PDBx/mmCIF: 5nppDownload

data_5NPP
# 
_entry.id   5NPP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.282 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5NPP         
WWPDB D_1200004502 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5NPP 
_pdbx_database_status.recvd_initial_deposition_date   2017-04-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bax, B.D.'       1 ? 
'Chan, P.F.'      2 ? 
'Stavenger, R.A.' 3 ? 
# 
_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            'Proc. Natl. Acad. Sci. U.S.A.' 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            114 
_citation.language                  ? 
_citation.page_first                E4492 
_citation.page_last                 E4500 
_citation.title                     
'Thiophene antibacterials that allosterically stabilize DNA-cleavage complexes with DNA gyrase.' 
_citation.year                      2017 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.1700721114 
_citation.pdbx_database_id_PubMed   28507124 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Chan, P.F.'         1  
primary 'Germe, T.'          2  
primary 'Bax, B.D.'          3  
primary 'Huang, J.'          4  
primary 'Thalji, R.K.'       5  
primary 'Bacque, E.'         6  
primary 'Checchia, A.'       7  
primary 'Chen, D.'           8  
primary 'Cui, H.'            9  
primary 'Ding, X.'           10 
primary 'Ingraham, K.'       11 
primary 'McCloskey, L.'      12 
primary 'Raha, K.'           13 
primary 'Srikannathasan, V.' 14 
primary 'Maxwell, A.'        15 
primary 'Stavenger, R.A.'    16 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5NPP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     92.850 
_cell.length_a_esd                 ? 
_cell.length_b                     92.850 
_cell.length_b_esd                 ? 
_cell.length_c                     409.980 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         5NPP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                169 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 61' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
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 'DNA gyrase subunit B,DNA gyrase subunit B,DNA gyrase subunit A' 78125.000 2   5.99.1.3,5.99.1.3,5.99.1.3 ? ? ? 
2  polymer     syn 
;DNA (5'-D(*AP*GP*CP*CP*GP*TP*AP*GP*GP*TP*AP*CP*CP*TP*AP*CP*GP*GP*CP*T)-3')
;
2451.630  2   ?                          ? ? ? 
3  polymer     syn 
;DNA (5'-D(*AP*GP*CP*CP*GP*TP*AP*GP*GP*TP*AP*CP*CP*TP*AP*CP*GP*GP*CP*T)-3')
;
3638.379  2   ?                          ? ? ? 
4  non-polymer syn 'MANGANESE (II) ION' 54.938    2   ?                          ? ? ? 
5  non-polymer syn '~{N}-[(1~{R})-2-azanyl-1-phenyl-ethyl]-5-(2-chlorophenyl)-2-methyl-thiophene-3-carboxamide' 370.896   2   ? ? 
? ? 
6  non-polymer syn GLYCEROL 92.094    9   ?                          ? ? ? 
7  non-polymer syn 'SODIUM ION' 22.990    1   ?                          ? ? ? 
8  non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    1   ?                          ? ? ? 
9  non-polymer syn 
;(1R)-1-[(4-{[(6,7-dihydro[1,4]dioxino[2,3-c]pyridazin-3-yl)methyl]amino}piperidin-1-yl)methyl]-9-fluoro-1,2-dihydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
;
451.493   1   ?                          ? ? ? 
10 water       nat water 18.015    843 ?                          ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)'        no no 
;MDVASLPGKLADCSSKSPEECEIFLVEGDSAGGSTKSGRDSRTQAILPLRGKILNVEKARLDRILNNNEIRQMITAFGTG
IGGDFDLAKARYHKIVIMTDADVDGAHIRTLLLTFFYRFMRPLIEAGYVYIAQPPTGYKGLGEMNADQLWETTMNPEHRA
LLQVKLEDAIEADQTFEMLMGDVVENRRQFIEDNAVYANLDFAELPQSRINERNITSEMRESFLDYAMSVIVARALPDVR
DGLKPVHRRILYGLNEQGMTPDKSYKKSARIVGDVMGKYHPHGDSSIYEAMVRMAQDFSYRYPLVDGQGNFGSMDGDGAA
AMRYTEARMTKITLELLRDINKDTIDFIDNYDGNEREPSVLPARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLS
KNPDISIAELMEDIEGPDFPTAGLILGKSGIRRAYETGRGSIQMRSRAVIEERGGGRQRIVVTEIPFQVNKARMIEKIAE
LVRDKKIDGITDLRDETSLRTGVRVVIDVRKDANASVILNNLYKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEHQ
KTVVRRRTQYNLRKAKDRAHILEGLRIALDHIDEIISTIRESDTDKVAMESLQQRFKLSEKQAQAILDMRLRRLTGLERD
KIEAEYNELLNYISELETILADEEVLLQLVRDELTEIRDRFGDDRRTEIQLG
;
;MDVASLPGKLADCSSKSPEECEIFLVEGDSAGGSTKSGRDSRTQAILPLRGKILNVEKARLDRILNNNEIRQMITAFGTG
IGGDFDLAKARYHKIVIMTDADVDGAHIRTLLLTFFYRFMRPLIEAGYVYIAQPPTGYKGLGEMNADQLWETTMNPEHRA
LLQVKLEDAIEADQTFEMLMGDVVENRRQFIEDNAVYANLDFAELPQSRINERNITSEMRESFLDYAMSVIVARALPDVR
DGLKPVHRRILYGLNEQGMTPDKSYKKSARIVGDVMGKYHPHGDSSIYEAMVRMAQDFSYRYPLVDGQGNFGSMDGDGAA
AMRYTEARMTKITLELLRDINKDTIDFIDNYDGNEREPSVLPARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLS
KNPDISIAELMEDIEGPDFPTAGLILGKSGIRRAYETGRGSIQMRSRAVIEERGGGRQRIVVTEIPFQVNKARMIEKIAE
LVRDKKIDGITDLRDETSLRTGVRVVIDVRKDANASVILNNLYKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEHQ
KTVVRRRTQYNLRKAKDRAHILEGLRIALDHIDEIISTIRESDTDKVAMESLQQRFKLSEKQAQAILDMRLRRLTGLERD
KIEAEYNELLNYISELETILADEEVLLQLVRDELTEIRDRFGDDRRTEIQLG
;
B,D ? 
2 polydeoxyribonucleotide no no '(DA)(DG)(DC)(DC)(DG)(DT)(DA)(DG)' AGCCGTAG E,F ? 
3 polydeoxyribonucleotide no no '(DG)(DT)(DA)(DC)(DC)(DT)(DA)(DC)(DG)(DG)(DC)(DT)' GTACCTACGGCT A,C ? 
# 
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   ASP n 
1 3   VAL n 
1 4   ALA n 
1 5   SER n 
1 6   LEU n 
1 7   PRO n 
1 8   GLY n 
1 9   LYS n 
1 10  LEU n 
1 11  ALA n 
1 12  ASP n 
1 13  CYS n 
1 14  SER n 
1 15  SER n 
1 16  LYS n 
1 17  SER n 
1 18  PRO n 
1 19  GLU n 
1 20  GLU n 
1 21  CYS n 
1 22  GLU n 
1 23  ILE n 
1 24  PHE n 
1 25  LEU n 
1 26  VAL n 
1 27  GLU n 
1 28  GLY n 
1 29  ASP n 
1 30  SER n 
1 31  ALA n 
1 32  GLY n 
1 33  GLY n 
1 34  SER n 
1 35  THR n 
1 36  LYS n 
1 37  SER n 
1 38  GLY n 
1 39  ARG n 
1 40  ASP n 
1 41  SER n 
1 42  ARG n 
1 43  THR n 
1 44  GLN n 
1 45  ALA n 
1 46  ILE n 
1 47  LEU n 
1 48  PRO n 
1 49  LEU n 
1 50  ARG n 
1 51  GLY n 
1 52  LYS n 
1 53  ILE n 
1 54  LEU n 
1 55  ASN n 
1 56  VAL n 
1 57  GLU n 
1 58  LYS n 
1 59  ALA n 
1 60  ARG n 
1 61  LEU n 
1 62  ASP n 
1 63  ARG n 
1 64  ILE n 
1 65  LEU n 
1 66  ASN n 
1 67  ASN n 
1 68  ASN n 
1 69  GLU n 
1 70  ILE n 
1 71  ARG n 
1 72  GLN n 
1 73  MET n 
1 74  ILE n 
1 75  THR n 
1 76  ALA n 
1 77  PHE n 
1 78  GLY n 
1 79  THR n 
1 80  GLY n 
1 81  ILE n 
1 82  GLY n 
1 83  GLY n 
1 84  ASP n 
1 85  PHE n 
1 86  ASP n 
1 87  LEU n 
1 88  ALA n 
1 89  LYS n 
1 90  ALA n 
1 91  ARG n 
1 92  TYR n 
1 93  HIS n 
1 94  LYS n 
1 95  ILE n 
1 96  VAL n 
1 97  ILE n 
1 98  MET n 
1 99  THR n 
1 100 ASP n 
1 101 ALA n 
1 102 ASP n 
1 103 VAL n 
1 104 ASP n 
1 105 GLY n 
1 106 ALA n 
1 107 HIS n 
1 108 ILE n 
1 109 ARG n 
1 110 THR n 
1 111 LEU n 
1 112 LEU n 
1 113 LEU n 
1 114 THR n 
1 115 PHE n 
1 116 PHE n 
1 117 TYR n 
1 118 ARG n 
1 119 PHE n 
1 120 MET n 
1 121 ARG n 
1 122 PRO n 
1 123 LEU n 
1 124 ILE n 
1 125 GLU n 
1 126 ALA n 
1 127 GLY n 
1 128 TYR n 
1 129 VAL n 
1 130 TYR n 
1 131 ILE n 
1 132 ALA n 
1 133 GLN n 
1 134 PRO n 
1 135 PRO n 
1 136 THR n 
1 137 GLY n 
1 138 TYR n 
1 139 LYS n 
1 140 GLY n 
1 141 LEU n 
1 142 GLY n 
1 143 GLU n 
1 144 MET n 
1 145 ASN n 
1 146 ALA n 
1 147 ASP n 
1 148 GLN n 
1 149 LEU n 
1 150 TRP n 
1 151 GLU n 
1 152 THR n 
1 153 THR n 
1 154 MET n 
1 155 ASN n 
1 156 PRO n 
1 157 GLU n 
1 158 HIS n 
1 159 ARG n 
1 160 ALA n 
1 161 LEU n 
1 162 LEU n 
1 163 GLN n 
1 164 VAL n 
1 165 LYS n 
1 166 LEU n 
1 167 GLU n 
1 168 ASP n 
1 169 ALA n 
1 170 ILE n 
1 171 GLU n 
1 172 ALA n 
1 173 ASP n 
1 174 GLN n 
1 175 THR n 
1 176 PHE n 
1 177 GLU n 
1 178 MET n 
1 179 LEU n 
1 180 MET n 
1 181 GLY n 
1 182 ASP n 
1 183 VAL n 
1 184 VAL n 
1 185 GLU n 
1 186 ASN n 
1 187 ARG n 
1 188 ARG n 
1 189 GLN n 
1 190 PHE n 
1 191 ILE n 
1 192 GLU n 
1 193 ASP n 
1 194 ASN n 
1 195 ALA n 
1 196 VAL n 
1 197 TYR n 
1 198 ALA n 
1 199 ASN n 
1 200 LEU n 
1 201 ASP n 
1 202 PHE n 
1 203 ALA n 
1 204 GLU n 
1 205 LEU n 
1 206 PRO n 
1 207 GLN n 
1 208 SER n 
1 209 ARG n 
1 210 ILE n 
1 211 ASN n 
1 212 GLU n 
1 213 ARG n 
1 214 ASN n 
1 215 ILE n 
1 216 THR n 
1 217 SER n 
1 218 GLU n 
1 219 MET n 
1 220 ARG n 
1 221 GLU n 
1 222 SER n 
1 223 PHE n 
1 224 LEU n 
1 225 ASP n 
1 226 TYR n 
1 227 ALA n 
1 228 MET n 
1 229 SER n 
1 230 VAL n 
1 231 ILE n 
1 232 VAL n 
1 233 ALA n 
1 234 ARG n 
1 235 ALA n 
1 236 LEU n 
1 237 PRO n 
1 238 ASP n 
1 239 VAL n 
1 240 ARG n 
1 241 ASP n 
1 242 GLY n 
1 243 LEU n 
1 244 LYS n 
1 245 PRO n 
1 246 VAL n 
1 247 HIS n 
1 248 ARG n 
1 249 ARG n 
1 250 ILE n 
1 251 LEU n 
1 252 TYR n 
1 253 GLY n 
1 254 LEU n 
1 255 ASN n 
1 256 GLU n 
1 257 GLN n 
1 258 GLY n 
1 259 MET n 
1 260 THR n 
1 261 PRO n 
1 262 ASP n 
1 263 LYS n 
1 264 SER n 
1 265 TYR n 
1 266 LYS n 
1 267 LYS n 
1 268 SER n 
1 269 ALA n 
1 270 ARG n 
1 271 ILE n 
1 272 VAL n 
1 273 GLY n 
1 274 ASP n 
1 275 VAL n 
1 276 MET n 
1 277 GLY n 
1 278 LYS n 
1 279 TYR n 
1 280 HIS n 
1 281 PRO n 
1 282 HIS n 
1 283 GLY n 
1 284 ASP n 
1 285 SER n 
1 286 SER n 
1 287 ILE n 
1 288 TYR n 
1 289 GLU n 
1 290 ALA n 
1 291 MET n 
1 292 VAL n 
1 293 ARG n 
1 294 MET n 
1 295 ALA n 
1 296 GLN n 
1 297 ASP n 
1 298 PHE n 
1 299 SER n 
1 300 TYR n 
1 301 ARG n 
1 302 TYR n 
1 303 PRO n 
1 304 LEU n 
1 305 VAL n 
1 306 ASP n 
1 307 GLY n 
1 308 GLN n 
1 309 GLY n 
1 310 ASN n 
1 311 PHE n 
1 312 GLY n 
1 313 SER n 
1 314 MET n 
1 315 ASP n 
1 316 GLY n 
1 317 ASP n 
1 318 GLY n 
1 319 ALA n 
1 320 ALA n 
1 321 ALA n 
1 322 MET n 
1 323 ARG n 
1 324 TYR n 
1 325 THR n 
1 326 GLU n 
1 327 ALA n 
1 328 ARG n 
1 329 MET n 
1 330 THR n 
1 331 LYS n 
1 332 ILE n 
1 333 THR n 
1 334 LEU n 
1 335 GLU n 
1 336 LEU n 
1 337 LEU n 
1 338 ARG n 
1 339 ASP n 
1 340 ILE n 
1 341 ASN n 
1 342 LYS n 
1 343 ASP n 
1 344 THR n 
1 345 ILE n 
1 346 ASP n 
1 347 PHE n 
1 348 ILE n 
1 349 ASP n 
1 350 ASN n 
1 351 TYR n 
1 352 ASP n 
1 353 GLY n 
1 354 ASN n 
1 355 GLU n 
1 356 ARG n 
1 357 GLU n 
1 358 PRO n 
1 359 SER n 
1 360 VAL n 
1 361 LEU n 
1 362 PRO n 
1 363 ALA n 
1 364 ARG n 
1 365 PHE n 
1 366 PRO n 
1 367 ASN n 
1 368 LEU n 
1 369 LEU n 
1 370 ALA n 
1 371 ASN n 
1 372 GLY n 
1 373 ALA n 
1 374 SER n 
1 375 GLY n 
1 376 ILE n 
1 377 ALA n 
1 378 VAL n 
1 379 GLY n 
1 380 MET n 
1 381 ALA n 
1 382 THR n 
1 383 ASN n 
1 384 ILE n 
1 385 PRO n 
1 386 PRO n 
1 387 HIS n 
1 388 ASN n 
1 389 LEU n 
1 390 THR n 
1 391 GLU n 
1 392 LEU n 
1 393 ILE n 
1 394 ASN n 
1 395 GLY n 
1 396 VAL n 
1 397 LEU n 
1 398 SER n 
1 399 LEU n 
1 400 SER n 
1 401 LYS n 
1 402 ASN n 
1 403 PRO n 
1 404 ASP n 
1 405 ILE n 
1 406 SER n 
1 407 ILE n 
1 408 ALA n 
1 409 GLU n 
1 410 LEU n 
1 411 MET n 
1 412 GLU n 
1 413 ASP n 
1 414 ILE n 
1 415 GLU n 
1 416 GLY n 
1 417 PRO n 
1 418 ASP n 
1 419 PHE n 
1 420 PRO n 
1 421 THR n 
1 422 ALA n 
1 423 GLY n 
1 424 LEU n 
1 425 ILE n 
1 426 LEU n 
1 427 GLY n 
1 428 LYS n 
1 429 SER n 
1 430 GLY n 
1 431 ILE n 
1 432 ARG n 
1 433 ARG n 
1 434 ALA n 
1 435 TYR n 
1 436 GLU n 
1 437 THR n 
1 438 GLY n 
1 439 ARG n 
1 440 GLY n 
1 441 SER n 
1 442 ILE n 
1 443 GLN n 
1 444 MET n 
1 445 ARG n 
1 446 SER n 
1 447 ARG n 
1 448 ALA n 
1 449 VAL n 
1 450 ILE n 
1 451 GLU n 
1 452 GLU n 
1 453 ARG n 
1 454 GLY n 
1 455 GLY n 
1 456 GLY n 
1 457 ARG n 
1 458 GLN n 
1 459 ARG n 
1 460 ILE n 
1 461 VAL n 
1 462 VAL n 
1 463 THR n 
1 464 GLU n 
1 465 ILE n 
1 466 PRO n 
1 467 PHE n 
1 468 GLN n 
1 469 VAL n 
1 470 ASN n 
1 471 LYS n 
1 472 ALA n 
1 473 ARG n 
1 474 MET n 
1 475 ILE n 
1 476 GLU n 
1 477 LYS n 
1 478 ILE n 
1 479 ALA n 
1 480 GLU n 
1 481 LEU n 
1 482 VAL n 
1 483 ARG n 
1 484 ASP n 
1 485 LYS n 
1 486 LYS n 
1 487 ILE n 
1 488 ASP n 
1 489 GLY n 
1 490 ILE n 
1 491 THR n 
1 492 ASP n 
1 493 LEU n 
1 494 ARG n 
1 495 ASP n 
1 496 GLU n 
1 497 THR n 
1 498 SER n 
1 499 LEU n 
1 500 ARG n 
1 501 THR n 
1 502 GLY n 
1 503 VAL n 
1 504 ARG n 
1 505 VAL n 
1 506 VAL n 
1 507 ILE n 
1 508 ASP n 
1 509 VAL n 
1 510 ARG n 
1 511 LYS n 
1 512 ASP n 
1 513 ALA n 
1 514 ASN n 
1 515 ALA n 
1 516 SER n 
1 517 VAL n 
1 518 ILE n 
1 519 LEU n 
1 520 ASN n 
1 521 ASN n 
1 522 LEU n 
1 523 TYR n 
1 524 LYS n 
1 525 GLN n 
1 526 THR n 
1 527 PRO n 
1 528 LEU n 
1 529 GLN n 
1 530 THR n 
1 531 SER n 
1 532 PHE n 
1 533 GLY n 
1 534 VAL n 
1 535 ASN n 
1 536 MET n 
1 537 ILE n 
1 538 ALA n 
1 539 LEU n 
1 540 VAL n 
1 541 ASN n 
1 542 GLY n 
1 543 ARG n 
1 544 PRO n 
1 545 LYS n 
1 546 LEU n 
1 547 ILE n 
1 548 ASN n 
1 549 LEU n 
1 550 LYS n 
1 551 GLU n 
1 552 ALA n 
1 553 LEU n 
1 554 VAL n 
1 555 HIS n 
1 556 TYR n 
1 557 LEU n 
1 558 GLU n 
1 559 HIS n 
1 560 GLN n 
1 561 LYS n 
1 562 THR n 
1 563 VAL n 
1 564 VAL n 
1 565 ARG n 
1 566 ARG n 
1 567 ARG n 
1 568 THR n 
1 569 GLN n 
1 570 TYR n 
1 571 ASN n 
1 572 LEU n 
1 573 ARG n 
1 574 LYS n 
1 575 ALA n 
1 576 LYS n 
1 577 ASP n 
1 578 ARG n 
1 579 ALA n 
1 580 HIS n 
1 581 ILE n 
1 582 LEU n 
1 583 GLU n 
1 584 GLY n 
1 585 LEU n 
1 586 ARG n 
1 587 ILE n 
1 588 ALA n 
1 589 LEU n 
1 590 ASP n 
1 591 HIS n 
1 592 ILE n 
1 593 ASP n 
1 594 GLU n 
1 595 ILE n 
1 596 ILE n 
1 597 SER n 
1 598 THR n 
1 599 ILE n 
1 600 ARG n 
1 601 GLU n 
1 602 SER n 
1 603 ASP n 
1 604 THR n 
1 605 ASP n 
1 606 LYS n 
1 607 VAL n 
1 608 ALA n 
1 609 MET n 
1 610 GLU n 
1 611 SER n 
1 612 LEU n 
1 613 GLN n 
1 614 GLN n 
1 615 ARG n 
1 616 PHE n 
1 617 LYS n 
1 618 LEU n 
1 619 SER n 
1 620 GLU n 
1 621 LYS n 
1 622 GLN n 
1 623 ALA n 
1 624 GLN n 
1 625 ALA n 
1 626 ILE n 
1 627 LEU n 
1 628 ASP n 
1 629 MET n 
1 630 ARG n 
1 631 LEU n 
1 632 ARG n 
1 633 ARG n 
1 634 LEU n 
1 635 THR n 
1 636 GLY n 
1 637 LEU n 
1 638 GLU n 
1 639 ARG n 
1 640 ASP n 
1 641 LYS n 
1 642 ILE n 
1 643 GLU n 
1 644 ALA n 
1 645 GLU n 
1 646 TYR n 
1 647 ASN n 
1 648 GLU n 
1 649 LEU n 
1 650 LEU n 
1 651 ASN n 
1 652 TYR n 
1 653 ILE n 
1 654 SER n 
1 655 GLU n 
1 656 LEU n 
1 657 GLU n 
1 658 THR n 
1 659 ILE n 
1 660 LEU n 
1 661 ALA n 
1 662 ASP n 
1 663 GLU n 
1 664 GLU n 
1 665 VAL n 
1 666 LEU n 
1 667 LEU n 
1 668 GLN n 
1 669 LEU n 
1 670 VAL n 
1 671 ARG n 
1 672 ASP n 
1 673 GLU n 
1 674 LEU n 
1 675 THR n 
1 676 GLU n 
1 677 ILE n 
1 678 ARG n 
1 679 ASP n 
1 680 ARG n 
1 681 PHE n 
1 682 GLY n 
1 683 ASP n 
1 684 ASP n 
1 685 ARG n 
1 686 ARG n 
1 687 THR n 
1 688 GLU n 
1 689 ILE n 
1 690 GLN n 
1 691 LEU n 
1 692 GLY n 
2 1   DA  n 
2 2   DG  n 
2 3   DC  n 
2 4   DC  n 
2 5   DG  n 
2 6   DT  n 
2 7   DA  n 
2 8   DG  n 
3 1   DG  n 
3 2   DT  n 
3 3   DA  n 
3 4   DC  n 
3 5   DC  n 
3 6   DT  n 
3 7   DA  n 
3 8   DC  n 
3 9   DG  n 
3 10  DG  n 
3 11  DC  n 
3 12  DT  n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   135 ? ? 'gyrB, SA0005' ? N315 ? ? ? ? 'Staphylococcus aureus' 158879 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 138 200 ? ? 'gyrB, SA0005' ? N315 ? ? ? ? 'Staphylococcus aureus' 158879 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 3 sample 'Biological sequence' 203 692 ? ? 'gyrA, SA0006' ? N315 ? ? ? ? 'Staphylococcus aureus' 158879 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_pdbx_entity_src_syn.entity_id 
_pdbx_entity_src_syn.pdbx_src_id 
_pdbx_entity_src_syn.pdbx_alt_source_flag 
_pdbx_entity_src_syn.pdbx_beg_seq_num 
_pdbx_entity_src_syn.pdbx_end_seq_num 
_pdbx_entity_src_syn.organism_scientific 
_pdbx_entity_src_syn.organism_common_name 
_pdbx_entity_src_syn.ncbi_taxonomy_id 
_pdbx_entity_src_syn.details 
2 1 sample 1 20 ' synthetic construct' ? 32630 ? 
3 1 sample 1 20 ' synthetic construct' ? 32630 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP GYRB_STAAN P66937 ? 1 
;DVASLPGKLADCSSKSPEECEIFLVEGDSAGGSTKSGRDSRTQAILPLRGKILNVEKARLDRILNNNEIRQMITAFGTGI
GGDFDLAKARYHKIVIMTDADVDGAHIRTLLLTFFYRFMRPLIEAGYVYIAQPP
;
410 
2 UNP GYRB_STAAN P66937 ? 1 YKGLGEMNADQLWETTMNPEHRALLQVKLEDAIEADQTFEMLMGDVVENRRQFIEDNAVYANL 580 
3 UNP GYRA_STAAN Q99XG5 ? 1 
;AELPQSRINERNITSEMRESFLDYAMSVIVARALPDVRDGLKPVHRRILYGLNEQGMTPDKSYKKSARIVGDVMGKYHPH
GDSSIYEAMVRMAQDFSYRYPLVDGQGNFGSMDGDGAAAMRYTEARMTKITLELLRDINKDTIDFIDNYDGNEREPSVLP
ARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLSKNPDISIAELMEDIEGPDFPTAGLILGKSGIRRAYETGRGSI
QMRSRAVIEERGGGRQRIVVTEIPFQVNKARMIEKIAELVRDKKIDGITDLRDETSLRTGVRVVIDVRKDANASVILNNL
YKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEHQKTVVRRRTQYNLRKAKDRAHILEGLRIALDHIDEIISTIRES
DTDKVAMESLQQRFKLSEKQAQAILDMRLRRLTGLERDKIEAEYNELLNYISELETILADEEVLLQLVRDELTEIRDRFG
DDRRTEIQLG
;
2   
4 PDB 5NPP       5NPP   ? 2 ? 1   
5 PDB 5NPP       5NPP   ? 3 ? 1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 5NPP B 2   ? 135 ? P66937 410 ? 543 ? 410  543  
2  2 5NPP B 138 ? 200 ? P66937 580 ? 642 ? 580  999  
3  3 5NPP B 203 ? 692 ? Q99XG5 2   ? 491 ? 1002 1491 
4  1 5NPP D 2   ? 135 ? P66937 410 ? 543 ? 410  543  
5  2 5NPP D 138 ? 200 ? P66937 580 ? 642 ? 580  999  
6  3 5NPP D 203 ? 692 ? Q99XG5 2   ? 491 ? 1002 1491 
7  4 5NPP E 1   ? 8   ? 5NPP   -8  ? -1  ? -8   -1   
8  5 5NPP A 1   ? 12  ? 5NPP   1   ? 12  ? 1    12   
9  4 5NPP F 1   ? 8   ? 5NPP   -8  ? -1  ? -8   -1   
10 5 5NPP C 1   ? 12  ? 5NPP   1   ? 12  ? 1    12   
# 
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 5NPP MET B 1   ? UNP P66937 ? ? 'initiating methionine' 409  1  
1 5NPP THR B 136 ? UNP P66937 ? ? linker                  544  2  
1 5NPP GLY B 137 ? UNP P66937 ? ? linker                  545  3  
2 5NPP ASP B 201 ? UNP P66937 ? ? linker                  1000 4  
2 5NPP PHE B 202 ? UNP P66937 ? ? linker                  1001 5  
4 5NPP MET D 1   ? UNP P66937 ? ? 'initiating methionine' 409  6  
4 5NPP THR D 136 ? UNP P66937 ? ? linker                  544  7  
4 5NPP GLY D 137 ? UNP P66937 ? ? linker                  545  8  
5 5NPP ASP D 201 ? UNP P66937 ? ? linker                  1000 9  
5 5NPP PHE D 202 ? UNP P66937 ? ? linker                  1001 10 
# 
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 
6EJ non-polymer         . 
;(1R)-1-[(4-{[(6,7-dihydro[1,4]dioxino[2,3-c]pyridazin-3-yl)methyl]amino}piperidin-1-yl)methyl]-9-fluoro-1,2-dihydro-4H-pyrrolo[3,2,1-ij]quinolin-4-one
;
?                               'C24 H26 F N5 O3'   451.493 
94K non-polymer         . '~{N}-[(1~{R})-2-azanyl-1-phenyl-ethyl]-5-(2-chlorophenyl)-2-methyl-thiophene-3-carboxamide' ? 
'C20 H19 Cl N2 O S' 370.896 
ALA 'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'      121.158 
DA  'DNA linking'       y "2'-DEOXYADENOSINE-5'-MONOPHOSPHATE" ?                               'C10 H14 N5 O6 P'   331.222 
DC  'DNA linking'       y "2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE" ?                               'C9 H14 N3 O7 P'    307.197 
DG  'DNA linking'       y "2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE" ?                               'C10 H14 N5 O7 P'   347.221 
DMS non-polymer         . 'DIMETHYL SULFOXIDE' ?                               'C2 H6 O S'         78.133  
DT  'DNA linking'       y "THYMIDINE-5'-MONOPHOSPHATE" ?                               'C10 H15 N2 O8 P'   322.208 
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  
GOL non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
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 
MN  non-polymer         . 'MANGANESE (II) ION' ?                               'Mn 2'              54.938  
NA  non-polymer         . 'SODIUM ION' ?                               'Na 1'              22.990  
PHE 'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?                               'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?                               'C5 H11 N O2'       117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5NPP 
_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            3.10 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         60.35 
_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          MICROBATCH 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '7-11% PEG 5000 MME, 130-190 mM Bis-Tris pH 6.2' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 S 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-02-13 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9173 
_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                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9173 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5NPP 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.220 
_reflns.d_resolution_low                 19.890 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       97193 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.100 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  5.200 
_reflns.pdbx_Rmerge_I_obs                0.111 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            9.500 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             0 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.124 
_reflns.pdbx_Rpim_I_all                  0.053 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         502194 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.997 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
2.220  2.260  ? 1.1 ? ? ? ? ? 99.300 ? ? ? ? 1.158 ? ? ? ? ? ? ? ? 4.900 ? ? ? ? 1.287 0.553 ? 1 1 0.538 ? 
12.160 19.890 ? ?   ? ? ? ? ? 75.600 ? ? ? ? 0.029 ? ? ? ? ? ? ? ? 5.900 ? ? ? ? 0.031 0.013 ? 2 1 0.999 ? 
# 
_refine.aniso_B[1][1]                            -0.6600 
_refine.aniso_B[1][2]                            -0.3300 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            -0.6600 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            2.1300 
_refine.B_iso_max                                123.650 
_refine.B_iso_mean                               43.0960 
_refine.B_iso_min                                18.380 
_refine.correlation_coeff_Fo_to_Fc               0.9640 
_refine.correlation_coeff_Fo_to_Fc_free          0.9380 
_refine.details                                  'U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 5NPP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.2200 
_refine.ls_d_res_low                             19.8900 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     92297 
_refine.ls_number_reflns_R_free                  4893 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.1100 
_refine.ls_percent_reflns_R_free                 5.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1841 
_refine.ls_R_factor_R_free                       0.2269 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1818 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.2320 
_refine.pdbx_overall_ESU_R_Free                  0.1920 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             7.3570 
_refine.overall_SU_ML                            0.1690 
_refine.overall_SU_R_Cruickshank_DPI             0.2322 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       2.2200 
_refine_hist.d_res_low                        19.8900 
_refine_hist.pdbx_number_atoms_ligand         177 
_refine_hist.number_atoms_solvent             851 
_refine_hist.number_atoms_total               12408 
_refine_hist.pdbx_number_residues_total       1383 
_refine_hist.pdbx_B_iso_mean_ligand           50.23 
_refine_hist.pdbx_B_iso_mean_solvent          47.80 
_refine_hist.pdbx_number_atoms_protein        10580 
_refine_hist.pdbx_number_atoms_nucleic_acid   800 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.015  0.019  12356 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.781  1.912  16903 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 4.538  5.000  1413  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 33.413 23.669 556   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 16.722 15.000 2063  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 20.780 15.000 124   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.107  0.200  1833  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.021  9171  ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.2200 
_refine_ls_shell.d_res_low                        2.2770 
_refine_ls_shell.number_reflns_all                7125 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             365 
_refine_ls_shell.number_reflns_R_work             6760 
_refine_ls_shell.percent_reflns_obs               99.2500 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.3230 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.3090 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     5NPP 
_struct.title                        '2.22A STRUCTURE OF THIOPHENE2 AND GSK945237 WITH S.AUREUS DNA GYRASE AND DNA' 
_struct.pdbx_descriptor              'DNA gyrase subunit B, DNA gyrase subunit A/DNA Complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        5NPP 
_struct_keywords.text            'TYPE IIA TOPOISOMERASE, ANTIBACTERIAL, INHIBITOR, ISOMERASE' 
_struct_keywords.pdbx_keywords   ISOMERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1  ? 
B  N N 1  ? 
C  N N 2  ? 
D  N N 3  ? 
E  N N 2  ? 
F  N N 3  ? 
G  N N 4  ? 
H  N N 5  ? 
I  N N 6  ? 
J  N N 6  ? 
K  N N 6  ? 
L  N N 7  ? 
M  N N 8  ? 
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 6  ? 
U  N N 9  ? 
V  N N 6  ? 
W  N N 10 ? 
X  N N 10 ? 
Y  N N 10 ? 
Z  N N 10 ? 
AA N N 10 ? 
BA N N 10 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 17  ? GLU A 20  ? SER B 425  GLU B 428  5 ? 4  
HELX_P HELX_P2  AA2 GLY A 28  ? ARG A 39  ? GLY B 436  ARG B 447  1 ? 12 
HELX_P HELX_P3  AA3 ARG A 60  ? ASN A 67  ? ARG B 468  ASN B 475  1 ? 8  
HELX_P HELX_P4  AA4 ASN A 67  ? GLY A 78  ? ASN B 475  GLY B 486  1 ? 12 
HELX_P HELX_P5  AA5 ILE A 81  ? PHE A 85  ? ILE B 489  PHE B 493  5 ? 5  
HELX_P HELX_P6  AA6 ASP A 86  ? ALA A 90  ? ASP B 494  ALA B 498  5 ? 5  
HELX_P HELX_P7  AA7 ASP A 102 ? MET A 120 ? ASP B 510  MET B 528  1 ? 19 
HELX_P HELX_P8  AA8 MET A 120 ? ALA A 126 ? MET B 528  ALA B 534  1 ? 7  
HELX_P HELX_P9  AA9 GLY A 140 ? MET A 144 ? GLY B 582  MET B 586  5 ? 5  
HELX_P HELX_P10 AB1 ASN A 145 ? MET A 154 ? ASN B 587  MET B 596  1 ? 10 
HELX_P HELX_P11 AB2 ASP A 168 ? GLY A 181 ? ASP B 610  GLY B 623  1 ? 14 
HELX_P HELX_P12 AB3 VAL A 183 ? ALA A 195 ? VAL B 625  ALA B 637  1 ? 13 
HELX_P HELX_P13 AB4 ILE A 215 ? ALA A 233 ? ILE B 1014 ALA B 1032 1 ? 19 
HELX_P HELX_P14 AB5 LYS A 244 ? GLN A 257 ? LYS B 1043 GLN B 1056 1 ? 14 
HELX_P HELX_P15 AB6 SER A 268 ? TYR A 279 ? SER B 1067 TYR B 1078 1 ? 12 
HELX_P HELX_P16 AB7 GLY A 283 ? ALA A 295 ? GLY B 1082 ALA B 1094 1 ? 13 
HELX_P HELX_P17 AB8 THR A 330 ? ARG A 338 ? THR B 1129 ARG B 1137 1 ? 9  
HELX_P HELX_P18 AB9 PRO A 366 ? GLY A 372 ? PRO B 1165 GLY B 1171 1 ? 7  
HELX_P HELX_P19 AC1 ASN A 388 ? LYS A 401 ? ASN B 1187 LYS B 1200 1 ? 14 
HELX_P HELX_P20 AC2 SER A 406 ? MET A 411 ? SER B 1205 MET B 1210 1 ? 6  
HELX_P HELX_P21 AC3 LYS A 428 ? GLY A 438 ? LYS B 1227 GLY B 1237 1 ? 11 
HELX_P HELX_P22 AC4 ASN A 470 ? ASP A 484 ? ASN B 1269 ASP B 1283 1 ? 15 
HELX_P HELX_P23 AC5 ASN A 514 ? THR A 526 ? ASN B 1313 THR B 1325 1 ? 13 
HELX_P HELX_P24 AC6 ASN A 548 ? HIS A 591 ? ASN B 1347 HIS B 1390 1 ? 44 
HELX_P HELX_P25 AC7 HIS A 591 ? GLU A 601 ? HIS B 1390 GLU B 1400 1 ? 11 
HELX_P HELX_P26 AC8 THR A 604 ? LYS A 617 ? THR B 1403 LYS B 1416 1 ? 14 
HELX_P HELX_P27 AC9 SER A 619 ? MET A 629 ? SER B 1418 MET B 1428 1 ? 11 
HELX_P HELX_P28 AD1 ARG A 630 ? THR A 635 ? ARG B 1429 THR B 1434 5 ? 6  
HELX_P HELX_P29 AD2 LEU A 637 ? ASP A 662 ? LEU B 1436 ASP B 1461 1 ? 26 
HELX_P HELX_P30 AD3 ASP A 662 ? GLY A 682 ? ASP B 1461 GLY B 1481 1 ? 21 
HELX_P HELX_P31 AD4 SER B 17  ? GLU B 20  ? SER D 425  GLU D 428  5 ? 4  
HELX_P HELX_P32 AD5 GLY B 28  ? ARG B 39  ? GLY D 436  ARG D 447  1 ? 12 
HELX_P HELX_P33 AD6 ARG B 60  ? ASN B 67  ? ARG D 468  ASN D 475  1 ? 8  
HELX_P HELX_P34 AD7 ASN B 67  ? GLY B 78  ? ASN D 475  GLY D 486  1 ? 12 
HELX_P HELX_P35 AD8 ILE B 81  ? PHE B 85  ? ILE D 489  PHE D 493  5 ? 5  
HELX_P HELX_P36 AD9 ASP B 86  ? ALA B 90  ? ASP D 494  ALA D 498  5 ? 5  
HELX_P HELX_P37 AE1 ASP B 102 ? MET B 120 ? ASP D 510  MET D 528  1 ? 19 
HELX_P HELX_P38 AE2 MET B 120 ? GLY B 127 ? MET D 528  GLY D 535  1 ? 8  
HELX_P HELX_P39 AE3 GLY B 140 ? MET B 144 ? GLY D 582  MET D 586  5 ? 5  
HELX_P HELX_P40 AE4 ASN B 145 ? MET B 154 ? ASN D 587  MET D 596  1 ? 10 
HELX_P HELX_P41 AE5 ASP B 168 ? GLY B 181 ? ASP D 610  GLY D 623  1 ? 14 
HELX_P HELX_P42 AE6 VAL B 183 ? ALA B 195 ? VAL D 625  ALA D 637  1 ? 13 
HELX_P HELX_P43 AE7 ILE B 215 ? ALA B 233 ? ILE D 1014 ALA D 1032 1 ? 19 
HELX_P HELX_P44 AE8 LYS B 244 ? GLN B 257 ? LYS D 1043 GLN D 1056 1 ? 14 
HELX_P HELX_P45 AE9 SER B 268 ? TYR B 279 ? SER D 1067 TYR D 1078 1 ? 12 
HELX_P HELX_P46 AF1 GLY B 283 ? ALA B 295 ? GLY D 1082 ALA D 1094 1 ? 13 
HELX_P HELX_P47 AF2 THR B 330 ? ARG B 338 ? THR D 1129 ARG D 1137 1 ? 9  
HELX_P HELX_P48 AF3 PRO B 366 ? GLY B 372 ? PRO D 1165 GLY D 1171 1 ? 7  
HELX_P HELX_P49 AF4 ASN B 388 ? LYS B 401 ? ASN D 1187 LYS D 1200 1 ? 14 
HELX_P HELX_P50 AF5 SER B 406 ? ILE B 414 ? SER D 1205 ILE D 1213 1 ? 9  
HELX_P HELX_P51 AF6 LYS B 428 ? GLY B 438 ? LYS D 1227 GLY D 1237 1 ? 11 
HELX_P HELX_P52 AF7 ASN B 470 ? ASP B 484 ? ASN D 1269 ASP D 1283 1 ? 15 
HELX_P HELX_P53 AF8 ASN B 514 ? THR B 526 ? ASN D 1313 THR D 1325 1 ? 13 
HELX_P HELX_P54 AF9 ASN B 548 ? HIS B 591 ? ASN D 1347 HIS D 1390 1 ? 44 
HELX_P HELX_P55 AG1 HIS B 591 ? SER B 602 ? HIS D 1390 SER D 1401 1 ? 12 
HELX_P HELX_P56 AG2 THR B 604 ? LYS B 617 ? THR D 1403 LYS D 1416 1 ? 14 
HELX_P HELX_P57 AG3 SER B 619 ? MET B 629 ? SER D 1418 MET D 1428 1 ? 11 
HELX_P HELX_P58 AG4 ARG B 630 ? LEU B 634 ? ARG D 1429 LEU D 1433 5 ? 5  
HELX_P HELX_P59 AG5 THR B 635 ? ASP B 662 ? THR D 1434 ASP D 1461 1 ? 28 
HELX_P HELX_P60 AG6 ASP B 662 ? GLY B 682 ? ASP D 1461 GLY D 1481 1 ? 21 
# 
_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 
metalc1  metalc ? ? A ASP 100 OD2 ? ? ? 1_555 G  MN  .  MN ? ? B ASP 508  B MN  1501 1_555 ? ? ? ? ? ? ?            2.756 ? 
metalc2  metalc ? ? A ASP 102 OD2 ? ? ? 1_555 G  MN  .  MN ? ? B ASP 510  B MN  1501 1_555 ? ? ? ? ? ? ?            2.014 ? 
metalc3  metalc ? ? A TYR 523 O   ? ? ? 1_555 L  NA  .  NA ? ? B TYR 1322 B NA  1506 1_555 ? ? ? ? ? ? ?            2.339 ? 
metalc4  metalc ? ? A THR 526 O   ? ? ? 1_555 L  NA  .  NA ? ? B THR 1325 B NA  1506 1_555 ? ? ? ? ? ? ?            2.498 ? 
metalc5  metalc ? ? A GLN 529 O   ? ? ? 1_555 L  NA  .  NA ? ? B GLN 1328 B NA  1506 1_555 ? ? ? ? ? ? ?            2.643 ? 
metalc6  metalc ? ? B ASP 100 OD2 ? ? ? 1_555 N  MN  .  MN ? ? D ASP 508  D MN  1501 1_555 ? ? ? ? ? ? ?            2.613 ? 
metalc7  metalc ? ? B ASP 102 OD2 ? ? ? 1_555 N  MN  .  MN ? ? D ASP 510  D MN  1501 1_555 ? ? ? ? ? ? ?            2.245 ? 
metalc8  metalc ? ? G MN  .   MN  ? ? ? 1_555 W  HOH .  O  ? ? B MN  1501 B HOH 1740 1_555 ? ? ? ? ? ? ?            2.321 ? 
metalc9  metalc ? ? G MN  .   MN  ? ? ? 1_555 X  HOH .  O  ? ? B MN  1501 D HOH 1714 1_555 ? ? ? ? ? ? ?            2.399 ? 
metalc10 metalc ? ? G MN  .   MN  ? ? ? 1_555 W  HOH .  O  ? ? B MN  1501 B HOH 1796 1_555 ? ? ? ? ? ? ?            2.768 ? 
metalc11 metalc ? ? G MN  .   MN  ? ? ? 1_555 W  HOH .  O  ? ? B MN  1501 B HOH 1765 1_555 ? ? ? ? ? ? ?            2.355 ? 
metalc12 metalc ? ? L NA  .   NA  ? ? ? 1_555 W  HOH .  O  ? ? B NA  1506 B HOH 1926 1_555 ? ? ? ? ? ? ?            2.334 ? 
metalc13 metalc ? ? N MN  .   MN  ? ? ? 1_555 X  HOH .  O  ? ? D MN  1501 D HOH 1673 1_555 ? ? ? ? ? ? ?            2.302 ? 
metalc14 metalc ? ? N MN  .   MN  ? ? ? 1_555 X  HOH .  O  ? ? D MN  1501 D HOH 1738 1_555 ? ? ? ? ? ? ?            2.202 ? 
metalc15 metalc ? ? N MN  .   MN  ? ? ? 1_555 AA HOH .  O  ? ? D MN  1501 F HOH 112  1_555 ? ? ? ? ? ? ?            2.266 ? 
metalc16 metalc ? ? N MN  .   MN  ? ? ? 1_555 X  HOH .  O  ? ? D MN  1501 D HOH 1683 1_555 ? ? ? ? ? ? ?            1.989 ? 
metalc17 metalc ? ? L NA  .   NA  ? ? ? 1_555 X  HOH .  O  ? ? B NA  1506 D HOH 1916 1_665 ? ? ? ? ? ? ?            2.468 ? 
hydrog1  hydrog ? ? D DG  1   N1  A ? ? 1_555 F  DC  4  N3 ? ? A DG  1    C DC  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog2  hydrog ? ? D DG  1   N1  B ? ? 1_555 F  DC  4  N3 ? ? A DG  1    C DC  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog3  hydrog ? ? D DG  1   N2  A ? ? 1_555 F  DC  4  O2 ? ? A DG  1    C DC  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog4  hydrog ? ? D DG  1   N2  B ? ? 1_555 F  DC  4  O2 ? ? A DG  1    C DC  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog5  hydrog ? ? D DG  1   O6  A ? ? 1_555 F  DC  4  N4 ? ? A DG  1    C DC  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog6  hydrog ? ? D DG  1   O6  B ? ? 1_555 F  DC  4  N4 ? ? A DG  1    C DC  4    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog7  hydrog ? ? D DT  2   N3  A ? ? 1_555 F  DA  3  N1 ? ? A DT  2    C DA  3    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog8  hydrog ? ? D DT  2   N3  B ? ? 1_555 F  DA  3  N1 ? ? A DT  2    C DA  3    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog9  hydrog ? ? D DT  2   O4  A ? ? 1_555 F  DA  3  N6 ? ? A DT  2    C DA  3    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog10 hydrog ? ? D DT  2   O4  B ? ? 1_555 F  DA  3  N6 ? ? A DT  2    C DA  3    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog11 hydrog ? ? D DA  3   N1  ? ? ? 1_555 F  DT  2  N3 ? ? A DA  3    C DT  2    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog12 hydrog ? ? D DA  3   N6  ? ? ? 1_555 F  DT  2  O4 ? ? A DA  3    C DT  2    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog13 hydrog ? ? D DC  4   N3  A ? ? 1_555 F  DG  1  N1 ? ? A DC  4    C DG  1    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog14 hydrog ? ? D DC  4   N3  B ? ? 1_555 F  DG  1  N1 ? ? A DC  4    C DG  1    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog15 hydrog ? ? D DC  4   N4  A ? ? 1_555 F  DG  1  O6 ? ? A DC  4    C DG  1    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog16 hydrog ? ? D DC  4   N4  B ? ? 1_555 F  DG  1  O6 ? ? A DC  4    C DG  1    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog17 hydrog ? ? D DC  4   O2  A ? ? 1_555 F  DG  1  N2 ? ? A DC  4    C DG  1    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog18 hydrog ? ? D DC  4   O2  B ? ? 1_555 F  DG  1  N2 ? ? A DC  4    C DG  1    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog19 hydrog ? ? D DC  5   N3  A ? ? 1_555 E  DG  8  N1 ? ? A DC  5    F DG  -1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog20 hydrog ? ? D DC  5   N3  B ? ? 1_555 E  DG  8  N1 ? ? A DC  5    F DG  -1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog21 hydrog ? ? D DC  5   N4  A ? ? 1_555 E  DG  8  O6 ? ? A DC  5    F DG  -1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog22 hydrog ? ? D DC  5   N4  B ? ? 1_555 E  DG  8  O6 ? ? A DC  5    F DG  -1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog23 hydrog ? ? D DC  5   O2  A ? ? 1_555 E  DG  8  N2 ? ? A DC  5    F DG  -1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog24 hydrog ? ? D DC  5   O2  B ? ? 1_555 E  DG  8  N2 ? ? A DC  5    F DG  -1   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog25 hydrog ? ? D DT  6   N3  ? ? ? 1_555 E  DA  7  N1 ? ? A DT  6    F DA  -2   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog26 hydrog ? ? D DT  6   O4  ? ? ? 1_555 E  DA  7  N6 ? ? A DT  6    F DA  -2   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog27 hydrog ? ? D DA  7   N1  ? ? ? 1_555 E  DT  6  N3 ? ? A DA  7    F DT  -3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog28 hydrog ? ? D DA  7   N6  ? ? ? 1_555 E  DT  6  O4 ? ? A DA  7    F DT  -3   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog29 hydrog ? ? D DC  8   N3  ? ? ? 1_555 E  DG  5  N1 ? ? A DC  8    F DG  -4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog30 hydrog ? ? D DC  8   N4  ? ? ? 1_555 E  DG  5  O6 ? ? A DC  8    F DG  -4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog31 hydrog ? ? D DC  8   O2  ? ? ? 1_555 E  DG  5  N2 ? ? A DC  8    F DG  -4   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog32 hydrog ? ? D DG  9   N1  ? ? ? 1_555 E  DC  4  N3 ? ? A DG  9    F DC  -5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog33 hydrog ? ? D DG  9   N2  ? ? ? 1_555 E  DC  4  O2 ? ? A DG  9    F DC  -5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog34 hydrog ? ? D DG  9   O6  ? ? ? 1_555 E  DC  4  N4 ? ? A DG  9    F DC  -5   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog35 hydrog ? ? D DG  10  N1  ? ? ? 1_555 E  DC  3  N3 ? ? A DG  10   F DC  -6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog36 hydrog ? ? D DG  10  N2  ? ? ? 1_555 E  DC  3  O2 ? ? A DG  10   F DC  -6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog37 hydrog ? ? D DG  10  O6  ? ? ? 1_555 E  DC  3  N4 ? ? A DG  10   F DC  -6   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog38 hydrog ? ? D DC  11  N3  ? ? ? 1_555 E  DG  2  N1 ? ? A DC  11   F DG  -7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog39 hydrog ? ? D DC  11  N4  ? ? ? 1_555 E  DG  2  O6 ? ? A DC  11   F DG  -7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog40 hydrog ? ? D DC  11  O2  ? ? ? 1_555 E  DG  2  N2 ? ? A DC  11   F DG  -7   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog41 hydrog ? ? D DT  12  N3  ? ? ? 1_555 E  DA  1  N7 A ? A DT  12   F DA  -8   1_555 ? ? ? ? ? ? HOOGSTEEN    ?     ? 
hydrog42 hydrog ? ? D DT  12  N3  ? ? ? 1_555 E  DA  1  N7 B ? A DT  12   F DA  -8   1_555 ? ? ? ? ? ? HOOGSTEEN    ?     ? 
hydrog43 hydrog ? ? D DT  12  O4  ? ? ? 1_555 E  DA  1  N6 A ? A DT  12   F DA  -8   1_555 ? ? ? ? ? ? HOOGSTEEN    ?     ? 
hydrog44 hydrog ? ? D DT  12  O4  ? ? ? 1_555 E  DA  1  N6 B ? A DT  12   F DA  -8   1_555 ? ? ? ? ? ? HOOGSTEEN    ?     ? 
hydrog45 hydrog ? ? C DG  2   N1  ? ? ? 1_555 F  DC  11 N3 A ? E DG  -7   C DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog46 hydrog ? ? C DG  2   N1  ? ? ? 1_555 F  DC  11 N3 B ? E DG  -7   C DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog47 hydrog ? ? C DG  2   N2  ? ? ? 1_555 F  DC  11 O2 A ? E DG  -7   C DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog48 hydrog ? ? C DG  2   N2  ? ? ? 1_555 F  DC  11 O2 B ? E DG  -7   C DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog49 hydrog ? ? C DG  2   O6  ? ? ? 1_555 F  DC  11 N4 A ? E DG  -7   C DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog50 hydrog ? ? C DG  2   O6  ? ? ? 1_555 F  DC  11 N4 B ? E DG  -7   C DC  11   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog51 hydrog ? ? C DC  3   N3  ? ? ? 1_555 F  DG  10 N1 ? ? E DC  -6   C DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog52 hydrog ? ? C DC  3   N4  ? ? ? 1_555 F  DG  10 O6 ? ? E DC  -6   C DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog53 hydrog ? ? C DC  3   O2  ? ? ? 1_555 F  DG  10 N2 ? ? E DC  -6   C DG  10   1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog54 hydrog ? ? C DC  4   N3  ? ? ? 1_555 F  DG  9  N1 ? ? E DC  -5   C DG  9    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog55 hydrog ? ? C DC  4   N4  ? ? ? 1_555 F  DG  9  O6 ? ? E DC  -5   C DG  9    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog56 hydrog ? ? C DC  4   O2  ? ? ? 1_555 F  DG  9  N2 ? ? E DC  -5   C DG  9    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog57 hydrog ? ? C DG  5   N1  ? ? ? 1_555 F  DC  8  N3 ? ? E DG  -4   C DC  8    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog58 hydrog ? ? C DG  5   N2  ? ? ? 1_555 F  DC  8  O2 ? ? E DG  -4   C DC  8    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog59 hydrog ? ? C DG  5   O6  ? ? ? 1_555 F  DC  8  N4 ? ? E DG  -4   C DC  8    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog60 hydrog ? ? C DT  6   N3  ? ? ? 1_555 F  DA  7  N1 ? ? E DT  -3   C DA  7    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog61 hydrog ? ? C DT  6   O4  ? ? ? 1_555 F  DA  7  N6 ? ? E DT  -3   C DA  7    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog62 hydrog ? ? C DA  7   N1  ? ? ? 1_555 F  DT  6  N3 ? ? E DA  -2   C DT  6    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog63 hydrog ? ? C DA  7   N6  ? ? ? 1_555 F  DT  6  O4 ? ? E DA  -2   C DT  6    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog64 hydrog ? ? C DG  8   N1  ? ? ? 1_555 F  DC  5  N3 A ? E DG  -1   C DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog65 hydrog ? ? C DG  8   N1  ? ? ? 1_555 F  DC  5  N3 B ? E DG  -1   C DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog66 hydrog ? ? C DG  8   N2  ? ? ? 1_555 F  DC  5  O2 A ? E DG  -1   C DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog67 hydrog ? ? C DG  8   N2  ? ? ? 1_555 F  DC  5  O2 B ? E DG  -1   C DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog68 hydrog ? ? C DG  8   O6  ? ? ? 1_555 F  DC  5  N4 A ? E DG  -1   C DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
hydrog69 hydrog ? ? C DG  8   O6  ? ? ? 1_555 F  DC  5  N4 B ? E DG  -1   C DC  5    1_555 ? ? ? ? ? ? WATSON-CRICK ?     ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
metalc ? ? 
hydrog ? ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LEU 
_struct_mon_prot_cis.label_seq_id           691 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LEU 
_struct_mon_prot_cis.auth_seq_id            1490 
_struct_mon_prot_cis.auth_asym_id           B 
_struct_mon_prot_cis.pdbx_label_comp_id_2   GLY 
_struct_mon_prot_cis.pdbx_label_seq_id_2    692 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    GLY 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     1491 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    B 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -1.08 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 6 ? 
AA9 ? 3 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? anti-parallel 
AA8 5 6 ? parallel      
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? parallel      
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 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 GLN A 44  ? PRO A 48  ? GLN B 452  PRO B 456  
AA1 2 GLU A 22  ? VAL A 26  ? GLU B 430  VAL B 434  
AA1 3 LYS A 94  ? MET A 98  ? LYS B 502  MET B 506  
AA1 4 VAL A 129 ? ILE A 131 ? VAL B 537  ILE B 539  
AA1 5 LEU A 162 ? LYS A 165 ? LEU B 604  LYS B 607  
AA1 6 GLU A 212 ? ASN A 214 ? GLU B 1011 ASN B 1013 
AA2 1 LYS A 266 ? LYS A 267 ? LYS B 1065 LYS B 1066 
AA2 2 GLU A 326 ? MET A 329 ? GLU B 1125 MET B 1128 
AA2 3 VAL A 305 ? GLN A 308 ? VAL B 1104 GLN B 1107 
AA3 1 PHE A 347 ? ASP A 349 ? PHE B 1146 ASP B 1148 
AA3 2 ARG A 356 ? PRO A 358 ? ARG B 1155 PRO B 1157 
AA4 1 ALA A 373 ? ILE A 376 ? ALA B 1172 ILE B 1175 
AA4 2 ALA A 381 ? ILE A 384 ? ALA B 1180 ILE B 1183 
AA5 1 GLN A 529 ? ASN A 535 ? GLN B 1328 ASN B 1334 
AA5 2 ARG A 439 ? ARG A 445 ? ARG B 1238 ARG B 1244 
AA5 3 LEU A 424 ? LEU A 426 ? LEU B 1223 LEU B 1225 
AA5 4 GLU A 688 ? GLN A 690 ? GLU B 1487 GLN B 1489 
AA6 1 ARG A 447 ? GLY A 454 ? ARG B 1246 GLY B 1253 
AA6 2 ARG A 457 ? GLU A 464 ? ARG B 1256 GLU B 1263 
AA6 3 VAL A 505 ? VAL A 509 ? VAL B 1304 VAL B 1308 
AA6 4 ILE A 490 ? ASP A 495 ? ILE B 1289 ASP B 1294 
AA7 1 ILE A 537 ? VAL A 540 ? ILE B 1336 VAL B 1339 
AA7 2 ARG A 543 ? LEU A 546 ? ARG B 1342 LEU B 1345 
AA8 1 GLN B 44  ? PRO B 48  ? GLN D 452  PRO D 456  
AA8 2 GLU B 22  ? VAL B 26  ? GLU D 430  VAL D 434  
AA8 3 LYS B 94  ? MET B 98  ? LYS D 502  MET D 506  
AA8 4 VAL B 129 ? ILE B 131 ? VAL D 537  ILE D 539  
AA8 5 LEU B 162 ? LYS B 165 ? LEU D 604  LYS D 607  
AA8 6 GLU B 212 ? ASN B 214 ? GLU D 1011 ASN D 1013 
AA9 1 LYS B 266 ? LYS B 267 ? LYS D 1065 LYS D 1066 
AA9 2 GLU B 326 ? MET B 329 ? GLU D 1125 MET D 1128 
AA9 3 VAL B 305 ? GLN B 308 ? VAL D 1104 GLN D 1107 
AB1 1 PHE B 347 ? ASP B 349 ? PHE D 1146 ASP D 1148 
AB1 2 ARG B 356 ? PRO B 358 ? ARG D 1155 PRO D 1157 
AB2 1 ALA B 373 ? ILE B 376 ? ALA D 1172 ILE D 1175 
AB2 2 ALA B 381 ? ILE B 384 ? ALA D 1180 ILE D 1183 
AB3 1 GLN B 529 ? ASN B 535 ? GLN D 1328 ASN D 1334 
AB3 2 ARG B 439 ? ARG B 445 ? ARG D 1238 ARG D 1244 
AB3 3 LEU B 424 ? LEU B 426 ? LEU D 1223 LEU D 1225 
AB3 4 GLU B 688 ? GLN B 690 ? GLU D 1487 GLN D 1489 
AB4 1 ARG B 447 ? GLY B 454 ? ARG D 1246 GLY D 1253 
AB4 2 ARG B 457 ? GLU B 464 ? ARG D 1256 GLU D 1263 
AB4 3 VAL B 505 ? VAL B 509 ? VAL D 1304 VAL D 1308 
AB4 4 ILE B 490 ? ASP B 495 ? ILE D 1289 ASP D 1294 
AB5 1 ILE B 537 ? VAL B 540 ? ILE D 1336 VAL D 1339 
AB5 2 ARG B 543 ? LEU B 546 ? ARG D 1342 LEU D 1345 
# 
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 O ALA A 45  ? O ALA B 453  N GLU A 22  ? N GLU B 430  
AA1 2 3 N ILE A 23  ? N ILE B 431  O VAL A 96  ? O VAL B 504  
AA1 3 4 N ILE A 97  ? N ILE B 505  O TYR A 130 ? O TYR B 538  
AA1 4 5 N VAL A 129 ? N VAL B 537  O VAL A 164 ? O VAL B 606  
AA1 5 6 N LYS A 165 ? N LYS B 607  O ARG A 213 ? O ARG B 1012 
AA2 1 2 N LYS A 266 ? N LYS B 1065 O ALA A 327 ? O ALA B 1126 
AA2 2 3 O ARG A 328 ? O ARG B 1127 N ASP A 306 ? N ASP B 1105 
AA3 1 2 N ILE A 348 ? N ILE B 1147 O GLU A 357 ? O GLU B 1156 
AA4 1 2 N ALA A 373 ? N ALA B 1172 O ILE A 384 ? O ILE B 1183 
AA5 1 2 O THR A 530 ? O THR B 1329 N MET A 444 ? N MET B 1243 
AA5 2 3 O ARG A 445 ? O ARG B 1244 N LEU A 424 ? N LEU B 1223 
AA5 3 4 N ILE A 425 ? N ILE B 1224 O GLN A 690 ? O GLN B 1489 
AA6 1 2 N GLU A 451 ? N GLU B 1250 O ARG A 459 ? O ARG B 1258 
AA6 2 3 N VAL A 462 ? N VAL B 1261 O VAL A 505 ? O VAL B 1304 
AA6 3 4 O VAL A 506 ? O VAL B 1305 N ARG A 494 ? N ARG B 1293 
AA7 1 2 N VAL A 540 ? N VAL B 1339 O ARG A 543 ? O ARG B 1342 
AA8 1 2 O ALA B 45  ? O ALA D 453  N GLU B 22  ? N GLU D 430  
AA8 2 3 N LEU B 25  ? N LEU D 433  O VAL B 96  ? O VAL D 504  
AA8 3 4 N ILE B 95  ? N ILE D 503  O TYR B 130 ? O TYR D 538  
AA8 4 5 N VAL B 129 ? N VAL D 537  O VAL B 164 ? O VAL D 606  
AA8 5 6 N GLN B 163 ? N GLN D 605  O ARG B 213 ? O ARG D 1012 
AA9 1 2 N LYS B 266 ? N LYS D 1065 O ALA B 327 ? O ALA D 1126 
AA9 2 3 O ARG B 328 ? O ARG D 1127 N ASP B 306 ? N ASP D 1105 
AB1 1 2 N ILE B 348 ? N ILE D 1147 O GLU B 357 ? O GLU D 1156 
AB2 1 2 N ALA B 373 ? N ALA D 1172 O ILE B 384 ? O ILE D 1183 
AB3 1 2 O THR B 530 ? O THR D 1329 N MET B 444 ? N MET D 1243 
AB3 2 3 O ARG B 445 ? O ARG D 1244 N LEU B 424 ? N LEU D 1223 
AB3 3 4 N ILE B 425 ? N ILE D 1224 O GLN B 690 ? O GLN D 1489 
AB4 1 2 N VAL B 449 ? N VAL D 1248 O VAL B 461 ? O VAL D 1260 
AB4 2 3 N ILE B 460 ? N ILE D 1259 O ILE B 507 ? O ILE D 1306 
AB4 3 4 O VAL B 506 ? O VAL D 1305 N ARG B 494 ? N ARG D 1293 
AB5 1 2 N VAL B 540 ? N VAL D 1339 O ARG B 543 ? O ARG D 1342 
# 
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 MN  1501 ? 6  'binding site for residue MN B 1501'  
AC2 Software B 94K 1502 ? 9  'binding site for residue 94K B 1502' 
AC3 Software B GOL 1503 ? 7  'binding site for residue GOL B 1503' 
AC4 Software B GOL 1504 ? 7  'binding site for residue GOL B 1504' 
AC5 Software B GOL 1505 ? 6  'binding site for residue GOL B 1505' 
AC6 Software B NA  1506 ? 6  'binding site for residue NA B 1506'  
AC7 Software B DMS 1507 ? 5  'binding site for residue DMS B 1507' 
AC8 Software D MN  1501 ? 6  'binding site for residue MN D 1501'  
AC9 Software D 94K 1502 ? 12 'binding site for residue 94K D 1502' 
AD1 Software D GOL 1503 ? 6  'binding site for residue GOL D 1503' 
AD2 Software D GOL 1504 ? 8  'binding site for residue GOL D 1504' 
AD3 Software D GOL 1505 ? 5  'binding site for residue GOL D 1505' 
AD4 Software D GOL 1506 ? 3  'binding site for residue GOL D 1506' 
AD5 Software A GOL 101  ? 6  'binding site for residue GOL A 101'  
AD6 Software C 6EJ 101  ? 16 'binding site for residue 6EJ C 101'  
AD7 Software C GOL 102  ? 8  'binding site for residue GOL C 102'  
# 
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 6  ASP A  100 ? ASP B 508  . ? 1_555 ? 
2   AC1 6  ASP A  102 ? ASP B 510  . ? 1_555 ? 
3   AC1 6  HOH W  .   ? HOH B 1740 . ? 1_555 ? 
4   AC1 6  HOH W  .   ? HOH B 1765 . ? 1_555 ? 
5   AC1 6  HOH W  .   ? HOH B 1796 . ? 1_555 ? 
6   AC1 6  HOH X  .   ? HOH D 1714 . ? 1_555 ? 
7   AC2 9  ARG A  188 ? ARG B 630  . ? 1_555 ? 
8   AC2 9  ILE A  191 ? ILE B 633  . ? 1_555 ? 
9   AC2 9  GLU A  192 ? GLU B 634  . ? 1_555 ? 
10  AC2 9  VAL A  232 ? VAL B 1031 . ? 1_555 ? 
11  AC2 9  MET A  380 ? MET B 1179 . ? 1_555 ? 
12  AC2 9  ARG A  543 ? ARG B 1342 . ? 1_555 ? 
13  AC2 9  PRO A  544 ? PRO B 1343 . ? 1_555 ? 
14  AC2 9  HOH W  .   ? HOH B 1826 . ? 1_555 ? 
15  AC2 9  HOH W  .   ? HOH B 1833 . ? 1_555 ? 
16  AC3 7  GLU A  452 ? GLU B 1251 . ? 1_555 ? 
17  AC3 7  GLY A  456 ? GLY B 1255 . ? 1_555 ? 
18  AC3 7  ARG A  457 ? ARG B 1256 . ? 1_555 ? 
19  AC3 7  HOH W  .   ? HOH B 1605 . ? 1_555 ? 
20  AC3 7  HOH W  .   ? HOH B 1861 . ? 1_555 ? 
21  AC3 7  SER B  516 ? SER D 1315 . ? 5_554 ? 
22  AC3 7  ASN B  520 ? ASN D 1319 . ? 5_554 ? 
23  AC4 7  ARG A  248 ? ARG B 1047 . ? 1_555 ? 
24  AC4 7  ARG A  249 ? ARG B 1048 . ? 1_555 ? 
25  AC4 7  ILE A  348 ? ILE B 1147 . ? 1_555 ? 
26  AC4 7  GLU A  357 ? GLU B 1156 . ? 1_555 ? 
27  AC4 7  HOH W  .   ? HOH B 1673 . ? 1_555 ? 
28  AC4 7  HOH W  .   ? HOH B 1722 . ? 1_555 ? 
29  AC4 7  HOH W  .   ? HOH B 1746 . ? 1_555 ? 
30  AC5 6  GLU A  391 ? GLU B 1190 . ? 1_555 ? 
31  AC5 6  GLU A  415 ? GLU B 1214 . ? 1_555 ? 
32  AC5 6  ASP A  683 ? ASP B 1482 . ? 1_555 ? 
33  AC5 6  ASP A  684 ? ASP B 1483 . ? 1_555 ? 
34  AC5 6  ARG A  685 ? ARG B 1484 . ? 1_555 ? 
35  AC5 6  HOH W  .   ? HOH B 1721 . ? 1_555 ? 
36  AC6 6  TYR A  523 ? TYR B 1322 . ? 1_555 ? 
37  AC6 6  LYS A  524 ? LYS B 1323 . ? 1_555 ? 
38  AC6 6  THR A  526 ? THR B 1325 . ? 1_555 ? 
39  AC6 6  GLN A  529 ? GLN B 1328 . ? 1_555 ? 
40  AC6 6  HOH W  .   ? HOH B 1926 . ? 1_555 ? 
41  AC6 6  HOH X  .   ? HOH D 1916 . ? 1_665 ? 
42  AC7 5  PHE A  298 ? PHE B 1097 . ? 1_555 ? 
43  AC7 5  MET A  314 ? MET B 1113 . ? 1_555 ? 
44  AC7 5  GLY A  316 ? GLY B 1115 . ? 1_555 ? 
45  AC7 5  HOH W  .   ? HOH B 1904 . ? 1_555 ? 
46  AC7 5  HOH W  .   ? HOH B 1963 . ? 1_555 ? 
47  AC8 6  ASP B  100 ? ASP D 508  . ? 1_555 ? 
48  AC8 6  ASP B  102 ? ASP D 510  . ? 1_555 ? 
49  AC8 6  HOH X  .   ? HOH D 1673 . ? 1_555 ? 
50  AC8 6  HOH X  .   ? HOH D 1683 . ? 1_555 ? 
51  AC8 6  HOH X  .   ? HOH D 1738 . ? 1_555 ? 
52  AC8 6  HOH AA .   ? HOH F 112  . ? 1_555 ? 
53  AC9 12 ARG B  188 ? ARG D 630  . ? 1_555 ? 
54  AC9 12 ILE B  191 ? ILE D 633  . ? 1_555 ? 
55  AC9 12 GLU B  192 ? GLU D 634  . ? 1_555 ? 
56  AC9 12 ALA B  195 ? ALA D 637  . ? 1_555 ? 
57  AC9 12 VAL B  232 ? VAL D 1031 . ? 1_555 ? 
58  AC9 12 MET B  380 ? MET D 1179 . ? 1_555 ? 
59  AC9 12 ARG B  543 ? ARG D 1342 . ? 1_555 ? 
60  AC9 12 PRO B  544 ? PRO D 1343 . ? 1_555 ? 
61  AC9 12 HOH X  .   ? HOH D 1672 . ? 1_555 ? 
62  AC9 12 HOH X  .   ? HOH D 1828 . ? 1_555 ? 
63  AC9 12 HOH X  .   ? HOH D 1899 . ? 1_555 ? 
64  AC9 12 HOH X  .   ? HOH D 1965 . ? 1_555 ? 
65  AD1 6  PRO B  245 ? PRO D 1044 . ? 1_555 ? 
66  AD1 6  ARG B  248 ? ARG D 1047 . ? 1_555 ? 
67  AD1 6  GLU B  357 ? GLU D 1156 . ? 1_555 ? 
68  AD1 6  HOH X  .   ? HOH D 1688 . ? 1_555 ? 
69  AD1 6  HOH X  .   ? HOH D 1737 . ? 1_555 ? 
70  AD1 6  HOH X  .   ? HOH D 1837 . ? 1_555 ? 
71  AD2 8  ARG A  445 ? ARG B 1244 . ? 6_555 ? 
72  AD2 8  ASN A  520 ? ASN B 1319 . ? 6_555 ? 
73  AD2 8  GLU B  452 ? GLU D 1251 . ? 1_555 ? 
74  AD2 8  GLY B  456 ? GLY D 1255 . ? 1_555 ? 
75  AD2 8  ARG B  457 ? ARG D 1256 . ? 1_555 ? 
76  AD2 8  GLN B  458 ? GLN D 1257 . ? 1_555 ? 
77  AD2 8  HOH X  .   ? HOH D 1678 . ? 1_555 ? 
78  AD2 8  HOH X  .   ? HOH D 1754 . ? 1_555 ? 
79  AD3 5  GLY B  316 ? GLY D 1115 . ? 1_555 ? 
80  AD3 5  GLN B  468 ? GLN D 1267 . ? 1_555 ? 
81  AD3 5  HOH X  .   ? HOH D 1818 . ? 1_555 ? 
82  AD3 5  HOH X  .   ? HOH D 1866 . ? 1_555 ? 
83  AD3 5  DC  E  4   ? DC  F -5   . ? 1_555 ? 
84  AD4 3  ASP B  590 ? ASP D 1389 . ? 1_555 ? 
85  AD4 3  HIS B  591 ? HIS D 1390 . ? 1_555 ? 
86  AD4 3  DA  C  1   ? DA  E -8   . ? 1_445 ? 
87  AD5 6  DG  D  1   ? DG  A 1    . ? 1_555 ? 
88  AD5 6  DT  D  2   ? DT  A 2    . ? 1_555 ? 
89  AD5 6  HOH Z  .   ? HOH A 216  . ? 1_555 ? 
90  AD5 6  SER A  285 ? SER B 1084 . ? 1_555 ? 
91  AD5 6  HOH W  .   ? HOH B 1742 . ? 1_555 ? 
92  AD5 6  DG  C  8   ? DG  E -1   . ? 1_555 ? 
93  AD6 16 DT  D  2   ? DT  A 2    . ? 1_555 ? 
94  AD6 16 DA  D  3   ? DA  A 3    . ? 1_555 ? 
95  AD6 16 ALA A  269 ? ALA B 1068 . ? 1_555 ? 
96  AD6 16 GLY A  273 ? GLY B 1072 . ? 1_555 ? 
97  AD6 16 MET A  276 ? MET B 1075 . ? 1_555 ? 
98  AD6 16 ASP A  284 ? ASP B 1083 . ? 1_555 ? 
99  AD6 16 MET A  322 ? MET B 1121 . ? 1_555 ? 
100 AD6 16 HOH W  .   ? HOH B 1727 . ? 1_555 ? 
101 AD6 16 HOH W  .   ? HOH B 1855 . ? 1_555 ? 
102 AD6 16 DT  F  2   ? DT  C 2    . ? 1_555 ? 
103 AD6 16 DA  F  3   ? DA  C 3    . ? 1_555 ? 
104 AD6 16 HOH BA .   ? HOH C 219  . ? 1_555 ? 
105 AD6 16 ALA B  269 ? ALA D 1068 . ? 1_555 ? 
106 AD6 16 MET B  276 ? MET D 1075 . ? 1_555 ? 
107 AD6 16 ASP B  284 ? ASP D 1083 . ? 1_555 ? 
108 AD6 16 MET B  322 ? MET D 1121 . ? 1_555 ? 
109 AD7 8  DG  F  1   ? DG  C 1    . ? 1_555 ? 
110 AD7 8  DT  F  2   ? DT  C 2    . ? 1_555 ? 
111 AD7 8  HOH BA .   ? HOH C 206  . ? 1_555 ? 
112 AD7 8  HOH BA .   ? HOH C 208  . ? 1_555 ? 
113 AD7 8  SER B  285 ? SER D 1084 . ? 1_555 ? 
114 AD7 8  HOH X  .   ? HOH D 1669 . ? 1_555 ? 
115 AD7 8  DA  E  7   ? DA  F -2   . ? 1_555 ? 
116 AD7 8  DG  E  8   ? DG  F -1   . ? 1_555 ? 
# 
_atom_sites.entry_id                    5NPP 
_atom_sites.fract_transf_matrix[1][1]   0.010770 
_atom_sites.fract_transf_matrix[1][2]   0.006218 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012436 
_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]   0.002439 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
MN 
N  
NA 
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N     . LYS A  1  9   ? 4.661   60.320  54.880 1.00 55.35  ? 417  LYS B N     1 
ATOM   2     C  CA    . LYS A  1  9   ? 4.628   58.874  55.210 1.00 51.79  ? 417  LYS B CA    1 
ATOM   3     C  C     . LYS A  1  9   ? 4.538   58.630  56.731 1.00 56.60  ? 417  LYS B C     1 
ATOM   4     O  O     . LYS A  1  9   ? 4.172   57.533  57.155 1.00 55.46  ? 417  LYS B O     1 
ATOM   5     C  CB    . LYS A  1  9   ? 5.856   58.186  54.621 1.00 51.27  ? 417  LYS B CB    1 
ATOM   6     N  N     . LEU A  1  10  ? 4.849   59.646  57.543 1.00 58.67  ? 418  LEU B N     1 
ATOM   7     C  CA    . LEU A  1  10  ? 4.829   59.508  58.990 1.00 47.76  ? 418  LEU B CA    1 
ATOM   8     C  C     . LEU A  1  10  ? 3.427   59.234  59.537 1.00 44.61  ? 418  LEU B C     1 
ATOM   9     O  O     . LEU A  1  10  ? 2.493   59.918  59.206 1.00 44.78  ? 418  LEU B O     1 
ATOM   10    C  CB    . LEU A  1  10  ? 5.395   60.758  59.633 1.00 40.10  ? 418  LEU B CB    1 
ATOM   11    C  CG    . LEU A  1  10  ? 5.320   60.834  61.161 1.00 47.70  ? 418  LEU B CG    1 
ATOM   12    C  CD1   . LEU A  1  10  ? 6.216   59.834  61.893 1.00 40.79  ? 418  LEU B CD1   1 
ATOM   13    C  CD2   . LEU A  1  10  ? 5.723   62.243  61.567 1.00 40.47  ? 418  LEU B CD2   1 
ATOM   14    N  N     . ALA A  1  11  ? 3.278   58.207  60.341 1.00 43.71  ? 419  ALA B N     1 
ATOM   15    C  CA    . ALA A  1  11  ? 2.031   58.025  61.073 1.00 44.29  ? 419  ALA B CA    1 
ATOM   16    C  C     . ALA A  1  11  ? 2.277   58.357  62.529 1.00 47.05  ? 419  ALA B C     1 
ATOM   17    O  O     . ALA A  1  11  ? 2.796   57.536  63.292 1.00 40.84  ? 419  ALA B O     1 
ATOM   18    C  CB    . ALA A  1  11  ? 1.538   56.612  60.923 1.00 42.39  ? 419  ALA B CB    1 
ATOM   19    N  N     . ASP A  1  12  ? 1.918   59.574  62.914 1.00 51.19  ? 420  ASP B N     1 
ATOM   20    C  CA    . ASP A  1  12  ? 2.238   60.054  64.238 1.00 48.20  ? 420  ASP B CA    1 
ATOM   21    C  C     . ASP A  1  12  ? 1.354   59.513  65.319 1.00 47.11  ? 420  ASP B C     1 
ATOM   22    O  O     . ASP A  1  12  ? 0.278   59.034  65.053 1.00 49.48  ? 420  ASP B O     1 
ATOM   23    C  CB    . ASP A  1  12  ? 2.131   61.547  64.221 1.00 44.87  ? 420  ASP B CB    1 
ATOM   24    C  CG    . ASP A  1  12  ? 3.137   62.171  65.103 1.00 49.47  ? 420  ASP B CG    1 
ATOM   25    O  OD1   . ASP A  1  12  ? 3.736   61.475  65.947 1.00 47.92  ? 420  ASP B OD1   1 
ATOM   26    O  OD2   . ASP A  1  12  ? 3.332   63.379  64.983 1.00 52.79  ? 420  ASP B OD2   1 
ATOM   27    N  N     . CYS A  1  13  ? 1.807   59.587  66.560 1.00 50.32  ? 421  CYS B N     1 
ATOM   28    C  CA    . CYS A  1  13  ? 0.951   59.219  67.695 1.00 49.42  ? 421  CYS B CA    1 
ATOM   29    C  C     . CYS A  1  13  ? 0.103   60.409  68.199 1.00 54.70  ? 421  CYS B C     1 
ATOM   30    O  O     . CYS A  1  13  ? 0.353   61.539  67.779 1.00 56.99  ? 421  CYS B O     1 
ATOM   31    C  CB    . CYS A  1  13  ? 1.814   58.647  68.822 1.00 47.36  ? 421  CYS B CB    1 
ATOM   32    S  SG    . CYS A  1  13  ? 3.133   59.773  69.318 1.00 51.00  ? 421  CYS B SG    1 
ATOM   33    N  N     . SER A  1  14  ? -0.819  60.160  69.142 1.00 59.76  ? 422  SER B N     1 
ATOM   34    C  CA    . SER A  1  14  ? -1.719  61.206  69.695 1.00 53.69  ? 422  SER B CA    1 
ATOM   35    C  C     . SER A  1  14  ? -1.032  62.156  70.656 1.00 49.92  ? 422  SER B C     1 
ATOM   36    O  O     . SER A  1  14  ? -1.097  63.366  70.512 1.00 50.03  ? 422  SER B O     1 
ATOM   37    C  CB    . SER A  1  14  ? -2.829  60.571  70.500 1.00 50.92  ? 422  SER B CB    1 
ATOM   38    O  OG    . SER A  1  14  ? -3.648  59.812  69.685 1.00 68.13  ? 422  SER B OG    1 
ATOM   39    N  N     . SER A  1  15  ? -0.403  61.583  71.669 1.00 51.38  ? 423  SER B N     1 
ATOM   40    C  CA    . SER A  1  15  ? 0.263   62.352  72.710 1.00 57.31  ? 423  SER B CA    1 
ATOM   41    C  C     . SER A  1  15  ? 1.267   63.327  72.128 1.00 60.71  ? 423  SER B C     1 
ATOM   42    O  O     . SER A  1  15  ? 1.892   63.051  71.101 1.00 68.96  ? 423  SER B O     1 
ATOM   43    C  CB    . SER A  1  15  ? 0.947   61.422  73.694 1.00 49.06  ? 423  SER B CB    1 
ATOM   44    O  OG    . SER A  1  15  ? 1.881   62.112  74.486 1.00 50.71  ? 423  SER B OG    1 
ATOM   45    N  N     A LYS A  1  16  ? 1.376   64.438  72.842 0.50 65.51  ? 424  LYS B N     1 
ATOM   46    N  N     B LYS A  1  16  ? 1.408   64.501  72.753 0.50 63.99  ? 424  LYS B N     1 
ATOM   47    C  CA    A LYS A  1  16  ? 2.160   65.585  72.468 0.50 66.98  ? 424  LYS B CA    1 
ATOM   48    C  CA    B LYS A  1  16  ? 2.373   65.524  72.303 0.50 64.18  ? 424  LYS B CA    1 
ATOM   49    C  C     A LYS A  1  16  ? 3.328   65.666  73.405 0.50 68.45  ? 424  LYS B C     1 
ATOM   50    C  C     B LYS A  1  16  ? 3.412   65.677  73.389 0.50 66.57  ? 424  LYS B C     1 
ATOM   51    O  O     A LYS A  1  16  ? 4.136   66.586  73.338 0.50 73.83  ? 424  LYS B O     1 
ATOM   52    O  O     B LYS A  1  16  ? 4.241   66.600  73.362 0.50 71.05  ? 424  LYS B O     1 
ATOM   53    C  CB    A LYS A  1  16  ? 1.313   66.842  72.635 0.50 66.06  ? 424  LYS B CB    1 
ATOM   54    C  CB    B LYS A  1  16  ? 1.704   66.866  71.988 0.50 59.81  ? 424  LYS B CB    1 
ATOM   55    C  CG    A LYS A  1  16  ? 0.498   66.957  73.937 0.50 62.29  ? 424  LYS B CG    1 
ATOM   56    C  CG    B LYS A  1  16  ? 1.247   67.031  70.536 0.50 55.77  ? 424  LYS B CG    1 
ATOM   57    C  CD    A LYS A  1  16  ? 1.338   66.959  75.205 0.50 62.52  ? 424  LYS B CD    1 
ATOM   58    C  CD    B LYS A  1  16  ? 2.094   66.160  69.612 0.50 51.83  ? 424  LYS B CD    1 
ATOM   59    C  CE    A LYS A  1  16  ? 1.694   68.361  75.678 0.50 58.12  ? 424  LYS B CE    1 
ATOM   60    C  CE    B LYS A  1  16  ? 1.687   66.294  68.151 0.50 50.13  ? 424  LYS B CE    1 
ATOM   61    N  NZ    A LYS A  1  16  ? 2.921   68.288  76.522 0.50 53.76  ? 424  LYS B NZ    1 
ATOM   62    N  NZ    B LYS A  1  16  ? 1.597   64.965  67.495 0.50 43.55  ? 424  LYS B NZ    1 
ATOM   63    N  N     . SER A  1  17  ? 3.324   64.747  74.337 1.00 66.09  ? 425  SER B N     1 
ATOM   64    C  CA    . SER A  1  17  ? 4.256   64.712  75.401 1.00 62.63  ? 425  SER B CA    1 
ATOM   65    C  C     . SER A  1  17  ? 5.428   63.794  74.986 1.00 60.37  ? 425  SER B C     1 
ATOM   66    O  O     . SER A  1  17  ? 5.337   62.563  75.140 1.00 60.69  ? 425  SER B O     1 
ATOM   67    C  CB    . SER A  1  17  ? 3.537   64.236  76.663 1.00 62.89  ? 425  SER B CB    1 
ATOM   68    O  OG    . SER A  1  17  ? 4.448   63.801  77.656 1.00 67.30  ? 425  SER B OG    1 
ATOM   69    N  N     . PRO A  1  18  ? 6.544   64.384  74.476 1.00 56.05  ? 426  PRO B N     1 
ATOM   70    C  CA    . PRO A  1  18  ? 7.586   63.445  74.010 1.00 55.92  ? 426  PRO B CA    1 
ATOM   71    C  C     . PRO A  1  18  ? 8.108   62.497  75.040 1.00 57.45  ? 426  PRO B C     1 
ATOM   72    O  O     . PRO A  1  18  ? 8.761   61.578  74.821 1.00 60.27  ? 426  PRO B O     1 
ATOM   73    C  CB    . PRO A  1  18  ? 8.781   64.358  73.743 1.00 57.92  ? 426  PRO B CB    1 
ATOM   74    C  CG    . PRO A  1  18  ? 8.161   65.612  73.243 1.00 58.56  ? 426  PRO B CG    1 
ATOM   75    C  CD    . PRO A  1  18  ? 6.971   65.787  74.196 1.00 54.89  ? 426  PRO B CD    1 
ATOM   76    N  N     A GLU A  1  19  ? 7.903   62.778  76.277 0.50 58.88  ? 427  GLU B N     1 
ATOM   77    N  N     B GLU A  1  19  ? 7.907   62.754  76.278 0.50 59.37  ? 427  GLU B N     1 
ATOM   78    C  CA    A GLU A  1  19  ? 8.679   61.958  77.120 0.50 58.81  ? 427  GLU B CA    1 
ATOM   79    C  CA    B GLU A  1  19  ? 8.720   61.899  77.058 0.50 59.46  ? 427  GLU B CA    1 
ATOM   80    C  C     A GLU A  1  19  ? 8.221   60.489  77.046 0.50 55.90  ? 427  GLU B C     1 
ATOM   81    C  C     B GLU A  1  19  ? 8.212   60.463  77.074 0.50 55.84  ? 427  GLU B C     1 
ATOM   82    O  O     A GLU A  1  19  ? 8.966   59.568  77.266 0.50 52.91  ? 427  GLU B O     1 
ATOM   83    O  O     B GLU A  1  19  ? 8.928   59.536  77.347 0.50 51.78  ? 427  GLU B O     1 
ATOM   84    C  CB    A GLU A  1  19  ? 8.390   62.413  78.478 0.50 68.24  ? 427  GLU B CB    1 
ATOM   85    C  CB    B GLU A  1  19  ? 8.716   62.462  78.397 0.50 70.37  ? 427  GLU B CB    1 
ATOM   86    C  CG    A GLU A  1  19  ? 6.884   62.447  78.723 0.50 71.87  ? 427  GLU B CG    1 
ATOM   87    C  CG    B GLU A  1  19  ? 9.227   63.882  78.278 0.50 76.79  ? 427  GLU B CG    1 
ATOM   88    C  CD    A GLU A  1  19  ? 6.471   63.103  80.019 0.50 71.55  ? 427  GLU B CD    1 
ATOM   89    C  CD    B GLU A  1  19  ? 9.667   64.499  79.599 0.50 77.86  ? 427  GLU B CD    1 
ATOM   90    O  OE1   A GLU A  1  19  ? 7.216   62.986  81.010 0.50 71.84  ? 427  GLU B OE1   1 
ATOM   91    O  OE1   B GLU A  1  19  ? 9.627   63.813  80.640 0.50 80.45  ? 427  GLU B OE1   1 
ATOM   92    O  OE2   A GLU A  1  19  ? 5.385   63.725  80.034 0.50 70.03  ? 427  GLU B OE2   1 
ATOM   93    O  OE2   B GLU A  1  19  ? 10.104  65.668  79.569 0.50 82.43  ? 427  GLU B OE2   1 
ATOM   94    N  N     . GLU A  1  20  ? 6.964   60.306  76.721 1.00 54.39  ? 428  GLU B N     1 
ATOM   95    C  CA    . GLU A  1  20  ? 6.425   59.052  76.645 1.00 55.97  ? 428  GLU B CA    1 
ATOM   96    C  C     . GLU A  1  20  ? 6.183   58.558  75.215 1.00 57.75  ? 428  GLU B C     1 
ATOM   97    O  O     . GLU A  1  20  ? 5.521   57.519  75.019 1.00 57.33  ? 428  GLU B O     1 
ATOM   98    C  CB    . GLU A  1  20  ? 5.138   59.189  77.411 1.00 54.57  ? 428  GLU B CB    1 
ATOM   99    C  CG    . GLU A  1  20  ? 3.983   59.791  76.632 1.00 60.40  ? 428  GLU B CG    1 
ATOM   100   C  CD    . GLU A  1  20  ? 2.675   59.827  77.389 1.00 68.45  ? 428  GLU B CD    1 
ATOM   101   O  OE1   . GLU A  1  20  ? 2.510   59.035  78.335 1.00 70.61  ? 428  GLU B OE1   1 
ATOM   102   O  OE2   . GLU A  1  20  ? 1.808   60.630  76.978 1.00 63.90  ? 428  GLU B OE2   1 
ATOM   103   N  N     . CYS A  1  21  ? 6.662   59.279  74.211 1.00 53.92  ? 429  CYS B N     1 
ATOM   104   C  CA    . CYS A  1  21  ? 6.369   58.897  72.819 1.00 49.43  ? 429  CYS B CA    1 
ATOM   105   C  C     . CYS A  1  21  ? 7.540   58.202  72.133 1.00 55.17  ? 429  CYS B C     1 
ATOM   106   O  O     . CYS A  1  21  ? 8.718   58.429  72.430 1.00 56.48  ? 429  CYS B O     1 
ATOM   107   C  CB    . CYS A  1  21  ? 5.989   60.117  72.043 1.00 51.73  ? 429  CYS B CB    1 
ATOM   108   S  SG    . CYS A  1  21  ? 4.406   60.856  72.477 1.00 53.82  ? 429  CYS B SG    1 
ATOM   109   N  N     . GLU A  1  22  ? 7.205   57.308  71.222 1.00 45.80  ? 430  GLU B N     1 
ATOM   110   C  CA    . GLU A  1  22  ? 8.221   56.510  70.579 1.00 40.44  ? 430  GLU B CA    1 
ATOM   111   C  C     . GLU A  1  22  ? 8.019   56.582  69.092 1.00 40.13  ? 430  GLU B C     1 
ATOM   112   O  O     . GLU A  1  22  ? 6.885   56.610  68.626 1.00 42.40  ? 430  GLU B O     1 
ATOM   113   C  CB    . GLU A  1  22  ? 8.160   55.065  71.063 1.00 36.07  ? 430  GLU B CB    1 
ATOM   114   C  CG    . GLU A  1  22  ? 8.015   54.905  72.564 1.00 38.71  ? 430  GLU B CG    1 
ATOM   115   C  CD    . GLU A  1  22  ? 7.771   53.457  73.028 1.00 42.46  ? 430  GLU B CD    1 
ATOM   116   O  OE1   . GLU A  1  22  ? 8.001   53.145  74.218 1.00 41.29  ? 430  GLU B OE1   1 
ATOM   117   O  OE2   . GLU A  1  22  ? 7.382   52.601  72.214 1.00 42.30  ? 430  GLU B OE2   1 
ATOM   118   N  N     . ILE A  1  23  ? 9.105   56.657  68.326 1.00 38.70  ? 431  ILE B N     1 
ATOM   119   C  CA    . ILE A  1  23  ? 8.964   56.573  66.871 1.00 36.28  ? 431  ILE B CA    1 
ATOM   120   C  C     . ILE A  1  23  ? 9.717   55.339  66.343 1.00 40.44  ? 431  ILE B C     1 
ATOM   121   O  O     . ILE A  1  23  ? 10.879  55.134  66.682 1.00 40.73  ? 431  ILE B O     1 
ATOM   122   C  CB    . ILE A  1  23  ? 9.389   57.854  66.174 1.00 33.87  ? 431  ILE B CB    1 
ATOM   123   C  CG1   . ILE A  1  23  ? 9.033   57.763  64.694 1.00 36.55  ? 431  ILE B CG1   1 
ATOM   124   C  CG2   . ILE A  1  23  ? 10.900  58.103  66.335 1.00 33.03  ? 431  ILE B CG2   1 
ATOM   125   C  CD1   . ILE A  1  23  ? 9.359   59.022  63.895 1.00 31.21  ? 431  ILE B CD1   1 
ATOM   126   N  N     . PHE A  1  24  ? 9.068   54.553  65.498 1.00 37.50  ? 432  PHE B N     1 
ATOM   127   C  CA    . PHE A  1  24  ? 9.663   53.306  65.010 1.00 35.94  ? 432  PHE B CA    1 
ATOM   128   C  C     . PHE A  1  24  ? 9.990   53.490  63.559 1.00 32.76  ? 432  PHE B C     1 
ATOM   129   O  O     . PHE A  1  24  ? 9.117   53.779  62.779 1.00 34.34  ? 432  PHE B O     1 
ATOM   130   C  CB    . PHE A  1  24  ? 8.636   52.176  65.111 1.00 36.02  ? 432  PHE B CB    1 
ATOM   131   C  CG    . PHE A  1  24  ? 8.459   51.653  66.479 1.00 37.78  ? 432  PHE B CG    1 
ATOM   132   C  CD1   . PHE A  1  24  ? 7.642   52.317  67.385 1.00 41.22  ? 432  PHE B CD1   1 
ATOM   133   C  CD2   . PHE A  1  24  ? 9.133   50.510  66.890 1.00 36.62  ? 432  PHE B CD2   1 
ATOM   134   C  CE1   . PHE A  1  24  ? 7.503   51.841  68.675 1.00 41.28  ? 432  PHE B CE1   1 
ATOM   135   C  CE2   . PHE A  1  24  ? 8.990   50.029  68.178 1.00 40.33  ? 432  PHE B CE2   1 
ATOM   136   C  CZ    . PHE A  1  24  ? 8.142   50.685  69.073 1.00 39.83  ? 432  PHE B CZ    1 
ATOM   137   N  N     . LEU A  1  25  ? 11.245  53.289  63.210 1.00 32.60  ? 433  LEU B N     1 
ATOM   138   C  CA    . LEU A  1  25  ? 11.726  53.371  61.838 1.00 33.39  ? 433  LEU B CA    1 
ATOM   139   C  C     . LEU A  1  25  ? 11.746  51.964  61.225 1.00 31.27  ? 433  LEU B C     1 
ATOM   140   O  O     . LEU A  1  25  ? 12.480  51.115  61.691 1.00 30.11  ? 433  LEU B O     1 
ATOM   141   C  CB    . LEU A  1  25  ? 13.142  53.956  61.857 1.00 33.40  ? 433  LEU B CB    1 
ATOM   142   C  CG    . LEU A  1  25  ? 13.332  55.335  62.469 1.00 36.99  ? 433  LEU B CG    1 
ATOM   143   C  CD1   . LEU A  1  25  ? 14.808  55.656  62.515 1.00 35.23  ? 433  LEU B CD1   1 
ATOM   144   C  CD2   . LEU A  1  25  ? 12.602  56.333  61.581 1.00 41.11  ? 433  LEU B CD2   1 
ATOM   145   N  N     . VAL A  1  26  ? 10.929  51.741  60.208 1.00 32.80  ? 434  VAL B N     1 
ATOM   146   C  CA    . VAL A  1  26  ? 10.775  50.397  59.561 1.00 38.54  ? 434  VAL B CA    1 
ATOM   147   C  C     . VAL A  1  26  ? 11.250  50.436  58.116 1.00 39.09  ? 434  VAL B C     1 
ATOM   148   O  O     . VAL A  1  26  ? 11.342  51.543  57.521 1.00 46.17  ? 434  VAL B O     1 
ATOM   149   C  CB    . VAL A  1  26  ? 9.327   49.858  59.610 1.00 36.38  ? 434  VAL B CB    1 
ATOM   150   C  CG1   . VAL A  1  26  ? 8.901   49.677  61.032 1.00 39.18  ? 434  VAL B CG1   1 
ATOM   151   C  CG2   . VAL A  1  26  ? 8.357   50.807  58.935 1.00 40.69  ? 434  VAL B CG2   1 
ATOM   152   N  N     . GLU A  1  27  ? 11.561  49.266  57.548 1.00 44.97  ? 435  GLU B N     1 
ATOM   153   C  CA    . GLU A  1  27  ? 12.182  49.181  56.210 1.00 50.59  ? 435  GLU B CA    1 
ATOM   154   C  C     . GLU A  1  27  ? 11.357  49.710  55.011 1.00 60.72  ? 435  GLU B C     1 
ATOM   155   O  O     . GLU A  1  27  ? 11.869  50.441  54.148 1.00 63.21  ? 435  GLU B O     1 
ATOM   156   C  CB    . GLU A  1  27  ? 12.725  47.794  55.919 1.00 47.10  ? 435  GLU B CB    1 
ATOM   157   C  CG    . GLU A  1  27  ? 14.086  47.519  56.496 1.00 43.95  ? 435  GLU B CG    1 
ATOM   158   C  CD    . GLU A  1  27  ? 14.660  46.163  56.035 1.00 48.31  ? 435  GLU B CD    1 
ATOM   159   O  OE1   . GLU A  1  27  ? 15.032  45.320  56.905 1.00 46.27  ? 435  GLU B OE1   1 
ATOM   160   O  OE2   . GLU A  1  27  ? 14.749  45.913  54.811 1.00 41.25  ? 435  GLU B OE2   1 
ATOM   161   N  N     . GLY A  1  28  ? 10.096  49.315  54.935 1.00 60.83  ? 436  GLY B N     1 
ATOM   162   C  CA    . GLY A  1  28  ? 9.251   49.770  53.825 1.00 48.60  ? 436  GLY B CA    1 
ATOM   163   C  C     . GLY A  1  28  ? 7.813   49.818  54.209 1.00 43.37  ? 436  GLY B C     1 
ATOM   164   O  O     . GLY A  1  28  ? 7.488   49.699  55.411 1.00 41.65  ? 436  GLY B O     1 
ATOM   165   N  N     . ASP A  1  29  ? 6.955   50.007  53.203 1.00 40.91  ? 437  ASP B N     1 
ATOM   166   C  CA    . ASP A  1  29  ? 5.543   50.071  53.467 1.00 41.48  ? 437  ASP B CA    1 
ATOM   167   C  C     . ASP A  1  29  ? 5.047   48.712  53.807 1.00 39.38  ? 437  ASP B C     1 
ATOM   168   O  O     . ASP A  1  29  ? 3.953   48.603  54.343 1.00 43.07  ? 437  ASP B O     1 
ATOM   169   C  CB    . ASP A  1  29  ? 4.756   50.627  52.299 1.00 49.72  ? 437  ASP B CB    1 
ATOM   170   C  CG    . ASP A  1  29  ? 4.846   52.160  52.195 1.00 59.84  ? 437  ASP B CG    1 
ATOM   171   O  OD1   . ASP A  1  29  ? 4.974   52.862  53.232 1.00 58.95  ? 437  ASP B OD1   1 
ATOM   172   O  OD2   . ASP A  1  29  ? 4.775   52.668  51.061 1.00 62.78  ? 437  ASP B OD2   1 
ATOM   173   N  N     . SER A  1  30  ? 5.847   47.672  53.534 1.00 36.82  ? 438  SER B N     1 
ATOM   174   C  CA    . SER A  1  30  ? 5.396   46.313  53.810 1.00 42.15  ? 438  SER B CA    1 
ATOM   175   C  C     . SER A  1  30  ? 5.251   46.077  55.311 1.00 45.62  ? 438  SER B C     1 
ATOM   176   O  O     . SER A  1  30  ? 4.276   45.487  55.777 1.00 46.10  ? 438  SER B O     1 
ATOM   177   C  CB    . SER A  1  30  ? 6.319   45.267  53.166 1.00 38.56  ? 438  SER B CB    1 
ATOM   178   O  OG    . SER A  1  30  ? 6.011   45.101  51.774 1.00 39.12  ? 438  SER B OG    1 
ATOM   179   N  N     . ALA A  1  31  ? 6.240   46.541  56.063 1.00 49.11  ? 439  ALA B N     1 
ATOM   180   C  CA    . ALA A  1  31  ? 6.217   46.416  57.496 1.00 51.03  ? 439  ALA B CA    1 
ATOM   181   C  C     . ALA A  1  31  ? 5.413   47.553  58.077 1.00 47.72  ? 439  ALA B C     1 
ATOM   182   O  O     . ALA A  1  31  ? 4.844   47.409  59.121 1.00 44.41  ? 439  ALA B O     1 
ATOM   183   C  CB    . ALA A  1  31  ? 7.629   46.425  58.037 1.00 55.64  ? 439  ALA B CB    1 
ATOM   184   N  N     . GLY A  1  32  ? 5.339   48.670  57.384 1.00 45.90  ? 440  GLY B N     1 
ATOM   185   C  CA    . GLY A  1  32  ? 4.654   49.813  57.932 1.00 49.39  ? 440  GLY B CA    1 
ATOM   186   C  C     . GLY A  1  32  ? 3.187   49.621  58.245 1.00 44.84  ? 440  GLY B C     1 
ATOM   187   O  O     . GLY A  1  32  ? 2.698   50.147  59.203 1.00 53.64  ? 440  GLY B O     1 
ATOM   188   N  N     . GLY A  1  33  ? 2.483   48.927  57.379 1.00 47.48  ? 441  GLY B N     1 
ATOM   189   C  CA    . GLY A  1  33  ? 1.065   48.736  57.552 1.00 45.72  ? 441  GLY B CA    1 
ATOM   190   C  C     . GLY A  1  33  ? 0.797   47.792  58.714 1.00 50.39  ? 441  GLY B C     1 
ATOM   191   O  O     . GLY A  1  33  ? -0.193  47.964  59.409 1.00 55.19  ? 441  GLY B O     1 
ATOM   192   N  N     . SER A  1  34  ? 1.640   46.784  58.928 1.00 45.17  ? 442  SER B N     1 
ATOM   193   C  CA    . SER A  1  34  ? 1.377   45.868  60.023 1.00 46.04  ? 442  SER B CA    1 
ATOM   194   C  C     . SER A  1  34  ? 1.663   46.611  61.338 1.00 48.63  ? 442  SER B C     1 
ATOM   195   O  O     . SER A  1  34  ? 0.945   46.450  62.327 1.00 49.80  ? 442  SER B O     1 
ATOM   196   C  CB    . SER A  1  34  ? 2.269   44.646  59.928 1.00 48.01  ? 442  SER B CB    1 
ATOM   197   O  OG    . SER A  1  34  ? 2.661   44.405  58.597 1.00 56.57  ? 442  SER B OG    1 
ATOM   198   N  N     . THR A  1  35  ? 2.684   47.458  61.288 1.00 42.49  ? 443  THR B N     1 
ATOM   199   C  CA    . THR A  1  35  ? 3.124   48.254  62.385 1.00 40.25  ? 443  THR B CA    1 
ATOM   200   C  C     . THR A  1  35  ? 2.127   49.333  62.788 1.00 38.31  ? 443  THR B C     1 
ATOM   201   O  O     . THR A  1  35  ? 1.941   49.548  63.972 1.00 35.53  ? 443  THR B O     1 
ATOM   202   C  CB    . THR A  1  35  ? 4.476   48.845  61.984 1.00 46.01  ? 443  THR B CB    1 
ATOM   203   O  OG1   . THR A  1  35  ? 5.382   47.752  61.872 1.00 48.57  ? 443  THR B OG1   1 
ATOM   204   C  CG2   . THR A  1  35  ? 5.006   49.644  63.058 1.00 50.27  ? 443  THR B CG2   1 
ATOM   205   N  N     A LYS A  1  36  ? 1.550   50.005  61.796 0.50 34.88  ? 444  LYS B N     1 
ATOM   206   N  N     B LYS A  1  36  ? 1.550   50.009  61.794 0.50 34.53  ? 444  LYS B N     1 
ATOM   207   C  CA    A LYS A  1  36  ? 0.448   50.914  61.999 0.50 41.72  ? 444  LYS B CA    1 
ATOM   208   C  CA    B LYS A  1  36  ? 0.447   50.930  61.980 0.50 41.10  ? 444  LYS B CA    1 
ATOM   209   C  C     A LYS A  1  36  ? -0.736  50.295  62.713 0.50 44.32  ? 444  LYS B C     1 
ATOM   210   C  C     B LYS A  1  36  ? -0.740  50.302  62.701 0.50 43.89  ? 444  LYS B C     1 
ATOM   211   O  O     A LYS A  1  36  ? -1.283  50.921  63.616 0.50 45.68  ? 444  LYS B O     1 
ATOM   212   O  O     B LYS A  1  36  ? -1.278  50.921  63.614 0.50 45.27  ? 444  LYS B O     1 
ATOM   213   C  CB    A LYS A  1  36  ? -0.025  51.480  60.669 0.50 43.63  ? 444  LYS B CB    1 
ATOM   214   C  CB    B LYS A  1  36  ? -0.006  51.513  60.632 0.50 42.36  ? 444  LYS B CB    1 
ATOM   215   C  CG    A LYS A  1  36  ? 0.187   52.969  60.531 0.50 45.30  ? 444  LYS B CG    1 
ATOM   216   C  CG    B LYS A  1  36  ? 0.260   53.001  60.419 0.50 43.15  ? 444  LYS B CG    1 
ATOM   217   C  CD    A LYS A  1  36  ? 0.380   53.385  59.084 0.50 46.77  ? 444  LYS B CD    1 
ATOM   218   C  CD    B LYS A  1  36  ? 0.624   53.390  58.977 0.50 43.61  ? 444  LYS B CD    1 
ATOM   219   C  CE    A LYS A  1  36  ? -0.915  53.957  58.514 0.50 45.83  ? 444  LYS B CE    1 
ATOM   220   C  CE    B LYS A  1  36  ? 2.082   53.848  58.863 0.50 43.92  ? 444  LYS B CE    1 
ATOM   221   N  NZ    A LYS A  1  36  ? -0.631  54.885  57.383 0.50 44.34  ? 444  LYS B NZ    1 
ATOM   222   N  NZ    B LYS A  1  36  ? 2.419   54.696  57.679 0.50 37.21  ? 444  LYS B NZ    1 
ATOM   223   N  N     . SER A  1  37  ? -1.120  49.090  62.293 1.00 44.99  ? 445  SER B N     1 
ATOM   224   C  CA    . SER A  1  37  ? -2.208  48.359  62.891 1.00 51.65  ? 445  SER B CA    1 
ATOM   225   C  C     . SER A  1  37  ? -1.929  47.815  64.273 1.00 55.17  ? 445  SER B C     1 
ATOM   226   O  O     . SER A  1  37  ? -2.815  47.826  65.143 1.00 52.09  ? 445  SER B O     1 
ATOM   227   C  CB    . SER A  1  37  ? -2.599  47.222  61.981 1.00 52.85  ? 445  SER B CB    1 
ATOM   228   O  OG    . SER A  1  37  ? -3.422  47.719  60.972 1.00 57.38  ? 445  SER B OG    1 
ATOM   229   N  N     . GLY A  1  38  ? -0.709  47.336  64.481 1.00 51.55  ? 446  GLY B N     1 
ATOM   230   C  CA    . GLY A  1  38  ? -0.439  46.655  65.714 1.00 42.19  ? 446  GLY B CA    1 
ATOM   231   C  C     . GLY A  1  38  ? -0.088  47.606  66.846 1.00 47.15  ? 446  GLY B C     1 
ATOM   232   O  O     . GLY A  1  38  ? -0.219  47.261  68.009 1.00 47.49  ? 446  GLY B O     1 
ATOM   233   N  N     . ARG A  1  39  ? 0.379   48.808  66.526 1.00 45.62  ? 447  ARG B N     1 
ATOM   234   C  CA    . ARG A  1  39  ? 0.914   49.704  67.543 1.00 44.99  ? 447  ARG B CA    1 
ATOM   235   C  C     . ARG A  1  39  ? -0.129  50.292  68.496 1.00 47.95  ? 447  ARG B C     1 
ATOM   236   O  O     . ARG A  1  39  ? -1.340  50.248  68.229 1.00 43.75  ? 447  ARG B O     1 
ATOM   237   C  CB    . ARG A  1  39  ? 1.579   50.861  66.837 1.00 40.56  ? 447  ARG B CB    1 
ATOM   238   C  CG    . ARG A  1  39  ? 0.600   51.955  66.503 1.00 38.99  ? 447  ARG B CG    1 
ATOM   239   C  CD    . ARG A  1  39  ? 1.179   53.000  65.637 1.00 42.50  ? 447  ARG B CD    1 
ATOM   240   N  NE    . ARG A  1  39  ? 0.133   53.522  64.775 1.00 46.00  ? 447  ARG B NE    1 
ATOM   241   C  CZ    . ARG A  1  39  ? 0.003   54.799  64.487 1.00 42.38  ? 447  ARG B CZ    1 
ATOM   242   N  NH1   . ARG A  1  39  ? -0.958  55.210  63.709 1.00 39.49  ? 447  ARG B NH1   1 
ATOM   243   N  NH2   . ARG A  1  39  ? 0.833   55.670  65.012 1.00 42.81  ? 447  ARG B NH2   1 
ATOM   244   N  N     . ASP A  1  40  ? 0.361   50.868  69.587 1.00 46.46  ? 448  ASP B N     1 
ATOM   245   C  CA    . ASP A  1  40  ? -0.420  51.760  70.386 1.00 48.90  ? 448  ASP B CA    1 
ATOM   246   C  C     . ASP A  1  40  ? -0.313  53.146  69.796 1.00 45.91  ? 448  ASP B C     1 
ATOM   247   O  O     . ASP A  1  40  ? 0.676   53.805  70.003 1.00 45.69  ? 448  ASP B O     1 
ATOM   248   C  CB    . ASP A  1  40  ? 0.211   51.798  71.765 1.00 57.63  ? 448  ASP B CB    1 
ATOM   249   C  CG    . ASP A  1  40  ? -0.631  52.522  72.779 1.00 58.37  ? 448  ASP B CG    1 
ATOM   250   O  OD1   . ASP A  1  40  ? -1.516  53.323  72.413 1.00 55.68  ? 448  ASP B OD1   1 
ATOM   251   O  OD2   . ASP A  1  40  ? -0.382  52.293  73.969 1.00 61.03  ? 448  ASP B OD2   1 
ATOM   252   N  N     . SER A  1  41  ? -1.336  53.599  69.095 1.00 45.66  ? 449  SER B N     1 
ATOM   253   C  CA    . SER A  1  41  ? -1.283  54.901  68.396 1.00 44.63  ? 449  SER B CA    1 
ATOM   254   C  C     . SER A  1  41  ? -1.247  56.108  69.291 1.00 47.04  ? 449  SER B C     1 
ATOM   255   O  O     . SER A  1  41  ? -1.041  57.194  68.817 1.00 48.58  ? 449  SER B O     1 
ATOM   256   C  CB    . SER A  1  41  ? -2.455  55.032  67.423 1.00 44.99  ? 449  SER B CB    1 
ATOM   257   O  OG    . SER A  1  41  ? -3.631  55.313  68.143 1.00 49.05  ? 449  SER B OG    1 
ATOM   258   N  N     . ARG A  1  42  ? -1.492  55.928  70.574 1.00 47.42  ? 450  ARG B N     1 
ATOM   259   C  CA    . ARG A  1  42  ? -1.396  57.017  71.487 1.00 51.87  ? 450  ARG B CA    1 
ATOM   260   C  C     . ARG A  1  42  ? 0.046   57.432  71.706 1.00 53.61  ? 450  ARG B C     1 
ATOM   261   O  O     . ARG A  1  42  ? 0.327   58.595  71.873 1.00 53.99  ? 450  ARG B O     1 
ATOM   262   C  CB    . ARG A  1  42  ? -2.050  56.642  72.802 1.00 51.99  ? 450  ARG B CB    1 
ATOM   263   C  CG    . ARG A  1  42  ? -2.430  57.859  73.620 1.00 59.06  ? 450  ARG B CG    1 
ATOM   264   C  CD    . ARG A  1  42  ? -2.822  57.495  75.064 1.00 59.08  ? 450  ARG B CD    1 
ATOM   265   N  NE    . ARG A  1  42  ? -1.699  57.041  75.914 1.00 62.81  ? 450  ARG B NE    1 
ATOM   266   C  CZ    . ARG A  1  42  ? -0.861  57.858  76.559 1.00 55.42  ? 450  ARG B CZ    1 
ATOM   267   N  NH1   . ARG A  1  42  ? -0.993  59.189  76.450 1.00 49.62  ? 450  ARG B NH1   1 
ATOM   268   N  NH2   . ARG A  1  42  ? 0.108   57.340  77.311 1.00 47.63  ? 450  ARG B NH2   1 
ATOM   269   N  N     . THR A  1  43  ? 0.962   56.482  71.720 1.00 53.44  ? 451  THR B N     1 
ATOM   270   C  CA    . THR A  1  43  ? 2.348   56.837  72.039 1.00 52.39  ? 451  THR B CA    1 
ATOM   271   C  C     . THR A  1  43  ? 3.382   56.331  71.032 1.00 53.30  ? 451  THR B C     1 
ATOM   272   O  O     . THR A  1  43  ? 4.581   56.507  71.231 1.00 48.71  ? 451  THR B O     1 
ATOM   273   C  CB    . THR A  1  43  ? 2.762   56.272  73.416 1.00 49.03  ? 451  THR B CB    1 
ATOM   274   O  OG1   . THR A  1  43  ? 2.443   54.883  73.457 1.00 48.02  ? 451  THR B OG1   1 
ATOM   275   C  CG2   . THR A  1  43  ? 2.076   56.972  74.529 1.00 45.07  ? 451  THR B CG2   1 
ATOM   276   N  N     . GLN A  1  44  ? 2.936   55.656  69.985 1.00 49.06  ? 452  GLN B N     1 
ATOM   277   C  CA    . GLN A  1  44  ? 3.872   55.036  69.057 1.00 42.67  ? 452  GLN B CA    1 
ATOM   278   C  C     . GLN A  1  44  ? 3.627   55.597  67.682 1.00 44.87  ? 452  GLN B C     1 
ATOM   279   O  O     . GLN A  1  44  ? 2.543   55.451  67.129 1.00 41.82  ? 452  GLN B O     1 
ATOM   280   C  CB    . GLN A  1  44  ? 3.734   53.515  69.115 1.00 38.08  ? 452  GLN B CB    1 
ATOM   281   C  CG    . GLN A  1  44  ? 4.132   52.950  70.483 1.00 38.31  ? 452  GLN B CG    1 
ATOM   282   C  CD    . GLN A  1  44  ? 4.029   51.436  70.569 1.00 42.28  ? 452  GLN B CD    1 
ATOM   283   O  OE1   . GLN A  1  44  ? 3.214   50.808  69.878 1.00 43.33  ? 452  GLN B OE1   1 
ATOM   284   N  NE2   . GLN A  1  44  ? 4.892   50.828  71.400 1.00 39.32  ? 452  GLN B NE2   1 
ATOM   285   N  N     . ALA A  1  45  ? 4.628   56.290  67.146 1.00 44.32  ? 453  ALA B N     1 
ATOM   286   C  CA    . ALA A  1  45  ? 4.568   56.818  65.773 1.00 40.39  ? 453  ALA B CA    1 
ATOM   287   C  C     . ALA A  1  45  ? 5.324   55.854  64.840 1.00 41.96  ? 453  ALA B C     1 
ATOM   288   O  O     . ALA A  1  45  ? 6.237   55.128  65.299 1.00 37.55  ? 453  ALA B O     1 
ATOM   289   C  CB    . ALA A  1  45  ? 5.190   58.204  65.731 1.00 35.31  ? 453  ALA B CB    1 
ATOM   290   N  N     . ILE A  1  46  ? 4.978   55.821  63.547 1.00 39.21  ? 454  ILE B N     1 
ATOM   291   C  CA    . ILE A  1  46  ? 5.680   54.954  62.608 1.00 36.80  ? 454  ILE B CA    1 
ATOM   292   C  C     . ILE A  1  46  ? 6.220   55.700  61.385 1.00 40.89  ? 454  ILE B C     1 
ATOM   293   O  O     . ILE A  1  46  ? 5.460   56.373  60.671 1.00 39.26  ? 454  ILE B O     1 
ATOM   294   C  CB    . ILE A  1  46  ? 4.818   53.797  62.045 1.00 42.36  ? 454  ILE B CB    1 
ATOM   295   C  CG1   . ILE A  1  46  ? 4.069   53.017  63.124 1.00 41.21  ? 454  ILE B CG1   1 
ATOM   296   C  CG2   . ILE A  1  46  ? 5.673   52.892  61.128 1.00 36.05  ? 454  ILE B CG2   1 
ATOM   297   C  CD1   . ILE A  1  46  ? 4.924   52.095  63.969 1.00 43.86  ? 454  ILE B CD1   1 
ATOM   298   N  N     . LEU A  1  47  ? 7.522   55.558  61.115 1.00 36.62  ? 455  LEU B N     1 
ATOM   299   C  CA    . LEU A  1  47  ? 8.069   56.172  59.926 1.00 36.90  ? 455  LEU B CA    1 
ATOM   300   C  C     . LEU A  1  47  ? 8.650   55.109  58.974 1.00 42.99  ? 455  LEU B C     1 
ATOM   301   O  O     . LEU A  1  47  ? 9.799   54.638  59.187 1.00 39.92  ? 455  LEU B O     1 
ATOM   302   C  CB    . LEU A  1  47  ? 9.083   57.251  60.310 1.00 36.31  ? 455  LEU B CB    1 
ATOM   303   C  CG    . LEU A  1  47  ? 9.781   57.936  59.134 1.00 37.82  ? 455  LEU B CG    1 
ATOM   304   C  CD1   . LEU A  1  47  ? 8.762   58.523  58.168 1.00 43.78  ? 455  LEU B CD1   1 
ATOM   305   C  CD2   . LEU A  1  47  ? 10.780  58.978  59.596 1.00 33.96  ? 455  LEU B CD2   1 
ATOM   306   N  N     . PRO A  1  48  ? 7.873   54.715  57.938 1.00 42.74  ? 456  PRO B N     1 
ATOM   307   C  CA    . PRO A  1  48  ? 8.510   53.764  57.004 1.00 44.90  ? 456  PRO B CA    1 
ATOM   308   C  C     . PRO A  1  48  ? 9.627   54.367  56.165 1.00 40.65  ? 456  PRO B C     1 
ATOM   309   O  O     . PRO A  1  48  ? 9.477   55.462  55.663 1.00 39.03  ? 456  PRO B O     1 
ATOM   310   C  CB    . PRO A  1  48  ? 7.368   53.357  56.042 1.00 42.39  ? 456  PRO B CB    1 
ATOM   311   C  CG    . PRO A  1  48  ? 6.100   53.847  56.698 1.00 51.45  ? 456  PRO B CG    1 
ATOM   312   C  CD    . PRO A  1  48  ? 6.513   55.064  57.469 1.00 46.62  ? 456  PRO B CD    1 
ATOM   313   N  N     . LEU A  1  49  ? 10.726  53.628  55.991 1.00 41.79  ? 457  LEU B N     1 
ATOM   314   C  CA    . LEU A  1  49  ? 11.824  54.066  55.114 1.00 49.47  ? 457  LEU B CA    1 
ATOM   315   C  C     . LEU A  1  49  ? 11.629  53.553  53.666 1.00 52.60  ? 457  LEU B C     1 
ATOM   316   O  O     . LEU A  1  49  ? 10.601  52.999  53.349 1.00 64.96  ? 457  LEU B O     1 
ATOM   317   C  CB    . LEU A  1  49  ? 13.153  53.604  55.692 1.00 53.10  ? 457  LEU B CB    1 
ATOM   318   C  CG    . LEU A  1  49  ? 13.486  54.140  57.083 1.00 53.30  ? 457  LEU B CG    1 
ATOM   319   C  CD1   . LEU A  1  49  ? 14.871  53.672  57.498 1.00 61.30  ? 457  LEU B CD1   1 
ATOM   320   C  CD2   . LEU A  1  49  ? 13.411  55.648  57.054 1.00 51.64  ? 457  LEU B CD2   1 
ATOM   321   N  N     . ARG A  1  50  ? 12.594  53.753  52.786 1.00 54.49  ? 458  ARG B N     1 
ATOM   322   C  CA    . ARG A  1  50  ? 12.489  53.272  51.406 1.00 50.08  ? 458  ARG B CA    1 
ATOM   323   C  C     . ARG A  1  50  ? 13.702  52.413  51.040 1.00 51.07  ? 458  ARG B C     1 
ATOM   324   O  O     . ARG A  1  50  ? 14.527  52.777  50.183 1.00 53.54  ? 458  ARG B O     1 
ATOM   325   C  CB    . ARG A  1  50  ? 12.317  54.461  50.464 1.00 50.61  ? 458  ARG B CB    1 
ATOM   326   C  CG    . ARG A  1  50  ? 10.903  54.600  49.939 1.00 64.28  ? 458  ARG B CG    1 
ATOM   327   C  CD    . ARG A  1  50  ? 10.516  56.031  49.678 1.00 66.71  ? 458  ARG B CD    1 
ATOM   328   N  NE    . ARG A  1  50  ? 9.899   56.122  48.370 1.00 80.81  ? 458  ARG B NE    1 
ATOM   329   C  CZ    . ARG A  1  50  ? 9.170   57.146  47.937 1.00 85.07  ? 458  ARG B CZ    1 
ATOM   330   N  NH1   . ARG A  1  50  ? 8.951   58.219  48.703 1.00 84.78  ? 458  ARG B NH1   1 
ATOM   331   N  NH2   . ARG A  1  50  ? 8.657   57.086  46.720 1.00 92.08  ? 458  ARG B NH2   1 
ATOM   332   N  N     . GLY A  1  51  ? 13.834  51.292  51.737 1.00 41.47  ? 459  GLY B N     1 
ATOM   333   C  CA    . GLY A  1  51  ? 14.947  50.386  51.526 1.00 38.39  ? 459  GLY B CA    1 
ATOM   334   C  C     . GLY A  1  51  ? 16.271  50.933  51.965 1.00 40.14  ? 459  GLY B C     1 
ATOM   335   O  O     . GLY A  1  51  ? 16.349  51.552  53.027 1.00 43.50  ? 459  GLY B O     1 
ATOM   336   N  N     . LYS A  1  52  ? 17.309  50.729  51.160 1.00 32.06  ? 460  LYS B N     1 
ATOM   337   C  CA    . LYS A  1  52  ? 18.624  51.163  51.584 1.00 31.60  ? 460  LYS B CA    1 
ATOM   338   C  C     . LYS A  1  52  ? 18.608  52.659  51.580 1.00 32.24  ? 460  LYS B C     1 
ATOM   339   O  O     . LYS A  1  52  ? 18.058  53.246  50.689 1.00 32.76  ? 460  LYS B O     1 
ATOM   340   C  CB    . LYS A  1  52  ? 19.707  50.644  50.645 1.00 31.07  ? 460  LYS B CB    1 
ATOM   341   C  CG    . LYS A  1  52  ? 19.731  49.117  50.522 1.00 29.77  ? 460  LYS B CG    1 
ATOM   342   C  CD    . LYS A  1  52  ? 20.528  48.570  51.665 1.00 29.15  ? 460  LYS B CD    1 
ATOM   343   C  CE    . LYS A  1  52  ? 20.205  47.124  51.974 1.00 25.51  ? 460  LYS B CE    1 
ATOM   344   N  NZ    . LYS A  1  52  ? 21.373  46.320  51.483 1.00 22.24  ? 460  LYS B NZ    1 
ATOM   345   N  N     . ILE A  1  53  ? 19.243  53.234  52.586 1.00 32.51  ? 461  ILE B N     1 
ATOM   346   C  CA    . ILE A  1  53  ? 19.316  54.670  52.922 1.00 34.53  ? 461  ILE B CA    1 
ATOM   347   C  C     . ILE A  1  53  ? 20.688  55.235  52.518 1.00 31.33  ? 461  ILE B C     1 
ATOM   348   O  O     . ILE A  1  53  ? 21.690  54.501  52.483 1.00 28.83  ? 461  ILE B O     1 
ATOM   349   C  CB    . ILE A  1  53  ? 19.192  54.732  54.485 1.00 38.07  ? 461  ILE B CB    1 
ATOM   350   C  CG1   . ILE A  1  53  ? 17.722  54.636  54.851 1.00 45.82  ? 461  ILE B CG1   1 
ATOM   351   C  CG2   . ILE A  1  53  ? 19.803  55.962  55.138 1.00 39.88  ? 461  ILE B CG2   1 
ATOM   352   C  CD1   . ILE A  1  53  ? 16.964  55.932  54.699 1.00 49.02  ? 461  ILE B CD1   1 
ATOM   353   N  N     . LEU A  1  54  ? 20.758  56.532  52.286 1.00 34.36  ? 462  LEU B N     1 
ATOM   354   C  CA    . LEU A  1  54  ? 22.018  57.146  51.991 1.00 31.92  ? 462  LEU B CA    1 
ATOM   355   C  C     . LEU A  1  54  ? 23.100  56.910  53.009 1.00 29.38  ? 462  LEU B C     1 
ATOM   356   O  O     . LEU A  1  54  ? 22.844  57.042  54.208 1.00 32.50  ? 462  LEU B O     1 
ATOM   357   C  CB    . LEU A  1  54  ? 21.801  58.632  51.761 1.00 34.12  ? 462  LEU B CB    1 
ATOM   358   C  CG    . LEU A  1  54  ? 22.965  59.472  51.187 1.00 34.16  ? 462  LEU B CG    1 
ATOM   359   C  CD1   . LEU A  1  54  ? 23.282  59.145  49.723 1.00 33.23  ? 462  LEU B CD1   1 
ATOM   360   C  CD2   . LEU A  1  54  ? 22.487  60.912  51.325 1.00 36.70  ? 462  LEU B CD2   1 
ATOM   361   N  N     . ASN A  1  55  ? 24.302  56.581  52.552 1.00 30.25  ? 463  ASN B N     1 
ATOM   362   C  CA    . ASN A  1  55  ? 25.417  56.441  53.481 1.00 31.83  ? 463  ASN B CA    1 
ATOM   363   C  C     . ASN A  1  55  ? 25.968  57.846  53.611 1.00 34.04  ? 463  ASN B C     1 
ATOM   364   O  O     . ASN A  1  55  ? 26.576  58.336  52.679 1.00 35.36  ? 463  ASN B O     1 
ATOM   365   C  CB    . ASN A  1  55  ? 26.483  55.531  52.892 1.00 28.16  ? 463  ASN B CB    1 
ATOM   366   C  CG    . ASN A  1  55  ? 27.645  55.316  53.845 1.00 32.43  ? 463  ASN B CG    1 
ATOM   367   O  OD1   . ASN A  1  55  ? 27.883  56.112  54.725 1.00 29.35  ? 463  ASN B OD1   1 
ATOM   368   N  ND2   . ASN A  1  55  ? 28.362  54.202  53.691 1.00 33.20  ? 463  ASN B ND2   1 
ATOM   369   N  N     . VAL A  1  56  ? 25.755  58.474  54.748 1.00 34.21  ? 464  VAL B N     1 
ATOM   370   C  CA    . VAL A  1  56  ? 26.181  59.883  54.912 1.00 38.50  ? 464  VAL B CA    1 
ATOM   371   C  C     . VAL A  1  56  ? 27.693  59.985  55.077 1.00 37.81  ? 464  VAL B C     1 
ATOM   372   O  O     . VAL A  1  56  ? 28.277  61.044  54.878 1.00 38.37  ? 464  VAL B O     1 
ATOM   373   C  CB    . VAL A  1  56  ? 25.452  60.610  56.088 1.00 35.72  ? 464  VAL B CB    1 
ATOM   374   C  CG1   . VAL A  1  56  ? 23.969  60.667  55.800 1.00 33.71  ? 464  VAL B CG1   1 
ATOM   375   C  CG2   . VAL A  1  56  ? 25.756  59.946  57.441 1.00 32.76  ? 464  VAL B CG2   1 
ATOM   376   N  N     . GLU A  1  57  ? 28.323  58.874  55.417 1.00 39.50  ? 465  GLU B N     1 
ATOM   377   C  CA    . GLU A  1  57  ? 29.778  58.835  55.575 1.00 35.14  ? 465  GLU B CA    1 
ATOM   378   C  C     . GLU A  1  57  ? 30.467  59.008  54.217 1.00 40.87  ? 465  GLU B C     1 
ATOM   379   O  O     . GLU A  1  57  ? 31.573  59.520  54.169 1.00 43.01  ? 465  GLU B O     1 
ATOM   380   C  CB    . GLU A  1  57  ? 30.218  57.526  56.209 1.00 38.49  ? 465  GLU B CB    1 
ATOM   381   C  CG    . GLU A  1  57  ? 31.640  57.520  56.728 1.00 41.56  ? 465  GLU B CG    1 
ATOM   382   C  CD    . GLU A  1  57  ? 31.800  58.295  58.035 1.00 42.80  ? 465  GLU B CD    1 
ATOM   383   O  OE1   . GLU A  1  57  ? 32.938  58.482  58.498 1.00 41.92  ? 465  GLU B OE1   1 
ATOM   384   O  OE2   . GLU A  1  57  ? 30.782  58.767  58.572 1.00 38.98  ? 465  GLU B OE2   1 
ATOM   385   N  N     . LYS A  1  58  ? 29.810  58.624  53.128 1.00 37.49  ? 466  LYS B N     1 
ATOM   386   C  CA    . LYS A  1  58  ? 30.402  58.782  51.816 1.00 37.87  ? 466  LYS B CA    1 
ATOM   387   C  C     . LYS A  1  58  ? 29.833  59.948  51.041 1.00 41.33  ? 466  LYS B C     1 
ATOM   388   O  O     . LYS A  1  58  ? 30.291  60.228  49.960 1.00 45.86  ? 466  LYS B O     1 
ATOM   389   C  CB    . LYS A  1  58  ? 30.220  57.489  50.978 1.00 33.32  ? 466  LYS B CB    1 
ATOM   390   C  CG    . LYS A  1  58  ? 31.006  56.304  51.494 1.00 30.25  ? 466  LYS B CG    1 
ATOM   391   C  CD    . LYS A  1  58  ? 30.685  55.076  50.651 1.00 30.29  ? 466  LYS B CD    1 
ATOM   392   C  CE    . LYS A  1  58  ? 31.489  53.884  51.167 1.00 27.23  ? 466  LYS B CE    1 
ATOM   393   N  NZ    . LYS A  1  58  ? 30.978  52.591  50.689 1.00 29.57  ? 466  LYS B NZ    1 
ATOM   394   N  N     . ALA A  1  59  ? 28.823  60.616  51.571 1.00 40.59  ? 467  ALA B N     1 
ATOM   395   C  CA    . ALA A  1  59  ? 28.169  61.664  50.803 1.00 39.41  ? 467  ALA B CA    1 
ATOM   396   C  C     . ALA A  1  59  ? 28.497  63.068  51.307 1.00 36.05  ? 467  ALA B C     1 
ATOM   397   O  O     . ALA A  1  59  ? 28.608  63.317  52.489 1.00 46.15  ? 467  ALA B O     1 
ATOM   398   C  CB    . ALA A  1  59  ? 26.648  61.423  50.749 1.00 33.65  ? 467  ALA B CB    1 
ATOM   399   N  N     . ARG A  1  60  ? 28.618  63.968  50.364 1.00 38.77  ? 468  ARG B N     1 
ATOM   400   C  CA    . ARG A  1  60  ? 28.734  65.406  50.641 1.00 42.83  ? 468  ARG B CA    1 
ATOM   401   C  C     . ARG A  1  60  ? 27.402  66.001  51.129 1.00 43.49  ? 468  ARG B C     1 
ATOM   402   O  O     . ARG A  1  60  ? 26.339  65.469  50.819 1.00 42.01  ? 468  ARG B O     1 
ATOM   403   C  CB    . ARG A  1  60  ? 29.211  66.106  49.372 1.00 40.20  ? 468  ARG B CB    1 
ATOM   404   C  CG    . ARG A  1  60  ? 30.607  65.638  49.018 1.00 37.29  ? 468  ARG B CG    1 
ATOM   405   C  CD    . ARG A  1  60  ? 31.174  66.308  47.782 1.00 37.28  ? 468  ARG B CD    1 
ATOM   406   N  NE    . ARG A  1  60  ? 32.593  65.951  47.667 1.00 35.20  ? 468  ARG B NE    1 
ATOM   407   C  CZ    . ARG A  1  60  ? 33.597  66.569  48.274 1.00 36.23  ? 468  ARG B CZ    1 
ATOM   408   N  NH1   . ARG A  1  60  ? 34.815  66.080  48.068 1.00 35.93  ? 468  ARG B NH1   1 
ATOM   409   N  NH2   . ARG A  1  60  ? 33.426  67.661  49.064 1.00 35.95  ? 468  ARG B NH2   1 
ATOM   410   N  N     . LEU A  1  61  ? 27.474  67.098  51.864 1.00 42.39  ? 469  LEU B N     1 
ATOM   411   C  CA    . LEU A  1  61  ? 26.308  67.679  52.486 1.00 43.43  ? 469  LEU B CA    1 
ATOM   412   C  C     . LEU A  1  61  ? 25.157  68.028  51.544 1.00 40.59  ? 469  LEU B C     1 
ATOM   413   O  O     . LEU A  1  61  ? 24.021  67.826  51.910 1.00 42.29  ? 469  LEU B O     1 
ATOM   414   C  CB    . LEU A  1  61  ? 26.709  68.891  53.306 1.00 44.89  ? 469  LEU B CB    1 
ATOM   415   C  CG    . LEU A  1  61  ? 25.609  69.353  54.281 1.00 46.86  ? 469  LEU B CG    1 
ATOM   416   C  CD1   . LEU A  1  61  ? 25.488  68.503  55.551 1.00 39.31  ? 469  LEU B CD1   1 
ATOM   417   C  CD2   . LEU A  1  61  ? 25.861  70.813  54.643 1.00 40.38  ? 469  LEU B CD2   1 
ATOM   418   N  N     . ASP A  1  62  ? 25.435  68.527  50.336 1.00 35.82  ? 470  ASP B N     1 
ATOM   419   C  CA    . ASP A  1  62  ? 24.323  68.925  49.465 1.00 36.19  ? 470  ASP B CA    1 
ATOM   420   C  C     . ASP A  1  62  ? 23.443  67.710  49.158 1.00 42.04  ? 470  ASP B C     1 
ATOM   421   O  O     . ASP A  1  62  ? 22.213  67.811  49.142 1.00 38.87  ? 470  ASP B O     1 
ATOM   422   C  CB    . ASP A  1  62  ? 24.784  69.598  48.172 1.00 41.50  ? 470  ASP B CB    1 
ATOM   423   C  CG    . ASP A  1  62  ? 25.515  68.619  47.218 1.00 57.43  ? 470  ASP B CG    1 
ATOM   424   O  OD1   . ASP A  1  62  ? 26.206  67.635  47.654 1.00 53.31  ? 470  ASP B OD1   1 
ATOM   425   O  OD2   . ASP A  1  62  ? 25.356  68.812  46.002 1.00 59.68  ? 470  ASP B OD2   1 
ATOM   426   N  N     . ARG A  1  63  ? 24.057  66.551  48.925 1.00 40.74  ? 471  ARG B N     1 
ATOM   427   C  CA    . ARG A  1  63  ? 23.306  65.348  48.621 1.00 39.05  ? 471  ARG B CA    1 
ATOM   428   C  C     . ARG A  1  63  ? 22.569  64.864  49.872 1.00 38.37  ? 471  ARG B C     1 
ATOM   429   O  O     . ARG A  1  63  ? 21.396  64.446  49.763 1.00 31.82  ? 471  ARG B O     1 
ATOM   430   C  CB    . ARG A  1  63  ? 24.253  64.277  48.111 1.00 43.61  ? 471  ARG B CB    1 
ATOM   431   C  CG    . ARG A  1  63  ? 23.578  63.082  47.499 1.00 47.05  ? 471  ARG B CG    1 
ATOM   432   C  CD    . ARG A  1  63  ? 24.634  62.140  46.949 1.00 49.24  ? 471  ARG B CD    1 
ATOM   433   N  NE    . ARG A  1  63  ? 24.068  60.845  46.594 1.00 56.72  ? 471  ARG B NE    1 
ATOM   434   C  CZ    . ARG A  1  63  ? 24.765  59.716  46.603 1.00 60.51  ? 471  ARG B CZ    1 
ATOM   435   N  NH1   . ARG A  1  63  ? 26.050  59.731  46.972 1.00 64.51  ? 471  ARG B NH1   1 
ATOM   436   N  NH2   . ARG A  1  63  ? 24.165  58.581  46.276 1.00 56.29  ? 471  ARG B NH2   1 
ATOM   437   N  N     . ILE A  1  64  ? 23.221  64.947  51.042 1.00 32.30  ? 472  ILE B N     1 
ATOM   438   C  CA    . ILE A  1  64  ? 22.547  64.535  52.286 1.00 32.87  ? 472  ILE B CA    1 
ATOM   439   C  C     . ILE A  1  64  ? 21.253  65.301  52.544 1.00 42.64  ? 472  ILE B C     1 
ATOM   440   O  O     . ILE A  1  64  ? 20.227  64.726  52.852 1.00 45.72  ? 472  ILE B O     1 
ATOM   441   C  CB    . ILE A  1  64  ? 23.492  64.611  53.504 1.00 29.67  ? 472  ILE B CB    1 
ATOM   442   C  CG1   . ILE A  1  64  ? 24.682  63.662  53.322 1.00 27.83  ? 472  ILE B CG1   1 
ATOM   443   C  CG2   . ILE A  1  64  ? 22.755  64.349  54.805 1.00 27.58  ? 472  ILE B CG2   1 
ATOM   444   C  CD1   . ILE A  1  64  ? 25.813  63.829  54.317 1.00 30.69  ? 472  ILE B CD1   1 
ATOM   445   N  N     . LEU A  1  65  ? 21.357  66.625  52.462 1.00 48.62  ? 473  LEU B N     1 
ATOM   446   C  CA    . LEU A  1  65  ? 20.261  67.543  52.766 1.00 43.57  ? 473  LEU B CA    1 
ATOM   447   C  C     . LEU A  1  65  ? 19.124  67.425  51.782 1.00 43.10  ? 473  LEU B C     1 
ATOM   448   O  O     . LEU A  1  65  ? 17.993  67.664  52.132 1.00 48.20  ? 473  LEU B O     1 
ATOM   449   C  CB    . LEU A  1  65  ? 20.787  68.985  52.835 1.00 41.22  ? 473  LEU B CB    1 
ATOM   450   C  CG    . LEU A  1  65  ? 21.654  69.227  54.067 1.00 44.49  ? 473  LEU B CG    1 
ATOM   451   C  CD1   . LEU A  1  65  ? 21.906  70.705  54.313 1.00 47.08  ? 473  LEU B CD1   1 
ATOM   452   C  CD2   . LEU A  1  65  ? 21.044  68.565  55.293 1.00 40.91  ? 473  LEU B CD2   1 
ATOM   453   N  N     . ASN A  1  66  ? 19.427  67.049  50.546 1.00 43.12  ? 474  ASN B N     1 
ATOM   454   C  CA    . ASN A  1  66  ? 18.394  66.907  49.547 1.00 44.42  ? 474  ASN B CA    1 
ATOM   455   C  C     . ASN A  1  66  ? 17.752  65.526  49.448 1.00 45.05  ? 474  ASN B C     1 
ATOM   456   O  O     . ASN A  1  66  ? 16.830  65.332  48.654 1.00 46.51  ? 474  ASN B O     1 
ATOM   457   C  CB    . ASN A  1  66  ? 18.868  67.435  48.207 1.00 52.51  ? 474  ASN B CB    1 
ATOM   458   C  CG    . ASN A  1  66  ? 18.972  68.967  48.219 1.00 64.58  ? 474  ASN B CG    1 
ATOM   459   O  OD1   . ASN A  1  66  ? 18.046  69.677  47.790 1.00 76.09  ? 474  ASN B OD1   1 
ATOM   460   N  ND2   . ASN A  1  66  ? 20.075  69.482  48.784 1.00 63.95  ? 474  ASN B ND2   1 
ATOM   461   N  N     . ASN A  1  67  ? 18.193  64.598  50.290 1.00 39.69  ? 475  ASN B N     1 
ATOM   462   C  CA    . ASN A  1  67  ? 17.647  63.245  50.304 1.00 39.33  ? 475  ASN B CA    1 
ATOM   463   C  C     . ASN A  1  67  ? 16.319  63.198  51.078 1.00 37.47  ? 475  ASN B C     1 
ATOM   464   O  O     . ASN A  1  67  ? 16.241  63.631  52.216 1.00 40.69  ? 475  ASN B O     1 
ATOM   465   C  CB    . ASN A  1  67  ? 18.668  62.298  50.947 1.00 36.16  ? 475  ASN B CB    1 
ATOM   466   C  CG    . ASN A  1  67  ? 18.222  60.866  50.883 1.00 39.10  ? 475  ASN B CG    1 
ATOM   467   O  OD1   . ASN A  1  67  ? 17.631  60.322  51.826 1.00 36.04  ? 475  ASN B OD1   1 
ATOM   468   N  ND2   . ASN A  1  67  ? 18.495  60.244  49.749 1.00 35.44  ? 475  ASN B ND2   1 
ATOM   469   N  N     . ASN A  1  68  ? 15.290  62.657  50.468 1.00 42.06  ? 476  ASN B N     1 
ATOM   470   C  CA    . ASN A  1  68  ? 13.954  62.654  51.089 1.00 45.96  ? 476  ASN B CA    1 
ATOM   471   C  C     . ASN A  1  68  ? 13.843  61.840  52.359 1.00 48.10  ? 476  ASN B C     1 
ATOM   472   O  O     . ASN A  1  68  ? 13.119  62.209  53.248 1.00 47.53  ? 476  ASN B O     1 
ATOM   473   C  CB    . ASN A  1  68  ? 12.880  62.199  50.114 1.00 55.17  ? 476  ASN B CB    1 
ATOM   474   C  CG    . ASN A  1  68  ? 12.893  63.020  48.852 1.00 66.67  ? 476  ASN B CG    1 
ATOM   475   O  OD1   . ASN A  1  68  ? 12.411  64.168  48.818 1.00 71.42  ? 476  ASN B OD1   1 
ATOM   476   N  ND2   . ASN A  1  68  ? 13.508  62.463  47.812 1.00 72.28  ? 476  ASN B ND2   1 
ATOM   477   N  N     . GLU A  1  69  ? 14.576  60.739  52.449 1.00 50.34  ? 477  GLU B N     1 
ATOM   478   C  CA    . GLU A  1  69  ? 14.559  59.921  53.662 1.00 47.08  ? 477  GLU B CA    1 
ATOM   479   C  C     . GLU A  1  69  ? 15.220  60.614  54.837 1.00 42.88  ? 477  GLU B C     1 
ATOM   480   O  O     . GLU A  1  69  ? 14.719  60.547  55.957 1.00 43.24  ? 477  GLU B O     1 
ATOM   481   C  CB    . GLU A  1  69  ? 15.240  58.570  53.411 1.00 53.65  ? 477  GLU B CB    1 
ATOM   482   C  CG    . GLU A  1  69  ? 14.290  57.437  53.056 1.00 62.76  ? 477  GLU B CG    1 
ATOM   483   C  CD    . GLU A  1  69  ? 13.457  57.754  51.843 1.00 74.38  ? 477  GLU B CD    1 
ATOM   484   O  OE1   . GLU A  1  69  ? 14.052  57.987  50.753 1.00 81.52  ? 477  GLU B OE1   1 
ATOM   485   O  OE2   . GLU A  1  69  ? 12.213  57.775  51.984 1.00 75.01  ? 477  GLU B OE2   1 
ATOM   486   N  N     . ILE A  1  70  ? 16.358  61.250  54.591 1.00 40.19  ? 478  ILE B N     1 
ATOM   487   C  CA    . ILE A  1  70  ? 17.058  61.962  55.627 1.00 37.98  ? 478  ILE B CA    1 
ATOM   488   C  C     . ILE A  1  70  ? 16.168  63.121  56.081 1.00 40.22  ? 478  ILE B C     1 
ATOM   489   O  O     . ILE A  1  70  ? 16.023  63.362  57.277 1.00 39.58  ? 478  ILE B O     1 
ATOM   490   C  CB    . ILE A  1  70  ? 18.377  62.550  55.095 1.00 38.39  ? 478  ILE B CB    1 
ATOM   491   C  CG1   . ILE A  1  70  ? 19.306  61.440  54.571 1.00 35.82  ? 478  ILE B CG1   1 
ATOM   492   C  CG2   . ILE A  1  70  ? 19.038  63.461  56.138 1.00 32.81  ? 478  ILE B CG2   1 
ATOM   493   C  CD1   . ILE A  1  70  ? 19.901  60.528  55.633 1.00 33.23  ? 478  ILE B CD1   1 
ATOM   494   N  N     . ARG A  1  71  ? 15.586  63.835  55.128 1.00 36.42  ? 479  ARG B N     1 
ATOM   495   C  CA    . ARG A  1  71  ? 14.719  64.950  55.450 1.00 44.47  ? 479  ARG B CA    1 
ATOM   496   C  C     . ARG A  1  71  ? 13.526  64.563  56.312 1.00 45.72  ? 479  ARG B C     1 
ATOM   497   O  O     . ARG A  1  71  ? 13.215  65.268  57.267 1.00 45.68  ? 479  ARG B O     1 
ATOM   498   C  CB    . ARG A  1  71  ? 14.228  65.606  54.172 1.00 51.09  ? 479  ARG B CB    1 
ATOM   499   C  CG    . ARG A  1  71  ? 15.059  66.787  53.697 1.00 56.69  ? 479  ARG B CG    1 
ATOM   500   C  CD    . ARG A  1  71  ? 15.113  66.804  52.192 1.00 61.13  ? 479  ARG B CD    1 
ATOM   501   N  NE    . ARG A  1  71  ? 14.561  68.068  51.716 1.00 71.44  ? 479  ARG B NE    1 
ATOM   502   C  CZ    . ARG A  1  71  ? 13.416  68.145  51.046 1.00 80.54  ? 479  ARG B CZ    1 
ATOM   503   N  NH1   . ARG A  1  71  ? 12.735  67.034  50.781 1.00 87.50  ? 479  ARG B NH1   1 
ATOM   504   N  NH2   . ARG A  1  71  ? 12.950  69.314  50.645 1.00 83.73  ? 479  ARG B NH2   1 
ATOM   505   N  N     . GLN A  1  72  ? 12.872  63.441  55.980 1.00 44.39  ? 480  GLN B N     1 
ATOM   506   C  CA    . GLN A  1  72  ? 11.711  62.989  56.728 1.00 44.74  ? 480  GLN B CA    1 
ATOM   507   C  C     . GLN A  1  72  ? 12.083  62.672  58.166 1.00 44.70  ? 480  GLN B C     1 
ATOM   508   O  O     . GLN A  1  72  ? 11.359  63.024  59.081 1.00 53.10  ? 480  GLN B O     1 
ATOM   509   C  CB    . GLN A  1  72  ? 11.060  61.794  56.061 1.00 49.25  ? 480  GLN B CB    1 
ATOM   510   C  CG    . GLN A  1  72  ? 10.514  62.119  54.681 1.00 58.22  ? 480  GLN B CG    1 
ATOM   511   C  CD    . GLN A  1  72  ? 9.440   61.175  54.215 1.00 72.50  ? 480  GLN B CD    1 
ATOM   512   O  OE1   . GLN A  1  72  ? 9.443   60.732  53.065 1.00 93.39  ? 480  GLN B OE1   1 
ATOM   513   N  NE2   . GLN A  1  72  ? 8.475   60.883  55.094 1.00 86.41  ? 480  GLN B NE2   1 
ATOM   514   N  N     . MET A  1  73  ? 13.219  62.030  58.362 1.00 39.16  ? 481  MET B N     1 
ATOM   515   C  CA    . MET A  1  73  ? 13.656  61.724  59.696 1.00 39.70  ? 481  MET B CA    1 
ATOM   516   C  C     . MET A  1  73  ? 13.978  62.995  60.481 1.00 39.54  ? 481  MET B C     1 
ATOM   517   O  O     . MET A  1  73  ? 13.650  63.090  61.657 1.00 41.50  ? 481  MET B O     1 
ATOM   518   C  CB    . MET A  1  73  ? 14.888  60.809  59.690 1.00 33.38  ? 481  MET B CB    1 
ATOM   519   C  CG    . MET A  1  73  ? 14.516  59.351  59.653 1.00 37.04  ? 481  MET B CG    1 
ATOM   520   S  SD    . MET A  1  73  ? 16.015  58.367  59.635 1.00 36.21  ? 481  MET B SD    1 
ATOM   521   C  CE    . MET A  1  73  ? 16.562  58.563  57.935 1.00 34.32  ? 481  MET B CE    1 
ATOM   522   N  N     . ILE A  1  74  ? 14.645  63.943  59.842 1.00 40.09  ? 482  ILE B N     1 
ATOM   523   C  CA    . ILE A  1  74  ? 14.996  65.207  60.503 1.00 42.62  ? 482  ILE B CA    1 
ATOM   524   C  C     . ILE A  1  74  ? 13.712  65.921  60.891 1.00 40.31  ? 482  ILE B C     1 
ATOM   525   O  O     . ILE A  1  74  ? 13.532  66.299  62.046 1.00 42.29  ? 482  ILE B O     1 
ATOM   526   C  CB    . ILE A  1  74  ? 15.840  66.122  59.587 1.00 45.05  ? 482  ILE B CB    1 
ATOM   527   C  CG1   . ILE A  1  74  ? 17.231  65.497  59.363 1.00 43.42  ? 482  ILE B CG1   1 
ATOM   528   C  CG2   . ILE A  1  74  ? 15.944  67.541  60.171 1.00 41.90  ? 482  ILE B CG2   1 
ATOM   529   C  CD1   . ILE A  1  74  ? 17.976  66.098  58.179 1.00 38.63  ? 482  ILE B CD1   1 
ATOM   530   N  N     . THR A  1  75  ? 12.812  66.064  59.928 1.00 43.30  ? 483  THR B N     1 
ATOM   531   C  CA    . THR A  1  75  ? 11.532  66.713  60.186 1.00 47.08  ? 483  THR B CA    1 
ATOM   532   C  C     . THR A  1  75  ? 10.788  66.046  61.323 1.00 49.65  ? 483  THR B C     1 
ATOM   533   O  O     . THR A  1  75  ? 10.283  66.733  62.206 1.00 53.78  ? 483  THR B O     1 
ATOM   534   C  CB    . THR A  1  75  ? 10.627  66.686  58.962 1.00 46.11  ? 483  THR B CB    1 
ATOM   535   O  OG1   . THR A  1  75  ? 11.279  67.353  57.874 1.00 52.43  ? 483  THR B OG1   1 
ATOM   536   C  CG2   . THR A  1  75  ? 9.329   67.378  59.259 1.00 40.76  ? 483  THR B CG2   1 
ATOM   537   N  N     . ALA A  1  76  ? 10.723  64.717  61.306 1.00 47.39  ? 484  ALA B N     1 
ATOM   538   C  CA    . ALA A  1  76  ? 9.975   63.988  62.318 1.00 47.46  ? 484  ALA B CA    1 
ATOM   539   C  C     . ALA A  1  76  ? 10.565  64.122  63.713 1.00 43.76  ? 484  ALA B C     1 
ATOM   540   O  O     . ALA A  1  76  ? 9.817   64.262  64.666 1.00 44.64  ? 484  ALA B O     1 
ATOM   541   C  CB    . ALA A  1  76  ? 9.825   62.533  61.939 1.00 49.84  ? 484  ALA B CB    1 
ATOM   542   N  N     . PHE A  1  77  ? 11.883  64.060  63.827 1.00 39.26  ? 485  PHE B N     1 
ATOM   543   C  CA    . PHE A  1  77  ? 12.544  64.146  65.118 1.00 39.89  ? 485  PHE B CA    1 
ATOM   544   C  C     . PHE A  1  77  ? 12.371  65.542  65.767 1.00 48.52  ? 485  PHE B C     1 
ATOM   545   O  O     . PHE A  1  77  ? 12.212  65.636  66.987 1.00 47.26  ? 485  PHE B O     1 
ATOM   546   C  CB    . PHE A  1  77  ? 14.032  63.787  65.007 1.00 40.25  ? 485  PHE B CB    1 
ATOM   547   C  CG    . PHE A  1  77  ? 14.293  62.367  64.639 1.00 39.74  ? 485  PHE B CG    1 
ATOM   548   C  CD1   . PHE A  1  77  ? 13.240  61.455  64.435 1.00 41.34  ? 485  PHE B CD1   1 
ATOM   549   C  CD2   . PHE A  1  77  ? 15.613  61.916  64.493 1.00 44.01  ? 485  PHE B CD2   1 
ATOM   550   C  CE1   . PHE A  1  77  ? 13.489  60.127  64.067 1.00 38.66  ? 485  PHE B CE1   1 
ATOM   551   C  CE2   . PHE A  1  77  ? 15.871  60.578  64.135 1.00 48.15  ? 485  PHE B CE2   1 
ATOM   552   C  CZ    . PHE A  1  77  ? 14.799  59.687  63.913 1.00 40.62  ? 485  PHE B CZ    1 
ATOM   553   N  N     . GLY A  1  78  ? 12.387  66.605  64.946 1.00 42.01  ? 486  GLY B N     1 
ATOM   554   C  CA    . GLY A  1  78  ? 12.196  67.954  65.439 1.00 41.55  ? 486  GLY B CA    1 
ATOM   555   C  C     . GLY A  1  78  ? 13.418  68.621  66.045 1.00 45.50  ? 486  GLY B C     1 
ATOM   556   O  O     . GLY A  1  78  ? 13.398  69.821  66.303 1.00 46.63  ? 486  GLY B O     1 
ATOM   557   N  N     . THR A  1  79  ? 14.500  67.858  66.225 1.00 43.37  ? 487  THR B N     1 
ATOM   558   C  CA    . THR A  1  79  ? 15.720  68.363  66.838 1.00 44.56  ? 487  THR B CA    1 
ATOM   559   C  C     . THR A  1  79  ? 16.614  69.264  65.979 1.00 46.29  ? 487  THR B C     1 
ATOM   560   O  O     . THR A  1  79  ? 17.497  69.910  66.515 1.00 49.60  ? 487  THR B O     1 
ATOM   561   C  CB    . THR A  1  79  ? 16.609  67.206  67.302 1.00 45.96  ? 487  THR B CB    1 
ATOM   562   O  OG1   . THR A  1  79  ? 16.911  66.404  66.166 1.00 44.91  ? 487  THR B OG1   1 
ATOM   563   C  CG2   . THR A  1  79  ? 15.922  66.368  68.348 1.00 49.96  ? 487  THR B CG2   1 
ATOM   564   N  N     . GLY A  1  80  ? 16.439  69.275  64.664 1.00 45.88  ? 488  GLY B N     1 
ATOM   565   C  CA    . GLY A  1  80  ? 17.397  69.897  63.755 1.00 42.73  ? 488  GLY B CA    1 
ATOM   566   C  C     . GLY A  1  80  ? 18.618  68.970  63.658 1.00 53.70  ? 488  GLY B C     1 
ATOM   567   O  O     . GLY A  1  80  ? 18.595  67.816  64.121 1.00 48.73  ? 488  GLY B O     1 
ATOM   568   N  N     . ILE A  1  81  ? 19.707  69.442  63.075 1.00 51.08  ? 489  ILE B N     1 
ATOM   569   C  CA    . ILE A  1  81  ? 20.872  68.558  62.890 1.00 49.40  ? 489  ILE B CA    1 
ATOM   570   C  C     . ILE A  1  81  ? 22.226  69.233  63.141 1.00 58.07  ? 489  ILE B C     1 
ATOM   571   O  O     . ILE A  1  81  ? 22.361  70.454  63.004 1.00 58.45  ? 489  ILE B O     1 
ATOM   572   C  CB    . ILE A  1  81  ? 20.908  67.938  61.478 1.00 50.19  ? 489  ILE B CB    1 
ATOM   573   C  CG1   . ILE A  1  81  ? 20.739  69.026  60.422 1.00 48.45  ? 489  ILE B CG1   1 
ATOM   574   C  CG2   . ILE A  1  81  ? 19.870  66.839  61.304 1.00 49.23  ? 489  ILE B CG2   1 
ATOM   575   C  CD1   . ILE A  1  81  ? 20.876  68.517  59.002 1.00 51.42  ? 489  ILE B CD1   1 
ATOM   576   N  N     . GLY A  1  82  ? 23.235  68.428  63.480 1.00 56.05  ? 490  GLY B N     1 
ATOM   577   C  CA    . GLY A  1  82  ? 24.602  68.909  63.711 1.00 60.14  ? 490  GLY B CA    1 
ATOM   578   C  C     . GLY A  1  82  ? 24.795  70.007  64.754 1.00 63.98  ? 490  GLY B C     1 
ATOM   579   O  O     . GLY A  1  82  ? 24.510  69.820  65.930 1.00 58.29  ? 490  GLY B O     1 
ATOM   580   N  N     . GLY A  1  83  ? 25.300  71.152  64.299 1.00 67.67  ? 491  GLY B N     1 
ATOM   581   C  CA    . GLY A  1  83  ? 25.573  72.307  65.156 1.00 66.81  ? 491  GLY B CA    1 
ATOM   582   C  C     . GLY A  1  83  ? 24.303  72.913  65.729 1.00 64.82  ? 491  GLY B C     1 
ATOM   583   O  O     . GLY A  1  83  ? 24.299  73.400  66.863 1.00 62.53  ? 491  GLY B O     1 
ATOM   584   N  N     . ASP A  1  84  ? 23.224  72.859  64.951 1.00 59.06  ? 492  ASP B N     1 
ATOM   585   C  CA    . ASP A  1  84  ? 21.927  73.401  65.372 1.00 63.06  ? 492  ASP B CA    1 
ATOM   586   C  C     . ASP A  1  84  ? 21.054  72.379  66.093 1.00 59.19  ? 492  ASP B C     1 
ATOM   587   O  O     . ASP A  1  84  ? 19.895  72.635  66.362 1.00 55.24  ? 492  ASP B O     1 
ATOM   588   C  CB    . ASP A  1  84  ? 21.167  73.949  64.175 1.00 68.11  ? 492  ASP B CB    1 
ATOM   589   C  CG    . ASP A  1  84  ? 21.904  75.072  63.497 1.00 76.03  ? 492  ASP B CG    1 
ATOM   590   O  OD1   . ASP A  1  84  ? 22.730  75.739  64.159 1.00 91.57  ? 492  ASP B OD1   1 
ATOM   591   O  OD2   . ASP A  1  84  ? 21.665  75.287  62.300 1.00 92.60  ? 492  ASP B OD2   1 
ATOM   592   N  N     . PHE A  1  85  ? 21.614  71.212  66.371 1.00 51.68  ? 493  PHE B N     1 
ATOM   593   C  CA    . PHE A  1  85  ? 20.866  70.167  67.036 1.00 52.86  ? 493  PHE B CA    1 
ATOM   594   C  C     . PHE A  1  85  ? 20.388  70.576  68.443 1.00 56.17  ? 493  PHE B C     1 
ATOM   595   O  O     . PHE A  1  85  ? 21.161  71.052  69.232 1.00 57.12  ? 493  PHE B O     1 
ATOM   596   C  CB    . PHE A  1  85  ? 21.701  68.885  67.097 1.00 49.17  ? 493  PHE B CB    1 
ATOM   597   C  CG    . PHE A  1  85  ? 21.017  67.758  67.790 1.00 51.65  ? 493  PHE B CG    1 
ATOM   598   C  CD1   . PHE A  1  85  ? 21.124  67.611  69.180 1.00 49.63  ? 493  PHE B CD1   1 
ATOM   599   C  CD2   . PHE A  1  85  ? 20.247  66.843  67.058 1.00 50.39  ? 493  PHE B CD2   1 
ATOM   600   C  CE1   . PHE A  1  85  ? 20.497  66.559  69.817 1.00 50.57  ? 493  PHE B CE1   1 
ATOM   601   C  CE2   . PHE A  1  85  ? 19.624  65.783  67.692 1.00 52.33  ? 493  PHE B CE2   1 
ATOM   602   C  CZ    . PHE A  1  85  ? 19.724  65.656  69.076 1.00 48.58  ? 493  PHE B CZ    1 
ATOM   603   N  N     . ASP A  1  86  ? 19.110  70.386  68.739 1.00 56.05  ? 494  ASP B N     1 
ATOM   604   C  CA    . ASP A  1  86  ? 18.562  70.738  70.046 1.00 51.91  ? 494  ASP B CA    1 
ATOM   605   C  C     . ASP A  1  86  ? 17.847  69.570  70.704 1.00 48.05  ? 494  ASP B C     1 
ATOM   606   O  O     . ASP A  1  86  ? 16.683  69.274  70.346 1.00 46.95  ? 494  ASP B O     1 
ATOM   607   C  CB    . ASP A  1  86  ? 17.564  71.894  69.906 1.00 57.66  ? 494  ASP B CB    1 
ATOM   608   C  CG    . ASP A  1  86  ? 17.290  72.608  71.239 1.00 64.41  ? 494  ASP B CG    1 
ATOM   609   O  OD1   . ASP A  1  86  ? 17.536  72.048  72.349 1.00 65.54  ? 494  ASP B OD1   1 
ATOM   610   O  OD2   . ASP A  1  86  ? 16.815  73.756  71.160 1.00 70.14  ? 494  ASP B OD2   1 
ATOM   611   N  N     . LEU A  1  87  ? 18.498  68.944  71.678 1.00 42.44  ? 495  LEU B N     1 
ATOM   612   C  CA    . LEU A  1  87  ? 17.899  67.793  72.338 1.00 48.61  ? 495  LEU B CA    1 
ATOM   613   C  C     . LEU A  1  87  ? 16.499  68.054  72.927 1.00 55.48  ? 495  LEU B C     1 
ATOM   614   O  O     . LEU A  1  87  ? 15.643  67.158  72.943 1.00 51.42  ? 495  LEU B O     1 
ATOM   615   C  CB    . LEU A  1  87  ? 18.815  67.246  73.417 1.00 44.39  ? 495  LEU B CB    1 
ATOM   616   C  CG    . LEU A  1  87  ? 18.379  65.879  73.958 1.00 50.33  ? 495  LEU B CG    1 
ATOM   617   C  CD1   . LEU A  1  87  ? 18.475  64.767  72.911 1.00 51.60  ? 495  LEU B CD1   1 
ATOM   618   C  CD2   . LEU A  1  87  ? 19.208  65.508  75.171 1.00 57.35  ? 495  LEU B CD2   1 
ATOM   619   N  N     . ALA A  1  88  ? 16.276  69.280  73.404 1.00 53.25  ? 496  ALA B N     1 
ATOM   620   C  CA    . ALA A  1  88  ? 15.028  69.634  74.076 1.00 53.44  ? 496  ALA B CA    1 
ATOM   621   C  C     . ALA A  1  88  ? 13.857  69.588  73.118 1.00 56.89  ? 496  ALA B C     1 
ATOM   622   O  O     . ALA A  1  88  ? 12.758  69.267  73.520 1.00 65.07  ? 496  ALA B O     1 
ATOM   623   C  CB    . ALA A  1  88  ? 15.131  71.013  74.709 1.00 48.07  ? 496  ALA B CB    1 
ATOM   624   N  N     . LYS A  1  89  ? 14.098  69.890  71.843 1.00 57.61  ? 497  LYS B N     1 
ATOM   625   C  CA    . LYS A  1  89  ? 13.056  69.900  70.835 1.00 50.75  ? 497  LYS B CA    1 
ATOM   626   C  C     . LYS A  1  89  ? 12.631  68.506  70.350 1.00 50.99  ? 497  LYS B C     1 
ATOM   627   O  O     . LYS A  1  89  ? 11.622  68.389  69.662 1.00 53.46  ? 497  LYS B O     1 
ATOM   628   C  CB    . LYS A  1  89  ? 13.455  70.807  69.669 1.00 56.16  ? 497  LYS B CB    1 
ATOM   629   C  CG    . LYS A  1  89  ? 13.571  72.272  70.094 1.00 58.19  ? 497  LYS B CG    1 
ATOM   630   C  CD    . LYS A  1  89  ? 13.391  73.261  68.956 1.00 63.24  ? 497  LYS B CD    1 
ATOM   631   C  CE    . LYS A  1  89  ? 13.415  74.677  69.509 1.00 67.88  ? 497  LYS B CE    1 
ATOM   632   N  NZ    . LYS A  1  89  ? 13.476  75.733  68.456 1.00 69.93  ? 497  LYS B NZ    1 
ATOM   633   N  N     . ALA A  1  90  ? 13.372  67.456  70.705 1.00 44.27  ? 498  ALA B N     1 
ATOM   634   C  CA    . ALA A  1  90  ? 12.993  66.101  70.300 1.00 44.54  ? 498  ALA B CA    1 
ATOM   635   C  C     . ALA A  1  90  ? 11.529  65.831  70.559 1.00 50.01  ? 498  ALA B C     1 
ATOM   636   O  O     . ALA A  1  90  ? 10.995  66.172  71.620 1.00 61.06  ? 498  ALA B O     1 
ATOM   637   C  CB    . ALA A  1  90  ? 13.824  65.061  70.986 1.00 37.55  ? 498  ALA B CB    1 
ATOM   638   N  N     . ARG A  1  91  ? 10.871  65.235  69.578 1.00 47.91  ? 499  ARG B N     1 
ATOM   639   C  CA    . ARG A  1  91  ? 9.466   64.938  69.696 1.00 44.28  ? 499  ARG B CA    1 
ATOM   640   C  C     . ARG A  1  91  ? 9.246   63.534  70.216 1.00 44.24  ? 499  ARG B C     1 
ATOM   641   O  O     . ARG A  1  91  ? 8.140   63.197  70.541 1.00 43.95  ? 499  ARG B O     1 
ATOM   642   C  CB    . ARG A  1  91  ? 8.820   65.131  68.347 1.00 49.39  ? 499  ARG B CB    1 
ATOM   643   C  CG    . ARG A  1  91  ? 9.178   66.496  67.793 1.00 52.81  ? 499  ARG B CG    1 
ATOM   644   C  CD    . ARG A  1  91  ? 8.553   66.852  66.453 1.00 51.81  ? 499  ARG B CD    1 
ATOM   645   N  NE    . ARG A  1  91  ? 7.121   66.671  66.466 1.00 53.70  ? 499  ARG B NE    1 
ATOM   646   C  CZ    . ARG A  1  91  ? 6.487   65.630  65.928 1.00 54.83  ? 499  ARG B CZ    1 
ATOM   647   N  NH1   . ARG A  1  91  ? 7.160   64.689  65.289 1.00 52.10  ? 499  ARG B NH1   1 
ATOM   648   N  NH2   . ARG A  1  91  ? 5.173   65.537  66.037 1.00 53.83  ? 499  ARG B NH2   1 
ATOM   649   N  N     . TYR A  1  92  ? 10.286  62.726  70.334 1.00 39.36  ? 500  TYR B N     1 
ATOM   650   C  CA    . TYR A  1  92  ? 10.092  61.398  70.861 1.00 40.52  ? 500  TYR B CA    1 
ATOM   651   C  C     . TYR A  1  92  ? 11.304  61.158  71.686 1.00 41.96  ? 500  TYR B C     1 
ATOM   652   O  O     . TYR A  1  92  ? 12.359  61.638  71.336 1.00 40.96  ? 500  TYR B O     1 
ATOM   653   C  CB    . TYR A  1  92  ? 10.045  60.353  69.723 1.00 40.22  ? 500  TYR B CB    1 
ATOM   654   C  CG    . TYR A  1  92  ? 9.107   60.676  68.636 1.00 37.48  ? 500  TYR B CG    1 
ATOM   655   C  CD1   . TYR A  1  92  ? 9.515   61.435  67.536 1.00 35.70  ? 500  TYR B CD1   1 
ATOM   656   C  CD2   . TYR A  1  92  ? 7.784   60.275  68.729 1.00 37.61  ? 500  TYR B CD2   1 
ATOM   657   C  CE1   . TYR A  1  92  ? 8.625   61.735  66.541 1.00 32.95  ? 500  TYR B CE1   1 
ATOM   658   C  CE2   . TYR A  1  92  ? 6.887   60.605  67.765 1.00 37.62  ? 500  TYR B CE2   1 
ATOM   659   C  CZ    . TYR A  1  92  ? 7.321   61.306  66.666 1.00 36.10  ? 500  TYR B CZ    1 
ATOM   660   O  OH    . TYR A  1  92  ? 6.407   61.615  65.725 1.00 36.50  ? 500  TYR B OH    1 
ATOM   661   N  N     . HIS A  1  93  ? 11.178  60.423  72.777 1.00 40.89  ? 501  HIS B N     1 
ATOM   662   C  CA    . HIS A  1  93  ? 12.345  60.135  73.601 1.00 45.02  ? 501  HIS B CA    1 
ATOM   663   C  C     . HIS A  1  93  ? 12.842  58.736  73.287 1.00 42.92  ? 501  HIS B C     1 
ATOM   664   O  O     . HIS A  1  93  ? 13.853  58.289  73.826 1.00 42.20  ? 501  HIS B O     1 
ATOM   665   C  CB    . HIS A  1  93  ? 12.017  60.352  75.106 1.00 45.57  ? 501  HIS B CB    1 
ATOM   666   C  CG    . HIS A  1  93  ? 12.120  61.791  75.538 1.00 53.07  ? 501  HIS B CG    1 
ATOM   667   N  ND1   . HIS A  1  93  ? 12.442  62.175  76.823 1.00 48.10  ? 501  HIS B ND1   1 
ATOM   668   C  CD2   . HIS A  1  93  ? 11.930  62.941  74.844 1.00 50.84  ? 501  HIS B CD2   1 
ATOM   669   C  CE1   . HIS A  1  93  ? 12.455  63.493  76.894 1.00 51.36  ? 501  HIS B CE1   1 
ATOM   670   N  NE2   . HIS A  1  93  ? 12.149  63.983  75.705 1.00 52.50  ? 501  HIS B NE2   1 
ATOM   671   N  N     . LYS A  1  94  ? 12.116  58.038  72.424 1.00 45.21  ? 502  LYS B N     1 
ATOM   672   C  CA    . LYS A  1  94  ? 12.589  56.755  71.924 1.00 49.04  ? 502  LYS B CA    1 
ATOM   673   C  C     . LYS A  1  94  ? 12.491  56.741  70.408 1.00 50.50  ? 502  LYS B C     1 
ATOM   674   O  O     . LYS A  1  94  ? 11.408  56.841  69.831 1.00 45.48  ? 502  LYS B O     1 
ATOM   675   C  CB    . LYS A  1  94  ? 11.820  55.603  72.549 1.00 47.07  ? 502  LYS B CB    1 
ATOM   676   C  CG    . LYS A  1  94  ? 12.283  55.259  73.947 1.00 47.34  ? 502  LYS B CG    1 
ATOM   677   C  CD    . LYS A  1  94  ? 11.645  53.939  74.355 1.00 45.62  ? 502  LYS B CD    1 
ATOM   678   C  CE    . LYS A  1  94  ? 11.844  53.615  75.816 1.00 44.94  ? 502  LYS B CE    1 
ATOM   679   N  NZ    . LYS A  1  94  ? 10.956  54.455  76.621 1.00 47.23  ? 502  LYS B NZ    1 
ATOM   680   N  N     . ILE A  1  95  ? 13.643  56.634  69.774 1.00 47.08  ? 503  ILE B N     1 
ATOM   681   C  CA    . ILE A  1  95  ? 13.703  56.448  68.347 1.00 41.55  ? 503  ILE B CA    1 
ATOM   682   C  C     . ILE A  1  95  ? 14.105  55.018  68.130 1.00 39.13  ? 503  ILE B C     1 
ATOM   683   O  O     . ILE A  1  95  ? 15.185  54.664  68.489 1.00 39.12  ? 503  ILE B O     1 
ATOM   684   C  CB    . ILE A  1  95  ? 14.761  57.357  67.738 1.00 40.05  ? 503  ILE B CB    1 
ATOM   685   C  CG1   . ILE A  1  95  ? 14.201  58.753  67.527 1.00 41.29  ? 503  ILE B CG1   1 
ATOM   686   C  CG2   . ILE A  1  95  ? 15.082  56.892  66.333 1.00 39.57  ? 503  ILE B CG2   1 
ATOM   687   C  CD1   . ILE A  1  95  ? 14.312  59.677  68.681 1.00 41.69  ? 503  ILE B CD1   1 
ATOM   688   N  N     . VAL A  1  96  ? 13.268  54.193  67.537 1.00 33.61  ? 504  VAL B N     1 
ATOM   689   C  CA    . VAL A  1  96  ? 13.552  52.764  67.565 1.00 34.23  ? 504  VAL B CA    1 
ATOM   690   C  C     . VAL A  1  96  ? 13.829  52.216  66.155 1.00 38.36  ? 504  VAL B C     1 
ATOM   691   O  O     . VAL A  1  96  ? 12.967  52.311  65.274 1.00 36.69  ? 504  VAL B O     1 
ATOM   692   C  CB    . VAL A  1  96  ? 12.343  52.008  68.132 1.00 35.54  ? 504  VAL B CB    1 
ATOM   693   C  CG1   . VAL A  1  96  ? 12.669  50.537  68.276 1.00 33.29  ? 504  VAL B CG1   1 
ATOM   694   C  CG2   . VAL A  1  96  ? 11.964  52.583  69.473 1.00 33.00  ? 504  VAL B CG2   1 
ATOM   695   N  N     . ILE A  1  97  ? 14.984  51.599  65.948 1.00 32.39  ? 505  ILE B N     1 
ATOM   696   C  CA    . ILE A  1  97  ? 15.294  51.085  64.634 1.00 34.61  ? 505  ILE B CA    1 
ATOM   697   C  C     . ILE A  1  97  ? 14.726  49.690  64.522 1.00 34.02  ? 505  ILE B C     1 
ATOM   698   O  O     . ILE A  1  97  ? 15.055  48.824  65.299 1.00 33.86  ? 505  ILE B O     1 
ATOM   699   C  CB    . ILE A  1  97  ? 16.807  51.051  64.426 1.00 34.00  ? 505  ILE B CB    1 
ATOM   700   C  CG1   . ILE A  1  97  ? 17.350  52.483  64.434 1.00 34.26  ? 505  ILE B CG1   1 
ATOM   701   C  CG2   . ILE A  1  97  ? 17.172  50.370  63.125 1.00 31.73  ? 505  ILE B CG2   1 
ATOM   702   C  CD1   . ILE A  1  97  ? 18.841  52.527  64.547 1.00 29.23  ? 505  ILE B CD1   1 
ATOM   703   N  N     . MET A  1  98  ? 13.873  49.486  63.538 1.00 36.45  ? 506  MET B N     1 
ATOM   704   C  CA    . MET A  1  98  ? 13.197  48.219  63.376 1.00 39.87  ? 506  MET B CA    1 
ATOM   705   C  C     . MET A  1  98  ? 13.271  47.701  61.938 1.00 42.89  ? 506  MET B C     1 
ATOM   706   O  O     . MET A  1  98  ? 12.321  47.832  61.175 1.00 42.33  ? 506  MET B O     1 
ATOM   707   C  CB    . MET A  1  98  ? 11.746  48.382  63.787 1.00 41.75  ? 506  MET B CB    1 
ATOM   708   C  CG    . MET A  1  98  ? 11.013  47.059  63.975 1.00 48.28  ? 506  MET B CG    1 
ATOM   709   S  SD    . MET A  1  98  ? 9.512   47.181  64.993 1.00 53.05  ? 506  MET B SD    1 
ATOM   710   C  CE    . MET A  1  98  ? 8.348   47.786  63.851 1.00 42.33  ? 506  MET B CE    1 
ATOM   711   N  N     . THR A  1  99  ? 14.383  47.076  61.598 1.00 40.02  ? 507  THR B N     1 
ATOM   712   C  CA    . THR A  1  99  ? 14.557  46.510  60.285 1.00 40.41  ? 507  THR B CA    1 
ATOM   713   C  C     . THR A  1  99  ? 14.253  45.041  60.417 1.00 39.76  ? 507  THR B C     1 
ATOM   714   O  O     . THR A  1  99  ? 14.070  44.558  61.525 1.00 39.67  ? 507  THR B O     1 
ATOM   715   C  CB    . THR A  1  99  ? 16.006  46.603  59.792 1.00 40.17  ? 507  THR B CB    1 
ATOM   716   O  OG1   . THR A  1  99  ? 16.857  45.805  60.633 1.00 38.75  ? 507  THR B OG1   1 
ATOM   717   C  CG2   . THR A  1  99  ? 16.480  47.966  59.783 1.00 33.33  ? 507  THR B CG2   1 
ATOM   718   N  N     . ASP A  1  100 ? 14.275  44.326  59.300 1.00 41.10  ? 508  ASP B N     1 
ATOM   719   C  CA    . ASP A  1  100 ? 14.080  42.870  59.293 1.00 41.97  ? 508  ASP B CA    1 
ATOM   720   C  C     . ASP A  1  100 ? 15.277  42.195  59.923 1.00 39.15  ? 508  ASP B C     1 
ATOM   721   O  O     . ASP A  1  100 ? 16.381  42.736  59.882 1.00 40.30  ? 508  ASP B O     1 
ATOM   722   C  CB    . ASP A  1  100 ? 13.992  42.362  57.860 1.00 42.55  ? 508  ASP B CB    1 
ATOM   723   C  CG    . ASP A  1  100 ? 12.808  42.885  57.128 1.00 50.46  ? 508  ASP B CG    1 
ATOM   724   O  OD1   . ASP A  1  100 ? 11.932  43.591  57.722 1.00 56.84  ? 508  ASP B OD1   1 
ATOM   725   O  OD2   . ASP A  1  100 ? 12.740  42.584  55.910 1.00 50.98  ? 508  ASP B OD2   1 
ATOM   726   N  N     . ALA A  1  101 ? 15.091  41.003  60.483 1.00 41.60  ? 509  ALA B N     1 
ATOM   727   C  CA    . ALA A  1  101 ? 16.216  40.245  61.058 1.00 41.31  ? 509  ALA B CA    1 
ATOM   728   C  C     . ALA A  1  101 ? 16.975  39.451  59.996 1.00 42.89  ? 509  ALA B C     1 
ATOM   729   O  O     . ALA A  1  101 ? 16.977  38.215  60.024 1.00 48.28  ? 509  ALA B O     1 
ATOM   730   C  CB    . ALA A  1  101 ? 15.719  39.318  62.133 1.00 38.42  ? 509  ALA B CB    1 
ATOM   731   N  N     . ASP A  1  102 ? 17.553  40.152  59.032 1.00 39.08  ? 510  ASP B N     1 
ATOM   732   C  CA    . ASP A  1  102 ? 18.284  39.530  57.950 1.00 37.40  ? 510  ASP B CA    1 
ATOM   733   C  C     . ASP A  1  102 ? 19.468  40.441  57.664 1.00 38.69  ? 510  ASP B C     1 
ATOM   734   O  O     . ASP A  1  102 ? 19.568  41.536  58.231 1.00 38.06  ? 510  ASP B O     1 
ATOM   735   C  CB    . ASP A  1  102 ? 17.399  39.276  56.704 1.00 33.30  ? 510  ASP B CB    1 
ATOM   736   C  CG    . ASP A  1  102 ? 16.795  40.543  56.123 1.00 38.19  ? 510  ASP B CG    1 
ATOM   737   O  OD1   . ASP A  1  102 ? 17.402  41.626  56.340 1.00 41.80  ? 510  ASP B OD1   1 
ATOM   738   O  OD2   . ASP A  1  102 ? 15.751  40.446  55.421 1.00 40.04  ? 510  ASP B OD2   1 
ATOM   739   N  N     . VAL A  1  103 ? 20.364  39.995  56.785 1.00 37.90  ? 511  VAL B N     1 
ATOM   740   C  CA    . VAL A  1  103 ? 21.588  40.744  56.498 1.00 34.72  ? 511  VAL B CA    1 
ATOM   741   C  C     . VAL A  1  103 ? 21.365  42.158  55.950 1.00 36.73  ? 511  VAL B C     1 
ATOM   742   O  O     . VAL A  1  103 ? 22.133  43.060  56.267 1.00 33.51  ? 511  VAL B O     1 
ATOM   743   C  CB    . VAL A  1  103 ? 22.583  39.944  55.653 1.00 34.70  ? 511  VAL B CB    1 
ATOM   744   C  CG1   . VAL A  1  103 ? 23.067  38.702  56.461 1.00 27.36  ? 511  VAL B CG1   1 
ATOM   745   C  CG2   . VAL A  1  103 ? 22.011  39.655  54.261 1.00 28.70  ? 511  VAL B CG2   1 
ATOM   746   N  N     . ASP A  1  104 ? 20.325  42.353  55.142 1.00 32.87  ? 512  ASP B N     1 
ATOM   747   C  CA    . ASP A  1  104 ? 20.090  43.649  54.599 1.00 32.82  ? 512  ASP B CA    1 
ATOM   748   C  C     . ASP A  1  104 ? 19.476  44.576  55.587 1.00 34.30  ? 512  ASP B C     1 
ATOM   749   O  O     . ASP A  1  104 ? 19.676  45.760  55.480 1.00 34.94  ? 512  ASP B O     1 
ATOM   750   C  CB    . ASP A  1  104 ? 19.250  43.581  53.347 1.00 29.44  ? 512  ASP B CB    1 
ATOM   751   C  CG    . ASP A  1  104 ? 19.985  42.950  52.249 1.00 31.98  ? 512  ASP B CG    1 
ATOM   752   O  OD1   . ASP A  1  104 ? 20.804  43.659  51.624 1.00 31.59  ? 512  ASP B OD1   1 
ATOM   753   O  OD2   . ASP A  1  104 ? 19.843  41.703  52.068 1.00 33.86  ? 512  ASP B OD2   1 
ATOM   754   N  N     . GLY A  1  105 ? 18.797  44.007  56.574 1.00 33.13  ? 513  GLY B N     1 
ATOM   755   C  CA    . GLY A  1  105 ? 18.252  44.753  57.681 1.00 28.95  ? 513  GLY B CA    1 
ATOM   756   C  C     . GLY A  1  105 ? 19.427  45.261  58.534 1.00 33.26  ? 513  GLY B C     1 
ATOM   757   O  O     . GLY A  1  105 ? 19.429  46.389  59.020 1.00 31.90  ? 513  GLY B O     1 
ATOM   758   N  N     . ALA A  1  106 ? 20.425  44.416  58.693 1.00 29.62  ? 514  ALA B N     1 
ATOM   759   C  CA    . ALA A  1  106 ? 21.583  44.791  59.424 1.00 31.86  ? 514  ALA B CA    1 
ATOM   760   C  C     . ALA A  1  106 ? 22.302  45.931  58.731 1.00 30.96  ? 514  ALA B C     1 
ATOM   761   O  O     . ALA A  1  106 ? 22.852  46.765  59.389 1.00 27.82  ? 514  ALA B O     1 
ATOM   762   C  CB    . ALA A  1  106 ? 22.528  43.610  59.572 1.00 30.21  ? 514  ALA B CB    1 
ATOM   763   N  N     . HIS A  1  107 ? 22.315  45.932  57.409 1.00 28.69  ? 515  HIS B N     1 
ATOM   764   C  CA    . HIS A  1  107 ? 22.996  46.982  56.698 1.00 27.72  ? 515  HIS B CA    1 
ATOM   765   C  C     . HIS A  1  107 ? 22.255  48.311  56.894 1.00 30.06  ? 515  HIS B C     1 
ATOM   766   O  O     . HIS A  1  107 ? 22.893  49.359  57.116 1.00 26.06  ? 515  HIS B O     1 
ATOM   767   C  CB    . HIS A  1  107 ? 22.997  46.613  55.214 1.00 27.02  ? 515  HIS B CB    1 
ATOM   768   C  CG    . HIS A  1  107 ? 23.840  47.501  54.376 1.00 29.33  ? 515  HIS B CG    1 
ATOM   769   N  ND1   . HIS A  1  107 ? 23.570  47.753  53.042 1.00 31.99  ? 515  HIS B ND1   1 
ATOM   770   C  CD2   . HIS A  1  107 ? 24.997  48.153  54.659 1.00 26.54  ? 515  HIS B CD2   1 
ATOM   771   C  CE1   . HIS A  1  107 ? 24.529  48.533  52.549 1.00 28.61  ? 515  HIS B CE1   1 
ATOM   772   N  NE2   . HIS A  1  107 ? 25.375  48.830  53.527 1.00 25.15  ? 515  HIS B NE2   1 
ATOM   773   N  N     . ILE A  1  108 ? 20.917  48.272  56.819 1.00 28.88  ? 516  ILE B N     1 
ATOM   774   C  CA    . ILE A  1  108 ? 20.116  49.444  56.973 1.00 29.62  ? 516  ILE B CA    1 
ATOM   775   C  C     . ILE A  1  108 ? 20.339  50.067  58.345 1.00 32.30  ? 516  ILE B C     1 
ATOM   776   O  O     . ILE A  1  108 ? 20.481  51.259  58.460 1.00 33.83  ? 516  ILE B O     1 
ATOM   777   C  CB    . ILE A  1  108 ? 18.644  49.137  56.671 1.00 31.57  ? 516  ILE B CB    1 
ATOM   778   C  CG1   . ILE A  1  108 ? 18.506  49.075  55.121 1.00 28.70  ? 516  ILE B CG1   1 
ATOM   779   C  CG2   . ILE A  1  108 ? 17.724  50.221  57.286 1.00 27.90  ? 516  ILE B CG2   1 
ATOM   780   C  CD1   . ILE A  1  108 ? 17.257  48.304  54.650 1.00 27.94  ? 516  ILE B CD1   1 
ATOM   781   N  N     . ARG A  1  109 ? 20.456  49.234  59.350 1.00 31.57  ? 517  ARG B N     1 
ATOM   782   C  CA    . ARG A  1  109 ? 20.774  49.635  60.671 1.00 29.89  ? 517  ARG B CA    1 
ATOM   783   C  C     . ARG A  1  109 ? 22.117  50.349  60.795 1.00 32.15  ? 517  ARG B C     1 
ATOM   784   O  O     . ARG A  1  109 ? 22.180  51.313  61.538 1.00 34.01  ? 517  ARG B O     1 
ATOM   785   C  CB    . ARG A  1  109 ? 20.821  48.378  61.491 1.00 32.90  ? 517  ARG B CB    1 
ATOM   786   C  CG    . ARG A  1  109 ? 20.786  48.565  62.994 1.00 39.34  ? 517  ARG B CG    1 
ATOM   787   C  CD    . ARG A  1  109 ? 20.130  47.341  63.600 1.00 40.35  ? 517  ARG B CD    1 
ATOM   788   N  NE    . ARG A  1  109 ? 21.040  46.226  63.508 1.00 43.27  ? 517  ARG B NE    1 
ATOM   789   C  CZ    . ARG A  1  109 ? 20.705  45.033  63.068 1.00 40.45  ? 517  ARG B CZ    1 
ATOM   790   N  NH1   . ARG A  1  109 ? 19.463  44.782  62.739 1.00 38.14  ? 517  ARG B NH1   1 
ATOM   791   N  NH2   . ARG A  1  109 ? 21.621  44.089  62.993 1.00 38.69  ? 517  ARG B NH2   1 
ATOM   792   N  N     . THR A  1  110 ? 23.165  49.881  60.105 1.00 27.95  ? 518  THR B N     1 
ATOM   793   C  CA    . THR A  1  110 ? 24.430  50.583  60.149 1.00 29.69  ? 518  THR B CA    1 
ATOM   794   C  C     . THR A  1  110 ? 24.348  51.936  59.473 1.00 30.10  ? 518  THR B C     1 
ATOM   795   O  O     . THR A  1  110 ? 25.007  52.853  59.905 1.00 36.76  ? 518  THR B O     1 
ATOM   796   C  CB    . THR A  1  110 ? 25.614  49.767  59.572 1.00 26.36  ? 518  THR B CB    1 
ATOM   797   O  OG1   . THR A  1  110 ? 25.473  49.575  58.141 1.00 27.68  ? 518  THR B OG1   1 
ATOM   798   C  CG2   . THR A  1  110 ? 25.672  48.449  60.242 1.00 25.63  ? 518  THR B CG2   1 
ATOM   799   N  N     . LEU A  1  111 ? 23.585  52.016  58.382 1.00 30.43  ? 519  LEU B N     1 
ATOM   800   C  CA    . LEU A  1  111 ? 23.372  53.243  57.671 1.00 33.42  ? 519  LEU B CA    1 
ATOM   801   C  C     . LEU A  1  111 ? 22.615  54.258  58.513 1.00 35.82  ? 519  LEU B C     1 
ATOM   802   O  O     . LEU A  1  111 ? 22.956  55.425  58.463 1.00 33.89  ? 519  LEU B O     1 
ATOM   803   C  CB    . LEU A  1  111 ? 22.622  52.986  56.378 1.00 32.62  ? 519  LEU B CB    1 
ATOM   804   C  CG    . LEU A  1  111 ? 23.397  52.150  55.371 1.00 33.78  ? 519  LEU B CG    1 
ATOM   805   C  CD1   . LEU A  1  111 ? 22.423  51.583  54.335 1.00 32.73  ? 519  LEU B CD1   1 
ATOM   806   C  CD2   . LEU A  1  111 ? 24.443  53.028  54.698 1.00 29.31  ? 519  LEU B CD2   1 
ATOM   807   N  N     . LEU A  1  112 ? 21.620  53.802  59.283 1.00 34.03  ? 520  LEU B N     1 
ATOM   808   C  CA    . LEU A  1  112 ? 20.850  54.702  60.129 1.00 35.10  ? 520  LEU B CA    1 
ATOM   809   C  C     . LEU A  1  112 ? 21.702  55.211  61.307 1.00 37.50  ? 520  LEU B C     1 
ATOM   810   O  O     . LEU A  1  112 ? 21.726  56.404  61.600 1.00 32.71  ? 520  LEU B O     1 
ATOM   811   C  CB    . LEU A  1  112 ? 19.584  54.030  60.637 1.00 30.74  ? 520  LEU B CB    1 
ATOM   812   C  CG    . LEU A  1  112 ? 18.428  53.866  59.661 1.00 33.34  ? 520  LEU B CG    1 
ATOM   813   C  CD1   . LEU A  1  112 ? 17.346  53.070  60.389 1.00 32.33  ? 520  LEU B CD1   1 
ATOM   814   C  CD2   . LEU A  1  112 ? 17.908  55.239  59.190 1.00 31.78  ? 520  LEU B CD2   1 
ATOM   815   N  N     . LEU A  1  113 ? 22.433  54.296  61.941 1.00 33.34  ? 521  LEU B N     1 
ATOM   816   C  CA    . LEU A  1  113 ? 23.292  54.699  63.022 1.00 33.68  ? 521  LEU B CA    1 
ATOM   817   C  C     . LEU A  1  113 ? 24.376  55.636  62.509 1.00 36.41  ? 521  LEU B C     1 
ATOM   818   O  O     . LEU A  1  113 ? 24.813  56.512  63.236 1.00 34.76  ? 521  LEU B O     1 
ATOM   819   C  CB    . LEU A  1  113 ? 23.928  53.507  63.695 1.00 32.60  ? 521  LEU B CB    1 
ATOM   820   C  CG    . LEU A  1  113 ? 23.050  52.589  64.502 1.00 34.42  ? 521  LEU B CG    1 
ATOM   821   C  CD1   . LEU A  1  113 ? 23.844  51.329  64.907 1.00 28.86  ? 521  LEU B CD1   1 
ATOM   822   C  CD2   . LEU A  1  113 ? 22.467  53.346  65.681 1.00 32.45  ? 521  LEU B CD2   1 
ATOM   823   N  N     . THR A  1  114 ? 24.799  55.452  61.260 1.00 36.54  ? 522  THR B N     1 
ATOM   824   C  CA    . THR A  1  114 ? 25.827  56.314  60.705 1.00 33.35  ? 522  THR B CA    1 
ATOM   825   C  C     . THR A  1  114 ? 25.276  57.744  60.597 1.00 36.69  ? 522  THR B C     1 
ATOM   826   O  O     . THR A  1  114 ? 25.947  58.693  60.944 1.00 37.88  ? 522  THR B O     1 
ATOM   827   C  CB    . THR A  1  114 ? 26.357  55.831  59.336 1.00 31.69  ? 522  THR B CB    1 
ATOM   828   O  OG1   . THR A  1  114 ? 27.020  54.563  59.491 1.00 33.64  ? 522  THR B OG1   1 
ATOM   829   C  CG2   . THR A  1  114 ? 27.358  56.833  58.749 1.00 28.88  ? 522  THR B CG2   1 
ATOM   830   N  N     . PHE A  1  115 ? 24.046  57.880  60.131 1.00 34.32  ? 523  PHE B N     1 
ATOM   831   C  CA    . PHE A  1  115 ? 23.414  59.177  60.049 1.00 33.37  ? 523  PHE B CA    1 
ATOM   832   C  C     . PHE A  1  115 ? 23.241  59.786  61.440 1.00 37.62  ? 523  PHE B C     1 
ATOM   833   O  O     . PHE A  1  115 ? 23.523  60.966  61.632 1.00 37.85  ? 523  PHE B O     1 
ATOM   834   C  CB    . PHE A  1  115 ? 22.067  59.070  59.342 1.00 35.45  ? 523  PHE B CB    1 
ATOM   835   C  CG    . PHE A  1  115 ? 21.249  60.315  59.417 1.00 35.33  ? 523  PHE B CG    1 
ATOM   836   C  CD1   . PHE A  1  115 ? 21.782  61.539  58.959 1.00 33.52  ? 523  PHE B CD1   1 
ATOM   837   C  CD2   . PHE A  1  115 ? 19.948  60.278  59.921 1.00 35.00  ? 523  PHE B CD2   1 
ATOM   838   C  CE1   . PHE A  1  115 ? 21.021  62.692  59.020 1.00 35.45  ? 523  PHE B CE1   1 
ATOM   839   C  CE2   . PHE A  1  115 ? 19.164  61.445  59.969 1.00 33.17  ? 523  PHE B CE2   1 
ATOM   840   C  CZ    . PHE A  1  115 ? 19.713  62.660  59.538 1.00 36.48  ? 523  PHE B CZ    1 
ATOM   841   N  N     . PHE A  1  116 ? 22.799  58.988  62.400 1.00 35.09  ? 524  PHE B N     1 
ATOM   842   C  CA    . PHE A  1  116 ? 22.583  59.479  63.767 1.00 39.99  ? 524  PHE B CA    1 
ATOM   843   C  C     . PHE A  1  116 ? 23.883  59.925  64.439 1.00 41.95  ? 524  PHE B C     1 
ATOM   844   O  O     . PHE A  1  116 ? 23.930  60.974  65.045 1.00 39.88  ? 524  PHE B O     1 
ATOM   845   C  CB    . PHE A  1  116 ? 21.885  58.454  64.659 1.00 37.18  ? 524  PHE B CB    1 
ATOM   846   C  CG    . PHE A  1  116 ? 20.524  58.039  64.179 1.00 41.55  ? 524  PHE B CG    1 
ATOM   847   C  CD1   . PHE A  1  116 ? 19.738  58.872  63.369 1.00 42.48  ? 524  PHE B CD1   1 
ATOM   848   C  CD2   . PHE A  1  116 ? 20.014  56.802  64.561 1.00 38.93  ? 524  PHE B CD2   1 
ATOM   849   C  CE1   . PHE A  1  116 ? 18.484  58.453  62.931 1.00 41.63  ? 524  PHE B CE1   1 
ATOM   850   C  CE2   . PHE A  1  116 ? 18.750  56.386  64.143 1.00 40.36  ? 524  PHE B CE2   1 
ATOM   851   C  CZ    . PHE A  1  116 ? 17.983  57.213  63.310 1.00 37.43  ? 524  PHE B CZ    1 
ATOM   852   N  N     . TYR A  1  117 ? 24.943  59.136  64.295 1.00 39.52  ? 525  TYR B N     1 
ATOM   853   C  CA    . TYR A  1  117 ? 26.218  59.476  64.898 1.00 38.01  ? 525  TYR B CA    1 
ATOM   854   C  C     . TYR A  1  117 ? 26.821  60.744  64.294 1.00 37.28  ? 525  TYR B C     1 
ATOM   855   O  O     . TYR A  1  117 ? 27.424  61.529  64.991 1.00 42.79  ? 525  TYR B O     1 
ATOM   856   C  CB    . TYR A  1  117 ? 27.203  58.315  64.781 1.00 40.63  ? 525  TYR B CB    1 
ATOM   857   C  CG    . TYR A  1  117 ? 28.452  58.542  65.572 1.00 41.93  ? 525  TYR B CG    1 
ATOM   858   C  CD1   . TYR A  1  117 ? 28.455  58.318  66.957 1.00 44.97  ? 525  TYR B CD1   1 
ATOM   859   C  CD2   . TYR A  1  117 ? 29.613  59.006  64.972 1.00 44.03  ? 525  TYR B CD2   1 
ATOM   860   C  CE1   . TYR A  1  117 ? 29.587  58.520  67.706 1.00 47.28  ? 525  TYR B CE1   1 
ATOM   861   C  CE2   . TYR A  1  117 ? 30.767  59.231  65.723 1.00 50.44  ? 525  TYR B CE2   1 
ATOM   862   C  CZ    . TYR A  1  117 ? 30.737  58.977  67.087 1.00 48.37  ? 525  TYR B CZ    1 
ATOM   863   O  OH    . TYR A  1  117 ? 31.841  59.179  67.849 1.00 55.29  ? 525  TYR B OH    1 
ATOM   864   N  N     . ARG A  1  118 ? 26.641  60.936  62.992 1.00 40.10  ? 526  ARG B N     1 
ATOM   865   C  CA    . ARG A  1  118 ? 27.197  62.073  62.297 1.00 39.69  ? 526  ARG B CA    1 
ATOM   866   C  C     . ARG A  1  118 ? 26.422  63.365  62.380 1.00 41.00  ? 526  ARG B C     1 
ATOM   867   O  O     . ARG A  1  118 ? 27.036  64.421  62.344 1.00 44.17  ? 526  ARG B O     1 
ATOM   868   C  CB    . ARG A  1  118 ? 27.475  61.722  60.830 1.00 41.05  ? 526  ARG B CB    1 
ATOM   869   C  CG    . ARG A  1  118 ? 28.593  60.686  60.655 1.00 41.24  ? 526  ARG B CG    1 
ATOM   870   C  CD    . ARG A  1  118 ? 29.813  61.093  61.447 1.00 41.37  ? 526  ARG B CD    1 
ATOM   871   N  NE    . ARG A  1  118 ? 30.936  60.199  61.201 1.00 47.65  ? 526  ARG B NE    1 
ATOM   872   C  CZ    . ARG A  1  118 ? 32.087  60.241  61.866 1.00 50.33  ? 526  ARG B CZ    1 
ATOM   873   N  NH1   . ARG A  1  118 ? 32.251  61.108  62.851 1.00 62.77  ? 526  ARG B NH1   1 
ATOM   874   N  NH2   . ARG A  1  118 ? 33.078  59.406  61.565 1.00 47.00  ? 526  ARG B NH2   1 
ATOM   875   N  N     . PHE A  1  119 ? 25.098  63.287  62.453 1.00 39.71  ? 527  PHE B N     1 
ATOM   876   C  CA    . PHE A  1  119 ? 24.231  64.467  62.466 1.00 44.33  ? 527  PHE B CA    1 
ATOM   877   C  C     . PHE A  1  119 ? 23.416  64.683  63.732 1.00 43.81  ? 527  PHE B C     1 
ATOM   878   O  O     . PHE A  1  119 ? 22.868  65.760  63.917 1.00 43.91  ? 527  PHE B O     1 
ATOM   879   C  CB    . PHE A  1  119 ? 23.332  64.479  61.245 1.00 41.30  ? 527  PHE B CB    1 
ATOM   880   C  CG    . PHE A  1  119 ? 24.085  64.721  59.992 1.00 51.07  ? 527  PHE B CG    1 
ATOM   881   C  CD1   . PHE A  1  119 ? 24.745  63.658  59.343 1.00 49.73  ? 527  PHE B CD1   1 
ATOM   882   C  CD2   . PHE A  1  119 ? 24.213  66.015  59.484 1.00 49.09  ? 527  PHE B CD2   1 
ATOM   883   C  CE1   . PHE A  1  119 ? 25.495  63.895  58.202 1.00 53.73  ? 527  PHE B CE1   1 
ATOM   884   C  CE2   . PHE A  1  119 ? 24.946  66.252  58.323 1.00 50.32  ? 527  PHE B CE2   1 
ATOM   885   C  CZ    . PHE A  1  119 ? 25.584  65.192  57.678 1.00 52.94  ? 527  PHE B CZ    1 
ATOM   886   N  N     . MET A  1  120 ? 23.342  63.688  64.602 1.00 39.81  ? 528  MET B N     1 
ATOM   887   C  CA    . MET A  1  120 ? 22.499  63.791  65.778 1.00 38.92  ? 528  MET B CA    1 
ATOM   888   C  C     . MET A  1  120 ? 23.117  63.043  66.932 1.00 39.95  ? 528  MET B C     1 
ATOM   889   O  O     . MET A  1  120 ? 22.425  62.284  67.588 1.00 37.95  ? 528  MET B O     1 
ATOM   890   C  CB    . MET A  1  120 ? 21.094  63.243  65.487 1.00 35.37  ? 528  MET B CB    1 
ATOM   891   C  CG    . MET A  1  120 ? 20.408  63.903  64.294 1.00 37.40  ? 528  MET B CG    1 
ATOM   892   S  SD    . MET A  1  120 ? 18.770  63.205  64.050 1.00 51.96  ? 528  MET B SD    1 
ATOM   893   C  CE    . MET A  1  120 ? 18.112  64.307  62.802 1.00 41.57  ? 528  MET B CE    1 
ATOM   894   N  N     . ARG A  1  121 ? 24.429  63.206  67.155 1.00 40.09  ? 529  ARG B N     1 
ATOM   895   C  CA    . ARG A  1  121 ? 25.111  62.448  68.207 1.00 37.75  ? 529  ARG B CA    1 
ATOM   896   C  C     . ARG A  1  121 ? 24.543  62.633  69.622 1.00 40.86  ? 529  ARG B C     1 
ATOM   897   O  O     . ARG A  1  121 ? 24.553  61.651  70.403 1.00 41.80  ? 529  ARG B O     1 
ATOM   898   C  CB    . ARG A  1  121 ? 26.590  62.760  68.173 1.00 43.69  ? 529  ARG B CB    1 
ATOM   899   C  CG    . ARG A  1  121 ? 27.452  61.906  69.083 1.00 43.17  ? 529  ARG B CG    1 
ATOM   900   C  CD    . ARG A  1  121 ? 28.910  62.117  68.727 1.00 56.24  ? 529  ARG B CD    1 
ATOM   901   N  NE    . ARG A  1  121 ? 29.751  62.277  69.914 1.00 72.98  ? 529  ARG B NE    1 
ATOM   902   C  CZ    . ARG A  1  121 ? 31.022  62.661  69.889 1.00 78.12  ? 529  ARG B CZ    1 
ATOM   903   N  NH1   . ARG A  1  121 ? 31.637  62.881  68.738 1.00 73.80  ? 529  ARG B NH1   1 
ATOM   904   N  NH2   . ARG A  1  121 ? 31.686  62.784  71.021 1.00 86.83  ? 529  ARG B NH2   1 
ATOM   905   N  N     . PRO A  1  122 ? 24.043  63.877  69.980 1.00 43.56  ? 530  PRO B N     1 
ATOM   906   C  CA    . PRO A  1  122 ? 23.516  63.952  71.337 1.00 45.77  ? 530  PRO B CA    1 
ATOM   907   C  C     . PRO A  1  122 ? 22.305  63.053  71.547 1.00 47.14  ? 530  PRO B C     1 
ATOM   908   O  O     . PRO A  1  122 ? 22.083  62.570  72.646 1.00 47.34  ? 530  PRO B O     1 
ATOM   909   C  CB    . PRO A  1  122 ? 23.073  65.411  71.452 1.00 44.28  ? 530  PRO B CB    1 
ATOM   910   C  CG    . PRO A  1  122 ? 23.981  66.132  70.559 1.00 42.51  ? 530  PRO B CG    1 
ATOM   911   C  CD    . PRO A  1  122 ? 23.954  65.227  69.358 1.00 49.25  ? 530  PRO B CD    1 
ATOM   912   N  N     . LEU A  1  123 ? 21.557  62.809  70.487 1.00 42.75  ? 531  LEU B N     1 
ATOM   913   C  CA    . LEU A  1  123 ? 20.452  61.904  70.557 1.00 43.14  ? 531  LEU B CA    1 
ATOM   914   C  C     . LEU A  1  123 ? 20.905  60.513  70.997 1.00 41.96  ? 531  LEU B C     1 
ATOM   915   O  O     . LEU A  1  123 ? 20.246  59.879  71.809 1.00 42.22  ? 531  LEU B O     1 
ATOM   916   C  CB    . LEU A  1  123 ? 19.843  61.836  69.200 1.00 46.02  ? 531  LEU B CB    1 
ATOM   917   C  CG    . LEU A  1  123 ? 18.421  61.369  69.030 1.00 47.35  ? 531  LEU B CG    1 
ATOM   918   C  CD1   . LEU A  1  123 ? 17.498  62.563  69.191 1.00 50.36  ? 531  LEU B CD1   1 
ATOM   919   C  CD2   . LEU A  1  123 ? 18.282  60.909  67.607 1.00 48.00  ? 531  LEU B CD2   1 
ATOM   920   N  N     . ILE A  1  124 ? 22.064  60.071  70.525 1.00 39.81  ? 532  ILE B N     1 
ATOM   921   C  CA    . ILE A  1  124 ? 22.595  58.805  71.010 1.00 44.96  ? 532  ILE B CA    1 
ATOM   922   C  C     . ILE A  1  124 ? 23.117  58.934  72.439 1.00 50.94  ? 532  ILE B C     1 
ATOM   923   O  O     . ILE A  1  124 ? 22.954  58.020  73.235 1.00 44.80  ? 532  ILE B O     1 
ATOM   924   C  CB    . ILE A  1  124 ? 23.729  58.290  70.133 1.00 43.49  ? 532  ILE B CB    1 
ATOM   925   C  CG1   . ILE A  1  124 ? 23.265  58.167  68.675 1.00 41.18  ? 532  ILE B CG1   1 
ATOM   926   C  CG2   . ILE A  1  124 ? 24.239  56.949  70.663 1.00 44.05  ? 532  ILE B CG2   1 
ATOM   927   C  CD1   . ILE A  1  124 ? 24.359  57.854  67.704 1.00 37.79  ? 532  ILE B CD1   1 
ATOM   928   N  N     . GLU A  1  125 ? 23.756  60.071  72.733 1.00 53.87  ? 533  GLU B N     1 
ATOM   929   C  CA    . GLU A  1  125 ? 24.359  60.307  74.030 1.00 50.56  ? 533  GLU B CA    1 
ATOM   930   C  C     . GLU A  1  125 ? 23.302  60.355  75.110 1.00 51.16  ? 533  GLU B C     1 
ATOM   931   O  O     . GLU A  1  125 ? 23.501  59.806  76.166 1.00 52.01  ? 533  GLU B O     1 
ATOM   932   C  CB    . GLU A  1  125 ? 25.131  61.604  73.994 1.00 51.42  ? 533  GLU B CB    1 
ATOM   933   C  CG    . GLU A  1  125 ? 26.514  61.391  73.438 1.00 59.29  ? 533  GLU B CG    1 
ATOM   934   C  CD    . GLU A  1  125 ? 27.231  62.675  73.034 1.00 61.77  ? 533  GLU B CD    1 
ATOM   935   O  OE1   . GLU A  1  125 ? 26.610  63.728  72.782 1.00 56.00  ? 533  GLU B OE1   1 
ATOM   936   O  OE2   . GLU A  1  125 ? 28.472  62.618  72.953 1.00 71.34  ? 533  GLU B OE2   1 
ATOM   937   N  N     . ALA A  1  126 ? 22.159  60.957  74.779 1.00 45.85  ? 534  ALA B N     1 
ATOM   938   C  CA    . ALA A  1  126 ? 21.029  61.036  75.641 1.00 41.85  ? 534  ALA B CA    1 
ATOM   939   C  C     . ALA A  1  126 ? 20.377  59.703  75.916 1.00 46.58  ? 534  ALA B C     1 
ATOM   940   O  O     . ALA A  1  126 ? 19.619  59.582  76.856 1.00 49.76  ? 534  ALA B O     1 
ATOM   941   C  CB    . ALA A  1  126 ? 20.010  62.005  75.061 1.00 39.06  ? 534  ALA B CB    1 
ATOM   942   N  N     . GLY A  1  127 ? 20.618  58.701  75.087 1.00 48.74  ? 535  GLY B N     1 
ATOM   943   C  CA    . GLY A  1  127 ? 20.044  57.383  75.344 1.00 47.03  ? 535  GLY B CA    1 
ATOM   944   C  C     . GLY A  1  127 ? 18.726  57.191  74.649 1.00 46.79  ? 535  GLY B C     1 
ATOM   945   O  O     . GLY A  1  127 ? 18.033  56.248  74.981 1.00 46.01  ? 535  GLY B O     1 
ATOM   946   N  N     . TYR A  1  128 ? 18.420  58.036  73.660 1.00 42.40  ? 536  TYR B N     1 
ATOM   947   C  CA    . TYR A  1  128 ? 17.118  58.044  73.015 1.00 46.41  ? 536  TYR B CA    1 
ATOM   948   C  C     . TYR A  1  128 ? 17.037  57.021  71.854 1.00 47.28  ? 536  TYR B C     1 
ATOM   949   O  O     . TYR A  1  128 ? 15.946  56.748  71.343 1.00 41.95  ? 536  TYR B O     1 
ATOM   950   C  CB    . TYR A  1  128 ? 16.824  59.430  72.471 1.00 44.08  ? 536  TYR B CB    1 
ATOM   951   C  CG    . TYR A  1  128 ? 16.459  60.491  73.469 1.00 46.17  ? 536  TYR B CG    1 
ATOM   952   C  CD1   . TYR A  1  128 ? 16.561  60.270  74.845 1.00 50.53  ? 536  TYR B CD1   1 
ATOM   953   C  CD2   . TYR A  1  128 ? 16.014  61.756  73.028 1.00 47.66  ? 536  TYR B CD2   1 
ATOM   954   C  CE1   . TYR A  1  128 ? 16.237  61.276  75.753 1.00 45.25  ? 536  TYR B CE1   1 
ATOM   955   C  CE2   . TYR A  1  128 ? 15.675  62.756  73.924 1.00 45.40  ? 536  TYR B CE2   1 
ATOM   956   C  CZ    . TYR A  1  128 ? 15.798  62.507  75.276 1.00 46.57  ? 536  TYR B CZ    1 
ATOM   957   O  OH    . TYR A  1  128 ? 15.475  63.493  76.153 1.00 50.04  ? 536  TYR B OH    1 
ATOM   958   N  N     . VAL A  1  129 ? 18.183  56.467  71.444 1.00 47.47  ? 537  VAL B N     1 
ATOM   959   C  CA    . VAL A  1  129 ? 18.212  55.633  70.271 1.00 40.49  ? 537  VAL B CA    1 
ATOM   960   C  C     . VAL A  1  129 ? 18.193  54.171  70.652 1.00 42.01  ? 537  VAL B C     1 
ATOM   961   O  O     . VAL A  1  129 ? 18.972  53.731  71.437 1.00 40.51  ? 537  VAL B O     1 
ATOM   962   C  CB    . VAL A  1  129 ? 19.413  55.952  69.390 1.00 41.77  ? 537  VAL B CB    1 
ATOM   963   C  CG1   . VAL A  1  129 ? 19.490  54.982  68.237 1.00 41.11  ? 537  VAL B CG1   1 
ATOM   964   C  CG2   . VAL A  1  129 ? 19.308  57.353  68.844 1.00 35.37  ? 537  VAL B CG2   1 
ATOM   965   N  N     . TYR A  1  130 ? 17.262  53.414  70.100 1.00 43.32  ? 538  TYR B N     1 
ATOM   966   C  CA    . TYR A  1  130 ? 17.162  51.985  70.402 1.00 41.17  ? 538  TYR B CA    1 
ATOM   967   C  C     . TYR A  1  130 ? 17.090  51.103  69.149 1.00 40.20  ? 538  TYR B C     1 
ATOM   968   O  O     . TYR A  1  130 ? 16.845  51.566  68.018 1.00 42.48  ? 538  TYR B O     1 
ATOM   969   C  CB    . TYR A  1  130 ? 15.900  51.724  71.217 1.00 43.90  ? 538  TYR B CB    1 
ATOM   970   C  CG    . TYR A  1  130 ? 15.792  52.464  72.537 1.00 48.02  ? 538  TYR B CG    1 
ATOM   971   C  CD1   . TYR A  1  130 ? 15.433  53.833  72.571 1.00 46.74  ? 538  TYR B CD1   1 
ATOM   972   C  CD2   . TYR A  1  130 ? 16.003  51.792  73.749 1.00 43.30  ? 538  TYR B CD2   1 
ATOM   973   C  CE1   . TYR A  1  130 ? 15.311  54.510  73.762 1.00 47.35  ? 538  TYR B CE1   1 
ATOM   974   C  CE2   . TYR A  1  130 ? 15.867  52.472  74.953 1.00 45.48  ? 538  TYR B CE2   1 
ATOM   975   C  CZ    . TYR A  1  130 ? 15.538  53.833  74.939 1.00 50.59  ? 538  TYR B CZ    1 
ATOM   976   O  OH    . TYR A  1  130 ? 15.399  54.543  76.108 1.00 50.45  ? 538  TYR B OH    1 
ATOM   977   N  N     . ILE A  1  131 ? 17.268  49.804  69.360 1.00 42.04  ? 539  ILE B N     1 
ATOM   978   C  CA    . ILE A  1  131 ? 17.124  48.802  68.323 1.00 40.55  ? 539  ILE B CA    1 
ATOM   979   C  C     . ILE A  1  131 ? 16.123  47.746  68.766 1.00 40.35  ? 539  ILE B C     1 
ATOM   980   O  O     . ILE A  1  131 ? 16.289  47.098  69.804 1.00 45.82  ? 539  ILE B O     1 
ATOM   981   C  CB    . ILE A  1  131 ? 18.466  48.135  68.018 1.00 41.83  ? 539  ILE B CB    1 
ATOM   982   C  CG1   . ILE A  1  131 ? 19.458  49.192  67.503 1.00 41.80  ? 539  ILE B CG1   1 
ATOM   983   C  CG2   . ILE A  1  131 ? 18.302  47.015  66.989 1.00 34.24  ? 539  ILE B CG2   1 
ATOM   984   C  CD1   . ILE A  1  131 ? 20.863  48.628  67.395 1.00 38.27  ? 539  ILE B CD1   1 
ATOM   985   N  N     . ALA A  1  132 ? 15.099  47.536  67.938 1.00 39.54  ? 540  ALA B N     1 
ATOM   986   C  CA    . ALA A  1  132 ? 14.043  46.559  68.213 1.00 35.27  ? 540  ALA B CA    1 
ATOM   987   C  C     . ALA A  1  132 ? 14.581  45.214  67.901 1.00 38.98  ? 540  ALA B C     1 
ATOM   988   O  O     . ALA A  1  132 ? 15.525  45.088  67.144 1.00 40.19  ? 540  ALA B O     1 
ATOM   989   C  CB    . ALA A  1  132 ? 12.878  46.811  67.298 1.00 32.95  ? 540  ALA B CB    1 
ATOM   990   N  N     . GLN A  1  133 ? 13.948  44.179  68.403 1.00 41.90  ? 541  GLN B N     1 
ATOM   991   C  CA    . GLN A  1  133 ? 14.476  42.858  68.117 1.00 47.57  ? 541  GLN B CA    1 
ATOM   992   C  C     . GLN A  1  133 ? 13.389  41.905  67.685 1.00 50.08  ? 541  GLN B C     1 
ATOM   993   O  O     . GLN A  1  133 ? 12.966  41.077  68.458 1.00 56.55  ? 541  GLN B O     1 
ATOM   994   C  CB    . GLN A  1  133 ? 15.166  42.309  69.344 1.00 51.20  ? 541  GLN B CB    1 
ATOM   995   C  CG    . GLN A  1  133 ? 16.370  43.099  69.807 1.00 52.19  ? 541  GLN B CG    1 
ATOM   996   C  CD    . GLN A  1  133 ? 17.257  42.237  70.657 1.00 53.71  ? 541  GLN B CD    1 
ATOM   997   O  OE1   . GLN A  1  133 ? 16.911  41.903  71.785 1.00 57.96  ? 541  GLN B OE1   1 
ATOM   998   N  NE2   . GLN A  1  133 ? 18.388  41.820  70.106 1.00 55.74  ? 541  GLN B NE2   1 
ATOM   999   N  N     . PRO A  1  134 ? 12.935  41.997  66.452 1.00 48.45  ? 542  PRO B N     1 
ATOM   1000  C  CA    . PRO A  1  134 ? 11.816  41.159  66.021 1.00 50.70  ? 542  PRO B CA    1 
ATOM   1001  C  C     . PRO A  1  134 ? 12.248  39.707  65.998 1.00 51.94  ? 542  PRO B C     1 
ATOM   1002  O  O     . PRO A  1  134 ? 13.478  39.463  65.942 1.00 60.96  ? 542  PRO B O     1 
ATOM   1003  C  CB    . PRO A  1  134 ? 11.558  41.637  64.592 1.00 49.13  ? 542  PRO B CB    1 
ATOM   1004  C  CG    . PRO A  1  134 ? 12.287  42.905  64.451 1.00 51.25  ? 542  PRO B CG    1 
ATOM   1005  C  CD    . PRO A  1  134 ? 13.439  42.861  65.380 1.00 46.42  ? 542  PRO B CD    1 
ATOM   1006  N  N     . PRO A  1  135 ? 11.278  38.750  66.037 1.00 49.17  ? 543  PRO B N     1 
ATOM   1007  C  CA    . PRO A  1  135 ? 11.797  37.370  66.026 1.00 52.56  ? 543  PRO B CA    1 
ATOM   1008  C  C     . PRO A  1  135 ? 12.224  36.887  64.635 1.00 65.50  ? 543  PRO B C     1 
ATOM   1009  O  O     . PRO A  1  135 ? 11.706  37.347  63.591 1.00 63.68  ? 543  PRO B O     1 
ATOM   1010  C  CB    . PRO A  1  135 ? 10.598  36.534  66.487 1.00 51.89  ? 543  PRO B CB    1 
ATOM   1011  C  CG    . PRO A  1  135 ? 9.416   37.289  65.984 1.00 48.95  ? 543  PRO B CG    1 
ATOM   1012  C  CD    . PRO A  1  135 ? 9.788   38.762  66.086 1.00 45.34  ? 543  PRO B CD    1 
ATOM   1013  N  N     . THR A  1  136 ? 13.151  35.950  64.638 1.00 76.63  ? 544  THR B N     1 
ATOM   1014  C  CA    . THR A  1  136 ? 13.627  35.348  63.407 1.00 85.08  ? 544  THR B CA    1 
ATOM   1015  C  C     . THR A  1  136 ? 12.619  34.289  62.938 1.00 91.33  ? 544  THR B C     1 
ATOM   1016  O  O     . THR A  1  136 ? 11.648  33.963  63.660 1.00 82.98  ? 544  THR B O     1 
ATOM   1017  C  CB    . THR A  1  136 ? 15.012  34.736  63.625 1.00 81.49  ? 544  THR B CB    1 
ATOM   1018  O  OG1   . THR A  1  136 ? 14.933  33.772  64.675 1.00 81.75  ? 544  THR B OG1   1 
ATOM   1019  C  CG2   . THR A  1  136 ? 15.976  35.802  64.051 1.00 79.21  ? 544  THR B CG2   1 
ATOM   1020  N  N     . GLY A  1  137 ? 12.830  33.811  61.708 1.00 90.89  ? 545  GLY B N     1 
ATOM   1021  C  CA    . GLY A  1  137 ? 11.991  32.808  61.071 1.00 86.67  ? 545  GLY B CA    1 
ATOM   1022  C  C     . GLY A  1  137 ? 10.989  33.418  60.125 1.00 90.37  ? 545  GLY B C     1 
ATOM   1023  O  O     . GLY A  1  137 ? 10.098  32.744  59.627 1.00 83.66  ? 545  GLY B O     1 
ATOM   1024  N  N     A TYR A  1  138 ? 11.137  34.688  59.786 0.50 85.77  ? 580  TYR B N     1 
ATOM   1025  N  N     B TYR A  1  138 ? 11.156  34.714  59.918 0.50 98.23  ? 580  TYR B N     1 
ATOM   1026  C  CA    A TYR A  1  138 ? 10.019  35.322  59.133 0.50 81.13  ? 580  TYR B CA    1 
ATOM   1027  C  CA    B TYR A  1  138 ? 10.277  35.437  59.057 0.50 101.79 ? 580  TYR B CA    1 
ATOM   1028  C  C     A TYR A  1  138 ? 10.239  35.719  57.662 0.50 75.62  ? 580  TYR B C     1 
ATOM   1029  C  C     B TYR A  1  138 ? 11.024  35.972  57.866 0.50 95.17  ? 580  TYR B C     1 
ATOM   1030  O  O     A TYR A  1  138 ? 9.310   35.682  56.846 0.50 61.73  ? 580  TYR B O     1 
ATOM   1031  O  O     B TYR A  1  138 ? 12.124  36.518  57.998 0.50 86.43  ? 580  TYR B O     1 
ATOM   1032  C  CB    A TYR A  1  138 ? 9.480   36.455  60.003 0.50 75.87  ? 580  TYR B CB    1 
ATOM   1033  C  CB    B TYR A  1  138 ? 9.619   36.566  59.816 0.50 106.15 ? 580  TYR B CB    1 
ATOM   1034  C  CG    A TYR A  1  138 ? 8.363   36.041  60.957 0.50 67.90  ? 580  TYR B CG    1 
ATOM   1035  C  CG    B TYR A  1  138 ? 8.644   36.116  60.874 0.50 105.97 ? 580  TYR B CG    1 
ATOM   1036  C  CD1   A TYR A  1  138 ? 7.096   35.728  60.474 0.50 69.49  ? 580  TYR B CD1   1 
ATOM   1037  C  CD1   B TYR A  1  138 ? 7.333   35.792  60.552 0.50 108.72 ? 580  TYR B CD1   1 
ATOM   1038  C  CD2   A TYR A  1  138 ? 8.557   35.993  62.331 0.50 63.56  ? 580  TYR B CD2   1 
ATOM   1039  C  CD2   B TYR A  1  138 ? 9.026   36.042  62.194 0.50 103.76 ? 580  TYR B CD2   1 
ATOM   1040  C  CE1   A TYR A  1  138 ? 6.062   35.364  61.322 0.50 63.66  ? 580  TYR B CE1   1 
ATOM   1041  C  CE1   B TYR A  1  138 ? 6.433   35.394  61.524 0.50 108.95 ? 580  TYR B CE1   1 
ATOM   1042  C  CE2   A TYR A  1  138 ? 7.524   35.631  63.183 0.50 60.71  ? 580  TYR B CE2   1 
ATOM   1043  C  CE2   B TYR A  1  138 ? 8.138   35.661  63.179 0.50 104.93 ? 580  TYR B CE2   1 
ATOM   1044  C  CZ    A TYR A  1  138 ? 6.271   35.323  62.671 0.50 65.15  ? 580  TYR B CZ    1 
ATOM   1045  C  CZ    B TYR A  1  138 ? 6.836   35.335  62.841 0.50 110.33 ? 580  TYR B CZ    1 
ATOM   1046  O  OH    A TYR A  1  138 ? 5.212   34.953  63.488 0.50 61.71  ? 580  TYR B OH    1 
ATOM   1047  O  OH    B TYR A  1  138 ? 5.921   34.943  63.804 0.50 115.98 ? 580  TYR B OH    1 
ATOM   1048  N  N     A LYS A  1  139 ? 11.483  36.065  57.329 0.50 72.54  ? 581  LYS B N     1 
ATOM   1049  N  N     B LYS A  1  139 ? 10.393  35.816  56.705 0.50 88.58  ? 581  LYS B N     1 
ATOM   1050  C  CA    A LYS A  1  139 ? 11.812  36.519  55.979 0.50 71.64  ? 581  LYS B CA    1 
ATOM   1051  C  CA    B LYS A  1  139 ? 10.887  36.340  55.446 0.50 88.10  ? 581  LYS B CA    1 
ATOM   1052  C  C     A LYS A  1  139 ? 11.044  37.813  55.648 0.50 69.30  ? 581  LYS B C     1 
ATOM   1053  C  C     B LYS A  1  139 ? 10.606  37.840  55.325 0.50 81.14  ? 581  LYS B C     1 
ATOM   1054  O  O     A LYS A  1  139 ? 10.585  37.997  54.521 0.50 66.10  ? 581  LYS B O     1 
ATOM   1055  O  O     B LYS A  1  139 ? 10.368  38.336  54.231 0.50 80.55  ? 581  LYS B O     1 
ATOM   1056  C  CB    A LYS A  1  139 ? 11.517  35.404  54.954 0.50 69.78  ? 581  LYS B CB    1 
ATOM   1057  C  CB    B LYS A  1  139 ? 10.219  35.584  54.288 0.50 92.01  ? 581  LYS B CB    1 
ATOM   1058  C  CG    A LYS A  1  139 ? 11.280  35.857  53.504 0.50 64.40  ? 581  LYS B CG    1 
ATOM   1059  C  CG    B LYS A  1  139 ? 10.758  35.876  52.890 0.50 82.42  ? 581  LYS B CG    1 
ATOM   1060  C  CD    A LYS A  1  139 ? 10.134  35.084  52.838 0.50 55.67  ? 581  LYS B CD    1 
ATOM   1061  C  CD    B LYS A  1  139 ? 10.432  34.713  51.967 0.50 79.32  ? 581  LYS B CD    1 
ATOM   1062  C  CE    A LYS A  1  139 ? 8.753   35.592  53.283 0.50 52.98  ? 581  LYS B CE    1 
ATOM   1063  C  CE    B LYS A  1  139 ? 10.408  35.112  50.501 0.50 78.28  ? 581  LYS B CE    1 
ATOM   1064  N  NZ    A LYS A  1  139 ? 7.571   34.681  53.121 0.50 44.86  ? 581  LYS B NZ    1 
ATOM   1065  N  NZ    B LYS A  1  139 ? 10.545  33.925  49.612 0.50 75.78  ? 581  LYS B NZ    1 
ATOM   1066  N  N     A GLY A  1  140 ? 10.895  38.705  56.632 0.50 67.21  ? 582  GLY B N     1 
ATOM   1067  N  N     B GLY A  1  140 ? 10.621  38.549  56.454 0.50 75.76  ? 582  GLY B N     1 
ATOM   1068  C  CA    A GLY A  1  140 ? 10.323  39.986  56.360 0.50 60.28  ? 582  GLY B CA    1 
ATOM   1069  C  CA    B GLY A  1  140 ? 10.477  39.983  56.452 0.50 64.73  ? 582  GLY B CA    1 
ATOM   1070  C  C     A GLY A  1  140 ? 9.305   40.400  57.372 0.50 55.85  ? 582  GLY B C     1 
ATOM   1071  C  C     B GLY A  1  140 ? 9.386   40.392  57.395 0.50 58.52  ? 582  GLY B C     1 
ATOM   1072  O  O     A GLY A  1  140 ? 8.478   39.616  57.837 0.50 52.03  ? 582  GLY B O     1 
ATOM   1073  O  O     B GLY A  1  140 ? 8.597   39.587  57.851 0.50 55.37  ? 582  GLY B O     1 
ATOM   1074  N  N     . LEU A  1  141 ? 9.293   41.667  57.645 1.00 53.52  ? 583  LEU B N     1 
ATOM   1075  C  CA    . LEU A  1  141 ? 8.347   42.130  58.594 1.00 49.69  ? 583  LEU B CA    1 
ATOM   1076  C  C     . LEU A  1  141 ? 6.948   42.218  58.061 1.00 49.66  ? 583  LEU B C     1 
ATOM   1077  O  O     . LEU A  1  141 ? 5.996   42.095  58.858 1.00 45.80  ? 583  LEU B O     1 
ATOM   1078  C  CB    . LEU A  1  141 ? 8.840   43.408  59.161 1.00 51.63  ? 583  LEU B CB    1 
ATOM   1079  C  CG    . LEU A  1  141 ? 9.882   43.350  60.298 1.00 50.55  ? 583  LEU B CG    1 
ATOM   1080  C  CD1   . LEU A  1  141 ? 10.542  44.697  60.466 1.00 44.49  ? 583  LEU B CD1   1 
ATOM   1081  C  CD2   . LEU A  1  141 ? 9.319   42.898  61.646 1.00 47.02  ? 583  LEU B CD2   1 
ATOM   1082  N  N     . GLY A  1  142 ? 6.853   42.441  56.734 1.00 44.60  ? 584  GLY B N     1 
ATOM   1083  C  CA    . GLY A  1  142 ? 5.651   42.268  55.955 1.00 40.57  ? 584  GLY B CA    1 
ATOM   1084  C  C     . GLY A  1  142 ? 5.042   40.876  56.155 1.00 46.33  ? 584  GLY B C     1 
ATOM   1085  O  O     . GLY A  1  142 ? 3.827   40.693  55.894 1.00 35.41  ? 584  GLY B O     1 
ATOM   1086  N  N     . GLU A  1  143 ? 5.855   39.937  56.663 1.00 45.61  ? 585  GLU B N     1 
ATOM   1087  C  CA    . GLU A  1  143 ? 5.462   38.557  56.820 1.00 49.18  ? 585  GLU B CA    1 
ATOM   1088  C  C     . GLU A  1  143 ? 4.668   38.358  58.122 1.00 47.30  ? 585  GLU B C     1 
ATOM   1089  O  O     . GLU A  1  143 ? 3.892   37.376  58.264 1.00 40.73  ? 585  GLU B O     1 
ATOM   1090  C  CB    . GLU A  1  143 ? 6.705   37.660  56.851 1.00 60.20  ? 585  GLU B CB    1 
ATOM   1091  C  CG    . GLU A  1  143 ? 6.640   36.433  55.992 1.00 78.87  ? 585  GLU B CG    1 
ATOM   1092  C  CD    . GLU A  1  143 ? 5.571   35.482  56.414 1.00 82.94  ? 585  GLU B CD    1 
ATOM   1093  O  OE1   . GLU A  1  143 ? 5.841   34.677  57.308 1.00 82.12  ? 585  GLU B OE1   1 
ATOM   1094  O  OE2   . GLU A  1  143 ? 4.462   35.537  55.830 1.00 86.75  ? 585  GLU B OE2   1 
ATOM   1095  N  N     . MET A  1  144 ? 4.882   39.251  59.085 1.00 37.41  ? 586  MET B N     1 
ATOM   1096  C  CA    . MET A  1  144 ? 4.221   39.092  60.363 1.00 42.74  ? 586  MET B CA    1 
ATOM   1097  C  C     . MET A  1  144 ? 2.835   39.728  60.405 1.00 46.27  ? 586  MET B C     1 
ATOM   1098  O  O     . MET A  1  144 ? 2.620   40.781  59.837 1.00 46.41  ? 586  MET B O     1 
ATOM   1099  C  CB    . MET A  1  144 ? 5.087   39.660  61.474 1.00 45.15  ? 586  MET B CB    1 
ATOM   1100  C  CG    . MET A  1  144 ? 6.373   38.869  61.683 1.00 51.64  ? 586  MET B CG    1 
ATOM   1101  S  SD    . MET A  1  144 ? 7.532   39.741  62.725 1.00 57.02  ? 586  MET B SD    1 
ATOM   1102  C  CE    . MET A  1  144 ? 6.755   39.518  64.309 1.00 38.04  ? 586  MET B CE    1 
ATOM   1103  N  N     . ASN A  1  145 ? 1.907   39.080  61.104 1.00 50.47  ? 587  ASN B N     1 
ATOM   1104  C  CA    . ASN A  1  145 ? 0.585   39.666  61.386 1.00 47.77  ? 587  ASN B CA    1 
ATOM   1105  C  C     . ASN A  1  145 ? 0.809   40.742  62.413 1.00 48.74  ? 587  ASN B C     1 
ATOM   1106  O  O     . ASN A  1  145 ? 1.782   40.698  63.167 1.00 41.85  ? 587  ASN B O     1 
ATOM   1107  C  CB    . ASN A  1  145 ? -0.352  38.638  61.978 1.00 39.80  ? 587  ASN B CB    1 
ATOM   1108  C  CG    . ASN A  1  145 ? -0.686  37.521  61.001 1.00 44.06  ? 587  ASN B CG    1 
ATOM   1109  O  OD1   . ASN A  1  145 ? -0.692  37.678  59.778 1.00 42.32  ? 587  ASN B OD1   1 
ATOM   1110  N  ND2   . ASN A  1  145 ? -0.962  36.365  61.551 1.00 46.31  ? 587  ASN B ND2   1 
ATOM   1111  N  N     . ALA A  1  146 ? -0.090  41.701  62.445 1.00 48.43  ? 588  ALA B N     1 
ATOM   1112  C  CA    . ALA A  1  146 ? 0.031   42.826  63.313 1.00 44.57  ? 588  ALA B CA    1 
ATOM   1113  C  C     . ALA A  1  146 ? 0.073   42.484  64.804 1.00 47.55  ? 588  ALA B C     1 
ATOM   1114  O  O     . ALA A  1  146 ? 0.757   43.149  65.545 1.00 44.69  ? 588  ALA B O     1 
ATOM   1115  C  CB    . ALA A  1  146 ? -1.101  43.782  63.037 1.00 48.98  ? 588  ALA B CB    1 
ATOM   1116  N  N     . ASP A  1  147 ? -0.688  41.485  65.248 1.00 45.81  ? 589  ASP B N     1 
ATOM   1117  C  CA    . ASP A  1  147 ? -0.696  41.151  66.667 1.00 45.13  ? 589  ASP B CA    1 
ATOM   1118  C  C     . ASP A  1  147 ? 0.655   40.558  67.101 1.00 46.79  ? 589  ASP B C     1 
ATOM   1119  O  O     . ASP A  1  147 ? 1.106   40.811  68.201 1.00 41.35  ? 589  ASP B O     1 
ATOM   1120  C  CB    . ASP A  1  147 ? -1.885  40.253  67.002 1.00 51.43  ? 589  ASP B CB    1 
ATOM   1121  C  CG    . ASP A  1  147 ? -1.787  38.844  66.388 1.00 59.98  ? 589  ASP B CG    1 
ATOM   1122  O  OD1   . ASP A  1  147 ? -1.087  38.622  65.382 1.00 68.41  ? 589  ASP B OD1   1 
ATOM   1123  O  OD2   . ASP A  1  147 ? -2.434  37.929  66.933 1.00 73.22  ? 589  ASP B OD2   1 
ATOM   1124  N  N     . GLN A  1  148 ? 1.300   39.808  66.199 1.00 47.04  ? 590  GLN B N     1 
ATOM   1125  C  CA    . GLN A  1  148 ? 2.613   39.236  66.470 1.00 51.00  ? 590  GLN B CA    1 
ATOM   1126  C  C     . GLN A  1  148 ? 3.668   40.334  66.604 1.00 52.38  ? 590  GLN B C     1 
ATOM   1127  O  O     . GLN A  1  148 ? 4.525   40.251  67.463 1.00 52.46  ? 590  GLN B O     1 
ATOM   1128  C  CB    . GLN A  1  148 ? 3.031   38.277  65.382 1.00 48.75  ? 590  GLN B CB    1 
ATOM   1129  C  CG    . GLN A  1  148 ? 2.221   37.009  65.315 1.00 58.18  ? 590  GLN B CG    1 
ATOM   1130  C  CD    . GLN A  1  148 ? 2.282   36.336  63.936 1.00 65.96  ? 590  GLN B CD    1 
ATOM   1131  O  OE1   . GLN A  1  148 ? 2.708   36.924  62.919 1.00 59.13  ? 590  GLN B OE1   1 
ATOM   1132  N  NE2   . GLN A  1  148 ? 1.861   35.080  63.903 1.00 63.59  ? 590  GLN B NE2   1 
ATOM   1133  N  N     . LEU A  1  149 ? 3.593   41.347  65.737 1.00 50.85  ? 591  LEU B N     1 
ATOM   1134  C  CA    . LEU A  1  149 ? 4.478   42.512  65.771 1.00 50.39  ? 591  LEU B CA    1 
ATOM   1135  C  C     . LEU A  1  149 ? 4.357   43.250  67.096 1.00 54.18  ? 591  LEU B C     1 
ATOM   1136  O  O     . LEU A  1  149 ? 5.362   43.609  67.699 1.00 50.73  ? 591  LEU B O     1 
ATOM   1137  C  CB    . LEU A  1  149 ? 4.104   43.476  64.659 1.00 51.04  ? 591  LEU B CB    1 
ATOM   1138  C  CG    . LEU A  1  149 ? 5.159   43.973  63.676 1.00 58.79  ? 591  LEU B CG    1 
ATOM   1139  C  CD1   . LEU A  1  149 ? 6.450   43.181  63.799 1.00 58.96  ? 591  LEU B CD1   1 
ATOM   1140  C  CD2   . LEU A  1  149 ? 4.574   43.873  62.266 1.00 57.82  ? 591  LEU B CD2   1 
ATOM   1141  N  N     . TRP A  1  150 ? 3.121   43.415  67.572 1.00 45.71  ? 592  TRP B N     1 
ATOM   1142  C  CA    . TRP A  1  150 ? 2.887   44.105  68.814 1.00 47.50  ? 592  TRP B CA    1 
ATOM   1143  C  C     . TRP A  1  150 ? 3.423   43.365  70.047 1.00 50.22  ? 592  TRP B C     1 
ATOM   1144  O  O     . TRP A  1  150 ? 4.038   43.974  70.911 1.00 53.93  ? 592  TRP B O     1 
ATOM   1145  C  CB    . TRP A  1  150 ? 1.387   44.400  68.959 1.00 47.57  ? 592  TRP B CB    1 
ATOM   1146  C  CG    . TRP A  1  150 ? 0.938   44.714  70.370 1.00 42.98  ? 592  TRP B CG    1 
ATOM   1147  C  CD1   . TRP A  1  150 ? 0.251   43.889  71.194 1.00 41.10  ? 592  TRP B CD1   1 
ATOM   1148  C  CD2   . TRP A  1  150 ? 1.156   45.929  71.089 1.00 42.21  ? 592  TRP B CD2   1 
ATOM   1149  N  NE1   . TRP A  1  150 ? 0.006   44.517  72.390 1.00 42.85  ? 592  TRP B NE1   1 
ATOM   1150  C  CE2   . TRP A  1  150 ? 0.555   45.770  72.353 1.00 43.99  ? 592  TRP B CE2   1 
ATOM   1151  C  CE3   . TRP A  1  150 ? 1.808   47.139  70.792 1.00 44.80  ? 592  TRP B CE3   1 
ATOM   1152  C  CZ2   . TRP A  1  150 ? 0.572   46.773  73.323 1.00 43.91  ? 592  TRP B CZ2   1 
ATOM   1153  C  CZ3   . TRP A  1  150 ? 1.832   48.131  71.763 1.00 46.11  ? 592  TRP B CZ3   1 
ATOM   1154  C  CH2   . TRP A  1  150 ? 1.213   47.940  73.014 1.00 44.28  ? 592  TRP B CH2   1 
ATOM   1155  N  N     . GLU A  1  151 ? 3.175   42.065  70.120 1.00 46.14  ? 593  GLU B N     1 
ATOM   1156  C  CA    . GLU A  1  151 ? 3.543   41.305  71.295 1.00 49.61  ? 593  GLU B CA    1 
ATOM   1157  C  C     . GLU A  1  151 ? 5.021   41.072  71.411 1.00 55.42  ? 593  GLU B C     1 
ATOM   1158  O  O     . GLU A  1  151 ? 5.589   41.162  72.492 1.00 58.02  ? 593  GLU B O     1 
ATOM   1159  C  CB    . GLU A  1  151 ? 2.880   39.933  71.258 1.00 49.22  ? 593  GLU B CB    1 
ATOM   1160  C  CG    . GLU A  1  151 ? 1.390   39.966  71.511 1.00 58.09  ? 593  GLU B CG    1 
ATOM   1161  C  CD    . GLU A  1  151 ? 1.029   40.617  72.842 1.00 69.41  ? 593  GLU B CD    1 
ATOM   1162  O  OE1   . GLU A  1  151 ? 1.926   40.860  73.706 1.00 65.32  ? 593  GLU B OE1   1 
ATOM   1163  O  OE2   . GLU A  1  151 ? -0.179  40.881  73.020 1.00 74.77  ? 593  GLU B OE2   1 
ATOM   1164  N  N     . THR A  1  152 ? 5.649   40.798  70.286 1.00 53.20  ? 594  THR B N     1 
ATOM   1165  C  CA    . THR A  1  152 ? 7.041   40.459  70.297 1.00 51.73  ? 594  THR B CA    1 
ATOM   1166  C  C     . THR A  1  152 ? 7.968   41.636  70.271 1.00 50.14  ? 594  THR B C     1 
ATOM   1167  O  O     . THR A  1  152 ? 9.052   41.535  70.811 1.00 54.97  ? 594  THR B O     1 
ATOM   1168  C  CB    . THR A  1  152 ? 7.364   39.501  69.153 1.00 52.63  ? 594  THR B CB    1 
ATOM   1169  O  OG1   . THR A  1  152 ? 7.199   40.171  67.881 1.00 52.14  ? 594  THR B OG1   1 
ATOM   1170  C  CG2   . THR A  1  152 ? 6.448   38.285  69.266 1.00 45.34  ? 594  THR B CG2   1 
ATOM   1171  N  N     . THR A  1  153 ? 7.559   42.752  69.681 1.00 46.95  ? 595  THR B N     1 
ATOM   1172  C  CA    . THR A  1  153 ? 8.477   43.822  69.399 1.00 44.38  ? 595  THR B CA    1 
ATOM   1173  C  C     . THR A  1  153 ? 8.026   45.213  69.821 1.00 48.22  ? 595  THR B C     1 
ATOM   1174  O  O     . THR A  1  153 ? 8.855   46.087  70.022 1.00 49.36  ? 595  THR B O     1 
ATOM   1175  C  CB    . THR A  1  153 ? 8.707   43.790  67.891 1.00 47.66  ? 595  THR B CB    1 
ATOM   1176  O  OG1   . THR A  1  153 ? 8.674   42.414  67.498 1.00 47.88  ? 595  THR B OG1   1 
ATOM   1177  C  CG2   . THR A  1  153 ? 10.032  44.331  67.523 1.00 47.05  ? 595  THR B CG2   1 
ATOM   1178  N  N     . MET A  1  154 ? 6.728   45.457  69.925 1.00 49.10  ? 596  MET B N     1 
ATOM   1179  C  CA    . MET A  1  154 ? 6.281   46.823  70.190 1.00 50.50  ? 596  MET B CA    1 
ATOM   1180  C  C     . MET A  1  154 ? 5.629   46.971  71.541 1.00 54.60  ? 596  MET B C     1 
ATOM   1181  O  O     . MET A  1  154 ? 5.573   48.062  72.049 1.00 47.65  ? 596  MET B O     1 
ATOM   1182  C  CB    . MET A  1  154 ? 5.319   47.287  69.132 1.00 50.82  ? 596  MET B CB    1 
ATOM   1183  C  CG    . MET A  1  154 ? 5.872   47.072  67.729 1.00 58.10  ? 596  MET B CG    1 
ATOM   1184  S  SD    . MET A  1  154 ? 4.642   47.667  66.580 1.00 58.50  ? 596  MET B SD    1 
ATOM   1185  C  CE    . MET A  1  154 ? 4.811   49.416  66.851 1.00 52.98  ? 596  MET B CE    1 
ATOM   1186  N  N     . ASN A  1  155 ? 5.132   45.890  72.116 1.00 52.83  ? 597  ASN B N     1 
ATOM   1187  C  CA    . ASN A  1  155 ? 4.504   45.952  73.401 1.00 53.12  ? 597  ASN B CA    1 
ATOM   1188  C  C     . ASN A  1  155 ? 5.566   46.152  74.461 1.00 49.54  ? 597  ASN B C     1 
ATOM   1189  O  O     . ASN A  1  155 ? 6.457   45.398  74.509 1.00 46.76  ? 597  ASN B O     1 
ATOM   1190  C  CB    . ASN A  1  155 ? 3.797   44.653  73.649 1.00 51.66  ? 597  ASN B CB    1 
ATOM   1191  C  CG    . ASN A  1  155 ? 2.938   44.710  74.888 1.00 54.83  ? 597  ASN B CG    1 
ATOM   1192  O  OD1   . ASN A  1  155 ? 2.229   43.774  75.194 1.00 59.78  ? 597  ASN B OD1   1 
ATOM   1193  N  ND2   . ASN A  1  155 ? 2.974   45.823  75.595 1.00 49.85  ? 597  ASN B ND2   1 
ATOM   1194  N  N     . PRO A  1  156 ? 5.410   47.130  75.348 1.00 46.38  ? 598  PRO B N     1 
ATOM   1195  C  CA    . PRO A  1  156 ? 6.443   47.449  76.324 1.00 49.09  ? 598  PRO B CA    1 
ATOM   1196  C  C     . PRO A  1  156 ? 6.474   46.409  77.428 1.00 56.16  ? 598  PRO B C     1 
ATOM   1197  O  O     . PRO A  1  156 ? 7.490   46.168  78.039 1.00 62.97  ? 598  PRO B O     1 
ATOM   1198  C  CB    . PRO A  1  156 ? 6.096   48.857  76.778 1.00 43.84  ? 598  PRO B CB    1 
ATOM   1199  C  CG    . PRO A  1  156 ? 4.709   49.094  76.290 1.00 44.66  ? 598  PRO B CG    1 
ATOM   1200  C  CD    . PRO A  1  156 ? 4.548   48.265  75.050 1.00 44.88  ? 598  PRO B CD    1 
ATOM   1201  N  N     A GLU A  1  157 ? 5.400   45.656  77.460 0.50 58.40  ? 599  GLU B N     1 
ATOM   1202  N  N     B GLU A  1  157 ? 5.385   45.727  77.718 0.50 57.82  ? 599  GLU B N     1 
ATOM   1203  C  CA    A GLU A  1  157 ? 5.281   44.607  78.413 0.50 58.48  ? 599  GLU B CA    1 
ATOM   1204  C  CA    B GLU A  1  157 ? 5.457   44.569  78.586 0.50 59.14  ? 599  GLU B CA    1 
ATOM   1205  C  C     A GLU A  1  157 ? 6.128   43.370  78.107 0.50 59.61  ? 599  GLU B C     1 
ATOM   1206  C  C     B GLU A  1  157 ? 6.228   43.329  78.113 0.50 60.26  ? 599  GLU B C     1 
ATOM   1207  O  O     A GLU A  1  157 ? 6.626   42.711  79.023 0.50 62.96  ? 599  GLU B O     1 
ATOM   1208  O  O     B GLU A  1  157 ? 6.649   42.521  78.931 0.50 64.00  ? 599  GLU B O     1 
ATOM   1209  C  CB    A GLU A  1  157 ? 3.827   44.222  78.526 0.50 63.02  ? 599  GLU B CB    1 
ATOM   1210  C  CB    B GLU A  1  157 ? 4.055   44.114  78.890 0.50 65.47  ? 599  GLU B CB    1 
ATOM   1211  C  CG    A GLU A  1  157 ? 2.931   45.256  79.177 0.50 65.48  ? 599  GLU B CG    1 
ATOM   1212  C  CG    B GLU A  1  157 ? 3.059   45.247  78.999 0.50 70.93  ? 599  GLU B CG    1 
ATOM   1213  C  CD    A GLU A  1  157 ? 1.605   44.643  79.626 0.50 67.87  ? 599  GLU B CD    1 
ATOM   1214  C  CD    B GLU A  1  157 ? 3.353   46.186  80.153 0.50 73.67  ? 599  GLU B CD    1 
ATOM   1215  O  OE1   A GLU A  1  157 ? 0.590   44.749  78.891 0.50 62.22  ? 599  GLU B OE1   1 
ATOM   1216  O  OE1   B GLU A  1  157 ? 4.291   45.907  80.931 0.50 78.19  ? 599  GLU B OE1   1 
ATOM   1217  O  OE2   A GLU A  1  157 ? 1.591   44.017  80.709 0.50 68.18  ? 599  GLU B OE2   1 
ATOM   1218  O  OE2   B GLU A  1  157 ? 2.616   47.191  80.304 0.50 72.33  ? 599  GLU B OE2   1 
ATOM   1219  N  N     . HIS A  1  158 ? 6.273   43.041  76.827 1.00 60.79  ? 600  HIS B N     1 
ATOM   1220  C  CA    . HIS A  1  158 ? 7.044   41.882  76.456 1.00 60.07  ? 600  HIS B CA    1 
ATOM   1221  C  C     . HIS A  1  158 ? 8.232   42.158  75.598 1.00 57.20  ? 600  HIS B C     1 
ATOM   1222  O  O     . HIS A  1  158 ? 9.043   41.268  75.382 1.00 59.22  ? 600  HIS B O     1 
ATOM   1223  C  CB    . HIS A  1  158 ? 6.190   40.790  75.859 1.00 63.37  ? 600  HIS B CB    1 
ATOM   1224  C  CG    . HIS A  1  158 ? 4.968   40.474  76.653 1.00 73.03  ? 600  HIS B CG    1 
ATOM   1225  N  ND1   . HIS A  1  158 ? 3.777   41.128  76.440 1.00 84.93  ? 600  HIS B ND1   1 
ATOM   1226  C  CD2   . HIS A  1  158 ? 4.741   39.597  77.657 1.00 71.42  ? 600  HIS B CD2   1 
ATOM   1227  C  CE1   . HIS A  1  158 ? 2.857   40.657  77.257 1.00 81.03  ? 600  HIS B CE1   1 
ATOM   1228  N  NE2   . HIS A  1  158 ? 3.420   39.735  78.017 1.00 80.91  ? 600  HIS B NE2   1 
ATOM   1229  N  N     . ARG A  1  159 ? 8.374   43.378  75.105 1.00 54.74  ? 601  ARG B N     1 
ATOM   1230  C  CA    . ARG A  1  159 ? 9.420   43.630  74.089 1.00 52.35  ? 601  ARG B CA    1 
ATOM   1231  C  C     . ARG A  1  159 ? 10.797  43.649  74.685 1.00 48.04  ? 601  ARG B C     1 
ATOM   1232  O  O     . ARG A  1  159 ? 10.932  43.963  75.833 1.00 50.04  ? 601  ARG B O     1 
ATOM   1233  C  CB    . ARG A  1  159 ? 9.197   44.937  73.363 1.00 51.78  ? 601  ARG B CB    1 
ATOM   1234  C  CG    . ARG A  1  159 ? 9.434   46.189  74.202 1.00 48.27  ? 601  ARG B CG    1 
ATOM   1235  C  CD    . ARG A  1  159 ? 8.781   47.389  73.557 1.00 43.91  ? 601  ARG B CD    1 
ATOM   1236  N  NE    . ARG A  1  159 ? 9.155   48.583  74.298 1.00 43.37  ? 601  ARG B NE    1 
ATOM   1237  C  CZ    . ARG A  1  159 ? 8.779   49.816  73.960 1.00 47.16  ? 601  ARG B CZ    1 
ATOM   1238  N  NH1   . ARG A  1  159 ? 8.026   50.033  72.886 1.00 45.41  ? 601  ARG B NH1   1 
ATOM   1239  N  NH2   . ARG A  1  159 ? 9.150   50.841  74.700 1.00 49.00  ? 601  ARG B NH2   1 
ATOM   1240  N  N     . ALA A  1  160 ? 11.807  43.293  73.919 1.00 48.39  ? 602  ALA B N     1 
ATOM   1241  C  CA    . ALA A  1  160 ? 13.167  43.533  74.371 1.00 46.77  ? 602  ALA B CA    1 
ATOM   1242  C  C     . ALA A  1  160 ? 13.848  44.518  73.441 1.00 49.87  ? 602  ALA B C     1 
ATOM   1243  O  O     . ALA A  1  160 ? 14.112  44.217  72.284 1.00 54.46  ? 602  ALA B O     1 
ATOM   1244  C  CB    . ALA A  1  160 ? 13.934  42.240  74.432 1.00 40.69  ? 602  ALA B CB    1 
ATOM   1245  N  N     . LEU A  1  161 ? 14.120  45.697  73.946 1.00 48.52  ? 603  LEU B N     1 
ATOM   1246  C  CA    . LEU A  1  161 ? 14.774  46.731  73.166 1.00 49.05  ? 603  LEU B CA    1 
ATOM   1247  C  C     . LEU A  1  161 ? 16.223  46.857  73.576 1.00 51.85  ? 603  LEU B C     1 
ATOM   1248  O  O     . LEU A  1  161 ? 16.527  46.725  74.753 1.00 59.42  ? 603  LEU B O     1 
ATOM   1249  C  CB    . LEU A  1  161 ? 14.112  48.057  73.430 1.00 43.53  ? 603  LEU B CB    1 
ATOM   1250  C  CG    . LEU A  1  161 ? 12.722  48.311  72.911 1.00 42.23  ? 603  LEU B CG    1 
ATOM   1251  C  CD1   . LEU A  1  161 ? 12.422  49.813  73.074 1.00 40.02  ? 603  LEU B CD1   1 
ATOM   1252  C  CD2   . LEU A  1  161 ? 12.497  47.875  71.457 1.00 42.28  ? 603  LEU B CD2   1 
ATOM   1253  N  N     . LEU A  1  162 ? 17.105  47.116  72.624 1.00 49.31  ? 604  LEU B N     1 
ATOM   1254  C  CA    . LEU A  1  162 ? 18.479  47.440  72.941 1.00 47.04  ? 604  LEU B CA    1 
ATOM   1255  C  C     . LEU A  1  162 ? 18.680  48.936  72.905 1.00 47.58  ? 604  LEU B C     1 
ATOM   1256  O  O     . LEU A  1  162 ? 18.413  49.587  71.928 1.00 47.02  ? 604  LEU B O     1 
ATOM   1257  C  CB    . LEU A  1  162 ? 19.401  46.796  71.933 1.00 47.90  ? 604  LEU B CB    1 
ATOM   1258  C  CG    . LEU A  1  162 ? 19.351  45.271  71.900 1.00 53.98  ? 604  LEU B CG    1 
ATOM   1259  C  CD1   . LEU A  1  162 ? 20.303  44.747  70.840 1.00 56.17  ? 604  LEU B CD1   1 
ATOM   1260  C  CD2   . LEU A  1  162 ? 19.685  44.594  73.234 1.00 47.65  ? 604  LEU B CD2   1 
ATOM   1261  N  N     . GLN A  1  163 ? 19.189  49.496  73.978 1.00 48.95  ? 605  GLN B N     1 
ATOM   1262  C  CA    . GLN A  1  163 ? 19.390  50.897  74.003 1.00 47.57  ? 605  GLN B CA    1 
ATOM   1263  C  C     . GLN A  1  163 ? 20.794  51.089  73.501 1.00 48.21  ? 605  GLN B C     1 
ATOM   1264  O  O     . GLN A  1  163 ? 21.710  50.438  73.994 1.00 49.65  ? 605  GLN B O     1 
ATOM   1265  C  CB    . GLN A  1  163 ? 19.245  51.402  75.419 1.00 47.57  ? 605  GLN B CB    1 
ATOM   1266  C  CG    . GLN A  1  163 ? 19.547  52.879  75.481 1.00 51.15  ? 605  GLN B CG    1 
ATOM   1267  C  CD    . GLN A  1  163 ? 19.291  53.436  76.829 1.00 50.77  ? 605  GLN B CD    1 
ATOM   1268  O  OE1   . GLN A  1  163 ? 19.644  52.855  77.843 1.00 53.65  ? 605  GLN B OE1   1 
ATOM   1269  N  NE2   . GLN A  1  163 ? 18.667  54.577  76.851 1.00 53.81  ? 605  GLN B NE2   1 
ATOM   1270  N  N     . VAL A  1  164 ? 20.973  51.963  72.520 1.00 44.36  ? 606  VAL B N     1 
ATOM   1271  C  CA    . VAL A  1  164 ? 22.309  52.151  71.952 1.00 45.48  ? 606  VAL B CA    1 
ATOM   1272  C  C     . VAL A  1  164 ? 23.118  53.038  72.872 1.00 47.97  ? 606  VAL B C     1 
ATOM   1273  O  O     . VAL A  1  164 ? 22.637  54.095  73.288 1.00 47.67  ? 606  VAL B O     1 
ATOM   1274  C  CB    . VAL A  1  164 ? 22.271  52.754  70.523 1.00 43.94  ? 606  VAL B CB    1 
ATOM   1275  C  CG1   . VAL A  1  164 ? 23.656  52.883  69.961 1.00 37.93  ? 606  VAL B CG1   1 
ATOM   1276  C  CG2   . VAL A  1  164 ? 21.483  51.856  69.606 1.00 44.44  ? 606  VAL B CG2   1 
ATOM   1277  N  N     . LYS A  1  165 ? 24.349  52.623  73.184 1.00 45.93  ? 607  LYS B N     1 
ATOM   1278  C  CA    . LYS A  1  165 ? 25.198  53.369  74.118 1.00 46.63  ? 607  LYS B CA    1 
ATOM   1279  C  C     . LYS A  1  165 ? 26.515  53.786  73.494 1.00 46.15  ? 607  LYS B C     1 
ATOM   1280  O  O     . LYS A  1  165 ? 27.168  52.972  72.831 1.00 53.53  ? 607  LYS B O     1 
ATOM   1281  C  CB    . LYS A  1  165 ? 25.427  52.539  75.373 1.00 49.94  ? 607  LYS B CB    1 
ATOM   1282  N  N     . LEU A  1  166 ? 26.892  55.045  73.676 1.00 47.23  ? 608  LEU B N     1 
ATOM   1283  C  CA    . LEU A  1  166 ? 28.148  55.557  73.150 1.00 50.50  ? 608  LEU B CA    1 
ATOM   1284  C  C     . LEU A  1  166 ? 29.195  55.577  74.259 1.00 55.76  ? 608  LEU B C     1 
ATOM   1285  O  O     . LEU A  1  166 ? 29.120  56.435  75.094 1.00 63.18  ? 608  LEU B O     1 
ATOM   1286  C  CB    . LEU A  1  166 ? 27.957  56.953  72.559 1.00 45.14  ? 608  LEU B CB    1 
ATOM   1287  C  CG    . LEU A  1  166 ? 29.258  57.615  72.055 1.00 49.12  ? 608  LEU B CG    1 
ATOM   1288  C  CD1   . LEU A  1  166 ? 30.202  56.699  71.264 1.00 49.58  ? 608  LEU B CD1   1 
ATOM   1289  C  CD2   . LEU A  1  166 ? 28.999  58.873  71.253 1.00 45.69  ? 608  LEU B CD2   1 
ATOM   1290  N  N     . GLU A  1  167 ? 30.165  54.663  74.246 1.00 55.65  ? 609  GLU B N     1 
ATOM   1291  C  CA    . GLU A  1  167 ? 31.176  54.633  75.293 1.00 55.70  ? 609  GLU B CA    1 
ATOM   1292  C  C     . GLU A  1  167 ? 32.434  55.412  74.977 1.00 56.72  ? 609  GLU B C     1 
ATOM   1293  O  O     . GLU A  1  167 ? 32.811  56.317  75.703 1.00 70.91  ? 609  GLU B O     1 
ATOM   1294  C  CB    . GLU A  1  167 ? 31.491  53.208  75.691 1.00 50.72  ? 609  GLU B CB    1 
ATOM   1295  C  CG    . GLU A  1  167 ? 30.262  52.554  76.289 1.00 69.54  ? 609  GLU B CG    1 
ATOM   1296  C  CD    . GLU A  1  167 ? 30.387  51.045  76.465 1.00 87.59  ? 609  GLU B CD    1 
ATOM   1297  O  OE1   . GLU A  1  167 ? 31.504  50.502  76.310 1.00 109.51 ? 609  GLU B OE1   1 
ATOM   1298  O  OE2   . GLU A  1  167 ? 29.356  50.394  76.766 1.00 92.45  ? 609  GLU B OE2   1 
ATOM   1299  N  N     . ASP A  1  168 ? 33.086  55.061  73.894 1.00 58.31  ? 610  ASP B N     1 
ATOM   1300  C  CA    . ASP A  1  168 ? 34.333  55.700  73.533 1.00 47.30  ? 610  ASP B CA    1 
ATOM   1301  C  C     . ASP A  1  168 ? 34.134  56.423  72.240 1.00 50.09  ? 610  ASP B C     1 
ATOM   1302  O  O     . ASP A  1  168 ? 33.950  55.798  71.185 1.00 51.73  ? 610  ASP B O     1 
ATOM   1303  C  CB    . ASP A  1  168 ? 35.425  54.659  73.392 1.00 48.76  ? 610  ASP B CB    1 
ATOM   1304  C  CG    . ASP A  1  168 ? 36.796  55.258  73.347 1.00 49.79  ? 610  ASP B CG    1 
ATOM   1305  O  OD1   . ASP A  1  168 ? 36.936  56.491  73.181 1.00 57.56  ? 610  ASP B OD1   1 
ATOM   1306  O  OD2   . ASP A  1  168 ? 37.742  54.472  73.479 1.00 54.63  ? 610  ASP B OD2   1 
ATOM   1307  N  N     . ALA A  1  169 ? 34.160  57.749  72.310 1.00 49.84  ? 611  ALA B N     1 
ATOM   1308  C  CA    . ALA A  1  169 ? 33.933  58.541  71.133 1.00 45.68  ? 611  ALA B CA    1 
ATOM   1309  C  C     . ALA A  1  169 ? 35.086  58.469  70.148 1.00 54.76  ? 611  ALA B C     1 
ATOM   1310  O  O     . ALA A  1  169 ? 34.867  58.635  68.944 1.00 58.41  ? 611  ALA B O     1 
ATOM   1311  C  CB    . ALA A  1  169 ? 33.613  59.967  71.493 1.00 44.99  ? 611  ALA B CB    1 
ATOM   1312  N  N     . ILE A  1  170 ? 36.301  58.234  70.624 1.00 59.49  ? 612  ILE B N     1 
ATOM   1313  C  CA    . ILE A  1  170 ? 37.425  58.157  69.709 1.00 61.09  ? 612  ILE B CA    1 
ATOM   1314  C  C     . ILE A  1  170 ? 37.298  56.875  68.901 1.00 58.22  ? 612  ILE B C     1 
ATOM   1315  O  O     . ILE A  1  170 ? 37.474  56.919  67.700 1.00 57.18  ? 612  ILE B O     1 
ATOM   1316  C  CB    . ILE A  1  170 ? 38.789  58.273  70.442 1.00 57.17  ? 612  ILE B CB    1 
ATOM   1317  C  CG1   . ILE A  1  170 ? 38.976  59.694  71.012 1.00 59.41  ? 612  ILE B CG1   1 
ATOM   1318  C  CG2   . ILE A  1  170 ? 39.962  57.886  69.557 1.00 51.97  ? 612  ILE B CG2   1 
ATOM   1319  C  CD1   . ILE A  1  170 ? 38.944  60.861  70.021 1.00 54.57  ? 612  ILE B CD1   1 
ATOM   1320  N  N     . GLU A  1  171 ? 36.963  55.773  69.570 1.00 49.24  ? 613  GLU B N     1 
ATOM   1321  C  CA    . GLU A  1  171 ? 36.857  54.463  68.979 1.00 51.13  ? 613  GLU B CA    1 
ATOM   1322  C  C     . GLU A  1  171 ? 35.683  54.429  67.996 1.00 51.91  ? 613  GLU B C     1 
ATOM   1323  O  O     . GLU A  1  171 ? 35.766  53.793  66.969 1.00 49.23  ? 613  GLU B O     1 
ATOM   1324  C  CB    . GLU A  1  171 ? 36.670  53.461  70.100 1.00 51.24  ? 613  GLU B CB    1 
ATOM   1325  C  CG    . GLU A  1  171 ? 36.567  52.001  69.707 1.00 61.44  ? 613  GLU B CG    1 
ATOM   1326  C  CD    . GLU A  1  171 ? 35.926  51.126  70.806 1.00 70.59  ? 613  GLU B CD    1 
ATOM   1327  O  OE1   . GLU A  1  171 ? 34.859  51.495  71.375 1.00 80.81  ? 613  GLU B OE1   1 
ATOM   1328  O  OE2   . GLU A  1  171 ? 36.476  50.038  71.097 1.00 73.83  ? 613  GLU B OE2   1 
ATOM   1329  N  N     . ALA A  1  172 ? 34.588  55.109  68.327 1.00 50.05  ? 614  ALA B N     1 
ATOM   1330  C  CA    . ALA A  1  172 ? 33.413  55.141  67.478 1.00 42.75  ? 614  ALA B CA    1 
ATOM   1331  C  C     . ALA A  1  172 ? 33.673  55.949  66.216 1.00 43.08  ? 614  ALA B C     1 
ATOM   1332  O  O     . ALA A  1  172 ? 33.186  55.589  65.153 1.00 42.71  ? 614  ALA B O     1 
ATOM   1333  C  CB    . ALA A  1  172 ? 32.223  55.697  68.230 1.00 38.22  ? 614  ALA B CB    1 
ATOM   1334  N  N     . ASP A  1  173 ? 34.437  57.035  66.334 1.00 42.59  ? 615  ASP B N     1 
ATOM   1335  C  CA    . ASP A  1  173 ? 34.766  57.861  65.190 1.00 43.13  ? 615  ASP B CA    1 
ATOM   1336  C  C     . ASP A  1  173 ? 35.495  57.000  64.168 1.00 44.29  ? 615  ASP B C     1 
ATOM   1337  O  O     . ASP A  1  173 ? 35.238  57.056  62.963 1.00 43.46  ? 615  ASP B O     1 
ATOM   1338  C  CB    . ASP A  1  173 ? 35.701  58.995  65.585 1.00 43.79  ? 615  ASP B CB    1 
ATOM   1339  C  CG    . ASP A  1  173 ? 34.977  60.214  66.147 1.00 59.96  ? 615  ASP B CG    1 
ATOM   1340  O  OD1   . ASP A  1  173 ? 33.730  60.217  66.300 1.00 57.59  ? 615  ASP B OD1   1 
ATOM   1341  O  OD2   . ASP A  1  173 ? 35.690  61.199  66.460 1.00 63.98  ? 615  ASP B OD2   1 
ATOM   1342  N  N     . GLN A  1  174 ? 36.417  56.209  64.695 1.00 41.78  ? 616  GLN B N     1 
ATOM   1343  C  CA    . GLN A  1  174 ? 37.278  55.358  63.923 1.00 43.99  ? 616  GLN B CA    1 
ATOM   1344  C  C     . GLN A  1  174 ? 36.524  54.230  63.252 1.00 37.99  ? 616  GLN B C     1 
ATOM   1345  O  O     . GLN A  1  174 ? 36.808  53.936  62.121 1.00 37.32  ? 616  GLN B O     1 
ATOM   1346  C  CB    . GLN A  1  174 ? 38.396  54.831  64.826 1.00 40.45  ? 616  GLN B CB    1 
ATOM   1347  C  CG    . GLN A  1  174 ? 39.395  55.947  65.087 1.00 49.72  ? 616  GLN B CG    1 
ATOM   1348  C  CD    . GLN A  1  174 ? 40.476  55.591  66.093 1.00 58.10  ? 616  GLN B CD    1 
ATOM   1349  O  OE1   . GLN A  1  174 ? 40.424  54.551  66.784 1.00 56.64  ? 616  GLN B OE1   1 
ATOM   1350  N  NE2   . GLN A  1  174 ? 41.473  56.475  66.188 1.00 61.06  ? 616  GLN B NE2   1 
ATOM   1351  N  N     . THR A  1  175 ? 35.581  53.628  63.979 1.00 34.98  ? 617  THR B N     1 
ATOM   1352  C  CA    . THR A  1  175 ? 34.711  52.590  63.511 1.00 36.40  ? 617  THR B CA    1 
ATOM   1353  C  C     . THR A  1  175 ? 33.782  53.021  62.383 1.00 40.89  ? 617  THR B C     1 
ATOM   1354  O  O     . THR A  1  175 ? 33.667  52.295  61.405 1.00 41.71  ? 617  THR B O     1 
ATOM   1355  C  CB    . THR A  1  175 ? 33.852  52.096  64.650 1.00 38.98  ? 617  THR B CB    1 
ATOM   1356  O  OG1   . THR A  1  175 ? 34.700  51.544  65.630 1.00 40.61  ? 617  THR B OG1   1 
ATOM   1357  C  CG2   . THR A  1  175 ? 32.886  51.037  64.207 1.00 34.93  ? 617  THR B CG2   1 
ATOM   1358  N  N     . PHE A  1  176 ? 33.176  54.199  62.501 1.00 37.18  ? 618  PHE B N     1 
ATOM   1359  C  CA    . PHE A  1  176 ? 32.309  54.741  61.481 1.00 33.73  ? 618  PHE B CA    1 
ATOM   1360  C  C     . PHE A  1  176 ? 33.147  55.057  60.235 1.00 37.41  ? 618  PHE B C     1 
ATOM   1361  O  O     . PHE A  1  176 ? 32.793  54.746  59.157 1.00 35.32  ? 618  PHE B O     1 
ATOM   1362  C  CB    . PHE A  1  176 ? 31.512  55.938  62.013 1.00 33.93  ? 618  PHE B CB    1 
ATOM   1363  C  CG    . PHE A  1  176 ? 30.268  55.543  62.729 1.00 38.65  ? 618  PHE B CG    1 
ATOM   1364  C  CD1   . PHE A  1  176 ? 29.171  55.029  62.038 1.00 40.29  ? 618  PHE B CD1   1 
ATOM   1365  C  CD2   . PHE A  1  176 ? 30.185  55.654  64.109 1.00 39.45  ? 618  PHE B CD2   1 
ATOM   1366  C  CE1   . PHE A  1  176 ? 28.016  54.643  62.696 1.00 39.04  ? 618  PHE B CE1   1 
ATOM   1367  C  CE2   . PHE A  1  176 ? 29.029  55.259  64.776 1.00 45.02  ? 618  PHE B CE2   1 
ATOM   1368  C  CZ    . PHE A  1  176 ? 27.935  54.758  64.061 1.00 41.49  ? 618  PHE B CZ    1 
ATOM   1369  N  N     A GLU A  1  177 ? 34.346  55.567  60.441 0.50 38.98  ? 619  GLU B N     1 
ATOM   1370  N  N     B GLU A  1  177 ? 34.353  55.576  60.411 0.50 37.75  ? 619  GLU B N     1 
ATOM   1371  C  CA    A GLU A  1  177 ? 35.244  55.820  59.346 0.50 38.67  ? 619  GLU B CA    1 
ATOM   1372  C  CA    B GLU A  1  177 ? 35.279  55.822  59.301 0.50 36.97  ? 619  GLU B CA    1 
ATOM   1373  C  C     A GLU A  1  177 ? 35.738  54.599  58.560 0.50 36.06  ? 619  GLU B C     1 
ATOM   1374  C  C     B GLU A  1  177 ? 35.733  54.577  58.531 0.50 34.74  ? 619  GLU B C     1 
ATOM   1375  O  O     A GLU A  1  177 ? 35.739  54.566  57.346 0.50 35.76  ? 619  GLU B O     1 
ATOM   1376  O  O     B GLU A  1  177 ? 35.747  54.524  57.318 0.50 34.13  ? 619  GLU B O     1 
ATOM   1377  C  CB    A GLU A  1  177 ? 36.449  56.593  59.824 0.50 43.19  ? 619  GLU B CB    1 
ATOM   1378  C  CB    B GLU A  1  177 ? 36.527  56.512  59.861 0.50 39.35  ? 619  GLU B CB    1 
ATOM   1379  C  CG    A GLU A  1  177 ? 37.035  57.148  58.522 0.50 43.65  ? 619  GLU B CG    1 
ATOM   1380  C  CG    B GLU A  1  177 ? 36.556  58.049  59.862 0.50 40.86  ? 619  GLU B CG    1 
ATOM   1381  C  CD    A GLU A  1  177 ? 38.554  57.261  58.409 0.50 55.80  ? 619  GLU B CD    1 
ATOM   1382  C  CD    B GLU A  1  177 ? 37.888  58.636  60.382 0.50 40.48  ? 619  GLU B CD    1 
ATOM   1383  O  OE1   A GLU A  1  177 ? 39.281  57.006  59.400 0.50 59.20  ? 619  GLU B OE1   1 
ATOM   1384  O  OE1   B GLU A  1  177 ? 38.861  58.669  59.603 0.50 43.33  ? 619  GLU B OE1   1 
ATOM   1385  O  OE2   A GLU A  1  177 ? 39.027  57.626  57.295 0.50 55.87  ? 619  GLU B OE2   1 
ATOM   1386  O  OE2   B GLU A  1  177 ? 38.010  59.098  61.529 0.50 37.05  ? 619  GLU B OE2   1 
ATOM   1387  N  N     . MET A  1  178 ? 36.190  53.604  59.269 1.00 34.35  ? 620  MET B N     1 
ATOM   1388  C  CA    . MET A  1  178 ? 36.604  52.362  58.704 1.00 37.49  ? 620  MET B CA    1 
ATOM   1389  C  C     . MET A  1  178 ? 35.466  51.566  58.041 1.00 34.02  ? 620  MET B C     1 
ATOM   1390  O  O     . MET A  1  178 ? 35.601  51.210  56.876 1.00 35.33  ? 620  MET B O     1 
ATOM   1391  C  CB    . MET A  1  178 ? 37.178  51.567  59.836 1.00 33.84  ? 620  MET B CB    1 
ATOM   1392  C  CG    . MET A  1  178 ? 37.579  50.147  59.460 1.00 37.03  ? 620  MET B CG    1 
ATOM   1393  S  SD    . MET A  1  178 ? 38.283  49.209  60.842 1.00 47.59  ? 620  MET B SD    1 
ATOM   1394  C  CE    . MET A  1  178 ? 36.854  48.932  61.891 1.00 42.27  ? 620  MET B CE    1 
ATOM   1395  N  N     . LEU A  1  179 ? 34.363  51.343  58.747 1.00 32.77  ? 621  LEU B N     1 
ATOM   1396  C  CA    . LEU A  1  179 ? 33.270  50.589  58.166 1.00 33.96  ? 621  LEU B CA    1 
ATOM   1397  C  C     . LEU A  1  179 ? 32.536  51.278  57.055 1.00 34.66  ? 621  LEU B C     1 
ATOM   1398  O  O     . LEU A  1  179 ? 32.211  50.636  56.072 1.00 32.21  ? 621  LEU B O     1 
ATOM   1399  C  CB    . LEU A  1  179 ? 32.278  50.198  59.207 1.00 33.65  ? 621  LEU B CB    1 
ATOM   1400  C  CG    . LEU A  1  179 ? 32.914  49.253  60.244 1.00 35.81  ? 621  LEU B CG    1 
ATOM   1401  C  CD1   . LEU A  1  179 ? 31.874  48.852  61.285 1.00 31.21  ? 621  LEU B CD1   1 
ATOM   1402  C  CD2   . LEU A  1  179 ? 33.457  48.035  59.501 1.00 32.53  ? 621  LEU B CD2   1 
ATOM   1403  N  N     . MET A  1  180 ? 32.279  52.572  57.181 1.00 30.55  ? 622  MET B N     1 
ATOM   1404  C  CA    . MET A  1  180 ? 31.428  53.220  56.252 1.00 30.59  ? 622  MET B CA    1 
ATOM   1405  C  C     . MET A  1  180 ? 32.062  54.255  55.381 1.00 33.29  ? 622  MET B C     1 
ATOM   1406  O  O     . MET A  1  180 ? 31.407  54.775  54.467 1.00 38.17  ? 622  MET B O     1 
ATOM   1407  C  CB    . MET A  1  180 ? 30.251  53.831  56.943 1.00 28.32  ? 622  MET B CB    1 
ATOM   1408  C  CG    . MET A  1  180 ? 29.743  52.996  58.065 1.00 33.12  ? 622  MET B CG    1 
ATOM   1409  S  SD    . MET A  1  180 ? 28.899  51.505  57.495 1.00 31.85  ? 622  MET B SD    1 
ATOM   1410  C  CE    . MET A  1  180 ? 27.462  52.231  56.704 1.00 26.55  ? 622  MET B CE    1 
ATOM   1411  N  N     . GLY A  1  181 ? 33.335  54.530  55.597 1.00 31.19  ? 623  GLY B N     1 
ATOM   1412  C  CA    . GLY A  1  181 ? 34.040  55.539  54.823 1.00 30.92  ? 623  GLY B CA    1 
ATOM   1413  C  C     . GLY A  1  181 ? 34.388  55.146  53.388 1.00 33.79  ? 623  GLY B C     1 
ATOM   1414  O  O     . GLY A  1  181 ? 34.072  54.060  52.912 1.00 34.07  ? 623  GLY B O     1 
ATOM   1415  N  N     . ASP A  1  182 ? 35.085  56.035  52.703 1.00 33.97  ? 624  ASP B N     1 
ATOM   1416  C  CA    . ASP A  1  182 ? 35.409  55.793  51.326 1.00 38.10  ? 624  ASP B CA    1 
ATOM   1417  C  C     . ASP A  1  182 ? 36.662  54.946  51.088 1.00 39.36  ? 624  ASP B C     1 
ATOM   1418  O  O     . ASP A  1  182 ? 36.925  54.621  49.933 1.00 41.98  ? 624  ASP B O     1 
ATOM   1419  C  CB    . ASP A  1  182 ? 35.453  57.072  50.510 1.00 38.87  ? 624  ASP B CB    1 
ATOM   1420  C  CG    . ASP A  1  182 ? 36.374  58.103  51.090 1.00 51.26  ? 624  ASP B CG    1 
ATOM   1421  O  OD1   . ASP A  1  182 ? 37.486  57.746  51.573 1.00 55.72  ? 624  ASP B OD1   1 
ATOM   1422  O  OD2   . ASP A  1  182 ? 35.967  59.298  51.056 1.00 55.83  ? 624  ASP B OD2   1 
ATOM   1423  N  N     . VAL A  1  183 ? 37.439  54.612  52.122 1.00 34.45  ? 625  VAL B N     1 
ATOM   1424  C  CA    . VAL A  1  183 ? 38.639  53.805  51.862 1.00 34.00  ? 625  VAL B CA    1 
ATOM   1425  C  C     . VAL A  1  183 ? 38.280  52.301  51.878 1.00 39.39  ? 625  VAL B C     1 
ATOM   1426  O  O     . VAL A  1  183 ? 37.996  51.711  52.916 1.00 41.11  ? 625  VAL B O     1 
ATOM   1427  C  CB    . VAL A  1  183 ? 39.731  54.113  52.870 1.00 32.36  ? 625  VAL B CB    1 
ATOM   1428  C  CG1   . VAL A  1  183 ? 40.965  53.299  52.563 1.00 31.80  ? 625  VAL B CG1   1 
ATOM   1429  C  CG2   . VAL A  1  183 ? 40.069  55.600  52.829 1.00 32.22  ? 625  VAL B CG2   1 
ATOM   1430  N  N     . VAL A  1  184 ? 38.291  51.684  50.716 1.00 37.01  ? 626  VAL B N     1 
ATOM   1431  C  CA    . VAL A  1  184 ? 37.917  50.297  50.641 1.00 35.09  ? 626  VAL B CA    1 
ATOM   1432  C  C     . VAL A  1  184 ? 38.884  49.344  51.346 1.00 34.77  ? 626  VAL B C     1 
ATOM   1433  O  O     . VAL A  1  184 ? 38.453  48.388  51.952 1.00 33.70  ? 626  VAL B O     1 
ATOM   1434  C  CB    . VAL A  1  184 ? 37.653  49.900  49.195 1.00 35.49  ? 626  VAL B CB    1 
ATOM   1435  C  CG1   . VAL A  1  184 ? 37.317  48.438  49.113 1.00 32.19  ? 626  VAL B CG1   1 
ATOM   1436  C  CG2   . VAL A  1  184 ? 36.478  50.692  48.649 1.00 32.52  ? 626  VAL B CG2   1 
ATOM   1437  N  N     . GLU A  1  185 ? 40.183  49.604  51.303 1.00 32.79  ? 627  GLU B N     1 
ATOM   1438  C  CA    . GLU A  1  185 ? 41.132  48.647  51.827 1.00 31.56  ? 627  GLU B CA    1 
ATOM   1439  C  C     . GLU A  1  185 ? 41.003  48.412  53.315 1.00 35.03  ? 627  GLU B C     1 
ATOM   1440  O  O     . GLU A  1  185 ? 41.111  47.285  53.748 1.00 42.37  ? 627  GLU B O     1 
ATOM   1441  C  CB    . GLU A  1  185 ? 42.547  49.067  51.450 1.00 34.38  ? 627  GLU B CB    1 
ATOM   1442  C  CG    . GLU A  1  185 ? 43.658  48.204  52.020 1.00 36.07  ? 627  GLU B CG    1 
ATOM   1443  C  CD    . GLU A  1  185 ? 43.578  46.738  51.588 1.00 41.36  ? 627  GLU B CD    1 
ATOM   1444  O  OE1   . GLU A  1  185 ? 42.898  46.367  50.596 1.00 45.94  ? 627  GLU B OE1   1 
ATOM   1445  O  OE2   . GLU A  1  185 ? 44.227  45.948  52.248 1.00 44.74  ? 627  GLU B OE2   1 
ATOM   1446  N  N     . ASN A  1  186 ? 40.772  49.447  54.104 1.00 36.62  ? 628  ASN B N     1 
ATOM   1447  C  CA    . ASN A  1  186 ? 40.668  49.282  55.554 1.00 36.64  ? 628  ASN B CA    1 
ATOM   1448  C  C     . ASN A  1  186 ? 39.436  48.447  55.945 1.00 39.30  ? 628  ASN B C     1 
ATOM   1449  O  O     . ASN A  1  186 ? 39.492  47.581  56.822 1.00 37.85  ? 628  ASN B O     1 
ATOM   1450  C  CB    . ASN A  1  186 ? 40.613  50.665  56.185 1.00 36.94  ? 628  ASN B CB    1 
ATOM   1451  C  CG    . ASN A  1  186 ? 41.937  51.429  56.008 1.00 42.83  ? 628  ASN B CG    1 
ATOM   1452  O  OD1   . ASN A  1  186 ? 43.008  50.827  55.849 1.00 40.99  ? 628  ASN B OD1   1 
ATOM   1453  N  ND2   . ASN A  1  186 ? 41.862  52.752  56.032 1.00 41.53  ? 628  ASN B ND2   1 
ATOM   1454  N  N     . ARG A  1  187 ? 38.342  48.711  55.232 1.00 35.10  ? 629  ARG B N     1 
ATOM   1455  C  CA    . ARG A  1  187 ? 37.133  47.982  55.368 1.00 33.30  ? 629  ARG B CA    1 
ATOM   1456  C  C     . ARG A  1  187 ? 37.342  46.543  54.923 1.00 33.37  ? 629  ARG B C     1 
ATOM   1457  O  O     . ARG A  1  187 ? 36.823  45.642  55.527 1.00 35.77  ? 629  ARG B O     1 
ATOM   1458  C  CB    . ARG A  1  187 ? 36.050  48.700  54.565 1.00 33.02  ? 629  ARG B CB    1 
ATOM   1459  C  CG    . ARG A  1  187 ? 34.874  47.836  54.223 1.00 30.62  ? 629  ARG B CG    1 
ATOM   1460  C  CD    . ARG A  1  187 ? 33.625  48.632  53.769 1.00 26.74  ? 629  ARG B CD    1 
ATOM   1461  N  NE    . ARG A  1  187 ? 33.878  49.517  52.622 1.00 31.74  ? 629  ARG B NE    1 
ATOM   1462  C  CZ    . ARG A  1  187 ? 34.116  50.838  52.699 1.00 28.91  ? 629  ARG B CZ    1 
ATOM   1463  N  NH1   . ARG A  1  187 ? 34.074  51.456  53.856 1.00 29.77  ? 629  ARG B NH1   1 
ATOM   1464  N  NH2   . ARG A  1  187 ? 34.358  51.540  51.630 1.00 26.99  ? 629  ARG B NH2   1 
ATOM   1465  N  N     . ARG A  1  188 ? 38.056  46.337  53.830 1.00 36.23  ? 630  ARG B N     1 
ATOM   1466  C  CA    . ARG A  1  188 ? 38.344  44.971  53.431 1.00 39.79  ? 630  ARG B CA    1 
ATOM   1467  C  C     . ARG A  1  188 ? 39.210  44.253  54.485 1.00 39.53  ? 630  ARG B C     1 
ATOM   1468  O  O     . ARG A  1  188 ? 38.972  43.124  54.776 1.00 38.30  ? 630  ARG B O     1 
ATOM   1469  C  CB    . ARG A  1  188 ? 39.024  44.949  52.087 1.00 36.02  ? 630  ARG B CB    1 
ATOM   1470  C  CG    . ARG A  1  188 ? 39.101  43.543  51.565 1.00 38.89  ? 630  ARG B CG    1 
ATOM   1471  C  CD    . ARG A  1  188 ? 40.254  43.337  50.603 1.00 42.34  ? 630  ARG B CD    1 
ATOM   1472  N  NE    . ARG A  1  188 ? 41.534  43.687  51.197 1.00 38.32  ? 630  ARG B NE    1 
ATOM   1473  C  CZ    . ARG A  1  188 ? 42.203  42.906  52.051 1.00 40.84  ? 630  ARG B CZ    1 
ATOM   1474  N  NH1   . ARG A  1  188 ? 41.760  41.702  52.403 1.00 37.24  ? 630  ARG B NH1   1 
ATOM   1475  N  NH2   . ARG A  1  188 ? 43.350  43.316  52.534 1.00 35.90  ? 630  ARG B NH2   1 
ATOM   1476  N  N     . GLN A  1  189 ? 40.194  44.933  55.040 1.00 35.71  ? 631  GLN B N     1 
ATOM   1477  C  CA    . GLN A  1  189 ? 41.018  44.325  56.072 1.00 40.88  ? 631  GLN B CA    1 
ATOM   1478  C  C     . GLN A  1  189 ? 40.193  43.950  57.326 1.00 36.22  ? 631  GLN B C     1 
ATOM   1479  O  O     . GLN A  1  189 ? 40.403  42.918  57.919 1.00 35.58  ? 631  GLN B O     1 
ATOM   1480  C  CB    . GLN A  1  189 ? 42.196  45.261  56.451 1.00 37.79  ? 631  GLN B CB    1 
ATOM   1481  C  CG    . GLN A  1  189 ? 43.246  44.565  57.297 1.00 42.40  ? 631  GLN B CG    1 
ATOM   1482  C  CD    . GLN A  1  189 ? 43.868  43.381  56.585 1.00 49.79  ? 631  GLN B CD    1 
ATOM   1483  O  OE1   . GLN A  1  189 ? 44.419  43.528  55.510 1.00 56.61  ? 631  GLN B OE1   1 
ATOM   1484  N  NE2   . GLN A  1  189 ? 43.771  42.196  57.177 1.00 52.71  ? 631  GLN B NE2   1 
ATOM   1485  N  N     . PHE A  1  190 ? 39.263  44.803  57.702 1.00 31.27  ? 632  PHE B N     1 
ATOM   1486  C  CA    . PHE A  1  190 ? 38.392  44.519  58.818 1.00 34.05  ? 632  PHE B CA    1 
ATOM   1487  C  C     . PHE A  1  190 ? 37.556  43.263  58.591 1.00 37.18  ? 632  PHE B C     1 
ATOM   1488  O  O     . PHE A  1  190 ? 37.382  42.444  59.514 1.00 37.09  ? 632  PHE B O     1 
ATOM   1489  C  CB    . PHE A  1  190 ? 37.464  45.706  59.132 1.00 36.45  ? 632  PHE B CB    1 
ATOM   1490  C  CG    . PHE A  1  190 ? 36.318  45.346  60.030 1.00 39.94  ? 632  PHE B CG    1 
ATOM   1491  C  CD1   . PHE A  1  190 ? 36.470  45.376  61.423 1.00 41.33  ? 632  PHE B CD1   1 
ATOM   1492  C  CD2   . PHE A  1  190 ? 35.081  44.962  59.494 1.00 40.01  ? 632  PHE B CD2   1 
ATOM   1493  C  CE1   . PHE A  1  190 ? 35.408  45.038  62.260 1.00 40.97  ? 632  PHE B CE1   1 
ATOM   1494  C  CE2   . PHE A  1  190 ? 34.016  44.616  60.333 1.00 43.56  ? 632  PHE B CE2   1 
ATOM   1495  C  CZ    . PHE A  1  190 ? 34.180  44.655  61.718 1.00 46.36  ? 632  PHE B CZ    1 
ATOM   1496  N  N     . ILE A  1  191 ? 37.030  43.115  57.368 1.00 33.57  ? 633  ILE B N     1 
ATOM   1497  C  CA    . ILE A  1  191 ? 36.181  41.967  57.067 1.00 33.43  ? 633  ILE B CA    1 
ATOM   1498  C  C     . ILE A  1  191 ? 37.004  40.663  57.080 1.00 35.07  ? 633  ILE B C     1 
ATOM   1499  O  O     . ILE A  1  191 ? 36.556  39.651  57.613 1.00 35.41  ? 633  ILE B O     1 
ATOM   1500  C  CB    . ILE A  1  191 ? 35.472  42.126  55.721 1.00 29.82  ? 633  ILE B CB    1 
ATOM   1501  C  CG1   . ILE A  1  191 ? 34.604  43.380  55.736 1.00 32.68  ? 633  ILE B CG1   1 
ATOM   1502  C  CG2   . ILE A  1  191 ? 34.584  40.939  55.482 1.00 29.54  ? 633  ILE B CG2   1 
ATOM   1503  C  CD1   . ILE A  1  191 ? 34.266  43.853  54.350 1.00 26.10  ? 633  ILE B CD1   1 
ATOM   1504  N  N     . GLU A  1  192 ? 38.212  40.724  56.523 1.00 35.77  ? 634  GLU B N     1 
ATOM   1505  C  CA    . GLU A  1  192 ? 39.067  39.572  56.457 1.00 36.95  ? 634  GLU B CA    1 
ATOM   1506  C  C     . GLU A  1  192 ? 39.447  39.110  57.851 1.00 40.29  ? 634  GLU B C     1 
ATOM   1507  O  O     . GLU A  1  192 ? 39.425  37.904  58.139 1.00 44.41  ? 634  GLU B O     1 
ATOM   1508  C  CB    . GLU A  1  192 ? 40.314  39.875  55.669 1.00 36.39  ? 634  GLU B CB    1 
ATOM   1509  C  CG    . GLU A  1  192 ? 41.219  38.648  55.581 1.00 35.83  ? 634  GLU B CG    1 
ATOM   1510  C  CD    . GLU A  1  192 ? 42.518  38.928  54.869 1.00 38.70  ? 634  GLU B CD    1 
ATOM   1511  O  OE1   . GLU A  1  192 ? 43.122  37.962  54.431 1.00 48.33  ? 634  GLU B OE1   1 
ATOM   1512  O  OE2   . GLU A  1  192 ? 42.956  40.090  54.717 1.00 42.02  ? 634  GLU B OE2   1 
ATOM   1513  N  N     . ASP A  1  193 ? 39.781  40.078  58.710 1.00 38.65  ? 635  ASP B N     1 
ATOM   1514  C  CA    . ASP A  1  193 ? 40.221  39.790  60.068 1.00 38.58  ? 635  ASP B CA    1 
ATOM   1515  C  C     . ASP A  1  193 ? 39.131  39.216  60.946 1.00 45.62  ? 635  ASP B C     1 
ATOM   1516  O  O     . ASP A  1  193 ? 39.402  38.446  61.851 1.00 45.07  ? 635  ASP B O     1 
ATOM   1517  C  CB    . ASP A  1  193 ? 40.791  41.020  60.723 1.00 37.22  ? 635  ASP B CB    1 
ATOM   1518  C  CG    . ASP A  1  193 ? 42.134  41.426  60.140 1.00 38.98  ? 635  ASP B CG    1 
ATOM   1519  O  OD1   . ASP A  1  193 ? 42.767  40.613  59.464 1.00 43.50  ? 635  ASP B OD1   1 
ATOM   1520  O  OD2   . ASP A  1  193 ? 42.576  42.575  60.360 1.00 47.12  ? 635  ASP B OD2   1 
ATOM   1521  N  N     . ASN A  1  194 ? 37.885  39.598  60.702 1.00 43.77  ? 636  ASN B N     1 
ATOM   1522  C  CA    . ASN A  1  194 ? 36.817  39.170  61.572 1.00 45.49  ? 636  ASN B CA    1 
ATOM   1523  C  C     . ASN A  1  194 ? 35.900  38.121  60.999 1.00 48.12  ? 636  ASN B C     1 
ATOM   1524  O  O     . ASN A  1  194 ? 35.095  37.604  61.725 1.00 52.42  ? 636  ASN B O     1 
ATOM   1525  C  CB    . ASN A  1  194 ? 35.998  40.380  62.057 1.00 41.21  ? 636  ASN B CB    1 
ATOM   1526  C  CG    . ASN A  1  194 ? 36.847  41.328  62.861 1.00 43.35  ? 636  ASN B CG    1 
ATOM   1527  O  OD1   . ASN A  1  194 ? 36.935  41.148  64.048 1.00 54.49  ? 636  ASN B OD1   1 
ATOM   1528  N  ND2   . ASN A  1  194 ? 37.452  42.333  62.236 1.00 41.97  ? 636  ASN B ND2   1 
ATOM   1529  N  N     A ALA A  1  195 ? 35.972  37.888  59.688 0.70 49.12  ? 637  ALA B N     1 
ATOM   1530  N  N     B ALA A  1  195 ? 36.083  37.686  59.759 0.30 47.80  ? 637  ALA B N     1 
ATOM   1531  C  CA    A ALA A  1  195 ? 35.082  36.912  59.081 0.70 52.89  ? 637  ALA B CA    1 
ATOM   1532  C  CA    B ALA A  1  195 ? 35.041  36.946  59.057 0.30 48.53  ? 637  ALA B CA    1 
ATOM   1533  C  C     A ALA A  1  195 ? 35.384  35.482  59.564 0.70 55.65  ? 637  ALA B C     1 
ATOM   1534  C  C     B ALA A  1  195 ? 34.944  35.512  59.570 0.30 48.60  ? 637  ALA B C     1 
ATOM   1535  O  O     A ALA A  1  195 ? 36.565  35.084  59.693 0.70 59.89  ? 637  ALA B O     1 
ATOM   1536  O  O     B ALA A  1  195 ? 33.982  34.798  59.293 0.30 51.56  ? 637  ALA B O     1 
ATOM   1537  C  CB    A ALA A  1  195 ? 35.109  37.022  57.566 0.70 55.10  ? 637  ALA B CB    1 
ATOM   1538  C  CB    B ALA A  1  195 ? 35.267  36.995  57.556 0.30 49.90  ? 637  ALA B CB    1 
ATOM   1539  N  N     A VAL A  1  196 ? 34.305  34.756  59.853 0.70 61.30  ? 638  VAL B N     1 
ATOM   1540  N  N     B VAL A  1  196 ? 35.937  35.101  60.347 0.30 48.96  ? 638  VAL B N     1 
ATOM   1541  C  CA    A VAL A  1  196 ? 34.343  33.364  60.301 0.70 65.92  ? 638  VAL B CA    1 
ATOM   1542  C  CA    B VAL A  1  196 ? 35.876  33.789  60.979 0.30 49.32  ? 638  VAL B CA    1 
ATOM   1543  C  C     A VAL A  1  196 ? 33.087  32.604  59.887 0.70 69.24  ? 638  VAL B C     1 
ATOM   1544  C  C     B VAL A  1  196 ? 34.828  33.887  62.103 0.30 51.38  ? 638  VAL B C     1 
ATOM   1545  O  O     A VAL A  1  196 ? 32.023  33.190  59.729 0.70 65.95  ? 638  VAL B O     1 
ATOM   1546  O  O     B VAL A  1  196 ? 35.122  33.668  63.275 0.30 53.69  ? 638  VAL B O     1 
ATOM   1547  C  CB    A VAL A  1  196 ? 34.480  33.249  61.841 0.70 71.08  ? 638  VAL B CB    1 
ATOM   1548  C  CB    B VAL A  1  196 ? 37.279  33.307  61.441 0.30 45.40  ? 638  VAL B CB    1 
ATOM   1549  C  CG1   A VAL A  1  196 ? 35.950  33.063  62.231 0.70 72.78  ? 638  VAL B CG1   1 
ATOM   1550  C  CG1   B VAL A  1  196 ? 37.191  31.954  62.129 0.30 40.31  ? 638  VAL B CG1   1 
ATOM   1551  C  CG2   A VAL A  1  196 ? 33.817  34.442  62.556 0.70 72.82  ? 638  VAL B CG2   1 
ATOM   1552  C  CG2   B VAL A  1  196 ? 38.220  33.234  60.241 0.30 42.15  ? 638  VAL B CG2   1 
ATOM   1553  N  N     A TYR A  1  197 ? 33.211  31.287  59.764 0.70 73.57  ? 639  TYR B N     1 
ATOM   1554  N  N     B TYR A  1  197 ? 33.610  34.272  61.703 0.30 51.08  ? 639  TYR B N     1 
ATOM   1555  C  CA    A TYR A  1  197 ? 32.075  30.428  59.413 0.70 67.70  ? 639  TYR B CA    1 
ATOM   1556  C  CA    B TYR A  1  197 ? 32.469  34.503  62.595 0.30 47.69  ? 639  TYR B CA    1 
ATOM   1557  C  C     A TYR A  1  197 ? 31.496  29.745  60.640 0.70 70.60  ? 639  TYR B C     1 
ATOM   1558  C  C     B TYR A  1  197 ? 31.577  35.593  62.008 0.30 44.60  ? 639  TYR B C     1 
ATOM   1559  O  O     A TYR A  1  197 ? 31.460  30.333  61.720 0.70 70.29  ? 639  TYR B O     1 
ATOM   1560  O  O     B TYR A  1  197 ? 30.705  36.126  62.680 0.30 40.60  ? 639  TYR B O     1 
ATOM   1561  C  CB    A TYR A  1  197 ? 32.480  29.385  58.378 0.70 61.89  ? 639  TYR B CB    1 
ATOM   1562  C  CB    B TYR A  1  197 ? 32.930  34.872  64.012 0.30 48.79  ? 639  TYR B CB    1 
ATOM   1563  C  CG    A TYR A  1  197 ? 32.303  29.831  56.961 0.70 57.59  ? 639  TYR B CG    1 
ATOM   1564  C  CG    B TYR A  1  197 ? 33.028  36.349  64.331 0.30 48.89  ? 639  TYR B CG    1 
ATOM   1565  C  CD1   A TYR A  1  197 ? 31.012  30.124  56.454 0.70 56.34  ? 639  TYR B CD1   1 
ATOM   1566  C  CD1   B TYR A  1  197 ? 31.892  37.093  64.621 0.30 48.64  ? 639  TYR B CD1   1 
ATOM   1567  C  CD2   A TYR A  1  197 ? 33.415  29.957  56.114 0.70 53.55  ? 639  TYR B CD2   1 
ATOM   1568  C  CD2   B TYR A  1  197 ? 34.268  36.985  64.402 0.30 47.77  ? 639  TYR B CD2   1 
ATOM   1569  C  CE1   A TYR A  1  197 ? 30.847  30.564  55.147 0.70 56.85  ? 639  TYR B CE1   1 
ATOM   1570  C  CE1   B TYR A  1  197 ? 31.982  38.439  64.933 0.30 49.42  ? 639  TYR B CE1   1 
ATOM   1571  C  CE2   A TYR A  1  197 ? 33.266  30.377  54.796 0.70 52.68  ? 639  TYR B CE2   1 
ATOM   1572  C  CE2   B TYR A  1  197 ? 34.375  38.338  64.689 0.30 47.89  ? 639  TYR B CE2   1 
ATOM   1573  C  CZ    A TYR A  1  197 ? 31.987  30.685  54.317 0.70 51.79  ? 639  TYR B CZ    1 
ATOM   1574  C  CZ    B TYR A  1  197 ? 33.226  39.046  64.982 0.30 50.07  ? 639  TYR B CZ    1 
ATOM   1575  O  OH    A TYR A  1  197 ? 31.819  31.090  53.032 0.70 40.22  ? 639  TYR B OH    1 
ATOM   1576  O  OH    B TYR A  1  197 ? 33.352  40.375  65.269 0.30 49.08  ? 639  TYR B OH    1 
ATOM   1577  N  N     . ILE A  1  210 ? 21.941  43.061  78.893 1.00 83.37  ? 1009 ILE B N     1 
ATOM   1578  C  CA    . ILE A  1  210 ? 20.787  42.315  78.357 1.00 86.09  ? 1009 ILE B CA    1 
ATOM   1579  C  C     . ILE A  1  210 ? 19.794  43.301  77.696 1.00 88.06  ? 1009 ILE B C     1 
ATOM   1580  O  O     . ILE A  1  210 ? 18.823  42.871  77.072 1.00 88.76  ? 1009 ILE B O     1 
ATOM   1581  C  CB    . ILE A  1  210 ? 20.152  41.376  79.435 1.00 71.20  ? 1009 ILE B CB    1 
ATOM   1582  N  N     . ASN A  1  211 ? 20.051  44.601  77.789 1.00 79.31  ? 1010 ASN B N     1 
ATOM   1583  C  CA    . ASN A  1  211 ? 19.202  45.534  77.097 1.00 73.92  ? 1010 ASN B CA    1 
ATOM   1584  C  C     . ASN A  1  211 ? 19.970  46.739  76.622 1.00 70.72  ? 1010 ASN B C     1 
ATOM   1585  O  O     . ASN A  1  211 ? 19.358  47.730  76.222 1.00 76.97  ? 1010 ASN B O     1 
ATOM   1586  C  CB    . ASN A  1  211 ? 17.946  45.947  77.916 1.00 79.41  ? 1010 ASN B CB    1 
ATOM   1587  C  CG    . ASN A  1  211 ? 18.256  46.276  79.380 1.00 92.27  ? 1010 ASN B CG    1 
ATOM   1588  O  OD1   . ASN A  1  211 ? 19.006  47.215  79.695 1.00 92.20  ? 1010 ASN B OD1   1 
ATOM   1589  N  ND2   . ASN A  1  211 ? 17.652  45.516  80.286 1.00 87.77  ? 1010 ASN B ND2   1 
ATOM   1590  N  N     . GLU A  1  212 ? 21.293  46.672  76.667 1.00 59.98  ? 1011 GLU B N     1 
ATOM   1591  C  CA    . GLU A  1  212 ? 22.116  47.792  76.236 1.00 55.95  ? 1011 GLU B CA    1 
ATOM   1592  C  C     . GLU A  1  212 ? 23.069  47.354  75.184 1.00 53.43  ? 1011 GLU B C     1 
ATOM   1593  O  O     . GLU A  1  212 ? 23.547  46.257  75.259 1.00 56.21  ? 1011 GLU B O     1 
ATOM   1594  C  CB    . GLU A  1  212 ? 22.961  48.283  77.371 1.00 61.32  ? 1011 GLU B CB    1 
ATOM   1595  C  CG    . GLU A  1  212 ? 22.251  49.126  78.413 1.00 75.89  ? 1011 GLU B CG    1 
ATOM   1596  C  CD    . GLU A  1  212 ? 23.249  49.683  79.421 1.00 87.80  ? 1011 GLU B CD    1 
ATOM   1597  O  OE1   . GLU A  1  212 ? 23.985  48.855  80.017 1.00 91.88  ? 1011 GLU B OE1   1 
ATOM   1598  O  OE2   . GLU A  1  212 ? 23.316  50.931  79.607 1.00 89.81  ? 1011 GLU B OE2   1 
ATOM   1599  N  N     . ARG A  1  213 ? 23.374  48.210  74.225 1.00 52.50  ? 1012 ARG B N     1 
ATOM   1600  C  CA    . ARG A  1  213 ? 24.224  47.802  73.134 1.00 47.28  ? 1012 ARG B CA    1 
ATOM   1601  C  C     . ARG A  1  213 ? 25.247  48.883  72.842 1.00 46.26  ? 1012 ARG B C     1 
ATOM   1602  O  O     . ARG A  1  213 ? 24.881  50.019  72.547 1.00 47.01  ? 1012 ARG B O     1 
ATOM   1603  C  CB    . ARG A  1  213 ? 23.359  47.511  71.906 1.00 52.76  ? 1012 ARG B CB    1 
ATOM   1604  C  CG    . ARG A  1  213 ? 24.124  47.135  70.657 1.00 61.57  ? 1012 ARG B CG    1 
ATOM   1605  C  CD    . ARG A  1  213 ? 24.933  45.863  70.849 1.00 59.72  ? 1012 ARG B CD    1 
ATOM   1606  N  NE    . ARG A  1  213 ? 24.992  45.089  69.614 1.00 61.39  ? 1012 ARG B NE    1 
ATOM   1607  C  CZ    . ARG A  1  213 ? 25.815  44.065  69.391 1.00 61.87  ? 1012 ARG B CZ    1 
ATOM   1608  N  NH1   . ARG A  1  213 ? 26.677  43.689  70.315 1.00 56.20  ? 1012 ARG B NH1   1 
ATOM   1609  N  NH2   . ARG A  1  213 ? 25.777  43.428  68.225 1.00 64.93  ? 1012 ARG B NH2   1 
ATOM   1610  N  N     . ASN A  1  214 ? 26.522  48.543  72.940 1.00 37.28  ? 1013 ASN B N     1 
ATOM   1611  C  CA    . ASN A  1  214 ? 27.559  49.496  72.599 1.00 42.47  ? 1013 ASN B CA    1 
ATOM   1612  C  C     . ASN A  1  214 ? 27.494  49.745  71.104 1.00 41.59  ? 1013 ASN B C     1 
ATOM   1613  O  O     . ASN A  1  214 ? 27.419  48.793  70.340 1.00 42.50  ? 1013 ASN B O     1 
ATOM   1614  C  CB    . ASN A  1  214 ? 28.937  48.918  72.972 1.00 47.69  ? 1013 ASN B CB    1 
ATOM   1615  C  CG    . ASN A  1  214 ? 30.082  49.857  72.622 1.00 55.80  ? 1013 ASN B CG    1 
ATOM   1616  O  OD1   . ASN A  1  214 ? 30.947  49.507  71.858 1.00 67.15  ? 1013 ASN B OD1   1 
ATOM   1617  N  ND2   . ASN A  1  214 ? 30.062  51.065  73.149 1.00 72.07  ? 1013 ASN B ND2   1 
ATOM   1618  N  N     . ILE A  1  215 ? 27.523  51.002  70.698 1.00 38.63  ? 1014 ILE B N     1 
ATOM   1619  C  CA    . ILE A  1  215 ? 27.379  51.367  69.295 1.00 36.72  ? 1014 ILE B CA    1 
ATOM   1620  C  C     . ILE A  1  215 ? 28.540  50.825  68.432 1.00 42.96  ? 1014 ILE B C     1 
ATOM   1621  O  O     . ILE A  1  215 ? 28.304  50.360  67.317 1.00 47.14  ? 1014 ILE B O     1 
ATOM   1622  C  CB    . ILE A  1  215 ? 27.179  52.890  69.102 1.00 32.42  ? 1014 ILE B CB    1 
ATOM   1623  C  CG1   . ILE A  1  215 ? 26.716  53.180  67.673 1.00 33.02  ? 1014 ILE B CG1   1 
ATOM   1624  C  CG2   . ILE A  1  215 ? 28.504  53.635  69.333 1.00 32.09  ? 1014 ILE B CG2   1 
ATOM   1625  C  CD1   . ILE A  1  215 ? 26.230  54.603  67.427 1.00 34.90  ? 1014 ILE B CD1   1 
ATOM   1626  N  N     . THR A  1  216 ? 29.774  50.900  68.923 1.00 43.67  ? 1015 THR B N     1 
ATOM   1627  C  CA    . THR A  1  216 ? 30.896  50.398  68.169 1.00 40.02  ? 1015 THR B CA    1 
ATOM   1628  C  C     . THR A  1  216 ? 30.724  48.873  67.921 1.00 40.25  ? 1015 THR B C     1 
ATOM   1629  O  O     . THR A  1  216 ? 30.950  48.401  66.813 1.00 38.83  ? 1015 THR B O     1 
ATOM   1630  C  CB    . THR A  1  216 ? 32.216  50.749  68.880 1.00 35.73  ? 1015 THR B CB    1 
ATOM   1631  O  OG1   . THR A  1  216 ? 32.554  52.090  68.557 1.00 43.11  ? 1015 THR B OG1   1 
ATOM   1632  C  CG2   . THR A  1  216 ? 33.406  49.835  68.464 1.00 35.72  ? 1015 THR B CG2   1 
ATOM   1633  N  N     . SER A  1  217 ? 30.306  48.137  68.947 1.00 40.57  ? 1016 SER B N     1 
ATOM   1634  C  CA    . SER A  1  217 ? 30.068  46.690  68.820 1.00 43.03  ? 1016 SER B CA    1 
ATOM   1635  C  C     . SER A  1  217 ? 28.944  46.376  67.836 1.00 40.78  ? 1016 SER B C     1 
ATOM   1636  O  O     . SER A  1  217 ? 29.061  45.428  67.048 1.00 38.74  ? 1016 SER B O     1 
ATOM   1637  C  CB    . SER A  1  217 ? 29.722  46.083  70.162 1.00 43.91  ? 1016 SER B CB    1 
ATOM   1638  O  OG    . SER A  1  217 ? 30.767  46.250  71.077 1.00 56.58  ? 1016 SER B OG    1 
ATOM   1639  N  N     . GLU A  1  218 ? 27.878  47.192  67.894 1.00 36.69  ? 1017 GLU B N     1 
ATOM   1640  C  CA    . GLU A  1  218 ? 26.717  46.998  67.063 1.00 35.94  ? 1017 GLU B CA    1 
ATOM   1641  C  C     . GLU A  1  218 ? 27.106  47.217  65.609 1.00 37.57  ? 1017 GLU B C     1 
ATOM   1642  O  O     . GLU A  1  218 ? 26.703  46.448  64.730 1.00 33.25  ? 1017 GLU B O     1 
ATOM   1643  C  CB    . GLU A  1  218 ? 25.589  47.937  67.465 1.00 35.71  ? 1017 GLU B CB    1 
ATOM   1644  C  CG    . GLU A  1  218 ? 24.396  47.939  66.500 1.00 37.98  ? 1017 GLU B CG    1 
ATOM   1645  C  CD    . GLU A  1  218 ? 23.657  46.586  66.450 1.00 41.30  ? 1017 GLU B CD    1 
ATOM   1646  O  OE1   . GLU A  1  218 ? 23.606  45.866  67.474 1.00 41.54  ? 1017 GLU B OE1   1 
ATOM   1647  O  OE2   . GLU A  1  218 ? 23.157  46.215  65.383 1.00 39.67  ? 1017 GLU B OE2   1 
ATOM   1648  N  N     . MET A  1  219 ? 27.911  48.245  65.365 1.00 36.75  ? 1018 MET B N     1 
ATOM   1649  C  CA    . MET A  1  219 ? 28.349  48.560  64.009 1.00 32.43  ? 1018 MET B CA    1 
ATOM   1650  C  C     . MET A  1  219 ? 29.252  47.463  63.476 1.00 35.91  ? 1018 MET B C     1 
ATOM   1651  O  O     . MET A  1  219 ? 29.058  47.002  62.365 1.00 41.51  ? 1018 MET B O     1 
ATOM   1652  C  CB    . MET A  1  219 ? 29.104  49.889  63.965 1.00 31.12  ? 1018 MET B CB    1 
ATOM   1653  C  CG    . MET A  1  219 ? 28.194  51.101  64.128 1.00 35.13  ? 1018 MET B CG    1 
ATOM   1654  S  SD    . MET A  1  219 ? 27.118  51.382  62.738 1.00 37.89  ? 1018 MET B SD    1 
ATOM   1655  C  CE    . MET A  1  219 ? 28.290  51.501  61.418 1.00 31.69  ? 1018 MET B CE    1 
ATOM   1656  N  N     . ARG A  1  220 ? 30.242  47.046  64.247 1.00 35.58  ? 1019 ARG B N     1 
ATOM   1657  C  CA    . ARG A  1  220 ? 31.179  46.051  63.781 1.00 32.77  ? 1019 ARG B CA    1 
ATOM   1658  C  C     . ARG A  1  220 ? 30.405  44.750  63.476 1.00 33.97  ? 1019 ARG B C     1 
ATOM   1659  O  O     . ARG A  1  220 ? 30.599  44.177  62.431 1.00 35.44  ? 1019 ARG B O     1 
ATOM   1660  C  CB    . ARG A  1  220 ? 32.293  45.842  64.804 1.00 28.99  ? 1019 ARG B CB    1 
ATOM   1661  C  CG    . ARG A  1  220 ? 33.299  47.013  64.882 1.00 33.73  ? 1019 ARG B CG    1 
ATOM   1662  C  CD    . ARG A  1  220 ? 34.174  47.050  66.139 1.00 33.58  ? 1019 ARG B CD    1 
ATOM   1663  N  NE    . ARG A  1  220 ? 35.035  45.878  66.170 1.00 44.35  ? 1019 ARG B NE    1 
ATOM   1664  C  CZ    . ARG A  1  220 ? 36.270  45.815  65.666 1.00 51.99  ? 1019 ARG B CZ    1 
ATOM   1665  N  NH1   . ARG A  1  220 ? 36.819  46.889  65.098 1.00 60.44  ? 1019 ARG B NH1   1 
ATOM   1666  N  NH2   . ARG A  1  220 ? 36.944  44.665  65.703 1.00 51.21  ? 1019 ARG B NH2   1 
ATOM   1667  N  N     . GLU A  1  221 ? 29.520  44.304  64.349 1.00 34.37  ? 1020 GLU B N     1 
ATOM   1668  C  CA    . GLU A  1  221 ? 28.807  43.049  64.130 1.00 37.07  ? 1020 GLU B CA    1 
ATOM   1669  C  C     . GLU A  1  221 ? 27.766  43.095  63.041 1.00 35.05  ? 1020 GLU B C     1 
ATOM   1670  O  O     . GLU A  1  221 ? 27.618  42.142  62.303 1.00 34.61  ? 1020 GLU B O     1 
ATOM   1671  C  CB    . GLU A  1  221 ? 28.129  42.590  65.396 1.00 43.83  ? 1020 GLU B CB    1 
ATOM   1672  C  CG    . GLU A  1  221 ? 29.143  42.086  66.391 1.00 58.98  ? 1020 GLU B CG    1 
ATOM   1673  C  CD    . GLU A  1  221 ? 28.558  41.883  67.775 1.00 64.83  ? 1020 GLU B CD    1 
ATOM   1674  O  OE1   . GLU A  1  221 ? 29.322  42.075  68.750 1.00 66.87  ? 1020 GLU B OE1   1 
ATOM   1675  O  OE2   . GLU A  1  221 ? 27.354  41.521  67.894 1.00 65.83  ? 1020 GLU B OE2   1 
ATOM   1676  N  N     . SER A  1  222 ? 27.011  44.182  62.952 1.00 34.40  ? 1021 SER B N     1 
ATOM   1677  C  CA    . SER A  1  222 ? 25.981  44.288  61.938 1.00 28.96  ? 1021 SER B CA    1 
ATOM   1678  C  C     . SER A  1  222 ? 26.623  44.469  60.565 1.00 31.34  ? 1021 SER B C     1 
ATOM   1679  O  O     . SER A  1  222 ? 26.148  43.936  59.593 1.00 34.48  ? 1021 SER B O     1 
ATOM   1680  C  CB    . SER A  1  222 ? 25.089  45.492  62.231 1.00 29.16  ? 1021 SER B CB    1 
ATOM   1681  O  OG    . SER A  1  222 ? 24.142  45.185  63.193 1.00 34.23  ? 1021 SER B OG    1 
ATOM   1682  N  N     . PHE A  1  223 ? 27.646  45.294  60.465 1.00 31.03  ? 1022 PHE B N     1 
ATOM   1683  C  CA    . PHE A  1  223 ? 28.300  45.472  59.200 1.00 33.12  ? 1022 PHE B CA    1 
ATOM   1684  C  C     . PHE A  1  223 ? 29.015  44.193  58.703 1.00 32.82  ? 1022 PHE B C     1 
ATOM   1685  O  O     . PHE A  1  223 ? 28.982  43.879  57.507 1.00 33.33  ? 1022 PHE B O     1 
ATOM   1686  C  CB    . PHE A  1  223 ? 29.269  46.647  59.245 1.00 30.27  ? 1022 PHE B CB    1 
ATOM   1687  C  CG    . PHE A  1  223 ? 29.632  47.096  57.911 1.00 30.44  ? 1022 PHE B CG    1 
ATOM   1688  C  CD1   . PHE A  1  223 ? 28.747  47.907  57.201 1.00 29.82  ? 1022 PHE B CD1   1 
ATOM   1689  C  CD2   . PHE A  1  223 ? 30.796  46.639  57.305 1.00 28.87  ? 1022 PHE B CD2   1 
ATOM   1690  C  CE1   . PHE A  1  223 ? 29.051  48.289  55.889 1.00 31.70  ? 1022 PHE B CE1   1 
ATOM   1691  C  CE2   . PHE A  1  223 ? 31.112  47.046  56.009 1.00 28.49  ? 1022 PHE B CE2   1 
ATOM   1692  C  CZ    . PHE A  1  223 ? 30.239  47.857  55.300 1.00 26.91  ? 1022 PHE B CZ    1 
ATOM   1693  N  N     . LEU A  1  224 ? 29.670  43.483  59.602 1.00 30.97  ? 1023 LEU B N     1 
ATOM   1694  C  CA    . LEU A  1  224 ? 30.387  42.282  59.233 1.00 32.94  ? 1023 LEU B CA    1 
ATOM   1695  C  C     . LEU A  1  224 ? 29.419  41.215  58.729 1.00 32.81  ? 1023 LEU B C     1 
ATOM   1696  O  O     . LEU A  1  224 ? 29.761  40.460  57.803 1.00 35.72  ? 1023 LEU B O     1 
ATOM   1697  C  CB    . LEU A  1  224 ? 31.159  41.745  60.418 1.00 36.51  ? 1023 LEU B CB    1 
ATOM   1698  C  CG    . LEU A  1  224 ? 31.954  40.462  60.210 1.00 41.18  ? 1023 LEU B CG    1 
ATOM   1699  C  CD1   . LEU A  1  224 ? 33.107  40.676  59.226 1.00 43.17  ? 1023 LEU B CD1   1 
ATOM   1700  C  CD2   . LEU A  1  224 ? 32.444  39.964  61.549 1.00 39.05  ? 1023 LEU B CD2   1 
ATOM   1701  N  N     A ASP A  1  225 ? 28.245  41.140  59.339 0.50 30.82  ? 1024 ASP B N     1 
ATOM   1702  N  N     B ASP A  1  225 ? 28.246  41.171  59.355 0.50 31.12  ? 1024 ASP B N     1 
ATOM   1703  C  CA    A ASP A  1  225 ? 27.245  40.207  58.902 0.50 32.11  ? 1024 ASP B CA    1 
ATOM   1704  C  CA    B ASP A  1  225 ? 27.204  40.246  58.995 0.50 32.51  ? 1024 ASP B CA    1 
ATOM   1705  C  C     A ASP A  1  225 ? 26.819  40.480  57.476 0.50 32.04  ? 1024 ASP B C     1 
ATOM   1706  C  C     B ASP A  1  225 ? 26.758  40.479  57.539 0.50 32.36  ? 1024 ASP B C     1 
ATOM   1707  O  O     A ASP A  1  225 ? 26.678  39.558  56.704 0.50 33.25  ? 1024 ASP B O     1 
ATOM   1708  O  O     B ASP A  1  225 ? 26.697  39.542  56.752 0.50 33.12  ? 1024 ASP B O     1 
ATOM   1709  C  CB    A ASP A  1  225 ? 26.020  40.286  59.801 0.50 32.18  ? 1024 ASP B CB    1 
ATOM   1710  C  CB    B ASP A  1  225 ? 26.050  40.384  59.990 0.50 33.27  ? 1024 ASP B CB    1 
ATOM   1711  C  CG    A ASP A  1  225 ? 26.181  39.488  61.064 0.50 31.68  ? 1024 ASP B CG    1 
ATOM   1712  C  CG    B ASP A  1  225 ? 24.932  39.467  59.703 0.50 32.55  ? 1024 ASP B CG    1 
ATOM   1713  O  OD1   A ASP A  1  225 ? 27.196  38.784  61.192 0.50 31.42  ? 1024 ASP B OD1   1 
ATOM   1714  O  OD1   B ASP A  1  225 ? 25.218  38.371  59.219 0.50 36.00  ? 1024 ASP B OD1   1 
ATOM   1715  O  OD2   A ASP A  1  225 ? 25.297  39.578  61.935 0.50 32.13  ? 1024 ASP B OD2   1 
ATOM   1716  O  OD2   B ASP A  1  225 ? 23.770  39.811  59.988 0.50 32.51  ? 1024 ASP B OD2   1 
ATOM   1717  N  N     . TYR A  1  226 ? 26.577  41.748  57.163 1.00 31.48  ? 1025 TYR B N     1 
ATOM   1718  C  CA    . TYR A  1  226 ? 26.157  42.133  55.849 1.00 29.74  ? 1025 TYR B CA    1 
ATOM   1719  C  C     . TYR A  1  226 ? 27.259  41.944  54.843 1.00 29.56  ? 1025 TYR B C     1 
ATOM   1720  O  O     . TYR A  1  226 ? 27.017  41.444  53.779 1.00 31.43  ? 1025 TYR B O     1 
ATOM   1721  C  CB    . TYR A  1  226 ? 25.648  43.584  55.827 1.00 26.76  ? 1025 TYR B CB    1 
ATOM   1722  C  CG    . TYR A  1  226 ? 25.313  44.051  54.445 1.00 28.31  ? 1025 TYR B CG    1 
ATOM   1723  C  CD1   . TYR A  1  226 ? 24.184  43.577  53.799 1.00 30.62  ? 1025 TYR B CD1   1 
ATOM   1724  C  CD2   . TYR A  1  226 ? 26.105  44.960  53.788 1.00 28.87  ? 1025 TYR B CD2   1 
ATOM   1725  C  CE1   . TYR A  1  226 ? 23.824  44.022  52.539 1.00 29.67  ? 1025 TYR B CE1   1 
ATOM   1726  C  CE2   . TYR A  1  226 ? 25.780  45.397  52.518 1.00 27.50  ? 1025 TYR B CE2   1 
ATOM   1727  C  CZ    . TYR A  1  226 ? 24.640  44.918  51.916 1.00 30.41  ? 1025 TYR B CZ    1 
ATOM   1728  O  OH    . TYR A  1  226 ? 24.287  45.282  50.667 1.00 31.72  ? 1025 TYR B OH    1 
ATOM   1729  N  N     . ALA A  1  227 ? 28.457  42.406  55.164 1.00 29.49  ? 1026 ALA B N     1 
ATOM   1730  C  CA    . ALA A  1  227 ? 29.592  42.308  54.222 1.00 27.67  ? 1026 ALA B CA    1 
ATOM   1731  C  C     . ALA A  1  227 ? 29.923  40.874  53.890 1.00 26.81  ? 1026 ALA B C     1 
ATOM   1732  O  O     . ALA A  1  227 ? 30.223  40.550  52.770 1.00 31.52  ? 1026 ALA B O     1 
ATOM   1733  C  CB    . ALA A  1  227 ? 30.835  42.964  54.767 1.00 20.28  ? 1026 ALA B CB    1 
ATOM   1734  N  N     . MET A  1  228 ? 29.899  40.019  54.872 1.00 26.37  ? 1027 MET B N     1 
ATOM   1735  C  CA    . MET A  1  228 ? 30.254  38.610  54.623 1.00 33.61  ? 1027 MET B CA    1 
ATOM   1736  C  C     . MET A  1  228 ? 29.208  37.943  53.775 1.00 33.45  ? 1027 MET B C     1 
ATOM   1737  O  O     . MET A  1  228 ? 29.551  37.132  52.896 1.00 32.06  ? 1027 MET B O     1 
ATOM   1738  C  CB    . MET A  1  228 ? 30.353  37.840  55.936 1.00 40.75  ? 1027 MET B CB    1 
ATOM   1739  C  CG    . MET A  1  228 ? 31.567  36.935  56.019 1.00 58.28  ? 1027 MET B CG    1 
ATOM   1740  S  SD    . MET A  1  228 ? 31.491  35.911  57.499 1.00 67.59  ? 1027 MET B SD    1 
ATOM   1741  C  CE    . MET A  1  228 ? 30.418  34.635  56.845 1.00 55.32  ? 1027 MET B CE    1 
ATOM   1742  N  N     . SER A  1  229 ? 27.932  38.252  54.031 1.00 30.71  ? 1028 SER B N     1 
ATOM   1743  C  CA    . SER A  1  229 ? 26.831  37.637  53.256 1.00 29.59  ? 1028 SER B CA    1 
ATOM   1744  C  C     . SER A  1  229 ? 26.925  38.039  51.807 1.00 32.39  ? 1028 SER B C     1 
ATOM   1745  O  O     . SER A  1  229 ? 26.732  37.218  50.949 1.00 34.02  ? 1028 SER B O     1 
ATOM   1746  C  CB    . SER A  1  229 ? 25.500  38.118  53.780 1.00 30.60  ? 1028 SER B CB    1 
ATOM   1747  O  OG    . SER A  1  229 ? 24.486  37.270  53.310 1.00 31.85  ? 1028 SER B OG    1 
ATOM   1748  N  N     . VAL A  1  230 ? 27.283  39.294  51.524 1.00 27.25  ? 1029 VAL B N     1 
ATOM   1749  C  CA    . VAL A  1  230 ? 27.420  39.753  50.173 1.00 24.78  ? 1029 VAL B CA    1 
ATOM   1750  C  C     . VAL A  1  230 ? 28.609  39.097  49.464 1.00 25.70  ? 1029 VAL B C     1 
ATOM   1751  O  O     . VAL A  1  230 ? 28.535  38.790  48.313 1.00 25.22  ? 1029 VAL B O     1 
ATOM   1752  C  CB    . VAL A  1  230 ? 27.577  41.284  50.113 1.00 27.74  ? 1029 VAL B CB    1 
ATOM   1753  C  CG1   . VAL A  1  230 ? 27.906  41.701  48.693 1.00 24.44  ? 1029 VAL B CG1   1 
ATOM   1754  C  CG2   . VAL A  1  230 ? 26.272  41.940  50.556 1.00 26.84  ? 1029 VAL B CG2   1 
ATOM   1755  N  N     . ILE A  1  231 ? 29.721  38.934  50.143 1.00 29.50  ? 1030 ILE B N     1 
ATOM   1756  C  CA    . ILE A  1  231 ? 30.897  38.266  49.589 1.00 30.70  ? 1030 ILE B CA    1 
ATOM   1757  C  C     . ILE A  1  231 ? 30.645  36.776  49.316 1.00 30.09  ? 1030 ILE B C     1 
ATOM   1758  O  O     . ILE A  1  231 ? 30.904  36.309  48.231 1.00 28.90  ? 1030 ILE B O     1 
ATOM   1759  C  CB    . ILE A  1  231 ? 32.099  38.422  50.550 1.00 29.39  ? 1030 ILE B CB    1 
ATOM   1760  C  CG1   . ILE A  1  231 ? 32.547  39.889  50.540 1.00 29.07  ? 1030 ILE B CG1   1 
ATOM   1761  C  CG2   . ILE A  1  231 ? 33.226  37.444  50.211 1.00 27.85  ? 1030 ILE B CG2   1 
ATOM   1762  C  CD1   . ILE A  1  231 ? 33.423  40.284  51.734 1.00 29.20  ? 1030 ILE B CD1   1 
ATOM   1763  N  N     . VAL A  1  232 ? 30.138  36.047  50.300 1.00 32.14  ? 1031 VAL B N     1 
ATOM   1764  C  CA    . VAL A  1  232 ? 29.952  34.603  50.141 1.00 30.11  ? 1031 VAL B CA    1 
ATOM   1765  C  C     . VAL A  1  232 ? 28.594  34.185  49.681 1.00 31.23  ? 1031 VAL B C     1 
ATOM   1766  O  O     . VAL A  1  232 ? 28.453  33.049  49.271 1.00 36.58  ? 1031 VAL B O     1 
ATOM   1767  C  CB    . VAL A  1  232 ? 30.335  33.802  51.418 1.00 31.71  ? 1031 VAL B CB    1 
ATOM   1768  C  CG1   . VAL A  1  232 ? 31.663  34.303  52.030 1.00 24.37  ? 1031 VAL B CG1   1 
ATOM   1769  C  CG2   . VAL A  1  232 ? 29.228  33.818  52.471 1.00 29.88  ? 1031 VAL B CG2   1 
ATOM   1770  N  N     . ALA A  1  233 ? 27.597  35.059  49.702 1.00 28.85  ? 1032 ALA B N     1 
ATOM   1771  C  CA    . ALA A  1  233 ? 26.247  34.608  49.313 1.00 28.65  ? 1032 ALA B CA    1 
ATOM   1772  C  C     . ALA A  1  233 ? 25.483  35.629  48.462 1.00 29.04  ? 1032 ALA B C     1 
ATOM   1773  O  O     . ALA A  1  233 ? 24.301  35.869  48.621 1.00 30.69  ? 1032 ALA B O     1 
ATOM   1774  C  CB    . ALA A  1  233 ? 25.469  34.252  50.580 1.00 25.34  ? 1032 ALA B CB    1 
ATOM   1775  N  N     . ARG A  1  234 ? 26.144  36.230  47.496 1.00 31.12  ? 1033 ARG B N     1 
ATOM   1776  C  CA    . ARG A  1  234 ? 25.470  37.173  46.619 1.00 26.68  ? 1033 ARG B CA    1 
ATOM   1777  C  C     . ARG A  1  234 ? 26.238  37.656  45.392 1.00 27.27  ? 1033 ARG B C     1 
ATOM   1778  O  O     . ARG A  1  234 ? 25.743  37.493  44.308 1.00 27.23  ? 1033 ARG B O     1 
ATOM   1779  C  CB    . ARG A  1  234 ? 24.980  38.400  47.399 1.00 24.69  ? 1033 ARG B CB    1 
ATOM   1780  C  CG    . ARG A  1  234 ? 24.247  39.408  46.543 1.00 28.06  ? 1033 ARG B CG    1 
ATOM   1781  C  CD    . ARG A  1  234 ? 23.564  40.542  47.332 1.00 28.68  ? 1033 ARG B CD    1 
ATOM   1782  N  NE    . ARG A  1  234 ? 22.741  39.960  48.398 1.00 28.41  ? 1033 ARG B NE    1 
ATOM   1783  C  CZ    . ARG A  1  234 ? 22.094  40.647  49.337 1.00 32.98  ? 1033 ARG B CZ    1 
ATOM   1784  N  NH1   . ARG A  1  234 ? 22.127  41.991  49.346 1.00 29.40  ? 1033 ARG B NH1   1 
ATOM   1785  N  NH2   . ARG A  1  234 ? 21.409  39.974  50.270 1.00 32.86  ? 1033 ARG B NH2   1 
ATOM   1786  N  N     . ALA A  1  235 ? 27.349  38.360  45.589 1.00 25.62  ? 1034 ALA B N     1 
ATOM   1787  C  CA    . ALA A  1  235 ? 27.961  39.129  44.497 1.00 28.09  ? 1034 ALA B CA    1 
ATOM   1788  C  C     . ALA A  1  235 ? 29.150  38.422  43.813 1.00 28.44  ? 1034 ALA B C     1 
ATOM   1789  O  O     . ALA A  1  235 ? 29.556  38.843  42.751 1.00 28.56  ? 1034 ALA B O     1 
ATOM   1790  C  CB    . ALA A  1  235 ? 28.400  40.533  45.006 1.00 25.55  ? 1034 ALA B CB    1 
ATOM   1791  N  N     . LEU A  1  236 ? 29.681  37.365  44.388 1.00 25.98  ? 1035 LEU B N     1 
ATOM   1792  C  CA    . LEU A  1  236 ? 30.867  36.695  43.830 1.00 28.76  ? 1035 LEU B CA    1 
ATOM   1793  C  C     . LEU A  1  236 ? 30.547  35.237  43.420 1.00 30.39  ? 1035 LEU B C     1 
ATOM   1794  O  O     . LEU A  1  236 ? 29.830  34.525  44.111 1.00 31.12  ? 1035 LEU B O     1 
ATOM   1795  C  CB    . LEU A  1  236 ? 32.000  36.676  44.861 1.00 25.62  ? 1035 LEU B CB    1 
ATOM   1796  C  CG    . LEU A  1  236 ? 32.427  38.029  45.420 1.00 27.49  ? 1035 LEU B CG    1 
ATOM   1797  C  CD1   . LEU A  1  236 ? 33.480  37.896  46.497 1.00 24.19  ? 1035 LEU B CD1   1 
ATOM   1798  C  CD2   . LEU A  1  236 ? 32.941  38.897  44.281 1.00 26.51  ? 1035 LEU B CD2   1 
ATOM   1799  N  N     . PRO A  1  237 ? 31.048  34.816  42.270 1.00 29.85  ? 1036 PRO B N     1 
ATOM   1800  C  CA    . PRO A  1  237 ? 30.824  33.477  41.754 1.00 30.79  ? 1036 PRO B CA    1 
ATOM   1801  C  C     . PRO A  1  237 ? 31.676  32.405  42.463 1.00 32.60  ? 1036 PRO B C     1 
ATOM   1802  O  O     . PRO A  1  237 ? 32.759  32.704  42.987 1.00 29.29  ? 1036 PRO B O     1 
ATOM   1803  C  CB    . PRO A  1  237 ? 31.276  33.612  40.313 1.00 30.17  ? 1036 PRO B CB    1 
ATOM   1804  C  CG    . PRO A  1  237 ? 32.417  34.588  40.397 1.00 29.48  ? 1036 PRO B CG    1 
ATOM   1805  C  CD    . PRO A  1  237 ? 32.014  35.575  41.457 1.00 31.79  ? 1036 PRO B CD    1 
ATOM   1806  N  N     . ASP A  1  238 ? 31.143  31.189  42.554 1.00 30.87  ? 1037 ASP B N     1 
ATOM   1807  C  CA    . ASP A  1  238 ? 31.946  30.062  42.970 1.00 28.58  ? 1037 ASP B CA    1 
ATOM   1808  C  C     . ASP A  1  238 ? 32.945  29.690  41.884 1.00 27.40  ? 1037 ASP B C     1 
ATOM   1809  O  O     . ASP A  1  238 ? 32.557  29.648  40.705 1.00 30.57  ? 1037 ASP B O     1 
ATOM   1810  C  CB    . ASP A  1  238 ? 31.054  28.863  43.302 1.00 30.77  ? 1037 ASP B CB    1 
ATOM   1811  C  CG    . ASP A  1  238 ? 31.805  27.815  44.099 1.00 31.51  ? 1037 ASP B CG    1 
ATOM   1812  O  OD1   . ASP A  1  238 ? 32.644  27.097  43.533 1.00 30.86  ? 1037 ASP B OD1   1 
ATOM   1813  O  OD2   . ASP A  1  238 ? 31.657  27.763  45.341 1.00 36.75  ? 1037 ASP B OD2   1 
ATOM   1814  N  N     . VAL A  1  239 ? 34.197  29.390  42.251 1.00 27.30  ? 1038 VAL B N     1 
ATOM   1815  C  CA    . VAL A  1  239 ? 35.211  29.043  41.259 1.00 27.08  ? 1038 VAL B CA    1 
ATOM   1816  C  C     . VAL A  1  239 ? 34.834  27.743  40.543 1.00 28.45  ? 1038 VAL B C     1 
ATOM   1817  O  O     . VAL A  1  239 ? 35.172  27.541  39.373 1.00 30.00  ? 1038 VAL B O     1 
ATOM   1818  C  CB    . VAL A  1  239 ? 36.645  28.930  41.854 1.00 26.23  ? 1038 VAL B CB    1 
ATOM   1819  C  CG1   . VAL A  1  239 ? 36.795  27.667  42.690 1.00 24.62  ? 1038 VAL B CG1   1 
ATOM   1820  C  CG2   . VAL A  1  239 ? 37.674  28.847  40.748 1.00 24.88  ? 1038 VAL B CG2   1 
ATOM   1821  N  N     . ARG A  1  240 ? 34.107  26.892  41.227 1.00 28.22  ? 1039 ARG B N     1 
ATOM   1822  C  CA    . ARG A  1  240 ? 33.749  25.559  40.667 1.00 29.00  ? 1039 ARG B CA    1 
ATOM   1823  C  C     . ARG A  1  240 ? 32.704  25.573  39.564 1.00 33.56  ? 1039 ARG B C     1 
ATOM   1824  O  O     . ARG A  1  240 ? 32.932  24.964  38.522 1.00 34.18  ? 1039 ARG B O     1 
ATOM   1825  C  CB    . ARG A  1  240 ? 33.343  24.623  41.791 1.00 25.92  ? 1039 ARG B CB    1 
ATOM   1826  C  CG    . ARG A  1  240 ? 34.466  24.352  42.788 1.00 26.70  ? 1039 ARG B CG    1 
ATOM   1827  C  CD    . ARG A  1  240 ? 33.938  23.705  44.068 1.00 29.22  ? 1039 ARG B CD    1 
ATOM   1828  N  NE    . ARG A  1  240 ? 33.030  24.601  44.778 1.00 31.93  ? 1039 ARG B NE    1 
ATOM   1829  C  CZ    . ARG A  1  240 ? 32.247  24.225  45.774 1.00 32.90  ? 1039 ARG B CZ    1 
ATOM   1830  N  NH1   . ARG A  1  240 ? 32.254  22.956  46.172 1.00 30.59  ? 1039 ARG B NH1   1 
ATOM   1831  N  NH2   . ARG A  1  240 ? 31.467  25.116  46.375 1.00 32.01  ? 1039 ARG B NH2   1 
ATOM   1832  N  N     . ASP A  1  241 ? 31.575  26.274  39.736 1.00 31.05  ? 1040 ASP B N     1 
ATOM   1833  C  CA    . ASP A  1  241 ? 30.567  26.269  38.635 1.00 29.81  ? 1040 ASP B CA    1 
ATOM   1834  C  C     . ASP A  1  241 ? 30.372  27.661  38.029 1.00 30.79  ? 1040 ASP B C     1 
ATOM   1835  O  O     . ASP A  1  241 ? 29.572  27.843  37.160 1.00 32.87  ? 1040 ASP B O     1 
ATOM   1836  C  CB    . ASP A  1  241 ? 29.208  25.746  39.150 1.00 33.29  ? 1040 ASP B CB    1 
ATOM   1837  C  CG    . ASP A  1  241 ? 28.664  26.551  40.347 1.00 35.43  ? 1040 ASP B CG    1 
ATOM   1838  O  OD1   . ASP A  1  241 ? 29.192  27.674  40.666 1.00 32.78  ? 1040 ASP B OD1   1 
ATOM   1839  O  OD2   . ASP A  1  241 ? 27.677  26.052  40.961 1.00 35.07  ? 1040 ASP B OD2   1 
ATOM   1840  N  N     . GLY A  1  242 ? 31.131  28.638  38.498 1.00 28.66  ? 1041 GLY B N     1 
ATOM   1841  C  CA    . GLY A  1  242 ? 31.078  29.981  37.975 1.00 26.35  ? 1041 GLY B CA    1 
ATOM   1842  C  C     . GLY A  1  242 ? 29.795  30.728  38.273 1.00 30.10  ? 1041 GLY B C     1 
ATOM   1843  O  O     . GLY A  1  242 ? 29.464  31.681  37.558 1.00 31.19  ? 1041 GLY B O     1 
ATOM   1844  N  N     . LEU A  1  243 ? 29.057  30.313  39.293 1.00 26.65  ? 1042 LEU B N     1 
ATOM   1845  C  CA    . LEU A  1  243 ? 27.772  30.919  39.540 1.00 27.99  ? 1042 LEU B CA    1 
ATOM   1846  C  C     . LEU A  1  243 ? 27.657  31.608  40.886 1.00 27.74  ? 1042 LEU B C     1 
ATOM   1847  O  O     . LEU A  1  243 ? 28.328  31.248  41.875 1.00 28.70  ? 1042 LEU B O     1 
ATOM   1848  C  CB    . LEU A  1  243 ? 26.682  29.833  39.490 1.00 28.14  ? 1042 LEU B CB    1 
ATOM   1849  C  CG    . LEU A  1  243 ? 26.537  29.030  38.223 1.00 28.83  ? 1042 LEU B CG    1 
ATOM   1850  C  CD1   . LEU A  1  243 ? 25.521  27.922  38.509 1.00 30.63  ? 1042 LEU B CD1   1 
ATOM   1851  C  CD2   . LEU A  1  243 ? 26.143  29.855  37.025 1.00 30.61  ? 1042 LEU B CD2   1 
ATOM   1852  N  N     . LYS A  1  244 ? 26.733  32.567  40.929 1.00 27.91  ? 1043 LYS B N     1 
ATOM   1853  C  CA    . LYS A  1  244 ? 26.301  33.237  42.155 1.00 26.25  ? 1043 LYS B CA    1 
ATOM   1854  C  C     . LYS A  1  244 ? 25.041  32.549  42.594 1.00 27.47  ? 1043 LYS B C     1 
ATOM   1855  O  O     . LYS A  1  244 ? 24.402  31.864  41.761 1.00 25.18  ? 1043 LYS B O     1 
ATOM   1856  C  CB    . LYS A  1  244 ? 26.000  34.713  41.886 1.00 24.52  ? 1043 LYS B CB    1 
ATOM   1857  C  CG    . LYS A  1  244 ? 27.193  35.478  41.266 1.00 28.10  ? 1043 LYS B CG    1 
ATOM   1858  C  CD    . LYS A  1  244 ? 26.830  36.959  41.057 1.00 28.20  ? 1043 LYS B CD    1 
ATOM   1859  C  CE    . LYS A  1  244 ? 27.887  37.746  40.264 1.00 29.34  ? 1043 LYS B CE    1 
ATOM   1860  N  NZ    . LYS A  1  244 ? 27.363  39.108  39.924 1.00 29.54  ? 1043 LYS B NZ    1 
ATOM   1861  N  N     . PRO A  1  245 ? 24.663  32.719  43.885 1.00 27.67  ? 1044 PRO B N     1 
ATOM   1862  C  CA    . PRO A  1  245 ? 23.477  32.024  44.383 1.00 27.12  ? 1044 PRO B CA    1 
ATOM   1863  C  C     . PRO A  1  245 ? 22.249  32.236  43.532 1.00 27.47  ? 1044 PRO B C     1 
ATOM   1864  O  O     . PRO A  1  245 ? 21.571  31.268  43.230 1.00 27.76  ? 1044 PRO B O     1 
ATOM   1865  C  CB    . PRO A  1  245 ? 23.297  32.585  45.794 1.00 24.48  ? 1044 PRO B CB    1 
ATOM   1866  C  CG    . PRO A  1  245 ? 24.745  32.941  46.207 1.00 24.25  ? 1044 PRO B CG    1 
ATOM   1867  C  CD    . PRO A  1  245 ? 25.394  33.427  44.965 1.00 24.52  ? 1044 PRO B CD    1 
ATOM   1868  N  N     . VAL A  1  246 ? 21.960  33.465  43.145 1.00 28.71  ? 1045 VAL B N     1 
ATOM   1869  C  CA    . VAL A  1  246 ? 20.705  33.675  42.403 1.00 29.55  ? 1045 VAL B CA    1 
ATOM   1870  C  C     . VAL A  1  246 ? 20.707  32.899  41.068 1.00 29.97  ? 1045 VAL B C     1 
ATOM   1871  O  O     . VAL A  1  246 ? 19.708  32.302  40.687 1.00 27.37  ? 1045 VAL B O     1 
ATOM   1872  C  CB    . VAL A  1  246 ? 20.344  35.173  42.188 1.00 28.33  ? 1045 VAL B CB    1 
ATOM   1873  C  CG1   . VAL A  1  246 ? 21.348  35.872  41.282 1.00 27.47  ? 1045 VAL B CG1   1 
ATOM   1874  C  CG2   . VAL A  1  246 ? 18.914  35.261  41.626 1.00 29.86  ? 1045 VAL B CG2   1 
ATOM   1875  N  N     . HIS A  1  247 ? 21.839  32.891  40.364 1.00 31.08  ? 1046 HIS B N     1 
ATOM   1876  C  CA    . HIS A  1  247 ? 21.903  32.149  39.092 1.00 29.75  ? 1046 HIS B CA    1 
ATOM   1877  C  C     . HIS A  1  247 ? 21.799  30.639  39.316 1.00 29.61  ? 1046 HIS B C     1 
ATOM   1878  O  O     . HIS A  1  247 ? 21.141  29.944  38.559 1.00 29.19  ? 1046 HIS B O     1 
ATOM   1879  C  CB    . HIS A  1  247 ? 23.161  32.469  38.344 1.00 31.91  ? 1046 HIS B CB    1 
ATOM   1880  C  CG    . HIS A  1  247 ? 23.309  33.922  38.047 1.00 38.94  ? 1046 HIS B CG    1 
ATOM   1881  N  ND1   . HIS A  1  247 ? 24.089  34.748  38.815 1.00 40.46  ? 1046 HIS B ND1   1 
ATOM   1882  C  CD2   . HIS A  1  247 ? 22.738  34.714  37.108 1.00 40.61  ? 1046 HIS B CD2   1 
ATOM   1883  C  CE1   . HIS A  1  247 ? 24.007  35.982  38.366 1.00 43.34  ? 1046 HIS B CE1   1 
ATOM   1884  N  NE2   . HIS A  1  247 ? 23.199  35.990  37.326 1.00 40.05  ? 1046 HIS B NE2   1 
ATOM   1885  N  N     . ARG A  1  248 ? 22.392  30.154  40.390 1.00 30.35  ? 1047 ARG B N     1 
ATOM   1886  C  CA    . ARG A  1  248 ? 22.363  28.740  40.689 1.00 31.56  ? 1047 ARG B CA    1 
ATOM   1887  C  C     . ARG A  1  248 ? 20.958  28.295  41.010 1.00 30.61  ? 1047 ARG B C     1 
ATOM   1888  O  O     . ARG A  1  248 ? 20.530  27.256  40.580 1.00 31.72  ? 1047 ARG B O     1 
ATOM   1889  C  CB    . ARG A  1  248 ? 23.249  28.428  41.855 1.00 25.65  ? 1047 ARG B CB    1 
ATOM   1890  C  CG    . ARG A  1  248 ? 23.667  26.958  41.870 1.00 26.14  ? 1047 ARG B CG    1 
ATOM   1891  C  CD    . ARG A  1  248 ? 24.577  26.664  43.030 1.00 25.68  ? 1047 ARG B CD    1 
ATOM   1892  N  NE    . ARG A  1  248 ? 25.917  27.169  42.793 1.00 27.76  ? 1047 ARG B NE    1 
ATOM   1893  C  CZ    . ARG A  1  248 ? 26.434  28.246  43.382 1.00 30.29  ? 1047 ARG B CZ    1 
ATOM   1894  N  NH1   . ARG A  1  248 ? 25.735  28.918  44.288 1.00 33.50  ? 1047 ARG B NH1   1 
ATOM   1895  N  NH2   . ARG A  1  248 ? 27.681  28.611  43.139 1.00 28.51  ? 1047 ARG B NH2   1 
ATOM   1896  N  N     . ARG A  1  249 ? 20.264  29.101  41.796 1.00 34.12  ? 1048 ARG B N     1 
ATOM   1897  C  CA    . ARG A  1  249 ? 18.902  28.820  42.179 1.00 30.91  ? 1048 ARG B CA    1 
ATOM   1898  C  C     . ARG A  1  249 ? 17.943  28.872  40.981 1.00 29.81  ? 1048 ARG B C     1 
ATOM   1899  O  O     . ARG A  1  249 ? 17.042  28.048  40.902 1.00 30.61  ? 1048 ARG B O     1 
ATOM   1900  C  CB    . ARG A  1  249 ? 18.488  29.758  43.281 1.00 26.51  ? 1048 ARG B CB    1 
ATOM   1901  C  CG    . ARG A  1  249 ? 19.239  29.483  44.555 1.00 29.61  ? 1048 ARG B CG    1 
ATOM   1902  C  CD    . ARG A  1  249 ? 19.014  30.581  45.584 1.00 28.88  ? 1048 ARG B CD    1 
ATOM   1903  N  NE    . ARG A  1  249 ? 19.561  30.163  46.876 1.00 30.41  ? 1048 ARG B NE    1 
ATOM   1904  C  CZ    . ARG A  1  249 ? 19.930  30.991  47.845 1.00 31.06  ? 1048 ARG B CZ    1 
ATOM   1905  N  NH1   . ARG A  1  249 ? 19.792  32.309  47.711 1.00 30.02  ? 1048 ARG B NH1   1 
ATOM   1906  N  NH2   . ARG A  1  249 ? 20.441  30.505  48.950 1.00 31.88  ? 1048 ARG B NH2   1 
ATOM   1907  N  N     . ILE A  1  250 ? 18.150  29.812  40.065 1.00 27.83  ? 1049 ILE B N     1 
ATOM   1908  C  CA    . ILE A  1  250 ? 17.367  29.862  38.843 1.00 28.10  ? 1049 ILE B CA    1 
ATOM   1909  C  C     . ILE A  1  250 ? 17.551  28.589  38.014 1.00 31.41  ? 1049 ILE B C     1 
ATOM   1910  O  O     . ILE A  1  250 ? 16.582  28.002  37.571 1.00 30.09  ? 1049 ILE B O     1 
ATOM   1911  C  CB    . ILE A  1  250 ? 17.725  31.047  37.952 1.00 24.36  ? 1049 ILE B CB    1 
ATOM   1912  C  CG1   . ILE A  1  250 ? 17.131  32.337  38.510 1.00 25.57  ? 1049 ILE B CG1   1 
ATOM   1913  C  CG2   . ILE A  1  250 ? 17.160  30.891  36.560 1.00 22.15  ? 1049 ILE B CG2   1 
ATOM   1914  C  CD1   . ILE A  1  250 ? 17.906  33.591  38.033 1.00 20.89  ? 1049 ILE B CD1   1 
ATOM   1915  N  N     . LEU A  1  251 ? 18.795  28.169  37.797 1.00 30.69  ? 1050 LEU B N     1 
ATOM   1916  C  CA    . LEU A  1  251 ? 19.040  26.997  37.017 1.00 29.55  ? 1050 LEU B CA    1 
ATOM   1917  C  C     . LEU A  1  251 ? 18.533  25.727  37.675 1.00 31.88  ? 1050 LEU B C     1 
ATOM   1918  O  O     . LEU A  1  251 ? 18.052  24.834  36.984 1.00 31.66  ? 1050 LEU B O     1 
ATOM   1919  C  CB    . LEU A  1  251 ? 20.520  26.884  36.658 1.00 31.96  ? 1050 LEU B CB    1 
ATOM   1920  C  CG    . LEU A  1  251 ? 21.082  28.030  35.820 1.00 35.78  ? 1050 LEU B CG    1 
ATOM   1921  C  CD1   . LEU A  1  251 ? 22.551  27.728  35.587 1.00 40.00  ? 1050 LEU B CD1   1 
ATOM   1922  C  CD2   . LEU A  1  251 ? 20.322  28.261  34.514 1.00 35.69  ? 1050 LEU B CD2   1 
ATOM   1923  N  N     . TYR A  1  252 ? 18.691  25.624  38.997 1.00 32.62  ? 1051 TYR B N     1 
ATOM   1924  C  CA    . TYR A  1  252 ? 18.237  24.479  39.730 1.00 35.78  ? 1051 TYR B CA    1 
ATOM   1925  C  C     . TYR A  1  252 ? 16.720  24.486  39.688 1.00 35.84  ? 1051 TYR B C     1 
ATOM   1926  O  O     . TYR A  1  252 ? 16.105  23.439  39.551 1.00 39.67  ? 1051 TYR B O     1 
ATOM   1927  C  CB    . TYR A  1  252 ? 18.760  24.506  41.170 1.00 34.50  ? 1051 TYR B CB    1 
ATOM   1928  C  CG    . TYR A  1  252 ? 18.323  23.321  41.974 1.00 35.61  ? 1051 TYR B CG    1 
ATOM   1929  C  CD1   . TYR A  1  252 ? 18.698  22.027  41.610 1.00 35.71  ? 1051 TYR B CD1   1 
ATOM   1930  C  CD2   . TYR A  1  252 ? 17.514  23.493  43.121 1.00 38.95  ? 1051 TYR B CD2   1 
ATOM   1931  C  CE1   . TYR A  1  252 ? 18.296  20.934  42.371 1.00 37.14  ? 1051 TYR B CE1   1 
ATOM   1932  C  CE2   . TYR A  1  252 ? 17.107  22.408  43.893 1.00 39.21  ? 1051 TYR B CE2   1 
ATOM   1933  C  CZ    . TYR A  1  252 ? 17.513  21.140  43.512 1.00 39.95  ? 1051 TYR B CZ    1 
ATOM   1934  O  OH    . TYR A  1  252 ? 17.115  20.087  44.265 1.00 43.58  ? 1051 TYR B OH    1 
ATOM   1935  N  N     . GLY A  1  253 ? 16.147  25.688  39.756 1.00 34.34  ? 1052 GLY B N     1 
ATOM   1936  C  CA    . GLY A  1  253 ? 14.687  25.853  39.633 1.00 35.27  ? 1052 GLY B CA    1 
ATOM   1937  C  C     . GLY A  1  253 ? 14.157  25.351  38.298 1.00 37.65  ? 1052 GLY B C     1 
ATOM   1938  O  O     . GLY A  1  253 ? 13.169  24.671  38.252 1.00 35.39  ? 1052 GLY B O     1 
ATOM   1939  N  N     . LEU A  1  254 ? 14.878  25.622  37.227 1.00 34.92  ? 1053 LEU B N     1 
ATOM   1940  C  CA    . LEU A  1  254 ? 14.494  25.127  35.928 1.00 39.92  ? 1053 LEU B CA    1 
ATOM   1941  C  C     . LEU A  1  254 ? 14.625  23.603  35.817 1.00 39.32  ? 1053 LEU B C     1 
ATOM   1942  O  O     . LEU A  1  254 ? 13.791  22.962  35.186 1.00 42.22  ? 1053 LEU B O     1 
ATOM   1943  C  CB    . LEU A  1  254 ? 15.333  25.787  34.830 1.00 33.04  ? 1053 LEU B CB    1 
ATOM   1944  C  CG    . LEU A  1  254 ? 15.193  27.278  34.638 1.00 32.07  ? 1053 LEU B CG    1 
ATOM   1945  C  CD1   . LEU A  1  254 ? 16.333  27.767  33.787 1.00 29.17  ? 1053 LEU B CD1   1 
ATOM   1946  C  CD2   . LEU A  1  254 ? 13.842  27.554  33.974 1.00 29.66  ? 1053 LEU B CD2   1 
ATOM   1947  N  N     . ASN A  1  255 ? 15.661  23.038  36.437 1.00 39.32  ? 1054 ASN B N     1 
ATOM   1948  C  CA    . ASN A  1  255 ? 15.871  21.611  36.354 1.00 40.49  ? 1054 ASN B CA    1 
ATOM   1949  C  C     . ASN A  1  255 ? 14.794  20.882  37.135 1.00 45.85  ? 1054 ASN B C     1 
ATOM   1950  O  O     . ASN A  1  255 ? 14.295  19.880  36.681 1.00 48.49  ? 1054 ASN B O     1 
ATOM   1951  C  CB    . ASN A  1  255 ? 17.229  21.280  36.894 1.00 34.59  ? 1054 ASN B CB    1 
ATOM   1952  C  CG    . ASN A  1  255 ? 17.669  19.879  36.530 1.00 33.55  ? 1054 ASN B CG    1 
ATOM   1953  O  OD1   . ASN A  1  255 ? 17.891  19.091  37.407 1.00 34.91  ? 1054 ASN B OD1   1 
ATOM   1954  N  ND2   . ASN A  1  255 ? 17.814  19.574  35.249 1.00 29.83  ? 1054 ASN B ND2   1 
ATOM   1955  N  N     . GLU A  1  256 ? 14.473  21.418  38.312 1.00 51.89  ? 1055 GLU B N     1 
ATOM   1956  C  CA    . GLU A  1  256 ? 13.483  20.859  39.198 1.00 53.91  ? 1055 GLU B CA    1 
ATOM   1957  C  C     . GLU A  1  256 ? 12.085  20.942  38.538 1.00 51.67  ? 1055 GLU B C     1 
ATOM   1958  O  O     . GLU A  1  256 ? 11.338  20.038  38.488 1.00 53.40  ? 1055 GLU B O     1 
ATOM   1959  C  CB    . GLU A  1  256 ? 13.586  21.541  40.568 1.00 59.95  ? 1055 GLU B CB    1 
ATOM   1960  C  CG    . GLU A  1  256 ? 13.518  20.587  41.743 1.00 66.87  ? 1055 GLU B CG    1 
ATOM   1961  C  CD    . GLU A  1  256 ? 14.596  19.510  41.713 1.00 76.77  ? 1055 GLU B CD    1 
ATOM   1962  O  OE1   . GLU A  1  256 ? 14.500  18.583  42.545 1.00 83.21  ? 1055 GLU B OE1   1 
ATOM   1963  O  OE2   . GLU A  1  256 ? 15.520  19.573  40.851 1.00 80.32  ? 1055 GLU B OE2   1 
ATOM   1964  N  N     A GLN A  1  257 ? 11.787  22.038  37.914 0.70 53.03  ? 1056 GLN B N     1 
ATOM   1965  N  N     B GLN A  1  257 ? 11.755  22.003  37.871 0.30 52.10  ? 1056 GLN B N     1 
ATOM   1966  C  CA    A GLN A  1  257 ? 10.488  22.103  37.315 0.70 57.66  ? 1056 GLN B CA    1 
ATOM   1967  C  CA    B GLN A  1  257 ? 10.424  21.971  37.325 0.30 53.58  ? 1056 GLN B CA    1 
ATOM   1968  C  C     A GLN A  1  257 ? 10.404  21.291  36.008 0.70 60.12  ? 1056 GLN B C     1 
ATOM   1969  C  C     B GLN A  1  257 ? 10.390  21.265  35.984 0.30 55.63  ? 1056 GLN B C     1 
ATOM   1970  O  O     A GLN A  1  257 ? 9.378   21.294  35.348 0.70 56.34  ? 1056 GLN B O     1 
ATOM   1971  O  O     B GLN A  1  257 ? 9.406   21.319  35.271 0.30 53.80  ? 1056 GLN B O     1 
ATOM   1972  C  CB    A GLN A  1  257 ? 10.220  23.530  37.025 0.70 59.85  ? 1056 GLN B CB    1 
ATOM   1973  C  CB    B GLN A  1  257 ? 9.972   23.361  37.194 0.30 52.66  ? 1056 GLN B CB    1 
ATOM   1974  C  CG    A GLN A  1  257 ? 10.112  24.459  38.241 0.70 62.36  ? 1056 GLN B CG    1 
ATOM   1975  C  CG    B GLN A  1  257 ? 9.605   23.974  38.520 0.30 51.52  ? 1056 GLN B CG    1 
ATOM   1976  C  CD    A GLN A  1  257 ? 10.171  25.943  37.841 0.70 63.19  ? 1056 GLN B CD    1 
ATOM   1977  C  CD    B GLN A  1  257 ? 8.455   23.246  39.158 0.30 51.88  ? 1056 GLN B CD    1 
ATOM   1978  O  OE1   A GLN A  1  257 ? 9.538   26.373  36.876 0.70 71.33  ? 1056 GLN B OE1   1 
ATOM   1979  O  OE1   B GLN A  1  257 ? 8.212   22.071  38.882 0.30 50.07  ? 1056 GLN B OE1   1 
ATOM   1980  N  NE2   A GLN A  1  257 ? 10.881  26.725  38.588 0.70 61.93  ? 1056 GLN B NE2   1 
ATOM   1981  N  NE2   B GLN A  1  257 ? 7.763   23.933  40.066 0.30 51.39  ? 1056 GLN B NE2   1 
ATOM   1982  N  N     . GLY A  1  258 ? 11.494  20.604  35.660 1.00 55.92  ? 1057 GLY B N     1 
ATOM   1983  C  CA    . GLY A  1  258 ? 11.607  19.863  34.424 1.00 58.22  ? 1057 GLY B CA    1 
ATOM   1984  C  C     . GLY A  1  258 ? 11.602  20.700  33.146 1.00 59.05  ? 1057 GLY B C     1 
ATOM   1985  O  O     . GLY A  1  258 ? 11.225  20.216  32.076 1.00 55.69  ? 1057 GLY B O     1 
ATOM   1986  N  N     A MET A  1  259 ? 12.064  21.944  33.259 0.50 59.58  ? 1058 MET B N     1 
ATOM   1987  N  N     B MET A  1  259 ? 12.013  21.961  33.230 0.50 63.11  ? 1058 MET B N     1 
ATOM   1988  C  CA    A MET A  1  259 ? 12.092  22.876  32.130 0.50 59.24  ? 1058 MET B CA    1 
ATOM   1989  C  CA    B MET A  1  259 ? 12.002  22.826  32.047 0.50 64.87  ? 1058 MET B CA    1 
ATOM   1990  C  C     A MET A  1  259 ? 13.301  22.635  31.212 0.50 61.17  ? 1058 MET B C     1 
ATOM   1991  C  C     B MET A  1  259 ? 13.248  22.632  31.185 0.50 64.85  ? 1058 MET B C     1 
ATOM   1992  O  O     A MET A  1  259 ? 14.157  23.526  31.035 0.50 55.83  ? 1058 MET B O     1 
ATOM   1993  O  O     B MET A  1  259 ? 14.033  23.564  30.949 0.50 60.48  ? 1058 MET B O     1 
ATOM   1994  C  CB    A MET A  1  259 ? 12.077  24.310  32.652 0.50 55.75  ? 1058 MET B CB    1 
ATOM   1995  C  CB    B MET A  1  259 ? 11.800  24.281  32.439 0.50 65.05  ? 1058 MET B CB    1 
ATOM   1996  C  CG    A MET A  1  259 ? 10.769  24.693  33.350 0.50 55.31  ? 1058 MET B CG    1 
ATOM   1997  C  CG    B MET A  1  259 ? 10.458  24.552  33.108 0.50 66.90  ? 1058 MET B CG    1 
ATOM   1998  S  SD    A MET A  1  259 ? 9.468   24.786  32.098 0.50 51.92  ? 1058 MET B SD    1 
ATOM   1999  S  SD    B MET A  1  259 ? 10.559  26.013  34.166 0.50 75.68  ? 1058 MET B SD    1 
ATOM   2000  C  CE    A MET A  1  259 ? 8.959   23.091  31.823 0.50 51.37  ? 1058 MET B CE    1 
ATOM   2001  C  CE    B MET A  1  259 ? 9.006   25.926  35.072 0.50 69.71  ? 1058 MET B CE    1 
ATOM   2002  N  N     . THR A  1  260 ? 13.389  21.428  30.659 1.00 59.76  ? 1059 THR B N     1 
ATOM   2003  C  CA    . THR A  1  260 ? 14.505  21.071  29.792 1.00 54.46  ? 1059 THR B CA    1 
ATOM   2004  C  C     . THR A  1  260 ? 14.290  21.551  28.360 1.00 56.30  ? 1059 THR B C     1 
ATOM   2005  O  O     . THR A  1  260 ? 13.173  21.947  28.004 1.00 59.97  ? 1059 THR B O     1 
ATOM   2006  C  CB    . THR A  1  260 ? 14.770  19.551  29.834 1.00 58.41  ? 1059 THR B CB    1 
ATOM   2007  O  OG1   . THR A  1  260 ? 13.618  18.852  29.357 1.00 55.99  ? 1059 THR B OG1   1 
ATOM   2008  C  CG2   . THR A  1  260 ? 15.136  19.103  31.230 1.00 51.49  ? 1059 THR B CG2   1 
ATOM   2009  N  N     . PRO A  1  261 ? 15.333  21.510  27.535 1.00 51.77  ? 1060 PRO B N     1 
ATOM   2010  C  CA    . PRO A  1  261 ? 15.237  22.002  26.133 1.00 56.77  ? 1060 PRO B CA    1 
ATOM   2011  C  C     . PRO A  1  261 ? 14.211  21.265  25.248 1.00 59.22  ? 1060 PRO B C     1 
ATOM   2012  O  O     . PRO A  1  261 ? 13.716  21.851  24.304 1.00 57.66  ? 1060 PRO B O     1 
ATOM   2013  C  CB    . PRO A  1  261 ? 16.658  21.777  25.571 1.00 48.70  ? 1060 PRO B CB    1 
ATOM   2014  C  CG    . PRO A  1  261 ? 17.531  21.651  26.793 1.00 52.41  ? 1060 PRO B CG    1 
ATOM   2015  C  CD    . PRO A  1  261 ? 16.667  20.979  27.833 1.00 46.70  ? 1060 PRO B CD    1 
ATOM   2016  N  N     . ASP A  1  262 ? 13.937  19.993  25.545 1.00 64.93  ? 1061 ASP B N     1 
ATOM   2017  C  CA    . ASP A  1  262 ? 12.903  19.208  24.845 1.00 64.30  ? 1061 ASP B CA    1 
ATOM   2018  C  C     . ASP A  1  262 ? 11.464  19.638  25.214 1.00 59.36  ? 1061 ASP B C     1 
ATOM   2019  O  O     . ASP A  1  262 ? 10.582  19.538  24.370 1.00 57.61  ? 1061 ASP B O     1 
ATOM   2020  C  CB    . ASP A  1  262 ? 13.107  17.703  25.108 1.00 61.89  ? 1061 ASP B CB    1 
ATOM   2021  C  CG    . ASP A  1  262 ? 13.099  17.375  26.591 1.00 64.76  ? 1061 ASP B CG    1 
ATOM   2022  O  OD1   . ASP A  1  262 ? 13.418  18.262  27.390 1.00 72.55  ? 1061 ASP B OD1   1 
ATOM   2023  O  OD2   . ASP A  1  262 ? 12.771  16.246  26.968 1.00 75.01  ? 1061 ASP B OD2   1 
ATOM   2024  N  N     . LYS A  1  263 ? 11.264  20.096  26.457 1.00 59.23  ? 1062 LYS B N     1 
ATOM   2025  C  CA    . LYS A  1  263 ? 9.962   20.552  26.968 1.00 54.87  ? 1062 LYS B CA    1 
ATOM   2026  C  C     . LYS A  1  263 ? 9.662   21.939  26.452 1.00 53.00  ? 1062 LYS B C     1 
ATOM   2027  O  O     . LYS A  1  263 ? 10.564  22.628  25.943 1.00 52.49  ? 1062 LYS B O     1 
ATOM   2028  C  CB    . LYS A  1  263 ? 9.924   20.512  28.504 1.00 59.90  ? 1062 LYS B CB    1 
ATOM   2029  C  CG    . LYS A  1  263 ? 10.108  19.110  29.096 1.00 55.88  ? 1062 LYS B CG    1 
ATOM   2030  C  CD    . LYS A  1  263 ? 9.286   18.061  28.364 1.00 56.84  ? 1062 LYS B CD    1 
ATOM   2031  N  N     . SER A  1  264 ? 8.399   22.353  26.506 1.00 50.74  ? 1063 SER B N     1 
ATOM   2032  C  CA    . SER A  1  264 ? 8.060   23.680  25.977 1.00 53.78  ? 1063 SER B CA    1 
ATOM   2033  C  C     . SER A  1  264 ? 8.460   24.785  26.973 1.00 49.39  ? 1063 SER B C     1 
ATOM   2034  O  O     . SER A  1  264 ? 8.719   24.525  28.139 1.00 44.26  ? 1063 SER B O     1 
ATOM   2035  C  CB    . SER A  1  264 ? 6.579   23.791  25.565 1.00 55.01  ? 1063 SER B CB    1 
ATOM   2036  O  OG    . SER A  1  264 ? 5.750   23.658  26.691 1.00 64.51  ? 1063 SER B OG    1 
ATOM   2037  N  N     . TYR A  1  265 ? 8.452   26.012  26.488 1.00 44.07  ? 1064 TYR B N     1 
ATOM   2038  C  CA    . TYR A  1  265 ? 8.795   27.164  27.291 1.00 47.48  ? 1064 TYR B CA    1 
ATOM   2039  C  C     . TYR A  1  265 ? 7.810   27.336  28.440 1.00 52.17  ? 1064 TYR B C     1 
ATOM   2040  O  O     . TYR A  1  265 ? 6.624   27.122  28.263 1.00 53.06  ? 1064 TYR B O     1 
ATOM   2041  C  CB    . TYR A  1  265 ? 8.798   28.418  26.448 1.00 40.20  ? 1064 TYR B CB    1 
ATOM   2042  C  CG    . TYR A  1  265 ? 9.907   28.500  25.452 1.00 42.17  ? 1064 TYR B CG    1 
ATOM   2043  C  CD1   . TYR A  1  265 ? 11.141  29.024  25.809 1.00 35.90  ? 1064 TYR B CD1   1 
ATOM   2044  C  CD2   . TYR A  1  265 ? 9.707   28.098  24.113 1.00 38.26  ? 1064 TYR B CD2   1 
ATOM   2045  C  CE1   . TYR A  1  265 ? 12.166  29.132  24.886 1.00 40.79  ? 1064 TYR B CE1   1 
ATOM   2046  C  CE2   . TYR A  1  265 ? 10.720  28.196  23.198 1.00 39.12  ? 1064 TYR B CE2   1 
ATOM   2047  C  CZ    . TYR A  1  265 ? 11.950  28.717  23.591 1.00 43.08  ? 1064 TYR B CZ    1 
ATOM   2048  O  OH    . TYR A  1  265 ? 12.961  28.865  22.676 1.00 43.20  ? 1064 TYR B OH    1 
ATOM   2049  N  N     . LYS A  1  266 ? 8.334   27.712  29.613 1.00 52.84  ? 1065 LYS B N     1 
ATOM   2050  C  CA    . LYS A  1  266 ? 7.527   27.975  30.784 1.00 43.79  ? 1065 LYS B CA    1 
ATOM   2051  C  C     . LYS A  1  266 ? 7.466   29.496  30.946 1.00 45.37  ? 1065 LYS B C     1 
ATOM   2052  O  O     . LYS A  1  266 ? 8.454   30.199  30.675 1.00 40.03  ? 1065 LYS B O     1 
ATOM   2053  C  CB    . LYS A  1  266 ? 8.110   27.310  31.986 1.00 41.37  ? 1065 LYS B CB    1 
ATOM   2054  N  N     . LYS A  1  267 ? 6.316   30.011  31.378 1.00 43.78  ? 1066 LYS B N     1 
ATOM   2055  C  CA    . LYS A  1  267 ? 6.203   31.451  31.575 1.00 43.56  ? 1066 LYS B CA    1 
ATOM   2056  C  C     . LYS A  1  267 ? 7.152   31.936  32.659 1.00 38.39  ? 1066 LYS B C     1 
ATOM   2057  O  O     . LYS A  1  267 ? 7.324   31.268  33.683 1.00 38.18  ? 1066 LYS B O     1 
ATOM   2058  C  CB    . LYS A  1  267 ? 4.772   31.854  31.904 1.00 45.99  ? 1066 LYS B CB    1 
ATOM   2059  C  CG    . LYS A  1  267 ? 4.488   33.282  31.463 1.00 53.66  ? 1066 LYS B CG    1 
ATOM   2060  C  CD    . LYS A  1  267 ? 4.110   34.131  32.650 1.00 51.79  ? 1066 LYS B CD    1 
ATOM   2061  C  CE    . LYS A  1  267 ? 2.587   34.021  32.899 1.00 56.70  ? 1066 LYS B CE    1 
ATOM   2062  N  NZ    . LYS A  1  267 ? 1.778   34.173  31.644 1.00 50.49  ? 1066 LYS B NZ    1 
ATOM   2063  N  N     . SER A  1  268 ? 7.773   33.084  32.413 1.00 34.38  ? 1067 SER B N     1 
ATOM   2064  C  CA    . SER A  1  268 ? 8.759   33.636  33.353 1.00 35.81  ? 1067 SER B CA    1 
ATOM   2065  C  C     . SER A  1  268 ? 8.219   33.961  34.742 1.00 34.74  ? 1067 SER B C     1 
ATOM   2066  O  O     . SER A  1  268 ? 8.913   33.714  35.727 1.00 31.05  ? 1067 SER B O     1 
ATOM   2067  C  CB    . SER A  1  268 ? 9.436   34.870  32.778 1.00 35.96  ? 1067 SER B CB    1 
ATOM   2068  O  OG    . SER A  1  268 ? 10.157  34.565  31.603 1.00 37.08  ? 1067 SER B OG    1 
ATOM   2069  N  N     . ALA A  1  269 ? 6.985   34.478  34.818 1.00 35.18  ? 1068 ALA B N     1 
ATOM   2070  C  CA    . ALA A  1  269 ? 6.390   34.822  36.090 1.00 34.41  ? 1068 ALA B CA    1 
ATOM   2071  C  C     . ALA A  1  269 ? 6.284   33.597  36.982 1.00 34.62  ? 1068 ALA B C     1 
ATOM   2072  O  O     . ALA A  1  269 ? 6.560   33.658  38.190 1.00 38.50  ? 1068 ALA B O     1 
ATOM   2073  C  CB    . ALA A  1  269 ? 5.021   35.485  35.907 1.00 35.72  ? 1068 ALA B CB    1 
ATOM   2074  N  N     . ARG A  1  270 ? 5.932   32.470  36.381 1.00 33.53  ? 1069 ARG B N     1 
ATOM   2075  C  CA    . ARG A  1  270 ? 5.784   31.252  37.132 1.00 36.56  ? 1069 ARG B CA    1 
ATOM   2076  C  C     . ARG A  1  270 ? 7.139   30.702  37.582 1.00 33.96  ? 1069 ARG B C     1 
ATOM   2077  O  O     . ARG A  1  270 ? 7.258   30.173  38.682 1.00 32.46  ? 1069 ARG B O     1 
ATOM   2078  C  CB    . ARG A  1  270 ? 4.986   30.238  36.308 1.00 38.80  ? 1069 ARG B CB    1 
ATOM   2079  C  CG    . ARG A  1  270 ? 4.760   28.949  37.046 1.00 44.59  ? 1069 ARG B CG    1 
ATOM   2080  C  CD    . ARG A  1  270 ? 3.702   28.077  36.400 1.00 49.63  ? 1069 ARG B CD    1 
ATOM   2081  N  NE    . ARG A  1  270 ? 3.675   26.806  37.122 1.00 50.08  ? 1069 ARG B NE    1 
ATOM   2082  C  CZ    . ARG A  1  270 ? 3.317   25.650  36.573 1.00 56.92  ? 1069 ARG B CZ    1 
ATOM   2083  N  NH1   . ARG A  1  270 ? 2.939   25.603  35.299 1.00 58.06  ? 1069 ARG B NH1   1 
ATOM   2084  N  NH2   . ARG A  1  270 ? 3.327   24.544  37.302 1.00 70.68  ? 1069 ARG B NH2   1 
ATOM   2085  N  N     . ILE A  1  271 ? 8.152   30.810  36.730 1.00 34.12  ? 1070 ILE B N     1 
ATOM   2086  C  CA    . ILE A  1  271 ? 9.512   30.343  37.059 1.00 29.99  ? 1070 ILE B CA    1 
ATOM   2087  C  C     . ILE A  1  271 ? 10.039  31.181  38.222 1.00 32.39  ? 1070 ILE B C     1 
ATOM   2088  O  O     . ILE A  1  271 ? 10.576  30.670  39.190 1.00 31.45  ? 1070 ILE B O     1 
ATOM   2089  C  CB    . ILE A  1  271 ? 10.462  30.548  35.862 1.00 35.25  ? 1070 ILE B CB    1 
ATOM   2090  C  CG1   . ILE A  1  271 ? 10.024  29.679  34.666 1.00 32.58  ? 1070 ILE B CG1   1 
ATOM   2091  C  CG2   . ILE A  1  271 ? 11.919  30.305  36.272 1.00 32.03  ? 1070 ILE B CG2   1 
ATOM   2092  C  CD1   . ILE A  1  271 ? 10.826  29.939  33.428 1.00 29.87  ? 1070 ILE B CD1   1 
ATOM   2093  N  N     . VAL A  1  272 ? 9.833   32.487  38.128 1.00 32.58  ? 1071 VAL B N     1 
ATOM   2094  C  CA    . VAL A  1  272 ? 10.326  33.381  39.128 1.00 33.01  ? 1071 VAL B CA    1 
ATOM   2095  C  C     . VAL A  1  272 ? 9.634   33.217  40.479 1.00 37.27  ? 1071 VAL B C     1 
ATOM   2096  O  O     . VAL A  1  272 ? 10.290  33.315  41.489 1.00 36.84  ? 1071 VAL B O     1 
ATOM   2097  C  CB    . VAL A  1  272 ? 10.202  34.849  38.651 1.00 34.56  ? 1071 VAL B CB    1 
ATOM   2098  C  CG1   . VAL A  1  272 ? 10.442  35.806  39.797 1.00 27.11  ? 1071 VAL B CG1   1 
ATOM   2099  C  CG2   . VAL A  1  272 ? 11.125  35.108  37.459 1.00 28.48  ? 1071 VAL B CG2   1 
ATOM   2100  N  N     . GLY A  1  273 ? 8.315   32.987  40.495 1.00 35.04  ? 1072 GLY B N     1 
ATOM   2101  C  CA    . GLY A  1  273 ? 7.615   32.842  41.750 1.00 32.19  ? 1072 GLY B CA    1 
ATOM   2102  C  C     . GLY A  1  273 ? 8.050   31.559  42.427 1.00 31.28  ? 1072 GLY B C     1 
ATOM   2103  O  O     . GLY A  1  273 ? 8.162   31.501  43.658 1.00 28.42  ? 1072 GLY B O     1 
ATOM   2104  N  N     . ASP A  1  274 ? 8.270   30.531  41.622 1.00 31.24  ? 1073 ASP B N     1 
ATOM   2105  C  CA    . ASP A  1  274 ? 8.807   29.284  42.116 1.00 36.25  ? 1073 ASP B CA    1 
ATOM   2106  C  C     . ASP A  1  274 ? 10.180  29.395  42.729 1.00 33.01  ? 1073 ASP B C     1 
ATOM   2107  O  O     . ASP A  1  274 ? 10.394  28.847  43.802 1.00 34.47  ? 1073 ASP B O     1 
ATOM   2108  C  CB    . ASP A  1  274 ? 8.853   28.298  40.972 1.00 44.08  ? 1073 ASP B CB    1 
ATOM   2109  C  CG    . ASP A  1  274 ? 9.088   26.895  41.443 1.00 63.78  ? 1073 ASP B CG    1 
ATOM   2110  O  OD1   . ASP A  1  274 ? 8.079   26.270  41.848 1.00 79.91  ? 1073 ASP B OD1   1 
ATOM   2111  O  OD2   . ASP A  1  274 ? 10.272  26.417  41.400 1.00 66.85  ? 1073 ASP B OD2   1 
ATOM   2112  N  N     . VAL A  1  275 ? 11.101  30.107  42.075 1.00 31.09  ? 1074 VAL B N     1 
ATOM   2113  C  CA    . VAL A  1  275 ? 12.437  30.295  42.632 1.00 30.63  ? 1074 VAL B CA    1 
ATOM   2114  C  C     . VAL A  1  275 ? 12.353  31.130  43.898 1.00 31.57  ? 1074 VAL B C     1 
ATOM   2115  O  O     . VAL A  1  275 ? 13.094  30.890  44.871 1.00 33.32  ? 1074 VAL B O     1 
ATOM   2116  C  CB    . VAL A  1  275 ? 13.348  31.000  41.606 1.00 31.86  ? 1074 VAL B CB    1 
ATOM   2117  C  CG1   . VAL A  1  275 ? 14.644  31.438  42.249 1.00 29.59  ? 1074 VAL B CG1   1 
ATOM   2118  C  CG2   . VAL A  1  275 ? 13.652  30.057  40.462 1.00 32.68  ? 1074 VAL B CG2   1 
ATOM   2119  N  N     A MET A  1  276 ? 11.483  32.140  43.915 0.50 31.01  ? 1075 MET B N     1 
ATOM   2120  N  N     B MET A  1  276 ? 11.399  32.063  43.855 0.50 34.10  ? 1075 MET B N     1 
ATOM   2121  C  CA    A MET A  1  276 ? 11.291  32.990  45.087 0.50 32.53  ? 1075 MET B CA    1 
ATOM   2122  C  CA    B MET A  1  276 ? 11.152  33.008  44.922 0.50 37.64  ? 1075 MET B CA    1 
ATOM   2123  C  C     A MET A  1  276 ? 10.782  32.219  46.309 0.50 35.41  ? 1075 MET B C     1 
ATOM   2124  C  C     B MET A  1  276 ? 10.690  32.340  46.229 0.50 40.47  ? 1075 MET B C     1 
ATOM   2125  O  O     A MET A  1  276 ? 11.315  32.377  47.419 0.50 37.93  ? 1075 MET B O     1 
ATOM   2126  O  O     B MET A  1  276 ? 11.228  32.642  47.297 0.50 46.98  ? 1075 MET B O     1 
ATOM   2127  C  CB    A MET A  1  276 ? 10.315  34.131  44.780 0.50 30.33  ? 1075 MET B CB    1 
ATOM   2128  C  CB    B MET A  1  276 ? 10.158  34.092  44.469 0.50 38.12  ? 1075 MET B CB    1 
ATOM   2129  C  CG    A MET A  1  276 ? 10.776  35.139  43.760 0.50 29.20  ? 1075 MET B CG    1 
ATOM   2130  C  CG    B MET A  1  276 ? 10.233  35.385  45.307 0.50 42.05  ? 1075 MET B CG    1 
ATOM   2131  S  SD    A MET A  1  276 ? 9.542   36.412  43.410 0.50 32.66  ? 1075 MET B SD    1 
ATOM   2132  S  SD    B MET A  1  276 ? 9.296   36.777  44.597 0.50 50.00  ? 1075 MET B SD    1 
ATOM   2133  C  CE    A MET A  1  276 ? 9.370   37.011  45.101 0.50 29.65  ? 1075 MET B CE    1 
ATOM   2134  C  CE    B MET A  1  276 ? 9.836   36.539  42.923 0.50 49.49  ? 1075 MET B CE    1 
ATOM   2135  N  N     . GLY A  1  277 ? 9.720   31.424  46.125 1.00 35.71  ? 1076 GLY B N     1 
ATOM   2136  C  CA    . GLY A  1  277 ? 9.190   30.640  47.233 1.00 33.14  ? 1076 GLY B CA    1 
ATOM   2137  C  C     . GLY A  1  277 ? 10.121  29.582  47.781 1.00 34.78  ? 1076 GLY B C     1 
ATOM   2138  O  O     . GLY A  1  277 ? 10.294  29.447  49.004 1.00 38.35  ? 1076 GLY B O     1 
ATOM   2139  N  N     . LYS A  1  278 ? 10.749  28.845  46.875 1.00 32.77  ? 1077 LYS B N     1 
ATOM   2140  C  CA    . LYS A  1  278 ? 11.624  27.730  47.250 1.00 38.18  ? 1077 LYS B CA    1 
ATOM   2141  C  C     . LYS A  1  278 ? 13.084  28.022  47.613 1.00 36.43  ? 1077 LYS B C     1 
ATOM   2142  O  O     . LYS A  1  278 ? 13.615  27.360  48.500 1.00 36.72  ? 1077 LYS B O     1 
ATOM   2143  C  CB    . LYS A  1  278 ? 11.612  26.682  46.149 1.00 35.49  ? 1077 LYS B CB    1 
ATOM   2144  C  CG    . LYS A  1  278 ? 10.263  26.006  45.942 1.00 35.25  ? 1077 LYS B CG    1 
ATOM   2145  C  CD    . LYS A  1  278 ? 10.459  24.957  44.852 1.00 39.22  ? 1077 LYS B CD    1 
ATOM   2146  C  CE    . LYS A  1  278 ? 9.220   24.144  44.586 1.00 49.15  ? 1077 LYS B CE    1 
ATOM   2147  N  NZ    . LYS A  1  278 ? 9.183   23.542  43.222 1.00 53.24  ? 1077 LYS B NZ    1 
ATOM   2148  N  N     . TYR A  1  279 ? 13.760  28.963  46.940 1.00 32.11  ? 1078 TYR B N     1 
ATOM   2149  C  CA    . TYR A  1  279 ? 15.202  29.106  47.214 1.00 32.02  ? 1078 TYR B CA    1 
ATOM   2150  C  C     . TYR A  1  279 ? 15.797  30.491  47.404 1.00 34.50  ? 1078 TYR B C     1 
ATOM   2151  O  O     . TYR A  1  279 ? 16.890  30.620  48.004 1.00 38.49  ? 1078 TYR B O     1 
ATOM   2152  C  CB    . TYR A  1  279 ? 16.014  28.436  46.125 1.00 33.45  ? 1078 TYR B CB    1 
ATOM   2153  C  CG    . TYR A  1  279 ? 15.408  27.200  45.519 1.00 31.67  ? 1078 TYR B CG    1 
ATOM   2154  C  CD1   . TYR A  1  279 ? 15.449  25.964  46.194 1.00 32.48  ? 1078 TYR B CD1   1 
ATOM   2155  C  CD2   . TYR A  1  279 ? 14.822  27.256  44.258 1.00 29.43  ? 1078 TYR B CD2   1 
ATOM   2156  C  CE1   . TYR A  1  279 ? 14.893  24.819  45.639 1.00 31.30  ? 1078 TYR B CE1   1 
ATOM   2157  C  CE2   . TYR A  1  279 ? 14.267  26.110  43.669 1.00 32.69  ? 1078 TYR B CE2   1 
ATOM   2158  C  CZ    . TYR A  1  279 ? 14.328  24.905  44.371 1.00 35.52  ? 1078 TYR B CZ    1 
ATOM   2159  O  OH    . TYR A  1  279 ? 13.809  23.798  43.831 1.00 41.76  ? 1078 TYR B OH    1 
ATOM   2160  N  N     . HIS A  1  280 ? 15.131  31.516  46.913 1.00 32.18  ? 1079 HIS B N     1 
ATOM   2161  C  CA    . HIS A  1  280 ? 15.783  32.809  46.884 1.00 33.60  ? 1079 HIS B CA    1 
ATOM   2162  C  C     . HIS A  1  280 ? 14.874  33.814  47.508 1.00 32.74  ? 1079 HIS B C     1 
ATOM   2163  O  O     . HIS A  1  280 ? 13.981  34.314  46.772 1.00 30.89  ? 1079 HIS B O     1 
ATOM   2164  C  CB    . HIS A  1  280 ? 16.099  33.200  45.427 1.00 31.89  ? 1079 HIS B CB    1 
ATOM   2165  C  CG    . HIS A  1  280 ? 17.149  34.270  45.303 1.00 33.70  ? 1079 HIS B CG    1 
ATOM   2166  N  ND1   . HIS A  1  280 ? 18.453  34.072  45.718 1.00 32.64  ? 1079 HIS B ND1   1 
ATOM   2167  C  CD2   . HIS A  1  280 ? 17.100  35.534  44.808 1.00 29.90  ? 1079 HIS B CD2   1 
ATOM   2168  C  CE1   . HIS A  1  280 ? 19.149  35.174  45.496 1.00 31.90  ? 1079 HIS B CE1   1 
ATOM   2169  N  NE2   . HIS A  1  280 ? 18.356  36.071  44.925 1.00 29.83  ? 1079 HIS B NE2   1 
ATOM   2170  N  N     . PRO A  1  281 ? 15.082  34.127  48.831 1.00 29.81  ? 1080 PRO B N     1 
ATOM   2171  C  CA    . PRO A  1  281 ? 14.078  35.037  49.382 1.00 28.95  ? 1080 PRO B CA    1 
ATOM   2172  C  C     . PRO A  1  281 ? 14.461  36.499  49.190 1.00 32.31  ? 1080 PRO B C     1 
ATOM   2173  O  O     . PRO A  1  281 ? 14.843  37.160  50.124 1.00 32.42  ? 1080 PRO B O     1 
ATOM   2174  C  CB    . PRO A  1  281 ? 14.076  34.680  50.870 1.00 29.94  ? 1080 PRO B CB    1 
ATOM   2175  C  CG    . PRO A  1  281 ? 15.494  34.255  51.169 1.00 30.96  ? 1080 PRO B CG    1 
ATOM   2176  C  CD    . PRO A  1  281 ? 16.075  33.762  49.884 1.00 27.09  ? 1080 PRO B CD    1 
ATOM   2177  N  N     . HIS A  1  282 ? 14.385  36.968  47.947 1.00 33.17  ? 1081 HIS B N     1 
ATOM   2178  C  CA    . HIS A  1  282 ? 14.705  38.327  47.624 1.00 30.58  ? 1081 HIS B CA    1 
ATOM   2179  C  C     . HIS A  1  282 ? 13.739  38.798  46.577 1.00 31.23  ? 1081 HIS B C     1 
ATOM   2180  O  O     . HIS A  1  282 ? 12.802  38.081  46.257 1.00 32.05  ? 1081 HIS B O     1 
ATOM   2181  C  CB    . HIS A  1  282 ? 16.153  38.436  47.169 1.00 27.79  ? 1081 HIS B CB    1 
ATOM   2182  C  CG    . HIS A  1  282 ? 17.119  37.998  48.208 1.00 30.91  ? 1081 HIS B CG    1 
ATOM   2183  N  ND1   . HIS A  1  282 ? 17.419  38.756  49.334 1.00 29.10  ? 1081 HIS B ND1   1 
ATOM   2184  C  CD2   . HIS A  1  282 ? 17.879  36.872  48.284 1.00 29.55  ? 1081 HIS B CD2   1 
ATOM   2185  C  CE1   . HIS A  1  282 ? 18.317  38.096  50.058 1.00 29.98  ? 1081 HIS B CE1   1 
ATOM   2186  N  NE2   . HIS A  1  282 ? 18.629  36.965  49.434 1.00 28.24  ? 1081 HIS B NE2   1 
ATOM   2187  N  N     . GLY A  1  283 ? 13.937  40.004  46.059 1.00 33.38  ? 1082 GLY B N     1 
ATOM   2188  C  CA    . GLY A  1  283 ? 12.964  40.596  45.125 1.00 34.16  ? 1082 GLY B CA    1 
ATOM   2189  C  C     . GLY A  1  283 ? 12.812  39.875  43.787 1.00 38.89  ? 1082 GLY B C     1 
ATOM   2190  O  O     . GLY A  1  283 ? 13.767  39.201  43.306 1.00 32.76  ? 1082 GLY B O     1 
ATOM   2191  N  N     . ASP A  1  284 ? 11.598  39.973  43.205 1.00 34.44  ? 1083 ASP B N     1 
ATOM   2192  C  CA    . ASP A  1  284 ? 11.310  39.362  41.930 1.00 32.71  ? 1083 ASP B CA    1 
ATOM   2193  C  C     . ASP A  1  284 ? 12.170  39.946  40.809 1.00 32.33  ? 1083 ASP B C     1 
ATOM   2194  O  O     . ASP A  1  284 ? 12.589  39.221  39.930 1.00 38.50  ? 1083 ASP B O     1 
ATOM   2195  C  CB    . ASP A  1  284 ? 9.817   39.466  41.587 1.00 38.84  ? 1083 ASP B CB    1 
ATOM   2196  C  CG    . ASP A  1  284 ? 9.354   40.925  41.405 1.00 42.61  ? 1083 ASP B CG    1 
ATOM   2197  O  OD1   . ASP A  1  284 ? 9.021   41.543  42.398 1.00 44.80  ? 1083 ASP B OD1   1 
ATOM   2198  O  OD2   . ASP A  1  284 ? 9.324   41.454  40.290 1.00 45.00  ? 1083 ASP B OD2   1 
ATOM   2199  N  N     . SER A  1  285 ? 12.421  41.250  40.820 1.00 27.93  ? 1084 SER B N     1 
ATOM   2200  C  CA    . SER A  1  285 ? 13.211  41.822  39.762 1.00 30.77  ? 1084 SER B CA    1 
ATOM   2201  C  C     . SER A  1  285 ? 14.677  41.379  39.779 1.00 29.13  ? 1084 SER B C     1 
ATOM   2202  O  O     . SER A  1  285 ? 15.279  41.287  38.702 1.00 33.46  ? 1084 SER B O     1 
ATOM   2203  C  CB    . SER A  1  285 ? 13.034  43.355  39.692 1.00 29.43  ? 1084 SER B CB    1 
ATOM   2204  O  OG    . SER A  1  285 ? 13.709  43.927  40.781 1.00 37.26  ? 1084 SER B OG    1 
ATOM   2205  N  N     . SER A  1  286 ? 15.239  41.113  40.960 1.00 28.86  ? 1085 SER B N     1 
ATOM   2206  C  CA    . SER A  1  286 ? 16.621  40.579  41.037 1.00 33.23  ? 1085 SER B CA    1 
ATOM   2207  C  C     . SER A  1  286 ? 16.712  39.227  40.366 1.00 30.54  ? 1085 SER B C     1 
ATOM   2208  O  O     . SER A  1  286 ? 17.669  38.997  39.668 1.00 34.95  ? 1085 SER B O     1 
ATOM   2209  C  CB    . SER A  1  286 ? 17.083  40.347  42.490 1.00 31.48  ? 1085 SER B CB    1 
ATOM   2210  O  OG    . SER A  1  286 ? 17.467  41.546  43.091 1.00 34.23  ? 1085 SER B OG    1 
ATOM   2211  N  N     . ILE A  1  287 ? 15.725  38.357  40.613 1.00 30.21  ? 1086 ILE B N     1 
ATOM   2212  C  CA    . ILE A  1  287 ? 15.679  37.058  39.996 1.00 29.52  ? 1086 ILE B CA    1 
ATOM   2213  C  C     . ILE A  1  287 ? 15.409  37.134  38.497 1.00 32.57  ? 1086 ILE B C     1 
ATOM   2214  O  O     . ILE A  1  287 ? 16.106  36.503  37.707 1.00 30.26  ? 1086 ILE B O     1 
ATOM   2215  C  CB    . ILE A  1  287 ? 14.596  36.187  40.662 1.00 33.06  ? 1086 ILE B CB    1 
ATOM   2216  C  CG1   . ILE A  1  287 ? 14.875  36.043  42.167 1.00 27.88  ? 1086 ILE B CG1   1 
ATOM   2217  C  CG2   . ILE A  1  287 ? 14.504  34.805  39.984 1.00 32.37  ? 1086 ILE B CG2   1 
ATOM   2218  C  CD1   . ILE A  1  287 ? 13.709  35.530  42.960 1.00 30.12  ? 1086 ILE B CD1   1 
ATOM   2219  N  N     . TYR A  1  288 ? 14.392  37.896  38.096 1.00 28.93  ? 1087 TYR B N     1 
ATOM   2220  C  CA    . TYR A  1  288 ? 14.034  37.975  36.713 1.00 28.01  ? 1087 TYR B CA    1 
ATOM   2221  C  C     . TYR A  1  288 ? 15.135  38.607  35.864 1.00 31.37  ? 1087 TYR B C     1 
ATOM   2222  O  O     . TYR A  1  288 ? 15.422  38.131  34.765 1.00 35.04  ? 1087 TYR B O     1 
ATOM   2223  C  CB    . TYR A  1  288 ? 12.714  38.754  36.551 1.00 30.23  ? 1087 TYR B CB    1 
ATOM   2224  C  CG    . TYR A  1  288 ? 12.272  38.846  35.107 1.00 31.34  ? 1087 TYR B CG    1 
ATOM   2225  C  CD1   . TYR A  1  288 ? 12.101  37.689  34.336 1.00 29.02  ? 1087 TYR B CD1   1 
ATOM   2226  C  CD2   . TYR A  1  288 ? 12.042  40.099  34.501 1.00 29.29  ? 1087 TYR B CD2   1 
ATOM   2227  C  CE1   . TYR A  1  288 ? 11.679  37.757  33.008 1.00 29.73  ? 1087 TYR B CE1   1 
ATOM   2228  C  CE2   . TYR A  1  288 ? 11.659  40.161  33.184 1.00 30.18  ? 1087 TYR B CE2   1 
ATOM   2229  C  CZ    . TYR A  1  288 ? 11.467  38.979  32.443 1.00 27.51  ? 1087 TYR B CZ    1 
ATOM   2230  O  OH    . TYR A  1  288 ? 11.081  39.047  31.125 1.00 29.10  ? 1087 TYR B OH    1 
ATOM   2231  N  N     . GLU A  1  289 ? 15.750  39.681  36.330 1.00 29.04  ? 1088 GLU B N     1 
ATOM   2232  C  CA    . GLU A  1  289 ? 16.816  40.282  35.535 1.00 30.33  ? 1088 GLU B CA    1 
ATOM   2233  C  C     . GLU A  1  289 ? 18.064  39.371  35.450 1.00 28.75  ? 1088 GLU B C     1 
ATOM   2234  O  O     . GLU A  1  289 ? 18.704  39.303  34.434 1.00 30.05  ? 1088 GLU B O     1 
ATOM   2235  C  CB    . GLU A  1  289 ? 17.172  41.671  36.035 1.00 32.59  ? 1088 GLU B CB    1 
ATOM   2236  C  CG    . GLU A  1  289 ? 16.188  42.700  35.545 1.00 39.75  ? 1088 GLU B CG    1 
ATOM   2237  C  CD    . GLU A  1  289 ? 16.188  43.955  36.423 1.00 47.30  ? 1088 GLU B CD    1 
ATOM   2238  O  OE1   . GLU A  1  289 ? 15.163  44.642  36.474 1.00 51.54  ? 1088 GLU B OE1   1 
ATOM   2239  O  OE2   . GLU A  1  289 ? 17.204  44.256  37.071 1.00 55.45  ? 1088 GLU B OE2   1 
ATOM   2240  N  N     . ALA A  1  290 ? 18.367  38.627  36.494 1.00 29.37  ? 1089 ALA B N     1 
ATOM   2241  C  CA    . ALA A  1  290 ? 19.481  37.664  36.412 1.00 29.79  ? 1089 ALA B CA    1 
ATOM   2242  C  C     . ALA A  1  290 ? 19.193  36.601  35.342 1.00 31.17  ? 1089 ALA B C     1 
ATOM   2243  O  O     . ALA A  1  290 ? 20.082  36.184  34.645 1.00 34.26  ? 1089 ALA B O     1 
ATOM   2244  C  CB    . ALA A  1  290 ? 19.714  37.031  37.767 1.00 24.85  ? 1089 ALA B CB    1 
ATOM   2245  N  N     . MET A  1  291 ? 17.954  36.150  35.248 1.00 30.22  ? 1090 MET B N     1 
ATOM   2246  C  CA    . MET A  1  291 ? 17.566  35.163  34.277 1.00 32.09  ? 1090 MET B CA    1 
ATOM   2247  C  C     . MET A  1  291 ? 17.585  35.692  32.859 1.00 29.55  ? 1090 MET B C     1 
ATOM   2248  O  O     . MET A  1  291 ? 17.898  34.981  31.930 1.00 30.13  ? 1090 MET B O     1 
ATOM   2249  C  CB    . MET A  1  291 ? 16.149  34.664  34.570 1.00 33.03  ? 1090 MET B CB    1 
ATOM   2250  C  CG    . MET A  1  291 ? 15.713  33.653  33.555 1.00 35.31  ? 1090 MET B CG    1 
ATOM   2251  S  SD    . MET A  1  291 ? 14.178  32.803  33.952 1.00 41.54  ? 1090 MET B SD    1 
ATOM   2252  C  CE    . MET A  1  291 ? 12.976  33.854  33.194 1.00 34.50  ? 1090 MET B CE    1 
ATOM   2253  N  N     . VAL A  1  292 ? 17.162  36.922  32.706 1.00 27.71  ? 1091 VAL B N     1 
ATOM   2254  C  CA    . VAL A  1  292 ? 17.176  37.586  31.439 1.00 28.37  ? 1091 VAL B CA    1 
ATOM   2255  C  C     . VAL A  1  292 ? 18.592  37.720  30.845 1.00 27.92  ? 1091 VAL B C     1 
ATOM   2256  O  O     . VAL A  1  292 ? 18.762  37.516  29.654 1.00 31.62  ? 1091 VAL B O     1 
ATOM   2257  C  CB    . VAL A  1  292 ? 16.513  38.958  31.575 1.00 28.82  ? 1091 VAL B CB    1 
ATOM   2258  C  CG1   . VAL A  1  292 ? 16.913  39.871  30.434 1.00 26.18  ? 1091 VAL B CG1   1 
ATOM   2259  C  CG2   . VAL A  1  292 ? 15.001  38.726  31.617 1.00 30.84  ? 1091 VAL B CG2   1 
ATOM   2260  N  N     . ARG A  1  293 ? 19.575  38.069  31.653 1.00 25.36  ? 1092 ARG B N     1 
ATOM   2261  C  CA    . ARG A  1  293 ? 20.952  38.159  31.196 1.00 30.99  ? 1092 ARG B CA    1 
ATOM   2262  C  C     . ARG A  1  293 ? 21.481  36.806  30.735 1.00 31.72  ? 1092 ARG B C     1 
ATOM   2263  O  O     . ARG A  1  293 ? 22.156  36.736  29.713 1.00 33.73  ? 1092 ARG B O     1 
ATOM   2264  C  CB    . ARG A  1  293 ? 21.855  38.812  32.238 1.00 33.29  ? 1092 ARG B CB    1 
ATOM   2265  C  CG    . ARG A  1  293 ? 21.542  40.304  32.415 1.00 39.64  ? 1092 ARG B CG    1 
ATOM   2266  C  CD    . ARG A  1  293 ? 22.460  41.002  33.427 1.00 47.37  ? 1092 ARG B CD    1 
ATOM   2267  N  NE    . ARG A  1  293 ? 22.104  40.685  34.813 1.00 57.07  ? 1092 ARG B NE    1 
ATOM   2268  C  CZ    . ARG A  1  293 ? 21.324  41.423  35.614 1.00 52.17  ? 1092 ARG B CZ    1 
ATOM   2269  N  NH1   . ARG A  1  293 ? 21.093  41.007  36.870 1.00 42.94  ? 1092 ARG B NH1   1 
ATOM   2270  N  NH2   . ARG A  1  293 ? 20.808  42.568  35.175 1.00 45.90  ? 1092 ARG B NH2   1 
ATOM   2271  N  N     . MET A  1  294 ? 21.141  35.735  31.449 1.00 29.79  ? 1093 MET B N     1 
ATOM   2272  C  CA    . MET A  1  294 ? 21.569  34.387  31.052 1.00 31.11  ? 1093 MET B CA    1 
ATOM   2273  C  C     . MET A  1  294 ? 21.020  34.034  29.682 1.00 32.71  ? 1093 MET B C     1 
ATOM   2274  O  O     . MET A  1  294 ? 21.611  33.291  28.963 1.00 37.60  ? 1093 MET B O     1 
ATOM   2275  C  CB    . MET A  1  294 ? 21.143  33.362  32.084 1.00 30.78  ? 1093 MET B CB    1 
ATOM   2276  C  CG    . MET A  1  294 ? 21.924  33.501  33.382 1.00 34.44  ? 1093 MET B CG    1 
ATOM   2277  S  SD    . MET A  1  294 ? 21.712  32.192  34.602 1.00 38.70  ? 1093 MET B SD    1 
ATOM   2278  C  CE    . MET A  1  294 ? 20.002  32.429  35.011 1.00 34.58  ? 1093 MET B CE    1 
ATOM   2279  N  N     . ALA A  1  295 ? 19.886  34.610  29.316 1.00 30.72  ? 1094 ALA B N     1 
ATOM   2280  C  CA    . ALA A  1  295 ? 19.322  34.434  27.998 1.00 30.72  ? 1094 ALA B CA    1 
ATOM   2281  C  C     . ALA A  1  295 ? 19.886  35.300  26.855 1.00 30.14  ? 1094 ALA B C     1 
ATOM   2282  O  O     . ALA A  1  295 ? 19.539  35.099  25.715 1.00 30.31  ? 1094 ALA B O     1 
ATOM   2283  C  CB    . ALA A  1  295 ? 17.805  34.624  28.089 1.00 34.44  ? 1094 ALA B CB    1 
ATOM   2284  N  N     . GLN A  1  296 ? 20.699  36.307  27.153 1.00 29.69  ? 1095 GLN B N     1 
ATOM   2285  C  CA    . GLN A  1  296 ? 21.059  37.271  26.125 1.00 29.52  ? 1095 GLN B CA    1 
ATOM   2286  C  C     . GLN A  1  296 ? 22.345  36.824  25.506 1.00 32.69  ? 1095 GLN B C     1 
ATOM   2287  O  O     . GLN A  1  296 ? 23.339  36.677  26.229 1.00 30.24  ? 1095 GLN B O     1 
ATOM   2288  C  CB    . GLN A  1  296 ? 21.273  38.678  26.683 1.00 28.93  ? 1095 GLN B CB    1 
ATOM   2289  C  CG    . GLN A  1  296 ? 20.037  39.222  27.355 1.00 29.50  ? 1095 GLN B CG    1 
ATOM   2290  C  CD    . GLN A  1  296 ? 20.268  40.540  28.093 1.00 32.70  ? 1095 GLN B CD    1 
ATOM   2291  O  OE1   . GLN A  1  296 ? 21.293  40.804  28.711 1.00 30.23  ? 1095 GLN B OE1   1 
ATOM   2292  N  NE2   . GLN A  1  296 ? 19.290  41.389  28.014 1.00 36.48  ? 1095 GLN B NE2   1 
ATOM   2293  N  N     . ASP A  1  297 ? 22.358  36.663  24.175 1.00 28.96  ? 1096 ASP B N     1 
ATOM   2294  C  CA    . ASP A  1  297 ? 23.553  36.186  23.552 1.00 30.98  ? 1096 ASP B CA    1 
ATOM   2295  C  C     . ASP A  1  297 ? 24.625  37.266  23.371 1.00 31.17  ? 1096 ASP B C     1 
ATOM   2296  O  O     . ASP A  1  297 ? 25.765  36.953  22.990 1.00 28.13  ? 1096 ASP B O     1 
ATOM   2297  C  CB    . ASP A  1  297 ? 23.196  35.471  22.232 1.00 35.45  ? 1096 ASP B CB    1 
ATOM   2298  C  CG    . ASP A  1  297 ? 22.571  36.371  21.217 1.00 37.96  ? 1096 ASP B CG    1 
ATOM   2299  O  OD1   . ASP A  1  297 ? 22.615  37.609  21.348 1.00 46.74  ? 1096 ASP B OD1   1 
ATOM   2300  O  OD2   . ASP A  1  297 ? 22.054  35.819  20.231 1.00 51.05  ? 1096 ASP B OD2   1 
ATOM   2301  N  N     . PHE A  1  298 ? 24.261  38.514  23.638 1.00 27.07  ? 1097 PHE B N     1 
ATOM   2302  C  CA    . PHE A  1  298 ? 25.252  39.600  23.614 1.00 28.63  ? 1097 PHE B CA    1 
ATOM   2303  C  C     . PHE A  1  298 ? 25.851  39.800  25.004 1.00 32.77  ? 1097 PHE B C     1 
ATOM   2304  O  O     . PHE A  1  298 ? 26.742  40.583  25.161 1.00 39.82  ? 1097 PHE B O     1 
ATOM   2305  C  CB    . PHE A  1  298 ? 24.658  40.914  23.102 1.00 30.07  ? 1097 PHE B CB    1 
ATOM   2306  C  CG    . PHE A  1  298 ? 23.426  41.348  23.842 1.00 29.28  ? 1097 PHE B CG    1 
ATOM   2307  C  CD1   . PHE A  1  298 ? 23.570  42.047  25.037 1.00 28.35  ? 1097 PHE B CD1   1 
ATOM   2308  C  CD2   . PHE A  1  298 ? 22.145  41.043  23.371 1.00 29.75  ? 1097 PHE B CD2   1 
ATOM   2309  C  CE1   . PHE A  1  298 ? 22.470  42.485  25.749 1.00 32.28  ? 1097 PHE B CE1   1 
ATOM   2310  C  CE2   . PHE A  1  298 ? 21.007  41.435  24.130 1.00 33.83  ? 1097 PHE B CE2   1 
ATOM   2311  C  CZ    . PHE A  1  298 ? 21.183  42.169  25.324 1.00 31.04  ? 1097 PHE B CZ    1 
ATOM   2312  N  N     . SER A  1  299 ? 25.378  39.055  25.990 1.00 28.12  ? 1098 SER B N     1 
ATOM   2313  C  CA    . SER A  1  299 ? 25.903  39.112  27.363 1.00 27.50  ? 1098 SER B CA    1 
ATOM   2314  C  C     . SER A  1  299 ? 26.668  37.809  27.746 1.00 28.98  ? 1098 SER B C     1 
ATOM   2315  O  O     . SER A  1  299 ? 27.803  37.849  28.195 1.00 29.69  ? 1098 SER B O     1 
ATOM   2316  C  CB    . SER A  1  299 ? 24.770  39.324  28.388 1.00 28.76  ? 1098 SER B CB    1 
ATOM   2317  O  OG    . SER A  1  299 ? 24.034  40.495  28.092 1.00 36.71  ? 1098 SER B OG    1 
ATOM   2318  N  N     . TYR A  1  300 ? 26.033  36.666  27.501 1.00 30.27  ? 1099 TYR B N     1 
ATOM   2319  C  CA    . TYR A  1  300 ? 26.599  35.348  27.811 1.00 29.72  ? 1099 TYR B CA    1 
ATOM   2320  C  C     . TYR A  1  300 ? 27.254  34.712  26.563 1.00 32.53  ? 1099 TYR B C     1 
ATOM   2321  O  O     . TYR A  1  300 ? 26.623  34.515  25.511 1.00 29.16  ? 1099 TYR B O     1 
ATOM   2322  C  CB    . TYR A  1  300 ? 25.538  34.435  28.403 1.00 29.90  ? 1099 TYR B CB    1 
ATOM   2323  C  CG    . TYR A  1  300 ? 25.389  34.534  29.897 1.00 31.64  ? 1099 TYR B CG    1 
ATOM   2324  C  CD1   . TYR A  1  300 ? 24.929  35.716  30.473 1.00 29.03  ? 1099 TYR B CD1   1 
ATOM   2325  C  CD2   . TYR A  1  300 ? 25.717  33.463  30.748 1.00 28.89  ? 1099 TYR B CD2   1 
ATOM   2326  C  CE1   . TYR A  1  300 ? 24.820  35.881  31.823 1.00 28.64  ? 1099 TYR B CE1   1 
ATOM   2327  C  CE2   . TYR A  1  300 ? 25.609  33.599  32.121 1.00 29.57  ? 1099 TYR B CE2   1 
ATOM   2328  C  CZ    . TYR A  1  300 ? 25.143  34.832  32.642 1.00 32.45  ? 1099 TYR B CZ    1 
ATOM   2329  O  OH    . TYR A  1  300 ? 24.978  35.084  33.992 1.00 33.55  ? 1099 TYR B OH    1 
ATOM   2330  N  N     . ARG A  1  301 ? 28.526  34.355  26.705 1.00 28.74  ? 1100 ARG B N     1 
ATOM   2331  C  CA    . ARG A  1  301 ? 29.236  33.694  25.644 1.00 29.67  ? 1100 ARG B CA    1 
ATOM   2332  C  C     . ARG A  1  301 ? 28.622  32.327  25.306 1.00 26.89  ? 1100 ARG B C     1 
ATOM   2333  O  O     . ARG A  1  301 ? 28.614  31.929  24.161 1.00 29.68  ? 1100 ARG B O     1 
ATOM   2334  C  CB    . ARG A  1  301 ? 30.680  33.551  26.095 1.00 28.07  ? 1100 ARG B CB    1 
ATOM   2335  C  CG    . ARG A  1  301 ? 31.716  33.373  25.008 1.00 29.48  ? 1100 ARG B CG    1 
ATOM   2336  C  CD    . ARG A  1  301 ? 31.326  33.905  23.662 1.00 31.62  ? 1100 ARG B CD    1 
ATOM   2337  N  NE    . ARG A  1  301 ? 32.294  33.405  22.701 1.00 31.89  ? 1100 ARG B NE    1 
ATOM   2338  C  CZ    . ARG A  1  301 ? 32.082  32.359  21.900 1.00 32.82  ? 1100 ARG B CZ    1 
ATOM   2339  N  NH1   . ARG A  1  301 ? 30.923  31.698  21.944 1.00 28.50  ? 1100 ARG B NH1   1 
ATOM   2340  N  NH2   . ARG A  1  301 ? 33.034  31.975  21.054 1.00 32.24  ? 1100 ARG B NH2   1 
ATOM   2341  N  N     . TYR A  1  302 ? 28.154  31.630  26.309 1.00 24.17  ? 1101 TYR B N     1 
ATOM   2342  C  CA    . TYR A  1  302 ? 27.361  30.418  26.126 1.00 27.52  ? 1101 TYR B CA    1 
ATOM   2343  C  C     . TYR A  1  302 ? 26.133  30.587  26.993 1.00 24.32  ? 1101 TYR B C     1 
ATOM   2344  O  O     . TYR A  1  302 ? 26.148  30.345  28.159 1.00 27.47  ? 1101 TYR B O     1 
ATOM   2345  C  CB    . TYR A  1  302 ? 28.196  29.171  26.565 1.00 25.79  ? 1101 TYR B CB    1 
ATOM   2346  C  CG    . TYR A  1  302 ? 29.467  29.107  25.777 1.00 25.18  ? 1101 TYR B CG    1 
ATOM   2347  C  CD1   . TYR A  1  302 ? 29.457  28.591  24.468 1.00 26.24  ? 1101 TYR B CD1   1 
ATOM   2348  C  CD2   . TYR A  1  302 ? 30.612  29.741  26.244 1.00 25.35  ? 1101 TYR B CD2   1 
ATOM   2349  C  CE1   . TYR A  1  302 ? 30.581  28.610  23.687 1.00 27.36  ? 1101 TYR B CE1   1 
ATOM   2350  C  CE2   . TYR A  1  302 ? 31.768  29.762  25.492 1.00 24.73  ? 1101 TYR B CE2   1 
ATOM   2351  C  CZ    . TYR A  1  302 ? 31.744  29.204  24.220 1.00 29.11  ? 1101 TYR B CZ    1 
ATOM   2352  O  OH    . TYR A  1  302 ? 32.848  29.225  23.445 1.00 29.98  ? 1101 TYR B OH    1 
ATOM   2353  N  N     . PRO A  1  303 ? 25.068  31.044  26.412 1.00 25.31  ? 1102 PRO B N     1 
ATOM   2354  C  CA    . PRO A  1  303 ? 23.834  31.380  27.155 1.00 25.59  ? 1102 PRO B CA    1 
ATOM   2355  C  C     . PRO A  1  303 ? 23.288  30.215  27.915 1.00 29.55  ? 1102 PRO B C     1 
ATOM   2356  O  O     . PRO A  1  303 ? 23.285  29.083  27.378 1.00 26.65  ? 1102 PRO B O     1 
ATOM   2357  C  CB    . PRO A  1  303 ? 22.870  31.747  26.041 1.00 25.86  ? 1102 PRO B CB    1 
ATOM   2358  C  CG    . PRO A  1  303 ? 23.767  32.361  25.022 1.00 26.20  ? 1102 PRO B CG    1 
ATOM   2359  C  CD    . PRO A  1  303 ? 24.999  31.481  25.006 1.00 24.79  ? 1102 PRO B CD    1 
ATOM   2360  N  N     . LEU A  1  304 ? 22.865  30.472  29.147 1.00 30.60  ? 1103 LEU B N     1 
ATOM   2361  C  CA    . LEU A  1  304 ? 22.384  29.399  30.006 1.00 30.50  ? 1103 LEU B CA    1 
ATOM   2362  C  C     . LEU A  1  304 ? 20.863  29.305  29.970 1.00 33.27  ? 1103 LEU B C     1 
ATOM   2363  O  O     . LEU A  1  304 ? 20.308  28.350  30.444 1.00 31.73  ? 1103 LEU B O     1 
ATOM   2364  C  CB    . LEU A  1  304 ? 22.863  29.620  31.447 1.00 26.24  ? 1103 LEU B CB    1 
ATOM   2365  C  CG    . LEU A  1  304 ? 24.394  29.707  31.587 1.00 27.79  ? 1103 LEU B CG    1 
ATOM   2366  C  CD1   . LEU A  1  304 ? 24.791  29.918  33.016 1.00 22.39  ? 1103 LEU B CD1   1 
ATOM   2367  C  CD2   . LEU A  1  304 ? 25.076  28.442  31.041 1.00 26.26  ? 1103 LEU B CD2   1 
ATOM   2368  N  N     . VAL A  1  305 ? 20.197  30.315  29.429 1.00 34.57  ? 1104 VAL B N     1 
ATOM   2369  C  CA    . VAL A  1  305 ? 18.747  30.333  29.398 1.00 31.76  ? 1104 VAL B CA    1 
ATOM   2370  C  C     . VAL A  1  305 ? 18.280  30.497  27.966 1.00 31.62  ? 1104 VAL B C     1 
ATOM   2371  O  O     . VAL A  1  305 ? 18.905  31.222  27.174 1.00 28.23  ? 1104 VAL B O     1 
ATOM   2372  C  CB    . VAL A  1  305 ? 18.180  31.424  30.299 1.00 30.00  ? 1104 VAL B CB    1 
ATOM   2373  C  CG1   . VAL A  1  305 ? 16.680  31.574  30.085 1.00 31.94  ? 1104 VAL B CG1   1 
ATOM   2374  C  CG2   . VAL A  1  305 ? 18.454  31.067  31.742 1.00 29.31  ? 1104 VAL B CG2   1 
ATOM   2375  N  N     . ASP A  1  306 ? 17.225  29.773  27.610 1.00 30.07  ? 1105 ASP B N     1 
ATOM   2376  C  CA    . ASP A  1  306 ? 16.631  29.884  26.301 1.00 31.79  ? 1105 ASP B CA    1 
ATOM   2377  C  C     . ASP A  1  306 ? 15.340  30.665  26.489 1.00 33.30  ? 1105 ASP B C     1 
ATOM   2378  O  O     . ASP A  1  306 ? 14.374  30.187  27.124 1.00 31.45  ? 1105 ASP B O     1 
ATOM   2379  C  CB    . ASP A  1  306 ? 16.313  28.464  25.841 1.00 35.16  ? 1105 ASP B CB    1 
ATOM   2380  C  CG    . ASP A  1  306 ? 15.659  28.424  24.475 1.00 38.54  ? 1105 ASP B CG    1 
ATOM   2381  O  OD1   . ASP A  1  306 ? 15.462  29.466  23.830 1.00 36.66  ? 1105 ASP B OD1   1 
ATOM   2382  O  OD2   . ASP A  1  306 ? 15.365  27.312  24.017 1.00 35.83  ? 1105 ASP B OD2   1 
ATOM   2383  N  N     . GLY A  1  307 ? 15.319  31.865  25.926 1.00 35.06  ? 1106 GLY B N     1 
ATOM   2384  C  CA    . GLY A  1  307 ? 14.232  32.797  26.162 1.00 33.21  ? 1106 GLY B CA    1 
ATOM   2385  C  C     . GLY A  1  307 ? 13.341  32.942  24.980 1.00 37.24  ? 1106 GLY B C     1 
ATOM   2386  O  O     . GLY A  1  307 ? 13.804  32.895  23.840 1.00 41.13  ? 1106 GLY B O     1 
ATOM   2387  N  N     . GLN A  1  308 ? 12.043  33.076  25.218 1.00 38.43  ? 1107 GLN B N     1 
ATOM   2388  C  CA    . GLN A  1  308 ? 11.137  33.304  24.114 1.00 37.95  ? 1107 GLN B CA    1 
ATOM   2389  C  C     . GLN A  1  308 ? 10.506  34.653  24.382 1.00 38.76  ? 1107 GLN B C     1 
ATOM   2390  O  O     . GLN A  1  308 ? 9.958   34.858  25.469 1.00 38.51  ? 1107 GLN B O     1 
ATOM   2391  C  CB    . GLN A  1  308 ? 10.092  32.176  24.071 1.00 43.74  ? 1107 GLN B CB    1 
ATOM   2392  C  CG    . GLN A  1  308 ? 8.831   32.462  23.273 1.00 43.52  ? 1107 GLN B CG    1 
ATOM   2393  C  CD    . GLN A  1  308 ? 9.080   32.389  21.788 1.00 53.32  ? 1107 GLN B CD    1 
ATOM   2394  O  OE1   . GLN A  1  308 ? 9.749   31.463  21.315 1.00 63.00  ? 1107 GLN B OE1   1 
ATOM   2395  N  NE2   . GLN A  1  308 ? 8.534   33.362  21.025 1.00 56.85  ? 1107 GLN B NE2   1 
ATOM   2396  N  N     . GLY A  1  309 ? 10.571  35.570  23.419 1.00 32.06  ? 1108 GLY B N     1 
ATOM   2397  C  CA    . GLY A  1  309 ? 9.996   36.886  23.635 1.00 31.97  ? 1108 GLY B CA    1 
ATOM   2398  C  C     . GLY A  1  309 ? 11.051  37.965  23.738 1.00 33.83  ? 1108 GLY B C     1 
ATOM   2399  O  O     . GLY A  1  309 ? 12.219  37.744  23.395 1.00 33.65  ? 1108 GLY B O     1 
ATOM   2400  N  N     . ASN A  1  310 ? 10.638  39.147  24.156 1.00 31.02  ? 1109 ASN B N     1 
ATOM   2401  C  CA    . ASN A  1  310 ? 11.569  40.261  24.266 1.00 33.15  ? 1109 ASN B CA    1 
ATOM   2402  C  C     . ASN A  1  310 ? 12.509  40.133  25.486 1.00 35.16  ? 1109 ASN B C     1 
ATOM   2403  O  O     . ASN A  1  310 ? 12.062  40.231  26.643 1.00 33.19  ? 1109 ASN B O     1 
ATOM   2404  C  CB    . ASN A  1  310 ? 10.767  41.565  24.280 1.00 30.54  ? 1109 ASN B CB    1 
ATOM   2405  C  CG    . ASN A  1  310 ? 11.629  42.777  24.510 1.00 32.95  ? 1109 ASN B CG    1 
ATOM   2406  O  OD1   . ASN A  1  310 ? 12.866  42.688  24.560 1.00 33.02  ? 1109 ASN B OD1   1 
ATOM   2407  N  ND2   . ASN A  1  310 ? 10.960  43.939  24.715 1.00 29.02  ? 1109 ASN B ND2   1 
ATOM   2408  N  N     . PHE A  1  311 ? 13.783  39.896  25.231 1.00 31.65  ? 1110 PHE B N     1 
ATOM   2409  C  CA    . PHE A  1  311 ? 14.701  39.704  26.331 1.00 30.06  ? 1110 PHE B CA    1 
ATOM   2410  C  C     . PHE A  1  311 ? 15.712  40.816  26.351 1.00 32.18  ? 1110 PHE B C     1 
ATOM   2411  O  O     . PHE A  1  311 ? 16.837  40.652  26.828 1.00 33.64  ? 1110 PHE B O     1 
ATOM   2412  C  CB    . PHE A  1  311 ? 15.366  38.316  26.219 1.00 29.98  ? 1110 PHE B CB    1 
ATOM   2413  C  CG    . PHE A  1  311 ? 14.642  37.284  26.988 1.00 30.56  ? 1110 PHE B CG    1 
ATOM   2414  C  CD1   . PHE A  1  311 ? 13.468  36.747  26.480 1.00 31.12  ? 1110 PHE B CD1   1 
ATOM   2415  C  CD2   . PHE A  1  311 ? 15.026  36.968  28.278 1.00 31.06  ? 1110 PHE B CD2   1 
ATOM   2416  C  CE1   . PHE A  1  311 ? 12.752  35.831  27.206 1.00 32.04  ? 1110 PHE B CE1   1 
ATOM   2417  C  CE2   . PHE A  1  311 ? 14.301  36.051  29.016 1.00 32.12  ? 1110 PHE B CE2   1 
ATOM   2418  C  CZ    . PHE A  1  311 ? 13.155  35.477  28.488 1.00 30.63  ? 1110 PHE B CZ    1 
ATOM   2419  N  N     . GLY A  1  312 ? 15.335  41.963  25.822 1.00 33.08  ? 1111 GLY B N     1 
ATOM   2420  C  CA    . GLY A  1  312 ? 16.224  43.114  25.853 1.00 31.68  ? 1111 GLY B CA    1 
ATOM   2421  C  C     . GLY A  1  312 ? 17.197  43.176  24.685 1.00 38.51  ? 1111 GLY B C     1 
ATOM   2422  O  O     . GLY A  1  312 ? 17.256  42.267  23.836 1.00 35.93  ? 1111 GLY B O     1 
ATOM   2423  N  N     . SER A  1  313 ? 17.982  44.252  24.637 1.00 35.64  ? 1112 SER B N     1 
ATOM   2424  C  CA    . SER A  1  313 ? 18.825  44.537  23.461 1.00 34.49  ? 1112 SER B CA    1 
ATOM   2425  C  C     . SER A  1  313 ? 20.176  45.124  23.854 1.00 35.52  ? 1112 SER B C     1 
ATOM   2426  O  O     . SER A  1  313 ? 20.443  45.381  25.033 1.00 40.34  ? 1112 SER B O     1 
ATOM   2427  C  CB    . SER A  1  313 ? 18.111  45.498  22.520 1.00 36.61  ? 1112 SER B CB    1 
ATOM   2428  O  OG    . SER A  1  313 ? 18.101  46.814  23.106 1.00 36.98  ? 1112 SER B OG    1 
ATOM   2429  N  N     . MET A  1  314 ? 21.037  45.342  22.870 1.00 38.87  ? 1113 MET B N     1 
ATOM   2430  C  CA    . MET A  1  314 ? 22.341  45.944  23.101 1.00 38.95  ? 1113 MET B CA    1 
ATOM   2431  C  C     . MET A  1  314 ? 22.214  47.437  23.327 1.00 43.94  ? 1113 MET B C     1 
ATOM   2432  O  O     . MET A  1  314 ? 23.178  48.065  23.690 1.00 43.66  ? 1113 MET B O     1 
ATOM   2433  C  CB    . MET A  1  314 ? 23.257  45.691  21.916 1.00 44.73  ? 1113 MET B CB    1 
ATOM   2434  C  CG    . MET A  1  314 ? 23.707  44.251  21.798 1.00 49.47  ? 1113 MET B CG    1 
ATOM   2435  S  SD    . MET A  1  314 ? 24.596  43.926  20.275 1.00 53.02  ? 1113 MET B SD    1 
ATOM   2436  C  CE    . MET A  1  314 ? 26.042  44.921  20.569 1.00 42.29  ? 1113 MET B CE    1 
ATOM   2437  N  N     . ASP A  1  315 ? 21.024  47.998  23.120 1.00 39.06  ? 1114 ASP B N     1 
ATOM   2438  C  CA    . ASP A  1  315 ? 20.824  49.402  23.345 1.00 39.48  ? 1114 ASP B CA    1 
ATOM   2439  C  C     . ASP A  1  315 ? 20.324  49.669  24.724 1.00 45.05  ? 1114 ASP B C     1 
ATOM   2440  O  O     . ASP A  1  315 ? 20.052  50.814  25.056 1.00 45.52  ? 1114 ASP B O     1 
ATOM   2441  C  CB    . ASP A  1  315 ? 19.792  49.925  22.389 1.00 42.89  ? 1114 ASP B CB    1 
ATOM   2442  C  CG    . ASP A  1  315 ? 20.344  50.104  20.996 1.00 47.88  ? 1114 ASP B CG    1 
ATOM   2443  O  OD1   . ASP A  1  315 ? 21.570  49.980  20.803 1.00 45.01  ? 1114 ASP B OD1   1 
ATOM   2444  O  OD2   . ASP A  1  315 ? 19.557  50.364  20.082 1.00 49.41  ? 1114 ASP B OD2   1 
ATOM   2445  N  N     . GLY A  1  316 ? 20.166  48.613  25.528 1.00 41.37  ? 1115 GLY B N     1 
ATOM   2446  C  CA    . GLY A  1  316 ? 19.787  48.762  26.915 1.00 40.73  ? 1115 GLY B CA    1 
ATOM   2447  C  C     . GLY A  1  316 ? 18.290  48.802  27.109 1.00 42.12  ? 1115 GLY B C     1 
ATOM   2448  O  O     . GLY A  1  316 ? 17.854  49.126  28.182 1.00 43.55  ? 1115 GLY B O     1 
ATOM   2449  N  N     . ASP A  1  317 ? 17.507  48.472  26.082 1.00 46.78  ? 1116 ASP B N     1 
ATOM   2450  C  CA    . ASP A  1  317 ? 16.103  48.164  26.249 1.00 50.84  ? 1116 ASP B CA    1 
ATOM   2451  C  C     . ASP A  1  317 ? 16.048  46.992  27.224 1.00 47.60  ? 1116 ASP B C     1 
ATOM   2452  O  O     . ASP A  1  317 ? 16.820  46.051  27.104 1.00 45.38  ? 1116 ASP B O     1 
ATOM   2453  C  CB    . ASP A  1  317 ? 15.484  47.703  24.937 1.00 52.38  ? 1116 ASP B CB    1 
ATOM   2454  C  CG    . ASP A  1  317 ? 15.423  48.792  23.916 1.00 71.39  ? 1116 ASP B CG    1 
ATOM   2455  O  OD1   . ASP A  1  317 ? 15.148  49.945  24.301 1.00 90.18  ? 1116 ASP B OD1   1 
ATOM   2456  O  OD2   . ASP A  1  317 ? 15.628  48.522  22.714 1.00 86.19  ? 1116 ASP B OD2   1 
ATOM   2457  N  N     . GLY A  1  318 ? 15.172  47.060  28.206 1.00 44.26  ? 1117 GLY B N     1 
ATOM   2458  C  CA    . GLY A  1  318 ? 15.022  45.944  29.109 1.00 39.62  ? 1117 GLY B CA    1 
ATOM   2459  C  C     . GLY A  1  318 ? 14.136  44.888  28.471 1.00 42.13  ? 1117 GLY B C     1 
ATOM   2460  O  O     . GLY A  1  318 ? 13.565  45.061  27.338 1.00 38.15  ? 1117 GLY B O     1 
ATOM   2461  N  N     . ALA A  1  319 ? 14.057  43.765  29.171 1.00 36.74  ? 1118 ALA B N     1 
ATOM   2462  C  CA    . ALA A  1  319 ? 13.269  42.670  28.678 1.00 38.40  ? 1118 ALA B CA    1 
ATOM   2463  C  C     . ALA A  1  319 ? 11.797  43.072  28.881 1.00 36.86  ? 1118 ALA B C     1 
ATOM   2464  O  O     . ALA A  1  319 ? 11.498  43.954  29.667 1.00 37.70  ? 1118 ALA B O     1 
ATOM   2465  C  CB    . ALA A  1  319 ? 13.614  41.392  29.427 1.00 30.36  ? 1118 ALA B CB    1 
ATOM   2466  N  N     . ALA A  1  320 ? 10.905  42.399  28.175 1.00 35.71  ? 1119 ALA B N     1 
ATOM   2467  C  CA    . ALA A  1  320 ? 9.485   42.535  28.377 1.00 33.07  ? 1119 ALA B CA    1 
ATOM   2468  C  C     . ALA A  1  320 ? 9.186   42.132  29.832 1.00 39.94  ? 1119 ALA B C     1 
ATOM   2469  O  O     . ALA A  1  320 ? 10.008  41.483  30.526 1.00 34.79  ? 1119 ALA B O     1 
ATOM   2470  C  CB    . ALA A  1  320 ? 8.761   41.652  27.413 1.00 30.26  ? 1119 ALA B CB    1 
ATOM   2471  N  N     . ALA A  1  321 ? 8.056   42.597  30.341 1.00 37.13  ? 1120 ALA B N     1 
ATOM   2472  C  CA    . ALA A  1  321 ? 7.632   42.247  31.667 1.00 33.18  ? 1120 ALA B CA    1 
ATOM   2473  C  C     . ALA A  1  321 ? 7.581   40.707  31.718 1.00 35.89  ? 1120 ALA B C     1 
ATOM   2474  O  O     . ALA A  1  321 ? 7.297   40.041  30.690 1.00 28.88  ? 1120 ALA B O     1 
ATOM   2475  C  CB    . ALA A  1  321 ? 6.239   42.816  31.906 1.00 34.76  ? 1120 ALA B CB    1 
ATOM   2476  N  N     . MET A  1  322 ? 7.781   40.155  32.906 1.00 31.43  ? 1121 MET B N     1 
ATOM   2477  C  CA    . MET A  1  322 ? 7.779   38.716  33.068 1.00 36.82  ? 1121 MET B CA    1 
ATOM   2478  C  C     . MET A  1  322 ? 6.436   38.022  32.775 1.00 37.49  ? 1121 MET B C     1 
ATOM   2479  O  O     . MET A  1  322 ? 6.399   36.790  32.643 1.00 31.05  ? 1121 MET B O     1 
ATOM   2480  C  CB    . MET A  1  322 ? 8.374   38.267  34.422 1.00 37.71  ? 1121 MET B CB    1 
ATOM   2481  C  CG    . MET A  1  322 ? 7.556   38.544  35.644 1.00 39.90  ? 1121 MET B CG    1 
ATOM   2482  S  SD    . MET A  1  322 ? 8.378   38.062  37.171 1.00 38.57  ? 1121 MET B SD    1 
ATOM   2483  C  CE    . MET A  1  322 ? 9.406   39.483  37.483 1.00 49.01  ? 1121 MET B CE    1 
ATOM   2484  N  N     . ARG A  1  323 ? 5.371   38.808  32.676 1.00 33.29  ? 1122 ARG B N     1 
ATOM   2485  C  CA    . ARG A  1  323 ? 4.050   38.246  32.351 1.00 35.59  ? 1122 ARG B CA    1 
ATOM   2486  C  C     . ARG A  1  323 ? 4.017   37.802  30.902 1.00 31.68  ? 1122 ARG B C     1 
ATOM   2487  O  O     . ARG A  1  323 ? 3.178   36.995  30.549 1.00 32.14  ? 1122 ARG B O     1 
ATOM   2488  C  CB    . ARG A  1  323 ? 2.907   39.260  32.593 1.00 32.40  ? 1122 ARG B CB    1 
ATOM   2489  C  CG    . ARG A  1  323 ? 3.066   40.564  31.813 1.00 35.08  ? 1122 ARG B CG    1 
ATOM   2490  C  CD    . ARG A  1  323 ? 1.900   41.533  32.020 1.00 36.22  ? 1122 ARG B CD    1 
ATOM   2491  N  NE    . ARG A  1  323 ? 0.675   40.959  31.442 1.00 36.65  ? 1122 ARG B NE    1 
ATOM   2492  C  CZ    . ARG A  1  323 ? -0.489  41.585  31.340 1.00 41.53  ? 1122 ARG B CZ    1 
ATOM   2493  N  NH1   . ARG A  1  323 ? -0.635  42.842  31.765 1.00 38.34  ? 1122 ARG B NH1   1 
ATOM   2494  N  NH2   . ARG A  1  323 ? -1.508  40.935  30.797 1.00 40.66  ? 1122 ARG B NH2   1 
ATOM   2495  N  N     . TYR A  1  324 ? 4.920   38.336  30.079 1.00 28.24  ? 1123 TYR B N     1 
ATOM   2496  C  CA    . TYR A  1  324 ? 4.934   38.016  28.655 1.00 31.79  ? 1123 TYR B CA    1 
ATOM   2497  C  C     . TYR A  1  324 ? 5.977   37.006  28.201 1.00 35.40  ? 1123 TYR B C     1 
ATOM   2498  O  O     . TYR A  1  324 ? 5.754   36.288  27.234 1.00 38.13  ? 1123 TYR B O     1 
ATOM   2499  C  CB    . TYR A  1  324 ? 5.091   39.275  27.807 1.00 31.59  ? 1123 TYR B CB    1 
ATOM   2500  C  CG    . TYR A  1  324 ? 3.987   40.282  28.033 1.00 35.07  ? 1123 TYR B CG    1 
ATOM   2501  C  CD1   . TYR A  1  324 ? 2.635   39.964  27.769 1.00 33.71  ? 1123 TYR B CD1   1 
ATOM   2502  C  CD2   . TYR A  1  324 ? 4.287   41.539  28.522 1.00 33.53  ? 1123 TYR B CD2   1 
ATOM   2503  C  CE1   . TYR A  1  324 ? 1.627   40.884  28.005 1.00 34.64  ? 1123 TYR B CE1   1 
ATOM   2504  C  CE2   . TYR A  1  324 ? 3.283   42.474  28.736 1.00 31.83  ? 1123 TYR B CE2   1 
ATOM   2505  C  CZ    . TYR A  1  324 ? 1.970   42.135  28.479 1.00 34.76  ? 1123 TYR B CZ    1 
ATOM   2506  O  OH    . TYR A  1  324 ? 1.011   43.072  28.689 1.00 40.08  ? 1123 TYR B OH    1 
ATOM   2507  N  N     . THR A  1  325 ? 7.128   36.986  28.856 1.00 38.34  ? 1124 THR B N     1 
ATOM   2508  C  CA    . THR A  1  325 ? 8.225   36.120  28.433 1.00 34.85  ? 1124 THR B CA    1 
ATOM   2509  C  C     . THR A  1  325 ? 8.140   34.698  28.980 1.00 33.40  ? 1124 THR B C     1 
ATOM   2510  O  O     . THR A  1  325 ? 7.520   34.419  30.008 1.00 38.32  ? 1124 THR B O     1 
ATOM   2511  C  CB    . THR A  1  325 ? 9.578   36.727  28.775 1.00 30.69  ? 1124 THR B CB    1 
ATOM   2512  O  OG1   . THR A  1  325 ? 9.669   36.981  30.199 1.00 28.58  ? 1124 THR B OG1   1 
ATOM   2513  C  CG2   . THR A  1  325 ? 9.805   37.973  27.972 1.00 27.44  ? 1124 THR B CG2   1 
ATOM   2514  N  N     . GLU A  1  326 ? 8.786   33.796  28.255 1.00 35.13  ? 1125 GLU B N     1 
ATOM   2515  C  CA    . GLU A  1  326 ? 8.856   32.386  28.633 1.00 36.75  ? 1125 GLU B CA    1 
ATOM   2516  C  C     . GLU A  1  326 ? 10.311  31.968  28.568 1.00 33.16  ? 1125 GLU B C     1 
ATOM   2517  O  O     . GLU A  1  326 ? 11.117  32.639  27.932 1.00 35.83  ? 1125 GLU B O     1 
ATOM   2518  C  CB    . GLU A  1  326 ? 8.005   31.561  27.662 1.00 40.44  ? 1125 GLU B CB    1 
ATOM   2519  C  CG    . GLU A  1  326 ? 6.676   32.204  27.343 1.00 53.56  ? 1125 GLU B CG    1 
ATOM   2520  C  CD    . GLU A  1  326 ? 5.617   31.199  26.971 1.00 66.07  ? 1125 GLU B CD    1 
ATOM   2521  O  OE1   . GLU A  1  326 ? 5.569   30.079  27.538 1.00 71.20  ? 1125 GLU B OE1   1 
ATOM   2522  O  OE2   . GLU A  1  326 ? 4.810   31.558  26.107 1.00 79.16  ? 1125 GLU B OE2   1 
ATOM   2523  N  N     . ALA A  1  327 ? 10.650  30.844  29.205 1.00 30.24  ? 1126 ALA B N     1 
ATOM   2524  C  CA    . ALA A  1  327 ? 12.037  30.437  29.244 1.00 31.96  ? 1126 ALA B CA    1 
ATOM   2525  C  C     . ALA A  1  327 ? 12.206  28.954  29.475 1.00 33.39  ? 1126 ALA B C     1 
ATOM   2526  O  O     . ALA A  1  327 ? 11.279  28.304  29.910 1.00 30.49  ? 1126 ALA B O     1 
ATOM   2527  C  CB    . ALA A  1  327 ? 12.814  31.225  30.303 1.00 26.29  ? 1126 ALA B CB    1 
ATOM   2528  N  N     . ARG A  1  328 ? 13.399  28.443  29.153 1.00 32.82  ? 1127 ARG B N     1 
ATOM   2529  C  CA    . ARG A  1  328 ? 13.807  27.099  29.513 1.00 34.53  ? 1127 ARG B CA    1 
ATOM   2530  C  C     . ARG A  1  328 ? 15.338  27.028  29.466 1.00 36.27  ? 1127 ARG B C     1 
ATOM   2531  O  O     . ARG A  1  328 ? 16.006  27.991  29.096 1.00 35.57  ? 1127 ARG B O     1 
ATOM   2532  C  CB    . ARG A  1  328 ? 13.204  26.067  28.548 1.00 33.89  ? 1127 ARG B CB    1 
ATOM   2533  C  CG    . ARG A  1  328 ? 13.636  26.246  27.089 1.00 34.04  ? 1127 ARG B CG    1 
ATOM   2534  C  CD    . ARG A  1  328 ? 12.821  25.349  26.199 1.00 30.49  ? 1127 ARG B CD    1 
ATOM   2535  N  NE    . ARG A  1  328 ? 13.235  25.597  24.838 1.00 38.01  ? 1127 ARG B NE    1 
ATOM   2536  C  CZ    . ARG A  1  328 ? 12.547  25.229  23.768 1.00 42.17  ? 1127 ARG B CZ    1 
ATOM   2537  N  NH1   . ARG A  1  328 ? 11.412  24.593  23.951 1.00 44.32  ? 1127 ARG B NH1   1 
ATOM   2538  N  NH2   . ARG A  1  328 ? 12.995  25.513  22.526 1.00 34.94  ? 1127 ARG B NH2   1 
ATOM   2539  N  N     . MET A  1  329 ? 15.867  25.875  29.819 1.00 33.37  ? 1128 MET B N     1 
ATOM   2540  C  CA    . MET A  1  329 ? 17.296  25.658  29.808 1.00 32.82  ? 1128 MET B CA    1 
ATOM   2541  C  C     . MET A  1  329 ? 17.770  25.631  28.376 1.00 32.36  ? 1128 MET B C     1 
ATOM   2542  O  O     . MET A  1  329 ? 17.043  25.232  27.496 1.00 33.75  ? 1128 MET B O     1 
ATOM   2543  C  CB    . MET A  1  329 ? 17.621  24.320  30.445 1.00 34.28  ? 1128 MET B CB    1 
ATOM   2544  C  CG    . MET A  1  329 ? 17.495  24.359  31.965 1.00 41.45  ? 1128 MET B CG    1 
ATOM   2545  S  SD    . MET A  1  329 ? 17.846  22.731  32.727 1.00 52.09  ? 1128 MET B SD    1 
ATOM   2546  C  CE    . MET A  1  329 ? 16.313  21.858  32.602 1.00 51.31  ? 1128 MET B CE    1 
ATOM   2547  N  N     . THR A  1  330 ? 18.993  26.042  28.147 1.00 28.16  ? 1129 THR B N     1 
ATOM   2548  C  CA    . THR A  1  330 ? 19.635  25.728  26.921 1.00 25.71  ? 1129 THR B CA    1 
ATOM   2549  C  C     . THR A  1  330 ? 20.198  24.339  27.069 1.00 26.03  ? 1129 THR B C     1 
ATOM   2550  O  O     . THR A  1  330 ? 20.261  23.793  28.128 1.00 30.45  ? 1129 THR B O     1 
ATOM   2551  C  CB    . THR A  1  330 ? 20.788  26.737  26.572 1.00 25.05  ? 1129 THR B CB    1 
ATOM   2552  O  OG1   . THR A  1  330 ? 21.736  26.769  27.629 1.00 22.54  ? 1129 THR B OG1   1 
ATOM   2553  C  CG2   . THR A  1  330 ? 20.225  28.114  26.413 1.00 21.22  ? 1129 THR B CG2   1 
ATOM   2554  N  N     . LYS A  1  331 ? 20.641  23.791  25.971 1.00 31.19  ? 1130 LYS B N     1 
ATOM   2555  C  CA    . LYS A  1  331 ? 21.290  22.510  25.927 1.00 33.98  ? 1130 LYS B CA    1 
ATOM   2556  C  C     . LYS A  1  331 ? 22.568  22.454  26.708 1.00 33.74  ? 1130 LYS B C     1 
ATOM   2557  O  O     . LYS A  1  331 ? 22.810  21.439  27.365 1.00 31.93  ? 1130 LYS B O     1 
ATOM   2558  C  CB    . LYS A  1  331 ? 21.559  22.170  24.456 1.00 34.16  ? 1130 LYS B CB    1 
ATOM   2559  C  CG    . LYS A  1  331 ? 20.331  21.554  23.821 1.00 40.53  ? 1130 LYS B CG    1 
ATOM   2560  C  CD    . LYS A  1  331 ? 20.442  21.610  22.321 1.00 50.36  ? 1130 LYS B CD    1 
ATOM   2561  C  CE    . LYS A  1  331 ? 19.319  20.794  21.717 1.00 54.43  ? 1130 LYS B CE    1 
ATOM   2562  N  NZ    . LYS A  1  331 ? 19.627  20.600  20.279 1.00 56.21  ? 1130 LYS B NZ    1 
ATOM   2563  N  N     . ILE A  1  332 ? 23.383  23.522  26.647 1.00 30.04  ? 1131 ILE B N     1 
ATOM   2564  C  CA    . ILE A  1  332 ? 24.604  23.498  27.392 1.00 28.54  ? 1131 ILE B CA    1 
ATOM   2565  C  C     . ILE A  1  332 ? 24.370  23.560  28.893 1.00 31.98  ? 1131 ILE B C     1 
ATOM   2566  O  O     . ILE A  1  332 ? 25.205  23.068  29.662 1.00 32.92  ? 1131 ILE B O     1 
ATOM   2567  C  CB    . ILE A  1  332 ? 25.616  24.575  26.901 1.00 30.64  ? 1131 ILE B CB    1 
ATOM   2568  C  CG1   . ILE A  1  332 ? 27.042  24.116  27.266 1.00 28.10  ? 1131 ILE B CG1   1 
ATOM   2569  C  CG2   . ILE A  1  332 ? 25.267  26.013  27.403 1.00 23.04  ? 1131 ILE B CG2   1 
ATOM   2570  C  CD1   . ILE A  1  332 ? 28.087  25.052  26.731 1.00 25.56  ? 1131 ILE B CD1   1 
ATOM   2571  N  N     . THR A  1  333 ? 23.257  24.139  29.331 1.00 27.20  ? 1132 THR B N     1 
ATOM   2572  C  CA    . THR A  1  333 ? 22.962  24.193  30.746 1.00 29.63  ? 1132 THR B CA    1 
ATOM   2573  C  C     . THR A  1  333 ? 22.698  22.802  31.321 1.00 31.05  ? 1132 THR B C     1 
ATOM   2574  O  O     . THR A  1  333 ? 22.881  22.594  32.493 1.00 30.25  ? 1132 THR B O     1 
ATOM   2575  C  CB    . THR A  1  333 ? 21.722  25.049  30.955 1.00 35.19  ? 1132 THR B CB    1 
ATOM   2576  O  OG1   . THR A  1  333 ? 22.102  26.396  30.716 1.00 35.79  ? 1132 THR B OG1   1 
ATOM   2577  C  CG2   . THR A  1  333 ? 21.166  24.901  32.372 1.00 30.71  ? 1132 THR B CG2   1 
ATOM   2578  N  N     . LEU A  1  334 ? 22.285  21.863  30.465 1.00 28.97  ? 1133 LEU B N     1 
ATOM   2579  C  CA    . LEU A  1  334 ? 22.134  20.449  30.899 1.00 35.72  ? 1133 LEU B CA    1 
ATOM   2580  C  C     . LEU A  1  334 ? 23.455  19.878  31.359 1.00 30.23  ? 1133 LEU B C     1 
ATOM   2581  O  O     . LEU A  1  334 ? 23.487  19.086  32.274 1.00 32.59  ? 1133 LEU B O     1 
ATOM   2582  C  CB    . LEU A  1  334 ? 21.590  19.553  29.798 1.00 34.98  ? 1133 LEU B CB    1 
ATOM   2583  C  CG    . LEU A  1  334 ? 20.147  19.779  29.345 1.00 42.38  ? 1133 LEU B CG    1 
ATOM   2584  C  CD1   . LEU A  1  334 ? 19.900  18.983  28.067 1.00 38.93  ? 1133 LEU B CD1   1 
ATOM   2585  C  CD2   . LEU A  1  334 ? 19.133  19.466  30.452 1.00 38.26  ? 1133 LEU B CD2   1 
ATOM   2586  N  N     . GLU A  1  335 ? 24.531  20.327  30.725 1.00 30.76  ? 1134 GLU B N     1 
ATOM   2587  C  CA    . GLU A  1  335 ? 25.889  19.987  31.199 1.00 30.33  ? 1134 GLU B CA    1 
ATOM   2588  C  C     . GLU A  1  335 ? 26.266  20.578  32.539 1.00 30.33  ? 1134 GLU B C     1 
ATOM   2589  O  O     . GLU A  1  335 ? 27.121  20.021  33.163 1.00 32.45  ? 1134 GLU B O     1 
ATOM   2590  C  CB    . GLU A  1  335 ? 26.939  20.321  30.149 1.00 26.31  ? 1134 GLU B CB    1 
ATOM   2591  C  CG    . GLU A  1  335 ? 26.649  19.715  28.792 1.00 33.92  ? 1134 GLU B CG    1 
ATOM   2592  C  CD    . GLU A  1  335 ? 26.637  18.197  28.833 1.00 34.62  ? 1134 GLU B CD    1 
ATOM   2593  O  OE1   . GLU A  1  335 ? 25.966  17.611  27.950 1.00 41.81  ? 1134 GLU B OE1   1 
ATOM   2594  O  OE2   . GLU A  1  335 ? 27.312  17.631  29.737 1.00 32.97  ? 1134 GLU B OE2   1 
ATOM   2595  N  N     . LEU A  1  336 ? 25.640  21.704  32.958 1.00 26.50  ? 1135 LEU B N     1 
ATOM   2596  C  CA    . LEU A  1  336 ? 25.896  22.242  34.292 1.00 26.84  ? 1135 LEU B CA    1 
ATOM   2597  C  C     . LEU A  1  336 ? 25.253  21.364  35.328 1.00 27.01  ? 1135 LEU B C     1 
ATOM   2598  O  O     . LEU A  1  336 ? 25.793  21.171  36.398 1.00 29.41  ? 1135 LEU B O     1 
ATOM   2599  C  CB    . LEU A  1  336 ? 25.355  23.692  34.449 1.00 26.17  ? 1135 LEU B CB    1 
ATOM   2600  C  CG    . LEU A  1  336 ? 26.131  24.748  33.661 1.00 26.45  ? 1135 LEU B CG    1 
ATOM   2601  C  CD1   . LEU A  1  336 ? 25.446  26.098  33.790 1.00 23.12  ? 1135 LEU B CD1   1 
ATOM   2602  C  CD2   . LEU A  1  336 ? 27.590  24.822  34.120 1.00 26.75  ? 1135 LEU B CD2   1 
ATOM   2603  N  N     . LEU A  1  337 ? 24.083  20.836  34.988 1.00 30.03  ? 1136 LEU B N     1 
ATOM   2604  C  CA    . LEU A  1  337 ? 23.279  20.093  35.947 1.00 30.92  ? 1136 LEU B CA    1 
ATOM   2605  C  C     . LEU A  1  337 ? 23.475  18.583  35.841 1.00 30.54  ? 1136 LEU B C     1 
ATOM   2606  O  O     . LEU A  1  337 ? 22.944  17.841  36.643 1.00 30.31  ? 1136 LEU B O     1 
ATOM   2607  C  CB    . LEU A  1  337 ? 21.794  20.374  35.719 1.00 30.10  ? 1136 LEU B CB    1 
ATOM   2608  C  CG    . LEU A  1  337 ? 21.443  21.822  36.057 1.00 31.48  ? 1136 LEU B CG    1 
ATOM   2609  C  CD1   . LEU A  1  337 ? 20.338  22.213  35.107 1.00 30.56  ? 1136 LEU B CD1   1 
ATOM   2610  C  CD2   . LEU A  1  337 ? 21.045  21.965  37.528 1.00 28.17  ? 1136 LEU B CD2   1 
ATOM   2611  N  N     . ARG A  1  338 ? 24.213  18.140  34.861 1.00 30.63  ? 1137 ARG B N     1 
ATOM   2612  C  CA    . ARG A  1  338 ? 24.441  16.694  34.650 1.00 36.53  ? 1137 ARG B CA    1 
ATOM   2613  C  C     . ARG A  1  338 ? 25.047  16.026  35.881 1.00 34.71  ? 1137 ARG B C     1 
ATOM   2614  O  O     . ARG A  1  338 ? 26.121  16.458  36.376 1.00 35.39  ? 1137 ARG B O     1 
ATOM   2615  C  CB    . ARG A  1  338 ? 25.381  16.542  33.463 1.00 33.07  ? 1137 ARG B CB    1 
ATOM   2616  C  CG    . ARG A  1  338 ? 25.684  15.130  33.050 1.00 35.01  ? 1137 ARG B CG    1 
ATOM   2617  C  CD    . ARG A  1  338 ? 26.255  15.103  31.637 1.00 40.66  ? 1137 ARG B CD    1 
ATOM   2618  N  NE    . ARG A  1  338 ? 27.269  14.043  31.499 1.00 49.85  ? 1137 ARG B NE    1 
ATOM   2619  C  CZ    . ARG A  1  338 ? 28.235  14.008  30.586 1.00 48.20  ? 1137 ARG B CZ    1 
ATOM   2620  N  NH1   . ARG A  1  338 ? 28.380  15.011  29.726 1.00 44.85  ? 1137 ARG B NH1   1 
ATOM   2621  N  NH2   . ARG A  1  338 ? 29.059  12.959  30.542 1.00 48.65  ? 1137 ARG B NH2   1 
ATOM   2622  N  N     . ASP A  1  339 ? 24.379  14.981  36.365 1.00 35.47  ? 1138 ASP B N     1 
ATOM   2623  C  CA    . ASP A  1  339 ? 24.884  14.119  37.487 1.00 36.14  ? 1138 ASP B CA    1 
ATOM   2624  C  C     . ASP A  1  339 ? 24.554  14.674  38.830 1.00 32.81  ? 1138 ASP B C     1 
ATOM   2625  O  O     . ASP A  1  339 ? 25.048  14.208  39.842 1.00 34.57  ? 1138 ASP B O     1 
ATOM   2626  C  CB    . ASP A  1  339 ? 26.419  13.907  37.426 1.00 40.03  ? 1138 ASP B CB    1 
ATOM   2627  C  CG    . ASP A  1  339 ? 26.867  13.255  36.148 1.00 40.16  ? 1138 ASP B CG    1 
ATOM   2628  O  OD1   . ASP A  1  339 ? 26.065  12.539  35.567 1.00 39.63  ? 1138 ASP B OD1   1 
ATOM   2629  O  OD2   . ASP A  1  339 ? 28.015  13.432  35.724 1.00 44.09  ? 1138 ASP B OD2   1 
ATOM   2630  N  N     . ILE A  1  340 ? 23.706  15.691  38.868 1.00 36.47  ? 1139 ILE B N     1 
ATOM   2631  C  CA    . ILE A  1  340 ? 23.328  16.343  40.093 1.00 33.13  ? 1139 ILE B CA    1 
ATOM   2632  C  C     . ILE A  1  340 ? 22.583  15.377  40.984 1.00 34.32  ? 1139 ILE B C     1 
ATOM   2633  O  O     . ILE A  1  340 ? 22.620  15.499  42.176 1.00 32.94  ? 1139 ILE B O     1 
ATOM   2634  C  CB    . ILE A  1  340 ? 22.506  17.650  39.814 1.00 34.26  ? 1139 ILE B CB    1 
ATOM   2635  C  CG1   . ILE A  1  340 ? 22.549  18.565  41.030 1.00 34.15  ? 1139 ILE B CG1   1 
ATOM   2636  C  CG2   . ILE A  1  340 ? 21.055  17.389  39.423 1.00 30.26  ? 1139 ILE B CG2   1 
ATOM   2637  C  CD1   . ILE A  1  340 ? 22.238  20.017  40.695 1.00 36.60  ? 1139 ILE B CD1   1 
ATOM   2638  N  N     . ASN A  1  341 ? 21.894  14.404  40.417 1.00 38.90  ? 1140 ASN B N     1 
ATOM   2639  C  CA    . ASN A  1  341 ? 21.194  13.457  41.316 1.00 44.41  ? 1140 ASN B CA    1 
ATOM   2640  C  C     . ASN A  1  341 ? 21.945  12.153  41.554 1.00 44.31  ? 1140 ASN B C     1 
ATOM   2641  O  O     . ASN A  1  341 ? 21.343  11.133  41.823 1.00 44.30  ? 1140 ASN B O     1 
ATOM   2642  C  CB    . ASN A  1  341 ? 19.758  13.235  40.809 1.00 45.78  ? 1140 ASN B CB    1 
ATOM   2643  C  CG    . ASN A  1  341 ? 18.928  14.511  40.927 1.00 49.92  ? 1140 ASN B CG    1 
ATOM   2644  O  OD1   . ASN A  1  341 ? 18.999  15.232  41.965 1.00 46.35  ? 1140 ASN B OD1   1 
ATOM   2645  N  ND2   . ASN A  1  341 ? 18.204  14.848  39.864 1.00 48.92  ? 1140 ASN B ND2   1 
ATOM   2646  N  N     . LYS A  1  342 ? 23.267  12.195  41.438 1.00 37.44  ? 1141 LYS B N     1 
ATOM   2647  C  CA    . LYS A  1  342 ? 24.108  11.015  41.685 1.00 38.63  ? 1141 LYS B CA    1 
ATOM   2648  C  C     . LYS A  1  342 ? 25.093  11.313  42.766 1.00 36.81  ? 1141 LYS B C     1 
ATOM   2649  O  O     . LYS A  1  342 ? 26.249  10.871  42.718 1.00 37.17  ? 1141 LYS B O     1 
ATOM   2650  C  CB    . LYS A  1  342 ? 24.818  10.607  40.427 1.00 36.19  ? 1141 LYS B CB    1 
ATOM   2651  C  CG    . LYS A  1  342 ? 23.802  10.323  39.355 1.00 43.69  ? 1141 LYS B CG    1 
ATOM   2652  C  CD    . LYS A  1  342 ? 24.445  9.917   38.058 1.00 49.03  ? 1141 LYS B CD    1 
ATOM   2653  C  CE    . LYS A  1  342 ? 23.392  9.422   37.095 1.00 56.17  ? 1141 LYS B CE    1 
ATOM   2654  N  NZ    . LYS A  1  342 ? 23.644  10.077  35.775 1.00 54.98  ? 1141 LYS B NZ    1 
ATOM   2655  N  N     . ASP A  1  343 ? 24.642  12.107  43.726 1.00 33.44  ? 1142 ASP B N     1 
ATOM   2656  C  CA    . ASP A  1  343 ? 25.431  12.423  44.883 1.00 38.91  ? 1142 ASP B CA    1 
ATOM   2657  C  C     . ASP A  1  343 ? 26.849  12.925  44.517 1.00 39.07  ? 1142 ASP B C     1 
ATOM   2658  O  O     . ASP A  1  343 ? 27.871  12.505  45.088 1.00 41.83  ? 1142 ASP B O     1 
ATOM   2659  C  CB    . ASP A  1  343 ? 25.451  11.207  45.794 1.00 38.21  ? 1142 ASP B CB    1 
ATOM   2660  C  CG    . ASP A  1  343 ? 26.215  11.444  47.079 1.00 44.60  ? 1142 ASP B CG    1 
ATOM   2661  O  OD1   . ASP A  1  343 ? 26.138  12.551  47.655 1.00 46.22  ? 1142 ASP B OD1   1 
ATOM   2662  O  OD2   . ASP A  1  343 ? 26.932  10.513  47.491 1.00 48.39  ? 1142 ASP B OD2   1 
ATOM   2663  N  N     . THR A  1  344 ? 26.894  13.777  43.512 1.00 34.25  ? 1143 THR B N     1 
ATOM   2664  C  CA    . THR A  1  344 ? 28.149  14.392  43.066 1.00 36.25  ? 1143 THR B CA    1 
ATOM   2665  C  C     . THR A  1  344 ? 28.459  15.715  43.805 1.00 38.33  ? 1143 THR B C     1 
ATOM   2666  O  O     . THR A  1  344 ? 29.619  16.129  43.904 1.00 37.40  ? 1143 THR B O     1 
ATOM   2667  C  CB    . THR A  1  344 ? 28.109  14.706  41.575 1.00 33.20  ? 1143 THR B CB    1 
ATOM   2668  O  OG1   . THR A  1  344 ? 26.895  15.396  41.300 1.00 33.31  ? 1143 THR B OG1   1 
ATOM   2669  C  CG2   . THR A  1  344 ? 28.220  13.431  40.760 1.00 32.20  ? 1143 THR B CG2   1 
ATOM   2670  N  N     . ILE A  1  345 ? 27.422  16.371  44.313 1.00 37.29  ? 1144 ILE B N     1 
ATOM   2671  C  CA    . ILE A  1  345 ? 27.580  17.666  44.999 1.00 35.60  ? 1144 ILE B CA    1 
ATOM   2672  C  C     . ILE A  1  345 ? 26.768  17.649  46.268 1.00 35.43  ? 1144 ILE B C     1 
ATOM   2673  O  O     . ILE A  1  345 ? 25.770  16.938  46.367 1.00 38.73  ? 1144 ILE B O     1 
ATOM   2674  C  CB    . ILE A  1  345 ? 27.191  18.888  44.067 1.00 31.15  ? 1144 ILE B CB    1 
ATOM   2675  C  CG1   . ILE A  1  345 ? 25.755  18.756  43.546 1.00 29.49  ? 1144 ILE B CG1   1 
ATOM   2676  C  CG2   . ILE A  1  345 ? 28.112  18.927  42.840 1.00 24.53  ? 1144 ILE B CG2   1 
ATOM   2677  C  CD1   . ILE A  1  345 ? 24.676  19.271  44.462 1.00 31.95  ? 1144 ILE B CD1   1 
ATOM   2678  N  N     . ASP A  1  346 ? 27.188  18.440  47.238 1.00 30.99  ? 1145 ASP B N     1 
ATOM   2679  C  CA    . ASP A  1  346 ? 26.465  18.504  48.499 1.00 33.56  ? 1145 ASP B CA    1 
ATOM   2680  C  C     . ASP A  1  346 ? 25.233  19.379  48.434 1.00 40.38  ? 1145 ASP B C     1 
ATOM   2681  O  O     . ASP A  1  346 ? 25.305  20.538  47.989 1.00 38.76  ? 1145 ASP B O     1 
ATOM   2682  C  CB    . ASP A  1  346 ? 27.387  19.018  49.577 1.00 33.14  ? 1145 ASP B CB    1 
ATOM   2683  C  CG    . ASP A  1  346 ? 28.514  18.045  49.888 1.00 39.87  ? 1145 ASP B CG    1 
ATOM   2684  O  OD1   . ASP A  1  346 ? 28.538  16.866  49.395 1.00 42.14  ? 1145 ASP B OD1   1 
ATOM   2685  O  OD2   . ASP A  1  346 ? 29.407  18.471  50.631 1.00 47.31  ? 1145 ASP B OD2   1 
ATOM   2686  N  N     . PHE A  1  347 ? 24.104  18.844  48.880 1.00 36.92  ? 1146 PHE B N     1 
ATOM   2687  C  CA    . PHE A  1  347 ? 22.903  19.656  49.039 1.00 37.70  ? 1146 PHE B CA    1 
ATOM   2688  C  C     . PHE A  1  347 ? 22.863  20.292  50.412 1.00 38.84  ? 1146 PHE B C     1 
ATOM   2689  O  O     . PHE A  1  347 ? 23.440  19.764  51.356 1.00 34.71  ? 1146 PHE B O     1 
ATOM   2690  C  CB    . PHE A  1  347 ? 21.655  18.809  48.836 1.00 34.25  ? 1146 PHE B CB    1 
ATOM   2691  C  CG    . PHE A  1  347 ? 21.335  18.579  47.408 1.00 36.56  ? 1146 PHE B CG    1 
ATOM   2692  C  CD1   . PHE A  1  347 ? 21.862  17.484  46.738 1.00 35.84  ? 1146 PHE B CD1   1 
ATOM   2693  C  CD2   . PHE A  1  347 ? 20.480  19.450  46.721 1.00 35.87  ? 1146 PHE B CD2   1 
ATOM   2694  C  CE1   . PHE A  1  347 ? 21.561  17.262  45.385 1.00 35.63  ? 1146 PHE B CE1   1 
ATOM   2695  C  CE2   . PHE A  1  347 ? 20.183  19.243  45.371 1.00 39.77  ? 1146 PHE B CE2   1 
ATOM   2696  C  CZ    . PHE A  1  347 ? 20.729  18.145  44.695 1.00 36.40  ? 1146 PHE B CZ    1 
ATOM   2697  N  N     . ILE A  1  348 ? 22.168  21.427  50.521 1.00 35.34  ? 1147 ILE B N     1 
ATOM   2698  C  CA    . ILE A  1  348 ? 21.964  22.055  51.814 1.00 36.55  ? 1147 ILE B CA    1 
ATOM   2699  C  C     . ILE A  1  348 ? 20.501  22.402  51.998 1.00 34.58  ? 1147 ILE B C     1 
ATOM   2700  O  O     . ILE A  1  348 ? 19.729  22.432  51.044 1.00 34.21  ? 1147 ILE B O     1 
ATOM   2701  C  CB    . ILE A  1  348 ? 22.826  23.320  51.962 1.00 37.70  ? 1147 ILE B CB    1 
ATOM   2702  C  CG1   . ILE A  1  348 ? 22.467  24.342  50.866 1.00 38.26  ? 1147 ILE B CG1   1 
ATOM   2703  C  CG2   . ILE A  1  348 ? 24.323  22.959  52.032 1.00 34.12  ? 1147 ILE B CG2   1 
ATOM   2704  C  CD1   . ILE A  1  348 ? 23.413  25.514  50.669 1.00 39.25  ? 1147 ILE B CD1   1 
ATOM   2705  N  N     . ASP A  1  349 ? 20.132  22.702  53.233 1.00 36.02  ? 1148 ASP B N     1 
ATOM   2706  C  CA    . ASP A  1  349 ? 18.770  23.134  53.502 1.00 40.13  ? 1148 ASP B CA    1 
ATOM   2707  C  C     . ASP A  1  349 ? 18.571  24.489  52.858 1.00 40.27  ? 1148 ASP B C     1 
ATOM   2708  O  O     . ASP A  1  349 ? 19.539  25.250  52.735 1.00 35.43  ? 1148 ASP B O     1 
ATOM   2709  C  CB    . ASP A  1  349 ? 18.556  23.269  55.008 1.00 40.65  ? 1148 ASP B CB    1 
ATOM   2710  C  CG    . ASP A  1  349 ? 18.331  21.935  55.681 1.00 42.23  ? 1148 ASP B CG    1 
ATOM   2711  O  OD1   . ASP A  1  349 ? 18.256  20.910  54.977 1.00 43.50  ? 1148 ASP B OD1   1 
ATOM   2712  O  OD2   . ASP A  1  349 ? 18.208  21.941  56.919 1.00 49.15  ? 1148 ASP B OD2   1 
ATOM   2713  N  N     . ASN A  1  350 ? 17.341  24.793  52.453 1.00 38.73  ? 1149 ASN B N     1 
ATOM   2714  C  CA    . ASN A  1  350 ? 17.074  26.102  51.895 1.00 42.27  ? 1149 ASN B CA    1 
ATOM   2715  C  C     . ASN A  1  350 ? 16.979  27.151  53.023 1.00 38.31  ? 1149 ASN B C     1 
ATOM   2716  O  O     . ASN A  1  350 ? 17.277  26.869  54.169 1.00 39.46  ? 1149 ASN B O     1 
ATOM   2717  C  CB    . ASN A  1  350 ? 15.817  26.052  51.035 1.00 41.17  ? 1149 ASN B CB    1 
ATOM   2718  C  CG    . ASN A  1  350 ? 14.559  25.974  51.857 1.00 36.57  ? 1149 ASN B CG    1 
ATOM   2719  O  OD1   . ASN A  1  350 ? 14.552  25.463  52.976 1.00 38.46  ? 1149 ASN B OD1   1 
ATOM   2720  N  ND2   . ASN A  1  350 ? 13.480  26.489  51.304 1.00 41.29  ? 1149 ASN B ND2   1 
ATOM   2721  N  N     . TYR A  1  351 ? 16.549  28.359  52.691 1.00 39.01  ? 1150 TYR B N     1 
ATOM   2722  C  CA    . TYR A  1  351 ? 16.495  29.437  53.690 1.00 35.98  ? 1150 TYR B CA    1 
ATOM   2723  C  C     . TYR A  1  351 ? 15.481  29.179  54.806 1.00 40.14  ? 1150 TYR B C     1 
ATOM   2724  O  O     . TYR A  1  351 ? 15.686  29.652  55.895 1.00 44.83  ? 1150 TYR B O     1 
ATOM   2725  C  CB    . TYR A  1  351 ? 16.195  30.806  53.043 1.00 36.26  ? 1150 TYR B CB    1 
ATOM   2726  C  CG    . TYR A  1  351 ? 14.822  30.925  52.430 1.00 33.68  ? 1150 TYR B CG    1 
ATOM   2727  C  CD1   . TYR A  1  351 ? 14.496  30.336  51.181 1.00 31.94  ? 1150 TYR B CD1   1 
ATOM   2728  C  CD2   . TYR A  1  351 ? 13.823  31.558  53.137 1.00 37.00  ? 1150 TYR B CD2   1 
ATOM   2729  C  CE1   . TYR A  1  351 ? 13.201  30.408  50.655 1.00 34.31  ? 1150 TYR B CE1   1 
ATOM   2730  C  CE2   . TYR A  1  351 ? 12.514  31.630  52.639 1.00 34.08  ? 1150 TYR B CE2   1 
ATOM   2731  C  CZ    . TYR A  1  351 ? 12.217  31.083  51.408 1.00 34.59  ? 1150 TYR B CZ    1 
ATOM   2732  O  OH    . TYR A  1  351 ? 10.942  31.223  50.931 1.00 36.89  ? 1150 TYR B OH    1 
ATOM   2733  N  N     . ASP A  1  352 ? 14.382  28.471  54.543 1.00 39.94  ? 1151 ASP B N     1 
ATOM   2734  C  CA    . ASP A  1  352 ? 13.404  28.294  55.610 1.00 39.49  ? 1151 ASP B CA    1 
ATOM   2735  C  C     . ASP A  1  352 ? 13.304  26.842  56.108 1.00 42.57  ? 1151 ASP B C     1 
ATOM   2736  O  O     . ASP A  1  352 ? 12.388  26.512  56.876 1.00 42.72  ? 1151 ASP B O     1 
ATOM   2737  C  CB    . ASP A  1  352 ? 12.021  28.764  55.149 1.00 34.66  ? 1151 ASP B CB    1 
ATOM   2738  C  CG    . ASP A  1  352 ? 11.491  27.960  53.980 1.00 36.17  ? 1151 ASP B CG    1 
ATOM   2739  O  OD1   . ASP A  1  352 ? 12.084  26.893  53.626 1.00 34.89  ? 1151 ASP B OD1   1 
ATOM   2740  O  OD2   . ASP A  1  352 ? 10.474  28.405  53.416 1.00 31.57  ? 1151 ASP B OD2   1 
ATOM   2741  N  N     . GLY A  1  353 ? 14.196  25.970  55.638 1.00 43.21  ? 1152 GLY B N     1 
ATOM   2742  C  CA    . GLY A  1  353 ? 14.160  24.581  56.080 1.00 37.34  ? 1152 GLY B CA    1 
ATOM   2743  C  C     . GLY A  1  353 ? 13.133  23.684  55.385 1.00 41.90  ? 1152 GLY B C     1 
ATOM   2744  O  O     . GLY A  1  353 ? 13.085  22.488  55.662 1.00 54.23  ? 1152 GLY B O     1 
ATOM   2745  N  N     . ASN A  1  354 ? 12.314  24.231  54.490 1.00 40.58  ? 1153 ASN B N     1 
ATOM   2746  C  CA    . ASN A  1  354 ? 11.320  23.419  53.800 1.00 40.03  ? 1153 ASN B CA    1 
ATOM   2747  C  C     . ASN A  1  354 ? 11.789  22.802  52.507 1.00 39.91  ? 1153 ASN B C     1 
ATOM   2748  O  O     . ASN A  1  354 ? 11.030  22.101  51.873 1.00 40.64  ? 1153 ASN B O     1 
ATOM   2749  C  CB    . ASN A  1  354 ? 10.073  24.247  53.504 1.00 45.52  ? 1153 ASN B CB    1 
ATOM   2750  C  CG    . ASN A  1  354 ? 9.329   24.640  54.747 1.00 52.08  ? 1153 ASN B CG    1 
ATOM   2751  O  OD1   . ASN A  1  354 ? 9.299   23.929  55.744 1.00 54.79  ? 1153 ASN B OD1   1 
ATOM   2752  N  ND2   . ASN A  1  354 ? 8.700   25.790  54.676 1.00 57.32  ? 1153 ASN B ND2   1 
ATOM   2753  N  N     . GLU A  1  355 ? 13.010  23.115  52.079 1.00 36.47  ? 1154 GLU B N     1 
ATOM   2754  C  CA    . GLU A  1  355 ? 13.536  22.599  50.821 1.00 34.09  ? 1154 GLU B CA    1 
ATOM   2755  C  C     . GLU A  1  355 ? 15.026  22.319  50.931 1.00 35.08  ? 1154 GLU B C     1 
ATOM   2756  O  O     . GLU A  1  355 ? 15.707  22.737  51.880 1.00 34.58  ? 1154 GLU B O     1 
ATOM   2757  C  CB    . GLU A  1  355 ? 13.295  23.585  49.653 1.00 38.67  ? 1154 GLU B CB    1 
ATOM   2758  C  CG    . GLU A  1  355 ? 11.872  24.133  49.514 1.00 39.97  ? 1154 GLU B CG    1 
ATOM   2759  C  CD    . GLU A  1  355 ? 10.883  23.138  48.928 1.00 38.57  ? 1154 GLU B CD    1 
ATOM   2760  O  OE1   . GLU A  1  355 ? 11.263  22.017  48.497 1.00 37.12  ? 1154 GLU B OE1   1 
ATOM   2761  O  OE2   . GLU A  1  355 ? 9.695   23.509  48.899 1.00 42.33  ? 1154 GLU B OE2   1 
ATOM   2762  N  N     . ARG A  1  356 ? 15.537  21.688  49.886 1.00 38.23  ? 1155 ARG B N     1 
ATOM   2763  C  CA    . ARG A  1  356 ? 16.968  21.398  49.763 1.00 39.04  ? 1155 ARG B CA    1 
ATOM   2764  C  C     . ARG A  1  356 ? 17.408  22.043  48.478 1.00 39.52  ? 1155 ARG B C     1 
ATOM   2765  O  O     . ARG A  1  356 ? 16.684  22.013  47.446 1.00 37.51  ? 1155 ARG B O     1 
ATOM   2766  C  CB    . ARG A  1  356 ? 17.235  19.877  49.706 1.00 37.80  ? 1155 ARG B CB    1 
ATOM   2767  C  CG    . ARG A  1  356 ? 16.828  19.134  50.978 1.00 38.10  ? 1155 ARG B CG    1 
ATOM   2768  C  CD    . ARG A  1  356 ? 17.787  19.372  52.126 1.00 43.49  ? 1155 ARG B CD    1 
ATOM   2769  N  NE    . ARG A  1  356 ? 18.949  18.515  51.992 1.00 47.55  ? 1155 ARG B NE    1 
ATOM   2770  C  CZ    . ARG A  1  356 ? 20.010  18.554  52.797 1.00 51.37  ? 1155 ARG B CZ    1 
ATOM   2771  N  NH1   . ARG A  1  356 ? 20.066  19.409  53.819 1.00 55.59  ? 1155 ARG B NH1   1 
ATOM   2772  N  NH2   . ARG A  1  356 ? 21.025  17.715  52.576 1.00 47.71  ? 1155 ARG B NH2   1 
ATOM   2773  N  N     . GLU A  1  357 ? 18.614  22.592  48.484 1.00 34.42  ? 1156 GLU B N     1 
ATOM   2774  C  CA    . GLU A  1  357 ? 19.143  23.173  47.255 1.00 33.61  ? 1156 GLU B CA    1 
ATOM   2775  C  C     . GLU A  1  357 ? 20.602  22.755  47.102 1.00 33.69  ? 1156 GLU B C     1 
ATOM   2776  O  O     . GLU A  1  357 ? 21.248  22.379  48.091 1.00 31.52  ? 1156 GLU B O     1 
ATOM   2777  C  CB    . GLU A  1  357 ? 18.993  24.716  47.291 1.00 29.80  ? 1156 GLU B CB    1 
ATOM   2778  C  CG    . GLU A  1  357 ? 19.777  25.392  48.418 1.00 29.97  ? 1156 GLU B CG    1 
ATOM   2779  C  CD    . GLU A  1  357 ? 19.874  26.933  48.263 1.00 32.60  ? 1156 GLU B CD    1 
ATOM   2780  O  OE1   . GLU A  1  357 ? 19.919  27.633  49.319 1.00 28.24  ? 1156 GLU B OE1   1 
ATOM   2781  O  OE2   . GLU A  1  357 ? 19.952  27.437  47.106 1.00 31.66  ? 1156 GLU B OE2   1 
ATOM   2782  N  N     . PRO A  1  358 ? 21.136  22.847  45.879 1.00 32.33  ? 1157 PRO B N     1 
ATOM   2783  C  CA    . PRO A  1  358 ? 22.539  22.491  45.676 1.00 28.72  ? 1157 PRO B CA    1 
ATOM   2784  C  C     . PRO A  1  358 ? 23.502  23.572  46.163 1.00 31.00  ? 1157 PRO B C     1 
ATOM   2785  O  O     . PRO A  1  358 ? 23.248  24.790  45.957 1.00 28.69  ? 1157 PRO B O     1 
ATOM   2786  C  CB    . PRO A  1  358 ? 22.637  22.378  44.163 1.00 31.92  ? 1157 PRO B CB    1 
ATOM   2787  C  CG    . PRO A  1  358 ? 21.524  23.204  43.610 1.00 30.46  ? 1157 PRO B CG    1 
ATOM   2788  C  CD    . PRO A  1  358 ? 20.409  23.012  44.610 1.00 31.63  ? 1157 PRO B CD    1 
ATOM   2789  N  N     . SER A  1  359 ? 24.591  23.159  46.800 1.00 27.21  ? 1158 SER B N     1 
ATOM   2790  C  CA    . SER A  1  359 ? 25.612  24.093  47.213 1.00 28.00  ? 1158 SER B CA    1 
ATOM   2791  C  C     . SER A  1  359 ? 26.396  24.515  45.982 1.00 28.47  ? 1158 SER B C     1 
ATOM   2792  O  O     . SER A  1  359 ? 26.902  25.616  45.936 1.00 30.30  ? 1158 SER B O     1 
ATOM   2793  C  CB    . SER A  1  359 ? 26.544  23.482  48.259 1.00 28.68  ? 1158 SER B CB    1 
ATOM   2794  O  OG    . SER A  1  359 ? 27.297  22.398  47.682 1.00 31.46  ? 1158 SER B OG    1 
ATOM   2795  N  N     . VAL A  1  360 ? 26.477  23.660  44.977 1.00 29.59  ? 1159 VAL B N     1 
ATOM   2796  C  CA    . VAL A  1  360 ? 27.261  23.969  43.757 1.00 26.06  ? 1159 VAL B CA    1 
ATOM   2797  C  C     . VAL A  1  360 ? 26.746  23.039  42.707 1.00 25.14  ? 1159 VAL B C     1 
ATOM   2798  O  O     . VAL A  1  360 ? 26.177  21.977  43.039 1.00 27.25  ? 1159 VAL B O     1 
ATOM   2799  C  CB    . VAL A  1  360 ? 28.793  23.745  44.029 1.00 29.30  ? 1159 VAL B CB    1 
ATOM   2800  C  CG1   . VAL A  1  360 ? 29.068  22.299  44.400 1.00 31.83  ? 1159 VAL B CG1   1 
ATOM   2801  C  CG2   . VAL A  1  360 ? 29.706  24.217  42.897 1.00 26.41  ? 1159 VAL B CG2   1 
ATOM   2802  N  N     . LEU A  1  361 ? 26.916  23.390  41.438 1.00 26.35  ? 1160 LEU B N     1 
ATOM   2803  C  CA    . LEU A  1  361 ? 26.509  22.494  40.389 1.00 26.98  ? 1160 LEU B CA    1 
ATOM   2804  C  C     . LEU A  1  361 ? 27.664  21.609  39.914 1.00 30.77  ? 1160 LEU B C     1 
ATOM   2805  O  O     . LEU A  1  361 ? 28.831  21.993  40.016 1.00 28.90  ? 1160 LEU B O     1 
ATOM   2806  C  CB    . LEU A  1  361 ? 25.904  23.287  39.230 1.00 29.17  ? 1160 LEU B CB    1 
ATOM   2807  C  CG    . LEU A  1  361 ? 24.647  24.161  39.525 1.00 30.66  ? 1160 LEU B CG    1 
ATOM   2808  C  CD1   . LEU A  1  361 ? 23.984  24.616  38.240 1.00 26.60  ? 1160 LEU B CD1   1 
ATOM   2809  C  CD2   . LEU A  1  361 ? 23.638  23.476  40.453 1.00 28.08  ? 1160 LEU B CD2   1 
ATOM   2810  N  N     . PRO A  1  362 ? 27.344  20.432  39.379 1.00 32.05  ? 1161 PRO B N     1 
ATOM   2811  C  CA    . PRO A  1  362 ? 28.418  19.573  38.856 1.00 32.79  ? 1161 PRO B CA    1 
ATOM   2812  C  C     . PRO A  1  362 ? 29.267  20.272  37.779 1.00 33.50  ? 1161 PRO B C     1 
ATOM   2813  O  O     . PRO A  1  362 ? 30.461  20.044  37.744 1.00 32.70  ? 1161 PRO B O     1 
ATOM   2814  C  CB    . PRO A  1  362 ? 27.645  18.399  38.236 1.00 31.39  ? 1161 PRO B CB    1 
ATOM   2815  C  CG    . PRO A  1  362 ? 26.373  18.307  39.033 1.00 30.65  ? 1161 PRO B CG    1 
ATOM   2816  C  CD    . PRO A  1  362 ? 26.022  19.764  39.328 1.00 31.16  ? 1161 PRO B CD    1 
ATOM   2817  N  N     . ALA A  1  363 ? 28.652  21.132  36.954 1.00 31.15  ? 1162 ALA B N     1 
ATOM   2818  C  CA    . ALA A  1  363 ? 29.358  21.996  36.035 1.00 34.43  ? 1162 ALA B CA    1 
ATOM   2819  C  C     . ALA A  1  363 ? 30.350  21.251  35.109 1.00 39.21  ? 1162 ALA B C     1 
ATOM   2820  O  O     . ALA A  1  363 ? 31.571  21.422  35.229 1.00 43.33  ? 1162 ALA B O     1 
ATOM   2821  C  CB    . ALA A  1  363 ? 30.101  23.085  36.806 1.00 30.31  ? 1162 ALA B CB    1 
ATOM   2822  N  N     . ARG A  1  364 ? 29.834  20.438  34.195 1.00 34.74  ? 1163 ARG B N     1 
ATOM   2823  C  CA    . ARG A  1  364 ? 30.659  19.600  33.338 1.00 31.55  ? 1163 ARG B CA    1 
ATOM   2824  C  C     . ARG A  1  364 ? 31.483  20.363  32.306 1.00 36.61  ? 1163 ARG B C     1 
ATOM   2825  O  O     . ARG A  1  364 ? 32.327  19.758  31.631 1.00 36.03  ? 1163 ARG B O     1 
ATOM   2826  C  CB    . ARG A  1  364 ? 29.837  18.442  32.742 1.00 30.64  ? 1163 ARG B CB    1 
ATOM   2827  C  CG    . ARG A  1  364 ? 29.080  17.604  33.788 1.00 28.31  ? 1163 ARG B CG    1 
ATOM   2828  C  CD    . ARG A  1  364 ? 29.875  17.152  35.011 1.00 34.10  ? 1163 ARG B CD    1 
ATOM   2829  N  NE    . ARG A  1  364 ? 31.145  16.519  34.619 1.00 35.77  ? 1163 ARG B NE    1 
ATOM   2830  C  CZ    . ARG A  1  364 ? 31.243  15.311  34.043 1.00 38.36  ? 1163 ARG B CZ    1 
ATOM   2831  N  NH1   . ARG A  1  364 ? 30.153  14.532  33.901 1.00 28.91  ? 1163 ARG B NH1   1 
ATOM   2832  N  NH2   . ARG A  1  364 ? 32.430  14.911  33.598 1.00 33.75  ? 1163 ARG B NH2   1 
ATOM   2833  N  N     . PHE A  1  365 ? 31.293  21.685  32.204 1.00 38.43  ? 1164 PHE B N     1 
ATOM   2834  C  CA    . PHE A  1  365 ? 32.171  22.555  31.393 1.00 33.04  ? 1164 PHE B CA    1 
ATOM   2835  C  C     . PHE A  1  365 ? 32.661  23.692  32.292 1.00 35.01  ? 1164 PHE B C     1 
ATOM   2836  O  O     . PHE A  1  365 ? 32.016  24.003  33.264 1.00 35.92  ? 1164 PHE B O     1 
ATOM   2837  C  CB    . PHE A  1  365 ? 31.492  23.032  30.105 1.00 28.85  ? 1164 PHE B CB    1 
ATOM   2838  C  CG    . PHE A  1  365 ? 30.433  24.094  30.284 1.00 28.12  ? 1164 PHE B CG    1 
ATOM   2839  C  CD1   . PHE A  1  365 ? 29.098  23.747  30.516 1.00 25.61  ? 1164 PHE B CD1   1 
ATOM   2840  C  CD2   . PHE A  1  365 ? 30.774  25.452  30.173 1.00 24.17  ? 1164 PHE B CD2   1 
ATOM   2841  C  CE1   . PHE A  1  365 ? 28.117  24.746  30.638 1.00 27.31  ? 1164 PHE B CE1   1 
ATOM   2842  C  CE2   . PHE A  1  365 ? 29.800  26.450  30.304 1.00 25.16  ? 1164 PHE B CE2   1 
ATOM   2843  C  CZ    . PHE A  1  365 ? 28.465  26.102  30.566 1.00 24.86  ? 1164 PHE B CZ    1 
ATOM   2844  N  N     . PRO A  1  366 ? 33.840  24.285  32.001 1.00 35.45  ? 1165 PRO B N     1 
ATOM   2845  C  CA    . PRO A  1  366 ? 34.412  25.321  32.878 1.00 33.46  ? 1165 PRO B CA    1 
ATOM   2846  C  C     . PRO A  1  366 ? 33.677  26.657  32.767 1.00 35.21  ? 1165 PRO B C     1 
ATOM   2847  O  O     . PRO A  1  366 ? 34.145  27.589  32.095 1.00 36.93  ? 1165 PRO B O     1 
ATOM   2848  C  CB    . PRO A  1  366 ? 35.862  25.457  32.389 1.00 29.64  ? 1165 PRO B CB    1 
ATOM   2849  C  CG    . PRO A  1  366 ? 35.815  24.993  30.978 1.00 30.04  ? 1165 PRO B CG    1 
ATOM   2850  C  CD    . PRO A  1  366 ? 34.791  23.890  30.949 1.00 31.80  ? 1165 PRO B CD    1 
ATOM   2851  N  N     . ASN A  1  367 ? 32.530  26.746  33.448 1.00 30.57  ? 1166 ASN B N     1 
ATOM   2852  C  CA    . ASN A  1  367 ? 31.646  27.861  33.230 1.00 29.98  ? 1166 ASN B CA    1 
ATOM   2853  C  C     . ASN A  1  367 ? 32.147  29.242  33.759 1.00 26.41  ? 1166 ASN B C     1 
ATOM   2854  O  O     . ASN A  1  367 ? 31.860  30.266  33.175 1.00 26.21  ? 1166 ASN B O     1 
ATOM   2855  C  CB    . ASN A  1  367 ? 30.292  27.511  33.776 1.00 27.80  ? 1166 ASN B CB    1 
ATOM   2856  C  CG    . ASN A  1  367 ? 29.295  28.615  33.546 1.00 26.65  ? 1166 ASN B CG    1 
ATOM   2857  O  OD1   . ASN A  1  367 ? 29.046  29.002  32.412 1.00 27.72  ? 1166 ASN B OD1   1 
ATOM   2858  N  ND2   . ASN A  1  367 ? 28.728  29.147  34.625 1.00 24.31  ? 1166 ASN B ND2   1 
ATOM   2859  N  N     . LEU A  1  368 ? 32.873  29.231  34.862 1.00 28.66  ? 1167 LEU B N     1 
ATOM   2860  C  CA    . LEU A  1  368 ? 33.468  30.448  35.382 1.00 32.31  ? 1167 LEU B CA    1 
ATOM   2861  C  C     . LEU A  1  368 ? 34.174  31.238  34.308 1.00 31.64  ? 1167 LEU B C     1 
ATOM   2862  O  O     . LEU A  1  368 ? 33.788  32.386  34.026 1.00 31.70  ? 1167 LEU B O     1 
ATOM   2863  C  CB    . LEU A  1  368 ? 34.434  30.184  36.539 1.00 28.75  ? 1167 LEU B CB    1 
ATOM   2864  C  CG    . LEU A  1  368 ? 34.959  31.540  37.109 1.00 30.69  ? 1167 LEU B CG    1 
ATOM   2865  C  CD1   . LEU A  1  368 ? 33.920  32.386  37.819 1.00 25.86  ? 1167 LEU B CD1   1 
ATOM   2866  C  CD2   . LEU A  1  368 ? 36.145  31.332  38.012 1.00 27.84  ? 1167 LEU B CD2   1 
ATOM   2867  N  N     . LEU A  1  369 ? 35.168  30.600  33.699 1.00 31.52  ? 1168 LEU B N     1 
ATOM   2868  C  CA    . LEU A  1  369 ? 35.902  31.226  32.588 1.00 28.56  ? 1168 LEU B CA    1 
ATOM   2869  C  C     . LEU A  1  369 ? 35.134  31.349  31.316 1.00 24.71  ? 1168 LEU B C     1 
ATOM   2870  O  O     . LEU A  1  369 ? 35.352  32.307  30.575 1.00 28.62  ? 1168 LEU B O     1 
ATOM   2871  C  CB    . LEU A  1  369 ? 37.248  30.536  32.334 1.00 24.81  ? 1168 LEU B CB    1 
ATOM   2872  C  CG    . LEU A  1  369 ? 38.133  30.600  33.567 1.00 26.96  ? 1168 LEU B CG    1 
ATOM   2873  C  CD1   . LEU A  1  369 ? 39.248  29.573  33.431 1.00 28.72  ? 1168 LEU B CD1   1 
ATOM   2874  C  CD2   . LEU A  1  369 ? 38.698  31.991  33.806 1.00 26.35  ? 1168 LEU B CD2   1 
ATOM   2875  N  N     . ALA A  1  370 ? 34.294  30.355  31.014 1.00 23.42  ? 1169 ALA B N     1 
ATOM   2876  C  CA    . ALA A  1  370 ? 33.590  30.364  29.716 1.00 24.42  ? 1169 ALA B CA    1 
ATOM   2877  C  C     . ALA A  1  370 ? 32.696  31.605  29.599 1.00 25.89  ? 1169 ALA B C     1 
ATOM   2878  O  O     . ALA A  1  370 ? 32.767  32.337  28.652 1.00 26.11  ? 1169 ALA B O     1 
ATOM   2879  C  CB    . ALA A  1  370 ? 32.757  29.109  29.543 1.00 22.76  ? 1169 ALA B CB    1 
ATOM   2880  N  N     . ASN A  1  371 ? 31.904  31.852  30.629 1.00 27.86  ? 1170 ASN B N     1 
ATOM   2881  C  CA    . ASN A  1  371 ? 30.919  32.929  30.607 1.00 30.09  ? 1170 ASN B CA    1 
ATOM   2882  C  C     . ASN A  1  371 ? 31.395  34.139  31.382 1.00 30.36  ? 1170 ASN B C     1 
ATOM   2883  O  O     . ASN A  1  371 ? 30.788  35.175  31.256 1.00 28.63  ? 1170 ASN B O     1 
ATOM   2884  C  CB    . ASN A  1  371 ? 29.551  32.457  31.135 1.00 25.52  ? 1170 ASN B CB    1 
ATOM   2885  C  CG    . ASN A  1  371 ? 28.690  31.872  30.050 1.00 27.56  ? 1170 ASN B CG    1 
ATOM   2886  O  OD1   . ASN A  1  371 ? 28.570  32.454  28.972 1.00 29.19  ? 1170 ASN B OD1   1 
ATOM   2887  N  ND2   . ASN A  1  371 ? 28.091  30.692  30.303 1.00 26.31  ? 1170 ASN B ND2   1 
ATOM   2888  N  N     . GLY A  1  372 ? 32.490  34.013  32.137 1.00 29.64  ? 1171 GLY B N     1 
ATOM   2889  C  CA    . GLY A  1  372 ? 32.991  35.175  32.886 1.00 35.25  ? 1171 GLY B CA    1 
ATOM   2890  C  C     . GLY A  1  372 ? 32.063  35.555  34.039 1.00 35.99  ? 1171 GLY B C     1 
ATOM   2891  O  O     . GLY A  1  372 ? 31.127  34.809  34.393 1.00 36.19  ? 1171 GLY B O     1 
ATOM   2892  N  N     . ALA A  1  373 ? 32.331  36.714  34.625 1.00 31.33  ? 1172 ALA B N     1 
ATOM   2893  C  CA    . ALA A  1  373 ? 31.550  37.197  35.768 1.00 28.53  ? 1172 ALA B CA    1 
ATOM   2894  C  C     . ALA A  1  373 ? 31.834  38.658  36.112 1.00 31.96  ? 1172 ALA B C     1 
ATOM   2895  O  O     . ALA A  1  373 ? 32.997  39.108  36.018 1.00 31.55  ? 1172 ALA B O     1 
ATOM   2896  C  CB    . ALA A  1  373 ? 31.864  36.390  36.979 1.00 29.33  ? 1172 ALA B CB    1 
ATOM   2897  N  N     . SER A  1  374 ? 30.812  39.397  36.555 1.00 30.41  ? 1173 SER B N     1 
ATOM   2898  C  CA    . SER A  1  374 ? 31.086  40.730  37.127 1.00 35.26  ? 1173 SER B CA    1 
ATOM   2899  C  C     . SER A  1  374 ? 30.255  40.903  38.384 1.00 34.01  ? 1173 SER B C     1 
ATOM   2900  O  O     . SER A  1  374 ? 29.061  40.583  38.381 1.00 36.66  ? 1173 SER B O     1 
ATOM   2901  C  CB    . SER A  1  374 ? 30.874  41.860  36.124 1.00 33.09  ? 1173 SER B CB    1 
ATOM   2902  O  OG    . SER A  1  374 ? 29.531  42.022  35.857 1.00 41.66  ? 1173 SER B OG    1 
ATOM   2903  N  N     . GLY A  1  375 ? 30.860  41.395  39.460 1.00 32.15  ? 1174 GLY B N     1 
ATOM   2904  C  CA    . GLY A  1  375 ? 30.073  41.566  40.721 1.00 27.64  ? 1174 GLY B CA    1 
ATOM   2905  C  C     . GLY A  1  375 ? 30.711  42.634  41.574 1.00 29.61  ? 1174 GLY B C     1 
ATOM   2906  O  O     . GLY A  1  375 ? 31.963  42.670  41.749 1.00 32.21  ? 1174 GLY B O     1 
ATOM   2907  N  N     . ILE A  1  376 ? 29.887  43.522  42.091 1.00 27.10  ? 1175 ILE B N     1 
ATOM   2908  C  CA    . ILE A  1  376 ? 30.348  44.451  43.099 1.00 29.19  ? 1175 ILE B CA    1 
ATOM   2909  C  C     . ILE A  1  376 ? 29.979  43.932  44.467 1.00 27.55  ? 1175 ILE B C     1 
ATOM   2910  O  O     . ILE A  1  376 ? 28.801  43.798  44.761 1.00 27.33  ? 1175 ILE B O     1 
ATOM   2911  C  CB    . ILE A  1  376 ? 29.689  45.801  42.908 1.00 29.45  ? 1175 ILE B CB    1 
ATOM   2912  C  CG1   . ILE A  1  376 ? 29.872  46.221  41.431 1.00 29.73  ? 1175 ILE B CG1   1 
ATOM   2913  C  CG2   . ILE A  1  376 ? 30.203  46.802  43.965 1.00 28.41  ? 1175 ILE B CG2   1 
ATOM   2914  C  CD1   . ILE A  1  376 ? 28.812  47.184  40.913 1.00 31.09  ? 1175 ILE B CD1   1 
ATOM   2915  N  N     . ALA A  1  377 ? 30.975  43.612  45.285 1.00 29.32  ? 1176 ALA B N     1 
ATOM   2916  C  CA    . ALA A  1  377 ? 30.661  43.097  46.623 1.00 29.85  ? 1176 ALA B CA    1 
ATOM   2917  C  C     . ALA A  1  377 ? 30.830  44.150  47.703 1.00 29.89  ? 1176 ALA B C     1 
ATOM   2918  O  O     . ALA A  1  377 ? 30.366  45.266  47.542 1.00 29.52  ? 1176 ALA B O     1 
ATOM   2919  C  CB    . ALA A  1  377 ? 31.437  41.801  46.934 1.00 26.22  ? 1176 ALA B CB    1 
ATOM   2920  N  N     . VAL A  1  378 ? 31.470  43.804  48.837 1.00 31.87  ? 1177 VAL B N     1 
ATOM   2921  C  CA    . VAL A  1  378 ? 31.811  44.801  49.827 1.00 27.80  ? 1177 VAL B CA    1 
ATOM   2922  C  C     . VAL A  1  378 ? 33.282  44.544  50.079 1.00 34.59  ? 1177 VAL B C     1 
ATOM   2923  O  O     . VAL A  1  378 ? 33.681  43.394  50.225 1.00 37.52  ? 1177 VAL B O     1 
ATOM   2924  C  CB    . VAL A  1  378 ? 30.984  44.641  51.101 1.00 29.44  ? 1177 VAL B CB    1 
ATOM   2925  C  CG1   . VAL A  1  378 ? 31.378  45.651  52.131 1.00 24.89  ? 1177 VAL B CG1   1 
ATOM   2926  C  CG2   . VAL A  1  378 ? 29.500  44.850  50.875 1.00 28.28  ? 1177 VAL B CG2   1 
ATOM   2927  N  N     . GLY A  1  379 ? 34.113  45.581  50.079 1.00 31.42  ? 1178 GLY B N     1 
ATOM   2928  C  CA    . GLY A  1  379 ? 35.547  45.380  50.291 1.00 28.69  ? 1178 GLY B CA    1 
ATOM   2929  C  C     . GLY A  1  379 ? 36.253  44.927  49.048 1.00 30.91  ? 1178 GLY B C     1 
ATOM   2930  O  O     . GLY A  1  379 ? 37.481  44.939  49.007 1.00 32.94  ? 1178 GLY B O     1 
ATOM   2931  N  N     . MET A  1  380 ? 35.502  44.547  48.019 1.00 32.53  ? 1179 MET B N     1 
ATOM   2932  C  CA    . MET A  1  380 ? 36.141  44.020  46.819 1.00 31.13  ? 1179 MET B CA    1 
ATOM   2933  C  C     . MET A  1  380 ? 35.116  43.902  45.687 1.00 31.64  ? 1179 MET B C     1 
ATOM   2934  O  O     . MET A  1  380 ? 33.911  44.003  45.908 1.00 32.35  ? 1179 MET B O     1 
ATOM   2935  C  CB    . MET A  1  380 ? 36.755  42.625  47.108 1.00 30.38  ? 1179 MET B CB    1 
ATOM   2936  C  CG    . MET A  1  380 ? 35.792  41.671  47.741 1.00 28.07  ? 1179 MET B CG    1 
ATOM   2937  S  SD    . MET A  1  380 ? 36.509  40.043  48.021 1.00 34.41  ? 1179 MET B SD    1 
ATOM   2938  C  CE    . MET A  1  380 ? 37.840  40.378  49.166 1.00 34.92  ? 1179 MET B CE    1 
ATOM   2939  N  N     . ALA A  1  381 ? 35.605  43.666  44.464 1.00 32.84  ? 1180 ALA B N     1 
ATOM   2940  C  CA    . ALA A  1  381 ? 34.715  43.415  43.330 1.00 31.32  ? 1180 ALA B CA    1 
ATOM   2941  C  C     . ALA A  1  381 ? 35.334  42.379  42.444 1.00 33.83  ? 1180 ALA B C     1 
ATOM   2942  O  O     . ALA A  1  381 ? 36.503  42.073  42.616 1.00 34.30  ? 1180 ALA B O     1 
ATOM   2943  C  CB    . ALA A  1  381 ? 34.496  44.684  42.549 1.00 30.32  ? 1180 ALA B CB    1 
ATOM   2944  N  N     . THR A  1  382 ? 34.587  41.854  41.476 1.00 28.54  ? 1181 THR B N     1 
ATOM   2945  C  CA    . THR A  1  382 ? 35.207  40.862  40.592 1.00 29.52  ? 1181 THR B CA    1 
ATOM   2946  C  C     . THR A  1  382 ? 34.875  41.226  39.155 1.00 27.78  ? 1181 THR B C     1 
ATOM   2947  O  O     . THR A  1  382 ? 33.781  41.766  38.863 1.00 27.64  ? 1181 THR B O     1 
ATOM   2948  C  CB    . THR A  1  382 ? 34.735  39.383  40.906 1.00 30.86  ? 1181 THR B CB    1 
ATOM   2949  O  OG1   . THR A  1  382 ? 35.466  38.481  40.089 1.00 30.74  ? 1181 THR B OG1   1 
ATOM   2950  C  CG2   . THR A  1  382 ? 33.212  39.204  40.534 1.00 24.66  ? 1181 THR B CG2   1 
ATOM   2951  N  N     . ASN A  1  383 ? 35.781  40.895  38.255 1.00 24.84  ? 1182 ASN B N     1 
ATOM   2952  C  CA    . ASN A  1  383 ? 35.534  41.161  36.825 1.00 26.67  ? 1182 ASN B CA    1 
ATOM   2953  C  C     . ASN A  1  383 ? 36.308  40.116  36.029 1.00 27.48  ? 1182 ASN B C     1 
ATOM   2954  O  O     . ASN A  1  383 ? 37.524  40.213  35.860 1.00 32.32  ? 1182 ASN B O     1 
ATOM   2955  C  CB    . ASN A  1  383 ? 35.948  42.589  36.454 1.00 28.98  ? 1182 ASN B CB    1 
ATOM   2956  C  CG    . ASN A  1  383 ? 35.142  43.149  35.312 1.00 31.83  ? 1182 ASN B CG    1 
ATOM   2957  O  OD1   . ASN A  1  383 ? 33.990  42.757  35.092 1.00 31.12  ? 1182 ASN B OD1   1 
ATOM   2958  N  ND2   . ASN A  1  383 ? 35.734  44.084  34.573 1.00 30.32  ? 1182 ASN B ND2   1 
ATOM   2959  N  N     . ILE A  1  384 ? 35.619  39.095  35.572 1.00 28.07  ? 1183 ILE B N     1 
ATOM   2960  C  CA    . ILE A  1  384 ? 36.276  38.000  34.846 1.00 27.71  ? 1183 ILE B CA    1 
ATOM   2961  C  C     . ILE A  1  384 ? 35.669  37.945  33.451 1.00 26.64  ? 1183 ILE B C     1 
ATOM   2962  O  O     . ILE A  1  384 ? 34.452  37.782  33.324 1.00 27.35  ? 1183 ILE B O     1 
ATOM   2963  C  CB    . ILE A  1  384 ? 36.010  36.654  35.534 1.00 27.07  ? 1183 ILE B CB    1 
ATOM   2964  C  CG1   . ILE A  1  384 ? 36.523  36.698  36.968 1.00 29.01  ? 1183 ILE B CG1   1 
ATOM   2965  C  CG2   . ILE A  1  384 ? 36.695  35.517  34.743 1.00 31.27  ? 1183 ILE B CG2   1 
ATOM   2966  C  CD1   . ILE A  1  384 ? 36.226  35.469  37.800 1.00 23.80  ? 1183 ILE B CD1   1 
ATOM   2967  N  N     . PRO A  1  385 ? 36.489  38.080  32.417 1.00 25.36  ? 1184 PRO B N     1 
ATOM   2968  C  CA    . PRO A  1  385 ? 35.931  38.075  31.053 1.00 25.05  ? 1184 PRO B CA    1 
ATOM   2969  C  C     . PRO A  1  385 ? 35.626  36.642  30.572 1.00 30.05  ? 1184 PRO B C     1 
ATOM   2970  O  O     . PRO A  1  385 ? 36.174  35.679  31.100 1.00 27.24  ? 1184 PRO B O     1 
ATOM   2971  C  CB    . PRO A  1  385 ? 37.059  38.648  30.224 1.00 23.30  ? 1184 PRO B CB    1 
ATOM   2972  C  CG    . PRO A  1  385 ? 38.311  38.210  30.939 1.00 23.72  ? 1184 PRO B CG    1 
ATOM   2973  C  CD    . PRO A  1  385 ? 37.969  38.174  32.415 1.00 24.98  ? 1184 PRO B CD    1 
ATOM   2974  N  N     . PRO A  1  386 ? 34.714  36.513  29.619 1.00 29.80  ? 1185 PRO B N     1 
ATOM   2975  C  CA    . PRO A  1  386 ? 34.370  35.200  29.043 1.00 28.46  ? 1185 PRO B CA    1 
ATOM   2976  C  C     . PRO A  1  386 ? 35.477  34.680  28.134 1.00 30.39  ? 1185 PRO B C     1 
ATOM   2977  O  O     . PRO A  1  386 ? 36.366  35.442  27.717 1.00 29.35  ? 1185 PRO B O     1 
ATOM   2978  C  CB    . PRO A  1  386 ? 33.146  35.516  28.179 1.00 27.16  ? 1185 PRO B CB    1 
ATOM   2979  C  CG    . PRO A  1  386 ? 33.341  36.981  27.800 1.00 25.63  ? 1185 PRO B CG    1 
ATOM   2980  C  CD    . PRO A  1  386 ? 33.911  37.611  29.038 1.00 26.62  ? 1185 PRO B CD    1 
ATOM   2981  N  N     . HIS A  1  387 ? 35.417  33.397  27.836 1.00 26.19  ? 1186 HIS B N     1 
ATOM   2982  C  CA    . HIS A  1  387 ? 36.441  32.738  27.049 1.00 29.55  ? 1186 HIS B CA    1 
ATOM   2983  C  C     . HIS A  1  387 ? 35.849  31.732  26.064 1.00 34.09  ? 1186 HIS B C     1 
ATOM   2984  O  O     . HIS A  1  387 ? 34.646  31.347  26.166 1.00 34.48  ? 1186 HIS B O     1 
ATOM   2985  C  CB    . HIS A  1  387 ? 37.398  32.019  27.954 1.00 25.82  ? 1186 HIS B CB    1 
ATOM   2986  C  CG    . HIS A  1  387 ? 38.261  32.944  28.732 1.00 28.34  ? 1186 HIS B CG    1 
ATOM   2987  N  ND1   . HIS A  1  387 ? 37.849  33.523  29.924 1.00 32.19  ? 1186 HIS B ND1   1 
ATOM   2988  C  CD2   . HIS A  1  387 ? 39.539  33.350  28.537 1.00 28.87  ? 1186 HIS B CD2   1 
ATOM   2989  C  CE1   . HIS A  1  387 ? 38.816  34.307  30.383 1.00 31.22  ? 1186 HIS B CE1   1 
ATOM   2990  N  NE2   . HIS A  1  387 ? 39.859  34.203  29.575 1.00 27.46  ? 1186 HIS B NE2   1 
ATOM   2991  N  N     . ASN A  1  388 ? 36.682  31.317  25.110 1.00 31.23  ? 1187 ASN B N     1 
ATOM   2992  C  CA    . ASN A  1  388 ? 36.267  30.347  24.123 1.00 32.59  ? 1187 ASN B CA    1 
ATOM   2993  C  C     . ASN A  1  388 ? 36.258  28.946  24.734 1.00 33.35  ? 1187 ASN B C     1 
ATOM   2994  O  O     . ASN A  1  388 ? 37.248  28.499  25.340 1.00 32.34  ? 1187 ASN B O     1 
ATOM   2995  C  CB    . ASN A  1  388 ? 37.169  30.365  22.896 1.00 34.35  ? 1187 ASN B CB    1 
ATOM   2996  C  CG    . ASN A  1  388 ? 36.722  29.337  21.868 1.00 37.80  ? 1187 ASN B CG    1 
ATOM   2997  O  OD1   . ASN A  1  388 ? 37.176  28.196  21.870 1.00 37.95  ? 1187 ASN B OD1   1 
ATOM   2998  N  ND2   . ASN A  1  388 ? 35.793  29.734  21.008 1.00 32.99  ? 1187 ASN B ND2   1 
ATOM   2999  N  N     . LEU A  1  389 ? 35.151  28.241  24.567 1.00 29.57  ? 1188 LEU B N     1 
ATOM   3000  C  CA    . LEU A  1  389 ? 35.026  26.988  25.253 1.00 30.56  ? 1188 LEU B CA    1 
ATOM   3001  C  C     . LEU A  1  389 ? 36.010  25.910  24.716 1.00 28.84  ? 1188 LEU B C     1 
ATOM   3002  O  O     . LEU A  1  389 ? 36.517  25.094  25.477 1.00 32.67  ? 1188 LEU B O     1 
ATOM   3003  C  CB    . LEU A  1  389 ? 33.575  26.515  25.167 1.00 28.19  ? 1188 LEU B CB    1 
ATOM   3004  C  CG    . LEU A  1  389 ? 33.287  25.184  25.829 1.00 26.63  ? 1188 LEU B CG    1 
ATOM   3005  C  CD1   . LEU A  1  389 ? 33.365  25.261  27.348 1.00 24.25  ? 1188 LEU B CD1   1 
ATOM   3006  C  CD2   . LEU A  1  389 ? 31.899  24.783  25.376 1.00 31.71  ? 1188 LEU B CD2   1 
ATOM   3007  N  N     . THR A  1  390 ? 36.217  25.891  23.403 1.00 28.80  ? 1189 THR B N     1 
ATOM   3008  C  CA    . THR A  1  390 ? 37.129  24.957  22.815 1.00 29.67  ? 1189 THR B CA    1 
ATOM   3009  C  C     . THR A  1  390 ? 38.493  25.186  23.399 1.00 29.22  ? 1189 THR B C     1 
ATOM   3010  O  O     . THR A  1  390 ? 39.174  24.225  23.786 1.00 30.64  ? 1189 THR B O     1 
ATOM   3011  C  CB    . THR A  1  390 ? 37.216  25.113  21.271 1.00 34.82  ? 1189 THR B CB    1 
ATOM   3012  O  OG1   . THR A  1  390 ? 35.906  25.130  20.697 1.00 35.38  ? 1189 THR B OG1   1 
ATOM   3013  C  CG2   . THR A  1  390 ? 38.028  23.940  20.639 1.00 29.23  ? 1189 THR B CG2   1 
ATOM   3014  N  N     . GLU A  1  391 ? 38.894  26.456  23.456 1.00 28.46  ? 1190 GLU B N     1 
ATOM   3015  C  CA    . GLU A  1  391 ? 40.200  26.816  24.054 1.00 29.72  ? 1190 GLU B CA    1 
ATOM   3016  C  C     . GLU A  1  391 ? 40.281  26.419  25.505 1.00 29.56  ? 1190 GLU B C     1 
ATOM   3017  O  O     . GLU A  1  391 ? 41.277  25.852  25.926 1.00 38.80  ? 1190 GLU B O     1 
ATOM   3018  C  CB    . GLU A  1  391 ? 40.507  28.322  23.899 1.00 26.65  ? 1190 GLU B CB    1 
ATOM   3019  C  CG    . GLU A  1  391 ? 40.610  28.713  22.435 1.00 25.23  ? 1190 GLU B CG    1 
ATOM   3020  C  CD    . GLU A  1  391 ? 40.932  30.196  22.261 1.00 29.14  ? 1190 GLU B CD    1 
ATOM   3021  O  OE1   . GLU A  1  391 ? 41.265  30.890  23.238 1.00 31.62  ? 1190 GLU B OE1   1 
ATOM   3022  O  OE2   . GLU A  1  391 ? 40.925  30.693  21.138 1.00 29.96  ? 1190 GLU B OE2   1 
ATOM   3023  N  N     . LEU A  1  392 ? 39.260  26.715  26.286 1.00 26.02  ? 1191 LEU B N     1 
ATOM   3024  C  CA    . LEU A  1  392 ? 39.333  26.411  27.739 1.00 26.66  ? 1191 LEU B CA    1 
ATOM   3025  C  C     . LEU A  1  392 ? 39.493  24.909  27.957 1.00 28.25  ? 1191 LEU B C     1 
ATOM   3026  O  O     . LEU A  1  392 ? 40.251  24.498  28.803 1.00 26.10  ? 1191 LEU B O     1 
ATOM   3027  C  CB    . LEU A  1  392 ? 38.085  26.864  28.487 1.00 23.15  ? 1191 LEU B CB    1 
ATOM   3028  C  CG    . LEU A  1  392 ? 37.935  28.387  28.638 1.00 28.70  ? 1191 LEU B CG    1 
ATOM   3029  C  CD1   . LEU A  1  392 ? 36.543  28.637  29.258 1.00 23.73  ? 1191 LEU B CD1   1 
ATOM   3030  C  CD2   . LEU A  1  392 ? 39.108  29.027  29.444 1.00 25.56  ? 1191 LEU B CD2   1 
ATOM   3031  N  N     . ILE A  1  393 ? 38.710  24.096  27.241 1.00 28.75  ? 1192 ILE B N     1 
ATOM   3032  C  CA    . ILE A  1  393 ? 38.762  22.657  27.488 1.00 30.78  ? 1192 ILE B CA    1 
ATOM   3033  C  C     . ILE A  1  393 ? 40.137  22.087  27.076 1.00 30.58  ? 1192 ILE B C     1 
ATOM   3034  O  O     . ILE A  1  393 ? 40.734  21.284  27.791 1.00 35.69  ? 1192 ILE B O     1 
ATOM   3035  C  CB    . ILE A  1  393 ? 37.579  21.963  26.825 1.00 30.95  ? 1192 ILE B CB    1 
ATOM   3036  C  CG1   . ILE A  1  393 ? 36.292  22.296  27.601 1.00 29.94  ? 1192 ILE B CG1   1 
ATOM   3037  C  CG2   . ILE A  1  393 ? 37.806  20.464  26.782 1.00 31.29  ? 1192 ILE B CG2   1 
ATOM   3038  C  CD1   . ILE A  1  393 ? 35.041  21.794  26.920 1.00 30.88  ? 1192 ILE B CD1   1 
ATOM   3039  N  N     . ASN A  1  394 ? 40.650  22.574  25.960 1.00 34.68  ? 1193 ASN B N     1 
ATOM   3040  C  CA    . ASN A  1  394 ? 41.995  22.221  25.564 1.00 37.65  ? 1193 ASN B CA    1 
ATOM   3041  C  C     . ASN A  1  394 ? 43.003  22.572  26.650 1.00 37.79  ? 1193 ASN B C     1 
ATOM   3042  O  O     . ASN A  1  394 ? 43.884  21.746  26.960 1.00 32.46  ? 1193 ASN B O     1 
ATOM   3043  C  CB    . ASN A  1  394 ? 42.334  22.833  24.223 1.00 36.91  ? 1193 ASN B CB    1 
ATOM   3044  C  CG    . ASN A  1  394 ? 41.647  22.111  23.083 1.00 34.69  ? 1193 ASN B CG    1 
ATOM   3045  O  OD1   . ASN A  1  394 ? 41.221  20.976  23.217 1.00 35.24  ? 1193 ASN B OD1   1 
ATOM   3046  N  ND2   . ASN A  1  394 ? 41.565  22.764  21.966 1.00 36.46  ? 1193 ASN B ND2   1 
ATOM   3047  N  N     . GLY A  1  395 ? 42.833  23.745  27.262 1.00 33.41  ? 1194 GLY B N     1 
ATOM   3048  C  CA    . GLY A  1  395 ? 43.676  24.140  28.394 1.00 32.83  ? 1194 GLY B CA    1 
ATOM   3049  C  C     . GLY A  1  395 ? 43.578  23.164  29.555 1.00 33.40  ? 1194 GLY B C     1 
ATOM   3050  O  O     . GLY A  1  395 ? 44.604  22.732  30.140 1.00 29.27  ? 1194 GLY B O     1 
ATOM   3051  N  N     . VAL A  1  396 ? 42.359  22.781  29.882 1.00 32.92  ? 1195 VAL B N     1 
ATOM   3052  C  CA    . VAL A  1  396 ? 42.177  21.890  31.011 1.00 33.31  ? 1195 VAL B CA    1 
ATOM   3053  C  C     . VAL A  1  396 ? 42.832  20.520  30.712 1.00 35.06  ? 1195 VAL B C     1 
ATOM   3054  O  O     . VAL A  1  396 ? 43.457  19.907  31.590 1.00 33.74  ? 1195 VAL B O     1 
ATOM   3055  C  CB    . VAL A  1  396 ? 40.674  21.693  31.292 1.00 35.57  ? 1195 VAL B CB    1 
ATOM   3056  C  CG1   . VAL A  1  396 ? 40.503  20.602  32.350 1.00 27.04  ? 1195 VAL B CG1   1 
ATOM   3057  C  CG2   . VAL A  1  396 ? 40.067  23.006  31.762 1.00 29.98  ? 1195 VAL B CG2   1 
ATOM   3058  N  N     . LEU A  1  397 ? 42.675  20.058  29.482 1.00 33.97  ? 1196 LEU B N     1 
ATOM   3059  C  CA    . LEU A  1  397 ? 43.314  18.824  29.019 1.00 34.06  ? 1196 LEU B CA    1 
ATOM   3060  C  C     . LEU A  1  397 ? 44.822  18.878  29.144 1.00 35.05  ? 1196 LEU B C     1 
ATOM   3061  O  O     . LEU A  1  397 ? 45.431  17.944  29.707 1.00 36.33  ? 1196 LEU B O     1 
ATOM   3062  C  CB    . LEU A  1  397 ? 42.910  18.539  27.588 1.00 33.11  ? 1196 LEU B CB    1 
ATOM   3063  C  CG    . LEU A  1  397 ? 41.434  18.115  27.449 1.00 36.77  ? 1196 LEU B CG    1 
ATOM   3064  C  CD1   . LEU A  1  397 ? 41.140  17.980  25.977 1.00 33.26  ? 1196 LEU B CD1   1 
ATOM   3065  C  CD2   . LEU A  1  397 ? 41.021  16.831  28.205 1.00 33.65  ? 1196 LEU B CD2   1 
ATOM   3066  N  N     . SER A  1  398 ? 45.413  19.972  28.658 1.00 37.15  ? 1197 SER B N     1 
ATOM   3067  C  CA    . SER A  1  398 ? 46.856  20.159  28.746 1.00 35.04  ? 1197 SER B CA    1 
ATOM   3068  C  C     . SER A  1  398 ? 47.284  20.156  30.180 1.00 37.40  ? 1197 SER B C     1 
ATOM   3069  O  O     . SER A  1  398 ? 48.286  19.501  30.536 1.00 39.13  ? 1197 SER B O     1 
ATOM   3070  C  CB    . SER A  1  398 ? 47.319  21.429  28.084 1.00 34.61  ? 1197 SER B CB    1 
ATOM   3071  O  OG    . SER A  1  398 ? 47.038  21.405  26.688 1.00 33.91  ? 1197 SER B OG    1 
ATOM   3072  N  N     . LEU A  1  399 ? 46.510  20.839  31.022 1.00 37.16  ? 1198 LEU B N     1 
ATOM   3073  C  CA    . LEU A  1  399 ? 46.835  20.869  32.461 1.00 32.18  ? 1198 LEU B CA    1 
ATOM   3074  C  C     . LEU A  1  399 ? 46.705  19.486  33.075 1.00 33.24  ? 1198 LEU B C     1 
ATOM   3075  O  O     . LEU A  1  399 ? 47.482  19.158  33.972 1.00 32.21  ? 1198 LEU B O     1 
ATOM   3076  C  CB    . LEU A  1  399 ? 45.924  21.859  33.170 1.00 30.64  ? 1198 LEU B CB    1 
ATOM   3077  C  CG    . LEU A  1  399 ? 45.840  21.787  34.701 1.00 37.69  ? 1198 LEU B CG    1 
ATOM   3078  C  CD1   . LEU A  1  399 ? 47.161  22.257  35.299 1.00 34.53  ? 1198 LEU B CD1   1 
ATOM   3079  C  CD2   . LEU A  1  399 ? 44.660  22.559  35.307 1.00 31.84  ? 1198 LEU B CD2   1 
ATOM   3080  N  N     . SER A  1  400 ? 45.720  18.697  32.618 1.00 31.48  ? 1199 SER B N     1 
ATOM   3081  C  CA    . SER A  1  400 ? 45.468  17.399  33.246 1.00 34.62  ? 1199 SER B CA    1 
ATOM   3082  C  C     . SER A  1  400 ? 46.624  16.449  32.946 1.00 32.33  ? 1199 SER B C     1 
ATOM   3083  O  O     . SER A  1  400 ? 46.818  15.505  33.656 1.00 36.95  ? 1199 SER B O     1 
ATOM   3084  C  CB    . SER A  1  400 ? 44.158  16.750  32.791 1.00 31.97  ? 1199 SER B CB    1 
ATOM   3085  O  OG    . SER A  1  400 ? 44.259  16.272  31.406 1.00 32.57  ? 1199 SER B OG    1 
ATOM   3086  N  N     . LYS A  1  401 ? 47.357  16.730  31.893 1.00 35.92  ? 1200 LYS B N     1 
ATOM   3087  C  CA    . LYS A  1  401 ? 48.500  15.934  31.514 1.00 38.19  ? 1200 LYS B CA    1 
ATOM   3088  C  C     . LYS A  1  401 ? 49.798  16.486  32.092 1.00 40.00  ? 1200 LYS B C     1 
ATOM   3089  O  O     . LYS A  1  401 ? 50.838  15.850  31.981 1.00 42.72  ? 1200 LYS B O     1 
ATOM   3090  C  CB    . LYS A  1  401 ? 48.567  15.835  29.974 1.00 35.67  ? 1200 LYS B CB    1 
ATOM   3091  C  CG    . LYS A  1  401 ? 47.462  14.944  29.433 1.00 35.50  ? 1200 LYS B CG    1 
ATOM   3092  C  CD    . LYS A  1  401 ? 47.395  15.077  27.930 1.00 38.22  ? 1200 LYS B CD    1 
ATOM   3093  C  CE    . LYS A  1  401 ? 46.327  14.150  27.337 1.00 47.06  ? 1200 LYS B CE    1 
ATOM   3094  N  NZ    . LYS A  1  401 ? 45.582  14.913  26.274 1.00 47.69  ? 1200 LYS B NZ    1 
ATOM   3095  N  N     . ASN A  1  402 ? 49.751  17.657  32.728 1.00 38.65  ? 1201 ASN B N     1 
ATOM   3096  C  CA    . ASN A  1  402 ? 50.974  18.266  33.255 1.00 35.38  ? 1201 ASN B CA    1 
ATOM   3097  C  C     . ASN A  1  402 ? 50.712  19.313  34.306 1.00 35.19  ? 1201 ASN B C     1 
ATOM   3098  O  O     . ASN A  1  402 ? 50.591  20.500  34.008 1.00 35.04  ? 1201 ASN B O     1 
ATOM   3099  C  CB    . ASN A  1  402 ? 51.837  18.823  32.121 1.00 36.46  ? 1201 ASN B CB    1 
ATOM   3100  C  CG    . ASN A  1  402 ? 53.010  19.667  32.627 1.00 37.07  ? 1201 ASN B CG    1 
ATOM   3101  O  OD1   . ASN A  1  402 ? 53.380  19.604  33.785 1.00 37.76  ? 1201 ASN B OD1   1 
ATOM   3102  N  ND2   . ASN A  1  402 ? 53.564  20.489  31.755 1.00 35.75  ? 1201 ASN B ND2   1 
ATOM   3103  N  N     . PRO A  1  403 ? 50.654  18.874  35.562 1.00 40.65  ? 1202 PRO B N     1 
ATOM   3104  C  CA    . PRO A  1  403 ? 50.389  19.755  36.707 1.00 37.19  ? 1202 PRO B CA    1 
ATOM   3105  C  C     . PRO A  1  403 ? 51.346  20.917  36.731 1.00 40.68  ? 1202 PRO B C     1 
ATOM   3106  O  O     . PRO A  1  403 ? 50.998  21.949  37.285 1.00 43.61  ? 1202 PRO B O     1 
ATOM   3107  C  CB    . PRO A  1  403 ? 50.676  18.875  37.918 1.00 34.24  ? 1202 PRO B CB    1 
ATOM   3108  C  CG    . PRO A  1  403 ? 50.575  17.461  37.426 1.00 38.01  ? 1202 PRO B CG    1 
ATOM   3109  C  CD    . PRO A  1  403 ? 50.938  17.482  35.972 1.00 35.34  ? 1202 PRO B CD    1 
ATOM   3110  N  N     . ASP A  1  404 ? 52.545  20.758  36.169 1.00 39.47  ? 1203 ASP B N     1 
ATOM   3111  C  CA    . ASP A  1  404 ? 53.526  21.857  36.212 1.00 45.37  ? 1203 ASP B CA    1 
ATOM   3112  C  C     . ASP A  1  404 ? 53.463  22.751  35.003 1.00 41.63  ? 1203 ASP B C     1 
ATOM   3113  O  O     . ASP A  1  404 ? 54.368  23.536  34.784 1.00 38.93  ? 1203 ASP B O     1 
ATOM   3114  C  CB    . ASP A  1  404 ? 54.952  21.344  36.348 1.00 50.49  ? 1203 ASP B CB    1 
ATOM   3115  C  CG    . ASP A  1  404 ? 55.177  20.617  37.646 1.00 62.18  ? 1203 ASP B CG    1 
ATOM   3116  O  OD1   . ASP A  1  404 ? 54.818  21.116  38.753 1.00 62.24  ? 1203 ASP B OD1   1 
ATOM   3117  O  OD2   . ASP A  1  404 ? 55.704  19.495  37.553 1.00 72.78  ? 1203 ASP B OD2   1 
ATOM   3118  N  N     . ILE A  1  405 ? 52.417  22.642  34.203 1.00 39.46  ? 1204 ILE B N     1 
ATOM   3119  C  CA    . ILE A  1  405 ? 52.333  23.502  33.055 1.00 38.07  ? 1204 ILE B CA    1 
ATOM   3120  C  C     . ILE A  1  405 ? 52.368  24.994  33.475 1.00 37.97  ? 1204 ILE B C     1 
ATOM   3121  O  O     . ILE A  1  405 ? 51.796  25.376  34.502 1.00 39.72  ? 1204 ILE B O     1 
ATOM   3122  C  CB    . ILE A  1  405 ? 51.068  23.186  32.263 1.00 40.80  ? 1204 ILE B CB    1 
ATOM   3123  C  CG1   . ILE A  1  405 ? 51.102  23.896  30.905 1.00 38.59  ? 1204 ILE B CG1   1 
ATOM   3124  C  CG2   . ILE A  1  405 ? 49.809  23.579  33.075 1.00 38.18  ? 1204 ILE B CG2   1 
ATOM   3125  C  CD1   . ILE A  1  405 ? 49.998  23.430  29.967 1.00 37.56  ? 1204 ILE B CD1   1 
ATOM   3126  N  N     . SER A  1  406 ? 53.036  25.822  32.689 1.00 36.22  ? 1205 SER B N     1 
ATOM   3127  C  CA    . SER A  1  406 ? 53.092  27.273  32.982 1.00 36.12  ? 1205 SER B CA    1 
ATOM   3128  C  C     . SER A  1  406 ? 51.920  28.035  32.312 1.00 36.09  ? 1205 SER B C     1 
ATOM   3129  O  O     . SER A  1  406 ? 51.296  27.539  31.377 1.00 32.49  ? 1205 SER B O     1 
ATOM   3130  C  CB    . SER A  1  406 ? 54.415  27.847  32.457 1.00 30.20  ? 1205 SER B CB    1 
ATOM   3131  O  OG    . SER A  1  406 ? 54.356  27.848  31.033 1.00 39.98  ? 1205 SER B OG    1 
ATOM   3132  N  N     . ILE A  1  407 ? 51.723  29.265  32.736 1.00 36.84  ? 1206 ILE B N     1 
ATOM   3133  C  CA    . ILE A  1  407 ? 50.753  30.182  32.154 1.00 34.02  ? 1206 ILE B CA    1 
ATOM   3134  C  C     . ILE A  1  407 ? 51.021  30.381  30.672 1.00 38.60  ? 1206 ILE B C     1 
ATOM   3135  O  O     . ILE A  1  407 ? 50.088  30.354  29.869 1.00 42.10  ? 1206 ILE B O     1 
ATOM   3136  C  CB    . ILE A  1  407 ? 50.833  31.545  32.895 1.00 36.35  ? 1206 ILE B CB    1 
ATOM   3137  C  CG1   . ILE A  1  407 ? 50.524  31.382  34.388 1.00 36.14  ? 1206 ILE B CG1   1 
ATOM   3138  C  CG2   . ILE A  1  407 ? 49.962  32.623  32.278 1.00 31.98  ? 1206 ILE B CG2   1 
ATOM   3139  C  CD1   . ILE A  1  407 ? 49.202  30.738  34.754 1.00 35.47  ? 1206 ILE B CD1   1 
ATOM   3140  N  N     . ALA A  1  408 ? 52.284  30.594  30.296 1.00 35.08  ? 1207 ALA B N     1 
ATOM   3141  C  CA    . ALA A  1  408 ? 52.633  30.820  28.911 1.00 36.56  ? 1207 ALA B CA    1 
ATOM   3142  C  C     . ALA A  1  408 ? 52.238  29.621  28.040 1.00 36.49  ? 1207 ALA B C     1 
ATOM   3143  O  O     . ALA A  1  408 ? 51.728  29.763  26.941 1.00 38.59  ? 1207 ALA B O     1 
ATOM   3144  C  CB    . ALA A  1  408 ? 54.144  31.078  28.823 1.00 37.88  ? 1207 ALA B CB    1 
ATOM   3145  N  N     . GLU A  1  409 ? 52.477  28.425  28.559 1.00 38.12  ? 1208 GLU B N     1 
ATOM   3146  C  CA    . GLU A  1  409 ? 52.072  27.224  27.858 1.00 40.10  ? 1208 GLU B CA    1 
ATOM   3147  C  C     . GLU A  1  409 ? 50.554  27.111  27.772 1.00 36.52  ? 1208 GLU B C     1 
ATOM   3148  O  O     . GLU A  1  409 ? 50.019  26.756  26.758 1.00 36.86  ? 1208 GLU B O     1 
ATOM   3149  C  CB    . GLU A  1  409 ? 52.626  25.999  28.549 1.00 44.56  ? 1208 GLU B CB    1 
ATOM   3150  C  CG    . GLU A  1  409 ? 54.159  25.942  28.602 1.00 51.51  ? 1208 GLU B CG    1 
ATOM   3151  C  CD    . GLU A  1  409 ? 54.647  24.641  29.208 1.00 55.93  ? 1208 GLU B CD    1 
ATOM   3152  O  OE1   . GLU A  1  409 ? 54.693  23.668  28.403 1.00 60.57  ? 1208 GLU B OE1   1 
ATOM   3153  O  OE2   . GLU A  1  409 ? 54.974  24.598  30.441 1.00 49.33  ? 1208 GLU B OE2   1 
ATOM   3154  N  N     . LEU A  1  410 ? 49.874  27.450  28.852 1.00 33.85  ? 1209 LEU B N     1 
ATOM   3155  C  CA    . LEU A  1  410 ? 48.422  27.409  28.848 1.00 37.73  ? 1209 LEU B CA    1 
ATOM   3156  C  C     . LEU A  1  410 ? 47.889  28.371  27.815 1.00 37.76  ? 1209 LEU B C     1 
ATOM   3157  O  O     . LEU A  1  410 ? 46.898  28.072  27.163 1.00 38.73  ? 1209 LEU B O     1 
ATOM   3158  C  CB    . LEU A  1  410 ? 47.866  27.713  30.227 1.00 33.36  ? 1209 LEU B CB    1 
ATOM   3159  C  CG    . LEU A  1  410 ? 47.872  26.512  31.165 1.00 33.59  ? 1209 LEU B CG    1 
ATOM   3160  C  CD1   . LEU A  1  410 ? 47.684  27.037  32.606 1.00 28.69  ? 1209 LEU B CD1   1 
ATOM   3161  C  CD2   . LEU A  1  410 ? 46.843  25.449  30.780 1.00 27.89  ? 1209 LEU B CD2   1 
ATOM   3162  N  N     . MET A  1  411 ? 48.604  29.465  27.591 1.00 35.88  ? 1210 MET B N     1 
ATOM   3163  C  CA    . MET A  1  411 ? 48.133  30.469  26.659 1.00 36.46  ? 1210 MET B CA    1 
ATOM   3164  C  C     . MET A  1  411 ? 48.265  29.989  25.259 1.00 38.51  ? 1210 MET B C     1 
ATOM   3165  O  O     . MET A  1  411 ? 47.698  30.598  24.365 1.00 39.79  ? 1210 MET B O     1 
ATOM   3166  C  CB    . MET A  1  411 ? 48.859  31.791  26.821 1.00 34.64  ? 1210 MET B CB    1 
ATOM   3167  C  CG    . MET A  1  411 ? 48.378  32.519  28.053 1.00 35.81  ? 1210 MET B CG    1 
ATOM   3168  S  SD    . MET A  1  411 ? 49.174  34.097  28.275 1.00 36.54  ? 1210 MET B SD    1 
ATOM   3169  C  CE    . MET A  1  411 ? 48.783  34.813  26.705 1.00 26.49  ? 1210 MET B CE    1 
ATOM   3170  N  N     . GLU A  1  412 ? 48.979  28.872  25.078 1.00 36.06  ? 1211 GLU B N     1 
ATOM   3171  C  CA    . GLU A  1  412 ? 49.030  28.233  23.754 1.00 35.04  ? 1211 GLU B CA    1 
ATOM   3172  C  C     . GLU A  1  412 ? 47.689  27.581  23.433 1.00 35.77  ? 1211 GLU B C     1 
ATOM   3173  O  O     . GLU A  1  412 ? 47.359  27.408  22.260 1.00 37.26  ? 1211 GLU B O     1 
ATOM   3174  C  CB    . GLU A  1  412 ? 50.149  27.186  23.673 1.00 41.61  ? 1211 GLU B CB    1 
ATOM   3175  C  CG    . GLU A  1  412 ? 51.547  27.725  24.033 1.00 49.01  ? 1211 GLU B CG    1 
ATOM   3176  C  CD    . GLU A  1  412 ? 52.664  26.679  24.010 1.00 51.59  ? 1211 GLU B CD    1 
ATOM   3177  O  OE1   . GLU A  1  412 ? 53.788  27.033  24.397 1.00 59.50  ? 1211 GLU B OE1   1 
ATOM   3178  O  OE2   . GLU A  1  412 ? 52.447  25.498  23.658 1.00 60.65  ? 1211 GLU B OE2   1 
ATOM   3179  N  N     . ASP A  1  413 ? 46.911  27.244  24.454 1.00 33.67  ? 1212 ASP B N     1 
ATOM   3180  C  CA    . ASP A  1  413 ? 45.525  26.842  24.238 1.00 32.67  ? 1212 ASP B CA    1 
ATOM   3181  C  C     . ASP A  1  413 ? 44.584  28.028  24.341 1.00 36.47  ? 1212 ASP B C     1 
ATOM   3182  O  O     . ASP A  1  413 ? 43.770  28.234  23.472 1.00 34.92  ? 1212 ASP B O     1 
ATOM   3183  C  CB    . ASP A  1  413 ? 45.134  25.835  25.267 1.00 32.62  ? 1212 ASP B CB    1 
ATOM   3184  C  CG    . ASP A  1  413 ? 45.807  24.505  25.026 1.00 34.89  ? 1212 ASP B CG    1 
ATOM   3185  O  OD1   . ASP A  1  413 ? 45.690  23.962  23.908 1.00 34.17  ? 1212 ASP B OD1   1 
ATOM   3186  O  OD2   . ASP A  1  413 ? 46.450  23.975  25.937 1.00 36.12  ? 1212 ASP B OD2   1 
ATOM   3187  N  N     . ILE A  1  414 ? 44.721  28.819  25.399 1.00 33.45  ? 1213 ILE B N     1 
ATOM   3188  C  CA    . ILE A  1  414 ? 43.797  29.876  25.707 1.00 33.38  ? 1213 ILE B CA    1 
ATOM   3189  C  C     . ILE A  1  414 ? 44.462  31.181  25.325 1.00 35.56  ? 1213 ILE B C     1 
ATOM   3190  O  O     . ILE A  1  414 ? 45.301  31.707  26.045 1.00 31.90  ? 1213 ILE B O     1 
ATOM   3191  C  CB    . ILE A  1  414 ? 43.531  29.838  27.220 1.00 33.27  ? 1213 ILE B CB    1 
ATOM   3192  C  CG1   . ILE A  1  414 ? 43.008  28.449  27.586 1.00 31.66  ? 1213 ILE B CG1   1 
ATOM   3193  C  CG2   . ILE A  1  414 ? 42.565  30.943  27.673 1.00 29.63  ? 1213 ILE B CG2   1 
ATOM   3194  C  CD1   . ILE A  1  414 ? 42.829  28.226  29.074 1.00 24.58  ? 1213 ILE B CD1   1 
ATOM   3195  N  N     . GLU A  1  415 ? 44.080  31.698  24.182 1.00 34.53  ? 1214 GLU B N     1 
ATOM   3196  C  CA    . GLU A  1  415 ? 44.740  32.859  23.607 1.00 41.08  ? 1214 GLU B CA    1 
ATOM   3197  C  C     . GLU A  1  415 ? 44.420  34.120  24.391 1.00 38.00  ? 1214 GLU B C     1 
ATOM   3198  O  O     . GLU A  1  415 ? 45.245  34.994  24.501 1.00 36.41  ? 1214 GLU B O     1 
ATOM   3199  C  CB    . GLU A  1  415 ? 44.305  33.060  22.163 1.00 44.65  ? 1214 GLU B CB    1 
ATOM   3200  C  CG    . GLU A  1  415 ? 45.014  32.168  21.153 1.00 59.30  ? 1214 GLU B CG    1 
ATOM   3201  C  CD    . GLU A  1  415 ? 44.218  32.000  19.860 1.00 66.82  ? 1214 GLU B CD    1 
ATOM   3202  O  OE1   . GLU A  1  415 ? 43.723  33.004  19.295 1.00 71.18  ? 1214 GLU B OE1   1 
ATOM   3203  O  OE2   . GLU A  1  415 ? 44.080  30.857  19.389 1.00 76.71  ? 1214 GLU B OE2   1 
ATOM   3204  N  N     . GLY A  1  416 ? 43.207  34.199  24.912 1.00 32.99  ? 1215 GLY B N     1 
ATOM   3205  C  CA    . GLY A  1  416 ? 42.743  35.377  25.572 1.00 31.83  ? 1215 GLY B CA    1 
ATOM   3206  C  C     . GLY A  1  416 ? 41.251  35.260  25.762 1.00 33.74  ? 1215 GLY B C     1 
ATOM   3207  O  O     . GLY A  1  416 ? 40.673  34.198  25.538 1.00 31.84  ? 1215 GLY B O     1 
ATOM   3208  N  N     . PRO A  1  417 ? 40.613  36.344  26.186 1.00 32.66  ? 1216 PRO B N     1 
ATOM   3209  C  CA    . PRO A  1  417 ? 39.170  36.370  26.370 1.00 27.56  ? 1216 PRO B CA    1 
ATOM   3210  C  C     . PRO A  1  417 ? 38.519  36.261  25.023 1.00 30.66  ? 1216 PRO B C     1 
ATOM   3211  O  O     . PRO A  1  417 ? 39.138  36.655  24.056 1.00 29.55  ? 1216 PRO B O     1 
ATOM   3212  C  CB    . PRO A  1  417 ? 38.923  37.763  26.902 1.00 28.77  ? 1216 PRO B CB    1 
ATOM   3213  C  CG    . PRO A  1  417 ? 40.171  38.158  27.576 1.00 32.06  ? 1216 PRO B CG    1 
ATOM   3214  C  CD    . PRO A  1  417 ? 41.301  37.449  26.885 1.00 30.01  ? 1216 PRO B CD    1 
ATOM   3215  N  N     . ASP A  1  418 ? 37.292  35.724  24.951 1.00 30.58  ? 1217 ASP B N     1 
ATOM   3216  C  CA    . ASP A  1  418 ? 36.557  35.669  23.718 1.00 26.54  ? 1217 ASP B CA    1 
ATOM   3217  C  C     . ASP A  1  418 ? 35.138  36.180  24.005 1.00 28.17  ? 1217 ASP B C     1 
ATOM   3218  O  O     . ASP A  1  418 ? 34.304  35.481  24.615 1.00 28.34  ? 1217 ASP B O     1 
ATOM   3219  C  CB    . ASP A  1  418 ? 36.557  34.217  23.243 1.00 30.57  ? 1217 ASP B CB    1 
ATOM   3220  C  CG    . ASP A  1  418 ? 35.904  34.055  21.872 1.00 32.44  ? 1217 ASP B CG    1 
ATOM   3221  O  OD1   . ASP A  1  418 ? 35.921  35.065  21.120 1.00 32.31  ? 1217 ASP B OD1   1 
ATOM   3222  O  OD2   . ASP A  1  418 ? 35.385  32.932  21.589 1.00 28.54  ? 1217 ASP B OD2   1 
ATOM   3223  N  N     . PHE A  1  419 ? 34.871  37.421  23.632 1.00 27.01  ? 1218 PHE B N     1 
ATOM   3224  C  CA    . PHE A  1  419 ? 33.626  38.062  24.022 1.00 27.79  ? 1218 PHE B CA    1 
ATOM   3225  C  C     . PHE A  1  419 ? 32.430  37.651  23.171 1.00 29.63  ? 1218 PHE B C     1 
ATOM   3226  O  O     . PHE A  1  419 ? 32.617  37.427  21.949 1.00 26.81  ? 1218 PHE B O     1 
ATOM   3227  C  CB    . PHE A  1  419 ? 33.802  39.584  23.917 1.00 26.52  ? 1218 PHE B CB    1 
ATOM   3228  C  CG    . PHE A  1  419 ? 34.879  40.110  24.785 1.00 27.19  ? 1218 PHE B CG    1 
ATOM   3229  C  CD1   . PHE A  1  419 ? 34.771  40.025  26.209 1.00 26.66  ? 1218 PHE B CD1   1 
ATOM   3230  C  CD2   . PHE A  1  419 ? 36.025  40.660  24.204 1.00 25.86  ? 1218 PHE B CD2   1 
ATOM   3231  C  CE1   . PHE A  1  419 ? 35.788  40.505  27.009 1.00 26.36  ? 1218 PHE B CE1   1 
ATOM   3232  C  CE2   . PHE A  1  419 ? 37.057  41.119  25.009 1.00 29.32  ? 1218 PHE B CE2   1 
ATOM   3233  C  CZ    . PHE A  1  419 ? 36.927  41.055  26.440 1.00 25.25  ? 1218 PHE B CZ    1 
ATOM   3234  N  N     . PRO A  1  420 ? 31.209  37.557  23.787 1.00 30.34  ? 1219 PRO B N     1 
ATOM   3235  C  CA    . PRO A  1  420 ? 30.132  37.141  22.830 1.00 31.13  ? 1219 PRO B CA    1 
ATOM   3236  C  C     . PRO A  1  420 ? 29.974  38.152  21.726 1.00 31.58  ? 1219 PRO B C     1 
ATOM   3237  O  O     . PRO A  1  420 ? 29.530  37.859  20.601 1.00 34.27  ? 1219 PRO B O     1 
ATOM   3238  C  CB    . PRO A  1  420 ? 28.846  37.067  23.717 1.00 31.33  ? 1219 PRO B CB    1 
ATOM   3239  C  CG    . PRO A  1  420 ? 29.175  37.839  24.988 1.00 29.05  ? 1219 PRO B CG    1 
ATOM   3240  C  CD    . PRO A  1  420 ? 30.694  37.662  25.169 1.00 24.30  ? 1219 PRO B CD    1 
ATOM   3241  N  N     . THR A  1  421 ? 30.368  39.375  22.032 1.00 30.02  ? 1220 THR B N     1 
ATOM   3242  C  CA    . THR A  1  421 ? 30.221  40.493  21.100 1.00 30.64  ? 1220 THR B CA    1 
ATOM   3243  C  C     . THR A  1  421 ? 31.365  40.612  20.086 1.00 34.50  ? 1220 THR B C     1 
ATOM   3244  O  O     . THR A  1  421 ? 31.394  41.579  19.309 1.00 32.53  ? 1220 THR B O     1 
ATOM   3245  C  CB    . THR A  1  421 ? 30.100  41.787  21.895 1.00 31.52  ? 1220 THR B CB    1 
ATOM   3246  O  OG1   . THR A  1  421 ? 31.099  41.793  22.928 1.00 32.88  ? 1220 THR B OG1   1 
ATOM   3247  C  CG2   . THR A  1  421 ? 28.715  41.901  22.528 1.00 24.71  ? 1220 THR B CG2   1 
ATOM   3248  N  N     . ALA A  1  422 ? 32.283  39.631  20.076 1.00 26.06  ? 1221 ALA B N     1 
ATOM   3249  C  CA    . ALA A  1  422 ? 33.383  39.608  19.114 1.00 27.88  ? 1221 ALA B CA    1 
ATOM   3250  C  C     . ALA A  1  422 ? 34.337  40.794  19.263 1.00 27.42  ? 1221 ALA B C     1 
ATOM   3251  O  O     . ALA A  1  422 ? 34.768  41.085  20.369 1.00 29.03  ? 1221 ALA B O     1 
ATOM   3252  C  CB    . ALA A  1  422 ? 32.844  39.450  17.682 1.00 22.68  ? 1221 ALA B CB    1 
ATOM   3253  N  N     . GLY A  1  423 ? 34.644  41.484  18.175 1.00 25.40  ? 1222 GLY B N     1 
ATOM   3254  C  CA    . GLY A  1  423 ? 35.527  42.686  18.261 1.00 29.87  ? 1222 GLY B CA    1 
ATOM   3255  C  C     . GLY A  1  423 ? 37.001  42.313  18.262 1.00 30.89  ? 1222 GLY B C     1 
ATOM   3256  O  O     . GLY A  1  423 ? 37.387  41.226  17.859 1.00 29.53  ? 1222 GLY B O     1 
ATOM   3257  N  N     . LEU A  1  424 ? 37.830  43.231  18.732 1.00 34.53  ? 1223 LEU B N     1 
ATOM   3258  C  CA    . LEU A  1  424 ? 39.281  43.059  18.739 1.00 30.47  ? 1223 LEU B CA    1 
ATOM   3259  C  C     . LEU A  1  424 ? 39.830  43.319  20.132 1.00 34.42  ? 1223 LEU B C     1 
ATOM   3260  O  O     . LEU A  1  424 ? 39.292  44.133  20.888 1.00 33.52  ? 1223 LEU B O     1 
ATOM   3261  C  CB    . LEU A  1  424 ? 39.918  44.064  17.806 1.00 34.93  ? 1223 LEU B CB    1 
ATOM   3262  C  CG    . LEU A  1  424 ? 39.910  43.860  16.294 1.00 33.97  ? 1223 LEU B CG    1 
ATOM   3263  C  CD1   . LEU A  1  424 ? 38.541  44.048  15.779 1.00 34.92  ? 1223 LEU B CD1   1 
ATOM   3264  C  CD2   . LEU A  1  424 ? 40.747  45.003  15.777 1.00 36.54  ? 1223 LEU B CD2   1 
ATOM   3265  N  N     . ILE A  1  425 ? 40.891  42.597  20.502 1.00 30.44  ? 1224 ILE B N     1 
ATOM   3266  C  CA    . ILE A  1  425 ? 41.677  42.954  21.627 1.00 32.71  ? 1224 ILE B CA    1 
ATOM   3267  C  C     . ILE A  1  425 ? 43.010  43.396  21.071 1.00 37.42  ? 1224 ILE B C     1 
ATOM   3268  O  O     . ILE A  1  425 ? 43.556  42.736  20.197 1.00 43.81  ? 1224 ILE B O     1 
ATOM   3269  C  CB    . ILE A  1  425 ? 41.865  41.751  22.564 1.00 31.44  ? 1224 ILE B CB    1 
ATOM   3270  C  CG1   . ILE A  1  425 ? 40.604  41.489  23.371 1.00 29.74  ? 1224 ILE B CG1   1 
ATOM   3271  C  CG2   . ILE A  1  425 ? 42.969  42.004  23.570 1.00 29.83  ? 1224 ILE B CG2   1 
ATOM   3272  C  CD1   . ILE A  1  425 ? 40.569  40.096  23.988 1.00 25.56  ? 1224 ILE B CD1   1 
ATOM   3273  N  N     . LEU A  1  426 ? 43.563  44.479  21.582 1.00 40.85  ? 1225 LEU B N     1 
ATOM   3274  C  CA    . LEU A  1  426 ? 44.870  44.969  21.109 1.00 38.57  ? 1225 LEU B CA    1 
ATOM   3275  C  C     . LEU A  1  426 ? 46.016  44.464  21.933 1.00 39.21  ? 1225 LEU B C     1 
ATOM   3276  O  O     . LEU A  1  426 ? 46.197  44.912  23.057 1.00 35.74  ? 1225 LEU B O     1 
ATOM   3277  C  CB    . LEU A  1  426 ? 44.915  46.446  21.311 1.00 34.25  ? 1225 LEU B CB    1 
ATOM   3278  C  CG    . LEU A  1  426 ? 43.802  47.212  20.656 1.00 37.00  ? 1225 LEU B CG    1 
ATOM   3279  C  CD1   . LEU A  1  426 ? 44.060  48.695  20.950 1.00 34.37  ? 1225 LEU B CD1   1 
ATOM   3280  C  CD2   . LEU A  1  426 ? 43.862  46.912  19.166 1.00 37.89  ? 1225 LEU B CD2   1 
ATOM   3281  N  N     . GLY A  1  427 ? 46.816  43.571  21.378 1.00 38.96  ? 1226 GLY B N     1 
ATOM   3282  C  CA    . GLY A  1  427 ? 48.027  43.137  22.064 1.00 35.68  ? 1226 GLY B CA    1 
ATOM   3283  C  C     . GLY A  1  427 ? 47.767  42.035  23.049 1.00 43.47  ? 1226 GLY B C     1 
ATOM   3284  O  O     . GLY A  1  427 ? 46.598  41.763  23.489 1.00 40.13  ? 1226 GLY B O     1 
ATOM   3285  N  N     . LYS A  1  428 ? 48.852  41.376  23.405 1.00 41.58  ? 1227 LYS B N     1 
ATOM   3286  C  CA    . LYS A  1  428 ? 48.727  40.233  24.249 1.00 41.25  ? 1227 LYS B CA    1 
ATOM   3287  C  C     . LYS A  1  428 ? 49.250  40.537  25.657 1.00 35.82  ? 1227 LYS B C     1 
ATOM   3288  O  O     . LYS A  1  428 ? 49.310  39.655  26.534 1.00 38.96  ? 1227 LYS B O     1 
ATOM   3289  C  CB    . LYS A  1  428 ? 49.408  39.068  23.538 1.00 47.60  ? 1227 LYS B CB    1 
ATOM   3290  C  CG    . LYS A  1  428 ? 48.595  37.792  23.593 1.00 53.59  ? 1227 LYS B CG    1 
ATOM   3291  C  CD    . LYS A  1  428 ? 48.629  36.987  22.306 1.00 60.21  ? 1227 LYS B CD    1 
ATOM   3292  C  CE    . LYS A  1  428 ? 47.698  35.768  22.417 1.00 61.37  ? 1227 LYS B CE    1 
ATOM   3293  N  NZ    . LYS A  1  428 ? 47.294  35.290  21.057 1.00 59.53  ? 1227 LYS B NZ    1 
ATOM   3294  N  N     . SER A  1  429 ? 49.649  41.788  25.877 1.00 33.24  ? 1228 SER B N     1 
ATOM   3295  C  CA    . SER A  1  429 ? 50.418  42.071  27.089 1.00 34.88  ? 1228 SER B CA    1 
ATOM   3296  C  C     . SER A  1  429 ? 49.505  42.259  28.335 1.00 35.09  ? 1228 SER B C     1 
ATOM   3297  O  O     . SER A  1  429 ? 49.862  41.857  29.430 1.00 30.88  ? 1228 SER B O     1 
ATOM   3298  C  CB    . SER A  1  429 ? 51.411  43.248  26.885 1.00 39.95  ? 1228 SER B CB    1 
ATOM   3299  O  OG    . SER A  1  429 ? 50.924  44.445  27.493 1.00 48.15  ? 1228 SER B OG    1 
ATOM   3300  N  N     . GLY A  1  430 ? 48.342  42.889  28.165 1.00 33.24  ? 1229 GLY B N     1 
ATOM   3301  C  CA    . GLY A  1  430 ? 47.380  42.934  29.220 1.00 28.92  ? 1229 GLY B CA    1 
ATOM   3302  C  C     . GLY A  1  430 ? 46.755  41.581  29.510 1.00 30.81  ? 1229 GLY B C     1 
ATOM   3303  O  O     . GLY A  1  430 ? 46.469  41.289  30.648 1.00 33.66  ? 1229 GLY B O     1 
ATOM   3304  N  N     . ILE A  1  431 ? 46.533  40.774  28.483 1.00 33.59  ? 1230 ILE B N     1 
ATOM   3305  C  CA    . ILE A  1  431 ? 46.031  39.410  28.653 1.00 34.45  ? 1230 ILE B CA    1 
ATOM   3306  C  C     . ILE A  1  431 ? 47.026  38.609  29.482 1.00 36.59  ? 1230 ILE B C     1 
ATOM   3307  O  O     . ILE A  1  431 ? 46.640  37.861  30.395 1.00 31.99  ? 1230 ILE B O     1 
ATOM   3308  C  CB    . ILE A  1  431 ? 45.871  38.748  27.293 1.00 34.81  ? 1230 ILE B CB    1 
ATOM   3309  C  CG1   . ILE A  1  431 ? 44.715  39.366  26.482 1.00 31.63  ? 1230 ILE B CG1   1 
ATOM   3310  C  CG2   . ILE A  1  431 ? 45.702  37.254  27.442 1.00 33.53  ? 1230 ILE B CG2   1 
ATOM   3311  C  CD1   . ILE A  1  431 ? 44.733  38.902  25.032 1.00 27.34  ? 1230 ILE B CD1   1 
ATOM   3312  N  N     . ARG A  1  432 ? 48.311  38.746  29.157 1.00 33.01  ? 1231 ARG B N     1 
ATOM   3313  C  CA    . ARG A  1  432 ? 49.307  37.984  29.869 1.00 34.83  ? 1231 ARG B CA    1 
ATOM   3314  C  C     . ARG A  1  432 ? 49.411  38.326  31.364 1.00 33.68  ? 1231 ARG B C     1 
ATOM   3315  O  O     . ARG A  1  432 ? 49.548  37.446  32.185 1.00 34.22  ? 1231 ARG B O     1 
ATOM   3316  C  CB    . ARG A  1  432 ? 50.650  38.192  29.196 1.00 39.64  ? 1231 ARG B CB    1 
ATOM   3317  C  CG    . ARG A  1  432 ? 51.748  37.265  29.682 1.00 45.15  ? 1231 ARG B CG    1 
ATOM   3318  C  CD    . ARG A  1  432 ? 52.989  37.356  28.794 1.00 61.08  ? 1231 ARG B CD    1 
ATOM   3319  N  NE    . ARG A  1  432 ? 52.751  37.060  27.365 1.00 64.00  ? 1231 ARG B NE    1 
ATOM   3320  C  CZ    . ARG A  1  432 ? 52.801  37.943  26.367 1.00 65.34  ? 1231 ARG B CZ    1 
ATOM   3321  N  NH1   . ARG A  1  432 ? 53.073  39.250  26.565 1.00 65.97  ? 1231 ARG B NH1   1 
ATOM   3322  N  NH2   . ARG A  1  432 ? 52.582  37.486  25.156 1.00 75.53  ? 1231 ARG B NH2   1 
ATOM   3323  N  N     A ARG A  1  433 ? 49.351  39.607  31.678 0.70 34.24  ? 1232 ARG B N     1 
ATOM   3324  N  N     B ARG A  1  433 ? 49.362  39.619  31.680 0.30 33.00  ? 1232 ARG B N     1 
ATOM   3325  C  CA    A ARG A  1  433 ? 49.424  40.082  33.048 0.70 37.30  ? 1232 ARG B CA    1 
ATOM   3326  C  CA    B ARG A  1  433 ? 49.402  40.147  33.055 0.30 33.44  ? 1232 ARG B CA    1 
ATOM   3327  C  C     A ARG A  1  433 ? 48.197  39.618  33.856 0.70 34.80  ? 1232 ARG B C     1 
ATOM   3328  C  C     B ARG A  1  433 ? 48.204  39.626  33.856 0.30 32.39  ? 1232 ARG B C     1 
ATOM   3329  O  O     A ARG A  1  433 ? 48.312  39.232  35.023 0.70 35.89  ? 1232 ARG B O     1 
ATOM   3330  O  O     B ARG A  1  433 ? 48.346  39.131  34.979 0.30 33.07  ? 1232 ARG B O     1 
ATOM   3331  C  CB    A ARG A  1  433 ? 49.508  41.603  33.037 0.70 38.17  ? 1232 ARG B CB    1 
ATOM   3332  C  CB    B ARG A  1  433 ? 49.402  41.687  32.991 0.30 32.77  ? 1232 ARG B CB    1 
ATOM   3333  C  CG    A ARG A  1  433 ? 49.281  42.233  34.376 0.70 43.10  ? 1232 ARG B CG    1 
ATOM   3334  C  CG    B ARG A  1  433 ? 49.563  42.472  34.278 0.30 34.20  ? 1232 ARG B CG    1 
ATOM   3335  C  CD    A ARG A  1  433 ? 50.140  43.465  34.626 0.70 60.68  ? 1232 ARG B CD    1 
ATOM   3336  C  CD    B ARG A  1  433 ? 49.806  43.968  33.952 0.30 35.52  ? 1232 ARG B CD    1 
ATOM   3337  N  NE    A ARG A  1  433 ? 50.780  43.302  35.942 0.70 61.81  ? 1232 ARG B NE    1 
ATOM   3338  N  NE    B ARG A  1  433 ? 50.160  44.797  35.111 0.30 37.32  ? 1232 ARG B NE    1 
ATOM   3339  C  CZ    A ARG A  1  433 ? 52.081  43.147  36.145 0.70 65.08  ? 1232 ARG B CZ    1 
ATOM   3340  C  CZ    B ARG A  1  433 ? 50.247  46.134  35.117 0.30 39.37  ? 1232 ARG B CZ    1 
ATOM   3341  N  NH1   A ARG A  1  433 ? 52.955  43.221  35.143 0.70 61.54  ? 1232 ARG B NH1   1 
ATOM   3342  N  NH1   B ARG A  1  433 ? 49.994  46.839  34.017 0.30 36.52  ? 1232 ARG B NH1   1 
ATOM   3343  N  NH2   A ARG A  1  433 ? 52.507  42.960  37.379 0.70 70.50  ? 1232 ARG B NH2   1 
ATOM   3344  N  NH2   B ARG A  1  433 ? 50.587  46.773  36.238 0.30 34.78  ? 1232 ARG B NH2   1 
ATOM   3345  N  N     . ALA A  1  434 ? 47.031  39.698  33.238 1.00 30.51  ? 1233 ALA B N     1 
ATOM   3346  C  CA    . ALA A  1  434 ? 45.806  39.231  33.881 1.00 30.42  ? 1233 ALA B CA    1 
ATOM   3347  C  C     . ALA A  1  434 ? 45.846  37.718  34.175 1.00 27.93  ? 1233 ALA B C     1 
ATOM   3348  O  O     . ALA A  1  434 ? 45.461  37.284  35.238 1.00 28.36  ? 1233 ALA B O     1 
ATOM   3349  C  CB    . ALA A  1  434 ? 44.620  39.607  33.000 1.00 29.05  ? 1233 ALA B CB    1 
ATOM   3350  N  N     . TYR A  1  435 ? 46.325  36.934  33.216 1.00 26.48  ? 1234 TYR B N     1 
ATOM   3351  C  CA    . TYR A  1  435 ? 46.465  35.470  33.419 1.00 29.96  ? 1234 TYR B CA    1 
ATOM   3352  C  C     . TYR A  1  435 ? 47.515  35.039  34.417 1.00 33.43  ? 1234 TYR B C     1 
ATOM   3353  O  O     . TYR A  1  435 ? 47.322  34.071  35.132 1.00 29.69  ? 1234 TYR B O     1 
ATOM   3354  C  CB    . TYR A  1  435 ? 46.773  34.778  32.101 1.00 30.48  ? 1234 TYR B CB    1 
ATOM   3355  C  CG    . TYR A  1  435 ? 45.586  34.768  31.182 1.00 29.10  ? 1234 TYR B CG    1 
ATOM   3356  C  CD1   . TYR A  1  435 ? 44.317  35.108  31.666 1.00 29.01  ? 1234 TYR B CD1   1 
ATOM   3357  C  CD2   . TYR A  1  435 ? 45.729  34.366  29.849 1.00 29.42  ? 1234 TYR B CD2   1 
ATOM   3358  C  CE1   . TYR A  1  435 ? 43.214  35.082  30.838 1.00 32.04  ? 1234 TYR B CE1   1 
ATOM   3359  C  CE2   . TYR A  1  435 ? 44.650  34.298  29.022 1.00 28.97  ? 1234 TYR B CE2   1 
ATOM   3360  C  CZ    . TYR A  1  435 ? 43.390  34.655  29.514 1.00 33.22  ? 1234 TYR B CZ    1 
ATOM   3361  O  OH    . TYR A  1  435 ? 42.317  34.627  28.678 1.00 32.18  ? 1234 TYR B OH    1 
ATOM   3362  N  N     . GLU A  1  436 ? 48.598  35.811  34.493 1.00 37.09  ? 1235 GLU B N     1 
ATOM   3363  C  CA    . GLU A  1  436 ? 49.676  35.542  35.440 1.00 34.17  ? 1235 GLU B CA    1 
ATOM   3364  C  C     . GLU A  1  436 ? 49.306  35.999  36.824 1.00 32.61  ? 1235 GLU B C     1 
ATOM   3365  O  O     . GLU A  1  436 ? 49.732  35.396  37.763 1.00 34.68  ? 1235 GLU B O     1 
ATOM   3366  C  CB    . GLU A  1  436 ? 50.961  36.241  35.009 1.00 35.09  ? 1235 GLU B CB    1 
ATOM   3367  C  CG    . GLU A  1  436 ? 51.529  35.793  33.696 1.00 44.58  ? 1235 GLU B CG    1 
ATOM   3368  C  CD    . GLU A  1  436 ? 52.888  36.406  33.412 1.00 58.55  ? 1235 GLU B CD    1 
ATOM   3369  O  OE1   . GLU A  1  436 ? 53.612  35.900  32.531 1.00 73.67  ? 1235 GLU B OE1   1 
ATOM   3370  O  OE2   . GLU A  1  436 ? 53.268  37.394  34.074 1.00 69.59  ? 1235 GLU B OE2   1 
ATOM   3371  N  N     . THR A  1  437 ? 48.543  37.085  36.964 1.00 32.05  ? 1236 THR B N     1 
ATOM   3372  C  CA    . THR A  1  437 ? 48.295  37.616  38.289 1.00 32.52  ? 1236 THR B CA    1 
ATOM   3373  C  C     . THR A  1  437 ? 46.837  37.752  38.699 1.00 36.46  ? 1236 THR B C     1 
ATOM   3374  O  O     . THR A  1  437 ? 46.555  38.027  39.864 1.00 36.60  ? 1236 THR B O     1 
ATOM   3375  C  CB    . THR A  1  437 ? 48.897  39.026  38.427 1.00 32.45  ? 1236 THR B CB    1 
ATOM   3376  O  OG1   . THR A  1  437 ? 48.075  39.938  37.706 1.00 27.54  ? 1236 THR B OG1   1 
ATOM   3377  C  CG2   . THR A  1  437 ? 50.304  39.079  37.833 1.00 27.43  ? 1236 THR B CG2   1 
ATOM   3378  N  N     . GLY A  1  438 ? 45.899  37.616  37.760 1.00 32.85  ? 1237 GLY B N     1 
ATOM   3379  C  CA    . GLY A  1  438 ? 44.505  37.834  38.031 1.00 32.47  ? 1237 GLY B CA    1 
ATOM   3380  C  C     . GLY A  1  438 ? 44.060  39.255  37.855 1.00 35.32  ? 1237 GLY B C     1 
ATOM   3381  O  O     . GLY A  1  438 ? 42.872  39.505  37.977 1.00 28.79  ? 1237 GLY B O     1 
ATOM   3382  N  N     . ARG A  1  439 ? 44.993  40.180  37.594 1.00 31.13  ? 1238 ARG B N     1 
ATOM   3383  C  CA    . ARG A  1  439 ? 44.651  41.589  37.358 1.00 36.09  ? 1238 ARG B CA    1 
ATOM   3384  C  C     . ARG A  1  439 ? 45.309  42.081  36.085 1.00 35.87  ? 1238 ARG B C     1 
ATOM   3385  O  O     . ARG A  1  439 ? 46.481  41.826  35.859 1.00 35.99  ? 1238 ARG B O     1 
ATOM   3386  C  CB    . ARG A  1  439 ? 45.181  42.432  38.490 1.00 33.72  ? 1238 ARG B CB    1 
ATOM   3387  C  CG    . ARG A  1  439 ? 44.829  41.940  39.899 1.00 43.27  ? 1238 ARG B CG    1 
ATOM   3388  C  CD    . ARG A  1  439 ? 43.770  42.780  40.575 1.00 45.97  ? 1238 ARG B CD    1 
ATOM   3389  N  NE    . ARG A  1  439 ? 44.100  44.204  40.492 1.00 57.41  ? 1238 ARG B NE    1 
ATOM   3390  C  CZ    . ARG A  1  439 ? 43.185  45.165  40.292 1.00 63.54  ? 1238 ARG B CZ    1 
ATOM   3391  N  NH1   . ARG A  1  439 ? 43.562  46.419  40.185 1.00 65.96  ? 1238 ARG B NH1   1 
ATOM   3392  N  NH2   . ARG A  1  439 ? 41.886  44.876  40.190 1.00 61.21  ? 1238 ARG B NH2   1 
ATOM   3393  N  N     . GLY A  1  440 ? 44.598  42.807  35.244 1.00 35.38  ? 1239 GLY B N     1 
ATOM   3394  C  CA    . GLY A  1  440 ? 45.247  43.322  34.020 1.00 35.84  ? 1239 GLY B CA    1 
ATOM   3395  C  C     . GLY A  1  440 ? 44.258  44.190  33.304 1.00 37.98  ? 1239 GLY B C     1 
ATOM   3396  O  O     . GLY A  1  440 ? 43.074  44.027  33.455 1.00 38.51  ? 1239 GLY B O     1 
ATOM   3397  N  N     . SER A  1  441 ? 44.723  45.106  32.487 1.00 36.34  ? 1240 SER B N     1 
ATOM   3398  C  CA    . SER A  1  441 ? 43.788  45.866  31.733 1.00 35.25  ? 1240 SER B CA    1 
ATOM   3399  C  C     . SER A  1  441 ? 43.855  45.428  30.290 1.00 34.99  ? 1240 SER B C     1 
ATOM   3400  O  O     . SER A  1  441 ? 44.924  45.306  29.721 1.00 38.04  ? 1240 SER B O     1 
ATOM   3401  C  CB    . SER A  1  441 ? 44.111  47.332  31.921 1.00 36.90  ? 1240 SER B CB    1 
ATOM   3402  O  OG    . SER A  1  441 ? 43.507  48.090  30.900 1.00 40.41  ? 1240 SER B OG    1 
ATOM   3403  N  N     . ILE A  1  442 ? 42.715  45.152  29.699 1.00 35.77  ? 1241 ILE B N     1 
ATOM   3404  C  CA    . ILE A  1  442 ? 42.701  44.628  28.331 1.00 35.20  ? 1241 ILE B CA    1 
ATOM   3405  C  C     . ILE A  1  442 ? 41.957  45.579  27.423 1.00 36.16  ? 1241 ILE B C     1 
ATOM   3406  O  O     . ILE A  1  442 ? 40.771  45.826  27.634 1.00 37.01  ? 1241 ILE B O     1 
ATOM   3407  C  CB    . ILE A  1  442 ? 42.023  43.232  28.285 1.00 35.44  ? 1241 ILE B CB    1 
ATOM   3408  C  CG1   . ILE A  1  442 ? 42.867  42.206  29.067 1.00 37.35  ? 1241 ILE B CG1   1 
ATOM   3409  C  CG2   . ILE A  1  442 ? 41.802  42.757  26.843 1.00 34.63  ? 1241 ILE B CG2   1 
ATOM   3410  C  CD1   . ILE A  1  442 ? 42.261  40.813  29.197 1.00 31.72  ? 1241 ILE B CD1   1 
ATOM   3411  N  N     . GLN A  1  443 ? 42.631  46.093  26.397 1.00 38.71  ? 1242 GLN B N     1 
ATOM   3412  C  CA    . GLN A  1  443 ? 42.026  47.045  25.456 1.00 38.33  ? 1242 GLN B CA    1 
ATOM   3413  C  C     . GLN A  1  443 ? 41.154  46.351  24.410 1.00 36.56  ? 1242 GLN B C     1 
ATOM   3414  O  O     . GLN A  1  443 ? 41.671  45.580  23.612 1.00 32.81  ? 1242 GLN B O     1 
ATOM   3415  C  CB    . GLN A  1  443 ? 43.113  47.833  24.728 1.00 41.90  ? 1242 GLN B CB    1 
ATOM   3416  C  CG    . GLN A  1  443 ? 43.850  48.807  25.607 1.00 45.85  ? 1242 GLN B CG    1 
ATOM   3417  C  CD    . GLN A  1  443 ? 42.908  49.772  26.323 1.00 55.15  ? 1242 GLN B CD    1 
ATOM   3418  O  OE1   . GLN A  1  443 ? 41.971  50.352  25.735 1.00 52.38  ? 1242 GLN B OE1   1 
ATOM   3419  N  NE2   . GLN A  1  443 ? 43.142  49.935  27.609 1.00 56.06  ? 1242 GLN B NE2   1 
ATOM   3420  N  N     . MET A  1  444 ? 39.866  46.666  24.400 1.00 32.61  ? 1243 MET B N     1 
ATOM   3421  C  CA    . MET A  1  444 ? 38.919  46.093  23.423 1.00 32.91  ? 1243 MET B CA    1 
ATOM   3422  C  C     . MET A  1  444 ? 38.592  47.177  22.381 1.00 33.04  ? 1243 MET B C     1 
ATOM   3423  O  O     . MET A  1  444 ? 38.220  48.295  22.729 1.00 34.22  ? 1243 MET B O     1 
ATOM   3424  C  CB    . MET A  1  444 ? 37.598  45.697  24.092 1.00 30.17  ? 1243 MET B CB    1 
ATOM   3425  C  CG    . MET A  1  444 ? 37.696  44.773  25.294 1.00 30.08  ? 1243 MET B CG    1 
ATOM   3426  S  SD    . MET A  1  444 ? 36.032  44.359  25.903 1.00 34.97  ? 1243 MET B SD    1 
ATOM   3427  C  CE    . MET A  1  444 ? 35.492  45.825  26.743 1.00 24.24  ? 1243 MET B CE    1 
ATOM   3428  N  N     . ARG A  1  445 ? 38.644  46.834  21.112 1.00 32.03  ? 1244 ARG B N     1 
ATOM   3429  C  CA    . ARG A  1  445 ? 38.323  47.795  20.091 1.00 32.60  ? 1244 ARG B CA    1 
ATOM   3430  C  C     . ARG A  1  445 ? 37.184  47.301  19.240 1.00 36.74  ? 1244 ARG B C     1 
ATOM   3431  O  O     . ARG A  1  445 ? 37.057  46.094  19.030 1.00 36.05  ? 1244 ARG B O     1 
ATOM   3432  C  CB    . ARG A  1  445 ? 39.550  47.927  19.237 1.00 33.63  ? 1244 ARG B CB    1 
ATOM   3433  C  CG    . ARG A  1  445 ? 39.782  49.322  18.770 1.00 31.68  ? 1244 ARG B CG    1 
ATOM   3434  C  CD    . ARG A  1  445 ? 41.108  49.413  18.083 1.00 31.10  ? 1244 ARG B CD    1 
ATOM   3435  N  NE    . ARG A  1  445 ? 41.889  50.417  18.770 1.00 36.35  ? 1244 ARG B NE    1 
ATOM   3436  C  CZ    . ARG A  1  445 ? 42.924  51.020  18.224 1.00 37.01  ? 1244 ARG B CZ    1 
ATOM   3437  N  NH1   . ARG A  1  445 ? 43.291  50.734  16.991 1.00 34.31  ? 1244 ARG B NH1   1 
ATOM   3438  N  NH2   . ARG A  1  445 ? 43.560  51.940  18.915 1.00 37.74  ? 1244 ARG B NH2   1 
ATOM   3439  N  N     . SER A  1  446 ? 36.349  48.208  18.757 1.00 32.26  ? 1245 SER B N     1 
ATOM   3440  C  CA    . SER A  1  446 ? 35.305  47.845  17.807 1.00 32.96  ? 1245 SER B CA    1 
ATOM   3441  C  C     . SER A  1  446 ? 35.860  47.340  16.499 1.00 33.60  ? 1245 SER B C     1 
ATOM   3442  O  O     . SER A  1  446 ? 36.980  47.677  16.134 1.00 36.03  ? 1245 SER B O     1 
ATOM   3443  C  CB    . SER A  1  446 ? 34.487  49.064  17.473 1.00 28.72  ? 1245 SER B CB    1 
ATOM   3444  O  OG    . SER A  1  446 ? 33.853  49.508  18.615 1.00 31.87  ? 1245 SER B OG    1 
ATOM   3445  N  N     . ARG A  1  447 ? 35.067  46.576  15.755 1.00 34.50  ? 1246 ARG B N     1 
ATOM   3446  C  CA    . ARG A  1  447 ? 35.508  46.251  14.415 1.00 33.69  ? 1246 ARG B CA    1 
ATOM   3447  C  C     . ARG A  1  447 ? 34.989  47.321  13.499 1.00 31.78  ? 1246 ARG B C     1 
ATOM   3448  O  O     . ARG A  1  447 ? 33.765  47.460  13.348 1.00 28.51  ? 1246 ARG B O     1 
ATOM   3449  C  CB    . ARG A  1  447 ? 35.027  44.865  13.952 1.00 31.03  ? 1246 ARG B CB    1 
ATOM   3450  C  CG    . ARG A  1  447 ? 35.535  44.473  12.571 1.00 29.85  ? 1246 ARG B CG    1 
ATOM   3451  C  CD    . ARG A  1  447 ? 35.254  43.011  12.153 1.00 27.26  ? 1246 ARG B CD    1 
ATOM   3452  N  NE    . ARG A  1  447 ? 35.978  42.061  13.005 1.00 24.65  ? 1246 ARG B NE    1 
ATOM   3453  C  CZ    . ARG A  1  447 ? 37.294  41.799  12.847 1.00 28.32  ? 1246 ARG B CZ    1 
ATOM   3454  N  NH1   . ARG A  1  447 ? 38.017  42.398  11.897 1.00 26.18  ? 1246 ARG B NH1   1 
ATOM   3455  N  NH2   . ARG A  1  447 ? 37.909  40.951  13.644 1.00 28.73  ? 1246 ARG B NH2   1 
ATOM   3456  N  N     . ALA A  1  448 ? 35.916  48.045  12.867 1.00 28.94  ? 1247 ALA B N     1 
ATOM   3457  C  CA    . ALA A  1  448 ? 35.539  49.188  12.061 1.00 33.06  ? 1247 ALA B CA    1 
ATOM   3458  C  C     . ALA A  1  448 ? 36.350  49.149  10.785 1.00 33.38  ? 1247 ALA B C     1 
ATOM   3459  O  O     . ALA A  1  448 ? 37.504  48.734  10.804 1.00 35.55  ? 1247 ALA B O     1 
ATOM   3460  C  CB    . ALA A  1  448 ? 35.757  50.505  12.819 1.00 30.01  ? 1247 ALA B CB    1 
ATOM   3461  N  N     . VAL A  1  449 ? 35.733  49.505  9.669  1.00 32.56  ? 1248 VAL B N     1 
ATOM   3462  C  CA    . VAL A  1  449 ? 36.470  49.597  8.411  1.00 35.11  ? 1248 VAL B CA    1 
ATOM   3463  C  C     . VAL A  1  449 ? 36.143  50.925  7.762  1.00 34.86  ? 1248 VAL B C     1 
ATOM   3464  O  O     . VAL A  1  449 ? 35.144  51.577  8.128  1.00 35.19  ? 1248 VAL B O     1 
ATOM   3465  C  CB    . VAL A  1  449 ? 36.116  48.439  7.448  1.00 38.25  ? 1248 VAL B CB    1 
ATOM   3466  C  CG1   . VAL A  1  449 ? 36.350  47.083  8.100  1.00 30.46  ? 1248 VAL B CG1   1 
ATOM   3467  C  CG2   . VAL A  1  449 ? 34.676  48.547  6.963  1.00 32.54  ? 1248 VAL B CG2   1 
ATOM   3468  N  N     . ILE A  1  450 ? 36.968  51.330  6.818  1.00 31.41  ? 1249 ILE B N     1 
ATOM   3469  C  CA    . ILE A  1  450 ? 36.692  52.559  6.116  1.00 31.38  ? 1249 ILE B CA    1 
ATOM   3470  C  C     . ILE A  1  450 ? 36.335  52.174  4.684  1.00 30.56  ? 1249 ILE B C     1 
ATOM   3471  O  O     . ILE A  1  450 ? 37.031  51.347  4.042  1.00 31.01  ? 1249 ILE B O     1 
ATOM   3472  C  CB    . ILE A  1  450 ? 37.947  53.469  6.163  1.00 35.76  ? 1249 ILE B CB    1 
ATOM   3473  C  CG1   . ILE A  1  450 ? 38.108  54.010  7.579  1.00 34.07  ? 1249 ILE B CG1   1 
ATOM   3474  C  CG2   . ILE A  1  450 ? 37.858  54.552  5.100  1.00 32.26  ? 1249 ILE B CG2   1 
ATOM   3475  C  CD1   . ILE A  1  450 ? 39.461  54.603  7.847  1.00 41.74  ? 1249 ILE B CD1   1 
ATOM   3476  N  N     . GLU A  1  451 ? 35.288  52.767  4.166  1.00 32.58  ? 1250 GLU B N     1 
ATOM   3477  C  CA    . GLU A  1  451 ? 34.853  52.421  2.815  1.00 31.91  ? 1250 GLU B CA    1 
ATOM   3478  C  C     . GLU A  1  451 ? 34.296  53.656  2.093  1.00 34.33  ? 1250 GLU B C     1 
ATOM   3479  O  O     . GLU A  1  451 ? 33.825  54.621  2.725  1.00 35.14  ? 1250 GLU B O     1 
ATOM   3480  C  CB    . GLU A  1  451 ? 33.808  51.285  2.932  1.00 31.26  ? 1250 GLU B CB    1 
ATOM   3481  C  CG    . GLU A  1  451 ? 32.425  51.706  3.296  1.00 28.26  ? 1250 GLU B CG    1 
ATOM   3482  C  CD    . GLU A  1  451 ? 31.449  50.541  3.403  1.00 34.94  ? 1250 GLU B CD    1 
ATOM   3483  O  OE1   . GLU A  1  451 ? 31.829  49.348  3.375  1.00 37.02  ? 1250 GLU B OE1   1 
ATOM   3484  O  OE2   . GLU A  1  451 ? 30.254  50.799  3.560  1.00 32.64  ? 1250 GLU B OE2   1 
ATOM   3485  N  N     . GLU A  1  452 ? 34.301  53.579  0.771  1.00 34.16  ? 1251 GLU B N     1 
ATOM   3486  C  CA    . GLU A  1  452 ? 33.745  54.611  -0.059 1.00 33.49  ? 1251 GLU B CA    1 
ATOM   3487  C  C     . GLU A  1  452 ? 32.214  54.624  -0.050 1.00 33.06  ? 1251 GLU B C     1 
ATOM   3488  O  O     . GLU A  1  452 ? 31.557  53.574  0.063  1.00 30.76  ? 1251 GLU B O     1 
ATOM   3489  C  CB    . GLU A  1  452 ? 34.263  54.397  -1.469 1.00 38.11  ? 1251 GLU B CB    1 
ATOM   3490  C  CG    . GLU A  1  452 ? 33.833  53.079  -2.096 1.00 43.38  ? 1251 GLU B CG    1 
ATOM   3491  C  CD    . GLU A  1  452 ? 34.679  52.725  -3.299 1.00 42.87  ? 1251 GLU B CD    1 
ATOM   3492  O  OE1   . GLU A  1  452 ? 34.340  53.262  -4.385 1.00 41.49  ? 1251 GLU B OE1   1 
ATOM   3493  O  OE2   . GLU A  1  452 ? 35.671  51.943  -3.134 1.00 39.84  ? 1251 GLU B OE2   1 
ATOM   3494  N  N     . ARG A  1  453 ? 31.632  55.811  -0.133 1.00 36.53  ? 1252 ARG B N     1 
ATOM   3495  C  CA    . ARG A  1  453 ? 30.170  55.920  -0.179 1.00 41.41  ? 1252 ARG B CA    1 
ATOM   3496  C  C     . ARG A  1  453 ? 29.667  56.621  -1.446 1.00 43.86  ? 1252 ARG B C     1 
ATOM   3497  O  O     . ARG A  1  453 ? 28.483  56.902  -1.583 1.00 43.90  ? 1252 ARG B O     1 
ATOM   3498  C  CB    . ARG A  1  453 ? 29.639  56.627  1.060  1.00 42.16  ? 1252 ARG B CB    1 
ATOM   3499  C  CG    . ARG A  1  453 ? 30.231  58.001  1.321  1.00 40.35  ? 1252 ARG B CG    1 
ATOM   3500  C  CD    . ARG A  1  453 ? 29.671  58.516  2.647  1.00 40.58  ? 1252 ARG B CD    1 
ATOM   3501  N  NE    . ARG A  1  453 ? 30.373  59.730  3.087  1.00 45.38  ? 1252 ARG B NE    1 
ATOM   3502  C  CZ    . ARG A  1  453 ? 29.891  60.968  2.977  1.00 39.30  ? 1252 ARG B CZ    1 
ATOM   3503  N  NH1   . ARG A  1  453 ? 30.599  61.981  3.414  1.00 39.26  ? 1252 ARG B NH1   1 
ATOM   3504  N  NH2   . ARG A  1  453 ? 28.715  61.187  2.425  1.00 39.22  ? 1252 ARG B NH2   1 
ATOM   3505  N  N     . GLY A  1  454 ? 30.582  56.905  -2.355 1.00 42.98  ? 1253 GLY B N     1 
ATOM   3506  C  CA    . GLY A  1  454 ? 30.244  57.598  -3.587 1.00 53.89  ? 1253 GLY B CA    1 
ATOM   3507  C  C     . GLY A  1  454 ? 30.558  59.079  -3.602 1.00 53.29  ? 1253 GLY B C     1 
ATOM   3508  O  O     . GLY A  1  454 ? 30.462  59.759  -2.588 1.00 63.27  ? 1253 GLY B O     1 
ATOM   3509  N  N     . GLY A  1  455 ? 30.946  59.566  -4.769 1.00 51.67  ? 1254 GLY B N     1 
ATOM   3510  C  CA    . GLY A  1  455 ? 31.199  60.971  -4.948 1.00 48.18  ? 1254 GLY B CA    1 
ATOM   3511  C  C     . GLY A  1  455 ? 32.565  61.303  -4.470 1.00 49.41  ? 1254 GLY B C     1 
ATOM   3512  O  O     . GLY A  1  455 ? 32.867  62.467  -4.252 1.00 56.01  ? 1254 GLY B O     1 
ATOM   3513  N  N     . GLY A  1  456 ? 33.396  60.280  -4.293 1.00 46.46  ? 1255 GLY B N     1 
ATOM   3514  C  CA    . GLY A  1  456 ? 34.751  60.489  -3.771 1.00 45.43  ? 1255 GLY B CA    1 
ATOM   3515  C  C     . GLY A  1  456 ? 34.687  60.650  -2.247 1.00 46.97  ? 1255 GLY B C     1 
ATOM   3516  O  O     . GLY A  1  456 ? 35.668  61.043  -1.616 1.00 50.17  ? 1255 GLY B O     1 
ATOM   3517  N  N     . ARG A  1  457 ? 33.525  60.343  -1.660 1.00 41.88  ? 1256 ARG B N     1 
ATOM   3518  C  CA    . ARG A  1  457 ? 33.372  60.424  -0.230 1.00 43.00  ? 1256 ARG B CA    1 
ATOM   3519  C  C     . ARG A  1  457 ? 33.491  59.065  0.451  1.00 45.08  ? 1256 ARG B C     1 
ATOM   3520  O  O     . ARG A  1  457 ? 33.332  58.008  -0.221 1.00 40.74  ? 1256 ARG B O     1 
ATOM   3521  C  CB    . ARG A  1  457 ? 32.064  61.093  0.138  1.00 45.76  ? 1256 ARG B CB    1 
ATOM   3522  C  CG    . ARG A  1  457 ? 32.075  62.614  -0.140 1.00 51.48  ? 1256 ARG B CG    1 
ATOM   3523  C  CD    . ARG A  1  457 ? 30.777  63.293  0.286  1.00 52.35  ? 1256 ARG B CD    1 
ATOM   3524  N  NE    . ARG A  1  457 ? 29.677  62.658  -0.423 1.00 67.33  ? 1256 ARG B NE    1 
ATOM   3525  C  CZ    . ARG A  1  457 ? 29.183  63.099  -1.575 1.00 74.34  ? 1256 ARG B CZ    1 
ATOM   3526  N  NH1   . ARG A  1  457 ? 29.666  64.223  -2.120 1.00 67.54  ? 1256 ARG B NH1   1 
ATOM   3527  N  NH2   . ARG A  1  457 ? 28.185  62.431  -2.152 1.00 76.75  ? 1256 ARG B NH2   1 
ATOM   3528  N  N     . GLN A  1  458 ? 33.756  59.078  1.768  1.00 37.29  ? 1257 GLN B N     1 
ATOM   3529  C  CA    . GLN A  1  458 ? 33.957  57.841  2.516  1.00 38.02  ? 1257 GLN B CA    1 
ATOM   3530  C  C     . GLN A  1  458 ? 33.114  57.750  3.766  1.00 42.90  ? 1257 GLN B C     1 
ATOM   3531  O  O     . GLN A  1  458 ? 32.591  58.752  4.236  1.00 38.88  ? 1257 GLN B O     1 
ATOM   3532  C  CB    . GLN A  1  458 ? 35.414  57.726  2.910  1.00 34.17  ? 1257 GLN B CB    1 
ATOM   3533  C  CG    . GLN A  1  458 ? 36.356  57.262  1.802  1.00 37.16  ? 1257 GLN B CG    1 
ATOM   3534  C  CD    . GLN A  1  458 ? 37.824  57.322  2.214  1.00 37.77  ? 1257 GLN B CD    1 
ATOM   3535  O  OE1   . GLN A  1  458 ? 38.279  58.306  2.830  1.00 42.95  ? 1257 GLN B OE1   1 
ATOM   3536  N  NE2   . GLN A  1  458 ? 38.571  56.274  1.897  1.00 36.23  ? 1257 GLN B NE2   1 
ATOM   3537  N  N     . ARG A  1  459 ? 32.984  56.547  4.326  1.00 44.04  ? 1258 ARG B N     1 
ATOM   3538  C  CA    . ARG A  1  459 ? 32.377  56.378  5.662  1.00 34.42  ? 1258 ARG B CA    1 
ATOM   3539  C  C     . ARG A  1  459 ? 33.149  55.387  6.504  1.00 35.19  ? 1258 ARG B C     1 
ATOM   3540  O  O     . ARG A  1  459 ? 33.924  54.577  5.983  1.00 35.78  ? 1258 ARG B O     1 
ATOM   3541  C  CB    . ARG A  1  459 ? 30.922  55.963  5.546  1.00 35.31  ? 1258 ARG B CB    1 
ATOM   3542  C  CG    . ARG A  1  459 ? 30.681  54.858  4.547  1.00 37.70  ? 1258 ARG B CG    1 
ATOM   3543  C  CD    . ARG A  1  459 ? 29.292  54.326  4.734  1.00 36.90  ? 1258 ARG B CD    1 
ATOM   3544  N  NE    . ARG A  1  459 ? 29.085  53.252  3.806  1.00 39.31  ? 1258 ARG B NE    1 
ATOM   3545  C  CZ    . ARG A  1  459 ? 28.183  53.268  2.850  1.00 41.84  ? 1258 ARG B CZ    1 
ATOM   3546  N  NH1   . ARG A  1  459 ? 27.366  54.311  2.695  1.00 36.06  ? 1258 ARG B NH1   1 
ATOM   3547  N  NH2   . ARG A  1  459 ? 28.115  52.220  2.039  1.00 41.57  ? 1258 ARG B NH2   1 
ATOM   3548  N  N     . ILE A  1  460 ? 32.997  55.478  7.817  1.00 33.30  ? 1259 ILE B N     1 
ATOM   3549  C  CA    . ILE A  1  460 ? 33.571  54.466  8.676  1.00 32.81  ? 1259 ILE B CA    1 
ATOM   3550  C  C     . ILE A  1  460 ? 32.392  53.575  9.017  1.00 35.53  ? 1259 ILE B C     1 
ATOM   3551  O  O     . ILE A  1  460 ? 31.306  54.087  9.286  1.00 32.53  ? 1259 ILE B O     1 
ATOM   3552  C  CB    . ILE A  1  460 ? 34.095  55.088  9.940  1.00 32.74  ? 1259 ILE B CB    1 
ATOM   3553  C  CG1   . ILE A  1  460 ? 35.311  55.916  9.650  1.00 34.79  ? 1259 ILE B CG1   1 
ATOM   3554  C  CG2   . ILE A  1  460 ? 34.541  54.024  10.893 1.00 30.80  ? 1259 ILE B CG2   1 
ATOM   3555  C  CD1   . ILE A  1  460 ? 35.456  57.030  10.632 1.00 32.02  ? 1259 ILE B CD1   1 
ATOM   3556  N  N     . VAL A  1  461 ? 32.554  52.266  8.927  1.00 33.24  ? 1260 VAL B N     1 
ATOM   3557  C  CA    . VAL A  1  461 ? 31.450  51.366  9.261  1.00 30.21  ? 1260 VAL B CA    1 
ATOM   3558  C  C     . VAL A  1  461 ? 31.859  50.437  10.381 1.00 31.78  ? 1260 VAL B C     1 
ATOM   3559  O  O     . VAL A  1  461 ? 32.876  49.732  10.288 1.00 33.48  ? 1260 VAL B O     1 
ATOM   3560  C  CB    . VAL A  1  461 ? 31.030  50.514  8.063  1.00 32.11  ? 1260 VAL B CB    1 
ATOM   3561  C  CG1   . VAL A  1  461 ? 29.883  49.583  8.388  1.00 31.19  ? 1260 VAL B CG1   1 
ATOM   3562  C  CG2   . VAL A  1  461 ? 30.649  51.383  6.895  1.00 31.24  ? 1260 VAL B CG2   1 
ATOM   3563  N  N     . VAL A  1  462 ? 31.059  50.409  11.436 1.00 28.78  ? 1261 VAL B N     1 
ATOM   3564  C  CA    . VAL A  1  462 ? 31.365  49.615  12.624 1.00 28.60  ? 1261 VAL B CA    1 
ATOM   3565  C  C     . VAL A  1  462 ? 30.404  48.430  12.753 1.00 32.41  ? 1261 VAL B C     1 
ATOM   3566  O  O     . VAL A  1  462 ? 29.193  48.582  12.730 1.00 32.33  ? 1261 VAL B O     1 
ATOM   3567  C  CB    . VAL A  1  462 ? 31.197  50.484  13.874 1.00 30.35  ? 1261 VAL B CB    1 
ATOM   3568  C  CG1   . VAL A  1  462 ? 31.444  49.676  15.126 1.00 29.66  ? 1261 VAL B CG1   1 
ATOM   3569  C  CG2   . VAL A  1  462 ? 32.113  51.717  13.819 1.00 30.93  ? 1261 VAL B CG2   1 
ATOM   3570  N  N     . THR A  1  463 ? 30.933  47.224  12.862 1.00 30.82  ? 1262 THR B N     1 
ATOM   3571  C  CA    . THR A  1  463 ? 30.042  46.054  12.815 1.00 33.16  ? 1262 THR B CA    1 
ATOM   3572  C  C     . THR A  1  463 ? 30.147  45.240  14.046 1.00 33.52  ? 1262 THR B C     1 
ATOM   3573  O  O     . THR A  1  463 ? 29.324  44.353  14.256 1.00 35.24  ? 1262 THR B O     1 
ATOM   3574  C  CB    . THR A  1  463 ? 30.307  45.158  11.601 1.00 32.28  ? 1262 THR B CB    1 
ATOM   3575  O  OG1   . THR A  1  463 ? 31.684  44.777  11.607 1.00 33.24  ? 1262 THR B OG1   1 
ATOM   3576  C  CG2   . THR A  1  463 ? 29.990  45.911  10.361 1.00 30.48  ? 1262 THR B CG2   1 
ATOM   3577  N  N     . GLU A  1  464 ? 31.112  45.580  14.905 1.00 31.08  ? 1263 GLU B N     1 
ATOM   3578  C  CA    . GLU A  1  464 ? 31.255  44.940  16.190 1.00 30.66  ? 1263 GLU B CA    1 
ATOM   3579  C  C     . GLU A  1  464 ? 31.673  46.001  17.158 1.00 35.02  ? 1263 GLU B C     1 
ATOM   3580  O  O     . GLU A  1  464 ? 32.492  46.855  16.816 1.00 37.92  ? 1263 GLU B O     1 
ATOM   3581  C  CB    . GLU A  1  464 ? 32.314  43.819  16.105 1.00 26.82  ? 1263 GLU B CB    1 
ATOM   3582  C  CG    . GLU A  1  464 ? 31.913  42.707  15.161 1.00 26.54  ? 1263 GLU B CG    1 
ATOM   3583  C  CD    . GLU A  1  464 ? 33.055  41.731  14.896 1.00 33.07  ? 1263 GLU B CD    1 
ATOM   3584  O  OE1   . GLU A  1  464 ? 32.832  40.836  14.075 1.00 36.43  ? 1263 GLU B OE1   1 
ATOM   3585  O  OE2   . GLU A  1  464 ? 34.151  41.808  15.513 1.00 32.75  ? 1263 GLU B OE2   1 
ATOM   3586  N  N     . ILE A  1  465 ? 31.131  45.931  18.381 1.00 35.30  ? 1264 ILE B N     1 
ATOM   3587  C  CA    . ILE A  1  465 ? 31.484  46.896  19.425 1.00 36.73  ? 1264 ILE B CA    1 
ATOM   3588  C  C     . ILE A  1  465 ? 32.020  46.163  20.645 1.00 34.67  ? 1264 ILE B C     1 
ATOM   3589  O  O     . ILE A  1  465 ? 31.838  44.926  20.758 1.00 35.11  ? 1264 ILE B O     1 
ATOM   3590  C  CB    . ILE A  1  465 ? 30.277  47.764  19.820 1.00 40.57  ? 1264 ILE B CB    1 
ATOM   3591  C  CG1   . ILE A  1  465 ? 29.140  46.878  20.320 1.00 44.01  ? 1264 ILE B CG1   1 
ATOM   3592  C  CG2   . ILE A  1  465 ? 29.813  48.602  18.640 1.00 42.95  ? 1264 ILE B CG2   1 
ATOM   3593  C  CD1   . ILE A  1  465 ? 27.959  47.656  20.809 1.00 48.57  ? 1264 ILE B CD1   1 
ATOM   3594  N  N     . PRO A  1  466 ? 32.693  46.905  21.577 1.00 31.43  ? 1265 PRO B N     1 
ATOM   3595  C  CA    . PRO A  1  466 ? 33.224  46.160  22.728 1.00 29.21  ? 1265 PRO B CA    1 
ATOM   3596  C  C     . PRO A  1  466 ? 32.167  45.549  23.649 1.00 29.40  ? 1265 PRO B C     1 
ATOM   3597  O  O     . PRO A  1  466 ? 31.030  45.967  23.691 1.00 30.70  ? 1265 PRO B O     1 
ATOM   3598  C  CB    . PRO A  1  466 ? 34.032  47.223  23.473 1.00 28.61  ? 1265 PRO B CB    1 
ATOM   3599  C  CG    . PRO A  1  466 ? 34.305  48.307  22.457 1.00 29.36  ? 1265 PRO B CG    1 
ATOM   3600  C  CD    . PRO A  1  466 ? 33.031  48.340  21.695 1.00 28.00  ? 1265 PRO B CD    1 
ATOM   3601  N  N     . PHE A  1  467 ? 32.582  44.529  24.373 1.00 30.29  ? 1266 PHE B N     1 
ATOM   3602  C  CA    . PHE A  1  467 ? 31.753  43.811  25.342 1.00 33.34  ? 1266 PHE B CA    1 
ATOM   3603  C  C     . PHE A  1  467 ? 31.182  44.735  26.433 1.00 36.29  ? 1266 PHE B C     1 
ATOM   3604  O  O     . PHE A  1  467 ? 31.880  45.581  26.965 1.00 37.70  ? 1266 PHE B O     1 
ATOM   3605  C  CB    . PHE A  1  467 ? 32.582  42.708  25.995 1.00 28.43  ? 1266 PHE B CB    1 
ATOM   3606  C  CG    . PHE A  1  467 ? 31.805  41.821  26.920 1.00 27.83  ? 1266 PHE B CG    1 
ATOM   3607  C  CD1   . PHE A  1  467 ? 30.600  41.225  26.525 1.00 27.32  ? 1266 PHE B CD1   1 
ATOM   3608  C  CD2   . PHE A  1  467 ? 32.290  41.566  28.201 1.00 27.06  ? 1266 PHE B CD2   1 
ATOM   3609  C  CE1   . PHE A  1  467 ? 29.905  40.373  27.399 1.00 26.89  ? 1266 PHE B CE1   1 
ATOM   3610  C  CE2   . PHE A  1  467 ? 31.601  40.749  29.080 1.00 26.02  ? 1266 PHE B CE2   1 
ATOM   3611  C  CZ    . PHE A  1  467 ? 30.403  40.124  28.663 1.00 27.74  ? 1266 PHE B CZ    1 
ATOM   3612  N  N     . GLN A  1  468 ? 29.896  44.564  26.723 1.00 31.54  ? 1267 GLN B N     1 
ATOM   3613  C  CA    . GLN A  1  468 ? 29.174  45.391  27.679 1.00 33.63  ? 1267 GLN B CA    1 
ATOM   3614  C  C     . GLN A  1  468 ? 29.149  46.878  27.364 1.00 35.20  ? 1267 GLN B C     1 
ATOM   3615  O  O     . GLN A  1  468 ? 29.051  47.688  28.253 1.00 37.52  ? 1267 GLN B O     1 
ATOM   3616  C  CB    . GLN A  1  468 ? 29.687  45.181  29.109 1.00 34.18  ? 1267 GLN B CB    1 
ATOM   3617  C  CG    . GLN A  1  468 ? 29.578  43.736  29.606 1.00 41.39  ? 1267 GLN B CG    1 
ATOM   3618  C  CD    . GLN A  1  468 ? 30.246  43.553  30.942 1.00 47.97  ? 1267 GLN B CD    1 
ATOM   3619  O  OE1   . GLN A  1  468 ? 31.354  44.029  31.170 1.00 52.74  ? 1267 GLN B OE1   1 
ATOM   3620  N  NE2   . GLN A  1  468 ? 29.551  42.891  31.857 1.00 55.22  ? 1267 GLN B NE2   1 
ATOM   3621  N  N     . VAL A  1  469 ? 29.169  47.244  26.098 1.00 33.87  ? 1268 VAL B N     1 
ATOM   3622  C  CA    . VAL A  1  469 ? 29.039  48.636  25.676 1.00 32.73  ? 1268 VAL B CA    1 
ATOM   3623  C  C     . VAL A  1  469 ? 27.637  48.859  25.079 1.00 36.24  ? 1268 VAL B C     1 
ATOM   3624  O  O     . VAL A  1  469 ? 27.229  48.197  24.150 1.00 37.34  ? 1268 VAL B O     1 
ATOM   3625  C  CB    . VAL A  1  469 ? 30.102  48.988  24.647 1.00 30.67  ? 1268 VAL B CB    1 
ATOM   3626  C  CG1   . VAL A  1  469 ? 29.820  50.350  24.026 1.00 29.54  ? 1268 VAL B CG1   1 
ATOM   3627  C  CG2   . VAL A  1  469 ? 31.491  48.901  25.258 1.00 32.70  ? 1268 VAL B CG2   1 
ATOM   3628  N  N     . ASN A  1  470 ? 26.891  49.794  25.645 1.00 38.87  ? 1269 ASN B N     1 
ATOM   3629  C  CA    . ASN A  1  470 ? 25.561  50.084  25.151 1.00 34.33  ? 1269 ASN B CA    1 
ATOM   3630  C  C     . ASN A  1  470 ? 25.733  50.813  23.830 1.00 35.86  ? 1269 ASN B C     1 
ATOM   3631  O  O     . ASN A  1  470 ? 26.299  51.913  23.778 1.00 40.53  ? 1269 ASN B O     1 
ATOM   3632  C  CB    . ASN A  1  470 ? 24.816  50.960  26.171 1.00 36.89  ? 1269 ASN B CB    1 
ATOM   3633  C  CG    . ASN A  1  470 ? 23.408  51.283  25.739 1.00 37.37  ? 1269 ASN B CG    1 
ATOM   3634  O  OD1   . ASN A  1  470 ? 23.123  51.587  24.568 1.00 42.29  ? 1269 ASN B OD1   1 
ATOM   3635  N  ND2   . ASN A  1  470 ? 22.515  51.156  26.665 1.00 37.73  ? 1269 ASN B ND2   1 
ATOM   3636  N  N     . LYS A  1  471 ? 25.265  50.196  22.755 1.00 34.70  ? 1270 LYS B N     1 
ATOM   3637  C  CA    . LYS A  1  471 ? 25.441  50.769  21.432 1.00 34.09  ? 1270 LYS B CA    1 
ATOM   3638  C  C     . LYS A  1  471 ? 24.783  52.157  21.284 1.00 38.24  ? 1270 LYS B C     1 
ATOM   3639  O  O     . LYS A  1  471 ? 25.421  53.083  20.797 1.00 35.61  ? 1270 LYS B O     1 
ATOM   3640  C  CB    . LYS A  1  471 ? 24.911  49.802  20.372 1.00 31.02  ? 1270 LYS B CB    1 
ATOM   3641  C  CG    . LYS A  1  471 ? 24.867  50.398  18.977 1.00 30.83  ? 1270 LYS B CG    1 
ATOM   3642  C  CD    . LYS A  1  471 ? 24.732  49.382  17.857 1.00 31.58  ? 1270 LYS B CD    1 
ATOM   3643  C  CE    . LYS A  1  471 ? 23.606  48.373  18.085 1.00 32.70  ? 1270 LYS B CE    1 
ATOM   3644  N  NZ    . LYS A  1  471 ? 22.276  48.998  17.874 1.00 33.89  ? 1270 LYS B NZ    1 
ATOM   3645  N  N     . ALA A  1  472 ? 23.526  52.287  21.713 1.00 37.53  ? 1271 ALA B N     1 
ATOM   3646  C  CA    . ALA A  1  472 ? 22.808  53.554  21.568 1.00 37.21  ? 1271 ALA B CA    1 
ATOM   3647  C  C     . ALA A  1  472 ? 23.543  54.656  22.348 1.00 37.71  ? 1271 ALA B C     1 
ATOM   3648  O  O     . ALA A  1  472 ? 23.702  55.777  21.875 1.00 38.76  ? 1271 ALA B O     1 
ATOM   3649  C  CB    . ALA A  1  472 ? 21.377  53.426  22.061 1.00 28.52  ? 1271 ALA B CB    1 
ATOM   3650  N  N     . ARG A  1  473 ? 24.020  54.304  23.521 1.00 35.49  ? 1272 ARG B N     1 
ATOM   3651  C  CA    . ARG A  1  473 ? 24.693  55.257  24.343 1.00 39.58  ? 1272 ARG B CA    1 
ATOM   3652  C  C     . ARG A  1  473 ? 26.047  55.654  23.793 1.00 42.57  ? 1272 ARG B C     1 
ATOM   3653  O  O     . ARG A  1  473 ? 26.485  56.787  23.989 1.00 41.38  ? 1272 ARG B O     1 
ATOM   3654  C  CB    . ARG A  1  473 ? 24.809  54.700  25.751 1.00 43.05  ? 1272 ARG B CB    1 
ATOM   3655  C  CG    . ARG A  1  473 ? 25.555  55.641  26.613 1.00 51.80  ? 1272 ARG B CG    1 
ATOM   3656  C  CD    . ARG A  1  473 ? 25.897  55.072  27.948 1.00 57.33  ? 1272 ARG B CD    1 
ATOM   3657  N  NE    . ARG A  1  473 ? 24.706  54.571  28.615 1.00 66.26  ? 1272 ARG B NE    1 
ATOM   3658  C  CZ    . ARG A  1  473 ? 24.614  53.353  29.140 1.00 64.89  ? 1272 ARG B CZ    1 
ATOM   3659  N  NH1   . ARG A  1  473 ? 25.651  52.526  29.091 1.00 64.61  ? 1272 ARG B NH1   1 
ATOM   3660  N  NH2   . ARG A  1  473 ? 23.501  52.976  29.733 1.00 63.65  ? 1272 ARG B NH2   1 
ATOM   3661  N  N     . MET A  1  474 ? 26.738  54.711  23.163 1.00 42.92  ? 1273 MET B N     1 
ATOM   3662  C  CA    . MET A  1  474 ? 27.998  55.015  22.502 1.00 40.54  ? 1273 MET B CA    1 
ATOM   3663  C  C     . MET A  1  474 ? 27.735  55.943  21.327 1.00 39.60  ? 1273 MET B C     1 
ATOM   3664  O  O     . MET A  1  474 ? 28.528  56.785  21.060 1.00 38.71  ? 1273 MET B O     1 
ATOM   3665  C  CB    . MET A  1  474 ? 28.624  53.749  21.978 1.00 40.76  ? 1273 MET B CB    1 
ATOM   3666  C  CG    . MET A  1  474 ? 29.816  54.027  21.069 1.00 44.48  ? 1273 MET B CG    1 
ATOM   3667  S  SD    . MET A  1  474 ? 30.441  52.477  20.369 1.00 46.39  ? 1273 MET B SD    1 
ATOM   3668  C  CE    . MET A  1  474 ? 29.390  52.414  18.892 1.00 42.57  ? 1273 MET B CE    1 
ATOM   3669  N  N     . ILE A  1  475 ? 26.644  55.736  20.602 1.00 36.45  ? 1274 ILE B N     1 
ATOM   3670  C  CA    . ILE A  1  475 ? 26.314  56.586  19.501 1.00 39.54  ? 1274 ILE B CA    1 
ATOM   3671  C  C     . ILE A  1  475 ? 26.011  58.020  19.960 1.00 43.96  ? 1274 ILE B C     1 
ATOM   3672  O  O     . ILE A  1  475 ? 26.365  58.969  19.257 1.00 44.09  ? 1274 ILE B O     1 
ATOM   3673  C  CB    . ILE A  1  475 ? 25.128  56.012  18.724 1.00 38.19  ? 1274 ILE B CB    1 
ATOM   3674  C  CG1   . ILE A  1  475 ? 25.613  54.804  17.950 1.00 39.09  ? 1274 ILE B CG1   1 
ATOM   3675  C  CG2   . ILE A  1  475 ? 24.526  57.024  17.741 1.00 33.82  ? 1274 ILE B CG2   1 
ATOM   3676  C  CD1   . ILE A  1  475 ? 24.465  54.005  17.410 1.00 34.76  ? 1274 ILE B CD1   1 
ATOM   3677  N  N     A GLU A  1  476 ? 25.332  58.134  21.092 0.50 41.33  ? 1275 GLU B N     1 
ATOM   3678  N  N     B GLU A  1  476 ? 25.390  58.175  21.127 0.50 40.95  ? 1275 GLU B N     1 
ATOM   3679  C  CA    A GLU A  1  476 ? 25.044  59.397  21.719 0.50 43.93  ? 1275 GLU B CA    1 
ATOM   3680  C  CA    B GLU A  1  476 ? 25.045  59.498  21.636 0.50 43.16  ? 1275 GLU B CA    1 
ATOM   3681  C  C     A GLU A  1  476 ? 26.308  60.170  22.077 0.50 42.97  ? 1275 GLU B C     1 
ATOM   3682  C  C     B GLU A  1  476 ? 26.301  60.232  22.139 0.50 42.42  ? 1275 GLU B C     1 
ATOM   3683  O  O     A GLU A  1  476 ? 26.375  61.366  21.902 0.50 43.19  ? 1275 GLU B O     1 
ATOM   3684  O  O     B GLU A  1  476 ? 26.405  61.467  22.015 0.50 43.25  ? 1275 GLU B O     1 
ATOM   3685  C  CB    A GLU A  1  476 ? 24.286  59.128  22.998 0.50 44.71  ? 1275 GLU B CB    1 
ATOM   3686  C  CB    B GLU A  1  476 ? 23.957  59.393  22.706 0.50 43.68  ? 1275 GLU B CB    1 
ATOM   3687  C  CG    A GLU A  1  476 ? 22.835  59.546  23.014 0.50 45.15  ? 1275 GLU B CG    1 
ATOM   3688  C  CG    B GLU A  1  476 ? 23.760  60.666  23.506 0.50 41.33  ? 1275 GLU B CG    1 
ATOM   3689  C  CD    A GLU A  1  476 ? 22.138  58.903  24.170 0.50 47.65  ? 1275 GLU B CD    1 
ATOM   3690  C  CD    B GLU A  1  476 ? 23.175  61.823  22.691 0.50 40.42  ? 1275 GLU B CD    1 
ATOM   3691  O  OE1   A GLU A  1  476 ? 22.695  58.992  25.288 0.50 46.85  ? 1275 GLU B OE1   1 
ATOM   3692  O  OE1   B GLU A  1  476 ? 22.044  61.702  22.185 0.50 36.44  ? 1275 GLU B OE1   1 
ATOM   3693  O  OE2   A GLU A  1  476 ? 21.071  58.292  23.952 0.50 48.26  ? 1275 GLU B OE2   1 
ATOM   3694  O  OE2   B GLU A  1  476 ? 23.837  62.874  22.570 0.50 39.12  ? 1275 GLU B OE2   1 
ATOM   3695  N  N     . LYS A  1  477 ? 27.289  59.467  22.612 1.00 40.15  ? 1276 LYS B N     1 
ATOM   3696  C  CA    . LYS A  1  477 ? 28.567  60.055  22.903 1.00 40.51  ? 1276 LYS B CA    1 
ATOM   3697  C  C     . LYS A  1  477 ? 29.225  60.648  21.683 1.00 46.47  ? 1276 LYS B C     1 
ATOM   3698  O  O     . LYS A  1  477 ? 29.806  61.745  21.770 1.00 49.29  ? 1276 LYS B O     1 
ATOM   3699  C  CB    . LYS A  1  477 ? 29.511  59.095  23.583 1.00 42.02  ? 1276 LYS B CB    1 
ATOM   3700  C  CG    . LYS A  1  477 ? 29.130  58.839  25.025 1.00 56.16  ? 1276 LYS B CG    1 
ATOM   3701  C  CD    . LYS A  1  477 ? 30.299  58.360  25.886 1.00 62.06  ? 1276 LYS B CD    1 
ATOM   3702  C  CE    . LYS A  1  477 ? 29.773  57.741  27.171 1.00 65.29  ? 1276 LYS B CE    1 
ATOM   3703  N  NZ    . LYS A  1  477 ? 28.496  58.371  27.593 1.00 67.87  ? 1276 LYS B NZ    1 
ATOM   3704  N  N     . ILE A  1  478 ? 29.107  59.950  20.557 1.00 42.65  ? 1277 ILE B N     1 
ATOM   3705  C  CA    . ILE A  1  478 ? 29.719  60.409  19.323 1.00 41.60  ? 1277 ILE B CA    1 
ATOM   3706  C  C     . ILE A  1  478 ? 28.983  61.649  18.846 1.00 43.44  ? 1277 ILE B C     1 
ATOM   3707  O  O     . ILE A  1  478 ? 29.623  62.566  18.352 1.00 37.84  ? 1277 ILE B O     1 
ATOM   3708  C  CB    . ILE A  1  478 ? 29.697  59.336  18.204 1.00 39.94  ? 1277 ILE B CB    1 
ATOM   3709  C  CG1   . ILE A  1  478 ? 30.542  58.133  18.630 1.00 38.48  ? 1277 ILE B CG1   1 
ATOM   3710  C  CG2   . ILE A  1  478 ? 30.206  59.920  16.872 1.00 37.15  ? 1277 ILE B CG2   1 
ATOM   3711  C  CD1   . ILE A  1  478 ? 30.417  56.932  17.732 1.00 32.22  ? 1277 ILE B CD1   1 
ATOM   3712  N  N     . ALA A  1  479 ? 27.657  61.627  18.947 1.00 41.01  ? 1278 ALA B N     1 
ATOM   3713  C  CA    . ALA A  1  479 ? 26.851  62.712  18.461 1.00 40.52  ? 1278 ALA B CA    1 
ATOM   3714  C  C     . ALA A  1  479 ? 27.175  63.930  19.285 1.00 49.97  ? 1278 ALA B C     1 
ATOM   3715  O  O     . ALA A  1  479 ? 27.209  65.013  18.758 1.00 52.47  ? 1278 ALA B O     1 
ATOM   3716  C  CB    . ALA A  1  479 ? 25.392  62.357  18.614 1.00 35.03  ? 1278 ALA B CB    1 
ATOM   3717  N  N     . GLU A  1  480 ? 27.390  63.719  20.588 1.00 54.77  ? 1279 GLU B N     1 
ATOM   3718  C  CA    . GLU A  1  480 ? 27.707  64.771  21.528 1.00 52.34  ? 1279 GLU B CA    1 
ATOM   3719  C  C     . GLU A  1  480 ? 29.013  65.427  21.173 1.00 50.04  ? 1279 GLU B C     1 
ATOM   3720  O  O     . GLU A  1  480 ? 29.105  66.630  21.118 1.00 47.75  ? 1279 GLU B O     1 
ATOM   3721  C  CB    . GLU A  1  480 ? 27.849  64.191  22.929 1.00 65.19  ? 1279 GLU B CB    1 
ATOM   3722  C  CG    . GLU A  1  480 ? 26.646  64.425  23.834 1.00 78.75  ? 1279 GLU B CG    1 
ATOM   3723  C  CD    . GLU A  1  480 ? 26.823  63.819  25.203 1.00 81.74  ? 1279 GLU B CD    1 
ATOM   3724  O  OE1   . GLU A  1  480 ? 25.867  63.157  25.656 1.00 84.35  ? 1279 GLU B OE1   1 
ATOM   3725  O  OE2   . GLU A  1  480 ? 27.913  64.005  25.809 1.00 78.73  ? 1279 GLU B OE2   1 
ATOM   3726  N  N     . LEU A  1  481 ? 30.016  64.611  20.891 1.00 50.30  ? 1280 LEU B N     1 
ATOM   3727  C  CA    . LEU A  1  481 ? 31.322  65.110  20.550 1.00 46.89  ? 1280 LEU B CA    1 
ATOM   3728  C  C     . LEU A  1  481 ? 31.260  65.959  19.299 1.00 49.06  ? 1280 LEU B C     1 
ATOM   3729  O  O     . LEU A  1  481 ? 31.956  66.944  19.211 1.00 50.77  ? 1280 LEU B O     1 
ATOM   3730  C  CB    . LEU A  1  481 ? 32.238  63.954  20.273 1.00 45.21  ? 1280 LEU B CB    1 
ATOM   3731  C  CG    . LEU A  1  481 ? 33.281  63.336  21.165 1.00 49.97  ? 1280 LEU B CG    1 
ATOM   3732  C  CD1   . LEU A  1  481 ? 33.981  62.329  20.247 1.00 52.57  ? 1280 LEU B CD1   1 
ATOM   3733  C  CD2   . LEU A  1  481 ? 34.279  64.342  21.721 1.00 48.70  ? 1280 LEU B CD2   1 
ATOM   3734  N  N     . VAL A  1  482 ? 30.447  65.554  18.341 1.00 48.08  ? 1281 VAL B N     1 
ATOM   3735  C  CA    . VAL A  1  482 ? 30.321  66.272  17.091 1.00 52.67  ? 1281 VAL B CA    1 
ATOM   3736  C  C     . VAL A  1  482 ? 29.633  67.610  17.308 1.00 55.01  ? 1281 VAL B C     1 
ATOM   3737  O  O     . VAL A  1  482 ? 30.042  68.621  16.742 1.00 61.68  ? 1281 VAL B O     1 
ATOM   3738  C  CB    . VAL A  1  482 ? 29.515  65.447  16.077 1.00 47.10  ? 1281 VAL B CB    1 
ATOM   3739  C  CG1   . VAL A  1  482 ? 29.020  66.311  14.929 1.00 44.72  ? 1281 VAL B CG1   1 
ATOM   3740  C  CG2   . VAL A  1  482 ? 30.376  64.300  15.591 1.00 46.24  ? 1281 VAL B CG2   1 
ATOM   3741  N  N     . ARG A  1  483 ? 28.601  67.627  18.130 1.00 48.94  ? 1282 ARG B N     1 
ATOM   3742  C  CA    . ARG A  1  483 ? 27.838  68.860  18.332 1.00 55.54  ? 1282 ARG B CA    1 
ATOM   3743  C  C     . ARG A  1  483 ? 28.601  69.897  19.166 1.00 58.94  ? 1282 ARG B C     1 
ATOM   3744  O  O     . ARG A  1  483 ? 28.402  71.093  18.998 1.00 64.72  ? 1282 ARG B O     1 
ATOM   3745  C  CB    . ARG A  1  483 ? 26.506  68.537  18.970 1.00 55.96  ? 1282 ARG B CB    1 
ATOM   3746  C  CG    . ARG A  1  483 ? 26.053  69.519  20.042 1.00 63.38  ? 1282 ARG B CG    1 
ATOM   3747  C  CD    . ARG A  1  483 ? 25.027  68.905  20.970 1.00 66.55  ? 1282 ARG B CD    1 
ATOM   3748  N  NE    . ARG A  1  483 ? 24.427  67.715  20.362 1.00 76.66  ? 1282 ARG B NE    1 
ATOM   3749  C  CZ    . ARG A  1  483 ? 24.146  66.586  21.012 1.00 72.83  ? 1282 ARG B CZ    1 
ATOM   3750  N  NH1   . ARG A  1  483 ? 24.391  66.474  22.312 1.00 78.96  ? 1282 ARG B NH1   1 
ATOM   3751  N  NH2   . ARG A  1  483 ? 23.599  65.581  20.359 1.00 63.62  ? 1282 ARG B NH2   1 
ATOM   3752  N  N     . ASP A  1  484 ? 29.469  69.415  20.056 1.00 56.95  ? 1283 ASP B N     1 
ATOM   3753  C  CA    . ASP A  1  484 ? 30.287  70.240  20.926 1.00 55.70  ? 1283 ASP B CA    1 
ATOM   3754  C  C     . ASP A  1  484 ? 31.573  70.625  20.255 1.00 58.05  ? 1283 ASP B C     1 
ATOM   3755  O  O     . ASP A  1  484 ? 32.420  71.281  20.857 1.00 63.12  ? 1283 ASP B O     1 
ATOM   3756  C  CB    . ASP A  1  484 ? 30.577  69.520  22.244 1.00 51.34  ? 1283 ASP B CB    1 
ATOM   3757  C  CG    . ASP A  1  484 ? 29.342  69.429  23.149 1.00 53.92  ? 1283 ASP B CG    1 
ATOM   3758  O  OD1   . ASP A  1  484 ? 28.218  69.831  22.748 1.00 56.50  ? 1283 ASP B OD1   1 
ATOM   3759  O  OD2   . ASP A  1  484 ? 29.491  68.919  24.272 1.00 60.41  ? 1283 ASP B OD2   1 
ATOM   3760  N  N     . LYS A  1  485 ? 31.717  70.237  18.995 1.00 53.80  ? 1284 LYS B N     1 
ATOM   3761  C  CA    . LYS A  1  485 ? 32.915  70.517  18.206 1.00 55.35  ? 1284 LYS B CA    1 
ATOM   3762  C  C     . LYS A  1  485 ? 34.191  69.964  18.793 1.00 52.30  ? 1284 LYS B C     1 
ATOM   3763  O  O     . LYS A  1  485 ? 35.256  70.538  18.607 1.00 61.64  ? 1284 LYS B O     1 
ATOM   3764  C  CB    . LYS A  1  485 ? 33.081  72.023  17.899 1.00 59.22  ? 1284 LYS B CB    1 
ATOM   3765  C  CG    . LYS A  1  485 ? 31.779  72.781  17.655 1.00 61.67  ? 1284 LYS B CG    1 
ATOM   3766  C  CD    . LYS A  1  485 ? 31.145  72.388  16.335 1.00 56.93  ? 1284 LYS B CD    1 
ATOM   3767  N  N     . LYS A  1  486 ? 34.112  68.823  19.459 1.00 50.82  ? 1285 LYS B N     1 
ATOM   3768  C  CA    . LYS A  1  486 ? 35.319  68.222  20.035 1.00 46.75  ? 1285 LYS B CA    1 
ATOM   3769  C  C     . LYS A  1  486 ? 35.997  67.242  19.088 1.00 43.46  ? 1285 LYS B C     1 
ATOM   3770  O  O     . LYS A  1  486 ? 37.059  66.688  19.392 1.00 42.86  ? 1285 LYS B O     1 
ATOM   3771  C  CB    . LYS A  1  486 ? 35.016  67.586  21.379 1.00 48.64  ? 1285 LYS B CB    1 
ATOM   3772  C  CG    . LYS A  1  486 ? 34.921  68.586  22.514 1.00 48.53  ? 1285 LYS B CG    1 
ATOM   3773  C  CD    . LYS A  1  486 ? 34.178  67.974  23.696 1.00 53.30  ? 1285 LYS B CD    1 
ATOM   3774  C  CE    . LYS A  1  486 ? 34.439  68.811  24.941 1.00 51.71  ? 1285 LYS B CE    1 
ATOM   3775  N  NZ    . LYS A  1  486 ? 33.546  68.340  26.019 1.00 54.76  ? 1285 LYS B NZ    1 
ATOM   3776  N  N     . ILE A  1  487 ? 35.394  67.044  17.925 1.00 45.50  ? 1286 ILE B N     1 
ATOM   3777  C  CA    . ILE A  1  487 ? 35.983  66.177  16.908 1.00 43.67  ? 1286 ILE B CA    1 
ATOM   3778  C  C     . ILE A  1  487 ? 35.684  66.780  15.567 1.00 45.20  ? 1286 ILE B C     1 
ATOM   3779  O  O     . ILE A  1  487 ? 34.604  67.275  15.351 1.00 44.95  ? 1286 ILE B O     1 
ATOM   3780  C  CB    . ILE A  1  487 ? 35.484  64.684  17.014 1.00 42.89  ? 1286 ILE B CB    1 
ATOM   3781  C  CG1   . ILE A  1  487 ? 36.422  63.760  16.231 1.00 41.26  ? 1286 ILE B CG1   1 
ATOM   3782  C  CG2   . ILE A  1  487 ? 33.997  64.513  16.659 1.00 38.63  ? 1286 ILE B CG2   1 
ATOM   3783  C  CD1   . ILE A  1  487 ? 36.123  62.303  16.446 1.00 39.43  ? 1286 ILE B CD1   1 
ATOM   3784  N  N     . ASP A  1  488 ? 36.641  66.705  14.663 1.00 50.94  ? 1287 ASP B N     1 
ATOM   3785  C  CA    . ASP A  1  488 ? 36.488  67.245  13.344 1.00 54.37  ? 1287 ASP B CA    1 
ATOM   3786  C  C     . ASP A  1  488 ? 36.207  66.163  12.304 1.00 55.05  ? 1287 ASP B C     1 
ATOM   3787  O  O     . ASP A  1  488 ? 36.735  65.052  12.415 1.00 48.86  ? 1287 ASP B O     1 
ATOM   3788  C  CB    . ASP A  1  488 ? 37.791  67.927  13.006 1.00 62.25  ? 1287 ASP B CB    1 
ATOM   3789  C  CG    . ASP A  1  488 ? 37.785  68.546  11.632 1.00 73.79  ? 1287 ASP B CG    1 
ATOM   3790  O  OD1   . ASP A  1  488 ? 36.987  69.489  11.410 1.00 71.57  ? 1287 ASP B OD1   1 
ATOM   3791  O  OD2   . ASP A  1  488 ? 38.582  68.093  10.777 1.00 78.24  ? 1287 ASP B OD2   1 
ATOM   3792  N  N     . GLY A  1  489 ? 35.379  66.512  11.317 1.00 52.77  ? 1288 GLY B N     1 
ATOM   3793  C  CA    . GLY A  1  489 ? 35.190  65.735  10.114 1.00 50.46  ? 1288 GLY B CA    1 
ATOM   3794  C  C     . GLY A  1  489 ? 33.990  64.820  9.933  1.00 49.23  ? 1288 GLY B C     1 
ATOM   3795  O  O     . GLY A  1  489 ? 33.940  64.103  8.946  1.00 49.02  ? 1288 GLY B O     1 
ATOM   3796  N  N     . ILE A  1  490 ? 33.022  64.837  10.836 1.00 44.08  ? 1289 ILE B N     1 
ATOM   3797  C  CA    . ILE A  1  490 ? 31.928  63.883  10.751 1.00 42.46  ? 1289 ILE B CA    1 
ATOM   3798  C  C     . ILE A  1  490 ? 30.680  64.574  10.245 1.00 46.71  ? 1289 ILE B C     1 
ATOM   3799  O  O     . ILE A  1  490 ? 30.279  65.579  10.789 1.00 42.72  ? 1289 ILE B O     1 
ATOM   3800  C  CB    . ILE A  1  490 ? 31.676  63.191  12.085 1.00 38.22  ? 1289 ILE B CB    1 
ATOM   3801  C  CG1   . ILE A  1  490 ? 32.855  62.289  12.431 1.00 36.96  ? 1289 ILE B CG1   1 
ATOM   3802  C  CG2   . ILE A  1  490 ? 30.350  62.446  12.083 1.00 33.72  ? 1289 ILE B CG2   1 
ATOM   3803  C  CD1   . ILE A  1  490 ? 32.738  61.676  13.823 1.00 37.42  ? 1289 ILE B CD1   1 
ATOM   3804  N  N     . THR A  1  491 ? 30.086  64.028  9.181  1.00 44.72  ? 1290 THR B N     1 
ATOM   3805  C  CA    . THR A  1  491 ? 28.939  64.659  8.557  1.00 46.98  ? 1290 THR B CA    1 
ATOM   3806  C  C     . THR A  1  491 ? 27.613  63.964  8.834  1.00 45.75  ? 1290 THR B C     1 
ATOM   3807  O  O     . THR A  1  491 ? 26.567  64.562  8.674  1.00 49.56  ? 1290 THR B O     1 
ATOM   3808  C  CB    . THR A  1  491 ? 29.124  64.830  7.021  1.00 50.08  ? 1290 THR B CB    1 
ATOM   3809  O  OG1   . THR A  1  491 ? 29.342  63.555  6.404  1.00 58.91  ? 1290 THR B OG1   1 
ATOM   3810  C  CG2   . THR A  1  491 ? 30.292  65.675  6.729  1.00 43.73  ? 1290 THR B CG2   1 
ATOM   3811  N  N     . ASP A  1  492 ? 27.610  62.698  9.182  1.00 44.73  ? 1291 ASP B N     1 
ATOM   3812  C  CA    . ASP A  1  492 ? 26.360  62.035  9.534  1.00 42.88  ? 1291 ASP B CA    1 
ATOM   3813  C  C     . ASP A  1  492 ? 26.678  60.872  10.440 1.00 42.92  ? 1291 ASP B C     1 
ATOM   3814  O  O     . ASP A  1  492 ? 27.812  60.397  10.449 1.00 47.56  ? 1291 ASP B O     1 
ATOM   3815  C  CB    . ASP A  1  492 ? 25.686  61.523  8.264  1.00 49.89  ? 1291 ASP B CB    1 
ATOM   3816  C  CG    . ASP A  1  492 ? 24.226  61.348  8.437  1.00 52.91  ? 1291 ASP B CG    1 
ATOM   3817  O  OD1   . ASP A  1  492 ? 23.693  61.771  9.465  1.00 62.33  ? 1291 ASP B OD1   1 
ATOM   3818  O  OD2   . ASP A  1  492 ? 23.578  60.813  7.539  1.00 63.32  ? 1291 ASP B OD2   1 
ATOM   3819  N  N     . LEU A  1  493 ? 25.707  60.407  11.206 1.00 40.24  ? 1292 LEU B N     1 
ATOM   3820  C  CA    . LEU A  1  493 ? 25.898  59.268  12.058 1.00 38.42  ? 1292 LEU B CA    1 
ATOM   3821  C  C     . LEU A  1  493 ? 24.597  58.513  12.037 1.00 40.97  ? 1292 LEU B C     1 
ATOM   3822  O  O     . LEU A  1  493 ? 23.540  59.107  12.234 1.00 43.51  ? 1292 LEU B O     1 
ATOM   3823  C  CB    . LEU A  1  493 ? 26.281  59.753  13.456 1.00 38.39  ? 1292 LEU B CB    1 
ATOM   3824  C  CG    . LEU A  1  493 ? 26.346  58.799  14.636 1.00 43.53  ? 1292 LEU B CG    1 
ATOM   3825  C  CD1   . LEU A  1  493 ? 27.504  57.797  14.596 1.00 39.39  ? 1292 LEU B CD1   1 
ATOM   3826  C  CD2   . LEU A  1  493 ? 26.446  59.717  15.835 1.00 37.50  ? 1292 LEU B CD2   1 
ATOM   3827  N  N     . ARG A  1  494 ? 24.619  57.214  11.731 1.00 41.64  ? 1293 ARG B N     1 
ATOM   3828  C  CA    . ARG A  1  494 ? 23.342  56.443  11.714 1.00 37.70  ? 1293 ARG B CA    1 
ATOM   3829  C  C     . ARG A  1  494 ? 23.518  55.049  12.272 1.00 38.74  ? 1293 ARG B C     1 
ATOM   3830  O  O     . ARG A  1  494 ? 24.556  54.435  12.123 1.00 39.90  ? 1293 ARG B O     1 
ATOM   3831  C  CB    . ARG A  1  494 ? 22.791  56.309  10.316 1.00 37.46  ? 1293 ARG B CB    1 
ATOM   3832  C  CG    . ARG A  1  494 ? 22.875  57.589  9.522  1.00 43.26  ? 1293 ARG B CG    1 
ATOM   3833  C  CD    . ARG A  1  494 ? 22.120  57.515  8.203  1.00 45.59  ? 1293 ARG B CD    1 
ATOM   3834  N  NE    . ARG A  1  494 ? 22.742  56.602  7.258  1.00 44.72  ? 1293 ARG B NE    1 
ATOM   3835  C  CZ    . ARG A  1  494 ? 23.853  56.845  6.568  1.00 44.70  ? 1293 ARG B CZ    1 
ATOM   3836  N  NH1   . ARG A  1  494 ? 24.513  57.984  6.694  1.00 45.99  ? 1293 ARG B NH1   1 
ATOM   3837  N  NH2   . ARG A  1  494 ? 24.315  55.927  5.745  1.00 48.70  ? 1293 ARG B NH2   1 
ATOM   3838  N  N     . ASP A  1  495 ? 22.499  54.530  12.925 1.00 39.10  ? 1294 ASP B N     1 
ATOM   3839  C  CA    . ASP A  1  495 ? 22.518  53.158  13.331 1.00 40.25  ? 1294 ASP B CA    1 
ATOM   3840  C  C     . ASP A  1  495 ? 21.697  52.381  12.318 1.00 40.53  ? 1294 ASP B C     1 
ATOM   3841  O  O     . ASP A  1  495 ? 20.495  52.447  12.325 1.00 37.80  ? 1294 ASP B O     1 
ATOM   3842  C  CB    . ASP A  1  495 ? 22.022  52.951  14.765 1.00 38.79  ? 1294 ASP B CB    1 
ATOM   3843  C  CG    . ASP A  1  495 ? 22.320  51.563  15.284 1.00 39.59  ? 1294 ASP B CG    1 
ATOM   3844  O  OD1   . ASP A  1  495 ? 22.883  50.769  14.549 1.00 40.33  ? 1294 ASP B OD1   1 
ATOM   3845  O  OD2   . ASP A  1  495 ? 22.000  51.248  16.437 1.00 42.41  ? 1294 ASP B OD2   1 
ATOM   3846  N  N     . GLU A  1  496 ? 22.385  51.640  11.458 1.00 41.19  ? 1295 GLU B N     1 
ATOM   3847  C  CA    . GLU A  1  496 ? 21.725  50.838  10.433 1.00 41.36  ? 1295 GLU B CA    1 
ATOM   3848  C  C     . GLU A  1  496 ? 21.566  49.382  10.843 1.00 38.99  ? 1295 GLU B C     1 
ATOM   3849  O  O     . GLU A  1  496 ? 21.206  48.538  10.026 1.00 44.62  ? 1295 GLU B O     1 
ATOM   3850  C  CB    . GLU A  1  496 ? 22.486  50.933  9.115  1.00 44.71  ? 1295 GLU B CB    1 
ATOM   3851  C  CG    . GLU A  1  496 ? 22.592  52.367  8.619  1.00 46.38  ? 1295 GLU B CG    1 
ATOM   3852  C  CD    . GLU A  1  496 ? 23.166  52.452  7.209  1.00 44.72  ? 1295 GLU B CD    1 
ATOM   3853  O  OE1   . GLU A  1  496 ? 23.811  51.478  6.724  1.00 49.53  ? 1295 GLU B OE1   1 
ATOM   3854  O  OE2   . GLU A  1  496 ? 22.938  53.495  6.585  1.00 44.82  ? 1295 GLU B OE2   1 
ATOM   3855  N  N     . THR A  1  497 ? 21.841  49.088  12.108 1.00 37.23  ? 1296 THR B N     1 
ATOM   3856  C  CA    . THR A  1  497 ? 21.699  47.744  12.647 1.00 36.85  ? 1296 THR B CA    1 
ATOM   3857  C  C     . THR A  1  497 ? 20.338  47.148  12.342 1.00 41.25  ? 1296 THR B C     1 
ATOM   3858  O  O     . THR A  1  497 ? 19.332  47.830  12.445 1.00 40.01  ? 1296 THR B O     1 
ATOM   3859  C  CB    . THR A  1  497 ? 21.872  47.756  14.173 1.00 33.13  ? 1296 THR B CB    1 
ATOM   3860  O  OG1   . THR A  1  497 ? 23.211  48.176  14.491 1.00 37.12  ? 1296 THR B OG1   1 
ATOM   3861  C  CG2   . THR A  1  497 ? 21.618  46.350  14.767 1.00 31.18  ? 1296 THR B CG2   1 
ATOM   3862  N  N     . SER A  1  498 ? 20.317  45.876  11.965 1.00 43.25  ? 1297 SER B N     1 
ATOM   3863  C  CA    . SER A  1  498 ? 19.067  45.171  11.686 1.00 40.23  ? 1297 SER B CA    1 
ATOM   3864  C  C     . SER A  1  498 ? 19.296  43.708  11.909 1.00 40.79  ? 1297 SER B C     1 
ATOM   3865  O  O     . SER A  1  498 ? 20.437  43.265  12.076 1.00 35.40  ? 1297 SER B O     1 
ATOM   3866  C  CB    . SER A  1  498 ? 18.630  45.410  10.259 1.00 44.49  ? 1297 SER B CB    1 
ATOM   3867  O  OG    . SER A  1  498 ? 19.345  44.573  9.366  1.00 52.11  ? 1297 SER B OG    1 
ATOM   3868  N  N     . LEU A  1  499 ? 18.210  42.943  11.934 1.00 43.07  ? 1298 LEU B N     1 
ATOM   3869  C  CA    . LEU A  1  499 ? 18.335  41.522  12.105 1.00 46.83  ? 1298 LEU B CA    1 
ATOM   3870  C  C     . LEU A  1  499 ? 19.063  40.896  10.938 1.00 48.64  ? 1298 LEU B C     1 
ATOM   3871  O  O     . LEU A  1  499 ? 19.849  40.012  11.125 1.00 55.05  ? 1298 LEU B O     1 
ATOM   3872  C  CB    . LEU A  1  499 ? 16.976  40.900  12.266 1.00 51.63  ? 1298 LEU B CB    1 
ATOM   3873  C  CG    . LEU A  1  499 ? 16.281  40.932  13.634 1.00 54.66  ? 1298 LEU B CG    1 
ATOM   3874  C  CD1   . LEU A  1  499 ? 15.173  39.902  13.569 1.00 54.77  ? 1298 LEU B CD1   1 
ATOM   3875  C  CD2   . LEU A  1  499 ? 17.165  40.619  14.835 1.00 48.10  ? 1298 LEU B CD2   1 
ATOM   3876  N  N     . ARG A  1  500 ? 18.820  41.387  9.734  1.00 49.99  ? 1299 ARG B N     1 
ATOM   3877  C  CA    . ARG A  1  500 ? 19.457  40.902  8.535  1.00 53.11  ? 1299 ARG B CA    1 
ATOM   3878  C  C     . ARG A  1  500 ? 20.936  41.187  8.437  1.00 48.05  ? 1299 ARG B C     1 
ATOM   3879  O  O     . ARG A  1  500 ? 21.706  40.311  8.143  1.00 49.11  ? 1299 ARG B O     1 
ATOM   3880  C  CB    . ARG A  1  500 ? 18.753  41.508  7.358  1.00 61.87  ? 1299 ARG B CB    1 
ATOM   3881  C  CG    . ARG A  1  500 ? 17.315  40.995  7.215  1.00 77.67  ? 1299 ARG B CG    1 
ATOM   3882  C  CD    . ARG A  1  500 ? 16.378  41.210  8.417  1.00 73.92  ? 1299 ARG B CD    1 
ATOM   3883  N  NE    . ARG A  1  500 ? 15.868  42.572  8.466  1.00 67.81  ? 1299 ARG B NE    1 
ATOM   3884  C  CZ    . ARG A  1  500 ? 14.923  42.994  9.298  1.00 68.03  ? 1299 ARG B CZ    1 
ATOM   3885  N  NH1   . ARG A  1  500 ? 14.417  42.173  10.213 1.00 69.81  ? 1299 ARG B NH1   1 
ATOM   3886  N  NH2   . ARG A  1  500 ? 14.504  44.252  9.243  1.00 66.53  ? 1299 ARG B NH2   1 
ATOM   3887  N  N     . THR A  1  501 ? 21.333  42.397  8.761  1.00 51.73  ? 1300 THR B N     1 
ATOM   3888  C  CA    . THR A  1  501 ? 22.713  42.818  8.637  1.00 50.01  ? 1300 THR B CA    1 
ATOM   3889  C  C     . THR A  1  501 ? 23.592  42.738  9.865  1.00 50.10  ? 1300 THR B C     1 
ATOM   3890  O  O     . THR A  1  501 ? 24.807  42.863  9.755  1.00 52.22  ? 1300 THR B O     1 
ATOM   3891  C  CB    . THR A  1  501 ? 22.748  44.241  8.081  1.00 62.33  ? 1300 THR B CB    1 
ATOM   3892  O  OG1   . THR A  1  501 ? 22.723  45.188  9.156  1.00 58.98  ? 1300 THR B OG1   1 
ATOM   3893  C  CG2   . THR A  1  501 ? 21.569  44.444  7.134  1.00 57.57  ? 1300 THR B CG2   1 
ATOM   3894  N  N     . GLY A  1  502 ? 23.037  42.538  11.054 1.00 45.19  ? 1301 GLY B N     1 
ATOM   3895  C  CA    . GLY A  1  502 ? 23.881  42.588  12.238 1.00 39.88  ? 1301 GLY B CA    1 
ATOM   3896  C  C     . GLY A  1  502 ? 24.109  44.039  12.651 1.00 41.50  ? 1301 GLY B C     1 
ATOM   3897  O  O     . GLY A  1  502 ? 23.494  44.924  12.122 1.00 38.56  ? 1301 GLY B O     1 
ATOM   3898  N  N     . VAL A  1  503 ? 24.986  44.272  13.602 1.00 42.75  ? 1302 VAL B N     1 
ATOM   3899  C  CA    . VAL A  1  503 ? 25.318  45.617  14.015 1.00 40.23  ? 1302 VAL B CA    1 
ATOM   3900  C  C     . VAL A  1  503 ? 25.920  46.345  12.844 1.00 39.51  ? 1302 VAL B C     1 
ATOM   3901  O  O     . VAL A  1  503 ? 26.811  45.840  12.181 1.00 36.72  ? 1302 VAL B O     1 
ATOM   3902  C  CB    . VAL A  1  503 ? 26.339  45.563  15.142 1.00 39.98  ? 1302 VAL B CB    1 
ATOM   3903  C  CG1   . VAL A  1  503 ? 26.953  46.927  15.425 1.00 37.77  ? 1302 VAL B CG1   1 
ATOM   3904  C  CG2   . VAL A  1  503 ? 25.685  45.009  16.388 1.00 38.23  ? 1302 VAL B CG2   1 
ATOM   3905  N  N     . ARG A  1  504 ? 25.431  47.544  12.573 1.00 36.35  ? 1303 ARG B N     1 
ATOM   3906  C  CA    . ARG A  1  504 ? 26.070  48.353  11.559 1.00 34.33  ? 1303 ARG B CA    1 
ATOM   3907  C  C     . ARG A  1  504 ? 25.959  49.805  11.946 1.00 34.64  ? 1303 ARG B C     1 
ATOM   3908  O  O     . ARG A  1  504 ? 24.907  50.395  11.841 1.00 35.17  ? 1303 ARG B O     1 
ATOM   3909  C  CB    . ARG A  1  504 ? 25.386  48.112  10.215 1.00 32.79  ? 1303 ARG B CB    1 
ATOM   3910  C  CG    . ARG A  1  504 ? 26.006  48.852  9.060  1.00 32.07  ? 1303 ARG B CG    1 
ATOM   3911  C  CD    . ARG A  1  504 ? 25.253  48.456  7.809  1.00 29.30  ? 1303 ARG B CD    1 
ATOM   3912  N  NE    . ARG A  1  504 ? 25.593  49.378  6.753  1.00 30.43  ? 1303 ARG B NE    1 
ATOM   3913  C  CZ    . ARG A  1  504 ? 26.674  49.273  5.976  1.00 31.77  ? 1303 ARG B CZ    1 
ATOM   3914  N  NH1   . ARG A  1  504 ? 27.531  48.258  6.084  1.00 28.89  ? 1303 ARG B NH1   1 
ATOM   3915  N  NH2   . ARG A  1  504 ? 26.930  50.199  5.088  1.00 29.98  ? 1303 ARG B NH2   1 
ATOM   3916  N  N     . VAL A  1  505 ? 27.033  50.416  12.345 1.00 32.76  ? 1304 VAL B N     1 
ATOM   3917  C  CA    . VAL A  1  505 ? 26.928  51.810  12.736 1.00 31.90  ? 1304 VAL B CA    1 
ATOM   3918  C  C     . VAL A  1  505 ? 27.768  52.558  11.760 1.00 31.56  ? 1304 VAL B C     1 
ATOM   3919  O  O     . VAL A  1  505 ? 28.886  52.162  11.457 1.00 30.36  ? 1304 VAL B O     1 
ATOM   3920  C  CB    . VAL A  1  505 ? 27.469  52.022  14.158 1.00 32.71  ? 1304 VAL B CB    1 
ATOM   3921  C  CG1   . VAL A  1  505 ? 27.390  53.506  14.535 1.00 32.04  ? 1304 VAL B CG1   1 
ATOM   3922  C  CG2   . VAL A  1  505 ? 26.687  51.163  15.127 1.00 29.04  ? 1304 VAL B CG2   1 
ATOM   3923  N  N     . VAL A  1  506 ? 27.226  53.618  11.211 1.00 34.31  ? 1305 VAL B N     1 
ATOM   3924  C  CA    . VAL A  1  506 ? 27.872  54.247  10.063 1.00 33.10  ? 1305 VAL B CA    1 
ATOM   3925  C  C     . VAL A  1  506 ? 28.210  55.680  10.401 1.00 35.72  ? 1305 VAL B C     1 
ATOM   3926  O  O     . VAL A  1  506 ? 27.351  56.424  10.853 1.00 35.76  ? 1305 VAL B O     1 
ATOM   3927  C  CB    . VAL A  1  506 ? 26.924  54.233  8.873  1.00 32.59  ? 1305 VAL B CB    1 
ATOM   3928  C  CG1   . VAL A  1  506 ? 27.523  55.071  7.753  1.00 34.22  ? 1305 VAL B CG1   1 
ATOM   3929  C  CG2   . VAL A  1  506 ? 26.625  52.794  8.448  1.00 34.09  ? 1305 VAL B CG2   1 
ATOM   3930  N  N     . ILE A  1  507 ? 29.448  56.079  10.181 1.00 37.90  ? 1306 ILE B N     1 
ATOM   3931  C  CA    . ILE A  1  507 ? 29.824  57.458  10.420 1.00 37.66  ? 1306 ILE B CA    1 
ATOM   3932  C  C     . ILE A  1  507 ? 30.305  58.045  9.120  1.00 39.26  ? 1306 ILE B C     1 
ATOM   3933  O  O     . ILE A  1  507 ? 31.350  57.653  8.650  1.00 38.16  ? 1306 ILE B O     1 
ATOM   3934  C  CB    . ILE A  1  507 ? 30.946  57.496  11.458 1.00 39.92  ? 1306 ILE B CB    1 
ATOM   3935  C  CG1   . ILE A  1  507 ? 30.442  56.912  12.762 1.00 37.82  ? 1306 ILE B CG1   1 
ATOM   3936  C  CG2   . ILE A  1  507 ? 31.381  58.922  11.738 1.00 43.91  ? 1306 ILE B CG2   1 
ATOM   3937  C  CD1   . ILE A  1  507 ? 31.289  55.819  13.312 1.00 37.21  ? 1306 ILE B CD1   1 
ATOM   3938  N  N     . ASP A  1  508 ? 29.560  58.977  8.525  1.00 41.58  ? 1307 ASP B N     1 
ATOM   3939  C  CA    . ASP A  1  508 ? 30.022  59.644  7.277  1.00 40.38  ? 1307 ASP B CA    1 
ATOM   3940  C  C     . ASP A  1  508 ? 31.101  60.623  7.520  1.00 41.58  ? 1307 ASP B C     1 
ATOM   3941  O  O     . ASP A  1  508 ? 31.127  61.238  8.547  1.00 42.11  ? 1307 ASP B O     1 
ATOM   3942  C  CB    . ASP A  1  508 ? 28.899  60.321  6.602  1.00 41.50  ? 1307 ASP B CB    1 
ATOM   3943  C  CG    . ASP A  1  508 ? 27.966  59.344  5.999  1.00 47.41  ? 1307 ASP B CG    1 
ATOM   3944  O  OD1   . ASP A  1  508 ? 28.363  58.155  5.873  1.00 42.45  ? 1307 ASP B OD1   1 
ATOM   3945  O  OD2   . ASP A  1  508 ? 26.838  59.738  5.659  1.00 48.75  ? 1307 ASP B OD2   1 
ATOM   3946  N  N     . VAL A  1  509 ? 32.019  60.736  6.597  1.00 40.71  ? 1308 VAL B N     1 
ATOM   3947  C  CA    . VAL A  1  509 ? 33.179  61.546  6.820  1.00 44.58  ? 1308 VAL B CA    1 
ATOM   3948  C  C     . VAL A  1  509 ? 33.131  62.601  5.753  1.00 46.83  ? 1308 VAL B C     1 
ATOM   3949  O  O     . VAL A  1  509 ? 32.726  62.309  4.621  1.00 41.89  ? 1308 VAL B O     1 
ATOM   3950  C  CB    . VAL A  1  509 ? 34.425  60.668  6.673  1.00 48.41  ? 1308 VAL B CB    1 
ATOM   3951  C  CG1   . VAL A  1  509 ? 35.672  61.509  6.591  1.00 43.79  ? 1308 VAL B CG1   1 
ATOM   3952  C  CG2   . VAL A  1  509 ? 34.512  59.749  7.873  1.00 45.19  ? 1308 VAL B CG2   1 
ATOM   3953  N  N     . ARG A  1  510 ? 33.513  63.826  6.116  1.00 47.81  ? 1309 ARG B N     1 
ATOM   3954  C  CA    . ARG A  1  510 ? 33.568  64.950  5.180  1.00 48.07  ? 1309 ARG B CA    1 
ATOM   3955  C  C     . ARG A  1  510 ? 34.551  64.648  4.073  1.00 44.89  ? 1309 ARG B C     1 
ATOM   3956  O  O     . ARG A  1  510 ? 35.616  64.107  4.324  1.00 42.97  ? 1309 ARG B O     1 
ATOM   3957  C  CB    . ARG A  1  510 ? 33.997  66.235  5.890  1.00 52.20  ? 1309 ARG B CB    1 
ATOM   3958  C  CG    . ARG A  1  510 ? 34.087  67.456  4.988  1.00 52.54  ? 1309 ARG B CG    1 
ATOM   3959  C  CD    . ARG A  1  510 ? 34.627  68.694  5.695  1.00 52.00  ? 1309 ARG B CD    1 
ATOM   3960  N  NE    . ARG A  1  510 ? 35.988  68.511  6.197  1.00 52.76  ? 1309 ARG B NE    1 
ATOM   3961  C  CZ    . ARG A  1  510 ? 36.341  68.654  7.485  1.00 55.82  ? 1309 ARG B CZ    1 
ATOM   3962  N  NH1   . ARG A  1  510 ? 35.436  68.995  8.409  1.00 52.15  ? 1309 ARG B NH1   1 
ATOM   3963  N  NH2   . ARG A  1  510 ? 37.604  68.459  7.863  1.00 49.61  ? 1309 ARG B NH2   1 
ATOM   3964  N  N     . LYS A  1  511 ? 34.184  65.029  2.852  1.00 46.32  ? 1310 LYS B N     1 
ATOM   3965  C  CA    . LYS A  1  511 ? 35.007  64.827  1.692  1.00 42.97  ? 1310 LYS B CA    1 
ATOM   3966  C  C     . LYS A  1  511 ? 36.392  65.415  1.861  1.00 42.11  ? 1310 LYS B C     1 
ATOM   3967  O  O     . LYS A  1  511 ? 36.542  66.579  2.226  1.00 41.60  ? 1310 LYS B O     1 
ATOM   3968  C  CB    . LYS A  1  511 ? 34.300  65.442  0.489  1.00 45.98  ? 1310 LYS B CB    1 
ATOM   3969  C  CG    . LYS A  1  511 ? 34.986  65.113  -0.842 1.00 50.83  ? 1310 LYS B CG    1 
ATOM   3970  C  CD    . LYS A  1  511 ? 34.089  65.517  -2.011 1.00 53.46  ? 1310 LYS B CD    1 
ATOM   3971  C  CE    . LYS A  1  511 ? 34.460  64.723  -3.240 1.00 59.56  ? 1310 LYS B CE    1 
ATOM   3972  N  NZ    . LYS A  1  511 ? 35.919  64.783  -3.477 1.00 62.97  ? 1310 LYS B NZ    1 
ATOM   3973  N  N     . ASP A  1  512 ? 37.397  64.603  1.569  1.00 43.38  ? 1311 ASP B N     1 
ATOM   3974  C  CA    . ASP A  1  512 ? 38.810  64.995  1.662  1.00 47.31  ? 1311 ASP B CA    1 
ATOM   3975  C  C     . ASP A  1  512 ? 39.374  65.016  3.060  1.00 52.55  ? 1311 ASP B C     1 
ATOM   3976  O  O     . ASP A  1  512 ? 40.567  65.264  3.212  1.00 64.07  ? 1311 ASP B O     1 
ATOM   3977  C  CB    . ASP A  1  512 ? 39.088  66.335  0.993  1.00 56.30  ? 1311 ASP B CB    1 
ATOM   3978  C  CG    . ASP A  1  512 ? 38.742  66.324  -0.481 1.00 66.73  ? 1311 ASP B CG    1 
ATOM   3979  O  OD1   . ASP A  1  512 ? 39.151  65.361  -1.191 1.00 71.66  ? 1311 ASP B OD1   1 
ATOM   3980  O  OD2   . ASP A  1  512 ? 38.096  67.299  -0.938 1.00 76.00  ? 1311 ASP B OD2   1 
ATOM   3981  N  N     . ALA A  1  513 ? 38.553  64.729  4.076  1.00 45.62  ? 1312 ALA B N     1 
ATOM   3982  C  CA    . ALA A  1  513 ? 39.059  64.520  5.419  1.00 45.46  ? 1312 ALA B CA    1 
ATOM   3983  C  C     . ALA A  1  513 ? 39.706  63.140  5.521  1.00 44.52  ? 1312 ALA B C     1 
ATOM   3984  O  O     . ALA A  1  513 ? 39.336  62.232  4.769  1.00 48.35  ? 1312 ALA B O     1 
ATOM   3985  C  CB    . ALA A  1  513 ? 37.938  64.672  6.405  1.00 40.37  ? 1312 ALA B CB    1 
ATOM   3986  N  N     . ASN A  1  514 ? 40.672  62.986  6.424  1.00 42.62  ? 1313 ASN B N     1 
ATOM   3987  C  CA    . ASN A  1  514 ? 41.352  61.715  6.583  1.00 37.17  ? 1313 ASN B CA    1 
ATOM   3988  C  C     . ASN A  1  514 ? 40.517  60.821  7.481  1.00 38.30  ? 1313 ASN B C     1 
ATOM   3989  O  O     . ASN A  1  514 ? 40.404  61.067  8.654  1.00 43.40  ? 1313 ASN B O     1 
ATOM   3990  C  CB    . ASN A  1  514 ? 42.765  61.897  7.123  1.00 37.65  ? 1313 ASN B CB    1 
ATOM   3991  C  CG    . ASN A  1  514 ? 43.567  60.600  7.129  1.00 42.90  ? 1313 ASN B CG    1 
ATOM   3992  O  OD1   . ASN A  1  514 ? 43.053  59.522  7.387  1.00 45.21  ? 1313 ASN B OD1   1 
ATOM   3993  N  ND2   . ASN A  1  514 ? 44.833  60.710  6.888  1.00 43.40  ? 1313 ASN B ND2   1 
ATOM   3994  N  N     . ALA A  1  515 ? 39.918  59.786  6.917  1.00 38.60  ? 1314 ALA B N     1 
ATOM   3995  C  CA    . ALA A  1  515 ? 39.041  58.919  7.703  1.00 37.15  ? 1314 ALA B CA    1 
ATOM   3996  C  C     . ALA A  1  515 ? 39.741  58.070  8.780  1.00 34.15  ? 1314 ALA B C     1 
ATOM   3997  O  O     . ALA A  1  515 ? 39.173  57.816  9.803  1.00 29.31  ? 1314 ALA B O     1 
ATOM   3998  C  CB    . ALA A  1  515 ? 38.185  58.058  6.791  1.00 37.94  ? 1314 ALA B CB    1 
ATOM   3999  N  N     . SER A  1  516 ? 40.957  57.618  8.527  1.00 33.93  ? 1315 SER B N     1 
ATOM   4000  C  CA    . SER A  1  516 ? 41.689  56.889  9.519  1.00 35.64  ? 1315 SER B CA    1 
ATOM   4001  C  C     . SER A  1  516 ? 41.987  57.756  10.744 1.00 40.08  ? 1315 SER B C     1 
ATOM   4002  O  O     . SER A  1  516 ? 42.002  57.267  11.882 1.00 38.64  ? 1315 SER B O     1 
ATOM   4003  C  CB    . SER A  1  516 ? 42.984  56.413  8.902  1.00 37.99  ? 1315 SER B CB    1 
ATOM   4004  O  OG    . SER A  1  516 ? 42.735  55.471  7.871  1.00 42.90  ? 1315 SER B OG    1 
ATOM   4005  N  N     . VAL A  1  517 ? 42.255  59.049  10.513 1.00 43.99  ? 1316 VAL B N     1 
ATOM   4006  C  CA    . VAL A  1  517 ? 42.517  59.998  11.583 1.00 39.58  ? 1316 VAL B CA    1 
ATOM   4007  C  C     . VAL A  1  517 ? 41.254  60.160  12.408 1.00 40.34  ? 1316 VAL B C     1 
ATOM   4008  O  O     . VAL A  1  517 ? 41.304  60.119  13.645 1.00 37.81  ? 1316 VAL B O     1 
ATOM   4009  C  CB    . VAL A  1  517 ? 43.013  61.360  11.026 1.00 40.94  ? 1316 VAL B CB    1 
ATOM   4010  C  CG1   . VAL A  1  517 ? 42.779  62.538  11.987 1.00 37.86  ? 1316 VAL B CG1   1 
ATOM   4011  C  CG2   . VAL A  1  517 ? 44.473  61.249  10.564 1.00 35.62  ? 1316 VAL B CG2   1 
ATOM   4012  N  N     . ILE A  1  518 ? 40.121  60.288  11.725 1.00 37.09  ? 1317 ILE B N     1 
ATOM   4013  C  CA    . ILE A  1  518 ? 38.871  60.457  12.432 1.00 36.32  ? 1317 ILE B CA    1 
ATOM   4014  C  C     . ILE A  1  518 ? 38.568  59.245  13.309 1.00 38.92  ? 1317 ILE B C     1 
ATOM   4015  O  O     . ILE A  1  518 ? 38.137  59.397  14.427 1.00 41.76  ? 1317 ILE B O     1 
ATOM   4016  C  CB    . ILE A  1  518 ? 37.743  60.724  11.466 1.00 38.65  ? 1317 ILE B CB    1 
ATOM   4017  C  CG1   . ILE A  1  518 ? 37.934  62.107  10.830 1.00 39.67  ? 1317 ILE B CG1   1 
ATOM   4018  C  CG2   . ILE A  1  518 ? 36.416  60.693  12.184 1.00 37.71  ? 1317 ILE B CG2   1 
ATOM   4019  C  CD1   . ILE A  1  518 ? 36.922  62.380  9.748  1.00 34.41  ? 1317 ILE B CD1   1 
ATOM   4020  N  N     . LEU A  1  519 ? 38.838  58.047  12.805 1.00 38.48  ? 1318 LEU B N     1 
ATOM   4021  C  CA    . LEU A  1  519 ? 38.608  56.803  13.510 1.00 37.19  ? 1318 LEU B CA    1 
ATOM   4022  C  C     . LEU A  1  519 ? 39.512  56.646  14.715 1.00 38.46  ? 1318 LEU B C     1 
ATOM   4023  O  O     . LEU A  1  519 ? 39.074  56.206  15.745 1.00 32.46  ? 1318 LEU B O     1 
ATOM   4024  C  CB    . LEU A  1  519 ? 38.764  55.617  12.540 1.00 36.61  ? 1318 LEU B CB    1 
ATOM   4025  C  CG    . LEU A  1  519 ? 38.685  54.189  13.067 1.00 37.03  ? 1318 LEU B CG    1 
ATOM   4026  C  CD1   . LEU A  1  519 ? 37.331  53.825  13.658 1.00 35.93  ? 1318 LEU B CD1   1 
ATOM   4027  C  CD2   . LEU A  1  519 ? 39.025  53.195  11.976 1.00 32.62  ? 1318 LEU B CD2   1 
ATOM   4028  N  N     . ASN A  1  520 ? 40.778  56.996  14.575 1.00 36.07  ? 1319 ASN B N     1 
ATOM   4029  C  CA    . ASN A  1  520 ? 41.642  56.959  15.727 1.00 37.55  ? 1319 ASN B CA    1 
ATOM   4030  C  C     . ASN A  1  520 ? 41.191  57.900  16.827 1.00 38.53  ? 1319 ASN B C     1 
ATOM   4031  O  O     . ASN A  1  520 ? 41.311  57.572  17.975 1.00 43.04  ? 1319 ASN B O     1 
ATOM   4032  C  CB    . ASN A  1  520 ? 43.051  57.305  15.327 1.00 38.15  ? 1319 ASN B CB    1 
ATOM   4033  C  CG    . ASN A  1  520 ? 43.779  56.122  14.773 1.00 50.76  ? 1319 ASN B CG    1 
ATOM   4034  O  OD1   . ASN A  1  520 ? 43.690  55.008  15.300 1.00 52.89  ? 1319 ASN B OD1   1 
ATOM   4035  N  ND2   . ASN A  1  520 ? 44.519  56.338  13.696 1.00 56.51  ? 1319 ASN B ND2   1 
ATOM   4036  N  N     . ASN A  1  521 ? 40.660  59.064  16.472 1.00 36.97  ? 1320 ASN B N     1 
ATOM   4037  C  CA    . ASN A  1  521 ? 40.121  59.972  17.435 1.00 37.32  ? 1320 ASN B CA    1 
ATOM   4038  C  C     . ASN A  1  521 ? 38.885  59.452  18.115 1.00 39.85  ? 1320 ASN B C     1 
ATOM   4039  O  O     . ASN A  1  521 ? 38.680  59.662  19.325 1.00 36.69  ? 1320 ASN B O     1 
ATOM   4040  C  CB    . ASN A  1  521 ? 39.780  61.289  16.777 1.00 40.00  ? 1320 ASN B CB    1 
ATOM   4041  C  CG    . ASN A  1  521 ? 41.021  62.126  16.440 1.00 46.92  ? 1320 ASN B CG    1 
ATOM   4042  O  OD1   . ASN A  1  521 ? 42.106  61.965  17.023 1.00 44.47  ? 1320 ASN B OD1   1 
ATOM   4043  N  ND2   . ASN A  1  521 ? 40.866  63.011  15.464 1.00 45.72  ? 1320 ASN B ND2   1 
ATOM   4044  N  N     . LEU A  1  522 ? 38.048  58.772  17.351 1.00 40.62  ? 1321 LEU B N     1 
ATOM   4045  C  CA    . LEU A  1  522 ? 36.873  58.121  17.934 1.00 36.64  ? 1321 LEU B CA    1 
ATOM   4046  C  C     . LEU A  1  522 ? 37.220  57.042  18.945 1.00 35.58  ? 1321 LEU B C     1 
ATOM   4047  O  O     . LEU A  1  522 ? 36.506  56.906  19.905 1.00 38.70  ? 1321 LEU B O     1 
ATOM   4048  C  CB    . LEU A  1  522 ? 36.003  57.569  16.825 1.00 35.22  ? 1321 LEU B CB    1 
ATOM   4049  C  CG    . LEU A  1  522 ? 35.135  58.601  16.108 1.00 36.79  ? 1321 LEU B CG    1 
ATOM   4050  C  CD1   . LEU A  1  522 ? 34.626  58.025  14.787 1.00 39.39  ? 1321 LEU B CD1   1 
ATOM   4051  C  CD2   . LEU A  1  522 ? 33.956  59.092  16.932 1.00 35.44  ? 1321 LEU B CD2   1 
ATOM   4052  N  N     . TYR A  1  523 ? 38.282  56.265  18.712 1.00 37.11  ? 1322 TYR B N     1 
ATOM   4053  C  CA    . TYR A  1  523 ? 38.773  55.306  19.691 1.00 36.86  ? 1322 TYR B CA    1 
ATOM   4054  C  C     . TYR A  1  523 ? 39.238  55.957  20.967 1.00 42.37  ? 1322 TYR B C     1 
ATOM   4055  O  O     . TYR A  1  523 ? 38.925  55.477  22.038 1.00 40.01  ? 1322 TYR B O     1 
ATOM   4056  C  CB    . TYR A  1  523 ? 39.950  54.525  19.109 1.00 36.58  ? 1322 TYR B CB    1 
ATOM   4057  C  CG    . TYR A  1  523 ? 39.627  53.528  18.013 1.00 41.20  ? 1322 TYR B CG    1 
ATOM   4058  C  CD1   . TYR A  1  523 ? 38.485  52.708  18.064 1.00 38.57  ? 1322 TYR B CD1   1 
ATOM   4059  C  CD2   . TYR A  1  523 ? 40.489  53.397  16.934 1.00 38.81  ? 1322 TYR B CD2   1 
ATOM   4060  C  CE1   . TYR A  1  523 ? 38.227  51.797  17.086 1.00 38.50  ? 1322 TYR B CE1   1 
ATOM   4061  C  CE2   . TYR A  1  523 ? 40.261  52.496  15.936 1.00 37.98  ? 1322 TYR B CE2   1 
ATOM   4062  C  CZ    . TYR A  1  523 ? 39.137  51.681  16.026 1.00 46.31  ? 1322 TYR B CZ    1 
ATOM   4063  O  OH    . TYR A  1  523 ? 38.915  50.772  15.028 1.00 45.87  ? 1322 TYR B OH    1 
ATOM   4064  N  N     . LYS A  1  524 ? 39.968  57.073  20.858 1.00 44.64  ? 1323 LYS B N     1 
ATOM   4065  C  CA    . LYS A  1  524 ? 40.465  57.786  22.028 1.00 35.54  ? 1323 LYS B CA    1 
ATOM   4066  C  C     . LYS A  1  524 ? 39.346  58.473  22.808 1.00 38.11  ? 1323 LYS B C     1 
ATOM   4067  O  O     . LYS A  1  524 ? 39.403  58.518  24.042 1.00 38.55  ? 1323 LYS B O     1 
ATOM   4068  C  CB    . LYS A  1  524 ? 41.551  58.797  21.630 1.00 32.15  ? 1323 LYS B CB    1 
ATOM   4069  N  N     . GLN A  1  525 ? 38.318  58.970  22.131 1.00 34.09  ? 1324 GLN B N     1 
ATOM   4070  C  CA    . GLN A  1  525 ? 37.360  59.815  22.818 1.00 36.21  ? 1324 GLN B CA    1 
ATOM   4071  C  C     . GLN A  1  525 ? 35.973  59.260  23.015 1.00 40.21  ? 1324 GLN B C     1 
ATOM   4072  O  O     . GLN A  1  525 ? 35.068  59.970  23.529 1.00 40.94  ? 1324 GLN B O     1 
ATOM   4073  C  CB    . GLN A  1  525 ? 37.205  61.132  22.089 1.00 40.22  ? 1324 GLN B CB    1 
ATOM   4074  C  CG    . GLN A  1  525 ? 38.497  61.847  21.770 1.00 40.78  ? 1324 GLN B CG    1 
ATOM   4075  C  CD    . GLN A  1  525 ? 38.206  62.990  20.810 1.00 51.47  ? 1324 GLN B CD    1 
ATOM   4076  O  OE1   . GLN A  1  525 ? 37.433  63.890  21.137 1.00 65.60  ? 1324 GLN B OE1   1 
ATOM   4077  N  NE2   . GLN A  1  525 ? 38.785  62.955  19.619 1.00 49.55  ? 1324 GLN B NE2   1 
ATOM   4078  N  N     . THR A  1  526 ? 35.756  58.015  22.601 1.00 37.45  ? 1325 THR B N     1 
ATOM   4079  C  CA    . THR A  1  526 ? 34.433  57.381  22.795 1.00 35.05  ? 1325 THR B CA    1 
ATOM   4080  C  C     . THR A  1  526 ? 34.573  55.925  23.252 1.00 34.84  ? 1325 THR B C     1 
ATOM   4081  O  O     . THR A  1  526 ? 35.680  55.339  23.193 1.00 33.03  ? 1325 THR B O     1 
ATOM   4082  C  CB    . THR A  1  526 ? 33.600  57.379  21.464 1.00 40.46  ? 1325 THR B CB    1 
ATOM   4083  O  OG1   . THR A  1  526 ? 34.186  56.460  20.525 1.00 37.08  ? 1325 THR B OG1   1 
ATOM   4084  C  CG2   . THR A  1  526 ? 33.542  58.725  20.821 1.00 36.16  ? 1325 THR B CG2   1 
ATOM   4085  N  N     . PRO A  1  527 ? 33.444  55.276  23.654 1.00 35.43  ? 1326 PRO B N     1 
ATOM   4086  C  CA    . PRO A  1  527 ? 33.552  53.853  23.985 1.00 35.15  ? 1326 PRO B CA    1 
ATOM   4087  C  C     . PRO A  1  527 ? 33.859  52.896  22.811 1.00 37.76  ? 1326 PRO B C     1 
ATOM   4088  O  O     . PRO A  1  527 ? 33.911  51.675  22.980 1.00 41.39  ? 1326 PRO B O     1 
ATOM   4089  C  CB    . PRO A  1  527 ? 32.149  53.522  24.549 1.00 35.45  ? 1326 PRO B CB    1 
ATOM   4090  C  CG    . PRO A  1  527 ? 31.623  54.847  25.029 1.00 35.84  ? 1326 PRO B CG    1 
ATOM   4091  C  CD    . PRO A  1  527 ? 32.051  55.738  23.885 1.00 34.18  ? 1326 PRO B CD    1 
ATOM   4092  N  N     . LEU A  1  528 ? 34.072  53.438  21.636 1.00 35.77  ? 1327 LEU B N     1 
ATOM   4093  C  CA    . LEU A  1  528 ? 34.390  52.639  20.491 1.00 35.71  ? 1327 LEU B CA    1 
ATOM   4094  C  C     . LEU A  1  528 ? 35.668  51.822  20.771 1.00 35.05  ? 1327 LEU B C     1 
ATOM   4095  O  O     . LEU A  1  528 ? 35.858  50.811  20.157 1.00 30.55  ? 1327 LEU B O     1 
ATOM   4096  C  CB    . LEU A  1  528 ? 34.594  53.564  19.331 1.00 39.23  ? 1327 LEU B CB    1 
ATOM   4097  C  CG    . LEU A  1  528 ? 34.381  53.001  17.974 1.00 51.28  ? 1327 LEU B CG    1 
ATOM   4098  C  CD1   . LEU A  1  528 ? 32.896  52.996  17.600 1.00 48.08  ? 1327 LEU B CD1   1 
ATOM   4099  C  CD2   . LEU A  1  528 ? 35.227  53.903  17.090 1.00 51.93  ? 1327 LEU B CD2   1 
ATOM   4100  N  N     . GLN A  1  529 ? 36.510  52.284  21.705 1.00 31.27  ? 1328 GLN B N     1 
ATOM   4101  C  CA    . GLN A  1  529 ? 37.588  51.506  22.249 1.00 31.56  ? 1328 GLN B CA    1 
ATOM   4102  C  C     . GLN A  1  529 ? 37.323  51.602  23.737 1.00 37.23  ? 1328 GLN B C     1 
ATOM   4103  O  O     . GLN A  1  529 ? 36.994  52.698  24.239 1.00 37.18  ? 1328 GLN B O     1 
ATOM   4104  C  CB    . GLN A  1  529 ? 38.959  52.078  21.913 1.00 29.38  ? 1328 GLN B CB    1 
ATOM   4105  C  CG    . GLN A  1  529 ? 40.022  51.353  22.727 1.00 30.94  ? 1328 GLN B CG    1 
ATOM   4106  C  CD    . GLN A  1  529 ? 41.416  51.612  22.248 1.00 34.92  ? 1328 GLN B CD    1 
ATOM   4107  O  OE1   . GLN A  1  529 ? 41.641  51.924  21.088 1.00 38.09  ? 1328 GLN B OE1   1 
ATOM   4108  N  NE2   . GLN A  1  529 ? 42.379  51.422  23.137 1.00 36.44  ? 1328 GLN B NE2   1 
ATOM   4109  N  N     . THR A  1  530 ? 37.398  50.490  24.451 1.00 32.05  ? 1329 THR B N     1 
ATOM   4110  C  CA    . THR A  1  530 ? 37.062  50.526  25.854 1.00 34.13  ? 1329 THR B CA    1 
ATOM   4111  C  C     . THR A  1  530 ? 37.992  49.548  26.519 1.00 34.17  ? 1329 THR B C     1 
ATOM   4112  O  O     . THR A  1  530 ? 38.490  48.643  25.905 1.00 40.89  ? 1329 THR B O     1 
ATOM   4113  C  CB    . THR A  1  530 ? 35.623  50.025  26.043 1.00 36.12  ? 1329 THR B CB    1 
ATOM   4114  O  OG1   . THR A  1  530 ? 34.738  51.084  25.771 1.00 40.42  ? 1329 THR B OG1   1 
ATOM   4115  C  CG2   . THR A  1  530 ? 35.400  49.677  27.443 1.00 31.81  ? 1329 THR B CG2   1 
ATOM   4116  N  N     . SER A  1  531 ? 38.174  49.685  27.795 1.00 33.80  ? 1330 SER B N     1 
ATOM   4117  C  CA    . SER A  1  531 ? 39.008  48.788  28.544 1.00 38.28  ? 1330 SER B CA    1 
ATOM   4118  C  C     . SER A  1  531 ? 38.233  47.819  29.449 1.00 34.94  ? 1330 SER B C     1 
ATOM   4119  O  O     . SER A  1  531 ? 37.280  48.187  30.092 1.00 39.83  ? 1330 SER B O     1 
ATOM   4120  C  CB    . SER A  1  531 ? 39.964  49.616  29.400 1.00 36.24  ? 1330 SER B CB    1 
ATOM   4121  O  OG    . SER A  1  531 ? 40.843  48.746  30.060 1.00 56.10  ? 1330 SER B OG    1 
ATOM   4122  N  N     . PHE A  1  532 ? 38.674  46.574  29.489 1.00 34.91  ? 1331 PHE B N     1 
ATOM   4123  C  CA    . PHE A  1  532 ? 38.118  45.595  30.406 1.00 31.69  ? 1331 PHE B CA    1 
ATOM   4124  C  C     . PHE A  1  532 ? 39.110  45.382  31.509 1.00 29.90  ? 1331 PHE B C     1 
ATOM   4125  O  O     . PHE A  1  532 ? 40.183  44.881  31.261 1.00 35.90  ? 1331 PHE B O     1 
ATOM   4126  C  CB    . PHE A  1  532 ? 37.808  44.279  29.662 1.00 30.73  ? 1331 PHE B CB    1 
ATOM   4127  C  CG    . PHE A  1  532 ? 37.086  43.275  30.500 1.00 31.23  ? 1331 PHE B CG    1 
ATOM   4128  C  CD1   . PHE A  1  532 ? 37.767  42.573  31.501 1.00 26.66  ? 1331 PHE B CD1   1 
ATOM   4129  C  CD2   . PHE A  1  532 ? 35.726  43.038  30.311 1.00 30.18  ? 1331 PHE B CD2   1 
ATOM   4130  C  CE1   . PHE A  1  532 ? 37.107  41.644  32.271 1.00 29.63  ? 1331 PHE B CE1   1 
ATOM   4131  C  CE2   . PHE A  1  532 ? 35.061  42.106  31.103 1.00 29.41  ? 1331 PHE B CE2   1 
ATOM   4132  C  CZ    . PHE A  1  532 ? 35.740  41.401  32.076 1.00 28.59  ? 1331 PHE B CZ    1 
ATOM   4133  N  N     . GLY A  1  533 ? 38.775  45.778  32.728 1.00 30.99  ? 1332 GLY B N     1 
ATOM   4134  C  CA    . GLY A  1  533 ? 39.737  45.644  33.831 1.00 26.67  ? 1332 GLY B CA    1 
ATOM   4135  C  C     . GLY A  1  533 ? 39.551  44.295  34.474 1.00 29.84  ? 1332 GLY B C     1 
ATOM   4136  O  O     . GLY A  1  533 ? 38.571  44.067  35.172 1.00 31.86  ? 1332 GLY B O     1 
ATOM   4137  N  N     . VAL A  1  534 ? 40.480  43.387  34.244 1.00 28.12  ? 1333 VAL B N     1 
ATOM   4138  C  CA    . VAL A  1  534 ? 40.367  42.059  34.775 1.00 25.92  ? 1333 VAL B CA    1 
ATOM   4139  C  C     . VAL A  1  534 ? 40.743  42.078  36.230 1.00 31.01  ? 1333 VAL B C     1 
ATOM   4140  O  O     . VAL A  1  534 ? 41.724  42.668  36.606 1.00 34.39  ? 1333 VAL B O     1 
ATOM   4141  C  CB    . VAL A  1  534 ? 41.274  41.072  34.025 1.00 28.86  ? 1333 VAL B CB    1 
ATOM   4142  C  CG1   . VAL A  1  534 ? 41.153  39.663  34.615 1.00 24.09  ? 1333 VAL B CG1   1 
ATOM   4143  C  CG2   . VAL A  1  534 ? 40.899  41.052  32.529 1.00 27.33  ? 1333 VAL B CG2   1 
ATOM   4144  N  N     . ASN A  1  535 ? 39.928  41.426  37.065 1.00 30.06  ? 1334 ASN B N     1 
ATOM   4145  C  CA    . ASN A  1  535 ? 40.169  41.348  38.484 1.00 28.92  ? 1334 ASN B CA    1 
ATOM   4146  C  C     . ASN A  1  535 ? 39.506  40.032  38.877 1.00 32.17  ? 1334 ASN B C     1 
ATOM   4147  O  O     . ASN A  1  535 ? 38.310  39.994  39.209 1.00 29.38  ? 1334 ASN B O     1 
ATOM   4148  C  CB    . ASN A  1  535 ? 39.510  42.560  39.166 1.00 28.45  ? 1334 ASN B CB    1 
ATOM   4149  C  CG    . ASN A  1  535 ? 39.685  42.546  40.691 1.00 32.34  ? 1334 ASN B CG    1 
ATOM   4150  O  OD1   . ASN A  1  535 ? 40.689  42.064  41.226 1.00 31.67  ? 1334 ASN B OD1   1 
ATOM   4151  N  ND2   . ASN A  1  535 ? 38.704  43.092  41.396 1.00 35.57  ? 1334 ASN B ND2   1 
ATOM   4152  N  N     . MET A  1  536 ? 40.237  38.931  38.765 1.00 29.83  ? 1335 MET B N     1 
ATOM   4153  C  CA    . MET A  1  536 ? 39.594  37.615  38.921 1.00 29.40  ? 1335 MET B CA    1 
ATOM   4154  C  C     . MET A  1  536 ? 39.452  37.138  40.333 1.00 28.90  ? 1335 MET B C     1 
ATOM   4155  O  O     . MET A  1  536 ? 40.292  36.436  40.839 1.00 29.54  ? 1335 MET B O     1 
ATOM   4156  C  CB    . MET A  1  536 ? 40.322  36.570  38.127 1.00 32.90  ? 1335 MET B CB    1 
ATOM   4157  C  CG    . MET A  1  536 ? 40.473  36.957  36.659 1.00 35.30  ? 1335 MET B CG    1 
ATOM   4158  S  SD    . MET A  1  536 ? 40.627  35.549  35.557 1.00 41.75  ? 1335 MET B SD    1 
ATOM   4159  C  CE    . MET A  1  536 ? 42.392  35.251  35.616 1.00 35.56  ? 1335 MET B CE    1 
ATOM   4160  N  N     . ILE A  1  537 ? 38.336  37.498  40.960 1.00 29.07  ? 1336 ILE B N     1 
ATOM   4161  C  CA    . ILE A  1  537 ? 38.075  37.077  42.324 1.00 28.59  ? 1336 ILE B CA    1 
ATOM   4162  C  C     . ILE A  1  537 ? 36.906  36.094  42.303 1.00 30.80  ? 1336 ILE B C     1 
ATOM   4163  O  O     . ILE A  1  537 ? 35.852  36.379  41.746 1.00 31.05  ? 1336 ILE B O     1 
ATOM   4164  C  CB    . ILE A  1  537 ? 37.806  38.294  43.243 1.00 29.17  ? 1336 ILE B CB    1 
ATOM   4165  C  CG1   . ILE A  1  537 ? 39.118  39.068  43.479 1.00 28.78  ? 1336 ILE B CG1   1 
ATOM   4166  C  CG2   . ILE A  1  537 ? 37.169  37.876  44.555 1.00 27.17  ? 1336 ILE B CG2   1 
ATOM   4167  C  CD1   . ILE A  1  537 ? 38.964  40.383  44.193 1.00 23.79  ? 1336 ILE B CD1   1 
ATOM   4168  N  N     . ALA A  1  538 ? 37.085  34.932  42.886 1.00 30.56  ? 1337 ALA B N     1 
ATOM   4169  C  CA    . ALA A  1  538 ? 35.995  33.972  42.939 1.00 29.80  ? 1337 ALA B CA    1 
ATOM   4170  C  C     . ALA A  1  538 ? 36.110  33.366  44.294 1.00 30.27  ? 1337 ALA B C     1 
ATOM   4171  O  O     . ALA A  1  538 ? 37.128  33.488  44.928 1.00 32.95  ? 1337 ALA B O     1 
ATOM   4172  C  CB    . ALA A  1  538 ? 36.149  32.900  41.862 1.00 30.80  ? 1337 ALA B CB    1 
ATOM   4173  N  N     . LEU A  1  539 ? 35.101  32.618  44.707 1.00 27.47  ? 1338 LEU B N     1 
ATOM   4174  C  CA    . LEU A  1  539 ? 35.149  31.986  46.001 1.00 29.76  ? 1338 LEU B CA    1 
ATOM   4175  C  C     . LEU A  1  539 ? 35.804  30.618  45.851 1.00 31.24  ? 1338 LEU B C     1 
ATOM   4176  O  O     . LEU A  1  539 ? 35.421  29.807  45.004 1.00 33.17  ? 1338 LEU B O     1 
ATOM   4177  C  CB    . LEU A  1  539 ? 33.733  31.802  46.541 1.00 28.23  ? 1338 LEU B CB    1 
ATOM   4178  C  CG    . LEU A  1  539 ? 32.822  33.009  46.717 1.00 26.70  ? 1338 LEU B CG    1 
ATOM   4179  C  CD1   . LEU A  1  539 ? 31.407  32.507  46.907 1.00 22.36  ? 1338 LEU B CD1   1 
ATOM   4180  C  CD2   . LEU A  1  539 ? 33.267  33.754  47.917 1.00 26.49  ? 1338 LEU B CD2   1 
ATOM   4181  N  N     . VAL A  1  540 ? 36.781  30.382  46.688 1.00 34.16  ? 1339 VAL B N     1 
ATOM   4182  C  CA    . VAL A  1  540 ? 37.571  29.146  46.712 1.00 31.59  ? 1339 VAL B CA    1 
ATOM   4183  C  C     . VAL A  1  540 ? 37.444  28.624  48.094 1.00 31.35  ? 1339 VAL B C     1 
ATOM   4184  O  O     . VAL A  1  540 ? 37.894  29.266  49.038 1.00 28.96  ? 1339 VAL B O     1 
ATOM   4185  C  CB    . VAL A  1  540 ? 39.059  29.400  46.382 1.00 30.59  ? 1339 VAL B CB    1 
ATOM   4186  C  CG1   . VAL A  1  540 ? 39.869  28.091  46.456 1.00 28.16  ? 1339 VAL B CG1   1 
ATOM   4187  C  CG2   . VAL A  1  540 ? 39.184  30.045  44.995 1.00 28.77  ? 1339 VAL B CG2   1 
ATOM   4188  N  N     . ASN A  1  541 ? 36.820  27.440  48.226 1.00 31.88  ? 1340 ASN B N     1 
ATOM   4189  C  CA    . ASN A  1  541 ? 36.494  26.869  49.544 1.00 36.58  ? 1340 ASN B CA    1 
ATOM   4190  C  C     . ASN A  1  541 ? 35.733  27.877  50.419 1.00 38.02  ? 1340 ASN B C     1 
ATOM   4191  O  O     . ASN A  1  541 ? 35.971  27.975  51.626 1.00 42.48  ? 1340 ASN B O     1 
ATOM   4192  C  CB    . ASN A  1  541 ? 37.728  26.438  50.382 1.00 42.90  ? 1340 ASN B CB    1 
ATOM   4193  C  CG    . ASN A  1  541 ? 38.649  25.482  49.668 1.00 55.86  ? 1340 ASN B CG    1 
ATOM   4194  O  OD1   . ASN A  1  541 ? 38.207  24.506  49.034 1.00 63.83  ? 1340 ASN B OD1   1 
ATOM   4195  N  ND2   . ASN A  1  541 ? 39.975  25.693  49.842 1.00 59.43  ? 1340 ASN B ND2   1 
ATOM   4196  N  N     . GLY A  1  542 ? 34.803  28.610  49.842 1.00 37.53  ? 1341 GLY B N     1 
ATOM   4197  C  CA    . GLY A  1  542 ? 34.013  29.530  50.663 1.00 38.09  ? 1341 GLY B CA    1 
ATOM   4198  C  C     . GLY A  1  542 ? 34.639  30.876  50.989 1.00 38.49  ? 1341 GLY B C     1 
ATOM   4199  O  O     . GLY A  1  542 ? 34.087  31.613  51.760 1.00 38.29  ? 1341 GLY B O     1 
ATOM   4200  N  N     . ARG A  1  543 ? 35.798  31.196  50.427 1.00 35.77  ? 1342 ARG B N     1 
ATOM   4201  C  CA    . ARG A  1  543 ? 36.453  32.453  50.767 1.00 34.38  ? 1342 ARG B CA    1 
ATOM   4202  C  C     . ARG A  1  543 ? 36.806  33.201  49.485 1.00 34.38  ? 1342 ARG B C     1 
ATOM   4203  O  O     . ARG A  1  543 ? 37.206  32.563  48.493 1.00 30.71  ? 1342 ARG B O     1 
ATOM   4204  C  CB    . ARG A  1  543 ? 37.675  32.186  51.630 1.00 40.48  ? 1342 ARG B CB    1 
ATOM   4205  C  CG    . ARG A  1  543 ? 37.301  31.568  52.960 1.00 45.11  ? 1342 ARG B CG    1 
ATOM   4206  C  CD    . ARG A  1  543 ? 38.315  30.518  53.362 1.00 54.86  ? 1342 ARG B CD    1 
ATOM   4207  N  NE    . ARG A  1  543 ? 39.321  31.041  54.273 1.00 64.11  ? 1342 ARG B NE    1 
ATOM   4208  C  CZ    . ARG A  1  543 ? 39.392  30.760  55.582 1.00 61.89  ? 1342 ARG B CZ    1 
ATOM   4209  N  NH1   . ARG A  1  543 ? 40.364  31.290  56.301 1.00 62.63  ? 1342 ARG B NH1   1 
ATOM   4210  N  NH2   . ARG A  1  543 ? 38.512  29.954  56.177 1.00 50.43  ? 1342 ARG B NH2   1 
ATOM   4211  N  N     . PRO A  1  544 ? 36.645  34.555  49.488 1.00 32.45  ? 1343 PRO B N     1 
ATOM   4212  C  CA    . PRO A  1  544 ? 37.028  35.191  48.230 1.00 29.76  ? 1343 PRO B CA    1 
ATOM   4213  C  C     . PRO A  1  544 ? 38.534  35.063  48.042 1.00 30.44  ? 1343 PRO B C     1 
ATOM   4214  O  O     . PRO A  1  544 ? 39.311  35.046  49.041 1.00 30.22  ? 1343 PRO B O     1 
ATOM   4215  C  CB    . PRO A  1  544 ? 36.625  36.666  48.421 1.00 28.48  ? 1343 PRO B CB    1 
ATOM   4216  C  CG    . PRO A  1  544 ? 36.740  36.876  49.899 1.00 31.84  ? 1343 PRO B CG    1 
ATOM   4217  C  CD    . PRO A  1  544 ? 36.217  35.554  50.492 1.00 32.00  ? 1343 PRO B CD    1 
ATOM   4218  N  N     . LYS A  1  545 ? 38.952  34.983  46.780 1.00 30.03  ? 1344 LYS B N     1 
ATOM   4219  C  CA    . LYS A  1  545 ? 40.368  34.860  46.479 1.00 31.27  ? 1344 LYS B CA    1 
ATOM   4220  C  C     . LYS A  1  545 ? 40.662  35.388  45.072 1.00 33.04  ? 1344 LYS B C     1 
ATOM   4221  O  O     . LYS A  1  545 ? 39.937  35.069  44.111 1.00 30.58  ? 1344 LYS B O     1 
ATOM   4222  C  CB    . LYS A  1  545 ? 40.768  33.388  46.621 1.00 32.07  ? 1344 LYS B CB    1 
ATOM   4223  C  CG    . LYS A  1  545 ? 42.256  33.139  46.602 1.00 36.38  ? 1344 LYS B CG    1 
ATOM   4224  C  CD    . LYS A  1  545 ? 42.550  31.643  46.855 1.00 40.75  ? 1344 LYS B CD    1 
ATOM   4225  C  CE    . LYS A  1  545 ? 44.045  31.335  47.098 1.00 40.01  ? 1344 LYS B CE    1 
ATOM   4226  N  NZ    . LYS A  1  545 ? 44.930  31.974  46.040 1.00 47.18  ? 1344 LYS B NZ    1 
ATOM   4227  N  N     . LEU A  1  546 ? 41.746  36.148  44.951 1.00 28.54  ? 1345 LEU B N     1 
ATOM   4228  C  CA    . LEU A  1  546 ? 42.204  36.621  43.668 1.00 29.67  ? 1345 LEU B CA    1 
ATOM   4229  C  C     . LEU A  1  546 ? 42.999  35.500  43.040 1.00 29.83  ? 1345 LEU B C     1 
ATOM   4230  O  O     . LEU A  1  546 ? 43.944  35.056  43.651 1.00 34.71  ? 1345 LEU B O     1 
ATOM   4231  C  CB    . LEU A  1  546 ? 43.060  37.895  43.839 1.00 28.87  ? 1345 LEU B CB    1 
ATOM   4232  C  CG    . LEU A  1  546 ? 43.759  38.398  42.571 1.00 34.88  ? 1345 LEU B CG    1 
ATOM   4233  C  CD1   . LEU A  1  546 ? 42.749  38.693  41.448 1.00 31.69  ? 1345 LEU B CD1   1 
ATOM   4234  C  CD2   . LEU A  1  546 ? 44.603  39.632  42.897 1.00 30.88  ? 1345 LEU B CD2   1 
ATOM   4235  N  N     . ILE A  1  547 ? 42.622  35.041  41.851 1.00 29.84  ? 1346 ILE B N     1 
ATOM   4236  C  CA    . ILE A  1  547 ? 43.253  33.861  41.283 1.00 30.47  ? 1346 ILE B CA    1 
ATOM   4237  C  C     . ILE A  1  547 ? 43.742  34.161  39.886 1.00 34.48  ? 1346 ILE B C     1 
ATOM   4238  O  O     . ILE A  1  547 ? 43.163  34.956  39.162 1.00 32.25  ? 1346 ILE B O     1 
ATOM   4239  C  CB    . ILE A  1  547 ? 42.315  32.621  41.229 1.00 30.58  ? 1346 ILE B CB    1 
ATOM   4240  C  CG1   . ILE A  1  547 ? 41.070  32.918  40.414 1.00 32.72  ? 1346 ILE B CG1   1 
ATOM   4241  C  CG2   . ILE A  1  547 ? 41.840  32.271  42.611 1.00 34.26  ? 1346 ILE B CG2   1 
ATOM   4242  C  CD1   . ILE A  1  547 ? 40.078  31.787  40.405 1.00 29.30  ? 1346 ILE B CD1   1 
ATOM   4243  N  N     . ASN A  1  548 ? 44.797  33.472  39.455 1.00 33.84  ? 1347 ASN B N     1 
ATOM   4244  C  CA    . ASN A  1  548 ? 45.316  33.670  38.114 1.00 30.49  ? 1347 ASN B CA    1 
ATOM   4245  C  C     . ASN A  1  548 ? 44.694  32.583  37.249 1.00 30.11  ? 1347 ASN B C     1 
ATOM   4246  O  O     . ASN A  1  548 ? 43.843  31.828  37.767 1.00 31.15  ? 1347 ASN B O     1 
ATOM   4247  C  CB    . ASN A  1  548 ? 46.868  33.751  38.097 1.00 31.29  ? 1347 ASN B CB    1 
ATOM   4248  C  CG    . ASN A  1  548 ? 47.554  32.429  38.390 1.00 36.83  ? 1347 ASN B CG    1 
ATOM   4249  O  OD1   . ASN A  1  548 ? 46.964  31.353  38.291 1.00 33.98  ? 1347 ASN B OD1   1 
ATOM   4250  N  ND2   . ASN A  1  548 ? 48.841  32.505  38.716 1.00 36.11  ? 1347 ASN B ND2   1 
ATOM   4251  N  N     . LEU A  1  549 ? 45.046  32.521  35.962 1.00 26.53  ? 1348 LEU B N     1 
ATOM   4252  C  CA    . LEU A  1  549 ? 44.434  31.587  35.054 1.00 31.34  ? 1348 LEU B CA    1 
ATOM   4253  C  C     . LEU A  1  549 ? 44.640  30.107  35.417 1.00 33.53  ? 1348 LEU B C     1 
ATOM   4254  O  O     . LEU A  1  549 ? 43.708  29.345  35.325 1.00 34.65  ? 1348 LEU B O     1 
ATOM   4255  C  CB    . LEU A  1  549 ? 44.910  31.817  33.631 1.00 27.61  ? 1348 LEU B CB    1 
ATOM   4256  C  CG    . LEU A  1  549 ? 44.335  30.864  32.573 1.00 35.20  ? 1348 LEU B CG    1 
ATOM   4257  C  CD1   . LEU A  1  549 ? 42.904  31.164  32.167 1.00 33.46  ? 1348 LEU B CD1   1 
ATOM   4258  C  CD2   . LEU A  1  549 ? 45.206  30.867  31.331 1.00 35.56  ? 1348 LEU B CD2   1 
ATOM   4259  N  N     . LYS A  1  550 ? 45.853  29.713  35.786 1.00 30.79  ? 1349 LYS B N     1 
ATOM   4260  C  CA    . LYS A  1  550 ? 46.112  28.336  36.103 1.00 33.66  ? 1349 LYS B CA    1 
ATOM   4261  C  C     . LYS A  1  550 ? 45.399  27.905  37.377 1.00 36.04  ? 1349 LYS B C     1 
ATOM   4262  O  O     . LYS A  1  550 ? 44.920  26.816  37.436 1.00 37.97  ? 1349 LYS B O     1 
ATOM   4263  C  CB    . LYS A  1  550 ? 47.604  28.134  36.266 1.00 29.35  ? 1349 LYS B CB    1 
ATOM   4264  C  CG    . LYS A  1  550 ? 47.944  26.776  36.816 1.00 29.78  ? 1349 LYS B CG    1 
ATOM   4265  C  CD    . LYS A  1  550 ? 49.454  26.546  36.748 1.00 28.25  ? 1349 LYS B CD    1 
ATOM   4266  C  CE    . LYS A  1  550 ? 49.631  25.105  37.150 1.00 30.75  ? 1349 LYS B CE    1 
ATOM   4267  N  NZ    . LYS A  1  550 ? 51.080  24.792  37.084 1.00 33.87  ? 1349 LYS B NZ    1 
ATOM   4268  N  N     . GLU A  1  551 ? 45.362  28.760  38.383 1.00 31.34  ? 1350 GLU B N     1 
ATOM   4269  C  CA    . GLU A  1  551 ? 44.689  28.417  39.606 1.00 31.98  ? 1350 GLU B CA    1 
ATOM   4270  C  C     . GLU A  1  551 ? 43.178  28.221  39.396 1.00 34.94  ? 1350 GLU B C     1 
ATOM   4271  O  O     . GLU A  1  551 ? 42.613  27.377  40.022 1.00 36.60  ? 1350 GLU B O     1 
ATOM   4272  C  CB    . GLU A  1  551 ? 44.932  29.491  40.680 1.00 36.97  ? 1350 GLU B CB    1 
ATOM   4273  C  CG    . GLU A  1  551 ? 44.021  29.317  41.888 1.00 41.44  ? 1350 GLU B CG    1 
ATOM   4274  C  CD    . GLU A  1  551 ? 44.511  29.977  43.153 1.00 43.03  ? 1350 GLU B CD    1 
ATOM   4275  O  OE1   . GLU A  1  551 ? 45.342  30.894  43.072 1.00 46.01  ? 1350 GLU B OE1   1 
ATOM   4276  O  OE2   . GLU A  1  551 ? 44.023  29.571  44.236 1.00 43.45  ? 1350 GLU B OE2   1 
ATOM   4277  N  N     . ALA A  1  552 ? 42.564  29.008  38.510 1.00 33.79  ? 1351 ALA B N     1 
ATOM   4278  C  CA    . ALA A  1  552 ? 41.183  28.822  38.144 1.00 32.48  ? 1351 ALA B CA    1 
ATOM   4279  C  C     . ALA A  1  552 ? 40.962  27.491  37.390 1.00 30.91  ? 1351 ALA B C     1 
ATOM   4280  O  O     . ALA A  1  552 ? 39.972  26.829  37.634 1.00 25.53  ? 1351 ALA B O     1 
ATOM   4281  C  CB    . ALA A  1  552 ? 40.679  29.988  37.323 1.00 26.74  ? 1351 ALA B CB    1 
ATOM   4282  N  N     . LEU A  1  553 ? 41.870  27.113  36.491 1.00 31.10  ? 1352 LEU B N     1 
ATOM   4283  C  CA    . LEU A  1  553 ? 41.768  25.806  35.870 1.00 30.85  ? 1352 LEU B CA    1 
ATOM   4284  C  C     . LEU A  1  553 ? 41.964  24.645  36.809 1.00 32.14  ? 1352 LEU B C     1 
ATOM   4285  O  O     . LEU A  1  553 ? 41.234  23.613  36.719 1.00 30.27  ? 1352 LEU B O     1 
ATOM   4286  C  CB    . LEU A  1  553 ? 42.681  25.742  34.682 1.00 31.96  ? 1352 LEU B CB    1 
ATOM   4287  C  CG    . LEU A  1  553 ? 42.511  26.810  33.579 1.00 28.26  ? 1352 LEU B CG    1 
ATOM   4288  C  CD1   . LEU A  1  553 ? 43.673  26.784  32.599 1.00 31.27  ? 1352 LEU B CD1   1 
ATOM   4289  C  CD2   . LEU A  1  553 ? 41.287  26.496  32.779 1.00 25.57  ? 1352 LEU B CD2   1 
ATOM   4290  N  N     . VAL A  1  554 ? 42.917  24.798  37.719 1.00 33.65  ? 1353 VAL B N     1 
ATOM   4291  C  CA    . VAL A  1  554 ? 43.233  23.745  38.721 1.00 32.59  ? 1353 VAL B CA    1 
ATOM   4292  C  C     . VAL A  1  554 ? 42.017  23.473  39.605 1.00 35.07  ? 1353 VAL B C     1 
ATOM   4293  O  O     . VAL A  1  554 ? 41.610  22.332  39.780 1.00 31.87  ? 1353 VAL B O     1 
ATOM   4294  C  CB    . VAL A  1  554 ? 44.457  24.150  39.570 1.00 32.10  ? 1353 VAL B CB    1 
ATOM   4295  C  CG1   . VAL A  1  554 ? 44.580  23.326  40.830 1.00 29.33  ? 1353 VAL B CG1   1 
ATOM   4296  C  CG2   . VAL A  1  554 ? 45.763  24.038  38.738 1.00 30.34  ? 1353 VAL B CG2   1 
ATOM   4297  N  N     . HIS A  1  555 ? 41.396  24.528  40.138 1.00 33.47  ? 1354 HIS B N     1 
ATOM   4298  C  CA    . HIS A  1  555 ? 40.224  24.323  40.979 1.00 30.75  ? 1354 HIS B CA    1 
ATOM   4299  C  C     . HIS A  1  555 ? 39.080  23.692  40.191 1.00 30.52  ? 1354 HIS B C     1 
ATOM   4300  O  O     . HIS A  1  555 ? 38.363  22.851  40.707 1.00 33.38  ? 1354 HIS B O     1 
ATOM   4301  C  CB    . HIS A  1  555 ? 39.772  25.617  41.605 1.00 32.89  ? 1354 HIS B CB    1 
ATOM   4302  C  CG    . HIS A  1  555 ? 40.713  26.165  42.637 1.00 32.23  ? 1354 HIS B CG    1 
ATOM   4303  N  ND1   . HIS A  1  555 ? 41.208  25.432  43.689 1.00 29.34  ? 1354 HIS B ND1   1 
ATOM   4304  C  CD2   . HIS A  1  555 ? 41.248  27.403  42.755 1.00 31.56  ? 1354 HIS B CD2   1 
ATOM   4305  C  CE1   . HIS A  1  555 ? 42.005  26.196  44.412 1.00 31.23  ? 1354 HIS B CE1   1 
ATOM   4306  N  NE2   . HIS A  1  555 ? 42.047  27.396  43.865 1.00 31.48  ? 1354 HIS B NE2   1 
ATOM   4307  N  N     . TYR A  1  556 ? 38.964  24.050  38.928 1.00 31.01  ? 1355 TYR B N     1 
ATOM   4308  C  CA    . TYR A  1  556 ? 37.951  23.473  38.083 1.00 33.54  ? 1355 TYR B CA    1 
ATOM   4309  C  C     . TYR A  1  556 ? 38.188  21.988  37.822 1.00 33.38  ? 1355 TYR B C     1 
ATOM   4310  O  O     . TYR A  1  556 ? 37.244  21.223  37.887 1.00 33.92  ? 1355 TYR B O     1 
ATOM   4311  C  CB    . TYR A  1  556 ? 37.795  24.240  36.746 1.00 29.36  ? 1355 TYR B CB    1 
ATOM   4312  C  CG    . TYR A  1  556 ? 36.829  23.553  35.911 1.00 29.99  ? 1355 TYR B CG    1 
ATOM   4313  C  CD1   . TYR A  1  556 ? 35.464  23.563  36.265 1.00 32.17  ? 1355 TYR B CD1   1 
ATOM   4314  C  CD2   . TYR A  1  556 ? 37.242  22.808  34.813 1.00 29.78  ? 1355 TYR B CD2   1 
ATOM   4315  C  CE1   . TYR A  1  556 ? 34.543  22.871  35.532 1.00 27.53  ? 1355 TYR B CE1   1 
ATOM   4316  C  CE2   . TYR A  1  556 ? 36.330  22.118  34.059 1.00 28.30  ? 1355 TYR B CE2   1 
ATOM   4317  C  CZ    . TYR A  1  556 ? 34.979  22.151  34.452 1.00 32.12  ? 1355 TYR B CZ    1 
ATOM   4318  O  OH    . TYR A  1  556 ? 34.031  21.497  33.756 1.00 31.07  ? 1355 TYR B OH    1 
ATOM   4319  N  N     . LEU A  1  557 ? 39.425  21.604  37.513 1.00 32.85  ? 1356 LEU B N     1 
ATOM   4320  C  CA    . LEU A  1  557 ? 39.744  20.229  37.248 1.00 32.07  ? 1356 LEU B CA    1 
ATOM   4321  C  C     . LEU A  1  557 ? 39.540  19.400  38.492 1.00 36.98  ? 1356 LEU B C     1 
ATOM   4322  O  O     . LEU A  1  557 ? 39.053  18.275  38.393 1.00 37.98  ? 1356 LEU B O     1 
ATOM   4323  C  CB    . LEU A  1  557 ? 41.174  20.128  36.743 1.00 34.03  ? 1356 LEU B CB    1 
ATOM   4324  C  CG    . LEU A  1  557 ? 41.775  18.730  36.487 1.00 35.60  ? 1356 LEU B CG    1 
ATOM   4325  C  CD1   . LEU A  1  557 ? 40.902  17.958  35.504 1.00 34.33  ? 1356 LEU B CD1   1 
ATOM   4326  C  CD2   . LEU A  1  557 ? 43.180  18.861  35.880 1.00 30.74  ? 1356 LEU B CD2   1 
ATOM   4327  N  N     . GLU A  1  558 ? 39.874  19.960  39.665 1.00 33.03  ? 1357 GLU B N     1 
ATOM   4328  C  CA    . GLU A  1  558 ? 39.674  19.228  40.914 1.00 30.85  ? 1357 GLU B CA    1 
ATOM   4329  C  C     . GLU A  1  558 ? 38.221  18.940  41.149 1.00 31.57  ? 1357 GLU B C     1 
ATOM   4330  O  O     . GLU A  1  558 ? 37.854  17.819  41.534 1.00 35.67  ? 1357 GLU B O     1 
ATOM   4331  C  CB    . GLU A  1  558 ? 40.237  19.978  42.097 1.00 32.79  ? 1357 GLU B CB    1 
ATOM   4332  C  CG    . GLU A  1  558 ? 41.761  19.862  42.218 1.00 45.91  ? 1357 GLU B CG    1 
ATOM   4333  C  CD    . GLU A  1  558 ? 42.237  18.389  42.158 1.00 50.68  ? 1357 GLU B CD    1 
ATOM   4334  O  OE1   . GLU A  1  558 ? 41.710  17.543  42.926 1.00 54.71  ? 1357 GLU B OE1   1 
ATOM   4335  O  OE2   . GLU A  1  558 ? 43.126  18.099  41.334 1.00 48.84  ? 1357 GLU B OE2   1 
ATOM   4336  N  N     . HIS A  1  559 ? 37.390  19.951  40.908 1.00 26.46  ? 1358 HIS B N     1 
ATOM   4337  C  CA    . HIS A  1  559 ? 35.939  19.802  41.065 1.00 26.70  ? 1358 HIS B CA    1 
ATOM   4338  C  C     . HIS A  1  559 ? 35.438  18.669  40.172 1.00 26.69  ? 1358 HIS B C     1 
ATOM   4339  O  O     . HIS A  1  559 ? 34.651  17.852  40.609 1.00 28.74  ? 1358 HIS B O     1 
ATOM   4340  C  CB    . HIS A  1  559 ? 35.268  21.101  40.685 1.00 29.82  ? 1358 HIS B CB    1 
ATOM   4341  C  CG    . HIS A  1  559 ? 33.781  21.065  40.781 1.00 28.79  ? 1358 HIS B CG    1 
ATOM   4342  N  ND1   . HIS A  1  559 ? 33.117  20.676  41.921 1.00 27.49  ? 1358 HIS B ND1   1 
ATOM   4343  C  CD2   . HIS A  1  559 ? 32.828  21.388  39.875 1.00 28.33  ? 1358 HIS B CD2   1 
ATOM   4344  C  CE1   . HIS A  1  559 ? 31.814  20.783  41.721 1.00 27.03  ? 1358 HIS B CE1   1 
ATOM   4345  N  NE2   . HIS A  1  559 ? 31.611  21.207  40.482 1.00 27.66  ? 1358 HIS B NE2   1 
ATOM   4346  N  N     . GLN A  1  560 ? 35.940  18.627  38.930 1.00 28.88  ? 1359 GLN B N     1 
ATOM   4347  C  CA    . GLN A  1  560 ? 35.530  17.607  37.988 1.00 30.22  ? 1359 GLN B CA    1 
ATOM   4348  C  C     . GLN A  1  560 ? 35.966  16.214  38.416 1.00 35.53  ? 1359 GLN B C     1 
ATOM   4349  O  O     . GLN A  1  560 ? 35.236  15.271  38.176 1.00 38.55  ? 1359 GLN B O     1 
ATOM   4350  C  CB    . GLN A  1  560 ? 36.063  17.881  36.583 1.00 27.84  ? 1359 GLN B CB    1 
ATOM   4351  C  CG    . GLN A  1  560 ? 35.511  19.135  35.973 1.00 28.39  ? 1359 GLN B CG    1 
ATOM   4352  C  CD    . GLN A  1  560 ? 34.002  19.120  36.033 1.00 33.74  ? 1359 GLN B CD    1 
ATOM   4353  O  OE1   . GLN A  1  560 ? 33.365  18.398  35.269 1.00 32.22  ? 1359 GLN B OE1   1 
ATOM   4354  N  NE2   . GLN A  1  560 ? 33.428  19.834  36.984 1.00 28.00  ? 1359 GLN B NE2   1 
ATOM   4355  N  N     . LYS A  1  561 ? 37.164  16.090  38.994 1.00 34.55  ? 1360 LYS B N     1 
ATOM   4356  C  CA    . LYS A  1  561 ? 37.683  14.789  39.455 1.00 37.16  ? 1360 LYS B CA    1 
ATOM   4357  C  C     . LYS A  1  561 ? 36.793  14.308  40.576 1.00 37.99  ? 1360 LYS B C     1 
ATOM   4358  O  O     . LYS A  1  561 ? 36.413  13.144  40.629 1.00 35.10  ? 1360 LYS B O     1 
ATOM   4359  C  CB    . LYS A  1  561 ? 39.127  14.930  39.935 1.00 35.51  ? 1360 LYS B CB    1 
ATOM   4360  C  CG    . LYS A  1  561 ? 40.133  14.976  38.763 1.00 38.20  ? 1360 LYS B CG    1 
ATOM   4361  C  CD    . LYS A  1  561 ? 41.473  15.555  39.176 1.00 43.15  ? 1360 LYS B CD    1 
ATOM   4362  C  CE    . LYS A  1  561 ? 42.088  14.773  40.356 1.00 42.10  ? 1360 LYS B CE    1 
ATOM   4363  N  NZ    . LYS A  1  561 ? 43.507  15.209  40.520 1.00 46.33  ? 1360 LYS B NZ    1 
ATOM   4364  N  N     . THR A  1  562 ? 36.457  15.250  41.452 1.00 33.31  ? 1361 THR B N     1 
ATOM   4365  C  CA    . THR A  1  562 ? 35.566  14.991  42.560 1.00 35.24  ? 1361 THR B CA    1 
ATOM   4366  C  C     . THR A  1  562 ? 34.150  14.618  42.100 1.00 39.64  ? 1361 THR B C     1 
ATOM   4367  O  O     . THR A  1  562 ? 33.556  13.697  42.660 1.00 38.71  ? 1361 THR B O     1 
ATOM   4368  C  CB    . THR A  1  562 ? 35.484  16.185  43.494 1.00 35.37  ? 1361 THR B CB    1 
ATOM   4369  O  OG1   . THR A  1  562 ? 36.765  16.404  44.072 1.00 39.95  ? 1361 THR B OG1   1 
ATOM   4370  C  CG2   . THR A  1  562 ? 34.485  15.980  44.595 1.00 35.20  ? 1361 THR B CG2   1 
ATOM   4371  N  N     . VAL A  1  563 ? 33.613  15.316  41.104 1.00 36.83  ? 1362 VAL B N     1 
ATOM   4372  C  CA    . VAL A  1  563 ? 32.271  15.003  40.658 1.00 35.08  ? 1362 VAL B CA    1 
ATOM   4373  C  C     . VAL A  1  563 ? 32.229  13.585  40.058 1.00 39.70  ? 1362 VAL B C     1 
ATOM   4374  O  O     . VAL A  1  563 ? 31.341  12.811  40.348 1.00 36.46  ? 1362 VAL B O     1 
ATOM   4375  C  CB    . VAL A  1  563 ? 31.825  16.034  39.637 1.00 35.44  ? 1362 VAL B CB    1 
ATOM   4376  C  CG1   . VAL A  1  563 ? 30.636  15.529  38.787 1.00 33.31  ? 1362 VAL B CG1   1 
ATOM   4377  C  CG2   . VAL A  1  563 ? 31.515  17.339  40.358 1.00 27.81  ? 1362 VAL B CG2   1 
ATOM   4378  N  N     . VAL A  1  564 ? 33.198  13.270  39.207 1.00 41.74  ? 1363 VAL B N     1 
ATOM   4379  C  CA    . VAL A  1  564 ? 33.269  11.963  38.564 1.00 41.67  ? 1363 VAL B CA    1 
ATOM   4380  C  C     . VAL A  1  564 ? 33.532  10.847  39.576 1.00 40.96  ? 1363 VAL B C     1 
ATOM   4381  O  O     . VAL A  1  564 ? 32.921  9.809   39.502 1.00 43.24  ? 1363 VAL B O     1 
ATOM   4382  C  CB    . VAL A  1  564 ? 34.280  11.973  37.404 1.00 43.59  ? 1363 VAL B CB    1 
ATOM   4383  C  CG1   . VAL A  1  564 ? 34.527  10.580  36.818 1.00 37.19  ? 1363 VAL B CG1   1 
ATOM   4384  C  CG2   . VAL A  1  564 ? 33.793  12.940  36.322 1.00 33.69  ? 1363 VAL B CG2   1 
ATOM   4385  N  N     . ARG A  1  565 ? 34.389  11.095  40.544 1.00 39.60  ? 1364 ARG B N     1 
ATOM   4386  C  CA    . ARG A  1  565 ? 34.667  10.122  41.594 1.00 44.45  ? 1364 ARG B CA    1 
ATOM   4387  C  C     . ARG A  1  565 ? 33.404  9.789   42.399 1.00 44.25  ? 1364 ARG B C     1 
ATOM   4388  O  O     . ARG A  1  565 ? 33.122  8.636   42.710 1.00 43.74  ? 1364 ARG B O     1 
ATOM   4389  C  CB    . ARG A  1  565 ? 35.772  10.611  42.525 1.00 41.21  ? 1364 ARG B CB    1 
ATOM   4390  C  CG    . ARG A  1  565 ? 36.377  9.518   43.394 1.00 43.69  ? 1364 ARG B CG    1 
ATOM   4391  C  CD    . ARG A  1  565 ? 37.435  10.010  44.376 1.00 49.99  ? 1364 ARG B CD    1 
ATOM   4392  N  NE    . ARG A  1  565 ? 38.442  10.868  43.710 1.00 60.43  ? 1364 ARG B NE    1 
ATOM   4393  C  CZ    . ARG A  1  565 ? 38.510  12.205  43.839 1.00 65.95  ? 1364 ARG B CZ    1 
ATOM   4394  N  NH1   . ARG A  1  565 ? 37.654  12.873  44.641 1.00 64.04  ? 1364 ARG B NH1   1 
ATOM   4395  N  NH2   . ARG A  1  565 ? 39.440  12.887  43.178 1.00 63.07  ? 1364 ARG B NH2   1 
ATOM   4396  N  N     . ARG A  1  566 ? 32.669  10.827  42.759 1.00 41.58  ? 1365 ARG B N     1 
ATOM   4397  C  CA    . ARG A  1  566 ? 31.474  10.696  43.539 1.00 34.96  ? 1365 ARG B CA    1 
ATOM   4398  C  C     . ARG A  1  566 ? 30.394  10.076  42.700 1.00 35.61  ? 1365 ARG B C     1 
ATOM   4399  O  O     . ARG A  1  566 ? 29.621  9.304   43.221 1.00 34.72  ? 1365 ARG B O     1 
ATOM   4400  C  CB    . ARG A  1  566 ? 31.039  12.052  44.036 1.00 37.31  ? 1365 ARG B CB    1 
ATOM   4401  C  CG    . ARG A  1  566 ? 31.644  12.388  45.391 1.00 37.49  ? 1365 ARG B CG    1 
ATOM   4402  C  CD    . ARG A  1  566 ? 31.267  13.807  45.805 1.00 40.70  ? 1365 ARG B CD    1 
ATOM   4403  N  NE    . ARG A  1  566 ? 29.913  13.829  46.347 1.00 42.20  ? 1365 ARG B NE    1 
ATOM   4404  C  CZ    . ARG A  1  566 ? 29.491  14.728  47.215 1.00 39.97  ? 1365 ARG B CZ    1 
ATOM   4405  N  NH1   . ARG A  1  566 ? 30.317  15.682  47.622 1.00 37.23  ? 1365 ARG B NH1   1 
ATOM   4406  N  NH2   . ARG A  1  566 ? 28.246  14.682  47.673 1.00 35.63  ? 1365 ARG B NH2   1 
ATOM   4407  N  N     . ARG A  1  567 ? 30.336  10.406  41.407 1.00 32.96  ? 1366 ARG B N     1 
ATOM   4408  C  CA    . ARG A  1  567 ? 29.343  9.841   40.551 1.00 30.76  ? 1366 ARG B CA    1 
ATOM   4409  C  C     . ARG A  1  567 ? 29.587  8.335   40.431 1.00 34.41  ? 1366 ARG B C     1 
ATOM   4410  O  O     . ARG A  1  567 ? 28.634  7.537   40.510 1.00 27.94  ? 1366 ARG B O     1 
ATOM   4411  C  CB    . ARG A  1  567 ? 29.363  10.487  39.169 1.00 32.28  ? 1366 ARG B CB    1 
ATOM   4412  C  CG    . ARG A  1  567 ? 28.215  10.049  38.284 1.00 28.60  ? 1366 ARG B CG    1 
ATOM   4413  C  CD    . ARG A  1  567 ? 28.407  10.370  36.830 1.00 30.93  ? 1366 ARG B CD    1 
ATOM   4414  N  NE    . ARG A  1  567 ? 29.578  9.699   36.282 1.00 35.46  ? 1366 ARG B NE    1 
ATOM   4415  C  CZ    . ARG A  1  567 ? 30.237  10.123  35.208 1.00 38.87  ? 1366 ARG B CZ    1 
ATOM   4416  N  NH1   . ARG A  1  567 ? 29.904  11.268  34.607 1.00 31.80  ? 1366 ARG B NH1   1 
ATOM   4417  N  NH2   . ARG A  1  567 ? 31.282  9.425   34.779 1.00 36.17  ? 1366 ARG B NH2   1 
ATOM   4418  N  N     . THR A  1  568 ? 30.855  7.953   40.257 1.00 35.41  ? 1367 THR B N     1 
ATOM   4419  C  CA    . THR A  1  568 ? 31.203  6.563   40.135 1.00 31.90  ? 1367 THR B CA    1 
ATOM   4420  C  C     . THR A  1  568 ? 30.860  5.773   41.412 1.00 35.89  ? 1367 THR B C     1 
ATOM   4421  O  O     . THR A  1  568 ? 30.355  4.659   41.341 1.00 37.47  ? 1367 THR B O     1 
ATOM   4422  C  CB    . THR A  1  568 ? 32.680  6.441   39.827 1.00 30.82  ? 1367 THR B CB    1 
ATOM   4423  O  OG1   . THR A  1  568 ? 32.905  7.092   38.599 1.00 33.07  ? 1367 THR B OG1   1 
ATOM   4424  C  CG2   . THR A  1  568 ? 33.061  4.950   39.624 1.00 31.46  ? 1367 THR B CG2   1 
ATOM   4425  N  N     . GLN A  1  569 ? 31.147  6.370   42.568 1.00 36.54  ? 1368 GLN B N     1 
ATOM   4426  C  CA    . GLN A  1  569 ? 30.854  5.761   43.839 1.00 41.16  ? 1368 GLN B CA    1 
ATOM   4427  C  C     . GLN A  1  569 ? 29.355  5.586   44.042 1.00 40.64  ? 1368 GLN B C     1 
ATOM   4428  O  O     . GLN A  1  569 ? 28.923  4.594   44.624 1.00 39.56  ? 1368 GLN B O     1 
ATOM   4429  C  CB    . GLN A  1  569 ? 31.439  6.576   44.996 1.00 40.52  ? 1368 GLN B CB    1 
ATOM   4430  C  CG    . GLN A  1  569 ? 32.931  6.396   45.120 1.00 49.26  ? 1368 GLN B CG    1 
ATOM   4431  C  CD    . GLN A  1  569 ? 33.639  7.388   46.012 1.00 50.62  ? 1368 GLN B CD    1 
ATOM   4432  O  OE1   . GLN A  1  569 ? 34.631  7.019   46.616 1.00 55.11  ? 1368 GLN B OE1   1 
ATOM   4433  N  NE2   . GLN A  1  569 ? 33.173  8.654   46.065 1.00 49.18  ? 1368 GLN B NE2   1 
ATOM   4434  N  N     . TYR A  1  570 ? 28.571  6.568   43.592 1.00 39.57  ? 1369 TYR B N     1 
ATOM   4435  C  CA    . TYR A  1  570 ? 27.127  6.491   43.728 1.00 37.39  ? 1369 TYR B CA    1 
ATOM   4436  C  C     . TYR A  1  570 ? 26.600  5.362   42.854 1.00 34.99  ? 1369 TYR B C     1 
ATOM   4437  O  O     . TYR A  1  570 ? 25.804  4.573   43.275 1.00 33.66  ? 1369 TYR B O     1 
ATOM   4438  C  CB    . TYR A  1  570 ? 26.484  7.825   43.313 1.00 36.31  ? 1369 TYR B CB    1 
ATOM   4439  C  CG    . TYR A  1  570 ? 25.003  7.745   43.076 1.00 34.33  ? 1369 TYR B CG    1 
ATOM   4440  C  CD1   . TYR A  1  570 ? 24.111  7.841   44.147 1.00 33.91  ? 1369 TYR B CD1   1 
ATOM   4441  C  CD2   . TYR A  1  570 ? 24.500  7.555   41.787 1.00 33.43  ? 1369 TYR B CD2   1 
ATOM   4442  C  CE1   . TYR A  1  570 ? 22.740  7.811   43.932 1.00 33.66  ? 1369 TYR B CE1   1 
ATOM   4443  C  CE2   . TYR A  1  570 ? 23.129  7.487   41.556 1.00 32.06  ? 1369 TYR B CE2   1 
ATOM   4444  C  CZ    . TYR A  1  570 ? 22.268  7.623   42.632 1.00 33.80  ? 1369 TYR B CZ    1 
ATOM   4445  O  OH    . TYR A  1  570 ? 20.910  7.547   42.413 1.00 37.22  ? 1369 TYR B OH    1 
ATOM   4446  N  N     . ASN A  1  571 ? 27.045  5.339   41.610 1.00 35.51  ? 1370 ASN B N     1 
ATOM   4447  C  CA    . ASN A  1  571 ? 26.633  4.327   40.691 1.00 37.90  ? 1370 ASN B CA    1 
ATOM   4448  C  C     . ASN A  1  571 ? 26.986  2.914   41.156 1.00 38.88  ? 1370 ASN B C     1 
ATOM   4449  O  O     . ASN A  1  571 ? 26.184  1.998   40.979 1.00 34.40  ? 1370 ASN B O     1 
ATOM   4450  C  CB    . ASN A  1  571 ? 27.203  4.607   39.303 1.00 41.42  ? 1370 ASN B CB    1 
ATOM   4451  C  CG    . ASN A  1  571 ? 26.426  5.683   38.565 1.00 41.49  ? 1370 ASN B CG    1 
ATOM   4452  O  OD1   . ASN A  1  571 ? 25.256  5.880   38.818 1.00 50.94  ? 1370 ASN B OD1   1 
ATOM   4453  N  ND2   . ASN A  1  571 ? 27.083  6.387   37.670 1.00 45.53  ? 1370 ASN B ND2   1 
ATOM   4454  N  N     . LEU A  1  572 ? 28.164  2.761   41.771 1.00 38.92  ? 1371 LEU B N     1 
ATOM   4455  C  CA    . LEU A  1  572 ? 28.633  1.493   42.300 1.00 41.05  ? 1371 LEU B CA    1 
ATOM   4456  C  C     . LEU A  1  572 ? 27.760  1.059   43.460 1.00 40.93  ? 1371 LEU B C     1 
ATOM   4457  O  O     . LEU A  1  572 ? 27.357  -0.106  43.513 1.00 40.64  ? 1371 LEU B O     1 
ATOM   4458  C  CB    . LEU A  1  572 ? 30.102  1.583   42.733 1.00 39.19  ? 1371 LEU B CB    1 
ATOM   4459  C  CG    . LEU A  1  572 ? 30.734  0.340   43.398 1.00 33.90  ? 1371 LEU B CG    1 
ATOM   4460  C  CD1   . LEU A  1  572 ? 30.579  -0.858  42.465 1.00 32.37  ? 1371 LEU B CD1   1 
ATOM   4461  C  CD2   . LEU A  1  572 ? 32.193  0.573   43.770 1.00 29.29  ? 1371 LEU B CD2   1 
ATOM   4462  N  N     . ARG A  1  573 ? 27.475  1.986   44.367 1.00 38.99  ? 1372 ARG B N     1 
ATOM   4463  C  CA    . ARG A  1  573 ? 26.580  1.720   45.495 1.00 41.87  ? 1372 ARG B CA    1 
ATOM   4464  C  C     . ARG A  1  573 ? 25.225  1.278   45.002 1.00 41.47  ? 1372 ARG B C     1 
ATOM   4465  O  O     . ARG A  1  573 ? 24.626  0.346   45.544 1.00 41.43  ? 1372 ARG B O     1 
ATOM   4466  C  CB    . ARG A  1  573 ? 26.331  2.962   46.312 1.00 44.23  ? 1372 ARG B CB    1 
ATOM   4467  C  CG    . ARG A  1  573 ? 27.340  3.270   47.395 1.00 47.79  ? 1372 ARG B CG    1 
ATOM   4468  C  CD    . ARG A  1  573 ? 26.704  4.200   48.439 1.00 51.23  ? 1372 ARG B CD    1 
ATOM   4469  N  NE    . ARG A  1  573 ? 26.179  5.439   47.865 1.00 52.39  ? 1372 ARG B NE    1 
ATOM   4470  C  CZ    . ARG A  1  573 ? 26.929  6.487   47.499 1.00 59.66  ? 1372 ARG B CZ    1 
ATOM   4471  N  NH1   . ARG A  1  573 ? 28.252  6.547   47.685 1.00 47.93  ? 1372 ARG B NH1   1 
ATOM   4472  N  NH2   . ARG A  1  573 ? 26.338  7.536   46.987 1.00 54.67  ? 1372 ARG B NH2   1 
ATOM   4473  N  N     . LYS A  1  574 ? 24.756  1.965   43.967 1.00 37.21  ? 1373 LYS B N     1 
ATOM   4474  C  CA    . LYS A  1  574 ? 23.447  1.713   43.408 1.00 42.28  ? 1373 LYS B CA    1 
ATOM   4475  C  C     . LYS A  1  574 ? 23.391  0.369   42.693 1.00 39.24  ? 1373 LYS B C     1 
ATOM   4476  O  O     . LYS A  1  574 ? 22.393  -0.348  42.783 1.00 33.20  ? 1373 LYS B O     1 
ATOM   4477  C  CB    . LYS A  1  574 ? 23.059  2.819   42.444 1.00 44.57  ? 1373 LYS B CB    1 
ATOM   4478  C  CG    . LYS A  1  574 ? 21.617  2.731   41.985 1.00 57.54  ? 1373 LYS B CG    1 
ATOM   4479  C  CD    . LYS A  1  574 ? 21.269  3.740   40.884 1.00 64.52  ? 1373 LYS B CD    1 
ATOM   4480  C  CE    . LYS A  1  574 ? 19.760  3.884   40.742 1.00 63.12  ? 1373 LYS B CE    1 
ATOM   4481  N  NZ    . LYS A  1  574 ? 19.133  4.439   41.993 1.00 72.39  ? 1373 LYS B NZ    1 
ATOM   4482  N  N     . ALA A  1  575 ? 24.444  0.063   41.965 1.00 35.93  ? 1374 ALA B N     1 
ATOM   4483  C  CA    . ALA A  1  575 ? 24.505  -1.145  41.198 1.00 40.35  ? 1374 ALA B CA    1 
ATOM   4484  C  C     . ALA A  1  575 ? 24.585  -2.377  42.128 1.00 42.09  ? 1374 ALA B C     1 
ATOM   4485  O  O     . ALA A  1  575 ? 23.957  -3.346  41.871 1.00 44.25  ? 1374 ALA B O     1 
ATOM   4486  C  CB    . ALA A  1  575 ? 25.669  -1.086  40.230 1.00 34.31  ? 1374 ALA B CB    1 
ATOM   4487  N  N     . LYS A  1  576 ? 25.351  -2.318  43.189 1.00 42.34  ? 1375 LYS B N     1 
ATOM   4488  C  CA    . LYS A  1  576 ? 25.354  -3.378  44.167 1.00 43.17  ? 1375 LYS B CA    1 
ATOM   4489  C  C     . LYS A  1  576 ? 24.049  -3.530  44.873 1.00 40.86  ? 1375 LYS B C     1 
ATOM   4490  O  O     . LYS A  1  576 ? 23.684  -4.643  45.219 1.00 37.99  ? 1375 LYS B O     1 
ATOM   4491  C  CB    . LYS A  1  576 ? 26.416  -3.132  45.196 1.00 37.04  ? 1375 LYS B CB    1 
ATOM   4492  C  CG    . LYS A  1  576 ? 27.774  -3.374  44.616 1.00 43.79  ? 1375 LYS B CG    1 
ATOM   4493  C  CD    . LYS A  1  576 ? 28.795  -3.049  45.660 1.00 44.11  ? 1375 LYS B CD    1 
ATOM   4494  C  CE    . LYS A  1  576 ? 30.150  -3.464  45.135 1.00 50.73  ? 1375 LYS B CE    1 
ATOM   4495  N  NZ    . LYS A  1  576 ? 31.203  -2.806  45.963 1.00 66.05  ? 1375 LYS B NZ    1 
ATOM   4496  N  N     . ASP A  1  577 ? 23.373  -2.421  45.148 1.00 37.26  ? 1376 ASP B N     1 
ATOM   4497  C  CA    . ASP A  1  577 ? 22.079  -2.505  45.809 1.00 36.62  ? 1376 ASP B CA    1 
ATOM   4498  C  C     . ASP A  1  577 ? 21.154  -3.298  44.913 1.00 32.79  ? 1376 ASP B C     1 
ATOM   4499  O  O     . ASP A  1  577 ? 20.440  -4.154  45.373 1.00 33.00  ? 1376 ASP B O     1 
ATOM   4500  C  CB    . ASP A  1  577 ? 21.490  -1.124  46.097 1.00 37.85  ? 1376 ASP B CB    1 
ATOM   4501  C  CG    . ASP A  1  577 ? 22.070  -0.473  47.354 1.00 43.97  ? 1376 ASP B CG    1 
ATOM   4502  O  OD1   . ASP A  1  577 ? 22.681  -1.120  48.247 1.00 43.99  ? 1376 ASP B OD1   1 
ATOM   4503  O  OD2   . ASP A  1  577 ? 21.914  0.760   47.457 1.00 49.75  ? 1376 ASP B OD2   1 
ATOM   4504  N  N     . ARG A  1  578 ? 21.223  -3.022  43.612 1.00 31.04  ? 1377 ARG B N     1 
ATOM   4505  C  CA    . ARG A  1  578 ? 20.361  -3.625  42.649 1.00 31.86  ? 1377 ARG B CA    1 
ATOM   4506  C  C     . ARG A  1  578 ? 20.708  -5.109  42.436 1.00 33.74  ? 1377 ARG B C     1 
ATOM   4507  O  O     . ARG A  1  578 ? 19.827  -5.924  42.348 1.00 30.66  ? 1377 ARG B O     1 
ATOM   4508  C  CB    . ARG A  1  578 ? 20.427  -2.865  41.329 1.00 27.36  ? 1377 ARG B CB    1 
ATOM   4509  C  CG    . ARG A  1  578 ? 19.517  -3.434  40.241 1.00 28.41  ? 1377 ARG B CG    1 
ATOM   4510  C  CD    . ARG A  1  578 ? 18.036  -3.541  40.655 1.00 32.74  ? 1377 ARG B CD    1 
ATOM   4511  N  NE    . ARG A  1  578 ? 17.259  -4.058  39.553 1.00 31.85  ? 1377 ARG B NE    1 
ATOM   4512  C  CZ    . ARG A  1  578 ? 15.950  -4.325  39.608 1.00 37.97  ? 1377 ARG B CZ    1 
ATOM   4513  N  NH1   . ARG A  1  578 ? 15.193  -4.103  40.678 1.00 37.84  ? 1377 ARG B NH1   1 
ATOM   4514  N  NH2   . ARG A  1  578 ? 15.339  -4.802  38.558 1.00 34.79  ? 1377 ARG B NH2   1 
ATOM   4515  N  N     . ALA A  1  579 ? 21.982  -5.429  42.385 1.00 30.61  ? 1378 ALA B N     1 
ATOM   4516  C  CA    . ALA A  1  579 ? 22.383  -6.791  42.206 1.00 34.97  ? 1378 ALA B CA    1 
ATOM   4517  C  C     . ALA A  1  579 ? 21.854  -7.634  43.357 1.00 35.82  ? 1378 ALA B C     1 
ATOM   4518  O  O     . ALA A  1  579 ? 21.384  -8.731  43.144 1.00 38.88  ? 1378 ALA B O     1 
ATOM   4519  C  CB    . ALA A  1  579 ? 23.874  -6.840  42.129 1.00 32.44  ? 1378 ALA B CB    1 
ATOM   4520  N  N     . HIS A  1  580 ? 21.884  -7.061  44.560 1.00 37.04  ? 1379 HIS B N     1 
ATOM   4521  C  CA    . HIS A  1  580 ? 21.410  -7.701  45.716 1.00 35.75  ? 1379 HIS B CA    1 
ATOM   4522  C  C     . HIS A  1  580 ? 19.931  -8.018  45.649 1.00 39.55  ? 1379 HIS B C     1 
ATOM   4523  O  O     . HIS A  1  580 ? 19.544  -9.107  46.017 1.00 46.24  ? 1379 HIS B O     1 
ATOM   4524  C  CB    . HIS A  1  580 ? 21.723  -6.843  46.913 1.00 33.84  ? 1379 HIS B CB    1 
ATOM   4525  C  CG    . HIS A  1  580 ? 21.338  -7.448  48.209 1.00 34.24  ? 1379 HIS B CG    1 
ATOM   4526  N  ND1   . HIS A  1  580 ? 22.134  -8.369  48.855 1.00 39.28  ? 1379 HIS B ND1   1 
ATOM   4527  C  CD2   . HIS A  1  580 ? 20.251  -7.270  48.993 1.00 38.84  ? 1379 HIS B CD2   1 
ATOM   4528  C  CE1   . HIS A  1  580 ? 21.576  -8.707  50.002 1.00 42.30  ? 1379 HIS B CE1   1 
ATOM   4529  N  NE2   . HIS A  1  580 ? 20.421  -8.067  50.102 1.00 45.33  ? 1379 HIS B NE2   1 
ATOM   4530  N  N     . ILE A  1  581 ? 19.124  -7.092  45.158 1.00 36.15  ? 1380 ILE B N     1 
ATOM   4531  C  CA    . ILE A  1  581 ? 17.709  -7.341  45.012 1.00 39.64  ? 1380 ILE B CA    1 
ATOM   4532  C  C     . ILE A  1  581 ? 17.458  -8.482  44.032 1.00 38.56  ? 1380 ILE B C     1 
ATOM   4533  O  O     . ILE A  1  581 ? 16.596  -9.302  44.262 1.00 40.61  ? 1380 ILE B O     1 
ATOM   4534  C  CB    . ILE A  1  581 ? 16.963  -6.064  44.502 1.00 36.43  ? 1380 ILE B CB    1 
ATOM   4535  C  CG1   . ILE A  1  581 ? 16.950  -4.944  45.551 1.00 32.23  ? 1380 ILE B CG1   1 
ATOM   4536  C  CG2   . ILE A  1  581 ? 15.552  -6.402  44.082 1.00 33.26  ? 1380 ILE B CG2   1 
ATOM   4537  C  CD1   . ILE A  1  581 ? 16.472  -5.352  46.928 1.00 31.44  ? 1380 ILE B CD1   1 
ATOM   4538  N  N     . LEU A  1  582 ? 18.187  -8.482  42.916 1.00 38.86  ? 1381 LEU B N     1 
ATOM   4539  C  CA    . LEU A  1  582 ? 18.014  -9.453  41.884 1.00 40.61  ? 1381 LEU B CA    1 
ATOM   4540  C  C     . LEU A  1  582 ? 18.418  -10.847 42.344 1.00 42.28  ? 1381 LEU B C     1 
ATOM   4541  O  O     . LEU A  1  582 ? 17.870  -11.817 41.896 1.00 41.78  ? 1381 LEU B O     1 
ATOM   4542  C  CB    . LEU A  1  582 ? 18.844  -9.075  40.687 1.00 40.21  ? 1381 LEU B CB    1 
ATOM   4543  C  CG    . LEU A  1  582 ? 18.347  -7.883  39.888 1.00 40.76  ? 1381 LEU B CG    1 
ATOM   4544  C  CD1   . LEU A  1  582 ? 19.380  -7.497  38.841 1.00 38.78  ? 1381 LEU B CD1   1 
ATOM   4545  C  CD2   . LEU A  1  582 ? 17.022  -8.174  39.219 1.00 40.79  ? 1381 LEU B CD2   1 
ATOM   4546  N  N     . GLU A  1  583 ? 19.349  -10.931 43.261 1.00 38.26  ? 1382 GLU B N     1 
ATOM   4547  C  CA    . GLU A  1  583 ? 19.716  -12.213 43.807 1.00 40.24  ? 1382 GLU B CA    1 
ATOM   4548  C  C     . GLU A  1  583 ? 18.550  -12.714 44.646 1.00 44.15  ? 1382 GLU B C     1 
ATOM   4549  O  O     . GLU A  1  583 ? 18.312  -13.895 44.693 1.00 40.37  ? 1382 GLU B O     1 
ATOM   4550  C  CB    . GLU A  1  583 ? 20.964  -12.078 44.661 1.00 33.87  ? 1382 GLU B CB    1 
ATOM   4551  C  CG    . GLU A  1  583 ? 22.189  -11.966 43.788 1.00 34.65  ? 1382 GLU B CG    1 
ATOM   4552  C  CD    . GLU A  1  583 ? 23.335  -11.373 44.515 1.00 37.67  ? 1382 GLU B CD    1 
ATOM   4553  O  OE1   . GLU A  1  583 ? 23.211  -11.097 45.739 1.00 40.96  ? 1382 GLU B OE1   1 
ATOM   4554  O  OE2   . GLU A  1  583 ? 24.363  -11.165 43.863 1.00 41.44  ? 1382 GLU B OE2   1 
ATOM   4555  N  N     . GLY A  1  584 ? 17.811  -11.803 45.272 1.00 40.06  ? 1383 GLY B N     1 
ATOM   4556  C  CA    . GLY A  1  584 ? 16.660  -12.209 46.033 1.00 36.80  ? 1383 GLY B CA    1 
ATOM   4557  C  C     . GLY A  1  584 ? 15.515  -12.591 45.111 1.00 37.78  ? 1383 GLY B C     1 
ATOM   4558  O  O     . GLY A  1  584 ? 14.705  -13.443 45.457 1.00 45.46  ? 1383 GLY B O     1 
ATOM   4559  N  N     . LEU A  1  585 ? 15.417  -11.934 43.965 1.00 35.42  ? 1384 LEU B N     1 
ATOM   4560  C  CA    . LEU A  1  585 ? 14.341  -12.198 43.017 1.00 37.36  ? 1384 LEU B CA    1 
ATOM   4561  C  C     . LEU A  1  585 ? 14.615  -13.516 42.297 1.00 37.85  ? 1384 LEU B C     1 
ATOM   4562  O  O     . LEU A  1  585 ? 13.674  -14.228 41.954 1.00 34.18  ? 1384 LEU B O     1 
ATOM   4563  C  CB    . LEU A  1  585 ? 14.154  -11.063 42.006 1.00 30.23  ? 1384 LEU B CB    1 
ATOM   4564  C  CG    . LEU A  1  585 ? 13.611  -9.764  42.621 1.00 37.09  ? 1384 LEU B CG    1 
ATOM   4565  C  CD1   . LEU A  1  585 ? 13.530  -8.684  41.583 1.00 35.85  ? 1384 LEU B CD1   1 
ATOM   4566  C  CD2   . LEU A  1  585 ? 12.243  -9.884  43.224 1.00 36.17  ? 1384 LEU B CD2   1 
ATOM   4567  N  N     A ARG A  1  586 ? 15.896  -13.806 42.064 0.50 36.34  ? 1385 ARG B N     1 
ATOM   4568  N  N     B ARG A  1  586 ? 15.895  -13.842 42.115 0.50 37.34  ? 1385 ARG B N     1 
ATOM   4569  C  CA    A ARG A  1  586 ? 16.303  -15.024 41.409 0.50 37.32  ? 1385 ARG B CA    1 
ATOM   4570  C  CA    B ARG A  1  586 ? 16.323  -15.060 41.459 0.50 38.99  ? 1385 ARG B CA    1 
ATOM   4571  C  C     A ARG A  1  586 ? 15.900  -16.188 42.316 0.50 39.09  ? 1385 ARG B C     1 
ATOM   4572  C  C     B ARG A  1  586 ? 15.876  -16.188 42.335 0.50 40.21  ? 1385 ARG B C     1 
ATOM   4573  O  O     A ARG A  1  586 ? 15.310  -17.158 41.834 0.50 39.11  ? 1385 ARG B O     1 
ATOM   4574  O  O     B ARG A  1  586 ? 15.250  -17.115 41.869 0.50 39.89  ? 1385 ARG B O     1 
ATOM   4575  C  CB    A ARG A  1  586 ? 17.808  -15.020 41.103 0.50 37.38  ? 1385 ARG B CB    1 
ATOM   4576  C  CB    B ARG A  1  586 ? 17.842  -15.115 41.377 0.50 40.92  ? 1385 ARG B CB    1 
ATOM   4577  C  CG    A ARG A  1  586 ? 18.662  -15.672 42.174 0.50 39.32  ? 1385 ARG B CG    1 
ATOM   4578  C  CG    B ARG A  1  586 ? 18.458  -15.515 40.059 0.50 42.58  ? 1385 ARG B CG    1 
ATOM   4579  C  CD    A ARG A  1  586 ? 20.123  -15.694 41.797 0.50 35.21  ? 1385 ARG B CD    1 
ATOM   4580  C  CD    B ARG A  1  586 ? 18.231  -16.962 39.615 0.50 42.61  ? 1385 ARG B CD    1 
ATOM   4581  N  NE    A ARG A  1  586 ? 21.026  -15.720 42.932 0.50 29.98  ? 1385 ARG B NE    1 
ATOM   4582  N  NE    B ARG A  1  586 ? 16.846  -17.291 39.208 0.50 44.68  ? 1385 ARG B NE    1 
ATOM   4583  C  CZ    A ARG A  1  586 ? 22.321  -15.466 42.822 0.50 26.93  ? 1385 ARG B CZ    1 
ATOM   4584  C  CZ    B ARG A  1  586 ? 16.314  -17.011 38.016 0.50 47.67  ? 1385 ARG B CZ    1 
ATOM   4585  N  NH1   A ARG A  1  586 ? 22.813  -15.157 41.626 0.50 25.86  ? 1385 ARG B NH1   1 
ATOM   4586  N  NH1   B ARG A  1  586 ? 17.012  -16.364 37.095 0.50 54.43  ? 1385 ARG B NH1   1 
ATOM   4587  N  NH2   A ARG A  1  586 ? 23.122  -15.538 43.881 0.50 22.90  ? 1385 ARG B NH2   1 
ATOM   4588  N  NH2   B ARG A  1  586 ? 15.070  -17.364 37.733 0.50 47.48  ? 1385 ARG B NH2   1 
ATOM   4589  N  N     . ILE A  1  587 ? 16.168  -16.058 43.627 1.00 41.24  ? 1386 ILE B N     1 
ATOM   4590  C  CA    . ILE A  1  587 ? 15.846  -17.060 44.593 1.00 34.97  ? 1386 ILE B CA    1 
ATOM   4591  C  C     . ILE A  1  587 ? 14.347  -17.224 44.722 1.00 38.01  ? 1386 ILE B C     1 
ATOM   4592  O  O     . ILE A  1  587 ? 13.858  -18.324 44.868 1.00 45.40  ? 1386 ILE B O     1 
ATOM   4593  C  CB    . ILE A  1  587 ? 16.453  -16.742 45.965 1.00 41.06  ? 1386 ILE B CB    1 
ATOM   4594  C  CG1   . ILE A  1  587 ? 17.962  -17.070 46.009 1.00 41.88  ? 1386 ILE B CG1   1 
ATOM   4595  C  CG2   . ILE A  1  587 ? 15.713  -17.469 47.092 1.00 36.89  ? 1386 ILE B CG2   1 
ATOM   4596  C  CD1   . ILE A  1  587 ? 18.666  -16.434 47.216 1.00 39.15  ? 1386 ILE B CD1   1 
ATOM   4597  N  N     . ALA A  1  588 ? 13.612  -16.139 44.679 1.00 33.26  ? 1387 ALA B N     1 
ATOM   4598  C  CA    . ALA A  1  588 ? 12.183  -16.221 44.770 1.00 34.91  ? 1387 ALA B CA    1 
ATOM   4599  C  C     . ALA A  1  588 ? 11.568  -16.945 43.605 1.00 36.36  ? 1387 ALA B C     1 
ATOM   4600  O  O     . ALA A  1  588 ? 10.649  -17.706 43.826 1.00 38.19  ? 1387 ALA B O     1 
ATOM   4601  C  CB    . ALA A  1  588 ? 11.573  -14.830 44.896 1.00 34.69  ? 1387 ALA B CB    1 
ATOM   4602  N  N     . LEU A  1  589 ? 12.001  -16.654 42.374 1.00 35.84  ? 1388 LEU B N     1 
ATOM   4603  C  CA    . LEU A  1  589 ? 11.448  -17.320 41.197 1.00 37.10  ? 1388 LEU B CA    1 
ATOM   4604  C  C     . LEU A  1  589 ? 11.833  -18.798 41.157 1.00 36.96  ? 1388 LEU B C     1 
ATOM   4605  O  O     . LEU A  1  589 ? 11.064  -19.597 40.730 1.00 40.59  ? 1388 LEU B O     1 
ATOM   4606  C  CB    . LEU A  1  589 ? 11.931  -16.643 39.924 1.00 36.62  ? 1388 LEU B CB    1 
ATOM   4607  C  CG    . LEU A  1  589 ? 11.550  -15.176 39.692 1.00 41.45  ? 1388 LEU B CG    1 
ATOM   4608  C  CD1   . LEU A  1  589 ? 12.255  -14.572 38.488 1.00 39.19  ? 1388 LEU B CD1   1 
ATOM   4609  C  CD2   . LEU A  1  589 ? 10.070  -14.884 39.635 1.00 33.18  ? 1388 LEU B CD2   1 
ATOM   4610  N  N     . ASP A  1  590 ? 13.031  -19.145 41.603 1.00 40.46  ? 1389 ASP B N     1 
ATOM   4611  C  CA    . ASP A  1  590 ? 13.477  -20.518 41.655 1.00 38.37  ? 1389 ASP B CA    1 
ATOM   4612  C  C     . ASP A  1  590 ? 12.694  -21.338 42.622 1.00 39.36  ? 1389 ASP B C     1 
ATOM   4613  O  O     . ASP A  1  590 ? 12.651  -22.500 42.476 1.00 45.43  ? 1389 ASP B O     1 
ATOM   4614  C  CB    . ASP A  1  590 ? 14.928  -20.549 42.043 1.00 34.95  ? 1389 ASP B CB    1 
ATOM   4615  C  CG    . ASP A  1  590 ? 15.834  -20.128 40.892 1.00 39.06  ? 1389 ASP B CG    1 
ATOM   4616  O  OD1   . ASP A  1  590 ? 15.311  -19.964 39.763 1.00 37.59  ? 1389 ASP B OD1   1 
ATOM   4617  O  OD2   . ASP A  1  590 ? 17.070  -19.968 41.123 1.00 47.07  ? 1389 ASP B OD2   1 
ATOM   4618  N  N     . HIS A  1  591 ? 12.090  -20.729 43.622 1.00 35.95  ? 1390 HIS B N     1 
ATOM   4619  C  CA    . HIS A  1  591 ? 11.366  -21.423 44.624 1.00 35.29  ? 1390 HIS B CA    1 
ATOM   4620  C  C     . HIS A  1  591 ? 9.980   -20.905 44.735 1.00 35.07  ? 1390 HIS B C     1 
ATOM   4621  O  O     . HIS A  1  591 ? 9.453   -20.859 45.813 1.00 33.57  ? 1390 HIS B O     1 
ATOM   4622  C  CB    . HIS A  1  591 ? 12.050  -21.233 45.965 1.00 32.86  ? 1390 HIS B CB    1 
ATOM   4623  C  CG    . HIS A  1  591 ? 13.411  -21.804 45.981 1.00 38.96  ? 1390 HIS B CG    1 
ATOM   4624  N  ND1   . HIS A  1  591 ? 13.637  -23.160 46.040 1.00 39.92  ? 1390 HIS B ND1   1 
ATOM   4625  C  CD2   . HIS A  1  591 ? 14.618  -21.226 45.822 1.00 37.46  ? 1390 HIS B CD2   1 
ATOM   4626  C  CE1   . HIS A  1  591 ? 14.933  -23.383 45.963 1.00 40.66  ? 1390 HIS B CE1   1 
ATOM   4627  N  NE2   . HIS A  1  591 ? 15.551  -22.223 45.836 1.00 38.57  ? 1390 HIS B NE2   1 
ATOM   4628  N  N     . ILE A  1  592 ? 9.388   -20.504 43.634 1.00 36.11  ? 1391 ILE B N     1 
ATOM   4629  C  CA    . ILE A  1  592 ? 8.195   -19.684 43.690 1.00 39.00  ? 1391 ILE B CA    1 
ATOM   4630  C  C     . ILE A  1  592 ? 6.972   -20.292 44.355 1.00 42.84  ? 1391 ILE B C     1 
ATOM   4631  O  O     . ILE A  1  592 ? 6.217   -19.573 44.965 1.00 38.92  ? 1391 ILE B O     1 
ATOM   4632  C  CB    . ILE A  1  592 ? 7.836   -19.140 42.290 1.00 39.98  ? 1391 ILE B CB    1 
ATOM   4633  C  CG1   . ILE A  1  592 ? 6.808   -18.021 42.396 1.00 44.37  ? 1391 ILE B CG1   1 
ATOM   4634  C  CG2   . ILE A  1  592 ? 7.226   -20.203 41.404 1.00 35.95  ? 1391 ILE B CG2   1 
ATOM   4635  C  CD1   . ILE A  1  592 ? 7.297   -16.781 43.111 1.00 39.73  ? 1391 ILE B CD1   1 
ATOM   4636  N  N     . ASP A  1  593 ? 6.771   -21.596 44.241 1.00 38.45  ? 1392 ASP B N     1 
ATOM   4637  C  CA    . ASP A  1  593 ? 5.609   -22.167 44.862 1.00 40.36  ? 1392 ASP B CA    1 
ATOM   4638  C  C     . ASP A  1  593 ? 5.693   -22.073 46.368 1.00 38.96  ? 1392 ASP B C     1 
ATOM   4639  O  O     . ASP A  1  593 ? 4.717   -21.814 47.038 1.00 44.44  ? 1392 ASP B O     1 
ATOM   4640  C  CB    . ASP A  1  593 ? 5.486   -23.619 44.471 1.00 41.35  ? 1392 ASP B CB    1 
ATOM   4641  C  CG    . ASP A  1  593 ? 5.027   -23.780 43.079 1.00 47.83  ? 1392 ASP B CG    1 
ATOM   4642  O  OD1   . ASP A  1  593 ? 4.124   -23.006 42.703 1.00 45.64  ? 1392 ASP B OD1   1 
ATOM   4643  O  OD2   . ASP A  1  593 ? 5.571   -24.660 42.355 1.00 55.82  ? 1392 ASP B OD2   1 
ATOM   4644  N  N     . GLU A  1  594 ? 6.883   -22.279 46.893 1.00 39.26  ? 1393 GLU B N     1 
ATOM   4645  C  CA    . GLU A  1  594 ? 7.127   -22.220 48.311 1.00 42.74  ? 1393 GLU B CA    1 
ATOM   4646  C  C     . GLU A  1  594 ? 7.103   -20.784 48.808 1.00 41.45  ? 1393 GLU B C     1 
ATOM   4647  O  O     . GLU A  1  594 ? 6.632   -20.552 49.902 1.00 42.29  ? 1393 GLU B O     1 
ATOM   4648  C  CB    . GLU A  1  594 ? 8.464   -22.868 48.632 1.00 47.56  ? 1393 GLU B CB    1 
ATOM   4649  C  CG    . GLU A  1  594 ? 8.550   -23.383 50.057 1.00 66.53  ? 1393 GLU B CG    1 
ATOM   4650  C  CD    . GLU A  1  594 ? 9.828   -24.121 50.329 1.00 72.01  ? 1393 GLU B CD    1 
ATOM   4651  O  OE1   . GLU A  1  594 ? 10.563  -24.377 49.349 1.00 77.03  ? 1393 GLU B OE1   1 
ATOM   4652  O  OE2   . GLU A  1  594 ? 10.101  -24.404 51.518 1.00 72.86  ? 1393 GLU B OE2   1 
ATOM   4653  N  N     . ILE A  1  595 ? 7.574   -19.835 47.999 1.00 40.06  ? 1394 ILE B N     1 
ATOM   4654  C  CA    . ILE A  1  595 ? 7.487   -18.431 48.329 1.00 36.32  ? 1394 ILE B CA    1 
ATOM   4655  C  C     . ILE A  1  595 ? 6.042   -18.006 48.485 1.00 38.41  ? 1394 ILE B C     1 
ATOM   4656  O  O     . ILE A  1  595 ? 5.715   -17.395 49.457 1.00 37.32  ? 1394 ILE B O     1 
ATOM   4657  C  CB    . ILE A  1  595 ? 8.139   -17.610 47.201 1.00 33.50  ? 1394 ILE B CB    1 
ATOM   4658  C  CG1   . ILE A  1  595 ? 9.640   -17.881 47.194 1.00 33.65  ? 1394 ILE B CG1   1 
ATOM   4659  C  CG2   . ILE A  1  595 ? 7.853   -16.109 47.315 1.00 29.70  ? 1394 ILE B CG2   1 
ATOM   4660  C  CD1   . ILE A  1  595 ? 10.505  -16.902 47.951 1.00 30.64  ? 1394 ILE B CD1   1 
ATOM   4661  N  N     . ILE A  1  596 ? 5.188   -18.347 47.534 1.00 41.09  ? 1395 ILE B N     1 
ATOM   4662  C  CA    . ILE A  1  596 ? 3.803   -17.946 47.574 1.00 43.91  ? 1395 ILE B CA    1 
ATOM   4663  C  C     . ILE A  1  596 ? 3.092   -18.594 48.734 1.00 45.22  ? 1395 ILE B C     1 
ATOM   4664  O  O     . ILE A  1  596 ? 2.243   -17.991 49.351 1.00 48.41  ? 1395 ILE B O     1 
ATOM   4665  C  CB    . ILE A  1  596 ? 3.079   -18.426 46.308 1.00 45.38  ? 1395 ILE B CB    1 
ATOM   4666  C  CG1   . ILE A  1  596 ? 3.780   -17.921 45.077 1.00 43.02  ? 1395 ILE B CG1   1 
ATOM   4667  C  CG2   . ILE A  1  596 ? 1.605   -18.046 46.298 1.00 39.10  ? 1395 ILE B CG2   1 
ATOM   4668  C  CD1   . ILE A  1  596 ? 3.247   -16.641 44.504 1.00 40.98  ? 1395 ILE B CD1   1 
ATOM   4669  N  N     . SER A  1  597 ? 3.400   -19.848 49.011 1.00 46.60  ? 1396 SER B N     1 
ATOM   4670  C  CA    . SER A  1  597 ? 2.699   -20.519 50.080 1.00 43.15  ? 1396 SER B CA    1 
ATOM   4671  C  C     . SER A  1  597 ? 3.159   -19.940 51.411 1.00 43.87  ? 1396 SER B C     1 
ATOM   4672  O  O     . SER A  1  597 ? 2.403   -19.821 52.329 1.00 43.25  ? 1396 SER B O     1 
ATOM   4673  C  CB    . SER A  1  597 ? 2.910   -22.025 49.967 1.00 46.16  ? 1396 SER B CB    1 
ATOM   4674  O  OG    . SER A  1  597 ? 3.912   -22.492 50.836 1.00 56.89  ? 1396 SER B OG    1 
ATOM   4675  N  N     . THR A  1  598 ? 4.419   -19.528 51.488 1.00 44.19  ? 1397 THR B N     1 
ATOM   4676  C  CA    . THR A  1  598 ? 4.927   -18.885 52.672 1.00 43.09  ? 1397 THR B CA    1 
ATOM   4677  C  C     . THR A  1  598 ? 4.106   -17.616 52.926 1.00 44.67  ? 1397 THR B C     1 
ATOM   4678  O  O     . THR A  1  598 ? 3.672   -17.382 54.056 1.00 39.55  ? 1397 THR B O     1 
ATOM   4679  C  CB    . THR A  1  598 ? 6.408   -18.540 52.519 1.00 42.35  ? 1397 THR B CB    1 
ATOM   4680  O  OG1   . THR A  1  598 ? 7.143   -19.756 52.473 1.00 48.92  ? 1397 THR B OG1   1 
ATOM   4681  C  CG2   . THR A  1  598 ? 6.926   -17.667 53.645 1.00 43.92  ? 1397 THR B CG2   1 
ATOM   4682  N  N     . ILE A  1  599 ? 3.907   -16.809 51.878 1.00 41.03  ? 1398 ILE B N     1 
ATOM   4683  C  CA    . ILE A  1  599 ? 3.153   -15.589 52.003 1.00 38.82  ? 1398 ILE B CA    1 
ATOM   4684  C  C     . ILE A  1  599 ? 1.680   -15.864 52.301 1.00 38.62  ? 1398 ILE B C     1 
ATOM   4685  O  O     . ILE A  1  599 ? 1.117   -15.281 53.186 1.00 37.56  ? 1398 ILE B O     1 
ATOM   4686  C  CB    . ILE A  1  599 ? 3.352   -14.706 50.789 1.00 38.82  ? 1398 ILE B CB    1 
ATOM   4687  C  CG1   . ILE A  1  599 ? 4.796   -14.218 50.781 1.00 37.63  ? 1398 ILE B CG1   1 
ATOM   4688  C  CG2   . ILE A  1  599 ? 2.433   -13.492 50.850 1.00 38.13  ? 1398 ILE B CG2   1 
ATOM   4689  C  CD1   . ILE A  1  599 ? 5.382   -14.065 49.424 1.00 33.95  ? 1398 ILE B CD1   1 
ATOM   4690  N  N     . ARG A  1  600 ? 1.075   -16.797 51.600 1.00 43.22  ? 1399 ARG B N     1 
ATOM   4691  C  CA    . ARG A  1  600 ? -0.359  -17.080 51.823 1.00 46.87  ? 1399 ARG B CA    1 
ATOM   4692  C  C     . ARG A  1  600 ? -0.644  -17.485 53.251 1.00 47.73  ? 1399 ARG B C     1 
ATOM   4693  O  O     . ARG A  1  600 ? -1.684  -17.182 53.791 1.00 47.06  ? 1399 ARG B O     1 
ATOM   4694  C  CB    . ARG A  1  600 ? -0.811  -18.194 50.929 1.00 40.94  ? 1399 ARG B CB    1 
ATOM   4695  C  CG    . ARG A  1  600 ? -1.111  -17.744 49.511 1.00 41.55  ? 1399 ARG B CG    1 
ATOM   4696  C  CD    . ARG A  1  600 ? -1.321  -18.963 48.642 1.00 45.52  ? 1399 ARG B CD    1 
ATOM   4697  N  NE    . ARG A  1  600 ? -2.628  -19.573 48.823 1.00 49.08  ? 1399 ARG B NE    1 
ATOM   4698  C  CZ    . ARG A  1  600 ? -3.013  -20.686 48.229 1.00 47.34  ? 1399 ARG B CZ    1 
ATOM   4699  N  NH1   . ARG A  1  600 ? -4.234  -21.124 48.434 1.00 51.88  ? 1399 ARG B NH1   1 
ATOM   4700  N  NH2   . ARG A  1  600 ? -2.209  -21.335 47.395 1.00 45.87  ? 1399 ARG B NH2   1 
ATOM   4701  N  N     . GLU A  1  601 ? 0.320   -18.181 53.842 1.00 53.01  ? 1400 GLU B N     1 
ATOM   4702  C  CA    . GLU A  1  601 ? 0.219   -18.719 55.182 1.00 47.96  ? 1400 GLU B CA    1 
ATOM   4703  C  C     . GLU A  1  601 ? 0.504   -17.670 56.279 1.00 48.05  ? 1400 GLU B C     1 
ATOM   4704  O  O     . GLU A  1  601 ? 0.262   -17.918 57.455 1.00 49.91  ? 1400 GLU B O     1 
ATOM   4705  C  CB    . GLU A  1  601 ? 1.123   -19.963 55.287 1.00 51.94  ? 1400 GLU B CB    1 
ATOM   4706  C  CG    . GLU A  1  601 ? 1.939   -20.115 56.569 1.00 70.45  ? 1400 GLU B CG    1 
ATOM   4707  C  CD    . GLU A  1  601 ? 3.259   -20.839 56.388 1.00 76.34  ? 1400 GLU B CD    1 
ATOM   4708  O  OE1   . GLU A  1  601 ? 4.289   -20.274 56.808 1.00 79.24  ? 1400 GLU B OE1   1 
ATOM   4709  O  OE2   . GLU A  1  601 ? 3.269   -21.953 55.825 1.00 94.60  ? 1400 GLU B OE2   1 
ATOM   4710  N  N     . SER A  1  602 ? 0.961   -16.489 55.892 1.00 44.90  ? 1401 SER B N     1 
ATOM   4711  C  CA    . SER A  1  602 ? 1.291   -15.453 56.849 1.00 45.11  ? 1401 SER B CA    1 
ATOM   4712  C  C     . SER A  1  602 ? 0.140   -14.482 57.030 1.00 41.72  ? 1401 SER B C     1 
ATOM   4713  O  O     . SER A  1  602 ? -0.406  -13.991 56.072 1.00 46.46  ? 1401 SER B O     1 
ATOM   4714  C  CB    . SER A  1  602 ? 2.540   -14.703 56.398 1.00 45.46  ? 1401 SER B CB    1 
ATOM   4715  O  OG    . SER A  1  602 ? 3.642   -15.577 56.264 1.00 47.01  ? 1401 SER B OG    1 
ATOM   4716  N  N     . ASP A  1  603 ? -0.208  -14.219 58.279 1.00 48.35  ? 1402 ASP B N     1 
ATOM   4717  C  CA    . ASP A  1  603 ? -1.318  -13.338 58.633 1.00 52.51  ? 1402 ASP B CA    1 
ATOM   4718  C  C     . ASP A  1  603 ? -1.049  -11.908 58.257 1.00 53.64  ? 1402 ASP B C     1 
ATOM   4719  O  O     . ASP A  1  603 ? -1.929  -11.192 57.803 1.00 57.62  ? 1402 ASP B O     1 
ATOM   4720  C  CB    . ASP A  1  603 ? -1.555  -13.408 60.138 1.00 62.91  ? 1402 ASP B CB    1 
ATOM   4721  C  CG    . ASP A  1  603 ? -2.238  -14.706 60.570 1.00 80.32  ? 1402 ASP B CG    1 
ATOM   4722  O  OD1   . ASP A  1  603 ? -2.893  -15.367 59.730 1.00 89.20  ? 1402 ASP B OD1   1 
ATOM   4723  O  OD2   . ASP A  1  603 ? -2.129  -15.054 61.757 1.00 86.97  ? 1402 ASP B OD2   1 
ATOM   4724  N  N     . THR A  1  604 ? 0.182   -11.477 58.488 1.00 57.81  ? 1403 THR B N     1 
ATOM   4725  C  CA    . THR A  1  604 ? 0.573   -10.085 58.250 1.00 54.03  ? 1403 THR B CA    1 
ATOM   4726  C  C     . THR A  1  604 ? 1.865   -9.981  57.456 1.00 55.45  ? 1403 THR B C     1 
ATOM   4727  O  O     . THR A  1  604 ? 2.621   -10.945 57.284 1.00 54.82  ? 1403 THR B O     1 
ATOM   4728  C  CB    . THR A  1  604 ? 0.770   -9.299  59.554 1.00 49.26  ? 1403 THR B CB    1 
ATOM   4729  O  OG1   . THR A  1  604 ? 1.982   -9.748  60.204 1.00 54.34  ? 1403 THR B OG1   1 
ATOM   4730  C  CG2   . THR A  1  604 ? -0.433  -9.466  60.463 1.00 46.42  ? 1403 THR B CG2   1 
ATOM   4731  N  N     . ASP A  1  605 ? 2.105   -8.763  57.015 1.00 56.79  ? 1404 ASP B N     1 
ATOM   4732  C  CA    . ASP A  1  605 ? 3.250   -8.386  56.237 1.00 61.39  ? 1404 ASP B CA    1 
ATOM   4733  C  C     . ASP A  1  605 ? 4.535   -8.724  56.979 1.00 63.70  ? 1404 ASP B C     1 
ATOM   4734  O  O     . ASP A  1  605 ? 5.475   -9.282  56.395 1.00 65.42  ? 1404 ASP B O     1 
ATOM   4735  C  CB    . ASP A  1  605 ? 3.166   -6.889  56.013 1.00 65.92  ? 1404 ASP B CB    1 
ATOM   4736  C  CG    . ASP A  1  605 ? 3.655   -6.484  54.664 1.00 80.87  ? 1404 ASP B CG    1 
ATOM   4737  O  OD1   . ASP A  1  605 ? 4.899   -6.293  54.510 1.00 88.44  ? 1404 ASP B OD1   1 
ATOM   4738  O  OD2   . ASP A  1  605 ? 2.788   -6.338  53.756 1.00 91.83  ? 1404 ASP B OD2   1 
ATOM   4739  N  N     . LYS A  1  606 ? 4.565   -8.392  58.271 1.00 62.33  ? 1405 LYS B N     1 
ATOM   4740  C  CA    . LYS A  1  606 ? 5.735   -8.612  59.103 1.00 52.16  ? 1405 LYS B CA    1 
ATOM   4741  C  C     . LYS A  1  606 ? 6.078   -10.095 59.217 1.00 52.69  ? 1405 LYS B C     1 
ATOM   4742  O  O     . LYS A  1  606 ? 7.236   -10.488 59.150 1.00 54.65  ? 1405 LYS B O     1 
ATOM   4743  C  CB    . LYS A  1  606 ? 5.518   -8.001  60.478 1.00 46.30  ? 1405 LYS B CB    1 
ATOM   4744  N  N     . VAL A  1  607 ? 5.061   -10.925 59.421 1.00 48.18  ? 1406 VAL B N     1 
ATOM   4745  C  CA    . VAL A  1  607 ? 5.276   -12.352 59.587 1.00 44.95  ? 1406 VAL B CA    1 
ATOM   4746  C  C     . VAL A  1  607 ? 5.845   -12.947 58.306 1.00 52.19  ? 1406 VAL B C     1 
ATOM   4747  O  O     . VAL A  1  607 ? 6.744   -13.799 58.362 1.00 56.93  ? 1406 VAL B O     1 
ATOM   4748  C  CB    . VAL A  1  607 ? 3.958   -13.043 59.967 1.00 45.52  ? 1406 VAL B CB    1 
ATOM   4749  C  CG1   . VAL A  1  607 ? 4.056   -14.548 59.907 1.00 37.65  ? 1406 VAL B CG1   1 
ATOM   4750  C  CG2   . VAL A  1  607 ? 3.519   -12.564 61.349 1.00 46.86  ? 1406 VAL B CG2   1 
ATOM   4751  N  N     . ALA A  1  608 ? 5.322   -12.504 57.162 1.00 47.79  ? 1407 ALA B N     1 
ATOM   4752  C  CA    . ALA A  1  608 ? 5.796   -12.985 55.877 1.00 45.36  ? 1407 ALA B CA    1 
ATOM   4753  C  C     . ALA A  1  608 ? 7.274   -12.632 55.676 1.00 43.65  ? 1407 ALA B C     1 
ATOM   4754  O  O     . ALA A  1  608 ? 8.051   -13.447 55.216 1.00 45.21  ? 1407 ALA B O     1 
ATOM   4755  C  CB    . ALA A  1  608 ? 4.939   -12.416 54.753 1.00 37.23  ? 1407 ALA B CB    1 
ATOM   4756  N  N     . MET A  1  609 ? 7.648   -11.419 56.041 1.00 45.85  ? 1408 MET B N     1 
ATOM   4757  C  CA    . MET A  1  609 ? 9.040   -10.984 55.923 1.00 47.90  ? 1408 MET B CA    1 
ATOM   4758  C  C     . MET A  1  609 ? 9.998   -11.845 56.740 1.00 47.20  ? 1408 MET B C     1 
ATOM   4759  O  O     . MET A  1  609 ? 11.018  -12.271 56.231 1.00 53.04  ? 1408 MET B O     1 
ATOM   4760  C  CB    . MET A  1  609 ? 9.182   -9.548  56.350 1.00 47.50  ? 1408 MET B CB    1 
ATOM   4761  C  CG    . MET A  1  609 ? 8.512   -8.525  55.451 1.00 53.73  ? 1408 MET B CG    1 
ATOM   4762  S  SD    . MET A  1  609 ? 9.645   -7.909  54.213 1.00 72.55  ? 1408 MET B SD    1 
ATOM   4763  C  CE    . MET A  1  609 ? 10.849  -7.181  55.329 1.00 61.96  ? 1408 MET B CE    1 
ATOM   4764  N  N     . GLU A  1  610 ? 9.648   -12.125 57.988 1.00 46.21  ? 1409 GLU B N     1 
ATOM   4765  C  CA    . GLU A  1  610 ? 10.473  -12.944 58.848 1.00 44.32  ? 1409 GLU B CA    1 
ATOM   4766  C  C     . GLU A  1  610 ? 10.558  -14.367 58.296 1.00 50.17  ? 1409 GLU B C     1 
ATOM   4767  O  O     . GLU A  1  610 ? 11.632  -14.958 58.281 1.00 51.81  ? 1409 GLU B O     1 
ATOM   4768  C  CB    . GLU A  1  610 ? 9.935   -12.956 60.284 1.00 41.71  ? 1409 GLU B CB    1 
ATOM   4769  N  N     . SER A  1  611 ? 9.426   -14.910 57.843 1.00 42.89  ? 1410 SER B N     1 
ATOM   4770  C  CA    . SER A  1  611 ? 9.421   -16.265 57.309 1.00 45.45  ? 1410 SER B CA    1 
ATOM   4771  C  C     . SER A  1  611 ? 10.251  -16.421 56.026 1.00 44.89  ? 1410 SER B C     1 
ATOM   4772  O  O     . SER A  1  611 ? 11.012  -17.374 55.886 1.00 46.26  ? 1410 SER B O     1 
ATOM   4773  C  CB    . SER A  1  611 ? 8.012   -16.755 57.057 1.00 42.94  ? 1410 SER B CB    1 
ATOM   4774  O  OG    . SER A  1  611 ? 7.337   -16.909 58.272 1.00 46.64  ? 1410 SER B OG    1 
ATOM   4775  N  N     . LEU A  1  612 ? 10.117  -15.470 55.118 1.00 39.93  ? 1411 LEU B N     1 
ATOM   4776  C  CA    . LEU A  1  612 ? 10.888  -15.500 53.898 1.00 41.48  ? 1411 LEU B CA    1 
ATOM   4777  C  C     . LEU A  1  612 ? 12.377  -15.432 54.213 1.00 45.56  ? 1411 LEU B C     1 
ATOM   4778  O  O     . LEU A  1  612 ? 13.149  -16.230 53.687 1.00 52.64  ? 1411 LEU B O     1 
ATOM   4779  C  CB    . LEU A  1  612 ? 10.473  -14.338 52.991 1.00 41.35  ? 1411 LEU B CB    1 
ATOM   4780  C  CG    . LEU A  1  612 ? 9.128   -14.481 52.247 1.00 43.69  ? 1411 LEU B CG    1 
ATOM   4781  C  CD1   . LEU A  1  612 ? 8.711   -13.128 51.683 1.00 42.82  ? 1411 LEU B CD1   1 
ATOM   4782  C  CD2   . LEU A  1  612 ? 9.223   -15.552 51.158 1.00 41.99  ? 1411 LEU B CD2   1 
ATOM   4783  N  N     . GLN A  1  613 ? 12.770  -14.503 55.090 1.00 45.68  ? 1412 GLN B N     1 
ATOM   4784  C  CA    . GLN A  1  613 ? 14.169  -14.318 55.458 1.00 48.10  ? 1412 GLN B CA    1 
ATOM   4785  C  C     . GLN A  1  613 ? 14.839  -15.544 56.115 1.00 50.72  ? 1412 GLN B C     1 
ATOM   4786  O  O     . GLN A  1  613 ? 15.961  -15.886 55.753 1.00 46.45  ? 1412 GLN B O     1 
ATOM   4787  C  CB    . GLN A  1  613 ? 14.304  -13.136 56.395 1.00 48.35  ? 1412 GLN B CB    1 
ATOM   4788  C  CG    . GLN A  1  613 ? 13.991  -11.783 55.805 1.00 45.10  ? 1412 GLN B CG    1 
ATOM   4789  C  CD    . GLN A  1  613 ? 14.230  -10.671 56.809 1.00 53.74  ? 1412 GLN B CD    1 
ATOM   4790  O  OE1   . GLN A  1  613 ? 15.385  -10.389 57.191 1.00 52.80  ? 1412 GLN B OE1   1 
ATOM   4791  N  NE2   . GLN A  1  613 ? 13.149  -10.034 57.251 1.00 52.43  ? 1412 GLN B NE2   1 
ATOM   4792  N  N     . GLN A  1  614 ? 14.148  -16.189 57.060 1.00 45.82  ? 1413 GLN B N     1 
ATOM   4793  C  CA    . GLN A  1  614 ? 14.683  -17.336 57.727 1.00 48.48  ? 1413 GLN B CA    1 
ATOM   4794  C  C     . GLN A  1  614 ? 14.793  -18.538 56.811 1.00 58.17  ? 1413 GLN B C     1 
ATOM   4795  O  O     . GLN A  1  614 ? 15.842  -19.243 56.778 1.00 58.37  ? 1413 GLN B O     1 
ATOM   4796  C  CB    . GLN A  1  614 ? 13.844  -17.710 58.942 1.00 57.18  ? 1413 GLN B CB    1 
ATOM   4797  C  CG    . GLN A  1  614 ? 14.318  -17.069 60.237 1.00 70.74  ? 1413 GLN B CG    1 
ATOM   4798  C  CD    . GLN A  1  614 ? 13.989  -17.917 61.461 1.00 86.88  ? 1413 GLN B CD    1 
ATOM   4799  O  OE1   . GLN A  1  614 ? 14.879  -18.541 62.045 1.00 96.58  ? 1413 GLN B OE1   1 
ATOM   4800  N  NE2   . GLN A  1  614 ? 12.708  -17.966 61.838 1.00 84.10  ? 1413 GLN B NE2   1 
ATOM   4801  N  N     . ARG A  1  615 ? 13.709  -18.772 56.076 1.00 52.12  ? 1414 ARG B N     1 
ATOM   4802  C  CA    . ARG A  1  615 ? 13.563  -19.924 55.194 1.00 46.35  ? 1414 ARG B CA    1 
ATOM   4803  C  C     . ARG A  1  615 ? 14.491  -19.870 53.980 1.00 52.86  ? 1414 ARG B C     1 
ATOM   4804  O  O     . ARG A  1  615 ? 15.080  -20.901 53.593 1.00 56.74  ? 1414 ARG B O     1 
ATOM   4805  C  CB    . ARG A  1  615 ? 12.116  -20.012 54.769 1.00 46.48  ? 1414 ARG B CB    1 
ATOM   4806  C  CG    . ARG A  1  615 ? 11.695  -21.273 54.079 1.00 52.03  ? 1414 ARG B CG    1 
ATOM   4807  C  CD    . ARG A  1  615 ? 10.158  -21.318 54.082 1.00 55.04  ? 1414 ARG B CD    1 
ATOM   4808  N  NE    . ARG A  1  615 ? 9.575   -21.704 55.369 1.00 59.40  ? 1414 ARG B NE    1 
ATOM   4809  C  CZ    . ARG A  1  615 ? 8.336   -21.421 55.758 1.00 61.92  ? 1414 ARG B CZ    1 
ATOM   4810  N  NH1   . ARG A  1  615 ? 7.497   -20.766 54.980 1.00 63.52  ? 1414 ARG B NH1   1 
ATOM   4811  N  NH2   . ARG A  1  615 ? 7.901   -21.819 56.930 1.00 64.22  ? 1414 ARG B NH2   1 
ATOM   4812  N  N     . PHE A  1  616 ? 14.630  -18.679 53.379 1.00 48.13  ? 1415 PHE B N     1 
ATOM   4813  C  CA    . PHE A  1  616 ? 15.435  -18.539 52.165 1.00 42.98  ? 1415 PHE B CA    1 
ATOM   4814  C  C     . PHE A  1  616 ? 16.721  -17.725 52.298 1.00 42.20  ? 1415 PHE B C     1 
ATOM   4815  O  O     . PHE A  1  616 ? 17.315  -17.355 51.280 1.00 39.86  ? 1415 PHE B O     1 
ATOM   4816  C  CB    . PHE A  1  616 ? 14.577  -18.034 51.014 1.00 42.00  ? 1415 PHE B CB    1 
ATOM   4817  C  CG    . PHE A  1  616 ? 13.310  -18.801 50.838 1.00 46.52  ? 1415 PHE B CG    1 
ATOM   4818  C  CD1   . PHE A  1  616 ? 13.311  -20.011 50.164 1.00 49.61  ? 1415 PHE B CD1   1 
ATOM   4819  C  CD2   . PHE A  1  616 ? 12.110  -18.321 51.368 1.00 46.86  ? 1415 PHE B CD2   1 
ATOM   4820  C  CE1   . PHE A  1  616 ? 12.127  -20.731 50.006 1.00 51.92  ? 1415 PHE B CE1   1 
ATOM   4821  C  CE2   . PHE A  1  616 ? 10.921  -19.021 51.202 1.00 50.99  ? 1415 PHE B CE2   1 
ATOM   4822  C  CZ    . PHE A  1  616 ? 10.925  -20.248 50.517 1.00 50.84  ? 1415 PHE B CZ    1 
ATOM   4823  N  N     . LYS A  1  617 ? 17.159  -17.446 53.522 1.00 37.79  ? 1416 LYS B N     1 
ATOM   4824  C  CA    . LYS A  1  617 ? 18.422  -16.727 53.718 1.00 39.63  ? 1416 LYS B CA    1 
ATOM   4825  C  C     . LYS A  1  617 ? 18.333  -15.384 52.966 1.00 40.36  ? 1416 LYS B C     1 
ATOM   4826  O  O     . LYS A  1  617 ? 19.204  -15.030 52.140 1.00 42.14  ? 1416 LYS B O     1 
ATOM   4827  C  CB    . LYS A  1  617 ? 19.627  -17.512 53.154 1.00 38.25  ? 1416 LYS B CB    1 
ATOM   4828  C  CG    . LYS A  1  617 ? 20.122  -18.674 53.935 1.00 37.26  ? 1416 LYS B CG    1 
ATOM   4829  C  CD    . LYS A  1  617 ? 21.160  -19.434 53.121 1.00 37.79  ? 1416 LYS B CD    1 
ATOM   4830  C  CE    . LYS A  1  617 ? 22.557  -18.812 53.074 1.00 35.67  ? 1416 LYS B CE    1 
ATOM   4831  N  NZ    . LYS A  1  617 ? 22.992  -18.722 54.473 1.00 37.55  ? 1416 LYS B NZ    1 
ATOM   4832  N  N     . LEU A  1  618 ? 17.253  -14.664 53.182 1.00 42.21  ? 1417 LEU B N     1 
ATOM   4833  C  CA    . LEU A  1  618 ? 17.051  -13.392 52.475 1.00 39.84  ? 1417 LEU B CA    1 
ATOM   4834  C  C     . LEU A  1  618 ? 17.222  -12.214 53.405 1.00 37.09  ? 1417 LEU B C     1 
ATOM   4835  O  O     . LEU A  1  618 ? 16.829  -12.279 54.576 1.00 41.30  ? 1417 LEU B O     1 
ATOM   4836  C  CB    . LEU A  1  618 ? 15.657  -13.383 51.847 1.00 36.87  ? 1417 LEU B CB    1 
ATOM   4837  C  CG    . LEU A  1  618 ? 15.368  -14.402 50.745 1.00 34.74  ? 1417 LEU B CG    1 
ATOM   4838  C  CD1   . LEU A  1  618 ? 13.888  -14.497 50.484 1.00 34.46  ? 1417 LEU B CD1   1 
ATOM   4839  C  CD2   . LEU A  1  618 ? 16.110  -14.091 49.451 1.00 30.89  ? 1417 LEU B CD2   1 
ATOM   4840  N  N     . SER A  1  619 ? 17.823  -11.140 52.899 1.00 39.16  ? 1418 SER B N     1 
ATOM   4841  C  CA    . SER A  1  619 ? 17.899  -9.901  53.694 1.00 40.21  ? 1418 SER B CA    1 
ATOM   4842  C  C     . SER A  1  619 ? 16.529  -9.229  53.759 1.00 41.62  ? 1418 SER B C     1 
ATOM   4843  O  O     . SER A  1  619 ? 15.607  -9.595  53.045 1.00 42.65  ? 1418 SER B O     1 
ATOM   4844  C  CB    . SER A  1  619 ? 18.934  -8.934  53.141 1.00 37.55  ? 1418 SER B CB    1 
ATOM   4845  O  OG    . SER A  1  619 ? 18.495  -8.319  51.959 1.00 43.64  ? 1418 SER B OG    1 
ATOM   4846  N  N     . GLU A  1  620 ? 16.419  -8.254  54.628 1.00 48.05  ? 1419 GLU B N     1 
ATOM   4847  C  CA    . GLU A  1  620 ? 15.211  -7.514  54.823 1.00 49.61  ? 1419 GLU B CA    1 
ATOM   4848  C  C     . GLU A  1  620 ? 14.842  -6.804  53.530 1.00 45.55  ? 1419 GLU B C     1 
ATOM   4849  O  O     . GLU A  1  620 ? 13.693  -6.797  53.153 1.00 43.37  ? 1419 GLU B O     1 
ATOM   4850  C  CB    . GLU A  1  620 ? 15.395  -6.538  55.973 1.00 52.68  ? 1419 GLU B CB    1 
ATOM   4851  C  CG    . GLU A  1  620 ? 14.127  -5.797  56.342 1.00 59.69  ? 1419 GLU B CG    1 
ATOM   4852  C  CD    . GLU A  1  620 ? 14.211  -5.034  57.646 1.00 62.38  ? 1419 GLU B CD    1 
ATOM   4853  O  OE1   . GLU A  1  620 ? 13.668  -3.935  57.686 1.00 67.17  ? 1419 GLU B OE1   1 
ATOM   4854  O  OE2   . GLU A  1  620 ? 14.810  -5.504  58.627 1.00 68.70  ? 1419 GLU B OE2   1 
ATOM   4855  N  N     . LYS A  1  621 ? 15.822  -6.259  52.835 1.00 40.19  ? 1420 LYS B N     1 
ATOM   4856  C  CA    . LYS A  1  621 ? 15.557  -5.629  51.566 1.00 40.94  ? 1420 LYS B CA    1 
ATOM   4857  C  C     . LYS A  1  621 ? 15.129  -6.579  50.439 1.00 43.86  ? 1420 LYS B C     1 
ATOM   4858  O  O     . LYS A  1  621 ? 14.325  -6.200  49.591 1.00 45.16  ? 1420 LYS B O     1 
ATOM   4859  C  CB    . LYS A  1  621 ? 16.755  -4.775  51.157 1.00 45.94  ? 1420 LYS B CB    1 
ATOM   4860  C  CG    . LYS A  1  621 ? 16.647  -3.324  51.629 1.00 48.89  ? 1420 LYS B CG    1 
ATOM   4861  C  CD    . LYS A  1  621 ? 17.840  -2.492  51.221 1.00 53.86  ? 1420 LYS B CD    1 
ATOM   4862  C  CE    . LYS A  1  621 ? 18.960  -2.604  52.257 1.00 63.01  ? 1420 LYS B CE    1 
ATOM   4863  N  NZ    . LYS A  1  621 ? 19.988  -1.553  51.992 1.00 65.10  ? 1420 LYS B NZ    1 
ATOM   4864  N  N     . GLN A  1  622 ? 15.631  -7.815  50.450 1.00 41.56  ? 1421 GLN B N     1 
ATOM   4865  C  CA    . GLN A  1  622 ? 15.251  -8.799  49.428 1.00 35.15  ? 1421 GLN B CA    1 
ATOM   4866  C  C     . GLN A  1  622 ? 13.839  -9.247  49.613 1.00 31.21  ? 1421 GLN B C     1 
ATOM   4867  O  O     . GLN A  1  622 ? 13.102  -9.412  48.664 1.00 32.26  ? 1421 GLN B O     1 
ATOM   4868  C  CB    . GLN A  1  622 ? 16.219  -9.990  49.411 1.00 32.08  ? 1421 GLN B CB    1 
ATOM   4869  C  CG    . GLN A  1  622 ? 17.605  -9.596  48.886 1.00 34.19  ? 1421 GLN B CG    1 
ATOM   4870  C  CD    . GLN A  1  622 ? 18.640  -10.662 49.113 1.00 31.12  ? 1421 GLN B CD    1 
ATOM   4871  O  OE1   . GLN A  1  622 ? 18.601  -11.328 50.112 1.00 34.77  ? 1421 GLN B OE1   1 
ATOM   4872  N  NE2   . GLN A  1  622 ? 19.547  -10.821 48.182 1.00 30.03  ? 1421 GLN B NE2   1 
ATOM   4873  N  N     . ALA A  1  623 ? 13.476  -9.461  50.860 1.00 34.01  ? 1422 ALA B N     1 
ATOM   4874  C  CA    . ALA A  1  623 ? 12.163  -9.962  51.199 1.00 36.93  ? 1422 ALA B CA    1 
ATOM   4875  C  C     . ALA A  1  623 ? 11.087  -8.907  50.864 1.00 36.91  ? 1422 ALA B C     1 
ATOM   4876  O  O     . ALA A  1  623 ? 10.021  -9.266  50.461 1.00 36.90  ? 1422 ALA B O     1 
ATOM   4877  C  CB    . ALA A  1  623 ? 12.140  -10.345 52.676 1.00 31.02  ? 1422 ALA B CB    1 
ATOM   4878  N  N     . GLN A  1  624 ? 11.393  -7.625  51.064 1.00 37.99  ? 1423 GLN B N     1 
ATOM   4879  C  CA    . GLN A  1  624 ? 10.483  -6.546  50.775 1.00 37.72  ? 1423 GLN B CA    1 
ATOM   4880  C  C     . GLN A  1  624 ? 10.274  -6.470  49.295 1.00 38.68  ? 1423 GLN B C     1 
ATOM   4881  O  O     . GLN A  1  624 ? 9.151   -6.287  48.830 1.00 35.66  ? 1423 GLN B O     1 
ATOM   4882  C  CB    . GLN A  1  624 ? 11.079  -5.198  51.252 1.00 45.88  ? 1423 GLN B CB    1 
ATOM   4883  C  CG    . GLN A  1  624 ? 10.498  -4.695  52.556 1.00 57.05  ? 1423 GLN B CG    1 
ATOM   4884  C  CD    . GLN A  1  624 ? 8.994   -4.487  52.441 1.00 70.28  ? 1423 GLN B CD    1 
ATOM   4885  O  OE1   . GLN A  1  624 ? 8.484   -4.265  51.329 1.00 74.48  ? 1423 GLN B OE1   1 
ATOM   4886  N  NE2   . GLN A  1  624 ? 8.266   -4.577  53.569 1.00 77.13  ? 1423 GLN B NE2   1 
ATOM   4887  N  N     . ALA A  1  625 ? 11.370  -6.640  48.555 1.00 34.20  ? 1424 ALA B N     1 
ATOM   4888  C  CA    . ALA A  1  625 ? 11.299  -6.627  47.107 1.00 33.37  ? 1424 ALA B CA    1 
ATOM   4889  C  C     . ALA A  1  625 ? 10.468  -7.795  46.575 1.00 35.66  ? 1424 ALA B C     1 
ATOM   4890  O  O     . ALA A  1  625 ? 9.805   -7.669  45.583 1.00 38.08  ? 1424 ALA B O     1 
ATOM   4891  C  CB    . ALA A  1  625 ? 12.693  -6.663  46.537 1.00 27.01  ? 1424 ALA B CB    1 
ATOM   4892  N  N     . ILE A  1  626 ? 10.566  -8.951  47.200 1.00 35.34  ? 1425 ILE B N     1 
ATOM   4893  C  CA    . ILE A  1  626 ? 9.770   -10.064 46.809 1.00 35.18  ? 1425 ILE B CA    1 
ATOM   4894  C  C     . ILE A  1  626 ? 8.312   -9.814  47.097 1.00 35.30  ? 1425 ILE B C     1 
ATOM   4895  O  O     . ILE A  1  626 ? 7.478   -10.071 46.251 1.00 36.16  ? 1425 ILE B O     1 
ATOM   4896  C  CB    . ILE A  1  626 ? 10.270  -11.320 47.525 1.00 33.97  ? 1425 ILE B CB    1 
ATOM   4897  C  CG1   . ILE A  1  626 ? 11.625  -11.717 46.927 1.00 33.58  ? 1425 ILE B CG1   1 
ATOM   4898  C  CG2   . ILE A  1  626 ? 9.239   -12.447 47.445 1.00 33.92  ? 1425 ILE B CG2   1 
ATOM   4899  C  CD1   . ILE A  1  626 ? 12.384  -12.656 47.798 1.00 37.29  ? 1425 ILE B CD1   1 
ATOM   4900  N  N     . LEU A  1  627 ? 8.004   -9.302  48.279 1.00 35.85  ? 1426 LEU B N     1 
ATOM   4901  C  CA    . LEU A  1  627 ? 6.621   -8.965  48.600 1.00 38.98  ? 1426 LEU B CA    1 
ATOM   4902  C  C     . LEU A  1  627 ? 6.053   -7.851  47.729 1.00 37.33  ? 1426 LEU B C     1 
ATOM   4903  O  O     . LEU A  1  627 ? 4.840   -7.753  47.556 1.00 39.34  ? 1426 LEU B O     1 
ATOM   4904  C  CB    . LEU A  1  627 ? 6.469   -8.623  50.078 1.00 40.38  ? 1426 LEU B CB    1 
ATOM   4905  C  CG    . LEU A  1  627 ? 6.548   -9.756  51.093 1.00 42.38  ? 1426 LEU B CG    1 
ATOM   4906  C  CD1   . LEU A  1  627 ? 6.635   -9.141  52.488 1.00 44.71  ? 1426 LEU B CD1   1 
ATOM   4907  C  CD2   . LEU A  1  627 ? 5.320   -10.649 50.968 1.00 44.79  ? 1426 LEU B CD2   1 
ATOM   4908  N  N     . ASP A  1  628 ? 6.919   -7.029  47.176 1.00 37.11  ? 1427 ASP B N     1 
ATOM   4909  C  CA    . ASP A  1  628 ? 6.470   -5.948  46.282 1.00 40.21  ? 1427 ASP B CA    1 
ATOM   4910  C  C     . ASP A  1  628 ? 6.341   -6.374  44.829 1.00 40.46  ? 1427 ASP B C     1 
ATOM   4911  O  O     . ASP A  1  628 ? 5.810   -5.620  44.034 1.00 40.72  ? 1427 ASP B O     1 
ATOM   4912  C  CB    . ASP A  1  628 ? 7.434   -4.775  46.356 1.00 45.06  ? 1427 ASP B CB    1 
ATOM   4913  C  CG    . ASP A  1  628 ? 7.261   -3.953  47.597 1.00 51.08  ? 1427 ASP B CG    1 
ATOM   4914  O  OD1   . ASP A  1  628 ? 6.257   -4.148  48.320 1.00 47.09  ? 1427 ASP B OD1   1 
ATOM   4915  O  OD2   . ASP A  1  628 ? 8.148   -3.099  47.832 1.00 59.38  ? 1427 ASP B OD2   1 
ATOM   4916  N  N     . MET A  1  629 ? 6.792   -7.582  44.508 1.00 34.27  ? 1428 MET B N     1 
ATOM   4917  C  CA    . MET A  1  629 ? 6.749   -8.086  43.175 1.00 37.10  ? 1428 MET B CA    1 
ATOM   4918  C  C     . MET A  1  629 ? 5.329   -8.237  42.662 1.00 38.49  ? 1428 MET B C     1 
ATOM   4919  O  O     . MET A  1  629 ? 4.455   -8.776  43.370 1.00 38.40  ? 1428 MET B O     1 
ATOM   4920  C  CB    . MET A  1  629 ? 7.364   -9.462  43.204 1.00 37.58  ? 1428 MET B CB    1 
ATOM   4921  C  CG    . MET A  1  629 ? 8.017   -9.863  41.926 1.00 42.24  ? 1428 MET B CG    1 
ATOM   4922  S  SD    . MET A  1  629 ? 8.708   -11.557 41.760 1.00 51.13  ? 1428 MET B SD    1 
ATOM   4923  C  CE    . MET A  1  629 ? 9.207   -11.878 43.442 1.00 42.43  ? 1428 MET B CE    1 
ATOM   4924  N  N     . ARG A  1  630 ? 5.093   -7.790  41.424 1.00 37.64  ? 1429 ARG B N     1 
ATOM   4925  C  CA    . ARG A  1  630 ? 3.752   -7.970  40.858 1.00 36.59  ? 1429 ARG B CA    1 
ATOM   4926  C  C     . ARG A  1  630 ? 3.666   -9.341  40.215 1.00 34.93  ? 1429 ARG B C     1 
ATOM   4927  O  O     . ARG A  1  630 ? 4.675   -9.857  39.804 1.00 33.73  ? 1429 ARG B O     1 
ATOM   4928  C  CB    . ARG A  1  630 ? 3.454   -6.910  39.834 1.00 36.98  ? 1429 ARG B CB    1 
ATOM   4929  C  CG    . ARG A  1  630 ? 3.372   -5.520  40.406 1.00 41.96  ? 1429 ARG B CG    1 
ATOM   4930  C  CD    . ARG A  1  630 ? 3.215   -4.508  39.300 1.00 49.52  ? 1429 ARG B CD    1 
ATOM   4931  N  NE    . ARG A  1  630 ? 3.283   -3.144  39.807 1.00 52.39  ? 1429 ARG B NE    1 
ATOM   4932  C  CZ    . ARG A  1  630 ? 2.293   -2.481  40.403 1.00 55.52  ? 1429 ARG B CZ    1 
ATOM   4933  N  NH1   . ARG A  1  630 ? 1.113   -3.026  40.631 1.00 59.81  ? 1429 ARG B NH1   1 
ATOM   4934  N  NH2   . ARG A  1  630 ? 2.494   -1.241  40.786 1.00 62.46  ? 1429 ARG B NH2   1 
ATOM   4935  N  N     . LEU A  1  631 ? 2.473   -9.916  40.134 1.00 32.89  ? 1430 LEU B N     1 
ATOM   4936  C  CA    . LEU A  1  631 ? 2.252   -11.190 39.480 1.00 35.48  ? 1430 LEU B CA    1 
ATOM   4937  C  C     . LEU A  1  631 ? 2.740   -11.247 38.042 1.00 36.73  ? 1430 LEU B C     1 
ATOM   4938  O  O     . LEU A  1  631 ? 3.124   -12.300 37.574 1.00 38.11  ? 1430 LEU B O     1 
ATOM   4939  C  CB    . LEU A  1  631 ? 0.755   -11.562 39.512 1.00 33.16  ? 1430 LEU B CB    1 
ATOM   4940  C  CG    . LEU A  1  631 ? 0.210   -12.062 40.857 1.00 37.67  ? 1430 LEU B CG    1 
ATOM   4941  C  CD1   . LEU A  1  631 ? -1.249  -12.538 40.758 1.00 34.26  ? 1430 LEU B CD1   1 
ATOM   4942  C  CD2   . LEU A  1  631 ? 1.095   -13.177 41.426 1.00 38.55  ? 1430 LEU B CD2   1 
ATOM   4943  N  N     . ARG A  1  632 ? 2.709   -10.144 37.330 1.00 37.66  ? 1431 ARG B N     1 
ATOM   4944  C  CA    . ARG A  1  632 ? 3.062   -10.181 35.928 1.00 39.64  ? 1431 ARG B CA    1 
ATOM   4945  C  C     . ARG A  1  632 ? 4.546   -10.423 35.787 1.00 43.13  ? 1431 ARG B C     1 
ATOM   4946  O  O     . ARG A  1  632 ? 5.024   -10.589 34.717 1.00 50.95  ? 1431 ARG B O     1 
ATOM   4947  C  CB    . ARG A  1  632 ? 2.727   -8.878  35.263 1.00 38.66  ? 1431 ARG B CB    1 
ATOM   4948  C  CG    . ARG A  1  632 ? 3.522   -7.685  35.747 1.00 42.35  ? 1431 ARG B CG    1 
ATOM   4949  C  CD    . ARG A  1  632 ? 3.293   -6.454  34.858 1.00 43.98  ? 1431 ARG B CD    1 
ATOM   4950  N  NE    . ARG A  1  632 ? 1.934   -5.959  34.959 1.00 49.35  ? 1431 ARG B NE    1 
ATOM   4951  C  CZ    . ARG A  1  632 ? 1.039   -5.993  33.969 1.00 54.19  ? 1431 ARG B CZ    1 
ATOM   4952  N  NH1   . ARG A  1  632 ? 1.350   -6.452  32.751 1.00 60.79  ? 1431 ARG B NH1   1 
ATOM   4953  N  NH2   . ARG A  1  632 ? -0.182  -5.534  34.182 1.00 49.97  ? 1431 ARG B NH2   1 
ATOM   4954  N  N     . ARG A  1  633 ? 5.266   -10.464 36.876 1.00 40.86  ? 1432 ARG B N     1 
ATOM   4955  C  CA    . ARG A  1  633 ? 6.644   -10.768 36.758 1.00 44.88  ? 1432 ARG B CA    1 
ATOM   4956  C  C     . ARG A  1  633 ? 6.971   -12.245 36.767 1.00 46.42  ? 1432 ARG B C     1 
ATOM   4957  O  O     . ARG A  1  633 ? 8.133   -12.620 36.678 1.00 43.46  ? 1432 ARG B O     1 
ATOM   4958  C  CB    . ARG A  1  633 ? 7.407   -10.077 37.842 1.00 46.85  ? 1432 ARG B CB    1 
ATOM   4959  C  CG    . ARG A  1  633 ? 7.764   -8.710  37.378 1.00 53.56  ? 1432 ARG B CG    1 
ATOM   4960  C  CD    . ARG A  1  633 ? 8.488   -8.021  38.431 1.00 64.79  ? 1432 ARG B CD    1 
ATOM   4961  N  NE    . ARG A  1  633 ? 9.836   -7.742  37.998 1.00 75.52  ? 1432 ARG B NE    1 
ATOM   4962  C  CZ    . ARG A  1  633 ? 10.775  -7.305  38.824 1.00 79.62  ? 1432 ARG B CZ    1 
ATOM   4963  N  NH1   . ARG A  1  633 ? 10.504  -7.164  40.137 1.00 66.46  ? 1432 ARG B NH1   1 
ATOM   4964  N  NH2   . ARG A  1  633 ? 11.973  -7.018  38.331 1.00 75.31  ? 1432 ARG B NH2   1 
ATOM   4965  N  N     . LEU A  1  634 ? 5.938   -13.059 36.870 1.00 38.94  ? 1433 LEU B N     1 
ATOM   4966  C  CA    . LEU A  1  634 ? 6.081   -14.492 36.858 1.00 41.05  ? 1433 LEU B CA    1 
ATOM   4967  C  C     . LEU A  1  634 ? 5.993   -15.019 35.427 1.00 41.70  ? 1433 LEU B C     1 
ATOM   4968  O  O     . LEU A  1  634 ? 6.045   -16.226 35.212 1.00 47.32  ? 1433 LEU B O     1 
ATOM   4969  C  CB    . LEU A  1  634 ? 4.983   -15.108 37.711 1.00 42.49  ? 1433 LEU B CB    1 
ATOM   4970  C  CG    . LEU A  1  634 ? 5.321   -15.246 39.187 1.00 45.04  ? 1433 LEU B CG    1 
ATOM   4971  C  CD1   . LEU A  1  634 ? 6.026   -14.033 39.711 1.00 51.54  ? 1433 LEU B CD1   1 
ATOM   4972  C  CD2   . LEU A  1  634 ? 4.059   -15.469 39.999 1.00 46.49  ? 1433 LEU B CD2   1 
ATOM   4973  N  N     . THR A  1  635 ? 5.845   -14.123 34.456 1.00 42.56  ? 1434 THR B N     1 
ATOM   4974  C  CA    . THR A  1  635 ? 5.752   -14.549 33.071 1.00 47.01  ? 1434 THR B CA    1 
ATOM   4975  C  C     . THR A  1  635 ? 7.101   -15.055 32.562 1.00 55.41  ? 1434 THR B C     1 
ATOM   4976  O  O     . THR A  1  635 ? 8.136   -14.904 33.225 1.00 51.69  ? 1434 THR B O     1 
ATOM   4977  C  CB    . THR A  1  635 ? 5.211   -13.452 32.151 1.00 46.36  ? 1434 THR B CB    1 
ATOM   4978  O  OG1   . THR A  1  635 ? 6.084   -12.314 32.172 1.00 49.66  ? 1434 THR B OG1   1 
ATOM   4979  C  CG2   . THR A  1  635 ? 3.807   -13.061 32.553 1.00 47.59  ? 1434 THR B CG2   1 
ATOM   4980  N  N     A GLY A  1  636 ? 7.050   -15.787 31.448 0.50 57.68  ? 1435 GLY B N     1 
ATOM   4981  N  N     B GLY A  1  636 ? 7.109   -15.510 31.305 0.50 53.89  ? 1435 GLY B N     1 
ATOM   4982  C  CA    A GLY A  1  636 ? 8.182   -16.553 30.903 0.50 57.29  ? 1435 GLY B CA    1 
ATOM   4983  C  CA    B GLY A  1  636 ? 8.346   -15.837 30.594 0.50 50.52  ? 1435 GLY B CA    1 
ATOM   4984  C  C     A GLY A  1  636 ? 9.544   -15.905 30.675 0.50 62.79  ? 1435 GLY B C     1 
ATOM   4985  C  C     B GLY A  1  636 ? 9.275   -14.659 30.270 0.50 46.95  ? 1435 GLY B C     1 
ATOM   4986  O  O     A GLY A  1  636 ? 10.579  -16.484 31.030 0.50 57.80  ? 1435 GLY B O     1 
ATOM   4987  O  O     B GLY A  1  636 ? 10.498  -14.750 30.506 0.50 44.94  ? 1435 GLY B O     1 
ATOM   4988  N  N     A LEU A  1  637 ? 9.545   -14.711 30.074 0.50 69.15  ? 1436 LEU B N     1 
ATOM   4989  N  N     B LEU A  1  637 ? 8.730   -13.577 29.705 0.50 41.58  ? 1436 LEU B N     1 
ATOM   4990  C  CA    A LEU A  1  637 ? 10.784  -14.020 29.716 0.50 74.92  ? 1436 LEU B CA    1 
ATOM   4991  C  CA    B LEU A  1  637 ? 9.591   -12.455 29.245 0.50 46.32  ? 1436 LEU B CA    1 
ATOM   4992  C  C     A LEU A  1  637 ? 11.531  -13.414 30.917 0.50 73.33  ? 1436 LEU B C     1 
ATOM   4993  C  C     B LEU A  1  637 ? 10.150  -11.614 30.405 0.50 43.02  ? 1436 LEU B C     1 
ATOM   4994  O  O     A LEU A  1  637 ? 12.428  -12.587 30.739 0.50 80.30  ? 1436 LEU B O     1 
ATOM   4995  O  O     B LEU A  1  637 ? 11.303  -11.171 30.378 0.50 46.86  ? 1436 LEU B O     1 
ATOM   4996  C  CB    A LEU A  1  637 ? 10.528  -12.950 28.619 0.50 77.06  ? 1436 LEU B CB    1 
ATOM   4997  C  CB    B LEU A  1  637 ? 8.928   -11.560 28.160 0.50 46.44  ? 1436 LEU B CB    1 
ATOM   4998  C  CG    A LEU A  1  637 ? 9.558   -11.757 28.777 0.50 74.28  ? 1436 LEU B CG    1 
ATOM   4999  C  CG    B LEU A  1  637 ? 8.910   -11.967 26.660 0.50 46.98  ? 1436 LEU B CG    1 
ATOM   5000  C  CD1   A LEU A  1  637 ? 9.696   -11.097 30.142 0.50 70.97  ? 1436 LEU B CD1   1 
ATOM   5001  C  CD1   B LEU A  1  637 ? 9.067   -10.749 25.764 0.50 42.72  ? 1436 LEU B CD1   1 
ATOM   5002  C  CD2   A LEU A  1  637 ? 9.731   -10.726 27.657 0.50 68.28  ? 1436 LEU B CD2   1 
ATOM   5003  C  CD2   B LEU A  1  637 ? 9.930   -13.044 26.268 0.50 45.70  ? 1436 LEU B CD2   1 
ATOM   5004  N  N     A GLU A  1  638 ? 11.184  -13.836 32.131 0.50 70.39  ? 1437 GLU B N     1 
ATOM   5005  N  N     B GLU A  1  638 ? 9.336   -11.410 31.427 0.50 42.17  ? 1437 GLU B N     1 
ATOM   5006  C  CA    A GLU A  1  638 ? 11.681  -13.150 33.333 0.50 63.23  ? 1437 GLU B CA    1 
ATOM   5007  C  CA    B GLU A  1  638 ? 9.775   -10.711 32.625 0.50 45.03  ? 1437 GLU B CA    1 
ATOM   5008  C  C     A GLU A  1  638 ? 12.857  -13.822 34.043 0.50 59.60  ? 1437 GLU B C     1 
ATOM   5009  C  C     B GLU A  1  638 ? 10.792  -11.530 33.444 0.50 45.07  ? 1437 GLU B C     1 
ATOM   5010  O  O     A GLU A  1  638 ? 13.804  -13.149 34.430 0.50 58.32  ? 1437 GLU B O     1 
ATOM   5011  O  O     B GLU A  1  638 ? 11.703  -10.986 34.090 0.50 42.04  ? 1437 GLU B O     1 
ATOM   5012  C  CB    A GLU A  1  638 ? 10.550  -12.936 34.334 0.50 63.87  ? 1437 GLU B CB    1 
ATOM   5013  C  CB    B GLU A  1  638 ? 8.564   -10.339 33.473 0.50 47.26  ? 1437 GLU B CB    1 
ATOM   5014  C  CG    A GLU A  1  638 ? 9.300   -12.273 33.775 0.50 68.95  ? 1437 GLU B CG    1 
ATOM   5015  C  CG    B GLU A  1  638 ? 7.501   -9.515  32.732 0.50 46.23  ? 1437 GLU B CG    1 
ATOM   5016  C  CD    A GLU A  1  638 ? 9.494   -10.814 33.402 0.50 73.79  ? 1437 GLU B CD    1 
ATOM   5017  C  CD    B GLU A  1  638 ? 7.883   -8.054  32.563 0.50 49.59  ? 1437 GLU B CD    1 
ATOM   5018  O  OE1   A GLU A  1  638 ? 10.520  -10.226 33.804 0.50 78.06  ? 1437 GLU B OE1   1 
ATOM   5019  O  OE1   B GLU A  1  638 ? 9.082   -7.697  32.646 0.50 43.62  ? 1437 GLU B OE1   1 
ATOM   5020  O  OE2   A GLU A  1  638 ? 8.602   -10.256 32.713 0.50 78.41  ? 1437 GLU B OE2   1 
ATOM   5021  O  OE2   B GLU A  1  638 ? 6.958   -7.250  32.366 0.50 54.60  ? 1437 GLU B OE2   1 
ATOM   5022  N  N     A ARG A  1  639 ? 12.775  -15.135 34.260 0.50 52.59  ? 1438 ARG B N     1 
ATOM   5023  N  N     B ARG A  1  639 ? 10.616  -12.843 33.398 0.50 45.08  ? 1438 ARG B N     1 
ATOM   5024  C  CA    A ARG A  1  639 ? 13.883  -15.845 34.870 0.50 48.55  ? 1438 ARG B CA    1 
ATOM   5025  C  CA    B ARG A  1  639 ? 11.482  -13.794 34.063 0.50 48.69  ? 1438 ARG B CA    1 
ATOM   5026  C  C     A ARG A  1  639 ? 15.153  -15.459 34.101 0.50 47.71  ? 1438 ARG B C     1 
ATOM   5027  C  C     B ARG A  1  639 ? 12.882  -13.747 33.463 0.50 48.72  ? 1438 ARG B C     1 
ATOM   5028  O  O     A ARG A  1  639 ? 16.123  -15.018 34.682 0.50 42.76  ? 1438 ARG B O     1 
ATOM   5029  O  O     B ARG A  1  639 ? 13.882  -13.705 34.188 0.50 48.86  ? 1438 ARG B O     1 
ATOM   5030  C  CB    A ARG A  1  639 ? 13.633  -17.353 34.876 0.50 47.07  ? 1438 ARG B CB    1 
ATOM   5031  C  CB    B ARG A  1  639 ? 10.912  -15.204 33.867 0.50 50.68  ? 1438 ARG B CB    1 
ATOM   5032  C  CG    A ARG A  1  639 ? 14.394  -18.080 35.966 0.50 51.75  ? 1438 ARG B CG    1 
ATOM   5033  C  CG    B ARG A  1  639 ? 10.937  -16.071 35.102 0.50 54.77  ? 1438 ARG B CG    1 
ATOM   5034  C  CD    A ARG A  1  639 ? 14.321  -17.316 37.278 0.50 53.33  ? 1438 ARG B CD    1 
ATOM   5035  C  CD    B ARG A  1  639 ? 9.967   -17.224 34.998 0.50 56.29  ? 1438 ARG B CD    1 
ATOM   5036  N  NE    A ARG A  1  639 ? 15.423  -17.603 38.198 0.50 55.03  ? 1438 ARG B NE    1 
ATOM   5037  N  NE    B ARG A  1  639 ? 9.494   -17.631 36.320 0.50 58.35  ? 1438 ARG B NE    1 
ATOM   5038  C  CZ    A ARG A  1  639 ? 16.641  -17.055 38.113 0.50 59.61  ? 1438 ARG B CZ    1 
ATOM   5039  C  CZ    B ARG A  1  639 ? 8.992   -18.829 36.622 0.50 58.42  ? 1438 ARG B CZ    1 
ATOM   5040  N  NH1   A ARG A  1  639 ? 16.921  -16.185 37.149 0.50 67.21  ? 1438 ARG B NH1   1 
ATOM   5041  N  NH1   B ARG A  1  639 ? 8.872   -19.773 35.699 0.50 51.02  ? 1438 ARG B NH1   1 
ATOM   5042  N  NH2   A ARG A  1  639 ? 17.593  -17.369 38.989 0.50 60.05  ? 1438 ARG B NH2   1 
ATOM   5043  N  NH2   B ARG A  1  639 ? 8.611   -19.083 37.867 0.50 60.32  ? 1438 ARG B NH2   1 
ATOM   5044  N  N     A ASP A  1  640 ? 15.131  -15.579 32.780 0.50 50.41  ? 1439 ASP B N     1 
ATOM   5045  N  N     B ASP A  1  640 ? 12.940  -13.818 32.134 0.50 47.76  ? 1439 ASP B N     1 
ATOM   5046  C  CA    A ASP A  1  640 ? 16.242  -15.074 31.979 0.50 52.75  ? 1439 ASP B CA    1 
ATOM   5047  C  CA    B ASP A  1  640 ? 14.219  -13.831 31.439 0.50 49.38  ? 1439 ASP B CA    1 
ATOM   5048  C  C     A ASP A  1  640 ? 16.335  -13.524 31.904 0.50 56.38  ? 1439 ASP B C     1 
ATOM   5049  C  C     B ASP A  1  640 ? 14.939  -12.536 31.691 0.50 48.72  ? 1439 ASP B C     1 
ATOM   5050  O  O     A ASP A  1  640 ? 17.442  -12.989 31.920 0.50 58.55  ? 1439 ASP B O     1 
ATOM   5051  O  O     B ASP A  1  640 ? 16.141  -12.537 31.859 0.50 50.67  ? 1439 ASP B O     1 
ATOM   5052  C  CB    A ASP A  1  640 ? 16.249  -15.689 30.581 0.50 50.44  ? 1439 ASP B CB    1 
ATOM   5053  C  CB    B ASP A  1  640 ? 14.058  -14.076 29.939 0.50 48.78  ? 1439 ASP B CB    1 
ATOM   5054  C  CG    A ASP A  1  640 ? 15.940  -17.144 30.605 0.50 50.69  ? 1439 ASP B CG    1 
ATOM   5055  C  CG    B ASP A  1  640 ? 13.585  -15.484 29.628 0.50 52.18  ? 1439 ASP B CG    1 
ATOM   5056  O  OD1   A ASP A  1  640 ? 15.799  -17.700 31.720 0.50 51.17  ? 1439 ASP B OD1   1 
ATOM   5057  O  OD1   B ASP A  1  640 ? 13.660  -16.372 30.514 0.50 51.46  ? 1439 ASP B OD1   1 
ATOM   5058  O  OD2   A ASP A  1  640 ? 15.825  -17.731 29.513 0.50 50.12  ? 1439 ASP B OD2   1 
ATOM   5059  O  OD2   B ASP A  1  640 ? 13.124  -15.692 28.487 0.50 54.51  ? 1439 ASP B OD2   1 
ATOM   5060  N  N     A LYS A  1  641 ? 15.214  -12.803 31.824 0.50 54.00  ? 1440 LYS B N     1 
ATOM   5061  N  N     B LYS A  1  641 ? 14.194  -11.438 31.777 0.50 52.57  ? 1440 LYS B N     1 
ATOM   5062  C  CA    A LYS A  1  641 ? 15.286  -11.325 31.737 0.50 57.52  ? 1440 LYS B CA    1 
ATOM   5063  C  CA    B LYS A  1  641 ? 14.781  -10.147 32.073 0.50 53.38  ? 1440 LYS B CA    1 
ATOM   5064  C  C     A LYS A  1  641 ? 15.875  -10.637 32.989 0.50 60.33  ? 1440 LYS B C     1 
ATOM   5065  C  C     B LYS A  1  641 ? 15.737  -10.236 33.251 0.50 54.84  ? 1440 LYS B C     1 
ATOM   5066  O  O     A LYS A  1  641 ? 16.578  -9.644  32.891 0.50 64.82  ? 1440 LYS B O     1 
ATOM   5067  O  O     B LYS A  1  641 ? 16.646  -9.430  33.366 0.50 60.58  ? 1440 LYS B O     1 
ATOM   5068  C  CB    A LYS A  1  641 ? 13.938  -10.712 31.363 0.50 54.67  ? 1440 LYS B CB    1 
ATOM   5069  C  CB    B LYS A  1  641 ? 13.704  -9.118  32.415 0.50 54.76  ? 1440 LYS B CB    1 
ATOM   5070  C  CG    A LYS A  1  641 ? 13.897  -9.209  31.525 0.50 54.04  ? 1440 LYS B CG    1 
ATOM   5071  C  CG    B LYS A  1  641 ? 13.118  -8.357  31.240 0.50 56.94  ? 1440 LYS B CG    1 
ATOM   5072  C  CD    A LYS A  1  641 ? 12.711  -8.643  30.764 0.50 58.98  ? 1440 LYS B CD    1 
ATOM   5073  C  CD    B LYS A  1  641 ? 12.145  -7.290  31.737 0.50 59.77  ? 1440 LYS B CD    1 
ATOM   5074  C  CE    A LYS A  1  641 ? 12.424  -7.198  31.141 0.50 59.26  ? 1440 LYS B CE    1 
ATOM   5075  C  CE    B LYS A  1  641 ? 11.146  -6.878  30.662 0.50 62.31  ? 1440 LYS B CE    1 
ATOM   5076  N  NZ    A LYS A  1  641 ? 11.447  -6.590  30.190 0.50 59.75  ? 1440 LYS B NZ    1 
ATOM   5077  N  NZ    B LYS A  1  641 ? 10.101  -5.953  31.199 0.50 65.35  ? 1440 LYS B NZ    1 
ATOM   5078  N  N     . ILE A  1  642 ? 15.570  -11.184 34.152 1.00 57.73  ? 1441 ILE B N     1 
ATOM   5079  C  CA    . ILE A  1  642 ? 16.178  -10.836 35.399 1.00 50.20  ? 1441 ILE B CA    1 
ATOM   5080  C  C     . ILE A  1  642 ? 17.635  -11.222 35.352 1.00 48.24  ? 1441 ILE B C     1 
ATOM   5081  O  O     . ILE A  1  642 ? 18.483  -10.454 35.735 1.00 43.86  ? 1441 ILE B O     1 
ATOM   5082  C  CB    . ILE A  1  642 ? 15.384  -11.387 36.585 1.00 52.07  ? 1441 ILE B CB    1 
ATOM   5083  C  CG1   . ILE A  1  642 ? 14.219  -10.436 36.885 1.00 51.45  ? 1441 ILE B CG1   1 
ATOM   5084  C  CG2   . ILE A  1  642 ? 16.263  -11.734 37.800 1.00 48.63  ? 1441 ILE B CG2   1 
ATOM   5085  C  CD1   . ILE A  1  642 ? 13.353  -10.837 38.071 1.00 66.13  ? 1441 ILE B CD1   1 
ATOM   5086  N  N     . GLU A  1  643 ? 17.906  -12.396 34.806 1.00 51.87  ? 1442 GLU B N     1 
ATOM   5087  C  CA    . GLU A  1  643 ? 19.273  -12.875 34.690 1.00 57.28  ? 1442 GLU B CA    1 
ATOM   5088  C  C     . GLU A  1  643 ? 20.038  -11.997 33.693 1.00 57.91  ? 1442 GLU B C     1 
ATOM   5089  O  O     . GLU A  1  643 ? 21.231  -11.783 33.854 1.00 58.26  ? 1442 GLU B O     1 
ATOM   5090  C  CB    . GLU A  1  643 ? 19.328  -14.375 34.330 1.00 61.52  ? 1442 GLU B CB    1 
ATOM   5091  C  CG    . GLU A  1  643 ? 20.646  -15.078 34.735 1.00 69.96  ? 1442 GLU B CG    1 
ATOM   5092  C  CD    . GLU A  1  643 ? 20.734  -15.513 36.230 1.00 71.23  ? 1442 GLU B CD    1 
ATOM   5093  O  OE1   . GLU A  1  643 ? 20.097  -14.888 37.104 1.00 81.72  ? 1442 GLU B OE1   1 
ATOM   5094  O  OE2   . GLU A  1  643 ? 21.398  -16.502 36.561 1.00 65.19  ? 1442 GLU B OE2   1 
ATOM   5095  N  N     . ALA A  1  644 ? 19.334  -11.447 32.708 1.00 53.67  ? 1443 ALA B N     1 
ATOM   5096  C  CA    . ALA A  1  644 ? 19.952  -10.549 31.746 1.00 54.70  ? 1443 ALA B CA    1 
ATOM   5097  C  C     . ALA A  1  644 ? 20.409  -9.245  32.405 1.00 61.16  ? 1443 ALA B C     1 
ATOM   5098  O  O     . ALA A  1  644 ? 21.498  -8.750  32.100 1.00 64.57  ? 1443 ALA B O     1 
ATOM   5099  C  CB    . ALA A  1  644 ? 19.014  -10.257 30.597 1.00 56.34  ? 1443 ALA B CB    1 
ATOM   5100  N  N     . GLU A  1  645 ? 19.579  -8.701  33.293 1.00 59.13  ? 1444 GLU B N     1 
ATOM   5101  C  CA    . GLU A  1  645 ? 19.909  -7.486  33.982 1.00 50.70  ? 1444 GLU B CA    1 
ATOM   5102  C  C     . GLU A  1  645 ? 21.058  -7.764  34.911 1.00 56.18  ? 1444 GLU B C     1 
ATOM   5103  O  O     . GLU A  1  645 ? 21.992  -6.994  35.013 1.00 60.01  ? 1444 GLU B O     1 
ATOM   5104  C  CB    . GLU A  1  645 ? 18.743  -7.004  34.814 1.00 45.50  ? 1444 GLU B CB    1 
ATOM   5105  C  CG    . GLU A  1  645 ? 18.978  -5.580  35.257 1.00 40.92  ? 1444 GLU B CG    1 
ATOM   5106  C  CD    . GLU A  1  645 ? 17.902  -5.074  36.143 1.00 43.31  ? 1444 GLU B CD    1 
ATOM   5107  O  OE1   . GLU A  1  645 ? 18.122  -4.070  36.824 1.00 50.19  ? 1444 GLU B OE1   1 
ATOM   5108  O  OE2   . GLU A  1  645 ? 16.810  -5.660  36.151 1.00 46.06  ? 1444 GLU B OE2   1 
ATOM   5109  N  N     . TYR A  1  646 ? 20.968  -8.885  35.601 1.00 54.04  ? 1445 TYR B N     1 
ATOM   5110  C  CA    . TYR A  1  646 ? 21.976  -9.246  36.567 1.00 47.32  ? 1445 TYR B CA    1 
ATOM   5111  C  C     . TYR A  1  646 ? 23.328  -9.425  35.937 1.00 54.25  ? 1445 TYR B C     1 
ATOM   5112  O  O     . TYR A  1  646 ? 24.347  -9.136  36.550 1.00 58.68  ? 1445 TYR B O     1 
ATOM   5113  C  CB    . TYR A  1  646 ? 21.574  -10.506 37.290 1.00 40.87  ? 1445 TYR B CB    1 
ATOM   5114  C  CG    . TYR A  1  646 ? 22.505  -10.869 38.396 1.00 44.85  ? 1445 TYR B CG    1 
ATOM   5115  C  CD1   . TYR A  1  646 ? 22.469  -10.198 39.635 1.00 40.69  ? 1445 TYR B CD1   1 
ATOM   5116  C  CD2   . TYR A  1  646 ? 23.439  -11.876 38.210 1.00 42.37  ? 1445 TYR B CD2   1 
ATOM   5117  C  CE1   . TYR A  1  646 ? 23.361  -10.525 40.633 1.00 41.02  ? 1445 TYR B CE1   1 
ATOM   5118  C  CE2   . TYR A  1  646 ? 24.311  -12.220 39.211 1.00 44.68  ? 1445 TYR B CE2   1 
ATOM   5119  C  CZ    . TYR A  1  646 ? 24.273  -11.566 40.405 1.00 40.90  ? 1445 TYR B CZ    1 
ATOM   5120  O  OH    . TYR A  1  646 ? 25.158  -11.992 41.363 1.00 45.30  ? 1445 TYR B OH    1 
ATOM   5121  N  N     . ASN A  1  647 ? 23.347  -9.896  34.701 1.00 57.98  ? 1446 ASN B N     1 
ATOM   5122  C  CA    . ASN A  1  647 ? 24.609  -10.093 34.048 1.00 57.60  ? 1446 ASN B CA    1 
ATOM   5123  C  C     . ASN A  1  647 ? 25.291  -8.832  33.617 1.00 52.99  ? 1446 ASN B C     1 
ATOM   5124  O  O     . ASN A  1  647 ? 26.490  -8.724  33.769 1.00 49.81  ? 1446 ASN B O     1 
ATOM   5125  C  CB    . ASN A  1  647 ? 24.486  -11.106 32.928 1.00 65.45  ? 1446 ASN B CB    1 
ATOM   5126  C  CG    . ASN A  1  647 ? 24.626  -12.512 33.448 1.00 69.26  ? 1446 ASN B CG    1 
ATOM   5127  O  OD1   . ASN A  1  647 ? 25.528  -12.818 34.225 1.00 79.90  ? 1446 ASN B OD1   1 
ATOM   5128  N  ND2   . ASN A  1  647 ? 23.709  -13.359 33.068 1.00 79.13  ? 1446 ASN B ND2   1 
ATOM   5129  N  N     . GLU A  1  648 ? 24.526  -7.892  33.085 1.00 54.35  ? 1447 GLU B N     1 
ATOM   5130  C  CA    . GLU A  1  648 ? 25.053  -6.600  32.738 1.00 52.87  ? 1447 GLU B CA    1 
ATOM   5131  C  C     . GLU A  1  648 ? 25.557  -5.845  33.983 1.00 55.61  ? 1447 GLU B C     1 
ATOM   5132  O  O     . GLU A  1  648 ? 26.560  -5.205  33.924 1.00 52.00  ? 1447 GLU B O     1 
ATOM   5133  C  CB    . GLU A  1  648 ? 24.014  -5.806  31.955 1.00 49.60  ? 1447 GLU B CB    1 
ATOM   5134  N  N     . LEU A  1  649 ? 24.870  -5.960  35.110 1.00 58.13  ? 1448 LEU B N     1 
ATOM   5135  C  CA    . LEU A  1  649 ? 25.249  -5.246  36.301 1.00 54.75  ? 1448 LEU B CA    1 
ATOM   5136  C  C     . LEU A  1  649 ? 26.602  -5.652  36.802 1.00 56.22  ? 1448 LEU B C     1 
ATOM   5137  O  O     . LEU A  1  649 ? 27.364  -4.818  37.263 1.00 54.25  ? 1448 LEU B O     1 
ATOM   5138  C  CB    . LEU A  1  649 ? 24.263  -5.532  37.406 1.00 58.12  ? 1448 LEU B CB    1 
ATOM   5139  C  CG    . LEU A  1  649 ? 23.132  -4.551  37.704 1.00 63.24  ? 1448 LEU B CG    1 
ATOM   5140  C  CD1   . LEU A  1  649 ? 22.287  -5.138  38.810 1.00 58.30  ? 1448 LEU B CD1   1 
ATOM   5141  C  CD2   . LEU A  1  649 ? 23.676  -3.220  38.151 1.00 58.77  ? 1448 LEU B CD2   1 
ATOM   5142  N  N     . LEU A  1  650 ? 26.894  -6.944  36.672 1.00 51.04  ? 1449 LEU B N     1 
ATOM   5143  C  CA    . LEU A  1  650 ? 28.157  -7.485  37.156 1.00 53.07  ? 1449 LEU B CA    1 
ATOM   5144  C  C     . LEU A  1  650 ? 29.261  -6.970  36.291 1.00 51.12  ? 1449 LEU B C     1 
ATOM   5145  O  O     . LEU A  1  650 ? 30.337  -6.639  36.674 1.00 46.60  ? 1449 LEU B O     1 
ATOM   5146  C  CB    . LEU A  1  650 ? 28.127  -9.010  37.109 1.00 55.70  ? 1449 LEU B CB    1 
ATOM   5147  C  CG    . LEU A  1  650 ? 27.241  -9.701  38.144 1.00 57.76  ? 1449 LEU B CG    1 
ATOM   5148  C  CD1   . LEU A  1  650 ? 27.109  -11.177 37.836 1.00 64.74  ? 1449 LEU B CD1   1 
ATOM   5149  C  CD2   . LEU A  1  650 ? 27.762  -9.516  39.562 1.00 58.89  ? 1449 LEU B CD2   1 
ATOM   5150  N  N     A ASN A  1  651 ? 28.945  -6.868  35.056 0.50 53.18  ? 1450 ASN B N     1 
ATOM   5151  N  N     B ASN A  1  651 ? 29.001  -6.889  35.018 0.50 50.44  ? 1450 ASN B N     1 
ATOM   5152  C  CA    A ASN A  1  651 ? 29.887  -6.283  34.256 0.50 56.33  ? 1450 ASN B CA    1 
ATOM   5153  C  CA    B ASN A  1  651 ? 29.989  -6.229  34.234 0.50 51.42  ? 1450 ASN B CA    1 
ATOM   5154  C  C     A ASN A  1  651 ? 30.109  -4.806  34.592 0.50 57.09  ? 1450 ASN B C     1 
ATOM   5155  C  C     B ASN A  1  651 ? 30.144  -4.764  34.617 0.50 53.79  ? 1450 ASN B C     1 
ATOM   5156  O  O     A ASN A  1  651 ? 31.239  -4.343  34.628 0.50 61.22  ? 1450 ASN B O     1 
ATOM   5157  O  O     B ASN A  1  651 ? 31.258  -4.290  34.827 0.50 56.82  ? 1450 ASN B O     1 
ATOM   5158  C  CB    A ASN A  1  651 ? 29.385  -6.463  32.896 0.50 57.20  ? 1450 ASN B CB    1 
ATOM   5159  C  CB    B ASN A  1  651 ? 29.605  -6.394  32.830 0.50 48.31  ? 1450 ASN B CB    1 
ATOM   5160  C  CG    A ASN A  1  651 ? 30.400  -6.038  31.872 0.50 60.86  ? 1450 ASN B CG    1 
ATOM   5161  C  CG    B ASN A  1  651 ? 29.793  -7.801  32.370 0.50 48.32  ? 1450 ASN B CG    1 
ATOM   5162  O  OD1   A ASN A  1  651 ? 31.294  -6.810  31.523 0.50 62.39  ? 1450 ASN B OD1   1 
ATOM   5163  O  OD1   B ASN A  1  651 ? 30.338  -8.618  33.102 0.50 49.92  ? 1450 ASN B OD1   1 
ATOM   5164  N  ND2   A ASN A  1  651 ? 30.296  -4.801  31.397 0.50 68.20  ? 1450 ASN B ND2   1 
ATOM   5165  N  ND2   B ASN A  1  651 ? 29.367  -8.098  31.153 0.50 48.61  ? 1450 ASN B ND2   1 
ATOM   5166  N  N     . TYR A  1  652 ? 29.018  -4.083  34.787 1.00 52.22  ? 1451 TYR B N     1 
ATOM   5167  C  CA    . TYR A  1  652 ? 29.047  -2.692  35.115 1.00 48.44  ? 1451 TYR B CA    1 
ATOM   5168  C  C     . TYR A  1  652 ? 29.759  -2.452  36.429 1.00 46.34  ? 1451 TYR B C     1 
ATOM   5169  O  O     . TYR A  1  652 ? 30.536  -1.563  36.557 1.00 43.45  ? 1451 TYR B O     1 
ATOM   5170  C  CB    . TYR A  1  652 ? 27.628  -2.212  35.182 1.00 48.87  ? 1451 TYR B CB    1 
ATOM   5171  C  CG    . TYR A  1  652 ? 27.494  -0.760  35.346 1.00 45.60  ? 1451 TYR B CG    1 
ATOM   5172  C  CD1   . TYR A  1  652 ? 28.337  0.138   34.648 1.00 41.36  ? 1451 TYR B CD1   1 
ATOM   5173  C  CD2   . TYR A  1  652 ? 26.491  -0.265  36.154 1.00 46.10  ? 1451 TYR B CD2   1 
ATOM   5174  C  CE1   . TYR A  1  652 ? 28.183  1.484   34.813 1.00 41.84  ? 1451 TYR B CE1   1 
ATOM   5175  C  CE2   . TYR A  1  652 ? 26.320  1.072   36.311 1.00 41.52  ? 1451 TYR B CE2   1 
ATOM   5176  C  CZ    . TYR A  1  652 ? 27.166  1.917   35.650 1.00 42.74  ? 1451 TYR B CZ    1 
ATOM   5177  O  OH    . TYR A  1  652 ? 26.939  3.198   35.843 1.00 40.13  ? 1451 TYR B OH    1 
ATOM   5178  N  N     . ILE A  1  653 ? 29.482  -3.308  37.394 1.00 48.32  ? 1452 ILE B N     1 
ATOM   5179  C  CA    . ILE A  1  653 ? 30.100  -3.168  38.699 1.00 47.41  ? 1452 ILE B CA    1 
ATOM   5180  C  C     . ILE A  1  653 ? 31.619  -3.232  38.565 1.00 57.33  ? 1452 ILE B C     1 
ATOM   5181  O  O     . ILE A  1  653 ? 32.357  -2.474  39.213 1.00 58.27  ? 1452 ILE B O     1 
ATOM   5182  C  CB    . ILE A  1  653 ? 29.585  -4.218  39.695 1.00 42.96  ? 1452 ILE B CB    1 
ATOM   5183  C  CG1   . ILE A  1  653 ? 28.131  -3.903  40.093 1.00 38.55  ? 1452 ILE B CG1   1 
ATOM   5184  C  CG2   . ILE A  1  653 ? 30.480  -4.324  40.929 1.00 37.53  ? 1452 ILE B CG2   1 
ATOM   5185  C  CD1   . ILE A  1  653 ? 27.456  -4.987  40.913 1.00 40.11  ? 1452 ILE B CD1   1 
ATOM   5186  N  N     . SER A  1  654 ? 32.077  -4.145  37.715 1.00 56.00  ? 1453 SER B N     1 
ATOM   5187  C  CA    . SER A  1  654 ? 33.493  -4.318  37.475 1.00 52.38  ? 1453 SER B CA    1 
ATOM   5188  C  C     . SER A  1  654 ? 34.091  -3.075  36.832 1.00 47.74  ? 1453 SER B C     1 
ATOM   5189  O  O     . SER A  1  654 ? 35.180  -2.671  37.213 1.00 49.49  ? 1453 SER B O     1 
ATOM   5190  C  CB    . SER A  1  654 ? 33.696  -5.538  36.575 1.00 51.24  ? 1453 SER B CB    1 
ATOM   5191  O  OG    . SER A  1  654 ? 34.944  -6.144  36.811 1.00 71.21  ? 1453 SER B OG    1 
ATOM   5192  N  N     A GLU A  1  655 ? 33.367  -2.497  35.879 0.50 48.21  ? 1454 GLU B N     1 
ATOM   5193  N  N     B GLU A  1  655 ? 33.414  -2.487  35.847 0.50 47.95  ? 1454 GLU B N     1 
ATOM   5194  C  CA    A GLU A  1  655 ? 33.811  -1.289  35.203 0.50 52.35  ? 1454 GLU B CA    1 
ATOM   5195  C  CA    B GLU A  1  655 ? 33.899  -1.256  35.206 0.50 52.48  ? 1454 GLU B CA    1 
ATOM   5196  C  C     A GLU A  1  655 ? 33.972  -0.104  36.168 0.50 53.84  ? 1454 GLU B C     1 
ATOM   5197  C  C     B GLU A  1  655 ? 34.017  -0.088  36.216 0.50 53.80  ? 1454 GLU B C     1 
ATOM   5198  O  O     A GLU A  1  655 ? 34.948  0.632   36.094 0.50 55.03  ? 1454 GLU B O     1 
ATOM   5199  O  O     B GLU A  1  655 ? 35.011  0.640   36.235 0.50 55.15  ? 1454 GLU B O     1 
ATOM   5200  C  CB    A GLU A  1  655 ? 32.855  -0.895  34.085 0.50 51.36  ? 1454 GLU B CB    1 
ATOM   5201  C  CB    B GLU A  1  655 ? 33.012  -0.893  34.002 0.50 50.98  ? 1454 GLU B CB    1 
ATOM   5202  C  CG    A GLU A  1  655 ? 33.537  0.159   33.207 0.50 51.01  ? 1454 GLU B CG    1 
ATOM   5203  C  CG    B GLU A  1  655 ? 33.162  -1.810  32.786 0.50 52.68  ? 1454 GLU B CG    1 
ATOM   5204  C  CD    A GLU A  1  655 ? 32.654  0.920   32.220 0.50 53.63  ? 1454 GLU B CD    1 
ATOM   5205  C  CD    B GLU A  1  655 ? 31.931  -1.846  31.863 0.50 53.70  ? 1454 GLU B CD    1 
ATOM   5206  O  OE1   A GLU A  1  655 ? 31.414  0.816   32.209 0.50 53.87  ? 1454 GLU B OE1   1 
ATOM   5207  O  OE1   B GLU A  1  655 ? 31.034  -0.966  31.965 0.50 53.43  ? 1454 GLU B OE1   1 
ATOM   5208  O  OE2   A GLU A  1  655 ? 33.232  1.661   31.414 0.50 58.20  ? 1454 GLU B OE2   1 
ATOM   5209  O  OE2   B GLU A  1  655 ? 31.866  -2.766  31.017 0.50 51.38  ? 1454 GLU B OE2   1 
ATOM   5210  N  N     . LEU A  1  656 ? 33.012  0.054   37.074 1.00 52.79  ? 1455 LEU B N     1 
ATOM   5211  C  CA    . LEU A  1  656 ? 33.048  1.120   38.076 1.00 48.94  ? 1455 LEU B CA    1 
ATOM   5212  C  C     . LEU A  1  656 ? 34.193  0.933   39.049 1.00 50.03  ? 1455 LEU B C     1 
ATOM   5213  O  O     . LEU A  1  656 ? 34.844  1.902   39.439 1.00 43.05  ? 1455 LEU B O     1 
ATOM   5214  C  CB    . LEU A  1  656 ? 31.719  1.228   38.821 1.00 41.32  ? 1455 LEU B CB    1 
ATOM   5215  C  CG    . LEU A  1  656 ? 30.516  1.654   37.943 1.00 43.21  ? 1455 LEU B CG    1 
ATOM   5216  C  CD1   . LEU A  1  656 ? 29.237  1.343   38.683 1.00 39.21  ? 1455 LEU B CD1   1 
ATOM   5217  C  CD2   . LEU A  1  656 ? 30.574  3.124   37.507 1.00 41.11  ? 1455 LEU B CD2   1 
ATOM   5218  N  N     . GLU A  1  657 ? 34.462  -0.330  39.401 1.00 47.56  ? 1456 GLU B N     1 
ATOM   5219  C  CA    . GLU A  1  657 ? 35.564  -0.629  40.326 1.00 43.73  ? 1456 GLU B CA    1 
ATOM   5220  C  C     . GLU A  1  657 ? 36.937  -0.315  39.768 1.00 42.15  ? 1456 GLU B C     1 
ATOM   5221  O  O     . GLU A  1  657 ? 37.793  0.142   40.516 1.00 46.36  ? 1456 GLU B O     1 
ATOM   5222  C  CB    . GLU A  1  657 ? 35.495  -2.068  40.819 1.00 42.61  ? 1456 GLU B CB    1 
ATOM   5223  C  CG    . GLU A  1  657 ? 34.558  -2.188  41.997 1.00 45.14  ? 1456 GLU B CG    1 
ATOM   5224  C  CD    . GLU A  1  657 ? 34.205  -3.603  42.312 1.00 52.46  ? 1456 GLU B CD    1 
ATOM   5225  O  OE1   . GLU A  1  657 ? 33.614  -3.806  43.385 1.00 56.75  ? 1456 GLU B OE1   1 
ATOM   5226  O  OE2   . GLU A  1  657 ? 34.509  -4.497  41.488 1.00 59.54  ? 1456 GLU B OE2   1 
ATOM   5227  N  N     . THR A  1  658 ? 37.107  -0.524  38.474 1.00 42.48  ? 1457 THR B N     1 
ATOM   5228  C  CA    . THR A  1  658 ? 38.333  -0.241  37.790 1.00 45.92  ? 1457 THR B CA    1 
ATOM   5229  C  C     . THR A  1  658 ? 38.625  1.226   37.871 1.00 47.72  ? 1457 THR B C     1 
ATOM   5230  O  O     . THR A  1  658 ? 39.744  1.595   38.115 1.00 55.10  ? 1457 THR B O     1 
ATOM   5231  C  CB    . THR A  1  658 ? 38.204  -0.644  36.309 1.00 47.97  ? 1457 THR B CB    1 
ATOM   5232  O  OG1   . THR A  1  658 ? 38.054  -2.059  36.226 1.00 51.10  ? 1457 THR B OG1   1 
ATOM   5233  C  CG2   . THR A  1  658 ? 39.443  -0.247  35.556 1.00 42.95  ? 1457 THR B CG2   1 
ATOM   5234  N  N     . ILE A  1  659 ? 37.614  2.057   37.667 1.00 48.20  ? 1458 ILE B N     1 
ATOM   5235  C  CA    . ILE A  1  659 ? 37.778  3.492   37.720 1.00 44.83  ? 1458 ILE B CA    1 
ATOM   5236  C  C     . ILE A  1  659 ? 38.208  3.921   39.114 1.00 44.67  ? 1458 ILE B C     1 
ATOM   5237  O  O     . ILE A  1  659 ? 39.096  4.757   39.254 1.00 51.96  ? 1458 ILE B O     1 
ATOM   5238  C  CB    . ILE A  1  659 ? 36.487  4.226   37.309 1.00 45.64  ? 1458 ILE B CB    1 
ATOM   5239  C  CG1   . ILE A  1  659 ? 36.151  3.904   35.855 1.00 44.65  ? 1458 ILE B CG1   1 
ATOM   5240  C  CG2   . ILE A  1  659 ? 36.607  5.738   37.541 1.00 43.35  ? 1458 ILE B CG2   1 
ATOM   5241  C  CD1   . ILE A  1  659 ? 34.704  4.188   35.487 1.00 43.61  ? 1458 ILE B CD1   1 
ATOM   5242  N  N     . LEU A  1  660 ? 37.577  3.381   40.146 1.00 40.75  ? 1459 LEU B N     1 
ATOM   5243  C  CA    . LEU A  1  660 ? 37.915  3.798   41.506 1.00 38.18  ? 1459 LEU B CA    1 
ATOM   5244  C  C     . LEU A  1  660 ? 39.272  3.294   41.949 1.00 41.27  ? 1459 LEU B C     1 
ATOM   5245  O  O     . LEU A  1  660 ? 39.878  3.891   42.774 1.00 45.13  ? 1459 LEU B O     1 
ATOM   5246  C  CB    . LEU A  1  660 ? 36.847  3.356   42.493 1.00 34.60  ? 1459 LEU B CB    1 
ATOM   5247  C  CG    . LEU A  1  660 ? 35.473  4.042   42.284 1.00 39.49  ? 1459 LEU B CG    1 
ATOM   5248  C  CD1   . LEU A  1  660 ? 34.392  3.477   43.172 1.00 30.70  ? 1459 LEU B CD1   1 
ATOM   5249  C  CD2   . LEU A  1  660 ? 35.546  5.550   42.473 1.00 36.16  ? 1459 LEU B CD2   1 
ATOM   5250  N  N     . ALA A  1  661 ? 39.736  2.201   41.365 1.00 45.13  ? 1460 ALA B N     1 
ATOM   5251  C  CA    . ALA A  1  661 ? 41.005  1.605   41.709 1.00 49.69  ? 1460 ALA B CA    1 
ATOM   5252  C  C     . ALA A  1  661 ? 42.222  2.339   41.153 1.00 52.20  ? 1460 ALA B C     1 
ATOM   5253  O  O     . ALA A  1  661 ? 43.243  2.312   41.788 1.00 58.42  ? 1460 ALA B O     1 
ATOM   5254  C  CB    . ALA A  1  661 ? 41.018  0.152   41.254 1.00 43.27  ? 1460 ALA B CB    1 
ATOM   5255  N  N     . ASP A  1  662 ? 42.122  2.949   39.973 1.00 46.06  ? 1461 ASP B N     1 
ATOM   5256  C  CA    . ASP A  1  662 ? 43.224  3.660   39.362 1.00 46.16  ? 1461 ASP B CA    1 
ATOM   5257  C  C     . ASP A  1  662 ? 42.888  5.141   39.100 1.00 47.33  ? 1461 ASP B C     1 
ATOM   5258  O  O     . ASP A  1  662 ? 41.991  5.434   38.308 1.00 44.64  ? 1461 ASP B O     1 
ATOM   5259  C  CB    . ASP A  1  662 ? 43.565  2.976   38.028 1.00 48.39  ? 1461 ASP B CB    1 
ATOM   5260  C  CG    . ASP A  1  662 ? 44.857  3.450   37.434 1.00 49.65  ? 1461 ASP B CG    1 
ATOM   5261  O  OD1   . ASP A  1  662 ? 45.440  4.432   37.942 1.00 53.73  ? 1461 ASP B OD1   1 
ATOM   5262  O  OD2   . ASP A  1  662 ? 45.296  2.828   36.451 1.00 58.28  ? 1461 ASP B OD2   1 
ATOM   5263  N  N     . GLU A  1  663 ? 43.642  6.047   39.715 1.00 45.55  ? 1462 GLU B N     1 
ATOM   5264  C  CA    . GLU A  1  663 ? 43.484  7.497   39.528 1.00 47.52  ? 1462 GLU B CA    1 
ATOM   5265  C  C     . GLU A  1  663 ? 43.622  7.887   38.066 1.00 45.00  ? 1462 GLU B C     1 
ATOM   5266  O  O     . GLU A  1  663 ? 42.902  8.752   37.587 1.00 49.66  ? 1462 GLU B O     1 
ATOM   5267  C  CB    . GLU A  1  663 ? 44.536  8.297   40.302 1.00 48.62  ? 1462 GLU B CB    1 
ATOM   5268  C  CG    . GLU A  1  663 ? 44.449  8.262   41.819 1.00 66.47  ? 1462 GLU B CG    1 
ATOM   5269  C  CD    . GLU A  1  663 ? 43.161  8.857   42.407 1.00 86.15  ? 1462 GLU B CD    1 
ATOM   5270  O  OE1   . GLU A  1  663 ? 42.491  9.725   41.773 1.00 91.45  ? 1462 GLU B OE1   1 
ATOM   5271  O  OE2   . GLU A  1  663 ? 42.826  8.467   43.559 1.00 96.15  ? 1462 GLU B OE2   1 
ATOM   5272  N  N     . GLU A  1  664 ? 44.547  7.244   37.374 1.00 39.58  ? 1463 GLU B N     1 
ATOM   5273  C  CA    . GLU A  1  664 ? 44.764  7.543   35.969 1.00 44.90  ? 1463 GLU B CA    1 
ATOM   5274  C  C     . GLU A  1  664 ? 43.562  7.215   35.106 1.00 43.81  ? 1463 GLU B C     1 
ATOM   5275  O  O     . GLU A  1  664 ? 43.264  7.927   34.163 1.00 47.96  ? 1463 GLU B O     1 
ATOM   5276  C  CB    . GLU A  1  664 ? 45.990  6.797   35.431 1.00 48.38  ? 1463 GLU B CB    1 
ATOM   5277  C  CG    . GLU A  1  664 ? 46.369  7.176   34.002 1.00 55.18  ? 1463 GLU B CG    1 
ATOM   5278  C  CD    . GLU A  1  664 ? 46.636  8.682   33.840 1.00 56.08  ? 1463 GLU B CD    1 
ATOM   5279  O  OE1   . GLU A  1  664 ? 46.304  9.202   32.762 1.00 53.49  ? 1463 GLU B OE1   1 
ATOM   5280  O  OE2   . GLU A  1  664 ? 47.155  9.351   34.777 1.00 53.30  ? 1463 GLU B OE2   1 
ATOM   5281  N  N     . VAL A  1  665 ? 42.888  6.115   35.429 1.00 45.33  ? 1464 VAL B N     1 
ATOM   5282  C  CA    . VAL A  1  665 ? 41.693  5.712   34.708 1.00 39.48  ? 1464 VAL B CA    1 
ATOM   5283  C  C     . VAL A  1  665 ? 40.583  6.731   34.986 1.00 37.24  ? 1464 VAL B C     1 
ATOM   5284  O  O     . VAL A  1  665 ? 39.886  7.113   34.057 1.00 35.71  ? 1464 VAL B O     1 
ATOM   5285  C  CB    . VAL A  1  665 ? 41.217  4.308   35.132 1.00 37.77  ? 1464 VAL B CB    1 
ATOM   5286  C  CG1   . VAL A  1  665 ? 39.902  3.966   34.443 1.00 30.31  ? 1464 VAL B CG1   1 
ATOM   5287  C  CG2   . VAL A  1  665 ? 42.265  3.276   34.766 1.00 35.63  ? 1464 VAL B CG2   1 
ATOM   5288  N  N     . LEU A  1  666 ? 40.443  7.154   36.242 1.00 31.68  ? 1465 LEU B N     1 
ATOM   5289  C  CA    . LEU A  1  666 ? 39.459  8.158   36.621 1.00 38.67  ? 1465 LEU B CA    1 
ATOM   5290  C  C     . LEU A  1  666 ? 39.742  9.496   35.910 1.00 39.70  ? 1465 LEU B C     1 
ATOM   5291  O  O     . LEU A  1  666 ? 38.819  10.145  35.402 1.00 38.16  ? 1465 LEU B O     1 
ATOM   5292  C  CB    . LEU A  1  666 ? 39.447  8.350   38.126 1.00 42.40  ? 1465 LEU B CB    1 
ATOM   5293  C  CG    . LEU A  1  666 ? 38.647  9.576   38.673 1.00 51.76  ? 1465 LEU B CG    1 
ATOM   5294  C  CD1   . LEU A  1  666 ? 37.140  9.411   38.500 1.00 47.14  ? 1465 LEU B CD1   1 
ATOM   5295  C  CD2   . LEU A  1  666 ? 38.940  9.852   40.143 1.00 55.62  ? 1465 LEU B CD2   1 
ATOM   5296  N  N     . LEU A  1  667 ? 41.032  9.847   35.835 1.00 35.95  ? 1466 LEU B N     1 
ATOM   5297  C  CA    . LEU A  1  667 ? 41.452  11.053  35.193 1.00 37.05  ? 1466 LEU B CA    1 
ATOM   5298  C  C     . LEU A  1  667 ? 41.160  11.021  33.706 1.00 36.88  ? 1466 LEU B C     1 
ATOM   5299  O  O     . LEU A  1  667 ? 40.730  12.038  33.104 1.00 34.66  ? 1466 LEU B O     1 
ATOM   5300  C  CB    . LEU A  1  667 ? 42.946  11.313  35.472 1.00 38.56  ? 1466 LEU B CB    1 
ATOM   5301  C  CG    . LEU A  1  667 ? 43.454  12.712  35.125 1.00 42.44  ? 1466 LEU B CG    1 
ATOM   5302  C  CD1   . LEU A  1  667 ? 42.505  13.869  35.491 1.00 39.26  ? 1466 LEU B CD1   1 
ATOM   5303  C  CD2   . LEU A  1  667 ? 44.838  12.953  35.722 1.00 43.89  ? 1466 LEU B CD2   1 
ATOM   5304  N  N     . GLN A  1  668 ? 41.397  9.866   33.098 1.00 34.35  ? 1467 GLN B N     1 
ATOM   5305  C  CA    . GLN A  1  668 ? 41.122  9.697   31.648 1.00 40.66  ? 1467 GLN B CA    1 
ATOM   5306  C  C     . GLN A  1  668 ? 39.630  9.830   31.350 1.00 38.63  ? 1467 GLN B C     1 
ATOM   5307  O  O     . GLN A  1  668 ? 39.264  10.326  30.288 1.00 42.38  ? 1467 GLN B O     1 
ATOM   5308  C  CB    . GLN A  1  668 ? 41.623  8.329   31.122 1.00 37.56  ? 1467 GLN B CB    1 
ATOM   5309  C  CG    . GLN A  1  668 ? 41.649  8.239   29.608 1.00 35.94  ? 1467 GLN B CG    1 
ATOM   5310  C  CD    . GLN A  1  668 ? 42.411  9.400   28.983 1.00 41.64  ? 1467 GLN B CD    1 
ATOM   5311  O  OE1   . GLN A  1  668 ? 43.376  9.900   29.544 1.00 52.04  ? 1467 GLN B OE1   1 
ATOM   5312  N  NE2   . GLN A  1  668 ? 41.964  9.844   27.817 1.00 37.32  ? 1467 GLN B NE2   1 
ATOM   5313  N  N     . LEU A  1  669 ? 38.796  9.360   32.280 1.00 32.14  ? 1468 LEU B N     1 
ATOM   5314  C  CA    . LEU A  1  669 ? 37.365  9.436   32.107 1.00 36.17  ? 1468 LEU B CA    1 
ATOM   5315  C  C     . LEU A  1  669 ? 36.930  10.920  32.103 1.00 39.74  ? 1468 LEU B C     1 
ATOM   5316  O  O     . LEU A  1  669 ? 36.106  11.313  31.280 1.00 39.50  ? 1468 LEU B O     1 
ATOM   5317  C  CB    . LEU A  1  669 ? 36.678  8.725   33.253 1.00 34.17  ? 1468 LEU B CB    1 
ATOM   5318  C  CG    . LEU A  1  669 ? 35.137  8.619   33.244 1.00 39.28  ? 1468 LEU B CG    1 
ATOM   5319  C  CD1   . LEU A  1  669 ? 34.578  8.123   31.918 1.00 35.39  ? 1468 LEU B CD1   1 
ATOM   5320  C  CD2   . LEU A  1  669 ? 34.670  7.734   34.395 1.00 31.82  ? 1468 LEU B CD2   1 
ATOM   5321  N  N     . VAL A  1  670 ? 37.536  11.714  32.995 1.00 37.93  ? 1469 VAL B N     1 
ATOM   5322  C  CA    . VAL A  1  670 ? 37.283  13.152  33.049 1.00 34.64  ? 1469 VAL B CA    1 
ATOM   5323  C  C     . VAL A  1  670 ? 37.721  13.750  31.725 1.00 36.90  ? 1469 VAL B C     1 
ATOM   5324  O  O     . VAL A  1  670 ? 36.956  14.519  31.126 1.00 38.13  ? 1469 VAL B O     1 
ATOM   5325  C  CB    . VAL A  1  670 ? 38.001  13.815  34.209 1.00 32.48  ? 1469 VAL B CB    1 
ATOM   5326  C  CG1   . VAL A  1  670 ? 38.007  15.334  34.069 1.00 30.93  ? 1469 VAL B CG1   1 
ATOM   5327  C  CG2   . VAL A  1  670 ? 37.389  13.404  35.550 1.00 28.57  ? 1469 VAL B CG2   1 
ATOM   5328  N  N     . ARG A  1  671 ? 38.905  13.361  31.241 1.00 36.44  ? 1470 ARG B N     1 
ATOM   5329  C  CA    . ARG A  1  671 ? 39.385  13.874  29.972 1.00 35.25  ? 1470 ARG B CA    1 
ATOM   5330  C  C     . ARG A  1  671 ? 38.421  13.551  28.852 1.00 38.15  ? 1470 ARG B C     1 
ATOM   5331  O  O     . ARG A  1  671 ? 38.130  14.402  28.023 1.00 40.23  ? 1470 ARG B O     1 
ATOM   5332  C  CB    . ARG A  1  671 ? 40.749  13.306  29.614 1.00 36.66  ? 1470 ARG B CB    1 
ATOM   5333  C  CG    . ARG A  1  671 ? 41.896  13.705  30.530 1.00 39.31  ? 1470 ARG B CG    1 
ATOM   5334  C  CD    . ARG A  1  671 ? 43.238  13.367  29.879 1.00 42.62  ? 1470 ARG B CD    1 
ATOM   5335  N  NE    . ARG A  1  671 ? 44.304  13.489  30.875 1.00 42.00  ? 1470 ARG B NE    1 
ATOM   5336  C  CZ    . ARG A  1  671 ? 44.980  12.465  31.378 1.00 43.16  ? 1470 ARG B CZ    1 
ATOM   5337  N  NH1   . ARG A  1  671 ? 44.756  11.234  30.948 1.00 40.47  ? 1470 ARG B NH1   1 
ATOM   5338  N  NH2   . ARG A  1  671 ? 45.885  12.668  32.311 1.00 42.36  ? 1470 ARG B NH2   1 
ATOM   5339  N  N     . ASP A  1  672 ? 37.960  12.303  28.809 1.00 36.50  ? 1471 ASP B N     1 
ATOM   5340  C  CA    . ASP A  1  672 ? 37.069  11.864  27.738 1.00 36.70  ? 1471 ASP B CA    1 
ATOM   5341  C  C     . ASP A  1  672 ? 35.731  12.618  27.749 1.00 31.16  ? 1471 ASP B C     1 
ATOM   5342  O  O     . ASP A  1  672 ? 35.246  13.011  26.693 1.00 31.94  ? 1471 ASP B O     1 
ATOM   5343  C  CB    . ASP A  1  672 ? 36.772  10.348  27.829 1.00 37.26  ? 1471 ASP B CB    1 
ATOM   5344  C  CG    . ASP A  1  672 ? 37.995  9.480   27.557 1.00 41.22  ? 1471 ASP B CG    1 
ATOM   5345  O  OD1   . ASP A  1  672 ? 39.002  9.986   27.015 1.00 37.43  ? 1471 ASP B OD1   1 
ATOM   5346  O  OD2   . ASP A  1  672 ? 37.926  8.276   27.916 1.00 43.62  ? 1471 ASP B OD2   1 
ATOM   5347  N  N     . GLU A  1  673 ? 35.129  12.791  28.907 1.00 26.18  ? 1472 GLU B N     1 
ATOM   5348  C  CA    . GLU A  1  673 ? 33.843  13.465  28.984 1.00 33.64  ? 1472 GLU B CA    1 
ATOM   5349  C  C     . GLU A  1  673 ? 33.966  14.954  28.607 1.00 33.19  ? 1472 GLU B C     1 
ATOM   5350  O  O     . GLU A  1  673 ? 33.094  15.458  27.894 1.00 33.54  ? 1472 GLU B O     1 
ATOM   5351  C  CB    . GLU A  1  673 ? 33.185  13.234  30.336 1.00 32.78  ? 1472 GLU B CB    1 
ATOM   5352  C  CG    . GLU A  1  673 ? 32.845  11.782  30.560 1.00 33.03  ? 1472 GLU B CG    1 
ATOM   5353  C  CD    . GLU A  1  673 ? 32.152  11.497  31.865 1.00 37.91  ? 1472 GLU B CD    1 
ATOM   5354  O  OE1   . GLU A  1  673 ? 31.987  12.416  32.694 1.00 40.94  ? 1472 GLU B OE1   1 
ATOM   5355  O  OE2   . GLU A  1  673 ? 31.758  10.321  32.073 1.00 41.56  ? 1472 GLU B OE2   1 
ATOM   5356  N  N     . LEU A  1  674 ? 35.084  15.592  28.987 1.00 32.27  ? 1473 LEU B N     1 
ATOM   5357  C  CA    . LEU A  1  674 ? 35.362  16.985  28.619 1.00 33.57  ? 1473 LEU B CA    1 
ATOM   5358  C  C     . LEU A  1  674 ? 35.531  17.100  27.109 1.00 35.60  ? 1473 LEU B C     1 
ATOM   5359  O  O     . LEU A  1  674 ? 35.079  18.062  26.505 1.00 32.62  ? 1473 LEU B O     1 
ATOM   5360  C  CB    . LEU A  1  674 ? 36.640  17.491  29.315 1.00 34.26  ? 1473 LEU B CB    1 
ATOM   5361  C  CG    . LEU A  1  674 ? 36.540  18.062  30.716 1.00 39.48  ? 1473 LEU B CG    1 
ATOM   5362  C  CD1   . LEU A  1  674 ? 37.927  18.131  31.336 1.00 40.01  ? 1473 LEU B CD1   1 
ATOM   5363  C  CD2   . LEU A  1  674 ? 35.814  19.432  30.697 1.00 35.41  ? 1473 LEU B CD2   1 
ATOM   5364  N  N     . THR A  1  675 ? 36.192  16.109  26.508 1.00 34.08  ? 1474 THR B N     1 
ATOM   5365  C  CA    . THR A  1  675 ? 36.434  16.113  25.066 1.00 34.87  ? 1474 THR B CA    1 
ATOM   5366  C  C     . THR A  1  675 ? 35.109  15.938  24.332 1.00 38.36  ? 1474 THR B C     1 
ATOM   5367  O  O     . THR A  1  675 ? 34.856  16.542  23.367 1.00 39.72  ? 1474 THR B O     1 
ATOM   5368  C  CB    . THR A  1  675 ? 37.419  14.995  24.664 1.00 33.42  ? 1474 THR B CB    1 
ATOM   5369  O  OG1   . THR A  1  675 ? 38.687  15.210  25.305 1.00 34.12  ? 1474 THR B OG1   1 
ATOM   5370  C  CG2   . THR A  1  675 ? 37.626  15.016  23.173 1.00 28.28  ? 1474 THR B CG2   1 
ATOM   5371  N  N     A GLU A  1  676 ? 34.214  15.142  24.847 0.50 37.91  ? 1475 GLU B N     1 
ATOM   5372  N  N     B GLU A  1  676 ? 34.201  15.119  24.815 0.50 37.78  ? 1475 GLU B N     1 
ATOM   5373  C  CA    A GLU A  1  676 ? 32.962  15.027  24.172 0.50 36.06  ? 1475 GLU B CA    1 
ATOM   5374  C  CA    B GLU A  1  676 ? 32.927  15.044  24.134 0.50 35.98  ? 1475 GLU B CA    1 
ATOM   5375  C  C     A GLU A  1  676 ? 32.191  16.351  24.229 0.50 35.36  ? 1475 GLU B C     1 
ATOM   5376  C  C     B GLU A  1  676 ? 32.180  16.373  24.217 0.50 35.27  ? 1475 GLU B C     1 
ATOM   5377  O  O     A GLU A  1  676 ? 31.579  16.762  23.255 0.50 40.17  ? 1475 GLU B O     1 
ATOM   5378  O  O     B GLU A  1  676 ? 31.577  16.819  23.249 0.50 40.00  ? 1475 GLU B O     1 
ATOM   5379  C  CB    A GLU A  1  676 ? 32.235  13.924  24.857 0.50 35.98  ? 1475 GLU B CB    1 
ATOM   5380  C  CB    B GLU A  1  676 ? 32.116  13.965  24.773 0.50 36.01  ? 1475 GLU B CB    1 
ATOM   5381  C  CG    A GLU A  1  676 ? 31.069  13.361  24.088 0.50 38.40  ? 1475 GLU B CG    1 
ATOM   5382  C  CG    B GLU A  1  676 ? 32.761  12.594  24.791 0.50 38.85  ? 1475 GLU B CG    1 
ATOM   5383  C  CD    A GLU A  1  676 ? 29.765  14.093  24.366 0.50 41.87  ? 1475 GLU B CD    1 
ATOM   5384  C  CD    B GLU A  1  676 ? 31.944  11.550  25.561 0.50 43.49  ? 1475 GLU B CD    1 
ATOM   5385  O  OE1   A GLU A  1  676 ? 28.807  13.901  23.593 0.50 42.02  ? 1475 GLU B OE1   1 
ATOM   5386  O  OE1   B GLU A  1  676 ? 30.905  11.899  26.189 0.50 39.34  ? 1475 GLU B OE1   1 
ATOM   5387  O  OE2   A GLU A  1  676 ? 29.670  14.831  25.362 0.50 41.31  ? 1475 GLU B OE2   1 
ATOM   5388  O  OE2   B GLU A  1  676 ? 32.355  10.362  25.542 0.50 45.65  ? 1475 GLU B OE2   1 
ATOM   5389  N  N     . ILE A  1  677 ? 32.263  17.019  25.369 1.00 35.38  ? 1476 ILE B N     1 
ATOM   5390  C  CA    . ILE A  1  677 ? 31.601  18.304  25.557 1.00 36.88  ? 1476 ILE B CA    1 
ATOM   5391  C  C     . ILE A  1  677 ? 32.203  19.372  24.641 1.00 32.16  ? 1476 ILE B C     1 
ATOM   5392  O  O     . ILE A  1  677 ? 31.461  20.149  24.066 1.00 34.94  ? 1476 ILE B O     1 
ATOM   5393  C  CB    . ILE A  1  677 ? 31.628  18.744  27.044 1.00 36.58  ? 1476 ILE B CB    1 
ATOM   5394  C  CG1   . ILE A  1  677 ? 30.550  18.000  27.809 1.00 29.90  ? 1476 ILE B CG1   1 
ATOM   5395  C  CG2   . ILE A  1  677 ? 31.388  20.242  27.199 1.00 32.13  ? 1476 ILE B CG2   1 
ATOM   5396  C  CD1   . ILE A  1  677 ? 30.734  18.015  29.299 1.00 35.56  ? 1476 ILE B CD1   1 
ATOM   5397  N  N     . ARG A  1  678 ? 33.515  19.329  24.432 1.00 32.94  ? 1477 ARG B N     1 
ATOM   5398  C  CA    . ARG A  1  678 ? 34.205  20.247  23.552 1.00 30.37  ? 1477 ARG B CA    1 
ATOM   5399  C  C     . ARG A  1  678 ? 33.749  20.038  22.107 1.00 35.17  ? 1477 ARG B C     1 
ATOM   5400  O  O     . ARG A  1  678 ? 33.472  21.005  21.401 1.00 32.89  ? 1477 ARG B O     1 
ATOM   5401  C  CB    . ARG A  1  678 ? 35.705  20.040  23.660 1.00 29.81  ? 1477 ARG B CB    1 
ATOM   5402  C  CG    . ARG A  1  678 ? 36.546  21.072  22.914 1.00 34.07  ? 1477 ARG B CG    1 
ATOM   5403  C  CD    . ARG A  1  678 ? 37.968  20.565  22.684 1.00 34.97  ? 1477 ARG B CD    1 
ATOM   5404  N  NE    . ARG A  1  678 ? 37.943  19.438  21.758 1.00 40.23  ? 1477 ARG B NE    1 
ATOM   5405  C  CZ    . ARG A  1  678 ? 38.935  18.555  21.601 1.00 41.20  ? 1477 ARG B CZ    1 
ATOM   5406  N  NH1   . ARG A  1  678 ? 40.079  18.662  22.271 1.00 35.49  ? 1477 ARG B NH1   1 
ATOM   5407  N  NH2   . ARG A  1  678 ? 38.787  17.558  20.750 1.00 44.19  ? 1477 ARG B NH2   1 
ATOM   5408  N  N     . ASP A  1  679 ? 33.633  18.782  21.684 1.00 35.32  ? 1478 ASP B N     1 
ATOM   5409  C  CA    . ASP A  1  679 ? 33.177  18.472  20.326 1.00 36.46  ? 1478 ASP B CA    1 
ATOM   5410  C  C     . ASP A  1  679 ? 31.676  18.787  20.163 1.00 38.15  ? 1478 ASP B C     1 
ATOM   5411  O  O     . ASP A  1  679 ? 31.243  19.146  19.107 1.00 35.37  ? 1478 ASP B O     1 
ATOM   5412  C  CB    . ASP A  1  679 ? 33.460  16.992  19.983 1.00 41.47  ? 1478 ASP B CB    1 
ATOM   5413  C  CG    . ASP A  1  679 ? 34.970  16.656  19.948 1.00 44.77  ? 1478 ASP B CG    1 
ATOM   5414  O  OD1   . ASP A  1  679 ? 35.831  17.560  19.775 1.00 41.97  ? 1478 ASP B OD1   1 
ATOM   5415  O  OD2   . ASP A  1  679 ? 35.308  15.458  20.110 1.00 45.09  ? 1478 ASP B OD2   1 
ATOM   5416  N  N     A ARG A  1  680 ? 30.902  18.731  21.219 0.50 36.38  ? 1479 ARG B N     1 
ATOM   5417  N  N     B ARG A  1  680 ? 30.847  18.636  21.198 0.50 37.88  ? 1479 ARG B N     1 
ATOM   5418  C  CA    A ARG A  1  680 ? 29.525  19.015  21.015 0.50 37.81  ? 1479 ARG B CA    1 
ATOM   5419  C  CA    B ARG A  1  680 ? 29.424  18.981  21.062 0.50 39.90  ? 1479 ARG B CA    1 
ATOM   5420  C  C     A ARG A  1  680 ? 29.129  20.510  21.086 0.50 39.85  ? 1479 ARG B C     1 
ATOM   5421  C  C     B ARG A  1  680 ? 29.121  20.497  21.024 0.50 41.14  ? 1479 ARG B C     1 
ATOM   5422  O  O     A ARG A  1  680 ? 28.199  20.935  20.443 0.50 45.94  ? 1479 ARG B O     1 
ATOM   5423  O  O     B ARG A  1  680 ? 28.266  20.908  20.200 0.50 46.41  ? 1479 ARG B O     1 
ATOM   5424  C  CB    A ARG A  1  680 ? 28.729  18.165  21.943 0.50 34.03  ? 1479 ARG B CB    1 
ATOM   5425  C  CB    B ARG A  1  680 ? 28.589  18.272  22.108 0.50 38.64  ? 1479 ARG B CB    1 
ATOM   5426  C  CG    A ARG A  1  680 ? 27.253  18.363  21.781 0.50 39.40  ? 1479 ARG B CG    1 
ATOM   5427  C  CG    B ARG A  1  680 ? 27.083  18.378  21.879 0.50 47.76  ? 1479 ARG B CG    1 
ATOM   5428  C  CD    A ARG A  1  680 ? 26.483  17.190  22.423 0.50 45.00  ? 1479 ARG B CD    1 
ATOM   5429  C  CD    B ARG A  1  680 ? 26.338  17.286  22.669 0.50 55.34  ? 1479 ARG B CD    1 
ATOM   5430  N  NE    A ARG A  1  680 ? 26.319  17.295  23.884 0.50 39.83  ? 1479 ARG B NE    1 
ATOM   5431  N  NE    B ARG A  1  680 ? 25.070  17.665  23.324 0.50 49.93  ? 1479 ARG B NE    1 
ATOM   5432  C  CZ    A ARG A  1  680 ? 26.887  16.475  24.754 0.50 35.06  ? 1479 ARG B CZ    1 
ATOM   5433  C  CZ    B ARG A  1  680 ? 23.992  18.157  22.711 0.50 48.60  ? 1479 ARG B CZ    1 
ATOM   5434  N  NH1   A ARG A  1  680 ? 26.708  16.635  26.022 0.50 34.37  ? 1479 ARG B NH1   1 
ATOM   5435  N  NH1   B ARG A  1  680 ? 22.917  18.414  23.423 0.50 47.69  ? 1479 ARG B NH1   1 
ATOM   5436  N  NH2   A ARG A  1  680 ? 27.643  15.486  24.349 0.50 37.60  ? 1479 ARG B NH2   1 
ATOM   5437  N  NH2   B ARG A  1  680 ? 23.983  18.421  21.416 0.50 47.15  ? 1479 ARG B NH2   1 
ATOM   5438  N  N     . PHE A  1  681 ? 29.829  21.295  21.864 1.00 38.69  ? 1480 PHE B N     1 
ATOM   5439  C  CA    . PHE A  1  681 ? 29.451  22.690  22.214 1.00 37.06  ? 1480 PHE B CA    1 
ATOM   5440  C  C     . PHE A  1  681 ? 30.561  23.696  21.864 1.00 37.03  ? 1480 PHE B C     1 
ATOM   5441  O  O     . PHE A  1  681 ? 30.309  24.884  21.839 1.00 40.52  ? 1480 PHE B O     1 
ATOM   5442  C  CB    . PHE A  1  681 ? 29.159  22.722  23.726 1.00 34.17  ? 1480 PHE B CB    1 
ATOM   5443  C  CG    . PHE A  1  681 ? 27.901  22.010  24.102 1.00 36.18  ? 1480 PHE B CG    1 
ATOM   5444  C  CD1   . PHE A  1  681 ? 26.673  22.628  23.860 1.00 36.59  ? 1480 PHE B CD1   1 
ATOM   5445  C  CD2   . PHE A  1  681 ? 27.917  20.728  24.665 1.00 34.33  ? 1480 PHE B CD2   1 
ATOM   5446  C  CE1   . PHE A  1  681 ? 25.473  22.002  24.181 1.00 36.30  ? 1480 PHE B CE1   1 
ATOM   5447  C  CE2   . PHE A  1  681 ? 26.729  20.091  24.982 1.00 41.13  ? 1480 PHE B CE2   1 
ATOM   5448  C  CZ    . PHE A  1  681 ? 25.502  20.732  24.752 1.00 39.84  ? 1480 PHE B CZ    1 
ATOM   5449  N  N     . GLY A  1  682 ? 31.766  23.189  21.591 1.00 31.59  ? 1481 GLY B N     1 
ATOM   5450  C  CA    . GLY A  1  682 ? 32.913  24.013  21.222 1.00 30.47  ? 1481 GLY B CA    1 
ATOM   5451  C  C     . GLY A  1  682 ? 32.646  24.749  19.928 1.00 36.37  ? 1481 GLY B C     1 
ATOM   5452  O  O     . GLY A  1  682 ? 32.128  24.200  18.942 1.00 35.99  ? 1481 GLY B O     1 
ATOM   5453  N  N     . ASP A  1  683 ? 32.979  26.025  19.923 1.00 34.05  ? 1482 ASP B N     1 
ATOM   5454  C  CA    . ASP A  1  683 ? 32.712  26.823  18.747 1.00 33.77  ? 1482 ASP B CA    1 
ATOM   5455  C  C     . ASP A  1  683 ? 33.901  27.714  18.401 1.00 34.37  ? 1482 ASP B C     1 
ATOM   5456  O  O     . ASP A  1  683 ? 34.864  27.764  19.123 1.00 35.39  ? 1482 ASP B O     1 
ATOM   5457  C  CB    . ASP A  1  683 ? 31.413  27.640  18.916 1.00 34.02  ? 1482 ASP B CB    1 
ATOM   5458  C  CG    . ASP A  1  683 ? 31.505  28.703  19.991 1.00 38.18  ? 1482 ASP B CG    1 
ATOM   5459  O  OD1   . ASP A  1  683 ? 32.541  28.816  20.690 1.00 37.27  ? 1482 ASP B OD1   1 
ATOM   5460  O  OD2   . ASP A  1  683 ? 30.515  29.457  20.150 1.00 42.73  ? 1482 ASP B OD2   1 
ATOM   5461  N  N     . ASP A  1  684 ? 33.805  28.408  17.284 1.00 34.96  ? 1483 ASP B N     1 
ATOM   5462  C  CA    . ASP A  1  684 ? 34.883  29.269  16.809 1.00 38.22  ? 1483 ASP B CA    1 
ATOM   5463  C  C     . ASP A  1  684 ? 35.065  30.531  17.636 1.00 38.49  ? 1483 ASP B C     1 
ATOM   5464  O  O     . ASP A  1  684 ? 34.101  31.101  18.173 1.00 34.55  ? 1483 ASP B O     1 
ATOM   5465  C  CB    . ASP A  1  684 ? 34.574  29.721  15.367 1.00 41.40  ? 1483 ASP B CB    1 
ATOM   5466  C  CG    . ASP A  1  684 ? 34.699  28.629  14.367 1.00 45.58  ? 1483 ASP B CG    1 
ATOM   5467  O  OD1   . ASP A  1  684 ? 35.371  27.611  14.652 1.00 49.74  ? 1483 ASP B OD1   1 
ATOM   5468  O  OD2   . ASP A  1  684 ? 34.111  28.793  13.281 1.00 46.05  ? 1483 ASP B OD2   1 
ATOM   5469  N  N     . ARG A  1  685 ? 36.304  30.994  17.677 1.00 33.52  ? 1484 ARG B N     1 
ATOM   5470  C  CA    . ARG A  1  685 ? 36.662  32.192  18.336 1.00 30.14  ? 1484 ARG B CA    1 
ATOM   5471  C  C     . ARG A  1  685 ? 36.019  33.371  17.623 1.00 30.26  ? 1484 ARG B C     1 
ATOM   5472  O  O     . ARG A  1  685 ? 36.007  33.441  16.429 1.00 36.37  ? 1484 ARG B O     1 
ATOM   5473  C  CB    . ARG A  1  685 ? 38.190  32.296  18.348 1.00 26.55  ? 1484 ARG B CB    1 
ATOM   5474  C  CG    . ARG A  1  685 ? 38.682  33.698  18.455 1.00 25.96  ? 1484 ARG B CG    1 
ATOM   5475  C  CD    . ARG A  1  685 ? 40.172  33.751  18.806 1.00 25.67  ? 1484 ARG B CD    1 
ATOM   5476  N  NE    . ARG A  1  685 ? 40.438  33.383  20.190 1.00 28.12  ? 1484 ARG B NE    1 
ATOM   5477  C  CZ    . ARG A  1  685 ? 40.273  34.162  21.270 1.00 30.98  ? 1484 ARG B CZ    1 
ATOM   5478  N  NH1   . ARG A  1  685 ? 39.878  35.457  21.205 1.00 32.41  ? 1484 ARG B NH1   1 
ATOM   5479  N  NH2   . ARG A  1  685 ? 40.573  33.669  22.438 1.00 26.62  ? 1484 ARG B NH2   1 
ATOM   5480  N  N     . ARG A  1  686 ? 35.507  34.317  18.377 1.00 34.41  ? 1485 ARG B N     1 
ATOM   5481  C  CA    . ARG A  1  686 ? 34.869  35.522  17.824 1.00 34.50  ? 1485 ARG B CA    1 
ATOM   5482  C  C     . ARG A  1  686 ? 35.741  36.770  17.925 1.00 35.00  ? 1485 ARG B C     1 
ATOM   5483  O  O     . ARG A  1  686 ? 35.825  37.537  16.970 1.00 36.54  ? 1485 ARG B O     1 
ATOM   5484  C  CB    . ARG A  1  686 ? 33.550  35.783  18.537 1.00 36.63  ? 1485 ARG B CB    1 
ATOM   5485  C  CG    . ARG A  1  686 ? 32.567  34.629  18.462 1.00 33.94  ? 1485 ARG B CG    1 
ATOM   5486  C  CD    . ARG A  1  686 ? 31.306  34.945  19.221 1.00 33.38  ? 1485 ARG B CD    1 
ATOM   5487  N  NE    . ARG A  1  686 ? 30.365  33.821  19.172 1.00 35.82  ? 1485 ARG B NE    1 
ATOM   5488  C  CZ    . ARG A  1  686 ? 29.171  33.821  19.734 1.00 33.16  ? 1485 ARG B CZ    1 
ATOM   5489  N  NH1   . ARG A  1  686 ? 28.752  34.891  20.368 1.00 33.59  ? 1485 ARG B NH1   1 
ATOM   5490  N  NH2   . ARG A  1  686 ? 28.389  32.761  19.651 1.00 27.42  ? 1485 ARG B NH2   1 
ATOM   5491  N  N     . THR A  1  687 ? 36.387  36.971  19.068 1.00 31.51  ? 1486 THR B N     1 
ATOM   5492  C  CA    . THR A  1  687 ? 37.160  38.172  19.284 1.00 29.12  ? 1486 THR B CA    1 
ATOM   5493  C  C     . THR A  1  687 ? 38.553  37.980  18.686 1.00 31.29  ? 1486 THR B C     1 
ATOM   5494  O  O     . THR A  1  687 ? 39.230  36.957  18.944 1.00 30.56  ? 1486 THR B O     1 
ATOM   5495  C  CB    . THR A  1  687 ? 37.311  38.399  20.787 1.00 29.60  ? 1486 THR B CB    1 
ATOM   5496  O  OG1   . THR A  1  687 ? 36.030  38.633  21.352 1.00 31.88  ? 1486 THR B OG1   1 
ATOM   5497  C  CG2   . THR A  1  687 ? 38.238  39.561  21.056 1.00 25.37  ? 1486 THR B CG2   1 
ATOM   5498  N  N     . GLU A  1  688 ? 39.007  38.919  17.870 1.00 32.33  ? 1487 GLU B N     1 
ATOM   5499  C  CA    . GLU A  1  688 ? 40.328  38.766  17.264 1.00 33.08  ? 1487 GLU B CA    1 
ATOM   5500  C  C     . GLU A  1  688 ? 41.368  39.464  18.133 1.00 34.32  ? 1487 GLU B C     1 
ATOM   5501  O  O     . GLU A  1  688 ? 41.208  40.634  18.474 1.00 32.28  ? 1487 GLU B O     1 
ATOM   5502  C  CB    . GLU A  1  688 ? 40.375  39.316  15.855 1.00 31.34  ? 1487 GLU B CB    1 
ATOM   5503  C  CG    . GLU A  1  688 ? 41.780  39.259  15.235 1.00 37.50  ? 1487 GLU B CG    1 
ATOM   5504  C  CD    . GLU A  1  688 ? 41.880  39.983  13.883 1.00 42.80  ? 1487 GLU B CD    1 
ATOM   5505  O  OE1   . GLU A  1  688 ? 40.845  40.351  13.272 1.00 40.54  ? 1487 GLU B OE1   1 
ATOM   5506  O  OE2   . GLU A  1  688 ? 43.016  40.219  13.425 1.00 43.51  ? 1487 GLU B OE2   1 
ATOM   5507  N  N     . ILE A  1  689 ? 42.462  38.778  18.417 1.00 32.83  ? 1488 ILE B N     1 
ATOM   5508  C  CA    . ILE A  1  689 ? 43.527  39.382  19.155 1.00 34.85  ? 1488 ILE B CA    1 
ATOM   5509  C  C     . ILE A  1  689 ? 44.580  39.859  18.171 1.00 37.10  ? 1488 ILE B C     1 
ATOM   5510  O  O     . ILE A  1  689 ? 45.232  39.050  17.524 1.00 37.20  ? 1488 ILE B O     1 
ATOM   5511  C  CB    . ILE A  1  689 ? 44.083  38.376  20.155 1.00 35.32  ? 1488 ILE B CB    1 
ATOM   5512  C  CG1   . ILE A  1  689 ? 43.011  38.110  21.201 1.00 38.66  ? 1488 ILE B CG1   1 
ATOM   5513  C  CG2   . ILE A  1  689 ? 45.378  38.867  20.821 1.00 33.40  ? 1488 ILE B CG2   1 
ATOM   5514  C  CD1   . ILE A  1  689 ? 43.073  36.725  21.782 1.00 34.47  ? 1488 ILE B CD1   1 
ATOM   5515  N  N     . GLN A  1  690 ? 44.741  41.160  18.050 1.00 35.95  ? 1489 GLN B N     1 
ATOM   5516  C  CA    . GLN A  1  690 ? 45.754  41.691  17.119 1.00 43.33  ? 1489 GLN B CA    1 
ATOM   5517  C  C     . GLN A  1  690 ? 47.041  42.045  17.821 1.00 42.37  ? 1489 GLN B C     1 
ATOM   5518  O  O     . GLN A  1  690 ? 46.992  42.746  18.808 1.00 42.91  ? 1489 GLN B O     1 
ATOM   5519  C  CB    . GLN A  1  690 ? 45.260  42.938  16.368 1.00 37.14  ? 1489 GLN B CB    1 
ATOM   5520  C  CG    . GLN A  1  690 ? 44.093  42.657  15.438 1.00 48.11  ? 1489 GLN B CG    1 
ATOM   5521  C  CD    . GLN A  1  690 ? 43.949  43.675  14.333 1.00 44.46  ? 1489 GLN B CD    1 
ATOM   5522  O  OE1   . GLN A  1  690 ? 44.391  44.819  14.446 1.00 40.44  ? 1489 GLN B OE1   1 
ATOM   5523  N  NE2   . GLN A  1  690 ? 43.286  43.268  13.278 1.00 39.89  ? 1489 GLN B NE2   1 
ATOM   5524  N  N     . LEU A  1  691 ? 48.165  41.646  17.252 1.00 54.25  ? 1490 LEU B N     1 
ATOM   5525  C  CA    . LEU A  1  691 ? 49.481  42.064  17.730 1.00 62.22  ? 1490 LEU B CA    1 
ATOM   5526  C  C     . LEU A  1  691 ? 49.910  43.201  16.850 1.00 64.62  ? 1490 LEU B C     1 
ATOM   5527  O  O     . LEU A  1  691 ? 49.934  43.052  15.636 1.00 76.16  ? 1490 LEU B O     1 
ATOM   5528  C  CB    . LEU A  1  691 ? 50.463  40.916  17.587 1.00 69.17  ? 1490 LEU B CB    1 
ATOM   5529  C  CG    . LEU A  1  691 ? 49.966  39.485  17.852 1.00 79.26  ? 1490 LEU B CG    1 
ATOM   5530  C  CD1   . LEU A  1  691 ? 50.774  38.450  17.077 1.00 79.16  ? 1490 LEU B CD1   1 
ATOM   5531  C  CD2   . LEU A  1  691 ? 50.008  39.143  19.336 1.00 81.38  ? 1490 LEU B CD2   1 
ATOM   5532  N  N     . GLY A  1  692 ? 50.202  44.357  17.418 1.00 79.01  ? 1491 GLY B N     1 
ATOM   5533  C  CA    . GLY A  1  692 ? 50.114  44.611  18.845 1.00 80.94  ? 1491 GLY B CA    1 
ATOM   5534  C  C     . GLY A  1  692 ? 50.434  46.066  19.105 1.00 83.61  ? 1491 GLY B C     1 
ATOM   5535  O  O     . GLY A  1  692 ? 49.805  46.656  19.982 1.00 86.58  ? 1491 GLY B O     1 
ATOM   5536  O  OXT   . GLY A  1  692 ? 51.306  46.672  18.449 1.00 72.12  ? 1491 GLY B OXT   1 
ATOM   5537  N  N     . GLY B  1  8   ? 10.220  61.560  23.399 1.00 75.15  ? 416  GLY D N     1 
ATOM   5538  C  CA    . GLY B  1  8   ? 11.466  60.953  23.921 1.00 66.77  ? 416  GLY D CA    1 
ATOM   5539  C  C     . GLY B  1  8   ? 11.370  59.443  24.013 1.00 76.74  ? 416  GLY D C     1 
ATOM   5540  O  O     . GLY B  1  8   ? 12.400  58.753  24.090 1.00 78.76  ? 416  GLY D O     1 
ATOM   5541  N  N     . LYS B  1  9   ? 10.142  58.920  23.999 1.00 77.16  ? 417  LYS D N     1 
ATOM   5542  C  CA    . LYS B  1  9   ? 9.911   57.484  23.932 1.00 68.69  ? 417  LYS D CA    1 
ATOM   5543  C  C     . LYS B  1  9   ? 9.946   56.964  22.476 1.00 64.13  ? 417  LYS D C     1 
ATOM   5544  O  O     . LYS B  1  9   ? 10.075  55.763  22.231 1.00 61.20  ? 417  LYS D O     1 
ATOM   5545  C  CB    . LYS B  1  9   ? 8.594   57.123  24.616 1.00 62.38  ? 417  LYS D CB    1 
ATOM   5546  N  N     . LEU B  1  10  ? 9.868   57.893  21.529 1.00 57.72  ? 418  LEU D N     1 
ATOM   5547  C  CA    . LEU B  1  10  ? 9.853   57.624  20.111 1.00 53.88  ? 418  LEU D CA    1 
ATOM   5548  C  C     . LEU B  1  10  ? 11.200  57.140  19.581 1.00 54.65  ? 418  LEU D C     1 
ATOM   5549  O  O     . LEU B  1  10  ? 12.227  57.743  19.842 1.00 58.39  ? 418  LEU D O     1 
ATOM   5550  C  CB    . LEU B  1  10  ? 9.396   58.863  19.331 1.00 51.34  ? 418  LEU D CB    1 
ATOM   5551  C  CG    . LEU B  1  10  ? 9.533   58.801  17.805 1.00 53.63  ? 418  LEU D CG    1 
ATOM   5552  C  CD1   . LEU B  1  10  ? 8.292   58.190  17.194 1.00 54.70  ? 418  LEU D CD1   1 
ATOM   5553  C  CD2   . LEU B  1  10  ? 9.807   60.180  17.259 1.00 51.40  ? 418  LEU D CD2   1 
ATOM   5554  N  N     . ALA B  1  11  ? 11.170  56.053  18.819 1.00 51.31  ? 419  ALA D N     1 
ATOM   5555  C  CA    . ALA B  1  11  ? 12.341  55.562  18.149 1.00 47.04  ? 419  ALA D CA    1 
ATOM   5556  C  C     . ALA B  1  11  ? 12.118  55.791  16.698 1.00 53.04  ? 419  ALA D C     1 
ATOM   5557  O  O     . ALA B  1  11  ? 11.537  54.930  16.054 1.00 53.32  ? 419  ALA D O     1 
ATOM   5558  C  CB    . ALA B  1  11  ? 12.486  54.080  18.385 1.00 43.53  ? 419  ALA D CB    1 
ATOM   5559  N  N     . ASP B  1  12  ? 12.652  56.880  16.152 1.00 54.99  ? 420  ASP D N     1 
ATOM   5560  C  CA    . ASP B  1  12  ? 12.399  57.249  14.774 1.00 54.85  ? 420  ASP D CA    1 
ATOM   5561  C  C     . ASP B  1  12  ? 13.158  56.432  13.754 1.00 52.91  ? 420  ASP D C     1 
ATOM   5562  O  O     . ASP B  1  12  ? 14.123  55.798  14.074 1.00 54.30  ? 420  ASP D O     1 
ATOM   5563  C  CB    . ASP B  1  12  ? 12.736  58.710  14.587 1.00 56.40  ? 420  ASP D CB    1 
ATOM   5564  C  CG    . ASP B  1  12  ? 11.743  59.416  13.711 1.00 55.44  ? 420  ASP D CG    1 
ATOM   5565  O  OD1   . ASP B  1  12  ? 10.833  58.818  13.132 1.00 60.17  ? 420  ASP D OD1   1 
ATOM   5566  O  OD2   . ASP B  1  12  ? 11.857  60.623  13.617 1.00 68.26  ? 420  ASP D OD2   1 
ATOM   5567  N  N     . CYS B  1  13  ? 12.741  56.533  12.501 1.00 57.03  ? 421  CYS D N     1 
ATOM   5568  C  CA    . CYS B  1  13  ? 13.438  55.960  11.360 1.00 57.65  ? 421  CYS D CA    1 
ATOM   5569  C  C     . CYS B  1  13  ? 14.360  57.037  10.774 1.00 62.79  ? 421  CYS D C     1 
ATOM   5570  O  O     . CYS B  1  13  ? 14.067  58.233  10.902 1.00 70.70  ? 421  CYS D O     1 
ATOM   5571  C  CB    . CYS B  1  13  ? 12.428  55.524  10.318 1.00 53.45  ? 421  CYS D CB    1 
ATOM   5572  S  SG    . CYS B  1  13  ? 11.366  56.887  9.791  1.00 55.84  ? 421  CYS D SG    1 
ATOM   5573  N  N     . SER B  1  14  ? 15.475  56.626  10.166 1.00 64.94  ? 422  SER D N     1 
ATOM   5574  C  CA    . SER B  1  14  ? 16.447  57.587  9.579  1.00 66.88  ? 422  SER D CA    1 
ATOM   5575  C  C     . SER B  1  14  ? 15.957  58.393  8.362  1.00 67.33  ? 422  SER D C     1 
ATOM   5576  O  O     . SER B  1  14  ? 16.270  59.577  8.232  1.00 76.75  ? 422  SER D O     1 
ATOM   5577  C  CB    . SER B  1  14  ? 17.777  56.928  9.243  1.00 57.26  ? 422  SER D CB    1 
ATOM   5578  O  OG    . SER B  1  14  ? 17.563  55.854  8.349  1.00 66.88  ? 422  SER D OG    1 
ATOM   5579  N  N     . SER B  1  15  ? 15.186  57.773  7.482  1.00 69.10  ? 423  SER D N     1 
ATOM   5580  C  CA    . SER B  1  15  ? 14.674  58.486  6.327  1.00 69.87  ? 423  SER D CA    1 
ATOM   5581  C  C     . SER B  1  15  ? 13.889  59.715  6.764  1.00 76.76  ? 423  SER D C     1 
ATOM   5582  O  O     . SER B  1  15  ? 13.197  59.684  7.790  1.00 85.64  ? 423  SER D O     1 
ATOM   5583  C  CB    . SER B  1  15  ? 13.797  57.571  5.487  1.00 69.37  ? 423  SER D CB    1 
ATOM   5584  O  OG    . SER B  1  15  ? 13.077  58.303  4.517  1.00 64.60  ? 423  SER D OG    1 
ATOM   5585  N  N     . LYS B  1  16  ? 14.010  60.793  5.997  1.00 79.01  ? 424  LYS D N     1 
ATOM   5586  C  CA    . LYS B  1  16  ? 13.268  62.012  6.288  1.00 78.23  ? 424  LYS D CA    1 
ATOM   5587  C  C     . LYS B  1  16  ? 12.209  62.281  5.229  1.00 73.38  ? 424  LYS D C     1 
ATOM   5588  O  O     . LYS B  1  16  ? 11.636  63.359  5.164  1.00 74.11  ? 424  LYS D O     1 
ATOM   5589  C  CB    . LYS B  1  16  ? 14.217  63.192  6.500  1.00 75.54  ? 424  LYS D CB    1 
ATOM   5590  C  CG    . LYS B  1  16  ? 14.732  63.307  7.926  1.00 76.33  ? 424  LYS D CG    1 
ATOM   5591  C  CD    . LYS B  1  16  ? 13.569  63.467  8.915  1.00 83.46  ? 424  LYS D CD    1 
ATOM   5592  C  CE    . LYS B  1  16  ? 13.976  63.190  10.360 1.00 82.65  ? 424  LYS D CE    1 
ATOM   5593  N  NZ    . LYS B  1  16  ? 14.394  61.769  10.577 1.00 76.42  ? 424  LYS D NZ    1 
ATOM   5594  N  N     . SER B  1  17  ? 11.938  61.266  4.416  1.00 70.69  ? 425  SER D N     1 
ATOM   5595  C  CA    . SER B  1  17  ? 10.939  61.353  3.364  1.00 63.34  ? 425  SER D CA    1 
ATOM   5596  C  C     . SER B  1  17  ? 9.611   60.697  3.788  1.00 60.59  ? 425  SER D C     1 
ATOM   5597  O  O     . SER B  1  17  ? 9.483   59.446  3.725  1.00 58.65  ? 425  SER D O     1 
ATOM   5598  C  CB    . SER B  1  17  ? 11.487  60.690  2.102  1.00 61.87  ? 425  SER D CB    1 
ATOM   5599  O  OG    . SER B  1  17  ? 10.460  60.502  1.136  1.00 71.99  ? 425  SER D OG    1 
ATOM   5600  N  N     . PRO B  1  18  ? 8.602   61.511  4.219  1.00 57.43  ? 426  PRO D N     1 
ATOM   5601  C  CA    . PRO B  1  18  ? 7.395   60.808  4.701  1.00 57.57  ? 426  PRO D CA    1 
ATOM   5602  C  C     . PRO B  1  18  ? 6.723   59.974  3.718  1.00 64.23  ? 426  PRO D C     1 
ATOM   5603  O  O     . PRO B  1  18  ? 5.936   59.136  3.945  1.00 72.32  ? 426  PRO D O     1 
ATOM   5604  C  CB    . PRO B  1  18  ? 6.420   61.935  4.932  1.00 54.83  ? 426  PRO D CB    1 
ATOM   5605  C  CG    . PRO B  1  18  ? 7.286   63.040  5.420  1.00 56.20  ? 426  PRO D CG    1 
ATOM   5606  C  CD    . PRO B  1  18  ? 8.443   62.970  4.440  1.00 57.37  ? 426  PRO D CD    1 
ATOM   5607  N  N     A GLU B  1  19  ? 6.969   60.199  2.506  0.50 64.95  ? 427  GLU D N     1 
ATOM   5608  N  N     B GLU B  1  19  ? 6.918   60.199  2.479  0.50 67.78  ? 427  GLU D N     1 
ATOM   5609  C  CA    A GLU B  1  19  ? 6.180   59.339  1.753  0.50 60.40  ? 427  GLU D CA    1 
ATOM   5610  C  CA    B GLU B  1  19  ? 6.085   59.246  1.848  0.50 64.29  ? 427  GLU D CA    1 
ATOM   5611  C  C     A GLU B  1  19  ? 6.461   57.793  1.941  0.50 57.86  ? 427  GLU D C     1 
ATOM   5612  C  C     B GLU B  1  19  ? 6.422   57.737  2.047  0.50 60.11  ? 427  GLU D C     1 
ATOM   5613  O  O     A GLU B  1  19  ? 5.567   57.002  1.736  0.50 55.21  ? 427  GLU D O     1 
ATOM   5614  O  O     B GLU B  1  19  ? 5.543   56.913  1.938  0.50 57.82  ? 427  GLU D O     1 
ATOM   5615  C  CB    A GLU B  1  19  ? 6.503   59.761  0.411  0.50 59.56  ? 427  GLU D CB    1 
ATOM   5616  C  CB    B GLU B  1  19  ? 5.941   59.530  0.442  0.50 67.79  ? 427  GLU D CB    1 
ATOM   5617  C  CG    A GLU B  1  19  ? 6.067   61.203  0.223  0.50 53.50  ? 427  GLU D CG    1 
ATOM   5618  C  CG    B GLU B  1  19  ? 5.436   58.322  -0.296 0.50 63.21  ? 427  GLU D CG    1 
ATOM   5619  C  CD    A GLU B  1  19  ? 6.927   62.208  0.950  0.50 51.67  ? 427  GLU D CD    1 
ATOM   5620  C  CD    B GLU B  1  19  ? 5.288   58.644  -1.745 0.50 62.54  ? 427  GLU D CD    1 
ATOM   5621  O  OE1   A GLU B  1  19  ? 8.151   61.999  1.049  0.50 54.84  ? 427  GLU D OE1   1 
ATOM   5622  O  OE1   B GLU B  1  19  ? 5.459   59.840  -2.068 0.50 66.40  ? 427  GLU D OE1   1 
ATOM   5623  O  OE2   A GLU B  1  19  ? 6.376   63.236  1.385  0.50 49.32  ? 427  GLU D OE2   1 
ATOM   5624  O  OE2   B GLU B  1  19  ? 5.016   57.720  -2.536 0.50 62.86  ? 427  GLU D OE2   1 
ATOM   5625  N  N     . GLU B  1  20  ? 7.672   57.386  2.319  1.00 54.20  ? 428  GLU D N     1 
ATOM   5626  C  CA    . GLU B  1  20  ? 8.060   55.968  2.472  1.00 58.63  ? 428  GLU D CA    1 
ATOM   5627  C  C     . GLU B  1  20  ? 8.197   55.531  3.963  1.00 56.62  ? 428  GLU D C     1 
ATOM   5628  O  O     . GLU B  1  20  ? 8.574   54.410  4.264  1.00 46.58  ? 428  GLU D O     1 
ATOM   5629  C  CB    . GLU B  1  20  ? 9.392   55.802  1.763  1.00 54.04  ? 428  GLU D CB    1 
ATOM   5630  C  CG    . GLU B  1  20  ? 10.521  56.645  2.348  1.00 56.45  ? 428  GLU D CG    1 
ATOM   5631  C  CD    . GLU B  1  20  ? 11.878  56.373  1.709  1.00 60.39  ? 428  GLU D CD    1 
ATOM   5632  O  OE1   . GLU B  1  20  ? 12.053  55.322  1.061  1.00 58.35  ? 428  GLU D OE1   1 
ATOM   5633  O  OE2   . GLU B  1  20  ? 12.780  57.214  1.863  1.00 63.14  ? 428  GLU D OE2   1 
ATOM   5634  N  N     . CYS B  1  21  ? 7.900   56.454  4.869  1.00 58.10  ? 429  CYS D N     1 
ATOM   5635  C  CA    . CYS B  1  21  ? 8.018   56.230  6.300  1.00 57.88  ? 429  CYS D CA    1 
ATOM   5636  C  C     . CYS B  1  21  ? 6.753   55.714  6.978  1.00 60.46  ? 429  CYS D C     1 
ATOM   5637  O  O     . CYS B  1  21  ? 5.636   56.102  6.650  1.00 61.96  ? 429  CYS D O     1 
ATOM   5638  C  CB    . CYS B  1  21  ? 8.500   57.496  6.967  1.00 61.30  ? 429  CYS D CB    1 
ATOM   5639  S  SG    . CYS B  1  21  ? 10.221  57.864  6.591  1.00 68.17  ? 429  CYS D SG    1 
ATOM   5640  N  N     . GLU B  1  22  ? 6.941   54.813  7.934  1.00 59.41  ? 430  GLU D N     1 
ATOM   5641  C  CA    . GLU B  1  22  ? 5.825   54.224  8.687  1.00 55.56  ? 430  GLU D CA    1 
ATOM   5642  C  C     . GLU B  1  22  ? 6.094   54.317  10.174 1.00 55.52  ? 430  GLU D C     1 
ATOM   5643  O  O     . GLU B  1  22  ? 7.214   54.035  10.624 1.00 52.89  ? 430  GLU D O     1 
ATOM   5644  C  CB    . GLU B  1  22  ? 5.649   52.763  8.311  1.00 53.79  ? 430  GLU D CB    1 
ATOM   5645  C  CG    . GLU B  1  22  ? 5.662   52.518  6.806  1.00 58.67  ? 430  GLU D CG    1 
ATOM   5646  C  CD    . GLU B  1  22  ? 5.713   51.040  6.439  1.00 64.93  ? 430  GLU D CD    1 
ATOM   5647  O  OE1   . GLU B  1  22  ? 5.435   50.712  5.266  1.00 68.27  ? 430  GLU D OE1   1 
ATOM   5648  O  OE2   . GLU B  1  22  ? 6.018   50.197  7.306  1.00 56.80  ? 430  GLU D OE2   1 
ATOM   5649  N  N     . ILE B  1  23  ? 5.078   54.706  10.935 1.00 50.38  ? 431  ILE D N     1 
ATOM   5650  C  CA    . ILE B  1  23  ? 5.205   54.782  12.395 1.00 46.20  ? 431  ILE D CA    1 
ATOM   5651  C  C     . ILE B  1  23  ? 4.290   53.722  13.019 1.00 51.13  ? 431  ILE D C     1 
ATOM   5652  O  O     . ILE B  1  23  ? 3.096   53.663  12.738 1.00 46.66  ? 431  ILE D O     1 
ATOM   5653  C  CB    . ILE B  1  23  ? 4.902   56.182  12.924 1.00 43.21  ? 431  ILE D CB    1 
ATOM   5654  C  CG1   . ILE B  1  23  ? 5.042   56.205  14.434 1.00 41.69  ? 431  ILE D CG1   1 
ATOM   5655  C  CG2   . ILE B  1  23  ? 3.508   56.632  12.490 1.00 49.21  ? 431  ILE D CG2   1 
ATOM   5656  C  CD1   . ILE B  1  23  ? 5.057   57.593  15.043 1.00 38.47  ? 431  ILE D CD1   1 
ATOM   5657  N  N     . PHE B  1  24  ? 4.844   52.914  13.898 1.00 44.99  ? 432  PHE D N     1 
ATOM   5658  C  CA    . PHE B  1  24  ? 4.033   51.907  14.568 1.00 44.84  ? 432  PHE D CA    1 
ATOM   5659  C  C     . PHE B  1  24  ? 3.700   52.306  15.995 1.00 42.49  ? 432  PHE D C     1 
ATOM   5660  O  O     . PHE B  1  24  ? 4.584   52.695  16.771 1.00 36.94  ? 432  PHE D O     1 
ATOM   5661  C  CB    . PHE B  1  24  ? 4.742   50.555  14.538 1.00 45.35  ? 432  PHE D CB    1 
ATOM   5662  C  CG    . PHE B  1  24  ? 4.806   49.930  13.167 1.00 45.28  ? 432  PHE D CG    1 
ATOM   5663  C  CD1   . PHE B  1  24  ? 5.733   50.376  12.216 1.00 49.14  ? 432  PHE D CD1   1 
ATOM   5664  C  CD2   . PHE B  1  24  ? 3.935   48.888  12.821 1.00 47.03  ? 432  PHE D CD2   1 
ATOM   5665  C  CE1   . PHE B  1  24  ? 5.825   49.791  10.970 1.00 46.30  ? 432  PHE D CE1   1 
ATOM   5666  C  CE2   . PHE B  1  24  ? 3.997   48.308  11.564 1.00 44.01  ? 432  PHE D CE2   1 
ATOM   5667  C  CZ    . PHE B  1  24  ? 4.956   48.748  10.649 1.00 48.97  ? 432  PHE D CZ    1 
ATOM   5668  N  N     . LEU B  1  25  ? 2.410   52.230  16.316 1.00 36.54  ? 433  LEU D N     1 
ATOM   5669  C  CA    . LEU B  1  25  ? 1.923   52.484  17.660 1.00 40.91  ? 433  LEU D CA    1 
ATOM   5670  C  C     . LEU B  1  25  ? 1.703   51.144  18.380 1.00 40.65  ? 433  LEU D C     1 
ATOM   5671  O  O     . LEU B  1  25  ? 0.931   50.305  17.918 1.00 38.54  ? 433  LEU D O     1 
ATOM   5672  C  CB    . LEU B  1  25  ? 0.625   53.286  17.582 1.00 43.36  ? 433  LEU D CB    1 
ATOM   5673  C  CG    . LEU B  1  25  ? 0.654   54.572  16.755 1.00 42.71  ? 433  LEU D CG    1 
ATOM   5674  C  CD1   . LEU B  1  25  ? -0.700  55.259  16.861 1.00 37.77  ? 433  LEU D CD1   1 
ATOM   5675  C  CD2   . LEU B  1  25  ? 1.810   55.479  17.205 1.00 37.25  ? 433  LEU D CD2   1 
ATOM   5676  N  N     . VAL B  1  26  ? 2.407   50.942  19.481 1.00 39.54  ? 434  VAL D N     1 
ATOM   5677  C  CA    . VAL B  1  26  ? 2.316   49.683  20.247 1.00 42.94  ? 434  VAL D CA    1 
ATOM   5678  C  C     . VAL B  1  26  ? 1.950   49.973  21.694 1.00 44.63  ? 434  VAL D C     1 
ATOM   5679  O  O     . VAL B  1  26  ? 2.094   51.129  22.145 1.00 38.96  ? 434  VAL D O     1 
ATOM   5680  C  CB    . VAL B  1  26  ? 3.609   48.848  20.178 1.00 37.63  ? 434  VAL D CB    1 
ATOM   5681  C  CG1   . VAL B  1  26  ? 3.910   48.477  18.747 1.00 36.22  ? 434  VAL D CG1   1 
ATOM   5682  C  CG2   . VAL B  1  26  ? 4.780   49.632  20.741 1.00 37.97  ? 434  VAL D CG2   1 
ATOM   5683  N  N     . GLU B  1  27  ? 1.522   48.939  22.423 1.00 47.20  ? 435  GLU D N     1 
ATOM   5684  C  CA    . GLU B  1  27  ? 0.977   49.125  23.781 1.00 55.47  ? 435  GLU D CA    1 
ATOM   5685  C  C     . GLU B  1  27  ? 1.913   49.588  24.909 1.00 51.96  ? 435  GLU D C     1 
ATOM   5686  O  O     . GLU B  1  27  ? 1.479   50.285  25.830 1.00 50.19  ? 435  GLU D O     1 
ATOM   5687  C  CB    . GLU B  1  27  ? 0.209   47.887  24.232 1.00 52.22  ? 435  GLU D CB    1 
ATOM   5688  C  CG    . GLU B  1  27  ? -0.997  47.566  23.377 1.00 54.75  ? 435  GLU D CG    1 
ATOM   5689  C  CD    . GLU B  1  27  ? -1.851  46.470  23.989 1.00 57.39  ? 435  GLU D CD    1 
ATOM   5690  O  OE1   . GLU B  1  27  ? -2.519  45.740  23.228 1.00 52.04  ? 435  GLU D OE1   1 
ATOM   5691  O  OE2   . GLU B  1  27  ? -1.833  46.354  25.245 1.00 61.00  ? 435  GLU D OE2   1 
ATOM   5692  N  N     . GLY B  1  28  ? 3.170   49.172  24.868 1.00 51.19  ? 436  GLY D N     1 
ATOM   5693  C  CA    . GLY B  1  28  ? 4.087   49.451  25.976 1.00 44.17  ? 436  GLY D CA    1 
ATOM   5694  C  C     . GLY B  1  28  ? 5.449   49.064  25.535 1.00 42.32  ? 436  GLY D C     1 
ATOM   5695  O  O     . GLY B  1  28  ? 5.634   48.772  24.348 1.00 37.40  ? 436  GLY D O     1 
ATOM   5696  N  N     . ASP B  1  29  ? 6.386   49.096  26.478 1.00 39.20  ? 437  ASP D N     1 
ATOM   5697  C  CA    . ASP B  1  29  ? 7.796   48.802  26.208 1.00 40.71  ? 437  ASP D CA    1 
ATOM   5698  C  C     . ASP B  1  29  ? 8.032   47.324  25.984 1.00 39.59  ? 437  ASP D C     1 
ATOM   5699  O  O     . ASP B  1  29  ? 9.013   46.936  25.321 1.00 43.33  ? 437  ASP D O     1 
ATOM   5700  C  CB    . ASP B  1  29  ? 8.689   49.346  27.318 1.00 44.30  ? 437  ASP D CB    1 
ATOM   5701  C  CG    . ASP B  1  29  ? 8.771   50.880  27.291 1.00 50.08  ? 437  ASP D CG    1 
ATOM   5702  O  OD1   . ASP B  1  29  ? 8.634   51.450  26.195 1.00 47.66  ? 437  ASP D OD1   1 
ATOM   5703  O  OD2   . ASP B  1  29  ? 8.981   51.530  28.342 1.00 44.97  ? 437  ASP D OD2   1 
ATOM   5704  N  N     . SER B  1  30  ? 7.134   46.493  26.518 1.00 37.76  ? 438  SER D N     1 
ATOM   5705  C  CA    . SER B  1  30  ? 7.279   45.050  26.324 1.00 36.78  ? 438  SER D CA    1 
ATOM   5706  C  C     . SER B  1  30  ? 7.222   44.764  24.836 1.00 39.07  ? 438  SER D C     1 
ATOM   5707  O  O     . SER B  1  30  ? 8.146   44.176  24.264 1.00 38.55  ? 438  SER D O     1 
ATOM   5708  C  CB    . SER B  1  30  ? 6.257   44.268  27.116 1.00 33.84  ? 438  SER D CB    1 
ATOM   5709  O  OG    . SER B  1  30  ? 6.496   44.433  28.521 1.00 35.60  ? 438  SER D OG    1 
ATOM   5710  N  N     . ALA B  1  31  ? 6.182   45.281  24.207 1.00 41.73  ? 439  ALA D N     1 
ATOM   5711  C  CA    . ALA B  1  31  ? 5.997   45.163  22.784 1.00 39.03  ? 439  ALA D CA    1 
ATOM   5712  C  C     . ALA B  1  31  ? 7.009   45.999  22.053 1.00 43.49  ? 439  ALA D C     1 
ATOM   5713  O  O     . ALA B  1  31  ? 7.498   45.582  21.014 1.00 45.39  ? 439  ALA D O     1 
ATOM   5714  C  CB    . ALA B  1  31  ? 4.589   45.581  22.406 1.00 40.31  ? 439  ALA D CB    1 
ATOM   5715  N  N     . GLY B  1  32  ? 7.329   47.172  22.595 1.00 45.24  ? 440  GLY D N     1 
ATOM   5716  C  CA    . GLY B  1  32  ? 8.168   48.130  21.875 1.00 48.71  ? 440  GLY D CA    1 
ATOM   5717  C  C     . GLY B  1  32  ? 9.569   47.634  21.557 1.00 44.46  ? 440  GLY D C     1 
ATOM   5718  O  O     . GLY B  1  32  ? 10.137  47.983  20.533 1.00 44.76  ? 440  GLY D O     1 
ATOM   5719  N  N     . GLY B  1  33  ? 10.112  46.861  22.473 1.00 44.49  ? 441  GLY D N     1 
ATOM   5720  C  CA    . GLY B  1  33  ? 11.461  46.340  22.319 1.00 51.22  ? 441  GLY D CA    1 
ATOM   5721  C  C     . GLY B  1  33  ? 11.555  45.270  21.240 1.00 46.81  ? 441  GLY D C     1 
ATOM   5722  O  O     . GLY B  1  33  ? 12.520  45.253  20.501 1.00 51.11  ? 441  GLY D O     1 
ATOM   5723  N  N     . SER B  1  34  ? 10.532  44.421  21.118 1.00 49.02  ? 442  SER D N     1 
ATOM   5724  C  CA    . SER B  1  34  ? 10.558  43.404  20.065 1.00 50.86  ? 442  SER D CA    1 
ATOM   5725  C  C     . SER B  1  34  ? 10.433  44.169  18.750 1.00 52.00  ? 442  SER D C     1 
ATOM   5726  O  O     . SER B  1  34  ? 11.116  43.912  17.784 1.00 53.05  ? 442  SER D O     1 
ATOM   5727  C  CB    . SER B  1  34  ? 9.394   42.425  20.219 1.00 52.56  ? 442  SER D CB    1 
ATOM   5728  O  OG    . SER B  1  34  ? 9.476   41.706  21.413 1.00 59.57  ? 442  SER D OG    1 
ATOM   5729  N  N     A THR B  1  35  ? 9.644   45.221  18.820 0.50 47.89  ? 443  THR D N     1 
ATOM   5730  N  N     B THR B  1  35  ? 9.569   45.142  18.711 0.50 48.69  ? 443  THR D N     1 
ATOM   5731  C  CA    A THR B  1  35  ? 9.289   45.961  17.675 0.50 46.51  ? 443  THR D CA    1 
ATOM   5732  C  CA    B THR B  1  35  ? 9.389   45.835  17.498 0.50 48.58  ? 443  THR D CA    1 
ATOM   5733  C  C     A THR B  1  35  ? 10.519  46.709  17.124 0.50 46.93  ? 443  THR D C     1 
ATOM   5734  C  C     B THR B  1  35  ? 10.537  46.767  17.089 0.50 47.86  ? 443  THR D C     1 
ATOM   5735  O  O     A THR B  1  35  ? 10.853  46.606  15.897 0.50 45.12  ? 443  THR D O     1 
ATOM   5736  O  O     B THR B  1  35  ? 10.859  46.851  15.905 0.50 45.52  ? 443  THR D O     1 
ATOM   5737  C  CB    A THR B  1  35  ? 8.134   46.931  18.007 0.50 47.71  ? 443  THR D CB    1 
ATOM   5738  C  CB    B THR B  1  35  ? 7.995   46.421  17.484 0.50 50.98  ? 443  THR D CB    1 
ATOM   5739  O  OG1   A THR B  1  35  ? 7.003   46.209  18.511 0.50 42.48  ? 443  THR D OG1   1 
ATOM   5740  O  OG1   B THR B  1  35  ? 7.992   47.733  18.054 0.50 53.95  ? 443  THR D OG1   1 
ATOM   5741  C  CG2   A THR B  1  35  ? 7.710   47.635  16.763 0.50 41.19  ? 443  THR D CG2   1 
ATOM   5742  C  CG2   B THR B  1  35  ? 7.099   45.558  18.320 0.50 47.44  ? 443  THR D CG2   1 
ATOM   5743  N  N     . LYS B  1  36  ? 11.209  47.399  18.034 1.00 45.52  ? 444  LYS D N     1 
ATOM   5744  C  CA    . LYS B  1  36  ? 12.442  48.111  17.674 1.00 50.98  ? 444  LYS D CA    1 
ATOM   5745  C  C     . LYS B  1  36  ? 13.537  47.208  17.119 1.00 51.19  ? 444  LYS D C     1 
ATOM   5746  O  O     . LYS B  1  36  ? 14.273  47.629  16.261 1.00 55.67  ? 444  LYS D O     1 
ATOM   5747  C  CB    . LYS B  1  36  ? 13.032  48.816  18.852 1.00 53.71  ? 444  LYS D CB    1 
ATOM   5748  C  CG    . LYS B  1  36  ? 12.578  50.242  19.023 1.00 64.27  ? 444  LYS D CG    1 
ATOM   5749  C  CD    . LYS B  1  36  ? 12.718  50.697  20.472 1.00 67.91  ? 444  LYS D CD    1 
ATOM   5750  C  CE    . LYS B  1  36  ? 11.491  51.527  20.850 1.00 74.14  ? 444  LYS D CE    1 
ATOM   5751  N  NZ    . LYS B  1  36  ? 11.629  52.406  22.046 1.00 71.29  ? 444  LYS D NZ    1 
ATOM   5752  N  N     . SER B  1  37  ? 13.650  45.985  17.607 1.00 50.82  ? 445  SER D N     1 
ATOM   5753  C  CA    . SER B  1  37  ? 14.719  45.111  17.127 1.00 53.02  ? 445  SER D CA    1 
ATOM   5754  C  C     . SER B  1  37  ? 14.428  44.532  15.761 1.00 53.86  ? 445  SER D C     1 
ATOM   5755  O  O     . SER B  1  37  ? 15.351  44.386  14.930 1.00 52.00  ? 445  SER D O     1 
ATOM   5756  C  CB    . SER B  1  37  ? 14.982  43.984  18.102 1.00 47.73  ? 445  SER D CB    1 
ATOM   5757  O  OG    . SER B  1  37  ? 15.634  44.443  19.248 1.00 61.05  ? 445  SER D OG    1 
ATOM   5758  N  N     . GLY B  1  38  ? 13.150  44.242  15.527 1.00 49.42  ? 446  GLY D N     1 
ATOM   5759  C  CA    . GLY B  1  38  ? 12.746  43.568  14.314 1.00 51.40  ? 446  GLY D CA    1 
ATOM   5760  C  C     . GLY B  1  38  ? 12.502  44.454  13.121 1.00 47.33  ? 446  GLY D C     1 
ATOM   5761  O  O     . GLY B  1  38  ? 12.475  43.954  11.999 1.00 57.79  ? 446  GLY D O     1 
ATOM   5762  N  N     . ARG B  1  39  ? 12.306  45.749  13.350 1.00 45.45  ? 447  ARG D N     1 
ATOM   5763  C  CA    . ARG B  1  39  ? 11.940  46.674  12.283 1.00 43.61  ? 447  ARG D CA    1 
ATOM   5764  C  C     . ARG B  1  39  ? 13.055  46.975  11.277 1.00 50.09  ? 447  ARG D C     1 
ATOM   5765  O  O     . ARG B  1  39  ? 14.197  46.561  11.439 1.00 52.66  ? 447  ARG D O     1 
ATOM   5766  C  CB    . ARG B  1  39  ? 11.527  47.999  12.899 1.00 44.56  ? 447  ARG D CB    1 
ATOM   5767  C  CG    . ARG B  1  39  ? 12.694  48.740  13.537 1.00 41.89  ? 447  ARG D CG    1 
ATOM   5768  C  CD    . ARG B  1  39  ? 12.306  50.127  14.010 1.00 43.57  ? 447  ARG D CD    1 
ATOM   5769  N  NE    . ARG B  1  39  ? 13.388  50.693  14.817 1.00 47.58  ? 447  ARG D NE    1 
ATOM   5770  C  CZ    . ARG B  1  39  ? 13.601  51.986  14.986 1.00 52.02  ? 447  ARG D CZ    1 
ATOM   5771  N  NH1   . ARG B  1  39  ? 14.606  52.396  15.720 1.00 55.66  ? 447  ARG D NH1   1 
ATOM   5772  N  NH2   . ARG B  1  39  ? 12.798  52.870  14.417 1.00 57.46  ? 447  ARG D NH2   1 
ATOM   5773  N  N     . ASP B  1  40  ? 12.710  47.750  10.261 1.00 51.36  ? 448  ASP D N     1 
ATOM   5774  C  CA    . ASP B  1  40  ? 13.655  48.298  9.339  1.00 54.69  ? 448  ASP D CA    1 
ATOM   5775  C  C     . ASP B  1  40  ? 13.785  49.744  9.835  1.00 56.48  ? 448  ASP D C     1 
ATOM   5776  O  O     . ASP B  1  40  ? 12.869  50.566  9.627  1.00 50.94  ? 448  ASP D O     1 
ATOM   5777  C  CB    . ASP B  1  40  ? 13.074  48.260  7.926  1.00 56.16  ? 448  ASP D CB    1 
ATOM   5778  C  CG    . ASP B  1  40  ? 13.949  48.999  6.905  1.00 55.69  ? 448  ASP D CG    1 
ATOM   5779  O  OD1   . ASP B  1  40  ? 14.983  49.611  7.275  1.00 53.80  ? 448  ASP D OD1   1 
ATOM   5780  O  OD2   . ASP B  1  40  ? 13.600  48.949  5.723  1.00 54.60  ? 448  ASP D OD2   1 
ATOM   5781  N  N     . SER B  1  41  ? 14.896  50.044  10.503 1.00 45.80  ? 449  SER D N     1 
ATOM   5782  C  CA    . SER B  1  41  ? 15.059  51.360  11.112 1.00 50.15  ? 449  SER D CA    1 
ATOM   5783  C  C     . SER B  1  41  ? 15.111  52.521  10.098 1.00 55.62  ? 449  SER D C     1 
ATOM   5784  O  O     . SER B  1  41  ? 14.946  53.681  10.443 1.00 55.85  ? 449  SER D O     1 
ATOM   5785  C  CB    . SER B  1  41  ? 16.274  51.375  12.026 1.00 53.86  ? 449  SER D CB    1 
ATOM   5786  O  OG    . SER B  1  41  ? 17.452  51.084  11.347 1.00 55.49  ? 449  SER D OG    1 
ATOM   5787  N  N     . ARG B  1  42  ? 15.359  52.176  8.851  1.00 56.73  ? 450  ARG D N     1 
ATOM   5788  C  CA    . ARG B  1  42  ? 15.436  53.140  7.784  1.00 63.70  ? 450  ARG D CA    1 
ATOM   5789  C  C     . ARG B  1  42  ? 14.093  53.816  7.563  1.00 64.50  ? 450  ARG D C     1 
ATOM   5790  O  O     . ARG B  1  42  ? 14.018  55.019  7.427  1.00 61.07  ? 450  ARG D O     1 
ATOM   5791  C  CB    . ARG B  1  42  ? 15.810  52.365  6.531  1.00 70.35  ? 450  ARG D CB    1 
ATOM   5792  C  CG    . ARG B  1  42  ? 16.261  53.162  5.350  1.00 72.27  ? 450  ARG D CG    1 
ATOM   5793  C  CD    . ARG B  1  42  ? 16.215  52.281  4.085  1.00 71.12  ? 450  ARG D CD    1 
ATOM   5794  N  NE    . ARG B  1  42  ? 15.229  52.750  3.096  1.00 70.49  ? 450  ARG D NE    1 
ATOM   5795  C  CZ    . ARG B  1  42  ? 14.987  54.032  2.810  1.00 70.74  ? 450  ARG D CZ    1 
ATOM   5796  N  NH1   . ARG B  1  42  ? 14.094  54.325  1.899  1.00 69.46  ? 450  ARG D NH1   1 
ATOM   5797  N  NH2   . ARG B  1  42  ? 15.661  55.017  3.416  1.00 77.34  ? 450  ARG D NH2   1 
ATOM   5798  N  N     . THR B  1  43  ? 13.035  53.030  7.500  1.00 64.49  ? 451  THR D N     1 
ATOM   5799  C  CA    . THR B  1  43  ? 11.734  53.607  7.217  1.00 62.63  ? 451  THR D CA    1 
ATOM   5800  C  C     . THR B  1  43  ? 10.695  53.461  8.302  1.00 64.73  ? 451  THR D C     1 
ATOM   5801  O  O     . THR B  1  43  ? 9.634   54.053  8.179  1.00 57.28  ? 451  THR D O     1 
ATOM   5802  C  CB    . THR B  1  43  ? 11.130  53.044  5.932  1.00 60.04  ? 451  THR D CB    1 
ATOM   5803  O  OG1   . THR B  1  43  ? 11.152  51.620  5.976  1.00 52.11  ? 451  THR D OG1   1 
ATOM   5804  C  CG2   . THR B  1  43  ? 11.923  53.501  4.782  1.00 62.49  ? 451  THR D CG2   1 
ATOM   5805  N  N     . GLN B  1  44  ? 10.977  52.688  9.349  1.00 58.36  ? 452  GLN D N     1 
ATOM   5806  C  CA    . GLN B  1  44  ? 9.938   52.395  10.308 1.00 50.58  ? 452  GLN D CA    1 
ATOM   5807  C  C     . GLN B  1  44  ? 10.241  52.944  11.676 1.00 50.19  ? 452  GLN D C     1 
ATOM   5808  O  O     . GLN B  1  44  ? 11.249  52.637  12.243 1.00 52.33  ? 452  GLN D O     1 
ATOM   5809  C  CB    . GLN B  1  44  ? 9.699   50.898  10.371 1.00 52.52  ? 452  GLN D CB    1 
ATOM   5810  C  CG    . GLN B  1  44  ? 9.223   50.303  9.059  1.00 47.63  ? 452  GLN D CG    1 
ATOM   5811  C  CD    . GLN B  1  44  ? 9.111   48.785  9.126  1.00 53.65  ? 452  GLN D CD    1 
ATOM   5812  O  OE1   . GLN B  1  44  ? 9.776   48.120  9.910  1.00 50.36  ? 452  GLN D OE1   1 
ATOM   5813  N  NE2   . GLN B  1  44  ? 8.255   48.232  8.297  1.00 58.71  ? 452  GLN D NE2   1 
ATOM   5814  N  N     . ALA B  1  45  ? 9.334   53.736  12.217 1.00 50.66  ? 453  ALA D N     1 
ATOM   5815  C  CA    . ALA B  1  45  ? 9.450   54.275  13.560 1.00 48.39  ? 453  ALA D CA    1 
ATOM   5816  C  C     . ALA B  1  45  ? 8.532   53.544  14.559 1.00 47.45  ? 453  ALA D C     1 
ATOM   5817  O  O     . ALA B  1  45  ? 7.544   52.961  14.155 1.00 47.16  ? 453  ALA D O     1 
ATOM   5818  C  CB    . ALA B  1  45  ? 9.102   55.749  13.508 1.00 45.53  ? 453  ALA D CB    1 
ATOM   5819  N  N     . ILE B  1  46  ? 8.856   53.577  15.852 1.00 44.60  ? 454  ILE D N     1 
ATOM   5820  C  CA    . ILE B  1  46  ? 8.029   52.947  16.858 1.00 45.79  ? 454  ILE D CA    1 
ATOM   5821  C  C     . ILE B  1  46  ? 7.739   53.934  17.945 1.00 45.05  ? 454  ILE D C     1 
ATOM   5822  O  O     . ILE B  1  46  ? 8.656   54.530  18.511 1.00 42.33  ? 454  ILE D O     1 
ATOM   5823  C  CB    . ILE B  1  46  ? 8.749   51.799  17.587 1.00 48.31  ? 454  ILE D CB    1 
ATOM   5824  C  CG1   . ILE B  1  46  ? 9.566   50.937  16.631 1.00 45.87  ? 454  ILE D CG1   1 
ATOM   5825  C  CG2   . ILE B  1  46  ? 7.726   50.999  18.368 1.00 42.30  ? 454  ILE D CG2   1 
ATOM   5826  C  CD1   . ILE B  1  46  ? 8.704   50.232  15.608 1.00 47.36  ? 454  ILE D CD1   1 
ATOM   5827  N  N     . LEU B  1  47  ? 6.478   54.074  18.295 1.00 39.16  ? 455  LEU D N     1 
ATOM   5828  C  CA    . LEU B  1  47  ? 6.167   54.876  19.429 1.00 44.70  ? 455  LEU D CA    1 
ATOM   5829  C  C     . LEU B  1  47  ? 5.371   53.993  20.366 1.00 45.82  ? 455  LEU D C     1 
ATOM   5830  O  O     . LEU B  1  47  ? 4.243   53.656  20.091 1.00 44.18  ? 455  LEU D O     1 
ATOM   5831  C  CB    . LEU B  1  47  ? 5.365   56.124  19.047 1.00 45.00  ? 455  LEU D CB    1 
ATOM   5832  C  CG    . LEU B  1  47  ? 4.865   56.957  20.231 1.00 40.53  ? 455  LEU D CG    1 
ATOM   5833  C  CD1   . LEU B  1  47  ? 5.979   57.737  20.892 1.00 40.69  ? 455  LEU D CD1   1 
ATOM   5834  C  CD2   . LEU B  1  47  ? 3.811   57.918  19.777 1.00 43.87  ? 455  LEU D CD2   1 
ATOM   5835  N  N     . PRO B  1  48  ? 5.945   53.640  21.496 1.00 47.30  ? 456  PRO D N     1 
ATOM   5836  C  CA    . PRO B  1  48  ? 5.221   52.851  22.496 1.00 47.15  ? 456  PRO D CA    1 
ATOM   5837  C  C     . PRO B  1  48  ? 4.345   53.744  23.334 1.00 46.11  ? 456  PRO D C     1 
ATOM   5838  O  O     . PRO B  1  48  ? 4.770   54.816  23.762 1.00 40.73  ? 456  PRO D O     1 
ATOM   5839  C  CB    . PRO B  1  48  ? 6.335   52.251  23.362 1.00 47.59  ? 456  PRO D CB    1 
ATOM   5840  C  CG    . PRO B  1  48  ? 7.630   52.653  22.708 1.00 50.60  ? 456  PRO D CG    1 
ATOM   5841  C  CD    . PRO B  1  48  ? 7.354   53.850  21.856 1.00 50.75  ? 456  PRO D CD    1 
ATOM   5842  N  N     . LEU B  1  49  ? 3.127   53.302  23.574 1.00 47.48  ? 457  LEU D N     1 
ATOM   5843  C  CA    . LEU B  1  49  ? 2.207   54.076  24.407 1.00 55.16  ? 457  LEU D CA    1 
ATOM   5844  C  C     . LEU B  1  49  ? 2.234   53.556  25.846 1.00 55.96  ? 457  LEU D C     1 
ATOM   5845  O  O     . LEU B  1  49  ? 3.167   52.895  26.242 1.00 57.46  ? 457  LEU D O     1 
ATOM   5846  C  CB    . LEU B  1  49  ? 0.811   53.998  23.807 1.00 52.30  ? 457  LEU D CB    1 
ATOM   5847  C  CG    . LEU B  1  49  ? 0.760   54.583  22.403 1.00 49.44  ? 457  LEU D CG    1 
ATOM   5848  C  CD1   . LEU B  1  49  ? -0.572  54.227  21.822 1.00 50.67  ? 457  LEU D CD1   1 
ATOM   5849  C  CD2   . LEU B  1  49  ? 0.901   56.080  22.435 1.00 46.36  ? 457  LEU D CD2   1 
ATOM   5850  N  N     . ARG B  1  50  ? 1.230   53.842  26.654 1.00 52.79  ? 458  ARG D N     1 
ATOM   5851  C  CA    . ARG B  1  50  ? 1.262   53.379  28.029 1.00 52.84  ? 458  ARG D CA    1 
ATOM   5852  C  C     . ARG B  1  50  ? -0.023  52.745  28.453 1.00 48.49  ? 458  ARG D C     1 
ATOM   5853  O  O     . ARG B  1  50  ? -0.663  53.248  29.356 1.00 47.76  ? 458  ARG D O     1 
ATOM   5854  C  CB    . ARG B  1  50  ? 1.575   54.538  28.974 1.00 52.33  ? 458  ARG D CB    1 
ATOM   5855  C  CG    . ARG B  1  50  ? 2.952   54.444  29.537 1.00 62.74  ? 458  ARG D CG    1 
ATOM   5856  C  CD    . ARG B  1  50  ? 3.743   55.737  29.486 1.00 70.07  ? 458  ARG D CD    1 
ATOM   5857  N  NE    . ARG B  1  50  ? 3.940   56.231  30.846 1.00 79.32  ? 458  ARG D NE    1 
ATOM   5858  C  CZ    . ARG B  1  50  ? 5.065   56.762  31.317 1.00 84.34  ? 458  ARG D CZ    1 
ATOM   5859  N  NH1   . ARG B  1  50  ? 6.135   56.895  30.536 1.00 82.18  ? 458  ARG D NH1   1 
ATOM   5860  N  NH2   . ARG B  1  50  ? 5.114   57.159  32.584 1.00 80.76  ? 458  ARG D NH2   1 
ATOM   5861  N  N     . GLY B  1  51  ? -0.391  51.634  27.827 1.00 44.24  ? 459  GLY D N     1 
ATOM   5862  C  CA    . GLY B  1  51  ? -1.637  50.952  28.174 1.00 40.47  ? 459  GLY D CA    1 
ATOM   5863  C  C     . GLY B  1  51  ? -2.823  51.732  27.695 1.00 38.05  ? 459  GLY D C     1 
ATOM   5864  O  O     . GLY B  1  51  ? -2.796  52.304  26.598 1.00 37.73  ? 459  GLY D O     1 
ATOM   5865  N  N     . LYS B  1  52  ? -3.881  51.739  28.482 1.00 36.01  ? 460  LYS D N     1 
ATOM   5866  C  CA    . LYS B  1  52  ? -5.128  52.338  28.020 1.00 37.65  ? 460  LYS D CA    1 
ATOM   5867  C  C     . LYS B  1  52  ? -4.894  53.844  27.893 1.00 40.48  ? 460  LYS D C     1 
ATOM   5868  O  O     . LYS B  1  52  ? -4.282  54.423  28.799 1.00 33.44  ? 460  LYS D O     1 
ATOM   5869  C  CB    . LYS B  1  52  ? -6.191  52.097  29.056 1.00 37.80  ? 460  LYS D CB    1 
ATOM   5870  C  CG    . LYS B  1  52  ? -6.541  50.641  29.311 1.00 37.98  ? 460  LYS D CG    1 
ATOM   5871  C  CD    . LYS B  1  52  ? -7.298  50.132  28.121 1.00 38.48  ? 460  LYS D CD    1 
ATOM   5872  C  CE    . LYS B  1  52  ? -7.355  48.629  28.100 1.00 36.80  ? 460  LYS D CE    1 
ATOM   5873  N  NZ    . LYS B  1  52  ? -8.683  48.151  28.623 1.00 32.91  ? 460  LYS D NZ    1 
ATOM   5874  N  N     . ILE B  1  53  ? -5.339  54.459  26.798 1.00 37.62  ? 461  ILE D N     1 
ATOM   5875  C  CA    . ILE B  1  53  ? -5.130  55.891  26.618 1.00 40.58  ? 461  ILE D CA    1 
ATOM   5876  C  C     . ILE B  1  53  ? -6.457  56.609  26.794 1.00 38.83  ? 461  ILE D C     1 
ATOM   5877  O  O     . ILE B  1  53  ? -7.535  56.004  26.753 1.00 34.68  ? 461  ILE D O     1 
ATOM   5878  C  CB    . ILE B  1  53  ? -4.657  56.248  25.214 1.00 46.03  ? 461  ILE D CB    1 
ATOM   5879  C  CG1   . ILE B  1  53  ? -5.594  55.589  24.232 1.00 49.43  ? 461  ILE D CG1   1 
ATOM   5880  C  CG2   . ILE B  1  53  ? -3.247  55.772  24.977 1.00 50.26  ? 461  ILE D CG2   1 
ATOM   5881  C  CD1   . ILE B  1  53  ? -6.101  56.506  23.154 1.00 58.59  ? 461  ILE D CD1   1 
ATOM   5882  N  N     . LEU B  1  54  ? -6.367  57.904  26.959 1.00 33.70  ? 462  LEU D N     1 
ATOM   5883  C  CA    . LEU B  1  54  ? -7.508  58.716  27.218 1.00 37.67  ? 462  LEU D CA    1 
ATOM   5884  C  C     . LEU B  1  54  ? -8.627  58.552  26.195 1.00 39.29  ? 462  LEU D C     1 
ATOM   5885  O  O     . LEU B  1  54  ? -8.382  58.554  25.006 1.00 44.40  ? 462  LEU D O     1 
ATOM   5886  C  CB    . LEU B  1  54  ? -7.014  60.147  27.209 1.00 38.77  ? 462  LEU D CB    1 
ATOM   5887  C  CG    . LEU B  1  54  ? -8.019  61.242  27.552 1.00 45.98  ? 462  LEU D CG    1 
ATOM   5888  C  CD1   . LEU B  1  54  ? -8.473  61.186  29.019 1.00 44.00  ? 462  LEU D CD1   1 
ATOM   5889  C  CD2   . LEU B  1  54  ? -7.301  62.554  27.275 1.00 46.40  ? 462  LEU D CD2   1 
ATOM   5890  N  N     . ASN B  1  55  ? -9.857  58.413  26.652 1.00 39.81  ? 463  ASN D N     1 
ATOM   5891  C  CA    . ASN B  1  55  ? -10.979 58.388  25.716 1.00 40.64  ? 463  ASN D CA    1 
ATOM   5892  C  C     . ASN B  1  55  ? -11.372 59.852  25.483 1.00 41.97  ? 463  ASN D C     1 
ATOM   5893  O  O     . ASN B  1  55  ? -11.898 60.511  26.396 1.00 39.11  ? 463  ASN D O     1 
ATOM   5894  C  CB    . ASN B  1  55  ? -12.134 57.624  26.328 1.00 37.13  ? 463  ASN D CB    1 
ATOM   5895  C  CG    . ASN B  1  55  ? -13.384 57.620  25.451 1.00 45.08  ? 463  ASN D CG    1 
ATOM   5896  O  OD1   . ASN B  1  55  ? -13.491 58.332  24.451 1.00 45.83  ? 463  ASN D OD1   1 
ATOM   5897  N  ND2   . ASN B  1  55  ? -14.338 56.776  25.816 1.00 39.27  ? 463  ASN D ND2   1 
ATOM   5898  N  N     . VAL B  1  56  ? -11.089 60.368  24.292 1.00 41.42  ? 464  VAL D N     1 
ATOM   5899  C  CA    . VAL B  1  56  ? -11.293 61.804  24.058 1.00 46.34  ? 464  VAL D CA    1 
ATOM   5900  C  C     . VAL B  1  56  ? -12.746 62.111  23.821 1.00 46.37  ? 464  VAL D C     1 
ATOM   5901  O  O     . VAL B  1  56  ? -13.163 63.237  23.910 1.00 48.49  ? 464  VAL D O     1 
ATOM   5902  C  CB    . VAL B  1  56  ? -10.456 62.361  22.902 1.00 47.58  ? 464  VAL D CB    1 
ATOM   5903  C  CG1   . VAL B  1  56  ? -8.975  62.274  23.264 1.00 40.31  ? 464  VAL D CG1   1 
ATOM   5904  C  CG2   . VAL B  1  56  ? -10.804 61.659  21.595 1.00 45.42  ? 464  VAL D CG2   1 
ATOM   5905  N  N     . GLU B  1  57  ? -13.532 61.091  23.550 1.00 39.83  ? 465  GLU D N     1 
ATOM   5906  C  CA    . GLU B  1  57  ? -14.954 61.306  23.426 1.00 44.50  ? 465  GLU D CA    1 
ATOM   5907  C  C     . GLU B  1  57  ? -15.599 61.671  24.777 1.00 45.21  ? 465  GLU D C     1 
ATOM   5908  O  O     . GLU B  1  57  ? -16.644 62.261  24.802 1.00 50.28  ? 465  GLU D O     1 
ATOM   5909  C  CB    . GLU B  1  57  ? -15.605 60.070  22.823 1.00 42.72  ? 465  GLU D CB    1 
ATOM   5910  C  CG    . GLU B  1  57  ? -17.027 60.263  22.371 1.00 49.39  ? 465  GLU D CG    1 
ATOM   5911  C  CD    . GLU B  1  57  ? -17.117 61.034  21.052 1.00 60.68  ? 465  GLU D CD    1 
ATOM   5912  O  OE1   . GLU B  1  57  ? -16.094 61.262  20.373 1.00 59.59  ? 465  GLU D OE1   1 
ATOM   5913  O  OE2   . GLU B  1  57  ? -18.228 61.442  20.660 1.00 63.35  ? 465  GLU D OE2   1 
ATOM   5914  N  N     . LYS B  1  58  ? -14.984 61.292  25.886 1.00 44.92  ? 466  LYS D N     1 
ATOM   5915  C  CA    . LYS B  1  58  ? -15.536 61.582  27.205 1.00 41.17  ? 466  LYS D CA    1 
ATOM   5916  C  C     . LYS B  1  58  ? -14.777 62.658  27.947 1.00 45.36  ? 466  LYS D C     1 
ATOM   5917  O  O     . LYS B  1  58  ? -15.149 63.015  29.052 1.00 45.01  ? 466  LYS D O     1 
ATOM   5918  C  CB    . LYS B  1  58  ? -15.467 60.342  28.093 1.00 38.87  ? 466  LYS D CB    1 
ATOM   5919  C  CG    . LYS B  1  58  ? -16.631 59.382  27.910 1.00 40.54  ? 466  LYS D CG    1 
ATOM   5920  C  CD    . LYS B  1  58  ? -16.281 57.991  28.423 1.00 36.26  ? 466  LYS D CD    1 
ATOM   5921  C  CE    . LYS B  1  58  ? -17.430 57.045  28.126 1.00 35.48  ? 466  LYS D CE    1 
ATOM   5922  N  NZ    . LYS B  1  58  ? -17.184 55.681  28.665 1.00 35.09  ? 466  LYS D NZ    1 
ATOM   5923  N  N     . ALA B  1  59  ? -13.681 63.154  27.393 1.00 47.91  ? 467  ALA D N     1 
ATOM   5924  C  CA    . ALA B  1  59  ? -12.861 64.059  28.167 1.00 50.77  ? 467  ALA D CA    1 
ATOM   5925  C  C     . ALA B  1  59  ? -13.091 65.520  27.785 1.00 52.66  ? 467  ALA D C     1 
ATOM   5926  O  O     . ALA B  1  59  ? -13.574 65.796  26.686 1.00 52.19  ? 467  ALA D O     1 
ATOM   5927  C  CB    . ALA B  1  59  ? -11.417 63.698  28.011 1.00 47.64  ? 467  ALA D CB    1 
ATOM   5928  N  N     . ARG B  1  60  ? -12.769 66.429  28.711 1.00 53.36  ? 468  ARG D N     1 
ATOM   5929  C  CA    . ARG B  1  60  ? -12.774 67.879  28.445 1.00 62.07  ? 468  ARG D CA    1 
ATOM   5930  C  C     . ARG B  1  60  ? -11.540 68.163  27.600 1.00 64.79  ? 468  ARG D C     1 
ATOM   5931  O  O     . ARG B  1  60  ? -10.564 67.423  27.686 1.00 63.45  ? 468  ARG D O     1 
ATOM   5932  C  CB    . ARG B  1  60  ? -12.804 68.694  29.746 1.00 69.02  ? 468  ARG D CB    1 
ATOM   5933  C  CG    . ARG B  1  60  ? -13.942 68.229  30.668 1.00 82.17  ? 468  ARG D CG    1 
ATOM   5934  C  CD    . ARG B  1  60  ? -14.681 69.293  31.495 1.00 84.55  ? 468  ARG D CD    1 
ATOM   5935  N  NE    . ARG B  1  60  ? -13.903 69.814  32.639 1.00 100.92 ? 468  ARG D NE    1 
ATOM   5936  C  CZ    . ARG B  1  60  ? -14.364 70.069  33.877 1.00 101.26 ? 468  ARG D CZ    1 
ATOM   5937  N  NH1   . ARG B  1  60  ? -15.637 69.828  34.203 1.00 96.05  ? 468  ARG D NH1   1 
ATOM   5938  N  NH2   . ARG B  1  60  ? -13.533 70.566  34.803 1.00 83.62  ? 468  ARG D NH2   1 
ATOM   5939  N  N     . LEU B  1  61  ? -11.602 69.205  26.782 1.00 64.25  ? 469  LEU D N     1 
ATOM   5940  C  CA    . LEU B  1  61  ? -10.604 69.490  25.776 1.00 60.69  ? 469  LEU D CA    1 
ATOM   5941  C  C     . LEU B  1  61  ? -9.253  69.861  26.350 1.00 61.40  ? 469  LEU D C     1 
ATOM   5942  O  O     . LEU B  1  61  ? -8.233  69.546  25.776 1.00 60.53  ? 469  LEU D O     1 
ATOM   5943  C  CB    . LEU B  1  61  ? -11.130 70.586  24.871 1.00 60.06  ? 469  LEU D CB    1 
ATOM   5944  C  CG    . LEU B  1  61  ? -10.234 71.209  23.794 1.00 62.18  ? 469  LEU D CG    1 
ATOM   5945  C  CD1   . LEU B  1  61  ? -9.535  70.174  22.943 1.00 53.69  ? 469  LEU D CD1   1 
ATOM   5946  C  CD2   . LEU B  1  61  ? -11.094 72.092  22.905 1.00 62.41  ? 469  LEU D CD2   1 
ATOM   5947  N  N     . ASP B  1  62  ? -9.258  70.548  27.472 1.00 63.35  ? 470  ASP D N     1 
ATOM   5948  C  CA    . ASP B  1  62  ? -8.022  70.962  28.095 1.00 65.03  ? 470  ASP D CA    1 
ATOM   5949  C  C     . ASP B  1  62  ? -7.303  69.756  28.638 1.00 68.31  ? 470  ASP D C     1 
ATOM   5950  O  O     . ASP B  1  62  ? -6.090  69.732  28.656 1.00 66.69  ? 470  ASP D O     1 
ATOM   5951  C  CB    . ASP B  1  62  ? -8.334  71.904  29.220 1.00 69.30  ? 470  ASP D CB    1 
ATOM   5952  C  CG    . ASP B  1  62  ? -9.676  71.585  29.861 1.00 89.35  ? 470  ASP D CG    1 
ATOM   5953  O  OD1   . ASP B  1  62  ? -9.806  70.539  30.555 1.00 82.72  ? 470  ASP D OD1   1 
ATOM   5954  O  OD2   . ASP B  1  62  ? -10.627 72.371  29.624 1.00 96.62  ? 470  ASP D OD2   1 
ATOM   5955  N  N     . ARG B  1  63  ? -8.068  68.775  29.098 1.00 67.55  ? 471  ARG D N     1 
ATOM   5956  C  CA    . ARG B  1  63  ? -7.499  67.534  29.588 1.00 63.58  ? 471  ARG D CA    1 
ATOM   5957  C  C     . ARG B  1  63  ? -6.844  66.782  28.446 1.00 56.31  ? 471  ARG D C     1 
ATOM   5958  O  O     . ARG B  1  63  ? -5.739  66.291  28.599 1.00 51.73  ? 471  ARG D O     1 
ATOM   5959  C  CB    . ARG B  1  63  ? -8.583  66.677  30.221 1.00 61.09  ? 471  ARG D CB    1 
ATOM   5960  C  CG    . ARG B  1  63  ? -8.049  65.452  30.921 1.00 55.52  ? 471  ARG D CG    1 
ATOM   5961  C  CD    . ARG B  1  63  ? -9.109  64.830  31.740 1.00 61.01  ? 471  ARG D CD    1 
ATOM   5962  N  NE    . ARG B  1  63  ? -8.599  63.587  32.261 1.00 59.87  ? 471  ARG D NE    1 
ATOM   5963  C  CZ    . ARG B  1  63  ? -9.347  62.513  32.347 1.00 62.29  ? 471  ARG D CZ    1 
ATOM   5964  N  NH1   . ARG B  1  63  ? -10.603 62.604  31.936 1.00 61.18  ? 471  ARG D NH1   1 
ATOM   5965  N  NH2   . ARG B  1  63  ? -8.842  61.368  32.816 1.00 62.18  ? 471  ARG D NH2   1 
ATOM   5966  N  N     . ILE B  1  64  ? -7.520  66.755  27.310 1.00 51.24  ? 472  ILE D N     1 
ATOM   5967  C  CA    . ILE B  1  64  ? -7.022  66.094  26.148 1.00 51.93  ? 472  ILE D CA    1 
ATOM   5968  C  C     . ILE B  1  64  ? -5.721  66.708  25.694 1.00 60.50  ? 472  ILE D C     1 
ATOM   5969  O  O     . ILE B  1  64  ? -4.803  66.007  25.330 1.00 60.36  ? 472  ILE D O     1 
ATOM   5970  C  CB    . ILE B  1  64  ? -8.016  66.204  25.005 1.00 46.56  ? 472  ILE D CB    1 
ATOM   5971  C  CG1   . ILE B  1  64  ? -9.312  65.538  25.395 1.00 44.66  ? 472  ILE D CG1   1 
ATOM   5972  C  CG2   . ILE B  1  64  ? -7.431  65.561  23.756 1.00 49.29  ? 472  ILE D CG2   1 
ATOM   5973  C  CD1   . ILE B  1  64  ? -10.434 65.834  24.439 1.00 45.16  ? 472  ILE D CD1   1 
ATOM   5974  N  N     . LEU B  1  65  ? -5.658  68.030  25.708 1.00 64.62  ? 473  LEU D N     1 
ATOM   5975  C  CA    . LEU B  1  65  ? -4.475  68.720  25.243 1.00 63.12  ? 473  LEU D CA    1 
ATOM   5976  C  C     . LEU B  1  65  ? -3.300  68.594  26.196 1.00 60.17  ? 473  LEU D C     1 
ATOM   5977  O  O     . LEU B  1  65  ? -2.170  68.728  25.786 1.00 66.42  ? 473  LEU D O     1 
ATOM   5978  C  CB    . LEU B  1  65  ? -4.796  70.180  24.980 1.00 66.69  ? 473  LEU D CB    1 
ATOM   5979  C  CG    . LEU B  1  65  ? -5.921  70.379  23.965 1.00 76.03  ? 473  LEU D CG    1 
ATOM   5980  C  CD1   . LEU B  1  65  ? -6.160  71.861  23.758 1.00 73.04  ? 473  LEU D CD1   1 
ATOM   5981  C  CD2   . LEU B  1  65  ? -5.645  69.684  22.631 1.00 71.79  ? 473  LEU D CD2   1 
ATOM   5982  N  N     . ASN B  1  66  ? -3.588  68.349  27.466 1.00 60.34  ? 474  ASN D N     1 
ATOM   5983  C  CA    . ASN B  1  66  ? -2.575  68.249  28.488 1.00 59.40  ? 474  ASN D CA    1 
ATOM   5984  C  C     . ASN B  1  66  ? -2.099  66.814  28.766 1.00 56.90  ? 474  ASN D C     1 
ATOM   5985  O  O     . ASN B  1  66  ? -1.207  66.619  29.574 1.00 58.29  ? 474  ASN D O     1 
ATOM   5986  C  CB    . ASN B  1  66  ? -3.104  68.885  29.775 1.00 70.09  ? 474  ASN D CB    1 
ATOM   5987  C  CG    . ASN B  1  66  ? -2.014  69.563  30.564 1.00 83.76  ? 474  ASN D CG    1 
ATOM   5988  O  OD1   . ASN B  1  66  ? -1.401  70.511  30.066 1.00 82.56  ? 474  ASN D OD1   1 
ATOM   5989  N  ND2   . ASN B  1  66  ? -1.759  69.092  31.802 1.00 79.88  ? 474  ASN D ND2   1 
ATOM   5990  N  N     . ASN B  1  67  ? -2.682  65.833  28.092 1.00 52.61  ? 475  ASN D N     1 
ATOM   5991  C  CA    . ASN B  1  67  ? -2.363  64.439  28.313 1.00 46.41  ? 475  ASN D CA    1 
ATOM   5992  C  C     . ASN B  1  67  ? -1.101  64.078  27.561 1.00 49.91  ? 475  ASN D C     1 
ATOM   5993  O  O     . ASN B  1  67  ? -0.988  64.334  26.355 1.00 48.11  ? 475  ASN D O     1 
ATOM   5994  C  CB    . ASN B  1  67  ? -3.490  63.614  27.774 1.00 45.77  ? 475  ASN D CB    1 
ATOM   5995  C  CG    . ASN B  1  67  ? -3.258  62.113  27.939 1.00 45.54  ? 475  ASN D CG    1 
ATOM   5996  O  OD1   . ASN B  1  67  ? -2.666  61.489  27.105 1.00 42.63  ? 475  ASN D OD1   1 
ATOM   5997  N  ND2   . ASN B  1  67  ? -3.763  61.540  28.998 1.00 40.46  ? 475  ASN D ND2   1 
ATOM   5998  N  N     . ASN B  1  68  ? -0.172  63.480  28.286 1.00 55.08  ? 476  ASN D N     1 
ATOM   5999  C  CA    . ASN B  1  68  ? 1.152   63.206  27.722 1.00 59.67  ? 476  ASN D CA    1 
ATOM   6000  C  C     . ASN B  1  68  ? 1.181   62.252  26.559 1.00 58.26  ? 476  ASN D C     1 
ATOM   6001  O  O     . ASN B  1  68  ? 1.913   62.456  25.626 1.00 51.16  ? 476  ASN D O     1 
ATOM   6002  C  CB    . ASN B  1  68  ? 2.135   62.817  28.814 1.00 64.59  ? 476  ASN D CB    1 
ATOM   6003  C  CG    . ASN B  1  68  ? 2.369   63.963  29.777 1.00 77.03  ? 476  ASN D CG    1 
ATOM   6004  O  OD1   . ASN B  1  68  ? 2.072   65.119  29.470 1.00 89.63  ? 476  ASN D OD1   1 
ATOM   6005  N  ND2   . ASN B  1  68  ? 2.888   63.658  30.948 1.00 89.03  ? 476  ASN D ND2   1 
ATOM   6006  N  N     . GLU B  1  69  ? 0.379   61.204  26.618 1.00 51.47  ? 477  GLU D N     1 
ATOM   6007  C  CA    . GLU B  1  69  ? 0.357   60.259  25.546 1.00 52.63  ? 477  GLU D CA    1 
ATOM   6008  C  C     . GLU B  1  69  ? -0.201  60.871  24.277 1.00 49.87  ? 477  GLU D C     1 
ATOM   6009  O  O     . GLU B  1  69  ? 0.312   60.617  23.227 1.00 53.93  ? 477  GLU D O     1 
ATOM   6010  C  CB    . GLU B  1  69  ? -0.472  59.071  25.967 1.00 52.48  ? 477  GLU D CB    1 
ATOM   6011  C  CG    . GLU B  1  69  ? 0.373   57.882  26.265 1.00 63.23  ? 477  GLU D CG    1 
ATOM   6012  C  CD    . GLU B  1  69  ? 1.458   58.145  27.301 1.00 71.39  ? 477  GLU D CD    1 
ATOM   6013  O  OE1   . GLU B  1  69  ? 1.177   58.741  28.363 1.00 87.58  ? 477  GLU D OE1   1 
ATOM   6014  O  OE2   . GLU B  1  69  ? 2.606   57.745  27.062 1.00 66.97  ? 477  GLU D OE2   1 
ATOM   6015  N  N     . ILE B  1  70  ? -1.224  61.694  24.402 1.00 48.47  ? 478  ILE D N     1 
ATOM   6016  C  CA    . ILE B  1  70  ? -1.791  62.373  23.277 1.00 46.16  ? 478  ILE D CA    1 
ATOM   6017  C  C     . ILE B  1  70  ? -0.821  63.343  22.631 1.00 46.20  ? 478  ILE D C     1 
ATOM   6018  O  O     . ILE B  1  70  ? -0.773  63.439  21.422 1.00 43.06  ? 478  ILE D O     1 
ATOM   6019  C  CB    . ILE B  1  70  ? -3.044  63.137  23.727 1.00 46.91  ? 478  ILE D CB    1 
ATOM   6020  C  CG1   . ILE B  1  70  ? -4.142  62.159  24.159 1.00 44.28  ? 478  ILE D CG1   1 
ATOM   6021  C  CG2   . ILE B  1  70  ? -3.563  64.016  22.627 1.00 44.62  ? 478  ILE D CG2   1 
ATOM   6022  C  CD1   . ILE B  1  70  ? -4.835  61.433  23.020 1.00 38.72  ? 478  ILE D CD1   1 
ATOM   6023  N  N     . ARG B  1  71  ? -0.063  64.068  23.435 1.00 50.12  ? 479  ARG D N     1 
ATOM   6024  C  CA    . ARG B  1  71  ? 0.869   65.054  22.918 1.00 52.62  ? 479  ARG D CA    1 
ATOM   6025  C  C     . ARG B  1  71  ? 1.955   64.400  22.117 1.00 50.83  ? 479  ARG D C     1 
ATOM   6026  O  O     . ARG B  1  71  ? 2.398   64.943  21.137 1.00 51.00  ? 479  ARG D O     1 
ATOM   6027  C  CB    . ARG B  1  71  ? 1.545   65.786  24.045 1.00 51.14  ? 479  ARG D CB    1 
ATOM   6028  C  CG    . ARG B  1  71  ? 0.619   66.639  24.845 1.00 60.06  ? 479  ARG D CG    1 
ATOM   6029  C  CD    . ARG B  1  71  ? 1.430   67.276  25.930 1.00 73.00  ? 479  ARG D CD    1 
ATOM   6030  N  NE    . ARG B  1  71  ? 1.040   68.667  26.090 1.00 89.99  ? 479  ARG D NE    1 
ATOM   6031  C  CZ    . ARG B  1  71  ? 1.420   69.453  27.094 1.00 99.05  ? 479  ARG D CZ    1 
ATOM   6032  N  NH1   . ARG B  1  71  ? 2.213   68.993  28.065 1.00 100.97 ? 479  ARG D NH1   1 
ATOM   6033  N  NH2   . ARG B  1  71  ? 0.998   70.711  27.122 1.00 98.93  ? 479  ARG D NH2   1 
ATOM   6034  N  N     . GLN B  1  72  ? 2.395   63.243  22.584 1.00 49.89  ? 480  GLN D N     1 
ATOM   6035  C  CA    . GLN B  1  72  ? 3.520   62.584  21.990 1.00 54.12  ? 480  GLN D CA    1 
ATOM   6036  C  C     . GLN B  1  72  ? 3.179   62.114  20.602 1.00 52.40  ? 480  GLN D C     1 
ATOM   6037  O  O     . GLN B  1  72  ? 4.042   62.129  19.746 1.00 52.56  ? 480  GLN D O     1 
ATOM   6038  C  CB    . GLN B  1  72  ? 3.960   61.420  22.849 1.00 55.49  ? 480  GLN D CB    1 
ATOM   6039  C  CG    . GLN B  1  72  ? 5.136   61.750  23.727 1.00 65.83  ? 480  GLN D CG    1 
ATOM   6040  C  CD    . GLN B  1  72  ? 5.336   60.728  24.838 1.00 76.22  ? 480  GLN D CD    1 
ATOM   6041  O  OE1   . GLN B  1  72  ? 5.187   59.528  24.629 1.00 84.33  ? 480  GLN D OE1   1 
ATOM   6042  N  NE2   . GLN B  1  72  ? 5.692   61.199  26.023 1.00 82.91  ? 480  GLN D NE2   1 
ATOM   6043  N  N     . MET B  1  73  ? 1.927   61.701  20.411 1.00 49.37  ? 481  MET D N     1 
ATOM   6044  C  CA    . MET B  1  73  ? 1.463   61.308  19.105 1.00 50.24  ? 481  MET D CA    1 
ATOM   6045  C  C     . MET B  1  73  ? 1.410   62.518  18.191 1.00 51.57  ? 481  MET D C     1 
ATOM   6046  O  O     . MET B  1  73  ? 1.804   62.425  17.050 1.00 63.64  ? 481  MET D O     1 
ATOM   6047  C  CB    . MET B  1  73  ? 0.098   60.635  19.160 1.00 43.41  ? 481  MET D CB    1 
ATOM   6048  C  CG    . MET B  1  73  ? 0.164   59.235  19.707 1.00 47.23  ? 481  MET D CG    1 
ATOM   6049  S  SD    . MET B  1  73  ? -1.332  58.235  19.451 1.00 44.34  ? 481  MET D SD    1 
ATOM   6050  C  CE    . MET B  1  73  ? -2.356  59.028  20.679 1.00 42.18  ? 481  MET D CE    1 
ATOM   6051  N  N     . ILE B  1  74  ? 0.912   63.633  18.699 1.00 53.48  ? 482  ILE D N     1 
ATOM   6052  C  CA    . ILE B  1  74  ? 0.729   64.811  17.885 1.00 54.50  ? 482  ILE D CA    1 
ATOM   6053  C  C     . ILE B  1  74  ? 2.090   65.316  17.429 1.00 56.83  ? 482  ILE D C     1 
ATOM   6054  O  O     . ILE B  1  74  ? 2.280   65.674  16.283 1.00 60.53  ? 482  ILE D O     1 
ATOM   6055  C  CB    . ILE B  1  74  ? 0.051   65.911  18.701 1.00 59.22  ? 482  ILE D CB    1 
ATOM   6056  C  CG1   . ILE B  1  74  ? -1.410  65.611  18.939 1.00 51.15  ? 482  ILE D CG1   1 
ATOM   6057  C  CG2   . ILE B  1  74  ? 0.159   67.268  18.017 1.00 54.50  ? 482  ILE D CG2   1 
ATOM   6058  C  CD1   . ILE B  1  74  ? -1.962  66.452  20.061 1.00 52.21  ? 482  ILE D CD1   1 
ATOM   6059  N  N     . THR B  1  75  ? 3.034   65.322  18.347 1.00 47.57  ? 483  THR D N     1 
ATOM   6060  C  CA    . THR B  1  75  ? 4.359   65.733  18.045 1.00 48.89  ? 483  THR D CA    1 
ATOM   6061  C  C     . THR B  1  75  ? 5.013   64.793  17.067 1.00 54.72  ? 483  THR D C     1 
ATOM   6062  O  O     . THR B  1  75  ? 5.777   65.215  16.248 1.00 57.59  ? 483  THR D O     1 
ATOM   6063  C  CB    . THR B  1  75  ? 5.149   65.674  19.328 1.00 46.43  ? 483  THR D CB    1 
ATOM   6064  O  OG1   . THR B  1  75  ? 4.596   66.627  20.229 1.00 50.48  ? 483  THR D OG1   1 
ATOM   6065  C  CG2   . THR B  1  75  ? 6.583   65.947  19.114 1.00 48.59  ? 483  THR D CG2   1 
ATOM   6066  N  N     . ALA B  1  76  ? 4.768   63.504  17.201 1.00 57.11  ? 484  ALA D N     1 
ATOM   6067  C  CA    . ALA B  1  76  ? 5.347   62.534  16.300 1.00 55.27  ? 484  ALA D CA    1 
ATOM   6068  C  C     . ALA B  1  76  ? 4.770   62.614  14.892 1.00 58.66  ? 484  ALA D C     1 
ATOM   6069  O  O     . ALA B  1  76  ? 5.474   62.431  13.921 1.00 57.44  ? 484  ALA D O     1 
ATOM   6070  C  CB    . ALA B  1  76  ? 5.127   61.141  16.863 1.00 57.02  ? 484  ALA D CB    1 
ATOM   6071  N  N     . PHE B  1  77  ? 3.464   62.810  14.796 1.00 58.75  ? 485  PHE D N     1 
ATOM   6072  C  CA    . PHE B  1  77  ? 2.816   62.840  13.498 1.00 67.35  ? 485  PHE D CA    1 
ATOM   6073  C  C     . PHE B  1  77  ? 3.232   64.123  12.800 1.00 71.52  ? 485  PHE D C     1 
ATOM   6074  O  O     . PHE B  1  77  ? 3.563   64.116  11.625 1.00 68.88  ? 485  PHE D O     1 
ATOM   6075  C  CB    . PHE B  1  77  ? 1.296   62.734  13.637 1.00 64.25  ? 485  PHE D CB    1 
ATOM   6076  C  CG    . PHE B  1  77  ? 0.817   61.455  14.274 1.00 65.64  ? 485  PHE D CG    1 
ATOM   6077  C  CD1   . PHE B  1  77  ? 1.680   60.384  14.524 1.00 59.38  ? 485  PHE D CD1   1 
ATOM   6078  C  CD2   . PHE B  1  77  ? -0.538  61.313  14.600 1.00 63.09  ? 485  PHE D CD2   1 
ATOM   6079  C  CE1   . PHE B  1  77  ? 1.191   59.231  15.110 1.00 60.49  ? 485  PHE D CE1   1 
ATOM   6080  C  CE2   . PHE B  1  77  ? -1.024  60.159  15.173 1.00 56.19  ? 485  PHE D CE2   1 
ATOM   6081  C  CZ    . PHE B  1  77  ? -0.158  59.118  15.435 1.00 54.65  ? 485  PHE D CZ    1 
ATOM   6082  N  N     . GLY B  1  78  ? 3.273   65.210  13.563 1.00 73.16  ? 486  GLY D N     1 
ATOM   6083  C  CA    . GLY B  1  78  ? 3.783   66.462  13.057 1.00 76.22  ? 486  GLY D CA    1 
ATOM   6084  C  C     . GLY B  1  78  ? 2.761   67.334  12.371 1.00 76.02  ? 486  GLY D C     1 
ATOM   6085  O  O     . GLY B  1  78  ? 3.105   68.423  11.928 1.00 78.88  ? 486  GLY D O     1 
ATOM   6086  N  N     . THR B  1  79  ? 1.507   66.909  12.355 1.00 68.80  ? 487  THR D N     1 
ATOM   6087  C  CA    . THR B  1  79  ? 0.493   67.640  11.640 1.00 69.67  ? 487  THR D CA    1 
ATOM   6088  C  C     . THR B  1  79  ? -0.282  68.648  12.452 1.00 72.27  ? 487  THR D C     1 
ATOM   6089  O  O     . THR B  1  79  ? -1.077  69.371  11.870 1.00 73.65  ? 487  THR D O     1 
ATOM   6090  C  CB    . THR B  1  79  ? -0.567  66.692  11.115 1.00 62.75  ? 487  THR D CB    1 
ATOM   6091  O  OG1   . THR B  1  79  ? -1.293  66.213  12.242 1.00 73.51  ? 487  THR D OG1   1 
ATOM   6092  C  CG2   . THR B  1  79  ? 0.059   65.556  10.479 1.00 60.48  ? 487  THR D CG2   1 
ATOM   6093  N  N     . GLY B  1  80  ? -0.144  68.642  13.781 1.00 68.19  ? 488  GLY D N     1 
ATOM   6094  C  CA    . GLY B  1  80  ? -0.999  69.451  14.633 1.00 66.31  ? 488  GLY D CA    1 
ATOM   6095  C  C     . GLY B  1  80  ? -2.415  68.882  14.659 1.00 74.11  ? 488  GLY D C     1 
ATOM   6096  O  O     . GLY B  1  80  ? -2.702  67.870  14.026 1.00 69.90  ? 488  GLY D O     1 
ATOM   6097  N  N     . ILE B  1  81  ? -3.298  69.520  15.413 1.00 82.56  ? 489  ILE D N     1 
ATOM   6098  C  CA    . ILE B  1  81  ? -4.652  68.980  15.646 1.00 78.54  ? 489  ILE D CA    1 
ATOM   6099  C  C     . ILE B  1  81  ? -5.769  69.966  15.387 1.00 82.39  ? 489  ILE D C     1 
ATOM   6100  O  O     . ILE B  1  81  ? -5.581  71.186  15.504 1.00 83.69  ? 489  ILE D O     1 
ATOM   6101  C  CB    . ILE B  1  81  ? -4.830  68.474  17.087 1.00 72.17  ? 489  ILE D CB    1 
ATOM   6102  C  CG1   . ILE B  1  81  ? -4.179  69.458  18.061 1.00 65.56  ? 489  ILE D CG1   1 
ATOM   6103  C  CG2   . ILE B  1  81  ? -4.249  67.087  17.235 1.00 68.69  ? 489  ILE D CG2   1 
ATOM   6104  C  CD1   . ILE B  1  81  ? -4.991  69.748  19.309 1.00 61.63  ? 489  ILE D CD1   1 
ATOM   6105  N  N     . GLY B  1  82  ? -6.950  69.415  15.098 1.00 78.83  ? 490  GLY D N     1 
ATOM   6106  C  CA    . GLY B  1  82  ? -8.148  70.194  14.810 1.00 86.35  ? 490  GLY D CA    1 
ATOM   6107  C  C     . GLY B  1  82  ? -7.989  71.142  13.628 1.00 90.39  ? 490  GLY D C     1 
ATOM   6108  O  O     . GLY B  1  82  ? -7.613  70.717  12.520 1.00 81.52  ? 490  GLY D O     1 
ATOM   6109  N  N     . GLY B  1  83  ? -8.286  72.422  13.885 1.00 88.99  ? 491  GLY D N     1 
ATOM   6110  C  CA    . GLY B  1  83  ? -8.245  73.475  12.877 1.00 82.88  ? 491  GLY D CA    1 
ATOM   6111  C  C     . GLY B  1  83  ? -6.887  73.629  12.222 1.00 84.24  ? 491  GLY D C     1 
ATOM   6112  O  O     . GLY B  1  83  ? -6.794  73.834  11.018 1.00 89.54  ? 491  GLY D O     1 
ATOM   6113  N  N     . ASP B  1  84  ? -5.826  73.501  13.013 1.00 84.04  ? 492  ASP D N     1 
ATOM   6114  C  CA    . ASP B  1  84  ? -4.458  73.686  12.518 1.00 76.94  ? 492  ASP D CA    1 
ATOM   6115  C  C     . ASP B  1  84  ? -3.890  72.436  11.868 1.00 77.27  ? 492  ASP D C     1 
ATOM   6116  O  O     . ASP B  1  84  ? -2.763  72.455  11.377 1.00 74.68  ? 492  ASP D O     1 
ATOM   6117  C  CB    . ASP B  1  84  ? -3.550  74.157  13.648 1.00 74.42  ? 492  ASP D CB    1 
ATOM   6118  C  CG    . ASP B  1  84  ? -4.242  75.150  14.563 1.00 81.23  ? 492  ASP D CG    1 
ATOM   6119  O  OD1   . ASP B  1  84  ? -5.487  75.244  14.510 1.00 80.74  ? 492  ASP D OD1   1 
ATOM   6120  O  OD2   . ASP B  1  84  ? -3.561  75.836  15.338 1.00 80.80  ? 492  ASP D OD2   1 
ATOM   6121  N  N     . PHE B  1  85  ? -4.655  71.355  11.831 1.00 75.19  ? 493  PHE D N     1 
ATOM   6122  C  CA    . PHE B  1  85  ? -4.165  70.138  11.273 1.00 72.21  ? 493  PHE D CA    1 
ATOM   6123  C  C     . PHE B  1  85  ? -3.684  70.440  9.880  1.00 76.36  ? 493  PHE D C     1 
ATOM   6124  O  O     . PHE B  1  85  ? -4.383  71.115  9.155  1.00 92.43  ? 493  PHE D O     1 
ATOM   6125  C  CB    . PHE B  1  85  ? -5.291  69.157  11.171 1.00 69.87  ? 493  PHE D CB    1 
ATOM   6126  C  CG    . PHE B  1  85  ? -4.858  67.854  10.668 1.00 77.58  ? 493  PHE D CG    1 
ATOM   6127  C  CD1   . PHE B  1  85  ? -4.224  66.951  11.521 1.00 85.72  ? 493  PHE D CD1   1 
ATOM   6128  C  CD2   . PHE B  1  85  ? -5.011  67.526  9.340  1.00 79.43  ? 493  PHE D CD2   1 
ATOM   6129  C  CE1   . PHE B  1  85  ? -3.787  65.724  11.048 1.00 86.86  ? 493  PHE D CE1   1 
ATOM   6130  C  CE2   . PHE B  1  85  ? -4.563  66.308  8.877  1.00 85.97  ? 493  PHE D CE2   1 
ATOM   6131  C  CZ    . PHE B  1  85  ? -3.953  65.404  9.724  1.00 83.00  ? 493  PHE D CZ    1 
ATOM   6132  N  N     . ASP B  1  86  ? -2.488  69.988  9.523  1.00 78.94  ? 494  ASP D N     1 
ATOM   6133  C  CA    . ASP B  1  86  ? -1.975  70.179  8.182  1.00 70.91  ? 494  ASP D CA    1 
ATOM   6134  C  C     . ASP B  1  86  ? -1.520  68.859  7.648  1.00 63.32  ? 494  ASP D C     1 
ATOM   6135  O  O     . ASP B  1  86  ? -0.485  68.387  8.066  1.00 60.46  ? 494  ASP D O     1 
ATOM   6136  C  CB    . ASP B  1  86  ? -0.759  71.095  8.231  1.00 74.33  ? 494  ASP D CB    1 
ATOM   6137  C  CG    . ASP B  1  86  ? -0.395  71.641  6.879  1.00 80.30  ? 494  ASP D CG    1 
ATOM   6138  O  OD1   . ASP B  1  86  ? -1.012  71.266  5.856  1.00 75.58  ? 494  ASP D OD1   1 
ATOM   6139  O  OD2   . ASP B  1  86  ? 0.539   72.457  6.840  1.00 87.55  ? 494  ASP D OD2   1 
ATOM   6140  N  N     . LEU B  1  87  ? -2.219  68.291  6.681  1.00 58.13  ? 495  LEU D N     1 
ATOM   6141  C  CA    . LEU B  1  87  ? -1.850  66.969  6.209  1.00 61.58  ? 495  LEU D CA    1 
ATOM   6142  C  C     . LEU B  1  87  ? -0.483  66.924  5.566  1.00 67.31  ? 495  LEU D C     1 
ATOM   6143  O  O     . LEU B  1  87  ? 0.214   65.922  5.628  1.00 62.91  ? 495  LEU D O     1 
ATOM   6144  C  CB    . LEU B  1  87  ? -2.868  66.436  5.225  1.00 59.28  ? 495  LEU D CB    1 
ATOM   6145  C  CG    . LEU B  1  87  ? -2.594  65.000  4.762  1.00 59.57  ? 495  LEU D CG    1 
ATOM   6146  C  CD1   . LEU B  1  87  ? -2.749  64.000  5.899  1.00 68.54  ? 495  LEU D CD1   1 
ATOM   6147  C  CD2   . LEU B  1  87  ? -3.568  64.675  3.649  1.00 63.81  ? 495  LEU D CD2   1 
ATOM   6148  N  N     . ALA B  1  88  ? -0.101  68.021  4.947  1.00 73.38  ? 496  ALA D N     1 
ATOM   6149  C  CA    . ALA B  1  88  ? 1.098   68.017  4.166  1.00 71.53  ? 496  ALA D CA    1 
ATOM   6150  C  C     . ALA B  1  88  ? 2.291   67.949  5.103  1.00 73.12  ? 496  ALA D C     1 
ATOM   6151  O  O     . ALA B  1  88  ? 3.380   67.525  4.704  1.00 75.16  ? 496  ALA D O     1 
ATOM   6152  C  CB    . ALA B  1  88  ? 1.136   69.243  3.293  1.00 69.40  ? 496  ALA D CB    1 
ATOM   6153  N  N     . LYS B  1  89  ? 2.068   68.331  6.358  1.00 70.59  ? 497  LYS D N     1 
ATOM   6154  C  CA    . LYS B  1  89  ? 3.132   68.321  7.340  1.00 71.15  ? 497  LYS D CA    1 
ATOM   6155  C  C     . LYS B  1  89  ? 3.345   66.968  8.050  1.00 72.36  ? 497  LYS D C     1 
ATOM   6156  O  O     . LYS B  1  89  ? 4.208   66.873  8.920  1.00 64.42  ? 497  LYS D O     1 
ATOM   6157  C  CB    . LYS B  1  89  ? 2.881   69.398  8.370  1.00 65.28  ? 497  LYS D CB    1 
ATOM   6158  C  CG    . LYS B  1  89  ? 3.347   70.754  7.941  1.00 70.02  ? 497  LYS D CG    1 
ATOM   6159  C  CD    . LYS B  1  89  ? 3.726   71.573  9.148  1.00 80.00  ? 497  LYS D CD    1 
ATOM   6160  C  CE    . LYS B  1  89  ? 3.876   73.027  8.764  1.00 82.18  ? 497  LYS D CE    1 
ATOM   6161  N  NZ    . LYS B  1  89  ? 3.966   73.804  10.010 1.00 85.34  ? 497  LYS D NZ    1 
ATOM   6162  N  N     . ALA B  1  90  ? 2.573   65.949  7.675  1.00 61.88  ? 498  ALA D N     1 
ATOM   6163  C  CA    . ALA B  1  90  ? 2.707   64.626  8.269  1.00 62.22  ? 498  ALA D CA    1 
ATOM   6164  C  C     . ALA B  1  90  ? 4.101   64.084  8.077  1.00 61.65  ? 498  ALA D C     1 
ATOM   6165  O  O     . ALA B  1  90  ? 4.678   64.234  7.007  1.00 72.16  ? 498  ALA D O     1 
ATOM   6166  C  CB    . ALA B  1  90  ? 1.716   63.686  7.654  1.00 49.09  ? 498  ALA D CB    1 
ATOM   6167  N  N     . ARG B  1  91  ? 4.636   63.453  9.116  1.00 62.77  ? 499  ARG D N     1 
ATOM   6168  C  CA    . ARG B  1  91  ? 5.992   62.916  9.057  1.00 55.09  ? 499  ARG D CA    1 
ATOM   6169  C  C     . ARG B  1  91  ? 6.025   61.453  8.629  1.00 49.72  ? 499  ARG D C     1 
ATOM   6170  O  O     . ARG B  1  91  ? 7.091   60.926  8.390  1.00 49.25  ? 499  ARG D O     1 
ATOM   6171  C  CB    . ARG B  1  91  ? 6.698   63.116  10.381 1.00 56.13  ? 499  ARG D CB    1 
ATOM   6172  C  CG    . ARG B  1  91  ? 6.696   64.550  10.864 1.00 54.57  ? 499  ARG D CG    1 
ATOM   6173  C  CD    . ARG B  1  91  ? 7.863   64.892  11.794 1.00 66.54  ? 499  ARG D CD    1 
ATOM   6174  N  NE    . ARG B  1  91  ? 8.081   63.875  12.815 1.00 74.92  ? 499  ARG D NE    1 
ATOM   6175  C  CZ    . ARG B  1  91  ? 9.121   63.039  12.869 1.00 75.01  ? 499  ARG D CZ    1 
ATOM   6176  N  NH1   . ARG B  1  91  ? 10.111  63.082  11.974 1.00 76.97  ? 499  ARG D NH1   1 
ATOM   6177  N  NH2   . ARG B  1  91  ? 9.158   62.144  13.848 1.00 74.31  ? 499  ARG D NH2   1 
ATOM   6178  N  N     . TYR B  1  92  ? 4.856   60.827  8.507  1.00 48.35  ? 500  TYR D N     1 
ATOM   6179  C  CA    . TYR B  1  92  ? 4.743   59.427  8.102  1.00 55.29  ? 500  TYR D CA    1 
ATOM   6180  C  C     . TYR B  1  92  ? 3.469   59.323  7.315  1.00 58.44  ? 500  TYR D C     1 
ATOM   6181  O  O     . TYR B  1  92  ? 2.447   59.877  7.688  1.00 67.77  ? 500  TYR D O     1 
ATOM   6182  C  CB    . TYR B  1  92  ? 4.656   58.466  9.310  1.00 49.10  ? 500  TYR D CB    1 
ATOM   6183  C  CG    . TYR B  1  92  ? 5.646   58.730  10.407 1.00 47.72  ? 500  TYR D CG    1 
ATOM   6184  C  CD1   . TYR B  1  92  ? 5.353   59.624  11.449 1.00 47.76  ? 500  TYR D CD1   1 
ATOM   6185  C  CD2   . TYR B  1  92  ? 6.877   58.122  10.390 1.00 45.56  ? 500  TYR D CD2   1 
ATOM   6186  C  CE1   . TYR B  1  92  ? 6.271   59.875  12.440 1.00 45.61  ? 500  TYR D CE1   1 
ATOM   6187  C  CE2   . TYR B  1  92  ? 7.812   58.371  11.384 1.00 46.84  ? 500  TYR D CE2   1 
ATOM   6188  C  CZ    . TYR B  1  92  ? 7.501   59.245  12.411 1.00 46.55  ? 500  TYR D CZ    1 
ATOM   6189  O  OH    . TYR B  1  92  ? 8.419   59.515  13.401 1.00 51.01  ? 500  TYR D OH    1 
ATOM   6190  N  N     . HIS B  1  93  ? 3.527   58.617  6.196  1.00 57.89  ? 501  HIS D N     1 
ATOM   6191  C  CA    . HIS B  1  93  ? 2.352   58.432  5.363  1.00 59.47  ? 501  HIS D CA    1 
ATOM   6192  C  C     . HIS B  1  93  ? 1.620   57.175  5.787  1.00 60.20  ? 501  HIS D C     1 
ATOM   6193  O  O     . HIS B  1  93  ? 0.525   56.886  5.305  1.00 59.99  ? 501  HIS D O     1 
ATOM   6194  C  CB    . HIS B  1  93  ? 2.771   58.400  3.897  1.00 67.14  ? 501  HIS D CB    1 
ATOM   6195  C  CG    . HIS B  1  93  ? 2.807   59.754  3.262  1.00 72.44  ? 501  HIS D CG    1 
ATOM   6196  N  ND1   . HIS B  1  93  ? 2.159   60.042  2.078  1.00 67.41  ? 501  HIS D ND1   1 
ATOM   6197  C  CD2   . HIS B  1  93  ? 3.398   60.902  3.664  1.00 68.02  ? 501  HIS D CD2   1 
ATOM   6198  C  CE1   . HIS B  1  93  ? 2.359   61.313  1.782  1.00 74.85  ? 501  HIS D CE1   1 
ATOM   6199  N  NE2   . HIS B  1  93  ? 3.102   61.857  2.730  1.00 68.29  ? 501  HIS D NE2   1 
ATOM   6200  N  N     . LYS B  1  94  ? 2.230   56.435  6.703  1.00 57.95  ? 502  LYS D N     1 
ATOM   6201  C  CA    . LYS B  1  94  ? 1.624   55.240  7.280  1.00 57.89  ? 502  LYS D CA    1 
ATOM   6202  C  C     . LYS B  1  94  ? 1.673   55.351  8.805  1.00 51.15  ? 502  LYS D C     1 
ATOM   6203  O  O     . LYS B  1  94  ? 2.737   55.480  9.372  1.00 49.37  ? 502  LYS D O     1 
ATOM   6204  C  CB    . LYS B  1  94  ? 2.413   54.032  6.846  1.00 57.59  ? 502  LYS D CB    1 
ATOM   6205  C  CG    . LYS B  1  94  ? 1.613   52.882  6.303  1.00 55.86  ? 502  LYS D CG    1 
ATOM   6206  C  CD    . LYS B  1  94  ? 1.777   52.843  4.806  1.00 54.17  ? 502  LYS D CD    1 
ATOM   6207  C  CE    . LYS B  1  94  ? 1.701   51.442  4.278  1.00 48.81  ? 502  LYS D CE    1 
ATOM   6208  N  NZ    . LYS B  1  94  ? 2.300   51.393  2.932  1.00 56.02  ? 502  LYS D NZ    1 
ATOM   6209  N  N     . ILE B  1  95  ? 0.527   55.340  9.459  1.00 51.24  ? 503  ILE D N     1 
ATOM   6210  C  CA    . ILE B  1  95  ? 0.451   55.351  10.922 1.00 49.03  ? 503  ILE D CA    1 
ATOM   6211  C  C     . ILE B  1  95  ? -0.194  53.999  11.202 1.00 47.37  ? 503  ILE D C     1 
ATOM   6212  O  O     . ILE B  1  95  ? -1.323  53.744  10.792 1.00 46.73  ? 503  ILE D O     1 
ATOM   6213  C  CB    . ILE B  1  95  ? -0.417  56.515  11.435 1.00 49.04  ? 503  ILE D CB    1 
ATOM   6214  C  CG1   . ILE B  1  95  ? 0.314   57.856  11.325 1.00 51.62  ? 503  ILE D CG1   1 
ATOM   6215  C  CG2   . ILE B  1  95  ? -0.821  56.329  12.882 1.00 43.47  ? 503  ILE D CG2   1 
ATOM   6216  C  CD1   . ILE B  1  95  ? 0.408   58.418  9.936  1.00 53.52  ? 503  ILE D CD1   1 
ATOM   6217  N  N     . VAL B  1  96  ? 0.526   53.119  11.855 1.00 44.93  ? 504  VAL D N     1 
ATOM   6218  C  CA    . VAL B  1  96  ? 0.031   51.737  12.043 1.00 46.78  ? 504  VAL D CA    1 
ATOM   6219  C  C     . VAL B  1  96  ? -0.280  51.423  13.511 1.00 43.56  ? 504  VAL D C     1 
ATOM   6220  O  O     . VAL B  1  96  ? 0.594   51.542  14.376 1.00 47.25  ? 504  VAL D O     1 
ATOM   6221  C  CB    . VAL B  1  96  ? 1.044   50.685  11.556 1.00 45.44  ? 504  VAL D CB    1 
ATOM   6222  C  CG1   . VAL B  1  96  ? 0.378   49.322  11.540 1.00 43.57  ? 504  VAL D CG1   1 
ATOM   6223  C  CG2   . VAL B  1  96  ? 1.582   51.049  10.189 1.00 42.37  ? 504  VAL D CG2   1 
ATOM   6224  N  N     . ILE B  1  97  ? -1.511  50.997  13.775 1.00 37.88  ? 505  ILE D N     1 
ATOM   6225  C  CA    . ILE B  1  97  ? -1.913  50.614  15.102 1.00 37.74  ? 505  ILE D CA    1 
ATOM   6226  C  C     . ILE B  1  97  ? -1.582  49.148  15.302 1.00 38.80  ? 505  ILE D C     1 
ATOM   6227  O  O     . ILE B  1  97  ? -2.149  48.288  14.637 1.00 41.86  ? 505  ILE D O     1 
ATOM   6228  C  CB    . ILE B  1  97  ? -3.398  50.876  15.331 1.00 39.54  ? 505  ILE D CB    1 
ATOM   6229  C  CG1   . ILE B  1  97  ? -3.665  52.395  15.224 1.00 42.89  ? 505  ILE D CG1   1 
ATOM   6230  C  CG2   . ILE B  1  97  ? -3.819  50.364  16.724 1.00 39.93  ? 505  ILE D CG2   1 
ATOM   6231  C  CD1   . ILE B  1  97  ? -5.130  52.729  14.963 1.00 40.30  ? 505  ILE D CD1   1 
ATOM   6232  N  N     . MET B  1  98  ? -0.665  48.872  16.215 1.00 38.33  ? 506  MET D N     1 
ATOM   6233  C  CA    . MET B  1  98  ? -0.244  47.513  16.492 1.00 39.04  ? 506  MET D CA    1 
ATOM   6234  C  C     . MET B  1  98  ? -0.386  47.178  17.969 1.00 42.73  ? 506  MET D C     1 
ATOM   6235  O  O     . MET B  1  98  ? 0.600   47.099  18.711 1.00 44.19  ? 506  MET D O     1 
ATOM   6236  C  CB    . MET B  1  98  ? 1.197   47.319  16.060 1.00 39.08  ? 506  MET D CB    1 
ATOM   6237  C  CG    . MET B  1  98  ? 1.577   45.858  15.912 1.00 41.45  ? 506  MET D CG    1 
ATOM   6238  S  SD    . MET B  1  98  ? 3.058   45.594  14.912 1.00 50.39  ? 506  MET D SD    1 
ATOM   6239  C  CE    . MET B  1  98  ? 4.378   46.279  15.871 1.00 39.76  ? 506  MET D CE    1 
ATOM   6240  N  N     . THR B  1  99  ? -1.620  46.976  18.395 1.00 41.82  ? 507  THR D N     1 
ATOM   6241  C  CA    . THR B  1  99  ? -1.895  46.620  19.789 1.00 44.07  ? 507  THR D CA    1 
ATOM   6242  C  C     . THR B  1  99  ? -1.823  45.091  19.898 1.00 42.60  ? 507  THR D C     1 
ATOM   6243  O  O     . THR B  1  99  ? -1.706  44.419  18.881 1.00 45.33  ? 507  THR D O     1 
ATOM   6244  C  CB    . THR B  1  99  ? -3.303  47.095  20.203 1.00 47.09  ? 507  THR D CB    1 
ATOM   6245  O  OG1   . THR B  1  99  ? -4.270  46.408  19.401 1.00 47.55  ? 507  THR D OG1   1 
ATOM   6246  C  CG2   . THR B  1  99  ? -3.446  48.564  20.017 1.00 43.72  ? 507  THR D CG2   1 
ATOM   6247  N  N     . ASP B  1  100 ? -1.946  44.556  21.105 1.00 44.60  ? 508  ASP D N     1 
ATOM   6248  C  CA    . ASP B  1  100 ? -1.968  43.101  21.301 1.00 45.46  ? 508  ASP D CA    1 
ATOM   6249  C  C     . ASP B  1  100 ? -3.220  42.521  20.675 1.00 48.23  ? 508  ASP D C     1 
ATOM   6250  O  O     . ASP B  1  100 ? -4.271  43.166  20.615 1.00 42.49  ? 508  ASP D O     1 
ATOM   6251  C  CB    . ASP B  1  100 ? -1.939  42.740  22.787 1.00 53.92  ? 508  ASP D CB    1 
ATOM   6252  C  CG    . ASP B  1  100 ? -0.602  42.991  23.440 1.00 57.59  ? 508  ASP D CG    1 
ATOM   6253  O  OD1   . ASP B  1  100 ? 0.364   43.509  22.810 1.00 62.03  ? 508  ASP D OD1   1 
ATOM   6254  O  OD2   . ASP B  1  100 ? -0.489  42.632  24.617 1.00 63.89  ? 508  ASP D OD2   1 
ATOM   6255  N  N     . ALA B  1  101 ? -3.090  41.317  20.145 1.00 46.86  ? 509  ALA D N     1 
ATOM   6256  C  CA    . ALA B  1  101 ? -4.201  40.629  19.529 1.00 48.21  ? 509  ALA D CA    1 
ATOM   6257  C  C     . ALA B  1  101 ? -5.104  40.021  20.606 1.00 49.07  ? 509  ALA D C     1 
ATOM   6258  O  O     . ALA B  1  101 ? -5.276  38.803  20.660 1.00 52.35  ? 509  ALA D O     1 
ATOM   6259  C  CB    . ALA B  1  101 ? -3.680  39.551  18.609 1.00 45.19  ? 509  ALA D CB    1 
ATOM   6260  N  N     . ASP B  1  102 ? -5.657  40.858  21.455 1.00 40.37  ? 510  ASP D N     1 
ATOM   6261  C  CA    . ASP B  1  102 ? -6.547  40.395  22.472 1.00 42.75  ? 510  ASP D CA    1 
ATOM   6262  C  C     . ASP B  1  102 ? -7.599  41.479  22.750 1.00 42.26  ? 510  ASP D C     1 
ATOM   6263  O  O     . ASP B  1  102 ? -7.582  42.511  22.092 1.00 44.28  ? 510  ASP D O     1 
ATOM   6264  C  CB    . ASP B  1  102 ? -5.743  39.952  23.698 1.00 34.87  ? 510  ASP D CB    1 
ATOM   6265  C  CG    . ASP B  1  102 ? -4.927  41.045  24.286 1.00 40.62  ? 510  ASP D CG    1 
ATOM   6266  O  OD1   . ASP B  1  102 ? -5.166  42.253  24.090 1.00 40.30  ? 510  ASP D OD1   1 
ATOM   6267  O  OD2   . ASP B  1  102 ? -4.018  40.707  25.034 1.00 45.44  ? 510  ASP D OD2   1 
ATOM   6268  N  N     . VAL B  1  103 ? -8.532  41.213  23.657 1.00 40.33  ? 511  VAL D N     1 
ATOM   6269  C  CA    . VAL B  1  103 ? -9.657  42.129  23.883 1.00 36.49  ? 511  VAL D CA    1 
ATOM   6270  C  C     . VAL B  1  103 ? -9.253  43.515  24.382 1.00 41.34  ? 511  VAL D C     1 
ATOM   6271  O  O     . VAL B  1  103 ? -9.897  44.471  24.028 1.00 47.42  ? 511  VAL D O     1 
ATOM   6272  C  CB    . VAL B  1  103 ? -10.752 41.510  24.776 1.00 34.20  ? 511  VAL D CB    1 
ATOM   6273  C  CG1   . VAL B  1  103 ? -11.493 40.397  24.006 1.00 33.22  ? 511  VAL D CG1   1 
ATOM   6274  C  CG2   . VAL B  1  103 ? -10.189 41.017  26.115 1.00 33.66  ? 511  VAL D CG2   1 
ATOM   6275  N  N     . ASP B  1  104 ? -8.171  43.631  25.141 1.00 42.26  ? 512  ASP D N     1 
ATOM   6276  C  CA    . ASP B  1  104 ? -7.731  44.945  25.554 1.00 38.36  ? 512  ASP D CA    1 
ATOM   6277  C  C     . ASP B  1  104 ? -6.985  45.649  24.438 1.00 40.30  ? 512  ASP D C     1 
ATOM   6278  O  O     . ASP B  1  104 ? -7.042  46.870  24.324 1.00 36.79  ? 512  ASP D O     1 
ATOM   6279  C  CB    . ASP B  1  104 ? -6.891  44.822  26.794 1.00 38.22  ? 512  ASP D CB    1 
ATOM   6280  C  CG    . ASP B  1  104 ? -7.697  44.334  27.981 1.00 40.92  ? 512  ASP D CG    1 
ATOM   6281  O  OD1   . ASP B  1  104 ? -8.355  45.168  28.634 1.00 35.12  ? 512  ASP D OD1   1 
ATOM   6282  O  OD2   . ASP B  1  104 ? -7.707  43.110  28.264 1.00 41.58  ? 512  ASP D OD2   1 
ATOM   6283  N  N     . GLY B  1  105 ? -6.298  44.864  23.602 1.00 36.54  ? 513  GLY D N     1 
ATOM   6284  C  CA    . GLY B  1  105 ? -5.711  45.339  22.380 1.00 30.98  ? 513  GLY D CA    1 
ATOM   6285  C  C     . GLY B  1  105 ? -6.809  45.993  21.517 1.00 34.61  ? 513  GLY D C     1 
ATOM   6286  O  O     . GLY B  1  105 ? -6.665  47.117  21.057 1.00 32.93  ? 513  GLY D O     1 
ATOM   6287  N  N     . ALA B  1  106 ? -7.948  45.349  21.395 1.00 30.55  ? 514  ALA D N     1 
ATOM   6288  C  CA    . ALA B  1  106 ? -9.046  45.904  20.689 1.00 33.20  ? 514  ALA D CA    1 
ATOM   6289  C  C     . ALA B  1  106 ? -9.571  47.223  21.276 1.00 34.46  ? 514  ALA D C     1 
ATOM   6290  O  O     . ALA B  1  106 ? -9.922  48.137  20.538 1.00 40.38  ? 514  ALA D O     1 
ATOM   6291  C  CB    . ALA B  1  106 ? -10.171 44.870  20.611 1.00 33.17  ? 514  ALA D CB    1 
ATOM   6292  N  N     . HIS B  1  107 ? -9.689  47.302  22.589 1.00 33.06  ? 515  HIS D N     1 
ATOM   6293  C  CA    . HIS B  1  107 ? -10.162 48.501  23.242 1.00 32.30  ? 515  HIS D CA    1 
ATOM   6294  C  C     . HIS B  1  107 ? -9.247  49.655  22.974 1.00 31.68  ? 515  HIS D C     1 
ATOM   6295  O  O     . HIS B  1  107 ? -9.712  50.714  22.685 1.00 34.57  ? 515  HIS D O     1 
ATOM   6296  C  CB    . HIS B  1  107 ? -10.212 48.258  24.733 1.00 29.21  ? 515  HIS D CB    1 
ATOM   6297  C  CG    . HIS B  1  107 ? -10.910 49.314  25.501 1.00 31.15  ? 515  HIS D CG    1 
ATOM   6298  N  ND1   . HIS B  1  107 ? -10.523 49.655  26.787 1.00 29.66  ? 515  HIS D ND1   1 
ATOM   6299  C  CD2   . HIS B  1  107 ? -11.992 50.086  25.218 1.00 31.39  ? 515  HIS D CD2   1 
ATOM   6300  C  CE1   . HIS B  1  107 ? -11.335 50.579  27.263 1.00 27.69  ? 515  HIS D CE1   1 
ATOM   6301  N  NE2   . HIS B  1  107 ? -12.245 50.850  26.334 1.00 29.78  ? 515  HIS D NE2   1 
ATOM   6302  N  N     . ILE B  1  108 ? -7.948  49.413  23.022 1.00 33.77  ? 516  ILE D N     1 
ATOM   6303  C  CA    . ILE B  1  108 ? -6.959  50.459  22.866 1.00 34.97  ? 516  ILE D CA    1 
ATOM   6304  C  C     . ILE B  1  108 ? -7.000  50.992  21.459 1.00 37.57  ? 516  ILE D C     1 
ATOM   6305  O  O     . ILE B  1  108 ? -6.772  52.154  21.216 1.00 39.01  ? 516  ILE D O     1 
ATOM   6306  C  CB    . ILE B  1  108 ? -5.553  49.991  23.216 1.00 34.27  ? 516  ILE D CB    1 
ATOM   6307  C  CG1   . ILE B  1  108 ? -5.381  49.886  24.725 1.00 33.81  ? 516  ILE D CG1   1 
ATOM   6308  C  CG2   . ILE B  1  108 ? -4.477  50.992  22.713 1.00 35.54  ? 516  ILE D CG2   1 
ATOM   6309  C  CD1   . ILE B  1  108 ? -4.242  48.953  25.154 1.00 31.33  ? 516  ILE D CD1   1 
ATOM   6310  N  N     . ARG B  1  109 ? -7.287  50.111  20.527 1.00 39.79  ? 517  ARG D N     1 
ATOM   6311  C  CA    . ARG B  1  109 ? -7.517  50.511  19.170 1.00 41.17  ? 517  ARG D CA    1 
ATOM   6312  C  C     . ARG B  1  109 ? -8.774  51.385  19.023 1.00 43.30  ? 517  ARG D C     1 
ATOM   6313  O  O     . ARG B  1  109 ? -8.726  52.330  18.274 1.00 42.97  ? 517  ARG D O     1 
ATOM   6314  C  CB    . ARG B  1  109 ? -7.669  49.281  18.369 1.00 40.77  ? 517  ARG D CB    1 
ATOM   6315  C  CG    . ARG B  1  109 ? -7.683  49.479  16.877 1.00 44.13  ? 517  ARG D CG    1 
ATOM   6316  C  CD    . ARG B  1  109 ? -7.276  48.155  16.254 1.00 43.49  ? 517  ARG D CD    1 
ATOM   6317  N  NE    . ARG B  1  109 ? -8.305  47.143  16.432 1.00 43.33  ? 517  ARG D NE    1 
ATOM   6318  C  CZ    . ARG B  1  109 ? -8.052  45.934  16.894 1.00 40.42  ? 517  ARG D CZ    1 
ATOM   6319  N  NH1   . ARG B  1  109 ? -6.825  45.611  17.230 1.00 40.19  ? 517  ARG D NH1   1 
ATOM   6320  N  NH2   . ARG B  1  109 ? -9.019  45.056  17.000 1.00 38.70  ? 517  ARG D NH2   1 
ATOM   6321  N  N     . THR B  1  110 ? -9.864  51.085  19.730 1.00 36.89  ? 518  THR D N     1 
ATOM   6322  C  CA    . THR B  1  110 ? -11.028 51.927  19.590 1.00 35.92  ? 518  THR D CA    1 
ATOM   6323  C  C     . THR B  1  110 ? -10.738 53.293  20.183 1.00 39.16  ? 518  THR D C     1 
ATOM   6324  O  O     . THR B  1  110 ? -11.257 54.291  19.691 1.00 43.72  ? 518  THR D O     1 
ATOM   6325  C  CB    . THR B  1  110 ? -12.270 51.353  20.247 1.00 33.17  ? 518  THR D CB    1 
ATOM   6326  O  OG1   . THR B  1  110 ? -12.025 51.160  21.657 1.00 38.31  ? 518  THR D OG1   1 
ATOM   6327  C  CG2   . THR B  1  110 ? -12.594 50.071  19.658 1.00 30.71  ? 518  THR D CG2   1 
ATOM   6328  N  N     . LEU B  1  111 ? -9.925  53.328  21.233 1.00 36.25  ? 519  LEU D N     1 
ATOM   6329  C  CA    . LEU B  1  111 ? -9.529  54.567  21.825 1.00 37.83  ? 519  LEU D CA    1 
ATOM   6330  C  C     . LEU B  1  111 ? -8.639  55.364  20.890 1.00 38.74  ? 519  LEU D C     1 
ATOM   6331  O  O     . LEU B  1  111 ? -8.757  56.584  20.838 1.00 37.68  ? 519  LEU D O     1 
ATOM   6332  C  CB    . LEU B  1  111 ? -8.859  54.323  23.196 1.00 37.87  ? 519  LEU D CB    1 
ATOM   6333  C  CG    . LEU B  1  111 ? -9.751  53.671  24.279 1.00 33.85  ? 519  LEU D CG    1 
ATOM   6334  C  CD1   . LEU B  1  111 ? -8.922  52.987  25.358 1.00 32.95  ? 519  LEU D CD1   1 
ATOM   6335  C  CD2   . LEU B  1  111 ? -10.767 54.604  24.915 1.00 30.55  ? 519  LEU D CD2   1 
ATOM   6336  N  N     . LEU B  1  112 ? -7.767  54.695  20.141 1.00 38.71  ? 520  LEU D N     1 
ATOM   6337  C  CA    . LEU B  1  112 ? -6.876  55.413  19.247 1.00 40.58  ? 520  LEU D CA    1 
ATOM   6338  C  C     . LEU B  1  112 ? -7.643  55.945  18.029 1.00 44.89  ? 520  LEU D C     1 
ATOM   6339  O  O     . LEU B  1  112 ? -7.449  57.089  17.603 1.00 37.47  ? 520  LEU D O     1 
ATOM   6340  C  CB    . LEU B  1  112 ? -5.722  54.531  18.814 1.00 36.29  ? 520  LEU D CB    1 
ATOM   6341  C  CG    . LEU B  1  112 ? -4.658  54.348  19.884 1.00 37.05  ? 520  LEU D CG    1 
ATOM   6342  C  CD1   . LEU B  1  112 ? -3.792  53.163  19.481 1.00 37.04  ? 520  LEU D CD1   1 
ATOM   6343  C  CD2   . LEU B  1  112 ? -3.833  55.615  20.047 1.00 34.72  ? 520  LEU D CD2   1 
ATOM   6344  N  N     . LEU B  1  113 ? -8.527  55.124  17.486 1.00 37.80  ? 521  LEU D N     1 
ATOM   6345  C  CA    . LEU B  1  113 ? -9.281  55.571  16.355 1.00 42.16  ? 521  LEU D CA    1 
ATOM   6346  C  C     . LEU B  1  113 ? -10.139 56.760  16.711 1.00 45.30  ? 521  LEU D C     1 
ATOM   6347  O  O     . LEU B  1  113 ? -10.347 57.605  15.889 1.00 50.48  ? 521  LEU D O     1 
ATOM   6348  C  CB    . LEU B  1  113 ? -10.155 54.450  15.841 1.00 40.40  ? 521  LEU D CB    1 
ATOM   6349  C  CG    . LEU B  1  113 ? -9.338  53.358  15.132 1.00 38.24  ? 521  LEU D CG    1 
ATOM   6350  C  CD1   . LEU B  1  113 ? -10.178 52.121  14.868 1.00 32.57  ? 521  LEU D CD1   1 
ATOM   6351  C  CD2   . LEU B  1  113 ? -8.682  53.826  13.831 1.00 41.93  ? 521  LEU D CD2   1 
ATOM   6352  N  N     . THR B  1  114 ? -10.664 56.779  17.928 1.00 47.52  ? 522  THR D N     1 
ATOM   6353  C  CA    . THR B  1  114 ? -11.536 57.812  18.383 1.00 45.53  ? 522  THR D CA    1 
ATOM   6354  C  C     . THR B  1  114 ? -10.769 59.098  18.445 1.00 48.58  ? 522  THR D C     1 
ATOM   6355  O  O     . THR B  1  114 ? -11.285 60.124  18.127 1.00 51.07  ? 522  THR D O     1 
ATOM   6356  C  CB    . THR B  1  114 ? -12.036 57.507  19.784 1.00 41.03  ? 522  THR D CB    1 
ATOM   6357  O  OG1   . THR B  1  114 ? -12.741 56.276  19.747 1.00 41.97  ? 522  THR D OG1   1 
ATOM   6358  C  CG2   . THR B  1  114 ? -12.939 58.569  20.231 1.00 35.17  ? 522  THR D CG2   1 
ATOM   6359  N  N     . PHE B  1  115 ? -9.526  59.034  18.866 1.00 45.46  ? 523  PHE D N     1 
ATOM   6360  C  CA    . PHE B  1  115 ? -8.723  60.198  18.870 1.00 44.32  ? 523  PHE D CA    1 
ATOM   6361  C  C     . PHE B  1  115 ? -8.422  60.661  17.445 1.00 52.03  ? 523  PHE D C     1 
ATOM   6362  O  O     . PHE B  1  115 ? -8.517  61.841  17.158 1.00 47.63  ? 523  PHE D O     1 
ATOM   6363  C  CB    . PHE B  1  115 ? -7.433  59.919  19.595 1.00 48.19  ? 523  PHE D CB    1 
ATOM   6364  C  CG    . PHE B  1  115 ? -6.432  60.987  19.442 1.00 49.42  ? 523  PHE D CG    1 
ATOM   6365  C  CD1   . PHE B  1  115 ? -6.708  62.273  19.848 1.00 44.75  ? 523  PHE D CD1   1 
ATOM   6366  C  CD2   . PHE B  1  115 ? -5.201  60.693  18.890 1.00 49.07  ? 523  PHE D CD2   1 
ATOM   6367  C  CE1   . PHE B  1  115 ? -5.750  63.259  19.702 1.00 48.99  ? 523  PHE D CE1   1 
ATOM   6368  C  CE2   . PHE B  1  115 ? -4.230  61.653  18.735 1.00 45.29  ? 523  PHE D CE2   1 
ATOM   6369  C  CZ    . PHE B  1  115 ? -4.496  62.949  19.155 1.00 47.65  ? 523  PHE D CZ    1 
ATOM   6370  N  N     . PHE B  1  116 ? -8.065  59.743  16.559 1.00 46.97  ? 524  PHE D N     1 
ATOM   6371  C  CA    . PHE B  1  116 ? -7.766  60.125  15.183 1.00 53.92  ? 524  PHE D CA    1 
ATOM   6372  C  C     . PHE B  1  116 ? -8.978  60.755  14.495 1.00 54.18  ? 524  PHE D C     1 
ATOM   6373  O  O     . PHE B  1  116 ? -8.852  61.706  13.756 1.00 55.26  ? 524  PHE D O     1 
ATOM   6374  C  CB    . PHE B  1  116 ? -7.217  58.943  14.353 1.00 47.32  ? 524  PHE D CB    1 
ATOM   6375  C  CG    . PHE B  1  116 ? -5.939  58.395  14.860 1.00 44.63  ? 524  PHE D CG    1 
ATOM   6376  C  CD1   . PHE B  1  116 ? -5.080  59.175  15.634 1.00 47.57  ? 524  PHE D CD1   1 
ATOM   6377  C  CD2   . PHE B  1  116 ? -5.583  57.088  14.574 1.00 47.75  ? 524  PHE D CD2   1 
ATOM   6378  C  CE1   . PHE B  1  116 ? -3.886  58.652  16.116 1.00 49.76  ? 524  PHE D CE1   1 
ATOM   6379  C  CE2   . PHE B  1  116 ? -4.393  56.554  15.056 1.00 45.61  ? 524  PHE D CE2   1 
ATOM   6380  C  CZ    . PHE B  1  116 ? -3.548  57.336  15.830 1.00 46.43  ? 524  PHE D CZ    1 
ATOM   6381  N  N     . TYR B  1  117 ? -10.147 60.206  14.765 1.00 52.64  ? 525  TYR D N     1 
ATOM   6382  C  CA    . TYR B  1  117 ? -11.363 60.668  14.156 1.00 52.02  ? 525  TYR D CA    1 
ATOM   6383  C  C     . TYR B  1  117 ? -11.835 62.024  14.625 1.00 52.70  ? 525  TYR D C     1 
ATOM   6384  O  O     . TYR B  1  117 ? -12.272 62.824  13.832 1.00 64.35  ? 525  TYR D O     1 
ATOM   6385  C  CB    . TYR B  1  117 ? -12.465 59.657  14.352 1.00 55.21  ? 525  TYR D CB    1 
ATOM   6386  C  CG    . TYR B  1  117 ? -13.648 60.034  13.576 1.00 58.91  ? 525  TYR D CG    1 
ATOM   6387  C  CD1   . TYR B  1  117 ? -13.650 59.880  12.192 1.00 61.47  ? 525  TYR D CD1   1 
ATOM   6388  C  CD2   . TYR B  1  117 ? -14.754 60.588  14.200 1.00 62.41  ? 525  TYR D CD2   1 
ATOM   6389  C  CE1   . TYR B  1  117 ? -14.727 60.249  11.444 1.00 65.24  ? 525  TYR D CE1   1 
ATOM   6390  C  CE2   . TYR B  1  117 ? -15.854 60.954  13.461 1.00 62.64  ? 525  TYR D CE2   1 
ATOM   6391  C  CZ    . TYR B  1  117 ? -15.828 60.786  12.087 1.00 68.99  ? 525  TYR D CZ    1 
ATOM   6392  O  OH    . TYR B  1  117 ? -16.899 61.131  11.338 1.00 68.68  ? 525  TYR D OH    1 
ATOM   6393  N  N     . ARG B  1  118 ? -11.788 62.270  15.914 1.00 50.66  ? 526  ARG D N     1 
ATOM   6394  C  CA    . ARG B  1  118 ? -12.228 63.540  16.425 1.00 50.37  ? 526  ARG D CA    1 
ATOM   6395  C  C     . ARG B  1  118 ? -11.230 64.646  16.244 1.00 50.97  ? 526  ARG D C     1 
ATOM   6396  O  O     . ARG B  1  118 ? -11.603 65.785  16.224 1.00 56.44  ? 526  ARG D O     1 
ATOM   6397  C  CB    . ARG B  1  118 ? -12.599 63.415  17.899 1.00 47.04  ? 526  ARG D CB    1 
ATOM   6398  C  CG    . ARG B  1  118 ? -13.760 62.479  18.181 1.00 44.80  ? 526  ARG D CG    1 
ATOM   6399  C  CD    . ARG B  1  118 ? -14.920 62.879  17.337 1.00 44.16  ? 526  ARG D CD    1 
ATOM   6400  N  NE    . ARG B  1  118 ? -16.171 62.383  17.868 1.00 46.19  ? 526  ARG D NE    1 
ATOM   6401  C  CZ    . ARG B  1  118 ? -17.251 62.192  17.120 1.00 50.28  ? 526  ARG D CZ    1 
ATOM   6402  N  NH1   . ARG B  1  118 ? -17.184 62.469  15.826 1.00 53.65  ? 526  ARG D NH1   1 
ATOM   6403  N  NH2   . ARG B  1  118 ? -18.385 61.714  17.636 1.00 46.38  ? 526  ARG D NH2   1 
ATOM   6404  N  N     . PHE B  1  119 ? -9.959  64.323  16.152 1.00 50.15  ? 527  PHE D N     1 
ATOM   6405  C  CA    . PHE B  1  119 ? -8.943  65.356  16.222 1.00 54.78  ? 527  PHE D CA    1 
ATOM   6406  C  C     . PHE B  1  119 ? -8.011  65.393  15.044 1.00 57.40  ? 527  PHE D C     1 
ATOM   6407  O  O     . PHE B  1  119 ? -7.309  66.361  14.841 1.00 60.09  ? 527  PHE D O     1 
ATOM   6408  C  CB    . PHE B  1  119 ? -8.120  65.171  17.485 1.00 57.27  ? 527  PHE D CB    1 
ATOM   6409  C  CG    . PHE B  1  119 ? -8.757  65.727  18.666 1.00 56.87  ? 527  PHE D CG    1 
ATOM   6410  C  CD1   . PHE B  1  119 ? -9.749  65.005  19.345 1.00 54.20  ? 527  PHE D CD1   1 
ATOM   6411  C  CD2   . PHE B  1  119 ? -8.408  66.992  19.097 1.00 53.48  ? 527  PHE D CD2   1 
ATOM   6412  C  CE1   . PHE B  1  119 ? -10.371 65.543  20.460 1.00 52.31  ? 527  PHE D CE1   1 
ATOM   6413  C  CE2   . PHE B  1  119 ? -9.042  67.542  20.196 1.00 57.32  ? 527  PHE D CE2   1 
ATOM   6414  C  CZ    . PHE B  1  119 ? -10.024 66.826  20.888 1.00 53.78  ? 527  PHE D CZ    1 
ATOM   6415  N  N     . MET B  1  120 ? -7.968  64.318  14.287 1.00 54.44  ? 528  MET D N     1 
ATOM   6416  C  CA    . MET B  1  120 ? -6.990  64.237  13.248 1.00 55.91  ? 528  MET D CA    1 
ATOM   6417  C  C     . MET B  1  120 ? -7.613  63.604  12.040 1.00 56.03  ? 528  MET D C     1 
ATOM   6418  O  O     . MET B  1  120 ? -6.992  62.808  11.372 1.00 55.17  ? 528  MET D O     1 
ATOM   6419  C  CB    . MET B  1  120 ? -5.797  63.410  13.704 1.00 56.94  ? 528  MET D CB    1 
ATOM   6420  C  CG    . MET B  1  120 ? -4.867  64.166  14.588 1.00 56.22  ? 528  MET D CG    1 
ATOM   6421  S  SD    . MET B  1  120 ? -3.367  63.209  14.824 1.00 57.66  ? 528  MET D SD    1 
ATOM   6422  C  CE    . MET B  1  120 ? -2.495  64.347  15.884 1.00 50.98  ? 528  MET D CE    1 
ATOM   6423  N  N     . ARG B  1  121 ? -8.850  63.975  11.761 1.00 52.99  ? 529  ARG D N     1 
ATOM   6424  C  CA    . ARG B  1  121 ? -9.646  63.285  10.787 1.00 54.48  ? 529  ARG D CA    1 
ATOM   6425  C  C     . ARG B  1  121 ? -9.121  63.176  9.359  1.00 58.43  ? 529  ARG D C     1 
ATOM   6426  O  O     . ARG B  1  121 ? -9.341  62.181  8.701  1.00 58.05  ? 529  ARG D O     1 
ATOM   6427  C  CB    . ARG B  1  121 ? -10.988 63.935  10.770 1.00 54.40  ? 529  ARG D CB    1 
ATOM   6428  C  CG    . ARG B  1  121 ? -12.003 63.025  10.169 1.00 62.85  ? 529  ARG D CG    1 
ATOM   6429  C  CD    . ARG B  1  121 ? -13.340 63.649  10.342 1.00 68.51  ? 529  ARG D CD    1 
ATOM   6430  N  NE    . ARG B  1  121 ? -14.053 63.488  9.106  1.00 83.56  ? 529  ARG D NE    1 
ATOM   6431  C  CZ    . ARG B  1  121 ? -15.264 63.970  8.915  1.00 87.98  ? 529  ARG D CZ    1 
ATOM   6432  N  NH1   . ARG B  1  121 ? -15.860 64.642  9.893  1.00 76.98  ? 529  ARG D NH1   1 
ATOM   6433  N  NH2   . ARG B  1  121 ? -15.868 63.766  7.751  1.00 99.01  ? 529  ARG D NH2   1 
ATOM   6434  N  N     . PRO B  1  122 ? -8.469  64.213  8.860  1.00 61.93  ? 530  PRO D N     1 
ATOM   6435  C  CA    . PRO B  1  122 ? -7.994  64.181  7.497  1.00 62.41  ? 530  PRO D CA    1 
ATOM   6436  C  C     . PRO B  1  122 ? -7.025  63.047  7.316  1.00 62.68  ? 530  PRO D C     1 
ATOM   6437  O  O     . PRO B  1  122 ? -6.958  62.462  6.255  1.00 55.20  ? 530  PRO D O     1 
ATOM   6438  C  CB    . PRO B  1  122 ? -7.257  65.499  7.381  1.00 61.60  ? 530  PRO D CB    1 
ATOM   6439  C  CG    . PRO B  1  122 ? -8.066  66.399  8.206  1.00 59.57  ? 530  PRO D CG    1 
ATOM   6440  C  CD    . PRO B  1  122 ? -8.420  65.575  9.398  1.00 65.92  ? 530  PRO D CD    1 
ATOM   6441  N  N     . LEU B  1  123 ? -6.320  62.735  8.401  1.00 62.43  ? 531  LEU D N     1 
ATOM   6442  C  CA    . LEU B  1  123 ? -5.354  61.649  8.467  1.00 59.53  ? 531  LEU D CA    1 
ATOM   6443  C  C     . LEU B  1  123 ? -6.000  60.350  8.029  1.00 55.10  ? 531  LEU D C     1 
ATOM   6444  O  O     . LEU B  1  123 ? -5.435  59.618  7.230  1.00 58.01  ? 531  LEU D O     1 
ATOM   6445  C  CB    . LEU B  1  123 ? -4.806  61.532  9.890  1.00 64.82  ? 531  LEU D CB    1 
ATOM   6446  C  CG    . LEU B  1  123 ? -3.335  61.238  10.138 1.00 69.43  ? 531  LEU D CG    1 
ATOM   6447  C  CD1   . LEU B  1  123 ? -2.432  62.001  9.182  1.00 70.64  ? 531  LEU D CD1   1 
ATOM   6448  C  CD2   . LEU B  1  123 ? -3.010  61.609  11.566 1.00 73.62  ? 531  LEU D CD2   1 
ATOM   6449  N  N     . ILE B  1  124 ? -7.212  60.092  8.508  1.00 54.95  ? 532  ILE D N     1 
ATOM   6450  C  CA    . ILE B  1  124 ? -7.932  58.910  8.091  1.00 57.26  ? 532  ILE D CA    1 
ATOM   6451  C  C     . ILE B  1  124 ? -8.429  59.058  6.672  1.00 64.22  ? 532  ILE D C     1 
ATOM   6452  O  O     . ILE B  1  124 ? -8.463  58.104  5.912  1.00 59.48  ? 532  ILE D O     1 
ATOM   6453  C  CB    . ILE B  1  124 ? -9.146  58.647  8.991  1.00 59.98  ? 532  ILE D CB    1 
ATOM   6454  C  CG1   . ILE B  1  124 ? -8.681  58.240  10.380 1.00 62.95  ? 532  ILE D CG1   1 
ATOM   6455  C  CG2   . ILE B  1  124 ? -10.036 57.563  8.390  1.00 52.27  ? 532  ILE D CG2   1 
ATOM   6456  C  CD1   . ILE B  1  124 ? -9.751  58.441  11.412 1.00 61.41  ? 532  ILE D CD1   1 
ATOM   6457  N  N     . GLU B  1  125 ? -8.854  60.259  6.324  1.00 65.53  ? 533  GLU D N     1 
ATOM   6458  C  CA    . GLU B  1  125 ? -9.431  60.492  5.008  1.00 65.36  ? 533  GLU D CA    1 
ATOM   6459  C  C     . GLU B  1  125 ? -8.363  60.281  3.953  1.00 62.38  ? 533  GLU D C     1 
ATOM   6460  O  O     . GLU B  1  125 ? -8.635  59.662  2.937  1.00 60.02  ? 533  GLU D O     1 
ATOM   6461  C  CB    . GLU B  1  125 ? -9.970  61.900  4.937  1.00 66.30  ? 533  GLU D CB    1 
ATOM   6462  C  CG    . GLU B  1  125 ? -11.386 62.065  5.465  1.00 64.38  ? 533  GLU D CG    1 
ATOM   6463  C  CD    . GLU B  1  125 ? -11.721 63.511  5.838  1.00 67.22  ? 533  GLU D CD    1 
ATOM   6464  O  OE1   . GLU B  1  125 ? -12.876 63.768  6.206  1.00 75.12  ? 533  GLU D OE1   1 
ATOM   6465  O  OE2   . GLU B  1  125 ? -10.856 64.420  5.764  1.00 64.09  ? 533  GLU D OE2   1 
ATOM   6466  N  N     . ALA B  1  126 ? -7.134  60.727  4.257  1.00 59.25  ? 534  ALA D N     1 
ATOM   6467  C  CA    . ALA B  1  126 ? -5.976  60.565  3.385  1.00 53.15  ? 534  ALA D CA    1 
ATOM   6468  C  C     . ALA B  1  126 ? -5.573  59.117  3.197  1.00 56.62  ? 534  ALA D C     1 
ATOM   6469  O  O     . ALA B  1  126 ? -4.922  58.793  2.235  1.00 66.22  ? 534  ALA D O     1 
ATOM   6470  C  CB    . ALA B  1  126 ? -4.820  61.373  3.895  1.00 50.66  ? 534  ALA D CB    1 
ATOM   6471  N  N     . GLY B  1  127 ? -6.015  58.238  4.088  1.00 58.71  ? 535  GLY D N     1 
ATOM   6472  C  CA    . GLY B  1  127 ? -5.727  56.817  3.970  1.00 59.76  ? 535  GLY D CA    1 
ATOM   6473  C  C     . GLY B  1  127 ? -4.408  56.484  4.631  1.00 58.82  ? 535  GLY D C     1 
ATOM   6474  O  O     . GLY B  1  127 ? -3.782  55.484  4.304  1.00 59.30  ? 535  GLY D O     1 
ATOM   6475  N  N     . TYR B  1  128 ? -4.001  57.345  5.563  1.00 54.83  ? 536  TYR D N     1 
ATOM   6476  C  CA    . TYR B  1  128 ? -2.764  57.207  6.289  1.00 57.30  ? 536  TYR D CA    1 
ATOM   6477  C  C     . TYR B  1  128 ? -2.837  56.262  7.502  1.00 58.77  ? 536  TYR D C     1 
ATOM   6478  O  O     . TYR B  1  128 ? -1.796  55.847  8.015  1.00 54.46  ? 536  TYR D O     1 
ATOM   6479  C  CB    . TYR B  1  128 ? -2.313  58.581  6.755  1.00 56.15  ? 536  TYR D CB    1 
ATOM   6480  C  CG    . TYR B  1  128 ? -1.761  59.499  5.697  1.00 59.54  ? 536  TYR D CG    1 
ATOM   6481  C  CD1   . TYR B  1  128 ? -1.972  59.270  4.335  1.00 63.96  ? 536  TYR D CD1   1 
ATOM   6482  C  CD2   . TYR B  1  128 ? -1.042  60.638  6.062  1.00 62.13  ? 536  TYR D CD2   1 
ATOM   6483  C  CE1   . TYR B  1  128 ? -1.481  60.146  3.377  1.00 59.72  ? 536  TYR D CE1   1 
ATOM   6484  C  CE2   . TYR B  1  128 ? -0.549  61.506  5.107  1.00 61.55  ? 536  TYR D CE2   1 
ATOM   6485  C  CZ    . TYR B  1  128 ? -0.771  61.258  3.777  1.00 63.80  ? 536  TYR D CZ    1 
ATOM   6486  O  OH    . TYR B  1  128 ? -0.274  62.144  2.864  1.00 67.92  ? 536  TYR D OH    1 
ATOM   6487  N  N     . VAL B  1  129 ? -4.042  55.919  7.959  1.00 53.02  ? 537  VAL D N     1 
ATOM   6488  C  CA    . VAL B  1  129 ? -4.177  55.088  9.138  1.00 48.85  ? 537  VAL D CA    1 
ATOM   6489  C  C     . VAL B  1  129 ? -4.459  53.633  8.816  1.00 49.66  ? 537  VAL D C     1 
ATOM   6490  O  O     . VAL B  1  129 ? -5.386  53.308  8.080  1.00 46.69  ? 537  VAL D O     1 
ATOM   6491  C  CB    . VAL B  1  129 ? -5.219  55.648  10.128 1.00 53.37  ? 537  VAL D CB    1 
ATOM   6492  C  CG1   . VAL B  1  129 ? -5.346  54.730  11.339 1.00 53.22  ? 537  VAL D CG1   1 
ATOM   6493  C  CG2   . VAL B  1  129 ? -4.846  57.066  10.557 1.00 46.71  ? 537  VAL D CG2   1 
ATOM   6494  N  N     . TYR B  1  130 ? -3.644  52.755  9.401  1.00 48.74  ? 538  TYR D N     1 
ATOM   6495  C  CA    . TYR B  1  130 ? -3.751  51.310  9.174  1.00 49.71  ? 538  TYR D CA    1 
ATOM   6496  C  C     . TYR B  1  130 ? -3.807  50.537  10.480 1.00 48.59  ? 538  TYR D C     1 
ATOM   6497  O  O     . TYR B  1  130 ? -3.440  51.045  11.528 1.00 44.71  ? 538  TYR D O     1 
ATOM   6498  C  CB    . TYR B  1  130 ? -2.539  50.792  8.404  1.00 47.59  ? 538  TYR D CB    1 
ATOM   6499  C  CG    . TYR B  1  130 ? -2.281  51.479  7.085  1.00 55.94  ? 538  TYR D CG    1 
ATOM   6500  C  CD1   . TYR B  1  130 ? -1.725  52.763  7.037  1.00 54.77  ? 538  TYR D CD1   1 
ATOM   6501  C  CD2   . TYR B  1  130 ? -2.563  50.826  5.873  1.00 48.98  ? 538  TYR D CD2   1 
ATOM   6502  C  CE1   . TYR B  1  130 ? -1.497  53.383  5.832  1.00 57.75  ? 538  TYR D CE1   1 
ATOM   6503  C  CE2   . TYR B  1  130 ? -2.312  51.434  4.672  1.00 52.63  ? 538  TYR D CE2   1 
ATOM   6504  C  CZ    . TYR B  1  130 ? -1.781  52.709  4.659  1.00 56.61  ? 538  TYR D CZ    1 
ATOM   6505  O  OH    . TYR B  1  130 ? -1.522  53.317  3.455  1.00 63.86  ? 538  TYR D OH    1 
ATOM   6506  N  N     . ILE B  1  131 ? -4.225  49.284  10.388 1.00 43.90  ? 539  ILE D N     1 
ATOM   6507  C  CA    . ILE B  1  131 ? -4.210  48.386  11.494 1.00 40.84  ? 539  ILE D CA    1 
ATOM   6508  C  C     . ILE B  1  131 ? -3.364  47.156  11.183 1.00 40.70  ? 539  ILE D C     1 
ATOM   6509  O  O     . ILE B  1  131 ? -3.612  46.458  10.240 1.00 41.89  ? 539  ILE D O     1 
ATOM   6510  C  CB    . ILE B  1  131 ? -5.629  47.973  11.819 1.00 39.79  ? 539  ILE D CB    1 
ATOM   6511  C  CG1   . ILE B  1  131 ? -6.401  49.192  12.282 1.00 39.05  ? 539  ILE D CG1   1 
ATOM   6512  C  CG2   . ILE B  1  131 ? -5.662  46.924  12.899 1.00 34.29  ? 539  ILE D CG2   1 
ATOM   6513  C  CD1   . ILE B  1  131 ? -7.891  48.958  12.186 1.00 40.89  ? 539  ILE D CD1   1 
ATOM   6514  N  N     . ALA B  1  132 ? -2.405  46.844  12.039 1.00 42.61  ? 540  ALA D N     1 
ATOM   6515  C  CA    . ALA B  1  132 ? -1.530  45.694  11.859 1.00 42.64  ? 540  ALA D CA    1 
ATOM   6516  C  C     . ALA B  1  132 ? -2.237  44.441  12.182 1.00 46.94  ? 540  ALA D C     1 
ATOM   6517  O  O     . ALA B  1  132 ? -3.259  44.468  12.817 1.00 52.31  ? 540  ALA D O     1 
ATOM   6518  C  CB    . ALA B  1  132 ? -0.331  45.819  12.758 1.00 40.07  ? 540  ALA D CB    1 
ATOM   6519  N  N     . GLN B  1  133 ? -1.691  43.318  11.760 1.00 49.55  ? 541  GLN D N     1 
ATOM   6520  C  CA    . GLN B  1  133 ? -2.349  42.056  12.068 1.00 53.37  ? 541  GLN D CA    1 
ATOM   6521  C  C     . GLN B  1  133 ? -1.430  40.968  12.568 1.00 57.12  ? 541  GLN D C     1 
ATOM   6522  O  O     . GLN B  1  133 ? -1.110  40.027  11.850 1.00 52.52  ? 541  GLN D O     1 
ATOM   6523  C  CB    . GLN B  1  133 ? -3.143  41.567  10.889 1.00 56.87  ? 541  GLN D CB    1 
ATOM   6524  C  CG    . GLN B  1  133 ? -4.275  42.498  10.596 1.00 60.99  ? 541  GLN D CG    1 
ATOM   6525  C  CD    . GLN B  1  133 ? -5.180  41.903  9.617  1.00 65.01  ? 541  GLN D CD    1 
ATOM   6526  O  OE1   . GLN B  1  133 ? -6.267  41.483  9.960  1.00 77.82  ? 541  GLN D OE1   1 
ATOM   6527  N  NE2   . GLN B  1  133 ? -4.735  41.830  8.376  1.00 75.12  ? 541  GLN D NE2   1 
ATOM   6528  N  N     . PRO B  1  134 ? -1.058  41.063  13.834 1.00 57.50  ? 542  PRO D N     1 
ATOM   6529  C  CA    . PRO B  1  134 ? -0.128  40.145  14.476 1.00 60.18  ? 542  PRO D CA    1 
ATOM   6530  C  C     . PRO B  1  134 ? -0.688  38.719  14.578 1.00 63.60  ? 542  PRO D C     1 
ATOM   6531  O  O     . PRO B  1  134 ? -1.943  38.543  14.517 1.00 58.28  ? 542  PRO D O     1 
ATOM   6532  C  CB    . PRO B  1  134 ? 0.067   40.759  15.853 1.00 58.30  ? 542  PRO D CB    1 
ATOM   6533  C  CG    . PRO B  1  134 ? -0.382  42.166  15.716 1.00 60.36  ? 542  PRO D CG    1 
ATOM   6534  C  CD    . PRO B  1  134 ? -1.509  42.120  14.746 1.00 56.95  ? 542  PRO D CD    1 
ATOM   6535  N  N     . PRO B  1  135 ? 0.224   37.695  14.693 1.00 62.14  ? 543  PRO D N     1 
ATOM   6536  C  CA    . PRO B  1  135 ? -0.340  36.345  14.664 1.00 61.06  ? 543  PRO D CA    1 
ATOM   6537  C  C     . PRO B  1  135 ? -1.225  36.037  15.835 1.00 64.54  ? 543  PRO D C     1 
ATOM   6538  O  O     . PRO B  1  135 ? -1.079  36.606  16.936 1.00 60.77  ? 543  PRO D O     1 
ATOM   6539  C  CB    . PRO B  1  135 ? 0.889   35.423  14.732 1.00 60.64  ? 543  PRO D CB    1 
ATOM   6540  C  CG    . PRO B  1  135 ? 1.974   36.238  14.139 1.00 62.52  ? 543  PRO D CG    1 
ATOM   6541  C  CD    . PRO B  1  135 ? 1.700   37.626  14.680 1.00 58.08  ? 543  PRO D CD    1 
ATOM   6542  N  N     . THR B  1  136 ? -2.105  35.089  15.565 1.00 79.78  ? 544  THR D N     1 
ATOM   6543  C  CA    . THR B  1  136 ? -2.985  34.449  16.544 1.00 86.95  ? 544  THR D CA    1 
ATOM   6544  C  C     . THR B  1  136 ? -2.358  33.892  17.852 1.00 88.78  ? 544  THR D C     1 
ATOM   6545  O  O     . THR B  1  136 ? -2.928  34.098  18.913 1.00 84.10  ? 544  THR D O     1 
ATOM   6546  C  CB    . THR B  1  136 ? -3.830  33.354  15.857 1.00 86.47  ? 544  THR D CB    1 
ATOM   6547  O  OG1   . THR B  1  136 ? -4.830  32.927  16.773 1.00 92.32  ? 544  THR D OG1   1 
ATOM   6548  C  CG2   . THR B  1  136 ? -2.982  32.144  15.462 1.00 86.30  ? 544  THR D CG2   1 
ATOM   6549  N  N     . GLY B  1  137 ? -1.232  33.182  17.774 1.00 85.59  ? 545  GLY D N     1 
ATOM   6550  C  CA    . GLY B  1  137 ? -0.751  32.399  18.917 1.00 87.60  ? 545  GLY D CA    1 
ATOM   6551  C  C     . GLY B  1  137 ? -0.295  33.121  20.191 1.00 90.48  ? 545  GLY D C     1 
ATOM   6552  O  O     . GLY B  1  137 ? -0.478  32.621  21.303 1.00 98.61  ? 545  GLY D O     1 
ATOM   6553  N  N     . TYR B  1  138 ? 0.340   34.277  20.031 1.00 87.18  ? 580  TYR D N     1 
ATOM   6554  C  CA    . TYR B  1  138 ? 1.075   34.910  21.141 1.00 90.67  ? 580  TYR D CA    1 
ATOM   6555  C  C     . TYR B  1  138 ? 0.269   35.665  22.210 1.00 91.60  ? 580  TYR D C     1 
ATOM   6556  O  O     . TYR B  1  138 ? -0.824  36.213  21.931 1.00 75.30  ? 580  TYR D O     1 
ATOM   6557  C  CB    . TYR B  1  138 ? 2.196   35.771  20.557 1.00 90.67  ? 580  TYR D CB    1 
ATOM   6558  C  CG    . TYR B  1  138 ? 3.062   34.992  19.620 1.00 90.63  ? 580  TYR D CG    1 
ATOM   6559  C  CD1   . TYR B  1  138 ? 4.132   34.241  20.121 1.00 82.98  ? 580  TYR D CD1   1 
ATOM   6560  C  CD2   . TYR B  1  138 ? 2.777   34.948  18.226 1.00 84.59  ? 580  TYR D CD2   1 
ATOM   6561  C  CE1   . TYR B  1  138 ? 4.942   33.500  19.276 1.00 83.95  ? 580  TYR D CE1   1 
ATOM   6562  C  CE2   . TYR B  1  138 ? 3.557   34.194  17.378 1.00 85.62  ? 580  TYR D CE2   1 
ATOM   6563  C  CZ    . TYR B  1  138 ? 4.646   33.489  17.902 1.00 89.19  ? 580  TYR D CZ    1 
ATOM   6564  O  OH    . TYR B  1  138 ? 5.423   32.760  17.055 1.00 93.81  ? 580  TYR D OH    1 
ATOM   6565  N  N     . LYS B  1  139 ? 0.848   35.679  23.417 1.00 101.04 ? 581  LYS D N     1 
ATOM   6566  C  CA    . LYS B  1  139 ? 0.279   36.336  24.611 1.00 98.80  ? 581  LYS D CA    1 
ATOM   6567  C  C     . LYS B  1  139 ? 0.087   37.841  24.417 1.00 104.25 ? 581  LYS D C     1 
ATOM   6568  O  O     . LYS B  1  139 ? -0.983  38.393  24.714 1.00 122.23 ? 581  LYS D O     1 
ATOM   6569  C  CB    . LYS B  1  139 ? 1.164   36.103  25.839 1.00 82.35  ? 581  LYS D CB    1 
ATOM   6570  N  N     . GLY B  1  140 ? 1.127   38.486  23.913 1.00 98.59  ? 582  GLY D N     1 
ATOM   6571  C  CA    . GLY B  1  140 ? 1.169   39.928  23.644 1.00 70.41  ? 582  GLY D CA    1 
ATOM   6572  C  C     . GLY B  1  140 ? 2.357   40.028  22.732 1.00 59.48  ? 582  GLY D C     1 
ATOM   6573  O  O     . GLY B  1  140 ? 3.026   39.026  22.506 1.00 48.70  ? 582  GLY D O     1 
ATOM   6574  N  N     . LEU B  1  141 ? 2.653   41.204  22.213 1.00 53.35  ? 583  LEU D N     1 
ATOM   6575  C  CA    . LEU B  1  141 ? 3.772   41.273  21.271 1.00 61.64  ? 583  LEU D CA    1 
ATOM   6576  C  C     . LEU B  1  141 ? 5.103   41.070  21.985 1.00 56.25  ? 583  LEU D C     1 
ATOM   6577  O  O     . LEU B  1  141 ? 6.079   40.675  21.361 1.00 51.56  ? 583  LEU D O     1 
ATOM   6578  C  CB    . LEU B  1  141 ? 3.737   42.533  20.428 1.00 60.22  ? 583  LEU D CB    1 
ATOM   6579  C  CG    . LEU B  1  141 ? 2.399   42.704  19.700 1.00 58.79  ? 583  LEU D CG    1 
ATOM   6580  C  CD1   . LEU B  1  141 ? 2.439   43.950  18.839 1.00 55.75  ? 583  LEU D CD1   1 
ATOM   6581  C  CD2   . LEU B  1  141 ? 2.089   41.478  18.871 1.00 53.77  ? 583  LEU D CD2   1 
ATOM   6582  N  N     . GLY B  1  142 ? 5.081   41.291  23.309 1.00 53.33  ? 584  GLY D N     1 
ATOM   6583  C  CA    . GLY B  1  142 ? 6.235   41.107  24.187 1.00 44.18  ? 584  GLY D CA    1 
ATOM   6584  C  C     . GLY B  1  142 ? 6.633   39.629  24.219 1.00 49.99  ? 584  GLY D C     1 
ATOM   6585  O  O     . GLY B  1  142 ? 7.788   39.286  24.542 1.00 34.29  ? 584  GLY D O     1 
ATOM   6586  N  N     . GLU B  1  143 ? 5.684   38.755  23.863 1.00 49.86  ? 585  GLU D N     1 
ATOM   6587  C  CA    . GLU B  1  143 ? 5.982   37.359  23.815 1.00 54.12  ? 585  GLU D CA    1 
ATOM   6588  C  C     . GLU B  1  143 ? 6.619   36.866  22.512 1.00 46.40  ? 585  GLU D C     1 
ATOM   6589  O  O     . GLU B  1  143 ? 7.132   35.743  22.456 1.00 43.30  ? 585  GLU D O     1 
ATOM   6590  C  CB    . GLU B  1  143 ? 4.763   36.522  24.189 1.00 60.79  ? 585  GLU D CB    1 
ATOM   6591  C  CG    . GLU B  1  143 ? 5.199   35.090  24.377 1.00 71.46  ? 585  GLU D CG    1 
ATOM   6592  C  CD    . GLU B  1  143 ? 4.063   34.122  24.366 1.00 89.41  ? 585  GLU D CD    1 
ATOM   6593  O  OE1   . GLU B  1  143 ? 4.037   33.242  23.477 1.00 107.40 ? 585  GLU D OE1   1 
ATOM   6594  O  OE2   . GLU B  1  143 ? 3.201   34.207  25.270 1.00 96.26  ? 585  GLU D OE2   1 
ATOM   6595  N  N     . MET B  1  144 ? 6.618   37.699  21.489 1.00 46.20  ? 586  MET D N     1 
ATOM   6596  C  CA    . MET B  1  144 ? 7.254   37.353  20.213 1.00 46.42  ? 586  MET D CA    1 
ATOM   6597  C  C     . MET B  1  144 ? 8.725   37.734  20.133 1.00 49.27  ? 586  MET D C     1 
ATOM   6598  O  O     . MET B  1  144 ? 9.161   38.778  20.649 1.00 45.31  ? 586  MET D O     1 
ATOM   6599  C  CB    . MET B  1  144 ? 6.524   37.983  19.051 1.00 50.08  ? 586  MET D CB    1 
ATOM   6600  C  CG    . MET B  1  144 ? 5.059   37.597  19.007 1.00 57.74  ? 586  MET D CG    1 
ATOM   6601  S  SD    . MET B  1  144 ? 4.116   38.394  17.686 1.00 56.76  ? 586  MET D SD    1 
ATOM   6602  C  CE    . MET B  1  144 ? 4.719   37.474  16.280 1.00 52.85  ? 586  MET D CE    1 
ATOM   6603  N  N     . ASN B  1  145 ? 9.464   36.871  19.437 1.00 45.57  ? 587  ASN D N     1 
ATOM   6604  C  CA    . ASN B  1  145 ? 10.837  37.108  19.068 1.00 45.49  ? 587  ASN D CA    1 
ATOM   6605  C  C     . ASN B  1  145 ? 10.765  38.172  18.008 1.00 49.65  ? 587  ASN D C     1 
ATOM   6606  O  O     . ASN B  1  145 ? 9.781   38.270  17.285 1.00 44.17  ? 587  ASN D O     1 
ATOM   6607  C  CB    . ASN B  1  145 ? 11.442  35.837  18.512 1.00 42.15  ? 587  ASN D CB    1 
ATOM   6608  C  CG    . ASN B  1  145 ? 11.735  34.823  19.595 1.00 46.70  ? 587  ASN D CG    1 
ATOM   6609  O  OD1   . ASN B  1  145 ? 11.812  35.131  20.782 1.00 45.24  ? 587  ASN D OD1   1 
ATOM   6610  N  ND2   . ASN B  1  145 ? 11.900  33.597  19.192 1.00 55.72  ? 587  ASN D ND2   1 
ATOM   6611  N  N     . ALA B  1  146 ? 11.787  38.998  17.944 1.00 45.94  ? 588  ALA D N     1 
ATOM   6612  C  CA    . ALA B  1  146 ? 11.809  40.080  16.989 1.00 48.52  ? 588  ALA D CA    1 
ATOM   6613  C  C     . ALA B  1  146 ? 11.680  39.629  15.536 1.00 49.17  ? 588  ALA D C     1 
ATOM   6614  O  O     . ALA B  1  146 ? 10.986  40.258  14.742 1.00 43.36  ? 588  ALA D O     1 
ATOM   6615  C  CB    . ALA B  1  146 ? 13.047  40.904  17.163 1.00 43.64  ? 588  ALA D CB    1 
ATOM   6616  N  N     . ASP B  1  147 ? 12.336  38.522  15.212 1.00 46.59  ? 589  ASP D N     1 
ATOM   6617  C  CA    . ASP B  1  147 ? 12.304  38.008  13.857 1.00 48.86  ? 589  ASP D CA    1 
ATOM   6618  C  C     . ASP B  1  147 ? 10.898  37.540  13.471 1.00 49.34  ? 589  ASP D C     1 
ATOM   6619  O  O     . ASP B  1  147 ? 10.462  37.774  12.351 1.00 48.04  ? 589  ASP D O     1 
ATOM   6620  C  CB    . ASP B  1  147 ? 13.364  36.918  13.664 1.00 51.35  ? 589  ASP D CB    1 
ATOM   6621  C  CG    . ASP B  1  147 ? 13.064  35.663  14.451 1.00 57.26  ? 589  ASP D CG    1 
ATOM   6622  O  OD1   . ASP B  1  147 ? 12.643  35.737  15.619 1.00 65.39  ? 589  ASP D OD1   1 
ATOM   6623  O  OD2   . ASP B  1  147 ? 13.238  34.576  13.893 1.00 65.54  ? 589  ASP D OD2   1 
ATOM   6624  N  N     . GLN B  1  148 ? 10.178  36.905  14.389 1.00 48.37  ? 590  GLN D N     1 
ATOM   6625  C  CA    . GLN B  1  148 ? 8.825   36.473  14.043 1.00 54.77  ? 590  GLN D CA    1 
ATOM   6626  C  C     . GLN B  1  148 ? 7.846   37.642  13.911 1.00 56.18  ? 590  GLN D C     1 
ATOM   6627  O  O     . GLN B  1  148 ? 6.958   37.619  13.093 1.00 63.50  ? 590  GLN D O     1 
ATOM   6628  C  CB    . GLN B  1  148 ? 8.292   35.303  14.890 1.00 51.90  ? 590  GLN D CB    1 
ATOM   6629  C  CG    . GLN B  1  148 ? 8.134   35.546  16.378 1.00 68.01  ? 590  GLN D CG    1 
ATOM   6630  C  CD    . GLN B  1  148 ? 8.418   34.297  17.200 1.00 73.14  ? 590  GLN D CD    1 
ATOM   6631  O  OE1   . GLN B  1  148 ? 8.149   34.264  18.389 1.00 80.41  ? 590  GLN D OE1   1 
ATOM   6632  N  NE2   . GLN B  1  148 ? 8.974   33.264  16.563 1.00 73.48  ? 590  GLN D NE2   1 
ATOM   6633  N  N     . LEU B  1  149 ? 8.045   38.673  14.703 1.00 53.09  ? 591  LEU D N     1 
ATOM   6634  C  CA    . LEU B  1  149 ? 7.236   39.834  14.600 1.00 50.18  ? 591  LEU D CA    1 
ATOM   6635  C  C     . LEU B  1  149 ? 7.486   40.522  13.290 1.00 56.50  ? 591  LEU D C     1 
ATOM   6636  O  O     . LEU B  1  149 ? 6.550   41.025  12.717 1.00 61.69  ? 591  LEU D O     1 
ATOM   6637  C  CB    . LEU B  1  149 ? 7.614   40.776  15.708 1.00 52.88  ? 591  LEU D CB    1 
ATOM   6638  C  CG    . LEU B  1  149 ? 6.888   42.092  15.833 1.00 52.74  ? 591  LEU D CG    1 
ATOM   6639  C  CD1   . LEU B  1  149 ? 5.376   41.880  15.844 1.00 59.88  ? 591  LEU D CD1   1 
ATOM   6640  C  CD2   . LEU B  1  149 ? 7.334   42.599  17.173 1.00 55.98  ? 591  LEU D CD2   1 
ATOM   6641  N  N     . TRP B  1  150 ? 8.745   40.555  12.838 1.00 51.10  ? 592  TRP D N     1 
ATOM   6642  C  CA    . TRP B  1  150 ? 9.094   41.159  11.547 1.00 51.18  ? 592  TRP D CA    1 
ATOM   6643  C  C     . TRP B  1  150 ? 8.431   40.486  10.330 1.00 43.45  ? 592  TRP D C     1 
ATOM   6644  O  O     . TRP B  1  150 ? 7.779   41.136  9.549  1.00 50.04  ? 592  TRP D O     1 
ATOM   6645  C  CB    . TRP B  1  150 ? 10.625  41.228  11.380 1.00 50.98  ? 592  TRP D CB    1 
ATOM   6646  C  CG    . TRP B  1  150 ? 11.096  41.379  9.959  1.00 49.63  ? 592  TRP D CG    1 
ATOM   6647  C  CD1   . TRP B  1  150 ? 11.630  40.400  9.170  1.00 49.21  ? 592  TRP D CD1   1 
ATOM   6648  C  CD2   . TRP B  1  150 ? 11.078  42.579  9.155  1.00 50.90  ? 592  TRP D CD2   1 
ATOM   6649  N  NE1   . TRP B  1  150 ? 11.940  40.914  7.917  1.00 49.83  ? 592  TRP D NE1   1 
ATOM   6650  C  CE2   . TRP B  1  150 ? 11.610  42.241  7.885  1.00 45.08  ? 592  TRP D CE2   1 
ATOM   6651  C  CE3   . TRP B  1  150 ? 10.665  43.901  9.388  1.00 48.23  ? 592  TRP D CE3   1 
ATOM   6652  C  CZ2   . TRP B  1  150 ? 11.753  43.165  6.872  1.00 43.98  ? 592  TRP D CZ2   1 
ATOM   6653  C  CZ3   . TRP B  1  150 ? 10.782  44.796  8.373  1.00 50.34  ? 592  TRP D CZ3   1 
ATOM   6654  C  CH2   . TRP B  1  150 ? 11.343  44.440  7.130  1.00 47.00  ? 592  TRP D CH2   1 
ATOM   6655  N  N     . GLU B  1  151 ? 8.613   39.187  10.207 1.00 46.89  ? 593  GLU D N     1 
ATOM   6656  C  CA    . GLU B  1  151 ? 8.060   38.419  9.096  1.00 58.95  ? 593  GLU D CA    1 
ATOM   6657  C  C     . GLU B  1  151 ? 6.539   38.435  9.002  1.00 59.91  ? 593  GLU D C     1 
ATOM   6658  O  O     . GLU B  1  151 ? 5.993   38.700  7.938  1.00 65.13  ? 593  GLU D O     1 
ATOM   6659  C  CB    . GLU B  1  151 ? 8.550   36.968  9.157  1.00 63.79  ? 593  GLU D CB    1 
ATOM   6660  C  CG    . GLU B  1  151 ? 10.063  36.833  9.086  1.00 80.47  ? 593  GLU D CG    1 
ATOM   6661  C  CD    . GLU B  1  151 ? 10.643  37.263  7.746  1.00 83.79  ? 593  GLU D CD    1 
ATOM   6662  O  OE1   . GLU B  1  151 ? 9.893   37.709  6.849  1.00 87.48  ? 593  GLU D OE1   1 
ATOM   6663  O  OE2   . GLU B  1  151 ? 11.873  37.149  7.603  1.00 93.30  ? 593  GLU D OE2   1 
ATOM   6664  N  N     . THR B  1  152 ? 5.874   38.201  10.128 1.00 60.29  ? 594  THR D N     1 
ATOM   6665  C  CA    . THR B  1  152 ? 4.417   38.115  10.197 1.00 52.58  ? 594  THR D CA    1 
ATOM   6666  C  C     . THR B  1  152 ? 3.736   39.450  10.135 1.00 54.06  ? 594  THR D C     1 
ATOM   6667  O  O     . THR B  1  152 ? 2.683   39.543  9.544  1.00 64.54  ? 594  THR D O     1 
ATOM   6668  C  CB    . THR B  1  152 ? 3.958   37.402  11.480 1.00 51.90  ? 594  THR D CB    1 
ATOM   6669  O  OG1   . THR B  1  152 ? 4.213   38.239  12.631 1.00 52.58  ? 594  THR D OG1   1 
ATOM   6670  C  CG2   . THR B  1  152 ? 4.709   36.100  11.651 1.00 46.08  ? 594  THR D CG2   1 
ATOM   6671  N  N     . THR B  1  153 ? 4.310   40.504  10.714 1.00 54.84  ? 595  THR D N     1 
ATOM   6672  C  CA    . THR B  1  153 ? 3.544   41.720  10.914 1.00 50.33  ? 595  THR D CA    1 
ATOM   6673  C  C     . THR B  1  153 ? 4.109   42.983  10.342 1.00 50.19  ? 595  THR D C     1 
ATOM   6674  O  O     . THR B  1  153 ? 3.342   43.868  9.993  1.00 52.97  ? 595  THR D O     1 
ATOM   6675  C  CB    . THR B  1  153 ? 3.335   41.923  12.413 1.00 51.41  ? 595  THR D CB    1 
ATOM   6676  O  OG1   . THR B  1  153 ? 2.880   40.686  12.938 1.00 53.38  ? 595  THR D OG1   1 
ATOM   6677  C  CG2   . THR B  1  153 ? 2.286   42.889  12.663 1.00 53.41  ? 595  THR D CG2   1 
ATOM   6678  N  N     . MET B  1  154 ? 5.425   43.110  10.270 1.00 46.73  ? 596  MET D N     1 
ATOM   6679  C  CA    . MET B  1  154 ? 5.997   44.396  9.862  1.00 49.94  ? 596  MET D CA    1 
ATOM   6680  C  C     . MET B  1  154 ? 6.692   44.394  8.500  1.00 53.65  ? 596  MET D C     1 
ATOM   6681  O  O     . MET B  1  154 ? 7.087   45.460  8.019  1.00 51.71  ? 596  MET D O     1 
ATOM   6682  C  CB    . MET B  1  154 ? 7.007   44.883  10.892 1.00 49.98  ? 596  MET D CB    1 
ATOM   6683  C  CG    . MET B  1  154 ? 6.484   44.921  12.319 1.00 55.59  ? 596  MET D CG    1 
ATOM   6684  S  SD    . MET B  1  154 ? 7.777   45.460  13.438 1.00 58.61  ? 596  MET D SD    1 
ATOM   6685  C  CE    . MET B  1  154 ? 7.776   47.219  13.093 1.00 40.89  ? 596  MET D CE    1 
ATOM   6686  N  N     . ASN B  1  155 ? 6.917   43.211  7.940  1.00 55.54  ? 597  ASN D N     1 
ATOM   6687  C  CA    . ASN B  1  155 ? 7.598   43.059  6.666  1.00 55.84  ? 597  ASN D CA    1 
ATOM   6688  C  C     . ASN B  1  155 ? 6.669   43.455  5.518  1.00 56.95  ? 597  ASN D C     1 
ATOM   6689  O  O     . ASN B  1  155 ? 5.601   42.829  5.335  1.00 52.68  ? 597  ASN D O     1 
ATOM   6690  C  CB    . ASN B  1  155 ? 8.111   41.630  6.490  1.00 59.19  ? 597  ASN D CB    1 
ATOM   6691  C  CG    . ASN B  1  155 ? 9.126   41.519  5.357  1.00 61.78  ? 597  ASN D CG    1 
ATOM   6692  O  OD1   . ASN B  1  155 ? 9.438   42.510  4.700  1.00 60.16  ? 597  ASN D OD1   1 
ATOM   6693  N  ND2   . ASN B  1  155 ? 9.652   40.324  5.138  1.00 61.73  ? 597  ASN D ND2   1 
ATOM   6694  N  N     . PRO B  1  156 ? 7.081   44.500  4.753  1.00 55.77  ? 598  PRO D N     1 
ATOM   6695  C  CA    . PRO B  1  156 ? 6.127   44.889  3.719  1.00 62.92  ? 598  PRO D CA    1 
ATOM   6696  C  C     . PRO B  1  156 ? 5.883   43.764  2.722  1.00 66.96  ? 598  PRO D C     1 
ATOM   6697  O  O     . PRO B  1  156 ? 4.815   43.686  2.158  1.00 70.56  ? 598  PRO D O     1 
ATOM   6698  C  CB    . PRO B  1  156 ? 6.786   46.094  3.037  1.00 58.01  ? 598  PRO D CB    1 
ATOM   6699  C  CG    . PRO B  1  156 ? 7.822   46.567  3.968  1.00 56.31  ? 598  PRO D CG    1 
ATOM   6700  C  CD    . PRO B  1  156 ? 8.246   45.412  4.804  1.00 54.12  ? 598  PRO D CD    1 
ATOM   6701  N  N     . GLU B  1  157 ? 6.848   42.875  2.569  1.00 69.36  ? 599  GLU D N     1 
ATOM   6702  C  CA    . GLU B  1  157 ? 6.666   41.735  1.720  1.00 71.70  ? 599  GLU D CA    1 
ATOM   6703  C  C     . GLU B  1  157 ? 5.618   40.751  2.151  1.00 71.28  ? 599  GLU D C     1 
ATOM   6704  O  O     . GLU B  1  157 ? 4.934   40.227  1.316  1.00 82.31  ? 599  GLU D O     1 
ATOM   6705  C  CB    . GLU B  1  157 ? 7.984   41.033  1.522  1.00 76.24  ? 599  GLU D CB    1 
ATOM   6706  C  CG    . GLU B  1  157 ? 8.683   41.525  0.272  1.00 85.20  ? 599  GLU D CG    1 
ATOM   6707  C  CD    . GLU B  1  157 ? 10.183  41.513  0.415  1.00 98.41  ? 599  GLU D CD    1 
ATOM   6708  O  OE1   . GLU B  1  157 ? 10.693  40.666  1.199  1.00 111.92 ? 599  GLU D OE1   1 
ATOM   6709  O  OE2   . GLU B  1  157 ? 10.829  42.365  -0.236 1.00 98.84  ? 599  GLU D OE2   1 
ATOM   6710  N  N     . HIS B  1  158 ? 5.482   40.488  3.436  1.00 74.15  ? 600  HIS D N     1 
ATOM   6711  C  CA    . HIS B  1  158 ? 4.554   39.436  3.860  1.00 68.03  ? 600  HIS D CA    1 
ATOM   6712  C  C     . HIS B  1  158 ? 3.463   39.841  4.765  1.00 60.30  ? 600  HIS D C     1 
ATOM   6713  O  O     . HIS B  1  158 ? 2.557   39.047  5.020  1.00 64.59  ? 600  HIS D O     1 
ATOM   6714  C  CB    . HIS B  1  158 ? 5.292   38.302  4.527  1.00 73.55  ? 600  HIS D CB    1 
ATOM   6715  C  CG    . HIS B  1  158 ? 6.306   37.677  3.644  1.00 86.85  ? 600  HIS D CG    1 
ATOM   6716  N  ND1   . HIS B  1  158 ? 7.648   37.683  3.944  1.00 86.22  ? 600  HIS D ND1   1 
ATOM   6717  C  CD2   . HIS B  1  158 ? 6.185   37.078  2.439  1.00 87.30  ? 600  HIS D CD2   1 
ATOM   6718  C  CE1   . HIS B  1  158 ? 8.310   37.075  2.979  1.00 92.54  ? 600  HIS D CE1   1 
ATOM   6719  N  NE2   . HIS B  1  158 ? 7.446   36.702  2.052  1.00 91.90  ? 600  HIS D NE2   1 
ATOM   6720  N  N     . ARG B  1  159 ? 3.535   41.058  5.257  1.00 54.06  ? 601  ARG D N     1 
ATOM   6721  C  CA    . ARG B  1  159 ? 2.542   41.512  6.199  1.00 56.31  ? 601  ARG D CA    1 
ATOM   6722  C  C     . ARG B  1  159 ? 1.195   41.743  5.541  1.00 54.01  ? 601  ARG D C     1 
ATOM   6723  O  O     . ARG B  1  159 ? 1.092   42.017  4.348  1.00 58.61  ? 601  ARG D O     1 
ATOM   6724  C  CB    . ARG B  1  159 ? 3.013   42.795  6.890  1.00 55.42  ? 601  ARG D CB    1 
ATOM   6725  C  CG    . ARG B  1  159 ? 2.860   44.058  6.047  1.00 47.55  ? 601  ARG D CG    1 
ATOM   6726  C  CD    . ARG B  1  159 ? 3.796   45.159  6.485  1.00 48.68  ? 601  ARG D CD    1 
ATOM   6727  N  NE    . ARG B  1  159 ? 3.593   46.356  5.681  1.00 46.43  ? 601  ARG D NE    1 
ATOM   6728  C  CZ    . ARG B  1  159 ? 4.133   47.533  5.955  1.00 50.18  ? 601  ARG D CZ    1 
ATOM   6729  N  NH1   . ARG B  1  159 ? 4.916   47.680  7.004  1.00 60.17  ? 601  ARG D NH1   1 
ATOM   6730  N  NH2   . ARG B  1  159 ? 3.911   48.562  5.178  1.00 55.43  ? 601  ARG D NH2   1 
ATOM   6731  N  N     . ALA B  1  160 ? 0.163   41.653  6.340  1.00 54.10  ? 602  ALA D N     1 
ATOM   6732  C  CA    . ALA B  1  160 ? -1.165  42.064  5.892  1.00 52.95  ? 602  ALA D CA    1 
ATOM   6733  C  C     . ALA B  1  160 ? -1.635  43.291  6.687  1.00 55.26  ? 602  ALA D C     1 
ATOM   6734  O  O     . ALA B  1  160 ? -1.999  43.152  7.831  1.00 63.47  ? 602  ALA D O     1 
ATOM   6735  C  CB    . ALA B  1  160 ? -2.140  40.907  6.056  1.00 41.55  ? 602  ALA D CB    1 
ATOM   6736  N  N     . LEU B  1  161 ? -1.706  44.461  6.086  1.00 50.24  ? 603  LEU D N     1 
ATOM   6737  C  CA    . LEU B  1  161 ? -2.256  45.589  6.794  1.00 50.89  ? 603  LEU D CA    1 
ATOM   6738  C  C     . LEU B  1  161 ? -3.675  45.844  6.357  1.00 56.43  ? 603  LEU D C     1 
ATOM   6739  O  O     . LEU B  1  161 ? -4.003  45.587  5.204  1.00 60.17  ? 603  LEU D O     1 
ATOM   6740  C  CB    . LEU B  1  161 ? -1.455  46.829  6.517  1.00 45.91  ? 603  LEU D CB    1 
ATOM   6741  C  CG    . LEU B  1  161 ? -0.018  46.906  6.980  1.00 50.13  ? 603  LEU D CG    1 
ATOM   6742  C  CD1   . LEU B  1  161 ? 0.446   48.331  6.790  1.00 49.67  ? 603  LEU D CD1   1 
ATOM   6743  C  CD2   . LEU B  1  161 ? 0.172   46.548  8.429  1.00 47.67  ? 603  LEU D CD2   1 
ATOM   6744  N  N     . LEU B  1  162 ? -4.498  46.379  7.254  1.00 49.77  ? 604  LEU D N     1 
ATOM   6745  C  CA    . LEU B  1  162 ? -5.792  46.900  6.875  1.00 49.88  ? 604  LEU D CA    1 
ATOM   6746  C  C     . LEU B  1  162 ? -5.725  48.380  6.784  1.00 50.57  ? 604  LEU D C     1 
ATOM   6747  O  O     . LEU B  1  162 ? -5.291  49.010  7.710  1.00 53.94  ? 604  LEU D O     1 
ATOM   6748  C  CB    . LEU B  1  162 ? -6.828  46.567  7.923  1.00 57.45  ? 604  LEU D CB    1 
ATOM   6749  C  CG    . LEU B  1  162 ? -6.963  45.113  8.366  1.00 62.00  ? 604  LEU D CG    1 
ATOM   6750  C  CD1   . LEU B  1  162 ? -8.193  44.934  9.254  1.00 63.32  ? 604  LEU D CD1   1 
ATOM   6751  C  CD2   . LEU B  1  162 ? -7.041  44.141  7.196  1.00 59.57  ? 604  LEU D CD2   1 
ATOM   6752  N  N     . GLN B  1  163 ? -6.162  48.966  5.678  1.00 55.26  ? 605  GLN D N     1 
ATOM   6753  C  CA    . GLN B  1  163 ? -6.222  50.424  5.596  1.00 53.86  ? 605  GLN D CA    1 
ATOM   6754  C  C     . GLN B  1  163 ? -7.570  50.858  6.131  1.00 55.63  ? 605  GLN D C     1 
ATOM   6755  O  O     . GLN B  1  163 ? -8.586  50.217  5.856  1.00 52.91  ? 605  GLN D O     1 
ATOM   6756  C  CB    . GLN B  1  163 ? -6.035  50.887  4.173  1.00 49.84  ? 605  GLN D CB    1 
ATOM   6757  C  CG    . GLN B  1  163 ? -5.691  52.350  4.067  1.00 53.57  ? 605  GLN D CG    1 
ATOM   6758  C  CD    . GLN B  1  163 ? -5.426  52.775  2.607  1.00 56.05  ? 605  GLN D CD    1 
ATOM   6759  O  OE1   . GLN B  1  163 ? -5.833  52.110  1.676  1.00 54.18  ? 605  GLN D OE1   1 
ATOM   6760  N  NE2   . GLN B  1  163 ? -4.708  53.875  2.423  1.00 49.44  ? 605  GLN D NE2   1 
ATOM   6761  N  N     . VAL B  1  164 ? -7.578  51.925  6.901  1.00 51.55  ? 606  VAL D N     1 
ATOM   6762  C  CA    . VAL B  1  164 ? -8.824  52.359  7.469  1.00 54.86  ? 606  VAL D CA    1 
ATOM   6763  C  C     . VAL B  1  164 ? -9.478  53.310  6.497  1.00 53.50  ? 606  VAL D C     1 
ATOM   6764  O  O     . VAL B  1  164 ? -8.872  54.304  6.120  1.00 51.14  ? 606  VAL D O     1 
ATOM   6765  C  CB    . VAL B  1  164 ? -8.606  53.068  8.811  1.00 50.29  ? 606  VAL D CB    1 
ATOM   6766  C  CG1   . VAL B  1  164 ? -9.930  53.377  9.473  1.00 47.87  ? 606  VAL D CG1   1 
ATOM   6767  C  CG2   . VAL B  1  164 ? -7.741  52.223  9.693  1.00 45.15  ? 606  VAL D CG2   1 
ATOM   6768  N  N     . LYS B  1  165 ? -10.715 53.008  6.130  1.00 49.57  ? 607  LYS D N     1 
ATOM   6769  C  CA    . LYS B  1  165 ? -11.432 53.792  5.152  1.00 52.19  ? 607  LYS D CA    1 
ATOM   6770  C  C     . LYS B  1  165 ? -12.637 54.414  5.817  1.00 53.51  ? 607  LYS D C     1 
ATOM   6771  O  O     . LYS B  1  165 ? -13.379 53.719  6.503  1.00 59.00  ? 607  LYS D O     1 
ATOM   6772  C  CB    . LYS B  1  165 ? -11.854 52.911  3.970  1.00 49.54  ? 607  LYS D CB    1 
ATOM   6773  N  N     . LEU B  1  166 ? -12.826 55.718  5.619  1.00 56.62  ? 608  LEU D N     1 
ATOM   6774  C  CA    . LEU B  1  166 ? -13.984 56.427  6.116  1.00 54.76  ? 608  LEU D CA    1 
ATOM   6775  C  C     . LEU B  1  166 ? -15.018 56.523  5.021  1.00 61.70  ? 608  LEU D C     1 
ATOM   6776  O  O     . LEU B  1  166 ? -14.804 57.250  4.071  1.00 71.52  ? 608  LEU D O     1 
ATOM   6777  C  CB    . LEU B  1  166 ? -13.585 57.821  6.582  1.00 50.42  ? 608  LEU D CB    1 
ATOM   6778  C  CG    . LEU B  1  166 ? -14.740 58.804  6.897  1.00 50.64  ? 608  LEU D CG    1 
ATOM   6779  C  CD1   . LEU B  1  166 ? -15.811 58.265  7.863  1.00 48.35  ? 608  LEU D CD1   1 
ATOM   6780  C  CD2   . LEU B  1  166 ? -14.222 60.133  7.413  1.00 51.76  ? 608  LEU D CD2   1 
ATOM   6781  N  N     . GLU B  1  167 ? -16.144 55.849  5.173  1.00 68.35  ? 609  GLU D N     1 
ATOM   6782  C  CA    . GLU B  1  167 ? -17.163 55.831  4.123  1.00 71.05  ? 609  GLU D CA    1 
ATOM   6783  C  C     . GLU B  1  167 ? -18.317 56.821  4.320  1.00 69.59  ? 609  GLU D C     1 
ATOM   6784  O  O     . GLU B  1  167 ? -18.560 57.690  3.495  1.00 85.34  ? 609  GLU D O     1 
ATOM   6785  C  CB    . GLU B  1  167 ? -17.738 54.436  4.000  1.00 74.14  ? 609  GLU D CB    1 
ATOM   6786  C  CG    . GLU B  1  167 ? -16.720 53.371  3.624  1.00 90.92  ? 609  GLU D CG    1 
ATOM   6787  C  CD    . GLU B  1  167 ? -16.458 53.304  2.130  1.00 101.08 ? 609  GLU D CD    1 
ATOM   6788  O  OE1   . GLU B  1  167 ? -17.432 53.045  1.386  1.00 103.66 ? 609  GLU D OE1   1 
ATOM   6789  O  OE2   . GLU B  1  167 ? -15.284 53.505  1.711  1.00 100.02 ? 609  GLU D OE2   1 
ATOM   6790  N  N     . ASP B  1  168 ? -19.057 56.653  5.395  1.00 66.45  ? 610  ASP D N     1 
ATOM   6791  C  CA    . ASP B  1  168 ? -20.197 57.488  5.666  1.00 61.41  ? 610  ASP D CA    1 
ATOM   6792  C  C     . ASP B  1  168 ? -19.867 58.281  6.920  1.00 61.32  ? 610  ASP D C     1 
ATOM   6793  O  O     . ASP B  1  168 ? -19.774 57.725  8.003  1.00 60.15  ? 610  ASP D O     1 
ATOM   6794  C  CB    . ASP B  1  168 ? -21.420 56.597  5.840  1.00 59.85  ? 610  ASP D CB    1 
ATOM   6795  C  CG    . ASP B  1  168 ? -22.712 57.382  6.043  1.00 65.83  ? 610  ASP D CG    1 
ATOM   6796  O  OD1   . ASP B  1  168 ? -22.676 58.588  6.399  1.00 65.93  ? 610  ASP D OD1   1 
ATOM   6797  O  OD2   . ASP B  1  168 ? -23.785 56.765  5.851  1.00 66.44  ? 610  ASP D OD2   1 
ATOM   6798  N  N     . ALA B  1  169 ? -19.675 59.584  6.784  1.00 61.42  ? 611  ALA D N     1 
ATOM   6799  C  CA    . ALA B  1  169 ? -19.325 60.396  7.949  1.00 60.67  ? 611  ALA D CA    1 
ATOM   6800  C  C     . ALA B  1  169 ? -20.468 60.703  8.898  1.00 66.99  ? 611  ALA D C     1 
ATOM   6801  O  O     . ALA B  1  169 ? -20.221 60.907  10.057 1.00 73.04  ? 611  ALA D O     1 
ATOM   6802  C  CB    . ALA B  1  169 ? -18.606 61.670  7.552  1.00 60.12  ? 611  ALA D CB    1 
ATOM   6803  N  N     . ILE B  1  170 ? -21.702 60.725  8.438  1.00 72.24  ? 612  ILE D N     1 
ATOM   6804  C  CA    . ILE B  1  170 ? -22.818 60.834  9.369  1.00 67.12  ? 612  ILE D CA    1 
ATOM   6805  C  C     . ILE B  1  170 ? -22.854 59.616  10.246 1.00 63.45  ? 612  ILE D C     1 
ATOM   6806  O  O     . ILE B  1  170 ? -22.989 59.721  11.441 1.00 59.13  ? 612  ILE D O     1 
ATOM   6807  C  CB    . ILE B  1  170 ? -24.138 61.016  8.601  1.00 65.03  ? 612  ILE D CB    1 
ATOM   6808  C  CG1   . ILE B  1  170 ? -24.237 62.465  8.134  1.00 65.44  ? 612  ILE D CG1   1 
ATOM   6809  C  CG2   . ILE B  1  170 ? -25.373 60.623  9.395  1.00 59.69  ? 612  ILE D CG2   1 
ATOM   6810  C  CD1   . ILE B  1  170 ? -23.162 63.353  8.755  1.00 61.15  ? 612  ILE D CD1   1 
ATOM   6811  N  N     . GLU B  1  171 ? -22.681 58.469  9.617  1.00 56.62  ? 613  GLU D N     1 
ATOM   6812  C  CA    . GLU B  1  171 ? -22.714 57.208  10.284 1.00 59.01  ? 613  GLU D CA    1 
ATOM   6813  C  C     . GLU B  1  171 ? -21.547 57.038  11.245 1.00 58.92  ? 613  GLU D C     1 
ATOM   6814  O  O     . GLU B  1  171 ? -21.726 56.500  12.298 1.00 54.46  ? 613  GLU D O     1 
ATOM   6815  C  CB    . GLU B  1  171 ? -22.682 56.144  9.252  1.00 62.25  ? 613  GLU D CB    1 
ATOM   6816  C  CG    . GLU B  1  171 ? -23.083 54.777  9.725  1.00 62.63  ? 613  GLU D CG    1 
ATOM   6817  C  CD    . GLU B  1  171 ? -22.466 53.749  8.819  1.00 66.70  ? 613  GLU D CD    1 
ATOM   6818  O  OE1   . GLU B  1  171 ? -23.017 52.635  8.745  1.00 68.15  ? 613  GLU D OE1   1 
ATOM   6819  O  OE2   . GLU B  1  171 ? -21.427 54.070  8.176  1.00 72.60  ? 613  GLU D OE2   1 
ATOM   6820  N  N     . ALA B  1  172 ? -20.378 57.518  10.868 1.00 53.74  ? 614  ALA D N     1 
ATOM   6821  C  CA    . ALA B  1  172 ? -19.260 57.446  11.742 1.00 53.12  ? 614  ALA D CA    1 
ATOM   6822  C  C     . ALA B  1  172 ? -19.401 58.383  12.951 1.00 57.62  ? 614  ALA D C     1 
ATOM   6823  O  O     . ALA B  1  172 ? -18.996 58.014  14.033 1.00 55.97  ? 614  ALA D O     1 
ATOM   6824  C  CB    . ALA B  1  172 ? -17.962 57.677  10.988 1.00 51.69  ? 614  ALA D CB    1 
ATOM   6825  N  N     . ASP B  1  173 ? -19.969 59.568  12.799 1.00 60.29  ? 615  ASP D N     1 
ATOM   6826  C  CA    . ASP B  1  173 ? -20.190 60.380  13.999 1.00 63.73  ? 615  ASP D CA    1 
ATOM   6827  C  C     . ASP B  1  173 ? -21.138 59.689  14.963 1.00 58.31  ? 615  ASP D C     1 
ATOM   6828  O  O     . ASP B  1  173 ? -20.935 59.704  16.157 1.00 52.62  ? 615  ASP D O     1 
ATOM   6829  C  CB    . ASP B  1  173 ? -20.812 61.704  13.650 1.00 62.23  ? 615  ASP D CB    1 
ATOM   6830  C  CG    . ASP B  1  173 ? -19.950 62.531  12.775 1.00 69.14  ? 615  ASP D CG    1 
ATOM   6831  O  OD1   . ASP B  1  173 ? -18.705 62.424  12.810 1.00 72.03  ? 615  ASP D OD1   1 
ATOM   6832  O  OD2   . ASP B  1  173 ? -20.537 63.322  12.025 1.00 79.15  ? 615  ASP D OD2   1 
ATOM   6833  N  N     . GLN B  1  174 ? -22.167 59.066  14.426 1.00 54.70  ? 616  GLN D N     1 
ATOM   6834  C  CA    . GLN B  1  174 ? -23.157 58.457  15.256 1.00 57.81  ? 616  GLN D CA    1 
ATOM   6835  C  C     . GLN B  1  174 ? -22.539 57.275  15.958 1.00 60.45  ? 616  GLN D C     1 
ATOM   6836  O  O     . GLN B  1  174 ? -22.894 57.020  17.093 1.00 63.92  ? 616  GLN D O     1 
ATOM   6837  C  CB    . GLN B  1  174 ? -24.329 58.011  14.416 1.00 57.29  ? 616  GLN D CB    1 
ATOM   6838  C  CG    . GLN B  1  174 ? -25.042 59.178  13.775 1.00 65.27  ? 616  GLN D CG    1 
ATOM   6839  C  CD    . GLN B  1  174 ? -26.160 58.752  12.843 1.00 70.53  ? 616  GLN D CD    1 
ATOM   6840  O  OE1   . GLN B  1  174 ? -26.266 57.576  12.433 1.00 75.07  ? 616  GLN D OE1   1 
ATOM   6841  N  NE2   . GLN B  1  174 ? -27.019 59.705  12.509 1.00 65.82  ? 616  GLN D NE2   1 
ATOM   6842  N  N     . THR B  1  175 ? -21.607 56.594  15.285 1.00 56.24  ? 617  THR D N     1 
ATOM   6843  C  CA    . THR B  1  175 ? -20.905 55.462  15.828 1.00 52.69  ? 617  THR D CA    1 
ATOM   6844  C  C     . THR B  1  175 ? -19.961 55.780  16.976 1.00 50.00  ? 617  THR D C     1 
ATOM   6845  O  O     . THR B  1  175 ? -19.958 55.038  17.951 1.00 48.61  ? 617  THR D O     1 
ATOM   6846  C  CB    . THR B  1  175 ? -20.155 54.736  14.713 1.00 51.33  ? 617  THR D CB    1 
ATOM   6847  O  OG1   . THR B  1  175 ? -21.070 53.869  14.068 1.00 55.48  ? 617  THR D OG1   1 
ATOM   6848  C  CG2   . THR B  1  175 ? -19.037 53.889  15.247 1.00 49.96  ? 617  THR D CG2   1 
ATOM   6849  N  N     . PHE B  1  176 ? -19.158 56.841  16.865 1.00 45.10  ? 618  PHE D N     1 
ATOM   6850  C  CA    . PHE B  1  176 ? -18.244 57.167  17.932 1.00 46.15  ? 618  PHE D CA    1 
ATOM   6851  C  C     . PHE B  1  176 ? -19.000 57.672  19.136 1.00 49.78  ? 618  PHE D C     1 
ATOM   6852  O  O     . PHE B  1  176 ? -18.591 57.474  20.266 1.00 53.29  ? 618  PHE D O     1 
ATOM   6853  C  CB    . PHE B  1  176 ? -17.204 58.178  17.479 1.00 43.75  ? 618  PHE D CB    1 
ATOM   6854  C  CG    . PHE B  1  176 ? -16.145 57.594  16.651 1.00 47.49  ? 618  PHE D CG    1 
ATOM   6855  C  CD1   . PHE B  1  176 ? -15.025 57.059  17.234 1.00 47.10  ? 618  PHE D CD1   1 
ATOM   6856  C  CD2   . PHE B  1  176 ? -16.285 57.516  15.264 1.00 49.49  ? 618  PHE D CD2   1 
ATOM   6857  C  CE1   . PHE B  1  176 ? -14.019 56.463  16.453 1.00 50.86  ? 618  PHE D CE1   1 
ATOM   6858  C  CE2   . PHE B  1  176 ? -15.300 56.933  14.468 1.00 50.08  ? 618  PHE D CE2   1 
ATOM   6859  C  CZ    . PHE B  1  176 ? -14.141 56.399  15.066 1.00 49.99  ? 618  PHE D CZ    1 
ATOM   6860  N  N     . GLU B  1  177 ? -20.088 58.372  18.891 1.00 50.20  ? 619  GLU D N     1 
ATOM   6861  C  CA    . GLU B  1  177 ? -20.869 58.875  19.964 1.00 51.86  ? 619  GLU D CA    1 
ATOM   6862  C  C     . GLU B  1  177 ? -21.510 57.726  20.710 1.00 45.74  ? 619  GLU D C     1 
ATOM   6863  O  O     . GLU B  1  177 ? -21.529 57.702  21.939 1.00 46.30  ? 619  GLU D O     1 
ATOM   6864  C  CB    . GLU B  1  177 ? -21.940 59.769  19.411 1.00 56.93  ? 619  GLU D CB    1 
ATOM   6865  C  CG    . GLU B  1  177 ? -22.149 60.939  20.341 1.00 75.76  ? 619  GLU D CG    1 
ATOM   6866  C  CD    . GLU B  1  177 ? -23.554 61.471  20.361 1.00 94.13  ? 619  GLU D CD    1 
ATOM   6867  O  OE1   . GLU B  1  177 ? -24.109 61.622  21.477 1.00 95.61  ? 619  GLU D OE1   1 
ATOM   6868  O  OE2   . GLU B  1  177 ? -24.094 61.751  19.266 1.00 102.85 ? 619  GLU D OE2   1 
ATOM   6869  N  N     . MET B  1  178 ? -22.064 56.781  19.962 1.00 38.74  ? 620  MET D N     1 
ATOM   6870  C  CA    . MET B  1  178 ? -22.734 55.696  20.609 1.00 41.84  ? 620  MET D CA    1 
ATOM   6871  C  C     . MET B  1  178 ? -21.794 54.823  21.474 1.00 43.81  ? 620  MET D C     1 
ATOM   6872  O  O     . MET B  1  178 ? -22.114 54.549  22.618 1.00 44.95  ? 620  MET D O     1 
ATOM   6873  C  CB    . MET B  1  178 ? -23.427 54.868  19.583 1.00 39.43  ? 620  MET D CB    1 
ATOM   6874  C  CG    . MET B  1  178 ? -23.908 53.513  20.097 1.00 42.84  ? 620  MET D CG    1 
ATOM   6875  S  SD    . MET B  1  178 ? -24.797 52.581  18.832 1.00 53.10  ? 620  MET D SD    1 
ATOM   6876  C  CE    . MET B  1  178 ? -23.531 52.105  17.646 1.00 50.02  ? 620  MET D CE    1 
ATOM   6877  N  N     . LEU B  1  179 ? -20.689 54.379  20.892 1.00 41.79  ? 621  LEU D N     1 
ATOM   6878  C  CA    . LEU B  1  179 ? -19.736 53.486  21.549 1.00 43.55  ? 621  LEU D CA    1 
ATOM   6879  C  C     . LEU B  1  179 ? -18.862 54.157  22.597 1.00 41.33  ? 621  LEU D C     1 
ATOM   6880  O  O     . LEU B  1  179 ? -18.609 53.581  23.624 1.00 43.08  ? 621  LEU D O     1 
ATOM   6881  C  CB    . LEU B  1  179 ? -18.821 52.844  20.533 1.00 40.59  ? 621  LEU D CB    1 
ATOM   6882  C  CG    . LEU B  1  179 ? -19.448 52.027  19.407 1.00 45.63  ? 621  LEU D CG    1 
ATOM   6883  C  CD1   . LEU B  1  179 ? -18.352 51.514  18.489 1.00 42.39  ? 621  LEU D CD1   1 
ATOM   6884  C  CD2   . LEU B  1  179 ? -20.291 50.868  19.883 1.00 41.08  ? 621  LEU D CD2   1 
ATOM   6885  N  N     . MET B  1  180 ? -18.389 55.361  22.321 1.00 40.45  ? 622  MET D N     1 
ATOM   6886  C  CA    . MET B  1  180 ? -17.354 55.964  23.126 1.00 37.41  ? 622  MET D CA    1 
ATOM   6887  C  C     . MET B  1  180 ? -17.889 57.114  23.959 1.00 42.81  ? 622  MET D C     1 
ATOM   6888  O  O     . MET B  1  180 ? -17.180 57.674  24.803 1.00 40.43  ? 622  MET D O     1 
ATOM   6889  C  CB    . MET B  1  180 ? -16.248 56.457  22.242 1.00 33.21  ? 622  MET D CB    1 
ATOM   6890  C  CG    . MET B  1  180 ? -15.736 55.454  21.245 1.00 36.06  ? 622  MET D CG    1 
ATOM   6891  S  SD    . MET B  1  180 ? -15.241 53.868  21.975 1.00 37.47  ? 622  MET D SD    1 
ATOM   6892  C  CE    . MET B  1  180 ? -13.736 54.408  22.772 1.00 31.42  ? 622  MET D CE    1 
ATOM   6893  N  N     . GLY B  1  181 ? -19.172 57.423  23.769 1.00 42.79  ? 623  GLY D N     1 
ATOM   6894  C  CA    . GLY B  1  181 ? -19.718 58.632  24.351 1.00 38.58  ? 623  GLY D CA    1 
ATOM   6895  C  C     . GLY B  1  181 ? -20.105 58.424  25.778 1.00 39.51  ? 623  GLY D C     1 
ATOM   6896  O  O     . GLY B  1  181 ? -20.000 57.345  26.308 1.00 46.21  ? 623  GLY D O     1 
ATOM   6897  N  N     . ASP B  1  182 ? -20.607 59.456  26.409 1.00 40.73  ? 624  ASP D N     1 
ATOM   6898  C  CA    . ASP B  1  182 ? -20.922 59.338  27.820 1.00 45.03  ? 624  ASP D CA    1 
ATOM   6899  C  C     . ASP B  1  182 ? -22.345 58.851  28.125 1.00 43.47  ? 624  ASP D C     1 
ATOM   6900  O  O     . ASP B  1  182 ? -22.677 58.700  29.267 1.00 46.61  ? 624  ASP D O     1 
ATOM   6901  C  CB    . ASP B  1  182 ? -20.581 60.612  28.592 1.00 51.37  ? 624  ASP D CB    1 
ATOM   6902  C  CG    . ASP B  1  182 ? -21.282 61.837  28.031 1.00 65.80  ? 624  ASP D CG    1 
ATOM   6903  O  OD1   . ASP B  1  182 ? -22.421 61.701  27.497 1.00 71.46  ? 624  ASP D OD1   1 
ATOM   6904  O  OD2   . ASP B  1  182 ? -20.683 62.948  28.116 1.00 73.68  ? 624  ASP D OD2   1 
ATOM   6905  N  N     . VAL B  1  183 ? -23.184 58.565  27.143 1.00 43.09  ? 625  VAL D N     1 
ATOM   6906  C  CA    . VAL B  1  183 ? -24.472 57.952  27.465 1.00 43.13  ? 625  VAL D CA    1 
ATOM   6907  C  C     . VAL B  1  183 ? -24.389 56.422  27.547 1.00 45.03  ? 625  VAL D C     1 
ATOM   6908  O  O     . VAL B  1  183 ? -24.326 55.751  26.516 1.00 43.33  ? 625  VAL D O     1 
ATOM   6909  C  CB    . VAL B  1  183 ? -25.536 58.317  26.412 1.00 44.30  ? 625  VAL D CB    1 
ATOM   6910  C  CG1   . VAL B  1  183 ? -26.885 57.675  26.759 1.00 42.58  ? 625  VAL D CG1   1 
ATOM   6911  C  CG2   . VAL B  1  183 ? -25.660 59.815  26.273 1.00 40.09  ? 625  VAL D CG2   1 
ATOM   6912  N  N     . VAL B  1  184 ? -24.490 55.881  28.745 1.00 40.33  ? 626  VAL D N     1 
ATOM   6913  C  CA    . VAL B  1  184 ? -24.307 54.458  28.941 1.00 38.00  ? 626  VAL D CA    1 
ATOM   6914  C  C     . VAL B  1  184 ? -25.364 53.617  28.231 1.00 39.53  ? 626  VAL D C     1 
ATOM   6915  O  O     . VAL B  1  184 ? -25.021 52.577  27.655 1.00 39.44  ? 626  VAL D O     1 
ATOM   6916  C  CB    . VAL B  1  184 ? -24.280 54.102  30.434 1.00 35.64  ? 626  VAL D CB    1 
ATOM   6917  C  CG1   . VAL B  1  184 ? -24.226 52.590  30.635 1.00 32.62  ? 626  VAL D CG1   1 
ATOM   6918  C  CG2   . VAL B  1  184 ? -23.076 54.755  31.045 1.00 35.63  ? 626  VAL D CG2   1 
ATOM   6919  N  N     . GLU B  1  185 ? -26.627 54.047  28.275 1.00 38.97  ? 627  GLU D N     1 
ATOM   6920  C  CA    . GLU B  1  185 ? -27.738 53.218  27.791 1.00 38.40  ? 627  GLU D CA    1 
ATOM   6921  C  C     . GLU B  1  185 ? -27.617 52.870  26.312 1.00 43.71  ? 627  GLU D C     1 
ATOM   6922  O  O     . GLU B  1  185 ? -27.890 51.736  25.921 1.00 45.76  ? 627  GLU D O     1 
ATOM   6923  C  CB    . GLU B  1  185 ? -29.101 53.876  28.074 1.00 35.99  ? 627  GLU D CB    1 
ATOM   6924  C  CG    . GLU B  1  185 ? -30.314 53.097  27.549 1.00 38.03  ? 627  GLU D CG    1 
ATOM   6925  C  CD    . GLU B  1  185 ? -30.404 51.633  28.046 1.00 43.30  ? 627  GLU D CD    1 
ATOM   6926  O  OE1   . GLU B  1  185 ? -29.776 51.256  29.069 1.00 47.38  ? 627  GLU D OE1   1 
ATOM   6927  O  OE2   . GLU B  1  185 ? -31.111 50.835  27.419 1.00 41.08  ? 627  GLU D OE2   1 
ATOM   6928  N  N     . ASN B  1  186 ? -27.232 53.834  25.478 1.00 42.93  ? 628  ASN D N     1 
ATOM   6929  C  CA    . ASN B  1  186 ? -27.124 53.537  24.043 1.00 44.37  ? 628  ASN D CA    1 
ATOM   6930  C  C     . ASN B  1  186 ? -26.045 52.493  23.742 1.00 44.63  ? 628  ASN D C     1 
ATOM   6931  O  O     . ASN B  1  186 ? -26.215 51.642  22.871 1.00 46.80  ? 628  ASN D O     1 
ATOM   6932  C  CB    . ASN B  1  186 ? -26.982 54.822  23.248 1.00 38.42  ? 628  ASN D CB    1 
ATOM   6933  C  CG    . ASN B  1  186 ? -28.201 55.734  23.442 1.00 48.01  ? 628  ASN D CG    1 
ATOM   6934  O  OD1   . ASN B  1  186 ? -29.346 55.261  23.615 1.00 41.69  ? 628  ASN D OD1   1 
ATOM   6935  N  ND2   . ASN B  1  186 ? -27.970 57.030  23.440 1.00 46.14  ? 628  ASN D ND2   1 
ATOM   6936  N  N     . ARG B  1  187 ? -24.972 52.559  24.516 1.00 39.23  ? 629  ARG D N     1 
ATOM   6937  C  CA    . ARG B  1  187 ? -23.873 51.639  24.386 1.00 38.94  ? 629  ARG D CA    1 
ATOM   6938  C  C     . ARG B  1  187 ? -24.322 50.296  24.867 1.00 37.60  ? 629  ARG D C     1 
ATOM   6939  O  O     . ARG B  1  187 ? -23.958 49.325  24.288 1.00 38.74  ? 629  ARG D O     1 
ATOM   6940  C  CB    . ARG B  1  187 ? -22.753 52.120  25.244 1.00 37.55  ? 629  ARG D CB    1 
ATOM   6941  C  CG    . ARG B  1  187 ? -21.687 51.127  25.501 1.00 34.38  ? 629  ARG D CG    1 
ATOM   6942  C  CD    . ARG B  1  187 ? -20.392 51.880  25.773 1.00 37.23  ? 629  ARG D CD    1 
ATOM   6943  N  NE    . ARG B  1  187 ? -20.459 52.762  26.942 1.00 37.80  ? 629  ARG D NE    1 
ATOM   6944  C  CZ    . ARG B  1  187 ? -20.492 54.096  26.884 1.00 39.93  ? 629  ARG D CZ    1 
ATOM   6945  N  NH1   . ARG B  1  187 ? -20.478 54.718  25.719 1.00 40.87  ? 629  ARG D NH1   1 
ATOM   6946  N  NH2   . ARG B  1  187 ? -20.568 54.812  27.986 1.00 40.05  ? 629  ARG D NH2   1 
ATOM   6947  N  N     . ARG B  1  188 ? -25.098 50.254  25.940 1.00 35.90  ? 630  ARG D N     1 
ATOM   6948  C  CA    . ARG B  1  188 ? -25.566 48.981  26.444 1.00 39.19  ? 630  ARG D CA    1 
ATOM   6949  C  C     . ARG B  1  188 ? -26.465 48.321  25.424 1.00 40.83  ? 630  ARG D C     1 
ATOM   6950  O  O     . ARG B  1  188 ? -26.303 47.109  25.156 1.00 42.11  ? 630  ARG D O     1 
ATOM   6951  C  CB    . ARG B  1  188 ? -26.285 49.128  27.781 1.00 38.40  ? 630  ARG D CB    1 
ATOM   6952  C  CG    . ARG B  1  188 ? -26.664 47.787  28.405 1.00 39.05  ? 630  ARG D CG    1 
ATOM   6953  C  CD    . ARG B  1  188 ? -27.862 47.890  29.313 1.00 39.01  ? 630  ARG D CD    1 
ATOM   6954  N  NE    . ARG B  1  188 ? -28.984 48.401  28.556 1.00 43.32  ? 630  ARG D NE    1 
ATOM   6955  C  CZ    . ARG B  1  188 ? -29.791 47.649  27.822 1.00 45.64  ? 630  ARG D CZ    1 
ATOM   6956  N  NH1   . ARG B  1  188 ? -29.599 46.334  27.793 1.00 43.97  ? 630  ARG D NH1   1 
ATOM   6957  N  NH2   . ARG B  1  188 ? -30.798 48.219  27.149 1.00 45.90  ? 630  ARG D NH2   1 
ATOM   6958  N  N     . GLN B  1  189 ? -27.395 49.103  24.867 1.00 39.51  ? 631  GLN D N     1 
ATOM   6959  C  CA    . GLN B  1  189 ? -28.290 48.566  23.834 1.00 46.23  ? 631  GLN D CA    1 
ATOM   6960  C  C     . GLN B  1  189 ? -27.536 48.001  22.639 1.00 39.30  ? 631  GLN D C     1 
ATOM   6961  O  O     . GLN B  1  189 ? -27.807 46.895  22.200 1.00 37.36  ? 631  GLN D O     1 
ATOM   6962  C  CB    . GLN B  1  189 ? -29.339 49.589  23.378 1.00 44.48  ? 631  GLN D CB    1 
ATOM   6963  C  CG    . GLN B  1  189 ? -30.447 48.981  22.564 1.00 44.39  ? 631  GLN D CG    1 
ATOM   6964  C  CD    . GLN B  1  189 ? -31.230 47.895  23.313 1.00 55.01  ? 631  GLN D CD    1 
ATOM   6965  O  OE1   . GLN B  1  189 ? -31.842 48.154  24.359 1.00 55.74  ? 631  GLN D OE1   1 
ATOM   6966  N  NE2   . GLN B  1  189 ? -31.209 46.663  22.774 1.00 50.00  ? 631  GLN D NE2   1 
ATOM   6967  N  N     . PHE B  1  190 ? -26.576 48.760  22.139 1.00 40.87  ? 632  PHE D N     1 
ATOM   6968  C  CA    . PHE B  1  190 ? -25.746 48.267  21.039 1.00 39.98  ? 632  PHE D CA    1 
ATOM   6969  C  C     . PHE B  1  190 ? -25.135 46.893  21.359 1.00 42.13  ? 632  PHE D C     1 
ATOM   6970  O  O     . PHE B  1  190 ? -25.056 46.041  20.483 1.00 42.56  ? 632  PHE D O     1 
ATOM   6971  C  CB    . PHE B  1  190 ? -24.639 49.272  20.682 1.00 39.28  ? 632  PHE D CB    1 
ATOM   6972  C  CG    . PHE B  1  190 ? -23.526 48.654  19.925 1.00 43.89  ? 632  PHE D CG    1 
ATOM   6973  C  CD1   . PHE B  1  190 ? -23.669 48.374  18.564 1.00 43.90  ? 632  PHE D CD1   1 
ATOM   6974  C  CD2   . PHE B  1  190 ? -22.352 48.263  20.575 1.00 47.34  ? 632  PHE D CD2   1 
ATOM   6975  C  CE1   . PHE B  1  190 ? -22.648 47.757  17.868 1.00 44.08  ? 632  PHE D CE1   1 
ATOM   6976  C  CE2   . PHE B  1  190 ? -21.327 47.633  19.878 1.00 49.83  ? 632  PHE D CE2   1 
ATOM   6977  C  CZ    . PHE B  1  190 ? -21.486 47.376  18.524 1.00 50.10  ? 632  PHE D CZ    1 
ATOM   6978  N  N     . ILE B  1  191 ? -24.713 46.680  22.610 1.00 41.43  ? 633  ILE D N     1 
ATOM   6979  C  CA    . ILE B  1  191 ? -24.025 45.424  22.980 1.00 39.19  ? 633  ILE D CA    1 
ATOM   6980  C  C     . ILE B  1  191 ? -24.973 44.253  23.076 1.00 35.68  ? 633  ILE D C     1 
ATOM   6981  O  O     . ILE B  1  191 ? -24.688 43.190  22.556 1.00 37.64  ? 633  ILE D O     1 
ATOM   6982  C  CB    . ILE B  1  191 ? -23.243 45.570  24.311 1.00 43.44  ? 633  ILE D CB    1 
ATOM   6983  C  CG1   . ILE B  1  191 ? -22.237 46.726  24.249 1.00 43.37  ? 633  ILE D CG1   1 
ATOM   6984  C  CG2   . ILE B  1  191 ? -22.508 44.294  24.661 1.00 36.22  ? 633  ILE D CG2   1 
ATOM   6985  C  CD1   . ILE B  1  191 ? -21.685 47.119  25.599 1.00 33.87  ? 633  ILE D CD1   1 
ATOM   6986  N  N     . GLU B  1  192 ? -26.110 44.474  23.726 1.00 36.56  ? 634  GLU D N     1 
ATOM   6987  C  CA    . GLU B  1  192 ? -27.131 43.449  23.850 1.00 38.66  ? 634  GLU D CA    1 
ATOM   6988  C  C     . GLU B  1  192 ? -27.586 42.986  22.482 1.00 42.27  ? 634  GLU D C     1 
ATOM   6989  O  O     . GLU B  1  192 ? -27.726 41.774  22.272 1.00 45.64  ? 634  GLU D O     1 
ATOM   6990  C  CB    . GLU B  1  192 ? -28.324 43.937  24.648 1.00 34.71  ? 634  GLU D CB    1 
ATOM   6991  C  CG    . GLU B  1  192 ? -29.386 42.866  24.841 1.00 34.46  ? 634  GLU D CG    1 
ATOM   6992  C  CD    . GLU B  1  192 ? -30.676 43.389  25.413 1.00 39.79  ? 634  GLU D CD    1 
ATOM   6993  O  OE1   . GLU B  1  192 ? -31.542 42.536  25.741 1.00 45.86  ? 634  GLU D OE1   1 
ATOM   6994  O  OE2   . GLU B  1  192 ? -30.831 44.627  25.527 1.00 35.41  ? 634  GLU D OE2   1 
ATOM   6995  N  N     . ASP B  1  193 ? -27.776 43.946  21.570 1.00 42.59  ? 635  ASP D N     1 
ATOM   6996  C  CA    . ASP B  1  193 ? -28.246 43.641  20.210 1.00 44.02  ? 635  ASP D CA    1 
ATOM   6997  C  C     . ASP B  1  193 ? -27.261 42.810  19.423 1.00 47.01  ? 635  ASP D C     1 
ATOM   6998  O  O     . ASP B  1  193 ? -27.669 41.904  18.734 1.00 55.67  ? 635  ASP D O     1 
ATOM   6999  C  CB    . ASP B  1  193 ? -28.545 44.917  19.417 1.00 43.30  ? 635  ASP D CB    1 
ATOM   7000  C  CG    . ASP B  1  193 ? -29.742 45.680  19.958 1.00 45.12  ? 635  ASP D CG    1 
ATOM   7001  O  OD1   . ASP B  1  193 ? -30.500 45.121  20.774 1.00 47.38  ? 635  ASP D OD1   1 
ATOM   7002  O  OD2   . ASP B  1  193 ? -29.887 46.864  19.613 1.00 42.93  ? 635  ASP D OD2   1 
ATOM   7003  N  N     . ASN B  1  194 ? -25.965 43.097  19.554 1.00 47.10  ? 636  ASN D N     1 
ATOM   7004  C  CA    . ASN B  1  194 ? -24.949 42.377  18.808 1.00 46.22  ? 636  ASN D CA    1 
ATOM   7005  C  C     . ASN B  1  194 ? -24.192 41.284  19.527 1.00 48.64  ? 636  ASN D C     1 
ATOM   7006  O  O     . ASN B  1  194 ? -23.403 40.587  18.883 1.00 51.98  ? 636  ASN D O     1 
ATOM   7007  C  CB    . ASN B  1  194 ? -23.976 43.355  18.166 1.00 45.70  ? 636  ASN D CB    1 
ATOM   7008  C  CG    . ASN B  1  194 ? -24.689 44.341  17.270 1.00 49.67  ? 636  ASN D CG    1 
ATOM   7009  O  OD1   . ASN B  1  194 ? -24.575 44.294  16.045 1.00 52.41  ? 636  ASN D OD1   1 
ATOM   7010  N  ND2   . ASN B  1  194 ? -25.469 45.216  17.879 1.00 46.23  ? 636  ASN D ND2   1 
ATOM   7011  N  N     . ALA B  1  195 ? -24.413 41.122  20.824 1.00 49.03  ? 637  ALA D N     1 
ATOM   7012  C  CA    . ALA B  1  195 ? -23.675 40.109  21.565 1.00 59.14  ? 637  ALA D CA    1 
ATOM   7013  C  C     . ALA B  1  195 ? -24.026 38.683  21.100 1.00 61.46  ? 637  ALA D C     1 
ATOM   7014  O  O     . ALA B  1  195 ? -25.175 38.357  20.849 1.00 64.72  ? 637  ALA D O     1 
ATOM   7015  C  CB    . ALA B  1  195 ? -23.885 40.266  23.053 1.00 57.80  ? 637  ALA D CB    1 
ATOM   7016  N  N     . VAL B  1  196 ? -23.002 37.853  20.974 1.00 74.75  ? 638  VAL D N     1 
ATOM   7017  C  CA    . VAL B  1  196 ? -23.140 36.471  20.504 1.00 86.58  ? 638  VAL D CA    1 
ATOM   7018  C  C     . VAL B  1  196 ? -21.975 35.606  21.015 1.00 92.21  ? 638  VAL D C     1 
ATOM   7019  O  O     . VAL B  1  196 ? -20.933 36.125  21.385 1.00 90.81  ? 638  VAL D O     1 
ATOM   7020  C  CB    . VAL B  1  196 ? -23.200 36.427  18.949 1.00 86.46  ? 638  VAL D CB    1 
ATOM   7021  C  CG1   . VAL B  1  196 ? -21.951 37.064  18.344 1.00 80.94  ? 638  VAL D CG1   1 
ATOM   7022  C  CG2   . VAL B  1  196 ? -23.322 34.997  18.454 1.00 84.90  ? 638  VAL D CG2   1 
ATOM   7023  N  N     . TYR B  1  197 ? -22.140 34.287  20.966 1.00 109.82 ? 639  TYR D N     1 
ATOM   7024  C  CA    . TYR B  1  197 ? -21.073 33.358  21.350 1.00 103.04 ? 639  TYR D CA    1 
ATOM   7025  C  C     . TYR B  1  197 ? -20.331 32.749  20.155 1.00 97.06  ? 639  TYR D C     1 
ATOM   7026  O  O     . TYR B  1  197 ? -20.929 32.174  19.257 1.00 90.42  ? 639  TYR D O     1 
ATOM   7027  C  CB    . TYR B  1  197 ? -21.578 32.277  22.341 1.00 104.23 ? 639  TYR D CB    1 
ATOM   7028  C  CG    . TYR B  1  197 ? -21.514 32.725  23.778 1.00 98.37  ? 639  TYR D CG    1 
ATOM   7029  C  CD1   . TYR B  1  197 ? -20.269 32.878  24.420 1.00 99.69  ? 639  TYR D CD1   1 
ATOM   7030  C  CD2   . TYR B  1  197 ? -22.682 33.048  24.484 1.00 97.10  ? 639  TYR D CD2   1 
ATOM   7031  C  CE1   . TYR B  1  197 ? -20.188 33.337  25.722 1.00 96.41  ? 639  TYR D CE1   1 
ATOM   7032  C  CE2   . TYR B  1  197 ? -22.614 33.497  25.794 1.00 96.04  ? 639  TYR D CE2   1 
ATOM   7033  C  CZ    . TYR B  1  197 ? -21.363 33.643  26.405 1.00 93.67  ? 639  TYR D CZ    1 
ATOM   7034  O  OH    . TYR B  1  197 ? -21.260 34.080  27.693 1.00 68.22  ? 639  TYR D OH    1 
ATOM   7035  N  N     . ASN B  1  211 ? -7.815  43.979  2.730  1.00 74.23  ? 1010 ASN D N     1 
ATOM   7036  C  CA    . ASN B  1  211 ? -6.865  44.929  3.367  1.00 82.41  ? 1010 ASN D CA    1 
ATOM   7037  C  C     . ASN B  1  211 ? -7.428  46.340  3.526  1.00 79.14  ? 1010 ASN D C     1 
ATOM   7038  O  O     . ASN B  1  211 ? -6.732  47.231  4.013  1.00 83.15  ? 1010 ASN D O     1 
ATOM   7039  C  CB    . ASN B  1  211 ? -5.563  45.006  2.571  1.00 86.78  ? 1010 ASN D CB    1 
ATOM   7040  C  CG    . ASN B  1  211 ? -5.790  45.181  1.082  1.00 98.10  ? 1010 ASN D CG    1 
ATOM   7041  O  OD1   . ASN B  1  211 ? -6.659  45.930  0.616  1.00 105.67 ? 1010 ASN D OD1   1 
ATOM   7042  N  ND2   . ASN B  1  211 ? -5.002  44.474  0.326  1.00 110.78 ? 1010 ASN D ND2   1 
ATOM   7043  N  N     . GLU B  1  212 ? -8.694  46.541  3.150  1.00 75.49  ? 1011 GLU D N     1 
ATOM   7044  C  CA    . GLU B  1  212 ? -9.373  47.813  3.397  1.00 69.90  ? 1011 GLU D CA    1 
ATOM   7045  C  C     . GLU B  1  212 ? -10.494 47.618  4.414  1.00 67.56  ? 1011 GLU D C     1 
ATOM   7046  O  O     . GLU B  1  212 ? -11.242 46.665  4.318  1.00 68.17  ? 1011 GLU D O     1 
ATOM   7047  C  CB    . GLU B  1  212 ? -9.898  48.398  2.097  1.00 67.62  ? 1011 GLU D CB    1 
ATOM   7048  N  N     . ARG B  1  213 ? -10.546 48.481  5.414  1.00 58.33  ? 1012 ARG D N     1 
ATOM   7049  C  CA    . ARG B  1  213 ? -11.433 48.278  6.553  1.00 54.22  ? 1012 ARG D CA    1 
ATOM   7050  C  C     . ARG B  1  213 ? -12.217 49.549  6.837  1.00 51.09  ? 1012 ARG D C     1 
ATOM   7051  O  O     . ARG B  1  213 ? -11.629 50.611  7.080  1.00 53.47  ? 1012 ARG D O     1 
ATOM   7052  C  CB    . ARG B  1  213 ? -10.592 47.857  7.788  1.00 56.47  ? 1012 ARG D CB    1 
ATOM   7053  C  CG    . ARG B  1  213 ? -11.354 47.704  9.083  1.00 58.60  ? 1012 ARG D CG    1 
ATOM   7054  C  CD    . ARG B  1  213 ? -12.137 46.406  9.071  1.00 64.67  ? 1012 ARG D CD    1 
ATOM   7055  N  NE    . ARG B  1  213 ? -12.304 45.857  10.419 1.00 68.86  ? 1012 ARG D NE    1 
ATOM   7056  C  CZ    . ARG B  1  213 ? -13.305 45.060  10.802 1.00 74.02  ? 1012 ARG D CZ    1 
ATOM   7057  N  NH1   . ARG B  1  213 ? -14.255 44.704  9.941  1.00 71.78  ? 1012 ARG D NH1   1 
ATOM   7058  N  NH2   . ARG B  1  213 ? -13.338 44.594  12.048 1.00 76.22  ? 1012 ARG D NH2   1 
ATOM   7059  N  N     . ASN B  1  214 ? -13.538 49.464  6.806  1.00 49.57  ? 1013 ASN D N     1 
ATOM   7060  C  CA    . ASN B  1  214 ? -14.370 50.636  7.073  1.00 52.14  ? 1013 ASN D CA    1 
ATOM   7061  C  C     . ASN B  1  214 ? -14.258 50.987  8.574  1.00 51.81  ? 1013 ASN D C     1 
ATOM   7062  O  O     . ASN B  1  214 ? -14.359 50.097  9.401  1.00 49.32  ? 1013 ASN D O     1 
ATOM   7063  C  CB    . ASN B  1  214 ? -15.813 50.353  6.637  1.00 53.62  ? 1013 ASN D CB    1 
ATOM   7064  C  CG    . ASN B  1  214 ? -16.808 51.349  7.201  1.00 58.62  ? 1013 ASN D CG    1 
ATOM   7065  O  OD1   . ASN B  1  214 ? -17.792 50.948  7.783  1.00 73.83  ? 1013 ASN D OD1   1 
ATOM   7066  N  ND2   . ASN B  1  214 ? -16.542 52.644  7.057  1.00 59.07  ? 1013 ASN D ND2   1 
ATOM   7067  N  N     . ILE B  1  215 ? -14.018 52.248  8.895  1.00 45.79  ? 1014 ILE D N     1 
ATOM   7068  C  CA    . ILE B  1  215 ? -13.765 52.643  10.251 1.00 46.26  ? 1014 ILE D CA    1 
ATOM   7069  C  C     . ILE B  1  215 ? -14.928 52.380  11.205 1.00 54.29  ? 1014 ILE D C     1 
ATOM   7070  O  O     . ILE B  1  215 ? -14.685 52.149  12.383 1.00 51.01  ? 1014 ILE D O     1 
ATOM   7071  C  CB    . ILE B  1  215 ? -13.391 54.120  10.356 1.00 46.31  ? 1014 ILE D CB    1 
ATOM   7072  C  CG1   . ILE B  1  215 ? -12.856 54.409  11.776 1.00 40.29  ? 1014 ILE D CG1   1 
ATOM   7073  C  CG2   . ILE B  1  215 ? -14.607 54.986  10.039 1.00 46.33  ? 1014 ILE D CG2   1 
ATOM   7074  C  CD1   . ILE B  1  215 ? -12.147 55.727  12.003 1.00 34.89  ? 1014 ILE D CD1   1 
ATOM   7075  N  N     . THR B  1  216 ? -16.161 52.469  10.706 1.00 52.90  ? 1015 THR D N     1 
ATOM   7076  C  CA    . THR B  1  216 ? -17.340 52.156  11.469 1.00 50.65  ? 1015 THR D CA    1 
ATOM   7077  C  C     . THR B  1  216 ? -17.388 50.682  11.816 1.00 51.10  ? 1015 THR D C     1 
ATOM   7078  O  O     . THR B  1  216 ? -17.708 50.312  12.932 1.00 50.58  ? 1015 THR D O     1 
ATOM   7079  C  CB    . THR B  1  216 ? -18.595 52.590  10.693 1.00 47.67  ? 1015 THR D CB    1 
ATOM   7080  O  OG1   . THR B  1  216 ? -18.711 53.996  10.812 1.00 49.58  ? 1015 THR D OG1   1 
ATOM   7081  C  CG2   . THR B  1  216 ? -19.850 52.011  11.264 1.00 46.40  ? 1015 THR D CG2   1 
ATOM   7082  N  N     . SER B  1  217 ? -17.076 49.834  10.859 1.00 53.34  ? 1016 SER D N     1 
ATOM   7083  C  CA    . SER B  1  217 ? -17.097 48.381  11.108 1.00 56.54  ? 1016 SER D CA    1 
ATOM   7084  C  C     . SER B  1  217 ? -16.067 47.893  12.099 1.00 49.84  ? 1016 SER D C     1 
ATOM   7085  O  O     . SER B  1  217 ? -16.353 46.997  12.855 1.00 46.55  ? 1016 SER D O     1 
ATOM   7086  C  CB    . SER B  1  217 ? -16.922 47.619  9.816  1.00 52.56  ? 1016 SER D CB    1 
ATOM   7087  O  OG    . SER B  1  217 ? -18.006 47.901  8.976  1.00 61.69  ? 1016 SER D OG    1 
ATOM   7088  N  N     . GLU B  1  218 ? -14.877 48.489  12.027 1.00 48.34  ? 1017 GLU D N     1 
ATOM   7089  C  CA    . GLU B  1  218 ? -13.774 48.266  12.926 1.00 47.22  ? 1017 GLU D CA    1 
ATOM   7090  C  C     . GLU B  1  218 ? -14.114 48.692  14.335 1.00 52.36  ? 1017 GLU D C     1 
ATOM   7091  O  O     . GLU B  1  218 ? -13.773 47.994  15.246 1.00 52.54  ? 1017 GLU D O     1 
ATOM   7092  C  CB    . GLU B  1  218 ? -12.579 49.091  12.427 1.00 49.24  ? 1017 GLU D CB    1 
ATOM   7093  C  CG    . GLU B  1  218 ? -11.290 48.914  13.199 1.00 49.79  ? 1017 GLU D CG    1 
ATOM   7094  C  CD    . GLU B  1  218 ? -10.944 47.447  13.412 1.00 49.89  ? 1017 GLU D CD    1 
ATOM   7095  O  OE1   . GLU B  1  218 ? -11.023 46.629  12.471 1.00 46.51  ? 1017 GLU D OE1   1 
ATOM   7096  O  OE2   . GLU B  1  218 ? -10.592 47.125  14.551 1.00 55.80  ? 1017 GLU D OE2   1 
ATOM   7097  N  N     . MET B  1  219 ? -14.760 49.844  14.512 1.00 51.79  ? 1018 MET D N     1 
ATOM   7098  C  CA    . MET B  1  219 ? -15.106 50.277  15.852 1.00 47.63  ? 1018 MET D CA    1 
ATOM   7099  C  C     . MET B  1  219 ? -16.145 49.385  16.440 1.00 46.18  ? 1018 MET D C     1 
ATOM   7100  O  O     . MET B  1  219 ? -16.008 49.000  17.563 1.00 46.23  ? 1018 MET D O     1 
ATOM   7101  C  CB    . MET B  1  219 ? -15.608 51.673  15.823 1.00 46.96  ? 1018 MET D CB    1 
ATOM   7102  C  CG    . MET B  1  219 ? -14.508 52.648  15.482 1.00 46.88  ? 1018 MET D CG    1 
ATOM   7103  S  SD    . MET B  1  219 ? -13.398 52.887  16.867 1.00 44.45  ? 1018 MET D SD    1 
ATOM   7104  C  CE    . MET B  1  219 ? -14.553 53.299  18.163 1.00 45.31  ? 1018 MET D CE    1 
ATOM   7105  N  N     . ARG B  1  220 ? -17.160 49.037  15.665 1.00 47.31  ? 1019 ARG D N     1 
ATOM   7106  C  CA    . ARG B  1  220 ? -18.268 48.218  16.169 1.00 46.34  ? 1019 ARG D CA    1 
ATOM   7107  C  C     . ARG B  1  220 ? -17.807 46.847  16.583 1.00 44.02  ? 1019 ARG D C     1 
ATOM   7108  O  O     . ARG B  1  220 ? -18.194 46.368  17.628 1.00 40.54  ? 1019 ARG D O     1 
ATOM   7109  C  CB    . ARG B  1  220 ? -19.358 48.072  15.106 1.00 43.61  ? 1019 ARG D CB    1 
ATOM   7110  C  CG    . ARG B  1  220 ? -20.203 49.315  14.916 1.00 48.91  ? 1019 ARG D CG    1 
ATOM   7111  C  CD    . ARG B  1  220 ? -21.183 49.183  13.752 1.00 44.96  ? 1019 ARG D CD    1 
ATOM   7112  N  NE    . ARG B  1  220 ? -22.496 49.561  14.214 1.00 65.30  ? 1019 ARG D NE    1 
ATOM   7113  C  CZ    . ARG B  1  220 ? -23.492 48.699  14.444 1.00 73.82  ? 1019 ARG D CZ    1 
ATOM   7114  N  NH1   . ARG B  1  220 ? -24.637 49.178  14.907 1.00 69.30  ? 1019 ARG D NH1   1 
ATOM   7115  N  NH2   . ARG B  1  220 ? -23.363 47.370  14.203 1.00 67.22  ? 1019 ARG D NH2   1 
ATOM   7116  N  N     . GLU B  1  221 ? -16.999 46.212  15.751 1.00 39.82  ? 1020 GLU D N     1 
ATOM   7117  C  CA    . GLU B  1  221 ? -16.521 44.895  16.058 1.00 43.69  ? 1020 GLU D CA    1 
ATOM   7118  C  C     . GLU B  1  221 ? -15.469 44.885  17.133 1.00 42.92  ? 1020 GLU D C     1 
ATOM   7119  O  O     . GLU B  1  221 ? -15.497 44.001  17.945 1.00 36.88  ? 1020 GLU D O     1 
ATOM   7120  C  CB    . GLU B  1  221 ? -15.969 44.237  14.831 1.00 49.69  ? 1020 GLU D CB    1 
ATOM   7121  C  CG    . GLU B  1  221 ? -16.988 44.206  13.722 1.00 66.49  ? 1020 GLU D CG    1 
ATOM   7122  C  CD    . GLU B  1  221 ? -16.535 43.422  12.513 1.00 77.50  ? 1020 GLU D CD    1 
ATOM   7123  O  OE1   . GLU B  1  221 ? -17.255 43.515  11.497 1.00 94.85  ? 1020 GLU D OE1   1 
ATOM   7124  O  OE2   . GLU B  1  221 ? -15.495 42.706  12.565 1.00 84.85  ? 1020 GLU D OE2   1 
ATOM   7125  N  N     . SER B  1  222 ? -14.560 45.848  17.147 1.00 40.74  ? 1021 SER D N     1 
ATOM   7126  C  CA    . SER B  1  222 ? -13.569 45.863  18.164 1.00 39.08  ? 1021 SER D CA    1 
ATOM   7127  C  C     . SER B  1  222 ? -14.121 46.193  19.526 1.00 39.86  ? 1021 SER D C     1 
ATOM   7128  O  O     . SER B  1  222 ? -13.711 45.592  20.493 1.00 37.70  ? 1021 SER D O     1 
ATOM   7129  C  CB    . SER B  1  222 ? -12.523 46.872  17.823 1.00 40.83  ? 1021 SER D CB    1 
ATOM   7130  O  OG    . SER B  1  222 ? -11.615 46.257  16.966 1.00 41.91  ? 1021 SER D OG    1 
ATOM   7131  N  N     . PHE B  1  223 ? -15.016 47.168  19.597 1.00 39.05  ? 1022 PHE D N     1 
ATOM   7132  C  CA    . PHE B  1  223 ? -15.635 47.518  20.840 1.00 37.67  ? 1022 PHE D CA    1 
ATOM   7133  C  C     . PHE B  1  223 ? -16.528 46.419  21.398 1.00 39.17  ? 1022 PHE D C     1 
ATOM   7134  O  O     . PHE B  1  223 ? -16.539 46.229  22.598 1.00 40.22  ? 1022 PHE D O     1 
ATOM   7135  C  CB    . PHE B  1  223 ? -16.416 48.827  20.719 1.00 33.01  ? 1022 PHE D CB    1 
ATOM   7136  C  CG    . PHE B  1  223 ? -16.661 49.440  22.017 1.00 34.21  ? 1022 PHE D CG    1 
ATOM   7137  C  CD1   . PHE B  1  223 ? -15.623 50.108  22.672 1.00 32.54  ? 1022 PHE D CD1   1 
ATOM   7138  C  CD2   . PHE B  1  223 ? -17.902 49.284  22.652 1.00 34.44  ? 1022 PHE D CD2   1 
ATOM   7139  C  CE1   . PHE B  1  223 ? -15.841 50.654  23.942 1.00 34.52  ? 1022 PHE D CE1   1 
ATOM   7140  C  CE2   . PHE B  1  223 ? -18.117 49.844  23.889 1.00 30.95  ? 1022 PHE D CE2   1 
ATOM   7141  C  CZ    . PHE B  1  223 ? -17.081 50.520  24.541 1.00 33.01  ? 1022 PHE D CZ    1 
ATOM   7142  N  N     . LEU B  1  224 ? -17.286 45.733  20.550 1.00 39.12  ? 1023 LEU D N     1 
ATOM   7143  C  CA    . LEU B  1  224 ? -18.146 44.677  21.008 1.00 41.64  ? 1023 LEU D CA    1 
ATOM   7144  C  C     . LEU B  1  224 ? -17.292 43.530  21.553 1.00 42.58  ? 1023 LEU D C     1 
ATOM   7145  O  O     . LEU B  1  224 ? -17.667 42.842  22.488 1.00 38.95  ? 1023 LEU D O     1 
ATOM   7146  C  CB    . LEU B  1  224 ? -18.963 44.171  19.828 1.00 42.12  ? 1023 LEU D CB    1 
ATOM   7147  C  CG    . LEU B  1  224 ? -19.907 43.032  20.162 1.00 43.97  ? 1023 LEU D CG    1 
ATOM   7148  C  CD1   . LEU B  1  224 ? -21.029 43.515  21.084 1.00 48.90  ? 1023 LEU D CD1   1 
ATOM   7149  C  CD2   . LEU B  1  224 ? -20.432 42.425  18.877 1.00 46.23  ? 1023 LEU D CD2   1 
ATOM   7150  N  N     . ASP B  1  225 ? -16.146 43.319  20.941 1.00 38.91  ? 1024 ASP D N     1 
ATOM   7151  C  CA    . ASP B  1  225 ? -15.267 42.303  21.369 1.00 40.13  ? 1024 ASP D CA    1 
ATOM   7152  C  C     . ASP B  1  225 ? -14.773 42.547  22.767 1.00 36.69  ? 1024 ASP D C     1 
ATOM   7153  O  O     . ASP B  1  225 ? -14.787 41.635  23.569 1.00 36.31  ? 1024 ASP D O     1 
ATOM   7154  C  CB    . ASP B  1  225 ? -14.105 42.280  20.410 1.00 48.82  ? 1024 ASP D CB    1 
ATOM   7155  C  CG    . ASP B  1  225 ? -13.389 40.972  20.450 1.00 66.35  ? 1024 ASP D CG    1 
ATOM   7156  O  OD1   . ASP B  1  225 ? -14.084 39.927  20.514 1.00 80.03  ? 1024 ASP D OD1   1 
ATOM   7157  O  OD2   . ASP B  1  225 ? -12.132 40.957  20.448 1.00 75.58  ? 1024 ASP D OD2   1 
ATOM   7158  N  N     . TYR B  1  226 ? -14.327 43.784  23.040 1.00 33.09  ? 1025 TYR D N     1 
ATOM   7159  C  CA    . TYR B  1  226 ? -13.921 44.191  24.351 1.00 34.68  ? 1025 TYR D CA    1 
ATOM   7160  C  C     . TYR B  1  226 ? -15.041 44.178  25.363 1.00 36.59  ? 1025 TYR D C     1 
ATOM   7161  O  O     . TYR B  1  226 ? -14.864 43.647  26.446 1.00 40.97  ? 1025 TYR D O     1 
ATOM   7162  C  CB    . TYR B  1  226 ? -13.315 45.573  24.307 1.00 33.34  ? 1025 TYR D CB    1 
ATOM   7163  C  CG    . TYR B  1  226 ? -12.950 46.079  25.644 1.00 34.19  ? 1025 TYR D CG    1 
ATOM   7164  C  CD1   . TYR B  1  226 ? -11.859 45.532  26.299 1.00 35.04  ? 1025 TYR D CD1   1 
ATOM   7165  C  CD2   . TYR B  1  226 ? -13.642 47.139  26.229 1.00 34.12  ? 1025 TYR D CD2   1 
ATOM   7166  C  CE1   . TYR B  1  226 ? -11.454 45.988  27.515 1.00 32.85  ? 1025 TYR D CE1   1 
ATOM   7167  C  CE2   . TYR B  1  226 ? -13.231 47.623  27.459 1.00 32.42  ? 1025 TYR D CE2   1 
ATOM   7168  C  CZ    . TYR B  1  226 ? -12.151 47.011  28.087 1.00 34.37  ? 1025 TYR D CZ    1 
ATOM   7169  O  OH    . TYR B  1  226 ? -11.709 47.399  29.296 1.00 35.59  ? 1025 TYR D OH    1 
ATOM   7170  N  N     . ALA B  1  227 ? -16.188 44.762  24.996 1.00 35.47  ? 1026 ALA D N     1 
ATOM   7171  C  CA    . ALA B  1  227 ? -17.301 44.936  25.892 1.00 32.22  ? 1026 ALA D CA    1 
ATOM   7172  C  C     . ALA B  1  227 ? -17.841 43.604  26.340 1.00 31.85  ? 1026 ALA D C     1 
ATOM   7173  O  O     . ALA B  1  227 ? -18.201 43.434  27.463 1.00 37.28  ? 1026 ALA D O     1 
ATOM   7174  C  CB    . ALA B  1  227 ? -18.401 45.749  25.221 1.00 28.85  ? 1026 ALA D CB    1 
ATOM   7175  N  N     . MET B  1  228 ? -17.963 42.680  25.417 1.00 33.07  ? 1027 MET D N     1 
ATOM   7176  C  CA    . MET B  1  228 ? -18.480 41.352  25.693 1.00 36.54  ? 1027 MET D CA    1 
ATOM   7177  C  C     . MET B  1  228 ? -17.568 40.649  26.676 1.00 33.64  ? 1027 MET D C     1 
ATOM   7178  O  O     . MET B  1  228 ? -18.050 40.016  27.640 1.00 32.36  ? 1027 MET D O     1 
ATOM   7179  C  CB    . MET B  1  228 ? -18.562 40.500  24.412 1.00 41.07  ? 1027 MET D CB    1 
ATOM   7180  C  CG    . MET B  1  228 ? -19.926 40.464  23.737 1.00 54.93  ? 1027 MET D CG    1 
ATOM   7181  S  SD    . MET B  1  228 ? -20.275 38.816  23.024 1.00 68.55  ? 1027 MET D SD    1 
ATOM   7182  C  CE    . MET B  1  228 ? -19.407 37.696  24.142 1.00 50.01  ? 1027 MET D CE    1 
ATOM   7183  N  N     . SER B  1  229 ? -16.269 40.757  26.432 1.00 29.21  ? 1028 SER D N     1 
ATOM   7184  C  CA    . SER B  1  229 ? -15.285 40.054  27.231 1.00 31.68  ? 1028 SER D CA    1 
ATOM   7185  C  C     . SER B  1  229 ? -15.337 40.521  28.683 1.00 31.07  ? 1028 SER D C     1 
ATOM   7186  O  O     . SER B  1  229 ? -15.227 39.720  29.587 1.00 29.70  ? 1028 SER D O     1 
ATOM   7187  C  CB    . SER B  1  229 ? -13.879 40.290  26.640 1.00 28.40  ? 1028 SER D CB    1 
ATOM   7188  O  OG    . SER B  1  229 ? -12.953 39.438  27.270 1.00 31.93  ? 1028 SER D OG    1 
ATOM   7189  N  N     . VAL B  1  230 ? -15.510 41.829  28.882 1.00 30.47  ? 1029 VAL D N     1 
ATOM   7190  C  CA    . VAL B  1  230 ? -15.563 42.403  30.202 1.00 28.76  ? 1029 VAL D CA    1 
ATOM   7191  C  C     . VAL B  1  230 ? -16.809 41.949  30.944 1.00 24.94  ? 1029 VAL D C     1 
ATOM   7192  O  O     . VAL B  1  230 ? -16.753 41.686  32.111 1.00 29.05  ? 1029 VAL D O     1 
ATOM   7193  C  CB    . VAL B  1  230 ? -15.509 43.941  30.121 1.00 30.56  ? 1029 VAL D CB    1 
ATOM   7194  C  CG1   . VAL B  1  230 ? -15.667 44.562  31.500 1.00 31.52  ? 1029 VAL D CG1   1 
ATOM   7195  C  CG2   . VAL B  1  230 ? -14.149 44.346  29.575 1.00 32.43  ? 1029 VAL D CG2   1 
ATOM   7196  N  N     . ILE B  1  231 ? -17.936 41.904  30.294 1.00 27.80  ? 1030 ILE D N     1 
ATOM   7197  C  CA    . ILE B  1  231 ? -19.168 41.403  30.900 1.00 25.53  ? 1030 ILE D CA    1 
ATOM   7198  C  C     . ILE B  1  231 ? -19.114 39.928  31.251 1.00 28.28  ? 1030 ILE D C     1 
ATOM   7199  O  O     . ILE B  1  231 ? -19.485 39.560  32.370 1.00 31.22  ? 1030 ILE D O     1 
ATOM   7200  C  CB    . ILE B  1  231 ? -20.310 41.668  29.936 1.00 25.94  ? 1030 ILE D CB    1 
ATOM   7201  C  CG1   . ILE B  1  231 ? -20.559 43.162  29.887 1.00 26.50  ? 1030 ILE D CG1   1 
ATOM   7202  C  CG2   . ILE B  1  231 ? -21.589 40.952  30.344 1.00 28.27  ? 1030 ILE D CG2   1 
ATOM   7203  C  CD1   . ILE B  1  231 ? -21.336 43.594  28.656 1.00 30.83  ? 1030 ILE D CD1   1 
ATOM   7204  N  N     . VAL B  1  232 ? -18.696 39.067  30.329 1.00 26.75  ? 1031 VAL D N     1 
ATOM   7205  C  CA    . VAL B  1  232 ? -18.758 37.615  30.626 1.00 29.85  ? 1031 VAL D CA    1 
ATOM   7206  C  C     . VAL B  1  232 ? -17.486 37.011  31.171 1.00 29.24  ? 1031 VAL D C     1 
ATOM   7207  O  O     . VAL B  1  232 ? -17.502 35.864  31.645 1.00 35.29  ? 1031 VAL D O     1 
ATOM   7208  C  CB    . VAL B  1  232 ? -19.242 36.793  29.428 1.00 32.06  ? 1031 VAL D CB    1 
ATOM   7209  C  CG1   . VAL B  1  232 ? -20.360 37.542  28.682 1.00 34.08  ? 1031 VAL D CG1   1 
ATOM   7210  C  CG2   . VAL B  1  232 ? -18.112 36.546  28.458 1.00 27.83  ? 1031 VAL D CG2   1 
ATOM   7211  N  N     . ALA B  1  233 ? -16.377 37.737  31.140 1.00 29.46  ? 1032 ALA D N     1 
ATOM   7212  C  CA    . ALA B  1  233 ? -15.123 37.123  31.582 1.00 29.55  ? 1032 ALA D CA    1 
ATOM   7213  C  C     . ALA B  1  233 ? -14.218 38.151  32.294 1.00 30.88  ? 1032 ALA D C     1 
ATOM   7214  O  O     . ALA B  1  233 ? -12.992 38.190  32.057 1.00 30.96  ? 1032 ALA D O     1 
ATOM   7215  C  CB    . ALA B  1  233 ? -14.419 36.510  30.363 1.00 28.46  ? 1032 ALA D CB    1 
ATOM   7216  N  N     . ARG B  1  234 ? -14.797 38.962  33.172 1.00 31.63  ? 1033 ARG D N     1 
ATOM   7217  C  CA    . ARG B  1  234 ? -13.998 39.871  33.945 1.00 29.30  ? 1033 ARG D CA    1 
ATOM   7218  C  C     . ARG B  1  234 ? -14.715 40.505  35.131 1.00 32.56  ? 1033 ARG D C     1 
ATOM   7219  O  O     . ARG B  1  234 ? -14.321 40.264  36.269 1.00 30.19  ? 1033 ARG D O     1 
ATOM   7220  C  CB    . ARG B  1  234 ? -13.362 40.982  33.051 1.00 25.98  ? 1033 ARG D CB    1 
ATOM   7221  C  CG    . ARG B  1  234 ? -12.367 41.820  33.836 1.00 25.81  ? 1033 ARG D CG    1 
ATOM   7222  C  CD    . ARG B  1  234 ? -11.559 42.839  33.048 1.00 28.01  ? 1033 ARG D CD    1 
ATOM   7223  N  NE    . ARG B  1  234 ? -10.834 42.135  31.981 1.00 36.27  ? 1033 ARG D NE    1 
ATOM   7224  C  CZ    . ARG B  1  234 ? -10.116 42.664  30.984 1.00 32.08  ? 1033 ARG D CZ    1 
ATOM   7225  N  NH1   . ARG B  1  234 ? -9.935  43.984  30.850 1.00 28.06  ? 1033 ARG D NH1   1 
ATOM   7226  N  NH2   . ARG B  1  234 ? -9.541  41.812  30.127 1.00 34.41  ? 1033 ARG D NH2   1 
ATOM   7227  N  N     . ALA B  1  235 ? -15.695 41.386  34.860 1.00 31.05  ? 1034 ALA D N     1 
ATOM   7228  C  CA    . ALA B  1  235 ? -16.230 42.314  35.891 1.00 25.62  ? 1034 ALA D CA    1 
ATOM   7229  C  C     . ALA B  1  235 ? -17.439 41.822  36.623 1.00 29.41  ? 1034 ALA D C     1 
ATOM   7230  O  O     . ALA B  1  235 ? -17.734 42.341  37.705 1.00 33.16  ? 1034 ALA D O     1 
ATOM   7231  C  CB    . ALA B  1  235 ? -16.475 43.716  35.353 1.00 23.86  ? 1034 ALA D CB    1 
ATOM   7232  N  N     . LEU B  1  236 ? -18.128 40.811  36.104 1.00 29.63  ? 1035 LEU D N     1 
ATOM   7233  C  CA    . LEU B  1  236 ? -19.354 40.318  36.727 1.00 30.38  ? 1035 LEU D CA    1 
ATOM   7234  C  C     . LEU B  1  236 ? -19.224 38.927  37.323 1.00 33.93  ? 1035 LEU D C     1 
ATOM   7235  O  O     . LEU B  1  236 ? -18.577 38.067  36.742 1.00 31.77  ? 1035 LEU D O     1 
ATOM   7236  C  CB    . LEU B  1  236 ? -20.529 40.332  35.757 1.00 29.72  ? 1035 LEU D CB    1 
ATOM   7237  C  CG    . LEU B  1  236 ? -20.826 41.716  35.135 1.00 34.29  ? 1035 LEU D CG    1 
ATOM   7238  C  CD1   . LEU B  1  236 ? -21.900 41.628  34.051 1.00 32.62  ? 1035 LEU D CD1   1 
ATOM   7239  C  CD2   . LEU B  1  236 ? -21.179 42.777  36.191 1.00 35.77  ? 1035 LEU D CD2   1 
ATOM   7240  N  N     . PRO B  1  237 ? -19.858 38.693  38.488 1.00 34.35  ? 1036 PRO D N     1 
ATOM   7241  C  CA    . PRO B  1  237 ? -19.771 37.344  39.044 1.00 32.57  ? 1036 PRO D CA    1 
ATOM   7242  C  C     . PRO B  1  237 ? -20.780 36.376  38.397 1.00 27.70  ? 1036 PRO D C     1 
ATOM   7243  O  O     . PRO B  1  237 ? -21.808 36.792  37.807 1.00 28.60  ? 1036 PRO D O     1 
ATOM   7244  C  CB    . PRO B  1  237 ? -20.131 37.572  40.522 1.00 32.56  ? 1036 PRO D CB    1 
ATOM   7245  C  CG    . PRO B  1  237 ? -21.149 38.699  40.437 1.00 31.68  ? 1036 PRO D CG    1 
ATOM   7246  C  CD    . PRO B  1  237 ? -20.677 39.592  39.336 1.00 31.22  ? 1036 PRO D CD    1 
ATOM   7247  N  N     . ASP B  1  238 ? -20.495 35.096  38.509 1.00 24.28  ? 1037 ASP D N     1 
ATOM   7248  C  CA    . ASP B  1  238 ? -21.456 34.098  38.078 1.00 25.57  ? 1037 ASP D CA    1 
ATOM   7249  C  C     . ASP B  1  238 ? -22.476 33.943  39.204 1.00 25.47  ? 1037 ASP D C     1 
ATOM   7250  O  O     . ASP B  1  238 ? -22.114 33.925  40.372 1.00 25.45  ? 1037 ASP D O     1 
ATOM   7251  C  CB    . ASP B  1  238 ? -20.720 32.769  37.796 1.00 27.23  ? 1037 ASP D CB    1 
ATOM   7252  C  CG    . ASP B  1  238 ? -21.599 31.756  37.125 1.00 30.08  ? 1037 ASP D CG    1 
ATOM   7253  O  OD1   . ASP B  1  238 ? -22.532 31.247  37.791 1.00 30.42  ? 1037 ASP D OD1   1 
ATOM   7254  O  OD2   . ASP B  1  238 ? -21.375 31.491  35.911 1.00 34.96  ? 1037 ASP D OD2   1 
ATOM   7255  N  N     . VAL B  1  239 ? -23.738 33.779  38.852 1.00 27.21  ? 1038 VAL D N     1 
ATOM   7256  C  CA    . VAL B  1  239 ? -24.793 33.626  39.847 1.00 28.33  ? 1038 VAL D CA    1 
ATOM   7257  C  C     . VAL B  1  239 ? -24.621 32.355  40.672 1.00 32.03  ? 1038 VAL D C     1 
ATOM   7258  O  O     . VAL B  1  239 ? -24.975 32.319  41.844 1.00 31.49  ? 1038 VAL D O     1 
ATOM   7259  C  CB    . VAL B  1  239 ? -26.196 33.598  39.180 1.00 29.42  ? 1038 VAL D CB    1 
ATOM   7260  C  CG1   . VAL B  1  239 ? -26.479 32.263  38.495 1.00 24.89  ? 1038 VAL D CG1   1 
ATOM   7261  C  CG2   . VAL B  1  239 ? -27.276 33.916  40.178 1.00 26.53  ? 1038 VAL D CG2   1 
ATOM   7262  N  N     . ARG B  1  240 ? -24.069 31.314  40.068 1.00 30.42  ? 1039 ARG D N     1 
ATOM   7263  C  CA    . ARG B  1  240 ? -23.928 30.021  40.753 1.00 34.76  ? 1039 ARG D CA    1 
ATOM   7264  C  C     . ARG B  1  240 ? -22.875 29.992  41.866 1.00 35.83  ? 1039 ARG D C     1 
ATOM   7265  O  O     . ARG B  1  240 ? -23.154 29.451  42.948 1.00 33.60  ? 1039 ARG D O     1 
ATOM   7266  C  CB    . ARG B  1  240 ? -23.645 28.899  39.752 1.00 32.95  ? 1039 ARG D CB    1 
ATOM   7267  C  CG    . ARG B  1  240 ? -24.761 28.701  38.735 1.00 32.68  ? 1039 ARG D CG    1 
ATOM   7268  C  CD    . ARG B  1  240 ? -24.279 27.882  37.549 1.00 32.94  ? 1039 ARG D CD    1 
ATOM   7269  N  NE    . ARG B  1  240 ? -23.275 28.619  36.769 1.00 35.11  ? 1039 ARG D NE    1 
ATOM   7270  C  CZ    . ARG B  1  240 ? -22.547 28.088  35.791 1.00 31.11  ? 1039 ARG D CZ    1 
ATOM   7271  N  NH1   . ARG B  1  240 ? -22.689 26.810  35.474 1.00 28.54  ? 1039 ARG D NH1   1 
ATOM   7272  N  NH2   . ARG B  1  240 ? -21.665 28.828  35.149 1.00 23.00  ? 1039 ARG D NH2   1 
ATOM   7273  N  N     . ASP B  1  241 ? -21.684 30.561  41.633 1.00 34.19  ? 1040 ASP D N     1 
ATOM   7274  C  CA    . ASP B  1  241 ? -20.661 30.508  42.693 1.00 36.23  ? 1040 ASP D CA    1 
ATOM   7275  C  C     . ASP B  1  241 ? -20.232 31.867  43.235 1.00 31.05  ? 1040 ASP D C     1 
ATOM   7276  O  O     . ASP B  1  241 ? -19.376 31.952  44.115 1.00 33.02  ? 1040 ASP D O     1 
ATOM   7277  C  CB    . ASP B  1  241 ? -19.429 29.685  42.227 1.00 33.47  ? 1040 ASP D CB    1 
ATOM   7278  C  CG    . ASP B  1  241 ? -18.664 30.320  41.083 1.00 34.47  ? 1040 ASP D CG    1 
ATOM   7279  O  OD1   . ASP B  1  241 ? -18.983 31.460  40.684 1.00 30.90  ? 1040 ASP D OD1   1 
ATOM   7280  O  OD2   . ASP B  1  241 ? -17.709 29.655  40.588 1.00 32.93  ? 1040 ASP D OD2   1 
ATOM   7281  N  N     . GLY B  1  242 ? -20.840 32.913  42.700 1.00 30.05  ? 1041 GLY D N     1 
ATOM   7282  C  CA    . GLY B  1  242 ? -20.586 34.288  43.094 1.00 28.81  ? 1041 GLY D CA    1 
ATOM   7283  C  C     . GLY B  1  242 ? -19.201 34.797  42.725 1.00 31.56  ? 1041 GLY D C     1 
ATOM   7284  O  O     . GLY B  1  242 ? -18.756 35.823  43.289 1.00 30.33  ? 1041 GLY D O     1 
ATOM   7285  N  N     . LEU B  1  243 ? -18.513 34.123  41.791 1.00 28.57  ? 1042 LEU D N     1 
ATOM   7286  C  CA    . LEU B  1  243 ? -17.127 34.511  41.497 1.00 28.38  ? 1042 LEU D CA    1 
ATOM   7287  C  C     . LEU B  1  243 ? -16.934 35.140  40.139 1.00 30.65  ? 1042 LEU D C     1 
ATOM   7288  O  O     . LEU B  1  243 ? -17.658 34.827  39.207 1.00 27.83  ? 1042 LEU D O     1 
ATOM   7289  C  CB    . LEU B  1  243 ? -16.200 33.301  41.633 1.00 27.26  ? 1042 LEU D CB    1 
ATOM   7290  C  CG    . LEU B  1  243 ? -16.186 32.609  42.989 1.00 28.18  ? 1042 LEU D CG    1 
ATOM   7291  C  CD1   . LEU B  1  243 ? -15.382 31.297  42.919 1.00 24.28  ? 1042 LEU D CD1   1 
ATOM   7292  C  CD2   . LEU B  1  243 ? -15.642 33.531  44.093 1.00 24.81  ? 1042 LEU D CD2   1 
ATOM   7293  N  N     . LYS B  1  244 ? -15.938 36.017  40.016 1.00 33.48  ? 1043 LYS D N     1 
ATOM   7294  C  CA    . LYS B  1  244 ? -15.466 36.509  38.730 1.00 29.44  ? 1043 LYS D CA    1 
ATOM   7295  C  C     . LYS B  1  244 ? -14.337 35.565  38.352 1.00 31.88  ? 1043 LYS D C     1 
ATOM   7296  O  O     . LYS B  1  244 ? -13.818 34.895  39.274 1.00 35.10  ? 1043 LYS D O     1 
ATOM   7297  C  CB    . LYS B  1  244 ? -14.861 37.926  38.923 1.00 25.97  ? 1043 LYS D CB    1 
ATOM   7298  C  CG    . LYS B  1  244 ? -15.864 39.028  39.315 1.00 28.93  ? 1043 LYS D CG    1 
ATOM   7299  C  CD    . LYS B  1  244 ? -15.172 40.384  39.444 1.00 27.89  ? 1043 LYS D CD    1 
ATOM   7300  C  CE    . LYS B  1  244 ? -16.012 41.364  40.161 1.00 27.94  ? 1043 LYS D CE    1 
ATOM   7301  N  NZ    . LYS B  1  244 ? -15.252 42.667  40.416 1.00 32.89  ? 1043 LYS D NZ    1 
ATOM   7302  N  N     . PRO B  1  245 ? -13.914 35.548  37.036 1.00 31.94  ? 1044 PRO D N     1 
ATOM   7303  C  CA    . PRO B  1  245 ? -12.796 34.650  36.698 1.00 33.74  ? 1044 PRO D CA    1 
ATOM   7304  C  C     . PRO B  1  245 ? -11.525 34.763  37.513 1.00 32.15  ? 1044 PRO D C     1 
ATOM   7305  O  O     . PRO B  1  245 ? -10.944 33.737  37.778 1.00 32.87  ? 1044 PRO D O     1 
ATOM   7306  C  CB    . PRO B  1  245 ? -12.460 35.047  35.235 1.00 29.89  ? 1044 PRO D CB    1 
ATOM   7307  C  CG    . PRO B  1  245 ? -13.803 35.391  34.720 1.00 28.13  ? 1044 PRO D CG    1 
ATOM   7308  C  CD    . PRO B  1  245 ? -14.342 36.269  35.798 1.00 28.87  ? 1044 PRO D CD    1 
ATOM   7309  N  N     . VAL B  1  246 ? -11.066 35.969  37.852 1.00 26.64  ? 1045 VAL D N     1 
ATOM   7310  C  CA    . VAL B  1  246 ? -9.788  36.067  38.527 1.00 24.99  ? 1045 VAL D CA    1 
ATOM   7311  C  C     . VAL B  1  246 ? -9.913  35.404  39.921 1.00 26.39  ? 1045 VAL D C     1 
ATOM   7312  O  O     . VAL B  1  246 ? -8.999  34.724  40.384 1.00 27.62  ? 1045 VAL D O     1 
ATOM   7313  C  CB    . VAL B  1  246 ? -9.280  37.527  38.653 1.00 24.22  ? 1045 VAL D CB    1 
ATOM   7314  C  CG1   . VAL B  1  246 ? -10.162 38.361  39.586 1.00 22.60  ? 1045 VAL D CG1   1 
ATOM   7315  C  CG2   . VAL B  1  246 ? -7.854  37.497  39.202 1.00 22.34  ? 1045 VAL D CG2   1 
ATOM   7316  N  N     . HIS B  1  247 ? -11.062 35.575  40.575 1.00 27.18  ? 1046 HIS D N     1 
ATOM   7317  C  CA    . HIS B  1  247 ? -11.262 34.897  41.894 1.00 26.80  ? 1046 HIS D CA    1 
ATOM   7318  C  C     . HIS B  1  247 ? -11.346 33.389  41.774 1.00 26.50  ? 1046 HIS D C     1 
ATOM   7319  O  O     . HIS B  1  247 ? -10.760 32.664  42.577 1.00 25.75  ? 1046 HIS D O     1 
ATOM   7320  C  CB    . HIS B  1  247 ? -12.468 35.439  42.584 1.00 30.95  ? 1046 HIS D CB    1 
ATOM   7321  C  CG    . HIS B  1  247 ? -12.400 36.914  42.793 1.00 34.24  ? 1046 HIS D CG    1 
ATOM   7322  N  ND1   . HIS B  1  247 ? -12.981 37.791  41.915 1.00 38.40  ? 1046 HIS D ND1   1 
ATOM   7323  C  CD2   . HIS B  1  247 ? -11.785 37.671  43.736 1.00 38.65  ? 1046 HIS D CD2   1 
ATOM   7324  C  CE1   . HIS B  1  247 ? -12.727 39.032  42.297 1.00 40.73  ? 1046 HIS D CE1   1 
ATOM   7325  N  NE2   . HIS B  1  247 ? -11.986 38.988  43.394 1.00 37.61  ? 1046 HIS D NE2   1 
ATOM   7326  N  N     . ARG B  1  248 ? -12.059 32.923  40.749 1.00 26.29  ? 1047 ARG D N     1 
ATOM   7327  C  CA    . ARG B  1  248 ? -12.248 31.487  40.588 1.00 25.94  ? 1047 ARG D CA    1 
ATOM   7328  C  C     . ARG B  1  248 ? -10.859 30.847  40.283 1.00 28.66  ? 1047 ARG D C     1 
ATOM   7329  O  O     . ARG B  1  248 ? -10.520 29.821  40.811 1.00 30.17  ? 1047 ARG D O     1 
ATOM   7330  C  CB    . ARG B  1  248 ? -13.189 31.227  39.443 1.00 24.09  ? 1047 ARG D CB    1 
ATOM   7331  C  CG    . ARG B  1  248 ? -13.658 29.791  39.413 1.00 22.33  ? 1047 ARG D CG    1 
ATOM   7332  C  CD    . ARG B  1  248 ? -14.696 29.597  38.340 1.00 22.96  ? 1047 ARG D CD    1 
ATOM   7333  N  NE    . ARG B  1  248 ? -15.937 30.336  38.618 1.00 25.07  ? 1047 ARG D NE    1 
ATOM   7334  C  CZ    . ARG B  1  248 ? -16.384 31.421  37.947 1.00 27.41  ? 1047 ARG D CZ    1 
ATOM   7335  N  NH1   . ARG B  1  248 ? -15.691 31.952  36.944 1.00 28.23  ? 1047 ARG D NH1   1 
ATOM   7336  N  NH2   . ARG B  1  248 ? -17.573 31.980  38.250 1.00 29.15  ? 1047 ARG D NH2   1 
ATOM   7337  N  N     . ARG B  1  249 ? -10.058 31.526  39.467 1.00 29.40  ? 1048 ARG D N     1 
ATOM   7338  C  CA    . ARG B  1  249 ? -8.721  31.062  39.130 1.00 29.83  ? 1048 ARG D CA    1 
ATOM   7339  C  C     . ARG B  1  249 ? -7.791  31.043  40.334 1.00 29.56  ? 1048 ARG D C     1 
ATOM   7340  O  O     . ARG B  1  249 ? -7.096  30.038  40.552 1.00 31.77  ? 1048 ARG D O     1 
ATOM   7341  C  CB    . ARG B  1  249 ? -8.150  31.865  37.979 1.00 31.51  ? 1048 ARG D CB    1 
ATOM   7342  C  CG    . ARG B  1  249 ? -8.821  31.490  36.673 1.00 28.76  ? 1048 ARG D CG    1 
ATOM   7343  C  CD    . ARG B  1  249 ? -8.548  32.512  35.573 1.00 28.52  ? 1048 ARG D CD    1 
ATOM   7344  N  NE    . ARG B  1  249 ? -9.189  32.070  34.310 1.00 27.84  ? 1048 ARG D NE    1 
ATOM   7345  C  CZ    . ARG B  1  249 ? -9.477  32.852  33.287 1.00 27.30  ? 1048 ARG D CZ    1 
ATOM   7346  N  NH1   . ARG B  1  249 ? -9.161  34.137  33.305 1.00 27.82  ? 1048 ARG D NH1   1 
ATOM   7347  N  NH2   . ARG B  1  249 ? -10.054 32.331  32.238 1.00 29.34  ? 1048 ARG D NH2   1 
ATOM   7348  N  N     . ILE B  1  250 ? -7.864  32.075  41.160 1.00 29.26  ? 1049 ILE D N     1 
ATOM   7349  C  CA    . ILE B  1  250 ? -7.097  32.111  42.407 1.00 27.87  ? 1049 ILE D CA    1 
ATOM   7350  C  C     . ILE B  1  250 ? -7.475  30.933  43.290 1.00 28.92  ? 1049 ILE D C     1 
ATOM   7351  O  O     . ILE B  1  250 ? -6.603  30.231  43.819 1.00 30.00  ? 1049 ILE D O     1 
ATOM   7352  C  CB    . ILE B  1  250 ? -7.311  33.399  43.193 1.00 23.28  ? 1049 ILE D CB    1 
ATOM   7353  C  CG1   . ILE B  1  250 ? -6.526  34.535  42.516 1.00 26.04  ? 1049 ILE D CG1   1 
ATOM   7354  C  CG2   . ILE B  1  250 ? -6.727  33.236  44.590 1.00 19.30  ? 1049 ILE D CG2   1 
ATOM   7355  C  CD1   . ILE B  1  250 ? -7.018  35.935  42.880 1.00 23.85  ? 1049 ILE D CD1   1 
ATOM   7356  N  N     . LEU B  1  251 ? -8.767  30.740  43.490 1.00 27.50  ? 1050 LEU D N     1 
ATOM   7357  C  CA    . LEU B  1  251 ? -9.159  29.696  44.402 1.00 27.95  ? 1050 LEU D CA    1 
ATOM   7358  C  C     . LEU B  1  251 ? -8.830  28.306  43.857 1.00 27.05  ? 1050 LEU D C     1 
ATOM   7359  O  O     . LEU B  1  251 ? -8.444  27.415  44.594 1.00 23.62  ? 1050 LEU D O     1 
ATOM   7360  C  CB    . LEU B  1  251 ? -10.635 29.856  44.750 1.00 31.75  ? 1050 LEU D CB    1 
ATOM   7361  C  CG    . LEU B  1  251 ? -10.983 31.137  45.512 1.00 29.78  ? 1050 LEU D CG    1 
ATOM   7362  C  CD1   . LEU B  1  251 ? -12.472 31.241  45.810 1.00 32.15  ? 1050 LEU D CD1   1 
ATOM   7363  C  CD2   . LEU B  1  251 ? -10.248 31.193  46.801 1.00 30.36  ? 1050 LEU D CD2   1 
ATOM   7364  N  N     . TYR B  1  252 ? -8.955  28.135  42.538 1.00 31.80  ? 1051 TYR D N     1 
ATOM   7365  C  CA    . TYR B  1  252 ? -8.645  26.870  41.927 1.00 31.98  ? 1051 TYR D CA    1 
ATOM   7366  C  C     . TYR B  1  252 ? -7.148  26.603  41.999 1.00 35.48  ? 1051 TYR D C     1 
ATOM   7367  O  O     . TYR B  1  252 ? -6.727  25.474  42.155 1.00 36.96  ? 1051 TYR D O     1 
ATOM   7368  C  CB    . TYR B  1  252 ? -9.103  26.866  40.508 1.00 34.06  ? 1051 TYR D CB    1 
ATOM   7369  C  CG    . TYR B  1  252 ? -8.860  25.553  39.832 1.00 33.18  ? 1051 TYR D CG    1 
ATOM   7370  C  CD1   . TYR B  1  252 ? -9.504  24.414  40.285 1.00 32.19  ? 1051 TYR D CD1   1 
ATOM   7371  C  CD2   . TYR B  1  252 ? -8.007  25.466  38.738 1.00 33.21  ? 1051 TYR D CD2   1 
ATOM   7372  C  CE1   . TYR B  1  252 ? -9.307  23.206  39.666 1.00 37.84  ? 1051 TYR D CE1   1 
ATOM   7373  C  CE2   . TYR B  1  252 ? -7.800  24.266  38.106 1.00 35.73  ? 1051 TYR D CE2   1 
ATOM   7374  C  CZ    . TYR B  1  252 ? -8.449  23.142  38.584 1.00 37.53  ? 1051 TYR D CZ    1 
ATOM   7375  O  OH    . TYR B  1  252 ? -8.257  21.956  37.954 1.00 42.02  ? 1051 TYR D OH    1 
ATOM   7376  N  N     . GLY B  1  253 ? -6.363  27.669  41.917 1.00 36.40  ? 1052 GLY D N     1 
ATOM   7377  C  CA    . GLY B  1  253 ? -4.930  27.607  42.026 1.00 36.81  ? 1052 GLY D CA    1 
ATOM   7378  C  C     . GLY B  1  253 ? -4.503  27.159  43.365 1.00 38.25  ? 1052 GLY D C     1 
ATOM   7379  O  O     . GLY B  1  253 ? -3.585  26.362  43.445 1.00 44.56  ? 1052 GLY D O     1 
ATOM   7380  N  N     . LEU B  1  254 ? -5.148  27.675  44.398 1.00 38.07  ? 1053 LEU D N     1 
ATOM   7381  C  CA    . LEU B  1  254 ? -4.891  27.207  45.760 1.00 41.30  ? 1053 LEU D CA    1 
ATOM   7382  C  C     . LEU B  1  254 ? -5.332  25.769  45.951 1.00 40.98  ? 1053 LEU D C     1 
ATOM   7383  O  O     . LEU B  1  254 ? -4.707  25.073  46.669 1.00 49.38  ? 1053 LEU D O     1 
ATOM   7384  C  CB    . LEU B  1  254 ? -5.569  28.074  46.821 1.00 38.44  ? 1053 LEU D CB    1 
ATOM   7385  C  CG    . LEU B  1  254 ? -5.180  29.544  46.961 1.00 38.06  ? 1053 LEU D CG    1 
ATOM   7386  C  CD1   . LEU B  1  254 ? -6.278  30.225  47.754 1.00 37.64  ? 1053 LEU D CD1   1 
ATOM   7387  C  CD2   . LEU B  1  254 ? -3.855  29.630  47.687 1.00 35.42  ? 1053 LEU D CD2   1 
ATOM   7388  N  N     . ASN B  1  255 ? -6.413  25.324  45.335 1.00 39.32  ? 1054 ASN D N     1 
ATOM   7389  C  CA    . ASN B  1  255 ? -6.802  23.925  45.451 1.00 43.66  ? 1054 ASN D CA    1 
ATOM   7390  C  C     . ASN B  1  255 ? -5.790  22.960  44.827 1.00 44.95  ? 1054 ASN D C     1 
ATOM   7391  O  O     . ASN B  1  255 ? -5.451  21.985  45.418 1.00 44.46  ? 1054 ASN D O     1 
ATOM   7392  C  CB    . ASN B  1  255 ? -8.128  23.724  44.780 1.00 38.58  ? 1054 ASN D CB    1 
ATOM   7393  C  CG    . ASN B  1  255 ? -8.773  22.445  45.195 1.00 41.29  ? 1054 ASN D CG    1 
ATOM   7394  O  OD1   . ASN B  1  255 ? -8.957  22.209  46.395 1.00 41.16  ? 1054 ASN D OD1   1 
ATOM   7395  N  ND2   . ASN B  1  255 ? -9.120  21.592  44.211 1.00 44.45  ? 1054 ASN D ND2   1 
ATOM   7396  N  N     . GLU B  1  256 ? -5.366  23.276  43.603 1.00 55.18  ? 1055 GLU D N     1 
ATOM   7397  C  CA    . GLU B  1  256 ? -4.425  22.488  42.807 1.00 59.61  ? 1055 GLU D CA    1 
ATOM   7398  C  C     . GLU B  1  256 ? -2.973  22.444  43.320 1.00 61.02  ? 1055 GLU D C     1 
ATOM   7399  O  O     . GLU B  1  256 ? -2.201  21.621  42.890 1.00 66.31  ? 1055 GLU D O     1 
ATOM   7400  C  CB    . GLU B  1  256 ? -4.419  22.971  41.354 1.00 55.22  ? 1055 GLU D CB    1 
ATOM   7401  C  CG    . GLU B  1  256 ? -5.606  22.520  40.510 1.00 61.61  ? 1055 GLU D CG    1 
ATOM   7402  C  CD    . GLU B  1  256 ? -6.032  21.085  40.759 1.00 59.62  ? 1055 GLU D CD    1 
ATOM   7403  O  OE1   . GLU B  1  256 ? -5.247  20.143  40.511 1.00 62.07  ? 1055 GLU D OE1   1 
ATOM   7404  O  OE2   . GLU B  1  256 ? -7.156  20.916  41.248 1.00 62.73  ? 1055 GLU D OE2   1 
ATOM   7405  N  N     A GLN B  1  257 ? -2.631  23.374  44.206 0.50 63.56  ? 1056 GLN D N     1 
ATOM   7406  N  N     B GLN B  1  257 ? -2.562  23.341  44.206 0.50 63.61  ? 1056 GLN D N     1 
ATOM   7407  C  CA    A GLN B  1  257 ? -1.343  23.333  44.888 0.50 65.10  ? 1056 GLN D CA    1 
ATOM   7408  C  CA    B GLN B  1  257 ? -1.263  23.174  44.866 0.50 65.25  ? 1056 GLN D CA    1 
ATOM   7409  C  C     A GLN B  1  257 ? -1.405  22.614  46.239 0.50 64.07  ? 1056 GLN D C     1 
ATOM   7410  C  C     B GLN B  1  257 ? -1.389  22.582  46.260 0.50 64.10  ? 1056 GLN D C     1 
ATOM   7411  O  O     A GLN B  1  257 ? -0.381  22.513  46.928 0.50 67.06  ? 1056 GLN D O     1 
ATOM   7412  O  O     B GLN B  1  257 ? -0.413  22.574  47.017 0.50 66.26  ? 1056 GLN D O     1 
ATOM   7413  C  CB    A GLN B  1  257 ? -0.781  24.745  45.065 0.50 65.52  ? 1056 GLN D CB    1 
ATOM   7414  C  CB    B GLN B  1  257 ? -0.509  24.499  44.910 0.50 67.82  ? 1056 GLN D CB    1 
ATOM   7415  C  CG    A GLN B  1  257 ? 0.736   24.764  45.262 0.50 69.46  ? 1056 GLN D CG    1 
ATOM   7416  C  CG    B GLN B  1  257 ? -0.201  25.059  43.526 0.50 69.52  ? 1056 GLN D CG    1 
ATOM   7417  C  CD    A GLN B  1  257 ? 1.342   26.155  45.165 0.50 70.03  ? 1056 GLN D CD    1 
ATOM   7418  C  CD    B GLN B  1  257 ? 0.428   24.020  42.617 0.50 72.78  ? 1056 GLN D CD    1 
ATOM   7419  O  OE1   A GLN B  1  257 ? 2.329   26.456  45.818 0.50 60.50  ? 1056 GLN D OE1   1 
ATOM   7420  O  OE1   B GLN B  1  257 ? 1.209   23.185  43.071 0.50 74.53  ? 1056 GLN D OE1   1 
ATOM   7421  N  NE2   A GLN B  1  257 ? 0.732   27.011  44.367 0.50 68.97  ? 1056 GLN D NE2   1 
ATOM   7422  N  NE2   B GLN B  1  257 ? 0.079   24.051  41.337 0.50 69.46  ? 1056 GLN D NE2   1 
ATOM   7423  N  N     . GLY B  1  258 ? -2.601  22.131  46.596 1.00 60.26  ? 1057 GLY D N     1 
ATOM   7424  C  CA    . GLY B  1  258 ? -2.898  21.532  47.905 1.00 67.11  ? 1057 GLY D CA    1 
ATOM   7425  C  C     . GLY B  1  258 ? -2.721  22.538  49.062 1.00 74.60  ? 1057 GLY D C     1 
ATOM   7426  O  O     . GLY B  1  258 ? -2.174  22.177  50.085 1.00 73.17  ? 1057 GLY D O     1 
ATOM   7427  N  N     A MET B  1  259 ? -3.144  23.798  48.846 0.50 72.28  ? 1058 MET D N     1 
ATOM   7428  N  N     B MET B  1  259 ? -3.059  23.826  48.875 0.50 74.71  ? 1058 MET D N     1 
ATOM   7429  C  CA    A MET B  1  259 ? -2.970  24.903  49.827 0.50 74.06  ? 1058 MET D CA    1 
ATOM   7430  C  CA    B MET B  1  259 ? -2.838  24.867  49.939 0.50 76.84  ? 1058 MET D CA    1 
ATOM   7431  C  C     A MET B  1  259 ? -4.180  25.017  50.738 0.50 71.66  ? 1058 MET D C     1 
ATOM   7432  C  C     B MET B  1  259 ? -4.082  25.032  50.801 0.50 73.28  ? 1058 MET D C     1 
ATOM   7433  O  O     A MET B  1  259 ? -4.870  26.052  50.794 0.50 54.40  ? 1058 MET D O     1 
ATOM   7434  O  O     B MET B  1  259 ? -4.748  26.079  50.805 0.50 56.72  ? 1058 MET D O     1 
ATOM   7435  C  CB    A MET B  1  259 ? -2.697  26.247  49.150 0.50 71.40  ? 1058 MET D CB    1 
ATOM   7436  C  CB    B MET B  1  259 ? -2.418  26.218  49.362 0.50 76.31  ? 1058 MET D CB    1 
ATOM   7437  C  CG    A MET B  1  259 ? -1.324  26.399  48.487 0.50 69.82  ? 1058 MET D CG    1 
ATOM   7438  C  CG    B MET B  1  259 ? -1.063  26.286  48.647 0.50 75.47  ? 1058 MET D CG    1 
ATOM   7439  S  SD    A MET B  1  259 ? 0.124   26.159  49.545 0.50 67.12  ? 1058 MET D SD    1 
ATOM   7440  S  SD    B MET B  1  259 ? -1.072  27.537  47.350 0.50 75.39  ? 1058 MET D SD    1 
ATOM   7441  C  CE    A MET B  1  259 ? 0.201   24.392  49.807 0.50 69.63  ? 1058 MET D CE    1 
ATOM   7442  C  CE    B MET B  1  259 ? 0.406   27.177  46.402 0.50 81.27  ? 1058 MET D CE    1 
ATOM   7443  N  N     . THR B  1  260 ? -4.392  23.941  51.466 1.00 71.77  ? 1059 THR D N     1 
ATOM   7444  C  CA    . THR B  1  260 ? -5.559  23.754  52.282 1.00 70.40  ? 1059 THR D CA    1 
ATOM   7445  C  C     . THR B  1  260 ? -5.334  24.368  53.669 1.00 71.01  ? 1059 THR D C     1 
ATOM   7446  O  O     . THR B  1  260 ? -4.157  24.702  54.002 1.00 72.82  ? 1059 THR D O     1 
ATOM   7447  C  CB    . THR B  1  260 ? -5.853  22.234  52.335 1.00 67.44  ? 1059 THR D CB    1 
ATOM   7448  O  OG1   . THR B  1  260 ? -4.658  21.500  52.705 1.00 71.24  ? 1059 THR D OG1   1 
ATOM   7449  C  CG2   . THR B  1  260 ? -6.342  21.742  50.956 1.00 61.12  ? 1059 THR D CG2   1 
ATOM   7450  N  N     . PRO B  1  261 ? -6.424  24.543  54.486 1.00 62.14  ? 1060 PRO D N     1 
ATOM   7451  C  CA    . PRO B  1  261 ? -6.163  25.183  55.796 1.00 59.20  ? 1060 PRO D CA    1 
ATOM   7452  C  C     . PRO B  1  261 ? -5.200  24.401  56.679 1.00 71.70  ? 1060 PRO D C     1 
ATOM   7453  O  O     . PRO B  1  261 ? -4.398  25.021  57.368 1.00 75.68  ? 1060 PRO D O     1 
ATOM   7454  C  CB    . PRO B  1  261 ? -7.531  25.209  56.482 1.00 54.40  ? 1060 PRO D CB    1 
ATOM   7455  C  CG    . PRO B  1  261 ? -8.523  25.043  55.375 1.00 53.65  ? 1060 PRO D CG    1 
ATOM   7456  C  CD    . PRO B  1  261 ? -7.849  24.183  54.349 1.00 53.34  ? 1060 PRO D CD    1 
ATOM   7457  N  N     . ASP B  1  262 ? -5.286  23.067  56.647 1.00 83.40  ? 1061 ASP D N     1 
ATOM   7458  C  CA    . ASP B  1  262 ? -4.418  22.178  57.448 1.00 74.95  ? 1061 ASP D CA    1 
ATOM   7459  C  C     . ASP B  1  262 ? -2.971  22.307  56.972 1.00 72.44  ? 1061 ASP D C     1 
ATOM   7460  O  O     . ASP B  1  262 ? -2.078  22.291  57.781 1.00 77.19  ? 1061 ASP D O     1 
ATOM   7461  C  CB    . ASP B  1  262 ? -4.865  20.738  57.266 1.00 73.80  ? 1061 ASP D CB    1 
ATOM   7462  C  CG    . ASP B  1  262 ? -4.733  20.276  55.806 1.00 81.49  ? 1061 ASP D CG    1 
ATOM   7463  O  OD1   . ASP B  1  262 ? -4.674  21.124  54.899 1.00 84.55  ? 1061 ASP D OD1   1 
ATOM   7464  O  OD2   . ASP B  1  262 ? -4.674  19.069  55.573 1.00 93.97  ? 1061 ASP D OD2   1 
ATOM   7465  N  N     . LYS B  1  263 ? -2.778  22.469  55.666 1.00 68.60  ? 1062 LYS D N     1 
ATOM   7466  C  CA    . LYS B  1  263 ? -1.458  22.600  55.089 1.00 64.43  ? 1062 LYS D CA    1 
ATOM   7467  C  C     . LYS B  1  263 ? -0.919  23.989  55.371 1.00 61.95  ? 1062 LYS D C     1 
ATOM   7468  O  O     . LYS B  1  263 ? -1.678  24.916  55.643 1.00 60.82  ? 1062 LYS D O     1 
ATOM   7469  C  CB    . LYS B  1  263 ? -1.486  22.337  53.585 1.00 65.15  ? 1062 LYS D CB    1 
ATOM   7470  C  CG    . LYS B  1  263 ? -1.144  20.924  53.142 1.00 60.77  ? 1062 LYS D CG    1 
ATOM   7471  C  CD    . LYS B  1  263 ? -1.625  19.850  54.110 1.00 59.76  ? 1062 LYS D CD    1 
ATOM   7472  N  N     . SER B  1  264 ? 0.396   24.130  55.333 1.00 61.34  ? 1063 SER D N     1 
ATOM   7473  C  CA    . SER B  1  264 ? 0.983   25.434  55.691 1.00 60.24  ? 1063 SER D CA    1 
ATOM   7474  C  C     . SER B  1  264 ? 0.769   26.469  54.596 1.00 61.53  ? 1063 SER D C     1 
ATOM   7475  O  O     . SER B  1  264 ? 0.448   26.146  53.462 1.00 63.88  ? 1063 SER D O     1 
ATOM   7476  C  CB    . SER B  1  264 ? 2.452   25.344  56.134 1.00 61.45  ? 1063 SER D CB    1 
ATOM   7477  O  OG    . SER B  1  264 ? 3.348   25.236  55.054 1.00 57.05  ? 1063 SER D OG    1 
ATOM   7478  N  N     . TYR B  1  265 ? 0.953   27.720  54.955 1.00 51.86  ? 1064 TYR D N     1 
ATOM   7479  C  CA    . TYR B  1  265 ? 0.840   28.794  54.005 1.00 50.15  ? 1064 TYR D CA    1 
ATOM   7480  C  C     . TYR B  1  265 ? 1.861   28.648  52.892 1.00 54.91  ? 1064 TYR D C     1 
ATOM   7481  O  O     . TYR B  1  265 ? 2.924   28.110  53.116 1.00 61.57  ? 1064 TYR D O     1 
ATOM   7482  C  CB    . TYR B  1  265 ? 1.039   30.124  54.713 1.00 45.82  ? 1064 TYR D CB    1 
ATOM   7483  C  CG    . TYR B  1  265 ? 0.051   30.420  55.801 1.00 46.29  ? 1064 TYR D CG    1 
ATOM   7484  C  CD1   . TYR B  1  265 ? 0.278   29.985  57.123 1.00 43.55  ? 1064 TYR D CD1   1 
ATOM   7485  C  CD2   . TYR B  1  265 ? -1.097  31.168  55.534 1.00 45.02  ? 1064 TYR D CD2   1 
ATOM   7486  C  CE1   . TYR B  1  265 ? -0.620  30.294  58.120 1.00 44.93  ? 1064 TYR D CE1   1 
ATOM   7487  C  CE2   . TYR B  1  265 ? -2.003  31.494  56.522 1.00 43.83  ? 1064 TYR D CE2   1 
ATOM   7488  C  CZ    . TYR B  1  265 ? -1.763  31.058  57.799 1.00 45.61  ? 1064 TYR D CZ    1 
ATOM   7489  O  OH    . TYR B  1  265 ? -2.649  31.384  58.760 1.00 47.39  ? 1064 TYR D OH    1 
ATOM   7490  N  N     . LYS B  1  266 ? 1.505   29.087  51.695 1.00 55.81  ? 1065 LYS D N     1 
ATOM   7491  C  CA    . LYS B  1  266 ? 2.397   29.099  50.547 1.00 48.06  ? 1065 LYS D CA    1 
ATOM   7492  C  C     . LYS B  1  266 ? 2.622   30.564  50.223 1.00 44.79  ? 1065 LYS D C     1 
ATOM   7493  O  O     . LYS B  1  266 ? 1.733   31.394  50.384 1.00 44.99  ? 1065 LYS D O     1 
ATOM   7494  C  CB    . LYS B  1  266 ? 1.729   28.413  49.412 1.00 44.21  ? 1065 LYS D CB    1 
ATOM   7495  N  N     A LYS B  1  267 ? 3.811   30.909  49.763 0.50 44.56  ? 1066 LYS D N     1 
ATOM   7496  N  N     B LYS B  1  267 ? 3.804   30.899  49.742 0.50 44.12  ? 1066 LYS D N     1 
ATOM   7497  C  CA    A LYS B  1  267 ? 4.126   32.282  49.540 0.50 43.95  ? 1066 LYS D CA    1 
ATOM   7498  C  CA    B LYS B  1  267 ? 4.148   32.268  49.531 0.50 43.28  ? 1066 LYS D CA    1 
ATOM   7499  C  C     A LYS B  1  267 ? 3.317   32.707  48.361 0.50 42.18  ? 1066 LYS D C     1 
ATOM   7500  C  C     B LYS B  1  267 ? 3.370   32.719  48.330 0.50 41.77  ? 1066 LYS D C     1 
ATOM   7501  O  O     A LYS B  1  267 ? 3.141   32.074  47.358 0.50 38.48  ? 1066 LYS D O     1 
ATOM   7502  O  O     B LYS B  1  267 ? 3.141   32.065  47.365 0.50 38.20  ? 1066 LYS D O     1 
ATOM   7503  C  CB    A LYS B  1  267 ? 5.589   32.497  49.240 0.50 45.44  ? 1066 LYS D CB    1 
ATOM   7504  C  CB    B LYS B  1  267 ? 5.635   32.441  49.352 0.50 44.33  ? 1066 LYS D CB    1 
ATOM   7505  C  CG    A LYS B  1  267 ? 5.837   33.857  48.619 0.50 45.93  ? 1066 LYS D CG    1 
ATOM   7506  C  CG    B LYS B  1  267 ? 6.358   31.156  49.010 0.50 44.09  ? 1066 LYS D CG    1 
ATOM   7507  C  CD    A LYS B  1  267 ? 7.101   34.451  49.186 0.50 47.02  ? 1066 LYS D CD    1 
ATOM   7508  C  CD    B LYS B  1  267 ? 6.493   30.250  50.221 0.50 42.98  ? 1066 LYS D CD    1 
ATOM   7509  C  CE    A LYS B  1  267 ? 8.306   34.087  48.346 0.50 40.80  ? 1066 LYS D CE    1 
ATOM   7510  C  CE    B LYS B  1  267 ? 7.376   30.869  51.291 0.50 40.89  ? 1066 LYS D CE    1 
ATOM   7511  N  NZ    A LYS B  1  267 ? 9.543   34.336  49.118 0.50 47.69  ? 1066 LYS D NZ    1 
ATOM   7512  N  NZ    B LYS B  1  267 ? 7.646   29.846  52.331 0.50 40.80  ? 1066 LYS D NZ    1 
ATOM   7513  N  N     . SER B  1  268 ? 2.951   33.912  48.435 1.00 37.08  ? 1067 SER D N     1 
ATOM   7514  C  CA    . SER B  1  268 ? 2.038   34.513  47.547 1.00 38.03  ? 1067 SER D CA    1 
ATOM   7515  C  C     . SER B  1  268 ? 2.579   34.722  46.160 1.00 36.76  ? 1067 SER D C     1 
ATOM   7516  O  O     . SER B  1  268 ? 1.847   34.662  45.220 1.00 33.65  ? 1067 SER D O     1 
ATOM   7517  C  CB    . SER B  1  268 ? 1.774   35.818  48.194 1.00 35.68  ? 1067 SER D CB    1 
ATOM   7518  O  OG    . SER B  1  268 ? 0.750   35.761  49.187 1.00 27.36  ? 1067 SER D OG    1 
ATOM   7519  N  N     . ALA B  1  269 ? 3.880   34.927  46.046 1.00 36.39  ? 1068 ALA D N     1 
ATOM   7520  C  CA    . ALA B  1  269 ? 4.435   35.152  44.772 1.00 38.17  ? 1068 ALA D CA    1 
ATOM   7521  C  C     . ALA B  1  269 ? 4.406   33.877  43.922 1.00 37.57  ? 1068 ALA D C     1 
ATOM   7522  O  O     . ALA B  1  269 ? 4.294   33.942  42.699 1.00 36.23  ? 1068 ALA D O     1 
ATOM   7523  C  CB    . ALA B  1  269 ? 5.840   35.687  44.895 1.00 40.18  ? 1068 ALA D CB    1 
ATOM   7524  N  N     . ARG B  1  270 ? 4.500   32.726  44.572 1.00 35.18  ? 1069 ARG D N     1 
ATOM   7525  C  CA    . ARG B  1  270 ? 4.415   31.452  43.890 1.00 36.35  ? 1069 ARG D CA    1 
ATOM   7526  C  C     . ARG B  1  270 ? 2.954   31.176  43.475 1.00 33.87  ? 1069 ARG D C     1 
ATOM   7527  O  O     . ARG B  1  270 ? 2.725   30.709  42.391 1.00 34.06  ? 1069 ARG D O     1 
ATOM   7528  C  CB    . ARG B  1  270 ? 5.005   30.359  44.810 1.00 39.82  ? 1069 ARG D CB    1 
ATOM   7529  C  CG    . ARG B  1  270 ? 4.950   28.930  44.279 1.00 47.80  ? 1069 ARG D CG    1 
ATOM   7530  C  CD    . ARG B  1  270 ? 6.047   28.133  44.929 1.00 53.01  ? 1069 ARG D CD    1 
ATOM   7531  N  NE    . ARG B  1  270 ? 6.069   26.751  44.467 1.00 62.13  ? 1069 ARG D NE    1 
ATOM   7532  C  CZ    . ARG B  1  270 ? 6.173   25.694  45.272 1.00 66.06  ? 1069 ARG D CZ    1 
ATOM   7533  N  NH1   . ARG B  1  270 ? 6.181   24.467  44.768 1.00 75.36  ? 1069 ARG D NH1   1 
ATOM   7534  N  NH2   . ARG B  1  270 ? 6.259   25.861  46.586 1.00 71.10  ? 1069 ARG D NH2   1 
ATOM   7535  N  N     . ILE B  1  271 ? 1.983   31.511  44.347 1.00 33.01  ? 1070 ILE D N     1 
ATOM   7536  C  CA    . ILE B  1  271 ? 0.587   31.342  44.031 1.00 32.95  ? 1070 ILE D CA    1 
ATOM   7537  C  C     . ILE B  1  271 ? 0.234   32.222  42.837 1.00 32.90  ? 1070 ILE D C     1 
ATOM   7538  O  O     . ILE B  1  271 ? -0.465  31.792  41.960 1.00 33.76  ? 1070 ILE D O     1 
ATOM   7539  C  CB    . ILE B  1  271 ? -0.287  31.829  45.153 1.00 37.62  ? 1070 ILE D CB    1 
ATOM   7540  C  CG1   . ILE B  1  271 ? -0.102  30.953  46.396 1.00 36.83  ? 1070 ILE D CG1   1 
ATOM   7541  C  CG2   . ILE B  1  271 ? -1.755  31.900  44.679 1.00 32.67  ? 1070 ILE D CG2   1 
ATOM   7542  C  CD1   . ILE B  1  271 ? -0.717  31.550  47.635 1.00 34.14  ? 1070 ILE D CD1   1 
ATOM   7543  N  N     . VAL B  1  272 ? 0.709   33.455  42.831 1.00 30.21  ? 1071 VAL D N     1 
ATOM   7544  C  CA    . VAL B  1  272 ? 0.371   34.388  41.787 1.00 31.57  ? 1071 VAL D CA    1 
ATOM   7545  C  C     . VAL B  1  272 ? 1.049   33.983  40.468 1.00 32.80  ? 1071 VAL D C     1 
ATOM   7546  O  O     . VAL B  1  272 ? 0.393   33.937  39.411 1.00 31.97  ? 1071 VAL D O     1 
ATOM   7547  C  CB    . VAL B  1  272 ? 0.747   35.841  42.207 1.00 35.13  ? 1071 VAL D CB    1 
ATOM   7548  C  CG1   . VAL B  1  272 ? 0.647   36.780  41.004 1.00 29.91  ? 1071 VAL D CG1   1 
ATOM   7549  C  CG2   . VAL B  1  272 ? -0.143  36.321  43.353 1.00 29.94  ? 1071 VAL D CG2   1 
ATOM   7550  N  N     . GLY B  1  273 ? 2.340   33.630  40.529 1.00 29.75  ? 1072 GLY D N     1 
ATOM   7551  C  CA    . GLY B  1  273 ? 3.066   33.178  39.328 1.00 26.08  ? 1072 GLY D CA    1 
ATOM   7552  C  C     . GLY B  1  273 ? 2.388   31.955  38.745 1.00 27.48  ? 1072 GLY D C     1 
ATOM   7553  O  O     . GLY B  1  273 ? 2.236   31.835  37.524 1.00 26.24  ? 1072 GLY D O     1 
ATOM   7554  N  N     . ASP B  1  274 ? 1.972   31.056  39.619 1.00 26.67  ? 1073 ASP D N     1 
ATOM   7555  C  CA    . ASP B  1  274 ? 1.202   29.867  39.210 1.00 33.73  ? 1073 ASP D CA    1 
ATOM   7556  C  C     . ASP B  1  274 ? -0.137  30.177  38.521 1.00 33.72  ? 1073 ASP D C     1 
ATOM   7557  O  O     . ASP B  1  274 ? -0.461  29.587  37.484 1.00 33.30  ? 1073 ASP D O     1 
ATOM   7558  C  CB    . ASP B  1  274 ? 0.869   28.996  40.394 1.00 39.66  ? 1073 ASP D CB    1 
ATOM   7559  C  CG    . ASP B  1  274 ? 1.493   27.674  40.326 1.00 57.74  ? 1073 ASP D CG    1 
ATOM   7560  O  OD1   . ASP B  1  274 ? 2.756   27.554  40.379 1.00 70.62  ? 1073 ASP D OD1   1 
ATOM   7561  O  OD2   . ASP B  1  274 ? 0.677   26.715  40.248 1.00 74.61  ? 1073 ASP D OD2   1 
ATOM   7562  N  N     . VAL B  1  275 ? -0.913  31.087  39.107 1.00 31.13  ? 1074 VAL D N     1 
ATOM   7563  C  CA    . VAL B  1  275 ? -2.211  31.445  38.526 1.00 32.26  ? 1074 VAL D CA    1 
ATOM   7564  C  C     . VAL B  1  275 ? -2.011  32.114  37.166 1.00 31.27  ? 1074 VAL D C     1 
ATOM   7565  O  O     . VAL B  1  275 ? -2.743  31.848  36.232 1.00 34.00  ? 1074 VAL D O     1 
ATOM   7566  C  CB    . VAL B  1  275 ? -2.982  32.378  39.476 1.00 31.78  ? 1074 VAL D CB    1 
ATOM   7567  C  CG1   . VAL B  1  275 ? -4.190  32.939  38.775 1.00 31.65  ? 1074 VAL D CG1   1 
ATOM   7568  C  CG2   . VAL B  1  275 ? -3.452  31.634  40.703 1.00 30.66  ? 1074 VAL D CG2   1 
ATOM   7569  N  N     . MET B  1  276 ? -0.999  32.989  37.079 1.00 32.65  ? 1075 MET D N     1 
ATOM   7570  C  CA    . MET B  1  276 ? -0.667  33.708  35.862 1.00 37.62  ? 1075 MET D CA    1 
ATOM   7571  C  C     . MET B  1  276 ? -0.307  32.760  34.708 1.00 38.59  ? 1075 MET D C     1 
ATOM   7572  O  O     . MET B  1  276 ? -0.817  32.889  33.609 1.00 40.08  ? 1075 MET D O     1 
ATOM   7573  C  CB    . MET B  1  276 ? 0.526   34.644  36.067 1.00 36.47  ? 1075 MET D CB    1 
ATOM   7574  C  CG    . MET B  1  276 ? 0.319   35.850  36.937 1.00 41.15  ? 1075 MET D CG    1 
ATOM   7575  S  SD    . MET B  1  276 ? 1.769   36.943  37.091 1.00 40.15  ? 1075 MET D SD    1 
ATOM   7576  C  CE    . MET B  1  276 ? 1.781   37.580  35.405 1.00 34.41  ? 1075 MET D CE    1 
ATOM   7577  N  N     . GLY B  1  277 ? 0.593   31.817  34.975 1.00 38.01  ? 1076 GLY D N     1 
ATOM   7578  C  CA    . GLY B  1  277 ? 1.039   30.882  33.958 1.00 36.46  ? 1076 GLY D CA    1 
ATOM   7579  C  C     . GLY B  1  277 ? -0.042  29.923  33.527 1.00 35.28  ? 1076 GLY D C     1 
ATOM   7580  O  O     . GLY B  1  277 ? -0.207  29.666  32.336 1.00 38.60  ? 1076 GLY D O     1 
ATOM   7581  N  N     . LYS B  1  278 ? -0.799  29.399  34.479 1.00 31.30  ? 1077 LYS D N     1 
ATOM   7582  C  CA    . LYS B  1  278 ? -1.795  28.374  34.140 1.00 34.74  ? 1077 LYS D CA    1 
ATOM   7583  C  C     . LYS B  1  278 ? -3.168  28.859  33.689 1.00 34.50  ? 1077 LYS D C     1 
ATOM   7584  O  O     . LYS B  1  278 ? -3.748  28.265  32.797 1.00 34.63  ? 1077 LYS D O     1 
ATOM   7585  C  CB    . LYS B  1  278 ? -1.951  27.408  35.305 1.00 36.24  ? 1077 LYS D CB    1 
ATOM   7586  C  CG    . LYS B  1  278 ? -0.740  26.510  35.565 1.00 39.29  ? 1077 LYS D CG    1 
ATOM   7587  C  CD    . LYS B  1  278 ? -1.078  25.563  36.688 1.00 50.48  ? 1077 LYS D CD    1 
ATOM   7588  C  CE    . LYS B  1  278 ? 0.108   24.823  37.273 1.00 63.98  ? 1077 LYS D CE    1 
ATOM   7589  N  NZ    . LYS B  1  278 ? -0.272  23.831  38.327 1.00 66.35  ? 1077 LYS D NZ    1 
ATOM   7590  N  N     . TYR B  1  279 ? -3.706  29.911  34.301 1.00 33.19  ? 1078 TYR D N     1 
ATOM   7591  C  CA    . TYR B  1  279 ? -5.083  30.293  34.009 1.00 32.59  ? 1078 TYR D CA    1 
ATOM   7592  C  C     . TYR B  1  279 ? -5.408  31.747  33.704 1.00 35.40  ? 1078 TYR D C     1 
ATOM   7593  O  O     . TYR B  1  279 ? -6.415  32.007  33.027 1.00 36.40  ? 1078 TYR D O     1 
ATOM   7594  C  CB    . TYR B  1  279 ? -5.961  29.917  35.200 1.00 39.11  ? 1078 TYR D CB    1 
ATOM   7595  C  CG    . TYR B  1  279 ? -5.559  28.635  35.925 1.00 37.70  ? 1078 TYR D CG    1 
ATOM   7596  C  CD1   . TYR B  1  279 ? -5.773  27.373  35.337 1.00 36.79  ? 1078 TYR D CD1   1 
ATOM   7597  C  CD2   . TYR B  1  279 ? -4.969  28.693  37.174 1.00 33.78  ? 1078 TYR D CD2   1 
ATOM   7598  C  CE1   . TYR B  1  279 ? -5.392  26.233  35.993 1.00 38.01  ? 1078 TYR D CE1   1 
ATOM   7599  C  CE2   . TYR B  1  279 ? -4.588  27.542  37.861 1.00 33.08  ? 1078 TYR D CE2   1 
ATOM   7600  C  CZ    . TYR B  1  279 ? -4.815  26.319  37.259 1.00 36.28  ? 1078 TYR D CZ    1 
ATOM   7601  O  OH    . TYR B  1  279 ? -4.460  25.153  37.874 1.00 36.78  ? 1078 TYR D OH    1 
ATOM   7602  N  N     . HIS B  1  280 ? -4.608  32.688  34.198 1.00 31.78  ? 1079 HIS D N     1 
ATOM   7603  C  CA    . HIS B  1  280 ? -5.068  34.064  34.151 1.00 32.58  ? 1079 HIS D CA    1 
ATOM   7604  C  C     . HIS B  1  280 ? -4.070  34.918  33.435 1.00 33.89  ? 1079 HIS D C     1 
ATOM   7605  O  O     . HIS B  1  280 ? -3.083  35.412  34.059 1.00 32.22  ? 1079 HIS D O     1 
ATOM   7606  C  CB    . HIS B  1  280 ? -5.348  34.578  35.561 1.00 30.54  ? 1079 HIS D CB    1 
ATOM   7607  C  CG    . HIS B  1  280 ? -6.186  35.820  35.591 1.00 30.60  ? 1079 HIS D CG    1 
ATOM   7608  N  ND1   . HIS B  1  280 ? -7.530  35.808  35.256 1.00 30.51  ? 1079 HIS D ND1   1 
ATOM   7609  C  CD2   . HIS B  1  280 ? -5.885  37.106  35.896 1.00 28.18  ? 1079 HIS D CD2   1 
ATOM   7610  C  CE1   . HIS B  1  280 ? -8.030  37.026  35.393 1.00 29.30  ? 1079 HIS D CE1   1 
ATOM   7611  N  NE2   . HIS B  1  280 ? -7.061  37.833  35.793 1.00 31.22  ? 1079 HIS D NE2   1 
ATOM   7612  N  N     . PRO B  1  281 ? -4.290  35.086  32.102 1.00 34.61  ? 1080 PRO D N     1 
ATOM   7613  C  CA    . PRO B  1  281 ? -3.187  35.792  31.402 1.00 34.55  ? 1080 PRO D CA    1 
ATOM   7614  C  C     . PRO B  1  281 ? -3.247  37.307  31.568 1.00 36.23  ? 1080 PRO D C     1 
ATOM   7615  O  O     . PRO B  1  281 ? -3.395  38.034  30.606 1.00 35.96  ? 1080 PRO D O     1 
ATOM   7616  C  CB    . PRO B  1  281 ? -3.412  35.398  29.938 1.00 35.76  ? 1080 PRO D CB    1 
ATOM   7617  C  CG    . PRO B  1  281 ? -4.890  35.251  29.855 1.00 33.20  ? 1080 PRO D CG    1 
ATOM   7618  C  CD    . PRO B  1  281 ? -5.304  34.611  31.130 1.00 32.15  ? 1080 PRO D CD    1 
ATOM   7619  N  N     . HIS B  1  282 ? -3.147  37.773  32.806 1.00 31.07  ? 1081 HIS D N     1 
ATOM   7620  C  CA    . HIS B  1  282 ? -3.146  39.201  33.035 1.00 32.83  ? 1081 HIS D CA    1 
ATOM   7621  C  C     . HIS B  1  282 ? -2.065  39.588  33.992 1.00 31.99  ? 1081 HIS D C     1 
ATOM   7622  O  O     . HIS B  1  282 ? -1.274  38.733  34.380 1.00 30.90  ? 1081 HIS D O     1 
ATOM   7623  C  CB    . HIS B  1  282 ? -4.553  39.695  33.430 1.00 34.29  ? 1081 HIS D CB    1 
ATOM   7624  C  CG    . HIS B  1  282 ? -5.596  39.333  32.408 1.00 33.96  ? 1081 HIS D CG    1 
ATOM   7625  N  ND1   . HIS B  1  282 ? -5.703  39.983  31.203 1.00 28.11  ? 1081 HIS D ND1   1 
ATOM   7626  C  CD2   . HIS B  1  282 ? -6.532  38.351  32.390 1.00 32.99  ? 1081 HIS D CD2   1 
ATOM   7627  C  CE1   . HIS B  1  282 ? -6.681  39.439  30.496 1.00 32.50  ? 1081 HIS D CE1   1 
ATOM   7628  N  NE2   . HIS B  1  282 ? -7.192  38.441  31.189 1.00 34.78  ? 1081 HIS D NE2   1 
ATOM   7629  N  N     . GLY B  1  283 ? -1.979  40.880  34.313 1.00 35.06  ? 1082 GLY D N     1 
ATOM   7630  C  CA    . GLY B  1  283 ? -0.900  41.402  35.152 1.00 34.30  ? 1082 GLY D CA    1 
ATOM   7631  C  C     . GLY B  1  283 ? -0.939  40.853  36.573 1.00 39.50  ? 1082 GLY D C     1 
ATOM   7632  O  O     . GLY B  1  283 ? -2.023  40.516  37.095 1.00 39.34  ? 1082 GLY D O     1 
ATOM   7633  N  N     . ASP B  1  284 ? 0.244   40.711  37.175 1.00 33.94  ? 1083 ASP D N     1 
ATOM   7634  C  CA    . ASP B  1  284 ? 0.376   40.143  38.503 1.00 33.32  ? 1083 ASP D CA    1 
ATOM   7635  C  C     . ASP B  1  284 ? -0.379  40.919  39.583 1.00 35.62  ? 1083 ASP D C     1 
ATOM   7636  O  O     . ASP B  1  284 ? -0.934  40.314  40.513 1.00 33.24  ? 1083 ASP D O     1 
ATOM   7637  C  CB    . ASP B  1  284 ? 1.850   40.064  38.913 1.00 35.16  ? 1083 ASP D CB    1 
ATOM   7638  C  CG    . ASP B  1  284 ? 2.535   41.442  38.922 1.00 38.06  ? 1083 ASP D CG    1 
ATOM   7639  O  OD1   . ASP B  1  284 ? 2.710   42.029  37.839 1.00 38.83  ? 1083 ASP D OD1   1 
ATOM   7640  O  OD2   . ASP B  1  284 ? 2.892   41.951  39.993 1.00 38.41  ? 1083 ASP D OD2   1 
ATOM   7641  N  N     . SER B  1  285 ? -0.367  42.245  39.487 1.00 31.13  ? 1084 SER D N     1 
ATOM   7642  C  CA    . SER B  1  285 ? -1.065  43.044  40.482 1.00 34.88  ? 1084 SER D CA    1 
ATOM   7643  C  C     . SER B  1  285 ? -2.582  42.831  40.498 1.00 33.68  ? 1084 SER D C     1 
ATOM   7644  O  O     . SER B  1  285 ? -3.183  42.843  41.567 1.00 34.21  ? 1084 SER D O     1 
ATOM   7645  C  CB    . SER B  1  285 ? -0.697  44.542  40.402 1.00 38.58  ? 1084 SER D CB    1 
ATOM   7646  O  OG    . SER B  1  285 ? -1.356  45.146  39.321 1.00 41.09  ? 1084 SER D OG    1 
ATOM   7647  N  N     . SER B  1  286 ? -3.183  42.562  39.350 1.00 32.86  ? 1085 SER D N     1 
ATOM   7648  C  CA    . SER B  1  286 ? -4.645  42.291  39.330 1.00 35.57  ? 1085 SER D CA    1 
ATOM   7649  C  C     . SER B  1  286 ? -4.951  41.049  40.122 1.00 33.53  ? 1085 SER D C     1 
ATOM   7650  O  O     . SER B  1  286 ? -5.922  41.028  40.878 1.00 34.40  ? 1085 SER D O     1 
ATOM   7651  C  CB    . SER B  1  286 ? -5.177  42.159  37.891 1.00 34.82  ? 1085 SER D CB    1 
ATOM   7652  O  OG    . SER B  1  286 ? -5.301  43.456  37.295 1.00 30.40  ? 1085 SER D OG    1 
ATOM   7653  N  N     . ILE B  1  287 ? -4.080  40.041  39.972 1.00 32.69  ? 1086 ILE D N     1 
ATOM   7654  C  CA    . ILE B  1  287 ? -4.289  38.767  40.636 1.00 30.85  ? 1086 ILE D CA    1 
ATOM   7655  C  C     . ILE B  1  287 ? -4.032  38.943  42.144 1.00 31.09  ? 1086 ILE D C     1 
ATOM   7656  O  O     . ILE B  1  287 ? -4.907  38.650  42.981 1.00 35.85  ? 1086 ILE D O     1 
ATOM   7657  C  CB    . ILE B  1  287 ? -3.382  37.642  40.005 1.00 32.06  ? 1086 ILE D CB    1 
ATOM   7658  C  CG1   . ILE B  1  287 ? -3.737  37.393  38.508 1.00 30.12  ? 1086 ILE D CG1   1 
ATOM   7659  C  CG2   . ILE B  1  287 ? -3.453  36.364  40.839 1.00 29.72  ? 1086 ILE D CG2   1 
ATOM   7660  C  CD1   . ILE B  1  287 ? -2.656  36.681  37.666 1.00 30.93  ? 1086 ILE D CD1   1 
ATOM   7661  N  N     . TYR B  1  288 ? -2.886  39.531  42.472 1.00 29.13  ? 1087 TYR D N     1 
ATOM   7662  C  CA    . TYR B  1  288 ? -2.497  39.616  43.882 1.00 29.78  ? 1087 TYR D CA    1 
ATOM   7663  C  C     . TYR B  1  288 ? -3.478  40.496  44.642 1.00 28.80  ? 1087 TYR D C     1 
ATOM   7664  O  O     . TYR B  1  288 ? -3.915  40.160  45.728 1.00 30.74  ? 1087 TYR D O     1 
ATOM   7665  C  CB    . TYR B  1  288 ? -1.109  40.221  44.042 1.00 25.73  ? 1087 TYR D CB    1 
ATOM   7666  C  CG    . TYR B  1  288 ? -0.669  40.311  45.485 1.00 27.17  ? 1087 TYR D CG    1 
ATOM   7667  C  CD1   . TYR B  1  288 ? -0.678  39.181  46.317 1.00 24.70  ? 1087 TYR D CD1   1 
ATOM   7668  C  CD2   . TYR B  1  288 ? -0.210  41.515  46.025 1.00 25.25  ? 1087 TYR D CD2   1 
ATOM   7669  C  CE1   . TYR B  1  288 ? -0.273  39.263  47.637 1.00 26.10  ? 1087 TYR D CE1   1 
ATOM   7670  C  CE2   . TYR B  1  288 ? 0.217   41.584  47.333 1.00 25.05  ? 1087 TYR D CE2   1 
ATOM   7671  C  CZ    . TYR B  1  288 ? 0.221   40.462  48.141 1.00 27.77  ? 1087 TYR D CZ    1 
ATOM   7672  O  OH    . TYR B  1  288 ? 0.646   40.522  49.482 1.00 26.37  ? 1087 TYR D OH    1 
ATOM   7673  N  N     . GLU B  1  289 ? -3.856  41.608  44.045 1.00 27.38  ? 1088 GLU D N     1 
ATOM   7674  C  CA    . GLU B  1  289 ? -4.834  42.461  44.714 1.00 31.73  ? 1088 GLU D CA    1 
ATOM   7675  C  C     . GLU B  1  289 ? -6.199  41.818  44.884 1.00 28.81  ? 1088 GLU D C     1 
ATOM   7676  O  O     . GLU B  1  289 ? -6.825  42.022  45.906 1.00 30.62  ? 1088 GLU D O     1 
ATOM   7677  C  CB    . GLU B  1  289 ? -4.906  43.833  44.034 1.00 33.71  ? 1088 GLU D CB    1 
ATOM   7678  C  CG    . GLU B  1  289 ? -3.590  44.570  44.317 1.00 37.06  ? 1088 GLU D CG    1 
ATOM   7679  C  CD    . GLU B  1  289 ? -3.511  45.875  43.616 1.00 45.23  ? 1088 GLU D CD    1 
ATOM   7680  O  OE1   . GLU B  1  289 ? -2.395  46.424  43.604 1.00 59.74  ? 1088 GLU D OE1   1 
ATOM   7681  O  OE2   . GLU B  1  289 ? -4.557  46.357  43.117 1.00 53.39  ? 1088 GLU D OE2   1 
ATOM   7682  N  N     . ALA B  1  290 ? -6.622  41.008  43.931 1.00 28.59  ? 1089 ALA D N     1 
ATOM   7683  C  CA    . ALA B  1  290 ? -7.908  40.257  44.087 1.00 29.97  ? 1089 ALA D CA    1 
ATOM   7684  C  C     . ALA B  1  290 ? -7.762  39.271  45.261 1.00 31.90  ? 1089 ALA D C     1 
ATOM   7685  O  O     . ALA B  1  290 ? -8.663  39.143  46.079 1.00 29.60  ? 1089 ALA D O     1 
ATOM   7686  C  CB    . ALA B  1  290 ? -8.225  39.529  42.798 1.00 28.84  ? 1089 ALA D CB    1 
ATOM   7687  N  N     . MET B  1  291 ? -6.595  38.597  45.349 1.00 29.80  ? 1090 MET D N     1 
ATOM   7688  C  CA    . MET B  1  291 ? -6.393  37.623  46.396 1.00 28.11  ? 1090 MET D CA    1 
ATOM   7689  C  C     . MET B  1  291 ? -6.385  38.275  47.774 1.00 27.29  ? 1090 MET D C     1 
ATOM   7690  O  O     . MET B  1  291 ? -6.906  37.722  48.779 1.00 28.64  ? 1090 MET D O     1 
ATOM   7691  C  CB    . MET B  1  291 ? -5.086  36.815  46.164 1.00 28.26  ? 1090 MET D CB    1 
ATOM   7692  C  CG    . MET B  1  291 ? -4.900  35.738  47.264 1.00 29.88  ? 1090 MET D CG    1 
ATOM   7693  S  SD    . MET B  1  291 ? -3.382  34.735  47.047 1.00 32.87  ? 1090 MET D SD    1 
ATOM   7694  C  CE    . MET B  1  291 ? -2.169  35.793  47.837 1.00 29.06  ? 1090 MET D CE    1 
ATOM   7695  N  N     . VAL B  1  292 ? -5.743  39.443  47.842 1.00 28.72  ? 1091 VAL D N     1 
ATOM   7696  C  CA    . VAL B  1  292 ? -5.629  40.174  49.068 1.00 26.64  ? 1091 VAL D CA    1 
ATOM   7697  C  C     . VAL B  1  292 ? -7.003  40.553  49.603 1.00 27.32  ? 1091 VAL D C     1 
ATOM   7698  O  O     . VAL B  1  292 ? -7.259  40.417  50.779 1.00 27.86  ? 1091 VAL D O     1 
ATOM   7699  C  CB    . VAL B  1  292 ? -4.779  41.456  48.893 1.00 25.66  ? 1091 VAL D CB    1 
ATOM   7700  C  CG1   . VAL B  1  292 ? -5.010  42.373  50.085 1.00 24.68  ? 1091 VAL D CG1   1 
ATOM   7701  C  CG2   . VAL B  1  292 ? -3.312  41.120  48.813 1.00 24.30  ? 1091 VAL D CG2   1 
ATOM   7702  N  N     . ARG B  1  293 ? -7.881  41.047  48.756 1.00 25.57  ? 1092 ARG D N     1 
ATOM   7703  C  CA    . ARG B  1  293 ? -9.194  41.496  49.257 1.00 30.58  ? 1092 ARG D CA    1 
ATOM   7704  C  C     . ARG B  1  293 ? -9.961  40.312  49.838 1.00 32.25  ? 1092 ARG D C     1 
ATOM   7705  O  O     . ARG B  1  293 ? -10.636 40.478  50.871 1.00 30.88  ? 1092 ARG D O     1 
ATOM   7706  C  CB    . ARG B  1  293 ? -10.001 42.138  48.164 1.00 29.18  ? 1092 ARG D CB    1 
ATOM   7707  C  CG    . ARG B  1  293 ? -9.504  43.515  47.816 1.00 31.54  ? 1092 ARG D CG    1 
ATOM   7708  C  CD    . ARG B  1  293 ? -10.350 44.151  46.711 1.00 38.93  ? 1092 ARG D CD    1 
ATOM   7709  N  NE    . ARG B  1  293 ? -9.894  43.700  45.388 1.00 48.11  ? 1092 ARG D NE    1 
ATOM   7710  C  CZ    . ARG B  1  293 ? -9.047  44.332  44.547 1.00 50.62  ? 1092 ARG D CZ    1 
ATOM   7711  N  NH1   . ARG B  1  293 ? -8.523  45.543  44.823 1.00 45.84  ? 1092 ARG D NH1   1 
ATOM   7712  N  NH2   . ARG B  1  293 ? -8.761  43.730  43.385 1.00 38.23  ? 1092 ARG D NH2   1 
ATOM   7713  N  N     . MET B  1  294 ? -9.779  39.127  49.226 1.00 29.33  ? 1093 MET D N     1 
ATOM   7714  C  CA    . MET B  1  294 ? -10.444 37.892  49.674 1.00 32.49  ? 1093 MET D CA    1 
ATOM   7715  C  C     . MET B  1  294 ? -9.963  37.493  51.056 1.00 30.28  ? 1093 MET D C     1 
ATOM   7716  O  O     . MET B  1  294 ? -10.615 36.704  51.729 1.00 30.18  ? 1093 MET D O     1 
ATOM   7717  C  CB    . MET B  1  294 ? -10.226 36.741  48.688 1.00 33.54  ? 1093 MET D CB    1 
ATOM   7718  C  CG    . MET B  1  294 ? -11.047 36.847  47.383 1.00 40.48  ? 1093 MET D CG    1 
ATOM   7719  S  SD    . MET B  1  294 ? -10.963 35.365  46.313 1.00 43.40  ? 1093 MET D SD    1 
ATOM   7720  C  CE    . MET B  1  294 ? -9.290  35.529  45.736 1.00 36.89  ? 1093 MET D CE    1 
ATOM   7721  N  N     . ALA B  1  295 ? -8.853  38.080  51.505 1.00 28.35  ? 1094 ALA D N     1 
ATOM   7722  C  CA    . ALA B  1  295 ? -8.322  37.764  52.823 1.00 28.12  ? 1094 ALA D CA    1 
ATOM   7723  C  C     . ALA B  1  295 ? -8.675  38.791  53.883 1.00 29.99  ? 1094 ALA D C     1 
ATOM   7724  O  O     . ALA B  1  295 ? -8.403  38.567  55.030 1.00 31.41  ? 1094 ALA D O     1 
ATOM   7725  C  CB    . ALA B  1  295 ? -6.830  37.610  52.734 1.00 27.71  ? 1094 ALA D CB    1 
ATOM   7726  N  N     . GLN B  1  296 ? -9.292  39.910  53.493 1.00 27.95  ? 1095 GLN D N     1 
ATOM   7727  C  CA    . GLN B  1  296 ? -9.616  40.984  54.431 1.00 26.45  ? 1095 GLN D CA    1 
ATOM   7728  C  C     . GLN B  1  296 ? -10.935 40.780  55.128 1.00 26.88  ? 1095 GLN D C     1 
ATOM   7729  O  O     . GLN B  1  296 ? -11.962 40.703  54.480 1.00 23.62  ? 1095 GLN D O     1 
ATOM   7730  C  CB    . GLN B  1  296 ? -9.650  42.316  53.700 1.00 25.75  ? 1095 GLN D CB    1 
ATOM   7731  C  CG    . GLN B  1  296 ? -8.303  42.744  53.197 1.00 25.55  ? 1095 GLN D CG    1 
ATOM   7732  C  CD    . GLN B  1  296 ? -8.369  43.885  52.202 1.00 28.50  ? 1095 GLN D CD    1 
ATOM   7733  O  OE1   . GLN B  1  296 ? -9.384  44.132  51.554 1.00 32.40  ? 1095 GLN D OE1   1 
ATOM   7734  N  NE2   . GLN B  1  296 ? -7.276  44.634  52.123 1.00 23.70  ? 1095 GLN D NE2   1 
ATOM   7735  N  N     . ASP B  1  297 ? -10.920 40.691  56.449 1.00 28.14  ? 1096 ASP D N     1 
ATOM   7736  C  CA    . ASP B  1  297 ? -12.170 40.485  57.179 1.00 29.29  ? 1096 ASP D CA    1 
ATOM   7737  C  C     . ASP B  1  297 ? -13.038 41.743  57.239 1.00 30.39  ? 1096 ASP D C     1 
ATOM   7738  O  O     . ASP B  1  297 ? -14.187 41.682  57.656 1.00 30.33  ? 1096 ASP D O     1 
ATOM   7739  C  CB    . ASP B  1  297 ? -11.932 39.868  58.557 1.00 31.43  ? 1096 ASP D CB    1 
ATOM   7740  C  CG    . ASP B  1  297 ? -11.157 40.784  59.495 1.00 37.52  ? 1096 ASP D CG    1 
ATOM   7741  O  OD1   . ASP B  1  297 ? -10.940 41.993  59.195 1.00 38.22  ? 1096 ASP D OD1   1 
ATOM   7742  O  OD2   . ASP B  1  297 ? -10.739 40.297  60.554 1.00 40.22  ? 1096 ASP D OD2   1 
ATOM   7743  N  N     . PHE B  1  298 ? -12.517 42.863  56.754 1.00 26.54  ? 1097 PHE D N     1 
ATOM   7744  C  CA    . PHE B  1  298 ? -13.350 44.056  56.634 1.00 27.91  ? 1097 PHE D CA    1 
ATOM   7745  C  C     . PHE B  1  298 ? -13.914 44.162  55.216 1.00 28.60  ? 1097 PHE D C     1 
ATOM   7746  O  O     . PHE B  1  298 ? -14.739 45.021  54.948 1.00 30.58  ? 1097 PHE D O     1 
ATOM   7747  C  CB    . PHE B  1  298 ? -12.595 45.338  57.008 1.00 27.83  ? 1097 PHE D CB    1 
ATOM   7748  C  CG    . PHE B  1  298 ? -11.300 45.511  56.298 1.00 27.68  ? 1097 PHE D CG    1 
ATOM   7749  C  CD1   . PHE B  1  298 ? -11.287 46.031  55.017 1.00 24.30  ? 1097 PHE D CD1   1 
ATOM   7750  C  CD2   . PHE B  1  298 ? -10.072 45.155  56.922 1.00 28.53  ? 1097 PHE D CD2   1 
ATOM   7751  C  CE1   . PHE B  1  298 ? -10.061 46.201  54.327 1.00 27.28  ? 1097 PHE D CE1   1 
ATOM   7752  C  CE2   . PHE B  1  298 ? -8.854  45.345  56.226 1.00 29.63  ? 1097 PHE D CE2   1 
ATOM   7753  C  CZ    . PHE B  1  298 ? -8.858  45.864  54.914 1.00 24.01  ? 1097 PHE D CZ    1 
ATOM   7754  N  N     . SER B  1  299 ? -13.508 43.272  54.307 1.00 28.51  ? 1098 SER D N     1 
ATOM   7755  C  CA    . SER B  1  299 ? -14.044 43.272  52.945 1.00 27.27  ? 1098 SER D CA    1 
ATOM   7756  C  C     . SER B  1  299 ? -14.955 42.091  52.683 1.00 27.80  ? 1098 SER D C     1 
ATOM   7757  O  O     . SER B  1  299 ? -15.988 42.238  51.992 1.00 28.31  ? 1098 SER D O     1 
ATOM   7758  C  CB    . SER B  1  299 ? -12.950 43.283  51.887 1.00 28.60  ? 1098 SER D CB    1 
ATOM   7759  O  OG    . SER B  1  299 ? -12.118 44.414  52.080 1.00 33.49  ? 1098 SER D OG    1 
ATOM   7760  N  N     . TYR B  1  300 ? -14.570 40.916  53.160 1.00 25.16  ? 1099 TYR D N     1 
ATOM   7761  C  CA    . TYR B  1  300 ? -15.354 39.729  52.882 1.00 24.24  ? 1099 TYR D CA    1 
ATOM   7762  C  C     . TYR B  1  300 ? -16.074 39.332  54.160 1.00 26.29  ? 1099 TYR D C     1 
ATOM   7763  O  O     . TYR B  1  300 ? -15.449 39.072  55.197 1.00 25.87  ? 1099 TYR D O     1 
ATOM   7764  C  CB    . TYR B  1  300 ? -14.435 38.584  52.417 1.00 25.83  ? 1099 TYR D CB    1 
ATOM   7765  C  CG    . TYR B  1  300 ? -14.246 38.585  50.951 1.00 27.51  ? 1099 TYR D CG    1 
ATOM   7766  C  CD1   . TYR B  1  300 ? -13.607 39.662  50.311 1.00 27.08  ? 1099 TYR D CD1   1 
ATOM   7767  C  CD2   . TYR B  1  300 ? -14.811 37.577  50.172 1.00 25.35  ? 1099 TYR D CD2   1 
ATOM   7768  C  CE1   . TYR B  1  300 ? -13.477 39.701  48.939 1.00 27.40  ? 1099 TYR D CE1   1 
ATOM   7769  C  CE2   . TYR B  1  300 ? -14.713 37.614  48.784 1.00 27.35  ? 1099 TYR D CE2   1 
ATOM   7770  C  CZ    . TYR B  1  300 ? -14.010 38.675  48.185 1.00 32.49  ? 1099 TYR D CZ    1 
ATOM   7771  O  OH    . TYR B  1  300 ? -13.853 38.759  46.803 1.00 33.59  ? 1099 TYR D OH    1 
ATOM   7772  N  N     . ARG B  1  301 ? -17.409 39.303  54.074 1.00 24.12  ? 1100 ARG D N     1 
ATOM   7773  C  CA    . ARG B  1  301 ? -18.229 38.819  55.144 1.00 23.86  ? 1100 ARG D CA    1 
ATOM   7774  C  C     . ARG B  1  301 ? -17.809 37.391  55.561 1.00 24.81  ? 1100 ARG D C     1 
ATOM   7775  O  O     . ARG B  1  301 ? -17.846 37.077  56.759 1.00 27.15  ? 1100 ARG D O     1 
ATOM   7776  C  CB    . ARG B  1  301 ? -19.704 38.800  54.697 1.00 24.10  ? 1100 ARG D CB    1 
ATOM   7777  C  CG    . ARG B  1  301 ? -20.705 38.465  55.767 1.00 26.03  ? 1100 ARG D CG    1 
ATOM   7778  C  CD    . ARG B  1  301 ? -20.505 39.397  56.973 1.00 26.90  ? 1100 ARG D CD    1 
ATOM   7779  N  NE    . ARG B  1  301 ? -21.439 39.073  58.033 1.00 29.94  ? 1100 ARG D NE    1 
ATOM   7780  C  CZ    . ARG B  1  301 ? -21.264 38.114  58.908 1.00 30.46  ? 1100 ARG D CZ    1 
ATOM   7781  N  NH1   . ARG B  1  301 ? -20.179 37.372  58.832 1.00 30.91  ? 1100 ARG D NH1   1 
ATOM   7782  N  NH2   . ARG B  1  301 ? -22.188 37.885  59.854 1.00 31.65  ? 1100 ARG D NH2   1 
ATOM   7783  N  N     . TYR B  1  302 ? -17.435 36.560  54.605 1.00 23.08  ? 1101 TYR D N     1 
ATOM   7784  C  CA    . TYR B  1  302 ? -16.858 35.202  54.892 1.00 24.38  ? 1101 TYR D CA    1 
ATOM   7785  C  C     . TYR B  1  302 ? -15.574 35.071  54.066 1.00 24.01  ? 1101 TYR D C     1 
ATOM   7786  O  O     . TYR B  1  302 ? -15.614 34.733  52.904 1.00 26.47  ? 1101 TYR D O     1 
ATOM   7787  C  CB    . TYR B  1  302 ? -17.877 34.075  54.540 1.00 24.58  ? 1101 TYR D CB    1 
ATOM   7788  C  CG    . TYR B  1  302 ? -19.115 34.260  55.351 1.00 25.10  ? 1101 TYR D CG    1 
ATOM   7789  C  CD1   . TYR B  1  302 ? -19.178 33.789  56.707 1.00 24.01  ? 1101 TYR D CD1   1 
ATOM   7790  C  CD2   . TYR B  1  302 ? -20.210 35.059  54.850 1.00 25.55  ? 1101 TYR D CD2   1 
ATOM   7791  C  CE1   . TYR B  1  302 ? -20.327 34.032  57.482 1.00 24.07  ? 1101 TYR D CE1   1 
ATOM   7792  C  CE2   . TYR B  1  302 ? -21.344 35.274  55.620 1.00 22.99  ? 1101 TYR D CE2   1 
ATOM   7793  C  CZ    . TYR B  1  302 ? -21.399 34.805  56.929 1.00 24.21  ? 1101 TYR D CZ    1 
ATOM   7794  O  OH    . TYR B  1  302 ? -22.539 35.065  57.677 1.00 24.40  ? 1101 TYR D OH    1 
ATOM   7795  N  N     . PRO B  1  303 ? -14.434 35.471  54.630 1.00 25.09  ? 1102 PRO D N     1 
ATOM   7796  C  CA    . PRO B  1  303 ? -13.160 35.498  53.886 1.00 25.91  ? 1102 PRO D CA    1 
ATOM   7797  C  C     . PRO B  1  303 ? -12.816 34.143  53.241 1.00 29.88  ? 1102 PRO D C     1 
ATOM   7798  O  O     . PRO B  1  303 ? -13.092 33.065  53.834 1.00 23.55  ? 1102 PRO D O     1 
ATOM   7799  C  CB    . PRO B  1  303 ? -12.139 35.842  54.984 1.00 26.83  ? 1102 PRO D CB    1 
ATOM   7800  C  CG    . PRO B  1  303 ? -12.923 36.685  55.910 1.00 24.53  ? 1102 PRO D CG    1 
ATOM   7801  C  CD    . PRO B  1  303 ? -14.253 35.958  56.011 1.00 25.46  ? 1102 PRO D CD    1 
ATOM   7802  N  N     . LEU B  1  304 ? -12.300 34.229  52.026 1.00 28.62  ? 1103 LEU D N     1 
ATOM   7803  C  CA    . LEU B  1  304 ? -12.049 33.068  51.201 1.00 27.95  ? 1103 LEU D CA    1 
ATOM   7804  C  C     . LEU B  1  304 ? -10.569 32.715  51.248 1.00 31.85  ? 1103 LEU D C     1 
ATOM   7805  O  O     . LEU B  1  304 ? -10.179 31.610  50.915 1.00 27.27  ? 1103 LEU D O     1 
ATOM   7806  C  CB    . LEU B  1  304 ? -12.503 33.367  49.777 1.00 26.37  ? 1103 LEU D CB    1 
ATOM   7807  C  CG    . LEU B  1  304 ? -14.033 33.615  49.648 1.00 26.39  ? 1103 LEU D CG    1 
ATOM   7808  C  CD1   . LEU B  1  304 ? -14.458 33.777  48.219 1.00 21.51  ? 1103 LEU D CD1   1 
ATOM   7809  C  CD2   . LEU B  1  304 ? -14.866 32.533  50.357 1.00 25.55  ? 1103 LEU D CD2   1 
ATOM   7810  N  N     . VAL B  1  305 ? -9.746  33.697  51.628 1.00 29.28  ? 1104 VAL D N     1 
ATOM   7811  C  CA    . VAL B  1  305 ? -8.332  33.466  51.735 1.00 31.05  ? 1104 VAL D CA    1 
ATOM   7812  C  C     . VAL B  1  305 ? -7.893  33.738  53.154 1.00 35.66  ? 1104 VAL D C     1 
ATOM   7813  O  O     . VAL B  1  305 ? -8.386  34.679  53.819 1.00 33.30  ? 1104 VAL D O     1 
ATOM   7814  C  CB    . VAL B  1  305 ? -7.543  34.304  50.720 1.00 31.25  ? 1104 VAL D CB    1 
ATOM   7815  C  CG1   . VAL B  1  305 ? -6.035  34.213  50.956 1.00 29.25  ? 1104 VAL D CG1   1 
ATOM   7816  C  CG2   . VAL B  1  305 ? -7.885  33.870  49.305 1.00 26.93  ? 1104 VAL D CG2   1 
ATOM   7817  N  N     . ASP B  1  306 ? -6.995  32.890  53.633 1.00 31.72  ? 1105 ASP D N     1 
ATOM   7818  C  CA    . ASP B  1  306 ? -6.399  33.041  54.934 1.00 31.22  ? 1105 ASP D CA    1 
ATOM   7819  C  C     . ASP B  1  306 ? -4.982  33.577  54.703 1.00 30.71  ? 1105 ASP D C     1 
ATOM   7820  O  O     . ASP B  1  306 ? -4.076  32.870  54.168 1.00 29.06  ? 1105 ASP D O     1 
ATOM   7821  C  CB    . ASP B  1  306 ? -6.383  31.671  55.608 1.00 33.47  ? 1105 ASP D CB    1 
ATOM   7822  C  CG    . ASP B  1  306 ? -5.545  31.633  56.873 1.00 36.24  ? 1105 ASP D CG    1 
ATOM   7823  O  OD1   . ASP B  1  306 ? -4.986  32.674  57.339 1.00 38.06  ? 1105 ASP D OD1   1 
ATOM   7824  O  OD2   . ASP B  1  306 ? -5.433  30.519  57.397 1.00 35.44  ? 1105 ASP D OD2   1 
ATOM   7825  N  N     . GLY B  1  307 ? -4.774  34.834  55.049 1.00 31.35  ? 1106 GLY D N     1 
ATOM   7826  C  CA    . GLY B  1  307 ? -3.460  35.410  54.761 1.00 29.50  ? 1106 GLY D CA    1 
ATOM   7827  C  C     . GLY B  1  307 ? -2.532  35.506  55.944 1.00 35.77  ? 1106 GLY D C     1 
ATOM   7828  O  O     . GLY B  1  307 ? -2.979  35.741  57.055 1.00 39.50  ? 1106 GLY D O     1 
ATOM   7829  N  N     . GLN B  1  308 ? -1.246  35.289  55.719 1.00 35.19  ? 1107 GLN D N     1 
ATOM   7830  C  CA    . GLN B  1  308 ? -0.251  35.482  56.755 1.00 36.75  ? 1107 GLN D CA    1 
ATOM   7831  C  C     . GLN B  1  308 ? 0.566   36.701  56.400 1.00 31.74  ? 1107 GLN D C     1 
ATOM   7832  O  O     . GLN B  1  308 ? 1.139   36.767  55.351 1.00 32.86  ? 1107 GLN D O     1 
ATOM   7833  C  CB    . GLN B  1  308 ? 0.619   34.234  56.879 1.00 42.24  ? 1107 GLN D CB    1 
ATOM   7834  C  CG    . GLN B  1  308 ? 1.848   34.388  57.780 1.00 42.27  ? 1107 GLN D CG    1 
ATOM   7835  C  CD    . GLN B  1  308 ? 1.490   34.257  59.247 1.00 46.92  ? 1107 GLN D CD    1 
ATOM   7836  O  OE1   . GLN B  1  308 ? 0.975   33.230  59.684 1.00 53.81  ? 1107 GLN D OE1   1 
ATOM   7837  N  NE2   . GLN B  1  308 ? 1.748   35.302  60.013 1.00 48.15  ? 1107 GLN D NE2   1 
ATOM   7838  N  N     . GLY B  1  309 ? 0.588   37.693  57.266 1.00 28.86  ? 1108 GLY D N     1 
ATOM   7839  C  CA    . GLY B  1  309 ? 1.295   38.922  56.973 1.00 26.70  ? 1108 GLY D CA    1 
ATOM   7840  C  C     . GLY B  1  309 ? 0.399   40.119  56.843 1.00 29.72  ? 1108 GLY D C     1 
ATOM   7841  O  O     . GLY B  1  309 ? -0.754  40.094  57.300 1.00 32.63  ? 1108 GLY D O     1 
ATOM   7842  N  N     . ASN B  1  310 ? 0.917   41.161  56.222 1.00 30.59  ? 1109 ASN D N     1 
ATOM   7843  C  CA    . ASN B  1  310 ? 0.217   42.434  56.087 1.00 29.29  ? 1109 ASN D CA    1 
ATOM   7844  C  C     . ASN B  1  310 ? -0.689  42.407  54.889 1.00 31.13  ? 1109 ASN D C     1 
ATOM   7845  O  O     . ASN B  1  310 ? -0.230  42.502  53.733 1.00 29.40  ? 1109 ASN D O     1 
ATOM   7846  C  CB    . ASN B  1  310 ? 1.251   43.554  55.943 1.00 31.56  ? 1109 ASN D CB    1 
ATOM   7847  C  CG    . ASN B  1  310 ? 0.615   44.920  55.683 1.00 34.89  ? 1109 ASN D CG    1 
ATOM   7848  O  OD1   . ASN B  1  310 ? -0.580  45.122  55.869 1.00 31.86  ? 1109 ASN D OD1   1 
ATOM   7849  N  ND2   . ASN B  1  310 ? 1.425   45.864  55.246 1.00 29.99  ? 1109 ASN D ND2   1 
ATOM   7850  N  N     . PHE B  1  311 ? -1.993  42.300  55.151 1.00 28.45  ? 1110 PHE D N     1 
ATOM   7851  C  CA    . PHE B  1  311 ? -2.932  42.246  54.050 1.00 25.75  ? 1110 PHE D CA    1 
ATOM   7852  C  C     . PHE B  1  311 ? -3.804  43.487  53.920 1.00 30.71  ? 1110 PHE D C     1 
ATOM   7853  O  O     . PHE B  1  311 ? -4.923  43.384  53.439 1.00 30.53  ? 1110 PHE D O     1 
ATOM   7854  C  CB    . PHE B  1  311 ? -3.817  41.024  54.176 1.00 24.31  ? 1110 PHE D CB    1 
ATOM   7855  C  CG    . PHE B  1  311 ? -3.237  39.835  53.545 1.00 28.86  ? 1110 PHE D CG    1 
ATOM   7856  C  CD1   . PHE B  1  311 ? -2.175  39.154  54.140 1.00 30.64  ? 1110 PHE D CD1   1 
ATOM   7857  C  CD2   . PHE B  1  311 ? -3.679  39.421  52.323 1.00 29.23  ? 1110 PHE D CD2   1 
ATOM   7858  C  CE1   . PHE B  1  311 ? -1.603  38.054  53.522 1.00 33.51  ? 1110 PHE D CE1   1 
ATOM   7859  C  CE2   . PHE B  1  311 ? -3.123  38.325  51.685 1.00 32.54  ? 1110 PHE D CE2   1 
ATOM   7860  C  CZ    . PHE B  1  311 ? -2.063  37.643  52.264 1.00 30.97  ? 1110 PHE D CZ    1 
ATOM   7861  N  N     . GLY B  1  312 ? -3.309  44.644  54.361 1.00 27.07  ? 1111 GLY D N     1 
ATOM   7862  C  CA    . GLY B  1  312 ? -4.078  45.886  54.219 1.00 30.67  ? 1111 GLY D CA    1 
ATOM   7863  C  C     . GLY B  1  312 ? -4.903  46.197  55.430 1.00 34.50  ? 1111 GLY D C     1 
ATOM   7864  O  O     . GLY B  1  312 ? -5.035  45.359  56.305 1.00 38.88  ? 1111 GLY D O     1 
ATOM   7865  N  N     . SER B  1  313 ? -5.503  47.382  55.477 1.00 33.52  ? 1112 SER D N     1 
ATOM   7866  C  CA    . SER B  1  313 ? -6.258  47.785  56.633 1.00 30.75  ? 1112 SER D CA    1 
ATOM   7867  C  C     . SER B  1  313 ? -7.429  48.600  56.187 1.00 32.01  ? 1112 SER D C     1 
ATOM   7868  O  O     . SER B  1  313 ? -7.573  48.969  55.057 1.00 29.92  ? 1112 SER D O     1 
ATOM   7869  C  CB    . SER B  1  313 ? -5.376  48.640  57.527 1.00 29.90  ? 1112 SER D CB    1 
ATOM   7870  O  OG    . SER B  1  313 ? -5.130  49.853  56.819 1.00 33.77  ? 1112 SER D OG    1 
ATOM   7871  N  N     A MET B  1  314 ? -8.327  48.851  57.110 0.50 35.14  ? 1113 MET D N     1 
ATOM   7872  N  N     B MET B  1  314 ? -8.228  48.966  57.136 0.50 37.22  ? 1113 MET D N     1 
ATOM   7873  C  CA    A MET B  1  314 ? -9.475  49.706  56.836 0.50 37.25  ? 1113 MET D CA    1 
ATOM   7874  C  CA    B MET B  1  314 ? -9.435  49.682  56.857 0.50 41.36  ? 1113 MET D CA    1 
ATOM   7875  C  C     A MET B  1  314 ? -9.074  51.143  56.532 0.50 40.47  ? 1113 MET D C     1 
ATOM   7876  C  C     B MET B  1  314 ? -9.066  51.111  56.519 0.50 43.30  ? 1113 MET D C     1 
ATOM   7877  O  O     A MET B  1  314 ? -9.885  51.967  56.113 0.50 40.62  ? 1113 MET D O     1 
ATOM   7878  O  O     B MET B  1  314 ? -9.878  51.904  56.069 0.50 43.93  ? 1113 MET D O     1 
ATOM   7879  C  CB    A MET B  1  314 ? -10.318 49.726  58.067 0.50 36.89  ? 1113 MET D CB    1 
ATOM   7880  C  CB    B MET B  1  314 ? -10.213 49.634  58.128 0.50 44.25  ? 1113 MET D CB    1 
ATOM   7881  C  CG    A MET B  1  314 ? -10.940 48.408  58.477 0.50 40.03  ? 1113 MET D CG    1 
ATOM   7882  C  CG    B MET B  1  314 ? -11.630 50.123  58.068 0.50 53.87  ? 1113 MET D CG    1 
ATOM   7883  S  SD    A MET B  1  314 ? -12.158 48.417  59.827 0.50 43.20  ? 1113 MET D SD    1 
ATOM   7884  S  SD    B MET B  1  314 ? -12.258 49.515  59.632 0.50 60.90  ? 1113 MET D SD    1 
ATOM   7885  C  CE    A MET B  1  314 ? -13.599 49.141  59.019 0.50 43.29  ? 1113 MET D CE    1 
ATOM   7886  C  CE    B MET B  1  314 ? -11.523 47.875  59.597 0.50 55.53  ? 1113 MET D CE    1 
ATOM   7887  N  N     . ASP B  1  315 ? -7.816  51.462  56.782 1.00 38.87  ? 1114 ASP D N     1 
ATOM   7888  C  CA    . ASP B  1  315 ? -7.395  52.772  56.486 1.00 39.35  ? 1114 ASP D CA    1 
ATOM   7889  C  C     . ASP B  1  315 ? -6.901  52.881  55.054 1.00 45.97  ? 1114 ASP D C     1 
ATOM   7890  O  O     . ASP B  1  315 ? -6.463  53.975  54.613 1.00 44.98  ? 1114 ASP D O     1 
ATOM   7891  C  CB    . ASP B  1  315 ? -6.345  53.270  57.447 1.00 41.12  ? 1114 ASP D CB    1 
ATOM   7892  C  CG    . ASP B  1  315 ? -6.938  53.733  58.781 1.00 46.35  ? 1114 ASP D CG    1 
ATOM   7893  O  OD1   . ASP B  1  315 ? -8.188  53.777  58.917 1.00 40.98  ? 1114 ASP D OD1   1 
ATOM   7894  O  OD2   . ASP B  1  315 ? -6.161  54.067  59.683 1.00 46.02  ? 1114 ASP D OD2   1 
ATOM   7895  N  N     . GLY B  1  316 ? -6.950  51.768  54.303 1.00 41.70  ? 1115 GLY D N     1 
ATOM   7896  C  CA    . GLY B  1  316 ? -6.517  51.847  52.904 1.00 37.88  ? 1115 GLY D CA    1 
ATOM   7897  C  C     . GLY B  1  316 ? -5.020  51.751  52.743 1.00 38.72  ? 1115 GLY D C     1 
ATOM   7898  O  O     . GLY B  1  316 ? -4.543  51.972  51.648 1.00 39.52  ? 1115 GLY D O     1 
ATOM   7899  N  N     . ASP B  1  317 ? -4.287  51.426  53.813 1.00 36.59  ? 1116 ASP D N     1 
ATOM   7900  C  CA    . ASP B  1  317 ? -2.904  50.972  53.698 1.00 43.78  ? 1116 ASP D CA    1 
ATOM   7901  C  C     . ASP B  1  317 ? -2.934  49.739  52.805 1.00 41.50  ? 1116 ASP D C     1 
ATOM   7902  O  O     . ASP B  1  317 ? -3.853  48.895  52.879 1.00 45.93  ? 1116 ASP D O     1 
ATOM   7903  C  CB    . ASP B  1  317 ? -2.340  50.570  55.053 1.00 46.42  ? 1116 ASP D CB    1 
ATOM   7904  C  CG    . ASP B  1  317 ? -2.218  51.753  56.003 1.00 59.47  ? 1116 ASP D CG    1 
ATOM   7905  O  OD1   . ASP B  1  317 ? -1.631  52.759  55.567 1.00 71.11  ? 1116 ASP D OD1   1 
ATOM   7906  O  OD2   . ASP B  1  317 ? -2.679  51.699  57.177 1.00 64.39  ? 1116 ASP D OD2   1 
ATOM   7907  N  N     . GLY B  1  318 ? -1.977  49.627  51.916 1.00 42.46  ? 1117 GLY D N     1 
ATOM   7908  C  CA    . GLY B  1  318 ? -2.004  48.461  51.042 1.00 40.03  ? 1117 GLY D CA    1 
ATOM   7909  C  C     . GLY B  1  318 ? -1.384  47.275  51.750 1.00 39.31  ? 1117 GLY D C     1 
ATOM   7910  O  O     . GLY B  1  318 ? -0.783  47.373  52.871 1.00 40.29  ? 1117 GLY D O     1 
ATOM   7911  N  N     . ALA B  1  319 ? -1.540  46.134  51.102 1.00 32.76  ? 1118 ALA D N     1 
ATOM   7912  C  CA    . ALA B  1  319 ? -0.970  44.959  51.626 1.00 30.01  ? 1118 ALA D CA    1 
ATOM   7913  C  C     . ALA B  1  319 ? 0.545   45.016  51.427 1.00 32.38  ? 1118 ALA D C     1 
ATOM   7914  O  O     . ALA B  1  319 ? 1.070   45.738  50.586 1.00 33.88  ? 1118 ALA D O     1 
ATOM   7915  C  CB    . ALA B  1  319 ? -1.555  43.769  50.922 1.00 23.86  ? 1118 ALA D CB    1 
ATOM   7916  N  N     . ALA B  1  320 ? 1.255   44.153  52.126 1.00 33.56  ? 1119 ALA D N     1 
ATOM   7917  C  CA    . ALA B  1  320 ? 2.702   44.058  51.892 1.00 30.42  ? 1119 ALA D CA    1 
ATOM   7918  C  C     . ALA B  1  320 ? 2.956   43.458  50.506 1.00 30.52  ? 1119 ALA D C     1 
ATOM   7919  O  O     . ALA B  1  320 ? 2.100   42.758  49.946 1.00 29.05  ? 1119 ALA D O     1 
ATOM   7920  C  CB    . ALA B  1  320 ? 3.367   43.241  52.955 1.00 26.28  ? 1119 ALA D CB    1 
ATOM   7921  N  N     . ALA B  1  321 ? 4.124   43.759  49.947 1.00 28.34  ? 1120 ALA D N     1 
ATOM   7922  C  CA    . ALA B  1  321 ? 4.531   43.225  48.640 1.00 28.89  ? 1120 ALA D CA    1 
ATOM   7923  C  C     . ALA B  1  321 ? 4.308   41.697  48.641 1.00 29.87  ? 1120 ALA D C     1 
ATOM   7924  O  O     . ALA B  1  321 ? 4.509   41.025  49.664 1.00 26.17  ? 1120 ALA D O     1 
ATOM   7925  C  CB    . ALA B  1  321 ? 6.004   43.548  48.375 1.00 27.10  ? 1120 ALA D CB    1 
ATOM   7926  N  N     . MET B  1  322 ? 3.940   41.144  47.486 1.00 30.71  ? 1121 MET D N     1 
ATOM   7927  C  CA    . MET B  1  322 ? 3.677   39.689  47.412 1.00 34.61  ? 1121 MET D CA    1 
ATOM   7928  C  C     . MET B  1  322 ? 4.869   38.799  47.801 1.00 33.74  ? 1121 MET D C     1 
ATOM   7929  O  O     . MET B  1  322 ? 4.639   37.707  48.237 1.00 34.11  ? 1121 MET D O     1 
ATOM   7930  C  CB    . MET B  1  322 ? 3.030   39.267  46.077 1.00 38.31  ? 1121 MET D CB    1 
ATOM   7931  C  CG    . MET B  1  322 ? 3.936   39.214  44.884 1.00 39.15  ? 1121 MET D CG    1 
ATOM   7932  S  SD    . MET B  1  322 ? 3.114   38.648  43.386 1.00 42.68  ? 1121 MET D SD    1 
ATOM   7933  C  CE    . MET B  1  322 ? 2.440   40.208  42.817 1.00 40.04  ? 1121 MET D CE    1 
ATOM   7934  N  N     . ARG B  1  323 ? 6.109   39.293  47.713 1.00 34.12  ? 1122 ARG D N     1 
ATOM   7935  C  CA    . ARG B  1  323 ? 7.289   38.505  48.191 1.00 29.37  ? 1122 ARG D CA    1 
ATOM   7936  C  C     . ARG B  1  323 ? 7.204   38.241  49.681 1.00 34.29  ? 1122 ARG D C     1 
ATOM   7937  O  O     . ARG B  1  323 ? 7.826   37.279  50.154 1.00 33.13  ? 1122 ARG D O     1 
ATOM   7938  C  CB    . ARG B  1  323 ? 8.642   39.210  47.959 1.00 28.03  ? 1122 ARG D CB    1 
ATOM   7939  C  CG    . ARG B  1  323 ? 8.762   40.599  48.558 1.00 28.86  ? 1122 ARG D CG    1 
ATOM   7940  C  CD    . ARG B  1  323 ? 10.092  41.329  48.291 1.00 33.79  ? 1122 ARG D CD    1 
ATOM   7941  N  NE    . ARG B  1  323 ? 11.152  40.752  49.097 1.00 33.27  ? 1122 ARG D NE    1 
ATOM   7942  C  CZ    . ARG B  1  323 ? 12.414  41.144  49.164 1.00 37.86  ? 1122 ARG D CZ    1 
ATOM   7943  N  NH1   . ARG B  1  323 ? 12.894  42.188  48.482 1.00 36.15  ? 1122 ARG D NH1   1 
ATOM   7944  N  NH2   . ARG B  1  323 ? 13.218  40.448  49.963 1.00 36.70  ? 1122 ARG D NH2   1 
ATOM   7945  N  N     . TYR B  1  324 ? 6.495   39.100  50.439 1.00 27.81  ? 1123 TYR D N     1 
ATOM   7946  C  CA    . TYR B  1  324 ? 6.454   38.910  51.890 1.00 31.68  ? 1123 TYR D CA    1 
ATOM   7947  C  C     . TYR B  1  324 ? 5.275   38.101  52.410 1.00 37.62  ? 1123 TYR D C     1 
ATOM   7948  O  O     . TYR B  1  324 ? 5.410   37.392  53.417 1.00 35.43  ? 1123 TYR D O     1 
ATOM   7949  C  CB    . TYR B  1  324 ? 6.495   40.233  52.610 1.00 32.15  ? 1123 TYR D CB    1 
ATOM   7950  C  CG    . TYR B  1  324 ? 7.735   41.034  52.320 1.00 34.71  ? 1123 TYR D CG    1 
ATOM   7951  C  CD1   . TYR B  1  324 ? 9.021   40.507  52.610 1.00 33.59  ? 1123 TYR D CD1   1 
ATOM   7952  C  CD2   . TYR B  1  324 ? 7.635   42.295  51.771 1.00 31.25  ? 1123 TYR D CD2   1 
ATOM   7953  C  CE1   . TYR B  1  324 ? 10.168  41.220  52.344 1.00 37.05  ? 1123 TYR D CE1   1 
ATOM   7954  C  CE2   . TYR B  1  324 ? 8.781   43.042  51.496 1.00 33.96  ? 1123 TYR D CE2   1 
ATOM   7955  C  CZ    . TYR B  1  324 ? 10.045  42.500  51.796 1.00 38.09  ? 1123 TYR D CZ    1 
ATOM   7956  O  OH    . TYR B  1  324 ? 11.182  43.211  51.548 1.00 35.45  ? 1123 TYR D OH    1 
ATOM   7957  N  N     . THR B  1  325 ? 4.127   38.191  51.751 1.00 37.40  ? 1124 THR D N     1 
ATOM   7958  C  CA    . THR B  1  325 ? 2.962   37.533  52.308 1.00 34.97  ? 1124 THR D CA    1 
ATOM   7959  C  C     . THR B  1  325 ? 2.825   36.075  51.930 1.00 35.16  ? 1124 THR D C     1 
ATOM   7960  O  O     . THR B  1  325 ? 3.464   35.607  51.023 1.00 37.69  ? 1124 THR D O     1 
ATOM   7961  C  CB    . THR B  1  325 ? 1.723   38.265  51.923 1.00 30.29  ? 1124 THR D CB    1 
ATOM   7962  O  OG1   . THR B  1  325 ? 1.587   38.269  50.485 1.00 33.27  ? 1124 THR D OG1   1 
ATOM   7963  C  CG2   . THR B  1  325 ? 1.800   39.644  52.421 1.00 30.89  ? 1124 THR D CG2   1 
ATOM   7964  N  N     . GLU B  1  326 ? 2.006   35.354  52.668 1.00 35.79  ? 1125 GLU D N     1 
ATOM   7965  C  CA    . GLU B  1  326 ? 1.697   33.966  52.410 1.00 42.58  ? 1125 GLU D CA    1 
ATOM   7966  C  C     . GLU B  1  326 ? 0.194   33.778  52.516 1.00 40.01  ? 1125 GLU D C     1 
ATOM   7967  O  O     . GLU B  1  326 ? -0.462  34.557  53.131 1.00 40.88  ? 1125 GLU D O     1 
ATOM   7968  C  CB    . GLU B  1  326 ? 2.400   33.085  53.422 1.00 49.94  ? 1125 GLU D CB    1 
ATOM   7969  C  CG    . GLU B  1  326 ? 3.776   32.645  53.007 1.00 63.37  ? 1125 GLU D CG    1 
ATOM   7970  C  CD    . GLU B  1  326 ? 4.505   31.936  54.133 1.00 70.26  ? 1125 GLU D CD    1 
ATOM   7971  O  OE1   . GLU B  1  326 ? 4.773   30.717  53.997 1.00 71.36  ? 1125 GLU D OE1   1 
ATOM   7972  O  OE2   . GLU B  1  326 ? 4.776   32.591  55.164 1.00 82.07  ? 1125 GLU D OE2   1 
ATOM   7973  N  N     . ALA B  1  327 ? -0.353  32.710  51.979 1.00 36.61  ? 1126 ALA D N     1 
ATOM   7974  C  CA    . ALA B  1  327 ? -1.778  32.547  51.988 1.00 34.94  ? 1126 ALA D CA    1 
ATOM   7975  C  C     . ALA B  1  327 ? -2.137  31.089  51.807 1.00 38.11  ? 1126 ALA D C     1 
ATOM   7976  O  O     . ALA B  1  327 ? -1.351  30.275  51.343 1.00 34.53  ? 1126 ALA D O     1 
ATOM   7977  C  CB    . ALA B  1  327 ? -2.400  33.352  50.851 1.00 31.32  ? 1126 ALA D CB    1 
ATOM   7978  N  N     . ARG B  1  328 ? -3.384  30.787  52.153 1.00 35.59  ? 1127 ARG D N     1 
ATOM   7979  C  CA    . ARG B  1  328 ? -3.950  29.487  51.926 1.00 33.10  ? 1127 ARG D CA    1 
ATOM   7980  C  C     . ARG B  1  328 ? -5.470  29.663  51.959 1.00 35.38  ? 1127 ARG D C     1 
ATOM   7981  O  O     . ARG B  1  328 ? -5.966  30.735  52.220 1.00 36.22  ? 1127 ARG D O     1 
ATOM   7982  C  CB    . ARG B  1  328 ? -3.457  28.535  53.010 1.00 32.47  ? 1127 ARG D CB    1 
ATOM   7983  C  CG    . ARG B  1  328 ? -3.931  28.839  54.407 1.00 33.45  ? 1127 ARG D CG    1 
ATOM   7984  C  CD    . ARG B  1  328 ? -3.204  27.962  55.405 1.00 33.03  ? 1127 ARG D CD    1 
ATOM   7985  N  NE    . ARG B  1  328 ? -3.620  28.320  56.767 1.00 37.07  ? 1127 ARG D NE    1 
ATOM   7986  C  CZ    . ARG B  1  328 ? -3.054  27.851  57.881 1.00 38.77  ? 1127 ARG D CZ    1 
ATOM   7987  N  NH1   . ARG B  1  328 ? -2.045  26.984  57.827 1.00 36.36  ? 1127 ARG D NH1   1 
ATOM   7988  N  NH2   . ARG B  1  328 ? -3.495  28.278  59.063 1.00 37.20  ? 1127 ARG D NH2   1 
ATOM   7989  N  N     . MET B  1  329 ? -6.206  28.600  51.695 1.00 34.74  ? 1128 MET D N     1 
ATOM   7990  C  CA    . MET B  1  329 ? -7.649  28.636  51.763 1.00 31.91  ? 1128 MET D CA    1 
ATOM   7991  C  C     . MET B  1  329 ? -8.105  28.734  53.199 1.00 32.81  ? 1128 MET D C     1 
ATOM   7992  O  O     . MET B  1  329 ? -7.494  28.149  54.135 1.00 31.23  ? 1128 MET D O     1 
ATOM   7993  C  CB    . MET B  1  329 ? -8.218  27.359  51.214 1.00 33.97  ? 1128 MET D CB    1 
ATOM   7994  C  CG    . MET B  1  329 ? -7.949  27.097  49.751 1.00 39.48  ? 1128 MET D CG    1 
ATOM   7995  S  SD    . MET B  1  329 ? -8.669  25.495  49.413 1.00 50.07  ? 1128 MET D SD    1 
ATOM   7996  C  CE    . MET B  1  329 ? -7.299  24.712  48.600 1.00 52.97  ? 1128 MET D CE    1 
ATOM   7997  N  N     . THR B  1  330 ? -9.183  29.498  53.391 1.00 28.65  ? 1129 THR D N     1 
ATOM   7998  C  CA    . THR B  1  330 ? -9.912  29.410  54.658 1.00 28.71  ? 1129 THR D CA    1 
ATOM   7999  C  C     . THR B  1  330 ? -10.686 28.082  54.665 1.00 27.78  ? 1129 THR D C     1 
ATOM   8000  O  O     . THR B  1  330 ? -10.825 27.441  53.639 1.00 25.22  ? 1129 THR D O     1 
ATOM   8001  C  CB    . THR B  1  330 ? -10.864 30.603  54.850 1.00 28.85  ? 1129 THR D CB    1 
ATOM   8002  O  OG1   . THR B  1  330 ? -11.793 30.626  53.789 1.00 26.88  ? 1129 THR D OG1   1 
ATOM   8003  C  CG2   . THR B  1  330 ? -10.043 31.895  54.774 1.00 30.01  ? 1129 THR D CG2   1 
ATOM   8004  N  N     . LYS B  1  331 ? -11.141 27.671  55.829 1.00 28.68  ? 1130 LYS D N     1 
ATOM   8005  C  CA    . LYS B  1  331 ? -11.978 26.496  55.927 1.00 33.53  ? 1130 LYS D CA    1 
ATOM   8006  C  C     . LYS B  1  331 ? -13.251 26.571  55.082 1.00 33.56  ? 1130 LYS D C     1 
ATOM   8007  O  O     . LYS B  1  331 ? -13.569 25.605  54.434 1.00 32.44  ? 1130 LYS D O     1 
ATOM   8008  C  CB    . LYS B  1  331 ? -12.299 26.213  57.387 1.00 34.73  ? 1130 LYS D CB    1 
ATOM   8009  C  CG    . LYS B  1  331 ? -11.145 25.536  58.083 1.00 38.23  ? 1130 LYS D CG    1 
ATOM   8010  C  CD    . LYS B  1  331 ? -11.270 25.585  59.590 1.00 48.54  ? 1130 LYS D CD    1 
ATOM   8011  C  CE    . LYS B  1  331 ? -9.880  25.265  60.139 1.00 65.41  ? 1130 LYS D CE    1 
ATOM   8012  N  NZ    . LYS B  1  331 ? -9.685  25.425  61.616 1.00 77.78  ? 1130 LYS D NZ    1 
ATOM   8013  N  N     . ILE B  1  332 ? -13.937 27.723  55.040 1.00 30.38  ? 1131 ILE D N     1 
ATOM   8014  C  CA    . ILE B  1  332 ? -15.192 27.837  54.274 1.00 26.71  ? 1131 ILE D CA    1 
ATOM   8015  C  C     . ILE B  1  332 ? -14.928 27.736  52.787 1.00 29.90  ? 1131 ILE D C     1 
ATOM   8016  O  O     . ILE B  1  332 ? -15.806 27.299  52.032 1.00 28.24  ? 1131 ILE D O     1 
ATOM   8017  C  CB    . ILE B  1  332 ? -15.919 29.163  54.587 1.00 28.20  ? 1131 ILE D CB    1 
ATOM   8018  C  CG1   . ILE B  1  332 ? -17.446 28.956  54.476 1.00 25.73  ? 1131 ILE D CG1   1 
ATOM   8019  C  CG2   . ILE B  1  332 ? -15.362 30.323  53.737 1.00 26.29  ? 1131 ILE D CG2   1 
ATOM   8020  C  CD1   . ILE B  1  332 ? -18.216 30.200  54.838 1.00 26.72  ? 1131 ILE D CD1   1 
ATOM   8021  N  N     . THR B  1  333 ? -13.724 28.125  52.339 1.00 28.34  ? 1132 THR D N     1 
ATOM   8022  C  CA    . THR B  1  333 ? -13.363 27.980  50.926 1.00 27.19  ? 1132 THR D CA    1 
ATOM   8023  C  C     . THR B  1  333 ? -13.327 26.515  50.482 1.00 25.82  ? 1132 THR D C     1 
ATOM   8024  O  O     . THR B  1  333 ? -13.592 26.208  49.303 1.00 28.28  ? 1132 THR D O     1 
ATOM   8025  C  CB    . THR B  1  333 ? -12.017 28.665  50.638 1.00 30.33  ? 1132 THR D CB    1 
ATOM   8026  O  OG1   . THR B  1  333 ? -12.223 30.080  50.692 1.00 33.57  ? 1132 THR D OG1   1 
ATOM   8027  C  CG2   . THR B  1  333 ? -11.489 28.309  49.247 1.00 27.40  ? 1132 THR D CG2   1 
ATOM   8028  N  N     . LEU B  1  334 ? -13.032 25.617  51.415 1.00 26.02  ? 1133 LEU D N     1 
ATOM   8029  C  CA    . LEU B  1  334 ? -13.071 24.164  51.109 1.00 30.80  ? 1133 LEU D CA    1 
ATOM   8030  C  C     . LEU B  1  334 ? -14.502 23.773  50.676 1.00 31.40  ? 1133 LEU D C     1 
ATOM   8031  O  O     . LEU B  1  334 ? -14.700 22.919  49.834 1.00 31.62  ? 1133 LEU D O     1 
ATOM   8032  C  CB    . LEU B  1  334 ? -12.665 23.314  52.303 1.00 26.61  ? 1133 LEU D CB    1 
ATOM   8033  C  CG    . LEU B  1  334 ? -11.200 23.366  52.757 1.00 33.32  ? 1133 LEU D CG    1 
ATOM   8034  C  CD1   . LEU B  1  334 ? -11.015 22.566  54.045 1.00 29.45  ? 1133 LEU D CD1   1 
ATOM   8035  C  CD2   . LEU B  1  334 ? -10.260 22.827  51.688 1.00 33.64  ? 1133 LEU D CD2   1 
ATOM   8036  N  N     . GLU B  1  335 ? -15.499 24.443  51.261 1.00 29.67  ? 1134 GLU D N     1 
ATOM   8037  C  CA    . GLU B  1  335 ? -16.890 24.243  50.864 1.00 28.28  ? 1134 GLU D CA    1 
ATOM   8038  C  C     . GLU B  1  335 ? -17.174 24.711  49.414 1.00 30.66  ? 1134 GLU D C     1 
ATOM   8039  O  O     . GLU B  1  335 ? -17.996 24.141  48.715 1.00 33.68  ? 1134 GLU D O     1 
ATOM   8040  C  CB    . GLU B  1  335 ? -17.819 24.887  51.877 1.00 27.98  ? 1134 GLU D CB    1 
ATOM   8041  C  CG    . GLU B  1  335 ? -17.738 24.276  53.273 1.00 31.23  ? 1134 GLU D CG    1 
ATOM   8042  C  CD    . GLU B  1  335 ? -17.778 22.716  53.250 1.00 35.67  ? 1134 GLU D CD    1 
ATOM   8043  O  OE1   . GLU B  1  335 ? -17.110 22.141  54.093 1.00 37.52  ? 1134 GLU D OE1   1 
ATOM   8044  O  OE2   . GLU B  1  335 ? -18.454 22.079  52.405 1.00 33.78  ? 1134 GLU D OE2   1 
ATOM   8045  N  N     . LEU B  1  336 ? -16.440 25.722  48.939 1.00 26.87  ? 1135 LEU D N     1 
ATOM   8046  C  CA    . LEU B  1  336 ? -16.571 26.145  47.546 1.00 29.24  ? 1135 LEU D CA    1 
ATOM   8047  C  C     . LEU B  1  336 ? -15.980 25.151  46.568 1.00 30.06  ? 1135 LEU D C     1 
ATOM   8048  O  O     . LEU B  1  336 ? -16.480 24.992  45.486 1.00 31.14  ? 1135 LEU D O     1 
ATOM   8049  C  CB    . LEU B  1  336 ? -15.909 27.503  47.309 1.00 26.57  ? 1135 LEU D CB    1 
ATOM   8050  C  CG    . LEU B  1  336 ? -16.524 28.725  47.940 1.00 29.50  ? 1135 LEU D CG    1 
ATOM   8051  C  CD1   . LEU B  1  336 ? -15.641 29.927  47.692 1.00 26.43  ? 1135 LEU D CD1   1 
ATOM   8052  C  CD2   . LEU B  1  336 ? -17.944 28.979  47.421 1.00 29.95  ? 1135 LEU D CD2   1 
ATOM   8053  N  N     . LEU B  1  337 ? -14.889 24.504  46.966 1.00 31.58  ? 1136 LEU D N     1 
ATOM   8054  C  CA    . LEU B  1  337 ? -14.195 23.576  46.111 1.00 32.08  ? 1136 LEU D CA    1 
ATOM   8055  C  C     . LEU B  1  337 ? -14.608 22.113  46.316 1.00 34.13  ? 1136 LEU D C     1 
ATOM   8056  O  O     . LEU B  1  337 ? -14.194 21.264  45.576 1.00 33.29  ? 1136 LEU D O     1 
ATOM   8057  C  CB    . LEU B  1  337 ? -12.698 23.704  46.326 1.00 28.42  ? 1136 LEU D CB    1 
ATOM   8058  C  CG    . LEU B  1  337 ? -12.165 25.070  45.902 1.00 33.73  ? 1136 LEU D CG    1 
ATOM   8059  C  CD1   . LEU B  1  337 ? -10.963 25.419  46.728 1.00 32.21  ? 1136 LEU D CD1   1 
ATOM   8060  C  CD2   . LEU B  1  337 ? -11.849 25.156  44.406 1.00 31.47  ? 1136 LEU D CD2   1 
ATOM   8061  N  N     . ARG B  1  338 ? -15.432 21.836  47.305 1.00 37.05  ? 1137 ARG D N     1 
ATOM   8062  C  CA    . ARG B  1  338 ? -15.803 20.472  47.631 1.00 39.25  ? 1137 ARG D CA    1 
ATOM   8063  C  C     . ARG B  1  338 ? -16.377 19.711  46.442 1.00 39.80  ? 1137 ARG D C     1 
ATOM   8064  O  O     . ARG B  1  338 ? -17.367 20.149  45.861 1.00 38.09  ? 1137 ARG D O     1 
ATOM   8065  C  CB    . ARG B  1  338 ? -16.858 20.549  48.705 1.00 40.52  ? 1137 ARG D CB    1 
ATOM   8066  C  CG    . ARG B  1  338 ? -17.095 19.240  49.433 1.00 41.40  ? 1137 ARG D CG    1 
ATOM   8067  C  CD    . ARG B  1  338 ? -17.811 19.469  50.760 1.00 43.98  ? 1137 ARG D CD    1 
ATOM   8068  N  NE    . ARG B  1  338 ? -18.946 18.566  50.894 1.00 55.66  ? 1137 ARG D NE    1 
ATOM   8069  C  CZ    . ARG B  1  338 ? -19.925 18.663  51.798 1.00 57.38  ? 1137 ARG D CZ    1 
ATOM   8070  N  NH1   . ARG B  1  338 ? -20.862 17.730  51.807 1.00 49.46  ? 1137 ARG D NH1   1 
ATOM   8071  N  NH2   . ARG B  1  338 ? -19.987 19.680  52.670 1.00 47.32  ? 1137 ARG D NH2   1 
ATOM   8072  N  N     . ASP B  1  339 ? -15.789 18.555  46.122 1.00 35.97  ? 1138 ASP D N     1 
ATOM   8073  C  CA    . ASP B  1  339 ? -16.327 17.673  45.091 1.00 35.71  ? 1138 ASP D CA    1 
ATOM   8074  C  C     . ASP B  1  339 ? -16.117 18.155  43.683 1.00 35.61  ? 1138 ASP D C     1 
ATOM   8075  O  O     . ASP B  1  339 ? -16.741 17.674  42.743 1.00 31.70  ? 1138 ASP D O     1 
ATOM   8076  C  CB    . ASP B  1  339 ? -17.811 17.434  45.295 1.00 41.77  ? 1138 ASP D CB    1 
ATOM   8077  C  CG    . ASP B  1  339 ? -18.111 16.808  46.646 1.00 51.18  ? 1138 ASP D CG    1 
ATOM   8078  O  OD1   . ASP B  1  339 ? -17.250 16.087  47.201 1.00 55.01  ? 1138 ASP D OD1   1 
ATOM   8079  O  OD2   . ASP B  1  339 ? -19.230 16.988  47.141 1.00 51.69  ? 1138 ASP D OD2   1 
ATOM   8080  N  N     . ILE B  1  340 ? -15.192 19.082  43.528 1.00 31.11  ? 1139 ILE D N     1 
ATOM   8081  C  CA    . ILE B  1  340 ? -14.845 19.590  42.233 1.00 32.09  ? 1139 ILE D CA    1 
ATOM   8082  C  C     . ILE B  1  340 ? -14.229 18.482  41.354 1.00 37.84  ? 1139 ILE D C     1 
ATOM   8083  O  O     . ILE B  1  340 ? -14.326 18.531  40.135 1.00 35.42  ? 1139 ILE D O     1 
ATOM   8084  C  CB    . ILE B  1  340 ? -13.892 20.816  42.361 1.00 30.15  ? 1139 ILE D CB    1 
ATOM   8085  C  CG1   . ILE B  1  340 ? -13.825 21.533  41.031 1.00 27.18  ? 1139 ILE D CG1   1 
ATOM   8086  C  CG2   . ILE B  1  340 ? -12.490 20.418  42.773 1.00 29.37  ? 1139 ILE D CG2   1 
ATOM   8087  C  CD1   . ILE B  1  340 ? -13.216 22.903  41.149 1.00 25.41  ? 1139 ILE D CD1   1 
ATOM   8088  N  N     . ASN B  1  341 ? -13.602 17.491  41.976 1.00 36.91  ? 1140 ASN D N     1 
ATOM   8089  C  CA    . ASN B  1  341 ? -13.009 16.407  41.224 1.00 41.40  ? 1140 ASN D CA    1 
ATOM   8090  C  C     . ASN B  1  341 ? -13.903 15.206  41.121 1.00 45.68  ? 1140 ASN D C     1 
ATOM   8091  O  O     . ASN B  1  341 ? -13.473 14.151  40.693 1.00 54.10  ? 1140 ASN D O     1 
ATOM   8092  C  CB    . ASN B  1  341 ? -11.655 16.036  41.795 1.00 37.47  ? 1140 ASN D CB    1 
ATOM   8093  C  CG    . ASN B  1  341 ? -10.638 17.145  41.549 1.00 46.76  ? 1140 ASN D CG    1 
ATOM   8094  O  OD1   . ASN B  1  341 ? -10.510 17.680  40.428 1.00 48.53  ? 1140 ASN D OD1   1 
ATOM   8095  N  ND2   . ASN B  1  341 ? -9.967  17.559  42.607 1.00 55.24  ? 1140 ASN D ND2   1 
ATOM   8096  N  N     . LYS B  1  342 ? -15.166 15.370  41.467 1.00 41.51  ? 1141 LYS D N     1 
ATOM   8097  C  CA    . LYS B  1  342 ? -16.132 14.276  41.328 1.00 39.75  ? 1141 LYS D CA    1 
ATOM   8098  C  C     . LYS B  1  342 ? -17.108 14.582  40.218 1.00 39.61  ? 1141 LYS D C     1 
ATOM   8099  O  O     . LYS B  1  342 ? -18.287 14.321  40.352 1.00 40.40  ? 1141 LYS D O     1 
ATOM   8100  C  CB    . LYS B  1  342 ? -16.839 13.990  42.649 1.00 37.96  ? 1141 LYS D CB    1 
ATOM   8101  C  CG    . LYS B  1  342 ? -15.869 13.704  43.783 1.00 40.97  ? 1141 LYS D CG    1 
ATOM   8102  C  CD    . LYS B  1  342 ? -16.535 13.045  44.958 1.00 52.46  ? 1141 LYS D CD    1 
ATOM   8103  C  CE    . LYS B  1  342 ? -15.781 13.233  46.273 1.00 56.53  ? 1141 LYS D CE    1 
ATOM   8104  N  NZ    . LYS B  1  342 ? -16.121 14.563  46.848 1.00 61.61  ? 1141 LYS D NZ    1 
ATOM   8105  N  N     . ASP B  1  343 ? -16.604 15.170  39.127 1.00 40.47  ? 1142 ASP D N     1 
ATOM   8106  C  CA    . ASP B  1  343 ? -17.409 15.509  37.961 1.00 39.16  ? 1142 ASP D CA    1 
ATOM   8107  C  C     . ASP B  1  343 ? -18.688 16.338  38.263 1.00 41.79  ? 1142 ASP D C     1 
ATOM   8108  O  O     . ASP B  1  343 ? -19.753 16.183  37.650 1.00 43.60  ? 1142 ASP D O     1 
ATOM   8109  C  CB    . ASP B  1  343 ? -17.742 14.261  37.196 1.00 37.84  ? 1142 ASP D CB    1 
ATOM   8110  C  CG    . ASP B  1  343 ? -18.341 14.557  35.833 1.00 43.45  ? 1142 ASP D CG    1 
ATOM   8111  O  OD1   . ASP B  1  343 ? -17.981 15.573  35.240 1.00 41.47  ? 1142 ASP D OD1   1 
ATOM   8112  O  OD2   . ASP B  1  343 ? -19.188 13.785  35.352 1.00 47.12  ? 1142 ASP D OD2   1 
ATOM   8113  N  N     . THR B  1  344 ? -18.558 17.224  39.219 1.00 40.63  ? 1143 THR D N     1 
ATOM   8114  C  CA    . THR B  1  344 ? -19.671 18.052  39.599 1.00 38.27  ? 1143 THR D CA    1 
ATOM   8115  C  C     . THR B  1  344 ? -19.865 19.211  38.657 1.00 38.46  ? 1143 THR D C     1 
ATOM   8116  O  O     . THR B  1  344 ? -20.998 19.650  38.445 1.00 36.66  ? 1143 THR D O     1 
ATOM   8117  C  CB    . THR B  1  344 ? -19.537 18.556  41.038 1.00 36.84  ? 1143 THR D CB    1 
ATOM   8118  O  OG1   . THR B  1  344 ? -18.170 18.882  41.298 1.00 35.42  ? 1143 THR D OG1   1 
ATOM   8119  C  CG2   . THR B  1  344 ? -19.967 17.468  41.952 1.00 33.21  ? 1143 THR D CG2   1 
ATOM   8120  N  N     . ILE B  1  345 ? -18.772 19.742  38.120 1.00 35.56  ? 1144 ILE D N     1 
ATOM   8121  C  CA    . ILE B  1  345 ? -18.880 20.912  37.265 1.00 31.77  ? 1144 ILE D CA    1 
ATOM   8122  C  C     . ILE B  1  345 ? -18.111 20.681  36.014 1.00 32.42  ? 1144 ILE D C     1 
ATOM   8123  O  O     . ILE B  1  345 ? -17.233 19.821  35.963 1.00 37.41  ? 1144 ILE D O     1 
ATOM   8124  C  CB    . ILE B  1  345 ? -18.373 22.164  38.023 1.00 35.61  ? 1144 ILE D CB    1 
ATOM   8125  C  CG1   . ILE B  1  345 ? -16.942 21.967  38.553 1.00 34.98  ? 1144 ILE D CG1   1 
ATOM   8126  C  CG2   . ILE B  1  345 ? -19.259 22.425  39.223 1.00 26.13  ? 1144 ILE D CG2   1 
ATOM   8127  C  CD1   . ILE B  1  345 ? -15.852 22.275  37.540 1.00 35.25  ? 1144 ILE D CD1   1 
ATOM   8128  N  N     . ASP B  1  346 ? -18.374 21.475  34.994 1.00 33.37  ? 1145 ASP D N     1 
ATOM   8129  C  CA    . ASP B  1  346 ? -17.701 21.335  33.713 1.00 30.28  ? 1145 ASP D CA    1 
ATOM   8130  C  C     . ASP B  1  346 ? -16.388 22.062  33.614 1.00 38.38  ? 1145 ASP D C     1 
ATOM   8131  O  O     . ASP B  1  346 ? -16.323 23.306  33.724 1.00 34.30  ? 1145 ASP D O     1 
ATOM   8132  C  CB    . ASP B  1  346 ? -18.591 21.803  32.572 1.00 31.80  ? 1145 ASP D CB    1 
ATOM   8133  C  CG    . ASP B  1  346 ? -19.797 20.880  32.344 1.00 37.52  ? 1145 ASP D CG    1 
ATOM   8134  O  OD1   . ASP B  1  346 ? -19.897 19.783  32.903 1.00 38.78  ? 1145 ASP D OD1   1 
ATOM   8135  O  OD2   . ASP B  1  346 ? -20.668 21.279  31.586 1.00 35.11  ? 1145 ASP D OD2   1 
ATOM   8136  N  N     . PHE B  1  347 ? -15.310 21.305  33.372 1.00 33.80  ? 1146 PHE D N     1 
ATOM   8137  C  CA    . PHE B  1  347 ? -14.036 21.909  33.049 1.00 31.32  ? 1146 PHE D CA    1 
ATOM   8138  C  C     . PHE B  1  347 ? -13.992 22.398  31.614 1.00 34.37  ? 1146 PHE D C     1 
ATOM   8139  O  O     . PHE B  1  347 ? -14.732 21.949  30.755 1.00 36.47  ? 1146 PHE D O     1 
ATOM   8140  C  CB    . PHE B  1  347 ? -12.914 20.926  33.327 1.00 30.63  ? 1146 PHE D CB    1 
ATOM   8141  C  CG    . PHE B  1  347 ? -12.585 20.806  34.781 1.00 35.02  ? 1146 PHE D CG    1 
ATOM   8142  C  CD1   . PHE B  1  347 ? -13.284 19.941  35.612 1.00 33.27  ? 1146 PHE D CD1   1 
ATOM   8143  C  CD2   . PHE B  1  347 ? -11.545 21.554  35.328 1.00 31.98  ? 1146 PHE D CD2   1 
ATOM   8144  C  CE1   . PHE B  1  347 ? -12.919 19.851  36.963 1.00 33.90  ? 1146 PHE D CE1   1 
ATOM   8145  C  CE2   . PHE B  1  347 ? -11.210 21.481  36.675 1.00 29.79  ? 1146 PHE D CE2   1 
ATOM   8146  C  CZ    . PHE B  1  347 ? -11.860 20.618  37.476 1.00 29.17  ? 1146 PHE D CZ    1 
ATOM   8147  N  N     . ILE B  1  348 ? -13.109 23.341  31.349 1.00 34.67  ? 1147 ILE D N     1 
ATOM   8148  C  CA    . ILE B  1  348 ? -12.915 23.868  30.009 1.00 30.53  ? 1147 ILE D CA    1 
ATOM   8149  C  C     . ILE B  1  348 ? -11.414 24.063  29.792 1.00 31.63  ? 1147 ILE D C     1 
ATOM   8150  O  O     . ILE B  1  348 ? -10.627 24.053  30.749 1.00 32.16  ? 1147 ILE D O     1 
ATOM   8151  C  CB    . ILE B  1  348 ? -13.624 25.233  29.805 1.00 31.04  ? 1147 ILE D CB    1 
ATOM   8152  C  CG1   . ILE B  1  348 ? -13.291 26.201  30.958 1.00 34.16  ? 1147 ILE D CG1   1 
ATOM   8153  C  CG2   . ILE B  1  348 ? -15.143 25.083  29.722 1.00 30.08  ? 1147 ILE D CG2   1 
ATOM   8154  C  CD1   . ILE B  1  348 ? -13.595 27.644  30.616 1.00 28.18  ? 1147 ILE D CD1   1 
ATOM   8155  N  N     . ASP B  1  349 ? -11.028 24.272  28.543 1.00 28.97  ? 1148 ASP D N     1 
ATOM   8156  C  CA    . ASP B  1  349 ? -9.650  24.562  28.254 1.00 36.09  ? 1148 ASP D CA    1 
ATOM   8157  C  C     . ASP B  1  349 ? -9.242  25.926  28.747 1.00 38.04  ? 1148 ASP D C     1 
ATOM   8158  O  O     . ASP B  1  349 ? -9.981  26.872  28.637 1.00 37.04  ? 1148 ASP D O     1 
ATOM   8159  C  CB    . ASP B  1  349 ? -9.371  24.465  26.752 1.00 34.48  ? 1148 ASP D CB    1 
ATOM   8160  C  CG    . ASP B  1  349 ? -9.301  23.034  26.282 1.00 40.36  ? 1148 ASP D CG    1 
ATOM   8161  O  OD1   . ASP B  1  349 ? -9.381  22.069  27.092 1.00 40.30  ? 1148 ASP D OD1   1 
ATOM   8162  O  OD2   . ASP B  1  349 ? -9.148  22.914  25.070 1.00 47.68  ? 1148 ASP D OD2   1 
ATOM   8163  N  N     . ASN B  1  350 ? -8.022  26.013  29.240 1.00 38.92  ? 1149 ASN D N     1 
ATOM   8164  C  CA    . ASN B  1  350 ? -7.450  27.266  29.679 1.00 40.37  ? 1149 ASN D CA    1 
ATOM   8165  C  C     . ASN B  1  350 ? -7.115  28.173  28.468 1.00 39.58  ? 1149 ASN D C     1 
ATOM   8166  O  O     . ASN B  1  350 ? -7.263  27.777  27.340 1.00 39.35  ? 1149 ASN D O     1 
ATOM   8167  C  CB    . ASN B  1  350 ? -6.217  26.983  30.563 1.00 39.30  ? 1149 ASN D CB    1 
ATOM   8168  C  CG    . ASN B  1  350 ? -4.971  26.809  29.750 1.00 36.03  ? 1149 ASN D CG    1 
ATOM   8169  O  OD1   . ASN B  1  350 ? -5.006  26.223  28.664 1.00 34.62  ? 1149 ASN D OD1   1 
ATOM   8170  N  ND2   . ASN B  1  350 ? -3.864  27.332  30.253 1.00 32.12  ? 1149 ASN D ND2   1 
ATOM   8171  N  N     . TYR B  1  351 ? -6.646  29.387  28.720 1.00 40.80  ? 1150 TYR D N     1 
ATOM   8172  C  CA    . TYR B  1  351 ? -6.382  30.377  27.666 1.00 36.91  ? 1150 TYR D CA    1 
ATOM   8173  C  C     . TYR B  1  351 ? -5.479  29.916  26.507 1.00 41.34  ? 1150 TYR D C     1 
ATOM   8174  O  O     . TYR B  1  351 ? -5.706  30.315  25.378 1.00 42.23  ? 1150 TYR D O     1 
ATOM   8175  C  CB    . TYR B  1  351 ? -5.830  31.680  28.268 1.00 35.78  ? 1150 TYR D CB    1 
ATOM   8176  C  CG    . TYR B  1  351 ? -4.411  31.595  28.826 1.00 35.39  ? 1150 TYR D CG    1 
ATOM   8177  C  CD1   . TYR B  1  351 ? -3.300  31.851  27.994 1.00 36.20  ? 1150 TYR D CD1   1 
ATOM   8178  C  CD2   . TYR B  1  351 ? -4.181  31.282  30.165 1.00 33.18  ? 1150 TYR D CD2   1 
ATOM   8179  C  CE1   . TYR B  1  351 ? -2.013  31.786  28.492 1.00 33.94  ? 1150 TYR D CE1   1 
ATOM   8180  C  CE2   . TYR B  1  351 ? -2.901  31.224  30.671 1.00 32.66  ? 1150 TYR D CE2   1 
ATOM   8181  C  CZ    . TYR B  1  351 ? -1.834  31.476  29.838 1.00 35.29  ? 1150 TYR D CZ    1 
ATOM   8182  O  OH    . TYR B  1  351 ? -0.585  31.432  30.373 1.00 37.77  ? 1150 TYR D OH    1 
ATOM   8183  N  N     . ASP B  1  352 ? -4.435  29.133  26.788 1.00 43.84  ? 1151 ASP D N     1 
ATOM   8184  C  CA    . ASP B  1  352 ? -3.522  28.678  25.722 1.00 40.61  ? 1151 ASP D CA    1 
ATOM   8185  C  C     . ASP B  1  352 ? -3.729  27.209  25.363 1.00 43.75  ? 1151 ASP D C     1 
ATOM   8186  O  O     . ASP B  1  352 ? -3.001  26.648  24.523 1.00 44.18  ? 1151 ASP D O     1 
ATOM   8187  C  CB    . ASP B  1  352 ? -2.045  28.899  26.139 1.00 39.09  ? 1151 ASP D CB    1 
ATOM   8188  C  CG    . ASP B  1  352 ? -1.690  28.142  27.381 1.00 39.79  ? 1151 ASP D CG    1 
ATOM   8189  O  OD1   . ASP B  1  352 ? -2.550  27.474  27.948 1.00 45.60  ? 1151 ASP D OD1   1 
ATOM   8190  O  OD2   . ASP B  1  352 ? -0.550  28.214  27.787 1.00 41.54  ? 1151 ASP D OD2   1 
ATOM   8191  N  N     . GLY B  1  353 ? -4.686  26.556  26.003 1.00 45.65  ? 1152 GLY D N     1 
ATOM   8192  C  CA    . GLY B  1  353 ? -4.948  25.137  25.652 1.00 40.71  ? 1152 GLY D CA    1 
ATOM   8193  C  C     . GLY B  1  353 ? -4.037  24.116  26.335 1.00 42.03  ? 1152 GLY D C     1 
ATOM   8194  O  O     . GLY B  1  353 ? -4.219  22.934  26.135 1.00 44.23  ? 1152 GLY D O     1 
ATOM   8195  N  N     . ASN B  1  354 ? -3.106  24.563  27.164 1.00 41.65  ? 1153 ASN D N     1 
ATOM   8196  C  CA    . ASN B  1  354 ? -2.218  23.653  27.891 1.00 41.38  ? 1153 ASN D CA    1 
ATOM   8197  C  C     . ASN B  1  354 ? -2.742  23.212  29.227 1.00 41.19  ? 1153 ASN D C     1 
ATOM   8198  O  O     . ASN B  1  354 ? -2.111  22.401  29.887 1.00 39.13  ? 1153 ASN D O     1 
ATOM   8199  C  CB    . ASN B  1  354 ? -0.842  24.285  28.113 1.00 43.50  ? 1153 ASN D CB    1 
ATOM   8200  C  CG    . ASN B  1  354 ? -0.131  24.571  26.819 1.00 49.64  ? 1153 ASN D CG    1 
ATOM   8201  O  OD1   . ASN B  1  354 ? -0.229  23.795  25.867 1.00 52.45  ? 1153 ASN D OD1   1 
ATOM   8202  N  ND2   . ASN B  1  354 ? 0.569   25.702  26.765 1.00 49.88  ? 1153 ASN D ND2   1 
ATOM   8203  N  N     . GLU B  1  355 ? -3.867  23.773  29.652 1.00 37.43  ? 1154 GLU D N     1 
ATOM   8204  C  CA    . GLU B  1  355 ? -4.431  23.398  30.953 1.00 36.95  ? 1154 GLU D CA    1 
ATOM   8205  C  C     . GLU B  1  355 ? -5.949  23.303  30.861 1.00 39.18  ? 1154 GLU D C     1 
ATOM   8206  O  O     . GLU B  1  355 ? -6.585  23.712  29.844 1.00 35.75  ? 1154 GLU D O     1 
ATOM   8207  C  CB    . GLU B  1  355 ? -4.041  24.399  32.046 1.00 34.66  ? 1154 GLU D CB    1 
ATOM   8208  C  CG    . GLU B  1  355 ? -2.565  24.743  32.145 1.00 36.37  ? 1154 GLU D CG    1 
ATOM   8209  C  CD    . GLU B  1  355 ? -1.731  23.663  32.789 1.00 41.49  ? 1154 GLU D CD    1 
ATOM   8210  O  OE1   . GLU B  1  355 ? -2.299  22.769  33.425 1.00 42.70  ? 1154 GLU D OE1   1 
ATOM   8211  O  OE2   . GLU B  1  355 ? -0.486  23.707  32.694 1.00 41.91  ? 1154 GLU D OE2   1 
ATOM   8212  N  N     . ARG B  1  356 ? -6.530  22.819  31.954 1.00 34.61  ? 1155 ARG D N     1 
ATOM   8213  C  CA    . ARG B  1  356 ? -7.958  22.757  32.116 1.00 36.36  ? 1155 ARG D CA    1 
ATOM   8214  C  C     . ARG B  1  356 ? -8.304  23.537  33.372 1.00 36.13  ? 1155 ARG D C     1 
ATOM   8215  O  O     . ARG B  1  356 ? -7.640  23.397  34.440 1.00 35.29  ? 1155 ARG D O     1 
ATOM   8216  C  CB    . ARG B  1  356 ? -8.392  21.289  32.244 1.00 39.30  ? 1155 ARG D CB    1 
ATOM   8217  C  CG    . ARG B  1  356 ? -8.171  20.451  30.985 1.00 41.32  ? 1155 ARG D CG    1 
ATOM   8218  C  CD    . ARG B  1  356 ? -9.230  20.710  29.914 1.00 45.02  ? 1155 ARG D CD    1 
ATOM   8219  N  NE    . ARG B  1  356 ? -10.460 19.988  30.212 1.00 44.27  ? 1155 ARG D NE    1 
ATOM   8220  C  CZ    . ARG B  1  356 ? -11.585 20.084  29.497 1.00 41.59  ? 1155 ARG D CZ    1 
ATOM   8221  N  NH1   . ARG B  1  356 ? -11.624 20.862  28.420 1.00 38.37  ? 1155 ARG D NH1   1 
ATOM   8222  N  NH2   . ARG B  1  356 ? -12.654 19.372  29.850 1.00 38.66  ? 1155 ARG D NH2   1 
ATOM   8223  N  N     . GLU B  1  357 ? -9.363  24.333  33.284 1.00 32.51  ? 1156 GLU D N     1 
ATOM   8224  C  CA    . GLU B  1  357 ? -9.806  25.115  34.446 1.00 33.30  ? 1156 GLU D CA    1 
ATOM   8225  C  C     . GLU B  1  357 ? -11.324 24.946  34.592 1.00 35.41  ? 1156 GLU D C     1 
ATOM   8226  O  O     . GLU B  1  357 ? -12.035 24.733  33.585 1.00 37.60  ? 1156 GLU D O     1 
ATOM   8227  C  CB    . GLU B  1  357 ? -9.446  26.597  34.255 1.00 28.61  ? 1156 GLU D CB    1 
ATOM   8228  C  CG    . GLU B  1  357 ? -10.174 27.239  33.071 1.00 32.89  ? 1156 GLU D CG    1 
ATOM   8229  C  CD    . GLU B  1  357 ? -10.015 28.767  33.059 1.00 33.69  ? 1156 GLU D CD    1 
ATOM   8230  O  OE1   . GLU B  1  357 ? -10.012 29.343  31.964 1.00 29.16  ? 1156 GLU D OE1   1 
ATOM   8231  O  OE2   . GLU B  1  357 ? -9.915  29.390  34.147 1.00 30.48  ? 1156 GLU D OE2   1 
ATOM   8232  N  N     . PRO B  1  358 ? -11.840 25.091  35.823 1.00 32.15  ? 1157 PRO D N     1 
ATOM   8233  C  CA    . PRO B  1  358 ? -13.267 24.979  36.059 1.00 32.02  ? 1157 PRO D CA    1 
ATOM   8234  C  C     . PRO B  1  358 ? -14.059 26.169  35.509 1.00 35.27  ? 1157 PRO D C     1 
ATOM   8235  O  O     . PRO B  1  358 ? -13.646 27.317  35.636 1.00 32.36  ? 1157 PRO D O     1 
ATOM   8236  C  CB    . PRO B  1  358 ? -13.361 24.931  37.577 1.00 36.49  ? 1157 PRO D CB    1 
ATOM   8237  C  CG    . PRO B  1  358 ? -12.141 25.659  38.070 1.00 33.34  ? 1157 PRO D CG    1 
ATOM   8238  C  CD    . PRO B  1  358 ? -11.081 25.419  37.057 1.00 35.66  ? 1157 PRO D CD    1 
ATOM   8239  N  N     . SER B  1  359 ? -15.218 25.871  34.924 1.00 33.43  ? 1158 SER D N     1 
ATOM   8240  C  CA    . SER B  1  359 ? -16.128 26.906  34.425 1.00 33.69  ? 1158 SER D CA    1 
ATOM   8241  C  C     . SER B  1  359 ? -16.813 27.573  35.609 1.00 34.11  ? 1158 SER D C     1 
ATOM   8242  O  O     . SER B  1  359 ? -17.129 28.753  35.565 1.00 35.21  ? 1158 SER D O     1 
ATOM   8243  C  CB    . SER B  1  359 ? -17.176 26.352  33.453 1.00 30.57  ? 1158 SER D CB    1 
ATOM   8244  O  OG    . SER B  1  359 ? -17.913 25.297  34.067 1.00 31.74  ? 1158 SER D OG    1 
ATOM   8245  N  N     . VAL B  1  360 ? -17.038 26.796  36.663 1.00 32.18  ? 1159 VAL D N     1 
ATOM   8246  C  CA    . VAL B  1  360 ? -17.695 27.303  37.860 1.00 30.16  ? 1159 VAL D CA    1 
ATOM   8247  C  C     . VAL B  1  360 ? -17.288 26.358  39.010 1.00 32.17  ? 1159 VAL D C     1 
ATOM   8248  O  O     . VAL B  1  360 ? -16.969 25.200  38.772 1.00 34.79  ? 1159 VAL D O     1 
ATOM   8249  C  CB    . VAL B  1  360 ? -19.267 27.326  37.680 1.00 29.81  ? 1159 VAL D CB    1 
ATOM   8250  C  CG1   . VAL B  1  360 ? -19.834 25.915  37.493 1.00 27.98  ? 1159 VAL D CG1   1 
ATOM   8251  C  CG2   . VAL B  1  360 ? -19.952 27.990  38.871 1.00 27.87  ? 1159 VAL D CG2   1 
ATOM   8252  N  N     . LEU B  1  361 ? -17.353 26.844  40.237 1.00 30.35  ? 1160 LEU D N     1 
ATOM   8253  C  CA    . LEU B  1  361 ? -17.032 26.020  41.401 1.00 31.63  ? 1160 LEU D CA    1 
ATOM   8254  C  C     . LEU B  1  361 ? -18.278 25.325  41.964 1.00 33.85  ? 1160 LEU D C     1 
ATOM   8255  O  O     . LEU B  1  361 ? -19.378 25.840  41.758 1.00 36.38  ? 1160 LEU D O     1 
ATOM   8256  C  CB    . LEU B  1  361 ? -16.382 26.848  42.492 1.00 26.95  ? 1160 LEU D CB    1 
ATOM   8257  C  CG    . LEU B  1  361 ? -15.043 27.567  42.223 1.00 28.78  ? 1160 LEU D CG    1 
ATOM   8258  C  CD1   . LEU B  1  361 ? -14.410 27.935  43.537 1.00 26.99  ? 1160 LEU D CD1   1 
ATOM   8259  C  CD2   . LEU B  1  361 ? -14.105 26.733  41.400 1.00 24.10  ? 1160 LEU D CD2   1 
ATOM   8260  N  N     . PRO B  1  362 ? -18.114 24.171  42.661 1.00 33.02  ? 1161 PRO D N     1 
ATOM   8261  C  CA    . PRO B  1  362 ? -19.331 23.576  43.216 1.00 33.29  ? 1161 PRO D CA    1 
ATOM   8262  C  C     . PRO B  1  362 ? -20.100 24.462  44.183 1.00 36.62  ? 1161 PRO D C     1 
ATOM   8263  O  O     . PRO B  1  362 ? -21.323 24.358  44.235 1.00 33.54  ? 1161 PRO D O     1 
ATOM   8264  C  CB    . PRO B  1  362 ? -18.843 22.355  43.972 1.00 29.43  ? 1161 PRO D CB    1 
ATOM   8265  C  CG    . PRO B  1  362 ? -17.617 21.949  43.244 1.00 30.86  ? 1161 PRO D CG    1 
ATOM   8266  C  CD    . PRO B  1  362 ? -16.962 23.231  42.764 1.00 29.09  ? 1161 PRO D CD    1 
ATOM   8267  N  N     . ALA B  1  363 ? -19.411 25.306  44.934 1.00 33.89  ? 1162 ALA D N     1 
ATOM   8268  C  CA    . ALA B  1  363 ? -20.079 26.334  45.758 1.00 34.23  ? 1162 ALA D CA    1 
ATOM   8269  C  C     . ALA B  1  363 ? -21.151 25.833  46.711 1.00 32.90  ? 1162 ALA D C     1 
ATOM   8270  O  O     . ALA B  1  363 ? -22.298 26.213  46.618 1.00 35.96  ? 1162 ALA D O     1 
ATOM   8271  C  CB    . ALA B  1  363 ? -20.653 27.418  44.849 1.00 25.98  ? 1162 ALA D CB    1 
ATOM   8272  N  N     . ARG B  1  364 ? -20.740 25.015  47.654 1.00 36.05  ? 1163 ARG D N     1 
ATOM   8273  C  CA    . ARG B  1  364 ? -21.652 24.350  48.580 1.00 34.76  ? 1163 ARG D CA    1 
ATOM   8274  C  C     . ARG B  1  364 ? -22.316 25.322  49.548 1.00 39.67  ? 1163 ARG D C     1 
ATOM   8275  O  O     . ARG B  1  364 ? -23.277 24.956  50.227 1.00 35.12  ? 1163 ARG D O     1 
ATOM   8276  C  CB    . ARG B  1  364 ? -20.925 23.193  49.303 1.00 33.68  ? 1163 ARG D CB    1 
ATOM   8277  C  CG    . ARG B  1  364 ? -20.270 22.185  48.367 1.00 27.28  ? 1163 ARG D CG    1 
ATOM   8278  C  CD    . ARG B  1  364 ? -21.144 21.759  47.178 1.00 31.23  ? 1163 ARG D CD    1 
ATOM   8279  N  NE    . ARG B  1  364 ? -22.476 21.366  47.611 1.00 38.79  ? 1163 ARG D NE    1 
ATOM   8280  C  CZ    . ARG B  1  364 ? -22.735 20.238  48.267 1.00 35.40  ? 1163 ARG D CZ    1 
ATOM   8281  N  NH1   . ARG B  1  364 ? -21.772 19.351  48.476 1.00 30.92  ? 1163 ARG D NH1   1 
ATOM   8282  N  NH2   . ARG B  1  364 ? -23.954 20.025  48.727 1.00 36.88  ? 1163 ARG D NH2   1 
ATOM   8283  N  N     . PHE B  1  365 ? -21.862 26.581  49.569 1.00 40.97  ? 1164 PHE D N     1 
ATOM   8284  C  CA    . PHE B  1  365 ? -22.614 27.639  50.273 1.00 32.92  ? 1164 PHE D CA    1 
ATOM   8285  C  C     . PHE B  1  365 ? -22.961 28.754  49.274 1.00 33.61  ? 1164 PHE D C     1 
ATOM   8286  O  O     . PHE B  1  365 ? -22.319 28.884  48.222 1.00 33.77  ? 1164 PHE D O     1 
ATOM   8287  C  CB    . PHE B  1  365 ? -21.883 28.132  51.523 1.00 31.90  ? 1164 PHE D CB    1 
ATOM   8288  C  CG    . PHE B  1  365 ? -20.691 28.985  51.250 1.00 31.93  ? 1164 PHE D CG    1 
ATOM   8289  C  CD1   . PHE B  1  365 ? -19.449 28.410  51.004 1.00 30.27  ? 1164 PHE D CD1   1 
ATOM   8290  C  CD2   . PHE B  1  365 ? -20.821 30.381  51.213 1.00 30.99  ? 1164 PHE D CD2   1 
ATOM   8291  C  CE1   . PHE B  1  365 ? -18.348 29.217  50.764 1.00 33.93  ? 1164 PHE D CE1   1 
ATOM   8292  C  CE2   . PHE B  1  365 ? -19.736 31.183  50.952 1.00 33.32  ? 1164 PHE D CE2   1 
ATOM   8293  C  CZ    . PHE B  1  365 ? -18.490 30.608  50.700 1.00 33.76  ? 1164 PHE D CZ    1 
ATOM   8294  N  N     . PRO B  1  366 ? -24.035 29.531  49.553 1.00 35.06  ? 1165 PRO D N     1 
ATOM   8295  C  CA    . PRO B  1  366 ? -24.466 30.534  48.563 1.00 32.75  ? 1165 PRO D CA    1 
ATOM   8296  C  C     . PRO B  1  366 ? -23.580 31.776  48.588 1.00 33.17  ? 1165 PRO D C     1 
ATOM   8297  O  O     . PRO B  1  366 ? -23.966 32.799  49.137 1.00 30.56  ? 1165 PRO D O     1 
ATOM   8298  C  CB    . PRO B  1  366 ? -25.903 30.876  48.978 1.00 29.48  ? 1165 PRO D CB    1 
ATOM   8299  C  CG    . PRO B  1  366 ? -26.010 30.464  50.398 1.00 29.85  ? 1165 PRO D CG    1 
ATOM   8300  C  CD    . PRO B  1  366 ? -25.119 29.254  50.520 1.00 33.34  ? 1165 PRO D CD    1 
ATOM   8301  N  N     . ASN B  1  367 ? -22.404 31.652  47.970 1.00 29.85  ? 1166 ASN D N     1 
ATOM   8302  C  CA    . ASN B  1  367 ? -21.374 32.654  48.007 1.00 26.96  ? 1166 ASN D CA    1 
ATOM   8303  C  C     . ASN B  1  367 ? -21.690 34.050  47.404 1.00 26.65  ? 1166 ASN D C     1 
ATOM   8304  O  O     . ASN B  1  367 ? -21.261 35.060  47.956 1.00 30.67  ? 1166 ASN D O     1 
ATOM   8305  C  CB    . ASN B  1  367 ? -20.127 32.109  47.394 1.00 25.38  ? 1166 ASN D CB    1 
ATOM   8306  C  CG    . ASN B  1  367 ? -18.929 33.049  47.581 1.00 25.60  ? 1166 ASN D CG    1 
ATOM   8307  O  OD1   . ASN B  1  367 ? -18.647 33.500  48.662 1.00 28.13  ? 1166 ASN D OD1   1 
ATOM   8308  N  ND2   . ASN B  1  367 ? -18.223 33.305  46.509 1.00 25.76  ? 1166 ASN D ND2   1 
ATOM   8309  N  N     . LEU B  1  368 ? -22.406 34.094  46.302 1.00 26.62  ? 1167 LEU D N     1 
ATOM   8310  C  CA    . LEU B  1  368 ? -22.756 35.355  45.709 1.00 33.44  ? 1167 LEU D CA    1 
ATOM   8311  C  C     . LEU B  1  368 ? -23.455 36.332  46.673 1.00 34.58  ? 1167 LEU D C     1 
ATOM   8312  O  O     . LEU B  1  368 ? -23.048 37.493  46.847 1.00 35.31  ? 1167 LEU D O     1 
ATOM   8313  C  CB    . LEU B  1  368 ? -23.634 35.125  44.466 1.00 32.08  ? 1167 LEU D CB    1 
ATOM   8314  C  CG    . LEU B  1  368 ? -23.977 36.496  43.799 1.00 30.80  ? 1167 LEU D CG    1 
ATOM   8315  C  CD1   . LEU B  1  368 ? -22.858 37.066  42.947 1.00 28.18  ? 1167 LEU D CD1   1 
ATOM   8316  C  CD2   . LEU B  1  368 ? -25.275 36.434  43.022 1.00 26.14  ? 1167 LEU D CD2   1 
ATOM   8317  N  N     . LEU B  1  369 ? -24.526 35.842  47.282 1.00 32.04  ? 1168 LEU D N     1 
ATOM   8318  C  CA    . LEU B  1  369 ? -25.221 36.619  48.281 1.00 30.00  ? 1168 LEU D CA    1 
ATOM   8319  C  C     . LEU B  1  369 ? -24.422 36.768  49.576 1.00 30.19  ? 1168 LEU D C     1 
ATOM   8320  O  O     . LEU B  1  369 ? -24.415 37.875  50.181 1.00 32.04  ? 1168 LEU D O     1 
ATOM   8321  C  CB    . LEU B  1  369 ? -26.630 36.095  48.525 1.00 26.61  ? 1168 LEU D CB    1 
ATOM   8322  C  CG    . LEU B  1  369 ? -27.557 36.221  47.337 1.00 30.99  ? 1168 LEU D CG    1 
ATOM   8323  C  CD1   . LEU B  1  369 ? -28.835 35.384  47.555 1.00 31.39  ? 1168 LEU D CD1   1 
ATOM   8324  C  CD2   . LEU B  1  369 ? -27.866 37.717  47.074 1.00 32.91  ? 1168 LEU D CD2   1 
ATOM   8325  N  N     . ALA B  1  370 ? -23.699 35.712  49.977 1.00 26.04  ? 1169 ALA D N     1 
ATOM   8326  C  CA    . ALA B  1  370 ? -22.978 35.772  51.234 1.00 27.16  ? 1169 ALA D CA    1 
ATOM   8327  C  C     . ALA B  1  370 ? -21.855 36.823  51.243 1.00 27.54  ? 1169 ALA D C     1 
ATOM   8328  O  O     . ALA B  1  370 ? -21.698 37.544  52.223 1.00 29.02  ? 1169 ALA D O     1 
ATOM   8329  C  CB    . ALA B  1  370 ? -22.426 34.399  51.572 1.00 27.49  ? 1169 ALA D CB    1 
ATOM   8330  N  N     . ASN B  1  371 ? -21.046 36.849  50.183 1.00 26.81  ? 1170 ASN D N     1 
ATOM   8331  C  CA    . ASN B  1  371 ? -19.951 37.809  50.118 1.00 26.07  ? 1170 ASN D CA    1 
ATOM   8332  C  C     . ASN B  1  371 ? -20.241 39.040  49.274 1.00 27.05  ? 1170 ASN D C     1 
ATOM   8333  O  O     . ASN B  1  371 ? -19.525 40.040  49.353 1.00 24.85  ? 1170 ASN D O     1 
ATOM   8334  C  CB    . ASN B  1  371 ? -18.656 37.155  49.684 1.00 22.87  ? 1170 ASN D CB    1 
ATOM   8335  C  CG    . ASN B  1  371 ? -17.959 36.421  50.820 1.00 28.83  ? 1170 ASN D CG    1 
ATOM   8336  O  OD1   . ASN B  1  371 ? -17.725 36.982  51.884 1.00 26.22  ? 1170 ASN D OD1   1 
ATOM   8337  N  ND2   . ASN B  1  371 ? -17.666 35.102  50.621 1.00 25.67  ? 1170 ASN D ND2   1 
ATOM   8338  N  N     . GLY B  1  372 ? -21.301 38.979  48.463 1.00 32.60  ? 1171 GLY D N     1 
ATOM   8339  C  CA    . GLY B  1  372 ? -21.656 40.111  47.617 1.00 32.53  ? 1171 GLY D CA    1 
ATOM   8340  C  C     . GLY B  1  372 ? -20.704 40.280  46.452 1.00 34.47  ? 1171 GLY D C     1 
ATOM   8341  O  O     . GLY B  1  372 ? -19.818 39.442  46.258 1.00 32.12  ? 1171 GLY D O     1 
ATOM   8342  N  N     . ALA B  1  373 ? -20.835 41.382  45.724 1.00 34.45  ? 1172 ALA D N     1 
ATOM   8343  C  CA    . ALA B  1  373 ? -19.968 41.660  44.587 1.00 30.74  ? 1172 ALA D CA    1 
ATOM   8344  C  C     . ALA B  1  373 ? -20.113 43.127  44.205 1.00 31.48  ? 1172 ALA D C     1 
ATOM   8345  O  O     . ALA B  1  373 ? -21.196 43.722  44.296 1.00 32.85  ? 1172 ALA D O     1 
ATOM   8346  C  CB    . ALA B  1  373 ? -20.378 40.804  43.392 1.00 29.12  ? 1172 ALA D CB    1 
ATOM   8347  N  N     . SER B  1  374 ? -19.020 43.683  43.686 1.00 27.55  ? 1173 SER D N     1 
ATOM   8348  C  CA    . SER B  1  374 ? -19.020 44.975  43.069 1.00 32.98  ? 1173 SER D CA    1 
ATOM   8349  C  C     . SER B  1  374 ? -18.122 44.880  41.812 1.00 33.99  ? 1173 SER D C     1 
ATOM   8350  O  O     . SER B  1  374 ? -16.969 44.536  41.920 1.00 35.66  ? 1173 SER D O     1 
ATOM   8351  C  CB    . SER B  1  374 ? -18.552 46.053  44.067 1.00 32.48  ? 1173 SER D CB    1 
ATOM   8352  O  OG    . SER B  1  374 ? -17.179 46.211  44.005 1.00 36.88  ? 1173 SER D OG    1 
ATOM   8353  N  N     . GLY B  1  375 ? -18.649 45.211  40.644 1.00 33.41  ? 1174 GLY D N     1 
ATOM   8354  C  CA    . GLY B  1  375 ? -17.796 45.247  39.471 1.00 30.31  ? 1174 GLY D CA    1 
ATOM   8355  C  C     . GLY B  1  375 ? -18.256 46.288  38.467 1.00 31.14  ? 1174 GLY D C     1 
ATOM   8356  O  O     . GLY B  1  375 ? -19.449 46.455  38.239 1.00 38.61  ? 1174 GLY D O     1 
ATOM   8357  N  N     . ILE B  1  376 ? -17.322 46.976  37.832 1.00 31.64  ? 1175 ILE D N     1 
ATOM   8358  C  CA    . ILE B  1  376 ? -17.633 47.951  36.794 1.00 30.31  ? 1175 ILE D CA    1 
ATOM   8359  C  C     . ILE B  1  376 ? -17.358 47.279  35.449 1.00 29.29  ? 1175 ILE D C     1 
ATOM   8360  O  O     . ILE B  1  376 ? -16.199 46.919  35.117 1.00 26.77  ? 1175 ILE D O     1 
ATOM   8361  C  CB    . ILE B  1  376 ? -16.764 49.217  36.938 1.00 32.60  ? 1175 ILE D CB    1 
ATOM   8362  C  CG1   . ILE B  1  376 ? -16.980 49.851  38.308 1.00 29.66  ? 1175 ILE D CG1   1 
ATOM   8363  C  CG2   . ILE B  1  376 ? -17.077 50.222  35.821 1.00 31.50  ? 1175 ILE D CG2   1 
ATOM   8364  C  CD1   . ILE B  1  376 ? -15.787 50.726  38.757 1.00 28.34  ? 1175 ILE D CD1   1 
ATOM   8365  N  N     . ALA B  1  377 ? -18.410 47.078  34.676 1.00 28.89  ? 1176 ALA D N     1 
ATOM   8366  C  CA    . ALA B  1  377 ? -18.274 46.383  33.401 1.00 30.15  ? 1176 ALA D CA    1 
ATOM   8367  C  C     . ALA B  1  377 ? -18.273 47.378  32.272 1.00 28.66  ? 1176 ALA D C     1 
ATOM   8368  O  O     . ALA B  1  377 ? -17.687 48.448  32.371 1.00 37.49  ? 1176 ALA D O     1 
ATOM   8369  C  CB    . ALA B  1  377 ? -19.374 45.344  33.243 1.00 26.18  ? 1176 ALA D CB    1 
ATOM   8370  N  N     . VAL B  1  378 ? -18.898 47.035  31.172 1.00 30.68  ? 1177 VAL D N     1 
ATOM   8371  C  CA    . VAL B  1  378 ? -19.095 47.980  30.095 1.00 31.43  ? 1177 VAL D CA    1 
ATOM   8372  C  C     . VAL B  1  378 ? -20.598 47.962  29.817 1.00 37.73  ? 1177 VAL D C     1 
ATOM   8373  O  O     . VAL B  1  378 ? -21.185 46.886  29.572 1.00 37.24  ? 1177 VAL D O     1 
ATOM   8374  C  CB    . VAL B  1  378 ? -18.332 47.572  28.830 1.00 32.40  ? 1177 VAL D CB    1 
ATOM   8375  C  CG1   . VAL B  1  378 ? -18.669 48.513  27.669 1.00 30.89  ? 1177 VAL D CG1   1 
ATOM   8376  C  CG2   . VAL B  1  378 ? -16.831 47.532  29.070 1.00 27.23  ? 1177 VAL D CG2   1 
ATOM   8377  N  N     . GLY B  1  379 ? -21.235 49.128  29.890 1.00 33.68  ? 1178 GLY D N     1 
ATOM   8378  C  CA    . GLY B  1  379 ? -22.658 49.178  29.568 1.00 30.65  ? 1178 GLY D CA    1 
ATOM   8379  C  C     . GLY B  1  379 ? -23.470 48.912  30.822 1.00 32.68  ? 1178 GLY D C     1 
ATOM   8380  O  O     . GLY B  1  379 ? -24.709 49.095  30.862 1.00 33.75  ? 1178 GLY D O     1 
ATOM   8381  N  N     . MET B  1  380 ? -22.779 48.433  31.856 1.00 33.07  ? 1179 MET D N     1 
ATOM   8382  C  CA    . MET B  1  380 ? -23.445 48.026  33.095 1.00 31.52  ? 1179 MET D CA    1 
ATOM   8383  C  C     . MET B  1  380 ? -22.436 47.796  34.189 1.00 32.80  ? 1179 MET D C     1 
ATOM   8384  O  O     . MET B  1  380 ? -21.211 47.705  33.929 1.00 34.31  ? 1179 MET D O     1 
ATOM   8385  C  CB    . MET B  1  380 ? -24.248 46.725  32.919 1.00 32.29  ? 1179 MET D CB    1 
ATOM   8386  C  CG    . MET B  1  380 ? -23.388 45.526  32.478 1.00 33.26  ? 1179 MET D CG    1 
ATOM   8387  S  SD    . MET B  1  380 ? -24.473 44.149  32.188 1.00 35.87  ? 1179 MET D SD    1 
ATOM   8388  C  CE    . MET B  1  380 ? -25.760 44.866  31.146 1.00 40.26  ? 1179 MET D CE    1 
ATOM   8389  N  N     . ALA B  1  381 ? -22.954 47.691  35.411 1.00 28.76  ? 1180 ALA D N     1 
ATOM   8390  C  CA    . ALA B  1  381 ? -22.105 47.496  36.579 1.00 31.69  ? 1180 ALA D CA    1 
ATOM   8391  C  C     . ALA B  1  381 ? -22.887 46.629  37.555 1.00 31.69  ? 1180 ALA D C     1 
ATOM   8392  O  O     . ALA B  1  381 ? -24.065 46.406  37.364 1.00 37.86  ? 1180 ALA D O     1 
ATOM   8393  C  CB    . ALA B  1  381 ? -21.717 48.826  37.192 1.00 29.19  ? 1180 ALA D CB    1 
ATOM   8394  N  N     . THR B  1  382 ? -22.262 46.170  38.624 1.00 29.38  ? 1181 THR D N     1 
ATOM   8395  C  CA    . THR B  1  382 ? -22.986 45.350  39.593 1.00 27.82  ? 1181 THR D CA    1 
ATOM   8396  C  C     . THR B  1  382 ? -22.620 45.806  40.981 1.00 26.60  ? 1181 THR D C     1 
ATOM   8397  O  O     . THR B  1  382 ? -21.435 46.101  41.258 1.00 27.12  ? 1181 THR D O     1 
ATOM   8398  C  CB    . THR B  1  382 ? -22.672 43.830  39.463 1.00 30.23  ? 1181 THR D CB    1 
ATOM   8399  O  OG1   . THR B  1  382 ? -23.620 43.111  40.246 1.00 30.03  ? 1181 THR D OG1   1 
ATOM   8400  C  CG2   . THR B  1  382 ? -21.224 43.472  39.983 1.00 24.70  ? 1181 THR D CG2   1 
ATOM   8401  N  N     . ASN B  1  383 ? -23.632 45.851  41.848 1.00 27.77  ? 1182 ASN D N     1 
ATOM   8402  C  CA    . ASN B  1  383 ? -23.368 46.080  43.268 1.00 30.82  ? 1182 ASN D CA    1 
ATOM   8403  C  C     . ASN B  1  383 ? -24.278 45.172  44.065 1.00 29.78  ? 1182 ASN D C     1 
ATOM   8404  O  O     . ASN B  1  383 ? -25.518 45.380  44.140 1.00 28.60  ? 1182 ASN D O     1 
ATOM   8405  C  CB    . ASN B  1  383 ? -23.663 47.542  43.614 1.00 29.34  ? 1182 ASN D CB    1 
ATOM   8406  C  CG    . ASN B  1  383 ? -22.730 48.059  44.671 1.00 30.87  ? 1182 ASN D CG    1 
ATOM   8407  O  OD1   . ASN B  1  383 ? -21.654 47.496  44.928 1.00 34.87  ? 1182 ASN D OD1   1 
ATOM   8408  N  ND2   . ASN B  1  383 ? -23.123 49.137  45.295 1.00 29.78  ? 1182 ASN D ND2   1 
ATOM   8409  N  N     . ILE B  1  384 ? -23.695 44.153  44.683 1.00 29.45  ? 1183 ILE D N     1 
ATOM   8410  C  CA    . ILE B  1  384 ? -24.478 43.223  45.499 1.00 28.83  ? 1183 ILE D CA    1 
ATOM   8411  C  C     . ILE B  1  384 ? -23.918 43.245  46.915 1.00 30.23  ? 1183 ILE D C     1 
ATOM   8412  O  O     . ILE B  1  384 ? -22.726 43.016  47.092 1.00 34.77  ? 1183 ILE D O     1 
ATOM   8413  C  CB    . ILE B  1  384 ? -24.434 41.800  44.916 1.00 30.73  ? 1183 ILE D CB    1 
ATOM   8414  C  CG1   . ILE B  1  384 ? -25.102 41.799  43.547 1.00 32.13  ? 1183 ILE D CG1   1 
ATOM   8415  C  CG2   . ILE B  1  384 ? -25.195 40.828  45.800 1.00 27.42  ? 1183 ILE D CG2   1 
ATOM   8416  C  CD1   . ILE B  1  384 ? -24.797 40.552  42.699 1.00 30.87  ? 1183 ILE D CD1   1 
ATOM   8417  N  N     . PRO B  1  385 ? -24.741 43.544  47.909 1.00 28.03  ? 1184 PRO D N     1 
ATOM   8418  C  CA    . PRO B  1  385 ? -24.254 43.597  49.299 1.00 29.41  ? 1184 PRO D CA    1 
ATOM   8419  C  C     . PRO B  1  385 ? -24.092 42.159  49.854 1.00 30.87  ? 1184 PRO D C     1 
ATOM   8420  O  O     . PRO B  1  385 ? -24.786 41.240  49.418 1.00 28.99  ? 1184 PRO D O     1 
ATOM   8421  C  CB    . PRO B  1  385 ? -25.390 44.295  50.052 1.00 27.72  ? 1184 PRO D CB    1 
ATOM   8422  C  CG    . PRO B  1  385 ? -26.620 43.946  49.223 1.00 28.19  ? 1184 PRO D CG    1 
ATOM   8423  C  CD    . PRO B  1  385 ? -26.159 43.883  47.793 1.00 29.17  ? 1184 PRO D CD    1 
ATOM   8424  N  N     . PRO B  1  386 ? -23.201 41.990  50.830 1.00 30.65  ? 1185 PRO D N     1 
ATOM   8425  C  CA    . PRO B  1  386 ? -23.074 40.685  51.499 1.00 33.12  ? 1185 PRO D CA    1 
ATOM   8426  C  C     . PRO B  1  386 ? -24.257 40.395  52.447 1.00 31.60  ? 1185 PRO D C     1 
ATOM   8427  O  O     . PRO B  1  386 ? -25.039 41.295  52.755 1.00 30.07  ? 1185 PRO D O     1 
ATOM   8428  C  CB    . PRO B  1  386 ? -21.820 40.861  52.358 1.00 31.23  ? 1185 PRO D CB    1 
ATOM   8429  C  CG    . PRO B  1  386 ? -21.801 42.323  52.660 1.00 30.75  ? 1185 PRO D CG    1 
ATOM   8430  C  CD    . PRO B  1  386 ? -22.296 43.001  51.425 1.00 27.82  ? 1185 PRO D CD    1 
ATOM   8431  N  N     . HIS B  1  387 ? -24.373 39.141  52.874 1.00 26.63  ? 1186 HIS D N     1 
ATOM   8432  C  CA    . HIS B  1  387 ? -25.492 38.665  53.674 1.00 25.37  ? 1186 HIS D CA    1 
ATOM   8433  C  C     . HIS B  1  387 ? -25.047 37.684  54.740 1.00 28.62  ? 1186 HIS D C     1 
ATOM   8434  O  O     . HIS B  1  387 ? -23.898 37.150  54.710 1.00 27.47  ? 1186 HIS D O     1 
ATOM   8435  C  CB    . HIS B  1  387 ? -26.533 37.996  52.794 1.00 26.29  ? 1186 HIS D CB    1 
ATOM   8436  C  CG    . HIS B  1  387 ? -27.265 38.964  51.913 1.00 27.06  ? 1186 HIS D CG    1 
ATOM   8437  N  ND1   . HIS B  1  387 ? -26.727 39.454  50.740 1.00 25.38  ? 1186 HIS D ND1   1 
ATOM   8438  C  CD2   . HIS B  1  387 ? -28.481 39.551  52.050 1.00 26.94  ? 1186 HIS D CD2   1 
ATOM   8439  C  CE1   . HIS B  1  387 ? -27.571 40.315  50.204 1.00 29.11  ? 1186 HIS D CE1   1 
ATOM   8440  N  NE2   . HIS B  1  387 ? -28.658 40.367  50.962 1.00 26.90  ? 1186 HIS D NE2   1 
ATOM   8441  N  N     . ASN B  1  388 ? -25.931 37.449  55.711 1.00 27.06  ? 1187 ASN D N     1 
ATOM   8442  C  CA    . ASN B  1  388 ? -25.615 36.564  56.815 1.00 29.60  ? 1187 ASN D CA    1 
ATOM   8443  C  C     . ASN B  1  388 ? -25.816 35.112  56.347 1.00 30.23  ? 1187 ASN D C     1 
ATOM   8444  O  O     . ASN B  1  388 ? -26.855 34.797  55.734 1.00 29.13  ? 1187 ASN D O     1 
ATOM   8445  C  CB    . ASN B  1  388 ? -26.480 36.879  58.046 1.00 31.10  ? 1187 ASN D CB    1 
ATOM   8446  C  CG    . ASN B  1  388 ? -26.239 35.910  59.164 1.00 35.44  ? 1187 ASN D CG    1 
ATOM   8447  O  OD1   . ASN B  1  388 ? -26.875 34.846  59.226 1.00 40.55  ? 1187 ASN D OD1   1 
ATOM   8448  N  ND2   . ASN B  1  388 ? -25.316 36.260  60.061 1.00 30.44  ? 1187 ASN D ND2   1 
ATOM   8449  N  N     . LEU B  1  389 ? -24.834 34.244  56.621 1.00 27.66  ? 1188 LEU D N     1 
ATOM   8450  C  CA    . LEU B  1  389 ? -24.844 32.933  56.045 1.00 25.76  ? 1188 LEU D CA    1 
ATOM   8451  C  C     . LEU B  1  389 ? -26.001 32.036  56.547 1.00 24.28  ? 1188 LEU D C     1 
ATOM   8452  O  O     . LEU B  1  389 ? -26.608 31.316  55.778 1.00 25.71  ? 1188 LEU D O     1 
ATOM   8453  C  CB    . LEU B  1  389 ? -23.497 32.260  56.283 1.00 26.92  ? 1188 LEU D CB    1 
ATOM   8454  C  CG    . LEU B  1  389 ? -23.376 30.847  55.677 1.00 27.63  ? 1188 LEU D CG    1 
ATOM   8455  C  CD1   . LEU B  1  389 ? -23.642 30.806  54.174 1.00 23.99  ? 1188 LEU D CD1   1 
ATOM   8456  C  CD2   . LEU B  1  389 ? -22.005 30.286  56.001 1.00 29.50  ? 1188 LEU D CD2   1 
ATOM   8457  N  N     . THR B  1  390 ? -26.257 32.090  57.862 1.00 28.66  ? 1189 THR D N     1 
ATOM   8458  C  CA    . THR B  1  390 ? -27.359 31.412  58.492 1.00 28.32  ? 1189 THR D CA    1 
ATOM   8459  C  C     . THR B  1  390 ? -28.694 31.791  57.861 1.00 32.15  ? 1189 THR D C     1 
ATOM   8460  O  O     . THR B  1  390 ? -29.509 30.901  57.528 1.00 32.68  ? 1189 THR D O     1 
ATOM   8461  C  CB    . THR B  1  390 ? -27.407 31.727  59.987 1.00 31.19  ? 1189 THR D CB    1 
ATOM   8462  O  OG1   . THR B  1  390 ? -26.098 31.515  60.568 1.00 31.93  ? 1189 THR D OG1   1 
ATOM   8463  C  CG2   . THR B  1  390 ? -28.444 30.793  60.663 1.00 28.25  ? 1189 THR D CG2   1 
ATOM   8464  N  N     . GLU B  1  391 ? -28.905 33.098  57.671 1.00 32.50  ? 1190 GLU D N     1 
ATOM   8465  C  CA    . GLU B  1  391 ? -30.146 33.622  57.081 1.00 31.37  ? 1190 GLU D CA    1 
ATOM   8466  C  C     . GLU B  1  391 ? -30.291 33.155  55.654 1.00 28.30  ? 1190 GLU D C     1 
ATOM   8467  O  O     . GLU B  1  391 ? -31.379 32.747  55.273 1.00 29.78  ? 1190 GLU D O     1 
ATOM   8468  C  CB    . GLU B  1  391 ? -30.198 35.168  57.163 1.00 28.39  ? 1190 GLU D CB    1 
ATOM   8469  C  CG    . GLU B  1  391 ? -30.159 35.741  58.567 1.00 26.24  ? 1190 GLU D CG    1 
ATOM   8470  C  CD    . GLU B  1  391 ? -30.303 37.288  58.600 1.00 32.31  ? 1190 GLU D CD    1 
ATOM   8471  O  OE1   . GLU B  1  391 ? -30.562 37.941  57.570 1.00 25.74  ? 1190 GLU D OE1   1 
ATOM   8472  O  OE2   . GLU B  1  391 ? -30.196 37.863  59.681 1.00 28.73  ? 1190 GLU D OE2   1 
ATOM   8473  N  N     . LEU B  1  392 ? -29.205 33.199  54.878 1.00 28.05  ? 1191 LEU D N     1 
ATOM   8474  C  CA    . LEU B  1  392 ? -29.251 32.777  53.459 1.00 29.15  ? 1191 LEU D CA    1 
ATOM   8475  C  C     . LEU B  1  392 ? -29.551 31.306  53.289 1.00 31.71  ? 1191 LEU D C     1 
ATOM   8476  O  O     . LEU B  1  392 ? -30.336 30.939  52.396 1.00 28.25  ? 1191 LEU D O     1 
ATOM   8477  C  CB    . LEU B  1  392 ? -27.947 33.065  52.783 1.00 28.93  ? 1191 LEU D CB    1 
ATOM   8478  C  CG    . LEU B  1  392 ? -27.615 34.494  52.404 1.00 31.24  ? 1191 LEU D CG    1 
ATOM   8479  C  CD1   . LEU B  1  392 ? -26.243 34.480  51.706 1.00 27.36  ? 1191 LEU D CD1   1 
ATOM   8480  C  CD2   . LEU B  1  392 ? -28.731 35.079  51.490 1.00 24.82  ? 1191 LEU D CD2   1 
ATOM   8481  N  N     . ILE B  1  393 ? -28.929 30.467  54.141 1.00 28.68  ? 1192 ILE D N     1 
ATOM   8482  C  CA    . ILE B  1  393 ? -29.151 29.039  54.031 1.00 28.50  ? 1192 ILE D CA    1 
ATOM   8483  C  C     . ILE B  1  393 ? -30.596 28.718  54.430 1.00 29.77  ? 1192 ILE D C     1 
ATOM   8484  O  O     . ILE B  1  393 ? -31.240 27.861  53.838 1.00 36.39  ? 1192 ILE D O     1 
ATOM   8485  C  CB    . ILE B  1  393 ? -28.126 28.243  54.831 1.00 26.05  ? 1192 ILE D CB    1 
ATOM   8486  C  CG1   . ILE B  1  393 ? -26.747 28.341  54.164 1.00 23.56  ? 1192 ILE D CG1   1 
ATOM   8487  C  CG2   . ILE B  1  393 ? -28.549 26.763  54.893 1.00 26.37  ? 1192 ILE D CG2   1 
ATOM   8488  C  CD1   . ILE B  1  393 ? -25.702 27.446  54.768 1.00 26.73  ? 1192 ILE D CD1   1 
ATOM   8489  N  N     . ASN B  1  394 ? -31.103 29.412  55.441 1.00 32.37  ? 1193 ASN D N     1 
ATOM   8490  C  CA    . ASN B  1  394 ? -32.464 29.199  55.902 1.00 32.27  ? 1193 ASN D CA    1 
ATOM   8491  C  C     . ASN B  1  394 ? -33.446 29.622  54.807 1.00 34.46  ? 1193 ASN D C     1 
ATOM   8492  O  O     . ASN B  1  394 ? -34.456 28.982  54.605 1.00 31.79  ? 1193 ASN D O     1 
ATOM   8493  C  CB    . ASN B  1  394 ? -32.756 29.973  57.159 1.00 27.64  ? 1193 ASN D CB    1 
ATOM   8494  C  CG    . ASN B  1  394 ? -32.237 29.295  58.396 1.00 30.88  ? 1193 ASN D CG    1 
ATOM   8495  O  OD1   . ASN B  1  394 ? -31.971 28.082  58.410 1.00 30.48  ? 1193 ASN D OD1   1 
ATOM   8496  N  ND2   . ASN B  1  394 ? -32.126 30.072  59.487 1.00 29.93  ? 1193 ASN D ND2   1 
ATOM   8497  N  N     . GLY B  1  395 ? -33.109 30.686  54.085 1.00 33.32  ? 1194 GLY D N     1 
ATOM   8498  C  CA    . GLY B  1  395 ? -33.849 31.098  52.924 1.00 28.72  ? 1194 GLY D CA    1 
ATOM   8499  C  C     . GLY B  1  395 ? -33.833 30.091  51.808 1.00 31.95  ? 1194 GLY D C     1 
ATOM   8500  O  O     . GLY B  1  395 ? -34.861 29.853  51.154 1.00 33.80  ? 1194 GLY D O     1 
ATOM   8501  N  N     . VAL B  1  396 ? -32.679 29.482  51.556 1.00 29.57  ? 1195 VAL D N     1 
ATOM   8502  C  CA    . VAL B  1  396 ? -32.597 28.448  50.547 1.00 25.80  ? 1195 VAL D CA    1 
ATOM   8503  C  C     . VAL B  1  396 ? -33.428 27.225  50.954 1.00 26.33  ? 1195 VAL D C     1 
ATOM   8504  O  O     . VAL B  1  396 ? -34.081 26.643  50.129 1.00 26.80  ? 1195 VAL D O     1 
ATOM   8505  C  CB    . VAL B  1  396 ? -31.129 28.020  50.295 1.00 27.27  ? 1195 VAL D CB    1 
ATOM   8506  C  CG1   . VAL B  1  396 ? -31.106 26.748  49.403 1.00 22.47  ? 1195 VAL D CG1   1 
ATOM   8507  C  CG2   . VAL B  1  396 ? -30.383 29.171  49.653 1.00 22.39  ? 1195 VAL D CG2   1 
ATOM   8508  N  N     . LEU B  1  397 ? -33.400 26.861  52.232 1.00 27.32  ? 1196 LEU D N     1 
ATOM   8509  C  CA    . LEU B  1  397 ? -34.195 25.756  52.747 1.00 31.24  ? 1196 LEU D CA    1 
ATOM   8510  C  C     . LEU B  1  397 ? -35.696 26.011  52.624 1.00 33.54  ? 1196 LEU D C     1 
ATOM   8511  O  O     . LEU B  1  397 ? -36.459 25.116  52.271 1.00 36.91  ? 1196 LEU D O     1 
ATOM   8512  C  CB    . LEU B  1  397 ? -33.827 25.425  54.195 1.00 31.19  ? 1196 LEU D CB    1 
ATOM   8513  C  CG    . LEU B  1  397 ? -32.373 24.942  54.395 1.00 32.03  ? 1196 LEU D CG    1 
ATOM   8514  C  CD1   . LEU B  1  397 ? -32.052 24.788  55.862 1.00 29.19  ? 1196 LEU D CD1   1 
ATOM   8515  C  CD2   . LEU B  1  397 ? -32.185 23.589  53.749 1.00 31.44  ? 1196 LEU D CD2   1 
ATOM   8516  N  N     . SER B  1  398 ? -36.122 27.238  52.891 1.00 29.96  ? 1197 SER D N     1 
ATOM   8517  C  CA    . SER B  1  398 ? -37.544 27.619  52.753 1.00 28.76  ? 1197 SER D CA    1 
ATOM   8518  C  C     . SER B  1  398 ? -37.960 27.543  51.291 1.00 31.46  ? 1197 SER D C     1 
ATOM   8519  O  O     . SER B  1  398 ? -39.055 27.089  50.972 1.00 36.42  ? 1197 SER D O     1 
ATOM   8520  C  CB    . SER B  1  398 ? -37.770 29.011  53.315 1.00 26.36  ? 1197 SER D CB    1 
ATOM   8521  O  OG    . SER B  1  398 ? -37.710 28.946  54.749 1.00 30.13  ? 1197 SER D OG    1 
ATOM   8522  N  N     . LEU B  1  399 ? -37.079 27.953  50.385 1.00 28.18  ? 1198 LEU D N     1 
ATOM   8523  C  CA    . LEU B  1  399 ? -37.391 27.863  48.972 1.00 29.98  ? 1198 LEU D CA    1 
ATOM   8524  C  C     . LEU B  1  399 ? -37.503 26.404  48.481 1.00 32.32  ? 1198 LEU D C     1 
ATOM   8525  O  O     . LEU B  1  399 ? -38.342 26.092  47.626 1.00 33.28  ? 1198 LEU D O     1 
ATOM   8526  C  CB    . LEU B  1  399 ? -36.342 28.614  48.167 1.00 25.45  ? 1198 LEU D CB    1 
ATOM   8527  C  CG    . LEU B  1  399 ? -36.317 28.412  46.653 1.00 30.18  ? 1198 LEU D CG    1 
ATOM   8528  C  CD1   . LEU B  1  399 ? -37.600 29.023  46.054 1.00 31.06  ? 1198 LEU D CD1   1 
ATOM   8529  C  CD2   . LEU B  1  399 ? -35.035 29.043  46.079 1.00 27.93  ? 1198 LEU D CD2   1 
ATOM   8530  N  N     . SER B  1  400 ? -36.631 25.547  49.000 1.00 29.79  ? 1199 SER D N     1 
ATOM   8531  C  CA    . SER B  1  400 ? -36.580 24.138  48.602 1.00 34.44  ? 1199 SER D CA    1 
ATOM   8532  C  C     . SER B  1  400 ? -37.899 23.433  48.960 1.00 37.54  ? 1199 SER D C     1 
ATOM   8533  O  O     . SER B  1  400 ? -38.316 22.563  48.233 1.00 40.71  ? 1199 SER D O     1 
ATOM   8534  C  CB    . SER B  1  400 ? -35.375 23.415  49.247 1.00 29.67  ? 1199 SER D CB    1 
ATOM   8535  O  OG    . SER B  1  400 ? -35.533 23.238  50.645 1.00 32.75  ? 1199 SER D OG    1 
ATOM   8536  N  N     . LYS B  1  401 ? -38.561 23.880  50.027 1.00 36.59  ? 1200 LYS D N     1 
ATOM   8537  C  CA    . LYS B  1  401 ? -39.829 23.332  50.452 1.00 38.73  ? 1200 LYS D CA    1 
ATOM   8538  C  C     . LYS B  1  401 ? -41.018 24.031  49.792 1.00 42.80  ? 1200 LYS D C     1 
ATOM   8539  O  O     . LYS B  1  401 ? -42.148 23.594  49.950 1.00 45.98  ? 1200 LYS D O     1 
ATOM   8540  C  CB    . LYS B  1  401 ? -39.970 23.417  51.966 1.00 39.40  ? 1200 LYS D CB    1 
ATOM   8541  C  CG    . LYS B  1  401 ? -38.927 22.607  52.732 1.00 44.14  ? 1200 LYS D CG    1 
ATOM   8542  C  CD    . LYS B  1  401 ? -38.878 23.021  54.195 1.00 46.44  ? 1200 LYS D CD    1 
ATOM   8543  C  CE    . LYS B  1  401 ? -37.670 22.372  54.870 1.00 63.30  ? 1200 LYS D CE    1 
ATOM   8544  N  NZ    . LYS B  1  401 ? -37.223 22.870  56.209 1.00 57.18  ? 1200 LYS D NZ    1 
ATOM   8545  N  N     . ASN B  1  402 ? -40.777 25.124  49.074 1.00 42.38  ? 1201 ASN D N     1 
ATOM   8546  C  CA    . ASN B  1  402 ? -41.861 25.884  48.472 1.00 36.28  ? 1201 ASN D CA    1 
ATOM   8547  C  C     . ASN B  1  402 ? -41.388 26.662  47.257 1.00 38.46  ? 1201 ASN D C     1 
ATOM   8548  O  O     . ASN B  1  402 ? -40.843 27.809  47.403 1.00 41.83  ? 1201 ASN D O     1 
ATOM   8549  C  CB    . ASN B  1  402 ? -42.486 26.832  49.531 1.00 38.40  ? 1201 ASN D CB    1 
ATOM   8550  C  CG    . ASN B  1  402 ? -43.588 27.718  48.972 1.00 38.42  ? 1201 ASN D CG    1 
ATOM   8551  O  OD1   . ASN B  1  402 ? -44.036 27.557  47.827 1.00 37.18  ? 1201 ASN D OD1   1 
ATOM   8552  N  ND2   . ASN B  1  402 ? -44.027 28.672  49.789 1.00 34.63  ? 1201 ASN D ND2   1 
ATOM   8553  N  N     . PRO B  1  403 ? -41.586 26.076  46.035 1.00 39.36  ? 1202 PRO D N     1 
ATOM   8554  C  CA    . PRO B  1  403 ? -41.054 26.853  44.895 1.00 32.91  ? 1202 PRO D CA    1 
ATOM   8555  C  C     . PRO B  1  403 ? -41.759 28.202  44.698 1.00 36.34  ? 1202 PRO D C     1 
ATOM   8556  O  O     . PRO B  1  403 ? -41.163 29.095  44.098 1.00 29.12  ? 1202 PRO D O     1 
ATOM   8557  C  CB    . PRO B  1  403 ? -41.309 25.953  43.679 1.00 32.32  ? 1202 PRO D CB    1 
ATOM   8558  C  CG    . PRO B  1  403 ? -41.648 24.568  44.224 1.00 33.73  ? 1202 PRO D CG    1 
ATOM   8559  C  CD    . PRO B  1  403 ? -42.215 24.794  45.593 1.00 34.75  ? 1202 PRO D CD    1 
ATOM   8560  N  N     . ASP B  1  404 ? -43.000 28.337  45.175 1.00 35.41  ? 1203 ASP D N     1 
ATOM   8561  C  CA    . ASP B  1  404 ? -43.794 29.534  44.975 1.00 37.82  ? 1203 ASP D CA    1 
ATOM   8562  C  C     . ASP B  1  404 ? -43.682 30.586  46.087 1.00 37.77  ? 1203 ASP D C     1 
ATOM   8563  O  O     . ASP B  1  404 ? -44.527 31.534  46.187 1.00 31.03  ? 1203 ASP D O     1 
ATOM   8564  C  CB    . ASP B  1  404 ? -45.262 29.129  44.813 1.00 40.14  ? 1203 ASP D CB    1 
ATOM   8565  C  CG    . ASP B  1  404 ? -45.497 28.380  43.541 1.00 42.50  ? 1203 ASP D CG    1 
ATOM   8566  O  OD1   . ASP B  1  404 ? -44.933 28.739  42.474 1.00 45.25  ? 1203 ASP D OD1   1 
ATOM   8567  O  OD2   . ASP B  1  404 ? -46.250 27.422  43.614 1.00 48.10  ? 1203 ASP D OD2   1 
ATOM   8568  N  N     . ILE B  1  405 ? -42.681 30.428  46.945 1.00 33.78  ? 1204 ILE D N     1 
ATOM   8569  C  CA    . ILE B  1  405 ? -42.441 31.373  48.026 1.00 32.84  ? 1204 ILE D CA    1 
ATOM   8570  C  C     . ILE B  1  405 ? -42.274 32.816  47.482 1.00 30.49  ? 1204 ILE D C     1 
ATOM   8571  O  O     . ILE B  1  405 ? -41.710 33.047  46.408 1.00 30.72  ? 1204 ILE D O     1 
ATOM   8572  C  CB    . ILE B  1  405 ? -41.214 30.927  48.840 1.00 34.44  ? 1204 ILE D CB    1 
ATOM   8573  C  CG1   . ILE B  1  405 ? -41.201 31.583  50.230 1.00 33.27  ? 1204 ILE D CG1   1 
ATOM   8574  C  CG2   . ILE B  1  405 ? -39.936 31.205  48.067 1.00 34.34  ? 1204 ILE D CG2   1 
ATOM   8575  C  CD1   . ILE B  1  405 ? -40.215 30.961  51.158 1.00 31.05  ? 1204 ILE D CD1   1 
ATOM   8576  N  N     . SER B  1  406 ? -42.807 33.765  48.207 1.00 28.44  ? 1205 SER D N     1 
ATOM   8577  C  CA    . SER B  1  406 ? -42.732 35.144  47.751 1.00 32.13  ? 1205 SER D CA    1 
ATOM   8578  C  C     . SER B  1  406 ? -41.476 35.815  48.361 1.00 32.33  ? 1205 SER D C     1 
ATOM   8579  O  O     . SER B  1  406 ? -40.850 35.289  49.273 1.00 37.01  ? 1205 SER D O     1 
ATOM   8580  C  CB    . SER B  1  406 ? -44.002 35.905  48.171 1.00 27.12  ? 1205 SER D CB    1 
ATOM   8581  O  OG    . SER B  1  406 ? -44.003 36.050  49.581 1.00 32.30  ? 1205 SER D OG    1 
ATOM   8582  N  N     . ILE B  1  407 ? -41.161 37.001  47.874 1.00 32.20  ? 1206 ILE D N     1 
ATOM   8583  C  CA    . ILE B  1  407 ? -40.057 37.764  48.410 1.00 31.82  ? 1206 ILE D CA    1 
ATOM   8584  C  C     . ILE B  1  407 ? -40.298 38.123  49.866 1.00 33.05  ? 1206 ILE D C     1 
ATOM   8585  O  O     . ILE B  1  407 ? -39.377 38.074  50.694 1.00 32.87  ? 1206 ILE D O     1 
ATOM   8586  C  CB    . ILE B  1  407 ? -39.823 39.044  47.606 1.00 30.75  ? 1206 ILE D CB    1 
ATOM   8587  C  CG1   . ILE B  1  407 ? -39.467 38.710  46.142 1.00 31.81  ? 1206 ILE D CG1   1 
ATOM   8588  C  CG2   . ILE B  1  407 ? -38.777 39.915  48.299 1.00 29.95  ? 1206 ILE D CG2   1 
ATOM   8589  C  CD1   . ILE B  1  407 ? -38.151 37.988  45.914 1.00 35.11  ? 1206 ILE D CD1   1 
ATOM   8590  N  N     . ALA B  1  408 ? -41.539 38.477  50.198 1.00 31.55  ? 1207 ALA D N     1 
ATOM   8591  C  CA    . ALA B  1  408 ? -41.838 38.860  51.563 1.00 30.63  ? 1207 ALA D CA    1 
ATOM   8592  C  C     . ALA B  1  408 ? -41.590 37.668  52.501 1.00 29.75  ? 1207 ALA D C     1 
ATOM   8593  O  O     . ALA B  1  408 ? -41.067 37.829  53.577 1.00 33.53  ? 1207 ALA D O     1 
ATOM   8594  C  CB    . ALA B  1  408 ? -43.299 39.332  51.671 1.00 28.61  ? 1207 ALA D CB    1 
ATOM   8595  N  N     . GLU B  1  409 ? -42.005 36.471  52.090 1.00 31.89  ? 1208 GLU D N     1 
ATOM   8596  C  CA    . GLU B  1  409 ? -41.798 35.272  52.891 1.00 30.74  ? 1208 GLU D CA    1 
ATOM   8597  C  C     . GLU B  1  409 ? -40.318 34.949  53.045 1.00 27.38  ? 1208 GLU D C     1 
ATOM   8598  O  O     . GLU B  1  409 ? -39.868 34.588  54.141 1.00 25.70  ? 1208 GLU D O     1 
ATOM   8599  C  CB    . GLU B  1  409 ? -42.516 34.081  52.291 1.00 34.51  ? 1208 GLU D CB    1 
ATOM   8600  C  CG    . GLU B  1  409 ? -44.039 34.205  52.221 1.00 43.35  ? 1208 GLU D CG    1 
ATOM   8601  C  CD    . GLU B  1  409 ? -44.673 32.990  51.554 1.00 45.00  ? 1208 GLU D CD    1 
ATOM   8602  O  OE1   . GLU B  1  409 ? -44.612 32.867  50.297 1.00 51.78  ? 1208 GLU D OE1   1 
ATOM   8603  O  OE2   . GLU B  1  409 ? -45.174 32.119  52.286 1.00 55.34  ? 1208 GLU D OE2   1 
ATOM   8604  N  N     . LEU B  1  410 ? -39.572 35.131  51.975 1.00 25.40  ? 1209 LEU D N     1 
ATOM   8605  C  CA    . LEU B  1  410 ? -38.127 34.915  52.016 1.00 30.90  ? 1209 LEU D CA    1 
ATOM   8606  C  C     . LEU B  1  410 ? -37.447 35.869  53.006 1.00 36.33  ? 1209 LEU D C     1 
ATOM   8607  O  O     . LEU B  1  410 ? -36.506 35.476  53.715 1.00 38.03  ? 1209 LEU D O     1 
ATOM   8608  C  CB    . LEU B  1  410 ? -37.529 35.067  50.617 1.00 28.00  ? 1209 LEU D CB    1 
ATOM   8609  C  CG    . LEU B  1  410 ? -37.626 33.813  49.744 1.00 28.77  ? 1209 LEU D CG    1 
ATOM   8610  C  CD1   . LEU B  1  410 ? -37.401 34.139  48.251 1.00 28.58  ? 1209 LEU D CD1   1 
ATOM   8611  C  CD2   . LEU B  1  410 ? -36.670 32.690  50.182 1.00 29.65  ? 1209 LEU D CD2   1 
ATOM   8612  N  N     . MET B  1  411 ? -37.952 37.109  53.087 1.00 33.93  ? 1210 MET D N     1 
ATOM   8613  C  CA    . MET B  1  411 ? -37.395 38.095  53.981 1.00 33.90  ? 1210 MET D CA    1 
ATOM   8614  C  C     . MET B  1  411 ? -37.610 37.765  55.450 1.00 38.63  ? 1210 MET D C     1 
ATOM   8615  O  O     . MET B  1  411 ? -36.978 38.300  56.324 1.00 39.01  ? 1210 MET D O     1 
ATOM   8616  C  CB    . MET B  1  411 ? -37.933 39.450  53.659 1.00 34.33  ? 1210 MET D CB    1 
ATOM   8617  C  CG    . MET B  1  411 ? -37.193 40.107  52.518 1.00 32.53  ? 1210 MET D CG    1 
ATOM   8618  S  SD    . MET B  1  411 ? -37.884 41.775  52.174 1.00 38.41  ? 1210 MET D SD    1 
ATOM   8619  C  CE    . MET B  1  411 ? -37.242 42.766  53.494 1.00 31.09  ? 1210 MET D CE    1 
ATOM   8620  N  N     . GLU B  1  412 ? -38.523 36.847  55.715 1.00 39.51  ? 1211 GLU D N     1 
ATOM   8621  C  CA    . GLU B  1  412 ? -38.683 36.320  57.062 1.00 37.41  ? 1211 GLU D CA    1 
ATOM   8622  C  C     . GLU B  1  412 ? -37.452 35.547  57.456 1.00 35.06  ? 1211 GLU D C     1 
ATOM   8623  O  O     . GLU B  1  412 ? -37.100 35.526  58.577 1.00 39.31  ? 1211 GLU D O     1 
ATOM   8624  C  CB    . GLU B  1  412 ? -39.910 35.427  57.124 1.00 38.46  ? 1211 GLU D CB    1 
ATOM   8625  C  CG    . GLU B  1  412 ? -41.200 36.181  57.419 1.00 42.56  ? 1211 GLU D CG    1 
ATOM   8626  C  CD    . GLU B  1  412 ? -42.416 35.332  57.107 1.00 50.87  ? 1211 GLU D CD    1 
ATOM   8627  O  OE1   . GLU B  1  412 ? -43.347 35.854  56.478 1.00 58.51  ? 1211 GLU D OE1   1 
ATOM   8628  O  OE2   . GLU B  1  412 ? -42.451 34.127  57.471 1.00 55.26  ? 1211 GLU D OE2   1 
ATOM   8629  N  N     . ASP B  1  413 ? -36.755 34.949  56.504 1.00 35.16  ? 1212 ASP D N     1 
ATOM   8630  C  CA    . ASP B  1  413 ? -35.464 34.320  56.795 1.00 34.67  ? 1212 ASP D CA    1 
ATOM   8631  C  C     . ASP B  1  413 ? -34.340 35.331  56.626 1.00 33.82  ? 1212 ASP D C     1 
ATOM   8632  O  O     . ASP B  1  413 ? -33.405 35.345  57.382 1.00 35.78  ? 1212 ASP D O     1 
ATOM   8633  C  CB    . ASP B  1  413 ? -35.164 33.196  55.831 1.00 29.95  ? 1212 ASP D CB    1 
ATOM   8634  C  CG    . ASP B  1  413 ? -36.076 32.012  56.025 1.00 32.53  ? 1212 ASP D CG    1 
ATOM   8635  O  OD1   . ASP B  1  413 ? -36.241 31.538  57.154 1.00 31.65  ? 1212 ASP D OD1   1 
ATOM   8636  O  OD2   . ASP B  1  413 ? -36.590 31.504  55.026 1.00 33.72  ? 1212 ASP D OD2   1 
ATOM   8637  N  N     . ILE B  1  414 ? -34.410 36.146  55.595 1.00 31.60  ? 1213 ILE D N     1 
ATOM   8638  C  CA    . ILE B  1  414 ? -33.288 37.005  55.269 1.00 32.65  ? 1213 ILE D CA    1 
ATOM   8639  C  C     . ILE B  1  414 ? -33.729 38.468  55.490 1.00 39.89  ? 1213 ILE D C     1 
ATOM   8640  O  O     . ILE B  1  414 ? -34.482 39.041  54.662 1.00 36.60  ? 1213 ILE D O     1 
ATOM   8641  C  CB    . ILE B  1  414 ? -32.877 36.819  53.771 1.00 31.11  ? 1213 ILE D CB    1 
ATOM   8642  C  CG1   . ILE B  1  414 ? -32.358 35.434  53.556 1.00 31.24  ? 1213 ILE D CG1   1 
ATOM   8643  C  CG2   . ILE B  1  414 ? -31.809 37.827  53.344 1.00 31.65  ? 1213 ILE D CG2   1 
ATOM   8644  C  CD1   . ILE B  1  414 ? -32.492 34.940  52.139 1.00 25.31  ? 1213 ILE D CD1   1 
ATOM   8645  N  N     . GLU B  1  415 ? -33.212 39.064  56.557 1.00 39.21  ? 1214 GLU D N     1 
ATOM   8646  C  CA    . GLU B  1  415 ? -33.640 40.393  56.986 1.00 40.52  ? 1214 GLU D CA    1 
ATOM   8647  C  C     . GLU B  1  415 ? -33.151 41.476  56.056 1.00 36.70  ? 1214 GLU D C     1 
ATOM   8648  O  O     . GLU B  1  415 ? -33.827 42.427  55.829 1.00 38.58  ? 1214 GLU D O     1 
ATOM   8649  C  CB    . GLU B  1  415 ? -33.128 40.683  58.369 1.00 46.36  ? 1214 GLU D CB    1 
ATOM   8650  C  CG    . GLU B  1  415 ? -33.639 39.785  59.456 1.00 56.77  ? 1214 GLU D CG    1 
ATOM   8651  C  CD    . GLU B  1  415 ? -33.182 40.298  60.831 1.00 74.21  ? 1214 GLU D CD    1 
ATOM   8652  O  OE1   . GLU B  1  415 ? -33.235 41.546  61.096 1.00 71.80  ? 1214 GLU D OE1   1 
ATOM   8653  O  OE2   . GLU B  1  415 ? -32.761 39.444  61.663 1.00 73.55  ? 1214 GLU D OE2   1 
ATOM   8654  N  N     . GLY B  1  416 ? -31.969 41.298  55.507 1.00 32.93  ? 1215 GLY D N     1 
ATOM   8655  C  CA    . GLY B  1  416 ? -31.325 42.302  54.704 1.00 31.65  ? 1215 GLY D CA    1 
ATOM   8656  C  C     . GLY B  1  416 ? -29.842 41.977  54.623 1.00 35.94  ? 1215 GLY D C     1 
ATOM   8657  O  O     . GLY B  1  416 ? -29.388 40.904  55.083 1.00 33.05  ? 1215 GLY D O     1 
ATOM   8658  N  N     . PRO B  1  417 ? -29.065 42.928  54.097 1.00 34.54  ? 1216 PRO D N     1 
ATOM   8659  C  CA    . PRO B  1  417 ? -27.643 42.740  53.992 1.00 31.87  ? 1216 PRO D CA    1 
ATOM   8660  C  C     . PRO B  1  417 ? -27.024 42.643  55.378 1.00 32.08  ? 1216 PRO D C     1 
ATOM   8661  O  O     . PRO B  1  417 ? -27.480 43.281  56.307 1.00 34.11  ? 1216 PRO D O     1 
ATOM   8662  C  CB    . PRO B  1  417 ? -27.179 44.039  53.308 1.00 33.61  ? 1216 PRO D CB    1 
ATOM   8663  C  CG    . PRO B  1  417 ? -28.372 44.486  52.543 1.00 31.42  ? 1216 PRO D CG    1 
ATOM   8664  C  CD    . PRO B  1  417 ? -29.549 44.112  53.357 1.00 30.38  ? 1216 PRO D CD    1 
ATOM   8665  N  N     . ASP B  1  418 ? -25.942 41.896  55.501 1.00 35.32  ? 1217 ASP D N     1 
ATOM   8666  C  CA    . ASP B  1  418 ? -25.170 41.834  56.713 1.00 30.83  ? 1217 ASP D CA    1 
ATOM   8667  C  C     . ASP B  1  418 ? -23.713 42.161  56.383 1.00 30.75  ? 1217 ASP D C     1 
ATOM   8668  O  O     . ASP B  1  418 ? -23.008 41.338  55.828 1.00 31.24  ? 1217 ASP D O     1 
ATOM   8669  C  CB    . ASP B  1  418 ? -25.287 40.423  57.310 1.00 27.43  ? 1217 ASP D CB    1 
ATOM   8670  C  CG    . ASP B  1  418 ? -24.848 40.395  58.767 1.00 30.72  ? 1217 ASP D CG    1 
ATOM   8671  O  OD1   . ASP B  1  418 ? -24.696 41.484  59.395 1.00 30.95  ? 1217 ASP D OD1   1 
ATOM   8672  O  OD2   . ASP B  1  418 ? -24.583 39.280  59.266 1.00 25.98  ? 1217 ASP D OD2   1 
ATOM   8673  N  N     . PHE B  1  419 ? -23.286 43.366  56.695 1.00 29.92  ? 1218 PHE D N     1 
ATOM   8674  C  CA    . PHE B  1  419 ? -21.910 43.773  56.391 1.00 27.51  ? 1218 PHE D CA    1 
ATOM   8675  C  C     . PHE B  1  419 ? -20.852 43.218  57.361 1.00 26.78  ? 1218 PHE D C     1 
ATOM   8676  O  O     . PHE B  1  419 ? -21.120 43.062  58.567 1.00 26.94  ? 1218 PHE D O     1 
ATOM   8677  C  CB    . PHE B  1  419 ? -21.830 45.292  56.324 1.00 25.10  ? 1218 PHE D CB    1 
ATOM   8678  C  CG    . PHE B  1  419 ? -22.797 45.884  55.375 1.00 26.44  ? 1218 PHE D CG    1 
ATOM   8679  C  CD1   . PHE B  1  419 ? -22.692 45.673  54.006 1.00 24.65  ? 1218 PHE D CD1   1 
ATOM   8680  C  CD2   . PHE B  1  419 ? -23.838 46.698  55.848 1.00 26.80  ? 1218 PHE D CD2   1 
ATOM   8681  C  CE1   . PHE B  1  419 ? -23.576 46.272  53.110 1.00 25.04  ? 1218 PHE D CE1   1 
ATOM   8682  C  CE2   . PHE B  1  419 ? -24.758 47.254  54.956 1.00 27.02  ? 1218 PHE D CE2   1 
ATOM   8683  C  CZ    . PHE B  1  419 ? -24.639 47.055  53.576 1.00 23.58  ? 1218 PHE D CZ    1 
ATOM   8684  N  N     . PRO B  1  420 ? -19.652 42.886  56.828 1.00 28.86  ? 1219 PRO D N     1 
ATOM   8685  C  CA    . PRO B  1  420 ? -18.625 42.473  57.803 1.00 29.14  ? 1219 PRO D CA    1 
ATOM   8686  C  C     . PRO B  1  420 ? -18.229 43.544  58.780 1.00 29.27  ? 1219 PRO D C     1 
ATOM   8687  O  O     . PRO B  1  420 ? -17.765 43.246  59.866 1.00 29.75  ? 1219 PRO D O     1 
ATOM   8688  C  CB    . PRO B  1  420 ? -17.427 42.061  56.922 1.00 26.01  ? 1219 PRO D CB    1 
ATOM   8689  C  CG    . PRO B  1  420 ? -17.575 42.844  55.704 1.00 27.68  ? 1219 PRO D CG    1 
ATOM   8690  C  CD    . PRO B  1  420 ? -19.094 42.856  55.452 1.00 27.23  ? 1219 PRO D CD    1 
ATOM   8691  N  N     . THR B  1  421 ? -18.460 44.799  58.403 1.00 32.44  ? 1220 THR D N     1 
ATOM   8692  C  CA    . THR B  1  421 ? -18.105 45.937  59.225 1.00 29.64  ? 1220 THR D CA    1 
ATOM   8693  C  C     . THR B  1  421 ? -19.264 46.330  60.122 1.00 34.18  ? 1220 THR D C     1 
ATOM   8694  O  O     . THR B  1  421 ? -19.185 47.353  60.836 1.00 31.72  ? 1220 THR D O     1 
ATOM   8695  C  CB    . THR B  1  421 ? -17.776 47.122  58.316 1.00 31.08  ? 1220 THR D CB    1 
ATOM   8696  O  OG1   . THR B  1  421 ? -18.703 47.168  57.221 1.00 29.71  ? 1220 THR D OG1   1 
ATOM   8697  C  CG2   . THR B  1  421 ? -16.380 46.973  57.754 1.00 24.20  ? 1220 THR D CG2   1 
ATOM   8698  N  N     . ALA B  1  422 ? -20.336 45.513  60.104 1.00 29.21  ? 1221 ALA D N     1 
ATOM   8699  C  CA    . ALA B  1  422 ? -21.485 45.702  61.003 1.00 28.46  ? 1221 ALA D CA    1 
ATOM   8700  C  C     . ALA B  1  422 ? -22.231 47.011  60.724 1.00 28.60  ? 1221 ALA D C     1 
ATOM   8701  O  O     . ALA B  1  422 ? -22.610 47.264  59.590 1.00 35.37  ? 1221 ALA D O     1 
ATOM   8702  C  CB    . ALA B  1  422 ? -21.059 45.590  62.465 1.00 22.07  ? 1221 ALA D CB    1 
ATOM   8703  N  N     . GLY B  1  423 ? -22.398 47.859  61.728 1.00 27.01  ? 1222 GLY D N     1 
ATOM   8704  C  CA    . GLY B  1  423 ? -23.101 49.089  61.547 1.00 27.79  ? 1222 GLY D CA    1 
ATOM   8705  C  C     . GLY B  1  423 ? -24.630 48.950  61.572 1.00 30.95  ? 1222 GLY D C     1 
ATOM   8706  O  O     . GLY B  1  423 ? -25.201 47.951  62.051 1.00 28.98  ? 1222 GLY D O     1 
ATOM   8707  N  N     . LEU B  1  424 ? -25.300 49.980  61.051 1.00 31.83  ? 1223 LEU D N     1 
ATOM   8708  C  CA    . LEU B  1  424 ? -26.770 50.012  61.055 1.00 30.82  ? 1223 LEU D CA    1 
ATOM   8709  C  C     . LEU B  1  424 ? -27.310 50.254  59.686 1.00 33.35  ? 1223 LEU D C     1 
ATOM   8710  O  O     . LEU B  1  424 ? -26.684 50.940  58.843 1.00 29.06  ? 1223 LEU D O     1 
ATOM   8711  C  CB    . LEU B  1  424 ? -27.292 51.133  61.965 1.00 35.06  ? 1223 LEU D CB    1 
ATOM   8712  C  CG    . LEU B  1  424 ? -27.154 51.163  63.516 1.00 33.71  ? 1223 LEU D CG    1 
ATOM   8713  C  CD1   . LEU B  1  424 ? -25.705 51.156  64.029 1.00 34.35  ? 1223 LEU D CD1   1 
ATOM   8714  C  CD2   . LEU B  1  424 ? -27.823 52.465  63.943 1.00 38.85  ? 1223 LEU D CD2   1 
ATOM   8715  N  N     . ILE B  1  425 ? -28.470 49.656  59.414 1.00 30.19  ? 1224 ILE D N     1 
ATOM   8716  C  CA    . ILE B  1  425 ? -29.193 50.005  58.242 1.00 32.13  ? 1224 ILE D CA    1 
ATOM   8717  C  C     . ILE B  1  425 ? -30.458 50.707  58.756 1.00 34.41  ? 1224 ILE D C     1 
ATOM   8718  O  O     . ILE B  1  425 ? -31.146 50.225  59.660 1.00 33.31  ? 1224 ILE D O     1 
ATOM   8719  C  CB    . ILE B  1  425 ? -29.542 48.745  57.409 1.00 32.73  ? 1224 ILE D CB    1 
ATOM   8720  C  CG1   . ILE B  1  425 ? -28.343 48.285  56.596 1.00 30.99  ? 1224 ILE D CG1   1 
ATOM   8721  C  CG2   . ILE B  1  425 ? -30.681 49.026  56.422 1.00 30.20  ? 1224 ILE D CG2   1 
ATOM   8722  C  CD1   . ILE B  1  425 ? -28.493 46.862  56.029 1.00 27.35  ? 1224 ILE D CD1   1 
ATOM   8723  N  N     . LEU B  1  426 ? -30.830 51.811  58.118 1.00 35.26  ? 1225 LEU D N     1 
ATOM   8724  C  CA    . LEU B  1  426 ? -32.070 52.540  58.480 1.00 35.14  ? 1225 LEU D CA    1 
ATOM   8725  C  C     . LEU B  1  426 ? -33.266 52.141  57.652 1.00 33.58  ? 1225 LEU D C     1 
ATOM   8726  O  O     . LEU B  1  426 ? -33.323 52.512  56.471 1.00 38.78  ? 1225 LEU D O     1 
ATOM   8727  C  CB    . LEU B  1  426 ? -31.830 54.015  58.221 1.00 36.03  ? 1225 LEU D CB    1 
ATOM   8728  C  CG    . LEU B  1  426 ? -30.520 54.640  58.694 1.00 39.33  ? 1225 LEU D CG    1 
ATOM   8729  C  CD1   . LEU B  1  426 ? -30.480 56.147  58.405 1.00 43.78  ? 1225 LEU D CD1   1 
ATOM   8730  C  CD2   . LEU B  1  426 ? -30.269 54.331  60.169 1.00 39.63  ? 1225 LEU D CD2   1 
ATOM   8731  N  N     . GLY B  1  427 ? -34.181 51.354  58.217 1.00 35.37  ? 1226 GLY D N     1 
ATOM   8732  C  CA    . GLY B  1  427 ? -35.425 50.999  57.535 1.00 33.01  ? 1226 GLY D CA    1 
ATOM   8733  C  C     . GLY B  1  427 ? -35.327 49.777  56.665 1.00 37.68  ? 1226 GLY D C     1 
ATOM   8734  O  O     . GLY B  1  427 ? -34.226 49.311  56.333 1.00 34.23  ? 1226 GLY D O     1 
ATOM   8735  N  N     . LYS B  1  428 ? -36.491 49.270  56.276 1.00 38.52  ? 1227 LYS D N     1 
ATOM   8736  C  CA    . LYS B  1  428 ? -36.540 48.101  55.463 1.00 41.97  ? 1227 LYS D CA    1 
ATOM   8737  C  C     . LYS B  1  428 ? -36.974 48.428  54.074 1.00 38.36  ? 1227 LYS D C     1 
ATOM   8738  O  O     . LYS B  1  428 ? -37.165 47.546  53.288 1.00 45.16  ? 1227 LYS D O     1 
ATOM   8739  C  CB    . LYS B  1  428 ? -37.487 47.102  56.080 1.00 48.86  ? 1227 LYS D CB    1 
ATOM   8740  C  CG    . LYS B  1  428 ? -36.899 46.365  57.271 1.00 54.28  ? 1227 LYS D CG    1 
ATOM   8741  C  CD    . LYS B  1  428 ? -37.552 44.981  57.424 1.00 58.99  ? 1227 LYS D CD    1 
ATOM   8742  C  CE    . LYS B  1  428 ? -36.473 43.897  57.574 1.00 56.50  ? 1227 LYS D CE    1 
ATOM   8743  N  NZ    . LYS B  1  428 ? -36.143 43.576  59.010 1.00 60.00  ? 1227 LYS D NZ    1 
ATOM   8744  N  N     . SER B  1  429 ? -37.151 49.690  53.768 1.00 35.76  ? 1228 SER D N     1 
ATOM   8745  C  CA    . SER B  1  429 ? -37.844 50.016  52.498 1.00 37.80  ? 1228 SER D CA    1 
ATOM   8746  C  C     . SER B  1  429 ? -36.893 49.891  51.290 1.00 31.53  ? 1228 SER D C     1 
ATOM   8747  O  O     . SER B  1  429 ? -37.290 49.407  50.233 1.00 33.94  ? 1228 SER D O     1 
ATOM   8748  C  CB    . SER B  1  429 ? -38.533 51.395  52.524 1.00 34.59  ? 1228 SER D CB    1 
ATOM   8749  O  OG    . SER B  1  429 ? -37.840 52.287  51.624 1.00 43.33  ? 1228 SER D OG    1 
ATOM   8750  N  N     . GLY B  1  430 ? -35.648 50.326  51.424 1.00 31.06  ? 1229 GLY D N     1 
ATOM   8751  C  CA    . GLY B  1  430 ? -34.647 50.160  50.368 1.00 26.08  ? 1229 GLY D CA    1 
ATOM   8752  C  C     . GLY B  1  430 ? -34.303 48.676  50.165 1.00 28.66  ? 1229 GLY D C     1 
ATOM   8753  O  O     . GLY B  1  430 ? -34.133 48.228  49.030 1.00 28.38  ? 1229 GLY D O     1 
ATOM   8754  N  N     . ILE B  1  431 ? -34.224 47.910  51.237 1.00 30.19  ? 1230 ILE D N     1 
ATOM   8755  C  CA    . ILE B  1  431 ? -33.934 46.480  51.170 1.00 32.11  ? 1230 ILE D CA    1 
ATOM   8756  C  C     . ILE B  1  431 ? -35.069 45.784  50.403 1.00 32.74  ? 1230 ILE D C     1 
ATOM   8757  O  O     . ILE B  1  431 ? -34.835 44.927  49.554 1.00 35.28  ? 1230 ILE D O     1 
ATOM   8758  C  CB    . ILE B  1  431 ? -33.838 45.893  52.601 1.00 32.00  ? 1230 ILE D CB    1 
ATOM   8759  C  CG1   . ILE B  1  431 ? -32.543 46.382  53.292 1.00 30.19  ? 1230 ILE D CG1   1 
ATOM   8760  C  CG2   . ILE B  1  431 ? -34.018 44.339  52.619 1.00 32.16  ? 1230 ILE D CG2   1 
ATOM   8761  C  CD1   . ILE B  1  431 ? -32.588 46.210  54.788 1.00 29.78  ? 1230 ILE D CD1   1 
ATOM   8762  N  N     . ARG B  1  432 ? -36.289 46.145  50.740 1.00 34.40  ? 1231 ARG D N     1 
ATOM   8763  C  CA    . ARG B  1  432 ? -37.422 45.562  50.124 1.00 36.17  ? 1231 ARG D CA    1 
ATOM   8764  C  C     . ARG B  1  432 ? -37.435 45.868  48.630 1.00 38.13  ? 1231 ARG D C     1 
ATOM   8765  O  O     . ARG B  1  432 ? -37.619 45.070  47.821 1.00 36.54  ? 1231 ARG D O     1 
ATOM   8766  C  CB    . ARG B  1  432 ? -38.659 46.110  50.807 1.00 42.02  ? 1231 ARG D CB    1 
ATOM   8767  C  CG    . ARG B  1  432 ? -39.936 45.549  50.272 1.00 47.01  ? 1231 ARG D CG    1 
ATOM   8768  C  CD    . ARG B  1  432 ? -39.946 44.087  50.618 1.00 59.82  ? 1231 ARG D CD    1 
ATOM   8769  N  NE    . ARG B  1  432 ? -41.095 43.415  50.061 1.00 75.51  ? 1231 ARG D NE    1 
ATOM   8770  C  CZ    . ARG B  1  432 ? -41.995 42.775  50.777 1.00 76.46  ? 1231 ARG D CZ    1 
ATOM   8771  N  NH1   . ARG B  1  432 ? -41.863 42.697  52.098 1.00 81.14  ? 1231 ARG D NH1   1 
ATOM   8772  N  NH2   . ARG B  1  432 ? -43.009 42.206  50.159 1.00 81.83  ? 1231 ARG D NH2   1 
ATOM   8773  N  N     A ARG B  1  433 ? -37.190 47.077  48.247 0.50 33.84  ? 1232 ARG D N     1 
ATOM   8774  N  N     B ARG B  1  433 ? -37.202 47.080  48.245 0.50 35.54  ? 1232 ARG D N     1 
ATOM   8775  C  CA    A ARG B  1  433 ? -37.167 47.335  46.861 0.50 33.82  ? 1232 ARG D CA    1 
ATOM   8776  C  CA    B ARG B  1  433 ? -37.168 47.341  46.859 0.50 36.51  ? 1232 ARG D CA    1 
ATOM   8777  C  C     A ARG B  1  433 ? -36.072 46.546  46.132 0.50 31.87  ? 1232 ARG D C     1 
ATOM   8778  C  C     B ARG B  1  433 ? -36.070 46.557  46.125 0.50 33.59  ? 1232 ARG D C     1 
ATOM   8779  O  O     A ARG B  1  433 ? -36.308 46.002  45.049 0.50 32.32  ? 1232 ARG D O     1 
ATOM   8780  O  O     B ARG B  1  433 ? -36.328 45.940  45.088 0.50 34.26  ? 1232 ARG D O     1 
ATOM   8781  C  CB    A ARG B  1  433 ? -36.938 48.794  46.762 0.50 36.72  ? 1232 ARG D CB    1 
ATOM   8782  C  CB    B ARG B  1  433 ? -36.979 48.801  46.767 0.50 42.44  ? 1232 ARG D CB    1 
ATOM   8783  C  CG    A ARG B  1  433 ? -37.454 49.497  45.503 0.50 39.06  ? 1232 ARG D CG    1 
ATOM   8784  C  CG    B ARG B  1  433 ? -36.755 49.337  45.369 0.50 47.06  ? 1232 ARG D CG    1 
ATOM   8785  C  CD    A ARG B  1  433 ? -38.033 50.891  45.857 0.50 37.51  ? 1232 ARG D CD    1 
ATOM   8786  C  CD    B ARG B  1  433 ? -37.957 49.055  44.509 0.50 51.95  ? 1232 ARG D CD    1 
ATOM   8787  N  NE    A ARG B  1  433 ? -37.210 51.558  46.883 0.50 38.76  ? 1232 ARG D NE    1 
ATOM   8788  N  NE    B ARG B  1  433 ? -37.951 49.934  43.352 0.50 56.51  ? 1232 ARG D NE    1 
ATOM   8789  C  CZ    A ARG B  1  433 ? -37.664 52.227  47.948 0.50 36.92  ? 1232 ARG D CZ    1 
ATOM   8790  C  CZ    B ARG B  1  433 ? -38.991 50.109  42.552 0.50 58.95  ? 1232 ARG D CZ    1 
ATOM   8791  N  NH1   A ARG B  1  433 ? -38.965 52.359  48.167 0.50 38.64  ? 1232 ARG D NH1   1 
ATOM   8792  N  NH1   B ARG B  1  433 ? -40.127 49.451  42.787 0.50 59.76  ? 1232 ARG D NH1   1 
ATOM   8793  N  NH2   A ARG B  1  433 ? -36.806 52.771  48.801 0.50 33.20  ? 1232 ARG D NH2   1 
ATOM   8794  N  NH2   B ARG B  1  433 ? -38.886 50.935  41.518 0.50 55.50  ? 1232 ARG D NH2   1 
ATOM   8795  N  N     . ALA B  1  434 ? -34.890 46.493  46.729 1.00 28.89  ? 1233 ALA D N     1 
ATOM   8796  C  CA    . ALA B  1  434 ? -33.748 45.786  46.098 1.00 28.99  ? 1233 ALA D CA    1 
ATOM   8797  C  C     . ALA B  1  434 ? -34.037 44.258  45.919 1.00 28.71  ? 1233 ALA D C     1 
ATOM   8798  O  O     . ALA B  1  434 ? -33.746 43.680  44.905 1.00 29.95  ? 1233 ALA D O     1 
ATOM   8799  C  CB    . ALA B  1  434 ? -32.475 46.023  46.916 1.00 24.47  ? 1233 ALA D CB    1 
ATOM   8800  N  N     . TYR B  1  435 ? -34.592 43.633  46.938 1.00 26.50  ? 1234 TYR D N     1 
ATOM   8801  C  CA    . TYR B  1  435 ? -34.930 42.203  46.869 1.00 33.07  ? 1234 TYR D CA    1 
ATOM   8802  C  C     . TYR B  1  435 ? -36.036 41.915  45.842 1.00 32.72  ? 1234 TYR D C     1 
ATOM   8803  O  O     . TYR B  1  435 ? -36.007 40.904  45.175 1.00 32.23  ? 1234 TYR D O     1 
ATOM   8804  C  CB    . TYR B  1  435 ? -35.321 41.665  48.267 1.00 29.53  ? 1234 TYR D CB    1 
ATOM   8805  C  CG    . TYR B  1  435 ? -34.160 41.594  49.199 1.00 29.26  ? 1234 TYR D CG    1 
ATOM   8806  C  CD1   . TYR B  1  435 ? -32.821 41.760  48.711 1.00 25.96  ? 1234 TYR D CD1   1 
ATOM   8807  C  CD2   . TYR B  1  435 ? -34.369 41.340  50.588 1.00 26.93  ? 1234 TYR D CD2   1 
ATOM   8808  C  CE1   . TYR B  1  435 ? -31.747 41.685  49.583 1.00 25.51  ? 1234 TYR D CE1   1 
ATOM   8809  C  CE2   . TYR B  1  435 ? -33.298 41.218  51.453 1.00 25.77  ? 1234 TYR D CE2   1 
ATOM   8810  C  CZ    . TYR B  1  435 ? -31.990 41.418  50.950 1.00 27.89  ? 1234 TYR D CZ    1 
ATOM   8811  O  OH    . TYR B  1  435 ? -30.929 41.331  51.809 1.00 26.69  ? 1234 TYR D OH    1 
ATOM   8812  N  N     . GLU B  1  436 ? -36.973 42.854  45.684 1.00 34.30  ? 1235 GLU D N     1 
ATOM   8813  C  CA    . GLU B  1  436 ? -38.084 42.687  44.752 1.00 36.28  ? 1235 GLU D CA    1 
ATOM   8814  C  C     . GLU B  1  436 ? -37.651 42.925  43.324 1.00 33.11  ? 1235 GLU D C     1 
ATOM   8815  O  O     . GLU B  1  436 ? -38.114 42.243  42.431 1.00 33.32  ? 1235 GLU D O     1 
ATOM   8816  C  CB    . GLU B  1  436 ? -39.288 43.578  45.136 1.00 38.70  ? 1235 GLU D CB    1 
ATOM   8817  C  CG    . GLU B  1  436 ? -40.426 42.763  45.753 1.00 47.89  ? 1235 GLU D CG    1 
ATOM   8818  C  CD    . GLU B  1  436 ? -41.210 43.513  46.814 1.00 59.64  ? 1235 GLU D CD    1 
ATOM   8819  O  OE1   . GLU B  1  436 ? -41.125 44.773  46.851 1.00 60.09  ? 1235 GLU D OE1   1 
ATOM   8820  O  OE2   . GLU B  1  436 ? -41.920 42.831  47.576 1.00 70.04  ? 1235 GLU D OE2   1 
ATOM   8821  N  N     . THR B  1  437 ? -36.775 43.898  43.097 1.00 30.97  ? 1236 THR D N     1 
ATOM   8822  C  CA    . THR B  1  437 ? -36.447 44.307  41.754 1.00 29.08  ? 1236 THR D CA    1 
ATOM   8823  C  C     . THR B  1  437 ? -34.984 44.147  41.408 1.00 31.09  ? 1236 THR D C     1 
ATOM   8824  O  O     . THR B  1  437 ? -34.625 44.222  40.209 1.00 32.13  ? 1236 THR D O     1 
ATOM   8825  C  CB    . THR B  1  437 ? -36.765 45.803  41.561 1.00 29.77  ? 1236 THR D CB    1 
ATOM   8826  O  OG1   . THR B  1  437 ? -35.883 46.576  42.394 1.00 30.38  ? 1236 THR D OG1   1 
ATOM   8827  C  CG2   . THR B  1  437 ? -38.220 46.099  41.989 1.00 29.56  ? 1236 THR D CG2   1 
ATOM   8828  N  N     . GLY B  1  438 ? -34.136 43.970  42.413 1.00 28.39  ? 1237 GLY D N     1 
ATOM   8829  C  CA    . GLY B  1  438 ? -32.662 43.954  42.186 1.00 28.52  ? 1237 GLY D CA    1 
ATOM   8830  C  C     . GLY B  1  438 ? -32.052 45.351  42.261 1.00 32.83  ? 1237 GLY D C     1 
ATOM   8831  O  O     . GLY B  1  438 ? -30.825 45.492  42.166 1.00 35.47  ? 1237 GLY D O     1 
ATOM   8832  N  N     . ARG B  1  439 ? -32.880 46.393  42.409 1.00 31.79  ? 1238 ARG D N     1 
ATOM   8833  C  CA    . ARG B  1  439 ? -32.356 47.750  42.610 1.00 33.35  ? 1238 ARG D CA    1 
ATOM   8834  C  C     . ARG B  1  439 ? -33.046 48.452  43.770 1.00 35.08  ? 1238 ARG D C     1 
ATOM   8835  O  O     . ARG B  1  439 ? -34.273 48.431  43.893 1.00 37.98  ? 1238 ARG D O     1 
ATOM   8836  C  CB    . ARG B  1  439 ? -32.485 48.560  41.339 1.00 31.50  ? 1238 ARG D CB    1 
ATOM   8837  C  CG    . ARG B  1  439 ? -31.409 48.225  40.317 1.00 37.97  ? 1238 ARG D CG    1 
ATOM   8838  C  CD    . ARG B  1  439 ? -31.531 48.992  39.028 1.00 35.88  ? 1238 ARG D CD    1 
ATOM   8839  N  NE    . ARG B  1  439 ? -31.585 50.433  39.312 1.00 38.48  ? 1238 ARG D NE    1 
ATOM   8840  C  CZ    . ARG B  1  439 ? -30.523 51.225  39.443 1.00 40.18  ? 1238 ARG D CZ    1 
ATOM   8841  N  NH1   . ARG B  1  439 ? -29.283 50.743  39.345 1.00 38.49  ? 1238 ARG D NH1   1 
ATOM   8842  N  NH2   . ARG B  1  439 ? -30.700 52.515  39.666 1.00 34.33  ? 1238 ARG D NH2   1 
ATOM   8843  N  N     . GLY B  1  440 ? -32.260 49.005  44.671 1.00 39.26  ? 1239 GLY D N     1 
ATOM   8844  C  CA    . GLY B  1  440 ? -32.780 49.720  45.828 1.00 36.07  ? 1239 GLY D CA    1 
ATOM   8845  C  C     . GLY B  1  440 ? -31.642 50.546  46.418 1.00 38.86  ? 1239 GLY D C     1 
ATOM   8846  O  O     . GLY B  1  440 ? -30.454 50.272  46.199 1.00 39.41  ? 1239 GLY D O     1 
ATOM   8847  N  N     . SER B  1  441 ? -31.995 51.570  47.190 1.00 33.89  ? 1240 SER D N     1 
ATOM   8848  C  CA    . SER B  1  441 ? -31.003 52.355  47.910 1.00 34.20  ? 1240 SER D CA    1 
ATOM   8849  C  C     . SER B  1  441 ? -31.082 52.045  49.389 1.00 33.56  ? 1240 SER D C     1 
ATOM   8850  O  O     . SER B  1  441 ? -32.146 52.131  49.997 1.00 34.01  ? 1240 SER D O     1 
ATOM   8851  C  CB    . SER B  1  441 ? -31.288 53.830  47.696 1.00 36.88  ? 1240 SER D CB    1 
ATOM   8852  O  OG    . SER B  1  441 ? -30.230 54.620  48.183 1.00 42.11  ? 1240 SER D OG    1 
ATOM   8853  N  N     . ILE B  1  442 ? -29.953 51.674  49.977 1.00 34.75  ? 1241 ILE D N     1 
ATOM   8854  C  CA    . ILE B  1  442 ? -29.933 51.286  51.388 1.00 36.55  ? 1241 ILE D CA    1 
ATOM   8855  C  C     . ILE B  1  442 ? -29.118 52.261  52.188 1.00 38.43  ? 1241 ILE D C     1 
ATOM   8856  O  O     . ILE B  1  442 ? -27.976 52.504  51.829 1.00 40.05  ? 1241 ILE D O     1 
ATOM   8857  C  CB    . ILE B  1  442 ? -29.389 49.862  51.574 1.00 35.29  ? 1241 ILE D CB    1 
ATOM   8858  C  CG1   . ILE B  1  442 ? -30.363 48.870  50.914 1.00 37.90  ? 1241 ILE D CG1   1 
ATOM   8859  C  CG2   . ILE B  1  442 ? -29.286 49.557  53.047 1.00 33.11  ? 1241 ILE D CG2   1 
ATOM   8860  C  CD1   . ILE B  1  442 ? -29.785 47.484  50.782 1.00 36.69  ? 1241 ILE D CD1   1 
ATOM   8861  N  N     . GLN B  1  443 ? -29.703 52.800  53.268 1.00 39.00  ? 1242 GLN D N     1 
ATOM   8862  C  CA    . GLN B  1  443 ? -28.982 53.794  54.072 1.00 41.00  ? 1242 GLN D CA    1 
ATOM   8863  C  C     . GLN B  1  443 ? -28.227 53.147  55.190 1.00 35.06  ? 1242 GLN D C     1 
ATOM   8864  O  O     . GLN B  1  443 ? -28.811 52.434  55.996 1.00 34.56  ? 1242 GLN D O     1 
ATOM   8865  C  CB    . GLN B  1  443 ? -29.934 54.848  54.608 1.00 45.28  ? 1242 GLN D CB    1 
ATOM   8866  C  CG    . GLN B  1  443 ? -30.652 55.620  53.513 1.00 50.94  ? 1242 GLN D CG    1 
ATOM   8867  C  CD    . GLN B  1  443 ? -29.710 56.403  52.625 1.00 61.74  ? 1242 GLN D CD    1 
ATOM   8868  O  OE1   . GLN B  1  443 ? -28.740 57.038  53.081 1.00 72.01  ? 1242 GLN D OE1   1 
ATOM   8869  N  NE2   . GLN B  1  443 ? -29.989 56.369  51.352 1.00 67.16  ? 1242 GLN D NE2   1 
ATOM   8870  N  N     . MET B  1  444 ? -26.925 53.373  55.217 1.00 32.87  ? 1243 MET D N     1 
ATOM   8871  C  CA    . MET B  1  444 ? -26.059 52.769  56.227 1.00 32.31  ? 1243 MET D CA    1 
ATOM   8872  C  C     . MET B  1  444 ? -25.578 53.849  57.190 1.00 33.52  ? 1243 MET D C     1 
ATOM   8873  O  O     . MET B  1  444 ? -25.235 54.943  56.747 1.00 36.10  ? 1243 MET D O     1 
ATOM   8874  C  CB    . MET B  1  444 ? -24.836 52.137  55.557 1.00 30.65  ? 1243 MET D CB    1 
ATOM   8875  C  CG    . MET B  1  444 ? -25.117 50.947  54.667 1.00 33.63  ? 1243 MET D CG    1 
ATOM   8876  S  SD    . MET B  1  444 ? -23.519 50.249  54.104 1.00 40.98  ? 1243 MET D SD    1 
ATOM   8877  C  CE    . MET B  1  444 ? -22.885 51.508  53.012 1.00 37.00  ? 1243 MET D CE    1 
ATOM   8878  N  N     . ARG B  1  445 ? -25.529 53.542  58.493 1.00 28.92  ? 1244 ARG D N     1 
ATOM   8879  C  CA    . ARG B  1  445 ? -24.931 54.422  59.433 1.00 32.67  ? 1244 ARG D CA    1 
ATOM   8880  C  C     . ARG B  1  445 ? -23.845 53.767  60.265 1.00 31.58  ? 1244 ARG D C     1 
ATOM   8881  O  O     . ARG B  1  445 ? -23.886 52.605  60.500 1.00 28.01  ? 1244 ARG D O     1 
ATOM   8882  C  CB    . ARG B  1  445 ? -25.996 55.024  60.358 1.00 34.10  ? 1244 ARG D CB    1 
ATOM   8883  C  CG    . ARG B  1  445 ? -26.706 56.219  59.769 1.00 38.60  ? 1244 ARG D CG    1 
ATOM   8884  C  CD    . ARG B  1  445 ? -27.568 56.897  60.791 1.00 37.81  ? 1244 ARG D CD    1 
ATOM   8885  N  NE    . ARG B  1  445 ? -28.223 58.039  60.212 1.00 37.70  ? 1244 ARG D NE    1 
ATOM   8886  C  CZ    . ARG B  1  445 ? -29.151 58.765  60.832 1.00 37.15  ? 1244 ARG D CZ    1 
ATOM   8887  N  NH1   . ARG B  1  445 ? -29.502 58.498  62.091 1.00 30.37  ? 1244 ARG D NH1   1 
ATOM   8888  N  NH2   . ARG B  1  445 ? -29.685 59.802  60.186 1.00 35.71  ? 1244 ARG D NH2   1 
ATOM   8889  N  N     A SER B  1  446 ? -22.919 54.561  60.754 0.50 29.37  ? 1245 SER D N     1 
ATOM   8890  N  N     B SER B  1  446 ? -22.865 54.537  60.725 0.50 30.23  ? 1245 SER D N     1 
ATOM   8891  C  CA    A SER B  1  446 ? -21.931 54.089  61.683 0.50 29.37  ? 1245 SER D CA    1 
ATOM   8892  C  CA    B SER B  1  446 ? -21.852 54.075  61.675 0.50 30.87  ? 1245 SER D CA    1 
ATOM   8893  C  C     A SER B  1  446 ? -22.651 53.813  62.986 0.50 31.37  ? 1245 SER D C     1 
ATOM   8894  C  C     B SER B  1  446 ? -22.593 53.822  62.986 0.50 32.50  ? 1245 SER D C     1 
ATOM   8895  O  O     A SER B  1  446 ? -23.721 54.406  63.236 0.50 30.68  ? 1245 SER D O     1 
ATOM   8896  O  O     B SER B  1  446 ? -23.636 54.427  63.239 0.50 32.69  ? 1245 SER D O     1 
ATOM   8897  C  CB    A SER B  1  446 ? -20.938 55.207  61.916 0.50 27.98  ? 1245 SER D CB    1 
ATOM   8898  C  CB    B SER B  1  446 ? -20.851 55.207  61.914 0.50 30.24  ? 1245 SER D CB    1 
ATOM   8899  O  OG    A SER B  1  446 ? -20.251 55.491  60.722 0.50 24.50  ? 1245 SER D OG    1 
ATOM   8900  O  OG    B SER B  1  446 ? -21.526 56.306  62.485 0.50 28.40  ? 1245 SER D OG    1 
ATOM   8901  N  N     . ARG B  1  447 ? -22.116 52.908  63.797 1.00 29.16  ? 1246 ARG D N     1 
ATOM   8902  C  CA    . ARG B  1  447 ? -22.596 52.844  65.171 1.00 29.52  ? 1246 ARG D CA    1 
ATOM   8903  C  C     . ARG B  1  447 ? -21.937 53.908  66.017 1.00 30.41  ? 1246 ARG D C     1 
ATOM   8904  O  O     . ARG B  1  447 ? -20.710 53.855  66.224 1.00 31.44  ? 1246 ARG D O     1 
ATOM   8905  C  CB    . ARG B  1  447 ? -22.349 51.489  65.771 1.00 25.43  ? 1246 ARG D CB    1 
ATOM   8906  C  CG    . ARG B  1  447 ? -22.904 51.322  67.199 1.00 22.69  ? 1246 ARG D CG    1 
ATOM   8907  C  CD    . ARG B  1  447 ? -22.972 49.862  67.649 1.00 22.51  ? 1246 ARG D CD    1 
ATOM   8908  N  NE    . ARG B  1  447 ? -23.934 49.062  66.865 1.00 25.67  ? 1246 ARG D NE    1 
ATOM   8909  C  CZ    . ARG B  1  447 ? -25.255 49.061  67.089 1.00 27.90  ? 1246 ARG D CZ    1 
ATOM   8910  N  NH1   . ARG B  1  447 ? -25.788 49.831  68.042 1.00 27.92  ? 1246 ARG D NH1   1 
ATOM   8911  N  NH2   . ARG B  1  447 ? -26.054 48.267  66.401 1.00 26.40  ? 1246 ARG D NH2   1 
ATOM   8912  N  N     . ALA B  1  448 ? -22.712 54.901  66.460 1.00 29.12  ? 1247 ALA D N     1 
ATOM   8913  C  CA    . ALA B  1  448 ? -22.187 55.971  67.259 1.00 30.92  ? 1247 ALA D CA    1 
ATOM   8914  C  C     . ALA B  1  448 ? -23.034 56.172  68.508 1.00 35.62  ? 1247 ALA D C     1 
ATOM   8915  O  O     . ALA B  1  448 ? -24.279 55.952  68.510 1.00 36.48  ? 1247 ALA D O     1 
ATOM   8916  C  CB    . ALA B  1  448 ? -22.101 57.242  66.454 1.00 30.45  ? 1247 ALA D CB    1 
ATOM   8917  N  N     . VAL B  1  449 ? -22.372 56.557  69.602 1.00 33.05  ? 1248 VAL D N     1 
ATOM   8918  C  CA    . VAL B  1  449 ? -23.087 56.860  70.853 1.00 32.11  ? 1248 VAL D CA    1 
ATOM   8919  C  C     . VAL B  1  449 ? -22.566 58.152  71.437 1.00 34.37  ? 1248 VAL D C     1 
ATOM   8920  O  O     . VAL B  1  449 ? -21.426 58.531  71.165 1.00 30.21  ? 1248 VAL D O     1 
ATOM   8921  C  CB    . VAL B  1  449 ? -22.977 55.755  71.907 1.00 30.99  ? 1248 VAL D CB    1 
ATOM   8922  C  CG1   . VAL B  1  449 ? -23.536 54.433  71.385 1.00 34.15  ? 1248 VAL D CG1   1 
ATOM   8923  C  CG2   . VAL B  1  449 ? -21.564 55.612  72.489 1.00 29.38  ? 1248 VAL D CG2   1 
ATOM   8924  N  N     . ILE B  1  450 ? -23.383 58.814  72.247 1.00 34.21  ? 1249 ILE D N     1 
ATOM   8925  C  CA    . ILE B  1  450 ? -22.919 60.013  72.940 1.00 30.66  ? 1249 ILE D CA    1 
ATOM   8926  C  C     . ILE B  1  450 ? -22.629 59.610  74.376 1.00 29.59  ? 1249 ILE D C     1 
ATOM   8927  O  O     . ILE B  1  450 ? -23.497 58.998  75.044 1.00 28.41  ? 1249 ILE D O     1 
ATOM   8928  C  CB    . ILE B  1  450 ? -23.989 61.123  72.852 1.00 31.01  ? 1249 ILE D CB    1 
ATOM   8929  C  CG1   . ILE B  1  450 ? -23.986 61.711  71.431 1.00 29.66  ? 1249 ILE D CG1   1 
ATOM   8930  C  CG2   . ILE B  1  450 ? -23.680 62.228  73.840 1.00 26.25  ? 1249 ILE D CG2   1 
ATOM   8931  C  CD1   . ILE B  1  450 ? -25.349 61.904  70.805 1.00 37.45  ? 1249 ILE D CD1   1 
ATOM   8932  N  N     . GLU B  1  451 ? -21.448 59.949  74.873 1.00 29.86  ? 1250 GLU D N     1 
ATOM   8933  C  CA    . GLU B  1  451 ? -21.151 59.664  76.280 1.00 33.61  ? 1250 GLU D CA    1 
ATOM   8934  C  C     . GLU B  1  451 ? -20.413 60.794  76.968 1.00 34.52  ? 1250 GLU D C     1 
ATOM   8935  O  O     . GLU B  1  451 ? -19.785 61.591  76.296 1.00 34.12  ? 1250 GLU D O     1 
ATOM   8936  C  CB    . GLU B  1  451 ? -20.354 58.360  76.410 1.00 33.53  ? 1250 GLU D CB    1 
ATOM   8937  C  CG    . GLU B  1  451 ? -18.945 58.457  75.915 1.00 30.88  ? 1250 GLU D CG    1 
ATOM   8938  C  CD    . GLU B  1  451 ? -18.171 57.146  76.004 1.00 34.06  ? 1250 GLU D CD    1 
ATOM   8939  O  OE1   . GLU B  1  451 ? -18.777 56.052  76.047 1.00 35.79  ? 1250 GLU D OE1   1 
ATOM   8940  O  OE2   . GLU B  1  451 ? -16.936 57.189  75.990 1.00 31.90  ? 1250 GLU D OE2   1 
ATOM   8941  N  N     . GLU B  1  452 ? -20.510 60.859  78.297 1.00 34.74  ? 1251 GLU D N     1 
ATOM   8942  C  CA    . GLU B  1  452 ? -19.768 61.847  79.081 1.00 35.14  ? 1251 GLU D CA    1 
ATOM   8943  C  C     . GLU B  1  452 ? -18.273 61.574  79.070 1.00 38.29  ? 1251 GLU D C     1 
ATOM   8944  O  O     . GLU B  1  452 ? -17.845 60.406  79.035 1.00 36.00  ? 1251 GLU D O     1 
ATOM   8945  C  CB    . GLU B  1  452 ? -20.258 61.881  80.521 1.00 36.60  ? 1251 GLU D CB    1 
ATOM   8946  C  CG    . GLU B  1  452 ? -20.125 60.553  81.280 1.00 40.97  ? 1251 GLU D CG    1 
ATOM   8947  C  CD    . GLU B  1  452 ? -21.125 60.489  82.411 1.00 45.91  ? 1251 GLU D CD    1 
ATOM   8948  O  OE1   . GLU B  1  452 ? -22.236 59.954  82.196 1.00 44.86  ? 1251 GLU D OE1   1 
ATOM   8949  O  OE2   . GLU B  1  452 ? -20.811 61.034  83.485 1.00 51.04  ? 1251 GLU D OE2   1 
ATOM   8950  N  N     . ARG B  1  453 ? -17.476 62.638  79.077 1.00 39.58  ? 1252 ARG D N     1 
ATOM   8951  C  CA    . ARG B  1  453 ? -16.011 62.460  79.140 1.00 42.50  ? 1252 ARG D CA    1 
ATOM   8952  C  C     . ARG B  1  453 ? -15.493 63.128  80.402 1.00 45.83  ? 1252 ARG D C     1 
ATOM   8953  O  O     . ARG B  1  453 ? -14.299 63.173  80.635 1.00 49.47  ? 1252 ARG D O     1 
ATOM   8954  C  CB    . ARG B  1  453 ? -15.298 62.993  77.892 1.00 39.03  ? 1252 ARG D CB    1 
ATOM   8955  C  CG    . ARG B  1  453 ? -15.609 64.450  77.541 1.00 37.52  ? 1252 ARG D CG    1 
ATOM   8956  C  CD    . ARG B  1  453 ? -14.990 64.731  76.168 1.00 40.67  ? 1252 ARG D CD    1 
ATOM   8957  N  NE    . ARG B  1  453 ? -15.282 66.082  75.701 1.00 45.18  ? 1252 ARG D NE    1 
ATOM   8958  C  CZ    . ARG B  1  453 ? -14.441 67.113  75.790 1.00 47.08  ? 1252 ARG D CZ    1 
ATOM   8959  N  NH1   . ARG B  1  453 ? -13.237 66.958  76.336 1.00 45.95  ? 1252 ARG D NH1   1 
ATOM   8960  N  NH2   . ARG B  1  453 ? -14.807 68.295  75.302 1.00 47.29  ? 1252 ARG D NH2   1 
ATOM   8961  N  N     . GLY B  1  454 ? -16.405 63.640  81.218 1.00 48.54  ? 1253 GLY D N     1 
ATOM   8962  C  CA    . GLY B  1  454 ? -15.991 64.301  82.463 1.00 49.82  ? 1253 GLY D CA    1 
ATOM   8963  C  C     . GLY B  1  454 ? -16.010 65.828  82.355 1.00 54.70  ? 1253 GLY D C     1 
ATOM   8964  O  O     . GLY B  1  454 ? -15.852 66.390  81.278 1.00 53.27  ? 1253 GLY D O     1 
ATOM   8965  N  N     . GLY B  1  455 ? -16.197 66.491  83.488 1.00 51.53  ? 1254 GLY D N     1 
ATOM   8966  C  CA    . GLY B  1  455 ? -16.241 67.929  83.541 1.00 50.33  ? 1254 GLY D CA    1 
ATOM   8967  C  C     . GLY B  1  455 ? -17.539 68.504  83.036 1.00 51.72  ? 1254 GLY D C     1 
ATOM   8968  O  O     . GLY B  1  455 ? -17.626 69.704  82.806 1.00 53.36  ? 1254 GLY D O     1 
ATOM   8969  N  N     . GLY B  1  456 ? -18.548 67.662  82.821 1.00 49.34  ? 1255 GLY D N     1 
ATOM   8970  C  CA    . GLY B  1  456 ? -19.782 68.116  82.200 1.00 44.53  ? 1255 GLY D CA    1 
ATOM   8971  C  C     . GLY B  1  456 ? -19.655 68.128  80.678 1.00 44.83  ? 1255 GLY D C     1 
ATOM   8972  O  O     . GLY B  1  456 ? -20.605 68.442  79.973 1.00 45.44  ? 1255 GLY D O     1 
ATOM   8973  N  N     . ARG B  1  457 ? -18.474 67.780  80.176 1.00 41.64  ? 1256 ARG D N     1 
ATOM   8974  C  CA    . ARG B  1  457 ? -18.284 67.675  78.746 1.00 47.21  ? 1256 ARG D CA    1 
ATOM   8975  C  C     . ARG B  1  457 ? -18.733 66.293  78.184 1.00 47.22  ? 1256 ARG D C     1 
ATOM   8976  O  O     . ARG B  1  457 ? -18.910 65.312  78.936 1.00 42.77  ? 1256 ARG D O     1 
ATOM   8977  C  CB    . ARG B  1  457 ? -16.828 67.930  78.401 1.00 48.01  ? 1256 ARG D CB    1 
ATOM   8978  C  CG    . ARG B  1  457 ? -16.478 69.409  78.403 1.00 59.88  ? 1256 ARG D CG    1 
ATOM   8979  C  CD    . ARG B  1  457 ? -14.992 69.667  78.227 1.00 65.03  ? 1256 ARG D CD    1 
ATOM   8980  N  NE    . ARG B  1  457 ? -14.344 69.480  79.519 1.00 79.42  ? 1256 ARG D NE    1 
ATOM   8981  C  CZ    . ARG B  1  457 ? -13.945 70.469  80.303 1.00 79.17  ? 1256 ARG D CZ    1 
ATOM   8982  N  NH1   . ARG B  1  457 ? -14.089 71.726  79.906 1.00 78.56  ? 1256 ARG D NH1   1 
ATOM   8983  N  NH2   . ARG B  1  457 ? -13.384 70.199  81.472 1.00 87.62  ? 1256 ARG D NH2   1 
ATOM   8984  N  N     . GLN B  1  458 ? -18.901 66.217  76.867 1.00 43.90  ? 1257 GLN D N     1 
ATOM   8985  C  CA    . GLN B  1  458 ? -19.301 64.985  76.216 1.00 40.74  ? 1257 GLN D CA    1 
ATOM   8986  C  C     . GLN B  1  458 ? -18.486 64.721  74.975 1.00 40.98  ? 1257 GLN D C     1 
ATOM   8987  O  O     . GLN B  1  458 ? -17.799 65.607  74.466 1.00 34.26  ? 1257 GLN D O     1 
ATOM   8988  C  CB    . GLN B  1  458 ? -20.756 65.064  75.799 1.00 39.66  ? 1257 GLN D CB    1 
ATOM   8989  C  CG    . GLN B  1  458 ? -21.756 64.903  76.932 1.00 40.76  ? 1257 GLN D CG    1 
ATOM   8990  C  CD    . GLN B  1  458 ? -23.177 65.149  76.463 1.00 43.95  ? 1257 GLN D CD    1 
ATOM   8991  O  OE1   . GLN B  1  458 ? -23.444 66.132  75.756 1.00 52.05  ? 1257 GLN D OE1   1 
ATOM   8992  N  NE2   . GLN B  1  458 ? -24.106 64.293  76.888 1.00 40.06  ? 1257 GLN D NE2   1 
ATOM   8993  N  N     . ARG B  1  459 ? -18.605 63.497  74.474 1.00 34.74  ? 1258 ARG D N     1 
ATOM   8994  C  CA    . ARG B  1  459 ? -17.957 63.102  73.233 1.00 34.45  ? 1258 ARG D CA    1 
ATOM   8995  C  C     . ARG B  1  459 ? -18.872 62.197  72.424 1.00 36.63  ? 1258 ARG D C     1 
ATOM   8996  O  O     . ARG B  1  459 ? -19.784 61.574  72.963 1.00 39.17  ? 1258 ARG D O     1 
ATOM   8997  C  CB    . ARG B  1  459 ? -16.628 62.389  73.511 1.00 30.84  ? 1258 ARG D CB    1 
ATOM   8998  C  CG    . ARG B  1  459 ? -16.748 61.114  74.309 1.00 31.00  ? 1258 ARG D CG    1 
ATOM   8999  C  CD    . ARG B  1  459 ? -15.389 60.576  74.645 1.00 36.77  ? 1258 ARG D CD    1 
ATOM   9000  N  NE    . ARG B  1  459 ? -15.402 59.628  75.748 1.00 41.18  ? 1258 ARG D NE    1 
ATOM   9001  C  CZ    . ARG B  1  459 ? -14.419 59.497  76.625 1.00 42.27  ? 1258 ARG D CZ    1 
ATOM   9002  N  NH1   . ARG B  1  459 ? -13.347 60.245  76.553 1.00 41.62  ? 1258 ARG D NH1   1 
ATOM   9003  N  NH2   . ARG B  1  459 ? -14.501 58.580  77.561 1.00 47.77  ? 1258 ARG D NH2   1 
ATOM   9004  N  N     . ILE B  1  460 ? -18.604 62.087  71.132 1.00 35.13  ? 1259 ILE D N     1 
ATOM   9005  C  CA    . ILE B  1  460 ? -19.281 61.129  70.299 1.00 31.74  ? 1259 ILE D CA    1 
ATOM   9006  C  C     . ILE B  1  460 ? -18.265 60.017  70.034 1.00 33.28  ? 1259 ILE D C     1 
ATOM   9007  O  O     . ILE B  1  460 ? -17.120 60.283  69.693 1.00 33.35  ? 1259 ILE D O     1 
ATOM   9008  C  CB    . ILE B  1  460 ? -19.740 61.769  68.972 1.00 31.31  ? 1259 ILE D CB    1 
ATOM   9009  C  CG1   . ILE B  1  460 ? -20.865 62.754  69.210 1.00 32.01  ? 1259 ILE D CG1   1 
ATOM   9010  C  CG2   . ILE B  1  460 ? -20.264 60.737  68.002 1.00 32.22  ? 1259 ILE D CG2   1 
ATOM   9011  C  CD1   . ILE B  1  460 ? -20.961 63.815  68.149 1.00 29.16  ? 1259 ILE D CD1   1 
ATOM   9012  N  N     . VAL B  1  461 ? -18.700 58.771  70.190 1.00 32.15  ? 1260 VAL D N     1 
ATOM   9013  C  CA    . VAL B  1  461 ? -17.796 57.626  70.027 1.00 30.21  ? 1260 VAL D CA    1 
ATOM   9014  C  C     . VAL B  1  461 ? -18.334 56.727  68.964 1.00 27.74  ? 1260 VAL D C     1 
ATOM   9015  O  O     . VAL B  1  461 ? -19.480 56.228  69.090 1.00 24.98  ? 1260 VAL D O     1 
ATOM   9016  C  CB    . VAL B  1  461 ? -17.606 56.800  71.326 1.00 32.05  ? 1260 VAL D CB    1 
ATOM   9017  C  CG1   . VAL B  1  461 ? -16.622 55.662  71.064 1.00 33.07  ? 1260 VAL D CG1   1 
ATOM   9018  C  CG2   . VAL B  1  461 ? -17.036 57.645  72.411 1.00 27.44  ? 1260 VAL D CG2   1 
ATOM   9019  N  N     . VAL B  1  462 ? -17.533 56.501  67.914 1.00 28.19  ? 1261 VAL D N     1 
ATOM   9020  C  CA    . VAL B  1  462 ? -17.975 55.689  66.779 1.00 26.38  ? 1261 VAL D CA    1 
ATOM   9021  C  C     . VAL B  1  462 ? -17.236 54.369  66.861 1.00 28.25  ? 1261 VAL D C     1 
ATOM   9022  O  O     . VAL B  1  462 ? -16.019 54.358  66.857 1.00 28.23  ? 1261 VAL D O     1 
ATOM   9023  C  CB    . VAL B  1  462 ? -17.648 56.366  65.467 1.00 28.32  ? 1261 VAL D CB    1 
ATOM   9024  C  CG1   . VAL B  1  462 ? -18.029 55.473  64.259 1.00 25.07  ? 1261 VAL D CG1   1 
ATOM   9025  C  CG2   . VAL B  1  462 ? -18.352 57.706  65.388 1.00 29.42  ? 1261 VAL D CG2   1 
ATOM   9026  N  N     . THR B  1  463 ? -17.956 53.264  66.955 1.00 25.72  ? 1262 THR D N     1 
ATOM   9027  C  CA    . THR B  1  463 ? -17.316 51.942  67.104 1.00 27.82  ? 1262 THR D CA    1 
ATOM   9028  C  C     . THR B  1  463 ? -17.480 51.079  65.891 1.00 29.54  ? 1262 THR D C     1 
ATOM   9029  O  O     . THR B  1  463 ? -16.825 50.055  65.789 1.00 30.89  ? 1262 THR D O     1 
ATOM   9030  C  CB    . THR B  1  463 ? -17.840 51.173  68.329 1.00 28.87  ? 1262 THR D CB    1 
ATOM   9031  O  OG1   . THR B  1  463 ? -19.290 51.129  68.317 1.00 31.11  ? 1262 THR D OG1   1 
ATOM   9032  C  CG2   . THR B  1  463 ? -17.364 51.824  69.597 1.00 24.90  ? 1262 THR D CG2   1 
ATOM   9033  N  N     . GLU B  1  464 ? -18.292 51.499  64.928 1.00 30.42  ? 1263 GLU D N     1 
ATOM   9034  C  CA    . GLU B  1  464 ? -18.471 50.748  63.670 1.00 26.00  ? 1263 GLU D CA    1 
ATOM   9035  C  C     . GLU B  1  464 ? -18.739 51.774  62.582 1.00 31.74  ? 1263 GLU D C     1 
ATOM   9036  O  O     . GLU B  1  464 ? -19.400 52.791  62.821 1.00 28.88  ? 1263 GLU D O     1 
ATOM   9037  C  CB    . GLU B  1  464 ? -19.719 49.840  63.768 1.00 26.55  ? 1263 GLU D CB    1 
ATOM   9038  C  CG    . GLU B  1  464 ? -19.651 48.829  64.903 1.00 26.62  ? 1263 GLU D CG    1 
ATOM   9039  C  CD    . GLU B  1  464 ? -20.964 48.102  65.170 1.00 33.02  ? 1263 GLU D CD    1 
ATOM   9040  O  OE1   . GLU B  1  464 ? -20.928 47.291  66.102 1.00 38.28  ? 1263 GLU D OE1   1 
ATOM   9041  O  OE2   . GLU B  1  464 ? -22.014 48.285  64.492 1.00 29.78  ? 1263 GLU D OE2   1 
ATOM   9042  N  N     . ILE B  1  465 ? -18.214 51.503  61.378 1.00 34.14  ? 1264 ILE D N     1 
ATOM   9043  C  CA    . ILE B  1  465 ? -18.420 52.412  60.262 1.00 34.28  ? 1264 ILE D CA    1 
ATOM   9044  C  C     . ILE B  1  465 ? -19.064 51.710  59.090 1.00 33.32  ? 1264 ILE D C     1 
ATOM   9045  O  O     . ILE B  1  465 ? -19.053 50.509  59.040 1.00 36.49  ? 1264 ILE D O     1 
ATOM   9046  C  CB    . ILE B  1  465 ? -17.095 53.079  59.843 1.00 39.06  ? 1264 ILE D CB    1 
ATOM   9047  C  CG1   . ILE B  1  465 ? -16.107 52.029  59.392 1.00 38.02  ? 1264 ILE D CG1   1 
ATOM   9048  C  CG2   . ILE B  1  465 ? -16.500 53.883  61.006 1.00 38.34  ? 1264 ILE D CG2   1 
ATOM   9049  C  CD1   . ILE B  1  465 ? -14.887 52.627  58.780 1.00 40.90  ? 1264 ILE D CD1   1 
ATOM   9050  N  N     . PRO B  1  466 ? -19.644 52.455  58.143 1.00 36.04  ? 1265 PRO D N     1 
ATOM   9051  C  CA    . PRO B  1  466 ? -20.342 51.833  57.004 1.00 33.97  ? 1265 PRO D CA    1 
ATOM   9052  C  C     . PRO B  1  466 ? -19.380 51.029  56.112 1.00 31.52  ? 1265 PRO D C     1 
ATOM   9053  O  O     . PRO B  1  466 ? -18.186 51.289  56.076 1.00 30.96  ? 1265 PRO D O     1 
ATOM   9054  C  CB    . PRO B  1  466 ? -20.905 53.033  56.234 1.00 32.32  ? 1265 PRO D CB    1 
ATOM   9055  C  CG    . PRO B  1  466 ? -20.998 54.115  57.282 1.00 36.69  ? 1265 PRO D CG    1 
ATOM   9056  C  CD    . PRO B  1  466 ? -19.785 53.930  58.130 1.00 34.50  ? 1265 PRO D CD    1 
ATOM   9057  N  N     . PHE B  1  467 ? -19.949 50.065  55.420 1.00 29.48  ? 1266 PHE D N     1 
ATOM   9058  C  CA    . PHE B  1  467 ? -19.260 49.128  54.559 1.00 29.90  ? 1266 PHE D CA    1 
ATOM   9059  C  C     . PHE B  1  467 ? -18.531 49.831  53.434 1.00 33.53  ? 1266 PHE D C     1 
ATOM   9060  O  O     . PHE B  1  467 ? -19.097 50.631  52.725 1.00 35.88  ? 1266 PHE D O     1 
ATOM   9061  C  CB    . PHE B  1  467 ? -20.272 48.129  53.974 1.00 28.59  ? 1266 PHE D CB    1 
ATOM   9062  C  CG    . PHE B  1  467 ? -19.643 47.053  53.127 1.00 30.35  ? 1266 PHE D CG    1 
ATOM   9063  C  CD1   . PHE B  1  467 ? -18.540 46.333  53.587 1.00 29.33  ? 1266 PHE D CD1   1 
ATOM   9064  C  CD2   . PHE B  1  467 ? -20.141 46.775  51.869 1.00 28.53  ? 1266 PHE D CD2   1 
ATOM   9065  C  CE1   . PHE B  1  467 ? -17.951 45.354  52.773 1.00 29.82  ? 1266 PHE D CE1   1 
ATOM   9066  C  CE2   . PHE B  1  467 ? -19.594 45.801  51.071 1.00 29.37  ? 1266 PHE D CE2   1 
ATOM   9067  C  CZ    . PHE B  1  467 ? -18.488 45.065  51.521 1.00 28.80  ? 1266 PHE D CZ    1 
ATOM   9068  N  N     . GLN B  1  468 ? -17.264 49.493  53.270 1.00 31.74  ? 1267 GLN D N     1 
ATOM   9069  C  CA    . GLN B  1  468 ? -16.403 50.075  52.245 1.00 33.27  ? 1267 GLN D CA    1 
ATOM   9070  C  C     . GLN B  1  468 ? -15.994 51.549  52.445 1.00 35.78  ? 1267 GLN D C     1 
ATOM   9071  O  O     . GLN B  1  468 ? -15.383 52.128  51.555 1.00 34.73  ? 1267 GLN D O     1 
ATOM   9072  C  CB    . GLN B  1  468 ? -16.973 49.892  50.859 1.00 33.98  ? 1267 GLN D CB    1 
ATOM   9073  C  CG    . GLN B  1  468 ? -17.122 48.452  50.432 1.00 36.21  ? 1267 GLN D CG    1 
ATOM   9074  C  CD    . GLN B  1  468 ? -17.868 48.326  49.117 1.00 47.80  ? 1267 GLN D CD    1 
ATOM   9075  O  OE1   . GLN B  1  468 ? -18.895 49.005  48.875 1.00 51.38  ? 1267 GLN D OE1   1 
ATOM   9076  N  NE2   . GLN B  1  468 ? -17.378 47.442  48.255 1.00 49.16  ? 1267 GLN D NE2   1 
ATOM   9077  N  N     . VAL B  1  469 ? -16.272 52.126  53.606 1.00 34.99  ? 1268 VAL D N     1 
ATOM   9078  C  CA    . VAL B  1  469 ? -15.800 53.487  53.896 1.00 34.08  ? 1268 VAL D CA    1 
ATOM   9079  C  C     . VAL B  1  469 ? -14.383 53.427  54.454 1.00 35.38  ? 1268 VAL D C     1 
ATOM   9080  O  O     . VAL B  1  469 ? -14.095 52.635  55.377 1.00 36.00  ? 1268 VAL D O     1 
ATOM   9081  C  CB    . VAL B  1  469 ? -16.781 54.181  54.842 1.00 31.95  ? 1268 VAL D CB    1 
ATOM   9082  C  CG1   . VAL B  1  469 ? -16.169 55.394  55.501 1.00 31.34  ? 1268 VAL D CG1   1 
ATOM   9083  C  CG2   . VAL B  1  469 ? -18.109 54.499  54.117 1.00 27.22  ? 1268 VAL D CG2   1 
ATOM   9084  N  N     . ASN B  1  470 ? -13.509 54.267  53.933 1.00 35.27  ? 1269 ASN D N     1 
ATOM   9085  C  CA    . ASN B  1  470 ? -12.131 54.305  54.451 1.00 35.01  ? 1269 ASN D CA    1 
ATOM   9086  C  C     . ASN B  1  470 ? -12.134 55.139  55.746 1.00 35.49  ? 1269 ASN D C     1 
ATOM   9087  O  O     . ASN B  1  470 ? -12.499 56.306  55.711 1.00 38.15  ? 1269 ASN D O     1 
ATOM   9088  C  CB    . ASN B  1  470 ? -11.197 54.874  53.403 1.00 31.13  ? 1269 ASN D CB    1 
ATOM   9089  C  CG    . ASN B  1  470 ? -9.792  55.072  53.918 1.00 35.10  ? 1269 ASN D CG    1 
ATOM   9090  O  OD1   . ASN B  1  470 ? -9.540  55.505  55.074 1.00 36.65  ? 1269 ASN D OD1   1 
ATOM   9091  N  ND2   . ASN B  1  470 ? -8.862  54.766  53.070 1.00 30.19  ? 1269 ASN D ND2   1 
ATOM   9092  N  N     . LYS B  1  471 ? -11.766 54.508  56.866 1.00 33.69  ? 1270 LYS D N     1 
ATOM   9093  C  CA    . LYS B  1  471 ? -11.784 55.168  58.188 1.00 33.11  ? 1270 LYS D CA    1 
ATOM   9094  C  C     . LYS B  1  471 ? -10.957 56.455  58.240 1.00 35.55  ? 1270 LYS D C     1 
ATOM   9095  O  O     . LYS B  1  471 ? -11.496 57.516  58.540 1.00 35.75  ? 1270 LYS D O     1 
ATOM   9096  C  CB    . LYS B  1  471 ? -11.313 54.202  59.273 1.00 30.79  ? 1270 LYS D CB    1 
ATOM   9097  C  CG    . LYS B  1  471 ? -11.384 54.795  60.688 1.00 30.64  ? 1270 LYS D CG    1 
ATOM   9098  C  CD    . LYS B  1  471 ? -11.253 53.724  61.763 1.00 31.51  ? 1270 LYS D CD    1 
ATOM   9099  C  CE    . LYS B  1  471 ? -10.030 52.804  61.600 1.00 33.84  ? 1270 LYS D CE    1 
ATOM   9100  N  NZ    . LYS B  1  471 ? -8.769  53.570  61.837 1.00 38.97  ? 1270 LYS D NZ    1 
ATOM   9101  N  N     . ALA B  1  472 ? -9.674  56.346  57.899 1.00 33.42  ? 1271 ALA D N     1 
ATOM   9102  C  CA    . ALA B  1  472 ? -8.778  57.497  57.890 1.00 34.17  ? 1271 ALA D CA    1 
ATOM   9103  C  C     . ALA B  1  472 ? -9.325  58.615  57.008 1.00 37.47  ? 1271 ALA D C     1 
ATOM   9104  O  O     . ALA B  1  472 ? -9.288  59.781  57.395 1.00 43.16  ? 1271 ALA D O     1 
ATOM   9105  C  CB    . ALA B  1  472 ? -7.386  57.120  57.429 1.00 28.84  ? 1271 ALA D CB    1 
ATOM   9106  N  N     . ARG B  1  473 ? -9.858  58.274  55.844 1.00 38.78  ? 1272 ARG D N     1 
ATOM   9107  C  CA    . ARG B  1  473 ? -10.397 59.269  54.946 1.00 42.02  ? 1272 ARG D CA    1 
ATOM   9108  C  C     . ARG B  1  473 ? -11.611 59.938  55.545 1.00 42.15  ? 1272 ARG D C     1 
ATOM   9109  O  O     . ARG B  1  473 ? -11.794 61.150  55.396 1.00 47.02  ? 1272 ARG D O     1 
ATOM   9110  C  CB    . ARG B  1  473 ? -10.719 58.671  53.572 1.00 49.43  ? 1272 ARG D CB    1 
ATOM   9111  C  CG    . ARG B  1  473 ? -11.186 59.725  52.583 1.00 58.13  ? 1272 ARG D CG    1 
ATOM   9112  C  CD    . ARG B  1  473 ? -11.582 59.191  51.208 1.00 76.04  ? 1272 ARG D CD    1 
ATOM   9113  N  NE    . ARG B  1  473 ? -10.448 58.563  50.520 1.00 85.09  ? 1272 ARG D NE    1 
ATOM   9114  C  CZ    . ARG B  1  473 ? -10.359 57.268  50.202 1.00 82.15  ? 1272 ARG D CZ    1 
ATOM   9115  N  NH1   . ARG B  1  473 ? -11.355 56.418  50.441 1.00 72.17  ? 1272 ARG D NH1   1 
ATOM   9116  N  NH2   . ARG B  1  473 ? -9.261  56.841  49.602 1.00 88.40  ? 1272 ARG D NH2   1 
ATOM   9117  N  N     . MET B  1  474 ? -12.440 59.165  56.232 1.00 41.32  ? 1273 MET D N     1 
ATOM   9118  C  CA    . MET B  1  474 ? -13.641 59.715  56.877 1.00 39.24  ? 1273 MET D CA    1 
ATOM   9119  C  C     . MET B  1  474 ? -13.237 60.721  57.950 1.00 38.41  ? 1273 MET D C     1 
ATOM   9120  O  O     . MET B  1  474 ? -13.872 61.761  58.103 1.00 36.44  ? 1273 MET D O     1 
ATOM   9121  C  CB    . MET B  1  474 ? -14.478 58.602  57.476 1.00 36.50  ? 1273 MET D CB    1 
ATOM   9122  C  CG    . MET B  1  474 ? -15.775 59.088  58.097 1.00 38.43  ? 1273 MET D CG    1 
ATOM   9123  S  SD    . MET B  1  474 ? -16.443 57.798  59.157 1.00 51.13  ? 1273 MET D SD    1 
ATOM   9124  C  CE    . MET B  1  474 ? -15.328 58.115  60.594 1.00 37.20  ? 1273 MET D CE    1 
ATOM   9125  N  N     . ILE B  1  475 ? -12.175 60.398  58.674 1.00 32.05  ? 1274 ILE D N     1 
ATOM   9126  C  CA    . ILE B  1  475 ? -11.676 61.268  59.717 1.00 40.30  ? 1274 ILE D CA    1 
ATOM   9127  C  C     . ILE B  1  475 ? -11.089 62.563  59.123 1.00 41.25  ? 1274 ILE D C     1 
ATOM   9128  O  O     . ILE B  1  475 ? -11.359 63.639  59.620 1.00 43.40  ? 1274 ILE D O     1 
ATOM   9129  C  CB    . ILE B  1  475 ? -10.693 60.536  60.641 1.00 37.09  ? 1274 ILE D CB    1 
ATOM   9130  C  CG1   . ILE B  1  475 ? -11.396 59.404  61.354 1.00 34.74  ? 1274 ILE D CG1   1 
ATOM   9131  C  CG2   . ILE B  1  475 ? -10.083 61.511  61.630 1.00 33.86  ? 1274 ILE D CG2   1 
ATOM   9132  C  CD1   . ILE B  1  475 ? -10.425 58.492  62.105 1.00 32.68  ? 1274 ILE D CD1   1 
ATOM   9133  N  N     A GLU B  1  476 ? -10.380 62.441  58.006 0.50 43.96  ? 1275 GLU D N     1 
ATOM   9134  N  N     B GLU B  1  476 ? -10.315 62.501  58.054 0.50 42.59  ? 1275 GLU D N     1 
ATOM   9135  C  CA    A GLU B  1  476 ? -9.835  63.603  57.271 0.50 45.18  ? 1275 GLU D CA    1 
ATOM   9136  C  CA    B GLU B  1  476 ? -9.872  63.760  57.413 0.50 42.60  ? 1275 GLU D CA    1 
ATOM   9137  C  C     A GLU B  1  476 ? -10.962 64.562  56.865 0.50 44.05  ? 1275 GLU D C     1 
ATOM   9138  C  C     B GLU B  1  476 ? -11.008 64.627  56.883 0.50 42.48  ? 1275 GLU D C     1 
ATOM   9139  O  O     A GLU B  1  476 ? -10.830 65.777  56.944 0.50 47.64  ? 1275 GLU D O     1 
ATOM   9140  O  O     B GLU B  1  476 ? -10.903 65.844  56.835 0.50 45.80  ? 1275 GLU D O     1 
ATOM   9141  C  CB    A GLU B  1  476 ? -9.102  63.131  56.005 0.50 44.12  ? 1275 GLU D CB    1 
ATOM   9142  C  CB    B GLU B  1  476 ? -8.949  63.466  56.269 0.50 40.04  ? 1275 GLU D CB    1 
ATOM   9143  C  CG    A GLU B  1  476 ? -7.620  62.759  56.122 0.50 49.25  ? 1275 GLU D CG    1 
ATOM   9144  C  CG    B GLU B  1  476 ? -7.506  63.943  56.490 0.50 39.91  ? 1275 GLU D CG    1 
ATOM   9145  C  CD    A GLU B  1  476 ? -7.105  61.924  54.937 0.50 49.69  ? 1275 GLU D CD    1 
ATOM   9146  C  CD    B GLU B  1  476 ? -7.353  65.349  57.068 0.50 40.99  ? 1275 GLU D CD    1 
ATOM   9147  O  OE1   A GLU B  1  476 ? -7.558  62.161  53.783 0.50 50.50  ? 1275 GLU D OE1   1 
ATOM   9148  O  OE1   B GLU B  1  476 ? -6.702  65.447  58.128 0.50 42.35  ? 1275 GLU D OE1   1 
ATOM   9149  O  OE2   A GLU B  1  476 ? -6.239  61.036  55.157 0.50 46.56  ? 1275 GLU D OE2   1 
ATOM   9150  O  OE2   B GLU B  1  476 ? -7.857  66.360  56.496 0.50 41.54  ? 1275 GLU D OE2   1 
ATOM   9151  N  N     . LYS B  1  477 ? -12.066 63.975  56.429 1.00 41.20  ? 1276 LYS D N     1 
ATOM   9152  C  CA    . LYS B  1  477 ? -13.209 64.689  55.986 1.00 45.96  ? 1276 LYS D CA    1 
ATOM   9153  C  C     . LYS B  1  477 ? -13.818 65.512  57.124 1.00 47.49  ? 1276 LYS D C     1 
ATOM   9154  O  O     . LYS B  1  477 ? -14.166 66.677  56.927 1.00 48.48  ? 1276 LYS D O     1 
ATOM   9155  C  CB    . LYS B  1  477 ? -14.230 63.747  55.352 1.00 47.36  ? 1276 LYS D CB    1 
ATOM   9156  C  CG    . LYS B  1  477 ? -15.552 64.396  55.009 1.00 55.53  ? 1276 LYS D CG    1 
ATOM   9157  C  CD    . LYS B  1  477 ? -15.337 65.483  53.963 1.00 58.20  ? 1276 LYS D CD    1 
ATOM   9158  C  CE    . LYS B  1  477 ? -16.631 66.186  53.623 1.00 64.62  ? 1276 LYS D CE    1 
ATOM   9159  N  NZ    . LYS B  1  477 ? -16.504 66.825  52.284 1.00 69.42  ? 1276 LYS D NZ    1 
ATOM   9160  N  N     . ILE B  1  478 ? -13.901 64.905  58.295 1.00 43.33  ? 1277 ILE D N     1 
ATOM   9161  C  CA    . ILE B  1  478 ? -14.424 65.579  59.473 1.00 39.12  ? 1277 ILE D CA    1 
ATOM   9162  C  C     . ILE B  1  478 ? -13.465 66.725  59.831 1.00 43.09  ? 1277 ILE D C     1 
ATOM   9163  O  O     . ILE B  1  478 ? -13.922 67.816  60.145 1.00 38.45  ? 1277 ILE D O     1 
ATOM   9164  C  CB    . ILE B  1  478 ? -14.572 64.615  60.680 1.00 38.65  ? 1277 ILE D CB    1 
ATOM   9165  C  CG1   . ILE B  1  478 ? -15.493 63.433  60.317 1.00 39.30  ? 1277 ILE D CG1   1 
ATOM   9166  C  CG2   . ILE B  1  478 ? -15.068 65.343  61.913 1.00 36.95  ? 1277 ILE D CG2   1 
ATOM   9167  C  CD1   . ILE B  1  478 ? -15.803 62.487  61.442 1.00 39.01  ? 1277 ILE D CD1   1 
ATOM   9168  N  N     . ALA B  1  479 ? -12.147 66.458  59.809 1.00 35.62  ? 1278 ALA D N     1 
ATOM   9169  C  CA    . ALA B  1  479 ? -11.157 67.429  60.213 1.00 38.54  ? 1278 ALA D CA    1 
ATOM   9170  C  C     . ALA B  1  479 ? -11.213 68.632  59.298 1.00 48.47  ? 1278 ALA D C     1 
ATOM   9171  O  O     . ALA B  1  479 ? -11.081 69.764  59.772 1.00 48.14  ? 1278 ALA D O     1 
ATOM   9172  C  CB    . ALA B  1  479 ? -9.764  66.828  60.170 1.00 33.14  ? 1278 ALA D CB    1 
ATOM   9173  N  N     . GLU B  1  480 ? -11.388 68.373  57.989 1.00 51.97  ? 1279 GLU D N     1 
ATOM   9174  C  CA    . GLU B  1  480 ? -11.437 69.427  57.016 1.00 50.15  ? 1279 GLU D CA    1 
ATOM   9175  C  C     . GLU B  1  480 ? -12.681 70.314  57.239 1.00 52.51  ? 1279 GLU D C     1 
ATOM   9176  O  O     . GLU B  1  480 ? -12.603 71.518  57.132 1.00 48.85  ? 1279 GLU D O     1 
ATOM   9177  C  CB    . GLU B  1  480 ? -11.392 68.826  55.627 1.00 61.80  ? 1279 GLU D CB    1 
ATOM   9178  C  CG    . GLU B  1  480 ? -12.097 69.637  54.548 1.00 71.51  ? 1279 GLU D CG    1 
ATOM   9179  C  CD    . GLU B  1  480 ? -12.511 68.806  53.348 1.00 78.76  ? 1279 GLU D CD    1 
ATOM   9180  O  OE1   . GLU B  1  480 ? -13.702 68.907  52.939 1.00 73.28  ? 1279 GLU D OE1   1 
ATOM   9181  O  OE2   . GLU B  1  480 ? -11.640 68.059  52.818 1.00 83.18  ? 1279 GLU D OE2   1 
ATOM   9182  N  N     . LEU B  1  481 ? -13.821 69.701  57.530 1.00 47.81  ? 1280 LEU D N     1 
ATOM   9183  C  CA    . LEU B  1  481 ? -15.033 70.450  57.863 1.00 52.07  ? 1280 LEU D CA    1 
ATOM   9184  C  C     . LEU B  1  481 ? -14.859 71.359  59.083 1.00 56.29  ? 1280 LEU D C     1 
ATOM   9185  O  O     . LEU B  1  481 ? -15.317 72.483  59.090 1.00 56.15  ? 1280 LEU D O     1 
ATOM   9186  C  CB    . LEU B  1  481 ? -16.190 69.501  58.168 1.00 52.91  ? 1280 LEU D CB    1 
ATOM   9187  C  CG    . LEU B  1  481 ? -16.850 68.714  57.066 1.00 54.51  ? 1280 LEU D CG    1 
ATOM   9188  C  CD1   . LEU B  1  481 ? -18.012 67.922  57.655 1.00 53.25  ? 1280 LEU D CD1   1 
ATOM   9189  C  CD2   . LEU B  1  481 ? -17.305 69.700  55.995 1.00 55.17  ? 1280 LEU D CD2   1 
ATOM   9190  N  N     . VAL B  1  482 ? -14.198 70.838  60.116 1.00 54.94  ? 1281 VAL D N     1 
ATOM   9191  C  CA    . VAL B  1  482 ? -13.929 71.583  61.341 1.00 50.55  ? 1281 VAL D CA    1 
ATOM   9192  C  C     . VAL B  1  482 ? -12.981 72.738  61.015 1.00 58.10  ? 1281 VAL D C     1 
ATOM   9193  O  O     . VAL B  1  482 ? -13.181 73.845  61.477 1.00 63.47  ? 1281 VAL D O     1 
ATOM   9194  C  CB    . VAL B  1  482 ? -13.293 70.657  62.394 1.00 42.43  ? 1281 VAL D CB    1 
ATOM   9195  C  CG1   . VAL B  1  482 ? -12.496 71.390  63.434 1.00 39.35  ? 1281 VAL D CG1   1 
ATOM   9196  C  CG2   . VAL B  1  482 ? -14.335 69.733  63.000 1.00 39.23  ? 1281 VAL D CG2   1 
ATOM   9197  N  N     A ARG B  1  483 ? -11.964 72.455  60.214 0.50 57.29  ? 1282 ARG D N     1 
ATOM   9198  N  N     B ARG B  1  483 ? -11.959 72.441  60.221 0.50 59.57  ? 1282 ARG D N     1 
ATOM   9199  C  CA    A ARG B  1  483 ? -10.963 73.438  59.798 0.50 57.50  ? 1282 ARG D CA    1 
ATOM   9200  C  CA    B ARG B  1  483 ? -10.969 73.429  59.806 0.50 61.15  ? 1282 ARG D CA    1 
ATOM   9201  C  C     A ARG B  1  483 ? -11.570 74.544  58.944 0.50 59.31  ? 1282 ARG D C     1 
ATOM   9202  C  C     B ARG B  1  483 ? -11.581 74.541  58.955 0.50 61.51  ? 1282 ARG D C     1 
ATOM   9203  O  O     A ARG B  1  483 ? -11.217 75.691  59.097 0.50 61.48  ? 1282 ARG D O     1 
ATOM   9204  O  O     B ARG B  1  483 ? -11.248 75.691  59.131 0.50 63.34  ? 1282 ARG D O     1 
ATOM   9205  C  CB    A ARG B  1  483 ? -9.884  72.719  58.995 0.50 55.56  ? 1282 ARG D CB    1 
ATOM   9206  C  CB    B ARG B  1  483 ? -9.834  72.756  59.033 0.50 62.93  ? 1282 ARG D CB    1 
ATOM   9207  C  CG    A ARG B  1  483 ? -8.572  73.423  58.766 0.50 54.30  ? 1282 ARG D CG    1 
ATOM   9208  C  CG    B ARG B  1  483 ? -8.727  73.709  58.586 0.50 64.87  ? 1282 ARG D CG    1 
ATOM   9209  C  CD    A ARG B  1  483 ? -7.508  72.353  58.458 0.50 49.44  ? 1282 ARG D CD    1 
ATOM   9210  C  CD    B ARG B  1  483 ? -7.597  72.983  57.864 0.50 65.84  ? 1282 ARG D CD    1 
ATOM   9211  N  NE    A ARG B  1  483 ? -7.852  71.553  57.269 0.50 46.90  ? 1282 ARG D NE    1 
ATOM   9212  N  NE    B ARG B  1  483 ? -8.071  72.059  56.830 0.50 66.14  ? 1282 ARG D NE    1 
ATOM   9213  C  CZ    A ARG B  1  483 ? -7.716  70.229  57.151 0.50 40.66  ? 1282 ARG D CZ    1 
ATOM   9214  C  CZ    B ARG B  1  483 ? -8.323  72.408  55.576 0.50 60.15  ? 1282 ARG D CZ    1 
ATOM   9215  N  NH1   A ARG B  1  483 ? -7.236  69.496  58.153 0.50 32.46  ? 1282 ARG D NH1   1 
ATOM   9216  N  NH1   B ARG B  1  483 ? -8.186  73.664  55.193 0.50 61.69  ? 1282 ARG D NH1   1 
ATOM   9217  N  NH2   A ARG B  1  483 ? -8.063  69.644  56.011 0.50 39.64  ? 1282 ARG D NH2   1 
ATOM   9218  N  NH2   B ARG B  1  483 ? -8.733  71.511  54.714 0.50 58.03  ? 1282 ARG D NH2   1 
ATOM   9219  N  N     . ASP B  1  484 ? -12.498 74.185  58.061 1.00 59.31  ? 1283 ASP D N     1 
ATOM   9220  C  CA    . ASP B  1  484 ? -13.140 75.136  57.179 1.00 57.07  ? 1283 ASP D CA    1 
ATOM   9221  C  C     . ASP B  1  484 ? -14.305 75.778  57.897 1.00 61.66  ? 1283 ASP D C     1 
ATOM   9222  O  O     . ASP B  1  484 ? -15.004 76.618  57.339 1.00 70.42  ? 1283 ASP D O     1 
ATOM   9223  C  CB    . ASP B  1  484 ? -13.627 74.450  55.900 1.00 61.12  ? 1283 ASP D CB    1 
ATOM   9224  C  CG    . ASP B  1  484 ? -12.470 73.950  55.014 1.00 71.75  ? 1283 ASP D CG    1 
ATOM   9225  O  OD1   . ASP B  1  484 ? -11.292 74.306  55.264 1.00 72.17  ? 1283 ASP D OD1   1 
ATOM   9226  O  OD2   . ASP B  1  484 ? -12.730 73.175  54.064 1.00 75.51  ? 1283 ASP D OD2   1 
ATOM   9227  N  N     . LYS B  1  485 ? -14.527 75.369  59.142 1.00 60.45  ? 1284 LYS D N     1 
ATOM   9228  C  CA    . LYS B  1  485 ? -15.619 75.895  59.945 1.00 54.46  ? 1284 LYS D CA    1 
ATOM   9229  C  C     . LYS B  1  485 ? -16.966 75.608  59.317 1.00 54.93  ? 1284 LYS D C     1 
ATOM   9230  O  O     . LYS B  1  485 ? -17.902 76.376  59.448 1.00 55.55  ? 1284 LYS D O     1 
ATOM   9231  C  CB    . LYS B  1  485 ? -15.442 77.405  60.212 1.00 59.06  ? 1284 LYS D CB    1 
ATOM   9232  C  CG    . LYS B  1  485 ? -14.086 77.765  60.831 1.00 60.33  ? 1284 LYS D CG    1 
ATOM   9233  C  CD    . LYS B  1  485 ? -14.107 78.948  61.794 1.00 61.10  ? 1284 LYS D CD    1 
ATOM   9234  N  N     . LYS B  1  486 ? -17.065 74.480  58.627 1.00 58.36  ? 1285 LYS D N     1 
ATOM   9235  C  CA    . LYS B  1  486 ? -18.327 74.036  58.009 1.00 51.03  ? 1285 LYS D CA    1 
ATOM   9236  C  C     . LYS B  1  486 ? -19.177 73.247  58.993 1.00 47.63  ? 1285 LYS D C     1 
ATOM   9237  O  O     . LYS B  1  486 ? -20.333 72.957  58.737 1.00 47.13  ? 1285 LYS D O     1 
ATOM   9238  C  CB    . LYS B  1  486 ? -18.062 73.240  56.735 1.00 48.76  ? 1285 LYS D CB    1 
ATOM   9239  C  CG    . LYS B  1  486 ? -17.619 74.103  55.555 1.00 48.13  ? 1285 LYS D CG    1 
ATOM   9240  N  N     . ILE B  1  487 ? -18.594 72.905  60.128 1.00 43.59  ? 1286 ILE D N     1 
ATOM   9241  C  CA    . ILE B  1  487 ? -19.322 72.263  61.217 1.00 43.11  ? 1286 ILE D CA    1 
ATOM   9242  C  C     . ILE B  1  487 ? -18.920 72.941  62.517 1.00 43.92  ? 1286 ILE D C     1 
ATOM   9243  O  O     . ILE B  1  487 ? -17.739 73.285  62.717 1.00 47.55  ? 1286 ILE D O     1 
ATOM   9244  C  CB    . ILE B  1  487 ? -19.003 70.722  61.267 1.00 45.14  ? 1286 ILE D CB    1 
ATOM   9245  C  CG1   . ILE B  1  487 ? -19.911 70.023  62.239 1.00 45.08  ? 1286 ILE D CG1   1 
ATOM   9246  C  CG2   . ILE B  1  487 ? -17.537 70.445  61.596 1.00 42.71  ? 1286 ILE D CG2   1 
ATOM   9247  C  CD1   . ILE B  1  487 ? -20.612 68.892  61.552 1.00 55.95  ? 1286 ILE D CD1   1 
ATOM   9248  N  N     . ASP B  1  488 ? -19.864 73.069  63.439 1.00 44.16  ? 1287 ASP D N     1 
ATOM   9249  C  CA    . ASP B  1  488 ? -19.576 73.716  64.717 1.00 50.97  ? 1287 ASP D CA    1 
ATOM   9250  C  C     . ASP B  1  488 ? -19.583 72.759  65.942 1.00 51.98  ? 1287 ASP D C     1 
ATOM   9251  O  O     . ASP B  1  488 ? -20.295 71.766  65.948 1.00 59.12  ? 1287 ASP D O     1 
ATOM   9252  C  CB    . ASP B  1  488 ? -20.581 74.853  64.908 1.00 58.88  ? 1287 ASP D CB    1 
ATOM   9253  C  CG    . ASP B  1  488 ? -20.509 75.451  66.275 1.00 74.47  ? 1287 ASP D CG    1 
ATOM   9254  O  OD1   . ASP B  1  488 ? -19.548 76.203  66.547 1.00 84.27  ? 1287 ASP D OD1   1 
ATOM   9255  O  OD2   . ASP B  1  488 ? -21.405 75.146  67.091 1.00 89.83  ? 1287 ASP D OD2   1 
ATOM   9256  N  N     . GLY B  1  489 ? -18.776 73.072  66.946 1.00 45.49  ? 1288 GLY D N     1 
ATOM   9257  C  CA    . GLY B  1  489 ? -18.839 72.402  68.248 1.00 43.57  ? 1288 GLY D CA    1 
ATOM   9258  C  C     . GLY B  1  489 ? -17.896 71.245  68.505 1.00 45.65  ? 1288 GLY D C     1 
ATOM   9259  O  O     . GLY B  1  489 ? -17.991 70.575  69.523 1.00 43.62  ? 1288 GLY D O     1 
ATOM   9260  N  N     . ILE B  1  490 ? -16.947 71.020  67.608 1.00 46.72  ? 1289 ILE D N     1 
ATOM   9261  C  CA    . ILE B  1  490 ? -16.010 69.920  67.805 1.00 45.62  ? 1289 ILE D CA    1 
ATOM   9262  C  C     . ILE B  1  490 ? -14.662 70.405  68.339 1.00 46.13  ? 1289 ILE D C     1 
ATOM   9263  O  O     . ILE B  1  490 ? -13.900 71.089  67.639 1.00 44.81  ? 1289 ILE D O     1 
ATOM   9264  C  CB    . ILE B  1  490 ? -15.839 69.086  66.511 1.00 44.45  ? 1289 ILE D CB    1 
ATOM   9265  C  CG1   . ILE B  1  490 ? -17.154 68.413  66.144 1.00 42.96  ? 1289 ILE D CG1   1 
ATOM   9266  C  CG2   . ILE B  1  490 ? -14.721 68.053  66.665 1.00 43.97  ? 1289 ILE D CG2   1 
ATOM   9267  C  CD1   . ILE B  1  490 ? -17.150 67.761  64.764 1.00 37.68  ? 1289 ILE D CD1   1 
ATOM   9268  N  N     . THR B  1  491 ? -14.344 70.022  69.571 1.00 42.38  ? 1290 THR D N     1 
ATOM   9269  C  CA    . THR B  1  491 ? -13.054 70.394  70.160 1.00 42.88  ? 1290 THR D CA    1 
ATOM   9270  C  C     . THR B  1  491 ? -11.890 69.484  69.806 1.00 43.68  ? 1290 THR D C     1 
ATOM   9271  O  O     . THR B  1  491 ? -10.778 69.937  69.728 1.00 50.58  ? 1290 THR D O     1 
ATOM   9272  C  CB    . THR B  1  491 ? -13.145 70.535  71.690 1.00 49.94  ? 1290 THR D CB    1 
ATOM   9273  O  OG1   . THR B  1  491 ? -13.485 69.263  72.278 1.00 55.10  ? 1290 THR D OG1   1 
ATOM   9274  C  CG2   . THR B  1  491 ? -14.215 71.606  72.057 1.00 45.69  ? 1290 THR D CG2   1 
ATOM   9275  N  N     . ASP B  1  492 ? -12.125 68.191  69.606 1.00 47.80  ? 1291 ASP D N     1 
ATOM   9276  C  CA    . ASP B  1  492 ? -11.036 67.252  69.275 1.00 40.23  ? 1291 ASP D CA    1 
ATOM   9277  C  C     . ASP B  1  492 ? -11.530 66.033  68.457 1.00 40.39  ? 1291 ASP D C     1 
ATOM   9278  O  O     . ASP B  1  492 ? -12.678 65.632  68.553 1.00 45.08  ? 1291 ASP D O     1 
ATOM   9279  C  CB    . ASP B  1  492 ? -10.327 66.774  70.527 1.00 37.69  ? 1291 ASP D CB    1 
ATOM   9280  C  CG    . ASP B  1  492 ? -8.926  66.220  70.221 1.00 45.37  ? 1291 ASP D CG    1 
ATOM   9281  O  OD1   . ASP B  1  492 ? -8.408  66.456  69.108 1.00 52.84  ? 1291 ASP D OD1   1 
ATOM   9282  O  OD2   . ASP B  1  492 ? -8.319  65.528  71.079 1.00 44.47  ? 1291 ASP D OD2   1 
ATOM   9283  N  N     . LEU B  1  493 ? -10.651 65.451  67.665 1.00 34.81  ? 1292 LEU D N     1 
ATOM   9284  C  CA    . LEU B  1  493 ? -10.926 64.332  66.816 1.00 38.24  ? 1292 LEU D CA    1 
ATOM   9285  C  C     . LEU B  1  493 ? -9.738  63.380  66.904 1.00 39.88  ? 1292 LEU D C     1 
ATOM   9286  O  O     . LEU B  1  493 ? -8.633  63.739  66.601 1.00 43.66  ? 1292 LEU D O     1 
ATOM   9287  C  CB    . LEU B  1  493 ? -11.124 64.815  65.377 1.00 38.67  ? 1292 LEU D CB    1 
ATOM   9288  C  CG    . LEU B  1  493 ? -11.527 63.839  64.280 1.00 40.55  ? 1292 LEU D CG    1 
ATOM   9289  C  CD1   . LEU B  1  493 ? -12.802 63.102  64.583 1.00 38.04  ? 1292 LEU D CD1   1 
ATOM   9290  C  CD2   . LEU B  1  493 ? -11.648 64.602  62.987 1.00 39.16  ? 1292 LEU D CD2   1 
ATOM   9291  N  N     . ARG B  1  494 ? -9.961  62.142  67.324 1.00 41.62  ? 1293 ARG D N     1 
ATOM   9292  C  CA    . ARG B  1  494 ? -8.861  61.164  67.417 1.00 38.14  ? 1293 ARG D CA    1 
ATOM   9293  C  C     . ARG B  1  494 ? -9.321  59.761  67.044 1.00 40.26  ? 1293 ARG D C     1 
ATOM   9294  O  O     . ARG B  1  494 ? -10.490 59.370  67.299 1.00 39.93  ? 1293 ARG D O     1 
ATOM   9295  C  CB    . ARG B  1  494 ? -8.315  61.032  68.839 1.00 39.35  ? 1293 ARG D CB    1 
ATOM   9296  C  CG    . ARG B  1  494 ? -8.716  62.111  69.801 1.00 42.12  ? 1293 ARG D CG    1 
ATOM   9297  C  CD    . ARG B  1  494 ? -7.914  61.989  71.082 1.00 43.77  ? 1293 ARG D CD    1 
ATOM   9298  N  NE    . ARG B  1  494 ? -8.663  61.249  72.072 1.00 42.34  ? 1293 ARG D NE    1 
ATOM   9299  C  CZ    . ARG B  1  494 ? -9.674  61.763  72.760 1.00 44.94  ? 1293 ARG D CZ    1 
ATOM   9300  N  NH1   . ARG B  1  494 ? -10.035 63.021  72.563 1.00 42.51  ? 1293 ARG D NH1   1 
ATOM   9301  N  NH2   . ARG B  1  494 ? -10.328 61.015  73.650 1.00 42.92  ? 1293 ARG D NH2   1 
ATOM   9302  N  N     . ASP B  1  495 ? -8.381  59.001  66.488 1.00 35.44  ? 1294 ASP D N     1 
ATOM   9303  C  CA    . ASP B  1  495 ? -8.618  57.628  66.135 1.00 34.17  ? 1294 ASP D CA    1 
ATOM   9304  C  C     . ASP B  1  495 ? -7.981  56.826  67.215 1.00 33.64  ? 1294 ASP D C     1 
ATOM   9305  O  O     . ASP B  1  495 ? -6.766  56.776  67.308 1.00 35.53  ? 1294 ASP D O     1 
ATOM   9306  C  CB    . ASP B  1  495 ? -8.053  57.278  64.740 1.00 33.40  ? 1294 ASP D CB    1 
ATOM   9307  C  CG    . ASP B  1  495 ? -8.522  55.904  64.260 1.00 36.15  ? 1294 ASP D CG    1 
ATOM   9308  O  OD1   . ASP B  1  495 ? -9.204  55.215  65.024 1.00 38.31  ? 1294 ASP D OD1   1 
ATOM   9309  O  OD2   . ASP B  1  495 ? -8.235  55.513  63.125 1.00 40.13  ? 1294 ASP D OD2   1 
ATOM   9310  N  N     . GLU B  1  496 ? -8.789  56.186  68.041 1.00 32.43  ? 1295 GLU D N     1 
ATOM   9311  C  CA    . GLU B  1  496 ? -8.257  55.444  69.184 1.00 36.30  ? 1295 GLU D CA    1 
ATOM   9312  C  C     . GLU B  1  496 ? -8.384  53.966  68.867 1.00 36.43  ? 1295 GLU D C     1 
ATOM   9313  O  O     . GLU B  1  496 ? -8.258  53.156  69.753 1.00 40.45  ? 1295 GLU D O     1 
ATOM   9314  C  CB    . GLU B  1  496 ? -9.008  55.758  70.479 1.00 36.13  ? 1295 GLU D CB    1 
ATOM   9315  C  CG    . GLU B  1  496 ? -8.812  57.198  70.927 1.00 39.72  ? 1295 GLU D CG    1 
ATOM   9316  C  CD    . GLU B  1  496 ? -9.441  57.481  72.279 1.00 41.03  ? 1295 GLU D CD    1 
ATOM   9317  O  OE1   . GLU B  1  496 ? -10.239 56.658  72.783 1.00 45.50  ? 1295 GLU D OE1   1 
ATOM   9318  O  OE2   . GLU B  1  496 ? -9.153  58.519  72.842 1.00 43.16  ? 1295 GLU D OE2   1 
ATOM   9319  N  N     . THR B  1  497 ? -8.625  53.635  67.597 1.00 33.49  ? 1296 THR D N     1 
ATOM   9320  C  CA    . THR B  1  497 ? -8.753  52.262  67.185 1.00 33.53  ? 1296 THR D CA    1 
ATOM   9321  C  C     . THR B  1  497 ? -7.481  51.491  67.566 1.00 35.79  ? 1296 THR D C     1 
ATOM   9322  O  O     . THR B  1  497 ? -6.356  51.992  67.465 1.00 32.36  ? 1296 THR D O     1 
ATOM   9323  C  CB    . THR B  1  497 ? -8.971  52.158  65.676 1.00 33.21  ? 1296 THR D CB    1 
ATOM   9324  O  OG1   . THR B  1  497 ? -10.216 52.801  65.325 1.00 32.64  ? 1296 THR D OG1   1 
ATOM   9325  C  CG2   . THR B  1  497 ? -8.943  50.679  65.210 1.00 32.19  ? 1296 THR D CG2   1 
ATOM   9326  N  N     . SER B  1  498 ? -7.689  50.266  68.020 1.00 36.91  ? 1297 SER D N     1 
ATOM   9327  C  CA    . SER B  1  498 ? -6.583  49.404  68.381 1.00 39.09  ? 1297 SER D CA    1 
ATOM   9328  C  C     . SER B  1  498 ? -7.018  47.977  68.183 1.00 39.52  ? 1297 SER D C     1 
ATOM   9329  O  O     . SER B  1  498 ? -8.216  47.661  68.176 1.00 36.74  ? 1297 SER D O     1 
ATOM   9330  C  CB    . SER B  1  498 ? -6.117  49.651  69.831 1.00 41.44  ? 1297 SER D CB    1 
ATOM   9331  O  OG    . SER B  1  498 ? -6.653  48.699  70.683 1.00 46.07  ? 1297 SER D OG    1 
ATOM   9332  N  N     . LEU B  1  499 ? -6.032  47.113  68.028 1.00 40.27  ? 1298 LEU D N     1 
ATOM   9333  C  CA    . LEU B  1  499 ? -6.277  45.688  67.854 1.00 45.30  ? 1298 LEU D CA    1 
ATOM   9334  C  C     . LEU B  1  499 ? -7.033  45.158  69.043 1.00 45.94  ? 1298 LEU D C     1 
ATOM   9335  O  O     . LEU B  1  499 ? -7.975  44.398  68.906 1.00 48.36  ? 1298 LEU D O     1 
ATOM   9336  C  CB    . LEU B  1  499 ? -4.941  44.949  67.753 1.00 49.94  ? 1298 LEU D CB    1 
ATOM   9337  C  CG    . LEU B  1  499 ? -4.597  44.259  66.445 1.00 54.32  ? 1298 LEU D CG    1 
ATOM   9338  C  CD1   . LEU B  1  499 ? -5.132  44.988  65.198 1.00 53.84  ? 1298 LEU D CD1   1 
ATOM   9339  C  CD2   . LEU B  1  499 ? -3.079  44.103  66.439 1.00 58.67  ? 1298 LEU D CD2   1 
ATOM   9340  N  N     . ARG B  1  500 ? -6.609  45.611  70.210 1.00 45.18  ? 1299 ARG D N     1 
ATOM   9341  C  CA    . ARG B  1  500 ? -7.145  45.213  71.476 1.00 47.60  ? 1299 ARG D CA    1 
ATOM   9342  C  C     . ARG B  1  500 ? -8.537  45.757  71.745 1.00 49.62  ? 1299 ARG D C     1 
ATOM   9343  O  O     . ARG B  1  500 ? -9.380  45.028  72.207 1.00 54.29  ? 1299 ARG D O     1 
ATOM   9344  C  CB    . ARG B  1  500 ? -6.125  45.616  72.544 1.00 60.23  ? 1299 ARG D CB    1 
ATOM   9345  C  CG    . ARG B  1  500 ? -4.792  44.874  72.320 1.00 68.99  ? 1299 ARG D CG    1 
ATOM   9346  C  CD    . ARG B  1  500 ? -3.577  45.644  72.809 1.00 76.58  ? 1299 ARG D CD    1 
ATOM   9347  N  NE    . ARG B  1  500 ? -3.197  46.844  72.036 1.00 71.23  ? 1299 ARG D NE    1 
ATOM   9348  C  CZ    . ARG B  1  500 ? -2.586  46.846  70.848 1.00 62.34  ? 1299 ARG D CZ    1 
ATOM   9349  N  NH1   . ARG B  1  500 ? -2.307  45.719  70.203 1.00 59.01  ? 1299 ARG D NH1   1 
ATOM   9350  N  NH2   . ARG B  1  500 ? -2.237  47.994  70.296 1.00 51.92  ? 1299 ARG D NH2   1 
ATOM   9351  N  N     . THR B  1  501 ? -8.790  47.014  71.411 1.00 48.78  ? 1300 THR D N     1 
ATOM   9352  C  CA    . THR B  1  501 ? -10.094 47.621  71.667 1.00 41.44  ? 1300 THR D CA    1 
ATOM   9353  C  C     . THR B  1  501 ? -11.060 47.660  70.483 1.00 39.33  ? 1300 THR D C     1 
ATOM   9354  O  O     . THR B  1  501 ? -12.215 47.994  70.652 1.00 47.81  ? 1300 THR D O     1 
ATOM   9355  C  CB    . THR B  1  501 ? -9.957  49.052  72.204 1.00 48.54  ? 1300 THR D CB    1 
ATOM   9356  O  OG1   . THR B  1  501 ? -10.472 50.015  71.253 1.00 58.11  ? 1300 THR D OG1   1 
ATOM   9357  C  CG2   . THR B  1  501 ? -8.558  49.373  72.564 1.00 50.22  ? 1300 THR D CG2   1 
ATOM   9358  N  N     . GLY B  1  502 ? -10.626 47.346  69.268 1.00 39.59  ? 1301 GLY D N     1 
ATOM   9359  C  CA    . GLY B  1  502 ? -11.522 47.479  68.064 1.00 30.41  ? 1301 GLY D CA    1 
ATOM   9360  C  C     . GLY B  1  502 ? -11.525 48.917  67.530 1.00 32.73  ? 1301 GLY D C     1 
ATOM   9361  O  O     . GLY B  1  502 ? -10.816 49.763  68.023 1.00 35.16  ? 1301 GLY D O     1 
ATOM   9362  N  N     . VAL B  1  503 ? -12.301 49.181  66.506 1.00 33.88  ? 1302 VAL D N     1 
ATOM   9363  C  CA    . VAL B  1  503 ? -12.517 50.503  65.994 1.00 33.12  ? 1302 VAL D CA    1 
ATOM   9364  C  C     . VAL B  1  503 ? -13.038 51.445  67.099 1.00 34.21  ? 1302 VAL D C     1 
ATOM   9365  O  O     . VAL B  1  503 ? -14.033 51.171  67.754 1.00 33.55  ? 1302 VAL D O     1 
ATOM   9366  C  CB    . VAL B  1  503 ? -13.579 50.516  64.857 1.00 36.66  ? 1302 VAL D CB    1 
ATOM   9367  C  CG1   . VAL B  1  503 ? -13.935 51.951  64.480 1.00 35.30  ? 1302 VAL D CG1   1 
ATOM   9368  C  CG2   . VAL B  1  503 ? -13.188 49.715  63.623 1.00 31.56  ? 1302 VAL D CG2   1 
ATOM   9369  N  N     . ARG B  1  504 ? -12.369 52.579  67.264 1.00 30.59  ? 1303 ARG D N     1 
ATOM   9370  C  CA    . ARG B  1  504 ? -12.822 53.600  68.163 1.00 30.06  ? 1303 ARG D CA    1 
ATOM   9371  C  C     . ARG B  1  504 ? -12.442 54.979  67.643 1.00 30.67  ? 1303 ARG D C     1 
ATOM   9372  O  O     . ARG B  1  504 ? -11.271 55.335  67.614 1.00 30.07  ? 1303 ARG D O     1 
ATOM   9373  C  CB    . ARG B  1  504 ? -12.212 53.405  69.563 1.00 30.67  ? 1303 ARG D CB    1 
ATOM   9374  C  CG    . ARG B  1  504 ? -12.890 54.191  70.662 1.00 27.03  ? 1303 ARG D CG    1 
ATOM   9375  C  CD    . ARG B  1  504 ? -12.227 53.890  72.020 1.00 28.24  ? 1303 ARG D CD    1 
ATOM   9376  N  NE    . ARG B  1  504 ? -12.524 54.978  72.945 1.00 28.81  ? 1303 ARG D NE    1 
ATOM   9377  C  CZ    . ARG B  1  504 ? -13.640 55.089  73.659 1.00 32.04  ? 1303 ARG D CZ    1 
ATOM   9378  N  NH1   . ARG B  1  504 ? -14.612 54.162  73.612 1.00 28.52  ? 1303 ARG D NH1   1 
ATOM   9379  N  NH2   . ARG B  1  504 ? -13.818 56.165  74.401 1.00 31.96  ? 1303 ARG D NH2   1 
ATOM   9380  N  N     . VAL B  1  505 ? -13.449 55.770  67.291 1.00 28.57  ? 1304 VAL D N     1 
ATOM   9381  C  CA    . VAL B  1  505 ? -13.210 57.106  66.761 1.00 31.60  ? 1304 VAL D CA    1 
ATOM   9382  C  C     . VAL B  1  505 ? -13.930 58.055  67.643 1.00 33.02  ? 1304 VAL D C     1 
ATOM   9383  O  O     . VAL B  1  505 ? -15.133 57.892  67.893 1.00 29.35  ? 1304 VAL D O     1 
ATOM   9384  C  CB    . VAL B  1  505 ? -13.632 57.288  65.292 1.00 35.66  ? 1304 VAL D CB    1 
ATOM   9385  C  CG1   . VAL B  1  505 ? -13.286 58.688  64.831 1.00 38.23  ? 1304 VAL D CG1   1 
ATOM   9386  C  CG2   . VAL B  1  505 ? -12.927 56.300  64.379 1.00 29.09  ? 1304 VAL D CG2   1 
ATOM   9387  N  N     . VAL B  1  506 ? -13.193 59.048  68.154 1.00 32.09  ? 1305 VAL D N     1 
ATOM   9388  C  CA    . VAL B  1  506 ? -13.714 59.858  69.242 1.00 30.52  ? 1305 VAL D CA    1 
ATOM   9389  C  C     . VAL B  1  506 ? -13.802 61.297  68.762 1.00 30.97  ? 1305 VAL D C     1 
ATOM   9390  O  O     . VAL B  1  506 ? -12.796 61.869  68.275 1.00 29.55  ? 1305 VAL D O     1 
ATOM   9391  C  CB    . VAL B  1  506 ? -12.840 59.764  70.496 1.00 30.72  ? 1305 VAL D CB    1 
ATOM   9392  C  CG1   . VAL B  1  506 ? -13.424 60.657  71.578 1.00 32.25  ? 1305 VAL D CG1   1 
ATOM   9393  C  CG2   . VAL B  1  506 ? -12.745 58.331  70.976 1.00 30.76  ? 1305 VAL D CG2   1 
ATOM   9394  N  N     . ILE B  1  507 ? -14.997 61.864  68.847 1.00 30.35  ? 1306 ILE D N     1 
ATOM   9395  C  CA    . ILE B  1  507 ? -15.185 63.247  68.520 1.00 31.97  ? 1306 ILE D CA    1 
ATOM   9396  C  C     . ILE B  1  507 ? -15.542 63.994  69.795 1.00 35.73  ? 1306 ILE D C     1 
ATOM   9397  O  O     . ILE B  1  507 ? -16.599 63.770  70.352 1.00 38.30  ? 1306 ILE D O     1 
ATOM   9398  C  CB    . ILE B  1  507 ? -16.287 63.424  67.492 1.00 31.68  ? 1306 ILE D CB    1 
ATOM   9399  C  CG1   . ILE B  1  507 ? -15.882 62.762  66.184 1.00 31.99  ? 1306 ILE D CG1   1 
ATOM   9400  C  CG2   . ILE B  1  507 ? -16.541 64.918  67.216 1.00 36.40  ? 1306 ILE D CG2   1 
ATOM   9401  C  CD1   . ILE B  1  507 ? -16.989 61.908  65.643 1.00 38.54  ? 1306 ILE D CD1   1 
ATOM   9402  N  N     . ASP B  1  508 ? -14.665 64.874  70.246 1.00 35.39  ? 1307 ASP D N     1 
ATOM   9403  C  CA    . ASP B  1  508 ? -14.922 65.637  71.480 1.00 39.25  ? 1307 ASP D CA    1 
ATOM   9404  C  C     . ASP B  1  508 ? -15.799 66.825  71.193 1.00 39.32  ? 1307 ASP D C     1 
ATOM   9405  O  O     . ASP B  1  508 ? -15.621 67.521  70.181 1.00 45.06  ? 1307 ASP D O     1 
ATOM   9406  C  CB    . ASP B  1  508 ? -13.606 66.076  72.122 1.00 44.32  ? 1307 ASP D CB    1 
ATOM   9407  C  CG    . ASP B  1  508 ? -12.943 64.944  72.922 1.00 44.52  ? 1307 ASP D CG    1 
ATOM   9408  O  OD1   . ASP B  1  508 ? -13.608 63.898  73.176 1.00 48.48  ? 1307 ASP D OD1   1 
ATOM   9409  O  OD2   . ASP B  1  508 ? -11.750 65.072  73.251 1.00 45.09  ? 1307 ASP D OD2   1 
ATOM   9410  N  N     . VAL B  1  509 ? -16.776 67.048  72.053 1.00 39.36  ? 1308 VAL D N     1 
ATOM   9411  C  CA    . VAL B  1  509 ? -17.764 68.087  71.823 1.00 42.44  ? 1308 VAL D CA    1 
ATOM   9412  C  C     . VAL B  1  509 ? -17.534 69.246  72.789 1.00 49.77  ? 1308 VAL D C     1 
ATOM   9413  O  O     . VAL B  1  509 ? -17.277 69.016  73.999 1.00 45.00  ? 1308 VAL D O     1 
ATOM   9414  C  CB    . VAL B  1  509 ? -19.182 67.541  72.005 1.00 42.60  ? 1308 VAL D CB    1 
ATOM   9415  C  CG1   . VAL B  1  509 ? -20.199 68.682  72.017 1.00 41.58  ? 1308 VAL D CG1   1 
ATOM   9416  C  CG2   . VAL B  1  509 ? -19.516 66.612  70.855 1.00 41.77  ? 1308 VAL D CG2   1 
ATOM   9417  N  N     . ARG B  1  510 ? -17.635 70.475  72.270 1.00 51.41  ? 1309 ARG D N     1 
ATOM   9418  C  CA    . ARG B  1  510 ? -17.482 71.666  73.091 1.00 51.58  ? 1309 ARG D CA    1 
ATOM   9419  C  C     . ARG B  1  510 ? -18.495 71.652  74.212 1.00 46.76  ? 1309 ARG D C     1 
ATOM   9420  O  O     . ARG B  1  510 ? -19.658 71.326  73.974 1.00 45.98  ? 1309 ARG D O     1 
ATOM   9421  C  CB    . ARG B  1  510 ? -17.657 72.926  72.238 1.00 58.65  ? 1309 ARG D CB    1 
ATOM   9422  C  CG    . ARG B  1  510 ? -17.654 74.196  73.113 1.00 60.54  ? 1309 ARG D CG    1 
ATOM   9423  C  CD    . ARG B  1  510 ? -17.470 75.517  72.345 1.00 53.11  ? 1309 ARG D CD    1 
ATOM   9424  N  NE    . ARG B  1  510 ? -18.294 75.596  71.127 1.00 55.71  ? 1309 ARG D NE    1 
ATOM   9425  C  CZ    . ARG B  1  510 ? -19.631 75.515  71.087 1.00 55.10  ? 1309 ARG D CZ    1 
ATOM   9426  N  NH1   . ARG B  1  510 ? -20.356 75.353  72.209 1.00 58.28  ? 1309 ARG D NH1   1 
ATOM   9427  N  NH2   . ARG B  1  510 ? -20.241 75.582  69.909 1.00 50.43  ? 1309 ARG D NH2   1 
ATOM   9428  N  N     . LYS B  1  511 ? -18.053 72.013  75.420 1.00 47.63  ? 1310 LYS D N     1 
ATOM   9429  C  CA    . LYS B  1  511 ? -18.913 72.005  76.587 1.00 46.70  ? 1310 LYS D CA    1 
ATOM   9430  C  C     . LYS B  1  511 ? -20.190 72.789  76.362 1.00 48.88  ? 1310 LYS D C     1 
ATOM   9431  O  O     . LYS B  1  511 ? -20.157 73.931  75.903 1.00 52.77  ? 1310 LYS D O     1 
ATOM   9432  C  CB    . LYS B  1  511 ? -18.151 72.588  77.755 1.00 48.63  ? 1310 LYS D CB    1 
ATOM   9433  C  CG    . LYS B  1  511 ? -18.827 72.396  79.100 1.00 53.03  ? 1310 LYS D CG    1 
ATOM   9434  C  CD    . LYS B  1  511 ? -17.915 72.911  80.214 1.00 52.10  ? 1310 LYS D CD    1 
ATOM   9435  C  CE    . LYS B  1  511 ? -18.554 72.778  81.592 1.00 56.90  ? 1310 LYS D CE    1 
ATOM   9436  N  NZ    . LYS B  1  511 ? -20.017 72.579  81.458 1.00 65.16  ? 1310 LYS D NZ    1 
ATOM   9437  N  N     . ASP B  1  512 ? -21.313 72.159  76.666 1.00 48.72  ? 1311 ASP D N     1 
ATOM   9438  C  CA    . ASP B  1  512 ? -22.631 72.800  76.554 1.00 51.41  ? 1311 ASP D CA    1 
ATOM   9439  C  C     . ASP B  1  512 ? -23.228 72.795  75.170 1.00 49.94  ? 1311 ASP D C     1 
ATOM   9440  O  O     . ASP B  1  512 ? -24.394 73.170  75.019 1.00 49.99  ? 1311 ASP D O     1 
ATOM   9441  C  CB    . ASP B  1  512 ? -22.644 74.248  77.117 1.00 58.20  ? 1311 ASP D CB    1 
ATOM   9442  C  CG    . ASP B  1  512 ? -22.511 74.280  78.633 1.00 70.56  ? 1311 ASP D CG    1 
ATOM   9443  O  OD1   . ASP B  1  512 ? -23.231 73.486  79.299 1.00 63.82  ? 1311 ASP D OD1   1 
ATOM   9444  O  OD2   . ASP B  1  512 ? -21.713 75.111  79.162 1.00 73.97  ? 1311 ASP D OD2   1 
ATOM   9445  N  N     . ALA B  1  513 ? -22.475 72.350  74.162 1.00 51.15  ? 1312 ALA D N     1 
ATOM   9446  C  CA    . ALA B  1  513 ? -23.027 72.178  72.804 1.00 47.63  ? 1312 ALA D CA    1 
ATOM   9447  C  C     . ALA B  1  513 ? -23.844 70.884  72.745 1.00 43.91  ? 1312 ALA D C     1 
ATOM   9448  O  O     . ALA B  1  513 ? -23.638 69.950  73.533 1.00 45.70  ? 1312 ALA D O     1 
ATOM   9449  C  CB    . ALA B  1  513 ? -21.912 72.144  71.798 1.00 42.74  ? 1312 ALA D CB    1 
ATOM   9450  N  N     . ASN B  1  514 ? -24.813 70.863  71.860 1.00 43.17  ? 1313 ASN D N     1 
ATOM   9451  C  CA    . ASN B  1  514 ? -25.669 69.709  71.731 1.00 41.75  ? 1313 ASN D CA    1 
ATOM   9452  C  C     . ASN B  1  514 ? -24.985 68.644  70.854 1.00 40.08  ? 1313 ASN D C     1 
ATOM   9453  O  O     . ASN B  1  514 ? -24.845 68.815  69.661 1.00 39.55  ? 1313 ASN D O     1 
ATOM   9454  C  CB    . ASN B  1  514 ? -27.027 70.113  71.197 1.00 36.75  ? 1313 ASN D CB    1 
ATOM   9455  C  CG    . ASN B  1  514 ? -27.967 68.961  71.168 1.00 42.81  ? 1313 ASN D CG    1 
ATOM   9456  O  OD1   . ASN B  1  514 ? -27.603 67.882  70.717 1.00 43.97  ? 1313 ASN D OD1   1 
ATOM   9457  N  ND2   . ASN B  1  514 ? -29.175 69.155  71.656 1.00 41.03  ? 1313 ASN D ND2   1 
ATOM   9458  N  N     . ALA B  1  515 ? -24.577 67.547  71.479 1.00 39.41  ? 1314 ALA D N     1 
ATOM   9459  C  CA    . ALA B  1  515 ? -23.817 66.483  70.803 1.00 38.01  ? 1314 ALA D CA    1 
ATOM   9460  C  C     . ALA B  1  515 ? -24.666 65.747  69.774 1.00 35.40  ? 1314 ALA D C     1 
ATOM   9461  O  O     . ALA B  1  515 ? -24.151 65.325  68.760 1.00 37.43  ? 1314 ALA D O     1 
ATOM   9462  C  CB    . ALA B  1  515 ? -23.221 65.520  71.791 1.00 36.94  ? 1314 ALA D CB    1 
ATOM   9463  N  N     . SER B  1  516 ? -25.955 65.651  70.030 1.00 31.33  ? 1315 SER D N     1 
ATOM   9464  C  CA    . SER B  1  516 ? -26.850 65.000  69.117 1.00 35.91  ? 1315 SER D CA    1 
ATOM   9465  C  C     . SER B  1  516 ? -27.025 65.782  67.806 1.00 43.10  ? 1315 SER D C     1 
ATOM   9466  O  O     . SER B  1  516 ? -27.202 65.166  66.711 1.00 41.10  ? 1315 SER D O     1 
ATOM   9467  C  CB    . SER B  1  516 ? -28.209 64.787  69.754 1.00 36.46  ? 1315 SER D CB    1 
ATOM   9468  O  OG    . SER B  1  516 ? -28.149 63.855  70.762 1.00 44.95  ? 1315 SER D OG    1 
ATOM   9469  N  N     . VAL B  1  517 ? -26.976 67.120  67.903 1.00 41.66  ? 1316 VAL D N     1 
ATOM   9470  C  CA    . VAL B  1  517 ? -27.058 67.963  66.739 1.00 33.68  ? 1316 VAL D CA    1 
ATOM   9471  C  C     . VAL B  1  517 ? -25.812 67.821  65.960 1.00 31.22  ? 1316 VAL D C     1 
ATOM   9472  O  O     . VAL B  1  517 ? -25.842 67.737  64.727 1.00 39.78  ? 1316 VAL D O     1 
ATOM   9473  C  CB    . VAL B  1  517 ? -27.264 69.460  67.143 1.00 36.90  ? 1316 VAL D CB    1 
ATOM   9474  C  CG1   . VAL B  1  517 ? -26.954 70.403  65.984 1.00 32.62  ? 1316 VAL D CG1   1 
ATOM   9475  C  CG2   . VAL B  1  517 ? -28.690 69.685  67.695 1.00 32.13  ? 1316 VAL D CG2   1 
ATOM   9476  N  N     . ILE B  1  518 ? -24.677 67.820  66.645 1.00 35.76  ? 1317 ILE D N     1 
ATOM   9477  C  CA    . ILE B  1  518 ? -23.399 67.673  65.946 1.00 34.19  ? 1317 ILE D CA    1 
ATOM   9478  C  C     . ILE B  1  518 ? -23.360 66.342  65.181 1.00 38.18  ? 1317 ILE D C     1 
ATOM   9479  O  O     . ILE B  1  518 ? -22.895 66.294  64.045 1.00 44.51  ? 1317 ILE D O     1 
ATOM   9480  C  CB    . ILE B  1  518 ? -22.254 67.806  66.932 1.00 36.34  ? 1317 ILE D CB    1 
ATOM   9481  C  CG1   . ILE B  1  518 ? -22.256 69.241  67.486 1.00 36.08  ? 1317 ILE D CG1   1 
ATOM   9482  C  CG2   . ILE B  1  518 ? -20.938 67.442  66.263 1.00 33.44  ? 1317 ILE D CG2   1 
ATOM   9483  C  CD1   . ILE B  1  518 ? -21.210 69.589  68.582 1.00 35.23  ? 1317 ILE D CD1   1 
ATOM   9484  N  N     . LEU B  1  519 ? -23.860 65.275  65.805 1.00 38.99  ? 1318 LEU D N     1 
ATOM   9485  C  CA    . LEU B  1  519 ? -23.861 63.944  65.220 1.00 38.62  ? 1318 LEU D CA    1 
ATOM   9486  C  C     . LEU B  1  519 ? -24.721 63.930  63.982 1.00 40.60  ? 1318 LEU D C     1 
ATOM   9487  O  O     . LEU B  1  519 ? -24.281 63.452  62.959 1.00 38.59  ? 1318 LEU D O     1 
ATOM   9488  C  CB    . LEU B  1  519 ? -24.385 62.929  66.223 1.00 35.51  ? 1318 LEU D CB    1 
ATOM   9489  C  CG    . LEU B  1  519 ? -24.531 61.474  65.745 1.00 37.77  ? 1318 LEU D CG    1 
ATOM   9490  C  CD1   . LEU B  1  519 ? -23.274 60.921  65.065 1.00 29.05  ? 1318 LEU D CD1   1 
ATOM   9491  C  CD2   . LEU B  1  519 ? -24.884 60.544  66.897 1.00 33.77  ? 1318 LEU D CD2   1 
ATOM   9492  N  N     . ASN B  1  520 ? -25.944 64.458  64.100 1.00 40.25  ? 1319 ASN D N     1 
ATOM   9493  C  CA    . ASN B  1  520 ? -26.815 64.635  62.954 1.00 37.52  ? 1319 ASN D CA    1 
ATOM   9494  C  C     . ASN B  1  520 ? -26.181 65.371  61.806 1.00 40.43  ? 1319 ASN D C     1 
ATOM   9495  O  O     . ASN B  1  520 ? -26.299 64.938  60.642 1.00 49.17  ? 1319 ASN D O     1 
ATOM   9496  C  CB    . ASN B  1  520 ? -28.121 65.281  63.340 1.00 37.60  ? 1319 ASN D CB    1 
ATOM   9497  C  CG    . ASN B  1  520 ? -29.066 64.284  63.955 1.00 47.17  ? 1319 ASN D CG    1 
ATOM   9498  O  OD1   . ASN B  1  520 ? -28.915 63.056  63.816 1.00 49.56  ? 1319 ASN D OD1   1 
ATOM   9499  N  ND2   . ASN B  1  520 ? -30.032 64.791  64.656 1.00 49.24  ? 1319 ASN D ND2   1 
ATOM   9500  N  N     . ASN B  1  521 ? -25.465 66.430  62.117 1.00 37.09  ? 1320 ASN D N     1 
ATOM   9501  C  CA    . ASN B  1  521 ? -24.712 67.106  61.082 1.00 41.63  ? 1320 ASN D CA    1 
ATOM   9502  C  C     . ASN B  1  521 ? -23.598 66.237  60.463 1.00 40.24  ? 1320 ASN D C     1 
ATOM   9503  O  O     . ASN B  1  521 ? -23.346 66.266  59.235 1.00 42.46  ? 1320 ASN D O     1 
ATOM   9504  C  CB    . ASN B  1  521 ? -24.170 68.446  61.622 1.00 42.90  ? 1320 ASN D CB    1 
ATOM   9505  C  CG    . ASN B  1  521 ? -25.288 69.457  61.937 1.00 49.63  ? 1320 ASN D CG    1 
ATOM   9506  O  OD1   . ASN B  1  521 ? -26.395 69.432  61.374 1.00 53.28  ? 1320 ASN D OD1   1 
ATOM   9507  N  ND2   . ASN B  1  521 ? -25.001 70.338  62.865 1.00 52.08  ? 1320 ASN D ND2   1 
ATOM   9508  N  N     . LEU B  1  522 ? -22.910 65.480  61.311 1.00 39.56  ? 1321 LEU D N     1 
ATOM   9509  C  CA    . LEU B  1  522 ? -21.879 64.556  60.806 1.00 38.92  ? 1321 LEU D CA    1 
ATOM   9510  C  C     . LEU B  1  522 ? -22.484 63.536  59.827 1.00 34.66  ? 1321 LEU D C     1 
ATOM   9511  O  O     . LEU B  1  522 ? -21.865 63.228  58.810 1.00 33.42  ? 1321 LEU D O     1 
ATOM   9512  C  CB    . LEU B  1  522 ? -21.159 63.868  61.954 1.00 36.40  ? 1321 LEU D CB    1 
ATOM   9513  C  CG    . LEU B  1  522 ? -20.195 64.798  62.676 1.00 41.00  ? 1321 LEU D CG    1 
ATOM   9514  C  CD1   . LEU B  1  522 ? -19.709 64.151  63.960 1.00 40.51  ? 1321 LEU D CD1   1 
ATOM   9515  C  CD2   . LEU B  1  522 ? -18.995 65.180  61.817 1.00 36.85  ? 1321 LEU D CD2   1 
ATOM   9516  N  N     . TYR B  1  523 ? -23.719 63.084  60.097 1.00 30.00  ? 1322 TYR D N     1 
ATOM   9517  C  CA    . TYR B  1  523 ? -24.374 62.161  59.202 1.00 31.91  ? 1322 TYR D CA    1 
ATOM   9518  C  C     . TYR B  1  523 ? -24.645 62.798  57.862 1.00 35.10  ? 1322 TYR D C     1 
ATOM   9519  O  O     . TYR B  1  523 ? -24.476 62.153  56.820 1.00 38.12  ? 1322 TYR D O     1 
ATOM   9520  C  CB    . TYR B  1  523 ? -25.678 61.615  59.786 1.00 31.97  ? 1322 TYR D CB    1 
ATOM   9521  C  CG    . TYR B  1  523 ? -25.479 60.595  60.863 1.00 34.33  ? 1322 TYR D CG    1 
ATOM   9522  C  CD1   . TYR B  1  523 ? -24.444 59.656  60.773 1.00 32.10  ? 1322 TYR D CD1   1 
ATOM   9523  C  CD2   . TYR B  1  523 ? -26.343 60.543  61.978 1.00 32.45  ? 1322 TYR D CD2   1 
ATOM   9524  C  CE1   . TYR B  1  523 ? -24.280 58.712  61.776 1.00 31.81  ? 1322 TYR D CE1   1 
ATOM   9525  C  CE2   . TYR B  1  523 ? -26.196 59.594  62.965 1.00 30.65  ? 1322 TYR D CE2   1 
ATOM   9526  C  CZ    . TYR B  1  523 ? -25.140 58.685  62.843 1.00 33.56  ? 1322 TYR D CZ    1 
ATOM   9527  O  OH    . TYR B  1  523 ? -24.936 57.739  63.772 1.00 34.94  ? 1322 TYR D OH    1 
ATOM   9528  N  N     . LYS B  1  524 ? -25.033 64.073  57.876 1.00 34.77  ? 1323 LYS D N     1 
ATOM   9529  C  CA    . LYS B  1  524 ? -25.376 64.805  56.664 1.00 37.77  ? 1323 LYS D CA    1 
ATOM   9530  C  C     . LYS B  1  524 ? -24.163 65.114  55.796 1.00 34.44  ? 1323 LYS D C     1 
ATOM   9531  O  O     . LYS B  1  524 ? -24.244 65.048  54.578 1.00 41.29  ? 1323 LYS D O     1 
ATOM   9532  C  CB    . LYS B  1  524 ? -26.118 66.110  56.997 1.00 42.20  ? 1323 LYS D CB    1 
ATOM   9533  C  CG    . LYS B  1  524 ? -27.530 65.970  57.501 1.00 41.20  ? 1323 LYS D CG    1 
ATOM   9534  C  CD    . LYS B  1  524 ? -28.181 67.352  57.444 1.00 46.42  ? 1323 LYS D CD    1 
ATOM   9535  C  CE    . LYS B  1  524 ? -28.547 67.871  58.819 1.00 52.51  ? 1323 LYS D CE    1 
ATOM   9536  N  NZ    . LYS B  1  524 ? -29.669 67.040  59.365 1.00 53.45  ? 1323 LYS D NZ    1 
ATOM   9537  N  N     . GLN B  1  525 ? -23.027 65.417  56.406 1.00 34.03  ? 1324 GLN D N     1 
ATOM   9538  C  CA    . GLN B  1  525 ? -21.874 65.937  55.684 1.00 32.40  ? 1324 GLN D CA    1 
ATOM   9539  C  C     . GLN B  1  525 ? -20.668 65.053  55.589 1.00 35.84  ? 1324 GLN D C     1 
ATOM   9540  O  O     . GLN B  1  525 ? -19.635 65.495  55.070 1.00 35.51  ? 1324 GLN D O     1 
ATOM   9541  C  CB    . GLN B  1  525 ? -21.409 67.231  56.361 1.00 36.12  ? 1324 GLN D CB    1 
ATOM   9542  C  CG    . GLN B  1  525 ? -22.551 68.242  56.561 1.00 43.01  ? 1324 GLN D CG    1 
ATOM   9543  C  CD    . GLN B  1  525 ? -22.133 69.430  57.423 1.00 48.95  ? 1324 GLN D CD    1 
ATOM   9544  O  OE1   . GLN B  1  525 ? -21.138 70.112  57.158 1.00 44.78  ? 1324 GLN D OE1   1 
ATOM   9545  N  NE2   . GLN B  1  525 ? -22.893 69.674  58.462 1.00 45.89  ? 1324 GLN D NE2   1 
ATOM   9546  N  N     . THR B  1  526 ? -20.732 63.835  56.136 1.00 36.61  ? 1325 THR D N     1 
ATOM   9547  C  CA    . THR B  1  526 ? -19.547 62.966  56.070 1.00 34.12  ? 1325 THR D CA    1 
ATOM   9548  C  C     . THR B  1  526 ? -20.020 61.583  55.764 1.00 35.18  ? 1325 THR D C     1 
ATOM   9549  O  O     . THR B  1  526 ? -21.206 61.318  55.896 1.00 33.94  ? 1325 THR D O     1 
ATOM   9550  C  CB    . THR B  1  526 ? -18.791 62.946  57.404 1.00 36.83  ? 1325 THR D CB    1 
ATOM   9551  O  OG1   . THR B  1  526 ? -19.544 62.184  58.360 1.00 27.47  ? 1325 THR D OG1   1 
ATOM   9552  C  CG2   . THR B  1  526 ? -18.586 64.364  57.946 1.00 37.85  ? 1325 THR D CG2   1 
ATOM   9553  N  N     . PRO B  1  527 ? -19.109 60.679  55.364 1.00 35.81  ? 1326 PRO D N     1 
ATOM   9554  C  CA    . PRO B  1  527 ? -19.400 59.256  55.144 1.00 30.86  ? 1326 PRO D CA    1 
ATOM   9555  C  C     . PRO B  1  527 ? -19.846 58.486  56.391 1.00 30.93  ? 1326 PRO D C     1 
ATOM   9556  O  O     . PRO B  1  527 ? -20.132 57.319  56.297 1.00 34.65  ? 1326 PRO D O     1 
ATOM   9557  C  CB    . PRO B  1  527 ? -18.078 58.686  54.635 1.00 33.29  ? 1326 PRO D CB    1 
ATOM   9558  C  CG    . PRO B  1  527 ? -17.246 59.855  54.278 1.00 35.18  ? 1326 PRO D CG    1 
ATOM   9559  C  CD    . PRO B  1  527 ? -17.709 61.009  55.079 1.00 33.75  ? 1326 PRO D CD    1 
ATOM   9560  N  N     . LEU B  1  528 ? -19.989 59.148  57.533 1.00 32.97  ? 1327 LEU D N     1 
ATOM   9561  C  CA    . LEU B  1  528 ? -20.509 58.513  58.741 1.00 31.46  ? 1327 LEU D CA    1 
ATOM   9562  C  C     . LEU B  1  528 ? -21.880 57.902  58.438 1.00 32.84  ? 1327 LEU D C     1 
ATOM   9563  O  O     . LEU B  1  528 ? -22.232 56.889  58.976 1.00 34.98  ? 1327 LEU D O     1 
ATOM   9564  C  CB    . LEU B  1  528 ? -20.598 59.545  59.827 1.00 34.61  ? 1327 LEU D CB    1 
ATOM   9565  C  CG    . LEU B  1  528 ? -20.222 59.124  61.230 1.00 42.99  ? 1327 LEU D CG    1 
ATOM   9566  C  CD1   . LEU B  1  528 ? -18.765 58.749  61.326 1.00 36.77  ? 1327 LEU D CD1   1 
ATOM   9567  C  CD2   . LEU B  1  528 ? -20.515 60.271  62.178 1.00 50.89  ? 1327 LEU D CD2   1 
ATOM   9568  N  N     . GLN B  1  529 ? -22.607 58.503  57.498 1.00 34.17  ? 1328 GLN D N     1 
ATOM   9569  C  CA    . GLN B  1  529 ? -23.791 57.952  56.958 1.00 31.11  ? 1328 GLN D CA    1 
ATOM   9570  C  C     . GLN B  1  529 ? -23.457 57.776  55.472 1.00 35.61  ? 1328 GLN D C     1 
ATOM   9571  O  O     . GLN B  1  529 ? -22.981 58.677  54.807 1.00 34.43  ? 1328 GLN D O     1 
ATOM   9572  C  CB    . GLN B  1  529 ? -25.001 58.860  57.131 1.00 28.84  ? 1328 GLN D CB    1 
ATOM   9573  C  CG    . GLN B  1  529 ? -26.231 58.216  56.560 1.00 33.74  ? 1328 GLN D CG    1 
ATOM   9574  C  CD    . GLN B  1  529 ? -27.528 58.965  56.806 1.00 36.72  ? 1328 GLN D CD    1 
ATOM   9575  O  OE1   . GLN B  1  529 ? -27.721 59.574  57.837 1.00 46.54  ? 1328 GLN D OE1   1 
ATOM   9576  N  NE2   . GLN B  1  529 ? -28.437 58.870  55.873 1.00 37.60  ? 1328 GLN D NE2   1 
ATOM   9577  N  N     . THR B  1  530 ? -23.692 56.586  54.947 1.00 33.09  ? 1329 THR D N     1 
ATOM   9578  C  CA    . THR B  1  530 ? -23.390 56.315  53.553 1.00 32.02  ? 1329 THR D CA    1 
ATOM   9579  C  C     . THR B  1  530 ? -24.459 55.424  52.996 1.00 34.61  ? 1329 THR D C     1 
ATOM   9580  O  O     . THR B  1  530 ? -24.973 54.553  53.705 1.00 46.00  ? 1329 THR D O     1 
ATOM   9581  C  CB    . THR B  1  530 ? -22.024 55.554  53.435 1.00 34.54  ? 1329 THR D CB    1 
ATOM   9582  O  OG1   . THR B  1  530 ? -20.972 56.418  53.851 1.00 35.38  ? 1329 THR D OG1   1 
ATOM   9583  C  CG2   . THR B  1  530 ? -21.721 55.222  52.056 1.00 34.49  ? 1329 THR D CG2   1 
ATOM   9584  N  N     . SER B  1  531 ? -24.745 55.577  51.719 1.00 31.90  ? 1330 SER D N     1 
ATOM   9585  C  CA    . SER B  1  531 ? -25.685 54.661  51.093 1.00 33.19  ? 1330 SER D CA    1 
ATOM   9586  C  C     . SER B  1  531 ? -25.064 53.569  50.232 1.00 30.18  ? 1330 SER D C     1 
ATOM   9587  O  O     . SER B  1  531 ? -23.993 53.717  49.696 1.00 32.87  ? 1330 SER D O     1 
ATOM   9588  C  CB    . SER B  1  531 ? -26.805 55.405  50.349 1.00 35.57  ? 1330 SER D CB    1 
ATOM   9589  O  OG    . SER B  1  531 ? -26.266 56.020  49.212 1.00 43.30  ? 1330 SER D OG    1 
ATOM   9590  N  N     . PHE B  1  532 ? -25.748 52.445  50.137 1.00 28.69  ? 1331 PHE D N     1 
ATOM   9591  C  CA    . PHE B  1  532 ? -25.323 51.341  49.302 1.00 27.64  ? 1331 PHE D CA    1 
ATOM   9592  C  C     . PHE B  1  532 ? -26.377 51.204  48.249 1.00 29.85  ? 1331 PHE D C     1 
ATOM   9593  O  O     . PHE B  1  532 ? -27.530 50.907  48.582 1.00 32.36  ? 1331 PHE D O     1 
ATOM   9594  C  CB    . PHE B  1  532 ? -25.272 50.041  50.115 1.00 29.50  ? 1331 PHE D CB    1 
ATOM   9595  C  CG    . PHE B  1  532 ? -24.670 48.895  49.373 1.00 28.57  ? 1331 PHE D CG    1 
ATOM   9596  C  CD1   . PHE B  1  532 ? -25.392 48.276  48.390 1.00 29.85  ? 1331 PHE D CD1   1 
ATOM   9597  C  CD2   . PHE B  1  532 ? -23.331 48.510  49.573 1.00 29.86  ? 1331 PHE D CD2   1 
ATOM   9598  C  CE1   . PHE B  1  532 ? -24.886 47.207  47.683 1.00 33.88  ? 1331 PHE D CE1   1 
ATOM   9599  C  CE2   . PHE B  1  532 ? -22.788 47.448  48.843 1.00 26.85  ? 1331 PHE D CE2   1 
ATOM   9600  C  CZ    . PHE B  1  532 ? -23.561 46.776  47.907 1.00 29.06  ? 1331 PHE D CZ    1 
ATOM   9601  N  N     . GLY B  1  533 ? -26.039 51.443  46.981 1.00 29.69  ? 1332 GLY D N     1 
ATOM   9602  C  CA    . GLY B  1  533 ? -27.063 51.311  45.943 1.00 30.22  ? 1332 GLY D CA    1 
ATOM   9603  C  C     . GLY B  1  533 ? -27.016 49.915  45.341 1.00 31.79  ? 1332 GLY D C     1 
ATOM   9604  O  O     . GLY B  1  533 ? -26.033 49.602  44.619 1.00 28.33  ? 1332 GLY D O     1 
ATOM   9605  N  N     . VAL B  1  534 ? -28.040 49.112  45.600 1.00 30.31  ? 1333 VAL D N     1 
ATOM   9606  C  CA    . VAL B  1  534 ? -28.061 47.757  45.141 1.00 25.94  ? 1333 VAL D CA    1 
ATOM   9607  C  C     . VAL B  1  534 ? -28.404 47.711  43.644 1.00 28.43  ? 1333 VAL D C     1 
ATOM   9608  O  O     . VAL B  1  534 ? -29.420 48.277  43.163 1.00 28.54  ? 1333 VAL D O     1 
ATOM   9609  C  CB    . VAL B  1  534 ? -29.057 46.933  45.926 1.00 24.02  ? 1333 VAL D CB    1 
ATOM   9610  C  CG1   . VAL B  1  534 ? -28.984 45.468  45.472 1.00 26.25  ? 1333 VAL D CG1   1 
ATOM   9611  C  CG2   . VAL B  1  534 ? -28.775 47.028  47.426 1.00 25.16  ? 1333 VAL D CG2   1 
ATOM   9612  N  N     . ASN B  1  535 ? -27.527 47.034  42.935 1.00 29.40  ? 1334 ASN D N     1 
ATOM   9613  C  CA    . ASN B  1  535 ? -27.645 46.805  41.513 1.00 28.78  ? 1334 ASN D CA    1 
ATOM   9614  C  C     . ASN B  1  535 ? -27.251 45.318  41.281 1.00 28.59  ? 1334 ASN D C     1 
ATOM   9615  O  O     . ASN B  1  535 ? -26.119 45.019  40.954 1.00 25.94  ? 1334 ASN D O     1 
ATOM   9616  C  CB    . ASN B  1  535 ? -26.689 47.768  40.785 1.00 29.63  ? 1334 ASN D CB    1 
ATOM   9617  C  CG    . ASN B  1  535 ? -26.989 47.868  39.328 1.00 32.27  ? 1334 ASN D CG    1 
ATOM   9618  O  OD1   . ASN B  1  535 ? -26.117 48.167  38.492 1.00 39.56  ? 1334 ASN D OD1   1 
ATOM   9619  N  ND2   . ASN B  1  535 ? -28.253 47.663  39.005 1.00 30.30  ? 1334 ASN D ND2   1 
ATOM   9620  N  N     . MET B  1  536 ? -28.198 44.409  41.464 1.00 28.76  ? 1335 MET D N     1 
ATOM   9621  C  CA    . MET B  1  536 ? -27.867 42.969  41.471 1.00 30.75  ? 1335 MET D CA    1 
ATOM   9622  C  C     . MET B  1  536 ? -27.775 42.348  40.075 1.00 29.51  ? 1335 MET D C     1 
ATOM   9623  O  O     . MET B  1  536 ? -28.726 41.727  39.622 1.00 27.96  ? 1335 MET D O     1 
ATOM   9624  C  CB    . MET B  1  536 ? -28.861 42.186  42.319 1.00 29.33  ? 1335 MET D CB    1 
ATOM   9625  C  CG    . MET B  1  536 ? -28.968 42.686  43.721 1.00 30.35  ? 1335 MET D CG    1 
ATOM   9626  S  SD    . MET B  1  536 ? -29.298 41.415  44.956 1.00 36.41  ? 1335 MET D SD    1 
ATOM   9627  C  CE    . MET B  1  536 ? -31.064 41.079  44.682 1.00 30.06  ? 1335 MET D CE    1 
ATOM   9628  N  N     . ILE B  1  537 ? -26.626 42.517  39.420 1.00 27.54  ? 1336 ILE D N     1 
ATOM   9629  C  CA    . ILE B  1  537 ? -26.431 41.958  38.091 1.00 28.02  ? 1336 ILE D CA    1 
ATOM   9630  C  C     . ILE B  1  537 ? -25.376 40.861  38.162 1.00 32.29  ? 1336 ILE D C     1 
ATOM   9631  O  O     . ILE B  1  537 ? -24.262 41.082  38.672 1.00 32.96  ? 1336 ILE D O     1 
ATOM   9632  C  CB    . ILE B  1  537 ? -26.011 43.027  37.071 1.00 29.78  ? 1336 ILE D CB    1 
ATOM   9633  C  CG1   . ILE B  1  537 ? -27.172 43.953  36.705 1.00 32.95  ? 1336 ILE D CG1   1 
ATOM   9634  C  CG2   . ILE B  1  537 ? -25.434 42.419  35.821 1.00 27.63  ? 1336 ILE D CG2   1 
ATOM   9635  C  CD1   . ILE B  1  537 ? -26.754 45.233  35.969 1.00 27.63  ? 1336 ILE D CD1   1 
ATOM   9636  N  N     . ALA B  1  538 ? -25.701 39.697  37.621 1.00 30.17  ? 1337 ALA D N     1 
ATOM   9637  C  CA    . ALA B  1  538 ? -24.804 38.530  37.655 1.00 31.42  ? 1337 ALA D CA    1 
ATOM   9638  C  C     . ALA B  1  538 ? -24.957 37.772  36.388 1.00 34.50  ? 1337 ALA D C     1 
ATOM   9639  O  O     . ALA B  1  538 ? -26.000 37.927  35.688 1.00 35.31  ? 1337 ALA D O     1 
ATOM   9640  C  CB    . ALA B  1  538 ? -25.169 37.620  38.791 1.00 32.79  ? 1337 ALA D CB    1 
ATOM   9641  N  N     . LEU B  1  539 ? -23.988 36.908  36.090 1.00 29.74  ? 1338 LEU D N     1 
ATOM   9642  C  CA    . LEU B  1  539 ? -24.075 36.089  34.861 1.00 28.83  ? 1338 LEU D CA    1 
ATOM   9643  C  C     . LEU B  1  539 ? -25.029 34.906  35.079 1.00 32.06  ? 1338 LEU D C     1 
ATOM   9644  O  O     . LEU B  1  539 ? -24.772 34.027  35.898 1.00 32.48  ? 1338 LEU D O     1 
ATOM   9645  C  CB    . LEU B  1  539 ? -22.703 35.578  34.429 1.00 25.87  ? 1338 LEU D CB    1 
ATOM   9646  C  CG    . LEU B  1  539 ? -21.670 36.683  34.062 1.00 27.49  ? 1338 LEU D CG    1 
ATOM   9647  C  CD1   . LEU B  1  539 ? -20.284 36.097  33.853 1.00 21.94  ? 1338 LEU D CD1   1 
ATOM   9648  C  CD2   . LEU B  1  539 ? -22.177 37.537  32.888 1.00 27.28  ? 1338 LEU D CD2   1 
ATOM   9649  N  N     . VAL B  1  540 ? -26.133 34.902  34.344 1.00 34.48  ? 1339 VAL D N     1 
ATOM   9650  C  CA    . VAL B  1  540 ? -27.073 33.782  34.360 1.00 33.11  ? 1339 VAL D CA    1 
ATOM   9651  C  C     . VAL B  1  540 ? -27.027 33.175  32.976 1.00 39.35  ? 1339 VAL D C     1 
ATOM   9652  O  O     . VAL B  1  540 ? -27.278 33.856  31.966 1.00 39.24  ? 1339 VAL D O     1 
ATOM   9653  C  CB    . VAL B  1  540 ? -28.477 34.281  34.694 1.00 33.10  ? 1339 VAL D CB    1 
ATOM   9654  C  CG1   . VAL B  1  540 ? -29.461 33.127  34.750 1.00 31.24  ? 1339 VAL D CG1   1 
ATOM   9655  C  CG2   . VAL B  1  540 ? -28.451 35.056  36.033 1.00 30.09  ? 1339 VAL D CG2   1 
ATOM   9656  N  N     . ASN B  1  541 ? -26.676 31.895  32.902 1.00 37.93  ? 1340 ASN D N     1 
ATOM   9657  C  CA    . ASN B  1  541 ? -26.543 31.192  31.619 1.00 39.41  ? 1340 ASN D CA    1 
ATOM   9658  C  C     . ASN B  1  541 ? -25.636 31.933  30.653 1.00 43.90  ? 1340 ASN D C     1 
ATOM   9659  O  O     . ASN B  1  541 ? -25.925 32.034  29.443 1.00 45.20  ? 1340 ASN D O     1 
ATOM   9660  C  CB    . ASN B  1  541 ? -27.876 30.958  30.888 1.00 45.82  ? 1340 ASN D CB    1 
ATOM   9661  C  CG    . ASN B  1  541 ? -28.852 30.112  31.663 1.00 55.87  ? 1340 ASN D CG    1 
ATOM   9662  O  OD1   . ASN B  1  541 ? -28.481 29.262  32.475 1.00 62.17  ? 1340 ASN D OD1   1 
ATOM   9663  N  ND2   . ASN B  1  541 ? -30.137 30.339  31.403 1.00 64.57  ? 1340 ASN D ND2   1 
ATOM   9664  N  N     . GLY B  1  542 ? -24.550 32.476  31.182 1.00 43.51  ? 1341 GLY D N     1 
ATOM   9665  C  CA    . GLY B  1  542 ? -23.584 33.190  30.359 1.00 46.16  ? 1341 GLY D CA    1 
ATOM   9666  C  C     . GLY B  1  542 ? -23.998 34.562  29.880 1.00 47.62  ? 1341 GLY D C     1 
ATOM   9667  O  O     . GLY B  1  542 ? -23.365 35.119  28.972 1.00 51.53  ? 1341 GLY D O     1 
ATOM   9668  N  N     . ARG B  1  543 ? -25.063 35.124  30.458 1.00 46.21  ? 1342 ARG D N     1 
ATOM   9669  C  CA    . ARG B  1  543 ? -25.482 36.502  30.080 1.00 37.03  ? 1342 ARG D CA    1 
ATOM   9670  C  C     . ARG B  1  543 ? -25.717 37.288  31.320 1.00 33.96  ? 1342 ARG D C     1 
ATOM   9671  O  O     . ARG B  1  543 ? -26.179 36.740  32.301 1.00 27.42  ? 1342 ARG D O     1 
ATOM   9672  C  CB    . ARG B  1  543 ? -26.748 36.507  29.248 1.00 41.57  ? 1342 ARG D CB    1 
ATOM   9673  C  CG    . ARG B  1  543 ? -26.709 35.477  28.155 1.00 53.78  ? 1342 ARG D CG    1 
ATOM   9674  C  CD    . ARG B  1  543 ? -27.976 35.389  27.345 1.00 60.60  ? 1342 ARG D CD    1 
ATOM   9675  N  NE    . ARG B  1  543 ? -27.664 34.486  26.243 1.00 74.52  ? 1342 ARG D NE    1 
ATOM   9676  C  CZ    . ARG B  1  543 ? -28.218 34.521  25.039 1.00 77.20  ? 1342 ARG D CZ    1 
ATOM   9677  N  NH1   . ARG B  1  543 ? -29.138 35.434  24.736 1.00 78.82  ? 1342 ARG D NH1   1 
ATOM   9678  N  NH2   . ARG B  1  543 ? -27.827 33.636  24.133 1.00 86.25  ? 1342 ARG D NH2   1 
ATOM   9679  N  N     . PRO B  1  544 ? -25.409 38.595  31.293 1.00 31.43  ? 1343 PRO D N     1 
ATOM   9680  C  CA    . PRO B  1  544 ? -25.689 39.441  32.443 1.00 27.70  ? 1343 PRO D CA    1 
ATOM   9681  C  C     . PRO B  1  544 ? -27.208 39.545  32.620 1.00 27.97  ? 1343 PRO D C     1 
ATOM   9682  O  O     . PRO B  1  544 ? -27.982 39.683  31.647 1.00 29.30  ? 1343 PRO D O     1 
ATOM   9683  C  CB    . PRO B  1  544 ? -25.153 40.786  32.026 1.00 29.44  ? 1343 PRO D CB    1 
ATOM   9684  C  CG    . PRO B  1  544 ? -25.196 40.775  30.497 1.00 32.92  ? 1343 PRO D CG    1 
ATOM   9685  C  CD    . PRO B  1  544 ? -25.026 39.351  30.085 1.00 30.71  ? 1343 PRO D CD    1 
ATOM   9686  N  N     . LYS B  1  545 ? -27.635 39.544  33.856 1.00 27.19  ? 1344 LYS D N     1 
ATOM   9687  C  CA    . LYS B  1  545 ? -29.067 39.677  34.140 1.00 31.91  ? 1344 LYS D CA    1 
ATOM   9688  C  C     . LYS B  1  545 ? -29.284 40.378  35.486 1.00 30.36  ? 1344 LYS D C     1 
ATOM   9689  O  O     . LYS B  1  545 ? -28.632 40.071  36.470 1.00 29.05  ? 1344 LYS D O     1 
ATOM   9690  C  CB    . LYS B  1  545 ? -29.739 38.299  34.148 1.00 30.53  ? 1344 LYS D CB    1 
ATOM   9691  C  CG    . LYS B  1  545 ? -31.239 38.446  34.170 1.00 37.05  ? 1344 LYS D CG    1 
ATOM   9692  C  CD    . LYS B  1  545 ? -31.951 37.092  34.125 1.00 41.93  ? 1344 LYS D CD    1 
ATOM   9693  C  CE    . LYS B  1  545 ? -33.459 37.299  34.245 1.00 42.68  ? 1344 LYS D CE    1 
ATOM   9694  N  NZ    . LYS B  1  545 ? -34.083 35.947  34.031 1.00 54.02  ? 1344 LYS D NZ    1 
ATOM   9695  N  N     . LEU B  1  546 ? -30.217 41.322  35.510 1.00 31.49  ? 1345 LEU D N     1 
ATOM   9696  C  CA    . LEU B  1  546 ? -30.622 41.957  36.739 1.00 29.49  ? 1345 LEU D CA    1 
ATOM   9697  C  C     . LEU B  1  546 ? -31.551 40.970  37.391 1.00 30.03  ? 1345 LEU D C     1 
ATOM   9698  O  O     . LEU B  1  546 ? -32.518 40.553  36.768 1.00 32.80  ? 1345 LEU D O     1 
ATOM   9699  C  CB    . LEU B  1  546 ? -31.316 43.296  36.444 1.00 29.50  ? 1345 LEU D CB    1 
ATOM   9700  C  CG    . LEU B  1  546 ? -31.737 44.053  37.713 1.00 33.67  ? 1345 LEU D CG    1 
ATOM   9701  C  CD1   . LEU B  1  546 ? -30.497 44.511  38.470 1.00 33.23  ? 1345 LEU D CD1   1 
ATOM   9702  C  CD2   . LEU B  1  546 ? -32.567 45.290  37.358 1.00 34.12  ? 1345 LEU D CD2   1 
ATOM   9703  N  N     . ILE B  1  547 ? -31.268 40.601  38.646 1.00 30.64  ? 1346 ILE D N     1 
ATOM   9704  C  CA    . ILE B  1  547 ? -32.075 39.587  39.323 1.00 31.69  ? 1346 ILE D CA    1 
ATOM   9705  C  C     . ILE B  1  547 ? -32.514 40.008  40.694 1.00 32.96  ? 1346 ILE D C     1 
ATOM   9706  O  O     . ILE B  1  547 ? -31.780 40.725  41.389 1.00 32.40  ? 1346 ILE D O     1 
ATOM   9707  C  CB    . ILE B  1  547 ? -31.314 38.227  39.456 1.00 35.92  ? 1346 ILE D CB    1 
ATOM   9708  C  CG1   . ILE B  1  547 ? -30.004 38.480  40.252 1.00 29.28  ? 1346 ILE D CG1   1 
ATOM   9709  C  CG2   . ILE B  1  547 ? -31.047 37.657  38.060 1.00 39.86  ? 1346 ILE D CG2   1 
ATOM   9710  C  CD1   . ILE B  1  547 ? -29.081 37.315  40.403 1.00 28.60  ? 1346 ILE D CD1   1 
ATOM   9711  N  N     . ASN B  1  548 ? -33.689 39.520  41.126 1.00 34.23  ? 1347 ASN D N     1 
ATOM   9712  C  CA    . ASN B  1  548 ? -34.164 39.813  42.464 1.00 33.07  ? 1347 ASN D CA    1 
ATOM   9713  C  C     . ASN B  1  548 ? -33.637 38.781  43.425 1.00 31.91  ? 1347 ASN D C     1 
ATOM   9714  O  O     . ASN B  1  548 ? -32.885 37.914  43.010 1.00 35.03  ? 1347 ASN D O     1 
ATOM   9715  C  CB    . ASN B  1  548 ? -35.699 39.963  42.492 1.00 33.81  ? 1347 ASN D CB    1 
ATOM   9716  C  CG    . ASN B  1  548 ? -36.435 38.701  42.145 1.00 34.34  ? 1347 ASN D CG    1 
ATOM   9717  O  OD1   . ASN B  1  548 ? -35.987 37.599  42.383 1.00 31.76  ? 1347 ASN D OD1   1 
ATOM   9718  N  ND2   . ASN B  1  548 ? -37.599 38.873  41.608 1.00 34.43  ? 1347 ASN D ND2   1 
ATOM   9719  N  N     . LEU B  1  549 ? -34.013 38.862  44.704 1.00 30.19  ? 1348 LEU D N     1 
ATOM   9720  C  CA    . LEU B  1  549 ? -33.529 37.952  45.702 1.00 30.29  ? 1348 LEU D CA    1 
ATOM   9721  C  C     . LEU B  1  549 ? -33.930 36.520  45.428 1.00 30.25  ? 1348 LEU D C     1 
ATOM   9722  O  O     . LEU B  1  549 ? -33.095 35.613  45.573 1.00 29.34  ? 1348 LEU D O     1 
ATOM   9723  C  CB    . LEU B  1  549 ? -33.988 38.374  47.111 1.00 30.14  ? 1348 LEU D CB    1 
ATOM   9724  C  CG    . LEU B  1  549 ? -33.534 37.474  48.275 1.00 33.10  ? 1348 LEU D CG    1 
ATOM   9725  C  CD1   . LEU B  1  549 ? -32.010 37.550  48.468 1.00 30.66  ? 1348 LEU D CD1   1 
ATOM   9726  C  CD2   . LEU B  1  549 ? -34.249 37.959  49.535 1.00 32.72  ? 1348 LEU D CD2   1 
ATOM   9727  N  N     . LYS B  1  550 ? -35.204 36.321  45.094 1.00 30.22  ? 1349 LYS D N     1 
ATOM   9728  C  CA    . LYS B  1  550 ? -35.689 34.981  44.827 1.00 33.74  ? 1349 LYS D CA    1 
ATOM   9729  C  C     . LYS B  1  550 ? -34.962 34.324  43.651 1.00 31.67  ? 1349 LYS D C     1 
ATOM   9730  O  O     . LYS B  1  550 ? -34.542 33.158  43.747 1.00 30.17  ? 1349 LYS D O     1 
ATOM   9731  C  CB    . LYS B  1  550 ? -37.191 34.945  44.583 1.00 31.22  ? 1349 LYS D CB    1 
ATOM   9732  C  CG    . LYS B  1  550 ? -37.672 33.541  44.248 1.00 30.42  ? 1349 LYS D CG    1 
ATOM   9733  C  CD    . LYS B  1  550 ? -39.177 33.469  44.210 1.00 30.66  ? 1349 LYS D CD    1 
ATOM   9734  C  CE    . LYS B  1  550 ? -39.595 32.059  43.854 1.00 28.90  ? 1349 LYS D CE    1 
ATOM   9735  N  NZ    . LYS B  1  550 ? -41.102 31.959  43.922 1.00 31.64  ? 1349 LYS D NZ    1 
ATOM   9736  N  N     . GLU B  1  551 ? -34.820 35.065  42.565 1.00 28.60  ? 1350 GLU D N     1 
ATOM   9737  C  CA    . GLU B  1  551 ? -34.145 34.551  41.394 1.00 33.48  ? 1350 GLU D CA    1 
ATOM   9738  C  C     . GLU B  1  551 ? -32.664 34.157  41.681 1.00 37.99  ? 1350 GLU D C     1 
ATOM   9739  O  O     . GLU B  1  551 ? -32.185 33.115  41.205 1.00 34.99  ? 1350 GLU D O     1 
ATOM   9740  C  CB    . GLU B  1  551 ? -34.241 35.502  40.231 1.00 34.79  ? 1350 GLU D CB    1 
ATOM   9741  C  CG    . GLU B  1  551 ? -33.640 34.954  38.940 1.00 44.50  ? 1350 GLU D CG    1 
ATOM   9742  C  CD    . GLU B  1  551 ? -33.953 35.810  37.715 1.00 58.31  ? 1350 GLU D CD    1 
ATOM   9743  O  OE1   . GLU B  1  551 ? -34.566 36.911  37.897 1.00 56.13  ? 1350 GLU D OE1   1 
ATOM   9744  O  OE2   . GLU B  1  551 ? -33.556 35.374  36.598 1.00 55.09  ? 1350 GLU D OE2   1 
ATOM   9745  N  N     . ALA B  1  552 ? -31.979 34.968  42.473 1.00 30.75  ? 1351 ALA D N     1 
ATOM   9746  C  CA    . ALA B  1  552 ? -30.588 34.668  42.802 1.00 32.11  ? 1351 ALA D CA    1 
ATOM   9747  C  C     . ALA B  1  552 ? -30.565 33.342  43.594 1.00 32.43  ? 1351 ALA D C     1 
ATOM   9748  O  O     . ALA B  1  552 ? -29.727 32.507  43.380 1.00 30.31  ? 1351 ALA D O     1 
ATOM   9749  C  CB    . ALA B  1  552 ? -29.955 35.786  43.587 1.00 24.98  ? 1351 ALA D CB    1 
ATOM   9750  N  N     . LEU B  1  553 ? -31.525 33.151  44.480 1.00 33.23  ? 1352 LEU D N     1 
ATOM   9751  C  CA    . LEU B  1  553 ? -31.614 31.929  45.285 1.00 35.14  ? 1352 LEU D CA    1 
ATOM   9752  C  C     . LEU B  1  553 ? -32.060 30.690  44.470 1.00 34.09  ? 1352 LEU D C     1 
ATOM   9753  O  O     . LEU B  1  553 ? -31.588 29.601  44.695 1.00 34.28  ? 1352 LEU D O     1 
ATOM   9754  C  CB    . LEU B  1  553 ? -32.536 32.128  46.480 1.00 32.37  ? 1352 LEU D CB    1 
ATOM   9755  C  CG    . LEU B  1  553 ? -32.135 33.129  47.555 1.00 31.58  ? 1352 LEU D CG    1 
ATOM   9756  C  CD1   . LEU B  1  553 ? -33.355 33.405  48.423 1.00 28.62  ? 1352 LEU D CD1   1 
ATOM   9757  C  CD2   . LEU B  1  553 ? -31.002 32.580  48.388 1.00 30.81  ? 1352 LEU D CD2   1 
ATOM   9758  N  N     . VAL B  1  554 ? -32.945 30.882  43.506 1.00 36.56  ? 1353 VAL D N     1 
ATOM   9759  C  CA    . VAL B  1  554 ? -33.391 29.813  42.630 1.00 32.50  ? 1353 VAL D CA    1 
ATOM   9760  C  C     . VAL B  1  554 ? -32.237 29.315  41.791 1.00 32.87  ? 1353 VAL D C     1 
ATOM   9761  O  O     . VAL B  1  554 ? -32.098 28.116  41.587 1.00 31.05  ? 1353 VAL D O     1 
ATOM   9762  C  CB    . VAL B  1  554 ? -34.573 30.228  41.767 1.00 31.34  ? 1353 VAL D CB    1 
ATOM   9763  C  CG1   . VAL B  1  554 ? -34.813 29.239  40.616 1.00 28.73  ? 1353 VAL D CG1   1 
ATOM   9764  C  CG2   . VAL B  1  554 ? -35.814 30.398  42.654 1.00 31.09  ? 1353 VAL D CG2   1 
ATOM   9765  N  N     . HIS B  1  555 ? -31.409 30.223  41.301 1.00 32.43  ? 1354 HIS D N     1 
ATOM   9766  C  CA    . HIS B  1  555 ? -30.274 29.802  40.519 1.00 33.41  ? 1354 HIS D CA    1 
ATOM   9767  C  C     . HIS B  1  555 ? -29.269 29.089  41.383 1.00 35.34  ? 1354 HIS D C     1 
ATOM   9768  O  O     . HIS B  1  555 ? -28.716 28.092  40.938 1.00 35.63  ? 1354 HIS D O     1 
ATOM   9769  C  CB    . HIS B  1  555 ? -29.668 30.945  39.714 1.00 41.50  ? 1354 HIS D CB    1 
ATOM   9770  C  CG    . HIS B  1  555 ? -30.573 31.426  38.618 1.00 44.43  ? 1354 HIS D CG    1 
ATOM   9771  N  ND1   . HIS B  1  555 ? -31.082 30.586  37.662 1.00 42.61  ? 1354 HIS D ND1   1 
ATOM   9772  C  CD2   . HIS B  1  555 ? -31.057 32.655  38.332 1.00 41.07  ? 1354 HIS D CD2   1 
ATOM   9773  C  CE1   . HIS B  1  555 ? -31.864 31.267  36.848 1.00 40.88  ? 1354 HIS D CE1   1 
ATOM   9774  N  NE2   . HIS B  1  555 ? -31.858 32.525  37.230 1.00 41.62  ? 1354 HIS D NE2   1 
ATOM   9775  N  N     . TYR B  1  556 ? -29.069 29.548  42.620 1.00 32.40  ? 1355 TYR D N     1 
ATOM   9776  C  CA    . TYR B  1  556 ? -28.197 28.839  43.525 1.00 30.87  ? 1355 TYR D CA    1 
ATOM   9777  C  C     . TYR B  1  556 ? -28.663 27.414  43.850 1.00 32.33  ? 1355 TYR D C     1 
ATOM   9778  O  O     . TYR B  1  556 ? -27.846 26.480  43.874 1.00 28.95  ? 1355 TYR D O     1 
ATOM   9779  C  CB    . TYR B  1  556 ? -27.961 29.594  44.825 1.00 28.77  ? 1355 TYR D CB    1 
ATOM   9780  C  CG    . TYR B  1  556 ? -27.046 28.828  45.698 1.00 27.93  ? 1355 TYR D CG    1 
ATOM   9781  C  CD1   . TYR B  1  556 ? -25.757 28.560  45.300 1.00 28.94  ? 1355 TYR D CD1   1 
ATOM   9782  C  CD2   . TYR B  1  556 ? -27.504 28.273  46.855 1.00 30.95  ? 1355 TYR D CD2   1 
ATOM   9783  C  CE1   . TYR B  1  556 ? -24.929 27.807  46.091 1.00 29.27  ? 1355 TYR D CE1   1 
ATOM   9784  C  CE2   . TYR B  1  556 ? -26.692 27.529  47.671 1.00 31.41  ? 1355 TYR D CE2   1 
ATOM   9785  C  CZ    . TYR B  1  556 ? -25.409 27.291  47.253 1.00 30.06  ? 1355 TYR D CZ    1 
ATOM   9786  O  OH    . TYR B  1  556 ? -24.574 26.541  48.021 1.00 32.40  ? 1355 TYR D OH    1 
ATOM   9787  N  N     . LEU B  1  557 ? -29.952 27.261  44.121 1.00 29.82  ? 1356 LEU D N     1 
ATOM   9788  C  CA    . LEU B  1  557 ? -30.460 25.959  44.461 1.00 32.37  ? 1356 LEU D CA    1 
ATOM   9789  C  C     . LEU B  1  557 ? -30.437 25.022  43.256 1.00 34.68  ? 1356 LEU D C     1 
ATOM   9790  O  O     . LEU B  1  557 ? -30.077 23.919  43.387 1.00 36.98  ? 1356 LEU D O     1 
ATOM   9791  C  CB    . LEU B  1  557 ? -31.854 26.079  45.072 1.00 31.98  ? 1356 LEU D CB    1 
ATOM   9792  C  CG    . LEU B  1  557 ? -32.630 24.791  45.320 1.00 27.56  ? 1356 LEU D CG    1 
ATOM   9793  C  CD1   . LEU B  1  557 ? -32.013 23.960  46.409 1.00 29.47  ? 1356 LEU D CD1   1 
ATOM   9794  C  CD2   . LEU B  1  557 ? -33.996 25.189  45.790 1.00 29.38  ? 1356 LEU D CD2   1 
ATOM   9795  N  N     A GLU B  1  558 ? -30.733 25.459  42.047 0.50 30.88  ? 1357 GLU D N     1 
ATOM   9796  N  N     B GLU B  1  558 ? -30.717 25.464  42.049 0.50 32.83  ? 1357 GLU D N     1 
ATOM   9797  C  CA    A GLU B  1  558 ? -30.616 24.507  40.961 0.50 32.00  ? 1357 GLU D CA    1 
ATOM   9798  C  CA    B GLU B  1  558 ? -30.607 24.539  40.938 0.50 35.15  ? 1357 GLU D CA    1 
ATOM   9799  C  C     A GLU B  1  558 ? -29.201 23.988  40.770 0.50 31.88  ? 1357 GLU D C     1 
ATOM   9800  C  C     B GLU B  1  558 ? -29.204 23.986  40.787 0.50 33.79  ? 1357 GLU D C     1 
ATOM   9801  O  O     A GLU B  1  558 ? -28.994 22.836  40.478 0.50 35.16  ? 1357 GLU D O     1 
ATOM   9802  O  O     B GLU B  1  558 ? -29.004 22.835  40.488 0.50 37.08  ? 1357 GLU D O     1 
ATOM   9803  C  CB    A GLU B  1  558 ? -31.078 25.144  39.710 0.50 32.30  ? 1357 GLU D CB    1 
ATOM   9804  C  CB    B GLU B  1  558 ? -30.829 25.322  39.719 0.50 38.88  ? 1357 GLU D CB    1 
ATOM   9805  C  CG    A GLU B  1  558 ? -32.526 24.824  39.386 0.50 35.05  ? 1357 GLU D CG    1 
ATOM   9806  C  CG    B GLU B  1  558 ? -31.973 24.891  38.844 0.50 45.24  ? 1357 GLU D CG    1 
ATOM   9807  C  CD    A GLU B  1  558 ? -32.822 23.315  39.315 0.50 34.90  ? 1357 GLU D CD    1 
ATOM   9808  C  CD    B GLU B  1  558 ? -33.143 25.846  38.990 0.50 49.48  ? 1357 GLU D CD    1 
ATOM   9809  O  OE1   A GLU B  1  558 ? -32.021 22.523  38.744 0.50 33.08  ? 1357 GLU D OE1   1 
ATOM   9810  O  OE1   B GLU B  1  558 ? -33.741 25.874  40.090 0.50 54.94  ? 1357 GLU D OE1   1 
ATOM   9811  O  OE2   A GLU B  1  558 ? -33.873 22.929  39.841 0.50 32.67  ? 1357 GLU D OE2   1 
ATOM   9812  O  OE2   B GLU B  1  558 ? -33.454 26.577  38.007 0.50 50.43  ? 1357 GLU D OE2   1 
ATOM   9813  N  N     . HIS B  1  559 ? -28.235 24.866  40.934 1.00 30.39  ? 1358 HIS D N     1 
ATOM   9814  C  CA    . HIS B  1  559 ? -26.875 24.507  40.869 1.00 29.72  ? 1358 HIS D CA    1 
ATOM   9815  C  C     . HIS B  1  559 ? -26.488 23.424  41.882 1.00 31.69  ? 1358 HIS D C     1 
ATOM   9816  O  O     . HIS B  1  559 ? -25.848 22.484  41.503 1.00 31.77  ? 1358 HIS D O     1 
ATOM   9817  C  CB    . HIS B  1  559 ? -26.058 25.762  41.057 1.00 27.28  ? 1358 HIS D CB    1 
ATOM   9818  C  CG    . HIS B  1  559 ? -24.573 25.559  41.022 1.00 31.68  ? 1358 HIS D CG    1 
ATOM   9819  N  ND1   . HIS B  1  559 ? -23.896 25.076  39.916 1.00 30.88  ? 1358 HIS D ND1   1 
ATOM   9820  C  CD2   . HIS B  1  559 ? -23.615 25.812  41.961 1.00 35.84  ? 1358 HIS D CD2   1 
ATOM   9821  C  CE1   . HIS B  1  559 ? -22.595 25.020  40.185 1.00 30.92  ? 1358 HIS D CE1   1 
ATOM   9822  N  NE2   . HIS B  1  559 ? -22.394 25.460  41.418 1.00 30.17  ? 1358 HIS D NE2   1 
ATOM   9823  N  N     . GLN B  1  560 ? -26.928 23.569  43.146 1.00 28.18  ? 1359 GLN D N     1 
ATOM   9824  C  CA    . GLN B  1  560 ? -26.651 22.596  44.177 1.00 31.37  ? 1359 GLN D CA    1 
ATOM   9825  C  C     . GLN B  1  560 ? -27.290 21.235  43.849 1.00 34.00  ? 1359 GLN D C     1 
ATOM   9826  O  O     . GLN B  1  560 ? -26.702 20.211  44.110 1.00 32.40  ? 1359 GLN D O     1 
ATOM   9827  C  CB    . GLN B  1  560 ? -27.122 23.077  45.559 1.00 28.80  ? 1359 GLN D CB    1 
ATOM   9828  C  CG    . GLN B  1  560 ? -26.360 24.257  46.109 1.00 30.57  ? 1359 GLN D CG    1 
ATOM   9829  C  CD    . GLN B  1  560 ? -24.885 24.023  45.970 1.00 31.60  ? 1359 GLN D CD    1 
ATOM   9830  O  OE1   . GLN B  1  560 ? -24.257 23.340  46.805 1.00 31.95  ? 1359 GLN D OE1   1 
ATOM   9831  N  NE2   . GLN B  1  560 ? -24.309 24.569  44.882 1.00 27.90  ? 1359 GLN D NE2   1 
ATOM   9832  N  N     . LYS B  1  561 ? -28.485 21.248  43.272 1.00 30.53  ? 1360 LYS D N     1 
ATOM   9833  C  CA    . LYS B  1  561 ? -29.101 20.007  42.876 1.00 34.43  ? 1360 LYS D CA    1 
ATOM   9834  C  C     . LYS B  1  561 ? -28.303 19.355  41.770 1.00 33.46  ? 1360 LYS D C     1 
ATOM   9835  O  O     . LYS B  1  561 ? -28.092 18.170  41.810 1.00 35.51  ? 1360 LYS D O     1 
ATOM   9836  C  CB    . LYS B  1  561 ? -30.539 20.214  42.443 1.00 32.79  ? 1360 LYS D CB    1 
ATOM   9837  C  CG    . LYS B  1  561 ? -31.411 20.488  43.649 1.00 39.39  ? 1360 LYS D CG    1 
ATOM   9838  C  CD    . LYS B  1  561 ? -32.709 21.184  43.298 1.00 47.61  ? 1360 LYS D CD    1 
ATOM   9839  C  CE    . LYS B  1  561 ? -33.569 20.448  42.282 1.00 42.90  ? 1360 LYS D CE    1 
ATOM   9840  N  NZ    . LYS B  1  561 ? -34.915 21.009  42.522 1.00 58.39  ? 1360 LYS D NZ    1 
ATOM   9841  N  N     . THR B  1  562 ? -27.835 20.132  40.811 1.00 29.88  ? 1361 THR D N     1 
ATOM   9842  C  CA    . THR B  1  562 ? -27.075 19.578  39.727 1.00 34.04  ? 1361 THR D CA    1 
ATOM   9843  C  C     . THR B  1  562 ? -25.757 19.045  40.246 1.00 37.62  ? 1361 THR D C     1 
ATOM   9844  O  O     . THR B  1  562 ? -25.358 17.959  39.859 1.00 39.71  ? 1361 THR D O     1 
ATOM   9845  C  CB    . THR B  1  562 ? -26.879 20.569  38.582 1.00 33.43  ? 1361 THR D CB    1 
ATOM   9846  O  OG1   . THR B  1  562 ? -28.112 20.710  37.899 1.00 37.38  ? 1361 THR D OG1   1 
ATOM   9847  C  CG2   . THR B  1  562 ? -25.895 20.083  37.581 1.00 36.02  ? 1361 THR D CG2   1 
ATOM   9848  N  N     . VAL B  1  563 ? -25.091 19.795  41.110 1.00 37.78  ? 1362 VAL D N     1 
ATOM   9849  C  CA    . VAL B  1  563 ? -23.791 19.373  41.664 1.00 37.20  ? 1362 VAL D CA    1 
ATOM   9850  C  C     . VAL B  1  563 ? -23.944 18.053  42.456 1.00 44.93  ? 1362 VAL D C     1 
ATOM   9851  O  O     . VAL B  1  563 ? -23.168 17.139  42.269 1.00 40.76  ? 1362 VAL D O     1 
ATOM   9852  C  CB    . VAL B  1  563 ? -23.177 20.487  42.570 1.00 34.94  ? 1362 VAL D CB    1 
ATOM   9853  C  CG1   . VAL B  1  563 ? -22.107 19.945  43.521 1.00 28.73  ? 1362 VAL D CG1   1 
ATOM   9854  C  CG2   . VAL B  1  563 ? -22.685 21.657  41.720 1.00 26.45  ? 1362 VAL D CG2   1 
ATOM   9855  N  N     . VAL B  1  564 ? -24.930 17.969  43.357 1.00 39.65  ? 1363 VAL D N     1 
ATOM   9856  C  CA    . VAL B  1  564 ? -25.107 16.788  44.184 1.00 40.89  ? 1363 VAL D CA    1 
ATOM   9857  C  C     . VAL B  1  564 ? -25.494 15.559  43.366 1.00 40.50  ? 1363 VAL D C     1 
ATOM   9858  O  O     . VAL B  1  564 ? -25.002 14.460  43.631 1.00 39.43  ? 1363 VAL D O     1 
ATOM   9859  C  CB    . VAL B  1  564 ? -26.071 17.034  45.355 1.00 35.51  ? 1363 VAL D CB    1 
ATOM   9860  C  CG1   . VAL B  1  564 ? -26.433 15.757  46.082 1.00 33.47  ? 1363 VAL D CG1   1 
ATOM   9861  C  CG2   . VAL B  1  564 ? -25.446 18.001  46.320 1.00 32.19  ? 1363 VAL D CG2   1 
ATOM   9862  N  N     . ARG B  1  565 ? -26.347 15.765  42.380 1.00 38.32  ? 1364 ARG D N     1 
ATOM   9863  C  CA    . ARG B  1  565 ? -26.768 14.692  41.512 1.00 40.91  ? 1364 ARG D CA    1 
ATOM   9864  C  C     . ARG B  1  565 ? -25.583 14.146  40.715 1.00 38.68  ? 1364 ARG D C     1 
ATOM   9865  O  O     . ARG B  1  565 ? -25.467 12.952  40.527 1.00 40.77  ? 1364 ARG D O     1 
ATOM   9866  C  CB    . ARG B  1  565 ? -27.852 15.133  40.553 1.00 37.45  ? 1364 ARG D CB    1 
ATOM   9867  C  CG    . ARG B  1  565 ? -28.339 13.984  39.651 1.00 39.90  ? 1364 ARG D CG    1 
ATOM   9868  C  CD    . ARG B  1  565 ? -29.273 14.404  38.546 1.00 42.70  ? 1364 ARG D CD    1 
ATOM   9869  N  NE    . ARG B  1  565 ? -30.506 14.944  39.136 1.00 56.44  ? 1364 ARG D NE    1 
ATOM   9870  C  CZ    . ARG B  1  565 ? -30.877 16.234  39.082 1.00 61.00  ? 1364 ARG D CZ    1 
ATOM   9871  N  NH1   . ARG B  1  565 ? -32.010 16.609  39.660 1.00 61.36  ? 1364 ARG D NH1   1 
ATOM   9872  N  NH2   . ARG B  1  565 ? -30.127 17.153  38.458 1.00 58.90  ? 1364 ARG D NH2   1 
ATOM   9873  N  N     . ARG B  1  566 ? -24.733 15.027  40.226 1.00 42.36  ? 1365 ARG D N     1 
ATOM   9874  C  CA    . ARG B  1  566 ? -23.598 14.658  39.423 1.00 37.96  ? 1365 ARG D CA    1 
ATOM   9875  C  C     . ARG B  1  566 ? -22.561 13.961  40.275 1.00 39.51  ? 1365 ARG D C     1 
ATOM   9876  O  O     . ARG B  1  566 ? -21.946 13.007  39.805 1.00 35.93  ? 1365 ARG D O     1 
ATOM   9877  C  CB    . ARG B  1  566 ? -23.001 15.865  38.714 1.00 38.68  ? 1365 ARG D CB    1 
ATOM   9878  C  CG    . ARG B  1  566 ? -23.692 16.201  37.401 1.00 37.44  ? 1365 ARG D CG    1 
ATOM   9879  C  CD    . ARG B  1  566 ? -23.198 17.514  36.834 1.00 37.15  ? 1365 ARG D CD    1 
ATOM   9880  N  NE    . ARG B  1  566 ? -21.853 17.398  36.287 1.00 38.97  ? 1365 ARG D NE    1 
ATOM   9881  C  CZ    . ARG B  1  566 ? -21.397 18.148  35.302 1.00 32.84  ? 1365 ARG D CZ    1 
ATOM   9882  N  NH1   . ARG B  1  566 ? -22.134 19.094  34.786 1.00 35.30  ? 1365 ARG D NH1   1 
ATOM   9883  N  NH2   . ARG B  1  566 ? -20.191 17.982  34.862 1.00 30.74  ? 1365 ARG D NH2   1 
ATOM   9884  N  N     . ARG B  1  567 ? -22.360 14.434  41.507 1.00 36.40  ? 1366 ARG D N     1 
ATOM   9885  C  CA    . ARG B  1  567 ? -21.403 13.842  42.391 1.00 34.80  ? 1366 ARG D CA    1 
ATOM   9886  C  C     . ARG B  1  567 ? -21.862 12.394  42.689 1.00 37.34  ? 1366 ARG D C     1 
ATOM   9887  O  O     . ARG B  1  567 ? -21.058 11.496  42.761 1.00 39.27  ? 1366 ARG D O     1 
ATOM   9888  C  CB    . ARG B  1  567 ? -21.367 14.621  43.691 1.00 30.54  ? 1366 ARG D CB    1 
ATOM   9889  C  CG    . ARG B  1  567 ? -20.333 14.127  44.673 1.00 27.31  ? 1366 ARG D CG    1 
ATOM   9890  C  CD    . ARG B  1  567 ? -20.562 14.622  46.066 1.00 28.97  ? 1366 ARG D CD    1 
ATOM   9891  N  NE    . ARG B  1  567 ? -21.801 14.131  46.636 1.00 35.45  ? 1366 ARG D NE    1 
ATOM   9892  C  CZ    . ARG B  1  567 ? -22.443 14.716  47.648 1.00 37.86  ? 1366 ARG D CZ    1 
ATOM   9893  N  NH1   . ARG B  1  567 ? -21.968 15.851  48.169 1.00 35.34  ? 1366 ARG D NH1   1 
ATOM   9894  N  NH2   . ARG B  1  567 ? -23.581 14.195  48.107 1.00 30.06  ? 1366 ARG D NH2   1 
ATOM   9895  N  N     . THR B  1  568 ? -23.153 12.217  42.890 1.00 37.22  ? 1367 THR D N     1 
ATOM   9896  C  CA    . THR B  1  568 ? -23.711 10.956  43.215 1.00 33.32  ? 1367 THR D CA    1 
ATOM   9897  C  C     . THR B  1  568 ? -23.554 10.012  42.015 1.00 37.77  ? 1367 THR D C     1 
ATOM   9898  O  O     . THR B  1  568 ? -23.186 8.873   42.204 1.00 35.95  ? 1367 THR D O     1 
ATOM   9899  C  CB    . THR B  1  568 ? -25.207 11.143  43.600 1.00 37.96  ? 1367 THR D CB    1 
ATOM   9900  O  OG1   . THR B  1  568 ? -25.283 11.959  44.758 1.00 34.07  ? 1367 THR D OG1   1 
ATOM   9901  C  CG2   . THR B  1  568 ? -25.880 9.837   43.942 1.00 33.04  ? 1367 THR D CG2   1 
ATOM   9902  N  N     . GLN B  1  569 ? -23.793 10.498  40.802 1.00 34.05  ? 1368 GLN D N     1 
ATOM   9903  C  CA    . GLN B  1  569 ? -23.592 9.689   39.610 1.00 38.44  ? 1368 GLN D CA    1 
ATOM   9904  C  C     . GLN B  1  569 ? -22.137 9.306   39.415 1.00 41.42  ? 1368 GLN D C     1 
ATOM   9905  O  O     . GLN B  1  569 ? -21.832 8.168   39.034 1.00 45.65  ? 1368 GLN D O     1 
ATOM   9906  C  CB    . GLN B  1  569 ? -24.078 10.382  38.354 1.00 38.49  ? 1368 GLN D CB    1 
ATOM   9907  C  CG    . GLN B  1  569 ? -25.582 10.298  38.188 1.00 50.20  ? 1368 GLN D CG    1 
ATOM   9908  C  CD    . GLN B  1  569 ? -26.175 11.427  37.331 1.00 57.01  ? 1368 GLN D CD    1 
ATOM   9909  O  OE1   . GLN B  1  569 ? -27.362 11.410  37.032 1.00 65.23  ? 1368 GLN D OE1   1 
ATOM   9910  N  NE2   . GLN B  1  569 ? -25.365 12.392  36.929 1.00 53.58  ? 1368 GLN D NE2   1 
ATOM   9911  N  N     . TYR B  1  570 ? -21.241 10.264  39.666 1.00 38.38  ? 1369 TYR D N     1 
ATOM   9912  C  CA    . TYR B  1  570 ? -19.828 10.037  39.502 1.00 36.22  ? 1369 TYR D CA    1 
ATOM   9913  C  C     . TYR B  1  570 ? -19.380 8.990   40.497 1.00 35.63  ? 1369 TYR D C     1 
ATOM   9914  O  O     . TYR B  1  570 ? -18.610 8.102   40.150 1.00 38.28  ? 1369 TYR D O     1 
ATOM   9915  C  CB    . TYR B  1  570 ? -19.025 11.338  39.673 1.00 35.67  ? 1369 TYR D CB    1 
ATOM   9916  C  CG    . TYR B  1  570 ? -17.541 11.105  39.908 1.00 32.55  ? 1369 TYR D CG    1 
ATOM   9917  C  CD1   . TYR B  1  570 ? -17.062 10.846  41.160 1.00 33.47  ? 1369 TYR D CD1   1 
ATOM   9918  C  CD2   . TYR B  1  570 ? -16.650 11.139  38.874 1.00 35.59  ? 1369 TYR D CD2   1 
ATOM   9919  C  CE1   . TYR B  1  570 ? -15.724 10.628  41.394 1.00 35.11  ? 1369 TYR D CE1   1 
ATOM   9920  C  CE2   . TYR B  1  570 ? -15.291 10.921  39.080 1.00 37.59  ? 1369 TYR D CE2   1 
ATOM   9921  C  CZ    . TYR B  1  570 ? -14.854 10.662  40.359 1.00 36.52  ? 1369 TYR D CZ    1 
ATOM   9922  O  OH    . TYR B  1  570 ? -13.525 10.426  40.635 1.00 39.13  ? 1369 TYR D OH    1 
ATOM   9923  N  N     . ASN B  1  571 ? -19.850 9.118   41.736 1.00 34.13  ? 1370 ASN D N     1 
ATOM   9924  C  CA    . ASN B  1  571 ? -19.459 8.213   42.779 1.00 35.37  ? 1370 ASN D CA    1 
ATOM   9925  C  C     . ASN B  1  571 ? -19.991 6.803   42.530 1.00 39.37  ? 1370 ASN D C     1 
ATOM   9926  O  O     . ASN B  1  571 ? -19.334 5.840   42.900 1.00 36.18  ? 1370 ASN D O     1 
ATOM   9927  C  CB    . ASN B  1  571 ? -19.902 8.731   44.133 1.00 39.54  ? 1370 ASN D CB    1 
ATOM   9928  C  CG    . ASN B  1  571 ? -18.900 9.723   44.740 1.00 43.98  ? 1370 ASN D CG    1 
ATOM   9929  O  OD1   . ASN B  1  571 ? -17.700 9.472   44.792 1.00 46.91  ? 1370 ASN D OD1   1 
ATOM   9930  N  ND2   . ASN B  1  571 ? -19.398 10.848  45.201 1.00 40.74  ? 1370 ASN D ND2   1 
ATOM   9931  N  N     . LEU B  1  572 ? -21.159 6.691   41.895 1.00 38.99  ? 1371 LEU D N     1 
ATOM   9932  C  CA    . LEU B  1  572 ? -21.712 5.410   41.498 1.00 39.08  ? 1371 LEU D CA    1 
ATOM   9933  C  C     . LEU B  1  572 ? -20.883 4.701   40.411 1.00 41.69  ? 1371 LEU D C     1 
ATOM   9934  O  O     . LEU B  1  572 ? -20.633 3.513   40.521 1.00 38.41  ? 1371 LEU D O     1 
ATOM   9935  C  CB    . LEU B  1  572 ? -23.168 5.545   41.049 1.00 37.01  ? 1371 LEU D CB    1 
ATOM   9936  C  CG    . LEU B  1  572 ? -23.892 4.217   40.707 1.00 37.02  ? 1371 LEU D CG    1 
ATOM   9937  C  CD1   . LEU B  1  572 ? -23.899 3.323   41.934 1.00 32.37  ? 1371 LEU D CD1   1 
ATOM   9938  C  CD2   . LEU B  1  572 ? -25.330 4.477   40.264 1.00 33.19  ? 1371 LEU D CD2   1 
ATOM   9939  N  N     . ARG B  1  573 ? -20.465 5.416   39.376 1.00 38.60  ? 1372 ARG D N     1 
ATOM   9940  C  CA    . ARG B  1  573 ? -19.700 4.798   38.318 1.00 36.13  ? 1372 ARG D CA    1 
ATOM   9941  C  C     . ARG B  1  573 ? -18.385 4.330   38.890 1.00 39.32  ? 1372 ARG D C     1 
ATOM   9942  O  O     . ARG B  1  573 ? -17.938 3.229   38.571 1.00 39.87  ? 1372 ARG D O     1 
ATOM   9943  C  CB    . ARG B  1  573 ? -19.344 5.750   37.196 1.00 34.06  ? 1372 ARG D CB    1 
ATOM   9944  C  CG    . ARG B  1  573 ? -20.389 6.697   36.738 1.00 40.50  ? 1372 ARG D CG    1 
ATOM   9945  C  CD    . ARG B  1  573 ? -19.942 7.328   35.426 1.00 47.31  ? 1372 ARG D CD    1 
ATOM   9946  N  NE    . ARG B  1  573 ? -19.004 8.451   35.576 1.00 45.85  ? 1372 ARG D NE    1 
ATOM   9947  C  CZ    . ARG B  1  573 ? -19.382 9.722   35.784 1.00 44.84  ? 1372 ARG D CZ    1 
ATOM   9948  N  NH1   . ARG B  1  573 ? -20.660 10.075  35.816 1.00 39.93  ? 1372 ARG D NH1   1 
ATOM   9949  N  NH2   . ARG B  1  573 ? -18.475 10.658  35.931 1.00 43.92  ? 1372 ARG D NH2   1 
ATOM   9950  N  N     A LYS B  1  574 ? -17.779 5.178   39.720 0.50 37.22  ? 1373 LYS D N     1 
ATOM   9951  N  N     B LYS B  1  574 ? -17.738 5.172   39.695 0.50 37.52  ? 1373 LYS D N     1 
ATOM   9952  C  CA    A LYS B  1  574 ? -16.478 4.890   40.291 0.50 39.10  ? 1373 LYS D CA    1 
ATOM   9953  C  CA    B LYS B  1  574 ? -16.442 4.820   40.255 0.50 39.60  ? 1373 LYS D CA    1 
ATOM   9954  C  C     A LYS B  1  574 ? -16.532 3.665   41.205 0.50 40.21  ? 1373 LYS D C     1 
ATOM   9955  C  C     B LYS B  1  574 ? -16.528 3.634   41.213 0.50 40.44  ? 1373 LYS D C     1 
ATOM   9956  O  O     A LYS B  1  574 ? -15.613 2.821   41.189 0.50 40.52  ? 1373 LYS D O     1 
ATOM   9957  O  O     B LYS B  1  574 ? -15.598 2.822   41.274 0.50 40.74  ? 1373 LYS D O     1 
ATOM   9958  C  CB    A LYS B  1  574 ? -15.928 6.099   41.052 0.50 36.92  ? 1373 LYS D CB    1 
ATOM   9959  C  CB    B LYS B  1  574 ? -15.788 6.017   40.947 0.50 37.53  ? 1373 LYS D CB    1 
ATOM   9960  C  CG    A LYS B  1  574 ? -14.590 5.827   41.752 0.50 35.97  ? 1373 LYS D CG    1 
ATOM   9961  C  CG    B LYS B  1  574 ? -15.659 7.240   40.058 0.50 37.84  ? 1373 LYS D CG    1 
ATOM   9962  C  CD    A LYS B  1  574 ? -14.128 7.017   42.583 0.50 37.58  ? 1373 LYS D CD    1 
ATOM   9963  C  CD    B LYS B  1  574 ? -14.445 7.228   39.134 0.50 34.12  ? 1373 LYS D CD    1 
ATOM   9964  C  CE    A LYS B  1  574 ? -12.687 6.827   42.970 0.50 35.63  ? 1373 LYS D CE    1 
ATOM   9965  C  CE    B LYS B  1  574 ? -14.932 7.658   37.773 0.50 35.58  ? 1373 LYS D CE    1 
ATOM   9966  N  NZ    A LYS B  1  574 ? -12.630 6.869   44.447 0.50 38.09  ? 1373 LYS D NZ    1 
ATOM