A O   1 
HETATM 4459 O O   . HOH H 6 .   ? -33.992 35.128 -18.705 1.00 33.73  ? 827  HOH A O   1 
HETATM 4460 O O   . HOH H 6 .   ? -71.226 29.201 -25.987 1.00 29.19  ? 828  HOH A O   1 
HETATM 4461 O O   . HOH H 6 .   ? -56.304 30.834 -45.122 1.00 57.56  ? 829  HOH A O   1 
HETATM 4462 O O   . HOH H 6 .   ? -36.874 11.826 -27.207 1.00 33.67  ? 830  HOH A O   1 
HETATM 4463 O O   . HOH H 6 .   ? -39.172 39.350 -12.986 1.00 37.10  ? 831  HOH A O   1 
HETATM 4464 O O   . HOH H 6 .   ? -21.743 35.387 -54.514 1.00 47.78  ? 832  HOH A O   1 
HETATM 4465 O O   . HOH H 6 .   ? -32.356 26.611 -50.865 1.00 40.84  ? 833  HOH A O   1 
HETATM 4466 O O   . HOH H 6 .   ? -45.676 20.337 -54.823 1.00 36.23  ? 834  HOH A O   1 
HETATM 4467 O O   . HOH H 6 .   ? -54.458 6.220  -19.267 1.00 48.66  ? 835  HOH A O   1 
HETATM 4468 O O   . HOH H 6 .   ? -65.137 38.310 -41.189 1.00 24.85  ? 836  HOH A O   1 
HETATM 4469 O O   . HOH H 6 .   ? -60.385 26.038 -10.715 1.00 26.36  ? 837  HOH A O   1 
HETATM 4470 O O   . HOH H 6 .   ? -32.726 30.159 -24.752 1.00 31.34  ? 838  HOH A O   1 
HETATM 4471 O O   . HOH H 6 .   ? -52.222 40.946 -46.971 1.00 41.80  ? 839  HOH A O   1 
HETATM 4472 O O   . HOH H 6 .   ? -53.337 42.602 -13.373 1.00 27.61  ? 840  HOH A O   1 
HETATM 4473 O O   . HOH H 6 .   ? -45.270 8.480  -36.997 1.00 47.98  ? 841  HOH A O   1 
HETATM 4474 O O   . HOH H 6 .   ? -51.412 39.228 -52.935 1.00 33.58  ? 842  HOH A O   1 
HETATM 4475 O O   . HOH H 6 .   ? -30.805 35.349 -29.602 1.00 28.34  ? 843  HOH A O   1 
HETATM 4476 O O   . HOH H 6 .   ? -21.090 31.853 -22.374 1.00 53.69  ? 844  HOH A O   1 
HETATM 4477 O O   . HOH H 6 .   ? -55.844 40.103 -14.934 1.00 32.09  ? 845  HOH A O   1 
HETATM 4478 O O   . HOH H 6 .   ? -54.462 53.266 -43.960 1.00 46.48  ? 846  HOH A O   1 
HETATM 4479 O O   . HOH H 6 .   ? -44.832 54.480 -28.537 1.00 41.35  ? 847  HOH A O   1 
HETATM 4480 O O   . HOH H 6 .   ? -43.028 37.888 -55.913 1.00 38.04  ? 848  HOH A O   1 
HETATM 4481 O O   . HOH H 6 .   ? -44.506 32.274 -12.362 1.00 41.59  ? 849  HOH A O   1 
HETATM 4482 O O   . HOH H 6 .   ? -36.932 38.192 -12.126 1.00 37.39  ? 850  HOH A O   1 
HETATM 4483 O O   . HOH H 6 .   ? -52.805 45.553 -41.036 1.00 23.08  ? 851  HOH A O   1 
HETATM 4484 O O   . HOH H 6 .   ? -59.957 28.735 -42.598 1.00 43.71  ? 852  HOH A O   1 
HETATM 4485 O O   . HOH H 6 .   ? -45.932 44.276 -56.126 1.00 40.12  ? 853  HOH A O   1 
HETATM 4486 O O   . HOH H 6 .   ? -59.509 45.045 -20.838 1.00 38.03  ? 854  HOH A O   1 
HETATM 4487 O O   . HOH H 6 .   ? -71.529 40.067 -49.427 1.00 42.98  ? 855  HOH A O   1 
HETATM 4488 O O   . HOH H 6 .   ? -68.165 33.457 -35.774 1.00 30.83  ? 856  HOH A O   1 
HETATM 4489 O O   . HOH H 6 .   ? -59.682 50.499 -48.962 1.00 43.93  ? 857  HOH A O   1 
HETATM 4490 O O   . HOH H 6 .   ? -29.672 20.583 -32.864 1.00 48.44  ? 858  HOH A O   1 
HETATM 4491 O O   . HOH H 6 .   ? -67.794 24.160 -42.157 1.00 42.58  ? 859  HOH A O   1 
HETATM 4492 O O   . HOH H 6 .   ? -31.449 48.690 -53.683 1.00 39.26  ? 860  HOH A O   1 
HETATM 4493 O O   . HOH H 6 .   ? -50.321 30.054 -55.627 1.00 42.68  ? 861  HOH A O   1 
HETATM 4494 O O   . HOH H 6 .   ? -37.480 17.258 -23.167 1.00 36.46  ? 862  HOH A O   1 
HETATM 4495 O O   . HOH H 6 .   ? -56.008 56.095 -34.083 1.00 33.84  ? 863  HOH A O   1 
HETATM 4496 O O   . HOH H 6 .   ? -70.278 25.150 -42.186 1.00 39.56  ? 864  HOH A O   1 
HETATM 4497 O O   . HOH H 6 .   ? -46.556 8.449  -24.872 1.00 49.39  ? 865  HOH A O   1 
HETATM 4498 O O   . HOH H 6 .   ? -46.323 40.755 -13.040 1.00 26.64  ? 866  HOH A O   1 
HETATM 4499 O O   . HOH H 6 .   ? -30.805 38.755 -32.102 1.00 37.18  ? 867  HOH A O   1 
HETATM 4500 O O   . HOH H 6 .   ? -46.652 5.970  -26.343 1.00 47.82  ? 868  HOH A O   1 
HETATM 4501 O O   . HOH H 6 .   ? -63.853 38.763 -21.275 1.00 36.35  ? 869  HOH A O   1 
HETATM 4502 O O   . HOH H 6 .   ? -59.991 13.500 -28.584 1.00 34.66  ? 870  HOH A O   1 
HETATM 4503 O O   . HOH H 6 .   ? -63.317 54.286 -44.441 1.00 43.63  ? 871  HOH A O   1 
HETATM 4504 O O   . HOH H 6 .   ? -40.158 44.315 -38.743 1.00 35.16  ? 872  HOH A O   1 
HETATM 4505 O O   . HOH H 6 .   ? -38.132 57.335 -51.177 1.00 45.51  ? 873  HOH A O   1 
HETATM 4506 O O   . HOH H 6 .   ? -64.869 35.674 -40.129 1.00 25.46  ? 874  HOH A O   1 
HETATM 4507 O O   . HOH H 6 .   ? -60.778 38.622 -13.238 1.00 41.63  ? 875  HOH A O   1 
HETATM 4508 O O   . HOH H 6 .   ? -53.598 1.722  -20.186 1.00 53.81  ? 876  HOH A O   1 
HETATM 4509 O O   . HOH H 6 .   ? -66.473 15.344 -32.296 1.00 36.97  ? 877  HOH A O   1 
HETATM 4510 O O   . HOH H 6 .   ? -39.573 47.208 -39.684 1.00 42.98  ? 878  HOH A O   1 
HETATM 4511 O O   . HOH H 6 .   ? -29.542 28.199 -18.097 1.00 43.13  ? 879  HOH A O   1 
HETATM 4512 O O   . HOH H 6 .   ? -78.255 36.779 -28.643 1.00 38.79  ? 880  HOH A O   1 
HETATM 4513 O O   . HOH H 6 .   ? -60.866 56.566 -39.492 1.00 35.77  ? 881  HOH A O   1 
HETATM 4514 O O   . HOH H 6 .   ? -78.115 50.248 -43.834 1.00 42.10  ? 882  HOH A O   1 
HETATM 4515 O O   . HOH H 6 .   ? -40.953 19.339 -53.595 1.00 33.07  ? 883  HOH A O   1 
HETATM 4516 O O   . HOH H 6 .   ? -46.356 50.275 -30.353 1.00 22.85  ? 884  HOH A O   1 
HETATM 4517 O O   . HOH H 6 .   ? -37.568 42.505 -12.847 1.00 33.34  ? 885  HOH A O   1 
HETATM 4518 O O   . HOH H 6 .   ? -47.518 16.811 -14.495 1.00 49.92  ? 886  HOH A O   1 
HETATM 4519 O O   . HOH H 6 .   ? -27.930 28.831 -55.434 1.00 41.83  ? 887  HOH A O   1 
HETATM 4520 O O   . HOH H 6 .   ? -46.005 22.525 -10.419 1.00 46.66  ? 888  HOH A O   1 
HETATM 4521 O O   . HOH H 6 .   ? -58.139 18.895 -39.179 1.00 32.07  ? 889  HOH A O   1 
HETATM 4522 O O   . HOH H 6 .   ? -37.072 18.017 -20.592 1.00 50.71  ? 890  HOH A O   1 
HETATM 4523 O O   . HOH H 6 .   ? -48.535 30.852 -59.310 1.00 40.82  ? 891  HOH A O   1 
HETATM 4524 O O   . HOH H 6 .   ? -57.034 21.885 -8.175  1.00 49.24  ? 892  HOH A O   1 
HETATM 4525 O O   . HOH H 6 .   ? -62.198 38.319 -16.788 1.00 34.65  ? 893  HOH A O   1 
HETATM 4526 O O   . HOH H 6 .   ? -47.445 46.669 -14.089 1.00 35.58  ? 894  HOH A O   1 
HETATM 4527 O O   . HOH H 6 .   ? -52.686 46.244 -46.337 1.00 24.93  ? 895  HOH A O   1 
HETATM 4528 O O   . HOH H 6 .   ? -52.234 15.820 -9.222  1.00 48.17  ? 896  HOH A O   1 
HETATM 4529 O O   . HOH H 6 .   ? -73.965 31.087 -38.044 1.00 33.93  ? 897  HOH A O   1 
HETATM 4530 O O   . HOH H 6 .   ? -29.470 37.900 -39.698 1.00 29.16  ? 898  HOH A O   1 
HETATM 4531 O O   . HOH H 6 .   ? -34.673 44.985 -30.844 1.00 31.42  ? 899  HOH A O   1 
HETATM 4532 O O   . HOH H 6 .   ? -48.717 50.060 -30.621 1.00 25.77  ? 900  HOH A O   1 
HETATM 4533 O O   . HOH H 6 .   ? -48.944 55.345 -26.043 1.00 44.69  ? 901  HOH A O   1 
HETATM 4534 O O   . HOH H 6 .   ? -27.242 37.637 -38.305 1.00 33.05  ? 902  HOH A O   1 
HETATM 4535 O O   . HOH H 6 .   ? -51.273 32.287 -12.177 1.00 26.31  ? 903  HOH A O   1 
HETATM 4536 O O   . HOH H 6 .   ? -31.021 53.111 -54.475 1.00 50.21  ? 904  HOH A O   1 
HETATM 4537 O O   . HOH H 6 .   ? -41.828 20.465 -40.069 1.00 44.17  ? 905  HOH A O   1 
HETATM 4538 O O   . HOH H 6 .   ? -59.909 46.605 -38.635 1.00 32.68  ? 906  HOH A O   1 
HETATM 4539 O O   . HOH H 6 .   ? -37.527 5.834  -39.012 1.00 42.94  ? 907  HOH A O   1 
HETATM 4540 O O   . HOH H 6 .   ? -41.635 45.755 -33.024 1.00 31.27  ? 908  HOH A O   1 
HETATM 4541 O O   . HOH H 6 .   ? -52.563 49.418 -42.130 1.00 29.08  ? 909  HOH A O   1 
HETATM 4542 O O   . HOH H 6 .   ? -31.146 26.527 -40.224 1.00 38.89  ? 910  HOH A O   1 
HETATM 4543 O O   . HOH H 6 .   ? -39.410 22.839 -54.539 1.00 25.18  ? 911  HOH A O   1 
HETATM 4544 O O   . HOH H 6 .   ? -49.387 34.262 -11.872 1.00 30.77  ? 912  HOH A O   1 
HETATM 4545 O O   . HOH H 6 .   ? -73.739 28.053 -25.548 1.00 36.48  ? 913  HOH A O   1 
HETATM 4546 O O   . HOH H 6 .   ? -39.189 46.362 -33.647 1.00 38.83  ? 914  HOH A O   1 
HETATM 4547 O O   . HOH H 6 .   ? -46.621 34.439 -12.593 1.00 44.46  ? 915  HOH A O   1 
HETATM 4548 O O   . HOH H 6 .   ? -52.844 50.968 -38.126 1.00 25.26  ? 916  HOH A O   1 
HETATM 4549 O O   . HOH H 6 .   ? -53.531 15.478 -50.301 1.00 42.11  ? 917  HOH A O   1 
HETATM 4550 O O   . HOH H 6 .   ? -60.673 8.944  -11.906 1.00 45.97  ? 918  HOH A O   1 
HETATM 4551 O O   . HOH H 6 .   ? -63.403 26.370 -33.177 1.00 32.87  ? 919  HOH A O   1 
HETATM 4552 O O   . HOH H 6 .   ? -50.410 49.481 -51.997 1.00 36.78  ? 920  HOH A O   1 
HETATM 4553 O O   . HOH H 6 .   ? -42.136 48.058 -14.440 1.00 49.73  ? 921  HOH A O   1 
HETATM 4554 O O   . HOH H 6 .   ? -41.817 56.807 -52.286 1.00 39.35  ? 922  HOH A O   1 
HETATM 4555 O O   . HOH H 6 .   ? -40.065 54.437 -58.780 1.00 62.36  ? 923  HOH A O   1 
HETATM 4556 O O   . HOH H 6 .   ? -60.447 35.747 -10.934 1.00 40.66  ? 924  HOH A O   1 
HETATM 4557 O O   . HOH H 6 .   ? -54.129 7.018  -30.968 1.00 33.93  ? 925  HOH A O   1 
HETATM 4558 O O   . HOH H 6 .   ? -44.876 34.739 -62.585 1.00 49.30  ? 926  HOH A O   1 
HETATM 4559 O O   . HOH H 6 .   ? -79.483 41.138 -35.516 1.00 63.25  ? 927  HOH A O   1 
HETATM 4560 O O   . HOH H 6 .   ? -60.021 11.201 -30.559 1.00 41.39  ? 928  HOH A O   1 
HETATM 4561 O O   . HOH H 6 .   ? -52.566 23.727 -3.342  1.00 34.87  ? 929  HOH A O   1 
HETATM 4562 O O   . HOH H 6 .   ? -57.590 49.735 -51.050 1.00 45.44  ? 930  HOH A O   1 
HETATM 4563 O O   . HOH H 6 .   ? -68.007 29.782 -13.910 1.00 36.57  ? 931  HOH A O   1 
HETATM 4564 O O   . HOH H 6 .   ? -57.311 28.345 -43.502 1.00 41.20  ? 932  HOH A O   1 
HETATM 4565 O O   . HOH H 6 .   ? -52.419 32.248 -42.206 1.00 65.70  ? 933  HOH A O   1 
HETATM 4566 O O   . HOH H 6 .   ? -69.102 19.971 -6.568  1.00 46.01  ? 934  HOH A O   1 
HETATM 4567 O O   . HOH H 6 .   ? -57.392 35.579 -11.209 1.00 46.43  ? 935  HOH A O   1 
HETATM 4568 O O   . HOH H 6 .   ? -26.094 34.615 -51.246 1.00 45.80  ? 936  HOH A O   1 
HETATM 4569 O O   . HOH H 6 .   ? -38.064 12.684 -24.988 1.00 40.56  ? 937  HOH A O   1 
HETATM 4570 O O   . HOH H 6 .   ? -31.569 24.076 -15.997 1.00 41.61  ? 938  HOH A O   1 
HETATM 4571 O O   . HOH H 6 .   ? -44.411 47.272 -43.887 1.00 31.59  ? 939  HOH A O   1 
HETATM 4572 O O   . HOH H 6 .   ? -57.299 4.534  -15.911 1.00 47.26  ? 940  HOH A O   1 
HETATM 4573 O O   . HOH H 6 .   ? -42.969 31.214 -10.625 1.00 43.51  ? 941  HOH A O   1 
HETATM 4574 O O   . HOH H 6 .   ? -31.071 38.689 -18.196 1.00 41.76  ? 942  HOH A O   1 
HETATM 4575 O O   . HOH H 6 .   ? -57.751 0.955  -20.387 1.00 47.39  ? 943  HOH A O   1 
HETATM 4576 O O   . HOH H 6 .   ? -61.494 20.049 -42.918 1.00 57.12  ? 944  HOH A O   1 
HETATM 4577 O O   . HOH H 6 .   ? -56.087 4.396  -18.137 1.00 52.50  ? 945  HOH A O   1 
HETATM 4578 O O   . HOH H 6 .   ? -64.540 43.806 -21.254 1.00 47.12  ? 946  HOH A O   1 
HETATM 4579 O O   . HOH H 6 .   ? -54.326 40.630 -49.288 1.00 41.86  ? 947  HOH A O   1 
HETATM 4580 O O   . HOH H 6 .   ? -74.346 25.358 -10.847 1.00 48.78  ? 948  HOH A O   1 
HETATM 4581 O O   . HOH H 6 .   ? -49.134 48.455 -36.204 1.00 41.95  ? 949  HOH A O   1 
HETATM 4582 O O   . HOH H 6 .   ? -69.500 55.757 -39.513 1.00 43.48  ? 950  HOH A O   1 
HETATM 4583 O O   . HOH H 6 .   ? -65.929 40.522 -21.642 1.00 38.94  ? 951  HOH A O   1 
HETATM 4584 O O   . HOH H 6 .   ? -69.098 22.505 -7.726  1.00 45.07  ? 952  HOH A O   1 
HETATM 4585 O O   . HOH H 6 .   ? -39.076 8.333  -29.206 1.00 47.56  ? 953  HOH A O   1 
HETATM 4586 O O   . HOH H 6 .   ? -80.468 51.961 -37.597 1.00 50.70  ? 954  HOH A O   1 
HETATM 4587 O O   . HOH H 6 .   ? -42.867 17.267 -51.748 1.00 48.04  ? 955  HOH A O   1 
HETATM 4588 O O   . HOH H 6 .   ? -38.011 51.656 -56.142 1.00 53.43  ? 956  HOH A O   1 
HETATM 4589 O O   . HOH H 6 .   ? -56.031 0.000  -22.840 0.50 61.52  ? 957  HOH A O   1 
HETATM 4590 O O   . HOH H 6 .   ? -34.984 24.792 -49.381 1.00 46.61  ? 958  HOH A O   1 
HETATM 4591 O O   . HOH H 6 .   ? -51.778 46.904 -43.680 1.00 24.02  ? 959  HOH A O   1 
HETATM 4592 O O   . HOH H 6 .   ? -78.411 20.946 -20.785 1.00 41.83  ? 960  HOH A O   1 
HETATM 4593 O O   . HOH H 6 .   ? -51.001 50.700 -33.758 1.00 42.92  ? 961  HOH A O   1 
HETATM 4594 O O   . HOH H 6 .   ? -77.907 36.757 -39.524 1.00 51.66  ? 962  HOH A O   1 
HETATM 4595 O O   . HOH H 6 .   ? -63.225 56.261 -40.797 1.00 49.22  ? 963  HOH A O   1 
HETATM 4596 O O   . HOH H 6 .   ? -63.595 37.541 -18.817 1.00 34.16  ? 964  HOH A O   1 
HETATM 4597 O O   . HOH H 6 .   ? -60.318 57.431 -34.847 1.00 42.64  ? 965  HOH A O   1 
HETATM 4598 O O   . HOH H 6 .   ? -47.114 6.808  -20.297 1.00 51.54  ? 966  HOH A O   1 
HETATM 4599 O O   . HOH H 6 .   ? -35.908 38.780 -9.804  1.00 45.45  ? 967  HOH A O   1 
HETATM 4600 O O   . HOH H 6 .   ? -56.086 55.152 -27.918 1.00 45.72  ? 968  HOH A O   1 
HETATM 4601 O O   . HOH H 6 .   ? -43.111 12.973 -17.761 1.00 50.62  ? 969  HOH A O   1 
HETATM 4602 O O   . HOH H 6 .   ? -71.942 48.736 -22.298 1.00 57.66  ? 970  HOH A O   1 
HETATM 4603 O O   . HOH H 6 .   ? -35.301 23.347 -52.078 1.00 46.69  ? 971  HOH A O   1 
HETATM 4604 O O   . HOH H 6 .   ? -52.454 52.073 -42.736 1.00 40.08  ? 972  HOH A O   1 
HETATM 4605 O O   . HOH H 6 .   ? -45.342 48.060 -31.351 1.00 36.71  ? 973  HOH A O   1 
HETATM 4606 O O   . HOH H 6 .   ? -42.664 54.424 -27.204 1.00 46.43  ? 974  HOH A O   1 
HETATM 4607 O O   . HOH H 6 .   ? -36.858 22.861 -54.441 1.00 38.51  ? 975  HOH A O   1 
HETATM 4608 O O   . HOH H 6 .   ? -26.347 39.035 -49.207 1.00 44.78  ? 976  HOH A O   1 
HETATM 4609 O O   . HOH H 6 .   ? -51.307 49.256 -39.931 1.00 38.61  ? 977  HOH A O   1 
HETATM 4610 O O   . HOH H 6 .   ? -35.252 26.547 -48.118 1.00 35.69  ? 978  HOH A O   1 
HETATM 4611 O O   . HOH H 6 .   ? -54.058 54.778 -27.637 1.00 38.29  ? 979  HOH A O   1 
HETATM 4612 O O   . HOH H 6 .   ? -29.202 51.655 -37.209 1.00 35.12  ? 980  HOH A O   1 
HETATM 4613 O O   . HOH H 6 .   ? -71.818 31.263 -13.309 1.00 39.44  ? 981  HOH A O   1 
HETATM 4614 O O   . HOH H 6 .   ? -41.398 21.118 -56.197 1.00 44.00  ? 982  HOH A O   1 
HETATM 4615 O O   . HOH H 6 .   ? -35.967 22.736 -45.261 1.00 40.63  ? 983  HOH A O   1 
HETATM 4616 O O   . HOH H 6 .   ? -43.170 47.605 -39.756 1.00 42.22  ? 984  HOH A O   1 
HETATM 4617 O O   . HOH H 6 .   ? -66.476 24.607 -43.860 1.00 50.90  ? 985  HOH A O   1 
HETATM 4618 O O   . HOH H 6 .   ? -34.091 40.317 -12.546 1.00 50.16  ? 986  HOH A O   1 
HETATM 4619 O O   . HOH H 6 .   ? -31.863 36.517 -17.066 1.00 44.26  ? 987  HOH A O   1 
HETATM 4620 O O   . HOH H 6 .   ? -55.467 48.525 -52.783 1.00 39.58  ? 988  HOH A O   1 
HETATM 4621 O O   . HOH H 6 .   ? -52.286 52.897 -40.111 1.00 43.30  ? 989  HOH A O   1 
HETATM 4622 O O   . HOH H 6 .   ? -52.224 52.990 -32.288 1.00 29.91  ? 990  HOH A O   1 
HETATM 4623 O O   . HOH H 6 .   ? -24.337 38.658 -49.869 1.00 50.31  ? 991  HOH A O   1 
HETATM 4624 O O   . HOH H 6 .   ? -55.034 55.898 -31.256 1.00 43.57  ? 992  HOH A O   1 
HETATM 4625 O O   . HOH H 6 .   ? -61.646 13.214 -30.194 1.00 46.77  ? 993  HOH A O   1 
HETATM 4626 O O   . HOH H 6 .   ? -42.586 48.877 -42.385 1.00 50.63  ? 994  HOH A O   1 
HETATM 4627 O O   . HOH H 6 .   ? -52.041 55.185 -28.563 1.00 35.46  ? 995  HOH A O   1 
HETATM 4628 O O   . HOH H 6 .   ? -63.192 56.253 -43.288 1.00 44.87  ? 996  HOH A O   1 
HETATM 4629 O O   . HOH H 6 .   ? -37.295 9.253  -27.532 1.00 39.55  ? 997  HOH A O   1 
HETATM 4630 O O   . HOH H 6 .   ? -39.851 10.642 -23.657 1.00 33.61  ? 998  HOH A O   1 
HETATM 4631 O O   . HOH H 6 .   ? -50.017 52.548 -30.731 1.00 40.17  ? 999  HOH A O   1 
HETATM 4632 O O   . HOH H 6 .   ? -40.759 49.002 -40.638 1.00 45.17  ? 1000 HOH A O   1 
HETATM 4633 O O   . HOH H 6 .   ? -47.969 54.836 -31.449 1.00 48.28  ? 1001 HOH A O   1 
HETATM 4634 O O   . HOH H 6 .   ? -79.331 48.457 -44.047 1.00 48.16  ? 1002 HOH A O   1 
HETATM 4635 O O   . HOH H 6 .   ? -25.415 36.875 -47.923 1.00 54.35  ? 1003 HOH A 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   ASP 1   2   2   ASP ASP A . n 
A 1 2   HIS 2   3   3   HIS HIS A . n 
A 1 3   SER 3   4   4   SER SER A . n 
A 1 4   GLU 4   5   5   GLU GLU A . n 
A 1 5   LEU 5   6   6   LEU LEU A . n 
A 1 6   LEU 6   7   7   LEU LEU A . n 
A 1 7   VAL 7   8   8   VAL VAL A . n 
A 1 8   ASN 8   9   9   ASN ASN A . n 
A 1 9   THR 9   10  10  THR THR A . n 
A 1 10  LYS 10  11  11  LYS LYS A . n 
A 1 11  SER 11  12  12  SER SER A . n 
A 1 12  GLY 12  13  13  GLY GLY A . n 
A 1 13  LYS 13  14  14  LYS LYS A . n 
A 1 14  VAL 14  15  15  VAL VAL A . n 
A 1 15  MET 15  16  16  MET MET A . n 
A 1 16  GLY 16  17  17  GLY GLY A . n 
A 1 17  THR 17  18  18  THR THR A . n 
A 1 18  ARG 18  19  19  ARG ARG A . n 
A 1 19  VAL 19  20  20  VAL VAL A . n 
A 1 20  PRO 20  21  21  PRO PRO A . n 
A 1 21  VAL 21  22  22  VAL VAL A . n 
A 1 22  LEU 22  23  23  LEU LEU A . n 
A 1 23  SER 23  24  24  SER SER A . n 
A 1 24  SER 24  25  25  SER SER A . n 
A 1 25  HIS 25  26  26  HIS HIS A . n 
A 1 26  ILE 26  27  27  ILE ILE A . n 
A 1 27  SER 27  28  28  SER SER A . n 
A 1 28  ALA 28  29  29  ALA ALA A . n 
A 1 29  PHE 29  30  30  PHE PHE A . n 
A 1 30  LEU 30  31  31  LEU LEU A . n 
A 1 31  GLY 31  32  32  GLY GLY A . n 
A 1 32  ILE 32  33  33  ILE ILE A . n 
A 1 33  PRO 33  34  34  PRO PRO A . n 
A 1 34  PHE 34  35  35  PHE PHE A . n 
A 1 35  ALA 35  36  36  ALA ALA A . n 
A 1 36  GLU 36  37  37  GLU GLU A . n 
A 1 37  PRO 37  38  38  PRO PRO A . n 
A 1 38  PRO 38  39  39  PRO PRO A . n 
A 1 39  VAL 39  40  40  VAL VAL A . n 
A 1 40  GLY 40  41  41  GLY GLY A . n 
A 1 41  ASN 41  42  42  ASN ASN A . n 
A 1 42  MET 42  43  43  MET MET A . n 
A 1 43  ARG 43  44  44  ARG ARG A . n 
A 1 44  PHE 44  45  45  PHE PHE A . n 
A 1 45  ARG 45  46  46  ARG ARG A . n 
A 1 46  ARG 46  47  47  ARG ARG A . n 
A 1 47  PRO 47  48  48  PRO PRO A . n 
A 1 48  GLU 48  49  49  GLU GLU A . n 
A 1 49  PRO 49  50  50  PRO PRO A . n 
A 1 50  LYS 50  51  51  LYS LYS A . n 
A 1 51  LYS 51  52  52  LYS LYS A . n 
A 1 52  PRO 52  53  53  PRO PRO A . n 
A 1 53  TRP 53  54  54  TRP TRP A . n 
A 1 54  SER 54  55  55  SER SER A . n 
A 1 55  GLY 55  56  56  GLY GLY A . n 
A 1 56  VAL 56  57  57  VAL VAL A . n 
A 1 57  TRP 57  58  58  TRP TRP A . n 
A 1 58  ASN 58  59  59  ASN ASN A . n 
A 1 59  ALA 59  60  60  ALA ALA A . n 
A 1 60  SER 60  61  61  SER SER A . n 
A 1 61  THR 61  62  62  THR THR A . n 
A 1 62  TYR 62  63  63  TYR TYR A . n 
A 1 63  PRO 63  64  64  PRO PRO A . n 
A 1 64  ASN 64  65  65  ASN ASN A . n 
A 1 65  ASN 65  66  66  ASN ASN A . n 
A 1 66  CYS 66  67  67  CYS CYS A . n 
A 1 67  GLN 67  68  68  GLN GLN A . n 
A 1 68  GLN 68  69  69  GLN GLN A . n 
A 1 69  TYR 69  70  70  TYR TYR A . n 
A 1 70  VAL 70  71  71  VAL VAL A . n 
A 1 71  ASP 71  72  72  ASP ASP A . n 
A 1 72  GLU 72  73  73  GLU GLU A . n 
A 1 73  GLN 73  74  74  GLN GLN A . n 
A 1 74  PHE 74  75  75  PHE PHE A . n 
A 1 75  PRO 75  76  76  PRO PRO A . n 
A 1 76  GLY 76  77  77  GLY GLY A . n 
A 1 77  PHE 77  78  78  PHE PHE A . n 
A 1 78  SER 78  79  79  SER SER A . n 
A 1 79  GLY 79  80  80  GLY GLY A . n 
A 1 80  SER 80  81  81  SER SER A . n 
A 1 81  GLU 81  82  82  GLU GLU A . n 
A 1 82  MET 82  83  83  MET MET A . n 
A 1 83  TRP 83  84  84  TRP TRP A . n 
A 1 84  ASN 84  85  85  ASN ASN A . n 
A 1 85  PRO 85  86  86  PRO PRO A . n 
A 1 86  ASN 86  87  87  ASN ASN A . n 
A 1 87  ARG 87  88  88  ARG ARG A . n 
A 1 88  GLU 88  89  89  GLU GLU A . n 
A 1 89  MET 89  90  90  MET MET A . n 
A 1 90  SER 90  91  91  SER SER A . n 
A 1 91  GLU 91  92  92  GLU GLU A . n 
A 1 92  ASP 92  93  93  ASP ASP A . n 
A 1 93  CYS 93  94  94  CYS CYS A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  TYR 95  96  96  TYR TYR A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  ASN 97  98  98  ASN ASN A . n 
A 1 98  ILE 98  99  99  ILE ILE A . n 
A 1 99  TRP 99  100 100 TRP TRP A . n 
A 1 100 VAL 100 101 101 VAL VAL A . n 
A 1 101 PRO 101 102 102 PRO PRO A . n 
A 1 102 SER 102 103 103 SER SER A . n 
A 1 103 PRO 103 104 104 PRO PRO A . n 
A 1 104 ARG 104 105 105 ARG ARG A . n 
A 1 105 PRO 105 106 106 PRO PRO A . n 
A 1 106 LYS 106 107 107 LYS LYS A . n 
A 1 107 SER 107 108 108 SER SER A . n 
A 1 108 THR 108 109 109 THR THR A . n 
A 1 109 THR 109 110 110 THR THR A . n 
A 1 110 VAL 110 111 111 VAL VAL A . n 
A 1 111 MET 111 112 112 MET MET A . n 
A 1 112 VAL 112 113 113 VAL VAL A . n 
A 1 113 TRP 113 114 114 TRP TRP A . n 
A 1 114 ILE 114 115 115 ILE ILE A . n 
A 1 115 TYR 115 116 116 TYR TYR A . n 
A 1 116 GLY 116 117 117 GLY GLY A . n 
A 1 117 GLY 117 118 118 GLY GLY A . n 
A 1 118 GLY 118 119 119 GLY GLY A . n 
A 1 119 PHE 119 120 120 PHE PHE A . n 
A 1 120 TYR 120 121 121 TYR TYR A . n 
A 1 121 SER 121 122 122 SER SER A . n 
A 1 122 GLY 122 123 123 GLY GLY A . n 
A 1 123 SER 123 124 124 SER SER A . n 
A 1 124 SER 124 125 125 SER SER A . n 
A 1 125 THR 125 126 126 THR THR A . n 
A 1 126 LEU 126 127 127 LEU LEU A . n 
A 1 127 ASP 127 128 128 ASP ASP A . n 
A 1 128 VAL 128 129 129 VAL VAL A . n 
A 1 129 TYR 129 130 130 TYR TYR A . n 
A 1 130 ASN 130 131 131 ASN ASN A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 TYR 133 134 134 TYR TYR A . n 
A 1 134 LEU 134 135 135 LEU LEU A . n 
A 1 135 ALA 135 136 136 ALA ALA A . n 
A 1 136 TYR 136 137 137 TYR TYR A . n 
A 1 137 THR 137 138 138 THR THR A . n 
A 1 138 GLU 138 139 139 GLU GLU A . n 
A 1 139 GLU 139 140 140 GLU GLU A . n 
A 1 140 VAL 140 141 141 VAL VAL A . n 
A 1 141 VAL 141 142 142 VAL VAL A . n 
A 1 142 LEU 142 143 143 LEU LEU A . n 
A 1 143 VAL 143 144 144 VAL VAL A . n 
A 1 144 SER 144 145 145 SER SER A . n 
A 1 145 LEU 145 146 146 LEU LEU A . n 
A 1 146 SER 146 147 147 SER SER A . n 
A 1 147 TYR 147 148 148 TYR TYR A . n 
A 1 148 ARG 148 149 149 ARG ARG A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 ALA 151 152 152 ALA ALA A . n 
A 1 152 PHE 152 153 153 PHE PHE A . n 
A 1 153 GLY 153 154 154 GLY GLY A . n 
A 1 154 PHE 154 155 155 PHE PHE A . n 
A 1 155 LEU 155 156 156 LEU LEU A . n 
A 1 156 ALA 156 157 157 ALA ALA A . n 
A 1 157 LEU 157 158 158 LEU LEU A . n 
A 1 158 HIS 158 159 159 HIS HIS A . n 
A 1 159 GLY 159 160 160 GLY GLY A . n 
A 1 160 SER 160 161 161 SER SER A . n 
A 1 161 GLN 161 162 162 GLN GLN A . n 
A 1 162 GLU 162 163 163 GLU GLU A . n 
A 1 163 ALA 163 164 164 ALA ALA A . n 
A 1 164 PRO 164 165 165 PRO PRO A . n 
A 1 165 GLY 165 166 166 GLY GLY A . n 
A 1 166 ASN 166 167 167 ASN ASN A . n 
A 1 167 VAL 167 168 168 VAL VAL A . n 
A 1 168 GLY 168 169 169 GLY GLY A . n 
A 1 169 LEU 169 170 170 LEU LEU A . n 
A 1 170 LEU 170 171 171 LEU LEU A . n 
A 1 171 ASP 171 172 172 ASP ASP A . n 
A 1 172 GLN 172 173 173 GLN GLN A . n 
A 1 173 ARG 173 174 174 ARG ARG A . n 
A 1 174 MET 174 175 175 MET MET A . n 
A 1 175 ALA 175 176 176 ALA ALA A . n 
A 1 176 LEU 176 177 177 LEU LEU A . n 
A 1 177 GLN 177 178 178 GLN GLN A . n 
A 1 178 TRP 178 179 179 TRP TRP A . n 
A 1 179 VAL 179 180 180 VAL VAL A . n 
A 1 180 HIS 180 181 181 HIS HIS A . n 
A 1 181 ASP 181 182 182 ASP ASP A . n 
A 1 182 ASN 182 183 183 ASN ASN A . n 
A 1 183 ILE 183 184 184 ILE ILE A . n 
A 1 184 GLN 184 185 185 GLN GLN A . n 
A 1 185 PHE 185 186 186 PHE PHE A . n 
A 1 186 PHE 186 187 187 PHE PHE A . n 
A 1 187 GLY 187 188 188 GLY GLY A . n 
A 1 188 GLY 188 189 189 GLY GLY A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 PRO 190 191 191 PRO PRO A . n 
A 1 191 LYS 191 192 192 LYS LYS A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 VAL 193 194 194 VAL VAL A . n 
A 1 194 THR 194 195 195 THR THR A . n 
A 1 195 ILE 195 196 196 ILE ILE A . n 
A 1 196 PHE 196 197 197 PHE PHE A . n 
A 1 197 GLY 197 198 198 GLY GLY A . n 
A 1 198 GLU 198 199 199 GLU GLU A . n 
A 1 199 SER 199 200 200 SER SER A . n 
A 1 200 ALA 200 201 201 ALA ALA A . n 
A 1 201 GLY 201 202 202 GLY GLY A . n 
A 1 202 GLY 202 203 203 GLY GLY A . n 
A 1 203 ALA 203 204 204 ALA ALA A . n 
A 1 204 SER 204 205 205 SER SER A . n 
A 1 205 VAL 205 206 206 VAL VAL A . n 
A 1 206 GLY 206 207 207 GLY GLY A . n 
A 1 207 MET 207 208 208 MET MET A . n 
A 1 208 HIS 208 209 209 HIS HIS A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 LEU 210 211 211 LEU LEU A . n 
A 1 211 SER 211 212 212 SER SER A . n 
A 1 212 PRO 212 213 213 PRO PRO A . n 
A 1 213 GLY 213 214 214 GLY GLY A . n 
A 1 214 SER 214 215 215 SER SER A . n 
A 1 215 ARG 215 216 216 ARG ARG A . n 
A 1 216 ASP 216 217 217 ASP ASP A . n 
A 1 217 LEU 217 218 218 LEU LEU A . n 
A 1 218 PHE 218 219 219 PHE PHE A . n 
A 1 219 ARG 219 220 220 ARG ARG A . n 
A 1 220 ARG 220 221 221 ARG ARG A . n 
A 1 221 ALA 221 222 222 ALA ALA A . n 
A 1 222 ILE 222 223 223 ILE ILE A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 GLN 224 225 225 GLN GLN A . n 
A 1 225 SER 225 226 226 SER SER A . n 
A 1 226 GLY 226 227 227 GLY GLY A . n 
A 1 227 SER 227 228 228 SER SER A . n 
A 1 228 PRO 228 229 229 PRO PRO A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 CYS 230 231 231 CYS CYS A . n 
A 1 231 PRO 231 232 232 PRO PRO A . n 
A 1 232 TRP 232 233 233 TRP TRP A . n 
A 1 233 ALA 233 234 234 ALA ALA A . n 
A 1 234 SER 234 235 235 SER SER A . n 
A 1 235 VAL 235 236 236 VAL VAL A . n 
A 1 236 SER 236 237 237 SER SER A . n 
A 1 237 VAL 237 238 238 VAL VAL A . n 
A 1 238 ALA 238 239 239 ALA ALA A . n 
A 1 239 GLU 239 240 240 GLU GLU A . n 
A 1 240 GLY 240 241 241 GLY GLY A . n 
A 1 241 ARG 241 242 242 ARG ARG A . n 
A 1 242 ARG 242 243 243 ARG ARG A . n 
A 1 243 ARG 243 244 244 ARG ARG A . n 
A 1 244 ALA 244 245 245 ALA ALA A . n 
A 1 245 VAL 245 246 246 VAL VAL A . n 
A 1 246 GLU 246 247 247 GLU GLU A . n 
A 1 247 LEU 247 248 248 LEU LEU A . n 
A 1 248 GLY 248 249 249 GLY GLY A . n 
A 1 249 ARG 249 250 250 ARG ARG A . n 
A 1 250 ASN 250 251 251 ASN ASN A . n 
A 1 251 LEU 251 252 252 LEU LEU A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 CYS 253 254 254 CYS CYS A . n 
A 1 254 ASN 254 255 255 ASN ASN A . n 
A 1 255 LEU 255 256 256 LEU LEU A . n 
A 1 256 ASN 256 257 257 ASN ASN A . n 
A 1 257 SER 257 258 258 SER SER A . n 
A 1 258 ASP 258 259 259 ASP ASP A . n 
A 1 259 GLU 259 260 260 GLU GLU A . n 
A 1 260 GLU 260 261 261 GLU GLU A . n 
A 1 261 LEU 261 262 262 LEU LEU A . n 
A 1 262 ILE 262 263 263 ILE ILE A . n 
A 1 263 HIS 263 264 264 HIS HIS A . n 
A 1 264 CYS 264 265 265 CYS CYS A . n 
A 1 265 LEU 265 266 266 LEU LEU A . n 
A 1 266 ARG 266 267 267 ARG ARG A . n 
A 1 267 GLU 267 268 268 GLU GLU A . n 
A 1 268 LYS 268 269 269 LYS LYS A . n 
A 1 269 LYS 269 270 270 LYS LYS A . n 
A 1 270 PRO 270 271 271 PRO PRO A . n 
A 1 271 GLN 271 272 272 GLN GLN A . n 
A 1 272 GLU 272 273 273 GLU GLU A . n 
A 1 273 LEU 273 274 274 LEU LEU A . n 
A 1 274 ILE 274 275 275 ILE ILE A . n 
A 1 275 ASP 275 276 276 ASP ASP A . n 
A 1 276 VAL 276 277 277 VAL VAL A . n 
A 1 277 GLU 277 278 278 GLU GLU A . n 
A 1 278 TRP 278 279 279 TRP TRP A . n 
A 1 279 ASN 279 280 280 ASN ASN A . n 
A 1 280 VAL 280 281 281 VAL VAL A . n 
A 1 281 LEU 281 282 282 LEU LEU A . n 
A 1 282 PRO 282 283 283 PRO PRO A . n 
A 1 283 PHE 283 284 284 PHE PHE A . n 
A 1 284 ASP 284 285 285 ASP ASP A . n 
A 1 285 SER 285 286 286 SER SER A . n 
A 1 286 ILE 286 287 287 ILE ILE A . n 
A 1 287 PHE 287 288 288 PHE PHE A . n 
A 1 288 ARG 288 289 289 ARG ARG A . n 
A 1 289 PHE 289 290 290 PHE PHE A . n 
A 1 290 SER 290 291 291 SER SER A . n 
A 1 291 PHE 291 292 292 PHE PHE A . n 
A 1 292 VAL 292 293 293 VAL VAL A . n 
A 1 293 PRO 293 294 294 PRO PRO A . n 
A 1 294 VAL 294 295 295 VAL VAL A . n 
A 1 295 ILE 295 296 296 ILE ILE A . n 
A 1 296 ASP 296 297 297 ASP ASP A . n 
A 1 297 GLY 297 298 298 GLY GLY A . n 
A 1 298 GLU 298 299 299 GLU GLU A . n 
A 1 299 PHE 299 300 300 PHE PHE A . n 
A 1 300 PHE 300 301 301 PHE PHE A . n 
A 1 301 PRO 301 302 302 PRO PRO A . n 
A 1 302 THR 302 303 303 THR THR A . n 
A 1 303 SER 303 304 304 SER SER A . n 
A 1 304 LEU 304 305 305 LEU LEU A . n 
A 1 305 GLU 305 306 306 GLU GLU A . n 
A 1 306 SER 306 307 307 SER SER A . n 
A 1 307 MET 307 308 308 MET MET A . n 
A 1 308 LEU 308 309 309 LEU LEU A . n 
A 1 309 ASN 309 310 310 ASN ASN A . n 
A 1 310 SER 310 311 311 SER SER A . n 
A 1 311 GLY 311 312 312 GLY GLY A . n 
A 1 312 ASN 312 313 313 ASN ASN A . n 
A 1 313 PHE 313 314 314 PHE PHE A . n 
A 1 314 LYS 314 315 315 LYS LYS A . n 
A 1 315 LYS 315 316 316 LYS LYS A . n 
A 1 316 THR 316 317 317 THR THR A . n 
A 1 317 GLN 317 318 318 GLN GLN A . n 
A 1 318 ILE 318 319 319 ILE ILE A . n 
A 1 319 LEU 319 320 320 LEU LEU A . n 
A 1 320 LEU 320 321 321 LEU LEU A . n 
A 1 321 GLY 321 322 322 GLY GLY A . n 
A 1 322 VAL 322 323 323 VAL VAL A . n 
A 1 323 ASN 323 324 324 ASN ASN A . n 
A 1 324 LYS 324 325 325 LYS LYS A . n 
A 1 325 ASP 325 326 326 ASP ASP A . n 
A 1 326 GLU 326 327 327 GLU GLU A . n 
A 1 327 GLY 327 328 328 GLY GLY A . n 
A 1 328 SER 328 329 329 SER SER A . n 
A 1 329 PHE 329 330 330 PHE PHE A . n 
A 1 330 PHE 330 331 331 PHE PHE A . n 
A 1 331 LEU 331 332 332 LEU LEU A . n 
A 1 332 LEU 332 333 333 LEU LEU A . n 
A 1 333 TYR 333 334 334 TYR TYR A . n 
A 1 334 GLY 334 335 335 GLY GLY A . n 
A 1 335 ALA 335 336 336 ALA ALA A . n 
A 1 336 PRO 336 337 337 PRO PRO A . n 
A 1 337 GLY 337 338 338 GLY GLY A . n 
A 1 338 PHE 338 339 339 PHE PHE A . n 
A 1 339 SER 339 340 340 SER SER A . n 
A 1 340 LYS 340 341 341 LYS LYS A . n 
A 1 341 ASP 341 342 342 ASP ASP A . n 
A 1 342 SER 342 343 343 SER SER A . n 
A 1 343 GLU 343 344 344 GLU GLU A . n 
A 1 344 SER 344 345 345 SER SER A . n 
A 1 345 LYS 345 346 346 LYS LYS A . n 
A 1 346 ILE 346 347 347 ILE ILE A . n 
A 1 347 SER 347 348 348 SER SER A . n 
A 1 348 ARG 348 349 349 ARG ARG A . n 
A 1 349 GLU 349 350 350 GLU GLU A . n 
A 1 350 ASP 350 351 351 ASP ASP A . n 
A 1 351 PHE 351 352 352 PHE PHE A . n 
A 1 352 MET 352 353 353 MET MET A . n 
A 1 353 SER 353 354 354 SER SER A . n 
A 1 354 GLY 354 355 355 GLY GLY A . n 
A 1 355 VAL 355 356 356 VAL VAL A . n 
A 1 356 LYS 356 357 357 LYS LYS A . n 
A 1 357 LEU 357 358 358 LEU LEU A . n 
A 1 358 SER 358 359 359 SER SER A . n 
A 1 359 VAL 359 360 360 VAL VAL A . n 
A 1 360 PRO 360 361 361 PRO PRO A . n 
A 1 361 HIS 361 362 362 HIS HIS A . n 
A 1 362 ALA 362 363 363 ALA ALA A . n 
A 1 363 ASN 363 364 364 ASN ASN A . n 
A 1 364 ASP 364 365 365 ASP ASP A . n 
A 1 365 LEU 365 366 366 LEU LEU A . n 
A 1 366 GLY 366 367 367 GLY GLY A . n 
A 1 367 LEU 367 368 368 LEU LEU A . n 
A 1 368 ASP 368 369 369 ASP ASP A . n 
A 1 369 ALA 369 370 370 ALA ALA A . n 
A 1 370 VAL 370 371 371 VAL VAL A . n 
A 1 371 THR 371 372 372 THR THR A . n 
A 1 372 LEU 372 373 373 LEU LEU A . n 
A 1 373 GLN 373 374 374 GLN GLN A . n 
A 1 374 TYR 374 375 375 TYR TYR A . n 
A 1 375 THR 375 376 376 THR THR A . n 
A 1 376 ASP 376 377 377 ASP ASP A . n 
A 1 377 TRP 377 378 378 TRP TRP A . n 
A 1 378 MET 378 379 379 MET MET A . n 
A 1 379 ASP 379 380 380 ASP ASP A . n 
A 1 380 ASP 380 381 381 ASP ASP A . n 
A 1 381 ASN 381 382 382 ASN ASN A . n 
A 1 382 ASN 382 383 383 ASN ASN A . n 
A 1 383 GLY 383 384 384 GLY GLY A . n 
A 1 384 ILE 384 385 385 ILE ILE A . n 
A 1 385 LYS 385 386 386 LYS LYS A . n 
A 1 386 ASN 386 387 387 ASN ASN A . n 
A 1 387 ARG 387 388 388 ARG ARG A . n 
A 1 388 ASP 388 389 389 ASP ASP A . n 
A 1 389 GLY 389 390 390 GLY GLY A . n 
A 1 390 LEU 390 391 391 LEU LEU A . n 
A 1 391 ASP 391 392 392 ASP ASP A . n 
A 1 392 ASP 392 393 393 ASP ASP A . n 
A 1 393 ILE 393 394 394 ILE ILE A . n 
A 1 394 VAL 394 395 395 VAL VAL A . n 
A 1 395 GLY 395 396 396 GLY GLY A . n 
A 1 396 ASP 396 397 397 ASP ASP A . n 
A 1 397 HIS 397 398 398 HIS HIS A . n 
A 1 398 ASN 398 399 399 ASN ASN A . n 
A 1 399 VAL 399 400 400 VAL VAL A . n 
A 1 400 ILE 400 401 401 ILE ILE A . n 
A 1 401 CYS 401 402 402 CYS CYS A . n 
A 1 402 PRO 402 403 403 PRO PRO A . n 
A 1 403 LEU 403 404 404 LEU LEU A . n 
A 1 404 MET 404 405 405 MET MET A . n 
A 1 405 HIS 405 406 406 HIS HIS A . n 
A 1 406 PHE 406 407 407 PHE PHE A . n 
A 1 407 VAL 407 408 408 VAL VAL A . n 
A 1 408 ASN 408 409 409 ASN ASN A . n 
A 1 409 LYS 409 410 410 LYS LYS A . n 
A 1 410 TYR 410 411 411 TYR TYR A . n 
A 1 411 THR 411 412 412 THR THR A . n 
A 1 412 LYS 412 413 413 LYS LYS A . n 
A 1 413 PHE 413 414 414 PHE PHE A . n 
A 1 414 GLY 414 415 415 GLY GLY A . n 
A 1 415 ASN 415 416 416 ASN ASN A . n 
A 1 416 GLY 416 417 417 GLY GLY A . n 
A 1 417 THR 417 418 418 THR THR A . n 
A 1 418 TYR 418 419 419 TYR TYR A . n 
A 1 419 LEU 419 420 420 LEU LEU A . n 
A 1 420 TYR 420 421 421 TYR TYR A . n 
A 1 421 PHE 421 422 422 PHE PHE A . n 
A 1 422 PHE 422 423 423 PHE PHE A . n 
A 1 423 ASN 423 424 424 ASN ASN A . n 
A 1 424 HIS 424 425 425 HIS HIS A . n 
A 1 425 ARG 425 426 426 ARG ARG A . n 
A 1 426 ALA 426 427 427 ALA ALA A . n 
A 1 427 SER 427 428 428 SER SER A . n 
A 1 428 ASN 428 429 429 ASN ASN A . n 
A 1 429 LEU 429 430 430 LEU LEU A . n 
A 1 430 VAL 430 431 431 VAL VAL A . n 
A 1 431 TRP 431 432 432 TRP TRP A . n 
A 1 432 PRO 432 433 433 PRO PRO A . n 
A 1 433 GLU 433 434 434 GLU GLU A . n 
A 1 434 TRP 434 435 435 TRP TRP A . n 
A 1 435 MET 435 436 436 MET MET A . n 
A 1 436 GLY 436 437 437 GLY GLY A . n 
A 1 437 VAL 437 438 438 VAL VAL A . n 
A 1 438 ILE 438 439 439 ILE ILE A . n 
A 1 439 HIS 439 440 440 HIS HIS A . n 
A 1 440 GLY 440 441 441 GLY GLY A . n 
A 1 441 TYR 441 442 442 TYR TYR A . n 
A 1 442 GLU 442 443 443 GLU GLU A . n 
A 1 443 ILE 443 444 444 ILE ILE A . n 
A 1 444 GLU 444 445 445 GLU GLU A . n 
A 1 445 PHE 445 446 446 PHE PHE A . n 
A 1 446 VAL 446 447 447 VAL VAL A . n 
A 1 447 PHE 447 448 448 PHE PHE A . n 
A 1 448 GLY 448 449 449 GLY GLY A . n 
A 1 449 LEU 449 450 450 LEU LEU A . n 
A 1 450 PRO 450 451 451 PRO PRO A . n 
A 1 451 LEU 451 452 452 LEU LEU A . n 
A 1 452 VAL 452 453 453 VAL VAL A . n 
A 1 453 LYS 453 454 454 LYS LYS A . n 
A 1 454 GLU 454 455 455 GLU GLU A . n 
A 1 455 LEU 455 456 456 LEU LEU A . n 
A 1 456 ASN 456 457 457 ASN ASN A . n 
A 1 457 TYR 457 458 458 TYR TYR A . n 
A 1 458 THR 458 459 459 THR THR A . n 
A 1 459 ALA 459 460 460 ALA ALA A . n 
A 1 460 GLU 460 461 461 GLU GLU A . n 
A 1 461 GLU 461 462 462 GLU GLU A . n 
A 1 462 GLU 462 463 463 GLU GLU A . n 
A 1 463 ALA 463 464 464 ALA ALA A . n 
A 1 464 LEU 464 465 465 LEU LEU A . n 
A 1 465 SER 465 466 466 SER SER A . n 
A 1 466 ARG 466 467 467 ARG ARG A . n 
A 1 467 ARG 467 468 468 ARG ARG A . n 
A 1 468 ILE 468 469 469 ILE ILE A . n 
A 1 469 MET 469 470 470 MET MET A . n 
A 1 470 HIS 470 471 471 HIS HIS A . n 
A 1 471 TYR 471 472 472 TYR TYR A . n 
A 1 472 TRP 472 473 473 TRP TRP A . n 
A 1 473 ALA 473 474 474 ALA ALA A . n 
A 1 474 THR 474 475 475 THR THR A . n 
A 1 475 PHE 475 476 476 PHE PHE A . n 
A 1 476 ALA 476 477 477 ALA ALA A . n 
A 1 477 LYS 477 478 478 LYS LYS A . n 
A 1 478 THR 478 479 479 THR THR A . n 
A 1 479 GLY 479 480 480 GLY GLY A . n 
A 1 480 ASN 480 481 481 ASN ASN A . n 
A 1 481 PRO 481 482 482 PRO PRO A . n 
A 1 482 ASN 482 483 483 ASN ASN A . n 
A 1 483 GLU 483 484 484 GLU GLU A . n 
A 1 484 PRO 484 485 485 PRO PRO A . n 
A 1 485 HIS 485 486 486 HIS HIS A . n 
A 1 486 SER 486 487 487 SER SER A . n 
A 1 487 GLN 487 488 488 GLN GLN A . n 
A 1 488 GLU 488 489 489 GLU GLU A . n 
A 1 489 SER 489 490 490 SER SER A . n 
A 1 490 LYS 490 491 491 LYS LYS A . n 
A 1 491 TRP 491 492 492 TRP TRP A . n 
A 1 492 PRO 492 493 493 PRO PRO A . n 
A 1 493 LEU 493 494 494 LEU LEU A . n 
A 1 494 PHE 494 495 495 PHE PHE A . n 
A 1 495 THR 495 496 496 THR THR A . n 
A 1 496 THR 496 497 497 THR THR A . n 
A 1 497 LYS 497 498 498 LYS LYS A . n 
A 1 498 GLU 498 499 499 GLU GLU A . n 
A 1 499 GLN 499 500 500 GLN GLN A . n 
A 1 500 LYS 500 501 501 LYS LYS A . n 
A 1 501 PHE 501 502 502 PHE PHE A . n 
A 1 502 ILE 502 503 503 ILE ILE A . n 
A 1 503 ASP 503 504 504 ASP ASP A . n 
A 1 504 LEU 504 505 505 LEU LEU A . n 
A 1 505 ASN 505 506 506 ASN ASN A . n 
A 1 506 THR 506 507 507 THR THR A . n 
A 1 507 GLU 507 508 508 GLU GLU A . n 
A 1 508 PRO 508 509 509 PRO PRO A . n 
A 1 509 MET 509 510 510 MET MET A . n 
A 1 510 LYS 510 511 511 LYS LYS A . n 
A 1 511 VAL 511 512 512 VAL VAL A . n 
A 1 512 HIS 512 513 513 HIS HIS A . n 
A 1 513 GLN 513 514 514 GLN GLN A . n 
A 1 514 ARG 514 515 515 ARG ARG A . n 
A 1 515 LEU 515 516 516 LEU LEU A . n 
A 1 516 ARG 516 517 517 ARG ARG A . n 
A 1 517 VAL 517 518 518 VAL VAL A . n 
A 1 518 GLN 518 519 519 GLN GLN A . n 
A 1 519 MET 519 520 520 MET MET A . n 
A 1 520 CYS 520 521 521 CYS CYS A . n 
A 1 521 VAL 521 522 522 VAL VAL A . n 
A 1 522 PHE 522 523 523 PHE PHE A . n 
A 1 523 TRP 523 524 524 TRP TRP A . n 
A 1 524 ASN 524 525 525 ASN ASN A . n 
A 1 525 GLN 525 526 526 GLN GLN A . n 
A 1 526 PHE 526 527 527 PHE PHE A . n 
A 1 527 LEU 527 528 528 LEU LEU A . n 
A 1 528 PRO 528 529 529 PRO PRO A . n 
A 1 529 LYS 529 530 530 LYS LYS A . n 
A 1 530 LEU 530 531 531 LEU LEU A . n 
A 1 531 LEU 531 532 532 LEU LEU A . n 
A 1 532 ASN 532 533 533 ASN ASN A . n 
A 1 533 ALA 533 534 534 ALA ALA A . n 
A 1 534 THR 534 535 535 THR THR A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NAG 1   601  601  NAG NAG A . 
C 2 NAG 1   602  602  NAG NAG A . 
D 2 NAG 2   603  603  NAG NAG A . 
E 3 OMI 1   604  604  OMI OMI A . 
F 4 PG4 1   605  605  PG4 PG4 A . 
G 5 ACT 1   606  606  ACT ACT A . 
H 6 HOH 1   701  701  HOH HOH A . 
H 6 HOH 2   702  702  HOH HOH A . 
H 6 HOH 3   703  703  HOH HOH A . 
H 6 HOH 4   704  704  HOH HOH A . 
H 6 HOH 5   705  705  HOH HOH A . 
H 6 HOH 6   706  706  HOH HOH A . 
H 6 HOH 7   707  707  HOH HOH A . 
H 6 HOH 8   708  708  HOH HOH A . 
H 6 HOH 9   709  709  HOH HOH A . 
H 6 HOH 10  710  710  HOH HOH A . 
H 6 HOH 11  711  711  HOH HOH A . 
H 6 HOH 12  712  712  HOH HOH A . 
H 6 HOH 13  713  713  HOH HOH A . 
H 6 HOH 14  714  714  HOH HOH A . 
H 6 HOH 15  715  715  HOH HOH A . 
H 6 HOH 16  716  716  HOH HOH A . 
H 6 HOH 17  717  717  HOH HOH A . 
H 6 HOH 18  718  718  HOH HOH A . 
H 6 HOH 19  719  719  HOH HOH A . 
H 6 HOH 20  720  720  HOH HOH A . 
H 6 HOH 21  721  721  HOH HOH A . 
H 6 HOH 22  722  722  HOH HOH A . 
H 6 HOH 23  723  723  HOH HOH A . 
H 6 HOH 24  724  724  HOH HOH A . 
H 6 HOH 25  725  725  HOH HOH A . 
H 6 HOH 26  726  726  HOH HOH A . 
H 6 HOH 27  727  727  HOH HOH A . 
H 6 HOH 28  728  728  HOH HOH A . 
H 6 HOH 29  729  729  HOH HOH A . 
H 6 HOH 30  730  730  HOH HOH A . 
H 6 HOH 31  731  731  HOH HOH A . 
H 6 HOH 32  732  732  HOH HOH A . 
H 6 HOH 33  733  733  HOH HOH A . 
H 6 HOH 34  734  734  HOH HOH A . 
H 6 HOH 35  735  735  HOH HOH A . 
H 6 HOH 36  736  736  HOH HOH A . 
H 6 HOH 37  737  737  HOH HOH A . 
H 6 HOH 38  738  738  HOH HOH A . 
H 6 HOH 39  739  739  HOH HOH A . 
H 6 HOH 40  740  740  HOH HOH A . 
H 6 HOH 41  741  741  HOH HOH A . 
H 6 HOH 42  742  742  HOH HOH A . 
H 6 HOH 43  743  743  HOH HOH A . 
H 6 HOH 44  744  744  HOH HOH A . 
H 6 HOH 45  745  745  HOH HOH A . 
H 6 HOH 46  746  746  HOH HOH A . 
H 6 HOH 47  747  747  HOH HOH A . 
H 6 HOH 48  748  748  HOH HOH A . 
H 6 HOH 49  749  749  HOH HOH A . 
H 6 HOH 50  750  750  HOH HOH A . 
H 6 HOH 51  751  751  HOH HOH A . 
H 6 HOH 52  752  752  HOH HOH A . 
H 6 HOH 53  753  753  HOH HOH A . 
H 6 HOH 54  754  754  HOH HOH A . 
H 6 HOH 55  755  755  HOH HOH A . 
H 6 HOH 56  756  756  HOH HOH A . 
H 6 HOH 57  757  757  HOH HOH A . 
H 6 HOH 58  758  758  HOH HOH A . 
H 6 HOH 59  759  759  HOH HOH A . 
H 6 HOH 60  760  760  HOH HOH A . 
H 6 HOH 61  761  761  HOH HOH A . 
H 6 HOH 62  762  762  HOH HOH A . 
H 6 HOH 63  763  763  HOH HOH A . 
H 6 HOH 64  764  764  HOH HOH A . 
H 6 HOH 65  765  765  HOH HOH A . 
H 6 HOH 66  766  766  HOH HOH A . 
H 6 HOH 67  767  767  HOH HOH A . 
H 6 HOH 68  768  768  HOH HOH A . 
H 6 HOH 69  769  769  HOH HOH A . 
H 6 HOH 70  770  770  HOH HOH A . 
H 6 HOH 71  771  771  HOH HOH A . 
H 6 HOH 72  772  772  HOH HOH A . 
H 6 HOH 73  773  773  HOH HOH A . 
H 6 HOH 74  774  774  HOH HOH A . 
H 6 HOH 75  775  775  HOH HOH A . 
H 6 HOH 76  776  776  HOH HOH A . 
H 6 HOH 77  777  777  HOH HOH A . 
H 6 HOH 78  778  778  HOH HOH A . 
H 6 HOH 79  779  779  HOH HOH A . 
H 6 HOH 80  780  780  HOH HOH A . 
H 6 HOH 81  781  781  HOH HOH A . 
H 6 HOH 82  782  782  HOH HOH A . 
H 6 HOH 83  783  783  HOH HOH A . 
H 6 HOH 84  784  784  HOH HOH A . 
H 6 HOH 85  785  785  HOH HOH A . 
H 6 HOH 86  786  786  HOH HOH A . 
H 6 HOH 87  787  787  HOH HOH A . 
H 6 HOH 88  788  788  HOH HOH A . 
H 6 HOH 89  789  789  HOH HOH A . 
H 6 HOH 90  790  790  HOH HOH A . 
H 6 HOH 91  791  791  HOH HOH A . 
H 6 HOH 92  792  792  HOH HOH A . 
H 6 HOH 93  793  793  HOH HOH A . 
H 6 HOH 94  794  794  HOH HOH A . 
H 6 HOH 95  795  795  HOH HOH A . 
H 6 HOH 96  796  796  HOH HOH A . 
H 6 HOH 97  797  797  HOH HOH A . 
H 6 HOH 98  798  798  HOH HOH A . 
H 6 HOH 99  799  799  HOH HOH A . 
H 6 HOH 100 800  800  HOH HOH A . 
H 6 HOH 101 801  801  HOH HOH A . 
H 6 HOH 102 802  802  HOH HOH A . 
H 6 HOH 103 803  803  HOH HOH A . 
H 6 HOH 104 804  804  HOH HOH A . 
H 6 HOH 105 805  805  HOH HOH A . 
H 6 HOH 106 806  806  HOH HOH A . 
H 6 HOH 107 807  807  HOH HOH A . 
H 6 HOH 108 808  808  HOH HOH A . 
H 6 HOH 109 809  809  HOH HOH A . 
H 6 HOH 110 810  810  HOH HOH A . 
H 6 HOH 111 811  811  HOH HOH A . 
H 6 HOH 112 812  812  HOH HOH A . 
H 6 HOH 113 813  813  HOH HOH A . 
H 6 HOH 114 814  814  HOH HOH A . 
H 6 HOH 115 815  815  HOH HOH A . 
H 6 HOH 116 816  816  HOH HOH A . 
H 6 HOH 117 817  817  HOH HOH A . 
H 6 HOH 118 818  818  HOH HOH A . 
H 6 HOH 119 819  819  HOH HOH A . 
H 6 HOH 120 820  820  HOH HOH A . 
H 6 HOH 121 821  821  HOH HOH A . 
H 6 HOH 122 822  822  HOH HOH A . 
H 6 HOH 123 823  823  HOH HOH A . 
H 6 HOH 124 824  824  HOH HOH A . 
H 6 HOH 125 825  825  HOH HOH A . 
H 6 HOH 126 826  826  HOH HOH A . 
H 6 HOH 127 827  827  HOH HOH A . 
H 6 HOH 128 828  828  HOH HOH A . 
H 6 HOH 129 829  829  HOH HOH A . 
H 6 HOH 130 830  830  HOH HOH A . 
H 6 HOH 131 831  831  HOH HOH A . 
H 6 HOH 132 832  832  HOH HOH A . 
H 6 HOH 133 833  833  HOH HOH A . 
H 6 HOH 134 834  834  HOH HOH A . 
H 6 HOH 135 835  835  HOH HOH A . 
H 6 HOH 136 836  836  HOH HOH A . 
H 6 HOH 137 837  837  HOH HOH A . 
H 6 HOH 138 838  838  HOH HOH A . 
H 6 HOH 139 839  839  HOH HOH A . 
H 6 HOH 140 840  840  HOH HOH A . 
H 6 HOH 141 841  841  HOH HOH A . 
H 6 HOH 142 842  842  HOH HOH A . 
H 6 HOH 143 843  843  HOH HOH A . 
H 6 HOH 144 844  844  HOH HOH A . 
H 6 HOH 145 845  845  HOH HOH A . 
H 6 HOH 146 846  846  HOH HOH A . 
H 6 HOH 147 847  847  HOH HOH A . 
H 6 HOH 148 848  848  HOH HOH A . 
H 6 HOH 149 849  849  HOH HOH A . 
H 6 HOH 150 850  850  HOH HOH A . 
H 6 HOH 151 851  851  HOH HOH A . 
H 6 HOH 152 852  852  HOH HOH A . 
H 6 HOH 153 853  853  HOH HOH A . 
H 6 HOH 154 854  854  HOH HOH A . 
H 6 HOH 155 855  855  HOH HOH A . 
H 6 HOH 156 856  856  HOH HOH A . 
H 6 HOH 157 857  857  HOH HOH A . 
H 6 HOH 158 858  858  HOH HOH A . 
H 6 HOH 159 859  859  HOH HOH A . 
H 6 HOH 160 860  860  HOH HOH A . 
H 6 HOH 161 861  861  HOH HOH A . 
H 6 HOH 162 862  862  HOH HOH A . 
H 6 HOH 163 863  863  HOH HOH A . 
H 6 HOH 164 864  864  HOH HOH A . 
H 6 HOH 165 865  865  HOH HOH A . 
H 6 HOH 166 866  866  HOH HOH A . 
H 6 HOH 167 867  867  HOH HOH A . 
H 6 HOH 168 868  868  HOH HOH A . 
H 6 HOH 169 869  869  HOH HOH A . 
H 6 HOH 170 870  870  HOH HOH A . 
H 6 HOH 171 871  871  HOH HOH A . 
H 6 HOH 172 872  872  HOH HOH A . 
H 6 HOH 173 873  873  HOH HOH A . 
H 6 HOH 174 874  874  HOH HOH A . 
H 6 HOH 175 875  875  HOH HOH A . 
H 6 HOH 176 876  876  HOH HOH A . 
H 6 HOH 177 877  877  HOH HOH A . 
H 6 HOH 178 878  878  HOH HOH A . 
H 6 HOH 179 879  879  HOH HOH A . 
H 6 HOH 180 880  880  HOH HOH A . 
H 6 HOH 181 881  881  HOH HOH A . 
H 6 HOH 182 882  882  HOH HOH A . 
H 6 HOH 183 883  883  HOH HOH A . 
H 6 HOH 184 884  884  HOH HOH A . 
H 6 HOH 185 885  885  HOH HOH A . 
H 6 HOH 186 886  886  HOH HOH A . 
H 6 HOH 187 887  887  HOH HOH A . 
H 6 HOH 188 888  888  HOH HOH A . 
H 6 HOH 189 889  889  HOH HOH A . 
H 6 HOH 190 890  890  HOH HOH A . 
H 6 HOH 191 891  891  HOH HOH A . 
H 6 HOH 192 892  892  HOH HOH A . 
H 6 HOH 193 893  893  HOH HOH A . 
H 6 HOH 194 894  894  HOH HOH A . 
H 6 HOH 195 895  895  HOH HOH A . 
H 6 HOH 196 896  896  HOH HOH A . 
H 6 HOH 197 897  897  HOH HOH A . 
H 6 HOH 198 898  898  HOH HOH A . 
H 6 HOH 199 899  899  HOH HOH A . 
H 6 HOH 200 900  900  HOH HOH A . 
H 6 HOH 201 901  901  HOH HOH A . 
H 6 HOH 202 902  902  HOH HOH A . 
H 6 HOH 203 903  903  HOH HOH A . 
H 6 HOH 204 904  904  HOH HOH A . 
H 6 HOH 205 905  905  HOH HOH A . 
H 6 HOH 206 906  906  HOH HOH A . 
H 6 HOH 207 907  907  HOH HOH A . 
H 6 HOH 208 908  908  HOH HOH A . 
H 6 HOH 209 909  909  HOH HOH A . 
H 6 HOH 210 910  910  HOH HOH A . 
H 6 HOH 211 911  911  HOH HOH A . 
H 6 HOH 212 912  912  HOH HOH A . 
H 6 HOH 213 913  913  HOH HOH A . 
H 6 HOH 214 914  914  HOH HOH A . 
H 6 HOH 215 915  915  HOH HOH A . 
H 6 HOH 216 916  916  HOH HOH A . 
H 6 HOH 217 917  917  HOH HOH A . 
H 6 HOH 218 918  918  HOH HOH A . 
H 6 HOH 219 919  919  HOH HOH A . 
H 6 HOH 220 920  920  HOH HOH A . 
H 6 HOH 221 921  921  HOH HOH A . 
H 6 HOH 222 922  922  HOH HOH A . 
H 6 HOH 223 923  923  HOH HOH A . 
H 6 HOH 224 924  924  HOH HOH A . 
H 6 HOH 225 925  925  HOH HOH A . 
H 6 HOH 226 926  926  HOH HOH A . 
H 6 HOH 227 927  927  HOH HOH A . 
H 6 HOH 228 928  928  HOH HOH A . 
H 6 HOH 229 929  929  HOH HOH A . 
H 6 HOH 230 930  930  HOH HOH A . 
H 6 HOH 231 931  931  HOH HOH A . 
H 6 HOH 232 932  932  HOH HOH A . 
H 6 HOH 233 933  933  HOH HOH A . 
H 6 HOH 234 934  934  HOH HOH A . 
H 6 HOH 235 935  935  HOH HOH A . 
H 6 HOH 236 936  936  HOH HOH A . 
H 6 HOH 237 937  937  HOH HOH A . 
H 6 HOH 238 938  938  HOH HOH A . 
H 6 HOH 239 939  939  HOH HOH A . 
H 6 HOH 240 940  940  HOH HOH A . 
H 6 HOH 241 941  941  HOH HOH A . 
H 6 HOH 242 942  942  HOH HOH A . 
H 6 HOH 243 943  943  HOH HOH A . 
H 6 HOH 244 944  944  HOH HOH A . 
H 6 HOH 245 945  945  HOH HOH A . 
H 6 HOH 246 946  946  HOH HOH A . 
H 6 HOH 247 947  947  HOH HOH A . 
H 6 HOH 248 948  948  HOH HOH A . 
H 6 HOH 249 949  949  HOH HOH A . 
H 6 HOH 250 950  950  HOH HOH A . 
H 6 HOH 251 951  951  HOH HOH A . 
H 6 HOH 252 952  952  HOH HOH A . 
H 6 HOH 253 953  953  HOH HOH A . 
H 6 HOH 254 954  954  HOH HOH A . 
H 6 HOH 255 955  955  HOH HOH A . 
H 6 HOH 256 956  956  HOH HOH A . 
H 6 HOH 257 957  957  HOH HOH A . 
H 6 HOH 258 958  958  HOH HOH A . 
H 6 HOH 259 959  959  HOH HOH A . 
H 6 HOH 260 960  960  HOH HOH A . 
H 6 HOH 261 961  961  HOH HOH A . 
H 6 HOH 262 962  962  HOH HOH A . 
H 6 HOH 263 963  963  HOH HOH A . 
H 6 HOH 264 964  964  HOH HOH A . 
H 6 HOH 265 965  965  HOH HOH A . 
H 6 HOH 266 966  966  HOH HOH A . 
H 6 HOH 267 967  967  HOH HOH A . 
H 6 HOH 268 968  968  HOH HOH A . 
H 6 HOH 269 969  969  HOH HOH A . 
H 6 HOH 270 970  970  HOH HOH A . 
H 6 HOH 271 971  971  HOH HOH A . 
H 6 HOH 272 972  972  HOH HOH A . 
H 6 HOH 273 973  973  HOH HOH A . 
H 6 HOH 274 974  974  HOH HOH A . 
H 6 HOH 275 975  975  HOH HOH A . 
H 6 HOH 276 976  976  HOH HOH A . 
H 6 HOH 277 977  977  HOH HOH A . 
H 6 HOH 278 978  978  HOH HOH A . 
H 6 HOH 279 979  979  HOH HOH A . 
H 6 HOH 280 980  980  HOH HOH A . 
H 6 HOH 281 981  981  HOH HOH A . 
H 6 HOH 282 982  982  HOH HOH A . 
H 6 HOH 283 983  983  HOH HOH A . 
H 6 HOH 284 984  984  HOH HOH A . 
H 6 HOH 285 985  985  HOH HOH A . 
H 6 HOH 286 986  986  HOH HOH A . 
H 6 HOH 287 987  987  HOH HOH A . 
H 6 HOH 288 988  988  HOH HOH A . 
H 6 HOH 289 989  989  HOH HOH A . 
H 6 HOH 290 990  990  HOH HOH A . 
H 6 HOH 291 991  991  HOH HOH A . 
H 6 HOH 292 992  992  HOH HOH A . 
H 6 HOH 293 993  993  HOH HOH A . 
H 6 HOH 294 994  994  HOH HOH A . 
H 6 HOH 295 995  995  HOH HOH A . 
H 6 HOH 296 996  996  HOH HOH A . 
H 6 HOH 297 997  997  HOH HOH A . 
H 6 HOH 298 998  998  HOH HOH A . 
H 6 HOH 299 999  999  HOH HOH A . 
H 6 HOH 300 1000 1000 HOH HOH A . 
H 6 HOH 301 1001 1001 HOH HOH A . 
H 6 HOH 302 1002 1002 HOH HOH A . 
H 6 HOH 303 1003 1003 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3540  ? 
1 MORE         -3    ? 
1 'SSA (A^2)'  41060 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z          1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  
1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 6_554 -x,-x+y,-z-2/3 -0.5000000000 -0.8660254038 0.0000000000 0.0000000000 -0.8660254038 
0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -91.3666666667 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     957 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   H 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2017-04-05 
# 
_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_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.7.0032 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 968 ? ? O A HOH 979  ? ? 2.08 
2 1 O A HOH 976 ? ? O A HOH 991  ? ? 2.15 
3 1 O A HOH 882 ? ? O A HOH 1002 ? ? 2.18 
4 1 O A HOH 958 ? ? O A HOH 978  ? ? 2.18 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             3 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             3 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.206 
_pdbx_validate_rmsd_bond.bond_target_value         1.492 
_pdbx_validate_rmsd_bond.bond_deviation            -0.286 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.016 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CA  A ASP 2   ? ? CB A ASP 2   ? ? CG  A ASP 2   ? ? 156.06 113.40 42.66  2.20 N 
2  1 CB  A ASP 2   ? ? CG A ASP 2   ? ? OD1 A ASP 2   ? ? 98.38  118.30 -19.92 0.90 N 
3  1 CB  A ASP 2   ? ? CG A ASP 2   ? ? OD2 A ASP 2   ? ? 131.23 118.30 12.93  0.90 N 
4  1 CA  A HIS 3   ? ? CB A HIS 3   ? ? CG  A HIS 3   ? ? 124.89 113.60 11.29  1.70 N 
5  1 CB  A HIS 3   ? ? CG A HIS 3   ? ? CD2 A HIS 3   ? ? 139.37 131.40 7.97   1.20 N 
6  1 CB  A ASP 93  ? ? CG A ASP 93  ? ? OD1 A ASP 93  ? ? 124.85 118.30 6.55   0.90 N 
7  1 CB  A ASP 93  ? ? CG A ASP 93  ? ? OD2 A ASP 93  ? ? 112.30 118.30 -6.00  0.90 N 
8  1 NE  A ARG 174 ? ? CZ A ARG 174 ? ? NH1 A ARG 174 ? ? 123.63 120.30 3.33   0.50 N 
9  1 NE  A ARG 221 ? ? CZ A ARG 221 ? ? NH1 A ARG 221 ? ? 123.40 120.30 3.10   0.50 N 
10 1 NE  A ARG 221 ? ? CZ A ARG 221 ? ? NH2 A ARG 221 ? ? 115.86 120.30 -4.44  0.50 N 
11 1 NE  A ARG 243 ? ? CZ A ARG 243 ? ? NH1 A ARG 243 ? ? 124.03 120.30 3.73   0.50 N 
12 1 NE  A ARG 243 ? ? CZ A ARG 243 ? ? NH2 A ARG 243 ? ? 115.94 120.30 -4.36  0.50 N 
13 1 NE  A ARG 388 ? ? CZ A ARG 388 ? ? NH1 A ARG 388 ? ? 124.20 120.30 3.90   0.50 N 
14 1 NE  A ARG 388 ? ? CZ A ARG 388 ? ? NH2 A ARG 388 ? ? 116.09 120.30 -4.21  0.50 N 
15 1 NE  A ARG 426 ? ? CZ A ARG 426 ? ? NH1 A ARG 426 ? ? 123.91 120.30 3.61   0.50 N 
16 1 CB  A VAL 518 ? ? CA A VAL 518 ? ? C   A VAL 518 ? ? 97.04  111.40 -14.36 1.90 N 
17 1 CG1 A VAL 518 ? ? CB A VAL 518 ? ? CG2 A VAL 518 ? ? 121.71 110.90 10.81  1.60 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 VAL A 22  ? ? -160.03 116.85  
2  1 SER A 25  ? ? -161.88 -164.29 
3  1 PHE A 45  ? ? 77.45   -10.24  
4  1 CYS A 94  ? ? -143.62 10.21   
5  1 PRO A 102 ? ? -48.71  155.66  
6  1 SER A 108 ? ? -154.38 71.71   
7  1 LEU A 158 ? ? -112.12 78.97   
8  1 SER A 200 ? ? 58.42   -117.38 
9  1 GLU A 299 ? ? -125.56 -74.73  
10 1 THR A 317 ? ? -162.72 -158.99 
11 1 ASP A 380 ? ? -158.87 64.16   
12 1 VAL A 400 ? ? -129.81 -58.35  
13 1 ARG A 515 ? ? 60.09   63.63   
14 1 GLN A 526 ? ? -122.95 -51.77  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ASP 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     2 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.087 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       1003 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.93 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     N 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     PG4 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      605 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     O1 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    F 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    PG4 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     1 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    O1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE              NAG 
3 1-methyl-1,2-dihydro-3H-indol-3-one OMI 
4 'TETRAETHYLENE GLYCOL'              PG4 
5 'ACETATE ION'                       ACT 
6 water                               HOH 
# 
