data_1M1E
# 
_entry.id   1M1E 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.386 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   1M1E         pdb_00001m1e 10.2210/pdb1m1e/pdb 
RCSB  RCSB016477   ?            ?                   
WWPDB D_1000016477 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2002-10-16 
2 'Structure model' 1 1 2008-04-28 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2024-02-14 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Data collection'           
4 4 'Structure model' 'Database references'       
5 4 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' chem_comp_atom                
2 4 'Structure model' chem_comp_bond                
3 4 'Structure model' database_2                    
4 4 'Structure model' pdbx_initial_refinement_model 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_database_2.pdbx_DOI'                
2 4 'Structure model' '_database_2.pdbx_database_accession' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1M1E 
_pdbx_database_status.recvd_initial_deposition_date   2002-06-18 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Daniels, D.L.' 1 
'Weis, W.I.'    2 
# 
_citation.id                        primary 
_citation.title                     
;ICAT inhibits Beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules.
;
_citation.journal_abbrev            Mol.Cell 
_citation.journal_volume            10 
_citation.page_first                573 
_citation.page_last                 584 
_citation.year                      2002 
_citation.journal_id_ASTM           MOCEFL 
_citation.country                   US 
_citation.journal_id_ISSN           1097-2765 
_citation.journal_id_CSD            2168 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12408825 
_citation.pdbx_database_id_DOI      '10.1016/S1097-2765(02)00631-7' 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Daniels, D.L.' 1 ? 
primary 'Weis, W.I.'    2 ? 
# 
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 Beta-catenin 58844.117 1   ? ? 'Armadillo Repeat Region (RESIDUES 134-671)' ? 
2 polymer man ICAT         9181.345  1   ? ? ?                                            ? 
3 water   nat water        18.015    310 ? ? ?                                            ? 
# 
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 
;HAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARC
TAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKF
LAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDP
SQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLR
AGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAI
PRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRV
AAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYK
;
;HAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARC
TAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKF
LAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDP
SQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLR
AGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAI
PRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRV
AAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYK
;
A ? 
2 'polypeptide(L)' no no 
;MNREGAPGKSPEEMYIQQKVRVLLMLRKMGSNLTASEEEFLRTYAGVVNSQLSQLPPHSIDQGAEDVVMAFSRSETEDRR
Q
;
;MNREGAPGKSPEEMYIQQKVRVLLMLRKMGSNLTASEEEFLRTYAGVVNSQLSQLPPHSIDQGAEDVVMAFSRSETEDRR
Q
;
B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   ALA n 
1 3   VAL n 
1 4   VAL n 
1 5   ASN n 
1 6   LEU n 
1 7   ILE n 
1 8   ASN n 
1 9   TYR n 
1 10  GLN n 
1 11  ASP n 
1 12  ASP n 
1 13  ALA n 
1 14  GLU n 
1 15  LEU n 
1 16  ALA n 
1 17  THR n 
1 18  ARG n 
1 19  ALA n 
1 20  ILE n 
1 21  PRO n 
1 22  GLU n 
1 23  LEU n 
1 24  THR n 
1 25  LYS n 
1 26  LEU n 
1 27  LEU n 
1 28  ASN n 
1 29  ASP n 
1 30  GLU n 
1 31  ASP n 
1 32  GLN n 
1 33  VAL n 
1 34  VAL n 
1 35  VAL n 
1 36  ASN n 
1 37  LYS n 
1 38  ALA n 
1 39  ALA n 
1 40  VAL n 
1 41  MET n 
1 42  VAL n 
1 43  HIS n 
1 44  GLN n 
1 45  LEU n 
1 46  SER n 
1 47  LYS n 
1 48  LYS n 
1 49  GLU n 
1 50  ALA n 
1 51  SER n 
1 52  ARG n 
1 53  HIS n 
1 54  ALA n 
1 55  ILE n 
1 56  MET n 
1 57  ARG n 
1 58  SER n 
1 59  PRO n 
1 60  GLN n 
1 61  MET n 
1 62  VAL n 
1 63  SER n 
1 64  ALA n 
1 65  ILE n 
1 66  VAL n 
1 67  ARG n 
1 68  THR n 
1 69  MET n 
1 70  GLN n 
1 71  ASN n 
1 72  THR n 
1 73  ASN n 
1 74  ASP n 
1 75  VAL n 
1 76  GLU n 
1 77  THR n 
1 78  ALA n 
1 79  ARG n 
1 80  CYS n 
1 81  THR n 
1 82  ALA n 
1 83  GLY n 
1 84  THR n 
1 85  LEU n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  SER n 
1 90  HIS n 
1 91  HIS n 
1 92  ARG n 
1 93  GLU n 
1 94  GLY n 
1 95  LEU n 
1 96  LEU n 
1 97  ALA n 
1 98  ILE n 
1 99  PHE n 
1 100 LYS n 
1 101 SER n 
1 102 GLY n 
1 103 GLY n 
1 104 ILE n 
1 105 PRO n 
1 106 ALA n 
1 107 LEU n 
1 108 VAL n 
1 109 LYS n 
1 110 MET n 
1 111 LEU n 
1 112 GLY n 
1 113 SER n 
1 114 PRO n 
1 115 VAL n 
1 116 ASP n 
1 117 SER n 
1 118 VAL n 
1 119 LEU n 
1 120 PHE n 
1 121 TYR n 
1 122 ALA n 
1 123 ILE n 
1 124 THR n 
1 125 THR n 
1 126 LEU n 
1 127 HIS n 
1 128 ASN n 
1 129 LEU n 
1 130 LEU n 
1 131 LEU n 
1 132 HIS n 
1 133 GLN n 
1 134 GLU n 
1 135 GLY n 
1 136 ALA n 
1 137 LYS n 
1 138 MET n 
1 139 ALA n 
1 140 VAL n 
1 141 ARG n 
1 142 LEU n 
1 143 ALA n 
1 144 GLY n 
1 145 GLY n 
1 146 LEU n 
1 147 GLN n 
1 148 LYS n 
1 149 MET n 
1 150 VAL n 
1 151 ALA n 
1 152 LEU n 
1 153 LEU n 
1 154 ASN n 
1 155 LYS n 
1 156 THR n 
1 157 ASN n 
1 158 VAL n 
1 159 LYS n 
1 160 PHE n 
1 161 LEU n 
1 162 ALA n 
1 163 ILE n 
1 164 THR n 
1 165 THR n 
1 166 ASP n 
1 167 CYS n 
1 168 LEU n 
1 169 GLN n 
1 170 ILE n 
1 171 LEU n 
1 172 ALA n 
1 173 TYR n 
1 174 GLY n 
1 175 ASN n 
1 176 GLN n 
1 177 GLU n 
1 178 SER n 
1 179 LYS n 
1 180 LEU n 
1 181 ILE n 
1 182 ILE n 
1 183 LEU n 
1 184 ALA n 
1 185 SER n 
1 186 GLY n 
1 187 GLY n 
1 188 PRO n 
1 189 GLN n 
1 190 ALA n 
1 191 LEU n 
1 192 VAL n 
1 193 ASN n 
1 194 ILE n 
1 195 MET n 
1 196 ARG n 
1 197 THR n 
1 198 TYR n 
1 199 THR n 
1 200 TYR n 
1 201 GLU n 
1 202 LYS n 
1 203 LEU n 
1 204 LEU n 
1 205 TRP n 
1 206 THR n 
1 207 THR n 
1 208 SER n 
1 209 ARG n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 VAL n 
1 214 LEU n 
1 215 SER n 
1 216 VAL n 
1 217 CYS n 
1 218 SER n 
1 219 SER n 
1 220 ASN n 
1 221 LYS n 
1 222 PRO n 
1 223 ALA n 
1 224 ILE n 
1 225 VAL n 
1 226 GLU n 
1 227 ALA n 
1 228 GLY n 
1 229 GLY n 
1 230 MET n 
1 231 GLN n 
1 232 ALA n 
1 233 LEU n 
1 234 GLY n 
1 235 LEU n 
1 236 HIS n 
1 237 LEU n 
1 238 THR n 
1 239 ASP n 
1 240 PRO n 
1 241 SER n 
1 242 GLN n 
1 243 ARG n 
1 244 LEU n 
1 245 VAL n 
1 246 GLN n 
1 247 ASN n 
1 248 CYS n 
1 249 LEU n 
1 250 TRP n 
1 251 THR n 
1 252 LEU n 
1 253 ARG n 
1 254 ASN n 
1 255 LEU n 
1 256 SER n 
1 257 ASP n 
1 258 ALA n 
1 259 ALA n 
1 260 THR n 
1 261 LYS n 
1 262 GLN n 
1 263 GLU n 
1 264 GLY n 
1 265 MET n 
1 266 GLU n 
1 267 GLY n 
1 268 LEU n 
1 269 LEU n 
1 270 GLY n 
1 271 THR n 
1 272 LEU n 
1 273 VAL n 
1 274 GLN n 
1 275 LEU n 
1 276 LEU n 
1 277 GLY n 
1 278 SER n 
1 279 ASP n 
1 280 ASP n 
1 281 ILE n 
1 282 ASN n 
1 283 VAL n 
1 284 VAL n 
1 285 THR n 
1 286 CYS n 
1 287 ALA n 
1 288 ALA n 
1 289 GLY n 
1 290 ILE n 
1 291 LEU n 
1 292 SER n 
1 293 ASN n 
1 294 LEU n 
1 295 THR n 
1 296 CYS n 
1 297 ASN n 
1 298 ASN n 
1 299 TYR n 
1 300 LYS n 
1 301 ASN n 
1 302 LYS n 
1 303 MET n 
1 304 MET n 
1 305 VAL n 
1 306 CYS n 
1 307 GLN n 
1 308 VAL n 
1 309 GLY n 
1 310 GLY n 
1 311 ILE n 
1 312 GLU n 
1 313 ALA n 
1 314 LEU n 
1 315 VAL n 
1 316 ARG n 
1 317 THR n 
1 318 VAL n 
1 319 LEU n 
1 320 ARG n 
1 321 ALA n 
1 322 GLY n 
1 323 ASP n 
1 324 ARG n 
1 325 GLU n 
1 326 ASP n 
1 327 ILE n 
1 328 THR n 
1 329 GLU n 
1 330 PRO n 
1 331 ALA n 
1 332 ILE n 
1 333 CYS n 
1 334 ALA n 
1 335 LEU n 
1 336 ARG n 
1 337 HIS n 
1 338 LEU n 
1 339 THR n 
1 340 SER n 
1 341 ARG n 
1 342 HIS n 
1 343 GLN n 
1 344 GLU n 
1 345 ALA n 
1 346 GLU n 
1 347 MET n 
1 348 ALA n 
1 349 GLN n 
1 350 ASN n 
1 351 ALA n 
1 352 VAL n 
1 353 ARG n 
1 354 LEU n 
1 355 HIS n 
1 356 TYR n 
1 357 GLY n 
1 358 LEU n 
1 359 PRO n 
1 360 VAL n 
1 361 VAL n 
1 362 VAL n 
1 363 LYS n 
1 364 LEU n 
1 365 LEU n 
1 366 HIS n 
1 367 PRO n 
1 368 PRO n 
1 369 SER n 
1 370 HIS n 
1 371 TRP n 
1 372 PRO n 
1 373 LEU n 
1 374 ILE n 
1 375 LYS n 
1 376 ALA n 
1 377 THR n 
1 378 VAL n 
1 379 GLY n 
1 380 LEU n 
1 381 ILE n 
1 382 ARG n 
1 383 ASN n 
1 384 LEU n 
1 385 ALA n 
1 386 LEU n 
1 387 CYS n 
1 388 PRO n 
1 389 ALA n 
1 390 ASN n 
1 391 HIS n 
1 392 ALA n 
1 393 PRO n 
1 394 LEU n 
1 395 ARG n 
1 396 GLU n 
1 397 GLN n 
1 398 GLY n 
1 399 ALA n 
1 400 ILE n 
1 401 PRO n 
1 402 ARG n 
1 403 LEU n 
1 404 VAL n 
1 405 GLN n 
1 406 LEU n 
1 407 LEU n 
1 408 VAL n 
1 409 ARG n 
1 410 ALA n 
1 411 HIS n 
1 412 GLN n 
1 413 ASP n 
1 414 THR n 
1 415 GLN n 
1 416 ARG n 
1 417 ARG n 
1 418 THR n 
1 419 SER n 
1 420 MET n 
1 421 GLY n 
1 422 GLY n 
1 423 THR n 
1 424 GLN n 
1 425 GLN n 
1 426 GLN n 
1 427 PHE n 
1 428 VAL n 
1 429 GLU n 
1 430 GLY n 
1 431 VAL n 
1 432 ARG n 
1 433 MET n 
1 434 GLU n 
1 435 GLU n 
1 436 ILE n 
1 437 VAL n 
1 438 GLU n 
1 439 GLY n 
1 440 CYS n 
1 441 THR n 
1 442 GLY n 
1 443 ALA n 
1 444 LEU n 
1 445 HIS n 
1 446 ILE n 
1 447 LEU n 
1 448 ALA n 
1 449 ARG n 
1 450 ASP n 
1 451 VAL n 
1 452 HIS n 
1 453 ASN n 
1 454 ARG n 
1 455 ILE n 
1 456 VAL n 
1 457 ILE n 
1 458 ARG n 
1 459 GLY n 
1 460 LEU n 
1 461 ASN n 
1 462 THR n 
1 463 ILE n 
1 464 PRO n 
1 465 LEU n 
1 466 PHE n 
1 467 VAL n 
1 468 GLN n 
1 469 LEU n 
1 470 LEU n 
1 471 TYR n 
1 472 SER n 
1 473 PRO n 
1 474 ILE n 
1 475 GLU n 
1 476 ASN n 
1 477 ILE n 
1 478 GLN n 
1 479 ARG n 
1 480 VAL n 
1 481 ALA n 
1 482 ALA n 
1 483 GLY n 
1 484 VAL n 
1 485 LEU n 
1 486 CYS n 
1 487 GLU n 
1 488 LEU n 
1 489 ALA n 
1 490 GLN n 
1 491 ASP n 
1 492 LYS n 
1 493 GLU n 
1 494 ALA n 
1 495 ALA n 
1 496 GLU n 
1 497 ALA n 
1 498 ILE n 
1 499 GLU n 
1 500 ALA n 
1 501 GLU n 
1 502 GLY n 
1 503 ALA n 
1 504 THR n 
1 505 ALA n 
1 506 PRO n 
1 507 LEU n 
1 508 THR n 
1 509 GLU n 
1 510 LEU n 
1 511 LEU n 
1 512 HIS n 
1 513 SER n 
1 514 ARG n 
1 515 ASN n 
1 516 GLU n 
1 517 GLY n 
1 518 VAL n 
1 519 ALA n 
1 520 THR n 
1 521 TYR n 
1 522 ALA n 
1 523 ALA n 
1 524 ALA n 
1 525 VAL n 
1 526 LEU n 
1 527 PHE n 
1 528 ARG n 
1 529 MET n 
1 530 SER n 
1 531 GLU n 
1 532 ASP n 
1 533 LYS n 
1 534 PRO n 
1 535 GLN n 
1 536 ASP n 
1 537 TYR n 
1 538 LYS n 
2 1   MET n 
2 2   ASN n 
2 3   ARG n 
2 4   GLU n 
2 5   GLY n 
2 6   ALA n 
2 7   PRO n 
2 8   GLY n 
2 9   LYS n 
2 10  SER n 
2 11  PRO n 
2 12  GLU n 
2 13  GLU n 
2 14  MET n 
2 15  TYR n 
2 16  ILE n 
2 17  GLN n 
2 18  GLN n 
2 19  LYS n 
2 20  VAL n 
2 21  ARG n 
2 22  VAL n 
2 23  LEU n 
2 24  LEU n 
2 25  MET n 
2 26  LEU n 
2 27  ARG n 
2 28  LYS n 
2 29  MET n 
2 30  GLY n 
2 31  SER n 
2 32  ASN n 
2 33  LEU n 
2 34  THR n 
2 35  ALA n 
2 36  SER n 
2 37  GLU n 
2 38  GLU n 
2 39  GLU n 
2 40  PHE n 
2 41  LEU n 
2 42  ARG n 
2 43  THR n 
2 44  TYR n 
2 45  ALA n 
2 46  GLY n 
2 47  VAL n 
2 48  VAL n 
2 49  ASN n 
2 50  SER n 
2 51  GLN n 
2 52  LEU n 
2 53  SER n 
2 54  GLN n 
2 55  LEU n 
2 56  PRO n 
2 57  PRO n 
2 58  HIS n 
2 59  SER n 
2 60  ILE n 
2 61  ASP n 
2 62  GLN n 
2 63  GLY n 
2 64  ALA n 
2 65  GLU n 
2 66  ASP n 
2 67  VAL n 
2 68  VAL n 
2 69  MET n 
2 70  ALA n 
2 71  PHE n 
2 72  SER n 
2 73  ARG n 
2 74  SER n 
2 75  GLU n 
2 76  THR n 
2 77  GLU n 
2 78  ASP n 
2 79  ARG n 
2 80  ARG n 
2 81  GLN 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 ? ? ? 'house mouse' Mus  ? ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 'Escherichia coli'      562    Escherichia 
? ? ?                  ? ? Topp3 ? ? ? ? ? ? ? Plasmid ? ? ? pGEX-4T ? ? 
2 1 sample ? ? ? human         Homo ? ? ? ? ? ? ? 'Homo sapiens' 9606  ? ? ? ? ? ? ? ? 'Escherichia coli BL21' 511693 Escherichia 
? ? 'Escherichia coli' ? ? BL21  ? ? ? ? ? ? ? Plasmid ? ? ? pGEX-4T ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   HIS 1   134 ?   ?   ?   A . n 
A 1 2   ALA 2   135 ?   ?   ?   A . n 
A 1 3   VAL 3   136 ?   ?   ?   A . n 
A 1 4   VAL 4   137 ?   ?   ?   A . n 
A 1 5   ASN 5   138 ?   ?   ?   A . n 
A 1 6   LEU 6   139 ?   ?   ?   A . n 
A 1 7   ILE 7   140 ?   ?   ?   A . n 
A 1 8   ASN 8   141 ?   ?   ?   A . n 
A 1 9   TYR 9   142 ?   ?   ?   A . n 
A 1 10  GLN 10  143 ?   ?   ?   A . n 
A 1 11  ASP 11  144 ?   ?   ?   A . n 
A 1 12  ASP 12  145 ?   ?   ?   A . n 
A 1 13  ALA 13  146 ?   ?   ?   A . n 
A 1 14  GLU 14  147 ?   ?   ?   A . n 
A 1 15  LEU 15  148 ?   ?   ?   A . n 
A 1 16  ALA 16  149 ?   ?   ?   A . n 
A 1 17  THR 17  150 ?   ?   ?   A . n 
A 1 18  ARG 18  151 151 ARG ARG A . n 
A 1 19  ALA 19  152 152 ALA ALA A . n 
A 1 20  ILE 20  153 153 ILE ILE A . n 
A 1 21  PRO 21  154 154 PRO PRO A . n 
A 1 22  GLU 22  155 155 GLU ALA A . n 
A 1 23  LEU 23  156 156 LEU LEU A . n 
A 1 24  THR 24  157 157 THR THR A . n 
A 1 25  LYS 25  158 158 LYS ALA A . n 
A 1 26  LEU 26  159 159 LEU LEU A . n 
A 1 27  LEU 27  160 160 LEU LEU A . n 
A 1 28  ASN 28  161 161 ASN ASN A . n 
A 1 29  ASP 29  162 162 ASP ASP A . n 
A 1 30  GLU 30  163 163 GLU GLU A . n 
A 1 31  ASP 31  164 164 ASP ASP A . n 
A 1 32  GLN 32  165 165 GLN GLN A . n 
A 1 33  VAL 33  166 166 VAL VAL A . n 
A 1 34  VAL 34  167 167 VAL VAL A . n 
A 1 35  VAL 35  168 168 VAL VAL A . n 
A 1 36  ASN 36  169 169 ASN ASN A . n 
A 1 37  LYS 37  170 170 LYS LYS A . n 
A 1 38  ALA 38  171 171 ALA ALA A . n 
A 1 39  ALA 39  172 172 ALA ALA A . n 
A 1 40  VAL 40  173 173 VAL VAL A . n 
A 1 41  MET 41  174 174 MET MET A . n 
A 1 42  VAL 42  175 175 VAL VAL A . n 
A 1 43  HIS 43  176 176 HIS HIS A . n 
A 1 44  GLN 44  177 177 GLN GLN A . n 
A 1 45  LEU 45  178 178 LEU LEU A . n 
A 1 46  SER 46  179 179 SER SER A . n 
A 1 47  LYS 47  180 180 LYS LYS A . n 
A 1 48  LYS 48  181 181 LYS ALA A . n 
A 1 49  GLU 49  182 182 GLU GLU A . n 
A 1 50  ALA 50  183 183 ALA ALA A . n 
A 1 51  SER 51  184 184 SER SER A . n 
A 1 52  ARG 52  185 185 ARG ARG A . n 
A 1 53  HIS 53  186 186 HIS HIS A . n 
A 1 54  ALA 54  187 187 ALA ALA A . n 
A 1 55  ILE 55  188 188 ILE ILE A . n 
A 1 56  MET 56  189 189 MET MET A . n 
A 1 57  ARG 57  190 190 ARG ARG A . n 
A 1 58  SER 58  191 191 SER SER A . n 
A 1 59  PRO 59  192 192 PRO PRO A . n 
A 1 60  GLN 60  193 193 GLN GLN A . n 
A 1 61  MET 61  194 194 MET MET A . n 
A 1 62  VAL 62  195 195 VAL VAL A . n 
A 1 63  SER 63  196 196 SER SER A . n 
A 1 64  ALA 64  197 197 ALA ALA A . n 
A 1 65  ILE 65  198 198 ILE ILE A . n 
A 1 66  VAL 66  199 199 VAL VAL A . n 
A 1 67  ARG 67  200 200 ARG ARG A . n 
A 1 68  THR 68  201 201 THR THR A . n 
A 1 69  MET 69  202 202 MET MET A . n 
A 1 70  GLN 70  203 203 GLN GLN A . n 
A 1 71  ASN 71  204 204 ASN ASN A . n 
A 1 72  THR 72  205 205 THR THR A . n 
A 1 73  ASN 73  206 206 ASN ASN A . n 
A 1 74  ASP 74  207 207 ASP ASP A . n 
A 1 75  VAL 75  208 208 VAL VAL A . n 
A 1 76  GLU 76  209 209 GLU GLU A . n 
A 1 77  THR 77  210 210 THR THR A . n 
A 1 78  ALA 78  211 211 ALA ALA A . n 
A 1 79  ARG 79  212 212 ARG ARG A . n 
A 1 80  CYS 80  213 213 CYS CYS A . n 
A 1 81  THR 81  214 214 THR THR A . n 
A 1 82  ALA 82  215 215 ALA ALA A . n 
A 1 83  GLY 83  216 216 GLY GLY A . n 
A 1 84  THR 84  217 217 THR THR A . n 
A 1 85  LEU 85  218 218 LEU LEU A . n 
A 1 86  HIS 86  219 219 HIS HIS A . n 
A 1 87  ASN 87  220 220 ASN ASN A . n 
A 1 88  LEU 88  221 221 LEU LEU A . n 
A 1 89  SER 89  222 222 SER SER A . n 
A 1 90  HIS 90  223 223 HIS HIS A . n 
A 1 91  HIS 91  224 224 HIS HIS A . n 
A 1 92  ARG 92  225 225 ARG ARG A . n 
A 1 93  GLU 93  226 226 GLU GLU A . n 
A 1 94  GLY 94  227 227 GLY GLY A . n 
A 1 95  LEU 95  228 228 LEU LEU A . n 
A 1 96  LEU 96  229 229 LEU LEU A . n 
A 1 97  ALA 97  230 230 ALA ALA A . n 
A 1 98  ILE 98  231 231 ILE ILE A . n 
A 1 99  PHE 99  232 232 PHE PHE A . n 
A 1 100 LYS 100 233 233 LYS LYS A . n 
A 1 101 SER 101 234 234 SER SER A . n 
A 1 102 GLY 102 235 235 GLY GLY A . n 
A 1 103 GLY 103 236 236 GLY GLY A . n 
A 1 104 ILE 104 237 237 ILE ILE A . n 
A 1 105 PRO 105 238 238 PRO PRO A . n 
A 1 106 ALA 106 239 239 ALA ALA A . n 
A 1 107 LEU 107 240 240 LEU LEU A . n 
A 1 108 VAL 108 241 241 VAL VAL A . n 
A 1 109 LYS 109 242 242 LYS LYS A . n 
A 1 110 MET 110 243 243 MET MET A . n 
A 1 111 LEU 111 244 244 LEU LEU A . n 
A 1 112 GLY 112 245 245 GLY GLY A . n 
A 1 113 SER 113 246 246 SER SER A . n 
A 1 114 PRO 114 247 247 PRO PRO A . n 
A 1 115 VAL 115 248 248 VAL VAL A . n 
A 1 116 ASP 116 249 249 ASP ASP A . n 
A 1 117 SER 117 250 250 SER SER A . n 
A 1 118 VAL 118 251 251 VAL VAL A . n 
A 1 119 LEU 119 252 252 LEU LEU A . n 
A 1 120 PHE 120 253 253 PHE PHE A . n 
A 1 121 TYR 121 254 254 TYR TYR A . n 
A 1 122 ALA 122 255 255 ALA ALA A . n 
A 1 123 ILE 123 256 256 ILE ILE A . n 
A 1 124 THR 124 257 257 THR THR A . n 
A 1 125 THR 125 258 258 THR THR A . n 
A 1 126 LEU 126 259 259 LEU LEU A . n 
A 1 127 HIS 127 260 260 HIS HIS A . n 
A 1 128 ASN 128 261 261 ASN ASN A . n 
A 1 129 LEU 129 262 262 LEU LEU A . n 
A 1 130 LEU 130 263 263 LEU LEU A . n 
A 1 131 LEU 131 264 264 LEU LEU A . n 
A 1 132 HIS 132 265 265 HIS HIS A . n 
A 1 133 GLN 133 266 266 GLN GLN A . n 
A 1 134 GLU 134 267 267 GLU GLU A . n 
A 1 135 GLY 135 268 268 GLY GLY A . n 
A 1 136 ALA 136 269 269 ALA ALA A . n 
A 1 137 LYS 137 270 270 LYS LYS A . n 
A 1 138 MET 138 271 271 MET MET A . n 
A 1 139 ALA 139 272 272 ALA ALA A . n 
A 1 140 VAL 140 273 273 VAL VAL A . n 
A 1 141 ARG 141 274 274 ARG ARG A . n 
A 1 142 LEU 142 275 275 LEU LEU A . n 
A 1 143 ALA 143 276 276 ALA ALA A . n 
A 1 144 GLY 144 277 277 GLY GLY A . n 
A 1 145 GLY 145 278 278 GLY GLY A . n 
A 1 146 LEU 146 279 279 LEU LEU A . n 
A 1 147 GLN 147 280 280 GLN GLN A . n 
A 1 148 LYS 148 281 281 LYS LYS A . n 
A 1 149 MET 149 282 282 MET MET A . n 
A 1 150 VAL 150 283 283 VAL VAL A . n 
A 1 151 ALA 151 284 284 ALA ALA A . n 
A 1 152 LEU 152 285 285 LEU LEU A . n 
A 1 153 LEU 153 286 286 LEU LEU A . n 
A 1 154 ASN 154 287 287 ASN ASN A . n 
A 1 155 LYS 155 288 288 LYS LYS A . n 
A 1 156 THR 156 289 289 THR THR A . n 
A 1 157 ASN 157 290 290 ASN ASN A . n 
A 1 158 VAL 158 291 291 VAL VAL A . n 
A 1 159 LYS 159 292 292 LYS LYS A . n 
A 1 160 PHE 160 293 293 PHE PHE A . n 
A 1 161 LEU 161 294 294 LEU LEU A . n 
A 1 162 ALA 162 295 295 ALA ALA A . n 
A 1 163 ILE 163 296 296 ILE ILE A . n 
A 1 164 THR 164 297 297 THR THR A . n 
A 1 165 THR 165 298 298 THR THR A . n 
A 1 166 ASP 166 299 299 ASP ASP A . n 
A 1 167 CYS 167 300 300 CYS CYS A . n 
A 1 168 LEU 168 301 301 LEU LEU A . n 
A 1 169 GLN 169 302 302 GLN GLN A . n 
A 1 170 ILE 170 303 303 ILE ILE A . n 
A 1 171 LEU 171 304 304 LEU LEU A . n 
A 1 172 ALA 172 305 305 ALA ALA A . n 
A 1 173 TYR 173 306 306 TYR TYR A . n 
A 1 174 GLY 174 307 307 GLY GLY A . n 
A 1 175 ASN 175 308 308 ASN ASN A . n 
A 1 176 GLN 176 309 309 GLN GLN A . n 
A 1 177 GLU 177 310 310 GLU GLU A . n 
A 1 178 SER 178 311 311 SER SER A . n 
A 1 179 LYS 179 312 312 LYS LYS A . n 
A 1 180 LEU 180 313 313 LEU LEU A . n 
A 1 181 ILE 181 314 314 ILE ILE A . n 
A 1 182 ILE 182 315 315 ILE ILE A . n 
A 1 183 LEU 183 316 316 LEU LEU A . n 
A 1 184 ALA 184 317 317 ALA ALA A . n 
A 1 185 SER 185 318 318 SER SER A . n 
A 1 186 GLY 186 319 319 GLY GLY A . n 
A 1 187 GLY 187 320 320 GLY GLY A . n 
A 1 188 PRO 188 321 321 PRO PRO A . n 
A 1 189 GLN 189 322 322 GLN GLN A . n 
A 1 190 ALA 190 323 323 ALA ALA A . n 
A 1 191 LEU 191 324 324 LEU LEU A . n 
A 1 192 VAL 192 325 325 VAL VAL A . n 
A 1 193 ASN 193 326 326 ASN ASN A . n 
A 1 194 ILE 194 327 327 ILE ILE A . n 
A 1 195 MET 195 328 328 MET MET A . n 
A 1 196 ARG 196 329 329 ARG ARG A . n 
A 1 197 THR 197 330 330 THR THR A . n 
A 1 198 TYR 198 331 331 TYR TYR A . n 
A 1 199 THR 199 332 332 THR THR A . n 
A 1 200 TYR 200 333 333 TYR TYR A . n 
A 1 201 GLU 201 334 334 GLU GLU A . n 
A 1 202 LYS 202 335 335 LYS LYS A . n 
A 1 203 LEU 203 336 336 LEU LEU A . n 
A 1 204 LEU 204 337 337 LEU LEU A . n 
A 1 205 TRP 205 338 338 TRP TRP A . n 
A 1 206 THR 206 339 339 THR THR A . n 
A 1 207 THR 207 340 340 THR THR A . n 
A 1 208 SER 208 341 341 SER SER A . n 
A 1 209 ARG 209 342 342 ARG ARG A . n 
A 1 210 VAL 210 343 343 VAL VAL A . n 
A 1 211 LEU 211 344 344 LEU LEU A . n 
A 1 212 LYS 212 345 345 LYS LYS A . n 
A 1 213 VAL 213 346 346 VAL VAL A . n 
A 1 214 LEU 214 347 347 LEU LEU A . n 
A 1 215 SER 215 348 348 SER SER A . n 
A 1 216 VAL 216 349 349 VAL VAL A . n 
A 1 217 CYS 217 350 350 CYS CYS A . n 
A 1 218 SER 218 351 351 SER SER A . n 
A 1 219 SER 219 352 352 SER SER A . n 
A 1 220 ASN 220 353 353 ASN ASN A . n 
A 1 221 LYS 221 354 354 LYS LYS A . n 
A 1 222 PRO 222 355 355 PRO PRO A . n 
A 1 223 ALA 223 356 356 ALA ALA A . n 
A 1 224 ILE 224 357 357 ILE ILE A . n 
A 1 225 VAL 225 358 358 VAL VAL A . n 
A 1 226 GLU 226 359 359 GLU GLU A . n 
A 1 227 ALA 227 360 360 ALA ALA A . n 
A 1 228 GLY 228 361 361 GLY GLY A . n 
A 1 229 GLY 229 362 362 GLY GLY A . n 
A 1 230 MET 230 363 363 MET MET A . n 
A 1 231 GLN 231 364 364 GLN GLN A . n 
A 1 232 ALA 232 365 365 ALA ALA A . n 
A 1 233 LEU 233 366 366 LEU LEU A . n 
A 1 234 GLY 234 367 367 GLY GLY A . n 
A 1 235 LEU 235 368 368 LEU LEU A . n 
A 1 236 HIS 236 369 369 HIS HIS A . n 
A 1 237 LEU 237 370 370 LEU LEU A . n 
A 1 238 THR 238 371 371 THR THR A . n 
A 1 239 ASP 239 372 372 ASP ASP A . n 
A 1 240 PRO 240 373 373 PRO PRO A . n 
A 1 241 SER 241 374 374 SER SER A . n 
A 1 242 GLN 242 375 375 GLN GLN A . n 
A 1 243 ARG 243 376 376 ARG ARG A . n 
A 1 244 LEU 244 377 377 LEU LEU A . n 
A 1 245 VAL 245 378 378 VAL VAL A . n 
A 1 246 GLN 246 379 379 GLN GLN A . n 
A 1 247 ASN 247 380 380 ASN ASN A . n 
A 1 248 CYS 248 381 381 CYS CYS A . n 
A 1 249 LEU 249 382 382 LEU LEU A . n 
A 1 250 TRP 250 383 383 TRP TRP A . n 
A 1 251 THR 251 384 384 THR THR A . n 
A 1 252 LEU 252 385 385 LEU LEU A . n 
A 1 253 ARG 253 386 386 ARG ARG A . n 
A 1 254 ASN 254 387 387 ASN ASN A . n 
A 1 255 LEU 255 388 388 LEU LEU A . n 
A 1 256 SER 256 389 389 SER SER A . n 
A 1 257 ASP 257 390 390 ASP ASP A . n 
A 1 258 ALA 258 391 391 ALA ALA A . n 
A 1 259 ALA 259 392 392 ALA ALA A . n 
A 1 260 THR 260 393 393 THR THR A . n 
A 1 261 LYS 261 394 394 LYS LYS A . n 
A 1 262 GLN 262 395 395 GLN GLN A . n 
A 1 263 GLU 263 396 396 GLU GLU A . n 
A 1 264 GLY 264 397 397 GLY GLY A . n 
A 1 265 MET 265 398 398 MET MET A . n 
A 1 266 GLU 266 399 399 GLU GLU A . n 
A 1 267 GLY 267 400 400 GLY GLY A . n 
A 1 268 LEU 268 401 401 LEU LEU A . n 
A 1 269 LEU 269 402 402 LEU LEU A . n 
A 1 270 GLY 270 403 403 GLY GLY A . n 
A 1 271 THR 271 404 404 THR THR A . n 
A 1 272 LEU 272 405 405 LEU LEU A . n 
A 1 273 VAL 273 406 406 VAL VAL A . n 
A 1 274 GLN 274 407 407 GLN GLN A . n 
A 1 275 LEU 275 408 408 LEU LEU A . n 
A 1 276 LEU 276 409 409 LEU LEU A . n 
A 1 277 GLY 277 410 410 GLY GLY A . n 
A 1 278 SER 278 411 411 SER SER A . n 
A 1 279 ASP 279 412 412 ASP ASP A . n 
A 1 280 ASP 280 413 413 ASP ASP A . n 
A 1 281 ILE 281 414 414 ILE ILE A . n 
A 1 282 ASN 282 415 415 ASN ASN A . n 
A 1 283 VAL 283 416 416 VAL VAL A . n 
A 1 284 VAL 284 417 417 VAL VAL A . n 
A 1 285 THR 285 418 418 THR THR A . n 
A 1 286 CYS 286 419 419 CYS CYS A . n 
A 1 287 ALA 287 420 420 ALA ALA A . n 
A 1 288 ALA 288 421 421 ALA ALA A . n 
A 1 289 GLY 289 422 422 GLY GLY A . n 
A 1 290 ILE 290 423 423 ILE ILE A . n 
A 1 291 LEU 291 424 424 LEU LEU A . n 
A 1 292 SER 292 425 425 SER SER A . n 
A 1 293 ASN 293 426 426 ASN ASN A . n 
A 1 294 LEU 294 427 427 LEU LEU A . n 
A 1 295 THR 295 428 428 THR THR A . n 
A 1 296 CYS 296 429 429 CYS CYS A . n 
A 1 297 ASN 297 430 430 ASN ASN A . n 
A 1 298 ASN 298 431 431 ASN ASN A . n 
A 1 299 TYR 299 432 432 TYR TYR A . n 
A 1 300 LYS 300 433 433 LYS LYS A . n 
A 1 301 ASN 301 434 434 ASN ASN A . n 
A 1 302 LYS 302 435 435 LYS LYS A . n 
A 1 303 MET 303 436 436 MET MET A . n 
A 1 304 MET 304 437 437 MET MET A . n 
A 1 305 VAL 305 438 438 VAL VAL A . n 
A 1 306 CYS 306 439 439 CYS CYS A . n 
A 1 307 GLN 307 440 440 GLN GLN A . n 
A 1 308 VAL 308 441 441 VAL VAL A . n 
A 1 309 GLY 309 442 442 GLY GLY A . n 
A 1 310 GLY 310 443 443 GLY GLY A . n 
A 1 311 ILE 311 444 444 ILE ILE A . n 
A 1 312 GLU 312 445 445 GLU GLU A . n 
A 1 313 ALA 313 446 446 ALA ALA A . n 
A 1 314 LEU 314 447 447 LEU LEU A . n 
A 1 315 VAL 315 448 448 VAL VAL A . n 
A 1 316 ARG 316 449 449 ARG ARG A . n 
A 1 317 THR 317 450 450 THR THR A . n 
A 1 318 VAL 318 451 451 VAL VAL A . n 
A 1 319 LEU 319 452 452 LEU LEU A . n 
A 1 320 ARG 320 453 453 ARG ARG A . n 
A 1 321 ALA 321 454 454 ALA ALA A . n 
A 1 322 GLY 322 455 455 GLY GLY A . n 
A 1 323 ASP 323 456 456 ASP ASP A . n 
A 1 324 ARG 324 457 457 ARG ARG A . n 
A 1 325 GLU 325 458 458 GLU GLU A . n 
A 1 326 ASP 326 459 459 ASP ASP A . n 
A 1 327 ILE 327 460 460 ILE ILE A . n 
A 1 328 THR 328 461 461 THR THR A . n 
A 1 329 GLU 329 462 462 GLU GLU A . n 
A 1 330 PRO 330 463 463 PRO PRO A . n 
A 1 331 ALA 331 464 464 ALA ALA A . n 
A 1 332 ILE 332 465 465 ILE ILE A . n 
A 1 333 CYS 333 466 466 CYS CYS A . n 
A 1 334 ALA 334 467 467 ALA ALA A . n 
A 1 335 LEU 335 468 468 LEU LEU A . n 
A 1 336 ARG 336 469 469 ARG ARG A . n 
A 1 337 HIS 337 470 470 HIS HIS A . n 
A 1 338 LEU 338 471 471 LEU LEU A . n 
A 1 339 THR 339 472 472 THR THR A . n 
A 1 340 SER 340 473 473 SER SER A . n 
A 1 341 ARG 341 474 474 ARG ARG A . n 
A 1 342 HIS 342 475 475 HIS HIS A . n 
A 1 343 GLN 343 476 476 GLN GLN A . n 
A 1 344 GLU 344 477 477 GLU GLU A . n 
A 1 345 ALA 345 478 478 ALA ALA A . n 
A 1 346 GLU 346 479 479 GLU GLU A . n 
A 1 347 MET 347 480 480 MET MET A . n 
A 1 348 ALA 348 481 481 ALA ALA A . n 
A 1 349 GLN 349 482 482 GLN GLN A . n 
A 1 350 ASN 350 483 483 ASN ASN A . n 
A 1 351 ALA 351 484 484 ALA ALA A . n 
A 1 352 VAL 352 485 485 VAL VAL A . n 
A 1 353 ARG 353 486 486 ARG ARG A . n 
A 1 354 LEU 354 487 487 LEU LEU A . n 
A 1 355 HIS 355 488 488 HIS HIS A . n 
A 1 356 TYR 356 489 489 TYR TYR A . n 
A 1 357 GLY 357 490 490 GLY GLY A . n 
A 1 358 LEU 358 491 491 LEU LEU A . n 
A 1 359 PRO 359 492 492 PRO PRO A . n 
A 1 360 VAL 360 493 493 VAL VAL A . n 
A 1 361 VAL 361 494 494 VAL VAL A . n 
A 1 362 VAL 362 495 495 VAL VAL A . n 
A 1 363 LYS 363 496 496 LYS LYS A . n 
A 1 364 LEU 364 497 497 LEU LEU A . n 
A 1 365 LEU 365 498 498 LEU LEU A . n 
A 1 366 HIS 366 499 499 HIS HIS A . n 
A 1 367 PRO 367 500 500 PRO PRO A . n 
A 1 368 PRO 368 501 501 PRO PRO A . n 
A 1 369 SER 369 502 502 SER SER A . n 
A 1 370 HIS 370 503 503 HIS HIS A . n 
A 1 371 TRP 371 504 504 TRP TRP A . n 
A 1 372 PRO 372 505 505 PRO PRO A . n 
A 1 373 LEU 373 506 506 LEU LEU A . n 
A 1 374 ILE 374 507 507 ILE ILE A . n 
A 1 375 LYS 375 508 508 LYS LYS A . n 
A 1 376 ALA 376 509 509 ALA ALA A . n 
A 1 377 THR 377 510 510 THR THR A . n 
A 1 378 VAL 378 511 511 VAL VAL A . n 
A 1 379 GLY 379 512 512 GLY GLY A . n 
A 1 380 LEU 380 513 513 LEU LEU A . n 
A 1 381 ILE 381 514 514 ILE ILE A . n 
A 1 382 ARG 382 515 515 ARG ARG A . n 
A 1 383 ASN 383 516 516 ASN ASN A . n 
A 1 384 LEU 384 517 517 LEU LEU A . n 
A 1 385 ALA 385 518 518 ALA ALA A . n 
A 1 386 LEU 386 519 519 LEU LEU A . n 
A 1 387 CYS 387 520 520 CYS CYS A . n 
A 1 388 PRO 388 521 521 PRO PRO A . n 
A 1 389 ALA 389 522 522 ALA ALA A . n 
A 1 390 ASN 390 523 523 ASN ASN A . n 
A 1 391 HIS 391 524 524 HIS HIS A . n 
A 1 392 ALA 392 525 525 ALA ALA A . n 
A 1 393 PRO 393 526 526 PRO PRO A . n 
A 1 394 LEU 394 527 527 LEU LEU A . n 
A 1 395 ARG 395 528 528 ARG ARG A . n 
A 1 396 GLU 396 529 529 GLU GLU A . n 
A 1 397 GLN 397 530 530 GLN GLN A . n 
A 1 398 GLY 398 531 531 GLY GLY A . n 
A 1 399 ALA 399 532 532 ALA ALA A . n 
A 1 400 ILE 400 533 533 ILE ILE A . n 
A 1 401 PRO 401 534 534 PRO PRO A . n 
A 1 402 ARG 402 535 535 ARG ARG A . n 
A 1 403 LEU 403 536 536 LEU LEU A . n 
A 1 404 VAL 404 537 537 VAL VAL A . n 
A 1 405 GLN 405 538 538 GLN GLN A . n 
A 1 406 LEU 406 539 539 LEU LEU A . n 
A 1 407 LEU 407 540 540 LEU LEU A . n 
A 1 408 VAL 408 541 541 VAL VAL A . n 
A 1 409 ARG 409 542 542 ARG ARG A . n 
A 1 410 ALA 410 543 543 ALA ALA A . n 
A 1 411 HIS 411 544 544 HIS HIS A . n 
A 1 412 GLN 412 545 545 GLN GLN A . n 
A 1 413 ASP 413 546 546 ASP ASP A . n 
A 1 414 THR 414 547 547 THR THR A . n 
A 1 415 GLN 415 548 548 GLN GLN A . n 
A 1 416 ARG 416 549 549 ARG ARG A . n 
A 1 417 ARG 417 550 ?   ?   ?   A . n 
A 1 418 THR 418 551 ?   ?   ?   A . n 
A 1 419 SER 419 552 ?   ?   ?   A . n 
A 1 420 MET 420 553 ?   ?   ?   A . n 
A 1 421 GLY 421 554 ?   ?   ?   A . n 
A 1 422 GLY 422 555 ?   ?   ?   A . n 
A 1 423 THR 423 556 ?   ?   ?   A . n 
A 1 424 GLN 424 557 ?   ?   ?   A . n 
A 1 425 GLN 425 558 ?   ?   ?   A . n 
A 1 426 GLN 426 559 559 GLN GLN A . n 
A 1 427 PHE 427 560 560 PHE PHE A . n 
A 1 428 VAL 428 561 561 VAL VAL A . n 
A 1 429 GLU 429 562 562 GLU GLU A . n 
A 1 430 GLY 430 563 563 GLY GLY A . n 
A 1 431 VAL 431 564 564 VAL VAL A . n 
A 1 432 ARG 432 565 565 ARG ARG A . n 
A 1 433 MET 433 566 566 MET MET A . n 
A 1 434 GLU 434 567 567 GLU GLU A . n 
A 1 435 GLU 435 568 568 GLU GLU A . n 
A 1 436 ILE 436 569 569 ILE ILE A . n 
A 1 437 VAL 437 570 570 VAL VAL A . n 
A 1 438 GLU 438 571 571 GLU GLU A . n 
A 1 439 GLY 439 572 572 GLY GLY A . n 
A 1 440 CYS 440 573 573 CYS CYS A . n 
A 1 441 THR 441 574 574 THR THR A . n 
A 1 442 GLY 442 575 575 GLY GLY A . n 
A 1 443 ALA 443 576 576 ALA ALA A . n 
A 1 444 LEU 444 577 577 LEU LEU A . n 
A 1 445 HIS 445 578 578 HIS HIS A . n 
A 1 446 ILE 446 579 579 ILE ILE A . n 
A 1 447 LEU 447 580 580 LEU LEU A . n 
A 1 448 ALA 448 581 581 ALA ALA A . n 
A 1 449 ARG 449 582 582 ARG ARG A . n 
A 1 450 ASP 450 583 583 ASP ASP A . n 
A 1 451 VAL 451 584 584 VAL VAL A . n 
A 1 452 HIS 452 585 585 HIS HIS A . n 
A 1 453 ASN 453 586 586 ASN ASN A . n 
A 1 454 ARG 454 587 587 ARG ARG A . n 
A 1 455 ILE 455 588 588 ILE ILE A . n 
A 1 456 VAL 456 589 589 VAL VAL A . n 
A 1 457 ILE 457 590 590 ILE ILE A . n 
A 1 458 ARG 458 591 591 ARG ARG A . n 
A 1 459 GLY 459 592 592 GLY GLY A . n 
A 1 460 LEU 460 593 593 LEU LEU A . n 
A 1 461 ASN 461 594 594 ASN ASN A . n 
A 1 462 THR 462 595 595 THR THR A . n 
A 1 463 ILE 463 596 596 ILE ILE A . n 
A 1 464 PRO 464 597 597 PRO PRO A . n 
A 1 465 LEU 465 598 598 LEU LEU A . n 
A 1 466 PHE 466 599 599 PHE PHE A . n 
A 1 467 VAL 467 600 600 VAL VAL A . n 
A 1 468 GLN 468 601 601 GLN GLN A . n 
A 1 469 LEU 469 602 602 LEU LEU A . n 
A 1 470 LEU 470 603 603 LEU LEU A . n 
A 1 471 TYR 471 604 604 TYR TYR A . n 
A 1 472 SER 472 605 605 SER SER A . n 
A 1 473 PRO 473 606 606 PRO PRO A . n 
A 1 474 ILE 474 607 607 ILE ILE A . n 
A 1 475 GLU 475 608 608 GLU GLU A . n 
A 1 476 ASN 476 609 609 ASN ASN A . n 
A 1 477 ILE 477 610 610 ILE ILE A . n 
A 1 478 GLN 478 611 611 GLN GLN A . n 
A 1 479 ARG 479 612 612 ARG ARG A . n 
A 1 480 VAL 480 613 613 VAL VAL A . n 
A 1 481 ALA 481 614 614 ALA ALA A . n 
A 1 482 ALA 482 615 615 ALA ALA A . n 
A 1 483 GLY 483 616 616 GLY GLY A . n 
A 1 484 VAL 484 617 617 VAL VAL A . n 
A 1 485 LEU 485 618 618 LEU LEU A . n 
A 1 486 CYS 486 619 619 CYS CYS A . n 
A 1 487 GLU 487 620 620 GLU GLU A . n 
A 1 488 LEU 488 621 621 LEU LEU A . n 
A 1 489 ALA 489 622 622 ALA ALA A . n 
A 1 490 GLN 490 623 623 GLN GLN A . n 
A 1 491 ASP 491 624 624 ASP ASP A . n 
A 1 492 LYS 492 625 625 LYS LYS A . n 
A 1 493 GLU 493 626 626 GLU GLU A . n 
A 1 494 ALA 494 627 627 ALA ALA A . n 
A 1 495 ALA 495 628 628 ALA ALA A . n 
A 1 496 GLU 496 629 629 GLU GLU A . n 
A 1 497 ALA 497 630 630 ALA ALA A . n 
A 1 498 ILE 498 631 631 ILE ILE A . n 
A 1 499 GLU 499 632 632 GLU GLU A . n 
A 1 500 ALA 500 633 633 ALA ALA A . n 
A 1 501 GLU 501 634 634 GLU GLU A . n 
A 1 502 GLY 502 635 635 GLY GLY A . n 
A 1 503 ALA 503 636 636 ALA ALA A . n 
A 1 504 THR 504 637 637 THR THR A . n 
A 1 505 ALA 505 638 638 ALA ALA A . n 
A 1 506 PRO 506 639 639 PRO PRO A . n 
A 1 507 LEU 507 640 640 LEU LEU A . n 
A 1 508 THR 508 641 641 THR THR A . n 
A 1 509 GLU 509 642 642 GLU GLU A . n 
A 1 510 LEU 510 643 643 LEU LEU A . n 
A 1 511 LEU 511 644 644 LEU LEU A . n 
A 1 512 HIS 512 645 645 HIS HIS A . n 
A 1 513 SER 513 646 646 SER SER A . n 
A 1 514 ARG 514 647 647 ARG ARG A . n 
A 1 515 ASN 515 648 648 ASN ASN A . n 
A 1 516 GLU 516 649 649 GLU GLU A . n 
A 1 517 GLY 517 650 650 GLY GLY A . n 
A 1 518 VAL 518 651 651 VAL VAL A . n 
A 1 519 ALA 519 652 652 ALA ALA A . n 
A 1 520 THR 520 653 653 THR THR A . n 
A 1 521 TYR 521 654 654 TYR TYR A . n 
A 1 522 ALA 522 655 655 ALA ALA A . n 
A 1 523 ALA 523 656 656 ALA ALA A . n 
A 1 524 ALA 524 657 657 ALA ALA A . n 
A 1 525 VAL 525 658 658 VAL VAL A . n 
A 1 526 LEU 526 659 659 LEU LEU A . n 
A 1 527 PHE 527 660 660 PHE PHE A . n 
A 1 528 ARG 528 661 661 ARG ARG A . n 
A 1 529 MET 529 662 662 MET MET A . n 
A 1 530 SER 530 663 663 SER SER A . n 
A 1 531 GLU 531 664 664 GLU GLU A . n 
A 1 532 ASP 532 665 665 ASP ASP A . n 
A 1 533 LYS 533 666 666 LYS ALA A . n 
A 1 534 PRO 534 667 667 PRO PRO A . n 
A 1 535 GLN 535 668 668 GLN GLN A . n 
A 1 536 ASP 536 669 669 ASP ASP A . n 
A 1 537 TYR 537 670 670 TYR TYR A . n 
A 1 538 LYS 538 671 671 LYS LYS A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   ASN 2   2   ?   ?   ?   B . n 
B 2 3   ARG 3   3   ?   ?   ?   B . n 
B 2 4   GLU 4   4   ?   ?   ?   B . n 
B 2 5   GLY 5   5   ?   ?   ?   B . n 
B 2 6   ALA 6   6   ?   ?   ?   B . n 
B 2 7   PRO 7   7   ?   ?   ?   B . n 
B 2 8   GLY 8   8   ?   ?   ?   B . n 
B 2 9   LYS 9   9   9   LYS LYS B . n 
B 2 10  SER 10  10  10  SER SER B . n 
B 2 11  PRO 11  11  11  PRO PRO B . n 
B 2 12  GLU 12  12  12  GLU GLU B . n 
B 2 13  GLU 13  13  13  GLU GLU B . n 
B 2 14  MET 14  14  14  MET MET B . n 
B 2 15  TYR 15  15  15  TYR TYR B . n 
B 2 16  ILE 16  16  16  ILE ILE B . n 
B 2 17  GLN 17  17  17  GLN GLN B . n 
B 2 18  GLN 18  18  18  GLN GLN B . n 
B 2 19  LYS 19  19  19  LYS LYS B . n 
B 2 20  VAL 20  20  20  VAL VAL B . n 
B 2 21  ARG 21  21  21  ARG ARG B . n 
B 2 22  VAL 22  22  22  VAL VAL B . n 
B 2 23  LEU 23  23  23  LEU LEU B . n 
B 2 24  LEU 24  24  24  LEU LEU B . n 
B 2 25  MET 25  25  25  MET MET B . n 
B 2 26  LEU 26  26  26  LEU LEU B . n 
B 2 27  ARG 27  27  27  ARG ARG B . n 
B 2 28  LYS 28  28  28  LYS LYS B . n 
B 2 29  MET 29  29  29  MET MET B . n 
B 2 30  GLY 30  30  30  GLY GLY B . n 
B 2 31  SER 31  31  31  SER SER B . n 
B 2 32  ASN 32  32  32  ASN ASN B . n 
B 2 33  LEU 33  33  33  LEU LEU B . n 
B 2 34  THR 34  34  34  THR THR B . n 
B 2 35  ALA 35  35  35  ALA ALA B . n 
B 2 36  SER 36  36  36  SER SER B . n 
B 2 37  GLU 37  37  37  GLU GLU B . n 
B 2 38  GLU 38  38  38  GLU GLU B . n 
B 2 39  GLU 39  39  39  GLU GLU B . n 
B 2 40  PHE 40  40  40  PHE PHE B . n 
B 2 41  LEU 41  41  41  LEU LEU B . n 
B 2 42  ARG 42  42  42  ARG ARG B . n 
B 2 43  THR 43  43  43  THR THR B . n 
B 2 44  TYR 44  44  44  TYR TYR B . n 
B 2 45  ALA 45  45  45  ALA ALA B . n 
B 2 46  GLY 46  46  46  GLY GLY B . n 
B 2 47  VAL 47  47  47  VAL VAL B . n 
B 2 48  VAL 48  48  48  VAL VAL B . n 
B 2 49  ASN 49  49  49  ASN ASN B . n 
B 2 50  SER 50  50  50  SER SER B . n 
B 2 51  GLN 51  51  51  GLN GLN B . n 
B 2 52  LEU 52  52  52  LEU ALA B . n 
B 2 53  SER 53  53  53  SER SER B . n 
B 2 54  GLN 54  54  54  GLN ALA B . n 
B 2 55  LEU 55  55  ?   ?   ?   B . n 
B 2 56  PRO 56  56  ?   ?   ?   B . n 
B 2 57  PRO 57  57  ?   ?   ?   B . n 
B 2 58  HIS 58  58  ?   ?   ?   B . n 
B 2 59  SER 59  59  ?   ?   ?   B . n 
B 2 60  ILE 60  60  60  ILE ALA B . n 
B 2 61  ASP 61  61  61  ASP ASP B . n 
B 2 62  GLN 62  62  62  GLN ALA B . n 
B 2 63  GLY 63  63  63  GLY GLY B . n 
B 2 64  ALA 64  64  64  ALA ALA B . n 
B 2 65  GLU 65  65  65  GLU GLU B . n 
B 2 66  ASP 66  66  66  ASP ASP B . n 
B 2 67  VAL 67  67  67  VAL VAL B . n 
B 2 68  VAL 68  68  68  VAL VAL B . n 
B 2 69  MET 69  69  69  MET MET B . n 
B 2 70  ALA 70  70  70  ALA ALA B . n 
B 2 71  PHE 71  71  71  PHE PHE B . n 
B 2 72  SER 72  72  72  SER SER B . n 
B 2 73  ARG 73  73  73  ARG ARG B . n 
B 2 74  SER 74  74  74  SER SER B . n 
B 2 75  GLU 75  75  75  GLU GLU B . n 
B 2 76  THR 76  76  76  THR THR B . n 
B 2 77  GLU 77  77  77  GLU ALA B . n 
B 2 78  ASP 78  78  78  ASP ASP B . n 
B 2 79  ARG 79  79  ?   ?   ?   B . n 
B 2 80  ARG 80  80  ?   ?   ?   B . n 
B 2 81  GLN 81  81  ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 HOH 1   672 1   HOH WAT A . 
C 3 HOH 2   673 2   HOH WAT A . 
C 3 HOH 3   674 3   HOH WAT A . 
C 3 HOH 4   675 4   HOH WAT A . 
C 3 HOH 5   676 5   HOH WAT A . 
C 3 HOH 6   677 6   HOH WAT A . 
C 3 HOH 7   678 7   HOH WAT A . 
C 3 HOH 8   679 8   HOH WAT A . 
C 3 HOH 9   680 9   HOH WAT A . 
C 3 HOH 10  681 10  HOH WAT A . 
C 3 HOH 11  682 11  HOH WAT A . 
C 3 HOH 12  683 12  HOH WAT A . 
C 3 HOH 13  684 13  HOH WAT A . 
C 3 HOH 14  685 14  HOH WAT A . 
C 3 HOH 15  686 15  HOH WAT A . 
C 3 HOH 16  687 17  HOH WAT A . 
C 3 HOH 17  688 18  HOH WAT A . 
C 3 HOH 18  689 19  HOH WAT A . 
C 3 HOH 19  690 20  HOH WAT A . 
C 3 HOH 20  691 21  HOH WAT A . 
C 3 HOH 21  692 22  HOH WAT A . 
C 3 HOH 22  693 23  HOH WAT A . 
C 3 HOH 23  694 25  HOH WAT A . 
C 3 HOH 24  695 26  HOH WAT A . 
C 3 HOH 25  696 27  HOH WAT A . 
C 3 HOH 26  697 28  HOH WAT A . 
C 3 HOH 27  698 29  HOH WAT A . 
C 3 HOH 28  699 31  HOH WAT A . 
C 3 HOH 29  700 32  HOH WAT A . 
C 3 HOH 30  701 33  HOH WAT A . 
C 3 HOH 31  702 34  HOH WAT A . 
C 3 HOH 32  703 35  HOH WAT A . 
C 3 HOH 33  704 37  HOH WAT A . 
C 3 HOH 34  705 38  HOH WAT A . 
C 3 HOH 35  706 39  HOH WAT A . 
C 3 HOH 36  707 40  HOH WAT A . 
C 3 HOH 37  708 41  HOH WAT A . 
C 3 HOH 38  709 42  HOH WAT A . 
C 3 HOH 39  710 43  HOH WAT A . 
C 3 HOH 40  711 44  HOH WAT A . 
C 3 HOH 41  712 45  HOH WAT A . 
C 3 HOH 42  713 46  HOH WAT A . 
C 3 HOH 43  714 47  HOH WAT A . 
C 3 HOH 44  715 48  HOH WAT A . 
C 3 HOH 45  716 49  HOH WAT A . 
C 3 HOH 46  717 50  HOH WAT A . 
C 3 HOH 47  718 51  HOH WAT A . 
C 3 HOH 48  719 52  HOH WAT A . 
C 3 HOH 49  720 54  HOH WAT A . 
C 3 HOH 50  721 55  HOH WAT A . 
C 3 HOH 51  722 57  HOH WAT A . 
C 3 HOH 52  723 58  HOH WAT A . 
C 3 HOH 53  724 59  HOH WAT A . 
C 3 HOH 54  725 60  HOH WAT A . 
C 3 HOH 55  726 61  HOH WAT A . 
C 3 HOH 56  727 62  HOH WAT A . 
C 3 HOH 57  728 64  HOH WAT A . 
C 3 HOH 58  729 65  HOH WAT A . 
C 3 HOH 59  730 66  HOH WAT A . 
C 3 HOH 60  731 67  HOH WAT A . 
C 3 HOH 61  732 69  HOH WAT A . 
C 3 HOH 62  733 70  HOH WAT A . 
C 3 HOH 63  734 71  HOH WAT A . 
C 3 HOH 64  735 73  HOH WAT A . 
C 3 HOH 65  736 74  HOH WAT A . 
C 3 HOH 66  737 75  HOH WAT A . 
C 3 HOH 67  738 76  HOH WAT A . 
C 3 HOH 68  739 77  HOH WAT A . 
C 3 HOH 69  740 78  HOH WAT A . 
C 3 HOH 70  741 79  HOH WAT A . 
C 3 HOH 71  742 80  HOH WAT A . 
C 3 HOH 72  743 81  HOH WAT A . 
C 3 HOH 73  744 82  HOH WAT A . 
C 3 HOH 74  745 83  HOH WAT A . 
C 3 HOH 75  746 84  HOH WAT A . 
C 3 HOH 76  747 85  HOH WAT A . 
C 3 HOH 77  748 86  HOH WAT A . 
C 3 HOH 78  749 87  HOH WAT A . 
C 3 HOH 79  750 88  HOH WAT A . 
C 3 HOH 80  751 89  HOH WAT A . 
C 3 HOH 81  752 90  HOH WAT A . 
C 3 HOH 82  753 91  HOH WAT A . 
C 3 HOH 83  754 92  HOH WAT A . 
C 3 HOH 84  755 93  HOH WAT A . 
C 3 HOH 85  756 94  HOH WAT A . 
C 3 HOH 86  757 95  HOH WAT A . 
C 3 HOH 87  758 96  HOH WAT A . 
C 3 HOH 88  759 97  HOH WAT A . 
C 3 HOH 89  760 98  HOH WAT A . 
C 3 HOH 90  761 99  HOH WAT A . 
C 3 HOH 91  762 100 HOH WAT A . 
C 3 HOH 92  763 101 HOH WAT A . 
C 3 HOH 93  764 102 HOH WAT A . 
C 3 HOH 94  765 103 HOH WAT A . 
C 3 HOH 95  766 104 HOH WAT A . 
C 3 HOH 96  767 105 HOH WAT A . 
C 3 HOH 97  768 107 HOH WAT A . 
C 3 HOH 98  769 108 HOH WAT A . 
C 3 HOH 99  770 109 HOH WAT A . 
C 3 HOH 100 771 110 HOH WAT A . 
C 3 HOH 101 772 111 HOH WAT A . 
C 3 HOH 102 773 112 HOH WAT A . 
C 3 HOH 103 774 113 HOH WAT A . 
C 3 HOH 104 775 114 HOH WAT A . 
C 3 HOH 105 776 115 HOH WAT A . 
C 3 HOH 106 777 116 HOH WAT A . 
C 3 HOH 107 778 117 HOH WAT A . 
C 3 HOH 108 779 118 HOH WAT A . 
C 3 HOH 109 780 119 HOH WAT A . 
C 3 HOH 110 781 120 HOH WAT A . 
C 3 HOH 111 782 121 HOH WAT A . 
C 3 HOH 112 783 122 HOH WAT A . 
C 3 HOH 113 784 123 HOH WAT A . 
C 3 HOH 114 785 124 HOH WAT A . 
C 3 HOH 115 786 125 HOH WAT A . 
C 3 HOH 116 787 126 HOH WAT A . 
C 3 HOH 117 788 127 HOH WAT A . 
C 3 HOH 118 789 128 HOH WAT A . 
C 3 HOH 119 790 129 HOH WAT A . 
C 3 HOH 120 791 130 HOH WAT A . 
C 3 HOH 121 792 132 HOH WAT A . 
C 3 HOH 122 793 133 HOH WAT A . 
C 3 HOH 123 794 134 HOH WAT A . 
C 3 HOH 124 795 135 HOH WAT A . 
C 3 HOH 125 796 136 HOH WAT A . 
C 3 HOH 126 797 137 HOH WAT A . 
C 3 HOH 127 798 138 HOH WAT A . 
C 3 HOH 128 799 139 HOH WAT A . 
C 3 HOH 129 800 140 HOH WAT A . 
C 3 HOH 130 801 141 HOH WAT A . 
C 3 HOH 131 802 142 HOH WAT A . 
C 3 HOH 132 803 143 HOH WAT A . 
C 3 HOH 133 804 144 HOH WAT A . 
C 3 HOH 134 805 145 HOH WAT A . 
C 3 HOH 135 806 146 HOH WAT A . 
C 3 HOH 136 807 147 HOH WAT A . 
C 3 HOH 137 808 148 HOH WAT A . 
C 3 HOH 138 809 149 HOH WAT A . 
C 3 HOH 139 810 150 HOH WAT A . 
C 3 HOH 140 811 152 HOH WAT A . 
C 3 HOH 141 812 153 HOH WAT A . 
C 3 HOH 142 813 154 HOH WAT A . 
C 3 HOH 143 814 155 HOH WAT A . 
C 3 HOH 144 815 156 HOH WAT A . 
C 3 HOH 145 816 157 HOH WAT A . 
C 3 HOH 146 817 158 HOH WAT A . 
C 3 HOH 147 818 159 HOH WAT A . 
C 3 HOH 148 819 160 HOH WAT A . 
C 3 HOH 149 820 161 HOH WAT A . 
C 3 HOH 150 821 162 HOH WAT A . 
C 3 HOH 151 822 164 HOH WAT A . 
C 3 HOH 152 823 165 HOH WAT A . 
C 3 HOH 153 824 166 HOH WAT A . 
C 3 HOH 154 825 167 HOH WAT A . 
C 3 HOH 155 826 168 HOH WAT A . 
C 3 HOH 156 827 169 HOH WAT A . 
C 3 HOH 157 828 170 HOH WAT A . 
C 3 HOH 158 829 171 HOH WAT A . 
C 3 HOH 159 830 172 HOH WAT A . 
C 3 HOH 160 831 173 HOH WAT A . 
C 3 HOH 161 832 174 HOH WAT A . 
C 3 HOH 162 833 175 HOH WAT A . 
C 3 HOH 163 834 178 HOH WAT A . 
C 3 HOH 164 835 179 HOH WAT A . 
C 3 HOH 165 836 180 HOH WAT A . 
C 3 HOH 166 837 181 HOH WAT A . 
C 3 HOH 167 838 182 HOH WAT A . 
C 3 HOH 168 839 183 HOH WAT A . 
C 3 HOH 169 840 184 HOH WAT A . 
C 3 HOH 170 841 185 HOH WAT A . 
C 3 HOH 171 842 186 HOH WAT A . 
C 3 HOH 172 843 187 HOH WAT A . 
C 3 HOH 173 844 188 HOH WAT A . 
C 3 HOH 174 845 189 HOH WAT A . 
C 3 HOH 175 846 190 HOH WAT A . 
C 3 HOH 176 847 191 HOH WAT A . 
C 3 HOH 177 848 192 HOH WAT A . 
C 3 HOH 178 849 193 HOH WAT A . 
C 3 HOH 179 850 194 HOH WAT A . 
C 3 HOH 180 851 195 HOH WAT A . 
C 3 HOH 181 852 196 HOH WAT A . 
C 3 HOH 182 853 197 HOH WAT A . 
C 3 HOH 183 854 198 HOH WAT A . 
C 3 HOH 184 855 199 HOH WAT A . 
C 3 HOH 185 856 200 HOH WAT A . 
C 3 HOH 186 857 201 HOH WAT A . 
C 3 HOH 187 858 202 HOH WAT A . 
C 3 HOH 188 859 203 HOH WAT A . 
C 3 HOH 189 860 204 HOH WAT A . 
C 3 HOH 190 861 205 HOH WAT A . 
C 3 HOH 191 862 206 HOH WAT A . 
C 3 HOH 192 863 207 HOH WAT A . 
C 3 HOH 193 864 208 HOH WAT A . 
C 3 HOH 194 865 209 HOH WAT A . 
C 3 HOH 195 866 211 HOH WAT A . 
C 3 HOH 196 867 212 HOH WAT A . 
C 3 HOH 197 868 213 HOH WAT A . 
C 3 HOH 198 869 214 HOH WAT A . 
C 3 HOH 199 870 216 HOH WAT A . 
C 3 HOH 200 871 218 HOH WAT A . 
C 3 HOH 201 872 219 HOH WAT A . 
C 3 HOH 202 873 220 HOH WAT A . 
C 3 HOH 203 874 221 HOH WAT A . 
C 3 HOH 204 875 222 HOH WAT A . 
C 3 HOH 205 876 223 HOH WAT A . 
C 3 HOH 206 877 224 HOH WAT A . 
C 3 HOH 207 878 225 HOH WAT A . 
C 3 HOH 208 879 226 HOH WAT A . 
C 3 HOH 209 880 227 HOH WAT A . 
C 3 HOH 210 881 228 HOH WAT A . 
C 3 HOH 211 882 229 HOH WAT A . 
C 3 HOH 212 883 230 HOH WAT A . 
C 3 HOH 213 884 231 HOH WAT A . 
C 3 HOH 214 885 232 HOH WAT A . 
C 3 HOH 215 886 233 HOH WAT A . 
C 3 HOH 216 887 234 HOH WAT A . 
C 3 HOH 217 888 236 HOH WAT A . 
C 3 HOH 218 889 238 HOH WAT A . 
C 3 HOH 219 890 239 HOH WAT A . 
C 3 HOH 220 891 240 HOH WAT A . 
C 3 HOH 221 892 241 HOH WAT A . 
C 3 HOH 222 893 242 HOH WAT A . 
C 3 HOH 223 894 243 HOH WAT A . 
C 3 HOH 224 895 244 HOH WAT A . 
C 3 HOH 225 896 245 HOH WAT A . 
C 3 HOH 226 897 246 HOH WAT A . 
C 3 HOH 227 898 247 HOH WAT A . 
C 3 HOH 228 899 248 HOH WAT A . 
C 3 HOH 229 900 249 HOH WAT A . 
C 3 HOH 230 901 250 HOH WAT A . 
C 3 HOH 231 902 251 HOH WAT A . 
C 3 HOH 232 903 252 HOH WAT A . 
C 3 HOH 233 904 253 HOH WAT A . 
C 3 HOH 234 905 254 HOH WAT A . 
C 3 HOH 235 906 255 HOH WAT A . 
C 3 HOH 236 907 257 HOH WAT A . 
C 3 HOH 237 908 258 HOH WAT A . 
C 3 HOH 238 909 260 HOH WAT A . 
C 3 HOH 239 910 261 HOH WAT A . 
C 3 HOH 240 911 262 HOH WAT A . 
C 3 HOH 241 912 265 HOH WAT A . 
C 3 HOH 242 913 266 HOH WAT A . 
C 3 HOH 243 914 267 HOH WAT A . 
C 3 HOH 244 915 268 HOH WAT A . 
C 3 HOH 245 916 269 HOH WAT A . 
C 3 HOH 246 917 272 HOH WAT A . 
C 3 HOH 247 918 273 HOH WAT A . 
C 3 HOH 248 919 274 HOH WAT A . 
C 3 HOH 249 920 275 HOH WAT A . 
C 3 HOH 250 921 276 HOH WAT A . 
C 3 HOH 251 922 277 HOH WAT A . 
C 3 HOH 252 923 278 HOH WAT A . 
C 3 HOH 253 924 279 HOH WAT A . 
C 3 HOH 254 925 280 HOH WAT A . 
C 3 HOH 255 926 281 HOH WAT A . 
C 3 HOH 256 927 283 HOH WAT A . 
C 3 HOH 257 928 284 HOH WAT A . 
C 3 HOH 258 929 285 HOH WAT A . 
C 3 HOH 259 930 286 HOH WAT A . 
C 3 HOH 260 931 287 HOH WAT A . 
C 3 HOH 261 932 288 HOH WAT A . 
C 3 HOH 262 933 289 HOH WAT A . 
C 3 HOH 263 934 290 HOH WAT A . 
C 3 HOH 264 935 291 HOH WAT A . 
C 3 HOH 265 936 292 HOH WAT A . 
C 3 HOH 266 937 293 HOH WAT A . 
C 3 HOH 267 938 295 HOH WAT A . 
C 3 HOH 268 939 297 HOH WAT A . 
C 3 HOH 269 940 298 HOH WAT A . 
C 3 HOH 270 941 299 HOH WAT A . 
C 3 HOH 271 942 300 HOH WAT A . 
C 3 HOH 272 943 301 HOH WAT A . 
C 3 HOH 273 944 302 HOH WAT A . 
C 3 HOH 274 945 303 HOH WAT A . 
C 3 HOH 275 946 304 HOH WAT A . 
C 3 HOH 276 947 305 HOH WAT A . 
C 3 HOH 277 948 307 HOH WAT A . 
C 3 HOH 278 949 308 HOH WAT A . 
C 3 HOH 279 950 309 HOH WAT A . 
C 3 HOH 280 951 310 HOH WAT A . 
C 3 HOH 281 952 311 HOH WAT A . 
C 3 HOH 282 953 312 HOH WAT A . 
C 3 HOH 283 954 313 HOH WAT A . 
C 3 HOH 284 955 315 HOH WAT A . 
C 3 HOH 285 956 316 HOH WAT A . 
C 3 HOH 286 957 317 HOH WAT A . 
D 3 HOH 1   82  16  HOH WAT B . 
D 3 HOH 2   83  24  HOH WAT B . 
D 3 HOH 3   84  30  HOH WAT B . 
D 3 HOH 4   85  36  HOH WAT B . 
D 3 HOH 5   86  53  HOH WAT B . 
D 3 HOH 6   87  56  HOH WAT B . 
D 3 HOH 7   88  68  HOH WAT B . 
D 3 HOH 8   89  72  HOH WAT B . 
D 3 HOH 9   90  106 HOH WAT B . 
D 3 HOH 10  91  131 HOH WAT B . 
D 3 HOH 11  92  163 HOH WAT B . 
D 3 HOH 12  93  176 HOH WAT B . 
D 3 HOH 13  94  177 HOH WAT B . 
D 3 HOH 14  95  210 HOH WAT B . 
D 3 HOH 15  96  215 HOH WAT B . 
D 3 HOH 16  97  217 HOH WAT B . 
D 3 HOH 17  98  235 HOH WAT B . 
D 3 HOH 18  99  237 HOH WAT B . 
D 3 HOH 19  100 256 HOH WAT B . 
D 3 HOH 20  101 263 HOH WAT B . 
D 3 HOH 21  102 271 HOH WAT B . 
D 3 HOH 22  103 282 HOH WAT B . 
D 3 HOH 23  104 294 HOH WAT B . 
D 3 HOH 24  105 314 HOH WAT B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 155 ? CG  ? A GLU 22  CG  
2  1 Y 1 A GLU 155 ? CD  ? A GLU 22  CD  
3  1 Y 1 A GLU 155 ? OE1 ? A GLU 22  OE1 
4  1 Y 1 A GLU 155 ? OE2 ? A GLU 22  OE2 
5  1 Y 1 A LYS 158 ? CG  ? A LYS 25  CG  
6  1 Y 1 A LYS 158 ? CD  ? A LYS 25  CD  
7  1 Y 1 A LYS 158 ? CE  ? A LYS 25  CE  
8  1 Y 1 A LYS 158 ? NZ  ? A LYS 25  NZ  
9  1 Y 1 A LYS 181 ? CG  ? A LYS 48  CG  
10 1 Y 1 A LYS 181 ? CD  ? A LYS 48  CD  
11 1 Y 1 A LYS 181 ? CE  ? A LYS 48  CE  
12 1 Y 1 A LYS 181 ? NZ  ? A LYS 48  NZ  
13 1 Y 1 A LYS 666 ? CG  ? A LYS 533 CG  
14 1 Y 1 A LYS 666 ? CD  ? A LYS 533 CD  
15 1 Y 1 A LYS 666 ? CE  ? A LYS 533 CE  
16 1 Y 1 A LYS 666 ? NZ  ? A LYS 533 NZ  
17 1 Y 1 B LEU 52  ? CG  ? B LEU 52  CG  
18 1 Y 1 B LEU 52  ? CD1 ? B LEU 52  CD1 
19 1 Y 1 B LEU 52  ? CD2 ? B LEU 52  CD2 
20 1 Y 1 B GLN 54  ? CG  ? B GLN 54  CG  
21 1 Y 1 B GLN 54  ? CD  ? B GLN 54  CD  
22 1 Y 1 B GLN 54  ? OE1 ? B GLN 54  OE1 
23 1 Y 1 B GLN 54  ? NE2 ? B GLN 54  NE2 
24 1 Y 1 B ILE 60  ? CG1 ? B ILE 60  CG1 
25 1 Y 1 B ILE 60  ? CG2 ? B ILE 60  CG2 
26 1 Y 1 B ILE 60  ? CD1 ? B ILE 60  CD1 
27 1 Y 1 B GLN 62  ? CG  ? B GLN 62  CG  
28 1 Y 1 B GLN 62  ? CD  ? B GLN 62  CD  
29 1 Y 1 B GLN 62  ? OE1 ? B GLN 62  OE1 
30 1 Y 1 B GLN 62  ? NE2 ? B GLN 62  NE2 
31 1 Y 1 B GLU 77  ? CG  ? B GLU 77  CG  
32 1 Y 1 B GLU 77  ? CD  ? B GLU 77  CD  
33 1 Y 1 B GLU 77  ? OE1 ? B GLU 77  OE1 
34 1 Y 1 B GLU 77  ? OE2 ? B GLU 77  OE2 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MOSFLM 'data reduction' .         ? 1 
SCALA  'data scaling'   .         ? 2 
COMO   phasing          .         ? 3 
CNS    refinement       1.1       ? 4 
CCP4   'data scaling'   '(SCALA)' ? 5 
# 
_cell.entry_id           1M1E 
_cell.length_a           97.750 
_cell.length_b           97.320 
_cell.length_c           86.820 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1M1E 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
# 
_exptl.entry_id          1M1E 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   59.46 
_exptl_crystal.density_Matthews      3.03 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_details    'MES, MPD, DTT, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315' 
_diffrn_detector.pdbx_collection_date   2001-11-28 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    na 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRL BEAMLINE BL11-1' 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL11-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.97 
# 
_reflns.entry_id                     1M1E 
_reflns.observed_criterion_sigma_I   3.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            2.1 
_reflns.number_obs                   47814 
_reflns.number_all                   55512 
_reflns.percent_possible_obs         96.6 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.0590000 
_reflns.pdbx_netI_over_sigmaI        7.8 
_reflns.B_iso_Wilson_estimate        18.2 
_reflns.pdbx_redundancy              3.4 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.1 
_reflns_shell.d_res_low              2.16 
_reflns_shell.percent_possible_all   97.7 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.2500000 
_reflns_shell.meanI_over_sigI_obs    4.7 
_reflns_shell.pdbx_redundancy        2.6 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1M1E 
_refine.ls_number_reflns_obs                     47814 
_refine.ls_number_reflns_all                     47814 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                0 
_refine.ls_d_res_low                             43.56 
_refine.ls_d_res_high                            2.10 
_refine.ls_percent_reflns_obs                    97.4 
_refine.ls_R_factor_obs                          0.2020000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2020000 
_refine.ls_R_factor_R_free                       0.2280000 
_refine.ls_R_factor_R_free_error                 0.005 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  2415 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               35.5 
_refine.aniso_B[1][1]                            2.45 
_refine.aniso_B[2][2]                            6.75 
_refine.aniso_B[3][3]                            -9.20 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.34978 
_refine.solvent_model_param_bsol                 48.0775 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 1I7W' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1M1E 
_refine_analyze.Luzzati_coordinate_error_obs    0.23 
_refine_analyze.Luzzati_sigma_a_obs             0.15 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.27 
_refine_analyze.Luzzati_sigma_a_free            0.20 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4398 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             310 
_refine_hist.number_atoms_total               4708 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        43.56 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d                0.005 ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             1.1   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      18.3  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      0.80  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             1.39  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            2.20  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             2.40  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            3.56  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       2.10 
_refine_ls_shell.d_res_low                        2.23 
_refine_ls_shell.number_reflns_R_work             7473 
_refine_ls_shell.R_factor_R_work                  0.2120000 
_refine_ls_shell.percent_reflns_obs               97.5 
_refine_ls_shell.R_factor_R_free                  0.2460000 
_refine_ls_shell.R_factor_R_free_error            0.012 
_refine_ls_shell.percent_reflns_R_free            4.9 
_refine_ls_shell.number_reflns_R_free             389 
_refine_ls_shell.number_reflns_obs                389 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_all                     ? 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 PROTEIN_REP.PARAM PROTEIN.TOP 'X-RAY DIFFRACTION' 
2 WATER_REP.PARAM   WATER.TOP   'X-RAY DIFFRACTION' 
# 
_database_PDB_matrix.entry_id          1M1E 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_struct.entry_id                  1M1E 
_struct.title                     'Beta-catenin armadillo repeat domain bound to ICAT' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1M1E 
_struct_keywords.pdbx_keywords   'STRUCTURAL PROTEIN' 
_struct_keywords.text            'Cell adhesion, Cytoskeleton, Armadillo repeats, transciption factor, STRUCTURAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
1 UNP CTNB1_MOUSE 1 
;HAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARC
TAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKF
LAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDP
SQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLR
AGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAI
PRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRV
AAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYK
;
134 Q02248 ? 
2 UNP CNBP1_HUMAN 2 
;MNREGAPGKSPEEMYIQQKVRVLLMLRKMGSNLTASEEEFLRTYAGVVNSQLSQLPPHSIDQGAEDVVMAFSRSETEDRR
Q
;
1   Q9NSA3 ? 
# 
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 1M1E A 1 ? 538 ? Q02248 134 ? 671 ? 134 671 
2 2 1M1E B 1 ? 81  ? Q9NSA3 1   ? 81  ? 1   81  
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2950  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  25960 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_struct_biol.id                    1 
_struct_biol.pdbx_parent_biol_id   ? 
_struct_biol.details               ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ARG A 18  ? ASP A 29  ? ARG A 151 ASP A 162 1 ? 12 
HELX_P HELX_P2  2  ASP A 31  ? SER A 46  ? ASP A 164 SER A 179 1 ? 16 
HELX_P HELX_P3  3  LYS A 48  ? ARG A 57  ? LYS A 181 ARG A 190 1 ? 10 
HELX_P HELX_P4  4  SER A 58  ? GLN A 70  ? SER A 191 GLN A 203 1 ? 13 
HELX_P HELX_P5  5  ASP A 74  ? SER A 89  ? ASP A 207 SER A 222 1 ? 16 
HELX_P HELX_P6  6  HIS A 91  ? SER A 101 ? HIS A 224 SER A 234 1 ? 11 
HELX_P HELX_P7  7  GLY A 102 ? LEU A 111 ? GLY A 235 LEU A 244 1 ? 10 
HELX_P HELX_P8  8  VAL A 115 ? GLN A 133 ? VAL A 248 GLN A 266 1 ? 19 
HELX_P HELX_P9  9  GLY A 135 ? ALA A 143 ? GLY A 268 ALA A 276 1 ? 9  
HELX_P HELX_P10 10 GLY A 144 ? LEU A 152 ? GLY A 277 LEU A 285 1 ? 9  
HELX_P HELX_P11 11 LEU A 153 ? LYS A 155 ? LEU A 286 LYS A 288 5 ? 3  
HELX_P HELX_P12 12 ASN A 157 ? TYR A 173 ? ASN A 290 TYR A 306 1 ? 17 
HELX_P HELX_P13 13 ASN A 175 ? SER A 185 ? ASN A 308 SER A 318 1 ? 11 
HELX_P HELX_P14 14 GLY A 186 ? TYR A 198 ? GLY A 319 TYR A 331 1 ? 13 
HELX_P HELX_P15 15 TYR A 200 ? SER A 215 ? TYR A 333 SER A 348 1 ? 16 
HELX_P HELX_P16 16 SER A 219 ? ALA A 227 ? SER A 352 ALA A 360 1 ? 9  
HELX_P HELX_P17 17 GLY A 228 ? LEU A 235 ? GLY A 361 LEU A 368 1 ? 8  
HELX_P HELX_P18 18 SER A 241 ? SER A 256 ? SER A 374 SER A 389 1 ? 16 
HELX_P HELX_P19 19 ASP A 257 ? ALA A 259 ? ASP A 390 ALA A 392 5 ? 3  
HELX_P HELX_P20 20 MET A 265 ? LEU A 276 ? MET A 398 LEU A 409 1 ? 12 
HELX_P HELX_P21 21 ASP A 280 ? THR A 295 ? ASP A 413 THR A 428 1 ? 16 
HELX_P HELX_P22 22 ASN A 298 ? VAL A 308 ? ASN A 431 VAL A 441 1 ? 11 
HELX_P HELX_P23 23 GLY A 309 ? GLY A 322 ? GLY A 442 GLY A 455 1 ? 14 
HELX_P HELX_P24 24 ARG A 324 ? THR A 339 ? ARG A 457 THR A 472 1 ? 16 
HELX_P HELX_P25 25 GLU A 344 ? HIS A 355 ? GLU A 477 HIS A 488 1 ? 12 
HELX_P HELX_P26 26 GLY A 357 ? LEU A 364 ? GLY A 490 LEU A 497 1 ? 8  
HELX_P HELX_P27 27 HIS A 370 ? ALA A 385 ? HIS A 503 ALA A 518 1 ? 16 
HELX_P HELX_P28 28 LEU A 386 ? ALA A 389 ? LEU A 519 ALA A 522 5 ? 4  
HELX_P HELX_P29 29 ASN A 390 ? GLN A 397 ? ASN A 523 GLN A 530 1 ? 8  
HELX_P HELX_P30 30 GLY A 398 ? ARG A 416 ? GLY A 531 ARG A 549 1 ? 19 
HELX_P HELX_P31 31 MET A 433 ? ALA A 448 ? MET A 566 ALA A 581 1 ? 16 
HELX_P HELX_P32 32 ASP A 450 ? LEU A 460 ? ASP A 583 LEU A 593 1 ? 11 
HELX_P HELX_P33 33 THR A 462 ? LEU A 470 ? THR A 595 LEU A 603 1 ? 9  
HELX_P HELX_P34 34 ILE A 474 ? ALA A 489 ? ILE A 607 ALA A 622 1 ? 16 
HELX_P HELX_P35 35 ASP A 491 ? GLU A 501 ? ASP A 624 GLU A 634 1 ? 11 
HELX_P HELX_P36 36 ALA A 503 ? LEU A 511 ? ALA A 636 LEU A 644 1 ? 9  
HELX_P HELX_P37 37 ASN A 515 ? SER A 530 ? ASN A 648 SER A 663 1 ? 16 
HELX_P HELX_P38 38 SER B 10  ? MET B 29  ? SER B 10  MET B 29  1 ? 20 
HELX_P HELX_P39 39 THR B 34  ? TYR B 44  ? THR B 34  TYR B 44  1 ? 11 
HELX_P HELX_P40 40 TYR B 44  ? SER B 53  ? TYR B 44  SER B 53  1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           367 
_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           PRO 
_struct_mon_prot_cis.auth_seq_id            500 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    368 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     501 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       0.79 
# 
_struct_sheet.id               A 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     A 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 PHE A 427 ? VAL A 428 ? PHE A 560 VAL A 561 
A 2 VAL A 431 ? ARG A 432 ? VAL A 564 ARG A 565 
# 
_pdbx_struct_sheet_hbond.sheet_id                A 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   VAL 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    428 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    VAL 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     561 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   VAL 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    431 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    VAL 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     564 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 430 ? ? 58.27   16.96   
2 1 ASP A 665 ? ? -14.04  -91.62  
3 1 PRO A 667 ? ? -28.05  92.99   
4 1 GLN A 668 ? ? -100.39 -79.45  
5 1 ASP B 61  ? ? -55.10  -158.83 
6 1 GLN B 62  ? ? 74.32   36.01   
7 1 ALA B 64  ? ? -62.72  48.10   
8 1 GLU B 75  ? ? -80.86  -153.47 
9 1 GLU B 77  ? ? 69.74   -160.03 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A HIS 134 ? A HIS 1   
2  1 Y 1 A ALA 135 ? A ALA 2   
3  1 Y 1 A VAL 136 ? A VAL 3   
4  1 Y 1 A VAL 137 ? A VAL 4   
5  1 Y 1 A ASN 138 ? A ASN 5   
6  1 Y 1 A LEU 139 ? A LEU 6   
7  1 Y 1 A ILE 140 ? A ILE 7   
8  1 Y 1 A ASN 141 ? A ASN 8   
9  1 Y 1 A TYR 142 ? A TYR 9   
10 1 Y 1 A GLN 143 ? A GLN 10  
11 1 Y 1 A ASP 144 ? A ASP 11  
12 1 Y 1 A ASP 145 ? A ASP 12  
13 1 Y 1 A ALA 146 ? A ALA 13  
14 1 Y 1 A GLU 147 ? A GLU 14  
15 1 Y 1 A LEU 148 ? A LEU 15  
16 1 Y 1 A ALA 149 ? A ALA 16  
17 1 Y 1 A THR 150 ? A THR 17  
18 1 Y 1 A ARG 550 ? A ARG 417 
19 1 Y 1 A THR 551 ? A THR 418 
20 1 Y 1 A SER 552 ? A SER 419 
21 1 Y 1 A MET 553 ? A MET 420 
22 1 Y 1 A GLY 554 ? A GLY 421 
23 1 Y 1 A GLY 555 ? A GLY 422 
24 1 Y 1 A THR 556 ? A THR 423 
25 1 Y 1 A GLN 557 ? A GLN 424 
26 1 Y 1 A GLN 558 ? A GLN 425 
27 1 Y 1 B MET 1   ? B MET 1   
28 1 Y 1 B ASN 2   ? B ASN 2   
29 1 Y 1 B ARG 3   ? B ARG 3   
30 1 Y 1 B GLU 4   ? B GLU 4   
31 1 Y 1 B GLY 5   ? B GLY 5   
32 1 Y 1 B ALA 6   ? B ALA 6   
33 1 Y 1 B PRO 7   ? B PRO 7   
34 1 Y 1 B GLY 8   ? B GLY 8   
35 1 Y 1 B LEU 55  ? B LEU 55  
36 1 Y 1 B PRO 56  ? B PRO 56  
37 1 Y 1 B PRO 57  ? B PRO 57  
38 1 Y 1 B HIS 58  ? B HIS 58  
39 1 Y 1 B SER 59  ? B SER 59  
40 1 Y 1 B ARG 79  ? B ARG 79  
41 1 Y 1 B ARG 80  ? B ARG 80  
42 1 Y 1 B GLN 81  ? B GLN 81  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1I7W 
_pdbx_initial_refinement_model.details          'PDB ENTRY 1I7W' 
# 
_atom_sites.entry_id                    1M1E 
_atom_sites.fract_transf_matrix[1][1]   0.010230 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010275 
_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]   0.011518 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ARG A 1 18  ? 11.573 31.162  66.914  1.00 65.90  ? 151 ARG A N   1 
ATOM   2    C CA  . ARG A 1 18  ? 10.402 32.081  66.814  1.00 65.95  ? 151 ARG A CA  1 
ATOM   3    C C   . ARG A 1 18  ? 9.295  31.514  65.921  1.00 64.24  ? 151 ARG A C   1 
ATOM   4    O O   . ARG A 1 18  ? 8.827  30.391  66.125  1.00 63.73  ? 151 ARG A O   1 
ATOM   5    C CB  . ARG A 1 18  ? 10.852 33.447  66.280  1.00 67.99  ? 151 ARG A CB  1 
ATOM   6    C CG  . ARG A 1 18  ? 11.470 33.408  64.889  1.00 70.89  ? 151 ARG A CG  1 
ATOM   7    C CD  . ARG A 1 18  ? 11.967 34.780  64.469  1.00 73.36  ? 151 ARG A CD  1 
ATOM   8    N NE  . ARG A 1 18  ? 12.399 34.804  63.074  1.00 75.49  ? 151 ARG A NE  1 
ATOM   9    C CZ  . ARG A 1 18  ? 12.939 35.863  62.479  1.00 76.20  ? 151 ARG A CZ  1 
ATOM   10   N NH1 . ARG A 1 18  ? 13.118 36.989  63.160  1.00 77.32  ? 151 ARG A NH1 1 
ATOM   11   N NH2 . ARG A 1 18  ? 13.293 35.804  61.202  1.00 75.36  ? 151 ARG A NH2 1 
ATOM   12   N N   . ALA A 1 19  ? 8.880  32.303  64.934  1.00 62.28  ? 152 ALA A N   1 
ATOM   13   C CA  . ALA A 1 19  ? 7.828  31.903  64.008  1.00 60.32  ? 152 ALA A CA  1 
ATOM   14   C C   . ALA A 1 19  ? 8.159  30.623  63.247  1.00 58.39  ? 152 ALA A C   1 
ATOM   15   O O   . ALA A 1 19  ? 7.360  29.685  63.219  1.00 58.23  ? 152 ALA A O   1 
ATOM   16   C CB  . ALA A 1 19  ? 7.556  33.031  63.027  1.00 61.24  ? 152 ALA A CB  1 
ATOM   17   N N   . ILE A 1 20  ? 9.335  30.590  62.627  1.00 56.48  ? 153 ILE A N   1 
ATOM   18   C CA  . ILE A 1 20  ? 9.755  29.422  61.858  1.00 54.46  ? 153 ILE A CA  1 
ATOM   19   C C   . ILE A 1 20  ? 9.552  28.135  62.662  1.00 53.07  ? 153 ILE A C   1 
ATOM   20   O O   . ILE A 1 20  ? 8.803  27.249  62.247  1.00 51.21  ? 153 ILE A O   1 
ATOM   21   C CB  . ILE A 1 20  ? 11.244 29.529  61.429  1.00 53.76  ? 153 ILE A CB  1 
ATOM   22   C CG1 . ILE A 1 20  ? 11.484 30.837  60.668  1.00 53.69  ? 153 ILE A CG1 1 
ATOM   23   C CG2 . ILE A 1 20  ? 11.626 28.331  60.569  1.00 54.26  ? 153 ILE A CG2 1 
ATOM   24   C CD1 . ILE A 1 20  ? 10.692 30.972  59.383  1.00 53.55  ? 153 ILE A CD1 1 
ATOM   25   N N   . PRO A 1 21  ? 10.205 28.021  63.832  1.00 52.73  ? 154 PRO A N   1 
ATOM   26   C CA  . PRO A 1 21  ? 10.057 26.817  64.655  1.00 52.89  ? 154 PRO A CA  1 
ATOM   27   C C   . PRO A 1 21  ? 8.604  26.431  64.919  1.00 52.61  ? 154 PRO A C   1 
ATOM   28   O O   . PRO A 1 21  ? 8.231  25.264  64.789  1.00 52.58  ? 154 PRO A O   1 
ATOM   29   C CB  . PRO A 1 21  ? 10.804 27.186  65.930  1.00 53.29  ? 154 PRO A CB  1 
ATOM   30   C CG  . PRO A 1 21  ? 11.912 28.043  65.410  1.00 54.10  ? 154 PRO A CG  1 
ATOM   31   C CD  . PRO A 1 21  ? 11.175 28.947  64.445  1.00 53.05  ? 154 PRO A CD  1 
ATOM   32   N N   . GLU A 1 22  ? 7.787  27.413  65.287  1.00 53.09  ? 155 GLU A N   1 
ATOM   33   C CA  . GLU A 1 22  ? 6.376  27.164  65.565  1.00 52.82  ? 155 GLU A CA  1 
ATOM   34   C C   . GLU A 1 22  ? 5.653  26.712  64.299  1.00 52.07  ? 155 GLU A C   1 
ATOM   35   O O   . GLU A 1 22  ? 4.922  25.717  64.306  1.00 52.06  ? 155 GLU A O   1 
ATOM   36   C CB  . GLU A 1 22  ? 5.721  28.427  66.129  1.00 53.04  ? 155 GLU A CB  1 
ATOM   37   N N   . LEU A 1 23  ? 5.864  27.446  63.210  1.00 51.82  ? 156 LEU A N   1 
ATOM   38   C CA  . LEU A 1 23  ? 5.239  27.115  61.935  1.00 50.90  ? 156 LEU A CA  1 
ATOM   39   C C   . LEU A 1 23  ? 5.651  25.716  61.490  1.00 49.67  ? 156 LEU A C   1 
ATOM   40   O O   . LEU A 1 23  ? 4.822  24.944  61.006  1.00 49.24  ? 156 LEU A O   1 
ATOM   41   C CB  . LEU A 1 23  ? 5.634  28.146  60.877  1.00 51.43  ? 156 LEU A CB  1 
ATOM   42   C CG  . LEU A 1 23  ? 5.100  29.561  61.124  1.00 52.25  ? 156 LEU A CG  1 
ATOM   43   C CD1 . LEU A 1 23  ? 5.765  30.538  60.173  1.00 53.36  ? 156 LEU A CD1 1 
ATOM   44   C CD2 . LEU A 1 23  ? 3.587  29.575  60.947  1.00 51.76  ? 156 LEU A CD2 1 
ATOM   45   N N   . THR A 1 24  ? 6.931  25.393  61.660  1.00 48.77  ? 157 THR A N   1 
ATOM   46   C CA  . THR A 1 24  ? 7.441  24.077  61.288  1.00 48.99  ? 157 THR A CA  1 
ATOM   47   C C   . THR A 1 24  ? 6.673  23.011  62.060  1.00 50.46  ? 157 THR A C   1 
ATOM   48   O O   . THR A 1 24  ? 6.220  22.019  61.489  1.00 49.94  ? 157 THR A O   1 
ATOM   49   C CB  . THR A 1 24  ? 8.943  23.929  61.626  1.00 47.78  ? 157 THR A CB  1 
ATOM   50   O OG1 . THR A 1 24  ? 9.709  24.849  60.841  1.00 46.88  ? 157 THR A OG1 1 
ATOM   51   C CG2 . THR A 1 24  ? 9.416  22.517  61.335  1.00 46.15  ? 157 THR A CG2 1 
ATOM   52   N N   . LYS A 1 25  ? 6.538  23.227  63.365  1.00 52.29  ? 158 LYS A N   1 
ATOM   53   C CA  . LYS A 1 25  ? 5.827  22.295  64.229  1.00 54.41  ? 158 LYS A CA  1 
ATOM   54   C C   . LYS A 1 25  ? 4.374  22.168  63.775  1.00 55.89  ? 158 LYS A C   1 
ATOM   55   O O   . LYS A 1 25  ? 3.838  21.063  63.676  1.00 56.12  ? 158 LYS A O   1 
ATOM   56   C CB  . LYS A 1 25  ? 5.891  22.776  65.679  1.00 53.77  ? 158 LYS A CB  1 
ATOM   57   N N   . LEU A 1 26  ? 3.746  23.305  63.488  1.00 57.25  ? 159 LEU A N   1 
ATOM   58   C CA  . LEU A 1 26  ? 2.359  23.320  63.040  1.00 58.93  ? 159 LEU A CA  1 
ATOM   59   C C   . LEU A 1 26  ? 2.146  22.516  61.760  1.00 59.92  ? 159 LEU A C   1 
ATOM   60   O O   . LEU A 1 26  ? 1.133  21.831  61.616  1.00 59.80  ? 159 LEU A O   1 
ATOM   61   C CB  . LEU A 1 26  ? 1.886  24.763  62.834  1.00 59.29  ? 159 LEU A CB  1 
ATOM   62   C CG  . LEU A 1 26  ? 1.703  25.582  64.117  1.00 60.17  ? 159 LEU A CG  1 
ATOM   63   C CD1 . LEU A 1 26  ? 1.375  27.029  63.779  1.00 59.56  ? 159 LEU A CD1 1 
ATOM   64   C CD2 . LEU A 1 26  ? 0.591  24.963  64.952  1.00 60.21  ? 159 LEU A CD2 1 
ATOM   65   N N   . LEU A 1 27  ? 3.095  22.598  60.831  1.00 60.92  ? 160 LEU A N   1 
ATOM   66   C CA  . LEU A 1 27  ? 2.982  21.859  59.575  1.00 61.68  ? 160 LEU A CA  1 
ATOM   67   C C   . LEU A 1 27  ? 3.050  20.355  59.805  1.00 63.11  ? 160 LEU A C   1 
ATOM   68   O O   . LEU A 1 27  ? 2.479  19.577  59.039  1.00 62.82  ? 160 LEU A O   1 
ATOM   69   C CB  . LEU A 1 27  ? 4.085  22.277  58.598  1.00 60.01  ? 160 LEU A CB  1 
ATOM   70   C CG  . LEU A 1 27  ? 3.881  23.585  57.833  1.00 58.69  ? 160 LEU A CG  1 
ATOM   71   C CD1 . LEU A 1 27  ? 5.108  23.874  56.995  1.00 57.90  ? 160 LEU A CD1 1 
ATOM   72   C CD2 . LEU A 1 27  ? 2.650  23.483  56.948  1.00 57.18  ? 160 LEU A CD2 1 
ATOM   73   N N   . ASN A 1 28  ? 3.750  19.949  60.860  1.00 65.53  ? 161 ASN A N   1 
ATOM   74   C CA  . ASN A 1 28  ? 3.886  18.534  61.187  1.00 68.09  ? 161 ASN A CA  1 
ATOM   75   C C   . ASN A 1 28  ? 2.732  18.060  62.063  1.00 69.80  ? 161 ASN A C   1 
ATOM   76   O O   . ASN A 1 28  ? 2.601  16.868  62.339  1.00 69.94  ? 161 ASN A O   1 
ATOM   77   C CB  . ASN A 1 28  ? 5.209  18.278  61.913  1.00 67.95  ? 161 ASN A CB  1 
ATOM   78   C CG  . ASN A 1 28  ? 6.416  18.584  61.050  1.00 68.73  ? 161 ASN A CG  1 
ATOM   79   O OD1 . ASN A 1 28  ? 6.555  18.053  59.949  1.00 68.21  ? 161 ASN A OD1 1 
ATOM   80   N ND2 . ASN A 1 28  ? 7.301  19.441  61.551  1.00 68.29  ? 161 ASN A ND2 1 
ATOM   81   N N   . ASP A 1 29  ? 1.899  18.999  62.496  1.00 72.17  ? 162 ASP A N   1 
ATOM   82   C CA  . ASP A 1 29  ? 0.758  18.682  63.348  1.00 75.00  ? 162 ASP A CA  1 
ATOM   83   C C   . ASP A 1 29  ? -0.126 17.618  62.699  1.00 76.41  ? 162 ASP A C   1 
ATOM   84   O O   . ASP A 1 29  ? -0.200 17.522  61.474  1.00 76.42  ? 162 ASP A O   1 
ATOM   85   C CB  . ASP A 1 29  ? -0.052 19.951  63.622  1.00 75.57  ? 162 ASP A CB  1 
ATOM   86   C CG  . ASP A 1 29  ? -1.055 19.774  64.745  1.00 76.44  ? 162 ASP A CG  1 
ATOM   87   O OD1 . ASP A 1 29  ? -1.991 18.962  64.590  1.00 76.80  ? 162 ASP A OD1 1 
ATOM   88   O OD2 . ASP A 1 29  ? -0.903 20.448  65.786  1.00 76.33  ? 162 ASP A OD2 1 
ATOM   89   N N   . GLU A 1 30  ? -0.792 16.819  63.529  1.00 78.08  ? 163 GLU A N   1 
ATOM   90   C CA  . GLU A 1 30  ? -1.661 15.752  63.042  1.00 79.87  ? 163 GLU A CA  1 
ATOM   91   C C   . GLU A 1 30  ? -3.010 16.280  62.560  1.00 80.44  ? 163 GLU A C   1 
ATOM   92   O O   . GLU A 1 30  ? -3.704 15.619  61.786  1.00 80.23  ? 163 GLU A O   1 
ATOM   93   C CB  . GLU A 1 30  ? -1.884 14.706  64.141  1.00 80.90  ? 163 GLU A CB  1 
ATOM   94   C CG  . GLU A 1 30  ? -0.609 14.062  64.677  1.00 82.03  ? 163 GLU A CG  1 
ATOM   95   C CD  . GLU A 1 30  ? 0.179  14.978  65.601  1.00 82.97  ? 163 GLU A CD  1 
ATOM   96   O OE1 . GLU A 1 30  ? 1.261  14.564  66.067  1.00 83.34  ? 163 GLU A OE1 1 
ATOM   97   O OE2 . GLU A 1 30  ? -0.283 16.108  65.867  1.00 83.36  ? 163 GLU A OE2 1 
ATOM   98   N N   . ASP A 1 31  ? -3.381 17.469  63.025  1.00 81.35  ? 164 ASP A N   1 
ATOM   99   C CA  . ASP A 1 31  ? -4.644 18.081  62.630  1.00 82.23  ? 164 ASP A CA  1 
ATOM   100  C C   . ASP A 1 31  ? -4.479 18.770  61.283  1.00 82.19  ? 164 ASP A C   1 
ATOM   101  O O   . ASP A 1 31  ? -3.947 19.875  61.198  1.00 81.91  ? 164 ASP A O   1 
ATOM   102  C CB  . ASP A 1 31  ? -5.098 19.098  63.680  1.00 83.34  ? 164 ASP A CB  1 
ATOM   103  C CG  . ASP A 1 31  ? -6.371 19.819  63.277  1.00 84.54  ? 164 ASP A CG  1 
ATOM   104  O OD1 . ASP A 1 31  ? -7.375 19.136  62.986  1.00 85.51  ? 164 ASP A OD1 1 
ATOM   105  O OD2 . ASP A 1 31  ? -6.369 21.069  63.250  1.00 85.30  ? 164 ASP A OD2 1 
ATOM   106  N N   . GLN A 1 32  ? -4.944 18.109  60.231  1.00 82.24  ? 165 GLN A N   1 
ATOM   107  C CA  . GLN A 1 32  ? -4.839 18.644  58.881  1.00 82.44  ? 165 GLN A CA  1 
ATOM   108  C C   . GLN A 1 32  ? -5.329 20.086  58.752  1.00 82.14  ? 165 GLN A C   1 
ATOM   109  O O   . GLN A 1 32  ? -4.799 20.855  57.952  1.00 82.85  ? 165 GLN A O   1 
ATOM   110  C CB  . GLN A 1 32  ? -5.610 17.748  57.914  1.00 82.89  ? 165 GLN A CB  1 
ATOM   111  C CG  . GLN A 1 32  ? -5.519 18.181  56.467  1.00 84.29  ? 165 GLN A CG  1 
ATOM   112  C CD  . GLN A 1 32  ? -6.211 17.214  55.535  1.00 85.34  ? 165 GLN A CD  1 
ATOM   113  O OE1 . GLN A 1 32  ? -5.829 16.047  55.438  1.00 86.23  ? 165 GLN A OE1 1 
ATOM   114  N NE2 . GLN A 1 32  ? -7.240 17.691  54.843  1.00 85.62  ? 165 GLN A NE2 1 
ATOM   115  N N   . VAL A 1 33  ? -6.331 20.457  59.540  1.00 81.30  ? 166 VAL A N   1 
ATOM   116  C CA  . VAL A 1 33  ? -6.875 21.810  59.478  1.00 80.51  ? 166 VAL A CA  1 
ATOM   117  C C   . VAL A 1 33  ? -5.856 22.885  59.853  1.00 79.88  ? 166 VAL A C   1 
ATOM   118  O O   . VAL A 1 33  ? -5.942 24.020  59.379  1.00 79.65  ? 166 VAL A O   1 
ATOM   119  C CB  . VAL A 1 33  ? -8.106 21.961  60.398  1.00 80.50  ? 166 VAL A CB  1 
ATOM   120  C CG1 . VAL A 1 33  ? -8.715 23.345  60.228  1.00 80.02  ? 166 VAL A CG1 1 
ATOM   121  C CG2 . VAL A 1 33  ? -9.130 20.885  60.075  1.00 80.60  ? 166 VAL A CG2 1 
ATOM   122  N N   . VAL A 1 34  ? -4.891 22.533  60.699  1.00 78.96  ? 167 VAL A N   1 
ATOM   123  C CA  . VAL A 1 34  ? -3.881 23.496  61.125  1.00 77.94  ? 167 VAL A CA  1 
ATOM   124  C C   . VAL A 1 34  ? -2.742 23.647  60.120  1.00 76.90  ? 167 VAL A C   1 
ATOM   125  O O   . VAL A 1 34  ? -2.199 24.740  59.955  1.00 76.53  ? 167 VAL A O   1 
ATOM   126  C CB  . VAL A 1 34  ? -3.281 23.121  62.504  1.00 78.31  ? 167 VAL A CB  1 
ATOM   127  C CG1 . VAL A 1 34  ? -2.463 21.848  62.396  1.00 77.81  ? 167 VAL A CG1 1 
ATOM   128  C CG2 . VAL A 1 34  ? -2.421 24.264  63.024  1.00 78.10  ? 167 VAL A CG2 1 
ATOM   129  N N   . VAL A 1 35  ? -2.381 22.558  59.447  1.00 76.14  ? 168 VAL A N   1 
ATOM   130  C CA  . VAL A 1 35  ? -1.300 22.607  58.466  1.00 75.56  ? 168 VAL A CA  1 
ATOM   131  C C   . VAL A 1 35  ? -1.656 23.545  57.315  1.00 74.89  ? 168 VAL A C   1 
ATOM   132  O O   . VAL A 1 35  ? -0.836 24.359  56.893  1.00 75.03  ? 168 VAL A O   1 
ATOM   133  C CB  . VAL A 1 35  ? -0.977 21.200  57.895  1.00 74.93  ? 168 VAL A CB  1 
ATOM   134  C CG1 . VAL A 1 35  ? -0.706 20.232  59.031  1.00 74.83  ? 168 VAL A CG1 1 
ATOM   135  C CG2 . VAL A 1 35  ? -2.114 20.701  57.032  1.00 75.08  ? 168 VAL A CG2 1 
ATOM   136  N N   . ASN A 1 36  ? -2.883 23.429  56.818  0.50 74.10  ? 169 ASN A N   1 
ATOM   137  C CA  . ASN A 1 36  ? -3.353 24.268  55.724  0.50 73.27  ? 169 ASN A CA  1 
ATOM   138  C C   . ASN A 1 36  ? -3.249 25.730  56.122  0.50 72.64  ? 169 ASN A C   1 
ATOM   139  O O   . ASN A 1 36  ? -2.965 26.596  55.295  0.50 72.36  ? 169 ASN A O   1 
ATOM   140  C CB  . ASN A 1 36  ? -4.805 23.930  55.396  0.50 74.09  ? 169 ASN A CB  1 
ATOM   141  C CG  . ASN A 1 36  ? -4.970 22.512  54.896  1.00 75.18  ? 169 ASN A CG  1 
ATOM   142  O OD1 . ASN A 1 36  ? -4.492 21.563  55.513  1.00 74.98  ? 169 ASN A OD1 1 
ATOM   143  N ND2 . ASN A 1 36  ? -5.654 22.361  53.771  1.00 76.60  ? 169 ASN A ND2 1 
ATOM   144  N N   . LYS A 1 37  ? -3.483 25.991  57.402  1.00 72.09  ? 170 LYS A N   1 
ATOM   145  C CA  . LYS A 1 37  ? -3.423 27.343  57.938  1.00 71.65  ? 170 LYS A CA  1 
ATOM   146  C C   . LYS A 1 37  ? -1.970 27.736  58.177  1.00 70.50  ? 170 LYS A C   1 
ATOM   147  O O   . LYS A 1 37  ? -1.625 28.918  58.178  1.00 70.71  ? 170 LYS A O   1 
ATOM   148  C CB  . LYS A 1 37  ? -4.221 27.416  59.243  1.00 72.66  ? 170 LYS A CB  1 
ATOM   149  C CG  . LYS A 1 37  ? -4.292 28.799  59.870  1.00 73.85  ? 170 LYS A CG  1 
ATOM   150  C CD  . LYS A 1 37  ? -5.414 28.879  60.901  1.00 74.77  ? 170 LYS A CD  1 
ATOM   151  C CE  . LYS A 1 37  ? -5.268 27.822  61.990  1.00 75.69  ? 170 LYS A CE  1 
ATOM   152  N NZ  . LYS A 1 37  ? -6.376 27.888  62.986  1.00 75.29  ? 170 LYS A NZ  1 
ATOM   153  N N   . ALA A 1 38  ? -1.123 26.731  58.374  1.00 68.99  ? 171 ALA A N   1 
ATOM   154  C CA  . ALA A 1 38  ? 0.297  26.963  58.601  1.00 67.51  ? 171 ALA A CA  1 
ATOM   155  C C   . ALA A 1 38  ? 0.986  27.192  57.260  1.00 66.23  ? 171 ALA A C   1 
ATOM   156  O O   . ALA A 1 38  ? 1.967  27.928  57.171  1.00 66.44  ? 171 ALA A O   1 
ATOM   157  C CB  . ALA A 1 38  ? 0.915  25.764  59.311  1.00 67.20  ? 171 ALA A CB  1 
ATOM   158  N N   . ALA A 1 39  ? 0.455  26.560  56.218  1.00 65.14  ? 172 ALA A N   1 
ATOM   159  C CA  . ALA A 1 39  ? 1.007  26.684  54.875  1.00 64.16  ? 172 ALA A CA  1 
ATOM   160  C C   . ALA A 1 39  ? 0.825  28.098  54.334  1.00 63.66  ? 172 ALA A C   1 
ATOM   161  O O   . ALA A 1 39  ? 1.744  28.668  53.745  1.00 63.41  ? 172 ALA A O   1 
ATOM   162  C CB  . ALA A 1 39  ? 0.343  25.678  53.946  1.00 63.15  ? 172 ALA A CB  1 
ATOM   163  N N   . VAL A 1 40  ? -0.362 28.662  54.539  1.00 63.33  ? 173 VAL A N   1 
ATOM   164  C CA  . VAL A 1 40  ? -0.655 30.012  54.069  1.00 62.73  ? 173 VAL A CA  1 
ATOM   165  C C   . VAL A 1 40  ? 0.305  31.019  54.691  1.00 63.18  ? 173 VAL A C   1 
ATOM   166  O O   . VAL A 1 40  ? 0.830  31.901  54.006  1.00 62.93  ? 173 VAL A O   1 
ATOM   167  C CB  . VAL A 1 40  ? -2.102 30.428  54.419  1.00 63.16  ? 173 VAL A CB  1 
ATOM   168  C CG1 . VAL A 1 40  ? -2.343 31.876  54.009  1.00 61.53  ? 173 VAL A CG1 1 
ATOM   169  C CG2 . VAL A 1 40  ? -3.093 29.502  53.722  1.00 61.99  ? 173 VAL A CG2 1 
ATOM   170  N N   . MET A 1 41  ? 0.526  30.886  55.995  1.00 63.55  ? 174 MET A N   1 
ATOM   171  C CA  . MET A 1 41  ? 1.425  31.783  56.710  1.00 63.79  ? 174 MET A CA  1 
ATOM   172  C C   . MET A 1 41  ? 2.840  31.712  56.150  1.00 61.82  ? 174 MET A C   1 
ATOM   173  O O   . MET A 1 41  ? 3.468  32.741  55.895  1.00 61.15  ? 174 MET A O   1 
ATOM   174  C CB  . MET A 1 41  ? 1.446  31.437  58.202  1.00 66.75  ? 174 MET A CB  1 
ATOM   175  C CG  . MET A 1 41  ? 0.216  31.898  58.968  1.00 70.58  ? 174 MET A CG  1 
ATOM   176  S SD  . MET A 1 41  ? 0.061  33.701  58.984  1.00 75.89  ? 174 MET A SD  1 
ATOM   177  C CE  . MET A 1 41  ? 1.140  34.127  60.366  1.00 74.28  ? 174 MET A CE  1 
ATOM   178  N N   . VAL A 1 42  ? 3.340  30.494  55.962  1.00 60.12  ? 175 VAL A N   1 
ATOM   179  C CA  . VAL A 1 42  ? 4.684  30.304  55.432  1.00 58.02  ? 175 VAL A CA  1 
ATOM   180  C C   . VAL A 1 42  ? 4.780  30.880  54.024  1.00 56.89  ? 175 VAL A C   1 
ATOM   181  O O   . VAL A 1 42  ? 5.703  31.636  53.715  1.00 56.05  ? 175 VAL A O   1 
ATOM   182  C CB  . VAL A 1 42  ? 5.068  28.812  55.392  1.00 57.84  ? 175 VAL A CB  1 
ATOM   183  C CG1 . VAL A 1 42  ? 6.471  28.652  54.825  1.00 56.85  ? 175 VAL A CG1 1 
ATOM   184  C CG2 . VAL A 1 42  ? 4.988  28.221  56.791  1.00 56.79  ? 175 VAL A CG2 1 
ATOM   185  N N   . HIS A 1 43  ? 3.823  30.521  53.173  1.00 56.13  ? 176 HIS A N   1 
ATOM   186  C CA  . HIS A 1 43  ? 3.808  31.020  51.805  1.00 55.79  ? 176 HIS A CA  1 
ATOM   187  C C   . HIS A 1 43  ? 3.787  32.543  51.819  1.00 54.96  ? 176 HIS A C   1 
ATOM   188  O O   . HIS A 1 43  ? 4.435  33.189  50.996  1.00 54.14  ? 176 HIS A O   1 
ATOM   189  C CB  . HIS A 1 43  ? 2.585  30.487  51.051  1.00 56.81  ? 176 HIS A CB  1 
ATOM   190  C CG  . HIS A 1 43  ? 2.429  31.059  49.674  1.00 58.41  ? 176 HIS A CG  1 
ATOM   191  N ND1 . HIS A 1 43  ? 3.425  30.992  48.723  1.00 58.03  ? 176 HIS A ND1 1 
ATOM   192  C CD2 . HIS A 1 43  ? 1.399  31.720  49.093  1.00 58.77  ? 176 HIS A CD2 1 
ATOM   193  C CE1 . HIS A 1 43  ? 3.016  31.589  47.617  1.00 58.26  ? 176 HIS A CE1 1 
ATOM   194  N NE2 . HIS A 1 43  ? 1.790  32.040  47.816  1.00 58.97  ? 176 HIS A NE2 1 
ATOM   195  N N   . GLN A 1 44  ? 3.044  33.111  52.763  1.00 55.29  ? 177 GLN A N   1 
ATOM   196  C CA  . GLN A 1 44  ? 2.947  34.562  52.884  1.00 55.48  ? 177 GLN A CA  1 
ATOM   197  C C   . GLN A 1 44  ? 4.282  35.152  53.335  1.00 55.19  ? 177 GLN A C   1 
ATOM   198  O O   . GLN A 1 44  ? 4.670  36.240  52.905  1.00 54.45  ? 177 GLN A O   1 
ATOM   199  C CB  . GLN A 1 44  ? 1.846  34.935  53.881  1.00 56.99  ? 177 GLN A CB  1 
ATOM   200  C CG  . GLN A 1 44  ? 1.593  36.432  54.000  1.00 58.99  ? 177 GLN A CG  1 
ATOM   201  C CD  . GLN A 1 44  ? 1.252  37.075  52.666  1.00 60.88  ? 177 GLN A CD  1 
ATOM   202  O OE1 . GLN A 1 44  ? 0.351  36.622  51.954  1.00 61.10  ? 177 GLN A OE1 1 
ATOM   203  N NE2 . GLN A 1 44  ? 1.970  38.142  52.322  1.00 61.24  ? 177 GLN A NE2 1 
ATOM   204  N N   . LEU A 1 45  ? 4.983  34.423  54.199  1.00 54.74  ? 178 LEU A N   1 
ATOM   205  C CA  . LEU A 1 45  ? 6.276  34.865  54.707  1.00 54.31  ? 178 LEU A CA  1 
ATOM   206  C C   . LEU A 1 45  ? 7.385  34.730  53.671  1.00 53.49  ? 178 LEU A C   1 
ATOM   207  O O   . LEU A 1 45  ? 8.374  35.458  53.721  1.00 53.37  ? 178 LEU A O   1 
ATOM   208  C CB  . LEU A 1 45  ? 6.654  34.069  55.959  1.00 56.21  ? 178 LEU A CB  1 
ATOM   209  C CG  . LEU A 1 45  ? 5.919  34.425  57.253  1.00 58.19  ? 178 LEU A CG  1 
ATOM   210  C CD1 . LEU A 1 45  ? 6.272  33.420  58.336  1.00 59.50  ? 178 LEU A CD1 1 
ATOM   211  C CD2 . LEU A 1 45  ? 6.299  35.836  57.685  1.00 58.28  ? 178 LEU A CD2 1 
ATOM   212  N N   . SER A 1 46  ? 7.229  33.799  52.735  1.00 52.83  ? 179 SER A N   1 
ATOM   213  C CA  . SER A 1 46  ? 8.242  33.600  51.703  1.00 52.88  ? 179 SER A CA  1 
ATOM   214  C C   . SER A 1 46  ? 8.224  34.731  50.679  1.00 53.65  ? 179 SER A C   1 
ATOM   215  O O   . SER A 1 46  ? 9.117  34.832  49.837  1.00 53.44  ? 179 SER A O   1 
ATOM   216  C CB  . SER A 1 46  ? 8.031  32.254  50.999  1.00 52.21  ? 179 SER A CB  1 
ATOM   217  O OG  . SER A 1 46  ? 6.768  32.185  50.363  1.00 50.84  ? 179 SER A OG  1 
ATOM   218  N N   . LYS A 1 47  ? 7.207  35.585  50.762  1.00 54.71  ? 180 LYS A N   1 
ATOM   219  C CA  . LYS A 1 47  ? 7.072  36.705  49.840  1.00 55.52  ? 180 LYS A CA  1 
ATOM   220  C C   . LYS A 1 47  ? 7.862  37.922  50.300  1.00 56.31  ? 180 LYS A C   1 
ATOM   221  O O   . LYS A 1 47  ? 7.948  38.915  49.584  1.00 57.17  ? 180 LYS A O   1 
ATOM   222  C CB  . LYS A 1 47  ? 5.599  37.082  49.681  1.00 55.51  ? 180 LYS A CB  1 
ATOM   223  C CG  . LYS A 1 47  ? 4.731  35.948  49.166  1.00 56.50  ? 180 LYS A CG  1 
ATOM   224  C CD  . LYS A 1 47  ? 3.269  36.355  49.106  1.00 58.37  ? 180 LYS A CD  1 
ATOM   225  C CE  . LYS A 1 47  ? 2.395  35.206  48.630  1.00 59.54  ? 180 LYS A CE  1 
ATOM   226  N NZ  . LYS A 1 47  ? 0.950  35.577  48.619  1.00 61.31  ? 180 LYS A NZ  1 
ATOM   227  N N   . LYS A 1 48  ? 8.444  37.844  51.493  1.00 56.55  ? 181 LYS A N   1 
ATOM   228  C CA  . LYS A 1 48  ? 9.225  38.954  52.026  1.00 56.79  ? 181 LYS A CA  1 
ATOM   229  C C   . LYS A 1 48  ? 10.692 38.571  52.221  1.00 57.53  ? 181 LYS A C   1 
ATOM   230  O O   . LYS A 1 48  ? 11.005 37.542  52.817  1.00 57.10  ? 181 LYS A O   1 
ATOM   231  C CB  . LYS A 1 48  ? 8.623  39.429  53.346  1.00 56.37  ? 181 LYS A CB  1 
ATOM   232  N N   . GLU A 1 49  ? 11.579 39.421  51.712  1.00 58.68  ? 182 GLU A N   1 
ATOM   233  C CA  . GLU A 1 49  ? 13.027 39.230  51.791  1.00 59.94  ? 182 GLU A CA  1 
ATOM   234  C C   . GLU A 1 49  ? 13.501 38.563  53.089  1.00 59.40  ? 182 GLU A C   1 
ATOM   235  O O   . GLU A 1 49  ? 13.982 37.426  53.080  1.00 59.07  ? 182 GLU A O   1 
ATOM   236  C CB  . GLU A 1 49  ? 13.720 40.589  51.633  1.00 61.86  ? 182 GLU A CB  1 
ATOM   237  C CG  . GLU A 1 49  ? 15.235 40.538  51.506  1.00 65.30  ? 182 GLU A CG  1 
ATOM   238  C CD  . GLU A 1 49  ? 15.696 40.006  50.161  1.00 67.76  ? 182 GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 49  ? 16.910 40.079  49.879  1.00 68.45  ? 182 GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 49  ? 14.847 39.514  49.386  1.00 69.18  ? 182 GLU A OE2 1 
ATOM   241  N N   . ALA A 1 50  ? 13.366 39.283  54.198  1.00 57.73  ? 183 ALA A N   1 
ATOM   242  C CA  . ALA A 1 50  ? 13.786 38.793  55.506  1.00 56.30  ? 183 ALA A CA  1 
ATOM   243  C C   . ALA A 1 50  ? 13.249 37.405  55.857  1.00 55.28  ? 183 ALA A C   1 
ATOM   244  O O   . ALA A 1 50  ? 14.016 36.451  55.974  1.00 54.65  ? 183 ALA A O   1 
ATOM   245  C CB  . ALA A 1 50  ? 13.379 39.793  56.582  1.00 56.54  ? 183 ALA A CB  1 
ATOM   246  N N   . SER A 1 51  ? 11.936 37.296  56.033  1.00 53.44  ? 184 SER A N   1 
ATOM   247  C CA  . SER A 1 51  ? 11.328 36.018  56.388  1.00 53.34  ? 184 SER A CA  1 
ATOM   248  C C   . SER A 1 51  ? 11.680 34.896  55.415  1.00 52.90  ? 184 SER A C   1 
ATOM   249  O O   . SER A 1 51  ? 11.805 33.737  55.816  1.00 52.13  ? 184 SER A O   1 
ATOM   250  C CB  . SER A 1 51  ? 9.805  36.165  56.494  1.00 52.30  ? 184 SER A CB  1 
ATOM   251  O OG  . SER A 1 51  ? 9.274  36.862  55.383  1.00 53.50  ? 184 SER A OG  1 
ATOM   252  N N   . ARG A 1 52  ? 11.846 35.242  54.142  1.00 52.07  ? 185 ARG A N   1 
ATOM   253  C CA  . ARG A 1 52  ? 12.191 34.258  53.122  1.00 51.35  ? 185 ARG A CA  1 
ATOM   254  C C   . ARG A 1 52  ? 13.536 33.621  53.448  1.00 50.55  ? 185 ARG A C   1 
ATOM   255  O O   . ARG A 1 52  ? 13.676 32.395  53.428  1.00 49.42  ? 185 ARG A O   1 
ATOM   256  C CB  . ARG A 1 52  ? 12.268 34.928  51.750  1.00 52.20  ? 185 ARG A CB  1 
ATOM   257  C CG  . ARG A 1 52  ? 12.518 33.980  50.585  1.00 53.47  ? 185 ARG A CG  1 
ATOM   258  C CD  . ARG A 1 52  ? 12.763 34.784  49.315  1.00 55.93  ? 185 ARG A CD  1 
ATOM   259  N NE  . ARG A 1 52  ? 11.720 35.788  49.129  1.00 57.17  ? 185 ARG A NE  1 
ATOM   260  C CZ  . ARG A 1 52  ? 11.907 36.968  48.548  1.00 56.81  ? 185 ARG A CZ  1 
ATOM   261  N NH1 . ARG A 1 52  ? 13.104 37.307  48.087  1.00 56.45  ? 185 ARG A NH1 1 
ATOM   262  N NH2 . ARG A 1 52  ? 10.897 37.817  48.445  1.00 58.29  ? 185 ARG A NH2 1 
ATOM   263  N N   . HIS A 1 53  ? 14.523 34.460  53.744  1.00 49.46  ? 186 HIS A N   1 
ATOM   264  C CA  . HIS A 1 53  ? 15.856 33.979  54.072  1.00 50.71  ? 186 HIS A CA  1 
ATOM   265  C C   . HIS A 1 53  ? 15.848 33.155  55.353  1.00 50.13  ? 186 HIS A C   1 
ATOM   266  O O   . HIS A 1 53  ? 16.657 32.240  55.516  1.00 49.70  ? 186 HIS A O   1 
ATOM   267  C CB  . HIS A 1 53  ? 16.823 35.156  54.209  1.00 53.25  ? 186 HIS A CB  1 
ATOM   268  C CG  . HIS A 1 53  ? 17.106 35.854  52.915  1.00 56.95  ? 186 HIS A CG  1 
ATOM   269  N ND1 . HIS A 1 53  ? 17.975 36.918  52.818  1.00 58.57  ? 186 HIS A ND1 1 
ATOM   270  C CD2 . HIS A 1 53  ? 16.641 35.632  51.663  1.00 58.11  ? 186 HIS A CD2 1 
ATOM   271  C CE1 . HIS A 1 53  ? 18.035 37.322  51.561  1.00 58.82  ? 186 HIS A CE1 1 
ATOM   272  N NE2 . HIS A 1 53  ? 17.235 36.559  50.840  1.00 58.60  ? 186 HIS A NE2 1 
ATOM   273  N N   . ALA A 1 54  ? 14.931 33.480  56.258  1.00 48.38  ? 187 ALA A N   1 
ATOM   274  C CA  . ALA A 1 54  ? 14.818 32.754  57.517  1.00 47.07  ? 187 ALA A CA  1 
ATOM   275  C C   . ALA A 1 54  ? 14.305 31.349  57.227  1.00 45.95  ? 187 ALA A C   1 
ATOM   276  O O   . ALA A 1 54  ? 14.724 30.376  57.860  1.00 44.82  ? 187 ALA A O   1 
ATOM   277  C CB  . ALA A 1 54  ? 13.862 33.479  58.461  1.00 46.89  ? 187 ALA A CB  1 
ATOM   278  N N   . ILE A 1 55  ? 13.400 31.247  56.260  1.00 43.60  ? 188 ILE A N   1 
ATOM   279  C CA  . ILE A 1 55  ? 12.838 29.957  55.886  1.00 42.24  ? 188 ILE A CA  1 
ATOM   280  C C   . ILE A 1 55  ? 13.887 29.048  55.245  1.00 41.72  ? 188 ILE A C   1 
ATOM   281  O O   . ILE A 1 55  ? 14.050 27.896  55.647  1.00 40.08  ? 188 ILE A O   1 
ATOM   282  C CB  . ILE A 1 55  ? 11.656 30.124  54.902  1.00 40.64  ? 188 ILE A CB  1 
ATOM   283  C CG1 . ILE A 1 55  ? 10.477 30.792  55.614  1.00 42.18  ? 188 ILE A CG1 1 
ATOM   284  C CG2 . ILE A 1 55  ? 11.238 28.766  54.346  1.00 40.78  ? 188 ILE A CG2 1 
ATOM   285  C CD1 . ILE A 1 55  ? 9.306  31.120  54.703  1.00 40.30  ? 188 ILE A CD1 1 
ATOM   286  N N   . MET A 1 56  ? 14.604 29.573  54.258  1.00 41.42  ? 189 MET A N   1 
ATOM   287  C CA  . MET A 1 56  ? 15.606 28.785  53.558  1.00 43.07  ? 189 MET A CA  1 
ATOM   288  C C   . MET A 1 56  ? 16.799 28.368  54.408  1.00 43.15  ? 189 MET A C   1 
ATOM   289  O O   . MET A 1 56  ? 17.552 27.476  54.020  1.00 41.98  ? 189 MET A O   1 
ATOM   290  C CB  . MET A 1 56  ? 16.095 29.531  52.315  1.00 43.80  ? 189 MET A CB  1 
ATOM   291  C CG  . MET A 1 56  ? 16.640 30.918  52.569  1.00 45.94  ? 189 MET A CG  1 
ATOM   292  S SD  . MET A 1 56  ? 17.159 31.698  51.018  1.00 51.17  ? 189 MET A SD  1 
ATOM   293  C CE  . MET A 1 56  ? 15.644 31.602  50.095  1.00 46.71  ? 189 MET A CE  1 
ATOM   294  N N   . ARG A 1 57  ? 16.976 29.004  55.561  1.00 43.14  ? 190 ARG A N   1 
ATOM   295  C CA  . ARG A 1 57  ? 18.093 28.658  56.433  1.00 44.34  ? 190 ARG A CA  1 
ATOM   296  C C   . ARG A 1 57  ? 17.711 27.637  57.496  1.00 42.37  ? 190 ARG A C   1 
ATOM   297  O O   . ARG A 1 57  ? 18.526 27.272  58.339  1.00 43.60  ? 190 ARG A O   1 
ATOM   298  C CB  . ARG A 1 57  ? 18.670 29.923  57.074  1.00 46.23  ? 190 ARG A CB  1 
ATOM   299  C CG  . ARG A 1 57  ? 19.430 30.769  56.068  1.00 49.91  ? 190 ARG A CG  1 
ATOM   300  C CD  . ARG A 1 57  ? 19.755 32.152  56.587  1.00 52.67  ? 190 ARG A CD  1 
ATOM   301  N NE  . ARG A 1 57  ? 20.317 32.978  55.521  1.00 56.25  ? 190 ARG A NE  1 
ATOM   302  C CZ  . ARG A 1 57  ? 20.427 34.300  55.577  1.00 56.98  ? 190 ARG A CZ  1 
ATOM   303  N NH1 . ARG A 1 57  ? 20.015 34.959  56.651  1.00 57.17  ? 190 ARG A NH1 1 
ATOM   304  N NH2 . ARG A 1 57  ? 20.940 34.965  54.550  1.00 59.01  ? 190 ARG A NH2 1 
ATOM   305  N N   . SER A 1 58  ? 16.469 27.169  57.441  1.00 40.39  ? 191 SER A N   1 
ATOM   306  C CA  . SER A 1 58  ? 15.980 26.173  58.385  1.00 38.16  ? 191 SER A CA  1 
ATOM   307  C C   . SER A 1 58  ? 15.686 24.859  57.660  1.00 36.79  ? 191 SER A C   1 
ATOM   308  O O   . SER A 1 58  ? 14.648 24.714  57.014  1.00 34.88  ? 191 SER A O   1 
ATOM   309  C CB  . SER A 1 58  ? 14.712 26.676  59.075  1.00 38.13  ? 191 SER A CB  1 
ATOM   310  O OG  . SER A 1 58  ? 14.127 25.648  59.854  1.00 39.82  ? 191 SER A OG  1 
ATOM   311  N N   . PRO A 1 59  ? 16.606 23.886  57.755  1.00 35.76  ? 192 PRO A N   1 
ATOM   312  C CA  . PRO A 1 59  ? 16.434 22.585  57.103  1.00 35.03  ? 192 PRO A CA  1 
ATOM   313  C C   . PRO A 1 59  ? 15.115 21.930  57.487  1.00 34.64  ? 192 PRO A C   1 
ATOM   314  O O   . PRO A 1 59  ? 14.441 21.330  56.650  1.00 35.68  ? 192 PRO A O   1 
ATOM   315  C CB  . PRO A 1 59  ? 17.636 21.786  57.603  1.00 35.05  ? 192 PRO A CB  1 
ATOM   316  C CG  . PRO A 1 59  ? 18.680 22.844  57.790  1.00 35.55  ? 192 PRO A CG  1 
ATOM   317  C CD  . PRO A 1 59  ? 17.901 23.955  58.454  1.00 34.98  ? 192 PRO A CD  1 
ATOM   318  N N   . GLN A 1 60  ? 14.753 22.052  58.760  1.00 33.96  ? 193 GLN A N   1 
ATOM   319  C CA  . GLN A 1 60  ? 13.517 21.470  59.267  1.00 33.88  ? 193 GLN A CA  1 
ATOM   320  C C   . GLN A 1 60  ? 12.289 22.101  58.611  1.00 34.14  ? 193 GLN A C   1 
ATOM   321  O O   . GLN A 1 60  ? 11.332 21.402  58.266  1.00 32.15  ? 193 GLN A O   1 
ATOM   322  C CB  . GLN A 1 60  ? 13.439 21.632  60.791  1.00 36.10  ? 193 GLN A CB  1 
ATOM   323  C CG  . GLN A 1 60  ? 14.496 20.841  61.569  1.00 37.18  ? 193 GLN A CG  1 
ATOM   324  C CD  . GLN A 1 60  ? 15.851 21.533  61.631  1.00 38.54  ? 193 GLN A CD  1 
ATOM   325  O OE1 . GLN A 1 60  ? 16.054 22.591  61.035  1.00 37.78  ? 193 GLN A OE1 1 
ATOM   326  N NE2 . GLN A 1 60  ? 16.788 20.931  62.360  1.00 38.35  ? 193 GLN A NE2 1 
ATOM   327  N N   . MET A 1 61  ? 12.316 23.421  58.446  1.00 33.83  ? 194 MET A N   1 
ATOM   328  C CA  . MET A 1 61  ? 11.205 24.130  57.811  1.00 35.25  ? 194 MET A CA  1 
ATOM   329  C C   . MET A 1 61  ? 11.048 23.655  56.363  1.00 34.05  ? 194 MET A C   1 
ATOM   330  O O   . MET A 1 61  ? 9.971  23.215  55.954  1.00 32.89  ? 194 MET A O   1 
ATOM   331  C CB  . MET A 1 61  ? 11.453 25.640  57.835  1.00 37.90  ? 194 MET A CB  1 
ATOM   332  C CG  . MET A 1 61  ? 10.402 26.472  57.098  1.00 40.85  ? 194 MET A CG  1 
ATOM   333  S SD  . MET A 1 61  ? 8.783  26.504  57.900  1.00 47.24  ? 194 MET A SD  1 
ATOM   334  C CE  . MET A 1 61  ? 8.077  25.032  57.278  1.00 39.06  ? 194 MET A CE  1 
ATOM   335  N N   . VAL A 1 62  ? 12.130 23.733  55.595  1.00 32.50  ? 195 VAL A N   1 
ATOM   336  C CA  . VAL A 1 62  ? 12.091 23.309  54.198  1.00 31.26  ? 195 VAL A CA  1 
ATOM   337  C C   . VAL A 1 62  ? 11.633 21.857  54.047  1.00 32.75  ? 195 VAL A C   1 
ATOM   338  O O   . VAL A 1 62  ? 10.883 21.535  53.124  1.00 32.95  ? 195 VAL A O   1 
ATOM   339  C CB  . VAL A 1 62  ? 13.470 23.475  53.525  1.00 31.61  ? 195 VAL A CB  1 
ATOM   340  C CG1 . VAL A 1 62  ? 13.406 22.994  52.077  1.00 30.21  ? 195 VAL A CG1 1 
ATOM   341  C CG2 . VAL A 1 62  ? 13.907 24.934  53.590  1.00 27.60  ? 195 VAL A CG2 1 
ATOM   342  N N   . SER A 1 63  ? 12.078 20.983  54.947  1.00 33.31  ? 196 SER A N   1 
ATOM   343  C CA  . SER A 1 63  ? 11.690 19.576  54.880  1.00 34.33  ? 196 SER A CA  1 
ATOM   344  C C   . SER A 1 63  ? 10.196 19.428  55.126  1.00 35.01  ? 196 SER A C   1 
ATOM   345  O O   . SER A 1 63  ? 9.526  18.622  54.478  1.00 35.46  ? 196 SER A O   1 
ATOM   346  C CB  . SER A 1 63  ? 12.466 18.750  55.909  1.00 34.90  ? 196 SER A CB  1 
ATOM   347  O OG  . SER A 1 63  ? 13.853 18.764  55.623  1.00 36.97  ? 196 SER A OG  1 
ATOM   348  N N   . ALA A 1 64  ? 9.677  20.209  56.064  1.00 34.66  ? 197 ALA A N   1 
ATOM   349  C CA  . ALA A 1 64  ? 8.257  20.162  56.382  1.00 36.20  ? 197 ALA A CA  1 
ATOM   350  C C   . ALA A 1 64  ? 7.442  20.596  55.162  1.00 37.32  ? 197 ALA A C   1 
ATOM   351  O O   . ALA A 1 64  ? 6.464  19.943  54.794  1.00 37.46  ? 197 ALA A O   1 
ATOM   352  C CB  . ALA A 1 64  ? 7.958  21.071  57.570  1.00 35.86  ? 197 ALA A CB  1 
ATOM   353  N N   . ILE A 1 65  ? 7.847  21.701  54.541  1.00 37.75  ? 198 ILE A N   1 
ATOM   354  C CA  . ILE A 1 65  ? 7.159  22.210  53.360  1.00 37.31  ? 198 ILE A CA  1 
ATOM   355  C C   . ILE A 1 65  ? 7.145  21.139  52.270  1.00 38.13  ? 198 ILE A C   1 
ATOM   356  O O   . ILE A 1 65  ? 6.111  20.886  51.642  1.00 39.23  ? 198 ILE A O   1 
ATOM   357  C CB  . ILE A 1 65  ? 7.849  23.478  52.822  1.00 36.94  ? 198 ILE A CB  1 
ATOM   358  C CG1 . ILE A 1 65  ? 7.865  24.551  53.911  1.00 36.24  ? 198 ILE A CG1 1 
ATOM   359  C CG2 . ILE A 1 65  ? 7.117  23.985  51.585  1.00 37.18  ? 198 ILE A CG2 1 
ATOM   360  C CD1 . ILE A 1 65  ? 8.731  25.750  53.596  1.00 34.83  ? 198 ILE A CD1 1 
ATOM   361  N N   . VAL A 1 66  ? 8.295  20.507  52.057  1.00 37.30  ? 199 VAL A N   1 
ATOM   362  C CA  . VAL A 1 66  ? 8.418  19.455  51.054  1.00 39.29  ? 199 VAL A CA  1 
ATOM   363  C C   . VAL A 1 66  ? 7.484  18.283  51.363  1.00 41.43  ? 199 VAL A C   1 
ATOM   364  O O   . VAL A 1 66  ? 6.899  17.691  50.453  1.00 41.40  ? 199 VAL A O   1 
ATOM   365  C CB  . VAL A 1 66  ? 9.873  18.934  50.966  1.00 37.65  ? 199 VAL A CB  1 
ATOM   366  C CG1 . VAL A 1 66  ? 9.956  17.754  50.008  1.00 37.56  ? 199 VAL A CG1 1 
ATOM   367  C CG2 . VAL A 1 66  ? 10.791 20.049  50.494  1.00 38.07  ? 199 VAL A CG2 1 
ATOM   368  N N   . ARG A 1 67  ? 7.341  17.947  52.642  1.00 43.42  ? 200 ARG A N   1 
ATOM   369  C CA  . ARG A 1 67  ? 6.460  16.847  53.025  1.00 46.21  ? 200 ARG A CA  1 
ATOM   370  C C   . ARG A 1 67  ? 5.001  17.260  52.877  1.00 45.83  ? 200 ARG A C   1 
ATOM   371  O O   . ARG A 1 67  ? 4.207  16.549  52.269  1.00 46.77  ? 200 ARG A O   1 
ATOM   372  C CB  . ARG A 1 67  ? 6.706  16.417  54.473  1.00 48.00  ? 200 ARG A CB  1 
ATOM   373  C CG  . ARG A 1 67  ? 8.121  15.979  54.773  1.00 52.16  ? 200 ARG A CG  1 
ATOM   374  C CD  . ARG A 1 67  ? 8.159  15.080  56.004  1.00 55.06  ? 200 ARG A CD  1 
ATOM   375  N NE  . ARG A 1 67  ? 9.476  15.077  56.632  1.00 56.46  ? 200 ARG A NE  1 
ATOM   376  C CZ  . ARG A 1 67  ? 9.939  16.065  57.392  1.00 56.79  ? 200 ARG A CZ  1 
ATOM   377  N NH1 . ARG A 1 67  ? 9.188  17.135  57.621  1.00 56.84  ? 200 ARG A NH1 1 
ATOM   378  N NH2 . ARG A 1 67  ? 11.153 15.984  57.920  1.00 57.68  ? 200 ARG A NH2 1 
ATOM   379  N N   . THR A 1 68  ? 4.656  18.412  53.440  1.00 46.60  ? 201 THR A N   1 
ATOM   380  C CA  . THR A 1 68  ? 3.291  18.918  53.375  1.00 48.67  ? 201 THR A CA  1 
ATOM   381  C C   . THR A 1 68  ? 2.791  18.993  51.936  1.00 50.67  ? 201 THR A C   1 
ATOM   382  O O   . THR A 1 68  ? 1.639  18.669  51.654  1.00 50.54  ? 201 THR A O   1 
ATOM   383  C CB  . THR A 1 68  ? 3.183  20.327  53.998  1.00 48.94  ? 201 THR A CB  1 
ATOM   384  O OG1 . THR A 1 68  ? 3.551  20.275  55.382  1.00 48.39  ? 201 THR A OG1 1 
ATOM   385  C CG2 . THR A 1 68  ? 1.761  20.856  53.873  1.00 48.21  ? 201 THR A CG2 1 
ATOM   386  N N   . MET A 1 69  ? 3.666  19.415  51.028  1.00 52.31  ? 202 MET A N   1 
ATOM   387  C CA  . MET A 1 69  ? 3.299  19.548  49.624  1.00 52.90  ? 202 MET A CA  1 
ATOM   388  C C   . MET A 1 69  ? 2.948  18.226  48.954  1.00 54.75  ? 202 MET A C   1 
ATOM   389  O O   . MET A 1 69  ? 1.895  18.107  48.328  1.00 55.94  ? 202 MET A O   1 
ATOM   390  C CB  . MET A 1 69  ? 4.428  20.228  48.842  1.00 50.71  ? 202 MET A CB  1 
ATOM   391  C CG  . MET A 1 69  ? 4.124  20.427  47.358  1.00 47.87  ? 202 MET A CG  1 
ATOM   392  S SD  . MET A 1 69  ? 5.477  21.212  46.443  1.00 42.94  ? 202 MET A SD  1 
ATOM   393  C CE  . MET A 1 69  ? 6.609  19.818  46.266  1.00 37.34  ? 202 MET A CE  1 
ATOM   394  N N   . GLN A 1 70  ? 3.818  17.231  49.084  1.00 56.28  ? 203 GLN A N   1 
ATOM   395  C CA  . GLN A 1 70  ? 3.572  15.945  48.445  1.00 59.07  ? 203 GLN A CA  1 
ATOM   396  C C   . GLN A 1 70  ? 2.675  14.996  49.235  1.00 61.23  ? 203 GLN A C   1 
ATOM   397  O O   . GLN A 1 70  ? 2.633  13.800  48.948  1.00 61.90  ? 203 GLN A O   1 
ATOM   398  C CB  . GLN A 1 70  ? 4.896  15.248  48.136  1.00 59.42  ? 203 GLN A CB  1 
ATOM   399  C CG  . GLN A 1 70  ? 5.616  14.711  49.352  1.00 60.65  ? 203 GLN A CG  1 
ATOM   400  C CD  . GLN A 1 70  ? 6.883  13.975  48.983  1.00 62.07  ? 203 GLN A CD  1 
ATOM   401  O OE1 . GLN A 1 70  ? 6.862  13.040  48.180  1.00 61.95  ? 203 GLN A OE1 1 
ATOM   402  N NE2 . GLN A 1 70  ? 8.000  14.392  49.568  1.00 63.62  ? 203 GLN A NE2 1 
ATOM   403  N N   . ASN A 1 71  ? 1.958  15.522  50.223  1.00 63.34  ? 204 ASN A N   1 
ATOM   404  C CA  . ASN A 1 71  ? 1.063  14.693  51.025  1.00 64.98  ? 204 ASN A CA  1 
ATOM   405  C C   . ASN A 1 71  ? -0.341 15.276  51.091  1.00 65.58  ? 204 ASN A C   1 
ATOM   406  O O   . ASN A 1 71  ? -1.326 14.544  51.026  1.00 65.92  ? 204 ASN A O   1 
ATOM   407  C CB  . ASN A 1 71  ? 1.607  14.523  52.448  1.00 64.93  ? 204 ASN A CB  1 
ATOM   408  C CG  . ASN A 1 71  ? 2.890  13.718  52.489  1.00 66.21  ? 204 ASN A CG  1 
ATOM   409  O OD1 . ASN A 1 71  ? 2.992  12.661  51.865  1.00 65.67  ? 204 ASN A OD1 1 
ATOM   410  N ND2 . ASN A 1 71  ? 3.875  14.207  53.236  1.00 66.94  ? 204 ASN A ND2 1 
ATOM   411  N N   . THR A 1 72  ? -0.424 16.597  51.213  1.00 66.60  ? 205 THR A N   1 
ATOM   412  C CA  . THR A 1 72  ? -1.707 17.285  51.301  1.00 68.13  ? 205 THR A CA  1 
ATOM   413  C C   . THR A 1 72  ? -2.632 16.941  50.139  1.00 69.59  ? 205 THR A C   1 
ATOM   414  O O   . THR A 1 72  ? -2.183 16.542  49.065  1.00 69.76  ? 205 THR A O   1 
ATOM   415  C CB  . THR A 1 72  ? -1.515 18.818  51.342  1.00 68.54  ? 205 THR A CB  1 
ATOM   416  O OG1 . THR A 1 72  ? -2.783 19.457  51.539  1.00 68.65  ? 205 THR A OG1 1 
ATOM   417  C CG2 . THR A 1 72  ? -0.899 19.316  50.041  1.00 68.41  ? 205 THR A CG2 1 
ATOM   418  N N   . ASN A 1 73  ? -3.931 17.090  50.373  1.00 71.07  ? 206 ASN A N   1 
ATOM   419  C CA  . ASN A 1 73  ? -4.937 16.814  49.356  1.00 72.65  ? 206 ASN A CA  1 
ATOM   420  C C   . ASN A 1 73  ? -5.803 18.053  49.202  1.00 73.10  ? 206 ASN A C   1 
ATOM   421  O O   . ASN A 1 73  ? -6.793 18.053  48.471  1.00 73.83  ? 206 ASN A O   1 
ATOM   422  C CB  . ASN A 1 73  ? -5.803 15.621  49.764  1.00 73.70  ? 206 ASN A CB  1 
ATOM   423  C CG  . ASN A 1 73  ? -5.006 14.337  49.887  1.00 75.24  ? 206 ASN A CG  1 
ATOM   424  O OD1 . ASN A 1 73  ? -4.341 13.912  48.941  1.00 75.88  ? 206 ASN A OD1 1 
ATOM   425  N ND2 . ASN A 1 73  ? -5.071 13.709  51.057  1.00 75.57  ? 206 ASN A ND2 1 
ATOM   426  N N   . ASP A 1 74  ? -5.418 19.110  49.909  1.00 73.10  ? 207 ASP A N   1 
ATOM   427  C CA  . ASP A 1 74  ? -6.138 20.372  49.857  1.00 73.43  ? 207 ASP A CA  1 
ATOM   428  C C   . ASP A 1 74  ? -5.458 21.292  48.847  1.00 72.84  ? 207 ASP A C   1 
ATOM   429  O O   . ASP A 1 74  ? -4.361 21.796  49.092  1.00 72.90  ? 207 ASP A O   1 
ATOM   430  C CB  . ASP A 1 74  ? -6.143 21.024  51.237  1.00 74.72  ? 207 ASP A CB  1 
ATOM   431  C CG  . ASP A 1 74  ? -6.938 22.309  51.267  1.00 76.95  ? 207 ASP A CG  1 
ATOM   432  O OD1 . ASP A 1 74  ? -6.618 23.225  50.480  1.00 78.77  ? 207 ASP A OD1 1 
ATOM   433  O OD2 . ASP A 1 74  ? -7.882 22.404  52.080  1.00 78.44  ? 207 ASP A OD2 1 
ATOM   434  N N   . VAL A 1 75  ? -6.121 21.501  47.714  1.00 71.31  ? 208 VAL A N   1 
ATOM   435  C CA  . VAL A 1 75  ? -5.599 22.343  46.642  1.00 69.52  ? 208 VAL A CA  1 
ATOM   436  C C   . VAL A 1 75  ? -4.812 23.560  47.124  1.00 68.51  ? 208 VAL A C   1 
ATOM   437  O O   . VAL A 1 75  ? -3.685 23.787  46.682  1.00 68.79  ? 208 VAL A O   1 
ATOM   438  C CB  . VAL A 1 75  ? -6.743 22.831  45.712  1.00 69.27  ? 208 VAL A CB  1 
ATOM   439  C CG1 . VAL A 1 75  ? -7.744 23.667  46.498  1.00 68.92  ? 208 VAL A CG1 1 
ATOM   440  C CG2 . VAL A 1 75  ? -6.170 23.637  44.556  1.00 68.52  ? 208 VAL A CG2 1 
ATOM   441  N N   . GLU A 1 76  ? -5.399 24.336  48.030  1.00 67.02  ? 209 GLU A N   1 
ATOM   442  C CA  . GLU A 1 76  ? -4.748 25.538  48.538  1.00 65.99  ? 209 GLU A CA  1 
ATOM   443  C C   . GLU A 1 76  ? -3.453 25.259  49.300  1.00 64.98  ? 209 GLU A C   1 
ATOM   444  O O   . GLU A 1 76  ? -2.564 26.110  49.351  1.00 64.55  ? 209 GLU A O   1 
ATOM   445  C CB  . GLU A 1 76  ? -5.713 26.321  49.432  1.00 66.67  ? 209 GLU A CB  1 
ATOM   446  C CG  . GLU A 1 76  ? -5.153 27.640  49.959  1.00 68.61  ? 209 GLU A CG  1 
ATOM   447  C CD  . GLU A 1 76  ? -4.799 28.624  48.851  1.00 69.80  ? 209 GLU A CD  1 
ATOM   448  O OE1 . GLU A 1 76  ? -4.972 28.280  47.662  1.00 70.59  ? 209 GLU A OE1 1 
ATOM   449  O OE2 . GLU A 1 76  ? -4.347 29.746  49.171  1.00 69.99  ? 209 GLU A OE2 1 
ATOM   450  N N   . THR A 1 77  ? -3.348 24.073  49.892  1.00 63.41  ? 210 THR A N   1 
ATOM   451  C CA  . THR A 1 77  ? -2.153 23.707  50.645  1.00 62.41  ? 210 THR A CA  1 
ATOM   452  C C   . THR A 1 77  ? -1.014 23.348  49.699  1.00 60.48  ? 210 THR A C   1 
ATOM   453  O O   . THR A 1 77  ? 0.117  23.807  49.871  1.00 60.05  ? 210 THR A O   1 
ATOM   454  C CB  . THR A 1 77  ? -2.424 22.511  51.582  1.00 63.58  ? 210 THR A CB  1 
ATOM   455  O OG1 . THR A 1 77  ? -3.414 22.878  52.550  1.00 63.53  ? 210 THR A OG1 1 
ATOM   456  C CG2 . THR A 1 77  ? -1.147 22.098  52.307  1.00 63.70  ? 210 THR A CG2 1 
ATOM   457  N N   . ALA A 1 78  ? -1.317 22.523  48.703  1.00 58.29  ? 211 ALA A N   1 
ATOM   458  C CA  . ALA A 1 78  ? -0.319 22.114  47.724  1.00 55.85  ? 211 ALA A CA  1 
ATOM   459  C C   . ALA A 1 78  ? 0.172  23.353  46.983  1.00 54.47  ? 211 ALA A C   1 
ATOM   460  O O   . ALA A 1 78  ? 1.352  23.463  46.646  1.00 53.25  ? 211 ALA A O   1 
ATOM   461  C CB  . ALA A 1 78  ? -0.928 21.120  46.741  1.00 55.12  ? 211 ALA A CB  1 
ATOM   462  N N   . ARG A 1 79  ? -0.745 24.286  46.746  1.00 52.48  ? 212 ARG A N   1 
ATOM   463  C CA  . ARG A 1 79  ? -0.428 25.522  46.045  1.00 51.79  ? 212 ARG A CA  1 
ATOM   464  C C   . ARG A 1 79  ? 0.467  26.454  46.858  1.00 50.77  ? 212 ARG A C   1 
ATOM   465  O O   . ARG A 1 79  ? 1.361  27.096  46.307  1.00 48.95  ? 212 ARG A O   1 
ATOM   466  C CB  . ARG A 1 79  ? -1.717 26.258  45.661  1.00 53.29  ? 212 ARG A CB  1 
ATOM   467  C CG  . ARG A 1 79  ? -1.485 27.697  45.229  1.00 54.98  ? 212 ARG A CG  1 
ATOM   468  C CD  . ARG A 1 79  ? -2.785 28.444  45.002  1.00 58.92  ? 212 ARG A CD  1 
ATOM   469  N NE  . ARG A 1 79  ? -2.588 29.885  45.135  1.00 61.20  ? 212 ARG A NE  1 
ATOM   470  C CZ  . ARG A 1 79  ? -2.276 30.487  46.279  1.00 63.10  ? 212 ARG A CZ  1 
ATOM   471  N NH1 . ARG A 1 79  ? -2.131 29.771  47.387  1.00 65.16  ? 212 ARG A NH1 1 
ATOM   472  N NH2 . ARG A 1 79  ? -2.099 31.800  46.319  1.00 64.55  ? 212 ARG A NH2 1 
ATOM   473  N N   . CYS A 1 80  ? 0.222  26.539  48.162  1.00 49.45  ? 213 CYS A N   1 
ATOM   474  C CA  . CYS A 1 80  ? 1.025  27.404  49.021  1.00 48.87  ? 213 CYS A CA  1 
ATOM   475  C C   . CYS A 1 80  ? 2.409  26.817  49.282  1.00 45.88  ? 213 CYS A C   1 
ATOM   476  O O   . CYS A 1 80  ? 3.383  27.552  49.427  1.00 45.93  ? 213 CYS A O   1 
ATOM   477  C CB  . CYS A 1 80  ? 0.306  27.663  50.350  1.00 50.50  ? 213 CYS A CB  1 
ATOM   478  S SG  . CYS A 1 80  ? -1.096 28.808  50.227  1.00 56.17  ? 213 CYS A SG  1 
ATOM   479  N N   . THR A 1 81  ? 2.497  25.493  49.342  1.00 43.80  ? 214 THR A N   1 
ATOM   480  C CA  . THR A 1 81  ? 3.781  24.843  49.574  1.00 42.29  ? 214 THR A CA  1 
ATOM   481  C C   . THR A 1 81  ? 4.634  24.890  48.306  1.00 40.85  ? 214 THR A C   1 
ATOM   482  O O   . THR A 1 81  ? 5.814  25.237  48.358  1.00 41.36  ? 214 THR A O   1 
ATOM   483  C CB  . THR A 1 81  ? 3.597  23.381  50.031  1.00 40.63  ? 214 THR A CB  1 
ATOM   484  O OG1 . THR A 1 81  ? 2.724  22.696  49.127  1.00 42.35  ? 214 THR A OG1 1 
ATOM   485  C CG2 . THR A 1 81  ? 3.004  23.339  51.435  1.00 42.52  ? 214 THR A CG2 1 
ATOM   486  N N   . ALA A 1 82  ? 4.036  24.552  47.167  1.00 40.07  ? 215 ALA A N   1 
ATOM   487  C CA  . ALA A 1 82  ? 4.757  24.588  45.902  1.00 37.95  ? 215 ALA A CA  1 
ATOM   488  C C   . ALA A 1 82  ? 5.172  26.033  45.636  1.00 37.59  ? 215 ALA A C   1 
ATOM   489  O O   . ALA A 1 82  ? 6.271  26.300  45.153  1.00 36.23  ? 215 ALA A O   1 
ATOM   490  C CB  . ALA A 1 82  ? 3.871  24.079  44.778  1.00 37.90  ? 215 ALA A CB  1 
ATOM   491  N N   . GLY A 1 83  ? 4.283  26.964  45.969  1.00 37.64  ? 216 GLY A N   1 
ATOM   492  C CA  . GLY A 1 83  ? 4.568  28.372  45.769  1.00 37.14  ? 216 GLY A CA  1 
ATOM   493  C C   . GLY A 1 83  ? 5.709  28.854  46.641  1.00 36.77  ? 216 GLY A C   1 
ATOM   494  O O   . GLY A 1 83  ? 6.513  29.692  46.226  1.00 36.50  ? 216 GLY A O   1 
ATOM   495  N N   . THR A 1 84  ? 5.777  28.331  47.861  1.00 36.62  ? 217 THR A N   1 
ATOM   496  C CA  . THR A 1 84  ? 6.843  28.703  48.785  1.00 35.78  ? 217 THR A CA  1 
ATOM   497  C C   . THR A 1 84  ? 8.184  28.229  48.225  1.00 33.93  ? 217 THR A C   1 
ATOM   498  O O   . THR A 1 84  ? 9.159  28.985  48.191  1.00 34.07  ? 217 THR A O   1 
ATOM   499  C CB  . THR A 1 84  ? 6.622  28.073  50.178  1.00 37.66  ? 217 THR A CB  1 
ATOM   500  O OG1 . THR A 1 84  ? 5.407  28.580  50.747  1.00 38.58  ? 217 THR A OG1 1 
ATOM   501  C CG2 . THR A 1 84  ? 7.782  28.407  51.104  1.00 37.49  ? 217 THR A CG2 1 
ATOM   502  N N   . LEU A 1 85  ? 8.226  26.977  47.781  1.00 33.42  ? 218 LEU A N   1 
ATOM   503  C CA  . LEU A 1 85  ? 9.449  26.415  47.213  1.00 33.27  ? 218 LEU A CA  1 
ATOM   504  C C   . LEU A 1 85  ? 9.873  27.236  45.996  1.00 33.64  ? 218 LEU A C   1 
ATOM   505  O O   . LEU A 1 85  ? 11.062 27.505  45.791  1.00 32.20  ? 218 LEU A O   1 
ATOM   506  C CB  . LEU A 1 85  ? 9.224  24.953  46.821  1.00 32.45  ? 218 LEU A CB  1 
ATOM   507  C CG  . LEU A 1 85  ? 8.864  24.029  47.991  1.00 33.67  ? 218 LEU A CG  1 
ATOM   508  C CD1 . LEU A 1 85  ? 8.691  22.611  47.484  1.00 33.07  ? 218 LEU A CD1 1 
ATOM   509  C CD2 . LEU A 1 85  ? 9.959  24.083  49.061  1.00 32.00  ? 218 LEU A CD2 1 
ATOM   510  N N   . HIS A 1 86  ? 8.897  27.645  45.191  1.00 33.79  ? 219 HIS A N   1 
ATOM   511  C CA  . HIS A 1 86  ? 9.199  28.456  44.019  1.00 34.71  ? 219 HIS A CA  1 
ATOM   512  C C   . HIS A 1 86  ? 9.925  29.731  44.437  1.00 34.08  ? 219 HIS A C   1 
ATOM   513  O O   . HIS A 1 86  ? 10.941 30.094  43.846  1.00 32.92  ? 219 HIS A O   1 
ATOM   514  C CB  . HIS A 1 86  ? 7.917  28.820  43.267  1.00 36.04  ? 219 HIS A CB  1 
ATOM   515  C CG  . HIS A 1 86  ? 8.099  29.928  42.278  1.00 39.95  ? 219 HIS A CG  1 
ATOM   516  N ND1 . HIS A 1 86  ? 7.603  31.198  42.483  1.00 41.49  ? 219 HIS A ND1 1 
ATOM   517  C CD2 . HIS A 1 86  ? 8.769  29.971  41.102  1.00 41.22  ? 219 HIS A CD2 1 
ATOM   518  C CE1 . HIS A 1 86  ? 7.958  31.975  41.475  1.00 40.78  ? 219 HIS A CE1 1 
ATOM   519  N NE2 . HIS A 1 86  ? 8.667  31.256  40.624  1.00 42.39  ? 219 HIS A NE2 1 
ATOM   520  N N   . ASN A 1 87  ? 9.405  30.407  45.461  1.00 34.98  ? 220 ASN A N   1 
ATOM   521  C CA  . ASN A 1 87  ? 10.019 31.642  45.936  1.00 35.10  ? 220 ASN A CA  1 
ATOM   522  C C   . ASN A 1 87  ? 11.434 31.411  46.446  1.00 34.78  ? 220 ASN A C   1 
ATOM   523  O O   . ASN A 1 87  ? 12.331 32.210  46.185  1.00 35.65  ? 220 ASN A O   1 
ATOM   524  C CB  . ASN A 1 87  ? 9.173  32.285  47.044  1.00 37.22  ? 220 ASN A CB  1 
ATOM   525  C CG  . ASN A 1 87  ? 7.854  32.846  46.525  1.00 40.99  ? 220 ASN A CG  1 
ATOM   526  O OD1 . ASN A 1 87  ? 7.771  33.311  45.388  1.00 40.99  ? 220 ASN A OD1 1 
ATOM   527  N ND2 . ASN A 1 87  ? 6.823  32.819  47.364  1.00 42.11  ? 220 ASN A ND2 1 
ATOM   528  N N   . LEU A 1 88  ? 11.638 30.312  47.165  1.00 32.98  ? 221 LEU A N   1 
ATOM   529  C CA  . LEU A 1 88  ? 12.957 30.009  47.705  1.00 31.90  ? 221 LEU A CA  1 
ATOM   530  C C   . LEU A 1 88  ? 13.962 29.704  46.598  1.00 30.88  ? 221 LEU A C   1 
ATOM   531  O O   . LEU A 1 88  ? 15.149 29.997  46.737  1.00 29.29  ? 221 LEU A O   1 
ATOM   532  C CB  . LEU A 1 88  ? 12.882 28.816  48.664  1.00 30.90  ? 221 LEU A CB  1 
ATOM   533  C CG  . LEU A 1 88  ? 11.877 28.862  49.821  1.00 30.44  ? 221 LEU A CG  1 
ATOM   534  C CD1 . LEU A 1 88  ? 12.044 27.613  50.678  1.00 30.60  ? 221 LEU A CD1 1 
ATOM   535  C CD2 . LEU A 1 88  ? 12.093 30.116  50.659  1.00 30.53  ? 221 LEU A CD2 1 
ATOM   536  N N   . SER A 1 89  ? 13.480 29.128  45.498  1.00 30.09  ? 222 SER A N   1 
ATOM   537  C CA  . SER A 1 89  ? 14.343 28.752  44.375  1.00 28.78  ? 222 SER A CA  1 
ATOM   538  C C   . SER A 1 89  ? 15.008 29.927  43.661  1.00 29.70  ? 222 SER A C   1 
ATOM   539  O O   . SER A 1 89  ? 15.843 29.731  42.773  1.00 29.10  ? 222 SER A O   1 
ATOM   540  C CB  . SER A 1 89  ? 13.554 27.918  43.361  1.00 28.18  ? 222 SER A CB  1 
ATOM   541  O OG  . SER A 1 89  ? 12.606 28.706  42.659  1.00 27.19  ? 222 SER A OG  1 
ATOM   542  N N   . HIS A 1 90  ? 14.647 31.142  44.055  1.00 31.72  ? 223 HIS A N   1 
ATOM   543  C CA  . HIS A 1 90  ? 15.217 32.349  43.460  1.00 33.87  ? 223 HIS A CA  1 
ATOM   544  C C   . HIS A 1 90  ? 16.613 32.595  44.035  1.00 34.75  ? 223 HIS A C   1 
ATOM   545  O O   . HIS A 1 90  ? 17.421 33.328  43.457  1.00 33.27  ? 223 HIS A O   1 
ATOM   546  C CB  . HIS A 1 90  ? 14.311 33.547  43.769  1.00 37.80  ? 223 HIS A CB  1 
ATOM   547  C CG  . HIS A 1 90  ? 14.751 34.830  43.131  1.00 43.16  ? 223 HIS A CG  1 
ATOM   548  N ND1 . HIS A 1 90  ? 14.684 35.048  41.771  1.00 45.92  ? 223 HIS A ND1 1 
ATOM   549  C CD2 . HIS A 1 90  ? 15.244 35.972  43.670  1.00 45.54  ? 223 HIS A CD2 1 
ATOM   550  C CE1 . HIS A 1 90  ? 15.115 36.268  41.499  1.00 45.54  ? 223 HIS A CE1 1 
ATOM   551  N NE2 . HIS A 1 90  ? 15.460 36.850  42.634  1.00 44.97  ? 223 HIS A NE2 1 
ATOM   552  N N   . HIS A 1 91  ? 16.897 31.963  45.170  1.00 34.76  ? 224 HIS A N   1 
ATOM   553  C CA  . HIS A 1 91  ? 18.181 32.138  45.843  1.00 35.82  ? 224 HIS A CA  1 
ATOM   554  C C   . HIS A 1 91  ? 19.025 30.868  45.839  1.00 35.35  ? 224 HIS A C   1 
ATOM   555  O O   . HIS A 1 91  ? 18.497 29.755  45.789  1.00 32.30  ? 224 HIS A O   1 
ATOM   556  C CB  . HIS A 1 91  ? 17.939 32.583  47.287  1.00 38.55  ? 224 HIS A CB  1 
ATOM   557  C CG  . HIS A 1 91  ? 17.031 33.767  47.406  1.00 41.18  ? 224 HIS A CG  1 
ATOM   558  N ND1 . HIS A 1 91  ? 17.449 35.055  47.151  1.00 42.43  ? 224 HIS A ND1 1 
ATOM   559  C CD2 . HIS A 1 91  ? 15.716 33.853  47.722  1.00 41.78  ? 224 HIS A CD2 1 
ATOM   560  C CE1 . HIS A 1 91  ? 16.432 35.884  47.307  1.00 44.37  ? 224 HIS A CE1 1 
ATOM   561  N NE2 . HIS A 1 91  ? 15.368 35.180  47.653  1.00 42.53  ? 224 HIS A NE2 1 
ATOM   562  N N   . ARG A 1 92  ? 20.341 31.048  45.897  1.00 34.83  ? 225 ARG A N   1 
ATOM   563  C CA  . ARG A 1 92  ? 21.268 29.927  45.905  1.00 36.76  ? 225 ARG A CA  1 
ATOM   564  C C   . ARG A 1 92  ? 21.066 29.035  47.129  1.00 35.90  ? 225 ARG A C   1 
ATOM   565  O O   . ARG A 1 92  ? 21.048 27.813  47.010  1.00 35.16  ? 225 ARG A O   1 
ATOM   566  C CB  . ARG A 1 92  ? 22.710 30.438  45.854  1.00 39.49  ? 225 ARG A CB  1 
ATOM   567  C CG  . ARG A 1 92  ? 23.754 29.372  46.124  1.00 45.25  ? 225 ARG A CG  1 
ATOM   568  C CD  . ARG A 1 92  ? 25.062 29.688  45.419  1.00 49.99  ? 225 ARG A CD  1 
ATOM   569  N NE  . ARG A 1 92  ? 25.455 31.084  45.577  1.00 53.35  ? 225 ARG A NE  1 
ATOM   570  C CZ  . ARG A 1 92  ? 26.539 31.618  45.022  1.00 55.62  ? 225 ARG A CZ  1 
ATOM   571  N NH1 . ARG A 1 92  ? 27.340 30.869  44.275  1.00 56.99  ? 225 ARG A NH1 1 
ATOM   572  N NH2 . ARG A 1 92  ? 26.818 32.902  45.203  1.00 56.65  ? 225 ARG A NH2 1 
ATOM   573  N N   . GLU A 1 93  ? 20.910 29.647  48.299  1.00 34.87  ? 226 GLU A N   1 
ATOM   574  C CA  . GLU A 1 93  ? 20.695 28.887  49.525  1.00 35.78  ? 226 GLU A CA  1 
ATOM   575  C C   . GLU A 1 93  ? 19.356 28.162  49.472  1.00 32.98  ? 226 GLU A C   1 
ATOM   576  O O   . GLU A 1 93  ? 19.226 27.047  49.979  1.00 32.38  ? 226 GLU A O   1 
ATOM   577  C CB  . GLU A 1 93  ? 20.733 29.810  50.747  1.00 39.87  ? 226 GLU A CB  1 
ATOM   578  C CG  . GLU A 1 93  ? 22.118 30.365  51.064  1.00 46.91  ? 226 GLU A CG  1 
ATOM   579  C CD  . GLU A 1 93  ? 22.135 31.215  52.324  1.00 51.30  ? 226 GLU A CD  1 
ATOM   580  O OE1 . GLU A 1 93  ? 21.754 30.701  53.401  1.00 53.36  ? 226 GLU A OE1 1 
ATOM   581  O OE2 . GLU A 1 93  ? 22.530 32.399  52.237  1.00 54.16  ? 226 GLU A OE2 1 
ATOM   582  N N   . GLY A 1 94  ? 18.364 28.801  48.859  1.00 29.92  ? 227 GLY A N   1 
ATOM   583  C CA  . GLY A 1 94  ? 17.048 28.197  48.747  1.00 27.93  ? 227 GLY A CA  1 
ATOM   584  C C   . GLY A 1 94  ? 17.099 26.969  47.860  1.00 26.50  ? 227 GLY A C   1 
ATOM   585  O O   . GLY A 1 94  ? 16.507 25.938  48.178  1.00 28.43  ? 227 GLY A O   1 
ATOM   586  N N   . LEU A 1 95  ? 17.807 27.082  46.741  1.00 25.74  ? 228 LEU A N   1 
ATOM   587  C CA  . LEU A 1 95  ? 17.957 25.975  45.803  1.00 24.52  ? 228 LEU A CA  1 
ATOM   588  C C   . LEU A 1 95  ? 18.635 24.777  46.476  1.00 25.81  ? 228 LEU A C   1 
ATOM   589  O O   . LEU A 1 95  ? 18.202 23.635  46.310  1.00 22.28  ? 228 LEU A O   1 
ATOM   590  C CB  . LEU A 1 95  ? 18.785 26.423  44.591  1.00 24.80  ? 228 LEU A CB  1 
ATOM   591  C CG  . LEU A 1 95  ? 18.092 27.356  43.588  1.00 22.30  ? 228 LEU A CG  1 
ATOM   592  C CD1 . LEU A 1 95  ? 19.114 27.962  42.646  1.00 24.22  ? 228 LEU A CD1 1 
ATOM   593  C CD2 . LEU A 1 95  ? 17.047 26.578  42.807  1.00 21.63  ? 228 LEU A CD2 1 
ATOM   594  N N   . LEU A 1 96  ? 19.697 25.042  47.234  1.00 26.51  ? 229 LEU A N   1 
ATOM   595  C CA  . LEU A 1 96  ? 20.419 23.974  47.924  1.00 27.67  ? 229 LEU A CA  1 
ATOM   596  C C   . LEU A 1 96  ? 19.541 23.302  48.972  1.00 26.16  ? 229 LEU A C   1 
ATOM   597  O O   . LEU A 1 96  ? 19.484 22.078  49.055  1.00 27.34  ? 229 LEU A O   1 
ATOM   598  C CB  . LEU A 1 96  ? 21.681 24.525  48.591  1.00 29.44  ? 229 LEU A CB  1 
ATOM   599  C CG  . LEU A 1 96  ? 22.616 23.475  49.197  1.00 31.17  ? 229 LEU A CG  1 
ATOM   600  C CD1 . LEU A 1 96  ? 23.089 22.531  48.104  1.00 30.13  ? 229 LEU A CD1 1 
ATOM   601  C CD2 . LEU A 1 96  ? 23.809 24.162  49.862  1.00 32.29  ? 229 LEU A CD2 1 
ATOM   602  N N   . ALA A 1 97  ? 18.845 24.105  49.768  1.00 27.56  ? 230 ALA A N   1 
ATOM   603  C CA  . ALA A 1 97  ? 17.978 23.560  50.804  1.00 27.85  ? 230 ALA A CA  1 
ATOM   604  C C   . ALA A 1 97  ? 16.916 22.657  50.185  1.00 28.64  ? 230 ALA A C   1 
ATOM   605  O O   . ALA A 1 97  ? 16.657 21.557  50.684  1.00 28.61  ? 230 ALA A O   1 
ATOM   606  C CB  . ALA A 1 97  ? 17.323 24.688  51.591  1.00 27.45  ? 230 ALA A CB  1 
ATOM   607  N N   . ILE A 1 98  ? 16.295 23.120  49.103  1.00 26.80  ? 231 ILE A N   1 
ATOM   608  C CA  . ILE A 1 98  ? 15.271 22.325  48.433  1.00 27.12  ? 231 ILE A CA  1 
ATOM   609  C C   . ILE A 1 98  ? 15.877 21.014  47.942  1.00 26.95  ? 231 ILE A C   1 
ATOM   610  O O   . ILE A 1 98  ? 15.278 19.945  48.081  1.00 26.73  ? 231 ILE A O   1 
ATOM   611  C CB  . ILE A 1 98  ? 14.673 23.067  47.214  1.00 26.90  ? 231 ILE A CB  1 
ATOM   612  C CG1 . ILE A 1 98  ? 13.941 24.331  47.676  1.00 25.92  ? 231 ILE A CG1 1 
ATOM   613  C CG2 . ILE A 1 98  ? 13.720 22.139  46.468  1.00 26.64  ? 231 ILE A CG2 1 
ATOM   614  C CD1 . ILE A 1 98  ? 13.497 25.240  46.546  1.00 28.61  ? 231 ILE A CD1 1 
ATOM   615  N N   . PHE A 1 99  ? 17.064 21.112  47.356  1.00 27.01  ? 232 PHE A N   1 
ATOM   616  C CA  . PHE A 1 99  ? 17.761 19.945  46.836  1.00 29.34  ? 232 PHE A CA  1 
ATOM   617  C C   . PHE A 1 99  ? 18.015 18.939  47.959  1.00 31.02  ? 232 PHE A C   1 
ATOM   618  O O   . PHE A 1 99  ? 17.639 17.772  47.849  1.00 30.43  ? 232 PHE A O   1 
ATOM   619  C CB  . PHE A 1 99  ? 19.084 20.375  46.197  1.00 30.19  ? 232 PHE A CB  1 
ATOM   620  C CG  . PHE A 1 99  ? 19.854 19.247  45.569  1.00 33.97  ? 232 PHE A CG  1 
ATOM   621  C CD1 . PHE A 1 99  ? 19.310 18.515  44.516  1.00 34.94  ? 232 PHE A CD1 1 
ATOM   622  C CD2 . PHE A 1 99  ? 21.121 18.907  46.038  1.00 33.68  ? 232 PHE A CD2 1 
ATOM   623  C CE1 . PHE A 1 99  ? 20.015 17.455  43.938  1.00 37.67  ? 232 PHE A CE1 1 
ATOM   624  C CE2 . PHE A 1 99  ? 21.837 17.849  45.467  1.00 35.74  ? 232 PHE A CE2 1 
ATOM   625  C CZ  . PHE A 1 99  ? 21.283 17.121  44.415  1.00 35.46  ? 232 PHE A CZ  1 
ATOM   626  N N   . LYS A 1 100 ? 18.631 19.402  49.046  1.00 32.53  ? 233 LYS A N   1 
ATOM   627  C CA  . LYS A 1 100 ? 18.953 18.536  50.183  1.00 33.79  ? 233 LYS A CA  1 
ATOM   628  C C   . LYS A 1 100 ? 17.741 17.972  50.923  1.00 34.87  ? 233 LYS A C   1 
ATOM   629  O O   . LYS A 1 100 ? 17.833 16.919  51.553  1.00 34.77  ? 233 LYS A O   1 
ATOM   630  C CB  . LYS A 1 100 ? 19.853 19.285  51.172  1.00 34.83  ? 233 LYS A CB  1 
ATOM   631  C CG  . LYS A 1 100 ? 21.199 19.684  50.583  1.00 38.43  ? 233 LYS A CG  1 
ATOM   632  C CD  . LYS A 1 100 ? 22.059 20.483  51.564  1.00 44.42  ? 233 LYS A CD  1 
ATOM   633  C CE  . LYS A 1 100 ? 22.573 19.628  52.714  1.00 45.02  ? 233 LYS A CE  1 
ATOM   634  N NZ  . LYS A 1 100 ? 21.476 19.142  53.597  1.00 48.06  ? 233 LYS A NZ  1 
ATOM   635  N N   . SER A 1 101 ? 16.610 18.667  50.849  1.00 34.46  ? 234 SER A N   1 
ATOM   636  C CA  . SER A 1 101 ? 15.395 18.217  51.523  1.00 34.05  ? 234 SER A CA  1 
ATOM   637  C C   . SER A 1 101 ? 14.622 17.203  50.692  1.00 33.93  ? 234 SER A C   1 
ATOM   638  O O   . SER A 1 101 ? 13.486 16.864  51.024  1.00 34.50  ? 234 SER A O   1 
ATOM   639  C CB  . SER A 1 101 ? 14.477 19.405  51.818  1.00 35.33  ? 234 SER A CB  1 
ATOM   640  O OG  . SER A 1 101 ? 15.106 20.348  52.665  1.00 40.81  ? 234 SER A OG  1 
ATOM   641  N N   . GLY A 1 102 ? 15.227 16.727  49.609  1.00 32.71  ? 235 GLY A N   1 
ATOM   642  C CA  . GLY A 1 102 ? 14.544 15.766  48.762  1.00 31.46  ? 235 GLY A CA  1 
ATOM   643  C C   . GLY A 1 102 ? 13.380 16.412  48.032  1.00 30.87  ? 235 GLY A C   1 
ATOM   644  O O   . GLY A 1 102 ? 12.396 15.754  47.694  1.00 29.87  ? 235 GLY A O   1 
ATOM   645  N N   . GLY A 1 103 ? 13.498 17.711  47.778  1.00 29.50  ? 236 GLY A N   1 
ATOM   646  C CA  . GLY A 1 103 ? 12.439 18.430  47.097  1.00 29.48  ? 236 GLY A CA  1 
ATOM   647  C C   . GLY A 1 103 ? 12.195 18.054  45.646  1.00 29.15  ? 236 GLY A C   1 
ATOM   648  O O   . GLY A 1 103 ? 11.072 18.180  45.163  1.00 29.54  ? 236 GLY A O   1 
ATOM   649  N N   . ILE A 1 104 ? 13.223 17.585  44.945  1.00 28.42  ? 237 ILE A N   1 
ATOM   650  C CA  . ILE A 1 104 ? 13.062 17.227  43.538  1.00 28.48  ? 237 ILE A CA  1 
ATOM   651  C C   . ILE A 1 104 ? 12.052 16.106  43.305  1.00 30.93  ? 237 ILE A C   1 
ATOM   652  O O   . ILE A 1 104 ? 11.168 16.229  42.451  1.00 30.63  ? 237 ILE A O   1 
ATOM   653  C CB  . ILE A 1 104 ? 14.432 16.886  42.886  1.00 28.74  ? 237 ILE A CB  1 
ATOM   654  C CG1 . ILE A 1 104 ? 15.196 18.193  42.624  1.00 26.64  ? 237 ILE A CG1 1 
ATOM   655  C CG2 . ILE A 1 104 ? 14.235 16.080  41.604  1.00 26.68  ? 237 ILE A CG2 1 
ATOM   656  C CD1 . ILE A 1 104 ? 16.502 18.035  41.875  1.00 26.54  ? 237 ILE A CD1 1 
ATOM   657  N N   . PRO A 1 105 ? 12.164 14.994  44.050  1.00 31.21  ? 238 PRO A N   1 
ATOM   658  C CA  . PRO A 1 105 ? 11.190 13.921  43.835  1.00 32.74  ? 238 PRO A CA  1 
ATOM   659  C C   . PRO A 1 105 ? 9.764  14.395  44.118  1.00 33.05  ? 238 PRO A C   1 
ATOM   660  O O   . PRO A 1 105 ? 8.823  14.009  43.426  1.00 34.14  ? 238 PRO A O   1 
ATOM   661  C CB  . PRO A 1 105 ? 11.654 12.846  44.812  1.00 33.84  ? 238 PRO A CB  1 
ATOM   662  C CG  . PRO A 1 105 ? 13.147 13.014  44.771  1.00 32.97  ? 238 PRO A CG  1 
ATOM   663  C CD  . PRO A 1 105 ? 13.297 14.514  44.862  1.00 31.26  ? 238 PRO A CD  1 
ATOM   664  N N   . ALA A 1 106 ? 9.610  15.240  45.132  1.00 31.67  ? 239 ALA A N   1 
ATOM   665  C CA  . ALA A 1 106 ? 8.295  15.754  45.500  1.00 31.78  ? 239 ALA A CA  1 
ATOM   666  C C   . ALA A 1 106 ? 7.739  16.691  44.427  1.00 32.16  ? 239 ALA A C   1 
ATOM   667  O O   . ALA A 1 106 ? 6.539  16.695  44.159  1.00 31.22  ? 239 ALA A O   1 
ATOM   668  C CB  . ALA A 1 106 ? 8.374  16.484  46.834  1.00 30.90  ? 239 ALA A CB  1 
ATOM   669  N N   . LEU A 1 107 ? 8.617  17.486  43.822  1.00 30.57  ? 240 LEU A N   1 
ATOM   670  C CA  . LEU A 1 107 ? 8.206  18.421  42.782  1.00 29.89  ? 240 LEU A CA  1 
ATOM   671  C C   . LEU A 1 107 ? 7.770  17.669  41.528  1.00 30.66  ? 240 LEU A C   1 
ATOM   672  O O   . LEU A 1 107 ? 6.788  18.043  40.887  1.00 30.56  ? 240 LEU A O   1 
ATOM   673  C CB  . LEU A 1 107 ? 9.352  19.384  42.457  1.00 29.27  ? 240 LEU A CB  1 
ATOM   674  C CG  . LEU A 1 107 ? 9.658  20.414  43.549  1.00 27.61  ? 240 LEU A CG  1 
ATOM   675  C CD1 . LEU A 1 107 ? 10.991 21.091  43.285  1.00 27.75  ? 240 LEU A CD1 1 
ATOM   676  C CD2 . LEU A 1 107 ? 8.531  21.438  43.601  1.00 29.29  ? 240 LEU A CD2 1 
ATOM   677  N N   . VAL A 1 108 ? 8.501  16.610  41.186  1.00 30.95  ? 241 VAL A N   1 
ATOM   678  C CA  . VAL A 1 108 ? 8.176  15.800  40.019  1.00 32.39  ? 241 VAL A CA  1 
ATOM   679  C C   . VAL A 1 108 ? 6.800  15.159  40.204  1.00 34.15  ? 241 VAL A C   1 
ATOM   680  O O   . VAL A 1 108 ? 6.038  15.013  39.244  1.00 34.08  ? 241 VAL A O   1 
ATOM   681  C CB  . VAL A 1 108 ? 9.236  14.696  39.788  1.00 31.13  ? 241 VAL A CB  1 
ATOM   682  C CG1 . VAL A 1 108 ? 8.738  13.692  38.759  1.00 32.22  ? 241 VAL A CG1 1 
ATOM   683  C CG2 . VAL A 1 108 ? 10.535 15.323  39.299  1.00 31.35  ? 241 VAL A CG2 1 
ATOM   684  N N   . LYS A 1 109 ? 6.484  14.779  41.439  1.00 35.15  ? 242 LYS A N   1 
ATOM   685  C CA  . LYS A 1 109 ? 5.187  14.181  41.730  1.00 36.15  ? 242 LYS A CA  1 
ATOM   686  C C   . LYS A 1 109 ? 4.091  15.215  41.492  1.00 35.14  ? 242 LYS A C   1 
ATOM   687  O O   . LYS A 1 109 ? 3.031  14.896  40.962  1.00 35.71  ? 242 LYS A O   1 
ATOM   688  C CB  . LYS A 1 109 ? 5.119  13.697  43.183  1.00 38.72  ? 242 LYS A CB  1 
ATOM   689  C CG  . LYS A 1 109 ? 3.737  13.183  43.579  1.00 42.32  ? 242 LYS A CG  1 
ATOM   690  C CD  . LYS A 1 109 ? 3.683  12.676  45.017  1.00 44.87  ? 242 LYS A CD  1 
ATOM   691  C CE  . LYS A 1 109 ? 2.301  12.111  45.338  1.00 46.96  ? 242 LYS A CE  1 
ATOM   692  N NZ  . LYS A 1 109 ? 2.208  11.539  46.713  1.00 48.24  ? 242 LYS A NZ  1 
ATOM   693  N N   . MET A 1 110 ? 4.357  16.457  41.881  1.00 34.81  ? 243 MET A N   1 
ATOM   694  C CA  . MET A 1 110 ? 3.387  17.529  41.712  1.00 36.08  ? 243 MET A CA  1 
ATOM   695  C C   . MET A 1 110 ? 3.066  17.820  40.247  1.00 37.78  ? 243 MET A C   1 
ATOM   696  O O   . MET A 1 110 ? 2.089  18.513  39.947  1.00 38.84  ? 243 MET A O   1 
ATOM   697  C CB  . MET A 1 110 ? 3.881  18.809  42.392  1.00 35.64  ? 243 MET A CB  1 
ATOM   698  C CG  . MET A 1 110 ? 4.079  18.675  43.896  1.00 36.16  ? 243 MET A CG  1 
ATOM   699  S SD  . MET A 1 110 ? 2.654  17.944  44.747  1.00 40.90  ? 243 MET A SD  1 
ATOM   700  C CE  . MET A 1 110 ? 1.577  19.352  44.861  1.00 34.19  ? 243 MET A CE  1 
ATOM   701  N N   . LEU A 1 111 ? 3.883  17.302  39.335  1.00 37.72  ? 244 LEU A N   1 
ATOM   702  C CA  . LEU A 1 111 ? 3.646  17.522  37.913  1.00 39.43  ? 244 LEU A CA  1 
ATOM   703  C C   . LEU A 1 111 ? 2.405  16.766  37.449  1.00 42.36  ? 244 LEU A C   1 
ATOM   704  O O   . LEU A 1 111 ? 1.973  16.905  36.303  1.00 44.01  ? 244 LEU A O   1 
ATOM   705  C CB  . LEU A 1 111 ? 4.863  17.089  37.091  1.00 34.14  ? 244 LEU A CB  1 
ATOM   706  C CG  . LEU A 1 111 ? 6.107  17.962  37.296  1.00 33.78  ? 244 LEU A CG  1 
ATOM   707  C CD1 . LEU A 1 111 ? 7.210  17.520  36.348  1.00 30.54  ? 244 LEU A CD1 1 
ATOM   708  C CD2 . LEU A 1 111 ? 5.744  19.427  37.055  1.00 28.78  ? 244 LEU A CD2 1 
ATOM   709  N N   . GLY A 1 112 ? 1.835  15.967  38.347  1.00 44.66  ? 245 GLY A N   1 
ATOM   710  C CA  . GLY A 1 112 ? 0.641  15.209  38.014  1.00 46.36  ? 245 GLY A CA  1 
ATOM   711  C C   . GLY A 1 112 ? -0.607 15.868  38.571  1.00 47.78  ? 245 GLY A C   1 
ATOM   712  O O   . GLY A 1 112 ? -1.699 15.307  38.505  1.00 48.82  ? 245 GLY A O   1 
ATOM   713  N N   . SER A 1 113 ? -0.443 17.068  39.120  1.00 48.89  ? 246 SER A N   1 
ATOM   714  C CA  . SER A 1 113 ? -1.554 17.814  39.701  1.00 51.73  ? 246 SER A CA  1 
ATOM   715  C C   . SER A 1 113 ? -2.441 18.485  38.658  1.00 54.63  ? 246 SER A C   1 
ATOM   716  O O   . SER A 1 113 ? -1.951 19.140  37.735  1.00 55.39  ? 246 SER A O   1 
ATOM   717  C CB  . SER A 1 113 ? -1.027 18.883  40.657  1.00 51.71  ? 246 SER A CB  1 
ATOM   718  O OG  . SER A 1 113 ? -2.071 19.738  41.086  1.00 51.37  ? 246 SER A OG  1 
ATOM   719  N N   . PRO A 1 114 ? -3.766 18.323  38.793  1.00 56.04  ? 247 PRO A N   1 
ATOM   720  C CA  . PRO A 1 114 ? -4.720 18.923  37.857  1.00 56.61  ? 247 PRO A CA  1 
ATOM   721  C C   . PRO A 1 114 ? -4.774 20.438  38.025  1.00 57.22  ? 247 PRO A C   1 
ATOM   722  O O   . PRO A 1 114 ? -5.179 21.161  37.115  1.00 58.83  ? 247 PRO A O   1 
ATOM   723  C CB  . PRO A 1 114 ? -6.040 18.256  38.236  1.00 57.24  ? 247 PRO A CB  1 
ATOM   724  C CG  . PRO A 1 114 ? -5.606 16.923  38.780  1.00 57.15  ? 247 PRO A CG  1 
ATOM   725  C CD  . PRO A 1 114 ? -4.436 17.323  39.642  1.00 56.94  ? 247 PRO A CD  1 
ATOM   726  N N   . VAL A 1 115 ? -4.360 20.913  39.195  1.00 56.20  ? 248 VAL A N   1 
ATOM   727  C CA  . VAL A 1 115 ? -4.366 22.342  39.483  1.00 55.52  ? 248 VAL A CA  1 
ATOM   728  C C   . VAL A 1 115 ? -3.244 23.053  38.733  1.00 55.29  ? 248 VAL A C   1 
ATOM   729  O O   . VAL A 1 115 ? -2.065 22.778  38.959  1.00 55.81  ? 248 VAL A O   1 
ATOM   730  C CB  . VAL A 1 115 ? -4.193 22.603  40.990  1.00 55.45  ? 248 VAL A CB  1 
ATOM   731  C CG1 . VAL A 1 115 ? -4.438 24.071  41.295  1.00 55.59  ? 248 VAL A CG1 1 
ATOM   732  C CG2 . VAL A 1 115 ? -5.144 21.725  41.779  1.00 55.85  ? 248 VAL A CG2 1 
ATOM   733  N N   . ASP A 1 116 ? -3.612 23.971  37.843  1.00 54.10  ? 249 ASP A N   1 
ATOM   734  C CA  . ASP A 1 116 ? -2.618 24.706  37.070  1.00 52.88  ? 249 ASP A CA  1 
ATOM   735  C C   . ASP A 1 116 ? -1.667 25.503  37.956  1.00 50.76  ? 249 ASP A C   1 
ATOM   736  O O   . ASP A 1 116 ? -0.470 25.574  37.677  1.00 50.01  ? 249 ASP A O   1 
ATOM   737  C CB  . ASP A 1 116 ? -3.290 25.657  36.072  1.00 54.90  ? 249 ASP A CB  1 
ATOM   738  C CG  . ASP A 1 116 ? -4.027 24.925  34.964  1.00 56.90  ? 249 ASP A CG  1 
ATOM   739  O OD1 . ASP A 1 116 ? -3.516 23.893  34.479  1.00 58.00  ? 249 ASP A OD1 1 
ATOM   740  O OD2 . ASP A 1 116 ? -5.114 25.393  34.564  1.00 59.14  ? 249 ASP A OD2 1 
ATOM   741  N N   . SER A 1 117 ? -2.196 26.106  39.018  1.00 47.69  ? 250 SER A N   1 
ATOM   742  C CA  . SER A 1 117 ? -1.368 26.896  39.925  1.00 45.24  ? 250 SER A CA  1 
ATOM   743  C C   . SER A 1 117 ? -0.224 26.053  40.491  1.00 43.59  ? 250 SER A C   1 
ATOM   744  O O   . SER A 1 117 ? 0.919  26.503  40.554  1.00 42.15  ? 250 SER A O   1 
ATOM   745  C CB  . SER A 1 117 ? -2.215 27.453  41.071  1.00 45.13  ? 250 SER A CB  1 
ATOM   746  O OG  . SER A 1 117 ? -2.795 26.405  41.826  1.00 45.86  ? 250 SER A OG  1 
ATOM   747  N N   . VAL A 1 118 ? -0.544 24.829  40.896  1.00 42.59  ? 251 VAL A N   1 
ATOM   748  C CA  . VAL A 1 118 ? 0.443  23.911  41.450  1.00 42.63  ? 251 VAL A CA  1 
ATOM   749  C C   . VAL A 1 118 ? 1.466  23.530  40.382  1.00 41.52  ? 251 VAL A C   1 
ATOM   750  O O   . VAL A 1 118 ? 2.673  23.597  40.621  1.00 40.46  ? 251 VAL A O   1 
ATOM   751  C CB  . VAL A 1 118 ? -0.234 22.630  41.989  1.00 43.62  ? 251 VAL A CB  1 
ATOM   752  C CG1 . VAL A 1 118 ? 0.807  21.693  42.579  1.00 43.52  ? 251 VAL A CG1 1 
ATOM   753  C CG2 . VAL A 1 118 ? -1.269 22.999  43.041  1.00 43.44  ? 251 VAL A CG2 1 
ATOM   754  N N   . LEU A 1 119 ? 0.974  23.139  39.207  1.00 40.06  ? 252 LEU A N   1 
ATOM   755  C CA  . LEU A 1 119 ? 1.833  22.754  38.090  1.00 39.13  ? 252 LEU A CA  1 
ATOM   756  C C   . LEU A 1 119 ? 2.824  23.846  37.707  1.00 37.27  ? 252 LEU A C   1 
ATOM   757  O O   . LEU A 1 119 ? 4.000  23.569  37.481  1.00 36.95  ? 252 LEU A O   1 
ATOM   758  C CB  . LEU A 1 119 ? 0.993  22.400  36.859  1.00 40.76  ? 252 LEU A CB  1 
ATOM   759  C CG  . LEU A 1 119 ? 0.481  20.969  36.722  1.00 42.29  ? 252 LEU A CG  1 
ATOM   760  C CD1 . LEU A 1 119 ? -0.379 20.849  35.468  1.00 44.15  ? 252 LEU A CD1 1 
ATOM   761  C CD2 . LEU A 1 119 ? 1.660  20.016  36.645  1.00 43.20  ? 252 LEU A CD2 1 
ATOM   762  N N   . PHE A 1 120 ? 2.352  25.087  37.634  1.00 35.26  ? 253 PHE A N   1 
ATOM   763  C CA  . PHE A 1 120 ? 3.220  26.195  37.255  1.00 35.45  ? 253 PHE A CA  1 
ATOM   764  C C   . PHE A 1 120 ? 4.335  26.419  38.267  1.00 33.79  ? 253 PHE A C   1 
ATOM   765  O O   . PHE A 1 120 ? 5.491  26.639  37.890  1.00 32.52  ? 253 PHE A O   1 
ATOM   766  C CB  . PHE A 1 120 ? 2.419  27.486  37.091  1.00 39.53  ? 253 PHE A CB  1 
ATOM   767  C CG  . PHE A 1 120 ? 3.195  28.587  36.427  1.00 45.11  ? 253 PHE A CG  1 
ATOM   768  C CD1 . PHE A 1 120 ? 3.503  28.513  35.069  1.00 47.09  ? 253 PHE A CD1 1 
ATOM   769  C CD2 . PHE A 1 120 ? 3.650  29.680  37.160  1.00 47.47  ? 253 PHE A CD2 1 
ATOM   770  C CE1 . PHE A 1 120 ? 4.255  29.509  34.450  1.00 48.62  ? 253 PHE A CE1 1 
ATOM   771  C CE2 . PHE A 1 120 ? 4.405  30.686  36.550  1.00 49.38  ? 253 PHE A CE2 1 
ATOM   772  C CZ  . PHE A 1 120 ? 4.707  30.597  35.191  1.00 49.42  ? 253 PHE A CZ  1 
ATOM   773  N N   . TYR A 1 121 ? 3.986  26.387  39.551  1.00 30.20  ? 254 TYR A N   1 
ATOM   774  C CA  . TYR A 1 121 ? 4.980  26.564  40.605  1.00 30.72  ? 254 TYR A CA  1 
ATOM   775  C C   . TYR A 1 121 ? 5.991  25.414  40.547  1.00 28.69  ? 254 TYR A C   1 
ATOM   776  O O   . TYR A 1 121 ? 7.200  25.630  40.627  1.00 28.79  ? 254 TYR A O   1 
ATOM   777  C CB  . TYR A 1 121 ? 4.304  26.585  41.981  1.00 30.72  ? 254 TYR A CB  1 
ATOM   778  C CG  . TYR A 1 121 ? 3.649  27.901  42.340  1.00 34.28  ? 254 TYR A CG  1 
ATOM   779  C CD1 . TYR A 1 121 ? 2.481  27.934  43.102  1.00 35.31  ? 254 TYR A CD1 1 
ATOM   780  C CD2 . TYR A 1 121 ? 4.208  29.116  41.937  1.00 35.17  ? 254 TYR A CD2 1 
ATOM   781  C CE1 . TYR A 1 121 ? 1.883  29.140  43.453  1.00 36.46  ? 254 TYR A CE1 1 
ATOM   782  C CE2 . TYR A 1 121 ? 3.620  30.329  42.284  1.00 36.77  ? 254 TYR A CE2 1 
ATOM   783  C CZ  . TYR A 1 121 ? 2.457  30.333  43.041  1.00 38.04  ? 254 TYR A CZ  1 
ATOM   784  O OH  . TYR A 1 121 ? 1.865  31.532  43.375  1.00 41.39  ? 254 TYR A OH  1 
ATOM   785  N N   . ALA A 1 122 ? 5.479  24.198  40.388  1.00 25.72  ? 255 ALA A N   1 
ATOM   786  C CA  . ALA A 1 122 ? 6.312  23.006  40.329  1.00 26.25  ? 255 ALA A CA  1 
ATOM   787  C C   . ALA A 1 122 ? 7.309  22.999  39.166  1.00 25.96  ? 255 ALA A C   1 
ATOM   788  O O   . ALA A 1 122 ? 8.503  22.789  39.385  1.00 24.29  ? 255 ALA A O   1 
ATOM   789  C CB  . ALA A 1 122 ? 5.430  21.765  40.268  1.00 23.64  ? 255 ALA A CB  1 
ATOM   790  N N   . ILE A 1 123 ? 6.834  23.227  37.938  1.00 23.70  ? 256 ILE A N   1 
ATOM   791  C CA  . ILE A 1 123 ? 7.733  23.219  36.783  1.00 23.30  ? 256 ILE A CA  1 
ATOM   792  C C   . ILE A 1 123 ? 8.723  24.384  36.825  1.00 24.14  ? 256 ILE A C   1 
ATOM   793  O O   . ILE A 1 123 ? 9.858  24.255  36.361  1.00 24.22  ? 256 ILE A O   1 
ATOM   794  C CB  . ILE A 1 123 ? 6.955  23.261  35.423  1.00 23.07  ? 256 ILE A CB  1 
ATOM   795  C CG1 . ILE A 1 123 ? 7.896  22.899  34.273  1.00 25.32  ? 256 ILE A CG1 1 
ATOM   796  C CG2 . ILE A 1 123 ? 6.411  24.652  35.155  1.00 20.74  ? 256 ILE A CG2 1 
ATOM   797  C CD1 . ILE A 1 123 ? 8.314  21.445  34.245  1.00 26.33  ? 256 ILE A CD1 1 
ATOM   798  N N   . THR A 1 124 ? 8.298  25.520  37.372  1.00 22.98  ? 257 THR A N   1 
ATOM   799  C CA  . THR A 1 124 ? 9.187  26.677  37.460  1.00 25.11  ? 257 THR A CA  1 
ATOM   800  C C   . THR A 1 124 ? 10.286 26.431  38.494  1.00 24.29  ? 257 THR A C   1 
ATOM   801  O O   . THR A 1 124 ? 11.433 26.824  38.293  1.00 25.60  ? 257 THR A O   1 
ATOM   802  C CB  . THR A 1 124 ? 8.421  27.971  37.837  1.00 25.39  ? 257 THR A CB  1 
ATOM   803  O OG1 . THR A 1 124 ? 7.481  28.293  36.801  1.00 28.97  ? 257 THR A OG1 1 
ATOM   804  C CG2 . THR A 1 124 ? 9.393  29.133  37.992  1.00 26.61  ? 257 THR A CG2 1 
ATOM   805  N N   . THR A 1 125 ? 9.936  25.779  39.597  1.00 23.73  ? 258 THR A N   1 
ATOM   806  C CA  . THR A 1 125 ? 10.921 25.489  40.636  1.00 24.13  ? 258 THR A CA  1 
ATOM   807  C C   . THR A 1 125 ? 11.945 24.506  40.080  1.00 23.04  ? 258 THR A C   1 
ATOM   808  O O   . THR A 1 125 ? 13.144 24.669  40.288  1.00 24.10  ? 258 THR A O   1 
ATOM   809  C CB  . THR A 1 125 ? 10.255 24.888  41.890  1.00 24.49  ? 258 THR A CB  1 
ATOM   810  O OG1 . THR A 1 125 ? 9.209  25.762  42.329  1.00 25.15  ? 258 THR A OG1 1 
ATOM   811  C CG2 . THR A 1 125 ? 11.282 24.730  43.026  1.00 21.37  ? 258 THR A CG2 1 
ATOM   812  N N   . LEU A 1 126 ? 11.461 23.497  39.361  1.00 22.21  ? 259 LEU A N   1 
ATOM   813  C CA  . LEU A 1 126 ? 12.330 22.494  38.750  1.00 22.25  ? 259 LEU A CA  1 
ATOM   814  C C   . LEU A 1 126 ? 13.234 23.152  37.710  1.00 22.84  ? 259 LEU A C   1 
ATOM   815  O O   . LEU A 1 126 ? 14.406 22.793  37.574  1.00 21.22  ? 259 LEU A O   1 
ATOM   816  C CB  . LEU A 1 126 ? 11.490 21.401  38.087  1.00 22.09  ? 259 LEU A CB  1 
ATOM   817  C CG  . LEU A 1 126 ? 10.807 20.415  39.038  1.00 22.26  ? 259 LEU A CG  1 
ATOM   818  C CD1 . LEU A 1 126 ? 9.825  19.533  38.280  1.00 23.16  ? 259 LEU A CD1 1 
ATOM   819  C CD2 . LEU A 1 126 ? 11.876 19.560  39.710  1.00 24.34  ? 259 LEU A CD2 1 
ATOM   820  N N   . HIS A 1 127 ? 12.675 24.115  36.980  1.00 22.56  ? 260 HIS A N   1 
ATOM   821  C CA  . HIS A 1 127 ? 13.420 24.840  35.955  1.00 23.46  ? 260 HIS A CA  1 
ATOM   822  C C   . HIS A 1 127 ? 14.587 25.598  36.596  1.00 21.55  ? 260 HIS A C   1 
ATOM   823  O O   . HIS A 1 127 ? 15.693 25.602  36.066  1.00 22.38  ? 260 HIS A O   1 
ATOM   824  C CB  . HIS A 1 127 ? 12.494 25.820  35.224  1.00 24.90  ? 260 HIS A CB  1 
ATOM   825  C CG  . HIS A 1 127 ? 13.111 26.449  34.014  1.00 27.11  ? 260 HIS A CG  1 
ATOM   826  N ND1 . HIS A 1 127 ? 13.266 27.812  33.881  1.00 28.77  ? 260 HIS A ND1 1 
ATOM   827  C CD2 . HIS A 1 127 ? 13.615 25.900  32.882  1.00 27.85  ? 260 HIS A CD2 1 
ATOM   828  C CE1 . HIS A 1 127 ? 13.840 28.077  32.719  1.00 29.64  ? 260 HIS A CE1 1 
ATOM   829  N NE2 . HIS A 1 127 ? 14.063 26.934  32.094  1.00 28.08  ? 260 HIS A NE2 1 
ATOM   830  N N   . ASN A 1 128 ? 14.345 26.237  37.735  1.00 21.28  ? 261 ASN A N   1 
ATOM   831  C CA  . ASN A 1 128 ? 15.419 26.969  38.407  1.00 22.35  ? 261 ASN A CA  1 
ATOM   832  C C   . ASN A 1 128 ? 16.486 26.005  38.937  1.00 22.87  ? 261 ASN A C   1 
ATOM   833  O O   . ASN A 1 128 ? 17.676 26.314  38.917  1.00 23.11  ? 261 ASN A O   1 
ATOM   834  C CB  . ASN A 1 128 ? 14.858 27.833  39.543  1.00 22.06  ? 261 ASN A CB  1 
ATOM   835  C CG  . ASN A 1 128 ? 14.055 29.020  39.024  1.00 23.16  ? 261 ASN A CG  1 
ATOM   836  O OD1 . ASN A 1 128 ? 14.277 29.484  37.905  1.00 21.39  ? 261 ASN A OD1 1 
ATOM   837  N ND2 . ASN A 1 128 ? 13.131 29.523  39.838  1.00 21.88  ? 261 ASN A ND2 1 
ATOM   838  N N   . LEU A 1 129 ? 16.058 24.831  39.394  1.00 22.83  ? 262 LEU A N   1 
ATOM   839  C CA  . LEU A 1 129 ? 16.997 23.828  39.890  1.00 24.32  ? 262 LEU A CA  1 
ATOM   840  C C   . LEU A 1 129 ? 17.856 23.300  38.731  1.00 23.31  ? 262 LEU A C   1 
ATOM   841  O O   . LEU A 1 129 ? 19.081 23.222  38.840  1.00 23.58  ? 262 LEU A O   1 
ATOM   842  C CB  . LEU A 1 129 ? 16.231 22.681  40.555  1.00 23.90  ? 262 LEU A CB  1 
ATOM   843  C CG  . LEU A 1 129 ? 15.638 23.027  41.922  1.00 24.06  ? 262 LEU A CG  1 
ATOM   844  C CD1 . LEU A 1 129 ? 14.573 22.014  42.316  1.00 20.37  ? 262 LEU A CD1 1 
ATOM   845  C CD2 . LEU A 1 129 ? 16.759 23.070  42.949  1.00 22.24  ? 262 LEU A CD2 1 
ATOM   846  N N   . LEU A 1 130 ? 17.212 22.960  37.618  1.00 22.08  ? 263 LEU A N   1 
ATOM   847  C CA  . LEU A 1 130 ? 17.921 22.450  36.445  1.00 22.71  ? 263 LEU A CA  1 
ATOM   848  C C   . LEU A 1 130 ? 18.936 23.453  35.896  1.00 24.16  ? 263 LEU A C   1 
ATOM   849  O O   . LEU A 1 130 ? 20.024 23.074  35.456  1.00 23.11  ? 263 LEU A O   1 
ATOM   850  C CB  . LEU A 1 130 ? 16.918 22.071  35.354  1.00 21.10  ? 263 LEU A CB  1 
ATOM   851  C CG  . LEU A 1 130 ? 16.059 20.840  35.667  1.00 21.32  ? 263 LEU A CG  1 
ATOM   852  C CD1 . LEU A 1 130 ? 14.951 20.685  34.625  1.00 18.22  ? 263 LEU A CD1 1 
ATOM   853  C CD2 . LEU A 1 130 ? 16.952 19.598  35.688  1.00 18.99  ? 263 LEU A CD2 1 
ATOM   854  N N   . LEU A 1 131 ? 18.580 24.734  35.931  1.00 25.65  ? 264 LEU A N   1 
ATOM   855  C CA  . LEU A 1 131 ? 19.464 25.789  35.447  1.00 27.70  ? 264 LEU A CA  1 
ATOM   856  C C   . LEU A 1 131 ? 20.651 26.106  36.367  1.00 29.73  ? 264 LEU A C   1 
ATOM   857  O O   . LEU A 1 131 ? 21.750 26.370  35.880  1.00 30.13  ? 264 LEU A O   1 
ATOM   858  C CB  . LEU A 1 131 ? 18.675 27.084  35.231  1.00 29.12  ? 264 LEU A CB  1 
ATOM   859  C CG  . LEU A 1 131 ? 17.658 27.190  34.090  1.00 30.01  ? 264 LEU A CG  1 
ATOM   860  C CD1 . LEU A 1 131 ? 16.794 28.431  34.296  1.00 32.10  ? 264 LEU A CD1 1 
ATOM   861  C CD2 . LEU A 1 131 ? 18.383 27.261  32.755  1.00 31.30  ? 264 LEU A CD2 1 
ATOM   862  N N   . HIS A 1 132 ? 20.446 26.059  37.684  1.00 29.91  ? 265 HIS A N   1 
ATOM   863  C CA  . HIS A 1 132 ? 21.518 26.430  38.612  1.00 30.90  ? 265 HIS A CA  1 
ATOM   864  C C   . HIS A 1 132 ? 22.049 25.438  39.645  1.00 32.28  ? 265 HIS A C   1 
ATOM   865  O O   . HIS A 1 132 ? 23.196 25.573  40.087  1.00 32.68  ? 265 HIS A O   1 
ATOM   866  C CB  . HIS A 1 132 ? 21.115 27.702  39.371  1.00 31.37  ? 265 HIS A CB  1 
ATOM   867  C CG  . HIS A 1 132 ? 20.656 28.820  38.485  1.00 31.36  ? 265 HIS A CG  1 
ATOM   868  N ND1 . HIS A 1 132 ? 19.323 29.099  38.268  1.00 33.67  ? 265 HIS A ND1 1 
ATOM   869  C CD2 . HIS A 1 132 ? 21.352 29.723  37.755  1.00 31.43  ? 265 HIS A CD2 1 
ATOM   870  C CE1 . HIS A 1 132 ? 19.218 30.128  37.446  1.00 29.74  ? 265 HIS A CE1 1 
ATOM   871  N NE2 . HIS A 1 132 ? 20.435 30.525  37.120  1.00 31.85  ? 265 HIS A NE2 1 
ATOM   872  N N   . GLN A 1 133 ? 21.239 24.463  40.047  1.00 30.23  ? 266 GLN A N   1 
ATOM   873  C CA  . GLN A 1 133 ? 21.666 23.522  41.079  1.00 30.57  ? 266 GLN A CA  1 
ATOM   874  C C   . GLN A 1 133 ? 22.424 22.292  40.603  1.00 31.20  ? 266 GLN A C   1 
ATOM   875  O O   . GLN A 1 133 ? 21.873 21.425  39.920  1.00 28.99  ? 266 GLN A O   1 
ATOM   876  C CB  . GLN A 1 133 ? 20.459 23.077  41.911  1.00 30.16  ? 266 GLN A CB  1 
ATOM   877  C CG  . GLN A 1 133 ? 20.796 22.113  43.047  1.00 29.29  ? 266 GLN A CG  1 
ATOM   878  C CD  . GLN A 1 133 ? 21.776 22.702  44.048  1.00 31.22  ? 266 GLN A CD  1 
ATOM   879  O OE1 . GLN A 1 133 ? 21.535 23.771  44.617  1.00 29.18  ? 266 GLN A OE1 1 
ATOM   880  N NE2 . GLN A 1 133 ? 22.887 22.003  44.272  1.00 28.29  ? 266 GLN A NE2 1 
ATOM   881  N N   . GLU A 1 134 ? 23.696 22.223  40.984  1.00 32.15  ? 267 GLU A N   1 
ATOM   882  C CA  . GLU A 1 134 ? 24.543 21.090  40.632  1.00 34.43  ? 267 GLU A CA  1 
ATOM   883  C C   . GLU A 1 134 ? 23.895 19.815  41.170  1.00 31.76  ? 267 GLU A C   1 
ATOM   884  O O   . GLU A 1 134 ? 23.532 19.749  42.345  1.00 31.10  ? 267 GLU A O   1 
ATOM   885  C CB  . GLU A 1 134 ? 25.937 21.280  41.244  1.00 39.88  ? 267 GLU A CB  1 
ATOM   886  C CG  . GLU A 1 134 ? 26.885 20.100  41.073  1.00 48.01  ? 267 GLU A CG  1 
ATOM   887  C CD  . GLU A 1 134 ? 28.303 20.422  41.533  1.00 53.69  ? 267 GLU A CD  1 
ATOM   888  O OE1 . GLU A 1 134 ? 28.457 21.030  42.617  1.00 55.27  ? 267 GLU A OE1 1 
ATOM   889  O OE2 . GLU A 1 134 ? 29.264 20.059  40.817  1.00 55.13  ? 267 GLU A OE2 1 
ATOM   890  N N   . GLY A 1 135 ? 23.737 18.819  40.300  1.00 29.18  ? 268 GLY A N   1 
ATOM   891  C CA  . GLY A 1 135 ? 23.136 17.557  40.694  1.00 27.66  ? 268 GLY A CA  1 
ATOM   892  C C   . GLY A 1 135 ? 21.649 17.449  40.379  1.00 28.05  ? 268 GLY A C   1 
ATOM   893  O O   . GLY A 1 135 ? 21.079 16.356  40.395  1.00 27.07  ? 268 GLY A O   1 
ATOM   894  N N   . ALA A 1 136 ? 21.017 18.578  40.081  1.00 26.07  ? 269 ALA A N   1 
ATOM   895  C CA  . ALA A 1 136 ? 19.586 18.588  39.783  1.00 26.26  ? 269 ALA A CA  1 
ATOM   896  C C   . ALA A 1 136 ? 19.186 17.738  38.584  1.00 24.10  ? 269 ALA A C   1 
ATOM   897  O O   . ALA A 1 136 ? 18.170 17.055  38.623  1.00 22.57  ? 269 ALA A O   1 
ATOM   898  C CB  . ALA A 1 136 ? 19.096 20.031  39.582  1.00 26.08  ? 269 ALA A CB  1 
ATOM   899  N N   . LYS A 1 137 ? 19.973 17.776  37.516  1.00 25.11  ? 270 LYS A N   1 
ATOM   900  C CA  . LYS A 1 137 ? 19.627 17.004  36.331  1.00 26.81  ? 270 LYS A CA  1 
ATOM   901  C C   . LYS A 1 137 ? 19.520 15.503  36.585  1.00 28.50  ? 270 LYS A C   1 
ATOM   902  O O   . LYS A 1 137 ? 18.545 14.869  36.165  1.00 25.27  ? 270 LYS A O   1 
ATOM   903  C CB  . LYS A 1 137 ? 20.624 17.284  35.201  1.00 27.36  ? 270 LYS A CB  1 
ATOM   904  C CG  . LYS A 1 137 ? 20.593 18.733  34.732  1.00 28.35  ? 270 LYS A CG  1 
ATOM   905  C CD  . LYS A 1 137 ? 21.403 18.952  33.460  1.00 31.20  ? 270 LYS A CD  1 
ATOM   906  C CE  . LYS A 1 137 ? 22.874 18.673  33.672  1.00 31.93  ? 270 LYS A CE  1 
ATOM   907  N NZ  . LYS A 1 137 ? 23.651 18.929  32.423  1.00 35.46  ? 270 LYS A NZ  1 
ATOM   908  N N   . MET A 1 138 ? 20.506 14.928  37.272  1.00 29.03  ? 271 MET A N   1 
ATOM   909  C CA  . MET A 1 138 ? 20.470 13.492  37.559  1.00 30.20  ? 271 MET A CA  1 
ATOM   910  C C   . MET A 1 138 ? 19.261 13.158  38.422  1.00 28.67  ? 271 MET A C   1 
ATOM   911  O O   . MET A 1 138 ? 18.547 12.186  38.169  1.00 28.62  ? 271 MET A O   1 
ATOM   912  C CB  . MET A 1 138 ? 21.741 13.048  38.287  1.00 34.39  ? 271 MET A CB  1 
ATOM   913  C CG  . MET A 1 138 ? 21.772 11.553  38.599  1.00 39.19  ? 271 MET A CG  1 
ATOM   914  S SD  . MET A 1 138 ? 23.319 11.016  39.373  1.00 45.99  ? 271 MET A SD  1 
ATOM   915  C CE  . MET A 1 138 ? 24.452 11.118  37.971  1.00 45.39  ? 271 MET A CE  1 
ATOM   916  N N   . ALA A 1 139 ? 19.034 13.975  39.444  1.00 28.42  ? 272 ALA A N   1 
ATOM   917  C CA  . ALA A 1 139 ? 17.914 13.770  40.353  1.00 26.89  ? 272 ALA A CA  1 
ATOM   918  C C   . ALA A 1 139 ? 16.568 13.790  39.627  1.00 26.51  ? 272 ALA A C   1 
ATOM   919  O O   . ALA A 1 139 ? 15.686 12.986  39.928  1.00 27.48  ? 272 ALA A O   1 
ATOM   920  C CB  . ALA A 1 139 ? 17.939 14.828  41.452  1.00 25.36  ? 272 ALA A CB  1 
ATOM   921  N N   . VAL A 1 140 ? 16.405 14.707  38.675  1.00 25.76  ? 273 VAL A N   1 
ATOM   922  C CA  . VAL A 1 140 ? 15.150 14.797  37.928  1.00 25.27  ? 273 VAL A CA  1 
ATOM   923  C C   . VAL A 1 140 ? 14.977 13.589  37.020  1.00 25.60  ? 273 VAL A C   1 
ATOM   924  O O   . VAL A 1 140 ? 13.878 13.052  36.898  1.00 25.49  ? 273 VAL A O   1 
ATOM   925  C CB  . VAL A 1 140 ? 15.082 16.088  37.075  1.00 25.71  ? 273 VAL A CB  1 
ATOM   926  C CG1 . VAL A 1 140 ? 13.860 16.045  36.159  1.00 24.78  ? 273 VAL A CG1 1 
ATOM   927  C CG2 . VAL A 1 140 ? 14.992 17.308  37.991  1.00 26.75  ? 273 VAL A CG2 1 
ATOM   928  N N   . ARG A 1 141 ? 16.059 13.167  36.376  1.00 27.43  ? 274 ARG A N   1 
ATOM   929  C CA  . ARG A 1 141 ? 16.000 12.001  35.499  1.00 30.01  ? 274 ARG A CA  1 
ATOM   930  C C   . ARG A 1 141 ? 15.599 10.779  36.315  1.00 30.74  ? 274 ARG A C   1 
ATOM   931  O O   . ARG A 1 141 ? 14.672 10.055  35.947  1.00 31.25  ? 274 ARG A O   1 
ATOM   932  C CB  . ARG A 1 141 ? 17.359 11.746  34.846  1.00 30.93  ? 274 ARG A CB  1 
ATOM   933  C CG  . ARG A 1 141 ? 17.834 12.863  33.939  1.00 30.52  ? 274 ARG A CG  1 
ATOM   934  C CD  . ARG A 1 141 ? 19.156 12.506  33.290  1.00 32.24  ? 274 ARG A CD  1 
ATOM   935  N NE  . ARG A 1 141 ? 19.566 13.530  32.341  1.00 33.02  ? 274 ARG A NE  1 
ATOM   936  C CZ  . ARG A 1 141 ? 20.684 14.238  32.440  1.00 33.47  ? 274 ARG A CZ  1 
ATOM   937  N NH1 . ARG A 1 141 ? 21.518 14.029  33.452  1.00 33.84  ? 274 ARG A NH1 1 
ATOM   938  N NH2 . ARG A 1 141 ? 20.960 15.165  31.532  1.00 32.08  ? 274 ARG A NH2 1 
ATOM   939  N N   . LEU A 1 142 ? 16.294 10.561  37.432  1.00 32.16  ? 275 LEU A N   1 
ATOM   940  C CA  . LEU A 1 142 ? 16.011 9.417   38.301  1.00 33.69  ? 275 LEU A CA  1 
ATOM   941  C C   . LEU A 1 142 ? 14.588 9.411   38.837  1.00 32.78  ? 275 LEU A C   1 
ATOM   942  O O   . LEU A 1 142 ? 14.010 8.347   39.046  1.00 33.36  ? 275 LEU A O   1 
ATOM   943  C CB  . LEU A 1 142 ? 16.994 9.375   39.478  1.00 34.91  ? 275 LEU A CB  1 
ATOM   944  C CG  . LEU A 1 142 ? 18.445 9.018   39.142  1.00 37.40  ? 275 LEU A CG  1 
ATOM   945  C CD1 . LEU A 1 142 ? 19.305 9.150   40.393  1.00 37.01  ? 275 LEU A CD1 1 
ATOM   946  C CD2 . LEU A 1 142 ? 18.514 7.597   38.592  1.00 37.52  ? 275 LEU A CD2 1 
ATOM   947  N N   . ALA A 1 143 ? 14.021 10.595  39.054  1.00 31.73  ? 276 ALA A N   1 
ATOM   948  C CA  . ALA A 1 143 ? 12.661 10.692  39.576  1.00 31.26  ? 276 ALA A CA  1 
ATOM   949  C C   . ALA A 1 143 ? 11.599 10.507  38.496  1.00 30.54  ? 276 ALA A C   1 
ATOM   950  O O   . ALA A 1 143 ? 10.403 10.546  38.782  1.00 31.74  ? 276 ALA A O   1 
ATOM   951  C CB  . ALA A 1 143 ? 12.462 12.037  40.275  1.00 32.32  ? 276 ALA A CB  1 
ATOM   952  N N   . GLY A 1 144 ? 12.031 10.297  37.258  1.00 29.84  ? 277 GLY A N   1 
ATOM   953  C CA  . GLY A 1 144 ? 11.082 10.122  36.174  1.00 28.74  ? 277 GLY A CA  1 
ATOM   954  C C   . GLY A 1 144 ? 10.527 11.450  35.677  1.00 27.80  ? 277 GLY A C   1 
ATOM   955  O O   . GLY A 1 144 ? 9.419  11.511  35.145  1.00 26.89  ? 277 GLY A O   1 
ATOM   956  N N   . GLY A 1 145 ? 11.300 12.518  35.846  1.00 26.11  ? 278 GLY A N   1 
ATOM   957  C CA  . GLY A 1 145 ? 10.848 13.828  35.409  1.00 27.03  ? 278 GLY A CA  1 
ATOM   958  C C   . GLY A 1 145 ? 10.643 13.963  33.910  1.00 25.71  ? 278 GLY A C   1 
ATOM   959  O O   . GLY A 1 145 ? 9.751  14.687  33.467  1.00 26.33  ? 278 GLY A O   1 
ATOM   960  N N   . LEU A 1 146 ? 11.464 13.273  33.124  1.00 25.41  ? 279 LEU A N   1 
ATOM   961  C CA  . LEU A 1 146 ? 11.361 13.330  31.670  1.00 25.65  ? 279 LEU A CA  1 
ATOM   962  C C   . LEU A 1 146 ? 9.999  12.857  31.168  1.00 26.96  ? 279 LEU A C   1 
ATOM   963  O O   . LEU A 1 146 ? 9.343  13.552  30.388  1.00 24.75  ? 279 LEU A O   1 
ATOM   964  C CB  . LEU A 1 146 ? 12.463 12.484  31.027  1.00 25.94  ? 279 LEU A CB  1 
ATOM   965  C CG  . LEU A 1 146 ? 13.882 13.057  31.100  1.00 28.71  ? 279 LEU A CG  1 
ATOM   966  C CD1 . LEU A 1 146 ? 14.886 11.991  30.685  1.00 28.75  ? 279 LEU A CD1 1 
ATOM   967  C CD2 . LEU A 1 146 ? 13.991 14.286  30.200  1.00 25.62  ? 279 LEU A CD2 1 
ATOM   968  N N   . GLN A 1 147 ? 9.578  11.675  31.613  1.00 27.48  ? 280 GLN A N   1 
ATOM   969  C CA  . GLN A 1 147 ? 8.292  11.125  31.200  1.00 27.29  ? 280 GLN A CA  1 
ATOM   970  C C   . GLN A 1 147 ? 7.140  12.047  31.613  1.00 27.57  ? 280 GLN A C   1 
ATOM   971  O O   . GLN A 1 147 ? 6.175  12.219  30.869  1.00 27.21  ? 280 GLN A O   1 
ATOM   972  C CB  . GLN A 1 147 ? 8.085  9.728   31.800  1.00 27.98  ? 280 GLN A CB  1 
ATOM   973  C CG  . GLN A 1 147 ? 9.082  8.675   31.303  1.00 28.38  ? 280 GLN A CG  1 
ATOM   974  C CD  . GLN A 1 147 ? 10.366 8.625   32.122  1.00 29.29  ? 280 GLN A CD  1 
ATOM   975  O OE1 . GLN A 1 147 ? 10.778 9.614   32.731  1.00 29.81  ? 280 GLN A OE1 1 
ATOM   976  N NE2 . GLN A 1 147 ? 11.014 7.467   32.123  1.00 31.44  ? 280 GLN A NE2 1 
ATOM   977  N N   . LYS A 1 148 ? 7.247  12.641  32.796  1.00 27.97  ? 281 LYS A N   1 
ATOM   978  C CA  . LYS A 1 148 ? 6.216  13.550  33.293  1.00 28.26  ? 281 LYS A CA  1 
ATOM   979  C C   . LYS A 1 148 ? 6.131  14.814  32.438  1.00 27.12  ? 281 LYS A C   1 
ATOM   980  O O   . LYS A 1 148 ? 5.042  15.265  32.082  1.00 27.54  ? 281 LYS A O   1 
ATOM   981  C CB  . LYS A 1 148 ? 6.523  13.955  34.736  1.00 30.17  ? 281 LYS A CB  1 
ATOM   982  C CG  . LYS A 1 148 ? 6.386  12.836  35.753  1.00 37.64  ? 281 LYS A CG  1 
ATOM   983  C CD  . LYS A 1 148 ? 4.932  12.471  35.962  1.00 40.02  ? 281 LYS A CD  1 
ATOM   984  C CE  . LYS A 1 148 ? 4.759  11.534  37.144  1.00 43.04  ? 281 LYS A CE  1 
ATOM   985  N NZ  . LYS A 1 148 ? 3.318  11.240  37.368  1.00 46.83  ? 281 LYS A NZ  1 
ATOM   986  N N   . MET A 1 149 ? 7.289  15.386  32.121  1.00 25.12  ? 282 MET A N   1 
ATOM   987  C CA  . MET A 1 149 ? 7.346  16.606  31.321  1.00 26.89  ? 282 MET A CA  1 
ATOM   988  C C   . MET A 1 149 ? 6.800  16.414  29.910  1.00 25.48  ? 282 MET A C   1 
ATOM   989  O O   . MET A 1 149 ? 6.046  17.254  29.411  1.00 23.46  ? 282 MET A O   1 
ATOM   990  C CB  . MET A 1 149 ? 8.783  17.130  31.270  1.00 22.55  ? 282 MET A CB  1 
ATOM   991  C CG  . MET A 1 149 ? 9.259  17.644  32.620  1.00 24.05  ? 282 MET A CG  1 
ATOM   992  S SD  . MET A 1 149 ? 10.976 18.152  32.628  1.00 25.22  ? 282 MET A SD  1 
ATOM   993  C CE  . MET A 1 149 ? 11.157 18.619  34.360  1.00 20.92  ? 282 MET A CE  1 
ATOM   994  N N   . VAL A 1 150 ? 7.169  15.309  29.270  1.00 24.91  ? 283 VAL A N   1 
ATOM   995  C CA  . VAL A 1 150 ? 6.679  15.042  27.924  1.00 25.28  ? 283 VAL A CA  1 
ATOM   996  C C   . VAL A 1 150 ? 5.153  14.921  27.933  1.00 26.51  ? 283 VAL A C   1 
ATOM   997  O O   . VAL A 1 150 ? 4.477  15.422  27.033  1.00 26.61  ? 283 VAL A O   1 
ATOM   998  C CB  . VAL A 1 150 ? 7.292  13.741  27.342  1.00 25.05  ? 283 VAL A CB  1 
ATOM   999  C CG1 . VAL A 1 150 ? 6.586  13.364  26.037  1.00 24.53  ? 283 VAL A CG1 1 
ATOM   1000 C CG2 . VAL A 1 150 ? 8.787  13.943  27.071  1.00 22.09  ? 283 VAL A CG2 1 
ATOM   1001 N N   . ALA A 1 151 ? 4.617  14.269  28.960  1.00 27.34  ? 284 ALA A N   1 
ATOM   1002 C CA  . ALA A 1 151 ? 3.172  14.073  29.077  1.00 28.81  ? 284 ALA A CA  1 
ATOM   1003 C C   . ALA A 1 151 ? 2.405  15.384  29.266  1.00 30.39  ? 284 ALA A C   1 
ATOM   1004 O O   . ALA A 1 151 ? 1.216  15.467  28.958  1.00 30.92  ? 284 ALA A O   1 
ATOM   1005 C CB  . ALA A 1 151 ? 2.870  13.119  30.234  1.00 28.41  ? 284 ALA A CB  1 
ATOM   1006 N N   . LEU A 1 152 ? 3.082  16.407  29.773  1.00 29.28  ? 285 LEU A N   1 
ATOM   1007 C CA  . LEU A 1 152 ? 2.436  17.696  29.991  1.00 28.76  ? 285 LEU A CA  1 
ATOM   1008 C C   . LEU A 1 152 ? 2.422  18.568  28.737  1.00 28.13  ? 285 LEU A C   1 
ATOM   1009 O O   . LEU A 1 152 ? 1.807  19.641  28.723  1.00 25.79  ? 285 LEU A O   1 
ATOM   1010 C CB  . LEU A 1 152 ? 3.144  18.444  31.126  1.00 28.59  ? 285 LEU A CB  1 
ATOM   1011 C CG  . LEU A 1 152 ? 3.040  17.767  32.495  1.00 30.56  ? 285 LEU A CG  1 
ATOM   1012 C CD1 . LEU A 1 152 ? 3.965  18.450  33.497  1.00 29.63  ? 285 LEU A CD1 1 
ATOM   1013 C CD2 . LEU A 1 152 ? 1.587  17.809  32.960  1.00 31.28  ? 285 LEU A CD2 1 
ATOM   1014 N N   . LEU A 1 153 ? 3.094  18.108  27.684  1.00 27.50  ? 286 LEU A N   1 
ATOM   1015 C CA  . LEU A 1 153 ? 3.169  18.878  26.448  1.00 26.69  ? 286 LEU A CA  1 
ATOM   1016 C C   . LEU A 1 153 ? 1.840  19.013  25.722  1.00 26.23  ? 286 LEU A C   1 
ATOM   1017 O O   . LEU A 1 153 ? 1.767  19.692  24.703  1.00 26.20  ? 286 LEU A O   1 
ATOM   1018 C CB  . LEU A 1 153 ? 4.224  18.284  25.502  1.00 24.56  ? 286 LEU A CB  1 
ATOM   1019 C CG  . LEU A 1 153 ? 5.665  18.291  26.027  1.00 24.63  ? 286 LEU A CG  1 
ATOM   1020 C CD1 . LEU A 1 153 ? 6.598  17.802  24.936  1.00 23.27  ? 286 LEU A CD1 1 
ATOM   1021 C CD2 . LEU A 1 153 ? 6.070  19.694  26.465  1.00 25.60  ? 286 LEU A CD2 1 
ATOM   1022 N N   . ASN A 1 154 ? 0.789  18.373  26.233  1.00 26.87  ? 287 ASN A N   1 
ATOM   1023 C CA  . ASN A 1 154 ? -0.512 18.497  25.593  1.00 29.12  ? 287 ASN A CA  1 
ATOM   1024 C C   . ASN A 1 154 ? -1.338 19.623  26.213  1.00 28.94  ? 287 ASN A C   1 
ATOM   1025 O O   . ASN A 1 154 ? -2.478 19.853  25.810  1.00 27.96  ? 287 ASN A O   1 
ATOM   1026 C CB  . ASN A 1 154 ? -1.295 17.178  25.642  1.00 32.17  ? 287 ASN A CB  1 
ATOM   1027 C CG  . ASN A 1 154 ? -1.624 16.734  27.053  1.00 34.42  ? 287 ASN A CG  1 
ATOM   1028 O OD1 . ASN A 1 154 ? -2.422 15.818  27.248  1.00 39.27  ? 287 ASN A OD1 1 
ATOM   1029 N ND2 . ASN A 1 154 ? -1.009 17.369  28.041  1.00 33.49  ? 287 ASN A ND2 1 
ATOM   1030 N N   . LYS A 1 155 ? -0.770 20.323  27.195  1.00 28.03  ? 288 LYS A N   1 
ATOM   1031 C CA  . LYS A 1 155 ? -1.471 21.446  27.813  1.00 27.32  ? 288 LYS A CA  1 
ATOM   1032 C C   . LYS A 1 155 ? -1.480 22.584  26.792  1.00 27.28  ? 288 LYS A C   1 
ATOM   1033 O O   . LYS A 1 155 ? -0.745 22.536  25.798  1.00 26.06  ? 288 LYS A O   1 
ATOM   1034 C CB  . LYS A 1 155 ? -0.770 21.908  29.098  1.00 29.71  ? 288 LYS A CB  1 
ATOM   1035 C CG  . LYS A 1 155 ? -0.888 20.949  30.289  1.00 35.09  ? 288 LYS A CG  1 
ATOM   1036 C CD  . LYS A 1 155 ? -2.333 20.550  30.545  1.00 38.87  ? 288 LYS A CD  1 
ATOM   1037 C CE  . LYS A 1 155 ? -2.523 19.921  31.925  1.00 42.14  ? 288 LYS A CE  1 
ATOM   1038 N NZ  . LYS A 1 155 ? -2.493 20.964  32.991  1.00 43.41  ? 288 LYS A NZ  1 
ATOM   1039 N N   . THR A 1 156 ? -2.290 23.612  27.036  1.00 25.16  ? 289 THR A N   1 
ATOM   1040 C CA  . THR A 1 156 ? -2.381 24.723  26.097  1.00 26.12  ? 289 THR A CA  1 
ATOM   1041 C C   . THR A 1 156 ? -1.823 26.062  26.571  1.00 25.53  ? 289 THR A C   1 
ATOM   1042 O O   . THR A 1 156 ? -1.779 27.015  25.795  1.00 27.74  ? 289 THR A O   1 
ATOM   1043 C CB  . THR A 1 156 ? -3.841 24.942  25.646  1.00 26.69  ? 289 THR A CB  1 
ATOM   1044 O OG1 . THR A 1 156 ? -4.656 25.241  26.787  1.00 26.94  ? 289 THR A OG1 1 
ATOM   1045 C CG2 . THR A 1 156 ? -4.376 23.686  24.950  1.00 25.66  ? 289 THR A CG2 1 
ATOM   1046 N N   . ASN A 1 157 ? -1.419 26.150  27.835  1.00 24.36  ? 290 ASN A N   1 
ATOM   1047 C CA  . ASN A 1 157 ? -0.849 27.394  28.350  1.00 23.52  ? 290 ASN A CA  1 
ATOM   1048 C C   . ASN A 1 157 ? 0.552  27.512  27.741  1.00 23.80  ? 290 ASN A C   1 
ATOM   1049 O O   . ASN A 1 157 ? 1.446  26.721  28.060  1.00 22.15  ? 290 ASN A O   1 
ATOM   1050 C CB  . ASN A 1 157 ? -0.786 27.354  29.880  1.00 21.75  ? 290 ASN A CB  1 
ATOM   1051 C CG  . ASN A 1 157 ? -0.261 28.645  30.476  1.00 24.01  ? 290 ASN A CG  1 
ATOM   1052 O OD1 . ASN A 1 157 ? 0.883  29.033  30.234  1.00 23.44  ? 290 ASN A OD1 1 
ATOM   1053 N ND2 . ASN A 1 157 ? -1.099 29.326  31.259  1.00 24.13  ? 290 ASN A ND2 1 
ATOM   1054 N N   . VAL A 1 158 ? 0.740  28.496  26.863  1.00 23.67  ? 291 VAL A N   1 
ATOM   1055 C CA  . VAL A 1 158 ? 2.019  28.660  26.177  1.00 23.96  ? 291 VAL A CA  1 
ATOM   1056 C C   . VAL A 1 158 ? 3.214  29.050  27.036  1.00 24.83  ? 291 VAL A C   1 
ATOM   1057 O O   . VAL A 1 158 ? 4.347  28.716  26.693  1.00 24.39  ? 291 VAL A O   1 
ATOM   1058 C CB  . VAL A 1 158 ? 1.910  29.655  24.987  1.00 23.50  ? 291 VAL A CB  1 
ATOM   1059 C CG1 . VAL A 1 158 ? 0.985  29.075  23.914  1.00 21.47  ? 291 VAL A CG1 1 
ATOM   1060 C CG2 . VAL A 1 158 ? 1.412  31.011  25.462  1.00 21.01  ? 291 VAL A CG2 1 
ATOM   1061 N N   . LYS A 1 159 ? 2.979  29.756  28.137  1.00 24.24  ? 292 LYS A N   1 
ATOM   1062 C CA  . LYS A 1 159 ? 4.085  30.135  29.012  1.00 23.86  ? 292 LYS A CA  1 
ATOM   1063 C C   . LYS A 1 159 ? 4.511  28.903  29.806  1.00 22.69  ? 292 LYS A C   1 
ATOM   1064 O O   . LYS A 1 159 ? 5.699  28.707  30.091  1.00 20.08  ? 292 LYS A O   1 
ATOM   1065 C CB  . LYS A 1 159 ? 3.675  31.275  29.946  1.00 25.04  ? 292 LYS A CB  1 
ATOM   1066 C CG  . LYS A 1 159 ? 3.604  32.619  29.231  1.00 28.71  ? 292 LYS A CG  1 
ATOM   1067 C CD  . LYS A 1 159 ? 3.191  33.754  30.155  1.00 32.34  ? 292 LYS A CD  1 
ATOM   1068 C CE  . LYS A 1 159 ? 3.175  35.076  29.398  1.00 33.16  ? 292 LYS A CE  1 
ATOM   1069 N NZ  . LYS A 1 159 ? 2.672  36.189  30.248  1.00 38.77  ? 292 LYS A NZ  1 
ATOM   1070 N N   . PHE A 1 160 ? 3.535  28.070  30.148  1.00 21.72  ? 293 PHE A N   1 
ATOM   1071 C CA  . PHE A 1 160 ? 3.806  26.831  30.873  1.00 22.10  ? 293 PHE A CA  1 
ATOM   1072 C C   . PHE A 1 160 ? 4.596  25.894  29.955  1.00 21.88  ? 293 PHE A C   1 
ATOM   1073 O O   . PHE A 1 160 ? 5.576  25.279  30.377  1.00 21.60  ? 293 PHE A O   1 
ATOM   1074 C CB  . PHE A 1 160 ? 2.496  26.147  31.288  1.00 22.65  ? 293 PHE A CB  1 
ATOM   1075 C CG  . PHE A 1 160 ? 2.687  24.743  31.805  1.00 23.09  ? 293 PHE A CG  1 
ATOM   1076 C CD1 . PHE A 1 160 ? 3.115  24.514  33.109  1.00 24.95  ? 293 PHE A CD1 1 
ATOM   1077 C CD2 . PHE A 1 160 ? 2.471  23.651  30.974  1.00 22.75  ? 293 PHE A CD2 1 
ATOM   1078 C CE1 . PHE A 1 160 ? 3.329  23.217  33.573  1.00 22.61  ? 293 PHE A CE1 1 
ATOM   1079 C CE2 . PHE A 1 160 ? 2.684  22.346  31.429  1.00 24.63  ? 293 PHE A CE2 1 
ATOM   1080 C CZ  . PHE A 1 160 ? 3.112  22.133  32.735  1.00 24.23  ? 293 PHE A CZ  1 
ATOM   1081 N N   . LEU A 1 161 ? 4.163  25.788  28.699  1.00 20.87  ? 294 LEU A N   1 
ATOM   1082 C CA  . LEU A 1 161 ? 4.838  24.922  27.725  1.00 20.68  ? 294 LEU A CA  1 
ATOM   1083 C C   . LEU A 1 161 ? 6.267  25.386  27.446  1.00 19.64  ? 294 LEU A C   1 
ATOM   1084 O O   . LEU A 1 161 ? 7.173  24.566  27.259  1.00 21.51  ? 294 LEU A O   1 
ATOM   1085 C CB  . LEU A 1 161 ? 4.050  24.877  26.405  1.00 18.88  ? 294 LEU A CB  1 
ATOM   1086 C CG  . LEU A 1 161 ? 2.690  24.170  26.452  1.00 19.83  ? 294 LEU A CG  1 
ATOM   1087 C CD1 . LEU A 1 161 ? 2.028  24.263  25.090  1.00 19.32  ? 294 LEU A CD1 1 
ATOM   1088 C CD2 . LEU A 1 161 ? 2.867  22.708  26.853  1.00 19.39  ? 294 LEU A CD2 1 
ATOM   1089 N N   . ALA A 1 162 ? 6.466  26.699  27.407  1.00 18.47  ? 295 ALA A N   1 
ATOM   1090 C CA  . ALA A 1 162 ? 7.795  27.251  27.160  1.00 18.83  ? 295 ALA A CA  1 
ATOM   1091 C C   . ALA A 1 162 ? 8.767  26.808  28.268  1.00 19.96  ? 295 ALA A C   1 
ATOM   1092 O O   . ALA A 1 162 ? 9.906  26.417  27.993  1.00 19.50  ? 295 ALA A O   1 
ATOM   1093 C CB  . ALA A 1 162 ? 7.722  28.773  27.100  1.00 19.85  ? 295 ALA A CB  1 
ATOM   1094 N N   . ILE A 1 163 ? 8.314  26.857  29.518  1.00 20.14  ? 296 ILE A N   1 
ATOM   1095 C CA  . ILE A 1 163 ? 9.162  26.449  30.634  1.00 22.65  ? 296 ILE A CA  1 
ATOM   1096 C C   . ILE A 1 163 ? 9.409  24.940  30.606  1.00 22.95  ? 296 ILE A C   1 
ATOM   1097 O O   . ILE A 1 163 ? 10.541 24.481  30.786  1.00 23.31  ? 296 ILE A O   1 
ATOM   1098 C CB  . ILE A 1 163 ? 8.527  26.829  31.991  1.00 25.79  ? 296 ILE A CB  1 
ATOM   1099 C CG1 . ILE A 1 163 ? 8.448  28.352  32.111  1.00 27.63  ? 296 ILE A CG1 1 
ATOM   1100 C CG2 . ILE A 1 163 ? 9.367  26.271  33.144  1.00 25.50  ? 296 ILE A CG2 1 
ATOM   1101 C CD1 . ILE A 1 163 ? 7.723  28.820  33.345  1.00 31.26  ? 296 ILE A CD1 1 
ATOM   1102 N N   . THR A 1 164 ? 8.351  24.173  30.364  1.00 21.32  ? 297 THR A N   1 
ATOM   1103 C CA  . THR A 1 164 ? 8.462  22.721  30.326  1.00 21.45  ? 297 THR A CA  1 
ATOM   1104 C C   . THR A 1 164 ? 9.422  22.263  29.237  1.00 20.67  ? 297 THR A C   1 
ATOM   1105 O O   . THR A 1 164 ? 10.288 21.420  29.488  1.00 20.93  ? 297 THR A O   1 
ATOM   1106 C CB  . THR A 1 164 ? 7.081  22.064  30.107  1.00 19.72  ? 297 THR A CB  1 
ATOM   1107 O OG1 . THR A 1 164 ? 6.206  22.444  31.175  1.00 20.58  ? 297 THR A OG1 1 
ATOM   1108 C CG2 . THR A 1 164 ? 7.200  20.546  30.093  1.00 20.92  ? 297 THR A CG2 1 
ATOM   1109 N N   . THR A 1 165 ? 9.273  22.815  28.035  1.00 18.97  ? 298 THR A N   1 
ATOM   1110 C CA  . THR A 1 165 ? 10.154 22.445  26.934  1.00 19.90  ? 298 THR A CA  1 
ATOM   1111 C C   . THR A 1 165 ? 11.591 22.872  27.219  1.00 20.48  ? 298 THR A C   1 
ATOM   1112 O O   . THR A 1 165 ? 12.533 22.196  26.810  1.00 21.18  ? 298 THR A O   1 
ATOM   1113 C CB  . THR A 1 165 ? 9.694  23.055  25.570  1.00 20.33  ? 298 THR A CB  1 
ATOM   1114 O OG1 . THR A 1 165 ? 9.450  24.460  25.714  1.00 21.01  ? 298 THR A OG1 1 
ATOM   1115 C CG2 . THR A 1 165 ? 8.430  22.373  25.078  1.00 18.31  ? 298 THR A CG2 1 
ATOM   1116 N N   . ASP A 1 166 ? 11.777 23.980  27.929  1.00 20.72  ? 299 ASP A N   1 
ATOM   1117 C CA  . ASP A 1 166 ? 13.143 24.403  28.216  1.00 22.47  ? 299 ASP A CA  1 
ATOM   1118 C C   . ASP A 1 166 ? 13.772 23.408  29.185  1.00 22.48  ? 299 ASP A C   1 
ATOM   1119 O O   . ASP A 1 166 ? 14.966 23.138  29.103  1.00 22.61  ? 299 ASP A O   1 
ATOM   1120 C CB  . ASP A 1 166 ? 13.199 25.815  28.811  1.00 21.35  ? 299 ASP A CB  1 
ATOM   1121 C CG  . ASP A 1 166 ? 14.592 26.425  28.707  1.00 22.71  ? 299 ASP A CG  1 
ATOM   1122 O OD1 . ASP A 1 166 ? 15.080 27.002  29.698  1.00 25.50  ? 299 ASP A OD1 1 
ATOM   1123 O OD2 . ASP A 1 166 ? 15.205 26.324  27.625  1.00 24.39  ? 299 ASP A OD2 1 
ATOM   1124 N N   . CYS A 1 167 ? 12.967 22.865  30.098  1.00 20.70  ? 300 CYS A N   1 
ATOM   1125 C CA  . CYS A 1 167 ? 13.472 21.877  31.051  1.00 20.76  ? 300 CYS A CA  1 
ATOM   1126 C C   . CYS A 1 167 ? 13.956 20.662  30.269  1.00 18.89  ? 300 CYS A C   1 
ATOM   1127 O O   . CYS A 1 167 ? 15.013 20.104  30.557  1.00 20.43  ? 300 CYS A O   1 
ATOM   1128 C CB  . CYS A 1 167 ? 12.369 21.438  32.031  1.00 20.47  ? 300 CYS A CB  1 
ATOM   1129 S SG  . CYS A 1 167 ? 11.936 22.650  33.320  1.00 22.65  ? 300 CYS A SG  1 
ATOM   1130 N N   . LEU A 1 168 ? 13.171 20.252  29.278  1.00 18.09  ? 301 LEU A N   1 
ATOM   1131 C CA  . LEU A 1 168 ? 13.517 19.106  28.444  1.00 20.02  ? 301 LEU A CA  1 
ATOM   1132 C C   . LEU A 1 168 ? 14.815 19.350  27.666  1.00 20.65  ? 301 LEU A C   1 
ATOM   1133 O O   . LEU A 1 168 ? 15.603 18.429  27.446  1.00 22.40  ? 301 LEU A O   1 
ATOM   1134 C CB  . LEU A 1 168 ? 12.369 18.804  27.472  1.00 20.79  ? 301 LEU A CB  1 
ATOM   1135 C CG  . LEU A 1 168 ? 11.107 18.199  28.103  1.00 20.02  ? 301 LEU A CG  1 
ATOM   1136 C CD1 . LEU A 1 168 ? 9.977  18.138  27.078  1.00 18.73  ? 301 LEU A CD1 1 
ATOM   1137 C CD2 . LEU A 1 168 ? 11.428 16.804  28.623  1.00 22.70  ? 301 LEU A CD2 1 
ATOM   1138 N N   . GLN A 1 169 ? 15.032 20.595  27.251  1.00 20.86  ? 302 GLN A N   1 
ATOM   1139 C CA  . GLN A 1 169 ? 16.230 20.966  26.508  1.00 22.66  ? 302 GLN A CA  1 
ATOM   1140 C C   . GLN A 1 169 ? 17.453 20.775  27.413  1.00 22.51  ? 302 GLN A C   1 
ATOM   1141 O O   . GLN A 1 169 ? 18.448 20.170  27.017  1.00 21.86  ? 302 GLN A O   1 
ATOM   1142 C CB  . GLN A 1 169 ? 16.119 22.432  26.061  1.00 24.97  ? 302 GLN A CB  1 
ATOM   1143 C CG  . GLN A 1 169 ? 17.198 22.927  25.102  1.00 27.73  ? 302 GLN A CG  1 
ATOM   1144 C CD  . GLN A 1 169 ? 18.536 23.162  25.779  1.00 30.04  ? 302 GLN A CD  1 
ATOM   1145 O OE1 . GLN A 1 169 ? 18.595 23.585  26.930  1.00 30.30  ? 302 GLN A OE1 1 
ATOM   1146 N NE2 . GLN A 1 169 ? 19.619 22.909  25.054  1.00 32.96  ? 302 GLN A NE2 1 
ATOM   1147 N N   . ILE A 1 170 ? 17.358 21.288  28.634  1.00 22.04  ? 303 ILE A N   1 
ATOM   1148 C CA  . ILE A 1 170 ? 18.439 21.189  29.613  1.00 23.39  ? 303 ILE A CA  1 
ATOM   1149 C C   . ILE A 1 170 ? 18.763 19.736  29.966  1.00 23.29  ? 303 ILE A C   1 
ATOM   1150 O O   . ILE A 1 170 ? 19.925 19.364  30.107  1.00 24.02  ? 303 ILE A O   1 
ATOM   1151 C CB  . ILE A 1 170 ? 18.062 21.940  30.906  1.00 22.95  ? 303 ILE A CB  1 
ATOM   1152 C CG1 . ILE A 1 170 ? 17.871 23.429  30.594  1.00 23.10  ? 303 ILE A CG1 1 
ATOM   1153 C CG2 . ILE A 1 170 ? 19.144 21.742  31.977  1.00 23.27  ? 303 ILE A CG2 1 
ATOM   1154 C CD1 . ILE A 1 170 ? 17.253 24.207  31.723  1.00 21.46  ? 303 ILE A CD1 1 
ATOM   1155 N N   . LEU A 1 171 ? 17.725 18.921  30.102  1.00 23.35  ? 304 LEU A N   1 
ATOM   1156 C CA  . LEU A 1 171 ? 17.887 17.515  30.461  1.00 24.26  ? 304 LEU A CA  1 
ATOM   1157 C C   . LEU A 1 171 ? 18.425 16.656  29.330  1.00 25.64  ? 304 LEU A C   1 
ATOM   1158 O O   . LEU A 1 171 ? 19.136 15.674  29.563  1.00 26.03  ? 304 LEU A O   1 
ATOM   1159 C CB  . LEU A 1 171 ? 16.546 16.945  30.930  1.00 22.19  ? 304 LEU A CB  1 
ATOM   1160 C CG  . LEU A 1 171 ? 16.084 17.382  32.323  1.00 21.74  ? 304 LEU A CG  1 
ATOM   1161 C CD1 . LEU A 1 171 ? 14.618 17.029  32.516  1.00 19.76  ? 304 LEU A CD1 1 
ATOM   1162 C CD2 . LEU A 1 171 ? 16.961 16.701  33.386  1.00 22.60  ? 304 LEU A CD2 1 
ATOM   1163 N N   . ALA A 1 172 ? 18.083 17.031  28.101  1.00 25.68  ? 305 ALA A N   1 
ATOM   1164 C CA  . ALA A 1 172 ? 18.497 16.275  26.933  1.00 23.86  ? 305 ALA A CA  1 
ATOM   1165 C C   . ALA A 1 172 ? 19.871 16.654  26.405  1.00 25.55  ? 305 ALA A C   1 
ATOM   1166 O O   . ALA A 1 172 ? 20.572 15.815  25.846  1.00 23.55  ? 305 ALA A O   1 
ATOM   1167 C CB  . ALA A 1 172 ? 17.454 16.426  25.826  1.00 21.95  ? 305 ALA A CB  1 
ATOM   1168 N N   . TYR A 1 173 ? 20.261 17.911  26.580  1.00 26.89  ? 306 TYR A N   1 
ATOM   1169 C CA  . TYR A 1 173 ? 21.550 18.363  26.078  1.00 30.80  ? 306 TYR A CA  1 
ATOM   1170 C C   . TYR A 1 173 ? 22.716 17.474  26.503  1.00 33.42  ? 306 TYR A C   1 
ATOM   1171 O O   . TYR A 1 173 ? 22.970 17.294  27.692  1.00 34.58  ? 306 TYR A O   1 
ATOM   1172 C CB  . TYR A 1 173 ? 21.835 19.789  26.530  1.00 31.81  ? 306 TYR A CB  1 
ATOM   1173 C CG  . TYR A 1 173 ? 22.990 20.405  25.782  1.00 37.30  ? 306 TYR A CG  1 
ATOM   1174 C CD1 . TYR A 1 173 ? 22.861 20.752  24.440  1.00 40.12  ? 306 TYR A CD1 1 
ATOM   1175 C CD2 . TYR A 1 173 ? 24.222 20.615  26.404  1.00 39.89  ? 306 TYR A CD2 1 
ATOM   1176 C CE1 . TYR A 1 173 ? 23.931 21.294  23.728  1.00 44.04  ? 306 TYR A CE1 1 
ATOM   1177 C CE2 . TYR A 1 173 ? 25.301 21.156  25.701  1.00 42.32  ? 306 TYR A CE2 1 
ATOM   1178 C CZ  . TYR A 1 173 ? 25.145 21.492  24.364  1.00 44.26  ? 306 TYR A CZ  1 
ATOM   1179 O OH  . TYR A 1 173 ? 26.198 22.024  23.658  1.00 47.94  ? 306 TYR A OH  1 
ATOM   1180 N N   . GLY A 1 174 ? 23.427 16.932  25.520  1.00 35.66  ? 307 GLY A N   1 
ATOM   1181 C CA  . GLY A 1 174 ? 24.569 16.082  25.806  1.00 36.79  ? 307 GLY A CA  1 
ATOM   1182 C C   . GLY A 1 174 ? 24.280 14.865  26.664  1.00 39.05  ? 307 GLY A C   1 
ATOM   1183 O O   . GLY A 1 174 ? 25.160 14.397  27.388  1.00 41.21  ? 307 GLY A O   1 
ATOM   1184 N N   . ASN A 1 175 ? 23.058 14.346  26.595  1.00 37.73  ? 308 ASN A N   1 
ATOM   1185 C CA  . ASN A 1 175 ? 22.696 13.168  27.377  1.00 35.90  ? 308 ASN A CA  1 
ATOM   1186 C C   . ASN A 1 175 ? 21.830 12.251  26.515  1.00 34.96  ? 308 ASN A C   1 
ATOM   1187 O O   . ASN A 1 175 ? 20.610 12.408  26.447  1.00 32.76  ? 308 ASN A O   1 
ATOM   1188 C CB  . ASN A 1 175 ? 21.951 13.588  28.654  1.00 35.48  ? 308 ASN A CB  1 
ATOM   1189 C CG  . ASN A 1 175 ? 21.788 12.443  29.646  1.00 34.47  ? 308 ASN A CG  1 
ATOM   1190 O OD1 . ASN A 1 175 ? 20.891 11.610  29.519  1.00 32.15  ? 308 ASN A OD1 1 
ATOM   1191 N ND2 . ASN A 1 175 ? 22.668 12.397  30.639  1.00 35.34  ? 308 ASN A ND2 1 
ATOM   1192 N N   . GLN A 1 176 ? 22.484 11.301  25.852  1.00 33.78  ? 309 GLN A N   1 
ATOM   1193 C CA  . GLN A 1 176 ? 21.821 10.354  24.964  1.00 34.37  ? 309 GLN A CA  1 
ATOM   1194 C C   . GLN A 1 176 ? 20.722 9.555   25.653  1.00 33.60  ? 309 GLN A C   1 
ATOM   1195 O O   . GLN A 1 176 ? 19.675 9.296   25.065  1.00 34.62  ? 309 GLN A O   1 
ATOM   1196 C CB  . GLN A 1 176 ? 22.856 9.397   24.353  1.00 37.06  ? 309 GLN A CB  1 
ATOM   1197 C CG  . GLN A 1 176 ? 22.279 8.376   23.372  1.00 38.56  ? 309 GLN A CG  1 
ATOM   1198 C CD  . GLN A 1 176 ? 21.538 9.026   22.213  1.00 39.98  ? 309 GLN A CD  1 
ATOM   1199 O OE1 . GLN A 1 176 ? 22.063 9.914   21.544  1.00 40.48  ? 309 GLN A OE1 1 
ATOM   1200 N NE2 . GLN A 1 176 ? 20.312 8.579   21.969  1.00 41.57  ? 309 GLN A NE2 1 
ATOM   1201 N N   . GLU A 1 177 ? 20.959 9.163   26.896  1.00 33.10  ? 310 GLU A N   1 
ATOM   1202 C CA  . GLU A 1 177 ? 19.970 8.396   27.646  1.00 34.09  ? 310 GLU A CA  1 
ATOM   1203 C C   . GLU A 1 177 ? 18.653 9.170   27.751  1.00 32.46  ? 310 GLU A C   1 
ATOM   1204 O O   . GLU A 1 177 ? 17.572 8.604   27.583  1.00 31.11  ? 310 GLU A O   1 
ATOM   1205 C CB  . GLU A 1 177 ? 20.501 8.088   29.046  1.00 37.52  ? 310 GLU A CB  1 
ATOM   1206 C CG  . GLU A 1 177 ? 19.554 7.280   29.912  1.00 41.91  ? 310 GLU A CG  1 
ATOM   1207 C CD  . GLU A 1 177 ? 20.115 7.030   31.299  1.00 45.71  ? 310 GLU A CD  1 
ATOM   1208 O OE1 . GLU A 1 177 ? 20.372 8.019   32.026  1.00 46.22  ? 310 GLU A OE1 1 
ATOM   1209 O OE2 . GLU A 1 177 ? 20.302 5.847   31.658  1.00 45.47  ? 310 GLU A OE2 1 
ATOM   1210 N N   . SER A 1 178 ? 18.751 10.466  28.027  1.00 29.87  ? 311 SER A N   1 
ATOM   1211 C CA  . SER A 1 178 ? 17.563 11.305  28.148  1.00 27.58  ? 311 SER A CA  1 
ATOM   1212 C C   . SER A 1 178 ? 16.866 11.466  26.798  1.00 26.28  ? 311 SER A C   1 
ATOM   1213 O O   . SER A 1 178 ? 15.640 11.524  26.727  1.00 26.41  ? 311 SER A O   1 
ATOM   1214 C CB  . SER A 1 178 ? 17.938 12.675  28.717  1.00 25.97  ? 311 SER A CB  1 
ATOM   1215 O OG  . SER A 1 178 ? 18.407 12.560  30.052  1.00 26.80  ? 311 SER A OG  1 
ATOM   1216 N N   . LYS A 1 179 ? 17.648 11.529  25.725  1.00 25.97  ? 312 LYS A N   1 
ATOM   1217 C CA  . LYS A 1 179 ? 17.068 11.675  24.397  1.00 26.10  ? 312 LYS A CA  1 
ATOM   1218 C C   . LYS A 1 179 ? 16.231 10.452  24.043  1.00 26.50  ? 312 LYS A C   1 
ATOM   1219 O O   . LYS A 1 179 ? 15.171 10.572  23.435  1.00 25.96  ? 312 LYS A O   1 
ATOM   1220 C CB  . LYS A 1 179 ? 18.164 11.870  23.346  1.00 26.10  ? 312 LYS A CB  1 
ATOM   1221 C CG  . LYS A 1 179 ? 19.007 13.122  23.544  1.00 24.25  ? 312 LYS A CG  1 
ATOM   1222 C CD  . LYS A 1 179 ? 19.978 13.319  22.388  1.00 24.21  ? 312 LYS A CD  1 
ATOM   1223 C CE  . LYS A 1 179 ? 20.927 14.469  22.674  1.00 23.83  ? 312 LYS A CE  1 
ATOM   1224 N NZ  . LYS A 1 179 ? 21.779 14.781  21.498  1.00 28.17  ? 312 LYS A NZ  1 
ATOM   1225 N N   . LEU A 1 180 ? 16.711 9.272   24.420  1.00 27.23  ? 313 LEU A N   1 
ATOM   1226 C CA  . LEU A 1 180 ? 15.985 8.042   24.127  1.00 27.82  ? 313 LEU A CA  1 
ATOM   1227 C C   . LEU A 1 180 ? 14.707 7.932   24.945  1.00 27.10  ? 313 LEU A C   1 
ATOM   1228 O O   . LEU A 1 180 ? 13.694 7.417   24.468  1.00 28.82  ? 313 LEU A O   1 
ATOM   1229 C CB  . LEU A 1 180 ? 16.881 6.831   24.384  1.00 29.84  ? 313 LEU A CB  1 
ATOM   1230 C CG  . LEU A 1 180 ? 18.074 6.751   23.436  1.00 30.50  ? 313 LEU A CG  1 
ATOM   1231 C CD1 . LEU A 1 180 ? 18.899 5.505   23.748  1.00 34.18  ? 313 LEU A CD1 1 
ATOM   1232 C CD2 . LEU A 1 180 ? 17.572 6.714   21.997  1.00 29.09  ? 313 LEU A CD2 1 
ATOM   1233 N N   . ILE A 1 181 ? 14.746 8.413   26.182  1.00 26.16  ? 314 ILE A N   1 
ATOM   1234 C CA  . ILE A 1 181 ? 13.555 8.364   27.020  1.00 27.19  ? 314 ILE A CA  1 
ATOM   1235 C C   . ILE A 1 181 ? 12.501 9.315   26.442  1.00 25.77  ? 314 ILE A C   1 
ATOM   1236 O O   . ILE A 1 181 ? 11.303 9.013   26.434  1.00 23.90  ? 314 ILE A O   1 
ATOM   1237 C CB  . ILE A 1 181 ? 13.882 8.763   28.474  1.00 27.60  ? 314 ILE A CB  1 
ATOM   1238 C CG1 . ILE A 1 181 ? 14.729 7.661   29.123  1.00 28.91  ? 314 ILE A CG1 1 
ATOM   1239 C CG2 . ILE A 1 181 ? 12.597 9.022   29.252  1.00 27.06  ? 314 ILE A CG2 1 
ATOM   1240 C CD1 . ILE A 1 181 ? 15.146 7.958   30.547  1.00 31.23  ? 314 ILE A CD1 1 
ATOM   1241 N N   . ILE A 1 182 ? 12.959 10.457  25.941  1.00 24.73  ? 315 ILE A N   1 
ATOM   1242 C CA  . ILE A 1 182 ? 12.055 11.438  25.356  1.00 25.46  ? 315 ILE A CA  1 
ATOM   1243 C C   . ILE A 1 182 ? 11.370 10.816  24.143  1.00 25.89  ? 315 ILE A C   1 
ATOM   1244 O O   . ILE A 1 182 ? 10.161 10.956  23.956  1.00 23.96  ? 315 ILE A O   1 
ATOM   1245 C CB  . ILE A 1 182 ? 12.831 12.718  24.965  1.00 24.54  ? 315 ILE A CB  1 
ATOM   1246 C CG1 . ILE A 1 182 ? 13.197 13.480  26.244  1.00 21.82  ? 315 ILE A CG1 1 
ATOM   1247 C CG2 . ILE A 1 182 ? 12.000 13.588  24.030  1.00 22.05  ? 315 ILE A CG2 1 
ATOM   1248 C CD1 . ILE A 1 182 ? 14.132 14.660  26.029  1.00 23.21  ? 315 ILE A CD1 1 
ATOM   1249 N N   . LEU A 1 183 ? 12.149 10.106  23.335  1.00 27.86  ? 316 LEU A N   1 
ATOM   1250 C CA  . LEU A 1 183 ? 11.612 9.440   22.155  1.00 28.27  ? 316 LEU A CA  1 
ATOM   1251 C C   . LEU A 1 183 ? 10.570 8.392   22.546  1.00 29.53  ? 316 LEU A C   1 
ATOM   1252 O O   . LEU A 1 183 ? 9.468  8.367   21.994  1.00 29.55  ? 316 LEU A O   1 
ATOM   1253 C CB  . LEU A 1 183 ? 12.743 8.775   21.369  1.00 29.03  ? 316 LEU A CB  1 
ATOM   1254 C CG  . LEU A 1 183 ? 12.333 7.845   20.219  1.00 30.87  ? 316 LEU A CG  1 
ATOM   1255 C CD1 . LEU A 1 183 ? 11.480 8.604   19.209  1.00 30.68  ? 316 LEU A CD1 1 
ATOM   1256 C CD2 . LEU A 1 183 ? 13.585 7.281   19.556  1.00 29.85  ? 316 LEU A CD2 1 
ATOM   1257 N N   . ALA A 1 184 ? 10.913 7.534   23.505  1.00 29.92  ? 317 ALA A N   1 
ATOM   1258 C CA  . ALA A 1 184 ? 9.993  6.483   23.943  1.00 29.89  ? 317 ALA A CA  1 
ATOM   1259 C C   . ALA A 1 184 ? 8.700  7.051   24.521  1.00 30.79  ? 317 ALA A C   1 
ATOM   1260 O O   . ALA A 1 184 ? 7.671  6.374   24.539  1.00 30.65  ? 317 ALA A O   1 
ATOM   1261 C CB  . ALA A 1 184 ? 10.671 5.583   24.973  1.00 27.63  ? 317 ALA A CB  1 
ATOM   1262 N N   . SER A 1 185 ? 8.753  8.293   24.995  1.00 31.08  ? 318 SER A N   1 
ATOM   1263 C CA  . SER A 1 185 ? 7.573  8.933   25.570  1.00 30.43  ? 318 SER A CA  1 
ATOM   1264 C C   . SER A 1 185 ? 6.759  9.678   24.518  1.00 29.99  ? 318 SER A C   1 
ATOM   1265 O O   . SER A 1 185 ? 5.742  10.287  24.839  1.00 29.14  ? 318 SER A O   1 
ATOM   1266 C CB  . SER A 1 185 ? 7.981  9.919   26.666  1.00 30.91  ? 318 SER A CB  1 
ATOM   1267 O OG  . SER A 1 185 ? 8.686  9.272   27.702  1.00 33.23  ? 318 SER A OG  1 
ATOM   1268 N N   . GLY A 1 186 ? 7.209  9.635   23.266  1.00 30.73  ? 319 GLY A N   1 
ATOM   1269 C CA  . GLY A 1 186 ? 6.494  10.327  22.204  1.00 30.10  ? 319 GLY A CA  1 
ATOM   1270 C C   . GLY A 1 186 ? 6.807  11.816  22.130  1.00 29.31  ? 319 GLY A C   1 
ATOM   1271 O O   . GLY A 1 186 ? 5.989  12.610  21.667  1.00 28.33  ? 319 GLY A O   1 
ATOM   1272 N N   . GLY A 1 187 ? 7.995  12.194  22.589  1.00 28.82  ? 320 GLY A N   1 
ATOM   1273 C CA  . GLY A 1 187 ? 8.395  13.589  22.559  1.00 27.23  ? 320 GLY A CA  1 
ATOM   1274 C C   . GLY A 1 187 ? 8.379  14.196  21.165  1.00 26.93  ? 320 GLY A C   1 
ATOM   1275 O O   . GLY A 1 187 ? 7.846  15.290  20.979  1.00 26.22  ? 320 GLY A O   1 
ATOM   1276 N N   . PRO A 1 188 ? 8.947  13.512  20.159  1.00 25.09  ? 321 PRO A N   1 
ATOM   1277 C CA  . PRO A 1 188 ? 8.970  14.039  18.792  1.00 24.70  ? 321 PRO A CA  1 
ATOM   1278 C C   . PRO A 1 188 ? 7.627  14.540  18.259  1.00 24.98  ? 321 PRO A C   1 
ATOM   1279 O O   . PRO A 1 188 ? 7.530  15.670  17.770  1.00 20.88  ? 321 PRO A O   1 
ATOM   1280 C CB  . PRO A 1 188 ? 9.509  12.863  17.985  1.00 27.07  ? 321 PRO A CB  1 
ATOM   1281 C CG  . PRO A 1 188 ? 10.486 12.250  18.940  1.00 26.67  ? 321 PRO A CG  1 
ATOM   1282 C CD  . PRO A 1 188 ? 9.690  12.240  20.237  1.00 25.80  ? 321 PRO A CD  1 
ATOM   1283 N N   . GLN A 1 189 ? 6.591  13.711  18.347  1.00 23.29  ? 322 GLN A N   1 
ATOM   1284 C CA  . GLN A 1 189 ? 5.290  14.128  17.839  1.00 24.90  ? 322 GLN A CA  1 
ATOM   1285 C C   . GLN A 1 189 ? 4.718  15.263  18.680  1.00 24.39  ? 322 GLN A C   1 
ATOM   1286 O O   . GLN A 1 189 ? 4.091  16.177  18.145  1.00 22.36  ? 322 GLN A O   1 
ATOM   1287 C CB  . GLN A 1 189 ? 4.305  12.952  17.812  1.00 27.31  ? 322 GLN A CB  1 
ATOM   1288 C CG  . GLN A 1 189 ? 3.043  13.233  16.993  1.00 28.74  ? 322 GLN A CG  1 
ATOM   1289 C CD  . GLN A 1 189 ? 3.339  13.444  15.511  1.00 29.44  ? 322 GLN A CD  1 
ATOM   1290 O OE1 . GLN A 1 189 ? 3.709  12.511  14.803  1.00 29.85  ? 322 GLN A OE1 1 
ATOM   1291 N NE2 . GLN A 1 189 ? 3.184  14.678  15.042  1.00 31.10  ? 322 GLN A NE2 1 
ATOM   1292 N N   . ALA A 1 190 ? 4.935  15.207  19.994  1.00 22.47  ? 323 ALA A N   1 
ATOM   1293 C CA  . ALA A 1 190 ? 4.424  16.249  20.879  1.00 23.67  ? 323 ALA A CA  1 
ATOM   1294 C C   . ALA A 1 190 ? 5.114  17.583  20.573  1.00 22.25  ? 323 ALA A C   1 
ATOM   1295 O O   . ALA A 1 190 ? 4.467  18.633  20.522  1.00 21.12  ? 323 ALA A O   1 
ATOM   1296 C CB  . ALA A 1 190 ? 4.632  15.851  22.350  1.00 21.32  ? 323 ALA A CB  1 
ATOM   1297 N N   . LEU A 1 191 ? 6.425  17.539  20.359  1.00 21.08  ? 324 LEU A N   1 
ATOM   1298 C CA  . LEU A 1 191 ? 7.188  18.750  20.049  1.00 20.17  ? 324 LEU A CA  1 
ATOM   1299 C C   . LEU A 1 191 ? 6.821  19.324  18.674  1.00 20.39  ? 324 LEU A C   1 
ATOM   1300 O O   . LEU A 1 191 ? 6.693  20.539  18.513  1.00 19.71  ? 324 LEU A O   1 
ATOM   1301 C CB  . LEU A 1 191 ? 8.686  18.454  20.111  1.00 18.20  ? 324 LEU A CB  1 
ATOM   1302 C CG  . LEU A 1 191 ? 9.230  18.079  21.496  1.00 17.13  ? 324 LEU A CG  1 
ATOM   1303 C CD1 . LEU A 1 191 ? 10.641 17.542  21.349  1.00 16.70  ? 324 LEU A CD1 1 
ATOM   1304 C CD2 . LEU A 1 191 ? 9.205  19.299  22.427  1.00 16.27  ? 324 LEU A CD2 1 
ATOM   1305 N N   . VAL A 1 192 ? 6.651  18.449  17.688  1.00 19.86  ? 325 VAL A N   1 
ATOM   1306 C CA  . VAL A 1 192 ? 6.282  18.875  16.340  1.00 20.44  ? 325 VAL A CA  1 
ATOM   1307 C C   . VAL A 1 192 ? 4.886  19.500  16.363  1.00 21.42  ? 325 VAL A C   1 
ATOM   1308 O O   . VAL A 1 192 ? 4.640  20.504  15.696  1.00 21.24  ? 325 VAL A O   1 
ATOM   1309 C CB  . VAL A 1 192 ? 6.310  17.677  15.355  1.00 21.84  ? 325 VAL A CB  1 
ATOM   1310 C CG1 . VAL A 1 192 ? 5.597  18.030  14.055  1.00 20.66  ? 325 VAL A CG1 1 
ATOM   1311 C CG2 . VAL A 1 192 ? 7.753  17.294  15.063  1.00 21.55  ? 325 VAL A CG2 1 
ATOM   1312 N N   . ASN A 1 193 ? 3.979  18.907  17.138  1.00 21.00  ? 326 ASN A N   1 
ATOM   1313 C CA  . ASN A 1 193 ? 2.620  19.421  17.252  1.00 22.72  ? 326 ASN A CA  1 
ATOM   1314 C C   . ASN A 1 193 ? 2.634  20.851  17.779  1.00 22.43  ? 326 ASN A C   1 
ATOM   1315 O O   . ASN A 1 193 ? 1.853  21.691  17.331  1.00 22.69  ? 326 ASN A O   1 
ATOM   1316 C CB  . ASN A 1 193 ? 1.783  18.540  18.186  1.00 24.05  ? 326 ASN A CB  1 
ATOM   1317 C CG  . ASN A 1 193 ? 1.412  17.202  17.557  1.00 28.95  ? 326 ASN A CG  1 
ATOM   1318 O OD1 . ASN A 1 193 ? 1.674  16.956  16.374  1.00 28.10  ? 326 ASN A OD1 1 
ATOM   1319 N ND2 . ASN A 1 193 ? 0.790  16.332  18.352  1.00 29.19  ? 326 ASN A ND2 1 
ATOM   1320 N N   . ILE A 1 194 ? 3.511  21.124  18.742  1.00 21.66  ? 327 ILE A N   1 
ATOM   1321 C CA  . ILE A 1 194 ? 3.624  22.471  19.299  1.00 20.85  ? 327 ILE A CA  1 
ATOM   1322 C C   . ILE A 1 194 ? 4.034  23.453  18.198  1.00 20.27  ? 327 ILE A C   1 
ATOM   1323 O O   . ILE A 1 194 ? 3.473  24.545  18.091  1.00 20.00  ? 327 ILE A O   1 
ATOM   1324 C CB  . ILE A 1 194 ? 4.658  22.511  20.467  1.00 20.95  ? 327 ILE A CB  1 
ATOM   1325 C CG1 . ILE A 1 194 ? 4.029  21.920  21.732  1.00 20.79  ? 327 ILE A CG1 1 
ATOM   1326 C CG2 . ILE A 1 194 ? 5.116  23.938  20.736  1.00 19.53  ? 327 ILE A CG2 1 
ATOM   1327 C CD1 . ILE A 1 194 ? 5.009  21.732  22.882  1.00 18.89  ? 327 ILE A CD1 1 
ATOM   1328 N N   . MET A 1 195 ? 4.988  23.053  17.362  1.00 20.61  ? 328 MET A N   1 
ATOM   1329 C CA  . MET A 1 195 ? 5.458  23.915  16.279  1.00 21.62  ? 328 MET A CA  1 
ATOM   1330 C C   . MET A 1 195 ? 4.364  24.222  15.255  1.00 22.61  ? 328 MET A C   1 
ATOM   1331 O O   . MET A 1 195 ? 4.379  25.278  14.614  1.00 20.99  ? 328 MET A O   1 
ATOM   1332 C CB  . MET A 1 195 ? 6.652  23.277  15.551  1.00 21.33  ? 328 MET A CB  1 
ATOM   1333 C CG  . MET A 1 195 ? 7.900  23.018  16.409  1.00 22.73  ? 328 MET A CG  1 
ATOM   1334 S SD  . MET A 1 195 ? 8.525  24.460  17.319  1.00 23.73  ? 328 MET A SD  1 
ATOM   1335 C CE  . MET A 1 195 ? 9.069  25.520  15.983  1.00 16.98  ? 328 MET A CE  1 
ATOM   1336 N N   . ARG A 1 196 ? 3.420  23.301  15.098  1.00 20.96  ? 329 ARG A N   1 
ATOM   1337 C CA  . ARG A 1 196 ? 2.341  23.489  14.132  1.00 24.00  ? 329 ARG A CA  1 
ATOM   1338 C C   . ARG A 1 196 ? 1.104  24.151  14.736  1.00 23.95  ? 329 ARG A C   1 
ATOM   1339 O O   . ARG A 1 196 ? 0.242  24.642  14.010  1.00 23.99  ? 329 ARG A O   1 
ATOM   1340 C CB  . ARG A 1 196 ? 1.920  22.134  13.543  1.00 25.62  ? 329 ARG A CB  1 
ATOM   1341 C CG  . ARG A 1 196 ? 3.018  21.408  12.791  1.00 25.54  ? 329 ARG A CG  1 
ATOM   1342 C CD  . ARG A 1 196 ? 2.505  20.166  12.065  1.00 28.56  ? 329 ARG A CD  1 
ATOM   1343 N NE  . ARG A 1 196 ? 1.964  19.156  12.972  1.00 28.06  ? 329 ARG A NE  1 
ATOM   1344 C CZ  . ARG A 1 196 ? 1.980  17.848  12.725  1.00 31.63  ? 329 ARG A CZ  1 
ATOM   1345 N NH1 . ARG A 1 196 ? 2.515  17.382  11.599  1.00 30.24  ? 329 ARG A NH1 1 
ATOM   1346 N NH2 . ARG A 1 196 ? 1.455  17.003  13.599  1.00 31.15  ? 329 ARG A NH2 1 
ATOM   1347 N N   . THR A 1 197 ? 1.037  24.179  16.061  1.00 22.65  ? 330 THR A N   1 
ATOM   1348 C CA  . THR A 1 197 ? -0.129 24.699  16.759  1.00 24.11  ? 330 THR A CA  1 
ATOM   1349 C C   . THR A 1 197 ? -0.060 26.091  17.385  1.00 25.60  ? 330 THR A C   1 
ATOM   1350 O O   . THR A 1 197 ? -1.057 26.814  17.381  1.00 25.75  ? 330 THR A O   1 
ATOM   1351 C CB  . THR A 1 197 ? -0.544 23.698  17.858  1.00 24.16  ? 330 THR A CB  1 
ATOM   1352 O OG1 . THR A 1 197 ? -0.718 22.403  17.268  1.00 22.69  ? 330 THR A OG1 1 
ATOM   1353 C CG2 . THR A 1 197 ? -1.851 24.130  18.541  1.00 25.62  ? 330 THR A CG2 1 
ATOM   1354 N N   . TYR A 1 198 ? 1.099  26.472  17.918  1.00 23.42  ? 331 TYR A N   1 
ATOM   1355 C CA  . TYR A 1 198 ? 1.210  27.758  18.588  1.00 23.51  ? 331 TYR A CA  1 
ATOM   1356 C C   . TYR A 1 198 ? 2.006  28.844  17.878  1.00 22.81  ? 331 TYR A C   1 
ATOM   1357 O O   . TYR A 1 198 ? 2.821  28.562  17.003  1.00 21.13  ? 331 TYR A O   1 
ATOM   1358 C CB  . TYR A 1 198 ? 1.754  27.529  20.002  1.00 24.25  ? 331 TYR A CB  1 
ATOM   1359 C CG  . TYR A 1 198 ? 0.920  26.535  20.774  1.00 22.97  ? 331 TYR A CG  1 
ATOM   1360 C CD1 . TYR A 1 198 ? 1.327  25.208  20.916  1.00 23.33  ? 331 TYR A CD1 1 
ATOM   1361 C CD2 . TYR A 1 198 ? -0.307 26.910  21.318  1.00 23.74  ? 331 TYR A CD2 1 
ATOM   1362 C CE1 . TYR A 1 198 ? 0.526  24.275  21.585  1.00 24.07  ? 331 TYR A CE1 1 
ATOM   1363 C CE2 . TYR A 1 198 ? -1.116 25.989  21.984  1.00 25.30  ? 331 TYR A CE2 1 
ATOM   1364 C CZ  . TYR A 1 198 ? -0.696 24.675  22.114  1.00 25.79  ? 331 TYR A CZ  1 
ATOM   1365 O OH  . TYR A 1 198 ? -1.507 23.769  22.767  1.00 24.94  ? 331 TYR A OH  1 
ATOM   1366 N N   . THR A 1 199 ? 1.759  30.092  18.273  1.00 22.07  ? 332 THR A N   1 
ATOM   1367 C CA  . THR A 1 199 ? 2.428  31.240  17.668  1.00 23.37  ? 332 THR A CA  1 
ATOM   1368 C C   . THR A 1 199 ? 3.291  32.042  18.634  1.00 23.93  ? 332 THR A C   1 
ATOM   1369 O O   . THR A 1 199 ? 3.950  33.004  18.234  1.00 26.47  ? 332 THR A O   1 
ATOM   1370 C CB  . THR A 1 199 ? 1.401  32.201  17.042  1.00 25.51  ? 332 THR A CB  1 
ATOM   1371 O OG1 . THR A 1 199 ? 0.512  32.673  18.062  1.00 23.76  ? 332 THR A OG1 1 
ATOM   1372 C CG2 . THR A 1 199 ? 0.588  31.485  15.961  1.00 22.75  ? 332 THR A CG2 1 
ATOM   1373 N N   . TYR A 1 200 ? 3.280  31.662  19.904  1.00 21.92  ? 333 TYR A N   1 
ATOM   1374 C CA  . TYR A 1 200 ? 4.079  32.358  20.906  1.00 22.70  ? 333 TYR A CA  1 
ATOM   1375 C C   . TYR A 1 200 ? 5.569  32.124  20.620  1.00 22.33  ? 333 TYR A C   1 
ATOM   1376 O O   . TYR A 1 200 ? 6.057  30.996  20.694  1.00 21.66  ? 333 TYR A O   1 
ATOM   1377 C CB  . TYR A 1 200 ? 3.697  31.850  22.299  1.00 23.09  ? 333 TYR A CB  1 
ATOM   1378 C CG  . TYR A 1 200 ? 4.402  32.540  23.445  1.00 26.66  ? 333 TYR A CG  1 
ATOM   1379 C CD1 . TYR A 1 200 ? 4.454  33.934  23.527  1.00 27.57  ? 333 TYR A CD1 1 
ATOM   1380 C CD2 . TYR A 1 200 ? 4.982  31.796  24.475  1.00 25.90  ? 333 TYR A CD2 1 
ATOM   1381 C CE1 . TYR A 1 200 ? 5.066  34.572  24.608  1.00 27.95  ? 333 TYR A CE1 1 
ATOM   1382 C CE2 . TYR A 1 200 ? 5.591  32.421  25.561  1.00 27.24  ? 333 TYR A CE2 1 
ATOM   1383 C CZ  . TYR A 1 200 ? 5.630  33.805  25.623  1.00 28.53  ? 333 TYR A CZ  1 
ATOM   1384 O OH  . TYR A 1 200 ? 6.226  34.417  26.702  1.00 27.44  ? 333 TYR A OH  1 
ATOM   1385 N N   . GLU A 1 201 ? 6.281  33.203  20.303  1.00 21.19  ? 334 GLU A N   1 
ATOM   1386 C CA  . GLU A 1 201 ? 7.705  33.153  19.966  1.00 21.55  ? 334 GLU A CA  1 
ATOM   1387 C C   . GLU A 1 201 ? 8.617  32.436  20.961  1.00 21.65  ? 334 GLU A C   1 
ATOM   1388 O O   . GLU A 1 201 ? 9.450  31.629  20.550  1.00 21.08  ? 334 GLU A O   1 
ATOM   1389 C CB  . GLU A 1 201 ? 8.234  34.579  19.736  1.00 22.42  ? 334 GLU A CB  1 
ATOM   1390 C CG  . GLU A 1 201 ? 9.607  34.681  19.064  1.00 24.15  ? 334 GLU A CG  1 
ATOM   1391 C CD  . GLU A 1 201 ? 10.776 34.386  19.999  1.00 24.99  ? 334 GLU A CD  1 
ATOM   1392 O OE1 . GLU A 1 201 ? 10.626 34.554  21.227  1.00 24.00  ? 334 GLU A OE1 1 
ATOM   1393 O OE2 . GLU A 1 201 ? 11.858 34.003  19.499  1.00 24.69  ? 334 GLU A OE2 1 
ATOM   1394 N N   . LYS A 1 202 ? 8.478  32.713  22.255  1.00 21.08  ? 335 LYS A N   1 
ATOM   1395 C CA  . LYS A 1 202 ? 9.367  32.066  23.219  1.00 22.04  ? 335 LYS A CA  1 
ATOM   1396 C C   . LYS A 1 202 ? 9.197  30.552  23.226  1.00 21.85  ? 335 LYS A C   1 
ATOM   1397 O O   . LYS A 1 202 ? 10.173 29.804  23.346  1.00 20.86  ? 335 LYS A O   1 
ATOM   1398 C CB  . LYS A 1 202 ? 9.154  32.593  24.641  1.00 25.01  ? 335 LYS A CB  1 
ATOM   1399 C CG  . LYS A 1 202 ? 10.306 32.182  25.556  1.00 28.52  ? 335 LYS A CG  1 
ATOM   1400 C CD  . LYS A 1 202 ? 10.087 32.487  27.020  1.00 34.70  ? 335 LYS A CD  1 
ATOM   1401 C CE  . LYS A 1 202 ? 11.306 32.016  27.821  1.00 38.54  ? 335 LYS A CE  1 
ATOM   1402 N NZ  . LYS A 1 202 ? 11.128 32.063  29.299  1.00 41.48  ? 335 LYS A NZ  1 
ATOM   1403 N N   . LEU A 1 203 ? 7.951  30.107  23.119  1.00 19.92  ? 336 LEU A N   1 
ATOM   1404 C CA  . LEU A 1 203 ? 7.656  28.685  23.100  1.00 18.97  ? 336 LEU A CA  1 
ATOM   1405 C C   . LEU A 1 203 ? 8.206  28.048  21.827  1.00 20.07  ? 336 LEU A C   1 
ATOM   1406 O O   . LEU A 1 203 ? 8.831  26.988  21.873  1.00 19.56  ? 336 LEU A O   1 
ATOM   1407 C CB  . LEU A 1 203 ? 6.150  28.454  23.171  1.00 17.24  ? 336 LEU A CB  1 
ATOM   1408 C CG  . LEU A 1 203 ? 5.734  27.007  22.895  1.00 20.10  ? 336 LEU A CG  1 
ATOM   1409 C CD1 . LEU A 1 203 ? 6.450  26.072  23.873  1.00 15.58  ? 336 LEU A CD1 1 
ATOM   1410 C CD2 . LEU A 1 203 ? 4.221  26.881  23.001  1.00 17.97  ? 336 LEU A CD2 1 
ATOM   1411 N N   . LEU A 1 204 ? 7.969  28.694  20.688  1.00 17.85  ? 337 LEU A N   1 
ATOM   1412 C CA  . LEU A 1 204 ? 8.450  28.161  19.414  1.00 20.23  ? 337 LEU A CA  1 
ATOM   1413 C C   . LEU A 1 204 ? 9.968  28.029  19.452  1.00 19.64  ? 337 LEU A C   1 
ATOM   1414 O O   . LEU A 1 204 ? 10.527 27.027  19.003  1.00 17.74  ? 337 LEU A O   1 
ATOM   1415 C CB  . LEU A 1 204 ? 8.009  29.065  18.248  1.00 16.87  ? 337 LEU A CB  1 
ATOM   1416 C CG  . LEU A 1 204 ? 6.489  29.104  18.010  1.00 22.12  ? 337 LEU A CG  1 
ATOM   1417 C CD1 . LEU A 1 204 ? 6.133  30.182  16.998  1.00 19.33  ? 337 LEU A CD1 1 
ATOM   1418 C CD2 . LEU A 1 204 ? 6.008  27.736  17.522  1.00 18.78  ? 337 LEU A CD2 1 
ATOM   1419 N N   . TRP A 1 205 ? 10.624 29.043  20.011  1.00 19.59  ? 338 TRP A N   1 
ATOM   1420 C CA  . TRP A 1 205 ? 12.071 29.058  20.134  1.00 17.58  ? 338 TRP A CA  1 
ATOM   1421 C C   . TRP A 1 205 ? 12.579 27.954  21.065  1.00 17.11  ? 338 TRP A C   1 
ATOM   1422 O O   . TRP A 1 205 ? 13.492 27.210  20.701  1.00 18.75  ? 338 TRP A O   1 
ATOM   1423 C CB  . TRP A 1 205 ? 12.537 30.418  20.661  1.00 19.76  ? 338 TRP A CB  1 
ATOM   1424 C CG  . TRP A 1 205 ? 13.996 30.468  21.010  1.00 16.15  ? 338 TRP A CG  1 
ATOM   1425 C CD1 . TRP A 1 205 ? 15.054 30.331  20.155  1.00 19.20  ? 338 TRP A CD1 1 
ATOM   1426 C CD2 . TRP A 1 205 ? 14.555 30.676  22.313  1.00 19.40  ? 338 TRP A CD2 1 
ATOM   1427 N NE1 . TRP A 1 205 ? 16.241 30.443  20.846  1.00 19.08  ? 338 TRP A NE1 1 
ATOM   1428 C CE2 . TRP A 1 205 ? 15.963 30.654  22.173  1.00 20.31  ? 338 TRP A CE2 1 
ATOM   1429 C CE3 . TRP A 1 205 ? 14.001 30.879  23.588  1.00 20.00  ? 338 TRP A CE3 1 
ATOM   1430 C CZ2 . TRP A 1 205 ? 16.831 30.830  23.262  1.00 21.87  ? 338 TRP A CZ2 1 
ATOM   1431 C CZ3 . TRP A 1 205 ? 14.863 31.055  24.675  1.00 23.90  ? 338 TRP A CZ3 1 
ATOM   1432 C CH2 . TRP A 1 205 ? 16.266 31.028  24.502  1.00 22.58  ? 338 TRP A CH2 1 
ATOM   1433 N N   . THR A 1 206 ? 11.996 27.855  22.256  0.50 11.13  ? 339 THR A N   1 
ATOM   1434 C CA  . THR A 1 206 ? 12.414 26.842  23.217  0.50 13.29  ? 339 THR A CA  1 
ATOM   1435 C C   . THR A 1 206 ? 12.192 25.432  22.669  0.50 12.68  ? 339 THR A C   1 
ATOM   1436 O O   . THR A 1 206 ? 13.020 24.539  22.863  0.50 10.63  ? 339 THR A O   1 
ATOM   1437 C CB  . THR A 1 206 ? 11.658 26.993  24.562  0.50 13.44  ? 339 THR A CB  1 
ATOM   1438 O OG1 . THR A 1 206 ? 12.079 28.197  25.222  0.50 14.26  ? 339 THR A OG1 1 
ATOM   1439 C CG2 . THR A 1 206 ? 11.959 25.818  25.462  0.50 17.63  ? 339 THR A CG2 1 
ATOM   1440 N N   . THR A 1 207 ? 11.072 25.238  21.982  1.00 15.91  ? 340 THR A N   1 
ATOM   1441 C CA  . THR A 1 207 ? 10.749 23.935  21.405  1.00 17.84  ? 340 THR A CA  1 
ATOM   1442 C C   . THR A 1 207 ? 11.714 23.612  20.260  1.00 20.25  ? 340 THR A C   1 
ATOM   1443 O O   . THR A 1 207 ? 12.176 22.472  20.128  1.00 19.52  ? 340 THR A O   1 
ATOM   1444 C CB  . THR A 1 207 ? 9.293  23.909  20.898  1.00 19.78  ? 340 THR A CB  1 
ATOM   1445 O OG1 . THR A 1 207 ? 8.412  24.175  21.997  1.00 18.65  ? 340 THR A OG1 1 
ATOM   1446 C CG2 . THR A 1 207 ? 8.940  22.541  20.293  1.00 17.88  ? 340 THR A CG2 1 
ATOM   1447 N N   . SER A 1 208 ? 12.037 24.611  19.441  1.00 18.17  ? 341 SER A N   1 
ATOM   1448 C CA  . SER A 1 208 ? 12.962 24.381  18.333  1.00 19.74  ? 341 SER A CA  1 
ATOM   1449 C C   . SER A 1 208 ? 14.332 23.968  18.874  1.00 19.80  ? 341 SER A C   1 
ATOM   1450 O O   . SER A 1 208 ? 15.059 23.229  18.221  1.00 22.14  ? 341 SER A O   1 
ATOM   1451 C CB  . SER A 1 208 ? 13.105 25.635  17.452  1.00 20.00  ? 341 SER A CB  1 
ATOM   1452 O OG  . SER A 1 208 ? 13.877 26.633  18.094  1.00 20.67  ? 341 SER A OG  1 
ATOM   1453 N N   . ARG A 1 209 ? 14.678 24.438  20.068  1.00 20.59  ? 342 ARG A N   1 
ATOM   1454 C CA  . ARG A 1 209 ? 15.955 24.080  20.675  1.00 22.05  ? 342 ARG A CA  1 
ATOM   1455 C C   . ARG A 1 209 ? 15.946 22.628  21.143  1.00 20.89  ? 342 ARG A C   1 
ATOM   1456 O O   . ARG A 1 209 ? 16.960 21.944  21.067  1.00 20.89  ? 342 ARG A O   1 
ATOM   1457 C CB  . ARG A 1 209 ? 16.272 25.006  21.846  1.00 22.93  ? 342 ARG A CB  1 
ATOM   1458 C CG  . ARG A 1 209 ? 16.516 26.450  21.431  1.00 28.30  ? 342 ARG A CG  1 
ATOM   1459 C CD  . ARG A 1 209 ? 16.758 27.307  22.650  1.00 34.40  ? 342 ARG A CD  1 
ATOM   1460 N NE  . ARG A 1 209 ? 17.959 26.882  23.352  1.00 37.20  ? 342 ARG A NE  1 
ATOM   1461 C CZ  . ARG A 1 209 ? 18.175 27.078  24.646  1.00 39.63  ? 342 ARG A CZ  1 
ATOM   1462 N NH1 . ARG A 1 209 ? 17.267 27.693  25.390  1.00 41.57  ? 342 ARG A NH1 1 
ATOM   1463 N NH2 . ARG A 1 209 ? 19.301 26.648  25.196  1.00 42.45  ? 342 ARG A NH2 1 
ATOM   1464 N N   . VAL A 1 210 ? 14.803 22.157  21.633  1.00 20.53  ? 343 VAL A N   1 
ATOM   1465 C CA  . VAL A 1 210 ? 14.700 20.767  22.068  1.00 22.05  ? 343 VAL A CA  1 
ATOM   1466 C C   . VAL A 1 210 ? 14.855 19.896  20.824  1.00 21.94  ? 343 VAL A C   1 
ATOM   1467 O O   . VAL A 1 210 ? 15.624 18.933  20.818  1.00 20.19  ? 343 VAL A O   1 
ATOM   1468 C CB  . VAL A 1 210 ? 13.325 20.462  22.728  1.00 23.19  ? 343 VAL A CB  1 
ATOM   1469 C CG1 . VAL A 1 210 ? 13.258 18.993  23.150  1.00 22.01  ? 343 VAL A CG1 1 
ATOM   1470 C CG2 . VAL A 1 210 ? 13.121 21.348  23.943  1.00 22.00  ? 343 VAL A CG2 1 
ATOM   1471 N N   . LEU A 1 211 ? 14.129 20.249  19.765  1.00 21.37  ? 344 LEU A N   1 
ATOM   1472 C CA  . LEU A 1 211 ? 14.195 19.501  18.516  1.00 21.64  ? 344 LEU A CA  1 
ATOM   1473 C C   . LEU A 1 211 ? 15.607 19.504  17.942  1.00 21.45  ? 344 LEU A C   1 
ATOM   1474 O O   . LEU A 1 211 ? 16.044 18.503  17.372  1.00 22.86  ? 344 LEU A O   1 
ATOM   1475 C CB  . LEU A 1 211 ? 13.188 20.063  17.499  1.00 20.98  ? 344 LEU A CB  1 
ATOM   1476 C CG  . LEU A 1 211 ? 11.718 19.751  17.822  1.00 22.81  ? 344 LEU A CG  1 
ATOM   1477 C CD1 . LEU A 1 211 ? 10.785 20.618  16.982  1.00 20.87  ? 344 LEU A CD1 1 
ATOM   1478 C CD2 . LEU A 1 211 ? 11.446 18.266  17.579  1.00 20.92  ? 344 LEU A CD2 1 
ATOM   1479 N N   . LYS A 1 212 ? 16.325 20.616  18.095  1.00 21.47  ? 345 LYS A N   1 
ATOM   1480 C CA  . LYS A 1 212 ? 17.696 20.701  17.595  1.00 22.64  ? 345 LYS A CA  1 
ATOM   1481 C C   . LYS A 1 212 ? 18.596 19.700  18.333  1.00 23.20  ? 345 LYS A C   1 
ATOM   1482 O O   . LYS A 1 212 ? 19.445 19.048  17.718  1.00 22.27  ? 345 LYS A O   1 
ATOM   1483 C CB  . LYS A 1 212 ? 18.260 22.119  17.755  1.00 22.19  ? 345 LYS A CB  1 
ATOM   1484 C CG  . LYS A 1 212 ? 19.684 22.260  17.207  1.00 24.03  ? 345 LYS A CG  1 
ATOM   1485 C CD  . LYS A 1 212 ? 20.130 23.709  17.084  1.00 30.10  ? 345 LYS A CD  1 
ATOM   1486 C CE  . LYS A 1 212 ? 20.208 24.400  18.427  1.00 34.42  ? 345 LYS A CE  1 
ATOM   1487 N NZ  . LYS A 1 212 ? 21.167 23.720  19.328  1.00 40.56  ? 345 LYS A NZ  1 
ATOM   1488 N N   . VAL A 1 213 ? 18.410 19.589  19.647  1.00 22.67  ? 346 VAL A N   1 
ATOM   1489 C CA  . VAL A 1 213 ? 19.180 18.647  20.457  1.00 23.12  ? 346 VAL A CA  1 
ATOM   1490 C C   . VAL A 1 213 ? 18.863 17.200  20.041  1.00 24.44  ? 346 VAL A C   1 
ATOM   1491 O O   . VAL A 1 213 ? 19.756 16.360  19.945  1.00 23.88  ? 346 VAL A O   1 
ATOM   1492 C CB  . VAL A 1 213 ? 18.855 18.798  21.968  1.00 25.49  ? 346 VAL A CB  1 
ATOM   1493 C CG1 . VAL A 1 213 ? 19.457 17.633  22.752  1.00 27.21  ? 346 VAL A CG1 1 
ATOM   1494 C CG2 . VAL A 1 213 ? 19.411 20.116  22.499  1.00 26.79  ? 346 VAL A CG2 1 
ATOM   1495 N N   . LEU A 1 214 ? 17.587 16.913  19.801  1.00 22.96  ? 347 LEU A N   1 
ATOM   1496 C CA  . LEU A 1 214 ? 17.179 15.567  19.409  1.00 25.23  ? 347 LEU A CA  1 
ATOM   1497 C C   . LEU A 1 214 ? 17.530 15.220  17.959  1.00 25.54  ? 347 LEU A C   1 
ATOM   1498 O O   . LEU A 1 214 ? 17.699 14.048  17.628  1.00 26.93  ? 347 LEU A O   1 
ATOM   1499 C CB  . LEU A 1 214 ? 15.668 15.390  19.611  1.00 22.15  ? 347 LEU A CB  1 
ATOM   1500 C CG  . LEU A 1 214 ? 15.080 15.540  21.024  1.00 22.49  ? 347 LEU A CG  1 
ATOM   1501 C CD1 . LEU A 1 214 ? 13.570 15.422  20.940  1.00 22.95  ? 347 LEU A CD1 1 
ATOM   1502 C CD2 . LEU A 1 214 ? 15.640 14.469  21.961  1.00 22.63  ? 347 LEU A CD2 1 
ATOM   1503 N N   . SER A 1 215 ? 17.649 16.233  17.100  1.00 24.21  ? 348 SER A N   1 
ATOM   1504 C CA  . SER A 1 215 ? 17.938 15.999  15.682  1.00 23.36  ? 348 SER A CA  1 
ATOM   1505 C C   . SER A 1 215 ? 19.296 15.375  15.356  1.00 24.66  ? 348 SER A C   1 
ATOM   1506 O O   . SER A 1 215 ? 19.499 14.901  14.237  1.00 24.54  ? 348 SER A O   1 
ATOM   1507 C CB  . SER A 1 215 ? 17.783 17.295  14.877  1.00 21.13  ? 348 SER A CB  1 
ATOM   1508 O OG  . SER A 1 215 ? 18.770 18.243  15.232  1.00 20.74  ? 348 SER A OG  1 
ATOM   1509 N N   . VAL A 1 216 ? 20.227 15.377  16.306  1.00 25.55  ? 349 VAL A N   1 
ATOM   1510 C CA  . VAL A 1 216 ? 21.541 14.784  16.046  1.00 27.47  ? 349 VAL A CA  1 
ATOM   1511 C C   . VAL A 1 216 ? 21.594 13.330  16.508  1.00 28.64  ? 349 VAL A C   1 
ATOM   1512 O O   . VAL A 1 216 ? 22.608 12.655  16.344  1.00 29.88  ? 349 VAL A O   1 
ATOM   1513 C CB  . VAL A 1 216 ? 22.676 15.570  16.735  1.00 26.79  ? 349 VAL A CB  1 
ATOM   1514 C CG1 . VAL A 1 216 ? 22.732 16.988  16.184  1.00 28.61  ? 349 VAL A CG1 1 
ATOM   1515 C CG2 . VAL A 1 216 ? 22.463 15.586  18.241  1.00 29.08  ? 349 VAL A CG2 1 
ATOM   1516 N N   . CYS A 1 217 ? 20.492 12.861  17.086  1.00 28.67  ? 350 CYS A N   1 
ATOM   1517 C CA  . CYS A 1 217 ? 20.371 11.488  17.564  1.00 30.55  ? 350 CYS A CA  1 
ATOM   1518 C C   . CYS A 1 217 ? 19.807 10.621  16.439  1.00 31.55  ? 350 CYS A C   1 
ATOM   1519 O O   . CYS A 1 217 ? 18.769 10.943  15.862  1.00 31.99  ? 350 CYS A O   1 
ATOM   1520 C CB  . CYS A 1 217 ? 19.440 11.436  18.782  1.00 29.48  ? 350 CYS A CB  1 
ATOM   1521 S SG  . CYS A 1 217 ? 18.845 9.776   19.230  1.00 34.21  ? 350 CYS A SG  1 
ATOM   1522 N N   . SER A 1 218 ? 20.492 9.522   16.136  1.00 31.80  ? 351 SER A N   1 
ATOM   1523 C CA  . SER A 1 218 ? 20.079 8.613   15.066  1.00 32.36  ? 351 SER A CA  1 
ATOM   1524 C C   . SER A 1 218 ? 18.697 7.988   15.268  1.00 31.19  ? 351 SER A C   1 
ATOM   1525 O O   . SER A 1 218 ? 18.077 7.523   14.315  1.00 29.97  ? 351 SER A O   1 
ATOM   1526 C CB  . SER A 1 218 ? 21.127 7.506   14.886  1.00 34.66  ? 351 SER A CB  1 
ATOM   1527 O OG  . SER A 1 218 ? 21.284 6.746   16.075  1.00 38.21  ? 351 SER A OG  1 
ATOM   1528 N N   . SER A 1 219 ? 18.213 7.966   16.504  1.00 31.24  ? 352 SER A N   1 
ATOM   1529 C CA  . SER A 1 219 ? 16.894 7.401   16.770  1.00 30.59  ? 352 SER A CA  1 
ATOM   1530 C C   . SER A 1 219 ? 15.806 8.472   16.674  1.00 30.81  ? 352 SER A C   1 
ATOM   1531 O O   . SER A 1 219 ? 14.753 8.253   16.075  1.00 30.83  ? 352 SER A O   1 
ATOM   1532 C CB  . SER A 1 219 ? 16.867 6.760   18.153  1.00 32.03  ? 352 SER A CB  1 
ATOM   1533 O OG  . SER A 1 219 ? 17.785 5.687   18.224  1.00 37.11  ? 352 SER A OG  1 
ATOM   1534 N N   . ASN A 1 220 ? 16.063 9.636   17.259  1.00 28.05  ? 353 ASN A N   1 
ATOM   1535 C CA  . ASN A 1 220 ? 15.086 10.720  17.218  1.00 28.59  ? 353 ASN A CA  1 
ATOM   1536 C C   . ASN A 1 220 ? 14.923 11.342  15.833  1.00 26.51  ? 353 ASN A C   1 
ATOM   1537 O O   . ASN A 1 220 ? 13.813 11.707  15.451  1.00 26.67  ? 353 ASN A O   1 
ATOM   1538 C CB  . ASN A 1 220 ? 15.462 11.807  18.233  1.00 27.65  ? 353 ASN A CB  1 
ATOM   1539 C CG  . ASN A 1 220 ? 14.932 11.511  19.623  1.00 28.62  ? 353 ASN A CG  1 
ATOM   1540 O OD1 . ASN A 1 220 ? 13.754 11.738  19.915  1.00 25.42  ? 353 ASN A OD1 1 
ATOM   1541 N ND2 . ASN A 1 220 ? 15.797 10.989  20.486  1.00 26.17  ? 353 ASN A ND2 1 
ATOM   1542 N N   . LYS A 1 221 ? 16.018 11.451  15.082  1.00 26.95  ? 354 LYS A N   1 
ATOM   1543 C CA  . LYS A 1 221 ? 15.968 12.052  13.749  1.00 27.76  ? 354 LYS A CA  1 
ATOM   1544 C C   . LYS A 1 221 ? 14.859 11.470  12.870  1.00 28.40  ? 354 LYS A C   1 
ATOM   1545 O O   . LYS A 1 221 ? 13.995 12.207  12.390  1.00 29.43  ? 354 LYS A O   1 
ATOM   1546 C CB  . LYS A 1 221 ? 17.324 11.923  13.036  1.00 27.58  ? 354 LYS A CB  1 
ATOM   1547 C CG  . LYS A 1 221 ? 17.330 12.525  11.631  1.00 28.99  ? 354 LYS A CG  1 
ATOM   1548 C CD  . LYS A 1 221 ? 18.566 12.135  10.825  1.00 31.23  ? 354 LYS A CD  1 
ATOM   1549 C CE  . LYS A 1 221 ? 19.849 12.697  11.421  1.00 34.76  ? 354 LYS A CE  1 
ATOM   1550 N NZ  . LYS A 1 221 ? 21.028 12.436  10.545  1.00 31.59  ? 354 LYS A NZ  1 
ATOM   1551 N N   . PRO A 1 222 ? 14.862 10.142  12.646  1.00 28.41  ? 355 PRO A N   1 
ATOM   1552 C CA  . PRO A 1 222 ? 13.810 9.555   11.808  1.00 27.52  ? 355 PRO A CA  1 
ATOM   1553 C C   . PRO A 1 222 ? 12.416 9.811   12.368  1.00 25.87  ? 355 PRO A C   1 
ATOM   1554 O O   . PRO A 1 222 ? 11.474 10.065  11.620  1.00 27.70  ? 355 PRO A O   1 
ATOM   1555 C CB  . PRO A 1 222 ? 14.153 8.062   11.801  1.00 28.20  ? 355 PRO A CB  1 
ATOM   1556 C CG  . PRO A 1 222 ? 15.638 8.055   11.992  1.00 30.40  ? 355 PRO A CG  1 
ATOM   1557 C CD  . PRO A 1 222 ? 15.851 9.122   13.038  1.00 27.31  ? 355 PRO A CD  1 
ATOM   1558 N N   . ALA A 1 223 ? 12.285 9.741   13.688  1.00 24.04  ? 356 ALA A N   1 
ATOM   1559 C CA  . ALA A 1 223 ? 10.991 9.956   14.322  1.00 23.84  ? 356 ALA A CA  1 
ATOM   1560 C C   . ALA A 1 223 ? 10.493 11.393  14.122  1.00 23.36  ? 356 ALA A C   1 
ATOM   1561 O O   . ALA A 1 223 ? 9.303  11.616  13.893  1.00 24.13  ? 356 ALA A O   1 
ATOM   1562 C CB  . ALA A 1 223 ? 11.072 9.616   15.815  1.00 22.38  ? 356 ALA A CB  1 
ATOM   1563 N N   . ILE A 1 224 ? 11.397 12.365  14.210  1.00 21.89  ? 357 ILE A N   1 
ATOM   1564 C CA  . ILE A 1 224 ? 11.012 13.766  14.013  1.00 20.94  ? 357 ILE A CA  1 
ATOM   1565 C C   . ILE A 1 224 ? 10.536 13.972  12.566  1.00 21.57  ? 357 ILE A C   1 
ATOM   1566 O O   . ILE A 1 224 ? 9.504  14.605  12.324  1.00 21.08  ? 357 ILE A O   1 
ATOM   1567 C CB  . ILE A 1 224 ? 12.205 14.720  14.326  1.00 21.70  ? 357 ILE A CB  1 
ATOM   1568 C CG1 . ILE A 1 224 ? 12.584 14.600  15.804  1.00 20.47  ? 357 ILE A CG1 1 
ATOM   1569 C CG2 . ILE A 1 224 ? 11.826 16.170  14.014  1.00 20.59  ? 357 ILE A CG2 1 
ATOM   1570 C CD1 . ILE A 1 224 ? 13.879 15.311  16.171  1.00 20.29  ? 357 ILE A CD1 1 
ATOM   1571 N N   . VAL A 1 225 ? 11.280 13.420  11.610  1.00 21.67  ? 358 VAL A N   1 
ATOM   1572 C CA  . VAL A 1 225 ? 10.923 13.535  10.200  1.00 23.93  ? 358 VAL A CA  1 
ATOM   1573 C C   . VAL A 1 225 ? 9.557  12.908  9.906   1.00 26.53  ? 358 VAL A C   1 
ATOM   1574 O O   . VAL A 1 225 ? 8.716  13.522  9.251   1.00 26.93  ? 358 VAL A O   1 
ATOM   1575 C CB  . VAL A 1 225 ? 11.985 12.858  9.290   1.00 24.43  ? 358 VAL A CB  1 
ATOM   1576 C CG1 . VAL A 1 225 ? 11.479 12.782  7.862   1.00 22.77  ? 358 VAL A CG1 1 
ATOM   1577 C CG2 . VAL A 1 225 ? 13.280 13.642  9.329   1.00 23.54  ? 358 VAL A CG2 1 
ATOM   1578 N N   . GLU A 1 226 ? 9.340  11.687  10.388  1.00 26.86  ? 359 GLU A N   1 
ATOM   1579 C CA  . GLU A 1 226 ? 8.073  10.995  10.161  1.00 29.76  ? 359 GLU A CA  1 
ATOM   1580 C C   . GLU A 1 226 ? 6.890  11.701  10.816  1.00 28.41  ? 359 GLU A C   1 
ATOM   1581 O O   . GLU A 1 226 ? 5.753  11.582  10.355  1.00 26.78  ? 359 GLU A O   1 
ATOM   1582 C CB  . GLU A 1 226 ? 8.156  9.550   10.667  1.00 32.69  ? 359 GLU A CB  1 
ATOM   1583 C CG  . GLU A 1 226 ? 9.088  8.677   9.838   1.00 40.19  ? 359 GLU A CG  1 
ATOM   1584 C CD  . GLU A 1 226 ? 8.762  8.741   8.351   1.00 43.41  ? 359 GLU A CD  1 
ATOM   1585 O OE1 . GLU A 1 226 ? 7.602  8.445   7.982   1.00 46.02  ? 359 GLU A OE1 1 
ATOM   1586 O OE2 . GLU A 1 226 ? 9.660  9.089   7.553   1.00 44.77  ? 359 GLU A OE2 1 
ATOM   1587 N N   . ALA A 1 227 ? 7.163  12.438  11.888  1.00 27.12  ? 360 ALA A N   1 
ATOM   1588 C CA  . ALA A 1 227 ? 6.119  13.167  12.598  1.00 26.24  ? 360 ALA A CA  1 
ATOM   1589 C C   . ALA A 1 227 ? 5.735  14.452  11.865  1.00 25.16  ? 360 ALA A C   1 
ATOM   1590 O O   . ALA A 1 227 ? 4.820  15.160  12.286  1.00 26.45  ? 360 ALA A O   1 
ATOM   1591 C CB  . ALA A 1 227 ? 6.587  13.494  14.016  1.00 28.30  ? 360 ALA A CB  1 
ATOM   1592 N N   . GLY A 1 228 ? 6.434  14.747  10.771  1.00 23.89  ? 361 GLY A N   1 
ATOM   1593 C CA  . GLY A 1 228 ? 6.150  15.953  10.009  1.00 23.70  ? 361 GLY A CA  1 
ATOM   1594 C C   . GLY A 1 228 ? 6.981  17.138  10.474  1.00 23.44  ? 361 GLY A C   1 
ATOM   1595 O O   . GLY A 1 228 ? 6.601  18.300  10.285  1.00 21.17  ? 361 GLY A O   1 
ATOM   1596 N N   . GLY A 1 229 ? 8.129  16.838  11.074  1.00 22.93  ? 362 GLY A N   1 
ATOM   1597 C CA  . GLY A 1 229 ? 9.014  17.874  11.583  1.00 21.71  ? 362 GLY A CA  1 
ATOM   1598 C C   . GLY A 1 229 ? 9.579  18.859  10.572  1.00 22.38  ? 362 GLY A C   1 
ATOM   1599 O O   . GLY A 1 229 ? 9.701  20.050  10.870  1.00 21.97  ? 362 GLY A O   1 
ATOM   1600 N N   . MET A 1 230 ? 9.939  18.383  9.385   1.00 21.54  ? 363 MET A N   1 
ATOM   1601 C CA  . MET A 1 230 ? 10.495 19.274  8.371   1.00 22.32  ? 363 MET A CA  1 
ATOM   1602 C C   . MET A 1 230 ? 9.497  20.380  8.022   1.00 22.31  ? 363 MET A C   1 
ATOM   1603 O O   . MET A 1 230 ? 9.830  21.569  8.064   1.00 21.64  ? 363 MET A O   1 
ATOM   1604 C CB  . MET A 1 230 ? 10.849 18.499  7.096   1.00 21.55  ? 363 MET A CB  1 
ATOM   1605 C CG  . MET A 1 230 ? 11.907 17.412  7.268   1.00 23.42  ? 363 MET A CG  1 
ATOM   1606 S SD  . MET A 1 230 ? 13.492 18.033  7.866   1.00 23.68  ? 363 MET A SD  1 
ATOM   1607 C CE  . MET A 1 230 ? 14.200 18.733  6.387   1.00 21.05  ? 363 MET A CE  1 
ATOM   1608 N N   . GLN A 1 231 ? 8.276  19.973  7.691   1.00 22.29  ? 364 GLN A N   1 
ATOM   1609 C CA  . GLN A 1 231 ? 7.220  20.900  7.308   1.00 23.63  ? 364 GLN A CA  1 
ATOM   1610 C C   . GLN A 1 231 ? 6.833  21.864  8.421   1.00 22.65  ? 364 GLN A C   1 
ATOM   1611 O O   . GLN A 1 231 ? 6.559  23.029  8.157   1.00 24.59  ? 364 GLN A O   1 
ATOM   1612 C CB  . GLN A 1 231 ? 5.980  20.128  6.832   1.00 25.65  ? 364 GLN A CB  1 
ATOM   1613 C CG  . GLN A 1 231 ? 6.244  19.190  5.647   1.00 26.96  ? 364 GLN A CG  1 
ATOM   1614 C CD  . GLN A 1 231 ? 6.671  17.785  6.072   1.00 28.82  ? 364 GLN A CD  1 
ATOM   1615 O OE1 . GLN A 1 231 ? 7.295  17.596  7.118   1.00 27.08  ? 364 GLN A OE1 1 
ATOM   1616 N NE2 . GLN A 1 231 ? 6.346  16.796  5.247   1.00 28.46  ? 364 GLN A NE2 1 
ATOM   1617 N N   . ALA A 1 232 ? 6.813  21.375  9.658   1.00 22.27  ? 365 ALA A N   1 
ATOM   1618 C CA  . ALA A 1 232 ? 6.457  22.200  10.809  1.00 22.71  ? 365 ALA A CA  1 
ATOM   1619 C C   . ALA A 1 232 ? 7.536  23.254  11.060  1.00 22.95  ? 365 ALA A C   1 
ATOM   1620 O O   . ALA A 1 232 ? 7.229  24.412  11.321  1.00 21.59  ? 365 ALA A O   1 
ATOM   1621 C CB  . ALA A 1 232 ? 6.277  21.330  12.047  1.00 21.19  ? 365 ALA A CB  1 
ATOM   1622 N N   . LEU A 1 233 ? 8.799  22.847  10.986  1.00 21.46  ? 366 LEU A N   1 
ATOM   1623 C CA  . LEU A 1 233 ? 9.898  23.785  11.184  1.00 22.34  ? 366 LEU A CA  1 
ATOM   1624 C C   . LEU A 1 233 ? 9.893  24.825  10.062  1.00 22.13  ? 366 LEU A C   1 
ATOM   1625 O O   . LEU A 1 233 ? 10.187 25.999  10.296  1.00 23.70  ? 366 LEU A O   1 
ATOM   1626 C CB  . LEU A 1 233 ? 11.240 23.039  11.221  1.00 21.15  ? 366 LEU A CB  1 
ATOM   1627 C CG  . LEU A 1 233 ? 11.472 22.161  12.467  1.00 22.82  ? 366 LEU A CG  1 
ATOM   1628 C CD1 . LEU A 1 233 ? 12.665 21.232  12.240  1.00 23.01  ? 366 LEU A CD1 1 
ATOM   1629 C CD2 . LEU A 1 233 ? 11.716 23.037  13.689  1.00 17.42  ? 366 LEU A CD2 1 
ATOM   1630 N N   . GLY A 1 234 ? 9.538  24.392  8.852   1.00 21.60  ? 367 GLY A N   1 
ATOM   1631 C CA  . GLY A 1 234 ? 9.490  25.296  7.713   1.00 21.19  ? 367 GLY A CA  1 
ATOM   1632 C C   . GLY A 1 234 ? 8.490  26.435  7.854   1.00 21.59  ? 367 GLY A C   1 
ATOM   1633 O O   . GLY A 1 234 ? 8.656  27.499  7.261   1.00 22.09  ? 367 GLY A O   1 
ATOM   1634 N N   . LEU A 1 235 ? 7.449  26.217  8.646   1.00 21.81  ? 368 LEU A N   1 
ATOM   1635 C CA  . LEU A 1 235 ? 6.426  27.236  8.868   1.00 23.03  ? 368 LEU A CA  1 
ATOM   1636 C C   . LEU A 1 235 ? 6.966  28.509  9.523   1.00 23.99  ? 368 LEU A C   1 
ATOM   1637 O O   . LEU A 1 235 ? 6.352  29.573  9.425   1.00 24.85  ? 368 LEU A O   1 
ATOM   1638 C CB  . LEU A 1 235 ? 5.323  26.677  9.771   1.00 23.82  ? 368 LEU A CB  1 
ATOM   1639 C CG  . LEU A 1 235 ? 4.423  25.544  9.269   1.00 26.16  ? 368 LEU A CG  1 
ATOM   1640 C CD1 . LEU A 1 235 ? 3.562  25.050  10.424  1.00 26.78  ? 368 LEU A CD1 1 
ATOM   1641 C CD2 . LEU A 1 235 ? 3.555  26.031  8.122   1.00 22.64  ? 368 LEU A CD2 1 
ATOM   1642 N N   . HIS A 1 236 ? 8.118  28.408  10.177  1.00 22.67  ? 369 HIS A N   1 
ATOM   1643 C CA  . HIS A 1 236 ? 8.666  29.550  10.899  1.00 23.46  ? 369 HIS A CA  1 
ATOM   1644 C C   . HIS A 1 236 ? 9.910  30.218  10.319  1.00 23.42  ? 369 HIS A C   1 
ATOM   1645 O O   . HIS A 1 236 ? 10.508 31.083  10.966  1.00 25.62  ? 369 HIS A O   1 
ATOM   1646 C CB  . HIS A 1 236 ? 8.937  29.113  12.344  1.00 21.75  ? 369 HIS A CB  1 
ATOM   1647 C CG  . HIS A 1 236 ? 7.752  28.480  13.007  1.00 21.67  ? 369 HIS A CG  1 
ATOM   1648 N ND1 . HIS A 1 236 ? 6.681  29.211  13.479  1.00 20.04  ? 369 HIS A ND1 1 
ATOM   1649 C CD2 . HIS A 1 236 ? 7.444  27.178  13.226  1.00 22.21  ? 369 HIS A CD2 1 
ATOM   1650 C CE1 . HIS A 1 236 ? 5.766  28.387  13.959  1.00 21.68  ? 369 HIS A CE1 1 
ATOM   1651 N NE2 . HIS A 1 236 ? 6.203  27.148  13.817  1.00 19.52  ? 369 HIS A NE2 1 
ATOM   1652 N N   . LEU A 1 237 ? 10.290 29.841  9.105   1.00 23.52  ? 370 LEU A N   1 
ATOM   1653 C CA  . LEU A 1 237 ? 11.485 30.399  8.484   1.00 23.02  ? 370 LEU A CA  1 
ATOM   1654 C C   . LEU A 1 237 ? 11.380 31.866  8.065   1.00 25.56  ? 370 LEU A C   1 
ATOM   1655 O O   . LEU A 1 237 ? 12.374 32.454  7.652   1.00 24.82  ? 370 LEU A O   1 
ATOM   1656 C CB  . LEU A 1 237 ? 11.901 29.537  7.286   1.00 21.50  ? 370 LEU A CB  1 
ATOM   1657 C CG  . LEU A 1 237 ? 12.262 28.086  7.648   1.00 21.22  ? 370 LEU A CG  1 
ATOM   1658 C CD1 . LEU A 1 237 ? 12.596 27.286  6.392   1.00 19.99  ? 370 LEU A CD1 1 
ATOM   1659 C CD2 . LEU A 1 237 ? 13.444 28.081  8.597   1.00 21.03  ? 370 LEU A CD2 1 
ATOM   1660 N N   . THR A 1 238 ? 10.188 32.458  8.158   1.00 26.26  ? 371 THR A N   1 
ATOM   1661 C CA  . THR A 1 238 ? 10.038 33.867  7.804   1.00 28.87  ? 371 THR A CA  1 
ATOM   1662 C C   . THR A 1 238 ? 9.649  34.688  9.036   1.00 29.21  ? 371 THR A C   1 
ATOM   1663 O O   . THR A 1 238 ? 9.213  35.834  8.925   1.00 29.44  ? 371 THR A O   1 
ATOM   1664 C CB  . THR A 1 238 ? 8.994  34.088  6.666   1.00 28.98  ? 371 THR A CB  1 
ATOM   1665 O OG1 . THR A 1 238 ? 7.687  33.697  7.103   1.00 29.63  ? 371 THR A OG1 1 
ATOM   1666 C CG2 . THR A 1 238 ? 9.373  33.271  5.437   1.00 30.38  ? 371 THR A CG2 1 
ATOM   1667 N N   . ASP A 1 239 ? 9.820  34.094  10.214  1.00 28.28  ? 372 ASP A N   1 
ATOM   1668 C CA  . ASP A 1 239 ? 9.504  34.779  11.459  1.00 26.96  ? 372 ASP A CA  1 
ATOM   1669 C C   . ASP A 1 239 ? 10.528 35.894  11.673  1.00 27.87  ? 372 ASP A C   1 
ATOM   1670 O O   . ASP A 1 239 ? 11.694 35.754  11.300  1.00 25.71  ? 372 ASP A O   1 
ATOM   1671 C CB  . ASP A 1 239 ? 9.573  33.810  12.641  1.00 27.93  ? 372 ASP A CB  1 
ATOM   1672 C CG  . ASP A 1 239 ? 8.902  34.365  13.888  1.00 28.62  ? 372 ASP A CG  1 
ATOM   1673 O OD1 . ASP A 1 239 ? 7.721  34.031  14.117  1.00 28.06  ? 372 ASP A OD1 1 
ATOM   1674 O OD2 . ASP A 1 239 ? 9.548  35.143  14.629  1.00 26.23  ? 372 ASP A OD2 1 
ATOM   1675 N N   . PRO A 1 240 ? 10.098 37.024  12.257  1.00 26.73  ? 373 PRO A N   1 
ATOM   1676 C CA  . PRO A 1 240 ? 11.003 38.149  12.510  1.00 27.31  ? 373 PRO A CA  1 
ATOM   1677 C C   . PRO A 1 240 ? 12.084 37.788  13.533  1.00 26.49  ? 373 PRO A C   1 
ATOM   1678 O O   . PRO A 1 240 ? 13.150 38.399  13.567  1.00 26.79  ? 373 PRO A O   1 
ATOM   1679 C CB  . PRO A 1 240 ? 10.063 39.234  13.030  1.00 28.84  ? 373 PRO A CB  1 
ATOM   1680 C CG  . PRO A 1 240 ? 8.787  38.940  12.301  1.00 29.81  ? 373 PRO A CG  1 
ATOM   1681 C CD  . PRO A 1 240 ? 8.694  37.435  12.439  1.00 28.75  ? 373 PRO A CD  1 
ATOM   1682 N N   . SER A 1 241 ? 11.798 36.805  14.378  1.00 23.67  ? 374 SER A N   1 
ATOM   1683 C CA  . SER A 1 241 ? 12.762 36.380  15.381  1.00 23.59  ? 374 SER A CA  1 
ATOM   1684 C C   . SER A 1 241 ? 13.894 35.610  14.710  1.00 24.74  ? 374 SER A C   1 
ATOM   1685 O O   . SER A 1 241 ? 13.686 34.505  14.201  1.00 23.88  ? 374 SER A O   1 
ATOM   1686 C CB  . SER A 1 241 ? 12.093 35.487  16.424  1.00 21.15  ? 374 SER A CB  1 
ATOM   1687 O OG  . SER A 1 241 ? 13.067 34.868  17.243  1.00 23.64  ? 374 SER A OG  1 
ATOM   1688 N N   . GLN A 1 242 ? 15.090 36.194  14.713  1.00 24.00  ? 375 GLN A N   1 
ATOM   1689 C CA  . GLN A 1 242 ? 16.244 35.550  14.100  1.00 25.83  ? 375 GLN A CA  1 
ATOM   1690 C C   . GLN A 1 242 ? 16.713 34.332  14.892  1.00 24.71  ? 375 GLN A C   1 
ATOM   1691 O O   . GLN A 1 242 ? 17.235 33.385  14.307  1.00 24.20  ? 375 GLN A O   1 
ATOM   1692 C CB  . GLN A 1 242 ? 17.387 36.561  13.929  1.00 28.64  ? 375 GLN A CB  1 
ATOM   1693 C CG  . GLN A 1 242 ? 16.984 37.767  13.070  1.00 34.04  ? 375 GLN A CG  1 
ATOM   1694 C CD  . GLN A 1 242 ? 18.109 38.770  12.865  1.00 38.04  ? 375 GLN A CD  1 
ATOM   1695 O OE1 . GLN A 1 242 ? 19.002 38.565  12.041  1.00 42.60  ? 375 GLN A OE1 1 
ATOM   1696 N NE2 . GLN A 1 242 ? 18.071 39.859  13.620  1.00 38.69  ? 375 GLN A NE2 1 
ATOM   1697 N N   . ARG A 1 243 ? 16.530 34.341  16.213  1.00 22.80  ? 376 ARG A N   1 
ATOM   1698 C CA  . ARG A 1 243 ? 16.947 33.190  17.006  1.00 22.59  ? 376 ARG A CA  1 
ATOM   1699 C C   . ARG A 1 243 ? 16.064 31.986  16.672  1.00 22.50  ? 376 ARG A C   1 
ATOM   1700 O O   . ARG A 1 243 ? 16.541 30.852  16.646  1.00 20.90  ? 376 ARG A O   1 
ATOM   1701 C CB  . ARG A 1 243 ? 16.892 33.494  18.512  1.00 25.53  ? 376 ARG A CB  1 
ATOM   1702 C CG  . ARG A 1 243 ? 15.506 33.747  19.088  1.00 24.53  ? 376 ARG A CG  1 
ATOM   1703 C CD  . ARG A 1 243 ? 15.577 33.929  20.598  1.00 23.98  ? 376 ARG A CD  1 
ATOM   1704 N NE  . ARG A 1 243 ? 14.256 34.090  21.204  1.00 21.96  ? 376 ARG A NE  1 
ATOM   1705 C CZ  . ARG A 1 243 ? 14.050 34.243  22.510  1.00 22.17  ? 376 ARG A CZ  1 
ATOM   1706 N NH1 . ARG A 1 243 ? 15.077 34.257  23.347  1.00 23.79  ? 376 ARG A NH1 1 
ATOM   1707 N NH2 . ARG A 1 243 ? 12.818 34.380  22.982  1.00 21.82  ? 376 ARG A NH2 1 
ATOM   1708 N N   . LEU A 1 244 ? 14.785 32.238  16.401  1.00 20.73  ? 377 LEU A N   1 
ATOM   1709 C CA  . LEU A 1 244 ? 13.848 31.168  16.048  1.00 22.18  ? 377 LEU A CA  1 
ATOM   1710 C C   . LEU A 1 244 ? 14.159 30.630  14.657  1.00 24.01  ? 377 LEU A C   1 
ATOM   1711 O O   . LEU A 1 244 ? 14.170 29.416  14.433  1.00 25.20  ? 377 LEU A O   1 
ATOM   1712 C CB  . LEU A 1 244 ? 12.399 31.672  16.069  1.00 17.33  ? 377 LEU A CB  1 
ATOM   1713 C CG  . LEU A 1 244 ? 11.360 30.719  15.441  1.00 17.41  ? 377 LEU A CG  1 
ATOM   1714 C CD1 . LEU A 1 244 ? 11.354 29.377  16.180  1.00 14.44  ? 377 LEU A CD1 1 
ATOM   1715 C CD2 . LEU A 1 244 ? 9.972  31.358  15.493  1.00 15.53  ? 377 LEU A CD2 1 
ATOM   1716 N N   . VAL A 1 245 ? 14.402 31.541  13.721  1.00 24.02  ? 378 VAL A N   1 
ATOM   1717 C CA  . VAL A 1 245 ? 14.711 31.156  12.352  1.00 23.90  ? 378 VAL A CA  1 
ATOM   1718 C C   . VAL A 1 245 ? 15.999 30.334  12.306  1.00 25.15  ? 378 VAL A C   1 
ATOM   1719 O O   . VAL A 1 245 ? 16.036 29.267  11.693  1.00 24.17  ? 378 VAL A O   1 
ATOM   1720 C CB  . VAL A 1 245 ? 14.848 32.402  11.445  1.00 23.28  ? 378 VAL A CB  1 
ATOM   1721 C CG1 . VAL A 1 245 ? 15.400 32.016  10.073  1.00 22.78  ? 378 VAL A CG1 1 
ATOM   1722 C CG2 . VAL A 1 245 ? 13.487 33.058  11.278  1.00 21.35  ? 378 VAL A CG2 1 
ATOM   1723 N N   . GLN A 1 246 ? 17.043 30.810  12.976  1.00 24.22  ? 379 GLN A N   1 
ATOM   1724 C CA  . GLN A 1 246 ? 18.316 30.100  12.971  1.00 25.12  ? 379 GLN A CA  1 
ATOM   1725 C C   . GLN A 1 246 ? 18.221 28.707  13.597  1.00 23.98  ? 379 GLN A C   1 
ATOM   1726 O O   . GLN A 1 246 ? 18.793 27.752  13.082  1.00 24.25  ? 379 GLN A O   1 
ATOM   1727 C CB  . GLN A 1 246 ? 19.394 30.918  13.685  1.00 24.81  ? 379 GLN A CB  1 
ATOM   1728 C CG  . GLN A 1 246 ? 20.809 30.357  13.495  1.00 30.67  ? 379 GLN A CG  1 
ATOM   1729 C CD  . GLN A 1 246 ? 21.147 30.085  12.029  1.00 34.79  ? 379 GLN A CD  1 
ATOM   1730 O OE1 . GLN A 1 246 ? 21.044 28.950  11.551  1.00 37.42  ? 379 GLN A OE1 1 
ATOM   1731 N NE2 . GLN A 1 246 ? 21.538 31.129  11.308  1.00 36.83  ? 379 GLN A NE2 1 
ATOM   1732 N N   . ASN A 1 247 ? 17.505 28.592  14.710  1.00 22.20  ? 380 ASN A N   1 
ATOM   1733 C CA  . ASN A 1 247 ? 17.353 27.302  15.358  1.00 22.35  ? 380 ASN A CA  1 
ATOM   1734 C C   . ASN A 1 247 ? 16.559 26.339  14.492  1.00 22.86  ? 380 ASN A C   1 
ATOM   1735 O O   . ASN A 1 247 ? 16.842 25.135  14.481  1.00 21.56  ? 380 ASN A O   1 
ATOM   1736 C CB  . ASN A 1 247 ? 16.706 27.464  16.729  1.00 23.80  ? 380 ASN A CB  1 
ATOM   1737 C CG  . ASN A 1 247 ? 17.722 27.772  17.801  1.00 25.45  ? 380 ASN A CG  1 
ATOM   1738 O OD1 . ASN A 1 247 ? 18.434 26.883  18.261  1.00 29.92  ? 380 ASN A OD1 1 
ATOM   1739 N ND2 . ASN A 1 247 ? 17.815 29.036  18.189  1.00 29.43  ? 380 ASN A ND2 1 
ATOM   1740 N N   . CYS A 1 248 ? 15.571 26.856  13.762  1.00 20.20  ? 381 CYS A N   1 
ATOM   1741 C CA  . CYS A 1 248 ? 14.802 25.998  12.867  1.00 20.77  ? 381 CYS A CA  1 
ATOM   1742 C C   . CYS A 1 248 ? 15.722 25.537  11.737  1.00 20.62  ? 381 CYS A C   1 
ATOM   1743 O O   . CYS A 1 248 ? 15.758 24.350  11.398  1.00 20.04  ? 381 CYS A O   1 
ATOM   1744 C CB  . CYS A 1 248 ? 13.585 26.743  12.298  1.00 20.47  ? 381 CYS A CB  1 
ATOM   1745 S SG  . CYS A 1 248 ? 12.212 26.903  13.484  1.00 21.30  ? 381 CYS A SG  1 
ATOM   1746 N N   . LEU A 1 249 ? 16.490 26.469  11.174  1.00 20.37  ? 382 LEU A N   1 
ATOM   1747 C CA  . LEU A 1 249 ? 17.407 26.134  10.084  1.00 21.51  ? 382 LEU A CA  1 
ATOM   1748 C C   . LEU A 1 249 ? 18.455 25.090  10.475  1.00 21.24  ? 382 LEU A C   1 
ATOM   1749 O O   . LEU A 1 249 ? 18.726 24.174  9.698   1.00 21.71  ? 382 LEU A O   1 
ATOM   1750 C CB  . LEU A 1 249 ? 18.099 27.396  9.548   1.00 20.08  ? 382 LEU A CB  1 
ATOM   1751 C CG  . LEU A 1 249 ? 17.246 28.321  8.662   1.00 23.09  ? 382 LEU A CG  1 
ATOM   1752 C CD1 . LEU A 1 249 ? 18.024 29.600  8.344   1.00 21.10  ? 382 LEU A CD1 1 
ATOM   1753 C CD2 . LEU A 1 249 ? 16.874 27.598  7.367   1.00 21.16  ? 382 LEU A CD2 1 
ATOM   1754 N N   . TRP A 1 250 ? 19.051 25.225  11.659  1.00 21.71  ? 383 TRP A N   1 
ATOM   1755 C CA  . TRP A 1 250 ? 20.046 24.247  12.105  1.00 25.03  ? 383 TRP A CA  1 
ATOM   1756 C C   . TRP A 1 250 ? 19.407 22.872  12.252  1.00 24.17  ? 383 TRP A C   1 
ATOM   1757 O O   . TRP A 1 250 ? 19.969 21.856  11.836  1.00 24.79  ? 383 TRP A O   1 
ATOM   1758 C CB  . TRP A 1 250 ? 20.665 24.643  13.452  1.00 24.97  ? 383 TRP A CB  1 
ATOM   1759 C CG  . TRP A 1 250 ? 21.701 25.721  13.361  1.00 31.48  ? 383 TRP A CG  1 
ATOM   1760 C CD1 . TRP A 1 250 ? 22.610 25.903  12.355  1.00 31.71  ? 383 TRP A CD1 1 
ATOM   1761 C CD2 . TRP A 1 250 ? 21.972 26.735  14.337  1.00 33.15  ? 383 TRP A CD2 1 
ATOM   1762 N NE1 . TRP A 1 250 ? 23.428 26.969  12.644  1.00 35.85  ? 383 TRP A NE1 1 
ATOM   1763 C CE2 . TRP A 1 250 ? 23.059 27.498  13.854  1.00 36.03  ? 383 TRP A CE2 1 
ATOM   1764 C CE3 . TRP A 1 250 ? 21.403 27.072  15.573  1.00 36.68  ? 383 TRP A CE3 1 
ATOM   1765 C CZ2 . TRP A 1 250 ? 23.591 28.582  14.567  1.00 36.33  ? 383 TRP A CZ2 1 
ATOM   1766 C CZ3 . TRP A 1 250 ? 21.932 28.152  16.284  1.00 38.43  ? 383 TRP A CZ3 1 
ATOM   1767 C CH2 . TRP A 1 250 ? 23.016 28.893  15.774  1.00 38.10  ? 383 TRP A CH2 1 
ATOM   1768 N N   . THR A 1 251 ? 18.228 22.845  12.860  1.00 22.59  ? 384 THR A N   1 
ATOM   1769 C CA  . THR A 1 251 ? 17.522 21.595  13.065  1.00 22.71  ? 384 THR A CA  1 
ATOM   1770 C C   . THR A 1 251 ? 17.168 20.964  11.726  1.00 22.06  ? 384 THR A C   1 
ATOM   1771 O O   . THR A 1 251 ? 17.399 19.771  11.515  1.00 22.04  ? 384 THR A O   1 
ATOM   1772 C CB  . THR A 1 251 ? 16.247 21.826  13.889  1.00 20.85  ? 384 THR A CB  1 
ATOM   1773 O OG1 . THR A 1 251 ? 16.593 22.531  15.080  1.00 21.88  ? 384 THR A OG1 1 
ATOM   1774 C CG2 . THR A 1 251 ? 15.606 20.503  14.265  1.00 18.69  ? 384 THR A CG2 1 
ATOM   1775 N N   . LEU A 1 252 ? 16.619 21.767  10.820  1.00 21.08  ? 385 LEU A N   1 
ATOM   1776 C CA  . LEU A 1 252 ? 16.246 21.278  9.491   1.00 21.36  ? 385 LEU A CA  1 
ATOM   1777 C C   . LEU A 1 252 ? 17.444 20.654  8.776   1.00 22.56  ? 385 LEU A C   1 
ATOM   1778 O O   . LEU A 1 252 ? 17.323 19.613  8.127   1.00 18.59  ? 385 LEU A O   1 
ATOM   1779 C CB  . LEU A 1 252 ? 15.700 22.422  8.635   1.00 19.96  ? 385 LEU A CB  1 
ATOM   1780 C CG  . LEU A 1 252 ? 14.257 22.871  8.883   1.00 22.64  ? 385 LEU A CG  1 
ATOM   1781 C CD1 . LEU A 1 252 ? 14.016 24.232  8.231   1.00 20.23  ? 385 LEU A CD1 1 
ATOM   1782 C CD2 . LEU A 1 252 ? 13.305 21.818  8.319   1.00 17.28  ? 385 LEU A CD2 1 
ATOM   1783 N N   . ARG A 1 253 ? 18.601 21.295  8.899   1.00 22.59  ? 386 ARG A N   1 
ATOM   1784 C CA  . ARG A 1 253 ? 19.795 20.790  8.245   1.00 23.00  ? 386 ARG A CA  1 
ATOM   1785 C C   . ARG A 1 253 ? 20.264 19.464  8.836   1.00 23.86  ? 386 ARG A C   1 
ATOM   1786 O O   . ARG A 1 253 ? 20.692 18.575  8.096   1.00 22.17  ? 386 ARG A O   1 
ATOM   1787 C CB  . ARG A 1 253 ? 20.935 21.809  8.314   1.00 23.34  ? 386 ARG A CB  1 
ATOM   1788 C CG  . ARG A 1 253 ? 22.159 21.335  7.538   1.00 24.66  ? 386 ARG A CG  1 
ATOM   1789 C CD  . ARG A 1 253 ? 23.250 22.369  7.493   1.00 26.97  ? 386 ARG A CD  1 
ATOM   1790 N NE  . ARG A 1 253 ? 23.823 22.625  8.807   1.00 29.44  ? 386 ARG A NE  1 
ATOM   1791 C CZ  . ARG A 1 253 ? 24.830 23.465  9.019   1.00 33.87  ? 386 ARG A CZ  1 
ATOM   1792 N NH1 . ARG A 1 253 ? 25.367 24.121  7.998   1.00 31.71  ? 386 ARG A NH1 1 
ATOM   1793 N NH2 . ARG A 1 253 ? 25.296 23.652  10.248  1.00 33.99  ? 386 ARG A NH2 1 
ATOM   1794 N N   . ASN A 1 254 ? 20.203 19.340  10.162  1.00 23.07  ? 387 ASN A N   1 
ATOM   1795 C CA  . ASN A 1 254 ? 20.614 18.101  10.827  1.00 23.69  ? 387 ASN A CA  1 
ATOM   1796 C C   . ASN A 1 254 ? 19.703 16.944  10.401  1.00 23.08  ? 387 ASN A C   1 
ATOM   1797 O O   . ASN A 1 254 ? 20.147 15.801  10.246  1.00 21.15  ? 387 ASN A O   1 
ATOM   1798 C CB  . ASN A 1 254 ? 20.533 18.250  12.352  1.00 24.30  ? 387 ASN A CB  1 
ATOM   1799 C CG  . ASN A 1 254 ? 21.605 19.167  12.917  1.00 23.93  ? 387 ASN A CG  1 
ATOM   1800 O OD1 . ASN A 1 254 ? 22.651 19.375  12.307  1.00 24.82  ? 387 ASN A OD1 1 
ATOM   1801 N ND2 . ASN A 1 254 ? 21.353 19.701  14.107  1.00 22.57  ? 387 ASN A ND2 1 
ATOM   1802 N N   . LEU A 1 255 ? 18.428 17.262  10.212  1.00 21.45  ? 388 LEU A N   1 
ATOM   1803 C CA  . LEU A 1 255 ? 17.411 16.286  9.823   1.00 20.65  ? 388 LEU A CA  1 
ATOM   1804 C C   . LEU A 1 255 ? 17.356 15.975  8.326   1.00 20.42  ? 388 LEU A C   1 
ATOM   1805 O O   . LEU A 1 255 ? 16.920 14.892  7.934   1.00 21.90  ? 388 LEU A O   1 
ATOM   1806 C CB  . LEU A 1 255 ? 16.022 16.795  10.232  1.00 20.45  ? 388 LEU A CB  1 
ATOM   1807 C CG  . LEU A 1 255 ? 15.651 17.050  11.697  1.00 23.05  ? 388 LEU A CG  1 
ATOM   1808 C CD1 . LEU A 1 255 ? 14.315 17.786  11.778  1.00 18.82  ? 388 LEU A CD1 1 
ATOM   1809 C CD2 . LEU A 1 255 ? 15.565 15.731  12.438  1.00 20.98  ? 388 LEU A CD2 1 
ATOM   1810 N N   . SER A 1 256 ? 17.795 16.925  7.501   1.00 21.42  ? 389 SER A N   1 
ATOM   1811 C CA  . SER A 1 256 ? 17.703 16.808  6.046   1.00 21.53  ? 389 SER A CA  1 
ATOM   1812 C C   . SER A 1 256 ? 18.181 15.542  5.343   1.00 23.76  ? 389 SER A C   1 
ATOM   1813 O O   . SER A 1 256 ? 17.555 15.119  4.372   1.00 22.21  ? 389 SER A O   1 
ATOM   1814 C CB  . SER A 1 256 ? 18.341 18.034  5.372   1.00 21.03  ? 389 SER A CB  1 
ATOM   1815 O OG  . SER A 1 256 ? 19.732 18.120  5.620   1.00 22.29  ? 389 SER A OG  1 
ATOM   1816 N N   . ASP A 1 257 ? 19.268 14.929  5.807   1.00 25.10  ? 390 ASP A N   1 
ATOM   1817 C CA  . ASP A 1 257 ? 19.754 13.718  5.148   1.00 28.72  ? 390 ASP A CA  1 
ATOM   1818 C C   . ASP A 1 257 ? 18.779 12.547  5.310   1.00 28.61  ? 390 ASP A C   1 
ATOM   1819 O O   . ASP A 1 257 ? 18.880 11.547  4.604   1.00 29.65  ? 390 ASP A O   1 
ATOM   1820 C CB  . ASP A 1 257 ? 21.144 13.329  5.677   1.00 31.28  ? 390 ASP A CB  1 
ATOM   1821 C CG  . ASP A 1 257 ? 21.129 12.930  7.139   1.00 35.59  ? 390 ASP A CG  1 
ATOM   1822 O OD1 . ASP A 1 257 ? 20.550 13.672  7.956   1.00 37.57  ? 390 ASP A OD1 1 
ATOM   1823 O OD2 . ASP A 1 257 ? 21.707 11.877  7.475   1.00 40.02  ? 390 ASP A OD2 1 
ATOM   1824 N N   . ALA A 1 258 ? 17.827 12.679  6.230   1.00 26.41  ? 391 ALA A N   1 
ATOM   1825 C CA  . ALA A 1 258 ? 16.843 11.623  6.453   1.00 25.62  ? 391 ALA A CA  1 
ATOM   1826 C C   . ALA A 1 258 ? 15.441 12.029  5.990   1.00 24.73  ? 391 ALA A C   1 
ATOM   1827 O O   . ALA A 1 258 ? 14.457 11.354  6.303   1.00 23.60  ? 391 ALA A O   1 
ATOM   1828 C CB  . ALA A 1 258 ? 16.811 11.251  7.933   1.00 26.49  ? 391 ALA A CB  1 
ATOM   1829 N N   . ALA A 1 259 ? 15.345 13.115  5.227   1.00 23.55  ? 392 ALA A N   1 
ATOM   1830 C CA  . ALA A 1 259 ? 14.039 13.600  4.780   1.00 25.61  ? 392 ALA A CA  1 
ATOM   1831 C C   . ALA A 1 259 ? 13.828 13.629  3.268   1.00 25.31  ? 392 ALA A C   1 
ATOM   1832 O O   . ALA A 1 259 ? 12.883 14.263  2.790   1.00 25.32  ? 392 ALA A O   1 
ATOM   1833 C CB  . ALA A 1 259 ? 13.797 15.004  5.358   1.00 23.03  ? 392 ALA A CB  1 
ATOM   1834 N N   . THR A 1 260 ? 14.673 12.931  2.514   1.00 24.95  ? 393 THR A N   1 
ATOM   1835 C CA  . THR A 1 260 ? 14.557 12.954  1.054   1.00 27.23  ? 393 THR A CA  1 
ATOM   1836 C C   . THR A 1 260 ? 13.344 12.244  0.459   1.00 29.16  ? 393 THR A C   1 
ATOM   1837 O O   . THR A 1 260 ? 13.110 12.329  -0.751  1.00 30.60  ? 393 THR A O   1 
ATOM   1838 C CB  . THR A 1 260 ? 15.835 12.400  0.378   1.00 27.43  ? 393 THR A CB  1 
ATOM   1839 O OG1 . THR A 1 260 ? 15.928 10.984  0.586   1.00 28.82  ? 393 THR A OG1 1 
ATOM   1840 C CG2 . THR A 1 260 ? 17.062 13.068  0.969   1.00 24.69  ? 393 THR A CG2 1 
ATOM   1841 N N   . LYS A 1 261 ? 12.571 11.558  1.298   1.00 29.03  ? 394 LYS A N   1 
ATOM   1842 C CA  . LYS A 1 261 ? 11.380 10.854  0.829   1.00 30.39  ? 394 LYS A CA  1 
ATOM   1843 C C   . LYS A 1 261 ? 10.083 11.526  1.294   1.00 30.11  ? 394 LYS A C   1 
ATOM   1844 O O   . LYS A 1 261 ? 8.992  11.054  0.982   1.00 29.49  ? 394 LYS A O   1 
ATOM   1845 C CB  . LYS A 1 261 ? 11.399 9.390   1.303   1.00 30.59  ? 394 LYS A CB  1 
ATOM   1846 C CG  . LYS A 1 261 ? 12.543 8.555   0.720   1.00 33.86  ? 394 LYS A CG  1 
ATOM   1847 C CD  . LYS A 1 261 ? 12.452 8.491   -0.803  1.00 37.62  ? 394 LYS A CD  1 
ATOM   1848 C CE  . LYS A 1 261 ? 13.608 7.703   -1.420  1.00 39.32  ? 394 LYS A CE  1 
ATOM   1849 N NZ  . LYS A 1 261 ? 14.922 8.393   -1.277  1.00 39.59  ? 394 LYS A NZ  1 
ATOM   1850 N N   . GLN A 1 262 ? 10.202 12.625  2.036   1.00 28.73  ? 395 GLN A N   1 
ATOM   1851 C CA  . GLN A 1 262 ? 9.026  13.346  2.531   1.00 28.30  ? 395 GLN A CA  1 
ATOM   1852 C C   . GLN A 1 262 ? 8.251  14.062  1.426   1.00 28.95  ? 395 GLN A C   1 
ATOM   1853 O O   . GLN A 1 262 ? 8.838  14.535  0.451   1.00 28.65  ? 395 GLN A O   1 
ATOM   1854 C CB  . GLN A 1 262 ? 9.441  14.374  3.592   1.00 27.63  ? 395 GLN A CB  1 
ATOM   1855 C CG  . GLN A 1 262 ? 9.649  13.806  4.988   1.00 26.60  ? 395 GLN A CG  1 
ATOM   1856 C CD  . GLN A 1 262 ? 8.349  13.331  5.621   1.00 27.94  ? 395 GLN A CD  1 
ATOM   1857 O OE1 . GLN A 1 262 ? 7.378  14.085  5.717   1.00 27.26  ? 395 GLN A OE1 1 
ATOM   1858 N NE2 . GLN A 1 262 ? 8.327  12.076  6.058   1.00 26.22  ? 395 GLN A NE2 1 
ATOM   1859 N N   . GLU A 1 263 ? 6.932  14.137  1.594   1.00 29.19  ? 396 GLU A N   1 
ATOM   1860 C CA  . GLU A 1 263 ? 6.038  14.811  0.654   1.00 30.00  ? 396 GLU A CA  1 
ATOM   1861 C C   . GLU A 1 263 ? 5.524  16.087  1.331   1.00 29.47  ? 396 GLU A C   1 
ATOM   1862 O O   . GLU A 1 263 ? 5.784  16.309  2.514   1.00 29.71  ? 396 GLU A O   1 
ATOM   1863 C CB  . GLU A 1 263 ? 4.862  13.895  0.294   1.00 35.10  ? 396 GLU A CB  1 
ATOM   1864 C CG  . GLU A 1 263 ? 5.259  12.646  -0.481  1.00 40.64  ? 396 GLU A CG  1 
ATOM   1865 C CD  . GLU A 1 263 ? 5.457  12.913  -1.966  1.00 46.77  ? 396 GLU A CD  1 
ATOM   1866 O OE1 . GLU A 1 263 ? 5.945  14.009  -2.320  1.00 50.62  ? 396 GLU A OE1 1 
ATOM   1867 O OE2 . GLU A 1 263 ? 5.135  12.021  -2.782  1.00 49.79  ? 396 GLU A OE2 1 
ATOM   1868 N N   . GLY A 1 264 ? 4.799  16.920  0.588   1.00 28.08  ? 397 GLY A N   1 
ATOM   1869 C CA  . GLY A 1 264 ? 4.291  18.163  1.148   1.00 27.17  ? 397 GLY A CA  1 
ATOM   1870 C C   . GLY A 1 264 ? 5.411  19.122  1.532   1.00 28.20  ? 397 GLY A C   1 
ATOM   1871 O O   . GLY A 1 264 ? 5.291  19.871  2.505   1.00 26.28  ? 397 GLY A O   1 
ATOM   1872 N N   . MET A 1 265 ? 6.493  19.105  0.755   1.00 28.31  ? 398 MET A N   1 
ATOM   1873 C CA  . MET A 1 265 ? 7.664  19.949  1.008   1.00 30.12  ? 398 MET A CA  1 
ATOM   1874 C C   . MET A 1 265 ? 7.708  21.230  0.172   1.00 30.19  ? 398 MET A C   1 
ATOM   1875 O O   . MET A 1 265 ? 8.659  22.006  0.280   1.00 30.62  ? 398 MET A O   1 
ATOM   1876 C CB  . MET A 1 265 ? 8.948  19.149  0.741   1.00 31.08  ? 398 MET A CB  1 
ATOM   1877 C CG  . MET A 1 265 ? 9.102  17.881  1.568   1.00 30.37  ? 398 MET A CG  1 
ATOM   1878 S SD  . MET A 1 265 ? 9.472  18.190  3.308   1.00 30.50  ? 398 MET A SD  1 
ATOM   1879 C CE  . MET A 1 265 ? 11.278 18.150  3.307   1.00 28.78  ? 398 MET A CE  1 
ATOM   1880 N N   . GLU A 1 266 ? 6.691  21.454  -0.655  1.00 31.67  ? 399 GLU A N   1 
ATOM   1881 C CA  . GLU A 1 266 ? 6.642  22.639  -1.514  1.00 31.33  ? 399 GLU A CA  1 
ATOM   1882 C C   . GLU A 1 266 ? 6.932  23.950  -0.789  1.00 30.55  ? 399 GLU A C   1 
ATOM   1883 O O   . GLU A 1 266 ? 7.822  24.711  -1.184  1.00 27.89  ? 399 GLU A O   1 
ATOM   1884 C CB  . GLU A 1 266 ? 5.272  22.765  -2.188  1.00 36.11  ? 399 GLU A CB  1 
ATOM   1885 C CG  . GLU A 1 266 ? 4.873  21.619  -3.109  1.00 40.50  ? 399 GLU A CG  1 
ATOM   1886 C CD  . GLU A 1 266 ? 4.587  20.325  -2.366  1.00 44.03  ? 399 GLU A CD  1 
ATOM   1887 O OE1 . GLU A 1 266 ? 3.974  20.381  -1.276  1.00 43.39  ? 399 GLU A OE1 1 
ATOM   1888 O OE2 . GLU A 1 266 ? 4.960  19.249  -2.884  1.00 47.38  ? 399 GLU A OE2 1 
ATOM   1889 N N   . GLY A 1 267 ? 6.161  24.217  0.261   1.00 28.45  ? 400 GLY A N   1 
ATOM   1890 C CA  . GLY A 1 267 ? 6.329  25.445  1.015   1.00 26.75  ? 400 GLY A CA  1 
ATOM   1891 C C   . GLY A 1 267 ? 7.724  25.638  1.570   1.00 24.90  ? 400 GLY A C   1 
ATOM   1892 O O   . GLY A 1 267 ? 8.305  26.712  1.454   1.00 25.70  ? 400 GLY A O   1 
ATOM   1893 N N   . LEU A 1 268 ? 8.261  24.594  2.185   1.00 25.02  ? 401 LEU A N   1 
ATOM   1894 C CA  . LEU A 1 268 ? 9.600  24.649  2.756   1.00 23.21  ? 401 LEU A CA  1 
ATOM   1895 C C   . LEU A 1 268 ? 10.631 24.947  1.659   1.00 24.12  ? 401 LEU A C   1 
ATOM   1896 O O   . LEU A 1 268 ? 11.508 25.798  1.826   1.00 24.21  ? 401 LEU A O   1 
ATOM   1897 C CB  . LEU A 1 268 ? 9.917  23.312  3.427   1.00 23.31  ? 401 LEU A CB  1 
ATOM   1898 C CG  . LEU A 1 268 ? 11.354 23.043  3.873   1.00 22.43  ? 401 LEU A CG  1 
ATOM   1899 C CD1 . LEU A 1 268 ? 11.811 24.119  4.837   1.00 20.88  ? 401 LEU A CD1 1 
ATOM   1900 C CD2 . LEU A 1 268 ? 11.426 21.673  4.524   1.00 23.11  ? 401 LEU A CD2 1 
ATOM   1901 N N   . LEU A 1 269 ? 10.517 24.236  0.540   1.00 24.70  ? 402 LEU A N   1 
ATOM   1902 C CA  . LEU A 1 269 ? 11.435 24.410  -0.586  1.00 24.77  ? 402 LEU A CA  1 
ATOM   1903 C C   . LEU A 1 269 ? 11.403 25.848  -1.087  1.00 23.94  ? 402 LEU A C   1 
ATOM   1904 O O   . LEU A 1 269 ? 12.444 26.457  -1.314  1.00 23.58  ? 402 LEU A O   1 
ATOM   1905 C CB  . LEU A 1 269 ? 11.063 23.447  -1.721  1.00 25.23  ? 402 LEU A CB  1 
ATOM   1906 C CG  . LEU A 1 269 ? 11.844 22.139  -1.954  1.00 27.14  ? 402 LEU A CG  1 
ATOM   1907 C CD1 . LEU A 1 269 ? 12.757 21.806  -0.793  1.00 23.80  ? 402 LEU A CD1 1 
ATOM   1908 C CD2 . LEU A 1 269 ? 10.849 21.015  -2.215  1.00 22.77  ? 402 LEU A CD2 1 
ATOM   1909 N N   . GLY A 1 270 ? 10.201 26.392  -1.246  1.00 25.07  ? 403 GLY A N   1 
ATOM   1910 C CA  . GLY A 1 270 ? 10.073 27.759  -1.714  1.00 24.77  ? 403 GLY A CA  1 
ATOM   1911 C C   . GLY A 1 270 ? 10.771 28.748  -0.799  1.00 25.02  ? 403 GLY A C   1 
ATOM   1912 O O   . GLY A 1 270 ? 11.484 29.638  -1.260  1.00 24.53  ? 403 GLY A O   1 
ATOM   1913 N N   . THR A 1 271 ? 10.576 28.595  0.507   1.00 23.92  ? 404 THR A N   1 
ATOM   1914 C CA  . THR A 1 271 ? 11.201 29.502  1.462   1.00 24.34  ? 404 THR A CA  1 
ATOM   1915 C C   . THR A 1 271 ? 12.730 29.381  1.470   1.00 24.02  ? 404 THR A C   1 
ATOM   1916 O O   . THR A 1 271 ? 13.440 30.388  1.549   1.00 22.52  ? 404 THR A O   1 
ATOM   1917 C CB  . THR A 1 271 ? 10.676 29.250  2.894   1.00 26.11  ? 404 THR A CB  1 
ATOM   1918 O OG1 . THR A 1 271 ? 9.246  29.368  2.913   1.00 27.97  ? 404 THR A OG1 1 
ATOM   1919 C CG2 . THR A 1 271 ? 11.275 30.258  3.856   1.00 25.49  ? 404 THR A CG2 1 
ATOM   1920 N N   . LEU A 1 272 ? 13.236 28.153  1.396   1.00 22.90  ? 405 LEU A N   1 
ATOM   1921 C CA  . LEU A 1 272 ? 14.683 27.936  1.402   1.00 23.53  ? 405 LEU A CA  1 
ATOM   1922 C C   . LEU A 1 272 ? 15.342 28.654  0.229   1.00 23.10  ? 405 LEU A C   1 
ATOM   1923 O O   . LEU A 1 272 ? 16.418 29.234  0.377   1.00 24.23  ? 405 LEU A O   1 
ATOM   1924 C CB  . LEU A 1 272 ? 15.003 26.433  1.358   1.00 22.40  ? 405 LEU A CB  1 
ATOM   1925 C CG  . LEU A 1 272 ? 14.648 25.647  2.629   1.00 24.58  ? 405 LEU A CG  1 
ATOM   1926 C CD1 . LEU A 1 272 ? 14.692 24.149  2.345   1.00 22.53  ? 405 LEU A CD1 1 
ATOM   1927 C CD2 . LEU A 1 272 ? 15.617 26.009  3.758   1.00 22.27  ? 405 LEU A CD2 1 
ATOM   1928 N N   . VAL A 1 273 ? 14.700 28.625  -0.935  1.00 24.66  ? 406 VAL A N   1 
ATOM   1929 C CA  . VAL A 1 273 ? 15.254 29.300  -2.104  1.00 24.08  ? 406 VAL A CA  1 
ATOM   1930 C C   . VAL A 1 273 ? 15.334 30.807  -1.844  1.00 25.89  ? 406 VAL A C   1 
ATOM   1931 O O   . VAL A 1 273 ? 16.326 31.453  -2.184  1.00 24.05  ? 406 VAL A O   1 
ATOM   1932 C CB  . VAL A 1 273 ? 14.405 29.020  -3.371  1.00 24.22  ? 406 VAL A CB  1 
ATOM   1933 C CG1 . VAL A 1 273 ? 14.867 29.901  -4.523  1.00 21.55  ? 406 VAL A CG1 1 
ATOM   1934 C CG2 . VAL A 1 273 ? 14.545 27.550  -3.770  1.00 23.45  ? 406 VAL A CG2 1 
ATOM   1935 N N   . GLN A 1 274 ? 14.296 31.366  -1.228  1.00 26.74  ? 407 GLN A N   1 
ATOM   1936 C CA  . GLN A 1 274 ? 14.286 32.794  -0.919  1.00 28.34  ? 407 GLN A CA  1 
ATOM   1937 C C   . GLN A 1 274 ? 15.405 33.140  0.062   1.00 27.24  ? 407 GLN A C   1 
ATOM   1938 O O   . GLN A 1 274 ? 16.089 34.152  -0.094  1.00 27.41  ? 407 GLN A O   1 
ATOM   1939 C CB  . GLN A 1 274 ? 12.943 33.201  -0.308  1.00 32.97  ? 407 GLN A CB  1 
ATOM   1940 C CG  . GLN A 1 274 ? 11.745 32.998  -1.220  1.00 41.10  ? 407 GLN A CG  1 
ATOM   1941 C CD  . GLN A 1 274 ? 10.437 33.390  -0.551  1.00 45.05  ? 407 GLN A CD  1 
ATOM   1942 O OE1 . GLN A 1 274 ? 10.268 34.529  -0.115  1.00 48.93  ? 407 GLN A OE1 1 
ATOM   1943 N NE2 . GLN A 1 274 ? 9.506  32.446  -0.467  1.00 48.32  ? 407 GLN A NE2 1 
ATOM   1944 N N   . LEU A 1 275 ? 15.595 32.300  1.075   1.00 25.77  ? 408 LEU A N   1 
ATOM   1945 C CA  . LEU A 1 275 ? 16.632 32.548  2.071   1.00 24.79  ? 408 LEU A CA  1 
ATOM   1946 C C   . LEU A 1 275 ? 18.040 32.540  1.486   1.00 25.90  ? 408 LEU A C   1 
ATOM   1947 O O   . LEU A 1 275 ? 18.986 32.998  2.130   1.00 25.91  ? 408 LEU A O   1 
ATOM   1948 C CB  . LEU A 1 275 ? 16.536 31.528  3.210   1.00 23.28  ? 408 LEU A CB  1 
ATOM   1949 C CG  . LEU A 1 275 ? 15.258 31.586  4.066   1.00 24.31  ? 408 LEU A CG  1 
ATOM   1950 C CD1 . LEU A 1 275 ? 15.293 30.471  5.102   1.00 23.79  ? 408 LEU A CD1 1 
ATOM   1951 C CD2 . LEU A 1 275 ? 15.141 32.941  4.755   1.00 22.64  ? 408 LEU A CD2 1 
ATOM   1952 N N   . LEU A 1 276 ? 18.189 32.019  0.272   1.00 26.56  ? 409 LEU A N   1 
ATOM   1953 C CA  . LEU A 1 276 ? 19.503 31.992  -0.364  1.00 28.93  ? 409 LEU A CA  1 
ATOM   1954 C C   . LEU A 1 276 ? 19.978 33.415  -0.668  1.00 30.12  ? 409 LEU A C   1 
ATOM   1955 O O   . LEU A 1 276 ? 21.164 33.649  -0.888  1.00 30.99  ? 409 LEU A O   1 
ATOM   1956 C CB  . LEU A 1 276 ? 19.459 31.175  -1.661  1.00 27.87  ? 409 LEU A CB  1 
ATOM   1957 C CG  . LEU A 1 276 ? 19.317 29.651  -1.538  1.00 28.27  ? 409 LEU A CG  1 
ATOM   1958 C CD1 . LEU A 1 276 ? 19.193 29.039  -2.925  1.00 27.13  ? 409 LEU A CD1 1 
ATOM   1959 C CD2 . LEU A 1 276 ? 20.535 29.076  -0.811  1.00 26.20  ? 409 LEU A CD2 1 
ATOM   1960 N N   . GLY A 1 277 ? 19.047 34.362  -0.668  1.00 31.14  ? 410 GLY A N   1 
ATOM   1961 C CA  . GLY A 1 277 ? 19.401 35.742  -0.950  1.00 33.80  ? 410 GLY A CA  1 
ATOM   1962 C C   . GLY A 1 277 ? 19.655 36.573  0.296   1.00 35.62  ? 410 GLY A C   1 
ATOM   1963 O O   . GLY A 1 277 ? 19.863 37.783  0.210   1.00 34.81  ? 410 GLY A O   1 
ATOM   1964 N N   . SER A 1 278 ? 19.643 35.925  1.456   1.00 35.46  ? 411 SER A N   1 
ATOM   1965 C CA  . SER A 1 278 ? 19.873 36.617  2.719   1.00 35.74  ? 411 SER A CA  1 
ATOM   1966 C C   . SER A 1 278 ? 21.302 37.148  2.825   1.00 36.60  ? 411 SER A C   1 
ATOM   1967 O O   . SER A 1 278 ? 22.204 36.670  2.141   1.00 36.04  ? 411 SER A O   1 
ATOM   1968 C CB  . SER A 1 278 ? 19.589 35.664  3.886   1.00 35.09  ? 411 SER A CB  1 
ATOM   1969 O OG  . SER A 1 278 ? 19.947 36.242  5.132   1.00 33.88  ? 411 SER A OG  1 
ATOM   1970 N N   . ASP A 1 279 ? 21.501 38.144  3.681   1.00 39.38  ? 412 ASP A N   1 
ATOM   1971 C CA  . ASP A 1 279 ? 22.827 38.714  3.893   1.00 41.83  ? 412 ASP A CA  1 
ATOM   1972 C C   . ASP A 1 279 ? 23.479 38.049  5.094   1.00 41.77  ? 412 ASP A C   1 
ATOM   1973 O O   . ASP A 1 279 ? 24.648 38.288  5.395   1.00 42.54  ? 412 ASP A O   1 
ATOM   1974 C CB  . ASP A 1 279 ? 22.740 40.219  4.129   1.00 45.39  ? 412 ASP A CB  1 
ATOM   1975 C CG  . ASP A 1 279 ? 22.474 40.987  2.858   1.00 49.54  ? 412 ASP A CG  1 
ATOM   1976 O OD1 . ASP A 1 279 ? 23.211 40.763  1.872   1.00 51.75  ? 412 ASP A OD1 1 
ATOM   1977 O OD2 . ASP A 1 279 ? 21.536 41.813  2.844   1.00 51.70  ? 412 ASP A OD2 1 
ATOM   1978 N N   . ASP A 1 280 ? 22.705 37.212  5.778   1.00 40.43  ? 413 ASP A N   1 
ATOM   1979 C CA  . ASP A 1 280 ? 23.190 36.489  6.944   1.00 38.73  ? 413 ASP A CA  1 
ATOM   1980 C C   . ASP A 1 280 ? 23.875 35.208  6.467   1.00 38.30  ? 413 ASP A C   1 
ATOM   1981 O O   . ASP A 1 280 ? 23.228 34.310  5.927   1.00 38.15  ? 413 ASP A O   1 
ATOM   1982 C CB  . ASP A 1 280 ? 22.017 36.144  7.861   1.00 39.34  ? 413 ASP A CB  1 
ATOM   1983 C CG  . ASP A 1 280 ? 22.461 35.522  9.161   1.00 39.62  ? 413 ASP A CG  1 
ATOM   1984 O OD1 . ASP A 1 280 ? 23.336 34.634  9.129   1.00 39.66  ? 413 ASP A OD1 1 
ATOM   1985 O OD2 . ASP A 1 280 ? 21.926 35.915  10.219  1.00 42.29  ? 413 ASP A OD2 1 
ATOM   1986 N N   . ILE A 1 281 ? 25.185 35.128  6.672   1.00 37.77  ? 414 ILE A N   1 
ATOM   1987 C CA  . ILE A 1 281 ? 25.960 33.970  6.252   1.00 36.17  ? 414 ILE A CA  1 
ATOM   1988 C C   . ILE A 1 281 ? 25.439 32.637  6.775   1.00 35.18  ? 414 ILE A C   1 
ATOM   1989 O O   . ILE A 1 281 ? 25.410 31.657  6.034   1.00 34.01  ? 414 ILE A O   1 
ATOM   1990 C CB  . ILE A 1 281 ? 27.437 34.124  6.656   1.00 38.71  ? 414 ILE A CB  1 
ATOM   1991 C CG1 . ILE A 1 281 ? 28.052 35.291  5.885   1.00 41.52  ? 414 ILE A CG1 1 
ATOM   1992 C CG2 . ILE A 1 281 ? 28.211 32.836  6.361   1.00 40.65  ? 414 ILE A CG2 1 
ATOM   1993 C CD1 . ILE A 1 281 ? 27.966 35.137  4.372   1.00 44.12  ? 414 ILE A CD1 1 
ATOM   1994 N N   . ASN A 1 282 ? 25.031 32.593  8.041   1.00 33.28  ? 415 ASN A N   1 
ATOM   1995 C CA  . ASN A 1 282 ? 24.518 31.350  8.618   1.00 33.17  ? 415 ASN A CA  1 
ATOM   1996 C C   . ASN A 1 282 ? 23.228 30.901  7.950   1.00 31.41  ? 415 ASN A C   1 
ATOM   1997 O O   . ASN A 1 282 ? 23.009 29.705  7.741   1.00 32.41  ? 415 ASN A O   1 
ATOM   1998 C CB  . ASN A 1 282 ? 24.287 31.505  10.121  1.00 35.08  ? 415 ASN A CB  1 
ATOM   1999 C CG  . ASN A 1 282 ? 25.575 31.456  10.915  1.00 40.74  ? 415 ASN A CG  1 
ATOM   2000 O OD1 . ASN A 1 282 ? 25.585 31.734  12.115  1.00 43.54  ? 415 ASN A OD1 1 
ATOM   2001 N ND2 . ASN A 1 282 ? 26.669 31.090  10.254  1.00 42.61  ? 415 ASN A ND2 1 
ATOM   2002 N N   . VAL A 1 283 ? 22.367 31.859  7.625   1.00 28.84  ? 416 VAL A N   1 
ATOM   2003 C CA  . VAL A 1 283 ? 21.112 31.539  6.967   1.00 27.46  ? 416 VAL A CA  1 
ATOM   2004 C C   . VAL A 1 283 ? 21.403 30.956  5.590   1.00 27.95  ? 416 VAL A C   1 
ATOM   2005 O O   . VAL A 1 283 ? 20.863 29.912  5.224   1.00 27.40  ? 416 VAL A O   1 
ATOM   2006 C CB  . VAL A 1 283 ? 20.225 32.790  6.814   1.00 27.05  ? 416 VAL A CB  1 
ATOM   2007 C CG1 . VAL A 1 283 ? 19.046 32.492  5.895   1.00 23.27  ? 416 VAL A CG1 1 
ATOM   2008 C CG2 . VAL A 1 283 ? 19.723 33.229  8.181   1.00 26.80  ? 416 VAL A CG2 1 
ATOM   2009 N N   . VAL A 1 284 ? 22.260 31.636  4.832   1.00 26.74  ? 417 VAL A N   1 
ATOM   2010 C CA  . VAL A 1 284 ? 22.626 31.183  3.493   1.00 25.84  ? 417 VAL A CA  1 
ATOM   2011 C C   . VAL A 1 284 ? 23.287 29.796  3.528   1.00 25.21  ? 417 VAL A C   1 
ATOM   2012 O O   . VAL A 1 284 ? 22.918 28.914  2.755   1.00 24.85  ? 417 VAL A O   1 
ATOM   2013 C CB  . VAL A 1 284 ? 23.590 32.191  2.793   1.00 26.51  ? 417 VAL A CB  1 
ATOM   2014 C CG1 . VAL A 1 284 ? 23.991 31.669  1.408   1.00 22.86  ? 417 VAL A CG1 1 
ATOM   2015 C CG2 . VAL A 1 284 ? 22.916 33.552  2.659   1.00 22.30  ? 417 VAL A CG2 1 
ATOM   2016 N N   . THR A 1 285 ? 24.249 29.597  4.426   1.00 26.28  ? 418 THR A N   1 
ATOM   2017 C CA  . THR A 1 285 ? 24.929 28.304  4.515   1.00 28.30  ? 418 THR A CA  1 
ATOM   2018 C C   . THR A 1 285 ? 23.959 27.168  4.825   1.00 27.80  ? 418 THR A C   1 
ATOM   2019 O O   . THR A 1 285 ? 24.029 26.103  4.211   1.00 26.67  ? 418 THR A O   1 
ATOM   2020 C CB  . THR A 1 285 ? 26.011 28.294  5.606   1.00 30.02  ? 418 THR A CB  1 
ATOM   2021 O OG1 . THR A 1 285 ? 25.388 28.411  6.888   1.00 40.08  ? 418 THR A OG1 1 
ATOM   2022 C CG2 . THR A 1 285 ? 26.971 29.452  5.418   1.00 29.35  ? 418 THR A CG2 1 
ATOM   2023 N N   . CYS A 1 286 ? 23.062 27.392  5.786   1.00 25.86  ? 419 CYS A N   1 
ATOM   2024 C CA  . CYS A 1 286 ? 22.089 26.374  6.158   1.00 25.06  ? 419 CYS A CA  1 
ATOM   2025 C C   . CYS A 1 286 ? 21.117 26.087  5.028   1.00 23.58  ? 419 CYS A C   1 
ATOM   2026 O O   . CYS A 1 286 ? 20.851 24.924  4.709   1.00 23.79  ? 419 CYS A O   1 
ATOM   2027 C CB  . CYS A 1 286 ? 21.304 26.799  7.403   1.00 25.68  ? 419 CYS A CB  1 
ATOM   2028 S SG  . CYS A 1 286 ? 22.182 26.532  8.950   1.00 28.16  ? 419 CYS A SG  1 
ATOM   2029 N N   . ALA A 1 287 ? 20.576 27.146  4.431   1.00 22.63  ? 420 ALA A N   1 
ATOM   2030 C CA  . ALA A 1 287 ? 19.625 26.987  3.336   1.00 22.18  ? 420 ALA A CA  1 
ATOM   2031 C C   . ALA A 1 287 ? 20.248 26.175  2.208   1.00 21.20  ? 420 ALA A C   1 
ATOM   2032 O O   . ALA A 1 287 ? 19.598 25.301  1.636   1.00 23.14  ? 420 ALA A O   1 
ATOM   2033 C CB  . ALA A 1 287 ? 19.183 28.348  2.815   1.00 21.08  ? 420 ALA A CB  1 
ATOM   2034 N N   . ALA A 1 288 ? 21.503 26.464  1.884   1.00 19.48  ? 421 ALA A N   1 
ATOM   2035 C CA  . ALA A 1 288 ? 22.183 25.731  0.815   1.00 20.87  ? 421 ALA A CA  1 
ATOM   2036 C C   . ALA A 1 288 ? 22.369 24.264  1.203   1.00 19.85  ? 421 ALA A C   1 
ATOM   2037 O O   . ALA A 1 288 ? 22.173 23.367  0.382   1.00 21.07  ? 421 ALA A O   1 
ATOM   2038 C CB  . ALA A 1 288 ? 23.541 26.371  0.512   1.00 20.41  ? 421 ALA A CB  1 
ATOM   2039 N N   . GLY A 1 289 ? 22.747 24.025  2.454   1.00 19.94  ? 422 GLY A N   1 
ATOM   2040 C CA  . GLY A 1 289 ? 22.956 22.660  2.915   1.00 20.65  ? 422 GLY A CA  1 
ATOM   2041 C C   . GLY A 1 289 ? 21.671 21.851  2.910   1.00 22.23  ? 422 GLY A C   1 
ATOM   2042 O O   . GLY A 1 289 ? 21.654 20.692  2.498   1.00 20.92  ? 422 GLY A O   1 
ATOM   2043 N N   . ILE A 1 290 ? 20.586 22.458  3.380   1.00 21.94  ? 423 ILE A N   1 
ATOM   2044 C CA  . ILE A 1 290 ? 19.302 21.774  3.409   1.00 21.31  ? 423 ILE A CA  1 
ATOM   2045 C C   . ILE A 1 290 ? 18.839 21.457  1.983   1.00 22.82  ? 423 ILE A C   1 
ATOM   2046 O O   . ILE A 1 290 ? 18.393 20.344  1.704   1.00 22.72  ? 423 ILE A O   1 
ATOM   2047 C CB  . ILE A 1 290 ? 18.228 22.638  4.108   1.00 21.52  ? 423 ILE A CB  1 
ATOM   2048 C CG1 . ILE A 1 290 ? 18.634 22.901  5.564   1.00 20.76  ? 423 ILE A CG1 1 
ATOM   2049 C CG2 . ILE A 1 290 ? 16.873 21.937  4.035   1.00 18.85  ? 423 ILE A CG2 1 
ATOM   2050 C CD1 . ILE A 1 290 ? 17.806 23.983  6.265   1.00 20.65  ? 423 ILE A CD1 1 
ATOM   2051 N N   . LEU A 1 291 ? 18.943 22.435  1.086   1.00 20.58  ? 424 LEU A N   1 
ATOM   2052 C CA  . LEU A 1 291 ? 18.533 22.240  -0.305  1.00 22.21  ? 424 LEU A CA  1 
ATOM   2053 C C   . LEU A 1 291 ? 19.358 21.159  -1.005  1.00 22.79  ? 424 LEU A C   1 
ATOM   2054 O O   . LEU A 1 291 ? 18.851 20.435  -1.862  1.00 22.22  ? 424 LEU A O   1 
ATOM   2055 C CB  . LEU A 1 291 ? 18.646 23.552  -1.083  1.00 20.90  ? 424 LEU A CB  1 
ATOM   2056 C CG  . LEU A 1 291 ? 17.532 24.580  -0.837  1.00 21.08  ? 424 LEU A CG  1 
ATOM   2057 C CD1 . LEU A 1 291 ? 17.905 25.903  -1.468  1.00 21.94  ? 424 LEU A CD1 1 
ATOM   2058 C CD2 . LEU A 1 291 ? 16.213 24.061  -1.407  1.00 17.73  ? 424 LEU A CD2 1 
ATOM   2059 N N   . SER A 1 292 ? 20.631 21.063  -0.644  1.00 24.15  ? 425 SER A N   1 
ATOM   2060 C CA  . SER A 1 292 ? 21.508 20.059  -1.235  1.00 25.22  ? 425 SER A CA  1 
ATOM   2061 C C   . SER A 1 292 ? 20.961 18.655  -0.936  1.00 23.51  ? 425 SER A C   1 
ATOM   2062 O O   . SER A 1 292 ? 20.846 17.822  -1.833  1.00 25.08  ? 425 SER A O   1 
ATOM   2063 C CB  . SER A 1 292 ? 22.926 20.205  -0.675  1.00 26.71  ? 425 SER A CB  1 
ATOM   2064 O OG  . SER A 1 292 ? 23.824 19.326  -1.332  1.00 32.27  ? 425 SER A OG  1 
ATOM   2065 N N   . ASN A 1 293 ? 20.599 18.402  0.320   1.00 21.55  ? 426 ASN A N   1 
ATOM   2066 C CA  . ASN A 1 293 ? 20.073 17.091  0.685   1.00 21.94  ? 426 ASN A CA  1 
ATOM   2067 C C   . ASN A 1 293 ? 18.661 16.805  0.178   1.00 22.45  ? 426 ASN A C   1 
ATOM   2068 O O   . ASN A 1 293 ? 18.388 15.698  -0.270  1.00 21.45  ? 426 ASN A O   1 
ATOM   2069 C CB  . ASN A 1 293 ? 20.123 16.890  2.201   1.00 18.41  ? 426 ASN A CB  1 
ATOM   2070 C CG  . ASN A 1 293 ? 21.506 16.512  2.688   1.00 21.04  ? 426 ASN A CG  1 
ATOM   2071 O OD1 . ASN A 1 293 ? 22.318 15.993  1.923   1.00 21.81  ? 426 ASN A OD1 1 
ATOM   2072 N ND2 . ASN A 1 293 ? 21.777 16.753  3.966   1.00 19.97  ? 426 ASN A ND2 1 
ATOM   2073 N N   . LEU A 1 294 ? 17.768 17.795  0.240   1.00 23.57  ? 427 LEU A N   1 
ATOM   2074 C CA  . LEU A 1 294 ? 16.391 17.598  -0.212  1.00 23.30  ? 427 LEU A CA  1 
ATOM   2075 C C   . LEU A 1 294 ? 16.273 17.400  -1.730  1.00 24.13  ? 427 LEU A C   1 
ATOM   2076 O O   . LEU A 1 294 ? 15.282 16.852  -2.209  1.00 23.79  ? 427 LEU A O   1 
ATOM   2077 C CB  . LEU A 1 294 ? 15.504 18.769  0.254   1.00 22.13  ? 427 LEU A CB  1 
ATOM   2078 C CG  . LEU A 1 294 ? 15.399 18.956  1.780   1.00 21.24  ? 427 LEU A CG  1 
ATOM   2079 C CD1 . LEU A 1 294 ? 14.442 20.103  2.097   1.00 20.34  ? 427 LEU A CD1 1 
ATOM   2080 C CD2 . LEU A 1 294 ? 14.916 17.658  2.436   1.00 22.03  ? 427 LEU A CD2 1 
ATOM   2081 N N   . THR A 1 295 ? 17.274 17.841  -2.489  1.00 23.70  ? 428 THR A N   1 
ATOM   2082 C CA  . THR A 1 295 ? 17.235 17.652  -3.936  1.00 25.17  ? 428 THR A CA  1 
ATOM   2083 C C   . THR A 1 295 ? 17.874 16.316  -4.324  1.00 26.97  ? 428 THR A C   1 
ATOM   2084 O O   . THR A 1 295 ? 18.020 16.012  -5.505  1.00 28.51  ? 428 THR A O   1 
ATOM   2085 C CB  . THR A 1 295 ? 17.969 18.783  -4.701  1.00 24.57  ? 428 THR A CB  1 
ATOM   2086 O OG1 . THR A 1 295 ? 19.294 18.932  -4.183  1.00 23.95  ? 428 THR A OG1 1 
ATOM   2087 C CG2 . THR A 1 295 ? 17.209 20.104  -4.575  1.00 24.03  ? 428 THR A CG2 1 
ATOM   2088 N N   . CYS A 1 296 ? 18.247 15.519  -3.325  1.00 27.52  ? 429 CYS A N   1 
ATOM   2089 C CA  . CYS A 1 296 ? 18.858 14.214  -3.575  1.00 27.64  ? 429 CYS A CA  1 
ATOM   2090 C C   . CYS A 1 296 ? 17.850 13.141  -4.007  1.00 26.73  ? 429 CYS A C   1 
ATOM   2091 O O   . CYS A 1 296 ? 17.045 12.683  -3.202  1.00 25.33  ? 429 CYS A O   1 
ATOM   2092 C CB  . CYS A 1 296 ? 19.594 13.716  -2.323  1.00 27.55  ? 429 CYS A CB  1 
ATOM   2093 S SG  . CYS A 1 296 ? 21.229 14.432  -2.037  1.00 30.79  ? 429 CYS A SG  1 
ATOM   2094 N N   . ASN A 1 297 ? 17.903 12.756  -5.279  1.00 26.30  ? 430 ASN A N   1 
ATOM   2095 C CA  . ASN A 1 297 ? 17.044 11.706  -5.836  1.00 28.71  ? 430 ASN A CA  1 
ATOM   2096 C C   . ASN A 1 297 ? 15.535 11.903  -5.741  1.00 30.56  ? 430 ASN A C   1 
ATOM   2097 O O   . ASN A 1 297 ? 14.774 10.946  -5.892  1.00 32.21  ? 430 ASN A O   1 
ATOM   2098 C CB  . ASN A 1 297 ? 17.397 10.364  -5.194  1.00 27.17  ? 430 ASN A CB  1 
ATOM   2099 C CG  . ASN A 1 297 ? 18.881 10.100  -5.194  1.00 27.51  ? 430 ASN A CG  1 
ATOM   2100 O OD1 . ASN A 1 297 ? 19.517 10.057  -6.252  1.00 27.48  ? 430 ASN A OD1 1 
ATOM   2101 N ND2 . ASN A 1 297 ? 19.451 9.931   -4.008  1.00 28.55  ? 430 ASN A ND2 1 
ATOM   2102 N N   . ASN A 1 298 ? 15.092 13.125  -5.488  1.00 29.63  ? 431 ASN A N   1 
ATOM   2103 C CA  . ASN A 1 298 ? 13.662 13.380  -5.389  1.00 29.08  ? 431 ASN A CA  1 
ATOM   2104 C C   . ASN A 1 298 ? 13.289 14.276  -6.571  1.00 29.99  ? 431 ASN A C   1 
ATOM   2105 O O   . ASN A 1 298 ? 13.586 15.470  -6.563  1.00 27.67  ? 431 ASN A O   1 
ATOM   2106 C CB  . ASN A 1 298 ? 13.354 14.069  -4.057  1.00 28.37  ? 431 ASN A CB  1 
ATOM   2107 C CG  . ASN A 1 298 ? 11.870 14.169  -3.783  1.00 27.99  ? 431 ASN A CG  1 
ATOM   2108 O OD1 . ASN A 1 298 ? 11.114 14.687  -4.599  1.00 27.57  ? 431 ASN A OD1 1 
ATOM   2109 N ND2 . ASN A 1 298 ? 11.446 13.673  -2.628  1.00 27.64  ? 431 ASN A ND2 1 
ATOM   2110 N N   . TYR A 1 299 ? 12.651 13.704  -7.591  1.00 30.99  ? 432 TYR A N   1 
ATOM   2111 C CA  . TYR A 1 299 ? 12.299 14.490  -8.768  1.00 34.17  ? 432 TYR A CA  1 
ATOM   2112 C C   . TYR A 1 299 ? 11.244 15.560  -8.536  1.00 32.39  ? 432 TYR A C   1 
ATOM   2113 O O   . TYR A 1 299 ? 11.255 16.586  -9.211  1.00 32.33  ? 432 TYR A O   1 
ATOM   2114 C CB  . TYR A 1 299 ? 11.910 13.580  -9.948  1.00 40.00  ? 432 TYR A CB  1 
ATOM   2115 C CG  . TYR A 1 299 ? 10.749 12.646  -9.716  1.00 45.60  ? 432 TYR A CG  1 
ATOM   2116 C CD1 . TYR A 1 299 ? 9.432  13.110  -9.745  1.00 49.26  ? 432 TYR A CD1 1 
ATOM   2117 C CD2 . TYR A 1 299 ? 10.965 11.286  -9.498  1.00 48.53  ? 432 TYR A CD2 1 
ATOM   2118 C CE1 . TYR A 1 299 ? 8.353  12.233  -9.565  1.00 51.69  ? 432 TYR A CE1 1 
ATOM   2119 C CE2 . TYR A 1 299 ? 9.901  10.405  -9.315  1.00 51.82  ? 432 TYR A CE2 1 
ATOM   2120 C CZ  . TYR A 1 299 ? 8.598  10.882  -9.351  1.00 52.79  ? 432 TYR A CZ  1 
ATOM   2121 O OH  . TYR A 1 299 ? 7.549  10.004  -9.177  1.00 55.30  ? 432 TYR A OH  1 
ATOM   2122 N N   . LYS A 1 300 ? 10.348 15.348  -7.579  1.00 30.65  ? 433 LYS A N   1 
ATOM   2123 C CA  . LYS A 1 300 ? 9.334  16.355  -7.295  1.00 31.01  ? 433 LYS A CA  1 
ATOM   2124 C C   . LYS A 1 300 ? 9.992  17.559  -6.626  1.00 28.82  ? 433 LYS A C   1 
ATOM   2125 O O   . LYS A 1 300 ? 9.654  18.705  -6.924  1.00 28.77  ? 433 LYS A O   1 
ATOM   2126 C CB  . LYS A 1 300 ? 8.240  15.780  -6.394  1.00 35.25  ? 433 LYS A CB  1 
ATOM   2127 C CG  . LYS A 1 300 ? 7.478  14.628  -7.034  1.00 41.05  ? 433 LYS A CG  1 
ATOM   2128 C CD  . LYS A 1 300 ? 6.343  14.147  -6.151  1.00 44.82  ? 433 LYS A CD  1 
ATOM   2129 C CE  . LYS A 1 300 ? 5.607  12.984  -6.802  1.00 47.90  ? 433 LYS A CE  1 
ATOM   2130 N NZ  . LYS A 1 300 ? 4.445  12.538  -5.976  1.00 49.20  ? 433 LYS A NZ  1 
ATOM   2131 N N   . ASN A 1 301 ? 10.938 17.296  -5.727  1.00 28.19  ? 434 ASN A N   1 
ATOM   2132 C CA  . ASN A 1 301 ? 11.650 18.369  -5.034  1.00 25.80  ? 434 ASN A CA  1 
ATOM   2133 C C   . ASN A 1 301 ? 12.526 19.120  -6.034  1.00 24.80  ? 434 ASN A C   1 
ATOM   2134 O O   . ASN A 1 301 ? 12.633 20.341  -5.977  1.00 23.52  ? 434 ASN A O   1 
ATOM   2135 C CB  . ASN A 1 301 ? 12.519 17.808  -3.897  1.00 25.44  ? 434 ASN A CB  1 
ATOM   2136 C CG  . ASN A 1 301 ? 11.697 17.322  -2.709  1.00 26.62  ? 434 ASN A CG  1 
ATOM   2137 O OD1 . ASN A 1 301 ? 10.472 17.442  -2.691  1.00 26.45  ? 434 ASN A OD1 1 
ATOM   2138 N ND2 . ASN A 1 301 ? 12.376 16.773  -1.705  1.00 25.58  ? 434 ASN A ND2 1 
ATOM   2139 N N   . LYS A 1 302 ? 13.168 18.389  -6.943  1.00 24.35  ? 435 LYS A N   1 
ATOM   2140 C CA  . LYS A 1 302 ? 14.001 19.032  -7.951  1.00 24.43  ? 435 LYS A CA  1 
ATOM   2141 C C   . LYS A 1 302 ? 13.122 19.929  -8.821  1.00 25.30  ? 435 LYS A C   1 
ATOM   2142 O O   . LYS A 1 302 ? 13.481 21.076  -9.107  1.00 25.49  ? 435 LYS A O   1 
ATOM   2143 C CB  . LYS A 1 302 ? 14.702 17.987  -8.825  1.00 23.72  ? 435 LYS A CB  1 
ATOM   2144 C CG  . LYS A 1 302 ? 15.708 17.133  -8.061  1.00 24.35  ? 435 LYS A CG  1 
ATOM   2145 C CD  . LYS A 1 302 ? 16.491 16.234  -8.999  1.00 23.62  ? 435 LYS A CD  1 
ATOM   2146 C CE  . LYS A 1 302 ? 17.443 15.332  -8.232  1.00 22.60  ? 435 LYS A CE  1 
ATOM   2147 N NZ  . LYS A 1 302 ? 18.240 14.487  -9.152  1.00 23.98  ? 435 LYS A NZ  1 
ATOM   2148 N N   . MET A 1 303 ? 11.969 19.402  -9.226  1.00 25.19  ? 436 MET A N   1 
ATOM   2149 C CA  . MET A 1 303 ? 11.016 20.141  -10.061 1.00 29.27  ? 436 MET A CA  1 
ATOM   2150 C C   . MET A 1 303 ? 10.571 21.446  -9.400  1.00 29.08  ? 436 MET A C   1 
ATOM   2151 O O   . MET A 1 303 ? 10.561 22.507  -10.036 1.00 25.25  ? 436 MET A O   1 
ATOM   2152 C CB  . MET A 1 303 ? 9.770  19.291  -10.333 1.00 32.39  ? 436 MET A CB  1 
ATOM   2153 C CG  . MET A 1 303 ? 9.988  18.060  -11.200 1.00 40.22  ? 436 MET A CG  1 
ATOM   2154 S SD  . MET A 1 303 ? 10.174 18.457  -12.940 1.00 50.48  ? 436 MET A SD  1 
ATOM   2155 C CE  . MET A 1 303 ? 8.433  18.497  -13.451 1.00 46.46  ? 436 MET A CE  1 
ATOM   2156 N N   . MET A 1 304 ? 10.195 21.357  -8.124  1.00 29.14  ? 437 MET A N   1 
ATOM   2157 C CA  . MET A 1 304 ? 9.728  22.520  -7.374  1.00 30.33  ? 437 MET A CA  1 
ATOM   2158 C C   . MET A 1 304 ? 10.819 23.568  -7.180  1.00 29.76  ? 437 MET A C   1 
ATOM   2159 O O   . MET A 1 304 ? 10.562 24.764  -7.317  1.00 28.37  ? 437 MET A O   1 
ATOM   2160 C CB  . MET A 1 304 ? 9.181  22.084  -6.010  1.00 34.76  ? 437 MET A CB  1 
ATOM   2161 C CG  . MET A 1 304 ? 8.074  21.036  -6.107  1.00 44.50  ? 437 MET A CG  1 
ATOM   2162 S SD  . MET A 1 304 ? 7.356  20.521  -4.513  1.00 54.69  ? 437 MET A SD  1 
ATOM   2163 C CE  . MET A 1 304 ? 8.345  19.062  -4.110  1.00 49.68  ? 437 MET A CE  1 
ATOM   2164 N N   . VAL A 1 305 ? 12.033 23.123  -6.863  1.00 26.89  ? 438 VAL A N   1 
ATOM   2165 C CA  . VAL A 1 305 ? 13.138 24.053  -6.656  1.00 26.06  ? 438 VAL A CA  1 
ATOM   2166 C C   . VAL A 1 305 ? 13.425 24.838  -7.934  1.00 27.56  ? 438 VAL A C   1 
ATOM   2167 O O   . VAL A 1 305 ? 13.685 26.042  -7.880  1.00 28.28  ? 438 VAL A O   1 
ATOM   2168 C CB  . VAL A 1 305 ? 14.430 23.317  -6.191  1.00 24.46  ? 438 VAL A CB  1 
ATOM   2169 C CG1 . VAL A 1 305 ? 15.618 24.261  -6.216  1.00 23.48  ? 438 VAL A CG1 1 
ATOM   2170 C CG2 . VAL A 1 305 ? 14.240 22.783  -4.784  1.00 22.82  ? 438 VAL A CG2 1 
ATOM   2171 N N   . CYS A 1 306 ? 13.381 24.162  -9.081  1.00 27.07  ? 439 CYS A N   1 
ATOM   2172 C CA  . CYS A 1 306 ? 13.630 24.830  -10.354 1.00 29.53  ? 439 CYS A CA  1 
ATOM   2173 C C   . CYS A 1 306 ? 12.467 25.759  -10.693 1.00 30.41  ? 439 CYS A C   1 
ATOM   2174 O O   . CYS A 1 306 ? 12.660 26.842  -11.245 1.00 30.89  ? 439 CYS A O   1 
ATOM   2175 C CB  . CYS A 1 306 ? 13.803 23.806  -11.487 1.00 28.74  ? 439 CYS A CB  1 
ATOM   2176 S SG  . CYS A 1 306 ? 15.347 22.854  -11.443 1.00 26.17  ? 439 CYS A SG  1 
ATOM   2177 N N   . GLN A 1 307 ? 11.260 25.326  -10.352 1.00 31.32  ? 440 GLN A N   1 
ATOM   2178 C CA  . GLN A 1 307 ? 10.053 26.099  -10.626 1.00 33.76  ? 440 GLN A CA  1 
ATOM   2179 C C   . GLN A 1 307 ? 10.055 27.479  -9.964  1.00 33.61  ? 440 GLN A C   1 
ATOM   2180 O O   . GLN A 1 307 ? 9.557  28.444  -10.544 1.00 33.37  ? 440 GLN A O   1 
ATOM   2181 C CB  . GLN A 1 307 ? 8.826  25.308  -10.169 1.00 36.17  ? 440 GLN A CB  1 
ATOM   2182 C CG  . GLN A 1 307 ? 7.503  26.032  -10.323 1.00 43.05  ? 440 GLN A CG  1 
ATOM   2183 C CD  . GLN A 1 307 ? 6.339  25.209  -9.796  1.00 47.15  ? 440 GLN A CD  1 
ATOM   2184 O OE1 . GLN A 1 307 ? 6.117  24.077  -10.234 1.00 49.01  ? 440 GLN A OE1 1 
ATOM   2185 N NE2 . GLN A 1 307 ? 5.591  25.773  -8.852  1.00 46.14  ? 440 GLN A NE2 1 
ATOM   2186 N N   . VAL A 1 308 ? 10.615 27.574  -8.758  1.00 31.43  ? 441 VAL A N   1 
ATOM   2187 C CA  . VAL A 1 308 ? 10.649 28.848  -8.046  1.00 30.73  ? 441 VAL A CA  1 
ATOM   2188 C C   . VAL A 1 308 ? 11.942 29.639  -8.230  1.00 30.51  ? 441 VAL A C   1 
ATOM   2189 O O   . VAL A 1 308 ? 12.270 30.493  -7.408  1.00 31.65  ? 441 VAL A O   1 
ATOM   2190 C CB  . VAL A 1 308 ? 10.402 28.655  -6.526  1.00 30.70  ? 441 VAL A CB  1 
ATOM   2191 C CG1 . VAL A 1 308 ? 9.028  28.041  -6.297  1.00 29.10  ? 441 VAL A CG1 1 
ATOM   2192 C CG2 . VAL A 1 308 ? 11.492 27.779  -5.923  1.00 29.25  ? 441 VAL A CG2 1 
ATOM   2193 N N   . GLY A 1 309 ? 12.678 29.359  -9.303  1.00 29.70  ? 442 GLY A N   1 
ATOM   2194 C CA  . GLY A 1 309 ? 13.910 30.092  -9.554  1.00 27.36  ? 442 GLY A CA  1 
ATOM   2195 C C   . GLY A 1 309 ? 15.125 29.652  -8.753  1.00 25.17  ? 442 GLY A C   1 
ATOM   2196 O O   . GLY A 1 309 ? 16.051 30.434  -8.537  1.00 25.27  ? 442 GLY A O   1 
ATOM   2197 N N   . GLY A 1 310 ? 15.137 28.396  -8.322  1.00 24.91  ? 443 GLY A N   1 
ATOM   2198 C CA  . GLY A 1 310 ? 16.260 27.896  -7.550  1.00 23.11  ? 443 GLY A CA  1 
ATOM   2199 C C   . GLY A 1 310 ? 17.604 27.932  -8.259  1.00 22.19  ? 443 GLY A C   1 
ATOM   2200 O O   . GLY A 1 310 ? 18.634 28.174  -7.627  1.00 22.37  ? 443 GLY A O   1 
ATOM   2201 N N   . ILE A 1 311 ? 17.619 27.689  -9.566  1.00 22.91  ? 444 ILE A N   1 
ATOM   2202 C CA  . ILE A 1 311 ? 18.889 27.701  -10.294 1.00 22.67  ? 444 ILE A CA  1 
ATOM   2203 C C   . ILE A 1 311 ? 19.541 29.084  -10.226 1.00 23.42  ? 444 ILE A C   1 
ATOM   2204 O O   . ILE A 1 311 ? 20.720 29.209  -9.881  1.00 25.06  ? 444 ILE A O   1 
ATOM   2205 C CB  . ILE A 1 311 ? 18.700 27.305  -11.774 1.00 22.46  ? 444 ILE A CB  1 
ATOM   2206 C CG1 . ILE A 1 311 ? 18.138 25.879  -11.874 1.00 21.87  ? 444 ILE A CG1 1 
ATOM   2207 C CG2 . ILE A 1 311 ? 20.035 27.416  -12.515 1.00 21.46  ? 444 ILE A CG2 1 
ATOM   2208 C CD1 . ILE A 1 311 ? 19.081 24.789  -11.377 1.00 22.20  ? 444 ILE A CD1 1 
ATOM   2209 N N   . GLU A 1 312 ? 18.774 30.126  -10.537 1.00 24.30  ? 445 GLU A N   1 
ATOM   2210 C CA  . GLU A 1 312 ? 19.311 31.484  -10.498 1.00 24.11  ? 445 GLU A CA  1 
ATOM   2211 C C   . GLU A 1 312 ? 19.810 31.836  -9.099  1.00 24.09  ? 445 GLU A C   1 
ATOM   2212 O O   . GLU A 1 312 ? 20.902 32.387  -8.939  1.00 24.64  ? 445 GLU A O   1 
ATOM   2213 C CB  . GLU A 1 312 ? 18.246 32.498  -10.923 1.00 26.98  ? 445 GLU A CB  1 
ATOM   2214 C CG  . GLU A 1 312 ? 18.806 33.900  -11.132 1.00 33.27  ? 445 GLU A CG  1 
ATOM   2215 C CD  . GLU A 1 312 ? 17.730 34.945  -11.368 1.00 36.65  ? 445 GLU A CD  1 
ATOM   2216 O OE1 . GLU A 1 312 ? 16.657 34.598  -11.906 1.00 37.28  ? 445 GLU A OE1 1 
ATOM   2217 O OE2 . GLU A 1 312 ? 17.965 36.122  -11.026 1.00 40.77  ? 445 GLU A OE2 1 
ATOM   2218 N N   . ALA A 1 313 ? 19.010 31.515  -8.085  1.00 22.81  ? 446 ALA A N   1 
ATOM   2219 C CA  . ALA A 1 313 ? 19.375 31.808  -6.705  1.00 22.58  ? 446 ALA A CA  1 
ATOM   2220 C C   . ALA A 1 313 ? 20.646 31.077  -6.280  1.00 22.89  ? 446 ALA A C   1 
ATOM   2221 O O   . ALA A 1 313 ? 21.504 31.647  -5.607  1.00 24.96  ? 446 ALA A O   1 
ATOM   2222 C CB  . ALA A 1 313 ? 18.223 31.442  -5.768  1.00 24.43  ? 446 ALA A CB  1 
ATOM   2223 N N   . LEU A 1 314 ? 20.772 29.814  -6.667  1.00 21.45  ? 447 LEU A N   1 
ATOM   2224 C CA  . LEU A 1 314 ? 21.957 29.052  -6.298  1.00 22.08  ? 447 LEU A CA  1 
ATOM   2225 C C   . LEU A 1 314 ? 23.189 29.597  -7.012  1.00 20.96  ? 447 LEU A C   1 
ATOM   2226 O O   . LEU A 1 314 ? 24.262 29.674  -6.426  1.00 23.06  ? 447 LEU A O   1 
ATOM   2227 C CB  . LEU A 1 314 ? 21.759 27.565  -6.615  1.00 19.69  ? 447 LEU A CB  1 
ATOM   2228 C CG  . LEU A 1 314 ? 20.867 26.809  -5.629  1.00 19.39  ? 447 LEU A CG  1 
ATOM   2229 C CD1 . LEU A 1 314 ? 20.522 25.441  -6.186  1.00 20.14  ? 447 LEU A CD1 1 
ATOM   2230 C CD2 . LEU A 1 314 ? 21.581 26.679  -4.282  1.00 19.30  ? 447 LEU A CD2 1 
ATOM   2231 N N   . VAL A 1 315 ? 23.037 29.977  -8.276  1.00 23.81  ? 448 VAL A N   1 
ATOM   2232 C CA  . VAL A 1 315 ? 24.165 30.531  -9.022  1.00 25.20  ? 448 VAL A CA  1 
ATOM   2233 C C   . VAL A 1 315 ? 24.634 31.825  -8.351  1.00 26.10  ? 448 VAL A C   1 
ATOM   2234 O O   . VAL A 1 315 ? 25.837 32.045  -8.187  1.00 26.52  ? 448 VAL A O   1 
ATOM   2235 C CB  . VAL A 1 315 ? 23.785 30.809  -10.494 1.00 25.71  ? 448 VAL A CB  1 
ATOM   2236 C CG1 . VAL A 1 315 ? 24.893 31.595  -11.185 1.00 27.52  ? 448 VAL A CG1 1 
ATOM   2237 C CG2 . VAL A 1 315 ? 23.551 29.485  -11.222 1.00 26.16  ? 448 VAL A CG2 1 
ATOM   2238 N N   . ARG A 1 316 ? 23.685 32.674  -7.956  1.00 28.12  ? 449 ARG A N   1 
ATOM   2239 C CA  . ARG A 1 316 ? 24.017 33.927  -7.274  1.00 30.24  ? 449 ARG A CA  1 
ATOM   2240 C C   . ARG A 1 316 ? 24.744 33.633  -5.964  1.00 27.84  ? 449 ARG A C   1 
ATOM   2241 O O   . ARG A 1 316 ? 25.748 34.269  -5.636  1.00 28.90  ? 449 ARG A O   1 
ATOM   2242 C CB  . ARG A 1 316 ? 22.747 34.735  -6.987  1.00 34.16  ? 449 ARG A CB  1 
ATOM   2243 C CG  . ARG A 1 316 ? 22.181 35.423  -8.213  1.00 41.35  ? 449 ARG A CG  1 
ATOM   2244 C CD  . ARG A 1 316 ? 20.841 36.090  -7.939  1.00 48.04  ? 449 ARG A CD  1 
ATOM   2245 N NE  . ARG A 1 316 ? 20.453 36.952  -9.051  1.00 54.35  ? 449 ARG A NE  1 
ATOM   2246 C CZ  . ARG A 1 316 ? 19.296 37.601  -9.134  1.00 57.91  ? 449 ARG A CZ  1 
ATOM   2247 N NH1 . ARG A 1 316 ? 18.393 37.486  -8.168  1.00 59.12  ? 449 ARG A NH1 1 
ATOM   2248 N NH2 . ARG A 1 316 ? 19.048 38.379  -10.181 1.00 59.97  ? 449 ARG A NH2 1 
ATOM   2249 N N   . THR A 1 317 ? 24.234 32.661  -5.214  1.00 27.10  ? 450 THR A N   1 
ATOM   2250 C CA  . THR A 1 317 ? 24.846 32.279  -3.948  1.00 26.77  ? 450 THR A CA  1 
ATOM   2251 C C   . THR A 1 317 ? 26.303 31.884  -4.164  1.00 26.83  ? 450 THR A C   1 
ATOM   2252 O O   . THR A 1 317 ? 27.179 32.256  -3.384  1.00 28.68  ? 450 THR A O   1 
ATOM   2253 C CB  . THR A 1 317 ? 24.086 31.101  -3.305  1.00 28.21  ? 450 THR A CB  1 
ATOM   2254 O OG1 . THR A 1 317 ? 22.790 31.546  -2.896  1.00 27.14  ? 450 THR A OG1 1 
ATOM   2255 C CG2 . THR A 1 317 ? 24.836 30.559  -2.101  1.00 26.98  ? 450 THR A CG2 1 
ATOM   2256 N N   . VAL A 1 318 ? 26.565 31.135  -5.229  1.00 26.60  ? 451 VAL A N   1 
ATOM   2257 C CA  . VAL A 1 318 ? 27.930 30.709  -5.524  1.00 27.70  ? 451 VAL A CA  1 
ATOM   2258 C C   . VAL A 1 318 ? 28.792 31.920  -5.874  1.00 28.01  ? 451 VAL A C   1 
ATOM   2259 O O   . VAL A 1 318 ? 29.926 32.040  -5.409  1.00 25.02  ? 451 VAL A O   1 
ATOM   2260 C CB  . VAL A 1 318 ? 27.964 29.697  -6.691  1.00 27.28  ? 451 VAL A CB  1 
ATOM   2261 C CG1 . VAL A 1 318 ? 29.401 29.425  -7.105  1.00 27.99  ? 451 VAL A CG1 1 
ATOM   2262 C CG2 . VAL A 1 318 ? 27.289 28.394  -6.265  1.00 28.00  ? 451 VAL A CG2 1 
ATOM   2263 N N   . LEU A 1 319 ? 28.241 32.814  -6.687  1.00 30.26  ? 452 LEU A N   1 
ATOM   2264 C CA  . LEU A 1 319 ? 28.944 34.028  -7.089  1.00 33.77  ? 452 LEU A CA  1 
ATOM   2265 C C   . LEU A 1 319 ? 29.390 34.830  -5.870  1.00 34.20  ? 452 LEU A C   1 
ATOM   2266 O O   . LEU A 1 319 ? 30.564 35.168  -5.733  1.00 35.11  ? 452 LEU A O   1 
ATOM   2267 C CB  . LEU A 1 319 ? 28.035 34.900  -7.960  1.00 34.66  ? 452 LEU A CB  1 
ATOM   2268 C CG  . LEU A 1 319 ? 27.869 34.506  -9.427  1.00 37.58  ? 452 LEU A CG  1 
ATOM   2269 C CD1 . LEU A 1 319 ? 26.627 35.154  -10.016 1.00 38.78  ? 452 LEU A CD1 1 
ATOM   2270 C CD2 . LEU A 1 319 ? 29.107 34.932  -10.193 1.00 40.67  ? 452 LEU A CD2 1 
ATOM   2271 N N   . ARG A 1 320 ? 28.445 35.120  -4.982  1.00 35.73  ? 453 ARG A N   1 
ATOM   2272 C CA  . ARG A 1 320 ? 28.725 35.898  -3.778  1.00 36.89  ? 453 ARG A CA  1 
ATOM   2273 C C   . ARG A 1 320 ? 29.636 35.217  -2.760  1.00 36.13  ? 453 ARG A C   1 
ATOM   2274 O O   . ARG A 1 320 ? 30.412 35.883  -2.081  1.00 35.84  ? 453 ARG A O   1 
ATOM   2275 C CB  . ARG A 1 320 ? 27.415 36.286  -3.092  1.00 40.26  ? 453 ARG A CB  1 
ATOM   2276 C CG  . ARG A 1 320 ? 26.512 37.174  -3.930  1.00 47.07  ? 453 ARG A CG  1 
ATOM   2277 C CD  . ARG A 1 320 ? 25.299 37.611  -3.125  1.00 53.18  ? 453 ARG A CD  1 
ATOM   2278 N NE  . ARG A 1 320 ? 24.456 38.545  -3.866  1.00 59.13  ? 453 ARG A NE  1 
ATOM   2279 C CZ  . ARG A 1 320 ? 23.396 39.166  -3.353  1.00 62.27  ? 453 ARG A CZ  1 
ATOM   2280 N NH1 . ARG A 1 320 ? 23.043 38.955  -2.090  1.00 63.67  ? 453 ARG A NH1 1 
ATOM   2281 N NH2 . ARG A 1 320 ? 22.689 40.005  -4.103  1.00 63.69  ? 453 ARG A NH2 1 
ATOM   2282 N N   . ALA A 1 321 ? 29.540 33.896  -2.647  1.00 34.52  ? 454 ALA A N   1 
ATOM   2283 C CA  . ALA A 1 321 ? 30.355 33.160  -1.686  1.00 34.33  ? 454 ALA A CA  1 
ATOM   2284 C C   . ALA A 1 321 ? 31.859 33.250  -1.945  1.00 33.97  ? 454 ALA A C   1 
ATOM   2285 O O   . ALA A 1 321 ? 32.658 33.153  -1.014  1.00 34.04  ? 454 ALA A O   1 
ATOM   2286 C CB  . ALA A 1 321 ? 29.926 31.698  -1.655  1.00 33.65  ? 454 ALA A CB  1 
ATOM   2287 N N   . GLY A 1 322 ? 32.252 33.428  -3.201  1.00 33.70  ? 455 GLY A N   1 
ATOM   2288 C CA  . GLY A 1 322 ? 33.672 33.502  -3.500  1.00 32.57  ? 455 GLY A CA  1 
ATOM   2289 C C   . GLY A 1 322 ? 34.377 32.210  -3.119  1.00 33.63  ? 455 GLY A C   1 
ATOM   2290 O O   . GLY A 1 322 ? 34.038 31.139  -3.632  1.00 33.51  ? 455 GLY A O   1 
ATOM   2291 N N   . ASP A 1 323 ? 35.347 32.292  -2.213  1.00 33.28  ? 456 ASP A N   1 
ATOM   2292 C CA  . ASP A 1 323 ? 36.084 31.099  -1.795  1.00 34.59  ? 456 ASP A CA  1 
ATOM   2293 C C   . ASP A 1 323 ? 35.566 30.419  -0.528  1.00 33.31  ? 456 ASP A C   1 
ATOM   2294 O O   . ASP A 1 323 ? 36.233 29.532  0.008   1.00 32.83  ? 456 ASP A O   1 
ATOM   2295 C CB  . ASP A 1 323 ? 37.570 31.423  -1.607  1.00 37.74  ? 456 ASP A CB  1 
ATOM   2296 C CG  . ASP A 1 323 ? 37.811 32.477  -0.542  1.00 42.92  ? 456 ASP A CG  1 
ATOM   2297 O OD1 . ASP A 1 323 ? 37.183 32.398  0.537   1.00 43.14  ? 456 ASP A OD1 1 
ATOM   2298 O OD2 . ASP A 1 323 ? 38.640 33.381  -0.782  1.00 46.66  ? 456 ASP A OD2 1 
ATOM   2299 N N   . ARG A 1 324 ? 34.396 30.831  -0.045  1.00 32.76  ? 457 ARG A N   1 
ATOM   2300 C CA  . ARG A 1 324 ? 33.812 30.227  1.158   1.00 34.59  ? 457 ARG A CA  1 
ATOM   2301 C C   . ARG A 1 324 ? 33.166 28.888  0.797   1.00 33.48  ? 457 ARG A C   1 
ATOM   2302 O O   . ARG A 1 324 ? 32.007 28.827  0.380   1.00 31.65  ? 457 ARG A O   1 
ATOM   2303 C CB  . ARG A 1 324 ? 32.786 31.180  1.783   1.00 35.44  ? 457 ARG A CB  1 
ATOM   2304 C CG  . ARG A 1 324 ? 33.435 32.324  2.555   1.00 41.80  ? 457 ARG A CG  1 
ATOM   2305 C CD  . ARG A 1 324 ? 32.433 33.388  2.977   1.00 45.92  ? 457 ARG A CD  1 
ATOM   2306 N NE  . ARG A 1 324 ? 31.959 34.163  1.834   1.00 52.48  ? 457 ARG A NE  1 
ATOM   2307 C CZ  . ARG A 1 324 ? 31.252 35.284  1.930   1.00 55.06  ? 457 ARG A CZ  1 
ATOM   2308 N NH1 . ARG A 1 324 ? 30.932 35.769  3.123   1.00 56.30  ? 457 ARG A NH1 1 
ATOM   2309 N NH2 . ARG A 1 324 ? 30.870 35.926  0.832   1.00 54.71  ? 457 ARG A NH2 1 
ATOM   2310 N N   . GLU A 1 325 ? 33.935 27.817  0.972   1.00 32.80  ? 458 GLU A N   1 
ATOM   2311 C CA  . GLU A 1 325 ? 33.494 26.471  0.627   1.00 33.61  ? 458 GLU A CA  1 
ATOM   2312 C C   . GLU A 1 325 ? 32.367 25.890  1.472   1.00 34.42  ? 458 GLU A C   1 
ATOM   2313 O O   . GLU A 1 325 ? 31.698 24.943  1.049   1.00 33.98  ? 458 GLU A O   1 
ATOM   2314 C CB  . GLU A 1 325 ? 34.710 25.534  0.612   1.00 32.74  ? 458 GLU A CB  1 
ATOM   2315 C CG  . GLU A 1 325 ? 35.740 25.956  -0.440  1.00 32.53  ? 458 GLU A CG  1 
ATOM   2316 C CD  . GLU A 1 325 ? 36.919 25.010  -0.543  1.00 34.96  ? 458 GLU A CD  1 
ATOM   2317 O OE1 . GLU A 1 325 ? 36.700 23.783  -0.593  1.00 33.80  ? 458 GLU A OE1 1 
ATOM   2318 O OE2 . GLU A 1 325 ? 38.068 25.496  -0.584  1.00 36.04  ? 458 GLU A OE2 1 
ATOM   2319 N N   . ASP A 1 326 ? 32.148 26.450  2.657   1.00 33.21  ? 459 ASP A N   1 
ATOM   2320 C CA  . ASP A 1 326 ? 31.067 25.972  3.510   1.00 34.05  ? 459 ASP A CA  1 
ATOM   2321 C C   . ASP A 1 326 ? 29.748 26.354  2.837   1.00 31.75  ? 459 ASP A C   1 
ATOM   2322 O O   . ASP A 1 326 ? 28.686 25.826  3.175   1.00 31.33  ? 459 ASP A O   1 
ATOM   2323 C CB  . ASP A 1 326 ? 31.170 26.588  4.915   1.00 38.88  ? 459 ASP A CB  1 
ATOM   2324 C CG  . ASP A 1 326 ? 31.185 28.108  4.894   1.00 44.27  ? 459 ASP A CG  1 
ATOM   2325 O OD1 . ASP A 1 326 ? 31.958 28.692  4.098   1.00 46.65  ? 459 ASP A OD1 1 
ATOM   2326 O OD2 . ASP A 1 326 ? 30.434 28.723  5.685   1.00 49.40  ? 459 ASP A OD2 1 
ATOM   2327 N N   . ILE A 1 327 ? 29.830 27.264  1.869   1.00 29.48  ? 460 ILE A N   1 
ATOM   2328 C CA  . ILE A 1 327 ? 28.654 27.700  1.124   1.00 28.24  ? 460 ILE A CA  1 
ATOM   2329 C C   . ILE A 1 327 ? 28.650 27.147  -0.302  1.00 26.39  ? 460 ILE A C   1 
ATOM   2330 O O   . ILE A 1 327 ? 27.656 26.573  -0.744  1.00 25.33  ? 460 ILE A O   1 
ATOM   2331 C CB  . ILE A 1 327 ? 28.565 29.242  1.027   1.00 30.62  ? 460 ILE A CB  1 
ATOM   2332 C CG1 . ILE A 1 327 ? 28.280 29.841  2.407   1.00 32.32  ? 460 ILE A CG1 1 
ATOM   2333 C CG2 . ILE A 1 327 ? 27.471 29.635  0.038   1.00 25.42  ? 460 ILE A CG2 1 
ATOM   2334 C CD1 . ILE A 1 327 ? 28.176 31.359  2.409   1.00 35.91  ? 460 ILE A CD1 1 
ATOM   2335 N N   . THR A 1 328 ? 29.758 27.323  -1.018  1.00 25.49  ? 461 THR A N   1 
ATOM   2336 C CA  . THR A 1 328 ? 29.853 26.857  -2.400  1.00 25.41  ? 461 THR A CA  1 
ATOM   2337 C C   . THR A 1 328 ? 29.717 25.343  -2.569  1.00 24.77  ? 461 THR A C   1 
ATOM   2338 O O   . THR A 1 328 ? 29.120 24.875  -3.541  1.00 24.18  ? 461 THR A O   1 
ATOM   2339 C CB  . THR A 1 328 ? 31.187 27.297  -3.062  1.00 25.57  ? 461 THR A CB  1 
ATOM   2340 O OG1 . THR A 1 328 ? 32.294 26.776  -2.318  1.00 25.23  ? 461 THR A OG1 1 
ATOM   2341 C CG2 . THR A 1 328 ? 31.281 28.819  -3.120  1.00 24.58  ? 461 THR A CG2 1 
ATOM   2342 N N   . GLU A 1 329 ? 30.259 24.572  -1.634  1.00 24.18  ? 462 GLU A N   1 
ATOM   2343 C CA  . GLU A 1 329 ? 30.178 23.125  -1.753  1.00 26.20  ? 462 GLU A CA  1 
ATOM   2344 C C   . GLU A 1 329 ? 28.738 22.616  -1.778  1.00 25.90  ? 462 GLU A C   1 
ATOM   2345 O O   . GLU A 1 329 ? 28.351 21.897  -2.698  1.00 24.67  ? 462 GLU A O   1 
ATOM   2346 C CB  . GLU A 1 329 ? 30.942 22.429  -0.627  1.00 27.43  ? 462 GLU A CB  1 
ATOM   2347 C CG  . GLU A 1 329 ? 31.174 20.953  -0.926  1.00 30.90  ? 462 GLU A CG  1 
ATOM   2348 C CD  . GLU A 1 329 ? 31.849 20.223  0.210   1.00 34.60  ? 462 GLU A CD  1 
ATOM   2349 O OE1 . GLU A 1 329 ? 32.771 20.807  0.820   1.00 37.01  ? 462 GLU A OE1 1 
ATOM   2350 O OE2 . GLU A 1 329 ? 31.467 19.065  0.485   1.00 36.07  ? 462 GLU A OE2 1 
ATOM   2351 N N   . PRO A 1 330 ? 27.927 22.968  -0.763  1.00 25.19  ? 463 PRO A N   1 
ATOM   2352 C CA  . PRO A 1 330 ? 26.551 22.471  -0.811  1.00 23.47  ? 463 PRO A CA  1 
ATOM   2353 C C   . PRO A 1 330 ? 25.757 23.102  -1.952  1.00 22.90  ? 463 PRO A C   1 
ATOM   2354 O O   . PRO A 1 330 ? 24.894 22.451  -2.540  1.00 23.65  ? 463 PRO A O   1 
ATOM   2355 C CB  . PRO A 1 330 ? 26.004 22.819  0.576   1.00 23.55  ? 463 PRO A CB  1 
ATOM   2356 C CG  . PRO A 1 330 ? 26.789 24.048  0.946   1.00 25.63  ? 463 PRO A CG  1 
ATOM   2357 C CD  . PRO A 1 330 ? 28.183 23.693  0.495   1.00 25.41  ? 463 PRO A CD  1 
ATOM   2358 N N   . ALA A 1 331 ? 26.052 24.361  -2.280  1.00 21.90  ? 464 ALA A N   1 
ATOM   2359 C CA  . ALA A 1 331 ? 25.346 25.031  -3.375  1.00 19.54  ? 464 ALA A CA  1 
ATOM   2360 C C   . ALA A 1 331 ? 25.666 24.337  -4.704  1.00 20.53  ? 464 ALA A C   1 
ATOM   2361 O O   . ALA A 1 331 ? 24.779 24.138  -5.535  1.00 22.01  ? 464 ALA A O   1 
ATOM   2362 C CB  . ALA A 1 331 ? 25.735 26.508  -3.443  1.00 19.51  ? 464 ALA A CB  1 
ATOM   2363 N N   . ILE A 1 332 ? 26.931 23.969  -4.897  1.00 20.34  ? 465 ILE A N   1 
ATOM   2364 C CA  . ILE A 1 332 ? 27.358 23.273  -6.115  1.00 20.41  ? 465 ILE A CA  1 
ATOM   2365 C C   . ILE A 1 332 ? 26.719 21.868  -6.158  1.00 19.82  ? 465 ILE A C   1 
ATOM   2366 O O   . ILE A 1 332 ? 26.254 21.432  -7.212  1.00 19.19  ? 465 ILE A O   1 
ATOM   2367 C CB  . ILE A 1 332 ? 28.919 23.183  -6.182  1.00 21.28  ? 465 ILE A CB  1 
ATOM   2368 C CG1 . ILE A 1 332 ? 29.511 24.579  -6.444  1.00 19.54  ? 465 ILE A CG1 1 
ATOM   2369 C CG2 . ILE A 1 332 ? 29.367 22.207  -7.271  1.00 17.63  ? 465 ILE A CG2 1 
ATOM   2370 C CD1 . ILE A 1 332 ? 29.132 25.183  -7.796  1.00 18.42  ? 465 ILE A CD1 1 
ATOM   2371 N N   . CYS A 1 333 ? 26.680 21.169  -5.023  1.00 20.51  ? 466 CYS A N   1 
ATOM   2372 C CA  . CYS A 1 333 ? 26.053 19.838  -4.979  1.00 21.61  ? 466 CYS A CA  1 
ATOM   2373 C C   . CYS A 1 333 ? 24.559 19.959  -5.323  1.00 21.37  ? 466 CYS A C   1 
ATOM   2374 O O   . CYS A 1 333 ? 24.001 19.129  -6.039  1.00 20.55  ? 466 CYS A O   1 
ATOM   2375 C CB  . CYS A 1 333 ? 26.195 19.199  -3.588  1.00 24.54  ? 466 CYS A CB  1 
ATOM   2376 S SG  . CYS A 1 333 ? 27.872 18.684  -3.081  1.00 27.57  ? 466 CYS A SG  1 
ATOM   2377 N N   . ALA A 1 334 ? 23.906 20.996  -4.803  1.00 21.73  ? 467 ALA A N   1 
ATOM   2378 C CA  . ALA A 1 334 ? 22.491 21.193  -5.088  1.00 20.74  ? 467 ALA A CA  1 
ATOM   2379 C C   . ALA A 1 334 ? 22.315 21.374  -6.593  1.00 19.52  ? 467 ALA A C   1 
ATOM   2380 O O   . ALA A 1 334 ? 21.435 20.755  -7.199  1.00 19.01  ? 467 ALA A O   1 
ATOM   2381 C CB  . ALA A 1 334 ? 21.956 22.413  -4.335  1.00 21.52  ? 467 ALA A CB  1 
ATOM   2382 N N   . LEU A 1 335 ? 23.155 22.217  -7.191  1.00 17.52  ? 468 LEU A N   1 
ATOM   2383 C CA  . LEU A 1 335 ? 23.099 22.455  -8.631  1.00 18.50  ? 468 LEU A CA  1 
ATOM   2384 C C   . LEU A 1 335 ? 23.336 21.158  -9.401  1.00 20.13  ? 468 LEU A C   1 
ATOM   2385 O O   . LEU A 1 335 ? 22.680 20.898  -10.413 1.00 20.21  ? 468 LEU A O   1 
ATOM   2386 C CB  . LEU A 1 335 ? 24.139 23.505  -9.046  1.00 19.30  ? 468 LEU A CB  1 
ATOM   2387 C CG  . LEU A 1 335 ? 23.774 24.953  -8.699  1.00 21.94  ? 468 LEU A CG  1 
ATOM   2388 C CD1 . LEU A 1 335 ? 24.961 25.882  -8.949  1.00 22.12  ? 468 LEU A CD1 1 
ATOM   2389 C CD2 . LEU A 1 335 ? 22.570 25.372  -9.546  1.00 19.61  ? 468 LEU A CD2 1 
ATOM   2390 N N   . ARG A 1 336 ? 24.272 20.342  -8.928  1.00 19.41  ? 469 ARG A N   1 
ATOM   2391 C CA  . ARG A 1 336 ? 24.532 19.075  -9.598  1.00 21.62  ? 469 ARG A CA  1 
ATOM   2392 C C   . ARG A 1 336 ? 23.282 18.201  -9.552  1.00 20.37  ? 469 ARG A C   1 
ATOM   2393 O O   . ARG A 1 336 ? 22.914 17.581  -10.546 1.00 21.00  ? 469 ARG A O   1 
ATOM   2394 C CB  . ARG A 1 336 ? 25.702 18.318  -8.950  1.00 25.12  ? 469 ARG A CB  1 
ATOM   2395 C CG  . ARG A 1 336 ? 25.660 16.831  -9.302  1.00 31.08  ? 469 ARG A CG  1 
ATOM   2396 C CD  . ARG A 1 336 ? 27.002 16.217  -9.635  1.00 32.97  ? 469 ARG A CD  1 
ATOM   2397 N NE  . ARG A 1 336 ? 27.766 15.827  -8.459  1.00 36.48  ? 469 ARG A NE  1 
ATOM   2398 C CZ  . ARG A 1 336 ? 28.473 14.700  -8.367  1.00 37.75  ? 469 ARG A CZ  1 
ATOM   2399 N NH1 . ARG A 1 336 ? 28.506 13.841  -9.379  1.00 37.42  ? 469 ARG A NH1 1 
ATOM   2400 N NH2 . ARG A 1 336 ? 29.167 14.439  -7.268  1.00 36.36  ? 469 ARG A NH2 1 
ATOM   2401 N N   . HIS A 1 337 ? 22.623 18.151  -8.400  1.00 20.41  ? 470 HIS A N   1 
ATOM   2402 C CA  . HIS A 1 337 ? 21.412 17.339  -8.271  1.00 22.14  ? 470 HIS A CA  1 
ATOM   2403 C C   . HIS A 1 337 ? 20.306 17.840  -9.204  1.00 22.20  ? 470 HIS A C   1 
ATOM   2404 O O   . HIS A 1 337 ? 19.575 17.046  -9.805  1.00 21.89  ? 470 HIS A O   1 
ATOM   2405 C CB  . HIS A 1 337 ? 20.893 17.377  -6.825  1.00 20.96  ? 470 HIS A CB  1 
ATOM   2406 C CG  . HIS A 1 337 ? 21.883 16.894  -5.814  1.00 22.64  ? 470 HIS A CG  1 
ATOM   2407 N ND1 . HIS A 1 337 ? 21.773 17.183  -4.470  1.00 20.59  ? 470 HIS A ND1 1 
ATOM   2408 C CD2 . HIS A 1 337 ? 23.013 16.158  -5.950  1.00 21.73  ? 470 HIS A CD2 1 
ATOM   2409 C CE1 . HIS A 1 337 ? 22.796 16.652  -3.823  1.00 22.02  ? 470 HIS A CE1 1 
ATOM   2410 N NE2 . HIS A 1 337 ? 23.563 16.026  -4.698  1.00 23.26  ? 470 HIS A NE2 1 
ATOM   2411 N N   . LEU A 1 338 ? 20.204 19.164  -9.315  1.00 22.19  ? 471 LEU A N   1 
ATOM   2412 C CA  . LEU A 1 338 ? 19.178 19.830  -10.123 1.00 21.73  ? 471 LEU A CA  1 
ATOM   2413 C C   . LEU A 1 338 ? 19.384 19.811  -11.635 1.00 22.48  ? 471 LEU A C   1 
ATOM   2414 O O   . LEU A 1 338 ? 18.464 20.123  -12.392 1.00 23.30  ? 471 LEU A O   1 
ATOM   2415 C CB  . LEU A 1 338 ? 19.027 21.284  -9.652  1.00 20.25  ? 471 LEU A CB  1 
ATOM   2416 C CG  . LEU A 1 338 ? 18.465 21.517  -8.242  1.00 20.37  ? 471 LEU A CG  1 
ATOM   2417 C CD1 . LEU A 1 338 ? 18.704 22.960  -7.805  1.00 19.57  ? 471 LEU A CD1 1 
ATOM   2418 C CD2 . LEU A 1 338 ? 16.988 21.199  -8.232  1.00 17.40  ? 471 LEU A CD2 1 
ATOM   2419 N N   . THR A 1 339 ? 20.582 19.458  -12.086 1.00 22.52  ? 472 THR A N   1 
ATOM   2420 C CA  . THR A 1 339 ? 20.843 19.412  -13.522 1.00 21.13  ? 472 THR A CA  1 
ATOM   2421 C C   . THR A 1 339 ? 20.874 17.956  -13.986 1.00 23.85  ? 472 THR A C   1 
ATOM   2422 O O   . THR A 1 339 ? 21.479 17.621  -15.009 1.00 23.08  ? 472 THR A O   1 
ATOM   2423 C CB  . THR A 1 339 ? 22.184 20.094  -13.856 1.00 18.54  ? 472 THR A CB  1 
ATOM   2424 O OG1 . THR A 1 339 ? 23.195 19.620  -12.957 1.00 18.22  ? 472 THR A OG1 1 
ATOM   2425 C CG2 . THR A 1 339 ? 22.065 21.605  -13.720 1.00 15.92  ? 472 THR A CG2 1 
ATOM   2426 N N   . SER A 1 340 ? 20.200 17.091  -13.238 1.00 22.78  ? 473 SER A N   1 
ATOM   2427 C CA  . SER A 1 340 ? 20.189 15.682  -13.584 1.00 25.75  ? 473 SER A CA  1 
ATOM   2428 C C   . SER A 1 340 ? 18.982 14.877  -13.109 1.00 25.15  ? 473 SER A C   1 
ATOM   2429 O O   . SER A 1 340 ? 18.418 15.129  -12.047 1.00 23.44  ? 473 SER A O   1 
ATOM   2430 C CB  . SER A 1 340 ? 21.462 15.026  -13.042 1.00 28.67  ? 473 SER A CB  1 
ATOM   2431 O OG  . SER A 1 340 ? 21.398 13.620  -13.166 1.00 33.84  ? 473 SER A OG  1 
ATOM   2432 N N   . ARG A 1 341 ? 18.608 13.901  -13.930 1.00 26.95  ? 474 ARG A N   1 
ATOM   2433 C CA  . ARG A 1 341 ? 17.517 12.964  -13.661 1.00 29.16  ? 474 ARG A CA  1 
ATOM   2434 C C   . ARG A 1 341 ? 16.149 13.474  -13.214 1.00 30.08  ? 474 ARG A C   1 
ATOM   2435 O O   . ARG A 1 341 ? 15.623 13.059  -12.184 1.00 31.29  ? 474 ARG A O   1 
ATOM   2436 C CB  . ARG A 1 341 ? 18.008 11.888  -12.681 1.00 30.21  ? 474 ARG A CB  1 
ATOM   2437 C CG  . ARG A 1 341 ? 19.363 11.315  -13.085 1.00 34.06  ? 474 ARG A CG  1 
ATOM   2438 C CD  . ARG A 1 341 ? 19.729 10.017  -12.369 1.00 37.48  ? 474 ARG A CD  1 
ATOM   2439 N NE  . ARG A 1 341 ? 19.456 10.007  -10.931 1.00 44.49  ? 474 ARG A NE  1 
ATOM   2440 C CZ  . ARG A 1 341 ? 19.815 10.957  -10.065 1.00 47.18  ? 474 ARG A CZ  1 
ATOM   2441 N NH1 . ARG A 1 341 ? 20.474 12.041  -10.468 1.00 47.78  ? 474 ARG A NH1 1 
ATOM   2442 N NH2 . ARG A 1 341 ? 19.517 10.813  -8.780  1.00 45.02  ? 474 ARG A NH2 1 
ATOM   2443 N N   . HIS A 1 342 ? 15.575 14.382  -13.993 1.00 31.10  ? 475 HIS A N   1 
ATOM   2444 C CA  . HIS A 1 342 ? 14.234 14.871  -13.720 1.00 30.44  ? 475 HIS A CA  1 
ATOM   2445 C C   . HIS A 1 342 ? 13.747 15.656  -14.930 1.00 32.25  ? 475 HIS A C   1 
ATOM   2446 O O   . HIS A 1 342 ? 14.547 16.146  -15.729 1.00 30.88  ? 475 HIS A O   1 
ATOM   2447 C CB  . HIS A 1 342 ? 14.168 15.688  -12.415 1.00 28.12  ? 475 HIS A CB  1 
ATOM   2448 C CG  . HIS A 1 342 ? 14.580 17.121  -12.545 1.00 25.01  ? 475 HIS A CG  1 
ATOM   2449 N ND1 . HIS A 1 342 ? 15.880 17.544  -12.367 1.00 25.65  ? 475 HIS A ND1 1 
ATOM   2450 C CD2 . HIS A 1 342 ? 13.848 18.238  -12.770 1.00 23.85  ? 475 HIS A CD2 1 
ATOM   2451 C CE1 . HIS A 1 342 ? 15.930 18.861  -12.469 1.00 24.31  ? 475 HIS A CE1 1 
ATOM   2452 N NE2 . HIS A 1 342 ? 14.710 19.306  -12.713 1.00 26.91  ? 475 HIS A NE2 1 
ATOM   2453 N N   . GLN A 1 343 ? 12.430 15.747  -15.072 1.00 34.05  ? 476 GLN A N   1 
ATOM   2454 C CA  . GLN A 1 343 ? 11.808 16.421  -16.206 1.00 35.99  ? 476 GLN A CA  1 
ATOM   2455 C C   . GLN A 1 343 ? 12.365 17.801  -16.569 1.00 36.09  ? 476 GLN A C   1 
ATOM   2456 O O   . GLN A 1 343 ? 12.342 18.190  -17.741 1.00 35.53  ? 476 GLN A O   1 
ATOM   2457 C CB  . GLN A 1 343 ? 10.298 16.520  -15.971 1.00 39.52  ? 476 GLN A CB  1 
ATOM   2458 C CG  . GLN A 1 343 ? 9.497  16.900  -17.206 1.00 44.51  ? 476 GLN A CG  1 
ATOM   2459 C CD  . GLN A 1 343 ? 7.998  16.904  -16.948 1.00 49.63  ? 476 GLN A CD  1 
ATOM   2460 O OE1 . GLN A 1 343 ? 7.482  17.753  -16.216 1.00 50.23  ? 476 GLN A OE1 1 
ATOM   2461 N NE2 . GLN A 1 343 ? 7.292  15.946  -17.545 1.00 50.87  ? 476 GLN A NE2 1 
ATOM   2462 N N   . GLU A 1 344 ? 12.876 18.534  -15.584 1.00 34.21  ? 477 GLU A N   1 
ATOM   2463 C CA  . GLU A 1 344 ? 13.405 19.871  -15.847 1.00 34.21  ? 477 GLU A CA  1 
ATOM   2464 C C   . GLU A 1 344 ? 14.929 19.998  -15.816 1.00 31.26  ? 477 GLU A C   1 
ATOM   2465 O O   . GLU A 1 344 ? 15.458 21.110  -15.780 1.00 30.96  ? 477 GLU A O   1 
ATOM   2466 C CB  . GLU A 1 344 ? 12.801 20.870  -14.858 1.00 37.83  ? 477 GLU A CB  1 
ATOM   2467 C CG  . GLU A 1 344 ? 11.294 20.984  -14.946 1.00 44.24  ? 477 GLU A CG  1 
ATOM   2468 C CD  . GLU A 1 344 ? 10.836 21.463  -16.303 1.00 48.00  ? 477 GLU A CD  1 
ATOM   2469 O OE1 . GLU A 1 344 ? 11.172 22.609  -16.672 1.00 51.34  ? 477 GLU A OE1 1 
ATOM   2470 O OE2 . GLU A 1 344 ? 10.147 20.692  -17.004 1.00 51.68  ? 477 GLU A OE2 1 
ATOM   2471 N N   . ALA A 1 345 ? 15.635 18.874  -15.838 1.00 27.95  ? 478 ALA A N   1 
ATOM   2472 C CA  . ALA A 1 345 ? 17.095 18.909  -15.807 1.00 27.03  ? 478 ALA A CA  1 
ATOM   2473 C C   . ALA A 1 345 ? 17.680 19.702  -16.979 1.00 25.15  ? 478 ALA A C   1 
ATOM   2474 O O   . ALA A 1 345 ? 18.594 20.508  -16.796 1.00 22.49  ? 478 ALA A O   1 
ATOM   2475 C CB  . ALA A 1 345 ? 17.662 17.472  -15.799 1.00 27.18  ? 478 ALA A CB  1 
ATOM   2476 N N   . GLU A 1 346 ? 17.152 19.483  -18.180 1.00 26.30  ? 479 GLU A N   1 
ATOM   2477 C CA  . GLU A 1 346 ? 17.650 20.182  -19.363 1.00 28.18  ? 479 GLU A CA  1 
ATOM   2478 C C   . GLU A 1 346 ? 17.487 21.688  -19.223 1.00 29.29  ? 479 GLU A C   1 
ATOM   2479 O O   . GLU A 1 346 ? 18.395 22.452  -19.544 1.00 29.44  ? 479 GLU A O   1 
ATOM   2480 C CB  . GLU A 1 346 ? 16.927 19.692  -20.618 1.00 31.38  ? 479 GLU A CB  1 
ATOM   2481 C CG  . GLU A 1 346 ? 17.347 18.298  -21.058 1.00 39.69  ? 479 GLU A CG  1 
ATOM   2482 C CD  . GLU A 1 346 ? 16.485 17.756  -22.185 1.00 43.98  ? 479 GLU A CD  1 
ATOM   2483 O OE1 . GLU A 1 346 ? 16.168 18.528  -23.115 1.00 46.44  ? 479 GLU A OE1 1 
ATOM   2484 O OE2 . GLU A 1 346 ? 16.134 16.557  -22.144 1.00 46.94  ? 479 GLU A OE2 1 
ATOM   2485 N N   . MET A 1 347 ? 16.326 22.114  -18.743 1.00 29.64  ? 480 MET A N   1 
ATOM   2486 C CA  . MET A 1 347 ? 16.077 23.530  -18.547 1.00 30.93  ? 480 MET A CA  1 
ATOM   2487 C C   . MET A 1 347 ? 17.086 24.065  -17.531 1.00 28.23  ? 480 MET A C   1 
ATOM   2488 O O   . MET A 1 347 ? 17.645 25.148  -17.703 1.00 27.49  ? 480 MET A O   1 
ATOM   2489 C CB  . MET A 1 347 ? 14.649 23.744  -18.035 1.00 35.42  ? 480 MET A CB  1 
ATOM   2490 C CG  . MET A 1 347 ? 14.235 25.201  -17.935 1.00 43.01  ? 480 MET A CG  1 
ATOM   2491 S SD  . MET A 1 347 ? 12.518 25.390  -17.392 1.00 54.38  ? 480 MET A SD  1 
ATOM   2492 C CE  . MET A 1 347 ? 11.631 24.683  -18.801 1.00 49.44  ? 480 MET A CE  1 
ATOM   2493 N N   . ALA A 1 348 ? 17.330 23.293  -16.476 1.00 25.62  ? 481 ALA A N   1 
ATOM   2494 C CA  . ALA A 1 348 ? 18.274 23.707  -15.437 1.00 25.26  ? 481 ALA A CA  1 
ATOM   2495 C C   . ALA A 1 348 ? 19.692 23.852  -15.992 1.00 24.50  ? 481 ALA A C   1 
ATOM   2496 O O   . ALA A 1 348 ? 20.407 24.804  -15.665 1.00 24.96  ? 481 ALA A O   1 
ATOM   2497 C CB  . ALA A 1 348 ? 18.260 22.705  -14.286 1.00 24.56  ? 481 ALA A CB  1 
ATOM   2498 N N   . GLN A 1 349 ? 20.103 22.904  -16.828 1.00 24.88  ? 482 GLN A N   1 
ATOM   2499 C CA  . GLN A 1 349 ? 21.436 22.948  -17.429 1.00 24.32  ? 482 GLN A CA  1 
ATOM   2500 C C   . GLN A 1 349 ? 21.620 24.247  -18.212 1.00 25.97  ? 482 GLN A C   1 
ATOM   2501 O O   . GLN A 1 349 ? 22.683 24.868  -18.165 1.00 25.39  ? 482 GLN A O   1 
ATOM   2502 C CB  . GLN A 1 349 ? 21.626 21.759  -18.367 1.00 23.47  ? 482 GLN A CB  1 
ATOM   2503 C CG  . GLN A 1 349 ? 21.750 20.418  -17.673 1.00 19.26  ? 482 GLN A CG  1 
ATOM   2504 C CD  . GLN A 1 349 ? 21.316 19.287  -18.580 1.00 21.95  ? 482 GLN A CD  1 
ATOM   2505 O OE1 . GLN A 1 349 ? 21.278 19.445  -19.795 1.00 22.41  ? 482 GLN A OE1 1 
ATOM   2506 N NE2 . GLN A 1 349 ? 20.996 18.139  -17.998 1.00 19.26  ? 482 GLN A NE2 1 
ATOM   2507 N N   . ASN A 1 350 ? 20.577 24.644  -18.937 1.00 26.87  ? 483 ASN A N   1 
ATOM   2508 C CA  . ASN A 1 350 ? 20.603 25.871  -19.723 1.00 28.65  ? 483 ASN A CA  1 
ATOM   2509 C C   . ASN A 1 350 ? 20.524 27.096  -18.831 1.00 27.70  ? 483 ASN A C   1 
ATOM   2510 O O   . ASN A 1 350 ? 21.156 28.117  -19.107 1.00 28.99  ? 483 ASN A O   1 
ATOM   2511 C CB  . ASN A 1 350 ? 19.424 25.905  -20.697 1.00 34.14  ? 483 ASN A CB  1 
ATOM   2512 C CG  . ASN A 1 350 ? 19.803 25.452  -22.083 1.00 37.17  ? 483 ASN A CG  1 
ATOM   2513 O OD1 . ASN A 1 350 ? 20.561 26.129  -22.782 1.00 38.62  ? 483 ASN A OD1 1 
ATOM   2514 N ND2 . ASN A 1 350 ? 19.284 24.296  -22.492 1.00 40.52  ? 483 ASN A ND2 1 
ATOM   2515 N N   . ALA A 1 351 ? 19.736 26.993  -17.766 1.00 27.07  ? 484 ALA A N   1 
ATOM   2516 C CA  . ALA A 1 351 ? 19.560 28.104  -16.842 1.00 25.88  ? 484 ALA A CA  1 
ATOM   2517 C C   . ALA A 1 351 ? 20.875 28.530  -16.204 1.00 25.98  ? 484 ALA A C   1 
ATOM   2518 O O   . ALA A 1 351 ? 21.129 29.725  -16.037 1.00 25.47  ? 484 ALA A O   1 
ATOM   2519 C CB  . ALA A 1 351 ? 18.541 27.734  -15.760 1.00 26.83  ? 484 ALA A CB  1 
ATOM   2520 N N   . VAL A 1 352 ? 21.715 27.562  -15.845 1.00 23.53  ? 485 VAL A N   1 
ATOM   2521 C CA  . VAL A 1 352 ? 22.997 27.887  -15.227 1.00 20.64  ? 485 VAL A CA  1 
ATOM   2522 C C   . VAL A 1 352 ? 23.821 28.817  -16.114 1.00 22.44  ? 485 VAL A C   1 
ATOM   2523 O O   . VAL A 1 352 ? 24.515 29.704  -15.612 1.00 23.63  ? 485 VAL A O   1 
ATOM   2524 C CB  . VAL A 1 352 ? 23.820 26.612  -14.931 1.00 18.97  ? 485 VAL A CB  1 
ATOM   2525 C CG1 . VAL A 1 352 ? 25.240 26.997  -14.512 1.00 15.54  ? 485 VAL A CG1 1 
ATOM   2526 C CG2 . VAL A 1 352 ? 23.136 25.801  -13.828 1.00 14.82  ? 485 VAL A CG2 1 
ATOM   2527 N N   . ARG A 1 353 ? 23.747 28.610  -17.429 1.00 22.59  ? 486 ARG A N   1 
ATOM   2528 C CA  . ARG A 1 353 ? 24.491 29.442  -18.373 1.00 23.73  ? 486 ARG A CA  1 
ATOM   2529 C C   . ARG A 1 353 ? 23.847 30.818  -18.534 1.00 24.90  ? 486 ARG A C   1 
ATOM   2530 O O   . ARG A 1 353 ? 24.535 31.836  -18.523 1.00 23.72  ? 486 ARG A O   1 
ATOM   2531 C CB  . ARG A 1 353 ? 24.566 28.782  -19.750 1.00 23.08  ? 486 ARG A CB  1 
ATOM   2532 C CG  . ARG A 1 353 ? 25.410 29.578  -20.751 1.00 25.11  ? 486 ARG A CG  1 
ATOM   2533 C CD  . ARG A 1 353 ? 25.367 28.993  -22.158 1.00 25.81  ? 486 ARG A CD  1 
ATOM   2534 N NE  . ARG A 1 353 ? 24.082 29.218  -22.821 1.00 25.65  ? 486 ARG A NE  1 
ATOM   2535 C CZ  . ARG A 1 353 ? 23.073 28.351  -22.850 1.00 26.64  ? 486 ARG A CZ  1 
ATOM   2536 N NH1 . ARG A 1 353 ? 23.176 27.166  -22.253 1.00 23.08  ? 486 ARG A NH1 1 
ATOM   2537 N NH2 . ARG A 1 353 ? 21.946 28.679  -23.472 1.00 22.96  ? 486 ARG A NH2 1 
ATOM   2538 N N   . LEU A 1 354 ? 22.528 30.832  -18.692 1.00 26.23  ? 487 LEU A N   1 
ATOM   2539 C CA  . LEU A 1 354 ? 21.786 32.074  -18.870 1.00 29.50  ? 487 LEU A CA  1 
ATOM   2540 C C   . LEU A 1 354 ? 21.955 33.026  -17.685 1.00 30.93  ? 487 LEU A C   1 
ATOM   2541 O O   . LEU A 1 354 ? 21.874 34.243  -17.845 1.00 30.74  ? 487 LEU A O   1 
ATOM   2542 C CB  . LEU A 1 354 ? 20.305 31.764  -19.093 1.00 29.90  ? 487 LEU A CB  1 
ATOM   2543 C CG  . LEU A 1 354 ? 19.976 30.997  -20.382 1.00 32.61  ? 487 LEU A CG  1 
ATOM   2544 C CD1 . LEU A 1 354 ? 18.483 30.744  -20.472 1.00 33.81  ? 487 LEU A CD1 1 
ATOM   2545 C CD2 . LEU A 1 354 ? 20.445 31.792  -21.589 1.00 33.45  ? 487 LEU A CD2 1 
ATOM   2546 N N   . HIS A 1 355 ? 22.209 32.475  -16.500 1.00 31.09  ? 488 HIS A N   1 
ATOM   2547 C CA  . HIS A 1 355 ? 22.392 33.304  -15.315 1.00 30.71  ? 488 HIS A CA  1 
ATOM   2548 C C   . HIS A 1 355 ? 23.866 33.550  -15.011 1.00 31.37  ? 488 HIS A C   1 
ATOM   2549 O O   . HIS A 1 355 ? 24.243 33.830  -13.872 1.00 28.75  ? 488 HIS A O   1 
ATOM   2550 C CB  . HIS A 1 355 ? 21.681 32.669  -14.120 1.00 32.42  ? 488 HIS A CB  1 
ATOM   2551 C CG  . HIS A 1 355 ? 20.193 32.606  -14.281 1.00 32.98  ? 488 HIS A CG  1 
ATOM   2552 N ND1 . HIS A 1 355 ? 19.408 33.736  -14.370 1.00 34.53  ? 488 HIS A ND1 1 
ATOM   2553 C CD2 . HIS A 1 355 ? 19.353 31.553  -14.417 1.00 34.45  ? 488 HIS A CD2 1 
ATOM   2554 C CE1 . HIS A 1 355 ? 18.149 33.381  -14.557 1.00 33.93  ? 488 HIS A CE1 1 
ATOM   2555 N NE2 . HIS A 1 355 ? 18.088 32.062  -14.590 1.00 33.94  ? 488 HIS A NE2 1 
ATOM   2556 N N   . TYR A 1 356 ? 24.691 33.441  -16.052 1.00 31.03  ? 489 TYR A N   1 
ATOM   2557 C CA  . TYR A 1 356 ? 26.131 33.680  -15.968 1.00 32.13  ? 489 TYR A CA  1 
ATOM   2558 C C   . TYR A 1 356 ? 26.888 32.814  -14.964 1.00 31.61  ? 489 TYR A C   1 
ATOM   2559 O O   . TYR A 1 356 ? 27.854 33.269  -14.346 1.00 31.08  ? 489 TYR A O   1 
ATOM   2560 C CB  . TYR A 1 356 ? 26.384 35.161  -15.661 1.00 36.86  ? 489 TYR A CB  1 
ATOM   2561 C CG  . TYR A 1 356 ? 25.626 36.098  -16.580 1.00 41.59  ? 489 TYR A CG  1 
ATOM   2562 C CD1 . TYR A 1 356 ? 24.271 36.358  -16.378 1.00 43.43  ? 489 TYR A CD1 1 
ATOM   2563 C CD2 . TYR A 1 356 ? 26.250 36.683  -17.682 1.00 45.57  ? 489 TYR A CD2 1 
ATOM   2564 C CE1 . TYR A 1 356 ? 23.553 37.174  -17.250 1.00 47.83  ? 489 TYR A CE1 1 
ATOM   2565 C CE2 . TYR A 1 356 ? 25.539 37.504  -18.563 1.00 48.56  ? 489 TYR A CE2 1 
ATOM   2566 C CZ  . TYR A 1 356 ? 24.191 37.743  -18.339 1.00 48.79  ? 489 TYR A CZ  1 
ATOM   2567 O OH  . TYR A 1 356 ? 23.481 38.547  -19.200 1.00 51.50  ? 489 TYR A OH  1 
ATOM   2568 N N   . GLY A 1 357 ? 26.474 31.559  -14.826 1.00 30.11  ? 490 GLY A N   1 
ATOM   2569 C CA  . GLY A 1 357 ? 27.129 30.675  -13.880 1.00 27.97  ? 490 GLY A CA  1 
ATOM   2570 C C   . GLY A 1 357 ? 28.293 29.835  -14.383 1.00 27.98  ? 490 GLY A C   1 
ATOM   2571 O O   . GLY A 1 357 ? 29.041 29.290  -13.573 1.00 27.29  ? 490 GLY A O   1 
ATOM   2572 N N   . LEU A 1 358 ? 28.467 29.719  -15.696 1.00 25.44  ? 491 LEU A N   1 
ATOM   2573 C CA  . LEU A 1 358 ? 29.563 28.900  -16.221 1.00 26.32  ? 491 LEU A CA  1 
ATOM   2574 C C   . LEU A 1 358 ? 30.968 29.361  -15.819 1.00 25.86  ? 491 LEU A C   1 
ATOM   2575 O O   . LEU A 1 358 ? 31.807 28.541  -15.458 1.00 25.65  ? 491 LEU A O   1 
ATOM   2576 C CB  . LEU A 1 358 ? 29.463 28.780  -17.747 1.00 25.60  ? 491 LEU A CB  1 
ATOM   2577 C CG  . LEU A 1 358 ? 28.231 28.018  -18.253 1.00 27.79  ? 491 LEU A CG  1 
ATOM   2578 C CD1 . LEU A 1 358 ? 28.360 27.782  -19.747 1.00 25.82  ? 491 LEU A CD1 1 
ATOM   2579 C CD2 . LEU A 1 358 ? 28.104 26.680  -17.523 1.00 26.09  ? 491 LEU A CD2 1 
ATOM   2580 N N   . PRO A 1 359 ? 31.245 30.677  -15.875 1.00 27.74  ? 492 PRO A N   1 
ATOM   2581 C CA  . PRO A 1 359 ? 32.578 31.162  -15.497 1.00 27.53  ? 492 PRO A CA  1 
ATOM   2582 C C   . PRO A 1 359 ? 32.957 30.819  -14.053 1.00 28.03  ? 492 PRO A C   1 
ATOM   2583 O O   . PRO A 1 359 ? 34.087 30.408  -13.780 1.00 27.67  ? 492 PRO A O   1 
ATOM   2584 C CB  . PRO A 1 359 ? 32.478 32.672  -15.726 1.00 29.20  ? 492 PRO A CB  1 
ATOM   2585 C CG  . PRO A 1 359 ? 31.466 32.784  -16.828 1.00 30.09  ? 492 PRO A CG  1 
ATOM   2586 C CD  . PRO A 1 359 ? 30.418 31.774  -16.409 1.00 27.81  ? 492 PRO A CD  1 
ATOM   2587 N N   . VAL A 1 360 ? 32.018 30.988  -13.128 1.00 29.19  ? 493 VAL A N   1 
ATOM   2588 C CA  . VAL A 1 360 ? 32.301 30.684  -11.729 1.00 30.04  ? 493 VAL A CA  1 
ATOM   2589 C C   . VAL A 1 360 ? 32.403 29.186  -11.463 1.00 29.02  ? 493 VAL A C   1 
ATOM   2590 O O   . VAL A 1 360 ? 33.244 28.757  -10.671 1.00 29.68  ? 493 VAL A O   1 
ATOM   2591 C CB  . VAL A 1 360 ? 31.244 31.298  -10.781 1.00 32.87  ? 493 VAL A CB  1 
ATOM   2592 C CG1 . VAL A 1 360 ? 31.208 32.802  -10.983 1.00 36.80  ? 493 VAL A CG1 1 
ATOM   2593 C CG2 . VAL A 1 360 ? 29.873 30.698  -11.037 1.00 33.05  ? 493 VAL A CG2 1 
ATOM   2594 N N   . VAL A 1 361 ? 31.564 28.386  -12.121 1.00 25.76  ? 494 VAL A N   1 
ATOM   2595 C CA  . VAL A 1 361 ? 31.627 26.938  -11.923 1.00 23.47  ? 494 VAL A CA  1 
ATOM   2596 C C   . VAL A 1 361 ? 32.996 26.405  -12.344 1.00 24.07  ? 494 VAL A C   1 
ATOM   2597 O O   . VAL A 1 361 ? 33.632 25.645  -11.612 1.00 22.74  ? 494 VAL A O   1 
ATOM   2598 C CB  . VAL A 1 361 ? 30.524 26.199  -12.723 1.00 24.41  ? 494 VAL A CB  1 
ATOM   2599 C CG1 . VAL A 1 361 ? 30.773 24.696  -12.683 1.00 23.08  ? 494 VAL A CG1 1 
ATOM   2600 C CG2 . VAL A 1 361 ? 29.155 26.505  -12.126 1.00 22.27  ? 494 VAL A CG2 1 
ATOM   2601 N N   . VAL A 1 362 ? 33.463 26.811  -13.520 1.00 24.03  ? 495 VAL A N   1 
ATOM   2602 C CA  . VAL A 1 362 ? 34.765 26.357  -13.990 1.00 23.74  ? 495 VAL A CA  1 
ATOM   2603 C C   . VAL A 1 362 ? 35.890 26.875  -13.087 1.00 25.83  ? 495 VAL A C   1 
ATOM   2604 O O   . VAL A 1 362 ? 36.883 26.180  -12.851 1.00 24.67  ? 495 VAL A O   1 
ATOM   2605 C CB  . VAL A 1 362 ? 35.004 26.798  -15.453 1.00 22.92  ? 495 VAL A CB  1 
ATOM   2606 C CG1 . VAL A 1 362 ? 36.415 26.445  -15.893 1.00 20.61  ? 495 VAL A CG1 1 
ATOM   2607 C CG2 . VAL A 1 362 ? 33.987 26.115  -16.357 1.00 21.78  ? 495 VAL A CG2 1 
ATOM   2608 N N   . LYS A 1 363 ? 35.726 28.090  -12.568 1.00 25.93  ? 496 LYS A N   1 
ATOM   2609 C CA  . LYS A 1 363 ? 36.733 28.681  -11.685 1.00 27.13  ? 496 LYS A CA  1 
ATOM   2610 C C   . LYS A 1 363 ? 36.959 27.810  -10.445 1.00 26.40  ? 496 LYS A C   1 
ATOM   2611 O O   . LYS A 1 363 ? 38.095 27.647  -9.982  1.00 25.22  ? 496 LYS A O   1 
ATOM   2612 C CB  . LYS A 1 363 ? 36.291 30.085  -11.249 1.00 30.45  ? 496 LYS A CB  1 
ATOM   2613 C CG  . LYS A 1 363 ? 37.306 30.843  -10.395 1.00 33.65  ? 496 LYS A CG  1 
ATOM   2614 C CD  . LYS A 1 363 ? 36.717 32.168  -9.915  1.00 39.40  ? 496 LYS A CD  1 
ATOM   2615 C CE  . LYS A 1 363 ? 37.757 33.047  -9.223  1.00 43.25  ? 496 LYS A CE  1 
ATOM   2616 N NZ  . LYS A 1 363 ? 38.370 32.375  -8.040  1.00 46.56  ? 496 LYS A NZ  1 
ATOM   2617 N N   . LEU A 1 364 ? 35.878 27.233  -9.924  1.00 24.21  ? 497 LEU A N   1 
ATOM   2618 C CA  . LEU A 1 364 ? 35.969 26.405  -8.729  1.00 23.77  ? 497 LEU A CA  1 
ATOM   2619 C C   . LEU A 1 364 ? 36.810 25.132  -8.891  1.00 24.28  ? 497 LEU A C   1 
ATOM   2620 O O   . LEU A 1 364 ? 37.092 24.440  -7.906  1.00 21.68  ? 497 LEU A O   1 
ATOM   2621 C CB  . LEU A 1 364 ? 34.559 26.083  -8.214  1.00 26.58  ? 497 LEU A CB  1 
ATOM   2622 C CG  . LEU A 1 364 ? 33.820 27.342  -7.726  1.00 28.75  ? 497 LEU A CG  1 
ATOM   2623 C CD1 . LEU A 1 364 ? 32.407 27.005  -7.266  1.00 28.11  ? 497 LEU A CD1 1 
ATOM   2624 C CD2 . LEU A 1 364 ? 34.617 27.980  -6.579  1.00 28.56  ? 497 LEU A CD2 1 
ATOM   2625 N N   . LEU A 1 365 ? 37.218 24.827  -10.122 1.00 20.48  ? 498 LEU A N   1 
ATOM   2626 C CA  . LEU A 1 365 ? 38.066 23.658  -10.368 1.00 22.28  ? 498 LEU A CA  1 
ATOM   2627 C C   . LEU A 1 365 ? 39.523 23.942  -9.953  1.00 24.29  ? 498 LEU A C   1 
ATOM   2628 O O   . LEU A 1 365 ? 40.328 23.018  -9.805  1.00 22.52  ? 498 LEU A O   1 
ATOM   2629 C CB  . LEU A 1 365 ? 38.067 23.280  -11.859 1.00 20.63  ? 498 LEU A CB  1 
ATOM   2630 C CG  . LEU A 1 365 ? 36.836 22.672  -12.535 1.00 21.37  ? 498 LEU A CG  1 
ATOM   2631 C CD1 . LEU A 1 365 ? 37.185 22.360  -13.991 1.00 20.83  ? 498 LEU A CD1 1 
ATOM   2632 C CD2 . LEU A 1 365 ? 36.412 21.403  -11.814 1.00 17.06  ? 498 LEU A CD2 1 
ATOM   2633 N N   . HIS A 1 366 ? 39.858 25.219  -9.773  1.00 25.43  ? 499 HIS A N   1 
ATOM   2634 C CA  . HIS A 1 366 ? 41.227 25.601  -9.423  1.00 27.93  ? 499 HIS A CA  1 
ATOM   2635 C C   . HIS A 1 366 ? 41.441 25.943  -7.951  1.00 28.26  ? 499 HIS A C   1 
ATOM   2636 O O   . HIS A 1 366 ? 40.488 26.122  -7.201  1.00 27.68  ? 499 HIS A O   1 
ATOM   2637 C CB  . HIS A 1 366 ? 41.668 26.806  -10.268 1.00 27.91  ? 499 HIS A CB  1 
ATOM   2638 C CG  . HIS A 1 366 ? 41.534 26.599  -11.747 1.00 31.82  ? 499 HIS A CG  1 
ATOM   2639 N ND1 . HIS A 1 366 ? 40.344 26.776  -12.420 1.00 33.83  ? 499 HIS A ND1 1 
ATOM   2640 C CD2 . HIS A 1 366 ? 42.443 26.232  -12.682 1.00 31.48  ? 499 HIS A CD2 1 
ATOM   2641 C CE1 . HIS A 1 366 ? 40.527 26.531  -13.706 1.00 33.07  ? 499 HIS A CE1 1 
ATOM   2642 N NE2 . HIS A 1 366 ? 41.792 26.198  -13.891 1.00 32.97  ? 499 HIS A NE2 1 
ATOM   2643 N N   . PRO A 1 367 ? 42.711 26.025  -7.515  1.00 30.51  ? 500 PRO A N   1 
ATOM   2644 C CA  . PRO A 1 367 ? 42.963 26.363  -6.110  1.00 29.61  ? 500 PRO A CA  1 
ATOM   2645 C C   . PRO A 1 367 ? 42.301 27.716  -5.864  1.00 29.56  ? 500 PRO A C   1 
ATOM   2646 O O   . PRO A 1 367 ? 42.119 28.495  -6.798  1.00 29.94  ? 500 PRO A O   1 
ATOM   2647 C CB  . PRO A 1 367 ? 44.486 26.446  -6.046  1.00 29.89  ? 500 PRO A CB  1 
ATOM   2648 C CG  . PRO A 1 367 ? 44.913 25.421  -7.072  1.00 29.34  ? 500 PRO A CG  1 
ATOM   2649 C CD  . PRO A 1 367 ? 43.968 25.699  -8.217  1.00 28.67  ? 500 PRO A CD  1 
ATOM   2650 N N   . PRO A 1 368 ? 41.964 28.033  -4.606  1.00 30.68  ? 501 PRO A N   1 
ATOM   2651 C CA  . PRO A 1 368 ? 42.153 27.258  -3.377  1.00 29.58  ? 501 PRO A CA  1 
ATOM   2652 C C   . PRO A 1 368 ? 41.107 26.180  -3.072  1.00 30.05  ? 501 PRO A C   1 
ATOM   2653 O O   . PRO A 1 368 ? 41.061 25.664  -1.956  1.00 28.37  ? 501 PRO A O   1 
ATOM   2654 C CB  . PRO A 1 368 ? 42.172 28.341  -2.312  1.00 30.20  ? 501 PRO A CB  1 
ATOM   2655 C CG  . PRO A 1 368 ? 41.116 29.279  -2.810  1.00 30.91  ? 501 PRO A CG  1 
ATOM   2656 C CD  . PRO A 1 368 ? 41.411 29.368  -4.301  1.00 30.17  ? 501 PRO A CD  1 
ATOM   2657 N N   . SER A 1 369 ? 40.274 25.832  -4.046  1.00 28.87  ? 502 SER A N   1 
ATOM   2658 C CA  . SER A 1 369 ? 39.253 24.813  -3.815  1.00 28.17  ? 502 SER A CA  1 
ATOM   2659 C C   . SER A 1 369 ? 39.833 23.500  -3.294  1.00 27.95  ? 502 SER A C   1 
ATOM   2660 O O   . SER A 1 369 ? 40.857 23.026  -3.785  1.00 26.78  ? 502 SER A O   1 
ATOM   2661 C CB  . SER A 1 369 ? 38.472 24.540  -5.103  1.00 29.36  ? 502 SER A CB  1 
ATOM   2662 O OG  . SER A 1 369 ? 37.675 25.652  -5.464  1.00 28.90  ? 502 SER A OG  1 
ATOM   2663 N N   . HIS A 1 370 ? 39.178 22.913  -2.294  1.00 28.28  ? 503 HIS A N   1 
ATOM   2664 C CA  . HIS A 1 370 ? 39.635 21.640  -1.744  1.00 28.65  ? 503 HIS A CA  1 
ATOM   2665 C C   . HIS A 1 370 ? 38.962 20.506  -2.506  1.00 28.48  ? 503 HIS A C   1 
ATOM   2666 O O   . HIS A 1 370 ? 38.030 20.746  -3.272  1.00 28.38  ? 503 HIS A O   1 
ATOM   2667 C CB  . HIS A 1 370 ? 39.331 21.561  -0.244  1.00 30.24  ? 503 HIS A CB  1 
ATOM   2668 C CG  . HIS A 1 370 ? 40.208 22.447  0.586   1.00 32.62  ? 503 HIS A CG  1 
ATOM   2669 N ND1 . HIS A 1 370 ? 40.224 23.818  0.445   1.00 34.58  ? 503 HIS A ND1 1 
ATOM   2670 C CD2 . HIS A 1 370 ? 41.132 22.156  1.532   1.00 34.86  ? 503 HIS A CD2 1 
ATOM   2671 C CE1 . HIS A 1 370 ? 41.122 24.334  1.267   1.00 34.74  ? 503 HIS A CE1 1 
ATOM   2672 N NE2 . HIS A 1 370 ? 41.687 23.347  1.937   1.00 35.63  ? 503 HIS A NE2 1 
ATOM   2673 N N   . TRP A 1 371 ? 39.431 19.277  -2.300  1.00 27.64  ? 504 TRP A N   1 
ATOM   2674 C CA  . TRP A 1 371 ? 38.896 18.125  -3.019  1.00 27.58  ? 504 TRP A CA  1 
ATOM   2675 C C   . TRP A 1 371 ? 37.388 17.906  -3.031  1.00 26.13  ? 504 TRP A C   1 
ATOM   2676 O O   . TRP A 1 371 ? 36.816 17.643  -4.087  1.00 26.45  ? 504 TRP A O   1 
ATOM   2677 C CB  . TRP A 1 371 ? 39.604 16.840  -2.567  1.00 28.46  ? 504 TRP A CB  1 
ATOM   2678 C CG  . TRP A 1 371 ? 40.960 16.696  -3.198  1.00 29.91  ? 504 TRP A CG  1 
ATOM   2679 C CD1 . TRP A 1 371 ? 42.168 16.663  -2.557  1.00 30.73  ? 504 TRP A CD1 1 
ATOM   2680 C CD2 . TRP A 1 371 ? 41.250 16.615  -4.601  1.00 28.62  ? 504 TRP A CD2 1 
ATOM   2681 N NE1 . TRP A 1 371 ? 43.189 16.572  -3.474  1.00 30.76  ? 504 TRP A NE1 1 
ATOM   2682 C CE2 . TRP A 1 371 ? 42.655 16.542  -4.735  1.00 29.50  ? 504 TRP A CE2 1 
ATOM   2683 C CE3 . TRP A 1 371 ? 40.458 16.603  -5.759  1.00 28.53  ? 504 TRP A CE3 1 
ATOM   2684 C CZ2 . TRP A 1 371 ? 43.286 16.454  -5.979  1.00 28.14  ? 504 TRP A CZ2 1 
ATOM   2685 C CZ3 . TRP A 1 371 ? 41.083 16.517  -6.995  1.00 27.68  ? 504 TRP A CZ3 1 
ATOM   2686 C CH2 . TRP A 1 371 ? 42.487 16.445  -7.096  1.00 28.06  ? 504 TRP A CH2 1 
ATOM   2687 N N   . PRO A 1 372 ? 36.721 18.003  -1.871  1.00 26.21  ? 505 PRO A N   1 
ATOM   2688 C CA  . PRO A 1 372 ? 35.272 17.792  -1.886  1.00 25.24  ? 505 PRO A CA  1 
ATOM   2689 C C   . PRO A 1 372 ? 34.550 18.706  -2.874  1.00 24.84  ? 505 PRO A C   1 
ATOM   2690 O O   . PRO A 1 372 ? 33.683 18.255  -3.630  1.00 22.77  ? 505 PRO A O   1 
ATOM   2691 C CB  . PRO A 1 372 ? 34.875 18.059  -0.436  1.00 27.97  ? 505 PRO A CB  1 
ATOM   2692 C CG  . PRO A 1 372 ? 36.062 17.529  0.313   1.00 27.71  ? 505 PRO A CG  1 
ATOM   2693 C CD  . PRO A 1 372 ? 37.219 18.118  -0.488  1.00 25.37  ? 505 PRO A CD  1 
ATOM   2694 N N   . LEU A 1 373 ? 34.908 19.987  -2.867  1.00 23.97  ? 506 LEU A N   1 
ATOM   2695 C CA  . LEU A 1 373 ? 34.293 20.953  -3.774  1.00 24.45  ? 506 LEU A CA  1 
ATOM   2696 C C   . LEU A 1 373 ? 34.706 20.677  -5.224  1.00 23.92  ? 506 LEU A C   1 
ATOM   2697 O O   . LEU A 1 373 ? 33.907 20.840  -6.145  1.00 23.18  ? 506 LEU A O   1 
ATOM   2698 C CB  . LEU A 1 373 ? 34.695 22.382  -3.381  1.00 23.36  ? 506 LEU A CB  1 
ATOM   2699 C CG  . LEU A 1 373 ? 34.356 23.525  -4.348  1.00 25.44  ? 506 LEU A CG  1 
ATOM   2700 C CD1 . LEU A 1 373 ? 32.850 23.622  -4.551  1.00 23.19  ? 506 LEU A CD1 1 
ATOM   2701 C CD2 . LEU A 1 373 ? 34.903 24.840  -3.789  1.00 25.36  ? 506 LEU A CD2 1 
ATOM   2702 N N   . ILE A 1 374 ? 35.952 20.263  -5.432  1.00 23.73  ? 507 ILE A N   1 
ATOM   2703 C CA  . ILE A 1 374 ? 36.403 19.981  -6.791  1.00 23.82  ? 507 ILE A CA  1 
ATOM   2704 C C   . ILE A 1 374 ? 35.602 18.812  -7.357  1.00 24.11  ? 507 ILE A C   1 
ATOM   2705 O O   . ILE A 1 374 ? 35.164 18.851  -8.508  1.00 22.74  ? 507 ILE A O   1 
ATOM   2706 C CB  . ILE A 1 374 ? 37.907 19.652  -6.839  1.00 23.89  ? 507 ILE A CB  1 
ATOM   2707 C CG1 . ILE A 1 374 ? 38.712 20.920  -6.547  1.00 24.84  ? 507 ILE A CG1 1 
ATOM   2708 C CG2 . ILE A 1 374 ? 38.293 19.110  -8.223  1.00 21.44  ? 507 ILE A CG2 1 
ATOM   2709 C CD1 . ILE A 1 374 ? 40.209 20.710  -6.567  1.00 25.21  ? 507 ILE A CD1 1 
ATOM   2710 N N   . LYS A 1 375 ? 35.395 17.786  -6.536  1.00 23.78  ? 508 LYS A N   1 
ATOM   2711 C CA  . LYS A 1 375 ? 34.639 16.615  -6.963  1.00 23.90  ? 508 LYS A CA  1 
ATOM   2712 C C   . LYS A 1 375 ? 33.209 16.984  -7.333  1.00 23.93  ? 508 LYS A C   1 
ATOM   2713 O O   . LYS A 1 375 ? 32.683 16.524  -8.347  1.00 23.30  ? 508 LYS A O   1 
ATOM   2714 C CB  . LYS A 1 375 ? 34.623 15.552  -5.862  1.00 25.64  ? 508 LYS A CB  1 
ATOM   2715 C CG  . LYS A 1 375 ? 33.838 14.297  -6.240  1.00 30.20  ? 508 LYS A CG  1 
ATOM   2716 C CD  . LYS A 1 375 ? 34.157 13.126  -5.312  1.00 34.42  ? 508 LYS A CD  1 
ATOM   2717 C CE  . LYS A 1 375 ? 33.581 13.329  -3.930  1.00 37.70  ? 508 LYS A CE  1 
ATOM   2718 N NZ  . LYS A 1 375 ? 32.096 13.199  -3.937  1.00 41.54  ? 508 LYS A NZ  1 
ATOM   2719 N N   . ALA A 1 376 ? 32.574 17.809  -6.508  1.00 23.34  ? 509 ALA A N   1 
ATOM   2720 C CA  . ALA A 1 376 ? 31.204 18.224  -6.786  1.00 22.64  ? 509 ALA A CA  1 
ATOM   2721 C C   . ALA A 1 376 ? 31.149 19.072  -8.061  1.00 20.47  ? 509 ALA A C   1 
ATOM   2722 O O   . ALA A 1 376 ? 30.239 18.921  -8.876  1.00 21.83  ? 509 ALA A O   1 
ATOM   2723 C CB  . ALA A 1 376 ? 30.640 19.007  -5.598  1.00 22.44  ? 509 ALA A CB  1 
ATOM   2724 N N   . THR A 1 377 ? 32.128 19.956  -8.230  1.00 19.03  ? 510 THR A N   1 
ATOM   2725 C CA  . THR A 1 377 ? 32.195 20.828  -9.399  1.00 18.81  ? 510 THR A CA  1 
ATOM   2726 C C   . THR A 1 377 ? 32.370 20.031  -10.695 1.00 19.00  ? 510 THR A C   1 
ATOM   2727 O O   . THR A 1 377 ? 31.753 20.342  -11.713 1.00 18.62  ? 510 THR A O   1 
ATOM   2728 C CB  . THR A 1 377 ? 33.363 21.836  -9.263  1.00 20.54  ? 510 THR A CB  1 
ATOM   2729 O OG1 . THR A 1 377 ? 33.141 22.666  -8.114  1.00 21.68  ? 510 THR A OG1 1 
ATOM   2730 C CG2 . THR A 1 377 ? 33.468 22.715  -10.506 1.00 16.94  ? 510 THR A CG2 1 
ATOM   2731 N N   . VAL A 1 378 ? 33.229 19.018  -10.658 1.00 18.55  ? 511 VAL A N   1 
ATOM   2732 C CA  . VAL A 1 378 ? 33.454 18.168  -11.821 1.00 18.88  ? 511 VAL A CA  1 
ATOM   2733 C C   . VAL A 1 378 ? 32.140 17.470  -12.185 1.00 17.87  ? 511 VAL A C   1 
ATOM   2734 O O   . VAL A 1 378 ? 31.778 17.380  -13.359 1.00 17.62  ? 511 VAL A O   1 
ATOM   2735 C CB  . VAL A 1 378 ? 34.541 17.102  -11.520 1.00 19.97  ? 511 VAL A CB  1 
ATOM   2736 C CG1 . VAL A 1 378 ? 34.592 16.060  -12.642 1.00 18.40  ? 511 VAL A CG1 1 
ATOM   2737 C CG2 . VAL A 1 378 ? 35.903 17.790  -11.368 1.00 18.90  ? 511 VAL A CG2 1 
ATOM   2738 N N   . GLY A 1 379 ? 31.432 16.983  -11.169 1.00 17.49  ? 512 GLY A N   1 
ATOM   2739 C CA  . GLY A 1 379 ? 30.159 16.316  -11.402 1.00 20.14  ? 512 GLY A CA  1 
ATOM   2740 C C   . GLY A 1 379 ? 29.126 17.266  -11.997 1.00 21.50  ? 512 GLY A C   1 
ATOM   2741 O O   . GLY A 1 379 ? 28.310 16.873  -12.838 1.00 21.42  ? 512 GLY A O   1 
ATOM   2742 N N   . LEU A 1 380 ? 29.156 18.523  -11.565 1.00 21.86  ? 513 LEU A N   1 
ATOM   2743 C CA  . LEU A 1 380 ? 28.223 19.521  -12.084 1.00 20.44  ? 513 LEU A CA  1 
ATOM   2744 C C   . LEU A 1 380 ? 28.555 19.816  -13.545 1.00 19.83  ? 513 LEU A C   1 
ATOM   2745 O O   . LEU A 1 380 ? 27.662 19.903  -14.391 1.00 20.25  ? 513 LEU A O   1 
ATOM   2746 C CB  . LEU A 1 380 ? 28.303 20.808  -11.258 1.00 18.53  ? 513 LEU A CB  1 
ATOM   2747 C CG  . LEU A 1 380 ? 27.549 22.034  -11.793 1.00 21.44  ? 513 LEU A CG  1 
ATOM   2748 C CD1 . LEU A 1 380 ? 26.088 21.679  -12.083 1.00 19.74  ? 513 LEU A CD1 1 
ATOM   2749 C CD2 . LEU A 1 380 ? 27.634 23.162  -10.768 1.00 19.53  ? 513 LEU A CD2 1 
ATOM   2750 N N   . ILE A 1 381 ? 29.843 19.958  -13.849 1.00 18.77  ? 514 ILE A N   1 
ATOM   2751 C CA  . ILE A 1 381 ? 30.249 20.241  -15.223 1.00 19.87  ? 514 ILE A CA  1 
ATOM   2752 C C   . ILE A 1 381 ? 29.827 19.103  -16.154 1.00 20.75  ? 514 ILE A C   1 
ATOM   2753 O O   . ILE A 1 381 ? 29.438 19.327  -17.303 1.00 20.48  ? 514 ILE A O   1 
ATOM   2754 C CB  . ILE A 1 381 ? 31.771 20.469  -15.311 1.00 17.93  ? 514 ILE A CB  1 
ATOM   2755 C CG1 . ILE A 1 381 ? 32.122 21.811  -14.663 1.00 20.52  ? 514 ILE A CG1 1 
ATOM   2756 C CG2 . ILE A 1 381 ? 32.231 20.429  -16.760 1.00 20.21  ? 514 ILE A CG2 1 
ATOM   2757 C CD1 . ILE A 1 381 ? 33.611 22.063  -14.515 1.00 22.59  ? 514 ILE A CD1 1 
ATOM   2758 N N   . ARG A 1 382 ? 29.899 17.879  -15.652 1.00 20.71  ? 515 ARG A N   1 
ATOM   2759 C CA  . ARG A 1 382 ? 29.509 16.728  -16.449 1.00 22.97  ? 515 ARG A CA  1 
ATOM   2760 C C   . ARG A 1 382 ? 28.032 16.854  -16.839 1.00 23.02  ? 515 ARG A C   1 
ATOM   2761 O O   . ARG A 1 382 ? 27.658 16.583  -17.984 1.00 22.61  ? 515 ARG A O   1 
ATOM   2762 C CB  . ARG A 1 382 ? 29.741 15.441  -15.654 1.00 24.16  ? 515 ARG A CB  1 
ATOM   2763 C CG  . ARG A 1 382 ? 29.638 14.180  -16.490 1.00 32.09  ? 515 ARG A CG  1 
ATOM   2764 C CD  . ARG A 1 382 ? 28.212 13.884  -16.902 1.00 39.67  ? 515 ARG A CD  1 
ATOM   2765 N NE  . ARG A 1 382 ? 27.495 13.148  -15.871 1.00 46.11  ? 515 ARG A NE  1 
ATOM   2766 C CZ  . ARG A 1 382 ? 27.840 11.931  -15.460 1.00 50.73  ? 515 ARG A CZ  1 
ATOM   2767 N NH1 . ARG A 1 382 ? 28.892 11.322  -15.998 1.00 53.14  ? 515 ARG A NH1 1 
ATOM   2768 N NH2 . ARG A 1 382 ? 27.135 11.321  -14.515 1.00 50.85  ? 515 ARG A NH2 1 
ATOM   2769 N N   . ASN A 1 383 ? 27.196 17.255  -15.881 1.00 21.01  ? 516 ASN A N   1 
ATOM   2770 C CA  . ASN A 1 383 ? 25.766 17.430  -16.126 1.00 22.41  ? 516 ASN A CA  1 
ATOM   2771 C C   . ASN A 1 383 ? 25.487 18.611  -17.058 1.00 20.88  ? 516 ASN A C   1 
ATOM   2772 O O   . ASN A 1 383 ? 24.634 18.523  -17.937 1.00 23.47  ? 516 ASN A O   1 
ATOM   2773 C CB  . ASN A 1 383 ? 25.011 17.651  -14.806 1.00 22.77  ? 516 ASN A CB  1 
ATOM   2774 C CG  . ASN A 1 383 ? 24.906 16.391  -13.967 1.00 23.58  ? 516 ASN A CG  1 
ATOM   2775 O OD1 . ASN A 1 383 ? 25.248 15.298  -14.418 1.00 21.04  ? 516 ASN A OD1 1 
ATOM   2776 N ND2 . ASN A 1 383 ? 24.416 16.539  -12.738 1.00 20.96  ? 516 ASN A ND2 1 
ATOM   2777 N N   . LEU A 1 384 ? 26.196 19.718  -16.856 1.00 20.08  ? 517 LEU A N   1 
ATOM   2778 C CA  . LEU A 1 384 ? 26.009 20.903  -17.692 1.00 19.83  ? 517 LEU A CA  1 
ATOM   2779 C C   . LEU A 1 384 ? 26.374 20.611  -19.145 1.00 20.77  ? 517 LEU A C   1 
ATOM   2780 O O   . LEU A 1 384 ? 25.804 21.197  -20.071 1.00 20.46  ? 517 LEU A O   1 
ATOM   2781 C CB  . LEU A 1 384 ? 26.869 22.067  -17.170 1.00 21.35  ? 517 LEU A CB  1 
ATOM   2782 C CG  . LEU A 1 384 ? 26.540 22.575  -15.761 1.00 19.49  ? 517 LEU A CG  1 
ATOM   2783 C CD1 . LEU A 1 384 ? 27.597 23.585  -15.303 1.00 19.72  ? 517 LEU A CD1 1 
ATOM   2784 C CD2 . LEU A 1 384 ? 25.147 23.202  -15.769 1.00 21.02  ? 517 LEU A CD2 1 
ATOM   2785 N N   . ALA A 1 385 ? 27.322 19.696  -19.337 1.00 18.19  ? 518 ALA A N   1 
ATOM   2786 C CA  . ALA A 1 385 ? 27.780 19.323  -20.673 1.00 18.36  ? 518 ALA A CA  1 
ATOM   2787 C C   . ALA A 1 385 ? 26.726 18.535  -21.440 1.00 18.81  ? 518 ALA A C   1 
ATOM   2788 O O   . ALA A 1 385 ? 26.865 18.327  -22.642 1.00 16.78  ? 518 ALA A O   1 
ATOM   2789 C CB  . ALA A 1 385 ? 29.088 18.508  -20.584 1.00 16.29  ? 518 ALA A CB  1 
ATOM   2790 N N   . LEU A 1 386 ? 25.681 18.083  -20.751 1.00 19.19  ? 519 LEU A N   1 
ATOM   2791 C CA  . LEU A 1 386 ? 24.621 17.342  -21.432 1.00 22.14  ? 519 LEU A CA  1 
ATOM   2792 C C   . LEU A 1 386 ? 23.856 18.284  -22.359 1.00 22.07  ? 519 LEU A C   1 
ATOM   2793 O O   . LEU A 1 386 ? 23.206 17.846  -23.307 1.00 25.39  ? 519 LEU A O   1 
ATOM   2794 C CB  . LEU A 1 386 ? 23.665 16.706  -20.417 1.00 21.09  ? 519 LEU A CB  1 
ATOM   2795 C CG  . LEU A 1 386 ? 24.261 15.550  -19.603 1.00 23.58  ? 519 LEU A CG  1 
ATOM   2796 C CD1 . LEU A 1 386 ? 23.298 15.138  -18.495 1.00 22.29  ? 519 LEU A CD1 1 
ATOM   2797 C CD2 . LEU A 1 386 ? 24.548 14.374  -20.531 1.00 19.76  ? 519 LEU A CD2 1 
ATOM   2798 N N   . CYS A 1 387 ? 23.955 19.580  -22.083 1.00 21.77  ? 520 CYS A N   1 
ATOM   2799 C CA  . CYS A 1 387 ? 23.308 20.610  -22.893 1.00 21.75  ? 520 CYS A CA  1 
ATOM   2800 C C   . CYS A 1 387 ? 24.298 21.115  -23.953 1.00 22.03  ? 520 CYS A C   1 
ATOM   2801 O O   . CYS A 1 387 ? 25.318 21.726  -23.620 1.00 22.64  ? 520 CYS A O   1 
ATOM   2802 C CB  . CYS A 1 387 ? 22.861 21.760  -21.983 1.00 21.56  ? 520 CYS A CB  1 
ATOM   2803 S SG  . CYS A 1 387 ? 22.276 23.257  -22.814 1.00 27.71  ? 520 CYS A SG  1 
ATOM   2804 N N   . PRO A 1 388 ? 24.011 20.862  -25.247 1.00 24.36  ? 521 PRO A N   1 
ATOM   2805 C CA  . PRO A 1 388 ? 24.886 21.293  -26.345 1.00 23.77  ? 521 PRO A CA  1 
ATOM   2806 C C   . PRO A 1 388 ? 25.231 22.778  -26.326 1.00 25.15  ? 521 PRO A C   1 
ATOM   2807 O O   . PRO A 1 388 ? 26.328 23.172  -26.737 1.00 25.32  ? 521 PRO A O   1 
ATOM   2808 C CB  . PRO A 1 388 ? 24.092 20.910  -27.591 1.00 26.30  ? 521 PRO A CB  1 
ATOM   2809 C CG  . PRO A 1 388 ? 23.361 19.689  -27.149 1.00 25.76  ? 521 PRO A CG  1 
ATOM   2810 C CD  . PRO A 1 388 ? 22.872 20.086  -25.770 1.00 24.05  ? 521 PRO A CD  1 
ATOM   2811 N N   . ALA A 1 389 ? 24.301 23.604  -25.854 1.00 22.03  ? 522 ALA A N   1 
ATOM   2812 C CA  . ALA A 1 389 ? 24.546 25.040  -25.802 1.00 22.77  ? 522 ALA A CA  1 
ATOM   2813 C C   . ALA A 1 389 ? 25.619 25.393  -24.773 1.00 22.93  ? 522 ALA A C   1 
ATOM   2814 O O   . ALA A 1 389 ? 26.063 26.539  -24.712 1.00 24.83  ? 522 ALA A O   1 
ATOM   2815 C CB  . ALA A 1 389 ? 23.238 25.797  -25.504 1.00 20.30  ? 522 ALA A CB  1 
ATOM   2816 N N   . ASN A 1 390 ? 26.036 24.416  -23.966 1.00 22.34  ? 523 ASN A N   1 
ATOM   2817 C CA  . ASN A 1 390 ? 27.084 24.650  -22.966 1.00 23.50  ? 523 ASN A CA  1 
ATOM   2818 C C   . ASN A 1 390 ? 28.458 24.147  -23.424 1.00 24.30  ? 523 ASN A C   1 
ATOM   2819 O O   . ASN A 1 390 ? 29.476 24.446  -22.798 1.00 25.83  ? 523 ASN A O   1 
ATOM   2820 C CB  . ASN A 1 390 ? 26.742 23.974  -21.626 1.00 21.91  ? 523 ASN A CB  1 
ATOM   2821 C CG  . ASN A 1 390 ? 25.628 24.684  -20.872 1.00 21.34  ? 523 ASN A CG  1 
ATOM   2822 O OD1 . ASN A 1 390 ? 25.376 25.870  -21.090 1.00 21.30  ? 523 ASN A OD1 1 
ATOM   2823 N ND2 . ASN A 1 390 ? 24.968 23.962  -19.961 1.00 17.33  ? 523 ASN A ND2 1 
ATOM   2824 N N   . HIS A 1 391 ? 28.492 23.382  -24.510 1.00 24.77  ? 524 HIS A N   1 
ATOM   2825 C CA  . HIS A 1 391 ? 29.752 22.840  -25.008 1.00 25.51  ? 524 HIS A CA  1 
ATOM   2826 C C   . HIS A 1 391 ? 30.828 23.888  -25.287 1.00 26.37  ? 524 HIS A C   1 
ATOM   2827 O O   . HIS A 1 391 ? 31.938 23.790  -24.767 1.00 26.28  ? 524 HIS A O   1 
ATOM   2828 C CB  . HIS A 1 391 ? 29.505 22.013  -26.271 1.00 26.67  ? 524 HIS A CB  1 
ATOM   2829 C CG  . HIS A 1 391 ? 28.723 20.760  -26.031 1.00 26.69  ? 524 HIS A CG  1 
ATOM   2830 N ND1 . HIS A 1 391 ? 28.270 19.959  -27.056 1.00 26.50  ? 524 HIS A ND1 1 
ATOM   2831 C CD2 . HIS A 1 391 ? 28.322 20.163  -24.882 1.00 27.37  ? 524 HIS A CD2 1 
ATOM   2832 C CE1 . HIS A 1 391 ? 27.623 18.923  -26.551 1.00 27.22  ? 524 HIS A CE1 1 
ATOM   2833 N NE2 . HIS A 1 391 ? 27.640 19.024  -25.234 1.00 28.81  ? 524 HIS A NE2 1 
ATOM   2834 N N   . ALA A 1 392 ? 30.506 24.890  -26.100 1.00 25.32  ? 525 ALA A N   1 
ATOM   2835 C CA  . ALA A 1 392 ? 31.479 25.927  -26.440 1.00 24.72  ? 525 ALA A CA  1 
ATOM   2836 C C   . ALA A 1 392 ? 31.883 26.825  -25.264 1.00 24.67  ? 525 ALA A C   1 
ATOM   2837 O O   . ALA A 1 392 ? 33.072 27.031  -25.015 1.00 25.06  ? 525 ALA A O   1 
ATOM   2838 C CB  . ALA A 1 392 ? 30.956 26.781  -27.607 1.00 25.04  ? 525 ALA A CB  1 
ATOM   2839 N N   . PRO A 1 393 ? 30.906 27.375  -24.524 1.00 24.96  ? 526 PRO A N   1 
ATOM   2840 C CA  . PRO A 1 393 ? 31.295 28.233  -23.402 1.00 23.74  ? 526 PRO A CA  1 
ATOM   2841 C C   . PRO A 1 393 ? 32.123 27.504  -22.336 1.00 24.74  ? 526 PRO A C   1 
ATOM   2842 O O   . PRO A 1 393 ? 33.014 28.096  -21.728 1.00 22.92  ? 526 PRO A O   1 
ATOM   2843 C CB  . PRO A 1 393 ? 29.953 28.763  -22.880 1.00 25.39  ? 526 PRO A CB  1 
ATOM   2844 C CG  . PRO A 1 393 ? 28.979 27.707  -23.278 1.00 25.69  ? 526 PRO A CG  1 
ATOM   2845 C CD  . PRO A 1 393 ? 29.439 27.323  -24.666 1.00 25.12  ? 526 PRO A CD  1 
ATOM   2846 N N   . LEU A 1 394 ? 31.830 26.226  -22.106 1.00 22.77  ? 527 LEU A N   1 
ATOM   2847 C CA  . LEU A 1 394 ? 32.606 25.460  -21.137 1.00 22.68  ? 527 LEU A CA  1 
ATOM   2848 C C   . LEU A 1 394 ? 34.028 25.362  -21.672 1.00 21.66  ? 527 LEU A C   1 
ATOM   2849 O O   . LEU A 1 394 ? 34.996 25.548  -20.933 1.00 22.07  ? 527 LEU A O   1 
ATOM   2850 C CB  . LEU A 1 394 ? 32.018 24.056  -20.940 1.00 20.72  ? 527 LEU A CB  1 
ATOM   2851 C CG  . LEU A 1 394 ? 30.869 23.984  -19.927 1.00 22.39  ? 527 LEU A CG  1 
ATOM   2852 C CD1 . LEU A 1 394 ? 30.251 22.584  -19.922 1.00 20.27  ? 527 LEU A CD1 1 
ATOM   2853 C CD2 . LEU A 1 394 ? 31.397 24.350  -18.546 1.00 20.80  ? 527 LEU A CD2 1 
ATOM   2854 N N   . ARG A 1 395 ? 34.149 25.078  -22.965 1.00 20.46  ? 528 ARG A N   1 
ATOM   2855 C CA  . ARG A 1 395 ? 35.462 24.980  -23.592 1.00 21.34  ? 528 ARG A CA  1 
ATOM   2856 C C   . ARG A 1 395 ? 36.197 26.315  -23.441 1.00 24.33  ? 528 ARG A C   1 
ATOM   2857 O O   . ARG A 1 395 ? 37.338 26.365  -22.984 1.00 22.57  ? 528 ARG A O   1 
ATOM   2858 C CB  . ARG A 1 395 ? 35.329 24.645  -25.085 1.00 20.15  ? 528 ARG A CB  1 
ATOM   2859 C CG  . ARG A 1 395 ? 36.667 24.686  -25.825 1.00 20.55  ? 528 ARG A CG  1 
ATOM   2860 C CD  . ARG A 1 395 ? 36.567 24.258  -27.280 1.00 21.03  ? 528 ARG A CD  1 
ATOM   2861 N NE  . ARG A 1 395 ? 35.847 25.228  -28.102 1.00 24.95  ? 528 ARG A NE  1 
ATOM   2862 C CZ  . ARG A 1 395 ? 34.600 25.076  -28.532 1.00 28.52  ? 528 ARG A CZ  1 
ATOM   2863 N NH1 . ARG A 1 395 ? 33.913 23.980  -28.223 1.00 26.97  ? 528 ARG A NH1 1 
ATOM   2864 N NH2 . ARG A 1 395 ? 34.036 26.026  -29.270 1.00 29.58  ? 528 ARG A NH2 1 
ATOM   2865 N N   . GLU A 1 396 ? 35.521 27.396  -23.817 1.00 24.59  ? 529 GLU A N   1 
ATOM   2866 C CA  . GLU A 1 396 ? 36.099 28.734  -23.757 1.00 27.94  ? 529 GLU A CA  1 
ATOM   2867 C C   . GLU A 1 396 ? 36.524 29.175  -22.354 1.00 28.78  ? 529 GLU A C   1 
ATOM   2868 O O   . GLU A 1 396 ? 37.334 30.089  -22.210 1.00 29.74  ? 529 GLU A O   1 
ATOM   2869 C CB  . GLU A 1 396 ? 35.113 29.728  -24.394 1.00 31.49  ? 529 GLU A CB  1 
ATOM   2870 C CG  . GLU A 1 396 ? 34.783 29.332  -25.840 1.00 37.12  ? 529 GLU A CG  1 
ATOM   2871 C CD  . GLU A 1 396 ? 33.663 30.142  -26.475 1.00 43.16  ? 529 GLU A CD  1 
ATOM   2872 O OE1 . GLU A 1 396 ? 32.567 30.248  -25.874 1.00 46.09  ? 529 GLU A OE1 1 
ATOM   2873 O OE2 . GLU A 1 396 ? 33.875 30.657  -27.595 1.00 45.15  ? 529 GLU A OE2 1 
ATOM   2874 N N   . GLN A 1 397 ? 35.995 28.522  -21.321 1.00 27.99  ? 530 GLN A N   1 
ATOM   2875 C CA  . GLN A 1 397 ? 36.368 28.858  -19.947 1.00 27.33  ? 530 GLN A CA  1 
ATOM   2876 C C   . GLN A 1 397 ? 37.611 28.078  -19.504 1.00 25.08  ? 530 GLN A C   1 
ATOM   2877 O O   . GLN A 1 397 ? 38.057 28.195  -18.363 1.00 24.91  ? 530 GLN A O   1 
ATOM   2878 C CB  . GLN A 1 397 ? 35.212 28.570  -18.980 1.00 27.35  ? 530 GLN A CB  1 
ATOM   2879 C CG  . GLN A 1 397 ? 34.070 29.566  -19.047 1.00 28.63  ? 530 GLN A CG  1 
ATOM   2880 C CD  . GLN A 1 397 ? 34.538 31.004  -18.875 1.00 30.41  ? 530 GLN A CD  1 
ATOM   2881 O OE1 . GLN A 1 397 ? 35.241 31.334  -17.920 1.00 30.29  ? 530 GLN A OE1 1 
ATOM   2882 N NE2 . GLN A 1 397 ? 34.144 31.867  -19.804 1.00 32.09  ? 530 GLN A NE2 1 
ATOM   2883 N N   . GLY A 1 398 ? 38.162 27.279  -20.412 1.00 24.77  ? 531 GLY A N   1 
ATOM   2884 C CA  . GLY A 1 398 ? 39.358 26.511  -20.101 1.00 24.67  ? 531 GLY A CA  1 
ATOM   2885 C C   . GLY A 1 398 ? 39.137 25.256  -19.278 1.00 24.67  ? 531 GLY A C   1 
ATOM   2886 O O   . GLY A 1 398 ? 40.071 24.735  -18.665 1.00 26.83  ? 531 GLY A O   1 
ATOM   2887 N N   . ALA A 1 399 ? 37.914 24.745  -19.280 1.00 23.80  ? 532 ALA A N   1 
ATOM   2888 C CA  . ALA A 1 399 ? 37.593 23.553  -18.503 1.00 22.79  ? 532 ALA A CA  1 
ATOM   2889 C C   . ALA A 1 399 ? 38.355 22.288  -18.909 1.00 21.38  ? 532 ALA A C   1 
ATOM   2890 O O   . ALA A 1 399 ? 38.779 21.510  -18.057 1.00 21.17  ? 532 ALA A O   1 
ATOM   2891 C CB  . ALA A 1 399 ? 36.092 23.287  -18.575 1.00 22.52  ? 532 ALA A CB  1 
ATOM   2892 N N   . ILE A 1 400 ? 38.538 22.091  -20.207 1.00 21.18  ? 533 ILE A N   1 
ATOM   2893 C CA  . ILE A 1 400 ? 39.188 20.887  -20.703 1.00 21.51  ? 533 ILE A CA  1 
ATOM   2894 C C   . ILE A 1 400 ? 40.633 20.640  -20.257 1.00 22.13  ? 533 ILE A C   1 
ATOM   2895 O O   . ILE A 1 400 ? 40.958 19.542  -19.809 1.00 21.56  ? 533 ILE A O   1 
ATOM   2896 C CB  . ILE A 1 400 ? 39.065 20.814  -22.241 1.00 21.61  ? 533 ILE A CB  1 
ATOM   2897 C CG1 . ILE A 1 400 ? 37.578 20.923  -22.623 1.00 20.93  ? 533 ILE A CG1 1 
ATOM   2898 C CG2 . ILE A 1 400 ? 39.640 19.486  -22.758 1.00 19.55  ? 533 ILE A CG2 1 
ATOM   2899 C CD1 . ILE A 1 400 ? 37.290 20.846  -24.116 1.00 22.22  ? 533 ILE A CD1 1 
ATOM   2900 N N   . PRO A 1 401 ? 41.521 21.642  -20.373 1.00 21.58  ? 534 PRO A N   1 
ATOM   2901 C CA  . PRO A 1 401 ? 42.889 21.352  -19.923 1.00 21.46  ? 534 PRO A CA  1 
ATOM   2902 C C   . PRO A 1 401 ? 42.916 21.073  -18.416 1.00 19.66  ? 534 PRO A C   1 
ATOM   2903 O O   . PRO A 1 401 ? 43.657 20.216  -17.945 1.00 21.58  ? 534 PRO A O   1 
ATOM   2904 C CB  . PRO A 1 401 ? 43.656 22.627  -20.287 1.00 23.04  ? 534 PRO A CB  1 
ATOM   2905 C CG  . PRO A 1 401 ? 42.905 23.139  -21.503 1.00 23.77  ? 534 PRO A CG  1 
ATOM   2906 C CD  . PRO A 1 401 ? 41.457 22.925  -21.096 1.00 22.49  ? 534 PRO A CD  1 
ATOM   2907 N N   . ARG A 1 402 ? 42.103 21.800  -17.660 1.00 18.77  ? 535 ARG A N   1 
ATOM   2908 C CA  . ARG A 1 402 ? 42.063 21.611  -16.213 1.00 20.35  ? 535 ARG A CA  1 
ATOM   2909 C C   . ARG A 1 402 ? 41.508 20.223  -15.845 1.00 19.06  ? 535 ARG A C   1 
ATOM   2910 O O   . ARG A 1 402 ? 42.045 19.548  -14.970 1.00 20.77  ? 535 ARG A O   1 
ATOM   2911 C CB  . ARG A 1 402 ? 41.234 22.722  -15.557 1.00 18.15  ? 535 ARG A CB  1 
ATOM   2912 C CG  . ARG A 1 402 ? 41.112 22.607  -14.040 1.00 20.28  ? 535 ARG A CG  1 
ATOM   2913 C CD  . ARG A 1 402 ? 42.467 22.439  -13.355 1.00 20.22  ? 535 ARG A CD  1 
ATOM   2914 N NE  . ARG A 1 402 ? 42.329 22.439  -11.900 1.00 23.07  ? 535 ARG A NE  1 
ATOM   2915 C CZ  . ARG A 1 402 ? 43.298 22.104  -11.049 1.00 23.46  ? 535 ARG A CZ  1 
ATOM   2916 N NH1 . ARG A 1 402 ? 44.488 21.739  -11.502 1.00 22.63  ? 535 ARG A NH1 1 
ATOM   2917 N NH2 . ARG A 1 402 ? 43.068 22.116  -9.744  1.00 23.57  ? 535 ARG A NH2 1 
ATOM   2918 N N   . LEU A 1 403 ? 40.446 19.792  -16.515 1.00 18.13  ? 536 LEU A N   1 
ATOM   2919 C CA  . LEU A 1 403 ? 39.883 18.468  -16.247 1.00 18.34  ? 536 LEU A CA  1 
ATOM   2920 C C   . LEU A 1 403 ? 40.938 17.395  -16.555 1.00 20.42  ? 536 LEU A C   1 
ATOM   2921 O O   . LEU A 1 403 ? 41.078 16.415  -15.819 1.00 18.83  ? 536 LEU A O   1 
ATOM   2922 C CB  . LEU A 1 403 ? 38.638 18.233  -17.115 1.00 17.56  ? 536 LEU A CB  1 
ATOM   2923 C CG  . LEU A 1 403 ? 37.379 19.012  -16.725 1.00 19.26  ? 536 LEU A CG  1 
ATOM   2924 C CD1 . LEU A 1 403 ? 36.274 18.814  -17.768 1.00 20.02  ? 536 LEU A CD1 1 
ATOM   2925 C CD2 . LEU A 1 403 ? 36.913 18.532  -15.359 1.00 17.45  ? 536 LEU A CD2 1 
ATOM   2926 N N   . VAL A 1 404 ? 41.684 17.596  -17.640 1.00 19.44  ? 537 VAL A N   1 
ATOM   2927 C CA  . VAL A 1 404 ? 42.722 16.649  -18.049 1.00 22.80  ? 537 VAL A CA  1 
ATOM   2928 C C   . VAL A 1 404 ? 43.857 16.614  -17.024 1.00 22.79  ? 537 VAL A C   1 
ATOM   2929 O O   . VAL A 1 404 ? 44.354 15.543  -16.676 1.00 24.76  ? 537 VAL A O   1 
ATOM   2930 C CB  . VAL A 1 404 ? 43.280 17.010  -19.459 1.00 22.89  ? 537 VAL A CB  1 
ATOM   2931 C CG1 . VAL A 1 404 ? 44.498 16.152  -19.795 1.00 21.38  ? 537 VAL A CG1 1 
ATOM   2932 C CG2 . VAL A 1 404 ? 42.192 16.792  -20.506 1.00 20.94  ? 537 VAL A CG2 1 
ATOM   2933 N N   . GLN A 1 405 ? 44.256 17.786  -16.539 1.00 21.15  ? 538 GLN A N   1 
ATOM   2934 C CA  . GLN A 1 405 ? 45.316 17.871  -15.543 1.00 22.59  ? 538 GLN A CA  1 
ATOM   2935 C C   . GLN A 1 405 ? 44.909 17.149  -14.256 1.00 22.76  ? 538 GLN A C   1 
ATOM   2936 O O   . GLN A 1 405 ? 45.699 16.399  -13.683 1.00 22.27  ? 538 GLN A O   1 
ATOM   2937 C CB  . GLN A 1 405 ? 45.625 19.330  -15.226 1.00 21.78  ? 538 GLN A CB  1 
ATOM   2938 C CG  . GLN A 1 405 ? 46.615 19.507  -14.088 1.00 23.21  ? 538 GLN A CG  1 
ATOM   2939 C CD  . GLN A 1 405 ? 46.970 20.961  -13.870 1.00 24.10  ? 538 GLN A CD  1 
ATOM   2940 O OE1 . GLN A 1 405 ? 46.091 21.807  -13.719 1.00 24.72  ? 538 GLN A OE1 1 
ATOM   2941 N NE2 . GLN A 1 405 ? 48.264 21.260  -13.853 1.00 20.51  ? 538 GLN A NE2 1 
ATOM   2942 N N   . LEU A 1 406 ? 43.680 17.395  -13.802 1.00 22.33  ? 539 LEU A N   1 
ATOM   2943 C CA  . LEU A 1 406 ? 43.154 16.757  -12.595 1.00 22.24  ? 539 LEU A CA  1 
ATOM   2944 C C   . LEU A 1 406 ? 43.116 15.242  -12.779 1.00 22.83  ? 539 LEU A C   1 
ATOM   2945 O O   . LEU A 1 406 ? 43.471 14.481  -11.875 1.00 22.47  ? 539 LEU A O   1 
ATOM   2946 C CB  . LEU A 1 406 ? 41.739 17.271  -12.288 1.00 20.96  ? 539 LEU A CB  1 
ATOM   2947 C CG  . LEU A 1 406 ? 41.627 18.683  -11.696 1.00 23.23  ? 539 LEU A CG  1 
ATOM   2948 C CD1 . LEU A 1 406 ? 40.167 19.136  -11.672 1.00 22.01  ? 539 LEU A CD1 1 
ATOM   2949 C CD2 . LEU A 1 406 ? 42.222 18.680  -10.281 1.00 20.76  ? 539 LEU A CD2 1 
ATOM   2950 N N   . LEU A 1 407 ? 42.684 14.813  -13.961 1.00 22.75  ? 540 LEU A N   1 
ATOM   2951 C CA  . LEU A 1 407 ? 42.598 13.397  -14.285 1.00 23.35  ? 540 LEU A CA  1 
ATOM   2952 C C   . LEU A 1 407 ? 43.965 12.717  -14.235 1.00 23.68  ? 540 LEU A C   1 
ATOM   2953 O O   . LEU A 1 407 ? 44.109 11.651  -13.636 1.00 22.92  ? 540 LEU A O   1 
ATOM   2954 C CB  . LEU A 1 407 ? 42.001 13.212  -15.684 1.00 22.45  ? 540 LEU A CB  1 
ATOM   2955 C CG  . LEU A 1 407 ? 42.108 11.802  -16.277 1.00 26.38  ? 540 LEU A CG  1 
ATOM   2956 C CD1 . LEU A 1 407 ? 41.424 10.801  -15.340 1.00 26.40  ? 540 LEU A CD1 1 
ATOM   2957 C CD2 . LEU A 1 407 ? 41.475 11.772  -17.671 1.00 24.44  ? 540 LEU A CD2 1 
ATOM   2958 N N   . VAL A 1 408 ? 44.956 13.337  -14.872 1.00 23.34  ? 541 VAL A N   1 
ATOM   2959 C CA  . VAL A 1 408 ? 46.306 12.787  -14.919 1.00 23.57  ? 541 VAL A CA  1 
ATOM   2960 C C   . VAL A 1 408 ? 46.916 12.671  -13.530 1.00 25.37  ? 541 VAL A C   1 
ATOM   2961 O O   . VAL A 1 408 ? 47.449 11.622  -13.176 1.00 24.19  ? 541 VAL A O   1 
ATOM   2962 C CB  . VAL A 1 408 ? 47.232 13.649  -15.822 1.00 26.40  ? 541 VAL A CB  1 
ATOM   2963 C CG1 . VAL A 1 408 ? 48.687 13.201  -15.685 1.00 23.42  ? 541 VAL A CG1 1 
ATOM   2964 C CG2 . VAL A 1 408 ? 46.788 13.525  -17.276 1.00 23.91  ? 541 VAL A CG2 1 
ATOM   2965 N N   . ARG A 1 409 ? 46.834 13.740  -12.739 1.00 27.19  ? 542 ARG A N   1 
ATOM   2966 C CA  . ARG A 1 409 ? 47.392 13.710  -11.389 1.00 29.85  ? 542 ARG A CA  1 
ATOM   2967 C C   . ARG A 1 409 ? 46.696 12.682  -10.499 1.00 30.26  ? 542 ARG A C   1 
ATOM   2968 O O   . ARG A 1 409 ? 47.356 11.948  -9.766  1.00 31.88  ? 542 ARG A O   1 
ATOM   2969 C CB  . ARG A 1 409 ? 47.321 15.098  -10.743 1.00 29.99  ? 542 ARG A CB  1 
ATOM   2970 C CG  . ARG A 1 409 ? 48.162 16.152  -11.467 1.00 33.66  ? 542 ARG A CG  1 
ATOM   2971 C CD  . ARG A 1 409 ? 49.580 15.638  -11.705 1.00 37.99  ? 542 ARG A CD  1 
ATOM   2972 N NE  . ARG A 1 409 ? 50.440 16.608  -12.377 1.00 40.50  ? 542 ARG A NE  1 
ATOM   2973 C CZ  . ARG A 1 409 ? 51.660 16.329  -12.829 1.00 43.17  ? 542 ARG A CZ  1 
ATOM   2974 N NH1 . ARG A 1 409 ? 52.161 15.108  -12.679 1.00 43.38  ? 542 ARG A NH1 1 
ATOM   2975 N NH2 . ARG A 1 409 ? 52.380 17.265  -13.435 1.00 43.39  ? 542 ARG A NH2 1 
ATOM   2976 N N   . ALA A 1 410 ? 45.371 12.619  -10.569 1.00 29.65  ? 543 ALA A N   1 
ATOM   2977 C CA  . ALA A 1 410 ? 44.619 11.666  -9.754  1.00 29.87  ? 543 ALA A CA  1 
ATOM   2978 C C   . ALA A 1 410 ? 44.950 10.223  -10.140 1.00 30.41  ? 543 ALA A C   1 
ATOM   2979 O O   . ALA A 1 410 ? 45.033 9.343   -9.277  1.00 29.28  ? 543 ALA A O   1 
ATOM   2980 C CB  . ALA A 1 410 ? 43.123 11.915  -9.901  1.00 28.74  ? 543 ALA A CB  1 
ATOM   2981 N N   . HIS A 1 411 ? 45.142 9.984   -11.435 1.00 29.85  ? 544 HIS A N   1 
ATOM   2982 C CA  . HIS A 1 411 ? 45.466 8.645   -11.918 1.00 31.04  ? 544 HIS A CA  1 
ATOM   2983 C C   . HIS A 1 411 ? 46.842 8.214   -11.404 1.00 32.58  ? 544 HIS A C   1 
ATOM   2984 O O   . HIS A 1 411 ? 47.011 7.086   -10.931 1.00 30.46  ? 544 HIS A O   1 
ATOM   2985 C CB  . HIS A 1 411 ? 45.441 8.603   -13.451 1.00 30.22  ? 544 HIS A CB  1 
ATOM   2986 C CG  . HIS A 1 411 ? 45.868 7.287   -14.025 1.00 31.26  ? 544 HIS A CG  1 
ATOM   2987 N ND1 . HIS A 1 411 ? 45.221 6.103   -13.737 1.00 33.54  ? 544 HIS A ND1 1 
ATOM   2988 C CD2 . HIS A 1 411 ? 46.883 6.965   -14.861 1.00 31.46  ? 544 HIS A CD2 1 
ATOM   2989 C CE1 . HIS A 1 411 ? 45.820 5.110   -14.370 1.00 31.45  ? 544 HIS A CE1 1 
ATOM   2990 N NE2 . HIS A 1 411 ? 46.832 5.607   -15.060 1.00 30.43  ? 544 HIS A NE2 1 
ATOM   2991 N N   . GLN A 1 412 ? 47.821 9.110   -11.499 1.00 32.63  ? 545 GLN A N   1 
ATOM   2992 C CA  . GLN A 1 412 ? 49.165 8.805   -11.020 1.00 36.04  ? 545 GLN A CA  1 
ATOM   2993 C C   . GLN A 1 412 ? 49.104 8.485   -9.527  1.00 37.30  ? 545 GLN A C   1 
ATOM   2994 O O   . GLN A 1 412 ? 49.782 7.575   -9.050  1.00 38.44  ? 545 GLN A O   1 
ATOM   2995 C CB  . GLN A 1 412 ? 50.105 9.989   -11.269 1.00 34.03  ? 545 GLN A CB  1 
ATOM   2996 C CG  . GLN A 1 412 ? 50.210 10.376  -12.731 1.00 34.93  ? 545 GLN A CG  1 
ATOM   2997 C CD  . GLN A 1 412 ? 51.051 11.616  -12.955 1.00 35.96  ? 545 GLN A CD  1 
ATOM   2998 O OE1 . GLN A 1 412 ? 50.976 12.579  -12.191 1.00 37.39  ? 545 GLN A OE1 1 
ATOM   2999 N NE2 . GLN A 1 412 ? 51.846 11.606  -14.016 1.00 37.68  ? 545 GLN A NE2 1 
ATOM   3000 N N   . ASP A 1 413 ? 48.277 9.224   -8.794  1.00 38.21  ? 546 ASP A N   1 
ATOM   3001 C CA  . ASP A 1 413 ? 48.136 8.990   -7.363  1.00 40.78  ? 546 ASP A CA  1 
ATOM   3002 C C   . ASP A 1 413 ? 47.591 7.592   -7.077  1.00 42.50  ? 546 ASP A C   1 
ATOM   3003 O O   . ASP A 1 413 ? 47.973 6.970   -6.086  1.00 43.68  ? 546 ASP A O   1 
ATOM   3004 C CB  . ASP A 1 413 ? 47.216 10.041  -6.733  1.00 44.34  ? 546 ASP A CB  1 
ATOM   3005 C CG  . ASP A 1 413 ? 47.832 11.433  -6.724  1.00 48.07  ? 546 ASP A CG  1 
ATOM   3006 O OD1 . ASP A 1 413 ? 47.166 12.377  -6.247  1.00 50.81  ? 546 ASP A OD1 1 
ATOM   3007 O OD2 . ASP A 1 413 ? 48.981 11.591  -7.192  1.00 51.13  ? 546 ASP A OD2 1 
ATOM   3008 N N   . THR A 1 414 ? 46.708 7.092   -7.939  1.00 42.48  ? 547 THR A N   1 
ATOM   3009 C CA  . THR A 1 414 ? 46.135 5.762   -7.737  1.00 44.25  ? 547 THR A CA  1 
ATOM   3010 C C   . THR A 1 414 ? 47.120 4.651   -8.085  1.00 46.48  ? 547 THR A C   1 
ATOM   3011 O O   . THR A 1 414 ? 46.954 3.514   -7.646  1.00 46.24  ? 547 THR A O   1 
ATOM   3012 C CB  . THR A 1 414 ? 44.869 5.530   -8.593  1.00 43.09  ? 547 THR A CB  1 
ATOM   3013 O OG1 . THR A 1 414 ? 45.235 5.455   -9.975  1.00 40.48  ? 547 THR A OG1 1 
ATOM   3014 C CG2 . THR A 1 414 ? 43.863 6.657   -8.395  1.00 44.76  ? 547 THR A CG2 1 
ATOM   3015 N N   . GLN A 1 415 ? 48.140 4.974   -8.874  1.00 49.03  ? 548 GLN A N   1 
ATOM   3016 C CA  . GLN A 1 415 ? 49.125 3.976   -9.276  1.00 51.99  ? 548 GLN A CA  1 
ATOM   3017 C C   . GLN A 1 415 ? 50.297 3.867   -8.308  1.00 53.90  ? 548 GLN A C   1 
ATOM   3018 O O   . GLN A 1 415 ? 50.886 2.797   -8.164  1.00 54.53  ? 548 GLN A O   1 
ATOM   3019 C CB  . GLN A 1 415 ? 49.651 4.281   -10.682 1.00 51.36  ? 548 GLN A CB  1 
ATOM   3020 C CG  . GLN A 1 415 ? 48.572 4.358   -11.750 1.00 54.17  ? 548 GLN A CG  1 
ATOM   3021 C CD  . GLN A 1 415 ? 47.752 3.083   -11.861 1.00 55.39  ? 548 GLN A CD  1 
ATOM   3022 O OE1 . GLN A 1 415 ? 48.255 2.036   -12.272 1.00 56.62  ? 548 GLN A OE1 1 
ATOM   3023 N NE2 . GLN A 1 415 ? 46.479 3.168   -11.491 1.00 55.42  ? 548 GLN A NE2 1 
ATOM   3024 N N   . ARG A 1 416 ? 50.641 4.968   -7.646  1.00 56.48  ? 549 ARG A N   1 
ATOM   3025 C CA  . ARG A 1 416 ? 51.753 4.946   -6.701  1.00 58.78  ? 549 ARG A CA  1 
ATOM   3026 C C   . ARG A 1 416 ? 51.282 4.471   -5.331  1.00 58.97  ? 549 ARG A C   1 
ATOM   3027 O O   . ARG A 1 416 ? 51.332 3.280   -5.027  1.00 59.79  ? 549 ARG A O   1 
ATOM   3028 C CB  . ARG A 1 416 ? 52.386 6.334   -6.565  1.00 59.86  ? 549 ARG A CB  1 
ATOM   3029 C CG  . ARG A 1 416 ? 51.572 7.318   -5.743  1.00 62.76  ? 549 ARG A CG  1 
ATOM   3030 C CD  . ARG A 1 416 ? 52.424 8.502   -5.313  1.00 64.31  ? 549 ARG A CD  1 
ATOM   3031 N NE  . ARG A 1 416 ? 52.955 9.247   -6.451  1.00 66.72  ? 549 ARG A NE  1 
ATOM   3032 C CZ  . ARG A 1 416 ? 52.209 9.949   -7.297  1.00 67.28  ? 549 ARG A CZ  1 
ATOM   3033 N NH1 . ARG A 1 416 ? 50.896 10.003  -7.134  1.00 67.43  ? 549 ARG A NH1 1 
ATOM   3034 N NH2 . ARG A 1 416 ? 52.774 10.599  -8.307  1.00 67.54  ? 549 ARG A NH2 1 
ATOM   3035 N N   . GLN A 1 426 ? 45.146 6.623   0.034   1.00 83.35  ? 559 GLN A N   1 
ATOM   3036 C CA  . GLN A 1 426 ? 43.771 6.296   -0.326  1.00 83.32  ? 559 GLN A CA  1 
ATOM   3037 C C   . GLN A 1 426 ? 42.867 7.526   -0.268  1.00 82.62  ? 559 GLN A C   1 
ATOM   3038 O O   . GLN A 1 426 ? 42.521 8.109   -1.297  1.00 83.30  ? 559 GLN A O   1 
ATOM   3039 C CB  . GLN A 1 426 ? 43.222 5.218   0.612   1.00 83.73  ? 559 GLN A CB  1 
ATOM   3040 C CG  . GLN A 1 426 ? 41.759 4.878   0.371   1.00 85.13  ? 559 GLN A CG  1 
ATOM   3041 C CD  . GLN A 1 426 ? 41.219 3.878   1.373   1.00 85.85  ? 559 GLN A CD  1 
ATOM   3042 O OE1 . GLN A 1 426 ? 41.253 4.115   2.581   1.00 86.37  ? 559 GLN A OE1 1 
ATOM   3043 N NE2 . GLN A 1 426 ? 40.715 2.754   0.877   1.00 86.38  ? 559 GLN A NE2 1 
ATOM   3044 N N   . PHE A 1 427 ? 42.485 7.912   0.945   1.00 81.05  ? 560 PHE A N   1 
ATOM   3045 C CA  . PHE A 1 427 ? 41.617 9.063   1.147   1.00 79.35  ? 560 PHE A CA  1 
ATOM   3046 C C   . PHE A 1 427 ? 42.385 10.367  1.296   1.00 77.37  ? 560 PHE A C   1 
ATOM   3047 O O   . PHE A 1 427 ? 43.283 10.481  2.128   1.00 77.52  ? 560 PHE A O   1 
ATOM   3048 C CB  . PHE A 1 427 ? 40.747 8.850   2.387   1.00 80.85  ? 560 PHE A CB  1 
ATOM   3049 C CG  . PHE A 1 427 ? 39.593 7.918   2.164   1.00 82.42  ? 560 PHE A CG  1 
ATOM   3050 C CD1 . PHE A 1 427 ? 38.486 8.327   1.427   1.00 83.18  ? 560 PHE A CD1 1 
ATOM   3051 C CD2 . PHE A 1 427 ? 39.608 6.632   2.692   1.00 83.05  ? 560 PHE A CD2 1 
ATOM   3052 C CE1 . PHE A 1 427 ? 37.411 7.466   1.214   1.00 83.69  ? 560 PHE A CE1 1 
ATOM   3053 C CE2 . PHE A 1 427 ? 38.538 5.762   2.484   1.00 83.40  ? 560 PHE A CE2 1 
ATOM   3054 C CZ  . PHE A 1 427 ? 37.437 6.181   1.746   1.00 83.31  ? 560 PHE A CZ  1 
ATOM   3055 N N   . VAL A 1 428 ? 42.023 11.348  0.479   1.00 74.34  ? 561 VAL A N   1 
ATOM   3056 C CA  . VAL A 1 428 ? 42.650 12.660  0.531   1.00 71.43  ? 561 VAL A CA  1 
ATOM   3057 C C   . VAL A 1 428 ? 41.539 13.658  0.824   1.00 69.16  ? 561 VAL A C   1 
ATOM   3058 O O   . VAL A 1 428 ? 40.698 13.930  -0.033  1.00 69.03  ? 561 VAL A O   1 
ATOM   3059 C CB  . VAL A 1 428 ? 43.326 13.021  -0.809  1.00 71.36  ? 561 VAL A CB  1 
ATOM   3060 C CG1 . VAL A 1 428 ? 44.026 14.366  -0.692  1.00 70.71  ? 561 VAL A CG1 1 
ATOM   3061 C CG2 . VAL A 1 428 ? 44.322 11.938  -1.194  1.00 71.47  ? 561 VAL A CG2 1 
ATOM   3062 N N   . GLU A 1 429 ? 41.534 14.191  2.042   1.00 66.42  ? 562 GLU A N   1 
ATOM   3063 C CA  . GLU A 1 429 ? 40.509 15.139  2.462   1.00 63.41  ? 562 GLU A CA  1 
ATOM   3064 C C   . GLU A 1 429 ? 39.135 14.482  2.370   1.00 61.12  ? 562 GLU A C   1 
ATOM   3065 O O   . GLU A 1 429 ? 38.117 15.158  2.222   1.00 60.64  ? 562 GLU A O   1 
ATOM   3066 C CB  . GLU A 1 429 ? 40.552 16.402  1.594   1.00 63.73  ? 562 GLU A CB  1 
ATOM   3067 C CG  . GLU A 1 429 ? 41.797 17.256  1.804   1.00 64.07  ? 562 GLU A CG  1 
ATOM   3068 C CD  . GLU A 1 429 ? 41.812 18.504  0.940   1.00 64.41  ? 562 GLU A CD  1 
ATOM   3069 O OE1 . GLU A 1 429 ? 42.769 19.298  1.060   1.00 64.66  ? 562 GLU A OE1 1 
ATOM   3070 O OE2 . GLU A 1 429 ? 40.871 18.692  0.141   1.00 63.69  ? 562 GLU A OE2 1 
ATOM   3071 N N   . GLY A 1 430 ? 39.121 13.154  2.456   1.00 58.33  ? 563 GLY A N   1 
ATOM   3072 C CA  . GLY A 1 430 ? 37.873 12.413  2.396   1.00 55.13  ? 563 GLY A CA  1 
ATOM   3073 C C   . GLY A 1 430 ? 37.450 11.989  1.002   1.00 53.01  ? 563 GLY A C   1 
ATOM   3074 O O   . GLY A 1 430 ? 36.353 11.459  0.819   1.00 53.44  ? 563 GLY A O   1 
ATOM   3075 N N   . VAL A 1 431 ? 38.315 12.215  0.017   1.00 49.70  ? 564 VAL A N   1 
ATOM   3076 C CA  . VAL A 1 431 ? 38.009 11.851  -1.361  1.00 45.82  ? 564 VAL A CA  1 
ATOM   3077 C C   . VAL A 1 431 ? 39.071 10.930  -1.941  1.00 44.40  ? 564 VAL A C   1 
ATOM   3078 O O   . VAL A 1 431 ? 40.266 11.220  -1.870  1.00 44.53  ? 564 VAL A O   1 
ATOM   3079 C CB  . VAL A 1 431 ? 37.914 13.105  -2.268  1.00 44.51  ? 564 VAL A CB  1 
ATOM   3080 C CG1 . VAL A 1 431 ? 37.607 12.694  -3.701  1.00 43.48  ? 564 VAL A CG1 1 
ATOM   3081 C CG2 . VAL A 1 431 ? 36.842 14.044  -1.751  1.00 44.10  ? 564 VAL A CG2 1 
ATOM   3082 N N   . ARG A 1 432 ? 38.633 9.814   -2.512  1.00 42.89  ? 565 ARG A N   1 
ATOM   3083 C CA  . ARG A 1 432 ? 39.563 8.876   -3.129  1.00 42.42  ? 565 ARG A CA  1 
ATOM   3084 C C   . ARG A 1 432 ? 39.863 9.390   -4.534  1.00 39.99  ? 565 ARG A C   1 
ATOM   3085 O O   . ARG A 1 432 ? 38.967 9.863   -5.234  1.00 38.24  ? 565 ARG A O   1 
ATOM   3086 C CB  . ARG A 1 432 ? 38.948 7.476   -3.186  1.00 44.80  ? 565 ARG A CB  1 
ATOM   3087 C CG  . ARG A 1 432 ? 38.747 6.854   -1.812  1.00 50.00  ? 565 ARG A CG  1 
ATOM   3088 C CD  . ARG A 1 432 ? 38.002 5.526   -1.874  1.00 53.14  ? 565 ARG A CD  1 
ATOM   3089 N NE  . ARG A 1 432 ? 36.683 5.661   -2.488  1.00 55.46  ? 565 ARG A NE  1 
ATOM   3090 C CZ  . ARG A 1 432 ? 36.405 5.323   -3.744  1.00 57.83  ? 565 ARG A CZ  1 
ATOM   3091 N NH1 . ARG A 1 432 ? 37.355 4.824   -4.527  1.00 58.38  ? 565 ARG A NH1 1 
ATOM   3092 N NH2 . ARG A 1 432 ? 35.178 5.488   -4.221  1.00 58.10  ? 565 ARG A NH2 1 
ATOM   3093 N N   . MET A 1 433 ? 41.121 9.308   -4.945  1.00 38.02  ? 566 MET A N   1 
ATOM   3094 C CA  . MET A 1 433 ? 41.495 9.793   -6.259  1.00 37.66  ? 566 MET A CA  1 
ATOM   3095 C C   . MET A 1 433 ? 40.864 9.007   -7.402  1.00 37.06  ? 566 MET A C   1 
ATOM   3096 O O   . MET A 1 433 ? 40.847 9.476   -8.540  1.00 38.80  ? 566 MET A O   1 
ATOM   3097 C CB  . MET A 1 433 ? 43.015 9.828   -6.393  1.00 36.42  ? 566 MET A CB  1 
ATOM   3098 C CG  . MET A 1 433 ? 43.661 10.922  -5.544  1.00 35.08  ? 566 MET A CG  1 
ATOM   3099 S SD  . MET A 1 433 ? 43.009 12.589  -5.896  1.00 36.55  ? 566 MET A SD  1 
ATOM   3100 C CE  . MET A 1 433 ? 41.811 12.803  -4.593  1.00 35.66  ? 566 MET A CE  1 
ATOM   3101 N N   . GLU A 1 434 ? 40.337 7.822   -7.105  1.00 36.42  ? 567 GLU A N   1 
ATOM   3102 C CA  . GLU A 1 434 ? 39.681 7.020   -8.132  1.00 35.94  ? 567 GLU A CA  1 
ATOM   3103 C C   . GLU A 1 434 ? 38.385 7.740   -8.496  1.00 34.78  ? 567 GLU A C   1 
ATOM   3104 O O   . GLU A 1 434 ? 37.910 7.652   -9.632  1.00 33.13  ? 567 GLU A O   1 
ATOM   3105 C CB  . GLU A 1 434 ? 39.350 5.612   -7.617  1.00 39.92  ? 567 GLU A CB  1 
ATOM   3106 C CG  . GLU A 1 434 ? 40.531 4.863   -7.017  1.00 46.80  ? 567 GLU A CG  1 
ATOM   3107 C CD  . GLU A 1 434 ? 40.879 5.354   -5.622  1.00 49.48  ? 567 GLU A CD  1 
ATOM   3108 O OE1 . GLU A 1 434 ? 40.093 5.090   -4.687  1.00 53.46  ? 567 GLU A OE1 1 
ATOM   3109 O OE2 . GLU A 1 434 ? 41.931 6.009   -5.461  1.00 49.78  ? 567 GLU A OE2 1 
ATOM   3110 N N   . GLU A 1 435 ? 37.817 8.446   -7.519  1.00 31.80  ? 568 GLU A N   1 
ATOM   3111 C CA  . GLU A 1 435 ? 36.583 9.197   -7.725  1.00 32.31  ? 568 GLU A CA  1 
ATOM   3112 C C   . GLU A 1 435 ? 36.848 10.366  -8.666  1.00 29.99  ? 568 GLU A C   1 
ATOM   3113 O O   . GLU A 1 435 ? 35.994 10.727  -9.475  1.00 29.36  ? 568 GLU A O   1 
ATOM   3114 C CB  . GLU A 1 435 ? 36.042 9.740   -6.395  1.00 34.40  ? 568 GLU A CB  1 
ATOM   3115 C CG  . GLU A 1 435 ? 35.743 8.683   -5.340  1.00 38.98  ? 568 GLU A CG  1 
ATOM   3116 C CD  . GLU A 1 435 ? 35.201 9.291   -4.052  1.00 42.27  ? 568 GLU A CD  1 
ATOM   3117 O OE1 . GLU A 1 435 ? 34.052 9.786   -4.062  1.00 43.59  ? 568 GLU A OE1 1 
ATOM   3118 O OE2 . GLU A 1 435 ? 35.926 9.281   -3.032  1.00 44.67  ? 568 GLU A OE2 1 
ATOM   3119 N N   . ILE A 1 436 ? 38.030 10.963  -8.544  1.00 27.18  ? 569 ILE A N   1 
ATOM   3120 C CA  . ILE A 1 436 ? 38.404 12.083  -9.394  1.00 24.84  ? 569 ILE A CA  1 
ATOM   3121 C C   . ILE A 1 436 ? 38.664 11.577  -10.808 1.00 24.62  ? 569 ILE A C   1 
ATOM   3122 O O   . ILE A 1 436 ? 38.261 12.208  -11.788 1.00 25.35  ? 569 ILE A O   1 
ATOM   3123 C CB  . ILE A 1 436 ? 39.664 12.790  -8.861  1.00 24.51  ? 569 ILE A CB  1 
ATOM   3124 C CG1 . ILE A 1 436 ? 39.395 13.328  -7.451  1.00 25.94  ? 569 ILE A CG1 1 
ATOM   3125 C CG2 . ILE A 1 436 ? 40.067 13.918  -9.803  1.00 24.76  ? 569 ILE A CG2 1 
ATOM   3126 C CD1 . ILE A 1 436 ? 38.195 14.281  -7.361  1.00 25.88  ? 569 ILE A CD1 1 
ATOM   3127 N N   . VAL A 1 437 ? 39.331 10.431  -10.911 1.00 21.37  ? 570 VAL A N   1 
ATOM   3128 C CA  . VAL A 1 437 ? 39.611 9.841   -12.214 1.00 21.89  ? 570 VAL A CA  1 
ATOM   3129 C C   . VAL A 1 437 ? 38.293 9.577   -12.941 1.00 21.01  ? 570 VAL A C   1 
ATOM   3130 O O   . VAL A 1 437 ? 38.117 9.968   -14.098 1.00 21.12  ? 570 VAL A O   1 
ATOM   3131 C CB  . VAL A 1 437 ? 40.394 8.505   -12.078 1.00 20.68  ? 570 VAL A CB  1 
ATOM   3132 C CG1 . VAL A 1 437 ? 40.508 7.820   -13.438 1.00 21.43  ? 570 VAL A CG1 1 
ATOM   3133 C CG2 . VAL A 1 437 ? 41.785 8.779   -11.532 1.00 19.84  ? 570 VAL A CG2 1 
ATOM   3134 N N   . GLU A 1 438 ? 37.366 8.922   -12.249 1.00 21.80  ? 571 GLU A N   1 
ATOM   3135 C CA  . GLU A 1 438 ? 36.069 8.599   -12.822 1.00 22.74  ? 571 GLU A CA  1 
ATOM   3136 C C   . GLU A 1 438 ? 35.280 9.862   -13.174 1.00 22.45  ? 571 GLU A C   1 
ATOM   3137 O O   . GLU A 1 438 ? 34.698 9.951   -14.251 1.00 21.60  ? 571 GLU A O   1 
ATOM   3138 C CB  . GLU A 1 438 ? 35.250 7.758   -11.841 1.00 24.88  ? 571 GLU A CB  1 
ATOM   3139 C CG  . GLU A 1 438 ? 33.927 7.275   -12.411 1.00 29.46  ? 571 GLU A CG  1 
ATOM   3140 C CD  . GLU A 1 438 ? 33.052 6.612   -11.367 1.00 34.25  ? 571 GLU A CD  1 
ATOM   3141 O OE1 . GLU A 1 438 ? 33.595 5.880   -10.509 1.00 36.73  ? 571 GLU A OE1 1 
ATOM   3142 O OE2 . GLU A 1 438 ? 31.821 6.813   -11.411 1.00 36.26  ? 571 GLU A OE2 1 
ATOM   3143 N N   . GLY A 1 439 ? 35.253 10.828  -12.258 1.00 22.04  ? 572 GLY A N   1 
ATOM   3144 C CA  . GLY A 1 439 ? 34.519 12.060  -12.510 1.00 21.39  ? 572 GLY A CA  1 
ATOM   3145 C C   . GLY A 1 439 ? 35.032 12.871  -13.695 1.00 22.99  ? 572 GLY A C   1 
ATOM   3146 O O   . GLY A 1 439 ? 34.248 13.312  -14.539 1.00 23.15  ? 572 GLY A O   1 
ATOM   3147 N N   . CYS A 1 440 ? 36.344 13.073  -13.762 1.00 22.22  ? 573 CYS A N   1 
ATOM   3148 C CA  . CYS A 1 440 ? 36.942 13.838  -14.854 1.00 22.12  ? 573 CYS A CA  1 
ATOM   3149 C C   . CYS A 1 440 ? 36.787 13.137  -16.210 1.00 22.26  ? 573 CYS A C   1 
ATOM   3150 O O   . CYS A 1 440 ? 36.446 13.770  -17.209 1.00 20.30  ? 573 CYS A O   1 
ATOM   3151 C CB  . CYS A 1 440 ? 38.422 14.094  -14.565 1.00 23.31  ? 573 CYS A CB  1 
ATOM   3152 S SG  . CYS A 1 440 ? 38.745 15.231  -13.189 1.00 23.96  ? 573 CYS A SG  1 
ATOM   3153 N N   . THR A 1 441 ? 37.047 11.834  -16.255 1.00 21.65  ? 574 THR A N   1 
ATOM   3154 C CA  . THR A 1 441 ? 36.903 11.097  -17.506 1.00 20.48  ? 574 THR A CA  1 
ATOM   3155 C C   . THR A 1 441 ? 35.425 11.142  -17.912 1.00 19.12  ? 574 THR A C   1 
ATOM   3156 O O   . THR A 1 441 ? 35.092 11.224  -19.096 1.00 18.21  ? 574 THR A O   1 
ATOM   3157 C CB  . THR A 1 441 ? 37.369 9.627   -17.350 1.00 20.69  ? 574 THR A CB  1 
ATOM   3158 O OG1 . THR A 1 441 ? 38.719 9.610   -16.873 1.00 19.82  ? 574 THR A OG1 1 
ATOM   3159 C CG2 . THR A 1 441 ? 37.307 8.898   -18.680 1.00 18.10  ? 574 THR A CG2 1 
ATOM   3160 N N   . GLY A 1 442 ? 34.544 11.106  -16.917 1.00 19.26  ? 575 GLY A N   1 
ATOM   3161 C CA  . GLY A 1 442 ? 33.114 11.166  -17.191 1.00 19.73  ? 575 GLY A CA  1 
ATOM   3162 C C   . GLY A 1 442 ? 32.709 12.499  -17.812 1.00 20.05  ? 575 GLY A C   1 
ATOM   3163 O O   . GLY A 1 442 ? 31.910 12.538  -18.754 1.00 20.32  ? 575 GLY A O   1 
ATOM   3164 N N   . ALA A 1 443 ? 33.252 13.598  -17.295 1.00 18.18  ? 576 ALA A N   1 
ATOM   3165 C CA  . ALA A 1 443 ? 32.925 14.923  -17.838 1.00 19.47  ? 576 ALA A CA  1 
ATOM   3166 C C   . ALA A 1 443 ? 33.498 15.070  -19.248 1.00 19.47  ? 576 ALA A C   1 
ATOM   3167 O O   . ALA A 1 443 ? 32.854 15.629  -20.137 1.00 18.05  ? 576 ALA A O   1 
ATOM   3168 C CB  . ALA A 1 443 ? 33.477 16.024  -16.926 1.00 18.60  ? 576 ALA A CB  1 
ATOM   3169 N N   . LEU A 1 444 ? 34.710 14.563  -19.457 1.00 18.39  ? 577 LEU A N   1 
ATOM   3170 C CA  . LEU A 1 444 ? 35.340 14.652  -20.772 1.00 18.61  ? 577 LEU A CA  1 
ATOM   3171 C C   . LEU A 1 444 ? 34.535 13.823  -21.773 1.00 18.57  ? 577 LEU A C   1 
ATOM   3172 O O   . LEU A 1 444 ? 34.437 14.166  -22.951 1.00 20.13  ? 577 LEU A O   1 
ATOM   3173 C CB  . LEU A 1 444 ? 36.798 14.172  -20.693 1.00 17.41  ? 577 LEU A CB  1 
ATOM   3174 C CG  . LEU A 1 444 ? 37.735 15.118  -19.923 1.00 19.49  ? 577 LEU A CG  1 
ATOM   3175 C CD1 . LEU A 1 444 ? 39.079 14.457  -19.654 1.00 19.07  ? 577 LEU A CD1 1 
ATOM   3176 C CD2 . LEU A 1 444 ? 37.928 16.394  -20.728 1.00 19.61  ? 577 LEU A CD2 1 
ATOM   3177 N N   . HIS A 1 445 ? 33.952 12.730  -21.290 1.00 20.08  ? 578 HIS A N   1 
ATOM   3178 C CA  . HIS A 1 445 ? 33.120 11.865  -22.117 1.00 16.81  ? 578 HIS A CA  1 
ATOM   3179 C C   . HIS A 1 445 ? 31.942 12.660  -22.703 1.00 19.00  ? 578 HIS A C   1 
ATOM   3180 O O   . HIS A 1 445 ? 31.638 12.562  -23.898 1.00 19.66  ? 578 HIS A O   1 
ATOM   3181 C CB  . HIS A 1 445 ? 32.576 10.717  -21.268 1.00 18.26  ? 578 HIS A CB  1 
ATOM   3182 C CG  . HIS A 1 445 ? 31.671 9.788   -22.014 1.00 19.80  ? 578 HIS A CG  1 
ATOM   3183 N ND1 . HIS A 1 445 ? 30.779 8.951   -21.379 1.00 19.61  ? 578 HIS A ND1 1 
ATOM   3184 C CD2 . HIS A 1 445 ? 31.540 9.542   -23.338 1.00 19.25  ? 578 HIS A CD2 1 
ATOM   3185 C CE1 . HIS A 1 445 ? 30.138 8.229   -22.280 1.00 20.54  ? 578 HIS A CE1 1 
ATOM   3186 N NE2 . HIS A 1 445 ? 30.582 8.568   -23.477 1.00 20.01  ? 578 HIS A NE2 1 
ATOM   3187 N N   . ILE A 1 446 ? 31.277 13.451  -21.865 1.00 18.65  ? 579 ILE A N   1 
ATOM   3188 C CA  . ILE A 1 446 ? 30.135 14.231  -22.343 1.00 19.08  ? 579 ILE A CA  1 
ATOM   3189 C C   . ILE A 1 446 ? 30.608 15.381  -23.230 1.00 18.27  ? 579 ILE A C   1 
ATOM   3190 O O   . ILE A 1 446 ? 30.053 15.620  -24.301 1.00 21.11  ? 579 ILE A O   1 
ATOM   3191 C CB  . ILE A 1 446 ? 29.289 14.790  -21.161 1.00 16.71  ? 579 ILE A CB  1 
ATOM   3192 C CG1 . ILE A 1 446 ? 28.907 13.649  -20.205 1.00 18.34  ? 579 ILE A CG1 1 
ATOM   3193 C CG2 . ILE A 1 446 ? 28.010 15.450  -21.695 1.00 17.20  ? 579 ILE A CG2 1 
ATOM   3194 C CD1 . ILE A 1 446 ? 28.259 12.444  -20.892 1.00 20.77  ? 579 ILE A CD1 1 
ATOM   3195 N N   . LEU A 1 447 ? 31.646 16.083  -22.793 1.00 17.78  ? 580 LEU A N   1 
ATOM   3196 C CA  . LEU A 1 447 ? 32.181 17.197  -23.569 1.00 18.33  ? 580 LEU A CA  1 
ATOM   3197 C C   . LEU A 1 447 ? 32.643 16.749  -24.956 1.00 19.22  ? 580 LEU A C   1 
ATOM   3198 O O   . LEU A 1 447 ? 32.568 17.514  -25.920 1.00 19.51  ? 580 LEU A O   1 
ATOM   3199 C CB  . LEU A 1 447 ? 33.340 17.854  -22.805 1.00 17.05  ? 580 LEU A CB  1 
ATOM   3200 C CG  . LEU A 1 447 ? 32.889 18.679  -21.591 1.00 18.14  ? 580 LEU A CG  1 
ATOM   3201 C CD1 . LEU A 1 447 ? 34.061 18.963  -20.665 1.00 19.01  ? 580 LEU A CD1 1 
ATOM   3202 C CD2 . LEU A 1 447 ? 32.236 19.980  -22.084 1.00 16.76  ? 580 LEU A CD2 1 
ATOM   3203 N N   . ALA A 1 448 ? 33.108 15.506  -25.059 1.00 17.38  ? 581 ALA A N   1 
ATOM   3204 C CA  . ALA A 1 448 ? 33.577 14.977  -26.336 1.00 18.92  ? 581 ALA A CA  1 
ATOM   3205 C C   . ALA A 1 448 ? 32.463 14.835  -27.380 1.00 19.86  ? 581 ALA A C   1 
ATOM   3206 O O   . ALA A 1 448 ? 32.726 14.466  -28.521 1.00 19.69  ? 581 ALA A O   1 
ATOM   3207 C CB  . ALA A 1 448 ? 34.287 13.625  -26.121 1.00 17.04  ? 581 ALA A CB  1 
ATOM   3208 N N   . ARG A 1 449 ? 31.220 15.122  -27.003 1.00 21.43  ? 582 ARG A N   1 
ATOM   3209 C CA  . ARG A 1 449 ? 30.117 15.039  -27.964 1.00 21.56  ? 582 ARG A CA  1 
ATOM   3210 C C   . ARG A 1 449 ? 30.262 16.148  -29.007 1.00 20.11  ? 582 ARG A C   1 
ATOM   3211 O O   . ARG A 1 449 ? 29.688 16.083  -30.093 1.00 19.29  ? 582 ARG A O   1 
ATOM   3212 C CB  . ARG A 1 449 ? 28.767 15.195  -27.255 1.00 22.38  ? 582 ARG A CB  1 
ATOM   3213 C CG  . ARG A 1 449 ? 28.396 14.046  -26.338 1.00 21.55  ? 582 ARG A CG  1 
ATOM   3214 C CD  . ARG A 1 449 ? 27.109 14.352  -25.563 1.00 22.39  ? 582 ARG A CD  1 
ATOM   3215 N NE  . ARG A 1 449 ? 26.695 13.225  -24.733 1.00 19.72  ? 582 ARG A NE  1 
ATOM   3216 C CZ  . ARG A 1 449 ? 25.502 13.120  -24.156 1.00 21.10  ? 582 ARG A CZ  1 
ATOM   3217 N NH1 . ARG A 1 449 ? 24.595 14.078  -24.319 1.00 18.94  ? 582 ARG A NH1 1 
ATOM   3218 N NH2 . ARG A 1 449 ? 25.215 12.054  -23.420 1.00 17.93  ? 582 ARG A NH2 1 
ATOM   3219 N N   . ASP A 1 450 ? 31.034 17.172  -28.666 1.00 21.20  ? 583 ASP A N   1 
ATOM   3220 C CA  . ASP A 1 450 ? 31.251 18.300  -29.562 1.00 22.04  ? 583 ASP A CA  1 
ATOM   3221 C C   . ASP A 1 450 ? 32.553 18.144  -30.344 1.00 20.47  ? 583 ASP A C   1 
ATOM   3222 O O   . ASP A 1 450 ? 33.602 17.881  -29.762 1.00 18.78  ? 583 ASP A O   1 
ATOM   3223 C CB  . ASP A 1 450 ? 31.283 19.599  -28.758 1.00 21.73  ? 583 ASP A CB  1 
ATOM   3224 C CG  . ASP A 1 450 ? 31.571 20.798  -29.625 1.00 23.91  ? 583 ASP A CG  1 
ATOM   3225 O OD1 . ASP A 1 450 ? 32.753 21.190  -29.732 1.00 24.35  ? 583 ASP A OD1 1 
ATOM   3226 O OD2 . ASP A 1 450 ? 30.612 21.336  -30.212 1.00 25.28  ? 583 ASP A OD2 1 
ATOM   3227 N N   . VAL A 1 451 ? 32.482 18.322  -31.659 1.00 21.25  ? 584 VAL A N   1 
ATOM   3228 C CA  . VAL A 1 451 ? 33.656 18.168  -32.516 1.00 22.24  ? 584 VAL A CA  1 
ATOM   3229 C C   . VAL A 1 451 ? 34.832 19.073  -32.144 1.00 23.00  ? 584 VAL A C   1 
ATOM   3230 O O   . VAL A 1 451 ? 35.977 18.633  -32.169 1.00 24.57  ? 584 VAL A O   1 
ATOM   3231 C CB  . VAL A 1 451 ? 33.288 18.381  -34.010 1.00 24.64  ? 584 VAL A CB  1 
ATOM   3232 C CG1 . VAL A 1 451 ? 32.849 19.818  -34.252 1.00 23.96  ? 584 VAL A CG1 1 
ATOM   3233 C CG2 . VAL A 1 451 ? 34.481 18.011  -34.899 1.00 26.93  ? 584 VAL A CG2 1 
ATOM   3234 N N   . HIS A 1 452 ? 34.573 20.328  -31.795 1.00 23.86  ? 585 HIS A N   1 
ATOM   3235 C CA  . HIS A 1 452 ? 35.672 21.213  -31.422 1.00 25.67  ? 585 HIS A CA  1 
ATOM   3236 C C   . HIS A 1 452 ? 36.299 20.759  -30.105 1.00 25.44  ? 585 HIS A C   1 
ATOM   3237 O O   . HIS A 1 452 ? 37.513 20.873  -29.927 1.00 22.58  ? 585 HIS A O   1 
ATOM   3238 C CB  . HIS A 1 452 ? 35.194 22.664  -31.320 1.00 29.62  ? 585 HIS A CB  1 
ATOM   3239 C CG  . HIS A 1 452 ? 34.704 23.219  -32.620 1.00 35.74  ? 585 HIS A CG  1 
ATOM   3240 N ND1 . HIS A 1 452 ? 33.398 23.618  -32.815 1.00 39.70  ? 585 HIS A ND1 1 
ATOM   3241 C CD2 . HIS A 1 452 ? 35.332 23.390  -33.808 1.00 36.51  ? 585 HIS A CD2 1 
ATOM   3242 C CE1 . HIS A 1 452 ? 33.241 24.007  -34.069 1.00 40.59  ? 585 HIS A CE1 1 
ATOM   3243 N NE2 . HIS A 1 452 ? 34.400 23.878  -34.692 1.00 40.11  ? 585 HIS A NE2 1 
ATOM   3244 N N   . ASN A 1 453 ? 35.479 20.230  -29.193 1.00 22.93  ? 586 ASN A N   1 
ATOM   3245 C CA  . ASN A 1 453 ? 36.000 19.741  -27.912 1.00 23.44  ? 586 ASN A CA  1 
ATOM   3246 C C   . ASN A 1 453 ? 36.888 18.515  -28.136 1.00 22.67  ? 586 ASN A C   1 
ATOM   3247 O O   . ASN A 1 453 ? 37.904 18.346  -27.459 1.00 20.00  ? 586 ASN A O   1 
ATOM   3248 C CB  . ASN A 1 453 ? 34.862 19.381  -26.945 1.00 20.67  ? 586 ASN A CB  1 
ATOM   3249 C CG  . ASN A 1 453 ? 34.161 20.605  -26.391 1.00 23.19  ? 586 ASN A CG  1 
ATOM   3250 O OD1 . ASN A 1 453 ? 34.660 21.725  -26.520 1.00 22.07  ? 586 ASN A OD1 1 
ATOM   3251 N ND2 . ASN A 1 453 ? 33.005 20.399  -25.758 1.00 19.81  ? 586 ASN A ND2 1 
ATOM   3252 N N   . ARG A 1 454 ? 36.506 17.660  -29.084 1.00 20.54  ? 587 ARG A N   1 
ATOM   3253 C CA  . ARG A 1 454 ? 37.306 16.473  -29.378 1.00 21.89  ? 587 ARG A CA  1 
ATOM   3254 C C   . ARG A 1 454 ? 38.716 16.846  -29.816 1.00 21.58  ? 587 ARG A C   1 
ATOM   3255 O O   . ARG A 1 454 ? 39.692 16.184  -29.447 1.00 21.00  ? 587 ARG A O   1 
ATOM   3256 C CB  . ARG A 1 454 ? 36.646 15.631  -30.472 1.00 22.23  ? 587 ARG A CB  1 
ATOM   3257 C CG  . ARG A 1 454 ? 35.489 14.798  -29.971 1.00 22.86  ? 587 ARG A CG  1 
ATOM   3258 C CD  . ARG A 1 454 ? 34.865 14.000  -31.096 1.00 26.43  ? 587 ARG A CD  1 
ATOM   3259 N NE  . ARG A 1 454 ? 33.428 14.144  -30.983 1.00 35.48  ? 587 ARG A NE  1 
ATOM   3260 C CZ  . ARG A 1 454 ? 32.633 14.576  -31.946 1.00 29.76  ? 587 ARG A CZ  1 
ATOM   3261 N NH1 . ARG A 1 454 ? 33.126 14.900  -33.134 1.00 27.88  ? 587 ARG A NH1 1 
ATOM   3262 N NH2 . ARG A 1 454 ? 31.345 14.716  -31.691 1.00 31.88  ? 587 ARG A NH2 1 
ATOM   3263 N N   . ILE A 1 455 ? 38.818 17.903  -30.609 1.00 21.56  ? 588 ILE A N   1 
ATOM   3264 C CA  . ILE A 1 455 ? 40.114 18.372  -31.093 1.00 23.66  ? 588 ILE A CA  1 
ATOM   3265 C C   . ILE A 1 455 ? 40.986 18.822  -29.911 1.00 22.70  ? 588 ILE A C   1 
ATOM   3266 O O   . ILE A 1 455 ? 42.164 18.469  -29.838 1.00 24.74  ? 588 ILE A O   1 
ATOM   3267 C CB  . ILE A 1 455 ? 39.923 19.530  -32.113 1.00 25.99  ? 588 ILE A CB  1 
ATOM   3268 C CG1 . ILE A 1 455 ? 39.306 18.974  -33.401 1.00 26.28  ? 588 ILE A CG1 1 
ATOM   3269 C CG2 . ILE A 1 455 ? 41.254 20.224  -32.411 1.00 25.13  ? 588 ILE A CG2 1 
ATOM   3270 C CD1 . ILE A 1 455 ? 38.849 20.045  -34.373 1.00 28.90  ? 588 ILE A CD1 1 
ATOM   3271 N N   . VAL A 1 456 ? 40.405 19.572  -28.975 1.00 23.25  ? 589 VAL A N   1 
ATOM   3272 C CA  . VAL A 1 456 ? 41.151 20.037  -27.801 1.00 21.18  ? 589 VAL A CA  1 
ATOM   3273 C C   . VAL A 1 456 ? 41.580 18.843  -26.952 1.00 22.19  ? 589 VAL A C   1 
ATOM   3274 O O   . VAL A 1 456 ? 42.739 18.737  -26.545 1.00 20.48  ? 589 VAL A O   1 
ATOM   3275 C CB  . VAL A 1 456 ? 40.305 20.971  -26.902 1.00 21.34  ? 589 VAL A CB  1 
ATOM   3276 C CG1 . VAL A 1 456 ? 41.113 21.368  -25.667 1.00 18.78  ? 589 VAL A CG1 1 
ATOM   3277 C CG2 . VAL A 1 456 ? 39.884 22.212  -27.675 1.00 22.51  ? 589 VAL A CG2 1 
ATOM   3278 N N   . ILE A 1 457 ? 40.625 17.956  -26.679 1.00 21.22  ? 590 ILE A N   1 
ATOM   3279 C CA  . ILE A 1 457 ? 40.872 16.757  -25.885 1.00 20.24  ? 590 ILE A CA  1 
ATOM   3280 C C   . ILE A 1 457 ? 41.993 15.911  -26.502 1.00 20.43  ? 590 ILE A C   1 
ATOM   3281 O O   . ILE A 1 457 ? 42.911 15.477  -25.812 1.00 20.68  ? 590 ILE A O   1 
ATOM   3282 C CB  . ILE A 1 457 ? 39.582 15.893  -25.778 1.00 20.47  ? 590 ILE A CB  1 
ATOM   3283 C CG1 . ILE A 1 457 ? 38.543 16.612  -24.910 1.00 18.49  ? 590 ILE A CG1 1 
ATOM   3284 C CG2 . ILE A 1 457 ? 39.914 14.519  -25.222 1.00 16.09  ? 590 ILE A CG2 1 
ATOM   3285 C CD1 . ILE A 1 457 ? 37.179 15.911  -24.846 1.00 20.60  ? 590 ILE A CD1 1 
ATOM   3286 N N   . ARG A 1 458 ? 41.915 15.676  -27.805 1.00 21.55  ? 591 ARG A N   1 
ATOM   3287 C CA  . ARG A 1 458 ? 42.935 14.883  -28.467 1.00 23.09  ? 591 ARG A CA  1 
ATOM   3288 C C   . ARG A 1 458 ? 44.285 15.604  -28.497 1.00 22.50  ? 591 ARG A C   1 
ATOM   3289 O O   . ARG A 1 458 ? 45.332 14.974  -28.345 1.00 20.48  ? 591 ARG A O   1 
ATOM   3290 C CB  . ARG A 1 458 ? 42.508 14.540  -29.894 1.00 25.76  ? 591 ARG A CB  1 
ATOM   3291 C CG  . ARG A 1 458 ? 43.479 13.596  -30.575 1.00 30.10  ? 591 ARG A CG  1 
ATOM   3292 C CD  . ARG A 1 458 ? 43.155 13.412  -32.037 1.00 35.90  ? 591 ARG A CD  1 
ATOM   3293 N NE  . ARG A 1 458 ? 44.182 12.612  -32.691 1.00 39.58  ? 591 ARG A NE  1 
ATOM   3294 C CZ  . ARG A 1 458 ? 44.371 12.570  -34.003 1.00 40.69  ? 591 ARG A CZ  1 
ATOM   3295 N NH1 . ARG A 1 458 ? 43.598 13.287  -34.811 1.00 39.71  ? 591 ARG A NH1 1 
ATOM   3296 N NH2 . ARG A 1 458 ? 45.339 11.817  -34.504 1.00 42.33  ? 591 ARG A NH2 1 
ATOM   3297 N N   . GLY A 1 459 ? 44.254 16.921  -28.691 1.00 23.08  ? 592 GLY A N   1 
ATOM   3298 C CA  . GLY A 1 459 ? 45.484 17.700  -28.742 1.00 22.54  ? 592 GLY A CA  1 
ATOM   3299 C C   . GLY A 1 459 ? 46.247 17.759  -27.426 1.00 25.23  ? 592 GLY A C   1 
ATOM   3300 O O   . GLY A 1 459 ? 47.420 18.150  -27.390 1.00 23.87  ? 592 GLY A O   1 
ATOM   3301 N N   . LEU A 1 460 ? 45.580 17.382  -26.338 1.00 22.99  ? 593 LEU A N   1 
ATOM   3302 C CA  . LEU A 1 460 ? 46.209 17.379  -25.026 1.00 23.95  ? 593 LEU A CA  1 
ATOM   3303 C C   . LEU A 1 460 ? 46.882 16.032  -24.798 1.00 24.11  ? 593 LEU A C   1 
ATOM   3304 O O   . LEU A 1 460 ? 47.271 15.705  -23.683 1.00 26.53  ? 593 LEU A O   1 
ATOM   3305 C CB  . LEU A 1 460 ? 45.165 17.652  -23.933 1.00 23.35  ? 593 LEU A CB  1 
ATOM   3306 C CG  . LEU A 1 460 ? 44.632 19.093  -23.866 1.00 24.29  ? 593 LEU A CG  1 
ATOM   3307 C CD1 . LEU A 1 460 ? 43.315 19.151  -23.095 1.00 23.13  ? 593 LEU A CD1 1 
ATOM   3308 C CD2 . LEU A 1 460 ? 45.676 19.976  -23.204 1.00 23.55  ? 593 LEU A CD2 1 
ATOM   3309 N N   . ASN A 1 461 ? 47.018 15.258  -25.872 1.00 25.29  ? 594 ASN A N   1 
ATOM   3310 C CA  . ASN A 1 461 ? 47.650 13.942  -25.821 1.00 28.19  ? 594 ASN A CA  1 
ATOM   3311 C C   . ASN A 1 461 ? 47.045 13.070  -24.719 1.00 29.28  ? 594 ASN A C   1 
ATOM   3312 O O   . ASN A 1 461 ? 47.758 12.552  -23.859 1.00 30.19  ? 594 ASN A O   1 
ATOM   3313 C CB  . ASN A 1 461 ? 49.157 14.100  -25.596 1.00 28.30  ? 594 ASN A CB  1 
ATOM   3314 C CG  . ASN A 1 461 ? 49.914 12.809  -25.815 1.00 29.36  ? 594 ASN A CG  1 
ATOM   3315 O OD1 . ASN A 1 461 ? 49.757 12.157  -26.844 1.00 31.32  ? 594 ASN A OD1 1 
ATOM   3316 N ND2 . ASN A 1 461 ? 50.744 12.435  -24.850 1.00 31.80  ? 594 ASN A ND2 1 
ATOM   3317 N N   . THR A 1 462 ? 45.728 12.900  -24.774 1.00 27.67  ? 595 THR A N   1 
ATOM   3318 C CA  . THR A 1 462 ? 44.982 12.128  -23.787 1.00 27.40  ? 595 THR A CA  1 
ATOM   3319 C C   . THR A 1 462 ? 44.664 10.683  -24.167 1.00 27.09  ? 595 THR A C   1 
ATOM   3320 O O   . THR A 1 462 ? 44.362 9.866   -23.301 1.00 27.99  ? 595 THR A O   1 
ATOM   3321 C CB  . THR A 1 462 ? 43.649 12.814  -23.484 1.00 27.37  ? 595 THR A CB  1 
ATOM   3322 O OG1 . THR A 1 462 ? 42.956 13.057  -24.719 1.00 28.89  ? 595 THR A OG1 1 
ATOM   3323 C CG2 . THR A 1 462 ? 43.878 14.137  -22.764 1.00 26.06  ? 595 THR A CG2 1 
ATOM   3324 N N   . ILE A 1 463 ? 44.714 10.367  -25.454 1.00 27.50  ? 596 ILE A N   1 
ATOM   3325 C CA  . ILE A 1 463 ? 44.395 9.017   -25.901 1.00 28.58  ? 596 ILE A CA  1 
ATOM   3326 C C   . ILE A 1 463 ? 45.196 7.921   -25.195 1.00 29.29  ? 596 ILE A C   1 
ATOM   3327 O O   . ILE A 1 463 ? 44.631 6.911   -24.783 1.00 28.76  ? 596 ILE A O   1 
ATOM   3328 C CB  . ILE A 1 463 ? 44.536 8.911   -27.436 1.00 28.15  ? 596 ILE A CB  1 
ATOM   3329 C CG1 . ILE A 1 463 ? 43.396 9.708   -28.088 1.00 26.45  ? 596 ILE A CG1 1 
ATOM   3330 C CG2 . ILE A 1 463 ? 44.495 7.455   -27.883 1.00 28.29  ? 596 ILE A CG2 1 
ATOM   3331 C CD1 . ILE A 1 463 ? 43.450 9.768   -29.598 1.00 27.06  ? 596 ILE A CD1 1 
ATOM   3332 N N   . PRO A 1 464 ? 46.516 8.106   -25.035 1.00 30.52  ? 597 PRO A N   1 
ATOM   3333 C CA  . PRO A 1 464 ? 47.308 7.072   -24.353 1.00 30.67  ? 597 PRO A CA  1 
ATOM   3334 C C   . PRO A 1 464 ? 46.774 6.819   -22.940 1.00 29.22  ? 597 PRO A C   1 
ATOM   3335 O O   . PRO A 1 464 ? 46.714 5.680   -22.483 1.00 29.59  ? 597 PRO A O   1 
ATOM   3336 C CB  . PRO A 1 464 ? 48.713 7.669   -24.336 1.00 30.62  ? 597 PRO A CB  1 
ATOM   3337 C CG  . PRO A 1 464 ? 48.742 8.468   -25.612 1.00 32.28  ? 597 PRO A CG  1 
ATOM   3338 C CD  . PRO A 1 464 ? 47.390 9.155   -25.592 1.00 30.82  ? 597 PRO A CD  1 
ATOM   3339 N N   . LEU A 1 465 ? 46.383 7.891   -22.256 1.00 27.74  ? 598 LEU A N   1 
ATOM   3340 C CA  . LEU A 1 465 ? 45.850 7.782   -20.903 1.00 28.60  ? 598 LEU A CA  1 
ATOM   3341 C C   . LEU A 1 465 ? 44.509 7.045   -20.905 1.00 26.43  ? 598 LEU A C   1 
ATOM   3342 O O   . LEU A 1 465 ? 44.308 6.119   -20.123 1.00 26.13  ? 598 LEU A O   1 
ATOM   3343 C CB  . LEU A 1 465 ? 45.654 9.174   -20.293 1.00 30.95  ? 598 LEU A CB  1 
ATOM   3344 C CG  . LEU A 1 465 ? 45.585 9.308   -18.766 1.00 33.55  ? 598 LEU A CG  1 
ATOM   3345 C CD1 . LEU A 1 465 ? 45.126 10.710  -18.428 1.00 35.53  ? 598 LEU A CD1 1 
ATOM   3346 C CD2 . LEU A 1 465 ? 44.636 8.301   -18.159 1.00 37.28  ? 598 LEU A CD2 1 
ATOM   3347 N N   . PHE A 1 466 ? 43.593 7.467   -21.775 1.00 26.11  ? 599 PHE A N   1 
ATOM   3348 C CA  . PHE A 1 466 ? 42.275 6.842   -21.853 1.00 24.71  ? 599 PHE A CA  1 
ATOM   3349 C C   . PHE A 1 466 ? 42.404 5.339   -22.094 1.00 25.34  ? 599 PHE A C   1 
ATOM   3350 O O   . PHE A 1 466 ? 41.668 4.541   -21.515 1.00 27.62  ? 599 PHE A O   1 
ATOM   3351 C CB  . PHE A 1 466 ? 41.429 7.478   -22.969 1.00 20.85  ? 599 PHE A CB  1 
ATOM   3352 C CG  . PHE A 1 466 ? 41.030 8.912   -22.699 1.00 22.49  ? 599 PHE A CG  1 
ATOM   3353 C CD1 . PHE A 1 466 ? 40.741 9.343   -21.404 1.00 21.04  ? 599 PHE A CD1 1 
ATOM   3354 C CD2 . PHE A 1 466 ? 40.915 9.821   -23.744 1.00 21.63  ? 599 PHE A CD2 1 
ATOM   3355 C CE1 . PHE A 1 466 ? 40.341 10.659  -21.158 1.00 24.11  ? 599 PHE A CE1 1 
ATOM   3356 C CE2 . PHE A 1 466 ? 40.515 11.139  -23.511 1.00 23.05  ? 599 PHE A CE2 1 
ATOM   3357 C CZ  . PHE A 1 466 ? 40.228 11.560  -22.219 1.00 23.21  ? 599 PHE A CZ  1 
ATOM   3358 N N   . VAL A 1 467 ? 43.334 4.953   -22.957 1.00 26.25  ? 600 VAL A N   1 
ATOM   3359 C CA  . VAL A 1 467 ? 43.544 3.539   -23.242 1.00 27.33  ? 600 VAL A CA  1 
ATOM   3360 C C   . VAL A 1 467 ? 44.003 2.805   -21.983 1.00 26.33  ? 600 VAL A C   1 
ATOM   3361 O O   . VAL A 1 467 ? 43.560 1.694   -21.715 1.00 28.43  ? 600 VAL A O   1 
ATOM   3362 C CB  . VAL A 1 467 ? 44.580 3.346   -24.365 1.00 27.87  ? 600 VAL A CB  1 
ATOM   3363 C CG1 . VAL A 1 467 ? 44.907 1.865   -24.531 1.00 27.67  ? 600 VAL A CG1 1 
ATOM   3364 C CG2 . VAL A 1 467 ? 44.023 3.903   -25.667 1.00 28.39  ? 600 VAL A CG2 1 
ATOM   3365 N N   . GLN A 1 468 ? 44.879 3.428   -21.203 1.00 26.23  ? 601 GLN A N   1 
ATOM   3366 C CA  . GLN A 1 468 ? 45.356 2.806   -19.974 1.00 28.58  ? 601 GLN A CA  1 
ATOM   3367 C C   . GLN A 1 468 ? 44.239 2.652   -18.944 1.00 28.91  ? 601 GLN A C   1 
ATOM   3368 O O   . GLN A 1 468 ? 44.224 1.687   -18.180 1.00 29.35  ? 601 GLN A O   1 
ATOM   3369 C CB  . GLN A 1 468 ? 46.509 3.615   -19.372 1.00 30.19  ? 601 GLN A CB  1 
ATOM   3370 C CG  . GLN A 1 468 ? 47.807 3.461   -20.138 1.00 36.69  ? 601 GLN A CG  1 
ATOM   3371 C CD  . GLN A 1 468 ? 48.237 2.006   -20.252 1.00 39.16  ? 601 GLN A CD  1 
ATOM   3372 O OE1 . GLN A 1 468 ? 48.565 1.365   -19.252 1.00 41.13  ? 601 GLN A OE1 1 
ATOM   3373 N NE2 . GLN A 1 468 ? 48.227 1.477   -21.473 1.00 41.14  ? 601 GLN A NE2 1 
ATOM   3374 N N   . LEU A 1 469 ? 43.305 3.599   -18.922 1.00 26.68  ? 602 LEU A N   1 
ATOM   3375 C CA  . LEU A 1 469 ? 42.192 3.535   -17.977 1.00 25.82  ? 602 LEU A CA  1 
ATOM   3376 C C   . LEU A 1 469 ? 41.283 2.353   -18.293 1.00 26.57  ? 602 LEU A C   1 
ATOM   3377 O O   . LEU A 1 469 ? 40.452 1.957   -17.476 1.00 27.01  ? 602 LEU A O   1 
ATOM   3378 C CB  . LEU A 1 469 ? 41.385 4.833   -18.014 1.00 23.56  ? 602 LEU A CB  1 
ATOM   3379 C CG  . LEU A 1 469 ? 42.106 6.064   -17.466 1.00 23.43  ? 602 LEU A CG  1 
ATOM   3380 C CD1 . LEU A 1 469 ? 41.220 7.305   -17.622 1.00 22.23  ? 602 LEU A CD1 1 
ATOM   3381 C CD2 . LEU A 1 469 ? 42.447 5.820   -15.997 1.00 22.33  ? 602 LEU A CD2 1 
ATOM   3382 N N   . LEU A 1 470 ? 41.432 1.807   -19.495 1.00 27.44  ? 603 LEU A N   1 
ATOM   3383 C CA  . LEU A 1 470 ? 40.647 0.653   -19.916 1.00 29.18  ? 603 LEU A CA  1 
ATOM   3384 C C   . LEU A 1 470 ? 40.997 -0.539  -19.015 1.00 31.50  ? 603 LEU A C   1 
ATOM   3385 O O   . LEU A 1 470 ? 40.175 -1.435  -18.804 1.00 30.90  ? 603 LEU A O   1 
ATOM   3386 C CB  . LEU A 1 470 ? 40.966 0.323   -21.376 1.00 27.64  ? 603 LEU A CB  1 
ATOM   3387 C CG  . LEU A 1 470 ? 39.981 0.674   -22.501 1.00 29.61  ? 603 LEU A CG  1 
ATOM   3388 C CD1 . LEU A 1 470 ? 39.066 1.819   -22.114 1.00 25.90  ? 603 LEU A CD1 1 
ATOM   3389 C CD2 . LEU A 1 470 ? 40.773 0.996   -23.757 1.00 25.47  ? 603 LEU A CD2 1 
ATOM   3390 N N   . TYR A 1 471 ? 42.218 -0.531  -18.479 1.00 32.92  ? 604 TYR A N   1 
ATOM   3391 C CA  . TYR A 1 471 ? 42.691 -1.607  -17.605 1.00 34.62  ? 604 TYR A CA  1 
ATOM   3392 C C   . TYR A 1 471 ? 42.284 -1.423  -16.150 1.00 33.31  ? 604 TYR A C   1 
ATOM   3393 O O   . TYR A 1 471 ? 42.614 -2.246  -15.306 1.00 33.66  ? 604 TYR A O   1 
ATOM   3394 C CB  . TYR A 1 471 ? 44.218 -1.726  -17.662 1.00 36.44  ? 604 TYR A CB  1 
ATOM   3395 C CG  . TYR A 1 471 ? 44.783 -2.083  -19.020 1.00 38.37  ? 604 TYR A CG  1 
ATOM   3396 C CD1 . TYR A 1 471 ? 45.049 -1.097  -19.969 1.00 38.18  ? 604 TYR A CD1 1 
ATOM   3397 C CD2 . TYR A 1 471 ? 45.073 -3.407  -19.347 1.00 39.04  ? 604 TYR A CD2 1 
ATOM   3398 C CE1 . TYR A 1 471 ? 45.595 -1.420  -21.206 1.00 38.00  ? 604 TYR A CE1 1 
ATOM   3399 C CE2 . TYR A 1 471 ? 45.615 -3.741  -20.582 1.00 39.58  ? 604 TYR A CE2 1 
ATOM   3400 C CZ  . TYR A 1 471 ? 45.875 -2.744  -21.506 1.00 39.41  ? 604 TYR A CZ  1 
ATOM   3401 O OH  . TYR A 1 471 ? 46.418 -3.075  -22.727 1.00 41.88  ? 604 TYR A OH  1 
ATOM   3402 N N   . SER A 1 472 ? 41.581 -0.340  -15.851 1.00 32.53  ? 605 SER A N   1 
ATOM   3403 C CA  . SER A 1 472 ? 41.152 -0.093  -14.483 1.00 31.52  ? 605 SER A CA  1 
ATOM   3404 C C   . SER A 1 472 ? 40.276 -1.226  -13.960 1.00 32.61  ? 605 SER A C   1 
ATOM   3405 O O   . SER A 1 472 ? 39.506 -1.824  -14.713 1.00 30.46  ? 605 SER A O   1 
ATOM   3406 C CB  . SER A 1 472 ? 40.370 1.219   -14.399 1.00 30.69  ? 605 SER A CB  1 
ATOM   3407 O OG  . SER A 1 472 ? 39.810 1.389   -13.109 1.00 29.56  ? 605 SER A OG  1 
ATOM   3408 N N   . PRO A 1 473 ? 40.399 -1.547  -12.661 1.00 32.81  ? 606 PRO A N   1 
ATOM   3409 C CA  . PRO A 1 473 ? 39.604 -2.610  -12.039 1.00 34.19  ? 606 PRO A CA  1 
ATOM   3410 C C   . PRO A 1 473 ? 38.226 -2.071  -11.667 1.00 34.99  ? 606 PRO A C   1 
ATOM   3411 O O   . PRO A 1 473 ? 37.326 -2.831  -11.313 1.00 35.73  ? 606 PRO A O   1 
ATOM   3412 C CB  . PRO A 1 473 ? 40.427 -2.977  -10.808 1.00 35.23  ? 606 PRO A CB  1 
ATOM   3413 C CG  . PRO A 1 473 ? 41.011 -1.664  -10.411 1.00 33.74  ? 606 PRO A CG  1 
ATOM   3414 C CD  . PRO A 1 473 ? 41.468 -1.101  -11.749 1.00 33.88  ? 606 PRO A CD  1 
ATOM   3415 N N   . ILE A 1 474 ? 38.078 -0.750  -11.751 1.00 33.08  ? 607 ILE A N   1 
ATOM   3416 C CA  . ILE A 1 474 ? 36.822 -0.086  -11.425 1.00 31.66  ? 607 ILE A CA  1 
ATOM   3417 C C   . ILE A 1 474 ? 35.928 -0.053  -12.663 1.00 31.78  ? 607 ILE A C   1 
ATOM   3418 O O   . ILE A 1 474 ? 36.262 0.568   -13.672 1.00 30.29  ? 607 ILE A O   1 
ATOM   3419 C CB  . ILE A 1 474 ? 37.069 1.365   -10.943 1.00 33.39  ? 607 ILE A CB  1 
ATOM   3420 C CG1 . ILE A 1 474 ? 38.098 1.375   -9.803  1.00 33.70  ? 607 ILE A CG1 1 
ATOM   3421 C CG2 . ILE A 1 474 ? 35.752 1.997   -10.494 1.00 30.32  ? 607 ILE A CG2 1 
ATOM   3422 C CD1 . ILE A 1 474 ? 37.649 0.638   -8.554  1.00 35.19  ? 607 ILE A CD1 1 
ATOM   3423 N N   . GLU A 1 475 ? 34.784 -0.719  -12.570 1.00 30.55  ? 608 GLU A N   1 
ATOM   3424 C CA  . GLU A 1 475 ? 33.834 -0.798  -13.669 1.00 30.14  ? 608 GLU A CA  1 
ATOM   3425 C C   . GLU A 1 475 ? 33.377 0.557   -14.216 1.00 28.24  ? 608 GLU A C   1 
ATOM   3426 O O   . GLU A 1 475 ? 33.299 0.748   -15.427 1.00 27.32  ? 608 GLU A O   1 
ATOM   3427 C CB  . GLU A 1 475 ? 32.619 -1.613  -13.225 1.00 32.36  ? 608 GLU A CB  1 
ATOM   3428 C CG  . GLU A 1 475 ? 31.545 -1.766  -14.276 1.00 37.23  ? 608 GLU A CG  1 
ATOM   3429 C CD  . GLU A 1 475 ? 30.423 -2.676  -13.809 1.00 40.68  ? 608 GLU A CD  1 
ATOM   3430 O OE1 . GLU A 1 475 ? 30.698 -3.869  -13.547 1.00 41.47  ? 608 GLU A OE1 1 
ATOM   3431 O OE2 . GLU A 1 475 ? 29.274 -2.195  -13.700 1.00 38.86  ? 608 GLU A OE2 1 
ATOM   3432 N N   . ASN A 1 476 ? 33.069 1.499   -13.336 1.00 28.17  ? 609 ASN A N   1 
ATOM   3433 C CA  . ASN A 1 476 ? 32.625 2.801   -13.810 1.00 28.85  ? 609 ASN A CA  1 
ATOM   3434 C C   . ASN A 1 476 ? 33.726 3.578   -14.530 1.00 26.64  ? 609 ASN A C   1 
ATOM   3435 O O   . ASN A 1 476 ? 33.434 4.415   -15.383 1.00 24.91  ? 609 ASN A O   1 
ATOM   3436 C CB  . ASN A 1 476 ? 32.052 3.626   -12.661 1.00 32.73  ? 609 ASN A CB  1 
ATOM   3437 C CG  . ASN A 1 476 ? 30.733 3.074   -12.160 1.00 35.66  ? 609 ASN A CG  1 
ATOM   3438 O OD1 . ASN A 1 476 ? 30.038 2.356   -12.879 1.00 38.27  ? 609 ASN A OD1 1 
ATOM   3439 N ND2 . ASN A 1 476 ? 30.374 3.418   -10.932 1.00 39.62  ? 609 ASN A ND2 1 
ATOM   3440 N N   . ILE A 1 477 ? 34.983 3.295   -14.197 1.00 23.52  ? 610 ILE A N   1 
ATOM   3441 C CA  . ILE A 1 477 ? 36.102 3.965   -14.852 1.00 24.94  ? 610 ILE A CA  1 
ATOM   3442 C C   . ILE A 1 477 ? 36.248 3.370   -16.249 1.00 25.43  ? 610 ILE A C   1 
ATOM   3443 O O   . ILE A 1 477 ? 36.452 4.095   -17.227 1.00 23.99  ? 610 ILE A O   1 
ATOM   3444 C CB  . ILE A 1 477 ? 37.421 3.815   -14.027 1.00 25.78  ? 610 ILE A CB  1 
ATOM   3445 C CG1 . ILE A 1 477 ? 37.335 4.711   -12.784 1.00 25.73  ? 610 ILE A CG1 1 
ATOM   3446 C CG2 . ILE A 1 477 ? 38.642 4.217   -14.869 1.00 24.85  ? 610 ILE A CG2 1 
ATOM   3447 C CD1 . ILE A 1 477 ? 38.587 4.736   -11.925 1.00 26.86  ? 610 ILE A CD1 1 
ATOM   3448 N N   . GLN A 1 478 ? 36.114 2.047   -16.342 1.00 24.81  ? 611 GLN A N   1 
ATOM   3449 C CA  . GLN A 1 478 ? 36.185 1.355   -17.626 1.00 23.48  ? 611 GLN A CA  1 
ATOM   3450 C C   . GLN A 1 478 ? 35.108 1.910   -18.564 1.00 21.82  ? 611 GLN A C   1 
ATOM   3451 O O   . GLN A 1 478 ? 35.332 2.084   -19.761 1.00 21.80  ? 611 GLN A O   1 
ATOM   3452 C CB  . GLN A 1 478 ? 35.923 -0.143  -17.443 1.00 23.21  ? 611 GLN A CB  1 
ATOM   3453 C CG  . GLN A 1 478 ? 36.966 -0.906  -16.645 1.00 24.51  ? 611 GLN A CG  1 
ATOM   3454 C CD  . GLN A 1 478 ? 36.474 -2.298  -16.286 1.00 27.11  ? 611 GLN A CD  1 
ATOM   3455 O OE1 . GLN A 1 478 ? 35.458 -2.757  -16.809 1.00 27.97  ? 611 GLN A OE1 1 
ATOM   3456 N NE2 . GLN A 1 478 ? 37.191 -2.977  -15.397 1.00 26.37  ? 611 GLN A NE2 1 
ATOM   3457 N N   . ARG A 1 479 ? 33.934 2.165   -18.003 1.00 21.95  ? 612 ARG A N   1 
ATOM   3458 C CA  . ARG A 1 479 ? 32.796 2.675   -18.762 1.00 22.57  ? 612 ARG A CA  1 
ATOM   3459 C C   . ARG A 1 479 ? 33.030 4.057   -19.380 1.00 22.64  ? 612 ARG A C   1 
ATOM   3460 O O   . ARG A 1 479 ? 32.786 4.245   -20.575 1.00 22.96  ? 612 ARG A O   1 
ATOM   3461 C CB  . ARG A 1 479 ? 31.561 2.709   -17.865 1.00 22.85  ? 612 ARG A CB  1 
ATOM   3462 C CG  . ARG A 1 479 ? 30.248 2.990   -18.581 1.00 26.39  ? 612 ARG A CG  1 
ATOM   3463 C CD  . ARG A 1 479 ? 29.093 2.895   -17.593 1.00 30.65  ? 612 ARG A CD  1 
ATOM   3464 N NE  . ARG A 1 479 ? 27.791 2.780   -18.248 1.00 36.79  ? 612 ARG A NE  1 
ATOM   3465 C CZ  . ARG A 1 479 ? 27.186 3.763   -18.911 1.00 40.62  ? 612 ARG A CZ  1 
ATOM   3466 N NH1 . ARG A 1 479 ? 27.757 4.958   -19.019 1.00 40.69  ? 612 ARG A NH1 1 
ATOM   3467 N NH2 . ARG A 1 479 ? 26.001 3.547   -19.472 1.00 42.84  ? 612 ARG A NH2 1 
ATOM   3468 N N   . VAL A 1 480 ? 33.497 5.021   -18.583 1.00 21.07  ? 613 VAL A N   1 
ATOM   3469 C CA  . VAL A 1 480 ? 33.739 6.362   -19.112 1.00 20.93  ? 613 VAL A CA  1 
ATOM   3470 C C   . VAL A 1 480 ? 34.978 6.452   -20.008 1.00 22.11  ? 613 VAL A C   1 
ATOM   3471 O O   . VAL A 1 480 ? 35.040 7.303   -20.909 1.00 19.85  ? 613 VAL A O   1 
ATOM   3472 C CB  . VAL A 1 480 ? 33.821 7.431   -17.978 1.00 23.20  ? 613 VAL A CB  1 
ATOM   3473 C CG1 . VAL A 1 480 ? 32.438 7.598   -17.340 1.00 21.95  ? 613 VAL A CG1 1 
ATOM   3474 C CG2 . VAL A 1 480 ? 34.856 7.032   -16.924 1.00 18.26  ? 613 VAL A CG2 1 
ATOM   3475 N N   . ALA A 1 481 ? 35.960 5.581   -19.774 1.00 20.86  ? 614 ALA A N   1 
ATOM   3476 C CA  . ALA A 1 481 ? 37.165 5.567   -20.604 1.00 19.85  ? 614 ALA A CA  1 
ATOM   3477 C C   . ALA A 1 481 ? 36.765 5.036   -21.981 1.00 19.51  ? 614 ALA A C   1 
ATOM   3478 O O   . ALA A 1 481 ? 37.126 5.609   -23.006 1.00 19.05  ? 614 ALA A O   1 
ATOM   3479 C CB  . ALA A 1 481 ? 38.235 4.673   -19.983 1.00 22.45  ? 614 ALA A CB  1 
ATOM   3480 N N   . ALA A 1 482 ? 36.021 3.933   -22.002 1.00 18.45  ? 615 ALA A N   1 
ATOM   3481 C CA  . ALA A 1 482 ? 35.556 3.368   -23.264 1.00 18.65  ? 615 ALA A CA  1 
ATOM   3482 C C   . ALA A 1 482 ? 34.617 4.389   -23.919 1.00 19.55  ? 615 ALA A C   1 
ATOM   3483 O O   . ALA A 1 482 ? 34.612 4.560   -25.138 1.00 19.81  ? 615 ALA A O   1 
ATOM   3484 C CB  . ALA A 1 482 ? 34.810 2.062   -23.012 1.00 20.18  ? 615 ALA A CB  1 
ATOM   3485 N N   . GLY A 1 483 ? 33.823 5.063   -23.090 1.00 18.71  ? 616 GLY A N   1 
ATOM   3486 C CA  . GLY A 1 483 ? 32.895 6.064   -23.590 1.00 19.40  ? 616 GLY A CA  1 
ATOM   3487 C C   . GLY A 1 483 ? 33.568 7.224   -24.309 1.00 18.55  ? 616 GLY A C   1 
ATOM   3488 O O   . GLY A 1 483 ? 33.189 7.554   -25.429 1.00 18.32  ? 616 GLY A O   1 
ATOM   3489 N N   . VAL A 1 484 ? 34.570 7.844   -23.685 1.00 19.27  ? 617 VAL A N   1 
ATOM   3490 C CA  . VAL A 1 484 ? 35.241 8.974   -24.322 1.00 20.33  ? 617 VAL A CA  1 
ATOM   3491 C C   . VAL A 1 484 ? 35.983 8.517   -25.583 1.00 20.83  ? 617 VAL A C   1 
ATOM   3492 O O   . VAL A 1 484 ? 36.027 9.238   -26.583 1.00 17.64  ? 617 VAL A O   1 
ATOM   3493 C CB  . VAL A 1 484 ? 36.206 9.719   -23.327 1.00 21.77  ? 617 VAL A CB  1 
ATOM   3494 C CG1 . VAL A 1 484 ? 37.454 8.887   -23.040 1.00 20.26  ? 617 VAL A CG1 1 
ATOM   3495 C CG2 . VAL A 1 484 ? 36.590 11.079  -23.907 1.00 22.71  ? 617 VAL A CG2 1 
ATOM   3496 N N   . LEU A 1 485 ? 36.542 7.308   -25.548 1.00 21.41  ? 618 LEU A N   1 
ATOM   3497 C CA  . LEU A 1 485 ? 37.233 6.772   -26.719 1.00 21.81  ? 618 LEU A CA  1 
ATOM   3498 C C   . LEU A 1 485 ? 36.234 6.586   -27.860 1.00 22.44  ? 618 LEU A C   1 
ATOM   3499 O O   . LEU A 1 485 ? 36.551 6.832   -29.025 1.00 21.16  ? 618 LEU A O   1 
ATOM   3500 C CB  . LEU A 1 485 ? 37.894 5.434   -26.388 1.00 21.11  ? 618 LEU A CB  1 
ATOM   3501 C CG  . LEU A 1 485 ? 39.154 5.536   -25.528 1.00 23.34  ? 618 LEU A CG  1 
ATOM   3502 C CD1 . LEU A 1 485 ? 39.699 4.135   -25.271 1.00 22.00  ? 618 LEU A CD1 1 
ATOM   3503 C CD2 . LEU A 1 485 ? 40.193 6.408   -26.237 1.00 23.37  ? 618 LEU A CD2 1 
ATOM   3504 N N   . CYS A 1 486 ? 35.022 6.160   -27.508 1.00 22.24  ? 619 CYS A N   1 
ATOM   3505 C CA  . CYS A 1 486 ? 33.955 5.952   -28.477 1.00 21.31  ? 619 CYS A CA  1 
ATOM   3506 C C   . CYS A 1 486 ? 33.589 7.271   -29.169 1.00 22.47  ? 619 CYS A C   1 
ATOM   3507 O O   . CYS A 1 486 ? 33.486 7.329   -30.400 1.00 21.90  ? 619 CYS A O   1 
ATOM   3508 C CB  . CYS A 1 486 ? 32.721 5.365   -27.778 1.00 21.74  ? 619 CYS A CB  1 
ATOM   3509 S SG  . CYS A 1 486 ? 31.289 5.116   -28.857 1.00 22.70  ? 619 CYS A SG  1 
ATOM   3510 N N   . GLU A 1 487 ? 33.398 8.328   -28.382 1.00 20.61  ? 620 GLU A N   1 
ATOM   3511 C CA  . GLU A 1 487 ? 33.059 9.635   -28.953 1.00 22.40  ? 620 GLU A CA  1 
ATOM   3512 C C   . GLU A 1 487 ? 34.192 10.133  -29.853 1.00 21.73  ? 620 GLU A C   1 
ATOM   3513 O O   . GLU A 1 487 ? 33.950 10.645  -30.950 1.00 20.64  ? 620 GLU A O   1 
ATOM   3514 C CB  . GLU A 1 487 ? 32.803 10.664  -27.843 1.00 19.71  ? 620 GLU A CB  1 
ATOM   3515 C CG  . GLU A 1 487 ? 31.570 10.391  -26.984 1.00 23.03  ? 620 GLU A CG  1 
ATOM   3516 C CD  . GLU A 1 487 ? 30.257 10.539  -27.747 1.00 25.19  ? 620 GLU A CD  1 
ATOM   3517 O OE1 . GLU A 1 487 ? 30.280 10.987  -28.916 1.00 26.44  ? 620 GLU A OE1 1 
ATOM   3518 O OE2 . GLU A 1 487 ? 29.196 10.209  -27.173 1.00 25.30  ? 620 GLU A OE2 1 
ATOM   3519 N N   . LEU A 1 488 ? 35.428 9.983   -29.384 1.00 23.05  ? 621 LEU A N   1 
ATOM   3520 C CA  . LEU A 1 488 ? 36.595 10.425  -30.142 1.00 24.07  ? 621 LEU A CA  1 
ATOM   3521 C C   . LEU A 1 488 ? 36.739 9.639   -31.436 1.00 26.36  ? 621 LEU A C   1 
ATOM   3522 O O   . LEU A 1 488 ? 37.185 10.176  -32.455 1.00 25.82  ? 621 LEU A O   1 
ATOM   3523 C CB  . LEU A 1 488 ? 37.872 10.256  -29.312 1.00 22.04  ? 621 LEU A CB  1 
ATOM   3524 C CG  . LEU A 1 488 ? 38.100 11.202  -28.128 1.00 26.31  ? 621 LEU A CG  1 
ATOM   3525 C CD1 . LEU A 1 488 ? 39.308 10.732  -27.313 1.00 24.90  ? 621 LEU A CD1 1 
ATOM   3526 C CD2 . LEU A 1 488 ? 38.309 12.624  -28.643 1.00 23.25  ? 621 LEU A CD2 1 
ATOM   3527 N N   . ALA A 1 489 ? 36.355 8.365   -31.383 1.00 25.26  ? 622 ALA A N   1 
ATOM   3528 C CA  . ALA A 1 489 ? 36.448 7.472   -32.524 1.00 25.42  ? 622 ALA A CA  1 
ATOM   3529 C C   . ALA A 1 489 ? 35.461 7.794   -33.649 1.00 27.37  ? 622 ALA A C   1 
ATOM   3530 O O   . ALA A 1 489 ? 35.563 7.224   -34.737 1.00 25.95  ? 622 ALA A O   1 
ATOM   3531 C CB  . ALA A 1 489 ? 36.264 6.021   -32.060 1.00 25.94  ? 622 ALA A CB  1 
ATOM   3532 N N   . GLN A 1 490 ? 34.507 8.692   -33.405 1.00 26.80  ? 623 GLN A N   1 
ATOM   3533 C CA  . GLN A 1 490 ? 33.561 9.036   -34.463 1.00 28.14  ? 623 GLN A CA  1 
ATOM   3534 C C   . GLN A 1 490 ? 34.260 9.847   -35.554 1.00 28.90  ? 623 GLN A C   1 
ATOM   3535 O O   . GLN A 1 490 ? 33.695 10.062  -36.625 1.00 29.21  ? 623 GLN A O   1 
ATOM   3536 C CB  . GLN A 1 490 ? 32.365 9.821   -33.914 1.00 28.01  ? 623 GLN A CB  1 
ATOM   3537 C CG  . GLN A 1 490 ? 32.696 11.206  -33.424 1.00 30.11  ? 623 GLN A CG  1 
ATOM   3538 C CD  . GLN A 1 490 ? 31.526 11.852  -32.714 1.00 30.81  ? 623 GLN A CD  1 
ATOM   3539 O OE1 . GLN A 1 490 ? 30.601 12.351  -33.347 1.00 30.13  ? 623 GLN A OE1 1 
ATOM   3540 N NE2 . GLN A 1 490 ? 31.558 11.834  -31.384 1.00 29.43  ? 623 GLN A NE2 1 
ATOM   3541 N N   . ASP A 1 491 ? 35.478 10.314  -35.270 1.00 28.46  ? 624 ASP A N   1 
ATOM   3542 C CA  . ASP A 1 491 ? 36.263 11.062  -36.256 1.00 30.69  ? 624 ASP A CA  1 
ATOM   3543 C C   . ASP A 1 491 ? 37.324 10.098  -36.789 1.00 31.83  ? 624 ASP A C   1 
ATOM   3544 O O   . ASP A 1 491 ? 38.091 9.523   -36.017 1.00 30.68  ? 624 ASP A O   1 
ATOM   3545 C CB  . ASP A 1 491 ? 36.945 12.290  -35.631 1.00 29.78  ? 624 ASP A CB  1 
ATOM   3546 C CG  . ASP A 1 491 ? 35.947 13.334  -35.135 1.00 29.91  ? 624 ASP A CG  1 
ATOM   3547 O OD1 . ASP A 1 491 ? 34.883 13.505  -35.764 1.00 31.21  ? 624 ASP A OD1 1 
ATOM   3548 O OD2 . ASP A 1 491 ? 36.236 13.999  -34.124 1.00 27.16  ? 624 ASP A OD2 1 
ATOM   3549 N N   . LYS A 1 492 ? 37.361 9.931   -38.107 1.00 33.89  ? 625 LYS A N   1 
ATOM   3550 C CA  . LYS A 1 492 ? 38.291 9.012   -38.764 1.00 38.07  ? 625 LYS A CA  1 
ATOM   3551 C C   . LYS A 1 492 ? 39.734 9.011   -38.266 1.00 37.40  ? 625 LYS A C   1 
ATOM   3552 O O   . LYS A 1 492 ? 40.276 7.955   -37.941 1.00 36.86  ? 625 LYS A O   1 
ATOM   3553 C CB  . LYS A 1 492 ? 38.290 9.254   -40.276 1.00 41.01  ? 625 LYS A CB  1 
ATOM   3554 C CG  . LYS A 1 492 ? 36.940 9.042   -40.950 1.00 46.82  ? 625 LYS A CG  1 
ATOM   3555 C CD  . LYS A 1 492 ? 36.470 7.595   -40.868 1.00 50.14  ? 625 LYS A CD  1 
ATOM   3556 C CE  . LYS A 1 492 ? 35.164 7.406   -41.638 1.00 52.30  ? 625 LYS A CE  1 
ATOM   3557 N NZ  . LYS A 1 492 ? 34.668 6.003   -41.585 1.00 53.64  ? 625 LYS A NZ  1 
ATOM   3558 N N   . GLU A 1 493 ? 40.360 10.182  -38.218 1.00 38.40  ? 626 GLU A N   1 
ATOM   3559 C CA  . GLU A 1 493 ? 41.746 10.272  -37.772 1.00 39.10  ? 626 GLU A CA  1 
ATOM   3560 C C   . GLU A 1 493 ? 41.936 9.817   -36.334 1.00 37.66  ? 626 GLU A C   1 
ATOM   3561 O O   . GLU A 1 493 ? 42.882 9.091   -36.023 1.00 36.20  ? 626 GLU A O   1 
ATOM   3562 C CB  . GLU A 1 493 ? 42.270 11.702  -37.920 1.00 43.60  ? 626 GLU A CB  1 
ATOM   3563 C CG  . GLU A 1 493 ? 42.459 12.147  -39.359 1.00 49.84  ? 626 GLU A CG  1 
ATOM   3564 C CD  . GLU A 1 493 ? 43.266 13.430  -39.475 1.00 54.39  ? 626 GLU A CD  1 
ATOM   3565 O OE1 . GLU A 1 493 ? 43.513 13.876  -40.617 1.00 57.22  ? 626 GLU A OE1 1 
ATOM   3566 O OE2 . GLU A 1 493 ? 43.657 13.990  -38.426 1.00 57.07  ? 626 GLU A OE2 1 
ATOM   3567 N N   . ALA A 1 494 ? 41.038 10.246  -35.456 1.00 34.64  ? 627 ALA A N   1 
ATOM   3568 C CA  . ALA A 1 494 ? 41.130 9.878   -34.053 1.00 31.94  ? 627 ALA A CA  1 
ATOM   3569 C C   . ALA A 1 494 ? 40.972 8.369   -33.884 1.00 30.62  ? 627 ALA A C   1 
ATOM   3570 O O   . ALA A 1 494 ? 41.639 7.759   -33.047 1.00 30.57  ? 627 ALA A O   1 
ATOM   3571 C CB  . ALA A 1 494 ? 40.065 10.619  -33.248 1.00 31.43  ? 627 ALA A CB  1 
ATOM   3572 N N   . ALA A 1 495 ? 40.089 7.766   -34.675 1.00 29.94  ? 628 ALA A N   1 
ATOM   3573 C CA  . ALA A 1 495 ? 39.876 6.326   -34.590 1.00 30.90  ? 628 ALA A CA  1 
ATOM   3574 C C   . ALA A 1 495 ? 41.181 5.598   -34.922 1.00 33.18  ? 628 ALA A C   1 
ATOM   3575 O O   . ALA A 1 495 ? 41.529 4.599   -34.285 1.00 32.99  ? 628 ALA A O   1 
ATOM   3576 C CB  . ALA A 1 495 ? 38.772 5.899   -35.545 1.00 30.84  ? 628 ALA A CB  1 
ATOM   3577 N N   . GLU A 1 496 ? 41.909 6.108   -35.913 1.00 33.90  ? 629 GLU A N   1 
ATOM   3578 C CA  . GLU A 1 496 ? 43.179 5.501   -36.300 1.00 35.12  ? 629 GLU A CA  1 
ATOM   3579 C C   . GLU A 1 496 ? 44.209 5.640   -35.186 1.00 33.66  ? 629 GLU A C   1 
ATOM   3580 O O   . GLU A 1 496 ? 44.919 4.688   -34.868 1.00 33.05  ? 629 GLU A O   1 
ATOM   3581 C CB  . GLU A 1 496 ? 43.704 6.141   -37.586 1.00 37.99  ? 629 GLU A CB  1 
ATOM   3582 C CG  . GLU A 1 496 ? 42.969 5.673   -38.829 1.00 44.63  ? 629 GLU A CG  1 
ATOM   3583 C CD  . GLU A 1 496 ? 43.371 6.436   -40.076 1.00 50.05  ? 629 GLU A CD  1 
ATOM   3584 O OE1 . GLU A 1 496 ? 44.587 6.506   -40.372 1.00 52.59  ? 629 GLU A OE1 1 
ATOM   3585 O OE2 . GLU A 1 496 ? 42.466 6.963   -40.761 1.00 51.92  ? 629 GLU A OE2 1 
ATOM   3586 N N   . ALA A 1 497 ? 44.276 6.826   -34.586 1.00 32.42  ? 630 ALA A N   1 
ATOM   3587 C CA  . ALA A 1 497 ? 45.213 7.083   -33.497 1.00 32.24  ? 630 ALA A CA  1 
ATOM   3588 C C   . ALA A 1 497 ? 44.925 6.200   -32.281 1.00 31.87  ? 630 ALA A C   1 
ATOM   3589 O O   . ALA A 1 497 ? 45.843 5.787   -31.574 1.00 32.15  ? 630 ALA A O   1 
ATOM   3590 C CB  . ALA A 1 497 ? 45.155 8.553   -33.097 1.00 32.92  ? 630 ALA A CB  1 
ATOM   3591 N N   . ILE A 1 498 ? 43.649 5.922   -32.026 1.00 29.92  ? 631 ILE A N   1 
ATOM   3592 C CA  . ILE A 1 498 ? 43.281 5.079   -30.895 1.00 29.38  ? 631 ILE A CA  1 
ATOM   3593 C C   . ILE A 1 498 ? 43.775 3.653   -31.144 1.00 30.78  ? 631 ILE A C   1 
ATOM   3594 O O   . ILE A 1 498 ? 44.278 2.990   -30.239 1.00 30.38  ? 631 ILE A O   1 
ATOM   3595 C CB  . ILE A 1 498 ? 41.755 5.062   -30.687 1.00 27.32  ? 631 ILE A CB  1 
ATOM   3596 C CG1 . ILE A 1 498 ? 41.285 6.447   -30.232 1.00 25.81  ? 631 ILE A CG1 1 
ATOM   3597 C CG2 . ILE A 1 498 ? 41.378 3.989   -29.667 1.00 25.69  ? 631 ILE A CG2 1 
ATOM   3598 C CD1 . ILE A 1 498 ? 39.786 6.621   -30.249 1.00 24.49  ? 631 ILE A CD1 1 
ATOM   3599 N N   . GLU A 1 499 ? 43.634 3.184   -32.377 1.00 32.65  ? 632 GLU A N   1 
ATOM   3600 C CA  . GLU A 1 499 ? 44.090 1.843   -32.714 1.00 36.57  ? 632 GLU A CA  1 
ATOM   3601 C C   . GLU A 1 499 ? 45.615 1.782   -32.601 1.00 36.46  ? 632 GLU A C   1 
ATOM   3602 O O   . GLU A 1 499 ? 46.173 0.787   -32.141 1.00 35.63  ? 632 GLU A O   1 
ATOM   3603 C CB  . GLU A 1 499 ? 43.661 1.470   -34.134 1.00 37.41  ? 632 GLU A CB  1 
ATOM   3604 C CG  . GLU A 1 499 ? 44.011 0.038   -34.507 1.00 41.80  ? 632 GLU A CG  1 
ATOM   3605 C CD  . GLU A 1 499 ? 43.567 -0.330  -35.906 1.00 44.11  ? 632 GLU A CD  1 
ATOM   3606 O OE1 . GLU A 1 499 ? 44.003 0.344   -36.863 1.00 43.70  ? 632 GLU A OE1 1 
ATOM   3607 O OE2 . GLU A 1 499 ? 42.785 -1.297  -36.045 1.00 46.18  ? 632 GLU A OE2 1 
ATOM   3608 N N   . ALA A 1 500 ? 46.275 2.860   -33.014 1.00 37.18  ? 633 ALA A N   1 
ATOM   3609 C CA  . ALA A 1 500 ? 47.732 2.948   -32.966 1.00 38.74  ? 633 ALA A CA  1 
ATOM   3610 C C   . ALA A 1 500 ? 48.244 2.847   -31.530 1.00 38.89  ? 633 ALA A C   1 
ATOM   3611 O O   . ALA A 1 500 ? 49.420 2.560   -31.301 1.00 38.00  ? 633 ALA A O   1 
ATOM   3612 C CB  . ALA A 1 500 ? 48.199 4.264   -33.599 1.00 38.38  ? 633 ALA A CB  1 
ATOM   3613 N N   . GLU A 1 501 ? 47.354 3.082   -30.569 1.00 37.84  ? 634 GLU A N   1 
ATOM   3614 C CA  . GLU A 1 501 ? 47.710 3.017   -29.158 1.00 38.09  ? 634 GLU A CA  1 
ATOM   3615 C C   . GLU A 1 501 ? 47.477 1.643   -28.545 1.00 37.15  ? 634 GLU A C   1 
ATOM   3616 O O   . GLU A 1 501 ? 47.532 1.486   -27.327 1.00 38.68  ? 634 GLU A O   1 
ATOM   3617 C CB  . GLU A 1 501 ? 46.921 4.059   -28.364 1.00 41.32  ? 634 GLU A CB  1 
ATOM   3618 C CG  . GLU A 1 501 ? 47.403 5.481   -28.563 1.00 45.49  ? 634 GLU A CG  1 
ATOM   3619 C CD  . GLU A 1 501 ? 48.830 5.670   -28.099 1.00 47.93  ? 634 GLU A CD  1 
ATOM   3620 O OE1 . GLU A 1 501 ? 49.142 5.254   -26.963 1.00 50.82  ? 634 GLU A OE1 1 
ATOM   3621 O OE2 . GLU A 1 501 ? 49.636 6.238   -28.864 1.00 49.50  ? 634 GLU A OE2 1 
ATOM   3622 N N   . GLY A 1 502 ? 47.210 0.651   -29.386 1.00 36.22  ? 635 GLY A N   1 
ATOM   3623 C CA  . GLY A 1 502 ? 46.983 -0.694  -28.890 1.00 36.16  ? 635 GLY A CA  1 
ATOM   3624 C C   . GLY A 1 502 ? 45.740 -0.835  -28.029 1.00 35.87  ? 635 GLY A C   1 
ATOM   3625 O O   . GLY A 1 502 ? 45.733 -1.591  -27.055 1.00 36.10  ? 635 GLY A O   1 
ATOM   3626 N N   . ALA A 1 503 ? 44.683 -0.113  -28.389 1.00 34.48  ? 636 ALA A N   1 
ATOM   3627 C CA  . ALA A 1 503 ? 43.429 -0.165  -27.642 1.00 32.94  ? 636 ALA A CA  1 
ATOM   3628 C C   . ALA A 1 503 ? 42.638 -1.452  -27.899 1.00 31.00  ? 636 ALA A C   1 
ATOM   3629 O O   . ALA A 1 503 ? 41.857 -1.885  -27.055 1.00 29.04  ? 636 ALA A O   1 
ATOM   3630 C CB  . ALA A 1 503 ? 42.568 1.047   -27.992 1.00 32.35  ? 636 ALA A CB  1 
ATOM   3631 N N   . THR A 1 504 ? 42.851 -2.063  -29.059 1.00 32.00  ? 637 THR A N   1 
ATOM   3632 C CA  . THR A 1 504 ? 42.135 -3.281  -29.441 1.00 32.94  ? 637 THR A CA  1 
ATOM   3633 C C   . THR A 1 504 ? 42.090 -4.378  -28.377 1.00 33.09  ? 637 THR A C   1 
ATOM   3634 O O   . THR A 1 504 ? 41.017 -4.888  -28.054 1.00 33.37  ? 637 THR A O   1 
ATOM   3635 C CB  . THR A 1 504 ? 42.720 -3.884  -30.737 1.00 36.00  ? 637 THR A CB  1 
ATOM   3636 O OG1 . THR A 1 504 ? 42.768 -2.875  -31.753 1.00 36.58  ? 637 THR A OG1 1 
ATOM   3637 C CG2 . THR A 1 504 ? 41.850 -5.040  -31.230 1.00 34.83  ? 637 THR A CG2 1 
ATOM   3638 N N   . ALA A 1 505 ? 43.244 -4.740  -27.825 1.00 32.18  ? 638 ALA A N   1 
ATOM   3639 C CA  . ALA A 1 505 ? 43.289 -5.793  -26.816 1.00 32.37  ? 638 ALA A CA  1 
ATOM   3640 C C   . ALA A 1 505 ? 42.451 -5.462  -25.578 1.00 31.20  ? 638 ALA A C   1 
ATOM   3641 O O   . ALA A 1 505 ? 41.545 -6.217  -25.208 1.00 30.39  ? 638 ALA A O   1 
ATOM   3642 C CB  . ALA A 1 505 ? 44.746 -6.086  -26.415 1.00 31.95  ? 638 ALA A CB  1 
ATOM   3643 N N   . PRO A 1 506 ? 42.744 -4.335  -24.910 1.00 30.69  ? 639 PRO A N   1 
ATOM   3644 C CA  . PRO A 1 506 ? 41.933 -4.030  -23.729 1.00 29.86  ? 639 PRO A CA  1 
ATOM   3645 C C   . PRO A 1 506 ? 40.436 -3.878  -24.041 1.00 29.41  ? 639 PRO A C   1 
ATOM   3646 O O   . PRO A 1 506 ? 39.588 -4.251  -23.225 1.00 28.33  ? 639 PRO A O   1 
ATOM   3647 C CB  . PRO A 1 506 ? 42.583 -2.753  -23.176 1.00 30.92  ? 639 PRO A CB  1 
ATOM   3648 C CG  . PRO A 1 506 ? 43.247 -2.139  -24.371 1.00 29.48  ? 639 PRO A CG  1 
ATOM   3649 C CD  . PRO A 1 506 ? 43.808 -3.333  -25.101 1.00 30.92  ? 639 PRO A CD  1 
ATOM   3650 N N   . LEU A 1 507 ? 40.111 -3.352  -25.221 1.00 28.53  ? 640 LEU A N   1 
ATOM   3651 C CA  . LEU A 1 507 ? 38.713 -3.182  -25.615 1.00 29.30  ? 640 LEU A CA  1 
ATOM   3652 C C   . LEU A 1 507 ? 38.054 -4.541  -25.809 1.00 30.31  ? 640 LEU A C   1 
ATOM   3653 O O   . LEU A 1 507 ? 36.897 -4.746  -25.441 1.00 29.60  ? 640 LEU A O   1 
ATOM   3654 C CB  . LEU A 1 507 ? 38.608 -2.378  -26.916 1.00 29.62  ? 640 LEU A CB  1 
ATOM   3655 C CG  . LEU A 1 507 ? 38.957 -0.886  -26.838 1.00 28.52  ? 640 LEU A CG  1 
ATOM   3656 C CD1 . LEU A 1 507 ? 39.010 -0.293  -28.233 1.00 27.56  ? 640 LEU A CD1 1 
ATOM   3657 C CD2 . LEU A 1 507 ? 37.919 -0.166  -25.987 1.00 28.47  ? 640 LEU A CD2 1 
ATOM   3658 N N   . THR A 1 508 ? 38.800 -5.471  -26.394 1.00 30.98  ? 641 THR A N   1 
ATOM   3659 C CA  . THR A 1 508 ? 38.288 -6.811  -26.628 1.00 31.11  ? 641 THR A CA  1 
ATOM   3660 C C   . THR A 1 508 ? 37.920 -7.473  -25.305 1.00 29.92  ? 641 THR A C   1 
ATOM   3661 O O   . THR A 1 508 ? 36.898 -8.148  -25.206 1.00 30.26  ? 641 THR A O   1 
ATOM   3662 C CB  . THR A 1 508 ? 39.325 -7.665  -27.381 1.00 32.85  ? 641 THR A CB  1 
ATOM   3663 O OG1 . THR A 1 508 ? 39.567 -7.079  -28.668 1.00 32.63  ? 641 THR A OG1 1 
ATOM   3664 C CG2 . THR A 1 508 ? 38.819 -9.093  -27.565 1.00 32.92  ? 641 THR A CG2 1 
ATOM   3665 N N   . GLU A 1 509 ? 38.746 -7.270  -24.284 1.00 30.62  ? 642 GLU A N   1 
ATOM   3666 C CA  . GLU A 1 509 ? 38.479 -7.845  -22.969 1.00 30.88  ? 642 GLU A CA  1 
ATOM   3667 C C   . GLU A 1 509 ? 37.188 -7.299  -22.364 1.00 30.74  ? 642 GLU A C   1 
ATOM   3668 O O   . GLU A 1 509 ? 36.474 -8.005  -21.650 1.00 29.54  ? 642 GLU A O   1 
ATOM   3669 C CB  . GLU A 1 509 ? 39.649 -7.562  -22.021 1.00 35.65  ? 642 GLU A CB  1 
ATOM   3670 C CG  . GLU A 1 509 ? 40.848 -8.473  -22.228 1.00 39.53  ? 642 GLU A CG  1 
ATOM   3671 C CD  . GLU A 1 509 ? 40.536 -9.919  -21.877 1.00 42.71  ? 642 GLU A CD  1 
ATOM   3672 O OE1 . GLU A 1 509 ? 40.253 -10.204 -20.691 1.00 44.78  ? 642 GLU A OE1 1 
ATOM   3673 O OE2 . GLU A 1 509 ? 40.569 -10.769 -22.788 1.00 45.30  ? 642 GLU A OE2 1 
ATOM   3674 N N   . LEU A 1 510 ? 36.886 -6.038  -22.653 1.00 27.87  ? 643 LEU A N   1 
ATOM   3675 C CA  . LEU A 1 510 ? 35.685 -5.414  -22.122 1.00 28.00  ? 643 LEU A CA  1 
ATOM   3676 C C   . LEU A 1 510 ? 34.403 -5.911  -22.791 1.00 26.93  ? 643 LEU A C   1 
ATOM   3677 O O   . LEU A 1 510 ? 33.308 -5.679  -22.285 1.00 25.96  ? 643 LEU A O   1 
ATOM   3678 C CB  . LEU A 1 510 ? 35.786 -3.889  -22.257 1.00 26.29  ? 643 LEU A CB  1 
ATOM   3679 C CG  . LEU A 1 510 ? 36.886 -3.245  -21.409 1.00 26.03  ? 643 LEU A CG  1 
ATOM   3680 C CD1 . LEU A 1 510 ? 36.944 -1.747  -21.687 1.00 25.07  ? 643 LEU A CD1 1 
ATOM   3681 C CD2 . LEU A 1 510 ? 36.609 -3.515  -19.931 1.00 24.80  ? 643 LEU A CD2 1 
ATOM   3682 N N   . LEU A 1 511 ? 34.537 -6.598  -23.920 1.00 29.33  ? 644 LEU A N   1 
ATOM   3683 C CA  . LEU A 1 511 ? 33.369 -7.106  -24.631 1.00 29.63  ? 644 LEU A CA  1 
ATOM   3684 C C   . LEU A 1 511 ? 32.503 -8.059  -23.811 1.00 31.77  ? 644 LEU A C   1 
ATOM   3685 O O   . LEU A 1 511 ? 31.305 -8.158  -24.063 1.00 32.49  ? 644 LEU A O   1 
ATOM   3686 C CB  . LEU A 1 511 ? 33.786 -7.791  -25.931 1.00 30.96  ? 644 LEU A CB  1 
ATOM   3687 C CG  . LEU A 1 511 ? 34.398 -6.892  -27.005 1.00 32.31  ? 644 LEU A CG  1 
ATOM   3688 C CD1 . LEU A 1 511 ? 34.821 -7.740  -28.198 1.00 32.03  ? 644 LEU A CD1 1 
ATOM   3689 C CD2 . LEU A 1 511 ? 33.385 -5.822  -27.429 1.00 31.52  ? 644 LEU A CD2 1 
ATOM   3690 N N   . HIS A 1 512 ? 33.084 -8.763  -22.839 1.00 33.26  ? 645 HIS A N   1 
ATOM   3691 C CA  . HIS A 1 512 ? 32.266 -9.671  -22.033 1.00 34.12  ? 645 HIS A CA  1 
ATOM   3692 C C   . HIS A 1 512 ? 31.901 -9.103  -20.666 1.00 35.14  ? 645 HIS A C   1 
ATOM   3693 O O   . HIS A 1 512 ? 31.509 -9.838  -19.759 1.00 37.21  ? 645 HIS A O   1 
ATOM   3694 C CB  . HIS A 1 512 ? 32.925 -11.058 -21.874 1.00 33.60  ? 645 HIS A CB  1 
ATOM   3695 C CG  . HIS A 1 512 ? 34.262 -11.046 -21.198 1.00 31.54  ? 645 HIS A CG  1 
ATOM   3696 N ND1 . HIS A 1 512 ? 35.450 -10.991 -21.897 1.00 31.94  ? 645 HIS A ND1 1 
ATOM   3697 C CD2 . HIS A 1 512 ? 34.601 -11.124 -19.889 1.00 31.60  ? 645 HIS A CD2 1 
ATOM   3698 C CE1 . HIS A 1 512 ? 36.462 -11.038 -21.049 1.00 31.69  ? 645 HIS A CE1 1 
ATOM   3699 N NE2 . HIS A 1 512 ? 35.974 -11.119 -19.824 1.00 32.26  ? 645 HIS A NE2 1 
ATOM   3700 N N   . SER A 1 513 ? 32.022 -7.786  -20.527 1.00 34.29  ? 646 SER A N   1 
ATOM   3701 C CA  . SER A 1 513 ? 31.680 -7.114  -19.280 1.00 33.23  ? 646 SER A CA  1 
ATOM   3702 C C   . SER A 1 513 ? 30.190 -7.275  -18.986 1.00 34.51  ? 646 SER A C   1 
ATOM   3703 O O   . SER A 1 513 ? 29.373 -7.360  -19.908 1.00 34.35  ? 646 SER A O   1 
ATOM   3704 C CB  . SER A 1 513 ? 32.011 -5.622  -19.377 1.00 32.53  ? 646 SER A CB  1 
ATOM   3705 O OG  . SER A 1 513 ? 31.494 -4.918  -18.258 1.00 31.83  ? 646 SER A OG  1 
ATOM   3706 N N   . ARG A 1 514 ? 29.842 -7.321  -17.703 1.00 36.31  ? 647 ARG A N   1 
ATOM   3707 C CA  . ARG A 1 514 ? 28.448 -7.443  -17.286 1.00 39.28  ? 647 ARG A CA  1 
ATOM   3708 C C   . ARG A 1 514 ? 27.748 -6.108  -17.493 1.00 38.64  ? 647 ARG A C   1 
ATOM   3709 O O   . ARG A 1 514 ? 26.522 -6.045  -17.577 1.00 39.54  ? 647 ARG A O   1 
ATOM   3710 C CB  . ARG A 1 514 ? 28.355 -7.816  -15.803 1.00 42.19  ? 647 ARG A CB  1 
ATOM   3711 C CG  . ARG A 1 514 ? 28.677 -9.267  -15.476 1.00 47.48  ? 647 ARG A CG  1 
ATOM   3712 C CD  . ARG A 1 514 ? 27.587 -10.209 -15.950 1.00 48.96  ? 647 ARG A CD  1 
ATOM   3713 N NE  . ARG A 1 514 ? 27.862 -11.593 -15.569 1.00 49.94  ? 647 ARG A NE  1 
ATOM   3714 C CZ  . ARG A 1 514 ? 27.856 -12.045 -14.318 1.00 50.10  ? 647 ARG A CZ  1 
ATOM   3715 N NH1 . ARG A 1 514 ? 27.589 -11.223 -13.314 1.00 49.90  ? 647 ARG A NH1 1 
ATOM   3716 N NH2 . ARG A 1 514 ? 28.114 -13.326 -14.072 1.00 50.68  ? 647 ARG A NH2 1 
ATOM   3717 N N   . ASN A 1 515 ? 28.540 -5.043  -17.562 1.00 37.89  ? 648 ASN A N   1 
ATOM   3718 C CA  . ASN A 1 515 ? 28.023 -3.691  -17.749 1.00 37.35  ? 648 ASN A CA  1 
ATOM   3719 C C   . ASN A 1 515 ? 27.756 -3.435  -19.233 1.00 37.78  ? 648 ASN A C   1 
ATOM   3720 O O   . ASN A 1 515 ? 28.692 -3.313  -20.028 1.00 35.32  ? 648 ASN A O   1 
ATOM   3721 C CB  . ASN A 1 515 ? 29.043 -2.679  -17.209 1.00 38.42  ? 648 ASN A CB  1 
ATOM   3722 C CG  . ASN A 1 515 ? 28.532 -1.247  -17.240 1.00 37.95  ? 648 ASN A CG  1 
ATOM   3723 O OD1 . ASN A 1 515 ? 28.161 -0.727  -18.290 1.00 36.23  ? 648 ASN A OD1 1 
ATOM   3724 N ND2 . ASN A 1 515 ? 28.524 -0.602  -16.082 1.00 39.92  ? 648 ASN A ND2 1 
ATOM   3725 N N   . GLU A 1 516 ? 26.480 -3.357  -19.605 1.00 37.93  ? 649 GLU A N   1 
ATOM   3726 C CA  . GLU A 1 516 ? 26.114 -3.124  -20.998 1.00 38.73  ? 649 GLU A CA  1 
ATOM   3727 C C   . GLU A 1 516 ? 26.808 -1.907  -21.583 1.00 37.15  ? 649 GLU A C   1 
ATOM   3728 O O   . GLU A 1 516 ? 27.263 -1.938  -22.732 1.00 37.19  ? 649 GLU A O   1 
ATOM   3729 C CB  . GLU A 1 516 ? 24.605 -2.954  -21.146 1.00 42.52  ? 649 GLU A CB  1 
ATOM   3730 C CG  . GLU A 1 516 ? 23.839 -4.255  -21.162 1.00 49.01  ? 649 GLU A CG  1 
ATOM   3731 C CD  . GLU A 1 516 ? 22.473 -4.101  -21.798 1.00 53.57  ? 649 GLU A CD  1 
ATOM   3732 O OE1 . GLU A 1 516 ? 21.656 -3.311  -21.271 1.00 56.22  ? 649 GLU A OE1 1 
ATOM   3733 O OE2 . GLU A 1 516 ? 22.222 -4.765  -22.828 1.00 54.78  ? 649 GLU A OE2 1 
ATOM   3734 N N   . GLY A 1 517 ? 26.879 -0.836  -20.796 1.00 33.80  ? 650 GLY A N   1 
ATOM   3735 C CA  . GLY A 1 517 ? 27.532 0.375   -21.258 1.00 30.37  ? 650 GLY A CA  1 
ATOM   3736 C C   . GLY A 1 517 ? 28.970 0.096   -21.653 1.00 28.21  ? 650 GLY A C   1 
ATOM   3737 O O   . GLY A 1 517 ? 29.402 0.444   -22.756 1.00 26.15  ? 650 GLY A O   1 
ATOM   3738 N N   . VAL A 1 518 ? 29.719 -0.529  -20.748 1.00 25.99  ? 651 VAL A N   1 
ATOM   3739 C CA  . VAL A 1 518 ? 31.112 -0.864  -21.023 1.00 24.49  ? 651 VAL A CA  1 
ATOM   3740 C C   . VAL A 1 518 ? 31.211 -1.702  -22.298 1.00 24.34  ? 651 VAL A C   1 
ATOM   3741 O O   . VAL A 1 518 ? 31.962 -1.368  -23.213 1.00 24.37  ? 651 VAL A O   1 
ATOM   3742 C CB  . VAL A 1 518 ? 31.744 -1.653  -19.849 1.00 24.27  ? 651 VAL A CB  1 
ATOM   3743 C CG1 . VAL A 1 518 ? 33.124 -2.183  -20.245 1.00 23.51  ? 651 VAL A CG1 1 
ATOM   3744 C CG2 . VAL A 1 518 ? 31.864 -0.751  -18.630 1.00 21.89  ? 651 VAL A CG2 1 
ATOM   3745 N N   . ALA A 1 519 ? 30.435 -2.779  -22.362 1.00 23.95  ? 652 ALA A N   1 
ATOM   3746 C CA  . ALA A 1 519 ? 30.454 -3.666  -23.523 1.00 24.23  ? 652 ALA A CA  1 
ATOM   3747 C C   . ALA A 1 519 ? 30.070 -2.959  -24.818 1.00 23.43  ? 652 ALA A C   1 
ATOM   3748 O O   . ALA A 1 519 ? 30.658 -3.214  -25.871 1.00 21.90  ? 652 ALA A O   1 
ATOM   3749 C CB  . ALA A 1 519 ? 29.523 -4.867  -23.285 1.00 23.06  ? 652 ALA A CB  1 
ATOM   3750 N N   . THR A 1 520 ? 29.080 -2.074  -24.749 1.00 22.18  ? 653 THR A N   1 
ATOM   3751 C CA  . THR A 1 520 ? 28.643 -1.361  -25.947 1.00 22.29  ? 653 THR A CA  1 
ATOM   3752 C C   . THR A 1 520 ? 29.682 -0.349  -26.426 1.00 20.85  ? 653 THR A C   1 
ATOM   3753 O O   . THR A 1 520 ? 30.017 -0.319  -27.608 1.00 21.34  ? 653 THR A O   1 
ATOM   3754 C CB  . THR A 1 520 ? 27.304 -0.626  -25.712 1.00 22.64  ? 653 THR A CB  1 
ATOM   3755 O OG1 . THR A 1 520 ? 26.308 -1.569  -25.289 1.00 25.48  ? 653 THR A OG1 1 
ATOM   3756 C CG2 . THR A 1 520 ? 26.832 0.036   -27.000 1.00 24.94  ? 653 THR A CG2 1 
ATOM   3757 N N   . TYR A 1 521 ? 30.196 0.479   -25.520 1.00 20.19  ? 654 TYR A N   1 
ATOM   3758 C CA  . TYR A 1 521 ? 31.197 1.469   -25.924 1.00 21.24  ? 654 TYR A CA  1 
ATOM   3759 C C   . TYR A 1 521 ? 32.450 0.792   -26.490 1.00 21.52  ? 654 TYR A C   1 
ATOM   3760 O O   . TYR A 1 521 ? 32.993 1.227   -27.504 1.00 21.82  ? 654 TYR A O   1 
ATOM   3761 C CB  . TYR A 1 521 ? 31.589 2.374   -24.748 1.00 19.72  ? 654 TYR A CB  1 
ATOM   3762 C CG  . TYR A 1 521 ? 30.504 3.336   -24.289 1.00 19.92  ? 654 TYR A CG  1 
ATOM   3763 C CD1 . TYR A 1 521 ? 29.705 4.015   -25.211 1.00 21.67  ? 654 TYR A CD1 1 
ATOM   3764 C CD2 . TYR A 1 521 ? 30.298 3.586   -22.934 1.00 19.64  ? 654 TYR A CD2 1 
ATOM   3765 C CE1 . TYR A 1 521 ? 28.725 4.922   -24.791 1.00 21.73  ? 654 TYR A CE1 1 
ATOM   3766 C CE2 . TYR A 1 521 ? 29.322 4.488   -22.504 1.00 22.39  ? 654 TYR A CE2 1 
ATOM   3767 C CZ  . TYR A 1 521 ? 28.540 5.152   -23.437 1.00 20.58  ? 654 TYR A CZ  1 
ATOM   3768 O OH  . TYR A 1 521 ? 27.574 6.041   -23.014 1.00 22.47  ? 654 TYR A OH  1 
ATOM   3769 N N   . ALA A 1 522 ? 32.905 -0.272  -25.833 1.00 22.18  ? 655 ALA A N   1 
ATOM   3770 C CA  . ALA A 1 522 ? 34.096 -0.987  -26.286 1.00 22.39  ? 655 ALA A CA  1 
ATOM   3771 C C   . ALA A 1 522 ? 33.884 -1.534  -27.696 1.00 22.55  ? 655 ALA A C   1 
ATOM   3772 O O   . ALA A 1 522 ? 34.721 -1.328  -28.579 1.00 25.34  ? 655 ALA A O   1 
ATOM   3773 C CB  . ALA A 1 522 ? 34.439 -2.123  -25.312 1.00 21.77  ? 655 ALA A CB  1 
ATOM   3774 N N   . ALA A 1 523 ? 32.762 -2.218  -27.912 1.00 22.38  ? 656 ALA A N   1 
ATOM   3775 C CA  . ALA A 1 523 ? 32.458 -2.766  -29.232 1.00 22.50  ? 656 ALA A CA  1 
ATOM   3776 C C   . ALA A 1 523 ? 32.386 -1.656  -30.279 1.00 22.56  ? 656 ALA A C   1 
ATOM   3777 O O   . ALA A 1 523 ? 32.843 -1.831  -31.417 1.00 22.20  ? 656 ALA A O   1 
ATOM   3778 C CB  . ALA A 1 523 ? 31.130 -3.541  -29.201 1.00 23.54  ? 656 ALA A CB  1 
ATOM   3779 N N   . ALA A 1 524 ? 31.815 -0.514  -29.896 1.00 22.76  ? 657 ALA A N   1 
ATOM   3780 C CA  . ALA A 1 524 ? 31.689 0.618   -30.816 1.00 22.23  ? 657 ALA A CA  1 
ATOM   3781 C C   . ALA A 1 524 ? 33.058 1.141   -31.253 1.00 22.61  ? 657 ALA A C   1 
ATOM   3782 O O   . ALA A 1 524 ? 33.261 1.456   -32.424 1.00 21.67  ? 657 ALA A O   1 
ATOM   3783 C CB  . ALA A 1 524 ? 30.864 1.745   -30.171 1.00 22.65  ? 657 ALA A CB  1 
ATOM   3784 N N   . VAL A 1 525 ? 34.001 1.239   -30.319 1.00 23.18  ? 658 VAL A N   1 
ATOM   3785 C CA  . VAL A 1 525 ? 35.339 1.713   -30.677 1.00 23.68  ? 658 VAL A CA  1 
ATOM   3786 C C   . VAL A 1 525 ? 35.996 0.719   -31.644 1.00 23.81  ? 658 VAL A C   1 
ATOM   3787 O O   . VAL A 1 525 ? 36.655 1.117   -32.606 1.00 25.08  ? 658 VAL A O   1 
ATOM   3788 C CB  . VAL A 1 525 ? 36.253 1.874   -29.435 1.00 23.57  ? 658 VAL A CB  1 
ATOM   3789 C CG1 . VAL A 1 525 ? 37.625 2.394   -29.865 1.00 22.76  ? 658 VAL A CG1 1 
ATOM   3790 C CG2 . VAL A 1 525 ? 35.625 2.840   -28.440 1.00 22.44  ? 658 VAL A CG2 1 
ATOM   3791 N N   . LEU A 1 526 ? 35.808 -0.573  -31.390 1.00 24.85  ? 659 LEU A N   1 
ATOM   3792 C CA  . LEU A 1 526 ? 36.377 -1.609  -32.251 1.00 26.83  ? 659 LEU A CA  1 
ATOM   3793 C C   . LEU A 1 526 ? 35.802 -1.530  -33.664 1.00 27.53  ? 659 LEU A C   1 
ATOM   3794 O O   . LEU A 1 526 ? 36.538 -1.625  -34.645 1.00 28.49  ? 659 LEU A O   1 
ATOM   3795 C CB  . LEU A 1 526 ? 36.122 -2.996  -31.657 1.00 26.47  ? 659 LEU A CB  1 
ATOM   3796 C CG  . LEU A 1 526 ? 36.949 -3.344  -30.418 1.00 29.19  ? 659 LEU A CG  1 
ATOM   3797 C CD1 . LEU A 1 526 ? 36.452 -4.638  -29.801 1.00 29.84  ? 659 LEU A CD1 1 
ATOM   3798 C CD2 . LEU A 1 526 ? 38.415 -3.463  -30.812 1.00 29.22  ? 659 LEU A CD2 1 
ATOM   3799 N N   . PHE A 1 527 ? 34.489 -1.354  -33.770 1.00 28.29  ? 660 PHE A N   1 
ATOM   3800 C CA  . PHE A 1 527 ? 33.852 -1.244  -35.081 1.00 29.79  ? 660 PHE A CA  1 
ATOM   3801 C C   . PHE A 1 527 ? 34.360 -0.001  -35.810 1.00 30.91  ? 660 PHE A C   1 
ATOM   3802 O O   . PHE A 1 527 ? 34.692 -0.058  -36.992 1.00 30.05  ? 660 PHE A O   1 
ATOM   3803 C CB  . PHE A 1 527 ? 32.324 -1.159  -34.940 1.00 29.65  ? 660 PHE A CB  1 
ATOM   3804 C CG  . PHE A 1 527 ? 31.662 -2.480  -34.647 1.00 30.88  ? 660 PHE A CG  1 
ATOM   3805 C CD1 . PHE A 1 527 ? 30.755 -2.600  -33.597 1.00 30.57  ? 660 PHE A CD1 1 
ATOM   3806 C CD2 . PHE A 1 527 ? 31.931 -3.600  -35.431 1.00 32.83  ? 660 PHE A CD2 1 
ATOM   3807 C CE1 . PHE A 1 527 ? 30.126 -3.822  -33.323 1.00 32.50  ? 660 PHE A CE1 1 
ATOM   3808 C CE2 . PHE A 1 527 ? 31.307 -4.829  -35.169 1.00 35.00  ? 660 PHE A CE2 1 
ATOM   3809 C CZ  . PHE A 1 527 ? 30.400 -4.938  -34.111 1.00 33.46  ? 660 PHE A CZ  1 
ATOM   3810 N N   . ARG A 1 528 ? 34.423 1.125   -35.105 1.00 31.43  ? 661 ARG A N   1 
ATOM   3811 C CA  . ARG A 1 528 ? 34.890 2.361   -35.720 1.00 33.04  ? 661 ARG A CA  1 
ATOM   3812 C C   . ARG A 1 528 ? 36.360 2.306   -36.148 1.00 34.61  ? 661 ARG A C   1 
ATOM   3813 O O   . ARG A 1 528 ? 36.742 2.933   -37.133 1.00 35.21  ? 661 ARG A O   1 
ATOM   3814 C CB  . ARG A 1 528 ? 34.624 3.547   -34.780 1.00 30.02  ? 661 ARG A CB  1 
ATOM   3815 C CG  . ARG A 1 528 ? 33.139 3.933   -34.747 1.00 29.90  ? 661 ARG A CG  1 
ATOM   3816 C CD  . ARG A 1 528 ? 32.764 4.976   -33.686 1.00 28.89  ? 661 ARG A CD  1 
ATOM   3817 N NE  . ARG A 1 528 ? 31.354 5.345   -33.829 1.00 26.26  ? 661 ARG A NE  1 
ATOM   3818 C CZ  . ARG A 1 528 ? 30.700 6.211   -33.061 1.00 25.21  ? 661 ARG A CZ  1 
ATOM   3819 N NH1 . ARG A 1 528 ? 31.314 6.829   -32.056 1.00 23.31  ? 661 ARG A NH1 1 
ATOM   3820 N NH2 . ARG A 1 528 ? 29.420 6.467   -33.309 1.00 21.64  ? 661 ARG A NH2 1 
ATOM   3821 N N   . MET A 1 529 ? 37.182 1.548   -35.427 1.00 38.25  ? 662 MET A N   1 
ATOM   3822 C CA  . MET A 1 529 ? 38.597 1.437   -35.783 1.00 42.10  ? 662 MET A CA  1 
ATOM   3823 C C   . MET A 1 529 ? 38.800 0.569   -37.025 1.00 46.42  ? 662 MET A C   1 
ATOM   3824 O O   . MET A 1 529 ? 39.565 0.922   -37.922 1.00 47.13  ? 662 MET A O   1 
ATOM   3825 C CB  . MET A 1 529 ? 39.416 0.837   -34.630 1.00 39.66  ? 662 MET A CB  1 
ATOM   3826 C CG  . MET A 1 529 ? 39.570 1.725   -33.406 1.00 36.76  ? 662 MET A CG  1 
ATOM   3827 S SD  . MET A 1 529 ? 40.747 1.045   -32.199 1.00 34.11  ? 662 MET A SD  1 
ATOM   3828 C CE  . MET A 1 529 ? 40.002 -0.544  -31.854 1.00 33.81  ? 662 MET A CE  1 
ATOM   3829 N N   . SER A 1 530 ? 38.110 -0.566  -37.073 1.00 51.99  ? 663 SER A N   1 
ATOM   3830 C CA  . SER A 1 530 ? 38.234 -1.497  -38.192 1.00 57.69  ? 663 SER A CA  1 
ATOM   3831 C C   . SER A 1 530 ? 37.350 -1.131  -39.376 1.00 62.22  ? 663 SER A C   1 
ATOM   3832 O O   . SER A 1 530 ? 37.217 -1.907  -40.320 1.00 63.61  ? 663 SER A O   1 
ATOM   3833 C CB  . SER A 1 530 ? 37.890 -2.912  -37.733 1.00 57.01  ? 663 SER A CB  1 
ATOM   3834 O OG  . SER A 1 530 ? 36.520 -3.003  -37.384 1.00 58.29  ? 663 SER A OG  1 
ATOM   3835 N N   . GLU A 1 531 ? 36.740 0.045   -39.323 1.00 67.22  ? 664 GLU A N   1 
ATOM   3836 C CA  . GLU A 1 531 ? 35.878 0.491   -40.408 1.00 72.51  ? 664 GLU A CA  1 
ATOM   3837 C C   . GLU A 1 531 ? 36.664 1.344   -41.394 1.00 76.57  ? 664 GLU A C   1 
ATOM   3838 O O   . GLU A 1 531 ? 36.715 1.041   -42.589 1.00 76.74  ? 664 GLU A O   1 
ATOM   3839 C CB  . GLU A 1 531 ? 34.712 1.305   -39.858 1.00 72.22  ? 664 GLU A CB  1 
ATOM   3840 C CG  . GLU A 1 531 ? 33.879 1.967   -40.930 1.00 72.88  ? 664 GLU A CG  1 
ATOM   3841 C CD  . GLU A 1 531 ? 32.873 2.933   -40.354 1.00 73.75  ? 664 GLU A CD  1 
ATOM   3842 O OE1 . GLU A 1 531 ? 31.938 2.477   -39.663 1.00 74.75  ? 664 GLU A OE1 1 
ATOM   3843 O OE2 . GLU A 1 531 ? 33.025 4.151   -40.588 1.00 73.87  ? 664 GLU A OE2 1 
ATOM   3844 N N   . ASP A 1 532 ? 37.268 2.411   -40.871 1.00 81.07  ? 665 ASP A N   1 
ATOM   3845 C CA  . ASP A 1 532 ? 38.066 3.358   -41.650 1.00 85.18  ? 665 ASP A CA  1 
ATOM   3846 C C   . ASP A 1 532 ? 38.435 2.853   -43.042 1.00 87.10  ? 665 ASP A C   1 
ATOM   3847 O O   . ASP A 1 532 ? 37.689 3.042   -44.004 1.00 87.37  ? 665 ASP A O   1 
ATOM   3848 C CB  . ASP A 1 532 ? 39.353 3.712   -40.892 1.00 86.57  ? 665 ASP A CB  1 
ATOM   3849 C CG  . ASP A 1 532 ? 39.084 4.338   -39.534 1.00 87.81  ? 665 ASP A CG  1 
ATOM   3850 O OD1 . ASP A 1 532 ? 38.375 5.365   -39.479 1.00 88.87  ? 665 ASP A OD1 1 
ATOM   3851 O OD2 . ASP A 1 532 ? 39.590 3.805   -38.522 1.00 87.78  ? 665 ASP A OD2 1 
ATOM   3852 N N   . LYS A 1 533 ? 39.593 2.209   -43.134 1.00 89.24  ? 666 LYS A N   1 
ATOM   3853 C CA  . LYS A 1 533 ? 40.086 1.677   -44.396 1.00 91.30  ? 666 LYS A CA  1 
ATOM   3854 C C   . LYS A 1 533 ? 40.009 0.152   -44.496 1.00 92.63  ? 666 LYS A C   1 
ATOM   3855 O O   . LYS A 1 533 ? 39.640 -0.377  -45.544 1.00 92.57  ? 666 LYS A O   1 
ATOM   3856 C CB  . LYS A 1 533 ? 41.520 2.141   -44.626 1.00 91.16  ? 666 LYS A CB  1 
ATOM   3857 N N   . PRO A 1 534 ? 40.352 -0.572  -43.409 1.00 94.03  ? 667 PRO A N   1 
ATOM   3858 C CA  . PRO A 1 534 ? 40.314 -2.040  -43.414 1.00 95.36  ? 667 PRO A CA  1 
ATOM   3859 C C   . PRO A 1 534 ? 39.284 -2.616  -44.382 1.00 96.56  ? 667 PRO A C   1 
ATOM   3860 O O   . PRO A 1 534 ? 38.114 -2.795  -44.040 1.00 96.71  ? 667 PRO A O   1 
ATOM   3861 C CB  . PRO A 1 534 ? 40.018 -2.366  -41.959 1.00 94.98  ? 667 PRO A CB  1 
ATOM   3862 C CG  . PRO A 1 534 ? 40.860 -1.350  -41.255 1.00 94.38  ? 667 PRO A CG  1 
ATOM   3863 C CD  . PRO A 1 534 ? 40.588 -0.072  -42.041 1.00 94.18  ? 667 PRO A CD  1 
ATOM   3864 N N   . GLN A 1 535 ? 39.749 -2.906  -45.595 1.00 97.75  ? 668 GLN A N   1 
ATOM   3865 C CA  . GLN A 1 535 ? 38.911 -3.432  -46.667 1.00 98.61  ? 668 GLN A CA  1 
ATOM   3866 C C   . GLN A 1 535 ? 39.015 -4.942  -46.882 1.00 98.83  ? 668 GLN A C   1 
ATOM   3867 O O   . GLN A 1 535 ? 38.152 -5.703  -46.442 1.00 98.60  ? 668 GLN A O   1 
ATOM   3868 C CB  . GLN A 1 535 ? 39.256 -2.705  -47.970 1.00 99.25  ? 668 GLN A CB  1 
ATOM   3869 C CG  . GLN A 1 535 ? 40.756 -2.625  -48.247 1.00 100.84 ? 668 GLN A CG  1 
ATOM   3870 C CD  . GLN A 1 535 ? 41.089 -1.831  -49.497 1.00 101.96 ? 668 GLN A CD  1 
ATOM   3871 O OE1 . GLN A 1 535 ? 40.711 -0.665  -49.625 1.00 102.71 ? 668 GLN A OE1 1 
ATOM   3872 N NE2 . GLN A 1 535 ? 41.806 -2.458  -50.424 1.00 102.01 ? 668 GLN A NE2 1 
ATOM   3873 N N   . ASP A 1 536 ? 40.073 -5.365  -47.567 1.00 99.33  ? 669 ASP A N   1 
ATOM   3874 C CA  . ASP A 1 536 ? 40.290 -6.774  -47.873 1.00 99.60  ? 669 ASP A CA  1 
ATOM   3875 C C   . ASP A 1 536 ? 40.972 -7.542  -46.743 1.00 99.70  ? 669 ASP A C   1 
ATOM   3876 O O   . ASP A 1 536 ? 41.091 -7.054  -45.620 1.00 99.81  ? 669 ASP A O   1 
ATOM   3877 C CB  . ASP A 1 536 ? 41.133 -6.902  -49.146 1.00 99.66  ? 669 ASP A CB  1 
ATOM   3878 C CG  . ASP A 1 536 ? 40.548 -6.132  -50.314 1.00 100.09 ? 669 ASP A CG  1 
ATOM   3879 O OD1 . ASP A 1 536 ? 39.377 -6.382  -50.669 1.00 100.21 ? 669 ASP A OD1 1 
ATOM   3880 O OD2 . ASP A 1 536 ? 41.263 -5.278  -50.880 1.00 100.37 ? 669 ASP A OD2 1 
ATOM   3881 N N   . TYR A 1 537 ? 41.413 -8.755  -47.063 1.00 99.78  ? 670 TYR A N   1 
ATOM   3882 C CA  . TYR A 1 537 ? 42.099 -9.625  -46.114 1.00 99.79  ? 670 TYR A CA  1 
ATOM   3883 C C   . TYR A 1 537 ? 43.595 -9.567  -46.384 1.00 99.80  ? 670 TYR A C   1 
ATOM   3884 O O   . TYR A 1 537 ? 44.047 -8.831  -47.261 1.00 99.81  ? 670 TYR A O   1 
ATOM   3885 C CB  . TYR A 1 537 ? 41.627 -11.073 -46.280 1.00 100.39 ? 670 TYR A CB  1 
ATOM   3886 C CG  . TYR A 1 537 ? 40.233 -11.361 -45.774 1.00 101.04 ? 670 TYR A CG  1 
ATOM   3887 C CD1 . TYR A 1 537 ? 39.223 -10.403 -45.853 1.00 101.51 ? 670 TYR A CD1 1 
ATOM   3888 C CD2 . TYR A 1 537 ? 39.911 -12.615 -45.255 1.00 101.14 ? 670 TYR A CD2 1 
ATOM   3889 C CE1 . TYR A 1 537 ? 37.927 -10.687 -45.431 1.00 101.81 ? 670 TYR A CE1 1 
ATOM   3890 C CE2 . TYR A 1 537 ? 38.619 -12.910 -44.832 1.00 101.67 ? 670 TYR A CE2 1 
ATOM   3891 C CZ  . TYR A 1 537 ? 37.633 -11.942 -44.924 1.00 101.86 ? 670 TYR A CZ  1 
ATOM   3892 O OH  . TYR A 1 537 ? 36.353 -12.230 -44.519 1.00 102.18 ? 670 TYR A OH  1 
ATOM   3893 N N   . LYS A 1 538 ? 44.352 -10.356 -45.627 1.00 99.73  ? 671 LYS A N   1 
ATOM   3894 C CA  . LYS A 1 538 ? 45.801 -10.429 -45.775 1.00 99.61  ? 671 LYS A CA  1 
ATOM   3895 C C   . LYS A 1 538 ? 46.412 -11.156 -44.582 1.00 99.69  ? 671 LYS A C   1 
ATOM   3896 O O   . LYS A 1 538 ? 47.223 -10.536 -43.862 1.00 99.77  ? 671 LYS A O   1 
ATOM   3897 C CB  . LYS A 1 538 ? 46.408 -9.027  -45.888 1.00 99.23  ? 671 LYS A CB  1 
ATOM   3898 C CG  . LYS A 1 538 ? 47.666 -8.983  -46.738 1.00 98.52  ? 671 LYS A CG  1 
ATOM   3899 C CD  . LYS A 1 538 ? 47.349 -9.342  -48.184 1.00 97.70  ? 671 LYS A CD  1 
ATOM   3900 C CE  . LYS A 1 538 ? 48.609 -9.471  -49.020 1.00 97.50  ? 671 LYS A CE  1 
ATOM   3901 N NZ  . LYS A 1 538 ? 49.474 -10.581 -48.536 1.00 97.43  ? 671 LYS A NZ  1 
ATOM   3902 O OXT . LYS A 1 538 ? 46.067 -12.340 -44.382 1.00 99.92  ? 671 LYS A OXT 1 
ATOM   3903 N N   . LYS B 2 9   ? 23.378 -18.987 -41.280 1.00 42.32  ? 9   LYS B N   1 
ATOM   3904 C CA  . LYS B 2 9   ? 24.333 -18.037 -40.635 1.00 40.58  ? 9   LYS B CA  1 
ATOM   3905 C C   . LYS B 2 9   ? 25.787 -18.294 -41.004 1.00 38.42  ? 9   LYS B C   1 
ATOM   3906 O O   . LYS B 2 9   ? 26.128 -19.327 -41.585 1.00 36.72  ? 9   LYS B O   1 
ATOM   3907 C CB  . LYS B 2 9   ? 24.189 -18.081 -39.115 1.00 42.94  ? 9   LYS B CB  1 
ATOM   3908 C CG  . LYS B 2 9   ? 23.395 -16.931 -38.543 1.00 46.12  ? 9   LYS B CG  1 
ATOM   3909 C CD  . LYS B 2 9   ? 23.337 -17.007 -37.027 1.00 48.33  ? 9   LYS B CD  1 
ATOM   3910 C CE  . LYS B 2 9   ? 22.570 -15.822 -36.459 1.00 51.93  ? 9   LYS B CE  1 
ATOM   3911 N NZ  . LYS B 2 9   ? 21.219 -15.690 -37.084 1.00 53.89  ? 9   LYS B NZ  1 
ATOM   3912 N N   . SER B 2 10  ? 26.636 -17.337 -40.644 1.00 36.19  ? 10  SER B N   1 
ATOM   3913 C CA  . SER B 2 10  ? 28.064 -17.399 -40.924 1.00 33.88  ? 10  SER B CA  1 
ATOM   3914 C C   . SER B 2 10  ? 28.773 -16.311 -40.116 1.00 32.33  ? 10  SER B C   1 
ATOM   3915 O O   . SER B 2 10  ? 28.128 -15.459 -39.508 1.00 31.20  ? 10  SER B O   1 
ATOM   3916 C CB  . SER B 2 10  ? 28.308 -17.151 -42.410 1.00 33.44  ? 10  SER B CB  1 
ATOM   3917 O OG  . SER B 2 10  ? 27.895 -15.840 -42.765 1.00 35.40  ? 10  SER B OG  1 
ATOM   3918 N N   . PRO B 2 11  ? 30.112 -16.325 -40.104 1.00 31.47  ? 11  PRO B N   1 
ATOM   3919 C CA  . PRO B 2 11  ? 30.824 -15.294 -39.346 1.00 32.04  ? 11  PRO B CA  1 
ATOM   3920 C C   . PRO B 2 11  ? 30.405 -13.906 -39.838 1.00 32.22  ? 11  PRO B C   1 
ATOM   3921 O O   . PRO B 2 11  ? 30.124 -13.012 -39.043 1.00 30.77  ? 11  PRO B O   1 
ATOM   3922 C CB  . PRO B 2 11  ? 32.289 -15.601 -39.645 1.00 31.70  ? 11  PRO B CB  1 
ATOM   3923 C CG  . PRO B 2 11  ? 32.281 -17.098 -39.822 1.00 33.02  ? 11  PRO B CG  1 
ATOM   3924 C CD  . PRO B 2 11  ? 31.053 -17.305 -40.677 1.00 30.17  ? 11  PRO B CD  1 
ATOM   3925 N N   . GLU B 2 12  ? 30.360 -13.744 -41.158 1.00 32.60  ? 12  GLU B N   1 
ATOM   3926 C CA  . GLU B 2 12  ? 29.971 -12.475 -41.774 1.00 34.57  ? 12  GLU B CA  1 
ATOM   3927 C C   . GLU B 2 12  ? 28.624 -11.974 -41.259 1.00 33.79  ? 12  GLU B C   1 
ATOM   3928 O O   . GLU B 2 12  ? 28.499 -10.818 -40.857 1.00 31.83  ? 12  GLU B O   1 
ATOM   3929 C CB  . GLU B 2 12  ? 29.922 -12.630 -43.300 1.00 36.55  ? 12  GLU B CB  1 
ATOM   3930 C CG  . GLU B 2 12  ? 29.202 -11.514 -44.039 1.00 42.49  ? 12  GLU B CG  1 
ATOM   3931 C CD  . GLU B 2 12  ? 29.297 -11.661 -45.553 1.00 46.85  ? 12  GLU B CD  1 
ATOM   3932 O OE1 . GLU B 2 12  ? 29.043 -12.775 -46.067 1.00 48.81  ? 12  GLU B OE1 1 
ATOM   3933 O OE2 . GLU B 2 12  ? 29.622 -10.660 -46.228 1.00 47.63  ? 12  GLU B OE2 1 
ATOM   3934 N N   . GLU B 2 13  ? 27.616 -12.839 -41.270 1.00 33.43  ? 13  GLU B N   1 
ATOM   3935 C CA  . GLU B 2 13  ? 26.295 -12.443 -40.797 1.00 35.59  ? 13  GLU B CA  1 
ATOM   3936 C C   . GLU B 2 13  ? 26.280 -12.139 -39.302 1.00 35.35  ? 13  GLU B C   1 
ATOM   3937 O O   . GLU B 2 13  ? 25.564 -11.242 -38.853 1.00 34.08  ? 13  GLU B O   1 
ATOM   3938 C CB  . GLU B 2 13  ? 25.265 -13.526 -41.131 1.00 36.18  ? 13  GLU B CB  1 
ATOM   3939 C CG  . GLU B 2 13  ? 24.856 -13.517 -42.597 1.00 40.42  ? 13  GLU B CG  1 
ATOM   3940 C CD  . GLU B 2 13  ? 24.135 -14.781 -43.024 1.00 42.16  ? 13  GLU B CD  1 
ATOM   3941 O OE1 . GLU B 2 13  ? 23.176 -15.188 -42.335 1.00 42.76  ? 13  GLU B OE1 1 
ATOM   3942 O OE2 . GLU B 2 13  ? 24.529 -15.361 -44.059 1.00 45.27  ? 13  GLU B OE2 1 
ATOM   3943 N N   . MET B 2 14  ? 27.065 -12.884 -38.532 1.00 34.97  ? 14  MET B N   1 
ATOM   3944 C CA  . MET B 2 14  ? 27.124 -12.653 -37.095 1.00 36.85  ? 14  MET B CA  1 
ATOM   3945 C C   . MET B 2 14  ? 27.650 -11.242 -36.858 1.00 34.43  ? 14  MET B C   1 
ATOM   3946 O O   . MET B 2 14  ? 27.128 -10.506 -36.025 1.00 33.51  ? 14  MET B O   1 
ATOM   3947 C CB  . MET B 2 14  ? 28.053 -13.666 -36.425 1.00 40.33  ? 14  MET B CB  1 
ATOM   3948 C CG  . MET B 2 14  ? 27.525 -15.087 -36.425 1.00 46.22  ? 14  MET B CG  1 
ATOM   3949 S SD  . MET B 2 14  ? 25.988 -15.231 -35.494 1.00 53.62  ? 14  MET B SD  1 
ATOM   3950 C CE  . MET B 2 14  ? 26.636 -15.277 -33.819 1.00 51.82  ? 14  MET B CE  1 
ATOM   3951 N N   . TYR B 2 15  ? 28.685 -10.879 -37.608 1.00 33.10  ? 15  TYR B N   1 
ATOM   3952 C CA  . TYR B 2 15  ? 29.302 -9.564  -37.506 1.00 34.19  ? 15  TYR B CA  1 
ATOM   3953 C C   . TYR B 2 15  ? 28.256 -8.471  -37.717 1.00 34.07  ? 15  TYR B C   1 
ATOM   3954 O O   . TYR B 2 15  ? 28.153 -7.534  -36.922 1.00 31.60  ? 15  TYR B O   1 
ATOM   3955 C CB  . TYR B 2 15  ? 30.398 -9.425  -38.560 1.00 36.24  ? 15  TYR B CB  1 
ATOM   3956 C CG  . TYR B 2 15  ? 31.188 -8.140  -38.467 1.00 40.47  ? 15  TYR B CG  1 
ATOM   3957 C CD1 . TYR B 2 15  ? 32.270 -8.029  -37.596 1.00 42.91  ? 15  TYR B CD1 1 
ATOM   3958 C CD2 . TYR B 2 15  ? 30.857 -7.034  -39.253 1.00 41.81  ? 15  TYR B CD2 1 
ATOM   3959 C CE1 . TYR B 2 15  ? 33.011 -6.851  -37.512 1.00 45.04  ? 15  TYR B CE1 1 
ATOM   3960 C CE2 . TYR B 2 15  ? 31.589 -5.850  -39.176 1.00 44.34  ? 15  TYR B CE2 1 
ATOM   3961 C CZ  . TYR B 2 15  ? 32.666 -5.768  -38.305 1.00 44.90  ? 15  TYR B CZ  1 
ATOM   3962 O OH  . TYR B 2 15  ? 33.409 -4.612  -38.233 1.00 47.83  ? 15  TYR B OH  1 
ATOM   3963 N N   . ILE B 2 16  ? 27.487 -8.601  -38.796 1.00 32.76  ? 16  ILE B N   1 
ATOM   3964 C CA  . ILE B 2 16  ? 26.449 -7.632  -39.131 1.00 33.48  ? 16  ILE B CA  1 
ATOM   3965 C C   . ILE B 2 16  ? 25.409 -7.479  -38.024 1.00 33.75  ? 16  ILE B C   1 
ATOM   3966 O O   . ILE B 2 16  ? 25.100 -6.361  -37.606 1.00 32.90  ? 16  ILE B O   1 
ATOM   3967 C CB  . ILE B 2 16  ? 25.743 -8.025  -40.454 1.00 33.97  ? 16  ILE B CB  1 
ATOM   3968 C CG1 . ILE B 2 16  ? 26.716 -7.850  -41.622 1.00 33.29  ? 16  ILE B CG1 1 
ATOM   3969 C CG2 . ILE B 2 16  ? 24.490 -7.176  -40.668 1.00 34.01  ? 16  ILE B CG2 1 
ATOM   3970 C CD1 . ILE B 2 16  ? 26.239 -8.474  -42.914 1.00 36.06  ? 16  ILE B CD1 1 
ATOM   3971 N N   . GLN B 2 17  ? 24.869 -8.597  -37.550 1.00 33.51  ? 17  GLN B N   1 
ATOM   3972 C CA  . GLN B 2 17  ? 23.862 -8.558  -36.493 1.00 35.19  ? 17  GLN B CA  1 
ATOM   3973 C C   . GLN B 2 17  ? 24.392 -7.911  -35.218 1.00 34.99  ? 17  GLN B C   1 
ATOM   3974 O O   . GLN B 2 17  ? 23.659 -7.201  -34.524 1.00 33.66  ? 17  GLN B O   1 
ATOM   3975 C CB  . GLN B 2 17  ? 23.358 -9.971  -36.173 1.00 39.35  ? 17  GLN B CB  1 
ATOM   3976 C CG  . GLN B 2 17  ? 22.487 -10.583 -37.264 1.00 45.22  ? 17  GLN B CG  1 
ATOM   3977 C CD  . GLN B 2 17  ? 21.851 -11.898 -36.845 1.00 49.49  ? 17  GLN B CD  1 
ATOM   3978 O OE1 . GLN B 2 17  ? 21.101 -12.510 -37.610 1.00 52.38  ? 17  GLN B OE1 1 
ATOM   3979 N NE2 . GLN B 2 17  ? 22.147 -12.340 -35.626 1.00 50.81  ? 17  GLN B NE2 1 
ATOM   3980 N N   . GLN B 2 18  ? 25.661 -8.167  -34.909 1.00 34.19  ? 18  GLN B N   1 
ATOM   3981 C CA  . GLN B 2 18  ? 26.286 -7.607  -33.714 1.00 34.68  ? 18  GLN B CA  1 
ATOM   3982 C C   . GLN B 2 18  ? 26.501 -6.106  -33.859 1.00 32.22  ? 18  GLN B C   1 
ATOM   3983 O O   . GLN B 2 18  ? 26.263 -5.344  -32.922 1.00 31.60  ? 18  GLN B O   1 
ATOM   3984 C CB  . GLN B 2 18  ? 27.623 -8.299  -33.443 1.00 36.66  ? 18  GLN B CB  1 
ATOM   3985 C CG  . GLN B 2 18  ? 27.483 -9.701  -32.875 1.00 44.38  ? 18  GLN B CG  1 
ATOM   3986 C CD  . GLN B 2 18  ? 28.735 -10.542 -33.073 1.00 48.49  ? 18  GLN B CD  1 
ATOM   3987 O OE1 . GLN B 2 18  ? 29.851 -10.091 -32.804 1.00 51.83  ? 18  GLN B OE1 1 
ATOM   3988 N NE2 . GLN B 2 18  ? 28.554 -11.775 -33.539 1.00 49.47  ? 18  GLN B NE2 1 
ATOM   3989 N N   . LYS B 2 19  ? 26.954 -5.685  -35.036 1.00 30.02  ? 19  LYS B N   1 
ATOM   3990 C CA  . LYS B 2 19  ? 27.191 -4.270  -35.288 1.00 29.82  ? 19  LYS B CA  1 
ATOM   3991 C C   . LYS B 2 19  ? 25.872 -3.492  -35.241 1.00 28.40  ? 19  LYS B C   1 
ATOM   3992 O O   . LYS B 2 19  ? 25.816 -2.397  -34.687 1.00 27.60  ? 19  LYS B O   1 
ATOM   3993 C CB  . LYS B 2 19  ? 27.885 -4.080  -36.645 1.00 29.21  ? 19  LYS B CB  1 
ATOM   3994 C CG  . LYS B 2 19  ? 28.225 -2.626  -36.962 1.00 29.96  ? 19  LYS B CG  1 
ATOM   3995 C CD  . LYS B 2 19  ? 29.114 -2.500  -38.186 1.00 30.63  ? 19  LYS B CD  1 
ATOM   3996 C CE  . LYS B 2 19  ? 29.351 -1.038  -38.527 1.00 34.22  ? 19  LYS B CE  1 
ATOM   3997 N NZ  . LYS B 2 19  ? 30.412 -0.859  -39.560 1.00 34.82  ? 19  LYS B NZ  1 
ATOM   3998 N N   . VAL B 2 20  ? 24.812 -4.064  -35.807 1.00 27.48  ? 20  VAL B N   1 
ATOM   3999 C CA  . VAL B 2 20  ? 23.508 -3.412  -35.794 1.00 27.54  ? 20  VAL B CA  1 
ATOM   4000 C C   . VAL B 2 20  ? 23.045 -3.244  -34.353 1.00 29.50  ? 20  VAL B C   1 
ATOM   4001 O O   . VAL B 2 20  ? 22.562 -2.181  -33.964 1.00 30.29  ? 20  VAL B O   1 
ATOM   4002 C CB  . VAL B 2 20  ? 22.441 -4.241  -36.566 1.00 30.24  ? 20  VAL B CB  1 
ATOM   4003 C CG1 . VAL B 2 20  ? 21.036 -3.754  -36.214 1.00 26.88  ? 20  VAL B CG1 1 
ATOM   4004 C CG2 . VAL B 2 20  ? 22.673 -4.119  -38.071 1.00 26.25  ? 20  VAL B CG2 1 
ATOM   4005 N N   . ARG B 2 21  ? 23.196 -4.299  -33.561 1.00 29.07  ? 21  ARG B N   1 
ATOM   4006 C CA  . ARG B 2 21  ? 22.783 -4.259  -32.163 1.00 31.13  ? 21  ARG B CA  1 
ATOM   4007 C C   . ARG B 2 21  ? 23.558 -3.199  -31.377 1.00 28.31  ? 21  ARG B C   1 
ATOM   4008 O O   . ARG B 2 21  ? 22.975 -2.425  -30.624 1.00 29.29  ? 21  ARG B O   1 
ATOM   4009 C CB  . ARG B 2 21  ? 22.970 -5.638  -31.518 1.00 31.93  ? 21  ARG B CB  1 
ATOM   4010 C CG  . ARG B 2 21  ? 22.523 -5.702  -30.069 1.00 37.77  ? 21  ARG B CG  1 
ATOM   4011 C CD  . ARG B 2 21  ? 22.549 -7.132  -29.525 1.00 42.61  ? 21  ARG B CD  1 
ATOM   4012 N NE  . ARG B 2 21  ? 21.564 -7.994  -30.179 1.00 46.95  ? 21  ARG B NE  1 
ATOM   4013 C CZ  . ARG B 2 21  ? 21.816 -8.784  -31.222 1.00 49.05  ? 21  ARG B CZ  1 
ATOM   4014 N NH1 . ARG B 2 21  ? 23.032 -8.841  -31.748 1.00 49.44  ? 21  ARG B NH1 1 
ATOM   4015 N NH2 . ARG B 2 21  ? 20.842 -9.521  -31.740 1.00 49.60  ? 21  ARG B NH2 1 
ATOM   4016 N N   . VAL B 2 22  ? 24.874 -3.169  -31.550 1.00 28.26  ? 22  VAL B N   1 
ATOM   4017 C CA  . VAL B 2 22  ? 25.702 -2.188  -30.859 1.00 27.47  ? 22  VAL B CA  1 
ATOM   4018 C C   . VAL B 2 22  ? 25.326 -0.755  -31.259 1.00 28.13  ? 22  VAL B C   1 
ATOM   4019 O O   . VAL B 2 22  ? 25.175 0.115   -30.404 1.00 27.05  ? 22  VAL B O   1 
ATOM   4020 C CB  . VAL B 2 22  ? 27.199 -2.429  -31.157 1.00 27.92  ? 22  VAL B CB  1 
ATOM   4021 C CG1 . VAL B 2 22  ? 28.029 -1.229  -30.713 1.00 26.79  ? 22  VAL B CG1 1 
ATOM   4022 C CG2 . VAL B 2 22  ? 27.664 -3.694  -30.443 1.00 24.50  ? 22  VAL B CG2 1 
ATOM   4023 N N   . LEU B 2 23  ? 25.174 -0.514  -32.557 1.00 28.22  ? 23  LEU B N   1 
ATOM   4024 C CA  . LEU B 2 23  ? 24.825 0.822   -33.032 1.00 28.51  ? 23  LEU B CA  1 
ATOM   4025 C C   . LEU B 2 23  ? 23.481 1.295   -32.483 1.00 29.43  ? 23  LEU B C   1 
ATOM   4026 O O   . LEU B 2 23  ? 23.347 2.444   -32.062 1.00 29.06  ? 23  LEU B O   1 
ATOM   4027 C CB  . LEU B 2 23  ? 24.799 0.855   -34.558 1.00 27.03  ? 23  LEU B CB  1 
ATOM   4028 C CG  . LEU B 2 23  ? 26.133 0.624   -35.267 1.00 25.94  ? 23  LEU B CG  1 
ATOM   4029 C CD1 . LEU B 2 23  ? 25.908 0.684   -36.776 1.00 23.58  ? 23  LEU B CD1 1 
ATOM   4030 C CD2 . LEU B 2 23  ? 27.146 1.679   -34.831 1.00 23.32  ? 23  LEU B CD2 1 
ATOM   4031 N N   . LEU B 2 24  ? 22.486 0.411   -32.488 1.00 30.24  ? 24  LEU B N   1 
ATOM   4032 C CA  . LEU B 2 24  ? 21.169 0.767   -31.974 1.00 29.96  ? 24  LEU B CA  1 
ATOM   4033 C C   . LEU B 2 24  ? 21.249 1.103   -30.489 1.00 30.16  ? 24  LEU B C   1 
ATOM   4034 O O   . LEU B 2 24  ? 20.625 2.061   -30.021 1.00 29.77  ? 24  LEU B O   1 
ATOM   4035 C CB  . LEU B 2 24  ? 20.176 -0.379  -32.202 1.00 32.17  ? 24  LEU B CB  1 
ATOM   4036 C CG  . LEU B 2 24  ? 19.762 -0.630  -33.656 1.00 30.45  ? 24  LEU B CG  1 
ATOM   4037 C CD1 . LEU B 2 24  ? 18.766 -1.780  -33.707 1.00 33.39  ? 24  LEU B CD1 1 
ATOM   4038 C CD2 . LEU B 2 24  ? 19.148 0.632   -34.245 1.00 31.58  ? 24  LEU B CD2 1 
ATOM   4039 N N   . MET B 2 25  ? 22.022 0.318   -29.746 1.00 28.89  ? 25  MET B N   1 
ATOM   4040 C CA  . MET B 2 25  ? 22.180 0.552   -28.315 1.00 29.95  ? 25  MET B CA  1 
ATOM   4041 C C   . MET B 2 25  ? 22.950 1.857   -28.067 1.00 29.98  ? 25  MET B C   1 
ATOM   4042 O O   . MET B 2 25  ? 22.621 2.617   -27.157 1.00 27.32  ? 25  MET B O   1 
ATOM   4043 C CB  . MET B 2 25  ? 22.922 -0.621  -27.669 1.00 34.40  ? 25  MET B CB  1 
ATOM   4044 C CG  . MET B 2 25  ? 23.092 -0.505  -26.154 1.00 39.63  ? 25  MET B CG  1 
ATOM   4045 S SD  . MET B 2 25  ? 21.534 -0.607  -25.233 1.00 45.56  ? 25  MET B SD  1 
ATOM   4046 C CE  . MET B 2 25  ? 21.115 1.102   -25.080 1.00 46.18  ? 25  MET B CE  1 
ATOM   4047 N N   . LEU B 2 26  ? 23.967 2.114   -28.887 1.00 27.44  ? 26  LEU B N   1 
ATOM   4048 C CA  . LEU B 2 26  ? 24.772 3.323   -28.748 1.00 28.87  ? 26  LEU B CA  1 
ATOM   4049 C C   . LEU B 2 26  ? 23.907 4.572   -28.938 1.00 31.06  ? 26  LEU B C   1 
ATOM   4050 O O   . LEU B 2 26  ? 24.043 5.549   -28.198 1.00 29.91  ? 26  LEU B O   1 
ATOM   4051 C CB  . LEU B 2 26  ? 25.920 3.320   -29.769 1.00 26.92  ? 26  LEU B CB  1 
ATOM   4052 C CG  . LEU B 2 26  ? 26.940 4.466   -29.714 1.00 26.57  ? 26  LEU B CG  1 
ATOM   4053 C CD1 . LEU B 2 26  ? 27.637 4.493   -28.367 1.00 24.64  ? 26  LEU B CD1 1 
ATOM   4054 C CD2 . LEU B 2 26  ? 27.966 4.290   -30.823 1.00 26.64  ? 26  LEU B CD2 1 
ATOM   4055 N N   . ARG B 2 27  ? 23.017 4.537   -29.929 1.00 32.88  ? 27  ARG B N   1 
ATOM   4056 C CA  . ARG B 2 27  ? 22.138 5.673   -30.192 1.00 34.94  ? 27  ARG B CA  1 
ATOM   4057 C C   . ARG B 2 27  ? 21.175 5.835   -29.023 1.00 35.42  ? 27  ARG B C   1 
ATOM   4058 O O   . ARG B 2 27  ? 20.855 6.953   -28.613 1.00 34.91  ? 27  ARG B O   1 
ATOM   4059 C CB  . ARG B 2 27  ? 21.332 5.457   -31.475 1.00 38.00  ? 27  ARG B CB  1 
ATOM   4060 C CG  . ARG B 2 27  ? 20.613 6.717   -31.943 1.00 42.14  ? 27  ARG B CG  1 
ATOM   4061 C CD  . ARG B 2 27  ? 19.314 6.416   -32.665 1.00 42.97  ? 27  ARG B CD  1 
ATOM   4062 N NE  . ARG B 2 27  ? 19.487 5.782   -33.968 1.00 45.19  ? 27  ARG B NE  1 
ATOM   4063 C CZ  . ARG B 2 27  ? 20.123 6.330   -34.999 1.00 47.18  ? 27  ARG B CZ  1 
ATOM   4064 N NH1 . ARG B 2 27  ? 20.673 7.535   -34.892 1.00 46.94  ? 27  ARG B NH1 1 
ATOM   4065 N NH2 . ARG B 2 27  ? 20.178 5.683   -36.157 1.00 44.24  ? 27  ARG B NH2 1 
ATOM   4066 N N   . LYS B 2 28  ? 20.715 4.707   -28.491 1.00 34.51  ? 28  LYS B N   1 
ATOM   4067 C CA  . LYS B 2 28  ? 19.793 4.716   -27.368 1.00 35.58  ? 28  LYS B CA  1 
ATOM   4068 C C   . LYS B 2 28  ? 20.463 5.296   -26.125 1.00 34.82  ? 28  LYS B C   1 
ATOM   4069 O O   . LYS B 2 28  ? 19.803 5.911   -25.288 1.00 35.68  ? 28  LYS B O   1 
ATOM   4070 C CB  . LYS B 2 28  ? 19.300 3.295   -27.085 1.00 38.71  ? 28  LYS B CB  1 
ATOM   4071 C CG  . LYS B 2 28  ? 18.225 3.213   -26.023 1.00 43.27  ? 28  LYS B CG  1 
ATOM   4072 C CD  . LYS B 2 28  ? 17.727 1.783   -25.862 1.00 49.31  ? 28  LYS B CD  1 
ATOM   4073 C CE  . LYS B 2 28  ? 16.600 1.701   -24.840 1.00 51.07  ? 28  LYS B CE  1 
ATOM   4074 N NZ  . LYS B 2 28  ? 16.148 0.297   -24.642 1.00 54.97  ? 28  LYS B NZ  1 
ATOM   4075 N N   . MET B 2 29  ? 21.774 5.102   -26.005 1.00 33.48  ? 29  MET B N   1 
ATOM   4076 C CA  . MET B 2 29  ? 22.517 5.623   -24.860 1.00 31.52  ? 29  MET B CA  1 
ATOM   4077 C C   . MET B 2 29  ? 22.822 7.113   -25.033 1.00 30.41  ? 29  MET B C   1 
ATOM   4078 O O   . MET B 2 29  ? 23.459 7.729   -24.181 1.00 30.12  ? 29  MET B O   1 
ATOM   4079 C CB  . MET B 2 29  ? 23.820 4.835   -24.659 1.00 31.34  ? 29  MET B CB  1 
ATOM   4080 C CG  . MET B 2 29  ? 23.611 3.352   -24.367 1.00 33.37  ? 29  MET B CG  1 
ATOM   4081 S SD  . MET B 2 29  ? 25.139 2.431   -24.014 1.00 32.33  ? 29  MET B SD  1 
ATOM   4082 C CE  . MET B 2 29  ? 26.090 2.775   -25.466 1.00 38.32  ? 29  MET B CE  1 
ATOM   4083 N N   . GLY B 2 30  ? 22.384 7.686   -26.149 1.00 29.63  ? 30  GLY B N   1 
ATOM   4084 C CA  . GLY B 2 30  ? 22.592 9.108   -26.369 1.00 28.98  ? 30  GLY B CA  1 
ATOM   4085 C C   . GLY B 2 30  ? 23.792 9.565   -27.177 1.00 29.08  ? 30  GLY B C   1 
ATOM   4086 O O   . GLY B 2 30  ? 24.032 10.769  -27.271 1.00 29.22  ? 30  GLY B O   1 
ATOM   4087 N N   . SER B 2 31  ? 24.553 8.634   -27.749 1.00 27.65  ? 31  SER B N   1 
ATOM   4088 C CA  . SER B 2 31  ? 25.709 9.006   -28.554 1.00 26.50  ? 31  SER B CA  1 
ATOM   4089 C C   . SER B 2 31  ? 25.295 9.085   -30.015 1.00 27.99  ? 31  SER B C   1 
ATOM   4090 O O   . SER B 2 31  ? 24.418 8.337   -30.453 1.00 28.28  ? 31  SER B O   1 
ATOM   4091 C CB  . SER B 2 31  ? 26.841 7.978   -28.402 1.00 25.69  ? 31  SER B CB  1 
ATOM   4092 O OG  . SER B 2 31  ? 27.498 8.101   -27.150 1.00 27.64  ? 31  SER B OG  1 
ATOM   4093 N N   . ASN B 2 32  ? 25.917 9.995   -30.761 1.00 27.95  ? 32  ASN B N   1 
ATOM   4094 C CA  . ASN B 2 32  ? 25.620 10.157  -32.181 1.00 28.65  ? 32  ASN B CA  1 
ATOM   4095 C C   . ASN B 2 32  ? 26.329 9.085   -32.990 1.00 27.92  ? 32  ASN B C   1 
ATOM   4096 O O   . ASN B 2 32  ? 27.391 8.594   -32.599 1.00 27.82  ? 32  ASN B O   1 
ATOM   4097 C CB  . ASN B 2 32  ? 26.085 11.526  -32.696 1.00 32.81  ? 32  ASN B CB  1 
ATOM   4098 C CG  . ASN B 2 32  ? 25.226 12.669  -32.195 1.00 34.64  ? 32  ASN B CG  1 
ATOM   4099 O OD1 . ASN B 2 32  ? 23.999 12.597  -32.225 1.00 36.92  ? 32  ASN B OD1 1 
ATOM   4100 N ND2 . ASN B 2 32  ? 25.870 13.739  -31.746 1.00 34.17  ? 32  ASN B ND2 1 
ATOM   4101 N N   . LEU B 2 33  ? 25.735 8.728   -34.122 1.00 26.18  ? 33  LEU B N   1 
ATOM   4102 C CA  . LEU B 2 33  ? 26.320 7.737   -35.011 1.00 26.48  ? 33  LEU B CA  1 
ATOM   4103 C C   . LEU B 2 33  ? 26.977 8.489   -36.166 1.00 26.53  ? 33  LEU B C   1 
ATOM   4104 O O   . LEU B 2 33  ? 26.601 9.620   -36.467 1.00 27.88  ? 33  LEU B O   1 
ATOM   4105 C CB  . LEU B 2 33  ? 25.233 6.799   -35.542 1.00 25.82  ? 33  LEU B CB  1 
ATOM   4106 C CG  . LEU B 2 33  ? 24.432 6.038   -34.478 1.00 28.14  ? 33  LEU B CG  1 
ATOM   4107 C CD1 . LEU B 2 33  ? 23.430 5.103   -35.154 1.00 27.26  ? 33  LEU B CD1 1 
ATOM   4108 C CD2 . LEU B 2 33  ? 25.384 5.252   -33.582 1.00 27.62  ? 33  LEU B CD2 1 
ATOM   4109 N N   . THR B 2 34  ? 27.966 7.876   -36.802 1.00 25.30  ? 34  THR B N   1 
ATOM   4110 C CA  . THR B 2 34  ? 28.634 8.513   -37.928 1.00 26.64  ? 34  THR B CA  1 
ATOM   4111 C C   . THR B 2 34  ? 27.761 8.361   -39.168 1.00 28.26  ? 34  THR B C   1 
ATOM   4112 O O   . THR B 2 34  ? 26.751 7.648   -39.151 1.00 26.05  ? 34  THR B O   1 
ATOM   4113 C CB  . THR B 2 34  ? 29.972 7.848   -38.237 1.00 26.81  ? 34  THR B CB  1 
ATOM   4114 O OG1 . THR B 2 34  ? 29.732 6.489   -38.615 1.00 25.85  ? 34  THR B OG1 1 
ATOM   4115 C CG2 . THR B 2 34  ? 30.888 7.878   -37.012 1.00 26.51  ? 34  THR B CG2 1 
ATOM   4116 N N   . ALA B 2 35  ? 28.161 9.034   -40.242 1.00 27.87  ? 35  ALA B N   1 
ATOM   4117 C CA  . ALA B 2 35  ? 27.435 8.969   -41.501 1.00 29.44  ? 35  ALA B CA  1 
ATOM   4118 C C   . ALA B 2 35  ? 27.478 7.549   -42.073 1.00 29.95  ? 35  ALA B C   1 
ATOM   4119 O O   . ALA B 2 35  ? 26.475 7.047   -42.571 1.00 28.62  ? 35  ALA B O   1 
ATOM   4120 C CB  . ALA B 2 35  ? 28.039 9.956   -42.499 1.00 30.35  ? 35  ALA B CB  1 
ATOM   4121 N N   . SER B 2 36  ? 28.634 6.895   -42.001 1.00 31.25  ? 36  SER B N   1 
ATOM   4122 C CA  . SER B 2 36  ? 28.734 5.538   -42.526 1.00 31.29  ? 36  SER B CA  1 
ATOM   4123 C C   . SER B 2 36  ? 27.882 4.562   -41.708 1.00 30.59  ? 36  SER B C   1 
ATOM   4124 O O   . SER B 2 36  ? 27.355 3.587   -42.246 1.00 29.19  ? 36  SER B O   1 
ATOM   4125 C CB  . SER B 2 36  ? 30.200 5.077   -42.566 1.00 33.33  ? 36  SER B CB  1 
ATOM   4126 O OG  . SER B 2 36  ? 30.829 5.211   -41.304 1.00 38.03  ? 36  SER B OG  1 
ATOM   4127 N N   . GLU B 2 37  ? 27.728 4.828   -40.413 1.00 30.33  ? 37  GLU B N   1 
ATOM   4128 C CA  . GLU B 2 37  ? 26.916 3.950   -39.572 1.00 29.42  ? 37  GLU B CA  1 
ATOM   4129 C C   . GLU B 2 37  ? 25.430 4.102   -39.917 1.00 30.02  ? 37  GLU B C   1 
ATOM   4130 O O   . GLU B 2 37  ? 24.699 3.108   -39.991 1.00 28.56  ? 37  GLU B O   1 
ATOM   4131 C CB  . GLU B 2 37  ? 27.177 4.247   -38.089 1.00 29.03  ? 37  GLU B CB  1 
ATOM   4132 C CG  . GLU B 2 37  ? 28.648 4.046   -37.713 1.00 30.70  ? 37  GLU B CG  1 
ATOM   4133 C CD  . GLU B 2 37  ? 28.986 4.458   -36.286 1.00 30.76  ? 37  GLU B CD  1 
ATOM   4134 O OE1 . GLU B 2 37  ? 28.334 5.374   -35.738 1.00 28.01  ? 37  GLU B OE1 1 
ATOM   4135 O OE2 . GLU B 2 37  ? 29.930 3.869   -35.718 1.00 27.68  ? 37  GLU B OE2 1 
ATOM   4136 N N   . GLU B 2 38  ? 24.989 5.341   -40.133 1.00 31.08  ? 38  GLU B N   1 
ATOM   4137 C CA  . GLU B 2 38  ? 23.597 5.617   -40.497 1.00 32.24  ? 38  GLU B CA  1 
ATOM   4138 C C   . GLU B 2 38  ? 23.299 4.867   -41.789 1.00 31.54  ? 38  GLU B C   1 
ATOM   4139 O O   . GLU B 2 38  ? 22.233 4.275   -41.952 1.00 30.98  ? 38  GLU B O   1 
ATOM   4140 C CB  . GLU B 2 38  ? 23.395 7.120   -40.728 1.00 35.84  ? 38  GLU B CB  1 
ATOM   4141 C CG  . GLU B 2 38  ? 23.617 7.970   -39.493 1.00 37.26  ? 38  GLU B CG  1 
ATOM   4142 C CD  . GLU B 2 38  ? 22.393 8.046   -38.609 1.00 41.38  ? 38  GLU B CD  1 
ATOM   4143 O OE1 . GLU B 2 38  ? 21.696 7.018   -38.462 1.00 44.09  ? 38  GLU B OE1 1 
ATOM   4144 O OE2 . GLU B 2 38  ? 22.131 9.137   -38.056 1.00 43.48  ? 38  GLU B OE2 1 
ATOM   4145 N N   . GLU B 2 39  ? 24.262 4.916   -42.703 1.00 33.43  ? 39  GLU B N   1 
ATOM   4146 C CA  . GLU B 2 39  ? 24.183 4.247   -43.998 1.00 35.65  ? 39  GLU B CA  1 
ATOM   4147 C C   . GLU B 2 39  ? 24.085 2.732   -43.780 1.00 35.96  ? 39  GLU B C   1 
ATOM   4148 O O   . GLU B 2 39  ? 23.251 2.054   -44.386 1.00 34.20  ? 39  GLU B O   1 
ATOM   4149 C CB  . GLU B 2 39  ? 25.436 4.579   -44.808 1.00 36.95  ? 39  GLU B CB  1 
ATOM   4150 C CG  . GLU B 2 39  ? 25.616 3.773   -46.079 1.00 44.68  ? 39  GLU B CG  1 
ATOM   4151 C CD  . GLU B 2 39  ? 24.813 4.316   -47.234 1.00 48.22  ? 39  GLU B CD  1 
ATOM   4152 O OE1 . GLU B 2 39  ? 23.574 4.439   -47.103 1.00 50.88  ? 39  GLU B OE1 1 
ATOM   4153 O OE2 . GLU B 2 39  ? 25.428 4.619   -48.278 1.00 52.16  ? 39  GLU B OE2 1 
ATOM   4154 N N   . PHE B 2 40  ? 24.949 2.217   -42.909 1.00 35.58  ? 40  PHE B N   1 
ATOM   4155 C CA  . PHE B 2 40  ? 24.981 0.796   -42.575 1.00 33.67  ? 40  PHE B CA  1 
ATOM   4156 C C   . PHE B 2 40  ? 23.594 0.358   -42.112 1.00 33.14  ? 40  PHE B C   1 
ATOM   4157 O O   . PHE B 2 40  ? 23.078 -0.672  -42.551 1.00 32.67  ? 40  PHE B O   1 
ATOM   4158 C CB  . PHE B 2 40  ? 25.996 0.547   -41.452 1.00 34.57  ? 40  PHE B CB  1 
ATOM   4159 C CG  . PHE B 2 40  ? 26.140 -0.900  -41.065 1.00 34.88  ? 40  PHE B CG  1 
ATOM   4160 C CD1 . PHE B 2 40  ? 26.901 -1.772  -41.842 1.00 35.47  ? 40  PHE B CD1 1 
ATOM   4161 C CD2 . PHE B 2 40  ? 25.510 -1.394  -39.927 1.00 35.10  ? 40  PHE B CD2 1 
ATOM   4162 C CE1 . PHE B 2 40  ? 27.035 -3.118  -41.490 1.00 35.89  ? 40  PHE B CE1 1 
ATOM   4163 C CE2 . PHE B 2 40  ? 25.635 -2.739  -39.564 1.00 35.88  ? 40  PHE B CE2 1 
ATOM   4164 C CZ  . PHE B 2 40  ? 26.400 -3.602  -40.349 1.00 35.89  ? 40  PHE B CZ  1 
ATOM   4165 N N   . LEU B 2 41  ? 22.997 1.143   -41.221 1.00 32.45  ? 41  LEU B N   1 
ATOM   4166 C CA  . LEU B 2 41  ? 21.670 0.831   -40.698 1.00 34.00  ? 41  LEU B CA  1 
ATOM   4167 C C   . LEU B 2 41  ? 20.598 0.831   -41.788 1.00 35.82  ? 41  LEU B C   1 
ATOM   4168 O O   . LEU B 2 41  ? 19.565 0.173   -41.646 1.00 36.67  ? 41  LEU B O   1 
ATOM   4169 C CB  . LEU B 2 41  ? 21.284 1.819   -39.597 1.00 33.22  ? 41  LEU B CB  1 
ATOM   4170 C CG  . LEU B 2 41  ? 22.103 1.757   -38.303 1.00 33.01  ? 41  LEU B CG  1 
ATOM   4171 C CD1 . LEU B 2 41  ? 21.552 2.773   -37.315 1.00 30.62  ? 41  LEU B CD1 1 
ATOM   4172 C CD2 . LEU B 2 41  ? 22.042 0.353   -37.708 1.00 32.57  ? 41  LEU B CD2 1 
ATOM   4173 N N   . ARG B 2 42  ? 20.839 1.567   -42.870 1.00 36.32  ? 42  ARG B N   1 
ATOM   4174 C CA  . ARG B 2 42  ? 19.885 1.607   -43.976 1.00 38.52  ? 42  ARG B CA  1 
ATOM   4175 C C   . ARG B 2 42  ? 20.071 0.341   -44.795 1.00 37.14  ? 42  ARG B C   1 
ATOM   4176 O O   . ARG B 2 42  ? 19.110 -0.350  -45.115 1.00 37.61  ? 42  ARG B O   1 
ATOM   4177 C CB  . ARG B 2 42  ? 20.124 2.826   -44.874 1.00 38.35  ? 42  ARG B CB  1 
ATOM   4178 C CG  . ARG B 2 42  ? 19.885 4.157   -44.203 1.00 39.49  ? 42  ARG B CG  1 
ATOM   4179 C CD  . ARG B 2 42  ? 20.163 5.303   -45.163 1.00 38.96  ? 42  ARG B CD  1 
ATOM   4180 N NE  . ARG B 2 42  ? 20.457 6.526   -44.428 1.00 41.12  ? 42  ARG B NE  1 
ATOM   4181 C CZ  . ARG B 2 42  ? 21.562 7.239   -44.587 1.00 39.03  ? 42  ARG B CZ  1 
ATOM   4182 N NH1 . ARG B 2 42  ? 22.482 6.857   -45.462 1.00 35.50  ? 42  ARG B NH1 1 
ATOM   4183 N NH2 . ARG B 2 42  ? 21.749 8.333   -43.863 1.00 45.74  ? 42  ARG B NH2 1 
ATOM   4184 N N   . THR B 2 43  ? 21.323 0.050   -45.132 1.00 38.07  ? 43  THR B N   1 
ATOM   4185 C CA  . THR B 2 43  ? 21.656 -1.137  -45.903 1.00 38.40  ? 43  THR B CA  1 
ATOM   4186 C C   . THR B 2 43  ? 21.059 -2.382  -45.253 1.00 38.66  ? 43  THR B C   1 
ATOM   4187 O O   . THR B 2 43  ? 20.564 -3.272  -45.942 1.00 39.41  ? 43  THR B O   1 
ATOM   4188 C CB  . THR B 2 43  ? 23.177 -1.320  -46.000 1.00 39.40  ? 43  THR B CB  1 
ATOM   4189 O OG1 . THR B 2 43  ? 23.741 -0.228  -46.733 1.00 40.16  ? 43  THR B OG1 1 
ATOM   4190 C CG2 . THR B 2 43  ? 23.519 -2.632  -46.696 1.00 39.94  ? 43  THR B CG2 1 
ATOM   4191 N N   . TYR B 2 44  ? 21.107 -2.440  -43.924 1.00 37.27  ? 44  TYR B N   1 
ATOM   4192 C CA  . TYR B 2 44  ? 20.574 -3.586  -43.200 1.00 36.29  ? 44  TYR B CA  1 
ATOM   4193 C C   . TYR B 2 44  ? 19.343 -3.258  -42.375 1.00 37.42  ? 44  TYR B C   1 
ATOM   4194 O O   . TYR B 2 44  ? 19.213 -3.701  -41.232 1.00 37.05  ? 44  TYR B O   1 
ATOM   4195 C CB  . TYR B 2 44  ? 21.657 -4.194  -42.305 1.00 34.72  ? 44  TYR B CB  1 
ATOM   4196 C CG  . TYR B 2 44  ? 22.853 -4.666  -43.090 1.00 32.74  ? 44  TYR B CG  1 
ATOM   4197 C CD1 . TYR B 2 44  ? 24.000 -3.880  -43.192 1.00 33.46  ? 44  TYR B CD1 1 
ATOM   4198 C CD2 . TYR B 2 44  ? 22.820 -5.877  -43.781 1.00 33.04  ? 44  TYR B CD2 1 
ATOM   4199 C CE1 . TYR B 2 44  ? 25.086 -4.288  -43.965 1.00 31.80  ? 44  TYR B CE1 1 
ATOM   4200 C CE2 . TYR B 2 44  ? 23.900 -6.293  -44.560 1.00 30.96  ? 44  TYR B CE2 1 
ATOM   4201 C CZ  . TYR B 2 44  ? 25.027 -5.493  -44.646 1.00 33.06  ? 44  TYR B CZ  1 
ATOM   4202 O OH  . TYR B 2 44  ? 26.089 -5.887  -45.428 1.00 34.69  ? 44  TYR B OH  1 
ATOM   4203 N N   . ALA B 2 45  ? 18.432 -2.489  -42.967 1.00 38.37  ? 45  ALA B N   1 
ATOM   4204 C CA  . ALA B 2 45  ? 17.203 -2.108  -42.287 1.00 39.93  ? 45  ALA B CA  1 
ATOM   4205 C C   . ALA B 2 45  ? 16.441 -3.367  -41.896 1.00 41.23  ? 45  ALA B C   1 
ATOM   4206 O O   . ALA B 2 45  ? 15.748 -3.391  -40.876 1.00 41.20  ? 45  ALA B O   1 
ATOM   4207 C CB  . ALA B 2 45  ? 16.349 -1.233  -43.197 1.00 40.66  ? 45  ALA B CB  1 
ATOM   4208 N N   . GLY B 2 46  ? 16.579 -4.413  -42.709 1.00 41.97  ? 46  GLY B N   1 
ATOM   4209 C CA  . GLY B 2 46  ? 15.908 -5.667  -42.422 1.00 43.59  ? 46  GLY B CA  1 
ATOM   4210 C C   . GLY B 2 46  ? 16.344 -6.193  -41.067 1.00 45.42  ? 46  GLY B C   1 
ATOM   4211 O O   . GLY B 2 46  ? 15.513 -6.523  -40.222 1.00 46.04  ? 46  GLY B O   1 
ATOM   4212 N N   . VAL B 2 47  ? 17.656 -6.269  -40.857 1.00 46.38  ? 47  VAL B N   1 
ATOM   4213 C CA  . VAL B 2 47  ? 18.195 -6.741  -39.586 1.00 46.68  ? 47  VAL B CA  1 
ATOM   4214 C C   . VAL B 2 47  ? 17.771 -5.793  -38.469 1.00 47.64  ? 47  VAL B C   1 
ATOM   4215 O O   . VAL B 2 47  ? 17.471 -6.223  -37.355 1.00 46.79  ? 47  VAL B O   1 
ATOM   4216 C CB  . VAL B 2 47  ? 19.731 -6.806  -39.619 1.00 46.82  ? 47  VAL B CB  1 
ATOM   4217 C CG1 . VAL B 2 47  ? 20.263 -7.252  -38.263 1.00 46.62  ? 47  VAL B CG1 1 
ATOM   4218 C CG2 . VAL B 2 47  ? 20.185 -7.761  -40.714 1.00 46.65  ? 47  VAL B CG2 1 
ATOM   4219 N N   . VAL B 2 48  ? 17.748 -4.499  -38.778 1.00 49.33  ? 48  VAL B N   1 
ATOM   4220 C CA  . VAL B 2 48  ? 17.356 -3.483  -37.805 1.00 50.46  ? 48  VAL B CA  1 
ATOM   4221 C C   . VAL B 2 48  ? 15.930 -3.724  -37.329 1.00 52.31  ? 48  VAL B C   1 
ATOM   4222 O O   . VAL B 2 48  ? 15.680 -3.838  -36.131 1.00 51.94  ? 48  VAL B O   1 
ATOM   4223 C CB  . VAL B 2 48  ? 17.447 -2.061  -38.408 1.00 49.45  ? 48  VAL B CB  1 
ATOM   4224 C CG1 . VAL B 2 48  ? 16.840 -1.047  -37.452 1.00 49.13  ? 48  VAL B CG1 1 
ATOM   4225 C CG2 . VAL B 2 48  ? 18.897 -1.711  -38.691 1.00 48.94  ? 48  VAL B CG2 1 
ATOM   4226 N N   . ASN B 2 49  ? 14.998 -3.797  -38.274 1.00 55.44  ? 49  ASN B N   1 
ATOM   4227 C CA  . ASN B 2 49  ? 13.597 -4.028  -37.947 1.00 58.52  ? 49  ASN B CA  1 
ATOM   4228 C C   . ASN B 2 49  ? 13.447 -5.376  -37.263 1.00 60.16  ? 49  ASN B C   1 
ATOM   4229 O O   . ASN B 2 49  ? 12.608 -5.546  -36.378 1.00 61.17  ? 49  ASN B O   1 
ATOM   4230 C CB  . ASN B 2 49  ? 12.745 -3.993  -39.213 1.00 59.54  ? 49  ASN B CB  1 
ATOM   4231 C CG  . ASN B 2 49  ? 12.810 -2.655  -39.919 1.00 60.94  ? 49  ASN B CG  1 
ATOM   4232 O OD1 . ASN B 2 49  ? 12.510 -1.617  -39.330 1.00 62.96  ? 49  ASN B OD1 1 
ATOM   4233 N ND2 . ASN B 2 49  ? 13.201 -2.672  -41.188 1.00 61.78  ? 49  ASN B ND2 1 
ATOM   4234 N N   . SER B 2 50  ? 14.268 -6.334  -37.679 1.00 62.21  ? 50  SER B N   1 
ATOM   4235 C CA  . SER B 2 50  ? 14.241 -7.669  -37.099 1.00 65.07  ? 50  SER B CA  1 
ATOM   4236 C C   . SER B 2 50  ? 14.566 -7.597  -35.611 1.00 66.23  ? 50  SER B C   1 
ATOM   4237 O O   . SER B 2 50  ? 13.966 -8.301  -34.799 1.00 66.64  ? 50  SER B O   1 
ATOM   4238 C CB  . SER B 2 50  ? 15.255 -8.571  -37.803 1.00 65.38  ? 50  SER B CB  1 
ATOM   4239 O OG  . SER B 2 50  ? 15.320 -9.838  -37.174 1.00 67.46  ? 50  SER B OG  1 
ATOM   4240 N N   . GLN B 2 51  ? 15.522 -6.741  -35.261 1.00 67.20  ? 51  GLN B N   1 
ATOM   4241 C CA  . GLN B 2 51  ? 15.925 -6.570  -33.871 1.00 68.32  ? 51  GLN B CA  1 
ATOM   4242 C C   . GLN B 2 51  ? 15.014 -5.589  -33.140 1.00 70.43  ? 51  GLN B C   1 
ATOM   4243 O O   . GLN B 2 51  ? 14.801 -5.711  -31.932 1.00 70.94  ? 51  GLN B O   1 
ATOM   4244 C CB  . GLN B 2 51  ? 17.376 -6.091  -33.797 1.00 66.05  ? 51  GLN B CB  1 
ATOM   4245 C CG  . GLN B 2 51  ? 18.394 -7.198  -34.007 1.00 63.92  ? 51  GLN B CG  1 
ATOM   4246 C CD  . GLN B 2 51  ? 19.818 -6.687  -34.020 1.00 62.57  ? 51  GLN B CD  1 
ATOM   4247 O OE1 . GLN B 2 51  ? 20.201 -5.862  -33.191 1.00 61.99  ? 51  GLN B OE1 1 
ATOM   4248 N NE2 . GLN B 2 51  ? 20.617 -7.185  -34.956 1.00 60.59  ? 51  GLN B NE2 1 
ATOM   4249 N N   . LEU B 2 52  ? 14.476 -4.620  -33.874 1.00 72.70  ? 52  LEU B N   1 
ATOM   4250 C CA  . LEU B 2 52  ? 13.581 -3.629  -33.288 1.00 74.98  ? 52  LEU B CA  1 
ATOM   4251 C C   . LEU B 2 52  ? 12.386 -4.347  -32.673 1.00 76.55  ? 52  LEU B C   1 
ATOM   4252 O O   . LEU B 2 52  ? 11.639 -3.776  -31.876 1.00 76.74  ? 52  LEU B O   1 
ATOM   4253 C CB  . LEU B 2 52  ? 13.114 -2.646  -34.356 1.00 75.31  ? 52  LEU B CB  1 
ATOM   4254 N N   . SER B 2 53  ? 12.218 -5.610  -33.052 1.00 77.86  ? 53  SER B N   1 
ATOM   4255 C CA  . SER B 2 53  ? 11.126 -6.433  -32.554 1.00 78.57  ? 53  SER B CA  1 
ATOM   4256 C C   . SER B 2 53  ? 11.663 -7.531  -31.638 1.00 78.86  ? 53  SER B C   1 
ATOM   4257 O O   . SER B 2 53  ? 11.247 -8.686  -31.724 1.00 78.88  ? 53  SER B O   1 
ATOM   4258 C CB  . SER B 2 53  ? 10.369 -7.059  -33.728 1.00 78.92  ? 53  SER B CB  1 
ATOM   4259 O OG  . SER B 2 53  ? 9.911  -6.062  -34.625 1.00 79.11  ? 53  SER B OG  1 
ATOM   4260 N N   . GLN B 2 54  ? 12.593 -7.161  -30.762 1.00 79.15  ? 54  GLN B N   1 
ATOM   4261 C CA  . GLN B 2 54  ? 13.187 -8.112  -29.828 1.00 79.42  ? 54  GLN B CA  1 
ATOM   4262 C C   . GLN B 2 54  ? 12.836 -7.741  -28.392 1.00 79.46  ? 54  GLN B C   1 
ATOM   4263 O O   . GLN B 2 54  ? 13.493 -6.898  -27.782 1.00 79.53  ? 54  GLN B O   1 
ATOM   4264 C CB  . GLN B 2 54  ? 14.703 -8.145  -30.006 1.00 79.27  ? 54  GLN B CB  1 
ATOM   4265 N N   . ILE B 2 60  ? 21.176 2.236   -19.949 1.00 88.78  ? 60  ILE B N   1 
ATOM   4266 C CA  . ILE B 2 60  ? 20.000 2.634   -19.190 1.00 88.68  ? 60  ILE B CA  1 
ATOM   4267 C C   . ILE B 2 60  ? 20.377 3.437   -17.940 1.00 88.67  ? 60  ILE B C   1 
ATOM   4268 O O   . ILE B 2 60  ? 21.470 3.999   -17.856 1.00 89.00  ? 60  ILE B O   1 
ATOM   4269 C CB  . ILE B 2 60  ? 19.196 1.403   -18.802 1.00 88.89  ? 60  ILE B CB  1 
ATOM   4270 N N   . ASP B 2 61  ? 19.465 3.462   -16.970 1.00 88.51  ? 61  ASP B N   1 
ATOM   4271 C CA  . ASP B 2 61  ? 19.625 4.202   -15.714 1.00 87.94  ? 61  ASP B CA  1 
ATOM   4272 C C   . ASP B 2 61  ? 20.889 3.876   -14.911 1.00 86.99  ? 61  ASP B C   1 
ATOM   4273 O O   . ASP B 2 61  ? 21.872 3.363   -15.452 1.00 86.83  ? 61  ASP B O   1 
ATOM   4274 C CB  . ASP B 2 61  ? 18.396 3.971   -14.833 1.00 89.10  ? 61  ASP B CB  1 
ATOM   4275 C CG  . ASP B 2 61  ? 17.988 5.207   -14.060 1.00 90.39  ? 61  ASP B CG  1 
ATOM   4276 O OD1 . ASP B 2 61  ? 18.828 5.758   -13.320 1.00 91.45  ? 61  ASP B OD1 1 
ATOM   4277 O OD2 . ASP B 2 61  ? 16.819 5.627   -14.193 1.00 90.99  ? 61  ASP B OD2 1 
ATOM   4278 N N   . GLN B 2 62  ? 20.841 4.183   -13.613 1.00 85.72  ? 62  GLN B N   1 
ATOM   4279 C CA  . GLN B 2 62  ? 21.956 3.966   -12.687 1.00 83.89  ? 62  GLN B CA  1 
ATOM   4280 C C   . GLN B 2 62  ? 23.050 5.002   -12.920 1.00 82.63  ? 62  GLN B C   1 
ATOM   4281 O O   . GLN B 2 62  ? 24.237 4.700   -12.797 1.00 82.97  ? 62  GLN B O   1 
ATOM   4282 C CB  . GLN B 2 62  ? 22.523 2.556   -12.855 1.00 84.28  ? 62  GLN B CB  1 
ATOM   4283 N N   . GLY B 2 63  ? 22.655 6.226   -13.249 1.00 79.88  ? 63  GLY B N   1 
ATOM   4284 C CA  . GLY B 2 63  ? 23.652 7.241   -13.521 1.00 76.46  ? 63  GLY B CA  1 
ATOM   4285 C C   . GLY B 2 63  ? 24.013 8.166   -12.378 1.00 73.84  ? 63  GLY B C   1 
ATOM   4286 O O   . GLY B 2 63  ? 24.515 7.740   -11.336 1.00 74.32  ? 63  GLY B O   1 
ATOM   4287 N N   . ALA B 2 64  ? 23.746 9.449   -12.589 1.00 70.20  ? 64  ALA B N   1 
ATOM   4288 C CA  . ALA B 2 64  ? 24.052 10.493  -11.620 1.00 65.94  ? 64  ALA B CA  1 
ATOM   4289 C C   . ALA B 2 64  ? 23.333 10.407  -10.269 1.00 62.56  ? 64  ALA B C   1 
ATOM   4290 O O   . ALA B 2 64  ? 22.796 11.410  -9.798  1.00 62.78  ? 64  ALA B O   1 
ATOM   4291 C CB  . ALA B 2 64  ? 23.792 11.853  -12.256 1.00 65.94  ? 64  ALA B CB  1 
ATOM   4292 N N   . GLU B 2 65  ? 23.329 9.230   -9.642  1.00 57.29  ? 65  GLU B N   1 
ATOM   4293 C CA  . GLU B 2 65  ? 22.683 9.068   -8.338  1.00 52.41  ? 65  GLU B CA  1 
ATOM   4294 C C   . GLU B 2 65  ? 23.248 10.071  -7.321  1.00 48.26  ? 65  GLU B C   1 
ATOM   4295 O O   . GLU B 2 65  ? 24.465 10.200  -7.158  1.00 46.53  ? 65  GLU B O   1 
ATOM   4296 C CB  . GLU B 2 65  ? 22.864 7.633   -7.832  1.00 53.95  ? 65  GLU B CB  1 
ATOM   4297 C CG  . GLU B 2 65  ? 21.719 6.685   -8.194  1.00 57.67  ? 65  GLU B CG  1 
ATOM   4298 C CD  . GLU B 2 65  ? 20.776 6.419   -7.022  1.00 59.13  ? 65  GLU B CD  1 
ATOM   4299 O OE1 . GLU B 2 65  ? 19.599 6.839   -7.086  1.00 59.36  ? 65  GLU B OE1 1 
ATOM   4300 O OE2 . GLU B 2 65  ? 21.218 5.788   -6.036  1.00 60.81  ? 65  GLU B OE2 1 
ATOM   4301 N N   . ASP B 2 66  ? 22.344 10.778  -6.645  1.00 40.78  ? 66  ASP B N   1 
ATOM   4302 C CA  . ASP B 2 66  ? 22.711 11.793  -5.664  1.00 35.26  ? 66  ASP B CA  1 
ATOM   4303 C C   . ASP B 2 66  ? 23.030 11.213  -4.284  1.00 33.37  ? 66  ASP B C   1 
ATOM   4304 O O   . ASP B 2 66  ? 22.395 10.254  -3.844  1.00 30.07  ? 66  ASP B O   1 
ATOM   4305 C CB  . ASP B 2 66  ? 21.582 12.824  -5.561  1.00 30.59  ? 66  ASP B CB  1 
ATOM   4306 C CG  . ASP B 2 66  ? 21.135 13.335  -6.928  1.00 29.31  ? 66  ASP B CG  1 
ATOM   4307 O OD1 . ASP B 2 66  ? 22.014 13.637  -7.759  1.00 29.86  ? 66  ASP B OD1 1 
ATOM   4308 O OD2 . ASP B 2 66  ? 19.914 13.443  -7.173  1.00 23.67  ? 66  ASP B OD2 1 
ATOM   4309 N N   . VAL B 2 67  ? 24.015 11.807  -3.609  1.00 32.65  ? 67  VAL B N   1 
ATOM   4310 C CA  . VAL B 2 67  ? 24.447 11.358  -2.280  1.00 32.25  ? 67  VAL B CA  1 
ATOM   4311 C C   . VAL B 2 67  ? 24.229 12.433  -1.209  1.00 31.84  ? 67  VAL B C   1 
ATOM   4312 O O   . VAL B 2 67  ? 24.712 13.557  -1.343  1.00 30.54  ? 67  VAL B O   1 
ATOM   4313 C CB  . VAL B 2 67  ? 25.956 10.980  -2.283  1.00 33.83  ? 67  VAL B CB  1 
ATOM   4314 C CG1 . VAL B 2 67  ? 26.391 10.530  -0.893  1.00 33.43  ? 67  VAL B CG1 1 
ATOM   4315 C CG2 . VAL B 2 67  ? 26.215 9.868   -3.308  1.00 34.52  ? 67  VAL B CG2 1 
ATOM   4316 N N   . VAL B 2 68  ? 23.520 12.079  -0.140  1.00 31.46  ? 68  VAL B N   1 
ATOM   4317 C CA  . VAL B 2 68  ? 23.246 13.017  0.952   1.00 32.20  ? 68  VAL B CA  1 
ATOM   4318 C C   . VAL B 2 68  ? 24.492 13.325  1.788   1.00 34.29  ? 68  VAL B C   1 
ATOM   4319 O O   . VAL B 2 68  ? 25.416 12.505  1.871   1.00 33.30  ? 68  VAL B O   1 
ATOM   4320 C CB  . VAL B 2 68  ? 22.148 12.471  1.910   1.00 31.22  ? 68  VAL B CB  1 
ATOM   4321 C CG1 . VAL B 2 68  ? 20.855 12.251  1.145   1.00 31.13  ? 68  VAL B CG1 1 
ATOM   4322 C CG2 . VAL B 2 68  ? 22.613 11.165  2.553   1.00 29.94  ? 68  VAL B CG2 1 
ATOM   4323 N N   . MET B 2 69  ? 24.509 14.509  2.402   1.00 34.83  ? 69  MET B N   1 
ATOM   4324 C CA  . MET B 2 69  ? 25.619 14.948  3.255   1.00 37.77  ? 69  MET B CA  1 
ATOM   4325 C C   . MET B 2 69  ? 25.123 14.948  4.709   1.00 37.96  ? 69  MET B C   1 
ATOM   4326 O O   . MET B 2 69  ? 24.153 15.625  5.028   1.00 36.84  ? 69  MET B O   1 
ATOM   4327 C CB  . MET B 2 69  ? 26.080 16.370  2.852   1.00 42.26  ? 69  MET B CB  1 
ATOM   4328 C CG  . MET B 2 69  ? 26.379 16.557  1.353   1.00 49.42  ? 69  MET B CG  1 
ATOM   4329 S SD  . MET B 2 69  ? 27.089 18.201  0.907   1.00 57.46  ? 69  MET B SD  1 
ATOM   4330 C CE  . MET B 2 69  ? 25.653 19.273  0.935   1.00 53.76  ? 69  MET B CE  1 
ATOM   4331 N N   . ALA B 2 70  ? 25.786 14.197  5.588   1.00 39.21  ? 70  ALA B N   1 
ATOM   4332 C CA  . ALA B 2 70  ? 25.379 14.138  6.998   1.00 39.91  ? 70  ALA B CA  1 
ATOM   4333 C C   . ALA B 2 70  ? 25.907 15.364  7.755   1.00 40.39  ? 70  ALA B C   1 
ATOM   4334 O O   . ALA B 2 70  ? 27.079 15.411  8.141   1.00 40.56  ? 70  ALA B O   1 
ATOM   4335 C CB  . ALA B 2 70  ? 25.901 12.854  7.640   1.00 39.47  ? 70  ALA B CB  1 
ATOM   4336 N N   . PHE B 2 71  ? 25.045 16.358  7.963   1.00 40.30  ? 71  PHE B N   1 
ATOM   4337 C CA  . PHE B 2 71  ? 25.460 17.574  8.659   1.00 40.24  ? 71  PHE B CA  1 
ATOM   4338 C C   . PHE B 2 71  ? 25.381 17.484  10.182  1.00 42.34  ? 71  PHE B C   1 
ATOM   4339 O O   . PHE B 2 71  ? 25.962 18.319  10.876  1.00 43.90  ? 71  PHE B O   1 
ATOM   4340 C CB  . PHE B 2 71  ? 24.625 18.782  8.207   1.00 36.90  ? 71  PHE B CB  1 
ATOM   4341 C CG  . PHE B 2 71  ? 24.843 19.189  6.771   1.00 34.25  ? 71  PHE B CG  1 
ATOM   4342 C CD1 . PHE B 2 71  ? 23.954 18.783  5.777   1.00 30.26  ? 71  PHE B CD1 1 
ATOM   4343 C CD2 . PHE B 2 71  ? 25.915 20.006  6.419   1.00 32.09  ? 71  PHE B CD2 1 
ATOM   4344 C CE1 . PHE B 2 71  ? 24.128 19.187  4.450   1.00 29.85  ? 71  PHE B CE1 1 
ATOM   4345 C CE2 . PHE B 2 71  ? 26.098 20.415  5.093   1.00 32.17  ? 71  PHE B CE2 1 
ATOM   4346 C CZ  . PHE B 2 71  ? 25.201 20.005  4.109   1.00 30.87  ? 71  PHE B CZ  1 
ATOM   4347 N N   . SER B 2 72  ? 24.666 16.486  10.697  1.00 44.30  ? 72  SER B N   1 
ATOM   4348 C CA  . SER B 2 72  ? 24.500 16.312  12.145  1.00 49.18  ? 72  SER B CA  1 
ATOM   4349 C C   . SER B 2 72  ? 25.801 16.129  12.929  1.00 51.90  ? 72  SER B C   1 
ATOM   4350 O O   . SER B 2 72  ? 26.682 15.377  12.515  1.00 50.42  ? 72  SER B O   1 
ATOM   4351 C CB  . SER B 2 72  ? 23.587 15.114  12.435  1.00 48.58  ? 72  SER B CB  1 
ATOM   4352 O OG  . SER B 2 72  ? 22.289 15.315  11.909  1.00 52.44  ? 72  SER B OG  1 
ATOM   4353 N N   . ARG B 2 73  ? 25.896 16.814  14.070  1.00 55.20  ? 73  ARG B N   1 
ATOM   4354 C CA  . ARG B 2 73  ? 27.061 16.742  14.955  1.00 59.33  ? 73  ARG B CA  1 
ATOM   4355 C C   . ARG B 2 73  ? 26.612 16.820  16.423  1.00 61.32  ? 73  ARG B C   1 
ATOM   4356 O O   . ARG B 2 73  ? 26.356 17.905  16.948  1.00 61.35  ? 73  ARG B O   1 
ATOM   4357 C CB  . ARG B 2 73  ? 28.038 17.882  14.641  1.00 60.93  ? 73  ARG B CB  1 
ATOM   4358 C CG  . ARG B 2 73  ? 28.725 17.766  13.281  1.00 62.95  ? 73  ARG B CG  1 
ATOM   4359 C CD  . ARG B 2 73  ? 29.651 16.554  13.241  1.00 64.45  ? 73  ARG B CD  1 
ATOM   4360 N NE  . ARG B 2 73  ? 30.331 16.394  11.958  1.00 66.78  ? 73  ARG B NE  1 
ATOM   4361 C CZ  . ARG B 2 73  ? 29.723 16.108  10.808  1.00 68.26  ? 73  ARG B CZ  1 
ATOM   4362 N NH1 . ARG B 2 73  ? 28.407 15.949  10.764  1.00 68.47  ? 73  ARG B NH1 1 
ATOM   4363 N NH2 . ARG B 2 73  ? 30.436 15.971  9.699   1.00 68.62  ? 73  ARG B NH2 1 
ATOM   4364 N N   . SER B 2 74  ? 26.526 15.661  17.074  1.00 63.64  ? 74  SER B N   1 
ATOM   4365 C CA  . SER B 2 74  ? 26.087 15.560  18.470  1.00 66.93  ? 74  SER B CA  1 
ATOM   4366 C C   . SER B 2 74  ? 27.032 16.180  19.502  1.00 68.63  ? 74  SER B C   1 
ATOM   4367 O O   . SER B 2 74  ? 28.186 16.488  19.200  1.00 68.37  ? 74  SER B O   1 
ATOM   4368 C CB  . SER B 2 74  ? 25.856 14.088  18.838  1.00 66.96  ? 74  SER B CB  1 
ATOM   4369 O OG  . SER B 2 74  ? 24.888 13.485  17.996  1.00 67.39  ? 74  SER B OG  1 
ATOM   4370 N N   . GLU B 2 75  ? 26.527 16.357  20.724  1.00 70.97  ? 75  GLU B N   1 
ATOM   4371 C CA  . GLU B 2 75  ? 27.317 16.918  21.820  1.00 72.62  ? 75  GLU B CA  1 
ATOM   4372 C C   . GLU B 2 75  ? 28.182 15.800  22.402  1.00 75.22  ? 75  GLU B C   1 
ATOM   4373 O O   . GLU B 2 75  ? 28.498 14.838  21.705  1.00 76.44  ? 75  GLU B O   1 
ATOM   4374 C CB  . GLU B 2 75  ? 26.410 17.486  22.918  1.00 70.21  ? 75  GLU B CB  1 
ATOM   4375 C CG  . GLU B 2 75  ? 25.280 18.379  22.432  1.00 67.29  ? 75  GLU B CG  1 
ATOM   4376 C CD  . GLU B 2 75  ? 24.074 17.591  21.953  1.00 64.78  ? 75  GLU B CD  1 
ATOM   4377 O OE1 . GLU B 2 75  ? 23.540 16.778  22.739  1.00 61.89  ? 75  GLU B OE1 1 
ATOM   4378 O OE2 . GLU B 2 75  ? 23.656 17.792  20.795  1.00 63.74  ? 75  GLU B OE2 1 
ATOM   4379 N N   . THR B 2 76  ? 28.550 15.907  23.676  1.00 78.31  ? 76  THR B N   1 
ATOM   4380 C CA  . THR B 2 76  ? 29.391 14.883  24.293  1.00 81.11  ? 76  THR B CA  1 
ATOM   4381 C C   . THR B 2 76  ? 28.860 14.220  25.563  1.00 82.72  ? 76  THR B C   1 
ATOM   4382 O O   . THR B 2 76  ? 28.224 14.860  26.402  1.00 82.88  ? 76  THR B O   1 
ATOM   4383 C CB  . THR B 2 76  ? 30.799 15.437  24.610  1.00 81.63  ? 76  THR B CB  1 
ATOM   4384 O OG1 . THR B 2 76  ? 30.679 16.699  25.279  1.00 82.18  ? 76  THR B OG1 1 
ATOM   4385 C CG2 . THR B 2 76  ? 31.608 15.606  23.334  1.00 81.72  ? 76  THR B CG2 1 
ATOM   4386 N N   . GLU B 2 77  ? 29.140 12.922  25.676  1.00 84.84  ? 77  GLU B N   1 
ATOM   4387 C CA  . GLU B 2 77  ? 28.761 12.100  26.824  1.00 86.81  ? 77  GLU B CA  1 
ATOM   4388 C C   . GLU B 2 77  ? 27.274 11.799  26.996  1.00 88.32  ? 77  GLU B C   1 
ATOM   4389 O O   . GLU B 2 77  ? 26.483 11.885  26.054  1.00 88.56  ? 77  GLU B O   1 
ATOM   4390 C CB  . GLU B 2 77  ? 29.313 12.726  28.106  1.00 86.76  ? 77  GLU B CB  1 
ATOM   4391 N N   . ASP B 2 78  ? 26.919 11.427  28.223  1.00 89.75  ? 78  ASP B N   1 
ATOM   4392 C CA  . ASP B 2 78  ? 25.549 11.096  28.594  1.00 90.77  ? 78  ASP B CA  1 
ATOM   4393 C C   . ASP B 2 78  ? 25.340 11.516  30.048  1.00 91.51  ? 78  ASP B C   1 
ATOM   4394 O O   . ASP B 2 78  ? 25.215 10.624  30.916  1.00 92.00  ? 78  ASP B O   1 
ATOM   4395 C CB  . ASP B 2 78  ? 25.310 9.591   28.443  1.00 91.20  ? 78  ASP B CB  1 
ATOM   4396 C CG  . ASP B 2 78  ? 23.861 9.199   28.680  1.00 91.36  ? 78  ASP B CG  1 
ATOM   4397 O OD1 . ASP B 2 78  ? 23.336 9.465   29.783  1.00 91.83  ? 78  ASP B OD1 1 
ATOM   4398 O OD2 . ASP B 2 78  ? 23.249 8.617   27.761  1.00 91.25  ? 78  ASP B OD2 1 
HETATM 4399 O O   . HOH C 3 .   ? 13.808 7.321   33.548  1.00 43.23  ? 672 HOH A O   1 
HETATM 4400 O O   . HOH C 3 .   ? 25.227 23.890  5.045   1.00 23.28  ? 673 HOH A O   1 
HETATM 4401 O O   . HOH C 3 .   ? 44.525 20.595  -27.395 1.00 22.02  ? 674 HOH A O   1 
HETATM 4402 O O   . HOH C 3 .   ? 26.377 7.582   -24.779 1.00 26.19  ? 675 HOH A O   1 
HETATM 4403 O O   . HOH C 3 .   ? 9.105  15.879  8.120   1.00 23.11  ? 676 HOH A O   1 
HETATM 4404 O O   . HOH C 3 .   ? 27.733 11.800  -29.511 1.00 28.70  ? 677 HOH A O   1 
HETATM 4405 O O   . HOH C 3 .   ? 37.126 27.726  -3.775  1.00 26.88  ? 678 HOH A O   1 
HETATM 4406 O O   . HOH C 3 .   ? 6.135  23.848  5.622   1.00 28.62  ? 679 HOH A O   1 
HETATM 4407 O O   . HOH C 3 .   ? 29.034 11.270  -24.500 1.00 23.37  ? 680 HOH A O   1 
HETATM 4408 O O   . HOH C 3 .   ? 27.390 31.530  -18.086 1.00 26.97  ? 681 HOH A O   1 
HETATM 4409 O O   . HOH C 3 .   ? -2.598 28.650  18.964  1.00 25.26  ? 682 HOH A O   1 
HETATM 4410 O O   . HOH C 3 .   ? 15.902 16.902  45.833  1.00 25.04  ? 683 HOH A O   1 
HETATM 4411 O O   . HOH C 3 .   ? 37.785 12.899  -32.372 1.00 22.56  ? 684 HOH A O   1 
HETATM 4412 O O   . HOH C 3 .   ? 16.176 10.648  3.182   1.00 27.10  ? 685 HOH A O   1 
HETATM 4413 O O   . HOH C 3 .   ? 11.644 29.371  29.480  1.00 31.25  ? 686 HOH A O   1 
HETATM 4414 O O   . HOH C 3 .   ? 30.029 15.837  -33.442 1.00 22.38  ? 687 HOH A O   1 
HETATM 4415 O O   . HOH C 3 .   ? 6.747  10.900  18.952  1.00 31.08  ? 688 HOH A O   1 
HETATM 4416 O O   . HOH C 3 .   ? 45.139 22.885  -16.402 1.00 25.87  ? 689 HOH A O   1 
HETATM 4417 O O   . HOH C 3 .   ? 38.622 24.167  -22.569 1.00 23.73  ? 690 HOH A O   1 
HETATM 4418 O O   . HOH C 3 .   ? -0.520 21.436  23.186  1.00 29.80  ? 691 HOH A O   1 
HETATM 4419 O O   . HOH C 3 .   ? 45.605 12.215  -27.858 1.00 24.92  ? 692 HOH A O   1 
HETATM 4420 O O   . HOH C 3 .   ? 21.230 23.177  -26.286 1.00 26.24  ? 693 HOH A O   1 
HETATM 4421 O O   . HOH C 3 .   ? 32.922 14.185  -9.845  1.00 23.36  ? 694 HOH A O   1 
HETATM 4422 O O   . HOH C 3 .   ? 28.005 23.624  4.548   1.00 25.83  ? 695 HOH A O   1 
HETATM 4423 O O   . HOH C 3 .   ? 16.374 12.690  -9.636  1.00 25.33  ? 696 HOH A O   1 
HETATM 4424 O O   . HOH C 3 .   ? 6.400  31.869  13.392  1.00 25.49  ? 697 HOH A O   1 
HETATM 4425 O O   . HOH C 3 .   ? 20.975 33.801  11.714  1.00 26.93  ? 698 HOH A O   1 
HETATM 4426 O O   . HOH C 3 .   ? 16.542 33.851  -3.580  1.00 29.80  ? 699 HOH A O   1 
HETATM 4427 O O   . HOH C 3 .   ? 27.913 25.085  -27.613 1.00 22.11  ? 700 HOH A O   1 
HETATM 4428 O O   . HOH C 3 .   ? 18.906 37.044  9.861   1.00 42.00  ? 701 HOH A O   1 
HETATM 4429 O O   . HOH C 3 .   ? 11.643 31.813  38.609  1.00 48.38  ? 702 HOH A O   1 
HETATM 4430 O O   . HOH C 3 .   ? 35.730 21.401  -0.398  1.00 29.10  ? 703 HOH A O   1 
HETATM 4431 O O   . HOH C 3 .   ? 31.372 11.275  -37.474 1.00 34.74  ? 704 HOH A O   1 
HETATM 4432 O O   . HOH C 3 .   ? 7.420  9.888   14.562  1.00 31.72  ? 705 HOH A O   1 
HETATM 4433 O O   . HOH C 3 .   ? 2.478  27.270  14.508  1.00 25.68  ? 706 HOH A O   1 
HETATM 4434 O O   . HOH C 3 .   ? 28.734 13.629  -31.498 1.00 30.93  ? 707 HOH A O   1 
HETATM 4435 O O   . HOH C 3 .   ? 2.090  18.892  21.890  1.00 21.57  ? 708 HOH A O   1 
HETATM 4436 O O   . HOH C 3 .   ? 15.446 27.547  -11.594 1.00 25.26  ? 709 HOH A O   1 
HETATM 4437 O O   . HOH C 3 .   ? 15.299 11.802  42.342  1.00 35.87  ? 710 HOH A O   1 
HETATM 4438 O O   . HOH C 3 .   ? 49.331 16.866  -28.963 1.00 23.92  ? 711 HOH A O   1 
HETATM 4439 O O   . HOH C 3 .   ? 34.511 28.444  -2.864  1.00 25.17  ? 712 HOH A O   1 
HETATM 4440 O O   . HOH C 3 .   ? 0.589  16.804  21.157  1.00 34.00  ? 713 HOH A O   1 
HETATM 4441 O O   . HOH C 3 .   ? 27.197 9.779   -23.172 1.00 20.81  ? 714 HOH A O   1 
HETATM 4442 O O   . HOH C 3 .   ? 6.401  22.482  3.127   1.00 21.70  ? 715 HOH A O   1 
HETATM 4443 O O   . HOH C 3 .   ? 25.770 28.747  -26.076 1.00 34.93  ? 716 HOH A O   1 
HETATM 4444 O O   . HOH C 3 .   ? 19.832 25.374  -25.226 1.00 30.40  ? 717 HOH A O   1 
HETATM 4445 O O   . HOH C 3 .   ? 13.014 10.815  33.801  1.00 28.59  ? 718 HOH A O   1 
HETATM 4446 O O   . HOH C 3 .   ? 29.915 18.512  -32.982 1.00 26.47  ? 719 HOH A O   1 
HETATM 4447 O O   . HOH C 3 .   ? 30.770 10.220  -14.675 1.00 41.59  ? 720 HOH A O   1 
HETATM 4448 O O   . HOH C 3 .   ? 32.454 31.074  -5.880  1.00 29.98  ? 721 HOH A O   1 
HETATM 4449 O O   . HOH C 3 .   ? 21.854 16.054  7.636   1.00 25.58  ? 722 HOH A O   1 
HETATM 4450 O O   . HOH C 3 .   ? 24.814 16.887  -25.188 1.00 29.79  ? 723 HOH A O   1 
HETATM 4451 O O   . HOH C 3 .   ? 15.543 38.847  16.189  1.00 30.42  ? 724 HOH A O   1 
HETATM 4452 O O   . HOH C 3 .   ? 44.164 15.668  -9.497  1.00 31.54  ? 725 HOH A O   1 
HETATM 4453 O O   . HOH C 3 .   ? 3.948  18.860  9.560   1.00 26.00  ? 726 HOH A O   1 
HETATM 4454 O O   . HOH C 3 .   ? 29.510 8.939   -18.922 1.00 33.44  ? 727 HOH A O   1 
HETATM 4455 O O   . HOH C 3 .   ? -0.731 30.699  19.459  1.00 24.49  ? 728 HOH A O   1 
HETATM 4456 O O   . HOH C 3 .   ? 13.746 9.220   7.607   1.00 39.18  ? 729 HOH A O   1 
HETATM 4457 O O   . HOH C 3 .   ? 28.198 20.696  -29.696 1.00 29.18  ? 730 HOH A O   1 
HETATM 4458 O O   . HOH C 3 .   ? 36.159 -10.658 -24.494 1.00 38.13  ? 731 HOH A O   1 
HETATM 4459 O O   . HOH C 3 .   ? 32.004 16.144  -3.142  1.00 30.35  ? 732 HOH A O   1 
HETATM 4460 O O   . HOH C 3 .   ? 38.148 27.891  -1.115  1.00 34.76  ? 733 HOH A O   1 
HETATM 4461 O O   . HOH C 3 .   ? 12.339 29.512  35.815  1.00 28.01  ? 734 HOH A O   1 
HETATM 4462 O O   . HOH C 3 .   ? 28.977 6.407   -17.489 1.00 37.11  ? 735 HOH A O   1 
HETATM 4463 O O   . HOH C 3 .   ? 10.861 14.486  -13.184 1.00 35.32  ? 736 HOH A O   1 
HETATM 4464 O O   . HOH C 3 .   ? 22.191 17.458  30.182  1.00 32.65  ? 737 HOH A O   1 
HETATM 4465 O O   . HOH C 3 .   ? 16.282 30.043  -12.218 1.00 28.12  ? 738 HOH A O   1 
HETATM 4466 O O   . HOH C 3 .   ? 41.917 2.593   -11.924 1.00 37.74  ? 739 HOH A O   1 
HETATM 4467 O O   . HOH C 3 .   ? 39.063 28.288  -7.451  1.00 35.51  ? 740 HOH A O   1 
HETATM 4468 O O   . HOH C 3 .   ? 20.101 13.794  -16.884 1.00 33.54  ? 741 HOH A O   1 
HETATM 4469 O O   . HOH C 3 .   ? 30.046 7.589   -26.039 1.00 31.90  ? 742 HOH A O   1 
HETATM 4470 O O   . HOH C 3 .   ? 11.508 15.360  0.425   1.00 28.16  ? 743 HOH A O   1 
HETATM 4471 O O   . HOH C 3 .   ? 16.449 13.512  -16.849 1.00 40.07  ? 744 HOH A O   1 
HETATM 4472 O O   . HOH C 3 .   ? 3.742  16.945  -2.017  1.00 48.90  ? 745 HOH A O   1 
HETATM 4473 O O   . HOH C 3 .   ? -3.768 28.546  31.985  1.00 35.24  ? 746 HOH A O   1 
HETATM 4474 O O   . HOH C 3 .   ? 18.163 34.263  22.812  1.00 37.24  ? 747 HOH A O   1 
HETATM 4475 O O   . HOH C 3 .   ? 7.327  30.927  30.205  1.00 27.29  ? 748 HOH A O   1 
HETATM 4476 O O   . HOH C 3 .   ? 19.337 30.449  20.633  1.00 44.11  ? 749 HOH A O   1 
HETATM 4477 O O   . HOH C 3 .   ? 42.541 25.648  -18.264 1.00 28.72  ? 750 HOH A O   1 
HETATM 4478 O O   . HOH C 3 .   ? 23.258 20.799  16.128  1.00 34.71  ? 751 HOH A O   1 
HETATM 4479 O O   . HOH C 3 .   ? 10.505 19.189  59.435  1.00 39.92  ? 752 HOH A O   1 
HETATM 4480 O O   . HOH C 3 .   ? -6.394 23.760  28.171  1.00 30.66  ? 753 HOH A O   1 
HETATM 4481 O O   . HOH C 3 .   ? 32.203 -11.721 -17.915 1.00 26.19  ? 754 HOH A O   1 
HETATM 4482 O O   . HOH C 3 .   ? 15.734 33.102  -8.012  1.00 33.67  ? 755 HOH A O   1 
HETATM 4483 O O   . HOH C 3 .   ? 2.788  14.691  33.766  1.00 37.99  ? 756 HOH A O   1 
HETATM 4484 O O   . HOH C 3 .   ? 24.817 19.454  13.958  1.00 42.07  ? 757 HOH A O   1 
HETATM 4485 O O   . HOH C 3 .   ? 20.876 33.995  -4.096  1.00 33.17  ? 758 HOH A O   1 
HETATM 4486 O O   . HOH C 3 .   ? 17.562 36.920  5.875   1.00 38.59  ? 759 HOH A O   1 
HETATM 4487 O O   . HOH C 3 .   ? 0.004  24.799  11.305  1.00 38.05  ? 760 HOH A O   1 
HETATM 4488 O O   . HOH C 3 .   ? 7.327  32.123  9.024   1.00 32.50  ? 761 HOH A O   1 
HETATM 4489 O O   . HOH C 3 .   ? 15.249 31.571  36.391  1.00 38.10  ? 762 HOH A O   1 
HETATM 4490 O O   . HOH C 3 .   ? 13.849 5.109   22.664  1.00 31.15  ? 763 HOH A O   1 
HETATM 4491 O O   . HOH C 3 .   ? -3.507 19.734  23.204  1.00 40.89  ? 764 HOH A O   1 
HETATM 4492 O O   . HOH C 3 .   ? 30.798 7.617   -13.551 1.00 35.34  ? 765 HOH A O   1 
HETATM 4493 O O   . HOH C 3 .   ? 22.056 21.054  29.849  1.00 31.03  ? 766 HOH A O   1 
HETATM 4494 O O   . HOH C 3 .   ? 19.656 15.489  -18.772 1.00 39.49  ? 767 HOH A O   1 
HETATM 4495 O O   . HOH C 3 .   ? 21.328 23.428  28.072  1.00 39.85  ? 768 HOH A O   1 
HETATM 4496 O O   . HOH C 3 .   ? 33.724 -5.016  -16.743 1.00 38.01  ? 769 HOH A O   1 
HETATM 4497 O O   . HOH C 3 .   ? 5.198  35.806  20.306  1.00 30.88  ? 770 HOH A O   1 
HETATM 4498 O O   . HOH C 3 .   ? 43.878 17.662  -32.000 1.00 34.59  ? 771 HOH A O   1 
HETATM 4499 O O   . HOH C 3 .   ? 8.167  35.472  22.749  1.00 34.27  ? 772 HOH A O   1 
HETATM 4500 O O   . HOH C 3 .   ? 24.627 14.248  -11.205 1.00 39.03  ? 773 HOH A O   1 
HETATM 4501 O O   . HOH C 3 .   ? 36.349 28.018  2.869   1.00 36.49  ? 774 HOH A O   1 
HETATM 4502 O O   . HOH C 3 .   ? 15.193 25.237  24.803  1.00 33.94  ? 775 HOH A O   1 
HETATM 4503 O O   . HOH C 3 .   ? 35.934 5.714   -9.120  1.00 31.47  ? 776 HOH A O   1 
HETATM 4504 O O   . HOH C 3 .   ? 5.185  14.067  7.529   1.00 37.03  ? 777 HOH A O   1 
HETATM 4505 O O   . HOH C 3 .   ? 21.652 21.533  37.149  1.00 38.26  ? 778 HOH A O   1 
HETATM 4506 O O   . HOH C 3 .   ? 45.943 24.457  -13.500 1.00 43.06  ? 779 HOH A O   1 
HETATM 4507 O O   . HOH C 3 .   ? 6.849  17.696  -1.677  1.00 39.80  ? 780 HOH A O   1 
HETATM 4508 O O   . HOH C 3 .   ? 8.362  36.710  16.433  1.00 33.75  ? 781 HOH A O   1 
HETATM 4509 O O   . HOH C 3 .   ? 32.428 0.801   -10.644 1.00 40.84  ? 782 HOH A O   1 
HETATM 4510 O O   . HOH C 3 .   ? 8.704  15.422  -2.202  1.00 33.04  ? 783 HOH A O   1 
HETATM 4511 O O   . HOH C 3 .   ? 15.921 30.561  -14.857 1.00 36.82  ? 784 HOH A O   1 
HETATM 4512 O O   . HOH C 3 .   ? 38.184 -7.812  -30.869 1.00 48.07  ? 785 HOH A O   1 
HETATM 4513 O O   . HOH C 3 .   ? 7.572  36.589  26.266  1.00 41.96  ? 786 HOH A O   1 
HETATM 4514 O O   . HOH C 3 .   ? 2.483  14.578  25.206  1.00 37.07  ? 787 HOH A O   1 
HETATM 4515 O O   . HOH C 3 .   ? 20.894 26.280  56.938  1.00 43.72  ? 788 HOH A O   1 
HETATM 4516 O O   . HOH C 3 .   ? 48.842 16.954  -21.638 1.00 30.41  ? 789 HOH A O   1 
HETATM 4517 O O   . HOH C 3 .   ? 32.160 22.569  2.804   1.00 37.47  ? 790 HOH A O   1 
HETATM 4518 O O   . HOH C 3 .   ? 8.774  32.191  2.257   1.00 49.47  ? 791 HOH A O   1 
HETATM 4519 O O   . HOH C 3 .   ? 8.377  11.552  42.491  1.00 42.12  ? 792 HOH A O   1 
HETATM 4520 O O   . HOH C 3 .   ? 18.144 33.803  11.569  1.00 33.68  ? 793 HOH A O   1 
HETATM 4521 O O   . HOH C 3 .   ? 35.842 11.601  -39.755 1.00 40.36  ? 794 HOH A O   1 
HETATM 4522 O O   . HOH C 3 .   ? -0.023 31.994  31.739  1.00 45.34  ? 795 HOH A O   1 
HETATM 4523 O O   . HOH C 3 .   ? 22.077 23.657  33.490  1.00 39.38  ? 796 HOH A O   1 
HETATM 4524 O O   . HOH C 3 .   ? 3.159  20.376  3.967   1.00 39.59  ? 797 HOH A O   1 
HETATM 4525 O O   . HOH C 3 .   ? 31.216 23.902  -30.108 1.00 44.86  ? 798 HOH A O   1 
HETATM 4526 O O   . HOH C 3 .   ? 27.406 14.393  -12.132 1.00 33.40  ? 799 HOH A O   1 
HETATM 4527 O O   . HOH C 3 .   ? 39.835 27.976  -16.370 1.00 37.24  ? 800 HOH A O   1 
HETATM 4528 O O   . HOH C 3 .   ? 21.884 23.817  -28.852 1.00 31.27  ? 801 HOH A O   1 
HETATM 4529 O O   . HOH C 3 .   ? 10.029 9.999   5.120   1.00 33.12  ? 802 HOH A O   1 
HETATM 4530 O O   . HOH C 3 .   ? 43.955 25.342  -16.215 1.00 31.68  ? 803 HOH A O   1 
HETATM 4531 O O   . HOH C 3 .   ? 6.042  26.322  4.826   1.00 30.72  ? 804 HOH A O   1 
HETATM 4532 O O   . HOH C 3 .   ? 40.769 24.672  -24.092 1.00 27.39  ? 805 HOH A O   1 
HETATM 4533 O O   . HOH C 3 .   ? -8.365 23.167  26.736  1.00 31.38  ? 806 HOH A O   1 
HETATM 4534 O O   . HOH C 3 .   ? 23.268 16.397  37.602  1.00 28.87  ? 807 HOH A O   1 
HETATM 4535 O O   . HOH C 3 .   ? 14.746 33.611  -5.244  1.00 34.27  ? 808 HOH A O   1 
HETATM 4536 O O   . HOH C 3 .   ? 16.762 35.518  10.017  1.00 29.87  ? 809 HOH A O   1 
HETATM 4537 O O   . HOH C 3 .   ? 37.687 29.748  -5.349  1.00 33.71  ? 810 HOH A O   1 
HETATM 4538 O O   . HOH C 3 .   ? 0.341  27.456  10.283  1.00 34.23  ? 811 HOH A O   1 
HETATM 4539 O O   . HOH C 3 .   ? 45.748 18.043  -8.841  1.00 36.58  ? 812 HOH A O   1 
HETATM 4540 O O   . HOH C 3 .   ? 3.357  21.600  8.929   1.00 26.35  ? 813 HOH A O   1 
HETATM 4541 O O   . HOH C 3 .   ? -2.812 32.660  31.911  1.00 31.40  ? 814 HOH A O   1 
HETATM 4542 O O   . HOH C 3 .   ? 12.422 10.953  4.206   1.00 29.82  ? 815 HOH A O   1 
HETATM 4543 O O   . HOH C 3 .   ? 39.871 14.348  -32.144 1.00 33.08  ? 816 HOH A O   1 
HETATM 4544 O O   . HOH C 3 .   ? -4.680 26.917  30.074  1.00 27.78  ? 817 HOH A O   1 
HETATM 4545 O O   . HOH C 3 .   ? 1.780  29.087  12.786  1.00 40.38  ? 818 HOH A O   1 
HETATM 4546 O O   . HOH C 3 .   ? 0.624  20.943  21.071  1.00 33.94  ? 819 HOH A O   1 
HETATM 4547 O O   . HOH C 3 .   ? -0.410 19.603  14.714  1.00 33.20  ? 820 HOH A O   1 
HETATM 4548 O O   . HOH C 3 .   ? 3.145  22.416  6.331   1.00 37.99  ? 821 HOH A O   1 
HETATM 4549 O O   . HOH C 3 .   ? 17.894 9.973   -1.338  1.00 36.25  ? 822 HOH A O   1 
HETATM 4550 O O   . HOH C 3 .   ? 19.012 25.614  54.985  1.00 40.11  ? 823 HOH A O   1 
HETATM 4551 O O   . HOH C 3 .   ? 18.524 35.022  -4.754  1.00 38.71  ? 824 HOH A O   1 
HETATM 4552 O O   . HOH C 3 .   ? 40.259 30.516  -8.362  1.00 43.37  ? 825 HOH A O   1 
HETATM 4553 O O   . HOH C 3 .   ? 14.665 10.743  -2.568  1.00 40.43  ? 826 HOH A O   1 
HETATM 4554 O O   . HOH C 3 .   ? 44.841 -1.527  -31.318 1.00 38.21  ? 827 HOH A O   1 
HETATM 4555 O O   . HOH C 3 .   ? 39.017 22.996  -31.013 1.00 33.21  ? 828 HOH A O   1 
HETATM 4556 O O   . HOH C 3 .   ? 23.010 22.075  11.399  1.00 33.68  ? 829 HOH A O   1 
HETATM 4557 O O   . HOH C 3 .   ? 27.252 27.623  -27.992 1.00 33.92  ? 830 HOH A O   1 
HETATM 4558 O O   . HOH C 3 .   ? 14.126 9.433   42.757  1.00 50.78  ? 831 HOH A O   1 
HETATM 4559 O O   . HOH C 3 .   ? 16.775 15.142  -18.868 1.00 36.85  ? 832 HOH A O   1 
HETATM 4560 O O   . HOH C 3 .   ? 0.962  22.411  9.707   1.00 35.94  ? 833 HOH A O   1 
HETATM 4561 O O   . HOH C 3 .   ? 26.527 8.779   -20.760 1.00 26.54  ? 834 HOH A O   1 
HETATM 4562 O O   . HOH C 3 .   ? 17.909 34.571  -7.461  1.00 42.41  ? 835 HOH A O   1 
HETATM 4563 O O   . HOH C 3 .   ? 44.633 20.304  -7.875  1.00 37.83  ? 836 HOH A O   1 
HETATM 4564 O O   . HOH C 3 .   ? 22.849 9.082   17.705  1.00 50.11  ? 837 HOH A O   1 
HETATM 4565 O O   . HOH C 3 .   ? 45.341 14.037  -7.486  1.00 35.74  ? 838 HOH A O   1 
HETATM 4566 O O   . HOH C 3 .   ? 23.658 15.591  32.574  1.00 42.79  ? 839 HOH A O   1 
HETATM 4567 O O   . HOH C 3 .   ? 10.617 30.956  -3.443  1.00 36.73  ? 840 HOH A O   1 
HETATM 4568 O O   . HOH C 3 .   ? 23.641 10.327  6.343   1.00 38.03  ? 841 HOH A O   1 
HETATM 4569 O O   . HOH C 3 .   ? 36.155 3.946   -6.973  1.00 42.44  ? 842 HOH A O   1 
HETATM 4570 O O   . HOH C 3 .   ? 36.345 30.569  -15.253 1.00 31.05  ? 843 HOH A O   1 
HETATM 4571 O O   . HOH C 3 .   ? 32.895 18.228  2.737   1.00 37.27  ? 844 HOH A O   1 
HETATM 4572 O O   . HOH C 3 .   ? 15.793 26.207  -14.024 1.00 36.76  ? 845 HOH A O   1 
HETATM 4573 O O   . HOH C 3 .   ? 13.683 20.475  -19.330 1.00 32.61  ? 846 HOH A O   1 
HETATM 4574 O O   . HOH C 3 .   ? 16.527 27.329  -19.168 1.00 45.56  ? 847 HOH A O   1 
HETATM 4575 O O   . HOH C 3 .   ? 17.383 24.360  62.125  1.00 43.88  ? 848 HOH A O   1 
HETATM 4576 O O   . HOH C 3 .   ? 31.289 13.207  -11.451 1.00 36.56  ? 849 HOH A O   1 
HETATM 4577 O O   . HOH C 3 .   ? 5.957  33.146  10.826  1.00 36.17  ? 850 HOH A O   1 
HETATM 4578 O O   . HOH C 3 .   ? 24.736 16.011  -28.056 1.00 40.09  ? 851 HOH A O   1 
HETATM 4579 O O   . HOH C 3 .   ? 37.739 -12.958 -25.208 1.00 38.94  ? 852 HOH A O   1 
HETATM 4580 O O   . HOH C 3 .   ? 23.764 16.786  -0.522  1.00 35.43  ? 853 HOH A O   1 
HETATM 4581 O O   . HOH C 3 .   ? 10.854 13.871  48.652  1.00 42.91  ? 854 HOH A O   1 
HETATM 4582 O O   . HOH C 3 .   ? 5.491  12.868  3.606   1.00 44.96  ? 855 HOH A O   1 
HETATM 4583 O O   . HOH C 3 .   ? 29.104 -5.315  -27.171 1.00 34.85  ? 856 HOH A O   1 
HETATM 4584 O O   . HOH C 3 .   ? 6.745  21.648  -9.354  1.00 46.50  ? 857 HOH A O   1 
HETATM 4585 O O   . HOH C 3 .   ? 7.081  28.896  0.468   1.00 35.84  ? 858 HOH A O   1 
HETATM 4586 O O   . HOH C 3 .   ? 7.505  33.281  29.006  1.00 50.45  ? 859 HOH A O   1 
HETATM 4587 O O   . HOH C 3 .   ? 47.866 10.468  -22.433 1.00 40.96  ? 860 HOH A O   1 
HETATM 4588 O O   . HOH C 3 .   ? 26.351 33.325  -0.918  1.00 38.62  ? 861 HOH A O   1 
HETATM 4589 O O   . HOH C 3 .   ? 22.530 26.234  45.473  1.00 37.55  ? 862 HOH A O   1 
HETATM 4590 O O   . HOH C 3 .   ? 30.762 5.454   -15.280 1.00 29.85  ? 863 HOH A O   1 
HETATM 4591 O O   . HOH C 3 .   ? 20.466 7.025   19.055  1.00 46.82  ? 864 HOH A O   1 
HETATM 4592 O O   . HOH C 3 .   ? 24.419 31.999  -23.446 1.00 40.47  ? 865 HOH A O   1 
HETATM 4593 O O   . HOH C 3 .   ? 12.057 32.163  -5.192  1.00 34.05  ? 866 HOH A O   1 
HETATM 4594 O O   . HOH C 3 .   ? 31.266 12.213  -7.561  1.00 45.99  ? 867 HOH A O   1 
HETATM 4595 O O   . HOH C 3 .   ? 42.737 5.091   -12.034 1.00 41.14  ? 868 HOH A O   1 
HETATM 4596 O O   . HOH C 3 .   ? 46.759 -1.283  -24.463 1.00 39.65  ? 869 HOH A O   1 
HETATM 4597 O O   . HOH C 3 .   ? 45.949 -4.243  -28.637 1.00 45.19  ? 870 HOH A O   1 
HETATM 4598 O O   . HOH C 3 .   ? -3.738 19.378  54.107  1.00 49.34  ? 871 HOH A O   1 
HETATM 4599 O O   . HOH C 3 .   ? 3.183  12.323  21.862  1.00 46.47  ? 872 HOH A O   1 
HETATM 4600 O O   . HOH C 3 .   ? 38.521 29.401  -14.433 1.00 40.90  ? 873 HOH A O   1 
HETATM 4601 O O   . HOH C 3 .   ? 10.779 16.376  53.411  1.00 41.61  ? 874 HOH A O   1 
HETATM 4602 O O   . HOH C 3 .   ? 27.590 18.950  -31.372 1.00 42.55  ? 875 HOH A O   1 
HETATM 4603 O O   . HOH C 3 .   ? 13.387 6.097   15.748  1.00 46.31  ? 876 HOH A O   1 
HETATM 4604 O O   . HOH C 3 .   ? 28.825 24.827  -30.132 1.00 39.56  ? 877 HOH A O   1 
HETATM 4605 O O   . HOH C 3 .   ? 5.279  10.400  29.258  1.00 33.56  ? 878 HOH A O   1 
HETATM 4606 O O   . HOH C 3 .   ? 19.875 23.441  21.677  1.00 36.31  ? 879 HOH A O   1 
HETATM 4607 O O   . HOH C 3 .   ? 13.550 34.923  7.343   1.00 34.11  ? 880 HOH A O   1 
HETATM 4608 O O   . HOH C 3 .   ? 3.575  17.275  7.362   1.00 48.05  ? 881 HOH A O   1 
HETATM 4609 O O   . HOH C 3 .   ? 4.511  9.423   19.217  1.00 42.79  ? 882 HOH A O   1 
HETATM 4610 O O   . HOH C 3 .   ? 18.791 7.492   11.896  1.00 44.23  ? 883 HOH A O   1 
HETATM 4611 O O   . HOH C 3 .   ? 42.342 2.089   -9.239  1.00 43.41  ? 884 HOH A O   1 
HETATM 4612 O O   . HOH C 3 .   ? 25.476 27.743  11.177  1.00 44.48  ? 885 HOH A O   1 
HETATM 4613 O O   . HOH C 3 .   ? 29.556 21.754  3.611   1.00 34.42  ? 886 HOH A O   1 
HETATM 4614 O O   . HOH C 3 .   ? 35.512 6.897   -37.410 1.00 54.65  ? 887 HOH A O   1 
HETATM 4615 O O   . HOH C 3 .   ? 10.953 31.754  35.430  1.00 42.40  ? 888 HOH A O   1 
HETATM 4616 O O   . HOH C 3 .   ? 38.263 26.504  2.385   1.00 43.09  ? 889 HOH A O   1 
HETATM 4617 O O   . HOH C 3 .   ? 33.499 8.763   -39.333 1.00 46.70  ? 890 HOH A O   1 
HETATM 4618 O O   . HOH C 3 .   ? 26.296 22.357  -30.339 1.00 36.48  ? 891 HOH A O   1 
HETATM 4619 O O   . HOH C 3 .   ? 20.454 27.432  -26.687 1.00 39.67  ? 892 HOH A O   1 
HETATM 4620 O O   . HOH C 3 .   ? 8.488  27.442  4.502   1.00 32.19  ? 893 HOH A O   1 
HETATM 4621 O O   . HOH C 3 .   ? 40.536 -4.193  -20.466 1.00 33.06  ? 894 HOH A O   1 
HETATM 4622 O O   . HOH C 3 .   ? 25.136 26.064  46.365  1.00 45.04  ? 895 HOH A O   1 
HETATM 4623 O O   . HOH C 3 .   ? -7.170 25.204  30.489  1.00 38.24  ? 896 HOH A O   1 
HETATM 4624 O O   . HOH C 3 .   ? 15.061 8.286   4.068   1.00 45.49  ? 897 HOH A O   1 
HETATM 4625 O O   . HOH C 3 .   ? 16.915 29.174  29.708  1.00 41.59  ? 898 HOH A O   1 
HETATM 4626 O O   . HOH C 3 .   ? 11.484 4.431   21.501  1.00 42.21  ? 899 HOH A O   1 
HETATM 4627 O O   . HOH C 3 .   ? 14.739 31.304  33.846  1.00 46.87  ? 900 HOH A O   1 
HETATM 4628 O O   . HOH C 3 .   ? 3.732  10.952  26.902  1.00 45.71  ? 901 HOH A O   1 
HETATM 4629 O O   . HOH C 3 .   ? 20.342 14.675  -21.282 1.00 42.26  ? 902 HOH A O   1 
HETATM 4630 O O   . HOH C 3 .   ? 37.263 16.589  -34.218 1.00 42.86  ? 903 HOH A O   1 
HETATM 4631 O O   . HOH C 3 .   ? 15.249 17.153  -18.647 1.00 43.45  ? 904 HOH A O   1 
HETATM 4632 O O   . HOH C 3 .   ? -1.242 16.627  30.616  1.00 40.08  ? 905 HOH A O   1 
HETATM 4633 O O   . HOH C 3 .   ? 6.728  34.073  16.739  1.00 41.38  ? 906 HOH A O   1 
HETATM 4634 O O   . HOH C 3 .   ? 35.796 31.131  -6.560  1.00 50.00  ? 907 HOH A O   1 
HETATM 4635 O O   . HOH C 3 .   ? 3.840  30.425  8.306   1.00 44.72  ? 908 HOH A O   1 
HETATM 4636 O O   . HOH C 3 .   ? 28.092 14.875  -34.867 1.00 46.27  ? 909 HOH A O   1 
HETATM 4637 O O   . HOH C 3 .   ? -3.153 24.671  30.192  1.00 31.16  ? 910 HOH A O   1 
HETATM 4638 O O   . HOH C 3 .   ? 9.601  12.656  -6.175  1.00 41.27  ? 911 HOH A O   1 
HETATM 4639 O O   . HOH C 3 .   ? 24.659 24.338  -29.347 1.00 34.97  ? 912 HOH A O   1 
HETATM 4640 O O   . HOH C 3 .   ? 21.512 21.715  -30.766 1.00 32.55  ? 913 HOH A O   1 
HETATM 4641 O O   . HOH C 3 .   ? 14.582 24.124  -14.857 1.00 40.85  ? 914 HOH A O   1 
HETATM 4642 O O   . HOH C 3 .   ? 22.579 19.010  37.499  1.00 46.81  ? 915 HOH A O   1 
HETATM 4643 O O   . HOH C 3 .   ? 23.509 34.915  -1.101  1.00 52.57  ? 916 HOH A O   1 
HETATM 4644 O O   . HOH C 3 .   ? 25.157 18.442  44.581  1.00 47.00  ? 917 HOH A O   1 
HETATM 4645 O O   . HOH C 3 .   ? 33.956 -2.211  -10.272 1.00 49.34  ? 918 HOH A O   1 
HETATM 4646 O O   . HOH C 3 .   ? 37.354 17.089  -36.940 1.00 44.04  ? 919 HOH A O   1 
HETATM 4647 O O   . HOH C 3 .   ? 14.602 34.234  26.479  1.00 43.08  ? 920 HOH A O   1 
HETATM 4648 O O   . HOH C 3 .   ? 21.864 14.210  42.030  1.00 38.72  ? 921 HOH A O   1 
HETATM 4649 O O   . HOH C 3 .   ? 7.253  19.129  -8.293  1.00 42.29  ? 922 HOH A O   1 
HETATM 4650 O O   . HOH C 3 .   ? 11.598 24.438  -14.519 1.00 44.87  ? 923 HOH A O   1 
HETATM 4651 O O   . HOH C 3 .   ? 19.264 21.457  -25.635 1.00 45.52  ? 924 HOH A O   1 
HETATM 4652 O O   . HOH C 3 .   ? 5.650  35.701  13.604  1.00 41.24  ? 925 HOH A O   1 
HETATM 4653 O O   . HOH C 3 .   ? 16.355 35.063  7.560   1.00 42.85  ? 926 HOH A O   1 
HETATM 4654 O O   . HOH C 3 .   ? 24.382 34.631  11.710  1.00 38.89  ? 927 HOH A O   1 
HETATM 4655 O O   . HOH C 3 .   ? 23.043 12.582  20.692  1.00 46.57  ? 928 HOH A O   1 
HETATM 4656 O O   . HOH C 3 .   ? 6.469  11.078  40.569  1.00 40.48  ? 929 HOH A O   1 
HETATM 4657 O O   . HOH C 3 .   ? 25.107 24.246  42.511  1.00 41.62  ? 930 HOH A O   1 
HETATM 4658 O O   . HOH C 3 .   ? 40.222 31.037  -13.052 1.00 41.67  ? 931 HOH A O   1 
HETATM 4659 O O   . HOH C 3 .   ? 34.467 34.808  -19.391 1.00 48.86  ? 932 HOH A O   1 
HETATM 4660 O O   . HOH C 3 .   ? 17.197 5.729   27.826  1.00 39.07  ? 933 HOH A O   1 
HETATM 4661 O O   . HOH C 3 .   ? 28.814 23.921  7.185   1.00 43.87  ? 934 HOH A O   1 
HETATM 4662 O O   . HOH C 3 .   ? 34.022 13.451  -38.493 1.00 47.81  ? 935 HOH A O   1 
HETATM 4663 O O   . HOH C 3 .   ? 21.047 26.361  52.116  1.00 41.80  ? 936 HOH A O   1 
HETATM 4664 O O   . HOH C 3 .   ? 44.748 1.618   -15.331 1.00 42.27  ? 937 HOH A O   1 
HETATM 4665 O O   . HOH C 3 .   ? 7.732  9.271   35.192  1.00 43.53  ? 938 HOH A O   1 
HETATM 4666 O O   . HOH C 3 .   ? -4.453 22.635  29.083  1.00 42.54  ? 939 HOH A O   1 
HETATM 4667 O O   . HOH C 3 .   ? 11.427 10.859  -6.434  1.00 38.71  ? 940 HOH A O   1 
HETATM 4668 O O   . HOH C 3 .   ? 19.154 22.863  54.191  1.00 46.92  ? 941 HOH A O   1 
HETATM 4669 O O   . HOH C 3 .   ? 20.606 19.079  -29.691 1.00 39.59  ? 942 HOH A O   1 
HETATM 4670 O O   . HOH C 3 .   ? 22.683 11.065  13.267  1.00 40.51  ? 943 HOH A O   1 
HETATM 4671 O O   . HOH C 3 .   ? 8.119  30.434  -3.567  1.00 45.31  ? 944 HOH A O   1 
HETATM 4672 O O   . HOH C 3 .   ? 44.931 25.540  -11.490 1.00 41.40  ? 945 HOH A O   1 
HETATM 4673 O O   . HOH C 3 .   ? 32.410 3.760   -9.144  1.00 43.59  ? 946 HOH A O   1 
HETATM 4674 O O   . HOH C 3 .   ? 31.466 13.305  -13.991 1.00 42.66  ? 947 HOH A O   1 
HETATM 4675 O O   . HOH C 3 .   ? 23.301 21.825  32.225  1.00 50.86  ? 948 HOH A O   1 
HETATM 4676 O O   . HOH C 3 .   ? -1.943 28.551  10.239  1.00 42.91  ? 949 HOH A O   1 
HETATM 4677 O O   . HOH C 3 .   ? 33.494 30.734  -8.533  1.00 47.95  ? 950 HOH A O   1 
HETATM 4678 O O   . HOH C 3 .   ? 34.404 -11.258 -26.404 1.00 48.65  ? 951 HOH A O   1 
HETATM 4679 O O   . HOH C 3 .   ? 18.072 9.955   31.415  1.00 47.00  ? 952 HOH A O   1 
HETATM 4680 O O   . HOH C 3 .   ? 7.571  30.958  35.742  1.00 51.55  ? 953 HOH A O   1 
HETATM 4681 O O   . HOH C 3 .   ? 14.795 4.808   26.755  1.00 47.59  ? 954 HOH A O   1 
HETATM 4682 O O   . HOH C 3 .   ? 6.304  38.336  15.004  1.00 45.67  ? 955 HOH A O   1 
HETATM 4683 O O   . HOH C 3 .   ? 9.110  6.699   28.104  1.00 46.54  ? 956 HOH A O   1 
HETATM 4684 O O   . HOH C 3 .   ? 18.982 38.909  8.017   1.00 50.05  ? 957 HOH A O   1 
HETATM 4685 O O   . HOH D 3 .   ? 29.405 8.751   -30.805 1.00 24.12  ? 82  HOH B O   1 
HETATM 4686 O O   . HOH D 3 .   ? 24.859 8.456   -44.206 1.00 34.25  ? 83  HOH B O   1 
HETATM 4687 O O   . HOH D 3 .   ? 25.524 12.873  -28.208 1.00 25.33  ? 84  HOH B O   1 
HETATM 4688 O O   . HOH D 3 .   ? 27.503 -14.915 -45.282 1.00 27.91  ? 85  HOH B O   1 
HETATM 4689 O O   . HOH D 3 .   ? 25.472 13.562  -4.947  1.00 43.10  ? 86  HOH B O   1 
HETATM 4690 O O   . HOH D 3 .   ? 20.161 5.132   -40.660 1.00 33.91  ? 87  HOH B O   1 
HETATM 4691 O O   . HOH D 3 .   ? 31.204 8.150   -41.585 1.00 34.11  ? 88  HOH B O   1 
HETATM 4692 O O   . HOH D 3 .   ? 22.769 9.157   -0.012  1.00 29.48  ? 89  HOH B O   1 
HETATM 4693 O O   . HOH D 3 .   ? 21.763 12.500  -26.012 1.00 43.83  ? 90  HOH B O   1 
HETATM 4694 O O   . HOH D 3 .   ? 28.282 2.219   -44.626 1.00 44.79  ? 91  HOH B O   1 
HETATM 4695 O O   . HOH D 3 .   ? 24.486 10.799  -42.552 1.00 42.73  ? 92  HOH B O   1 
HETATM 4696 O O   . HOH D 3 .   ? 26.446 8.915   -46.104 1.00 45.42  ? 93  HOH B O   1 
HETATM 4697 O O   . HOH D 3 .   ? 24.479 14.033  -8.406  1.00 36.79  ? 94  HOH B O   1 
HETATM 4698 O O   . HOH D 3 .   ? 32.875 -1.632  -38.604 1.00 49.91  ? 95  HOH B O   1 
HETATM 4699 O O   . HOH D 3 .   ? 25.217 -21.630 -43.012 1.00 39.24  ? 96  HOH B O   1 
HETATM 4700 O O   . HOH D 3 .   ? 28.010 12.575  4.977   1.00 42.20  ? 97  HOH B O   1 
HETATM 4701 O O   . HOH D 3 .   ? 26.079 21.181  12.520  1.00 53.85  ? 98  HOH B O   1 
HETATM 4702 O O   . HOH D 3 .   ? 30.096 10.914  -39.832 1.00 43.84  ? 99  HOH B O   1 
HETATM 4703 O O   . HOH D 3 .   ? 17.447 1.115   -40.732 1.00 47.40  ? 100 HOH B O   1 
HETATM 4704 O O   . HOH D 3 .   ? 27.095 11.309  -46.147 1.00 41.17  ? 101 HOH B O   1 
HETATM 4705 O O   . HOH D 3 .   ? 21.890 1.800   -48.068 1.00 44.13  ? 102 HOH B O   1 
HETATM 4706 O O   . HOH D 3 .   ? 23.134 9.816   -34.573 1.00 37.13  ? 103 HOH B O   1 
HETATM 4707 O O   . HOH D 3 .   ? 29.092 7.227   -45.578 1.00 47.97  ? 104 HOH B O   1 
HETATM 4708 O O   . HOH D 3 .   ? 26.107 0.011   -45.560 1.00 44.82  ? 105 HOH B O   1 
# 
