data_5FBH
# 
_entry.id   5FBH 
# 
_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   5FBH         
WWPDB D_1000216322 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          5FBK 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5FBH 
_pdbx_database_status.recvd_initial_deposition_date   2015-12-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Zhang, T.'     1 
'Zhang, C.'     2 
'Miller, C.L.'  3 
'Zou, J.'       4 
'Moremen, K.W.' 5 
'Brown, E.M.'   6 
'Yang, J.J.'    7 
'Hu, J.'        8 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            2 
_citation.language                  ? 
_citation.page_first                e1600241 
_citation.page_last                 e1600241 
_citation.title                     
;Structural basis for regulation of human calcium-sensing receptor by magnesium ions and an unexpected tryptophan derivative co-agonist.
;
_citation.year                      2016 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/sciadv.1600241 
_citation.pdbx_database_id_PubMed   27386547 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Zhang, C.'       1  
primary 'Zhang, T.'       2  
primary 'Zou, J.'         3  
primary 'Miller, C.L.'    4  
primary 'Gorkhali, R.'    5  
primary 'Yang, J.Y.'      6  
primary 'Schilmiller, A.' 7  
primary 'Wang, S.'        8  
primary 'Huang, K.'       9  
primary 'Brown, E.M.'     10 
primary 'Moremen, K.W.'   11 
primary 'Hu, J.'          12 
primary 'Yang, J.J.'      13 
# 
_cell.entry_id           5FBH 
_cell.length_a           172.107 
_cell.length_b           83.106 
_cell.length_c           94.470 
_cell.angle_alpha        90.00 
_cell.angle_beta         105.15 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         5FBH 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Extracellular calcium-sensing receptor' 64215.383 2  ? ? 'UNP residues 20-541' ? 
2 non-polymer syn 'GADOLINIUM ION'                         157.250   2  ? ? ?                     ? 
3 non-polymer syn 'MAGNESIUM ION'                          24.305    3  ? ? ?                     ? 
4 non-polymer syn 'BICARBONATE ION'                        61.017    2  ? ? ?                     ? 
5 non-polymer syn 'CHLORIDE ION'                           35.453    2  ? ? ?                     ? 
6 non-polymer man N-ACETYL-D-GLUCOSAMINE                   221.208   7  ? ? ?                     ? 
7 non-polymer syn CYCLOMETHYLTRYPTOPHAN                    216.236   2  ? ? ?                     ? 
8 water       nat water                                    18.015    17 ? ? ?                     ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'CaSR,Parathyroid cell calcium-sensing receptor 1,PCaR1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MRLLTALFAYFIVALILAFSVSAKSMHHHHHHHHSAWSHPQFEKEFYGPDQRAQKKGDIILGGLFPIHFGVAAKDQDLKS
RPESVECIRYNFRGFRWLQAMIFAIEEINSSPALLPNLTLGYRIFDTCNTVSKALEATLSFVAQNKIDSLNLDEFCNCSE
HIPSTIAVVGATGSGVSTAVANLLGLFYIPQVSYASSSRLLSNKNQFKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIA
ADDDYGRPGIEKFREEAEERDI(CSO)IDFSELISQYSDEEEIQHVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNIT
GKIWLASEAWASSSLIAMPQYFHVVGGTIGFALKAGQIPGFREFLKKVHPRKSVHNGFAKEFWEETFNCHLQEGAKGPLP
VDTFLRGHEESGDRFSNSSTAFRPLCTGDENISSVETPYIDYTHLRISYNVYLAVYSIAHALQDIYTCLPGRGLFTNGSC
ADIKKVEAWQVLKHLRHLNFTNNMGEQVTFDE(CSO)GDLVGNYSIINWHLSPEDGSIVFKEVGYYNVYAKKGERLFINE
EKILWSGFSREVPFSN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRLLTALFAYFIVALILAFSVSAKSMHHHHHHHHSAWSHPQFEKEFYGPDQRAQKKGDIILGGLFPIHFGVAAKDQDLKS
RPESVECIRYNFRGFRWLQAMIFAIEEINSSPALLPNLTLGYRIFDTCNTVSKALEATLSFVAQNKIDSLNLDEFCNCSE
HIPSTIAVVGATGSGVSTAVANLLGLFYIPQVSYASSSRLLSNKNQFKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIA
ADDDYGRPGIEKFREEAEERDICIDFSELISQYSDEEEIQHVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNITGKIW
LASEAWASSSLIAMPQYFHVVGGTIGFALKAGQIPGFREFLKKVHPRKSVHNGFAKEFWEETFNCHLQEGAKGPLPVDTF
LRGHEESGDRFSNSSTAFRPLCTGDENISSVETPYIDYTHLRISYNVYLAVYSIAHALQDIYTCLPGRGLFTNGSCADIK
KVEAWQVLKHLRHLNFTNNMGEQVTFDECGDLVGNYSIINWHLSPEDGSIVFKEVGYYNVYAKKGERLFINEEKILWSGF
SREVPFSN
;
_entity_poly.pdbx_strand_id                 B,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   MET n 
1 2   ARG n 
1 3   LEU n 
1 4   LEU n 
1 5   THR n 
1 6   ALA n 
1 7   LEU n 
1 8   PHE n 
1 9   ALA n 
1 10  TYR n 
1 11  PHE n 
1 12  ILE n 
1 13  VAL n 
1 14  ALA n 
1 15  LEU n 
1 16  ILE n 
1 17  LEU n 
1 18  ALA n 
1 19  PHE n 
1 20  SER n 
1 21  VAL n 
1 22  SER n 
1 23  ALA n 
1 24  LYS n 
1 25  SER n 
1 26  MET n 
1 27  HIS n 
1 28  HIS n 
1 29  HIS n 
1 30  HIS n 
1 31  HIS n 
1 32  HIS n 
1 33  HIS n 
1 34  HIS n 
1 35  SER n 
1 36  ALA n 
1 37  TRP n 
1 38  SER n 
1 39  HIS n 
1 40  PRO n 
1 41  GLN n 
1 42  PHE n 
1 43  GLU n 
1 44  LYS n 
1 45  GLU n 
1 46  PHE n 
1 47  TYR n 
1 48  GLY n 
1 49  PRO n 
1 50  ASP n 
1 51  GLN n 
1 52  ARG n 
1 53  ALA n 
1 54  GLN n 
1 55  LYS n 
1 56  LYS n 
1 57  GLY n 
1 58  ASP n 
1 59  ILE n 
1 60  ILE n 
1 61  LEU n 
1 62  GLY n 
1 63  GLY n 
1 64  LEU n 
1 65  PHE n 
1 66  PRO n 
1 67  ILE n 
1 68  HIS n 
1 69  PHE n 
1 70  GLY n 
1 71  VAL n 
1 72  ALA n 
1 73  ALA n 
1 74  LYS n 
1 75  ASP n 
1 76  GLN n 
1 77  ASP n 
1 78  LEU n 
1 79  LYS n 
1 80  SER n 
1 81  ARG n 
1 82  PRO n 
1 83  GLU n 
1 84  SER n 
1 85  VAL n 
1 86  GLU n 
1 87  CYS n 
1 88  ILE n 
1 89  ARG n 
1 90  TYR n 
1 91  ASN n 
1 92  PHE n 
1 93  ARG n 
1 94  GLY n 
1 95  PHE n 
1 96  ARG n 
1 97  TRP n 
1 98  LEU n 
1 99  GLN n 
1 100 ALA n 
1 101 MET n 
1 102 ILE n 
1 103 PHE n 
1 104 ALA n 
1 105 ILE n 
1 106 GLU n 
1 107 GLU n 
1 108 ILE n 
1 109 ASN n 
1 110 SER n 
1 111 SER n 
1 112 PRO n 
1 113 ALA n 
1 114 LEU n 
1 115 LEU n 
1 116 PRO n 
1 117 ASN n 
1 118 LEU n 
1 119 THR n 
1 120 LEU n 
1 121 GLY n 
1 122 TYR n 
1 123 ARG n 
1 124 ILE n 
1 125 PHE n 
1 126 ASP n 
1 127 THR n 
1 128 CYS n 
1 129 ASN n 
1 130 THR n 
1 131 VAL n 
1 132 SER n 
1 133 LYS n 
1 134 ALA n 
1 135 LEU n 
1 136 GLU n 
1 137 ALA n 
1 138 THR n 
1 139 LEU n 
1 140 SER n 
1 141 PHE n 
1 142 VAL n 
1 143 ALA n 
1 144 GLN n 
1 145 ASN n 
1 146 LYS n 
1 147 ILE n 
1 148 ASP n 
1 149 SER n 
1 150 LEU n 
1 151 ASN n 
1 152 LEU n 
1 153 ASP n 
1 154 GLU n 
1 155 PHE n 
1 156 CYS n 
1 157 ASN n 
1 158 CYS n 
1 159 SER n 
1 160 GLU n 
1 161 HIS n 
1 162 ILE n 
1 163 PRO n 
1 164 SER n 
1 165 THR n 
1 166 ILE n 
1 167 ALA n 
1 168 VAL n 
1 169 VAL n 
1 170 GLY n 
1 171 ALA n 
1 172 THR n 
1 173 GLY n 
1 174 SER n 
1 175 GLY n 
1 176 VAL n 
1 177 SER n 
1 178 THR n 
1 179 ALA n 
1 180 VAL n 
1 181 ALA n 
1 182 ASN n 
1 183 LEU n 
1 184 LEU n 
1 185 GLY n 
1 186 LEU n 
1 187 PHE n 
1 188 TYR n 
1 189 ILE n 
1 190 PRO n 
1 191 GLN n 
1 192 VAL n 
1 193 SER n 
1 194 TYR n 
1 195 ALA n 
1 196 SER n 
1 197 SER n 
1 198 SER n 
1 199 ARG n 
1 200 LEU n 
1 201 LEU n 
1 202 SER n 
1 203 ASN n 
1 204 LYS n 
1 205 ASN n 
1 206 GLN n 
1 207 PHE n 
1 208 LYS n 
1 209 SER n 
1 210 PHE n 
1 211 LEU n 
1 212 ARG n 
1 213 THR n 
1 214 ILE n 
1 215 PRO n 
1 216 ASN n 
1 217 ASP n 
1 218 GLU n 
1 219 HIS n 
1 220 GLN n 
1 221 ALA n 
1 222 THR n 
1 223 ALA n 
1 224 MET n 
1 225 ALA n 
1 226 ASP n 
1 227 ILE n 
1 228 ILE n 
1 229 GLU n 
1 230 TYR n 
1 231 PHE n 
1 232 ARG n 
1 233 TRP n 
1 234 ASN n 
1 235 TRP n 
1 236 VAL n 
1 237 GLY n 
1 238 THR n 
1 239 ILE n 
1 240 ALA n 
1 241 ALA n 
1 242 ASP n 
1 243 ASP n 
1 244 ASP n 
1 245 TYR n 
1 246 GLY n 
1 247 ARG n 
1 248 PRO n 
1 249 GLY n 
1 250 ILE n 
1 251 GLU n 
1 252 LYS n 
1 253 PHE n 
1 254 ARG n 
1 255 GLU n 
1 256 GLU n 
1 257 ALA n 
1 258 GLU n 
1 259 GLU n 
1 260 ARG n 
1 261 ASP n 
1 262 ILE n 
1 263 CSO n 
1 264 ILE n 
1 265 ASP n 
1 266 PHE n 
1 267 SER n 
1 268 GLU n 
1 269 LEU n 
1 270 ILE n 
1 271 SER n 
1 272 GLN n 
1 273 TYR n 
1 274 SER n 
1 275 ASP n 
1 276 GLU n 
1 277 GLU n 
1 278 GLU n 
1 279 ILE n 
1 280 GLN n 
1 281 HIS n 
1 282 VAL n 
1 283 VAL n 
1 284 GLU n 
1 285 VAL n 
1 286 ILE n 
1 287 GLN n 
1 288 ASN n 
1 289 SER n 
1 290 THR n 
1 291 ALA n 
1 292 LYS n 
1 293 VAL n 
1 294 ILE n 
1 295 VAL n 
1 296 VAL n 
1 297 PHE n 
1 298 SER n 
1 299 SER n 
1 300 GLY n 
1 301 PRO n 
1 302 ASP n 
1 303 LEU n 
1 304 GLU n 
1 305 PRO n 
1 306 LEU n 
1 307 ILE n 
1 308 LYS n 
1 309 GLU n 
1 310 ILE n 
1 311 VAL n 
1 312 ARG n 
1 313 ARG n 
1 314 ASN n 
1 315 ILE n 
1 316 THR n 
1 317 GLY n 
1 318 LYS n 
1 319 ILE n 
1 320 TRP n 
1 321 LEU n 
1 322 ALA n 
1 323 SER n 
1 324 GLU n 
1 325 ALA n 
1 326 TRP n 
1 327 ALA n 
1 328 SER n 
1 329 SER n 
1 330 SER n 
1 331 LEU n 
1 332 ILE n 
1 333 ALA n 
1 334 MET n 
1 335 PRO n 
1 336 GLN n 
1 337 TYR n 
1 338 PHE n 
1 339 HIS n 
1 340 VAL n 
1 341 VAL n 
1 342 GLY n 
1 343 GLY n 
1 344 THR n 
1 345 ILE n 
1 346 GLY n 
1 347 PHE n 
1 348 ALA n 
1 349 LEU n 
1 350 LYS n 
1 351 ALA n 
1 352 GLY n 
1 353 GLN n 
1 354 ILE n 
1 355 PRO n 
1 356 GLY n 
1 357 PHE n 
1 358 ARG n 
1 359 GLU n 
1 360 PHE n 
1 361 LEU n 
1 362 LYS n 
1 363 LYS n 
1 364 VAL n 
1 365 HIS n 
1 366 PRO n 
1 367 ARG n 
1 368 LYS n 
1 369 SER n 
1 370 VAL n 
1 371 HIS n 
1 372 ASN n 
1 373 GLY n 
1 374 PHE n 
1 375 ALA n 
1 376 LYS n 
1 377 GLU n 
1 378 PHE n 
1 379 TRP n 
1 380 GLU n 
1 381 GLU n 
1 382 THR n 
1 383 PHE n 
1 384 ASN n 
1 385 CYS n 
1 386 HIS n 
1 387 LEU n 
1 388 GLN n 
1 389 GLU n 
1 390 GLY n 
1 391 ALA n 
1 392 LYS n 
1 393 GLY n 
1 394 PRO n 
1 395 LEU n 
1 396 PRO n 
1 397 VAL n 
1 398 ASP n 
1 399 THR n 
1 400 PHE n 
1 401 LEU n 
1 402 ARG n 
1 403 GLY n 
1 404 HIS n 
1 405 GLU n 
1 406 GLU n 
1 407 SER n 
1 408 GLY n 
1 409 ASP n 
1 410 ARG n 
1 411 PHE n 
1 412 SER n 
1 413 ASN n 
1 414 SER n 
1 415 SER n 
1 416 THR n 
1 417 ALA n 
1 418 PHE n 
1 419 ARG n 
1 420 PRO n 
1 421 LEU n 
1 422 CYS n 
1 423 THR n 
1 424 GLY n 
1 425 ASP n 
1 426 GLU n 
1 427 ASN n 
1 428 ILE n 
1 429 SER n 
1 430 SER n 
1 431 VAL n 
1 432 GLU n 
1 433 THR n 
1 434 PRO n 
1 435 TYR n 
1 436 ILE n 
1 437 ASP n 
1 438 TYR n 
1 439 THR n 
1 440 HIS n 
1 441 LEU n 
1 442 ARG n 
1 443 ILE n 
1 444 SER n 
1 445 TYR n 
1 446 ASN n 
1 447 VAL n 
1 448 TYR n 
1 449 LEU n 
1 450 ALA n 
1 451 VAL n 
1 452 TYR n 
1 453 SER n 
1 454 ILE n 
1 455 ALA n 
1 456 HIS n 
1 457 ALA n 
1 458 LEU n 
1 459 GLN n 
1 460 ASP n 
1 461 ILE n 
1 462 TYR n 
1 463 THR n 
1 464 CYS n 
1 465 LEU n 
1 466 PRO n 
1 467 GLY n 
1 468 ARG n 
1 469 GLY n 
1 470 LEU n 
1 471 PHE n 
1 472 THR n 
1 473 ASN n 
1 474 GLY n 
1 475 SER n 
1 476 CYS n 
1 477 ALA n 
1 478 ASP n 
1 479 ILE n 
1 480 LYS n 
1 481 LYS n 
1 482 VAL n 
1 483 GLU n 
1 484 ALA n 
1 485 TRP n 
1 486 GLN n 
1 487 VAL n 
1 488 LEU n 
1 489 LYS n 
1 490 HIS n 
1 491 LEU n 
1 492 ARG n 
1 493 HIS n 
1 494 LEU n 
1 495 ASN n 
1 496 PHE n 
1 497 THR n 
1 498 ASN n 
1 499 ASN n 
1 500 MET n 
1 501 GLY n 
1 502 GLU n 
1 503 GLN n 
1 504 VAL n 
1 505 THR n 
1 506 PHE n 
1 507 ASP n 
1 508 GLU n 
1 509 CSO n 
1 510 GLY n 
1 511 ASP n 
1 512 LEU n 
1 513 VAL n 
1 514 GLY n 
1 515 ASN n 
1 516 TYR n 
1 517 SER n 
1 518 ILE n 
1 519 ILE n 
1 520 ASN n 
1 521 TRP n 
1 522 HIS n 
1 523 LEU n 
1 524 SER n 
1 525 PRO n 
1 526 GLU n 
1 527 ASP n 
1 528 GLY n 
1 529 SER n 
1 530 ILE n 
1 531 VAL n 
1 532 PHE n 
1 533 LYS n 
1 534 GLU n 
1 535 VAL n 
1 536 GLY n 
1 537 TYR n 
1 538 TYR n 
1 539 ASN n 
1 540 VAL n 
1 541 TYR n 
1 542 ALA n 
1 543 LYS n 
1 544 LYS n 
1 545 GLY n 
1 546 GLU n 
1 547 ARG n 
1 548 LEU n 
1 549 PHE n 
1 550 ILE n 
1 551 ASN n 
1 552 GLU n 
1 553 GLU n 
1 554 LYS n 
1 555 ILE n 
1 556 LEU n 
1 557 TRP n 
1 558 SER n 
1 559 GLY n 
1 560 PHE n 
1 561 SER n 
1 562 ARG n 
1 563 GLU n 
1 564 VAL n 
1 565 PRO n 
1 566 PHE n 
1 567 SER n 
1 568 ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   568 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CASR, GPRC2A, PCAR1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            HEK293 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.db_code                    CASR_HUMAN 
_struct_ref.db_name                    UNP 
_struct_ref.details                    ? 
_struct_ref.entity_id                  1 
_struct_ref.id                         1 
_struct_ref.seq_align                  ? 
_struct_ref.seq_dif                    ? 
_struct_ref.pdbx_db_accession          P41180 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.pdbx_seq_one_letter_code   
;YGPDQRAQKKGDIILGGLFPIHFGVAAKDQDLKSRPESVECIRYNFRGFRWLQAMIFAIEEINSSPALLPNLTLGYRIFD
TCNTVSKALEATLSFVAQNKIDSLNLDEFCNCSEHIPSTIAVVGATGSGVSTAVANLLGLFYIPQVSYASSSRLLSNKNQ
FKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIAADDDYGRPGIEKFREEAEERDICIDFSELISQYSDEEEIQHVVEVI
QNSTAKVIVVFSSGPDLEPLIKEIVRRNITGKIWLASEAWASSSLIAMPQYFHVVGGTIGFALKAGQIPGFREFLKKVHP
RKSVHNGFAKEFWEETFNCHLQEGAKGPLPVDTFLRGHEESGDRFSNSSTAFRPLCTGDENISSVETPYIDYTHLRISYN
VYLAVYSIAHALQDIYTCLPGRGLFTNGSCADIKKVEAWQVLKHLRHLNFTNNMGEQVTFDECGDLVGNYSIINWHLSPE
DGSIVFKEVGYYNVYAKKGERLFINEEKILWSGFSREVPFSN
;
_struct_ref.pdbx_align_begin           20 
_struct_ref.pdbx_align_end             ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5FBH B 47 ? 568 ? P41180 20 ? 541 ? 20 541 
2 1 5FBH A 47 ? 568 ? P41180 20 ? 541 ? 20 541 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 5FBH MET B 1  ? UNP P41180 ? ? 'initiating methionine' -26 1  
1 5FBH ARG B 2  ? UNP P41180 ? ? 'expression tag'        -25 2  
1 5FBH LEU B 3  ? UNP P41180 ? ? 'expression tag'        -24 3  
1 5FBH LEU B 4  ? UNP P41180 ? ? 'expression tag'        -23 4  
1 5FBH THR B 5  ? UNP P41180 ? ? 'expression tag'        -22 5  
1 5FBH ALA B 6  ? UNP P41180 ? ? 'expression tag'        -21 6  
1 5FBH LEU B 7  ? UNP P41180 ? ? 'expression tag'        -20 7  
1 5FBH PHE B 8  ? UNP P41180 ? ? 'expression tag'        -19 8  
1 5FBH ALA B 9  ? UNP P41180 ? ? 'expression tag'        -18 9  
1 5FBH TYR B 10 ? UNP P41180 ? ? 'expression tag'        -17 10 
1 5FBH PHE B 11 ? UNP P41180 ? ? 'expression tag'        -16 11 
1 5FBH ILE B 12 ? UNP P41180 ? ? 'expression tag'        -15 12 
1 5FBH VAL B 13 ? UNP P41180 ? ? 'expression tag'        -14 13 
1 5FBH ALA B 14 ? UNP P41180 ? ? 'expression tag'        -13 14 
1 5FBH LEU B 15 ? UNP P41180 ? ? 'expression tag'        -12 15 
1 5FBH ILE B 16 ? UNP P41180 ? ? 'expression tag'        -11 16 
1 5FBH LEU B 17 ? UNP P41180 ? ? 'expression tag'        -10 17 
1 5FBH ALA B 18 ? UNP P41180 ? ? 'expression tag'        -9  18 
1 5FBH PHE B 19 ? UNP P41180 ? ? 'expression tag'        -8  19 
1 5FBH SER B 20 ? UNP P41180 ? ? 'expression tag'        -7  20 
1 5FBH VAL B 21 ? UNP P41180 ? ? 'expression tag'        -6  21 
1 5FBH SER B 22 ? UNP P41180 ? ? 'expression tag'        -5  22 
1 5FBH ALA B 23 ? UNP P41180 ? ? 'expression tag'        -4  23 
1 5FBH LYS B 24 ? UNP P41180 ? ? 'expression tag'        -3  24 
1 5FBH SER B 25 ? UNP P41180 ? ? 'expression tag'        -2  25 
1 5FBH MET B 26 ? UNP P41180 ? ? 'expression tag'        -1  26 
1 5FBH HIS B 27 ? UNP P41180 ? ? 'expression tag'        0   27 
1 5FBH HIS B 28 ? UNP P41180 ? ? 'expression tag'        1   28 
1 5FBH HIS B 29 ? UNP P41180 ? ? 'expression tag'        2   29 
1 5FBH HIS B 30 ? UNP P41180 ? ? 'expression tag'        3   30 
1 5FBH HIS B 31 ? UNP P41180 ? ? 'expression tag'        4   31 
1 5FBH HIS B 32 ? UNP P41180 ? ? 'expression tag'        5   32 
1 5FBH HIS B 33 ? UNP P41180 ? ? 'expression tag'        6   33 
1 5FBH HIS B 34 ? UNP P41180 ? ? 'expression tag'        7   34 
1 5FBH SER B 35 ? UNP P41180 ? ? 'expression tag'        8   35 
1 5FBH ALA B 36 ? UNP P41180 ? ? 'expression tag'        9   36 
1 5FBH TRP B 37 ? UNP P41180 ? ? 'expression tag'        10  37 
1 5FBH SER B 38 ? UNP P41180 ? ? 'expression tag'        11  38 
1 5FBH HIS B 39 ? UNP P41180 ? ? 'expression tag'        12  39 
1 5FBH PRO B 40 ? UNP P41180 ? ? 'expression tag'        13  40 
1 5FBH GLN B 41 ? UNP P41180 ? ? 'expression tag'        14  41 
1 5FBH PHE B 42 ? UNP P41180 ? ? 'expression tag'        15  42 
1 5FBH GLU B 43 ? UNP P41180 ? ? 'expression tag'        16  43 
1 5FBH LYS B 44 ? UNP P41180 ? ? 'expression tag'        17  44 
1 5FBH GLU B 45 ? UNP P41180 ? ? 'expression tag'        18  45 
1 5FBH PHE B 46 ? UNP P41180 ? ? 'expression tag'        19  46 
2 5FBH MET A 1  ? UNP P41180 ? ? 'initiating methionine' -26 47 
2 5FBH ARG A 2  ? UNP P41180 ? ? 'expression tag'        -25 48 
2 5FBH LEU A 3  ? UNP P41180 ? ? 'expression tag'        -24 49 
2 5FBH LEU A 4  ? UNP P41180 ? ? 'expression tag'        -23 50 
2 5FBH THR A 5  ? UNP P41180 ? ? 'expression tag'        -22 51 
2 5FBH ALA A 6  ? UNP P41180 ? ? 'expression tag'        -21 52 
2 5FBH LEU A 7  ? UNP P41180 ? ? 'expression tag'        -20 53 
2 5FBH PHE A 8  ? UNP P41180 ? ? 'expression tag'        -19 54 
2 5FBH ALA A 9  ? UNP P41180 ? ? 'expression tag'        -18 55 
2 5FBH TYR A 10 ? UNP P41180 ? ? 'expression tag'        -17 56 
2 5FBH PHE A 11 ? UNP P41180 ? ? 'expression tag'        -16 57 
2 5FBH ILE A 12 ? UNP P41180 ? ? 'expression tag'        -15 58 
2 5FBH VAL A 13 ? UNP P41180 ? ? 'expression tag'        -14 59 
2 5FBH ALA A 14 ? UNP P41180 ? ? 'expression tag'        -13 60 
2 5FBH LEU A 15 ? UNP P41180 ? ? 'expression tag'        -12 61 
2 5FBH ILE A 16 ? UNP P41180 ? ? 'expression tag'        -11 62 
2 5FBH LEU A 17 ? UNP P41180 ? ? 'expression tag'        -10 63 
2 5FBH ALA A 18 ? UNP P41180 ? ? 'expression tag'        -9  64 
2 5FBH PHE A 19 ? UNP P41180 ? ? 'expression tag'        -8  65 
2 5FBH SER A 20 ? UNP P41180 ? ? 'expression tag'        -7  66 
2 5FBH VAL A 21 ? UNP P41180 ? ? 'expression tag'        -6  67 
2 5FBH SER A 22 ? UNP P41180 ? ? 'expression tag'        -5  68 
2 5FBH ALA A 23 ? UNP P41180 ? ? 'expression tag'        -4  69 
2 5FBH LYS A 24 ? UNP P41180 ? ? 'expression tag'        -3  70 
2 5FBH SER A 25 ? UNP P41180 ? ? 'expression tag'        -2  71 
2 5FBH MET A 26 ? UNP P41180 ? ? 'expression tag'        -1  72 
2 5FBH HIS A 27 ? UNP P41180 ? ? 'expression tag'        0   73 
2 5FBH HIS A 28 ? UNP P41180 ? ? 'expression tag'        1   74 
2 5FBH HIS A 29 ? UNP P41180 ? ? 'expression tag'        2   75 
2 5FBH HIS A 30 ? UNP P41180 ? ? 'expression tag'        3   76 
2 5FBH HIS A 31 ? UNP P41180 ? ? 'expression tag'        4   77 
2 5FBH HIS A 32 ? UNP P41180 ? ? 'expression tag'        5   78 
2 5FBH HIS A 33 ? UNP P41180 ? ? 'expression tag'        6   79 
2 5FBH HIS A 34 ? UNP P41180 ? ? 'expression tag'        7   80 
2 5FBH SER A 35 ? UNP P41180 ? ? 'expression tag'        8   81 
2 5FBH ALA A 36 ? UNP P41180 ? ? 'expression tag'        9   82 
2 5FBH TRP A 37 ? UNP P41180 ? ? 'expression tag'        10  83 
2 5FBH SER A 38 ? UNP P41180 ? ? 'expression tag'        11  84 
2 5FBH HIS A 39 ? UNP P41180 ? ? 'expression tag'        12  85 
2 5FBH PRO A 40 ? UNP P41180 ? ? 'expression tag'        13  86 
2 5FBH GLN A 41 ? UNP P41180 ? ? 'expression tag'        14  87 
2 5FBH PHE A 42 ? UNP P41180 ? ? 'expression tag'        15  88 
2 5FBH GLU A 43 ? UNP P41180 ? ? 'expression tag'        16  89 
2 5FBH LYS A 44 ? UNP P41180 ? ? 'expression tag'        17  90 
2 5FBH GLU A 45 ? UNP P41180 ? ? 'expression tag'        18  91 
2 5FBH PHE A 46 ? UNP P41180 ? ? 'expression tag'        19  92 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
BCT non-polymer         . 'BICARBONATE ION'      ? 'C H O3 -1'      61.017  
CL  non-polymer         . 'CHLORIDE ION'         ? 'Cl -1'          35.453  
CSO 'L-peptide linking' n S-HYDROXYCYSTEINE      ? 'C3 H7 N O3 S'   137.158 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
GD3 non-polymer         . 'GADOLINIUM ION'       ? 'Gd 3'           157.250 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
MG  non-polymer         . 'MAGNESIUM ION'        ? 'Mg 2'           24.305  
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
TCR 'L-peptide linking' n CYCLOMETHYLTRYPTOPHAN  ? 'C12 H12 N2 O2'  216.236 
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                   5FBH 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.54 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         51.58 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            294 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '10% PEG 8000, 200 mM MgCl2, 10 mM CaCl2 and 100 mM Tris-HCl, 0.5 mM GdCl3' 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 300 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-11-21 
# 
_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   1.6985 
_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                        'APS BEAMLINE 21-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.6985 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.d_resolution_high            2.700 
_reflns.d_resolution_low             50.000 
_reflns.pdbx_number_measured_all     125177 
_reflns.number_obs                   34777 
_reflns.pdbx_Rmerge_I_obs            0.093 
_reflns.pdbx_netI_over_av_sigmaI     11.901 
_reflns.pdbx_netI_over_sigmaI        11.800 
_reflns.pdbx_chi_squared             1.061 
_reflns.pdbx_redundancy              3.600 
_reflns.percent_possible_obs         98.900 
_reflns.pdbx_Rrim_I_all              0.110 
_reflns.pdbx_Rpim_I_all              0.058 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     5FBH 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1  2.700 2.800  ? ? ? 0 0.772 ? ? 1.043 3.600 ? ? ? 3480 ? ? ? ? 99.900  0.905 0.468 0.645 
1 2  2.800 2.910  ? ? ? 0 0.529 ? ? 1.092 3.700 ? ? ? 3507 ? ? ? ? 100.000 0.619 0.319 0.773 
1 3  2.910 3.040  ? ? ? 0 0.374 ? ? 1.079 3.700 ? ? ? 3478 ? ? ? ? 99.900  0.439 0.227 0.862 
1 4  3.040 3.200  ? ? ? 0 0.260 ? ? 1.074 3.700 ? ? ? 3485 ? ? ? ? 99.700  0.306 0.159 0.918 
1 5  3.200 3.400  ? ? ? 0 0.174 ? ? 1.096 3.700 ? ? ? 3493 ? ? ? ? 99.500  0.205 0.106 0.959 
1 6  3.400 3.660  ? ? ? 0 0.124 ? ? 1.094 3.700 ? ? ? 3492 ? ? ? ? 99.300  0.145 0.076 0.979 
1 7  3.660 4.030  ? ? ? 0 0.089 ? ? 1.057 3.600 ? ? ? 3447 ? ? ? ? 98.700  0.105 0.055 0.989 
1 8  4.030 4.620  ? ? ? 0 0.070 ? ? 1.020 3.500 ? ? ? 3475 ? ? ? ? 98.700  0.083 0.044 0.991 
1 9  4.620 5.810  ? ? ? 0 0.064 ? ? 1.043 3.500 ? ? ? 3474 ? ? ? ? 98.200  0.076 0.040 0.992 
1 10 5.810 50.000 ? ? ? 0 0.059 ? ? 0.996 3.300 ? ? ? 3446 ? ? ? ? 95.200  0.072 0.040 0.991 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 5FBH 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     33039 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             46.08 
_refine.ls_d_res_high                            2.70 
_refine.ls_percent_reflns_obs                    97.4 
_refine.ls_R_factor_obs                          0.184 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.182 
_refine.ls_R_factor_R_free                       0.236 
_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                  1733 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.956 
_refine.correlation_coeff_Fo_to_Fc_free          0.931 
_refine.B_iso_mean                               65.27 
_refine.aniso_B[1][1]                            -0.60000 
_refine.aniso_B[2][2]                            0.41000 
_refine.aniso_B[3][3]                            0.88000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.52000 
_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' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_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                       0.741 
_refine.pdbx_overall_ESU_R_Free                  0.309 
_refine.overall_SU_ML                            0.233 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             11.524 
_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        7232 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         145 
_refine_hist.number_atoms_solvent             17 
_refine_hist.number_atoms_total               7394 
_refine_hist.d_res_high                       2.70 
_refine_hist.d_res_low                        46.08 
# 
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             0.012  0.019  ? 7577  'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.020  ? 6857  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.578  1.957  ? 10324 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.913  3.000  ? 15627 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.396  5.000  ? 936   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       32.835 23.814 ? 333   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       17.149 15.000 ? 1099  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       17.986 15.000 ? 37    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.087  0.200  ? 1160  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.006  0.020  ? 8671  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 1830  '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                  4.619  6.528  ? 3766  'X-RAY DIFFRACTION' ? 
r_mcbond_other               4.618  6.528  ? 3766  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 6.859  9.788  ? 4694  'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_it                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?     '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                       2.70 
_refine_ls_shell.d_res_low                        2.77 
_refine_ls_shell.number_reflns_R_work             1994 
_refine_ls_shell.R_factor_R_work                  0.3430 
_refine_ls_shell.percent_reflns_obs               79.44 
_refine_ls_shell.R_factor_R_free                  0.3880 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             108 
_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                     5FBH 
_struct.title                        
'Crystal structure of the extracellular domain of human calcium sensing receptor with bound Gd3+' 
_struct.pdbx_descriptor              'Extracellular calcium-sensing receptor' 
_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        5FBH 
_struct_keywords.text            'membrane protein, G-protein coupled receptor, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
J N N 6 ? 
K N N 7 ? 
L N N 2 ? 
M N N 3 ? 
N N N 4 ? 
O N N 5 ? 
P N N 6 ? 
Q N N 6 ? 
R N N 6 ? 
S N N 6 ? 
T N N 7 ? 
U N N 8 ? 
V N N 8 ? 
# 
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 ASN A 91  ? SER A 111 ? ASN B 64  SER B 84  1 ? 21 
HELX_P HELX_P2  AA2 THR A 130 ? VAL A 142 ? THR B 103 VAL B 115 1 ? 13 
HELX_P HELX_P3  AA3 VAL A 142 ? ASP A 148 ? VAL B 115 ASP B 121 1 ? 7  
HELX_P HELX_P4  AA4 GLY A 173 ? GLY A 185 ? GLY B 146 GLY B 158 1 ? 13 
HELX_P HELX_P5  AA5 LEU A 186 ? TYR A 188 ? LEU B 159 TYR B 161 5 ? 3  
HELX_P HELX_P6  AA6 SER A 198 ? ASN A 203 ? SER B 171 ASN B 176 5 ? 6  
HELX_P HELX_P7  AA7 ASN A 216 ? PHE A 231 ? ASN B 189 PHE B 204 1 ? 16 
HELX_P HELX_P8  AA8 TYR A 245 ? ARG A 260 ? TYR B 218 ARG B 233 1 ? 16 
HELX_P HELX_P9  AA9 ASP A 275 ? ASN A 288 ? ASP B 248 ASN B 261 1 ? 14 
HELX_P HELX_P10 AB1 SER A 299 ? ARG A 313 ? SER B 272 ARG B 286 1 ? 15 
HELX_P HELX_P11 AB2 MET A 334 ? GLN A 336 ? MET B 307 GLN B 309 5 ? 3  
HELX_P HELX_P12 AB3 TYR A 337 ? GLY A 342 ? TYR B 310 GLY B 315 1 ? 6  
HELX_P HELX_P13 AB4 GLY A 356 ? LYS A 362 ? GLY B 329 LYS B 335 1 ? 7  
HELX_P HELX_P14 AB5 PHE A 374 ? ASN A 384 ? PHE B 347 ASN B 357 1 ? 11 
HELX_P HELX_P15 AB6 ASN A 427 ? VAL A 431 ? ASN B 400 VAL B 404 5 ? 5  
HELX_P HELX_P16 AB7 ARG A 442 ? THR A 463 ? ARG B 415 THR B 436 1 ? 22 
HELX_P HELX_P17 AB8 PHE A 471 ? SER A 475 ? PHE B 444 SER B 448 5 ? 5  
HELX_P HELX_P18 AB9 ASP A 478 ? VAL A 482 ? ASP B 451 VAL B 455 5 ? 5  
HELX_P HELX_P19 AC1 GLU A 483 ? LEU A 494 ? GLU B 456 LEU B 467 1 ? 12 
HELX_P HELX_P20 AC2 GLU A 552 ? ILE A 555 ? GLU B 525 ILE B 528 5 ? 4  
HELX_P HELX_P21 AC3 ASN B 91  ? SER B 111 ? ASN A 64  SER A 84  1 ? 21 
HELX_P HELX_P22 AC4 THR B 130 ? VAL B 142 ? THR A 103 VAL A 115 1 ? 13 
HELX_P HELX_P23 AC5 VAL B 142 ? ASP B 148 ? VAL A 115 ASP A 121 1 ? 7  
HELX_P HELX_P24 AC6 GLY B 173 ? PHE B 187 ? GLY A 146 PHE A 160 1 ? 15 
HELX_P HELX_P25 AC7 SER B 198 ? ASN B 203 ? SER A 171 ASN A 176 5 ? 6  
HELX_P HELX_P26 AC8 ASP B 217 ? PHE B 231 ? ASP A 190 PHE A 204 1 ? 15 
HELX_P HELX_P27 AC9 TYR B 245 ? ARG B 260 ? TYR A 218 ARG A 233 1 ? 16 
HELX_P HELX_P28 AD1 ASP B 275 ? ASN B 288 ? ASP A 248 ASN A 261 1 ? 14 
HELX_P HELX_P29 AD2 SER B 299 ? ARG B 313 ? SER A 272 ARG A 286 1 ? 15 
HELX_P HELX_P30 AD3 SER B 323 ? SER B 328 ? SER A 296 SER A 301 1 ? 6  
HELX_P HELX_P31 AD4 MET B 334 ? GLN B 336 ? MET A 307 GLN A 309 5 ? 3  
HELX_P HELX_P32 AD5 TYR B 337 ? GLY B 342 ? TYR A 310 GLY A 315 1 ? 6  
HELX_P HELX_P33 AD6 GLY B 356 ? LYS B 363 ? GLY A 329 LYS A 336 1 ? 8  
HELX_P HELX_P34 AD7 PHE B 374 ? ASN B 384 ? PHE A 347 ASN A 357 1 ? 11 
HELX_P HELX_P35 AD8 ASN B 427 ? VAL B 431 ? ASN A 400 VAL A 404 5 ? 5  
HELX_P HELX_P36 AD9 ARG B 442 ? THR B 463 ? ARG A 415 THR A 436 1 ? 22 
HELX_P HELX_P37 AE1 PHE B 471 ? SER B 475 ? PHE A 444 SER A 448 5 ? 5  
HELX_P HELX_P38 AE2 GLU B 483 ? LEU B 494 ? GLU A 456 LEU A 467 1 ? 12 
HELX_P HELX_P39 AE3 GLU B 552 ? ILE B 555 ? GLU A 525 ILE A 528 5 ? 4  
# 
_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 87  SG  ? ? ? 1_555 A CYS 128 SG ? ? B CYS 60  B CYS 101 1_555 ? ? ? ? ? ? ? 2.017 ? 
disulf2  disulf ?    ? A CYS 385 SG  ? ? ? 1_555 A CYS 422 SG ? ? B CYS 358 B CYS 395 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf3  disulf ?    ? A CYS 464 SG  ? ? ? 1_555 A CYS 476 SG ? ? B CYS 437 B CYS 449 1_555 ? ? ? ? ? ? ? 2.058 ? 
disulf4  disulf ?    ? B CYS 87  SG  ? ? ? 1_555 B CYS 128 SG ? ? A CYS 60  A CYS 101 1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf5  disulf ?    ? B CYS 385 SG  ? ? ? 1_555 B CYS 422 SG ? ? A CYS 358 A CYS 395 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf6  disulf ?    ? B CYS 464 SG  ? ? ? 1_555 B CYS 476 SG ? ? A CYS 437 A CYS 449 1_555 ? ? ? ? ? ? ? 2.058 ? 
metalc1  metalc ?    ? A ILE 108 O   ? ? ? 1_555 E MG  .   MG ? ? B ILE 81  B MG  603 1_555 ? ? ? ? ? ? ? 2.785 ? 
metalc2  metalc ?    ? A LEU 114 O   ? ? ? 1_555 E MG  .   MG ? ? B LEU 87  B MG  603 1_555 ? ? ? ? ? ? ? 2.920 ? 
metalc3  metalc ?    ? A LEU 115 O   ? ? ? 1_555 E MG  .   MG ? ? B LEU 88  B MG  603 1_555 ? ? ? ? ? ? ? 2.607 ? 
metalc4  metalc ?    ? A GLU 256 OE1 ? ? ? 1_555 C GD3 .   GD ? ? B GLU 229 B GD3 601 1_555 ? ? ? ? ? ? ? 2.735 ? 
metalc5  metalc ?    ? A GLU 256 OE2 ? ? ? 1_555 C GD3 .   GD ? ? B GLU 229 B GD3 601 1_555 ? ? ? ? ? ? ? 2.700 ? 
metalc6  metalc ?    ? A GLU 259 OE1 ? ? ? 1_555 C GD3 .   GD ? ? B GLU 232 B GD3 601 1_555 ? ? ? ? ? ? ? 2.681 ? 
covale1  covale both ? A ILE 262 C   ? ? ? 1_555 A CSO 263 N  ? ? B ILE 235 B CSO 236 1_555 ? ? ? ? ? ? ? 1.326 ? 
covale2  covale both ? A CSO 263 C   ? ? ? 1_555 A ILE 264 N  ? ? B CSO 236 B ILE 237 1_555 ? ? ? ? ? ? ? 1.326 ? 
metalc7  metalc ?    ? A SER 267 O   ? ? ? 1_555 D MG  .   MG ? ? B SER 240 B MG  602 1_555 ? ? ? ? ? ? ? 2.573 ? 
metalc8  metalc ?    ? A SER 267 OG  ? ? ? 1_555 D MG  .   MG ? ? B SER 240 B MG  602 1_555 ? ? ? ? ? ? ? 2.381 ? 
covale3  covale one  ? A ASN 288 ND2 ? ? ? 1_555 H NAG .   C1 ? ? B ASN 261 B NAG 606 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale4  covale one  ? A ASN 314 ND2 ? ? ? 1_555 I NAG .   C1 ? ? B ASN 287 B NAG 607 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale5  covale one  ? A ASN 495 ND2 ? ? ? 1_555 J NAG .   C1 ? ? B ASN 468 B NAG 608 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale6  covale both ? A GLU 508 C   ? ? ? 1_555 A CSO 509 N  ? ? B GLU 481 B CSO 482 1_555 ? ? ? ? ? ? ? 1.330 ? 
covale7  covale both ? A CSO 509 C   ? ? ? 1_555 A GLY 510 N  ? ? B CSO 482 B GLY 483 1_555 ? ? ? ? ? ? ? 1.328 ? 
metalc9  metalc ?    ? B ILE 108 O   ? ? ? 1_555 M MG  .   MG ? ? A ILE 81  A MG  602 1_555 ? ? ? ? ? ? ? 2.521 ? 
metalc10 metalc ?    ? B SER 111 O   ? ? ? 1_555 M MG  .   MG ? ? A SER 84  A MG  602 1_555 ? ? ? ? ? ? ? 2.754 ? 
metalc11 metalc ?    ? B LEU 114 O   ? ? ? 1_555 M MG  .   MG ? ? A LEU 87  A MG  602 1_555 ? ? ? ? ? ? ? 2.526 ? 
metalc12 metalc ?    ? B LEU 115 O   ? ? ? 1_555 M MG  .   MG ? ? A LEU 88  A MG  602 1_555 ? ? ? ? ? ? ? 2.668 ? 
metalc13 metalc ?    ? B GLU 256 OE1 ? ? ? 1_555 L GD3 .   GD ? ? A GLU 229 A GD3 601 1_555 ? ? ? ? ? ? ? 2.732 ? 
metalc14 metalc ?    ? B GLU 256 OE2 ? ? ? 1_555 L GD3 .   GD ? ? A GLU 229 A GD3 601 1_555 ? ? ? ? ? ? ? 2.713 ? 
metalc15 metalc ?    ? B GLU 259 OE1 ? ? ? 1_555 L GD3 .   GD ? ? A GLU 232 A GD3 601 1_555 ? ? ? ? ? ? ? 2.526 ? 
covale8  covale both ? B ILE 262 C   ? ? ? 1_555 B CSO 263 N  ? ? A ILE 235 A CSO 236 1_555 ? ? ? ? ? ? ? 1.325 ? 
covale9  covale both ? B CSO 263 C   ? ? ? 1_555 B ILE 264 N  ? ? A CSO 236 A ILE 237 1_555 ? ? ? ? ? ? ? 1.333 ? 
covale10 covale one  ? B ASN 288 ND2 ? ? ? 1_555 P NAG .   C1 ? ? A ASN 261 A NAG 605 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale11 covale one  ? B ASN 314 ND2 ? ? ? 1_555 Q NAG .   C1 ? ? A ASN 287 A NAG 606 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale12 covale one  ? B ASN 495 ND2 ? ? ? 1_555 R NAG .   C1 ? ? A ASN 468 A NAG 607 1_555 ? ? ? ? ? ? ? 1.467 ? 
covale13 covale both ? B GLU 508 C   ? ? ? 1_555 B CSO 509 N  ? ? A GLU 481 A CSO 482 1_555 ? ? ? ? ? ? ? 1.343 ? 
covale14 covale both ? B CSO 509 C   ? ? ? 1_555 B GLY 510 N  ? ? A CSO 482 A GLY 483 1_555 ? ? ? ? ? ? ? 1.329 ? 
covale15 covale one  ? B ASN 515 ND2 ? ? ? 1_555 S NAG .   C1 ? ? A ASN 488 A NAG 608 1_555 ? ? ? ? ? ? ? 1.446 ? 
metalc16 metalc ?    ? D MG  .   MG  ? ? ? 1_555 U HOH .   O  ? ? B MG  602 B HOH 706 1_555 ? ? ? ? ? ? ? 2.539 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 170 A . ? GLY 143 B ALA 171 A ? ALA 144 B 1 -10.16 
2 GLY 170 B . ? GLY 143 A ALA 171 B ? ALA 144 A 1 -12.12 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 8 ? 
AA4 ? 2 ? 
AA5 ? 6 ? 
AA6 ? 2 ? 
AA7 ? 8 ? 
AA8 ? 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      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? anti-parallel 
AA7 6 7 ? anti-parallel 
AA7 7 8 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 53  ? LYS A 55  ? ALA B 26  LYS B 28  
AA1 2 LEU A 120 ? ASP A 126 ? LEU B 93  ASP B 99  
AA1 3 ILE A 59  ? PHE A 65  ? ILE B 32  PHE B 38  
AA1 4 THR A 165 ? VAL A 169 ? THR B 138 VAL B 142 
AA1 5 GLN A 191 ? SER A 193 ? GLN B 164 SER B 166 
AA1 6 PHE A 210 ? ARG A 212 ? PHE B 183 ARG B 185 
AA2 1 HIS A 68  ? VAL A 71  ? HIS B 41  VAL B 44  
AA2 2 CYS A 87  ? TYR A 90  ? CYS B 60  TYR B 63  
AA3 1 CSO A 263 ? ILE A 270 ? CSO B 236 ILE B 243 
AA3 2 TRP A 235 ? ALA A 241 ? TRP B 208 ALA B 214 
AA3 3 VAL A 293 ? PHE A 297 ? VAL B 266 PHE B 270 
AA3 4 ILE A 319 ? ALA A 322 ? ILE B 292 ALA B 295 
AA3 5 ILE A 345 ? LEU A 349 ? ILE B 318 LEU B 322 
AA3 6 TYR A 516 ? LEU A 523 ? TYR B 489 LEU B 496 
AA3 7 ILE A 530 ? TYR A 538 ? ILE B 503 TYR B 511 
AA3 8 LEU A 548 ? ILE A 550 ? LEU B 521 ILE B 523 
AA4 1 PHE A 496 ? THR A 497 ? PHE B 469 THR B 470 
AA4 2 GLN A 503 ? VAL A 504 ? GLN B 476 VAL B 477 
AA5 1 ALA B 53  ? LYS B 55  ? ALA A 26  LYS A 28  
AA5 2 LEU B 120 ? ASP B 126 ? LEU A 93  ASP A 99  
AA5 3 ILE B 59  ? PHE B 65  ? ILE A 32  PHE A 38  
AA5 4 THR B 165 ? VAL B 169 ? THR A 138 VAL A 142 
AA5 5 GLN B 191 ? SER B 193 ? GLN A 164 SER A 166 
AA5 6 PHE B 210 ? ARG B 212 ? PHE A 183 ARG A 185 
AA6 1 HIS B 68  ? VAL B 71  ? HIS A 41  VAL A 44  
AA6 2 CYS B 87  ? TYR B 90  ? CYS A 60  TYR A 63  
AA7 1 CSO B 263 ? ILE B 270 ? CSO A 236 ILE A 243 
AA7 2 TRP B 235 ? ALA B 241 ? TRP A 208 ALA A 214 
AA7 3 VAL B 293 ? PHE B 297 ? VAL A 266 PHE A 270 
AA7 4 ILE B 319 ? ALA B 322 ? ILE A 292 ALA A 295 
AA7 5 ILE B 345 ? ALA B 348 ? ILE A 318 ALA A 321 
AA7 6 TYR B 516 ? LEU B 523 ? TYR A 489 LEU A 496 
AA7 7 ILE B 530 ? TYR B 538 ? ILE A 503 TYR A 511 
AA7 8 LEU B 548 ? ILE B 550 ? LEU A 521 ILE A 523 
AA8 1 ASN B 495 ? THR B 497 ? ASN A 468 THR A 470 
AA8 2 GLN B 503 ? THR B 505 ? GLN A 476 THR A 478 
# 
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 ALA A 53  ? N ALA B 26  O ILE A 124 ? O ILE B 97  
AA1 2 3 O GLY A 121 ? O GLY B 94  N ILE A 59  ? N ILE B 32  
AA1 3 4 N ILE A 60  ? N ILE B 33  O ILE A 166 ? O ILE B 139 
AA1 4 5 N VAL A 168 ? N VAL B 141 O VAL A 192 ? O VAL B 165 
AA1 5 6 N GLN A 191 ? N GLN B 164 O LEU A 211 ? O LEU B 184 
AA2 1 2 N GLY A 70  ? N GLY B 43  O ILE A 88  ? O ILE B 61  
AA3 1 2 O ASP A 265 ? O ASP B 238 N VAL A 236 ? N VAL B 209 
AA3 2 3 N GLY A 237 ? N GLY B 210 O VAL A 295 ? O VAL B 268 
AA3 3 4 N ILE A 294 ? N ILE B 267 O ILE A 319 ? O ILE B 292 
AA3 4 5 N ALA A 322 ? N ALA B 295 O ILE A 345 ? O ILE B 318 
AA3 5 6 N ALA A 348 ? N ALA B 321 O SER A 517 ? O SER B 490 
AA3 6 7 N ASN A 520 ? N ASN B 493 O LYS A 533 ? O LYS B 506 
AA3 7 8 N TYR A 537 ? N TYR B 510 O PHE A 549 ? O PHE B 522 
AA4 1 2 N PHE A 496 ? N PHE B 469 O VAL A 504 ? O VAL B 477 
AA5 1 2 N ALA B 53  ? N ALA A 26  O ILE B 124 ? O ILE A 97  
AA5 2 3 O GLY B 121 ? O GLY A 94  N ILE B 59  ? N ILE A 32  
AA5 3 4 N GLY B 62  ? N GLY A 35  O ALA B 167 ? O ALA A 140 
AA5 4 5 N VAL B 168 ? N VAL A 141 O VAL B 192 ? O VAL A 165 
AA5 5 6 N SER B 193 ? N SER A 166 O LEU B 211 ? O LEU A 184 
AA6 1 2 N GLY B 70  ? N GLY A 43  O ILE B 88  ? O ILE A 61  
AA7 1 2 O ASP B 265 ? O ASP A 238 N VAL B 236 ? N VAL A 209 
AA7 2 3 N GLY B 237 ? N GLY A 210 O VAL B 293 ? O VAL A 266 
AA7 3 4 N ILE B 294 ? N ILE A 267 O ILE B 319 ? O ILE A 292 
AA7 4 5 N ALA B 322 ? N ALA A 295 O ILE B 345 ? O ILE A 318 
AA7 5 6 N ALA B 348 ? N ALA A 321 O SER B 517 ? O SER A 490 
AA7 6 7 N ILE B 518 ? N ILE A 491 O VAL B 535 ? O VAL A 508 
AA7 7 8 N TYR B 537 ? N TYR A 510 O PHE B 549 ? O PHE A 522 
AA8 1 2 N PHE B 496 ? N PHE A 469 O VAL B 504 ? O VAL A 477 
# 
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 B GD3 601 ? 2  'binding site for residue GD3 B 601'                            
AC2 Software B MG  602 ? 2  'binding site for residue MG B 602'                             
AC3 Software B MG  603 ? 4  'binding site for residue MG B 603'                             
AC4 Software B BCT 604 ? 7  'binding site for residue BCT B 604'                            
AC5 Software B CL  605 ? 3  'binding site for residue CL B 605'                             
AC6 Software B TCR 609 ? 10 'binding site for residue TCR B 609'                            
AC7 Software A GD3 601 ? 2  'binding site for residue GD3 A 601'                            
AC8 Software A MG  602 ? 5  'binding site for residue MG A 602'                             
AC9 Software A BCT 603 ? 7  'binding site for residue BCT A 603'                            
AD1 Software A CL  604 ? 4  'binding site for residue CL A 604'                             
AD2 Software A TCR 609 ? 8  'binding site for residue TCR A 609'                            
AD3 Software A NAG 605 ? 2  'binding site for Mono-Saccharide NAG A 605 bound to ASN A 261' 
AD4 Software A NAG 606 ? 2  'binding site for Mono-Saccharide NAG A 606 bound to ASN A 287' 
AD5 Software A NAG 607 ? 2  'binding site for Mono-Saccharide NAG A 607 bound to ASN A 468' 
AD6 Software A NAG 608 ? 3  'binding site for Mono-Saccharide NAG A 608 bound to ASN A 488' 
AD7 Software B NAG 606 ? 3  'binding site for Mono-Saccharide NAG B 606 bound to ASN B 261' 
AD8 Software B NAG 607 ? 1  'binding site for Mono-Saccharide NAG B 607 bound to ASN B 287' 
AD9 Software B NAG 608 ? 3  'binding site for Mono-Saccharide NAG B 608 bound to ASN B 468' 
# 
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 2  GLU A 256 ? GLU B 229 . ? 1_555 ? 
2  AC1 2  GLU A 259 ? GLU B 232 . ? 1_555 ? 
3  AC2 2  SER A 267 ? SER B 240 . ? 1_555 ? 
4  AC2 2  HOH U .   ? HOH B 706 . ? 1_555 ? 
5  AC3 4  ILE A 108 ? ILE B 81  . ? 1_555 ? 
6  AC3 4  ASN A 109 ? ASN B 82  . ? 1_555 ? 
7  AC3 4  LEU A 114 ? LEU B 87  . ? 1_555 ? 
8  AC3 4  LEU A 115 ? LEU B 88  . ? 1_555 ? 
9  AC4 7  ARG A 93  ? ARG B 66  . ? 1_555 ? 
10 AC4 7  ARG A 96  ? ARG B 69  . ? 1_555 ? 
11 AC4 7  TRP A 97  ? TRP B 70  . ? 1_555 ? 
12 AC4 7  LEU A 441 ? LEU B 414 . ? 1_555 ? 
13 AC4 7  ARG A 442 ? ARG B 415 . ? 1_555 ? 
14 AC4 7  ILE A 443 ? ILE B 416 . ? 1_555 ? 
15 AC4 7  SER A 444 ? SER B 417 . ? 1_555 ? 
16 AC5 3  PRO A 66  ? PRO B 39  . ? 1_555 ? 
17 AC5 3  THR A 127 ? THR B 100 . ? 1_555 ? 
18 AC5 3  THR A 172 ? THR B 145 . ? 1_555 ? 
19 AC6 10 ARG A 93  ? ARG B 66  . ? 1_555 ? 
20 AC6 10 TRP A 97  ? TRP B 70  . ? 1_555 ? 
21 AC6 10 THR A 172 ? THR B 145 . ? 1_555 ? 
22 AC6 10 GLY A 173 ? GLY B 146 . ? 1_555 ? 
23 AC6 10 SER A 174 ? SER B 147 . ? 1_555 ? 
24 AC6 10 ALA A 195 ? ALA B 168 . ? 1_555 ? 
25 AC6 10 SER A 196 ? SER B 169 . ? 1_555 ? 
26 AC6 10 SER A 197 ? SER B 170 . ? 1_555 ? 
27 AC6 10 TYR A 245 ? TYR B 218 . ? 1_555 ? 
28 AC6 10 GLU A 324 ? GLU B 297 . ? 1_555 ? 
29 AC7 2  GLU B 256 ? GLU A 229 . ? 1_555 ? 
30 AC7 2  GLU B 259 ? GLU A 232 . ? 1_555 ? 
31 AC8 5  ILE B 108 ? ILE A 81  . ? 1_555 ? 
32 AC8 5  ASN B 109 ? ASN A 82  . ? 1_555 ? 
33 AC8 5  SER B 111 ? SER A 84  . ? 1_555 ? 
34 AC8 5  LEU B 114 ? LEU A 87  . ? 1_555 ? 
35 AC8 5  LEU B 115 ? LEU A 88  . ? 1_555 ? 
36 AC9 7  ARG B 93  ? ARG A 66  . ? 1_555 ? 
37 AC9 7  ARG B 96  ? ARG A 69  . ? 1_555 ? 
38 AC9 7  TRP B 97  ? TRP A 70  . ? 1_555 ? 
39 AC9 7  LEU B 441 ? LEU A 414 . ? 1_555 ? 
40 AC9 7  ARG B 442 ? ARG A 415 . ? 1_555 ? 
41 AC9 7  ILE B 443 ? ILE A 416 . ? 1_555 ? 
42 AC9 7  SER B 444 ? SER A 417 . ? 1_555 ? 
43 AD1 4  PRO B 66  ? PRO A 39  . ? 1_555 ? 
44 AD1 4  THR B 127 ? THR A 100 . ? 1_555 ? 
45 AD1 4  ALA B 171 ? ALA A 144 . ? 1_555 ? 
46 AD1 4  THR B 172 ? THR A 145 . ? 1_555 ? 
47 AD2 8  TRP B 97  ? TRP A 70  . ? 1_555 ? 
48 AD2 8  GLY B 173 ? GLY A 146 . ? 1_555 ? 
49 AD2 8  SER B 174 ? SER A 147 . ? 1_555 ? 
50 AD2 8  ALA B 195 ? ALA A 168 . ? 1_555 ? 
51 AD2 8  SER B 196 ? SER A 169 . ? 1_555 ? 
52 AD2 8  SER B 197 ? SER A 170 . ? 1_555 ? 
53 AD2 8  TYR B 245 ? TYR A 218 . ? 1_555 ? 
54 AD2 8  GLU B 324 ? GLU A 297 . ? 1_555 ? 
55 AD3 2  GLU B 284 ? GLU A 257 . ? 1_555 ? 
56 AD3 2  ASN B 288 ? ASN A 261 . ? 1_555 ? 
57 AD4 2  ASN B 314 ? ASN A 287 . ? 1_555 ? 
58 AD4 2  ARG B 419 ? ARG A 392 . ? 2_556 ? 
59 AD5 2  ASN B 495 ? ASN A 468 . ? 1_555 ? 
60 AD5 2  THR B 505 ? THR A 478 . ? 1_555 ? 
61 AD6 3  ASN B 515 ? ASN A 488 . ? 1_555 ? 
62 AD6 3  ASN B 539 ? ASN A 512 . ? 1_555 ? 
63 AD6 3  TYR B 541 ? TYR A 514 . ? 1_555 ? 
64 AD7 3  HIS A 281 ? HIS B 254 . ? 1_555 ? 
65 AD7 3  GLU A 284 ? GLU B 257 . ? 1_555 ? 
66 AD7 3  ASN A 288 ? ASN B 261 . ? 1_555 ? 
67 AD8 1  ASN A 314 ? ASN B 287 . ? 1_555 ? 
68 AD9 3  ASP A 460 ? ASP B 433 . ? 2_556 ? 
69 AD9 3  LEU A 470 ? LEU B 443 . ? 2_556 ? 
70 AD9 3  ASN A 495 ? ASN B 468 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5FBH 
_atom_sites.fract_transf_matrix[1][1]   0.005810 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001573 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012033 
_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]   0.010967 
_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  
CL 
GD 
MG 
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   . GLY A 1 48  ? -17.410 -22.050 8.456   1.00 90.33  ? 21  GLY B N   1 
ATOM   2    C  CA  . GLY A 1 48  ? -18.706 -22.679 8.884   1.00 96.68  ? 21  GLY B CA  1 
ATOM   3    C  C   . GLY A 1 48  ? -19.944 -22.187 8.126   1.00 96.25  ? 21  GLY B C   1 
ATOM   4    O  O   . GLY A 1 48  ? -19.913 -22.091 6.906   1.00 110.49 ? 21  GLY B O   1 
ATOM   5    N  N   . PRO A 1 49  ? -21.057 -21.913 8.843   1.00 91.97  ? 22  PRO B N   1 
ATOM   6    C  CA  . PRO A 1 49  ? -22.294 -21.355 8.258   1.00 94.21  ? 22  PRO B CA  1 
ATOM   7    C  C   . PRO A 1 49  ? -22.188 -19.961 7.621   1.00 94.92  ? 22  PRO B C   1 
ATOM   8    O  O   . PRO A 1 49  ? -21.302 -19.166 7.966   1.00 92.17  ? 22  PRO B O   1 
ATOM   9    C  CB  . PRO A 1 49  ? -23.250 -21.318 9.454   1.00 87.16  ? 22  PRO B CB  1 
ATOM   10   C  CG  . PRO A 1 49  ? -22.832 -22.482 10.267  1.00 88.37  ? 22  PRO B CG  1 
ATOM   11   C  CD  . PRO A 1 49  ? -21.330 -22.515 10.163  1.00 91.52  ? 22  PRO B CD  1 
ATOM   12   N  N   . ASP A 1 50  ? -23.120 -19.675 6.715   1.00 91.82  ? 23  ASP B N   1 
ATOM   13   C  CA  . ASP A 1 50  ? -23.056 -18.464 5.900   1.00 96.77  ? 23  ASP B CA  1 
ATOM   14   C  C   . ASP A 1 50  ? -23.404 -17.182 6.661   1.00 84.43  ? 23  ASP B C   1 
ATOM   15   O  O   . ASP A 1 50  ? -22.661 -16.206 6.590   1.00 86.73  ? 23  ASP B O   1 
ATOM   16   C  CB  . ASP A 1 50  ? -23.931 -18.620 4.645   1.00 106.13 ? 23  ASP B CB  1 
ATOM   17   C  CG  . ASP A 1 50  ? -23.294 -19.546 3.596   1.00 110.78 ? 23  ASP B CG  1 
ATOM   18   O  OD1 . ASP A 1 50  ? -22.048 -19.645 3.565   1.00 109.12 ? 23  ASP B OD1 1 
ATOM   19   O  OD2 . ASP A 1 50  ? -24.033 -20.167 2.797   1.00 107.71 ? 23  ASP B OD2 1 
ATOM   20   N  N   . GLN A 1 51  ? -24.519 -17.192 7.387   1.00 76.09  ? 24  GLN B N   1 
ATOM   21   C  CA  . GLN A 1 51  ? -24.957 -16.029 8.167   1.00 73.30  ? 24  GLN B CA  1 
ATOM   22   C  C   . GLN A 1 51  ? -24.303 -16.053 9.571   1.00 67.48  ? 24  GLN B C   1 
ATOM   23   O  O   . GLN A 1 51  ? -24.358 -17.064 10.264  1.00 71.12  ? 24  GLN B O   1 
ATOM   24   C  CB  . GLN A 1 51  ? -26.483 -16.041 8.269   1.00 77.42  ? 24  GLN B CB  1 
ATOM   25   C  CG  . GLN A 1 51  ? -27.138 -14.670 8.401   1.00 82.26  ? 24  GLN B CG  1 
ATOM   26   C  CD  . GLN A 1 51  ? -28.632 -14.762 8.750   1.00 87.16  ? 24  GLN B CD  1 
ATOM   27   O  OE1 . GLN A 1 51  ? -29.134 -15.823 9.156   1.00 81.64  ? 24  GLN B OE1 1 
ATOM   28   N  NE2 . GLN A 1 51  ? -29.345 -13.637 8.621   1.00 84.51  ? 24  GLN B NE2 1 
ATOM   29   N  N   . ARG A 1 52  ? -23.672 -14.953 9.976   1.00 57.52  ? 25  ARG B N   1 
ATOM   30   C  CA  . ARG A 1 52  ? -22.922 -14.915 11.209  1.00 57.24  ? 25  ARG B CA  1 
ATOM   31   C  C   . ARG A 1 52  ? -22.632 -13.514 11.698  1.00 54.44  ? 25  ARG B C   1 
ATOM   32   O  O   . ARG A 1 52  ? -22.989 -12.553 11.068  1.00 60.27  ? 25  ARG B O   1 
ATOM   33   C  CB  . ARG A 1 52  ? -21.610 -15.620 11.008  1.00 59.58  ? 25  ARG B CB  1 
ATOM   34   C  CG  . ARG A 1 52  ? -20.785 -14.980 9.931   1.00 67.38  ? 25  ARG B CG  1 
ATOM   35   C  CD  . ARG A 1 52  ? -19.447 -15.677 9.838   1.00 73.99  ? 25  ARG B CD  1 
ATOM   36   N  NE  . ARG A 1 52  ? -19.596 -17.065 9.412   1.00 78.85  ? 25  ARG B NE  1 
ATOM   37   C  CZ  . ARG A 1 52  ? -18.683 -18.016 9.604   1.00 83.92  ? 25  ARG B CZ  1 
ATOM   38   N  NH1 . ARG A 1 52  ? -17.528 -17.744 10.225  1.00 79.43  ? 25  ARG B NH1 1 
ATOM   39   N  NH2 . ARG A 1 52  ? -18.922 -19.254 9.173   1.00 83.06  ? 25  ARG B NH2 1 
ATOM   40   N  N   . ALA A 1 53  ? -22.031 -13.435 12.872  1.00 54.65  ? 26  ALA B N   1 
ATOM   41   C  CA  . ALA A 1 53  ? -21.464 -12.216 13.428  1.00 55.31  ? 26  ALA B CA  1 
ATOM   42   C  C   . ALA A 1 53  ? -20.095 -12.628 13.862  1.00 57.30  ? 26  ALA B C   1 
ATOM   43   O  O   . ALA A 1 53  ? -19.939 -13.620 14.562  1.00 57.93  ? 26  ALA B O   1 
ATOM   44   C  CB  . ALA A 1 53  ? -22.244 -11.692 14.626  1.00 53.13  ? 26  ALA B CB  1 
ATOM   45   N  N   . GLN A 1 54  ? -19.103 -11.864 13.437  1.00 64.98  ? 27  GLN B N   1 
ATOM   46   C  CA  . GLN A 1 54  ? -17.732 -12.301 13.520  1.00 67.18  ? 27  GLN B CA  1 
ATOM   47   C  C   . GLN A 1 54  ? -16.789 -11.116 13.492  1.00 68.16  ? 27  GLN B C   1 
ATOM   48   O  O   . GLN A 1 54  ? -16.968 -10.177 12.724  1.00 61.50  ? 27  GLN B O   1 
ATOM   49   C  CB  . GLN A 1 54  ? -17.429 -13.260 12.385  1.00 69.98  ? 27  GLN B CB  1 
ATOM   50   C  CG  . GLN A 1 54  ? -15.953 -13.481 12.162  1.00 80.07  ? 27  GLN B CG  1 
ATOM   51   C  CD  . GLN A 1 54  ? -15.653 -14.875 11.653  1.00 89.89  ? 27  GLN B CD  1 
ATOM   52   O  OE1 . GLN A 1 54  ? -16.539 -15.579 11.166  1.00 91.25  ? 27  GLN B OE1 1 
ATOM   53   N  NE2 . GLN A 1 54  ? -14.392 -15.291 11.774  1.00 96.80  ? 27  GLN B NE2 1 
ATOM   54   N  N   . LYS A 1 55  ? -15.806 -11.172 14.383  1.00 74.05  ? 28  LYS B N   1 
ATOM   55   C  CA  . LYS A 1 55  ? -14.790 -10.150 14.506  1.00 78.52  ? 28  LYS B CA  1 
ATOM   56   C  C   . LYS A 1 55  ? -13.516 -10.796 14.978  1.00 70.35  ? 28  LYS B C   1 
ATOM   57   O  O   . LYS A 1 55  ? -13.551 -11.582 15.907  1.00 66.58  ? 28  LYS B O   1 
ATOM   58   C  CB  . LYS A 1 55  ? -15.224 -9.094  15.500  1.00 83.07  ? 28  LYS B CB  1 
ATOM   59   C  CG  . LYS A 1 55  ? -14.186 -8.008  15.693  1.00 92.32  ? 28  LYS B CG  1 
ATOM   60   C  CD  . LYS A 1 55  ? -14.837 -6.739  16.211  1.00 102.15 ? 28  LYS B CD  1 
ATOM   61   C  CE  . LYS A 1 55  ? -13.814 -5.667  16.541  1.00 105.35 ? 28  LYS B CE  1 
ATOM   62   N  NZ  . LYS A 1 55  ? -14.509 -4.382  16.827  1.00 112.00 ? 28  LYS B NZ  1 
ATOM   63   N  N   . LYS A 1 56  ? -12.402 -10.467 14.325  1.00 70.60  ? 29  LYS B N   1 
ATOM   64   C  CA  . LYS A 1 56  ? -11.101 -11.023 14.669  1.00 66.83  ? 29  LYS B CA  1 
ATOM   65   C  C   . LYS A 1 56  ? -10.704 -10.519 16.059  1.00 67.17  ? 29  LYS B C   1 
ATOM   66   O  O   . LYS A 1 56  ? -11.124 -9.414  16.493  1.00 54.78  ? 29  LYS B O   1 
ATOM   67   C  CB  . LYS A 1 56  ? -10.035 -10.625 13.627  1.00 68.22  ? 29  LYS B CB  1 
ATOM   68   N  N   . GLY A 1 57  ? -9.929  -11.355 16.761  1.00 64.46  ? 30  GLY B N   1 
ATOM   69   C  CA  . GLY A 1 57  ? -9.321  -10.993 18.054  1.00 63.02  ? 30  GLY B CA  1 
ATOM   70   C  C   . GLY A 1 57  ? -8.202  -11.956 18.439  1.00 62.65  ? 30  GLY B C   1 
ATOM   71   O  O   . GLY A 1 57  ? -7.851  -12.872 17.677  1.00 52.96  ? 30  GLY B O   1 
ATOM   72   N  N   . ASP A 1 58  ? -7.631  -11.759 19.623  1.00 65.94  ? 31  ASP B N   1 
ATOM   73   C  CA  . ASP A 1 58  ? -6.578  -12.667 20.110  1.00 65.53  ? 31  ASP B CA  1 
ATOM   74   C  C   . ASP A 1 58  ? -7.163  -13.898 20.720  1.00 69.34  ? 31  ASP B C   1 
ATOM   75   O  O   . ASP A 1 58  ? -6.535  -14.947 20.684  1.00 74.87  ? 31  ASP B O   1 
ATOM   76   C  CB  . ASP A 1 58  ? -5.755  -12.005 21.187  1.00 69.67  ? 31  ASP B CB  1 
ATOM   77   C  CG  . ASP A 1 58  ? -5.123  -10.753 20.719  1.00 68.53  ? 31  ASP B CG  1 
ATOM   78   O  OD1 . ASP A 1 58  ? -4.332  -10.844 19.750  1.00 68.34  ? 31  ASP B OD1 1 
ATOM   79   O  OD2 . ASP A 1 58  ? -5.436  -9.700  21.315  1.00 67.88  ? 31  ASP B OD2 1 
ATOM   80   N  N   . ILE A 1 59  ? -8.335  -13.746 21.344  1.00 67.61  ? 32  ILE B N   1 
ATOM   81   C  CA  . ILE A 1 59  ? -9.069  -14.862 21.924  1.00 68.29  ? 32  ILE B CA  1 
ATOM   82   C  C   . ILE A 1 59  ? -10.510 -14.836 21.458  1.00 60.31  ? 32  ILE B C   1 
ATOM   83   O  O   . ILE A 1 59  ? -11.187 -13.828 21.614  1.00 57.95  ? 32  ILE B O   1 
ATOM   84   C  CB  . ILE A 1 59  ? -9.037  -14.792 23.456  1.00 72.95  ? 32  ILE B CB  1 
ATOM   85   C  CG1 . ILE A 1 59  ? -7.625  -15.088 23.952  1.00 79.99  ? 32  ILE B CG1 1 
ATOM   86   C  CG2 . ILE A 1 59  ? -9.983  -15.809 24.057  1.00 72.74  ? 32  ILE B CG2 1 
ATOM   87   C  CD1 . ILE A 1 59  ? -7.370  -14.598 25.354  1.00 81.96  ? 32  ILE B CD1 1 
ATOM   88   N  N   . ILE A 1 60  ? -10.989 -15.946 20.900  1.00 61.23  ? 33  ILE B N   1 
ATOM   89   C  CA  . ILE A 1 60  ? -12.356 -15.957 20.367  1.00 59.85  ? 33  ILE B CA  1 
ATOM   90   C  C   . ILE A 1 60  ? -13.358 -16.620 21.293  1.00 56.78  ? 33  ILE B C   1 
ATOM   91   O  O   . ILE A 1 60  ? -13.130 -17.744 21.802  1.00 50.96  ? 33  ILE B O   1 
ATOM   92   C  CB  . ILE A 1 60  ? -12.484 -16.652 18.987  1.00 62.80  ? 33  ILE B CB  1 
ATOM   93   C  CG1 . ILE A 1 60  ? -11.407 -16.163 18.008  1.00 59.53  ? 33  ILE B CG1 1 
ATOM   94   C  CG2 . ILE A 1 60  ? -13.882 -16.391 18.416  1.00 63.10  ? 33  ILE B CG2 1 
ATOM   95   C  CD1 . ILE A 1 60  ? -11.256 -14.656 18.011  1.00 59.07  ? 33  ILE B CD1 1 
ATOM   96   N  N   . LEU A 1 61  ? -14.475 -15.910 21.478  1.00 49.36  ? 34  LEU B N   1 
ATOM   97   C  CA  . LEU A 1 61  ? -15.654 -16.486 22.050  1.00 46.50  ? 34  LEU B CA  1 
ATOM   98   C  C   . LEU A 1 61  ? -16.670 -16.932 20.982  1.00 47.10  ? 34  LEU B C   1 
ATOM   99   O  O   . LEU A 1 61  ? -17.166 -16.112 20.249  1.00 43.82  ? 34  LEU B O   1 
ATOM   100  C  CB  . LEU A 1 61  ? -16.340 -15.477 22.928  1.00 45.16  ? 34  LEU B CB  1 
ATOM   101  C  CG  . LEU A 1 61  ? -15.599 -14.895 24.120  1.00 49.69  ? 34  LEU B CG  1 
ATOM   102  C  CD1 . LEU A 1 61  ? -16.586 -14.727 25.262  1.00 51.04  ? 34  LEU B CD1 1 
ATOM   103  C  CD2 . LEU A 1 61  ? -14.420 -15.705 24.595  1.00 55.92  ? 34  LEU B CD2 1 
ATOM   104  N  N   . GLY A 1 62  ? -17.015 -18.219 20.958  1.00 46.54  ? 35  GLY B N   1 
ATOM   105  C  CA  . GLY A 1 62  ? -18.229 -18.705 20.291  1.00 45.66  ? 35  GLY B CA  1 
ATOM   106  C  C   . GLY A 1 62  ? -19.513 -18.202 20.947  1.00 50.36  ? 35  GLY B C   1 
ATOM   107  O  O   . GLY A 1 62  ? -19.502 -17.737 22.100  1.00 50.76  ? 35  GLY B O   1 
ATOM   108  N  N   . GLY A 1 63  ? -20.603 -18.250 20.172  1.00 52.45  ? 36  GLY B N   1 
ATOM   109  C  CA  . GLY A 1 63  ? -21.959 -17.859 20.591  1.00 51.43  ? 36  GLY B CA  1 
ATOM   110  C  C   . GLY A 1 63  ? -23.029 -18.600 19.752  1.00 49.21  ? 36  GLY B C   1 
ATOM   111  O  O   . GLY A 1 63  ? -22.820 -18.901 18.571  1.00 44.85  ? 36  GLY B O   1 
ATOM   112  N  N   . LEU A 1 64  ? -24.158 -18.922 20.381  1.00 42.77  ? 37  LEU B N   1 
ATOM   113  C  CA  . LEU A 1 64  ? -25.286 -19.562 19.727  1.00 40.97  ? 37  LEU B CA  1 
ATOM   114  C  C   . LEU A 1 64  ? -26.541 -18.839 20.182  1.00 42.69  ? 37  LEU B C   1 
ATOM   115  O  O   . LEU A 1 64  ? -26.771 -18.700 21.376  1.00 39.00  ? 37  LEU B O   1 
ATOM   116  C  CB  . LEU A 1 64  ? -25.360 -21.027 20.101  1.00 38.25  ? 37  LEU B CB  1 
ATOM   117  C  CG  . LEU A 1 64  ? -24.154 -21.805 19.618  1.00 40.88  ? 37  LEU B CG  1 
ATOM   118  C  CD1 . LEU A 1 64  ? -24.207 -23.187 20.230  1.00 41.06  ? 37  LEU B CD1 1 
ATOM   119  C  CD2 . LEU A 1 64  ? -24.125 -21.883 18.087  1.00 42.53  ? 37  LEU B CD2 1 
ATOM   120  N  N   . PHE A 1 65  ? -27.335 -18.340 19.238  1.00 44.71  ? 38  PHE B N   1 
ATOM   121  C  CA  . PHE A 1 65  ? -28.574 -17.648 19.582  1.00 44.63  ? 38  PHE B CA  1 
ATOM   122  C  C   . PHE A 1 65  ? -29.682 -18.053 18.619  1.00 44.84  ? 38  PHE B C   1 
ATOM   123  O  O   . PHE A 1 65  ? -29.386 -18.446 17.491  1.00 40.57  ? 38  PHE B O   1 
ATOM   124  C  CB  . PHE A 1 65  ? -28.364 -16.146 19.551  1.00 45.18  ? 38  PHE B CB  1 
ATOM   125  C  CG  . PHE A 1 65  ? -27.400 -15.660 20.583  1.00 44.67  ? 38  PHE B CG  1 
ATOM   126  C  CD1 . PHE A 1 65  ? -26.036 -15.687 20.335  1.00 44.90  ? 38  PHE B CD1 1 
ATOM   127  C  CD2 . PHE A 1 65  ? -27.859 -15.194 21.810  1.00 44.10  ? 38  PHE B CD2 1 
ATOM   128  C  CE1 . PHE A 1 65  ? -25.141 -15.260 21.286  1.00 42.93  ? 38  PHE B CE1 1 
ATOM   129  C  CE2 . PHE A 1 65  ? -26.976 -14.763 22.774  1.00 42.83  ? 38  PHE B CE2 1 
ATOM   130  C  CZ  . PHE A 1 65  ? -25.612 -14.811 22.506  1.00 46.46  ? 38  PHE B CZ  1 
ATOM   131  N  N   . PRO A 1 66  ? -30.955 -17.997 19.072  1.00 46.35  ? 39  PRO B N   1 
ATOM   132  C  CA  . PRO A 1 66  ? -32.092 -18.363 18.226  1.00 44.05  ? 39  PRO B CA  1 
ATOM   133  C  C   . PRO A 1 66  ? -32.659 -17.123 17.571  1.00 47.91  ? 39  PRO B C   1 
ATOM   134  O  O   . PRO A 1 66  ? -33.671 -16.540 18.056  1.00 47.65  ? 39  PRO B O   1 
ATOM   135  C  CB  . PRO A 1 66  ? -33.081 -18.966 19.221  1.00 44.48  ? 39  PRO B CB  1 
ATOM   136  C  CG  . PRO A 1 66  ? -32.791 -18.260 20.517  1.00 42.66  ? 39  PRO B CG  1 
ATOM   137  C  CD  . PRO A 1 66  ? -31.388 -17.731 20.460  1.00 44.91  ? 39  PRO B CD  1 
ATOM   138  N  N   . ILE A 1 67  ? -31.989 -16.724 16.481  1.00 46.96  ? 40  ILE B N   1 
ATOM   139  C  CA  . ILE A 1 67  ? -32.389 -15.560 15.691  1.00 49.12  ? 40  ILE B CA  1 
ATOM   140  C  C   . ILE A 1 67  ? -33.682 -15.843 14.903  1.00 53.28  ? 40  ILE B C   1 
ATOM   141  O  O   . ILE A 1 67  ? -34.468 -14.927 14.650  1.00 56.45  ? 40  ILE B O   1 
ATOM   142  C  CB  . ILE A 1 67  ? -31.298 -15.131 14.716  1.00 48.98  ? 40  ILE B CB  1 
ATOM   143  C  CG1 . ILE A 1 67  ? -29.929 -15.020 15.414  1.00 50.61  ? 40  ILE B CG1 1 
ATOM   144  C  CG2 . ILE A 1 67  ? -31.682 -13.813 14.078  1.00 51.82  ? 40  ILE B CG2 1 
ATOM   145  C  CD1 . ILE A 1 67  ? -29.881 -14.170 16.671  1.00 47.49  ? 40  ILE B CD1 1 
ATOM   146  N  N   . HIS A 1 68  ? -33.899 -17.103 14.522  1.00 49.34  ? 41  HIS B N   1 
ATOM   147  C  CA  . HIS A 1 68  ? -35.209 -17.534 14.102  1.00 51.28  ? 41  HIS B CA  1 
ATOM   148  C  C   . HIS A 1 68  ? -35.832 -18.489 15.086  1.00 52.21  ? 41  HIS B C   1 
ATOM   149  O  O   . HIS A 1 68  ? -35.127 -19.153 15.814  1.00 49.34  ? 41  HIS B O   1 
ATOM   150  C  CB  . HIS A 1 68  ? -35.092 -18.176 12.754  1.00 55.24  ? 41  HIS B CB  1 
ATOM   151  C  CG  . HIS A 1 68  ? -34.663 -17.211 11.711  1.00 56.62  ? 41  HIS B CG  1 
ATOM   152  N  ND1 . HIS A 1 68  ? -33.338 -16.919 11.490  1.00 57.38  ? 41  HIS B ND1 1 
ATOM   153  C  CD2 . HIS A 1 68  ? -35.378 -16.407 10.888  1.00 51.46  ? 41  HIS B CD2 1 
ATOM   154  C  CE1 . HIS A 1 68  ? -33.249 -16.012 10.537  1.00 58.03  ? 41  HIS B CE1 1 
ATOM   155  N  NE2 . HIS A 1 68  ? -34.471 -15.684 10.157  1.00 57.92  ? 41  HIS B NE2 1 
ATOM   156  N  N   . PHE A 1 69  ? -37.163 -18.555 15.113  1.00 51.94  ? 42  PHE B N   1 
ATOM   157  C  CA  . PHE A 1 69  ? -37.842 -19.465 16.038  1.00 50.60  ? 42  PHE B CA  1 
ATOM   158  C  C   . PHE A 1 69  ? -37.871 -20.895 15.525  1.00 52.55  ? 42  PHE B C   1 
ATOM   159  O  O   . PHE A 1 69  ? -38.310 -21.787 16.219  1.00 57.28  ? 42  PHE B O   1 
ATOM   160  C  CB  . PHE A 1 69  ? -39.273 -19.039 16.264  1.00 48.47  ? 42  PHE B CB  1 
ATOM   161  C  CG  . PHE A 1 69  ? -39.445 -17.827 17.141  1.00 49.46  ? 42  PHE B CG  1 
ATOM   162  C  CD1 . PHE A 1 69  ? -39.170 -17.881 18.487  1.00 49.00  ? 42  PHE B CD1 1 
ATOM   163  C  CD2 . PHE A 1 69  ? -39.975 -16.661 16.630  1.00 52.84  ? 42  PHE B CD2 1 
ATOM   164  C  CE1 . PHE A 1 69  ? -39.355 -16.786 19.310  1.00 47.67  ? 42  PHE B CE1 1 
ATOM   165  C  CE2 . PHE A 1 69  ? -40.194 -15.566 17.450  1.00 56.67  ? 42  PHE B CE2 1 
ATOM   166  C  CZ  . PHE A 1 69  ? -39.886 -15.635 18.802  1.00 54.11  ? 42  PHE B CZ  1 
ATOM   167  N  N   . GLY A 1 70  ? -37.456 -21.135 14.294  1.00 55.67  ? 43  GLY B N   1 
ATOM   168  C  CA  . GLY A 1 70  ? -37.663 -22.461 13.730  1.00 57.41  ? 43  GLY B CA  1 
ATOM   169  C  C   . GLY A 1 70  ? -37.177 -22.670 12.318  1.00 54.32  ? 43  GLY B C   1 
ATOM   170  O  O   . GLY A 1 70  ? -36.806 -21.747 11.641  1.00 53.54  ? 43  GLY B O   1 
ATOM   171  N  N   . VAL A 1 71  ? -37.193 -23.912 11.879  1.00 63.74  ? 44  VAL B N   1 
ATOM   172  C  CA  . VAL A 1 71  ? -36.821 -24.235 10.522  1.00 71.99  ? 44  VAL B CA  1 
ATOM   173  C  C   . VAL A 1 71  ? -38.076 -24.437 9.672   1.00 78.10  ? 44  VAL B C   1 
ATOM   174  O  O   . VAL A 1 71  ? -39.141 -24.791 10.186  1.00 75.94  ? 44  VAL B O   1 
ATOM   175  C  CB  . VAL A 1 71  ? -35.920 -25.467 10.540  1.00 78.68  ? 44  VAL B CB  1 
ATOM   176  C  CG1 . VAL A 1 71  ? -35.924 -26.204 9.212   1.00 92.48  ? 44  VAL B CG1 1 
ATOM   177  C  CG2 . VAL A 1 71  ? -34.514 -25.030 10.905  1.00 81.22  ? 44  VAL B CG2 1 
ATOM   178  N  N   . ALA A 1 72  ? -37.944 -24.176 8.375   1.00 88.39  ? 45  ALA B N   1 
ATOM   179  C  CA  . ALA A 1 72  ? -39.009 -24.437 7.407   1.00 96.02  ? 45  ALA B CA  1 
ATOM   180  C  C   . ALA A 1 72  ? -39.206 -25.943 7.247   1.00 103.15 ? 45  ALA B C   1 
ATOM   181  O  O   . ALA A 1 72  ? -38.275 -26.652 6.841   1.00 99.96  ? 45  ALA B O   1 
ATOM   182  C  CB  . ALA A 1 72  ? -38.657 -23.808 6.073   1.00 95.58  ? 45  ALA B CB  1 
ATOM   183  N  N   . ALA A 1 73  ? -40.412 -26.425 7.558   1.00 116.80 ? 46  ALA B N   1 
ATOM   184  C  CA  . ALA A 1 73  ? -40.684 -27.870 7.629   1.00 129.79 ? 46  ALA B CA  1 
ATOM   185  C  C   . ALA A 1 73  ? -41.188 -28.451 6.302   1.00 127.66 ? 46  ALA B C   1 
ATOM   186  O  O   . ALA A 1 73  ? -42.249 -29.074 6.252   1.00 128.10 ? 46  ALA B O   1 
ATOM   187  C  CB  . ALA A 1 73  ? -41.664 -28.178 8.765   1.00 126.88 ? 46  ALA B CB  1 
ATOM   188  N  N   . LYS A 1 74  ? -40.417 -28.248 5.234   1.00 121.55 ? 47  LYS B N   1 
ATOM   189  C  CA  . LYS A 1 74  ? -40.620 -28.968 3.986   1.00 120.97 ? 47  LYS B CA  1 
ATOM   190  C  C   . LYS A 1 74  ? -40.051 -30.366 4.199   1.00 125.65 ? 47  LYS B C   1 
ATOM   191  O  O   . LYS A 1 74  ? -38.929 -30.653 3.763   1.00 131.77 ? 47  LYS B O   1 
ATOM   192  C  CB  . LYS A 1 74  ? -39.908 -28.259 2.828   1.00 117.49 ? 47  LYS B CB  1 
ATOM   193  N  N   . ASP A 1 75  ? -40.829 -31.220 4.879   1.00 125.84 ? 48  ASP B N   1 
ATOM   194  C  CA  . ASP A 1 75  ? -40.354 -32.531 5.369   1.00 124.59 ? 48  ASP B CA  1 
ATOM   195  C  C   . ASP A 1 75  ? -39.846 -33.405 4.223   1.00 121.64 ? 48  ASP B C   1 
ATOM   196  O  O   . ASP A 1 75  ? -40.604 -33.757 3.313   1.00 115.74 ? 48  ASP B O   1 
ATOM   197  C  CB  . ASP A 1 75  ? -41.451 -33.261 6.162   1.00 114.93 ? 48  ASP B CB  1 
ATOM   198  N  N   . GLN A 1 76  ? -38.553 -33.734 4.274   1.00 121.70 ? 49  GLN B N   1 
ATOM   199  C  CA  . GLN A 1 76  ? -37.869 -34.386 3.154   1.00 113.88 ? 49  GLN B CA  1 
ATOM   200  C  C   . GLN A 1 76  ? -38.267 -35.840 2.962   1.00 107.14 ? 49  GLN B C   1 
ATOM   201  O  O   . GLN A 1 76  ? -38.061 -36.703 3.819   1.00 90.84  ? 49  GLN B O   1 
ATOM   202  C  CB  . GLN A 1 76  ? -36.352 -34.277 3.287   1.00 110.95 ? 49  GLN B CB  1 
ATOM   203  C  CG  . GLN A 1 76  ? -35.803 -33.005 2.664   1.00 121.01 ? 49  GLN B CG  1 
ATOM   204  C  CD  . GLN A 1 76  ? -34.807 -32.297 3.551   1.00 119.75 ? 49  GLN B CD  1 
ATOM   205  O  OE1 . GLN A 1 76  ? -34.731 -32.560 4.760   1.00 113.07 ? 49  GLN B OE1 1 
ATOM   206  N  NE2 . GLN A 1 76  ? -34.042 -31.376 2.959   1.00 113.20 ? 49  GLN B NE2 1 
ATOM   207  N  N   . ASP A 1 77  ? -38.845 -36.088 1.799   1.00 100.51 ? 50  ASP B N   1 
ATOM   208  C  CA  . ASP A 1 77  ? -39.098 -37.427 1.344   1.00 89.09  ? 50  ASP B CA  1 
ATOM   209  C  C   . ASP A 1 77  ? -37.828 -37.989 0.683   1.00 79.47  ? 50  ASP B C   1 
ATOM   210  O  O   . ASP A 1 77  ? -37.805 -39.144 0.291   1.00 81.53  ? 50  ASP B O   1 
ATOM   211  C  CB  . ASP A 1 77  ? -40.314 -37.439 0.410   1.00 95.56  ? 50  ASP B CB  1 
ATOM   212  C  CG  . ASP A 1 77  ? -40.316 -36.275 -0.590  1.00 101.12 ? 50  ASP B CG  1 
ATOM   213  O  OD1 . ASP A 1 77  ? -39.242 -35.657 -0.814  1.00 104.87 ? 50  ASP B OD1 1 
ATOM   214  O  OD2 . ASP A 1 77  ? -41.399 -35.989 -1.154  1.00 96.12  ? 50  ASP B OD2 1 
ATOM   215  N  N   . LEU A 1 78  ? -36.773 -37.174 0.592   1.00 73.79  ? 51  LEU B N   1 
ATOM   216  C  CA  . LEU A 1 78  ? -35.444 -37.592 0.109   1.00 68.86  ? 51  LEU B CA  1 
ATOM   217  C  C   . LEU A 1 78  ? -35.500 -38.103 -1.289  1.00 76.08  ? 51  LEU B C   1 
ATOM   218  O  O   . LEU A 1 78  ? -34.794 -39.071 -1.606  1.00 75.69  ? 51  LEU B O   1 
ATOM   219  C  CB  . LEU A 1 78  ? -34.826 -38.697 0.955   1.00 65.63  ? 51  LEU B CB  1 
ATOM   220  C  CG  . LEU A 1 78  ? -34.432 -38.402 2.383   1.00 63.68  ? 51  LEU B CG  1 
ATOM   221  C  CD1 . LEU A 1 78  ? -33.974 -39.679 3.066   1.00 62.18  ? 51  LEU B CD1 1 
ATOM   222  C  CD2 . LEU A 1 78  ? -33.334 -37.359 2.390   1.00 64.74  ? 51  LEU B CD2 1 
ATOM   223  N  N   . LYS A 1 79  ? -36.342 -37.465 -2.109  1.00 83.22  ? 52  LYS B N   1 
ATOM   224  C  CA  . LYS A 1 79  ? -36.471 -37.806 -3.521  1.00 84.66  ? 52  LYS B CA  1 
ATOM   225  C  C   . LYS A 1 79  ? -35.282 -37.289 -4.328  1.00 84.79  ? 52  LYS B C   1 
ATOM   226  O  O   . LYS A 1 79  ? -34.872 -37.926 -5.282  1.00 79.47  ? 52  LYS B O   1 
ATOM   227  C  CB  . LYS A 1 79  ? -37.779 -37.271 -4.089  1.00 94.66  ? 52  LYS B CB  1 
ATOM   228  C  CG  . LYS A 1 79  ? -38.981 -38.166 -3.819  1.00 101.17 ? 52  LYS B CG  1 
ATOM   229  C  CD  . LYS A 1 79  ? -40.153 -37.809 -4.731  1.00 107.99 ? 52  LYS B CD  1 
ATOM   230  C  CE  . LYS A 1 79  ? -40.807 -39.045 -5.355  1.00 108.51 ? 52  LYS B CE  1 
ATOM   231  N  NZ  . LYS A 1 79  ? -41.557 -39.880 -4.371  1.00 101.37 ? 52  LYS B NZ  1 
ATOM   232  N  N   . SER A 1 80  ? -34.734 -36.136 -3.949  1.00 90.28  ? 53  SER B N   1 
ATOM   233  C  CA  . SER A 1 80  ? -33.455 -35.659 -4.511  1.00 96.82  ? 53  SER B CA  1 
ATOM   234  C  C   . SER A 1 80  ? -32.508 -35.414 -3.350  1.00 93.20  ? 53  SER B C   1 
ATOM   235  O  O   . SER A 1 80  ? -32.912 -35.619 -2.203  1.00 93.07  ? 53  SER B O   1 
ATOM   236  C  CB  . SER A 1 80  ? -33.648 -34.377 -5.322  1.00 97.98  ? 53  SER B CB  1 
ATOM   237  O  OG  . SER A 1 80  ? -34.052 -33.296 -4.501  1.00 90.92  ? 53  SER B OG  1 
ATOM   238  N  N   . ARG A 1 81  ? -31.265 -35.003 -3.620  1.00 90.13  ? 54  ARG B N   1 
ATOM   239  C  CA  . ARG A 1 81  ? -30.338 -34.651 -2.526  1.00 93.15  ? 54  ARG B CA  1 
ATOM   240  C  C   . ARG A 1 81  ? -30.979 -33.573 -1.642  1.00 93.13  ? 54  ARG B C   1 
ATOM   241  O  O   . ARG A 1 81  ? -31.549 -32.601 -2.162  1.00 87.24  ? 54  ARG B O   1 
ATOM   242  C  CB  . ARG A 1 81  ? -28.979 -34.166 -3.042  1.00 96.55  ? 54  ARG B CB  1 
ATOM   243  C  CG  . ARG A 1 81  ? -28.134 -33.417 -2.005  1.00 102.23 ? 54  ARG B CG  1 
ATOM   244  C  CD  . ARG A 1 81  ? -26.630 -33.650 -2.155  1.00 108.45 ? 54  ARG B CD  1 
ATOM   245  N  NE  . ARG A 1 81  ? -26.148 -33.481 -3.531  1.00 118.31 ? 54  ARG B NE  1 
ATOM   246  C  CZ  . ARG A 1 81  ? -25.948 -34.466 -4.414  1.00 120.02 ? 54  ARG B CZ  1 
ATOM   247  N  NH1 . ARG A 1 81  ? -26.183 -35.734 -4.102  1.00 117.94 ? 54  ARG B NH1 1 
ATOM   248  N  NH2 . ARG A 1 81  ? -25.509 -34.179 -5.633  1.00 126.86 ? 54  ARG B NH2 1 
ATOM   249  N  N   . PRO A 1 82  ? -30.936 -33.768 -0.307  1.00 91.52  ? 55  PRO B N   1 
ATOM   250  C  CA  . PRO A 1 82  ? -31.441 -32.710 0.569   1.00 89.50  ? 55  PRO B CA  1 
ATOM   251  C  C   . PRO A 1 82  ? -30.526 -31.481 0.554   1.00 80.32  ? 55  PRO B C   1 
ATOM   252  O  O   . PRO A 1 82  ? -29.333 -31.600 0.804   1.00 67.83  ? 55  PRO B O   1 
ATOM   253  C  CB  . PRO A 1 82  ? -31.481 -33.356 1.970   1.00 87.71  ? 55  PRO B CB  1 
ATOM   254  C  CG  . PRO A 1 82  ? -30.945 -34.732 1.839   1.00 86.69  ? 55  PRO B CG  1 
ATOM   255  C  CD  . PRO A 1 82  ? -30.507 -34.975 0.429   1.00 89.99  ? 55  PRO B CD  1 
ATOM   256  N  N   . GLU A 1 83  ? -31.090 -30.323 0.227   1.00 85.55  ? 56  GLU B N   1 
ATOM   257  C  CA  . GLU A 1 83  ? -30.419 -29.043 0.450   1.00 89.11  ? 56  GLU B CA  1 
ATOM   258  C  C   . GLU A 1 83  ? -30.458 -28.751 1.956   1.00 90.19  ? 56  GLU B C   1 
ATOM   259  O  O   . GLU A 1 83  ? -31.049 -29.500 2.736   1.00 87.41  ? 56  GLU B O   1 
ATOM   260  C  CB  . GLU A 1 83  ? -31.109 -27.923 -0.349  1.00 81.60  ? 56  GLU B CB  1 
ATOM   261  N  N   . SER A 1 84  ? -29.818 -27.672 2.371   1.00 94.06  ? 57  SER B N   1 
ATOM   262  C  CA  . SER A 1 84  ? -29.881 -27.251 3.765   1.00 98.76  ? 57  SER B CA  1 
ATOM   263  C  C   . SER A 1 84  ? -31.237 -26.580 4.047   1.00 101.37 ? 57  SER B C   1 
ATOM   264  O  O   . SER A 1 84  ? -31.746 -25.835 3.208   1.00 100.16 ? 57  SER B O   1 
ATOM   265  C  CB  . SER A 1 84  ? -28.750 -26.279 4.053   1.00 93.46  ? 57  SER B CB  1 
ATOM   266  O  OG  . SER A 1 84  ? -28.859 -25.186 3.173   1.00 89.30  ? 57  SER B OG  1 
ATOM   267  N  N   . VAL A 1 85  ? -31.820 -26.843 5.220   1.00 97.28  ? 58  VAL B N   1 
ATOM   268  C  CA  . VAL A 1 85  ? -33.112 -26.249 5.583   1.00 94.82  ? 58  VAL B CA  1 
ATOM   269  C  C   . VAL A 1 85  ? -33.013 -24.706 5.706   1.00 89.03  ? 58  VAL B C   1 
ATOM   270  O  O   . VAL A 1 85  ? -31.931 -24.146 5.866   1.00 78.04  ? 58  VAL B O   1 
ATOM   271  C  CB  . VAL A 1 85  ? -33.654 -26.870 6.889   1.00 88.75  ? 58  VAL B CB  1 
ATOM   272  N  N   . GLU A 1 86  ? -34.134 -24.014 5.594   1.00 82.14  ? 59  GLU B N   1 
ATOM   273  C  CA  . GLU A 1 86  ? -34.127 -22.569 5.705   1.00 78.79  ? 59  GLU B CA  1 
ATOM   274  C  C   . GLU A 1 86  ? -34.743 -22.225 7.033   1.00 76.22  ? 59  GLU B C   1 
ATOM   275  O  O   . GLU A 1 86  ? -35.678 -22.905 7.479   1.00 78.94  ? 59  GLU B O   1 
ATOM   276  C  CB  . GLU A 1 86  ? -34.948 -21.934 4.582   1.00 89.53  ? 59  GLU B CB  1 
ATOM   277  N  N   . CYS A 1 87  ? -34.247 -21.160 7.654   1.00 64.56  ? 60  CYS B N   1 
ATOM   278  C  CA  . CYS A 1 87  ? -34.762 -20.751 8.941   1.00 66.05  ? 60  CYS B CA  1 
ATOM   279  C  C   . CYS A 1 87  ? -35.876 -19.759 8.765   1.00 67.75  ? 60  CYS B C   1 
ATOM   280  O  O   . CYS A 1 87  ? -35.794 -18.873 7.915   1.00 67.08  ? 60  CYS B O   1 
ATOM   281  C  CB  . CYS A 1 87  ? -33.648 -20.199 9.821   1.00 73.36  ? 60  CYS B CB  1 
ATOM   282  S  SG  . CYS A 1 87  ? -32.599 -21.570 10.367  1.00 83.60  ? 60  CYS B SG  1 
ATOM   283  N  N   . ILE A 1 88  ? -36.907 -19.905 9.598   1.00 65.80  ? 61  ILE B N   1 
ATOM   284  C  CA  . ILE A 1 88  ? -38.156 -19.192 9.420   1.00 64.73  ? 61  ILE B CA  1 
ATOM   285  C  C   . ILE A 1 88  ? -38.696 -18.555 10.728  1.00 59.01  ? 61  ILE B C   1 
ATOM   286  O  O   . ILE A 1 88  ? -38.495 -19.088 11.811  1.00 57.74  ? 61  ILE B O   1 
ATOM   287  C  CB  . ILE A 1 88  ? -39.166 -20.137 8.718   1.00 73.79  ? 61  ILE B CB  1 
ATOM   288  C  CG1 . ILE A 1 88  ? -39.960 -19.354 7.686   1.00 83.29  ? 61  ILE B CG1 1 
ATOM   289  C  CG2 . ILE A 1 88  ? -40.063 -20.897 9.697   1.00 74.39  ? 61  ILE B CG2 1 
ATOM   290  C  CD1 . ILE A 1 88  ? -39.136 -18.961 6.462   1.00 94.56  ? 61  ILE B CD1 1 
ATOM   291  N  N   . ARG A 1 89  ? -39.339 -17.390 10.587  1.00 56.82  ? 62  ARG B N   1 
ATOM   292  C  CA  . ARG A 1 89  ? -39.906 -16.550 11.668  1.00 51.76  ? 62  ARG B CA  1 
ATOM   293  C  C   . ARG A 1 89  ? -38.888 -15.857 12.549  1.00 49.98  ? 62  ARG B C   1 
ATOM   294  O  O   . ARG A 1 89  ? -38.391 -16.426 13.529  1.00 49.18  ? 62  ARG B O   1 
ATOM   295  C  CB  . ARG A 1 89  ? -40.860 -17.325 12.555  1.00 60.32  ? 62  ARG B CB  1 
ATOM   296  C  CG  . ARG A 1 89  ? -41.863 -18.169 11.813  1.00 68.96  ? 62  ARG B CG  1 
ATOM   297  C  CD  . ARG A 1 89  ? -42.592 -19.066 12.784  1.00 73.21  ? 62  ARG B CD  1 
ATOM   298  N  NE  . ARG A 1 89  ? -43.680 -18.335 13.403  1.00 79.00  ? 62  ARG B NE  1 
ATOM   299  C  CZ  . ARG A 1 89  ? -44.276 -18.684 14.535  1.00 84.88  ? 62  ARG B CZ  1 
ATOM   300  N  NH1 . ARG A 1 89  ? -43.869 -19.757 15.213  1.00 85.26  ? 62  ARG B NH1 1 
ATOM   301  N  NH2 . ARG A 1 89  ? -45.288 -17.948 14.987  1.00 79.90  ? 62  ARG B NH2 1 
ATOM   302  N  N   . TYR A 1 90  ? -38.609 -14.604 12.236  1.00 51.71  ? 63  TYR B N   1 
ATOM   303  C  CA  . TYR A 1 90  ? -37.545 -13.880 12.935  1.00 51.94  ? 63  TYR B CA  1 
ATOM   304  C  C   . TYR A 1 90  ? -37.860 -13.772 14.431  1.00 54.58  ? 63  TYR B C   1 
ATOM   305  O  O   . TYR A 1 90  ? -39.013 -13.537 14.803  1.00 58.24  ? 63  TYR B O   1 
ATOM   306  C  CB  . TYR A 1 90  ? -37.335 -12.497 12.314  1.00 49.28  ? 63  TYR B CB  1 
ATOM   307  C  CG  . TYR A 1 90  ? -35.927 -11.951 12.487  1.00 51.55  ? 63  TYR B CG  1 
ATOM   308  C  CD1 . TYR A 1 90  ? -34.903 -12.372 11.675  1.00 49.29  ? 63  TYR B CD1 1 
ATOM   309  C  CD2 . TYR A 1 90  ? -35.639 -11.009 13.467  1.00 51.26  ? 63  TYR B CD2 1 
ATOM   310  C  CE1 . TYR A 1 90  ? -33.635 -11.868 11.828  1.00 55.61  ? 63  TYR B CE1 1 
ATOM   311  C  CE2 . TYR A 1 90  ? -34.370 -10.508 13.634  1.00 50.38  ? 63  TYR B CE2 1 
ATOM   312  C  CZ  . TYR A 1 90  ? -33.370 -10.940 12.817  1.00 55.29  ? 63  TYR B CZ  1 
ATOM   313  O  OH  . TYR A 1 90  ? -32.087 -10.459 12.981  1.00 62.37  ? 63  TYR B OH  1 
ATOM   314  N  N   . ASN A 1 91  ? -36.845 -13.993 15.272  1.00 51.11  ? 64  ASN B N   1 
ATOM   315  C  CA  . ASN A 1 91  ? -36.938 -13.773 16.728  1.00 52.99  ? 64  ASN B CA  1 
ATOM   316  C  C   . ASN A 1 91  ? -36.215 -12.477 17.167  1.00 56.61  ? 64  ASN B C   1 
ATOM   317  O  O   . ASN A 1 91  ? -35.016 -12.468 17.432  1.00 59.00  ? 64  ASN B O   1 
ATOM   318  C  CB  . ASN A 1 91  ? -36.343 -14.967 17.467  1.00 55.06  ? 64  ASN B CB  1 
ATOM   319  C  CG  . ASN A 1 91  ? -36.522 -14.898 18.988  1.00 54.11  ? 64  ASN B CG  1 
ATOM   320  O  OD1 . ASN A 1 91  ? -37.215 -14.043 19.535  1.00 47.84  ? 64  ASN B OD1 1 
ATOM   321  N  ND2 . ASN A 1 91  ? -35.882 -15.832 19.672  1.00 58.15  ? 64  ASN B ND2 1 
ATOM   322  N  N   . PHE A 1 92  ? -36.960 -11.383 17.247  1.00 60.24  ? 65  PHE B N   1 
ATOM   323  C  CA  . PHE A 1 92  ? -36.407 -10.094 17.651  1.00 57.04  ? 65  PHE B CA  1 
ATOM   324  C  C   . PHE A 1 92  ? -35.775 -10.084 19.034  1.00 51.54  ? 65  PHE B C   1 
ATOM   325  O  O   . PHE A 1 92  ? -34.748 -9.482  19.240  1.00 47.97  ? 65  PHE B O   1 
ATOM   326  C  CB  . PHE A 1 92  ? -37.501 -9.044  17.579  1.00 60.21  ? 65  PHE B CB  1 
ATOM   327  C  CG  . PHE A 1 92  ? -37.881 -8.699  16.177  1.00 63.17  ? 65  PHE B CG  1 
ATOM   328  C  CD1 . PHE A 1 92  ? -36.980 -7.992  15.366  1.00 57.92  ? 65  PHE B CD1 1 
ATOM   329  C  CD2 . PHE A 1 92  ? -39.111 -9.104  15.653  1.00 58.73  ? 65  PHE B CD2 1 
ATOM   330  C  CE1 . PHE A 1 92  ? -37.312 -7.690  14.063  1.00 62.50  ? 65  PHE B CE1 1 
ATOM   331  C  CE2 . PHE A 1 92  ? -39.448 -8.798  14.352  1.00 57.14  ? 65  PHE B CE2 1 
ATOM   332  C  CZ  . PHE A 1 92  ? -38.544 -8.095  13.553  1.00 63.01  ? 65  PHE B CZ  1 
ATOM   333  N  N   . ARG A 1 93  ? -36.391 -10.776 19.970  1.00 50.99  ? 66  ARG B N   1 
ATOM   334  C  CA  . ARG A 1 93  ? -35.834 -10.891 21.291  1.00 49.23  ? 66  ARG B CA  1 
ATOM   335  C  C   . ARG A 1 93  ? -34.497 -11.581 21.208  1.00 49.13  ? 66  ARG B C   1 
ATOM   336  O  O   . ARG A 1 93  ? -33.556 -11.189 21.878  1.00 55.60  ? 66  ARG B O   1 
ATOM   337  C  CB  . ARG A 1 93  ? -36.784 -11.675 22.186  1.00 50.99  ? 66  ARG B CB  1 
ATOM   338  C  CG  . ARG A 1 93  ? -36.489 -11.613 23.660  1.00 53.81  ? 66  ARG B CG  1 
ATOM   339  C  CD  . ARG A 1 93  ? -37.594 -12.350 24.380  1.00 59.18  ? 66  ARG B CD  1 
ATOM   340  N  NE  . ARG A 1 93  ? -37.360 -12.508 25.819  1.00 67.33  ? 66  ARG B NE  1 
ATOM   341  C  CZ  . ARG A 1 93  ? -37.952 -13.427 26.588  1.00 73.88  ? 66  ARG B CZ  1 
ATOM   342  N  NH1 . ARG A 1 93  ? -38.815 -14.300 26.076  1.00 75.79  ? 66  ARG B NH1 1 
ATOM   343  N  NH2 . ARG A 1 93  ? -37.670 -13.488 27.886  1.00 80.97  ? 66  ARG B NH2 1 
ATOM   344  N  N   . GLY A 1 94  ? -34.405 -12.603 20.373  1.00 45.55  ? 67  GLY B N   1 
ATOM   345  C  CA  . GLY A 1 94  ? -33.166 -13.369 20.242  1.00 43.25  ? 67  GLY B CA  1 
ATOM   346  C  C   . GLY A 1 94  ? -32.056 -12.550 19.629  1.00 42.96  ? 67  GLY B C   1 
ATOM   347  O  O   . GLY A 1 94  ? -30.898 -12.711 19.942  1.00 50.00  ? 67  GLY B O   1 
ATOM   348  N  N   . PHE A 1 95  ? -32.404 -11.640 18.758  1.00 45.55  ? 68  PHE B N   1 
ATOM   349  C  CA  . PHE A 1 95  ? -31.407 -10.748 18.211  1.00 47.00  ? 68  PHE B CA  1 
ATOM   350  C  C   . PHE A 1 95  ? -30.922 -9.761  19.296  1.00 42.74  ? 68  PHE B C   1 
ATOM   351  O  O   . PHE A 1 95  ? -29.743 -9.412  19.372  1.00 42.00  ? 68  PHE B O   1 
ATOM   352  C  CB  . PHE A 1 95  ? -31.997 -10.018 16.998  1.00 49.41  ? 68  PHE B CB  1 
ATOM   353  C  CG  . PHE A 1 95  ? -31.008 -9.154  16.293  1.00 47.57  ? 68  PHE B CG  1 
ATOM   354  C  CD1 . PHE A 1 95  ? -30.023 -9.716  15.517  1.00 46.25  ? 68  PHE B CD1 1 
ATOM   355  C  CD2 . PHE A 1 95  ? -31.049 -7.779  16.441  1.00 45.43  ? 68  PHE B CD2 1 
ATOM   356  C  CE1 . PHE A 1 95  ? -29.090 -8.914  14.876  1.00 48.85  ? 68  PHE B CE1 1 
ATOM   357  C  CE2 . PHE A 1 95  ? -30.131 -6.977  15.801  1.00 45.25  ? 68  PHE B CE2 1 
ATOM   358  C  CZ  . PHE A 1 95  ? -29.137 -7.548  15.025  1.00 46.67  ? 68  PHE B CZ  1 
ATOM   359  N  N   . ARG A 1 96  ? -31.834 -9.331  20.151  1.00 38.60  ? 69  ARG B N   1 
ATOM   360  C  CA  . ARG A 1 96  ? -31.440 -8.535  21.280  1.00 39.99  ? 69  ARG B CA  1 
ATOM   361  C  C   . ARG A 1 96  ? -30.497 -9.337  22.169  1.00 40.84  ? 69  ARG B C   1 
ATOM   362  O  O   . ARG A 1 96  ? -29.518 -8.828  22.637  1.00 42.84  ? 69  ARG B O   1 
ATOM   363  C  CB  . ARG A 1 96  ? -32.653 -8.031  22.061  1.00 41.78  ? 69  ARG B CB  1 
ATOM   364  C  CG  . ARG A 1 96  ? -32.240 -7.489  23.398  1.00 46.96  ? 69  ARG B CG  1 
ATOM   365  C  CD  . ARG A 1 96  ? -33.219 -6.514  23.977  1.00 46.59  ? 69  ARG B CD  1 
ATOM   366  N  NE  . ARG A 1 96  ? -34.573 -6.966  23.823  1.00 49.87  ? 69  ARG B NE  1 
ATOM   367  C  CZ  . ARG A 1 96  ? -35.229 -7.768  24.660  1.00 56.68  ? 69  ARG B CZ  1 
ATOM   368  N  NH1 . ARG A 1 96  ? -34.654 -8.278  25.737  1.00 59.68  ? 69  ARG B NH1 1 
ATOM   369  N  NH2 . ARG A 1 96  ? -36.498 -8.075  24.410  1.00 59.81  ? 69  ARG B NH2 1 
ATOM   370  N  N   . TRP A 1 97  ? -30.753 -10.617 22.378  1.00 44.46  ? 70  TRP B N   1 
ATOM   371  C  CA  . TRP A 1 97  ? -29.804 -11.407 23.162  1.00 42.47  ? 70  TRP B CA  1 
ATOM   372  C  C   . TRP A 1 97  ? -28.449 -11.425 22.509  1.00 42.83  ? 70  TRP B C   1 
ATOM   373  O  O   . TRP A 1 97  ? -27.446 -11.307 23.181  1.00 44.53  ? 70  TRP B O   1 
ATOM   374  C  CB  . TRP A 1 97  ? -30.293 -12.836 23.339  1.00 39.99  ? 70  TRP B CB  1 
ATOM   375  C  CG  . TRP A 1 97  ? -31.498 -12.886 24.071  1.00 38.95  ? 70  TRP B CG  1 
ATOM   376  C  CD1 . TRP A 1 97  ? -32.086 -11.854 24.770  1.00 38.28  ? 70  TRP B CD1 1 
ATOM   377  C  CD2 . TRP A 1 97  ? -32.327 -14.025 24.248  1.00 39.44  ? 70  TRP B CD2 1 
ATOM   378  N  NE1 . TRP A 1 97  ? -33.257 -12.283 25.309  1.00 40.68  ? 70  TRP B NE1 1 
ATOM   379  C  CE2 . TRP A 1 97  ? -33.427 -13.618 25.018  1.00 40.00  ? 70  TRP B CE2 1 
ATOM   380  C  CE3 . TRP A 1 97  ? -32.264 -15.345 23.800  1.00 40.53  ? 70  TRP B CE3 1 
ATOM   381  C  CZ2 . TRP A 1 97  ? -34.449 -14.492 25.369  1.00 38.56  ? 70  TRP B CZ2 1 
ATOM   382  C  CZ3 . TRP A 1 97  ? -33.261 -16.200 24.139  1.00 37.25  ? 70  TRP B CZ3 1 
ATOM   383  C  CH2 . TRP A 1 97  ? -34.352 -15.770 24.916  1.00 40.49  ? 70  TRP B CH2 1 
ATOM   384  N  N   . LEU A 1 98  ? -28.409 -11.599 21.199  1.00 42.38  ? 71  LEU B N   1 
ATOM   385  C  CA  . LEU A 1 98  ? -27.126 -11.667 20.540  1.00 46.00  ? 71  LEU B CA  1 
ATOM   386  C  C   . LEU A 1 98  ? -26.458 -10.308 20.693  1.00 46.48  ? 71  LEU B C   1 
ATOM   387  O  O   . LEU A 1 98  ? -25.244 -10.250 20.856  1.00 45.30  ? 71  LEU B O   1 
ATOM   388  C  CB  . LEU A 1 98  ? -27.254 -12.110 19.067  1.00 46.68  ? 71  LEU B CB  1 
ATOM   389  C  CG  . LEU A 1 98  ? -26.030 -11.923 18.162  1.00 49.71  ? 71  LEU B CG  1 
ATOM   390  C  CD1 . LEU A 1 98  ? -26.061 -12.806 16.927  1.00 49.63  ? 71  LEU B CD1 1 
ATOM   391  C  CD2 . LEU A 1 98  ? -25.948 -10.488 17.717  1.00 48.91  ? 71  LEU B CD2 1 
ATOM   392  N  N   . GLN A 1 99  ? -27.232 -9.219  20.673  1.00 45.68  ? 72  GLN B N   1 
ATOM   393  C  CA  . GLN A 1 99  ? -26.597 -7.897  20.766  1.00 51.68  ? 72  GLN B CA  1 
ATOM   394  C  C   . GLN A 1 99  ? -25.869 -7.728  22.072  1.00 54.29  ? 72  GLN B C   1 
ATOM   395  O  O   . GLN A 1 99  ? -24.751 -7.188  22.094  1.00 53.59  ? 72  GLN B O   1 
ATOM   396  C  CB  . GLN A 1 99  ? -27.578 -6.754  20.607  1.00 53.81  ? 72  GLN B CB  1 
ATOM   397  C  CG  . GLN A 1 99  ? -28.065 -6.553  19.193  1.00 57.49  ? 72  GLN B CG  1 
ATOM   398  C  CD  . GLN A 1 99  ? -27.094 -5.781  18.327  1.00 56.81  ? 72  GLN B CD  1 
ATOM   399  O  OE1 . GLN A 1 99  ? -27.441 -4.715  17.799  1.00 62.45  ? 72  GLN B OE1 1 
ATOM   400  N  NE2 . GLN A 1 99  ? -25.894 -6.321  18.143  1.00 49.30  ? 72  GLN B NE2 1 
ATOM   401  N  N   . ALA A 1 100 ? -26.504 -8.210  23.141  1.00 53.43  ? 73  ALA B N   1 
ATOM   402  C  CA  . ALA A 1 100 ? -25.941 -8.169  24.496  1.00 52.52  ? 73  ALA B CA  1 
ATOM   403  C  C   . ALA A 1 100 ? -24.586 -8.820  24.569  1.00 50.18  ? 73  ALA B C   1 
ATOM   404  O  O   . ALA A 1 100 ? -23.743 -8.348  25.297  1.00 49.93  ? 73  ALA B O   1 
ATOM   405  C  CB  . ALA A 1 100 ? -26.878 -8.817  25.504  1.00 55.16  ? 73  ALA B CB  1 
ATOM   406  N  N   . MET A 1 101 ? -24.361 -9.892  23.823  1.00 48.59  ? 74  MET B N   1 
ATOM   407  C  CA  . MET A 1 101 ? -23.040 -10.514 23.825  1.00 49.89  ? 74  MET B CA  1 
ATOM   408  C  C   . MET A 1 101 ? -22.002 -9.626  23.148  1.00 53.59  ? 74  MET B C   1 
ATOM   409  O  O   . MET A 1 101 ? -20.888 -9.472  23.643  1.00 60.04  ? 74  MET B O   1 
ATOM   410  C  CB  . MET A 1 101 ? -23.072 -11.849 23.101  1.00 48.89  ? 74  MET B CB  1 
ATOM   411  C  CG  . MET A 1 101 ? -21.698 -12.411 22.823  1.00 47.78  ? 74  MET B CG  1 
ATOM   412  S  SD  . MET A 1 101 ? -21.755 -14.177 22.532  1.00 43.31  ? 74  MET B SD  1 
ATOM   413  C  CE  . MET A 1 101 ? -20.034 -14.515 22.162  1.00 43.40  ? 74  MET B CE  1 
ATOM   414  N  N   . ILE A 1 102 ? -22.372 -9.071  22.002  1.00 53.30  ? 75  ILE B N   1 
ATOM   415  C  CA  . ILE A 1 102 ? -21.530 -8.100  21.299  1.00 55.64  ? 75  ILE B CA  1 
ATOM   416  C  C   . ILE A 1 102 ? -21.285 -6.821  22.138  1.00 55.68  ? 75  ILE B C   1 
ATOM   417  O  O   . ILE A 1 102 ? -20.181 -6.318  22.166  1.00 54.05  ? 75  ILE B O   1 
ATOM   418  C  CB  . ILE A 1 102 ? -22.142 -7.724  19.927  1.00 53.67  ? 75  ILE B CB  1 
ATOM   419  C  CG1 . ILE A 1 102 ? -22.127 -8.933  18.985  1.00 57.16  ? 75  ILE B CG1 1 
ATOM   420  C  CG2 . ILE A 1 102 ? -21.342 -6.632  19.277  1.00 52.65  ? 75  ILE B CG2 1 
ATOM   421  C  CD1 . ILE A 1 102 ? -23.015 -8.771  17.764  1.00 56.32  ? 75  ILE B CD1 1 
ATOM   422  N  N   . PHE A 1 103 ? -22.308 -6.306  22.813  1.00 52.87  ? 76  PHE B N   1 
ATOM   423  C  CA  . PHE A 1 103 ? -22.141 -5.160  23.683  1.00 53.91  ? 76  PHE B CA  1 
ATOM   424  C  C   . PHE A 1 103 ? -21.150 -5.380  24.787  1.00 54.97  ? 76  PHE B C   1 
ATOM   425  O  O   . PHE A 1 103 ? -20.329 -4.541  25.062  1.00 60.61  ? 76  PHE B O   1 
ATOM   426  C  CB  . PHE A 1 103 ? -23.437 -4.818  24.368  1.00 59.38  ? 76  PHE B CB  1 
ATOM   427  C  CG  . PHE A 1 103 ? -23.321 -3.653  25.287  1.00 59.78  ? 76  PHE B CG  1 
ATOM   428  C  CD1 . PHE A 1 103 ? -23.287 -2.371  24.775  1.00 59.26  ? 76  PHE B CD1 1 
ATOM   429  C  CD2 . PHE A 1 103 ? -23.225 -3.835  26.658  1.00 64.41  ? 76  PHE B CD2 1 
ATOM   430  C  CE1 . PHE A 1 103 ? -23.188 -1.277  25.621  1.00 68.94  ? 76  PHE B CE1 1 
ATOM   431  C  CE2 . PHE A 1 103 ? -23.116 -2.745  27.518  1.00 64.34  ? 76  PHE B CE2 1 
ATOM   432  C  CZ  . PHE A 1 103 ? -23.102 -1.462  27.000  1.00 68.29  ? 76  PHE B CZ  1 
ATOM   433  N  N   . ALA A 1 104 ? -21.270 -6.512  25.454  1.00 64.27  ? 77  ALA B N   1 
ATOM   434  C  CA  . ALA A 1 104 ? -20.347 -6.890  26.519  1.00 57.72  ? 77  ALA B CA  1 
ATOM   435  C  C   . ALA A 1 104 ? -18.937 -7.055  25.965  1.00 51.41  ? 77  ALA B C   1 
ATOM   436  O  O   . ALA A 1 104 ? -17.995 -6.608  26.570  1.00 55.07  ? 77  ALA B O   1 
ATOM   437  C  CB  . ALA A 1 104 ? -20.817 -8.173  27.185  1.00 55.55  ? 77  ALA B CB  1 
ATOM   438  N  N   . ILE A 1 105 ? -18.783 -7.681  24.815  1.00 50.07  ? 78  ILE B N   1 
ATOM   439  C  CA  . ILE A 1 105 ? -17.441 -7.886  24.292  1.00 56.57  ? 78  ILE B CA  1 
ATOM   440  C  C   . ILE A 1 105 ? -16.765 -6.559  23.908  1.00 65.45  ? 78  ILE B C   1 
ATOM   441  O  O   . ILE A 1 105 ? -15.526 -6.436  23.953  1.00 61.16  ? 78  ILE B O   1 
ATOM   442  C  CB  . ILE A 1 105 ? -17.433 -8.850  23.105  1.00 53.79  ? 78  ILE B CB  1 
ATOM   443  C  CG1 . ILE A 1 105 ? -17.618 -10.278 23.618  1.00 57.64  ? 78  ILE B CG1 1 
ATOM   444  C  CG2 . ILE A 1 105 ? -16.105 -8.781  22.376  1.00 55.99  ? 78  ILE B CG2 1 
ATOM   445  C  CD1 . ILE A 1 105 ? -17.939 -11.267 22.518  1.00 57.65  ? 78  ILE B CD1 1 
ATOM   446  N  N   . GLU A 1 106 ? -17.580 -5.573  23.540  1.00 68.01  ? 79  GLU B N   1 
ATOM   447  C  CA  . GLU A 1 106 ? -17.054 -4.315  23.075  1.00 67.11  ? 79  GLU B CA  1 
ATOM   448  C  C   . GLU A 1 106 ? -16.786 -3.466  24.289  1.00 62.61  ? 79  GLU B C   1 
ATOM   449  O  O   . GLU A 1 106 ? -15.720 -2.880  24.369  1.00 64.18  ? 79  GLU B O   1 
ATOM   450  C  CB  . GLU A 1 106 ? -17.952 -3.673  21.993  1.00 74.03  ? 79  GLU B CB  1 
ATOM   451  C  CG  . GLU A 1 106 ? -17.477 -4.095  20.583  1.00 86.62  ? 79  GLU B CG  1 
ATOM   452  C  CD  . GLU A 1 106 ? -18.522 -3.999  19.452  1.00 95.66  ? 79  GLU B CD  1 
ATOM   453  O  OE1 . GLU A 1 106 ? -19.264 -2.987  19.386  1.00 93.14  ? 79  GLU B OE1 1 
ATOM   454  O  OE2 . GLU A 1 106 ? -18.568 -4.932  18.591  1.00 89.94  ? 79  GLU B OE2 1 
ATOM   455  N  N   . GLU A 1 107 ? -17.710 -3.468  25.253  1.00 59.41  ? 80  GLU B N   1 
ATOM   456  C  CA  . GLU A 1 107 ? -17.483 -2.909  26.626  1.00 61.16  ? 80  GLU B CA  1 
ATOM   457  C  C   . GLU A 1 107 ? -16.186 -3.427  27.273  1.00 63.81  ? 80  GLU B C   1 
ATOM   458  O  O   . GLU A 1 107 ? -15.429 -2.678  27.912  1.00 61.03  ? 80  GLU B O   1 
ATOM   459  C  CB  . GLU A 1 107 ? -18.654 -3.241  27.579  1.00 58.10  ? 80  GLU B CB  1 
ATOM   460  C  CG  . GLU A 1 107 ? -18.641 -2.502  28.911  1.00 57.52  ? 80  GLU B CG  1 
ATOM   461  C  CD  . GLU A 1 107 ? -19.979 -2.576  29.671  1.00 65.81  ? 80  GLU B CD  1 
ATOM   462  O  OE1 . GLU A 1 107 ? -20.194 -3.556  30.410  1.00 69.86  ? 80  GLU B OE1 1 
ATOM   463  O  OE2 . GLU A 1 107 ? -20.824 -1.650  29.567  1.00 66.32  ? 80  GLU B OE2 1 
ATOM   464  N  N   . ILE A 1 108 ? -15.913 -4.706  27.087  1.00 65.55  ? 81  ILE B N   1 
ATOM   465  C  CA  . ILE A 1 108 ? -14.716 -5.265  27.652  1.00 67.59  ? 81  ILE B CA  1 
ATOM   466  C  C   . ILE A 1 108 ? -13.461 -4.857  26.897  1.00 67.10  ? 81  ILE B C   1 
ATOM   467  O  O   . ILE A 1 108 ? -12.428 -4.623  27.529  1.00 65.86  ? 81  ILE B O   1 
ATOM   468  C  CB  . ILE A 1 108 ? -14.838 -6.778  27.784  1.00 66.13  ? 81  ILE B CB  1 
ATOM   469  C  CG1 . ILE A 1 108 ? -15.861 -7.060  28.892  1.00 70.17  ? 81  ILE B CG1 1 
ATOM   470  C  CG2 . ILE A 1 108 ? -13.475 -7.402  28.097  1.00 61.45  ? 81  ILE B CG2 1 
ATOM   471  C  CD1 . ILE A 1 108 ? -16.417 -8.462  28.858  1.00 77.03  ? 81  ILE B CD1 1 
ATOM   472  N  N   . ASN A 1 109 ? -13.524 -4.761  25.571  1.00 63.30  ? 82  ASN B N   1 
ATOM   473  C  CA  . ASN A 1 109 ? -12.324 -4.361  24.831  1.00 65.65  ? 82  ASN B CA  1 
ATOM   474  C  C   . ASN A 1 109 ? -12.025 -2.866  25.052  1.00 69.57  ? 82  ASN B C   1 
ATOM   475  O  O   . ASN A 1 109 ? -10.882 -2.443  24.994  1.00 69.79  ? 82  ASN B O   1 
ATOM   476  C  CB  . ASN A 1 109 ? -12.405 -4.739  23.342  1.00 62.81  ? 82  ASN B CB  1 
ATOM   477  C  CG  . ASN A 1 109 ? -12.269 -6.244  23.106  1.00 63.49  ? 82  ASN B CG  1 
ATOM   478  O  OD1 . ASN A 1 109 ? -11.576 -6.960  23.854  1.00 68.09  ? 82  ASN B OD1 1 
ATOM   479  N  ND2 . ASN A 1 109 ? -12.928 -6.734  22.070  1.00 53.32  ? 82  ASN B ND2 1 
ATOM   480  N  N   . SER A 1 110 ? -13.054 -2.085  25.350  1.00 70.11  ? 83  SER B N   1 
ATOM   481  C  CA  . SER A 1 110 ? -12.876 -0.698  25.744  1.00 75.87  ? 83  SER B CA  1 
ATOM   482  C  C   . SER A 1 110 ? -12.250 -0.568  27.130  1.00 83.77  ? 83  SER B C   1 
ATOM   483  O  O   . SER A 1 110 ? -11.418 0.297   27.348  1.00 90.33  ? 83  SER B O   1 
ATOM   484  C  CB  . SER A 1 110 ? -14.220 0.026   25.739  1.00 77.61  ? 83  SER B CB  1 
ATOM   485  O  OG  . SER A 1 110 ? -14.801 -0.054  24.450  1.00 83.15  ? 83  SER B OG  1 
ATOM   486  N  N   . SER A 1 111 ? -12.649 -1.415  28.073  1.00 97.42  ? 84  SER B N   1 
ATOM   487  C  CA  . SER A 1 111 ? -12.123 -1.292  29.433  1.00 95.96  ? 84  SER B CA  1 
ATOM   488  C  C   . SER A 1 111 ? -10.620 -1.536  29.421  1.00 91.63  ? 84  SER B C   1 
ATOM   489  O  O   . SER A 1 111 ? -10.146 -2.571  28.931  1.00 86.66  ? 84  SER B O   1 
ATOM   490  C  CB  . SER A 1 111 ? -12.813 -2.232  30.430  1.00 99.08  ? 84  SER B CB  1 
ATOM   491  O  OG  . SER A 1 111 ? -12.662 -1.754  31.765  1.00 99.54  ? 84  SER B OG  1 
ATOM   492  N  N   . PRO A 1 112 ? -9.867  -0.559  29.938  1.00 95.95  ? 85  PRO B N   1 
ATOM   493  C  CA  . PRO A 1 112 ? -8.416  -0.685  29.997  1.00 95.46  ? 85  PRO B CA  1 
ATOM   494  C  C   . PRO A 1 112 ? -8.004  -1.651  31.115  1.00 87.34  ? 85  PRO B C   1 
ATOM   495  O  O   . PRO A 1 112 ? -7.116  -2.479  30.906  1.00 86.30  ? 85  PRO B O   1 
ATOM   496  C  CB  . PRO A 1 112 ? -7.955  0.751   30.264  1.00 103.31 ? 85  PRO B CB  1 
ATOM   497  C  CG  . PRO A 1 112 ? -9.115  1.422   30.956  1.00 101.27 ? 85  PRO B CG  1 
ATOM   498  C  CD  . PRO A 1 112 ? -10.360 0.675   30.592  1.00 96.20  ? 85  PRO B CD  1 
ATOM   499  N  N   . ALA A 1 113 ? -8.674  -1.536  32.269  1.00 84.04  ? 86  ALA B N   1 
ATOM   500  C  CA  . ALA A 1 113 ? -8.591  -2.474  33.405  1.00 85.55  ? 86  ALA B CA  1 
ATOM   501  C  C   . ALA A 1 113 ? -8.632  -3.969  33.033  1.00 87.63  ? 86  ALA B C   1 
ATOM   502  O  O   . ALA A 1 113 ? -7.658  -4.708  33.226  1.00 92.19  ? 86  ALA B O   1 
ATOM   503  C  CB  . ALA A 1 113 ? -9.726  -2.165  34.382  1.00 87.00  ? 86  ALA B CB  1 
ATOM   504  N  N   . LEU A 1 114 ? -9.765  -4.398  32.490  1.00 85.34  ? 87  LEU B N   1 
ATOM   505  C  CA  . LEU A 1 114 ? -9.975  -5.789  32.140  1.00 80.12  ? 87  LEU B CA  1 
ATOM   506  C  C   . LEU A 1 114 ? -9.233  -6.141  30.847  1.00 76.30  ? 87  LEU B C   1 
ATOM   507  O  O   . LEU A 1 114 ? -9.454  -5.519  29.810  1.00 78.68  ? 87  LEU B O   1 
ATOM   508  C  CB  . LEU A 1 114 ? -11.478 -6.041  32.005  1.00 79.84  ? 87  LEU B CB  1 
ATOM   509  C  CG  . LEU A 1 114 ? -11.935 -7.463  32.337  1.00 82.32  ? 87  LEU B CG  1 
ATOM   510  C  CD1 . LEU A 1 114 ? -11.695 -7.807  33.793  1.00 83.78  ? 87  LEU B CD1 1 
ATOM   511  C  CD2 . LEU A 1 114 ? -13.413 -7.596  32.029  1.00 86.49  ? 87  LEU B CD2 1 
ATOM   512  N  N   . LEU A 1 115 ? -8.331  -7.115  30.920  1.00 79.49  ? 88  LEU B N   1 
ATOM   513  C  CA  . LEU A 1 115 ? -7.557  -7.581  29.748  1.00 80.57  ? 88  LEU B CA  1 
ATOM   514  C  C   . LEU A 1 115 ? -6.985  -6.454  28.887  1.00 84.94  ? 88  LEU B C   1 
ATOM   515  O  O   . LEU A 1 115 ? -7.522  -6.136  27.826  1.00 94.83  ? 88  LEU B O   1 
ATOM   516  C  CB  . LEU A 1 115 ? -8.418  -8.501  28.889  1.00 79.54  ? 88  LEU B CB  1 
ATOM   517  C  CG  . LEU A 1 115 ? -8.896  -9.766  29.599  1.00 76.97  ? 88  LEU B CG  1 
ATOM   518  C  CD1 . LEU A 1 115 ? -9.945  -10.492 28.790  1.00 72.78  ? 88  LEU B CD1 1 
ATOM   519  C  CD2 . LEU A 1 115 ? -7.714  -10.684 29.889  1.00 86.51  ? 88  LEU B CD2 1 
ATOM   520  N  N   . PRO A 1 116 ? -5.897  -5.826  29.356  1.00 98.45  ? 89  PRO B N   1 
ATOM   521  C  CA  . PRO A 1 116 ? -5.315  -4.691  28.629  1.00 94.34  ? 89  PRO B CA  1 
ATOM   522  C  C   . PRO A 1 116 ? -4.512  -5.070  27.375  1.00 89.13  ? 89  PRO B C   1 
ATOM   523  O  O   . PRO A 1 116 ? -4.762  -4.527  26.307  1.00 92.73  ? 89  PRO B O   1 
ATOM   524  C  CB  . PRO A 1 116 ? -4.428  -4.012  29.680  1.00 97.06  ? 89  PRO B CB  1 
ATOM   525  C  CG  . PRO A 1 116 ? -4.203  -5.027  30.748  1.00 95.92  ? 89  PRO B CG  1 
ATOM   526  C  CD  . PRO A 1 116 ? -5.386  -5.934  30.737  1.00 98.82  ? 89  PRO B CD  1 
ATOM   527  N  N   . ASN A 1 117 ? -3.565  -5.988  27.480  1.00 90.57  ? 90  ASN B N   1 
ATOM   528  C  CA  . ASN A 1 117 ? -2.745  -6.319  26.312  1.00 95.57  ? 90  ASN B CA  1 
ATOM   529  C  C   . ASN A 1 117 ? -3.556  -6.852  25.115  1.00 100.11 ? 90  ASN B C   1 
ATOM   530  O  O   . ASN A 1 117 ? -3.200  -6.566  23.973  1.00 92.36  ? 90  ASN B O   1 
ATOM   531  C  CB  . ASN A 1 117 ? -1.649  -7.318  26.696  1.00 99.15  ? 90  ASN B CB  1 
ATOM   532  N  N   . LEU A 1 118 ? -4.653  -7.583  25.395  1.00 109.71 ? 91  LEU B N   1 
ATOM   533  C  CA  . LEU A 1 118 ? -5.423  -8.403  24.404  1.00 98.64  ? 91  LEU B CA  1 
ATOM   534  C  C   . LEU A 1 118 ? -6.795  -7.829  23.904  1.00 87.06  ? 91  LEU B C   1 
ATOM   535  O  O   . LEU A 1 118 ? -7.360  -6.880  24.500  1.00 76.45  ? 91  LEU B O   1 
ATOM   536  C  CB  . LEU A 1 118 ? -5.707  -9.788  25.018  1.00 105.06 ? 91  LEU B CB  1 
ATOM   537  C  CG  . LEU A 1 118 ? -4.586  -10.797 25.307  1.00 113.85 ? 91  LEU B CG  1 
ATOM   538  C  CD1 . LEU A 1 118 ? -4.319  -11.700 24.109  1.00 111.73 ? 91  LEU B CD1 1 
ATOM   539  C  CD2 . LEU A 1 118 ? -3.295  -10.130 25.768  1.00 119.43 ? 91  LEU B CD2 1 
ATOM   540  N  N   . THR A 1 119 ? -7.307  -8.423  22.809  1.00 72.35  ? 92  THR B N   1 
ATOM   541  C  CA  . THR A 1 119 ? -8.715  -8.254  22.360  1.00 76.54  ? 92  THR B CA  1 
ATOM   542  C  C   . THR A 1 119 ? -9.486  -9.586  22.304  1.00 74.97  ? 92  THR B C   1 
ATOM   543  O  O   . THR A 1 119 ? -8.953  -10.626 21.887  1.00 78.29  ? 92  THR B O   1 
ATOM   544  C  CB  . THR A 1 119 ? -8.844  -7.680  20.931  1.00 77.54  ? 92  THR B CB  1 
ATOM   545  O  OG1 . THR A 1 119 ? -8.203  -8.568  19.994  1.00 78.44  ? 92  THR B OG1 1 
ATOM   546  C  CG2 . THR A 1 119 ? -8.276  -6.291  20.845  1.00 73.62  ? 92  THR B CG2 1 
ATOM   547  N  N   . LEU A 1 120 ? -10.754 -9.536  22.686  1.00 65.82  ? 93  LEU B N   1 
ATOM   548  C  CA  . LEU A 1 120 ? -11.640 -10.680 22.525  1.00 64.78  ? 93  LEU B CA  1 
ATOM   549  C  C   . LEU A 1 120 ? -12.385 -10.554 21.215  1.00 60.05  ? 93  LEU B C   1 
ATOM   550  O  O   . LEU A 1 120 ? -13.001 -9.533  20.933  1.00 56.17  ? 93  LEU B O   1 
ATOM   551  C  CB  . LEU A 1 120 ? -12.683 -10.703 23.635  1.00 68.33  ? 93  LEU B CB  1 
ATOM   552  C  CG  . LEU A 1 120 ? -12.139 -10.823 25.041  1.00 71.78  ? 93  LEU B CG  1 
ATOM   553  C  CD1 . LEU A 1 120 ? -13.284 -10.753 26.035  1.00 72.06  ? 93  LEU B CD1 1 
ATOM   554  C  CD2 . LEU A 1 120 ? -11.349 -12.114 25.168  1.00 70.21  ? 93  LEU B CD2 1 
ATOM   555  N  N   . GLY A 1 121 ? -12.368 -11.605 20.430  1.00 58.66  ? 94  GLY B N   1 
ATOM   556  C  CA  . GLY A 1 121 ? -13.228 -11.672 19.266  1.00 62.74  ? 94  GLY B CA  1 
ATOM   557  C  C   . GLY A 1 121 ? -14.442 -12.561 19.501  1.00 71.26  ? 94  GLY B C   1 
ATOM   558  O  O   . GLY A 1 121 ? -14.720 -13.038 20.622  1.00 70.49  ? 94  GLY B O   1 
ATOM   559  N  N   . TYR A 1 122 ? -15.174 -12.798 18.425  1.00 67.61  ? 95  TYR B N   1 
ATOM   560  C  CA  . TYR A 1 122 ? -16.335 -13.617 18.527  1.00 59.83  ? 95  TYR B CA  1 
ATOM   561  C  C   . TYR A 1 122 ? -16.745 -14.290 17.216  1.00 57.53  ? 95  TYR B C   1 
ATOM   562  O  O   . TYR A 1 122 ? -16.510 -13.755 16.154  1.00 54.75  ? 95  TYR B O   1 
ATOM   563  C  CB  . TYR A 1 122 ? -17.463 -12.783 19.111  1.00 59.18  ? 95  TYR B CB  1 
ATOM   564  C  CG  . TYR A 1 122 ? -17.815 -11.493 18.412  1.00 60.22  ? 95  TYR B CG  1 
ATOM   565  C  CD1 . TYR A 1 122 ? -18.472 -11.490 17.180  1.00 62.50  ? 95  TYR B CD1 1 
ATOM   566  C  CD2 . TYR A 1 122 ? -17.567 -10.267 19.018  1.00 61.73  ? 95  TYR B CD2 1 
ATOM   567  C  CE1 . TYR A 1 122 ? -18.839 -10.298 16.559  1.00 59.36  ? 95  TYR B CE1 1 
ATOM   568  C  CE2 . TYR A 1 122 ? -17.935 -9.081  18.407  1.00 64.05  ? 95  TYR B CE2 1 
ATOM   569  C  CZ  . TYR A 1 122 ? -18.573 -9.106  17.179  1.00 60.24  ? 95  TYR B CZ  1 
ATOM   570  O  OH  . TYR A 1 122 ? -18.943 -7.932  16.597  1.00 62.67  ? 95  TYR B OH  1 
ATOM   571  N  N   . ARG A 1 123 ? -17.309 -15.493 17.316  1.00 55.99  ? 96  ARG B N   1 
ATOM   572  C  CA  . ARG A 1 123 ? -17.937 -16.160 16.190  1.00 61.39  ? 96  ARG B CA  1 
ATOM   573  C  C   . ARG A 1 123 ? -19.306 -16.627 16.636  1.00 58.92  ? 96  ARG B C   1 
ATOM   574  O  O   . ARG A 1 123 ? -19.410 -17.608 17.362  1.00 58.87  ? 96  ARG B O   1 
ATOM   575  C  CB  . ARG A 1 123 ? -17.106 -17.338 15.699  1.00 68.76  ? 96  ARG B CB  1 
ATOM   576  C  CG  . ARG A 1 123 ? -15.933 -16.932 14.810  1.00 85.93  ? 96  ARG B CG  1 
ATOM   577  C  CD  . ARG A 1 123 ? -14.819 -17.982 14.787  1.00 92.70  ? 96  ARG B CD  1 
ATOM   578  N  NE  . ARG A 1 123 ? -15.291 -19.291 14.305  1.00 105.34 ? 96  ARG B NE  1 
ATOM   579  C  CZ  . ARG A 1 123 ? -14.753 -20.481 14.617  1.00 112.83 ? 96  ARG B CZ  1 
ATOM   580  N  NH1 . ARG A 1 123 ? -13.700 -20.582 15.439  1.00 110.84 ? 96  ARG B NH1 1 
ATOM   581  N  NH2 . ARG A 1 123 ? -15.281 -21.595 14.105  1.00 105.80 ? 96  ARG B NH2 1 
ATOM   582  N  N   . ILE A 1 124 ? -20.351 -15.937 16.167  1.00 53.44  ? 97  ILE B N   1 
ATOM   583  C  CA  . ILE A 1 124 ? -21.702 -16.162 16.634  1.00 49.30  ? 97  ILE B CA  1 
ATOM   584  C  C   . ILE A 1 124 ? -22.631 -16.621 15.532  1.00 52.47  ? 97  ILE B C   1 
ATOM   585  O  O   . ILE A 1 124 ? -22.701 -15.988 14.478  1.00 54.32  ? 97  ILE B O   1 
ATOM   586  C  CB  . ILE A 1 124 ? -22.253 -14.881 17.259  1.00 48.09  ? 97  ILE B CB  1 
ATOM   587  C  CG1 . ILE A 1 124 ? -21.274 -14.402 18.354  1.00 45.45  ? 97  ILE B CG1 1 
ATOM   588  C  CG2 . ILE A 1 124 ? -23.642 -15.151 17.802  1.00 48.18  ? 97  ILE B CG2 1 
ATOM   589  C  CD1 . ILE A 1 124 ? -21.631 -13.122 19.043  1.00 44.21  ? 97  ILE B CD1 1 
ATOM   590  N  N   . PHE A 1 125 ? -23.367 -17.700 15.802  1.00 52.10  ? 98  PHE B N   1 
ATOM   591  C  CA  . PHE A 1 125 ? -24.290 -18.315 14.840  1.00 50.05  ? 98  PHE B CA  1 
ATOM   592  C  C   . PHE A 1 125 ? -25.724 -18.420 15.340  1.00 51.11  ? 98  PHE B C   1 
ATOM   593  O  O   . PHE A 1 125 ? -25.983 -18.427 16.535  1.00 56.77  ? 98  PHE B O   1 
ATOM   594  C  CB  . PHE A 1 125 ? -23.834 -19.726 14.509  1.00 51.04  ? 98  PHE B CB  1 
ATOM   595  C  CG  . PHE A 1 125 ? -22.455 -19.798 13.971  1.00 58.53  ? 98  PHE B CG  1 
ATOM   596  C  CD1 . PHE A 1 125 ? -22.210 -19.542 12.634  1.00 67.01  ? 98  PHE B CD1 1 
ATOM   597  C  CD2 . PHE A 1 125 ? -21.397 -20.137 14.789  1.00 66.47  ? 98  PHE B CD2 1 
ATOM   598  C  CE1 . PHE A 1 125 ? -20.926 -19.602 12.124  1.00 69.78  ? 98  PHE B CE1 1 
ATOM   599  C  CE2 . PHE A 1 125 ? -20.113 -20.230 14.280  1.00 69.61  ? 98  PHE B CE2 1 
ATOM   600  C  CZ  . PHE A 1 125 ? -19.877 -19.959 12.945  1.00 66.00  ? 98  PHE B CZ  1 
ATOM   601  N  N   . ASP A 1 126 ? -26.646 -18.547 14.387  1.00 58.57  ? 99  ASP B N   1 
ATOM   602  C  CA  . ASP A 1 126 ? -28.094 -18.755 14.620  1.00 55.46  ? 99  ASP B CA  1 
ATOM   603  C  C   . ASP A 1 126 ? -28.380 -20.273 14.715  1.00 50.30  ? 99  ASP B C   1 
ATOM   604  O  O   . ASP A 1 126 ? -27.939 -21.027 13.866  1.00 49.64  ? 99  ASP B O   1 
ATOM   605  C  CB  . ASP A 1 126 ? -28.871 -18.129 13.440  1.00 58.20  ? 99  ASP B CB  1 
ATOM   606  C  CG  . ASP A 1 126 ? -30.398 -18.238 13.569  1.00 60.26  ? 99  ASP B CG  1 
ATOM   607  O  OD1 . ASP A 1 126 ? -30.916 -18.575 14.650  1.00 63.96  ? 99  ASP B OD1 1 
ATOM   608  O  OD2 . ASP A 1 126 ? -31.093 -17.961 12.563  1.00 59.64  ? 99  ASP B OD2 1 
ATOM   609  N  N   . THR A 1 127 ? -29.107 -20.693 15.739  1.00 44.90  ? 100 THR B N   1 
ATOM   610  C  CA  . THR A 1 127 ? -29.452 -22.079 15.961  1.00 47.11  ? 100 THR B CA  1 
ATOM   611  C  C   . THR A 1 127 ? -30.813 -22.432 15.386  1.00 49.80  ? 100 THR B C   1 
ATOM   612  O  O   . THR A 1 127 ? -31.182 -23.632 15.296  1.00 49.55  ? 100 THR B O   1 
ATOM   613  C  CB  . THR A 1 127 ? -29.670 -22.328 17.450  1.00 47.48  ? 100 THR B CB  1 
ATOM   614  O  OG1 . THR A 1 127 ? -30.723 -21.450 17.921  1.00 43.85  ? 100 THR B OG1 1 
ATOM   615  C  CG2 . THR A 1 127 ? -28.416 -22.103 18.213  1.00 48.43  ? 100 THR B CG2 1 
ATOM   616  N  N   . CYS A 1 128 ? -31.602 -21.399 15.112  1.00 45.48  ? 101 CYS B N   1 
ATOM   617  C  CA  . CYS A 1 128 ? -33.024 -21.579 14.785  1.00 53.17  ? 101 CYS B CA  1 
ATOM   618  C  C   . CYS A 1 128 ? -33.800 -22.501 15.756  1.00 52.16  ? 101 CYS B C   1 
ATOM   619  O  O   . CYS A 1 128 ? -34.689 -23.234 15.340  1.00 54.24  ? 101 CYS B O   1 
ATOM   620  C  CB  . CYS A 1 128 ? -33.152 -22.080 13.342  1.00 61.48  ? 101 CYS B CB  1 
ATOM   621  S  SG  . CYS A 1 128 ? -32.063 -21.128 12.261  1.00 69.09  ? 101 CYS B SG  1 
ATOM   622  N  N   . ASN A 1 129 ? -33.505 -22.425 17.051  1.00 46.92  ? 102 ASN B N   1 
ATOM   623  C  CA  . ASN A 1 129 ? -34.017 -23.413 17.996  1.00 48.79  ? 102 ASN B CA  1 
ATOM   624  C  C   . ASN A 1 129 ? -33.921 -24.814 17.476  1.00 46.35  ? 102 ASN B C   1 
ATOM   625  O  O   . ASN A 1 129 ? -34.856 -25.557 17.640  1.00 50.51  ? 102 ASN B O   1 
ATOM   626  C  CB  . ASN A 1 129 ? -35.478 -23.185 18.346  1.00 47.69  ? 102 ASN B CB  1 
ATOM   627  C  CG  . ASN A 1 129 ? -35.681 -21.978 19.164  1.00 55.35  ? 102 ASN B CG  1 
ATOM   628  O  OD1 . ASN A 1 129 ? -35.030 -21.792 20.208  1.00 57.81  ? 102 ASN B OD1 1 
ATOM   629  N  ND2 . ASN A 1 129 ? -36.572 -21.105 18.697  1.00 62.55  ? 102 ASN B ND2 1 
ATOM   630  N  N   . THR A 1 130 ? -32.824 -25.172 16.825  1.00 49.69  ? 103 THR B N   1 
ATOM   631  C  CA  . THR A 1 130 ? -32.767 -26.455 16.151  1.00 52.48  ? 103 THR B CA  1 
ATOM   632  C  C   . THR A 1 130 ? -31.458 -27.094 16.489  1.00 50.26  ? 103 THR B C   1 
ATOM   633  O  O   . THR A 1 130 ? -30.419 -26.468 16.319  1.00 52.10  ? 103 THR B O   1 
ATOM   634  C  CB  . THR A 1 130 ? -32.972 -26.324 14.614  1.00 57.21  ? 103 THR B CB  1 
ATOM   635  O  OG1 . THR A 1 130 ? -34.293 -25.827 14.340  1.00 57.61  ? 103 THR B OG1 1 
ATOM   636  C  CG2 . THR A 1 130 ? -32.861 -27.681 13.928  1.00 58.59  ? 103 THR B CG2 1 
ATOM   637  N  N   . VAL A 1 131 ? -31.515 -28.332 16.993  1.00 44.49  ? 104 VAL B N   1 
ATOM   638  C  CA  . VAL A 1 131 ? -30.305 -29.101 17.203  1.00 42.07  ? 104 VAL B CA  1 
ATOM   639  C  C   . VAL A 1 131 ? -29.426 -29.109 15.954  1.00 45.55  ? 104 VAL B C   1 
ATOM   640  O  O   . VAL A 1 131 ? -28.209 -28.910 16.038  1.00 47.65  ? 104 VAL B O   1 
ATOM   641  C  CB  . VAL A 1 131 ? -30.597 -30.551 17.592  1.00 38.74  ? 104 VAL B CB  1 
ATOM   642  C  CG1 . VAL A 1 131 ? -29.332 -31.388 17.573  1.00 42.76  ? 104 VAL B CG1 1 
ATOM   643  C  CG2 . VAL A 1 131 ? -31.184 -30.619 18.965  1.00 37.62  ? 104 VAL B CG2 1 
ATOM   644  N  N   . SER A 1 132 ? -30.019 -29.364 14.796  1.00 47.79  ? 105 SER B N   1 
ATOM   645  C  CA  . SER A 1 132 ? -29.182 -29.555 13.610  1.00 48.46  ? 105 SER B CA  1 
ATOM   646  C  C   . SER A 1 132 ? -28.358 -28.301 13.271  1.00 51.72  ? 105 SER B C   1 
ATOM   647  O  O   . SER A 1 132 ? -27.127 -28.362 13.121  1.00 53.68  ? 105 SER B O   1 
ATOM   648  C  CB  . SER A 1 132 ? -29.992 -30.070 12.441  1.00 42.21  ? 105 SER B CB  1 
ATOM   649  O  OG  . SER A 1 132 ? -30.910 -29.100 11.982  1.00 48.88  ? 105 SER B OG  1 
ATOM   650  N  N   . LYS A 1 133 ? -28.999 -27.152 13.208  1.00 54.63  ? 106 LYS B N   1 
ATOM   651  C  CA  . LYS A 1 133 ? -28.242 -25.918 12.921  1.00 57.80  ? 106 LYS B CA  1 
ATOM   652  C  C   . LYS A 1 133 ? -27.188 -25.662 13.997  1.00 50.30  ? 106 LYS B C   1 
ATOM   653  O  O   . LYS A 1 133 ? -26.089 -25.242 13.706  1.00 53.89  ? 106 LYS B O   1 
ATOM   654  C  CB  . LYS A 1 133 ? -29.177 -24.724 12.854  1.00 61.15  ? 106 LYS B CB  1 
ATOM   655  C  CG  . LYS A 1 133 ? -30.300 -24.885 11.850  1.00 67.36  ? 106 LYS B CG  1 
ATOM   656  C  CD  . LYS A 1 133 ? -29.814 -24.622 10.435  1.00 71.90  ? 106 LYS B CD  1 
ATOM   657  C  CE  . LYS A 1 133 ? -30.958 -24.809 9.448   1.00 76.80  ? 106 LYS B CE  1 
ATOM   658  N  NZ  . LYS A 1 133 ? -30.532 -24.645 8.037   1.00 79.91  ? 106 LYS B NZ  1 
ATOM   659  N  N   . ALA A 1 134 ? -27.539 -25.926 15.245  1.00 46.14  ? 107 ALA B N   1 
ATOM   660  C  CA  . ALA A 1 134 ? -26.647 -25.676 16.348  1.00 45.04  ? 107 ALA B CA  1 
ATOM   661  C  C   . ALA A 1 134 ? -25.452 -26.593 16.256  1.00 47.27  ? 107 ALA B C   1 
ATOM   662  O  O   . ALA A 1 134 ? -24.338 -26.164 16.519  1.00 51.78  ? 107 ALA B O   1 
ATOM   663  C  CB  . ALA A 1 134 ? -27.363 -25.877 17.663  1.00 46.28  ? 107 ALA B CB  1 
ATOM   664  N  N   . LEU A 1 135 ? -25.672 -27.848 15.880  1.00 46.68  ? 108 LEU B N   1 
ATOM   665  C  CA  . LEU A 1 135 ? -24.557 -28.767 15.670  1.00 51.42  ? 108 LEU B CA  1 
ATOM   666  C  C   . LEU A 1 135 ? -23.632 -28.414 14.488  1.00 50.02  ? 108 LEU B C   1 
ATOM   667  O  O   . LEU A 1 135 ? -22.434 -28.651 14.567  1.00 46.26  ? 108 LEU B O   1 
ATOM   668  C  CB  . LEU A 1 135 ? -25.054 -30.198 15.500  1.00 52.63  ? 108 LEU B CB  1 
ATOM   669  C  CG  . LEU A 1 135 ? -25.450 -30.956 16.749  1.00 52.83  ? 108 LEU B CG  1 
ATOM   670  C  CD1 . LEU A 1 135 ? -25.491 -32.422 16.407  1.00 51.75  ? 108 LEU B CD1 1 
ATOM   671  C  CD2 . LEU A 1 135 ? -24.470 -30.769 17.891  1.00 61.62  ? 108 LEU B CD2 1 
ATOM   672  N  N   . GLU A 1 136 ? -24.173 -27.888 13.387  1.00 57.92  ? 109 GLU B N   1 
ATOM   673  C  CA  . GLU A 1 136 ? -23.303 -27.454 12.275  1.00 60.84  ? 109 GLU B CA  1 
ATOM   674  C  C   . GLU A 1 136 ? -22.348 -26.441 12.877  1.00 59.82  ? 109 GLU B C   1 
ATOM   675  O  O   . GLU A 1 136 ? -21.150 -26.591 12.759  1.00 56.26  ? 109 GLU B O   1 
ATOM   676  C  CB  . GLU A 1 136 ? -24.059 -26.769 11.128  1.00 65.84  ? 109 GLU B CB  1 
ATOM   677  C  CG  . GLU A 1 136 ? -24.637 -27.652 10.036  1.00 77.40  ? 109 GLU B CG  1 
ATOM   678  C  CD  . GLU A 1 136 ? -25.526 -26.864 9.055   1.00 93.38  ? 109 GLU B CD  1 
ATOM   679  O  OE1 . GLU A 1 136 ? -25.597 -25.609 9.142   1.00 101.59 ? 109 GLU B OE1 1 
ATOM   680  O  OE2 . GLU A 1 136 ? -26.174 -27.495 8.188   1.00 100.90 ? 109 GLU B OE2 1 
ATOM   681  N  N   . ALA A 1 137 ? -22.902 -25.429 13.550  1.00 54.71  ? 110 ALA B N   1 
ATOM   682  C  CA  . ALA A 1 137 ? -22.115 -24.327 14.049  1.00 50.30  ? 110 ALA B CA  1 
ATOM   683  C  C   . ALA A 1 137 ? -21.076 -24.843 15.041  1.00 49.83  ? 110 ALA B C   1 
ATOM   684  O  O   . ALA A 1 137 ? -19.952 -24.405 15.106  1.00 51.04  ? 110 ALA B O   1 
ATOM   685  C  CB  . ALA A 1 137 ? -23.021 -23.312 14.693  1.00 49.57  ? 110 ALA B CB  1 
ATOM   686  N  N   . THR A 1 138 ? -21.443 -25.835 15.793  1.00 51.27  ? 111 THR B N   1 
ATOM   687  C  CA  . THR A 1 138 ? -20.559 -26.297 16.811  1.00 55.24  ? 111 THR B CA  1 
ATOM   688  C  C   . THR A 1 138 ? -19.401 -27.061 16.186  1.00 54.03  ? 111 THR B C   1 
ATOM   689  O  O   . THR A 1 138 ? -18.264 -27.008 16.681  1.00 56.90  ? 111 THR B O   1 
ATOM   690  C  CB  . THR A 1 138 ? -21.337 -27.156 17.823  1.00 54.12  ? 111 THR B CB  1 
ATOM   691  O  OG1 . THR A 1 138 ? -22.234 -26.307 18.542  1.00 49.13  ? 111 THR B OG1 1 
ATOM   692  C  CG2 . THR A 1 138 ? -20.405 -27.816 18.793  1.00 57.38  ? 111 THR B CG2 1 
ATOM   693  N  N   . LEU A 1 139 ? -19.680 -27.793 15.122  1.00 52.22  ? 112 LEU B N   1 
ATOM   694  C  CA  . LEU A 1 139 ? -18.604 -28.501 14.420  1.00 57.52  ? 112 LEU B CA  1 
ATOM   695  C  C   . LEU A 1 139 ? -17.507 -27.527 13.941  1.00 55.79  ? 112 LEU B C   1 
ATOM   696  O  O   . LEU A 1 139 ? -16.338 -27.868 13.922  1.00 52.70  ? 112 LEU B O   1 
ATOM   697  C  CB  . LEU A 1 139 ? -19.166 -29.298 13.246  1.00 58.10  ? 112 LEU B CB  1 
ATOM   698  C  CG  . LEU A 1 139 ? -19.888 -30.577 13.650  1.00 57.48  ? 112 LEU B CG  1 
ATOM   699  C  CD1 . LEU A 1 139 ? -20.615 -31.100 12.447  1.00 59.13  ? 112 LEU B CD1 1 
ATOM   700  C  CD2 . LEU A 1 139 ? -18.930 -31.642 14.138  1.00 57.61  ? 112 LEU B CD2 1 
ATOM   701  N  N   . SER A 1 140 ? -17.903 -26.307 13.599  1.00 55.16  ? 113 SER B N   1 
ATOM   702  C  CA  . SER A 1 140 ? -16.964 -25.288 13.222  1.00 57.70  ? 113 SER B CA  1 
ATOM   703  C  C   . SER A 1 140 ? -16.215 -24.755 14.436  1.00 54.96  ? 113 SER B C   1 
ATOM   704  O  O   . SER A 1 140 ? -15.050 -24.453 14.338  1.00 67.74  ? 113 SER B O   1 
ATOM   705  C  CB  . SER A 1 140 ? -17.670 -24.151 12.457  1.00 58.88  ? 113 SER B CB  1 
ATOM   706  O  OG  . SER A 1 140 ? -18.000 -23.077 13.316  1.00 58.54  ? 113 SER B OG  1 
ATOM   707  N  N   . PHE A 1 141 ? -16.875 -24.603 15.575  1.00 55.85  ? 114 PHE B N   1 
ATOM   708  C  CA  . PHE A 1 141 ? -16.196 -24.135 16.795  1.00 52.38  ? 114 PHE B CA  1 
ATOM   709  C  C   . PHE A 1 141 ? -15.054 -25.048 17.206  1.00 56.11  ? 114 PHE B C   1 
ATOM   710  O  O   . PHE A 1 141 ? -14.053 -24.573 17.714  1.00 71.50  ? 114 PHE B O   1 
ATOM   711  C  CB  . PHE A 1 141 ? -17.148 -24.133 17.999  1.00 53.81  ? 114 PHE B CB  1 
ATOM   712  C  CG  . PHE A 1 141 ? -18.142 -23.031 18.022  1.00 46.94  ? 114 PHE B CG  1 
ATOM   713  C  CD1 . PHE A 1 141 ? -17.890 -21.805 17.438  1.00 48.17  ? 114 PHE B CD1 1 
ATOM   714  C  CD2 . PHE A 1 141 ? -19.336 -23.231 18.683  1.00 48.81  ? 114 PHE B CD2 1 
ATOM   715  C  CE1 . PHE A 1 141 ? -18.827 -20.786 17.498  1.00 53.66  ? 114 PHE B CE1 1 
ATOM   716  C  CE2 . PHE A 1 141 ? -20.296 -22.234 18.746  1.00 52.63  ? 114 PHE B CE2 1 
ATOM   717  C  CZ  . PHE A 1 141 ? -20.035 -21.000 18.152  1.00 57.05  ? 114 PHE B CZ  1 
ATOM   718  N  N   . VAL A 1 142 ? -15.241 -26.356 17.035  1.00 59.04  ? 115 VAL B N   1 
ATOM   719  C  CA  . VAL A 1 142 ? -14.254 -27.362 17.406  1.00 60.37  ? 115 VAL B CA  1 
ATOM   720  C  C   . VAL A 1 142 ? -13.447 -27.881 16.214  1.00 61.78  ? 115 VAL B C   1 
ATOM   721  O  O   . VAL A 1 142 ? -12.930 -28.993 16.271  1.00 64.77  ? 115 VAL B O   1 
ATOM   722  C  CB  . VAL A 1 142 ? -14.902 -28.598 18.102  1.00 61.54  ? 115 VAL B CB  1 
ATOM   723  C  CG1 . VAL A 1 142 ? -15.699 -28.174 19.319  1.00 69.96  ? 115 VAL B CG1 1 
ATOM   724  C  CG2 . VAL A 1 142 ? -15.783 -29.390 17.163  1.00 58.40  ? 115 VAL B CG2 1 
ATOM   725  N  N   . ALA A 1 143 ? -13.311 -27.098 15.148  1.00 63.55  ? 116 ALA B N   1 
ATOM   726  C  CA  . ALA A 1 143 ? -12.726 -27.627 13.904  1.00 66.12  ? 116 ALA B CA  1 
ATOM   727  C  C   . ALA A 1 143 ? -11.252 -27.942 14.086  1.00 66.56  ? 116 ALA B C   1 
ATOM   728  O  O   . ALA A 1 143 ? -10.758 -28.947 13.580  1.00 57.21  ? 116 ALA B O   1 
ATOM   729  C  CB  . ALA A 1 143 ? -12.937 -26.656 12.752  1.00 65.71  ? 116 ALA B CB  1 
ATOM   730  N  N   . GLN A 1 144 ? -10.579 -27.089 14.857  1.00 79.07  ? 117 GLN B N   1 
ATOM   731  C  CA  . GLN A 1 144 ? -9.154  -27.232 15.126  1.00 89.45  ? 117 GLN B CA  1 
ATOM   732  C  C   . GLN A 1 144 ? -8.923  -28.476 16.007  1.00 89.97  ? 117 GLN B C   1 
ATOM   733  O  O   . GLN A 1 144 ? -8.461  -29.508 15.503  1.00 84.50  ? 117 GLN B O   1 
ATOM   734  C  CB  . GLN A 1 144 ? -8.594  -25.931 15.736  1.00 94.88  ? 117 GLN B CB  1 
ATOM   735  C  CG  . GLN A 1 144 ? -7.208  -25.547 15.227  1.00 104.34 ? 117 GLN B CG  1 
ATOM   736  C  CD  . GLN A 1 144 ? -6.112  -26.406 15.833  1.00 105.91 ? 117 GLN B CD  1 
ATOM   737  O  OE1 . GLN A 1 144 ? -5.620  -26.132 16.936  1.00 104.44 ? 117 GLN B OE1 1 
ATOM   738  N  NE2 . GLN A 1 144 ? -5.727  -27.458 15.118  1.00 104.20 ? 117 GLN B NE2 1 
ATOM   739  N  N   . ASN A 1 145 ? -9.241  -28.360 17.300  1.00 92.10  ? 118 ASN B N   1 
ATOM   740  C  CA  . ASN A 1 145 ? -9.463  -29.499 18.248  1.00 93.23  ? 118 ASN B CA  1 
ATOM   741  C  C   . ASN A 1 145 ? -9.811  -30.885 17.673  1.00 93.34  ? 118 ASN B C   1 
ATOM   742  O  O   . ASN A 1 145 ? -9.318  -31.910 18.163  1.00 88.64  ? 118 ASN B O   1 
ATOM   743  C  CB  . ASN A 1 145 ? -10.609 -29.174 19.230  1.00 90.94  ? 118 ASN B CB  1 
ATOM   744  C  CG  . ASN A 1 145 ? -10.601 -27.736 19.718  1.00 85.15  ? 118 ASN B CG  1 
ATOM   745  O  OD1 . ASN A 1 145 ? -10.079 -27.438 20.786  1.00 88.27  ? 118 ASN B OD1 1 
ATOM   746  N  ND2 . ASN A 1 145 ? -11.200 -26.842 18.943  1.00 85.70  ? 118 ASN B ND2 1 
ATOM   747  N  N   . LYS A 1 146 ? -10.713 -30.913 16.689  1.00 104.24 ? 119 LYS B N   1 
ATOM   748  C  CA  . LYS A 1 146 ? -11.148 -32.165 16.051  1.00 108.30 ? 119 LYS B CA  1 
ATOM   749  C  C   . LYS A 1 146 ? -10.059 -32.782 15.165  1.00 119.46 ? 119 LYS B C   1 
ATOM   750  O  O   . LYS A 1 146 ? -9.826  -34.004 15.216  1.00 116.27 ? 119 LYS B O   1 
ATOM   751  C  CB  . LYS A 1 146 ? -12.394 -31.935 15.207  1.00 100.16 ? 119 LYS B CB  1 
ATOM   752  C  CG  . LYS A 1 146 ? -12.950 -33.223 14.638  1.00 101.34 ? 119 LYS B CG  1 
ATOM   753  C  CD  . LYS A 1 146 ? -13.623 -32.978 13.312  1.00 107.53 ? 119 LYS B CD  1 
ATOM   754  C  CE  . LYS A 1 146 ? -13.382 -34.090 12.297  1.00 116.03 ? 119 LYS B CE  1 
ATOM   755  N  NZ  . LYS A 1 146 ? -14.412 -35.172 12.308  1.00 117.17 ? 119 LYS B NZ  1 
ATOM   756  N  N   . ILE A 1 147 ? -9.421  -31.938 14.343  1.00 117.19 ? 120 ILE B N   1 
ATOM   757  C  CA  . ILE A 1 147 ? -8.255  -32.338 13.547  1.00 104.90 ? 120 ILE B CA  1 
ATOM   758  C  C   . ILE A 1 147 ? -7.148  -32.912 14.458  1.00 104.45 ? 120 ILE B C   1 
ATOM   759  O  O   . ILE A 1 147 ? -6.441  -33.832 14.065  1.00 113.20 ? 120 ILE B O   1 
ATOM   760  C  CB  . ILE A 1 147 ? -7.726  -31.170 12.684  1.00 96.34  ? 120 ILE B CB  1 
ATOM   761  N  N   . ASP A 1 148 ? -7.031  -32.388 15.680  1.00 111.01 ? 121 ASP B N   1 
ATOM   762  C  CA  . ASP A 1 148 ? -6.182  -32.969 16.741  1.00 108.59 ? 121 ASP B CA  1 
ATOM   763  C  C   . ASP A 1 148 ? -6.969  -33.890 17.696  1.00 109.14 ? 121 ASP B C   1 
ATOM   764  O  O   . ASP A 1 148 ? -7.612  -34.863 17.288  1.00 103.51 ? 121 ASP B O   1 
ATOM   765  C  CB  . ASP A 1 148 ? -5.533  -31.853 17.574  1.00 108.85 ? 121 ASP B CB  1 
ATOM   766  C  CG  . ASP A 1 148 ? -4.690  -30.885 16.734  1.00 115.13 ? 121 ASP B CG  1 
ATOM   767  O  OD1 . ASP A 1 148 ? -4.346  -31.199 15.572  1.00 116.25 ? 121 ASP B OD1 1 
ATOM   768  O  OD2 . ASP A 1 148 ? -4.360  -29.798 17.248  1.00 110.22 ? 121 ASP B OD2 1 
ATOM   769  N  N   . SER A 1 164 ? -9.473  -20.326 16.317  1.00 68.36  ? 137 SER B N   1 
ATOM   770  C  CA  . SER A 1 164 ? -9.687  -21.188 17.478  1.00 72.54  ? 137 SER B CA  1 
ATOM   771  C  C   . SER A 1 164 ? -10.592 -20.621 18.630  1.00 71.87  ? 137 SER B C   1 
ATOM   772  O  O   . SER A 1 164 ? -10.418 -19.478 19.088  1.00 78.01  ? 137 SER B O   1 
ATOM   773  C  CB  . SER A 1 164 ? -8.338  -21.570 18.045  1.00 69.08  ? 137 SER B CB  1 
ATOM   774  O  OG  . SER A 1 164 ? -8.518  -22.591 18.993  1.00 62.38  ? 137 SER B OG  1 
ATOM   775  N  N   . THR A 1 165 ? -11.526 -21.450 19.113  1.00 69.35  ? 138 THR B N   1 
ATOM   776  C  CA  . THR A 1 165 ? -12.612 -21.012 20.021  1.00 65.85  ? 138 THR B CA  1 
ATOM   777  C  C   . THR A 1 165 ? -12.392 -21.431 21.469  1.00 61.08  ? 138 THR B C   1 
ATOM   778  O  O   . THR A 1 165 ? -12.271 -22.606 21.781  1.00 63.33  ? 138 THR B O   1 
ATOM   779  C  CB  . THR A 1 165 ? -13.986 -21.561 19.591  1.00 67.79  ? 138 THR B CB  1 
ATOM   780  O  OG1 . THR A 1 165 ? -14.292 -21.142 18.255  1.00 79.76  ? 138 THR B OG1 1 
ATOM   781  C  CG2 . THR A 1 165 ? -15.053 -21.017 20.483  1.00 70.88  ? 138 THR B CG2 1 
ATOM   782  N  N   . ILE A 1 166 ? -12.381 -20.461 22.364  1.00 56.80  ? 139 ILE B N   1 
ATOM   783  C  CA  . ILE A 1 166 ? -11.960 -20.714 23.730  1.00 58.07  ? 139 ILE B CA  1 
ATOM   784  C  C   . ILE A 1 166 ? -13.113 -21.065 24.688  1.00 57.82  ? 139 ILE B C   1 
ATOM   785  O  O   . ILE A 1 166 ? -12.908 -21.687 25.719  1.00 55.24  ? 139 ILE B O   1 
ATOM   786  C  CB  . ILE A 1 166 ? -11.138 -19.503 24.247  1.00 58.11  ? 139 ILE B CB  1 
ATOM   787  C  CG1 . ILE A 1 166 ? -9.988  -20.025 25.051  1.00 60.75  ? 139 ILE B CG1 1 
ATOM   788  C  CG2 . ILE A 1 166 ? -11.966 -18.473 25.009  1.00 55.80  ? 139 ILE B CG2 1 
ATOM   789  C  CD1 . ILE A 1 166 ? -9.021  -20.781 24.155  1.00 62.40  ? 139 ILE B CD1 1 
ATOM   790  N  N   . ALA A 1 167 ? -14.315 -20.648 24.322  1.00 54.49  ? 140 ALA B N   1 
ATOM   791  C  CA  . ALA A 1 167 ? -15.480 -20.754 25.158  1.00 52.38  ? 140 ALA B CA  1 
ATOM   792  C  C   . ALA A 1 167 ? -16.711 -20.431 24.285  1.00 52.26  ? 140 ALA B C   1 
ATOM   793  O  O   . ALA A 1 167 ? -16.613 -19.691 23.303  1.00 50.09  ? 140 ALA B O   1 
ATOM   794  C  CB  . ALA A 1 167 ? -15.354 -19.781 26.313  1.00 52.67  ? 140 ALA B CB  1 
ATOM   795  N  N   . VAL A 1 168 ? -17.858 -21.002 24.625  1.00 49.43  ? 141 VAL B N   1 
ATOM   796  C  CA  . VAL A 1 168 ? -19.086 -20.796 23.853  1.00 46.08  ? 141 VAL B CA  1 
ATOM   797  C  C   . VAL A 1 168 ? -20.145 -20.317 24.805  1.00 41.84  ? 141 VAL B C   1 
ATOM   798  O  O   . VAL A 1 168 ? -20.272 -20.862 25.888  1.00 48.98  ? 141 VAL B O   1 
ATOM   799  C  CB  . VAL A 1 168 ? -19.573 -22.103 23.190  1.00 46.34  ? 141 VAL B CB  1 
ATOM   800  C  CG1 . VAL A 1 168 ? -20.940 -21.936 22.574  1.00 50.54  ? 141 VAL B CG1 1 
ATOM   801  C  CG2 . VAL A 1 168 ? -18.614 -22.521 22.123  1.00 46.74  ? 141 VAL B CG2 1 
ATOM   802  N  N   . VAL A 1 169 ? -20.891 -19.302 24.380  1.00 43.93  ? 142 VAL B N   1 
ATOM   803  C  CA  . VAL A 1 169 ? -22.007 -18.702 25.114  1.00 45.06  ? 142 VAL B CA  1 
ATOM   804  C  C   . VAL A 1 169 ? -23.270 -19.197 24.446  1.00 46.49  ? 142 VAL B C   1 
ATOM   805  O  O   . VAL A 1 169 ? -23.473 -18.897 23.304  1.00 51.87  ? 142 VAL B O   1 
ATOM   806  C  CB  . VAL A 1 169 ? -21.953 -17.192 24.954  1.00 44.72  ? 142 VAL B CB  1 
ATOM   807  C  CG1 . VAL A 1 169 ? -23.211 -16.532 25.472  1.00 45.43  ? 142 VAL B CG1 1 
ATOM   808  C  CG2 . VAL A 1 169 ? -20.705 -16.649 25.626  1.00 46.47  ? 142 VAL B CG2 1 
ATOM   809  N  N   . GLY A 1 170 ? -24.091 -19.974 25.140  1.00 47.41  ? 143 GLY B N   1 
ATOM   810  C  CA  . GLY A 1 170 ? -25.247 -20.662 24.537  1.00 44.95  ? 143 GLY B CA  1 
ATOM   811  C  C   . GLY A 1 170 ? -25.446 -22.081 25.055  1.00 42.91  ? 143 GLY B C   1 
ATOM   812  O  O   . GLY A 1 170 ? -24.717 -22.514 25.942  1.00 42.85  ? 143 GLY B O   1 
ATOM   813  N  N   . ALA A 1 171 ? -26.438 -22.809 24.539  1.00 42.05  ? 144 ALA B N   1 
ATOM   814  C  CA  . ALA A 1 171 ? -27.492 -22.265 23.654  1.00 43.29  ? 144 ALA B CA  1 
ATOM   815  C  C   . ALA A 1 171 ? -28.723 -21.825 24.500  1.00 45.15  ? 144 ALA B C   1 
ATOM   816  O  O   . ALA A 1 171 ? -28.609 -21.629 25.719  1.00 48.85  ? 144 ALA B O   1 
ATOM   817  C  CB  . ALA A 1 171 ? -27.876 -23.328 22.654  1.00 42.18  ? 144 ALA B CB  1 
ATOM   818  N  N   . THR A 1 172 ? -29.892 -21.676 23.884  1.00 42.84  ? 145 THR B N   1 
ATOM   819  C  CA  . THR A 1 172 ? -31.111 -21.302 24.607  1.00 39.01  ? 145 THR B CA  1 
ATOM   820  C  C   . THR A 1 172 ? -31.929 -22.515 25.063  1.00 43.31  ? 145 THR B C   1 
ATOM   821  O  O   . THR A 1 172 ? -32.118 -22.734 26.264  1.00 54.76  ? 145 THR B O   1 
ATOM   822  C  CB  . THR A 1 172 ? -31.984 -20.427 23.730  1.00 37.51  ? 145 THR B CB  1 
ATOM   823  O  OG1 . THR A 1 172 ? -31.230 -19.283 23.328  1.00 38.78  ? 145 THR B OG1 1 
ATOM   824  C  CG2 . THR A 1 172 ? -33.279 -19.976 24.448  1.00 38.30  ? 145 THR B CG2 1 
ATOM   825  N  N   . GLY A 1 173 ? -32.438 -23.302 24.130  1.00 41.61  ? 146 GLY B N   1 
ATOM   826  C  CA  . GLY A 1 173 ? -33.263 -24.445 24.498  1.00 35.80  ? 146 GLY B CA  1 
ATOM   827  C  C   . GLY A 1 173 ? -32.388 -25.531 25.084  1.00 38.23  ? 146 GLY B C   1 
ATOM   828  O  O   . GLY A 1 173 ? -31.311 -25.830 24.556  1.00 41.24  ? 146 GLY B O   1 
ATOM   829  N  N   . SER A 1 174 ? -32.863 -26.151 26.156  1.00 37.52  ? 147 SER B N   1 
ATOM   830  C  CA  . SER A 1 174 ? -32.115 -27.170 26.845  1.00 38.49  ? 147 SER B CA  1 
ATOM   831  C  C   . SER A 1 174 ? -31.760 -28.366 25.957  1.00 40.10  ? 147 SER B C   1 
ATOM   832  O  O   . SER A 1 174 ? -30.704 -28.946 26.125  1.00 39.14  ? 147 SER B O   1 
ATOM   833  C  CB  . SER A 1 174 ? -32.899 -27.651 28.060  1.00 40.52  ? 147 SER B CB  1 
ATOM   834  O  OG  . SER A 1 174 ? -32.717 -26.767 29.165  1.00 41.57  ? 147 SER B OG  1 
ATOM   835  N  N   . GLY A 1 175 ? -32.644 -28.732 25.032  1.00 41.72  ? 148 GLY B N   1 
ATOM   836  C  CA  . GLY A 1 175 ? -32.377 -29.800 24.095  1.00 39.31  ? 148 GLY B CA  1 
ATOM   837  C  C   . GLY A 1 175 ? -31.229 -29.474 23.168  1.00 45.17  ? 148 GLY B C   1 
ATOM   838  O  O   . GLY A 1 175 ? -30.405 -30.350 22.811  1.00 49.58  ? 148 GLY B O   1 
ATOM   839  N  N   . VAL A 1 176 ? -31.148 -28.203 22.772  1.00 48.68  ? 149 VAL B N   1 
ATOM   840  C  CA  . VAL A 1 176 ? -30.063 -27.714 21.896  1.00 38.50  ? 149 VAL B CA  1 
ATOM   841  C  C   . VAL A 1 176 ? -28.738 -27.684 22.655  1.00 37.16  ? 149 VAL B C   1 
ATOM   842  O  O   . VAL A 1 176 ? -27.713 -28.179 22.173  1.00 33.40  ? 149 VAL B O   1 
ATOM   843  C  CB  . VAL A 1 176 ? -30.425 -26.329 21.375  1.00 38.11  ? 149 VAL B CB  1 
ATOM   844  C  CG1 . VAL A 1 176 ? -29.257 -25.664 20.655  1.00 43.18  ? 149 VAL B CG1 1 
ATOM   845  C  CG2 . VAL A 1 176 ? -31.588 -26.439 20.405  1.00 40.91  ? 149 VAL B CG2 1 
ATOM   846  N  N   . SER A 1 177 ? -28.768 -27.099 23.852  1.00 36.49  ? 150 SER B N   1 
ATOM   847  C  CA  . SER A 1 177 ? -27.595 -27.084 24.738  1.00 37.23  ? 150 SER B CA  1 
ATOM   848  C  C   . SER A 1 177 ? -27.061 -28.479 25.052  1.00 37.34  ? 150 SER B C   1 
ATOM   849  O  O   . SER A 1 177 ? -25.869 -28.659 25.186  1.00 35.81  ? 150 SER B O   1 
ATOM   850  C  CB  . SER A 1 177 ? -27.916 -26.364 26.046  1.00 38.35  ? 150 SER B CB  1 
ATOM   851  O  OG  . SER A 1 177 ? -27.829 -24.969 25.891  1.00 40.67  ? 150 SER B OG  1 
ATOM   852  N  N   . THR A 1 178 ? -27.955 -29.453 25.164  1.00 38.70  ? 151 THR B N   1 
ATOM   853  C  CA  . THR A 1 178 ? -27.563 -30.811 25.413  1.00 40.13  ? 151 THR B CA  1 
ATOM   854  C  C   . THR A 1 178 ? -26.742 -31.353 24.291  1.00 41.38  ? 151 THR B C   1 
ATOM   855  O  O   . THR A 1 178 ? -25.680 -31.880 24.513  1.00 43.37  ? 151 THR B O   1 
ATOM   856  C  CB  . THR A 1 178 ? -28.771 -31.715 25.562  1.00 43.12  ? 151 THR B CB  1 
ATOM   857  O  OG1 . THR A 1 178 ? -29.387 -31.411 26.792  1.00 42.10  ? 151 THR B OG1 1 
ATOM   858  C  CG2 . THR A 1 178 ? -28.356 -33.168 25.603  1.00 46.10  ? 151 THR B CG2 1 
ATOM   859  N  N   . ALA A 1 179 ? -27.238 -31.231 23.074  1.00 46.83  ? 152 ALA B N   1 
ATOM   860  C  CA  . ALA A 1 179 ? -26.496 -31.724 21.922  1.00 46.18  ? 152 ALA B CA  1 
ATOM   861  C  C   . ALA A 1 179 ? -25.176 -31.004 21.801  1.00 46.33  ? 152 ALA B C   1 
ATOM   862  O  O   . ALA A 1 179 ? -24.183 -31.601 21.453  1.00 54.16  ? 152 ALA B O   1 
ATOM   863  C  CB  . ALA A 1 179 ? -27.291 -31.556 20.641  1.00 44.37  ? 152 ALA B CB  1 
ATOM   864  N  N   . VAL A 1 180 ? -25.157 -29.717 22.072  1.00 48.45  ? 153 VAL B N   1 
ATOM   865  C  CA  . VAL A 1 180 ? -23.923 -28.945 21.877  1.00 50.41  ? 153 VAL B CA  1 
ATOM   866  C  C   . VAL A 1 180 ? -22.894 -29.373 22.909  1.00 48.33  ? 153 VAL B C   1 
ATOM   867  O  O   . VAL A 1 180 ? -21.734 -29.588 22.583  1.00 48.65  ? 153 VAL B O   1 
ATOM   868  C  CB  . VAL A 1 180 ? -24.225 -27.445 21.956  1.00 49.41  ? 153 VAL B CB  1 
ATOM   869  C  CG1 . VAL A 1 180 ? -22.990 -26.630 22.196  1.00 50.81  ? 153 VAL B CG1 1 
ATOM   870  C  CG2 . VAL A 1 180 ? -24.844 -27.020 20.651  1.00 54.85  ? 153 VAL B CG2 1 
ATOM   871  N  N   . ALA A 1 181 ? -23.357 -29.514 24.143  1.00 45.36  ? 154 ALA B N   1 
ATOM   872  C  CA  . ALA A 1 181 ? -22.554 -29.943 25.268  1.00 43.85  ? 154 ALA B CA  1 
ATOM   873  C  C   . ALA A 1 181 ? -21.934 -31.326 25.077  1.00 44.00  ? 154 ALA B C   1 
ATOM   874  O  O   . ALA A 1 181 ? -20.841 -31.585 25.518  1.00 40.84  ? 154 ALA B O   1 
ATOM   875  C  CB  . ALA A 1 181 ? -23.429 -29.971 26.513  1.00 46.33  ? 154 ALA B CB  1 
ATOM   876  N  N   . ASN A 1 182 ? -22.663 -32.238 24.463  1.00 45.63  ? 155 ASN B N   1 
ATOM   877  C  CA  . ASN A 1 182 ? -22.123 -33.528 24.211  1.00 46.05  ? 155 ASN B CA  1 
ATOM   878  C  C   . ASN A 1 182 ? -20.874 -33.373 23.370  1.00 47.45  ? 155 ASN B C   1 
ATOM   879  O  O   . ASN A 1 182 ? -19.894 -34.090 23.574  1.00 49.12  ? 155 ASN B O   1 
ATOM   880  C  CB  . ASN A 1 182 ? -23.148 -34.404 23.504  1.00 50.57  ? 155 ASN B CB  1 
ATOM   881  C  CG  . ASN A 1 182 ? -24.140 -35.031 24.458  1.00 52.51  ? 155 ASN B CG  1 
ATOM   882  O  OD1 . ASN A 1 182 ? -23.863 -35.210 25.652  1.00 58.08  ? 155 ASN B OD1 1 
ATOM   883  N  ND2 . ASN A 1 182 ? -25.302 -35.388 23.933  1.00 54.18  ? 155 ASN B ND2 1 
ATOM   884  N  N   . LEU A 1 183 ? -20.900 -32.408 22.461  1.00 48.93  ? 156 LEU B N   1 
ATOM   885  C  CA  . LEU A 1 183 ? -19.757 -32.136 21.582  1.00 52.59  ? 156 LEU B CA  1 
ATOM   886  C  C   . LEU A 1 183 ? -18.615 -31.361 22.216  1.00 50.52  ? 156 LEU B C   1 
ATOM   887  O  O   . LEU A 1 183 ? -17.490 -31.816 22.245  1.00 55.06  ? 156 LEU B O   1 
ATOM   888  C  CB  . LEU A 1 183 ? -20.204 -31.399 20.320  1.00 51.83  ? 156 LEU B CB  1 
ATOM   889  C  CG  . LEU A 1 183 ? -19.823 -32.185 19.089  1.00 55.19  ? 156 LEU B CG  1 
ATOM   890  C  CD1 . LEU A 1 183 ? -20.283 -31.454 17.860  1.00 61.49  ? 156 LEU B CD1 1 
ATOM   891  C  CD2 . LEU A 1 183 ? -18.323 -32.403 19.055  1.00 59.99  ? 156 LEU B CD2 1 
ATOM   892  N  N   . LEU A 1 184 ? -18.898 -30.171 22.700  1.00 52.41  ? 157 LEU B N   1 
ATOM   893  C  CA  . LEU A 1 184 ? -17.866 -29.351 23.304  1.00 50.77  ? 157 LEU B CA  1 
ATOM   894  C  C   . LEU A 1 184 ? -17.212 -30.093 24.451  1.00 51.01  ? 157 LEU B C   1 
ATOM   895  O  O   . LEU A 1 184 ? -16.021 -29.943 24.721  1.00 54.76  ? 157 LEU B O   1 
ATOM   896  C  CB  . LEU A 1 184 ? -18.483 -28.067 23.845  1.00 47.94  ? 157 LEU B CB  1 
ATOM   897  C  CG  . LEU A 1 184 ? -19.151 -27.185 22.815  1.00 45.38  ? 157 LEU B CG  1 
ATOM   898  C  CD1 . LEU A 1 184 ? -19.798 -26.021 23.535  1.00 48.13  ? 157 LEU B CD1 1 
ATOM   899  C  CD2 . LEU A 1 184 ? -18.148 -26.703 21.784  1.00 46.14  ? 157 LEU B CD2 1 
ATOM   900  N  N   . GLY A 1 185 ? -18.007 -30.887 25.147  1.00 47.33  ? 158 GLY B N   1 
ATOM   901  C  CA  . GLY A 1 185 ? -17.491 -31.654 26.264  1.00 48.88  ? 158 GLY B CA  1 
ATOM   902  C  C   . GLY A 1 185 ? -16.373 -32.606 25.923  1.00 44.55  ? 158 GLY B C   1 
ATOM   903  O  O   . GLY A 1 185 ? -15.529 -32.878 26.733  1.00 45.55  ? 158 GLY B O   1 
ATOM   904  N  N   . LEU A 1 186 ? -16.380 -33.131 24.719  1.00 49.83  ? 159 LEU B N   1 
ATOM   905  C  CA  . LEU A 1 186 ? -15.260 -33.926 24.251  1.00 55.86  ? 159 LEU B CA  1 
ATOM   906  C  C   . LEU A 1 186 ? -13.898 -33.206 24.298  1.00 56.22  ? 159 LEU B C   1 
ATOM   907  O  O   . LEU A 1 186 ? -12.894 -33.860 24.456  1.00 63.05  ? 159 LEU B O   1 
ATOM   908  C  CB  . LEU A 1 186 ? -15.492 -34.337 22.820  1.00 57.88  ? 159 LEU B CB  1 
ATOM   909  C  CG  . LEU A 1 186 ? -16.587 -35.347 22.630  1.00 60.88  ? 159 LEU B CG  1 
ATOM   910  C  CD1 . LEU A 1 186 ? -16.818 -35.500 21.139  1.00 62.98  ? 159 LEU B CD1 1 
ATOM   911  C  CD2 . LEU A 1 186 ? -16.180 -36.667 23.266  1.00 69.12  ? 159 LEU B CD2 1 
ATOM   912  N  N   . PHE A 1 187 ? -13.877 -31.886 24.143  1.00 51.72  ? 160 PHE B N   1 
ATOM   913  C  CA  . PHE A 1 187 ? -12.643 -31.116 23.991  1.00 48.17  ? 160 PHE B CA  1 
ATOM   914  C  C   . PHE A 1 187 ? -12.477 -30.193 25.152  1.00 44.99  ? 160 PHE B C   1 
ATOM   915  O  O   . PHE A 1 187 ? -11.671 -29.289 25.126  1.00 51.25  ? 160 PHE B O   1 
ATOM   916  C  CB  . PHE A 1 187 ? -12.734 -30.308 22.697  1.00 50.16  ? 160 PHE B CB  1 
ATOM   917  C  CG  . PHE A 1 187 ? -13.005 -31.171 21.508  1.00 56.62  ? 160 PHE B CG  1 
ATOM   918  C  CD1 . PHE A 1 187 ? -12.123 -32.216 21.191  1.00 61.60  ? 160 PHE B CD1 1 
ATOM   919  C  CD2 . PHE A 1 187 ? -14.144 -31.016 20.761  1.00 54.20  ? 160 PHE B CD2 1 
ATOM   920  C  CE1 . PHE A 1 187 ? -12.363 -33.058 20.122  1.00 64.21  ? 160 PHE B CE1 1 
ATOM   921  C  CE2 . PHE A 1 187 ? -14.390 -31.854 19.685  1.00 63.55  ? 160 PHE B CE2 1 
ATOM   922  C  CZ  . PHE A 1 187 ? -13.504 -32.878 19.362  1.00 64.85  ? 160 PHE B CZ  1 
ATOM   923  N  N   . TYR A 1 188 ? -13.279 -30.401 26.172  1.00 43.22  ? 161 TYR B N   1 
ATOM   924  C  CA  . TYR A 1 188 ? -13.220 -29.583 27.371  1.00 43.70  ? 161 TYR B CA  1 
ATOM   925  C  C   . TYR A 1 188 ? -13.367 -28.116 27.070  1.00 41.57  ? 161 TYR B C   1 
ATOM   926  O  O   . TYR A 1 188 ? -12.825 -27.284 27.735  1.00 51.21  ? 161 TYR B O   1 
ATOM   927  C  CB  . TYR A 1 188 ? -11.975 -29.927 28.213  1.00 41.94  ? 161 TYR B CB  1 
ATOM   928  C  CG  . TYR A 1 188 ? -12.079 -31.336 28.769  1.00 43.44  ? 161 TYR B CG  1 
ATOM   929  C  CD1 . TYR A 1 188 ? -11.607 -32.446 28.029  1.00 43.02  ? 161 TYR B CD1 1 
ATOM   930  C  CD2 . TYR A 1 188 ? -12.713 -31.573 29.989  1.00 41.01  ? 161 TYR B CD2 1 
ATOM   931  C  CE1 . TYR A 1 188 ? -11.743 -33.745 28.506  1.00 45.69  ? 161 TYR B CE1 1 
ATOM   932  C  CE2 . TYR A 1 188 ? -12.858 -32.869 30.485  1.00 45.41  ? 161 TYR B CE2 1 
ATOM   933  C  CZ  . TYR A 1 188 ? -12.378 -33.963 29.754  1.00 51.96  ? 161 TYR B CZ  1 
ATOM   934  O  OH  . TYR A 1 188 ? -12.526 -35.263 30.270  1.00 51.06  ? 161 TYR B OH  1 
ATOM   935  N  N   . ILE A 1 189 ? -14.184 -27.789 26.096  1.00 42.67  ? 162 ILE B N   1 
ATOM   936  C  CA  . ILE A 1 189 ? -14.423 -26.392 25.792  1.00 42.05  ? 162 ILE B CA  1 
ATOM   937  C  C   . ILE A 1 189 ? -15.514 -25.850 26.676  1.00 39.57  ? 162 ILE B C   1 
ATOM   938  O  O   . ILE A 1 189 ? -16.651 -26.243 26.562  1.00 43.79  ? 162 ILE B O   1 
ATOM   939  C  CB  . ILE A 1 189 ? -14.792 -26.244 24.322  1.00 42.13  ? 162 ILE B CB  1 
ATOM   940  C  CG1 . ILE A 1 189 ? -13.593 -26.697 23.504  1.00 44.23  ? 162 ILE B CG1 1 
ATOM   941  C  CG2 . ILE A 1 189 ? -15.103 -24.798 23.998  1.00 44.33  ? 162 ILE B CG2 1 
ATOM   942  C  CD1 . ILE A 1 189 ? -13.735 -26.464 22.026  1.00 48.66  ? 162 ILE B CD1 1 
ATOM   943  N  N   . PRO A 1 190 ? -15.186 -24.956 27.579  1.00 38.99  ? 163 PRO B N   1 
ATOM   944  C  CA  . PRO A 1 190 ? -16.281 -24.436 28.431  1.00 41.56  ? 163 PRO B CA  1 
ATOM   945  C  C   . PRO A 1 190 ? -17.456 -23.860 27.654  1.00 40.22  ? 163 PRO B C   1 
ATOM   946  O  O   . PRO A 1 190 ? -17.249 -23.174 26.659  1.00 42.76  ? 163 PRO B O   1 
ATOM   947  C  CB  . PRO A 1 190 ? -15.623 -23.305 29.206  1.00 40.90  ? 163 PRO B CB  1 
ATOM   948  C  CG  . PRO A 1 190 ? -14.488 -22.884 28.346  1.00 40.23  ? 163 PRO B CG  1 
ATOM   949  C  CD  . PRO A 1 190 ? -13.996 -24.116 27.628  1.00 39.14  ? 163 PRO B CD  1 
ATOM   950  N  N   . GLN A 1 191 ? -18.668 -24.161 28.118  1.00 39.42  ? 164 GLN B N   1 
ATOM   951  C  CA  . GLN A 1 191 ? -19.909 -23.663 27.552  1.00 36.05  ? 164 GLN B CA  1 
ATOM   952  C  C   . GLN A 1 191 ? -20.758 -23.029 28.674  1.00 38.74  ? 164 GLN B C   1 
ATOM   953  O  O   . GLN A 1 191 ? -21.063 -23.667 29.660  1.00 37.40  ? 164 GLN B O   1 
ATOM   954  C  CB  . GLN A 1 191 ? -20.659 -24.828 26.955  1.00 36.94  ? 164 GLN B CB  1 
ATOM   955  C  CG  . GLN A 1 191 ? -21.968 -24.464 26.252  1.00 37.86  ? 164 GLN B CG  1 
ATOM   956  C  CD  . GLN A 1 191 ? -22.806 -25.660 25.864  1.00 36.06  ? 164 GLN B CD  1 
ATOM   957  O  OE1 . GLN A 1 191 ? -22.312 -26.771 25.717  1.00 42.14  ? 164 GLN B OE1 1 
ATOM   958  N  NE2 . GLN A 1 191 ? -24.091 -25.437 25.695  1.00 40.77  ? 164 GLN B NE2 1 
ATOM   959  N  N   . VAL A 1 192 ? -21.152 -21.774 28.515  1.00 40.34  ? 165 VAL B N   1 
ATOM   960  C  CA  . VAL A 1 192 ? -21.916 -21.071 29.539  1.00 39.33  ? 165 VAL B CA  1 
ATOM   961  C  C   . VAL A 1 192 ? -23.250 -20.673 28.913  1.00 40.30  ? 165 VAL B C   1 
ATOM   962  O  O   . VAL A 1 192 ? -23.272 -19.787 28.074  1.00 42.41  ? 165 VAL B O   1 
ATOM   963  C  CB  . VAL A 1 192 ? -21.208 -19.778 29.981  1.00 40.56  ? 165 VAL B CB  1 
ATOM   964  C  CG1 . VAL A 1 192 ? -21.947 -19.137 31.136  1.00 41.43  ? 165 VAL B CG1 1 
ATOM   965  C  CG2 . VAL A 1 192 ? -19.774 -20.044 30.362  1.00 41.31  ? 165 VAL B CG2 1 
ATOM   966  N  N   . SER A 1 193 ? -24.349 -21.310 29.318  1.00 39.91  ? 166 SER B N   1 
ATOM   967  C  CA  . SER A 1 193 ? -25.660 -20.998 28.784  1.00 39.09  ? 166 SER B CA  1 
ATOM   968  C  C   . SER A 1 193 ? -26.367 -19.921 29.568  1.00 37.08  ? 166 SER B C   1 
ATOM   969  O  O   . SER A 1 193 ? -26.342 -19.924 30.786  1.00 39.84  ? 166 SER B O   1 
ATOM   970  C  CB  . SER A 1 193 ? -26.549 -22.252 28.732  1.00 42.09  ? 166 SER B CB  1 
ATOM   971  O  OG  . SER A 1 193 ? -27.867 -21.951 28.197  1.00 40.96  ? 166 SER B OG  1 
ATOM   972  N  N   . TYR A 1 194 ? -27.051 -19.050 28.842  1.00 38.78  ? 167 TYR B N   1 
ATOM   973  C  CA  . TYR A 1 194 ? -27.851 -17.931 29.389  1.00 42.10  ? 167 TYR B CA  1 
ATOM   974  C  C   . TYR A 1 194 ? -29.314 -18.303 29.629  1.00 42.25  ? 167 TYR B C   1 
ATOM   975  O  O   . TYR A 1 194 ? -30.048 -17.594 30.327  1.00 45.95  ? 167 TYR B O   1 
ATOM   976  C  CB  . TYR A 1 194 ? -27.808 -16.703 28.464  1.00 42.66  ? 167 TYR B CB  1 
ATOM   977  C  CG  . TYR A 1 194 ? -27.974 -17.071 27.012  1.00 44.98  ? 167 TYR B CG  1 
ATOM   978  C  CD1 . TYR A 1 194 ? -29.219 -17.201 26.460  1.00 42.07  ? 167 TYR B CD1 1 
ATOM   979  C  CD2 . TYR A 1 194 ? -26.867 -17.349 26.212  1.00 48.66  ? 167 TYR B CD2 1 
ATOM   980  C  CE1 . TYR A 1 194 ? -29.379 -17.568 25.142  1.00 47.14  ? 167 TYR B CE1 1 
ATOM   981  C  CE2 . TYR A 1 194 ? -27.023 -17.741 24.882  1.00 47.30  ? 167 TYR B CE2 1 
ATOM   982  C  CZ  . TYR A 1 194 ? -28.287 -17.842 24.355  1.00 47.21  ? 167 TYR B CZ  1 
ATOM   983  O  OH  . TYR A 1 194 ? -28.486 -18.199 23.038  1.00 50.97  ? 167 TYR B OH  1 
ATOM   984  N  N   . ALA A 1 195 ? -29.758 -19.399 29.052  1.00 41.94  ? 168 ALA B N   1 
ATOM   985  C  CA  . ALA A 1 195 ? -31.147 -19.754 29.213  1.00 39.81  ? 168 ALA B CA  1 
ATOM   986  C  C   . ALA A 1 195 ? -31.503 -21.235 29.387  1.00 39.76  ? 168 ALA B C   1 
ATOM   987  O  O   . ALA A 1 195 ? -32.631 -21.515 29.711  1.00 43.04  ? 168 ALA B O   1 
ATOM   988  C  CB  . ALA A 1 195 ? -31.917 -19.147 28.069  1.00 42.19  ? 168 ALA B CB  1 
ATOM   989  N  N   . SER A 1 196 ? -30.583 -22.188 29.224  1.00 40.64  ? 169 SER B N   1 
ATOM   990  C  CA  . SER A 1 196 ? -30.977 -23.613 29.257  1.00 43.87  ? 169 SER B CA  1 
ATOM   991  C  C   . SER A 1 196 ? -31.094 -24.139 30.675  1.00 43.52  ? 169 SER B C   1 
ATOM   992  O  O   . SER A 1 196 ? -30.102 -24.254 31.345  1.00 44.66  ? 169 SER B O   1 
ATOM   993  C  CB  . SER A 1 196 ? -29.954 -24.453 28.517  1.00 44.49  ? 169 SER B CB  1 
ATOM   994  O  OG  . SER A 1 196 ? -29.829 -24.001 27.195  1.00 44.51  ? 169 SER B OG  1 
ATOM   995  N  N   . SER A 1 197 ? -32.291 -24.480 31.126  1.00 43.58  ? 170 SER B N   1 
ATOM   996  C  CA  . SER A 1 197 ? -32.539 -24.667 32.569  1.00 43.05  ? 170 SER B CA  1 
ATOM   997  C  C   . SER A 1 197 ? -32.905 -26.077 32.972  1.00 40.60  ? 170 SER B C   1 
ATOM   998  O  O   . SER A 1 197 ? -33.247 -26.299 34.121  1.00 38.83  ? 170 SER B O   1 
ATOM   999  C  CB  . SER A 1 197 ? -33.652 -23.732 33.033  1.00 45.28  ? 170 SER B CB  1 
ATOM   1000 O  OG  . SER A 1 197 ? -34.785 -23.838 32.171  1.00 46.24  ? 170 SER B OG  1 
ATOM   1001 N  N   . SER A 1 198 ? -32.773 -27.044 32.076  1.00 40.77  ? 171 SER B N   1 
ATOM   1002 C  CA  . SER A 1 198 ? -33.118 -28.401 32.452  1.00 42.30  ? 171 SER B CA  1 
ATOM   1003 C  C   . SER A 1 198 ? -32.200 -28.894 33.524  1.00 44.68  ? 171 SER B C   1 
ATOM   1004 O  O   . SER A 1 198 ? -31.016 -28.657 33.477  1.00 46.41  ? 171 SER B O   1 
ATOM   1005 C  CB  . SER A 1 198 ? -32.983 -29.362 31.302  1.00 43.52  ? 171 SER B CB  1 
ATOM   1006 O  OG  . SER A 1 198 ? -33.181 -30.674 31.778  1.00 37.13  ? 171 SER B OG  1 
ATOM   1007 N  N   . ARG A 1 199 ? -32.753 -29.607 34.489  1.00 47.10  ? 172 ARG B N   1 
ATOM   1008 C  CA  . ARG A 1 199 ? -31.938 -30.233 35.525  1.00 46.53  ? 172 ARG B CA  1 
ATOM   1009 C  C   . ARG A 1 199 ? -30.954 -31.245 34.918  1.00 44.91  ? 172 ARG B C   1 
ATOM   1010 O  O   . ARG A 1 199 ? -29.978 -31.603 35.550  1.00 52.81  ? 172 ARG B O   1 
ATOM   1011 C  CB  . ARG A 1 199 ? -32.835 -30.968 36.540  1.00 44.83  ? 172 ARG B CB  1 
ATOM   1012 C  CG  . ARG A 1 199 ? -33.390 -32.265 36.004  1.00 43.94  ? 172 ARG B CG  1 
ATOM   1013 C  CD  . ARG A 1 199 ? -33.897 -33.188 37.084  1.00 45.94  ? 172 ARG B CD  1 
ATOM   1014 N  NE  . ARG A 1 199 ? -34.395 -34.475 36.546  1.00 46.53  ? 172 ARG B NE  1 
ATOM   1015 C  CZ  . ARG A 1 199 ? -33.642 -35.555 36.282  1.00 42.63  ? 172 ARG B CZ  1 
ATOM   1016 N  NH1 . ARG A 1 199 ? -32.356 -35.559 36.466  1.00 40.78  ? 172 ARG B NH1 1 
ATOM   1017 N  NH2 . ARG A 1 199 ? -34.193 -36.645 35.808  1.00 46.25  ? 172 ARG B NH2 1 
ATOM   1018 N  N   . LEU A 1 200 ? -31.231 -31.724 33.714  1.00 41.41  ? 173 LEU B N   1 
ATOM   1019 C  CA  . LEU A 1 200 ? -30.450 -32.765 33.124  1.00 40.91  ? 173 LEU B CA  1 
ATOM   1020 C  C   . LEU A 1 200 ? -29.048 -32.260 32.914  1.00 41.71  ? 173 LEU B C   1 
ATOM   1021 O  O   . LEU A 1 200 ? -28.091 -33.002 33.077  1.00 41.68  ? 173 LEU B O   1 
ATOM   1022 C  CB  . LEU A 1 200 ? -31.078 -33.199 31.801  1.00 45.22  ? 173 LEU B CB  1 
ATOM   1023 C  CG  . LEU A 1 200 ? -32.359 -34.027 31.959  1.00 52.97  ? 173 LEU B CG  1 
ATOM   1024 C  CD1 . LEU A 1 200 ? -32.980 -34.360 30.612  1.00 54.92  ? 173 LEU B CD1 1 
ATOM   1025 C  CD2 . LEU A 1 200 ? -32.117 -35.308 32.763  1.00 52.92  ? 173 LEU B CD2 1 
ATOM   1026 N  N   . LEU A 1 201 ? -28.925 -30.978 32.609  1.00 39.20  ? 174 LEU B N   1 
ATOM   1027 C  CA  . LEU A 1 201 ? -27.625 -30.390 32.404  1.00 43.91  ? 174 LEU B CA  1 
ATOM   1028 C  C   . LEU A 1 201 ? -26.750 -30.218 33.661  1.00 45.76  ? 174 LEU B C   1 
ATOM   1029 O  O   . LEU A 1 201 ? -25.575 -29.881 33.541  1.00 50.85  ? 174 LEU B O   1 
ATOM   1030 C  CB  . LEU A 1 201 ? -27.775 -29.043 31.715  1.00 40.36  ? 174 LEU B CB  1 
ATOM   1031 C  CG  . LEU A 1 201 ? -28.238 -29.194 30.305  1.00 38.77  ? 174 LEU B CG  1 
ATOM   1032 C  CD1 . LEU A 1 201 ? -28.823 -27.888 29.868  1.00 40.80  ? 174 LEU B CD1 1 
ATOM   1033 C  CD2 . LEU A 1 201 ? -27.051 -29.529 29.427  1.00 45.32  ? 174 LEU B CD2 1 
ATOM   1034 N  N   . SER A 1 202 ? -27.298 -30.411 34.848  1.00 46.58  ? 175 SER B N   1 
ATOM   1035 C  CA  . SER A 1 202 ? -26.480 -30.354 36.069  1.00 46.01  ? 175 SER B CA  1 
ATOM   1036 C  C   . SER A 1 202 ? -25.563 -31.539 36.250  1.00 46.66  ? 175 SER B C   1 
ATOM   1037 O  O   . SER A 1 202 ? -24.633 -31.494 37.053  1.00 48.15  ? 175 SER B O   1 
ATOM   1038 C  CB  . SER A 1 202 ? -27.359 -30.262 37.285  1.00 45.62  ? 175 SER B CB  1 
ATOM   1039 O  OG  . SER A 1 202 ? -27.796 -28.939 37.408  1.00 53.13  ? 175 SER B OG  1 
ATOM   1040 N  N   . ASN A 1 203 ? -25.840 -32.613 35.529  1.00 47.18  ? 176 ASN B N   1 
ATOM   1041 C  CA  . ASN A 1 203 ? -25.062 -33.818 35.655  1.00 47.59  ? 176 ASN B CA  1 
ATOM   1042 C  C   . ASN A 1 203 ? -23.671 -33.627 35.063  1.00 50.29  ? 176 ASN B C   1 
ATOM   1043 O  O   . ASN A 1 203 ? -23.530 -33.564 33.840  1.00 50.15  ? 176 ASN B O   1 
ATOM   1044 C  CB  . ASN A 1 203 ? -25.794 -34.900 34.913  1.00 50.12  ? 176 ASN B CB  1 
ATOM   1045 C  CG  . ASN A 1 203 ? -25.138 -36.247 35.017  1.00 50.41  ? 176 ASN B CG  1 
ATOM   1046 O  OD1 . ASN A 1 203 ? -25.752 -37.214 34.647  1.00 52.58  ? 176 ASN B OD1 1 
ATOM   1047 N  ND2 . ASN A 1 203 ? -23.919 -36.325 35.502  1.00 50.24  ? 176 ASN B ND2 1 
ATOM   1048 N  N   . LYS A 1 204 ? -22.655 -33.554 35.926  1.00 51.43  ? 177 LYS B N   1 
ATOM   1049 C  CA  . LYS A 1 204 ? -21.291 -33.265 35.477  1.00 57.31  ? 177 LYS B CA  1 
ATOM   1050 C  C   . LYS A 1 204 ? -20.497 -34.484 34.937  1.00 59.94  ? 177 LYS B C   1 
ATOM   1051 O  O   . LYS A 1 204 ? -19.432 -34.291 34.359  1.00 65.26  ? 177 LYS B O   1 
ATOM   1052 C  CB  . LYS A 1 204 ? -20.478 -32.544 36.572  1.00 60.82  ? 177 LYS B CB  1 
ATOM   1053 C  CG  . LYS A 1 204 ? -20.870 -31.092 36.927  1.00 63.95  ? 177 LYS B CG  1 
ATOM   1054 C  CD  . LYS A 1 204 ? -21.033 -30.141 35.732  1.00 69.16  ? 177 LYS B CD  1 
ATOM   1055 C  CE  . LYS A 1 204 ? -22.473 -30.146 35.164  1.00 65.91  ? 177 LYS B CE  1 
ATOM   1056 N  NZ  . LYS A 1 204 ? -22.800 -28.950 34.344  1.00 62.18  ? 177 LYS B NZ  1 
ATOM   1057 N  N   . ASN A 1 205 ? -20.966 -35.716 35.134  1.00 55.03  ? 178 ASN B N   1 
ATOM   1058 C  CA  . ASN A 1 205 ? -20.377 -36.841 34.411  1.00 58.63  ? 178 ASN B CA  1 
ATOM   1059 C  C   . ASN A 1 205 ? -20.696 -36.787 32.968  1.00 58.14  ? 178 ASN B C   1 
ATOM   1060 O  O   . ASN A 1 205 ? -19.812 -37.006 32.149  1.00 65.34  ? 178 ASN B O   1 
ATOM   1061 C  CB  . ASN A 1 205 ? -20.819 -38.206 34.931  1.00 65.62  ? 178 ASN B CB  1 
ATOM   1062 C  CG  . ASN A 1 205 ? -20.337 -38.456 36.326  1.00 69.66  ? 178 ASN B CG  1 
ATOM   1063 O  OD1 . ASN A 1 205 ? -19.180 -38.166 36.647  1.00 79.95  ? 178 ASN B OD1 1 
ATOM   1064 N  ND2 . ASN A 1 205 ? -21.219 -38.957 37.180  1.00 72.34  ? 178 ASN B ND2 1 
ATOM   1065 N  N   . GLN A 1 206 ? -21.950 -36.515 32.630  1.00 55.75  ? 179 GLN B N   1 
ATOM   1066 C  CA  . GLN A 1 206 ? -22.284 -36.387 31.227  1.00 54.80  ? 179 GLN B CA  1 
ATOM   1067 C  C   . GLN A 1 206 ? -21.825 -35.025 30.623  1.00 54.40  ? 179 GLN B C   1 
ATOM   1068 O  O   . GLN A 1 206 ? -21.357 -34.981 29.503  1.00 56.76  ? 179 GLN B O   1 
ATOM   1069 C  CB  . GLN A 1 206 ? -23.762 -36.641 30.991  1.00 56.84  ? 179 GLN B CB  1 
ATOM   1070 C  CG  . GLN A 1 206 ? -24.117 -36.412 29.533  1.00 67.78  ? 179 GLN B CG  1 
ATOM   1071 C  CD  . GLN A 1 206 ? -25.092 -37.388 28.909  1.00 76.08  ? 179 GLN B CD  1 
ATOM   1072 O  OE1 . GLN A 1 206 ? -25.698 -37.081 27.868  1.00 86.31  ? 179 GLN B OE1 1 
ATOM   1073 N  NE2 . GLN A 1 206 ? -25.215 -38.576 29.490  1.00 83.69  ? 179 GLN B NE2 1 
ATOM   1074 N  N   . PHE A 1 207 ? -21.956 -33.924 31.350  1.00 53.64  ? 180 PHE B N   1 
ATOM   1075 C  CA  . PHE A 1 207 ? -21.672 -32.606 30.786  1.00 50.81  ? 180 PHE B CA  1 
ATOM   1076 C  C   . PHE A 1 207 ? -20.514 -31.942 31.538  1.00 49.56  ? 180 PHE B C   1 
ATOM   1077 O  O   . PHE A 1 207 ? -20.686 -31.100 32.396  1.00 55.20  ? 180 PHE B O   1 
ATOM   1078 C  CB  . PHE A 1 207 ? -22.925 -31.752 30.770  1.00 46.85  ? 180 PHE B CB  1 
ATOM   1079 C  CG  . PHE A 1 207 ? -24.122 -32.445 30.185  1.00 44.13  ? 180 PHE B CG  1 
ATOM   1080 C  CD1 . PHE A 1 207 ? -24.226 -32.639 28.811  1.00 44.55  ? 180 PHE B CD1 1 
ATOM   1081 C  CD2 . PHE A 1 207 ? -25.177 -32.861 30.988  1.00 41.63  ? 180 PHE B CD2 1 
ATOM   1082 C  CE1 . PHE A 1 207 ? -25.346 -33.281 28.250  1.00 40.17  ? 180 PHE B CE1 1 
ATOM   1083 C  CE2 . PHE A 1 207 ? -26.289 -33.496 30.434  1.00 38.69  ? 180 PHE B CE2 1 
ATOM   1084 C  CZ  . PHE A 1 207 ? -26.364 -33.722 29.070  1.00 37.42  ? 180 PHE B CZ  1 
ATOM   1085 N  N   . LYS A 1 208 ? -19.320 -32.364 31.158  1.00 51.92  ? 181 LYS B N   1 
ATOM   1086 C  CA  . LYS A 1 208 ? -18.051 -31.936 31.737  1.00 46.04  ? 181 LYS B CA  1 
ATOM   1087 C  C   . LYS A 1 208 ? -17.741 -30.465 31.632  1.00 44.50  ? 181 LYS B C   1 
ATOM   1088 O  O   . LYS A 1 208 ? -17.070 -29.948 32.512  1.00 49.11  ? 181 LYS B O   1 
ATOM   1089 C  CB  . LYS A 1 208 ? -16.927 -32.704 31.044  1.00 47.99  ? 181 LYS B CB  1 
ATOM   1090 C  CG  . LYS A 1 208 ? -16.889 -34.156 31.454  1.00 52.01  ? 181 LYS B CG  1 
ATOM   1091 C  CD  . LYS A 1 208 ? -16.145 -34.986 30.449  1.00 66.10  ? 181 LYS B CD  1 
ATOM   1092 C  CE  . LYS A 1 208 ? -16.162 -36.451 30.876  1.00 80.89  ? 181 LYS B CE  1 
ATOM   1093 N  NZ  . LYS A 1 208 ? -15.086 -37.197 30.150  1.00 90.75  ? 181 LYS B NZ  1 
ATOM   1094 N  N   . SER A 1 209 ? -18.188 -29.780 30.575  1.00 40.01  ? 182 SER B N   1 
ATOM   1095 C  CA  . SER A 1 209 ? -17.803 -28.374 30.415  1.00 39.26  ? 182 SER B CA  1 
ATOM   1096 C  C   . SER A 1 209 ? -18.965 -27.371 30.423  1.00 37.95  ? 182 SER B C   1 
ATOM   1097 O  O   . SER A 1 209 ? -18.847 -26.253 29.915  1.00 38.26  ? 182 SER B O   1 
ATOM   1098 C  CB  . SER A 1 209 ? -16.878 -28.166 29.192  1.00 37.29  ? 182 SER B CB  1 
ATOM   1099 O  OG  . SER A 1 209 ? -17.562 -28.193 27.965  1.00 42.79  ? 182 SER B OG  1 
ATOM   1100 N  N   . PHE A 1 210 ? -20.055 -27.740 31.060  1.00 36.57  ? 183 PHE B N   1 
ATOM   1101 C  CA  . PHE A 1 210 ? -21.261 -26.943 30.966  1.00 38.47  ? 183 PHE B CA  1 
ATOM   1102 C  C   . PHE A 1 210 ? -21.504 -26.152 32.242  1.00 36.51  ? 183 PHE B C   1 
ATOM   1103 O  O   . PHE A 1 210 ? -21.503 -26.709 33.319  1.00 42.74  ? 183 PHE B O   1 
ATOM   1104 C  CB  . PHE A 1 210 ? -22.484 -27.824 30.684  1.00 37.98  ? 183 PHE B CB  1 
ATOM   1105 C  CG  . PHE A 1 210 ? -23.760 -27.046 30.575  1.00 39.98  ? 183 PHE B CG  1 
ATOM   1106 C  CD1 . PHE A 1 210 ? -24.593 -26.898 31.659  1.00 36.77  ? 183 PHE B CD1 1 
ATOM   1107 C  CD2 . PHE A 1 210 ? -24.112 -26.436 29.382  1.00 43.03  ? 183 PHE B CD2 1 
ATOM   1108 C  CE1 . PHE A 1 210 ? -25.776 -26.180 31.557  1.00 37.83  ? 183 PHE B CE1 1 
ATOM   1109 C  CE2 . PHE A 1 210 ? -25.299 -25.717 29.280  1.00 43.41  ? 183 PHE B CE2 1 
ATOM   1110 C  CZ  . PHE A 1 210 ? -26.125 -25.597 30.379  1.00 40.68  ? 183 PHE B CZ  1 
ATOM   1111 N  N   . LEU A 1 211 ? -21.701 -24.853 32.098  1.00 36.27  ? 184 LEU B N   1 
ATOM   1112 C  CA  . LEU A 1 211 ? -22.192 -24.023 33.167  1.00 39.30  ? 184 LEU B CA  1 
ATOM   1113 C  C   . LEU A 1 211 ? -23.263 -23.125 32.635  1.00 36.69  ? 184 LEU B C   1 
ATOM   1114 O  O   . LEU A 1 211 ? -23.456 -23.013 31.454  1.00 39.48  ? 184 LEU B O   1 
ATOM   1115 C  CB  . LEU A 1 211 ? -21.102 -23.137 33.732  1.00 44.95  ? 184 LEU B CB  1 
ATOM   1116 C  CG  . LEU A 1 211 ? -19.751 -23.781 33.992  1.00 49.72  ? 184 LEU B CG  1 
ATOM   1117 C  CD1 . LEU A 1 211 ? -18.805 -23.433 32.861  1.00 48.98  ? 184 LEU B CD1 1 
ATOM   1118 C  CD2 . LEU A 1 211 ? -19.225 -23.286 35.331  1.00 54.59  ? 184 LEU B CD2 1 
ATOM   1119 N  N   . ARG A 1 212 ? -23.953 -22.463 33.526  1.00 38.64  ? 185 ARG B N   1 
ATOM   1120 C  CA  . ARG A 1 212 ? -25.002 -21.598 33.117  1.00 43.65  ? 185 ARG B CA  1 
ATOM   1121 C  C   . ARG A 1 212 ? -25.188 -20.461 34.080  1.00 46.27  ? 185 ARG B C   1 
ATOM   1122 O  O   . ARG A 1 212 ? -24.993 -20.625 35.293  1.00 43.08  ? 185 ARG B O   1 
ATOM   1123 C  CB  . ARG A 1 212 ? -26.287 -22.395 32.998  1.00 45.14  ? 185 ARG B CB  1 
ATOM   1124 C  CG  . ARG A 1 212 ? -26.690 -23.224 34.201  1.00 41.12  ? 185 ARG B CG  1 
ATOM   1125 C  CD  . ARG A 1 212 ? -27.965 -23.983 33.831  1.00 40.83  ? 185 ARG B CD  1 
ATOM   1126 N  NE  . ARG A 1 212 ? -28.143 -25.202 34.606  1.00 40.50  ? 185 ARG B NE  1 
ATOM   1127 C  CZ  . ARG A 1 212 ? -28.984 -26.193 34.324  1.00 38.26  ? 185 ARG B CZ  1 
ATOM   1128 N  NH1 . ARG A 1 212 ? -29.788 -26.164 33.274  1.00 40.60  ? 185 ARG B NH1 1 
ATOM   1129 N  NH2 . ARG A 1 212 ? -29.019 -27.243 35.111  1.00 39.50  ? 185 ARG B NH2 1 
ATOM   1130 N  N   . THR A 1 213 ? -25.584 -19.318 33.528  1.00 47.61  ? 186 THR B N   1 
ATOM   1131 C  CA  . THR A 1 213 ? -25.915 -18.148 34.342  1.00 51.70  ? 186 THR B CA  1 
ATOM   1132 C  C   . THR A 1 213 ? -27.394 -18.067 34.678  1.00 52.28  ? 186 THR B C   1 
ATOM   1133 O  O   . THR A 1 213 ? -27.891 -16.991 34.974  1.00 57.80  ? 186 THR B O   1 
ATOM   1134 C  CB  . THR A 1 213 ? -25.536 -16.869 33.608  1.00 52.90  ? 186 THR B CB  1 
ATOM   1135 O  OG1 . THR A 1 213 ? -26.110 -16.887 32.291  1.00 49.85  ? 186 THR B OG1 1 
ATOM   1136 C  CG2 . THR A 1 213 ? -24.049 -16.764 33.505  1.00 56.14  ? 186 THR B CG2 1 
ATOM   1137 N  N   . ILE A 1 214 ? -28.095 -19.199 34.618  1.00 53.65  ? 187 ILE B N   1 
ATOM   1138 C  CA  . ILE A 1 214 ? -29.535 -19.261 34.912  1.00 50.94  ? 187 ILE B CA  1 
ATOM   1139 C  C   . ILE A 1 214 ? -29.755 -20.415 35.871  1.00 48.34  ? 187 ILE B C   1 
ATOM   1140 O  O   . ILE A 1 214 ? -29.023 -21.405 35.821  1.00 58.76  ? 187 ILE B O   1 
ATOM   1141 C  CB  . ILE A 1 214 ? -30.382 -19.455 33.623  1.00 54.82  ? 187 ILE B CB  1 
ATOM   1142 C  CG1 . ILE A 1 214 ? -31.868 -19.283 33.918  1.00 55.15  ? 187 ILE B CG1 1 
ATOM   1143 C  CG2 . ILE A 1 214 ? -30.178 -20.828 32.993  1.00 54.08  ? 187 ILE B CG2 1 
ATOM   1144 C  CD1 . ILE A 1 214 ? -32.766 -19.178 32.696  1.00 55.36  ? 187 ILE B CD1 1 
ATOM   1145 N  N   . PRO A 1 215 ? -30.712 -20.286 36.792  1.00 45.41  ? 188 PRO B N   1 
ATOM   1146 C  CA  . PRO A 1 215 ? -31.009 -21.403 37.721  1.00 44.81  ? 188 PRO B CA  1 
ATOM   1147 C  C   . PRO A 1 215 ? -31.763 -22.532 37.064  1.00 43.33  ? 188 PRO B C   1 
ATOM   1148 O  O   . PRO A 1 215 ? -32.590 -22.314 36.187  1.00 49.74  ? 188 PRO B O   1 
ATOM   1149 C  CB  . PRO A 1 215 ? -31.939 -20.805 38.756  1.00 43.66  ? 188 PRO B CB  1 
ATOM   1150 C  CG  . PRO A 1 215 ? -32.110 -19.362 38.402  1.00 45.41  ? 188 PRO B CG  1 
ATOM   1151 C  CD  . PRO A 1 215 ? -31.405 -19.040 37.142  1.00 45.88  ? 188 PRO B CD  1 
ATOM   1152 N  N   . ASN A 1 216 ? -31.498 -23.732 37.517  1.00 46.13  ? 189 ASN B N   1 
ATOM   1153 C  CA  . ASN A 1 216 ? -32.164 -24.880 36.989  1.00 51.18  ? 189 ASN B CA  1 
ATOM   1154 C  C   . ASN A 1 216 ? -33.607 -25.003 37.513  1.00 50.86  ? 189 ASN B C   1 
ATOM   1155 O  O   . ASN A 1 216 ? -33.995 -24.418 38.539  1.00 42.01  ? 189 ASN B O   1 
ATOM   1156 C  CB  . ASN A 1 216 ? -31.286 -26.134 37.187  1.00 58.79  ? 189 ASN B CB  1 
ATOM   1157 C  CG  . ASN A 1 216 ? -31.709 -27.024 38.340  1.00 61.46  ? 189 ASN B CG  1 
ATOM   1158 O  OD1 . ASN A 1 216 ? -32.857 -27.038 38.755  1.00 67.43  ? 189 ASN B OD1 1 
ATOM   1159 N  ND2 . ASN A 1 216 ? -30.772 -27.846 38.808  1.00 65.11  ? 189 ASN B ND2 1 
ATOM   1160 N  N   . ASP A 1 217 ? -34.388 -25.777 36.768  1.00 52.29  ? 190 ASP B N   1 
ATOM   1161 C  CA  . ASP A 1 217 ? -35.827 -25.849 36.947  1.00 52.65  ? 190 ASP B CA  1 
ATOM   1162 C  C   . ASP A 1 217 ? -36.337 -26.694 38.105  1.00 52.10  ? 190 ASP B C   1 
ATOM   1163 O  O   . ASP A 1 217 ? -37.518 -26.694 38.361  1.00 57.96  ? 190 ASP B O   1 
ATOM   1164 C  CB  . ASP A 1 217 ? -36.474 -26.307 35.647  1.00 52.93  ? 190 ASP B CB  1 
ATOM   1165 C  CG  . ASP A 1 217 ? -36.447 -25.224 34.580  1.00 56.26  ? 190 ASP B CG  1 
ATOM   1166 O  OD1 . ASP A 1 217 ? -36.554 -24.011 34.910  1.00 58.43  ? 190 ASP B OD1 1 
ATOM   1167 O  OD2 . ASP A 1 217 ? -36.299 -25.595 33.404  1.00 62.11  ? 190 ASP B OD2 1 
ATOM   1168 N  N   . GLU A 1 218 ? -35.477 -27.398 38.819  1.00 50.24  ? 191 GLU B N   1 
ATOM   1169 C  CA  . GLU A 1 218 ? -35.916 -28.001 40.059  1.00 50.39  ? 191 GLU B CA  1 
ATOM   1170 C  C   . GLU A 1 218 ? -36.599 -26.955 40.901  1.00 53.25  ? 191 GLU B C   1 
ATOM   1171 O  O   . GLU A 1 218 ? -37.615 -27.255 41.534  1.00 54.85  ? 191 GLU B O   1 
ATOM   1172 C  CB  . GLU A 1 218 ? -34.758 -28.596 40.856  1.00 54.25  ? 191 GLU B CB  1 
ATOM   1173 C  CG  . GLU A 1 218 ? -34.057 -29.755 40.177  1.00 59.21  ? 191 GLU B CG  1 
ATOM   1174 C  CD  . GLU A 1 218 ? -34.956 -30.974 39.969  1.00 59.98  ? 191 GLU B CD  1 
ATOM   1175 O  OE1 . GLU A 1 218 ? -34.751 -31.957 40.694  1.00 57.51  ? 191 GLU B OE1 1 
ATOM   1176 O  OE2 . GLU A 1 218 ? -35.848 -30.971 39.075  1.00 68.95  ? 191 GLU B OE2 1 
ATOM   1177 N  N   . HIS A 1 219 ? -36.063 -25.732 40.916  1.00 48.18  ? 192 HIS B N   1 
ATOM   1178 C  CA  . HIS A 1 219 ? -36.584 -24.717 41.818  1.00 51.56  ? 192 HIS B CA  1 
ATOM   1179 C  C   . HIS A 1 219 ? -37.909 -24.140 41.345  1.00 51.04  ? 192 HIS B C   1 
ATOM   1180 O  O   . HIS A 1 219 ? -38.848 -23.940 42.120  1.00 51.56  ? 192 HIS B O   1 
ATOM   1181 C  CB  . HIS A 1 219 ? -35.568 -23.605 41.988  1.00 57.60  ? 192 HIS B CB  1 
ATOM   1182 C  CG  . HIS A 1 219 ? -34.231 -24.098 42.423  1.00 62.71  ? 192 HIS B CG  1 
ATOM   1183 N  ND1 . HIS A 1 219 ? -34.030 -24.705 43.643  1.00 65.72  ? 192 HIS B ND1 1 
ATOM   1184 C  CD2 . HIS A 1 219 ? -33.035 -24.107 41.792  1.00 65.71  ? 192 HIS B CD2 1 
ATOM   1185 C  CE1 . HIS A 1 219 ? -32.762 -25.049 43.755  1.00 62.95  ? 192 HIS B CE1 1 
ATOM   1186 N  NE2 . HIS A 1 219 ? -32.140 -24.709 42.640  1.00 69.80  ? 192 HIS B NE2 1 
ATOM   1187 N  N   . GLN A 1 220 ? -37.976 -23.909 40.049  1.00 52.36  ? 193 GLN B N   1 
ATOM   1188 C  CA  . GLN A 1 220 ? -39.146 -23.316 39.432  1.00 53.02  ? 193 GLN B CA  1 
ATOM   1189 C  C   . GLN A 1 220 ? -40.395 -24.180 39.635  1.00 47.51  ? 193 GLN B C   1 
ATOM   1190 O  O   . GLN A 1 220 ? -41.467 -23.678 39.916  1.00 47.57  ? 193 GLN B O   1 
ATOM   1191 C  CB  . GLN A 1 220 ? -38.883 -23.126 37.937  1.00 51.88  ? 193 GLN B CB  1 
ATOM   1192 C  CG  . GLN A 1 220 ? -39.608 -21.940 37.381  1.00 52.13  ? 193 GLN B CG  1 
ATOM   1193 C  CD  . GLN A 1 220 ? -39.818 -22.017 35.905  1.00 53.46  ? 193 GLN B CD  1 
ATOM   1194 O  OE1 . GLN A 1 220 ? -38.964 -22.483 35.135  1.00 64.98  ? 193 GLN B OE1 1 
ATOM   1195 N  NE2 . GLN A 1 220 ? -40.962 -21.563 35.490  1.00 49.98  ? 193 GLN B NE2 1 
ATOM   1196 N  N   . ALA A 1 221 ? -40.213 -25.480 39.476  1.00 44.32  ? 194 ALA B N   1 
ATOM   1197 C  CA  . ALA A 1 221 ? -41.254 -26.476 39.631  1.00 44.31  ? 194 ALA B CA  1 
ATOM   1198 C  C   . ALA A 1 221 ? -41.709 -26.580 41.066  1.00 42.28  ? 194 ALA B C   1 
ATOM   1199 O  O   . ALA A 1 221 ? -42.869 -26.835 41.333  1.00 50.80  ? 194 ALA B O   1 
ATOM   1200 C  CB  . ALA A 1 221 ? -40.741 -27.853 39.169  1.00 45.33  ? 194 ALA B CB  1 
ATOM   1201 N  N   . THR A 1 222 ? -40.788 -26.464 41.989  1.00 40.62  ? 195 THR B N   1 
ATOM   1202 C  CA  . THR A 1 222 ? -41.148 -26.412 43.377  1.00 44.92  ? 195 THR B CA  1 
ATOM   1203 C  C   . THR A 1 222 ? -41.950 -25.110 43.658  1.00 45.72  ? 195 THR B C   1 
ATOM   1204 O  O   . THR A 1 222 ? -42.932 -25.139 44.380  1.00 43.63  ? 195 THR B O   1 
ATOM   1205 C  CB  . THR A 1 222 ? -39.889 -26.462 44.270  1.00 45.16  ? 195 THR B CB  1 
ATOM   1206 O  OG1 . THR A 1 222 ? -39.124 -27.631 43.966  1.00 49.23  ? 195 THR B OG1 1 
ATOM   1207 C  CG2 . THR A 1 222 ? -40.286 -26.538 45.697  1.00 46.22  ? 195 THR B CG2 1 
ATOM   1208 N  N   . ALA A 1 223 ? -41.526 -23.990 43.075  1.00 44.57  ? 196 ALA B N   1 
ATOM   1209 C  CA  . ALA A 1 223 ? -42.239 -22.723 43.232  1.00 46.19  ? 196 ALA B CA  1 
ATOM   1210 C  C   . ALA A 1 223 ? -43.662 -22.838 42.713  1.00 44.58  ? 196 ALA B C   1 
ATOM   1211 O  O   . ALA A 1 223 ? -44.600 -22.445 43.402  1.00 44.63  ? 196 ALA B O   1 
ATOM   1212 C  CB  . ALA A 1 223 ? -41.505 -21.586 42.525  1.00 46.13  ? 196 ALA B CB  1 
ATOM   1213 N  N   . MET A 1 224 ? -43.832 -23.396 41.518  1.00 47.06  ? 197 MET B N   1 
ATOM   1214 C  CA  . MET A 1 224 ? -45.174 -23.648 40.995  1.00 50.75  ? 197 MET B CA  1 
ATOM   1215 C  C   . MET A 1 224 ? -46.069 -24.406 42.007  1.00 49.74  ? 197 MET B C   1 
ATOM   1216 O  O   . MET A 1 224 ? -47.211 -24.027 42.272  1.00 45.79  ? 197 MET B O   1 
ATOM   1217 C  CB  . MET A 1 224 ? -45.092 -24.392 39.683  1.00 56.67  ? 197 MET B CB  1 
ATOM   1218 C  CG  . MET A 1 224 ? -45.168 -23.502 38.453  1.00 66.45  ? 197 MET B CG  1 
ATOM   1219 S  SD  . MET A 1 224 ? -44.426 -24.311 36.996  1.00 83.55  ? 197 MET B SD  1 
ATOM   1220 C  CE  . MET A 1 224 ? -44.895 -23.138 35.725  1.00 98.10  ? 197 MET B CE  1 
ATOM   1221 N  N   . ALA A 1 225 ? -45.550 -25.465 42.602  1.00 49.17  ? 198 ALA B N   1 
ATOM   1222 C  CA  . ALA A 1 225 ? -46.343 -26.186 43.582  1.00 49.37  ? 198 ALA B CA  1 
ATOM   1223 C  C   . ALA A 1 225 ? -46.639 -25.336 44.834  1.00 50.78  ? 198 ALA B C   1 
ATOM   1224 O  O   . ALA A 1 225 ? -47.724 -25.480 45.432  1.00 45.86  ? 198 ALA B O   1 
ATOM   1225 C  CB  . ALA A 1 225 ? -45.674 -27.488 43.954  1.00 47.06  ? 198 ALA B CB  1 
ATOM   1226 N  N   . ASP A 1 226 ? -45.690 -24.470 45.216  1.00 46.34  ? 199 ASP B N   1 
ATOM   1227 C  CA  . ASP A 1 226 ? -45.874 -23.564 46.349  1.00 51.35  ? 199 ASP B CA  1 
ATOM   1228 C  C   . ASP A 1 226 ? -46.933 -22.494 46.084  1.00 53.38  ? 199 ASP B C   1 
ATOM   1229 O  O   . ASP A 1 226 ? -47.676 -22.145 46.990  1.00 56.86  ? 199 ASP B O   1 
ATOM   1230 C  CB  . ASP A 1 226 ? -44.563 -22.874 46.764  1.00 53.85  ? 199 ASP B CB  1 
ATOM   1231 C  CG  . ASP A 1 226 ? -43.650 -23.776 47.574  1.00 57.25  ? 199 ASP B CG  1 
ATOM   1232 O  OD1 . ASP A 1 226 ? -44.071 -24.911 47.895  1.00 54.81  ? 199 ASP B OD1 1 
ATOM   1233 O  OD2 . ASP A 1 226 ? -42.504 -23.357 47.887  1.00 66.00  ? 199 ASP B OD2 1 
ATOM   1234 N  N   . ILE A 1 227 ? -46.988 -21.956 44.870  1.00 54.41  ? 200 ILE B N   1 
ATOM   1235 C  CA  . ILE A 1 227 ? -48.056 -21.012 44.501  1.00 55.40  ? 200 ILE B CA  1 
ATOM   1236 C  C   . ILE A 1 227 ? -49.431 -21.661 44.641  1.00 54.94  ? 200 ILE B C   1 
ATOM   1237 O  O   . ILE A 1 227 ? -50.360 -21.090 45.252  1.00 59.93  ? 200 ILE B O   1 
ATOM   1238 C  CB  . ILE A 1 227 ? -47.934 -20.516 43.049  1.00 60.53  ? 200 ILE B CB  1 
ATOM   1239 C  CG1 . ILE A 1 227 ? -46.730 -19.627 42.881  1.00 63.40  ? 200 ILE B CG1 1 
ATOM   1240 C  CG2 . ILE A 1 227 ? -49.133 -19.668 42.656  1.00 69.45  ? 200 ILE B CG2 1 
ATOM   1241 C  CD1 . ILE A 1 227 ? -46.744 -18.835 41.590  1.00 65.27  ? 200 ILE B CD1 1 
ATOM   1242 N  N   . ILE A 1 228 ? -49.571 -22.843 44.064  1.00 48.70  ? 201 ILE B N   1 
ATOM   1243 C  CA  . ILE A 1 228 ? -50.834 -23.553 44.152  1.00 49.77  ? 201 ILE B CA  1 
ATOM   1244 C  C   . ILE A 1 228 ? -51.216 -23.756 45.625  1.00 45.40  ? 201 ILE B C   1 
ATOM   1245 O  O   . ILE A 1 228 ? -52.297 -23.418 46.017  1.00 48.81  ? 201 ILE B O   1 
ATOM   1246 C  CB  . ILE A 1 228 ? -50.793 -24.878 43.362  1.00 47.28  ? 201 ILE B CB  1 
ATOM   1247 C  CG1 . ILE A 1 228 ? -50.639 -24.590 41.878  1.00 51.05  ? 201 ILE B CG1 1 
ATOM   1248 C  CG2 . ILE A 1 228 ? -52.074 -25.665 43.532  1.00 47.50  ? 201 ILE B CG2 1 
ATOM   1249 C  CD1 . ILE A 1 228 ? -50.169 -25.781 41.066  1.00 54.28  ? 201 ILE B CD1 1 
ATOM   1250 N  N   . GLU A 1 229 ? -50.316 -24.268 46.444  1.00 46.80  ? 202 GLU B N   1 
ATOM   1251 C  CA  . GLU A 1 229 ? -50.595 -24.442 47.885  1.00 47.89  ? 202 GLU B CA  1 
ATOM   1252 C  C   . GLU A 1 229 ? -50.941 -23.098 48.551  1.00 45.85  ? 202 GLU B C   1 
ATOM   1253 O  O   . GLU A 1 229 ? -51.782 -23.045 49.412  1.00 51.59  ? 202 GLU B O   1 
ATOM   1254 C  CB  . GLU A 1 229 ? -49.383 -25.085 48.572  1.00 50.39  ? 202 GLU B CB  1 
ATOM   1255 C  CG  . GLU A 1 229 ? -49.551 -25.459 50.021  1.00 55.16  ? 202 GLU B CG  1 
ATOM   1256 C  CD  . GLU A 1 229 ? -48.289 -26.004 50.688  1.00 59.58  ? 202 GLU B CD  1 
ATOM   1257 O  OE1 . GLU A 1 229 ? -48.436 -26.735 51.679  1.00 73.77  ? 202 GLU B OE1 1 
ATOM   1258 O  OE2 . GLU A 1 229 ? -47.154 -25.724 50.265  1.00 66.31  ? 202 GLU B OE2 1 
ATOM   1259 N  N   . TYR A 1 230 ? -50.299 -22.019 48.132  1.00 48.35  ? 203 TYR B N   1 
ATOM   1260 C  CA  . TYR A 1 230 ? -50.484 -20.694 48.714  1.00 50.53  ? 203 TYR B CA  1 
ATOM   1261 C  C   . TYR A 1 230 ? -51.925 -20.259 48.647  1.00 49.92  ? 203 TYR B C   1 
ATOM   1262 O  O   . TYR A 1 230 ? -52.449 -19.719 49.615  1.00 52.69  ? 203 TYR B O   1 
ATOM   1263 C  CB  . TYR A 1 230 ? -49.622 -19.671 47.964  1.00 52.29  ? 203 TYR B CB  1 
ATOM   1264 C  CG  . TYR A 1 230 ? -49.725 -18.241 48.483  1.00 54.30  ? 203 TYR B CG  1 
ATOM   1265 C  CD1 . TYR A 1 230 ? -48.974 -17.817 49.592  1.00 51.19  ? 203 TYR B CD1 1 
ATOM   1266 C  CD2 . TYR A 1 230 ? -50.523 -17.311 47.836  1.00 50.31  ? 203 TYR B CD2 1 
ATOM   1267 C  CE1 . TYR A 1 230 ? -49.059 -16.531 50.055  1.00 51.56  ? 203 TYR B CE1 1 
ATOM   1268 C  CE2 . TYR A 1 230 ? -50.607 -16.020 48.297  1.00 55.00  ? 203 TYR B CE2 1 
ATOM   1269 C  CZ  . TYR A 1 230 ? -49.876 -15.635 49.403  1.00 54.51  ? 203 TYR B CZ  1 
ATOM   1270 O  OH  . TYR A 1 230 ? -49.956 -14.333 49.833  1.00 57.36  ? 203 TYR B OH  1 
ATOM   1271 N  N   . PHE A 1 231 ? -52.544 -20.517 47.496  1.00 48.61  ? 204 PHE B N   1 
ATOM   1272 C  CA  . PHE A 1 231 ? -53.940 -20.194 47.244  1.00 47.58  ? 204 PHE B CA  1 
ATOM   1273 C  C   . PHE A 1 231 ? -54.881 -21.286 47.688  1.00 48.65  ? 204 PHE B C   1 
ATOM   1274 O  O   . PHE A 1 231 ? -56.076 -21.225 47.423  1.00 51.34  ? 204 PHE B O   1 
ATOM   1275 C  CB  . PHE A 1 231 ? -54.166 -19.926 45.753  1.00 49.07  ? 204 PHE B CB  1 
ATOM   1276 C  CG  . PHE A 1 231 ? -53.633 -18.603 45.318  1.00 54.65  ? 204 PHE B CG  1 
ATOM   1277 C  CD1 . PHE A 1 231 ? -54.315 -17.437 45.647  1.00 57.78  ? 204 PHE B CD1 1 
ATOM   1278 C  CD2 . PHE A 1 231 ? -52.431 -18.507 44.644  1.00 55.82  ? 204 PHE B CD2 1 
ATOM   1279 C  CE1 . PHE A 1 231 ? -53.833 -16.205 45.273  1.00 57.64  ? 204 PHE B CE1 1 
ATOM   1280 C  CE2 . PHE A 1 231 ? -51.939 -17.273 44.280  1.00 59.24  ? 204 PHE B CE2 1 
ATOM   1281 C  CZ  . PHE A 1 231 ? -52.639 -16.118 44.590  1.00 56.26  ? 204 PHE B CZ  1 
ATOM   1282 N  N   . ARG A 1 232 ? -54.351 -22.307 48.348  1.00 49.79  ? 205 ARG B N   1 
ATOM   1283 C  CA  . ARG A 1 232 ? -55.171 -23.385 48.848  1.00 46.47  ? 205 ARG B CA  1 
ATOM   1284 C  C   . ARG A 1 232 ? -55.912 -24.064 47.709  1.00 46.07  ? 205 ARG B C   1 
ATOM   1285 O  O   . ARG A 1 232 ? -56.989 -24.584 47.917  1.00 49.54  ? 205 ARG B O   1 
ATOM   1286 C  CB  . ARG A 1 232 ? -56.174 -22.848 49.878  1.00 46.92  ? 205 ARG B CB  1 
ATOM   1287 C  CG  . ARG A 1 232 ? -55.682 -21.702 50.750  1.00 48.05  ? 205 ARG B CG  1 
ATOM   1288 C  CD  . ARG A 1 232 ? -54.852 -22.174 51.917  1.00 53.84  ? 205 ARG B CD  1 
ATOM   1289 N  NE  . ARG A 1 232 ? -54.382 -21.066 52.764  1.00 61.79  ? 205 ARG B NE  1 
ATOM   1290 C  CZ  . ARG A 1 232 ? -53.685 -21.207 53.903  1.00 64.36  ? 205 ARG B CZ  1 
ATOM   1291 N  NH1 . ARG A 1 232 ? -53.378 -22.414 54.359  1.00 68.42  ? 205 ARG B NH1 1 
ATOM   1292 N  NH2 . ARG A 1 232 ? -53.302 -20.149 54.611  1.00 59.91  ? 205 ARG B NH2 1 
ATOM   1293 N  N   . TRP A 1 233 ? -55.358 -24.051 46.500  1.00 48.46  ? 206 TRP B N   1 
ATOM   1294 C  CA  . TRP A 1 233 ? -55.939 -24.829 45.407  1.00 48.44  ? 206 TRP B CA  1 
ATOM   1295 C  C   . TRP A 1 233 ? -55.527 -26.276 45.565  1.00 46.48  ? 206 TRP B C   1 
ATOM   1296 O  O   . TRP A 1 233 ? -54.550 -26.561 46.218  1.00 48.02  ? 206 TRP B O   1 
ATOM   1297 C  CB  . TRP A 1 233 ? -55.465 -24.318 44.069  1.00 48.91  ? 206 TRP B CB  1 
ATOM   1298 C  CG  . TRP A 1 233 ? -55.836 -22.924 43.800  1.00 51.97  ? 206 TRP B CG  1 
ATOM   1299 C  CD1 . TRP A 1 233 ? -56.872 -22.206 44.343  1.00 49.49  ? 206 TRP B CD1 1 
ATOM   1300 C  CD2 . TRP A 1 233 ? -55.185 -22.057 42.892  1.00 49.28  ? 206 TRP B CD2 1 
ATOM   1301 N  NE1 . TRP A 1 233 ? -56.881 -20.935 43.828  1.00 42.74  ? 206 TRP B NE1 1 
ATOM   1302 C  CE2 . TRP A 1 233 ? -55.849 -20.819 42.943  1.00 47.78  ? 206 TRP B CE2 1 
ATOM   1303 C  CE3 . TRP A 1 233 ? -54.087 -22.195 42.067  1.00 43.90  ? 206 TRP B CE3 1 
ATOM   1304 C  CZ2 . TRP A 1 233 ? -55.462 -19.751 42.182  1.00 49.94  ? 206 TRP B CZ2 1 
ATOM   1305 C  CZ3 . TRP A 1 233 ? -53.701 -21.132 41.325  1.00 46.07  ? 206 TRP B CZ3 1 
ATOM   1306 C  CH2 . TRP A 1 233 ? -54.383 -19.930 41.377  1.00 50.20  ? 206 TRP B CH2 1 
ATOM   1307 N  N   . ASN A 1 234 ? -56.283 -27.192 44.989  1.00 50.94  ? 207 ASN B N   1 
ATOM   1308 C  CA  . ASN A 1 234 ? -55.965 -28.610 45.119  1.00 51.08  ? 207 ASN B CA  1 
ATOM   1309 C  C   . ASN A 1 234 ? -56.319 -29.458 43.912  1.00 51.93  ? 207 ASN B C   1 
ATOM   1310 O  O   . ASN A 1 234 ? -56.409 -30.670 44.029  1.00 49.82  ? 207 ASN B O   1 
ATOM   1311 C  CB  . ASN A 1 234 ? -56.742 -29.153 46.279  1.00 50.18  ? 207 ASN B CB  1 
ATOM   1312 C  CG  . ASN A 1 234 ? -58.208 -29.184 45.994  1.00 53.67  ? 207 ASN B CG  1 
ATOM   1313 O  OD1 . ASN A 1 234 ? -58.641 -28.776 44.910  1.00 54.50  ? 207 ASN B OD1 1 
ATOM   1314 N  ND2 . ASN A 1 234 ? -58.996 -29.622 46.972  1.00 57.86  ? 207 ASN B ND2 1 
ATOM   1315 N  N   . TRP A 1 235 ? -56.526 -28.814 42.768  1.00 53.39  ? 208 TRP B N   1 
ATOM   1316 C  CA  . TRP A 1 235 ? -57.082 -29.466 41.606  1.00 53.75  ? 208 TRP B CA  1 
ATOM   1317 C  C   . TRP A 1 235 ? -56.531 -28.727 40.411  1.00 58.32  ? 208 TRP B C   1 
ATOM   1318 O  O   . TRP A 1 235 ? -56.869 -27.534 40.226  1.00 53.29  ? 208 TRP B O   1 
ATOM   1319 C  CB  . TRP A 1 235 ? -58.592 -29.321 41.650  1.00 54.34  ? 208 TRP B CB  1 
ATOM   1320 C  CG  . TRP A 1 235 ? -59.368 -30.019 40.597  1.00 57.43  ? 208 TRP B CG  1 
ATOM   1321 C  CD1 . TRP A 1 235 ? -60.238 -29.449 39.702  1.00 60.63  ? 208 TRP B CD1 1 
ATOM   1322 C  CD2 . TRP A 1 235 ? -59.409 -31.421 40.358  1.00 56.06  ? 208 TRP B CD2 1 
ATOM   1323 N  NE1 . TRP A 1 235 ? -60.788 -30.416 38.901  1.00 59.22  ? 208 TRP B NE1 1 
ATOM   1324 C  CE2 . TRP A 1 235 ? -60.307 -31.637 39.288  1.00 55.35  ? 208 TRP B CE2 1 
ATOM   1325 C  CE3 . TRP A 1 235 ? -58.772 -32.518 40.940  1.00 58.57  ? 208 TRP B CE3 1 
ATOM   1326 C  CZ2 . TRP A 1 235 ? -60.579 -32.902 38.785  1.00 57.43  ? 208 TRP B CZ2 1 
ATOM   1327 C  CZ3 . TRP A 1 235 ? -59.038 -33.796 40.434  1.00 60.93  ? 208 TRP B CZ3 1 
ATOM   1328 C  CH2 . TRP A 1 235 ? -59.935 -33.975 39.374  1.00 62.18  ? 208 TRP B CH2 1 
ATOM   1329 N  N   . VAL A 1 236 ? -55.684 -29.419 39.622  1.00 53.83  ? 209 VAL B N   1 
ATOM   1330 C  CA  . VAL A 1 236 ? -55.035 -28.814 38.439  1.00 55.30  ? 209 VAL B CA  1 
ATOM   1331 C  C   . VAL A 1 236 ? -54.811 -29.775 37.262  1.00 50.64  ? 209 VAL B C   1 
ATOM   1332 O  O   . VAL A 1 236 ? -54.826 -30.972 37.410  1.00 50.81  ? 209 VAL B O   1 
ATOM   1333 C  CB  . VAL A 1 236 ? -53.641 -28.215 38.783  1.00 51.93  ? 209 VAL B CB  1 
ATOM   1334 C  CG1 . VAL A 1 236 ? -53.720 -27.293 39.969  1.00 53.93  ? 209 VAL B CG1 1 
ATOM   1335 C  CG2 . VAL A 1 236 ? -52.634 -29.310 39.090  1.00 50.17  ? 209 VAL B CG2 1 
ATOM   1336 N  N   . GLY A 1 237 ? -54.542 -29.194 36.105  1.00 48.70  ? 210 GLY B N   1 
ATOM   1337 C  CA  . GLY A 1 237 ? -54.071 -29.911 34.949  1.00 47.85  ? 210 GLY B CA  1 
ATOM   1338 C  C   . GLY A 1 237 ? -52.659 -29.459 34.613  1.00 47.90  ? 210 GLY B C   1 
ATOM   1339 O  O   . GLY A 1 237 ? -52.206 -28.376 35.056  1.00 46.23  ? 210 GLY B O   1 
ATOM   1340 N  N   . THR A 1 238 ? -51.949 -30.315 33.874  1.00 43.91  ? 211 THR B N   1 
ATOM   1341 C  CA  . THR A 1 238 ? -50.613 -29.994 33.405  1.00 44.95  ? 211 THR B CA  1 
ATOM   1342 C  C   . THR A 1 238 ? -50.473 -30.279 31.947  1.00 45.45  ? 211 THR B C   1 
ATOM   1343 O  O   . THR A 1 238 ? -51.073 -31.222 31.395  1.00 44.59  ? 211 THR B O   1 
ATOM   1344 C  CB  . THR A 1 238 ? -49.541 -30.810 34.110  1.00 42.62  ? 211 THR B CB  1 
ATOM   1345 O  OG1 . THR A 1 238 ? -49.787 -32.190 33.857  1.00 49.27  ? 211 THR B OG1 1 
ATOM   1346 C  CG2 . THR A 1 238 ? -49.602 -30.560 35.610  1.00 43.12  ? 211 THR B CG2 1 
ATOM   1347 N  N   . ILE A 1 239 ? -49.665 -29.447 31.321  1.00 44.32  ? 212 ILE B N   1 
ATOM   1348 C  CA  . ILE A 1 239 ? -49.312 -29.603 29.931  1.00 41.73  ? 212 ILE B CA  1 
ATOM   1349 C  C   . ILE A 1 239 ? -47.844 -29.264 29.882  1.00 43.31  ? 212 ILE B C   1 
ATOM   1350 O  O   . ILE A 1 239 ? -47.412 -28.314 30.536  1.00 39.56  ? 212 ILE B O   1 
ATOM   1351 C  CB  . ILE A 1 239 ? -50.091 -28.620 29.080  1.00 45.24  ? 212 ILE B CB  1 
ATOM   1352 C  CG1 . ILE A 1 239 ? -51.534 -29.091 28.965  1.00 50.47  ? 212 ILE B CG1 1 
ATOM   1353 C  CG2 . ILE A 1 239 ? -49.482 -28.511 27.691  1.00 46.99  ? 212 ILE B CG2 1 
ATOM   1354 C  CD1 . ILE A 1 239 ? -52.487 -27.955 28.694  1.00 56.43  ? 212 ILE B CD1 1 
ATOM   1355 N  N   . ALA A 1 240 ? -47.064 -30.053 29.147  1.00 44.39  ? 213 ALA B N   1 
ATOM   1356 C  CA  . ALA A 1 240 ? -45.633 -29.804 29.055  1.00 42.62  ? 213 ALA B CA  1 
ATOM   1357 C  C   . ALA A 1 240 ? -45.142 -30.071 27.656  1.00 45.02  ? 213 ALA B C   1 
ATOM   1358 O  O   . ALA A 1 240 ? -45.678 -30.948 26.991  1.00 48.82  ? 213 ALA B O   1 
ATOM   1359 C  CB  . ALA A 1 240 ? -44.933 -30.691 30.016  1.00 42.29  ? 213 ALA B CB  1 
ATOM   1360 N  N   . ALA A 1 241 ? -44.140 -29.310 27.208  1.00 45.83  ? 214 ALA B N   1 
ATOM   1361 C  CA  . ALA A 1 241 ? -43.481 -29.557 25.911  1.00 45.31  ? 214 ALA B CA  1 
ATOM   1362 C  C   . ALA A 1 241 ? -42.706 -30.856 25.910  1.00 43.72  ? 214 ALA B C   1 
ATOM   1363 O  O   . ALA A 1 241 ? -41.997 -31.159 26.853  1.00 49.80  ? 214 ALA B O   1 
ATOM   1364 C  CB  . ALA A 1 241 ? -42.559 -28.416 25.569  1.00 46.57  ? 214 ALA B CB  1 
ATOM   1365 N  N   . ASP A 1 242 ? -42.860 -31.642 24.860  1.00 48.08  ? 215 ASP B N   1 
ATOM   1366 C  CA  . ASP A 1 242 ? -42.222 -32.957 24.781  1.00 49.94  ? 215 ASP B CA  1 
ATOM   1367 C  C   . ASP A 1 242 ? -40.747 -32.786 24.415  1.00 50.11  ? 215 ASP B C   1 
ATOM   1368 O  O   . ASP A 1 242 ? -40.358 -32.981 23.279  1.00 55.94  ? 215 ASP B O   1 
ATOM   1369 C  CB  . ASP A 1 242 ? -42.960 -33.845 23.769  1.00 49.11  ? 215 ASP B CB  1 
ATOM   1370 C  CG  . ASP A 1 242 ? -42.606 -35.323 23.902  1.00 55.68  ? 215 ASP B CG  1 
ATOM   1371 O  OD1 . ASP A 1 242 ? -41.810 -35.642 24.811  1.00 61.34  ? 215 ASP B OD1 1 
ATOM   1372 O  OD2 . ASP A 1 242 ? -43.134 -36.174 23.121  1.00 53.15  ? 215 ASP B OD2 1 
ATOM   1373 N  N   . ASP A 1 243 ? -39.934 -32.418 25.396  1.00 54.19  ? 216 ASP B N   1 
ATOM   1374 C  CA  . ASP A 1 243 ? -38.491 -32.196 25.200  1.00 55.35  ? 216 ASP B CA  1 
ATOM   1375 C  C   . ASP A 1 243 ? -37.779 -32.150 26.563  1.00 49.46  ? 216 ASP B C   1 
ATOM   1376 O  O   . ASP A 1 243 ? -38.437 -32.336 27.589  1.00 49.93  ? 216 ASP B O   1 
ATOM   1377 C  CB  . ASP A 1 243 ? -38.223 -30.926 24.376  1.00 54.45  ? 216 ASP B CB  1 
ATOM   1378 C  CG  . ASP A 1 243 ? -38.775 -29.632 25.030  1.00 60.19  ? 216 ASP B CG  1 
ATOM   1379 O  OD1 . ASP A 1 243 ? -38.567 -29.359 26.247  1.00 54.43  ? 216 ASP B OD1 1 
ATOM   1380 O  OD2 . ASP A 1 243 ? -39.400 -28.857 24.273  1.00 68.97  ? 216 ASP B OD2 1 
ATOM   1381 N  N   . ASP A 1 244 ? -36.463 -31.907 26.567  1.00 45.76  ? 217 ASP B N   1 
ATOM   1382 C  CA  . ASP A 1 244 ? -35.675 -31.988 27.790  1.00 46.75  ? 217 ASP B CA  1 
ATOM   1383 C  C   . ASP A 1 244 ? -35.870 -30.735 28.642  1.00 48.95  ? 217 ASP B C   1 
ATOM   1384 O  O   . ASP A 1 244 ? -35.270 -30.661 29.715  1.00 54.79  ? 217 ASP B O   1 
ATOM   1385 C  CB  . ASP A 1 244 ? -34.165 -32.129 27.533  1.00 55.23  ? 217 ASP B CB  1 
ATOM   1386 C  CG  . ASP A 1 244 ? -33.744 -33.473 26.919  1.00 61.68  ? 217 ASP B CG  1 
ATOM   1387 O  OD1 . ASP A 1 244 ? -34.356 -34.521 27.255  1.00 65.49  ? 217 ASP B OD1 1 
ATOM   1388 O  OD2 . ASP A 1 244 ? -32.743 -33.455 26.130  1.00 60.25  ? 217 ASP B OD2 1 
ATOM   1389 N  N   . TYR A 1 245 ? -36.653 -29.746 28.197  1.00 40.89  ? 218 TYR B N   1 
ATOM   1390 C  CA  . TYR A 1 245 ? -37.114 -28.701 29.133  1.00 42.45  ? 218 TYR B CA  1 
ATOM   1391 C  C   . TYR A 1 245 ? -38.452 -29.062 29.810  1.00 41.54  ? 218 TYR B C   1 
ATOM   1392 O  O   . TYR A 1 245 ? -38.541 -29.096 31.028  1.00 47.89  ? 218 TYR B O   1 
ATOM   1393 C  CB  . TYR A 1 245 ? -37.203 -27.352 28.441  1.00 38.55  ? 218 TYR B CB  1 
ATOM   1394 C  CG  . TYR A 1 245 ? -37.919 -26.248 29.176  1.00 36.23  ? 218 TYR B CG  1 
ATOM   1395 C  CD1 . TYR A 1 245 ? -37.356 -25.653 30.272  1.00 35.44  ? 218 TYR B CD1 1 
ATOM   1396 C  CD2 . TYR A 1 245 ? -39.120 -25.719 28.684  1.00 39.98  ? 218 TYR B CD2 1 
ATOM   1397 C  CE1 . TYR A 1 245 ? -37.995 -24.629 30.945  1.00 39.01  ? 218 TYR B CE1 1 
ATOM   1398 C  CE2 . TYR A 1 245 ? -39.764 -24.662 29.320  1.00 41.56  ? 218 TYR B CE2 1 
ATOM   1399 C  CZ  . TYR A 1 245 ? -39.198 -24.117 30.474  1.00 44.20  ? 218 TYR B CZ  1 
ATOM   1400 O  OH  . TYR A 1 245 ? -39.811 -23.038 31.142  1.00 46.08  ? 218 TYR B OH  1 
ATOM   1401 N  N   . GLY A 1 246 ? -39.469 -29.332 29.007  1.00 43.48  ? 219 GLY B N   1 
ATOM   1402 C  CA  . GLY A 1 246 ? -40.812 -29.650 29.490  1.00 40.68  ? 219 GLY B CA  1 
ATOM   1403 C  C   . GLY A 1 246 ? -40.887 -30.893 30.332  1.00 40.50  ? 219 GLY B C   1 
ATOM   1404 O  O   . GLY A 1 246 ? -41.266 -30.794 31.494  1.00 45.64  ? 219 GLY B O   1 
ATOM   1405 N  N   . ARG A 1 247 ? -40.485 -32.048 29.790  1.00 39.25  ? 220 ARG B N   1 
ATOM   1406 C  CA  . ARG A 1 247 ? -40.598 -33.321 30.532  1.00 38.73  ? 220 ARG B CA  1 
ATOM   1407 C  C   . ARG A 1 247 ? -39.981 -33.381 31.948  1.00 40.39  ? 220 ARG B C   1 
ATOM   1408 O  O   . ARG A 1 247 ? -40.658 -33.764 32.899  1.00 41.96  ? 220 ARG B O   1 
ATOM   1409 C  CB  . ARG A 1 247 ? -40.080 -34.490 29.710  1.00 39.24  ? 220 ARG B CB  1 
ATOM   1410 C  CG  . ARG A 1 247 ? -40.901 -34.755 28.462  1.00 44.13  ? 220 ARG B CG  1 
ATOM   1411 C  CD  . ARG A 1 247 ? -40.515 -36.052 27.765  1.00 44.00  ? 220 ARG B CD  1 
ATOM   1412 N  NE  . ARG A 1 247 ? -39.083 -36.120 27.533  1.00 45.21  ? 220 ARG B NE  1 
ATOM   1413 C  CZ  . ARG A 1 247 ? -38.459 -35.831 26.398  1.00 49.35  ? 220 ARG B CZ  1 
ATOM   1414 N  NH1 . ARG A 1 247 ? -39.112 -35.436 25.315  1.00 53.85  ? 220 ARG B NH1 1 
ATOM   1415 N  NH2 . ARG A 1 247 ? -37.144 -35.955 26.354  1.00 52.61  ? 220 ARG B NH2 1 
ATOM   1416 N  N   . PRO A 1 248 ? -38.695 -33.056 32.092  1.00 44.65  ? 221 PRO B N   1 
ATOM   1417 C  CA  . PRO A 1 248 ? -38.132 -33.091 33.455  1.00 43.05  ? 221 PRO B CA  1 
ATOM   1418 C  C   . PRO A 1 248 ? -38.762 -32.034 34.401  1.00 44.91  ? 221 PRO B C   1 
ATOM   1419 O  O   . PRO A 1 248 ? -38.937 -32.292 35.597  1.00 45.12  ? 221 PRO B O   1 
ATOM   1420 C  CB  . PRO A 1 248 ? -36.637 -32.802 33.248  1.00 41.87  ? 221 PRO B CB  1 
ATOM   1421 C  CG  . PRO A 1 248 ? -36.417 -32.642 31.780  1.00 45.37  ? 221 PRO B CG  1 
ATOM   1422 C  CD  . PRO A 1 248 ? -37.755 -32.497 31.098  1.00 45.82  ? 221 PRO B CD  1 
ATOM   1423 N  N   . GLY A 1 249 ? -39.111 -30.867 33.866  1.00 42.83  ? 222 GLY B N   1 
ATOM   1424 C  CA  . GLY A 1 249 ? -39.775 -29.831 34.649  1.00 42.88  ? 222 GLY B CA  1 
ATOM   1425 C  C   . GLY A 1 249 ? -41.106 -30.314 35.219  1.00 42.45  ? 222 GLY B C   1 
ATOM   1426 O  O   . GLY A 1 249 ? -41.317 -30.225 36.400  1.00 40.15  ? 222 GLY B O   1 
ATOM   1427 N  N   . ILE A 1 250 ? -42.009 -30.817 34.379  1.00 42.30  ? 223 ILE B N   1 
ATOM   1428 C  CA  . ILE A 1 250 ? -43.304 -31.257 34.882  1.00 48.48  ? 223 ILE B CA  1 
ATOM   1429 C  C   . ILE A 1 250 ? -43.237 -32.478 35.757  1.00 45.60  ? 223 ILE B C   1 
ATOM   1430 O  O   . ILE A 1 250 ? -44.096 -32.627 36.578  1.00 47.13  ? 223 ILE B O   1 
ATOM   1431 C  CB  . ILE A 1 250 ? -44.382 -31.497 33.774  1.00 49.77  ? 223 ILE B CB  1 
ATOM   1432 C  CG1 . ILE A 1 250 ? -45.758 -31.059 34.292  1.00 45.24  ? 223 ILE B CG1 1 
ATOM   1433 C  CG2 . ILE A 1 250 ? -44.424 -32.927 33.280  1.00 45.51  ? 223 ILE B CG2 1 
ATOM   1434 C  CD1 . ILE A 1 250 ? -45.874 -29.537 34.336  1.00 45.31  ? 223 ILE B CD1 1 
ATOM   1435 N  N   . GLU A 1 251 ? -42.249 -33.348 35.557  1.00 46.39  ? 224 GLU B N   1 
ATOM   1436 C  CA  . GLU A 1 251 ? -42.089 -34.518 36.397  1.00 46.84  ? 224 GLU B CA  1 
ATOM   1437 C  C   . GLU A 1 251 ? -41.779 -34.063 37.801  1.00 46.04  ? 224 GLU B C   1 
ATOM   1438 O  O   . GLU A 1 251 ? -42.322 -34.577 38.772  1.00 44.28  ? 224 GLU B O   1 
ATOM   1439 C  CB  . GLU A 1 251 ? -40.971 -35.411 35.864  1.00 50.75  ? 224 GLU B CB  1 
ATOM   1440 C  CG  . GLU A 1 251 ? -40.753 -36.731 36.613  1.00 55.65  ? 224 GLU B CG  1 
ATOM   1441 C  CD  . GLU A 1 251 ? -42.021 -37.493 37.019  1.00 65.03  ? 224 GLU B CD  1 
ATOM   1442 O  OE1 . GLU A 1 251 ? -41.884 -38.302 37.960  1.00 73.11  ? 224 GLU B OE1 1 
ATOM   1443 O  OE2 . GLU A 1 251 ? -43.136 -37.326 36.427  1.00 70.00  ? 224 GLU B OE2 1 
ATOM   1444 N  N   . LYS A 1 252 ? -40.928 -33.056 37.895  1.00 44.61  ? 225 LYS B N   1 
ATOM   1445 C  CA  . LYS A 1 252 ? -40.590 -32.505 39.160  1.00 44.34  ? 225 LYS B CA  1 
ATOM   1446 C  C   . LYS A 1 252 ? -41.807 -31.889 39.784  1.00 45.50  ? 225 LYS B C   1 
ATOM   1447 O  O   . LYS A 1 252 ? -42.066 -32.105 40.965  1.00 44.77  ? 225 LYS B O   1 
ATOM   1448 C  CB  . LYS A 1 252 ? -39.515 -31.451 38.995  1.00 48.67  ? 225 LYS B CB  1 
ATOM   1449 C  CG  . LYS A 1 252 ? -39.100 -30.747 40.279  1.00 51.63  ? 225 LYS B CG  1 
ATOM   1450 C  CD  . LYS A 1 252 ? -38.689 -31.701 41.375  1.00 47.65  ? 225 LYS B CD  1 
ATOM   1451 C  CE  . LYS A 1 252 ? -38.085 -30.923 42.525  1.00 51.62  ? 225 LYS B CE  1 
ATOM   1452 N  NZ  . LYS A 1 252 ? -37.756 -31.882 43.628  1.00 54.05  ? 225 LYS B NZ  1 
ATOM   1453 N  N   . PHE A 1 253 ? -42.550 -31.114 39.001  1.00 45.09  ? 226 PHE B N   1 
ATOM   1454 C  CA  . PHE A 1 253 ? -43.758 -30.499 39.513  1.00 45.43  ? 226 PHE B CA  1 
ATOM   1455 C  C   . PHE A 1 253 ? -44.723 -31.541 40.079  1.00 45.99  ? 226 PHE B C   1 
ATOM   1456 O  O   . PHE A 1 253 ? -45.297 -31.334 41.123  1.00 47.60  ? 226 PHE B O   1 
ATOM   1457 C  CB  . PHE A 1 253 ? -44.483 -29.668 38.467  1.00 44.88  ? 226 PHE B CB  1 
ATOM   1458 C  CG  . PHE A 1 253 ? -45.875 -29.263 38.910  1.00 47.80  ? 226 PHE B CG  1 
ATOM   1459 C  CD1 . PHE A 1 253 ? -46.042 -28.299 39.874  1.00 47.84  ? 226 PHE B CD1 1 
ATOM   1460 C  CD2 . PHE A 1 253 ? -46.987 -29.881 38.408  1.00 47.09  ? 226 PHE B CD2 1 
ATOM   1461 C  CE1 . PHE A 1 253 ? -47.284 -27.957 40.326  1.00 48.67  ? 226 PHE B CE1 1 
ATOM   1462 C  CE2 . PHE A 1 253 ? -48.234 -29.523 38.838  1.00 51.48  ? 226 PHE B CE2 1 
ATOM   1463 C  CZ  . PHE A 1 253 ? -48.386 -28.565 39.807  1.00 50.25  ? 226 PHE B CZ  1 
ATOM   1464 N  N   . ARG A 1 254 ? -44.864 -32.670 39.406  1.00 50.91  ? 227 ARG B N   1 
ATOM   1465 C  CA  . ARG A 1 254 ? -45.757 -33.730 39.852  1.00 53.25  ? 227 ARG B CA  1 
ATOM   1466 C  C   . ARG A 1 254 ? -45.359 -34.198 41.237  1.00 53.71  ? 227 ARG B C   1 
ATOM   1467 O  O   . ARG A 1 254 ? -46.174 -34.193 42.154  1.00 52.21  ? 227 ARG B O   1 
ATOM   1468 C  CB  . ARG A 1 254 ? -45.734 -34.895 38.876  1.00 52.82  ? 227 ARG B CB  1 
ATOM   1469 C  CG  . ARG A 1 254 ? -46.831 -35.918 39.135  1.00 55.90  ? 227 ARG B CG  1 
ATOM   1470 C  CD  . ARG A 1 254 ? -46.545 -37.275 38.480  1.00 58.83  ? 227 ARG B CD  1 
ATOM   1471 N  NE  . ARG A 1 254 ? -45.182 -37.765 38.762  1.00 64.10  ? 227 ARG B NE  1 
ATOM   1472 C  CZ  . ARG A 1 254 ? -44.741 -38.135 39.967  1.00 64.25  ? 227 ARG B CZ  1 
ATOM   1473 N  NH1 . ARG A 1 254 ? -45.533 -38.113 41.038  1.00 62.28  ? 227 ARG B NH1 1 
ATOM   1474 N  NH2 . ARG A 1 254 ? -43.488 -38.524 40.105  1.00 68.83  ? 227 ARG B NH2 1 
ATOM   1475 N  N   . GLU A 1 255 ? -44.094 -34.565 41.394  1.00 55.99  ? 228 GLU B N   1 
ATOM   1476 C  CA  . GLU A 1 255 ? -43.567 -34.970 42.697  1.00 57.80  ? 228 GLU B CA  1 
ATOM   1477 C  C   . GLU A 1 255 ? -43.936 -33.968 43.802  1.00 54.44  ? 228 GLU B C   1 
ATOM   1478 O  O   . GLU A 1 255 ? -44.421 -34.326 44.853  1.00 62.48  ? 228 GLU B O   1 
ATOM   1479 C  CB  . GLU A 1 255 ? -42.053 -35.122 42.608  1.00 57.71  ? 228 GLU B CB  1 
ATOM   1480 C  CG  . GLU A 1 255 ? -41.357 -35.469 43.907  1.00 61.30  ? 228 GLU B CG  1 
ATOM   1481 C  CD  . GLU A 1 255 ? -39.863 -35.214 43.841  1.00 75.04  ? 228 GLU B CD  1 
ATOM   1482 O  OE1 . GLU A 1 255 ? -39.241 -35.537 42.788  1.00 73.42  ? 228 GLU B OE1 1 
ATOM   1483 O  OE2 . GLU A 1 255 ? -39.321 -34.674 44.845  1.00 82.64  ? 228 GLU B OE2 1 
ATOM   1484 N  N   . GLU A 1 256 ? -43.713 -32.709 43.534  1.00 53.47  ? 229 GLU B N   1 
ATOM   1485 C  CA  . GLU A 1 256 ? -43.934 -31.678 44.509  1.00 55.49  ? 229 GLU B CA  1 
ATOM   1486 C  C   . GLU A 1 256 ? -45.399 -31.473 44.788  1.00 50.03  ? 229 GLU B C   1 
ATOM   1487 O  O   . GLU A 1 256 ? -45.787 -31.091 45.881  1.00 46.94  ? 229 GLU B O   1 
ATOM   1488 C  CB  . GLU A 1 256 ? -43.359 -30.363 43.984  1.00 59.22  ? 229 GLU B CB  1 
ATOM   1489 C  CG  . GLU A 1 256 ? -41.858 -30.364 43.859  1.00 65.53  ? 229 GLU B CG  1 
ATOM   1490 C  CD  . GLU A 1 256 ? -41.184 -30.669 45.167  1.00 73.37  ? 229 GLU B CD  1 
ATOM   1491 O  OE1 . GLU A 1 256 ? -41.569 -30.048 46.188  1.00 80.35  ? 229 GLU B OE1 1 
ATOM   1492 O  OE2 . GLU A 1 256 ? -40.277 -31.540 45.173  1.00 90.91  ? 229 GLU B OE2 1 
ATOM   1493 N  N   . ALA A 1 257 ? -46.206 -31.649 43.760  1.00 49.16  ? 230 ALA B N   1 
ATOM   1494 C  CA  . ALA A 1 257 ? -47.624 -31.500 43.910  1.00 49.62  ? 230 ALA B CA  1 
ATOM   1495 C  C   . ALA A 1 257 ? -48.141 -32.604 44.832  1.00 55.83  ? 230 ALA B C   1 
ATOM   1496 O  O   . ALA A 1 257 ? -48.899 -32.337 45.740  1.00 55.40  ? 230 ALA B O   1 
ATOM   1497 C  CB  . ALA A 1 257 ? -48.283 -31.568 42.554  1.00 48.36  ? 230 ALA B CB  1 
ATOM   1498 N  N   . GLU A 1 258 ? -47.711 -33.843 44.594  1.00 60.15  ? 231 GLU B N   1 
ATOM   1499 C  CA  . GLU A 1 258 ? -48.082 -34.947 45.450  1.00 59.48  ? 231 GLU B CA  1 
ATOM   1500 C  C   . GLU A 1 258 ? -47.740 -34.619 46.917  1.00 54.90  ? 231 GLU B C   1 
ATOM   1501 O  O   . GLU A 1 258 ? -48.599 -34.782 47.779  1.00 57.02  ? 231 GLU B O   1 
ATOM   1502 C  CB  . GLU A 1 258 ? -47.434 -36.268 44.981  1.00 60.13  ? 231 GLU B CB  1 
ATOM   1503 N  N   . GLU A 1 259 ? -46.536 -34.124 47.205  1.00 53.65  ? 232 GLU B N   1 
ATOM   1504 C  CA  . GLU A 1 259 ? -46.117 -33.872 48.608  1.00 60.27  ? 232 GLU B CA  1 
ATOM   1505 C  C   . GLU A 1 259 ? -47.083 -32.944 49.303  1.00 60.34  ? 232 GLU B C   1 
ATOM   1506 O  O   . GLU A 1 259 ? -47.229 -32.995 50.505  1.00 68.36  ? 232 GLU B O   1 
ATOM   1507 C  CB  . GLU A 1 259 ? -44.701 -33.281 48.712  1.00 66.11  ? 232 GLU B CB  1 
ATOM   1508 C  CG  . GLU A 1 259 ? -43.607 -34.344 48.676  1.00 84.14  ? 232 GLU B CG  1 
ATOM   1509 C  CD  . GLU A 1 259 ? -42.198 -33.773 48.521  1.00 102.42 ? 232 GLU B CD  1 
ATOM   1510 O  OE1 . GLU A 1 259 ? -42.041 -32.529 48.570  1.00 114.65 ? 232 GLU B OE1 1 
ATOM   1511 O  OE2 . GLU A 1 259 ? -41.241 -34.573 48.357  1.00 108.82 ? 232 GLU B OE2 1 
ATOM   1512 N  N   . ARG A 1 260 ? -47.753 -32.102 48.529  1.00 59.83  ? 233 ARG B N   1 
ATOM   1513 C  CA  . ARG A 1 260 ? -48.653 -31.104 49.057  1.00 54.69  ? 233 ARG B CA  1 
ATOM   1514 C  C   . ARG A 1 260 ? -50.120 -31.451 48.808  1.00 51.67  ? 233 ARG B C   1 
ATOM   1515 O  O   . ARG A 1 260 ? -50.985 -30.594 48.915  1.00 53.03  ? 233 ARG B O   1 
ATOM   1516 C  CB  . ARG A 1 260 ? -48.317 -29.761 48.407  1.00 53.38  ? 233 ARG B CB  1 
ATOM   1517 C  CG  . ARG A 1 260 ? -46.990 -29.157 48.826  1.00 48.54  ? 233 ARG B CG  1 
ATOM   1518 C  CD  . ARG A 1 260 ? -46.622 -28.110 47.787  1.00 52.07  ? 233 ARG B CD  1 
ATOM   1519 N  NE  . ARG A 1 260 ? -45.288 -27.545 47.965  1.00 53.12  ? 233 ARG B NE  1 
ATOM   1520 C  CZ  . ARG A 1 260 ? -44.141 -28.210 47.816  1.00 49.75  ? 233 ARG B CZ  1 
ATOM   1521 N  NH1 . ARG A 1 260 ? -44.097 -29.503 47.492  1.00 50.55  ? 233 ARG B NH1 1 
ATOM   1522 N  NH2 . ARG A 1 260 ? -43.012 -27.569 48.009  1.00 48.97  ? 233 ARG B NH2 1 
ATOM   1523 N  N   . ASP A 1 261 ? -50.403 -32.701 48.485  1.00 54.71  ? 234 ASP B N   1 
ATOM   1524 C  CA  . ASP A 1 261 ? -51.778 -33.155 48.208  1.00 65.07  ? 234 ASP B CA  1 
ATOM   1525 C  C   . ASP A 1 261 ? -52.562 -32.248 47.257  1.00 63.03  ? 234 ASP B C   1 
ATOM   1526 O  O   . ASP A 1 261 ? -53.694 -31.870 47.496  1.00 57.80  ? 234 ASP B O   1 
ATOM   1527 C  CB  . ASP A 1 261 ? -52.529 -33.451 49.504  1.00 68.72  ? 234 ASP B CB  1 
ATOM   1528 C  CG  . ASP A 1 261 ? -52.258 -34.850 49.988  1.00 82.49  ? 234 ASP B CG  1 
ATOM   1529 O  OD1 . ASP A 1 261 ? -52.578 -35.810 49.223  1.00 91.47  ? 234 ASP B OD1 1 
ATOM   1530 O  OD2 . ASP A 1 261 ? -51.690 -34.984 51.101  1.00 83.21  ? 234 ASP B OD2 1 
ATOM   1531 N  N   . ILE A 1 262 ? -51.905 -31.947 46.149  1.00 62.96  ? 235 ILE B N   1 
ATOM   1532 C  CA  . ILE A 1 262 ? -52.474 -31.252 45.030  1.00 58.02  ? 235 ILE B CA  1 
ATOM   1533 C  C   . ILE A 1 262 ? -52.777 -32.350 44.010  1.00 54.97  ? 235 ILE B C   1 
ATOM   1534 O  O   . ILE A 1 262 ? -51.898 -33.106 43.657  1.00 62.91  ? 235 ILE B O   1 
ATOM   1535 C  CB  . ILE A 1 262 ? -51.448 -30.217 44.502  1.00 56.64  ? 235 ILE B CB  1 
ATOM   1536 C  CG1 . ILE A 1 262 ? -51.460 -28.970 45.388  1.00 56.02  ? 235 ILE B CG1 1 
ATOM   1537 C  CG2 . ILE A 1 262 ? -51.730 -29.823 43.062  1.00 57.96  ? 235 ILE B CG2 1 
ATOM   1538 C  CD1 . ILE A 1 262 ? -50.180 -28.164 45.321  1.00 57.20  ? 235 ILE B CD1 1 
HETATM 1539 N  N   . CSO A 1 263 ? -54.012 -32.441 43.537  1.00 53.92  ? 236 CSO B N   1 
HETATM 1540 C  CA  . CSO A 1 263 ? -54.395 -33.494 42.592  1.00 57.06  ? 236 CSO B CA  1 
HETATM 1541 C  CB  . CSO A 1 263 ? -55.791 -34.088 42.862  1.00 63.02  ? 236 CSO B CB  1 
HETATM 1542 S  SG  . CSO A 1 263 ? -55.809 -34.752 44.517  1.00 78.78  ? 236 CSO B SG  1 
HETATM 1543 C  C   . CSO A 1 263 ? -54.354 -32.997 41.197  1.00 53.01  ? 236 CSO B C   1 
HETATM 1544 O  O   . CSO A 1 263 ? -54.772 -31.883 40.909  1.00 61.56  ? 236 CSO B O   1 
HETATM 1545 O  OD  . CSO A 1 263 ? -55.260 -36.406 44.383  1.00 78.99  ? 236 CSO B OD  1 
ATOM   1546 N  N   . ILE A 1 264 ? -53.847 -33.847 40.314  1.00 50.44  ? 237 ILE B N   1 
ATOM   1547 C  CA  . ILE A 1 264 ? -53.688 -33.549 38.912  1.00 44.16  ? 237 ILE B CA  1 
ATOM   1548 C  C   . ILE A 1 264 ? -54.666 -34.401 38.111  1.00 43.88  ? 237 ILE B C   1 
ATOM   1549 O  O   . ILE A 1 264 ? -54.614 -35.623 38.107  1.00 43.63  ? 237 ILE B O   1 
ATOM   1550 C  CB  . ILE A 1 264 ? -52.236 -33.848 38.497  1.00 46.38  ? 237 ILE B CB  1 
ATOM   1551 C  CG1 . ILE A 1 264 ? -51.285 -33.081 39.436  1.00 49.22  ? 237 ILE B CG1 1 
ATOM   1552 C  CG2 . ILE A 1 264 ? -51.997 -33.540 37.020  1.00 42.79  ? 237 ILE B CG2 1 
ATOM   1553 C  CD1 . ILE A 1 264 ? -49.817 -33.215 39.100  1.00 51.08  ? 237 ILE B CD1 1 
ATOM   1554 N  N   . ASP A 1 265 ? -55.577 -33.739 37.434  1.00 48.60  ? 238 ASP B N   1 
ATOM   1555 C  CA  . ASP A 1 265 ? -56.634 -34.415 36.723  1.00 50.04  ? 238 ASP B CA  1 
ATOM   1556 C  C   . ASP A 1 265 ? -56.228 -34.821 35.326  1.00 48.52  ? 238 ASP B C   1 
ATOM   1557 O  O   . ASP A 1 265 ? -56.822 -35.729 34.756  1.00 48.19  ? 238 ASP B O   1 
ATOM   1558 C  CB  . ASP A 1 265 ? -57.869 -33.506 36.618  1.00 49.53  ? 238 ASP B CB  1 
ATOM   1559 C  CG  . ASP A 1 265 ? -59.062 -34.231 35.978  1.00 51.87  ? 238 ASP B CG  1 
ATOM   1560 O  OD1 . ASP A 1 265 ? -59.458 -35.338 36.468  1.00 50.13  ? 238 ASP B OD1 1 
ATOM   1561 O  OD2 . ASP A 1 265 ? -59.566 -33.709 34.961  1.00 50.51  ? 238 ASP B OD2 1 
ATOM   1562 N  N   . PHE A 1 266 ? -55.309 -34.080 34.727  1.00 49.15  ? 239 PHE B N   1 
ATOM   1563 C  CA  . PHE A 1 266 ? -54.751 -34.511 33.451  1.00 49.87  ? 239 PHE B CA  1 
ATOM   1564 C  C   . PHE A 1 266 ? -53.349 -34.024 33.299  1.00 52.57  ? 239 PHE B C   1 
ATOM   1565 O  O   . PHE A 1 266 ? -52.929 -33.073 33.963  1.00 56.25  ? 239 PHE B O   1 
ATOM   1566 C  CB  . PHE A 1 266 ? -55.579 -34.061 32.235  1.00 50.06  ? 239 PHE B CB  1 
ATOM   1567 C  CG  . PHE A 1 266 ? -55.648 -32.579 32.047  1.00 45.93  ? 239 PHE B CG  1 
ATOM   1568 C  CD1 . PHE A 1 266 ? -54.603 -31.899 31.480  1.00 46.99  ? 239 PHE B CD1 1 
ATOM   1569 C  CD2 . PHE A 1 266 ? -56.759 -31.863 32.454  1.00 48.17  ? 239 PHE B CD2 1 
ATOM   1570 C  CE1 . PHE A 1 266 ? -54.639 -30.511 31.301  1.00 49.01  ? 239 PHE B CE1 1 
ATOM   1571 C  CE2 . PHE A 1 266 ? -56.806 -30.479 32.292  1.00 52.30  ? 239 PHE B CE2 1 
ATOM   1572 C  CZ  . PHE A 1 266 ? -55.741 -29.796 31.697  1.00 48.20  ? 239 PHE B CZ  1 
ATOM   1573 N  N   . SER A 1 267 ? -52.643 -34.699 32.399  1.00 55.74  ? 240 SER B N   1 
ATOM   1574 C  CA  . SER A 1 267 ? -51.271 -34.391 32.082  1.00 53.37  ? 240 SER B CA  1 
ATOM   1575 C  C   . SER A 1 267 ? -51.003 -34.751 30.621  1.00 49.79  ? 240 SER B C   1 
ATOM   1576 O  O   . SER A 1 267 ? -51.139 -35.899 30.262  1.00 55.13  ? 240 SER B O   1 
ATOM   1577 C  CB  . SER A 1 267 ? -50.377 -35.183 33.021  1.00 50.57  ? 240 SER B CB  1 
ATOM   1578 O  OG  . SER A 1 267 ? -50.246 -36.530 32.591  1.00 52.39  ? 240 SER B OG  1 
ATOM   1579 N  N   . GLU A 1 268 ? -50.647 -33.772 29.790  1.00 51.92  ? 241 GLU B N   1 
ATOM   1580 C  CA  . GLU A 1 268 ? -50.469 -33.980 28.346  1.00 50.07  ? 241 GLU B CA  1 
ATOM   1581 C  C   . GLU A 1 268 ? -49.216 -33.313 27.881  1.00 47.02  ? 241 GLU B C   1 
ATOM   1582 O  O   . GLU A 1 268 ? -48.794 -32.353 28.476  1.00 51.23  ? 241 GLU B O   1 
ATOM   1583 C  CB  . GLU A 1 268 ? -51.660 -33.398 27.537  1.00 57.79  ? 241 GLU B CB  1 
ATOM   1584 C  CG  . GLU A 1 268 ? -53.069 -33.935 27.893  1.00 57.29  ? 241 GLU B CG  1 
ATOM   1585 C  CD  . GLU A 1 268 ? -53.227 -35.456 27.731  1.00 60.56  ? 241 GLU B CD  1 
ATOM   1586 O  OE1 . GLU A 1 268 ? -53.737 -36.135 28.674  1.00 67.39  ? 241 GLU B OE1 1 
ATOM   1587 O  OE2 . GLU A 1 268 ? -52.836 -35.982 26.666  1.00 61.66  ? 241 GLU B OE2 1 
ATOM   1588 N  N   . LEU A 1 269 ? -48.631 -33.835 26.802  1.00 56.94  ? 242 LEU B N   1 
ATOM   1589 C  CA  . LEU A 1 269 ? -47.425 -33.285 26.144  1.00 50.80  ? 242 LEU B CA  1 
ATOM   1590 C  C   . LEU A 1 269 ? -47.777 -32.638 24.845  1.00 47.02  ? 242 LEU B C   1 
ATOM   1591 O  O   . LEU A 1 269 ? -48.641 -33.110 24.153  1.00 45.86  ? 242 LEU B O   1 
ATOM   1592 C  CB  . LEU A 1 269 ? -46.428 -34.400 25.832  1.00 52.25  ? 242 LEU B CB  1 
ATOM   1593 C  CG  . LEU A 1 269 ? -46.059 -35.263 27.035  1.00 55.67  ? 242 LEU B CG  1 
ATOM   1594 C  CD1 . LEU A 1 269 ? -44.977 -36.239 26.612  1.00 58.60  ? 242 LEU B CD1 1 
ATOM   1595 C  CD2 . LEU A 1 269 ? -45.597 -34.407 28.206  1.00 56.86  ? 242 LEU B CD2 1 
ATOM   1596 N  N   . ILE A 1 270 ? -47.086 -31.568 24.493  1.00 51.90  ? 243 ILE B N   1 
ATOM   1597 C  CA  . ILE A 1 270 ? -47.269 -30.932 23.175  1.00 55.81  ? 243 ILE B CA  1 
ATOM   1598 C  C   . ILE A 1 270 ? -45.937 -30.605 22.568  1.00 56.62  ? 243 ILE B C   1 
ATOM   1599 O  O   . ILE A 1 270 ? -44.893 -30.839 23.198  1.00 52.61  ? 243 ILE B O   1 
ATOM   1600 C  CB  . ILE A 1 270 ? -48.024 -29.606 23.269  1.00 58.23  ? 243 ILE B CB  1 
ATOM   1601 C  CG1 . ILE A 1 270 ? -47.184 -28.600 24.059  1.00 58.21  ? 243 ILE B CG1 1 
ATOM   1602 C  CG2 . ILE A 1 270 ? -49.386 -29.852 23.898  1.00 59.66  ? 243 ILE B CG2 1 
ATOM   1603 C  CD1 . ILE A 1 270 ? -47.931 -27.353 24.454  1.00 62.18  ? 243 ILE B CD1 1 
ATOM   1604 N  N   . SER A 1 271 ? -45.984 -30.043 21.358  1.00 53.21  ? 244 SER B N   1 
ATOM   1605 C  CA  . SER A 1 271 ? -44.783 -29.630 20.658  1.00 52.58  ? 244 SER B CA  1 
ATOM   1606 C  C   . SER A 1 271 ? -45.086 -28.687 19.511  1.00 51.61  ? 244 SER B C   1 
ATOM   1607 O  O   . SER A 1 271 ? -46.185 -28.675 18.965  1.00 51.83  ? 244 SER B O   1 
ATOM   1608 C  CB  . SER A 1 271 ? -44.061 -30.872 20.123  1.00 55.90  ? 244 SER B CB  1 
ATOM   1609 O  OG  . SER A 1 271 ? -43.524 -30.642 18.837  1.00 66.50  ? 244 SER B OG  1 
ATOM   1610 N  N   . GLN A 1 272 ? -44.080 -27.927 19.118  1.00 52.61  ? 245 GLN B N   1 
ATOM   1611 C  CA  . GLN A 1 272 ? -44.138 -27.142 17.896  1.00 57.01  ? 245 GLN B CA  1 
ATOM   1612 C  C   . GLN A 1 272 ? -44.672 -27.935 16.698  1.00 54.78  ? 245 GLN B C   1 
ATOM   1613 O  O   . GLN A 1 272 ? -45.451 -27.389 15.935  1.00 54.47  ? 245 GLN B O   1 
ATOM   1614 C  CB  . GLN A 1 272 ? -42.751 -26.588 17.589  1.00 62.34  ? 245 GLN B CB  1 
ATOM   1615 C  CG  . GLN A 1 272 ? -42.676 -25.662 16.401  1.00 70.01  ? 245 GLN B CG  1 
ATOM   1616 C  CD  . GLN A 1 272 ? -41.347 -24.945 16.333  1.00 76.47  ? 245 GLN B CD  1 
ATOM   1617 O  OE1 . GLN A 1 272 ? -40.451 -25.222 17.121  1.00 88.63  ? 245 GLN B OE1 1 
ATOM   1618 N  NE2 . GLN A 1 272 ? -41.216 -24.013 15.400  1.00 78.64  ? 245 GLN B NE2 1 
ATOM   1619 N  N   . TYR A 1 273 ? -44.293 -29.211 16.566  1.00 56.49  ? 246 TYR B N   1 
ATOM   1620 C  CA  . TYR A 1 273 ? -44.672 -30.060 15.404  1.00 61.47  ? 246 TYR B CA  1 
ATOM   1621 C  C   . TYR A 1 273 ? -45.776 -31.063 15.644  1.00 63.36  ? 246 TYR B C   1 
ATOM   1622 O  O   . TYR A 1 273 ? -45.902 -32.001 14.870  1.00 75.86  ? 246 TYR B O   1 
ATOM   1623 C  CB  . TYR A 1 273 ? -43.435 -30.808 14.851  1.00 62.85  ? 246 TYR B CB  1 
ATOM   1624 C  CG  . TYR A 1 273 ? -42.387 -29.798 14.519  1.00 72.84  ? 246 TYR B CG  1 
ATOM   1625 C  CD1 . TYR A 1 273 ? -42.533 -28.974 13.410  1.00 72.23  ? 246 TYR B CD1 1 
ATOM   1626 C  CD2 . TYR A 1 273 ? -41.312 -29.574 15.374  1.00 74.67  ? 246 TYR B CD2 1 
ATOM   1627 C  CE1 . TYR A 1 273 ? -41.601 -27.994 13.122  1.00 78.89  ? 246 TYR B CE1 1 
ATOM   1628 C  CE2 . TYR A 1 273 ? -40.383 -28.591 15.097  1.00 78.20  ? 246 TYR B CE2 1 
ATOM   1629 C  CZ  . TYR A 1 273 ? -40.532 -27.804 13.973  1.00 75.62  ? 246 TYR B CZ  1 
ATOM   1630 O  OH  . TYR A 1 273 ? -39.619 -26.812 13.704  1.00 80.42  ? 246 TYR B OH  1 
ATOM   1631 N  N   . SER A 1 274 ? -46.587 -30.894 16.685  1.00 64.50  ? 247 SER B N   1 
ATOM   1632 C  CA  . SER A 1 274 ? -47.759 -31.778 16.877  1.00 62.21  ? 247 SER B CA  1 
ATOM   1633 C  C   . SER A 1 274 ? -48.739 -31.628 15.723  1.00 61.30  ? 247 SER B C   1 
ATOM   1634 O  O   . SER A 1 274 ? -48.991 -30.516 15.272  1.00 58.86  ? 247 SER B O   1 
ATOM   1635 C  CB  . SER A 1 274 ? -48.503 -31.468 18.182  1.00 58.50  ? 247 SER B CB  1 
ATOM   1636 O  OG  . SER A 1 274 ? -47.614 -31.031 19.180  1.00 61.17  ? 247 SER B OG  1 
ATOM   1637 N  N   . ASP A 1 275 ? -49.310 -32.735 15.260  1.00 67.42  ? 248 ASP B N   1 
ATOM   1638 C  CA  . ASP A 1 275 ? -50.323 -32.673 14.192  1.00 71.45  ? 248 ASP B CA  1 
ATOM   1639 C  C   . ASP A 1 275 ? -51.713 -32.281 14.730  1.00 70.79  ? 248 ASP B C   1 
ATOM   1640 O  O   . ASP A 1 275 ? -51.948 -32.253 15.933  1.00 79.67  ? 248 ASP B O   1 
ATOM   1641 C  CB  . ASP A 1 275 ? -50.368 -33.979 13.382  1.00 77.11  ? 248 ASP B CB  1 
ATOM   1642 C  CG  . ASP A 1 275 ? -50.663 -35.220 14.229  1.00 85.75  ? 248 ASP B CG  1 
ATOM   1643 O  OD1 . ASP A 1 275 ? -51.463 -35.145 15.187  1.00 90.34  ? 248 ASP B OD1 1 
ATOM   1644 O  OD2 . ASP A 1 275 ? -50.099 -36.293 13.904  1.00 100.36 ? 248 ASP B OD2 1 
ATOM   1645 N  N   . GLU A 1 276 ? -52.632 -31.976 13.831  1.00 70.45  ? 249 GLU B N   1 
ATOM   1646 C  CA  . GLU A 1 276 ? -53.955 -31.508 14.216  1.00 65.92  ? 249 GLU B CA  1 
ATOM   1647 C  C   . GLU A 1 276 ? -54.664 -32.523 15.135  1.00 62.94  ? 249 GLU B C   1 
ATOM   1648 O  O   . GLU A 1 276 ? -55.338 -32.135 16.082  1.00 69.15  ? 249 GLU B O   1 
ATOM   1649 C  CB  . GLU A 1 276 ? -54.789 -31.159 12.952  1.00 58.32  ? 249 GLU B CB  1 
ATOM   1650 N  N   . GLU A 1 277 ? -54.500 -33.813 14.879  1.00 63.73  ? 250 GLU B N   1 
ATOM   1651 C  CA  . GLU A 1 277 ? -55.203 -34.837 15.672  1.00 69.65  ? 250 GLU B CA  1 
ATOM   1652 C  C   . GLU A 1 277 ? -54.699 -34.816 17.117  1.00 71.35  ? 250 GLU B C   1 
ATOM   1653 O  O   . GLU A 1 277 ? -55.488 -34.903 18.058  1.00 70.63  ? 250 GLU B O   1 
ATOM   1654 C  CB  . GLU A 1 277 ? -55.045 -36.247 15.051  1.00 67.03  ? 250 GLU B CB  1 
ATOM   1655 N  N   . GLU A 1 278 ? -53.378 -34.697 17.274  1.00 72.38  ? 251 GLU B N   1 
ATOM   1656 C  CA  . GLU A 1 278 ? -52.734 -34.584 18.585  1.00 65.25  ? 251 GLU B CA  1 
ATOM   1657 C  C   . GLU A 1 278 ? -53.192 -33.329 19.323  1.00 61.94  ? 251 GLU B C   1 
ATOM   1658 O  O   . GLU A 1 278 ? -53.436 -33.393 20.526  1.00 56.72  ? 251 GLU B O   1 
ATOM   1659 C  CB  . GLU A 1 278 ? -51.207 -34.569 18.452  1.00 68.24  ? 251 GLU B CB  1 
ATOM   1660 C  CG  . GLU A 1 278 ? -50.575 -35.906 18.062  1.00 78.94  ? 251 GLU B CG  1 
ATOM   1661 C  CD  . GLU A 1 278 ? -49.145 -35.793 17.499  1.00 85.54  ? 251 GLU B CD  1 
ATOM   1662 O  OE1 . GLU A 1 278 ? -48.785 -34.754 16.898  1.00 82.17  ? 251 GLU B OE1 1 
ATOM   1663 O  OE2 . GLU A 1 278 ? -48.368 -36.764 17.640  1.00 89.67  ? 251 GLU B OE2 1 
ATOM   1664 N  N   . ILE A 1 279 ? -53.307 -32.196 18.621  1.00 60.05  ? 252 ILE B N   1 
ATOM   1665 C  CA  . ILE A 1 279 ? -53.819 -30.962 19.252  1.00 62.26  ? 252 ILE B CA  1 
ATOM   1666 C  C   . ILE A 1 279 ? -55.292 -31.155 19.674  1.00 68.83  ? 252 ILE B C   1 
ATOM   1667 O  O   . ILE A 1 279 ? -55.661 -30.899 20.839  1.00 68.67  ? 252 ILE B O   1 
ATOM   1668 C  CB  . ILE A 1 279 ? -53.715 -29.717 18.338  1.00 58.39  ? 252 ILE B CB  1 
ATOM   1669 C  CG1 . ILE A 1 279 ? -52.292 -29.450 17.922  1.00 60.19  ? 252 ILE B CG1 1 
ATOM   1670 C  CG2 . ILE A 1 279 ? -54.252 -28.479 19.033  1.00 57.87  ? 252 ILE B CG2 1 
ATOM   1671 C  CD1 . ILE A 1 279 ? -51.344 -29.333 19.089  1.00 69.57  ? 252 ILE B CD1 1 
ATOM   1672 N  N   . GLN A 1 280 ? -56.117 -31.635 18.741  1.00 65.14  ? 253 GLN B N   1 
ATOM   1673 C  CA  . GLN A 1 280 ? -57.530 -31.827 19.027  1.00 67.06  ? 253 GLN B CA  1 
ATOM   1674 C  C   . GLN A 1 280 ? -57.663 -32.612 20.328  1.00 61.96  ? 253 GLN B C   1 
ATOM   1675 O  O   . GLN A 1 280 ? -58.462 -32.268 21.188  1.00 67.45  ? 253 GLN B O   1 
ATOM   1676 C  CB  . GLN A 1 280 ? -58.267 -32.531 17.871  1.00 63.05  ? 253 GLN B CB  1 
ATOM   1677 N  N   . HIS A 1 281 ? -56.853 -33.647 20.479  1.00 61.47  ? 254 HIS B N   1 
ATOM   1678 C  CA  . HIS A 1 281 ? -56.942 -34.510 21.641  1.00 59.37  ? 254 HIS B CA  1 
ATOM   1679 C  C   . HIS A 1 281 ? -56.658 -33.739 22.930  1.00 60.59  ? 254 HIS B C   1 
ATOM   1680 O  O   . HIS A 1 281 ? -57.334 -33.953 23.940  1.00 57.58  ? 254 HIS B O   1 
ATOM   1681 C  CB  . HIS A 1 281 ? -55.977 -35.685 21.507  1.00 59.83  ? 254 HIS B CB  1 
ATOM   1682 C  CG  . HIS A 1 281 ? -56.038 -36.626 22.661  1.00 68.76  ? 254 HIS B CG  1 
ATOM   1683 N  ND1 . HIS A 1 281 ? -55.024 -36.733 23.588  1.00 76.81  ? 254 HIS B ND1 1 
ATOM   1684 C  CD2 . HIS A 1 281 ? -57.017 -37.462 23.079  1.00 76.27  ? 254 HIS B CD2 1 
ATOM   1685 C  CE1 . HIS A 1 281 ? -55.358 -37.619 24.509  1.00 73.10  ? 254 HIS B CE1 1 
ATOM   1686 N  NE2 . HIS A 1 281 ? -56.568 -38.069 24.228  1.00 78.19  ? 254 HIS B NE2 1 
ATOM   1687 N  N   . VAL A 1 282 ? -55.677 -32.832 22.899  1.00 55.34  ? 255 VAL B N   1 
ATOM   1688 C  CA  . VAL A 1 282 ? -55.279 -32.150 24.122  1.00 57.53  ? 255 VAL B CA  1 
ATOM   1689 C  C   . VAL A 1 282 ? -56.375 -31.189 24.542  1.00 56.95  ? 255 VAL B C   1 
ATOM   1690 O  O   . VAL A 1 282 ? -56.799 -31.170 25.701  1.00 54.38  ? 255 VAL B O   1 
ATOM   1691 C  CB  . VAL A 1 282 ? -53.950 -31.400 23.959  1.00 55.80  ? 255 VAL B CB  1 
ATOM   1692 C  CG1 . VAL A 1 282 ? -53.656 -30.559 25.176  1.00 58.26  ? 255 VAL B CG1 1 
ATOM   1693 C  CG2 . VAL A 1 282 ? -52.830 -32.381 23.801  1.00 55.20  ? 255 VAL B CG2 1 
ATOM   1694 N  N   . VAL A 1 283 ? -56.842 -30.424 23.564  1.00 57.45  ? 256 VAL B N   1 
ATOM   1695 C  CA  . VAL A 1 283 ? -57.967 -29.528 23.742  1.00 56.11  ? 256 VAL B CA  1 
ATOM   1696 C  C   . VAL A 1 283 ? -59.205 -30.269 24.230  1.00 58.91  ? 256 VAL B C   1 
ATOM   1697 O  O   . VAL A 1 283 ? -59.988 -29.712 24.982  1.00 58.05  ? 256 VAL B O   1 
ATOM   1698 C  CB  . VAL A 1 283 ? -58.339 -28.823 22.444  1.00 57.35  ? 256 VAL B CB  1 
ATOM   1699 C  CG1 . VAL A 1 283 ? -59.349 -27.738 22.730  1.00 62.74  ? 256 VAL B CG1 1 
ATOM   1700 C  CG2 . VAL A 1 283 ? -57.130 -28.179 21.804  1.00 63.90  ? 256 VAL B CG2 1 
ATOM   1701 N  N   . GLU A 1 284 ? -59.400 -31.517 23.808  1.00 63.66  ? 257 GLU B N   1 
ATOM   1702 C  CA  . GLU A 1 284 ? -60.559 -32.296 24.282  1.00 72.81  ? 257 GLU B CA  1 
ATOM   1703 C  C   . GLU A 1 284 ? -60.419 -32.633 25.761  1.00 72.39  ? 257 GLU B C   1 
ATOM   1704 O  O   . GLU A 1 284 ? -61.329 -32.365 26.567  1.00 67.57  ? 257 GLU B O   1 
ATOM   1705 C  CB  . GLU A 1 284 ? -60.772 -33.575 23.465  1.00 76.32  ? 257 GLU B CB  1 
ATOM   1706 C  CG  . GLU A 1 284 ? -61.530 -33.331 22.172  1.00 83.72  ? 257 GLU B CG  1 
ATOM   1707 C  CD  . GLU A 1 284 ? -61.676 -34.581 21.333  1.00 91.85  ? 257 GLU B CD  1 
ATOM   1708 O  OE1 . GLU A 1 284 ? -62.273 -35.558 21.846  1.00 103.82 ? 257 GLU B OE1 1 
ATOM   1709 O  OE2 . GLU A 1 284 ? -61.200 -34.575 20.168  1.00 85.08  ? 257 GLU B OE2 1 
ATOM   1710 N  N   . VAL A 1 285 ? -59.266 -33.193 26.110  1.00 65.10  ? 258 VAL B N   1 
ATOM   1711 C  CA  . VAL A 1 285 ? -58.950 -33.457 27.501  1.00 61.58  ? 258 VAL B CA  1 
ATOM   1712 C  C   . VAL A 1 285 ? -59.208 -32.206 28.352  1.00 59.94  ? 258 VAL B C   1 
ATOM   1713 O  O   . VAL A 1 285 ? -59.816 -32.286 29.416  1.00 56.11  ? 258 VAL B O   1 
ATOM   1714 C  CB  . VAL A 1 285 ? -57.491 -33.898 27.663  1.00 61.90  ? 258 VAL B CB  1 
ATOM   1715 C  CG1 . VAL A 1 285 ? -57.114 -33.942 29.135  1.00 67.52  ? 258 VAL B CG1 1 
ATOM   1716 C  CG2 . VAL A 1 285 ? -57.262 -35.264 27.037  1.00 61.61  ? 258 VAL B CG2 1 
ATOM   1717 N  N   . ILE A 1 286 ? -58.763 -31.055 27.863  1.00 55.32  ? 259 ILE B N   1 
ATOM   1718 C  CA  . ILE A 1 286 ? -58.978 -29.814 28.571  1.00 57.91  ? 259 ILE B CA  1 
ATOM   1719 C  C   . ILE A 1 286 ? -60.485 -29.519 28.690  1.00 57.84  ? 259 ILE B C   1 
ATOM   1720 O  O   . ILE A 1 286 ? -61.011 -29.361 29.783  1.00 56.33  ? 259 ILE B O   1 
ATOM   1721 C  CB  . ILE A 1 286 ? -58.229 -28.646 27.876  1.00 61.77  ? 259 ILE B CB  1 
ATOM   1722 C  CG1 . ILE A 1 286 ? -56.718 -28.825 27.979  1.00 60.52  ? 259 ILE B CG1 1 
ATOM   1723 C  CG2 . ILE A 1 286 ? -58.583 -27.303 28.511  1.00 63.74  ? 259 ILE B CG2 1 
ATOM   1724 C  CD1 . ILE A 1 286 ? -55.924 -27.840 27.149  1.00 59.97  ? 259 ILE B CD1 1 
ATOM   1725 N  N   . GLN A 1 287 ? -61.171 -29.448 27.554  1.00 62.21  ? 260 GLN B N   1 
ATOM   1726 C  CA  . GLN A 1 287 ? -62.617 -29.208 27.525  1.00 61.10  ? 260 GLN B CA  1 
ATOM   1727 C  C   . GLN A 1 287 ? -63.348 -30.158 28.462  1.00 60.23  ? 260 GLN B C   1 
ATOM   1728 O  O   . GLN A 1 287 ? -64.286 -29.765 29.122  1.00 57.51  ? 260 GLN B O   1 
ATOM   1729 C  CB  . GLN A 1 287 ? -63.172 -29.396 26.109  1.00 65.37  ? 260 GLN B CB  1 
ATOM   1730 C  CG  . GLN A 1 287 ? -63.098 -28.168 25.211  1.00 69.08  ? 260 GLN B CG  1 
ATOM   1731 C  CD  . GLN A 1 287 ? -63.600 -28.433 23.782  1.00 75.57  ? 260 GLN B CD  1 
ATOM   1732 O  OE1 . GLN A 1 287 ? -63.302 -29.475 23.174  1.00 77.69  ? 260 GLN B OE1 1 
ATOM   1733 N  NE2 . GLN A 1 287 ? -64.345 -27.476 23.230  1.00 77.03  ? 260 GLN B NE2 1 
ATOM   1734 N  N   . ASN A 1 288 ? -62.904 -31.411 28.520  1.00 60.49  ? 261 ASN B N   1 
ATOM   1735 C  CA  . ASN A 1 288 ? -63.588 -32.432 29.292  1.00 59.98  ? 261 ASN B CA  1 
ATOM   1736 C  C   . ASN A 1 288 ? -63.268 -32.446 30.782  1.00 60.89  ? 261 ASN B C   1 
ATOM   1737 O  O   . ASN A 1 288 ? -63.732 -33.338 31.487  1.00 60.21  ? 261 ASN B O   1 
ATOM   1738 C  CB  . ASN A 1 288 ? -63.279 -33.812 28.703  1.00 65.30  ? 261 ASN B CB  1 
ATOM   1739 C  CG  . ASN A 1 288 ? -63.943 -34.033 27.355  1.00 75.73  ? 261 ASN B CG  1 
ATOM   1740 O  OD1 . ASN A 1 288 ? -64.475 -33.095 26.732  1.00 78.38  ? 261 ASN B OD1 1 
ATOM   1741 N  ND2 . ASN A 1 288 ? -63.911 -35.283 26.889  1.00 83.92  ? 261 ASN B ND2 1 
ATOM   1742 N  N   . SER A 1 289 ? -62.496 -31.474 31.274  1.00 61.18  ? 262 SER B N   1 
ATOM   1743 C  CA  . SER A 1 289 ? -62.030 -31.492 32.661  1.00 58.20  ? 262 SER B CA  1 
ATOM   1744 C  C   . SER A 1 289 ? -62.564 -30.335 33.487  1.00 60.42  ? 262 SER B C   1 
ATOM   1745 O  O   . SER A 1 289 ? -62.621 -29.193 33.021  1.00 60.18  ? 262 SER B O   1 
ATOM   1746 C  CB  . SER A 1 289 ? -60.506 -31.466 32.706  1.00 61.00  ? 262 SER B CB  1 
ATOM   1747 O  OG  . SER A 1 289 ? -60.021 -31.320 34.040  1.00 60.97  ? 262 SER B OG  1 
ATOM   1748 N  N   . THR A 1 290 ? -62.922 -30.625 34.737  1.00 66.86  ? 263 THR B N   1 
ATOM   1749 C  CA  . THR A 1 290 ? -63.386 -29.574 35.649  1.00 73.19  ? 263 THR B CA  1 
ATOM   1750 C  C   . THR A 1 290 ? -62.271 -28.616 36.088  1.00 71.43  ? 263 THR B C   1 
ATOM   1751 O  O   . THR A 1 290 ? -62.556 -27.586 36.673  1.00 83.44  ? 263 THR B O   1 
ATOM   1752 C  CB  . THR A 1 290 ? -64.082 -30.153 36.905  1.00 77.77  ? 263 THR B CB  1 
ATOM   1753 O  OG1 . THR A 1 290 ? -63.286 -31.197 37.477  1.00 89.04  ? 263 THR B OG1 1 
ATOM   1754 C  CG2 . THR A 1 290 ? -65.426 -30.713 36.538  1.00 82.16  ? 263 THR B CG2 1 
ATOM   1755 N  N   . ALA A 1 291 ? -61.014 -28.953 35.806  1.00 71.14  ? 264 ALA B N   1 
ATOM   1756 C  CA  . ALA A 1 291 ? -59.868 -28.142 36.227  1.00 61.88  ? 264 ALA B CA  1 
ATOM   1757 C  C   . ALA A 1 291 ? -59.889 -26.776 35.597  1.00 52.07  ? 264 ALA B C   1 
ATOM   1758 O  O   . ALA A 1 291 ? -60.094 -26.649 34.407  1.00 51.69  ? 264 ALA B O   1 
ATOM   1759 C  CB  . ALA A 1 291 ? -58.565 -28.841 35.872  1.00 60.06  ? 264 ALA B CB  1 
ATOM   1760 N  N   . LYS A 1 292 ? -59.658 -25.776 36.424  1.00 51.59  ? 265 LYS B N   1 
ATOM   1761 C  CA  . LYS A 1 292 ? -59.630 -24.383 36.024  1.00 57.27  ? 265 LYS B CA  1 
ATOM   1762 C  C   . LYS A 1 292 ? -58.154 -23.936 35.944  1.00 58.02  ? 265 LYS B C   1 
ATOM   1763 O  O   . LYS A 1 292 ? -57.797 -23.069 35.116  1.00 61.34  ? 265 LYS B O   1 
ATOM   1764 C  CB  . LYS A 1 292 ? -60.416 -23.523 37.057  1.00 56.51  ? 265 LYS B CB  1 
ATOM   1765 C  CG  . LYS A 1 292 ? -60.897 -22.143 36.584  1.00 61.70  ? 265 LYS B CG  1 
ATOM   1766 C  CD  . LYS A 1 292 ? -60.968 -21.097 37.722  1.00 68.01  ? 265 LYS B CD  1 
ATOM   1767 C  CE  . LYS A 1 292 ? -62.050 -20.005 37.562  1.00 65.38  ? 265 LYS B CE  1 
ATOM   1768 N  NZ  . LYS A 1 292 ? -61.869 -19.035 36.434  1.00 65.41  ? 265 LYS B NZ  1 
ATOM   1769 N  N   . VAL A 1 293 ? -57.306 -24.512 36.803  1.00 51.16  ? 266 VAL B N   1 
ATOM   1770 C  CA  . VAL A 1 293 ? -55.890 -24.152 36.849  1.00 54.37  ? 266 VAL B CA  1 
ATOM   1771 C  C   . VAL A 1 293 ? -55.033 -25.116 36.037  1.00 55.38  ? 266 VAL B C   1 
ATOM   1772 O  O   . VAL A 1 293 ? -55.013 -26.320 36.285  1.00 52.56  ? 266 VAL B O   1 
ATOM   1773 C  CB  . VAL A 1 293 ? -55.358 -24.072 38.283  1.00 53.00  ? 266 VAL B CB  1 
ATOM   1774 C  CG1 . VAL A 1 293 ? -53.864 -23.812 38.291  1.00 52.62  ? 266 VAL B CG1 1 
ATOM   1775 C  CG2 . VAL A 1 293 ? -56.058 -22.946 39.008  1.00 59.29  ? 266 VAL B CG2 1 
ATOM   1776 N  N   . ILE A 1 294 ? -54.291 -24.564 35.088  1.00 54.80  ? 267 ILE B N   1 
ATOM   1777 C  CA  . ILE A 1 294 ? -53.524 -25.381 34.173  1.00 52.50  ? 267 ILE B CA  1 
ATOM   1778 C  C   . ILE A 1 294 ? -52.093 -24.911 34.212  1.00 48.33  ? 267 ILE B C   1 
ATOM   1779 O  O   . ILE A 1 294 ? -51.811 -23.748 33.915  1.00 47.51  ? 267 ILE B O   1 
ATOM   1780 C  CB  . ILE A 1 294 ? -54.098 -25.278 32.768  1.00 52.79  ? 267 ILE B CB  1 
ATOM   1781 C  CG1 . ILE A 1 294 ? -55.561 -25.755 32.809  1.00 55.51  ? 267 ILE B CG1 1 
ATOM   1782 C  CG2 . ILE A 1 294 ? -53.259 -26.077 31.786  1.00 49.84  ? 267 ILE B CG2 1 
ATOM   1783 C  CD1 . ILE A 1 294 ? -56.227 -25.803 31.442  1.00 57.18  ? 267 ILE B CD1 1 
ATOM   1784 N  N   . VAL A 1 295 ? -51.212 -25.820 34.630  1.00 47.13  ? 268 VAL B N   1 
ATOM   1785 C  CA  . VAL A 1 295 ? -49.790 -25.567 34.711  1.00 45.99  ? 268 VAL B CA  1 
ATOM   1786 C  C   . VAL A 1 295 ? -49.149 -26.004 33.412  1.00 45.47  ? 268 VAL B C   1 
ATOM   1787 O  O   . VAL A 1 295 ? -49.322 -27.147 33.004  1.00 48.16  ? 268 VAL B O   1 
ATOM   1788 C  CB  . VAL A 1 295 ? -49.167 -26.392 35.824  1.00 43.42  ? 268 VAL B CB  1 
ATOM   1789 C  CG1 . VAL A 1 295 ? -47.669 -26.170 35.870  1.00 40.80  ? 268 VAL B CG1 1 
ATOM   1790 C  CG2 . VAL A 1 295 ? -49.817 -26.035 37.145  1.00 44.35  ? 268 VAL B CG2 1 
ATOM   1791 N  N   . VAL A 1 296 ? -48.413 -25.097 32.784  1.00 42.93  ? 269 VAL B N   1 
ATOM   1792 C  CA  . VAL A 1 296 ? -47.805 -25.339 31.493  1.00 44.78  ? 269 VAL B CA  1 
ATOM   1793 C  C   . VAL A 1 296 ? -46.298 -25.101 31.532  1.00 46.16  ? 269 VAL B C   1 
ATOM   1794 O  O   . VAL A 1 296 ? -45.850 -24.002 31.844  1.00 51.21  ? 269 VAL B O   1 
ATOM   1795 C  CB  . VAL A 1 296 ? -48.409 -24.403 30.443  1.00 49.46  ? 269 VAL B CB  1 
ATOM   1796 C  CG1 . VAL A 1 296 ? -47.873 -24.743 29.055  1.00 48.38  ? 269 VAL B CG1 1 
ATOM   1797 C  CG2 . VAL A 1 296 ? -49.947 -24.449 30.497  1.00 47.98  ? 269 VAL B CG2 1 
ATOM   1798 N  N   . PHE A 1 297 ? -45.525 -26.141 31.213  1.00 47.14  ? 270 PHE B N   1 
ATOM   1799 C  CA  . PHE A 1 297 ? -44.075 -26.093 31.226  1.00 44.67  ? 270 PHE B CA  1 
ATOM   1800 C  C   . PHE A 1 297 ? -43.532 -26.211 29.810  1.00 45.32  ? 270 PHE B C   1 
ATOM   1801 O  O   . PHE A 1 297 ? -43.385 -27.308 29.274  1.00 45.07  ? 270 PHE B O   1 
ATOM   1802 C  CB  . PHE A 1 297 ? -43.540 -27.202 32.097  1.00 45.93  ? 270 PHE B CB  1 
ATOM   1803 C  CG  . PHE A 1 297 ? -42.485 -26.740 33.058  1.00 53.52  ? 270 PHE B CG  1 
ATOM   1804 C  CD1 . PHE A 1 297 ? -41.245 -26.277 32.580  1.00 53.16  ? 270 PHE B CD1 1 
ATOM   1805 C  CD2 . PHE A 1 297 ? -42.725 -26.738 34.437  1.00 53.63  ? 270 PHE B CD2 1 
ATOM   1806 C  CE1 . PHE A 1 297 ? -40.264 -25.843 33.449  1.00 51.51  ? 270 PHE B CE1 1 
ATOM   1807 C  CE2 . PHE A 1 297 ? -41.750 -26.277 35.307  1.00 58.99  ? 270 PHE B CE2 1 
ATOM   1808 C  CZ  . PHE A 1 297 ? -40.518 -25.838 34.813  1.00 56.65  ? 270 PHE B CZ  1 
ATOM   1809 N  N   . SER A 1 298 ? -43.257 -25.076 29.186  1.00 42.82  ? 271 SER B N   1 
ATOM   1810 C  CA  . SER A 1 298 ? -42.999 -25.092 27.761  1.00 43.35  ? 271 SER B CA  1 
ATOM   1811 C  C   . SER A 1 298 ? -42.484 -23.785 27.240  1.00 44.26  ? 271 SER B C   1 
ATOM   1812 O  O   . SER A 1 298 ? -42.664 -22.736 27.843  1.00 50.43  ? 271 SER B O   1 
ATOM   1813 C  CB  . SER A 1 298 ? -44.292 -25.384 27.025  1.00 42.11  ? 271 SER B CB  1 
ATOM   1814 O  OG  . SER A 1 298 ? -44.146 -25.138 25.646  1.00 38.57  ? 271 SER B OG  1 
ATOM   1815 N  N   . SER A 1 299 ? -41.853 -23.862 26.091  1.00 43.60  ? 272 SER B N   1 
ATOM   1816 C  CA  . SER A 1 299 ? -41.433 -22.685 25.361  1.00 43.61  ? 272 SER B CA  1 
ATOM   1817 C  C   . SER A 1 299 ? -42.619 -22.151 24.583  1.00 44.91  ? 272 SER B C   1 
ATOM   1818 O  O   . SER A 1 299 ? -43.635 -22.844 24.442  1.00 40.15  ? 272 SER B O   1 
ATOM   1819 C  CB  . SER A 1 299 ? -40.371 -23.072 24.362  1.00 42.95  ? 272 SER B CB  1 
ATOM   1820 O  OG  . SER A 1 299 ? -40.929 -23.980 23.406  1.00 45.87  ? 272 SER B OG  1 
ATOM   1821 N  N   . GLY A 1 300 ? -42.462 -20.930 24.062  1.00 45.01  ? 273 GLY B N   1 
ATOM   1822 C  CA  . GLY A 1 300 ? -43.469 -20.290 23.218  1.00 46.61  ? 273 GLY B CA  1 
ATOM   1823 C  C   . GLY A 1 300 ? -43.734 -21.126 21.987  1.00 46.38  ? 273 GLY B C   1 
ATOM   1824 O  O   . GLY A 1 300 ? -44.872 -21.568 21.730  1.00 46.87  ? 273 GLY B O   1 
ATOM   1825 N  N   . PRO A 1 301 ? -42.673 -21.414 21.252  1.00 46.44  ? 274 PRO B N   1 
ATOM   1826 C  CA  . PRO A 1 301 ? -42.893 -22.123 20.013  1.00 45.57  ? 274 PRO B CA  1 
ATOM   1827 C  C   . PRO A 1 301 ? -43.568 -23.467 20.213  1.00 46.01  ? 274 PRO B C   1 
ATOM   1828 O  O   . PRO A 1 301 ? -44.441 -23.810 19.427  1.00 45.17  ? 274 PRO B O   1 
ATOM   1829 C  CB  . PRO A 1 301 ? -41.490 -22.230 19.420  1.00 44.38  ? 274 PRO B CB  1 
ATOM   1830 C  CG  . PRO A 1 301 ? -40.728 -21.067 20.005  1.00 42.73  ? 274 PRO B CG  1 
ATOM   1831 C  CD  . PRO A 1 301 ? -41.285 -20.932 21.385  1.00 46.83  ? 274 PRO B CD  1 
ATOM   1832 N  N   . ASP A 1 302 ? -43.239 -24.203 21.267  1.00 50.35  ? 275 ASP B N   1 
ATOM   1833 C  CA  . ASP A 1 302 ? -43.939 -25.497 21.496  1.00 59.39  ? 275 ASP B CA  1 
ATOM   1834 C  C   . ASP A 1 302 ? -45.408 -25.401 21.979  1.00 52.14  ? 275 ASP B C   1 
ATOM   1835 O  O   . ASP A 1 302 ? -46.142 -26.369 21.926  1.00 50.93  ? 275 ASP B O   1 
ATOM   1836 C  CB  . ASP A 1 302 ? -43.135 -26.388 22.445  1.00 61.45  ? 275 ASP B CB  1 
ATOM   1837 C  CG  . ASP A 1 302 ? -41.784 -26.747 21.871  1.00 70.71  ? 275 ASP B CG  1 
ATOM   1838 O  OD1 . ASP A 1 302 ? -41.742 -27.198 20.699  1.00 65.51  ? 275 ASP B OD1 1 
ATOM   1839 O  OD2 . ASP A 1 302 ? -40.769 -26.566 22.584  1.00 77.08  ? 275 ASP B OD2 1 
ATOM   1840 N  N   . LEU A 1 303 ? -45.808 -24.230 22.444  1.00 50.87  ? 276 LEU B N   1 
ATOM   1841 C  CA  . LEU A 1 303 ? -47.138 -23.997 22.976  1.00 54.01  ? 276 LEU B CA  1 
ATOM   1842 C  C   . LEU A 1 303 ? -48.108 -23.298 21.974  1.00 58.11  ? 276 LEU B C   1 
ATOM   1843 O  O   . LEU A 1 303 ? -49.329 -23.441 22.085  1.00 56.09  ? 276 LEU B O   1 
ATOM   1844 C  CB  . LEU A 1 303 ? -46.992 -23.129 24.215  1.00 53.24  ? 276 LEU B CB  1 
ATOM   1845 C  CG  . LEU A 1 303 ? -48.261 -22.743 24.947  1.00 48.22  ? 276 LEU B CG  1 
ATOM   1846 C  CD1 . LEU A 1 303 ? -48.960 -24.011 25.371  1.00 49.55  ? 276 LEU B CD1 1 
ATOM   1847 C  CD2 . LEU A 1 303 ? -47.936 -21.854 26.140  1.00 46.58  ? 276 LEU B CD2 1 
ATOM   1848 N  N   . GLU A 1 304 ? -47.559 -22.563 21.005  1.00 58.88  ? 277 GLU B N   1 
ATOM   1849 C  CA  . GLU A 1 304 ? -48.357 -21.734 20.087  1.00 60.28  ? 277 GLU B CA  1 
ATOM   1850 C  C   . GLU A 1 304 ? -49.459 -22.504 19.326  1.00 55.81  ? 277 GLU B C   1 
ATOM   1851 O  O   . GLU A 1 304 ? -50.589 -22.044 19.277  1.00 62.26  ? 277 GLU B O   1 
ATOM   1852 C  CB  . GLU A 1 304 ? -47.451 -20.905 19.148  1.00 60.05  ? 277 GLU B CB  1 
ATOM   1853 C  CG  . GLU A 1 304 ? -48.199 -20.230 18.017  1.00 67.33  ? 277 GLU B CG  1 
ATOM   1854 C  CD  . GLU A 1 304 ? -47.353 -19.249 17.205  1.00 74.31  ? 277 GLU B CD  1 
ATOM   1855 O  OE1 . GLU A 1 304 ? -46.359 -19.702 16.596  1.00 70.18  ? 277 GLU B OE1 1 
ATOM   1856 O  OE2 . GLU A 1 304 ? -47.696 -18.030 17.149  1.00 72.96  ? 277 GLU B OE2 1 
ATOM   1857 N  N   . PRO A 1 305 ? -49.153 -23.672 18.754  1.00 53.36  ? 278 PRO B N   1 
ATOM   1858 C  CA  . PRO A 1 305 ? -50.241 -24.460 18.153  1.00 52.60  ? 278 PRO B CA  1 
ATOM   1859 C  C   . PRO A 1 305 ? -51.373 -24.820 19.129  1.00 53.45  ? 278 PRO B C   1 
ATOM   1860 O  O   . PRO A 1 305 ? -52.528 -24.723 18.766  1.00 57.82  ? 278 PRO B O   1 
ATOM   1861 C  CB  . PRO A 1 305 ? -49.556 -25.757 17.674  1.00 51.07  ? 278 PRO B CB  1 
ATOM   1862 C  CG  . PRO A 1 305 ? -48.098 -25.458 17.648  1.00 53.10  ? 278 PRO B CG  1 
ATOM   1863 C  CD  . PRO A 1 305 ? -47.838 -24.322 18.605  1.00 55.78  ? 278 PRO B CD  1 
ATOM   1864 N  N   . LEU A 1 306 ? -51.075 -25.246 20.346  1.00 55.95  ? 279 LEU B N   1 
ATOM   1865 C  CA  . LEU A 1 306 ? -52.172 -25.582 21.251  1.00 58.81  ? 279 LEU B CA  1 
ATOM   1866 C  C   . LEU A 1 306 ? -52.984 -24.340 21.492  1.00 56.79  ? 279 LEU B C   1 
ATOM   1867 O  O   . LEU A 1 306 ? -54.168 -24.380 21.362  1.00 58.95  ? 279 LEU B O   1 
ATOM   1868 C  CB  . LEU A 1 306 ? -51.698 -26.149 22.576  1.00 63.82  ? 279 LEU B CB  1 
ATOM   1869 C  CG  . LEU A 1 306 ? -52.774 -26.314 23.668  1.00 65.93  ? 279 LEU B CG  1 
ATOM   1870 C  CD1 . LEU A 1 306 ? -53.792 -27.378 23.316  1.00 61.43  ? 279 LEU B CD1 1 
ATOM   1871 C  CD2 . LEU A 1 306 ? -52.098 -26.637 24.996  1.00 64.26  ? 279 LEU B CD2 1 
ATOM   1872 N  N   . ILE A 1 307 ? -52.335 -23.231 21.809  1.00 58.83  ? 280 ILE B N   1 
ATOM   1873 C  CA  . ILE A 1 307 ? -53.043 -21.989 22.100  1.00 61.41  ? 280 ILE B CA  1 
ATOM   1874 C  C   . ILE A 1 307 ? -53.902 -21.495 20.941  1.00 59.43  ? 280 ILE B C   1 
ATOM   1875 O  O   . ILE A 1 307 ? -55.016 -21.054 21.152  1.00 50.45  ? 280 ILE B O   1 
ATOM   1876 C  CB  . ILE A 1 307 ? -52.062 -20.901 22.534  1.00 63.79  ? 280 ILE B CB  1 
ATOM   1877 C  CG1 . ILE A 1 307 ? -51.538 -21.229 23.939  1.00 70.95  ? 280 ILE B CG1 1 
ATOM   1878 C  CG2 . ILE A 1 307 ? -52.705 -19.530 22.506  1.00 64.65  ? 280 ILE B CG2 1 
ATOM   1879 C  CD1 . ILE A 1 307 ? -52.567 -21.213 25.055  1.00 70.66  ? 280 ILE B CD1 1 
ATOM   1880 N  N   . LYS A 1 308 ? -53.395 -21.570 19.721  1.00 62.42  ? 281 LYS B N   1 
ATOM   1881 C  CA  . LYS A 1 308 ? -54.201 -21.178 18.572  1.00 60.37  ? 281 LYS B CA  1 
ATOM   1882 C  C   . LYS A 1 308 ? -55.536 -21.909 18.560  1.00 56.82  ? 281 LYS B C   1 
ATOM   1883 O  O   . LYS A 1 308 ? -56.576 -21.294 18.408  1.00 60.31  ? 281 LYS B O   1 
ATOM   1884 C  CB  . LYS A 1 308 ? -53.444 -21.398 17.267  1.00 58.11  ? 281 LYS B CB  1 
ATOM   1885 C  CG  . LYS A 1 308 ? -52.411 -20.316 17.043  1.00 65.52  ? 281 LYS B CG  1 
ATOM   1886 C  CD  . LYS A 1 308 ? -51.667 -20.479 15.727  1.00 70.86  ? 281 LYS B CD  1 
ATOM   1887 C  CE  . LYS A 1 308 ? -50.764 -19.273 15.483  1.00 77.97  ? 281 LYS B CE  1 
ATOM   1888 N  NZ  . LYS A 1 308 ? -49.667 -19.520 14.505  1.00 83.54  ? 281 LYS B NZ  1 
ATOM   1889 N  N   . GLU A 1 309 ? -55.522 -23.213 18.745  1.00 56.03  ? 282 GLU B N   1 
ATOM   1890 C  CA  . GLU A 1 309 ? -56.780 -23.974 18.773  1.00 62.31  ? 282 GLU B CA  1 
ATOM   1891 C  C   . GLU A 1 309 ? -57.702 -23.643 19.972  1.00 64.21  ? 282 GLU B C   1 
ATOM   1892 O  O   . GLU A 1 309 ? -58.922 -23.689 19.862  1.00 70.04  ? 282 GLU B O   1 
ATOM   1893 C  CB  . GLU A 1 309 ? -56.486 -25.464 18.787  1.00 60.69  ? 282 GLU B CB  1 
ATOM   1894 C  CG  . GLU A 1 309 ? -57.713 -26.324 18.566  1.00 70.75  ? 282 GLU B CG  1 
ATOM   1895 C  CD  . GLU A 1 309 ? -58.383 -26.113 17.213  1.00 75.15  ? 282 GLU B CD  1 
ATOM   1896 O  OE1 . GLU A 1 309 ? -59.545 -26.567 17.079  1.00 77.41  ? 282 GLU B OE1 1 
ATOM   1897 O  OE2 . GLU A 1 309 ? -57.758 -25.519 16.294  1.00 76.10  ? 282 GLU B OE2 1 
ATOM   1898 N  N   . ILE A 1 310 ? -57.110 -23.320 21.108  1.00 60.73  ? 283 ILE B N   1 
ATOM   1899 C  CA  . ILE A 1 310 ? -57.850 -23.029 22.311  1.00 62.03  ? 283 ILE B CA  1 
ATOM   1900 C  C   . ILE A 1 310 ? -58.577 -21.698 22.127  1.00 59.28  ? 283 ILE B C   1 
ATOM   1901 O  O   . ILE A 1 310 ? -59.712 -21.529 22.539  1.00 59.69  ? 283 ILE B O   1 
ATOM   1902 C  CB  . ILE A 1 310 ? -56.897 -23.040 23.531  1.00 62.44  ? 283 ILE B CB  1 
ATOM   1903 C  CG1 . ILE A 1 310 ? -56.564 -24.494 23.870  1.00 71.47  ? 283 ILE B CG1 1 
ATOM   1904 C  CG2 . ILE A 1 310 ? -57.526 -22.395 24.756  1.00 68.95  ? 283 ILE B CG2 1 
ATOM   1905 C  CD1 . ILE A 1 310 ? -55.662 -24.715 25.075  1.00 76.07  ? 283 ILE B CD1 1 
ATOM   1906 N  N   . VAL A 1 311 ? -57.897 -20.769 21.492  1.00 59.48  ? 284 VAL B N   1 
ATOM   1907 C  CA  . VAL A 1 311 ? -58.481 -19.507 21.062  1.00 59.29  ? 284 VAL B CA  1 
ATOM   1908 C  C   . VAL A 1 311 ? -59.569 -19.703 19.994  1.00 61.54  ? 284 VAL B C   1 
ATOM   1909 O  O   . VAL A 1 311 ? -60.593 -19.035 20.021  1.00 61.86  ? 284 VAL B O   1 
ATOM   1910 C  CB  . VAL A 1 311 ? -57.383 -18.599 20.506  1.00 51.82  ? 284 VAL B CB  1 
ATOM   1911 C  CG1 . VAL A 1 311 ? -57.981 -17.374 19.897  1.00 52.31  ? 284 VAL B CG1 1 
ATOM   1912 C  CG2 . VAL A 1 311 ? -56.420 -18.215 21.611  1.00 54.38  ? 284 VAL B CG2 1 
ATOM   1913 N  N   . ARG A 1 312 ? -59.345 -20.627 19.071  1.00 66.03  ? 285 ARG B N   1 
ATOM   1914 C  CA  . ARG A 1 312 ? -60.313 -20.913 18.011  1.00 69.01  ? 285 ARG B CA  1 
ATOM   1915 C  C   . ARG A 1 312 ? -61.615 -21.441 18.609  1.00 69.09  ? 285 ARG B C   1 
ATOM   1916 O  O   . ARG A 1 312 ? -62.687 -21.082 18.173  1.00 81.09  ? 285 ARG B O   1 
ATOM   1917 C  CB  . ARG A 1 312 ? -59.746 -21.931 17.017  1.00 73.11  ? 285 ARG B CB  1 
ATOM   1918 C  CG  . ARG A 1 312 ? -59.856 -21.554 15.542  1.00 82.38  ? 285 ARG B CG  1 
ATOM   1919 C  CD  . ARG A 1 312 ? -59.896 -22.804 14.660  1.00 86.21  ? 285 ARG B CD  1 
ATOM   1920 N  NE  . ARG A 1 312 ? -61.083 -23.590 15.006  1.00 96.23  ? 285 ARG B NE  1 
ATOM   1921 C  CZ  . ARG A 1 312 ? -61.197 -24.915 14.932  1.00 99.36  ? 285 ARG B CZ  1 
ATOM   1922 N  NH1 . ARG A 1 312 ? -62.342 -25.491 15.310  1.00 92.25  ? 285 ARG B NH1 1 
ATOM   1923 N  NH2 . ARG A 1 312 ? -60.183 -25.669 14.501  1.00 105.85 ? 285 ARG B NH2 1 
ATOM   1924 N  N   . ARG A 1 313 ? -61.528 -22.282 19.623  1.00 67.16  ? 286 ARG B N   1 
ATOM   1925 C  CA  . ARG A 1 313 ? -62.724 -22.811 20.253  1.00 63.85  ? 286 ARG B CA  1 
ATOM   1926 C  C   . ARG A 1 313 ? -63.179 -21.983 21.453  1.00 64.40  ? 286 ARG B C   1 
ATOM   1927 O  O   . ARG A 1 313 ? -63.972 -22.422 22.250  1.00 63.70  ? 286 ARG B O   1 
ATOM   1928 C  CB  . ARG A 1 313 ? -62.461 -24.236 20.680  1.00 67.35  ? 286 ARG B CB  1 
ATOM   1929 C  CG  . ARG A 1 313 ? -61.963 -25.101 19.541  1.00 69.16  ? 286 ARG B CG  1 
ATOM   1930 C  CD  . ARG A 1 313 ? -62.249 -26.549 19.870  1.00 77.65  ? 286 ARG B CD  1 
ATOM   1931 N  NE  . ARG A 1 313 ? -61.587 -27.475 18.967  1.00 84.33  ? 286 ARG B NE  1 
ATOM   1932 C  CZ  . ARG A 1 313 ? -61.746 -28.796 19.010  1.00 93.22  ? 286 ARG B CZ  1 
ATOM   1933 N  NH1 . ARG A 1 313 ? -62.560 -29.345 19.913  1.00 95.08  ? 286 ARG B NH1 1 
ATOM   1934 N  NH2 . ARG A 1 313 ? -61.082 -29.579 18.156  1.00 92.16  ? 286 ARG B NH2 1 
ATOM   1935 N  N   . ASN A 1 314 ? -62.651 -20.783 21.593  1.00 68.88  ? 287 ASN B N   1 
ATOM   1936 C  CA  . ASN A 1 314 ? -63.093 -19.865 22.623  1.00 73.72  ? 287 ASN B CA  1 
ATOM   1937 C  C   . ASN A 1 314 ? -63.142 -20.337 24.110  1.00 73.13  ? 287 ASN B C   1 
ATOM   1938 O  O   . ASN A 1 314 ? -63.926 -19.836 24.912  1.00 73.02  ? 287 ASN B O   1 
ATOM   1939 C  CB  . ASN A 1 314 ? -64.440 -19.316 22.206  1.00 79.98  ? 287 ASN B CB  1 
ATOM   1940 C  CG  . ASN A 1 314 ? -64.673 -17.930 22.750  1.00 91.58  ? 287 ASN B CG  1 
ATOM   1941 O  OD1 . ASN A 1 314 ? -63.786 -17.077 22.663  1.00 81.56  ? 287 ASN B OD1 1 
ATOM   1942 N  ND2 . ASN A 1 314 ? -65.874 -17.695 23.334  1.00 99.19  ? 287 ASN B ND2 1 
ATOM   1943 N  N   . ILE A 1 315 ? -62.255 -21.247 24.491  1.00 72.14  ? 288 ILE B N   1 
ATOM   1944 C  CA  . ILE A 1 315 ? -62.192 -21.737 25.869  1.00 64.84  ? 288 ILE B CA  1 
ATOM   1945 C  C   . ILE A 1 315 ? -61.663 -20.652 26.813  1.00 65.83  ? 288 ILE B C   1 
ATOM   1946 O  O   . ILE A 1 315 ? -60.570 -20.118 26.618  1.00 68.62  ? 288 ILE B O   1 
ATOM   1947 C  CB  . ILE A 1 315 ? -61.310 -22.987 25.949  1.00 63.80  ? 288 ILE B CB  1 
ATOM   1948 C  CG1 . ILE A 1 315 ? -61.951 -24.118 25.139  1.00 66.94  ? 288 ILE B CG1 1 
ATOM   1949 C  CG2 . ILE A 1 315 ? -61.098 -23.405 27.398  1.00 61.11  ? 288 ILE B CG2 1 
ATOM   1950 C  CD1 . ILE A 1 315 ? -61.026 -25.290 24.886  1.00 71.36  ? 288 ILE B CD1 1 
ATOM   1951 N  N   . THR A 1 316 ? -62.423 -20.388 27.870  1.00 64.11  ? 289 THR B N   1 
ATOM   1952 C  CA  . THR A 1 316 ? -62.386 -19.111 28.584  1.00 60.70  ? 289 THR B CA  1 
ATOM   1953 C  C   . THR A 1 316 ? -62.244 -19.282 30.095  1.00 62.36  ? 289 THR B C   1 
ATOM   1954 O  O   . THR A 1 316 ? -62.644 -20.301 30.668  1.00 56.02  ? 289 THR B O   1 
ATOM   1955 C  CB  . THR A 1 316 ? -63.676 -18.327 28.234  1.00 63.88  ? 289 THR B CB  1 
ATOM   1956 O  OG1 . THR A 1 316 ? -63.379 -17.361 27.231  1.00 64.50  ? 289 THR B OG1 1 
ATOM   1957 C  CG2 . THR A 1 316 ? -64.328 -17.623 29.440  1.00 70.06  ? 289 THR B CG2 1 
ATOM   1958 N  N   . GLY A 1 317 ? -61.672 -18.267 30.741  1.00 63.44  ? 290 GLY B N   1 
ATOM   1959 C  CA  . GLY A 1 317 ? -61.459 -18.299 32.184  1.00 62.20  ? 290 GLY B CA  1 
ATOM   1960 C  C   . GLY A 1 317 ? -60.854 -19.595 32.682  1.00 67.33  ? 290 GLY B C   1 
ATOM   1961 O  O   . GLY A 1 317 ? -61.434 -20.278 33.515  1.00 73.11  ? 290 GLY B O   1 
ATOM   1962 N  N   . LYS A 1 318 ? -59.701 -19.956 32.128  1.00 71.73  ? 291 LYS B N   1 
ATOM   1963 C  CA  . LYS A 1 318 ? -58.776 -20.853 32.800  1.00 65.04  ? 291 LYS B CA  1 
ATOM   1964 C  C   . LYS A 1 318 ? -57.733 -19.998 33.484  1.00 64.20  ? 291 LYS B C   1 
ATOM   1965 O  O   . LYS A 1 318 ? -57.424 -18.895 33.019  1.00 57.51  ? 291 LYS B O   1 
ATOM   1966 C  CB  . LYS A 1 318 ? -58.059 -21.726 31.800  1.00 66.49  ? 291 LYS B CB  1 
ATOM   1967 C  CG  . LYS A 1 318 ? -58.957 -22.681 31.074  1.00 66.43  ? 291 LYS B CG  1 
ATOM   1968 C  CD  . LYS A 1 318 ? -59.539 -23.678 32.031  1.00 66.86  ? 291 LYS B CD  1 
ATOM   1969 C  CE  . LYS A 1 318 ? -60.488 -24.584 31.299  1.00 71.30  ? 291 LYS B CE  1 
ATOM   1970 N  NZ  . LYS A 1 318 ? -61.223 -25.392 32.297  1.00 77.98  ? 291 LYS B NZ  1 
ATOM   1971 N  N   . ILE A 1 319 ? -57.180 -20.506 34.576  1.00 61.52  ? 292 ILE B N   1 
ATOM   1972 C  CA  . ILE A 1 319 ? -55.990 -19.900 35.171  1.00 58.80  ? 292 ILE B CA  1 
ATOM   1973 C  C   . ILE A 1 319 ? -54.760 -20.646 34.664  1.00 57.83  ? 292 ILE B C   1 
ATOM   1974 O  O   . ILE A 1 319 ? -54.590 -21.847 34.914  1.00 57.52  ? 292 ILE B O   1 
ATOM   1975 C  CB  . ILE A 1 319 ? -56.043 -19.956 36.698  1.00 63.25  ? 292 ILE B CB  1 
ATOM   1976 C  CG1 . ILE A 1 319 ? -57.368 -19.334 37.169  1.00 65.25  ? 292 ILE B CG1 1 
ATOM   1977 C  CG2 . ILE A 1 319 ? -54.808 -19.289 37.301  1.00 62.49  ? 292 ILE B CG2 1 
ATOM   1978 C  CD1 . ILE A 1 319 ? -57.555 -19.277 38.663  1.00 63.32  ? 292 ILE B CD1 1 
ATOM   1979 N  N   . TRP A 1 320 ? -53.921 -19.917 33.927  1.00 59.23  ? 293 TRP B N   1 
ATOM   1980 C  CA  . TRP A 1 320 ? -52.711 -20.448 33.319  1.00 49.94  ? 293 TRP B CA  1 
ATOM   1981 C  C   . TRP A 1 320 ? -51.523 -20.070 34.190  1.00 51.07  ? 293 TRP B C   1 
ATOM   1982 O  O   . TRP A 1 320 ? -51.330 -18.886 34.487  1.00 45.90  ? 293 TRP B O   1 
ATOM   1983 C  CB  . TRP A 1 320 ? -52.508 -19.817 31.970  1.00 47.61  ? 293 TRP B CB  1 
ATOM   1984 C  CG  . TRP A 1 320 ? -53.611 -20.051 30.993  1.00 53.25  ? 293 TRP B CG  1 
ATOM   1985 C  CD1 . TRP A 1 320 ? -54.571 -19.154 30.605  1.00 52.48  ? 293 TRP B CD1 1 
ATOM   1986 C  CD2 . TRP A 1 320 ? -53.843 -21.234 30.219  1.00 53.55  ? 293 TRP B CD2 1 
ATOM   1987 N  NE1 . TRP A 1 320 ? -55.387 -19.715 29.663  1.00 48.27  ? 293 TRP B NE1 1 
ATOM   1988 C  CE2 . TRP A 1 320 ? -54.964 -20.992 29.412  1.00 52.48  ? 293 TRP B CE2 1 
ATOM   1989 C  CE3 . TRP A 1 320 ? -53.208 -22.466 30.128  1.00 52.19  ? 293 TRP B CE3 1 
ATOM   1990 C  CZ2 . TRP A 1 320 ? -55.461 -21.936 28.537  1.00 55.12  ? 293 TRP B CZ2 1 
ATOM   1991 C  CZ3 . TRP A 1 320 ? -53.698 -23.389 29.262  1.00 57.80  ? 293 TRP B CZ3 1 
ATOM   1992 C  CH2 . TRP A 1 320 ? -54.817 -23.126 28.474  1.00 56.14  ? 293 TRP B CH2 1 
ATOM   1993 N  N   . LEU A 1 321 ? -50.740 -21.078 34.582  1.00 47.93  ? 294 LEU B N   1 
ATOM   1994 C  CA  . LEU A 1 321 ? -49.508 -20.899 35.321  1.00 46.82  ? 294 LEU B CA  1 
ATOM   1995 C  C   . LEU A 1 321 ? -48.324 -21.202 34.389  1.00 49.24  ? 294 LEU B C   1 
ATOM   1996 O  O   . LEU A 1 321 ? -48.140 -22.355 33.926  1.00 43.10  ? 294 LEU B O   1 
ATOM   1997 C  CB  . LEU A 1 321 ? -49.498 -21.872 36.479  1.00 55.18  ? 294 LEU B CB  1 
ATOM   1998 C  CG  . LEU A 1 321 ? -49.606 -21.329 37.888  1.00 64.81  ? 294 LEU B CG  1 
ATOM   1999 C  CD1 . LEU A 1 321 ? -50.898 -20.550 38.103  1.00 69.63  ? 294 LEU B CD1 1 
ATOM   2000 C  CD2 . LEU A 1 321 ? -49.524 -22.528 38.823  1.00 70.98  ? 294 LEU B CD2 1 
ATOM   2001 N  N   . ALA A 1 322 ? -47.513 -20.183 34.122  1.00 47.24  ? 295 ALA B N   1 
ATOM   2002 C  CA  . ALA A 1 322 ? -46.529 -20.247 33.034  1.00 49.35  ? 295 ALA B CA  1 
ATOM   2003 C  C   . ALA A 1 322 ? -45.152 -20.470 33.568  1.00 49.38  ? 295 ALA B C   1 
ATOM   2004 O  O   . ALA A 1 322 ? -44.759 -19.818 34.545  1.00 48.11  ? 295 ALA B O   1 
ATOM   2005 C  CB  . ALA A 1 322 ? -46.539 -18.967 32.220  1.00 51.08  ? 295 ALA B CB  1 
ATOM   2006 N  N   . SER A 1 323 ? -44.418 -21.376 32.925  1.00 44.98  ? 296 SER B N   1 
ATOM   2007 C  CA  . SER A 1 323 ? -43.012 -21.559 33.241  1.00 44.56  ? 296 SER B CA  1 
ATOM   2008 C  C   . SER A 1 323 ? -42.295 -20.370 32.620  1.00 45.62  ? 296 SER B C   1 
ATOM   2009 O  O   . SER A 1 323 ? -42.865 -19.698 31.757  1.00 47.45  ? 296 SER B O   1 
ATOM   2010 C  CB  . SER A 1 323 ? -42.484 -22.922 32.708  1.00 46.25  ? 296 SER B CB  1 
ATOM   2011 O  OG  . SER A 1 323 ? -42.247 -22.934 31.286  1.00 50.25  ? 296 SER B OG  1 
ATOM   2012 N  N   . GLU A 1 324 ? -41.052 -20.104 32.999  1.00 50.20  ? 297 GLU B N   1 
ATOM   2013 C  CA  . GLU A 1 324 ? -40.400 -18.855 32.590  1.00 52.62  ? 297 GLU B CA  1 
ATOM   2014 C  C   . GLU A 1 324 ? -40.210 -18.761 31.082  1.00 50.08  ? 297 GLU B C   1 
ATOM   2015 O  O   . GLU A 1 324 ? -40.079 -17.680 30.548  1.00 53.62  ? 297 GLU B O   1 
ATOM   2016 C  CB  . GLU A 1 324 ? -39.077 -18.636 33.339  1.00 61.26  ? 297 GLU B CB  1 
ATOM   2017 C  CG  . GLU A 1 324 ? -37.783 -19.100 32.648  1.00 77.58  ? 297 GLU B CG  1 
ATOM   2018 C  CD  . GLU A 1 324 ? -37.502 -20.595 32.815  1.00 88.13  ? 297 GLU B CD  1 
ATOM   2019 O  OE1 . GLU A 1 324 ? -36.722 -20.977 33.739  1.00 94.33  ? 297 GLU B OE1 1 
ATOM   2020 O  OE2 . GLU A 1 324 ? -38.065 -21.385 32.017  1.00 87.31  ? 297 GLU B OE2 1 
ATOM   2021 N  N   . ALA A 1 325 ? -40.215 -19.890 30.394  1.00 51.37  ? 298 ALA B N   1 
ATOM   2022 C  CA  . ALA A 1 325 ? -39.956 -19.892 28.956  1.00 54.76  ? 298 ALA B CA  1 
ATOM   2023 C  C   . ALA A 1 325 ? -41.085 -19.305 28.124  1.00 52.42  ? 298 ALA B C   1 
ATOM   2024 O  O   . ALA A 1 325 ? -40.843 -18.751 27.051  1.00 58.77  ? 298 ALA B O   1 
ATOM   2025 C  CB  . ALA A 1 325 ? -39.666 -21.302 28.485  1.00 58.08  ? 298 ALA B CB  1 
ATOM   2026 N  N   . TRP A 1 326 ? -42.324 -19.443 28.575  1.00 47.69  ? 299 TRP B N   1 
ATOM   2027 C  CA  . TRP A 1 326 ? -43.416 -18.809 27.836  1.00 45.87  ? 299 TRP B CA  1 
ATOM   2028 C  C   . TRP A 1 326 ? -44.050 -17.661 28.537  1.00 41.84  ? 299 TRP B C   1 
ATOM   2029 O  O   . TRP A 1 326 ? -44.775 -16.926 27.918  1.00 43.56  ? 299 TRP B O   1 
ATOM   2030 C  CB  . TRP A 1 326 ? -44.465 -19.803 27.339  1.00 45.88  ? 299 TRP B CB  1 
ATOM   2031 C  CG  . TRP A 1 326 ? -45.441 -20.348 28.311  1.00 50.24  ? 299 TRP B CG  1 
ATOM   2032 C  CD1 . TRP A 1 326 ? -45.304 -21.475 29.080  1.00 51.02  ? 299 TRP B CD1 1 
ATOM   2033 C  CD2 . TRP A 1 326 ? -46.752 -19.839 28.584  1.00 52.67  ? 299 TRP B CD2 1 
ATOM   2034 N  NE1 . TRP A 1 326 ? -46.441 -21.688 29.815  1.00 50.10  ? 299 TRP B NE1 1 
ATOM   2035 C  CE2 . TRP A 1 326 ? -47.345 -20.702 29.525  1.00 51.01  ? 299 TRP B CE2 1 
ATOM   2036 C  CE3 . TRP A 1 326 ? -47.482 -18.738 28.123  1.00 48.03  ? 299 TRP B CE3 1 
ATOM   2037 C  CZ2 . TRP A 1 326 ? -48.611 -20.481 30.021  1.00 52.39  ? 299 TRP B CZ2 1 
ATOM   2038 C  CZ3 . TRP A 1 326 ? -48.739 -18.526 28.612  1.00 43.54  ? 299 TRP B CZ3 1 
ATOM   2039 C  CH2 . TRP A 1 326 ? -49.295 -19.391 29.540  1.00 51.31  ? 299 TRP B CH2 1 
ATOM   2040 N  N   . ALA A 1 327 ? -43.699 -17.438 29.789  1.00 44.58  ? 300 ALA B N   1 
ATOM   2041 C  CA  . ALA A 1 327 ? -44.336 -16.390 30.573  1.00 46.81  ? 300 ALA B CA  1 
ATOM   2042 C  C   . ALA A 1 327 ? -44.072 -14.991 30.062  1.00 46.27  ? 300 ALA B C   1 
ATOM   2043 O  O   . ALA A 1 327 ? -44.765 -14.087 30.484  1.00 52.62  ? 300 ALA B O   1 
ATOM   2044 C  CB  . ALA A 1 327 ? -43.923 -16.497 32.035  1.00 49.75  ? 300 ALA B CB  1 
ATOM   2045 N  N   . SER A 1 328 ? -43.093 -14.806 29.167  1.00 51.54  ? 301 SER B N   1 
ATOM   2046 C  CA  . SER A 1 328 ? -42.766 -13.470 28.580  1.00 52.35  ? 301 SER B CA  1 
ATOM   2047 C  C   . SER A 1 328 ? -42.703 -13.521 27.063  1.00 56.05  ? 301 SER B C   1 
ATOM   2048 O  O   . SER A 1 328 ? -42.088 -12.654 26.433  1.00 52.82  ? 301 SER B O   1 
ATOM   2049 C  CB  . SER A 1 328 ? -41.412 -12.987 29.068  1.00 50.66  ? 301 SER B CB  1 
ATOM   2050 O  OG  . SER A 1 328 ? -41.414 -12.885 30.464  1.00 53.50  ? 301 SER B OG  1 
ATOM   2051 N  N   . SER A 1 329 ? -43.325 -14.547 26.485  1.00 57.65  ? 302 SER B N   1 
ATOM   2052 C  CA  . SER A 1 329 ? -43.148 -14.854 25.077  1.00 54.81  ? 302 SER B CA  1 
ATOM   2053 C  C   . SER A 1 329 ? -44.140 -14.063 24.233  1.00 60.29  ? 302 SER B C   1 
ATOM   2054 O  O   . SER A 1 329 ? -45.350 -14.115 24.465  1.00 59.57  ? 302 SER B O   1 
ATOM   2055 C  CB  . SER A 1 329 ? -43.345 -16.342 24.832  1.00 50.79  ? 302 SER B CB  1 
ATOM   2056 O  OG  . SER A 1 329 ? -43.386 -16.615 23.446  1.00 49.53  ? 302 SER B OG  1 
ATOM   2057 N  N   . SER A 1 330 ? -43.620 -13.361 23.232  1.00 59.48  ? 303 SER B N   1 
ATOM   2058 C  CA  . SER A 1 330 ? -44.436 -12.533 22.365  1.00 60.28  ? 303 SER B CA  1 
ATOM   2059 C  C   . SER A 1 330 ? -45.270 -13.362 21.403  1.00 58.54  ? 303 SER B C   1 
ATOM   2060 O  O   . SER A 1 330 ? -46.221 -12.856 20.832  1.00 73.15  ? 303 SER B O   1 
ATOM   2061 C  CB  . SER A 1 330 ? -43.557 -11.557 21.589  1.00 62.19  ? 303 SER B CB  1 
ATOM   2062 O  OG  . SER A 1 330 ? -42.797 -12.255 20.639  1.00 66.17  ? 303 SER B OG  1 
ATOM   2063 N  N   . LEU A 1 331 ? -44.922 -14.628 21.218  1.00 60.86  ? 304 LEU B N   1 
ATOM   2064 C  CA  . LEU A 1 331 ? -45.781 -15.569 20.481  1.00 59.01  ? 304 LEU B CA  1 
ATOM   2065 C  C   . LEU A 1 331 ? -47.090 -15.948 21.177  1.00 54.46  ? 304 LEU B C   1 
ATOM   2066 O  O   . LEU A 1 331 ? -48.001 -16.443 20.525  1.00 61.38  ? 304 LEU B O   1 
ATOM   2067 C  CB  . LEU A 1 331 ? -45.019 -16.855 20.182  1.00 57.40  ? 304 LEU B CB  1 
ATOM   2068 C  CG  . LEU A 1 331 ? -43.859 -16.649 19.222  1.00 61.05  ? 304 LEU B CG  1 
ATOM   2069 C  CD1 . LEU A 1 331 ? -43.019 -17.925 19.113  1.00 66.41  ? 304 LEU B CD1 1 
ATOM   2070 C  CD2 . LEU A 1 331 ? -44.367 -16.202 17.858  1.00 57.29  ? 304 LEU B CD2 1 
ATOM   2071 N  N   . ILE A 1 332 ? -47.173 -15.771 22.489  1.00 55.19  ? 305 ILE B N   1 
ATOM   2072 C  CA  . ILE A 1 332 ? -48.380 -16.150 23.243  1.00 54.53  ? 305 ILE B CA  1 
ATOM   2073 C  C   . ILE A 1 332 ? -49.059 -14.918 23.850  1.00 56.80  ? 305 ILE B C   1 
ATOM   2074 O  O   . ILE A 1 332 ? -50.283 -14.828 23.902  1.00 57.52  ? 305 ILE B O   1 
ATOM   2075 C  CB  . ILE A 1 332 ? -48.061 -17.169 24.364  1.00 55.43  ? 305 ILE B CB  1 
ATOM   2076 C  CG1 . ILE A 1 332 ? -47.167 -18.339 23.869  1.00 53.30  ? 305 ILE B CG1 1 
ATOM   2077 C  CG2 . ILE A 1 332 ? -49.341 -17.677 25.011  1.00 55.98  ? 305 ILE B CG2 1 
ATOM   2078 C  CD1 . ILE A 1 332 ? -47.728 -19.216 22.771  1.00 50.20  ? 305 ILE B CD1 1 
ATOM   2079 N  N   . ALA A 1 333 ? -48.265 -13.960 24.296  1.00 62.11  ? 306 ALA B N   1 
ATOM   2080 C  CA  . ALA A 1 333 ? -48.784 -12.728 24.869  1.00 63.43  ? 306 ALA B CA  1 
ATOM   2081 C  C   . ALA A 1 333 ? -49.169 -11.805 23.738  1.00 59.26  ? 306 ALA B C   1 
ATOM   2082 O  O   . ALA A 1 333 ? -48.505 -10.787 23.517  1.00 54.36  ? 306 ALA B O   1 
ATOM   2083 C  CB  . ALA A 1 333 ? -47.737 -12.065 25.771  1.00 61.16  ? 306 ALA B CB  1 
ATOM   2084 N  N   . MET A 1 334 ? -50.254 -12.164 23.048  1.00 63.26  ? 307 MET B N   1 
ATOM   2085 C  CA  . MET A 1 334 ? -50.797 -11.406 21.895  1.00 63.54  ? 307 MET B CA  1 
ATOM   2086 C  C   . MET A 1 334 ? -52.213 -10.948 22.217  1.00 58.04  ? 307 MET B C   1 
ATOM   2087 O  O   . MET A 1 334 ? -53.015 -11.755 22.679  1.00 60.93  ? 307 MET B O   1 
ATOM   2088 C  CB  . MET A 1 334 ? -50.843 -12.284 20.644  1.00 60.99  ? 307 MET B CB  1 
ATOM   2089 C  CG  . MET A 1 334 ? -49.482 -12.658 20.108  1.00 66.92  ? 307 MET B CG  1 
ATOM   2090 S  SD  . MET A 1 334 ? -49.522 -13.053 18.344  1.00 78.43  ? 307 MET B SD  1 
ATOM   2091 C  CE  . MET A 1 334 ? -49.508 -11.382 17.693  1.00 81.28  ? 307 MET B CE  1 
ATOM   2092 N  N   . PRO A 1 335 ? -52.549 -9.674  21.935  1.00 58.22  ? 308 PRO B N   1 
ATOM   2093 C  CA  . PRO A 1 335 ? -53.850 -9.159  22.356  1.00 56.47  ? 308 PRO B CA  1 
ATOM   2094 C  C   . PRO A 1 335 ? -55.063 -9.944  21.830  1.00 57.02  ? 308 PRO B C   1 
ATOM   2095 O  O   . PRO A 1 335 ? -56.055 -10.095 22.538  1.00 56.25  ? 308 PRO B O   1 
ATOM   2096 C  CB  . PRO A 1 335 ? -53.852 -7.728  21.810  1.00 54.32  ? 308 PRO B CB  1 
ATOM   2097 C  CG  . PRO A 1 335 ? -52.427 -7.392  21.602  1.00 58.53  ? 308 PRO B CG  1 
ATOM   2098 C  CD  . PRO A 1 335 ? -51.860 -8.686  21.092  1.00 60.83  ? 308 PRO B CD  1 
ATOM   2099 N  N   . GLN A 1 336 ? -54.994 -10.484 20.626  1.00 59.72  ? 309 GLN B N   1 
ATOM   2100 C  CA  . GLN A 1 336 ? -56.125 -11.283 20.162  1.00 65.63  ? 309 GLN B CA  1 
ATOM   2101 C  C   . GLN A 1 336 ? -56.303 -12.625 20.884  1.00 68.86  ? 309 GLN B C   1 
ATOM   2102 O  O   . GLN A 1 336 ? -57.291 -13.333 20.630  1.00 73.85  ? 309 GLN B O   1 
ATOM   2103 C  CB  . GLN A 1 336 ? -56.068 -11.510 18.654  1.00 67.93  ? 309 GLN B CB  1 
ATOM   2104 C  CG  . GLN A 1 336 ? -55.060 -12.530 18.192  1.00 69.17  ? 309 GLN B CG  1 
ATOM   2105 C  CD  . GLN A 1 336 ? -53.789 -11.883 17.730  1.00 75.61  ? 309 GLN B CD  1 
ATOM   2106 O  OE1 . GLN A 1 336 ? -53.456 -10.749 18.143  1.00 74.95  ? 309 GLN B OE1 1 
ATOM   2107 N  NE2 . GLN A 1 336 ? -53.059 -12.590 16.864  1.00 74.50  ? 309 GLN B NE2 1 
ATOM   2108 N  N   . TYR A 1 337 ? -55.350 -13.006 21.741  1.00 65.52  ? 310 TYR B N   1 
ATOM   2109 C  CA  . TYR A 1 337 ? -55.530 -14.200 22.552  1.00 63.46  ? 310 TYR B CA  1 
ATOM   2110 C  C   . TYR A 1 337 ? -56.000 -13.870 23.974  1.00 62.82  ? 310 TYR B C   1 
ATOM   2111 O  O   . TYR A 1 337 ? -56.291 -14.789 24.754  1.00 59.47  ? 310 TYR B O   1 
ATOM   2112 C  CB  . TYR A 1 337 ? -54.262 -15.020 22.636  1.00 60.11  ? 310 TYR B CB  1 
ATOM   2113 C  CG  . TYR A 1 337 ? -53.646 -15.519 21.339  1.00 64.31  ? 310 TYR B CG  1 
ATOM   2114 C  CD1 . TYR A 1 337 ? -54.365 -15.620 20.145  1.00 64.23  ? 310 TYR B CD1 1 
ATOM   2115 C  CD2 . TYR A 1 337 ? -52.314 -15.923 21.324  1.00 63.98  ? 310 TYR B CD2 1 
ATOM   2116 C  CE1 . TYR A 1 337 ? -53.752 -16.103 18.981  1.00 61.67  ? 310 TYR B CE1 1 
ATOM   2117 C  CE2 . TYR A 1 337 ? -51.711 -16.389 20.175  1.00 66.61  ? 310 TYR B CE2 1 
ATOM   2118 C  CZ  . TYR A 1 337 ? -52.423 -16.487 19.011  1.00 61.63  ? 310 TYR B CZ  1 
ATOM   2119 O  OH  . TYR A 1 337 ? -51.756 -16.981 17.913  1.00 61.61  ? 310 TYR B OH  1 
ATOM   2120 N  N   . PHE A 1 338 ? -56.136 -12.582 24.299  1.00 56.88  ? 311 PHE B N   1 
ATOM   2121 C  CA  . PHE A 1 338 ? -56.269 -12.183 25.692  1.00 58.18  ? 311 PHE B CA  1 
ATOM   2122 C  C   . PHE A 1 338 ? -57.469 -12.756 26.402  1.00 55.35  ? 311 PHE B C   1 
ATOM   2123 O  O   . PHE A 1 338 ? -57.459 -12.905 27.614  1.00 56.34  ? 311 PHE B O   1 
ATOM   2124 C  CB  . PHE A 1 338 ? -56.311 -10.684 25.838  1.00 57.31  ? 311 PHE B CB  1 
ATOM   2125 C  CG  . PHE A 1 338 ? -55.973 -10.220 27.212  1.00 59.93  ? 311 PHE B CG  1 
ATOM   2126 C  CD1 . PHE A 1 338 ? -54.641 -10.197 27.634  1.00 65.16  ? 311 PHE B CD1 1 
ATOM   2127 C  CD2 . PHE A 1 338 ? -56.965 -9.833  28.098  1.00 64.14  ? 311 PHE B CD2 1 
ATOM   2128 C  CE1 . PHE A 1 338 ? -54.295 -9.762  28.908  1.00 65.47  ? 311 PHE B CE1 1 
ATOM   2129 C  CE2 . PHE A 1 338 ? -56.632 -9.391  29.383  1.00 71.13  ? 311 PHE B CE2 1 
ATOM   2130 C  CZ  . PHE A 1 338 ? -55.292 -9.356  29.784  1.00 73.45  ? 311 PHE B CZ  1 
ATOM   2131 N  N   . HIS A 1 339 ? -58.504 -13.074 25.658  1.00 55.01  ? 312 HIS B N   1 
ATOM   2132 C  CA  . HIS A 1 339 ? -59.708 -13.626 26.272  1.00 59.55  ? 312 HIS B CA  1 
ATOM   2133 C  C   . HIS A 1 339 ? -59.495 -15.050 26.757  1.00 58.93  ? 312 HIS B C   1 
ATOM   2134 O  O   . HIS A 1 339 ? -60.260 -15.555 27.549  1.00 63.61  ? 312 HIS B O   1 
ATOM   2135 C  CB  . HIS A 1 339 ? -60.925 -13.510 25.327  1.00 60.60  ? 312 HIS B CB  1 
ATOM   2136 C  CG  . HIS A 1 339 ? -60.783 -14.232 24.023  1.00 63.73  ? 312 HIS B CG  1 
ATOM   2137 N  ND1 . HIS A 1 339 ? -59.995 -13.770 22.990  1.00 68.41  ? 312 HIS B ND1 1 
ATOM   2138 C  CD2 . HIS A 1 339 ? -61.375 -15.359 23.567  1.00 68.28  ? 312 HIS B CD2 1 
ATOM   2139 C  CE1 . HIS A 1 339 ? -60.093 -14.596 21.962  1.00 71.20  ? 312 HIS B CE1 1 
ATOM   2140 N  NE2 . HIS A 1 339 ? -60.931 -15.565 22.284  1.00 68.19  ? 312 HIS B NE2 1 
ATOM   2141 N  N   . VAL A 1 340 ? -58.457 -15.698 26.257  1.00 62.35  ? 313 VAL B N   1 
ATOM   2142 C  CA  . VAL A 1 340 ? -58.072 -17.017 26.721  1.00 63.02  ? 313 VAL B CA  1 
ATOM   2143 C  C   . VAL A 1 340 ? -56.904 -16.913 27.695  1.00 58.59  ? 313 VAL B C   1 
ATOM   2144 O  O   . VAL A 1 340 ? -56.917 -17.486 28.770  1.00 52.41  ? 313 VAL B O   1 
ATOM   2145 C  CB  . VAL A 1 340 ? -57.692 -17.890 25.518  1.00 69.74  ? 313 VAL B CB  1 
ATOM   2146 C  CG1 . VAL A 1 340 ? -57.045 -19.195 25.944  1.00 71.39  ? 313 VAL B CG1 1 
ATOM   2147 C  CG2 . VAL A 1 340 ? -58.931 -18.157 24.684  1.00 78.37  ? 313 VAL B CG2 1 
ATOM   2148 N  N   . VAL A 1 341 ? -55.909 -16.130 27.319  1.00 61.27  ? 314 VAL B N   1 
ATOM   2149 C  CA  . VAL A 1 341 ? -54.620 -16.186 27.949  1.00 60.04  ? 314 VAL B CA  1 
ATOM   2150 C  C   . VAL A 1 341 ? -54.448 -15.049 28.966  1.00 55.15  ? 314 VAL B C   1 
ATOM   2151 O  O   . VAL A 1 341 ? -53.479 -15.001 29.716  1.00 55.76  ? 314 VAL B O   1 
ATOM   2152 C  CB  . VAL A 1 341 ? -53.548 -16.222 26.832  1.00 66.89  ? 314 VAL B CB  1 
ATOM   2153 C  CG1 . VAL A 1 341 ? -52.999 -14.836 26.530  1.00 70.61  ? 314 VAL B CG1 1 
ATOM   2154 C  CG2 . VAL A 1 341 ? -52.439 -17.193 27.180  1.00 76.87  ? 314 VAL B CG2 1 
ATOM   2155 N  N   . GLY A 1 342 ? -55.409 -14.138 29.020  1.00 58.23  ? 315 GLY B N   1 
ATOM   2156 C  CA  . GLY A 1 342 ? -55.366 -13.025 29.969  1.00 51.50  ? 315 GLY B CA  1 
ATOM   2157 C  C   . GLY A 1 342 ? -55.311 -13.500 31.398  1.00 49.04  ? 315 GLY B C   1 
ATOM   2158 O  O   . GLY A 1 342 ? -55.997 -14.448 31.787  1.00 49.20  ? 315 GLY B O   1 
ATOM   2159 N  N   . GLY A 1 343 ? -54.475 -12.827 32.177  1.00 54.88  ? 316 GLY B N   1 
ATOM   2160 C  CA  . GLY A 1 343 ? -54.334 -13.083 33.600  1.00 52.04  ? 316 GLY B CA  1 
ATOM   2161 C  C   . GLY A 1 343 ? -53.402 -14.215 33.952  1.00 55.27  ? 316 GLY B C   1 
ATOM   2162 O  O   . GLY A 1 343 ? -53.325 -14.563 35.128  1.00 60.43  ? 316 GLY B O   1 
ATOM   2163 N  N   . THR A 1 344 ? -52.650 -14.769 32.984  1.00 54.07  ? 317 THR B N   1 
ATOM   2164 C  CA  . THR A 1 344 ? -51.730 -15.850 33.335  1.00 51.25  ? 317 THR B CA  1 
ATOM   2165 C  C   . THR A 1 344 ? -50.772 -15.365 34.396  1.00 51.20  ? 317 THR B C   1 
ATOM   2166 O  O   . THR A 1 344 ? -50.482 -14.178 34.490  1.00 55.56  ? 317 THR B O   1 
ATOM   2167 C  CB  . THR A 1 344 ? -50.949 -16.497 32.148  1.00 51.99  ? 317 THR B CB  1 
ATOM   2168 O  OG1 . THR A 1 344 ? -49.688 -15.861 31.932  1.00 55.14  ? 317 THR B OG1 1 
ATOM   2169 C  CG2 . THR A 1 344 ? -51.752 -16.497 30.887  1.00 49.73  ? 317 THR B CG2 1 
ATOM   2170 N  N   . ILE A 1 345 ? -50.295 -16.287 35.212  1.00 52.62  ? 318 ILE B N   1 
ATOM   2171 C  CA  . ILE A 1 345 ? -49.297 -15.973 36.209  1.00 51.45  ? 318 ILE B CA  1 
ATOM   2172 C  C   . ILE A 1 345 ? -48.091 -16.793 35.837  1.00 50.21  ? 318 ILE B C   1 
ATOM   2173 O  O   . ILE A 1 345 ? -48.226 -17.980 35.515  1.00 53.07  ? 318 ILE B O   1 
ATOM   2174 C  CB  . ILE A 1 345 ? -49.805 -16.377 37.586  1.00 53.64  ? 318 ILE B CB  1 
ATOM   2175 C  CG1 . ILE A 1 345 ? -51.047 -15.544 37.920  1.00 61.93  ? 318 ILE B CG1 1 
ATOM   2176 C  CG2 . ILE A 1 345 ? -48.717 -16.181 38.627  1.00 52.46  ? 318 ILE B CG2 1 
ATOM   2177 C  CD1 . ILE A 1 345 ? -51.860 -16.095 39.084  1.00 70.08  ? 318 ILE B CD1 1 
ATOM   2178 N  N   . GLY A 1 346 ? -46.916 -16.188 35.883  1.00 47.92  ? 319 GLY B N   1 
ATOM   2179 C  CA  . GLY A 1 346 ? -45.712 -16.886 35.479  1.00 53.92  ? 319 GLY B CA  1 
ATOM   2180 C  C   . GLY A 1 346 ? -44.435 -16.497 36.202  1.00 54.23  ? 319 GLY B C   1 
ATOM   2181 O  O   . GLY A 1 346 ? -44.414 -15.561 36.975  1.00 50.36  ? 319 GLY B O   1 
ATOM   2182 N  N   . PHE A 1 347 ? -43.363 -17.236 35.924  1.00 52.43  ? 320 PHE B N   1 
ATOM   2183 C  CA  . PHE A 1 347 ? -42.066 -16.915 36.449  1.00 50.05  ? 320 PHE B CA  1 
ATOM   2184 C  C   . PHE A 1 347 ? -41.249 -16.163 35.431  1.00 48.45  ? 320 PHE B C   1 
ATOM   2185 O  O   . PHE A 1 347 ? -41.440 -16.333 34.247  1.00 51.66  ? 320 PHE B O   1 
ATOM   2186 C  CB  . PHE A 1 347 ? -41.380 -18.179 36.910  1.00 51.09  ? 320 PHE B CB  1 
ATOM   2187 C  CG  . PHE A 1 347 ? -42.146 -18.879 37.985  1.00 51.12  ? 320 PHE B CG  1 
ATOM   2188 C  CD1 . PHE A 1 347 ? -41.953 -18.556 39.318  1.00 54.41  ? 320 PHE B CD1 1 
ATOM   2189 C  CD2 . PHE A 1 347 ? -43.121 -19.780 37.661  1.00 51.43  ? 320 PHE B CD2 1 
ATOM   2190 C  CE1 . PHE A 1 347 ? -42.690 -19.166 40.316  1.00 58.28  ? 320 PHE B CE1 1 
ATOM   2191 C  CE2 . PHE A 1 347 ? -43.862 -20.394 38.646  1.00 55.97  ? 320 PHE B CE2 1 
ATOM   2192 C  CZ  . PHE A 1 347 ? -43.653 -20.095 39.980  1.00 55.30  ? 320 PHE B CZ  1 
ATOM   2193 N  N   . ALA A 1 348 ? -40.418 -15.258 35.930  1.00 48.06  ? 321 ALA B N   1 
ATOM   2194 C  CA  . ALA A 1 348 ? -39.422 -14.567 35.163  1.00 51.57  ? 321 ALA B CA  1 
ATOM   2195 C  C   . ALA A 1 348 ? -38.152 -14.572 35.995  1.00 54.71  ? 321 ALA B C   1 
ATOM   2196 O  O   . ALA A 1 348 ? -38.221 -14.730 37.209  1.00 57.54  ? 321 ALA B O   1 
ATOM   2197 C  CB  . ALA A 1 348 ? -39.863 -13.143 34.900  1.00 55.24  ? 321 ALA B CB  1 
ATOM   2198 N  N   . LEU A 1 349 ? -36.993 -14.410 35.357  1.00 57.85  ? 322 LEU B N   1 
ATOM   2199 C  CA  . LEU A 1 349 ? -35.733 -14.322 36.102  1.00 58.46  ? 322 LEU B CA  1 
ATOM   2200 C  C   . LEU A 1 349 ? -35.643 -12.945 36.701  1.00 58.52  ? 322 LEU B C   1 
ATOM   2201 O  O   . LEU A 1 349 ? -36.362 -12.048 36.283  1.00 60.71  ? 322 LEU B O   1 
ATOM   2202 C  CB  . LEU A 1 349 ? -34.528 -14.574 35.210  1.00 59.28  ? 322 LEU B CB  1 
ATOM   2203 C  CG  . LEU A 1 349 ? -34.185 -16.004 34.776  1.00 58.35  ? 322 LEU B CG  1 
ATOM   2204 C  CD1 . LEU A 1 349 ? -34.401 -17.005 35.887  1.00 60.10  ? 322 LEU B CD1 1 
ATOM   2205 C  CD2 . LEU A 1 349 ? -34.993 -16.413 33.581  1.00 60.93  ? 322 LEU B CD2 1 
ATOM   2206 N  N   . LYS A 1 350 ? -34.786 -12.769 37.695  1.00 58.88  ? 323 LYS B N   1 
ATOM   2207 C  CA  . LYS A 1 350 ? -34.633 -11.443 38.266  1.00 63.91  ? 323 LYS B CA  1 
ATOM   2208 C  C   . LYS A 1 350 ? -34.098 -10.519 37.173  1.00 62.38  ? 323 LYS B C   1 
ATOM   2209 O  O   . LYS A 1 350 ? -33.313 -10.931 36.339  1.00 66.85  ? 323 LYS B O   1 
ATOM   2210 C  CB  . LYS A 1 350 ? -33.751 -11.433 39.539  1.00 67.30  ? 323 LYS B CB  1 
ATOM   2211 C  CG  . LYS A 1 350 ? -34.455 -11.861 40.850  1.00 74.13  ? 323 LYS B CG  1 
ATOM   2212 C  CD  . LYS A 1 350 ? -35.812 -11.181 41.111  1.00 77.17  ? 323 LYS B CD  1 
ATOM   2213 C  CE  . LYS A 1 350 ? -36.039 -10.700 42.551  1.00 82.73  ? 323 LYS B CE  1 
ATOM   2214 N  NZ  . LYS A 1 350 ? -35.859 -11.689 43.664  1.00 86.47  ? 323 LYS B NZ  1 
ATOM   2215 N  N   . ALA A 1 351 ? -34.591 -9.285  37.144  1.00 69.91  ? 324 ALA B N   1 
ATOM   2216 C  CA  . ALA A 1 351 ? -34.160 -8.286  36.159  1.00 64.48  ? 324 ALA B CA  1 
ATOM   2217 C  C   . ALA A 1 351 ? -32.762 -7.841  36.499  1.00 57.72  ? 324 ALA B C   1 
ATOM   2218 O  O   . ALA A 1 351 ? -32.365 -7.914  37.650  1.00 59.32  ? 324 ALA B O   1 
ATOM   2219 C  CB  . ALA A 1 351 ? -35.103 -7.086  36.179  1.00 64.84  ? 324 ALA B CB  1 
ATOM   2220 N  N   . GLY A 1 352 ? -32.016 -7.394  35.498  1.00 54.73  ? 325 GLY B N   1 
ATOM   2221 C  CA  . GLY A 1 352 ? -30.665 -6.883  35.692  1.00 54.40  ? 325 GLY B CA  1 
ATOM   2222 C  C   . GLY A 1 352 ? -30.530 -5.620  34.889  1.00 61.34  ? 325 GLY B C   1 
ATOM   2223 O  O   . GLY A 1 352 ? -31.419 -5.308  34.092  1.00 63.07  ? 325 GLY B O   1 
ATOM   2224 N  N   . GLN A 1 353 ? -29.430 -4.891  35.093  1.00 69.17  ? 326 GLN B N   1 
ATOM   2225 C  CA  . GLN A 1 353 ? -29.227 -3.582  34.468  1.00 67.77  ? 326 GLN B CA  1 
ATOM   2226 C  C   . GLN A 1 353 ? -27.961 -3.568  33.635  1.00 69.29  ? 326 GLN B C   1 
ATOM   2227 O  O   . GLN A 1 353 ? -26.917 -4.024  34.070  1.00 73.17  ? 326 GLN B O   1 
ATOM   2228 C  CB  . GLN A 1 353 ? -29.162 -2.471  35.516  1.00 78.31  ? 326 GLN B CB  1 
ATOM   2229 C  CG  . GLN A 1 353 ? -30.520 -1.955  35.983  1.00 89.19  ? 326 GLN B CG  1 
ATOM   2230 C  CD  . GLN A 1 353 ? -30.392 -0.793  36.964  1.00 106.17 ? 326 GLN B CD  1 
ATOM   2231 O  OE1 . GLN A 1 353 ? -29.488 0.045   36.852  1.00 103.20 ? 326 GLN B OE1 1 
ATOM   2232 N  NE2 . GLN A 1 353 ? -31.306 -0.732  37.930  1.00 115.18 ? 326 GLN B NE2 1 
ATOM   2233 N  N   . ILE A 1 354 ? -28.064 -3.038  32.425  1.00 71.43  ? 327 ILE B N   1 
ATOM   2234 C  CA  . ILE A 1 354 ? -26.916 -2.849  31.569  1.00 67.36  ? 327 ILE B CA  1 
ATOM   2235 C  C   . ILE A 1 354 ? -26.892 -1.391  31.082  1.00 69.87  ? 327 ILE B C   1 
ATOM   2236 O  O   . ILE A 1 354 ? -27.402 -1.070  30.005  1.00 68.33  ? 327 ILE B O   1 
ATOM   2237 C  CB  . ILE A 1 354 ? -26.967 -3.796  30.376  1.00 66.74  ? 327 ILE B CB  1 
ATOM   2238 C  CG1 . ILE A 1 354 ? -27.419 -5.188  30.812  1.00 71.76  ? 327 ILE B CG1 1 
ATOM   2239 C  CG2 . ILE A 1 354 ? -25.604 -3.850  29.718  1.00 68.99  ? 327 ILE B CG2 1 
ATOM   2240 C  CD1 . ILE A 1 354 ? -27.430 -6.213  29.689  1.00 74.17  ? 327 ILE B CD1 1 
ATOM   2241 N  N   . PRO A 1 355 ? -26.301 -0.493  31.882  1.00 72.64  ? 328 PRO B N   1 
ATOM   2242 C  CA  . PRO A 1 355 ? -26.165 0.894   31.437  1.00 70.41  ? 328 PRO B CA  1 
ATOM   2243 C  C   . PRO A 1 355 ? -25.470 0.957   30.102  1.00 68.50  ? 328 PRO B C   1 
ATOM   2244 O  O   . PRO A 1 355 ? -24.415 0.324   29.923  1.00 73.51  ? 328 PRO B O   1 
ATOM   2245 C  CB  . PRO A 1 355 ? -25.280 1.518   32.506  1.00 74.05  ? 328 PRO B CB  1 
ATOM   2246 C  CG  . PRO A 1 355 ? -25.491 0.653   33.711  1.00 76.40  ? 328 PRO B CG  1 
ATOM   2247 C  CD  . PRO A 1 355 ? -25.632 -0.728  33.171  1.00 69.30  ? 328 PRO B CD  1 
ATOM   2248 N  N   . GLY A 1 356 ? -26.085 1.671   29.164  1.00 65.14  ? 329 GLY B N   1 
ATOM   2249 C  CA  . GLY A 1 356 ? -25.529 1.835   27.817  1.00 65.38  ? 329 GLY B CA  1 
ATOM   2250 C  C   . GLY A 1 356 ? -26.163 0.933   26.774  1.00 68.99  ? 329 GLY B C   1 
ATOM   2251 O  O   . GLY A 1 356 ? -25.998 1.158   25.586  1.00 74.99  ? 329 GLY B O   1 
ATOM   2252 N  N   . PHE A 1 357 ? -26.892 -0.097  27.201  1.00 70.31  ? 330 PHE B N   1 
ATOM   2253 C  CA  . PHE A 1 357 ? -27.299 -1.149  26.275  1.00 60.84  ? 330 PHE B CA  1 
ATOM   2254 C  C   . PHE A 1 357 ? -28.361 -0.636  25.305  1.00 59.69  ? 330 PHE B C   1 
ATOM   2255 O  O   . PHE A 1 357 ? -28.150 -0.642  24.107  1.00 59.44  ? 330 PHE B O   1 
ATOM   2256 C  CB  . PHE A 1 357 ? -27.777 -2.389  27.030  1.00 55.87  ? 330 PHE B CB  1 
ATOM   2257 C  CG  . PHE A 1 357 ? -28.093 -3.558  26.139  1.00 51.83  ? 330 PHE B CG  1 
ATOM   2258 C  CD1 . PHE A 1 357 ? -27.173 -4.021  25.214  1.00 49.22  ? 330 PHE B CD1 1 
ATOM   2259 C  CD2 . PHE A 1 357 ? -29.312 -4.196  26.229  1.00 53.70  ? 330 PHE B CD2 1 
ATOM   2260 C  CE1 . PHE A 1 357 ? -27.458 -5.098  24.386  1.00 47.13  ? 330 PHE B CE1 1 
ATOM   2261 C  CE2 . PHE A 1 357 ? -29.602 -5.272  25.404  1.00 53.94  ? 330 PHE B CE2 1 
ATOM   2262 C  CZ  . PHE A 1 357 ? -28.666 -5.730  24.494  1.00 50.62  ? 330 PHE B CZ  1 
ATOM   2263 N  N   . ARG A 1 358 ? -29.482 -0.164  25.829  1.00 59.99  ? 331 ARG B N   1 
ATOM   2264 C  CA  . ARG A 1 358 ? -30.494 0.485   25.000  1.00 60.90  ? 331 ARG B CA  1 
ATOM   2265 C  C   . ARG A 1 358 ? -29.950 1.466   23.932  1.00 63.30  ? 331 ARG B C   1 
ATOM   2266 O  O   . ARG A 1 358 ? -30.451 1.492   22.823  1.00 54.61  ? 331 ARG B O   1 
ATOM   2267 C  CB  . ARG A 1 358 ? -31.485 1.222   25.869  1.00 60.47  ? 331 ARG B CB  1 
ATOM   2268 C  CG  . ARG A 1 358 ? -32.754 1.526   25.125  1.00 65.21  ? 331 ARG B CG  1 
ATOM   2269 C  CD  . ARG A 1 358 ? -33.882 1.939   26.045  1.00 67.72  ? 331 ARG B CD  1 
ATOM   2270 N  NE  . ARG A 1 358 ? -35.097 1.388   25.486  1.00 76.21  ? 331 ARG B NE  1 
ATOM   2271 C  CZ  . ARG A 1 358 ? -35.880 0.476   26.060  1.00 85.07  ? 331 ARG B CZ  1 
ATOM   2272 N  NH1 . ARG A 1 358 ? -35.664 0.010   27.290  1.00 78.76  ? 331 ARG B NH1 1 
ATOM   2273 N  NH2 . ARG A 1 358 ? -36.939 0.052   25.391  1.00 96.88  ? 331 ARG B NH2 1 
ATOM   2274 N  N   . GLU A 1 359 ? -28.928 2.255   24.259  1.00 68.73  ? 332 GLU B N   1 
ATOM   2275 C  CA  . GLU A 1 359 ? -28.300 3.138   23.262  1.00 68.53  ? 332 GLU B CA  1 
ATOM   2276 C  C   . GLU A 1 359 ? -27.593 2.328   22.187  1.00 69.14  ? 332 GLU B C   1 
ATOM   2277 O  O   . GLU A 1 359 ? -27.643 2.674   21.006  1.00 83.73  ? 332 GLU B O   1 
ATOM   2278 C  CB  . GLU A 1 359 ? -27.309 4.119   23.903  1.00 67.32  ? 332 GLU B CB  1 
ATOM   2279 N  N   . PHE A 1 360 ? -26.934 1.253   22.595  1.00 63.05  ? 333 PHE B N   1 
ATOM   2280 C  CA  . PHE A 1 360 ? -26.227 0.377   21.661  1.00 58.00  ? 333 PHE B CA  1 
ATOM   2281 C  C   . PHE A 1 360 ? -27.173 -0.301  20.641  1.00 59.81  ? 333 PHE B C   1 
ATOM   2282 O  O   . PHE A 1 360 ? -26.859 -0.443  19.443  1.00 59.13  ? 333 PHE B O   1 
ATOM   2283 C  CB  . PHE A 1 360 ? -25.474 -0.673  22.466  1.00 51.90  ? 333 PHE B CB  1 
ATOM   2284 C  CG  . PHE A 1 360 ? -24.746 -1.651  21.628  1.00 53.79  ? 333 PHE B CG  1 
ATOM   2285 C  CD1 . PHE A 1 360 ? -23.508 -1.319  21.063  1.00 53.53  ? 333 PHE B CD1 1 
ATOM   2286 C  CD2 . PHE A 1 360 ? -25.295 -2.919  21.380  1.00 50.69  ? 333 PHE B CD2 1 
ATOM   2287 C  CE1 . PHE A 1 360 ? -22.814 -2.242  20.291  1.00 51.68  ? 333 PHE B CE1 1 
ATOM   2288 C  CE2 . PHE A 1 360 ? -24.619 -3.836  20.594  1.00 49.15  ? 333 PHE B CE2 1 
ATOM   2289 C  CZ  . PHE A 1 360 ? -23.375 -3.502  20.057  1.00 52.27  ? 333 PHE B CZ  1 
ATOM   2290 N  N   . LEU A 1 361 ? -28.329 -0.716  21.140  1.00 63.19  ? 334 LEU B N   1 
ATOM   2291 C  CA  . LEU A 1 361 ? -29.351 -1.380  20.344  1.00 68.70  ? 334 LEU B CA  1 
ATOM   2292 C  C   . LEU A 1 361 ? -29.956 -0.450  19.301  1.00 75.97  ? 334 LEU B C   1 
ATOM   2293 O  O   . LEU A 1 361 ? -30.553 -0.924  18.351  1.00 76.77  ? 334 LEU B O   1 
ATOM   2294 C  CB  . LEU A 1 361 ? -30.499 -1.866  21.249  1.00 66.90  ? 334 LEU B CB  1 
ATOM   2295 C  CG  . LEU A 1 361 ? -30.630 -3.297  21.779  1.00 66.29  ? 334 LEU B CG  1 
ATOM   2296 C  CD1 . LEU A 1 361 ? -29.361 -4.137  21.685  1.00 62.58  ? 334 LEU B CD1 1 
ATOM   2297 C  CD2 . LEU A 1 361 ? -31.186 -3.258  23.200  1.00 66.60  ? 334 LEU B CD2 1 
ATOM   2298 N  N   . LYS A 1 362 ? -29.862 0.865   19.511  1.00 75.40  ? 335 LYS B N   1 
ATOM   2299 C  CA  . LYS A 1 362 ? -30.407 1.828   18.561  1.00 69.30  ? 335 LYS B CA  1 
ATOM   2300 C  C   . LYS A 1 362 ? -29.412 2.270   17.506  1.00 72.38  ? 335 LYS B C   1 
ATOM   2301 O  O   . LYS A 1 362 ? -29.778 3.006   16.617  1.00 82.99  ? 335 LYS B O   1 
ATOM   2302 C  CB  . LYS A 1 362 ? -30.956 3.034   19.287  1.00 68.99  ? 335 LYS B CB  1 
ATOM   2303 C  CG  . LYS A 1 362 ? -32.178 2.698   20.116  1.00 71.05  ? 335 LYS B CG  1 
ATOM   2304 C  CD  . LYS A 1 362 ? -32.658 3.903   20.911  1.00 73.26  ? 335 LYS B CD  1 
ATOM   2305 C  CE  . LYS A 1 362 ? -33.964 3.609   21.633  1.00 76.58  ? 335 LYS B CE  1 
ATOM   2306 N  NZ  . LYS A 1 362 ? -34.305 4.695   22.590  1.00 82.62  ? 335 LYS B NZ  1 
ATOM   2307 N  N   . LYS A 1 363 ? -28.178 1.802   17.578  1.00 76.22  ? 336 LYS B N   1 
ATOM   2308 C  CA  . LYS A 1 363 ? -27.185 2.114   16.566  1.00 87.65  ? 336 LYS B CA  1 
ATOM   2309 C  C   . LYS A 1 363 ? -27.083 1.038   15.480  1.00 88.35  ? 336 LYS B C   1 
ATOM   2310 O  O   . LYS A 1 363 ? -26.142 1.080   14.659  1.00 76.71  ? 336 LYS B O   1 
ATOM   2311 C  CB  . LYS A 1 363 ? -25.806 2.292   17.221  1.00 100.66 ? 336 LYS B CB  1 
ATOM   2312 C  CG  . LYS A 1 363 ? -25.664 3.521   18.115  1.00 103.14 ? 336 LYS B CG  1 
ATOM   2313 C  CD  . LYS A 1 363 ? -24.335 3.542   18.872  1.00 110.99 ? 336 LYS B CD  1 
ATOM   2314 C  CE  . LYS A 1 363 ? -23.120 3.255   17.990  1.00 112.30 ? 336 LYS B CE  1 
ATOM   2315 N  NZ  . LYS A 1 363 ? -21.867 3.230   18.793  1.00 115.34 ? 336 LYS B NZ  1 
ATOM   2316 N  N   . VAL A 1 364 ? -28.016 0.073   15.484  1.00 87.62  ? 337 VAL B N   1 
ATOM   2317 C  CA  . VAL A 1 364 ? -27.993 -1.033  14.499  1.00 79.76  ? 337 VAL B CA  1 
ATOM   2318 C  C   . VAL A 1 364 ? -28.073 -0.429  13.133  1.00 77.23  ? 337 VAL B C   1 
ATOM   2319 O  O   . VAL A 1 364 ? -28.876 0.483   12.920  1.00 85.44  ? 337 VAL B O   1 
ATOM   2320 C  CB  . VAL A 1 364 ? -29.228 -1.975  14.507  1.00 78.03  ? 337 VAL B CB  1 
ATOM   2321 C  CG1 . VAL A 1 364 ? -28.804 -3.379  14.100  1.00 81.71  ? 337 VAL B CG1 1 
ATOM   2322 C  CG2 . VAL A 1 364 ? -29.949 -2.000  15.826  1.00 74.02  ? 337 VAL B CG2 1 
ATOM   2323 N  N   . HIS A 1 365 ? -27.297 -0.944  12.192  1.00 74.89  ? 338 HIS B N   1 
ATOM   2324 C  CA  . HIS A 1 365 ? -27.430 -0.468  10.830  1.00 77.16  ? 338 HIS B CA  1 
ATOM   2325 C  C   . HIS A 1 365 ? -26.943 -1.482  9.844   1.00 71.21  ? 338 HIS B C   1 
ATOM   2326 O  O   . HIS A 1 365 ? -25.882 -2.030  10.035  1.00 70.44  ? 338 HIS B O   1 
ATOM   2327 C  CB  . HIS A 1 365 ? -26.629 0.812   10.620  1.00 86.82  ? 338 HIS B CB  1 
ATOM   2328 C  CG  . HIS A 1 365 ? -27.206 1.696   9.564   1.00 91.93  ? 338 HIS B CG  1 
ATOM   2329 N  ND1 . HIS A 1 365 ? -28.358 2.421   9.772   1.00 89.38  ? 338 HIS B ND1 1 
ATOM   2330 C  CD2 . HIS A 1 365 ? -26.813 1.961   8.296   1.00 82.38  ? 338 HIS B CD2 1 
ATOM   2331 C  CE1 . HIS A 1 365 ? -28.643 3.104   8.681   1.00 87.93  ? 338 HIS B CE1 1 
ATOM   2332 N  NE2 . HIS A 1 365 ? -27.723 2.840   7.771   1.00 86.50  ? 338 HIS B NE2 1 
ATOM   2333 N  N   . PRO A 1 366 ? -27.702 -1.707  8.764   1.00 69.08  ? 339 PRO B N   1 
ATOM   2334 C  CA  . PRO A 1 366 ? -27.246 -2.629  7.726   1.00 72.39  ? 339 PRO B CA  1 
ATOM   2335 C  C   . PRO A 1 366 ? -25.918 -2.249  7.076   1.00 74.02  ? 339 PRO B C   1 
ATOM   2336 O  O   . PRO A 1 366 ? -25.240 -3.109  6.567   1.00 71.76  ? 339 PRO B O   1 
ATOM   2337 C  CB  . PRO A 1 366 ? -28.361 -2.589  6.683   1.00 73.31  ? 339 PRO B CB  1 
ATOM   2338 C  CG  . PRO A 1 366 ? -29.382 -1.624  7.174   1.00 73.85  ? 339 PRO B CG  1 
ATOM   2339 C  CD  . PRO A 1 366 ? -29.104 -1.301  8.593   1.00 70.00  ? 339 PRO B CD  1 
ATOM   2340 N  N   . ARG A 1 367 ? -25.587 -0.964  7.070   1.00 85.33  ? 340 ARG B N   1 
ATOM   2341 C  CA  . ARG A 1 367 ? -24.331 -0.474  6.506   1.00 91.19  ? 340 ARG B CA  1 
ATOM   2342 C  C   . ARG A 1 367 ? -23.262 -0.381  7.593   1.00 90.09  ? 340 ARG B C   1 
ATOM   2343 O  O   . ARG A 1 367 ? -22.292 -1.128  7.562   1.00 91.48  ? 340 ARG B O   1 
ATOM   2344 C  CB  . ARG A 1 367 ? -24.534 0.900   5.834   1.00 98.31  ? 340 ARG B CB  1 
ATOM   2345 N  N   . LYS A 1 368 ? -23.456 0.528   8.551   1.00 92.61  ? 341 LYS B N   1 
ATOM   2346 C  CA  . LYS A 1 368 ? -22.516 0.765   9.671   1.00 94.36  ? 341 LYS B CA  1 
ATOM   2347 C  C   . LYS A 1 368 ? -22.003 -0.502  10.400  1.00 92.65  ? 341 LYS B C   1 
ATOM   2348 O  O   . LYS A 1 368 ? -20.813 -0.591  10.710  1.00 95.59  ? 341 LYS B O   1 
ATOM   2349 C  CB  . LYS A 1 368 ? -23.149 1.725   10.697  1.00 90.62  ? 341 LYS B CB  1 
ATOM   2350 N  N   . SER A 1 369 ? -22.887 -1.471  10.658  1.00 88.11  ? 342 SER B N   1 
ATOM   2351 C  CA  . SER A 1 369 ? -22.511 -2.748  11.324  1.00 84.11  ? 342 SER B CA  1 
ATOM   2352 C  C   . SER A 1 369 ? -21.836 -3.803  10.392  1.00 82.95  ? 342 SER B C   1 
ATOM   2353 O  O   . SER A 1 369 ? -22.482 -4.692  9.827   1.00 74.88  ? 342 SER B O   1 
ATOM   2354 C  CB  . SER A 1 369 ? -23.732 -3.348  12.037  1.00 80.87  ? 342 SER B CB  1 
ATOM   2355 O  OG  . SER A 1 369 ? -24.484 -2.351  12.728  1.00 81.62  ? 342 SER B OG  1 
ATOM   2356 N  N   . VAL A 1 370 ? -20.520 -3.682  10.247  1.00 87.27  ? 343 VAL B N   1 
ATOM   2357 C  CA  . VAL A 1 370 ? -19.746 -4.579  9.397   1.00 90.63  ? 343 VAL B CA  1 
ATOM   2358 C  C   . VAL A 1 370 ? -19.708 -6.008  9.963   1.00 86.18  ? 343 VAL B C   1 
ATOM   2359 O  O   . VAL A 1 370 ? -19.961 -6.972  9.251   1.00 85.05  ? 343 VAL B O   1 
ATOM   2360 C  CB  . VAL A 1 370 ? -18.297 -4.059  9.208   1.00 82.43  ? 343 VAL B CB  1 
ATOM   2361 N  N   . HIS A 1 371 ? -19.412 -6.135  11.250  1.00 80.61  ? 344 HIS B N   1 
ATOM   2362 C  CA  . HIS A 1 371 ? -19.113 -7.437  11.847  1.00 80.06  ? 344 HIS B CA  1 
ATOM   2363 C  C   . HIS A 1 371 ? -20.381 -8.295  12.091  1.00 80.50  ? 344 HIS B C   1 
ATOM   2364 O  O   . HIS A 1 371 ? -20.356 -9.520  11.912  1.00 71.18  ? 344 HIS B O   1 
ATOM   2365 C  CB  . HIS A 1 371 ? -18.305 -7.237  13.135  1.00 79.09  ? 344 HIS B CB  1 
ATOM   2366 C  CG  . HIS A 1 371 ? -17.053 -6.428  12.938  1.00 86.71  ? 344 HIS B CG  1 
ATOM   2367 N  ND1 . HIS A 1 371 ? -15.959 -6.901  12.236  1.00 87.92  ? 344 HIS B ND1 1 
ATOM   2368 C  CD2 . HIS A 1 371 ? -16.729 -5.170  13.337  1.00 82.60  ? 344 HIS B CD2 1 
ATOM   2369 C  CE1 . HIS A 1 371 ? -15.017 -5.971  12.214  1.00 82.46  ? 344 HIS B CE1 1 
ATOM   2370 N  NE2 . HIS A 1 371 ? -15.457 -4.914  12.880  1.00 78.36  ? 344 HIS B NE2 1 
ATOM   2371 N  N   . ASN A 1 372 ? -21.491 -7.640  12.437  1.00 70.43  ? 345 ASN B N   1 
ATOM   2372 C  CA  . ASN A 1 372 ? -22.779 -8.315  12.621  1.00 61.39  ? 345 ASN B CA  1 
ATOM   2373 C  C   . ASN A 1 372 ? -23.613 -8.604  11.354  1.00 61.22  ? 345 ASN B C   1 
ATOM   2374 O  O   . ASN A 1 372 ? -24.540 -7.869  11.032  1.00 66.71  ? 345 ASN B O   1 
ATOM   2375 C  CB  . ASN A 1 372 ? -23.617 -7.488  13.590  1.00 59.47  ? 345 ASN B CB  1 
ATOM   2376 C  CG  . ASN A 1 372 ? -24.820 -8.243  14.096  1.00 56.68  ? 345 ASN B CG  1 
ATOM   2377 O  OD1 . ASN A 1 372 ? -25.147 -9.319  13.586  1.00 48.98  ? 345 ASN B OD1 1 
ATOM   2378 N  ND2 . ASN A 1 372 ? -25.497 -7.681  15.102  1.00 56.67  ? 345 ASN B ND2 1 
ATOM   2379 N  N   . GLY A 1 373 ? -23.338 -9.716  10.680  1.00 61.78  ? 346 GLY B N   1 
ATOM   2380 C  CA  . GLY A 1 373 ? -24.085 -10.119 9.474   1.00 55.80  ? 346 GLY B CA  1 
ATOM   2381 C  C   . GLY A 1 373 ? -25.518 -10.598 9.648   1.00 62.85  ? 346 GLY B C   1 
ATOM   2382 O  O   . GLY A 1 373 ? -26.101 -11.156 8.711   1.00 73.25  ? 346 GLY B O   1 
ATOM   2383 N  N   . PHE A 1 374 ? -26.089 -10.404 10.839  1.00 61.21  ? 347 PHE B N   1 
ATOM   2384 C  CA  . PHE A 1 374 ? -27.503 -10.649 11.091  1.00 54.28  ? 347 PHE B CA  1 
ATOM   2385 C  C   . PHE A 1 374 ? -28.286 -9.354  11.001  1.00 53.66  ? 347 PHE B C   1 
ATOM   2386 O  O   . PHE A 1 374 ? -29.509 -9.373  11.036  1.00 52.99  ? 347 PHE B O   1 
ATOM   2387 C  CB  . PHE A 1 374 ? -27.696 -11.259 12.480  1.00 54.55  ? 347 PHE B CB  1 
ATOM   2388 C  CG  . PHE A 1 374 ? -27.190 -12.667 12.597  1.00 55.91  ? 347 PHE B CG  1 
ATOM   2389 C  CD1 . PHE A 1 374 ? -27.812 -13.697 11.924  1.00 55.61  ? 347 PHE B CD1 1 
ATOM   2390 C  CD2 . PHE A 1 374 ? -26.086 -12.967 13.387  1.00 58.62  ? 347 PHE B CD2 1 
ATOM   2391 C  CE1 . PHE A 1 374 ? -27.344 -14.998 12.018  1.00 56.49  ? 347 PHE B CE1 1 
ATOM   2392 C  CE2 . PHE A 1 374 ? -25.612 -14.263 13.484  1.00 56.48  ? 347 PHE B CE2 1 
ATOM   2393 C  CZ  . PHE A 1 374 ? -26.246 -15.282 12.802  1.00 57.12  ? 347 PHE B CZ  1 
ATOM   2394 N  N   . ALA A 1 375 ? -27.565 -8.236  10.905  1.00 57.61  ? 348 ALA B N   1 
ATOM   2395 C  CA  . ALA A 1 375 ? -28.150 -6.889  10.905  1.00 60.75  ? 348 ALA B CA  1 
ATOM   2396 C  C   . ALA A 1 375 ? -28.947 -6.547  9.637   1.00 61.30  ? 348 ALA B C   1 
ATOM   2397 O  O   . ALA A 1 375 ? -29.903 -5.775  9.699   1.00 62.43  ? 348 ALA B O   1 
ATOM   2398 C  CB  . ALA A 1 375 ? -27.046 -5.870  11.094  1.00 61.31  ? 348 ALA B CB  1 
ATOM   2399 N  N   . LYS A 1 376 ? -28.518 -7.093  8.500   1.00 58.74  ? 349 LYS B N   1 
ATOM   2400 C  CA  . LYS A 1 376 ? -29.259 -6.966  7.267   1.00 59.78  ? 349 LYS B CA  1 
ATOM   2401 C  C   . LYS A 1 376 ? -30.682 -7.511  7.510   1.00 58.05  ? 349 LYS B C   1 
ATOM   2402 O  O   . LYS A 1 376 ? -31.607 -6.707  7.640   1.00 55.72  ? 349 LYS B O   1 
ATOM   2403 C  CB  . LYS A 1 376 ? -28.523 -7.667  6.099   1.00 56.27  ? 349 LYS B CB  1 
ATOM   2404 N  N   . GLU A 1 377 ? -30.854 -8.839  7.635   1.00 57.04  ? 350 GLU B N   1 
ATOM   2405 C  CA  . GLU A 1 377 ? -32.205 -9.444  7.815   1.00 52.15  ? 350 GLU B CA  1 
ATOM   2406 C  C   . GLU A 1 377 ? -32.982 -8.854  8.991   1.00 49.31  ? 350 GLU B C   1 
ATOM   2407 O  O   . GLU A 1 377 ? -34.204 -8.799  8.983   1.00 56.37  ? 350 GLU B O   1 
ATOM   2408 C  CB  . GLU A 1 377 ? -32.147 -10.962 7.980   1.00 55.35  ? 350 GLU B CB  1 
ATOM   2409 C  CG  . GLU A 1 377 ? -33.540 -11.611 8.052   1.00 63.77  ? 350 GLU B CG  1 
ATOM   2410 C  CD  . GLU A 1 377 ? -33.556 -13.127 8.302   1.00 77.14  ? 350 GLU B CD  1 
ATOM   2411 O  OE1 . GLU A 1 377 ? -32.572 -13.653 8.876   1.00 92.25  ? 350 GLU B OE1 1 
ATOM   2412 O  OE2 . GLU A 1 377 ? -34.573 -13.795 7.952   1.00 80.39  ? 350 GLU B OE2 1 
ATOM   2413 N  N   . PHE A 1 378 ? -32.287 -8.417  10.019  1.00 50.16  ? 351 PHE B N   1 
ATOM   2414 C  CA  . PHE A 1 378 ? -32.956 -7.696  11.074  1.00 51.48  ? 351 PHE B CA  1 
ATOM   2415 C  C   . PHE A 1 378 ? -33.723 -6.519  10.470  1.00 54.98  ? 351 PHE B C   1 
ATOM   2416 O  O   . PHE A 1 378 ? -34.906 -6.352  10.736  1.00 61.64  ? 351 PHE B O   1 
ATOM   2417 C  CB  . PHE A 1 378 ? -31.961 -7.209  12.130  1.00 49.32  ? 351 PHE B CB  1 
ATOM   2418 C  CG  . PHE A 1 378 ? -32.546 -6.194  13.063  1.00 53.25  ? 351 PHE B CG  1 
ATOM   2419 C  CD1 . PHE A 1 378 ? -33.490 -6.570  13.996  1.00 54.04  ? 351 PHE B CD1 1 
ATOM   2420 C  CD2 . PHE A 1 378 ? -32.204 -4.863  12.963  1.00 51.05  ? 351 PHE B CD2 1 
ATOM   2421 C  CE1 . PHE A 1 378 ? -34.059 -5.633  14.839  1.00 58.76  ? 351 PHE B CE1 1 
ATOM   2422 C  CE2 . PHE A 1 378 ? -32.773 -3.931  13.800  1.00 54.52  ? 351 PHE B CE2 1 
ATOM   2423 C  CZ  . PHE A 1 378 ? -33.712 -4.311  14.732  1.00 56.15  ? 351 PHE B CZ  1 
ATOM   2424 N  N   . TRP A 1 379 ? -33.035 -5.716  9.667   1.00 56.55  ? 352 TRP B N   1 
ATOM   2425 C  CA  . TRP A 1 379 ? -33.592 -4.493  9.095   1.00 66.38  ? 352 TRP B CA  1 
ATOM   2426 C  C   . TRP A 1 379 ? -34.821 -4.764  8.243   1.00 63.15  ? 352 TRP B C   1 
ATOM   2427 O  O   . TRP A 1 379 ? -35.915 -4.227  8.476   1.00 56.13  ? 352 TRP B O   1 
ATOM   2428 C  CB  . TRP A 1 379 ? -32.536 -3.808  8.220   1.00 71.29  ? 352 TRP B CB  1 
ATOM   2429 C  CG  . TRP A 1 379 ? -32.801 -2.388  8.063   1.00 78.21  ? 352 TRP B CG  1 
ATOM   2430 C  CD1 . TRP A 1 379 ? -33.296 -1.772  6.979   1.00 77.38  ? 352 TRP B CD1 1 
ATOM   2431 C  CD2 . TRP A 1 379 ? -32.601 -1.377  9.058   1.00 81.01  ? 352 TRP B CD2 1 
ATOM   2432 N  NE1 . TRP A 1 379 ? -33.415 -0.417  7.221   1.00 84.87  ? 352 TRP B NE1 1 
ATOM   2433 C  CE2 . TRP A 1 379 ? -32.986 -0.154  8.492   1.00 79.22  ? 352 TRP B CE2 1 
ATOM   2434 C  CE3 . TRP A 1 379 ? -32.129 -1.392  10.369  1.00 71.37  ? 352 TRP B CE3 1 
ATOM   2435 C  CZ2 . TRP A 1 379 ? -32.912 1.041   9.187   1.00 79.24  ? 352 TRP B CZ2 1 
ATOM   2436 C  CZ3 . TRP A 1 379 ? -32.053 -0.208  11.056  1.00 73.67  ? 352 TRP B CZ3 1 
ATOM   2437 C  CH2 . TRP A 1 379 ? -32.443 0.991   10.472  1.00 75.87  ? 352 TRP B CH2 1 
ATOM   2438 N  N   . GLU A 1 380 ? -34.597 -5.629  7.261   1.00 60.85  ? 353 GLU B N   1 
ATOM   2439 C  CA  . GLU A 1 380 ? -35.613 -6.087  6.359   1.00 61.75  ? 353 GLU B CA  1 
ATOM   2440 C  C   . GLU A 1 380 ? -36.840 -6.564  7.135   1.00 65.52  ? 353 GLU B C   1 
ATOM   2441 O  O   . GLU A 1 380 ? -37.957 -6.205  6.787   1.00 78.13  ? 353 GLU B O   1 
ATOM   2442 C  CB  . GLU A 1 380 ? -35.056 -7.200  5.449   1.00 65.93  ? 353 GLU B CB  1 
ATOM   2443 C  CG  . GLU A 1 380 ? -34.015 -6.750  4.400   1.00 72.39  ? 353 GLU B CG  1 
ATOM   2444 C  CD  . GLU A 1 380 ? -33.460 -7.889  3.519   1.00 77.01  ? 353 GLU B CD  1 
ATOM   2445 O  OE1 . GLU A 1 380 ? -33.640 -9.071  3.872   1.00 87.12  ? 353 GLU B OE1 1 
ATOM   2446 O  OE2 . GLU A 1 380 ? -32.827 -7.619  2.467   1.00 79.15  ? 353 GLU B OE2 1 
ATOM   2447 N  N   . GLU A 1 381 ? -36.657 -7.353  8.191   1.00 60.40  ? 354 GLU B N   1 
ATOM   2448 C  CA  . GLU A 1 381 ? -37.808 -7.845  8.922   1.00 57.71  ? 354 GLU B CA  1 
ATOM   2449 C  C   . GLU A 1 381 ? -38.526 -6.720  9.643   1.00 60.33  ? 354 GLU B C   1 
ATOM   2450 O  O   . GLU A 1 381 ? -39.744 -6.684  9.728   1.00 64.16  ? 354 GLU B O   1 
ATOM   2451 C  CB  . GLU A 1 381 ? -37.392 -8.924  9.900   1.00 59.48  ? 354 GLU B CB  1 
ATOM   2452 C  CG  . GLU A 1 381 ? -37.037 -10.216 9.218   1.00 68.08  ? 354 GLU B CG  1 
ATOM   2453 C  CD  . GLU A 1 381 ? -38.229 -10.806 8.500   1.00 75.65  ? 354 GLU B CD  1 
ATOM   2454 O  OE1 . GLU A 1 381 ? -38.167 -10.909 7.254   1.00 79.49  ? 354 GLU B OE1 1 
ATOM   2455 O  OE2 . GLU A 1 381 ? -39.234 -11.127 9.180   1.00 72.47  ? 354 GLU B OE2 1 
ATOM   2456 N  N   . THR A 1 382 ? -37.757 -5.792  10.172  1.00 69.15  ? 355 THR B N   1 
ATOM   2457 C  CA  . THR A 1 382 ? -38.311 -4.739  10.991  1.00 72.53  ? 355 THR B CA  1 
ATOM   2458 C  C   . THR A 1 382 ? -39.156 -3.822  10.100  1.00 75.78  ? 355 THR B C   1 
ATOM   2459 O  O   . THR A 1 382 ? -40.296 -3.482  10.418  1.00 66.14  ? 355 THR B O   1 
ATOM   2460 C  CB  . THR A 1 382 ? -37.177 -3.929  11.661  1.00 72.85  ? 355 THR B CB  1 
ATOM   2461 O  OG1 . THR A 1 382 ? -36.299 -4.811  12.391  1.00 64.01  ? 355 THR B OG1 1 
ATOM   2462 C  CG2 . THR A 1 382 ? -37.761 -2.857  12.589  1.00 68.58  ? 355 THR B CG2 1 
ATOM   2463 N  N   . PHE A 1 383 ? -38.582 -3.449  8.965   1.00 79.66  ? 356 PHE B N   1 
ATOM   2464 C  CA  . PHE A 1 383 ? -39.179 -2.451  8.102   1.00 80.42  ? 356 PHE B CA  1 
ATOM   2465 C  C   . PHE A 1 383 ? -39.854 -3.040  6.870   1.00 82.53  ? 356 PHE B C   1 
ATOM   2466 O  O   . PHE A 1 383 ? -40.295 -2.311  5.986   1.00 74.75  ? 356 PHE B O   1 
ATOM   2467 C  CB  . PHE A 1 383 ? -38.099 -1.475  7.704   1.00 75.19  ? 356 PHE B CB  1 
ATOM   2468 C  CG  . PHE A 1 383 ? -37.550 -0.718  8.860   1.00 75.31  ? 356 PHE B CG  1 
ATOM   2469 C  CD1 . PHE A 1 383 ? -38.378 0.121   9.611   1.00 69.63  ? 356 PHE B CD1 1 
ATOM   2470 C  CD2 . PHE A 1 383 ? -36.213 -0.842  9.218   1.00 76.30  ? 356 PHE B CD2 1 
ATOM   2471 C  CE1 . PHE A 1 383 ? -37.872 0.842   10.681  1.00 68.28  ? 356 PHE B CE1 1 
ATOM   2472 C  CE2 . PHE A 1 383 ? -35.711 -0.120  10.289  1.00 75.15  ? 356 PHE B CE2 1 
ATOM   2473 C  CZ  . PHE A 1 383 ? -36.538 0.725   11.017  1.00 66.88  ? 356 PHE B CZ  1 
ATOM   2474 N  N   . ASN A 1 384 ? -39.926 -4.365  6.825   1.00 88.34  ? 357 ASN B N   1 
ATOM   2475 C  CA  . ASN A 1 384 ? -40.730 -5.063  5.841   1.00 85.91  ? 357 ASN B CA  1 
ATOM   2476 C  C   . ASN A 1 384 ? -40.317 -4.713  4.415   1.00 79.05  ? 357 ASN B C   1 
ATOM   2477 O  O   . ASN A 1 384 ? -41.157 -4.498  3.578   1.00 77.75  ? 357 ASN B O   1 
ATOM   2478 C  CB  . ASN A 1 384 ? -42.199 -4.721  6.083   1.00 88.10  ? 357 ASN B CB  1 
ATOM   2479 C  CG  . ASN A 1 384 ? -43.113 -5.879  5.807   1.00 89.36  ? 357 ASN B CG  1 
ATOM   2480 O  OD1 . ASN A 1 384 ? -43.995 -6.184  6.613   1.00 101.72 ? 357 ASN B OD1 1 
ATOM   2481 N  ND2 . ASN A 1 384 ? -42.906 -6.545  4.683   1.00 80.96  ? 357 ASN B ND2 1 
ATOM   2482 N  N   . CYS A 1 385 ? -39.015 -4.687  4.152   1.00 79.72  ? 358 CYS B N   1 
ATOM   2483 C  CA  . CYS A 1 385 ? -38.486 -4.245  2.878   1.00 82.19  ? 358 CYS B CA  1 
ATOM   2484 C  C   . CYS A 1 385 ? -37.286 -5.118  2.421   1.00 83.29  ? 358 CYS B C   1 
ATOM   2485 O  O   . CYS A 1 385 ? -37.057 -6.176  2.983   1.00 83.73  ? 358 CYS B O   1 
ATOM   2486 C  CB  . CYS A 1 385 ? -38.117 -2.769  3.029   1.00 89.53  ? 358 CYS B CB  1 
ATOM   2487 S  SG  . CYS A 1 385 ? -36.887 -2.418  4.300   1.00 87.50  ? 358 CYS B SG  1 
ATOM   2488 N  N   . HIS A 1 386 ? -36.538 -4.682  1.404   1.00 80.71  ? 359 HIS B N   1 
ATOM   2489 C  CA  . HIS A 1 386 ? -35.430 -5.449  0.833   1.00 79.12  ? 359 HIS B CA  1 
ATOM   2490 C  C   . HIS A 1 386 ? -34.253 -4.509  0.623   1.00 85.74  ? 359 HIS B C   1 
ATOM   2491 O  O   . HIS A 1 386 ? -34.443 -3.304  0.574   1.00 97.11  ? 359 HIS B O   1 
ATOM   2492 C  CB  . HIS A 1 386 ? -35.881 -6.033  -0.501  1.00 87.41  ? 359 HIS B CB  1 
ATOM   2493 C  CG  . HIS A 1 386 ? -34.816 -6.781  -1.237  1.00 87.83  ? 359 HIS B CG  1 
ATOM   2494 N  ND1 . HIS A 1 386 ? -34.615 -8.133  -1.074  1.00 96.71  ? 359 HIS B ND1 1 
ATOM   2495 C  CD2 . HIS A 1 386 ? -33.908 -6.373  -2.156  1.00 86.02  ? 359 HIS B CD2 1 
ATOM   2496 C  CE1 . HIS A 1 386 ? -33.622 -8.526  -1.853  1.00 98.92  ? 359 HIS B CE1 1 
ATOM   2497 N  NE2 . HIS A 1 386 ? -33.171 -7.475  -2.516  1.00 91.63  ? 359 HIS B NE2 1 
ATOM   2498 N  N   . LEU A 1 387 ? -33.045 -5.048  0.473   1.00 92.41  ? 360 LEU B N   1 
ATOM   2499 C  CA  . LEU A 1 387 ? -31.816 -4.246  0.473   1.00 96.09  ? 360 LEU B CA  1 
ATOM   2500 C  C   . LEU A 1 387 ? -30.936 -4.381  -0.780  1.00 100.53 ? 360 LEU B C   1 
ATOM   2501 O  O   . LEU A 1 387 ? -30.670 -5.495  -1.235  1.00 107.47 ? 360 LEU B O   1 
ATOM   2502 C  CB  . LEU A 1 387 ? -30.990 -4.676  1.685   1.00 106.25 ? 360 LEU B CB  1 
ATOM   2503 C  CG  . LEU A 1 387 ? -30.346 -3.598  2.559   1.00 107.25 ? 360 LEU B CG  1 
ATOM   2504 C  CD1 . LEU A 1 387 ? -31.378 -2.633  3.142   1.00 106.76 ? 360 LEU B CD1 1 
ATOM   2505 C  CD2 . LEU A 1 387 ? -29.569 -4.298  3.662   1.00 107.37 ? 360 LEU B CD2 1 
ATOM   2506 N  N   . GLN A 1 388 ? -30.445 -3.250  -1.297  1.00 106.77 ? 361 GLN B N   1 
ATOM   2507 C  CA  . GLN A 1 388 ? -29.565 -3.235  -2.483  1.00 105.94 ? 361 GLN B CA  1 
ATOM   2508 C  C   . GLN A 1 388 ? -28.164 -3.748  -2.157  1.00 96.94  ? 361 GLN B C   1 
ATOM   2509 O  O   . GLN A 1 388 ? -27.858 -4.917  -2.387  1.00 90.75  ? 361 GLN B O   1 
ATOM   2510 C  CB  . GLN A 1 388 ? -29.465 -1.818  -3.072  1.00 106.82 ? 361 GLN B CB  1 
ATOM   2511 N  N   . PHE A 1 418 ? -44.205 -7.558  -4.946  1.00 99.62  ? 391 PHE B N   1 
ATOM   2512 C  CA  . PHE A 1 418 ? -43.061 -6.644  -4.846  1.00 83.83  ? 391 PHE B CA  1 
ATOM   2513 C  C   . PHE A 1 418 ? -42.764 -6.347  -3.389  1.00 80.04  ? 391 PHE B C   1 
ATOM   2514 O  O   . PHE A 1 418 ? -43.648 -5.977  -2.623  1.00 81.91  ? 391 PHE B O   1 
ATOM   2515 C  CB  . PHE A 1 418 ? -43.338 -5.323  -5.589  1.00 72.76  ? 391 PHE B CB  1 
ATOM   2516 C  CG  . PHE A 1 418 ? -42.162 -4.402  -5.652  1.00 62.44  ? 391 PHE B CG  1 
ATOM   2517 C  CD1 . PHE A 1 418 ? -40.951 -4.832  -6.212  1.00 65.10  ? 391 PHE B CD1 1 
ATOM   2518 C  CD2 . PHE A 1 418 ? -42.257 -3.089  -5.187  1.00 66.22  ? 391 PHE B CD2 1 
ATOM   2519 C  CE1 . PHE A 1 418 ? -39.839 -3.983  -6.291  1.00 67.32  ? 391 PHE B CE1 1 
ATOM   2520 C  CE2 . PHE A 1 418 ? -41.149 -2.227  -5.258  1.00 72.89  ? 391 PHE B CE2 1 
ATOM   2521 C  CZ  . PHE A 1 418 ? -39.938 -2.672  -5.814  1.00 72.61  ? 391 PHE B CZ  1 
ATOM   2522 N  N   . ARG A 1 419 ? -41.513 -6.507  -3.013  1.00 75.70  ? 392 ARG B N   1 
ATOM   2523 C  CA  . ARG A 1 419 ? -41.102 -6.180  -1.681  1.00 75.49  ? 392 ARG B CA  1 
ATOM   2524 C  C   . ARG A 1 419 ? -40.422 -4.830  -1.805  1.00 69.75  ? 392 ARG B C   1 
ATOM   2525 O  O   . ARG A 1 419 ? -39.427 -4.690  -2.505  1.00 61.36  ? 392 ARG B O   1 
ATOM   2526 C  CB  . ARG A 1 419 ? -40.154 -7.265  -1.175  1.00 86.85  ? 392 ARG B CB  1 
ATOM   2527 C  CG  . ARG A 1 419 ? -39.959 -7.289  0.328   1.00 95.47  ? 392 ARG B CG  1 
ATOM   2528 C  CD  . ARG A 1 419 ? -39.757 -8.712  0.829   1.00 99.02  ? 392 ARG B CD  1 
ATOM   2529 N  NE  . ARG A 1 419 ? -38.967 -8.757  2.061   1.00 104.41 ? 392 ARG B NE  1 
ATOM   2530 C  CZ  . ARG A 1 419 ? -39.407 -8.387  3.265   1.00 110.38 ? 392 ARG B CZ  1 
ATOM   2531 N  NH1 . ARG A 1 419 ? -40.643 -7.923  3.435   1.00 115.70 ? 392 ARG B NH1 1 
ATOM   2532 N  NH2 . ARG A 1 419 ? -38.601 -8.471  4.318   1.00 106.59 ? 392 ARG B NH2 1 
ATOM   2533 N  N   . PRO A 1 420 ? -40.955 -3.817  -1.132  1.00 75.74  ? 393 PRO B N   1 
ATOM   2534 C  CA  . PRO A 1 420 ? -40.396 -2.478  -1.394  1.00 77.93  ? 393 PRO B CA  1 
ATOM   2535 C  C   . PRO A 1 420 ? -38.931 -2.436  -1.050  1.00 76.65  ? 393 PRO B C   1 
ATOM   2536 O  O   . PRO A 1 420 ? -38.571 -3.059  -0.070  1.00 92.45  ? 393 PRO B O   1 
ATOM   2537 C  CB  . PRO A 1 420 ? -41.196 -1.560  -0.464  1.00 79.18  ? 393 PRO B CB  1 
ATOM   2538 C  CG  . PRO A 1 420 ? -41.971 -2.451  0.471   1.00 77.76  ? 393 PRO B CG  1 
ATOM   2539 C  CD  . PRO A 1 420 ? -41.938 -3.857  -0.031  1.00 75.31  ? 393 PRO B CD  1 
ATOM   2540 N  N   . LEU A 1 421 ? -38.086 -1.755  -1.830  1.00 78.21  ? 394 LEU B N   1 
ATOM   2541 C  CA  . LEU A 1 421 ? -36.663 -1.569  -1.427  1.00 87.15  ? 394 LEU B CA  1 
ATOM   2542 C  C   . LEU A 1 421 ? -36.532 -0.660  -0.172  1.00 97.09  ? 394 LEU B C   1 
ATOM   2543 O  O   . LEU A 1 421 ? -37.447 0.129   0.125   1.00 95.35  ? 394 LEU B O   1 
ATOM   2544 C  CB  . LEU A 1 421 ? -35.813 -1.023  -2.575  1.00 82.64  ? 394 LEU B CB  1 
ATOM   2545 N  N   . CYS A 1 422 ? -35.420 -0.796  0.569   1.00 101.12 ? 395 CYS B N   1 
ATOM   2546 C  CA  . CYS A 1 422 ? -35.215 -0.068  1.849   1.00 102.93 ? 395 CYS B CA  1 
ATOM   2547 C  C   . CYS A 1 422 ? -34.352 1.169   1.652   1.00 98.87  ? 395 CYS B C   1 
ATOM   2548 O  O   . CYS A 1 422 ? -33.288 1.092   1.018   1.00 83.89  ? 395 CYS B O   1 
ATOM   2549 C  CB  . CYS A 1 422 ? -34.526 -0.929  2.932   1.00 106.56 ? 395 CYS B CB  1 
ATOM   2550 S  SG  . CYS A 1 422 ? -35.139 -2.610  3.253   1.00 111.70 ? 395 CYS B SG  1 
ATOM   2551 N  N   . THR A 1 423 ? -34.786 2.287   2.249   1.00 104.93 ? 396 THR B N   1 
ATOM   2552 C  CA  . THR A 1 423 ? -34.095 3.589   2.113   1.00 95.72  ? 396 THR B CA  1 
ATOM   2553 C  C   . THR A 1 423 ? -32.697 3.468   2.667   1.00 91.49  ? 396 THR B C   1 
ATOM   2554 O  O   . THR A 1 423 ? -31.763 4.003   2.094   1.00 89.40  ? 396 THR B O   1 
ATOM   2555 C  CB  . THR A 1 423 ? -34.814 4.783   2.840   1.00 102.23 ? 396 THR B CB  1 
ATOM   2556 O  OG1 . THR A 1 423 ? -34.565 4.752   4.251   1.00 97.11  ? 396 THR B OG1 1 
ATOM   2557 C  CG2 . THR A 1 423 ? -36.339 4.799   2.613   1.00 106.73 ? 396 THR B CG2 1 
ATOM   2558 N  N   . GLY A 1 424 ? -32.578 2.732   3.775   1.00 96.67  ? 397 GLY B N   1 
ATOM   2559 C  CA  . GLY A 1 424 ? -31.379 2.704   4.599   1.00 93.41  ? 397 GLY B CA  1 
ATOM   2560 C  C   . GLY A 1 424 ? -31.468 3.722   5.733   1.00 97.48  ? 397 GLY B C   1 
ATOM   2561 O  O   . GLY A 1 424 ? -30.715 3.644   6.697   1.00 102.44 ? 397 GLY B O   1 
ATOM   2562 N  N   . ASP A 1 425 ? -32.407 4.663   5.636   1.00 96.17  ? 398 ASP B N   1 
ATOM   2563 C  CA  . ASP A 1 425 ? -32.466 5.808   6.538   1.00 96.58  ? 398 ASP B CA  1 
ATOM   2564 C  C   . ASP A 1 425 ? -33.714 5.745   7.427   1.00 89.39  ? 398 ASP B C   1 
ATOM   2565 O  O   . ASP A 1 425 ? -34.091 6.746   8.052   1.00 90.22  ? 398 ASP B O   1 
ATOM   2566 C  CB  . ASP A 1 425 ? -32.444 7.128   5.729   1.00 102.30 ? 398 ASP B CB  1 
ATOM   2567 C  CG  . ASP A 1 425 ? -31.230 7.240   4.773   1.00 109.59 ? 398 ASP B CG  1 
ATOM   2568 O  OD1 . ASP A 1 425 ? -30.091 6.905   5.167   1.00 112.57 ? 398 ASP B OD1 1 
ATOM   2569 O  OD2 . ASP A 1 425 ? -31.414 7.683   3.619   1.00 109.01 ? 398 ASP B OD2 1 
ATOM   2570 N  N   . GLU A 1 426 ? -34.355 4.579   7.497   1.00 79.68  ? 399 GLU B N   1 
ATOM   2571 C  CA  . GLU A 1 426 ? -35.556 4.433   8.348   1.00 78.46  ? 399 GLU B CA  1 
ATOM   2572 C  C   . GLU A 1 426 ? -35.190 4.337   9.859   1.00 74.93  ? 399 GLU B C   1 
ATOM   2573 O  O   . GLU A 1 426 ? -34.012 4.207   10.213  1.00 66.93  ? 399 GLU B O   1 
ATOM   2574 C  CB  . GLU A 1 426 ? -36.477 3.283   7.877   1.00 78.24  ? 399 GLU B CB  1 
ATOM   2575 C  CG  . GLU A 1 426 ? -35.803 2.047   7.286   1.00 82.56  ? 399 GLU B CG  1 
ATOM   2576 C  CD  . GLU A 1 426 ? -35.681 2.034   5.760   1.00 86.51  ? 399 GLU B CD  1 
ATOM   2577 O  OE1 . GLU A 1 426 ? -36.689 2.254   5.059   1.00 93.31  ? 399 GLU B OE1 1 
ATOM   2578 O  OE2 . GLU A 1 426 ? -34.575 1.753   5.252   1.00 77.49  ? 399 GLU B OE2 1 
ATOM   2579 N  N   . ASN A 1 427 ? -36.190 4.448   10.735  1.00 70.98  ? 400 ASN B N   1 
ATOM   2580 C  CA  . ASN A 1 427 ? -35.955 4.679   12.163  1.00 74.56  ? 400 ASN B CA  1 
ATOM   2581 C  C   . ASN A 1 427 ? -36.470 3.561   13.053  1.00 77.64  ? 400 ASN B C   1 
ATOM   2582 O  O   . ASN A 1 427 ? -37.676 3.270   13.072  1.00 71.91  ? 400 ASN B O   1 
ATOM   2583 C  CB  . ASN A 1 427 ? -36.596 5.999   12.614  1.00 83.19  ? 400 ASN B CB  1 
ATOM   2584 C  CG  . ASN A 1 427 ? -36.074 6.468   13.973  1.00 92.21  ? 400 ASN B CG  1 
ATOM   2585 O  OD1 . ASN A 1 427 ? -36.346 5.857   15.023  1.00 97.20  ? 400 ASN B OD1 1 
ATOM   2586 N  ND2 . ASN A 1 427 ? -35.308 7.553   13.957  1.00 90.01  ? 400 ASN B ND2 1 
ATOM   2587 N  N   . ILE A 1 428 ? -35.555 2.977   13.828  1.00 79.34  ? 401 ILE B N   1 
ATOM   2588 C  CA  . ILE A 1 428 ? -35.887 1.852   14.714  1.00 84.09  ? 401 ILE B CA  1 
ATOM   2589 C  C   . ILE A 1 428 ? -37.010 2.163   15.698  1.00 81.12  ? 401 ILE B C   1 
ATOM   2590 O  O   . ILE A 1 428 ? -37.787 1.278   16.057  1.00 86.71  ? 401 ILE B O   1 
ATOM   2591 C  CB  . ILE A 1 428 ? -34.631 1.324   15.458  1.00 86.30  ? 401 ILE B CB  1 
ATOM   2592 C  CG1 . ILE A 1 428 ? -33.920 0.301   14.578  1.00 84.94  ? 401 ILE B CG1 1 
ATOM   2593 C  CG2 . ILE A 1 428 ? -34.980 0.653   16.783  1.00 84.88  ? 401 ILE B CG2 1 
ATOM   2594 C  CD1 . ILE A 1 428 ? -32.487 0.082   14.974  1.00 88.50  ? 401 ILE B CD1 1 
ATOM   2595 N  N   . SER A 1 429 ? -37.115 3.421   16.112  1.00 83.19  ? 402 SER B N   1 
ATOM   2596 C  CA  . SER A 1 429 ? -38.104 3.800   17.110  1.00 80.93  ? 402 SER B CA  1 
ATOM   2597 C  C   . SER A 1 429 ? -39.566 3.892   16.559  1.00 78.38  ? 402 SER B C   1 
ATOM   2598 O  O   . SER A 1 429 ? -40.502 4.094   17.327  1.00 77.25  ? 402 SER B O   1 
ATOM   2599 C  CB  . SER A 1 429 ? -37.644 5.090   17.820  1.00 74.29  ? 402 SER B CB  1 
ATOM   2600 N  N   . SER A 1 430 ? -39.780 3.703   15.257  1.00 78.17  ? 403 SER B N   1 
ATOM   2601 C  CA  . SER A 1 430 ? -41.146 3.806   14.672  1.00 79.94  ? 403 SER B CA  1 
ATOM   2602 C  C   . SER A 1 430 ? -41.954 2.503   14.650  1.00 89.01  ? 403 SER B C   1 
ATOM   2603 O  O   . SER A 1 430 ? -43.183 2.533   14.604  1.00 86.37  ? 403 SER B O   1 
ATOM   2604 C  CB  . SER A 1 430 ? -41.072 4.343   13.243  1.00 75.36  ? 403 SER B CB  1 
ATOM   2605 O  OG  . SER A 1 430 ? -40.006 3.719   12.546  1.00 75.47  ? 403 SER B OG  1 
ATOM   2606 N  N   . VAL A 1 431 ? -41.266 1.363   14.647  1.00 99.11  ? 404 VAL B N   1 
ATOM   2607 C  CA  . VAL A 1 431 ? -41.925 0.064   14.589  1.00 92.16  ? 404 VAL B CA  1 
ATOM   2608 C  C   . VAL A 1 431 ? -41.730 -0.607  15.937  1.00 89.89  ? 404 VAL B C   1 
ATOM   2609 O  O   . VAL A 1 431 ? -40.590 -0.805  16.347  1.00 93.61  ? 404 VAL B O   1 
ATOM   2610 C  CB  . VAL A 1 431 ? -41.307 -0.835  13.495  1.00 96.93  ? 404 VAL B CB  1 
ATOM   2611 C  CG1 . VAL A 1 431 ? -42.296 -1.907  13.065  1.00 93.93  ? 404 VAL B CG1 1 
ATOM   2612 C  CG2 . VAL A 1 431 ? -40.858 -0.011  12.295  1.00 96.94  ? 404 VAL B CG2 1 
ATOM   2613 N  N   . GLU A 1 432 ? -42.832 -0.929  16.620  1.00 87.84  ? 405 GLU B N   1 
ATOM   2614 C  CA  . GLU A 1 432 ? -42.809 -1.691  17.882  1.00 84.95  ? 405 GLU B CA  1 
ATOM   2615 C  C   . GLU A 1 432 ? -42.519 -3.168  17.603  1.00 82.97  ? 405 GLU B C   1 
ATOM   2616 O  O   . GLU A 1 432 ? -43.381 -3.871  17.072  1.00 90.15  ? 405 GLU B O   1 
ATOM   2617 C  CB  . GLU A 1 432 ? -44.158 -1.589  18.627  1.00 80.71  ? 405 GLU B CB  1 
ATOM   2618 N  N   . THR A 1 433 ? -41.303 -3.615  17.939  1.00 82.91  ? 406 THR B N   1 
ATOM   2619 C  CA  . THR A 1 433 ? -40.917 -5.046  17.963  1.00 72.07  ? 406 THR B CA  1 
ATOM   2620 C  C   . THR A 1 433 ? -40.268 -5.358  19.284  1.00 67.31  ? 406 THR B C   1 
ATOM   2621 O  O   . THR A 1 433 ? -39.731 -4.472  19.921  1.00 73.43  ? 406 THR B O   1 
ATOM   2622 C  CB  . THR A 1 433 ? -39.876 -5.415  16.888  1.00 72.17  ? 406 THR B CB  1 
ATOM   2623 O  OG1 . THR A 1 433 ? -38.637 -4.721  17.130  1.00 62.62  ? 406 THR B OG1 1 
ATOM   2624 C  CG2 . THR A 1 433 ? -40.412 -5.096  15.488  1.00 72.11  ? 406 THR B CG2 1 
ATOM   2625 N  N   . PRO A 1 434 ? -40.270 -6.629  19.688  1.00 68.18  ? 407 PRO B N   1 
ATOM   2626 C  CA  . PRO A 1 434 ? -39.596 -7.008  20.946  1.00 64.57  ? 407 PRO B CA  1 
ATOM   2627 C  C   . PRO A 1 434 ? -38.130 -6.580  21.095  1.00 61.48  ? 407 PRO B C   1 
ATOM   2628 O  O   . PRO A 1 434 ? -37.638 -6.471  22.209  1.00 69.53  ? 407 PRO B O   1 
ATOM   2629 C  CB  . PRO A 1 434 ? -39.715 -8.533  20.943  1.00 68.31  ? 407 PRO B CB  1 
ATOM   2630 C  CG  . PRO A 1 434 ? -41.021 -8.785  20.212  1.00 67.55  ? 407 PRO B CG  1 
ATOM   2631 C  CD  . PRO A 1 434 ? -41.093 -7.730  19.143  1.00 65.19  ? 407 PRO B CD  1 
ATOM   2632 N  N   . TYR A 1 435 ? -37.442 -6.316  19.994  1.00 57.84  ? 408 TYR B N   1 
ATOM   2633 C  CA  . TYR A 1 435 ? -36.077 -5.822  20.038  1.00 53.04  ? 408 TYR B CA  1 
ATOM   2634 C  C   . TYR A 1 435 ? -35.878 -4.712  21.042  1.00 57.47  ? 408 TYR B C   1 
ATOM   2635 O  O   . TYR A 1 435 ? -34.966 -4.757  21.855  1.00 65.69  ? 408 TYR B O   1 
ATOM   2636 C  CB  . TYR A 1 435 ? -35.715 -5.284  18.692  1.00 49.35  ? 408 TYR B CB  1 
ATOM   2637 C  CG  . TYR A 1 435 ? -34.302 -4.853  18.573  1.00 56.75  ? 408 TYR B CG  1 
ATOM   2638 C  CD1 . TYR A 1 435 ? -33.288 -5.774  18.642  1.00 59.01  ? 408 TYR B CD1 1 
ATOM   2639 C  CD2 . TYR A 1 435 ? -33.967 -3.531  18.319  1.00 60.96  ? 408 TYR B CD2 1 
ATOM   2640 C  CE1 . TYR A 1 435 ? -31.977 -5.397  18.490  1.00 58.49  ? 408 TYR B CE1 1 
ATOM   2641 C  CE2 . TYR A 1 435 ? -32.640 -3.145  18.165  1.00 59.42  ? 408 TYR B CE2 1 
ATOM   2642 C  CZ  . TYR A 1 435 ? -31.649 -4.091  18.256  1.00 54.58  ? 408 TYR B CZ  1 
ATOM   2643 O  OH  . TYR A 1 435 ? -30.308 -3.792  18.120  1.00 53.04  ? 408 TYR B OH  1 
ATOM   2644 N  N   . ILE A 1 436 ? -36.736 -3.704  20.974  1.00 63.04  ? 409 ILE B N   1 
ATOM   2645 C  CA  . ILE A 1 436 ? -36.632 -2.555  21.856  1.00 60.27  ? 409 ILE B CA  1 
ATOM   2646 C  C   . ILE A 1 436 ? -37.842 -2.383  22.781  1.00 59.68  ? 409 ILE B C   1 
ATOM   2647 O  O   . ILE A 1 436 ? -37.705 -1.800  23.830  1.00 59.99  ? 409 ILE B O   1 
ATOM   2648 C  CB  . ILE A 1 436 ? -36.350 -1.290  21.025  1.00 69.07  ? 409 ILE B CB  1 
ATOM   2649 C  CG1 . ILE A 1 436 ? -35.138 -0.576  21.578  1.00 69.88  ? 409 ILE B CG1 1 
ATOM   2650 C  CG2 . ILE A 1 436 ? -37.558 -0.360  20.918  1.00 80.41  ? 409 ILE B CG2 1 
ATOM   2651 C  CD1 . ILE A 1 436 ? -33.842 -1.247  21.185  1.00 68.24  ? 409 ILE B CD1 1 
ATOM   2652 N  N   . ASP A 1 437 ? -39.010 -2.909  22.420  1.00 67.75  ? 410 ASP B N   1 
ATOM   2653 C  CA  . ASP A 1 437 ? -40.229 -2.731  23.220  1.00 76.88  ? 410 ASP B CA  1 
ATOM   2654 C  C   . ASP A 1 437 ? -40.141 -3.720  24.381  1.00 74.94  ? 410 ASP B C   1 
ATOM   2655 O  O   . ASP A 1 437 ? -40.817 -4.746  24.393  1.00 73.94  ? 410 ASP B O   1 
ATOM   2656 C  CB  . ASP A 1 437 ? -41.504 -2.916  22.346  1.00 82.88  ? 410 ASP B CB  1 
ATOM   2657 C  CG  . ASP A 1 437 ? -42.828 -2.678  23.110  1.00 93.55  ? 410 ASP B CG  1 
ATOM   2658 O  OD1 . ASP A 1 437 ? -42.807 -2.272  24.292  1.00 101.12 ? 410 ASP B OD1 1 
ATOM   2659 O  OD2 . ASP A 1 437 ? -43.915 -2.903  22.516  1.00 107.02 ? 410 ASP B OD2 1 
ATOM   2660 N  N   . TYR A 1 438 ? -39.275 -3.392  25.342  1.00 71.67  ? 411 TYR B N   1 
ATOM   2661 C  CA  . TYR A 1 438 ? -39.118 -4.160  26.583  1.00 68.46  ? 411 TYR B CA  1 
ATOM   2662 C  C   . TYR A 1 438 ? -38.907 -3.188  27.717  1.00 65.56  ? 411 TYR B C   1 
ATOM   2663 O  O   . TYR A 1 438 ? -38.363 -2.115  27.524  1.00 68.61  ? 411 TYR B O   1 
ATOM   2664 C  CB  . TYR A 1 438 ? -37.890 -5.082  26.526  1.00 64.10  ? 411 TYR B CB  1 
ATOM   2665 C  CG  . TYR A 1 438 ? -36.571 -4.331  26.480  1.00 54.35  ? 411 TYR B CG  1 
ATOM   2666 C  CD1 . TYR A 1 438 ? -35.957 -3.898  27.641  1.00 52.25  ? 411 TYR B CD1 1 
ATOM   2667 C  CD2 . TYR A 1 438 ? -35.943 -4.068  25.282  1.00 49.28  ? 411 TYR B CD2 1 
ATOM   2668 C  CE1 . TYR A 1 438 ? -34.764 -3.211  27.611  1.00 46.85  ? 411 TYR B CE1 1 
ATOM   2669 C  CE2 . TYR A 1 438 ? -34.745 -3.393  25.247  1.00 48.93  ? 411 TYR B CE2 1 
ATOM   2670 C  CZ  . TYR A 1 438 ? -34.178 -2.954  26.417  1.00 47.74  ? 411 TYR B CZ  1 
ATOM   2671 O  OH  . TYR A 1 438 ? -32.998 -2.273  26.383  1.00 53.58  ? 411 TYR B OH  1 
ATOM   2672 N  N   . THR A 1 439 ? -39.258 -3.599  28.919  1.00 69.31  ? 412 THR B N   1 
ATOM   2673 C  CA  . THR A 1 439 ? -38.988 -2.774  30.069  1.00 73.85  ? 412 THR B CA  1 
ATOM   2674 C  C   . THR A 1 439 ? -37.805 -3.351  30.865  1.00 67.54  ? 412 THR B C   1 
ATOM   2675 O  O   . THR A 1 439 ? -36.798 -2.671  31.002  1.00 70.48  ? 412 THR B O   1 
ATOM   2676 C  CB  . THR A 1 439 ? -40.253 -2.483  30.910  1.00 84.87  ? 412 THR B CB  1 
ATOM   2677 O  OG1 . THR A 1 439 ? -39.880 -2.331  32.284  1.00 90.81  ? 412 THR B OG1 1 
ATOM   2678 C  CG2 . THR A 1 439 ? -41.325 -3.595  30.762  1.00 91.18  ? 412 THR B CG2 1 
ATOM   2679 N  N   . HIS A 1 440 ? -37.890 -4.601  31.322  1.00 64.48  ? 413 HIS B N   1 
ATOM   2680 C  CA  . HIS A 1 440 ? -36.778 -5.272  32.058  1.00 61.18  ? 413 HIS B CA  1 
ATOM   2681 C  C   . HIS A 1 440 ? -35.936 -6.233  31.211  1.00 56.26  ? 413 HIS B C   1 
ATOM   2682 O  O   . HIS A 1 440 ? -36.466 -7.015  30.433  1.00 59.24  ? 413 HIS B O   1 
ATOM   2683 C  CB  . HIS A 1 440 ? -37.322 -6.090  33.211  1.00 65.64  ? 413 HIS B CB  1 
ATOM   2684 C  CG  . HIS A 1 440 ? -38.306 -5.358  34.060  1.00 74.07  ? 413 HIS B CG  1 
ATOM   2685 N  ND1 . HIS A 1 440 ? -37.953 -4.726  35.233  1.00 81.46  ? 413 HIS B ND1 1 
ATOM   2686 C  CD2 . HIS A 1 440 ? -39.638 -5.166  33.914  1.00 77.37  ? 413 HIS B CD2 1 
ATOM   2687 C  CE1 . HIS A 1 440 ? -39.024 -4.169  35.768  1.00 83.22  ? 413 HIS B CE1 1 
ATOM   2688 N  NE2 . HIS A 1 440 ? -40.059 -4.424  34.990  1.00 81.16  ? 413 HIS B NE2 1 
ATOM   2689 N  N   . LEU A 1 441 ? -34.622 -6.168  31.392  1.00 58.36  ? 414 LEU B N   1 
ATOM   2690 C  CA  . LEU A 1 441 ? -33.665 -7.068  30.766  1.00 53.66  ? 414 LEU B CA  1 
ATOM   2691 C  C   . LEU A 1 441 ? -33.451 -8.222  31.699  1.00 52.32  ? 414 LEU B C   1 
ATOM   2692 O  O   . LEU A 1 441 ? -32.980 -8.027  32.793  1.00 58.76  ? 414 LEU B O   1 
ATOM   2693 C  CB  . LEU A 1 441 ? -32.331 -6.386  30.588  1.00 52.20  ? 414 LEU B CB  1 
ATOM   2694 C  CG  . LEU A 1 441 ? -32.245 -5.289  29.549  1.00 55.22  ? 414 LEU B CG  1 
ATOM   2695 C  CD1 . LEU A 1 441 ? -30.822 -4.769  29.515  1.00 58.84  ? 414 LEU B CD1 1 
ATOM   2696 C  CD2 . LEU A 1 441 ? -32.613 -5.776  28.155  1.00 57.72  ? 414 LEU B CD2 1 
ATOM   2697 N  N   . ARG A 1 442 ? -33.803 -9.422  31.262  1.00 52.78  ? 415 ARG B N   1 
ATOM   2698 C  CA  . ARG A 1 442 ? -33.693 -10.605 32.087  1.00 49.36  ? 415 ARG B CA  1 
ATOM   2699 C  C   . ARG A 1 442 ? -32.726 -11.603 31.461  1.00 46.45  ? 415 ARG B C   1 
ATOM   2700 O  O   . ARG A 1 442 ? -31.579 -11.648 31.888  1.00 50.88  ? 415 ARG B O   1 
ATOM   2701 C  CB  . ARG A 1 442 ? -35.076 -11.170 32.376  1.00 49.20  ? 415 ARG B CB  1 
ATOM   2702 C  CG  . ARG A 1 442 ? -36.057 -10.120 32.887  1.00 48.31  ? 415 ARG B CG  1 
ATOM   2703 C  CD  . ARG A 1 442 ? -37.296 -10.785 33.475  1.00 53.02  ? 415 ARG B CD  1 
ATOM   2704 N  NE  . ARG A 1 442 ? -38.463 -9.903  33.616  1.00 59.14  ? 415 ARG B NE  1 
ATOM   2705 C  CZ  . ARG A 1 442 ? -38.908 -9.347  34.755  1.00 63.60  ? 415 ARG B CZ  1 
ATOM   2706 N  NH1 . ARG A 1 442 ? -38.292 -9.517  35.924  1.00 59.47  ? 415 ARG B NH1 1 
ATOM   2707 N  NH2 . ARG A 1 442 ? -39.998 -8.584  34.719  1.00 71.93  ? 415 ARG B NH2 1 
ATOM   2708 N  N   . ILE A 1 443 ? -33.136 -12.367 30.450  1.00 45.57  ? 416 ILE B N   1 
ATOM   2709 C  CA  . ILE A 1 443 ? -32.191 -13.235 29.692  1.00 42.02  ? 416 ILE B CA  1 
ATOM   2710 C  C   . ILE A 1 443 ? -31.011 -12.434 29.138  1.00 42.13  ? 416 ILE B C   1 
ATOM   2711 O  O   . ILE A 1 443 ? -29.876 -12.869 29.199  1.00 48.49  ? 416 ILE B O   1 
ATOM   2712 C  CB  . ILE A 1 443 ? -32.858 -13.946 28.514  1.00 41.15  ? 416 ILE B CB  1 
ATOM   2713 C  CG1 . ILE A 1 443 ? -34.054 -14.836 28.951  1.00 46.19  ? 416 ILE B CG1 1 
ATOM   2714 C  CG2 . ILE A 1 443 ? -31.854 -14.766 27.762  1.00 39.73  ? 416 ILE B CG2 1 
ATOM   2715 C  CD1 . ILE A 1 443 ? -33.784 -15.858 30.021  1.00 46.41  ? 416 ILE B CD1 1 
ATOM   2716 N  N   . SER A 1 444 ? -31.254 -11.242 28.630  1.00 44.37  ? 417 SER B N   1 
ATOM   2717 C  CA  . SER A 1 444 ? -30.158 -10.391 28.128  1.00 45.15  ? 417 SER B CA  1 
ATOM   2718 C  C   . SER A 1 444 ? -29.090 -10.174 29.211  1.00 44.45  ? 417 SER B C   1 
ATOM   2719 O  O   . SER A 1 444 ? -27.887 -10.163 28.968  1.00 41.65  ? 417 SER B O   1 
ATOM   2720 C  CB  . SER A 1 444 ? -30.731 -9.059  27.645  1.00 48.05  ? 417 SER B CB  1 
ATOM   2721 O  OG  . SER A 1 444 ? -31.812 -9.264  26.706  1.00 49.37  ? 417 SER B OG  1 
ATOM   2722 N  N   . TYR A 1 445 ? -29.538 -10.019 30.433  1.00 46.56  ? 418 TYR B N   1 
ATOM   2723 C  CA  . TYR A 1 445 ? -28.612 -9.832  31.497  1.00 46.04  ? 418 TYR B CA  1 
ATOM   2724 C  C   . TYR A 1 445 ? -27.775 -11.095 31.645  1.00 48.32  ? 418 TYR B C   1 
ATOM   2725 O  O   . TYR A 1 445 ? -26.557 -11.010 31.756  1.00 49.93  ? 418 TYR B O   1 
ATOM   2726 C  CB  . TYR A 1 445 ? -29.331 -9.459  32.791  1.00 46.27  ? 418 TYR B CB  1 
ATOM   2727 C  CG  . TYR A 1 445 ? -28.344 -9.087  33.862  1.00 52.65  ? 418 TYR B CG  1 
ATOM   2728 C  CD1 . TYR A 1 445 ? -27.532 -7.937  33.730  1.00 52.09  ? 418 TYR B CD1 1 
ATOM   2729 C  CD2 . TYR A 1 445 ? -28.169 -9.897  34.973  1.00 54.29  ? 418 TYR B CD2 1 
ATOM   2730 C  CE1 . TYR A 1 445 ? -26.591 -7.615  34.678  1.00 53.90  ? 418 TYR B CE1 1 
ATOM   2731 C  CE2 . TYR A 1 445 ? -27.223 -9.586  35.944  1.00 59.83  ? 418 TYR B CE2 1 
ATOM   2732 C  CZ  . TYR A 1 445 ? -26.436 -8.450  35.799  1.00 62.99  ? 418 TYR B CZ  1 
ATOM   2733 O  OH  . TYR A 1 445 ? -25.508 -8.161  36.778  1.00 60.40  ? 418 TYR B OH  1 
ATOM   2734 N  N   . ASN A 1 446 ? -28.408 -12.266 31.612  1.00 44.98  ? 419 ASN B N   1 
ATOM   2735 C  CA  . ASN A 1 446 ? -27.651 -13.523 31.649  1.00 44.33  ? 419 ASN B CA  1 
ATOM   2736 C  C   . ASN A 1 446 ? -26.609 -13.712 30.544  1.00 41.31  ? 419 ASN B C   1 
ATOM   2737 O  O   . ASN A 1 446 ? -25.552 -14.327 30.737  1.00 39.68  ? 419 ASN B O   1 
ATOM   2738 C  CB  . ASN A 1 446 ? -28.579 -14.698 31.551  1.00 47.20  ? 419 ASN B CB  1 
ATOM   2739 C  CG  . ASN A 1 446 ? -29.499 -14.796 32.703  1.00 46.83  ? 419 ASN B CG  1 
ATOM   2740 O  OD1 . ASN A 1 446 ? -29.415 -14.031 33.654  1.00 52.42  ? 419 ASN B OD1 1 
ATOM   2741 N  ND2 . ASN A 1 446 ? -30.402 -15.750 32.623  1.00 52.70  ? 419 ASN B ND2 1 
ATOM   2742 N  N   . VAL A 1 447 ? -26.928 -13.204 29.378  1.00 39.43  ? 420 VAL B N   1 
ATOM   2743 C  CA  . VAL A 1 447 ? -25.983 -13.227 28.286  1.00 41.80  ? 420 VAL B CA  1 
ATOM   2744 C  C   . VAL A 1 447 ? -24.771 -12.404 28.664  1.00 43.15  ? 420 VAL B C   1 
ATOM   2745 O  O   . VAL A 1 447 ? -23.637 -12.800 28.454  1.00 41.63  ? 420 VAL B O   1 
ATOM   2746 C  CB  . VAL A 1 447 ? -26.612 -12.622 27.022  1.00 40.91  ? 420 VAL B CB  1 
ATOM   2747 C  CG1 . VAL A 1 447 ? -25.664 -12.745 25.827  1.00 41.50  ? 420 VAL B CG1 1 
ATOM   2748 C  CG2 . VAL A 1 447 ? -27.928 -13.330 26.737  1.00 43.67  ? 420 VAL B CG2 1 
ATOM   2749 N  N   . TYR A 1 448 ? -25.050 -11.233 29.207  1.00 48.60  ? 421 TYR B N   1 
ATOM   2750 C  CA  . TYR A 1 448 ? -24.045 -10.282 29.580  1.00 48.33  ? 421 TYR B CA  1 
ATOM   2751 C  C   . TYR A 1 448 ? -23.176 -10.878 30.669  1.00 50.80  ? 421 TYR B C   1 
ATOM   2752 O  O   . TYR A 1 448 ? -21.944 -10.818 30.558  1.00 53.20  ? 421 TYR B O   1 
ATOM   2753 C  CB  . TYR A 1 448 ? -24.757 -9.065  30.060  1.00 50.34  ? 421 TYR B CB  1 
ATOM   2754 C  CG  . TYR A 1 448 ? -23.921 -7.951  30.522  1.00 57.30  ? 421 TYR B CG  1 
ATOM   2755 C  CD1 . TYR A 1 448 ? -23.281 -7.122  29.604  1.00 60.30  ? 421 TYR B CD1 1 
ATOM   2756 C  CD2 . TYR A 1 448 ? -23.825 -7.653  31.886  1.00 60.85  ? 421 TYR B CD2 1 
ATOM   2757 C  CE1 . TYR A 1 448 ? -22.545 -6.034  30.033  1.00 64.36  ? 421 TYR B CE1 1 
ATOM   2758 C  CE2 . TYR A 1 448 ? -23.093 -6.563  32.327  1.00 64.25  ? 421 TYR B CE2 1 
ATOM   2759 C  CZ  . TYR A 1 448 ? -22.454 -5.759  31.394  1.00 65.14  ? 421 TYR B CZ  1 
ATOM   2760 O  OH  . TYR A 1 448 ? -21.716 -4.693  31.815  1.00 66.79  ? 421 TYR B OH  1 
ATOM   2761 N  N   . LEU A 1 449 ? -23.789 -11.513 31.674  1.00 45.53  ? 422 LEU B N   1 
ATOM   2762 C  CA  . LEU A 1 449 ? -22.996 -12.197 32.720  1.00 46.35  ? 422 LEU B CA  1 
ATOM   2763 C  C   . LEU A 1 449 ? -22.275 -13.415 32.230  1.00 45.56  ? 422 LEU B C   1 
ATOM   2764 O  O   . LEU A 1 449 ? -21.264 -13.819 32.808  1.00 47.63  ? 422 LEU B O   1 
ATOM   2765 C  CB  . LEU A 1 449 ? -23.828 -12.664 33.903  1.00 48.46  ? 422 LEU B CB  1 
ATOM   2766 C  CG  . LEU A 1 449 ? -24.456 -11.673 34.863  1.00 50.39  ? 422 LEU B CG  1 
ATOM   2767 C  CD1 . LEU A 1 449 ? -24.997 -12.493 36.012  1.00 52.95  ? 422 LEU B CD1 1 
ATOM   2768 C  CD2 . LEU A 1 449 ? -23.440 -10.688 35.380  1.00 55.26  ? 422 LEU B CD2 1 
ATOM   2769 N  N   . ALA A 1 450 ? -22.798 -14.062 31.215  1.00 45.12  ? 423 ALA B N   1 
ATOM   2770 C  CA  . ALA A 1 450 ? -22.114 -15.247 30.768  1.00 48.93  ? 423 ALA B CA  1 
ATOM   2771 C  C   . ALA A 1 450 ? -20.780 -14.811 30.167  1.00 47.59  ? 423 ALA B C   1 
ATOM   2772 O  O   . ALA A 1 450 ? -19.763 -15.474 30.354  1.00 48.31  ? 423 ALA B O   1 
ATOM   2773 C  CB  . ALA A 1 450 ? -22.965 -16.038 29.771  1.00 46.80  ? 423 ALA B CB  1 
ATOM   2774 N  N   . VAL A 1 451 ? -20.802 -13.707 29.439  1.00 46.09  ? 424 VAL B N   1 
ATOM   2775 C  CA  . VAL A 1 451 ? -19.604 -13.190 28.766  1.00 54.07  ? 424 VAL B CA  1 
ATOM   2776 C  C   . VAL A 1 451 ? -18.570 -12.630 29.758  1.00 52.11  ? 424 VAL B C   1 
ATOM   2777 O  O   . VAL A 1 451 ? -17.369 -12.786 29.572  1.00 53.34  ? 424 VAL B O   1 
ATOM   2778 C  CB  . VAL A 1 451 ? -19.969 -12.054 27.769  1.00 56.56  ? 424 VAL B CB  1 
ATOM   2779 C  CG1 . VAL A 1 451 ? -18.733 -11.288 27.324  1.00 56.07  ? 424 VAL B CG1 1 
ATOM   2780 C  CG2 . VAL A 1 451 ? -20.722 -12.607 26.560  1.00 56.81  ? 424 VAL B CG2 1 
ATOM   2781 N  N   . TYR A 1 452 ? -19.058 -11.938 30.774  1.00 50.96  ? 425 TYR B N   1 
ATOM   2782 C  CA  . TYR A 1 452 ? -18.218 -11.376 31.806  1.00 53.16  ? 425 TYR B CA  1 
ATOM   2783 C  C   . TYR A 1 452 ? -17.539 -12.493 32.645  1.00 53.30  ? 425 TYR B C   1 
ATOM   2784 O  O   . TYR A 1 452 ? -16.402 -12.357 33.059  1.00 58.82  ? 425 TYR B O   1 
ATOM   2785 C  CB  . TYR A 1 452 ? -19.040 -10.373 32.653  1.00 51.88  ? 425 TYR B CB  1 
ATOM   2786 C  CG  . TYR A 1 452 ? -18.788 -8.956  32.173  1.00 56.18  ? 425 TYR B CG  1 
ATOM   2787 C  CD1 . TYR A 1 452 ? -17.688 -8.237  32.622  1.00 55.14  ? 425 TYR B CD1 1 
ATOM   2788 C  CD2 . TYR A 1 452 ? -19.601 -8.358  31.237  1.00 57.59  ? 425 TYR B CD2 1 
ATOM   2789 C  CE1 . TYR A 1 452 ? -17.429 -6.968  32.178  1.00 53.20  ? 425 TYR B CE1 1 
ATOM   2790 C  CE2 . TYR A 1 452 ? -19.357 -7.077  30.802  1.00 57.19  ? 425 TYR B CE2 1 
ATOM   2791 C  CZ  . TYR A 1 452 ? -18.257 -6.393  31.265  1.00 56.81  ? 425 TYR B CZ  1 
ATOM   2792 O  OH  . TYR A 1 452 ? -17.983 -5.126  30.799  1.00 56.60  ? 425 TYR B OH  1 
ATOM   2793 N  N   . SER A 1 453 ? -18.220 -13.613 32.832  1.00 49.20  ? 426 SER B N   1 
ATOM   2794 C  CA  . SER A 1 453 ? -17.641 -14.783 33.483  1.00 47.14  ? 426 SER B CA  1 
ATOM   2795 C  C   . SER A 1 453 ? -16.445 -15.260 32.706  1.00 46.69  ? 426 SER B C   1 
ATOM   2796 O  O   . SER A 1 453 ? -15.372 -15.464 33.249  1.00 53.48  ? 426 SER B O   1 
ATOM   2797 C  CB  . SER A 1 453 ? -18.673 -15.917 33.584  1.00 44.91  ? 426 SER B CB  1 
ATOM   2798 O  OG  . SER A 1 453 ? -19.850 -15.421 34.236  1.00 49.71  ? 426 SER B OG  1 
ATOM   2799 N  N   . ILE A 1 454 ? -16.610 -15.439 31.421  1.00 46.74  ? 427 ILE B N   1 
ATOM   2800 C  CA  . ILE A 1 454 ? -15.522 -15.962 30.643  1.00 47.95  ? 427 ILE B CA  1 
ATOM   2801 C  C   . ILE A 1 454 ? -14.412 -14.958 30.705  1.00 51.66  ? 427 ILE B C   1 
ATOM   2802 O  O   . ILE A 1 454 ? -13.243 -15.355 30.689  1.00 49.54  ? 427 ILE B O   1 
ATOM   2803 C  CB  . ILE A 1 454 ? -15.921 -16.176 29.194  1.00 46.02  ? 427 ILE B CB  1 
ATOM   2804 C  CG1 . ILE A 1 454 ? -16.780 -17.419 29.127  1.00 49.41  ? 427 ILE B CG1 1 
ATOM   2805 C  CG2 . ILE A 1 454 ? -14.700 -16.388 28.319  1.00 46.32  ? 427 ILE B CG2 1 
ATOM   2806 C  CD1 . ILE A 1 454 ? -17.752 -17.415 27.975  1.00 50.58  ? 427 ILE B CD1 1 
ATOM   2807 N  N   . ALA A 1 455 ? -14.773 -13.671 30.764  1.00 49.90  ? 428 ALA B N   1 
ATOM   2808 C  CA  . ALA A 1 455 ? -13.781 -12.602 30.637  1.00 53.70  ? 428 ALA B CA  1 
ATOM   2809 C  C   . ALA A 1 455 ? -12.951 -12.552 31.901  1.00 54.04  ? 428 ALA B C   1 
ATOM   2810 O  O   . ALA A 1 455 ? -11.725 -12.697 31.854  1.00 50.44  ? 428 ALA B O   1 
ATOM   2811 C  CB  . ALA A 1 455 ? -14.445 -11.261 30.376  1.00 54.84  ? 428 ALA B CB  1 
ATOM   2812 N  N   . HIS A 1 456 ? -13.650 -12.409 33.024  1.00 54.85  ? 429 HIS B N   1 
ATOM   2813 C  CA  . HIS A 1 456 ? -13.060 -12.515 34.357  1.00 54.04  ? 429 HIS B CA  1 
ATOM   2814 C  C   . HIS A 1 456 ? -12.178 -13.768 34.632  1.00 53.50  ? 429 HIS B C   1 
ATOM   2815 O  O   . HIS A 1 456 ? -11.188 -13.671 35.332  1.00 58.14  ? 429 HIS B O   1 
ATOM   2816 C  CB  . HIS A 1 456 ? -14.155 -12.383 35.401  1.00 50.34  ? 429 HIS B CB  1 
ATOM   2817 C  CG  . HIS A 1 456 ? -14.609 -10.972 35.599  1.00 58.42  ? 429 HIS B CG  1 
ATOM   2818 N  ND1 . HIS A 1 456 ? -13.772 -9.988  36.066  1.00 63.53  ? 429 HIS B ND1 1 
ATOM   2819 C  CD2 . HIS A 1 456 ? -15.808 -10.376 35.399  1.00 68.63  ? 429 HIS B CD2 1 
ATOM   2820 C  CE1 . HIS A 1 456 ? -14.432 -8.847  36.149  1.00 65.81  ? 429 HIS B CE1 1 
ATOM   2821 N  NE2 . HIS A 1 456 ? -15.670 -9.054  35.747  1.00 68.75  ? 429 HIS B NE2 1 
ATOM   2822 N  N   . ALA A 1 457 ? -12.510 -14.920 34.077  1.00 51.38  ? 430 ALA B N   1 
ATOM   2823 C  CA  . ALA A 1 457 ? -11.693 -16.102 34.272  1.00 51.11  ? 430 ALA B CA  1 
ATOM   2824 C  C   . ALA A 1 457 ? -10.449 -15.999 33.449  1.00 55.70  ? 430 ALA B C   1 
ATOM   2825 O  O   . ALA A 1 457 ? -9.442  -16.585 33.790  1.00 64.20  ? 430 ALA B O   1 
ATOM   2826 C  CB  . ALA A 1 457 ? -12.455 -17.345 33.876  1.00 53.25  ? 430 ALA B CB  1 
ATOM   2827 N  N   . LEU A 1 458 ? -10.526 -15.274 32.339  1.00 62.65  ? 431 LEU B N   1 
ATOM   2828 C  CA  . LEU A 1 458 ? -9.329  -14.941 31.548  1.00 61.97  ? 431 LEU B CA  1 
ATOM   2829 C  C   . LEU A 1 458 ? -8.508  -13.887 32.275  1.00 58.29  ? 431 LEU B C   1 
ATOM   2830 O  O   . LEU A 1 458 ? -7.288  -13.924 32.231  1.00 61.47  ? 431 LEU B O   1 
ATOM   2831 C  CB  . LEU A 1 458 ? -9.676  -14.434 30.136  1.00 56.10  ? 431 LEU B CB  1 
ATOM   2832 C  CG  . LEU A 1 458 ? -10.302 -15.459 29.208  1.00 54.01  ? 431 LEU B CG  1 
ATOM   2833 C  CD1 . LEU A 1 458 ? -10.975 -14.759 28.061  1.00 58.40  ? 431 LEU B CD1 1 
ATOM   2834 C  CD2 . LEU A 1 458 ? -9.301  -16.452 28.688  1.00 54.00  ? 431 LEU B CD2 1 
ATOM   2835 N  N   . GLN A 1 459 ? -9.175  -12.952 32.929  1.00 54.04  ? 432 GLN B N   1 
ATOM   2836 C  CA  . GLN A 1 459 ? -8.477  -11.962 33.716  1.00 63.77  ? 432 GLN B CA  1 
ATOM   2837 C  C   . GLN A 1 459 ? -7.751  -12.605 34.888  1.00 69.30  ? 432 GLN B C   1 
ATOM   2838 O  O   . GLN A 1 459 ? -6.723  -12.077 35.330  1.00 69.78  ? 432 GLN B O   1 
ATOM   2839 C  CB  . GLN A 1 459 ? -9.432  -10.897 34.233  1.00 67.45  ? 432 GLN B CB  1 
ATOM   2840 C  CG  . GLN A 1 459 ? -8.784  -9.800  35.067  1.00 75.58  ? 432 GLN B CG  1 
ATOM   2841 C  CD  . GLN A 1 459 ? -7.818  -8.919  34.292  1.00 84.56  ? 432 GLN B CD  1 
ATOM   2842 O  OE1 . GLN A 1 459 ? -7.590  -9.100  33.086  1.00 93.47  ? 432 GLN B OE1 1 
ATOM   2843 N  NE2 . GLN A 1 459 ? -7.241  -7.950  34.989  1.00 87.33  ? 432 GLN B NE2 1 
ATOM   2844 N  N   . ASP A 1 460 ? -8.276  -13.733 35.386  1.00 66.38  ? 433 ASP B N   1 
ATOM   2845 C  CA  . ASP A 1 460 ? -7.655  -14.425 36.520  1.00 61.23  ? 433 ASP B CA  1 
ATOM   2846 C  C   . ASP A 1 460 ? -6.372  -15.103 36.049  1.00 64.30  ? 433 ASP B C   1 
ATOM   2847 O  O   . ASP A 1 460 ? -5.454  -15.300 36.838  1.00 77.64  ? 433 ASP B O   1 
ATOM   2848 C  CB  . ASP A 1 460 ? -8.616  -15.412 37.212  1.00 54.38  ? 433 ASP B CB  1 
ATOM   2849 C  CG  . ASP A 1 460 ? -9.712  -14.700 38.079  1.00 57.30  ? 433 ASP B CG  1 
ATOM   2850 O  OD1 . ASP A 1 460 ? -9.654  -13.475 38.298  1.00 54.01  ? 433 ASP B OD1 1 
ATOM   2851 O  OD2 . ASP A 1 460 ? -10.668 -15.371 38.553  1.00 61.04  ? 433 ASP B OD2 1 
ATOM   2852 N  N   . ILE A 1 461 ? -6.310  -15.425 34.763  1.00 63.23  ? 434 ILE B N   1 
ATOM   2853 C  CA  . ILE A 1 461 ? -5.128  -15.993 34.143  1.00 64.17  ? 434 ILE B CA  1 
ATOM   2854 C  C   . ILE A 1 461 ? -4.120  -14.901 33.751  1.00 71.65  ? 434 ILE B C   1 
ATOM   2855 O  O   . ILE A 1 461 ? -2.914  -15.140 33.778  1.00 75.13  ? 434 ILE B O   1 
ATOM   2856 C  CB  . ILE A 1 461 ? -5.503  -16.786 32.885  1.00 60.74  ? 434 ILE B CB  1 
ATOM   2857 C  CG1 . ILE A 1 461 ? -6.252  -18.052 33.273  1.00 60.25  ? 434 ILE B CG1 1 
ATOM   2858 C  CG2 . ILE A 1 461 ? -4.264  -17.156 32.097  1.00 64.53  ? 434 ILE B CG2 1 
ATOM   2859 C  CD1 . ILE A 1 461 ? -6.768  -18.843 32.086  1.00 59.59  ? 434 ILE B CD1 1 
ATOM   2860 N  N   . TYR A 1 462 ? -4.599  -13.717 33.374  1.00 69.33  ? 435 TYR B N   1 
ATOM   2861 C  CA  . TYR A 1 462 ? -3.702  -12.619 33.053  1.00 69.33  ? 435 TYR B CA  1 
ATOM   2862 C  C   . TYR A 1 462 ? -2.858  -12.234 34.270  1.00 72.90  ? 435 TYR B C   1 
ATOM   2863 O  O   . TYR A 1 462 ? -1.640  -12.126 34.173  1.00 74.65  ? 435 TYR B O   1 
ATOM   2864 C  CB  . TYR A 1 462 ? -4.477  -11.401 32.586  1.00 72.13  ? 435 TYR B CB  1 
ATOM   2865 C  CG  . TYR A 1 462 ? -3.586  -10.223 32.230  1.00 82.79  ? 435 TYR B CG  1 
ATOM   2866 C  CD1 . TYR A 1 462 ? -2.683  -10.306 31.168  1.00 83.92  ? 435 TYR B CD1 1 
ATOM   2867 C  CD2 . TYR A 1 462 ? -3.643  -9.027  32.958  1.00 83.83  ? 435 TYR B CD2 1 
ATOM   2868 C  CE1 . TYR A 1 462 ? -1.864  -9.243  30.843  1.00 84.81  ? 435 TYR B CE1 1 
ATOM   2869 C  CE2 . TYR A 1 462 ? -2.832  -7.956  32.632  1.00 87.58  ? 435 TYR B CE2 1 
ATOM   2870 C  CZ  . TYR A 1 462 ? -1.947  -8.074  31.571  1.00 90.72  ? 435 TYR B CZ  1 
ATOM   2871 O  OH  . TYR A 1 462 ? -1.133  -7.020  31.233  1.00 98.07  ? 435 TYR B OH  1 
ATOM   2872 N  N   . THR A 1 463 ? -3.535  -12.050 35.402  1.00 70.02  ? 436 THR B N   1 
ATOM   2873 C  CA  . THR A 1 463 ? -2.940  -11.683 36.685  1.00 62.45  ? 436 THR B CA  1 
ATOM   2874 C  C   . THR A 1 463 ? -2.427  -12.869 37.560  1.00 69.61  ? 436 THR B C   1 
ATOM   2875 O  O   . THR A 1 463 ? -2.034  -12.645 38.706  1.00 74.51  ? 436 THR B O   1 
ATOM   2876 C  CB  . THR A 1 463 ? -4.002  -10.997 37.569  1.00 58.98  ? 436 THR B CB  1 
ATOM   2877 O  OG1 . THR A 1 463 ? -5.022  -11.954 37.907  1.00 64.10  ? 436 THR B OG1 1 
ATOM   2878 C  CG2 . THR A 1 463 ? -4.643  -9.814  36.893  1.00 54.24  ? 436 THR B CG2 1 
ATOM   2879 N  N   . CYS A 1 464 ? -2.463  -14.111 37.073  1.00 74.02  ? 437 CYS B N   1 
ATOM   2880 C  CA  . CYS A 1 464 ? -1.991  -15.255 37.877  1.00 79.54  ? 437 CYS B CA  1 
ATOM   2881 C  C   . CYS A 1 464 ? -0.525  -15.079 38.270  1.00 82.69  ? 437 CYS B C   1 
ATOM   2882 O  O   . CYS A 1 464 ? 0.329   -14.775 37.422  1.00 75.00  ? 437 CYS B O   1 
ATOM   2883 C  CB  . CYS A 1 464 ? -2.145  -16.580 37.118  1.00 83.76  ? 437 CYS B CB  1 
ATOM   2884 S  SG  . CYS A 1 464 ? -1.598  -18.051 38.028  1.00 96.98  ? 437 CYS B SG  1 
ATOM   2885 N  N   . LEU A 1 465 ? -0.252  -15.287 39.559  1.00 92.27  ? 438 LEU B N   1 
ATOM   2886 C  CA  . LEU A 1 465 ? 1.099   -15.185 40.132  1.00 87.86  ? 438 LEU B CA  1 
ATOM   2887 C  C   . LEU A 1 465 ? 1.715   -16.564 40.326  1.00 73.19  ? 438 LEU B C   1 
ATOM   2888 O  O   . LEU A 1 465 ? 1.169   -17.390 41.068  1.00 63.88  ? 438 LEU B O   1 
ATOM   2889 C  CB  . LEU A 1 465 ? 1.019   -14.474 41.478  1.00 98.60  ? 438 LEU B CB  1 
ATOM   2890 C  CG  . LEU A 1 465 ? 0.623   -13.001 41.365  1.00 108.14 ? 438 LEU B CG  1 
ATOM   2891 C  CD1 . LEU A 1 465 ? 0.227   -12.429 42.727  1.00 111.04 ? 438 LEU B CD1 1 
ATOM   2892 C  CD2 . LEU A 1 465 ? 1.752   -12.196 40.702  1.00 103.34 ? 438 LEU B CD2 1 
ATOM   2893 N  N   . PRO A 1 466 ? 2.870   -16.812 39.693  1.00 77.20  ? 439 PRO B N   1 
ATOM   2894 C  CA  . PRO A 1 466 ? 3.397   -18.188 39.708  1.00 81.02  ? 439 PRO B CA  1 
ATOM   2895 C  C   . PRO A 1 466 ? 3.538   -18.687 41.142  1.00 71.51  ? 439 PRO B C   1 
ATOM   2896 O  O   . PRO A 1 466 ? 3.925   -17.926 42.016  1.00 69.21  ? 439 PRO B O   1 
ATOM   2897 C  CB  . PRO A 1 466 ? 4.770   -18.073 39.012  1.00 82.68  ? 439 PRO B CB  1 
ATOM   2898 C  CG  . PRO A 1 466 ? 4.994   -16.624 38.697  1.00 78.33  ? 439 PRO B CG  1 
ATOM   2899 C  CD  . PRO A 1 466 ? 3.914   -15.819 39.371  1.00 81.22  ? 439 PRO B CD  1 
ATOM   2900 N  N   . GLY A 1 467 ? 3.183   -19.931 41.393  1.00 67.47  ? 440 GLY B N   1 
ATOM   2901 C  CA  . GLY A 1 467 ? 3.096   -20.413 42.778  1.00 76.89  ? 440 GLY B CA  1 
ATOM   2902 C  C   . GLY A 1 467 ? 1.691   -20.395 43.371  1.00 79.16  ? 440 GLY B C   1 
ATOM   2903 O  O   . GLY A 1 467 ? 1.237   -21.408 43.925  1.00 77.02  ? 440 GLY B O   1 
ATOM   2904 N  N   . ARG A 1 468 ? 1.000   -19.259 43.243  1.00 84.46  ? 441 ARG B N   1 
ATOM   2905 C  CA  . ARG A 1 468 ? -0.413  -19.135 43.656  1.00 91.12  ? 441 ARG B CA  1 
ATOM   2906 C  C   . ARG A 1 468 ? -1.403  -19.240 42.441  1.00 86.41  ? 441 ARG B C   1 
ATOM   2907 O  O   . ARG A 1 468 ? -2.373  -18.485 42.340  1.00 74.82  ? 441 ARG B O   1 
ATOM   2908 C  CB  . ARG A 1 468 ? -0.617  -17.841 44.485  1.00 86.15  ? 441 ARG B CB  1 
ATOM   2909 N  N   . GLY A 1 469 ? -1.139  -20.194 41.541  1.00 82.81  ? 442 GLY B N   1 
ATOM   2910 C  CA  . GLY A 1 469 ? -2.017  -20.517 40.408  1.00 77.12  ? 442 GLY B CA  1 
ATOM   2911 C  C   . GLY A 1 469 ? -2.746  -21.842 40.612  1.00 75.01  ? 442 GLY B C   1 
ATOM   2912 O  O   . GLY A 1 469 ? -2.512  -22.540 41.591  1.00 81.77  ? 442 GLY B O   1 
ATOM   2913 N  N   . LEU A 1 470 ? -3.627  -22.203 39.683  1.00 72.80  ? 443 LEU B N   1 
ATOM   2914 C  CA  . LEU A 1 470 ? -4.537  -23.334 39.890  1.00 67.02  ? 443 LEU B CA  1 
ATOM   2915 C  C   . LEU A 1 470 ? -4.089  -24.638 39.243  1.00 66.59  ? 443 LEU B C   1 
ATOM   2916 O  O   . LEU A 1 470 ? -4.772  -25.648 39.395  1.00 67.43  ? 443 LEU B O   1 
ATOM   2917 C  CB  . LEU A 1 470 ? -5.947  -23.005 39.376  1.00 67.38  ? 443 LEU B CB  1 
ATOM   2918 C  CG  . LEU A 1 470 ? -6.747  -21.887 40.044  1.00 64.18  ? 443 LEU B CG  1 
ATOM   2919 C  CD1 . LEU A 1 470 ? -7.979  -21.625 39.216  1.00 66.58  ? 443 LEU B CD1 1 
ATOM   2920 C  CD2 . LEU A 1 470 ? -7.152  -22.226 41.446  1.00 62.72  ? 443 LEU B CD2 1 
ATOM   2921 N  N   . PHE A 1 471 ? -2.961  -24.643 38.534  1.00 66.78  ? 444 PHE B N   1 
ATOM   2922 C  CA  . PHE A 1 471 ? -2.494  -25.870 37.871  1.00 66.56  ? 444 PHE B CA  1 
ATOM   2923 C  C   . PHE A 1 471 ? -1.368  -26.540 38.685  1.00 73.26  ? 444 PHE B C   1 
ATOM   2924 O  O   . PHE A 1 471 ? -1.082  -26.086 39.792  1.00 90.95  ? 444 PHE B O   1 
ATOM   2925 C  CB  . PHE A 1 471 ? -2.148  -25.523 36.429  1.00 67.21  ? 444 PHE B CB  1 
ATOM   2926 C  CG  . PHE A 1 471 ? -3.272  -24.804 35.725  1.00 64.60  ? 444 PHE B CG  1 
ATOM   2927 C  CD1 . PHE A 1 471 ? -4.325  -25.515 35.166  1.00 66.94  ? 444 PHE B CD1 1 
ATOM   2928 C  CD2 . PHE A 1 471 ? -3.318  -23.418 35.693  1.00 65.29  ? 444 PHE B CD2 1 
ATOM   2929 C  CE1 . PHE A 1 471 ? -5.390  -24.860 34.567  1.00 71.79  ? 444 PHE B CE1 1 
ATOM   2930 C  CE2 . PHE A 1 471 ? -4.375  -22.749 35.085  1.00 71.05  ? 444 PHE B CE2 1 
ATOM   2931 C  CZ  . PHE A 1 471 ? -5.419  -23.469 34.527  1.00 70.57  ? 444 PHE B CZ  1 
ATOM   2932 N  N   . THR A 1 472 ? -0.767  -27.629 38.202  1.00 70.95  ? 445 THR B N   1 
ATOM   2933 C  CA  . THR A 1 472 ? 0.189   -28.395 39.023  1.00 72.71  ? 445 THR B CA  1 
ATOM   2934 C  C   . THR A 1 472 ? 1.300   -27.503 39.610  1.00 80.13  ? 445 THR B C   1 
ATOM   2935 O  O   . THR A 1 472 ? 1.734   -26.532 38.952  1.00 70.47  ? 445 THR B O   1 
ATOM   2936 C  CB  . THR A 1 472 ? 0.865   -29.515 38.220  1.00 77.92  ? 445 THR B CB  1 
ATOM   2937 O  OG1 . THR A 1 472 ? 1.282   -28.993 36.961  1.00 82.02  ? 445 THR B OG1 1 
ATOM   2938 C  CG2 . THR A 1 472 ? -0.082  -30.687 37.979  1.00 83.73  ? 445 THR B CG2 1 
ATOM   2939 N  N   . ASN A 1 473 ? 1.731   -27.841 40.842  1.00 80.85  ? 446 ASN B N   1 
ATOM   2940 C  CA  . ASN A 1 473 ? 2.800   -27.135 41.595  1.00 80.30  ? 446 ASN B CA  1 
ATOM   2941 C  C   . ASN A 1 473 ? 2.578   -25.610 41.646  1.00 83.03  ? 446 ASN B C   1 
ATOM   2942 O  O   . ASN A 1 473 ? 3.520   -24.803 41.495  1.00 85.73  ? 446 ASN B O   1 
ATOM   2943 C  CB  . ASN A 1 473 ? 4.211   -27.470 41.039  1.00 84.05  ? 446 ASN B CB  1 
ATOM   2944 C  CG  . ASN A 1 473 ? 4.593   -28.944 41.209  1.00 87.82  ? 446 ASN B CG  1 
ATOM   2945 O  OD1 . ASN A 1 473 ? 4.130   -29.620 42.127  1.00 93.43  ? 446 ASN B OD1 1 
ATOM   2946 N  ND2 . ASN A 1 473 ? 5.441   -29.446 40.317  1.00 90.49  ? 446 ASN B ND2 1 
ATOM   2947 N  N   . GLY A 1 474 ? 1.318   -25.221 41.840  1.00 74.78  ? 447 GLY B N   1 
ATOM   2948 C  CA  . GLY A 1 474 ? 0.923   -23.806 41.815  1.00 68.60  ? 447 GLY B CA  1 
ATOM   2949 C  C   . GLY A 1 474 ? 1.207   -23.070 40.512  1.00 67.74  ? 447 GLY B C   1 
ATOM   2950 O  O   . GLY A 1 474 ? 1.247   -21.856 40.507  1.00 69.66  ? 447 GLY B O   1 
ATOM   2951 N  N   . SER A 1 475 ? 1.398   -23.776 39.398  1.00 64.08  ? 448 SER B N   1 
ATOM   2952 C  CA  . SER A 1 475 ? 1.760   -23.103 38.154  1.00 65.30  ? 448 SER B CA  1 
ATOM   2953 C  C   . SER A 1 475 ? 0.579   -22.352 37.523  1.00 69.70  ? 448 SER B C   1 
ATOM   2954 O  O   . SER A 1 475 ? -0.588  -22.666 37.776  1.00 71.81  ? 448 SER B O   1 
ATOM   2955 C  CB  . SER A 1 475 ? 2.329   -24.096 37.142  1.00 65.65  ? 448 SER B CB  1 
ATOM   2956 O  OG  . SER A 1 475 ? 1.310   -24.898 36.581  1.00 70.28  ? 448 SER B OG  1 
ATOM   2957 N  N   . CYS A 1 476 ? 0.910   -21.361 36.701  1.00 73.00  ? 449 CYS B N   1 
ATOM   2958 C  CA  . CYS A 1 476 ? -0.071  -20.582 35.971  1.00 73.06  ? 449 CYS B CA  1 
ATOM   2959 C  C   . CYS A 1 476 ? -0.296  -21.116 34.555  1.00 74.16  ? 449 CYS B C   1 
ATOM   2960 O  O   . CYS A 1 476 ? 0.343   -22.077 34.121  1.00 76.19  ? 449 CYS B O   1 
ATOM   2961 C  CB  . CYS A 1 476 ? 0.368   -19.120 35.916  1.00 75.51  ? 449 CYS B CB  1 
ATOM   2962 S  SG  . CYS A 1 476 ? 0.385   -18.279 37.526  1.00 81.34  ? 449 CYS B SG  1 
ATOM   2963 N  N   . ALA A 1 477 ? -1.245  -20.501 33.857  1.00 77.48  ? 450 ALA B N   1 
ATOM   2964 C  CA  . ALA A 1 477 ? -1.439  -20.731 32.429  1.00 72.32  ? 450 ALA B CA  1 
ATOM   2965 C  C   . ALA A 1 477 ? -0.923  -19.517 31.680  1.00 67.65  ? 450 ALA B C   1 
ATOM   2966 O  O   . ALA A 1 477 ? -1.044  -18.401 32.175  1.00 72.37  ? 450 ALA B O   1 
ATOM   2967 C  CB  . ALA A 1 477 ? -2.903  -20.939 32.132  1.00 68.66  ? 450 ALA B CB  1 
ATOM   2968 N  N   . ASP A 1 478 ? -0.334  -19.739 30.512  1.00 64.17  ? 451 ASP B N   1 
ATOM   2969 C  CA  . ASP A 1 478 ? 0.128   -18.649 29.653  1.00 71.05  ? 451 ASP B CA  1 
ATOM   2970 C  C   . ASP A 1 478 ? -1.040  -18.078 28.848  1.00 69.86  ? 451 ASP B C   1 
ATOM   2971 O  O   . ASP A 1 478 ? -1.557  -18.754 27.946  1.00 72.57  ? 451 ASP B O   1 
ATOM   2972 C  CB  . ASP A 1 478 ? 1.229   -19.162 28.694  1.00 77.01  ? 451 ASP B CB  1 
ATOM   2973 C  CG  . ASP A 1 478 ? 1.610   -18.136 27.614  1.00 84.81  ? 451 ASP B CG  1 
ATOM   2974 O  OD1 . ASP A 1 478 ? 1.573   -16.906 27.876  1.00 68.55  ? 451 ASP B OD1 1 
ATOM   2975 O  OD2 . ASP A 1 478 ? 1.944   -18.574 26.487  1.00 104.73 ? 451 ASP B OD2 1 
ATOM   2976 N  N   . ILE A 1 479 ? -1.432  -16.838 29.138  1.00 63.24  ? 452 ILE B N   1 
ATOM   2977 C  CA  . ILE A 1 479 ? -2.500  -16.203 28.378  1.00 69.31  ? 452 ILE B CA  1 
ATOM   2978 C  C   . ILE A 1 479 ? -2.161  -15.962 26.900  1.00 79.09  ? 452 ILE B C   1 
ATOM   2979 O  O   . ILE A 1 479 ? -3.061  -15.883 26.058  1.00 82.06  ? 452 ILE B O   1 
ATOM   2980 C  CB  . ILE A 1 479 ? -3.003  -14.891 29.010  1.00 73.67  ? 452 ILE B CB  1 
ATOM   2981 C  CG1 . ILE A 1 479 ? -4.377  -14.534 28.419  1.00 72.71  ? 452 ILE B CG1 1 
ATOM   2982 C  CG2 . ILE A 1 479 ? -2.011  -13.757 28.813  1.00 72.20  ? 452 ILE B CG2 1 
ATOM   2983 C  CD1 . ILE A 1 479 ? -5.170  -13.528 29.231  1.00 76.36  ? 452 ILE B CD1 1 
ATOM   2984 N  N   . LYS A 1 480 ? -0.877  -15.850 26.574  1.00 85.07  ? 453 LYS B N   1 
ATOM   2985 C  CA  . LYS A 1 480 ? -0.468  -15.743 25.174  1.00 83.62  ? 453 LYS B CA  1 
ATOM   2986 C  C   . LYS A 1 480 ? -0.830  -17.021 24.427  1.00 77.45  ? 453 LYS B C   1 
ATOM   2987 O  O   . LYS A 1 480 ? -1.046  -16.978 23.234  1.00 87.26  ? 453 LYS B O   1 
ATOM   2988 C  CB  . LYS A 1 480 ? 1.049   -15.492 25.025  1.00 97.18  ? 453 LYS B CB  1 
ATOM   2989 C  CG  . LYS A 1 480 ? 1.627   -14.264 25.736  1.00 101.44 ? 453 LYS B CG  1 
ATOM   2990 C  CD  . LYS A 1 480 ? 1.085   -12.961 25.171  1.00 101.88 ? 453 LYS B CD  1 
ATOM   2991 C  CE  . LYS A 1 480 ? 1.338   -11.796 26.114  1.00 109.49 ? 453 LYS B CE  1 
ATOM   2992 N  NZ  . LYS A 1 480 ? 0.156   -10.885 26.164  1.00 111.18 ? 453 LYS B NZ  1 
ATOM   2993 N  N   . LYS A 1 481 ? -0.886  -18.153 25.122  1.00 74.01  ? 454 LYS B N   1 
ATOM   2994 C  CA  . LYS A 1 481 ? -1.145  -19.452 24.488  1.00 76.57  ? 454 LYS B CA  1 
ATOM   2995 C  C   . LYS A 1 481 ? -2.203  -20.293 25.272  1.00 74.52  ? 454 LYS B C   1 
ATOM   2996 O  O   . LYS A 1 481 ? -1.969  -21.471 25.551  1.00 69.82  ? 454 LYS B O   1 
ATOM   2997 C  CB  . LYS A 1 481 ? 0.182   -20.230 24.339  1.00 68.73  ? 454 LYS B CB  1 
ATOM   2998 N  N   . VAL A 1 482 ? -3.365  -19.697 25.578  1.00 66.64  ? 455 VAL B N   1 
ATOM   2999 C  CA  . VAL A 1 482 ? -4.384  -20.334 26.454  1.00 64.77  ? 455 VAL B CA  1 
ATOM   3000 C  C   . VAL A 1 482 ? -5.145  -21.453 25.779  1.00 61.23  ? 455 VAL B C   1 
ATOM   3001 O  O   . VAL A 1 482 ? -5.550  -21.299 24.638  1.00 61.56  ? 455 VAL B O   1 
ATOM   3002 C  CB  . VAL A 1 482 ? -5.547  -19.417 26.895  1.00 70.37  ? 455 VAL B CB  1 
ATOM   3003 C  CG1 . VAL A 1 482 ? -5.953  -19.768 28.313  1.00 76.35  ? 455 VAL B CG1 1 
ATOM   3004 C  CG2 . VAL A 1 482 ? -5.228  -17.946 26.795  1.00 78.78  ? 455 VAL B CG2 1 
ATOM   3005 N  N   . GLU A 1 483 ? -5.400  -22.532 26.519  1.00 56.40  ? 456 GLU B N   1 
ATOM   3006 C  CA  . GLU A 1 483 ? -6.200  -23.659 26.047  1.00 61.92  ? 456 GLU B CA  1 
ATOM   3007 C  C   . GLU A 1 483 ? -7.576  -23.718 26.741  1.00 64.51  ? 456 GLU B C   1 
ATOM   3008 O  O   . GLU A 1 483 ? -7.709  -23.372 27.911  1.00 60.28  ? 456 GLU B O   1 
ATOM   3009 C  CB  . GLU A 1 483 ? -5.433  -24.942 26.249  1.00 63.91  ? 456 GLU B CB  1 
ATOM   3010 C  CG  . GLU A 1 483 ? -4.048  -24.847 25.636  1.00 74.15  ? 456 GLU B CG  1 
ATOM   3011 C  CD  . GLU A 1 483 ? -3.338  -26.182 25.550  1.00 86.92  ? 456 GLU B CD  1 
ATOM   3012 O  OE1 . GLU A 1 483 ? -2.903  -26.725 26.598  1.00 84.00  ? 456 GLU B OE1 1 
ATOM   3013 O  OE2 . GLU A 1 483 ? -3.205  -26.680 24.414  1.00 101.87 ? 456 GLU B OE2 1 
ATOM   3014 N  N   . ALA A 1 484 ? -8.603  -24.145 26.003  1.00 60.73  ? 457 ALA B N   1 
ATOM   3015 C  CA  . ALA A 1 484 ? -9.972  -24.105 26.504  1.00 57.10  ? 457 ALA B CA  1 
ATOM   3016 C  C   . ALA A 1 484 ? -10.114 -24.689 27.898  1.00 52.28  ? 457 ALA B C   1 
ATOM   3017 O  O   . ALA A 1 484 ? -10.740 -24.078 28.750  1.00 54.52  ? 457 ALA B O   1 
ATOM   3018 C  CB  . ALA A 1 484 ? -10.920 -24.810 25.560  1.00 58.32  ? 457 ALA B CB  1 
ATOM   3019 N  N   . TRP A 1 485 ? -9.513  -25.844 28.133  1.00 49.58  ? 458 TRP B N   1 
ATOM   3020 C  CA  . TRP A 1 485 ? -9.642  -26.504 29.419  1.00 52.55  ? 458 TRP B CA  1 
ATOM   3021 C  C   . TRP A 1 485 ? -9.131  -25.663 30.617  1.00 54.70  ? 458 TRP B C   1 
ATOM   3022 O  O   . TRP A 1 485 ? -9.563  -25.849 31.770  1.00 50.43  ? 458 TRP B O   1 
ATOM   3023 C  CB  . TRP A 1 485 ? -8.984  -27.895 29.375  1.00 53.94  ? 458 TRP B CB  1 
ATOM   3024 C  CG  . TRP A 1 485 ? -7.506  -27.867 29.287  1.00 61.36  ? 458 TRP B CG  1 
ATOM   3025 C  CD1 . TRP A 1 485 ? -6.744  -27.883 28.141  1.00 67.73  ? 458 TRP B CD1 1 
ATOM   3026 C  CD2 . TRP A 1 485 ? -6.587  -27.813 30.376  1.00 64.60  ? 458 TRP B CD2 1 
ATOM   3027 N  NE1 . TRP A 1 485 ? -5.409  -27.834 28.456  1.00 64.39  ? 458 TRP B NE1 1 
ATOM   3028 C  CE2 . TRP A 1 485 ? -5.281  -27.789 29.821  1.00 67.82  ? 458 TRP B CE2 1 
ATOM   3029 C  CE3 . TRP A 1 485 ? -6.734  -27.770 31.769  1.00 67.53  ? 458 TRP B CE3 1 
ATOM   3030 C  CZ2 . TRP A 1 485 ? -4.134  -27.730 30.614  1.00 63.07  ? 458 TRP B CZ2 1 
ATOM   3031 C  CZ3 . TRP A 1 485 ? -5.586  -27.711 32.558  1.00 67.65  ? 458 TRP B CZ3 1 
ATOM   3032 C  CH2 . TRP A 1 485 ? -4.308  -27.692 31.974  1.00 67.95  ? 458 TRP B CH2 1 
ATOM   3033 N  N   . GLN A 1 486 ? -8.225  -24.726 30.352  1.00 53.83  ? 459 GLN B N   1 
ATOM   3034 C  CA  . GLN A 1 486 ? -7.713  -23.864 31.420  1.00 50.91  ? 459 GLN B CA  1 
ATOM   3035 C  C   . GLN A 1 486 ? -8.722  -22.815 31.786  1.00 47.34  ? 459 GLN B C   1 
ATOM   3036 O  O   . GLN A 1 486 ? -8.801  -22.392 32.955  1.00 46.24  ? 459 GLN B O   1 
ATOM   3037 C  CB  . GLN A 1 486 ? -6.383  -23.238 31.023  1.00 52.44  ? 459 GLN B CB  1 
ATOM   3038 C  CG  . GLN A 1 486 ? -5.342  -24.333 30.883  1.00 55.56  ? 459 GLN B CG  1 
ATOM   3039 C  CD  . GLN A 1 486 ? -4.065  -23.900 30.211  1.00 55.94  ? 459 GLN B CD  1 
ATOM   3040 O  OE1 . GLN A 1 486 ? -4.062  -23.078 29.305  1.00 54.67  ? 459 GLN B OE1 1 
ATOM   3041 N  NE2 . GLN A 1 486 ? -2.963  -24.476 30.654  1.00 65.21  ? 459 GLN B NE2 1 
ATOM   3042 N  N   . VAL A 1 487 ? -9.504  -22.399 30.795  1.00 45.34  ? 460 VAL B N   1 
ATOM   3043 C  CA  . VAL A 1 487 ? -10.572 -21.462 31.048  1.00 43.79  ? 460 VAL B CA  1 
ATOM   3044 C  C   . VAL A 1 487 ? -11.685 -22.183 31.824  1.00 43.37  ? 460 VAL B C   1 
ATOM   3045 O  O   . VAL A 1 487 ? -12.267 -21.609 32.758  1.00 42.48  ? 460 VAL B O   1 
ATOM   3046 C  CB  . VAL A 1 487 ? -11.066 -20.827 29.763  1.00 44.41  ? 460 VAL B CB  1 
ATOM   3047 C  CG1 . VAL A 1 487 ? -12.128 -19.762 30.066  1.00 43.70  ? 460 VAL B CG1 1 
ATOM   3048 C  CG2 . VAL A 1 487 ? -9.895  -20.173 29.068  1.00 48.63  ? 460 VAL B CG2 1 
ATOM   3049 N  N   . LEU A 1 488 ? -11.944 -23.440 31.474  1.00 39.03  ? 461 LEU B N   1 
ATOM   3050 C  CA  . LEU A 1 488 ? -12.945 -24.219 32.173  1.00 43.91  ? 461 LEU B CA  1 
ATOM   3051 C  C   . LEU A 1 488 ? -12.534 -24.197 33.634  1.00 47.57  ? 461 LEU B C   1 
ATOM   3052 O  O   . LEU A 1 488 ? -13.310 -23.806 34.525  1.00 42.08  ? 461 LEU B O   1 
ATOM   3053 C  CB  . LEU A 1 488 ? -12.978 -25.669 31.666  1.00 46.73  ? 461 LEU B CB  1 
ATOM   3054 C  CG  . LEU A 1 488 ? -14.307 -26.429 31.726  1.00 47.54  ? 461 LEU B CG  1 
ATOM   3055 C  CD1 . LEU A 1 488 ? -14.141 -27.943 31.672  1.00 44.52  ? 461 LEU B CD1 1 
ATOM   3056 C  CD2 . LEU A 1 488 ? -15.143 -26.042 32.919  1.00 48.71  ? 461 LEU B CD2 1 
ATOM   3057 N  N   . LYS A 1 489 ? -11.278 -24.577 33.864  1.00 48.18  ? 462 LYS B N   1 
ATOM   3058 C  CA  . LYS A 1 489 ? -10.750 -24.637 35.208  1.00 49.25  ? 462 LYS B CA  1 
ATOM   3059 C  C   . LYS A 1 489 ? -10.963 -23.326 35.930  1.00 49.76  ? 462 LYS B C   1 
ATOM   3060 O  O   . LYS A 1 489 ? -11.443 -23.303 37.064  1.00 53.58  ? 462 LYS B O   1 
ATOM   3061 C  CB  . LYS A 1 489 ? -9.281  -24.969 35.174  1.00 53.05  ? 462 LYS B CB  1 
ATOM   3062 C  CG  . LYS A 1 489 ? -8.618  -24.947 36.529  1.00 56.72  ? 462 LYS B CG  1 
ATOM   3063 C  CD  . LYS A 1 489 ? -9.210  -25.973 37.481  1.00 55.26  ? 462 LYS B CD  1 
ATOM   3064 C  CE  . LYS A 1 489 ? -8.506  -25.859 38.820  1.00 52.99  ? 462 LYS B CE  1 
ATOM   3065 N  NZ  . LYS A 1 489 ? -8.364  -27.190 39.385  1.00 53.55  ? 462 LYS B NZ  1 
ATOM   3066 N  N   . HIS A 1 490 ? -10.620 -22.228 35.279  1.00 45.48  ? 463 HIS B N   1 
ATOM   3067 C  CA  . HIS A 1 490 ? -10.819 -20.948 35.911  1.00 48.02  ? 463 HIS B CA  1 
ATOM   3068 C  C   . HIS A 1 490 ? -12.289 -20.629 36.125  1.00 50.87  ? 463 HIS B C   1 
ATOM   3069 O  O   . HIS A 1 490 ? -12.644 -20.022 37.128  1.00 53.40  ? 463 HIS B O   1 
ATOM   3070 C  CB  . HIS A 1 490 ? -10.097 -19.841 35.146  1.00 51.28  ? 463 HIS B CB  1 
ATOM   3071 C  CG  . HIS A 1 490 ? -8.696  -19.672 35.609  1.00 58.25  ? 463 HIS B CG  1 
ATOM   3072 N  ND1 . HIS A 1 490 ? -8.364  -18.817 36.639  1.00 54.78  ? 463 HIS B ND1 1 
ATOM   3073 C  CD2 . HIS A 1 490 ? -7.567  -20.352 35.287  1.00 56.32  ? 463 HIS B CD2 1 
ATOM   3074 C  CE1 . HIS A 1 490 ? -7.076  -18.943 36.892  1.00 56.22  ? 463 HIS B CE1 1 
ATOM   3075 N  NE2 . HIS A 1 490 ? -6.573  -19.875 36.096  1.00 56.38  ? 463 HIS B NE2 1 
ATOM   3076 N  N   . LEU A 1 491 ? -13.144 -21.040 35.195  1.00 46.75  ? 464 LEU B N   1 
ATOM   3077 C  CA  . LEU A 1 491 ? -14.549 -20.820 35.377  1.00 46.13  ? 464 LEU B CA  1 
ATOM   3078 C  C   . LEU A 1 491 ? -15.072 -21.641 36.571  1.00 46.55  ? 464 LEU B C   1 
ATOM   3079 O  O   . LEU A 1 491 ? -15.884 -21.159 37.306  1.00 43.77  ? 464 LEU B O   1 
ATOM   3080 C  CB  . LEU A 1 491 ? -15.307 -21.133 34.094  1.00 46.24  ? 464 LEU B CB  1 
ATOM   3081 C  CG  . LEU A 1 491 ? -15.234 -20.085 33.003  1.00 42.59  ? 464 LEU B CG  1 
ATOM   3082 C  CD1 . LEU A 1 491 ? -15.745 -20.656 31.703  1.00 40.63  ? 464 LEU B CD1 1 
ATOM   3083 C  CD2 . LEU A 1 491 ? -16.071 -18.891 33.391  1.00 46.49  ? 464 LEU B CD2 1 
ATOM   3084 N  N   . ARG A 1 492 ? -14.585 -22.858 36.785  1.00 55.88  ? 465 ARG B N   1 
ATOM   3085 C  CA  . ARG A 1 492 ? -15.011 -23.650 37.955  1.00 57.80  ? 465 ARG B CA  1 
ATOM   3086 C  C   . ARG A 1 492 ? -14.670 -22.962 39.284  1.00 56.18  ? 465 ARG B C   1 
ATOM   3087 O  O   . ARG A 1 492 ? -15.414 -23.127 40.247  1.00 59.78  ? 465 ARG B O   1 
ATOM   3088 C  CB  . ARG A 1 492 ? -14.429 -25.081 37.951  1.00 61.04  ? 465 ARG B CB  1 
ATOM   3089 C  CG  . ARG A 1 492 ? -14.681 -25.878 36.667  1.00 71.63  ? 465 ARG B CG  1 
ATOM   3090 C  CD  . ARG A 1 492 ? -15.128 -27.342 36.882  1.00 86.12  ? 465 ARG B CD  1 
ATOM   3091 N  NE  . ARG A 1 492 ? -14.055 -28.356 36.799  1.00 88.28  ? 465 ARG B NE  1 
ATOM   3092 C  CZ  . ARG A 1 492 ? -13.120 -28.568 37.735  1.00 92.41  ? 465 ARG B CZ  1 
ATOM   3093 N  NH1 . ARG A 1 492 ? -13.064 -27.845 38.851  1.00 94.33  ? 465 ARG B NH1 1 
ATOM   3094 N  NH2 . ARG A 1 492 ? -12.209 -29.507 37.556  1.00 94.85  ? 465 ARG B NH2 1 
ATOM   3095 N  N   . HIS A 1 493 ? -13.579 -22.184 39.345  1.00 54.62  ? 466 HIS B N   1 
ATOM   3096 C  CA  . HIS A 1 493 ? -13.174 -21.497 40.609  1.00 52.40  ? 466 HIS B CA  1 
ATOM   3097 C  C   . HIS A 1 493 ? -13.504 -20.007 40.670  1.00 45.90  ? 466 HIS B C   1 
ATOM   3098 O  O   . HIS A 1 493 ? -13.217 -19.335 41.638  1.00 48.65  ? 466 HIS B O   1 
ATOM   3099 C  CB  . HIS A 1 493 ? -11.686 -21.730 40.916  1.00 53.87  ? 466 HIS B CB  1 
ATOM   3100 C  CG  . HIS A 1 493 ? -11.361 -23.155 41.261  1.00 63.18  ? 466 HIS B CG  1 
ATOM   3101 N  ND1 . HIS A 1 493 ? -10.902 -23.543 42.503  1.00 66.57  ? 466 HIS B ND1 1 
ATOM   3102 C  CD2 . HIS A 1 493 ? -11.459 -24.292 40.529  1.00 70.48  ? 466 HIS B CD2 1 
ATOM   3103 C  CE1 . HIS A 1 493 ? -10.724 -24.853 42.519  1.00 70.09  ? 466 HIS B CE1 1 
ATOM   3104 N  NE2 . HIS A 1 493 ? -11.049 -25.332 41.329  1.00 70.19  ? 466 HIS B NE2 1 
ATOM   3105 N  N   . LEU A 1 494 ? -14.182 -19.500 39.666  1.00 48.39  ? 467 LEU B N   1 
ATOM   3106 C  CA  . LEU A 1 494 ? -14.445 -18.090 39.551  1.00 45.38  ? 467 LEU B CA  1 
ATOM   3107 C  C   . LEU A 1 494 ? -15.291 -17.581 40.698  1.00 48.82  ? 467 LEU B C   1 
ATOM   3108 O  O   . LEU A 1 494 ? -16.186 -18.280 41.211  1.00 59.62  ? 467 LEU B O   1 
ATOM   3109 C  CB  . LEU A 1 494 ? -15.132 -17.838 38.210  1.00 49.29  ? 467 LEU B CB  1 
ATOM   3110 C  CG  . LEU A 1 494 ? -15.490 -16.403 37.802  1.00 59.80  ? 467 LEU B CG  1 
ATOM   3111 C  CD1 . LEU A 1 494 ? -14.245 -15.546 37.633  1.00 60.06  ? 467 LEU B CD1 1 
ATOM   3112 C  CD2 . LEU A 1 494 ? -16.298 -16.383 36.505  1.00 59.46  ? 467 LEU B CD2 1 
ATOM   3113 N  N   . ASN A 1 495 ? -14.997 -16.348 41.089  1.00 52.06  ? 468 ASN B N   1 
ATOM   3114 C  CA  . ASN A 1 495 ? -15.796 -15.577 42.055  1.00 50.83  ? 468 ASN B CA  1 
ATOM   3115 C  C   . ASN A 1 495 ? -15.628 -14.119 41.735  1.00 53.36  ? 468 ASN B C   1 
ATOM   3116 O  O   . ASN A 1 495 ? -14.522 -13.642 41.810  1.00 59.28  ? 468 ASN B O   1 
ATOM   3117 C  CB  . ASN A 1 495 ? -15.272 -15.785 43.455  1.00 49.36  ? 468 ASN B CB  1 
ATOM   3118 C  CG  . ASN A 1 495 ? -16.194 -15.221 44.526  1.00 57.73  ? 468 ASN B CG  1 
ATOM   3119 O  OD1 . ASN A 1 495 ? -17.034 -14.359 44.270  1.00 54.46  ? 468 ASN B OD1 1 
ATOM   3120 N  ND2 . ASN A 1 495 ? -16.037 -15.750 45.763  1.00 63.80  ? 468 ASN B ND2 1 
ATOM   3121 N  N   . PHE A 1 496 ? -16.684 -13.399 41.368  1.00 52.96  ? 469 PHE B N   1 
ATOM   3122 C  CA  . PHE A 1 496 ? -16.509 -11.979 41.061  1.00 52.07  ? 469 PHE B CA  1 
ATOM   3123 C  C   . PHE A 1 496 ? -17.751 -11.181 41.351  1.00 54.62  ? 469 PHE B C   1 
ATOM   3124 O  O   . PHE A 1 496 ? -18.825 -11.729 41.613  1.00 54.67  ? 469 PHE B O   1 
ATOM   3125 C  CB  . PHE A 1 496 ? -16.043 -11.763 39.615  1.00 55.51  ? 469 PHE B CB  1 
ATOM   3126 C  CG  . PHE A 1 496 ? -17.134 -11.872 38.593  1.00 56.90  ? 469 PHE B CG  1 
ATOM   3127 C  CD1 . PHE A 1 496 ? -17.377 -13.068 37.949  1.00 55.03  ? 469 PHE B CD1 1 
ATOM   3128 C  CD2 . PHE A 1 496 ? -17.919 -10.774 38.280  1.00 61.39  ? 469 PHE B CD2 1 
ATOM   3129 C  CE1 . PHE A 1 496 ? -18.400 -13.180 37.034  1.00 54.69  ? 469 PHE B CE1 1 
ATOM   3130 C  CE2 . PHE A 1 496 ? -18.937 -10.875 37.352  1.00 57.95  ? 469 PHE B CE2 1 
ATOM   3131 C  CZ  . PHE A 1 496 ? -19.176 -12.081 36.735  1.00 56.82  ? 469 PHE B CZ  1 
ATOM   3132 N  N   . THR A 1 497 ? -17.604 -9.871  41.325  1.00 55.30  ? 470 THR B N   1 
ATOM   3133 C  CA  . THR A 1 497 ? -18.681 -9.020  41.771  1.00 60.88  ? 470 THR B CA  1 
ATOM   3134 C  C   . THR A 1 497 ? -19.212 -8.380  40.536  1.00 58.52  ? 470 THR B C   1 
ATOM   3135 O  O   . THR A 1 497 ? -18.451 -7.884  39.746  1.00 65.50  ? 470 THR B O   1 
ATOM   3136 C  CB  . THR A 1 497 ? -18.173 -7.991  42.798  1.00 67.96  ? 470 THR B CB  1 
ATOM   3137 O  OG1 . THR A 1 497 ? -17.562 -8.704  43.886  1.00 70.00  ? 470 THR B OG1 1 
ATOM   3138 C  CG2 . THR A 1 497 ? -19.315 -7.136  43.346  1.00 67.97  ? 470 THR B CG2 1 
ATOM   3139 N  N   . ASN A 1 498 ? -20.510 -8.443  40.326  1.00 61.58  ? 471 ASN B N   1 
ATOM   3140 C  CA  . ASN A 1 498 ? -21.055 -7.924  39.085  1.00 68.86  ? 471 ASN B CA  1 
ATOM   3141 C  C   . ASN A 1 498 ? -21.473 -6.468  39.251  1.00 70.62  ? 471 ASN B C   1 
ATOM   3142 O  O   . ASN A 1 498 ? -21.674 -6.004  40.359  1.00 71.77  ? 471 ASN B O   1 
ATOM   3143 C  CB  . ASN A 1 498 ? -22.180 -8.825  38.506  1.00 64.56  ? 471 ASN B CB  1 
ATOM   3144 C  CG  . ASN A 1 498 ? -23.376 -9.028  39.438  1.00 63.45  ? 471 ASN B CG  1 
ATOM   3145 O  OD1 . ASN A 1 498 ? -23.689 -8.216  40.320  1.00 63.41  ? 471 ASN B OD1 1 
ATOM   3146 N  ND2 . ASN A 1 498 ? -24.095 -10.121 39.196  1.00 68.56  ? 471 ASN B ND2 1 
ATOM   3147 N  N   . ASN A 1 499 ? -21.567 -5.743  38.149  1.00 77.07  ? 472 ASN B N   1 
ATOM   3148 C  CA  . ASN A 1 499 ? -22.145 -4.406  38.169  1.00 75.56  ? 472 ASN B CA  1 
ATOM   3149 C  C   . ASN A 1 499 ? -23.355 -4.254  39.118  1.00 67.51  ? 472 ASN B C   1 
ATOM   3150 O  O   . ASN A 1 499 ? -23.504 -3.222  39.730  1.00 78.82  ? 472 ASN B O   1 
ATOM   3151 C  CB  . ASN A 1 499 ? -22.520 -3.970  36.751  1.00 77.65  ? 472 ASN B CB  1 
ATOM   3152 C  CG  . ASN A 1 499 ? -23.753 -4.680  36.235  1.00 77.19  ? 472 ASN B CG  1 
ATOM   3153 O  OD1 . ASN A 1 499 ? -24.740 -4.046  35.893  1.00 79.02  ? 472 ASN B OD1 1 
ATOM   3154 N  ND2 . ASN A 1 499 ? -23.709 -6.004  36.201  1.00 76.21  ? 472 ASN B ND2 1 
ATOM   3155 N  N   . MET A 1 500 ? -24.198 -5.263  39.279  1.00 68.97  ? 473 MET B N   1 
ATOM   3156 C  CA  . MET A 1 500 ? -25.306 -5.160  40.245  1.00 78.43  ? 473 MET B CA  1 
ATOM   3157 C  C   . MET A 1 500 ? -24.811 -5.323  41.700  1.00 86.55  ? 473 MET B C   1 
ATOM   3158 O  O   . MET A 1 500 ? -25.613 -5.283  42.643  1.00 92.55  ? 473 MET B O   1 
ATOM   3159 C  CB  . MET A 1 500 ? -26.413 -6.211  39.977  1.00 82.70  ? 473 MET B CB  1 
ATOM   3160 C  CG  . MET A 1 500 ? -27.026 -6.248  38.572  1.00 78.60  ? 473 MET B CG  1 
ATOM   3161 S  SD  . MET A 1 500 ? -28.068 -4.860  38.087  1.00 85.51  ? 473 MET B SD  1 
ATOM   3162 C  CE  . MET A 1 500 ? -29.296 -4.755  39.397  1.00 79.97  ? 473 MET B CE  1 
ATOM   3163 N  N   . GLY A 1 501 ? -23.506 -5.527  41.884  1.00 84.28  ? 474 GLY B N   1 
ATOM   3164 C  CA  . GLY A 1 501 ? -22.911 -5.678  43.209  1.00 86.81  ? 474 GLY B CA  1 
ATOM   3165 C  C   . GLY A 1 501 ? -23.167 -7.033  43.839  1.00 88.39  ? 474 GLY B C   1 
ATOM   3166 O  O   . GLY A 1 501 ? -23.271 -7.153  45.053  1.00 85.31  ? 474 GLY B O   1 
ATOM   3167 N  N   . GLU A 1 502 ? -23.275 -8.058  43.012  1.00 89.11  ? 475 GLU B N   1 
ATOM   3168 C  CA  . GLU A 1 502 ? -23.489 -9.403  43.508  1.00 88.04  ? 475 GLU B CA  1 
ATOM   3169 C  C   . GLU A 1 502 ? -22.266 -10.277 43.196  1.00 79.81  ? 475 GLU B C   1 
ATOM   3170 O  O   . GLU A 1 502 ? -21.506 -10.011 42.257  1.00 61.33  ? 475 GLU B O   1 
ATOM   3171 C  CB  . GLU A 1 502 ? -24.755 -9.993  42.893  1.00 93.77  ? 475 GLU B CB  1 
ATOM   3172 C  CG  . GLU A 1 502 ? -26.022 -9.193  43.172  1.00 101.75 ? 475 GLU B CG  1 
ATOM   3173 C  CD  . GLU A 1 502 ? -27.009 -9.921  44.070  1.00 106.46 ? 475 GLU B CD  1 
ATOM   3174 O  OE1 . GLU A 1 502 ? -27.483 -11.004 43.677  1.00 99.25  ? 475 GLU B OE1 1 
ATOM   3175 O  OE2 . GLU A 1 502 ? -27.336 -9.402  45.159  1.00 121.24 ? 475 GLU B OE2 1 
ATOM   3176 N  N   . GLN A 1 503 ? -22.069 -11.305 44.016  1.00 73.50  ? 476 GLN B N   1 
ATOM   3177 C  CA  . GLN A 1 503 ? -21.006 -12.265 43.789  1.00 68.68  ? 476 GLN B CA  1 
ATOM   3178 C  C   . GLN A 1 503 ? -21.499 -13.319 42.810  1.00 60.06  ? 476 GLN B C   1 
ATOM   3179 O  O   . GLN A 1 503 ? -22.533 -13.929 42.990  1.00 56.41  ? 476 GLN B O   1 
ATOM   3180 C  CB  . GLN A 1 503 ? -20.571 -12.936 45.105  1.00 75.80  ? 476 GLN B CB  1 
ATOM   3181 C  CG  . GLN A 1 503 ? -19.925 -12.004 46.110  1.00 78.35  ? 476 GLN B CG  1 
ATOM   3182 C  CD  . GLN A 1 503 ? -18.853 -11.140 45.468  1.00 83.09  ? 476 GLN B CD  1 
ATOM   3183 O  OE1 . GLN A 1 503 ? -17.902 -11.649 44.871  1.00 82.07  ? 476 GLN B OE1 1 
ATOM   3184 N  NE2 . GLN A 1 503 ? -19.016 -9.822  45.563  1.00 88.69  ? 476 GLN B NE2 1 
ATOM   3185 N  N   . VAL A 1 504 ? -20.743 -13.545 41.769  1.00 52.69  ? 477 VAL B N   1 
ATOM   3186 C  CA  . VAL A 1 504 ? -21.085 -14.577 40.847  1.00 49.85  ? 477 VAL B CA  1 
ATOM   3187 C  C   . VAL A 1 504 ? -20.053 -15.683 40.975  1.00 49.53  ? 477 VAL B C   1 
ATOM   3188 O  O   . VAL A 1 504 ? -18.880 -15.488 40.654  1.00 53.21  ? 477 VAL B O   1 
ATOM   3189 C  CB  . VAL A 1 504 ? -21.097 -14.027 39.410  1.00 48.41  ? 477 VAL B CB  1 
ATOM   3190 C  CG1 . VAL A 1 504 ? -21.474 -15.134 38.445  1.00 48.93  ? 477 VAL B CG1 1 
ATOM   3191 C  CG2 . VAL A 1 504 ? -22.064 -12.860 39.298  1.00 46.40  ? 477 VAL B CG2 1 
ATOM   3192 N  N   . THR A 1 505 ? -20.500 -16.832 41.451  1.00 48.37  ? 478 THR B N   1 
ATOM   3193 C  CA  . THR A 1 505 ? -19.710 -18.045 41.487  1.00 51.79  ? 478 THR B CA  1 
ATOM   3194 C  C   . THR A 1 505 ? -20.645 -19.153 41.005  1.00 51.59  ? 478 THR B C   1 
ATOM   3195 O  O   . THR A 1 505 ? -21.859 -18.964 41.065  1.00 53.41  ? 478 THR B O   1 
ATOM   3196 C  CB  . THR A 1 505 ? -19.252 -18.380 42.935  1.00 60.30  ? 478 THR B CB  1 
ATOM   3197 O  OG1 . THR A 1 505 ? -20.393 -18.541 43.811  1.00 53.97  ? 478 THR B OG1 1 
ATOM   3198 C  CG2 . THR A 1 505 ? -18.355 -17.292 43.507  1.00 58.96  ? 478 THR B CG2 1 
ATOM   3199 N  N   . PHE A 1 506 ? -20.087 -20.295 40.573  1.00 47.74  ? 479 PHE B N   1 
ATOM   3200 C  CA  . PHE A 1 506 ? -20.850 -21.435 40.082  1.00 45.82  ? 479 PHE B CA  1 
ATOM   3201 C  C   . PHE A 1 506 ? -20.698 -22.611 41.014  1.00 48.44  ? 479 PHE B C   1 
ATOM   3202 O  O   . PHE A 1 506 ? -19.623 -22.881 41.482  1.00 49.47  ? 479 PHE B O   1 
ATOM   3203 C  CB  . PHE A 1 506 ? -20.343 -21.892 38.724  1.00 48.28  ? 479 PHE B CB  1 
ATOM   3204 C  CG  . PHE A 1 506 ? -20.445 -20.866 37.663  1.00 50.55  ? 479 PHE B CG  1 
ATOM   3205 C  CD1 . PHE A 1 506 ? -21.627 -20.692 36.958  1.00 56.38  ? 479 PHE B CD1 1 
ATOM   3206 C  CD2 . PHE A 1 506 ? -19.365 -20.080 37.351  1.00 50.44  ? 479 PHE B CD2 1 
ATOM   3207 C  CE1 . PHE A 1 506 ? -21.724 -19.720 35.975  1.00 57.63  ? 479 PHE B CE1 1 
ATOM   3208 C  CE2 . PHE A 1 506 ? -19.454 -19.110 36.369  1.00 52.60  ? 479 PHE B CE2 1 
ATOM   3209 C  CZ  . PHE A 1 506 ? -20.627 -18.931 35.680  1.00 53.91  ? 479 PHE B CZ  1 
ATOM   3210 N  N   . ASP A 1 507 ? -21.759 -23.367 41.230  1.00 53.61  ? 480 ASP B N   1 
ATOM   3211 C  CA  . ASP A 1 507 ? -21.696 -24.460 42.185  1.00 52.78  ? 480 ASP B CA  1 
ATOM   3212 C  C   . ASP A 1 507 ? -20.970 -25.686 41.616  1.00 51.60  ? 480 ASP B C   1 
ATOM   3213 O  O   . ASP A 1 507 ? -20.434 -25.642 40.502  1.00 47.18  ? 480 ASP B O   1 
ATOM   3214 C  CB  . ASP A 1 507 ? -23.100 -24.774 42.757  1.00 57.96  ? 480 ASP B CB  1 
ATOM   3215 C  CG  . ASP A 1 507 ? -24.008 -25.562 41.808  1.00 59.46  ? 480 ASP B CG  1 
ATOM   3216 O  OD1 . ASP A 1 507 ? -23.569 -26.094 40.760  1.00 63.93  ? 480 ASP B OD1 1 
ATOM   3217 O  OD2 . ASP A 1 507 ? -25.201 -25.660 42.141  1.00 64.62  ? 480 ASP B OD2 1 
ATOM   3218 N  N   . GLU A 1 508 ? -20.940 -26.758 42.410  1.00 54.94  ? 481 GLU B N   1 
ATOM   3219 C  CA  . GLU A 1 508 ? -20.319 -28.029 42.022  1.00 58.44  ? 481 GLU B CA  1 
ATOM   3220 C  C   . GLU A 1 508 ? -20.871 -28.545 40.696  1.00 54.86  ? 481 GLU B C   1 
ATOM   3221 O  O   . GLU A 1 508 ? -20.183 -29.286 40.000  1.00 64.52  ? 481 GLU B O   1 
ATOM   3222 C  CB  . GLU A 1 508 ? -20.537 -29.100 43.127  1.00 58.55  ? 481 GLU B CB  1 
HETATM 3223 N  N   . CSO A 1 509 ? -22.106 -28.179 40.364  1.00 54.23  ? 482 CSO B N   1 
HETATM 3224 C  CA  . CSO A 1 509 ? -22.751 -28.593 39.103  1.00 65.24  ? 482 CSO B CA  1 
HETATM 3225 C  CB  . CSO A 1 509 ? -24.181 -29.032 39.407  1.00 74.14  ? 482 CSO B CB  1 
HETATM 3226 S  SG  . CSO A 1 509 ? -24.083 -30.342 40.601  1.00 80.81  ? 482 CSO B SG  1 
HETATM 3227 C  C   . CSO A 1 509 ? -22.732 -27.564 37.991  1.00 63.47  ? 482 CSO B C   1 
HETATM 3228 O  O   . CSO A 1 509 ? -23.206 -27.829 36.897  1.00 66.60  ? 482 CSO B O   1 
HETATM 3229 O  OD  . CSO A 1 509 ? -24.802 -29.508 41.959  1.00 80.68  ? 482 CSO B OD  1 
ATOM   3230 N  N   . GLY A 1 510 ? -22.148 -26.396 38.233  1.00 61.52  ? 483 GLY B N   1 
ATOM   3231 C  CA  . GLY A 1 510 ? -22.001 -25.397 37.193  1.00 56.74  ? 483 GLY B CA  1 
ATOM   3232 C  C   . GLY A 1 510 ? -23.232 -24.534 37.071  1.00 53.79  ? 483 GLY B C   1 
ATOM   3233 O  O   . GLY A 1 510 ? -23.431 -23.890 36.065  1.00 52.55  ? 483 GLY B O   1 
ATOM   3234 N  N   . ASP A 1 511 ? -24.053 -24.517 38.110  1.00 51.14  ? 484 ASP B N   1 
ATOM   3235 C  CA  . ASP A 1 511 ? -25.296 -23.774 38.082  1.00 50.90  ? 484 ASP B CA  1 
ATOM   3236 C  C   . ASP A 1 511 ? -25.072 -22.507 38.849  1.00 49.82  ? 484 ASP B C   1 
ATOM   3237 O  O   . ASP A 1 511 ? -24.155 -22.403 39.626  1.00 47.00  ? 484 ASP B O   1 
ATOM   3238 C  CB  . ASP A 1 511 ? -26.411 -24.587 38.734  1.00 52.51  ? 484 ASP B CB  1 
ATOM   3239 C  CG  . ASP A 1 511 ? -26.668 -25.933 38.025  1.00 58.68  ? 484 ASP B CG  1 
ATOM   3240 O  OD1 . ASP A 1 511 ? -26.379 -26.116 36.813  1.00 73.91  ? 484 ASP B OD1 1 
ATOM   3241 O  OD2 . ASP A 1 511 ? -27.185 -26.828 38.684  1.00 63.12  ? 484 ASP B OD2 1 
ATOM   3242 N  N   . LEU A 1 512 ? -25.913 -21.523 38.631  1.00 54.67  ? 485 LEU B N   1 
ATOM   3243 C  CA  . LEU A 1 512 ? -25.806 -20.300 39.382  1.00 53.94  ? 485 LEU B CA  1 
ATOM   3244 C  C   . LEU A 1 512 ? -27.173 -20.014 39.933  1.00 54.34  ? 485 LEU B C   1 
ATOM   3245 O  O   . LEU A 1 512 ? -28.069 -19.702 39.185  1.00 68.11  ? 485 LEU B O   1 
ATOM   3246 C  CB  . LEU A 1 512 ? -25.303 -19.178 38.481  1.00 56.18  ? 485 LEU B CB  1 
ATOM   3247 C  CG  . LEU A 1 512 ? -25.531 -17.727 38.913  1.00 54.40  ? 485 LEU B CG  1 
ATOM   3248 C  CD1 . LEU A 1 512 ? -24.894 -17.406 40.245  1.00 61.77  ? 485 LEU B CD1 1 
ATOM   3249 C  CD2 . LEU A 1 512 ? -24.971 -16.804 37.862  1.00 50.84  ? 485 LEU B CD2 1 
ATOM   3250 N  N   . VAL A 1 513 ? -27.334 -20.165 41.239  1.00 65.05  ? 486 VAL B N   1 
ATOM   3251 C  CA  . VAL A 1 513 ? -28.606 -19.861 41.922  1.00 72.34  ? 486 VAL B CA  1 
ATOM   3252 C  C   . VAL A 1 513 ? -29.082 -18.418 41.741  1.00 65.59  ? 486 VAL B C   1 
ATOM   3253 O  O   . VAL A 1 513 ? -28.299 -17.477 41.537  1.00 73.47  ? 486 VAL B O   1 
ATOM   3254 C  CB  . VAL A 1 513 ? -28.554 -20.147 43.449  1.00 81.63  ? 486 VAL B CB  1 
ATOM   3255 C  CG1 . VAL A 1 513 ? -28.180 -21.601 43.713  1.00 85.22  ? 486 VAL B CG1 1 
ATOM   3256 C  CG2 . VAL A 1 513 ? -27.605 -19.195 44.175  1.00 81.68  ? 486 VAL B CG2 1 
ATOM   3257 N  N   . GLY A 1 514 ? -30.389 -18.276 41.842  1.00 61.06  ? 487 GLY B N   1 
ATOM   3258 C  CA  . GLY A 1 514 ? -31.089 -17.067 41.452  1.00 61.99  ? 487 GLY B CA  1 
ATOM   3259 C  C   . GLY A 1 514 ? -32.471 -17.143 42.057  1.00 63.47  ? 487 GLY B C   1 
ATOM   3260 O  O   . GLY A 1 514 ? -32.910 -18.212 42.491  1.00 57.98  ? 487 GLY B O   1 
ATOM   3261 N  N   . ASN A 1 515 ? -33.143 -16.000 42.123  1.00 70.37  ? 488 ASN B N   1 
ATOM   3262 C  CA  . ASN A 1 515 ? -34.529 -15.949 42.566  1.00 68.93  ? 488 ASN B CA  1 
ATOM   3263 C  C   . ASN A 1 515 ? -35.423 -15.741 41.364  1.00 64.46  ? 488 ASN B C   1 
ATOM   3264 O  O   . ASN A 1 515 ? -34.928 -15.576 40.244  1.00 69.36  ? 488 ASN B O   1 
ATOM   3265 C  CB  . ASN A 1 515 ? -34.714 -14.818 43.545  1.00 72.83  ? 488 ASN B CB  1 
ATOM   3266 C  CG  . ASN A 1 515 ? -34.008 -15.058 44.866  1.00 79.12  ? 488 ASN B CG  1 
ATOM   3267 O  OD1 . ASN A 1 515 ? -33.945 -16.187 45.379  1.00 63.47  ? 488 ASN B OD1 1 
ATOM   3268 N  ND2 . ASN A 1 515 ? -33.485 -13.955 45.431  1.00 92.68  ? 488 ASN B ND2 1 
ATOM   3269 N  N   . TYR A 1 516 ? -36.732 -15.771 41.583  1.00 60.84  ? 489 TYR B N   1 
ATOM   3270 C  CA  . TYR A 1 516 ? -37.706 -15.593 40.490  1.00 59.32  ? 489 TYR B CA  1 
ATOM   3271 C  C   . TYR A 1 516 ? -38.640 -14.409 40.777  1.00 58.28  ? 489 TYR B C   1 
ATOM   3272 O  O   . TYR A 1 516 ? -39.061 -14.177 41.918  1.00 48.56  ? 489 TYR B O   1 
ATOM   3273 C  CB  . TYR A 1 516 ? -38.564 -16.855 40.270  1.00 55.50  ? 489 TYR B CB  1 
ATOM   3274 C  CG  . TYR A 1 516 ? -37.824 -18.106 39.843  1.00 56.46  ? 489 TYR B CG  1 
ATOM   3275 C  CD1 . TYR A 1 516 ? -37.183 -18.172 38.613  1.00 54.98  ? 489 TYR B CD1 1 
ATOM   3276 C  CD2 . TYR A 1 516 ? -37.785 -19.232 40.656  1.00 58.34  ? 489 TYR B CD2 1 
ATOM   3277 C  CE1 . TYR A 1 516 ? -36.510 -19.307 38.218  1.00 53.10  ? 489 TYR B CE1 1 
ATOM   3278 C  CE2 . TYR A 1 516 ? -37.110 -20.384 40.256  1.00 59.44  ? 489 TYR B CE2 1 
ATOM   3279 C  CZ  . TYR A 1 516 ? -36.480 -20.410 39.030  1.00 55.47  ? 489 TYR B CZ  1 
ATOM   3280 O  OH  . TYR A 1 516 ? -35.807 -21.531 38.612  1.00 53.90  ? 489 TYR B OH  1 
ATOM   3281 N  N   . SER A 1 517 ? -38.932 -13.649 39.733  1.00 54.88  ? 490 SER B N   1 
ATOM   3282 C  CA  . SER A 1 517 ? -40.029 -12.727 39.774  1.00 53.60  ? 490 SER B CA  1 
ATOM   3283 C  C   . SER A 1 517 ? -41.303 -13.480 39.384  1.00 55.79  ? 490 SER B C   1 
ATOM   3284 O  O   . SER A 1 517 ? -41.259 -14.442 38.621  1.00 54.08  ? 490 SER B O   1 
ATOM   3285 C  CB  . SER A 1 517 ? -39.785 -11.574 38.824  1.00 51.83  ? 490 SER B CB  1 
ATOM   3286 O  OG  . SER A 1 517 ? -38.966 -10.643 39.475  1.00 58.41  ? 490 SER B OG  1 
ATOM   3287 N  N   . ILE A 1 518 ? -42.434 -13.036 39.923  1.00 50.63  ? 491 ILE B N   1 
ATOM   3288 C  CA  . ILE A 1 518 ? -43.703 -13.548 39.524  1.00 47.08  ? 491 ILE B CA  1 
ATOM   3289 C  C   . ILE A 1 518 ? -44.495 -12.467 38.851  1.00 50.39  ? 491 ILE B C   1 
ATOM   3290 O  O   . ILE A 1 518 ? -44.751 -11.423 39.463  1.00 54.56  ? 491 ILE B O   1 
ATOM   3291 C  CB  . ILE A 1 518 ? -44.471 -14.068 40.707  1.00 46.57  ? 491 ILE B CB  1 
ATOM   3292 C  CG1 . ILE A 1 518 ? -43.602 -15.092 41.429  1.00 50.31  ? 491 ILE B CG1 1 
ATOM   3293 C  CG2 . ILE A 1 518 ? -45.764 -14.698 40.208  1.00 44.55  ? 491 ILE B CG2 1 
ATOM   3294 C  CD1 . ILE A 1 518 ? -44.230 -15.659 42.679  1.00 54.86  ? 491 ILE B CD1 1 
ATOM   3295 N  N   . ILE A 1 519 ? -44.877 -12.718 37.596  1.00 47.85  ? 492 ILE B N   1 
ATOM   3296 C  CA  . ILE A 1 519 ? -45.539 -11.710 36.789  1.00 49.90  ? 492 ILE B CA  1 
ATOM   3297 C  C   . ILE A 1 519 ? -46.955 -12.127 36.447  1.00 53.21  ? 492 ILE B C   1 
ATOM   3298 O  O   . ILE A 1 519 ? -47.274 -13.320 36.416  1.00 59.19  ? 492 ILE B O   1 
ATOM   3299 C  CB  . ILE A 1 519 ? -44.793 -11.420 35.488  1.00 52.21  ? 492 ILE B CB  1 
ATOM   3300 C  CG1 . ILE A 1 519 ? -44.540 -12.714 34.680  1.00 58.24  ? 492 ILE B CG1 1 
ATOM   3301 C  CG2 . ILE A 1 519 ? -43.497 -10.714 35.790  1.00 48.57  ? 492 ILE B CG2 1 
ATOM   3302 C  CD1 . ILE A 1 519 ? -44.221 -12.479 33.210  1.00 55.47  ? 492 ILE B CD1 1 
ATOM   3303 N  N   . ASN A 1 520 ? -47.813 -11.142 36.198  1.00 52.37  ? 493 ASN B N   1 
ATOM   3304 C  CA  . ASN A 1 520 ? -49.192 -11.422 35.813  1.00 53.16  ? 493 ASN B CA  1 
ATOM   3305 C  C   . ASN A 1 520 ? -49.467 -10.671 34.551  1.00 49.70  ? 493 ASN B C   1 
ATOM   3306 O  O   . ASN A 1 520 ? -48.952 -9.584  34.396  1.00 58.71  ? 493 ASN B O   1 
ATOM   3307 C  CB  . ASN A 1 520 ? -50.117 -10.990 36.929  1.00 57.06  ? 493 ASN B CB  1 
ATOM   3308 C  CG  . ASN A 1 520 ? -51.543 -11.411 36.720  1.00 62.15  ? 493 ASN B CG  1 
ATOM   3309 O  OD1 . ASN A 1 520 ? -51.871 -12.301 35.933  1.00 73.55  ? 493 ASN B OD1 1 
ATOM   3310 N  ND2 . ASN A 1 520 ? -52.408 -10.782 37.463  1.00 64.43  ? 493 ASN B ND2 1 
ATOM   3311 N  N   . TRP A 1 521 ? -50.217 -11.270 33.635  1.00 50.27  ? 494 TRP B N   1 
ATOM   3312 C  CA  . TRP A 1 521 ? -50.510 -10.656 32.325  1.00 55.34  ? 494 TRP B CA  1 
ATOM   3313 C  C   . TRP A 1 521 ? -51.733 -9.695  32.345  1.00 58.17  ? 494 TRP B C   1 
ATOM   3314 O  O   . TRP A 1 521 ? -52.880 -10.140 32.460  1.00 57.54  ? 494 TRP B O   1 
ATOM   3315 C  CB  . TRP A 1 521 ? -50.768 -11.765 31.308  1.00 56.72  ? 494 TRP B CB  1 
ATOM   3316 C  CG  . TRP A 1 521 ? -49.549 -12.537 30.880  1.00 52.00  ? 494 TRP B CG  1 
ATOM   3317 C  CD1 . TRP A 1 521 ? -48.378 -12.621 31.528  1.00 51.57  ? 494 TRP B CD1 1 
ATOM   3318 C  CD2 . TRP A 1 521 ? -49.431 -13.362 29.721  1.00 47.17  ? 494 TRP B CD2 1 
ATOM   3319 N  NE1 . TRP A 1 521 ? -47.507 -13.408 30.829  1.00 49.99  ? 494 TRP B NE1 1 
ATOM   3320 C  CE2 . TRP A 1 521 ? -48.135 -13.883 29.718  1.00 48.04  ? 494 TRP B CE2 1 
ATOM   3321 C  CE3 . TRP A 1 521 ? -50.297 -13.697 28.678  1.00 50.66  ? 494 TRP B CE3 1 
ATOM   3322 C  CZ2 . TRP A 1 521 ? -47.666 -14.733 28.716  1.00 50.91  ? 494 TRP B CZ2 1 
ATOM   3323 C  CZ3 . TRP A 1 521 ? -49.833 -14.533 27.671  1.00 55.16  ? 494 TRP B CZ3 1 
ATOM   3324 C  CH2 . TRP A 1 521 ? -48.522 -15.033 27.691  1.00 52.02  ? 494 TRP B CH2 1 
ATOM   3325 N  N   . HIS A 1 522 ? -51.479 -8.389  32.260  1.00 62.67  ? 495 HIS B N   1 
ATOM   3326 C  CA  . HIS A 1 522 ? -52.554 -7.366  32.177  1.00 66.00  ? 495 HIS B CA  1 
ATOM   3327 C  C   . HIS A 1 522 ? -52.626 -6.772  30.785  1.00 65.12  ? 495 HIS B C   1 
ATOM   3328 O  O   . HIS A 1 522 ? -51.718 -6.962  29.978  1.00 65.36  ? 495 HIS B O   1 
ATOM   3329 C  CB  . HIS A 1 522 ? -52.317 -6.189  33.123  1.00 60.84  ? 495 HIS B CB  1 
ATOM   3330 C  CG  . HIS A 1 522 ? -52.282 -6.544  34.571  1.00 57.80  ? 495 HIS B CG  1 
ATOM   3331 N  ND1 . HIS A 1 522 ? -52.686 -7.761  35.061  1.00 63.92  ? 495 HIS B ND1 1 
ATOM   3332 C  CD2 . HIS A 1 522 ? -51.903 -5.815  35.646  1.00 65.66  ? 495 HIS B CD2 1 
ATOM   3333 C  CE1 . HIS A 1 522 ? -52.555 -7.770  36.377  1.00 65.81  ? 495 HIS B CE1 1 
ATOM   3334 N  NE2 . HIS A 1 522 ? -52.079 -6.602  36.757  1.00 65.20  ? 495 HIS B NE2 1 
ATOM   3335 N  N   . LEU A 1 523 ? -53.699 -6.025  30.528  1.00 73.94  ? 496 LEU B N   1 
ATOM   3336 C  CA  . LEU A 1 523 ? -53.870 -5.298  29.263  1.00 75.41  ? 496 LEU B CA  1 
ATOM   3337 C  C   . LEU A 1 523 ? -53.629 -3.830  29.512  1.00 76.11  ? 496 LEU B C   1 
ATOM   3338 O  O   . LEU A 1 523 ? -54.219 -3.263  30.414  1.00 72.86  ? 496 LEU B O   1 
ATOM   3339 C  CB  . LEU A 1 523 ? -55.276 -5.478  28.716  1.00 71.79  ? 496 LEU B CB  1 
ATOM   3340 C  CG  . LEU A 1 523 ? -55.296 -6.101  27.328  1.00 81.67  ? 496 LEU B CG  1 
ATOM   3341 C  CD1 . LEU A 1 523 ? -56.719 -6.351  26.857  1.00 84.56  ? 496 LEU B CD1 1 
ATOM   3342 C  CD2 . LEU A 1 523 ? -54.565 -5.225  26.335  1.00 87.19  ? 496 LEU B CD2 1 
ATOM   3343 N  N   . SER A 1 524 ? -52.740 -3.223  28.742  1.00 82.58  ? 497 SER B N   1 
ATOM   3344 C  CA  . SER A 1 524 ? -52.543 -1.777  28.816  1.00 93.48  ? 497 SER B CA  1 
ATOM   3345 C  C   . SER A 1 524 ? -53.825 -1.097  28.305  1.00 92.33  ? 497 SER B C   1 
ATOM   3346 O  O   . SER A 1 524 ? -54.287 -1.412  27.210  1.00 87.07  ? 497 SER B O   1 
ATOM   3347 C  CB  . SER A 1 524 ? -51.332 -1.349  27.969  1.00 94.13  ? 497 SER B CB  1 
ATOM   3348 O  OG  . SER A 1 524 ? -50.847 -0.074  28.353  1.00 90.94  ? 497 SER B OG  1 
ATOM   3349 N  N   . PRO A 1 525 ? -54.424 -0.198  29.108  1.00 97.11  ? 498 PRO B N   1 
ATOM   3350 C  CA  . PRO A 1 525 ? -55.527 0.607   28.585  1.00 105.34 ? 498 PRO B CA  1 
ATOM   3351 C  C   . PRO A 1 525 ? -55.021 1.725   27.638  1.00 110.58 ? 498 PRO B C   1 
ATOM   3352 O  O   . PRO A 1 525 ? -55.755 2.159   26.738  1.00 102.09 ? 498 PRO B O   1 
ATOM   3353 C  CB  . PRO A 1 525 ? -56.165 1.182   29.852  1.00 100.01 ? 498 PRO B CB  1 
ATOM   3354 C  CG  . PRO A 1 525 ? -55.031 1.295   30.818  1.00 100.21 ? 498 PRO B CG  1 
ATOM   3355 C  CD  . PRO A 1 525 ? -54.104 0.153   30.508  1.00 102.42 ? 498 PRO B CD  1 
ATOM   3356 N  N   . GLU A 1 526 ? -53.775 2.166   27.850  1.00 109.53 ? 499 GLU B N   1 
ATOM   3357 C  CA  . GLU A 1 526 ? -53.110 3.133   26.977  1.00 105.42 ? 499 GLU B CA  1 
ATOM   3358 C  C   . GLU A 1 526 ? -52.815 2.525   25.605  1.00 111.21 ? 499 GLU B C   1 
ATOM   3359 O  O   . GLU A 1 526 ? -53.126 3.126   24.583  1.00 125.60 ? 499 GLU B O   1 
ATOM   3360 C  CB  . GLU A 1 526 ? -51.805 3.634   27.623  1.00 93.22  ? 499 GLU B CB  1 
ATOM   3361 N  N   . ASP A 1 527 ? -52.232 1.326   25.593  1.00 115.23 ? 500 ASP B N   1 
ATOM   3362 C  CA  . ASP A 1 527 ? -51.714 0.706   24.366  1.00 107.67 ? 500 ASP B CA  1 
ATOM   3363 C  C   . ASP A 1 527 ? -52.655 -0.346  23.740  1.00 101.91 ? 500 ASP B C   1 
ATOM   3364 O  O   . ASP A 1 527 ? -52.612 -0.586  22.531  1.00 98.58  ? 500 ASP B O   1 
ATOM   3365 C  CB  . ASP A 1 527 ? -50.350 0.066   24.675  1.00 103.70 ? 500 ASP B CB  1 
ATOM   3366 C  CG  . ASP A 1 527 ? -49.417 0.035   23.473  1.00 97.99  ? 500 ASP B CG  1 
ATOM   3367 O  OD1 . ASP A 1 527 ? -49.886 0.010   22.310  1.00 87.80  ? 500 ASP B OD1 1 
ATOM   3368 O  OD2 . ASP A 1 527 ? -48.190 0.028   23.711  1.00 98.50  ? 500 ASP B OD2 1 
ATOM   3369 N  N   . GLY A 1 528 ? -53.495 -0.977  24.553  1.00 94.02  ? 501 GLY B N   1 
ATOM   3370 C  CA  . GLY A 1 528 ? -54.220 -2.170  24.116  1.00 88.07  ? 501 GLY B CA  1 
ATOM   3371 C  C   . GLY A 1 528 ? -53.341 -3.424  24.082  1.00 87.74  ? 501 GLY B C   1 
ATOM   3372 O  O   . GLY A 1 528 ? -53.796 -4.492  23.668  1.00 92.34  ? 501 GLY B O   1 
ATOM   3373 N  N   . SER A 1 529 ? -52.090 -3.314  24.532  1.00 82.20  ? 502 SER B N   1 
ATOM   3374 C  CA  . SER A 1 529 ? -51.137 -4.418  24.479  1.00 79.07  ? 502 SER B CA  1 
ATOM   3375 C  C   . SER A 1 529 ? -50.961 -5.021  25.870  1.00 78.97  ? 502 SER B C   1 
ATOM   3376 O  O   . SER A 1 529 ? -51.296 -4.404  26.887  1.00 80.65  ? 502 SER B O   1 
ATOM   3377 C  CB  . SER A 1 529 ? -49.778 -3.946  23.958  1.00 80.80  ? 502 SER B CB  1 
ATOM   3378 O  OG  . SER A 1 529 ? -49.027 -3.302  24.982  1.00 87.28  ? 502 SER B OG  1 
ATOM   3379 N  N   . ILE A 1 530 ? -50.411 -6.229  25.901  1.00 72.93  ? 503 ILE B N   1 
ATOM   3380 C  CA  . ILE A 1 530 ? -50.239 -6.980  27.139  1.00 71.10  ? 503 ILE B CA  1 
ATOM   3381 C  C   . ILE A 1 530 ? -49.046 -6.477  27.947  1.00 62.24  ? 503 ILE B C   1 
ATOM   3382 O  O   . ILE A 1 530 ? -48.022 -6.090  27.406  1.00 64.69  ? 503 ILE B O   1 
ATOM   3383 C  CB  . ILE A 1 530 ? -50.119 -8.488  26.846  1.00 75.38  ? 503 ILE B CB  1 
ATOM   3384 C  CG1 . ILE A 1 530 ? -51.442 -8.999  26.277  1.00 74.77  ? 503 ILE B CG1 1 
ATOM   3385 C  CG2 . ILE A 1 530 ? -49.798 -9.275  28.106  1.00 77.79  ? 503 ILE B CG2 1 
ATOM   3386 C  CD1 . ILE A 1 530 ? -51.293 -10.223 25.415  1.00 77.87  ? 503 ILE B CD1 1 
ATOM   3387 N  N   . VAL A 1 531 ? -49.207 -6.471  29.257  1.00 58.45  ? 504 VAL B N   1 
ATOM   3388 C  CA  . VAL A 1 531 ? -48.245 -5.871  30.162  1.00 58.81  ? 504 VAL B CA  1 
ATOM   3389 C  C   . VAL A 1 531 ? -47.885 -6.885  31.245  1.00 60.10  ? 504 VAL B C   1 
ATOM   3390 O  O   . VAL A 1 531 ? -48.764 -7.392  31.960  1.00 58.60  ? 504 VAL B O   1 
ATOM   3391 C  CB  . VAL A 1 531 ? -48.883 -4.653  30.839  1.00 59.35  ? 504 VAL B CB  1 
ATOM   3392 C  CG1 . VAL A 1 531 ? -47.893 -3.950  31.753  1.00 60.69  ? 504 VAL B CG1 1 
ATOM   3393 C  CG2 . VAL A 1 531 ? -49.432 -3.707  29.793  1.00 63.46  ? 504 VAL B CG2 1 
ATOM   3394 N  N   . PHE A 1 532 ? -46.606 -7.163  31.400  1.00 56.10  ? 505 PHE B N   1 
ATOM   3395 C  CA  . PHE A 1 532 ? -46.199 -8.140  32.385  1.00 58.22  ? 505 PHE B CA  1 
ATOM   3396 C  C   . PHE A 1 532 ? -46.037 -7.472  33.735  1.00 54.54  ? 505 PHE B C   1 
ATOM   3397 O  O   . PHE A 1 532 ? -44.951 -7.040  34.086  1.00 55.56  ? 505 PHE B O   1 
ATOM   3398 C  CB  . PHE A 1 532 ? -44.912 -8.859  31.940  1.00 60.38  ? 505 PHE B CB  1 
ATOM   3399 C  CG  . PHE A 1 532 ? -45.031 -9.491  30.590  1.00 61.18  ? 505 PHE B CG  1 
ATOM   3400 C  CD1 . PHE A 1 532 ? -46.140 -10.258 30.278  1.00 57.28  ? 505 PHE B CD1 1 
ATOM   3401 C  CD2 . PHE A 1 532 ? -44.067 -9.277  29.613  1.00 62.27  ? 505 PHE B CD2 1 
ATOM   3402 C  CE1 . PHE A 1 532 ? -46.264 -10.828 29.028  1.00 60.52  ? 505 PHE B CE1 1 
ATOM   3403 C  CE2 . PHE A 1 532 ? -44.189 -9.849  28.354  1.00 59.97  ? 505 PHE B CE2 1 
ATOM   3404 C  CZ  . PHE A 1 532 ? -45.289 -10.615 28.058  1.00 57.80  ? 505 PHE B CZ  1 
ATOM   3405 N  N   . LYS A 1 533 ? -47.120 -7.431  34.499  1.00 53.73  ? 506 LYS B N   1 
ATOM   3406 C  CA  . LYS A 1 533 ? -47.143 -6.760  35.790  1.00 57.22  ? 506 LYS B CA  1 
ATOM   3407 C  C   . LYS A 1 533 ? -46.414 -7.669  36.766  1.00 51.62  ? 506 LYS B C   1 
ATOM   3408 O  O   . LYS A 1 533 ? -46.737 -8.848  36.815  1.00 48.62  ? 506 LYS B O   1 
ATOM   3409 C  CB  . LYS A 1 533 ? -48.615 -6.515  36.223  1.00 64.28  ? 506 LYS B CB  1 
ATOM   3410 C  CG  . LYS A 1 533 ? -48.876 -5.255  37.045  1.00 76.73  ? 506 LYS B CG  1 
ATOM   3411 C  CD  . LYS A 1 533 ? -47.943 -5.167  38.254  1.00 94.33  ? 506 LYS B CD  1 
ATOM   3412 C  CE  . LYS A 1 533 ? -48.340 -4.091  39.262  1.00 103.15 ? 506 LYS B CE  1 
ATOM   3413 N  NZ  . LYS A 1 533 ? -48.597 -2.762  38.632  1.00 101.87 ? 506 LYS B NZ  1 
ATOM   3414 N  N   . GLU A 1 534 ? -45.415 -7.142  37.494  1.00 55.90  ? 507 GLU B N   1 
ATOM   3415 C  CA  . GLU A 1 534 ? -44.767 -7.871  38.626  1.00 60.82  ? 507 GLU B CA  1 
ATOM   3416 C  C   . GLU A 1 534 ? -45.694 -7.862  39.855  1.00 55.85  ? 507 GLU B C   1 
ATOM   3417 O  O   . GLU A 1 534 ? -46.159 -6.800  40.290  1.00 57.72  ? 507 GLU B O   1 
ATOM   3418 C  CB  . GLU A 1 534 ? -43.370 -7.299  38.990  1.00 65.76  ? 507 GLU B CB  1 
ATOM   3419 C  CG  . GLU A 1 534 ? -42.295 -7.461  37.891  1.00 80.43  ? 507 GLU B CG  1 
ATOM   3420 C  CD  . GLU A 1 534 ? -40.816 -7.312  38.351  1.00 91.87  ? 507 GLU B CD  1 
ATOM   3421 O  OE1 . GLU A 1 534 ? -40.429 -6.240  38.886  1.00 101.63 ? 507 GLU B OE1 1 
ATOM   3422 O  OE2 . GLU A 1 534 ? -40.007 -8.254  38.129  1.00 79.14  ? 507 GLU B OE2 1 
ATOM   3423 N  N   . VAL A 1 535 ? -45.983 -9.044  40.391  1.00 52.91  ? 508 VAL B N   1 
ATOM   3424 C  CA  . VAL A 1 535 ? -46.931 -9.173  41.504  1.00 52.88  ? 508 VAL B CA  1 
ATOM   3425 C  C   . VAL A 1 535 ? -46.399 -9.974  42.702  1.00 51.78  ? 508 VAL B C   1 
ATOM   3426 O  O   . VAL A 1 535 ? -47.155 -10.314 43.608  1.00 51.55  ? 508 VAL B O   1 
ATOM   3427 C  CB  . VAL A 1 535 ? -48.269 -9.797  41.037  1.00 56.72  ? 508 VAL B CB  1 
ATOM   3428 C  CG1 . VAL A 1 535 ? -48.827 -9.043  39.839  1.00 58.01  ? 508 VAL B CG1 1 
ATOM   3429 C  CG2 . VAL A 1 535 ? -48.112 -11.267 40.694  1.00 55.49  ? 508 VAL B CG2 1 
ATOM   3430 N  N   . GLY A 1 536 ? -45.100 -10.263 42.721  1.00 53.57  ? 509 GLY B N   1 
ATOM   3431 C  CA  . GLY A 1 536 ? -44.485 -11.017 43.830  1.00 50.18  ? 509 GLY B CA  1 
ATOM   3432 C  C   . GLY A 1 536 ? -43.120 -11.566 43.452  1.00 49.93  ? 509 GLY B C   1 
ATOM   3433 O  O   . GLY A 1 536 ? -42.590 -11.258 42.416  1.00 48.28  ? 509 GLY B O   1 
ATOM   3434 N  N   . TYR A 1 537 ? -42.534 -12.386 44.298  1.00 51.98  ? 510 TYR B N   1 
ATOM   3435 C  CA  . TYR A 1 537 ? -41.260 -12.977 43.968  1.00 49.68  ? 510 TYR B CA  1 
ATOM   3436 C  C   . TYR A 1 537 ? -41.151 -14.249 44.741  1.00 45.26  ? 510 TYR B C   1 
ATOM   3437 O  O   . TYR A 1 537 ? -41.899 -14.431 45.677  1.00 46.06  ? 510 TYR B O   1 
ATOM   3438 C  CB  . TYR A 1 537 ? -40.092 -12.016 44.285  1.00 55.72  ? 510 TYR B CB  1 
ATOM   3439 C  CG  . TYR A 1 537 ? -40.016 -11.523 45.710  1.00 58.46  ? 510 TYR B CG  1 
ATOM   3440 C  CD1 . TYR A 1 537 ? -40.703 -10.370 46.096  1.00 60.10  ? 510 TYR B CD1 1 
ATOM   3441 C  CD2 . TYR A 1 537 ? -39.235 -12.186 46.677  1.00 63.54  ? 510 TYR B CD2 1 
ATOM   3442 C  CE1 . TYR A 1 537 ? -40.640 -9.894  47.390  1.00 60.86  ? 510 TYR B CE1 1 
ATOM   3443 C  CE2 . TYR A 1 537 ? -39.168 -11.710 47.989  1.00 65.72  ? 510 TYR B CE2 1 
ATOM   3444 C  CZ  . TYR A 1 537 ? -39.882 -10.558 48.331  1.00 63.19  ? 510 TYR B CZ  1 
ATOM   3445 O  OH  . TYR A 1 537 ? -39.869 -10.050 49.600  1.00 63.00  ? 510 TYR B OH  1 
ATOM   3446 N  N   . TYR A 1 538 ? -40.250 -15.130 44.322  1.00 45.38  ? 511 TYR B N   1 
ATOM   3447 C  CA  . TYR A 1 538 ? -39.935 -16.365 45.040  1.00 51.02  ? 511 TYR B CA  1 
ATOM   3448 C  C   . TYR A 1 538 ? -38.460 -16.417 45.418  1.00 54.17  ? 511 TYR B C   1 
ATOM   3449 O  O   . TYR A 1 538 ? -37.607 -16.391 44.535  1.00 54.50  ? 511 TYR B O   1 
ATOM   3450 C  CB  . TYR A 1 538 ? -40.234 -17.538 44.135  1.00 49.65  ? 511 TYR B CB  1 
ATOM   3451 C  CG  . TYR A 1 538 ? -40.192 -18.892 44.794  1.00 46.60  ? 511 TYR B CG  1 
ATOM   3452 C  CD1 . TYR A 1 538 ? -41.222 -19.314 45.587  1.00 44.76  ? 511 TYR B CD1 1 
ATOM   3453 C  CD2 . TYR A 1 538 ? -39.150 -19.779 44.544  1.00 46.61  ? 511 TYR B CD2 1 
ATOM   3454 C  CE1 . TYR A 1 538 ? -41.198 -20.562 46.164  1.00 47.45  ? 511 TYR B CE1 1 
ATOM   3455 C  CE2 . TYR A 1 538 ? -39.121 -21.034 45.111  1.00 43.42  ? 511 TYR B CE2 1 
ATOM   3456 C  CZ  . TYR A 1 538 ? -40.148 -21.412 45.922  1.00 42.79  ? 511 TYR B CZ  1 
ATOM   3457 O  OH  . TYR A 1 538 ? -40.147 -22.643 46.489  1.00 42.20  ? 511 TYR B OH  1 
ATOM   3458 N  N   . ASN A 1 539 ? -38.166 -16.472 46.718  1.00 60.57  ? 512 ASN B N   1 
ATOM   3459 C  CA  . ASN A 1 539 ? -36.781 -16.526 47.223  1.00 58.27  ? 512 ASN B CA  1 
ATOM   3460 C  C   . ASN A 1 539 ? -36.463 -17.980 47.427  1.00 59.86  ? 512 ASN B C   1 
ATOM   3461 O  O   . ASN A 1 539 ? -37.035 -18.639 48.321  1.00 65.57  ? 512 ASN B O   1 
ATOM   3462 C  CB  . ASN A 1 539 ? -36.628 -15.784 48.560  1.00 65.56  ? 512 ASN B CB  1 
ATOM   3463 C  CG  . ASN A 1 539 ? -36.450 -14.266 48.402  1.00 71.15  ? 512 ASN B CG  1 
ATOM   3464 O  OD1 . ASN A 1 539 ? -36.414 -13.716 47.290  1.00 71.25  ? 512 ASN B OD1 1 
ATOM   3465 N  ND2 . ASN A 1 539 ? -36.332 -13.583 49.543  1.00 75.68  ? 512 ASN B ND2 1 
ATOM   3466 N  N   . VAL A 1 540 ? -35.564 -18.498 46.596  1.00 58.47  ? 513 VAL B N   1 
ATOM   3467 C  CA  . VAL A 1 540 ? -35.410 -19.948 46.467  1.00 54.86  ? 513 VAL B CA  1 
ATOM   3468 C  C   . VAL A 1 540 ? -34.882 -20.625 47.715  1.00 58.39  ? 513 VAL B C   1 
ATOM   3469 O  O   . VAL A 1 540 ? -35.304 -21.737 48.051  1.00 52.94  ? 513 VAL B O   1 
ATOM   3470 C  CB  . VAL A 1 540 ? -34.492 -20.289 45.307  1.00 56.68  ? 513 VAL B CB  1 
ATOM   3471 C  CG1 . VAL A 1 540 ? -34.225 -21.794 45.242  1.00 55.66  ? 513 VAL B CG1 1 
ATOM   3472 C  CG2 . VAL A 1 540 ? -35.127 -19.782 44.018  1.00 60.43  ? 513 VAL B CG2 1 
ATOM   3473 N  N   . TYR A 1 541 ? -33.972 -19.947 48.409  1.00 72.44  ? 514 TYR B N   1 
ATOM   3474 C  CA  . TYR A 1 541 ? -33.344 -20.499 49.622  1.00 81.55  ? 514 TYR B CA  1 
ATOM   3475 C  C   . TYR A 1 541 ? -33.847 -19.816 50.905  1.00 87.26  ? 514 TYR B C   1 
ATOM   3476 O  O   . TYR A 1 541 ? -33.349 -18.773 51.342  1.00 95.95  ? 514 TYR B O   1 
ATOM   3477 C  CB  . TYR A 1 541 ? -31.822 -20.448 49.479  1.00 81.49  ? 514 TYR B CB  1 
ATOM   3478 C  CG  . TYR A 1 541 ? -31.319 -21.441 48.441  1.00 79.90  ? 514 TYR B CG  1 
ATOM   3479 C  CD1 . TYR A 1 541 ? -30.942 -21.030 47.165  1.00 79.41  ? 514 TYR B CD1 1 
ATOM   3480 C  CD2 . TYR A 1 541 ? -31.274 -22.800 48.729  1.00 84.19  ? 514 TYR B CD2 1 
ATOM   3481 C  CE1 . TYR A 1 541 ? -30.505 -21.944 46.219  1.00 82.64  ? 514 TYR B CE1 1 
ATOM   3482 C  CE2 . TYR A 1 541 ? -30.838 -23.720 47.796  1.00 86.36  ? 514 TYR B CE2 1 
ATOM   3483 C  CZ  . TYR A 1 541 ? -30.447 -23.290 46.546  1.00 87.09  ? 514 TYR B CZ  1 
ATOM   3484 O  OH  . TYR A 1 541 ? -30.015 -24.227 45.630  1.00 93.81  ? 514 TYR B OH  1 
ATOM   3485 N  N   . ALA A 1 542 ? -34.863 -20.428 51.489  1.00 80.36  ? 515 ALA B N   1 
ATOM   3486 C  CA  . ALA A 1 542 ? -35.557 -19.856 52.594  1.00 81.52  ? 515 ALA B CA  1 
ATOM   3487 C  C   . ALA A 1 542 ? -36.453 -20.951 53.139  1.00 90.93  ? 515 ALA B C   1 
ATOM   3488 O  O   . ALA A 1 542 ? -36.825 -21.898 52.407  1.00 82.01  ? 515 ALA B O   1 
ATOM   3489 C  CB  . ALA A 1 542 ? -36.370 -18.666 52.126  1.00 87.13  ? 515 ALA B CB  1 
ATOM   3490 N  N   . LYS A 1 543 ? -36.793 -20.818 54.420  1.00 98.31  ? 516 LYS B N   1 
ATOM   3491 C  CA  . LYS A 1 543 ? -37.531 -21.854 55.147  1.00 102.39 ? 516 LYS B CA  1 
ATOM   3492 C  C   . LYS A 1 543 ? -38.958 -21.998 54.618  1.00 97.26  ? 516 LYS B C   1 
ATOM   3493 O  O   . LYS A 1 543 ? -39.691 -21.008 54.536  1.00 96.05  ? 516 LYS B O   1 
ATOM   3494 C  CB  . LYS A 1 543 ? -37.543 -21.538 56.649  1.00 103.67 ? 516 LYS B CB  1 
ATOM   3495 N  N   . LYS A 1 544 ? -39.332 -23.231 54.260  1.00 97.70  ? 517 LYS B N   1 
ATOM   3496 C  CA  . LYS A 1 544 ? -40.649 -23.541 53.672  1.00 106.16 ? 517 LYS B CA  1 
ATOM   3497 C  C   . LYS A 1 544 ? -41.774 -22.731 54.308  1.00 103.17 ? 517 LYS B C   1 
ATOM   3498 O  O   . LYS A 1 544 ? -42.011 -22.829 55.506  1.00 106.69 ? 517 LYS B O   1 
ATOM   3499 C  CB  . LYS A 1 544 ? -40.963 -25.041 53.805  1.00 108.20 ? 517 LYS B CB  1 
ATOM   3500 N  N   . GLY A 1 545 ? -42.463 -21.930 53.503  1.00 105.29 ? 518 GLY B N   1 
ATOM   3501 C  CA  . GLY A 1 545 ? -43.488 -21.025 54.027  1.00 96.06  ? 518 GLY B CA  1 
ATOM   3502 C  C   . GLY A 1 545 ? -42.997 -19.598 54.172  1.00 88.86  ? 518 GLY B C   1 
ATOM   3503 O  O   . GLY A 1 545 ? -43.786 -18.703 54.440  1.00 92.21  ? 518 GLY B O   1 
ATOM   3504 N  N   . GLU A 1 546 ? -41.699 -19.370 53.997  1.00 84.72  ? 519 GLU B N   1 
ATOM   3505 C  CA  . GLU A 1 546 ? -41.173 -18.012 53.940  1.00 79.01  ? 519 GLU B CA  1 
ATOM   3506 C  C   . GLU A 1 546 ? -40.418 -17.760 52.619  1.00 80.99  ? 519 GLU B C   1 
ATOM   3507 O  O   . GLU A 1 546 ? -39.471 -16.958 52.591  1.00 80.20  ? 519 GLU B O   1 
ATOM   3508 C  CB  . GLU A 1 546 ? -40.280 -17.745 55.157  1.00 76.52  ? 519 GLU B CB  1 
ATOM   3509 N  N   . ARG A 1 547 ? -40.845 -18.424 51.529  1.00 77.94  ? 520 ARG B N   1 
ATOM   3510 C  CA  . ARG A 1 547 ? -40.183 -18.292 50.199  1.00 71.31  ? 520 ARG B CA  1 
ATOM   3511 C  C   . ARG A 1 547 ? -40.969 -17.491 49.175  1.00 63.63  ? 520 ARG B C   1 
ATOM   3512 O  O   . ARG A 1 547 ? -40.402 -16.815 48.312  1.00 57.56  ? 520 ARG B O   1 
ATOM   3513 C  CB  . ARG A 1 547 ? -40.002 -19.652 49.566  1.00 71.90  ? 520 ARG B CB  1 
ATOM   3514 C  CG  . ARG A 1 547 ? -39.079 -20.602 50.265  1.00 72.34  ? 520 ARG B CG  1 
ATOM   3515 C  CD  . ARG A 1 547 ? -39.572 -21.997 49.933  1.00 81.36  ? 520 ARG B CD  1 
ATOM   3516 N  NE  . ARG A 1 547 ? -38.840 -23.063 50.611  1.00 93.08  ? 520 ARG B NE  1 
ATOM   3517 C  CZ  . ARG A 1 547 ? -39.175 -24.347 50.528  1.00 92.10  ? 520 ARG B CZ  1 
ATOM   3518 N  NH1 . ARG A 1 547 ? -40.224 -24.723 49.785  1.00 82.07  ? 520 ARG B NH1 1 
ATOM   3519 N  NH2 . ARG A 1 547 ? -38.468 -25.250 51.196  1.00 93.43  ? 520 ARG B NH2 1 
ATOM   3520 N  N   . LEU A 1 548 ? -42.281 -17.618 49.253  1.00 61.11  ? 521 LEU B N   1 
ATOM   3521 C  CA  . LEU A 1 548 ? -43.205 -16.984 48.319  1.00 62.58  ? 521 LEU B CA  1 
ATOM   3522 C  C   . LEU A 1 548 ? -43.769 -15.682 48.865  1.00 60.85  ? 521 LEU B C   1 
ATOM   3523 O  O   . LEU A 1 548 ? -44.299 -15.644 49.969  1.00 59.82  ? 521 LEU B O   1 
ATOM   3524 C  CB  . LEU A 1 548 ? -44.352 -17.944 48.084  1.00 61.38  ? 521 LEU B CB  1 
ATOM   3525 C  CG  . LEU A 1 548 ? -45.407 -17.652 47.051  1.00 62.74  ? 521 LEU B CG  1 
ATOM   3526 C  CD1 . LEU A 1 548 ? -44.809 -17.301 45.686  1.00 58.27  ? 521 LEU B CD1 1 
ATOM   3527 C  CD2 . LEU A 1 548 ? -46.258 -18.919 47.010  1.00 66.45  ? 521 LEU B CD2 1 
ATOM   3528 N  N   . PHE A 1 549 ? -43.665 -14.623 48.077  1.00 63.67  ? 522 PHE B N   1 
ATOM   3529 C  CA  . PHE A 1 549 ? -44.171 -13.321 48.459  1.00 67.63  ? 522 PHE B CA  1 
ATOM   3530 C  C   . PHE A 1 549 ? -45.007 -12.808 47.310  1.00 69.15  ? 522 PHE B C   1 
ATOM   3531 O  O   . PHE A 1 549 ? -44.483 -12.588 46.219  1.00 69.17  ? 522 PHE B O   1 
ATOM   3532 C  CB  . PHE A 1 549 ? -43.010 -12.371 48.766  1.00 73.72  ? 522 PHE B CB  1 
ATOM   3533 C  CG  . PHE A 1 549 ? -42.131 -12.844 49.903  1.00 85.54  ? 522 PHE B CG  1 
ATOM   3534 C  CD1 . PHE A 1 549 ? -41.121 -13.776 49.685  1.00 86.78  ? 522 PHE B CD1 1 
ATOM   3535 C  CD2 . PHE A 1 549 ? -42.336 -12.383 51.203  1.00 91.27  ? 522 PHE B CD2 1 
ATOM   3536 C  CE1 . PHE A 1 549 ? -40.327 -14.224 50.734  1.00 93.14  ? 522 PHE B CE1 1 
ATOM   3537 C  CE2 . PHE A 1 549 ? -41.548 -12.833 52.255  1.00 94.01  ? 522 PHE B CE2 1 
ATOM   3538 C  CZ  . PHE A 1 549 ? -40.539 -13.753 52.019  1.00 95.47  ? 522 PHE B CZ  1 
ATOM   3539 N  N   . ILE A 1 550 ? -46.307 -12.648 47.548  1.00 68.79  ? 523 ILE B N   1 
ATOM   3540 C  CA  . ILE A 1 550 ? -47.248 -12.238 46.504  1.00 71.69  ? 523 ILE B CA  1 
ATOM   3541 C  C   . ILE A 1 550 ? -48.139 -11.091 46.969  1.00 64.24  ? 523 ILE B C   1 
ATOM   3542 O  O   . ILE A 1 550 ? -48.588 -11.074 48.111  1.00 73.54  ? 523 ILE B O   1 
ATOM   3543 C  CB  . ILE A 1 550 ? -48.123 -13.437 46.055  1.00 74.59  ? 523 ILE B CB  1 
ATOM   3544 C  CG1 . ILE A 1 550 ? -47.267 -14.457 45.318  1.00 79.27  ? 523 ILE B CG1 1 
ATOM   3545 C  CG2 . ILE A 1 550 ? -49.253 -12.997 45.136  1.00 82.73  ? 523 ILE B CG2 1 
ATOM   3546 C  CD1 . ILE A 1 550 ? -48.047 -15.638 44.782  1.00 83.22  ? 523 ILE B CD1 1 
ATOM   3547 N  N   . ASN A 1 551 ? -48.404 -10.152 46.066  1.00 60.70  ? 524 ASN B N   1 
ATOM   3548 C  CA  . ASN A 1 551 ? -49.424 -9.120  46.269  1.00 61.42  ? 524 ASN B CA  1 
ATOM   3549 C  C   . ASN A 1 551 ? -50.763 -9.418  45.598  1.00 57.71  ? 524 ASN B C   1 
ATOM   3550 O  O   . ASN A 1 551 ? -51.036 -8.921  44.512  1.00 56.99  ? 524 ASN B O   1 
ATOM   3551 C  CB  . ASN A 1 551 ? -48.921 -7.796  45.730  1.00 68.67  ? 524 ASN B CB  1 
ATOM   3552 C  CG  . ASN A 1 551 ? -47.673 -7.321  46.430  1.00 78.31  ? 524 ASN B CG  1 
ATOM   3553 O  OD1 . ASN A 1 551 ? -47.214 -7.921  47.411  1.00 76.74  ? 524 ASN B OD1 1 
ATOM   3554 N  ND2 . ASN A 1 551 ? -47.111 -6.227  45.925  1.00 83.17  ? 524 ASN B ND2 1 
ATOM   3555 N  N   . GLU A 1 552 ? -51.616 -10.177 46.276  1.00 62.24  ? 525 GLU B N   1 
ATOM   3556 C  CA  . GLU A 1 552 ? -52.968 -10.527 45.784  1.00 67.60  ? 525 GLU B CA  1 
ATOM   3557 C  C   . GLU A 1 552 ? -53.745 -9.339  45.199  1.00 67.62  ? 525 GLU B C   1 
ATOM   3558 O  O   . GLU A 1 552 ? -54.450 -9.494  44.197  1.00 64.16  ? 525 GLU B O   1 
ATOM   3559 C  CB  . GLU A 1 552 ? -53.834 -11.112 46.910  1.00 70.42  ? 525 GLU B CB  1 
ATOM   3560 C  CG  . GLU A 1 552 ? -53.413 -12.447 47.482  1.00 72.53  ? 525 GLU B CG  1 
ATOM   3561 C  CD  . GLU A 1 552 ? -52.517 -12.319 48.685  1.00 73.43  ? 525 GLU B CD  1 
ATOM   3562 O  OE1 . GLU A 1 552 ? -51.799 -11.317 48.786  1.00 75.64  ? 525 GLU B OE1 1 
ATOM   3563 O  OE2 . GLU A 1 552 ? -52.504 -13.245 49.513  1.00 89.83  ? 525 GLU B OE2 1 
ATOM   3564 N  N   . GLU A 1 553 ? -53.646 -8.173  45.849  1.00 65.23  ? 526 GLU B N   1 
ATOM   3565 C  CA  . GLU A 1 553 ? -54.287 -6.948  45.351  1.00 65.40  ? 526 GLU B CA  1 
ATOM   3566 C  C   . GLU A 1 553 ? -53.942 -6.662  43.893  1.00 62.44  ? 526 GLU B C   1 
ATOM   3567 O  O   . GLU A 1 553 ? -54.760 -6.112  43.156  1.00 62.41  ? 526 GLU B O   1 
ATOM   3568 C  CB  . GLU A 1 553 ? -53.950 -5.709  46.209  1.00 65.53  ? 526 GLU B CB  1 
ATOM   3569 C  CG  . GLU A 1 553 ? -52.472 -5.357  46.341  1.00 73.70  ? 526 GLU B CG  1 
ATOM   3570 C  CD  . GLU A 1 553 ? -51.802 -5.982  47.569  1.00 83.12  ? 526 GLU B CD  1 
ATOM   3571 O  OE1 . GLU A 1 553 ? -52.419 -6.819  48.257  1.00 84.55  ? 526 GLU B OE1 1 
ATOM   3572 O  OE2 . GLU A 1 553 ? -50.639 -5.636  47.861  1.00 92.91  ? 526 GLU B OE2 1 
ATOM   3573 N  N   . LYS A 1 554 ? -52.743 -7.044  43.472  1.00 55.33  ? 527 LYS B N   1 
ATOM   3574 C  CA  . LYS A 1 554 ? -52.284 -6.661  42.162  1.00 54.96  ? 527 LYS B CA  1 
ATOM   3575 C  C   . LYS A 1 554 ? -52.741 -7.577  41.038  1.00 50.82  ? 527 LYS B C   1 
ATOM   3576 O  O   . LYS A 1 554 ? -52.537 -7.247  39.891  1.00 50.92  ? 527 LYS B O   1 
ATOM   3577 C  CB  . LYS A 1 554 ? -50.762 -6.522  42.172  1.00 59.04  ? 527 LYS B CB  1 
ATOM   3578 C  CG  . LYS A 1 554 ? -50.286 -5.149  42.600  1.00 61.12  ? 527 LYS B CG  1 
ATOM   3579 C  CD  . LYS A 1 554 ? -48.918 -5.201  43.247  1.00 67.05  ? 527 LYS B CD  1 
ATOM   3580 C  CE  . LYS A 1 554 ? -48.131 -3.916  43.015  1.00 73.47  ? 527 LYS B CE  1 
ATOM   3581 N  NZ  . LYS A 1 554 ? -47.166 -3.666  44.134  1.00 78.51  ? 527 LYS B NZ  1 
ATOM   3582 N  N   . ILE A 1 555 ? -53.372 -8.712  41.344  1.00 53.72  ? 528 ILE B N   1 
ATOM   3583 C  CA  . ILE A 1 555 ? -53.620 -9.753  40.326  1.00 49.42  ? 528 ILE B CA  1 
ATOM   3584 C  C   . ILE A 1 555 ? -54.963 -9.581  39.645  1.00 49.05  ? 528 ILE B C   1 
ATOM   3585 O  O   . ILE A 1 555 ? -55.961 -9.480  40.311  1.00 56.95  ? 528 ILE B O   1 
ATOM   3586 C  CB  . ILE A 1 555 ? -53.550 -11.180 40.936  1.00 48.74  ? 528 ILE B CB  1 
ATOM   3587 C  CG1 . ILE A 1 555 ? -52.153 -11.528 41.406  1.00 46.48  ? 528 ILE B CG1 1 
ATOM   3588 C  CG2 . ILE A 1 555 ? -53.925 -12.270 39.931  1.00 53.72  ? 528 ILE B CG2 1 
ATOM   3589 C  CD1 . ILE A 1 555 ? -52.141 -12.726 42.324  1.00 48.97  ? 528 ILE B CD1 1 
ATOM   3590 N  N   . LEU A 1 556 ? -54.973 -9.526  38.319  1.00 53.05  ? 529 LEU B N   1 
ATOM   3591 C  CA  . LEU A 1 556 ? -56.161 -9.773  37.504  1.00 55.53  ? 529 LEU B CA  1 
ATOM   3592 C  C   . LEU A 1 556 ? -56.254 -11.231 37.188  1.00 61.29  ? 529 LEU B C   1 
ATOM   3593 O  O   . LEU A 1 556 ? -55.322 -11.781 36.607  1.00 64.60  ? 529 LEU B O   1 
ATOM   3594 C  CB  . LEU A 1 556 ? -56.081 -9.032  36.163  1.00 60.49  ? 529 LEU B CB  1 
ATOM   3595 N  N   . TRP A 1 557 ? -57.378 -11.854 37.541  1.00 64.52  ? 530 TRP B N   1 
ATOM   3596 C  CA  . TRP A 1 557 ? -57.600 -13.282 37.280  1.00 64.49  ? 530 TRP B CA  1 
ATOM   3597 C  C   . TRP A 1 557 ? -58.173 -13.622 35.901  1.00 73.66  ? 530 TRP B C   1 
ATOM   3598 O  O   . TRP A 1 557 ? -58.092 -14.772 35.453  1.00 72.68  ? 530 TRP B O   1 
ATOM   3599 C  CB  . TRP A 1 557 ? -58.496 -13.852 38.359  1.00 63.64  ? 530 TRP B CB  1 
ATOM   3600 C  CG  . TRP A 1 557 ? -57.846 -13.857 39.709  1.00 65.19  ? 530 TRP B CG  1 
ATOM   3601 C  CD1 . TRP A 1 557 ? -58.134 -13.044 40.765  1.00 64.90  ? 530 TRP B CD1 1 
ATOM   3602 C  CD2 . TRP A 1 557 ? -56.790 -14.719 40.147  1.00 64.87  ? 530 TRP B CD2 1 
ATOM   3603 N  NE1 . TRP A 1 557 ? -57.330 -13.349 41.834  1.00 62.76  ? 530 TRP B NE1 1 
ATOM   3604 C  CE2 . TRP A 1 557 ? -56.496 -14.373 41.484  1.00 63.16  ? 530 TRP B CE2 1 
ATOM   3605 C  CE3 . TRP A 1 557 ? -56.061 -15.746 39.541  1.00 55.91  ? 530 TRP B CE3 1 
ATOM   3606 C  CZ2 . TRP A 1 557 ? -55.506 -15.023 42.221  1.00 65.23  ? 530 TRP B CZ2 1 
ATOM   3607 C  CZ3 . TRP A 1 557 ? -55.076 -16.382 40.276  1.00 56.76  ? 530 TRP B CZ3 1 
ATOM   3608 C  CH2 . TRP A 1 557 ? -54.815 -16.033 41.599  1.00 59.50  ? 530 TRP B CH2 1 
ATOM   3609 N  N   . SER A 1 558 ? -58.788 -12.628 35.263  1.00 90.08  ? 531 SER B N   1 
ATOM   3610 C  CA  . SER A 1 558 ? -59.132 -12.655 33.823  1.00 95.34  ? 531 SER B CA  1 
ATOM   3611 C  C   . SER A 1 558 ? -58.255 -11.700 32.990  1.00 96.82  ? 531 SER B C   1 
ATOM   3612 O  O   . SER A 1 558 ? -58.359 -11.712 31.759  1.00 90.22  ? 531 SER B O   1 
ATOM   3613 C  CB  . SER A 1 558 ? -60.604 -12.256 33.606  1.00 95.52  ? 531 SER B CB  1 
ATOM   3614 O  OG  . SER A 1 558 ? -60.784 -10.831 33.585  1.00 85.49  ? 531 SER B OG  1 
ATOM   3615 N  N   . GLY A 1 559 ? -57.455 -10.853 33.662  1.00 99.51  ? 532 GLY B N   1 
ATOM   3616 C  CA  . GLY A 1 559 ? -56.527 -9.918  33.008  1.00 97.00  ? 532 GLY B CA  1 
ATOM   3617 C  C   . GLY A 1 559 ? -57.009 -8.495  32.727  1.00 105.18 ? 532 GLY B C   1 
ATOM   3618 O  O   . GLY A 1 559 ? -56.211 -7.655  32.305  1.00 104.00 ? 532 GLY B O   1 
ATOM   3619 N  N   . PHE A 1 560 ? -58.296 -8.211  32.957  1.00 115.01 ? 533 PHE B N   1 
ATOM   3620 C  CA  . PHE A 1 560 ? -58.911 -6.921  32.569  1.00 103.24 ? 533 PHE B CA  1 
ATOM   3621 C  C   . PHE A 1 560 ? -59.414 -6.094  33.784  1.00 102.34 ? 533 PHE B C   1 
ATOM   3622 O  O   . PHE A 1 560 ? -60.170 -6.598  34.623  1.00 102.25 ? 533 PHE B O   1 
ATOM   3623 C  CB  . PHE A 1 560 ? -60.046 -7.176  31.557  1.00 90.28  ? 533 PHE B CB  1 
ATOM   3624 N  N   . SER A 1 561 ? -58.982 -4.826  33.850  1.00 111.69 ? 534 SER B N   1 
ATOM   3625 C  CA  . SER A 1 561 ? -59.332 -3.848  34.920  1.00 112.07 ? 534 SER B CA  1 
ATOM   3626 C  C   . SER A 1 561 ? -60.741 -3.990  35.488  1.00 103.57 ? 534 SER B C   1 
ATOM   3627 O  O   . SER A 1 561 ? -61.704 -3.580  34.853  1.00 102.17 ? 534 SER B O   1 
ATOM   3628 C  CB  . SER A 1 561 ? -59.152 -2.404  34.405  1.00 101.89 ? 534 SER B CB  1 
ATOM   3629 N  N   . PRO B 1 49  ? -9.741  -43.748 16.948  1.00 118.23 ? 22  PRO A N   1 
ATOM   3630 C  CA  . PRO B 1 49  ? -9.539  -44.448 18.214  1.00 119.62 ? 22  PRO A CA  1 
ATOM   3631 C  C   . PRO B 1 49  ? -8.653  -45.693 18.055  1.00 128.12 ? 22  PRO A C   1 
ATOM   3632 O  O   . PRO B 1 49  ? -8.659  -46.340 16.996  1.00 112.69 ? 22  PRO A O   1 
ATOM   3633 C  CB  . PRO B 1 49  ? -10.965 -44.827 18.636  1.00 108.02 ? 22  PRO A CB  1 
ATOM   3634 N  N   . ASP B 1 50  ? -7.902  -46.018 19.107  1.00 136.18 ? 23  ASP A N   1 
ATOM   3635 C  CA  . ASP B 1 50  ? -6.934  -47.128 19.080  1.00 132.53 ? 23  ASP A CA  1 
ATOM   3636 C  C   . ASP B 1 50  ? -7.584  -48.513 18.875  1.00 127.82 ? 23  ASP A C   1 
ATOM   3637 O  O   . ASP B 1 50  ? -7.294  -49.215 17.898  1.00 127.79 ? 23  ASP A O   1 
ATOM   3638 C  CB  . ASP B 1 50  ? -6.091  -47.129 20.372  1.00 132.51 ? 23  ASP A CB  1 
ATOM   3639 C  CG  . ASP B 1 50  ? -5.031  -46.022 20.394  1.00 139.25 ? 23  ASP A CG  1 
ATOM   3640 O  OD1 . ASP B 1 50  ? -5.083  -45.107 19.539  1.00 135.51 ? 23  ASP A OD1 1 
ATOM   3641 O  OD2 . ASP B 1 50  ? -4.138  -46.075 21.271  1.00 135.29 ? 23  ASP A OD2 1 
ATOM   3642 N  N   . GLN B 1 51  ? -8.479  -48.879 19.792  1.00 119.71 ? 24  GLN A N   1 
ATOM   3643 C  CA  . GLN B 1 51  ? -9.028  -50.237 19.874  1.00 102.29 ? 24  GLN A CA  1 
ATOM   3644 C  C   . GLN B 1 51  ? -10.245 -50.338 18.934  1.00 88.98  ? 24  GLN A C   1 
ATOM   3645 O  O   . GLN B 1 51  ? -11.222 -49.620 19.112  1.00 87.60  ? 24  GLN A O   1 
ATOM   3646 C  CB  . GLN B 1 51  ? -9.431  -50.509 21.329  1.00 99.15  ? 24  GLN A CB  1 
ATOM   3647 C  CG  . GLN B 1 51  ? -8.963  -51.825 21.927  1.00 106.51 ? 24  GLN A CG  1 
ATOM   3648 C  CD  . GLN B 1 51  ? -9.815  -52.251 23.124  1.00 112.32 ? 24  GLN A CD  1 
ATOM   3649 O  OE1 . GLN B 1 51  ? -10.569 -51.452 23.680  1.00 125.89 ? 24  GLN A OE1 1 
ATOM   3650 N  NE2 . GLN B 1 51  ? -9.719  -53.519 23.506  1.00 110.83 ? 24  GLN A NE2 1 
ATOM   3651 N  N   . ARG B 1 52  ? -10.188 -51.204 17.927  1.00 76.11  ? 25  ARG A N   1 
ATOM   3652 C  CA  . ARG B 1 52  ? -11.258 -51.271 16.938  1.00 73.52  ? 25  ARG A CA  1 
ATOM   3653 C  C   . ARG B 1 52  ? -11.251 -52.583 16.176  1.00 68.83  ? 25  ARG A C   1 
ATOM   3654 O  O   . ARG B 1 52  ? -10.444 -53.452 16.450  1.00 66.43  ? 25  ARG A O   1 
ATOM   3655 C  CB  . ARG B 1 52  ? -11.152 -50.099 15.954  1.00 79.47  ? 25  ARG A CB  1 
ATOM   3656 C  CG  . ARG B 1 52  ? -10.197 -50.326 14.793  1.00 83.93  ? 25  ARG A CG  1 
ATOM   3657 C  CD  . ARG B 1 52  ? -10.156 -49.134 13.846  1.00 89.94  ? 25  ARG A CD  1 
ATOM   3658 N  NE  . ARG B 1 52  ? -9.686  -47.902 14.489  1.00 93.94  ? 25  ARG A NE  1 
ATOM   3659 C  CZ  . ARG B 1 52  ? -9.507  -46.743 13.856  1.00 92.80  ? 25  ARG A CZ  1 
ATOM   3660 N  NH1 . ARG B 1 52  ? -9.750  -46.646 12.551  1.00 88.97  ? 25  ARG A NH1 1 
ATOM   3661 N  NH2 . ARG B 1 52  ? -9.083  -45.674 14.531  1.00 95.06  ? 25  ARG A NH2 1 
ATOM   3662 N  N   . ALA B 1 53  ? -12.174 -52.716 15.232  1.00 63.45  ? 26  ALA A N   1 
ATOM   3663 C  CA  . ALA B 1 53  ? -12.220 -53.850 14.341  1.00 66.82  ? 26  ALA A CA  1 
ATOM   3664 C  C   . ALA B 1 53  ? -12.492 -53.255 13.002  1.00 72.66  ? 26  ALA A C   1 
ATOM   3665 O  O   . ALA B 1 53  ? -13.409 -52.463 12.882  1.00 72.17  ? 26  ALA A O   1 
ATOM   3666 C  CB  . ALA B 1 53  ? -13.337 -54.801 14.719  1.00 66.82  ? 26  ALA A CB  1 
ATOM   3667 N  N   . GLN B 1 54  ? -11.693 -53.603 11.994  1.00 84.86  ? 27  GLN A N   1 
ATOM   3668 C  CA  . GLN B 1 54  ? -11.913 -53.046 10.662  1.00 88.20  ? 27  GLN A CA  1 
ATOM   3669 C  C   . GLN B 1 54  ? -11.315 -53.870 9.529   1.00 82.35  ? 27  GLN A C   1 
ATOM   3670 O  O   . GLN B 1 54  ? -10.383 -54.631 9.752   1.00 91.15  ? 27  GLN A O   1 
ATOM   3671 C  CB  . GLN B 1 54  ? -11.436 -51.589 10.610  1.00 87.70  ? 27  GLN A CB  1 
ATOM   3672 C  CG  . GLN B 1 54  ? -9.984  -51.358 10.255  1.00 88.27  ? 27  GLN A CG  1 
ATOM   3673 C  CD  . GLN B 1 54  ? -9.744  -49.894 9.955   1.00 87.64  ? 27  GLN A CD  1 
ATOM   3674 O  OE1 . GLN B 1 54  ? -9.676  -49.065 10.867  1.00 77.61  ? 27  GLN A OE1 1 
ATOM   3675 N  NE2 . GLN B 1 54  ? -9.659  -49.558 8.669   1.00 82.34  ? 27  GLN A NE2 1 
ATOM   3676 N  N   . LYS B 1 55  ? -11.884 -53.707 8.331   1.00 72.73  ? 28  LYS A N   1 
ATOM   3677 C  CA  . LYS B 1 55  ? -11.392 -54.324 7.098   1.00 68.52  ? 28  LYS A CA  1 
ATOM   3678 C  C   . LYS B 1 55  ? -11.774 -53.425 5.929   1.00 72.22  ? 28  LYS A C   1 
ATOM   3679 O  O   . LYS B 1 55  ? -12.898 -52.939 5.877   1.00 76.06  ? 28  LYS A O   1 
ATOM   3680 C  CB  . LYS B 1 55  ? -12.002 -55.715 6.897   1.00 67.02  ? 28  LYS A CB  1 
ATOM   3681 N  N   . LYS B 1 56  ? -10.845 -53.189 5.002   1.00 76.15  ? 29  LYS A N   1 
ATOM   3682 C  CA  . LYS B 1 56  ? -11.141 -52.432 3.771   1.00 73.65  ? 29  LYS A CA  1 
ATOM   3683 C  C   . LYS B 1 56  ? -12.354 -53.049 3.065   1.00 74.29  ? 29  LYS A C   1 
ATOM   3684 O  O   . LYS B 1 56  ? -12.716 -54.201 3.349   1.00 73.15  ? 29  LYS A O   1 
ATOM   3685 C  CB  . LYS B 1 56  ? -9.928  -52.429 2.824   1.00 67.64  ? 29  LYS A CB  1 
ATOM   3686 N  N   . GLY B 1 57  ? -12.984 -52.288 2.163   1.00 68.26  ? 30  GLY A N   1 
ATOM   3687 C  CA  . GLY B 1 57  ? -14.137 -52.786 1.368   1.00 66.50  ? 30  GLY A CA  1 
ATOM   3688 C  C   . GLY B 1 57  ? -14.669 -51.696 0.450   1.00 70.65  ? 30  GLY A C   1 
ATOM   3689 O  O   . GLY B 1 57  ? -14.242 -50.544 0.543   1.00 75.94  ? 30  GLY A O   1 
ATOM   3690 N  N   . ASP B 1 58  ? -15.595 -52.026 -0.437  1.00 71.13  ? 31  ASP A N   1 
ATOM   3691 C  CA  . ASP B 1 58  ? -16.035 -51.035 -1.424  1.00 79.43  ? 31  ASP A CA  1 
ATOM   3692 C  C   . ASP B 1 58  ? -16.945 -50.031 -0.783  1.00 84.79  ? 31  ASP A C   1 
ATOM   3693 O  O   . ASP B 1 58  ? -16.885 -48.843 -1.084  1.00 89.76  ? 31  ASP A O   1 
ATOM   3694 C  CB  . ASP B 1 58  ? -16.757 -51.708 -2.572  1.00 88.72  ? 31  ASP A CB  1 
ATOM   3695 C  CG  . ASP B 1 58  ? -15.864 -52.674 -3.305  1.00 101.38 ? 31  ASP A CG  1 
ATOM   3696 O  OD1 . ASP B 1 58  ? -14.881 -52.201 -3.927  1.00 109.32 ? 31  ASP A OD1 1 
ATOM   3697 O  OD2 . ASP B 1 58  ? -16.135 -53.899 -3.237  1.00 105.39 ? 31  ASP A OD2 1 
ATOM   3698 N  N   . ILE B 1 59  ? -17.799 -50.539 0.097   1.00 90.75  ? 32  ILE A N   1 
ATOM   3699 C  CA  . ILE B 1 59  ? -18.697 -49.741 0.898   1.00 83.42  ? 32  ILE A CA  1 
ATOM   3700 C  C   . ILE B 1 59  ? -18.492 -50.117 2.347   1.00 80.64  ? 32  ILE A C   1 
ATOM   3701 O  O   . ILE B 1 59  ? -18.588 -51.311 2.683   1.00 70.51  ? 32  ILE A O   1 
ATOM   3702 C  CB  . ILE B 1 59  ? -20.142 -50.058 0.529   1.00 82.02  ? 32  ILE A CB  1 
ATOM   3703 C  CG1 . ILE B 1 59  ? -20.462 -49.444 -0.824  1.00 81.43  ? 32  ILE A CG1 1 
ATOM   3704 C  CG2 . ILE B 1 59  ? -21.095 -49.534 1.594   1.00 82.58  ? 32  ILE A CG2 1 
ATOM   3705 C  CD1 . ILE B 1 59  ? -21.649 -50.105 -1.485  1.00 90.80  ? 32  ILE A CD1 1 
ATOM   3706 N  N   . ILE B 1 60  ? -18.256 -49.110 3.196   1.00 76.25  ? 33  ILE A N   1 
ATOM   3707 C  CA  . ILE B 1 60  ? -18.044 -49.345 4.630   1.00 77.87  ? 33  ILE A CA  1 
ATOM   3708 C  C   . ILE B 1 60  ? -19.312 -49.166 5.450   1.00 72.45  ? 33  ILE A C   1 
ATOM   3709 O  O   . ILE B 1 60  ? -20.040 -48.199 5.255   1.00 75.64  ? 33  ILE A O   1 
ATOM   3710 C  CB  . ILE B 1 60  ? -17.001 -48.377 5.219   1.00 83.10  ? 33  ILE A CB  1 
ATOM   3711 C  CG1 . ILE B 1 60  ? -15.755 -48.331 4.339   1.00 84.63  ? 33  ILE A CG1 1 
ATOM   3712 C  CG2 . ILE B 1 60  ? -16.634 -48.792 6.645   1.00 83.63  ? 33  ILE A CG2 1 
ATOM   3713 C  CD1 . ILE B 1 60  ? -15.210 -49.706 4.009   1.00 91.16  ? 33  ILE A CD1 1 
ATOM   3714 N  N   . LEU B 1 61  ? -19.560 -50.102 6.366   1.00 70.45  ? 34  LEU A N   1 
ATOM   3715 C  CA  . LEU B 1 61  ? -20.566 -49.940 7.435   1.00 64.78  ? 34  LEU A CA  1 
ATOM   3716 C  C   . LEU B 1 61  ? -19.920 -49.568 8.745   1.00 61.40  ? 34  LEU A C   1 
ATOM   3717 O  O   . LEU B 1 61  ? -18.985 -50.235 9.174   1.00 55.84  ? 34  LEU A O   1 
ATOM   3718 C  CB  . LEU B 1 61  ? -21.314 -51.239 7.707   1.00 61.49  ? 34  LEU A CB  1 
ATOM   3719 C  CG  . LEU B 1 61  ? -22.065 -51.869 6.556   1.00 66.06  ? 34  LEU A CG  1 
ATOM   3720 C  CD1 . LEU B 1 61  ? -23.111 -52.800 7.139   1.00 62.47  ? 34  LEU A CD1 1 
ATOM   3721 C  CD2 . LEU B 1 61  ? -22.684 -50.824 5.628   1.00 69.39  ? 34  LEU A CD2 1 
ATOM   3722 N  N   . GLY B 1 62  ? -20.455 -48.546 9.415   1.00 63.72  ? 35  GLY A N   1 
ATOM   3723 C  CA  . GLY B 1 62  ? -20.037 -48.241 10.796  1.00 59.24  ? 35  GLY A CA  1 
ATOM   3724 C  C   . GLY B 1 62  ? -20.620 -49.223 11.803  1.00 53.65  ? 35  GLY A C   1 
ATOM   3725 O  O   . GLY B 1 62  ? -21.601 -49.901 11.536  1.00 56.89  ? 35  GLY A O   1 
ATOM   3726 N  N   . GLY B 1 63  ? -20.031 -49.289 12.983  1.00 52.27  ? 36  GLY A N   1 
ATOM   3727 C  CA  . GLY B 1 63  ? -20.593 -50.095 14.046  1.00 50.73  ? 36  GLY A CA  1 
ATOM   3728 C  C   . GLY B 1 63  ? -20.263 -49.548 15.412  1.00 52.85  ? 36  GLY A C   1 
ATOM   3729 O  O   . GLY B 1 63  ? -19.122 -49.140 15.644  1.00 49.98  ? 36  GLY A O   1 
ATOM   3730 N  N   . LEU B 1 64  ? -21.249 -49.550 16.322  1.00 49.30  ? 37  LEU A N   1 
ATOM   3731 C  CA  . LEU B 1 64  ? -20.992 -49.174 17.711  1.00 47.66  ? 37  LEU A CA  1 
ATOM   3732 C  C   . LEU B 1 64  ? -21.470 -50.277 18.638  1.00 46.06  ? 37  LEU A C   1 
ATOM   3733 O  O   . LEU B 1 64  ? -22.527 -50.840 18.428  1.00 43.25  ? 37  LEU A O   1 
ATOM   3734 C  CB  . LEU B 1 64  ? -21.698 -47.874 18.023  1.00 48.18  ? 37  LEU A CB  1 
ATOM   3735 C  CG  . LEU B 1 64  ? -21.266 -46.697 17.156  1.00 50.83  ? 37  LEU A CG  1 
ATOM   3736 C  CD1 . LEU B 1 64  ? -22.188 -45.512 17.406  1.00 52.48  ? 37  LEU A CD1 1 
ATOM   3737 C  CD2 . LEU B 1 64  ? -19.823 -46.313 17.437  1.00 51.08  ? 37  LEU A CD2 1 
ATOM   3738 N  N   . PHE B 1 65  ? -20.667 -50.617 19.640  1.00 47.43  ? 38  PHE A N   1 
ATOM   3739 C  CA  . PHE B 1 65  ? -20.981 -51.728 20.553  1.00 49.27  ? 38  PHE A CA  1 
ATOM   3740 C  C   . PHE B 1 65  ? -20.326 -51.471 21.877  1.00 50.68  ? 38  PHE A C   1 
ATOM   3741 O  O   . PHE B 1 65  ? -19.255 -50.862 21.917  1.00 45.50  ? 38  PHE A O   1 
ATOM   3742 C  CB  . PHE B 1 65  ? -20.489 -53.070 20.007  1.00 50.50  ? 38  PHE A CB  1 
ATOM   3743 C  CG  . PHE B 1 65  ? -21.193 -53.489 18.769  1.00 49.04  ? 38  PHE A CG  1 
ATOM   3744 C  CD1 . PHE B 1 65  ? -20.718 -53.101 17.534  1.00 55.88  ? 38  PHE A CD1 1 
ATOM   3745 C  CD2 . PHE B 1 65  ? -22.358 -54.200 18.839  1.00 48.68  ? 38  PHE A CD2 1 
ATOM   3746 C  CE1 . PHE B 1 65  ? -21.396 -53.436 16.374  1.00 52.74  ? 38  PHE A CE1 1 
ATOM   3747 C  CE2 . PHE B 1 65  ? -23.034 -54.550 17.691  1.00 49.88  ? 38  PHE A CE2 1 
ATOM   3748 C  CZ  . PHE B 1 65  ? -22.550 -54.165 16.459  1.00 50.76  ? 38  PHE A CZ  1 
ATOM   3749 N  N   . PRO B 1 66  ? -20.963 -51.925 22.961  1.00 54.04  ? 39  PRO A N   1 
ATOM   3750 C  CA  . PRO B 1 66  ? -20.470 -51.777 24.327  1.00 59.23  ? 39  PRO A CA  1 
ATOM   3751 C  C   . PRO B 1 66  ? -19.603 -52.966 24.806  1.00 61.75  ? 39  PRO A C   1 
ATOM   3752 O  O   . PRO B 1 66  ? -20.052 -53.828 25.576  1.00 62.13  ? 39  PRO A O   1 
ATOM   3753 C  CB  . PRO B 1 66  ? -21.764 -51.677 25.134  1.00 60.41  ? 39  PRO A CB  1 
ATOM   3754 C  CG  . PRO B 1 66  ? -22.735 -52.520 24.366  1.00 60.36  ? 39  PRO A CG  1 
ATOM   3755 C  CD  . PRO B 1 66  ? -22.261 -52.612 22.934  1.00 56.86  ? 39  PRO A CD  1 
ATOM   3756 N  N   . ILE B 1 67  ? -18.356 -52.976 24.357  1.00 61.99  ? 40  ILE A N   1 
ATOM   3757 C  CA  . ILE B 1 67  ? -17.402 -54.046 24.675  1.00 61.45  ? 40  ILE A CA  1 
ATOM   3758 C  C   . ILE B 1 67  ? -17.001 -53.994 26.152  1.00 58.29  ? 40  ILE A C   1 
ATOM   3759 O  O   . ILE B 1 67  ? -16.665 -55.017 26.758  1.00 60.09  ? 40  ILE A O   1 
ATOM   3760 C  CB  . ILE B 1 67  ? -16.126 -53.938 23.795  1.00 59.37  ? 40  ILE A CB  1 
ATOM   3761 C  CG1 . ILE B 1 67  ? -16.486 -53.838 22.317  1.00 55.13  ? 40  ILE A CG1 1 
ATOM   3762 C  CG2 . ILE B 1 67  ? -15.220 -55.137 24.023  1.00 64.83  ? 40  ILE A CG2 1 
ATOM   3763 C  CD1 . ILE B 1 67  ? -17.448 -54.911 21.853  1.00 58.16  ? 40  ILE A CD1 1 
ATOM   3764 N  N   . HIS B 1 68  ? -17.013 -52.789 26.701  1.00 57.58  ? 41  HIS A N   1 
ATOM   3765 C  CA  . HIS B 1 68  ? -16.941 -52.580 28.131  1.00 64.98  ? 41  HIS A CA  1 
ATOM   3766 C  C   . HIS B 1 68  ? -18.235 -52.011 28.669  1.00 57.54  ? 41  HIS A C   1 
ATOM   3767 O  O   . HIS B 1 68  ? -18.921 -51.252 27.996  1.00 58.79  ? 41  HIS A O   1 
ATOM   3768 C  CB  . HIS B 1 68  ? -15.818 -51.618 28.459  1.00 70.50  ? 41  HIS A CB  1 
ATOM   3769 C  CG  . HIS B 1 68  ? -14.487 -52.144 28.080  1.00 73.40  ? 41  HIS A CG  1 
ATOM   3770 N  ND1 . HIS B 1 68  ? -13.965 -51.983 26.818  1.00 73.45  ? 41  HIS A ND1 1 
ATOM   3771 C  CD2 . HIS B 1 68  ? -13.595 -52.883 28.775  1.00 80.07  ? 41  HIS A CD2 1 
ATOM   3772 C  CE1 . HIS B 1 68  ? -12.786 -52.573 26.762  1.00 77.46  ? 41  HIS A CE1 1 
ATOM   3773 N  NE2 . HIS B 1 68  ? -12.542 -53.132 27.935  1.00 80.60  ? 41  HIS A NE2 1 
ATOM   3774 N  N   . PHE B 1 69  ? -18.551 -52.375 29.900  1.00 53.59  ? 42  PHE A N   1 
ATOM   3775 C  CA  . PHE B 1 69  ? -19.784 -51.921 30.522  1.00 54.58  ? 42  PHE A CA  1 
ATOM   3776 C  C   . PHE B 1 69  ? -19.738 -50.450 30.957  1.00 51.89  ? 42  PHE A C   1 
ATOM   3777 O  O   . PHE B 1 69  ? -20.778 -49.845 31.200  1.00 58.50  ? 42  PHE A O   1 
ATOM   3778 C  CB  . PHE B 1 69  ? -20.093 -52.777 31.745  1.00 53.67  ? 42  PHE A CB  1 
ATOM   3779 C  CG  . PHE B 1 69  ? -20.666 -54.126 31.432  1.00 53.25  ? 42  PHE A CG  1 
ATOM   3780 C  CD1 . PHE B 1 69  ? -21.871 -54.251 30.760  1.00 57.95  ? 42  PHE A CD1 1 
ATOM   3781 C  CD2 . PHE B 1 69  ? -20.042 -55.279 31.893  1.00 57.32  ? 42  PHE A CD2 1 
ATOM   3782 C  CE1 . PHE B 1 69  ? -22.429 -55.513 30.523  1.00 62.96  ? 42  PHE A CE1 1 
ATOM   3783 C  CE2 . PHE B 1 69  ? -20.588 -56.538 31.668  1.00 56.81  ? 42  PHE A CE2 1 
ATOM   3784 C  CZ  . PHE B 1 69  ? -21.781 -56.662 30.978  1.00 59.32  ? 42  PHE A CZ  1 
ATOM   3785 N  N   . GLY B 1 70  ? -18.552 -49.884 31.091  1.00 48.68  ? 43  GLY A N   1 
ATOM   3786 C  CA  . GLY B 1 70  ? -18.440 -48.546 31.621  1.00 53.47  ? 43  GLY A CA  1 
ATOM   3787 C  C   . GLY B 1 70  ? -17.050 -47.970 31.610  1.00 58.29  ? 43  GLY A C   1 
ATOM   3788 O  O   . GLY B 1 70  ? -16.134 -48.526 31.035  1.00 75.27  ? 43  GLY A O   1 
ATOM   3789 N  N   . VAL B 1 71  ? -16.898 -46.847 32.272  1.00 64.26  ? 44  VAL A N   1 
ATOM   3790 C  CA  . VAL B 1 71  ? -15.642 -46.122 32.295  1.00 71.02  ? 44  VAL A CA  1 
ATOM   3791 C  C   . VAL B 1 71  ? -15.176 -46.048 33.745  1.00 68.80  ? 44  VAL A C   1 
ATOM   3792 O  O   . VAL B 1 71  ? -15.978 -46.143 34.674  1.00 60.48  ? 44  VAL A O   1 
ATOM   3793 C  CB  . VAL B 1 71  ? -15.871 -44.717 31.674  1.00 79.97  ? 44  VAL A CB  1 
ATOM   3794 C  CG1 . VAL B 1 71  ? -14.870 -43.687 32.165  1.00 86.38  ? 44  VAL A CG1 1 
ATOM   3795 C  CG2 . VAL B 1 71  ? -15.843 -44.806 30.153  1.00 84.36  ? 44  VAL A CG2 1 
ATOM   3796 N  N   . ALA B 1 72  ? -13.874 -45.893 33.947  1.00 80.19  ? 45  ALA A N   1 
ATOM   3797 C  CA  . ALA B 1 72  ? -13.336 -45.651 35.292  1.00 81.26  ? 45  ALA A CA  1 
ATOM   3798 C  C   . ALA B 1 72  ? -13.639 -44.200 35.631  1.00 88.28  ? 45  ALA A C   1 
ATOM   3799 O  O   . ALA B 1 72  ? -13.203 -43.285 34.930  1.00 85.23  ? 45  ALA A O   1 
ATOM   3800 C  CB  . ALA B 1 72  ? -11.843 -45.905 35.322  1.00 82.42  ? 45  ALA A CB  1 
ATOM   3801 N  N   . ALA B 1 73  ? -14.397 -43.982 36.693  1.00 101.51 ? 46  ALA A N   1 
ATOM   3802 C  CA  . ALA B 1 73  ? -14.992 -42.666 36.918  1.00 116.47 ? 46  ALA A CA  1 
ATOM   3803 C  C   . ALA B 1 73  ? -14.066 -41.700 37.673  1.00 119.34 ? 46  ALA A C   1 
ATOM   3804 O  O   . ALA B 1 73  ? -14.521 -40.954 38.530  1.00 115.11 ? 46  ALA A O   1 
ATOM   3805 C  CB  . ALA B 1 73  ? -16.328 -42.813 37.641  1.00 117.64 ? 46  ALA A CB  1 
ATOM   3806 N  N   . LYS B 1 74  ? -12.778 -41.692 37.331  1.00 123.21 ? 47  LYS A N   1 
ATOM   3807 C  CA  . LYS B 1 74  ? -11.818 -40.793 37.962  1.00 112.64 ? 47  LYS A CA  1 
ATOM   3808 C  C   . LYS B 1 74  ? -12.134 -39.341 37.602  1.00 108.44 ? 47  LYS A C   1 
ATOM   3809 O  O   . LYS B 1 74  ? -11.840 -38.915 36.482  1.00 111.88 ? 47  LYS A O   1 
ATOM   3810 C  CB  . LYS B 1 74  ? -10.400 -41.149 37.505  1.00 114.39 ? 47  LYS A CB  1 
ATOM   3811 N  N   . ASP B 1 75  ? -12.739 -38.602 38.546  1.00 109.35 ? 48  ASP A N   1 
ATOM   3812 C  CA  . ASP B 1 75  ? -13.073 -37.161 38.378  1.00 108.07 ? 48  ASP A CA  1 
ATOM   3813 C  C   . ASP B 1 75  ? -11.807 -36.310 38.227  1.00 98.58  ? 48  ASP A C   1 
ATOM   3814 O  O   . ASP B 1 75  ? -10.840 -36.480 38.977  1.00 83.07  ? 48  ASP A O   1 
ATOM   3815 C  CB  . ASP B 1 75  ? -13.909 -36.626 39.556  1.00 102.20 ? 48  ASP A CB  1 
ATOM   3816 N  N   . GLN B 1 76  ? -11.826 -35.409 37.247  1.00 88.73  ? 49  GLN A N   1 
ATOM   3817 C  CA  . GLN B 1 76  ? -10.641 -34.663 36.863  1.00 88.67  ? 49  GLN A CA  1 
ATOM   3818 C  C   . GLN B 1 76  ? -10.673 -33.280 37.474  1.00 79.87  ? 49  GLN A C   1 
ATOM   3819 O  O   . GLN B 1 76  ? -11.598 -32.524 37.241  1.00 70.84  ? 49  GLN A O   1 
ATOM   3820 C  CB  . GLN B 1 76  ? -10.545 -34.539 35.344  1.00 90.79  ? 49  GLN A CB  1 
ATOM   3821 C  CG  . GLN B 1 76  ? -9.688  -35.604 34.693  1.00 93.41  ? 49  GLN A CG  1 
ATOM   3822 C  CD  . GLN B 1 76  ? -10.178 -35.939 33.299  1.00 103.34 ? 49  GLN A CD  1 
ATOM   3823 O  OE1 . GLN B 1 76  ? -11.357 -35.761 32.987  1.00 117.15 ? 49  GLN A OE1 1 
ATOM   3824 N  NE2 . GLN B 1 76  ? -9.284  -36.434 32.454  1.00 99.19  ? 49  GLN A NE2 1 
ATOM   3825 N  N   . ASP B 1 77  ? -9.641  -32.958 38.243  1.00 75.12  ? 50  ASP A N   1 
ATOM   3826 C  CA  . ASP B 1 77  ? -9.492  -31.630 38.799  1.00 74.60  ? 50  ASP A CA  1 
ATOM   3827 C  C   . ASP B 1 77  ? -8.879  -30.635 37.770  1.00 70.22  ? 50  ASP A C   1 
ATOM   3828 O  O   . ASP B 1 77  ? -8.710  -29.439 38.094  1.00 54.22  ? 50  ASP A O   1 
ATOM   3829 C  CB  . ASP B 1 77  ? -8.695  -31.672 40.122  1.00 77.48  ? 50  ASP A CB  1 
ATOM   3830 C  CG  . ASP B 1 77  ? -7.359  -32.428 40.007  1.00 79.09  ? 50  ASP A CG  1 
ATOM   3831 O  OD1 . ASP B 1 77  ? -6.903  -32.706 38.873  1.00 78.63  ? 50  ASP A OD1 1 
ATOM   3832 O  OD2 . ASP B 1 77  ? -6.769  -32.744 41.071  1.00 81.92  ? 50  ASP A OD2 1 
ATOM   3833 N  N   . LEU B 1 78  ? -8.582  -31.105 36.542  1.00 63.64  ? 51  LEU A N   1 
ATOM   3834 C  CA  . LEU B 1 78  ? -8.081  -30.217 35.468  1.00 66.01  ? 51  LEU A CA  1 
ATOM   3835 C  C   . LEU B 1 78  ? -6.966  -29.300 35.953  1.00 70.42  ? 51  LEU A C   1 
ATOM   3836 O  O   . LEU B 1 78  ? -7.005  -28.071 35.733  1.00 62.50  ? 51  LEU A O   1 
ATOM   3837 C  CB  . LEU B 1 78  ? -9.192  -29.315 34.938  1.00 63.97  ? 51  LEU A CB  1 
ATOM   3838 C  CG  . LEU B 1 78  ? -10.394 -29.939 34.271  1.00 60.36  ? 51  LEU A CG  1 
ATOM   3839 C  CD1 . LEU B 1 78  ? -11.410 -28.838 33.970  1.00 62.32  ? 51  LEU A CD1 1 
ATOM   3840 C  CD2 . LEU B 1 78  ? -9.942  -30.629 33.008  1.00 58.20  ? 51  LEU A CD2 1 
ATOM   3841 N  N   . LYS B 1 79  ? -6.018  -29.903 36.669  1.00 80.21  ? 52  LYS A N   1 
ATOM   3842 C  CA  . LYS B 1 79  ? -4.790  -29.244 37.098  1.00 76.90  ? 52  LYS A CA  1 
ATOM   3843 C  C   . LYS B 1 79  ? -3.776  -29.358 35.978  1.00 71.02  ? 52  LYS A C   1 
ATOM   3844 O  O   . LYS B 1 79  ? -2.872  -28.542 35.868  1.00 72.14  ? 52  LYS A O   1 
ATOM   3845 C  CB  . LYS B 1 79  ? -4.233  -29.905 38.356  1.00 86.60  ? 52  LYS A CB  1 
ATOM   3846 C  CG  . LYS B 1 79  ? -4.606  -29.225 39.661  1.00 92.84  ? 52  LYS A CG  1 
ATOM   3847 C  CD  . LYS B 1 79  ? -3.794  -29.832 40.803  1.00 103.62 ? 52  LYS A CD  1 
ATOM   3848 C  CE  . LYS B 1 79  ? -3.562  -28.848 41.930  1.00 108.03 ? 52  LYS A CE  1 
ATOM   3849 N  NZ  . LYS B 1 79  ? -4.847  -28.476 42.583  1.00 116.05 ? 52  LYS A NZ  1 
ATOM   3850 N  N   . SER B 1 80  ? -3.923  -30.395 35.160  1.00 72.36  ? 53  SER A N   1 
ATOM   3851 C  CA  . SER B 1 80  ? -3.115  -30.566 33.962  1.00 72.82  ? 53  SER A CA  1 
ATOM   3852 C  C   . SER B 1 80  ? -4.049  -30.983 32.850  1.00 67.50  ? 53  SER A C   1 
ATOM   3853 O  O   . SER B 1 80  ? -5.221  -31.208 33.101  1.00 66.85  ? 53  SER A O   1 
ATOM   3854 C  CB  . SER B 1 80  ? -2.089  -31.659 34.182  1.00 72.16  ? 53  SER A CB  1 
ATOM   3855 O  OG  . SER B 1 80  ? -2.718  -32.928 34.134  1.00 68.51  ? 53  SER A OG  1 
ATOM   3856 N  N   . ARG B 1 81  ? -3.523  -31.100 31.636  1.00 71.29  ? 54  ARG A N   1 
ATOM   3857 C  CA  . ARG B 1 81  ? -4.327  -31.448 30.479  1.00 71.77  ? 54  ARG A CA  1 
ATOM   3858 C  C   . ARG B 1 81  ? -5.052  -32.737 30.810  1.00 68.14  ? 54  ARG A C   1 
ATOM   3859 O  O   . ARG B 1 81  ? -4.468  -33.613 31.414  1.00 66.86  ? 54  ARG A O   1 
ATOM   3860 C  CB  . ARG B 1 81  ? -3.467  -31.630 29.227  1.00 79.13  ? 54  ARG A CB  1 
ATOM   3861 C  CG  . ARG B 1 81  ? -4.197  -32.316 28.064  1.00 95.69  ? 54  ARG A CG  1 
ATOM   3862 C  CD  . ARG B 1 81  ? -3.851  -31.752 26.687  1.00 103.06 ? 54  ARG A CD  1 
ATOM   3863 N  NE  . ARG B 1 81  ? -2.407  -31.565 26.489  1.00 113.23 ? 54  ARG A NE  1 
ATOM   3864 C  CZ  . ARG B 1 81  ? -1.741  -30.413 26.631  1.00 113.88 ? 54  ARG A CZ  1 
ATOM   3865 N  NH1 . ARG B 1 81  ? -2.358  -29.286 26.982  1.00 118.54 ? 54  ARG A NH1 1 
ATOM   3866 N  NH2 . ARG B 1 81  ? -0.436  -30.387 26.416  1.00 110.11 ? 54  ARG A NH2 1 
ATOM   3867 N  N   . PRO B 1 82  ? -6.337  -32.832 30.450  1.00 69.62  ? 55  PRO A N   1 
ATOM   3868 C  CA  . PRO B 1 82  ? -7.041  -34.079 30.726  1.00 72.77  ? 55  PRO A CA  1 
ATOM   3869 C  C   . PRO B 1 82  ? -6.674  -35.172 29.747  1.00 73.61  ? 55  PRO A C   1 
ATOM   3870 O  O   . PRO B 1 82  ? -6.620  -34.918 28.556  1.00 75.46  ? 55  PRO A O   1 
ATOM   3871 C  CB  . PRO B 1 82  ? -8.530  -33.714 30.589  1.00 74.33  ? 55  PRO A CB  1 
ATOM   3872 C  CG  . PRO B 1 82  ? -8.594  -32.262 30.258  1.00 74.46  ? 55  PRO A CG  1 
ATOM   3873 C  CD  . PRO B 1 82  ? -7.226  -31.742 29.989  1.00 71.23  ? 55  PRO A CD  1 
ATOM   3874 N  N   . GLU B 1 83  ? -6.422  -36.375 30.259  1.00 79.59  ? 56  GLU A N   1 
ATOM   3875 C  CA  . GLU B 1 83  ? -6.237  -37.561 29.427  1.00 84.71  ? 56  GLU A CA  1 
ATOM   3876 C  C   . GLU B 1 83  ? -7.613  -38.155 29.193  1.00 74.19  ? 56  GLU A C   1 
ATOM   3877 O  O   . GLU B 1 83  ? -8.542  -37.762 29.850  1.00 74.98  ? 56  GLU A O   1 
ATOM   3878 C  CB  . GLU B 1 83  ? -5.331  -38.582 30.135  1.00 87.92  ? 56  GLU A CB  1 
ATOM   3879 N  N   . SER B 1 84  ? -7.752  -39.095 28.268  1.00 71.61  ? 57  SER A N   1 
ATOM   3880 C  CA  . SER B 1 84  ? -9.030  -39.765 28.071  1.00 80.31  ? 57  SER A CA  1 
ATOM   3881 C  C   . SER B 1 84  ? -9.394  -40.698 29.267  1.00 84.07  ? 57  SER A C   1 
ATOM   3882 O  O   . SER B 1 84  ? -8.516  -41.125 30.027  1.00 79.11  ? 57  SER A O   1 
ATOM   3883 C  CB  . SER B 1 84  ? -9.011  -40.568 26.766  1.00 84.97  ? 57  SER A CB  1 
ATOM   3884 O  OG  . SER B 1 84  ? -8.457  -41.863 26.973  1.00 84.34  ? 57  SER A OG  1 
ATOM   3885 N  N   . VAL B 1 85  ? -10.688 -40.998 29.421  1.00 78.07  ? 58  VAL A N   1 
ATOM   3886 C  CA  . VAL B 1 85  ? -11.162 -41.965 30.417  1.00 79.62  ? 58  VAL A CA  1 
ATOM   3887 C  C   . VAL B 1 85  ? -10.836 -43.392 29.955  1.00 76.73  ? 58  VAL A C   1 
ATOM   3888 O  O   . VAL B 1 85  ? -10.713 -43.637 28.761  1.00 81.74  ? 58  VAL A O   1 
ATOM   3889 C  CB  . VAL B 1 85  ? -12.682 -41.827 30.643  1.00 81.49  ? 58  VAL A CB  1 
ATOM   3890 N  N   . GLU B 1 86  ? -10.670 -44.320 30.893  1.00 73.40  ? 59  GLU A N   1 
ATOM   3891 C  CA  . GLU B 1 86  ? -10.302 -45.690 30.558  1.00 71.23  ? 59  GLU A CA  1 
ATOM   3892 C  C   . GLU B 1 86  ? -11.532 -46.556 30.707  1.00 69.10  ? 59  GLU A C   1 
ATOM   3893 O  O   . GLU B 1 86  ? -12.269 -46.440 31.677  1.00 71.84  ? 59  GLU A O   1 
ATOM   3894 C  CB  . GLU B 1 86  ? -9.190  -46.211 31.473  1.00 70.36  ? 59  GLU A CB  1 
ATOM   3895 N  N   . CYS B 1 87  ? -11.747 -47.423 29.735  1.00 65.94  ? 60  CYS A N   1 
ATOM   3896 C  CA  . CYS B 1 87  ? -12.878 -48.308 29.749  1.00 67.24  ? 60  CYS A CA  1 
ATOM   3897 C  C   . CYS B 1 87  ? -12.617 -49.464 30.693  1.00 69.46  ? 60  CYS A C   1 
ATOM   3898 O  O   . CYS B 1 87  ? -11.535 -50.024 30.714  1.00 73.84  ? 60  CYS A O   1 
ATOM   3899 C  CB  . CYS B 1 87  ? -13.175 -48.776 28.325  1.00 74.70  ? 60  CYS A CB  1 
ATOM   3900 S  SG  . CYS B 1 87  ? -13.877 -47.409 27.331  1.00 83.75  ? 60  CYS A SG  1 
ATOM   3901 N  N   . ILE B 1 88  ? -13.616 -49.813 31.487  1.00 73.05  ? 61  ILE A N   1 
ATOM   3902 C  CA  . ILE B 1 88  ? -13.440 -50.767 32.562  1.00 74.04  ? 61  ILE A CA  1 
ATOM   3903 C  C   . ILE B 1 88  ? -14.588 -51.788 32.510  1.00 72.85  ? 61  ILE A C   1 
ATOM   3904 O  O   . ILE B 1 88  ? -15.697 -51.459 32.071  1.00 78.05  ? 61  ILE A O   1 
ATOM   3905 C  CB  . ILE B 1 88  ? -13.276 -49.999 33.915  1.00 80.41  ? 61  ILE A CB  1 
ATOM   3906 C  CG1 . ILE B 1 88  ? -12.189 -50.632 34.784  1.00 97.27  ? 61  ILE A CG1 1 
ATOM   3907 C  CG2 . ILE B 1 88  ? -14.573 -49.872 34.704  1.00 82.53  ? 61  ILE A CG2 1 
ATOM   3908 C  CD1 . ILE B 1 88  ? -10.775 -50.447 34.252  1.00 103.34 ? 61  ILE A CD1 1 
ATOM   3909 N  N   . ARG B 1 89  ? -14.288 -53.023 32.915  1.00 67.45  ? 62  ARG A N   1 
ATOM   3910 C  CA  . ARG B 1 89  ? -15.212 -54.192 32.897  1.00 65.57  ? 62  ARG A CA  1 
ATOM   3911 C  C   . ARG B 1 89  ? -15.628 -54.655 31.500  1.00 65.85  ? 62  ARG A C   1 
ATOM   3912 O  O   . ARG B 1 89  ? -16.392 -53.993 30.801  1.00 68.39  ? 62  ARG A O   1 
ATOM   3913 C  CB  . ARG B 1 89  ? -16.430 -53.981 33.783  1.00 67.26  ? 62  ARG A CB  1 
ATOM   3914 C  CG  . ARG B 1 89  ? -16.071 -53.504 35.181  1.00 73.13  ? 62  ARG A CG  1 
ATOM   3915 C  CD  . ARG B 1 89  ? -17.290 -52.934 35.884  1.00 84.91  ? 62  ARG A CD  1 
ATOM   3916 N  NE  . ARG B 1 89  ? -18.114 -54.017 36.396  1.00 96.64  ? 62  ARG A NE  1 
ATOM   3917 C  CZ  . ARG B 1 89  ? -19.438 -53.984 36.515  1.00 106.21 ? 62  ARG A CZ  1 
ATOM   3918 N  NH1 . ARG B 1 89  ? -20.134 -52.913 36.149  1.00 102.05 ? 62  ARG A NH1 1 
ATOM   3919 N  NH2 . ARG B 1 89  ? -20.071 -55.048 37.001  1.00 113.78 ? 62  ARG A NH2 1 
ATOM   3920 N  N   . TYR B 1 90  ? -15.121 -55.823 31.122  1.00 64.93  ? 63  TYR A N   1 
ATOM   3921 C  CA  . TYR B 1 90  ? -15.265 -56.343 29.782  1.00 65.08  ? 63  TYR A CA  1 
ATOM   3922 C  C   . TYR B 1 90  ? -16.658 -56.930 29.684  1.00 66.95  ? 63  TYR A C   1 
ATOM   3923 O  O   . TYR B 1 90  ? -17.112 -57.587 30.617  1.00 78.67  ? 63  TYR A O   1 
ATOM   3924 C  CB  . TYR B 1 90  ? -14.190 -57.417 29.487  1.00 59.43  ? 63  TYR A CB  1 
ATOM   3925 C  CG  . TYR B 1 90  ? -14.002 -57.654 28.000  1.00 57.83  ? 63  TYR A CG  1 
ATOM   3926 C  CD1 . TYR B 1 90  ? -13.098 -56.906 27.269  1.00 57.94  ? 63  TYR A CD1 1 
ATOM   3927 C  CD2 . TYR B 1 90  ? -14.757 -58.595 27.318  1.00 59.34  ? 63  TYR A CD2 1 
ATOM   3928 C  CE1 . TYR B 1 90  ? -12.936 -57.094 25.896  1.00 56.34  ? 63  TYR A CE1 1 
ATOM   3929 C  CE2 . TYR B 1 90  ? -14.602 -58.786 25.946  1.00 60.02  ? 63  TYR A CE2 1 
ATOM   3930 C  CZ  . TYR B 1 90  ? -13.694 -58.023 25.247  1.00 56.42  ? 63  TYR A CZ  1 
ATOM   3931 O  OH  . TYR B 1 90  ? -13.547 -58.190 23.890  1.00 63.84  ? 63  TYR A OH  1 
ATOM   3932 N  N   . ASN B 1 91  ? -17.335 -56.682 28.570  1.00 62.30  ? 64  ASN A N   1 
ATOM   3933 C  CA  . ASN B 1 91  ? -18.692 -57.172 28.370  1.00 65.82  ? 64  ASN A CA  1 
ATOM   3934 C  C   . ASN B 1 91  ? -18.716 -58.209 27.254  1.00 64.03  ? 64  ASN A C   1 
ATOM   3935 O  O   . ASN B 1 91  ? -18.774 -57.870 26.068  1.00 57.14  ? 64  ASN A O   1 
ATOM   3936 C  CB  . ASN B 1 91  ? -19.635 -55.994 28.072  1.00 67.77  ? 64  ASN A CB  1 
ATOM   3937 C  CG  . ASN B 1 91  ? -21.017 -56.431 27.604  1.00 67.33  ? 64  ASN A CG  1 
ATOM   3938 O  OD1 . ASN B 1 91  ? -21.457 -57.577 27.816  1.00 65.57  ? 64  ASN A OD1 1 
ATOM   3939 N  ND2 . ASN B 1 91  ? -21.707 -55.514 26.940  1.00 68.63  ? 64  ASN A ND2 1 
ATOM   3940 N  N   . PHE B 1 92  ? -18.686 -59.475 27.657  1.00 66.53  ? 65  PHE A N   1 
ATOM   3941 C  CA  . PHE B 1 92  ? -18.623 -60.611 26.719  1.00 68.91  ? 65  PHE A CA  1 
ATOM   3942 C  C   . PHE B 1 92  ? -19.834 -60.764 25.792  1.00 63.60  ? 65  PHE A C   1 
ATOM   3943 O  O   . PHE B 1 92  ? -19.723 -61.164 24.626  1.00 59.10  ? 65  PHE A O   1 
ATOM   3944 C  CB  . PHE B 1 92  ? -18.447 -61.901 27.515  1.00 71.28  ? 65  PHE A CB  1 
ATOM   3945 C  CG  . PHE B 1 92  ? -17.087 -62.040 28.133  1.00 69.02  ? 65  PHE A CG  1 
ATOM   3946 C  CD1 . PHE B 1 92  ? -15.985 -62.341 27.344  1.00 68.45  ? 65  PHE A CD1 1 
ATOM   3947 C  CD2 . PHE B 1 92  ? -16.908 -61.867 29.488  1.00 67.65  ? 65  PHE A CD2 1 
ATOM   3948 C  CE1 . PHE B 1 92  ? -14.725 -62.463 27.898  1.00 65.57  ? 65  PHE A CE1 1 
ATOM   3949 C  CE2 . PHE B 1 92  ? -15.654 -61.995 30.048  1.00 72.45  ? 65  PHE A CE2 1 
ATOM   3950 C  CZ  . PHE B 1 92  ? -14.557 -62.291 29.249  1.00 68.88  ? 65  PHE A CZ  1 
ATOM   3951 N  N   . ARG B 1 93  ? -21.001 -60.464 26.320  1.00 63.47  ? 66  ARG A N   1 
ATOM   3952 C  CA  . ARG B 1 93  ? -22.201 -60.462 25.509  1.00 62.78  ? 66  ARG A CA  1 
ATOM   3953 C  C   . ARG B 1 93  ? -22.077 -59.397 24.406  1.00 59.69  ? 66  ARG A C   1 
ATOM   3954 O  O   . ARG B 1 93  ? -22.528 -59.584 23.265  1.00 54.46  ? 66  ARG A O   1 
ATOM   3955 C  CB  . ARG B 1 93  ? -23.398 -60.190 26.409  1.00 59.29  ? 66  ARG A CB  1 
ATOM   3956 C  CG  . ARG B 1 93  ? -24.724 -60.402 25.743  1.00 58.85  ? 66  ARG A CG  1 
ATOM   3957 C  CD  . ARG B 1 93  ? -25.807 -60.063 26.719  1.00 60.43  ? 66  ARG A CD  1 
ATOM   3958 N  NE  . ARG B 1 93  ? -27.115 -60.048 26.083  1.00 67.32  ? 66  ARG A NE  1 
ATOM   3959 C  CZ  . ARG B 1 93  ? -28.247 -59.838 26.741  1.00 65.84  ? 66  ARG A CZ  1 
ATOM   3960 N  NH1 . ARG B 1 93  ? -28.224 -59.628 28.059  1.00 58.86  ? 66  ARG A NH1 1 
ATOM   3961 N  NH2 . ARG B 1 93  ? -29.396 -59.855 26.076  1.00 66.16  ? 66  ARG A NH2 1 
ATOM   3962 N  N   . GLY B 1 94  ? -21.446 -58.283 24.757  1.00 58.42  ? 67  GLY A N   1 
ATOM   3963 C  CA  . GLY B 1 94  ? -21.247 -57.180 23.820  1.00 59.28  ? 67  GLY A CA  1 
ATOM   3964 C  C   . GLY B 1 94  ? -20.297 -57.509 22.686  1.00 58.56  ? 67  GLY A C   1 
ATOM   3965 O  O   . GLY B 1 94  ? -20.514 -57.074 21.519  1.00 52.32  ? 67  GLY A O   1 
ATOM   3966 N  N   . PHE B 1 95  ? -19.235 -58.256 23.028  1.00 57.83  ? 68  PHE A N   1 
ATOM   3967 C  CA  . PHE B 1 95  ? -18.311 -58.791 22.020  1.00 60.20  ? 68  PHE A CA  1 
ATOM   3968 C  C   . PHE B 1 95  ? -19.055 -59.724 21.055  1.00 56.83  ? 68  PHE A C   1 
ATOM   3969 O  O   . PHE B 1 95  ? -18.902 -59.617 19.850  1.00 57.56  ? 68  PHE A O   1 
ATOM   3970 C  CB  . PHE B 1 95  ? -17.131 -59.502 22.674  1.00 67.14  ? 68  PHE A CB  1 
ATOM   3971 C  CG  . PHE B 1 95  ? -16.048 -59.914 21.700  1.00 76.46  ? 68  PHE A CG  1 
ATOM   3972 C  CD1 . PHE B 1 95  ? -15.263 -58.969 21.067  1.00 81.92  ? 68  PHE A CD1 1 
ATOM   3973 C  CD2 . PHE B 1 95  ? -15.804 -61.259 21.434  1.00 83.11  ? 68  PHE A CD2 1 
ATOM   3974 C  CE1 . PHE B 1 95  ? -14.272 -59.360 20.178  1.00 87.27  ? 68  PHE A CE1 1 
ATOM   3975 C  CE2 . PHE B 1 95  ? -14.814 -61.657 20.547  1.00 78.88  ? 68  PHE A CE2 1 
ATOM   3976 C  CZ  . PHE B 1 95  ? -14.051 -60.709 19.917  1.00 80.53  ? 68  PHE A CZ  1 
ATOM   3977 N  N   . ARG B 1 96  ? -19.906 -60.596 21.573  1.00 54.70  ? 69  ARG A N   1 
ATOM   3978 C  CA  . ARG B 1 96  ? -20.719 -61.431 20.697  1.00 57.77  ? 69  ARG A CA  1 
ATOM   3979 C  C   . ARG B 1 96  ? -21.583 -60.604 19.756  1.00 54.01  ? 69  ARG A C   1 
ATOM   3980 O  O   . ARG B 1 96  ? -21.688 -60.939 18.571  1.00 48.26  ? 69  ARG A O   1 
ATOM   3981 C  CB  . ARG B 1 96  ? -21.585 -62.414 21.490  1.00 61.58  ? 69  ARG A CB  1 
ATOM   3982 C  CG  . ARG B 1 96  ? -22.726 -62.997 20.679  1.00 63.90  ? 69  ARG A CG  1 
ATOM   3983 C  CD  . ARG B 1 96  ? -23.260 -64.289 21.280  1.00 70.74  ? 69  ARG A CD  1 
ATOM   3984 N  NE  . ARG B 1 96  ? -23.370 -64.281 22.744  1.00 72.23  ? 69  ARG A NE  1 
ATOM   3985 C  CZ  . ARG B 1 96  ? -24.462 -63.970 23.440  1.00 67.30  ? 69  ARG A CZ  1 
ATOM   3986 N  NH1 . ARG B 1 96  ? -25.583 -63.598 22.844  1.00 75.13  ? 69  ARG A NH1 1 
ATOM   3987 N  NH2 . ARG B 1 96  ? -24.421 -64.020 24.753  1.00 67.73  ? 69  ARG A NH2 1 
ATOM   3988 N  N   . TRP B 1 97  ? -22.215 -59.541 20.265  1.00 57.26  ? 70  TRP A N   1 
ATOM   3989 C  CA  . TRP B 1 97  ? -23.020 -58.672 19.382  1.00 56.81  ? 70  TRP A CA  1 
ATOM   3990 C  C   . TRP B 1 97  ? -22.179 -58.112 18.235  1.00 56.76  ? 70  TRP A C   1 
ATOM   3991 O  O   . TRP B 1 97  ? -22.592 -58.154 17.079  1.00 56.18  ? 70  TRP A O   1 
ATOM   3992 C  CB  . TRP B 1 97  ? -23.668 -57.511 20.126  1.00 59.24  ? 70  TRP A CB  1 
ATOM   3993 C  CG  . TRP B 1 97  ? -24.644 -57.911 21.177  1.00 58.16  ? 70  TRP A CG  1 
ATOM   3994 C  CD1 . TRP B 1 97  ? -25.196 -59.121 21.356  1.00 56.06  ? 70  TRP A CD1 1 
ATOM   3995 C  CD2 . TRP B 1 97  ? -25.186 -57.065 22.184  1.00 56.42  ? 70  TRP A CD2 1 
ATOM   3996 N  NE1 . TRP B 1 97  ? -26.040 -59.106 22.430  1.00 54.82  ? 70  TRP A NE1 1 
ATOM   3997 C  CE2 . TRP B 1 97  ? -26.048 -57.850 22.963  1.00 58.87  ? 70  TRP A CE2 1 
ATOM   3998 C  CE3 . TRP B 1 97  ? -25.023 -55.718 22.504  1.00 52.11  ? 70  TRP A CE3 1 
ATOM   3999 C  CZ2 . TRP B 1 97  ? -26.760 -57.333 24.044  1.00 62.67  ? 70  TRP A CZ2 1 
ATOM   4000 C  CZ3 . TRP B 1 97  ? -25.721 -55.207 23.568  1.00 58.88  ? 70  TRP A CZ3 1 
ATOM   4001 C  CH2 . TRP B 1 97  ? -26.583 -56.010 24.330  1.00 60.94  ? 70  TRP A CH2 1 
ATOM   4002 N  N   . LEU B 1 98  ? -21.000 -57.597 18.559  1.00 54.22  ? 71  LEU A N   1 
ATOM   4003 C  CA  . LEU B 1 98  ? -20.111 -57.130 17.536  1.00 57.78  ? 71  LEU A CA  1 
ATOM   4004 C  C   . LEU B 1 98  ? -19.734 -58.276 16.577  1.00 60.63  ? 71  LEU A C   1 
ATOM   4005 O  O   . LEU B 1 98  ? -19.565 -58.044 15.362  1.00 54.14  ? 71  LEU A O   1 
ATOM   4006 C  CB  . LEU B 1 98  ? -18.880 -56.497 18.169  1.00 62.59  ? 71  LEU A CB  1 
ATOM   4007 C  CG  . LEU B 1 98  ? -17.708 -56.285 17.210  1.00 68.13  ? 71  LEU A CG  1 
ATOM   4008 C  CD1 . LEU B 1 98  ? -16.743 -55.272 17.810  1.00 71.61  ? 71  LEU A CD1 1 
ATOM   4009 C  CD2 . LEU B 1 98  ? -16.973 -57.590 16.944  1.00 67.50  ? 71  LEU A CD2 1 
ATOM   4010 N  N   . GLN B 1 99  ? -19.595 -59.498 17.112  1.00 61.66  ? 72  GLN A N   1 
ATOM   4011 C  CA  . GLN B 1 99  ? -19.255 -60.677 16.274  1.00 66.37  ? 72  GLN A CA  1 
ATOM   4012 C  C   . GLN B 1 99  ? -20.367 -60.976 15.257  1.00 65.75  ? 72  GLN A C   1 
ATOM   4013 O  O   . GLN B 1 99  ? -20.073 -61.216 14.077  1.00 62.14  ? 72  GLN A O   1 
ATOM   4014 C  CB  . GLN B 1 99  ? -18.933 -61.933 17.107  1.00 65.11  ? 72  GLN A CB  1 
ATOM   4015 C  CG  . GLN B 1 99  ? -17.604 -61.910 17.848  1.00 68.49  ? 72  GLN A CG  1 
ATOM   4016 C  CD  . GLN B 1 99  ? -16.440 -62.411 17.015  1.00 74.97  ? 72  GLN A CD  1 
ATOM   4017 O  OE1 . GLN B 1 99  ? -15.819 -63.420 17.352  1.00 84.88  ? 72  GLN A OE1 1 
ATOM   4018 N  NE2 . GLN B 1 99  ? -16.139 -61.716 15.923  1.00 71.29  ? 72  GLN A NE2 1 
ATOM   4019 N  N   . ALA B 1 100 ? -21.623 -60.933 15.717  1.00 63.07  ? 73  ALA A N   1 
ATOM   4020 C  CA  . ALA B 1 100 ? -22.797 -61.076 14.842  1.00 62.18  ? 73  ALA A CA  1 
ATOM   4021 C  C   . ALA B 1 100 ? -22.756 -60.127 13.646  1.00 61.67  ? 73  ALA A C   1 
ATOM   4022 O  O   . ALA B 1 100 ? -23.189 -60.480 12.544  1.00 54.38  ? 73  ALA A O   1 
ATOM   4023 C  CB  . ALA B 1 100 ? -24.071 -60.838 15.629  1.00 63.03  ? 73  ALA A CB  1 
ATOM   4024 N  N   . MET B 1 101 ? -22.249 -58.918 13.867  1.00 62.26  ? 74  MET A N   1 
ATOM   4025 C  CA  . MET B 1 101 ? -22.153 -57.954 12.778  1.00 68.88  ? 74  MET A CA  1 
ATOM   4026 C  C   . MET B 1 101 ? -21.137 -58.403 11.752  1.00 66.81  ? 74  MET A C   1 
ATOM   4027 O  O   . MET B 1 101 ? -21.416 -58.376 10.568  1.00 69.62  ? 74  MET A O   1 
ATOM   4028 C  CB  . MET B 1 101 ? -21.747 -56.557 13.264  1.00 67.52  ? 74  MET A CB  1 
ATOM   4029 C  CG  . MET B 1 101 ? -21.457 -55.617 12.100  1.00 68.05  ? 74  MET A CG  1 
ATOM   4030 S  SD  . MET B 1 101 ? -21.449 -53.891 12.549  1.00 70.78  ? 74  MET A SD  1 
ATOM   4031 C  CE  . MET B 1 101 ? -20.654 -53.115 11.155  1.00 66.37  ? 74  MET A CE  1 
ATOM   4032 N  N   . ILE B 1 102 ? -19.949 -58.763 12.226  1.00 70.94  ? 75  ILE A N   1 
ATOM   4033 C  CA  . ILE B 1 102 ? -18.862 -59.183 11.364  1.00 69.65  ? 75  ILE A CA  1 
ATOM   4034 C  C   . ILE B 1 102 ? -19.294 -60.437 10.611  1.00 76.37  ? 75  ILE A C   1 
ATOM   4035 O  O   . ILE B 1 102 ? -19.043 -60.537 9.395   1.00 75.16  ? 75  ILE A O   1 
ATOM   4036 C  CB  . ILE B 1 102 ? -17.582 -59.474 12.169  1.00 74.70  ? 75  ILE A CB  1 
ATOM   4037 C  CG1 . ILE B 1 102 ? -17.065 -58.195 12.836  1.00 79.89  ? 75  ILE A CG1 1 
ATOM   4038 C  CG2 . ILE B 1 102 ? -16.494 -60.029 11.259  1.00 79.33  ? 75  ILE A CG2 1 
ATOM   4039 C  CD1 . ILE B 1 102 ? -15.847 -58.399 13.720  1.00 79.51  ? 75  ILE A CD1 1 
ATOM   4040 N  N   . PHE B 1 103 ? -19.953 -61.366 11.331  1.00 69.30  ? 76  PHE A N   1 
ATOM   4041 C  CA  . PHE B 1 103 ? -20.478 -62.606 10.743  1.00 69.50  ? 76  PHE A CA  1 
ATOM   4042 C  C   . PHE B 1 103 ? -21.378 -62.301 9.569   1.00 67.08  ? 76  PHE A C   1 
ATOM   4043 O  O   . PHE B 1 103 ? -21.209 -62.839 8.485   1.00 70.18  ? 76  PHE A O   1 
ATOM   4044 C  CB  . PHE B 1 103 ? -21.274 -63.419 11.768  1.00 70.31  ? 76  PHE A CB  1 
ATOM   4045 C  CG  . PHE B 1 103 ? -21.774 -64.742 11.244  1.00 78.33  ? 76  PHE A CG  1 
ATOM   4046 C  CD1 . PHE B 1 103 ? -20.971 -65.880 11.304  1.00 77.76  ? 76  PHE A CD1 1 
ATOM   4047 C  CD2 . PHE B 1 103 ? -23.052 -64.858 10.693  1.00 82.74  ? 76  PHE A CD2 1 
ATOM   4048 C  CE1 . PHE B 1 103 ? -21.428 -67.095 10.829  1.00 75.56  ? 76  PHE A CE1 1 
ATOM   4049 C  CE2 . PHE B 1 103 ? -23.513 -66.076 10.212  1.00 80.49  ? 76  PHE A CE2 1 
ATOM   4050 C  CZ  . PHE B 1 103 ? -22.701 -67.193 10.280  1.00 75.49  ? 76  PHE A CZ  1 
ATOM   4051 N  N   . ALA B 1 104 ? -22.341 -61.428 9.797   1.00 68.14  ? 77  ALA A N   1 
ATOM   4052 C  CA  . ALA B 1 104 ? -23.351 -61.164 8.802   1.00 69.28  ? 77  ALA A CA  1 
ATOM   4053 C  C   . ALA B 1 104 ? -22.712 -60.558 7.573   1.00 70.74  ? 77  ALA A C   1 
ATOM   4054 O  O   . ALA B 1 104 ? -23.190 -60.794 6.470   1.00 72.11  ? 77  ALA A O   1 
ATOM   4055 C  CB  . ALA B 1 104 ? -24.412 -60.244 9.365   1.00 68.48  ? 77  ALA A CB  1 
ATOM   4056 N  N   . ILE B 1 105 ? -21.631 -59.802 7.762   1.00 66.67  ? 78  ILE A N   1 
ATOM   4057 C  CA  . ILE B 1 105 ? -20.953 -59.135 6.650   1.00 73.48  ? 78  ILE A CA  1 
ATOM   4058 C  C   . ILE B 1 105 ? -20.173 -60.120 5.796   1.00 75.87  ? 78  ILE A C   1 
ATOM   4059 O  O   . ILE B 1 105 ? -20.254 -60.071 4.573   1.00 82.48  ? 78  ILE A O   1 
ATOM   4060 C  CB  . ILE B 1 105 ? -20.011 -57.999 7.126   1.00 70.88  ? 78  ILE A CB  1 
ATOM   4061 C  CG1 . ILE B 1 105 ? -20.832 -56.781 7.547   1.00 68.06  ? 78  ILE A CG1 1 
ATOM   4062 C  CG2 . ILE B 1 105 ? -19.038 -57.565 6.035   1.00 66.21  ? 78  ILE A CG2 1 
ATOM   4063 C  CD1 . ILE B 1 105 ? -20.064 -55.826 8.445   1.00 67.16  ? 78  ILE A CD1 1 
ATOM   4064 N  N   . GLU B 1 106 ? -19.409 -61.000 6.426   1.00 82.25  ? 79  GLU A N   1 
ATOM   4065 C  CA  . GLU B 1 106 ? -18.639 -61.980 5.665   1.00 84.09  ? 79  GLU A CA  1 
ATOM   4066 C  C   . GLU B 1 106 ? -19.597 -62.902 4.899   1.00 84.82  ? 79  GLU A C   1 
ATOM   4067 O  O   . GLU B 1 106 ? -19.528 -62.996 3.678   1.00 94.62  ? 79  GLU A O   1 
ATOM   4068 C  CB  . GLU B 1 106 ? -17.629 -62.704 6.564   1.00 85.17  ? 79  GLU A CB  1 
ATOM   4069 C  CG  . GLU B 1 106 ? -16.317 -61.912 6.632   1.00 94.88  ? 79  GLU A CG  1 
ATOM   4070 C  CD  . GLU B 1 106 ? -15.442 -62.142 7.870   1.00 97.18  ? 79  GLU A CD  1 
ATOM   4071 O  OE1 . GLU B 1 106 ? -15.658 -63.107 8.646   1.00 93.42  ? 79  GLU A OE1 1 
ATOM   4072 O  OE2 . GLU B 1 106 ? -14.503 -61.324 8.054   1.00 100.57 ? 79  GLU A OE2 1 
ATOM   4073 N  N   . GLU B 1 107 ? -20.553 -63.497 5.593   1.00 82.44  ? 80  GLU A N   1 
ATOM   4074 C  CA  . GLU B 1 107 ? -21.664 -64.205 4.934   1.00 80.99  ? 80  GLU A CA  1 
ATOM   4075 C  C   . GLU B 1 107 ? -22.262 -63.481 3.703   1.00 81.26  ? 80  GLU A C   1 
ATOM   4076 O  O   . GLU B 1 107 ? -22.638 -64.112 2.721   1.00 91.47  ? 80  GLU A O   1 
ATOM   4077 C  CB  . GLU B 1 107 ? -22.776 -64.484 5.958   1.00 74.00  ? 80  GLU A CB  1 
ATOM   4078 C  CG  . GLU B 1 107 ? -23.987 -65.220 5.398   1.00 72.37  ? 80  GLU A CG  1 
ATOM   4079 C  CD  . GLU B 1 107 ? -24.909 -65.722 6.495   1.00 74.33  ? 80  GLU A CD  1 
ATOM   4080 O  OE1 . GLU B 1 107 ? -26.130 -65.420 6.442   1.00 65.53  ? 80  GLU A OE1 1 
ATOM   4081 O  OE2 . GLU B 1 107 ? -24.400 -66.396 7.424   1.00 75.39  ? 80  GLU A OE2 1 
ATOM   4082 N  N   . ILE B 1 108 ? -22.383 -62.167 3.771   1.00 87.38  ? 81  ILE A N   1 
ATOM   4083 C  CA  . ILE B 1 108 ? -22.997 -61.404 2.688   1.00 88.90  ? 81  ILE A CA  1 
ATOM   4084 C  C   . ILE B 1 108 ? -22.012 -61.221 1.543   1.00 88.74  ? 81  ILE A C   1 
ATOM   4085 O  O   . ILE B 1 108 ? -22.390 -61.188 0.366   1.00 87.86  ? 81  ILE A O   1 
ATOM   4086 C  CB  . ILE B 1 108 ? -23.540 -60.057 3.206   1.00 85.14  ? 81  ILE A CB  1 
ATOM   4087 C  CG1 . ILE B 1 108 ? -24.857 -60.310 3.941   1.00 87.23  ? 81  ILE A CG1 1 
ATOM   4088 C  CG2 . ILE B 1 108 ? -23.766 -59.061 2.074   1.00 79.73  ? 81  ILE A CG2 1 
ATOM   4089 C  CD1 . ILE B 1 108 ? -25.309 -59.137 4.777   1.00 90.50  ? 81  ILE A CD1 1 
ATOM   4090 N  N   . ASN B 1 109 ? -20.745 -61.107 1.892   1.00 84.71  ? 82  ASN A N   1 
ATOM   4091 C  CA  . ASN B 1 109 ? -19.715 -61.106 0.886   1.00 87.28  ? 82  ASN A CA  1 
ATOM   4092 C  C   . ASN B 1 109 ? -19.602 -62.488 0.211   1.00 92.70  ? 82  ASN A C   1 
ATOM   4093 O  O   . ASN B 1 109 ? -19.534 -62.580 -1.030  1.00 87.85  ? 82  ASN A O   1 
ATOM   4094 C  CB  . ASN B 1 109 ? -18.415 -60.608 1.505   1.00 79.18  ? 82  ASN A CB  1 
ATOM   4095 C  CG  . ASN B 1 109 ? -18.429 -59.108 1.689   1.00 78.83  ? 82  ASN A CG  1 
ATOM   4096 O  OD1 . ASN B 1 109 ? -19.174 -58.405 1.000   1.00 78.65  ? 82  ASN A OD1 1 
ATOM   4097 N  ND2 . ASN B 1 109 ? -17.618 -58.605 2.606   1.00 77.97  ? 82  ASN A ND2 1 
ATOM   4098 N  N   . SER B 1 110 ? -19.650 -63.542 1.029   1.00 86.18  ? 83  SER A N   1 
ATOM   4099 C  CA  . SER B 1 110 ? -19.702 -64.929 0.553   1.00 81.72  ? 83  SER A CA  1 
ATOM   4100 C  C   . SER B 1 110 ? -20.897 -65.213 -0.339  1.00 84.64  ? 83  SER A C   1 
ATOM   4101 O  O   . SER B 1 110 ? -20.811 -66.034 -1.226  1.00 88.44  ? 83  SER A O   1 
ATOM   4102 C  CB  . SER B 1 110 ? -19.753 -65.901 1.733   1.00 77.62  ? 83  SER A CB  1 
ATOM   4103 O  OG  . SER B 1 110 ? -18.538 -65.880 2.461   1.00 74.49  ? 83  SER A OG  1 
ATOM   4104 N  N   . SER B 1 111 ? -22.028 -64.570 -0.090  1.00 98.03  ? 84  SER A N   1 
ATOM   4105 C  CA  . SER B 1 111 ? -23.173 -64.777 -0.958  1.00 107.61 ? 84  SER A CA  1 
ATOM   4106 C  C   . SER B 1 111 ? -22.871 -64.152 -2.320  1.00 109.06 ? 84  SER A C   1 
ATOM   4107 O  O   . SER B 1 111 ? -22.502 -62.981 -2.412  1.00 111.88 ? 84  SER A O   1 
ATOM   4108 C  CB  . SER B 1 111 ? -24.454 -64.195 -0.364  1.00 110.05 ? 84  SER A CB  1 
ATOM   4109 O  OG  . SER B 1 111 ? -25.573 -64.588 -1.139  1.00 114.58 ? 84  SER A OG  1 
ATOM   4110 N  N   . PRO B 1 112 ? -22.985 -64.951 -3.383  1.00 116.42 ? 85  PRO A N   1 
ATOM   4111 C  CA  . PRO B 1 112 ? -22.799 -64.391 -4.718  1.00 115.15 ? 85  PRO A CA  1 
ATOM   4112 C  C   . PRO B 1 112 ? -24.004 -63.545 -5.141  1.00 116.37 ? 85  PRO A C   1 
ATOM   4113 O  O   . PRO B 1 112 ? -23.820 -62.471 -5.730  1.00 95.82  ? 85  PRO A O   1 
ATOM   4114 C  CB  . PRO B 1 112 ? -22.678 -65.635 -5.594  1.00 117.30 ? 85  PRO A CB  1 
ATOM   4115 C  CG  . PRO B 1 112 ? -23.440 -66.705 -4.866  1.00 113.07 ? 85  PRO A CG  1 
ATOM   4116 C  CD  . PRO B 1 112 ? -23.336 -66.388 -3.406  1.00 109.90 ? 85  PRO A CD  1 
ATOM   4117 N  N   . ALA B 1 113 ? -25.204 -64.046 -4.805  1.00 117.49 ? 86  ALA A N   1 
ATOM   4118 C  CA  . ALA B 1 113 ? -26.507 -63.458 -5.151  1.00 122.36 ? 86  ALA A CA  1 
ATOM   4119 C  C   . ALA B 1 113 ? -26.675 -62.028 -4.653  1.00 131.80 ? 86  ALA A C   1 
ATOM   4120 O  O   . ALA B 1 113 ? -27.026 -61.122 -5.416  1.00 131.91 ? 86  ALA A O   1 
ATOM   4121 C  CB  . ALA B 1 113 ? -27.624 -64.319 -4.567  1.00 119.20 ? 86  ALA A CB  1 
ATOM   4122 N  N   . LEU B 1 114 ? -26.433 -61.845 -3.359  1.00 128.74 ? 87  LEU A N   1 
ATOM   4123 C  CA  . LEU B 1 114 ? -26.557 -60.544 -2.706  1.00 107.61 ? 87  LEU A CA  1 
ATOM   4124 C  C   . LEU B 1 114 ? -25.306 -59.674 -2.946  1.00 100.89 ? 87  LEU A C   1 
ATOM   4125 O  O   . LEU B 1 114 ? -24.199 -60.019 -2.516  1.00 91.37  ? 87  LEU A O   1 
ATOM   4126 C  CB  . LEU B 1 114 ? -26.785 -60.762 -1.210  1.00 99.42  ? 87  LEU A CB  1 
ATOM   4127 C  CG  . LEU B 1 114 ? -27.489 -59.632 -0.482  1.00 99.24  ? 87  LEU A CG  1 
ATOM   4128 C  CD1 . LEU B 1 114 ? -28.952 -59.590 -0.893  1.00 103.69 ? 87  LEU A CD1 1 
ATOM   4129 C  CD2 . LEU B 1 114 ? -27.343 -59.793 1.026   1.00 100.72 ? 87  LEU A CD2 1 
ATOM   4130 N  N   . LEU B 1 115 ? -25.494 -58.552 -3.639  1.00 100.13 ? 88  LEU A N   1 
ATOM   4131 C  CA  . LEU B 1 115 ? -24.403 -57.632 -3.966  1.00 103.38 ? 88  LEU A CA  1 
ATOM   4132 C  C   . LEU B 1 115 ? -23.209 -58.344 -4.596  1.00 109.61 ? 88  LEU A C   1 
ATOM   4133 O  O   . LEU B 1 115 ? -22.221 -58.641 -3.916  1.00 112.05 ? 88  LEU A O   1 
ATOM   4134 C  CB  . LEU B 1 115 ? -23.947 -56.862 -2.726  1.00 100.29 ? 88  LEU A CB  1 
ATOM   4135 C  CG  . LEU B 1 115 ? -24.973 -55.918 -2.102  1.00 100.44 ? 88  LEU A CG  1 
ATOM   4136 C  CD1 . LEU B 1 115 ? -24.335 -55.169 -0.940  1.00 96.81  ? 88  LEU A CD1 1 
ATOM   4137 C  CD2 . LEU B 1 115 ? -25.538 -54.950 -3.132  1.00 97.69  ? 88  LEU A CD2 1 
ATOM   4138 N  N   . PRO B 1 116 ? -23.303 -58.631 -5.899  1.00 113.57 ? 89  PRO A N   1 
ATOM   4139 C  CA  . PRO B 1 116 ? -22.218 -59.351 -6.570  1.00 118.66 ? 89  PRO A CA  1 
ATOM   4140 C  C   . PRO B 1 116 ? -20.994 -58.492 -6.911  1.00 108.76 ? 89  PRO A C   1 
ATOM   4141 O  O   . PRO B 1 116 ? -19.875 -58.875 -6.581  1.00 105.86 ? 89  PRO A O   1 
ATOM   4142 C  CB  . PRO B 1 116 ? -22.884 -59.916 -7.831  1.00 118.60 ? 89  PRO A CB  1 
ATOM   4143 C  CG  . PRO B 1 116 ? -24.104 -59.097 -8.037  1.00 116.87 ? 89  PRO A CG  1 
ATOM   4144 C  CD  . PRO B 1 116 ? -24.534 -58.576 -6.705  1.00 112.56 ? 89  PRO A CD  1 
ATOM   4145 N  N   . ASN B 1 117 ? -21.191 -57.341 -7.543  1.00 102.73 ? 90  ASN A N   1 
ATOM   4146 C  CA  . ASN B 1 117 ? -20.050 -56.519 -7.948  1.00 105.38 ? 90  ASN A CA  1 
ATOM   4147 C  C   . ASN B 1 117 ? -19.160 -56.040 -6.779  1.00 107.50 ? 90  ASN A C   1 
ATOM   4148 O  O   . ASN B 1 117 ? -17.984 -55.733 -6.989  1.00 104.93 ? 90  ASN A O   1 
ATOM   4149 C  CB  . ASN B 1 117 ? -20.526 -55.312 -8.770  1.00 103.84 ? 90  ASN A CB  1 
ATOM   4150 N  N   . LEU B 1 118 ? -19.705 -56.008 -5.558  1.00 104.30 ? 91  LEU A N   1 
ATOM   4151 C  CA  . LEU B 1 118 ? -19.124 -55.225 -4.454  1.00 97.62  ? 91  LEU A CA  1 
ATOM   4152 C  C   . LEU B 1 118 ? -18.823 -56.012 -3.182  1.00 85.36  ? 91  LEU A C   1 
ATOM   4153 O  O   . LEU B 1 118 ? -19.440 -57.045 -2.921  1.00 72.65  ? 91  LEU A O   1 
ATOM   4154 C  CB  . LEU B 1 118 ? -20.102 -54.113 -4.091  1.00 108.49 ? 91  LEU A CB  1 
ATOM   4155 C  CG  . LEU B 1 118 ? -20.755 -53.415 -5.293  1.00 125.31 ? 91  LEU A CG  1 
ATOM   4156 C  CD1 . LEU B 1 118 ? -21.842 -52.451 -4.842  1.00 123.81 ? 91  LEU A CD1 1 
ATOM   4157 C  CD2 . LEU B 1 118 ? -19.705 -52.688 -6.129  1.00 135.75 ? 91  LEU A CD2 1 
ATOM   4158 N  N   . THR B 1 119 ? -17.876 -55.513 -2.390  1.00 80.13  ? 92  THR A N   1 
ATOM   4159 C  CA  . THR B 1 119 ? -17.671 -56.009 -1.018  1.00 92.95  ? 92  THR A CA  1 
ATOM   4160 C  C   . THR B 1 119 ? -18.057 -54.954 0.021   1.00 90.87  ? 92  THR A C   1 
ATOM   4161 O  O   . THR B 1 119 ? -17.847 -53.744 -0.175  1.00 80.96  ? 92  THR A O   1 
ATOM   4162 C  CB  . THR B 1 119 ? -16.211 -56.427 -0.697  1.00 95.45  ? 92  THR A CB  1 
ATOM   4163 O  OG1 . THR B 1 119 ? -15.320 -55.356 -1.032  1.00 107.06 ? 92  THR A OG1 1 
ATOM   4164 C  CG2 . THR B 1 119 ? -15.807 -57.727 -1.427  1.00 93.92  ? 92  THR A CG2 1 
ATOM   4165 N  N   . LEU B 1 120 ? -18.604 -55.449 1.131   1.00 82.69  ? 93  LEU A N   1 
ATOM   4166 C  CA  . LEU B 1 120 ? -18.902 -54.639 2.292   1.00 79.54  ? 93  LEU A CA  1 
ATOM   4167 C  C   . LEU B 1 120 ? -17.747 -54.658 3.267   1.00 75.81  ? 93  LEU A C   1 
ATOM   4168 O  O   . LEU B 1 120 ? -17.287 -55.720 3.640   1.00 74.06  ? 93  LEU A O   1 
ATOM   4169 C  CB  . LEU B 1 120 ? -20.117 -55.202 3.012   1.00 79.79  ? 93  LEU A CB  1 
ATOM   4170 C  CG  . LEU B 1 120 ? -21.423 -55.099 2.247   1.00 78.55  ? 93  LEU A CG  1 
ATOM   4171 C  CD1 . LEU B 1 120 ? -22.525 -55.636 3.132   1.00 77.93  ? 93  LEU A CD1 1 
ATOM   4172 C  CD2 . LEU B 1 120 ? -21.714 -53.667 1.823   1.00 81.92  ? 93  LEU A CD2 1 
ATOM   4173 N  N   . GLY B 1 121 ? -17.306 -53.483 3.700   1.00 79.81  ? 94  GLY A N   1 
ATOM   4174 C  CA  . GLY B 1 121 ? -16.328 -53.366 4.783   1.00 80.18  ? 94  GLY A CA  1 
ATOM   4175 C  C   . GLY B 1 121 ? -16.948 -52.867 6.084   1.00 79.40  ? 94  GLY A C   1 
ATOM   4176 O  O   . GLY B 1 121 ? -18.154 -52.613 6.166   1.00 73.86  ? 94  GLY A O   1 
ATOM   4177 N  N   . TYR B 1 122 ? -16.112 -52.713 7.103   1.00 76.15  ? 95  TYR A N   1 
ATOM   4178 C  CA  . TYR B 1 122 ? -16.587 -52.287 8.395   1.00 74.43  ? 95  TYR A CA  1 
ATOM   4179 C  C   . TYR B 1 122 ? -15.535 -51.588 9.239   1.00 77.35  ? 95  TYR A C   1 
ATOM   4180 O  O   . TYR B 1 122 ? -14.384 -52.005 9.249   1.00 80.21  ? 95  TYR A O   1 
ATOM   4181 C  CB  . TYR B 1 122 ? -17.155 -53.486 9.154   1.00 77.24  ? 95  TYR A CB  1 
ATOM   4182 C  CG  . TYR B 1 122 ? -16.227 -54.675 9.382   1.00 77.09  ? 95  TYR A CG  1 
ATOM   4183 C  CD1 . TYR B 1 122 ? -15.211 -54.634 10.343  1.00 79.57  ? 95  TYR A CD1 1 
ATOM   4184 C  CD2 . TYR B 1 122 ? -16.421 -55.874 8.693   1.00 74.99  ? 95  TYR A CD2 1 
ATOM   4185 C  CE1 . TYR B 1 122 ? -14.388 -55.728 10.578  1.00 79.00  ? 95  TYR A CE1 1 
ATOM   4186 C  CE2 . TYR B 1 122 ? -15.611 -56.975 8.929   1.00 76.11  ? 95  TYR A CE2 1 
ATOM   4187 C  CZ  . TYR B 1 122 ? -14.592 -56.897 9.867   1.00 80.84  ? 95  TYR A CZ  1 
ATOM   4188 O  OH  . TYR B 1 122 ? -13.782 -57.996 10.096  1.00 85.65  ? 95  TYR A OH  1 
ATOM   4189 N  N   . ARG B 1 123 ? -15.940 -50.510 9.917   1.00 74.47  ? 96  ARG A N   1 
ATOM   4190 C  CA  . ARG B 1 123 ? -15.147 -49.875 10.972  1.00 73.13  ? 96  ARG A CA  1 
ATOM   4191 C  C   . ARG B 1 123 ? -16.025 -49.865 12.232  1.00 72.31  ? 96  ARG A C   1 
ATOM   4192 O  O   . ARG B 1 123 ? -17.108 -49.273 12.248  1.00 70.02  ? 96  ARG A O   1 
ATOM   4193 C  CB  . ARG B 1 123 ? -14.731 -48.451 10.574  1.00 79.74  ? 96  ARG A CB  1 
ATOM   4194 C  CG  . ARG B 1 123 ? -13.559 -48.390 9.603   1.00 90.80  ? 96  ARG A CG  1 
ATOM   4195 C  CD  . ARG B 1 123 ? -13.554 -47.121 8.752   1.00 97.17  ? 96  ARG A CD  1 
ATOM   4196 N  NE  . ARG B 1 123 ? -13.595 -45.906 9.571   1.00 105.01 ? 96  ARG A NE  1 
ATOM   4197 C  CZ  . ARG B 1 123 ? -14.143 -44.746 9.197   1.00 101.94 ? 96  ARG A CZ  1 
ATOM   4198 N  NH1 . ARG B 1 123 ? -14.728 -44.612 8.003   1.00 101.27 ? 96  ARG A NH1 1 
ATOM   4199 N  NH2 . ARG B 1 123 ? -14.125 -43.711 10.034  1.00 91.19  ? 96  ARG A NH2 1 
ATOM   4200 N  N   . ILE B 1 124 ? -15.547 -50.513 13.289  1.00 64.96  ? 97  ILE A N   1 
ATOM   4201 C  CA  . ILE B 1 124 ? -16.373 -50.842 14.428  1.00 57.33  ? 97  ILE A CA  1 
ATOM   4202 C  C   . ILE B 1 124 ? -15.712 -50.465 15.749  1.00 59.13  ? 97  ILE A C   1 
ATOM   4203 O  O   . ILE B 1 124 ? -14.701 -51.027 16.119  1.00 61.23  ? 97  ILE A O   1 
ATOM   4204 C  CB  . ILE B 1 124 ? -16.685 -52.346 14.441  1.00 54.21  ? 97  ILE A CB  1 
ATOM   4205 C  CG1 . ILE B 1 124 ? -17.428 -52.728 13.179  1.00 52.26  ? 97  ILE A CG1 1 
ATOM   4206 C  CG2 . ILE B 1 124 ? -17.557 -52.703 15.634  1.00 60.97  ? 97  ILE A CG2 1 
ATOM   4207 C  CD1 . ILE B 1 124 ? -17.926 -54.151 13.192  1.00 54.37  ? 97  ILE A CD1 1 
ATOM   4208 N  N   . PHE B 1 125 ? -16.326 -49.552 16.492  1.00 60.78  ? 98  PHE A N   1 
ATOM   4209 C  CA  . PHE B 1 125 ? -15.756 -49.088 17.735  1.00 57.88  ? 98  PHE A CA  1 
ATOM   4210 C  C   . PHE B 1 125 ? -16.526 -49.576 18.964  1.00 52.60  ? 98  PHE A C   1 
ATOM   4211 O  O   . PHE B 1 125 ? -17.591 -50.118 18.850  1.00 55.53  ? 98  PHE A O   1 
ATOM   4212 C  CB  . PHE B 1 125 ? -15.698 -47.555 17.734  1.00 58.38  ? 98  PHE A CB  1 
ATOM   4213 C  CG  . PHE B 1 125 ? -14.943 -46.971 16.587  1.00 59.64  ? 98  PHE A CG  1 
ATOM   4214 C  CD1 . PHE B 1 125 ? -13.574 -46.738 16.684  1.00 66.59  ? 98  PHE A CD1 1 
ATOM   4215 C  CD2 . PHE B 1 125 ? -15.595 -46.611 15.411  1.00 61.50  ? 98  PHE A CD2 1 
ATOM   4216 C  CE1 . PHE B 1 125 ? -12.870 -46.170 15.618  1.00 65.28  ? 98  PHE A CE1 1 
ATOM   4217 C  CE2 . PHE B 1 125 ? -14.893 -46.036 14.344  1.00 58.14  ? 98  PHE A CE2 1 
ATOM   4218 C  CZ  . PHE B 1 125 ? -13.537 -45.816 14.448  1.00 57.25  ? 98  PHE A CZ  1 
ATOM   4219 N  N   . ASP B 1 126 ? -15.923 -49.336 20.127  1.00 59.66  ? 99  ASP A N   1 
ATOM   4220 C  CA  . ASP B 1 126 ? -16.443 -49.585 21.468  1.00 57.18  ? 99  ASP A CA  1 
ATOM   4221 C  C   . ASP B 1 126 ? -16.990 -48.262 22.036  1.00 55.07  ? 99  ASP A C   1 
ATOM   4222 O  O   . ASP B 1 126 ? -16.301 -47.268 22.068  1.00 56.43  ? 99  ASP A O   1 
ATOM   4223 C  CB  . ASP B 1 126 ? -15.284 -50.102 22.366  1.00 53.57  ? 99  ASP A CB  1 
ATOM   4224 C  CG  . ASP B 1 126 ? -15.717 -50.430 23.820  1.00 63.30  ? 99  ASP A CG  1 
ATOM   4225 O  OD1 . ASP B 1 126 ? -16.938 -50.385 24.142  1.00 73.39  ? 99  ASP A OD1 1 
ATOM   4226 O  OD2 . ASP B 1 126 ? -14.827 -50.741 24.668  1.00 62.79  ? 99  ASP A OD2 1 
ATOM   4227 N  N   . THR B 1 127 ? -18.220 -48.268 22.520  1.00 59.93  ? 100 THR A N   1 
ATOM   4228 C  CA  . THR B 1 127 ? -18.799 -47.099 23.193  1.00 59.88  ? 100 THR A CA  1 
ATOM   4229 C  C   . THR B 1 127 ? -18.585 -47.080 24.702  1.00 57.50  ? 100 THR A C   1 
ATOM   4230 O  O   . THR B 1 127 ? -18.774 -46.044 25.338  1.00 56.48  ? 100 THR A O   1 
ATOM   4231 C  CB  . THR B 1 127 ? -20.308 -47.096 23.013  1.00 55.80  ? 100 THR A CB  1 
ATOM   4232 O  OG1 . THR B 1 127 ? -20.823 -48.329 23.538  1.00 54.65  ? 100 THR A OG1 1 
ATOM   4233 C  CG2 . THR B 1 127 ? -20.656 -46.960 21.552  1.00 53.61  ? 100 THR A CG2 1 
ATOM   4234 N  N   . CYS B 1 128 ? -18.256 -48.227 25.278  1.00 55.65  ? 101 CYS A N   1 
ATOM   4235 C  CA  . CYS B 1 128 ? -18.204 -48.366 26.727  1.00 60.92  ? 101 CYS A CA  1 
ATOM   4236 C  C   . CYS B 1 128 ? -19.497 -47.903 27.414  1.00 57.85  ? 101 CYS A C   1 
ATOM   4237 O  O   . CYS B 1 128 ? -19.442 -47.494 28.566  1.00 59.25  ? 101 CYS A O   1 
ATOM   4238 C  CB  . CYS B 1 128 ? -16.983 -47.621 27.284  1.00 63.29  ? 101 CYS A CB  1 
ATOM   4239 S  SG  . CYS B 1 128 ? -15.513 -48.197 26.400  1.00 79.55  ? 101 CYS A SG  1 
ATOM   4240 N  N   . ASN B 1 129 ? -20.644 -48.017 26.722  1.00 52.79  ? 102 ASN A N   1 
ATOM   4241 C  CA  . ASN B 1 129 ? -21.937 -47.404 27.140  1.00 55.73  ? 102 ASN A CA  1 
ATOM   4242 C  C   . ASN B 1 129 ? -21.834 -45.909 27.462  1.00 49.78  ? 102 ASN A C   1 
ATOM   4243 O  O   . ASN B 1 129 ? -22.466 -45.464 28.385  1.00 53.38  ? 102 ASN A O   1 
ATOM   4244 C  CB  . ASN B 1 129 ? -22.575 -48.071 28.382  1.00 53.34  ? 102 ASN A CB  1 
ATOM   4245 C  CG  . ASN B 1 129 ? -23.034 -49.483 28.137  1.00 59.00  ? 102 ASN A CG  1 
ATOM   4246 O  OD1 . ASN B 1 129 ? -23.756 -49.778 27.179  1.00 55.54  ? 102 ASN A OD1 1 
ATOM   4247 N  ND2 . ASN B 1 129 ? -22.632 -50.378 29.034  1.00 67.67  ? 102 ASN A ND2 1 
ATOM   4248 N  N   . THR B 1 130 ? -21.058 -45.156 26.700  1.00 46.57  ? 103 THR A N   1 
ATOM   4249 C  CA  . THR B 1 130 ? -20.708 -43.788 27.059  1.00 49.44  ? 103 THR A CA  1 
ATOM   4250 C  C   . THR B 1 130 ? -20.962 -42.889 25.843  1.00 50.12  ? 103 THR A C   1 
ATOM   4251 O  O   . THR B 1 130 ? -20.607 -43.225 24.711  1.00 51.66  ? 103 THR A O   1 
ATOM   4252 C  CB  . THR B 1 130 ? -19.241 -43.707 27.571  1.00 53.81  ? 103 THR A CB  1 
ATOM   4253 O  OG1 . THR B 1 130 ? -19.170 -44.170 28.921  1.00 56.23  ? 103 THR A OG1 1 
ATOM   4254 C  CG2 . THR B 1 130 ? -18.696 -42.325 27.581  1.00 60.04  ? 103 THR A CG2 1 
ATOM   4255 N  N   . VAL B 1 131 ? -21.617 -41.757 26.085  1.00 48.89  ? 104 VAL A N   1 
ATOM   4256 C  CA  . VAL B 1 131 ? -21.840 -40.795 25.027  1.00 49.22  ? 104 VAL A CA  1 
ATOM   4257 C  C   . VAL B 1 131 ? -20.507 -40.378 24.465  1.00 47.54  ? 104 VAL A C   1 
ATOM   4258 O  O   . VAL B 1 131 ? -20.339 -40.390 23.259  1.00 50.51  ? 104 VAL A O   1 
ATOM   4259 C  CB  . VAL B 1 131 ? -22.626 -39.559 25.503  1.00 48.03  ? 104 VAL A CB  1 
ATOM   4260 C  CG1 . VAL B 1 131 ? -22.619 -38.482 24.455  1.00 47.29  ? 104 VAL A CG1 1 
ATOM   4261 C  CG2 . VAL B 1 131 ? -24.056 -39.950 25.789  1.00 50.71  ? 104 VAL A CG2 1 
ATOM   4262 N  N   . SER B 1 132 ? -19.564 -40.035 25.338  1.00 45.93  ? 105 SER A N   1 
ATOM   4263 C  CA  . SER B 1 132 ? -18.313 -39.476 24.879  1.00 49.84  ? 105 SER A CA  1 
ATOM   4264 C  C   . SER B 1 132 ? -17.594 -40.424 23.915  1.00 50.80  ? 105 SER A C   1 
ATOM   4265 O  O   . SER B 1 132 ? -17.271 -40.019 22.820  1.00 51.73  ? 105 SER A O   1 
ATOM   4266 C  CB  . SER B 1 132 ? -17.430 -38.965 26.045  1.00 53.10  ? 105 SER A CB  1 
ATOM   4267 O  OG  . SER B 1 132 ? -16.967 -39.993 26.924  1.00 61.69  ? 105 SER A OG  1 
ATOM   4268 N  N   . LYS B 1 133 ? -17.410 -41.686 24.275  1.00 56.68  ? 106 LYS A N   1 
ATOM   4269 C  CA  . LYS B 1 133 ? -16.702 -42.638 23.402  1.00 59.21  ? 106 LYS A CA  1 
ATOM   4270 C  C   . LYS B 1 133 ? -17.466 -42.843 22.104  1.00 57.93  ? 106 LYS A C   1 
ATOM   4271 O  O   . LYS B 1 133 ? -16.887 -42.845 21.043  1.00 59.52  ? 106 LYS A O   1 
ATOM   4272 C  CB  . LYS B 1 133 ? -16.524 -44.011 24.066  1.00 62.94  ? 106 LYS A CB  1 
ATOM   4273 C  CG  . LYS B 1 133 ? -15.808 -44.036 25.410  1.00 61.51  ? 106 LYS A CG  1 
ATOM   4274 C  CD  . LYS B 1 133 ? -14.313 -43.998 25.274  1.00 69.40  ? 106 LYS A CD  1 
ATOM   4275 C  CE  . LYS B 1 133 ? -13.662 -43.767 26.636  1.00 84.80  ? 106 LYS A CE  1 
ATOM   4276 N  NZ  . LYS B 1 133 ? -12.207 -43.432 26.542  1.00 90.59  ? 106 LYS A NZ  1 
ATOM   4277 N  N   . ALA B 1 134 ? -18.778 -43.001 22.180  1.00 65.71  ? 107 ALA A N   1 
ATOM   4278 C  CA  . ALA B 1 134 ? -19.587 -43.118 20.965  1.00 60.48  ? 107 ALA A CA  1 
ATOM   4279 C  C   . ALA B 1 134 ? -19.452 -41.928 20.044  1.00 61.58  ? 107 ALA A C   1 
ATOM   4280 O  O   . ALA B 1 134 ? -19.494 -42.112 18.839  1.00 67.47  ? 107 ALA A O   1 
ATOM   4281 C  CB  . ALA B 1 134 ? -21.036 -43.312 21.303  1.00 59.68  ? 107 ALA A CB  1 
ATOM   4282 N  N   . LEU B 1 135 ? -19.302 -40.716 20.583  1.00 62.67  ? 108 LEU A N   1 
ATOM   4283 C  CA  . LEU B 1 135 ? -19.158 -39.520 19.732  1.00 61.98  ? 108 LEU A CA  1 
ATOM   4284 C  C   . LEU B 1 135 ? -17.760 -39.361 19.102  1.00 61.99  ? 108 LEU A C   1 
ATOM   4285 O  O   . LEU B 1 135 ? -17.649 -38.894 17.972  1.00 64.18  ? 108 LEU A O   1 
ATOM   4286 C  CB  . LEU B 1 135 ? -19.528 -38.235 20.478  1.00 65.09  ? 108 LEU A CB  1 
ATOM   4287 C  CG  . LEU B 1 135 ? -20.990 -37.792 20.602  1.00 66.95  ? 108 LEU A CG  1 
ATOM   4288 C  CD1 . LEU B 1 135 ? -21.046 -36.352 21.101  1.00 71.20  ? 108 LEU A CD1 1 
ATOM   4289 C  CD2 . LEU B 1 135 ? -21.756 -37.889 19.298  1.00 67.52  ? 108 LEU A CD2 1 
ATOM   4290 N  N   . GLU B 1 136 ? -16.697 -39.707 19.825  1.00 58.77  ? 109 GLU A N   1 
ATOM   4291 C  CA  . GLU B 1 136 ? -15.370 -39.755 19.218  1.00 58.11  ? 109 GLU A CA  1 
ATOM   4292 C  C   . GLU B 1 136 ? -15.468 -40.637 17.996  1.00 56.49  ? 109 GLU A C   1 
ATOM   4293 O  O   . GLU B 1 136 ? -15.106 -40.227 16.891  1.00 60.95  ? 109 GLU A O   1 
ATOM   4294 C  CB  . GLU B 1 136 ? -14.318 -40.335 20.169  1.00 65.16  ? 109 GLU A CB  1 
ATOM   4295 C  CG  . GLU B 1 136 ? -13.727 -39.345 21.181  1.00 72.35  ? 109 GLU A CG  1 
ATOM   4296 C  CD  . GLU B 1 136 ? -13.059 -40.016 22.394  1.00 80.24  ? 109 GLU A CD  1 
ATOM   4297 O  OE1 . GLU B 1 136 ? -12.913 -41.266 22.404  1.00 86.16  ? 109 GLU A OE1 1 
ATOM   4298 O  OE2 . GLU B 1 136 ? -12.678 -39.295 23.354  1.00 80.09  ? 109 GLU A OE2 1 
ATOM   4299 N  N   . ALA B 1 137 ? -15.970 -41.853 18.191  1.00 53.91  ? 110 ALA A N   1 
ATOM   4300 C  CA  . ALA B 1 137 ? -16.176 -42.801 17.080  1.00 54.61  ? 110 ALA A CA  1 
ATOM   4301 C  C   . ALA B 1 137 ? -16.992 -42.196 15.942  1.00 56.53  ? 110 ALA A C   1 
ATOM   4302 O  O   . ALA B 1 137 ? -16.634 -42.282 14.770  1.00 59.21  ? 110 ALA A O   1 
ATOM   4303 C  CB  . ALA B 1 137 ? -16.858 -44.059 17.593  1.00 53.63  ? 110 ALA A CB  1 
ATOM   4304 N  N   . THR B 1 138 ? -18.090 -41.555 16.305  1.00 57.77  ? 111 THR A N   1 
ATOM   4305 C  CA  . THR B 1 138 ? -18.990 -41.010 15.323  1.00 57.47  ? 111 THR A CA  1 
ATOM   4306 C  C   . THR B 1 138 ? -18.334 -39.918 14.503  1.00 55.72  ? 111 THR A C   1 
ATOM   4307 O  O   . THR B 1 138 ? -18.495 -39.880 13.290  1.00 60.12  ? 111 THR A O   1 
ATOM   4308 C  CB  . THR B 1 138 ? -20.292 -40.529 15.988  1.00 59.28  ? 111 THR A CB  1 
ATOM   4309 O  OG1 . THR B 1 138 ? -20.999 -41.667 16.513  1.00 58.32  ? 111 THR A OG1 1 
ATOM   4310 C  CG2 . THR B 1 138 ? -21.179 -39.869 14.982  1.00 61.31  ? 111 THR A CG2 1 
ATOM   4311 N  N   . LEU B 1 139 ? -17.576 -39.041 15.148  1.00 56.00  ? 112 LEU A N   1 
ATOM   4312 C  CA  . LEU B 1 139 ? -16.825 -38.016 14.423  1.00 54.36  ? 112 LEU A CA  1 
ATOM   4313 C  C   . LEU B 1 139 ? -15.924 -38.610 13.355  1.00 55.04  ? 112 LEU A C   1 
ATOM   4314 O  O   . LEU B 1 139 ? -15.790 -38.059 12.282  1.00 57.14  ? 112 LEU A O   1 
ATOM   4315 C  CB  . LEU B 1 139 ? -15.981 -37.197 15.373  1.00 55.82  ? 112 LEU A CB  1 
ATOM   4316 C  CG  . LEU B 1 139 ? -16.805 -36.194 16.154  1.00 56.71  ? 112 LEU A CG  1 
ATOM   4317 C  CD1 . LEU B 1 139 ? -16.040 -35.704 17.356  1.00 52.45  ? 112 LEU A CD1 1 
ATOM   4318 C  CD2 . LEU B 1 139 ? -17.202 -35.045 15.232  1.00 59.33  ? 112 LEU A CD2 1 
ATOM   4319 N  N   . SER B 1 140 ? -15.311 -39.743 13.622  1.00 55.89  ? 113 SER A N   1 
ATOM   4320 C  CA  . SER B 1 140 ? -14.547 -40.367 12.561  1.00 59.82  ? 113 SER A CA  1 
ATOM   4321 C  C   . SER B 1 140 ? -15.519 -40.903 11.478  1.00 60.20  ? 113 SER A C   1 
ATOM   4322 O  O   . SER B 1 140 ? -15.266 -40.737 10.291  1.00 63.96  ? 113 SER A O   1 
ATOM   4323 C  CB  . SER B 1 140 ? -13.591 -41.427 13.115  1.00 59.75  ? 113 SER A CB  1 
ATOM   4324 O  OG  . SER B 1 140 ? -14.237 -42.667 13.231  1.00 69.35  ? 113 SER A OG  1 
ATOM   4325 N  N   . PHE B 1 141 ? -16.654 -41.486 11.844  1.00 56.17  ? 114 PHE A N   1 
ATOM   4326 C  CA  . PHE B 1 141 ? -17.602 -41.906 10.793  1.00 57.47  ? 114 PHE A CA  1 
ATOM   4327 C  C   . PHE B 1 141 ? -17.935 -40.804 9.819   1.00 60.41  ? 114 PHE A C   1 
ATOM   4328 O  O   . PHE B 1 141 ? -18.008 -41.048 8.629   1.00 64.15  ? 114 PHE A O   1 
ATOM   4329 C  CB  . PHE B 1 141 ? -18.947 -42.390 11.345  1.00 59.59  ? 114 PHE A CB  1 
ATOM   4330 C  CG  . PHE B 1 141 ? -18.865 -43.651 12.135  1.00 64.40  ? 114 PHE A CG  1 
ATOM   4331 C  CD1 . PHE B 1 141 ? -17.936 -44.637 11.822  1.00 61.64  ? 114 PHE A CD1 1 
ATOM   4332 C  CD2 . PHE B 1 141 ? -19.729 -43.855 13.196  1.00 64.95  ? 114 PHE A CD2 1 
ATOM   4333 C  CE1 . PHE B 1 141 ? -17.872 -45.794 12.551  1.00 64.30  ? 114 PHE A CE1 1 
ATOM   4334 C  CE2 . PHE B 1 141 ? -19.662 -45.015 13.935  1.00 68.18  ? 114 PHE A CE2 1 
ATOM   4335 C  CZ  . PHE B 1 141 ? -18.730 -45.985 13.612  1.00 67.64  ? 114 PHE A CZ  1 
ATOM   4336 N  N   . VAL B 1 142 ? -18.194 -39.603 10.330  1.00 64.57  ? 115 VAL A N   1 
ATOM   4337 C  CA  . VAL B 1 142 ? -18.630 -38.506 9.466   1.00 61.69  ? 115 VAL A CA  1 
ATOM   4338 C  C   . VAL B 1 142 ? -17.478 -37.660 8.937   1.00 62.19  ? 115 VAL A C   1 
ATOM   4339 O  O   . VAL B 1 142 ? -17.735 -36.588 8.391   1.00 66.59  ? 115 VAL A O   1 
ATOM   4340 C  CB  . VAL B 1 142 ? -19.673 -37.568 10.148  1.00 57.28  ? 115 VAL A CB  1 
ATOM   4341 C  CG1 . VAL B 1 142 ? -20.885 -38.356 10.581  1.00 56.32  ? 115 VAL A CG1 1 
ATOM   4342 C  CG2 . VAL B 1 142 ? -19.087 -36.810 11.322  1.00 58.54  ? 115 VAL A CG2 1 
ATOM   4343 N  N   . ALA B 1 143 ? -16.233 -38.124 9.072   1.00 62.13  ? 116 ALA A N   1 
ATOM   4344 C  CA  . ALA B 1 143 ? -15.073 -37.233 8.904   1.00 68.98  ? 116 ALA A CA  1 
ATOM   4345 C  C   . ALA B 1 143 ? -15.041 -36.628 7.524   1.00 74.42  ? 116 ALA A C   1 
ATOM   4346 O  O   . ALA B 1 143 ? -14.845 -35.424 7.383   1.00 69.35  ? 116 ALA A O   1 
ATOM   4347 C  CB  . ALA B 1 143 ? -13.765 -37.969 9.175   1.00 71.66  ? 116 ALA A CB  1 
ATOM   4348 N  N   . GLN B 1 144 ? -15.251 -37.464 6.506   1.00 81.64  ? 117 GLN A N   1 
ATOM   4349 C  CA  . GLN B 1 144 ? -15.302 -36.961 5.143   1.00 90.90  ? 117 GLN A CA  1 
ATOM   4350 C  C   . GLN B 1 144 ? -16.403 -35.891 5.012   1.00 87.46  ? 117 GLN A C   1 
ATOM   4351 O  O   . GLN B 1 144 ? -16.114 -34.718 4.779   1.00 96.33  ? 117 GLN A O   1 
ATOM   4352 C  CB  . GLN B 1 144 ? -15.491 -38.101 4.134   1.00 96.95  ? 117 GLN A CB  1 
ATOM   4353 C  CG  . GLN B 1 144 ? -14.749 -37.856 2.825   1.00 104.86 ? 117 GLN A CG  1 
ATOM   4354 C  CD  . GLN B 1 144 ? -15.039 -36.484 2.231   1.00 101.21 ? 117 GLN A CD  1 
ATOM   4355 O  OE1 . GLN B 1 144 ? -16.184 -36.183 1.891   1.00 111.37 ? 117 GLN A OE1 1 
ATOM   4356 N  NE2 . GLN B 1 144 ? -14.007 -35.645 2.108   1.00 92.32  ? 117 GLN A NE2 1 
ATOM   4357 N  N   . ASN B 1 145 ? -17.646 -36.312 5.217   1.00 88.02  ? 118 ASN A N   1 
ATOM   4358 C  CA  . ASN B 1 145 ? -18.838 -35.446 5.156   1.00 86.20  ? 118 ASN A CA  1 
ATOM   4359 C  C   . ASN B 1 145 ? -18.692 -34.112 5.851   1.00 87.52  ? 118 ASN A C   1 
ATOM   4360 O  O   . ASN B 1 145 ? -19.149 -33.097 5.338   1.00 99.54  ? 118 ASN A O   1 
ATOM   4361 C  CB  . ASN B 1 145 ? -20.042 -36.137 5.812   1.00 84.57  ? 118 ASN A CB  1 
ATOM   4362 C  CG  . ASN B 1 145 ? -20.353 -37.488 5.206   1.00 82.23  ? 118 ASN A CG  1 
ATOM   4363 O  OD1 . ASN B 1 145 ? -21.323 -37.629 4.450   1.00 69.20  ? 118 ASN A OD1 1 
ATOM   4364 N  ND2 . ASN B 1 145 ? -19.526 -38.493 5.528   1.00 82.29  ? 118 ASN A ND2 1 
ATOM   4365 N  N   . LYS B 1 146 ? -18.104 -34.143 7.046   1.00 97.09  ? 119 LYS A N   1 
ATOM   4366 C  CA  . LYS B 1 146 ? -17.913 -32.954 7.904   1.00 97.72  ? 119 LYS A CA  1 
ATOM   4367 C  C   . LYS B 1 146 ? -16.993 -31.909 7.271   1.00 99.78  ? 119 LYS A C   1 
ATOM   4368 O  O   . LYS B 1 146 ? -17.310 -30.715 7.282   1.00 88.02  ? 119 LYS A O   1 
ATOM   4369 C  CB  . LYS B 1 146 ? -17.333 -33.384 9.259   1.00 93.20  ? 119 LYS A CB  1 
ATOM   4370 C  CG  . LYS B 1 146 ? -17.171 -32.256 10.266  1.00 88.83  ? 119 LYS A CG  1 
ATOM   4371 C  CD  . LYS B 1 146 ? -15.987 -32.503 11.191  1.00 87.15  ? 119 LYS A CD  1 
ATOM   4372 C  CE  . LYS B 1 146 ? -15.143 -31.246 11.370  1.00 92.74  ? 119 LYS A CE  1 
ATOM   4373 N  NZ  . LYS B 1 146 ? -15.391 -30.506 12.642  1.00 99.74  ? 119 LYS A NZ  1 
ATOM   4374 N  N   . ILE B 1 147 ? -15.864 -32.381 6.725   1.00 104.92 ? 120 ILE A N   1 
ATOM   4375 C  CA  . ILE B 1 147 ? -14.892 -31.536 6.028   1.00 112.45 ? 120 ILE A CA  1 
ATOM   4376 C  C   . ILE B 1 147 ? -15.540 -30.655 4.929   1.00 120.62 ? 120 ILE A C   1 
ATOM   4377 O  O   . ILE B 1 147 ? -15.087 -29.533 4.696   1.00 140.71 ? 120 ILE A O   1 
ATOM   4378 C  CB  . ILE B 1 147 ? -13.716 -32.375 5.458   1.00 101.52 ? 120 ILE A CB  1 
ATOM   4379 N  N   . ASP B 1 148 ? -16.601 -31.137 4.278   1.00 116.39 ? 121 ASP A N   1 
ATOM   4380 C  CA  . ASP B 1 148 ? -17.321 -30.342 3.264   1.00 118.69 ? 121 ASP A CA  1 
ATOM   4381 C  C   . ASP B 1 148 ? -17.906 -29.041 3.846   1.00 110.74 ? 121 ASP A C   1 
ATOM   4382 O  O   . ASP B 1 148 ? -18.817 -29.063 4.674   1.00 107.50 ? 121 ASP A O   1 
ATOM   4383 C  CB  . ASP B 1 148 ? -18.439 -31.172 2.590   1.00 119.08 ? 121 ASP A CB  1 
ATOM   4384 C  CG  . ASP B 1 148 ? -17.901 -32.339 1.726   1.00 110.49 ? 121 ASP A CG  1 
ATOM   4385 O  OD1 . ASP B 1 148 ? -16.668 -32.568 1.685   1.00 93.90  ? 121 ASP A OD1 1 
ATOM   4386 O  OD2 . ASP B 1 148 ? -18.729 -33.032 1.089   1.00 99.37  ? 121 ASP A OD2 1 
ATOM   4387 N  N   . SER B 1 164 ? -14.950 -43.310 4.147   1.00 79.73  ? 137 SER A N   1 
ATOM   4388 C  CA  . SER B 1 164 ? -16.307 -42.797 3.980   1.00 85.44  ? 137 SER A CA  1 
ATOM   4389 C  C   . SER B 1 164 ? -17.408 -43.825 4.335   1.00 94.48  ? 137 SER A C   1 
ATOM   4390 O  O   . SER B 1 164 ? -17.430 -44.928 3.784   1.00 117.52 ? 137 SER A O   1 
ATOM   4391 C  CB  . SER B 1 164 ? -16.500 -42.322 2.552   1.00 80.33  ? 137 SER A CB  1 
ATOM   4392 O  OG  . SER B 1 164 ? -17.858 -42.022 2.319   1.00 75.03  ? 137 SER A OG  1 
ATOM   4393 N  N   . THR B 1 165 ? -18.344 -43.427 5.208   1.00 88.61  ? 138 THR A N   1 
ATOM   4394 C  CA  . THR B 1 165 ? -19.277 -44.350 5.895   1.00 79.58  ? 138 THR A CA  1 
ATOM   4395 C  C   . THR B 1 165 ? -20.732 -44.234 5.401   1.00 67.75  ? 138 THR A C   1 
ATOM   4396 O  O   . THR B 1 165 ? -21.327 -43.161 5.409   1.00 66.86  ? 138 THR A O   1 
ATOM   4397 C  CB  . THR B 1 165 ? -19.223 -44.095 7.422   1.00 80.14  ? 138 THR A CB  1 
ATOM   4398 O  OG1 . THR B 1 165 ? -17.912 -44.405 7.905   1.00 82.52  ? 138 THR A OG1 1 
ATOM   4399 C  CG2 . THR B 1 165 ? -20.210 -44.952 8.166   1.00 84.42  ? 138 THR A CG2 1 
ATOM   4400 N  N   . ILE B 1 166 ? -21.319 -45.353 5.007   1.00 60.74  ? 139 ILE A N   1 
ATOM   4401 C  CA  . ILE B 1 166 ? -22.625 -45.335 4.343   1.00 62.05  ? 139 ILE A CA  1 
ATOM   4402 C  C   . ILE B 1 166 ? -23.810 -45.580 5.263   1.00 60.47  ? 139 ILE A C   1 
ATOM   4403 O  O   . ILE B 1 166 ? -24.960 -45.286 4.904   1.00 61.83  ? 139 ILE A O   1 
ATOM   4404 C  CB  . ILE B 1 166 ? -22.671 -46.376 3.197   1.00 63.77  ? 139 ILE A CB  1 
ATOM   4405 C  CG1 . ILE B 1 166 ? -23.344 -45.781 1.982   1.00 68.91  ? 139 ILE A CG1 1 
ATOM   4406 C  CG2 . ILE B 1 166 ? -23.406 -47.635 3.597   1.00 67.63  ? 139 ILE A CG2 1 
ATOM   4407 C  CD1 . ILE B 1 166 ? -22.583 -44.584 1.453   1.00 74.45  ? 139 ILE A CD1 1 
ATOM   4408 N  N   . ALA B 1 167 ? -23.539 -46.151 6.430   1.00 55.38  ? 140 ALA A N   1 
ATOM   4409 C  CA  . ALA B 1 167 ? -24.584 -46.528 7.365   1.00 52.87  ? 140 ALA A CA  1 
ATOM   4410 C  C   . ALA B 1 167 ? -23.906 -47.001 8.628   1.00 54.10  ? 140 ALA A C   1 
ATOM   4411 O  O   . ALA B 1 167 ? -22.710 -47.430 8.579   1.00 48.95  ? 140 ALA A O   1 
ATOM   4412 C  CB  . ALA B 1 167 ? -25.486 -47.632 6.799   1.00 50.83  ? 140 ALA A CB  1 
ATOM   4413 N  N   . VAL B 1 168 ? -24.646 -46.902 9.749   1.00 47.78  ? 141 VAL A N   1 
ATOM   4414 C  CA  . VAL B 1 168 ? -24.127 -47.360 11.039  1.00 48.13  ? 141 VAL A CA  1 
ATOM   4415 C  C   . VAL B 1 168 ? -25.090 -48.317 11.731  1.00 52.52  ? 141 VAL A C   1 
ATOM   4416 O  O   . VAL B 1 168 ? -26.324 -48.198 11.674  1.00 53.27  ? 141 VAL A O   1 
ATOM   4417 C  CB  . VAL B 1 168 ? -23.740 -46.194 11.985  1.00 48.20  ? 141 VAL A CB  1 
ATOM   4418 C  CG1 . VAL B 1 168 ? -23.043 -46.701 13.253  1.00 47.22  ? 141 VAL A CG1 1 
ATOM   4419 C  CG2 . VAL B 1 168 ? -22.812 -45.195 11.281  1.00 53.49  ? 141 VAL A CG2 1 
ATOM   4420 N  N   . VAL B 1 169 ? -24.488 -49.306 12.357  1.00 51.46  ? 142 VAL A N   1 
ATOM   4421 C  CA  . VAL B 1 169 ? -25.205 -50.209 13.190  1.00 55.29  ? 142 VAL A CA  1 
ATOM   4422 C  C   . VAL B 1 169 ? -24.936 -49.873 14.647  1.00 53.85  ? 142 VAL A C   1 
ATOM   4423 O  O   . VAL B 1 169 ? -23.822 -50.018 15.128  1.00 59.73  ? 142 VAL A O   1 
ATOM   4424 C  CB  . VAL B 1 169 ? -24.773 -51.639 12.891  1.00 58.38  ? 142 VAL A CB  1 
ATOM   4425 C  CG1 . VAL B 1 169 ? -25.355 -52.600 13.918  1.00 57.27  ? 142 VAL A CG1 1 
ATOM   4426 C  CG2 . VAL B 1 169 ? -25.210 -52.000 11.473  1.00 61.18  ? 142 VAL A CG2 1 
ATOM   4427 N  N   . GLY B 1 170 ? -25.972 -49.427 15.342  1.00 56.71  ? 143 GLY A N   1 
ATOM   4428 C  CA  . GLY B 1 170 ? -25.932 -49.176 16.792  1.00 51.76  ? 143 GLY A CA  1 
ATOM   4429 C  C   . GLY B 1 170 ? -26.619 -47.862 17.124  1.00 45.53  ? 143 GLY A C   1 
ATOM   4430 O  O   . GLY B 1 170 ? -27.422 -47.368 16.361  1.00 40.82  ? 143 GLY A O   1 
ATOM   4431 N  N   . ALA B 1 171 ? -26.345 -47.304 18.283  1.00 44.38  ? 144 ALA A N   1 
ATOM   4432 C  CA  . ALA B 1 171 ? -25.637 -47.978 19.355  1.00 47.52  ? 144 ALA A CA  1 
ATOM   4433 C  C   . ALA B 1 171 ? -26.590 -48.899 20.198  1.00 49.92  ? 144 ALA A C   1 
ATOM   4434 O  O   . ALA B 1 171 ? -27.679 -49.286 19.738  1.00 48.62  ? 144 ALA A O   1 
ATOM   4435 C  CB  . ALA B 1 171 ? -25.023 -46.902 20.219  1.00 46.48  ? 144 ALA A CB  1 
ATOM   4436 N  N   . THR B 1 172 ? -26.183 -49.229 21.428  1.00 49.25  ? 145 THR A N   1 
ATOM   4437 C  CA  . THR B 1 172 ? -27.020 -50.003 22.361  1.00 54.24  ? 145 THR A CA  1 
ATOM   4438 C  C   . THR B 1 172 ? -27.978 -49.143 23.212  1.00 53.06  ? 145 THR A C   1 
ATOM   4439 O  O   . THR B 1 172 ? -29.202 -49.201 23.041  1.00 51.97  ? 145 THR A O   1 
ATOM   4440 C  CB  . THR B 1 172 ? -26.138 -50.867 23.278  1.00 52.95  ? 145 THR A CB  1 
ATOM   4441 O  OG1 . THR B 1 172 ? -25.477 -51.835 22.461  1.00 60.94  ? 145 THR A OG1 1 
ATOM   4442 C  CG2 . THR B 1 172 ? -26.953 -51.603 24.303  1.00 52.58  ? 145 THR A CG2 1 
ATOM   4443 N  N   . GLY B 1 173 ? -27.412 -48.351 24.117  1.00 53.20  ? 146 GLY A N   1 
ATOM   4444 C  CA  . GLY B 1 173 ? -28.194 -47.527 25.032  1.00 47.76  ? 146 GLY A CA  1 
ATOM   4445 C  C   . GLY B 1 173 ? -28.864 -46.376 24.306  1.00 48.95  ? 146 GLY A C   1 
ATOM   4446 O  O   . GLY B 1 173 ? -28.212 -45.677 23.491  1.00 47.02  ? 146 GLY A O   1 
ATOM   4447 N  N   . SER B 1 174 ? -30.160 -46.190 24.582  1.00 41.80  ? 147 SER A N   1 
ATOM   4448 C  CA  . SER B 1 174 ? -30.920 -45.116 23.969  1.00 45.68  ? 147 SER A CA  1 
ATOM   4449 C  C   . SER B 1 174 ? -30.252 -43.724 24.095  1.00 42.17  ? 147 SER A C   1 
ATOM   4450 O  O   . SER B 1 174 ? -30.266 -42.953 23.154  1.00 41.94  ? 147 SER A O   1 
ATOM   4451 C  CB  . SER B 1 174 ? -32.342 -45.066 24.535  1.00 47.95  ? 147 SER A CB  1 
ATOM   4452 O  OG  . SER B 1 174 ? -33.162 -45.967 23.837  1.00 49.34  ? 147 SER A OG  1 
ATOM   4453 N  N   . GLY B 1 175 ? -29.665 -43.432 25.250  1.00 42.30  ? 148 GLY A N   1 
ATOM   4454 C  CA  . GLY B 1 175 ? -28.919 -42.196 25.493  1.00 41.27  ? 148 GLY A CA  1 
ATOM   4455 C  C   . GLY B 1 175 ? -27.727 -41.970 24.570  1.00 46.54  ? 148 GLY A C   1 
ATOM   4456 O  O   . GLY B 1 175 ? -27.391 -40.826 24.211  1.00 46.32  ? 148 GLY A O   1 
ATOM   4457 N  N   . VAL B 1 176 ? -27.072 -43.071 24.217  1.00 49.06  ? 149 VAL A N   1 
ATOM   4458 C  CA  . VAL B 1 176 ? -25.953 -43.045 23.321  1.00 46.67  ? 149 VAL A CA  1 
ATOM   4459 C  C   . VAL B 1 176 ? -26.476 -42.893 21.903  1.00 46.86  ? 149 VAL A C   1 
ATOM   4460 O  O   . VAL B 1 176 ? -26.006 -42.043 21.189  1.00 49.40  ? 149 VAL A O   1 
ATOM   4461 C  CB  . VAL B 1 176 ? -25.122 -44.328 23.457  1.00 47.29  ? 149 VAL A CB  1 
ATOM   4462 C  CG1 . VAL B 1 176 ? -24.044 -44.408 22.373  1.00 46.04  ? 149 VAL A CG1 1 
ATOM   4463 C  CG2 . VAL B 1 176 ? -24.516 -44.401 24.851  1.00 46.35  ? 149 VAL A CG2 1 
ATOM   4464 N  N   . SER B 1 177 ? -27.438 -43.710 21.493  1.00 47.66  ? 150 SER A N   1 
ATOM   4465 C  CA  . SER B 1 177 ? -27.979 -43.609 20.124  1.00 49.17  ? 150 SER A CA  1 
ATOM   4466 C  C   . SER B 1 177 ? -28.586 -42.232 19.858  1.00 46.18  ? 150 SER A C   1 
ATOM   4467 O  O   . SER B 1 177 ? -28.507 -41.719 18.749  1.00 51.30  ? 150 SER A O   1 
ATOM   4468 C  CB  . SER B 1 177 ? -29.040 -44.685 19.837  1.00 48.51  ? 150 SER A CB  1 
ATOM   4469 O  OG  . SER B 1 177 ? -28.493 -45.975 19.763  1.00 43.97  ? 150 SER A OG  1 
ATOM   4470 N  N   . THR B 1 178 ? -29.200 -41.645 20.863  1.00 41.64  ? 151 THR A N   1 
ATOM   4471 C  CA  . THR B 1 178 ? -29.638 -40.265 20.773  1.00 43.66  ? 151 THR A CA  1 
ATOM   4472 C  C   . THR B 1 178 ? -28.508 -39.317 20.382  1.00 41.68  ? 151 THR A C   1 
ATOM   4473 O  O   . THR B 1 178 ? -28.611 -38.584 19.453  1.00 40.09  ? 151 THR A O   1 
ATOM   4474 C  CB  . THR B 1 178 ? -30.161 -39.815 22.134  1.00 49.29  ? 151 THR A CB  1 
ATOM   4475 O  OG1 . THR B 1 178 ? -31.452 -40.397 22.340  1.00 49.61  ? 151 THR A OG1 1 
ATOM   4476 C  CG2 . THR B 1 178 ? -30.289 -38.298 22.186  1.00 61.33  ? 151 THR A CG2 1 
ATOM   4477 N  N   . ALA B 1 179 ? -27.420 -39.326 21.122  1.00 42.37  ? 152 ALA A N   1 
ATOM   4478 C  CA  . ALA B 1 179 ? -26.341 -38.419 20.854  1.00 43.74  ? 152 ALA A CA  1 
ATOM   4479 C  C   . ALA B 1 179 ? -25.815 -38.633 19.466  1.00 46.14  ? 152 ALA A C   1 
ATOM   4480 O  O   . ALA B 1 179 ? -25.611 -37.685 18.720  1.00 48.74  ? 152 ALA A O   1 
ATOM   4481 C  CB  . ALA B 1 179 ? -25.230 -38.628 21.850  1.00 45.44  ? 152 ALA A CB  1 
ATOM   4482 N  N   . VAL B 1 180 ? -25.599 -39.889 19.126  1.00 46.20  ? 153 VAL A N   1 
ATOM   4483 C  CA  . VAL B 1 180 ? -25.057 -40.237 17.831  1.00 50.69  ? 153 VAL A CA  1 
ATOM   4484 C  C   . VAL B 1 180 ? -26.002 -39.773 16.724  1.00 54.54  ? 153 VAL A C   1 
ATOM   4485 O  O   . VAL B 1 180 ? -25.576 -39.152 15.740  1.00 50.90  ? 153 VAL A O   1 
ATOM   4486 C  CB  . VAL B 1 180 ? -24.891 -41.752 17.724  1.00 50.43  ? 153 VAL A CB  1 
ATOM   4487 C  CG1 . VAL B 1 180 ? -24.722 -42.187 16.273  1.00 51.05  ? 153 VAL A CG1 1 
ATOM   4488 C  CG2 . VAL B 1 180 ? -23.721 -42.188 18.595  1.00 53.40  ? 153 VAL A CG2 1 
ATOM   4489 N  N   . ALA B 1 181 ? -27.283 -40.075 16.916  1.00 49.70  ? 154 ALA A N   1 
ATOM   4490 C  CA  . ALA B 1 181 ? -28.291 -39.827 15.919  1.00 47.43  ? 154 ALA A CA  1 
ATOM   4491 C  C   . ALA B 1 181 ? -28.381 -38.359 15.598  1.00 48.99  ? 154 ALA A C   1 
ATOM   4492 O  O   . ALA B 1 181 ? -28.694 -38.023 14.484  1.00 50.20  ? 154 ALA A O   1 
ATOM   4493 C  CB  . ALA B 1 181 ? -29.643 -40.337 16.400  1.00 46.01  ? 154 ALA A CB  1 
ATOM   4494 N  N   . ASN B 1 182 ? -28.145 -37.478 16.568  1.00 51.48  ? 155 ASN A N   1 
ATOM   4495 C  CA  . ASN B 1 182 ? -28.134 -36.049 16.272  1.00 53.82  ? 155 ASN A CA  1 
ATOM   4496 C  C   . ASN B 1 182 ? -27.061 -35.771 15.219  1.00 50.08  ? 155 ASN A C   1 
ATOM   4497 O  O   . ASN B 1 182 ? -27.271 -35.033 14.265  1.00 49.49  ? 155 ASN A O   1 
ATOM   4498 C  CB  . ASN B 1 182 ? -27.867 -35.201 17.531  1.00 55.84  ? 155 ASN A CB  1 
ATOM   4499 C  CG  . ASN B 1 182 ? -29.058 -35.140 18.475  1.00 53.46  ? 155 ASN A CG  1 
ATOM   4500 O  OD1 . ASN B 1 182 ? -30.209 -35.153 18.043  1.00 56.59  ? 155 ASN A OD1 1 
ATOM   4501 N  ND2 . ASN B 1 182 ? -28.778 -35.068 19.778  1.00 52.33  ? 155 ASN A ND2 1 
ATOM   4502 N  N   . LEU B 1 183 ? -25.917 -36.405 15.383  1.00 52.39  ? 156 LEU A N   1 
ATOM   4503 C  CA  . LEU B 1 183 ? -24.788 -36.182 14.479  1.00 53.16  ? 156 LEU A CA  1 
ATOM   4504 C  C   . LEU B 1 183 ? -24.951 -36.825 13.090  1.00 49.41  ? 156 LEU A C   1 
ATOM   4505 O  O   . LEU B 1 183 ? -24.743 -36.174 12.106  1.00 44.55  ? 156 LEU A O   1 
ATOM   4506 C  CB  . LEU B 1 183 ? -23.491 -36.679 15.122  1.00 52.71  ? 156 LEU A CB  1 
ATOM   4507 C  CG  . LEU B 1 183 ? -22.370 -35.648 15.130  1.00 55.65  ? 156 LEU A CG  1 
ATOM   4508 C  CD1 . LEU B 1 183 ? -21.096 -36.267 15.694  1.00 56.79  ? 156 LEU A CD1 1 
ATOM   4509 C  CD2 . LEU B 1 183 ? -22.118 -35.059 13.749  1.00 55.06  ? 156 LEU A CD2 1 
ATOM   4510 N  N   . LEU B 1 184 ? -25.326 -38.097 13.024  1.00 51.69  ? 157 LEU A N   1 
ATOM   4511 C  CA  . LEU B 1 184 ? -25.472 -38.781 11.752  1.00 52.27  ? 157 LEU A CA  1 
ATOM   4512 C  C   . LEU B 1 184 ? -26.560 -38.134 10.927  1.00 55.06  ? 157 LEU A C   1 
ATOM   4513 O  O   . LEU B 1 184 ? -26.430 -38.005 9.686   1.00 59.71  ? 157 LEU A O   1 
ATOM   4514 C  CB  . LEU B 1 184 ? -25.793 -40.248 11.960  1.00 52.37  ? 157 LEU A CB  1 
ATOM   4515 C  CG  . LEU B 1 184 ? -24.650 -41.045 12.578  1.00 53.88  ? 157 LEU A CG  1 
ATOM   4516 C  CD1 . LEU B 1 184 ? -25.087 -42.486 12.744  1.00 54.91  ? 157 LEU A CD1 1 
ATOM   4517 C  CD2 . LEU B 1 184 ? -23.393 -40.968 11.733  1.00 55.85  ? 157 LEU A CD2 1 
ATOM   4518 N  N   . GLY B 1 185 ? -27.619 -37.718 11.616  1.00 49.57  ? 158 GLY A N   1 
ATOM   4519 C  CA  . GLY B 1 185 ? -28.758 -37.014 10.992  1.00 50.63  ? 158 GLY A CA  1 
ATOM   4520 C  C   . GLY B 1 185 ? -28.412 -35.777 10.161  1.00 53.36  ? 158 GLY A C   1 
ATOM   4521 O  O   . GLY B 1 185 ? -29.052 -35.505 9.146   1.00 52.50  ? 158 GLY A O   1 
ATOM   4522 N  N   . LEU B 1 186 ? -27.415 -35.014 10.583  1.00 52.33  ? 159 LEU A N   1 
ATOM   4523 C  CA  . LEU B 1 186 ? -26.987 -33.863 9.788   1.00 60.47  ? 159 LEU A CA  1 
ATOM   4524 C  C   . LEU B 1 186 ? -26.624 -34.270 8.389   1.00 60.37  ? 159 LEU A C   1 
ATOM   4525 O  O   . LEU B 1 186 ? -26.957 -33.575 7.444   1.00 59.35  ? 159 LEU A O   1 
ATOM   4526 C  CB  . LEU B 1 186 ? -25.725 -33.233 10.370  1.00 62.60  ? 159 LEU A CB  1 
ATOM   4527 C  CG  . LEU B 1 186 ? -25.913 -32.416 11.617  1.00 62.75  ? 159 LEU A CG  1 
ATOM   4528 C  CD1 . LEU B 1 186 ? -24.546 -32.103 12.207  1.00 61.92  ? 159 LEU A CD1 1 
ATOM   4529 C  CD2 . LEU B 1 186 ? -26.692 -31.167 11.226  1.00 65.22  ? 159 LEU A CD2 1 
ATOM   4530 N  N   . PHE B 1 187 ? -25.908 -35.389 8.285   1.00 62.03  ? 160 PHE A N   1 
ATOM   4531 C  CA  . PHE B 1 187 ? -25.353 -35.863 7.026   1.00 59.25  ? 160 PHE A CA  1 
ATOM   4532 C  C   . PHE B 1 187 ? -26.213 -36.938 6.411   1.00 58.51  ? 160 PHE A C   1 
ATOM   4533 O  O   . PHE B 1 187 ? -25.782 -37.640 5.514   1.00 66.30  ? 160 PHE A O   1 
ATOM   4534 C  CB  . PHE B 1 187 ? -23.948 -36.364 7.298   1.00 57.95  ? 160 PHE A CB  1 
ATOM   4535 C  CG  . PHE B 1 187 ? -23.108 -35.354 8.016   1.00 65.95  ? 160 PHE A CG  1 
ATOM   4536 C  CD1 . PHE B 1 187 ? -22.926 -34.087 7.479   1.00 72.35  ? 160 PHE A CD1 1 
ATOM   4537 C  CD2 . PHE B 1 187 ? -22.541 -35.638 9.242   1.00 69.40  ? 160 PHE A CD2 1 
ATOM   4538 C  CE1 . PHE B 1 187 ? -22.180 -33.130 8.146   1.00 74.70  ? 160 PHE A CE1 1 
ATOM   4539 C  CE2 . PHE B 1 187 ? -21.782 -34.689 9.912   1.00 72.95  ? 160 PHE A CE2 1 
ATOM   4540 C  CZ  . PHE B 1 187 ? -21.601 -33.430 9.366   1.00 71.51  ? 160 PHE A CZ  1 
ATOM   4541 N  N   . TYR B 1 188 ? -27.429 -37.078 6.924   1.00 56.62  ? 161 TYR A N   1 
ATOM   4542 C  CA  . TYR B 1 188 ? -28.372 -38.075 6.461   1.00 55.34  ? 161 TYR A CA  1 
ATOM   4543 C  C   . TYR B 1 188 ? -27.756 -39.456 6.296   1.00 53.96  ? 161 TYR A C   1 
ATOM   4544 O  O   . TYR B 1 188 ? -28.141 -40.225 5.410   1.00 44.38  ? 161 TYR A O   1 
ATOM   4545 C  CB  . TYR B 1 188 ? -29.007 -37.622 5.162   1.00 52.25  ? 161 TYR A CB  1 
ATOM   4546 C  CG  . TYR B 1 188 ? -29.917 -36.456 5.344   1.00 55.03  ? 161 TYR A CG  1 
ATOM   4547 C  CD1 . TYR B 1 188 ? -29.425 -35.140 5.282   1.00 59.62  ? 161 TYR A CD1 1 
ATOM   4548 C  CD2 . TYR B 1 188 ? -31.266 -36.648 5.590   1.00 51.06  ? 161 TYR A CD2 1 
ATOM   4549 C  CE1 . TYR B 1 188 ? -30.275 -34.054 5.444   1.00 58.10  ? 161 TYR A CE1 1 
ATOM   4550 C  CE2 . TYR B 1 188 ? -32.120 -35.574 5.761   1.00 53.92  ? 161 TYR A CE2 1 
ATOM   4551 C  CZ  . TYR B 1 188 ? -31.630 -34.284 5.672   1.00 58.34  ? 161 TYR A CZ  1 
ATOM   4552 O  OH  . TYR B 1 188 ? -32.501 -33.226 5.803   1.00 63.23  ? 161 TYR A OH  1 
ATOM   4553 N  N   . ILE B 1 189 ? -26.837 -39.783 7.193   1.00 55.90  ? 162 ILE A N   1 
ATOM   4554 C  CA  . ILE B 1 189 ? -26.294 -41.122 7.234   1.00 56.73  ? 162 ILE A CA  1 
ATOM   4555 C  C   . ILE B 1 189 ? -27.259 -42.006 8.027   1.00 57.69  ? 162 ILE A C   1 
ATOM   4556 O  O   . ILE B 1 189 ? -27.531 -41.733 9.182   1.00 52.23  ? 162 ILE A O   1 
ATOM   4557 C  CB  . ILE B 1 189 ? -24.919 -41.114 7.878   1.00 56.92  ? 162 ILE A CB  1 
ATOM   4558 C  CG1 . ILE B 1 189 ? -24.032 -40.135 7.108   1.00 57.59  ? 162 ILE A CG1 1 
ATOM   4559 C  CG2 . ILE B 1 189 ? -24.346 -42.518 7.882   1.00 56.99  ? 162 ILE A CG2 1 
ATOM   4560 C  CD1 . ILE B 1 189 ? -22.598 -40.107 7.565   1.00 57.44  ? 162 ILE A CD1 1 
ATOM   4561 N  N   . PRO B 1 190 ? -27.802 -43.056 7.394   1.00 63.84  ? 163 PRO A N   1 
ATOM   4562 C  CA  . PRO B 1 190 ? -28.724 -43.934 8.123   1.00 60.21  ? 163 PRO A CA  1 
ATOM   4563 C  C   . PRO B 1 190 ? -28.023 -44.628 9.275   1.00 57.39  ? 163 PRO A C   1 
ATOM   4564 O  O   . PRO B 1 190 ? -26.845 -44.993 9.155   1.00 50.01  ? 163 PRO A O   1 
ATOM   4565 C  CB  . PRO B 1 190 ? -29.162 -44.963 7.072   1.00 58.73  ? 163 PRO A CB  1 
ATOM   4566 C  CG  . PRO B 1 190 ? -28.080 -44.941 6.058   1.00 62.91  ? 163 PRO A CG  1 
ATOM   4567 C  CD  . PRO B 1 190 ? -27.534 -43.549 6.031   1.00 64.19  ? 163 PRO A CD  1 
ATOM   4568 N  N   . GLN B 1 191 ? -28.746 -44.772 10.385  1.00 53.45  ? 164 GLN A N   1 
ATOM   4569 C  CA  . GLN B 1 191 ? -28.267 -45.472 11.547  1.00 47.29  ? 164 GLN A CA  1 
ATOM   4570 C  C   . GLN B 1 191 ? -29.325 -46.484 11.867  1.00 48.77  ? 164 GLN A C   1 
ATOM   4571 O  O   . GLN B 1 191 ? -30.493 -46.138 11.889  1.00 53.13  ? 164 GLN A O   1 
ATOM   4572 C  CB  . GLN B 1 191 ? -28.139 -44.493 12.685  1.00 49.83  ? 164 GLN A CB  1 
ATOM   4573 C  CG  . GLN B 1 191 ? -27.797 -45.101 14.047  1.00 51.12  ? 164 GLN A CG  1 
ATOM   4574 C  CD  . GLN B 1 191 ? -27.772 -44.050 15.138  1.00 51.75  ? 164 GLN A CD  1 
ATOM   4575 O  OE1 . GLN B 1 191 ? -27.852 -42.834 14.864  1.00 52.96  ? 164 GLN A OE1 1 
ATOM   4576 N  NE2 . GLN B 1 191 ? -27.683 -44.502 16.381  1.00 54.07  ? 164 GLN A NE2 1 
ATOM   4577 N  N   . VAL B 1 192 ? -28.932 -47.728 12.102  1.00 50.77  ? 165 VAL A N   1 
ATOM   4578 C  CA  . VAL B 1 192 ? -29.883 -48.781 12.460  1.00 52.53  ? 165 VAL A CA  1 
ATOM   4579 C  C   . VAL B 1 192 ? -29.522 -49.377 13.808  1.00 53.88  ? 165 VAL A C   1 
ATOM   4580 O  O   . VAL B 1 192 ? -28.505 -50.042 13.924  1.00 49.05  ? 165 VAL A O   1 
ATOM   4581 C  CB  . VAL B 1 192 ? -29.895 -49.909 11.421  1.00 54.04  ? 165 VAL A CB  1 
ATOM   4582 C  CG1 . VAL B 1 192 ? -30.838 -51.017 11.841  1.00 56.88  ? 165 VAL A CG1 1 
ATOM   4583 C  CG2 . VAL B 1 192 ? -30.298 -49.356 10.064  1.00 57.82  ? 165 VAL A CG2 1 
ATOM   4584 N  N   . SER B 1 193 ? -30.349 -49.161 14.831  1.00 55.76  ? 166 SER A N   1 
ATOM   4585 C  CA  . SER B 1 193 ? -30.025 -49.727 16.124  1.00 56.45  ? 166 SER A CA  1 
ATOM   4586 C  C   . SER B 1 193 ? -30.626 -51.094 16.358  1.00 54.76  ? 166 SER A C   1 
ATOM   4587 O  O   . SER B 1 193 ? -31.815 -51.325 16.150  1.00 56.39  ? 166 SER A O   1 
ATOM   4588 C  CB  . SER B 1 193 ? -30.435 -48.823 17.268  1.00 58.11  ? 166 SER A CB  1 
ATOM   4589 O  OG  . SER B 1 193 ? -29.911 -49.351 18.486  1.00 53.44  ? 166 SER A OG  1 
ATOM   4590 N  N   . TYR B 1 194 ? -29.765 -51.984 16.831  1.00 52.48  ? 167 TYR A N   1 
ATOM   4591 C  CA  . TYR B 1 194 ? -30.140 -53.319 17.273  1.00 50.96  ? 167 TYR A CA  1 
ATOM   4592 C  C   . TYR B 1 194 ? -30.763 -53.356 18.690  1.00 53.63  ? 167 TYR A C   1 
ATOM   4593 O  O   . TYR B 1 194 ? -31.342 -54.360 19.051  1.00 64.88  ? 167 TYR A O   1 
ATOM   4594 C  CB  . TYR B 1 194 ? -28.892 -54.209 17.231  1.00 48.58  ? 167 TYR A CB  1 
ATOM   4595 C  CG  . TYR B 1 194 ? -27.667 -53.621 17.914  1.00 44.70  ? 167 TYR A CG  1 
ATOM   4596 C  CD1 . TYR B 1 194 ? -27.444 -53.798 19.271  1.00 43.79  ? 167 TYR A CD1 1 
ATOM   4597 C  CD2 . TYR B 1 194 ? -26.719 -52.904 17.193  1.00 45.17  ? 167 TYR A CD2 1 
ATOM   4598 C  CE1 . TYR B 1 194 ? -26.318 -53.256 19.902  1.00 44.25  ? 167 TYR A CE1 1 
ATOM   4599 C  CE2 . TYR B 1 194 ? -25.596 -52.361 17.815  1.00 42.48  ? 167 TYR A CE2 1 
ATOM   4600 C  CZ  . TYR B 1 194 ? -25.397 -52.546 19.170  1.00 43.41  ? 167 TYR A CZ  1 
ATOM   4601 O  OH  . TYR B 1 194 ? -24.288 -52.030 19.811  1.00 45.66  ? 167 TYR A OH  1 
ATOM   4602 N  N   . ALA B 1 195 ? -30.649 -52.287 19.487  1.00 52.04  ? 168 ALA A N   1 
ATOM   4603 C  CA  . ALA B 1 195 ? -31.077 -52.325 20.901  1.00 51.34  ? 168 ALA A CA  1 
ATOM   4604 C  C   . ALA B 1 195 ? -31.610 -51.024 21.565  1.00 49.52  ? 168 ALA A C   1 
ATOM   4605 O  O   . ALA B 1 195 ? -32.045 -51.057 22.710  1.00 47.14  ? 168 ALA A O   1 
ATOM   4606 C  CB  . ALA B 1 195 ? -29.938 -52.883 21.751  1.00 52.24  ? 168 ALA A CB  1 
ATOM   4607 N  N   . SER B 1 196 ? -31.562 -49.880 20.904  1.00 46.03  ? 169 SER A N   1 
ATOM   4608 C  CA  . SER B 1 196 ? -32.166 -48.689 21.495  1.00 43.26  ? 169 SER A CA  1 
ATOM   4609 C  C   . SER B 1 196 ? -33.706 -48.589 21.291  1.00 41.21  ? 169 SER A C   1 
ATOM   4610 O  O   . SER B 1 196 ? -34.182 -48.443 20.184  1.00 38.41  ? 169 SER A O   1 
ATOM   4611 C  CB  . SER B 1 196 ? -31.454 -47.455 20.984  1.00 42.09  ? 169 SER A CB  1 
ATOM   4612 O  OG  . SER B 1 196 ? -30.133 -47.494 21.474  1.00 45.06  ? 169 SER A OG  1 
ATOM   4613 N  N   . SER B 1 197 ? -34.480 -48.626 22.371  1.00 39.92  ? 170 SER A N   1 
ATOM   4614 C  CA  . SER B 1 197 ? -35.941 -48.816 22.267  1.00 40.23  ? 170 SER A CA  1 
ATOM   4615 C  C   . SER B 1 197 ? -36.752 -47.636 22.849  1.00 44.19  ? 170 SER A C   1 
ATOM   4616 O  O   . SER B 1 197 ? -37.972 -47.746 23.071  1.00 41.90  ? 170 SER A O   1 
ATOM   4617 C  CB  . SER B 1 197 ? -36.323 -50.103 22.980  1.00 39.01  ? 170 SER A CB  1 
ATOM   4618 O  OG  . SER B 1 197 ? -35.765 -50.130 24.312  1.00 39.42  ? 170 SER A OG  1 
ATOM   4619 N  N   . SER B 1 198 ? -36.084 -46.502 23.057  1.00 41.74  ? 171 SER A N   1 
ATOM   4620 C  CA  . SER B 1 198 ? -36.752 -45.315 23.533  1.00 41.29  ? 171 SER A CA  1 
ATOM   4621 C  C   . SER B 1 198 ? -37.775 -44.786 22.519  1.00 40.25  ? 171 SER A C   1 
ATOM   4622 O  O   . SER B 1 198 ? -37.523 -44.739 21.332  1.00 41.19  ? 171 SER A O   1 
ATOM   4623 C  CB  . SER B 1 198 ? -35.739 -44.226 23.904  1.00 40.27  ? 171 SER A CB  1 
ATOM   4624 O  OG  . SER B 1 198 ? -36.427 -43.078 24.393  1.00 41.43  ? 171 SER A OG  1 
ATOM   4625 N  N   . ARG B 1 199 ? -38.953 -44.400 22.993  1.00 41.49  ? 172 ARG A N   1 
ATOM   4626 C  CA  . ARG B 1 199 ? -39.915 -43.781 22.094  1.00 39.68  ? 172 ARG A CA  1 
ATOM   4627 C  C   . ARG B 1 199 ? -39.412 -42.429 21.579  1.00 40.05  ? 172 ARG A C   1 
ATOM   4628 O  O   . ARG B 1 199 ? -39.931 -41.929 20.577  1.00 42.18  ? 172 ARG A O   1 
ATOM   4629 C  CB  . ARG B 1 199 ? -41.239 -43.550 22.806  1.00 40.81  ? 172 ARG A CB  1 
ATOM   4630 C  CG  . ARG B 1 199 ? -41.156 -42.405 23.776  1.00 43.55  ? 172 ARG A CG  1 
ATOM   4631 C  CD  . ARG B 1 199 ? -42.462 -41.762 24.041  1.00 49.39  ? 172 ARG A CD  1 
ATOM   4632 N  NE  . ARG B 1 199 ? -42.294 -40.639 24.963  1.00 56.51  ? 172 ARG A NE  1 
ATOM   4633 C  CZ  . ARG B 1 199 ? -42.147 -39.363 24.612  1.00 48.86  ? 172 ARG A CZ  1 
ATOM   4634 N  NH1 . ARG B 1 199 ? -42.105 -39.009 23.342  1.00 46.66  ? 172 ARG A NH1 1 
ATOM   4635 N  NH2 . ARG B 1 199 ? -42.045 -38.446 25.559  1.00 48.66  ? 172 ARG A NH2 1 
ATOM   4636 N  N   . LEU B 1 200 ? -38.457 -41.808 22.289  1.00 37.10  ? 173 LEU A N   1 
ATOM   4637 C  CA  . LEU B 1 200 ? -37.922 -40.529 21.872  1.00 38.20  ? 173 LEU A CA  1 
ATOM   4638 C  C   . LEU B 1 200 ? -37.356 -40.687 20.477  1.00 40.17  ? 173 LEU A C   1 
ATOM   4639 O  O   . LEU B 1 200 ? -37.526 -39.795 19.654  1.00 42.05  ? 173 LEU A O   1 
ATOM   4640 C  CB  . LEU B 1 200 ? -36.876 -39.971 22.840  1.00 38.89  ? 173 LEU A CB  1 
ATOM   4641 C  CG  . LEU B 1 200 ? -37.477 -39.714 24.228  1.00 45.89  ? 173 LEU A CG  1 
ATOM   4642 C  CD1 . LEU B 1 200 ? -36.401 -39.498 25.258  1.00 48.24  ? 173 LEU A CD1 1 
ATOM   4643 C  CD2 . LEU B 1 200 ? -38.477 -38.550 24.277  1.00 47.85  ? 173 LEU A CD2 1 
ATOM   4644 N  N   . LEU B 1 201 ? -36.783 -41.858 20.193  1.00 42.96  ? 174 LEU A N   1 
ATOM   4645 C  CA  . LEU B 1 201 ? -36.203 -42.132 18.891  1.00 46.25  ? 174 LEU A CA  1 
ATOM   4646 C  C   . LEU B 1 201 ? -37.180 -42.293 17.715  1.00 46.12  ? 174 LEU A C   1 
ATOM   4647 O  O   . LEU B 1 201 ? -36.753 -42.242 16.559  1.00 53.86  ? 174 LEU A O   1 
ATOM   4648 C  CB  . LEU B 1 201 ? -35.276 -43.340 18.978  1.00 47.26  ? 174 LEU A CB  1 
ATOM   4649 C  CG  . LEU B 1 201 ? -33.963 -43.053 19.708  1.00 48.87  ? 174 LEU A CG  1 
ATOM   4650 C  CD1 . LEU B 1 201 ? -33.320 -44.336 20.217  1.00 50.54  ? 174 LEU A CD1 1 
ATOM   4651 C  CD2 . LEU B 1 201 ? -32.982 -42.290 18.838  1.00 45.08  ? 174 LEU A CD2 1 
ATOM   4652 N  N   . SER B 1 202 ? -38.460 -42.490 17.979  1.00 45.48  ? 175 SER A N   1 
ATOM   4653 C  CA  . SER B 1 202 ? -39.488 -42.511 16.904  1.00 46.69  ? 175 SER A CA  1 
ATOM   4654 C  C   . SER B 1 202 ? -39.747 -41.135 16.286  1.00 48.24  ? 175 SER A C   1 
ATOM   4655 O  O   . SER B 1 202 ? -40.461 -41.032 15.286  1.00 48.13  ? 175 SER A O   1 
ATOM   4656 C  CB  . SER B 1 202 ? -40.849 -42.989 17.446  1.00 48.64  ? 175 SER A CB  1 
ATOM   4657 O  OG  . SER B 1 202 ? -40.795 -44.298 18.006  1.00 51.41  ? 175 SER A OG  1 
ATOM   4658 N  N   . ASN B 1 203 ? -39.220 -40.078 16.898  1.00 45.67  ? 176 ASN A N   1 
ATOM   4659 C  CA  . ASN B 1 203 ? -39.491 -38.752 16.448  1.00 44.16  ? 176 ASN A CA  1 
ATOM   4660 C  C   . ASN B 1 203 ? -38.586 -38.395 15.252  1.00 49.51  ? 176 ASN A C   1 
ATOM   4661 O  O   . ASN B 1 203 ? -37.405 -38.054 15.410  1.00 48.82  ? 176 ASN A O   1 
ATOM   4662 C  CB  . ASN B 1 203 ? -39.285 -37.798 17.597  1.00 46.44  ? 176 ASN A CB  1 
ATOM   4663 C  CG  . ASN B 1 203 ? -39.481 -36.353 17.193  1.00 54.03  ? 176 ASN A CG  1 
ATOM   4664 O  OD1 . ASN B 1 203 ? -39.296 -35.442 18.004  1.00 47.20  ? 176 ASN A OD1 1 
ATOM   4665 N  ND2 . ASN B 1 203 ? -39.822 -36.123 15.920  1.00 56.73  ? 176 ASN A ND2 1 
ATOM   4666 N  N   . LYS B 1 204 ? -39.158 -38.462 14.053  1.00 50.67  ? 177 LYS A N   1 
ATOM   4667 C  CA  . LYS B 1 204 ? -38.379 -38.303 12.839  1.00 47.61  ? 177 LYS A CA  1 
ATOM   4668 C  C   . LYS B 1 204 ? -38.070 -36.865 12.461  1.00 53.92  ? 177 LYS A C   1 
ATOM   4669 O  O   . LYS B 1 204 ? -37.158 -36.655 11.660  1.00 57.09  ? 177 LYS A O   1 
ATOM   4670 C  CB  . LYS B 1 204 ? -39.045 -38.963 11.661  1.00 45.16  ? 177 LYS A CB  1 
ATOM   4671 C  CG  . LYS B 1 204 ? -39.229 -40.461 11.720  1.00 44.92  ? 177 LYS A CG  1 
ATOM   4672 C  CD  . LYS B 1 204 ? -37.961 -41.252 11.926  1.00 46.17  ? 177 LYS A CD  1 
ATOM   4673 C  CE  . LYS B 1 204 ? -37.713 -41.525 13.398  1.00 48.98  ? 177 LYS A CE  1 
ATOM   4674 N  NZ  . LYS B 1 204 ? -36.730 -42.621 13.579  1.00 53.73  ? 177 LYS A NZ  1 
ATOM   4675 N  N   . ASN B 1 205 ? -38.777 -35.878 13.009  1.00 54.02  ? 178 ASN A N   1 
ATOM   4676 C  CA  . ASN B 1 205 ? -38.275 -34.487 12.924  1.00 57.46  ? 178 ASN A CA  1 
ATOM   4677 C  C   . ASN B 1 205 ? -36.903 -34.326 13.576  1.00 54.70  ? 178 ASN A C   1 
ATOM   4678 O  O   . ASN B 1 205 ? -36.007 -33.742 12.985  1.00 50.97  ? 178 ASN A O   1 
ATOM   4679 C  CB  . ASN B 1 205 ? -39.242 -33.480 13.555  1.00 64.35  ? 178 ASN A CB  1 
ATOM   4680 C  CG  . ASN B 1 205 ? -40.631 -33.561 12.950  1.00 68.90  ? 178 ASN A CG  1 
ATOM   4681 O  OD1 . ASN B 1 205 ? -40.810 -33.251 11.773  1.00 70.35  ? 178 ASN A OD1 1 
ATOM   4682 N  ND2 . ASN B 1 205 ? -41.622 -34.007 13.743  1.00 70.60  ? 178 ASN A ND2 1 
ATOM   4683 N  N   . GLN B 1 206 ? -36.718 -34.862 14.780  1.00 52.22  ? 179 GLN A N   1 
ATOM   4684 C  CA  . GLN B 1 206 ? -35.412 -34.757 15.408  1.00 52.55  ? 179 GLN A CA  1 
ATOM   4685 C  C   . GLN B 1 206 ? -34.462 -35.797 14.888  1.00 53.32  ? 179 GLN A C   1 
ATOM   4686 O  O   . GLN B 1 206 ? -33.304 -35.484 14.695  1.00 56.57  ? 179 GLN A O   1 
ATOM   4687 C  CB  . GLN B 1 206 ? -35.456 -34.859 16.933  1.00 60.49  ? 179 GLN A CB  1 
ATOM   4688 C  CG  . GLN B 1 206 ? -34.038 -34.840 17.520  1.00 71.64  ? 179 GLN A CG  1 
ATOM   4689 C  CD  . GLN B 1 206 ? -33.805 -33.954 18.752  1.00 81.91  ? 179 GLN A CD  1 
ATOM   4690 O  OE1 . GLN B 1 206 ? -32.785 -34.102 19.459  1.00 76.26  ? 179 GLN A OE1 1 
ATOM   4691 N  NE2 . GLN B 1 206 ? -34.714 -33.016 18.998  1.00 91.15  ? 179 GLN A NE2 1 
ATOM   4692 N  N   . PHE B 1 207 ? -34.912 -37.041 14.689  1.00 55.31  ? 180 PHE A N   1 
ATOM   4693 C  CA  . PHE B 1 207 ? -33.985 -38.099 14.261  1.00 50.54  ? 180 PHE A CA  1 
ATOM   4694 C  C   . PHE B 1 207 ? -34.341 -38.597 12.886  1.00 56.38  ? 180 PHE A C   1 
ATOM   4695 O  O   . PHE B 1 207 ? -35.010 -39.627 12.710  1.00 54.02  ? 180 PHE A O   1 
ATOM   4696 C  CB  . PHE B 1 207 ? -33.908 -39.233 15.246  1.00 45.80  ? 180 PHE A CB  1 
ATOM   4697 C  CG  . PHE B 1 207 ? -33.775 -38.785 16.640  1.00 44.79  ? 180 PHE A CG  1 
ATOM   4698 C  CD1 . PHE B 1 207 ? -32.567 -38.267 17.082  1.00 41.57  ? 180 PHE A CD1 1 
ATOM   4699 C  CD2 . PHE B 1 207 ? -34.881 -38.859 17.535  1.00 42.60  ? 180 PHE A CD2 1 
ATOM   4700 C  CE1 . PHE B 1 207 ? -32.433 -37.839 18.402  1.00 41.39  ? 180 PHE A CE1 1 
ATOM   4701 C  CE2 . PHE B 1 207 ? -34.751 -38.428 18.855  1.00 40.83  ? 180 PHE A CE2 1 
ATOM   4702 C  CZ  . PHE B 1 207 ? -33.530 -37.918 19.288  1.00 42.43  ? 180 PHE A CZ  1 
ATOM   4703 N  N   . LYS B 1 208 ? -33.818 -37.852 11.917  1.00 58.52  ? 181 LYS A N   1 
ATOM   4704 C  CA  . LYS B 1 208 ? -34.151 -38.014 10.523  1.00 52.78  ? 181 LYS A CA  1 
ATOM   4705 C  C   . LYS B 1 208 ? -33.632 -39.314 9.980   1.00 48.92  ? 181 LYS A C   1 
ATOM   4706 O  O   . LYS B 1 208 ? -34.223 -39.847 9.052   1.00 48.93  ? 181 LYS A O   1 
ATOM   4707 C  CB  . LYS B 1 208 ? -33.564 -36.862 9.715   1.00 55.04  ? 181 LYS A CB  1 
ATOM   4708 C  CG  . LYS B 1 208 ? -34.212 -35.532 10.035  1.00 63.40  ? 181 LYS A CG  1 
ATOM   4709 C  CD  . LYS B 1 208 ? -33.506 -34.407 9.324   1.00 74.53  ? 181 LYS A CD  1 
ATOM   4710 C  CE  . LYS B 1 208 ? -34.394 -33.176 9.267   1.00 80.67  ? 181 LYS A CE  1 
ATOM   4711 N  NZ  . LYS B 1 208 ? -33.655 -32.074 8.574   1.00 87.33  ? 181 LYS A NZ  1 
ATOM   4712 N  N   . SER B 1 209 ? -32.538 -39.836 10.524  1.00 41.18  ? 182 SER A N   1 
ATOM   4713 C  CA  . SER B 1 209 ? -31.879 -40.920 9.835   1.00 40.42  ? 182 SER A CA  1 
ATOM   4714 C  C   . SER B 1 209 ? -31.797 -42.174 10.666  1.00 42.17  ? 182 SER A C   1 
ATOM   4715 O  O   . SER B 1 209 ? -30.953 -43.047 10.378  1.00 41.69  ? 182 SER A O   1 
ATOM   4716 C  CB  . SER B 1 209 ? -30.490 -40.470 9.340   1.00 45.30  ? 182 SER A CB  1 
ATOM   4717 O  OG  . SER B 1 209 ? -29.448 -40.716 10.289  1.00 45.77  ? 182 SER A OG  1 
ATOM   4718 N  N   . PHE B 1 210 ? -32.700 -42.298 11.654  1.00 43.67  ? 183 PHE A N   1 
ATOM   4719 C  CA  . PHE B 1 210 ? -32.628 -43.378 12.642  1.00 42.58  ? 183 PHE A CA  1 
ATOM   4720 C  C   . PHE B 1 210 ? -33.696 -44.398 12.365  1.00 47.46  ? 183 PHE A C   1 
ATOM   4721 O  O   . PHE B 1 210 ? -34.850 -44.026 12.158  1.00 49.22  ? 183 PHE A O   1 
ATOM   4722 C  CB  . PHE B 1 210 ? -32.824 -42.853 14.069  1.00 41.11  ? 183 PHE A CB  1 
ATOM   4723 C  CG  . PHE B 1 210 ? -32.782 -43.932 15.131  1.00 39.84  ? 183 PHE A CG  1 
ATOM   4724 C  CD1 . PHE B 1 210 ? -33.939 -44.436 15.687  1.00 44.04  ? 183 PHE A CD1 1 
ATOM   4725 C  CD2 . PHE B 1 210 ? -31.579 -44.429 15.585  1.00 40.34  ? 183 PHE A CD2 1 
ATOM   4726 C  CE1 . PHE B 1 210 ? -33.889 -45.442 16.681  1.00 44.88  ? 183 PHE A CE1 1 
ATOM   4727 C  CE2 . PHE B 1 210 ? -31.524 -45.407 16.575  1.00 43.97  ? 183 PHE A CE2 1 
ATOM   4728 C  CZ  . PHE B 1 210 ? -32.687 -45.932 17.118  1.00 41.02  ? 183 PHE A CZ  1 
ATOM   4729 N  N   . LEU B 1 211 ? -33.301 -45.673 12.366  1.00 51.12  ? 184 LEU A N   1 
ATOM   4730 C  CA  . LEU B 1 211 ? -34.231 -46.801 12.378  1.00 52.19  ? 184 LEU A CA  1 
ATOM   4731 C  C   . LEU B 1 211 ? -33.698 -47.868 13.318  1.00 50.26  ? 184 LEU A C   1 
ATOM   4732 O  O   . LEU B 1 211 ? -32.553 -47.787 13.754  1.00 45.27  ? 184 LEU A O   1 
ATOM   4733 C  CB  . LEU B 1 211 ? -34.409 -47.411 11.000  1.00 56.19  ? 184 LEU A CB  1 
ATOM   4734 C  CG  . LEU B 1 211 ? -34.461 -46.407 9.858   1.00 66.84  ? 184 LEU A CG  1 
ATOM   4735 C  CD1 . LEU B 1 211 ? -33.070 -46.225 9.271   1.00 68.48  ? 184 LEU A CD1 1 
ATOM   4736 C  CD2 . LEU B 1 211 ? -35.463 -46.834 8.796   1.00 71.21  ? 184 LEU A CD2 1 
ATOM   4737 N  N   . ARG B 1 212 ? -34.532 -48.863 13.632  1.00 45.83  ? 185 ARG A N   1 
ATOM   4738 C  CA  . ARG B 1 212 ? -34.136 -49.876 14.572  1.00 43.67  ? 185 ARG A CA  1 
ATOM   4739 C  C   . ARG B 1 212 ? -34.803 -51.174 14.298  1.00 44.92  ? 185 ARG A C   1 
ATOM   4740 O  O   . ARG B 1 212 ? -35.898 -51.203 13.740  1.00 46.28  ? 185 ARG A O   1 
ATOM   4741 C  CB  . ARG B 1 212 ? -34.456 -49.432 15.972  1.00 42.93  ? 185 ARG A CB  1 
ATOM   4742 C  CG  . ARG B 1 212 ? -35.839 -48.870 16.133  1.00 42.84  ? 185 ARG A CG  1 
ATOM   4743 C  CD  . ARG B 1 212 ? -36.058 -48.524 17.591  1.00 44.31  ? 185 ARG A CD  1 
ATOM   4744 N  NE  . ARG B 1 212 ? -37.072 -47.485 17.767  1.00 42.63  ? 185 ARG A NE  1 
ATOM   4745 C  CZ  . ARG B 1 212 ? -37.115 -46.655 18.801  1.00 43.47  ? 185 ARG A CZ  1 
ATOM   4746 N  NH1 . ARG B 1 212 ? -36.189 -46.697 19.787  1.00 42.16  ? 185 ARG A NH1 1 
ATOM   4747 N  NH2 . ARG B 1 212 ? -38.089 -45.759 18.843  1.00 45.75  ? 185 ARG A NH2 1 
ATOM   4748 N  N   . THR B 1 213 ? -34.119 -52.248 14.685  1.00 48.04  ? 186 THR A N   1 
ATOM   4749 C  CA  . THR B 1 213 ? -34.593 -53.618 14.496  1.00 52.69  ? 186 THR A CA  1 
ATOM   4750 C  C   . THR B 1 213 ? -34.978 -54.129 15.867  1.00 56.71  ? 186 THR A C   1 
ATOM   4751 O  O   . THR B 1 213 ? -34.863 -55.323 16.161  1.00 59.13  ? 186 THR A O   1 
ATOM   4752 C  CB  . THR B 1 213 ? -33.484 -54.526 13.965  1.00 54.87  ? 186 THR A CB  1 
ATOM   4753 O  OG1 . THR B 1 213 ? -32.372 -54.483 14.868  1.00 59.25  ? 186 THR A OG1 1 
ATOM   4754 C  CG2 . THR B 1 213 ? -33.010 -54.062 12.621  1.00 60.16  ? 186 THR A CG2 1 
ATOM   4755 N  N   . ILE B 1 214 ? -35.393 -53.206 16.724  1.00 54.99  ? 187 ILE A N   1 
ATOM   4756 C  CA  . ILE B 1 214 ? -35.955 -53.560 17.996  1.00 55.50  ? 187 ILE A CA  1 
ATOM   4757 C  C   . ILE B 1 214 ? -37.220 -52.758 18.104  1.00 52.71  ? 187 ILE A C   1 
ATOM   4758 O  O   . ILE B 1 214 ? -37.265 -51.644 17.572  1.00 53.64  ? 187 ILE A O   1 
ATOM   4759 C  CB  . ILE B 1 214 ? -34.993 -53.290 19.167  1.00 56.61  ? 187 ILE A CB  1 
ATOM   4760 C  CG1 . ILE B 1 214 ? -35.576 -53.887 20.453  1.00 54.28  ? 187 ILE A CG1 1 
ATOM   4761 C  CG2 . ILE B 1 214 ? -34.670 -51.807 19.306  1.00 57.47  ? 187 ILE A CG2 1 
ATOM   4762 C  CD1 . ILE B 1 214 ? -34.556 -54.062 21.554  1.00 56.01  ? 187 ILE A CD1 1 
ATOM   4763 N  N   . PRO B 1 215 ? -38.275 -53.347 18.713  1.00 51.11  ? 188 PRO A N   1 
ATOM   4764 C  CA  . PRO B 1 215 ? -39.502 -52.578 18.977  1.00 52.48  ? 188 PRO A CA  1 
ATOM   4765 C  C   . PRO B 1 215 ? -39.287 -51.503 20.026  1.00 48.60  ? 188 PRO A C   1 
ATOM   4766 O  O   . PRO B 1 215 ? -38.479 -51.680 20.942  1.00 54.40  ? 188 PRO A O   1 
ATOM   4767 C  CB  . PRO B 1 215 ? -40.488 -53.627 19.512  1.00 53.53  ? 188 PRO A CB  1 
ATOM   4768 C  CG  . PRO B 1 215 ? -39.876 -54.959 19.217  1.00 51.58  ? 188 PRO A CG  1 
ATOM   4769 C  CD  . PRO B 1 215 ? -38.398 -54.739 19.179  1.00 49.97  ? 188 PRO A CD  1 
ATOM   4770 N  N   . ASN B 1 216 ? -40.006 -50.397 19.907  1.00 51.87  ? 189 ASN A N   1 
ATOM   4771 C  CA  . ASN B 1 216 ? -39.917 -49.369 20.934  1.00 51.48  ? 189 ASN A CA  1 
ATOM   4772 C  C   . ASN B 1 216 ? -40.739 -49.773 22.132  1.00 46.45  ? 189 ASN A C   1 
ATOM   4773 O  O   . ASN B 1 216 ? -41.538 -50.684 22.055  1.00 51.26  ? 189 ASN A O   1 
ATOM   4774 C  CB  . ASN B 1 216 ? -40.264 -47.992 20.390  1.00 52.19  ? 189 ASN A CB  1 
ATOM   4775 C  CG  . ASN B 1 216 ? -41.719 -47.695 20.439  1.00 54.58  ? 189 ASN A CG  1 
ATOM   4776 O  OD1 . ASN B 1 216 ? -42.406 -48.140 21.337  1.00 63.69  ? 189 ASN A OD1 1 
ATOM   4777 N  ND2 . ASN B 1 216 ? -42.194 -46.886 19.505  1.00 58.66  ? 189 ASN A ND2 1 
ATOM   4778 N  N   . ASP B 1 217 ? -40.512 -49.113 23.250  1.00 51.14  ? 190 ASP A N   1 
ATOM   4779 C  CA  . ASP B 1 217 ? -41.033 -49.565 24.539  1.00 54.13  ? 190 ASP A CA  1 
ATOM   4780 C  C   . ASP B 1 217 ? -42.480 -49.220 24.869  1.00 54.84  ? 190 ASP A C   1 
ATOM   4781 O  O   . ASP B 1 217 ? -43.011 -49.651 25.914  1.00 58.08  ? 190 ASP A O   1 
ATOM   4782 C  CB  . ASP B 1 217 ? -40.110 -49.077 25.651  1.00 55.30  ? 190 ASP A CB  1 
ATOM   4783 C  CG  . ASP B 1 217 ? -38.770 -49.806 25.630  1.00 62.65  ? 190 ASP A CG  1 
ATOM   4784 O  OD1 . ASP B 1 217 ? -38.801 -51.054 25.519  1.00 59.27  ? 190 ASP A OD1 1 
ATOM   4785 O  OD2 . ASP B 1 217 ? -37.696 -49.143 25.703  1.00 77.24  ? 190 ASP A OD2 1 
ATOM   4786 N  N   . GLU B 1 218 ? -43.137 -48.478 23.993  1.00 52.27  ? 191 GLU A N   1 
ATOM   4787 C  CA  . GLU B 1 218 ? -44.516 -48.113 24.244  1.00 58.61  ? 191 GLU A CA  1 
ATOM   4788 C  C   . GLU B 1 218 ? -45.327 -49.326 24.728  1.00 59.78  ? 191 GLU A C   1 
ATOM   4789 O  O   . GLU B 1 218 ? -45.991 -49.258 25.754  1.00 65.15  ? 191 GLU A O   1 
ATOM   4790 C  CB  . GLU B 1 218 ? -45.114 -47.489 22.990  1.00 63.81  ? 191 GLU A CB  1 
ATOM   4791 C  CG  . GLU B 1 218 ? -44.440 -46.182 22.590  1.00 66.58  ? 191 GLU A CG  1 
ATOM   4792 C  CD  . GLU B 1 218 ? -44.718 -45.089 23.583  1.00 65.50  ? 191 GLU A CD  1 
ATOM   4793 O  OE1 . GLU B 1 218 ? -45.748 -44.429 23.366  1.00 75.41  ? 191 GLU A OE1 1 
ATOM   4794 O  OE2 . GLU B 1 218 ? -43.952 -44.930 24.572  1.00 65.25  ? 191 GLU A OE2 1 
ATOM   4795 N  N   . HIS B 1 219 ? -45.217 -50.452 24.031  1.00 58.32  ? 192 HIS A N   1 
ATOM   4796 C  CA  . HIS B 1 219 ? -45.998 -51.637 24.384  1.00 57.89  ? 192 HIS A CA  1 
ATOM   4797 C  C   . HIS B 1 219 ? -45.523 -52.305 25.647  1.00 57.61  ? 192 HIS A C   1 
ATOM   4798 O  O   . HIS B 1 219 ? -46.318 -52.703 26.467  1.00 63.44  ? 192 HIS A O   1 
ATOM   4799 C  CB  . HIS B 1 219 ? -45.985 -52.676 23.266  1.00 60.45  ? 192 HIS A CB  1 
ATOM   4800 C  CG  . HIS B 1 219 ? -47.022 -52.436 22.214  1.00 56.96  ? 192 HIS A CG  1 
ATOM   4801 N  ND1 . HIS B 1 219 ? -48.374 -52.452 22.487  1.00 60.53  ? 192 HIS A ND1 1 
ATOM   4802 C  CD2 . HIS B 1 219 ? -46.903 -52.181 20.893  1.00 54.92  ? 192 HIS A CD2 1 
ATOM   4803 C  CE1 . HIS B 1 219 ? -49.043 -52.203 21.375  1.00 60.80  ? 192 HIS A CE1 1 
ATOM   4804 N  NE2 . HIS B 1 219 ? -48.172 -52.036 20.395  1.00 58.67  ? 192 HIS A NE2 1 
ATOM   4805 N  N   . GLN B 1 220 ? -44.223 -52.458 25.783  1.00 55.80  ? 193 GLN A N   1 
ATOM   4806 C  CA  . GLN B 1 220 ? -43.656 -53.042 26.968  1.00 49.52  ? 193 GLN A CA  1 
ATOM   4807 C  C   . GLN B 1 220 ? -44.144 -52.365 28.232  1.00 49.14  ? 193 GLN A C   1 
ATOM   4808 O  O   . GLN B 1 220 ? -44.436 -53.028 29.199  1.00 52.17  ? 193 GLN A O   1 
ATOM   4809 C  CB  . GLN B 1 220 ? -42.140 -52.926 26.929  1.00 58.63  ? 193 GLN A CB  1 
ATOM   4810 C  CG  . GLN B 1 220 ? -41.474 -54.066 27.650  1.00 65.22  ? 193 GLN A CG  1 
ATOM   4811 C  CD  . GLN B 1 220 ? -39.986 -53.905 27.771  1.00 61.89  ? 193 GLN A CD  1 
ATOM   4812 O  OE1 . GLN B 1 220 ? -39.279 -53.713 26.801  1.00 73.05  ? 193 GLN A OE1 1 
ATOM   4813 N  NE2 . GLN B 1 220 ? -39.510 -54.010 28.977  1.00 64.24  ? 193 GLN A NE2 1 
ATOM   4814 N  N   . ALA B 1 221 ? -44.216 -51.041 28.246  1.00 50.53  ? 194 ALA A N   1 
ATOM   4815 C  CA  . ALA B 1 221 ? -44.590 -50.329 29.469  1.00 47.99  ? 194 ALA A CA  1 
ATOM   4816 C  C   . ALA B 1 221 ? -46.074 -50.499 29.702  1.00 48.48  ? 194 ALA A C   1 
ATOM   4817 O  O   . ALA B 1 221 ? -46.522 -50.526 30.844  1.00 51.45  ? 194 ALA A O   1 
ATOM   4818 C  CB  . ALA B 1 221 ? -44.242 -48.846 29.370  1.00 50.13  ? 194 ALA A CB  1 
ATOM   4819 N  N   . THR B 1 222 ? -46.838 -50.597 28.618  1.00 46.68  ? 195 THR A N   1 
ATOM   4820 C  CA  . THR B 1 222 ? -48.248 -50.896 28.734  1.00 48.68  ? 195 THR A CA  1 
ATOM   4821 C  C   . THR B 1 222 ? -48.403 -52.349 29.278  1.00 50.45  ? 195 THR A C   1 
ATOM   4822 O  O   . THR B 1 222 ? -49.236 -52.605 30.163  1.00 46.35  ? 195 THR A O   1 
ATOM   4823 C  CB  . THR B 1 222 ? -48.997 -50.717 27.383  1.00 49.39  ? 195 THR A CB  1 
ATOM   4824 O  OG1 . THR B 1 222 ? -48.633 -49.480 26.743  1.00 49.07  ? 195 THR A OG1 1 
ATOM   4825 C  CG2 . THR B 1 222 ? -50.491 -50.728 27.611  1.00 46.91  ? 195 THR A CG2 1 
ATOM   4826 N  N   . ALA B 1 223 ? -47.584 -53.282 28.782  1.00 46.11  ? 196 ALA A N   1 
ATOM   4827 C  CA  . ALA B 1 223 ? -47.677 -54.667 29.205  1.00 47.80  ? 196 ALA A CA  1 
ATOM   4828 C  C   . ALA B 1 223 ? -47.513 -54.706 30.690  1.00 51.24  ? 196 ALA A C   1 
ATOM   4829 O  O   . ALA B 1 223 ? -48.276 -55.370 31.397  1.00 49.13  ? 196 ALA A O   1 
ATOM   4830 C  CB  . ALA B 1 223 ? -46.608 -55.519 28.565  1.00 49.70  ? 196 ALA A CB  1 
ATOM   4831 N  N   . MET B 1 224 ? -46.510 -53.986 31.173  1.00 51.17  ? 197 MET A N   1 
ATOM   4832 C  CA  . MET B 1 224 ? -46.275 -53.969 32.595  1.00 52.42  ? 197 MET A CA  1 
ATOM   4833 C  C   . MET B 1 224 ? -47.548 -53.603 33.349  1.00 53.48  ? 197 MET A C   1 
ATOM   4834 O  O   . MET B 1 224 ? -47.849 -54.214 34.375  1.00 50.33  ? 197 MET A O   1 
ATOM   4835 C  CB  . MET B 1 224 ? -45.173 -52.990 32.953  1.00 55.93  ? 197 MET A CB  1 
ATOM   4836 C  CG  . MET B 1 224 ? -43.824 -53.633 33.153  1.00 58.03  ? 197 MET A CG  1 
ATOM   4837 S  SD  . MET B 1 224 ? -42.524 -52.435 32.853  1.00 69.95  ? 197 MET A SD  1 
ATOM   4838 C  CE  . MET B 1 224 ? -41.113 -53.529 33.022  1.00 85.50  ? 197 MET A CE  1 
ATOM   4839 N  N   . ALA B 1 225 ? -48.288 -52.604 32.850  1.00 48.19  ? 198 ALA A N   1 
ATOM   4840 C  CA  . ALA B 1 225 ? -49.458 -52.131 33.572  1.00 46.34  ? 198 ALA A CA  1 
ATOM   4841 C  C   . ALA B 1 225 ? -50.596 -53.146 33.416  1.00 51.05  ? 198 ALA A C   1 
ATOM   4842 O  O   . ALA B 1 225 ? -51.386 -53.314 34.317  1.00 49.87  ? 198 ALA A O   1 
ATOM   4843 C  CB  . ALA B 1 225 ? -49.866 -50.740 33.109  1.00 45.64  ? 198 ALA A CB  1 
ATOM   4844 N  N   . ASP B 1 226 ? -50.650 -53.842 32.279  1.00 54.40  ? 199 ASP A N   1 
ATOM   4845 C  CA  . ASP B 1 226 ? -51.580 -54.961 32.106  1.00 52.61  ? 199 ASP A CA  1 
ATOM   4846 C  C   . ASP B 1 226 ? -51.322 -56.074 33.127  1.00 52.77  ? 199 ASP A C   1 
ATOM   4847 O  O   . ASP B 1 226 ? -52.260 -56.630 33.678  1.00 57.42  ? 199 ASP A O   1 
ATOM   4848 C  CB  . ASP B 1 226 ? -51.554 -55.505 30.661  1.00 45.71  ? 199 ASP A CB  1 
ATOM   4849 C  CG  . ASP B 1 226 ? -52.385 -54.649 29.714  1.00 51.00  ? 199 ASP A CG  1 
ATOM   4850 O  OD1 . ASP B 1 226 ? -53.166 -53.807 30.211  1.00 58.63  ? 199 ASP A OD1 1 
ATOM   4851 O  OD2 . ASP B 1 226 ? -52.274 -54.774 28.480  1.00 55.25  ? 199 ASP A OD2 1 
ATOM   4852 N  N   . ILE B 1 227 ? -50.059 -56.373 33.393  1.00 50.01  ? 200 ILE A N   1 
ATOM   4853 C  CA  . ILE B 1 227 ? -49.711 -57.411 34.339  1.00 52.49  ? 200 ILE A CA  1 
ATOM   4854 C  C   . ILE B 1 227 ? -50.206 -57.010 35.731  1.00 56.37  ? 200 ILE A C   1 
ATOM   4855 O  O   . ILE B 1 227 ? -50.875 -57.782 36.416  1.00 57.25  ? 200 ILE A O   1 
ATOM   4856 C  CB  . ILE B 1 227 ? -48.195 -57.699 34.306  1.00 52.23  ? 200 ILE A CB  1 
ATOM   4857 C  CG1 . ILE B 1 227 ? -47.843 -58.470 33.038  1.00 55.17  ? 200 ILE A CG1 1 
ATOM   4858 C  CG2 . ILE B 1 227 ? -47.743 -58.487 35.514  1.00 53.47  ? 200 ILE A CG2 1 
ATOM   4859 C  CD1 . ILE B 1 227 ? -46.351 -58.597 32.780  1.00 59.82  ? 200 ILE A CD1 1 
ATOM   4860 N  N   . ILE B 1 228 ? -49.914 -55.791 36.147  1.00 59.13  ? 201 ILE A N   1 
ATOM   4861 C  CA  . ILE B 1 228 ? -50.409 -55.312 37.454  1.00 58.15  ? 201 ILE A CA  1 
ATOM   4862 C  C   . ILE B 1 228 ? -51.939 -55.333 37.610  1.00 54.36  ? 201 ILE A C   1 
ATOM   4863 O  O   . ILE B 1 228 ? -52.426 -55.839 38.605  1.00 52.51  ? 201 ILE A O   1 
ATOM   4864 C  CB  . ILE B 1 228 ? -49.854 -53.918 37.753  1.00 57.67  ? 201 ILE A CB  1 
ATOM   4865 C  CG1 . ILE B 1 228 ? -48.369 -54.059 38.099  1.00 54.22  ? 201 ILE A CG1 1 
ATOM   4866 C  CG2 . ILE B 1 228 ? -50.626 -53.244 38.879  1.00 56.70  ? 201 ILE A CG2 1 
ATOM   4867 C  CD1 . ILE B 1 228 ? -47.591 -52.810 37.817  1.00 55.30  ? 201 ILE A CD1 1 
ATOM   4868 N  N   . GLU B 1 229 ? -52.678 -54.779 36.643  1.00 55.72  ? 202 GLU A N   1 
ATOM   4869 C  CA  . GLU B 1 229 ? -54.160 -54.889 36.577  1.00 57.79  ? 202 GLU A CA  1 
ATOM   4870 C  C   . GLU B 1 229 ? -54.590 -56.348 36.773  1.00 54.95  ? 202 GLU A C   1 
ATOM   4871 O  O   . GLU B 1 229 ? -55.386 -56.653 37.648  1.00 45.53  ? 202 GLU A O   1 
ATOM   4872 C  CB  . GLU B 1 229 ? -54.681 -54.351 35.229  1.00 62.09  ? 202 GLU A CB  1 
ATOM   4873 C  CG  . GLU B 1 229 ? -56.198 -54.226 35.072  1.00 70.09  ? 202 GLU A CG  1 
ATOM   4874 C  CD  . GLU B 1 229 ? -56.635 -53.602 33.718  1.00 73.19  ? 202 GLU A CD  1 
ATOM   4875 O  OE1 . GLU B 1 229 ? -57.657 -52.886 33.660  1.00 81.19  ? 202 GLU A OE1 1 
ATOM   4876 O  OE2 . GLU B 1 229 ? -55.974 -53.812 32.687  1.00 67.61  ? 202 GLU A OE2 1 
ATOM   4877 N  N   . TYR B 1 230 ? -53.983 -57.252 36.010  1.00 55.50  ? 203 TYR A N   1 
ATOM   4878 C  CA  . TYR B 1 230 ? -54.320 -58.673 36.067  1.00 57.31  ? 203 TYR A CA  1 
ATOM   4879 C  C   . TYR B 1 230 ? -54.304 -59.256 37.473  1.00 54.21  ? 203 TYR A C   1 
ATOM   4880 O  O   . TYR B 1 230 ? -55.262 -59.891 37.873  1.00 54.05  ? 203 TYR A O   1 
ATOM   4881 C  CB  . TYR B 1 230 ? -53.371 -59.484 35.194  1.00 59.23  ? 203 TYR A CB  1 
ATOM   4882 C  CG  . TYR B 1 230 ? -53.720 -60.946 35.082  1.00 64.45  ? 203 TYR A CG  1 
ATOM   4883 C  CD1 . TYR B 1 230 ? -54.659 -61.381 34.153  1.00 68.21  ? 203 TYR A CD1 1 
ATOM   4884 C  CD2 . TYR B 1 230 ? -53.100 -61.901 35.889  1.00 62.41  ? 203 TYR A CD2 1 
ATOM   4885 C  CE1 . TYR B 1 230 ? -54.982 -62.726 34.041  1.00 70.75  ? 203 TYR A CE1 1 
ATOM   4886 C  CE2 . TYR B 1 230 ? -53.408 -63.244 35.768  1.00 65.72  ? 203 TYR A CE2 1 
ATOM   4887 C  CZ  . TYR B 1 230 ? -54.350 -63.653 34.841  1.00 66.04  ? 203 TYR A CZ  1 
ATOM   4888 O  OH  . TYR B 1 230 ? -54.676 -64.978 34.697  1.00 65.96  ? 203 TYR A OH  1 
ATOM   4889 N  N   . PHE B 1 231 ? -53.214 -59.062 38.205  1.00 53.82  ? 204 PHE A N   1 
ATOM   4890 C  CA  . PHE B 1 231 ? -53.113 -59.565 39.578  1.00 53.15  ? 204 PHE A CA  1 
ATOM   4891 C  C   . PHE B 1 231 ? -53.761 -58.639 40.607  1.00 55.44  ? 204 PHE A C   1 
ATOM   4892 O  O   . PHE B 1 231 ? -53.683 -58.897 41.804  1.00 57.05  ? 204 PHE A O   1 
ATOM   4893 C  CB  . PHE B 1 231 ? -51.646 -59.809 39.963  1.00 56.27  ? 204 PHE A CB  1 
ATOM   4894 C  CG  . PHE B 1 231 ? -51.009 -60.950 39.240  1.00 53.28  ? 204 PHE A CG  1 
ATOM   4895 C  CD1 . PHE B 1 231 ? -51.135 -62.249 39.723  1.00 51.74  ? 204 PHE A CD1 1 
ATOM   4896 C  CD2 . PHE B 1 231 ? -50.288 -60.732 38.085  1.00 54.71  ? 204 PHE A CD2 1 
ATOM   4897 C  CE1 . PHE B 1 231 ? -50.557 -63.316 39.065  1.00 53.07  ? 204 PHE A CE1 1 
ATOM   4898 C  CE2 . PHE B 1 231 ? -49.689 -61.795 37.413  1.00 58.25  ? 204 PHE A CE2 1 
ATOM   4899 C  CZ  . PHE B 1 231 ? -49.826 -63.086 37.904  1.00 60.90  ? 204 PHE A CZ  1 
ATOM   4900 N  N   . ARG B 1 232 ? -54.392 -57.550 40.157  1.00 62.63  ? 205 ARG A N   1 
ATOM   4901 C  CA  . ARG B 1 232 ? -55.073 -56.615 41.071  1.00 59.58  ? 205 ARG A CA  1 
ATOM   4902 C  C   . ARG B 1 232 ? -54.132 -55.985 42.102  1.00 58.19  ? 205 ARG A C   1 
ATOM   4903 O  O   . ARG B 1 232 ? -54.547 -55.662 43.209  1.00 52.86  ? 205 ARG A O   1 
ATOM   4904 C  CB  . ARG B 1 232 ? -56.188 -57.329 41.813  1.00 61.15  ? 205 ARG A CB  1 
ATOM   4905 C  CG  . ARG B 1 232 ? -56.801 -58.479 41.047  1.00 66.92  ? 205 ARG A CG  1 
ATOM   4906 C  CD  . ARG B 1 232 ? -57.749 -58.087 39.926  1.00 62.06  ? 205 ARG A CD  1 
ATOM   4907 N  NE  . ARG B 1 232 ? -58.393 -59.324 39.489  1.00 61.34  ? 205 ARG A NE  1 
ATOM   4908 C  CZ  . ARG B 1 232 ? -59.380 -59.402 38.623  1.00 65.41  ? 205 ARG A CZ  1 
ATOM   4909 N  NH1 . ARG B 1 232 ? -59.862 -58.327 38.036  1.00 81.03  ? 205 ARG A NH1 1 
ATOM   4910 N  NH2 . ARG B 1 232 ? -59.873 -60.575 38.331  1.00 73.42  ? 205 ARG A NH2 1 
ATOM   4911 N  N   . TRP B 1 233 ? -52.860 -55.848 41.735  1.00 60.51  ? 206 TRP A N   1 
ATOM   4912 C  CA  . TRP B 1 233 ? -51.897 -55.099 42.514  1.00 59.18  ? 206 TRP A CA  1 
ATOM   4913 C  C   . TRP B 1 233 ? -52.224 -53.632 42.426  1.00 58.45  ? 206 TRP A C   1 
ATOM   4914 O  O   . TRP B 1 233 ? -52.857 -53.188 41.470  1.00 66.63  ? 206 TRP A O   1 
ATOM   4915 C  CB  . TRP B 1 233 ? -50.497 -55.375 42.015  1.00 60.15  ? 206 TRP A CB  1 
ATOM   4916 C  CG  . TRP B 1 233 ? -50.098 -56.801 42.240  1.00 66.10  ? 206 TRP A CG  1 
ATOM   4917 C  CD1 . TRP B 1 233 ? -50.535 -57.627 43.233  1.00 64.49  ? 206 TRP A CD1 1 
ATOM   4918 C  CD2 . TRP B 1 233 ? -49.166 -57.562 41.474  1.00 63.59  ? 206 TRP A CD2 1 
ATOM   4919 N  NE1 . TRP B 1 233 ? -49.927 -58.840 43.136  1.00 62.56  ? 206 TRP A NE1 1 
ATOM   4920 C  CE2 . TRP B 1 233 ? -49.095 -58.838 42.054  1.00 63.36  ? 206 TRP A CE2 1 
ATOM   4921 C  CE3 . TRP B 1 233 ? -48.394 -57.293 40.349  1.00 62.97  ? 206 TRP A CE3 1 
ATOM   4922 C  CZ2 . TRP B 1 233 ? -48.282 -59.842 41.552  1.00 61.25  ? 206 TRP A CZ2 1 
ATOM   4923 C  CZ3 . TRP B 1 233 ? -47.586 -58.293 39.849  1.00 65.43  ? 206 TRP A CZ3 1 
ATOM   4924 C  CH2 . TRP B 1 233 ? -47.535 -59.552 40.456  1.00 62.23  ? 206 TRP A CH2 1 
ATOM   4925 N  N   . ASN B 1 234 ? -51.796 -52.879 43.421  1.00 55.37  ? 207 ASN A N   1 
ATOM   4926 C  CA  . ASN B 1 234 ? -52.529 -51.694 43.766  1.00 65.54  ? 207 ASN A CA  1 
ATOM   4927 C  C   . ASN B 1 234 ? -51.739 -50.468 44.064  1.00 73.86  ? 207 ASN A C   1 
ATOM   4928 O  O   . ASN B 1 234 ? -52.260 -49.386 43.694  1.00 82.37  ? 207 ASN A O   1 
ATOM   4929 C  CB  . ASN B 1 234 ? -53.405 -51.962 44.987  1.00 82.39  ? 207 ASN A CB  1 
ATOM   4930 N  N   . TRP B 1 235 ? -50.577 -50.587 44.765  1.00 56.20  ? 208 TRP A N   1 
ATOM   4931 C  CA  . TRP B 1 235 ? -49.761 -49.369 45.143  1.00 58.63  ? 208 TRP A CA  1 
ATOM   4932 C  C   . TRP B 1 235 ? -48.294 -49.611 44.937  1.00 58.59  ? 208 TRP A C   1 
ATOM   4933 O  O   . TRP B 1 235 ? -47.545 -49.861 45.888  1.00 58.34  ? 208 TRP A O   1 
ATOM   4934 C  CB  . TRP B 1 235 ? -49.964 -48.913 46.617  1.00 61.76  ? 208 TRP A CB  1 
ATOM   4935 C  CG  . TRP B 1 235 ? -51.092 -47.978 46.829  1.00 56.93  ? 208 TRP A CG  1 
ATOM   4936 C  CD1 . TRP B 1 235 ? -52.385 -48.311 47.077  1.00 56.55  ? 208 TRP A CD1 1 
ATOM   4937 C  CD2 . TRP B 1 235 ? -51.044 -46.547 46.766  1.00 63.00  ? 208 TRP A CD2 1 
ATOM   4938 N  NE1 . TRP B 1 235 ? -53.159 -47.176 47.179  1.00 60.71  ? 208 TRP A NE1 1 
ATOM   4939 C  CE2 . TRP B 1 235 ? -52.360 -46.075 46.991  1.00 63.56  ? 208 TRP A CE2 1 
ATOM   4940 C  CE3 . TRP B 1 235 ? -50.020 -45.613 46.543  1.00 62.27  ? 208 TRP A CE3 1 
ATOM   4941 C  CZ2 . TRP B 1 235 ? -52.681 -44.701 47.006  1.00 61.26  ? 208 TRP A CZ2 1 
ATOM   4942 C  CZ3 . TRP B 1 235 ? -50.340 -44.251 46.563  1.00 62.69  ? 208 TRP A CZ3 1 
ATOM   4943 C  CH2 . TRP B 1 235 ? -51.664 -43.810 46.788  1.00 60.72  ? 208 TRP A CH2 1 
ATOM   4944 N  N   . VAL B 1 236 ? -47.864 -49.500 43.693  1.00 55.85  ? 209 VAL A N   1 
ATOM   4945 C  CA  . VAL B 1 236 ? -46.562 -50.023 43.287  1.00 48.21  ? 209 VAL A CA  1 
ATOM   4946 C  C   . VAL B 1 236 ? -45.441 -48.987 43.364  1.00 49.27  ? 209 VAL A C   1 
ATOM   4947 O  O   . VAL B 1 236 ? -45.684 -47.778 43.411  1.00 52.04  ? 209 VAL A O   1 
ATOM   4948 C  CB  . VAL B 1 236 ? -46.711 -50.604 41.891  1.00 49.65  ? 209 VAL A CB  1 
ATOM   4949 C  CG1 . VAL B 1 236 ? -47.939 -51.505 41.883  1.00 47.72  ? 209 VAL A CG1 1 
ATOM   4950 C  CG2 . VAL B 1 236 ? -46.880 -49.502 40.848  1.00 53.83  ? 209 VAL A CG2 1 
ATOM   4951 N  N   . GLY B 1 237 ? -44.212 -49.476 43.428  1.00 49.44  ? 210 GLY A N   1 
ATOM   4952 C  CA  . GLY B 1 237 ? -43.010 -48.637 43.385  1.00 46.05  ? 210 GLY A CA  1 
ATOM   4953 C  C   . GLY B 1 237 ? -42.462 -48.561 41.966  1.00 47.39  ? 210 GLY A C   1 
ATOM   4954 O  O   . GLY B 1 237 ? -42.714 -49.448 41.137  1.00 42.49  ? 210 GLY A O   1 
ATOM   4955 N  N   . THR B 1 238 ? -41.758 -47.470 41.659  1.00 48.45  ? 211 THR A N   1 
ATOM   4956 C  CA  . THR B 1 238 ? -41.102 -47.350 40.371  1.00 47.07  ? 211 THR A CA  1 
ATOM   4957 C  C   . THR B 1 238 ? -39.683 -46.888 40.484  1.00 48.09  ? 211 THR A C   1 
ATOM   4958 O  O   . THR B 1 238 ? -39.357 -45.991 41.276  1.00 42.39  ? 211 THR A O   1 
ATOM   4959 C  CB  . THR B 1 238 ? -41.846 -46.460 39.358  1.00 48.81  ? 211 THR A CB  1 
ATOM   4960 O  OG1 . THR B 1 238 ? -41.981 -45.123 39.838  1.00 53.56  ? 211 THR A OG1 1 
ATOM   4961 C  CG2 . THR B 1 238 ? -43.225 -47.030 39.060  1.00 51.67  ? 211 THR A CG2 1 
ATOM   4962 N  N   . ILE B 1 239 ? -38.835 -47.533 39.682  1.00 46.72  ? 212 ILE A N   1 
ATOM   4963 C  CA  . ILE B 1 239 ? -37.434 -47.196 39.604  1.00 46.62  ? 212 ILE A CA  1 
ATOM   4964 C  C   . ILE B 1 239 ? -36.994 -47.222 38.150  1.00 45.36  ? 212 ILE A C   1 
ATOM   4965 O  O   . ILE B 1 239 ? -37.283 -48.165 37.404  1.00 43.27  ? 212 ILE A O   1 
ATOM   4966 C  CB  . ILE B 1 239 ? -36.608 -48.170 40.443  1.00 48.88  ? 212 ILE A CB  1 
ATOM   4967 C  CG1 . ILE B 1 239 ? -36.898 -47.942 41.925  1.00 49.91  ? 212 ILE A CG1 1 
ATOM   4968 C  CG2 . ILE B 1 239 ? -35.131 -47.959 40.232  1.00 48.52  ? 212 ILE A CG2 1 
ATOM   4969 C  CD1 . ILE B 1 239 ? -36.547 -49.148 42.759  1.00 52.78  ? 212 ILE A CD1 1 
ATOM   4970 N  N   . ALA B 1 240 ? -36.284 -46.170 37.756  1.00 46.23  ? 213 ALA A N   1 
ATOM   4971 C  CA  . ALA B 1 240 ? -35.836 -46.004 36.381  1.00 44.41  ? 213 ALA A CA  1 
ATOM   4972 C  C   . ALA B 1 240 ? -34.433 -45.434 36.290  1.00 44.71  ? 213 ALA A C   1 
ATOM   4973 O  O   . ALA B 1 240 ? -34.075 -44.495 37.025  1.00 44.89  ? 213 ALA A O   1 
ATOM   4974 C  CB  . ALA B 1 240 ? -36.782 -45.079 35.669  1.00 50.05  ? 213 ALA A CB  1 
ATOM   4975 N  N   . ALA B 1 241 ? -33.632 -45.994 35.386  1.00 43.95  ? 214 ALA A N   1 
ATOM   4976 C  CA  . ALA B 1 241 ? -32.366 -45.363 35.020  1.00 41.05  ? 214 ALA A CA  1 
ATOM   4977 C  C   . ALA B 1 241 ? -32.594 -43.925 34.570  1.00 38.00  ? 214 ALA A C   1 
ATOM   4978 O  O   . ALA B 1 241 ? -33.429 -43.670 33.740  1.00 38.93  ? 214 ALA A O   1 
ATOM   4979 C  CB  . ALA B 1 241 ? -31.691 -46.129 33.912  1.00 39.30  ? 214 ALA A CB  1 
ATOM   4980 N  N   . ASP B 1 242 ? -31.831 -42.994 35.118  1.00 38.60  ? 215 ASP A N   1 
ATOM   4981 C  CA  . ASP B 1 242 ? -31.839 -41.600 34.670  1.00 40.66  ? 215 ASP A CA  1 
ATOM   4982 C  C   . ASP B 1 242 ? -31.246 -41.333 33.265  1.00 44.52  ? 215 ASP A C   1 
ATOM   4983 O  O   . ASP B 1 242 ? -30.187 -40.711 33.120  1.00 45.26  ? 215 ASP A O   1 
ATOM   4984 C  CB  . ASP B 1 242 ? -31.123 -40.703 35.681  1.00 38.67  ? 215 ASP A CB  1 
ATOM   4985 C  CG  . ASP B 1 242 ? -31.679 -39.274 35.677  1.00 45.12  ? 215 ASP A CG  1 
ATOM   4986 O  OD1 . ASP B 1 242 ? -32.611 -38.967 34.903  1.00 52.14  ? 215 ASP A OD1 1 
ATOM   4987 O  OD2 . ASP B 1 242 ? -31.230 -38.443 36.476  1.00 49.70  ? 215 ASP A OD2 1 
ATOM   4988 N  N   . ASP B 1 243 ? -31.973 -41.724 32.231  1.00 44.72  ? 216 ASP A N   1 
ATOM   4989 C  CA  . ASP B 1 243 ? -31.497 -41.542 30.873  1.00 47.52  ? 216 ASP A CA  1 
ATOM   4990 C  C   . ASP B 1 243 ? -32.663 -41.673 29.920  1.00 48.95  ? 216 ASP A C   1 
ATOM   4991 O  O   . ASP B 1 243 ? -33.812 -41.674 30.357  1.00 53.75  ? 216 ASP A O   1 
ATOM   4992 C  CB  . ASP B 1 243 ? -30.414 -42.572 30.558  1.00 53.18  ? 216 ASP A CB  1 
ATOM   4993 C  CG  . ASP B 1 243 ? -30.910 -44.008 30.682  1.00 59.07  ? 216 ASP A CG  1 
ATOM   4994 O  OD1 . ASP B 1 243 ? -31.965 -44.359 30.116  1.00 63.86  ? 216 ASP A OD1 1 
ATOM   4995 O  OD2 . ASP B 1 243 ? -30.236 -44.793 31.357  1.00 73.02  ? 216 ASP A OD2 1 
ATOM   4996 N  N   . ASP B 1 244 ? -32.397 -41.822 28.626  1.00 48.68  ? 217 ASP A N   1 
ATOM   4997 C  CA  . ASP B 1 244 ? -33.475 -41.744 27.668  1.00 45.87  ? 217 ASP A CA  1 
ATOM   4998 C  C   . ASP B 1 244 ? -34.139 -43.066 27.503  1.00 47.17  ? 217 ASP A C   1 
ATOM   4999 O  O   . ASP B 1 244 ? -35.105 -43.154 26.744  1.00 48.49  ? 217 ASP A O   1 
ATOM   5000 C  CB  . ASP B 1 244 ? -32.974 -41.210 26.327  1.00 50.02  ? 217 ASP A CB  1 
ATOM   5001 C  CG  . ASP B 1 244 ? -32.695 -39.699 26.360  1.00 55.11  ? 217 ASP A CG  1 
ATOM   5002 O  OD1 . ASP B 1 244 ? -33.251 -39.004 27.260  1.00 59.54  ? 217 ASP A OD1 1 
ATOM   5003 O  OD2 . ASP B 1 244 ? -31.931 -39.203 25.487  1.00 54.97  ? 217 ASP A OD2 1 
ATOM   5004 N  N   . TYR B 1 245 ? -33.645 -44.107 28.191  1.00 46.76  ? 218 TYR A N   1 
ATOM   5005 C  CA  . TYR B 1 245 ? -34.332 -45.412 28.193  1.00 44.99  ? 218 TYR A CA  1 
ATOM   5006 C  C   . TYR B 1 245 ? -35.299 -45.472 29.347  1.00 42.55  ? 218 TYR A C   1 
ATOM   5007 O  O   . TYR B 1 245 ? -36.463 -45.754 29.151  1.00 44.35  ? 218 TYR A O   1 
ATOM   5008 C  CB  . TYR B 1 245 ? -33.355 -46.582 28.231  1.00 43.20  ? 218 TYR A CB  1 
ATOM   5009 C  CG  . TYR B 1 245 ? -33.959 -47.961 28.491  1.00 47.47  ? 218 TYR A CG  1 
ATOM   5010 C  CD1 . TYR B 1 245 ? -34.772 -48.574 27.547  1.00 45.19  ? 218 TYR A CD1 1 
ATOM   5011 C  CD2 . TYR B 1 245 ? -33.689 -48.671 29.683  1.00 49.65  ? 218 TYR A CD2 1 
ATOM   5012 C  CE1 . TYR B 1 245 ? -35.329 -49.818 27.783  1.00 46.75  ? 218 TYR A CE1 1 
ATOM   5013 C  CE2 . TYR B 1 245 ? -34.235 -49.952 29.914  1.00 46.12  ? 218 TYR A CE2 1 
ATOM   5014 C  CZ  . TYR B 1 245 ? -35.052 -50.519 28.965  1.00 44.85  ? 218 TYR A CZ  1 
ATOM   5015 O  OH  . TYR B 1 245 ? -35.613 -51.778 29.138  1.00 43.73  ? 218 TYR A OH  1 
ATOM   5016 N  N   . GLY B 1 246 ? -34.811 -45.159 30.532  1.00 44.86  ? 219 GLY A N   1 
ATOM   5017 C  CA  . GLY B 1 246 ? -35.568 -45.338 31.760  1.00 44.88  ? 219 GLY A CA  1 
ATOM   5018 C  C   . GLY B 1 246 ? -36.647 -44.306 31.959  1.00 44.81  ? 219 GLY A C   1 
ATOM   5019 O  O   . GLY B 1 246 ? -37.806 -44.665 32.099  1.00 50.07  ? 219 GLY A O   1 
ATOM   5020 N  N   . ARG B 1 247 ? -36.293 -43.027 31.943  1.00 42.70  ? 220 ARG A N   1 
ATOM   5021 C  CA  . ARG B 1 247 ? -37.304 -41.966 32.099  1.00 43.26  ? 220 ARG A CA  1 
ATOM   5022 C  C   . ARG B 1 247 ? -38.518 -42.125 31.162  1.00 44.54  ? 220 ARG A C   1 
ATOM   5023 O  O   . ARG B 1 247 ? -39.656 -42.054 31.627  1.00 51.99  ? 220 ARG A O   1 
ATOM   5024 C  CB  . ARG B 1 247 ? -36.701 -40.554 31.975  1.00 39.85  ? 220 ARG A CB  1 
ATOM   5025 C  CG  . ARG B 1 247 ? -35.635 -40.257 33.036  1.00 43.73  ? 220 ARG A CG  1 
ATOM   5026 C  CD  . ARG B 1 247 ? -35.142 -38.816 33.008  1.00 42.74  ? 220 ARG A CD  1 
ATOM   5027 N  NE  . ARG B 1 247 ? -34.727 -38.453 31.678  1.00 43.68  ? 220 ARG A NE  1 
ATOM   5028 C  CZ  . ARG B 1 247 ? -33.470 -38.382 31.292  1.00 50.25  ? 220 ARG A CZ  1 
ATOM   5029 N  NH1 . ARG B 1 247 ? -32.491 -38.613 32.150  1.00 57.28  ? 220 ARG A NH1 1 
ATOM   5030 N  NH2 . ARG B 1 247 ? -33.186 -38.069 30.043  1.00 54.76  ? 220 ARG A NH2 1 
ATOM   5031 N  N   . PRO B 1 248 ? -38.297 -42.328 29.849  1.00 42.98  ? 221 PRO A N   1 
ATOM   5032 C  CA  . PRO B 1 248 ? -39.481 -42.371 29.017  1.00 43.49  ? 221 PRO A CA  1 
ATOM   5033 C  C   . PRO B 1 248 ? -40.299 -43.617 29.172  1.00 41.23  ? 221 PRO A C   1 
ATOM   5034 O  O   . PRO B 1 248 ? -41.496 -43.580 28.947  1.00 51.08  ? 221 PRO A O   1 
ATOM   5035 C  CB  . PRO B 1 248 ? -38.924 -42.279 27.587  1.00 41.04  ? 221 PRO A CB  1 
ATOM   5036 C  CG  . PRO B 1 248 ? -37.622 -41.676 27.721  1.00 39.76  ? 221 PRO A CG  1 
ATOM   5037 C  CD  . PRO B 1 248 ? -37.089 -42.181 29.030  1.00 42.00  ? 221 PRO A CD  1 
ATOM   5038 N  N   . GLY B 1 249 ? -39.656 -44.718 29.501  1.00 41.58  ? 222 GLY A N   1 
ATOM   5039 C  CA  . GLY B 1 249 ? -40.366 -45.953 29.750  1.00 42.18  ? 222 GLY A CA  1 
ATOM   5040 C  C   . GLY B 1 249 ? -41.248 -45.812 30.967  1.00 47.26  ? 222 GLY A C   1 
ATOM   5041 O  O   . GLY B 1 249 ? -42.398 -46.199 30.955  1.00 54.45  ? 222 GLY A O   1 
ATOM   5042 N  N   . ILE B 1 250 ? -40.721 -45.247 32.038  1.00 49.31  ? 223 ILE A N   1 
ATOM   5043 C  CA  . ILE B 1 250 ? -41.516 -45.120 33.232  1.00 50.59  ? 223 ILE A CA  1 
ATOM   5044 C  C   . ILE B 1 250 ? -42.588 -44.051 33.056  1.00 49.58  ? 223 ILE A C   1 
ATOM   5045 O  O   . ILE B 1 250 ? -43.633 -44.136 33.681  1.00 52.48  ? 223 ILE A O   1 
ATOM   5046 C  CB  . ILE B 1 250 ? -40.647 -44.881 34.502  1.00 55.00  ? 223 ILE A CB  1 
ATOM   5047 C  CG1 . ILE B 1 250 ? -41.219 -45.652 35.694  1.00 60.27  ? 223 ILE A CG1 1 
ATOM   5048 C  CG2 . ILE B 1 250 ? -40.561 -43.417 34.878  1.00 57.12  ? 223 ILE A CG2 1 
ATOM   5049 C  CD1 . ILE B 1 250 ? -41.025 -47.159 35.599  1.00 59.80  ? 223 ILE A CD1 1 
ATOM   5050 N  N   . GLU B 1 251 ? -42.336 -43.042 32.228  1.00 46.42  ? 224 GLU A N   1 
ATOM   5051 C  CA  . GLU B 1 251 ? -43.325 -42.003 31.997  1.00 49.69  ? 224 GLU A CA  1 
ATOM   5052 C  C   . GLU B 1 251 ? -44.505 -42.657 31.275  1.00 47.43  ? 224 GLU A C   1 
ATOM   5053 O  O   . GLU B 1 251 ? -45.667 -42.354 31.542  1.00 43.70  ? 224 GLU A O   1 
ATOM   5054 C  CB  . GLU B 1 251 ? -42.693 -40.810 31.233  1.00 58.66  ? 224 GLU A CB  1 
ATOM   5055 C  CG  . GLU B 1 251 ? -43.523 -40.105 30.144  1.00 67.09  ? 224 GLU A CG  1 
ATOM   5056 C  CD  . GLU B 1 251 ? -42.767 -40.000 28.791  1.00 85.17  ? 224 GLU A CD  1 
ATOM   5057 O  OE1 . GLU B 1 251 ? -42.646 -41.050 28.062  1.00 84.29  ? 224 GLU A OE1 1 
ATOM   5058 O  OE2 . GLU B 1 251 ? -42.291 -38.873 28.444  1.00 77.23  ? 224 GLU A OE2 1 
ATOM   5059 N  N   . LYS B 1 252 ? -44.202 -43.604 30.396  1.00 45.63  ? 225 LYS A N   1 
ATOM   5060 C  CA  . LYS B 1 252 ? -45.252 -44.308 29.688  1.00 46.04  ? 225 LYS A CA  1 
ATOM   5061 C  C   . LYS B 1 252 ? -45.987 -45.225 30.642  1.00 43.90  ? 225 LYS A C   1 
ATOM   5062 O  O   . LYS B 1 252 ? -47.201 -45.242 30.677  1.00 44.23  ? 225 LYS A O   1 
ATOM   5063 C  CB  . LYS B 1 252 ? -44.702 -45.093 28.512  1.00 45.30  ? 225 LYS A CB  1 
ATOM   5064 C  CG  . LYS B 1 252 ? -45.746 -45.966 27.834  1.00 47.57  ? 225 LYS A CG  1 
ATOM   5065 C  CD  . LYS B 1 252 ? -46.817 -45.123 27.191  1.00 47.26  ? 225 LYS A CD  1 
ATOM   5066 C  CE  . LYS B 1 252 ? -47.689 -45.951 26.244  1.00 50.69  ? 225 LYS A CE  1 
ATOM   5067 N  NZ  . LYS B 1 252 ? -48.874 -45.132 25.842  1.00 51.05  ? 225 LYS A NZ  1 
ATOM   5068 N  N   . PHE B 1 253 ? -45.243 -45.973 31.427  1.00 44.94  ? 226 PHE A N   1 
ATOM   5069 C  CA  . PHE B 1 253 ? -45.845 -46.799 32.435  1.00 49.40  ? 226 PHE A CA  1 
ATOM   5070 C  C   . PHE B 1 253 ? -46.798 -46.025 33.320  1.00 48.92  ? 226 PHE A C   1 
ATOM   5071 O  O   . PHE B 1 253 ? -47.830 -46.524 33.686  1.00 52.78  ? 226 PHE A O   1 
ATOM   5072 C  CB  . PHE B 1 253 ? -44.807 -47.448 33.345  1.00 52.09  ? 226 PHE A CB  1 
ATOM   5073 C  CG  . PHE B 1 253 ? -45.431 -48.158 34.503  1.00 51.44  ? 226 PHE A CG  1 
ATOM   5074 C  CD1 . PHE B 1 253 ? -46.227 -49.298 34.291  1.00 50.96  ? 226 PHE A CD1 1 
ATOM   5075 C  CD2 . PHE B 1 253 ? -45.314 -47.661 35.782  1.00 52.49  ? 226 PHE A CD2 1 
ATOM   5076 C  CE1 . PHE B 1 253 ? -46.858 -49.944 35.351  1.00 48.29  ? 226 PHE A CE1 1 
ATOM   5077 C  CE2 . PHE B 1 253 ? -45.936 -48.312 36.856  1.00 54.03  ? 226 PHE A CE2 1 
ATOM   5078 C  CZ  . PHE B 1 253 ? -46.709 -49.449 36.636  1.00 49.72  ? 226 PHE A CZ  1 
ATOM   5079 N  N   . ARG B 1 254 ? -46.451 -44.814 33.682  1.00 52.78  ? 227 ARG A N   1 
ATOM   5080 C  CA  . ARG B 1 254 ? -47.296 -44.058 34.598  1.00 57.82  ? 227 ARG A CA  1 
ATOM   5081 C  C   . ARG B 1 254 ? -48.588 -43.668 33.942  1.00 48.89  ? 227 ARG A C   1 
ATOM   5082 O  O   . ARG B 1 254 ? -49.604 -43.649 34.576  1.00 54.61  ? 227 ARG A O   1 
ATOM   5083 C  CB  . ARG B 1 254 ? -46.579 -42.813 35.087  1.00 63.77  ? 227 ARG A CB  1 
ATOM   5084 C  CG  . ARG B 1 254 ? -47.388 -41.993 36.050  1.00 67.84  ? 227 ARG A CG  1 
ATOM   5085 C  CD  . ARG B 1 254 ? -46.539 -40.901 36.693  1.00 70.34  ? 227 ARG A CD  1 
ATOM   5086 N  NE  . ARG B 1 254 ? -46.783 -40.904 38.140  1.00 71.54  ? 227 ARG A NE  1 
ATOM   5087 C  CZ  . ARG B 1 254 ? -45.894 -41.221 39.068  1.00 65.03  ? 227 ARG A CZ  1 
ATOM   5088 N  NH1 . ARG B 1 254 ? -44.646 -41.529 38.755  1.00 69.08  ? 227 ARG A NH1 1 
ATOM   5089 N  NH2 . ARG B 1 254 ? -46.255 -41.189 40.337  1.00 73.34  ? 227 ARG A NH2 1 
ATOM   5090 N  N   . GLU B 1 255 ? -48.555 -43.357 32.663  1.00 53.40  ? 228 GLU A N   1 
ATOM   5091 C  CA  . GLU B 1 255 ? -49.780 -42.967 31.942  1.00 54.95  ? 228 GLU A CA  1 
ATOM   5092 C  C   . GLU B 1 255 ? -50.765 -44.117 31.889  1.00 54.83  ? 228 GLU A C   1 
ATOM   5093 O  O   . GLU B 1 255 ? -51.958 -43.932 32.063  1.00 51.72  ? 228 GLU A O   1 
ATOM   5094 C  CB  . GLU B 1 255 ? -49.429 -42.551 30.538  1.00 53.31  ? 228 GLU A CB  1 
ATOM   5095 C  CG  . GLU B 1 255 ? -50.582 -42.251 29.625  1.00 56.45  ? 228 GLU A CG  1 
ATOM   5096 C  CD  . GLU B 1 255 ? -50.130 -42.238 28.177  1.00 69.88  ? 228 GLU A CD  1 
ATOM   5097 O  OE1 . GLU B 1 255 ? -49.054 -41.651 27.880  1.00 75.84  ? 228 GLU A OE1 1 
ATOM   5098 O  OE2 . GLU B 1 255 ? -50.831 -42.841 27.334  1.00 82.59  ? 228 GLU A OE2 1 
ATOM   5099 N  N   . GLU B 1 256 ? -50.231 -45.301 31.630  1.00 57.66  ? 229 GLU A N   1 
ATOM   5100 C  CA  . GLU B 1 256 ? -51.000 -46.523 31.569  1.00 54.28  ? 229 GLU A CA  1 
ATOM   5101 C  C   . GLU B 1 256 ? -51.464 -46.944 32.935  1.00 52.54  ? 229 GLU A C   1 
ATOM   5102 O  O   . GLU B 1 256 ? -52.494 -47.552 33.058  1.00 59.25  ? 229 GLU A O   1 
ATOM   5103 C  CB  . GLU B 1 256 ? -50.148 -47.635 30.992  1.00 56.82  ? 229 GLU A CB  1 
ATOM   5104 C  CG  . GLU B 1 256 ? -49.681 -47.342 29.602  1.00 58.91  ? 229 GLU A CG  1 
ATOM   5105 C  CD  . GLU B 1 256 ? -50.842 -47.068 28.700  1.00 65.84  ? 229 GLU A CD  1 
ATOM   5106 O  OE1 . GLU B 1 256 ? -51.831 -47.821 28.772  1.00 67.93  ? 229 GLU A OE1 1 
ATOM   5107 O  OE2 . GLU B 1 256 ? -50.780 -46.091 27.929  1.00 75.37  ? 229 GLU A OE2 1 
ATOM   5108 N  N   . ALA B 1 257 ? -50.701 -46.641 33.965  1.00 49.95  ? 230 ALA A N   1 
ATOM   5109 C  CA  . ALA B 1 257 ? -51.139 -46.960 35.305  1.00 52.26  ? 230 ALA A CA  1 
ATOM   5110 C  C   . ALA B 1 257 ? -52.293 -46.058 35.673  1.00 52.82  ? 230 ALA A C   1 
ATOM   5111 O  O   . ALA B 1 257 ? -53.190 -46.502 36.366  1.00 58.29  ? 230 ALA A O   1 
ATOM   5112 C  CB  . ALA B 1 257 ? -50.006 -46.803 36.314  1.00 54.08  ? 230 ALA A CB  1 
ATOM   5113 N  N   . GLU B 1 258 ? -52.273 -44.801 35.227  1.00 50.82  ? 231 GLU A N   1 
ATOM   5114 C  CA  . GLU B 1 258 ? -53.365 -43.876 35.542  1.00 56.53  ? 231 GLU A CA  1 
ATOM   5115 C  C   . GLU B 1 258 ? -54.668 -44.342 34.874  1.00 61.84  ? 231 GLU A C   1 
ATOM   5116 O  O   . GLU B 1 258 ? -55.705 -44.391 35.526  1.00 73.59  ? 231 GLU A O   1 
ATOM   5117 C  CB  . GLU B 1 258 ? -53.039 -42.423 35.163  1.00 54.94  ? 231 GLU A CB  1 
ATOM   5118 N  N   . GLU B 1 259 ? -54.608 -44.753 33.610  1.00 63.45  ? 232 GLU A N   1 
ATOM   5119 C  CA  . GLU B 1 259 ? -55.798 -45.236 32.890  1.00 63.77  ? 232 GLU A CA  1 
ATOM   5120 C  C   . GLU B 1 259 ? -56.463 -46.449 33.545  1.00 62.26  ? 232 GLU A C   1 
ATOM   5121 O  O   . GLU B 1 259 ? -57.621 -46.746 33.236  1.00 64.14  ? 232 GLU A O   1 
ATOM   5122 C  CB  . GLU B 1 259 ? -55.466 -45.554 31.418  1.00 68.85  ? 232 GLU A CB  1 
ATOM   5123 C  CG  . GLU B 1 259 ? -55.502 -44.319 30.507  1.00 84.73  ? 232 GLU A CG  1 
ATOM   5124 C  CD  . GLU B 1 259 ? -54.547 -44.386 29.302  1.00 99.61  ? 232 GLU A CD  1 
ATOM   5125 O  OE1 . GLU B 1 259 ? -54.312 -45.511 28.799  1.00 102.78 ? 232 GLU A OE1 1 
ATOM   5126 O  OE2 . GLU B 1 259 ? -54.041 -43.315 28.845  1.00 94.58  ? 232 GLU A OE2 1 
ATOM   5127 N  N   . ARG B 1 260 ? -55.727 -47.140 34.424  1.00 59.20  ? 233 ARG A N   1 
ATOM   5128 C  CA  . ARG B 1 260 ? -56.164 -48.385 35.075  1.00 53.37  ? 233 ARG A CA  1 
ATOM   5129 C  C   . ARG B 1 260 ? -56.352 -48.226 36.587  1.00 57.20  ? 233 ARG A C   1 
ATOM   5130 O  O   . ARG B 1 260 ? -56.492 -49.191 37.338  1.00 55.94  ? 233 ARG A O   1 
ATOM   5131 C  CB  . ARG B 1 260 ? -55.137 -49.464 34.787  1.00 48.98  ? 233 ARG A CB  1 
ATOM   5132 C  CG  . ARG B 1 260 ? -55.137 -49.897 33.338  1.00 47.52  ? 233 ARG A CG  1 
ATOM   5133 C  CD  . ARG B 1 260 ? -53.977 -50.821 33.067  1.00 51.77  ? 233 ARG A CD  1 
ATOM   5134 N  NE  . ARG B 1 260 ? -53.904 -51.240 31.660  1.00 56.05  ? 233 ARG A NE  1 
ATOM   5135 C  CZ  . ARG B 1 260 ? -53.547 -50.467 30.642  1.00 51.83  ? 233 ARG A CZ  1 
ATOM   5136 N  NH1 . ARG B 1 260 ? -53.228 -49.194 30.799  1.00 57.56  ? 233 ARG A NH1 1 
ATOM   5137 N  NH2 . ARG B 1 260 ? -53.519 -50.969 29.446  1.00 53.56  ? 233 ARG A NH2 1 
ATOM   5138 N  N   . ASP B 1 261 ? -56.343 -46.986 37.039  1.00 59.07  ? 234 ASP A N   1 
ATOM   5139 C  CA  . ASP B 1 261 ? -56.497 -46.703 38.446  1.00 61.46  ? 234 ASP A CA  1 
ATOM   5140 C  C   . ASP B 1 261 ? -55.501 -47.486 39.318  1.00 53.84  ? 234 ASP A C   1 
ATOM   5141 O  O   . ASP B 1 261 ? -55.857 -47.927 40.379  1.00 56.68  ? 234 ASP A O   1 
ATOM   5142 C  CB  . ASP B 1 261 ? -57.959 -46.932 38.877  1.00 63.85  ? 234 ASP A CB  1 
ATOM   5143 C  CG  . ASP B 1 261 ? -58.951 -46.044 38.115  1.00 74.75  ? 234 ASP A CG  1 
ATOM   5144 O  OD1 . ASP B 1 261 ? -58.629 -44.869 37.817  1.00 89.44  ? 234 ASP A OD1 1 
ATOM   5145 O  OD2 . ASP B 1 261 ? -60.065 -46.515 37.800  1.00 84.97  ? 234 ASP A OD2 1 
ATOM   5146 N  N   . ILE B 1 262 ? -54.254 -47.603 38.858  1.00 51.10  ? 235 ILE A N   1 
ATOM   5147 C  CA  . ILE B 1 262 ? -53.129 -48.194 39.613  1.00 50.62  ? 235 ILE A CA  1 
ATOM   5148 C  C   . ILE B 1 262 ? -52.315 -47.065 40.164  1.00 47.23  ? 235 ILE A C   1 
ATOM   5149 O  O   . ILE B 1 262 ? -51.841 -46.242 39.391  1.00 46.93  ? 235 ILE A O   1 
ATOM   5150 C  CB  . ILE B 1 262 ? -52.174 -48.963 38.685  1.00 53.28  ? 235 ILE A CB  1 
ATOM   5151 C  CG1 . ILE B 1 262 ? -52.803 -50.278 38.257  1.00 55.69  ? 235 ILE A CG1 1 
ATOM   5152 C  CG2 . ILE B 1 262 ? -50.813 -49.206 39.327  1.00 53.59  ? 235 ILE A CG2 1 
ATOM   5153 C  CD1 . ILE B 1 262 ? -52.341 -50.700 36.874  1.00 58.84  ? 235 ILE A CD1 1 
HETATM 5154 N  N   . CSO B 1 263 ? -52.115 -47.064 41.474  1.00 48.41  ? 236 CSO A N   1 
HETATM 5155 C  CA  . CSO B 1 263 ? -51.468 -45.973 42.178  1.00 51.90  ? 236 CSO A CA  1 
HETATM 5156 C  CB  . CSO B 1 263 ? -52.126 -45.743 43.551  1.00 57.85  ? 236 CSO A CB  1 
HETATM 5157 S  SG  . CSO B 1 263 ? -53.825 -45.246 43.421  1.00 65.15  ? 236 CSO A SG  1 
HETATM 5158 C  C   . CSO B 1 263 ? -50.025 -46.304 42.399  1.00 52.99  ? 236 CSO A C   1 
HETATM 5159 O  O   . CSO B 1 263 ? -49.680 -47.451 42.638  1.00 59.82  ? 236 CSO A O   1 
HETATM 5160 O  OD  . CSO B 1 263 ? -53.739 -43.524 43.136  1.00 77.11  ? 236 CSO A OD  1 
ATOM   5161 N  N   . ILE B 1 264 ? -49.181 -45.272 42.377  1.00 55.72  ? 237 ILE A N   1 
ATOM   5162 C  CA  . ILE B 1 264 ? -47.734 -45.392 42.532  1.00 51.38  ? 237 ILE A CA  1 
ATOM   5163 C  C   . ILE B 1 264 ? -47.260 -44.790 43.852  1.00 49.72  ? 237 ILE A C   1 
ATOM   5164 O  O   . ILE B 1 264 ? -47.460 -43.605 44.088  1.00 46.44  ? 237 ILE A O   1 
ATOM   5165 C  CB  . ILE B 1 264 ? -47.050 -44.687 41.336  1.00 49.38  ? 237 ILE A CB  1 
ATOM   5166 C  CG1 . ILE B 1 264 ? -47.540 -45.359 40.052  1.00 51.92  ? 237 ILE A CG1 1 
ATOM   5167 C  CG2 . ILE B 1 264 ? -45.519 -44.734 41.455  1.00 47.02  ? 237 ILE A CG2 1 
ATOM   5168 C  CD1 . ILE B 1 264 ? -46.913 -44.806 38.793  1.00 60.14  ? 237 ILE A CD1 1 
ATOM   5169 N  N   . ASP B 1 265 ? -46.606 -45.579 44.702  1.00 53.17  ? 238 ASP A N   1 
ATOM   5170 C  CA  . ASP B 1 265 ? -46.185 -45.051 46.023  1.00 61.82  ? 238 ASP A CA  1 
ATOM   5171 C  C   . ASP B 1 265 ? -44.891 -44.229 45.967  1.00 56.51  ? 238 ASP A C   1 
ATOM   5172 O  O   . ASP B 1 265 ? -44.717 -43.274 46.710  1.00 62.65  ? 238 ASP A O   1 
ATOM   5173 C  CB  . ASP B 1 265 ? -46.071 -46.152 47.112  1.00 63.43  ? 238 ASP A CB  1 
ATOM   5174 C  CG  . ASP B 1 265 ? -45.832 -45.557 48.527  1.00 72.35  ? 238 ASP A CG  1 
ATOM   5175 O  OD1 . ASP B 1 265 ? -46.507 -44.556 48.896  1.00 75.45  ? 238 ASP A OD1 1 
ATOM   5176 O  OD2 . ASP B 1 265 ? -44.948 -46.059 49.264  1.00 81.44  ? 238 ASP A OD2 1 
ATOM   5177 N  N   . PHE B 1 266 ? -43.984 -44.604 45.093  1.00 54.70  ? 239 PHE A N   1 
ATOM   5178 C  CA  . PHE B 1 266 ? -42.742 -43.878 44.970  1.00 54.35  ? 239 PHE A CA  1 
ATOM   5179 C  C   . PHE B 1 266 ? -42.183 -44.037 43.548  1.00 50.01  ? 239 PHE A C   1 
ATOM   5180 O  O   . PHE B 1 266 ? -42.569 -44.994 42.821  1.00 48.79  ? 239 PHE A O   1 
ATOM   5181 C  CB  . PHE B 1 266 ? -41.740 -44.371 46.039  1.00 54.32  ? 239 PHE A CB  1 
ATOM   5182 C  CG  . PHE B 1 266 ? -41.249 -45.788 45.832  1.00 53.13  ? 239 PHE A CG  1 
ATOM   5183 C  CD1 . PHE B 1 266 ? -40.388 -46.112 44.774  1.00 54.00  ? 239 PHE A CD1 1 
ATOM   5184 C  CD2 . PHE B 1 266 ? -41.596 -46.795 46.725  1.00 52.51  ? 239 PHE A CD2 1 
ATOM   5185 C  CE1 . PHE B 1 266 ? -39.903 -47.405 44.605  1.00 51.47  ? 239 PHE A CE1 1 
ATOM   5186 C  CE2 . PHE B 1 266 ? -41.129 -48.090 46.547  1.00 53.53  ? 239 PHE A CE2 1 
ATOM   5187 C  CZ  . PHE B 1 266 ? -40.277 -48.394 45.489  1.00 53.44  ? 239 PHE A CZ  1 
ATOM   5188 N  N   . SER B 1 267 ? -41.299 -43.112 43.170  1.00 40.64  ? 240 SER A N   1 
ATOM   5189 C  CA  . SER B 1 267 ? -40.545 -43.228 41.925  1.00 46.24  ? 240 SER A CA  1 
ATOM   5190 C  C   . SER B 1 267 ? -39.125 -42.620 41.998  1.00 46.00  ? 240 SER A C   1 
ATOM   5191 O  O   . SER B 1 267 ? -38.938 -41.430 42.145  1.00 42.53  ? 240 SER A O   1 
ATOM   5192 C  CB  . SER B 1 267 ? -41.336 -42.612 40.770  1.00 52.14  ? 240 SER A CB  1 
ATOM   5193 O  OG  . SER B 1 267 ? -41.516 -41.243 41.001  1.00 62.41  ? 240 SER A OG  1 
ATOM   5194 N  N   . GLU B 1 268 ? -38.111 -43.461 41.922  1.00 49.10  ? 241 GLU A N   1 
ATOM   5195 C  CA  . GLU B 1 268 ? -36.759 -43.001 42.085  1.00 48.99  ? 241 GLU A CA  1 
ATOM   5196 C  C   . GLU B 1 268 ? -35.965 -43.192 40.807  1.00 46.87  ? 241 GLU A C   1 
ATOM   5197 O  O   . GLU B 1 268 ? -36.342 -44.000 39.974  1.00 51.46  ? 241 GLU A O   1 
ATOM   5198 C  CB  . GLU B 1 268 ? -36.109 -43.732 43.255  1.00 53.39  ? 241 GLU A CB  1 
ATOM   5199 C  CG  . GLU B 1 268 ? -36.777 -43.458 44.609  1.00 58.45  ? 241 GLU A CG  1 
ATOM   5200 C  CD  . GLU B 1 268 ? -36.950 -41.971 44.940  1.00 61.94  ? 241 GLU A CD  1 
ATOM   5201 O  OE1 . GLU B 1 268 ? -38.081 -41.527 45.248  1.00 67.03  ? 241 GLU A OE1 1 
ATOM   5202 O  OE2 . GLU B 1 268 ? -35.954 -41.238 44.890  1.00 72.26  ? 241 GLU A OE2 1 
ATOM   5203 N  N   . LEU B 1 269 ? -34.894 -42.410 40.654  1.00 47.06  ? 242 LEU A N   1 
ATOM   5204 C  CA  . LEU B 1 269 ? -33.965 -42.534 39.544  1.00 51.64  ? 242 LEU A CA  1 
ATOM   5205 C  C   . LEU B 1 269 ? -32.621 -43.131 40.002  1.00 52.14  ? 242 LEU A C   1 
ATOM   5206 O  O   . LEU B 1 269 ? -32.211 -42.956 41.144  1.00 49.86  ? 242 LEU A O   1 
ATOM   5207 C  CB  . LEU B 1 269 ? -33.766 -41.174 38.890  1.00 54.99  ? 242 LEU A CB  1 
ATOM   5208 C  CG  . LEU B 1 269 ? -35.048 -40.580 38.285  1.00 59.95  ? 242 LEU A CG  1 
ATOM   5209 C  CD1 . LEU B 1 269 ? -34.791 -39.183 37.741  1.00 60.86  ? 242 LEU A CD1 1 
ATOM   5210 C  CD2 . LEU B 1 269 ? -35.641 -41.454 37.191  1.00 56.81  ? 242 LEU A CD2 1 
ATOM   5211 N  N   . ILE B 1 270 ? -31.964 -43.873 39.120  1.00 49.92  ? 243 ILE A N   1 
ATOM   5212 C  CA  . ILE B 1 270 ? -30.666 -44.484 39.431  1.00 51.90  ? 243 ILE A CA  1 
ATOM   5213 C  C   . ILE B 1 270 ? -29.757 -44.428 38.219  1.00 51.90  ? 243 ILE A C   1 
ATOM   5214 O  O   . ILE B 1 270 ? -30.199 -44.130 37.129  1.00 55.90  ? 243 ILE A O   1 
ATOM   5215 C  CB  . ILE B 1 270 ? -30.800 -45.979 39.839  1.00 53.39  ? 243 ILE A CB  1 
ATOM   5216 C  CG1 . ILE B 1 270 ? -31.546 -46.787 38.768  1.00 52.28  ? 243 ILE A CG1 1 
ATOM   5217 C  CG2 . ILE B 1 270 ? -31.537 -46.105 41.145  1.00 56.67  ? 243 ILE A CG2 1 
ATOM   5218 C  CD1 . ILE B 1 270 ? -31.583 -48.267 39.037  1.00 51.66  ? 243 ILE A CD1 1 
ATOM   5219 N  N   . SER B 1 271 ? -28.499 -44.790 38.411  1.00 54.56  ? 244 SER A N   1 
ATOM   5220 C  CA  . SER B 1 271 ? -27.484 -44.781 37.356  1.00 54.16  ? 244 SER A CA  1 
ATOM   5221 C  C   . SER B 1 271 ? -26.280 -45.663 37.731  1.00 51.94  ? 244 SER A C   1 
ATOM   5222 O  O   . SER B 1 271 ? -25.916 -45.789 38.906  1.00 50.07  ? 244 SER A O   1 
ATOM   5223 C  CB  . SER B 1 271 ? -27.005 -43.322 37.136  1.00 54.40  ? 244 SER A CB  1 
ATOM   5224 O  OG  . SER B 1 271 ? -25.710 -43.260 36.545  1.00 52.55  ? 244 SER A OG  1 
ATOM   5225 N  N   . GLN B 1 272 ? -25.606 -46.205 36.731  1.00 52.88  ? 245 GLN A N   1 
ATOM   5226 C  CA  . GLN B 1 272 ? -24.284 -46.823 36.952  1.00 51.21  ? 245 GLN A CA  1 
ATOM   5227 C  C   . GLN B 1 272 ? -23.394 -45.945 37.815  1.00 51.70  ? 245 GLN A C   1 
ATOM   5228 O  O   . GLN B 1 272 ? -22.762 -46.455 38.717  1.00 54.07  ? 245 GLN A O   1 
ATOM   5229 C  CB  . GLN B 1 272 ? -23.628 -47.070 35.621  1.00 54.26  ? 245 GLN A CB  1 
ATOM   5230 C  CG  . GLN B 1 272 ? -22.248 -47.663 35.606  1.00 56.91  ? 245 GLN A CG  1 
ATOM   5231 C  CD  . GLN B 1 272 ? -21.905 -48.159 34.201  1.00 65.83  ? 245 GLN A CD  1 
ATOM   5232 O  OE1 . GLN B 1 272 ? -22.696 -48.011 33.255  1.00 77.60  ? 245 GLN A OE1 1 
ATOM   5233 N  NE2 . GLN B 1 272 ? -20.740 -48.744 34.057  1.00 61.06  ? 245 GLN A NE2 1 
ATOM   5234 N  N   . TYR B 1 273 ? -23.398 -44.622 37.602  1.00 54.21  ? 246 TYR A N   1 
ATOM   5235 C  CA  . TYR B 1 273 ? -22.457 -43.712 38.307  1.00 53.58  ? 246 TYR A CA  1 
ATOM   5236 C  C   . TYR B 1 273 ? -22.997 -42.990 39.521  1.00 55.62  ? 246 TYR A C   1 
ATOM   5237 O  O   . TYR B 1 273 ? -22.417 -41.992 39.943  1.00 55.85  ? 246 TYR A O   1 
ATOM   5238 C  CB  . TYR B 1 273 ? -21.876 -42.698 37.325  1.00 50.55  ? 246 TYR A CB  1 
ATOM   5239 C  CG  . TYR B 1 273 ? -21.266 -43.428 36.187  1.00 50.48  ? 246 TYR A CG  1 
ATOM   5240 C  CD1 . TYR B 1 273 ? -20.003 -43.992 36.311  1.00 49.57  ? 246 TYR A CD1 1 
ATOM   5241 C  CD2 . TYR B 1 273 ? -21.998 -43.677 35.029  1.00 50.73  ? 246 TYR A CD2 1 
ATOM   5242 C  CE1 . TYR B 1 273 ? -19.444 -44.721 35.275  1.00 50.28  ? 246 TYR A CE1 1 
ATOM   5243 C  CE2 . TYR B 1 273 ? -21.469 -44.425 33.995  1.00 51.47  ? 246 TYR A CE2 1 
ATOM   5244 C  CZ  . TYR B 1 273 ? -20.190 -44.940 34.112  1.00 51.95  ? 246 TYR A CZ  1 
ATOM   5245 O  OH  . TYR B 1 273 ? -19.657 -45.663 33.066  1.00 50.82  ? 246 TYR A OH  1 
ATOM   5246 N  N   . SER B 1 274 ? -24.081 -43.492 40.103  1.00 58.99  ? 247 SER A N   1 
ATOM   5247 C  CA  . SER B 1 274 ? -24.639 -42.864 41.314  1.00 62.85  ? 247 SER A CA  1 
ATOM   5248 C  C   . SER B 1 274 ? -23.707 -43.061 42.504  1.00 62.40  ? 247 SER A C   1 
ATOM   5249 O  O   . SER B 1 274 ? -23.282 -44.172 42.770  1.00 62.05  ? 247 SER A O   1 
ATOM   5250 C  CB  . SER B 1 274 ? -26.004 -43.480 41.657  1.00 65.18  ? 247 SER A CB  1 
ATOM   5251 O  OG  . SER B 1 274 ? -26.842 -43.564 40.513  1.00 69.51  ? 247 SER A OG  1 
ATOM   5252 N  N   . ASP B 1 275 ? -23.407 -41.998 43.239  1.00 63.82  ? 248 ASP A N   1 
ATOM   5253 C  CA  . ASP B 1 275 ? -22.644 -42.146 44.481  1.00 62.22  ? 248 ASP A CA  1 
ATOM   5254 C  C   . ASP B 1 275 ? -23.416 -42.885 45.600  1.00 62.54  ? 248 ASP A C   1 
ATOM   5255 O  O   . ASP B 1 275 ? -24.608 -43.178 45.468  1.00 59.19  ? 248 ASP A O   1 
ATOM   5256 C  CB  . ASP B 1 275 ? -22.126 -40.779 44.958  1.00 67.72  ? 248 ASP A CB  1 
ATOM   5257 C  CG  . ASP B 1 275 ? -23.227 -39.838 45.426  1.00 74.42  ? 248 ASP A CG  1 
ATOM   5258 O  OD1 . ASP B 1 275 ? -24.275 -40.303 45.936  1.00 82.56  ? 248 ASP A OD1 1 
ATOM   5259 O  OD2 . ASP B 1 275 ? -23.019 -38.609 45.307  1.00 81.20  ? 248 ASP A OD2 1 
ATOM   5260 N  N   . GLU B 1 276 ? -22.728 -43.159 46.705  1.00 62.94  ? 249 GLU A N   1 
ATOM   5261 C  CA  . GLU B 1 276 ? -23.296 -43.943 47.806  1.00 65.62  ? 249 GLU A CA  1 
ATOM   5262 C  C   . GLU B 1 276 ? -24.474 -43.242 48.509  1.00 65.33  ? 249 GLU A C   1 
ATOM   5263 O  O   . GLU B 1 276 ? -25.398 -43.918 49.000  1.00 68.50  ? 249 GLU A O   1 
ATOM   5264 C  CB  . GLU B 1 276 ? -22.202 -44.345 48.824  1.00 64.23  ? 249 GLU A CB  1 
ATOM   5265 N  N   . GLU B 1 277 ? -24.456 -41.911 48.553  1.00 61.77  ? 250 GLU A N   1 
ATOM   5266 C  CA  . GLU B 1 277 ? -25.544 -41.164 49.204  1.00 68.20  ? 250 GLU A CA  1 
ATOM   5267 C  C   . GLU B 1 277 ? -26.835 -41.335 48.411  1.00 70.32  ? 250 GLU A C   1 
ATOM   5268 O  O   . GLU B 1 277 ? -27.908 -41.508 48.983  1.00 76.70  ? 250 GLU A O   1 
ATOM   5269 C  CB  . GLU B 1 277 ? -25.203 -39.670 49.368  1.00 65.94  ? 250 GLU A CB  1 
ATOM   5270 N  N   . GLU B 1 278 ? -26.711 -41.321 47.089  1.00 71.53  ? 251 GLU A N   1 
ATOM   5271 C  CA  . GLU B 1 278 ? -27.862 -41.460 46.200  1.00 68.21  ? 251 GLU A CA  1 
ATOM   5272 C  C   . GLU B 1 278 ? -28.440 -42.853 46.234  1.00 61.39  ? 251 GLU A C   1 
ATOM   5273 O  O   . GLU B 1 278 ? -29.619 -43.016 46.018  1.00 59.80  ? 251 GLU A O   1 
ATOM   5274 C  CB  . GLU B 1 278 ? -27.486 -41.089 44.755  1.00 74.00  ? 251 GLU A CB  1 
ATOM   5275 C  CG  . GLU B 1 278 ? -27.257 -39.583 44.529  1.00 77.36  ? 251 GLU A CG  1 
ATOM   5276 C  CD  . GLU B 1 278 ? -26.329 -39.259 43.351  1.00 80.87  ? 251 GLU A CD  1 
ATOM   5277 O  OE1 . GLU B 1 278 ? -25.391 -40.053 43.038  1.00 75.56  ? 251 GLU A OE1 1 
ATOM   5278 O  OE2 . GLU B 1 278 ? -26.536 -38.189 42.735  1.00 76.42  ? 251 GLU A OE2 1 
ATOM   5279 N  N   . ILE B 1 279 ? -27.614 -43.860 46.494  1.00 60.49  ? 252 ILE A N   1 
ATOM   5280 C  CA  . ILE B 1 279 ? -28.105 -45.215 46.587  1.00 57.06  ? 252 ILE A CA  1 
ATOM   5281 C  C   . ILE B 1 279 ? -28.777 -45.406 47.922  1.00 63.68  ? 252 ILE A C   1 
ATOM   5282 O  O   . ILE B 1 279 ? -29.882 -45.957 47.982  1.00 74.75  ? 252 ILE A O   1 
ATOM   5283 C  CB  . ILE B 1 279 ? -26.999 -46.267 46.464  1.00 58.89  ? 252 ILE A CB  1 
ATOM   5284 C  CG1 . ILE B 1 279 ? -26.230 -46.106 45.160  1.00 61.46  ? 252 ILE A CG1 1 
ATOM   5285 C  CG2 . ILE B 1 279 ? -27.604 -47.666 46.530  1.00 62.61  ? 252 ILE A CG2 1 
ATOM   5286 C  CD1 . ILE B 1 279 ? -27.111 -46.131 43.928  1.00 65.91  ? 252 ILE A CD1 1 
ATOM   5287 N  N   . GLN B 1 280 ? -28.118 -44.963 48.994  1.00 63.43  ? 253 GLN A N   1 
ATOM   5288 C  CA  . GLN B 1 280 ? -28.678 -45.143 50.336  1.00 67.54  ? 253 GLN A CA  1 
ATOM   5289 C  C   . GLN B 1 280 ? -30.092 -44.618 50.312  1.00 61.67  ? 253 GLN A C   1 
ATOM   5290 O  O   . GLN B 1 280 ? -31.003 -45.270 50.804  1.00 65.47  ? 253 GLN A O   1 
ATOM   5291 C  CB  . GLN B 1 280 ? -27.855 -44.443 51.443  1.00 70.07  ? 253 GLN A CB  1 
ATOM   5292 N  N   . HIS B 1 281 ? -30.273 -43.456 49.691  1.00 61.60  ? 254 HIS A N   1 
ATOM   5293 C  CA  . HIS B 1 281 ? -31.573 -42.818 49.639  1.00 56.69  ? 254 HIS A CA  1 
ATOM   5294 C  C   . HIS B 1 281 ? -32.621 -43.693 48.938  1.00 58.66  ? 254 HIS A C   1 
ATOM   5295 O  O   . HIS B 1 281 ? -33.750 -43.810 49.423  1.00 59.63  ? 254 HIS A O   1 
ATOM   5296 C  CB  . HIS B 1 281 ? -31.473 -41.470 48.955  1.00 55.80  ? 254 HIS A CB  1 
ATOM   5297 C  CG  . HIS B 1 281 ? -32.784 -40.767 48.862  1.00 64.52  ? 254 HIS A CG  1 
ATOM   5298 N  ND1 . HIS B 1 281 ? -33.586 -40.835 47.737  1.00 65.07  ? 254 HIS A ND1 1 
ATOM   5299 C  CD2 . HIS B 1 281 ? -33.466 -40.033 49.774  1.00 63.86  ? 254 HIS A CD2 1 
ATOM   5300 C  CE1 . HIS B 1 281 ? -34.694 -40.145 47.952  1.00 72.64  ? 254 HIS A CE1 1 
ATOM   5301 N  NE2 . HIS B 1 281 ? -34.648 -39.653 49.181  1.00 74.49  ? 254 HIS A NE2 1 
ATOM   5302 N  N   . VAL B 1 282 ? -32.251 -44.332 47.830  1.00 53.71  ? 255 VAL A N   1 
ATOM   5303 C  CA  . VAL B 1 282 ? -33.213 -45.153 47.109  1.00 57.47  ? 255 VAL A CA  1 
ATOM   5304 C  C   . VAL B 1 282 ? -33.554 -46.368 47.943  1.00 61.97  ? 255 VAL A C   1 
ATOM   5305 O  O   . VAL B 1 282 ? -34.744 -46.688 48.113  1.00 64.11  ? 255 VAL A O   1 
ATOM   5306 C  CB  . VAL B 1 282 ? -32.701 -45.583 45.723  1.00 58.25  ? 255 VAL A CB  1 
ATOM   5307 C  CG1 . VAL B 1 282 ? -33.655 -46.572 45.073  1.00 59.54  ? 255 VAL A CG1 1 
ATOM   5308 C  CG2 . VAL B 1 282 ? -32.584 -44.374 44.828  1.00 55.46  ? 255 VAL A CG2 1 
ATOM   5309 N  N   . VAL B 1 283 ? -32.518 -47.026 48.477  1.00 61.37  ? 256 VAL A N   1 
ATOM   5310 C  CA  . VAL B 1 283 ? -32.713 -48.157 49.400  1.00 58.54  ? 256 VAL A CA  1 
ATOM   5311 C  C   . VAL B 1 283 ? -33.579 -47.756 50.597  1.00 56.35  ? 256 VAL A C   1 
ATOM   5312 O  O   . VAL B 1 283 ? -34.435 -48.524 51.035  1.00 56.87  ? 256 VAL A O   1 
ATOM   5313 C  CB  . VAL B 1 283 ? -31.387 -48.740 49.900  1.00 59.49  ? 256 VAL A CB  1 
ATOM   5314 C  CG1 . VAL B 1 283 ? -31.622 -49.785 50.973  1.00 60.23  ? 256 VAL A CG1 1 
ATOM   5315 C  CG2 . VAL B 1 283 ? -30.636 -49.368 48.753  1.00 63.01  ? 256 VAL A CG2 1 
ATOM   5316 N  N   . GLU B 1 284 ? -33.402 -46.552 51.114  1.00 56.89  ? 257 GLU A N   1 
ATOM   5317 C  CA  . GLU B 1 284 ? -34.291 -46.112 52.192  1.00 61.85  ? 257 GLU A CA  1 
ATOM   5318 C  C   . GLU B 1 284 ? -35.736 -45.995 51.732  1.00 63.95  ? 257 GLU A C   1 
ATOM   5319 O  O   . GLU B 1 284 ? -36.612 -46.583 52.362  1.00 58.82  ? 257 GLU A O   1 
ATOM   5320 C  CB  . GLU B 1 284 ? -33.801 -44.832 52.837  1.00 63.26  ? 257 GLU A CB  1 
ATOM   5321 C  CG  . GLU B 1 284 ? -32.630 -45.133 53.763  1.00 70.59  ? 257 GLU A CG  1 
ATOM   5322 C  CD  . GLU B 1 284 ? -32.116 -43.915 54.487  1.00 78.17  ? 257 GLU A CD  1 
ATOM   5323 O  OE1 . GLU B 1 284 ? -32.853 -42.909 54.525  1.00 84.79  ? 257 GLU A OE1 1 
ATOM   5324 O  OE2 . GLU B 1 284 ? -30.980 -43.969 55.015  1.00 82.15  ? 257 GLU A OE2 1 
ATOM   5325 N  N   . VAL B 1 285 ? -35.973 -45.309 50.607  1.00 60.26  ? 258 VAL A N   1 
ATOM   5326 C  CA  . VAL B 1 285 ? -37.326 -45.165 50.076  1.00 54.46  ? 258 VAL A CA  1 
ATOM   5327 C  C   . VAL B 1 285 ? -37.973 -46.534 49.934  1.00 57.30  ? 258 VAL A C   1 
ATOM   5328 O  O   . VAL B 1 285 ? -39.129 -46.725 50.316  1.00 61.10  ? 258 VAL A O   1 
ATOM   5329 C  CB  . VAL B 1 285 ? -37.357 -44.448 48.716  1.00 53.08  ? 258 VAL A CB  1 
ATOM   5330 C  CG1 . VAL B 1 285 ? -38.742 -44.525 48.089  1.00 57.37  ? 258 VAL A CG1 1 
ATOM   5331 C  CG2 . VAL B 1 285 ? -36.963 -42.985 48.853  1.00 52.82  ? 258 VAL A CG2 1 
ATOM   5332 N  N   . ILE B 1 286 ? -37.226 -47.495 49.412  1.00 57.95  ? 259 ILE A N   1 
ATOM   5333 C  CA  . ILE B 1 286 ? -37.763 -48.853 49.258  1.00 60.70  ? 259 ILE A CA  1 
ATOM   5334 C  C   . ILE B 1 286 ? -38.108 -49.514 50.590  1.00 63.24  ? 259 ILE A C   1 
ATOM   5335 O  O   . ILE B 1 286 ? -39.209 -50.056 50.747  1.00 63.58  ? 259 ILE A O   1 
ATOM   5336 C  CB  . ILE B 1 286 ? -36.789 -49.786 48.530  1.00 57.01  ? 259 ILE A CB  1 
ATOM   5337 C  CG1 . ILE B 1 286 ? -36.621 -49.360 47.074  1.00 53.93  ? 259 ILE A CG1 1 
ATOM   5338 C  CG2 . ILE B 1 286 ? -37.301 -51.219 48.590  1.00 57.05  ? 259 ILE A CG2 1 
ATOM   5339 C  CD1 . ILE B 1 286 ? -35.562 -50.150 46.332  1.00 53.55  ? 259 ILE A CD1 1 
ATOM   5340 N  N   . GLN B 1 287 ? -37.140 -49.498 51.511  1.00 64.58  ? 260 GLN A N   1 
ATOM   5341 C  CA  . GLN B 1 287 ? -37.328 -50.000 52.867  1.00 63.73  ? 260 GLN A CA  1 
ATOM   5342 C  C   . GLN B 1 287 ? -38.535 -49.360 53.560  1.00 65.66  ? 260 GLN A C   1 
ATOM   5343 O  O   . GLN B 1 287 ? -39.401 -50.085 54.044  1.00 66.14  ? 260 GLN A O   1 
ATOM   5344 C  CB  . GLN B 1 287 ? -36.091 -49.749 53.708  1.00 65.75  ? 260 GLN A CB  1 
ATOM   5345 C  CG  . GLN B 1 287 ? -34.963 -50.703 53.440  1.00 69.64  ? 260 GLN A CG  1 
ATOM   5346 C  CD  . GLN B 1 287 ? -33.813 -50.528 54.419  1.00 76.67  ? 260 GLN A CD  1 
ATOM   5347 O  OE1 . GLN B 1 287 ? -33.426 -49.405 54.759  1.00 69.15  ? 260 GLN A OE1 1 
ATOM   5348 N  NE2 . GLN B 1 287 ? -33.241 -51.651 54.863  1.00 87.68  ? 260 GLN A NE2 1 
ATOM   5349 N  N   . ASN B 1 288 ? -38.612 -48.020 53.578  1.00 61.28  ? 261 ASN A N   1 
ATOM   5350 C  CA  . ASN B 1 288 ? -39.773 -47.303 54.172  1.00 62.27  ? 261 ASN A CA  1 
ATOM   5351 C  C   . ASN B 1 288 ? -41.133 -47.459 53.434  1.00 62.52  ? 261 ASN A C   1 
ATOM   5352 O  O   . ASN B 1 288 ? -42.107 -46.810 53.811  1.00 72.56  ? 261 ASN A O   1 
ATOM   5353 C  CB  . ASN B 1 288 ? -39.490 -45.798 54.394  1.00 57.28  ? 261 ASN A CB  1 
ATOM   5354 C  CG  . ASN B 1 288 ? -38.226 -45.546 55.194  1.00 68.83  ? 261 ASN A CG  1 
ATOM   5355 O  OD1 . ASN B 1 288 ? -37.532 -46.485 55.594  1.00 72.32  ? 261 ASN A OD1 1 
ATOM   5356 N  ND2 . ASN B 1 288 ? -37.904 -44.274 55.421  1.00 78.08  ? 261 ASN A ND2 1 
ATOM   5357 N  N   . SER B 1 289 ? -41.225 -48.319 52.421  1.00 59.56  ? 262 SER A N   1 
ATOM   5358 C  CA  . SER B 1 289 ? -42.471 -48.451 51.649  1.00 55.83  ? 262 SER A CA  1 
ATOM   5359 C  C   . SER B 1 289 ? -43.262 -49.753 51.938  1.00 58.43  ? 262 SER A C   1 
ATOM   5360 O  O   . SER B 1 289 ? -42.701 -50.819 52.198  1.00 63.09  ? 262 SER A O   1 
ATOM   5361 C  CB  . SER B 1 289 ? -42.155 -48.333 50.164  1.00 50.26  ? 262 SER A CB  1 
ATOM   5362 O  OG  . SER B 1 289 ? -43.316 -48.223 49.356  1.00 46.54  ? 262 SER A OG  1 
ATOM   5363 N  N   . THR B 1 290 ? -44.577 -49.638 51.888  1.00 55.23  ? 263 THR A N   1 
ATOM   5364 C  CA  . THR B 1 290 ? -45.446 -50.770 52.022  1.00 59.38  ? 263 THR A CA  1 
ATOM   5365 C  C   . THR B 1 290 ? -45.500 -51.567 50.694  1.00 62.40  ? 263 THR A C   1 
ATOM   5366 O  O   . THR B 1 290 ? -45.991 -52.714 50.660  1.00 56.86  ? 263 THR A O   1 
ATOM   5367 C  CB  . THR B 1 290 ? -46.865 -50.298 52.394  1.00 63.23  ? 263 THR A CB  1 
ATOM   5368 O  OG1 . THR B 1 290 ? -47.374 -49.442 51.361  1.00 52.87  ? 263 THR A OG1 1 
ATOM   5369 C  CG2 . THR B 1 290 ? -46.852 -49.551 53.748  1.00 67.72  ? 263 THR A CG2 1 
ATOM   5370 N  N   . ALA B 1 291 ? -45.006 -50.962 49.611  1.00 59.49  ? 264 ALA A N   1 
ATOM   5371 C  CA  . ALA B 1 291 ? -45.045 -51.583 48.281  1.00 62.27  ? 264 ALA A CA  1 
ATOM   5372 C  C   . ALA B 1 291 ? -44.215 -52.871 48.166  1.00 60.69  ? 264 ALA A C   1 
ATOM   5373 O  O   . ALA B 1 291 ? -43.030 -52.874 48.475  1.00 61.33  ? 264 ALA A O   1 
ATOM   5374 C  CB  . ALA B 1 291 ? -44.590 -50.586 47.230  1.00 59.66  ? 264 ALA A CB  1 
ATOM   5375 N  N   . LYS B 1 292 ? -44.864 -53.954 47.736  1.00 57.43  ? 265 LYS A N   1 
ATOM   5376 C  CA  . LYS B 1 292 ? -44.188 -55.218 47.448  1.00 57.61  ? 265 LYS A CA  1 
ATOM   5377 C  C   . LYS B 1 292 ? -43.807 -55.263 45.963  1.00 57.50  ? 265 LYS A C   1 
ATOM   5378 O  O   . LYS B 1 292 ? -42.805 -55.904 45.595  1.00 59.02  ? 265 LYS A O   1 
ATOM   5379 C  CB  . LYS B 1 292 ? -45.080 -56.433 47.809  1.00 52.38  ? 265 LYS A CB  1 
ATOM   5380 N  N   . VAL B 1 293 ? -44.611 -54.615 45.112  1.00 51.40  ? 266 VAL A N   1 
ATOM   5381 C  CA  . VAL B 1 293 ? -44.391 -54.655 43.675  1.00 50.75  ? 266 VAL A CA  1 
ATOM   5382 C  C   . VAL B 1 293 ? -43.556 -53.458 43.192  1.00 52.32  ? 266 VAL A C   1 
ATOM   5383 O  O   . VAL B 1 293 ? -43.956 -52.297 43.332  1.00 47.22  ? 266 VAL A O   1 
ATOM   5384 C  CB  . VAL B 1 293 ? -45.714 -54.699 42.900  1.00 50.33  ? 266 VAL A CB  1 
ATOM   5385 C  CG1 . VAL B 1 293 ? -45.462 -54.507 41.416  1.00 49.05  ? 266 VAL A CG1 1 
ATOM   5386 C  CG2 . VAL B 1 293 ? -46.408 -56.041 43.112  1.00 53.85  ? 266 VAL A CG2 1 
ATOM   5387 N  N   . ILE B 1 294 ? -42.402 -53.748 42.595  1.00 54.49  ? 267 ILE A N   1 
ATOM   5388 C  CA  . ILE B 1 294 ? -41.523 -52.689 42.118  1.00 52.86  ? 267 ILE A CA  1 
ATOM   5389 C  C   . ILE B 1 294 ? -41.222 -52.809 40.634  1.00 47.32  ? 267 ILE A C   1 
ATOM   5390 O  O   . ILE B 1 294 ? -40.636 -53.772 40.188  1.00 45.96  ? 267 ILE A O   1 
ATOM   5391 C  CB  . ILE B 1 294 ? -40.234 -52.631 42.946  1.00 54.53  ? 267 ILE A CB  1 
ATOM   5392 C  CG1 . ILE B 1 294 ? -40.603 -52.659 44.449  1.00 54.22  ? 267 ILE A CG1 1 
ATOM   5393 C  CG2 . ILE B 1 294 ? -39.443 -51.371 42.575  1.00 52.46  ? 267 ILE A CG2 1 
ATOM   5394 C  CD1 . ILE B 1 294 ? -39.481 -52.283 45.387  1.00 55.73  ? 267 ILE A CD1 1 
ATOM   5395 N  N   . VAL B 1 295 ? -41.646 -51.803 39.885  1.00 45.73  ? 268 VAL A N   1 
ATOM   5396 C  CA  . VAL B 1 295 ? -41.388 -51.728 38.459  1.00 48.17  ? 268 VAL A CA  1 
ATOM   5397 C  C   . VAL B 1 295 ? -40.080 -51.021 38.181  1.00 49.91  ? 268 VAL A C   1 
ATOM   5398 O  O   . VAL B 1 295 ? -39.920 -49.846 38.531  1.00 47.31  ? 268 VAL A O   1 
ATOM   5399 C  CB  . VAL B 1 295 ? -42.477 -50.921 37.750  1.00 45.54  ? 268 VAL A CB  1 
ATOM   5400 C  CG1 . VAL B 1 295 ? -42.237 -50.906 36.253  1.00 42.64  ? 268 VAL A CG1 1 
ATOM   5401 C  CG2 . VAL B 1 295 ? -43.811 -51.554 38.049  1.00 48.42  ? 268 VAL A CG2 1 
ATOM   5402 N  N   . VAL B 1 296 ? -39.178 -51.728 37.504  1.00 52.19  ? 269 VAL A N   1 
ATOM   5403 C  CA  . VAL B 1 296 ? -37.829 -51.245 37.227  1.00 50.44  ? 269 VAL A CA  1 
ATOM   5404 C  C   . VAL B 1 296 ? -37.461 -51.205 35.744  1.00 49.50  ? 269 VAL A C   1 
ATOM   5405 O  O   . VAL B 1 296 ? -37.267 -52.234 35.076  1.00 44.31  ? 269 VAL A O   1 
ATOM   5406 C  CB  . VAL B 1 296 ? -36.826 -52.128 37.952  1.00 52.78  ? 269 VAL A CB  1 
ATOM   5407 C  CG1 . VAL B 1 296 ? -35.420 -51.587 37.749  1.00 54.88  ? 269 VAL A CG1 1 
ATOM   5408 C  CG2 . VAL B 1 296 ? -37.201 -52.203 39.442  1.00 52.42  ? 269 VAL A CG2 1 
ATOM   5409 N  N   . PHE B 1 297 ? -37.316 -49.995 35.245  1.00 52.27  ? 270 PHE A N   1 
ATOM   5410 C  CA  . PHE B 1 297 ? -36.980 -49.789 33.836  1.00 54.00  ? 270 PHE A CA  1 
ATOM   5411 C  C   . PHE B 1 297 ? -35.539 -49.355 33.710  1.00 52.61  ? 270 PHE A C   1 
ATOM   5412 O  O   . PHE B 1 297 ? -35.226 -48.177 33.872  1.00 47.49  ? 270 PHE A O   1 
ATOM   5413 C  CB  . PHE B 1 297 ? -37.880 -48.720 33.251  1.00 56.29  ? 270 PHE A CB  1 
ATOM   5414 C  CG  . PHE B 1 297 ? -38.524 -49.130 31.994  1.00 58.65  ? 270 PHE A CG  1 
ATOM   5415 C  CD1 . PHE B 1 297 ? -37.804 -49.129 30.807  1.00 59.27  ? 270 PHE A CD1 1 
ATOM   5416 C  CD2 . PHE B 1 297 ? -39.844 -49.561 31.990  1.00 56.20  ? 270 PHE A CD2 1 
ATOM   5417 C  CE1 . PHE B 1 297 ? -38.405 -49.520 29.620  1.00 53.82  ? 270 PHE A CE1 1 
ATOM   5418 C  CE2 . PHE B 1 297 ? -40.435 -49.971 30.810  1.00 56.28  ? 270 PHE A CE2 1 
ATOM   5419 C  CZ  . PHE B 1 297 ? -39.717 -49.936 29.621  1.00 52.30  ? 270 PHE A CZ  1 
ATOM   5420 N  N   . SER B 1 298 ? -34.649 -50.307 33.448  1.00 55.00  ? 271 SER A N   1 
ATOM   5421 C  CA  . SER B 1 298 ? -33.227 -49.999 33.440  1.00 51.75  ? 271 SER A CA  1 
ATOM   5422 C  C   . SER B 1 298 ? -32.427 -51.041 32.741  1.00 49.48  ? 271 SER A C   1 
ATOM   5423 O  O   . SER B 1 298 ? -32.888 -52.133 32.532  1.00 51.30  ? 271 SER A O   1 
ATOM   5424 C  CB  . SER B 1 298 ? -32.700 -49.888 34.879  1.00 53.40  ? 271 SER A CB  1 
ATOM   5425 O  OG  . SER B 1 298 ? -31.278 -49.716 34.905  1.00 52.70  ? 271 SER A OG  1 
ATOM   5426 N  N   . SER B 1 299 ? -31.206 -50.672 32.388  1.00 55.28  ? 272 SER A N   1 
ATOM   5427 C  CA  . SER B 1 299 ? -30.181 -51.618 31.961  1.00 51.70  ? 272 SER A CA  1 
ATOM   5428 C  C   . SER B 1 299 ? -29.551 -52.207 33.209  1.00 50.68  ? 272 SER A C   1 
ATOM   5429 O  O   . SER B 1 299 ? -29.643 -51.636 34.310  1.00 47.70  ? 272 SER A O   1 
ATOM   5430 C  CB  . SER B 1 299 ? -29.092 -50.917 31.134  1.00 48.55  ? 272 SER A CB  1 
ATOM   5431 O  OG  . SER B 1 299 ? -28.154 -50.228 31.976  1.00 48.26  ? 272 SER A OG  1 
ATOM   5432 N  N   . GLY B 1 300 ? -28.901 -53.351 33.023  1.00 51.43  ? 273 GLY A N   1 
ATOM   5433 C  CA  . GLY B 1 300 ? -28.222 -54.047 34.110  1.00 46.67  ? 273 GLY A CA  1 
ATOM   5434 C  C   . GLY B 1 300 ? -27.204 -53.132 34.738  1.00 47.71  ? 273 GLY A C   1 
ATOM   5435 O  O   . GLY B 1 300 ? -27.207 -52.939 35.957  1.00 46.33  ? 273 GLY A O   1 
ATOM   5436 N  N   . PRO B 1 301 ? -26.329 -52.548 33.908  1.00 48.95  ? 274 PRO A N   1 
ATOM   5437 C  CA  . PRO B 1 301 ? -25.233 -51.743 34.462  1.00 49.26  ? 274 PRO A CA  1 
ATOM   5438 C  C   . PRO B 1 301 ? -25.662 -50.551 35.307  1.00 55.38  ? 274 PRO A C   1 
ATOM   5439 O  O   . PRO B 1 301 ? -24.978 -50.236 36.265  1.00 63.75  ? 274 PRO A O   1 
ATOM   5440 C  CB  . PRO B 1 301 ? -24.478 -51.293 33.230  1.00 47.59  ? 274 PRO A CB  1 
ATOM   5441 C  CG  . PRO B 1 301 ? -24.719 -52.395 32.245  1.00 50.18  ? 274 PRO A CG  1 
ATOM   5442 C  CD  . PRO B 1 301 ? -26.085 -52.937 32.507  1.00 46.33  ? 274 PRO A CD  1 
ATOM   5443 N  N   . ASP B 1 302 ? -26.781 -49.908 34.976  1.00 59.46  ? 275 ASP A N   1 
ATOM   5444 C  CA  . ASP B 1 302 ? -27.301 -48.792 35.788  1.00 59.05  ? 275 ASP A CA  1 
ATOM   5445 C  C   . ASP B 1 302 ? -28.023 -49.270 37.044  1.00 56.52  ? 275 ASP A C   1 
ATOM   5446 O  O   . ASP B 1 302 ? -28.155 -48.538 38.007  1.00 53.21  ? 275 ASP A O   1 
ATOM   5447 C  CB  . ASP B 1 302 ? -28.275 -47.938 34.966  1.00 61.70  ? 275 ASP A CB  1 
ATOM   5448 C  CG  . ASP B 1 302 ? -27.601 -47.193 33.821  1.00 62.86  ? 275 ASP A CG  1 
ATOM   5449 O  OD1 . ASP B 1 302 ? -26.562 -46.527 34.059  1.00 67.37  ? 275 ASP A OD1 1 
ATOM   5450 O  OD2 . ASP B 1 302 ? -28.141 -47.250 32.686  1.00 65.08  ? 275 ASP A OD2 1 
ATOM   5451 N  N   . LEU B 1 303 ? -28.522 -50.495 37.001  1.00 58.31  ? 276 LEU A N   1 
ATOM   5452 C  CA  . LEU B 1 303 ? -29.230 -51.099 38.117  1.00 58.73  ? 276 LEU A CA  1 
ATOM   5453 C  C   . LEU B 1 303 ? -28.291 -51.729 39.157  1.00 58.82  ? 276 LEU A C   1 
ATOM   5454 O  O   . LEU B 1 303 ? -28.618 -51.790 40.338  1.00 56.21  ? 276 LEU A O   1 
ATOM   5455 C  CB  . LEU B 1 303 ? -30.173 -52.192 37.565  1.00 59.96  ? 276 LEU A CB  1 
ATOM   5456 C  CG  . LEU B 1 303 ? -31.156 -52.883 38.524  1.00 55.85  ? 276 LEU A CG  1 
ATOM   5457 C  CD1 . LEU B 1 303 ? -32.008 -51.829 39.209  1.00 62.51  ? 276 LEU A CD1 1 
ATOM   5458 C  CD2 . LEU B 1 303 ? -32.038 -53.870 37.786  1.00 52.69  ? 276 LEU A CD2 1 
ATOM   5459 N  N   . GLU B 1 304 ? -27.133 -52.211 38.713  1.00 63.39  ? 277 GLU A N   1 
ATOM   5460 C  CA  . GLU B 1 304 ? -26.355 -53.160 39.504  1.00 68.30  ? 277 GLU A CA  1 
ATOM   5461 C  C   . GLU B 1 304 ? -25.928 -52.581 40.842  1.00 65.53  ? 277 GLU A C   1 
ATOM   5462 O  O   . GLU B 1 304 ? -26.003 -53.263 41.860  1.00 70.67  ? 277 GLU A O   1 
ATOM   5463 C  CB  . GLU B 1 304 ? -25.157 -53.690 38.711  1.00 72.33  ? 277 GLU A CB  1 
ATOM   5464 C  CG  . GLU B 1 304 ? -24.089 -54.328 39.571  1.00 81.87  ? 277 GLU A CG  1 
ATOM   5465 C  CD  . GLU B 1 304 ? -22.932 -54.876 38.762  1.00 96.28  ? 277 GLU A CD  1 
ATOM   5466 O  OE1 . GLU B 1 304 ? -22.287 -54.085 38.025  1.00 97.48  ? 277 GLU A OE1 1 
ATOM   5467 O  OE2 . GLU B 1 304 ? -22.655 -56.097 38.886  1.00 101.63 ? 277 GLU A OE2 1 
ATOM   5468 N  N   . PRO B 1 305 ? -25.492 -51.321 40.850  1.00 61.26  ? 278 PRO A N   1 
ATOM   5469 C  CA  . PRO B 1 305 ? -25.157 -50.715 42.136  1.00 63.49  ? 278 PRO A CA  1 
ATOM   5470 C  C   . PRO B 1 305 ? -26.313 -50.758 43.125  1.00 62.34  ? 278 PRO A C   1 
ATOM   5471 O  O   . PRO B 1 305 ? -26.093 -51.058 44.291  1.00 67.06  ? 278 PRO A O   1 
ATOM   5472 C  CB  . PRO B 1 305 ? -24.794 -49.260 41.768  1.00 62.82  ? 278 PRO A CB  1 
ATOM   5473 C  CG  . PRO B 1 305 ? -24.318 -49.344 40.354  1.00 59.99  ? 278 PRO A CG  1 
ATOM   5474 C  CD  . PRO B 1 305 ? -25.107 -50.462 39.711  1.00 62.10  ? 278 PRO A CD  1 
ATOM   5475 N  N   . LEU B 1 306 ? -27.528 -50.469 42.668  1.00 59.61  ? 279 LEU A N   1 
ATOM   5476 C  CA  . LEU B 1 306 ? -28.694 -50.567 43.550  1.00 62.04  ? 279 LEU A CA  1 
ATOM   5477 C  C   . LEU B 1 306 ? -28.886 -52.013 44.101  1.00 59.86  ? 279 LEU A C   1 
ATOM   5478 O  O   . LEU B 1 306 ? -28.961 -52.222 45.325  1.00 52.68  ? 279 LEU A O   1 
ATOM   5479 C  CB  . LEU B 1 306 ? -29.948 -50.057 42.840  1.00 57.77  ? 279 LEU A CB  1 
ATOM   5480 C  CG  . LEU B 1 306 ? -31.248 -50.115 43.640  1.00 61.38  ? 279 LEU A CG  1 
ATOM   5481 C  CD1 . LEU B 1 306 ? -31.275 -49.174 44.839  1.00 61.21  ? 279 LEU A CD1 1 
ATOM   5482 C  CD2 . LEU B 1 306 ? -32.397 -49.821 42.699  1.00 64.95  ? 279 LEU A CD2 1 
ATOM   5483 N  N   . ILE B 1 307 ? -28.923 -53.002 43.214  1.00 52.34  ? 280 ILE A N   1 
ATOM   5484 C  CA  . ILE B 1 307 ? -29.110 -54.360 43.670  1.00 59.44  ? 280 ILE A CA  1 
ATOM   5485 C  C   . ILE B 1 307 ? -28.055 -54.780 44.738  1.00 64.61  ? 280 ILE A C   1 
ATOM   5486 O  O   . ILE B 1 307 ? -28.396 -55.380 45.762  1.00 74.54  ? 280 ILE A O   1 
ATOM   5487 C  CB  . ILE B 1 307 ? -29.170 -55.334 42.484  1.00 60.14  ? 280 ILE A CB  1 
ATOM   5488 C  CG1 . ILE B 1 307 ? -30.452 -55.116 41.671  1.00 67.77  ? 280 ILE A CG1 1 
ATOM   5489 C  CG2 . ILE B 1 307 ? -29.140 -56.781 42.941  1.00 58.42  ? 280 ILE A CG2 1 
ATOM   5490 C  CD1 . ILE B 1 307 ? -31.754 -55.498 42.377  1.00 71.53  ? 280 ILE A CD1 1 
ATOM   5491 N  N   . LYS B 1 308 ? -26.795 -54.440 44.530  1.00 59.06  ? 281 LYS A N   1 
ATOM   5492 C  CA  . LYS B 1 308 ? -25.769 -54.797 45.496  1.00 55.71  ? 281 LYS A CA  1 
ATOM   5493 C  C   . LYS B 1 308 ? -26.134 -54.319 46.869  1.00 53.36  ? 281 LYS A C   1 
ATOM   5494 O  O   . LYS B 1 308 ? -26.047 -55.074 47.828  1.00 58.28  ? 281 LYS A O   1 
ATOM   5495 C  CB  . LYS B 1 308 ? -24.386 -54.241 45.106  1.00 52.79  ? 281 LYS A CB  1 
ATOM   5496 C  CG  . LYS B 1 308 ? -23.748 -55.079 44.011  1.00 53.03  ? 281 LYS A CG  1 
ATOM   5497 C  CD  . LYS B 1 308 ? -22.468 -54.454 43.552  1.00 56.94  ? 281 LYS A CD  1 
ATOM   5498 C  CE  . LYS B 1 308 ? -21.776 -55.370 42.554  1.00 63.94  ? 281 LYS A CE  1 
ATOM   5499 N  NZ  . LYS B 1 308 ? -20.509 -54.794 41.988  1.00 69.34  ? 281 LYS A NZ  1 
ATOM   5500 N  N   . GLU B 1 309 ? -26.557 -53.072 46.978  1.00 54.41  ? 282 GLU A N   1 
ATOM   5501 C  CA  . GLU B 1 309 ? -26.831 -52.513 48.295  1.00 55.19  ? 282 GLU A CA  1 
ATOM   5502 C  C   . GLU B 1 309 ? -28.099 -53.116 48.887  1.00 55.19  ? 282 GLU A C   1 
ATOM   5503 O  O   . GLU B 1 309 ? -28.236 -53.155 50.093  1.00 59.03  ? 282 GLU A O   1 
ATOM   5504 C  CB  . GLU B 1 309 ? -26.930 -51.004 48.231  1.00 56.22  ? 282 GLU A CB  1 
ATOM   5505 C  CG  . GLU B 1 309 ? -27.118 -50.318 49.577  1.00 66.09  ? 282 GLU A CG  1 
ATOM   5506 C  CD  . GLU B 1 309 ? -25.953 -50.480 50.543  1.00 72.71  ? 282 GLU A CD  1 
ATOM   5507 O  OE1 . GLU B 1 309 ? -26.147 -50.178 51.748  1.00 75.08  ? 282 GLU A OE1 1 
ATOM   5508 O  OE2 . GLU B 1 309 ? -24.850 -50.885 50.110  1.00 79.60  ? 282 GLU A OE2 1 
ATOM   5509 N  N   . ILE B 1 310 ? -28.997 -53.609 48.038  1.00 54.99  ? 283 ILE A N   1 
ATOM   5510 C  CA  . ILE B 1 310 ? -30.273 -54.152 48.481  1.00 58.62  ? 283 ILE A CA  1 
ATOM   5511 C  C   . ILE B 1 310 ? -30.067 -55.560 49.029  1.00 60.25  ? 283 ILE A C   1 
ATOM   5512 O  O   . ILE B 1 310 ? -30.639 -55.952 50.054  1.00 55.66  ? 283 ILE A O   1 
ATOM   5513 C  CB  . ILE B 1 310 ? -31.299 -54.156 47.322  1.00 60.48  ? 283 ILE A CB  1 
ATOM   5514 C  CG1 . ILE B 1 310 ? -31.842 -52.731 47.133  1.00 69.59  ? 283 ILE A CG1 1 
ATOM   5515 C  CG2 . ILE B 1 310 ? -32.472 -55.096 47.607  1.00 58.22  ? 283 ILE A CG2 1 
ATOM   5516 C  CD1 . ILE B 1 310 ? -32.724 -52.535 45.906  1.00 72.35  ? 283 ILE A CD1 1 
ATOM   5517 N  N   . VAL B 1 311 ? -29.278 -56.323 48.294  1.00 58.81  ? 284 VAL A N   1 
ATOM   5518 C  CA  . VAL B 1 311 ? -28.808 -57.595 48.740  1.00 56.29  ? 284 VAL A CA  1 
ATOM   5519 C  C   . VAL B 1 311 ? -28.028 -57.395 50.037  1.00 62.63  ? 284 VAL A C   1 
ATOM   5520 O  O   . VAL B 1 311 ? -28.212 -58.142 51.008  1.00 62.62  ? 284 VAL A O   1 
ATOM   5521 C  CB  . VAL B 1 311 ? -27.924 -58.199 47.660  1.00 58.10  ? 284 VAL A CB  1 
ATOM   5522 C  CG1 . VAL B 1 311 ? -27.119 -59.382 48.193  1.00 56.29  ? 284 VAL A CG1 1 
ATOM   5523 C  CG2 . VAL B 1 311 ? -28.807 -58.601 46.488  1.00 59.78  ? 284 VAL A CG2 1 
ATOM   5524 N  N   . ARG B 1 312 ? -27.179 -56.372 50.080  1.00 61.95  ? 285 ARG A N   1 
ATOM   5525 C  CA  . ARG B 1 312 ? -26.432 -56.116 51.304  1.00 65.97  ? 285 ARG A CA  1 
ATOM   5526 C  C   . ARG B 1 312 ? -27.395 -56.022 52.502  1.00 67.69  ? 285 ARG A C   1 
ATOM   5527 O  O   . ARG B 1 312 ? -27.167 -56.664 53.515  1.00 68.17  ? 285 ARG A O   1 
ATOM   5528 C  CB  . ARG B 1 312 ? -25.579 -54.854 51.195  1.00 68.37  ? 285 ARG A CB  1 
ATOM   5529 C  CG  . ARG B 1 312 ? -24.148 -55.039 51.666  1.00 73.50  ? 285 ARG A CG  1 
ATOM   5530 C  CD  . ARG B 1 312 ? -23.539 -53.709 52.055  1.00 83.50  ? 285 ARG A CD  1 
ATOM   5531 N  NE  . ARG B 1 312 ? -24.179 -53.198 53.273  1.00 93.18  ? 285 ARG A NE  1 
ATOM   5532 C  CZ  . ARG B 1 312 ? -24.254 -51.913 53.632  1.00 99.77  ? 285 ARG A CZ  1 
ATOM   5533 N  NH1 . ARG B 1 312 ? -24.870 -51.593 54.767  1.00 95.91  ? 285 ARG A NH1 1 
ATOM   5534 N  NH2 . ARG B 1 312 ? -23.728 -50.945 52.872  1.00 104.10 ? 285 ARG A NH2 1 
ATOM   5535 N  N   . ARG B 1 313 ? -28.481 -55.261 52.367  1.00 64.42  ? 286 ARG A N   1 
ATOM   5536 C  CA  . ARG B 1 313 ? -29.411 -55.033 53.475  1.00 65.01  ? 286 ARG A CA  1 
ATOM   5537 C  C   . ARG B 1 313 ? -30.535 -56.070 53.530  1.00 68.76  ? 286 ARG A C   1 
ATOM   5538 O  O   . ARG B 1 313 ? -31.517 -55.909 54.275  1.00 67.65  ? 286 ARG A O   1 
ATOM   5539 C  CB  . ARG B 1 313 ? -29.999 -53.624 53.406  1.00 63.86  ? 286 ARG A CB  1 
ATOM   5540 C  CG  . ARG B 1 313 ? -28.938 -52.552 53.395  1.00 69.18  ? 286 ARG A CG  1 
ATOM   5541 C  CD  . ARG B 1 313 ? -29.545 -51.236 53.809  1.00 76.41  ? 286 ARG A CD  1 
ATOM   5542 N  NE  . ARG B 1 313 ? -28.716 -50.072 53.506  1.00 78.20  ? 286 ARG A NE  1 
ATOM   5543 C  CZ  . ARG B 1 313 ? -29.028 -48.830 53.877  1.00 87.07  ? 286 ARG A CZ  1 
ATOM   5544 N  NH1 . ARG B 1 313 ? -30.141 -48.592 54.570  1.00 84.20  ? 286 ARG A NH1 1 
ATOM   5545 N  NH2 . ARG B 1 313 ? -28.231 -47.815 53.554  1.00 95.10  ? 286 ARG A NH2 1 
ATOM   5546 N  N   . ASN B 1 314 ? -30.406 -57.131 52.743  1.00 65.91  ? 287 ASN A N   1 
ATOM   5547 C  CA  . ASN B 1 314 ? -31.296 -58.263 52.879  1.00 70.51  ? 287 ASN A CA  1 
ATOM   5548 C  C   . ASN B 1 314 ? -32.774 -57.940 52.643  1.00 76.31  ? 287 ASN A C   1 
ATOM   5549 O  O   . ASN B 1 314 ? -33.646 -58.508 53.309  1.00 79.06  ? 287 ASN A O   1 
ATOM   5550 C  CB  . ASN B 1 314 ? -31.138 -58.805 54.282  1.00 72.73  ? 287 ASN A CB  1 
ATOM   5551 C  CG  . ASN B 1 314 ? -31.519 -60.244 54.396  1.00 79.42  ? 287 ASN A CG  1 
ATOM   5552 O  OD1 . ASN B 1 314 ? -31.495 -60.999 53.401  1.00 65.74  ? 287 ASN A OD1 1 
ATOM   5553 N  ND2 . ASN B 1 314 ? -31.882 -60.649 55.635  1.00 92.77  ? 287 ASN A ND2 1 
ATOM   5554 N  N   . ILE B 1 315 ? -33.065 -57.043 51.700  1.00 72.99  ? 288 ILE A N   1 
ATOM   5555 C  CA  . ILE B 1 315 ? -34.445 -56.646 51.457  1.00 70.29  ? 288 ILE A CA  1 
ATOM   5556 C  C   . ILE B 1 315 ? -35.184 -57.667 50.588  1.00 73.45  ? 288 ILE A C   1 
ATOM   5557 O  O   . ILE B 1 315 ? -34.884 -57.858 49.408  1.00 69.78  ? 288 ILE A O   1 
ATOM   5558 C  CB  . ILE B 1 315 ? -34.554 -55.239 50.875  1.00 68.92  ? 288 ILE A CB  1 
ATOM   5559 C  CG1 . ILE B 1 315 ? -33.953 -54.243 51.859  1.00 73.76  ? 288 ILE A CG1 1 
ATOM   5560 C  CG2 . ILE B 1 315 ? -36.015 -54.898 50.621  1.00 66.74  ? 288 ILE A CG2 1 
ATOM   5561 C  CD1 . ILE B 1 315 ? -33.750 -52.853 51.300  1.00 76.06  ? 288 ILE A CD1 1 
ATOM   5562 N  N   . THR B 1 316 ? -36.222 -58.240 51.193  1.00 77.14  ? 289 THR A N   1 
ATOM   5563 C  CA  . THR B 1 316 ? -36.749 -59.534 50.821  1.00 76.11  ? 289 THR A CA  1 
ATOM   5564 C  C   . THR B 1 316 ? -38.201 -59.482 50.404  1.00 67.16  ? 289 THR A C   1 
ATOM   5565 O  O   . THR B 1 316 ? -38.952 -58.571 50.752  1.00 65.88  ? 289 THR A O   1 
ATOM   5566 C  CB  . THR B 1 316 ? -36.505 -60.518 52.008  1.00 85.72  ? 289 THR A CB  1 
ATOM   5567 O  OG1 . THR B 1 316 ? -35.468 -61.421 51.632  1.00 92.09  ? 289 THR A OG1 1 
ATOM   5568 C  CG2 . THR B 1 316 ? -37.756 -61.332 52.462  1.00 84.48  ? 289 THR A CG2 1 
ATOM   5569 N  N   . GLY B 1 317 ? -38.586 -60.489 49.646  1.00 67.08  ? 290 GLY A N   1 
ATOM   5570 C  CA  . GLY B 1 317 ? -39.974 -60.671 49.258  1.00 68.03  ? 290 GLY A CA  1 
ATOM   5571 C  C   . GLY B 1 317 ? -40.556 -59.560 48.409  1.00 70.82  ? 290 GLY A C   1 
ATOM   5572 O  O   . GLY B 1 317 ? -41.755 -59.294 48.488  1.00 68.00  ? 290 GLY A O   1 
ATOM   5573 N  N   . LYS B 1 318 ? -39.730 -58.901 47.596  1.00 69.64  ? 291 LYS A N   1 
ATOM   5574 C  CA  . LYS B 1 318 ? -40.265 -57.926 46.651  1.00 63.86  ? 291 LYS A CA  1 
ATOM   5575 C  C   . LYS B 1 318 ? -40.588 -58.607 45.358  1.00 56.20  ? 291 LYS A C   1 
ATOM   5576 O  O   . LYS B 1 318 ? -39.960 -59.586 44.984  1.00 54.75  ? 291 LYS A O   1 
ATOM   5577 C  CB  . LYS B 1 318 ? -39.292 -56.784 46.400  1.00 63.71  ? 291 LYS A CB  1 
ATOM   5578 C  CG  . LYS B 1 318 ? -38.985 -55.969 47.642  1.00 60.87  ? 291 LYS A CG  1 
ATOM   5579 C  CD  . LYS B 1 318 ? -40.170 -55.158 48.144  1.00 57.59  ? 291 LYS A CD  1 
ATOM   5580 C  CE  . LYS B 1 318 ? -39.752 -54.439 49.417  1.00 56.53  ? 291 LYS A CE  1 
ATOM   5581 N  NZ  . LYS B 1 318 ? -40.879 -53.803 50.138  1.00 55.03  ? 291 LYS A NZ  1 
ATOM   5582 N  N   . ILE B 1 319 ? -41.588 -58.093 44.670  1.00 56.49  ? 292 ILE A N   1 
ATOM   5583 C  CA  . ILE B 1 319 ? -41.890 -58.589 43.346  1.00 54.25  ? 292 ILE A CA  1 
ATOM   5584 C  C   . ILE B 1 319 ? -41.387 -57.566 42.347  1.00 57.93  ? 292 ILE A C   1 
ATOM   5585 O  O   . ILE B 1 319 ? -41.909 -56.450 42.259  1.00 62.77  ? 292 ILE A O   1 
ATOM   5586 C  CB  . ILE B 1 319 ? -43.380 -58.853 43.149  1.00 53.73  ? 292 ILE A CB  1 
ATOM   5587 C  CG1 . ILE B 1 319 ? -43.924 -59.751 44.285  1.00 51.73  ? 292 ILE A CG1 1 
ATOM   5588 C  CG2 . ILE B 1 319 ? -43.589 -59.486 41.783  1.00 54.98  ? 292 ILE A CG2 1 
ATOM   5589 C  CD1 . ILE B 1 319 ? -45.375 -60.171 44.147  1.00 49.92  ? 292 ILE A CD1 1 
ATOM   5590 N  N   . TRP B 1 320 ? -40.356 -57.974 41.611  1.00 59.95  ? 293 TRP A N   1 
ATOM   5591 C  CA  . TRP B 1 320 ? -39.663 -57.145 40.637  1.00 59.00  ? 293 TRP A CA  1 
ATOM   5592 C  C   . TRP B 1 320 ? -40.274 -57.359 39.257  1.00 58.65  ? 293 TRP A C   1 
ATOM   5593 O  O   . TRP B 1 320 ? -40.332 -58.479 38.751  1.00 63.27  ? 293 TRP A O   1 
ATOM   5594 C  CB  . TRP B 1 320 ? -38.161 -57.491 40.618  1.00 57.72  ? 293 TRP A CB  1 
ATOM   5595 C  CG  . TRP B 1 320 ? -37.494 -57.357 41.968  1.00 59.16  ? 293 TRP A CG  1 
ATOM   5596 C  CD1 . TRP B 1 320 ? -37.226 -58.357 42.846  1.00 63.89  ? 293 TRP A CD1 1 
ATOM   5597 C  CD2 . TRP B 1 320 ? -37.047 -56.154 42.593  1.00 60.41  ? 293 TRP A CD2 1 
ATOM   5598 N  NE1 . TRP B 1 320 ? -36.638 -57.858 43.980  1.00 62.18  ? 293 TRP A NE1 1 
ATOM   5599 C  CE2 . TRP B 1 320 ? -36.514 -56.508 43.854  1.00 61.50  ? 293 TRP A CE2 1 
ATOM   5600 C  CE3 . TRP B 1 320 ? -37.044 -54.811 42.214  1.00 59.02  ? 293 TRP A CE3 1 
ATOM   5601 C  CZ2 . TRP B 1 320 ? -35.982 -55.574 44.736  1.00 64.44  ? 293 TRP A CZ2 1 
ATOM   5602 C  CZ3 . TRP B 1 320 ? -36.513 -53.873 43.103  1.00 62.07  ? 293 TRP A CZ3 1 
ATOM   5603 C  CH2 . TRP B 1 320 ? -35.996 -54.261 44.347  1.00 65.11  ? 293 TRP A CH2 1 
ATOM   5604 N  N   . LEU B 1 321 ? -40.755 -56.280 38.663  1.00 55.98  ? 294 LEU A N   1 
ATOM   5605 C  CA  . LEU B 1 321 ? -41.141 -56.288 37.271  1.00 54.43  ? 294 LEU A CA  1 
ATOM   5606 C  C   . LEU B 1 321 ? -39.987 -55.677 36.461  1.00 56.86  ? 294 LEU A C   1 
ATOM   5607 O  O   . LEU B 1 321 ? -39.625 -54.504 36.622  1.00 50.57  ? 294 LEU A O   1 
ATOM   5608 C  CB  . LEU B 1 321 ? -42.431 -55.508 37.080  1.00 58.96  ? 294 LEU A CB  1 
ATOM   5609 C  CG  . LEU B 1 321 ? -43.739 -56.311 37.016  1.00 65.15  ? 294 LEU A CG  1 
ATOM   5610 C  CD1 . LEU B 1 321 ? -43.764 -57.492 37.979  1.00 71.43  ? 294 LEU A CD1 1 
ATOM   5611 C  CD2 . LEU B 1 321 ? -44.916 -55.393 37.300  1.00 61.53  ? 294 LEU A CD2 1 
ATOM   5612 N  N   . ALA B 1 322 ? -39.427 -56.490 35.574  1.00 56.45  ? 295 ALA A N   1 
ATOM   5613 C  CA  . ALA B 1 322 ? -38.179 -56.178 34.925  1.00 51.71  ? 295 ALA A CA  1 
ATOM   5614 C  C   . ALA B 1 322 ? -38.416 -55.797 33.502  1.00 52.56  ? 295 ALA A C   1 
ATOM   5615 O  O   . ALA B 1 322 ? -39.019 -56.577 32.769  1.00 48.85  ? 295 ALA A O   1 
ATOM   5616 C  CB  . ALA B 1 322 ? -37.287 -57.380 34.961  1.00 54.27  ? 295 ALA A CB  1 
ATOM   5617 N  N   . SER B 1 323 ? -37.940 -54.604 33.115  1.00 49.71  ? 296 SER A N   1 
ATOM   5618 C  CA  . SER B 1 323 ? -37.887 -54.215 31.709  1.00 47.40  ? 296 SER A CA  1 
ATOM   5619 C  C   . SER B 1 323 ? -36.855 -55.097 31.036  1.00 47.84  ? 296 SER A C   1 
ATOM   5620 O  O   . SER B 1 323 ? -35.993 -55.661 31.687  1.00 49.15  ? 296 SER A O   1 
ATOM   5621 C  CB  . SER B 1 323 ? -37.492 -52.739 31.534  1.00 47.92  ? 296 SER A CB  1 
ATOM   5622 O  OG  . SER B 1 323 ? -36.090 -52.513 31.762  1.00 49.52  ? 296 SER A OG  1 
ATOM   5623 N  N   . GLU B 1 324 ? -36.903 -55.156 29.721  1.00 54.58  ? 297 GLU A N   1 
ATOM   5624 C  CA  . GLU B 1 324 ? -36.203 -56.183 28.942  1.00 58.19  ? 297 GLU A CA  1 
ATOM   5625 C  C   . GLU B 1 324 ? -34.698 -56.001 28.982  1.00 53.74  ? 297 GLU A C   1 
ATOM   5626 O  O   . GLU B 1 324 ? -33.967 -56.953 28.866  1.00 54.56  ? 297 GLU A O   1 
ATOM   5627 C  CB  . GLU B 1 324 ? -36.770 -56.225 27.517  1.00 58.19  ? 297 GLU A CB  1 
ATOM   5628 C  CG  . GLU B 1 324 ? -35.954 -57.007 26.530  1.00 72.47  ? 297 GLU A CG  1 
ATOM   5629 C  CD  . GLU B 1 324 ? -34.757 -56.230 26.037  1.00 87.00  ? 297 GLU A CD  1 
ATOM   5630 O  OE1 . GLU B 1 324 ? -34.876 -54.982 25.890  1.00 102.45 ? 297 GLU A OE1 1 
ATOM   5631 O  OE2 . GLU B 1 324 ? -33.704 -56.878 25.805  1.00 90.54  ? 297 GLU A OE2 1 
ATOM   5632 N  N   . ALA B 1 325 ? -34.250 -54.779 29.213  1.00 58.01  ? 298 ALA A N   1 
ATOM   5633 C  CA  . ALA B 1 325 ? -32.831 -54.472 29.290  1.00 57.16  ? 298 ALA A CA  1 
ATOM   5634 C  C   . ALA B 1 325 ? -32.101 -55.155 30.442  1.00 59.26  ? 298 ALA A C   1 
ATOM   5635 O  O   . ALA B 1 325 ? -30.875 -55.286 30.388  1.00 70.81  ? 298 ALA A O   1 
ATOM   5636 C  CB  . ALA B 1 325 ? -32.652 -52.971 29.405  1.00 56.98  ? 298 ALA A CB  1 
ATOM   5637 N  N   . TRP B 1 326 ? -32.821 -55.533 31.500  1.00 55.05  ? 299 TRP A N   1 
ATOM   5638 C  CA  . TRP B 1 326 ? -32.212 -56.287 32.613  1.00 52.95  ? 299 TRP A CA  1 
ATOM   5639 C  C   . TRP B 1 326 ? -32.872 -57.625 32.937  1.00 50.71  ? 299 TRP A C   1 
ATOM   5640 O  O   . TRP B 1 326 ? -32.315 -58.412 33.678  1.00 47.46  ? 299 TRP A O   1 
ATOM   5641 C  CB  . TRP B 1 326 ? -32.101 -55.437 33.883  1.00 51.63  ? 299 TRP A CB  1 
ATOM   5642 C  CG  . TRP B 1 326 ? -33.367 -55.210 34.696  1.00 51.89  ? 299 TRP A CG  1 
ATOM   5643 C  CD1 . TRP B 1 326 ? -34.297 -54.236 34.508  1.00 51.50  ? 299 TRP A CD1 1 
ATOM   5644 C  CD2 . TRP B 1 326 ? -33.777 -55.928 35.857  1.00 52.97  ? 299 TRP A CD2 1 
ATOM   5645 N  NE1 . TRP B 1 326 ? -35.259 -54.307 35.471  1.00 54.06  ? 299 TRP A NE1 1 
ATOM   5646 C  CE2 . TRP B 1 326 ? -34.962 -55.349 36.310  1.00 54.64  ? 299 TRP A CE2 1 
ATOM   5647 C  CE3 . TRP B 1 326 ? -33.259 -57.011 36.553  1.00 58.95  ? 299 TRP A CE3 1 
ATOM   5648 C  CZ2 . TRP B 1 326 ? -35.638 -55.824 37.433  1.00 53.10  ? 299 TRP A CZ2 1 
ATOM   5649 C  CZ3 . TRP B 1 326 ? -33.934 -57.473 37.681  1.00 55.03  ? 299 TRP A CZ3 1 
ATOM   5650 C  CH2 . TRP B 1 326 ? -35.098 -56.882 38.101  1.00 52.38  ? 299 TRP A CH2 1 
ATOM   5651 N  N   . ALA B 1 327 ? -34.029 -57.888 32.349  1.00 50.21  ? 300 ALA A N   1 
ATOM   5652 C  CA  . ALA B 1 327 ? -34.769 -59.113 32.596  1.00 51.35  ? 300 ALA A CA  1 
ATOM   5653 C  C   . ALA B 1 327 ? -33.956 -60.375 32.277  1.00 55.58  ? 300 ALA A C   1 
ATOM   5654 O  O   . ALA B 1 327 ? -34.284 -61.445 32.782  1.00 55.13  ? 300 ALA A O   1 
ATOM   5655 C  CB  . ALA B 1 327 ? -36.041 -59.092 31.774  1.00 48.72  ? 300 ALA A CB  1 
ATOM   5656 N  N   . SER B 1 328 ? -32.917 -60.226 31.439  1.00 61.30  ? 301 SER A N   1 
ATOM   5657 C  CA  . SER B 1 328 ? -31.967 -61.297 31.084  1.00 62.12  ? 301 SER A CA  1 
ATOM   5658 C  C   . SER B 1 328 ? -30.516 -61.003 31.436  1.00 61.03  ? 301 SER A C   1 
ATOM   5659 O  O   . SER B 1 328 ? -29.622 -61.512 30.782  1.00 67.98  ? 301 SER A O   1 
ATOM   5660 C  CB  . SER B 1 328 ? -31.995 -61.491 29.578  1.00 59.70  ? 301 SER A CB  1 
ATOM   5661 O  OG  . SER B 1 328 ? -33.296 -61.787 29.164  1.00 66.70  ? 301 SER A OG  1 
ATOM   5662 N  N   . SER B 1 329 ? -30.256 -60.156 32.418  1.00 59.22  ? 302 SER A N   1 
ATOM   5663 C  CA  . SER B 1 329 ? -28.918 -59.575 32.520  1.00 57.15  ? 302 SER A CA  1 
ATOM   5664 C  C   . SER B 1 329 ? -28.081 -60.341 33.503  1.00 57.77  ? 302 SER A C   1 
ATOM   5665 O  O   . SER B 1 329 ? -28.448 -60.486 34.673  1.00 54.39  ? 302 SER A O   1 
ATOM   5666 C  CB  . SER B 1 329 ? -28.989 -58.113 32.942  1.00 55.13  ? 302 SER A CB  1 
ATOM   5667 O  OG  . SER B 1 329 ? -27.779 -57.700 33.536  1.00 55.17  ? 302 SER A OG  1 
ATOM   5668 N  N   . SER B 1 330 ? -26.927 -60.792 33.035  1.00 57.13  ? 303 SER A N   1 
ATOM   5669 C  CA  . SER B 1 330 ? -26.023 -61.572 33.878  1.00 55.94  ? 303 SER A CA  1 
ATOM   5670 C  C   . SER B 1 330 ? -25.370 -60.770 35.045  1.00 55.55  ? 303 SER A C   1 
ATOM   5671 O  O   . SER B 1 330 ? -24.880 -61.338 36.018  1.00 69.41  ? 303 SER A O   1 
ATOM   5672 C  CB  . SER B 1 330 ? -24.966 -62.205 32.991  1.00 53.02  ? 303 SER A CB  1 
ATOM   5673 O  OG  . SER B 1 330 ? -23.963 -61.265 32.714  1.00 54.06  ? 303 SER A OG  1 
ATOM   5674 N  N   . LEU B 1 331 ? -25.359 -59.454 34.959  1.00 54.28  ? 304 LEU A N   1 
ATOM   5675 C  CA  . LEU B 1 331 ? -24.927 -58.641 36.084  1.00 56.69  ? 304 LEU A CA  1 
ATOM   5676 C  C   . LEU B 1 331 ? -25.878 -58.673 37.277  1.00 58.22  ? 304 LEU A C   1 
ATOM   5677 O  O   . LEU B 1 331 ? -25.456 -58.386 38.388  1.00 55.58  ? 304 LEU A O   1 
ATOM   5678 C  CB  . LEU B 1 331 ? -24.791 -57.185 35.665  1.00 58.44  ? 304 LEU A CB  1 
ATOM   5679 C  CG  . LEU B 1 331 ? -23.697 -56.900 34.667  1.00 62.08  ? 304 LEU A CG  1 
ATOM   5680 C  CD1 . LEU B 1 331 ? -23.746 -55.452 34.182  1.00 67.99  ? 304 LEU A CD1 1 
ATOM   5681 C  CD2 . LEU B 1 331 ? -22.372 -57.216 35.316  1.00 63.42  ? 304 LEU A CD2 1 
ATOM   5682 N  N   . ILE B 1 332 ? -27.155 -58.969 37.040  1.00 62.72  ? 305 ILE A N   1 
ATOM   5683 C  CA  . ILE B 1 332 ? -28.175 -59.001 38.106  1.00 63.12  ? 305 ILE A CA  1 
ATOM   5684 C  C   . ILE B 1 332 ? -28.648 -60.434 38.409  1.00 61.50  ? 305 ILE A C   1 
ATOM   5685 O  O   . ILE B 1 332 ? -28.964 -60.768 39.553  1.00 59.17  ? 305 ILE A O   1 
ATOM   5686 C  CB  . ILE B 1 332 ? -29.440 -58.158 37.718  1.00 66.23  ? 305 ILE A CB  1 
ATOM   5687 C  CG1 . ILE B 1 332 ? -29.074 -56.770 37.138  1.00 63.13  ? 305 ILE A CG1 1 
ATOM   5688 C  CG2 . ILE B 1 332 ? -30.400 -58.028 38.906  1.00 64.34  ? 305 ILE A CG2 1 
ATOM   5689 C  CD1 . ILE B 1 332 ? -28.411 -55.775 38.085  1.00 57.97  ? 305 ILE A CD1 1 
ATOM   5690 N  N   . ALA B 1 333 ? -28.761 -61.250 37.365  1.00 62.98  ? 306 ALA A N   1 
ATOM   5691 C  CA  . ALA B 1 333 ? -29.189 -62.637 37.497  1.00 64.73  ? 306 ALA A CA  1 
ATOM   5692 C  C   . ALA B 1 333 ? -28.041 -63.477 38.041  1.00 60.91  ? 306 ALA A C   1 
ATOM   5693 O  O   . ALA B 1 333 ? -27.473 -64.279 37.323  1.00 64.17  ? 306 ALA A O   1 
ATOM   5694 C  CB  . ALA B 1 333 ? -29.661 -63.183 36.143  1.00 63.91  ? 306 ALA A CB  1 
ATOM   5695 N  N   . MET B 1 334 ? -27.744 -63.296 39.324  1.00 63.58  ? 307 MET A N   1 
ATOM   5696 C  CA  . MET B 1 334 ? -26.630 -63.946 40.003  1.00 69.05  ? 307 MET A CA  1 
ATOM   5697 C  C   . MET B 1 334 ? -27.119 -64.685 41.244  1.00 71.11  ? 307 MET A C   1 
ATOM   5698 O  O   . MET B 1 334 ? -27.799 -64.099 42.093  1.00 72.85  ? 307 MET A O   1 
ATOM   5699 C  CB  . MET B 1 334 ? -25.598 -62.902 40.410  1.00 76.44  ? 307 MET A CB  1 
ATOM   5700 C  CG  . MET B 1 334 ? -24.919 -62.237 39.216  1.00 84.58  ? 307 MET A CG  1 
ATOM   5701 S  SD  . MET B 1 334 ? -23.178 -61.894 39.512  1.00 90.47  ? 307 MET A SD  1 
ATOM   5702 C  CE  . MET B 1 334 ? -22.568 -63.581 39.608  1.00 91.92  ? 307 MET A CE  1 
ATOM   5703 N  N   . PRO B 1 335 ? -26.753 -65.971 41.380  1.00 72.85  ? 308 PRO A N   1 
ATOM   5704 C  CA  . PRO B 1 335 ? -27.349 -66.789 42.439  1.00 69.40  ? 308 PRO A CA  1 
ATOM   5705 C  C   . PRO B 1 335 ? -27.226 -66.204 43.828  1.00 68.47  ? 308 PRO A C   1 
ATOM   5706 O  O   . PRO B 1 335 ? -28.112 -66.400 44.640  1.00 68.81  ? 308 PRO A O   1 
ATOM   5707 C  CB  . PRO B 1 335 ? -26.563 -68.089 42.360  1.00 67.86  ? 308 PRO A CB  1 
ATOM   5708 C  CG  . PRO B 1 335 ? -26.107 -68.135 40.942  1.00 72.92  ? 308 PRO A CG  1 
ATOM   5709 C  CD  . PRO B 1 335 ? -25.722 -66.720 40.649  1.00 70.37  ? 308 PRO A CD  1 
ATOM   5710 N  N   . GLN B 1 336 ? -26.151 -65.482 44.109  1.00 67.55  ? 309 GLN A N   1 
ATOM   5711 C  CA  . GLN B 1 336 ? -26.026 -64.863 45.418  1.00 65.85  ? 309 GLN A CA  1 
ATOM   5712 C  C   . GLN B 1 336 ? -26.961 -63.672 45.633  1.00 67.81  ? 309 GLN A C   1 
ATOM   5713 O  O   . GLN B 1 336 ? -26.962 -63.093 46.722  1.00 65.98  ? 309 GLN A O   1 
ATOM   5714 C  CB  . GLN B 1 336 ? -24.576 -64.455 45.721  1.00 71.04  ? 309 GLN A CB  1 
ATOM   5715 C  CG  . GLN B 1 336 ? -23.991 -63.301 44.915  1.00 71.49  ? 309 GLN A CG  1 
ATOM   5716 C  CD  . GLN B 1 336 ? -23.254 -63.756 43.669  1.00 78.13  ? 309 GLN A CD  1 
ATOM   5717 O  OE1 . GLN B 1 336 ? -23.514 -64.839 43.130  1.00 73.86  ? 309 GLN A OE1 1 
ATOM   5718 N  NE2 . GLN B 1 336 ? -22.347 -62.910 43.180  1.00 87.62  ? 309 GLN A NE2 1 
ATOM   5719 N  N   . TYR B 1 337 ? -27.725 -63.268 44.615  1.00 67.99  ? 310 TYR A N   1 
ATOM   5720 C  CA  . TYR B 1 337 ? -28.763 -62.261 44.835  1.00 66.76  ? 310 TYR A CA  1 
ATOM   5721 C  C   . TYR B 1 337 ? -30.183 -62.859 44.879  1.00 66.79  ? 310 TYR A C   1 
ATOM   5722 O  O   . TYR B 1 337 ? -31.157 -62.123 44.993  1.00 74.22  ? 310 TYR A O   1 
ATOM   5723 C  CB  . TYR B 1 337 ? -28.742 -61.198 43.747  1.00 67.34  ? 310 TYR A CB  1 
ATOM   5724 C  CG  . TYR B 1 337 ? -27.430 -60.525 43.438  1.00 64.43  ? 310 TYR A CG  1 
ATOM   5725 C  CD1 . TYR B 1 337 ? -26.474 -60.281 44.412  1.00 65.87  ? 310 TYR A CD1 1 
ATOM   5726 C  CD2 . TYR B 1 337 ? -27.182 -60.079 42.161  1.00 63.18  ? 310 TYR A CD2 1 
ATOM   5727 C  CE1 . TYR B 1 337 ? -25.287 -59.636 44.101  1.00 65.89  ? 310 TYR A CE1 1 
ATOM   5728 C  CE2 . TYR B 1 337 ? -26.010 -59.436 41.837  1.00 69.62  ? 310 TYR A CE2 1 
ATOM   5729 C  CZ  . TYR B 1 337 ? -25.066 -59.216 42.799  1.00 67.85  ? 310 TYR A CZ  1 
ATOM   5730 O  OH  . TYR B 1 337 ? -23.924 -58.579 42.407  1.00 72.26  ? 310 TYR A OH  1 
ATOM   5731 N  N   . PHE B 1 338 ? -30.315 -64.174 44.810  1.00 59.50  ? 311 PHE A N   1 
ATOM   5732 C  CA  . PHE B 1 338 ? -31.610 -64.792 44.545  1.00 60.93  ? 311 PHE A CA  1 
ATOM   5733 C  C   . PHE B 1 338 ? -32.630 -64.631 45.667  1.00 65.35  ? 311 PHE A C   1 
ATOM   5734 O  O   . PHE B 1 338 ? -33.838 -64.753 45.432  1.00 61.86  ? 311 PHE A O   1 
ATOM   5735 C  CB  . PHE B 1 338 ? -31.421 -66.267 44.271  1.00 64.83  ? 311 PHE A CB  1 
ATOM   5736 C  CG  . PHE B 1 338 ? -32.578 -66.911 43.590  1.00 65.16  ? 311 PHE A CG  1 
ATOM   5737 C  CD1 . PHE B 1 338 ? -32.741 -66.782 42.228  1.00 67.05  ? 311 PHE A CD1 1 
ATOM   5738 C  CD2 . PHE B 1 338 ? -33.492 -67.672 44.308  1.00 66.20  ? 311 PHE A CD2 1 
ATOM   5739 C  CE1 . PHE B 1 338 ? -33.801 -67.400 41.572  1.00 67.45  ? 311 PHE A CE1 1 
ATOM   5740 C  CE2 . PHE B 1 338 ? -34.547 -68.298 43.663  1.00 68.25  ? 311 PHE A CE2 1 
ATOM   5741 C  CZ  . PHE B 1 338 ? -34.698 -68.160 42.286  1.00 68.81  ? 311 PHE A CZ  1 
ATOM   5742 N  N   . HIS B 1 339 ? -32.147 -64.375 46.879  1.00 65.84  ? 312 HIS A N   1 
ATOM   5743 C  CA  . HIS B 1 339 ? -33.023 -64.108 48.034  1.00 67.13  ? 312 HIS A CA  1 
ATOM   5744 C  C   . HIS B 1 339 ? -33.678 -62.727 47.932  1.00 65.85  ? 312 HIS A C   1 
ATOM   5745 O  O   . HIS B 1 339 ? -34.658 -62.410 48.622  1.00 63.48  ? 312 HIS A O   1 
ATOM   5746 C  CB  . HIS B 1 339 ? -32.267 -64.277 49.366  1.00 73.96  ? 312 HIS A CB  1 
ATOM   5747 C  CG  . HIS B 1 339 ? -31.127 -63.316 49.558  1.00 82.92  ? 312 HIS A CG  1 
ATOM   5748 N  ND1 . HIS B 1 339 ? -29.915 -63.442 48.904  1.00 84.76  ? 312 HIS A ND1 1 
ATOM   5749 C  CD2 . HIS B 1 339 ? -31.012 -62.221 50.348  1.00 88.15  ? 312 HIS A CD2 1 
ATOM   5750 C  CE1 . HIS B 1 339 ? -29.116 -62.456 49.268  1.00 85.72  ? 312 HIS A CE1 1 
ATOM   5751 N  NE2 . HIS B 1 339 ? -29.755 -61.702 50.145  1.00 85.91  ? 312 HIS A NE2 1 
ATOM   5752 N  N   . VAL B 1 340 ? -33.132 -61.899 47.055  1.00 68.31  ? 313 VAL A N   1 
ATOM   5753 C  CA  . VAL B 1 340 ? -33.707 -60.589 46.765  1.00 66.21  ? 313 VAL A CA  1 
ATOM   5754 C  C   . VAL B 1 340 ? -34.397 -60.588 45.417  1.00 61.66  ? 313 VAL A C   1 
ATOM   5755 O  O   . VAL B 1 340 ? -35.521 -60.120 45.269  1.00 64.75  ? 313 VAL A O   1 
ATOM   5756 C  CB  . VAL B 1 340 ? -32.605 -59.518 46.778  1.00 63.65  ? 313 VAL A CB  1 
ATOM   5757 C  CG1 . VAL B 1 340 ? -33.038 -58.271 46.016  1.00 61.00  ? 313 VAL A CG1 1 
ATOM   5758 C  CG2 . VAL B 1 340 ? -32.212 -59.212 48.219  1.00 63.92  ? 313 VAL A CG2 1 
ATOM   5759 N  N   . VAL B 1 341 ? -33.718 -61.150 44.441  1.00 60.62  ? 314 VAL A N   1 
ATOM   5760 C  CA  . VAL B 1 341 ? -34.064 -60.934 43.072  1.00 60.54  ? 314 VAL A CA  1 
ATOM   5761 C  C   . VAL B 1 341 ? -34.854 -62.087 42.522  1.00 55.00  ? 314 VAL A C   1 
ATOM   5762 O  O   . VAL B 1 341 ? -35.323 -62.012 41.411  1.00 51.80  ? 314 VAL A O   1 
ATOM   5763 C  CB  . VAL B 1 341 ? -32.757 -60.744 42.279  1.00 65.58  ? 314 VAL A CB  1 
ATOM   5764 C  CG1 . VAL B 1 341 ? -32.256 -62.067 41.726  1.00 65.34  ? 314 VAL A CG1 1 
ATOM   5765 C  CG2 . VAL B 1 341 ? -32.927 -59.700 41.199  1.00 69.71  ? 314 VAL A CG2 1 
ATOM   5766 N  N   . GLY B 1 342 ? -34.984 -63.170 43.287  1.00 56.49  ? 315 GLY A N   1 
ATOM   5767 C  CA  . GLY B 1 342 ? -35.673 -64.371 42.812  1.00 53.46  ? 315 GLY A CA  1 
ATOM   5768 C  C   . GLY B 1 342 ? -37.152 -64.145 42.518  1.00 52.52  ? 315 GLY A C   1 
ATOM   5769 O  O   . GLY B 1 342 ? -37.866 -63.443 43.251  1.00 44.64  ? 315 GLY A O   1 
ATOM   5770 N  N   . GLY B 1 343 ? -37.613 -64.746 41.436  1.00 53.88  ? 316 GLY A N   1 
ATOM   5771 C  CA  . GLY B 1 343 ? -39.007 -64.650 41.054  1.00 57.44  ? 316 GLY A CA  1 
ATOM   5772 C  C   . GLY B 1 343 ? -39.361 -63.392 40.292  1.00 64.19  ? 316 GLY A C   1 
ATOM   5773 O  O   . GLY B 1 343 ? -40.538 -63.100 40.109  1.00 66.72  ? 316 GLY A O   1 
ATOM   5774 N  N   . THR B 1 344 ? -38.373 -62.640 39.806  1.00 65.27  ? 317 THR A N   1 
ATOM   5775 C  CA  . THR B 1 344 ? -38.729 -61.466 39.042  1.00 61.38  ? 317 THR A CA  1 
ATOM   5776 C  C   . THR B 1 344 ? -39.418 -61.910 37.774  1.00 57.88  ? 317 THR A C   1 
ATOM   5777 O  O   . THR B 1 344 ? -39.162 -62.987 37.268  1.00 51.72  ? 317 THR A O   1 
ATOM   5778 C  CB  . THR B 1 344 ? -37.555 -60.513 38.705  1.00 66.21  ? 317 THR A CB  1 
ATOM   5779 O  OG1 . THR B 1 344 ? -36.908 -60.890 37.482  1.00 66.74  ? 317 THR A OG1 1 
ATOM   5780 C  CG2 . THR B 1 344 ? -36.577 -60.439 39.832  1.00 64.01  ? 317 THR A CG2 1 
ATOM   5781 N  N   . ILE B 1 345 ? -40.298 -61.047 37.283  1.00 60.52  ? 318 ILE A N   1 
ATOM   5782 C  CA  . ILE B 1 345 ? -41.058 -61.272 36.066  1.00 60.02  ? 318 ILE A CA  1 
ATOM   5783 C  C   . ILE B 1 345 ? -40.626 -60.164 35.123  1.00 59.06  ? 318 ILE A C   1 
ATOM   5784 O  O   . ILE B 1 345 ? -40.515 -59.008 35.551  1.00 52.21  ? 318 ILE A O   1 
ATOM   5785 C  CB  . ILE B 1 345 ? -42.577 -61.151 36.307  1.00 63.66  ? 318 ILE A CB  1 
ATOM   5786 C  CG1 . ILE B 1 345 ? -43.044 -62.186 37.347  1.00 67.18  ? 318 ILE A CG1 1 
ATOM   5787 C  CG2 . ILE B 1 345 ? -43.342 -61.324 34.997  1.00 62.75  ? 318 ILE A CG2 1 
ATOM   5788 C  CD1 . ILE B 1 345 ? -44.284 -61.776 38.098  1.00 62.70  ? 318 ILE A CD1 1 
ATOM   5789 N  N   . GLY B 1 346 ? -40.421 -60.537 33.854  1.00 55.05  ? 319 GLY A N   1 
ATOM   5790 C  CA  . GLY B 1 346 ? -39.758 -59.702 32.879  1.00 54.41  ? 319 GLY A CA  1 
ATOM   5791 C  C   . GLY B 1 346 ? -40.121 -59.962 31.430  1.00 54.49  ? 319 GLY A C   1 
ATOM   5792 O  O   . GLY B 1 346 ? -40.948 -60.799 31.136  1.00 57.79  ? 319 GLY A O   1 
ATOM   5793 N  N   . PHE B 1 347 ? -39.518 -59.201 30.524  1.00 54.61  ? 320 PHE A N   1 
ATOM   5794 C  CA  . PHE B 1 347 ? -39.859 -59.282 29.112  1.00 55.71  ? 320 PHE A CA  1 
ATOM   5795 C  C   . PHE B 1 347 ? -38.640 -59.674 28.354  1.00 49.79  ? 320 PHE A C   1 
ATOM   5796 O  O   . PHE B 1 347 ? -37.546 -59.424 28.813  1.00 52.28  ? 320 PHE A O   1 
ATOM   5797 C  CB  . PHE B 1 347 ? -40.406 -57.962 28.610  1.00 53.28  ? 320 PHE A CB  1 
ATOM   5798 C  CG  . PHE B 1 347 ? -41.666 -57.573 29.294  1.00 60.81  ? 320 PHE A CG  1 
ATOM   5799 C  CD1 . PHE B 1 347 ? -42.885 -57.946 28.780  1.00 67.47  ? 320 PHE A CD1 1 
ATOM   5800 C  CD2 . PHE B 1 347 ? -41.629 -56.906 30.495  1.00 64.09  ? 320 PHE A CD2 1 
ATOM   5801 C  CE1 . PHE B 1 347 ? -44.052 -57.613 29.428  1.00 69.01  ? 320 PHE A CE1 1 
ATOM   5802 C  CE2 . PHE B 1 347 ? -42.789 -56.577 31.152  1.00 67.15  ? 320 PHE A CE2 1 
ATOM   5803 C  CZ  . PHE B 1 347 ? -44.007 -56.927 30.617  1.00 66.97  ? 320 PHE A CZ  1 
ATOM   5804 N  N   . ALA B 1 348 ? -38.842 -60.346 27.231  1.00 46.20  ? 321 ALA A N   1 
ATOM   5805 C  CA  . ALA B 1 348 ? -37.752 -60.828 26.411  1.00 46.91  ? 321 ALA A CA  1 
ATOM   5806 C  C   . ALA B 1 348 ? -38.183 -60.750 24.968  1.00 55.15  ? 321 ALA A C   1 
ATOM   5807 O  O   . ALA B 1 348 ? -39.373 -60.951 24.652  1.00 50.14  ? 321 ALA A O   1 
ATOM   5808 C  CB  . ALA B 1 348 ? -37.376 -62.243 26.778  1.00 45.01  ? 321 ALA A CB  1 
ATOM   5809 N  N   . LEU B 1 349 ? -37.234 -60.419 24.090  1.00 60.34  ? 322 LEU A N   1 
ATOM   5810 C  CA  . LEU B 1 349 ? -37.551 -60.326 22.663  1.00 62.74  ? 322 LEU A CA  1 
ATOM   5811 C  C   . LEU B 1 349 ? -37.768 -61.729 22.093  1.00 64.17  ? 322 LEU A C   1 
ATOM   5812 O  O   . LEU B 1 349 ? -37.353 -62.700 22.710  1.00 61.86  ? 322 LEU A O   1 
ATOM   5813 C  CB  . LEU B 1 349 ? -36.419 -59.634 21.906  1.00 65.58  ? 322 LEU A CB  1 
ATOM   5814 C  CG  . LEU B 1 349 ? -36.259 -58.112 21.990  1.00 70.37  ? 322 LEU A CG  1 
ATOM   5815 C  CD1 . LEU B 1 349 ? -37.597 -57.394 22.149  1.00 67.08  ? 322 LEU A CD1 1 
ATOM   5816 C  CD2 . LEU B 1 349 ? -35.298 -57.742 23.115  1.00 79.39  ? 322 LEU A CD2 1 
ATOM   5817 N  N   . LYS B 1 350 ? -38.408 -61.839 20.924  1.00 67.24  ? 323 LYS A N   1 
ATOM   5818 C  CA  . LYS B 1 350 ? -38.446 -63.126 20.197  1.00 66.16  ? 323 LYS A CA  1 
ATOM   5819 C  C   . LYS B 1 350 ? -37.022 -63.520 19.892  1.00 65.12  ? 323 LYS A C   1 
ATOM   5820 O  O   . LYS B 1 350 ? -36.209 -62.678 19.532  1.00 67.58  ? 323 LYS A O   1 
ATOM   5821 C  CB  . LYS B 1 350 ? -39.245 -63.068 18.871  1.00 62.71  ? 323 LYS A CB  1 
ATOM   5822 N  N   . ALA B 1 351 ? -36.719 -64.801 20.057  1.00 71.59  ? 324 ALA A N   1 
ATOM   5823 C  CA  . ALA B 1 351 ? -35.438 -65.381 19.609  1.00 68.86  ? 324 ALA A CA  1 
ATOM   5824 C  C   . ALA B 1 351 ? -35.351 -65.459 18.082  1.00 66.01  ? 324 ALA A C   1 
ATOM   5825 O  O   . ALA B 1 351 ? -36.379 -65.433 17.369  1.00 58.88  ? 324 ALA A O   1 
ATOM   5826 C  CB  . ALA B 1 351 ? -35.253 -66.767 20.204  1.00 72.70  ? 324 ALA A CB  1 
ATOM   5827 N  N   . GLY B 1 352 ? -34.116 -65.530 17.589  1.00 67.39  ? 325 GLY A N   1 
ATOM   5828 C  CA  . GLY B 1 352 ? -33.840 -65.709 16.154  1.00 69.52  ? 325 GLY A CA  1 
ATOM   5829 C  C   . GLY B 1 352 ? -32.769 -66.766 15.955  1.00 70.80  ? 325 GLY A C   1 
ATOM   5830 O  O   . GLY B 1 352 ? -32.045 -67.092 16.889  1.00 75.14  ? 325 GLY A O   1 
ATOM   5831 N  N   . GLN B 1 353 ? -32.669 -67.318 14.753  1.00 79.64  ? 326 GLN A N   1 
ATOM   5832 C  CA  . GLN B 1 353 ? -31.672 -68.353 14.475  1.00 84.49  ? 326 GLN A CA  1 
ATOM   5833 C  C   . GLN B 1 353 ? -30.627 -67.828 13.518  1.00 78.93  ? 326 GLN A C   1 
ATOM   5834 O  O   . GLN B 1 353 ? -30.964 -67.197 12.521  1.00 70.50  ? 326 GLN A O   1 
ATOM   5835 C  CB  . GLN B 1 353 ? -32.327 -69.576 13.854  1.00 95.41  ? 326 GLN A CB  1 
ATOM   5836 C  CG  . GLN B 1 353 ? -33.011 -70.507 14.840  1.00 102.67 ? 326 GLN A CG  1 
ATOM   5837 C  CD  . GLN B 1 353 ? -33.671 -71.702 14.149  1.00 111.29 ? 326 GLN A CD  1 
ATOM   5838 O  OE1 . GLN B 1 353 ? -33.466 -71.956 12.952  1.00 109.41 ? 326 GLN A OE1 1 
ATOM   5839 N  NE2 . GLN B 1 353 ? -34.466 -72.445 14.907  1.00 112.04 ? 326 GLN A NE2 1 
ATOM   5840 N  N   . ILE B 1 354 ? -29.365 -68.092 13.834  1.00 84.94  ? 327 ILE A N   1 
ATOM   5841 C  CA  . ILE B 1 354 ? -28.249 -67.780 12.939  1.00 90.49  ? 327 ILE A CA  1 
ATOM   5842 C  C   . ILE B 1 354 ? -27.399 -69.055 12.748  1.00 92.86  ? 327 ILE A C   1 
ATOM   5843 O  O   . ILE B 1 354 ? -26.495 -69.347 13.557  1.00 90.07  ? 327 ILE A O   1 
ATOM   5844 C  CB  . ILE B 1 354 ? -27.361 -66.618 13.462  1.00 87.11  ? 327 ILE A CB  1 
ATOM   5845 C  CG1 . ILE B 1 354 ? -28.206 -65.463 13.999  1.00 79.44  ? 327 ILE A CG1 1 
ATOM   5846 C  CG2 . ILE B 1 354 ? -26.451 -66.103 12.351  1.00 89.93  ? 327 ILE A CG2 1 
ATOM   5847 C  CD1 . ILE B 1 354 ? -27.375 -64.331 14.579  1.00 77.25  ? 327 ILE A CD1 1 
ATOM   5848 N  N   . PRO B 1 355 ? -27.709 -69.839 11.694  1.00 89.62  ? 328 PRO A N   1 
ATOM   5849 C  CA  . PRO B 1 355 ? -26.841 -70.950 11.307  1.00 84.53  ? 328 PRO A CA  1 
ATOM   5850 C  C   . PRO B 1 355 ? -25.405 -70.488 10.972  1.00 85.25  ? 328 PRO A C   1 
ATOM   5851 O  O   . PRO B 1 355 ? -25.203 -69.477 10.273  1.00 71.19  ? 328 PRO A O   1 
ATOM   5852 C  CB  . PRO B 1 355 ? -27.535 -71.524 10.068  1.00 84.17  ? 328 PRO A CB  1 
ATOM   5853 C  CG  . PRO B 1 355 ? -28.963 -71.125 10.207  1.00 88.11  ? 328 PRO A CG  1 
ATOM   5854 C  CD  . PRO B 1 355 ? -28.930 -69.782 10.869  1.00 88.90  ? 328 PRO A CD  1 
ATOM   5855 N  N   . GLY B 1 356 ? -24.428 -71.219 11.510  1.00 84.12  ? 329 GLY A N   1 
ATOM   5856 C  CA  . GLY B 1 356 ? -23.020 -70.954 11.254  1.00 80.83  ? 329 GLY A CA  1 
ATOM   5857 C  C   . GLY B 1 356 ? -22.385 -70.101 12.325  1.00 88.27  ? 329 GLY A C   1 
ATOM   5858 O  O   . GLY B 1 356 ? -21.155 -70.100 12.468  1.00 90.58  ? 329 GLY A O   1 
ATOM   5859 N  N   . PHE B 1 357 ? -23.216 -69.385 13.088  1.00 88.29  ? 330 PHE A N   1 
ATOM   5860 C  CA  . PHE B 1 357 ? -22.731 -68.334 13.967  1.00 80.29  ? 330 PHE A CA  1 
ATOM   5861 C  C   . PHE B 1 357 ? -22.009 -68.924 15.161  1.00 78.57  ? 330 PHE A C   1 
ATOM   5862 O  O   . PHE B 1 357 ? -20.926 -68.474 15.515  1.00 78.94  ? 330 PHE A O   1 
ATOM   5863 C  CB  . PHE B 1 357 ? -23.885 -67.419 14.410  1.00 84.72  ? 330 PHE A CB  1 
ATOM   5864 C  CG  . PHE B 1 357 ? -23.454 -66.276 15.289  1.00 71.48  ? 330 PHE A CG  1 
ATOM   5865 C  CD1 . PHE B 1 357 ? -22.498 -65.378 14.845  1.00 67.46  ? 330 PHE A CD1 1 
ATOM   5866 C  CD2 . PHE B 1 357 ? -24.004 -66.104 16.550  1.00 69.46  ? 330 PHE A CD2 1 
ATOM   5867 C  CE1 . PHE B 1 357 ? -22.074 -64.336 15.642  1.00 65.45  ? 330 PHE A CE1 1 
ATOM   5868 C  CE2 . PHE B 1 357 ? -23.596 -65.055 17.354  1.00 70.66  ? 330 PHE A CE2 1 
ATOM   5869 C  CZ  . PHE B 1 357 ? -22.622 -64.173 16.899  1.00 69.90  ? 330 PHE A CZ  1 
ATOM   5870 N  N   . ARG B 1 358 ? -22.586 -69.951 15.769  1.00 85.41  ? 331 ARG A N   1 
ATOM   5871 C  CA  . ARG B 1 358 ? -21.914 -70.595 16.900  1.00 84.99  ? 331 ARG A CA  1 
ATOM   5872 C  C   . ARG B 1 358 ? -20.504 -71.057 16.533  1.00 85.94  ? 331 ARG A C   1 
ATOM   5873 O  O   . ARG B 1 358 ? -19.551 -70.804 17.275  1.00 80.18  ? 331 ARG A O   1 
ATOM   5874 C  CB  . ARG B 1 358 ? -22.723 -71.774 17.457  1.00 82.76  ? 331 ARG A CB  1 
ATOM   5875 C  CG  . ARG B 1 358 ? -22.142 -72.263 18.777  1.00 83.53  ? 331 ARG A CG  1 
ATOM   5876 C  CD  . ARG B 1 358 ? -23.135 -73.037 19.622  1.00 89.19  ? 331 ARG A CD  1 
ATOM   5877 N  NE  . ARG B 1 358 ? -22.832 -72.851 21.041  1.00 93.96  ? 331 ARG A NE  1 
ATOM   5878 C  CZ  . ARG B 1 358 ? -23.623 -72.252 21.930  1.00 98.14  ? 331 ARG A CZ  1 
ATOM   5879 N  NH1 . ARG B 1 358 ? -24.817 -71.781 21.591  1.00 107.25 ? 331 ARG A NH1 1 
ATOM   5880 N  NH2 . ARG B 1 358 ? -23.221 -72.141 23.187  1.00 107.35 ? 331 ARG A NH2 1 
ATOM   5881 N  N   . GLU B 1 359 ? -20.382 -71.738 15.390  1.00 94.13  ? 332 GLU A N   1 
ATOM   5882 C  CA  . GLU B 1 359 ? -19.071 -72.151 14.864  1.00 91.53  ? 332 GLU A CA  1 
ATOM   5883 C  C   . GLU B 1 359 ? -18.138 -70.939 14.652  1.00 83.56  ? 332 GLU A C   1 
ATOM   5884 O  O   . GLU B 1 359 ? -16.961 -70.994 14.993  1.00 79.20  ? 332 GLU A O   1 
ATOM   5885 C  CB  . GLU B 1 359 ? -19.233 -72.950 13.559  1.00 87.38  ? 332 GLU A CB  1 
ATOM   5886 N  N   . PHE B 1 360 ? -18.677 -69.849 14.110  1.00 80.96  ? 333 PHE A N   1 
ATOM   5887 C  CA  . PHE B 1 360 ? -17.898 -68.643 13.847  1.00 81.87  ? 333 PHE A CA  1 
ATOM   5888 C  C   . PHE B 1 360 ? -17.301 -68.027 15.120  1.00 77.96  ? 333 PHE A C   1 
ATOM   5889 O  O   . PHE B 1 360 ? -16.158 -67.546 15.144  1.00 67.75  ? 333 PHE A O   1 
ATOM   5890 C  CB  . PHE B 1 360 ? -18.779 -67.624 13.141  1.00 86.44  ? 333 PHE A CB  1 
ATOM   5891 C  CG  . PHE B 1 360 ? -18.106 -66.311 12.911  1.00 95.03  ? 333 PHE A CG  1 
ATOM   5892 C  CD1 . PHE B 1 360 ? -17.438 -66.065 11.720  1.00 97.07  ? 333 PHE A CD1 1 
ATOM   5893 C  CD2 . PHE B 1 360 ? -18.142 -65.313 13.884  1.00 92.95  ? 333 PHE A CD2 1 
ATOM   5894 C  CE1 . PHE B 1 360 ? -16.818 -64.848 11.497  1.00 98.66  ? 333 PHE A CE1 1 
ATOM   5895 C  CE2 . PHE B 1 360 ? -17.521 -64.098 13.671  1.00 93.92  ? 333 PHE A CE2 1 
ATOM   5896 C  CZ  . PHE B 1 360 ? -16.859 -63.865 12.474  1.00 97.78  ? 333 PHE A CZ  1 
ATOM   5897 N  N   . LEU B 1 361 ? -18.100 -68.040 16.177  1.00 82.96  ? 334 LEU A N   1 
ATOM   5898 C  CA  . LEU B 1 361 ? -17.684 -67.529 17.479  1.00 83.96  ? 334 LEU A CA  1 
ATOM   5899 C  C   . LEU B 1 361 ? -16.540 -68.309 18.091  1.00 82.18  ? 334 LEU A C   1 
ATOM   5900 O  O   . LEU B 1 361 ? -15.925 -67.819 19.020  1.00 83.61  ? 334 LEU A O   1 
ATOM   5901 C  CB  . LEU B 1 361 ? -18.853 -67.591 18.468  1.00 90.91  ? 334 LEU A CB  1 
ATOM   5902 C  CG  . LEU B 1 361 ? -19.824 -66.442 18.752  1.00 87.59  ? 334 LEU A CG  1 
ATOM   5903 C  CD1 . LEU B 1 361 ? -19.627 -65.225 17.859  1.00 90.32  ? 334 LEU A CD1 1 
ATOM   5904 C  CD2 . LEU B 1 361 ? -21.242 -66.990 18.677  1.00 82.34  ? 334 LEU A CD2 1 
ATOM   5905 N  N   . LYS B 1 362 ? -16.298 -69.539 17.632  1.00 95.86  ? 335 LYS A N   1 
ATOM   5906 C  CA  . LYS B 1 362 ? -15.220 -70.393 18.192  1.00 93.53  ? 335 LYS A CA  1 
ATOM   5907 C  C   . LYS B 1 362 ? -13.890 -70.269 17.431  1.00 85.65  ? 335 LYS A C   1 
ATOM   5908 O  O   . LYS B 1 362 ? -12.849 -70.688 17.941  1.00 76.26  ? 335 LYS A O   1 
ATOM   5909 C  CB  . LYS B 1 362 ? -15.662 -71.862 18.273  1.00 96.60  ? 335 LYS A CB  1 
ATOM   5910 C  CG  . LYS B 1 362 ? -16.639 -72.167 19.414  1.00 105.07 ? 335 LYS A CG  1 
ATOM   5911 C  CD  . LYS B 1 362 ? -17.238 -73.574 19.301  1.00 104.80 ? 335 LYS A CD  1 
ATOM   5912 C  CE  . LYS B 1 362 ? -18.209 -73.901 20.425  1.00 100.38 ? 335 LYS A CE  1 
ATOM   5913 N  NZ  . LYS B 1 362 ? -18.903 -75.200 20.180  1.00 98.10  ? 335 LYS A NZ  1 
ATOM   5914 N  N   . LYS B 1 363 ? -13.915 -69.664 16.242  1.00 78.87  ? 336 LYS A N   1 
ATOM   5915 C  CA  . LYS B 1 363 ? -12.679 -69.361 15.518  1.00 82.99  ? 336 LYS A CA  1 
ATOM   5916 C  C   . LYS B 1 363 ? -11.932 -68.089 16.024  1.00 86.83  ? 336 LYS A C   1 
ATOM   5917 O  O   . LYS B 1 363 ? -10.989 -67.611 15.373  1.00 83.07  ? 336 LYS A O   1 
ATOM   5918 C  CB  . LYS B 1 363 ? -12.970 -69.257 14.013  1.00 77.88  ? 336 LYS A CB  1 
ATOM   5919 N  N   . VAL B 1 364 ? -12.323 -67.548 17.177  1.00 87.07  ? 337 VAL A N   1 
ATOM   5920 C  CA  . VAL B 1 364 ? -11.715 -66.302 17.651  1.00 98.40  ? 337 VAL A CA  1 
ATOM   5921 C  C   . VAL B 1 364 ? -10.275 -66.605 17.959  1.00 95.02  ? 337 VAL A C   1 
ATOM   5922 O  O   . VAL B 1 364 ? -10.010 -67.619 18.584  1.00 103.90 ? 337 VAL A O   1 
ATOM   5923 C  CB  . VAL B 1 364 ? -12.302 -65.763 18.981  1.00 102.43 ? 337 VAL A CB  1 
ATOM   5924 C  CG1 . VAL B 1 364 ? -12.172 -64.248 19.033  1.00 107.48 ? 337 VAL A CG1 1 
ATOM   5925 C  CG2 . VAL B 1 364 ? -13.739 -66.159 19.178  1.00 99.52  ? 337 VAL A CG2 1 
ATOM   5926 N  N   . HIS B 1 365 ? -9.349  -65.738 17.557  1.00 98.40  ? 338 HIS A N   1 
ATOM   5927 C  CA  . HIS B 1 365 ? -7.937  -65.936 17.921  1.00 104.04 ? 338 HIS A CA  1 
ATOM   5928 C  C   . HIS B 1 365 ? -7.148  -64.636 17.949  1.00 89.98  ? 338 HIS A C   1 
ATOM   5929 O  O   . HIS B 1 365 ? -7.187  -63.879 16.989  1.00 84.43  ? 338 HIS A O   1 
ATOM   5930 C  CB  . HIS B 1 365 ? -7.242  -66.925 16.962  1.00 111.41 ? 338 HIS A CB  1 
ATOM   5931 C  CG  . HIS B 1 365 ? -6.178  -67.748 17.624  1.00 116.88 ? 338 HIS A CG  1 
ATOM   5932 N  ND1 . HIS B 1 365 ? -6.474  -68.812 18.450  1.00 122.67 ? 338 HIS A ND1 1 
ATOM   5933 C  CD2 . HIS B 1 365 ? -4.829  -67.654 17.605  1.00 122.43 ? 338 HIS A CD2 1 
ATOM   5934 C  CE1 . HIS B 1 365 ? -5.353  -69.345 18.902  1.00 124.26 ? 338 HIS A CE1 1 
ATOM   5935 N  NE2 . HIS B 1 365 ? -4.340  -68.659 18.406  1.00 130.82 ? 338 HIS A NE2 1 
ATOM   5936 N  N   . PRO B 1 366 ? -6.401  -64.389 19.037  1.00 89.94  ? 339 PRO A N   1 
ATOM   5937 C  CA  . PRO B 1 366 ? -5.587  -63.162 19.094  1.00 93.28  ? 339 PRO A CA  1 
ATOM   5938 C  C   . PRO B 1 366 ? -4.592  -63.047 17.935  1.00 100.18 ? 339 PRO A C   1 
ATOM   5939 O  O   . PRO B 1 366 ? -4.375  -61.949 17.409  1.00 95.90  ? 339 PRO A O   1 
ATOM   5940 C  CB  . PRO B 1 366 ? -4.857  -63.251 20.446  1.00 91.21  ? 339 PRO A CB  1 
ATOM   5941 C  CG  . PRO B 1 366 ? -5.271  -64.535 21.087  1.00 93.41  ? 339 PRO A CG  1 
ATOM   5942 C  CD  . PRO B 1 366 ? -6.400  -65.142 20.305  1.00 92.55  ? 339 PRO A CD  1 
ATOM   5943 N  N   . ARG B 1 367 ? -3.999  -64.175 17.549  1.00 108.24 ? 340 ARG A N   1 
ATOM   5944 C  CA  . ARG B 1 367 ? -3.163  -64.243 16.350  1.00 108.69 ? 340 ARG A CA  1 
ATOM   5945 C  C   . ARG B 1 367 ? -4.030  -64.176 15.096  1.00 99.70  ? 340 ARG A C   1 
ATOM   5946 O  O   . ARG B 1 367 ? -4.129  -63.121 14.482  1.00 93.18  ? 340 ARG A O   1 
ATOM   5947 C  CB  . ARG B 1 367 ? -2.302  -65.520 16.344  1.00 110.18 ? 340 ARG A CB  1 
ATOM   5948 N  N   . LYS B 1 368 ? -4.679  -65.292 14.755  1.00 110.31 ? 341 LYS A N   1 
ATOM   5949 C  CA  . LYS B 1 368 ? -5.385  -65.472 13.471  1.00 115.94 ? 341 LYS A CA  1 
ATOM   5950 C  C   . LYS B 1 368 ? -6.403  -64.370 13.103  1.00 118.11 ? 341 LYS A C   1 
ATOM   5951 O  O   . LYS B 1 368 ? -6.578  -64.087 11.916  1.00 118.42 ? 341 LYS A O   1 
ATOM   5952 C  CB  . LYS B 1 368 ? -6.059  -66.860 13.418  1.00 110.20 ? 341 LYS A CB  1 
ATOM   5953 N  N   . SER B 1 369 ? -7.066  -63.764 14.098  1.00 114.65 ? 342 SER A N   1 
ATOM   5954 C  CA  . SER B 1 369 ? -8.020  -62.664 13.851  1.00 102.96 ? 342 SER A CA  1 
ATOM   5955 C  C   . SER B 1 369 ? -7.282  -61.333 13.676  1.00 105.98 ? 342 SER A C   1 
ATOM   5956 O  O   . SER B 1 369 ? -7.146  -60.550 14.624  1.00 95.77  ? 342 SER A O   1 
ATOM   5957 C  CB  . SER B 1 369 ? -9.044  -62.545 14.983  1.00 92.12  ? 342 SER A CB  1 
ATOM   5958 O  OG  . SER B 1 369 ? -9.650  -63.788 15.270  1.00 93.75  ? 342 SER A OG  1 
ATOM   5959 N  N   . VAL B 1 370 ? -6.803  -61.086 12.456  1.00 113.87 ? 343 VAL A N   1 
ATOM   5960 C  CA  . VAL B 1 370 ? -6.005  -59.886 12.161  1.00 109.68 ? 343 VAL A CA  1 
ATOM   5961 C  C   . VAL B 1 370 ? -6.867  -58.620 12.179  1.00 102.46 ? 343 VAL A C   1 
ATOM   5962 O  O   . VAL B 1 370 ? -6.386  -57.572 12.599  1.00 90.60  ? 343 VAL A O   1 
ATOM   5963 C  CB  . VAL B 1 370 ? -5.261  -59.994 10.804  1.00 93.15  ? 343 VAL A CB  1 
ATOM   5964 N  N   . HIS B 1 371 ? -8.133  -58.740 11.758  1.00 101.37 ? 344 HIS A N   1 
ATOM   5965 C  CA  . HIS B 1 371 ? -9.033  -57.589 11.558  1.00 101.50 ? 344 HIS A CA  1 
ATOM   5966 C  C   . HIS B 1 371 ? -9.801  -57.103 12.819  1.00 95.36  ? 344 HIS A C   1 
ATOM   5967 O  O   . HIS B 1 371 ? -10.212 -55.948 12.875  1.00 85.53  ? 344 HIS A O   1 
ATOM   5968 C  CB  . HIS B 1 371 ? -10.044 -57.909 10.447  1.00 108.53 ? 344 HIS A CB  1 
ATOM   5969 C  CG  . HIS B 1 371 ? -9.419  -58.307 9.140   1.00 115.54 ? 344 HIS A CG  1 
ATOM   5970 N  ND1 . HIS B 1 371 ? -8.751  -57.414 8.327   1.00 120.68 ? 344 HIS A ND1 1 
ATOM   5971 C  CD2 . HIS B 1 371 ? -9.383  -59.498 8.497   1.00 111.80 ? 344 HIS A CD2 1 
ATOM   5972 C  CE1 . HIS B 1 371 ? -8.324  -58.039 7.245   1.00 117.99 ? 344 HIS A CE1 1 
ATOM   5973 N  NE2 . HIS B 1 371 ? -8.696  -59.304 7.323   1.00 119.46 ? 344 HIS A NE2 1 
ATOM   5974 N  N   . ASN B 1 372 ? -9.980  -57.976 13.812  1.00 85.14  ? 345 ASN A N   1 
ATOM   5975 C  CA  . ASN B 1 372 ? -10.734 -57.673 15.034  1.00 74.57  ? 345 ASN A CA  1 
ATOM   5976 C  C   . ASN B 1 372 ? -9.820  -57.387 16.225  1.00 70.49  ? 345 ASN A C   1 
ATOM   5977 O  O   . ASN B 1 372 ? -9.558  -58.238 17.063  1.00 61.94  ? 345 ASN A O   1 
ATOM   5978 C  CB  . ASN B 1 372 ? -11.669 -58.846 15.353  1.00 72.70  ? 345 ASN A CB  1 
ATOM   5979 C  CG  . ASN B 1 372 ? -12.584 -58.599 16.559  1.00 74.16  ? 345 ASN A CG  1 
ATOM   5980 O  OD1 . ASN B 1 372 ? -12.278 -57.832 17.502  1.00 63.23  ? 345 ASN A OD1 1 
ATOM   5981 N  ND2 . ASN B 1 372 ? -13.723 -59.299 16.545  1.00 73.90  ? 345 ASN A ND2 1 
ATOM   5982 N  N   . GLY B 1 373 ? -9.391  -56.148 16.336  1.00 73.32  ? 346 GLY A N   1 
ATOM   5983 C  CA  . GLY B 1 373 ? -8.485  -55.754 17.404  1.00 74.63  ? 346 GLY A CA  1 
ATOM   5984 C  C   . GLY B 1 373 ? -9.071  -55.757 18.803  1.00 81.65  ? 346 GLY A C   1 
ATOM   5985 O  O   . GLY B 1 373 ? -8.457  -55.209 19.731  1.00 81.31  ? 346 GLY A O   1 
ATOM   5986 N  N   . PHE B 1 374 ? -10.257 -56.339 18.979  1.00 80.04  ? 347 PHE A N   1 
ATOM   5987 C  CA  . PHE B 1 374 ? -10.771 -56.529 20.328  1.00 78.50  ? 347 PHE A CA  1 
ATOM   5988 C  C   . PHE B 1 374 ? -10.464 -57.920 20.848  1.00 78.92  ? 347 PHE A C   1 
ATOM   5989 O  O   . PHE B 1 374 ? -10.639 -58.184 22.037  1.00 85.43  ? 347 PHE A O   1 
ATOM   5990 C  CB  . PHE B 1 374 ? -12.276 -56.257 20.393  1.00 78.44  ? 347 PHE A CB  1 
ATOM   5991 C  CG  . PHE B 1 374 ? -12.642 -54.825 20.131  1.00 66.69  ? 347 PHE A CG  1 
ATOM   5992 C  CD1 . PHE B 1 374 ? -12.419 -53.863 21.090  1.00 67.26  ? 347 PHE A CD1 1 
ATOM   5993 C  CD2 . PHE B 1 374 ? -13.198 -54.451 18.924  1.00 63.62  ? 347 PHE A CD2 1 
ATOM   5994 C  CE1 . PHE B 1 374 ? -12.742 -52.543 20.852  1.00 65.01  ? 347 PHE A CE1 1 
ATOM   5995 C  CE2 . PHE B 1 374 ? -13.532 -53.149 18.677  1.00 61.10  ? 347 PHE A CE2 1 
ATOM   5996 C  CZ  . PHE B 1 374 ? -13.302 -52.189 19.641  1.00 66.76  ? 347 PHE A CZ  1 
ATOM   5997 N  N   . ALA B 1 375 ? -10.002 -58.809 19.972  1.00 80.46  ? 348 ALA A N   1 
ATOM   5998 C  CA  . ALA B 1 375 ? -9.792  -60.213 20.353  1.00 76.67  ? 348 ALA A CA  1 
ATOM   5999 C  C   . ALA B 1 375 ? -8.697  -60.414 21.406  1.00 72.40  ? 348 ALA A C   1 
ATOM   6000 O  O   . ALA B 1 375 ? -8.808  -61.304 22.237  1.00 67.29  ? 348 ALA A O   1 
ATOM   6001 C  CB  . ALA B 1 375 ? -9.504  -61.060 19.128  1.00 72.11  ? 348 ALA A CB  1 
ATOM   6002 N  N   . LYS B 1 376 ? -7.648  -59.594 21.368  1.00 72.21  ? 349 LYS A N   1 
ATOM   6003 C  CA  . LYS B 1 376 ? -6.557  -59.723 22.338  1.00 75.33  ? 349 LYS A CA  1 
ATOM   6004 C  C   . LYS B 1 376 ? -7.082  -59.557 23.755  1.00 82.73  ? 349 LYS A C   1 
ATOM   6005 O  O   . LYS B 1 376 ? -6.863  -60.440 24.602  1.00 92.83  ? 349 LYS A O   1 
ATOM   6006 C  CB  . LYS B 1 376 ? -5.411  -58.734 22.075  1.00 69.43  ? 349 LYS A CB  1 
ATOM   6007 N  N   . GLU B 1 377 ? -7.788  -58.453 24.018  1.00 80.98  ? 350 GLU A N   1 
ATOM   6008 C  CA  . GLU B 1 377 ? -8.365  -58.248 25.352  1.00 79.84  ? 350 GLU A CA  1 
ATOM   6009 C  C   . GLU B 1 377 ? -9.436  -59.281 25.651  1.00 75.02  ? 350 GLU A C   1 
ATOM   6010 O  O   . GLU B 1 377 ? -9.607  -59.684 26.797  1.00 72.79  ? 350 GLU A O   1 
ATOM   6011 C  CB  . GLU B 1 377 ? -8.967  -56.863 25.515  1.00 85.16  ? 350 GLU A CB  1 
ATOM   6012 C  CG  . GLU B 1 377 ? -9.487  -56.596 26.930  1.00 84.46  ? 350 GLU A CG  1 
ATOM   6013 C  CD  . GLU B 1 377 ? -9.924  -55.160 27.120  1.00 85.13  ? 350 GLU A CD  1 
ATOM   6014 O  OE1 . GLU B 1 377 ? -10.360 -54.538 26.116  1.00 83.22  ? 350 GLU A OE1 1 
ATOM   6015 O  OE2 . GLU B 1 377 ? -9.832  -54.661 28.267  1.00 82.64  ? 350 GLU A OE2 1 
ATOM   6016 N  N   . PHE B 1 378 ? -10.166 -59.702 24.628  1.00 72.75  ? 351 PHE A N   1 
ATOM   6017 C  CA  . PHE B 1 378 ? -11.135 -60.764 24.821  1.00 74.40  ? 351 PHE A CA  1 
ATOM   6018 C  C   . PHE B 1 378 ? -10.396 -61.950 25.418  1.00 75.94  ? 351 PHE A C   1 
ATOM   6019 O  O   . PHE B 1 378 ? -10.786 -62.465 26.456  1.00 77.27  ? 351 PHE A O   1 
ATOM   6020 C  CB  . PHE B 1 378 ? -11.815 -61.156 23.500  1.00 72.31  ? 351 PHE A CB  1 
ATOM   6021 C  CG  . PHE B 1 378 ? -12.557 -62.459 23.570  1.00 78.13  ? 351 PHE A CG  1 
ATOM   6022 C  CD1 . PHE B 1 378 ? -13.810 -62.527 24.150  1.00 80.89  ? 351 PHE A CD1 1 
ATOM   6023 C  CD2 . PHE B 1 378 ? -11.990 -63.620 23.084  1.00 83.67  ? 351 PHE A CD2 1 
ATOM   6024 C  CE1 . PHE B 1 378 ? -14.494 -63.728 24.230  1.00 86.68  ? 351 PHE A CE1 1 
ATOM   6025 C  CE2 . PHE B 1 378 ? -12.669 -64.823 23.161  1.00 89.94  ? 351 PHE A CE2 1 
ATOM   6026 C  CZ  . PHE B 1 378 ? -13.923 -64.881 23.735  1.00 86.78  ? 351 PHE A CZ  1 
ATOM   6027 N  N   . TRP B 1 379 ? -9.308  -62.345 24.762  1.00 79.75  ? 352 TRP A N   1 
ATOM   6028 C  CA  . TRP B 1 379 ? -8.557  -63.530 25.139  1.00 82.93  ? 352 TRP A CA  1 
ATOM   6029 C  C   . TRP B 1 379 ? -8.060  -63.434 26.571  1.00 78.13  ? 352 TRP A C   1 
ATOM   6030 O  O   . TRP B 1 379 ? -8.356  -64.294 27.407  1.00 72.58  ? 352 TRP A O   1 
ATOM   6031 C  CB  . TRP B 1 379 ? -7.377  -63.738 24.190  1.00 88.49  ? 352 TRP A CB  1 
ATOM   6032 C  CG  . TRP B 1 379 ? -6.923  -65.162 24.169  1.00 94.69  ? 352 TRP A CG  1 
ATOM   6033 C  CD1 . TRP B 1 379 ? -5.884  -65.703 24.861  1.00 92.09  ? 352 TRP A CD1 1 
ATOM   6034 C  CD2 . TRP B 1 379 ? -7.513  -66.235 23.423  1.00 97.60  ? 352 TRP A CD2 1 
ATOM   6035 N  NE1 . TRP B 1 379 ? -5.788  -67.046 24.598  1.00 91.19  ? 352 TRP A NE1 1 
ATOM   6036 C  CE2 . TRP B 1 379 ? -6.771  -67.400 23.712  1.00 95.64  ? 352 TRP A CE2 1 
ATOM   6037 C  CE3 . TRP B 1 379 ? -8.593  -66.323 22.536  1.00 91.19  ? 352 TRP A CE3 1 
ATOM   6038 C  CZ2 . TRP B 1 379 ? -7.075  -68.646 23.146  1.00 91.17  ? 352 TRP A CZ2 1 
ATOM   6039 C  CZ3 . TRP B 1 379 ? -8.890  -67.554 21.974  1.00 92.01  ? 352 TRP A CZ3 1 
ATOM   6040 C  CH2 . TRP B 1 379 ? -8.132  -68.700 22.284  1.00 90.26  ? 352 TRP A CH2 1 
ATOM   6041 N  N   . GLU B 1 380 ? -7.344  -62.353 26.838  1.00 76.43  ? 353 GLU A N   1 
ATOM   6042 C  CA  . GLU B 1 380 ? -6.824  -62.039 28.171  1.00 83.99  ? 353 GLU A CA  1 
ATOM   6043 C  C   . GLU B 1 380 ? -7.873  -62.063 29.302  1.00 82.26  ? 353 GLU A C   1 
ATOM   6044 O  O   . GLU B 1 380 ? -7.614  -62.559 30.388  1.00 87.91  ? 353 GLU A O   1 
ATOM   6045 C  CB  . GLU B 1 380 ? -6.126  -60.666 28.131  1.00 88.43  ? 353 GLU A CB  1 
ATOM   6046 C  CG  . GLU B 1 380 ? -4.894  -60.634 27.223  1.00 91.17  ? 353 GLU A CG  1 
ATOM   6047 C  CD  . GLU B 1 380 ? -4.233  -59.275 27.131  1.00 94.72  ? 353 GLU A CD  1 
ATOM   6048 O  OE1 . GLU B 1 380 ? -4.958  -58.251 27.125  1.00 102.37 ? 353 GLU A OE1 1 
ATOM   6049 O  OE2 . GLU B 1 380 ? -2.983  -59.239 27.059  1.00 92.23  ? 353 GLU A OE2 1 
ATOM   6050 N  N   . GLU B 1 381 ? -9.054  -61.521 29.054  1.00 85.79  ? 354 GLU A N   1 
ATOM   6051 C  CA  . GLU B 1 381 ? -10.099 -61.492 30.077  1.00 83.61  ? 354 GLU A CA  1 
ATOM   6052 C  C   . GLU B 1 381 ? -10.717 -62.863 30.292  1.00 75.37  ? 354 GLU A C   1 
ATOM   6053 O  O   . GLU B 1 381 ? -11.065 -63.211 31.416  1.00 69.66  ? 354 GLU A O   1 
ATOM   6054 C  CB  . GLU B 1 381 ? -11.186 -60.474 29.700  1.00 83.03  ? 354 GLU A CB  1 
ATOM   6055 C  CG  . GLU B 1 381 ? -10.689 -59.045 29.720  1.00 84.74  ? 354 GLU A CG  1 
ATOM   6056 C  CD  . GLU B 1 381 ? -10.034 -58.695 31.040  1.00 89.19  ? 354 GLU A CD  1 
ATOM   6057 O  OE1 . GLU B 1 381 ? -8.851  -58.280 31.032  1.00 81.74  ? 354 GLU A OE1 1 
ATOM   6058 O  OE2 . GLU B 1 381 ? -10.701 -58.875 32.082  1.00 95.61  ? 354 GLU A OE2 1 
ATOM   6059 N  N   . THR B 1 382 ? -10.872 -63.618 29.207  1.00 73.07  ? 355 THR A N   1 
ATOM   6060 C  CA  . THR B 1 382 ? -11.445 -64.957 29.263  1.00 75.78  ? 355 THR A CA  1 
ATOM   6061 C  C   . THR B 1 382 ? -10.578 -65.895 30.087  1.00 82.97  ? 355 THR A C   1 
ATOM   6062 O  O   . THR B 1 382 ? -11.047 -66.567 30.997  1.00 82.80  ? 355 THR A O   1 
ATOM   6063 C  CB  . THR B 1 382 ? -11.535 -65.576 27.869  1.00 73.66  ? 355 THR A CB  1 
ATOM   6064 O  OG1 . THR B 1 382 ? -12.161 -64.649 26.983  1.00 80.00  ? 355 THR A OG1 1 
ATOM   6065 C  CG2 . THR B 1 382 ? -12.344 -66.870 27.909  1.00 73.06  ? 355 THR A CG2 1 
ATOM   6066 N  N   . PHE B 1 383 ? -9.299  -65.929 29.749  1.00 88.29  ? 356 PHE A N   1 
ATOM   6067 C  CA  . PHE B 1 383 ? -8.375  -66.889 30.325  1.00 87.11  ? 356 PHE A CA  1 
ATOM   6068 C  C   . PHE B 1 383 ? -7.547  -66.306 31.459  1.00 91.65  ? 356 PHE A C   1 
ATOM   6069 O  O   . PHE B 1 383 ? -6.719  -67.003 32.041  1.00 96.91  ? 356 PHE A O   1 
ATOM   6070 C  CB  . PHE B 1 383 ? -7.475  -67.425 29.218  1.00 80.00  ? 356 PHE A CB  1 
ATOM   6071 C  CG  . PHE B 1 383 ? -8.232  -68.120 28.141  1.00 71.06  ? 356 PHE A CG  1 
ATOM   6072 C  CD1 . PHE B 1 383 ? -8.947  -69.260 28.438  1.00 67.06  ? 356 PHE A CD1 1 
ATOM   6073 C  CD2 . PHE B 1 383 ? -8.260  -67.628 26.842  1.00 77.87  ? 356 PHE A CD2 1 
ATOM   6074 C  CE1 . PHE B 1 383 ? -9.660  -69.929 27.458  1.00 66.12  ? 356 PHE A CE1 1 
ATOM   6075 C  CE2 . PHE B 1 383 ? -8.978  -68.292 25.854  1.00 73.91  ? 356 PHE A CE2 1 
ATOM   6076 C  CZ  . PHE B 1 383 ? -9.675  -69.444 26.164  1.00 70.21  ? 356 PHE A CZ  1 
ATOM   6077 N  N   . ASN B 1 384 ? -7.768  -65.032 31.771  1.00 99.12  ? 357 ASN A N   1 
ATOM   6078 C  CA  . ASN B 1 384 ? -7.188  -64.422 32.960  1.00 101.47 ? 357 ASN A CA  1 
ATOM   6079 C  C   . ASN B 1 384 ? -5.657  -64.400 32.874  1.00 102.68 ? 357 ASN A C   1 
ATOM   6080 O  O   . ASN B 1 384 ? -4.969  -64.743 33.833  1.00 105.98 ? 357 ASN A O   1 
ATOM   6081 C  CB  . ASN B 1 384 ? -7.672  -65.199 34.191  1.00 104.08 ? 357 ASN A CB  1 
ATOM   6082 C  CG  . ASN B 1 384 ? -8.067  -64.296 35.336  1.00 111.74 ? 357 ASN A CG  1 
ATOM   6083 O  OD1 . ASN B 1 384 ? -9.200  -64.355 35.814  1.00 118.15 ? 357 ASN A OD1 1 
ATOM   6084 N  ND2 . ASN B 1 384 ? -7.141  -63.454 35.781  1.00 110.36 ? 357 ASN A ND2 1 
ATOM   6085 N  N   . CYS B 1 385 ? -5.133  -63.996 31.715  1.00 106.62 ? 358 CYS A N   1 
ATOM   6086 C  CA  . CYS B 1 385 ? -3.696  -64.104 31.413  1.00 108.10 ? 358 CYS A CA  1 
ATOM   6087 C  C   . CYS B 1 385 ? -3.140  -62.855 30.689  1.00 109.07 ? 358 CYS A C   1 
ATOM   6088 O  O   . CYS B 1 385 ? -3.847  -61.863 30.556  1.00 115.84 ? 358 CYS A O   1 
ATOM   6089 C  CB  . CYS B 1 385 ? -3.411  -65.421 30.652  1.00 108.96 ? 358 CYS A CB  1 
ATOM   6090 S  SG  . CYS B 1 385 ? -4.199  -65.688 29.040  1.00 108.06 ? 358 CYS A SG  1 
ATOM   6091 N  N   . HIS B 1 386 ? -1.869  -62.889 30.281  1.00 117.79 ? 359 HIS A N   1 
ATOM   6092 C  CA  . HIS B 1 386 ? -1.212  -61.765 29.582  1.00 127.09 ? 359 HIS A CA  1 
ATOM   6093 C  C   . HIS B 1 386 ? -0.596  -62.270 28.252  1.00 119.65 ? 359 HIS A C   1 
ATOM   6094 O  O   . HIS B 1 386 ? -0.339  -63.463 28.101  1.00 119.97 ? 359 HIS A O   1 
ATOM   6095 C  CB  . HIS B 1 386 ? -0.166  -61.119 30.515  1.00 136.05 ? 359 HIS A CB  1 
ATOM   6096 C  CG  . HIS B 1 386 ? 0.438   -59.850 29.986  1.00 159.50 ? 359 HIS A CG  1 
ATOM   6097 N  ND1 . HIS B 1 386 ? -0.189  -58.623 30.074  1.00 165.21 ? 359 HIS A ND1 1 
ATOM   6098 C  CD2 . HIS B 1 386 ? 1.628   -59.618 29.377  1.00 167.78 ? 359 HIS A CD2 1 
ATOM   6099 C  CE1 . HIS B 1 386 ? 0.581   -57.695 29.531  1.00 162.59 ? 359 HIS A CE1 1 
ATOM   6100 N  NE2 . HIS B 1 386 ? 1.690   -58.272 29.102  1.00 165.43 ? 359 HIS A NE2 1 
ATOM   6101 N  N   . LEU B 1 387 ? -0.374  -61.377 27.291  1.00 110.70 ? 360 LEU A N   1 
ATOM   6102 C  CA  . LEU B 1 387 ? 0.007   -61.786 25.944  1.00 108.74 ? 360 LEU A CA  1 
ATOM   6103 C  C   . LEU B 1 387 ? 1.422   -61.340 25.527  1.00 120.11 ? 360 LEU A C   1 
ATOM   6104 O  O   . LEU B 1 387 ? 1.780   -60.168 25.660  1.00 119.41 ? 360 LEU A O   1 
ATOM   6105 C  CB  . LEU B 1 387 ? -1.033  -61.251 24.962  1.00 102.34 ? 360 LEU A CB  1 
ATOM   6106 C  CG  . LEU B 1 387 ? -1.591  -62.270 23.979  1.00 106.01 ? 360 LEU A CG  1 
ATOM   6107 C  CD1 . LEU B 1 387 ? -2.196  -63.477 24.685  1.00 106.45 ? 360 LEU A CD1 1 
ATOM   6108 C  CD2 . LEU B 1 387 ? -2.630  -61.593 23.108  1.00 105.48 ? 360 LEU A CD2 1 
ATOM   6109 N  N   . GLN B 1 388 ? 2.214   -62.287 25.015  1.00 127.84 ? 361 GLN A N   1 
ATOM   6110 C  CA  . GLN B 1 388 ? 3.569   -62.015 24.513  1.00 122.54 ? 361 GLN A CA  1 
ATOM   6111 C  C   . GLN B 1 388 ? 3.512   -61.730 23.021  1.00 114.10 ? 361 GLN A C   1 
ATOM   6112 O  O   . GLN B 1 388 ? 3.696   -60.592 22.603  1.00 117.11 ? 361 GLN A O   1 
ATOM   6113 C  CB  . GLN B 1 388 ? 4.506   -63.205 24.777  1.00 114.85 ? 361 GLN A CB  1 
ATOM   6114 N  N   . ARG B 1 419 ? -1.097  -62.752 37.112  1.00 88.56  ? 392 ARG A N   1 
ATOM   6115 C  CA  . ARG B 1 419 ? -0.911  -62.290 35.730  1.00 102.51 ? 392 ARG A CA  1 
ATOM   6116 C  C   . ARG B 1 419 ? 0.002   -63.194 34.854  1.00 102.61 ? 392 ARG A C   1 
ATOM   6117 O  O   . ARG B 1 419 ? 0.906   -62.687 34.182  1.00 108.03 ? 392 ARG A O   1 
ATOM   6118 C  CB  . ARG B 1 419 ? -0.379  -60.844 35.728  1.00 100.04 ? 392 ARG A CB  1 
ATOM   6119 N  N   . PRO B 1 420 ? -0.250  -64.524 34.834  1.00 101.50 ? 393 PRO A N   1 
ATOM   6120 C  CA  . PRO B 1 420 ? 0.510   -65.482 33.995  1.00 101.60 ? 393 PRO A CA  1 
ATOM   6121 C  C   . PRO B 1 420 ? 0.385   -65.226 32.489  1.00 106.66 ? 393 PRO A C   1 
ATOM   6122 O  O   . PRO B 1 420 ? -0.626  -64.695 32.057  1.00 118.75 ? 393 PRO A O   1 
ATOM   6123 C  CB  . PRO B 1 420 ? -0.118  -66.835 34.341  1.00 97.50  ? 393 PRO A CB  1 
ATOM   6124 C  CG  . PRO B 1 420 ? -1.443  -66.518 34.932  1.00 100.03 ? 393 PRO A CG  1 
ATOM   6125 C  CD  . PRO B 1 420 ? -1.278  -65.207 35.639  1.00 102.11 ? 393 PRO A CD  1 
ATOM   6126 N  N   . LEU B 1 421 ? 1.399   -65.595 31.701  1.00 109.51 ? 394 LEU A N   1 
ATOM   6127 C  CA  . LEU B 1 421 ? 1.378   -65.358 30.244  1.00 107.33 ? 394 LEU A CA  1 
ATOM   6128 C  C   . LEU B 1 421 ? 0.564   -66.458 29.546  1.00 109.06 ? 394 LEU A C   1 
ATOM   6129 O  O   . LEU B 1 421 ? 0.479   -67.586 30.046  1.00 100.72 ? 394 LEU A O   1 
ATOM   6130 C  CB  . LEU B 1 421 ? 2.803   -65.259 29.664  1.00 97.77  ? 394 LEU A CB  1 
ATOM   6131 N  N   . CYS B 1 422 ? -0.041  -66.114 28.405  1.00 113.35 ? 395 CYS A N   1 
ATOM   6132 C  CA  . CYS B 1 422 ? -0.962  -67.016 27.698  1.00 123.33 ? 395 CYS A CA  1 
ATOM   6133 C  C   . CYS B 1 422 ? -0.227  -67.903 26.708  1.00 125.17 ? 395 CYS A C   1 
ATOM   6134 O  O   . CYS B 1 422 ? 0.637   -67.431 25.968  1.00 118.47 ? 395 CYS A O   1 
ATOM   6135 C  CB  . CYS B 1 422 ? -2.039  -66.243 26.911  1.00 126.75 ? 395 CYS A CB  1 
ATOM   6136 S  SG  . CYS B 1 422 ? -2.865  -64.857 27.736  1.00 128.67 ? 395 CYS A SG  1 
ATOM   6137 N  N   . THR B 1 423 ? -0.629  -69.173 26.658  1.00 132.66 ? 396 THR A N   1 
ATOM   6138 C  CA  . THR B 1 423 ? -0.054  -70.146 25.716  1.00 126.68 ? 396 THR A CA  1 
ATOM   6139 C  C   . THR B 1 423 ? -0.437  -69.794 24.264  1.00 132.52 ? 396 THR A C   1 
ATOM   6140 O  O   . THR B 1 423 ? 0.314   -70.085 23.327  1.00 135.36 ? 396 THR A O   1 
ATOM   6141 C  CB  . THR B 1 423 ? -0.457  -71.628 26.037  1.00 118.99 ? 396 THR A CB  1 
ATOM   6142 O  OG1 . THR B 1 423 ? -1.668  -71.994 25.356  1.00 109.84 ? 396 THR A OG1 1 
ATOM   6143 C  CG2 . THR B 1 423 ? -0.616  -71.877 27.552  1.00 111.63 ? 396 THR A CG2 1 
ATOM   6144 N  N   . GLY B 1 424 ? -1.601  -69.165 24.087  1.00 134.18 ? 397 GLY A N   1 
ATOM   6145 C  CA  . GLY B 1 424 ? -2.135  -68.877 22.757  1.00 132.06 ? 397 GLY A CA  1 
ATOM   6146 C  C   . GLY B 1 424 ? -2.772  -70.096 22.111  1.00 132.83 ? 397 GLY A C   1 
ATOM   6147 O  O   . GLY B 1 424 ? -3.145  -70.053 20.938  1.00 129.35 ? 397 GLY A O   1 
ATOM   6148 N  N   . ASP B 1 425 ? -2.890  -71.184 22.877  1.00 132.97 ? 398 ASP A N   1 
ATOM   6149 C  CA  . ASP B 1 425 ? -3.450  -72.442 22.388  1.00 132.12 ? 398 ASP A CA  1 
ATOM   6150 C  C   . ASP B 1 425 ? -4.793  -72.761 23.037  1.00 120.39 ? 398 ASP A C   1 
ATOM   6151 O  O   . ASP B 1 425 ? -5.565  -73.555 22.496  1.00 118.87 ? 398 ASP A O   1 
ATOM   6152 C  CB  . ASP B 1 425 ? -2.471  -73.603 22.661  1.00 134.67 ? 398 ASP A CB  1 
ATOM   6153 C  CG  . ASP B 1 425 ? -1.123  -73.435 21.946  1.00 136.43 ? 398 ASP A CG  1 
ATOM   6154 O  OD1 . ASP B 1 425 ? -1.024  -72.644 20.982  1.00 144.29 ? 398 ASP A OD1 1 
ATOM   6155 O  OD2 . ASP B 1 425 ? -0.154  -74.111 22.349  1.00 130.41 ? 398 ASP A OD2 1 
ATOM   6156 N  N   . GLU B 1 426 ? -5.074  -72.121 24.175  1.00 113.55 ? 399 GLU A N   1 
ATOM   6157 C  CA  . GLU B 1 426 ? -6.158  -72.545 25.097  1.00 104.76 ? 399 GLU A CA  1 
ATOM   6158 C  C   . GLU B 1 426 ? -7.568  -72.548 24.492  1.00 93.77  ? 399 GLU A C   1 
ATOM   6159 O  O   . GLU B 1 426 ? -7.812  -71.968 23.431  1.00 92.53  ? 399 GLU A O   1 
ATOM   6160 C  CB  . GLU B 1 426 ? -6.133  -71.753 26.432  1.00 101.98 ? 399 GLU A CB  1 
ATOM   6161 C  CG  . GLU B 1 426 ? -5.802  -70.260 26.339  1.00 102.65 ? 399 GLU A CG  1 
ATOM   6162 C  CD  . GLU B 1 426 ? -4.377  -69.900 26.768  1.00 99.38  ? 399 GLU A CD  1 
ATOM   6163 O  OE1 . GLU B 1 426 ? -3.973  -70.316 27.886  1.00 93.71  ? 399 GLU A OE1 1 
ATOM   6164 O  OE2 . GLU B 1 426 ? -3.682  -69.174 25.999  1.00 86.96  ? 399 GLU A OE2 1 
ATOM   6165 N  N   . ASN B 1 427 ? -8.481  -73.232 25.174  1.00 89.91  ? 400 ASN A N   1 
ATOM   6166 C  CA  . ASN B 1 427 ? -9.800  -73.533 24.615  1.00 98.92  ? 400 ASN A CA  1 
ATOM   6167 C  C   . ASN B 1 427 ? -10.910 -72.605 25.144  1.00 103.69 ? 400 ASN A C   1 
ATOM   6168 O  O   . ASN B 1 427 ? -11.174 -72.543 26.353  1.00 94.47  ? 400 ASN A O   1 
ATOM   6169 C  CB  . ASN B 1 427 ? -10.159 -75.001 24.889  1.00 97.71  ? 400 ASN A CB  1 
ATOM   6170 C  CG  . ASN B 1 427 ? -11.221 -75.537 23.942  1.00 99.11  ? 400 ASN A CG  1 
ATOM   6171 O  OD1 . ASN B 1 427 ? -12.373 -75.752 24.333  1.00 104.29 ? 400 ASN A OD1 1 
ATOM   6172 N  ND2 . ASN B 1 427 ? -10.834 -75.762 22.691  1.00 103.63 ? 400 ASN A ND2 1 
ATOM   6173 N  N   . ILE B 1 428 ? -11.550 -71.885 24.226  1.00 101.73 ? 401 ILE A N   1 
ATOM   6174 C  CA  . ILE B 1 428 ? -12.727 -71.074 24.543  1.00 104.27 ? 401 ILE A CA  1 
ATOM   6175 C  C   . ILE B 1 428 ? -13.850 -71.878 25.195  1.00 98.30  ? 401 ILE A C   1 
ATOM   6176 O  O   . ILE B 1 428 ? -14.521 -71.375 26.097  1.00 91.60  ? 401 ILE A O   1 
ATOM   6177 C  CB  . ILE B 1 428 ? -13.285 -70.401 23.273  1.00 110.08 ? 401 ILE A CB  1 
ATOM   6178 C  CG1 . ILE B 1 428 ? -12.461 -69.156 22.943  1.00 114.16 ? 401 ILE A CG1 1 
ATOM   6179 C  CG2 . ILE B 1 428 ? -14.757 -70.031 23.440  1.00 111.59 ? 401 ILE A CG2 1 
ATOM   6180 C  CD1 . ILE B 1 428 ? -12.559 -68.725 21.494  1.00 117.66 ? 401 ILE A CD1 1 
ATOM   6181 N  N   . SER B 1 429 ? -14.052 -73.113 24.735  1.00 94.75  ? 402 SER A N   1 
ATOM   6182 C  CA  . SER B 1 429 ? -15.135 -73.958 25.234  1.00 89.14  ? 402 SER A CA  1 
ATOM   6183 C  C   . SER B 1 429 ? -14.885 -74.500 26.663  1.00 90.63  ? 402 SER A C   1 
ATOM   6184 O  O   . SER B 1 429 ? -15.726 -75.249 27.181  1.00 93.86  ? 402 SER A O   1 
ATOM   6185 C  CB  . SER B 1 429 ? -15.427 -75.093 24.239  1.00 77.41  ? 402 SER A CB  1 
ATOM   6186 N  N   . SER B 1 430 ? -13.767 -74.110 27.299  1.00 83.89  ? 403 SER A N   1 
ATOM   6187 C  CA  . SER B 1 430 ? -13.487 -74.474 28.705  1.00 91.96  ? 403 SER A CA  1 
ATOM   6188 C  C   . SER B 1 430 ? -14.069 -73.519 29.758  1.00 101.28 ? 403 SER A C   1 
ATOM   6189 O  O   . SER B 1 430 ? -14.609 -73.984 30.775  1.00 91.42  ? 403 SER A O   1 
ATOM   6190 C  CB  . SER B 1 430 ? -11.975 -74.630 28.953  1.00 92.14  ? 403 SER A CB  1 
ATOM   6191 O  OG  . SER B 1 430 ? -11.243 -73.472 28.598  1.00 89.10  ? 403 SER A OG  1 
ATOM   6192 N  N   . VAL B 1 431 ? -13.945 -72.203 29.516  1.00 112.76 ? 404 VAL A N   1 
ATOM   6193 C  CA  . VAL B 1 431 ? -14.368 -71.149 30.476  1.00 114.21 ? 404 VAL A CA  1 
ATOM   6194 C  C   . VAL B 1 431 ? -15.830 -70.718 30.235  1.00 109.22 ? 404 VAL A C   1 
ATOM   6195 O  O   . VAL B 1 431 ? -16.232 -70.491 29.091  1.00 111.86 ? 404 VAL A O   1 
ATOM   6196 C  CB  . VAL B 1 431 ? -13.462 -69.884 30.405  1.00 119.72 ? 404 VAL A CB  1 
ATOM   6197 C  CG1 . VAL B 1 431 ? -13.668 -68.997 31.633  1.00 121.59 ? 404 VAL A CG1 1 
ATOM   6198 C  CG2 . VAL B 1 431 ? -11.990 -70.258 30.275  1.00 119.01 ? 404 VAL A CG2 1 
ATOM   6199 N  N   . GLU B 1 432 ? -16.620 -70.610 31.307  1.00 96.25  ? 405 GLU A N   1 
ATOM   6200 C  CA  . GLU B 1 432 ? -18.023 -70.210 31.187  1.00 95.32  ? 405 GLU A CA  1 
ATOM   6201 C  C   . GLU B 1 432 ? -18.126 -68.676 31.270  1.00 92.49  ? 405 GLU A C   1 
ATOM   6202 O  O   . GLU B 1 432 ? -17.894 -68.084 32.341  1.00 79.63  ? 405 GLU A O   1 
ATOM   6203 C  CB  . GLU B 1 432 ? -18.883 -70.879 32.272  1.00 87.43  ? 405 GLU A CB  1 
ATOM   6204 N  N   . THR B 1 433 ? -18.426 -68.054 30.119  1.00 82.27  ? 406 THR A N   1 
ATOM   6205 C  CA  . THR B 1 433 ? -18.763 -66.624 30.020  1.00 72.64  ? 406 THR A CA  1 
ATOM   6206 C  C   . THR B 1 433 ? -19.916 -66.430 29.027  1.00 71.67  ? 406 THR A C   1 
ATOM   6207 O  O   . THR B 1 433 ? -20.131 -67.274 28.167  1.00 82.47  ? 406 THR A O   1 
ATOM   6208 C  CB  . THR B 1 433 ? -17.570 -65.751 29.541  1.00 70.58  ? 406 THR A CB  1 
ATOM   6209 O  OG1 . THR B 1 433 ? -17.373 -65.910 28.128  1.00 69.77  ? 406 THR A OG1 1 
ATOM   6210 C  CG2 . THR B 1 433 ? -16.292 -66.074 30.303  1.00 68.89  ? 406 THR A CG2 1 
ATOM   6211 N  N   . PRO B 1 434 ? -20.639 -65.295 29.114  1.00 72.14  ? 407 PRO A N   1 
ATOM   6212 C  CA  . PRO B 1 434 ? -21.767 -65.010 28.218  1.00 67.59  ? 407 PRO A CA  1 
ATOM   6213 C  C   . PRO B 1 434 ? -21.449 -65.044 26.734  1.00 71.90  ? 407 PRO A C   1 
ATOM   6214 O  O   . PRO B 1 434 ? -22.368 -65.138 25.924  1.00 78.97  ? 407 PRO A O   1 
ATOM   6215 C  CB  . PRO B 1 434 ? -22.156 -63.588 28.601  1.00 68.95  ? 407 PRO A CB  1 
ATOM   6216 C  CG  . PRO B 1 434 ? -21.710 -63.436 30.014  1.00 66.99  ? 407 PRO A CG  1 
ATOM   6217 C  CD  . PRO B 1 434 ? -20.437 -64.205 30.092  1.00 70.73  ? 407 PRO A CD  1 
ATOM   6218 N  N   . TYR B 1 435 ? -20.173 -64.944 26.377  1.00 70.46  ? 408 TYR A N   1 
ATOM   6219 C  CA  . TYR B 1 435 ? -19.749 -65.009 24.979  1.00 71.85  ? 408 TYR A CA  1 
ATOM   6220 C  C   . TYR B 1 435 ? -20.285 -66.215 24.259  1.00 75.62  ? 408 TYR A C   1 
ATOM   6221 O  O   . TYR B 1 435 ? -20.697 -66.124 23.113  1.00 79.39  ? 408 TYR A O   1 
ATOM   6222 C  CB  . TYR B 1 435 ? -18.227 -65.059 24.885  1.00 71.52  ? 408 TYR A CB  1 
ATOM   6223 C  CG  . TYR B 1 435 ? -17.716 -65.114 23.467  1.00 71.27  ? 408 TYR A CG  1 
ATOM   6224 C  CD1 . TYR B 1 435 ? -18.021 -64.107 22.580  1.00 77.41  ? 408 TYR A CD1 1 
ATOM   6225 C  CD2 . TYR B 1 435 ? -16.914 -66.160 23.013  1.00 73.39  ? 408 TYR A CD2 1 
ATOM   6226 C  CE1 . TYR B 1 435 ? -17.560 -64.133 21.279  1.00 76.48  ? 408 TYR A CE1 1 
ATOM   6227 C  CE2 . TYR B 1 435 ? -16.437 -66.186 21.711  1.00 68.93  ? 408 TYR A CE2 1 
ATOM   6228 C  CZ  . TYR B 1 435 ? -16.767 -65.164 20.852  1.00 69.09  ? 408 TYR A CZ  1 
ATOM   6229 O  OH  . TYR B 1 435 ? -16.342 -65.118 19.556  1.00 63.43  ? 408 TYR A OH  1 
ATOM   6230 N  N   . ILE B 1 436 ? -20.227 -67.359 24.927  1.00 88.47  ? 409 ILE A N   1 
ATOM   6231 C  CA  . ILE B 1 436 ? -20.729 -68.609 24.361  1.00 93.95  ? 409 ILE A CA  1 
ATOM   6232 C  C   . ILE B 1 436 ? -21.835 -69.214 25.209  1.00 83.94  ? 409 ILE A C   1 
ATOM   6233 O  O   . ILE B 1 436 ? -22.691 -69.907 24.682  1.00 83.08  ? 409 ILE A O   1 
ATOM   6234 C  CB  . ILE B 1 436 ? -19.569 -69.626 24.141  1.00 106.95 ? 409 ILE A CB  1 
ATOM   6235 C  CG1 . ILE B 1 436 ? -19.528 -70.067 22.685  1.00 109.30 ? 409 ILE A CG1 1 
ATOM   6236 C  CG2 . ILE B 1 436 ? -19.645 -70.840 25.074  1.00 111.91 ? 409 ILE A CG2 1 
ATOM   6237 C  CD1 . ILE B 1 436 ? -19.042 -68.976 21.757  1.00 110.65 ? 409 ILE A CD1 1 
ATOM   6238 N  N   . ASP B 1 437 ? -21.810 -68.968 26.515  1.00 80.98  ? 410 ASP A N   1 
ATOM   6239 C  CA  . ASP B 1 437 ? -22.813 -69.515 27.412  1.00 89.36  ? 410 ASP A CA  1 
ATOM   6240 C  C   . ASP B 1 437 ? -24.126 -68.755 27.245  1.00 87.58  ? 410 ASP A C   1 
ATOM   6241 O  O   . ASP B 1 437 ? -24.431 -67.824 27.989  1.00 99.42  ? 410 ASP A O   1 
ATOM   6242 C  CB  . ASP B 1 437 ? -22.321 -69.449 28.868  1.00 95.50  ? 410 ASP A CB  1 
ATOM   6243 C  CG  . ASP B 1 437 ? -23.244 -70.176 29.839  1.00 95.66  ? 410 ASP A CG  1 
ATOM   6244 O  OD1 . ASP B 1 437 ? -24.091 -70.965 29.360  1.00 96.37  ? 410 ASP A OD1 1 
ATOM   6245 O  OD2 . ASP B 1 437 ? -23.114 -69.964 31.073  1.00 95.03  ? 410 ASP A OD2 1 
ATOM   6246 N  N   . TYR B 1 438 ? -24.884 -69.153 26.235  1.00 84.34  ? 411 TYR A N   1 
ATOM   6247 C  CA  . TYR B 1 438 ? -26.205 -68.590 25.955  1.00 79.64  ? 411 TYR A CA  1 
ATOM   6248 C  C   . TYR B 1 438 ? -26.982 -69.692 25.273  1.00 82.86  ? 411 TYR A C   1 
ATOM   6249 O  O   . TYR B 1 438 ? -26.383 -70.564 24.612  1.00 78.65  ? 411 TYR A O   1 
ATOM   6250 C  CB  . TYR B 1 438 ? -26.120 -67.417 24.980  1.00 74.99  ? 411 TYR A CB  1 
ATOM   6251 C  CG  . TYR B 1 438 ? -25.684 -67.837 23.568  1.00 71.73  ? 411 TYR A CG  1 
ATOM   6252 C  CD1 . TYR B 1 438 ? -26.604 -68.387 22.647  1.00 65.85  ? 411 TYR A CD1 1 
ATOM   6253 C  CD2 . TYR B 1 438 ? -24.350 -67.697 23.159  1.00 65.58  ? 411 TYR A CD2 1 
ATOM   6254 C  CE1 . TYR B 1 438 ? -26.208 -68.758 21.363  1.00 63.48  ? 411 TYR A CE1 1 
ATOM   6255 C  CE2 . TYR B 1 438 ? -23.947 -68.071 21.882  1.00 63.99  ? 411 TYR A CE2 1 
ATOM   6256 C  CZ  . TYR B 1 438 ? -24.869 -68.602 20.985  1.00 62.48  ? 411 TYR A CZ  1 
ATOM   6257 O  OH  . TYR B 1 438 ? -24.441 -68.988 19.723  1.00 57.28  ? 411 TYR A OH  1 
ATOM   6258 N  N   . THR B 1 439 ? -28.303 -69.621 25.394  1.00 82.67  ? 412 THR A N   1 
ATOM   6259 C  CA  . THR B 1 439 ? -29.195 -70.548 24.706  1.00 83.47  ? 412 THR A CA  1 
ATOM   6260 C  C   . THR B 1 439 ? -29.848 -69.873 23.505  1.00 78.55  ? 412 THR A C   1 
ATOM   6261 O  O   . THR B 1 439 ? -29.797 -70.416 22.430  1.00 77.55  ? 412 THR A O   1 
ATOM   6262 C  CB  . THR B 1 439 ? -30.277 -71.177 25.621  1.00 91.06  ? 412 THR A CB  1 
ATOM   6263 O  OG1 . THR B 1 439 ? -31.558 -70.998 25.005  1.00 97.89  ? 412 THR A OG1 1 
ATOM   6264 C  CG2 . THR B 1 439 ? -30.293 -70.580 27.072  1.00 88.22  ? 412 THR A CG2 1 
ATOM   6265 N  N   . HIS B 1 440 ? -30.443 -68.693 23.683  1.00 79.88  ? 413 HIS A N   1 
ATOM   6266 C  CA  . HIS B 1 440 ? -31.119 -67.991 22.575  1.00 80.15  ? 413 HIS A CA  1 
ATOM   6267 C  C   . HIS B 1 440 ? -30.370 -66.763 22.048  1.00 72.13  ? 413 HIS A C   1 
ATOM   6268 O  O   . HIS B 1 440 ? -29.739 -66.044 22.798  1.00 71.81  ? 413 HIS A O   1 
ATOM   6269 C  CB  . HIS B 1 440 ? -32.493 -67.489 22.998  1.00 83.92  ? 413 HIS A CB  1 
ATOM   6270 C  CG  . HIS B 1 440 ? -33.352 -68.514 23.651  1.00 92.96  ? 413 HIS A CG  1 
ATOM   6271 N  ND1 . HIS B 1 440 ? -34.224 -69.312 22.942  1.00 95.88  ? 413 HIS A ND1 1 
ATOM   6272 C  CD2 . HIS B 1 440 ? -33.514 -68.837 24.956  1.00 90.60  ? 413 HIS A CD2 1 
ATOM   6273 C  CE1 . HIS B 1 440 ? -34.869 -70.100 23.783  1.00 99.15  ? 413 HIS A CE1 1 
ATOM   6274 N  NE2 . HIS B 1 440 ? -34.458 -69.830 25.010  1.00 92.97  ? 413 HIS A NE2 1 
ATOM   6275 N  N   . LEU B 1 441 ? -30.506 -66.503 20.754  1.00 71.43  ? 414 LEU A N   1 
ATOM   6276 C  CA  . LEU B 1 441 ? -29.992 -65.290 20.145  1.00 68.22  ? 414 LEU A CA  1 
ATOM   6277 C  C   . LEU B 1 441 ? -31.155 -64.305 19.945  1.00 68.31  ? 414 LEU A C   1 
ATOM   6278 O  O   . LEU B 1 441 ? -32.056 -64.542 19.126  1.00 59.41  ? 414 LEU A O   1 
ATOM   6279 C  CB  . LEU B 1 441 ? -29.321 -65.599 18.799  1.00 72.84  ? 414 LEU A CB  1 
ATOM   6280 C  CG  . LEU B 1 441 ? -28.066 -66.485 18.743  1.00 70.23  ? 414 LEU A CG  1 
ATOM   6281 C  CD1 . LEU B 1 441 ? -27.606 -66.603 17.295  1.00 76.87  ? 414 LEU A CD1 1 
ATOM   6282 C  CD2 . LEU B 1 441 ? -26.932 -65.922 19.583  1.00 74.31  ? 414 LEU A CD2 1 
ATOM   6283 N  N   . ARG B 1 442 ? -31.115 -63.209 20.712  1.00 71.24  ? 415 ARG A N   1 
ATOM   6284 C  CA  . ARG B 1 442 ? -32.123 -62.148 20.698  1.00 62.95  ? 415 ARG A CA  1 
ATOM   6285 C  C   . ARG B 1 442 ? -31.551 -60.806 20.201  1.00 62.68  ? 415 ARG A C   1 
ATOM   6286 O  O   . ARG B 1 442 ? -31.787 -60.424 19.042  1.00 63.11  ? 415 ARG A O   1 
ATOM   6287 C  CB  . ARG B 1 442 ? -32.743 -62.037 22.080  1.00 63.19  ? 415 ARG A CB  1 
ATOM   6288 C  CG  . ARG B 1 442 ? -33.387 -63.338 22.521  1.00 64.50  ? 415 ARG A CG  1 
ATOM   6289 C  CD  . ARG B 1 442 ? -34.382 -63.143 23.646  1.00 68.61  ? 415 ARG A CD  1 
ATOM   6290 N  NE  . ARG B 1 442 ? -34.330 -64.264 24.592  1.00 75.66  ? 415 ARG A NE  1 
ATOM   6291 C  CZ  . ARG B 1 442 ? -35.276 -65.188 24.778  1.00 80.24  ? 415 ARG A CZ  1 
ATOM   6292 N  NH1 . ARG B 1 442 ? -36.427 -65.175 24.105  1.00 80.45  ? 415 ARG A NH1 1 
ATOM   6293 N  NH2 . ARG B 1 442 ? -35.066 -66.146 25.671  1.00 86.61  ? 415 ARG A NH2 1 
ATOM   6294 N  N   . ILE B 1 443 ? -30.799 -60.083 21.029  1.00 57.71  ? 416 ILE A N   1 
ATOM   6295 C  CA  . ILE B 1 443 ? -30.151 -58.860 20.527  1.00 54.46  ? 416 ILE A CA  1 
ATOM   6296 C  C   . ILE B 1 443 ? -29.205 -59.212 19.374  1.00 53.96  ? 416 ILE A C   1 
ATOM   6297 O  O   . ILE B 1 443 ? -29.171 -58.500 18.382  1.00 52.54  ? 416 ILE A O   1 
ATOM   6298 C  CB  . ILE B 1 443 ? -29.422 -58.068 21.638  1.00 56.62  ? 416 ILE A CB  1 
ATOM   6299 C  CG1 . ILE B 1 443 ? -30.404 -57.635 22.742  1.00 55.92  ? 416 ILE A CG1 1 
ATOM   6300 C  CG2 . ILE B 1 443 ? -28.710 -56.833 21.095  1.00 56.34  ? 416 ILE A CG2 1 
ATOM   6301 C  CD1 . ILE B 1 443 ? -31.617 -56.899 22.252  1.00 52.47  ? 416 ILE A CD1 1 
ATOM   6302 N  N   . SER B 1 444 ? -28.464 -60.318 19.495  1.00 60.53  ? 417 SER A N   1 
ATOM   6303 C  CA  . SER B 1 444 ? -27.522 -60.779 18.442  1.00 56.66  ? 417 SER A CA  1 
ATOM   6304 C  C   . SER B 1 444 ? -28.279 -60.925 17.126  1.00 53.64  ? 417 SER A C   1 
ATOM   6305 O  O   . SER B 1 444 ? -27.817 -60.530 16.054  1.00 53.63  ? 417 SER A O   1 
ATOM   6306 C  CB  . SER B 1 444 ? -26.888 -62.148 18.797  1.00 62.29  ? 417 SER A CB  1 
ATOM   6307 O  OG  . SER B 1 444 ? -26.050 -62.152 19.962  1.00 52.83  ? 417 SER A OG  1 
ATOM   6308 N  N   . TYR B 1 445 ? -29.473 -61.477 17.190  1.00 52.57  ? 418 TYR A N   1 
ATOM   6309 C  CA  . TYR B 1 445 ? -30.266 -61.557 15.975  1.00 54.52  ? 418 TYR A CA  1 
ATOM   6310 C  C   . TYR B 1 445 ? -30.645 -60.183 15.427  1.00 58.68  ? 418 TYR A C   1 
ATOM   6311 O  O   . TYR B 1 445 ? -30.667 -59.984 14.220  1.00 61.95  ? 418 TYR A O   1 
ATOM   6312 C  CB  . TYR B 1 445 ? -31.510 -62.406 16.190  1.00 55.21  ? 418 TYR A CB  1 
ATOM   6313 C  CG  . TYR B 1 445 ? -32.219 -62.715 14.894  1.00 61.96  ? 418 TYR A CG  1 
ATOM   6314 C  CD1 . TYR B 1 445 ? -31.652 -63.581 13.959  1.00 64.58  ? 418 TYR A CD1 1 
ATOM   6315 C  CD2 . TYR B 1 445 ? -33.444 -62.137 14.593  1.00 60.75  ? 418 TYR A CD2 1 
ATOM   6316 C  CE1 . TYR B 1 445 ? -32.297 -63.872 12.777  1.00 69.18  ? 418 TYR A CE1 1 
ATOM   6317 C  CE2 . TYR B 1 445 ? -34.093 -62.428 13.416  1.00 62.84  ? 418 TYR A CE2 1 
ATOM   6318 C  CZ  . TYR B 1 445 ? -33.522 -63.296 12.513  1.00 67.53  ? 418 TYR A CZ  1 
ATOM   6319 O  OH  . TYR B 1 445 ? -34.173 -63.582 11.332  1.00 70.73  ? 418 TYR A OH  1 
ATOM   6320 N  N   . ASN B 1 446 ? -30.962 -59.237 16.309  1.00 61.21  ? 419 ASN A N   1 
ATOM   6321 C  CA  . ASN B 1 446 ? -31.184 -57.855 15.877  1.00 59.23  ? 419 ASN A CA  1 
ATOM   6322 C  C   . ASN B 1 446 ? -29.990 -57.223 15.121  1.00 55.64  ? 419 ASN A C   1 
ATOM   6323 O  O   . ASN B 1 446 ? -30.161 -56.488 14.123  1.00 50.85  ? 419 ASN A O   1 
ATOM   6324 C  CB  . ASN B 1 446 ? -31.563 -57.010 17.087  1.00 58.83  ? 419 ASN A CB  1 
ATOM   6325 C  CG  . ASN B 1 446 ? -32.938 -57.349 17.608  1.00 59.88  ? 419 ASN A CG  1 
ATOM   6326 O  OD1 . ASN B 1 446 ? -33.688 -58.071 16.962  1.00 63.88  ? 419 ASN A OD1 1 
ATOM   6327 N  ND2 . ASN B 1 446 ? -33.282 -56.820 18.775  1.00 63.17  ? 419 ASN A ND2 1 
ATOM   6328 N  N   . VAL B 1 447 ? -28.788 -57.535 15.585  1.00 51.33  ? 420 VAL A N   1 
ATOM   6329 C  CA  . VAL B 1 447 ? -27.575 -56.994 14.984  1.00 52.70  ? 420 VAL A CA  1 
ATOM   6330 C  C   . VAL B 1 447 ? -27.462 -57.499 13.582  1.00 54.91  ? 420 VAL A C   1 
ATOM   6331 O  O   . VAL B 1 447 ? -27.252 -56.727 12.669  1.00 61.68  ? 420 VAL A O   1 
ATOM   6332 C  CB  . VAL B 1 447 ? -26.322 -57.446 15.741  1.00 54.03  ? 420 VAL A CB  1 
ATOM   6333 C  CG1 . VAL B 1 447 ? -25.081 -56.822 15.117  1.00 54.62  ? 420 VAL A CG1 1 
ATOM   6334 C  CG2 . VAL B 1 447 ? -26.461 -57.114 17.225  1.00 55.16  ? 420 VAL A CG2 1 
ATOM   6335 N  N   . TYR B 1 448 ? -27.597 -58.818 13.453  1.00 58.38  ? 421 TYR A N   1 
ATOM   6336 C  CA  . TYR B 1 448 ? -27.650 -59.547 12.186  1.00 57.61  ? 421 TYR A CA  1 
ATOM   6337 C  C   . TYR B 1 448 ? -28.639 -58.914 11.259  1.00 53.78  ? 421 TYR A C   1 
ATOM   6338 O  O   . TYR B 1 448 ? -28.294 -58.579 10.150  1.00 63.66  ? 421 TYR A O   1 
ATOM   6339 C  CB  . TYR B 1 448 ? -28.058 -61.003 12.495  1.00 67.91  ? 421 TYR A CB  1 
ATOM   6340 C  CG  . TYR B 1 448 ? -28.055 -61.996 11.356  1.00 72.51  ? 421 TYR A CG  1 
ATOM   6341 C  CD1 . TYR B 1 448 ? -26.872 -62.620 10.952  1.00 73.91  ? 421 TYR A CD1 1 
ATOM   6342 C  CD2 . TYR B 1 448 ? -29.251 -62.375 10.734  1.00 77.91  ? 421 TYR A CD2 1 
ATOM   6343 C  CE1 . TYR B 1 448 ? -26.875 -63.563 9.929   1.00 77.96  ? 421 TYR A CE1 1 
ATOM   6344 C  CE2 . TYR B 1 448 ? -29.262 -63.305 9.704   1.00 80.59  ? 421 TYR A CE2 1 
ATOM   6345 C  CZ  . TYR B 1 448 ? -28.076 -63.898 9.310   1.00 81.64  ? 421 TYR A CZ  1 
ATOM   6346 O  OH  . TYR B 1 448 ? -28.093 -64.806 8.284   1.00 85.00  ? 421 TYR A OH  1 
ATOM   6347 N  N   . LEU B 1 449 ? -29.868 -58.721 11.720  1.00 56.82  ? 422 LEU A N   1 
ATOM   6348 C  CA  . LEU B 1 449 ? -30.923 -58.156 10.872  1.00 63.08  ? 422 LEU A CA  1 
ATOM   6349 C  C   . LEU B 1 449 ? -30.695 -56.708 10.509  1.00 61.59  ? 422 LEU A C   1 
ATOM   6350 O  O   . LEU B 1 449 ? -31.210 -56.244 9.495   1.00 62.51  ? 422 LEU A O   1 
ATOM   6351 C  CB  . LEU B 1 449 ? -32.286 -58.221 11.550  1.00 68.60  ? 422 LEU A CB  1 
ATOM   6352 C  CG  . LEU B 1 449 ? -33.061 -59.526 11.623  1.00 73.25  ? 422 LEU A CG  1 
ATOM   6353 C  CD1 . LEU B 1 449 ? -34.434 -59.210 12.200  1.00 70.87  ? 422 LEU A CD1 1 
ATOM   6354 C  CD2 . LEU B 1 449 ? -33.190 -60.162 10.247  1.00 78.69  ? 422 LEU A CD2 1 
ATOM   6355 N  N   . ALA B 1 450 ? -29.996 -55.977 11.368  1.00 58.59  ? 423 ALA A N   1 
ATOM   6356 C  CA  . ALA B 1 450 ? -29.714 -54.583 11.084  1.00 60.89  ? 423 ALA A CA  1 
ATOM   6357 C  C   . ALA B 1 450 ? -28.776 -54.524 9.886   1.00 60.08  ? 423 ALA A C   1 
ATOM   6358 O  O   . ALA B 1 450 ? -28.975 -53.726 8.980   1.00 62.62  ? 423 ALA A O   1 
ATOM   6359 C  CB  . ALA B 1 450 ? -29.097 -53.894 12.292  1.00 62.55  ? 423 ALA A CB  1 
ATOM   6360 N  N   . VAL B 1 451 ? -27.772 -55.398 9.881   1.00 62.67  ? 424 VAL A N   1 
ATOM   6361 C  CA  . VAL B 1 451 ? -26.786 -55.484 8.796   1.00 61.32  ? 424 VAL A CA  1 
ATOM   6362 C  C   . VAL B 1 451 ? -27.418 -55.924 7.481   1.00 60.25  ? 424 VAL A C   1 
ATOM   6363 O  O   . VAL B 1 451 ? -27.111 -55.355 6.439   1.00 53.60  ? 424 VAL A O   1 
ATOM   6364 C  CB  . VAL B 1 451 ? -25.695 -56.511 9.117   1.00 61.04  ? 424 VAL A CB  1 
ATOM   6365 C  CG1 . VAL B 1 451 ? -24.824 -56.748 7.906   1.00 65.18  ? 424 VAL A CG1 1 
ATOM   6366 C  CG2 . VAL B 1 451 ? -24.844 -56.032 10.265  1.00 66.73  ? 424 VAL A CG2 1 
ATOM   6367 N  N   . TYR B 1 452 ? -28.274 -56.947 7.526   1.00 57.31  ? 425 TYR A N   1 
ATOM   6368 C  CA  . TYR B 1 452 ? -28.941 -57.405 6.311   1.00 62.34  ? 425 TYR A CA  1 
ATOM   6369 C  C   . TYR B 1 452 ? -29.909 -56.366 5.781   1.00 61.77  ? 425 TYR A C   1 
ATOM   6370 O  O   . TYR B 1 452 ? -30.155 -56.330 4.599   1.00 60.77  ? 425 TYR A O   1 
ATOM   6371 C  CB  . TYR B 1 452 ? -29.671 -58.735 6.520   1.00 69.75  ? 425 TYR A CB  1 
ATOM   6372 C  CG  . TYR B 1 452 ? -28.875 -59.978 6.133   1.00 70.37  ? 425 TYR A CG  1 
ATOM   6373 C  CD1 . TYR B 1 452 ? -29.039 -60.568 4.877   1.00 74.05  ? 425 TYR A CD1 1 
ATOM   6374 C  CD2 . TYR B 1 452 ? -27.989 -60.567 7.022   1.00 67.25  ? 425 TYR A CD2 1 
ATOM   6375 C  CE1 . TYR B 1 452 ? -28.339 -61.701 4.510   1.00 73.98  ? 425 TYR A CE1 1 
ATOM   6376 C  CE2 . TYR B 1 452 ? -27.281 -61.700 6.665   1.00 78.29  ? 425 TYR A CE2 1 
ATOM   6377 C  CZ  . TYR B 1 452 ? -27.458 -62.263 5.407   1.00 80.83  ? 425 TYR A CZ  1 
ATOM   6378 O  OH  . TYR B 1 452 ? -26.747 -63.386 5.045   1.00 83.37  ? 425 TYR A OH  1 
ATOM   6379 N  N   . SER B 1 453 ? -30.461 -55.520 6.646   1.00 67.30  ? 426 SER A N   1 
ATOM   6380 C  CA  . SER B 1 453 ? -31.365 -54.467 6.193   1.00 64.97  ? 426 SER A CA  1 
ATOM   6381 C  C   . SER B 1 453 ? -30.575 -53.428 5.415   1.00 65.42  ? 426 SER A C   1 
ATOM   6382 O  O   . SER B 1 453 ? -31.016 -52.927 4.388   1.00 63.87  ? 426 SER A O   1 
ATOM   6383 C  CB  . SER B 1 453 ? -32.107 -53.833 7.375   1.00 66.56  ? 426 SER A CB  1 
ATOM   6384 O  OG  . SER B 1 453 ? -32.935 -54.790 8.044   1.00 64.63  ? 426 SER A OG  1 
ATOM   6385 N  N   . ILE B 1 454 ? -29.388 -53.108 5.895   1.00 64.17  ? 427 ILE A N   1 
ATOM   6386 C  CA  . ILE B 1 454 ? -28.518 -52.234 5.130   1.00 67.73  ? 427 ILE A CA  1 
ATOM   6387 C  C   . ILE B 1 454 ? -28.239 -52.905 3.774   1.00 69.62  ? 427 ILE A C   1 
ATOM   6388 O  O   . ILE B 1 454 ? -28.442 -52.300 2.711   1.00 66.35  ? 427 ILE A O   1 
ATOM   6389 C  CB  . ILE B 1 454 ? -27.232 -51.902 5.919   1.00 60.58  ? 427 ILE A CB  1 
ATOM   6390 C  CG1 . ILE B 1 454 ? -27.599 -50.976 7.065   1.00 61.86  ? 427 ILE A CG1 1 
ATOM   6391 C  CG2 . ILE B 1 454 ? -26.209 -51.210 5.035   1.00 63.15  ? 427 ILE A CG2 1 
ATOM   6392 C  CD1 . ILE B 1 454 ? -26.548 -50.866 8.143   1.00 64.26  ? 427 ILE A CD1 1 
ATOM   6393 N  N   . ALA B 1 455 ? -27.828 -54.170 3.828   1.00 70.19  ? 428 ALA A N   1 
ATOM   6394 C  CA  . ALA B 1 455 ? -27.558 -54.972 2.622   1.00 72.94  ? 428 ALA A CA  1 
ATOM   6395 C  C   . ALA B 1 455 ? -28.713 -55.018 1.599   1.00 66.85  ? 428 ALA A C   1 
ATOM   6396 O  O   . ALA B 1 455 ? -28.545 -54.660 0.442   1.00 69.37  ? 428 ALA A O   1 
ATOM   6397 C  CB  . ALA B 1 455 ? -27.172 -56.387 3.021   1.00 72.84  ? 428 ALA A CB  1 
ATOM   6398 N  N   . HIS B 1 456 ? -29.875 -55.466 2.036   1.00 61.29  ? 429 HIS A N   1 
ATOM   6399 C  CA  . HIS B 1 456 ? -31.051 -55.496 1.193   1.00 63.69  ? 429 HIS A CA  1 
ATOM   6400 C  C   . HIS B 1 456 ? -31.510 -54.150 0.612   1.00 61.24  ? 429 HIS A C   1 
ATOM   6401 O  O   . HIS B 1 456 ? -32.202 -54.135 -0.402  1.00 59.03  ? 429 HIS A O   1 
ATOM   6402 C  CB  . HIS B 1 456 ? -32.212 -56.159 1.939   1.00 69.24  ? 429 HIS A CB  1 
ATOM   6403 C  CG  . HIS B 1 456 ? -32.124 -57.651 1.957   1.00 76.30  ? 429 HIS A CG  1 
ATOM   6404 N  ND1 . HIS B 1 456 ? -32.427 -58.424 0.854   1.00 83.43  ? 429 HIS A ND1 1 
ATOM   6405 C  CD2 . HIS B 1 456 ? -31.746 -58.511 2.929   1.00 77.42  ? 429 HIS A CD2 1 
ATOM   6406 C  CE1 . HIS B 1 456 ? -32.242 -59.697 1.149   1.00 84.62  ? 429 HIS A CE1 1 
ATOM   6407 N  NE2 . HIS B 1 456 ? -31.824 -59.776 2.401   1.00 88.50  ? 429 HIS A NE2 1 
ATOM   6408 N  N   . ALA B 1 457 ? -31.151 -53.034 1.241   1.00 63.97  ? 430 ALA A N   1 
ATOM   6409 C  CA  . ALA B 1 457 ? -31.476 -51.719 0.687   1.00 66.93  ? 430 ALA A CA  1 
ATOM   6410 C  C   . ALA B 1 457 ? -30.443 -51.345 -0.384  1.00 64.95  ? 430 ALA A C   1 
ATOM   6411 O  O   . ALA B 1 457 ? -30.786 -50.740 -1.400  1.00 68.54  ? 430 ALA A O   1 
ATOM   6412 C  CB  . ALA B 1 457 ? -31.526 -50.660 1.781   1.00 73.07  ? 430 ALA A CB  1 
ATOM   6413 N  N   . LEU B 1 458 ? -29.188 -51.703 -0.152  1.00 62.27  ? 431 LEU A N   1 
ATOM   6414 C  CA  . LEU B 1 458 ? -28.162 -51.632 -1.198  1.00 69.86  ? 431 LEU A CA  1 
ATOM   6415 C  C   . LEU B 1 458 ? -28.478 -52.509 -2.401  1.00 70.92  ? 431 LEU A C   1 
ATOM   6416 O  O   . LEU B 1 458 ? -28.253 -52.096 -3.530  1.00 72.03  ? 431 LEU A O   1 
ATOM   6417 C  CB  . LEU B 1 458 ? -26.793 -52.053 -0.661  1.00 68.01  ? 431 LEU A CB  1 
ATOM   6418 C  CG  . LEU B 1 458 ? -26.111 -51.025 0.235   1.00 69.07  ? 431 LEU A CG  1 
ATOM   6419 C  CD1 . LEU B 1 458 ? -24.866 -51.639 0.866   1.00 68.26  ? 431 LEU A CD1 1 
ATOM   6420 C  CD2 . LEU B 1 458 ? -25.785 -49.739 -0.522  1.00 63.97  ? 431 LEU A CD2 1 
ATOM   6421 N  N   . GLN B 1 459 ? -28.977 -53.719 -2.154  1.00 75.65  ? 432 GLN A N   1 
ATOM   6422 C  CA  . GLN B 1 459 ? -29.351 -54.646 -3.235  1.00 81.45  ? 432 GLN A CA  1 
ATOM   6423 C  C   . GLN B 1 459 ? -30.438 -54.009 -4.082  1.00 77.96  ? 432 GLN A C   1 
ATOM   6424 O  O   . GLN B 1 459 ? -30.388 -54.070 -5.298  1.00 84.00  ? 432 GLN A O   1 
ATOM   6425 C  CB  . GLN B 1 459 ? -29.823 -56.003 -2.668  1.00 85.52  ? 432 GLN A CB  1 
ATOM   6426 C  CG  . GLN B 1 459 ? -30.274 -57.059 -3.683  1.00 88.35  ? 432 GLN A CG  1 
ATOM   6427 C  CD  . GLN B 1 459 ? -29.163 -57.598 -4.595  1.00 90.69  ? 432 GLN A CD  1 
ATOM   6428 O  OE1 . GLN B 1 459 ? -27.960 -57.454 -4.327  1.00 87.11  ? 432 GLN A OE1 1 
ATOM   6429 N  NE2 . GLN B 1 459 ? -29.576 -58.236 -5.686  1.00 88.39  ? 432 GLN A NE2 1 
ATOM   6430 N  N   . ASP B 1 460 ? -31.399 -53.365 -3.434  1.00 75.63  ? 433 ASP A N   1 
ATOM   6431 C  CA  . ASP B 1 460 ? -32.500 -52.746 -4.145  1.00 72.69  ? 433 ASP A CA  1 
ATOM   6432 C  C   . ASP B 1 460 ? -32.063 -51.567 -4.971  1.00 74.39  ? 433 ASP A C   1 
ATOM   6433 O  O   . ASP B 1 460 ? -32.857 -51.054 -5.746  1.00 73.30  ? 433 ASP A O   1 
ATOM   6434 C  CB  . ASP B 1 460 ? -33.588 -52.320 -3.172  1.00 73.20  ? 433 ASP A CB  1 
ATOM   6435 C  CG  . ASP B 1 460 ? -34.350 -53.496 -2.619  1.00 73.74  ? 433 ASP A CG  1 
ATOM   6436 O  OD1 . ASP B 1 460 ? -34.141 -54.630 -3.083  1.00 83.34  ? 433 ASP A OD1 1 
ATOM   6437 O  OD2 . ASP B 1 460 ? -35.176 -53.292 -1.718  1.00 93.67  ? 433 ASP A OD2 1 
ATOM   6438 N  N   . ILE B 1 461 ? -30.818 -51.128 -4.793  1.00 76.94  ? 434 ILE A N   1 
ATOM   6439 C  CA  . ILE B 1 461 ? -30.244 -50.084 -5.630  1.00 83.95  ? 434 ILE A CA  1 
ATOM   6440 C  C   . ILE B 1 461 ? -29.603 -50.704 -6.866  1.00 88.41  ? 434 ILE A C   1 
ATOM   6441 O  O   . ILE B 1 461 ? -29.839 -50.253 -7.989  1.00 89.97  ? 434 ILE A O   1 
ATOM   6442 C  CB  . ILE B 1 461 ? -29.228 -49.228 -4.843  1.00 84.09  ? 434 ILE A CB  1 
ATOM   6443 C  CG1 . ILE B 1 461 ? -29.980 -48.380 -3.807  1.00 80.64  ? 434 ILE A CG1 1 
ATOM   6444 C  CG2 . ILE B 1 461 ? -28.424 -48.320 -5.781  1.00 84.39  ? 434 ILE A CG2 1 
ATOM   6445 C  CD1 . ILE B 1 461 ? -29.092 -47.738 -2.757  1.00 79.57  ? 434 ILE A CD1 1 
ATOM   6446 N  N   . TYR B 1 462 ? -28.791 -51.731 -6.638  1.00 94.69  ? 435 TYR A N   1 
ATOM   6447 C  CA  . TYR B 1 462 ? -28.206 -52.553 -7.701  1.00 100.76 ? 435 TYR A CA  1 
ATOM   6448 C  C   . TYR B 1 462 ? -29.251 -52.914 -8.755  1.00 93.77  ? 435 TYR A C   1 
ATOM   6449 O  O   . TYR B 1 462 ? -29.023 -52.728 -9.944  1.00 94.48  ? 435 TYR A O   1 
ATOM   6450 C  CB  . TYR B 1 462 ? -27.607 -53.839 -7.099  1.00 110.87 ? 435 TYR A CB  1 
ATOM   6451 C  CG  . TYR B 1 462 ? -26.759 -54.679 -8.043  1.00 131.34 ? 435 TYR A CG  1 
ATOM   6452 C  CD1 . TYR B 1 462 ? -25.492 -54.250 -8.448  1.00 141.15 ? 435 TYR A CD1 1 
ATOM   6453 C  CD2 . TYR B 1 462 ? -27.208 -55.921 -8.498  1.00 142.14 ? 435 TYR A CD2 1 
ATOM   6454 C  CE1 . TYR B 1 462 ? -24.712 -55.019 -9.298  1.00 149.85 ? 435 TYR A CE1 1 
ATOM   6455 C  CE2 . TYR B 1 462 ? -26.434 -56.698 -9.348  1.00 144.96 ? 435 TYR A CE2 1 
ATOM   6456 C  CZ  . TYR B 1 462 ? -25.190 -56.243 -9.747  1.00 150.90 ? 435 TYR A CZ  1 
ATOM   6457 O  OH  . TYR B 1 462 ? -24.421 -57.013 -10.590 1.00 149.77 ? 435 TYR A OH  1 
ATOM   6458 N  N   . THR B 1 463 ? -30.410 -53.378 -8.302  1.00 84.46  ? 436 THR A N   1 
ATOM   6459 C  CA  . THR B 1 463 ? -31.442 -53.924 -9.178  1.00 82.52  ? 436 THR A CA  1 
ATOM   6460 C  C   . THR B 1 463 ? -32.556 -52.921 -9.526  1.00 86.84  ? 436 THR A C   1 
ATOM   6461 O  O   . THR B 1 463 ? -33.666 -53.327 -9.865  1.00 90.19  ? 436 THR A O   1 
ATOM   6462 C  CB  . THR B 1 463 ? -32.113 -55.150 -8.519  1.00 76.22  ? 436 THR A CB  1 
ATOM   6463 O  OG1 . THR B 1 463 ? -33.019 -54.720 -7.489  1.00 78.78  ? 436 THR A OG1 1 
ATOM   6464 C  CG2 . THR B 1 463 ? -31.080 -56.085 -7.926  1.00 75.45  ? 436 THR A CG2 1 
ATOM   6465 N  N   . CYS B 1 464 ? -32.284 -51.624 -9.427  1.00 91.87  ? 437 CYS A N   1 
ATOM   6466 C  CA  . CYS B 1 464 ? -33.317 -50.615 -9.695  1.00 96.74  ? 437 CYS A CA  1 
ATOM   6467 C  C   . CYS B 1 464 ? -33.567 -50.537 -11.193 1.00 90.49  ? 437 CYS A C   1 
ATOM   6468 O  O   . CYS B 1 464 ? -32.619 -50.630 -11.981 1.00 88.86  ? 437 CYS A O   1 
ATOM   6469 C  CB  . CYS B 1 464 ? -32.892 -49.233 -9.170  1.00 100.42 ? 437 CYS A CB  1 
ATOM   6470 S  SG  . CYS B 1 464 ? -34.191 -47.969 -9.257  1.00 118.13 ? 437 CYS A SG  1 
ATOM   6471 N  N   . LEU B 1 465 ? -34.829 -50.362 -11.582 1.00 82.38  ? 438 LEU A N   1 
ATOM   6472 C  CA  . LEU B 1 465 ? -35.182 -50.246 -12.998 1.00 86.67  ? 438 LEU A CA  1 
ATOM   6473 C  C   . LEU B 1 465 ? -35.581 -48.828 -13.351 1.00 89.50  ? 438 LEU A C   1 
ATOM   6474 O  O   . LEU B 1 465 ? -36.597 -48.326 -12.866 1.00 89.51  ? 438 LEU A O   1 
ATOM   6475 C  CB  . LEU B 1 465 ? -36.304 -51.211 -13.368 1.00 88.67  ? 438 LEU A CB  1 
ATOM   6476 C  CG  . LEU B 1 465 ? -35.913 -52.687 -13.205 1.00 96.55  ? 438 LEU A CG  1 
ATOM   6477 C  CD1 . LEU B 1 465 ? -37.059 -53.611 -13.626 1.00 94.30  ? 438 LEU A CD1 1 
ATOM   6478 C  CD2 . LEU B 1 465 ? -34.615 -53.004 -13.956 1.00 91.28  ? 438 LEU A CD2 1 
ATOM   6479 N  N   . PRO B 1 466 ? -34.793 -48.177 -14.217 1.00 98.05  ? 439 PRO A N   1 
ATOM   6480 C  CA  . PRO B 1 466 ? -35.028 -46.758 -14.472 1.00 107.20 ? 439 PRO A CA  1 
ATOM   6481 C  C   . PRO B 1 466 ? -36.487 -46.473 -14.813 1.00 102.46 ? 439 PRO A C   1 
ATOM   6482 O  O   . PRO B 1 466 ? -37.051 -47.154 -15.654 1.00 116.31 ? 439 PRO A O   1 
ATOM   6483 C  CB  . PRO B 1 466 ? -34.097 -46.464 -15.650 1.00 111.37 ? 439 PRO A CB  1 
ATOM   6484 C  CG  . PRO B 1 466 ? -32.981 -47.452 -15.483 1.00 107.77 ? 439 PRO A CG  1 
ATOM   6485 C  CD  . PRO B 1 466 ? -33.667 -48.699 -15.019 1.00 101.64 ? 439 PRO A CD  1 
ATOM   6486 N  N   . GLY B 1 467 ? -37.096 -45.505 -14.134 1.00 99.15  ? 440 GLY A N   1 
ATOM   6487 C  CA  . GLY B 1 467 ? -38.528 -45.227 -14.286 1.00 100.06 ? 440 GLY A CA  1 
ATOM   6488 C  C   . GLY B 1 467 ? -39.413 -45.857 -13.206 1.00 106.67 ? 440 GLY A C   1 
ATOM   6489 O  O   . GLY B 1 467 ? -40.460 -45.300 -12.849 1.00 101.60 ? 440 GLY A O   1 
ATOM   6490 N  N   . ARG B 1 468 ? -39.018 -47.020 -12.687 1.00 106.92 ? 441 ARG A N   1 
ATOM   6491 C  CA  . ARG B 1 468 ? -39.760 -47.665 -11.593 1.00 108.62 ? 441 ARG A CA  1 
ATOM   6492 C  C   . ARG B 1 468 ? -39.154 -47.381 -10.188 1.00 108.02 ? 441 ARG A C   1 
ATOM   6493 O  O   . ARG B 1 468 ? -39.696 -47.831 -9.171  1.00 103.96 ? 441 ARG A O   1 
ATOM   6494 C  CB  . ARG B 1 468 ? -39.858 -49.175 -11.860 1.00 101.56 ? 441 ARG A CB  1 
ATOM   6495 N  N   . GLY B 1 469 ? -38.063 -46.610 -10.142 1.00 107.69 ? 442 GLY A N   1 
ATOM   6496 C  CA  . GLY B 1 469 ? -37.324 -46.325 -8.903  1.00 105.08 ? 442 GLY A CA  1 
ATOM   6497 C  C   . GLY B 1 469 ? -37.978 -45.354 -7.926  1.00 106.87 ? 442 GLY A C   1 
ATOM   6498 O  O   . GLY B 1 469 ? -39.137 -44.963 -8.095  1.00 103.79 ? 442 GLY A O   1 
ATOM   6499 N  N   . LEU B 1 470 ? -37.216 -44.958 -6.903  1.00 106.01 ? 443 LEU A N   1 
ATOM   6500 C  CA  . LEU B 1 470 ? -37.749 -44.186 -5.765  1.00 94.73  ? 443 LEU A CA  1 
ATOM   6501 C  C   . LEU B 1 470 ? -37.514 -42.682 -5.831  1.00 86.64  ? 443 LEU A C   1 
ATOM   6502 O  O   . LEU B 1 470 ? -38.211 -41.916 -5.168  1.00 77.96  ? 443 LEU A O   1 
ATOM   6503 C  CB  . LEU B 1 470 ? -37.155 -44.712 -4.464  1.00 89.53  ? 443 LEU A CB  1 
ATOM   6504 C  CG  . LEU B 1 470 ? -37.724 -46.048 -4.000  1.00 89.59  ? 443 LEU A CG  1 
ATOM   6505 C  CD1 . LEU B 1 470 ? -36.889 -46.602 -2.859  1.00 95.17  ? 443 LEU A CD1 1 
ATOM   6506 C  CD2 . LEU B 1 470 ? -39.178 -45.907 -3.576  1.00 81.41  ? 443 LEU A CD2 1 
ATOM   6507 N  N   . PHE B 1 471 ? -36.553 -42.264 -6.641  1.00 87.83  ? 444 PHE A N   1 
ATOM   6508 C  CA  . PHE B 1 471 ? -36.107 -40.877 -6.654  1.00 92.82  ? 444 PHE A CA  1 
ATOM   6509 C  C   . PHE B 1 471 ? -36.847 -39.981 -7.658  1.00 101.26 ? 444 PHE A C   1 
ATOM   6510 O  O   . PHE B 1 471 ? -38.013 -40.241 -7.962  1.00 102.92 ? 444 PHE A O   1 
ATOM   6511 C  CB  . PHE B 1 471 ? -34.595 -40.885 -6.816  1.00 88.42  ? 444 PHE A CB  1 
ATOM   6512 C  CG  . PHE B 1 471 ? -33.921 -41.664 -5.734  1.00 91.43  ? 444 PHE A CG  1 
ATOM   6513 C  CD1 . PHE B 1 471 ? -33.802 -41.129 -4.459  1.00 91.83  ? 444 PHE A CD1 1 
ATOM   6514 C  CD2 . PHE B 1 471 ? -33.490 -42.953 -5.955  1.00 94.70  ? 444 PHE A CD2 1 
ATOM   6515 C  CE1 . PHE B 1 471 ? -33.214 -41.852 -3.445  1.00 91.89  ? 444 PHE A CE1 1 
ATOM   6516 C  CE2 . PHE B 1 471 ? -32.901 -43.686 -4.943  1.00 95.06  ? 444 PHE A CE2 1 
ATOM   6517 C  CZ  . PHE B 1 471 ? -32.763 -43.135 -3.687  1.00 93.32  ? 444 PHE A CZ  1 
ATOM   6518 N  N   . THR B 1 472 ? -36.195 -38.898 -8.097  1.00 114.31 ? 445 THR A N   1 
ATOM   6519 C  CA  . THR B 1 472 ? -36.792 -37.875 -8.972  1.00 119.29 ? 445 THR A CA  1 
ATOM   6520 C  C   . THR B 1 472 ? -37.177 -38.473 -10.318 1.00 126.77 ? 445 THR A C   1 
ATOM   6521 O  O   . THR B 1 472 ? -36.358 -39.149 -10.948 1.00 125.51 ? 445 THR A O   1 
ATOM   6522 C  CB  . THR B 1 472 ? -35.799 -36.703 -9.207  1.00 116.94 ? 445 THR A CB  1 
ATOM   6523 O  OG1 . THR B 1 472 ? -35.652 -35.946 -8.000  1.00 117.12 ? 445 THR A OG1 1 
ATOM   6524 C  CG2 . THR B 1 472 ? -36.263 -35.767 -10.323 1.00 114.28 ? 445 THR A CG2 1 
ATOM   6525 N  N   . ASN B 1 473 ? -38.414 -38.219 -10.754 1.00 131.05 ? 446 ASN A N   1 
ATOM   6526 C  CA  . ASN B 1 473 ? -38.934 -38.767 -12.015 1.00 131.48 ? 446 ASN A CA  1 
ATOM   6527 C  C   . ASN B 1 473 ? -38.642 -40.267 -12.091 1.00 128.82 ? 446 ASN A C   1 
ATOM   6528 O  O   . ASN B 1 473 ? -38.024 -40.754 -13.048 1.00 119.46 ? 446 ASN A O   1 
ATOM   6529 C  CB  . ASN B 1 473 ? -38.325 -38.035 -13.223 1.00 124.37 ? 446 ASN A CB  1 
ATOM   6530 C  CG  . ASN B 1 473 ? -38.624 -36.551 -13.218 1.00 114.49 ? 446 ASN A CG  1 
ATOM   6531 O  OD1 . ASN B 1 473 ? -39.785 -36.139 -13.142 1.00 106.57 ? 446 ASN A OD1 1 
ATOM   6532 N  ND2 . ASN B 1 473 ? -37.576 -35.737 -13.305 1.00 110.91 ? 446 ASN A ND2 1 
ATOM   6533 N  N   . GLY B 1 474 ? -39.052 -40.974 -11.040 1.00 118.49 ? 447 GLY A N   1 
ATOM   6534 C  CA  . GLY B 1 474 ? -38.775 -42.399 -10.875 1.00 109.52 ? 447 GLY A CA  1 
ATOM   6535 C  C   . GLY B 1 474 ? -37.331 -42.847 -11.051 1.00 104.84 ? 447 GLY A C   1 
ATOM   6536 O  O   . GLY B 1 474 ? -37.097 -44.045 -11.184 1.00 111.92 ? 447 GLY A O   1 
ATOM   6537 N  N   . SER B 1 475 ? -36.358 -41.926 -11.039 1.00 93.24  ? 448 SER A N   1 
ATOM   6538 C  CA  . SER B 1 475 ? -34.974 -42.283 -11.402 1.00 92.06  ? 448 SER A CA  1 
ATOM   6539 C  C   . SER B 1 475 ? -34.358 -43.230 -10.385 1.00 86.92  ? 448 SER A C   1 
ATOM   6540 O  O   . SER B 1 475 ? -35.003 -43.602 -9.395  1.00 81.67  ? 448 SER A O   1 
ATOM   6541 C  CB  . SER B 1 475 ? -34.082 -41.042 -11.600 1.00 96.35  ? 448 SER A CB  1 
ATOM   6542 O  OG  . SER B 1 475 ? -33.864 -40.334 -10.394 1.00 105.79 ? 448 SER A OG  1 
ATOM   6543 N  N   . CYS B 1 476 ? -33.122 -43.641 -10.646 1.00 84.38  ? 449 CYS A N   1 
ATOM   6544 C  CA  . CYS B 1 476 ? -32.432 -44.569 -9.771  1.00 89.11  ? 449 CYS A CA  1 
ATOM   6545 C  C   . CYS B 1 476 ? -31.119 -43.949 -9.332  1.00 90.78  ? 449 CYS A C   1 
ATOM   6546 O  O   . CYS B 1 476 ? -30.855 -42.788 -9.638  1.00 88.72  ? 449 CYS A O   1 
ATOM   6547 C  CB  . CYS B 1 476 ? -32.211 -45.914 -10.480 1.00 92.20  ? 449 CYS A CB  1 
ATOM   6548 S  SG  . CYS B 1 476 ? -33.746 -46.785 -10.880 1.00 106.66 ? 449 CYS A SG  1 
ATOM   6549 N  N   . ALA B 1 477 ? -30.312 -44.723 -8.606  1.00 88.99  ? 450 ALA A N   1 
ATOM   6550 C  CA  . ALA B 1 477 ? -29.069 -44.248 -8.042  1.00 89.48  ? 450 ALA A CA  1 
ATOM   6551 C  C   . ALA B 1 477 ? -27.926 -45.150 -8.463  1.00 87.36  ? 450 ALA A C   1 
ATOM   6552 O  O   . ALA B 1 477 ? -28.009 -46.366 -8.339  1.00 87.19  ? 450 ALA A O   1 
ATOM   6553 C  CB  . ALA B 1 477 ? -29.184 -44.233 -6.524  1.00 97.59  ? 450 ALA A CB  1 
ATOM   6554 N  N   . ASP B 1 478 ? -26.846 -44.553 -8.939  1.00 90.26  ? 451 ASP A N   1 
ATOM   6555 C  CA  . ASP B 1 478 ? -25.662 -45.321 -9.281  1.00 98.00  ? 451 ASP A CA  1 
ATOM   6556 C  C   . ASP B 1 478 ? -25.098 -45.968 -8.018  1.00 92.55  ? 451 ASP A C   1 
ATOM   6557 O  O   . ASP B 1 478 ? -24.750 -45.274 -7.071  1.00 102.89 ? 451 ASP A O   1 
ATOM   6558 C  CB  . ASP B 1 478 ? -24.607 -44.427 -9.965  1.00 106.57 ? 451 ASP A CB  1 
ATOM   6559 C  CG  . ASP B 1 478 ? -23.180 -45.004 -9.877  1.00 109.38 ? 451 ASP A CG  1 
ATOM   6560 O  OD1 . ASP B 1 478 ? -22.981 -46.224 -10.107 1.00 92.71  ? 451 ASP A OD1 1 
ATOM   6561 O  OD2 . ASP B 1 478 ? -22.252 -44.226 -9.559  1.00 114.54 ? 451 ASP A OD2 1 
ATOM   6562 N  N   . ILE B 1 479 ? -25.011 -47.296 -8.026  1.00 91.80  ? 452 ILE A N   1 
ATOM   6563 C  CA  . ILE B 1 479 ? -24.426 -48.059 -6.921  1.00 91.38  ? 452 ILE A CA  1 
ATOM   6564 C  C   . ILE B 1 479 ? -22.893 -47.991 -6.871  1.00 98.73  ? 452 ILE A C   1 
ATOM   6565 O  O   . ILE B 1 479 ? -22.288 -48.216 -5.821  1.00 104.70 ? 452 ILE A O   1 
ATOM   6566 C  CB  . ILE B 1 479 ? -24.876 -49.543 -6.939  1.00 93.28  ? 452 ILE A CB  1 
ATOM   6567 C  CG1 . ILE B 1 479 ? -24.465 -50.226 -5.635  1.00 98.63  ? 452 ILE A CG1 1 
ATOM   6568 C  CG2 . ILE B 1 479 ? -24.292 -50.297 -8.130  1.00 90.63  ? 452 ILE A CG2 1 
ATOM   6569 C  CD1 . ILE B 1 479 ? -25.029 -51.612 -5.450  1.00 102.77 ? 452 ILE A CD1 1 
ATOM   6570 N  N   . LYS B 1 480 ? -22.245 -47.709 -7.992  1.00 107.23 ? 453 LYS A N   1 
ATOM   6571 C  CA  . LYS B 1 480 ? -20.794 -47.542 -7.960  1.00 114.20 ? 453 LYS A CA  1 
ATOM   6572 C  C   . LYS B 1 480 ? -20.421 -46.293 -7.145  1.00 115.91 ? 453 LYS A C   1 
ATOM   6573 O  O   . LYS B 1 480 ? -19.387 -46.282 -6.486  1.00 113.19 ? 453 LYS A O   1 
ATOM   6574 C  CB  . LYS B 1 480 ? -20.213 -47.475 -9.377  1.00 119.78 ? 453 LYS A CB  1 
ATOM   6575 N  N   . LYS B 1 481 ? -21.284 -45.271 -7.172  1.00 119.46 ? 454 LYS A N   1 
ATOM   6576 C  CA  . LYS B 1 481 ? -21.064 -43.994 -6.465  1.00 117.24 ? 454 LYS A CA  1 
ATOM   6577 C  C   . LYS B 1 481 ? -22.290 -43.614 -5.587  1.00 106.31 ? 454 LYS A C   1 
ATOM   6578 O  O   . LYS B 1 481 ? -22.871 -42.532 -5.740  1.00 99.13  ? 454 LYS A O   1 
ATOM   6579 C  CB  . LYS B 1 481 ? -20.735 -42.873 -7.476  1.00 103.13 ? 454 LYS A CB  1 
ATOM   6580 N  N   . VAL B 1 482 ? -22.661 -44.497 -4.658  1.00 92.92  ? 455 VAL A N   1 
ATOM   6581 C  CA  . VAL B 1 482 ? -23.864 -44.284 -3.816  1.00 93.53  ? 455 VAL A CA  1 
ATOM   6582 C  C   . VAL B 1 482 ? -23.594 -43.238 -2.749  1.00 91.05  ? 455 VAL A C   1 
ATOM   6583 O  O   . VAL B 1 482 ? -22.452 -43.056 -2.310  1.00 91.29  ? 455 VAL A O   1 
ATOM   6584 C  CB  . VAL B 1 482 ? -24.329 -45.527 -3.005  1.00 93.30  ? 455 VAL A CB  1 
ATOM   6585 C  CG1 . VAL B 1 482 ? -25.846 -45.623 -3.016  1.00 90.99  ? 455 VAL A CG1 1 
ATOM   6586 C  CG2 . VAL B 1 482 ? -23.731 -46.819 -3.512  1.00 97.02  ? 455 VAL A CG2 1 
ATOM   6587 N  N   . GLU B 1 483 ? -24.651 -42.584 -2.292  1.00 84.95  ? 456 GLU A N   1 
ATOM   6588 C  CA  . GLU B 1 483 ? -24.530 -41.655 -1.176  1.00 82.45  ? 456 GLU A CA  1 
ATOM   6589 C  C   . GLU B 1 483 ? -25.473 -42.034 -0.042  1.00 76.11  ? 456 GLU A C   1 
ATOM   6590 O  O   . GLU B 1 483 ? -26.647 -42.359 -0.262  1.00 78.08  ? 456 GLU A O   1 
ATOM   6591 C  CB  . GLU B 1 483 ? -24.780 -40.235 -1.649  1.00 81.38  ? 456 GLU A CB  1 
ATOM   6592 C  CG  . GLU B 1 483 ? -23.772 -39.800 -2.696  1.00 89.58  ? 456 GLU A CG  1 
ATOM   6593 C  CD  . GLU B 1 483 ? -24.133 -38.484 -3.355  1.00 98.46  ? 456 GLU A CD  1 
ATOM   6594 O  OE1 . GLU B 1 483 ? -25.342 -38.214 -3.542  1.00 97.68  ? 456 GLU A OE1 1 
ATOM   6595 O  OE2 . GLU B 1 483 ? -23.199 -37.726 -3.698  1.00 103.48 ? 456 GLU A OE2 1 
ATOM   6596 N  N   . ALA B 1 484 ? -24.941 -41.983 1.174   1.00 71.41  ? 457 ALA A N   1 
ATOM   6597 C  CA  . ALA B 1 484 ? -25.671 -42.373 2.390   1.00 65.76  ? 457 ALA A CA  1 
ATOM   6598 C  C   . ALA B 1 484 ? -27.157 -42.111 2.362   1.00 60.20  ? 457 ALA A C   1 
ATOM   6599 O  O   . ALA B 1 484 ? -27.923 -43.001 2.674   1.00 65.61  ? 457 ALA A O   1 
ATOM   6600 C  CB  . ALA B 1 484 ? -25.078 -41.688 3.586   1.00 65.61  ? 457 ALA A CB  1 
ATOM   6601 N  N   . TRP B 1 485 ? -27.567 -40.908 1.983   1.00 59.86  ? 458 TRP A N   1 
ATOM   6602 C  CA  . TRP B 1 485 ? -29.004 -40.555 1.976   1.00 61.76  ? 458 TRP A CA  1 
ATOM   6603 C  C   . TRP B 1 485 ? -29.851 -41.358 1.007   1.00 61.48  ? 458 TRP A C   1 
ATOM   6604 O  O   . TRP B 1 485 ? -31.085 -41.381 1.125   1.00 58.45  ? 458 TRP A O   1 
ATOM   6605 C  CB  . TRP B 1 485 ? -29.214 -39.069 1.675   1.00 62.25  ? 458 TRP A CB  1 
ATOM   6606 C  CG  . TRP B 1 485 ? -28.824 -38.656 0.291   1.00 66.07  ? 458 TRP A CG  1 
ATOM   6607 C  CD1 . TRP B 1 485 ? -27.572 -38.327 -0.148  1.00 64.26  ? 458 TRP A CD1 1 
ATOM   6608 C  CD2 . TRP B 1 485 ? -29.693 -38.520 -0.836  1.00 65.52  ? 458 TRP A CD2 1 
ATOM   6609 N  NE1 . TRP B 1 485 ? -27.613 -37.991 -1.474  1.00 66.83  ? 458 TRP A NE1 1 
ATOM   6610 C  CE2 . TRP B 1 485 ? -28.905 -38.100 -1.922  1.00 69.54  ? 458 TRP A CE2 1 
ATOM   6611 C  CE3 . TRP B 1 485 ? -31.055 -38.728 -1.036  1.00 66.88  ? 458 TRP A CE3 1 
ATOM   6612 C  CZ2 . TRP B 1 485 ? -29.439 -37.876 -3.192  1.00 67.79  ? 458 TRP A CZ2 1 
ATOM   6613 C  CZ3 . TRP B 1 485 ? -31.583 -38.503 -2.298  1.00 68.72  ? 458 TRP A CZ3 1 
ATOM   6614 C  CH2 . TRP B 1 485 ? -30.773 -38.085 -3.357  1.00 67.22  ? 458 TRP A CH2 1 
ATOM   6615 N  N   . GLN B 1 486 ? -29.206 -41.962 0.013   1.00 66.24  ? 459 GLN A N   1 
ATOM   6616 C  CA  . GLN B 1 486 ? -29.923 -42.851 -0.906  1.00 69.33  ? 459 GLN A CA  1 
ATOM   6617 C  C   . GLN B 1 486 ? -30.247 -44.156 -0.210  1.00 63.27  ? 459 GLN A C   1 
ATOM   6618 O  O   . GLN B 1 486 ? -31.373 -44.652 -0.266  1.00 61.83  ? 459 GLN A O   1 
ATOM   6619 C  CB  . GLN B 1 486 ? -29.121 -43.079 -2.177  1.00 74.21  ? 459 GLN A CB  1 
ATOM   6620 C  CG  . GLN B 1 486 ? -29.254 -41.907 -3.140  1.00 77.00  ? 459 GLN A CG  1 
ATOM   6621 C  CD  . GLN B 1 486 ? -28.077 -41.742 -4.083  1.00 76.72  ? 459 GLN A CD  1 
ATOM   6622 O  OE1 . GLN B 1 486 ? -27.051 -42.443 -3.997  1.00 64.93  ? 459 GLN A OE1 1 
ATOM   6623 N  NE2 . GLN B 1 486 ? -28.218 -40.786 -4.990  1.00 81.97  ? 459 GLN A NE2 1 
ATOM   6624 N  N   . VAL B 1 487 ? -29.276 -44.679 0.510   1.00 54.76  ? 460 VAL A N   1 
ATOM   6625 C  CA  . VAL B 1 487 ? -29.565 -45.806 1.358   1.00 52.75  ? 460 VAL A CA  1 
ATOM   6626 C  C   . VAL B 1 487 ? -30.669 -45.446 2.374   1.00 56.15  ? 460 VAL A C   1 
ATOM   6627 O  O   . VAL B 1 487 ? -31.557 -46.238 2.642   1.00 52.22  ? 460 VAL A O   1 
ATOM   6628 C  CB  . VAL B 1 487 ? -28.320 -46.269 2.093   1.00 52.54  ? 460 VAL A CB  1 
ATOM   6629 C  CG1 . VAL B 1 487 ? -28.576 -47.633 2.685   1.00 54.59  ? 460 VAL A CG1 1 
ATOM   6630 C  CG2 . VAL B 1 487 ? -27.124 -46.295 1.151   1.00 57.23  ? 460 VAL A CG2 1 
ATOM   6631 N  N   . LEU B 1 488 ? -30.617 -44.248 2.953   1.00 65.64  ? 461 LEU A N   1 
ATOM   6632 C  CA  . LEU B 1 488 ? -31.643 -43.857 3.923   1.00 61.57  ? 461 LEU A CA  1 
ATOM   6633 C  C   . LEU B 1 488 ? -32.988 -44.014 3.243   1.00 56.14  ? 461 LEU A C   1 
ATOM   6634 O  O   . LEU B 1 488 ? -33.865 -44.744 3.709   1.00 54.04  ? 461 LEU A O   1 
ATOM   6635 C  CB  . LEU B 1 488 ? -31.462 -42.416 4.417   1.00 60.20  ? 461 LEU A CB  1 
ATOM   6636 C  CG  . LEU B 1 488 ? -31.797 -42.097 5.890   1.00 56.74  ? 461 LEU A CG  1 
ATOM   6637 C  CD1 . LEU B 1 488 ? -32.311 -40.678 6.011   1.00 55.18  ? 461 LEU A CD1 1 
ATOM   6638 C  CD2 . LEU B 1 488 ? -32.805 -43.037 6.520   1.00 56.72  ? 461 LEU A CD2 1 
ATOM   6639 N  N   . LYS B 1 489 ? -33.123 -43.367 2.102   1.00 56.15  ? 462 LYS A N   1 
ATOM   6640 C  CA  . LYS B 1 489 ? -34.357 -43.467 1.325   1.00 63.21  ? 462 LYS A CA  1 
ATOM   6641 C  C   . LYS B 1 489 ? -34.812 -44.916 1.118   1.00 64.43  ? 462 LYS A C   1 
ATOM   6642 O  O   . LYS B 1 489 ? -35.966 -45.272 1.367   1.00 60.56  ? 462 LYS A O   1 
ATOM   6643 C  CB  . LYS B 1 489 ? -34.174 -42.793 -0.020  1.00 61.10  ? 462 LYS A CB  1 
ATOM   6644 C  CG  . LYS B 1 489 ? -35.387 -42.858 -0.905  1.00 64.53  ? 462 LYS A CG  1 
ATOM   6645 C  CD  . LYS B 1 489 ? -36.571 -42.159 -0.292  1.00 66.68  ? 462 LYS A CD  1 
ATOM   6646 C  CE  . LYS B 1 489 ? -37.743 -42.169 -1.248  1.00 68.66  ? 462 LYS A CE  1 
ATOM   6647 N  NZ  . LYS B 1 489 ? -38.765 -41.147 -0.892  1.00 74.43  ? 462 LYS A NZ  1 
ATOM   6648 N  N   . HIS B 1 490 ? -33.893 -45.756 0.677   1.00 62.27  ? 463 HIS A N   1 
ATOM   6649 C  CA  . HIS B 1 490 ? -34.250 -47.131 0.434   1.00 63.26  ? 463 HIS A CA  1 
ATOM   6650 C  C   . HIS B 1 490 ? -34.591 -47.856 1.717   1.00 61.31  ? 463 HIS A C   1 
ATOM   6651 O  O   . HIS B 1 490 ? -35.519 -48.644 1.740   1.00 68.90  ? 463 HIS A O   1 
ATOM   6652 C  CB  . HIS B 1 490 ? -33.162 -47.861 -0.367  1.00 69.14  ? 463 HIS A CB  1 
ATOM   6653 C  CG  . HIS B 1 490 ? -33.376 -47.776 -1.847  1.00 73.85  ? 463 HIS A CG  1 
ATOM   6654 N  ND1 . HIS B 1 490 ? -34.166 -48.671 -2.534  1.00 75.17  ? 463 HIS A ND1 1 
ATOM   6655 C  CD2 . HIS B 1 490 ? -32.948 -46.870 -2.759  1.00 76.36  ? 463 HIS A CD2 1 
ATOM   6656 C  CE1 . HIS B 1 490 ? -34.202 -48.327 -3.809  1.00 81.97  ? 463 HIS A CE1 1 
ATOM   6657 N  NE2 . HIS B 1 490 ? -33.467 -47.241 -3.973  1.00 79.81  ? 463 HIS A NE2 1 
ATOM   6658 N  N   . LEU B 1 491 ? -33.862 -47.584 2.786   1.00 59.37  ? 464 LEU A N   1 
ATOM   6659 C  CA  . LEU B 1 491 ? -34.192 -48.175 4.060   1.00 59.19  ? 464 LEU A CA  1 
ATOM   6660 C  C   . LEU B 1 491 ? -35.616 -47.797 4.531   1.00 61.25  ? 464 LEU A C   1 
ATOM   6661 O  O   . LEU B 1 491 ? -36.337 -48.632 5.100   1.00 63.95  ? 464 LEU A O   1 
ATOM   6662 C  CB  . LEU B 1 491 ? -33.158 -47.782 5.096   1.00 57.16  ? 464 LEU A CB  1 
ATOM   6663 C  CG  . LEU B 1 491 ? -31.902 -48.619 5.020   1.00 57.93  ? 464 LEU A CG  1 
ATOM   6664 C  CD1 . LEU B 1 491 ? -30.817 -47.921 5.818   1.00 59.03  ? 464 LEU A CD1 1 
ATOM   6665 C  CD2 . LEU B 1 491 ? -32.137 -50.042 5.524   1.00 56.27  ? 464 LEU A CD2 1 
ATOM   6666 N  N   . ARG B 1 492 ? -36.052 -46.574 4.268   1.00 57.27  ? 465 ARG A N   1 
ATOM   6667 C  CA  . ARG B 1 492 ? -37.407 -46.188 4.689   1.00 60.79  ? 465 ARG A CA  1 
ATOM   6668 C  C   . ARG B 1 492 ? -38.443 -47.044 4.022   1.00 61.71  ? 465 ARG A C   1 
ATOM   6669 O  O   . ARG B 1 492 ? -39.487 -47.302 4.615   1.00 63.86  ? 465 ARG A O   1 
ATOM   6670 C  CB  . ARG B 1 492 ? -37.732 -44.724 4.373   1.00 65.67  ? 465 ARG A CB  1 
ATOM   6671 C  CG  . ARG B 1 492 ? -36.788 -43.738 5.025   1.00 66.64  ? 465 ARG A CG  1 
ATOM   6672 C  CD  . ARG B 1 492 ? -37.381 -42.350 5.037   1.00 72.20  ? 465 ARG A CD  1 
ATOM   6673 N  NE  . ARG B 1 492 ? -36.541 -41.475 5.849   1.00 72.37  ? 465 ARG A NE  1 
ATOM   6674 C  CZ  . ARG B 1 492 ? -36.534 -40.150 5.775   1.00 68.52  ? 465 ARG A CZ  1 
ATOM   6675 N  NH1 . ARG B 1 492 ? -37.317 -39.506 4.914   1.00 75.59  ? 465 ARG A NH1 1 
ATOM   6676 N  NH2 . ARG B 1 492 ? -35.717 -39.465 6.557   1.00 68.99  ? 465 ARG A NH2 1 
ATOM   6677 N  N   . HIS B 1 493 ? -38.180 -47.463 2.782   1.00 65.10  ? 466 HIS A N   1 
ATOM   6678 C  CA  . HIS B 1 493 ? -39.178 -48.236 2.028   1.00 68.56  ? 466 HIS A CA  1 
ATOM   6679 C  C   . HIS B 1 493 ? -38.851 -49.743 1.919   1.00 62.48  ? 466 HIS A C   1 
ATOM   6680 O  O   . HIS B 1 493 ? -39.598 -50.510 1.344   1.00 65.62  ? 466 HIS A O   1 
ATOM   6681 C  CB  . HIS B 1 493 ? -39.449 -47.557 0.677   1.00 68.60  ? 466 HIS A CB  1 
ATOM   6682 C  CG  . HIS B 1 493 ? -39.789 -46.099 0.807   1.00 76.22  ? 466 HIS A CG  1 
ATOM   6683 N  ND1 . HIS B 1 493 ? -40.529 -45.597 1.864   1.00 81.74  ? 466 HIS A ND1 1 
ATOM   6684 C  CD2 . HIS B 1 493 ? -39.469 -45.033 0.034   1.00 75.54  ? 466 HIS A CD2 1 
ATOM   6685 C  CE1 . HIS B 1 493 ? -40.653 -44.287 1.734   1.00 76.88  ? 466 HIS A CE1 1 
ATOM   6686 N  NE2 . HIS B 1 493 ? -40.015 -43.919 0.633   1.00 80.60  ? 466 HIS A NE2 1 
ATOM   6687 N  N   . LEU B 1 494 ? -37.773 -50.168 2.553   1.00 58.63  ? 467 LEU A N   1 
ATOM   6688 C  CA  . LEU B 1 494 ? -37.363 -51.551 2.499   1.00 64.18  ? 467 LEU A CA  1 
ATOM   6689 C  C   . LEU B 1 494 ? -38.452 -52.515 3.001   1.00 72.65  ? 467 LEU A C   1 
ATOM   6690 O  O   . LEU B 1 494 ? -39.255 -52.194 3.902   1.00 72.54  ? 467 LEU A O   1 
ATOM   6691 C  CB  . LEU B 1 494 ? -36.085 -51.724 3.320   1.00 66.60  ? 467 LEU A CB  1 
ATOM   6692 C  CG  . LEU B 1 494 ? -35.424 -53.099 3.346   1.00 70.30  ? 467 LEU A CG  1 
ATOM   6693 C  CD1 . LEU B 1 494 ? -34.852 -53.387 1.979   1.00 72.68  ? 467 LEU A CD1 1 
ATOM   6694 C  CD2 . LEU B 1 494 ? -34.329 -53.196 4.413   1.00 70.09  ? 467 LEU A CD2 1 
ATOM   6695 N  N   . ASN B 1 495 ? -38.441 -53.696 2.386   1.00 77.19  ? 468 ASN A N   1 
ATOM   6696 C  CA  . ASN B 1 495 ? -39.348 -54.797 2.663   1.00 70.55  ? 468 ASN A CA  1 
ATOM   6697 C  C   . ASN B 1 495 ? -38.668 -56.051 2.145   1.00 71.23  ? 468 ASN A C   1 
ATOM   6698 O  O   . ASN B 1 495 ? -38.434 -56.179 0.948   1.00 79.81  ? 468 ASN A O   1 
ATOM   6699 C  CB  . ASN B 1 495 ? -40.661 -54.595 1.924   1.00 71.58  ? 468 ASN A CB  1 
ATOM   6700 C  CG  . ASN B 1 495 ? -41.747 -55.529 2.407   1.00 81.86  ? 468 ASN A CG  1 
ATOM   6701 O  OD1 . ASN B 1 495 ? -41.481 -56.468 3.154   1.00 86.38  ? 468 ASN A OD1 1 
ATOM   6702 N  ND2 . ASN B 1 495 ? -43.000 -55.264 1.980   1.00 96.34  ? 468 ASN A ND2 1 
ATOM   6703 N  N   . PHE B 1 496 ? -38.299 -56.950 3.040   1.00 68.28  ? 469 PHE A N   1 
ATOM   6704 C  CA  . PHE B 1 496 ? -37.638 -58.169 2.647   1.00 64.39  ? 469 PHE A CA  1 
ATOM   6705 C  C   . PHE B 1 496 ? -37.931 -59.285 3.640   1.00 72.31  ? 469 PHE A C   1 
ATOM   6706 O  O   . PHE B 1 496 ? -38.549 -59.063 4.699   1.00 63.96  ? 469 PHE A O   1 
ATOM   6707 C  CB  . PHE B 1 496 ? -36.146 -57.940 2.548   1.00 66.54  ? 469 PHE A CB  1 
ATOM   6708 C  CG  . PHE B 1 496 ? -35.449 -57.875 3.887   1.00 75.77  ? 469 PHE A CG  1 
ATOM   6709 C  CD1 . PHE B 1 496 ? -35.274 -56.662 4.543   1.00 69.54  ? 469 PHE A CD1 1 
ATOM   6710 C  CD2 . PHE B 1 496 ? -34.959 -59.033 4.489   1.00 78.87  ? 469 PHE A CD2 1 
ATOM   6711 C  CE1 . PHE B 1 496 ? -34.636 -56.607 5.765   1.00 67.14  ? 469 PHE A CE1 1 
ATOM   6712 C  CE2 . PHE B 1 496 ? -34.324 -58.979 5.710   1.00 72.91  ? 469 PHE A CE2 1 
ATOM   6713 C  CZ  . PHE B 1 496 ? -34.159 -57.760 6.346   1.00 71.76  ? 469 PHE A CZ  1 
ATOM   6714 N  N   . THR B 1 497 ? -37.470 -60.485 3.289   1.00 74.27  ? 470 THR A N   1 
ATOM   6715 C  CA  . THR B 1 497 ? -37.793 -61.691 4.035   1.00 78.00  ? 470 THR A CA  1 
ATOM   6716 C  C   . THR B 1 497 ? -36.563 -62.248 4.730   1.00 81.25  ? 470 THR A C   1 
ATOM   6717 O  O   . THR B 1 497 ? -35.603 -62.654 4.077   1.00 86.79  ? 470 THR A O   1 
ATOM   6718 C  CB  . THR B 1 497 ? -38.351 -62.779 3.101   1.00 77.48  ? 470 THR A CB  1 
ATOM   6719 O  OG1 . THR B 1 497 ? -39.372 -62.218 2.274   1.00 74.34  ? 470 THR A OG1 1 
ATOM   6720 C  CG2 . THR B 1 497 ? -38.930 -63.941 3.912   1.00 84.71  ? 470 THR A CG2 1 
ATOM   6721 N  N   . ASN B 1 498 ? -36.587 -62.296 6.054   1.00 80.38  ? 471 ASN A N   1 
ATOM   6722 C  CA  . ASN B 1 498 ? -35.454 -62.863 6.769   1.00 80.57  ? 471 ASN A CA  1 
ATOM   6723 C  C   . ASN B 1 498 ? -35.385 -64.390 6.688   1.00 81.45  ? 471 ASN A C   1 
ATOM   6724 O  O   . ASN B 1 498 ? -36.295 -65.060 6.182   1.00 78.63  ? 471 ASN A O   1 
ATOM   6725 C  CB  . ASN B 1 498 ? -35.391 -62.359 8.232   1.00 85.47  ? 471 ASN A CB  1 
ATOM   6726 C  CG  . ASN B 1 498 ? -36.598 -62.769 9.086   1.00 83.67  ? 471 ASN A CG  1 
ATOM   6727 O  OD1 . ASN B 1 498 ? -37.269 -63.760 8.821   1.00 79.97  ? 471 ASN A OD1 1 
ATOM   6728 N  ND2 . ASN B 1 498 ? -36.844 -62.011 10.148  1.00 81.34  ? 471 ASN A ND2 1 
ATOM   6729 N  N   . ASN B 1 499 ? -34.268 -64.913 7.175   1.00 88.34  ? 472 ASN A N   1 
ATOM   6730 C  CA  . ASN B 1 499 ? -34.027 -66.354 7.285   1.00 89.19  ? 472 ASN A CA  1 
ATOM   6731 C  C   . ASN B 1 499 ? -35.037 -67.126 8.144   1.00 90.23  ? 472 ASN A C   1 
ATOM   6732 O  O   . ASN B 1 499 ? -35.112 -68.347 8.046   1.00 99.02  ? 472 ASN A O   1 
ATOM   6733 C  CB  . ASN B 1 499 ? -32.607 -66.615 7.809   1.00 85.23  ? 472 ASN A CB  1 
ATOM   6734 C  CG  . ASN B 1 499 ? -32.436 -66.216 9.264   1.00 89.85  ? 472 ASN A CG  1 
ATOM   6735 O  OD1 . ASN B 1 499 ? -32.092 -67.040 10.117  1.00 83.46  ? 472 ASN A OD1 1 
ATOM   6736 N  ND2 . ASN B 1 499 ? -32.699 -64.947 9.560   1.00 92.80  ? 472 ASN A ND2 1 
ATOM   6737 N  N   . MET B 1 500 ? -35.794 -66.430 8.988   1.00 85.99  ? 473 MET A N   1 
ATOM   6738 C  CA  . MET B 1 500 ? -36.870 -67.066 9.756   1.00 87.36  ? 473 MET A CA  1 
ATOM   6739 C  C   . MET B 1 500 ? -38.199 -67.096 8.979   1.00 89.41  ? 473 MET A C   1 
ATOM   6740 O  O   . MET B 1 500 ? -39.213 -67.539 9.513   1.00 83.57  ? 473 MET A O   1 
ATOM   6741 C  CB  . MET B 1 500 ? -37.092 -66.333 11.088  1.00 85.78  ? 473 MET A CB  1 
ATOM   6742 C  CG  . MET B 1 500 ? -35.865 -66.208 11.973  1.00 86.35  ? 473 MET A CG  1 
ATOM   6743 S  SD  . MET B 1 500 ? -35.366 -67.721 12.795  1.00 102.40 ? 473 MET A SD  1 
ATOM   6744 C  CE  . MET B 1 500 ? -36.894 -68.125 13.664  1.00 95.02  ? 473 MET A CE  1 
ATOM   6745 N  N   . GLY B 1 501 ? -38.202 -66.607 7.739   1.00 97.20  ? 474 GLY A N   1 
ATOM   6746 C  CA  . GLY B 1 501 ? -39.439 -66.478 6.949   1.00 102.77 ? 474 GLY A CA  1 
ATOM   6747 C  C   . GLY B 1 501 ? -40.399 -65.354 7.356   1.00 100.59 ? 474 GLY A C   1 
ATOM   6748 O  O   . GLY B 1 501 ? -41.618 -65.532 7.307   1.00 90.09  ? 474 GLY A O   1 
ATOM   6749 N  N   . GLU B 1 502 ? -39.855 -64.192 7.728   1.00 99.89  ? 475 GLU A N   1 
ATOM   6750 C  CA  . GLU B 1 502 ? -40.660 -63.036 8.160   1.00 93.01  ? 475 GLU A CA  1 
ATOM   6751 C  C   . GLU B 1 502 ? -40.452 -61.793 7.270   1.00 81.99  ? 475 GLU A C   1 
ATOM   6752 O  O   . GLU B 1 502 ? -39.406 -61.634 6.624   1.00 67.99  ? 475 GLU A O   1 
ATOM   6753 C  CB  . GLU B 1 502 ? -40.342 -62.692 9.618   1.00 98.04  ? 475 GLU A CB  1 
ATOM   6754 C  CG  . GLU B 1 502 ? -40.702 -63.781 10.623  1.00 101.10 ? 475 GLU A CG  1 
ATOM   6755 C  CD  . GLU B 1 502 ? -42.086 -63.586 11.212  1.00 105.09 ? 475 GLU A CD  1 
ATOM   6756 O  OE1 . GLU B 1 502 ? -42.208 -62.834 12.206  1.00 97.78  ? 475 GLU A OE1 1 
ATOM   6757 O  OE2 . GLU B 1 502 ? -43.050 -64.184 10.683  1.00 106.48 ? 475 GLU A OE2 1 
ATOM   6758 N  N   . GLN B 1 503 ? -41.469 -60.932 7.233   1.00 75.70  ? 476 GLN A N   1 
ATOM   6759 C  CA  . GLN B 1 503 ? -41.388 -59.671 6.511   1.00 80.81  ? 476 GLN A CA  1 
ATOM   6760 C  C   . GLN B 1 503 ? -40.826 -58.617 7.417   1.00 74.72  ? 476 GLN A C   1 
ATOM   6761 O  O   . GLN B 1 503 ? -41.418 -58.328 8.439   1.00 76.69  ? 476 GLN A O   1 
ATOM   6762 C  CB  . GLN B 1 503 ? -42.755 -59.212 5.992   1.00 85.40  ? 476 GLN A CB  1 
ATOM   6763 C  CG  . GLN B 1 503 ? -43.304 -60.083 4.874   1.00 89.43  ? 476 GLN A CG  1 
ATOM   6764 C  CD  . GLN B 1 503 ? -42.240 -60.412 3.848   1.00 96.76  ? 476 GLN A CD  1 
ATOM   6765 O  OE1 . GLN B 1 503 ? -41.612 -59.506 3.294   1.00 112.01 ? 476 GLN A OE1 1 
ATOM   6766 N  NE2 . GLN B 1 503 ? -42.004 -61.705 3.611   1.00 91.41  ? 476 GLN A NE2 1 
ATOM   6767 N  N   . VAL B 1 504 ? -39.683 -58.053 7.025   1.00 74.38  ? 477 VAL A N   1 
ATOM   6768 C  CA  . VAL B 1 504 ? -39.023 -56.995 7.776   1.00 70.82  ? 477 VAL A CA  1 
ATOM   6769 C  C   . VAL B 1 504 ? -39.223 -55.676 7.047   1.00 66.30  ? 477 VAL A C   1 
ATOM   6770 O  O   . VAL B 1 504 ? -38.651 -55.458 5.992   1.00 79.23  ? 477 VAL A O   1 
ATOM   6771 C  CB  . VAL B 1 504 ? -37.517 -57.299 7.961   1.00 74.55  ? 477 VAL A CB  1 
ATOM   6772 C  CG1 . VAL B 1 504 ? -36.818 -56.189 8.720   1.00 70.16  ? 477 VAL A CG1 1 
ATOM   6773 C  CG2 . VAL B 1 504 ? -37.330 -58.609 8.719   1.00 76.08  ? 477 VAL A CG2 1 
ATOM   6774 N  N   . THR B 1 505 ? -40.091 -54.834 7.594   1.00 64.22  ? 478 THR A N   1 
ATOM   6775 C  CA  . THR B 1 505 ? -40.240 -53.450 7.169   1.00 69.64  ? 478 THR A CA  1 
ATOM   6776 C  C   . THR B 1 505 ? -40.280 -52.539 8.391   1.00 63.81  ? 478 THR A C   1 
ATOM   6777 O  O   . THR B 1 505 ? -40.607 -52.982 9.483   1.00 59.51  ? 478 THR A O   1 
ATOM   6778 C  CB  . THR B 1 505 ? -41.565 -53.193 6.438   1.00 73.47  ? 478 THR A CB  1 
ATOM   6779 O  OG1 . THR B 1 505 ? -42.654 -53.522 7.310   1.00 67.78  ? 478 THR A OG1 1 
ATOM   6780 C  CG2 . THR B 1 505 ? -41.656 -53.996 5.180   1.00 79.47  ? 478 THR A CG2 1 
ATOM   6781 N  N   . PHE B 1 506 ? -39.977 -51.265 8.166   1.00 59.26  ? 479 PHE A N   1 
ATOM   6782 C  CA  . PHE B 1 506 ? -39.975 -50.253 9.204   1.00 61.20  ? 479 PHE A CA  1 
ATOM   6783 C  C   . PHE B 1 506 ? -41.153 -49.302 8.925   1.00 63.60  ? 479 PHE A C   1 
ATOM   6784 O  O   . PHE B 1 506 ? -41.458 -49.022 7.763   1.00 64.60  ? 479 PHE A O   1 
ATOM   6785 C  CB  . PHE B 1 506 ? -38.642 -49.468 9.229   1.00 58.32  ? 479 PHE A CB  1 
ATOM   6786 C  CG  . PHE B 1 506 ? -37.408 -50.329 9.271   1.00 60.62  ? 479 PHE A CG  1 
ATOM   6787 C  CD1 . PHE B 1 506 ? -36.916 -50.823 10.486  1.00 65.51  ? 479 PHE A CD1 1 
ATOM   6788 C  CD2 . PHE B 1 506 ? -36.710 -50.635 8.106   1.00 64.16  ? 479 PHE A CD2 1 
ATOM   6789 C  CE1 . PHE B 1 506 ? -35.767 -51.630 10.531  1.00 63.00  ? 479 PHE A CE1 1 
ATOM   6790 C  CE2 . PHE B 1 506 ? -35.562 -51.427 8.148   1.00 64.78  ? 479 PHE A CE2 1 
ATOM   6791 C  CZ  . PHE B 1 506 ? -35.089 -51.927 9.360   1.00 59.87  ? 479 PHE A CZ  1 
ATOM   6792 N  N   . ASP B 1 507 ? -41.820 -48.822 9.976   1.00 61.20  ? 480 ASP A N   1 
ATOM   6793 C  CA  . ASP B 1 507 ? -42.997 -47.965 9.799   1.00 61.41  ? 480 ASP A CA  1 
ATOM   6794 C  C   . ASP B 1 507 ? -42.566 -46.532 9.490   1.00 60.20  ? 480 ASP A C   1 
ATOM   6795 O  O   . ASP B 1 507 ? -41.380 -46.270 9.279   1.00 58.25  ? 480 ASP A O   1 
ATOM   6796 C  CB  . ASP B 1 507 ? -43.949 -48.040 11.018  1.00 65.63  ? 480 ASP A CB  1 
ATOM   6797 C  CG  . ASP B 1 507 ? -43.328 -47.504 12.310  1.00 72.23  ? 480 ASP A CG  1 
ATOM   6798 O  OD1 . ASP B 1 507 ? -42.330 -46.753 12.255  1.00 81.82  ? 480 ASP A OD1 1 
ATOM   6799 O  OD2 . ASP B 1 507 ? -43.842 -47.835 13.398  1.00 73.54  ? 480 ASP A OD2 1 
ATOM   6800 N  N   . GLU B 1 508 ? -43.538 -45.623 9.449   1.00 60.83  ? 481 GLU A N   1 
ATOM   6801 C  CA  . GLU B 1 508 ? -43.301 -44.196 9.208   1.00 62.74  ? 481 GLU A CA  1 
ATOM   6802 C  C   . GLU B 1 508 ? -42.264 -43.564 10.200  1.00 66.01  ? 481 GLU A C   1 
ATOM   6803 O  O   . GLU B 1 508 ? -41.598 -42.566 9.858   1.00 63.61  ? 481 GLU A O   1 
ATOM   6804 C  CB  . GLU B 1 508 ? -44.657 -43.440 9.228   1.00 59.40  ? 481 GLU A CB  1 
HETATM 6805 N  N   . CSO B 1 509 ? -42.121 -44.163 11.393  1.00 60.92  ? 482 CSO A N   1 
HETATM 6806 C  CA  . CSO B 1 509 ? -41.167 -43.720 12.414  1.00 58.77  ? 482 CSO A CA  1 
HETATM 6807 C  CB  . CSO B 1 509 ? -41.859 -43.762 13.776  1.00 65.91  ? 482 CSO A CB  1 
HETATM 6808 S  SG  . CSO B 1 509 ? -43.248 -42.677 13.783  1.00 67.80  ? 482 CSO A SG  1 
HETATM 6809 C  C   . CSO B 1 509 ? -39.901 -44.538 12.487  1.00 58.36  ? 482 CSO A C   1 
HETATM 6810 O  O   . CSO B 1 509 ? -39.039 -44.294 13.337  1.00 63.60  ? 482 CSO A O   1 
HETATM 6811 O  OD  . CSO B 1 509 ? -44.570 -43.812 13.881  1.00 82.69  ? 482 CSO A OD  1 
ATOM   6812 N  N   . GLY B 1 510 ? -39.752 -45.518 11.602  1.00 57.93  ? 483 GLY A N   1 
ATOM   6813 C  CA  . GLY B 1 510 ? -38.506 -46.275 11.502  1.00 51.59  ? 483 GLY A CA  1 
ATOM   6814 C  C   . GLY B 1 510 ? -38.428 -47.318 12.582  1.00 50.24  ? 483 GLY A C   1 
ATOM   6815 O  O   . GLY B 1 510 ? -37.349 -47.729 12.968  1.00 54.66  ? 483 GLY A O   1 
ATOM   6816 N  N   . ASP B 1 511 ? -39.586 -47.744 13.059  1.00 51.98  ? 484 ASP A N   1 
ATOM   6817 C  CA  . ASP B 1 511 ? -39.692 -48.729 14.107  1.00 60.84  ? 484 ASP A CA  1 
ATOM   6818 C  C   . ASP B 1 511 ? -40.144 -50.080 13.519  1.00 65.00  ? 484 ASP A C   1 
ATOM   6819 O  O   . ASP B 1 511 ? -40.632 -50.175 12.401  1.00 70.49  ? 484 ASP A O   1 
ATOM   6820 C  CB  . ASP B 1 511 ? -40.728 -48.276 15.167  1.00 68.04  ? 484 ASP A CB  1 
ATOM   6821 C  CG  . ASP B 1 511 ? -40.305 -47.005 15.980  1.00 72.32  ? 484 ASP A CG  1 
ATOM   6822 O  OD1 . ASP B 1 511 ? -39.102 -46.797 16.331  1.00 73.34  ? 484 ASP A OD1 1 
ATOM   6823 O  OD2 . ASP B 1 511 ? -41.231 -46.225 16.305  1.00 66.57  ? 484 ASP A OD2 1 
ATOM   6824 N  N   . LEU B 1 512 ? -40.045 -51.114 14.329  1.00 70.10  ? 485 LEU A N   1 
ATOM   6825 C  CA  . LEU B 1 512 ? -40.390 -52.445 13.931  1.00 65.66  ? 485 LEU A CA  1 
ATOM   6826 C  C   . LEU B 1 512 ? -41.144 -53.058 15.117  1.00 69.97  ? 485 LEU A C   1 
ATOM   6827 O  O   . LEU B 1 512 ? -40.635 -53.086 16.244  1.00 74.12  ? 485 LEU A O   1 
ATOM   6828 C  CB  . LEU B 1 512 ? -39.091 -53.183 13.632  1.00 64.87  ? 485 LEU A CB  1 
ATOM   6829 C  CG  . LEU B 1 512 ? -39.127 -54.655 13.310  1.00 74.59  ? 485 LEU A CG  1 
ATOM   6830 C  CD1 . LEU B 1 512 ? -40.012 -54.857 12.081  1.00 86.52  ? 485 LEU A CD1 1 
ATOM   6831 C  CD2 . LEU B 1 512 ? -37.712 -55.174 13.066  1.00 76.27  ? 485 LEU A CD2 1 
ATOM   6832 N  N   . VAL B 1 513 ? -42.368 -53.519 14.872  1.00 71.98  ? 486 VAL A N   1 
ATOM   6833 C  CA  . VAL B 1 513 ? -43.161 -54.238 15.891  1.00 66.79  ? 486 VAL A CA  1 
ATOM   6834 C  C   . VAL B 1 513 ? -42.648 -55.635 16.224  1.00 62.51  ? 486 VAL A C   1 
ATOM   6835 O  O   . VAL B 1 513 ? -41.996 -56.303 15.418  1.00 60.58  ? 486 VAL A O   1 
ATOM   6836 C  CB  . VAL B 1 513 ? -44.636 -54.378 15.492  1.00 76.04  ? 486 VAL A CB  1 
ATOM   6837 C  CG1 . VAL B 1 513 ? -45.322 -53.015 15.458  1.00 75.61  ? 486 VAL A CG1 1 
ATOM   6838 C  CG2 . VAL B 1 513 ? -44.760 -55.070 14.142  1.00 88.73  ? 486 VAL A CG2 1 
ATOM   6839 N  N   . GLY B 1 514 ? -42.954 -56.061 17.443  1.00 61.51  ? 487 GLY A N   1 
ATOM   6840 C  CA  . GLY B 1 514 ? -42.505 -57.338 17.964  1.00 56.56  ? 487 GLY A CA  1 
ATOM   6841 C  C   . GLY B 1 514 ? -43.318 -57.740 19.168  1.00 54.95  ? 487 GLY A C   1 
ATOM   6842 O  O   . GLY B 1 514 ? -43.689 -56.899 19.974  1.00 58.42  ? 487 GLY A O   1 
ATOM   6843 N  N   . ASN B 1 515 ? -43.621 -59.024 19.297  1.00 58.91  ? 488 ASN A N   1 
ATOM   6844 C  CA  . ASN B 1 515 ? -44.230 -59.500 20.538  1.00 61.33  ? 488 ASN A CA  1 
ATOM   6845 C  C   . ASN B 1 515 ? -43.163 -59.630 21.614  1.00 62.53  ? 488 ASN A C   1 
ATOM   6846 O  O   . ASN B 1 515 ? -42.005 -59.284 21.400  1.00 61.68  ? 488 ASN A O   1 
ATOM   6847 C  CB  . ASN B 1 515 ? -44.910 -60.838 20.356  1.00 61.30  ? 488 ASN A CB  1 
ATOM   6848 C  CG  . ASN B 1 515 ? -46.094 -60.781 19.404  1.00 70.80  ? 488 ASN A CG  1 
ATOM   6849 O  OD1 . ASN B 1 515 ? -46.774 -59.753 19.259  1.00 59.55  ? 488 ASN A OD1 1 
ATOM   6850 N  ND2 . ASN B 1 515 ? -46.350 -61.933 18.744  1.00 82.51  ? 488 ASN A ND2 1 
ATOM   6851 N  N   . TYR B 1 516 ? -43.568 -60.105 22.785  1.00 63.36  ? 489 TYR A N   1 
ATOM   6852 C  CA  . TYR B 1 516 ? -42.655 -60.329 23.884  1.00 59.43  ? 489 TYR A CA  1 
ATOM   6853 C  C   . TYR B 1 516 ? -43.002 -61.676 24.557  1.00 58.80  ? 489 TYR A C   1 
ATOM   6854 O  O   . TYR B 1 516 ? -44.169 -62.067 24.653  1.00 58.87  ? 489 TYR A O   1 
ATOM   6855 C  CB  . TYR B 1 516 ? -42.783 -59.207 24.903  1.00 59.83  ? 489 TYR A CB  1 
ATOM   6856 C  CG  . TYR B 1 516 ? -42.412 -57.799 24.456  1.00 65.86  ? 489 TYR A CG  1 
ATOM   6857 C  CD1 . TYR B 1 516 ? -41.096 -57.343 24.510  1.00 62.02  ? 489 TYR A CD1 1 
ATOM   6858 C  CD2 . TYR B 1 516 ? -43.392 -56.896 24.064  1.00 70.19  ? 489 TYR A CD2 1 
ATOM   6859 C  CE1 . TYR B 1 516 ? -40.769 -56.050 24.151  1.00 63.67  ? 489 TYR A CE1 1 
ATOM   6860 C  CE2 . TYR B 1 516 ? -43.073 -55.595 23.698  1.00 74.30  ? 489 TYR A CE2 1 
ATOM   6861 C  CZ  . TYR B 1 516 ? -41.761 -55.170 23.745  1.00 73.81  ? 489 TYR A CZ  1 
ATOM   6862 O  OH  . TYR B 1 516 ? -41.465 -53.859 23.387  1.00 82.53  ? 489 TYR A OH  1 
ATOM   6863 N  N   . SER B 1 517 ? -41.983 -62.391 24.989  1.00 55.13  ? 490 SER A N   1 
ATOM   6864 C  CA  . SER B 1 517 ? -42.161 -63.437 25.970  1.00 59.83  ? 490 SER A CA  1 
ATOM   6865 C  C   . SER B 1 517 ? -42.207 -62.795 27.338  1.00 55.51  ? 490 SER A C   1 
ATOM   6866 O  O   . SER B 1 517 ? -41.620 -61.720 27.554  1.00 54.02  ? 490 SER A O   1 
ATOM   6867 C  CB  . SER B 1 517 ? -40.984 -64.416 25.957  1.00 63.67  ? 490 SER A CB  1 
ATOM   6868 O  OG  . SER B 1 517 ? -41.375 -65.632 25.362  1.00 78.67  ? 490 SER A OG  1 
ATOM   6869 N  N   . ILE B 1 518 ? -42.832 -63.490 28.278  1.00 46.45  ? 491 ILE A N   1 
ATOM   6870 C  CA  . ILE B 1 518 ? -42.780 -63.078 29.652  1.00 47.10  ? 491 ILE A CA  1 
ATOM   6871 C  C   . ILE B 1 518 ? -42.132 -64.195 30.392  1.00 50.82  ? 491 ILE A C   1 
ATOM   6872 O  O   . ILE B 1 518 ? -42.571 -65.318 30.246  1.00 55.04  ? 491 ILE A O   1 
ATOM   6873 C  CB  . ILE B 1 518 ? -44.167 -62.792 30.224  1.00 49.73  ? 491 ILE A CB  1 
ATOM   6874 C  CG1 . ILE B 1 518 ? -44.836 -61.683 29.426  1.00 50.82  ? 491 ILE A CG1 1 
ATOM   6875 C  CG2 . ILE B 1 518 ? -44.076 -62.372 31.683  1.00 49.25  ? 491 ILE A CG2 1 
ATOM   6876 C  CD1 . ILE B 1 518 ? -46.305 -61.598 29.683  1.00 56.51  ? 491 ILE A CD1 1 
ATOM   6877 N  N   . ILE B 1 519 ? -41.111 -63.863 31.197  1.00 56.22  ? 492 ILE A N   1 
ATOM   6878 C  CA  . ILE B 1 519 ? -40.226 -64.823 31.853  1.00 54.05  ? 492 ILE A CA  1 
ATOM   6879 C  C   . ILE B 1 519 ? -40.100 -64.563 33.324  1.00 56.60  ? 492 ILE A C   1 
ATOM   6880 O  O   . ILE B 1 519 ? -40.289 -63.437 33.786  1.00 62.00  ? 492 ILE A O   1 
ATOM   6881 C  CB  . ILE B 1 519 ? -38.784 -64.761 31.316  1.00 57.33  ? 492 ILE A CB  1 
ATOM   6882 C  CG1 . ILE B 1 519 ? -38.179 -63.374 31.577  1.00 59.40  ? 492 ILE A CG1 1 
ATOM   6883 C  CG2 . ILE B 1 519 ? -38.771 -65.165 29.840  1.00 57.01  ? 492 ILE A CG2 1 
ATOM   6884 C  CD1 . ILE B 1 519 ? -36.665 -63.298 31.475  1.00 63.71  ? 492 ILE A CD1 1 
ATOM   6885 N  N   . ASN B 1 520 ? -39.725 -65.615 34.049  1.00 55.48  ? 493 ASN A N   1 
ATOM   6886 C  CA  . ASN B 1 520 ? -39.751 -65.604 35.498  1.00 54.23  ? 493 ASN A CA  1 
ATOM   6887 C  C   . ASN B 1 520 ? -38.471 -66.246 35.949  1.00 53.63  ? 493 ASN A C   1 
ATOM   6888 O  O   . ASN B 1 520 ? -38.009 -67.200 35.336  1.00 62.06  ? 493 ASN A O   1 
ATOM   6889 C  CB  . ASN B 1 520 ? -40.995 -66.365 35.995  1.00 56.44  ? 493 ASN A CB  1 
ATOM   6890 C  CG  . ASN B 1 520 ? -41.258 -66.219 37.500  1.00 56.35  ? 493 ASN A CG  1 
ATOM   6891 O  OD1 . ASN B 1 520 ? -40.825 -65.274 38.179  1.00 57.20  ? 493 ASN A OD1 1 
ATOM   6892 N  ND2 . ASN B 1 520 ? -42.002 -67.164 38.019  1.00 54.95  ? 493 ASN A ND2 1 
ATOM   6893 N  N   . TRP B 1 521 ? -37.881 -65.688 36.993  1.00 54.79  ? 494 TRP A N   1 
ATOM   6894 C  CA  . TRP B 1 521 ? -36.545 -66.072 37.427  1.00 60.45  ? 494 TRP A CA  1 
ATOM   6895 C  C   . TRP B 1 521 ? -36.612 -67.256 38.417  1.00 67.04  ? 494 TRP A C   1 
ATOM   6896 O  O   . TRP B 1 521 ? -36.883 -67.064 39.622  1.00 60.76  ? 494 TRP A O   1 
ATOM   6897 C  CB  . TRP B 1 521 ? -35.832 -64.861 38.056  1.00 53.51  ? 494 TRP A CB  1 
ATOM   6898 C  CG  . TRP B 1 521 ? -35.364 -63.808 37.055  1.00 54.43  ? 494 TRP A CG  1 
ATOM   6899 C  CD1 . TRP B 1 521 ? -35.840 -63.590 35.782  1.00 57.66  ? 494 TRP A CD1 1 
ATOM   6900 C  CD2 . TRP B 1 521 ? -34.350 -62.823 37.268  1.00 46.02  ? 494 TRP A CD2 1 
ATOM   6901 N  NE1 . TRP B 1 521 ? -35.162 -62.545 35.196  1.00 56.60  ? 494 TRP A NE1 1 
ATOM   6902 C  CE2 . TRP B 1 521 ? -34.235 -62.074 36.087  1.00 48.83  ? 494 TRP A CE2 1 
ATOM   6903 C  CE3 . TRP B 1 521 ? -33.512 -62.530 38.337  1.00 49.70  ? 494 TRP A CE3 1 
ATOM   6904 C  CZ2 . TRP B 1 521 ? -33.325 -61.052 35.950  1.00 53.11  ? 494 TRP A CZ2 1 
ATOM   6905 C  CZ3 . TRP B 1 521 ? -32.615 -61.507 38.219  1.00 55.31  ? 494 TRP A CZ3 1 
ATOM   6906 C  CH2 . TRP B 1 521 ? -32.524 -60.769 37.031  1.00 58.36  ? 494 TRP A CH2 1 
ATOM   6907 N  N   . HIS B 1 522 ? -36.370 -68.469 37.903  1.00 69.82  ? 495 HIS A N   1 
ATOM   6908 C  CA  . HIS B 1 522 ? -36.204 -69.673 38.748  1.00 71.13  ? 495 HIS A CA  1 
ATOM   6909 C  C   . HIS B 1 522 ? -34.733 -69.959 39.080  1.00 68.09  ? 495 HIS A C   1 
ATOM   6910 O  O   . HIS B 1 522 ? -33.844 -69.427 38.444  1.00 65.28  ? 495 HIS A O   1 
ATOM   6911 C  CB  . HIS B 1 522 ? -36.821 -70.902 38.077  1.00 70.14  ? 495 HIS A CB  1 
ATOM   6912 C  CG  . HIS B 1 522 ? -38.269 -70.744 37.716  1.00 74.15  ? 495 HIS A CG  1 
ATOM   6913 N  ND1 . HIS B 1 522 ? -39.097 -69.815 38.312  1.00 84.10  ? 495 HIS A ND1 1 
ATOM   6914 C  CD2 . HIS B 1 522 ? -39.041 -71.421 36.837  1.00 76.25  ? 495 HIS A CD2 1 
ATOM   6915 C  CE1 . HIS B 1 522 ? -40.310 -69.913 37.799  1.00 80.57  ? 495 HIS A CE1 1 
ATOM   6916 N  NE2 . HIS B 1 522 ? -40.301 -70.875 36.896  1.00 86.87  ? 495 HIS A NE2 1 
ATOM   6917 N  N   . LEU B 1 523 ? -34.494 -70.767 40.112  1.00 76.17  ? 496 LEU A N   1 
ATOM   6918 C  CA  . LEU B 1 523 ? -33.169 -71.378 40.339  1.00 77.65  ? 496 LEU A CA  1 
ATOM   6919 C  C   . LEU B 1 523 ? -33.122 -72.732 39.660  1.00 79.55  ? 496 LEU A C   1 
ATOM   6920 O  O   . LEU B 1 523 ? -34.131 -73.437 39.612  1.00 76.95  ? 496 LEU A O   1 
ATOM   6921 C  CB  . LEU B 1 523 ? -32.856 -71.564 41.828  1.00 74.00  ? 496 LEU A CB  1 
ATOM   6922 C  CG  . LEU B 1 523 ? -31.798 -70.631 42.396  1.00 76.18  ? 496 LEU A CG  1 
ATOM   6923 C  CD1 . LEU B 1 523 ? -31.622 -70.870 43.884  1.00 75.97  ? 496 LEU A CD1 1 
ATOM   6924 C  CD2 . LEU B 1 523 ? -30.473 -70.835 41.681  1.00 83.41  ? 496 LEU A CD2 1 
ATOM   6925 N  N   . SER B 1 524 ? -31.954 -73.086 39.132  1.00 87.53  ? 497 SER A N   1 
ATOM   6926 C  CA  . SER B 1 524 ? -31.733 -74.429 38.603  1.00 96.68  ? 497 SER A CA  1 
ATOM   6927 C  C   . SER B 1 524 ? -31.484 -75.403 39.758  1.00 94.72  ? 497 SER A C   1 
ATOM   6928 O  O   . SER B 1 524 ? -30.622 -75.157 40.615  1.00 84.70  ? 497 SER A O   1 
ATOM   6929 C  CB  . SER B 1 524 ? -30.531 -74.458 37.664  1.00 106.26 ? 497 SER A CB  1 
ATOM   6930 O  OG  . SER B 1 524 ? -30.432 -75.712 37.011  1.00 106.90 ? 497 SER A OG  1 
ATOM   6931 N  N   . PRO B 1 525 ? -32.234 -76.513 39.784  1.00 97.88  ? 498 PRO A N   1 
ATOM   6932 C  CA  . PRO B 1 525 ? -32.053 -77.523 40.829  1.00 102.77 ? 498 PRO A CA  1 
ATOM   6933 C  C   . PRO B 1 525 ? -30.735 -78.317 40.680  1.00 111.73 ? 498 PRO A C   1 
ATOM   6934 O  O   . PRO B 1 525 ? -30.070 -78.591 41.682  1.00 116.32 ? 498 PRO A O   1 
ATOM   6935 C  CB  . PRO B 1 525 ? -33.262 -78.431 40.635  1.00 103.80 ? 498 PRO A CB  1 
ATOM   6936 C  CG  . PRO B 1 525 ? -33.581 -78.331 39.175  1.00 99.06  ? 498 PRO A CG  1 
ATOM   6937 C  CD  . PRO B 1 525 ? -33.208 -76.938 38.759  1.00 97.54  ? 498 PRO A CD  1 
ATOM   6938 N  N   . GLU B 1 526 ? -30.369 -78.674 39.447  1.00 108.56 ? 499 GLU A N   1 
ATOM   6939 C  CA  . GLU B 1 526 ? -29.048 -79.228 39.143  1.00 113.36 ? 499 GLU A CA  1 
ATOM   6940 C  C   . GLU B 1 526 ? -27.940 -78.192 39.382  1.00 110.27 ? 499 GLU A C   1 
ATOM   6941 O  O   . GLU B 1 526 ? -27.059 -78.351 40.232  1.00 105.49 ? 499 GLU A O   1 
ATOM   6942 C  CB  . GLU B 1 526 ? -29.003 -79.658 37.669  1.00 112.69 ? 499 GLU A CB  1 
ATOM   6943 N  N   . ASP B 1 527 ? -28.043 -77.100 38.641  1.00 111.89 ? 500 ASP A N   1 
ATOM   6944 C  CA  . ASP B 1 527 ? -26.952 -76.145 38.443  1.00 103.88 ? 500 ASP A CA  1 
ATOM   6945 C  C   . ASP B 1 527 ? -26.715 -75.091 39.552  1.00 95.57  ? 500 ASP A C   1 
ATOM   6946 O  O   . ASP B 1 527 ? -25.612 -74.558 39.665  1.00 80.10  ? 500 ASP A O   1 
ATOM   6947 C  CB  . ASP B 1 527 ? -27.217 -75.422 37.114  1.00 98.61  ? 500 ASP A CB  1 
ATOM   6948 C  CG  . ASP B 1 527 ? -25.966 -74.973 36.446  1.00 99.98  ? 500 ASP A CG  1 
ATOM   6949 O  OD1 . ASP B 1 527 ? -24.965 -74.762 37.162  1.00 102.81 ? 500 ASP A OD1 1 
ATOM   6950 O  OD2 . ASP B 1 527 ? -25.986 -74.832 35.201  1.00 106.56 ? 500 ASP A OD2 1 
ATOM   6951 N  N   . GLY B 1 528 ? -27.749 -74.755 40.324  1.00 92.51  ? 501 GLY A N   1 
ATOM   6952 C  CA  . GLY B 1 528 ? -27.683 -73.625 41.254  1.00 90.70  ? 501 GLY A CA  1 
ATOM   6953 C  C   . GLY B 1 528 ? -27.662 -72.262 40.552  1.00 93.59  ? 501 GLY A C   1 
ATOM   6954 O  O   . GLY B 1 528 ? -27.558 -71.209 41.218  1.00 87.79  ? 501 GLY A O   1 
ATOM   6955 N  N   . SER B 1 529 ? -27.758 -72.275 39.216  1.00 77.93  ? 502 SER A N   1 
ATOM   6956 C  CA  . SER B 1 529 ? -27.720 -71.059 38.426  1.00 75.50  ? 502 SER A CA  1 
ATOM   6957 C  C   . SER B 1 529 ? -29.147 -70.635 38.197  1.00 84.94  ? 502 SER A C   1 
ATOM   6958 O  O   . SER B 1 529 ? -30.079 -71.423 38.415  1.00 87.96  ? 502 SER A O   1 
ATOM   6959 C  CB  . SER B 1 529 ? -27.005 -71.268 37.079  1.00 73.48  ? 502 SER A CB  1 
ATOM   6960 O  OG  . SER B 1 529 ? -27.878 -71.688 36.036  1.00 63.78  ? 502 SER A OG  1 
ATOM   6961 N  N   . ILE B 1 530 ? -29.304 -69.394 37.738  1.00 81.19  ? 503 ILE A N   1 
ATOM   6962 C  CA  . ILE B 1 530 ? -30.606 -68.792 37.527  1.00 75.16  ? 503 ILE A CA  1 
ATOM   6963 C  C   . ILE B 1 530 ? -31.082 -69.068 36.113  1.00 74.02  ? 503 ILE A C   1 
ATOM   6964 O  O   . ILE B 1 530 ? -30.298 -69.061 35.172  1.00 80.19  ? 503 ILE A O   1 
ATOM   6965 C  CB  . ILE B 1 530 ? -30.564 -67.281 37.835  1.00 79.91  ? 503 ILE A CB  1 
ATOM   6966 C  CG1 . ILE B 1 530 ? -30.494 -67.093 39.358  1.00 83.43  ? 503 ILE A CG1 1 
ATOM   6967 C  CG2 . ILE B 1 530 ? -31.784 -66.561 37.274  1.00 80.10  ? 503 ILE A CG2 1 
ATOM   6968 C  CD1 . ILE B 1 530 ? -30.098 -65.709 39.819  1.00 82.69  ? 503 ILE A CD1 1 
ATOM   6969 N  N   . VAL B 1 531 ? -32.385 -69.288 35.993  1.00 73.25  ? 504 VAL A N   1 
ATOM   6970 C  CA  . VAL B 1 531 ? -33.006 -69.810 34.798  1.00 76.82  ? 504 VAL A CA  1 
ATOM   6971 C  C   . VAL B 1 531 ? -34.196 -68.931 34.419  1.00 78.16  ? 504 VAL A C   1 
ATOM   6972 O  O   . VAL B 1 531 ? -35.032 -68.572 35.270  1.00 69.68  ? 504 VAL A O   1 
ATOM   6973 C  CB  . VAL B 1 531 ? -33.517 -71.250 35.048  1.00 80.71  ? 504 VAL A CB  1 
ATOM   6974 C  CG1 . VAL B 1 531 ? -34.001 -71.898 33.754  1.00 84.35  ? 504 VAL A CG1 1 
ATOM   6975 C  CG2 . VAL B 1 531 ? -32.423 -72.088 35.688  1.00 84.59  ? 504 VAL A CG2 1 
ATOM   6976 N  N   . PHE B 1 532 ? -34.291 -68.605 33.137  1.00 70.16  ? 505 PHE A N   1 
ATOM   6977 C  CA  . PHE B 1 532 ? -35.371 -67.759 32.683  1.00 70.25  ? 505 PHE A CA  1 
ATOM   6978 C  C   . PHE B 1 532 ? -36.475 -68.641 32.103  1.00 68.64  ? 505 PHE A C   1 
ATOM   6979 O  O   . PHE B 1 532 ? -36.436 -69.033 30.947  1.00 63.55  ? 505 PHE A O   1 
ATOM   6980 C  CB  . PHE B 1 532 ? -34.842 -66.682 31.710  1.00 65.79  ? 505 PHE A CB  1 
ATOM   6981 C  CG  . PHE B 1 532 ? -33.694 -65.885 32.274  1.00 60.90  ? 505 PHE A CG  1 
ATOM   6982 C  CD1 . PHE B 1 532 ? -33.818 -65.225 33.490  1.00 63.52  ? 505 PHE A CD1 1 
ATOM   6983 C  CD2 . PHE B 1 532 ? -32.487 -65.831 31.623  1.00 62.55  ? 505 PHE A CD2 1 
ATOM   6984 C  CE1 . PHE B 1 532 ? -32.760 -64.508 34.032  1.00 62.88  ? 505 PHE A CE1 1 
ATOM   6985 C  CE2 . PHE B 1 532 ? -31.429 -65.123 32.156  1.00 62.85  ? 505 PHE A CE2 1 
ATOM   6986 C  CZ  . PHE B 1 532 ? -31.562 -64.456 33.355  1.00 62.76  ? 505 PHE A CZ  1 
ATOM   6987 N  N   . LYS B 1 533 ? -37.457 -68.950 32.939  1.00 71.55  ? 506 LYS A N   1 
ATOM   6988 C  CA  . LYS B 1 533 ? -38.586 -69.797 32.550  1.00 80.66  ? 506 LYS A CA  1 
ATOM   6989 C  C   . LYS B 1 533 ? -39.652 -68.927 31.907  1.00 73.44  ? 506 LYS A C   1 
ATOM   6990 O  O   . LYS B 1 533 ? -40.094 -67.969 32.531  1.00 75.71  ? 506 LYS A O   1 
ATOM   6991 C  CB  . LYS B 1 533 ? -39.177 -70.482 33.807  1.00 88.43  ? 506 LYS A CB  1 
ATOM   6992 C  CG  . LYS B 1 533 ? -39.869 -71.833 33.605  1.00 90.01  ? 506 LYS A CG  1 
ATOM   6993 C  CD  . LYS B 1 533 ? -40.795 -71.872 32.390  1.00 96.50  ? 506 LYS A CD  1 
ATOM   6994 C  CE  . LYS B 1 533 ? -41.858 -72.971 32.472  1.00 98.46  ? 506 LYS A CE  1 
ATOM   6995 N  NZ  . LYS B 1 533 ? -41.336 -74.347 32.717  1.00 99.91  ? 506 LYS A NZ  1 
ATOM   6996 N  N   . GLU B 1 534 ? -40.084 -69.255 30.687  1.00 73.45  ? 507 GLU A N   1 
ATOM   6997 C  CA  . GLU B 1 534 ? -41.219 -68.530 30.070  1.00 71.00  ? 507 GLU A CA  1 
ATOM   6998 C  C   . GLU B 1 534 ? -42.542 -68.854 30.749  1.00 72.62  ? 507 GLU A C   1 
ATOM   6999 O  O   . GLU B 1 534 ? -42.914 -70.021 30.881  1.00 83.95  ? 507 GLU A O   1 
ATOM   7000 C  CB  . GLU B 1 534 ? -41.402 -68.845 28.588  1.00 69.36  ? 507 GLU A CB  1 
ATOM   7001 C  CG  . GLU B 1 534 ? -42.587 -68.077 28.012  1.00 73.89  ? 507 GLU A CG  1 
ATOM   7002 C  CD  . GLU B 1 534 ? -43.026 -68.499 26.620  1.00 77.53  ? 507 GLU A CD  1 
ATOM   7003 O  OE1 . GLU B 1 534 ? -42.193 -68.506 25.674  1.00 71.68  ? 507 GLU A OE1 1 
ATOM   7004 O  OE2 . GLU B 1 534 ? -44.244 -68.775 26.480  1.00 85.76  ? 507 GLU A OE2 1 
ATOM   7005 N  N   . VAL B 1 535 ? -43.287 -67.823 31.127  1.00 66.22  ? 508 VAL A N   1 
ATOM   7006 C  CA  . VAL B 1 535 ? -44.562 -68.029 31.778  1.00 57.31  ? 508 VAL A CA  1 
ATOM   7007 C  C   . VAL B 1 535 ? -45.710 -67.248 31.161  1.00 60.10  ? 508 VAL A C   1 
ATOM   7008 O  O   . VAL B 1 535 ? -46.828 -67.251 31.686  1.00 61.84  ? 508 VAL A O   1 
ATOM   7009 C  CB  . VAL B 1 535 ? -44.442 -67.695 33.250  1.00 56.75  ? 508 VAL A CB  1 
ATOM   7010 C  CG1 . VAL B 1 535 ? -43.187 -68.358 33.802  1.00 55.71  ? 508 VAL A CG1 1 
ATOM   7011 C  CG2 . VAL B 1 535 ? -44.398 -66.184 33.444  1.00 63.52  ? 508 VAL A CG2 1 
ATOM   7012 N  N   . GLY B 1 536 ? -45.476 -66.596 30.033  1.00 58.51  ? 509 GLY A N   1 
ATOM   7013 C  CA  . GLY B 1 536 ? -46.574 -65.895 29.388  1.00 59.59  ? 509 GLY A CA  1 
ATOM   7014 C  C   . GLY B 1 536 ? -46.056 -65.252 28.134  1.00 61.70  ? 509 GLY A C   1 
ATOM   7015 O  O   . GLY B 1 536 ? -44.882 -65.426 27.802  1.00 60.36  ? 509 GLY A O   1 
ATOM   7016 N  N   . TYR B 1 537 ? -46.940 -64.552 27.429  1.00 62.75  ? 510 TYR A N   1 
ATOM   7017 C  CA  . TYR B 1 537 ? -46.573 -63.796 26.245  1.00 70.05  ? 510 TYR A CA  1 
ATOM   7018 C  C   . TYR B 1 537 ? -47.406 -62.508 26.206  1.00 70.01  ? 510 TYR A C   1 
ATOM   7019 O  O   . TYR B 1 537 ? -48.421 -62.389 26.929  1.00 66.37  ? 510 TYR A O   1 
ATOM   7020 C  CB  . TYR B 1 537 ? -46.715 -64.633 24.942  1.00 74.66  ? 510 TYR A CB  1 
ATOM   7021 C  CG  . TYR B 1 537 ? -48.096 -65.220 24.636  1.00 91.21  ? 510 TYR A CG  1 
ATOM   7022 C  CD1 . TYR B 1 537 ? -48.437 -66.529 25.040  1.00 99.96  ? 510 TYR A CD1 1 
ATOM   7023 C  CD2 . TYR B 1 537 ? -49.056 -64.490 23.912  1.00 98.83  ? 510 TYR A CD2 1 
ATOM   7024 C  CE1 . TYR B 1 537 ? -49.688 -67.072 24.751  1.00 96.43  ? 510 TYR A CE1 1 
ATOM   7025 C  CE2 . TYR B 1 537 ? -50.311 -65.029 23.621  1.00 94.31  ? 510 TYR A CE2 1 
ATOM   7026 C  CZ  . TYR B 1 537 ? -50.621 -66.312 24.042  1.00 96.28  ? 510 TYR A CZ  1 
ATOM   7027 O  OH  . TYR B 1 537 ? -51.861 -66.838 23.757  1.00 99.37  ? 510 TYR A OH  1 
ATOM   7028 N  N   . TYR B 1 538 ? -46.940 -61.538 25.410  1.00 59.20  ? 511 TYR A N   1 
ATOM   7029 C  CA  . TYR B 1 538 ? -47.704 -60.321 25.146  1.00 62.03  ? 511 TYR A CA  1 
ATOM   7030 C  C   . TYR B 1 538 ? -47.828 -60.181 23.646  1.00 60.65  ? 511 TYR A C   1 
ATOM   7031 O  O   . TYR B 1 538 ? -46.836 -60.076 22.958  1.00 61.38  ? 511 TYR A O   1 
ATOM   7032 C  CB  . TYR B 1 538 ? -47.032 -59.082 25.767  1.00 60.21  ? 511 TYR A CB  1 
ATOM   7033 C  CG  . TYR B 1 538 ? -47.917 -57.857 25.849  1.00 53.02  ? 511 TYR A CG  1 
ATOM   7034 C  CD1 . TYR B 1 538 ? -48.948 -57.786 26.790  1.00 57.72  ? 511 TYR A CD1 1 
ATOM   7035 C  CD2 . TYR B 1 538 ? -47.721 -56.766 25.007  1.00 51.76  ? 511 TYR A CD2 1 
ATOM   7036 C  CE1 . TYR B 1 538 ? -49.779 -56.673 26.873  1.00 59.50  ? 511 TYR A CE1 1 
ATOM   7037 C  CE2 . TYR B 1 538 ? -48.532 -55.640 25.098  1.00 55.82  ? 511 TYR A CE2 1 
ATOM   7038 C  CZ  . TYR B 1 538 ? -49.568 -55.610 26.034  1.00 57.85  ? 511 TYR A CZ  1 
ATOM   7039 O  OH  . TYR B 1 538 ? -50.382 -54.525 26.161  1.00 63.85  ? 511 TYR A OH  1 
ATOM   7040 N  N   . ASN B 1 539 ? -49.043 -60.241 23.132  1.00 65.37  ? 512 ASN A N   1 
ATOM   7041 C  CA  . ASN B 1 539 ? -49.226 -60.211 21.705  1.00 66.02  ? 512 ASN A CA  1 
ATOM   7042 C  C   . ASN B 1 539 ? -49.684 -58.832 21.376  1.00 63.35  ? 512 ASN A C   1 
ATOM   7043 O  O   . ASN B 1 539 ? -50.787 -58.443 21.735  1.00 60.99  ? 512 ASN A O   1 
ATOM   7044 C  CB  . ASN B 1 539 ? -50.238 -61.265 21.248  1.00 70.83  ? 512 ASN A CB  1 
ATOM   7045 C  CG  . ASN B 1 539 ? -50.698 -61.068 19.799  1.00 70.55  ? 512 ASN A CG  1 
ATOM   7046 O  OD1 . ASN B 1 539 ? -49.968 -60.572 18.942  1.00 74.21  ? 512 ASN A OD1 1 
ATOM   7047 N  ND2 . ASN B 1 539 ? -51.920 -61.465 19.529  1.00 67.91  ? 512 ASN A ND2 1 
ATOM   7048 N  N   . VAL B 1 540 ? -48.818 -58.119 20.668  1.00 66.54  ? 513 VAL A N   1 
ATOM   7049 C  CA  . VAL B 1 540 ? -48.986 -56.712 20.326  1.00 67.31  ? 513 VAL A CA  1 
ATOM   7050 C  C   . VAL B 1 540 ? -50.087 -56.482 19.274  1.00 72.42  ? 513 VAL A C   1 
ATOM   7051 O  O   . VAL B 1 540 ? -50.643 -55.380 19.183  1.00 70.48  ? 513 VAL A O   1 
ATOM   7052 C  CB  . VAL B 1 540 ? -47.619 -56.166 19.849  1.00 70.42  ? 513 VAL A CB  1 
ATOM   7053 C  CG1 . VAL B 1 540 ? -47.748 -54.855 19.099  1.00 78.83  ? 513 VAL A CG1 1 
ATOM   7054 C  CG2 . VAL B 1 540 ? -46.699 -56.014 21.039  1.00 69.99  ? 513 VAL A CG2 1 
ATOM   7055 N  N   . TYR B 1 541 ? -50.430 -57.523 18.510  1.00 77.83  ? 514 TYR A N   1 
ATOM   7056 C  CA  . TYR B 1 541 ? -51.448 -57.418 17.435  1.00 81.64  ? 514 TYR A CA  1 
ATOM   7057 C  C   . TYR B 1 541 ? -52.886 -57.568 17.915  1.00 77.61  ? 514 TYR A C   1 
ATOM   7058 O  O   . TYR B 1 541 ? -53.799 -57.013 17.315  1.00 90.54  ? 514 TYR A O   1 
ATOM   7059 C  CB  . TYR B 1 541 ? -51.164 -58.424 16.319  1.00 84.03  ? 514 TYR A CB  1 
ATOM   7060 C  CG  . TYR B 1 541 ? -49.785 -58.237 15.733  1.00 88.14  ? 514 TYR A CG  1 
ATOM   7061 C  CD1 . TYR B 1 541 ? -49.572 -57.381 14.650  1.00 83.96  ? 514 TYR A CD1 1 
ATOM   7062 C  CD2 . TYR B 1 541 ? -48.681 -58.883 16.301  1.00 89.44  ? 514 TYR A CD2 1 
ATOM   7063 C  CE1 . TYR B 1 541 ? -48.301 -57.204 14.132  1.00 88.35  ? 514 TYR A CE1 1 
ATOM   7064 C  CE2 . TYR B 1 541 ? -47.412 -58.710 15.800  1.00 88.37  ? 514 TYR A CE2 1 
ATOM   7065 C  CZ  . TYR B 1 541 ? -47.225 -57.879 14.718  1.00 91.13  ? 514 TYR A CZ  1 
ATOM   7066 O  OH  . TYR B 1 541 ? -45.947 -57.739 14.256  1.00 88.78  ? 514 TYR A OH  1 
ATOM   7067 N  N   . ALA B 1 542 ? -53.082 -58.299 19.005  1.00 77.92  ? 515 ALA A N   1 
ATOM   7068 C  CA  . ALA B 1 542 ? -54.396 -58.425 19.650  1.00 70.82  ? 515 ALA A CA  1 
ATOM   7069 C  C   . ALA B 1 542 ? -54.953 -57.084 20.133  1.00 69.83  ? 515 ALA A C   1 
ATOM   7070 O  O   . ALA B 1 542 ? -54.201 -56.166 20.410  1.00 73.79  ? 515 ALA A O   1 
ATOM   7071 C  CB  . ALA B 1 542 ? -54.300 -59.387 20.816  1.00 70.83  ? 515 ALA A CB  1 
ATOM   7072 N  N   . LYS B 1 543 ? -56.275 -56.987 20.241  1.00 73.93  ? 516 LYS A N   1 
ATOM   7073 C  CA  . LYS B 1 543 ? -56.935 -55.739 20.656  1.00 79.15  ? 516 LYS A CA  1 
ATOM   7074 C  C   . LYS B 1 543 ? -56.649 -55.411 22.139  1.00 78.48  ? 516 LYS A C   1 
ATOM   7075 O  O   . LYS B 1 543 ? -56.312 -56.309 22.920  1.00 75.38  ? 516 LYS A O   1 
ATOM   7076 C  CB  . LYS B 1 543 ? -58.456 -55.808 20.380  1.00 72.43  ? 516 LYS A CB  1 
ATOM   7077 N  N   . LYS B 1 544 ? -56.784 -54.126 22.503  1.00 77.47  ? 517 LYS A N   1 
ATOM   7078 C  CA  . LYS B 1 544 ? -56.578 -53.636 23.882  1.00 72.73  ? 517 LYS A CA  1 
ATOM   7079 C  C   . LYS B 1 544 ? -57.364 -54.507 24.869  1.00 76.67  ? 517 LYS A C   1 
ATOM   7080 O  O   . LYS B 1 544 ? -58.516 -54.812 24.615  1.00 77.30  ? 517 LYS A O   1 
ATOM   7081 C  CB  . LYS B 1 544 ? -57.005 -52.162 24.008  1.00 62.47  ? 517 LYS A CB  1 
ATOM   7082 N  N   . GLY B 1 545 ? -56.731 -54.928 25.966  1.00 78.04  ? 518 GLY A N   1 
ATOM   7083 C  CA  . GLY B 1 545 ? -57.378 -55.777 26.974  1.00 75.74  ? 518 GLY A CA  1 
ATOM   7084 C  C   . GLY B 1 545 ? -57.243 -57.279 26.725  1.00 77.38  ? 518 GLY A C   1 
ATOM   7085 O  O   . GLY B 1 545 ? -57.540 -58.072 27.609  1.00 72.54  ? 518 GLY A O   1 
ATOM   7086 N  N   . GLU B 1 546 ? -56.788 -57.669 25.531  1.00 82.14  ? 519 GLU A N   1 
ATOM   7087 C  CA  . GLU B 1 546 ? -56.680 -59.087 25.127  1.00 80.20  ? 519 GLU A CA  1 
ATOM   7088 C  C   . GLU B 1 546 ? -55.273 -59.419 24.593  1.00 76.89  ? 519 GLU A C   1 
ATOM   7089 O  O   . GLU B 1 546 ? -55.109 -60.274 23.718  1.00 72.32  ? 519 GLU A O   1 
ATOM   7090 C  CB  . GLU B 1 546 ? -57.732 -59.391 24.045  1.00 77.80  ? 519 GLU A CB  1 
ATOM   7091 N  N   . ARG B 1 547 ? -54.263 -58.731 25.120  1.00 74.40  ? 520 ARG A N   1 
ATOM   7092 C  CA  . ARG B 1 547 ? -52.891 -58.860 24.628  1.00 68.34  ? 520 ARG A CA  1 
ATOM   7093 C  C   . ARG B 1 547 ? -52.032 -59.681 25.556  1.00 63.66  ? 520 ARG A C   1 
ATOM   7094 O  O   . ARG B 1 547 ? -51.117 -60.358 25.109  1.00 59.90  ? 520 ARG A O   1 
ATOM   7095 C  CB  . ARG B 1 547 ? -52.249 -57.489 24.499  1.00 70.72  ? 520 ARG A CB  1 
ATOM   7096 C  CG  . ARG B 1 547 ? -53.019 -56.551 23.601  1.00 65.19  ? 520 ARG A CG  1 
ATOM   7097 C  CD  . ARG B 1 547 ? -52.073 -55.728 22.787  1.00 61.97  ? 520 ARG A CD  1 
ATOM   7098 N  NE  . ARG B 1 547 ? -52.825 -54.753 22.035  1.00 69.40  ? 520 ARG A NE  1 
ATOM   7099 C  CZ  . ARG B 1 547 ? -52.907 -53.456 22.314  1.00 70.31  ? 520 ARG A CZ  1 
ATOM   7100 N  NH1 . ARG B 1 547 ? -52.257 -52.910 23.350  1.00 78.26  ? 520 ARG A NH1 1 
ATOM   7101 N  NH2 . ARG B 1 547 ? -53.638 -52.697 21.524  1.00 60.80  ? 520 ARG A NH2 1 
ATOM   7102 N  N   . LEU B 1 548 ? -52.310 -59.591 26.850  1.00 62.66  ? 521 LEU A N   1 
ATOM   7103 C  CA  . LEU B 1 548 ? -51.573 -60.352 27.855  1.00 59.83  ? 521 LEU A CA  1 
ATOM   7104 C  C   . LEU B 1 548 ? -52.098 -61.779 27.978  1.00 62.97  ? 521 LEU A C   1 
ATOM   7105 O  O   . LEU B 1 548 ? -53.292 -62.017 27.896  1.00 66.97  ? 521 LEU A O   1 
ATOM   7106 C  CB  . LEU B 1 548 ? -51.705 -59.676 29.216  1.00 53.71  ? 521 LEU A CB  1 
ATOM   7107 C  CG  . LEU B 1 548 ? -51.040 -60.379 30.403  1.00 54.05  ? 521 LEU A CG  1 
ATOM   7108 C  CD1 . LEU B 1 548 ? -49.547 -60.616 30.224  1.00 48.96  ? 521 LEU A CD1 1 
ATOM   7109 C  CD2 . LEU B 1 548 ? -51.309 -59.579 31.666  1.00 57.34  ? 521 LEU A CD2 1 
ATOM   7110 N  N   . PHE B 1 549 ? -51.184 -62.718 28.175  1.00 63.86  ? 522 PHE A N   1 
ATOM   7111 C  CA  . PHE B 1 549 ? -51.529 -64.046 28.584  1.00 62.45  ? 522 PHE A CA  1 
ATOM   7112 C  C   . PHE B 1 549 ? -50.528 -64.484 29.628  1.00 60.47  ? 522 PHE A C   1 
ATOM   7113 O  O   . PHE B 1 549 ? -49.341 -64.318 29.418  1.00 69.68  ? 522 PHE A O   1 
ATOM   7114 C  CB  . PHE B 1 549 ? -51.473 -64.984 27.382  1.00 67.58  ? 522 PHE A CB  1 
ATOM   7115 C  CG  . PHE B 1 549 ? -51.601 -66.438 27.749  1.00 78.41  ? 522 PHE A CG  1 
ATOM   7116 C  CD1 . PHE B 1 549 ? -52.858 -67.006 27.948  1.00 75.41  ? 522 PHE A CD1 1 
ATOM   7117 C  CD2 . PHE B 1 549 ? -50.463 -67.234 27.930  1.00 81.33  ? 522 PHE A CD2 1 
ATOM   7118 C  CE1 . PHE B 1 549 ? -52.981 -68.335 28.294  1.00 75.71  ? 522 PHE A CE1 1 
ATOM   7119 C  CE2 . PHE B 1 549 ? -50.587 -68.563 28.283  1.00 81.39  ? 522 PHE A CE2 1 
ATOM   7120 C  CZ  . PHE B 1 549 ? -51.852 -69.111 28.455  1.00 82.63  ? 522 PHE A CZ  1 
ATOM   7121 N  N   . ILE B 1 550 ? -51.002 -65.072 30.724  1.00 63.95  ? 523 ILE A N   1 
ATOM   7122 C  CA  . ILE B 1 550 ? -50.135 -65.606 31.781  1.00 69.53  ? 523 ILE A CA  1 
ATOM   7123 C  C   . ILE B 1 550 ? -50.605 -66.975 32.285  1.00 73.44  ? 523 ILE A C   1 
ATOM   7124 O  O   . ILE B 1 550 ? -51.795 -67.163 32.510  1.00 81.45  ? 523 ILE A O   1 
ATOM   7125 C  CB  . ILE B 1 550 ? -50.102 -64.653 32.983  1.00 76.42  ? 523 ILE A CB  1 
ATOM   7126 C  CG1 . ILE B 1 550 ? -49.577 -63.289 32.547  1.00 85.33  ? 523 ILE A CG1 1 
ATOM   7127 C  CG2 . ILE B 1 550 ? -49.247 -65.230 34.109  1.00 80.54  ? 523 ILE A CG2 1 
ATOM   7128 C  CD1 . ILE B 1 550 ? -49.116 -62.405 33.690  1.00 90.58  ? 523 ILE A CD1 1 
ATOM   7129 N  N   . ASN B 1 551 ? -49.668 -67.912 32.467  1.00 77.30  ? 524 ASN A N   1 
ATOM   7130 C  CA  . ASN B 1 551 ? -49.936 -69.176 33.153  1.00 83.30  ? 524 ASN A CA  1 
ATOM   7131 C  C   . ASN B 1 551 ? -49.548 -69.072 34.597  1.00 74.66  ? 524 ASN A C   1 
ATOM   7132 O  O   . ASN B 1 551 ? -48.399 -69.342 34.932  1.00 75.99  ? 524 ASN A O   1 
ATOM   7133 C  CB  . ASN B 1 551 ? -49.160 -70.351 32.542  1.00 94.60  ? 524 ASN A CB  1 
ATOM   7134 C  CG  . ASN B 1 551 ? -49.701 -70.768 31.195  1.00 115.57 ? 524 ASN A CG  1 
ATOM   7135 O  OD1 . ASN B 1 551 ? -50.821 -70.417 30.835  1.00 138.41 ? 524 ASN A OD1 1 
ATOM   7136 N  ND2 . ASN B 1 551 ? -48.907 -71.519 30.439  1.00 126.27 ? 524 ASN A ND2 1 
ATOM   7137 N  N   . GLU B 1 552 ? -50.505 -68.714 35.455  1.00 75.17  ? 525 GLU A N   1 
ATOM   7138 C  CA  . GLU B 1 552 ? -50.270 -68.655 36.915  1.00 71.87  ? 525 GLU A CA  1 
ATOM   7139 C  C   . GLU B 1 552 ? -49.537 -69.887 37.444  1.00 70.42  ? 525 GLU A C   1 
ATOM   7140 O  O   . GLU B 1 552 ? -48.584 -69.747 38.208  1.00 70.40  ? 525 GLU A O   1 
ATOM   7141 C  CB  . GLU B 1 552 ? -51.576 -68.513 37.699  1.00 74.17  ? 525 GLU A CB  1 
ATOM   7142 C  CG  . GLU B 1 552 ? -52.146 -67.108 37.848  1.00 80.01  ? 525 GLU A CG  1 
ATOM   7143 C  CD  . GLU B 1 552 ? -53.367 -66.868 36.978  1.00 86.14  ? 525 GLU A CD  1 
ATOM   7144 O  OE1 . GLU B 1 552 ? -53.305 -67.205 35.761  1.00 93.03  ? 525 GLU A OE1 1 
ATOM   7145 O  OE2 . GLU B 1 552 ? -54.375 -66.337 37.519  1.00 80.70  ? 525 GLU A OE2 1 
ATOM   7146 N  N   . GLU B 1 553 ? -49.969 -71.083 37.026  1.00 70.89  ? 526 GLU A N   1 
ATOM   7147 C  CA  . GLU B 1 553 ? -49.370 -72.345 37.503  1.00 73.80  ? 526 GLU A CA  1 
ATOM   7148 C  C   . GLU B 1 553 ? -47.833 -72.409 37.282  1.00 77.86  ? 526 GLU A C   1 
ATOM   7149 O  O   . GLU B 1 553 ? -47.103 -73.011 38.092  1.00 74.57  ? 526 GLU A O   1 
ATOM   7150 C  CB  . GLU B 1 553 ? -50.067 -73.553 36.852  1.00 74.54  ? 526 GLU A CB  1 
ATOM   7151 N  N   . LYS B 1 554 ? -47.351 -71.761 36.213  1.00 74.80  ? 527 LYS A N   1 
ATOM   7152 C  CA  . LYS B 1 554 ? -45.930 -71.748 35.875  1.00 68.65  ? 527 LYS A CA  1 
ATOM   7153 C  C   . LYS B 1 554 ? -45.064 -70.788 36.738  1.00 71.92  ? 527 LYS A C   1 
ATOM   7154 O  O   . LYS B 1 554 ? -43.822 -70.883 36.687  1.00 71.87  ? 527 LYS A O   1 
ATOM   7155 C  CB  . LYS B 1 554 ? -45.754 -71.466 34.374  1.00 66.87  ? 527 LYS A CB  1 
ATOM   7156 N  N   . ILE B 1 555 ? -45.683 -69.923 37.559  1.00 68.66  ? 528 ILE A N   1 
ATOM   7157 C  CA  . ILE B 1 555 ? -44.927 -68.889 38.333  1.00 70.55  ? 528 ILE A CA  1 
ATOM   7158 C  C   . ILE B 1 555 ? -44.461 -69.377 39.687  1.00 63.35  ? 528 ILE A C   1 
ATOM   7159 O  O   . ILE B 1 555 ? -45.267 -69.782 40.503  1.00 76.09  ? 528 ILE A O   1 
ATOM   7160 C  CB  . ILE B 1 555 ? -45.754 -67.566 38.576  1.00 71.11  ? 528 ILE A CB  1 
ATOM   7161 C  CG1 . ILE B 1 555 ? -45.937 -66.776 37.276  1.00 71.69  ? 528 ILE A CG1 1 
ATOM   7162 C  CG2 . ILE B 1 555 ? -45.096 -66.629 39.593  1.00 63.36  ? 528 ILE A CG2 1 
ATOM   7163 C  CD1 . ILE B 1 555 ? -47.167 -65.893 37.287  1.00 71.54  ? 528 ILE A CD1 1 
ATOM   7164 N  N   . LEU B 1 556 ? -43.167 -69.298 39.942  1.00 63.40  ? 529 LEU A N   1 
ATOM   7165 C  CA  . LEU B 1 556 ? -42.649 -69.447 41.293  1.00 68.90  ? 529 LEU A CA  1 
ATOM   7166 C  C   . LEU B 1 556 ? -42.393 -68.099 41.959  1.00 71.05  ? 529 LEU A C   1 
ATOM   7167 O  O   . LEU B 1 556 ? -41.552 -67.302 41.486  1.00 75.73  ? 529 LEU A O   1 
ATOM   7168 C  CB  . LEU B 1 556 ? -41.381 -70.299 41.272  1.00 78.65  ? 529 LEU A CB  1 
ATOM   7169 C  CG  . LEU B 1 556 ? -41.552 -71.712 40.672  1.00 81.29  ? 529 LEU A CG  1 
ATOM   7170 C  CD1 . LEU B 1 556 ? -40.251 -72.478 40.874  1.00 83.79  ? 529 LEU A CD1 1 
ATOM   7171 C  CD2 . LEU B 1 556 ? -42.729 -72.486 41.284  1.00 74.36  ? 529 LEU A CD2 1 
ATOM   7172 N  N   . TRP B 1 557 ? -43.060 -67.885 43.097  1.00 66.97  ? 530 TRP A N   1 
ATOM   7173 C  CA  . TRP B 1 557 ? -43.278 -66.543 43.618  1.00 67.28  ? 530 TRP A CA  1 
ATOM   7174 C  C   . TRP B 1 557 ? -42.135 -65.799 44.294  1.00 73.14  ? 530 TRP A C   1 
ATOM   7175 O  O   . TRP B 1 557 ? -42.169 -64.573 44.392  1.00 98.25  ? 530 TRP A O   1 
ATOM   7176 C  CB  . TRP B 1 557 ? -44.566 -66.471 44.440  1.00 62.84  ? 530 TRP A CB  1 
ATOM   7177 C  CG  . TRP B 1 557 ? -45.730 -66.334 43.524  1.00 65.51  ? 530 TRP A CG  1 
ATOM   7178 C  CD1 . TRP B 1 557 ? -46.684 -67.261 43.267  1.00 65.15  ? 530 TRP A CD1 1 
ATOM   7179 C  CD2 . TRP B 1 557 ? -46.016 -65.218 42.684  1.00 63.83  ? 530 TRP A CD2 1 
ATOM   7180 N  NE1 . TRP B 1 557 ? -47.563 -66.790 42.331  1.00 61.76  ? 530 TRP A NE1 1 
ATOM   7181 C  CE2 . TRP B 1 557 ? -47.176 -65.534 41.958  1.00 63.07  ? 530 TRP A CE2 1 
ATOM   7182 C  CE3 . TRP B 1 557 ? -45.389 -63.983 42.462  1.00 66.33  ? 530 TRP A CE3 1 
ATOM   7183 C  CZ2 . TRP B 1 557 ? -47.739 -64.656 41.036  1.00 65.94  ? 530 TRP A CZ2 1 
ATOM   7184 C  CZ3 . TRP B 1 557 ? -45.928 -63.119 41.536  1.00 59.94  ? 530 TRP A CZ3 1 
ATOM   7185 C  CH2 . TRP B 1 557 ? -47.096 -63.456 40.839  1.00 67.99  ? 530 TRP A CH2 1 
ATOM   7186 N  N   . SER B 1 558 ? -41.103 -66.465 44.737  1.00 69.27  ? 531 SER A N   1 
ATOM   7187 C  CA  . SER B 1 558 ? -39.886 -65.692 44.992  1.00 68.78  ? 531 SER A CA  1 
ATOM   7188 C  C   . SER B 1 558 ? -38.763 -66.524 44.465  1.00 72.44  ? 531 SER A C   1 
ATOM   7189 O  O   . SER B 1 558 ? -37.688 -66.626 45.075  1.00 76.51  ? 531 SER A O   1 
ATOM   7190 C  CB  . SER B 1 558 ? -39.726 -65.331 46.467  1.00 64.03  ? 531 SER A CB  1 
ATOM   7191 O  OG  . SER B 1 558 ? -40.717 -64.393 46.827  1.00 58.09  ? 531 SER A OG  1 
ATOM   7192 N  N   . GLY B 1 559 ? -39.052 -67.101 43.299  1.00 72.24  ? 532 GLY A N   1 
ATOM   7193 C  CA  . GLY B 1 559 ? -38.187 -68.054 42.641  1.00 78.85  ? 532 GLY A CA  1 
ATOM   7194 C  C   . GLY B 1 559 ? -38.542 -69.503 42.898  1.00 83.03  ? 532 GLY A C   1 
ATOM   7195 O  O   . GLY B 1 559 ? -38.112 -70.375 42.133  1.00 90.78  ? 532 GLY A O   1 
ATOM   7196 N  N   . PHE B 1 560 ? -39.322 -69.759 43.959  1.00 86.01  ? 533 PHE A N   1 
ATOM   7197 C  CA  . PHE B 1 560 ? -39.544 -71.124 44.468  1.00 84.64  ? 533 PHE A CA  1 
ATOM   7198 C  C   . PHE B 1 560 ? -40.990 -71.552 44.763  1.00 84.81  ? 533 PHE A C   1 
ATOM   7199 O  O   . PHE B 1 560 ? -41.334 -72.715 44.528  1.00 92.19  ? 533 PHE A O   1 
ATOM   7200 C  CB  . PHE B 1 560 ? -38.684 -71.355 45.722  1.00 86.15  ? 533 PHE A CB  1 
ATOM   7201 C  CG  . PHE B 1 560 ? -39.038 -70.472 46.891  1.00 90.06  ? 533 PHE A CG  1 
ATOM   7202 C  CD1 . PHE B 1 560 ? -40.050 -70.847 47.799  1.00 85.65  ? 533 PHE A CD1 1 
ATOM   7203 C  CD2 . PHE B 1 560 ? -38.345 -69.279 47.112  1.00 90.33  ? 533 PHE A CD2 1 
ATOM   7204 C  CE1 . PHE B 1 560 ? -40.367 -70.040 48.885  1.00 82.16  ? 533 PHE A CE1 1 
ATOM   7205 C  CE2 . PHE B 1 560 ? -38.661 -68.462 48.200  1.00 90.53  ? 533 PHE A CE2 1 
ATOM   7206 C  CZ  . PHE B 1 560 ? -39.673 -68.842 49.085  1.00 87.92  ? 533 PHE A CZ  1 
ATOM   7207 N  N   . SER B 1 561 ? -41.822 -70.626 45.260  1.00 81.29  ? 534 SER A N   1 
ATOM   7208 C  CA  . SER B 1 561 ? -43.142 -70.937 45.862  1.00 64.99  ? 534 SER A CA  1 
ATOM   7209 C  C   . SER B 1 561 ? -44.309 -71.009 44.878  1.00 62.29  ? 534 SER A C   1 
ATOM   7210 O  O   . SER B 1 561 ? -44.509 -70.081 44.111  1.00 63.07  ? 534 SER A O   1 
ATOM   7211 C  CB  . SER B 1 561 ? -43.456 -69.880 46.910  1.00 64.43  ? 534 SER A CB  1 
ATOM   7212 O  OG  . SER B 1 561 ? -44.774 -70.002 47.390  1.00 64.95  ? 534 SER A OG  1 
ATOM   7213 N  N   . ARG B 1 562 ? -45.081 -72.110 44.901  1.00 66.85  ? 535 ARG A N   1 
ATOM   7214 C  CA  . ARG B 1 562 ? -46.294 -72.242 44.070  1.00 60.25  ? 535 ARG A CA  1 
ATOM   7215 C  C   . ARG B 1 562 ? -47.562 -71.811 44.857  1.00 58.94  ? 535 ARG A C   1 
ATOM   7216 O  O   . ARG B 1 562 ? -48.650 -71.703 44.295  1.00 59.05  ? 535 ARG A O   1 
ATOM   7217 C  CB  . ARG B 1 562 ? -46.406 -73.650 43.464  1.00 51.01  ? 535 ARG A CB  1 
ATOM   7218 N  N   . GLU B 1 563 ? -47.402 -71.491 46.135  1.00 60.99  ? 536 GLU A N   1 
ATOM   7219 C  CA  . GLU B 1 563 ? -48.523 -71.126 46.999  1.00 70.90  ? 536 GLU A CA  1 
ATOM   7220 C  C   . GLU B 1 563 ? -48.695 -69.584 47.112  1.00 75.86  ? 536 GLU A C   1 
ATOM   7221 O  O   . GLU B 1 563 ? -48.049 -68.957 47.941  1.00 73.13  ? 536 GLU A O   1 
ATOM   7222 C  CB  . GLU B 1 563 ? -48.295 -71.752 48.383  1.00 69.36  ? 536 GLU A CB  1 
ATOM   7223 N  N   . VAL B 1 564 ? -49.554 -68.980 46.281  1.00 77.45  ? 537 VAL A N   1 
ATOM   7224 C  CA  . VAL B 1 564 ? -49.760 -67.507 46.281  1.00 75.50  ? 537 VAL A CA  1 
ATOM   7225 C  C   . VAL B 1 564 ? -50.719 -66.994 47.392  1.00 69.35  ? 537 VAL A C   1 
ATOM   7226 O  O   . VAL B 1 564 ? -51.732 -67.614 47.701  1.00 64.92  ? 537 VAL A O   1 
ATOM   7227 C  CB  . VAL B 1 564 ? -50.230 -66.972 44.890  1.00 60.29  ? 537 VAL A CB  1 
ATOM   7228 N  N   . PRO B 1 565 ? -50.388 -65.827 47.955  1.00 68.25  ? 538 PRO A N   1 
ATOM   7229 C  CA  . PRO B 1 565 ? -50.645 -64.752 48.903  1.00 72.64  ? 538 PRO A CA  1 
ATOM   7230 C  C   . PRO B 1 565 ? -49.568 -64.753 49.993  1.00 71.55  ? 538 PRO A C   1 
ATOM   7231 O  O   . PRO B 1 565 ? -49.027 -65.819 50.329  1.00 65.57  ? 538 PRO A O   1 
ATOM   7232 C  CB  . PRO B 1 565 ? -52.055 -65.070 49.434  1.00 68.87  ? 538 PRO A CB  1 
HETATM 7233 GD GD  . GD3 C 2 .   ? -39.773 -31.315 47.816  1.00 107.06 ? 601 GD3 B GD  1 
HETATM 7234 MG MG  . MG  D 3 .   ? -49.912 -38.090 30.824  1.00 62.84  ? 602 MG  B MG  1 
HETATM 7235 MG MG  . MG  E 3 .   ? -9.937  -5.720  26.937  1.00 77.41  ? 603 MG  B MG  1 
HETATM 7236 C  C   . BCT F 4 .   ? -34.720 -10.503 28.114  1.00 56.51  ? 604 BCT B C   1 
HETATM 7237 O  O1  . BCT F 4 .   ? -35.140 -11.094 27.098  1.00 57.47  ? 604 BCT B O1  1 
HETATM 7238 O  O2  . BCT F 4 .   ? -35.164 -10.797 29.232  1.00 64.57  ? 604 BCT B O2  1 
HETATM 7239 O  O3  . BCT F 4 .   ? -33.803 -9.539  28.041  1.00 45.12  ? 604 BCT B O3  1 
HETATM 7240 CL CL  . CL  G 5 .   ? -30.442 -21.189 20.727  1.00 71.17  ? 605 CL  B CL  1 
HETATM 7241 C  C1  . NAG H 6 .   ? -64.524 -35.634 25.637  1.00 105.01 ? 606 NAG B C1  1 
HETATM 7242 C  C2  . NAG H 6 .   ? -63.931 -36.927 25.062  1.00 115.70 ? 606 NAG B C2  1 
HETATM 7243 C  C3  . NAG H 6 .   ? -64.798 -37.347 23.883  1.00 122.49 ? 606 NAG B C3  1 
HETATM 7244 C  C4  . NAG H 6 .   ? -66.204 -37.665 24.396  1.00 125.99 ? 606 NAG B C4  1 
HETATM 7245 C  C5  . NAG H 6 .   ? -66.829 -36.439 25.096  1.00 121.79 ? 606 NAG B C5  1 
HETATM 7246 C  C6  . NAG H 6 .   ? -68.067 -36.825 25.930  1.00 112.08 ? 606 NAG B C6  1 
HETATM 7247 C  C7  . NAG H 6 .   ? -61.456 -37.060 25.376  1.00 106.92 ? 606 NAG B C7  1 
HETATM 7248 C  C8  . NAG H 6 .   ? -60.119 -36.921 24.705  1.00 104.56 ? 606 NAG B C8  1 
HETATM 7249 N  N2  . NAG H 6 .   ? -62.540 -36.831 24.607  1.00 112.31 ? 606 NAG B N2  1 
HETATM 7250 O  O3  . NAG H 6 .   ? -64.211 -38.457 23.241  1.00 126.46 ? 606 NAG B O3  1 
HETATM 7251 O  O4  . NAG H 6 .   ? -67.030 -38.108 23.335  1.00 108.21 ? 606 NAG B O4  1 
HETATM 7252 O  O5  . NAG H 6 .   ? -65.917 -35.727 25.934  1.00 113.38 ? 606 NAG B O5  1 
HETATM 7253 O  O6  . NAG H 6 .   ? -67.801 -36.795 27.323  1.00 88.70  ? 606 NAG B O6  1 
HETATM 7254 O  O7  . NAG H 6 .   ? -61.474 -37.359 26.572  1.00 92.59  ? 606 NAG B O7  1 
HETATM 7255 C  C1  . NAG I 6 .   ? -66.267 -16.434 23.927  1.00 113.87 ? 607 NAG B C1  1 
HETATM 7256 C  C2  . NAG I 6 .   ? -67.226 -15.841 22.891  1.00 124.27 ? 607 NAG B C2  1 
HETATM 7257 C  C3  . NAG I 6 .   ? -67.996 -14.643 23.438  1.00 131.87 ? 607 NAG B C3  1 
HETATM 7258 C  C4  . NAG I 6 .   ? -68.542 -14.968 24.833  1.00 128.00 ? 607 NAG B C4  1 
HETATM 7259 C  C5  . NAG I 6 .   ? -67.400 -15.438 25.743  1.00 123.13 ? 607 NAG B C5  1 
HETATM 7260 C  C6  . NAG I 6 .   ? -67.826 -15.647 27.204  1.00 121.28 ? 607 NAG B C6  1 
HETATM 7261 C  C7  . NAG I 6 .   ? -66.661 -16.082 20.518  1.00 123.03 ? 607 NAG B C7  1 
HETATM 7262 C  C8  . NAG I 6 .   ? -65.762 -15.642 19.396  1.00 115.87 ? 607 NAG B C8  1 
HETATM 7263 N  N2  . NAG I 6 .   ? -66.452 -15.500 21.705  1.00 120.37 ? 607 NAG B N2  1 
HETATM 7264 O  O3  . NAG I 6 .   ? -69.046 -14.326 22.545  1.00 133.64 ? 607 NAG B O3  1 
HETATM 7265 O  O4  . NAG I 6 .   ? -69.183 -13.840 25.390  1.00 121.23 ? 607 NAG B O4  1 
HETATM 7266 O  O5  . NAG I 6 .   ? -66.859 -16.622 25.197  1.00 112.20 ? 607 NAG B O5  1 
HETATM 7267 O  O6  . NAG I 6 .   ? -67.850 -17.008 27.581  1.00 109.21 ? 607 NAG B O6  1 
HETATM 7268 O  O7  . NAG I 6 .   ? -67.539 -16.931 20.314  1.00 115.73 ? 607 NAG B O7  1 
HETATM 7269 C  C1  . NAG J 6 .   ? -16.765 -15.386 46.954  1.00 59.22  ? 608 NAG B C1  1 
HETATM 7270 C  C2  . NAG J 6 .   ? -16.803 -16.562 47.919  1.00 59.42  ? 608 NAG B C2  1 
HETATM 7271 C  C3  . NAG J 6 .   ? -17.504 -16.140 49.222  1.00 68.35  ? 608 NAG B C3  1 
HETATM 7272 C  C4  . NAG J 6 .   ? -16.783 -14.954 49.811  1.00 61.15  ? 608 NAG B C4  1 
HETATM 7273 C  C5  . NAG J 6 .   ? -16.699 -13.828 48.807  1.00 62.71  ? 608 NAG B C5  1 
HETATM 7274 C  C6  . NAG J 6 .   ? -15.931 -12.717 49.502  1.00 60.47  ? 608 NAG B C6  1 
HETATM 7275 C  C7  . NAG J 6 .   ? -16.891 -18.941 47.287  1.00 72.29  ? 608 NAG B C7  1 
HETATM 7276 C  C8  . NAG J 6 .   ? -17.723 -20.076 46.774  1.00 81.31  ? 608 NAG B C8  1 
HETATM 7277 N  N2  . NAG J 6 .   ? -17.477 -17.740 47.409  1.00 62.85  ? 608 NAG B N2  1 
HETATM 7278 O  O3  . NAG J 6 .   ? -17.611 -17.127 50.261  1.00 71.12  ? 608 NAG B O3  1 
HETATM 7279 O  O4  . NAG J 6 .   ? -17.591 -14.500 50.853  1.00 63.73  ? 608 NAG B O4  1 
HETATM 7280 O  O5  . NAG J 6 .   ? -16.137 -14.246 47.555  1.00 60.57  ? 608 NAG B O5  1 
HETATM 7281 O  O6  . NAG J 6 .   ? -15.378 -11.903 48.506  1.00 69.12  ? 608 NAG B O6  1 
HETATM 7282 O  O7  . NAG J 6 .   ? -15.719 -19.188 47.531  1.00 79.51  ? 608 NAG B O7  1 
HETATM 7283 N  N   . TCR K 7 .   ? -35.033 -22.676 29.569  1.00 47.51  ? 609 TCR B N   1 
HETATM 7284 C  CA  . TCR K 7 .   ? -35.772 -23.231 28.464  1.00 41.41  ? 609 TCR B CA  1 
HETATM 7285 C  CB  . TCR K 7 .   ? -35.638 -22.312 27.275  1.00 44.72  ? 609 TCR B CB  1 
HETATM 7286 C  CG  . TCR K 7 .   ? -35.927 -20.922 27.703  1.00 44.75  ? 609 TCR B CG  1 
HETATM 7287 C  CD2 . TCR K 7 .   ? -36.476 -19.810 26.966  1.00 47.53  ? 609 TCR B CD2 1 
HETATM 7288 C  CE2 . TCR K 7 .   ? -36.569 -18.696 27.926  1.00 46.96  ? 609 TCR B CE2 1 
HETATM 7289 C  CE3 . TCR K 7 .   ? -36.822 -19.689 25.637  1.00 57.95  ? 609 TCR B CE3 1 
HETATM 7290 C  CD1 . TCR K 7 .   ? -35.770 -20.423 29.057  1.00 49.41  ? 609 TCR B CD1 1 
HETATM 7291 N  NE1 . TCR K 7 .   ? -36.137 -19.117 29.119  1.00 48.49  ? 609 TCR B NE1 1 
HETATM 7292 C  CZ2 . TCR K 7 .   ? -37.041 -17.479 27.473  1.00 55.28  ? 609 TCR B CZ2 1 
HETATM 7293 C  CZ3 . TCR K 7 .   ? -37.294 -18.431 25.222  1.00 63.54  ? 609 TCR B CZ3 1 
HETATM 7294 C  CH2 . TCR K 7 .   ? -37.396 -17.348 26.120  1.00 58.60  ? 609 TCR B CH2 1 
HETATM 7295 C  C9  . TCR K 7 .   ? -35.293 -21.358 30.148  1.00 53.36  ? 609 TCR B C9  1 
HETATM 7296 C  C   . TCR K 7 .   ? -35.034 -24.452 28.068  1.00 40.19  ? 609 TCR B C   1 
HETATM 7297 O  OXT . TCR K 7 .   ? -34.110 -24.823 28.888  1.00 36.61  ? 609 TCR B OXT 1 
HETATM 7298 O  O1  . TCR K 7 .   ? -35.341 -24.959 26.940  1.00 31.90  ? 609 TCR B O1  1 
HETATM 7299 GD GD  . GD3 L 2 .   ? -53.196 -46.542 26.781  1.00 120.39 ? 601 GD3 A GD  1 
HETATM 7300 MG MG  . MG  M 3 .   ? -21.766 -60.370 -1.936  1.00 95.13  ? 602 MG  A MG  1 
HETATM 7301 C  C   . BCT N 4 .   ? -28.715 -61.730 22.886  1.00 67.29  ? 603 BCT A C   1 
HETATM 7302 O  O1  . BCT N 4 .   ? -29.256 -62.183 21.879  1.00 70.08  ? 603 BCT A O1  1 
HETATM 7303 O  O2  . BCT N 4 .   ? -29.318 -61.246 23.899  1.00 61.27  ? 603 BCT A O2  1 
HETATM 7304 O  O3  . BCT N 4 .   ? -27.414 -61.790 22.774  1.00 61.77  ? 603 BCT A O3  1 
HETATM 7305 CL CL  . CL  O 5 .   ? -23.126 -49.065 22.369  1.00 65.97  ? 604 CL  A CL  1 
HETATM 7306 C  C1  . NAG P 6 .   ? -36.709 -43.963 56.170  1.00 95.35  ? 605 NAG A C1  1 
HETATM 7307 C  C2  . NAG P 6 .   ? -36.438 -42.459 56.014  1.00 105.56 ? 605 NAG A C2  1 
HETATM 7308 C  C3  . NAG P 6 .   ? -35.539 -41.860 57.093  1.00 114.02 ? 605 NAG A C3  1 
HETATM 7309 C  C4  . NAG P 6 .   ? -36.014 -42.294 58.471  1.00 121.12 ? 605 NAG A C4  1 
HETATM 7310 C  C5  . NAG P 6 .   ? -36.011 -43.830 58.495  1.00 120.72 ? 605 NAG A C5  1 
HETATM 7311 C  C6  . NAG P 6 .   ? -36.365 -44.404 59.869  1.00 113.01 ? 605 NAG A C6  1 
HETATM 7312 C  C7  . NAG P 6 .   ? -36.570 -42.040 53.645  1.00 96.97  ? 605 NAG A C7  1 
HETATM 7313 C  C8  . NAG P 6 .   ? -35.866 -41.774 52.347  1.00 100.00 ? 605 NAG A C8  1 
HETATM 7314 N  N2  . NAG P 6 .   ? -35.833 -42.192 54.727  1.00 98.72  ? 605 NAG A N2  1 
HETATM 7315 O  O3  . NAG P 6 .   ? -35.534 -40.456 56.978  1.00 108.43 ? 605 NAG A O3  1 
HETATM 7316 O  O4  . NAG P 6 .   ? -35.142 -41.749 59.439  1.00 120.65 ? 605 NAG A O4  1 
HETATM 7317 O  O5  . NAG P 6 .   ? -36.904 -44.359 57.516  1.00 110.93 ? 605 NAG A O5  1 
HETATM 7318 O  O6  . NAG P 6 .   ? -37.765 -44.560 60.002  1.00 104.47 ? 605 NAG A O6  1 
HETATM 7319 O  O7  . NAG P 6 .   ? -37.789 -42.124 53.688  1.00 97.62  ? 605 NAG A O7  1 
HETATM 7320 C  C1  . NAG Q 6 .   ? -32.257 -61.990 56.009  1.00 119.09 ? 606 NAG A C1  1 
HETATM 7321 C  C2  . NAG Q 6 .   ? -31.392 -62.927 56.841  1.00 124.50 ? 606 NAG A C2  1 
HETATM 7322 C  C3  . NAG Q 6 .   ? -31.627 -64.309 56.268  1.00 127.84 ? 606 NAG A C3  1 
HETATM 7323 C  C4  . NAG Q 6 .   ? -33.131 -64.630 56.261  1.00 134.08 ? 606 NAG A C4  1 
HETATM 7324 C  C5  . NAG Q 6 .   ? -34.087 -63.433 56.059  1.00 137.23 ? 606 NAG A C5  1 
HETATM 7325 C  C6  . NAG Q 6 .   ? -35.426 -63.677 56.757  1.00 141.85 ? 606 NAG A C6  1 
HETATM 7326 C  C7  . NAG Q 6 .   ? -29.518 -61.580 57.641  1.00 109.28 ? 606 NAG A C7  1 
HETATM 7327 C  C8  . NAG Q 6 .   ? -28.042 -61.285 57.612  1.00 112.42 ? 606 NAG A C8  1 
HETATM 7328 N  N2  . NAG Q 6 .   ? -29.974 -62.574 56.873  1.00 114.16 ? 606 NAG A N2  1 
HETATM 7329 O  O3  . NAG Q 6 .   ? -30.907 -65.223 57.061  1.00 128.84 ? 606 NAG A O3  1 
HETATM 7330 O  O4  . NAG Q 6 .   ? -33.399 -65.545 55.220  1.00 132.11 ? 606 NAG A O4  1 
HETATM 7331 O  O5  . NAG Q 6 .   ? -33.574 -62.171 56.469  1.00 122.16 ? 606 NAG A O5  1 
HETATM 7332 O  O6  . NAG Q 6 .   ? -36.451 -63.034 56.025  1.00 144.44 ? 606 NAG A O6  1 
HETATM 7333 O  O7  . NAG Q 6 .   ? -30.256 -60.901 58.353  1.00 93.79  ? 606 NAG A O7  1 
HETATM 7334 C  C1  . NAG R 6 .   ? -44.204 -56.029 2.321   1.00 109.71 ? 607 NAG A C1  1 
HETATM 7335 C  C2  . NAG R 6 .   ? -45.392 -55.116 2.674   1.00 111.28 ? 607 NAG A C2  1 
HETATM 7336 C  C3  . NAG R 6 .   ? -46.674 -55.890 2.938   1.00 109.82 ? 607 NAG A C3  1 
HETATM 7337 C  C4  . NAG R 6 .   ? -46.928 -57.004 1.933   1.00 107.62 ? 607 NAG A C4  1 
HETATM 7338 C  C5  . NAG R 6 .   ? -45.673 -57.775 1.534   1.00 109.52 ? 607 NAG A C5  1 
HETATM 7339 C  C6  . NAG R 6 .   ? -46.016 -58.650 0.324   1.00 101.74 ? 607 NAG A C6  1 
HETATM 7340 C  C7  . NAG R 6 .   ? -45.147 -52.940 3.803   1.00 114.21 ? 607 NAG A C7  1 
HETATM 7341 C  C8  . NAG R 6 .   ? -44.913 -52.203 5.094   1.00 112.78 ? 607 NAG A C8  1 
HETATM 7342 N  N2  . NAG R 6 .   ? -45.169 -54.280 3.850   1.00 114.13 ? 607 NAG A N2  1 
HETATM 7343 O  O3  . NAG R 6 .   ? -47.742 -54.973 2.881   1.00 113.31 ? 607 NAG A O3  1 
HETATM 7344 O  O4  . NAG R 6 .   ? -47.807 -57.926 2.526   1.00 106.86 ? 607 NAG A O4  1 
HETATM 7345 O  O5  . NAG R 6 .   ? -44.583 -56.905 1.262   1.00 113.12 ? 607 NAG A O5  1 
HETATM 7346 O  O6  . NAG R 6 .   ? -44.873 -58.949 -0.436  1.00 89.47  ? 607 NAG A O6  1 
HETATM 7347 O  O7  . NAG R 6 .   ? -45.298 -52.296 2.763   1.00 104.20 ? 607 NAG A O7  1 
HETATM 7348 C  C1  . NAG S 6 .   ? -47.393 -62.218 17.784  1.00 96.66  ? 608 NAG A C1  1 
HETATM 7349 C  C2  . NAG S 6 .   ? -46.858 -62.673 16.423  1.00 105.17 ? 608 NAG A C2  1 
HETATM 7350 C  C3  . NAG S 6 .   ? -48.050 -63.057 15.571  1.00 114.06 ? 608 NAG A C3  1 
HETATM 7351 C  C4  . NAG S 6 .   ? -48.708 -64.251 16.251  1.00 117.44 ? 608 NAG A C4  1 
HETATM 7352 C  C5  . NAG S 6 .   ? -49.179 -63.878 17.651  1.00 108.00 ? 608 NAG A C5  1 
HETATM 7353 C  C6  . NAG S 6 .   ? -49.654 -65.116 18.418  1.00 104.16 ? 608 NAG A C6  1 
HETATM 7354 C  C7  . NAG S 6 .   ? -44.704 -61.543 15.821  1.00 116.32 ? 608 NAG A C7  1 
HETATM 7355 C  C8  . NAG S 6 .   ? -43.848 -62.421 16.705  1.00 121.14 ? 608 NAG A C8  1 
HETATM 7356 N  N2  . NAG S 6 .   ? -46.044 -61.685 15.728  1.00 106.41 ? 608 NAG A N2  1 
HETATM 7357 O  O3  . NAG S 6 .   ? -47.653 -63.347 14.247  1.00 106.56 ? 608 NAG A O3  1 
HETATM 7358 O  O4  . NAG S 6 .   ? -49.826 -64.640 15.501  1.00 134.89 ? 608 NAG A O4  1 
HETATM 7359 O  O5  . NAG S 6 .   ? -48.133 -63.268 18.382  1.00 110.97 ? 608 NAG A O5  1 
HETATM 7360 O  O6  . NAG S 6 .   ? -48.641 -65.628 19.264  1.00 98.37  ? 608 NAG A O6  1 
HETATM 7361 O  O7  . NAG S 6 .   ? -44.122 -60.667 15.182  1.00 106.41 ? 608 NAG A O7  1 
HETATM 7362 N  N   . TCR T 7 .   ? -33.314 -50.751 25.301  1.00 40.63  ? 609 TCR A N   1 
HETATM 7363 C  CA  . TCR T 7 .   ? -32.165 -50.188 25.979  1.00 36.89  ? 609 TCR A CA  1 
HETATM 7364 C  CB  . TCR T 7 .   ? -30.823 -50.855 26.268  1.00 39.03  ? 609 TCR A CB  1 
HETATM 7365 C  CG  . TCR T 7 .   ? -31.050 -52.282 26.073  1.00 40.82  ? 609 TCR A CG  1 
HETATM 7366 C  CD2 . TCR T 7 .   ? -30.218 -53.407 26.477  1.00 44.67  ? 609 TCR A CD2 1 
HETATM 7367 C  CE2 . TCR T 7 .   ? -30.973 -54.629 26.071  1.00 46.00  ? 609 TCR A CE2 1 
HETATM 7368 C  CE3 . TCR T 7 .   ? -28.997 -53.475 27.087  1.00 48.98  ? 609 TCR A CE3 1 
HETATM 7369 C  CD1 . TCR T 7 .   ? -32.293 -52.902 25.533  1.00 45.30  ? 609 TCR A CD1 1 
HETATM 7370 N  NE1 . TCR T 7 .   ? -32.163 -54.258 25.532  1.00 50.45  ? 609 TCR A NE1 1 
HETATM 7371 C  CZ2 . TCR T 7 .   ? -30.415 -55.855 26.292  1.00 45.14  ? 609 TCR A CZ2 1 
HETATM 7372 C  CZ3 . TCR T 7 .   ? -28.478 -54.763 27.294  1.00 55.14  ? 609 TCR A CZ3 1 
HETATM 7373 C  CH2 . TCR T 7 .   ? -29.170 -55.938 26.901  1.00 48.72  ? 609 TCR A CH2 1 
HETATM 7374 C  C9  . TCR T 7 .   ? -33.484 -52.152 25.032  1.00 42.45  ? 609 TCR A C9  1 
HETATM 7375 C  C   . TCR T 7 .   ? -31.997 -48.746 25.669  1.00 37.78  ? 609 TCR A C   1 
HETATM 7376 O  OXT . TCR T 7 .   ? -31.149 -48.143 26.358  1.00 32.81  ? 609 TCR A OXT 1 
HETATM 7377 O  O1  . TCR T 7 .   ? -32.637 -48.251 24.673  1.00 34.40  ? 609 TCR A O1  1 
HETATM 7378 O  O   . HOH U 8 .   ? -20.148 -4.666  13.246  1.00 61.96  ? 701 HOH B O   1 
HETATM 7379 O  O   . HOH U 8 .   ? -39.016 -24.106 21.555  1.00 61.41  ? 702 HOH B O   1 
HETATM 7380 O  O   . HOH U 8 .   ? -60.167 -16.022 30.272  1.00 48.86  ? 703 HOH B O   1 
HETATM 7381 O  O   . HOH U 8 .   ? -40.121 -26.163 25.249  1.00 41.69  ? 704 HOH B O   1 
HETATM 7382 O  O   . HOH U 8 .   ? -35.595 -29.809 34.752  1.00 42.87  ? 705 HOH B O   1 
HETATM 7383 O  O   . HOH U 8 .   ? -52.404 -38.317 31.255  1.00 48.17  ? 706 HOH B O   1 
HETATM 7384 O  O   . HOH U 8 .   ? -40.020 -11.879 16.978  1.00 49.78  ? 707 HOH B O   1 
HETATM 7385 O  O   . HOH U 8 .   ? -36.795 -36.018 29.382  1.00 48.09  ? 708 HOH B O   1 
HETATM 7386 O  O   . HOH U 8 .   ? -63.464 -22.436 33.407  1.00 60.95  ? 709 HOH B O   1 
HETATM 7387 O  O   . HOH U 8 .   ? -25.257 -2.006  17.436  1.00 51.67  ? 710 HOH B O   1 
HETATM 7388 O  O   . HOH U 8 .   ? -18.021 -27.974 34.614  1.00 71.51  ? 711 HOH B O   1 
HETATM 7389 O  O   . HOH V 8 .   ? -41.712 -39.918 20.423  1.00 47.40  ? 701 HOH A O   1 
HETATM 7390 O  O   . HOH V 8 .   ? -26.249 -56.428 31.480  1.00 43.77  ? 702 HOH A O   1 
HETATM 7391 O  O   . HOH V 8 .   ? -29.421 -33.113 13.806  1.00 37.54  ? 703 HOH A O   1 
HETATM 7392 O  O   . HOH V 8 .   ? -37.921 -53.603 -0.575  1.00 55.45  ? 704 HOH A O   1 
HETATM 7393 O  O   . HOH V 8 .   ? -25.447 -52.954 28.191  1.00 57.57  ? 705 HOH A O   1 
HETATM 7394 O  O   . HOH V 8 .   ? -40.524 -38.040 32.021  1.00 38.90  ? 706 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   MET 1   -26 ?   ?   ?   B . n 
A 1 2   ARG 2   -25 ?   ?   ?   B . n 
A 1 3   LEU 3   -24 ?   ?   ?   B . n 
A 1 4   LEU 4   -23 ?   ?   ?   B . n 
A 1 5   THR 5   -22 ?   ?   ?   B . n 
A 1 6   ALA 6   -21 ?   ?   ?   B . n 
A 1 7   LEU 7   -20 ?   ?   ?   B . n 
A 1 8   PHE 8   -19 ?   ?   ?   B . n 
A 1 9   ALA 9   -18 ?   ?   ?   B . n 
A 1 10  TYR 10  -17 ?   ?   ?   B . n 
A 1 11  PHE 11  -16 ?   ?   ?   B . n 
A 1 12  ILE 12  -15 ?   ?   ?   B . n 
A 1 13  VAL 13  -14 ?   ?   ?   B . n 
A 1 14  ALA 14  -13 ?   ?   ?   B . n 
A 1 15  LEU 15  -12 ?   ?   ?   B . n 
A 1 16  ILE 16  -11 ?   ?   ?   B . n 
A 1 17  LEU 17  -10 ?   ?   ?   B . n 
A 1 18  ALA 18  -9  ?   ?   ?   B . n 
A 1 19  PHE 19  -8  ?   ?   ?   B . n 
A 1 20  SER 20  -7  ?   ?   ?   B . n 
A 1 21  VAL 21  -6  ?   ?   ?   B . n 
A 1 22  SER 22  -5  ?   ?   ?   B . n 
A 1 23  ALA 23  -4  ?   ?   ?   B . n 
A 1 24  LYS 24  -3  ?   ?   ?   B . n 
A 1 25  SER 25  -2  ?   ?   ?   B . n 
A 1 26  MET 26  -1  ?   ?   ?   B . n 
A 1 27  HIS 27  0   ?   ?   ?   B . n 
A 1 28  HIS 28  1   ?   ?   ?   B . n 
A 1 29  HIS 29  2   ?   ?   ?   B . n 
A 1 30  HIS 30  3   ?   ?   ?   B . n 
A 1 31  HIS 31  4   ?   ?   ?   B . n 
A 1 32  HIS 32  5   ?   ?   ?   B . n 
A 1 33  HIS 33  6   ?   ?   ?   B . n 
A 1 34  HIS 34  7   ?   ?   ?   B . n 
A 1 35  SER 35  8   ?   ?   ?   B . n 
A 1 36  ALA 36  9   ?   ?   ?   B . n 
A 1 37  TRP 37  10  ?   ?   ?   B . n 
A 1 38  SER 38  11  ?   ?   ?   B . n 
A 1 39  HIS 39  12  ?   ?   ?   B . n 
A 1 40  PRO 40  13  ?   ?   ?   B . n 
A 1 41  GLN 41  14  ?   ?   ?   B . n 
A 1 42  PHE 42  15  ?   ?   ?   B . n 
A 1 43  GLU 43  16  ?   ?   ?   B . n 
A 1 44  LYS 44  17  ?   ?   ?   B . n 
A 1 45  GLU 45  18  ?   ?   ?   B . n 
A 1 46  PHE 46  19  ?   ?   ?   B . n 
A 1 47  TYR 47  20  ?   ?   ?   B . n 
A 1 48  GLY 48  21  21  GLY GLY B . n 
A 1 49  PRO 49  22  22  PRO PRO B . n 
A 1 50  ASP 50  23  23  ASP ASP B . n 
A 1 51  GLN 51  24  24  GLN GLN B . n 
A 1 52  ARG 52  25  25  ARG ARG B . n 
A 1 53  ALA 53  26  26  ALA ALA B . n 
A 1 54  GLN 54  27  27  GLN GLN B . n 
A 1 55  LYS 55  28  28  LYS LYS B . n 
A 1 56  LYS 56  29  29  LYS LYS B . n 
A 1 57  GLY 57  30  30  GLY GLY B . n 
A 1 58  ASP 58  31  31  ASP ASP B . n 
A 1 59  ILE 59  32  32  ILE ILE B . n 
A 1 60  ILE 60  33  33  ILE ILE B . n 
A 1 61  LEU 61  34  34  LEU LEU B . n 
A 1 62  GLY 62  35  35  GLY GLY B . n 
A 1 63  GLY 63  36  36  GLY GLY B . n 
A 1 64  LEU 64  37  37  LEU LEU B . n 
A 1 65  PHE 65  38  38  PHE PHE B . n 
A 1 66  PRO 66  39  39  PRO PRO B . n 
A 1 67  ILE 67  40  40  ILE ILE B . n 
A 1 68  HIS 68  41  41  HIS HIS B . n 
A 1 69  PHE 69  42  42  PHE PHE B . n 
A 1 70  GLY 70  43  43  GLY GLY B . n 
A 1 71  VAL 71  44  44  VAL VAL B . n 
A 1 72  ALA 72  45  45  ALA ALA B . n 
A 1 73  ALA 73  46  46  ALA ALA B . n 
A 1 74  LYS 74  47  47  LYS LYS B . n 
A 1 75  ASP 75  48  48  ASP ASP B . n 
A 1 76  GLN 76  49  49  GLN GLN B . n 
A 1 77  ASP 77  50  50  ASP ASP B . n 
A 1 78  LEU 78  51  51  LEU LEU B . n 
A 1 79  LYS 79  52  52  LYS LYS B . n 
A 1 80  SER 80  53  53  SER SER B . n 
A 1 81  ARG 81  54  54  ARG ARG B . n 
A 1 82  PRO 82  55  55  PRO PRO B . n 
A 1 83  GLU 83  56  56  GLU GLU B . n 
A 1 84  SER 84  57  57  SER SER B . n 
A 1 85  VAL 85  58  58  VAL VAL B . n 
A 1 86  GLU 86  59  59  GLU GLU B . n 
A 1 87  CYS 87  60  60  CYS CYS B . n 
A 1 88  ILE 88  61  61  ILE ILE B . n 
A 1 89  ARG 89  62  62  ARG ARG B . n 
A 1 90  TYR 90  63  63  TYR TYR B . n 
A 1 91  ASN 91  64  64  ASN ASN B . n 
A 1 92  PHE 92  65  65  PHE PHE B . n 
A 1 93  ARG 93  66  66  ARG ARG B . n 
A 1 94  GLY 94  67  67  GLY GLY B . n 
A 1 95  PHE 95  68  68  PHE PHE B . n 
A 1 96  ARG 96  69  69  ARG ARG B . n 
A 1 97  TRP 97  70  70  TRP TRP B . n 
A 1 98  LEU 98  71  71  LEU LEU B . n 
A 1 99  GLN 99  72  72  GLN GLN B . n 
A 1 100 ALA 100 73  73  ALA ALA B . n 
A 1 101 MET 101 74  74  MET MET B . n 
A 1 102 ILE 102 75  75  ILE ILE B . n 
A 1 103 PHE 103 76  76  PHE PHE B . n 
A 1 104 ALA 104 77  77  ALA ALA B . n 
A 1 105 ILE 105 78  78  ILE ILE B . n 
A 1 106 GLU 106 79  79  GLU GLU B . n 
A 1 107 GLU 107 80  80  GLU GLU B . n 
A 1 108 ILE 108 81  81  ILE ILE B . n 
A 1 109 ASN 109 82  82  ASN ASN B . n 
A 1 110 SER 110 83  83  SER SER B . n 
A 1 111 SER 111 84  84  SER SER B . n 
A 1 112 PRO 112 85  85  PRO PRO B . n 
A 1 113 ALA 113 86  86  ALA ALA B . n 
A 1 114 LEU 114 87  87  LEU LEU B . n 
A 1 115 LEU 115 88  88  LEU LEU B . n 
A 1 116 PRO 116 89  89  PRO PRO B . n 
A 1 117 ASN 117 90  90  ASN ASN B . n 
A 1 118 LEU 118 91  91  LEU LEU B . n 
A 1 119 THR 119 92  92  THR THR B . n 
A 1 120 LEU 120 93  93  LEU LEU B . n 
A 1 121 GLY 121 94  94  GLY GLY B . n 
A 1 122 TYR 122 95  95  TYR TYR B . n 
A 1 123 ARG 123 96  96  ARG ARG B . n 
A 1 124 ILE 124 97  97  ILE ILE B . n 
A 1 125 PHE 125 98  98  PHE PHE B . n 
A 1 126 ASP 126 99  99  ASP ASP B . n 
A 1 127 THR 127 100 100 THR THR B . n 
A 1 128 CYS 128 101 101 CYS CYS B . n 
A 1 129 ASN 129 102 102 ASN ASN B . n 
A 1 130 THR 130 103 103 THR THR B . n 
A 1 131 VAL 131 104 104 VAL VAL B . n 
A 1 132 SER 132 105 105 SER SER B . n 
A 1 133 LYS 133 106 106 LYS LYS B . n 
A 1 134 ALA 134 107 107 ALA ALA B . n 
A 1 135 LEU 135 108 108 LEU LEU B . n 
A 1 136 GLU 136 109 109 GLU GLU B . n 
A 1 137 ALA 137 110 110 ALA ALA B . n 
A 1 138 THR 138 111 111 THR THR B . n 
A 1 139 LEU 139 112 112 LEU LEU B . n 
A 1 140 SER 140 113 113 SER SER B . n 
A 1 141 PHE 141 114 114 PHE PHE B . n 
A 1 142 VAL 142 115 115 VAL VAL B . n 
A 1 143 ALA 143 116 116 ALA ALA B . n 
A 1 144 GLN 144 117 117 GLN GLN B . n 
A 1 145 ASN 145 118 118 ASN ASN B . n 
A 1 146 LYS 146 119 119 LYS LYS B . n 
A 1 147 ILE 147 120 120 ILE ILE B . n 
A 1 148 ASP 148 121 121 ASP ASP B . n 
A 1 149 SER 149 122 ?   ?   ?   B . n 
A 1 150 LEU 150 123 ?   ?   ?   B . n 
A 1 151 ASN 151 124 ?   ?   ?   B . n 
A 1 152 LEU 152 125 ?   ?   ?   B . n 
A 1 153 ASP 153 126 ?   ?   ?   B . n 
A 1 154 GLU 154 127 ?   ?   ?   B . n 
A 1 155 PHE 155 128 ?   ?   ?   B . n 
A 1 156 CYS 156 129 ?   ?   ?   B . n 
A 1 157 ASN 157 130 ?   ?   ?   B . n 
A 1 158 CYS 158 131 ?   ?   ?   B . n 
A 1 159 SER 159 132 ?   ?   ?   B . n 
A 1 160 GLU 160 133 ?   ?   ?   B . n 
A 1 161 HIS 161 134 ?   ?   ?   B . n 
A 1 162 ILE 162 135 ?   ?   ?   B . n 
A 1 163 PRO 163 136 ?   ?   ?   B . n 
A 1 164 SER 164 137 137 SER SER B . n 
A 1 165 THR 165 138 138 THR THR B . n 
A 1 166 ILE 166 139 139 ILE ILE B . n 
A 1 167 ALA 167 140 140 ALA ALA B . n 
A 1 168 VAL 168 141 141 VAL VAL B . n 
A 1 169 VAL 169 142 142 VAL VAL B . n 
A 1 170 GLY 170 143 143 GLY GLY B . n 
A 1 171 ALA 171 144 144 ALA ALA B . n 
A 1 172 THR 172 145 145 THR THR B . n 
A 1 173 GLY 173 146 146 GLY GLY B . n 
A 1 174 SER 174 147 147 SER SER B . n 
A 1 175 GLY 175 148 148 GLY GLY B . n 
A 1 176 VAL 176 149 149 VAL VAL B . n 
A 1 177 SER 177 150 150 SER SER B . n 
A 1 178 THR 178 151 151 THR THR B . n 
A 1 179 ALA 179 152 152 ALA ALA B . n 
A 1 180 VAL 180 153 153 VAL VAL B . n 
A 1 181 ALA 181 154 154 ALA ALA B . n 
A 1 182 ASN 182 155 155 ASN ASN B . n 
A 1 183 LEU 183 156 156 LEU LEU B . n 
A 1 184 LEU 184 157 157 LEU LEU B . n 
A 1 185 GLY 185 158 158 GLY GLY B . n 
A 1 186 LEU 186 159 159 LEU LEU B . n 
A 1 187 PHE 187 160 160 PHE PHE B . n 
A 1 188 TYR 188 161 161 TYR TYR B . n 
A 1 189 ILE 189 162 162 ILE ILE B . n 
A 1 190 PRO 190 163 163 PRO PRO B . n 
A 1 191 GLN 191 164 164 GLN GLN B . n 
A 1 192 VAL 192 165 165 VAL VAL B . n 
A 1 193 SER 193 166 166 SER SER B . n 
A 1 194 TYR 194 167 167 TYR TYR B . n 
A 1 195 ALA 195 168 168 ALA ALA B . n 
A 1 196 SER 196 169 169 SER SER B . n 
A 1 197 SER 197 170 170 SER SER B . n 
A 1 198 SER 198 171 171 SER SER B . n 
A 1 199 ARG 199 172 172 ARG ARG B . n 
A 1 200 LEU 200 173 173 LEU LEU B . n 
A 1 201 LEU 201 174 174 LEU LEU B . n 
A 1 202 SER 202 175 175 SER SER B . n 
A 1 203 ASN 203 176 176 ASN ASN B . n 
A 1 204 LYS 204 177 177 LYS LYS B . n 
A 1 205 ASN 205 178 178 ASN ASN B . n 
A 1 206 GLN 206 179 179 GLN GLN B . n 
A 1 207 PHE 207 180 180 PHE PHE B . n 
A 1 208 LYS 208 181 181 LYS LYS B . n 
A 1 209 SER 209 182 182 SER SER B . n 
A 1 210 PHE 210 183 183 PHE PHE B . n 
A 1 211 LEU 211 184 184 LEU LEU B . n 
A 1 212 ARG 212 185 185 ARG ARG B . n 
A 1 213 THR 213 186 186 THR THR B . n 
A 1 214 ILE 214 187 187 ILE ILE B . n 
A 1 215 PRO 215 188 188 PRO PRO B . n 
A 1 216 ASN 216 189 189 ASN ASN B . n 
A 1 217 ASP 217 190 190 ASP ASP B . n 
A 1 218 GLU 218 191 191 GLU GLU B . n 
A 1 219 HIS 219 192 192 HIS HIS B . n 
A 1 220 GLN 220 193 193 GLN GLN B . n 
A 1 221 ALA 221 194 194 ALA ALA B . n 
A 1 222 THR 222 195 195 THR THR B . n 
A 1 223 ALA 223 196 196 ALA ALA B . n 
A 1 224 MET 224 197 197 MET MET B . n 
A 1 225 ALA 225 198 198 ALA ALA B . n 
A 1 226 ASP 226 199 199 ASP ASP B . n 
A 1 227 ILE 227 200 200 ILE ILE B . n 
A 1 228 ILE 228 201 201 ILE ILE B . n 
A 1 229 GLU 229 202 202 GLU GLU B . n 
A 1 230 TYR 230 203 203 TYR TYR B . n 
A 1 231 PHE 231 204 204 PHE PHE B . n 
A 1 232 ARG 232 205 205 ARG ARG B . n 
A 1 233 TRP 233 206 206 TRP TRP B . n 
A 1 234 ASN 234 207 207 ASN ASN B . n 
A 1 235 TRP 235 208 208 TRP TRP B . n 
A 1 236 VAL 236 209 209 VAL VAL B . n 
A 1 237 GLY 237 210 210 GLY GLY B . n 
A 1 238 THR 238 211 211 THR THR B . n 
A 1 239 ILE 239 212 212 ILE ILE B . n 
A 1 240 ALA 240 213 213 ALA ALA B . n 
A 1 241 ALA 241 214 214 ALA ALA B . n 
A 1 242 ASP 242 215 215 ASP ASP B . n 
A 1 243 ASP 243 216 216 ASP ASP B . n 
A 1 244 ASP 244 217 217 ASP ASP B . n 
A 1 245 TYR 245 218 218 TYR TYR B . n 
A 1 246 GLY 246 219 219 GLY GLY B . n 
A 1 247 ARG 247 220 220 ARG ARG B . n 
A 1 248 PRO 248 221 221 PRO PRO B . n 
A 1 249 GLY 249 222 222 GLY GLY B . n 
A 1 250 ILE 250 223 223 ILE ILE B . n 
A 1 251 GLU 251 224 224 GLU GLU B . n 
A 1 252 LYS 252 225 225 LYS LYS B . n 
A 1 253 PHE 253 226 226 PHE PHE B . n 
A 1 254 ARG 254 227 227 ARG ARG B . n 
A 1 255 GLU 255 228 228 GLU GLU B . n 
A 1 256 GLU 256 229 229 GLU GLU B . n 
A 1 257 ALA 257 230 230 ALA ALA B . n 
A 1 258 GLU 258 231 231 GLU GLU B . n 
A 1 259 GLU 259 232 232 GLU GLU B . n 
A 1 260 ARG 260 233 233 ARG ARG B . n 
A 1 261 ASP 261 234 234 ASP ASP B . n 
A 1 262 ILE 262 235 235 ILE ILE B . n 
A 1 263 CSO 263 236 236 CSO CSO B . n 
A 1 264 ILE 264 237 237 ILE ILE B . n 
A 1 265 ASP 265 238 238 ASP ASP B . n 
A 1 266 PHE 266 239 239 PHE PHE B . n 
A 1 267 SER 267 240 240 SER SER B . n 
A 1 268 GLU 268 241 241 GLU GLU B . n 
A 1 269 LEU 269 242 242 LEU LEU B . n 
A 1 270 ILE 270 243 243 ILE ILE B . n 
A 1 271 SER 271 244 244 SER SER B . n 
A 1 272 GLN 272 245 245 GLN GLN B . n 
A 1 273 TYR 273 246 246 TYR TYR B . n 
A 1 274 SER 274 247 247 SER SER B . n 
A 1 275 ASP 275 248 248 ASP ASP B . n 
A 1 276 GLU 276 249 249 GLU GLU B . n 
A 1 277 GLU 277 250 250 GLU GLU B . n 
A 1 278 GLU 278 251 251 GLU GLU B . n 
A 1 279 ILE 279 252 252 ILE ILE B . n 
A 1 280 GLN 280 253 253 GLN GLN B . n 
A 1 281 HIS 281 254 254 HIS HIS B . n 
A 1 282 VAL 282 255 255 VAL VAL B . n 
A 1 283 VAL 283 256 256 VAL VAL B . n 
A 1 284 GLU 284 257 257 GLU GLU B . n 
A 1 285 VAL 285 258 258 VAL VAL B . n 
A 1 286 ILE 286 259 259 ILE ILE B . n 
A 1 287 GLN 287 260 260 GLN GLN B . n 
A 1 288 ASN 288 261 261 ASN ASN B . n 
A 1 289 SER 289 262 262 SER SER B . n 
A 1 290 THR 290 263 263 THR THR B . n 
A 1 291 ALA 291 264 264 ALA ALA B . n 
A 1 292 LYS 292 265 265 LYS LYS B . n 
A 1 293 VAL 293 266 266 VAL VAL B . n 
A 1 294 ILE 294 267 267 ILE ILE B . n 
A 1 295 VAL 295 268 268 VAL VAL B . n 
A 1 296 VAL 296 269 269 VAL VAL B . n 
A 1 297 PHE 297 270 270 PHE PHE B . n 
A 1 298 SER 298 271 271 SER SER B . n 
A 1 299 SER 299 272 272 SER SER B . n 
A 1 300 GLY 300 273 273 GLY GLY B . n 
A 1 301 PRO 301 274 274 PRO PRO B . n 
A 1 302 ASP 302 275 275 ASP ASP B . n 
A 1 303 LEU 303 276 276 LEU LEU B . n 
A 1 304 GLU 304 277 277 GLU GLU B . n 
A 1 305 PRO 305 278 278 PRO PRO B . n 
A 1 306 LEU 306 279 279 LEU LEU B . n 
A 1 307 ILE 307 280 280 ILE ILE B . n 
A 1 308 LYS 308 281 281 LYS LYS B . n 
A 1 309 GLU 309 282 282 GLU GLU B . n 
A 1 310 ILE 310 283 283 ILE ILE B . n 
A 1 311 VAL 311 284 284 VAL VAL B . n 
A 1 312 ARG 312 285 285 ARG ARG B . n 
A 1 313 ARG 313 286 286 ARG ARG B . n 
A 1 314 ASN 314 287 287 ASN ASN B . n 
A 1 315 ILE 315 288 288 ILE ILE B . n 
A 1 316 THR 316 289 289 THR THR B . n 
A 1 317 GLY 317 290 290 GLY GLY B . n 
A 1 318 LYS 318 291 291 LYS LYS B . n 
A 1 319 ILE 319 292 292 ILE ILE B . n 
A 1 320 TRP 320 293 293 TRP TRP B . n 
A 1 321 LEU 321 294 294 LEU LEU B . n 
A 1 322 ALA 322 295 295 ALA ALA B . n 
A 1 323 SER 323 296 296 SER SER B . n 
A 1 324 GLU 324 297 297 GLU GLU B . n 
A 1 325 ALA 325 298 298 ALA ALA B . n 
A 1 326 TRP 326 299 299 TRP TRP B . n 
A 1 327 ALA 327 300 300 ALA ALA B . n 
A 1 328 SER 328 301 301 SER SER B . n 
A 1 329 SER 329 302 302 SER SER B . n 
A 1 330 SER 330 303 303 SER SER B . n 
A 1 331 LEU 331 304 304 LEU LEU B . n 
A 1 332 ILE 332 305 305 ILE ILE B . n 
A 1 333 ALA 333 306 306 ALA ALA B . n 
A 1 334 MET 334 307 307 MET MET B . n 
A 1 335 PRO 335 308 308 PRO PRO B . n 
A 1 336 GLN 336 309 309 GLN GLN B . n 
A 1 337 TYR 337 310 310 TYR TYR B . n 
A 1 338 PHE 338 311 311 PHE PHE B . n 
A 1 339 HIS 339 312 312 HIS HIS B . n 
A 1 340 VAL 340 313 313 VAL VAL B . n 
A 1 341 VAL 341 314 314 VAL VAL B . n 
A 1 342 GLY 342 315 315 GLY GLY B . n 
A 1 343 GLY 343 316 316 GLY GLY B . n 
A 1 344 THR 344 317 317 THR THR B . n 
A 1 345 ILE 345 318 318 ILE ILE B . n 
A 1 346 GLY 346 319 319 GLY GLY B . n 
A 1 347 PHE 347 320 320 PHE PHE B . n 
A 1 348 ALA 348 321 321 ALA ALA B . n 
A 1 349 LEU 349 322 322 LEU LEU B . n 
A 1 350 LYS 350 323 323 LYS LYS B . n 
A 1 351 ALA 351 324 324 ALA ALA B . n 
A 1 352 GLY 352 325 325 GLY GLY B . n 
A 1 353 GLN 353 326 326 GLN GLN B . n 
A 1 354 ILE 354 327 327 ILE ILE B . n 
A 1 355 PRO 355 328 328 PRO PRO B . n 
A 1 356 GLY 356 329 329 GLY GLY B . n 
A 1 357 PHE 357 330 330 PHE PHE B . n 
A 1 358 ARG 358 331 331 ARG ARG B . n 
A 1 359 GLU 359 332 332 GLU GLU B . n 
A 1 360 PHE 360 333 333 PHE PHE B . n 
A 1 361 LEU 361 334 334 LEU LEU B . n 
A 1 362 LYS 362 335 335 LYS LYS B . n 
A 1 363 LYS 363 336 336 LYS LYS B . n 
A 1 364 VAL 364 337 337 VAL VAL B . n 
A 1 365 HIS 365 338 338 HIS HIS B . n 
A 1 366 PRO 366 339 339 PRO PRO B . n 
A 1 367 ARG 367 340 340 ARG ARG B . n 
A 1 368 LYS 368 341 341 LYS LYS B . n 
A 1 369 SER 369 342 342 SER SER B . n 
A 1 370 VAL 370 343 343 VAL VAL B . n 
A 1 371 HIS 371 344 344 HIS HIS B . n 
A 1 372 ASN 372 345 345 ASN ASN B . n 
A 1 373 GLY 373 346 346 GLY GLY B . n 
A 1 374 PHE 374 347 347 PHE PHE B . n 
A 1 375 ALA 375 348 348 ALA ALA B . n 
A 1 376 LYS 376 349 349 LYS LYS B . n 
A 1 377 GLU 377 350 350 GLU GLU B . n 
A 1 378 PHE 378 351 351 PHE PHE B . n 
A 1 379 TRP 379 352 352 TRP TRP B . n 
A 1 380 GLU 380 353 353 GLU GLU B . n 
A 1 381 GLU 381 354 354 GLU GLU B . n 
A 1 382 THR 382 355 355 THR THR B . n 
A 1 383 PHE 383 356 356 PHE PHE B . n 
A 1 384 ASN 384 357 357 ASN ASN B . n 
A 1 385 CYS 385 358 358 CYS CYS B . n 
A 1 386 HIS 386 359 359 HIS HIS B . n 
A 1 387 LEU 387 360 360 LEU LEU B . n 
A 1 388 GLN 388 361 361 GLN GLN B . n 
A 1 389 GLU 389 362 ?   ?   ?   B . n 
A 1 390 GLY 390 363 ?   ?   ?   B . n 
A 1 391 ALA 391 364 ?   ?   ?   B . n 
A 1 392 LYS 392 365 ?   ?   ?   B . n 
A 1 393 GLY 393 366 ?   ?   ?   B . n 
A 1 394 PRO 394 367 ?   ?   ?   B . n 
A 1 395 LEU 395 368 ?   ?   ?   B . n 
A 1 396 PRO 396 369 ?   ?   ?   B . n 
A 1 397 VAL 397 370 ?   ?   ?   B . n 
A 1 398 ASP 398 371 ?   ?   ?   B . n 
A 1 399 THR 399 372 ?   ?   ?   B . n 
A 1 400 PHE 400 373 ?   ?   ?   B . n 
A 1 401 LEU 401 374 ?   ?   ?   B . n 
A 1 402 ARG 402 375 ?   ?   ?   B . n 
A 1 403 GLY 403 376 ?   ?   ?   B . n 
A 1 404 HIS 404 377 ?   ?   ?   B . n 
A 1 405 GLU 405 378 ?   ?   ?   B . n 
A 1 406 GLU 406 379 ?   ?   ?   B . n 
A 1 407 SER 407 380 ?   ?   ?   B . n 
A 1 408 GLY 408 381 ?   ?   ?   B . n 
A 1 409 ASP 409 382 ?   ?   ?   B . n 
A 1 410 ARG 410 383 ?   ?   ?   B . n 
A 1 411 PHE 411 384 ?   ?   ?   B . n 
A 1 412 SER 412 385 ?   ?   ?   B . n 
A 1 413 ASN 413 386 ?   ?   ?   B . n 
A 1 414 SER 414 387 ?   ?   ?   B . n 
A 1 415 SER 415 388 ?   ?   ?   B . n 
A 1 416 THR 416 389 ?   ?   ?   B . n 
A 1 417 ALA 417 390 ?   ?   ?   B . n 
A 1 418 PHE 418 391 391 PHE PHE B . n 
A 1 419 ARG 419 392 392 ARG ARG B . n 
A 1 420 PRO 420 393 393 PRO PRO B . n 
A 1 421 LEU 421 394 394 LEU LEU B . n 
A 1 422 CYS 422 395 395 CYS CYS B . n 
A 1 423 THR 423 396 396 THR THR B . n 
A 1 424 GLY 424 397 397 GLY GLY B . n 
A 1 425 ASP 425 398 398 ASP ASP B . n 
A 1 426 GLU 426 399 399 GLU GLU B . n 
A 1 427 ASN 427 400 400 ASN ASN B . n 
A 1 428 ILE 428 401 401 ILE ILE B . n 
A 1 429 SER 429 402 402 SER SER B . n 
A 1 430 SER 430 403 403 SER SER B . n 
A 1 431 VAL 431 404 404 VAL VAL B . n 
A 1 432 GLU 432 405 405 GLU GLU B . n 
A 1 433 THR 433 406 406 THR THR B . n 
A 1 434 PRO 434 407 407 PRO PRO B . n 
A 1 435 TYR 435 408 408 TYR TYR B . n 
A 1 436 ILE 436 409 409 ILE ILE B . n 
A 1 437 ASP 437 410 410 ASP ASP B . n 
A 1 438 TYR 438 411 411 TYR TYR B . n 
A 1 439 THR 439 412 412 THR THR B . n 
A 1 440 HIS 440 413 413 HIS HIS B . n 
A 1 441 LEU 441 414 414 LEU LEU B . n 
A 1 442 ARG 442 415 415 ARG ARG B . n 
A 1 443 ILE 443 416 416 ILE ILE B . n 
A 1 444 SER 444 417 417 SER SER B . n 
A 1 445 TYR 445 418 418 TYR TYR B . n 
A 1 446 ASN 446 419 419 ASN ASN B . n 
A 1 447 VAL 447 420 420 VAL VAL B . n 
A 1 448 TYR 448 421 421 TYR TYR B . n 
A 1 449 LEU 449 422 422 LEU LEU B . n 
A 1 450 ALA 450 423 423 ALA ALA B . n 
A 1 451 VAL 451 424 424 VAL VAL B . n 
A 1 452 TYR 452 425 425 TYR TYR B . n 
A 1 453 SER 453 426 426 SER SER B . n 
A 1 454 ILE 454 427 427 ILE ILE B . n 
A 1 455 ALA 455 428 428 ALA ALA B . n 
A 1 456 HIS 456 429 429 HIS HIS B . n 
A 1 457 ALA 457 430 430 ALA ALA B . n 
A 1 458 LEU 458 431 431 LEU LEU B . n 
A 1 459 GLN 459 432 432 GLN GLN B . n 
A 1 460 ASP 460 433 433 ASP ASP B . n 
A 1 461 ILE 461 434 434 ILE ILE B . n 
A 1 462 TYR 462 435 435 TYR TYR B . n 
A 1 463 THR 463 436 436 THR THR B . n 
A 1 464 CYS 464 437 437 CYS CYS B . n 
A 1 465 LEU 465 438 438 LEU LEU B . n 
A 1 466 PRO 466 439 439 PRO PRO B . n 
A 1 467 GLY 467 440 440 GLY GLY B . n 
A 1 468 ARG 468 441 441 ARG ARG B . n 
A 1 469 GLY 469 442 442 GLY GLY B . n 
A 1 470 LEU 470 443 443 LEU LEU B . n 
A 1 471 PHE 471 444 444 PHE PHE B . n 
A 1 472 THR 472 445 445 THR THR B . n 
A 1 473 ASN 473 446 446 ASN ASN B . n 
A 1 474 GLY 474 447 447 GLY GLY B . n 
A 1 475 SER 475 448 448 SER SER B . n 
A 1 476 CYS 476 449 449 CYS CYS B . n 
A 1 477 ALA 477 450 450 ALA ALA B . n 
A 1 478 ASP 478 451 451 ASP ASP B . n 
A 1 479 ILE 479 452 452 ILE ILE B . n 
A 1 480 LYS 480 453 453 LYS LYS B . n 
A 1 481 LYS 481 454 454 LYS LYS B . n 
A 1 482 VAL 482 455 455 VAL VAL B . n 
A 1 483 GLU 483 456 456 GLU GLU B . n 
A 1 484 ALA 484 457 457 ALA ALA B . n 
A 1 485 TRP 485 458 458 TRP TRP B . n 
A 1 486 GLN 486 459 459 GLN GLN B . n 
A 1 487 VAL 487 460 460 VAL VAL B . n 
A 1 488 LEU 488 461 461 LEU LEU B . n 
A 1 489 LYS 489 462 462 LYS LYS B . n 
A 1 490 HIS 490 463 463 HIS HIS B . n 
A 1 491 LEU 491 464 464 LEU LEU B . n 
A 1 492 ARG 492 465 465 ARG ARG B . n 
A 1 493 HIS 493 466 466 HIS HIS B . n 
A 1 494 LEU 494 467 467 LEU LEU B . n 
A 1 495 ASN 495 468 468 ASN ASN B . n 
A 1 496 PHE 496 469 469 PHE PHE B . n 
A 1 497 THR 497 470 470 THR THR B . n 
A 1 498 ASN 498 471 471 ASN ASN B . n 
A 1 499 ASN 499 472 472 ASN ASN B . n 
A 1 500 MET 500 473 473 MET MET B . n 
A 1 501 GLY 501 474 474 GLY GLY B . n 
A 1 502 GLU 502 475 475 GLU GLU B . n 
A 1 503 GLN 503 476 476 GLN GLN B . n 
A 1 504 VAL 504 477 477 VAL VAL B . n 
A 1 505 THR 505 478 478 THR THR B . n 
A 1 506 PHE 506 479 479 PHE PHE B . n 
A 1 507 ASP 507 480 480 ASP ASP B . n 
A 1 508 GLU 508 481 481 GLU GLU B . n 
A 1 509 CSO 509 482 482 CSO CSO B . n 
A 1 510 GLY 510 483 483 GLY GLY B . n 
A 1 511 ASP 511 484 484 ASP ASP B . n 
A 1 512 LEU 512 485 485 LEU LEU B . n 
A 1 513 VAL 513 486 486 VAL VAL B . n 
A 1 514 GLY 514 487 487 GLY GLY B . n 
A 1 515 ASN 515 488 488 ASN ASN B . n 
A 1 516 TYR 516 489 489 TYR TYR B . n 
A 1 517 SER 517 490 490 SER SER B . n 
A 1 518 ILE 518 491 491 ILE ILE B . n 
A 1 519 ILE 519 492 492 ILE ILE B . n 
A 1 520 ASN 520 493 493 ASN ASN B . n 
A 1 521 TRP 521 494 494 TRP TRP B . n 
A 1 522 HIS 522 495 495 HIS HIS B . n 
A 1 523 LEU 523 496 496 LEU LEU B . n 
A 1 524 SER 524 497 497 SER SER B . n 
A 1 525 PRO 525 498 498 PRO PRO B . n 
A 1 526 GLU 526 499 499 GLU GLU B . n 
A 1 527 ASP 527 500 500 ASP ASP B . n 
A 1 528 GLY 528 501 501 GLY GLY B . n 
A 1 529 SER 529 502 502 SER SER B . n 
A 1 530 ILE 530 503 503 ILE ILE B . n 
A 1 531 VAL 531 504 504 VAL VAL B . n 
A 1 532 PHE 532 505 505 PHE PHE B . n 
A 1 533 LYS 533 506 506 LYS LYS B . n 
A 1 534 GLU 534 507 507 GLU GLU B . n 
A 1 535 VAL 535 508 508 VAL VAL B . n 
A 1 536 GLY 536 509 509 GLY GLY B . n 
A 1 537 TYR 537 510 510 TYR TYR B . n 
A 1 538 TYR 538 511 511 TYR TYR B . n 
A 1 539 ASN 539 512 512 ASN ASN B . n 
A 1 540 VAL 540 513 513 VAL VAL B . n 
A 1 541 TYR 541 514 514 TYR TYR B . n 
A 1 542 ALA 542 515 515 ALA ALA B . n 
A 1 543 LYS 543 516 516 LYS LYS B . n 
A 1 544 LYS 544 517 517 LYS LYS B . n 
A 1 545 GLY 545 518 518 GLY GLY B . n 
A 1 546 GLU 546 519 519 GLU GLU B . n 
A 1 547 ARG 547 520 520 ARG ARG B . n 
A 1 548 LEU 548 521 521 LEU LEU B . n 
A 1 549 PHE 549 522 522 PHE PHE B . n 
A 1 550 ILE 550 523 523 ILE ILE B . n 
A 1 551 ASN 551 524 524 ASN ASN B . n 
A 1 552 GLU 552 525 525 GLU GLU B . n 
A 1 553 GLU 553 526 526 GLU GLU B . n 
A 1 554 LYS 554 527 527 LYS LYS B . n 
A 1 555 ILE 555 528 528 ILE ILE B . n 
A 1 556 LEU 556 529 529 LEU LEU B . n 
A 1 557 TRP 557 530 530 TRP TRP B . n 
A 1 558 SER 558 531 531 SER SER B . n 
A 1 559 GLY 559 532 532 GLY GLY B . n 
A 1 560 PHE 560 533 533 PHE PHE B . n 
A 1 561 SER 561 534 534 SER SER B . n 
A 1 562 ARG 562 535 ?   ?   ?   B . n 
A 1 563 GLU 563 536 ?   ?   ?   B . n 
A 1 564 VAL 564 537 ?   ?   ?   B . n 
A 1 565 PRO 565 538 ?   ?   ?   B . n 
A 1 566 PHE 566 539 ?   ?   ?   B . n 
A 1 567 SER 567 540 ?   ?   ?   B . n 
A 1 568 ASN 568 541 ?   ?   ?   B . n 
B 1 1   MET 1   -26 ?   ?   ?   A . n 
B 1 2   ARG 2   -25 ?   ?   ?   A . n 
B 1 3   LEU 3   -24 ?   ?   ?   A . n 
B 1 4   LEU 4   -23 ?   ?   ?   A . n 
B 1 5   THR 5   -22 ?   ?   ?   A . n 
B 1 6   ALA 6   -21 ?   ?   ?   A . n 
B 1 7   LEU 7   -20 ?   ?   ?   A . n 
B 1 8   PHE 8   -19 ?   ?   ?   A . n 
B 1 9   ALA 9   -18 ?   ?   ?   A . n 
B 1 10  TYR 10  -17 ?   ?   ?   A . n 
B 1 11  PHE 11  -16 ?   ?   ?   A . n 
B 1 12  ILE 12  -15 ?   ?   ?   A . n 
B 1 13  VAL 13  -14 ?   ?   ?   A . n 
B 1 14  ALA 14  -13 ?   ?   ?   A . n 
B 1 15  LEU 15  -12 ?   ?   ?   A . n 
B 1 16  ILE 16  -11 ?   ?   ?   A . n 
B 1 17  LEU 17  -10 ?   ?   ?   A . n 
B 1 18  ALA 18  -9  ?   ?   ?   A . n 
B 1 19  PHE 19  -8  ?   ?   ?   A . n 
B 1 20  SER 20  -7  ?   ?   ?   A . n 
B 1 21  VAL 21  -6  ?   ?   ?   A . n 
B 1 22  SER 22  -5  ?   ?   ?   A . n 
B 1 23  ALA 23  -4  ?   ?   ?   A . n 
B 1 24  LYS 24  -3  ?   ?   ?   A . n 
B 1 25  SER 25  -2  ?   ?   ?   A . n 
B 1 26  MET 26  -1  ?   ?   ?   A . n 
B 1 27  HIS 27  0   ?   ?   ?   A . n 
B 1 28  HIS 28  1   ?   ?   ?   A . n 
B 1 29  HIS 29  2   ?   ?   ?   A . n 
B 1 30  HIS 30  3   ?   ?   ?   A . n 
B 1 31  HIS 31  4   ?   ?   ?   A . n 
B 1 32  HIS 32  5   ?   ?   ?   A . n 
B 1 33  HIS 33  6   ?   ?   ?   A . n 
B 1 34  HIS 34  7   ?   ?   ?   A . n 
B 1 35  SER 35  8   ?   ?   ?   A . n 
B 1 36  ALA 36  9   ?   ?   ?   A . n 
B 1 37  TRP 37  10  ?   ?   ?   A . n 
B 1 38  SER 38  11  ?   ?   ?   A . n 
B 1 39  HIS 39  12  ?   ?   ?   A . n 
B 1 40  PRO 40  13  ?   ?   ?   A . n 
B 1 41  GLN 41  14  ?   ?   ?   A . n 
B 1 42  PHE 42  15  ?   ?   ?   A . n 
B 1 43  GLU 43  16  ?   ?   ?   A . n 
B 1 44  LYS 44  17  ?   ?   ?   A . n 
B 1 45  GLU 45  18  ?   ?   ?   A . n 
B 1 46  PHE 46  19  ?   ?   ?   A . n 
B 1 47  TYR 47  20  ?   ?   ?   A . n 
B 1 48  GLY 48  21  ?   ?   ?   A . n 
B 1 49  PRO 49  22  22  PRO PRO A . n 
B 1 50  ASP 50  23  23  ASP ASP A . n 
B 1 51  GLN 51  24  24  GLN GLN A . n 
B 1 52  ARG 52  25  25  ARG ARG A . n 
B 1 53  ALA 53  26  26  ALA ALA A . n 
B 1 54  GLN 54  27  27  GLN GLN A . n 
B 1 55  LYS 55  28  28  LYS LYS A . n 
B 1 56  LYS 56  29  29  LYS LYS A . n 
B 1 57  GLY 57  30  30  GLY GLY A . n 
B 1 58  ASP 58  31  31  ASP ASP A . n 
B 1 59  ILE 59  32  32  ILE ILE A . n 
B 1 60  ILE 60  33  33  ILE ILE A . n 
B 1 61  LEU 61  34  34  LEU LEU A . n 
B 1 62  GLY 62  35  35  GLY GLY A . n 
B 1 63  GLY 63  36  36  GLY GLY A . n 
B 1 64  LEU 64  37  37  LEU LEU A . n 
B 1 65  PHE 65  38  38  PHE PHE A . n 
B 1 66  PRO 66  39  39  PRO PRO A . n 
B 1 67  ILE 67  40  40  ILE ILE A . n 
B 1 68  HIS 68  41  41  HIS HIS A . n 
B 1 69  PHE 69  42  42  PHE PHE A . n 
B 1 70  GLY 70  43  43  GLY GLY A . n 
B 1 71  VAL 71  44  44  VAL VAL A . n 
B 1 72  ALA 72  45  45  ALA ALA A . n 
B 1 73  ALA 73  46  46  ALA ALA A . n 
B 1 74  LYS 74  47  47  LYS LYS A . n 
B 1 75  ASP 75  48  48  ASP ASP A . n 
B 1 76  GLN 76  49  49  GLN GLN A . n 
B 1 77  ASP 77  50  50  ASP ASP A . n 
B 1 78  LEU 78  51  51  LEU LEU A . n 
B 1 79  LYS 79  52  52  LYS LYS A . n 
B 1 80  SER 80  53  53  SER SER A . n 
B 1 81  ARG 81  54  54  ARG ARG A . n 
B 1 82  PRO 82  55  55  PRO PRO A . n 
B 1 83  GLU 83  56  56  GLU GLU A . n 
B 1 84  SER 84  57  57  SER SER A . n 
B 1 85  VAL 85  58  58  VAL VAL A . n 
B 1 86  GLU 86  59  59  GLU GLU A . n 
B 1 87  CYS 87  60  60  CYS CYS A . n 
B 1 88  ILE 88  61  61  ILE ILE A . n 
B 1 89  ARG 89  62  62  ARG ARG A . n 
B 1 90  TYR 90  63  63  TYR TYR A . n 
B 1 91  ASN 91  64  64  ASN ASN A . n 
B 1 92  PHE 92  65  65  PHE PHE A . n 
B 1 93  ARG 93  66  66  ARG ARG A . n 
B 1 94  GLY 94  67  67  GLY GLY A . n 
B 1 95  PHE 95  68  68  PHE PHE A . n 
B 1 96  ARG 96  69  69  ARG ARG A . n 
B 1 97  TRP 97  70  70  TRP TRP A . n 
B 1 98  LEU 98  71  71  LEU LEU A . n 
B 1 99  GLN 99  72  72  GLN GLN A . n 
B 1 100 ALA 100 73  73  ALA ALA A . n 
B 1 101 MET 101 74  74  MET MET A . n 
B 1 102 ILE 102 75  75  ILE ILE A . n 
B 1 103 PHE 103 76  76  PHE PHE A . n 
B 1 104 ALA 104 77  77  ALA ALA A . n 
B 1 105 ILE 105 78  78  ILE ILE A . n 
B 1 106 GLU 106 79  79  GLU GLU A . n 
B 1 107 GLU 107 80  80  GLU GLU A . n 
B 1 108 ILE 108 81  81  ILE ILE A . n 
B 1 109 ASN 109 82  82  ASN ASN A . n 
B 1 110 SER 110 83  83  SER SER A . n 
B 1 111 SER 111 84  84  SER SER A . n 
B 1 112 PRO 112 85  85  PRO PRO A . n 
B 1 113 ALA 113 86  86  ALA ALA A . n 
B 1 114 LEU 114 87  87  LEU LEU A . n 
B 1 115 LEU 115 88  88  LEU LEU A . n 
B 1 116 PRO 116 89  89  PRO PRO A . n 
B 1 117 ASN 117 90  90  ASN ASN A . n 
B 1 118 LEU 118 91  91  LEU LEU A . n 
B 1 119 THR 119 92  92  THR THR A . n 
B 1 120 LEU 120 93  93  LEU LEU A . n 
B 1 121 GLY 121 94  94  GLY GLY A . n 
B 1 122 TYR 122 95  95  TYR TYR A . n 
B 1 123 ARG 123 96  96  ARG ARG A . n 
B 1 124 ILE 124 97  97  ILE ILE A . n 
B 1 125 PHE 125 98  98  PHE PHE A . n 
B 1 126 ASP 126 99  99  ASP ASP A . n 
B 1 127 THR 127 100 100 THR THR A . n 
B 1 128 CYS 128 101 101 CYS CYS A . n 
B 1 129 ASN 129 102 102 ASN ASN A . n 
B 1 130 THR 130 103 103 THR THR A . n 
B 1 131 VAL 131 104 104 VAL VAL A . n 
B 1 132 SER 132 105 105 SER SER A . n 
B 1 133 LYS 133 106 106 LYS LYS A . n 
B 1 134 ALA 134 107 107 ALA ALA A . n 
B 1 135 LEU 135 108 108 LEU LEU A . n 
B 1 136 GLU 136 109 109 GLU GLU A . n 
B 1 137 ALA 137 110 110 ALA ALA A . n 
B 1 138 THR 138 111 111 THR THR A . n 
B 1 139 LEU 139 112 112 LEU LEU A . n 
B 1 140 SER 140 113 113 SER SER A . n 
B 1 141 PHE 141 114 114 PHE PHE A . n 
B 1 142 VAL 142 115 115 VAL VAL A . n 
B 1 143 ALA 143 116 116 ALA ALA A . n 
B 1 144 GLN 144 117 117 GLN GLN A . n 
B 1 145 ASN 145 118 118 ASN ASN A . n 
B 1 146 LYS 146 119 119 LYS LYS A . n 
B 1 147 ILE 147 120 120 ILE ILE A . n 
B 1 148 ASP 148 121 121 ASP ASP A . n 
B 1 149 SER 149 122 ?   ?   ?   A . n 
B 1 150 LEU 150 123 ?   ?   ?   A . n 
B 1 151 ASN 151 124 ?   ?   ?   A . n 
B 1 152 LEU 152 125 ?   ?   ?   A . n 
B 1 153 ASP 153 126 ?   ?   ?   A . n 
B 1 154 GLU 154 127 ?   ?   ?   A . n 
B 1 155 PHE 155 128 ?   ?   ?   A . n 
B 1 156 CYS 156 129 ?   ?   ?   A . n 
B 1 157 ASN 157 130 ?   ?   ?   A . n 
B 1 158 CYS 158 131 ?   ?   ?   A . n 
B 1 159 SER 159 132 ?   ?   ?   A . n 
B 1 160 GLU 160 133 ?   ?   ?   A . n 
B 1 161 HIS 161 134 ?   ?   ?   A . n 
B 1 162 ILE 162 135 ?   ?   ?   A . n 
B 1 163 PRO 163 136 ?   ?   ?   A . n 
B 1 164 SER 164 137 137 SER SER A . n 
B 1 165 THR 165 138 138 THR THR A . n 
B 1 166 ILE 166 139 139 ILE ILE A . n 
B 1 167 ALA 167 140 140 ALA ALA A . n 
B 1 168 VAL 168 141 141 VAL VAL A . n 
B 1 169 VAL 169 142 142 VAL VAL A . n 
B 1 170 GLY 170 143 143 GLY GLY A . n 
B 1 171 ALA 171 144 144 ALA ALA A . n 
B 1 172 THR 172 145 145 THR THR A . n 
B 1 173 GLY 173 146 146 GLY GLY A . n 
B 1 174 SER 174 147 147 SER SER A . n 
B 1 175 GLY 175 148 148 GLY GLY A . n 
B 1 176 VAL 176 149 149 VAL VAL A . n 
B 1 177 SER 177 150 150 SER SER A . n 
B 1 178 THR 178 151 151 THR THR A . n 
B 1 179 ALA 179 152 152 ALA ALA A . n 
B 1 180 VAL 180 153 153 VAL VAL A . n 
B 1 181 ALA 181 154 154 ALA ALA A . n 
B 1 182 ASN 182 155 155 ASN ASN A . n 
B 1 183 LEU 183 156 156 LEU LEU A . n 
B 1 184 LEU 184 157 157 LEU LEU A . n 
B 1 185 GLY 185 158 158 GLY GLY A . n 
B 1 186 LEU 186 159 159 LEU LEU A . n 
B 1 187 PHE 187 160 160 PHE PHE A . n 
B 1 188 TYR 188 161 161 TYR TYR A . n 
B 1 189 ILE 189 162 162 ILE ILE A . n 
B 1 190 PRO 190 163 163 PRO PRO A . n 
B 1 191 GLN 191 164 164 GLN GLN A . n 
B 1 192 VAL 192 165 165 VAL VAL A . n 
B 1 193 SER 193 166 166 SER SER A . n 
B 1 194 TYR 194 167 167 TYR TYR A . n 
B 1 195 ALA 195 168 168 ALA ALA A . n 
B 1 196 SER 196 169 169 SER SER A . n 
B 1 197 SER 197 170 170 SER SER A . n 
B 1 198 SER 198 171 171 SER SER A . n 
B 1 199 ARG 199 172 172 ARG ARG A . n 
B 1 200 LEU 200 173 173 LEU LEU A . n 
B 1 201 LEU 201 174 174 LEU LEU A . n 
B 1 202 SER 202 175 175 SER SER A . n 
B 1 203 ASN 203 176 176 ASN ASN A . n 
B 1 204 LYS 204 177 177 LYS LYS A . n 
B 1 205 ASN 205 178 178 ASN ASN A . n 
B 1 206 GLN 206 179 179 GLN GLN A . n 
B 1 207 PHE 207 180 180 PHE PHE A . n 
B 1 208 LYS 208 181 181 LYS LYS A . n 
B 1 209 SER 209 182 182 SER SER A . n 
B 1 210 PHE 210 183 183 PHE PHE A . n 
B 1 211 LEU 211 184 184 LEU LEU A . n 
B 1 212 ARG 212 185 185 ARG ARG A . n 
B 1 213 THR 213 186 186 THR THR A . n 
B 1 214 ILE 214 187 187 ILE ILE A . n 
B 1 215 PRO 215 188 188 PRO PRO A . n 
B 1 216 ASN 216 189 189 ASN ASN A . n 
B 1 217 ASP 217 190 190 ASP ASP A . n 
B 1 218 GLU 218 191 191 GLU GLU A . n 
B 1 219 HIS 219 192 192 HIS HIS A . n 
B 1 220 GLN 220 193 193 GLN GLN A . n 
B 1 221 ALA 221 194 194 ALA ALA A . n 
B 1 222 THR 222 195 195 THR THR A . n 
B 1 223 ALA 223 196 196 ALA ALA A . n 
B 1 224 MET 224 197 197 MET MET A . n 
B 1 225 ALA 225 198 198 ALA ALA A . n 
B 1 226 ASP 226 199 199 ASP ASP A . n 
B 1 227 ILE 227 200 200 ILE ILE A . n 
B 1 228 ILE 228 201 201 ILE ILE A . n 
B 1 229 GLU 229 202 202 GLU GLU A . n 
B 1 230 TYR 230 203 203 TYR TYR A . n 
B 1 231 PHE 231 204 204 PHE PHE A . n 
B 1 232 ARG 232 205 205 ARG ARG A . n 
B 1 233 TRP 233 206 206 TRP TRP A . n 
B 1 234 ASN 234 207 207 ASN ASN A . n 
B 1 235 TRP 235 208 208 TRP TRP A . n 
B 1 236 VAL 236 209 209 VAL VAL A . n 
B 1 237 GLY 237 210 210 GLY GLY A . n 
B 1 238 THR 238 211 211 THR THR A . n 
B 1 239 ILE 239 212 212 ILE ILE A . n 
B 1 240 ALA 240 213 213 ALA ALA A . n 
B 1 241 ALA 241 214 214 ALA ALA A . n 
B 1 242 ASP 242 215 215 ASP ASP A . n 
B 1 243 ASP 243 216 216 ASP ASP A . n 
B 1 244 ASP 244 217 217 ASP ASP A . n 
B 1 245 TYR 245 218 218 TYR TYR A . n 
B 1 246 GLY 246 219 219 GLY GLY A . n 
B 1 247 ARG 247 220 220 ARG ARG A . n 
B 1 248 PRO 248 221 221 PRO PRO A . n 
B 1 249 GLY 249 222 222 GLY GLY A . n 
B 1 250 ILE 250 223 223 ILE ILE A . n 
B 1 251 GLU 251 224 224 GLU GLU A . n 
B 1 252 LYS 252 225 225 LYS LYS A . n 
B 1 253 PHE 253 226 226 PHE PHE A . n 
B 1 254 ARG 254 227 227 ARG ARG A . n 
B 1 255 GLU 255 228 228 GLU GLU A . n 
B 1 256 GLU 256 229 229 GLU GLU A . n 
B 1 257 ALA 257 230 230 ALA ALA A . n 
B 1 258 GLU 258 231 231 GLU GLU A . n 
B 1 259 GLU 259 232 232 GLU GLU A . n 
B 1 260 ARG 260 233 233 ARG ARG A . n 
B 1 261 ASP 261 234 234 ASP ASP A . n 
B 1 262 ILE 262 235 235 ILE ILE A . n 
B 1 263 CSO 263 236 236 CSO CSO A . n 
B 1 264 ILE 264 237 237 ILE ILE A . n 
B 1 265 ASP 265 238 238 ASP ASP A . n 
B 1 266 PHE 266 239 239 PHE PHE A . n 
B 1 267 SER 267 240 240 SER SER A . n 
B 1 268 GLU 268 241 241 GLU GLU A . n 
B 1 269 LEU 269 242 242 LEU LEU A . n 
B 1 270 ILE 270 243 243 ILE ILE A . n 
B 1 271 SER 271 244 244 SER SER A . n 
B 1 272 GLN 272 245 245 GLN GLN A . n 
B 1 273 TYR 273 246 246 TYR TYR A . n 
B 1 274 SER 274 247 247 SER SER A . n 
B 1 275 ASP 275 248 248 ASP ASP A . n 
B 1 276 GLU 276 249 249 GLU GLU A . n 
B 1 277 GLU 277 250 250 GLU GLU A . n 
B 1 278 GLU 278 251 251 GLU GLU A . n 
B 1 279 ILE 279 252 252 ILE ILE A . n 
B 1 280 GLN 280 253 253 GLN GLN A . n 
B 1 281 HIS 281 254 254 HIS HIS A . n 
B 1 282 VAL 282 255 255 VAL VAL A . n 
B 1 283 VAL 283 256 256 VAL VAL A . n 
B 1 284 GLU 284 257 257 GLU GLU A . n 
B 1 285 VAL 285 258 258 VAL VAL A . n 
B 1 286 ILE 286 259 259 ILE ILE A . n 
B 1 287 GLN 287 260 260 GLN GLN A . n 
B 1 288 ASN 288 261 261 ASN ASN A . n 
B 1 289 SER 289 262 262 SER SER A . n 
B 1 290 THR 290 263 263 THR THR A . n 
B 1 291 ALA 291 264 264 ALA ALA A . n 
B 1 292 LYS 292 265 265 LYS LYS A . n 
B 1 293 VAL 293 266 266 VAL VAL A . n 
B 1 294 ILE 294 267 267 ILE ILE A . n 
B 1 295 VAL 295 268 268 VAL VAL A . n 
B 1 296 VAL 296 269 269 VAL VAL A . n 
B 1 297 PHE 297 270 270 PHE PHE A . n 
B 1 298 SER 298 271 271 SER SER A . n 
B 1 299 SER 299 272 272 SER SER A . n 
B 1 300 GLY 300 273 273 GLY GLY A . n 
B 1 301 PRO 301 274 274 PRO PRO A . n 
B 1 302 ASP 302 275 275 ASP ASP A . n 
B 1 303 LEU 303 276 276 LEU LEU A . n 
B 1 304 GLU 304 277 277 GLU GLU A . n 
B 1 305 PRO 305 278 278 PRO PRO A . n 
B 1 306 LEU 306 279 279 LEU LEU A . n 
B 1 307 ILE 307 280 280 ILE ILE A . n 
B 1 308 LYS 308 281 281 LYS LYS A . n 
B 1 309 GLU 309 282 282 GLU GLU A . n 
B 1 310 ILE 310 283 283 ILE ILE A . n 
B 1 311 VAL 311 284 284 VAL VAL A . n 
B 1 312 ARG 312 285 285 ARG ARG A . n 
B 1 313 ARG 313 286 286 ARG ARG A . n 
B 1 314 ASN 314 287 287 ASN ASN A . n 
B 1 315 ILE 315 288 288 ILE ILE A . n 
B 1 316 THR 316 289 289 THR THR A . n 
B 1 317 GLY 317 290 290 GLY GLY A . n 
B 1 318 LYS 318 291 291 LYS LYS A . n 
B 1 319 ILE 319 292 292 ILE ILE A . n 
B 1 320 TRP 320 293 293 TRP TRP A . n 
B 1 321 LEU 321 294 294 LEU LEU A . n 
B 1 322 ALA 322 295 295 ALA ALA A . n 
B 1 323 SER 323 296 296 SER SER A . n 
B 1 324 GLU 324 297 297 GLU GLU A . n 
B 1 325 ALA 325 298 298 ALA ALA A . n 
B 1 326 TRP 326 299 299 TRP TRP A . n 
B 1 327 ALA 327 300 300 ALA ALA A . n 
B 1 328 SER 328 301 301 SER SER A . n 
B 1 329 SER 329 302 302 SER SER A . n 
B 1 330 SER 330 303 303 SER SER A . n 
B 1 331 LEU 331 304 304 LEU LEU A . n 
B 1 332 ILE 332 305 305 ILE ILE A . n 
B 1 333 ALA 333 306 306 ALA ALA A . n 
B 1 334 MET 334 307 307 MET MET A . n 
B 1 335 PRO 335 308 308 PRO PRO A . n 
B 1 336 GLN 336 309 309 GLN GLN A . n 
B 1 337 TYR 337 310 310 TYR TYR A . n 
B 1 338 PHE 338 311 311 PHE PHE A . n 
B 1 339 HIS 339 312 312 HIS HIS A . n 
B 1 340 VAL 340 313 313 VAL VAL A . n 
B 1 341 VAL 341 314 314 VAL VAL A . n 
B 1 342 GLY 342 315 315 GLY GLY A . n 
B 1 343 GLY 343 316 316 GLY GLY A . n 
B 1 344 THR 344 317 317 THR THR A . n 
B 1 345 ILE 345 318 318 ILE ILE A . n 
B 1 346 GLY 346 319 319 GLY GLY A . n 
B 1 347 PHE 347 320 320 PHE PHE A . n 
B 1 348 ALA 348 321 321 ALA ALA A . n 
B 1 349 LEU 349 322 322 LEU LEU A . n 
B 1 350 LYS 350 323 323 LYS LYS A . n 
B 1 351 ALA 351 324 324 ALA ALA A . n 
B 1 352 GLY 352 325 325 GLY GLY A . n 
B 1 353 GLN 353 326 326 GLN GLN A . n 
B 1 354 ILE 354 327 327 ILE ILE A . n 
B 1 355 PRO 355 328 328 PRO PRO A . n 
B 1 356 GLY 356 329 329 GLY GLY A . n 
B 1 357 PHE 357 330 330 PHE PHE A . n 
B 1 358 ARG 358 331 331 ARG ARG A . n 
B 1 359 GLU 359 332 332 GLU GLU A . n 
B 1 360 PHE 360 333 333 PHE PHE A . n 
B 1 361 LEU 361 334 334 LEU LEU A . n 
B 1 362 LYS 362 335 335 LYS LYS A . n 
B 1 363 LYS 363 336 336 LYS LYS A . n 
B 1 364 VAL 364 337 337 VAL VAL A . n 
B 1 365 HIS 365 338 338 HIS HIS A . n 
B 1 366 PRO 366 339 339 PRO PRO A . n 
B 1 367 ARG 367 340 340 ARG ARG A . n 
B 1 368 LYS 368 341 341 LYS LYS A . n 
B 1 369 SER 369 342 342 SER SER A . n 
B 1 370 VAL 370 343 343 VAL VAL A . n 
B 1 371 HIS 371 344 344 HIS HIS A . n 
B 1 372 ASN 372 345 345 ASN ASN A . n 
B 1 373 GLY 373 346 346 GLY GLY A . n 
B 1 374 PHE 374 347 347 PHE PHE A . n 
B 1 375 ALA 375 348 348 ALA ALA A . n 
B 1 376 LYS 376 349 349 LYS LYS A . n 
B 1 377 GLU 377 350 350 GLU GLU A . n 
B 1 378 PHE 378 351 351 PHE PHE A . n 
B 1 379 TRP 379 352 352 TRP TRP A . n 
B 1 380 GLU 380 353 353 GLU GLU A . n 
B 1 381 GLU 381 354 354 GLU GLU A . n 
B 1 382 THR 382 355 355 THR THR A . n 
B 1 383 PHE 383 356 356 PHE PHE A . n 
B 1 384 ASN 384 357 357 ASN ASN A . n 
B 1 385 CYS 385 358 358 CYS CYS A . n 
B 1 386 HIS 386 359 359 HIS HIS A . n 
B 1 387 LEU 387 360 360 LEU LEU A . n 
B 1 388 GLN 388 361 361 GLN GLN A . n 
B 1 389 GLU 389 362 ?   ?   ?   A . n 
B 1 390 GLY 390 363 ?   ?   ?   A . n 
B 1 391 ALA 391 364 ?   ?   ?   A . n 
B 1 392 LYS 392 365 ?   ?   ?   A . n 
B 1 393 GLY 393 366 ?   ?   ?   A . n 
B 1 394 PRO 394 367 ?   ?   ?   A . n 
B 1 395 LEU 395 368 ?   ?   ?   A . n 
B 1 396 PRO 396 369 ?   ?   ?   A . n 
B 1 397 VAL 397 370 ?   ?   ?   A . n 
B 1 398 ASP 398 371 ?   ?   ?   A . n 
B 1 399 THR 399 372 ?   ?   ?   A . n 
B 1 400 PHE 400 373 ?   ?   ?   A . n 
B 1 401 LEU 401 374 ?   ?   ?   A . n 
B 1 402 ARG 402 375 ?   ?   ?   A . n 
B 1 403 GLY 403 376 ?   ?   ?   A . n 
B 1 404 HIS 404 377 ?   ?   ?   A . n 
B 1 405 GLU 405 378 ?   ?   ?   A . n 
B 1 406 GLU 406 379 ?   ?   ?   A . n 
B 1 407 SER 407 380 ?   ?   ?   A . n 
B 1 408 GLY 408 381 ?   ?   ?   A . n 
B 1 409 ASP 409 382 ?   ?   ?   A . n 
B 1 410 ARG 410 383 ?   ?   ?   A . n 
B 1 411 PHE 411 384 ?   ?   ?   A . n 
B 1 412 SER 412 385 ?   ?   ?   A . n 
B 1 413 ASN 413 386 ?   ?   ?   A . n 
B 1 414 SER 414 387 ?   ?   ?   A . n 
B 1 415 SER 415 388 ?   ?   ?   A . n 
B 1 416 THR 416 389 ?   ?   ?   A . n 
B 1 417 ALA 417 390 ?   ?   ?   A . n 
B 1 418 PHE 418 391 ?   ?   ?   A . n 
B 1 419 ARG 419 392 392 ARG ARG A . n 
B 1 420 PRO 420 393 393 PRO PRO A . n 
B 1 421 LEU 421 394 394 LEU LEU A . n 
B 1 422 CYS 422 395 395 CYS CYS A . n 
B 1 423 THR 423 396 396 THR THR A . n 
B 1 424 GLY 424 397 397 GLY GLY A . n 
B 1 425 ASP 425 398 398 ASP ASP A . n 
B 1 426 GLU 426 399 399 GLU GLU A . n 
B 1 427 ASN 427 400 400 ASN ASN A . n 
B 1 428 ILE 428 401 401 ILE ILE A . n 
B 1 429 SER 429 402 402 SER SER A . n 
B 1 430 SER 430 403 403 SER SER A . n 
B 1 431 VAL 431 404 404 VAL VAL A . n 
B 1 432 GLU 432 405 405 GLU GLU A . n 
B 1 433 THR 433 406 406 THR THR A . n 
B 1 434 PRO 434 407 407 PRO PRO A . n 
B 1 435 TYR 435 408 408 TYR TYR A . n 
B 1 436 ILE 436 409 409 ILE ILE A . n 
B 1 437 ASP 437 410 410 ASP ASP A . n 
B 1 438 TYR 438 411 411 TYR TYR A . n 
B 1 439 THR 439 412 412 THR THR A . n 
B 1 440 HIS 440 413 413 HIS HIS A . n 
B 1 441 LEU 441 414 414 LEU LEU A . n 
B 1 442 ARG 442 415 415 ARG ARG A . n 
B 1 443 ILE 443 416 416 ILE ILE A . n 
B 1 444 SER 444 417 417 SER SER A . n 
B 1 445 TYR 445 418 418 TYR TYR A . n 
B 1 446 ASN 446 419 419 ASN ASN A . n 
B 1 447 VAL 447 420 420 VAL VAL A . n 
B 1 448 TYR 448 421 421 TYR TYR A . n 
B 1 449 LEU 449 422 422 LEU LEU A . n 
B 1 450 ALA 450 423 423 ALA ALA A . n 
B 1 451 VAL 451 424 424 VAL VAL A . n 
B 1 452 TYR 452 425 425 TYR TYR A . n 
B 1 453 SER 453 426 426 SER SER A . n 
B 1 454 ILE 454 427 427 ILE ILE A . n 
B 1 455 ALA 455 428 428 ALA ALA A . n 
B 1 456 HIS 456 429 429 HIS HIS A . n 
B 1 457 ALA 457 430 430 ALA ALA A . n 
B 1 458 LEU 458 431 431 LEU LEU A . n 
B 1 459 GLN 459 432 432 GLN GLN A . n 
B 1 460 ASP 460 433 433 ASP ASP A . n 
B 1 461 ILE 461 434 434 ILE ILE A . n 
B 1 462 TYR 462 435 435 TYR TYR A . n 
B 1 463 THR 463 436 436 THR THR A . n 
B 1 464 CYS 464 437 437 CYS CYS A . n 
B 1 465 LEU 465 438 438 LEU LEU A . n 
B 1 466 PRO 466 439 439 PRO PRO A . n 
B 1 467 GLY 467 440 440 GLY GLY A . n 
B 1 468 ARG 468 441 441 ARG ARG A . n 
B 1 469 GLY 469 442 442 GLY GLY A . n 
B 1 470 LEU 470 443 443 LEU LEU A . n 
B 1 471 PHE 471 444 444 PHE PHE A . n 
B 1 472 THR 472 445 445 THR THR A . n 
B 1 473 ASN 473 446 446 ASN ASN A . n 
B 1 474 GLY 474 447 447 GLY GLY A . n 
B 1 475 SER 475 448 448 SER SER A . n 
B 1 476 CYS 476 449 449 CYS CYS A . n 
B 1 477 ALA 477 450 450 ALA ALA A . n 
B 1 478 ASP 478 451 451 ASP ASP A . n 
B 1 479 ILE 479 452 452 ILE ILE A . n 
B 1 480 LYS 480 453 453 LYS LYS A . n 
B 1 481 LYS 481 454 454 LYS LYS A . n 
B 1 482 VAL 482 455 455 VAL VAL A . n 
B 1 483 GLU 483 456 456 GLU GLU A . n 
B 1 484 ALA 484 457 457 ALA ALA A . n 
B 1 485 TRP 485 458 458 TRP TRP A . n 
B 1 486 GLN 486 459 459 GLN GLN A . n 
B 1 487 VAL 487 460 460 VAL VAL A . n 
B 1 488 LEU 488 461 461 LEU LEU A . n 
B 1 489 LYS 489 462 462 LYS LYS A . n 
B 1 490 HIS 490 463 463 HIS HIS A . n 
B 1 491 LEU 491 464 464 LEU LEU A . n 
B 1 492 ARG 492 465 465 ARG ARG A . n 
B 1 493 HIS 493 466 466 HIS HIS A . n 
B 1 494 LEU 494 467 467 LEU LEU A . n 
B 1 495 ASN 495 468 468 ASN ASN A . n 
B 1 496 PHE 496 469 469 PHE PHE A . n 
B 1 497 THR 497 470 470 THR THR A . n 
B 1 498 ASN 498 471 471 ASN ASN A . n 
B 1 499 ASN 499 472 472 ASN ASN A . n 
B 1 500 MET 500 473 473 MET MET A . n 
B 1 501 GLY 501 474 474 GLY GLY A . n 
B 1 502 GLU 502 475 475 GLU GLU A . n 
B 1 503 GLN 503 476 476 GLN GLN A . n 
B 1 504 VAL 504 477 477 VAL VAL A . n 
B 1 505 THR 505 478 478 THR THR A . n 
B 1 506 PHE 506 479 479 PHE PHE A . n 
B 1 507 ASP 507 480 480 ASP ASP A . n 
B 1 508 GLU 508 481 481 GLU GLU A . n 
B 1 509 CSO 509 482 482 CSO CSO A . n 
B 1 510 GLY 510 483 483 GLY GLY A . n 
B 1 511 ASP 511 484 484 ASP ASP A . n 
B 1 512 LEU 512 485 485 LEU LEU A . n 
B 1 513 VAL 513 486 486 VAL VAL A . n 
B 1 514 GLY 514 487 487 GLY GLY A . n 
B 1 515 ASN 515 488 488 ASN ASN A . n 
B 1 516 TYR 516 489 489 TYR TYR A . n 
B 1 517 SER 517 490 490 SER SER A . n 
B 1 518 ILE 518 491 491 ILE ILE A . n 
B 1 519 ILE 519 492 492 ILE ILE A . n 
B 1 520 ASN 520 493 493 ASN ASN A . n 
B 1 521 TRP 521 494 494 TRP TRP A . n 
B 1 522 HIS 522 495 495 HIS HIS A . n 
B 1 523 LEU 523 496 496 LEU LEU A . n 
B 1 524 SER 524 497 497 SER SER A . n 
B 1 525 PRO 525 498 498 PRO PRO A . n 
B 1 526 GLU 526 499 499 GLU GLU A . n 
B 1 527 ASP 527 500 500 ASP ASP A . n 
B 1 528 GLY 528 501 501 GLY GLY A . n 
B 1 529 SER 529 502 502 SER SER A . n 
B 1 530 ILE 530 503 503 ILE ILE A . n 
B 1 531 VAL 531 504 504 VAL VAL A . n 
B 1 532 PHE 532 505 505 PHE PHE A . n 
B 1 533 LYS 533 506 506 LYS LYS A . n 
B 1 534 GLU 534 507 507 GLU GLU A . n 
B 1 535 VAL 535 508 508 VAL VAL A . n 
B 1 536 GLY 536 509 509 GLY GLY A . n 
B 1 537 TYR 537 510 510 TYR TYR A . n 
B 1 538 TYR 538 511 511 TYR TYR A . n 
B 1 539 ASN 539 512 512 ASN ASN A . n 
B 1 540 VAL 540 513 513 VAL VAL A . n 
B 1 541 TYR 541 514 514 TYR TYR A . n 
B 1 542 ALA 542 515 515 ALA ALA A . n 
B 1 543 LYS 543 516 516 LYS LYS A . n 
B 1 544 LYS 544 517 517 LYS LYS A . n 
B 1 545 GLY 545 518 518 GLY GLY A . n 
B 1 546 GLU 546 519 519 GLU GLU A . n 
B 1 547 ARG 547 520 520 ARG ARG A . n 
B 1 548 LEU 548 521 521 LEU LEU A . n 
B 1 549 PHE 549 522 522 PHE PHE A . n 
B 1 550 ILE 550 523 523 ILE ILE A . n 
B 1 551 ASN 551 524 524 ASN ASN A . n 
B 1 552 GLU 552 525 525 GLU GLU A . n 
B 1 553 GLU 553 526 526 GLU GLU A . n 
B 1 554 LYS 554 527 527 LYS LYS A . n 
B 1 555 ILE 555 528 528 ILE ILE A . n 
B 1 556 LEU 556 529 529 LEU LEU A . n 
B 1 557 TRP 557 530 530 TRP TRP A . n 
B 1 558 SER 558 531 531 SER SER A . n 
B 1 559 GLY 559 532 532 GLY GLY A . n 
B 1 560 PHE 560 533 533 PHE PHE A . n 
B 1 561 SER 561 534 534 SER SER A . n 
B 1 562 ARG 562 535 535 ARG ARG A . n 
B 1 563 GLU 563 536 536 GLU GLU A . n 
B 1 564 VAL 564 537 537 VAL VAL A . n 
B 1 565 PRO 565 538 538 PRO PRO A . n 
B 1 566 PHE 566 539 ?   ?   ?   A . n 
B 1 567 SER 567 540 ?   ?   ?   A . n 
B 1 568 ASN 568 541 ?   ?   ?   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 
C 2 GD3 1  601 601 GD3 GD3 B . 
D 3 MG  1  602 602 MG  MG  B . 
E 3 MG  1  603 603 MG  MG  B . 
F 4 BCT 1  604 604 BCT BCT B . 
G 5 CL  1  605 605 CL  CL  B . 
H 6 NAG 1  606 606 NAG NAG B . 
I 6 NAG 1  607 607 NAG NAG B . 
J 6 NAG 1  608 608 NAG NAG B . 
K 7 TCR 1  609 609 TCR TCR B . 
L 2 GD3 1  601 601 GD3 GD3 A . 
M 3 MG  1  602 602 MG  MG  A . 
N 4 BCT 1  603 603 BCT BCT A . 
O 5 CL  1  604 604 CL  CL  A . 
P 6 NAG 1  605 605 NAG NAG A . 
Q 6 NAG 1  606 606 NAG NAG A . 
R 6 NAG 1  607 607 NAG NAG A . 
S 6 NAG 1  608 608 NAG NAG A . 
T 7 TCR 1  609 609 TCR TCR A . 
U 8 HOH 1  701 701 HOH HOH B . 
U 8 HOH 2  702 702 HOH HOH B . 
U 8 HOH 3  703 703 HOH HOH B . 
U 8 HOH 4  704 704 HOH HOH B . 
U 8 HOH 5  705 705 HOH HOH B . 
U 8 HOH 6  706 706 HOH HOH B . 
U 8 HOH 7  707 707 HOH HOH B . 
U 8 HOH 8  708 708 HOH HOH B . 
U 8 HOH 9  709 709 HOH HOH B . 
U 8 HOH 10 710 710 HOH HOH B . 
U 8 HOH 11 711 711 HOH HOH B . 
V 8 HOH 1  701 701 HOH HOH A . 
V 8 HOH 2  702 702 HOH HOH A . 
V 8 HOH 3  703 703 HOH HOH A . 
V 8 HOH 4  704 704 HOH HOH A . 
V 8 HOH 5  705 705 HOH HOH A . 
V 8 HOH 6  706 706 HOH HOH A . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A CSO 263 B CSO 236 ? CYS 'modified residue' 
2 A CSO 509 B CSO 482 ? CYS 'modified residue' 
3 B CSO 263 A CSO 236 ? CYS 'modified residue' 
4 B CSO 509 A CSO 482 ? CYS 'modified residue' 
# 
_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 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V 
# 
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)' 7350  ? 
1 MORE         -51   ? 
1 'SSA (A^2)'  38240 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A ILE 108 ? B ILE 81  ? 1_555 MG ? E MG  . ? B MG  603 ? 1_555 O   ? A LEU 114 ? B LEU 87  ? 1_555 84.9  ? 
2  O   ? A ILE 108 ? B ILE 81  ? 1_555 MG ? E MG  . ? B MG  603 ? 1_555 O   ? A LEU 115 ? B LEU 88  ? 1_555 145.0 ? 
3  O   ? A LEU 114 ? B LEU 87  ? 1_555 MG ? E MG  . ? B MG  603 ? 1_555 O   ? A LEU 115 ? B LEU 88  ? 1_555 61.5  ? 
4  OE1 ? A GLU 256 ? B GLU 229 ? 1_555 GD ? C GD3 . ? B GD3 601 ? 1_555 OE2 ? A GLU 256 ? B GLU 229 ? 1_555 48.2  ? 
5  OE1 ? A GLU 256 ? B GLU 229 ? 1_555 GD ? C GD3 . ? B GD3 601 ? 1_555 OE1 ? A GLU 259 ? B GLU 232 ? 1_555 79.7  ? 
6  OE2 ? A GLU 256 ? B GLU 229 ? 1_555 GD ? C GD3 . ? B GD3 601 ? 1_555 OE1 ? A GLU 259 ? B GLU 232 ? 1_555 94.6  ? 
7  O   ? A SER 267 ? B SER 240 ? 1_555 MG ? D MG  . ? B MG  602 ? 1_555 OG  ? A SER 267 ? B SER 240 ? 1_555 62.4  ? 
8  O   ? A SER 267 ? B SER 240 ? 1_555 MG ? D MG  . ? B MG  602 ? 1_555 O   ? U HOH .   ? B HOH 706 ? 1_555 69.2  ? 
9  OG  ? A SER 267 ? B SER 240 ? 1_555 MG ? D MG  . ? B MG  602 ? 1_555 O   ? U HOH .   ? B HOH 706 ? 1_555 78.2  ? 
10 O   ? B ILE 108 ? A ILE 81  ? 1_555 MG ? M MG  . ? A MG  602 ? 1_555 O   ? B SER 111 ? A SER 84  ? 1_555 77.5  ? 
11 O   ? B ILE 108 ? A ILE 81  ? 1_555 MG ? M MG  . ? A MG  602 ? 1_555 O   ? B LEU 114 ? A LEU 87  ? 1_555 90.9  ? 
12 O   ? B SER 111 ? A SER 84  ? 1_555 MG ? M MG  . ? A MG  602 ? 1_555 O   ? B LEU 114 ? A LEU 87  ? 1_555 80.5  ? 
13 O   ? B ILE 108 ? A ILE 81  ? 1_555 MG ? M MG  . ? A MG  602 ? 1_555 O   ? B LEU 115 ? A LEU 88  ? 1_555 147.7 ? 
14 O   ? B SER 111 ? A SER 84  ? 1_555 MG ? M MG  . ? A MG  602 ? 1_555 O   ? B LEU 115 ? A LEU 88  ? 1_555 116.1 ? 
15 O   ? B LEU 114 ? A LEU 87  ? 1_555 MG ? M MG  . ? A MG  602 ? 1_555 O   ? B LEU 115 ? A LEU 88  ? 1_555 64.9  ? 
16 OE1 ? B GLU 256 ? A GLU 229 ? 1_555 GD ? L GD3 . ? A GD3 601 ? 1_555 OE2 ? B GLU 256 ? A GLU 229 ? 1_555 47.5  ? 
17 OE1 ? B GLU 256 ? A GLU 229 ? 1_555 GD ? L GD3 . ? A GD3 601 ? 1_555 OE1 ? B GLU 259 ? A GLU 232 ? 1_555 80.2  ? 
18 OE2 ? B GLU 256 ? A GLU 229 ? 1_555 GD ? L GD3 . ? A GD3 601 ? 1_555 OE1 ? B GLU 259 ? A GLU 232 ? 1_555 89.3  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2016-06-22 
2 'Structure model' 1 1 2016-07-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0049 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALEPACK   ? ? ? .        2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.15     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-2000    ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .        5 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             VAL 
_pdbx_validate_rmsd_angle.auth_seq_id_1              537 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              538 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_3              538 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                151.00 
_pdbx_validate_rmsd_angle.angle_target_value         119.30 
_pdbx_validate_rmsd_angle.angle_deviation            31.70 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.50 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA B 46  ? ? -91.76  55.30   
2  1 ARG B 62  ? ? 70.44   96.85   
3  1 LEU B 88  ? ? 45.33   76.86   
4  1 GLN B 117 ? ? -68.74  -75.55  
5  1 ASN B 118 ? ? -21.15  -43.90  
6  1 THR B 145 ? ? -92.66  -63.70  
7  1 ALA B 168 ? ? -141.63 -8.47   
8  1 ASN B 207 ? ? -146.95 17.68   
9  1 ARG B 340 ? ? -93.09  -66.79  
10 1 LYS B 349 ? ? -56.27  -72.65  
11 1 ARG B 415 ? ? -118.13 -78.74  
12 1 ARG B 441 ? ? -100.20 43.03   
13 1 ASN B 472 ? ? -37.89  -34.90  
14 1 LYS B 517 ? ? -38.49  119.50  
15 1 ALA A 46  ? ? -86.56  41.56   
16 1 ARG A 62  ? ? 65.90   109.90  
17 1 LEU A 88  ? ? 50.47   80.22   
18 1 ALA A 144 ? ? -81.84  -159.37 
19 1 ALA A 168 ? ? -149.11 -6.11   
20 1 ASN A 207 ? ? -137.28 -38.99  
21 1 ASP A 215 ? ? -68.97  72.90   
22 1 ASP A 216 ? ? -162.79 -165.95 
23 1 ASN A 261 ? ? -67.34  7.15    
24 1 ARG A 340 ? ? -72.71  -77.22  
25 1 ARG A 415 ? ? -115.20 -76.90  
26 1 PHE A 444 ? ? -91.18  -154.91 
27 1 PHE A 533 ? ? -132.25 -36.05  
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 B LYS 29  ? CG  ? A LYS 56  CG  
2   1 Y 1 B LYS 29  ? CD  ? A LYS 56  CD  
3   1 Y 1 B LYS 29  ? CE  ? A LYS 56  CE  
4   1 Y 1 B LYS 29  ? NZ  ? A LYS 56  NZ  
5   1 Y 1 B LYS 47  ? CG  ? A LYS 74  CG  
6   1 Y 1 B LYS 47  ? CD  ? A LYS 74  CD  
7   1 Y 1 B LYS 47  ? CE  ? A LYS 74  CE  
8   1 Y 1 B LYS 47  ? NZ  ? A LYS 74  NZ  
9   1 Y 1 B ASP 48  ? CG  ? A ASP 75  CG  
10  1 Y 1 B ASP 48  ? OD1 ? A ASP 75  OD1 
11  1 Y 1 B ASP 48  ? OD2 ? A ASP 75  OD2 
12  1 Y 1 B GLU 56  ? CG  ? A GLU 83  CG  
13  1 Y 1 B GLU 56  ? CD  ? A GLU 83  CD  
14  1 Y 1 B GLU 56  ? OE1 ? A GLU 83  OE1 
15  1 Y 1 B GLU 56  ? OE2 ? A GLU 83  OE2 
16  1 Y 1 B VAL 58  ? CG1 ? A VAL 85  CG1 
17  1 Y 1 B VAL 58  ? CG2 ? A VAL 85  CG2 
18  1 Y 1 B GLU 59  ? CG  ? A GLU 86  CG  
19  1 Y 1 B GLU 59  ? CD  ? A GLU 86  CD  
20  1 Y 1 B GLU 59  ? OE1 ? A GLU 86  OE1 
21  1 Y 1 B GLU 59  ? OE2 ? A GLU 86  OE2 
22  1 Y 1 B ASN 90  ? CG  ? A ASN 117 CG  
23  1 Y 1 B ASN 90  ? OD1 ? A ASN 117 OD1 
24  1 Y 1 B ASN 90  ? ND2 ? A ASN 117 ND2 
25  1 Y 1 B ILE 120 ? CG1 ? A ILE 147 CG1 
26  1 Y 1 B ILE 120 ? CG2 ? A ILE 147 CG2 
27  1 Y 1 B ILE 120 ? CD1 ? A ILE 147 CD1 
28  1 Y 1 B GLU 231 ? CG  ? A GLU 258 CG  
29  1 Y 1 B GLU 231 ? CD  ? A GLU 258 CD  
30  1 Y 1 B GLU 231 ? OE1 ? A GLU 258 OE1 
31  1 Y 1 B GLU 231 ? OE2 ? A GLU 258 OE2 
32  1 Y 1 B GLU 249 ? CG  ? A GLU 276 CG  
33  1 Y 1 B GLU 249 ? CD  ? A GLU 276 CD  
34  1 Y 1 B GLU 249 ? OE1 ? A GLU 276 OE1 
35  1 Y 1 B GLU 249 ? OE2 ? A GLU 276 OE2 
36  1 Y 1 B GLU 250 ? CG  ? A GLU 277 CG  
37  1 Y 1 B GLU 250 ? CD  ? A GLU 277 CD  
38  1 Y 1 B GLU 250 ? OE1 ? A GLU 277 OE1 
39  1 Y 1 B GLU 250 ? OE2 ? A GLU 277 OE2 
40  1 Y 1 B GLN 253 ? CG  ? A GLN 280 CG  
41  1 Y 1 B GLN 253 ? CD  ? A GLN 280 CD  
42  1 Y 1 B GLN 253 ? OE1 ? A GLN 280 OE1 
43  1 Y 1 B GLN 253 ? NE2 ? A GLN 280 NE2 
44  1 Y 1 B GLU 332 ? CG  ? A GLU 359 CG  
45  1 Y 1 B GLU 332 ? CD  ? A GLU 359 CD  
46  1 Y 1 B GLU 332 ? OE1 ? A GLU 359 OE1 
47  1 Y 1 B GLU 332 ? OE2 ? A GLU 359 OE2 
48  1 Y 1 B ARG 340 ? CG  ? A ARG 367 CG  
49  1 Y 1 B ARG 340 ? CD  ? A ARG 367 CD  
50  1 Y 1 B ARG 340 ? NE  ? A ARG 367 NE  
51  1 Y 1 B ARG 340 ? CZ  ? A ARG 367 CZ  
52  1 Y 1 B ARG 340 ? NH1 ? A ARG 367 NH1 
53  1 Y 1 B ARG 340 ? NH2 ? A ARG 367 NH2 
54  1 Y 1 B LYS 341 ? CG  ? A LYS 368 CG  
55  1 Y 1 B LYS 341 ? CD  ? A LYS 368 CD  
56  1 Y 1 B LYS 341 ? CE  ? A LYS 368 CE  
57  1 Y 1 B LYS 341 ? NZ  ? A LYS 368 NZ  
58  1 Y 1 B VAL 343 ? CG1 ? A VAL 370 CG1 
59  1 Y 1 B VAL 343 ? CG2 ? A VAL 370 CG2 
60  1 Y 1 B LYS 349 ? CG  ? A LYS 376 CG  
61  1 Y 1 B LYS 349 ? CD  ? A LYS 376 CD  
62  1 Y 1 B LYS 349 ? CE  ? A LYS 376 CE  
63  1 Y 1 B LYS 349 ? NZ  ? A LYS 376 NZ  
64  1 Y 1 B GLN 361 ? CG  ? A GLN 388 CG  
65  1 Y 1 B GLN 361 ? CD  ? A GLN 388 CD  
66  1 Y 1 B GLN 361 ? OE1 ? A GLN 388 OE1 
67  1 Y 1 B GLN 361 ? NE2 ? A GLN 388 NE2 
68  1 Y 1 B LEU 394 ? CG  ? A LEU 421 CG  
69  1 Y 1 B LEU 394 ? CD1 ? A LEU 421 CD1 
70  1 Y 1 B LEU 394 ? CD2 ? A LEU 421 CD2 
71  1 Y 1 B SER 402 ? OG  ? A SER 429 OG  
72  1 Y 1 B GLU 405 ? CG  ? A GLU 432 CG  
73  1 Y 1 B GLU 405 ? CD  ? A GLU 432 CD  
74  1 Y 1 B GLU 405 ? OE1 ? A GLU 432 OE1 
75  1 Y 1 B GLU 405 ? OE2 ? A GLU 432 OE2 
76  1 Y 1 B ARG 441 ? CG  ? A ARG 468 CG  
77  1 Y 1 B ARG 441 ? CD  ? A ARG 468 CD  
78  1 Y 1 B ARG 441 ? NE  ? A ARG 468 NE  
79  1 Y 1 B ARG 441 ? CZ  ? A ARG 468 CZ  
80  1 Y 1 B ARG 441 ? NH1 ? A ARG 468 NH1 
81  1 Y 1 B ARG 441 ? NH2 ? A ARG 468 NH2 
82  1 Y 1 B LYS 454 ? CG  ? A LYS 481 CG  
83  1 Y 1 B LYS 454 ? CD  ? A LYS 481 CD  
84  1 Y 1 B LYS 454 ? CE  ? A LYS 481 CE  
85  1 Y 1 B LYS 454 ? NZ  ? A LYS 481 NZ  
86  1 Y 1 B GLU 481 ? CG  ? A GLU 508 CG  
87  1 Y 1 B GLU 481 ? CD  ? A GLU 508 CD  
88  1 Y 1 B GLU 481 ? OE1 ? A GLU 508 OE1 
89  1 Y 1 B GLU 481 ? OE2 ? A GLU 508 OE2 
90  1 Y 1 B GLU 499 ? CG  ? A GLU 526 CG  
91  1 Y 1 B GLU 499 ? CD  ? A GLU 526 CD  
92  1 Y 1 B GLU 499 ? OE1 ? A GLU 526 OE1 
93  1 Y 1 B GLU 499 ? OE2 ? A GLU 526 OE2 
94  1 Y 1 B LYS 516 ? CG  ? A LYS 543 CG  
95  1 Y 1 B LYS 516 ? CD  ? A LYS 543 CD  
96  1 Y 1 B LYS 516 ? CE  ? A LYS 543 CE  
97  1 Y 1 B LYS 516 ? NZ  ? A LYS 543 NZ  
98  1 Y 1 B LYS 517 ? CG  ? A LYS 544 CG  
99  1 Y 1 B LYS 517 ? CD  ? A LYS 544 CD  
100 1 Y 1 B LYS 517 ? CE  ? A LYS 544 CE  
101 1 Y 1 B LYS 517 ? NZ  ? A LYS 544 NZ  
102 1 Y 1 B GLU 519 ? CG  ? A GLU 546 CG  
103 1 Y 1 B GLU 519 ? CD  ? A GLU 546 CD  
104 1 Y 1 B GLU 519 ? OE1 ? A GLU 546 OE1 
105 1 Y 1 B GLU 519 ? OE2 ? A GLU 546 OE2 
106 1 Y 1 B LEU 529 ? CG  ? A LEU 556 CG  
107 1 Y 1 B LEU 529 ? CD1 ? A LEU 556 CD1 
108 1 Y 1 B LEU 529 ? CD2 ? A LEU 556 CD2 
109 1 Y 1 B PHE 533 ? CG  ? A PHE 560 CG  
110 1 Y 1 B PHE 533 ? CD1 ? A PHE 560 CD1 
111 1 Y 1 B PHE 533 ? CD2 ? A PHE 560 CD2 
112 1 Y 1 B PHE 533 ? CE1 ? A PHE 560 CE1 
113 1 Y 1 B PHE 533 ? CE2 ? A PHE 560 CE2 
114 1 Y 1 B PHE 533 ? CZ  ? A PHE 560 CZ  
115 1 Y 1 B SER 534 ? OG  ? A SER 561 OG  
116 1 Y 1 A PRO 22  ? CG  ? B PRO 49  CG  
117 1 Y 1 A PRO 22  ? CD  ? B PRO 49  CD  
118 1 Y 1 A LYS 28  ? CG  ? B LYS 55  CG  
119 1 Y 1 A LYS 28  ? CD  ? B LYS 55  CD  
120 1 Y 1 A LYS 28  ? CE  ? B LYS 55  CE  
121 1 Y 1 A LYS 28  ? NZ  ? B LYS 55  NZ  
122 1 Y 1 A LYS 29  ? CG  ? B LYS 56  CG  
123 1 Y 1 A LYS 29  ? CD  ? B LYS 56  CD  
124 1 Y 1 A LYS 29  ? CE  ? B LYS 56  CE  
125 1 Y 1 A LYS 29  ? NZ  ? B LYS 56  NZ  
126 1 Y 1 A LYS 47  ? CG  ? B LYS 74  CG  
127 1 Y 1 A LYS 47  ? CD  ? B LYS 74  CD  
128 1 Y 1 A LYS 47  ? CE  ? B LYS 74  CE  
129 1 Y 1 A LYS 47  ? NZ  ? B LYS 74  NZ  
130 1 Y 1 A ASP 48  ? CG  ? B ASP 75  CG  
131 1 Y 1 A ASP 48  ? OD1 ? B ASP 75  OD1 
132 1 Y 1 A ASP 48  ? OD2 ? B ASP 75  OD2 
133 1 Y 1 A GLU 56  ? CG  ? B GLU 83  CG  
134 1 Y 1 A GLU 56  ? CD  ? B GLU 83  CD  
135 1 Y 1 A GLU 56  ? OE1 ? B GLU 83  OE1 
136 1 Y 1 A GLU 56  ? OE2 ? B GLU 83  OE2 
137 1 Y 1 A VAL 58  ? CG1 ? B VAL 85  CG1 
138 1 Y 1 A VAL 58  ? CG2 ? B VAL 85  CG2 
139 1 Y 1 A GLU 59  ? CG  ? B GLU 86  CG  
140 1 Y 1 A GLU 59  ? CD  ? B GLU 86  CD  
141 1 Y 1 A GLU 59  ? OE1 ? B GLU 86  OE1 
142 1 Y 1 A GLU 59  ? OE2 ? B GLU 86  OE2 
143 1 Y 1 A ASN 90  ? CG  ? B ASN 117 CG  
144 1 Y 1 A ASN 90  ? OD1 ? B ASN 117 OD1 
145 1 Y 1 A ASN 90  ? ND2 ? B ASN 117 ND2 
146 1 Y 1 A ILE 120 ? CG1 ? B ILE 147 CG1 
147 1 Y 1 A ILE 120 ? CG2 ? B ILE 147 CG2 
148 1 Y 1 A ILE 120 ? CD1 ? B ILE 147 CD1 
149 1 Y 1 A ASN 207 ? CG  ? B ASN 234 CG  
150 1 Y 1 A ASN 207 ? OD1 ? B ASN 234 OD1 
151 1 Y 1 A ASN 207 ? ND2 ? B ASN 234 ND2 
152 1 Y 1 A GLU 231 ? CG  ? B GLU 258 CG  
153 1 Y 1 A GLU 231 ? CD  ? B GLU 258 CD  
154 1 Y 1 A GLU 231 ? OE1 ? B GLU 258 OE1 
155 1 Y 1 A GLU 231 ? OE2 ? B GLU 258 OE2 
156 1 Y 1 A GLU 249 ? CG  ? B GLU 276 CG  
157 1 Y 1 A GLU 249 ? CD  ? B GLU 276 CD  
158 1 Y 1 A GLU 249 ? OE1 ? B GLU 276 OE1 
159 1 Y 1 A GLU 249 ? OE2 ? B GLU 276 OE2 
160 1 Y 1 A GLU 250 ? CG  ? B GLU 277 CG  
161 1 Y 1 A GLU 250 ? CD  ? B GLU 277 CD  
162 1 Y 1 A GLU 250 ? OE1 ? B GLU 277 OE1 
163 1 Y 1 A GLU 250 ? OE2 ? B GLU 277 OE2 
164 1 Y 1 A GLN 253 ? CG  ? B GLN 280 CG  
165 1 Y 1 A GLN 253 ? CD  ? B GLN 280 CD  
166 1 Y 1 A GLN 253 ? OE1 ? B GLN 280 OE1 
167 1 Y 1 A GLN 253 ? NE2 ? B GLN 280 NE2 
168 1 Y 1 A LYS 265 ? CG  ? B LYS 292 CG  
169 1 Y 1 A LYS 265 ? CD  ? B LYS 292 CD  
170 1 Y 1 A LYS 265 ? CE  ? B LYS 292 CE  
171 1 Y 1 A LYS 265 ? NZ  ? B LYS 292 NZ  
172 1 Y 1 A LYS 323 ? CG  ? B LYS 350 CG  
173 1 Y 1 A LYS 323 ? CD  ? B LYS 350 CD  
174 1 Y 1 A LYS 323 ? CE  ? B LYS 350 CE  
175 1 Y 1 A LYS 323 ? NZ  ? B LYS 350 NZ  
176 1 Y 1 A GLU 332 ? CG  ? B GLU 359 CG  
177 1 Y 1 A GLU 332 ? CD  ? B GLU 359 CD  
178 1 Y 1 A GLU 332 ? OE1 ? B GLU 359 OE1 
179 1 Y 1 A GLU 332 ? OE2 ? B GLU 359 OE2 
180 1 Y 1 A LYS 336 ? CG  ? B LYS 363 CG  
181 1 Y 1 A LYS 336 ? CD  ? B LYS 363 CD  
182 1 Y 1 A LYS 336 ? CE  ? B LYS 363 CE  
183 1 Y 1 A LYS 336 ? NZ  ? B LYS 363 NZ  
184 1 Y 1 A ARG 340 ? CG  ? B ARG 367 CG  
185 1 Y 1 A ARG 340 ? CD  ? B ARG 367 CD  
186 1 Y 1 A ARG 340 ? NE  ? B ARG 367 NE  
187 1 Y 1 A ARG 340 ? CZ  ? B ARG 367 CZ  
188 1 Y 1 A ARG 340 ? NH1 ? B ARG 367 NH1 
189 1 Y 1 A ARG 340 ? NH2 ? B ARG 367 NH2 
190 1 Y 1 A LYS 341 ? CG  ? B LYS 368 CG  
191 1 Y 1 A LYS 341 ? CD  ? B LYS 368 CD  
192 1 Y 1 A LYS 341 ? CE  ? B LYS 368 CE  
193 1 Y 1 A LYS 341 ? NZ  ? B LYS 368 NZ  
194 1 Y 1 A VAL 343 ? CG1 ? B VAL 370 CG1 
195 1 Y 1 A VAL 343 ? CG2 ? B VAL 370 CG2 
196 1 Y 1 A LYS 349 ? CG  ? B LYS 376 CG  
197 1 Y 1 A LYS 349 ? CD  ? B LYS 376 CD  
198 1 Y 1 A LYS 349 ? CE  ? B LYS 376 CE  
199 1 Y 1 A LYS 349 ? NZ  ? B LYS 376 NZ  
200 1 Y 1 A GLN 361 ? CG  ? B GLN 388 CG  
201 1 Y 1 A GLN 361 ? CD  ? B GLN 388 CD  
202 1 Y 1 A GLN 361 ? OE1 ? B GLN 388 OE1 
203 1 Y 1 A GLN 361 ? NE2 ? B GLN 388 NE2 
204 1 Y 1 A ARG 392 ? CG  ? B ARG 419 CG  
205 1 Y 1 A ARG 392 ? CD  ? B ARG 419 CD  
206 1 Y 1 A ARG 392 ? NE  ? B ARG 419 NE  
207 1 Y 1 A ARG 392 ? CZ  ? B ARG 419 CZ  
208 1 Y 1 A ARG 392 ? NH1 ? B ARG 419 NH1 
209 1 Y 1 A ARG 392 ? NH2 ? B ARG 419 NH2 
210 1 Y 1 A LEU 394 ? CG  ? B LEU 421 CG  
211 1 Y 1 A LEU 394 ? CD1 ? B LEU 421 CD1 
212 1 Y 1 A LEU 394 ? CD2 ? B LEU 421 CD2 
213 1 Y 1 A SER 402 ? OG  ? B SER 429 OG  
214 1 Y 1 A GLU 405 ? CG  ? B GLU 432 CG  
215 1 Y 1 A GLU 405 ? CD  ? B GLU 432 CD  
216 1 Y 1 A GLU 405 ? OE1 ? B GLU 432 OE1 
217 1 Y 1 A GLU 405 ? OE2 ? B GLU 432 OE2 
218 1 Y 1 A ARG 441 ? CG  ? B ARG 468 CG  
219 1 Y 1 A ARG 441 ? CD  ? B ARG 468 CD  
220 1 Y 1 A ARG 441 ? NE  ? B ARG 468 NE  
221 1 Y 1 A ARG 441 ? CZ  ? B ARG 468 CZ  
222 1 Y 1 A ARG 441 ? NH1 ? B ARG 468 NH1 
223 1 Y 1 A ARG 441 ? NH2 ? B ARG 468 NH2 
224 1 Y 1 A LYS 453 ? CG  ? B LYS 480 CG  
225 1 Y 1 A LYS 453 ? CD  ? B LYS 480 CD  
226 1 Y 1 A LYS 453 ? CE  ? B LYS 480 CE  
227 1 Y 1 A LYS 453 ? NZ  ? B LYS 480 NZ  
228 1 Y 1 A LYS 454 ? CG  ? B LYS 481 CG  
229 1 Y 1 A LYS 454 ? CD  ? B LYS 481 CD  
230 1 Y 1 A LYS 454 ? CE  ? B LYS 481 CE  
231 1 Y 1 A LYS 454 ? NZ  ? B LYS 481 NZ  
232 1 Y 1 A GLU 481 ? CG  ? B GLU 508 CG  
233 1 Y 1 A GLU 481 ? CD  ? B GLU 508 CD  
234 1 Y 1 A GLU 481 ? OE1 ? B GLU 508 OE1 
235 1 Y 1 A GLU 481 ? OE2 ? B GLU 508 OE2 
236 1 Y 1 A GLU 499 ? CG  ? B GLU 526 CG  
237 1 Y 1 A GLU 499 ? CD  ? B GLU 526 CD  
238 1 Y 1 A GLU 499 ? OE1 ? B GLU 526 OE1 
239 1 Y 1 A GLU 499 ? OE2 ? B GLU 526 OE2 
240 1 Y 1 A LYS 516 ? CG  ? B LYS 543 CG  
241 1 Y 1 A LYS 516 ? CD  ? B LYS 543 CD  
242 1 Y 1 A LYS 516 ? CE  ? B LYS 543 CE  
243 1 Y 1 A LYS 516 ? NZ  ? B LYS 543 NZ  
244 1 Y 1 A LYS 517 ? CG  ? B LYS 544 CG  
245 1 Y 1 A LYS 517 ? CD  ? B LYS 544 CD  
246 1 Y 1 A LYS 517 ? CE  ? B LYS 544 CE  
247 1 Y 1 A LYS 517 ? NZ  ? B LYS 544 NZ  
248 1 Y 1 A GLU 519 ? CG  ? B GLU 546 CG  
249 1 Y 1 A GLU 519 ? CD  ? B GLU 546 CD  
250 1 Y 1 A GLU 519 ? OE1 ? B GLU 546 OE1 
251 1 Y 1 A GLU 519 ? OE2 ? B GLU 546 OE2 
252 1 Y 1 A GLU 526 ? CG  ? B GLU 553 CG  
253 1 Y 1 A GLU 526 ? CD  ? B GLU 553 CD  
254 1 Y 1 A GLU 526 ? OE1 ? B GLU 553 OE1 
255 1 Y 1 A GLU 526 ? OE2 ? B GLU 553 OE2 
256 1 Y 1 A LYS 527 ? CG  ? B LYS 554 CG  
257 1 Y 1 A LYS 527 ? CD  ? B LYS 554 CD  
258 1 Y 1 A LYS 527 ? CE  ? B LYS 554 CE  
259 1 Y 1 A LYS 527 ? NZ  ? B LYS 554 NZ  
260 1 Y 1 A ARG 535 ? CG  ? B ARG 562 CG  
261 1 Y 1 A ARG 535 ? CD  ? B ARG 562 CD  
262 1 Y 1 A ARG 535 ? NE  ? B ARG 562 NE  
263 1 Y 1 A ARG 535 ? CZ  ? B ARG 562 CZ  
264 1 Y 1 A ARG 535 ? NH1 ? B ARG 562 NH1 
265 1 Y 1 A ARG 535 ? NH2 ? B ARG 562 NH2 
266 1 Y 1 A GLU 536 ? CG  ? B GLU 563 CG  
267 1 Y 1 A GLU 536 ? CD  ? B GLU 563 CD  
268 1 Y 1 A GLU 536 ? OE1 ? B GLU 563 OE1 
269 1 Y 1 A GLU 536 ? OE2 ? B GLU 563 OE2 
270 1 Y 1 A VAL 537 ? CG1 ? B VAL 564 CG1 
271 1 Y 1 A VAL 537 ? CG2 ? B VAL 564 CG2 
272 1 Y 1 A PRO 538 ? CG  ? B PRO 565 CG  
273 1 Y 1 A PRO 538 ? CD  ? B PRO 565 CD  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 B MET -26 ? A MET 1   
2   1 Y 1 B ARG -25 ? A ARG 2   
3   1 Y 1 B LEU -24 ? A LEU 3   
4   1 Y 1 B LEU -23 ? A LEU 4   
5   1 Y 1 B THR -22 ? A THR 5   
6   1 Y 1 B ALA -21 ? A ALA 6   
7   1 Y 1 B LEU -20 ? A LEU 7   
8   1 Y 1 B PHE -19 ? A PHE 8   
9   1 Y 1 B ALA -18 ? A ALA 9   
10  1 Y 1 B TYR -17 ? A TYR 10  
11  1 Y 1 B PHE -16 ? A PHE 11  
12  1 Y 1 B ILE -15 ? A ILE 12  
13  1 Y 1 B VAL -14 ? A VAL 13  
14  1 Y 1 B ALA -13 ? A ALA 14  
15  1 Y 1 B LEU -12 ? A LEU 15  
16  1 Y 1 B ILE -11 ? A ILE 16  
17  1 Y 1 B LEU -10 ? A LEU 17  
18  1 Y 1 B ALA -9  ? A ALA 18  
19  1 Y 1 B PHE -8  ? A PHE 19  
20  1 Y 1 B SER -7  ? A SER 20  
21  1 Y 1 B VAL -6  ? A VAL 21  
22  1 Y 1 B SER -5  ? A SER 22  
23  1 Y 1 B ALA -4  ? A ALA 23  
24  1 Y 1 B LYS -3  ? A LYS 24  
25  1 Y 1 B SER -2  ? A SER 25  
26  1 Y 1 B MET -1  ? A MET 26  
27  1 Y 1 B HIS 0   ? A HIS 27  
28  1 Y 1 B HIS 1   ? A HIS 28  
29  1 Y 1 B HIS 2   ? A HIS 29  
30  1 Y 1 B HIS 3   ? A HIS 30  
31  1 Y 1 B HIS 4   ? A HIS 31  
32  1 Y 1 B HIS 5   ? A HIS 32  
33  1 Y 1 B HIS 6   ? A HIS 33  
34  1 Y 1 B HIS 7   ? A HIS 34  
35  1 Y 1 B SER 8   ? A SER 35  
36  1 Y 1 B ALA 9   ? A ALA 36  
37  1 Y 1 B TRP 10  ? A TRP 37  
38  1 Y 1 B SER 11  ? A SER 38  
39  1 Y 1 B HIS 12  ? A HIS 39  
40  1 Y 1 B PRO 13  ? A PRO 40  
41  1 Y 1 B GLN 14  ? A GLN 41  
42  1 Y 1 B PHE 15  ? A PHE 42  
43  1 Y 1 B GLU 16  ? A GLU 43  
44  1 Y 1 B LYS 17  ? A LYS 44  
45  1 Y 1 B GLU 18  ? A GLU 45  
46  1 Y 1 B PHE 19  ? A PHE 46  
47  1 Y 1 B TYR 20  ? A TYR 47  
48  1 Y 1 B SER 122 ? A SER 149 
49  1 Y 1 B LEU 123 ? A LEU 150 
50  1 Y 1 B ASN 124 ? A ASN 151 
51  1 Y 1 B LEU 125 ? A LEU 152 
52  1 Y 1 B ASP 126 ? A ASP 153 
53  1 Y 1 B GLU 127 ? A GLU 154 
54  1 Y 1 B PHE 128 ? A PHE 155 
55  1 Y 1 B CYS 129 ? A CYS 156 
56  1 Y 1 B ASN 130 ? A ASN 157 
57  1 Y 1 B CYS 131 ? A CYS 158 
58  1 Y 1 B SER 132 ? A SER 159 
59  1 Y 1 B GLU 133 ? A GLU 160 
60  1 Y 1 B HIS 134 ? A HIS 161 
61  1 Y 1 B ILE 135 ? A ILE 162 
62  1 Y 1 B PRO 136 ? A PRO 163 
63  1 Y 1 B GLU 362 ? A GLU 389 
64  1 Y 1 B GLY 363 ? A GLY 390 
65  1 Y 1 B ALA 364 ? A ALA 391 
66  1 Y 1 B LYS 365 ? A LYS 392 
67  1 Y 1 B GLY 366 ? A GLY 393 
68  1 Y 1 B PRO 367 ? A PRO 394 
69  1 Y 1 B LEU 368 ? A LEU 395 
70  1 Y 1 B PRO 369 ? A PRO 396 
71  1 Y 1 B VAL 370 ? A VAL 397 
72  1 Y 1 B ASP 371 ? A ASP 398 
73  1 Y 1 B THR 372 ? A THR 399 
74  1 Y 1 B PHE 373 ? A PHE 400 
75  1 Y 1 B LEU 374 ? A LEU 401 
76  1 Y 1 B ARG 375 ? A ARG 402 
77  1 Y 1 B GLY 376 ? A GLY 403 
78  1 Y 1 B HIS 377 ? A HIS 404 
79  1 Y 1 B GLU 378 ? A GLU 405 
80  1 Y 1 B GLU 379 ? A GLU 406 
81  1 Y 1 B SER 380 ? A SER 407 
82  1 Y 1 B GLY 381 ? A GLY 408 
83  1 Y 1 B ASP 382 ? A ASP 409 
84  1 Y 1 B ARG 383 ? A ARG 410 
85  1 Y 1 B PHE 384 ? A PHE 411 
86  1 Y 1 B SER 385 ? A SER 412 
87  1 Y 1 B ASN 386 ? A ASN 413 
88  1 Y 1 B SER 387 ? A SER 414 
89  1 Y 1 B SER 388 ? A SER 415 
90  1 Y 1 B THR 389 ? A THR 416 
91  1 Y 1 B ALA 390 ? A ALA 417 
92  1 Y 1 B ARG 535 ? A ARG 562 
93  1 Y 1 B GLU 536 ? A GLU 563 
94  1 Y 1 B VAL 537 ? A VAL 564 
95  1 Y 1 B PRO 538 ? A PRO 565 
96  1 Y 1 B PHE 539 ? A PHE 566 
97  1 Y 1 B SER 540 ? A SER 567 
98  1 Y 1 B ASN 541 ? A ASN 568 
99  1 Y 1 A MET -26 ? B MET 1   
100 1 Y 1 A ARG -25 ? B ARG 2   
101 1 Y 1 A LEU -24 ? B LEU 3   
102 1 Y 1 A LEU -23 ? B LEU 4   
103 1 Y 1 A THR -22 ? B THR 5   
104 1 Y 1 A ALA -21 ? B ALA 6   
105 1 Y 1 A LEU -20 ? B LEU 7   
106 1 Y 1 A PHE -19 ? B PHE 8   
107 1 Y 1 A ALA -18 ? B ALA 9   
108 1 Y 1 A TYR -17 ? B TYR 10  
109 1 Y 1 A PHE -16 ? B PHE 11  
110 1 Y 1 A ILE -15 ? B ILE 12  
111 1 Y 1 A VAL -14 ? B VAL 13  
112 1 Y 1 A ALA -13 ? B ALA 14  
113 1 Y 1 A LEU -12 ? B LEU 15  
114 1 Y 1 A ILE -11 ? B ILE 16  
115 1 Y 1 A LEU -10 ? B LEU 17  
116 1 Y 1 A ALA -9  ? B ALA 18  
117 1 Y 1 A PHE -8  ? B PHE 19  
118 1 Y 1 A SER -7  ? B SER 20  
119 1 Y 1 A VAL -6  ? B VAL 21  
120 1 Y 1 A SER -5  ? B SER 22  
121 1 Y 1 A ALA -4  ? B ALA 23  
122 1 Y 1 A LYS -3  ? B LYS 24  
123 1 Y 1 A SER -2  ? B SER 25  
124 1 Y 1 A MET -1  ? B MET 26  
125 1 Y 1 A HIS 0   ? B HIS 27  
126 1 Y 1 A HIS 1   ? B HIS 28  
127 1 Y 1 A HIS 2   ? B HIS 29  
128 1 Y 1 A HIS 3   ? B HIS 30  
129 1 Y 1 A HIS 4   ? B HIS 31  
130 1 Y 1 A HIS 5   ? B HIS 32  
131 1 Y 1 A HIS 6   ? B HIS 33  
132 1 Y 1 A HIS 7   ? B HIS 34  
133 1 Y 1 A SER 8   ? B SER 35  
134 1 Y 1 A ALA 9   ? B ALA 36  
135 1 Y 1 A TRP 10  ? B TRP 37  
136 1 Y 1 A SER 11  ? B SER 38  
137 1 Y 1 A HIS 12  ? B HIS 39  
138 1 Y 1 A PRO 13  ? B PRO 40  
139 1 Y 1 A GLN 14  ? B GLN 41  
140 1 Y 1 A PHE 15  ? B PHE 42  
141 1 Y 1 A GLU 16  ? B GLU 43  
142 1 Y 1 A LYS 17  ? B LYS 44  
143 1 Y 1 A GLU 18  ? B GLU 45  
144 1 Y 1 A PHE 19  ? B PHE 46  
145 1 Y 1 A TYR 20  ? B TYR 47  
146 1 Y 1 A GLY 21  ? B GLY 48  
147 1 Y 1 A SER 122 ? B SER 149 
148 1 Y 1 A LEU 123 ? B LEU 150 
149 1 Y 1 A ASN 124 ? B ASN 151 
150 1 Y 1 A LEU 125 ? B LEU 152 
151 1 Y 1 A ASP 126 ? B ASP 153 
152 1 Y 1 A GLU 127 ? B GLU 154 
153 1 Y 1 A PHE 128 ? B PHE 155 
154 1 Y 1 A CYS 129 ? B CYS 156 
155 1 Y 1 A ASN 130 ? B ASN 157 
156 1 Y 1 A CYS 131 ? B CYS 158 
157 1 Y 1 A SER 132 ? B SER 159 
158 1 Y 1 A GLU 133 ? B GLU 160 
159 1 Y 1 A HIS 134 ? B HIS 161 
160 1 Y 1 A ILE 135 ? B ILE 162 
161 1 Y 1 A PRO 136 ? B PRO 163 
162 1 Y 1 A GLU 362 ? B GLU 389 
163 1 Y 1 A GLY 363 ? B GLY 390 
164 1 Y 1 A ALA 364 ? B ALA 391 
165 1 Y 1 A LYS 365 ? B LYS 392 
166 1 Y 1 A GLY 366 ? B GLY 393 
167 1 Y 1 A PRO 367 ? B PRO 394 
168 1 Y 1 A LEU 368 ? B LEU 395 
169 1 Y 1 A PRO 369 ? B PRO 396 
170 1 Y 1 A VAL 370 ? B VAL 397 
171 1 Y 1 A ASP 371 ? B ASP 398 
172 1 Y 1 A THR 372 ? B THR 399 
173 1 Y 1 A PHE 373 ? B PHE 400 
174 1 Y 1 A LEU 374 ? B LEU 401 
175 1 Y 1 A ARG 375 ? B ARG 402 
176 1 Y 1 A GLY 376 ? B GLY 403 
177 1 Y 1 A HIS 377 ? B HIS 404 
178 1 Y 1 A GLU 378 ? B GLU 405 
179 1 Y 1 A GLU 379 ? B GLU 406 
180 1 Y 1 A SER 380 ? B SER 407 
181 1 Y 1 A GLY 381 ? B GLY 408 
182 1 Y 1 A ASP 382 ? B ASP 409 
183 1 Y 1 A ARG 383 ? B ARG 410 
184 1 Y 1 A PHE 384 ? B PHE 411 
185 1 Y 1 A SER 385 ? B SER 412 
186 1 Y 1 A ASN 386 ? B ASN 413 
187 1 Y 1 A SER 387 ? B SER 414 
188 1 Y 1 A SER 388 ? B SER 415 
189 1 Y 1 A THR 389 ? B THR 416 
190 1 Y 1 A ALA 390 ? B ALA 417 
191 1 Y 1 A PHE 391 ? B PHE 418 
192 1 Y 1 A PHE 539 ? B PHE 566 
193 1 Y 1 A SER 540 ? B SER 567 
194 1 Y 1 A ASN 541 ? B ASN 568 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'GADOLINIUM ION'       GD3 
3 'MAGNESIUM ION'        MG  
4 'BICARBONATE ION'      BCT 
5 'CHLORIDE ION'         CL  
6 N-ACETYL-D-GLUCOSAMINE NAG 
7 CYCLOMETHYLTRYPTOPHAN  TCR 
8 water                  HOH 
# 
