data_8PU5
# 
_entry.id   8PU5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8PU5         pdb_00008pu5 10.2210/pdb8pu5/pdb 
WWPDB D_1292130035 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-12 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_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             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
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  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8PU5 
_pdbx_database_status.recvd_initial_deposition_date   2023-07-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mw240@cam.ac.uk 
_pdbx_contact_author.name_first         Martin 
_pdbx_contact_author.name_last          Welch 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3646-1733 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wang, M.'  1 0000-0001-9286-8242 
'Brear, P.' 2 0000-0002-4045-0474 
'Welch, M.' 3 0000-0003-3646-1733 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2334 
_citation.page_last                 2334 
_citation.title                     
'Pseudomonas aeruginosa acyl-CoA dehydrogenases and structure-guided inversion of their substrate specificity.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57532-z 
_citation.pdbx_database_id_PubMed   40057486 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wang, M.'         1  0000-0001-9286-8242 
primary 'Medarametla, P.'  2  ?                   
primary 'Kronenberger, T.' 3  0000-0001-6933-7590 
primary 'Deingruber, T.'   4  0000-0002-6017-9490 
primary 'Brear, P.'        5  0000-0002-4045-0474 
primary 'Figueroa, W.'     6  0000-0003-0882-5106 
primary 'Ho, P.M.'         7  0000-0001-5565-1415 
primary 'Krueger, T.'      8  0000-0002-8132-8870 
primary 'Pearce, J.C.'     9  ?                   
primary 'Poso, A.'         10 0000-0003-4196-4204 
primary 'Wakefield, J.G.'  11 ?                   
primary 'Spring, D.R.'     12 ?                   
primary 'Welch, M.'        13 0000-0003-3646-1733 
# 
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 'Probable acyl-CoA dehydrogenase'        65567.664 1   ? ? ? ? 
2 non-polymer syn Palmitoyl-CoA                            1005.943  1   ? ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                           62.068    4   ? ? ? ? 
4 non-polymer syn 'TRIETHYLENE GLYCOL'                     150.173   1   ? ? ? ? 
5 non-polymer syn 'NITRATE ION'                            62.005    2   ? ? ? ? 
6 non-polymer syn 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 122.143   1   ? ? ? ? 
7 water       nat water                                    18.015    413 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GHMPDYKAPLRDIRFVRDELLGYEAHYQSLPGAEDATPDMVNAILEEGAKFCEQVIAPLNRVGDLEGCTWSADGVKTPTG
FKEAYQQFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVGQANWSWGMYPGLSHGAMNTLHAHGTAEQQATYLTKLVSGE
WTGTMCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAGEHDMADNIVHIVLARLPDAPQGTKGISLFIVPKFLPN
AEGNAGERNAVSCGSIEHKMGIHGNATCVMNFDAATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYA
RERLQMRSLTGPKAPEKPADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDIVQRSQDEEQKKAADSMLAFLTPIAK
AFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYAGTTGVQALDLLGRKVLMTQGEALKGFTKIVHKFCQAN
EANEAVKEFVAPLAQLNKEWGDLTMKVGMAAMKDREEVGAASVDYLMYSGYACLAYFWADMARLAAEKLAAGTGEEAFYK
AKLQTARFYFQRILPRTRAHVAAMLSGANNLMEMAEEDFALGY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GHMPDYKAPLRDIRFVRDELLGYEAHYQSLPGAEDATPDMVNAILEEGAKFCEQVIAPLNRVGDLEGCTWSADGVKTPTG
FKEAYQQFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVGQANWSWGMYPGLSHGAMNTLHAHGTAEQQATYLTKLVSGE
WTGTMCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAGEHDMADNIVHIVLARLPDAPQGTKGISLFIVPKFLPN
AEGNAGERNAVSCGSIEHKMGIHGNATCVMNFDAATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYA
RERLQMRSLTGPKAPEKPADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDIVQRSQDEEQKKAADSMLAFLTPIAK
AFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYAGTTGVQALDLLGRKVLMTQGEALKGFTKIVHKFCQAN
EANEAVKEFVAPLAQLNKEWGDLTMKVGMAAMKDREEVGAASVDYLMYSGYACLAYFWADMARLAAEKLAAGTGEEAFYK
AKLQTARFYFQRILPRTRAHVAAMLSGANNLMEMAEEDFALGY
;
_entity_poly.pdbx_strand_id                 B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 Palmitoyl-CoA                            PKZ 
3 1,2-ETHANEDIOL                           EDO 
4 'TRIETHYLENE GLYCOL'                     PGE 
5 'NITRATE ION'                            NO3 
6 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL TRS 
7 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   HIS n 
1 3   MET n 
1 4   PRO n 
1 5   ASP n 
1 6   TYR n 
1 7   LYS n 
1 8   ALA n 
1 9   PRO n 
1 10  LEU n 
1 11  ARG n 
1 12  ASP n 
1 13  ILE n 
1 14  ARG n 
1 15  PHE n 
1 16  VAL n 
1 17  ARG n 
1 18  ASP n 
1 19  GLU n 
1 20  LEU n 
1 21  LEU n 
1 22  GLY n 
1 23  TYR n 
1 24  GLU n 
1 25  ALA n 
1 26  HIS n 
1 27  TYR n 
1 28  GLN n 
1 29  SER n 
1 30  LEU n 
1 31  PRO n 
1 32  GLY n 
1 33  ALA n 
1 34  GLU n 
1 35  ASP n 
1 36  ALA n 
1 37  THR n 
1 38  PRO n 
1 39  ASP n 
1 40  MET n 
1 41  VAL n 
1 42  ASN n 
1 43  ALA n 
1 44  ILE n 
1 45  LEU n 
1 46  GLU n 
1 47  GLU n 
1 48  GLY n 
1 49  ALA n 
1 50  LYS n 
1 51  PHE n 
1 52  CYS n 
1 53  GLU n 
1 54  GLN n 
1 55  VAL n 
1 56  ILE n 
1 57  ALA n 
1 58  PRO n 
1 59  LEU n 
1 60  ASN n 
1 61  ARG n 
1 62  VAL n 
1 63  GLY n 
1 64  ASP n 
1 65  LEU n 
1 66  GLU n 
1 67  GLY n 
1 68  CYS n 
1 69  THR n 
1 70  TRP n 
1 71  SER n 
1 72  ALA n 
1 73  ASP n 
1 74  GLY n 
1 75  VAL n 
1 76  LYS n 
1 77  THR n 
1 78  PRO n 
1 79  THR n 
1 80  GLY n 
1 81  PHE n 
1 82  LYS n 
1 83  GLU n 
1 84  ALA n 
1 85  TYR n 
1 86  GLN n 
1 87  GLN n 
1 88  PHE n 
1 89  VAL n 
1 90  GLU n 
1 91  GLY n 
1 92  GLY n 
1 93  TRP n 
1 94  PRO n 
1 95  SER n 
1 96  LEU n 
1 97  ALA n 
1 98  HIS n 
1 99  ASP n 
1 100 VAL n 
1 101 GLU n 
1 102 HIS n 
1 103 GLY n 
1 104 GLY n 
1 105 GLN n 
1 106 GLY n 
1 107 LEU n 
1 108 PRO n 
1 109 GLU n 
1 110 SER n 
1 111 LEU n 
1 112 GLY n 
1 113 LEU n 
1 114 ALA n 
1 115 ILE n 
1 116 SER n 
1 117 GLU n 
1 118 MET n 
1 119 VAL n 
1 120 GLY n 
1 121 GLN n 
1 122 ALA n 
1 123 ASN n 
1 124 TRP n 
1 125 SER n 
1 126 TRP n 
1 127 GLY n 
1 128 MET n 
1 129 TYR n 
1 130 PRO n 
1 131 GLY n 
1 132 LEU n 
1 133 SER n 
1 134 HIS n 
1 135 GLY n 
1 136 ALA n 
1 137 MET n 
1 138 ASN n 
1 139 THR n 
1 140 LEU n 
1 141 HIS n 
1 142 ALA n 
1 143 HIS n 
1 144 GLY n 
1 145 THR n 
1 146 ALA n 
1 147 GLU n 
1 148 GLN n 
1 149 GLN n 
1 150 ALA n 
1 151 THR n 
1 152 TYR n 
1 153 LEU n 
1 154 THR n 
1 155 LYS n 
1 156 LEU n 
1 157 VAL n 
1 158 SER n 
1 159 GLY n 
1 160 GLU n 
1 161 TRP n 
1 162 THR n 
1 163 GLY n 
1 164 THR n 
1 165 MET n 
1 166 CYS n 
1 167 LEU n 
1 168 THR n 
1 169 GLU n 
1 170 PRO n 
1 171 HIS n 
1 172 CYS n 
1 173 GLY n 
1 174 THR n 
1 175 ASP n 
1 176 LEU n 
1 177 GLY n 
1 178 MET n 
1 179 LEU n 
1 180 ARG n 
1 181 THR n 
1 182 LYS n 
1 183 ALA n 
1 184 GLU n 
1 185 PRO n 
1 186 GLN n 
1 187 ALA n 
1 188 ASP n 
1 189 GLY n 
1 190 SER n 
1 191 TYR n 
1 192 LYS n 
1 193 VAL n 
1 194 THR n 
1 195 GLY n 
1 196 THR n 
1 197 LYS n 
1 198 ILE n 
1 199 PHE n 
1 200 ILE n 
1 201 SER n 
1 202 ALA n 
1 203 GLY n 
1 204 GLU n 
1 205 HIS n 
1 206 ASP n 
1 207 MET n 
1 208 ALA n 
1 209 ASP n 
1 210 ASN n 
1 211 ILE n 
1 212 VAL n 
1 213 HIS n 
1 214 ILE n 
1 215 VAL n 
1 216 LEU n 
1 217 ALA n 
1 218 ARG n 
1 219 LEU n 
1 220 PRO n 
1 221 ASP n 
1 222 ALA n 
1 223 PRO n 
1 224 GLN n 
1 225 GLY n 
1 226 THR n 
1 227 LYS n 
1 228 GLY n 
1 229 ILE n 
1 230 SER n 
1 231 LEU n 
1 232 PHE n 
1 233 ILE n 
1 234 VAL n 
1 235 PRO n 
1 236 LYS n 
1 237 PHE n 
1 238 LEU n 
1 239 PRO n 
1 240 ASN n 
1 241 ALA n 
1 242 GLU n 
1 243 GLY n 
1 244 ASN n 
1 245 ALA n 
1 246 GLY n 
1 247 GLU n 
1 248 ARG n 
1 249 ASN n 
1 250 ALA n 
1 251 VAL n 
1 252 SER n 
1 253 CYS n 
1 254 GLY n 
1 255 SER n 
1 256 ILE n 
1 257 GLU n 
1 258 HIS n 
1 259 LYS n 
1 260 MET n 
1 261 GLY n 
1 262 ILE n 
1 263 HIS n 
1 264 GLY n 
1 265 ASN n 
1 266 ALA n 
1 267 THR n 
1 268 CYS n 
1 269 VAL n 
1 270 MET n 
1 271 ASN n 
1 272 PHE n 
1 273 ASP n 
1 274 ALA n 
1 275 ALA n 
1 276 THR n 
1 277 GLY n 
1 278 PHE n 
1 279 LEU n 
1 280 ILE n 
1 281 GLY n 
1 282 PRO n 
1 283 PRO n 
1 284 ASN n 
1 285 LYS n 
1 286 GLY n 
1 287 LEU n 
1 288 ASN n 
1 289 CYS n 
1 290 MET n 
1 291 PHE n 
1 292 THR n 
1 293 PHE n 
1 294 MET n 
1 295 ASN n 
1 296 THR n 
1 297 ALA n 
1 298 ARG n 
1 299 LEU n 
1 300 GLY n 
1 301 THR n 
1 302 ALA n 
1 303 LEU n 
1 304 GLN n 
1 305 GLY n 
1 306 LEU n 
1 307 ALA n 
1 308 HIS n 
1 309 ALA n 
1 310 GLU n 
1 311 VAL n 
1 312 GLY n 
1 313 PHE n 
1 314 GLN n 
1 315 GLY n 
1 316 GLY n 
1 317 ILE n 
1 318 ALA n 
1 319 TYR n 
1 320 ALA n 
1 321 ARG n 
1 322 GLU n 
1 323 ARG n 
1 324 LEU n 
1 325 GLN n 
1 326 MET n 
1 327 ARG n 
1 328 SER n 
1 329 LEU n 
1 330 THR n 
1 331 GLY n 
1 332 PRO n 
1 333 LYS n 
1 334 ALA n 
1 335 PRO n 
1 336 GLU n 
1 337 LYS n 
1 338 PRO n 
1 339 ALA n 
1 340 ASP n 
1 341 PRO n 
1 342 ILE n 
1 343 ILE n 
1 344 VAL n 
1 345 HIS n 
1 346 PRO n 
1 347 ASP n 
1 348 VAL n 
1 349 ARG n 
1 350 ARG n 
1 351 MET n 
1 352 LEU n 
1 353 LEU n 
1 354 THR n 
1 355 MET n 
1 356 LYS n 
1 357 ALA n 
1 358 PHE n 
1 359 ALA n 
1 360 GLU n 
1 361 GLY n 
1 362 ASN n 
1 363 ARG n 
1 364 ALA n 
1 365 MET n 
1 366 LEU n 
1 367 TYR n 
1 368 PHE n 
1 369 ALA n 
1 370 ALA n 
1 371 LYS n 
1 372 GLN n 
1 373 VAL n 
1 374 ASP n 
1 375 ILE n 
1 376 VAL n 
1 377 GLN n 
1 378 ARG n 
1 379 SER n 
1 380 GLN n 
1 381 ASP n 
1 382 GLU n 
1 383 GLU n 
1 384 GLN n 
1 385 LYS n 
1 386 LYS n 
1 387 ALA n 
1 388 ALA n 
1 389 ASP n 
1 390 SER n 
1 391 MET n 
1 392 LEU n 
1 393 ALA n 
1 394 PHE n 
1 395 LEU n 
1 396 THR n 
1 397 PRO n 
1 398 ILE n 
1 399 ALA n 
1 400 LYS n 
1 401 ALA n 
1 402 PHE n 
1 403 MET n 
1 404 THR n 
1 405 GLU n 
1 406 VAL n 
1 407 GLY n 
1 408 PHE n 
1 409 GLU n 
1 410 SER n 
1 411 ALA n 
1 412 ASN n 
1 413 HIS n 
1 414 GLY n 
1 415 VAL n 
1 416 GLN n 
1 417 ILE n 
1 418 PHE n 
1 419 GLY n 
1 420 GLY n 
1 421 HIS n 
1 422 GLY n 
1 423 PHE n 
1 424 ILE n 
1 425 ALA n 
1 426 GLU n 
1 427 HIS n 
1 428 GLY n 
1 429 MET n 
1 430 GLU n 
1 431 GLN n 
1 432 ASN n 
1 433 VAL n 
1 434 ARG n 
1 435 ASP n 
1 436 SER n 
1 437 ARG n 
1 438 ILE n 
1 439 SER n 
1 440 MET n 
1 441 LEU n 
1 442 TYR n 
1 443 ALA n 
1 444 GLY n 
1 445 THR n 
1 446 THR n 
1 447 GLY n 
1 448 VAL n 
1 449 GLN n 
1 450 ALA n 
1 451 LEU n 
1 452 ASP n 
1 453 LEU n 
1 454 LEU n 
1 455 GLY n 
1 456 ARG n 
1 457 LYS n 
1 458 VAL n 
1 459 LEU n 
1 460 MET n 
1 461 THR n 
1 462 GLN n 
1 463 GLY n 
1 464 GLU n 
1 465 ALA n 
1 466 LEU n 
1 467 LYS n 
1 468 GLY n 
1 469 PHE n 
1 470 THR n 
1 471 LYS n 
1 472 ILE n 
1 473 VAL n 
1 474 HIS n 
1 475 LYS n 
1 476 PHE n 
1 477 CYS n 
1 478 GLN n 
1 479 ALA n 
1 480 ASN n 
1 481 GLU n 
1 482 ALA n 
1 483 ASN n 
1 484 GLU n 
1 485 ALA n 
1 486 VAL n 
1 487 LYS n 
1 488 GLU n 
1 489 PHE n 
1 490 VAL n 
1 491 ALA n 
1 492 PRO n 
1 493 LEU n 
1 494 ALA n 
1 495 GLN n 
1 496 LEU n 
1 497 ASN n 
1 498 LYS n 
1 499 GLU n 
1 500 TRP n 
1 501 GLY n 
1 502 ASP n 
1 503 LEU n 
1 504 THR n 
1 505 MET n 
1 506 LYS n 
1 507 VAL n 
1 508 GLY n 
1 509 MET n 
1 510 ALA n 
1 511 ALA n 
1 512 MET n 
1 513 LYS n 
1 514 ASP n 
1 515 ARG n 
1 516 GLU n 
1 517 GLU n 
1 518 VAL n 
1 519 GLY n 
1 520 ALA n 
1 521 ALA n 
1 522 SER n 
1 523 VAL n 
1 524 ASP n 
1 525 TYR n 
1 526 LEU n 
1 527 MET n 
1 528 TYR n 
1 529 SER n 
1 530 GLY n 
1 531 TYR n 
1 532 ALA n 
1 533 CYS n 
1 534 LEU n 
1 535 ALA n 
1 536 TYR n 
1 537 PHE n 
1 538 TRP n 
1 539 ALA n 
1 540 ASP n 
1 541 MET n 
1 542 ALA n 
1 543 ARG n 
1 544 LEU n 
1 545 ALA n 
1 546 ALA n 
1 547 GLU n 
1 548 LYS n 
1 549 LEU n 
1 550 ALA n 
1 551 ALA n 
1 552 GLY n 
1 553 THR n 
1 554 GLY n 
1 555 GLU n 
1 556 GLU n 
1 557 ALA n 
1 558 PHE n 
1 559 TYR n 
1 560 LYS n 
1 561 ALA n 
1 562 LYS n 
1 563 LEU n 
1 564 GLN n 
1 565 THR n 
1 566 ALA n 
1 567 ARG n 
1 568 PHE n 
1 569 TYR n 
1 570 PHE n 
1 571 GLN n 
1 572 ARG n 
1 573 ILE n 
1 574 LEU n 
1 575 PRO n 
1 576 ARG n 
1 577 THR n 
1 578 ARG n 
1 579 ALA n 
1 580 HIS n 
1 581 VAL n 
1 582 ALA n 
1 583 ALA n 
1 584 MET n 
1 585 LEU n 
1 586 SER n 
1 587 GLY n 
1 588 ALA n 
1 589 ASN n 
1 590 ASN n 
1 591 LEU n 
1 592 MET n 
1 593 GLU n 
1 594 MET n 
1 595 ALA n 
1 596 GLU n 
1 597 GLU n 
1 598 ASP n 
1 599 PHE n 
1 600 ALA n 
1 601 LEU n 
1 602 GLY n 
1 603 TYR n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   603 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PA0506 
_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      'Pseudomonas aeruginosa' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     287 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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               'Rosetta(DE3) pLysS' 
_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                   ? 
# 
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  
EDO non-polymer         . 1,2-ETHANEDIOL                           'ETHYLENE GLYCOL' 'C2 H6 O2'            62.068   
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  
NO3 non-polymer         . 'NITRATE ION'                            ?                 'N O3 -1'             62.005   
PGE non-polymer         . 'TRIETHYLENE GLYCOL'                     ?                 'C6 H14 O4'           150.173  
PHE 'L-peptide linking' y PHENYLALANINE                            ?                 'C9 H11 N O2'         165.189  
PKZ non-polymer         . Palmitoyl-CoA                            ?                 'C37 H66 N7 O17 P3 S' 1005.943 
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  
TRS non-polymer         . 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 'TRIS BUFFER'     'C4 H12 N O3 1'       122.143  
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   GLY 1   -1  ?   ?   ?   B . n 
A 1 2   HIS 2   0   ?   ?   ?   B . n 
A 1 3   MET 3   1   ?   ?   ?   B . n 
A 1 4   PRO 4   2   ?   ?   ?   B . n 
A 1 5   ASP 5   3   3   ASP ASP B . n 
A 1 6   TYR 6   4   4   TYR TYR B . n 
A 1 7   LYS 7   5   5   LYS LYS B . n 
A 1 8   ALA 8   6   6   ALA ALA B . n 
A 1 9   PRO 9   7   7   PRO PRO B . n 
A 1 10  LEU 10  8   8   LEU LEU B . n 
A 1 11  ARG 11  9   9   ARG ARG B . n 
A 1 12  ASP 12  10  10  ASP ASP B . n 
A 1 13  ILE 13  11  11  ILE ILE B . n 
A 1 14  ARG 14  12  12  ARG ARG B . n 
A 1 15  PHE 15  13  13  PHE PHE B . n 
A 1 16  VAL 16  14  14  VAL VAL B . n 
A 1 17  ARG 17  15  15  ARG ARG B . n 
A 1 18  ASP 18  16  16  ASP ASP B . n 
A 1 19  GLU 19  17  17  GLU GLU B . n 
A 1 20  LEU 20  18  18  LEU LEU B . n 
A 1 21  LEU 21  19  19  LEU LEU B . n 
A 1 22  GLY 22  20  20  GLY GLY B . n 
A 1 23  TYR 23  21  21  TYR TYR B . n 
A 1 24  GLU 24  22  22  GLU GLU B . n 
A 1 25  ALA 25  23  23  ALA ALA B . n 
A 1 26  HIS 26  24  24  HIS HIS B . n 
A 1 27  TYR 27  25  25  TYR TYR B . n 
A 1 28  GLN 28  26  26  GLN GLN B . n 
A 1 29  SER 29  27  27  SER SER B . n 
A 1 30  LEU 30  28  28  LEU LEU B . n 
A 1 31  PRO 31  29  29  PRO PRO B . n 
A 1 32  GLY 32  30  30  GLY GLY B . n 
A 1 33  ALA 33  31  31  ALA ALA B . n 
A 1 34  GLU 34  32  32  GLU GLU B . n 
A 1 35  ASP 35  33  33  ASP ASP B . n 
A 1 36  ALA 36  34  34  ALA ALA B . n 
A 1 37  THR 37  35  35  THR THR B . n 
A 1 38  PRO 38  36  36  PRO PRO B . n 
A 1 39  ASP 39  37  37  ASP ASP B . n 
A 1 40  MET 40  38  38  MET MET B . n 
A 1 41  VAL 41  39  39  VAL VAL B . n 
A 1 42  ASN 42  40  40  ASN ASN B . n 
A 1 43  ALA 43  41  41  ALA ALA B . n 
A 1 44  ILE 44  42  42  ILE ILE B . n 
A 1 45  LEU 45  43  43  LEU LEU B . n 
A 1 46  GLU 46  44  44  GLU GLU B . n 
A 1 47  GLU 47  45  45  GLU GLU B . n 
A 1 48  GLY 48  46  46  GLY GLY B . n 
A 1 49  ALA 49  47  47  ALA ALA B . n 
A 1 50  LYS 50  48  48  LYS LYS B . n 
A 1 51  PHE 51  49  49  PHE PHE B . n 
A 1 52  CYS 52  50  50  CYS CYS B . n 
A 1 53  GLU 53  51  51  GLU GLU B . n 
A 1 54  GLN 54  52  52  GLN GLN B . n 
A 1 55  VAL 55  53  53  VAL VAL B . n 
A 1 56  ILE 56  54  54  ILE ILE B . n 
A 1 57  ALA 57  55  55  ALA ALA B . n 
A 1 58  PRO 58  56  56  PRO PRO B . n 
A 1 59  LEU 59  57  57  LEU LEU B . n 
A 1 60  ASN 60  58  58  ASN ASN B . n 
A 1 61  ARG 61  59  59  ARG ARG B . n 
A 1 62  VAL 62  60  60  VAL VAL B . n 
A 1 63  GLY 63  61  61  GLY GLY B . n 
A 1 64  ASP 64  62  62  ASP ASP B . n 
A 1 65  LEU 65  63  63  LEU LEU B . n 
A 1 66  GLU 66  64  64  GLU GLU B . n 
A 1 67  GLY 67  65  65  GLY GLY B . n 
A 1 68  CYS 68  66  66  CYS CYS B . n 
A 1 69  THR 69  67  67  THR THR B . n 
A 1 70  TRP 70  68  68  TRP TRP B . n 
A 1 71  SER 71  69  69  SER SER B . n 
A 1 72  ALA 72  70  70  ALA ALA B . n 
A 1 73  ASP 73  71  71  ASP ASP B . n 
A 1 74  GLY 74  72  72  GLY GLY B . n 
A 1 75  VAL 75  73  73  VAL VAL B . n 
A 1 76  LYS 76  74  74  LYS LYS B . n 
A 1 77  THR 77  75  75  THR THR B . n 
A 1 78  PRO 78  76  76  PRO PRO B . n 
A 1 79  THR 79  77  77  THR THR B . n 
A 1 80  GLY 80  78  78  GLY GLY B . n 
A 1 81  PHE 81  79  79  PHE PHE B . n 
A 1 82  LYS 82  80  80  LYS LYS B . n 
A 1 83  GLU 83  81  81  GLU GLU B . n 
A 1 84  ALA 84  82  82  ALA ALA B . n 
A 1 85  TYR 85  83  83  TYR TYR B . n 
A 1 86  GLN 86  84  84  GLN GLN B . n 
A 1 87  GLN 87  85  85  GLN GLN B . n 
A 1 88  PHE 88  86  86  PHE PHE B . n 
A 1 89  VAL 89  87  87  VAL VAL B . n 
A 1 90  GLU 90  88  88  GLU GLU B . n 
A 1 91  GLY 91  89  89  GLY GLY B . n 
A 1 92  GLY 92  90  90  GLY GLY B . n 
A 1 93  TRP 93  91  91  TRP TRP B . n 
A 1 94  PRO 94  92  92  PRO PRO B . n 
A 1 95  SER 95  93  93  SER SER B . n 
A 1 96  LEU 96  94  94  LEU LEU B . n 
A 1 97  ALA 97  95  95  ALA ALA B . n 
A 1 98  HIS 98  96  96  HIS HIS B . n 
A 1 99  ASP 99  97  97  ASP ASP B . n 
A 1 100 VAL 100 98  98  VAL VAL B . n 
A 1 101 GLU 101 99  99  GLU GLU B . n 
A 1 102 HIS 102 100 100 HIS HIS B . n 
A 1 103 GLY 103 101 101 GLY GLY B . n 
A 1 104 GLY 104 102 102 GLY GLY B . n 
A 1 105 GLN 105 103 103 GLN GLN B . n 
A 1 106 GLY 106 104 104 GLY GLY B . n 
A 1 107 LEU 107 105 105 LEU LEU B . n 
A 1 108 PRO 108 106 106 PRO PRO B . n 
A 1 109 GLU 109 107 107 GLU GLU B . n 
A 1 110 SER 110 108 108 SER SER B . n 
A 1 111 LEU 111 109 109 LEU LEU B . n 
A 1 112 GLY 112 110 110 GLY GLY B . n 
A 1 113 LEU 113 111 111 LEU LEU B . n 
A 1 114 ALA 114 112 112 ALA ALA B . n 
A 1 115 ILE 115 113 113 ILE ILE B . n 
A 1 116 SER 116 114 114 SER SER B . n 
A 1 117 GLU 117 115 115 GLU GLU B . n 
A 1 118 MET 118 116 116 MET MET B . n 
A 1 119 VAL 119 117 117 VAL VAL B . n 
A 1 120 GLY 120 118 118 GLY GLY B . n 
A 1 121 GLN 121 119 119 GLN GLN B . n 
A 1 122 ALA 122 120 120 ALA ALA B . n 
A 1 123 ASN 123 121 121 ASN ASN B . n 
A 1 124 TRP 124 122 122 TRP TRP B . n 
A 1 125 SER 125 123 123 SER SER B . n 
A 1 126 TRP 126 124 124 TRP TRP B . n 
A 1 127 GLY 127 125 125 GLY GLY B . n 
A 1 128 MET 128 126 126 MET MET B . n 
A 1 129 TYR 129 127 127 TYR TYR B . n 
A 1 130 PRO 130 128 128 PRO PRO B . n 
A 1 131 GLY 131 129 129 GLY GLY B . n 
A 1 132 LEU 132 130 130 LEU LEU B . n 
A 1 133 SER 133 131 131 SER SER B . n 
A 1 134 HIS 134 132 132 HIS HIS B . n 
A 1 135 GLY 135 133 133 GLY GLY B . n 
A 1 136 ALA 136 134 134 ALA ALA B . n 
A 1 137 MET 137 135 135 MET MET B . n 
A 1 138 ASN 138 136 136 ASN ASN B . n 
A 1 139 THR 139 137 137 THR THR B . n 
A 1 140 LEU 140 138 138 LEU LEU B . n 
A 1 141 HIS 141 139 139 HIS HIS B . n 
A 1 142 ALA 142 140 140 ALA ALA B . n 
A 1 143 HIS 143 141 141 HIS HIS B . n 
A 1 144 GLY 144 142 142 GLY GLY B . n 
A 1 145 THR 145 143 143 THR THR B . n 
A 1 146 ALA 146 144 144 ALA ALA B . n 
A 1 147 GLU 147 145 145 GLU GLU B . n 
A 1 148 GLN 148 146 146 GLN GLN B . n 
A 1 149 GLN 149 147 147 GLN GLN B . n 
A 1 150 ALA 150 148 148 ALA ALA B . n 
A 1 151 THR 151 149 149 THR THR B . n 
A 1 152 TYR 152 150 150 TYR TYR B . n 
A 1 153 LEU 153 151 151 LEU LEU B . n 
A 1 154 THR 154 152 152 THR THR B . n 
A 1 155 LYS 155 153 153 LYS LYS B . n 
A 1 156 LEU 156 154 154 LEU LEU B . n 
A 1 157 VAL 157 155 155 VAL VAL B . n 
A 1 158 SER 158 156 156 SER SER B . n 
A 1 159 GLY 159 157 157 GLY GLY B . n 
A 1 160 GLU 160 158 158 GLU GLU B . n 
A 1 161 TRP 161 159 159 TRP TRP B . n 
A 1 162 THR 162 160 160 THR THR B . n 
A 1 163 GLY 163 161 161 GLY GLY B . n 
A 1 164 THR 164 162 162 THR THR B . n 
A 1 165 MET 165 163 163 MET MET B . n 
A 1 166 CYS 166 164 164 CYS CYS B . n 
A 1 167 LEU 167 165 165 LEU LEU B . n 
A 1 168 THR 168 166 166 THR THR B . n 
A 1 169 GLU 169 167 167 GLU GLU B . n 
A 1 170 PRO 170 168 168 PRO PRO B . n 
A 1 171 HIS 171 169 169 HIS HIS B . n 
A 1 172 CYS 172 170 170 CYS CYS B . n 
A 1 173 GLY 173 171 171 GLY GLY B . n 
A 1 174 THR 174 172 172 THR THR B . n 
A 1 175 ASP 175 173 173 ASP ASP B . n 
A 1 176 LEU 176 174 174 LEU LEU B . n 
A 1 177 GLY 177 175 175 GLY GLY B . n 
A 1 178 MET 178 176 176 MET MET B . n 
A 1 179 LEU 179 177 177 LEU LEU B . n 
A 1 180 ARG 180 178 178 ARG ARG B . n 
A 1 181 THR 181 179 179 THR THR B . n 
A 1 182 LYS 182 180 180 LYS LYS B . n 
A 1 183 ALA 183 181 181 ALA ALA B . n 
A 1 184 GLU 184 182 182 GLU GLU B . n 
A 1 185 PRO 185 183 183 PRO PRO B . n 
A 1 186 GLN 186 184 184 GLN GLN B . n 
A 1 187 ALA 187 185 185 ALA ALA B . n 
A 1 188 ASP 188 186 186 ASP ASP B . n 
A 1 189 GLY 189 187 187 GLY GLY B . n 
A 1 190 SER 190 188 188 SER SER B . n 
A 1 191 TYR 191 189 189 TYR TYR B . n 
A 1 192 LYS 192 190 190 LYS LYS B . n 
A 1 193 VAL 193 191 191 VAL VAL B . n 
A 1 194 THR 194 192 192 THR THR B . n 
A 1 195 GLY 195 193 193 GLY GLY B . n 
A 1 196 THR 196 194 194 THR THR B . n 
A 1 197 LYS 197 195 195 LYS LYS B . n 
A 1 198 ILE 198 196 196 ILE ILE B . n 
A 1 199 PHE 199 197 197 PHE PHE B . n 
A 1 200 ILE 200 198 198 ILE ILE B . n 
A 1 201 SER 201 199 199 SER SER B . n 
A 1 202 ALA 202 200 200 ALA ALA B . n 
A 1 203 GLY 203 201 201 GLY GLY B . n 
A 1 204 GLU 204 202 202 GLU GLU B . n 
A 1 205 HIS 205 203 203 HIS HIS B . n 
A 1 206 ASP 206 204 204 ASP ASP B . n 
A 1 207 MET 207 205 205 MET MET B . n 
A 1 208 ALA 208 206 206 ALA ALA B . n 
A 1 209 ASP 209 207 207 ASP ASP B . n 
A 1 210 ASN 210 208 208 ASN ASN B . n 
A 1 211 ILE 211 209 209 ILE ILE B . n 
A 1 212 VAL 212 210 210 VAL VAL B . n 
A 1 213 HIS 213 211 211 HIS HIS B . n 
A 1 214 ILE 214 212 212 ILE ILE B . n 
A 1 215 VAL 215 213 213 VAL VAL B . n 
A 1 216 LEU 216 214 214 LEU LEU B . n 
A 1 217 ALA 217 215 215 ALA ALA B . n 
A 1 218 ARG 218 216 216 ARG ARG B . n 
A 1 219 LEU 219 217 217 LEU LEU B . n 
A 1 220 PRO 220 218 218 PRO PRO B . n 
A 1 221 ASP 221 219 219 ASP ASP B . n 
A 1 222 ALA 222 220 220 ALA ALA B . n 
A 1 223 PRO 223 221 221 PRO PRO B . n 
A 1 224 GLN 224 222 222 GLN GLN B . n 
A 1 225 GLY 225 223 223 GLY GLY B . n 
A 1 226 THR 226 224 224 THR THR B . n 
A 1 227 LYS 227 225 225 LYS LYS B . n 
A 1 228 GLY 228 226 226 GLY GLY B . n 
A 1 229 ILE 229 227 227 ILE ILE B . n 
A 1 230 SER 230 228 228 SER SER B . n 
A 1 231 LEU 231 229 229 LEU LEU B . n 
A 1 232 PHE 232 230 230 PHE PHE B . n 
A 1 233 ILE 233 231 231 ILE ILE B . n 
A 1 234 VAL 234 232 232 VAL VAL B . n 
A 1 235 PRO 235 233 233 PRO PRO B . n 
A 1 236 LYS 236 234 234 LYS LYS B . n 
A 1 237 PHE 237 235 235 PHE PHE B . n 
A 1 238 LEU 238 236 236 LEU LEU B . n 
A 1 239 PRO 239 237 237 PRO PRO B . n 
A 1 240 ASN 240 238 238 ASN ASN B . n 
A 1 241 ALA 241 239 239 ALA ALA B . n 
A 1 242 GLU 242 240 240 GLU GLU B . n 
A 1 243 GLY 243 241 241 GLY GLY B . n 
A 1 244 ASN 244 242 242 ASN ASN B . n 
A 1 245 ALA 245 243 243 ALA ALA B . n 
A 1 246 GLY 246 244 244 GLY GLY B . n 
A 1 247 GLU 247 245 245 GLU GLU B . n 
A 1 248 ARG 248 246 246 ARG ARG B . n 
A 1 249 ASN 249 247 247 ASN ASN B . n 
A 1 250 ALA 250 248 248 ALA ALA B . n 
A 1 251 VAL 251 249 249 VAL VAL B . n 
A 1 252 SER 252 250 250 SER SER B . n 
A 1 253 CYS 253 251 251 CYS CYS B . n 
A 1 254 GLY 254 252 252 GLY GLY B . n 
A 1 255 SER 255 253 253 SER SER B . n 
A 1 256 ILE 256 254 254 ILE ILE B . n 
A 1 257 GLU 257 255 255 GLU GLU B . n 
A 1 258 HIS 258 256 256 HIS HIS B . n 
A 1 259 LYS 259 257 257 LYS LYS B . n 
A 1 260 MET 260 258 258 MET MET B . n 
A 1 261 GLY 261 259 259 GLY GLY B . n 
A 1 262 ILE 262 260 260 ILE ILE B . n 
A 1 263 HIS 263 261 261 HIS HIS B . n 
A 1 264 GLY 264 262 262 GLY GLY B . n 
A 1 265 ASN 265 263 263 ASN ASN B . n 
A 1 266 ALA 266 264 264 ALA ALA B . n 
A 1 267 THR 267 265 265 THR THR B . n 
A 1 268 CYS 268 266 266 CYS CYS B . n 
A 1 269 VAL 269 267 267 VAL VAL B . n 
A 1 270 MET 270 268 268 MET MET B . n 
A 1 271 ASN 271 269 269 ASN ASN B . n 
A 1 272 PHE 272 270 270 PHE PHE B . n 
A 1 273 ASP 273 271 271 ASP ASP B . n 
A 1 274 ALA 274 272 272 ALA ALA B . n 
A 1 275 ALA 275 273 273 ALA ALA B . n 
A 1 276 THR 276 274 274 THR THR B . n 
A 1 277 GLY 277 275 275 GLY GLY B . n 
A 1 278 PHE 278 276 276 PHE PHE B . n 
A 1 279 LEU 279 277 277 LEU LEU B . n 
A 1 280 ILE 280 278 278 ILE ILE B . n 
A 1 281 GLY 281 279 279 GLY GLY B . n 
A 1 282 PRO 282 280 280 PRO PRO B . n 
A 1 283 PRO 283 281 281 PRO PRO B . n 
A 1 284 ASN 284 282 282 ASN ASN B . n 
A 1 285 LYS 285 283 283 LYS LYS B . n 
A 1 286 GLY 286 284 284 GLY GLY B . n 
A 1 287 LEU 287 285 285 LEU LEU B . n 
A 1 288 ASN 288 286 286 ASN ASN B . n 
A 1 289 CYS 289 287 287 CYS CYS B . n 
A 1 290 MET 290 288 288 MET MET B . n 
A 1 291 PHE 291 289 289 PHE PHE B . n 
A 1 292 THR 292 290 290 THR THR B . n 
A 1 293 PHE 293 291 291 PHE PHE B . n 
A 1 294 MET 294 292 292 MET MET B . n 
A 1 295 ASN 295 293 293 ASN ASN B . n 
A 1 296 THR 296 294 294 THR THR B . n 
A 1 297 ALA 297 295 295 ALA ALA B . n 
A 1 298 ARG 298 296 296 ARG ARG B . n 
A 1 299 LEU 299 297 297 LEU LEU B . n 
A 1 300 GLY 300 298 298 GLY GLY B . n 
A 1 301 THR 301 299 299 THR THR B . n 
A 1 302 ALA 302 300 300 ALA ALA B . n 
A 1 303 LEU 303 301 301 LEU LEU B . n 
A 1 304 GLN 304 302 302 GLN GLN B . n 
A 1 305 GLY 305 303 303 GLY GLY B . n 
A 1 306 LEU 306 304 304 LEU LEU B . n 
A 1 307 ALA 307 305 305 ALA ALA B . n 
A 1 308 HIS 308 306 306 HIS HIS B . n 
A 1 309 ALA 309 307 307 ALA ALA B . n 
A 1 310 GLU 310 308 308 GLU GLU B . n 
A 1 311 VAL 311 309 309 VAL VAL B . n 
A 1 312 GLY 312 310 310 GLY GLY B . n 
A 1 313 PHE 313 311 311 PHE PHE B . n 
A 1 314 GLN 314 312 312 GLN GLN B . n 
A 1 315 GLY 315 313 313 GLY GLY B . n 
A 1 316 GLY 316 314 314 GLY GLY B . n 
A 1 317 ILE 317 315 315 ILE ILE B . n 
A 1 318 ALA 318 316 316 ALA ALA B . n 
A 1 319 TYR 319 317 317 TYR TYR B . n 
A 1 320 ALA 320 318 318 ALA ALA B . n 
A 1 321 ARG 321 319 319 ARG ARG B . n 
A 1 322 GLU 322 320 320 GLU GLU B . n 
A 1 323 ARG 323 321 321 ARG ARG B . n 
A 1 324 LEU 324 322 322 LEU LEU B . n 
A 1 325 GLN 325 323 323 GLN GLN B . n 
A 1 326 MET 326 324 324 MET MET B . n 
A 1 327 ARG 327 325 325 ARG ARG B . n 
A 1 328 SER 328 326 326 SER SER B . n 
A 1 329 LEU 329 327 327 LEU LEU B . n 
A 1 330 THR 330 328 328 THR THR B . n 
A 1 331 GLY 331 329 329 GLY GLY B . n 
A 1 332 PRO 332 330 330 PRO PRO B . n 
A 1 333 LYS 333 331 331 LYS LYS B . n 
A 1 334 ALA 334 332 332 ALA ALA B . n 
A 1 335 PRO 335 333 333 PRO PRO B . n 
A 1 336 GLU 336 334 334 GLU GLU B . n 
A 1 337 LYS 337 335 335 LYS LYS B . n 
A 1 338 PRO 338 336 336 PRO PRO B . n 
A 1 339 ALA 339 337 337 ALA ALA B . n 
A 1 340 ASP 340 338 338 ASP ASP B . n 
A 1 341 PRO 341 339 339 PRO PRO B . n 
A 1 342 ILE 342 340 340 ILE ILE B . n 
A 1 343 ILE 343 341 341 ILE ILE B . n 
A 1 344 VAL 344 342 342 VAL VAL B . n 
A 1 345 HIS 345 343 343 HIS HIS B . n 
A 1 346 PRO 346 344 344 PRO PRO B . n 
A 1 347 ASP 347 345 345 ASP ASP B . n 
A 1 348 VAL 348 346 346 VAL VAL B . n 
A 1 349 ARG 349 347 347 ARG ARG B . n 
A 1 350 ARG 350 348 348 ARG ARG B . n 
A 1 351 MET 351 349 349 MET MET B . n 
A 1 352 LEU 352 350 350 LEU LEU B . n 
A 1 353 LEU 353 351 351 LEU LEU B . n 
A 1 354 THR 354 352 352 THR THR B . n 
A 1 355 MET 355 353 353 MET MET B . n 
A 1 356 LYS 356 354 354 LYS LYS B . n 
A 1 357 ALA 357 355 355 ALA ALA B . n 
A 1 358 PHE 358 356 356 PHE PHE B . n 
A 1 359 ALA 359 357 357 ALA ALA B . n 
A 1 360 GLU 360 358 358 GLU GLU B . n 
A 1 361 GLY 361 359 359 GLY GLY B . n 
A 1 362 ASN 362 360 360 ASN ASN B . n 
A 1 363 ARG 363 361 361 ARG ARG B . n 
A 1 364 ALA 364 362 362 ALA ALA B . n 
A 1 365 MET 365 363 363 MET MET B . n 
A 1 366 LEU 366 364 364 LEU LEU B . n 
A 1 367 TYR 367 365 365 TYR TYR B . n 
A 1 368 PHE 368 366 366 PHE PHE B . n 
A 1 369 ALA 369 367 367 ALA ALA B . n 
A 1 370 ALA 370 368 368 ALA ALA B . n 
A 1 371 LYS 371 369 369 LYS LYS B . n 
A 1 372 GLN 372 370 370 GLN GLN B . n 
A 1 373 VAL 373 371 371 VAL VAL B . n 
A 1 374 ASP 374 372 372 ASP ASP B . n 
A 1 375 ILE 375 373 373 ILE ILE B . n 
A 1 376 VAL 376 374 374 VAL VAL B . n 
A 1 377 GLN 377 375 375 GLN GLN B . n 
A 1 378 ARG 378 376 376 ARG ARG B . n 
A 1 379 SER 379 377 377 SER SER B . n 
A 1 380 GLN 380 378 378 GLN GLN B . n 
A 1 381 ASP 381 379 379 ASP ASP B . n 
A 1 382 GLU 382 380 380 GLU GLU B . n 
A 1 383 GLU 383 381 381 GLU GLU B . n 
A 1 384 GLN 384 382 382 GLN GLN B . n 
A 1 385 LYS 385 383 383 LYS LYS B . n 
A 1 386 LYS 386 384 384 LYS LYS B . n 
A 1 387 ALA 387 385 385 ALA ALA B . n 
A 1 388 ALA 388 386 386 ALA ALA B . n 
A 1 389 ASP 389 387 387 ASP ASP B . n 
A 1 390 SER 390 388 388 SER SER B . n 
A 1 391 MET 391 389 389 MET MET B . n 
A 1 392 LEU 392 390 390 LEU LEU B . n 
A 1 393 ALA 393 391 391 ALA ALA B . n 
A 1 394 PHE 394 392 392 PHE PHE B . n 
A 1 395 LEU 395 393 393 LEU LEU B . n 
A 1 396 THR 396 394 394 THR THR B . n 
A 1 397 PRO 397 395 395 PRO PRO B . n 
A 1 398 ILE 398 396 396 ILE ILE B . n 
A 1 399 ALA 399 397 397 ALA ALA B . n 
A 1 400 LYS 400 398 398 LYS LYS B . n 
A 1 401 ALA 401 399 399 ALA ALA B . n 
A 1 402 PHE 402 400 400 PHE PHE B . n 
A 1 403 MET 403 401 401 MET MET B . n 
A 1 404 THR 404 402 402 THR THR B . n 
A 1 405 GLU 405 403 403 GLU GLU B . n 
A 1 406 VAL 406 404 404 VAL VAL B . n 
A 1 407 GLY 407 405 405 GLY GLY B . n 
A 1 408 PHE 408 406 406 PHE PHE B . n 
A 1 409 GLU 409 407 407 GLU GLU B . n 
A 1 410 SER 410 408 408 SER SER B . n 
A 1 411 ALA 411 409 409 ALA ALA B . n 
A 1 412 ASN 412 410 410 ASN ASN B . n 
A 1 413 HIS 413 411 411 HIS HIS B . n 
A 1 414 GLY 414 412 412 GLY GLY B . n 
A 1 415 VAL 415 413 413 VAL VAL B . n 
A 1 416 GLN 416 414 414 GLN GLN B . n 
A 1 417 ILE 417 415 415 ILE ILE B . n 
A 1 418 PHE 418 416 416 PHE PHE B . n 
A 1 419 GLY 419 417 417 GLY GLY B . n 
A 1 420 GLY 420 418 418 GLY GLY B . n 
A 1 421 HIS 421 419 419 HIS HIS B . n 
A 1 422 GLY 422 420 420 GLY GLY B . n 
A 1 423 PHE 423 421 421 PHE PHE B . n 
A 1 424 ILE 424 422 422 ILE ILE B . n 
A 1 425 ALA 425 423 423 ALA ALA B . n 
A 1 426 GLU 426 424 424 GLU GLU B . n 
A 1 427 HIS 427 425 425 HIS HIS B . n 
A 1 428 GLY 428 426 426 GLY GLY B . n 
A 1 429 MET 429 427 427 MET MET B . n 
A 1 430 GLU 430 428 428 GLU GLU B . n 
A 1 431 GLN 431 429 429 GLN GLN B . n 
A 1 432 ASN 432 430 430 ASN ASN B . n 
A 1 433 VAL 433 431 431 VAL VAL B . n 
A 1 434 ARG 434 432 432 ARG ARG B . n 
A 1 435 ASP 435 433 433 ASP ASP B . n 
A 1 436 SER 436 434 434 SER SER B . n 
A 1 437 ARG 437 435 435 ARG ARG B . n 
A 1 438 ILE 438 436 436 ILE ILE B . n 
A 1 439 SER 439 437 437 SER SER B . n 
A 1 440 MET 440 438 438 MET MET B . n 
A 1 441 LEU 441 439 439 LEU LEU B . n 
A 1 442 TYR 442 440 440 TYR TYR B . n 
A 1 443 ALA 443 441 441 ALA ALA B . n 
A 1 444 GLY 444 442 442 GLY GLY B . n 
A 1 445 THR 445 443 443 THR THR B . n 
A 1 446 THR 446 444 444 THR THR B . n 
A 1 447 GLY 447 445 445 GLY GLY B . n 
A 1 448 VAL 448 446 446 VAL VAL B . n 
A 1 449 GLN 449 447 447 GLN GLN B . n 
A 1 450 ALA 450 448 448 ALA ALA B . n 
A 1 451 LEU 451 449 449 LEU LEU B . n 
A 1 452 ASP 452 450 450 ASP ASP B . n 
A 1 453 LEU 453 451 451 LEU LEU B . n 
A 1 454 LEU 454 452 452 LEU LEU B . n 
A 1 455 GLY 455 453 453 GLY GLY B . n 
A 1 456 ARG 456 454 454 ARG ARG B . n 
A 1 457 LYS 457 455 455 LYS LYS B . n 
A 1 458 VAL 458 456 456 VAL VAL B . n 
A 1 459 LEU 459 457 457 LEU LEU B . n 
A 1 460 MET 460 458 458 MET MET B . n 
A 1 461 THR 461 459 459 THR THR B . n 
A 1 462 GLN 462 460 460 GLN GLN B . n 
A 1 463 GLY 463 461 461 GLY GLY B . n 
A 1 464 GLU 464 462 462 GLU GLU B . n 
A 1 465 ALA 465 463 463 ALA ALA B . n 
A 1 466 LEU 466 464 464 LEU LEU B . n 
A 1 467 LYS 467 465 465 LYS LYS B . n 
A 1 468 GLY 468 466 466 GLY GLY B . n 
A 1 469 PHE 469 467 467 PHE PHE B . n 
A 1 470 THR 470 468 468 THR THR B . n 
A 1 471 LYS 471 469 469 LYS LYS B . n 
A 1 472 ILE 472 470 470 ILE ILE B . n 
A 1 473 VAL 473 471 471 VAL VAL B . n 
A 1 474 HIS 474 472 472 HIS HIS B . n 
A 1 475 LYS 475 473 473 LYS LYS B . n 
A 1 476 PHE 476 474 474 PHE PHE B . n 
A 1 477 CYS 477 475 475 CYS CYS B . n 
A 1 478 GLN 478 476 476 GLN GLN B . n 
A 1 479 ALA 479 477 477 ALA ALA B . n 
A 1 480 ASN 480 478 478 ASN ASN B . n 
A 1 481 GLU 481 479 479 GLU GLU B . n 
A 1 482 ALA 482 480 480 ALA ALA B . n 
A 1 483 ASN 483 481 481 ASN ASN B . n 
A 1 484 GLU 484 482 482 GLU GLU B . n 
A 1 485 ALA 485 483 483 ALA ALA B . n 
A 1 486 VAL 486 484 484 VAL VAL B . n 
A 1 487 LYS 487 485 485 LYS LYS B . n 
A 1 488 GLU 488 486 486 GLU GLU B . n 
A 1 489 PHE 489 487 487 PHE PHE B . n 
A 1 490 VAL 490 488 488 VAL VAL B . n 
A 1 491 ALA 491 489 489 ALA ALA B . n 
A 1 492 PRO 492 490 490 PRO PRO B . n 
A 1 493 LEU 493 491 491 LEU LEU B . n 
A 1 494 ALA 494 492 492 ALA ALA B . n 
A 1 495 GLN 495 493 493 GLN GLN B . n 
A 1 496 LEU 496 494 494 LEU LEU B . n 
A 1 497 ASN 497 495 495 ASN ASN B . n 
A 1 498 LYS 498 496 496 LYS LYS B . n 
A 1 499 GLU 499 497 497 GLU GLU B . n 
A 1 500 TRP 500 498 498 TRP TRP B . n 
A 1 501 GLY 501 499 499 GLY GLY B . n 
A 1 502 ASP 502 500 500 ASP ASP B . n 
A 1 503 LEU 503 501 501 LEU LEU B . n 
A 1 504 THR 504 502 502 THR THR B . n 
A 1 505 MET 505 503 503 MET MET B . n 
A 1 506 LYS 506 504 504 LYS LYS B . n 
A 1 507 VAL 507 505 505 VAL VAL B . n 
A 1 508 GLY 508 506 506 GLY GLY B . n 
A 1 509 MET 509 507 507 MET MET B . n 
A 1 510 ALA 510 508 508 ALA ALA B . n 
A 1 511 ALA 511 509 509 ALA ALA B . n 
A 1 512 MET 512 510 510 MET MET B . n 
A 1 513 LYS 513 511 511 LYS LYS B . n 
A 1 514 ASP 514 512 512 ASP ASP B . n 
A 1 515 ARG 515 513 513 ARG ARG B . n 
A 1 516 GLU 516 514 514 GLU GLU B . n 
A 1 517 GLU 517 515 515 GLU GLU B . n 
A 1 518 VAL 518 516 516 VAL VAL B . n 
A 1 519 GLY 519 517 517 GLY GLY B . n 
A 1 520 ALA 520 518 518 ALA ALA B . n 
A 1 521 ALA 521 519 519 ALA ALA B . n 
A 1 522 SER 522 520 520 SER SER B . n 
A 1 523 VAL 523 521 521 VAL VAL B . n 
A 1 524 ASP 524 522 522 ASP ASP B . n 
A 1 525 TYR 525 523 523 TYR TYR B . n 
A 1 526 LEU 526 524 524 LEU LEU B . n 
A 1 527 MET 527 525 525 MET MET B . n 
A 1 528 TYR 528 526 526 TYR TYR B . n 
A 1 529 SER 529 527 527 SER SER B . n 
A 1 530 GLY 530 528 528 GLY GLY B . n 
A 1 531 TYR 531 529 529 TYR TYR B . n 
A 1 532 ALA 532 530 530 ALA ALA B . n 
A 1 533 CYS 533 531 531 CYS CYS B . n 
A 1 534 LEU 534 532 532 LEU LEU B . n 
A 1 535 ALA 535 533 533 ALA ALA B . n 
A 1 536 TYR 536 534 534 TYR TYR B . n 
A 1 537 PHE 537 535 535 PHE PHE B . n 
A 1 538 TRP 538 536 536 TRP TRP B . n 
A 1 539 ALA 539 537 537 ALA ALA B . n 
A 1 540 ASP 540 538 538 ASP ASP B . n 
A 1 541 MET 541 539 539 MET MET B . n 
A 1 542 ALA 542 540 540 ALA ALA B . n 
A 1 543 ARG 543 541 541 ARG ARG B . n 
A 1 544 LEU 544 542 542 LEU LEU B . n 
A 1 545 ALA 545 543 543 ALA ALA B . n 
A 1 546 ALA 546 544 544 ALA ALA B . n 
A 1 547 GLU 547 545 545 GLU GLU B . n 
A 1 548 LYS 548 546 546 LYS LYS B . n 
A 1 549 LEU 549 547 547 LEU LEU B . n 
A 1 550 ALA 550 548 548 ALA ALA B . n 
A 1 551 ALA 551 549 549 ALA ALA B . n 
A 1 552 GLY 552 550 550 GLY GLY B . n 
A 1 553 THR 553 551 551 THR THR B . n 
A 1 554 GLY 554 552 552 GLY GLY B . n 
A 1 555 GLU 555 553 553 GLU GLU B . n 
A 1 556 GLU 556 554 554 GLU GLU B . n 
A 1 557 ALA 557 555 555 ALA ALA B . n 
A 1 558 PHE 558 556 556 PHE PHE B . n 
A 1 559 TYR 559 557 557 TYR TYR B . n 
A 1 560 LYS 560 558 558 LYS LYS B . n 
A 1 561 ALA 561 559 559 ALA ALA B . n 
A 1 562 LYS 562 560 560 LYS LYS B . n 
A 1 563 LEU 563 561 561 LEU LEU B . n 
A 1 564 GLN 564 562 562 GLN GLN B . n 
A 1 565 THR 565 563 563 THR THR B . n 
A 1 566 ALA 566 564 564 ALA ALA B . n 
A 1 567 ARG 567 565 565 ARG ARG B . n 
A 1 568 PHE 568 566 566 PHE PHE B . n 
A 1 569 TYR 569 567 567 TYR TYR B . n 
A 1 570 PHE 570 568 568 PHE PHE B . n 
A 1 571 GLN 571 569 569 GLN GLN B . n 
A 1 572 ARG 572 570 570 ARG ARG B . n 
A 1 573 ILE 573 571 571 ILE ILE B . n 
A 1 574 LEU 574 572 572 LEU LEU B . n 
A 1 575 PRO 575 573 573 PRO PRO B . n 
A 1 576 ARG 576 574 574 ARG ARG B . n 
A 1 577 THR 577 575 575 THR THR B . n 
A 1 578 ARG 578 576 576 ARG ARG B . n 
A 1 579 ALA 579 577 577 ALA ALA B . n 
A 1 580 HIS 580 578 578 HIS HIS B . n 
A 1 581 VAL 581 579 579 VAL VAL B . n 
A 1 582 ALA 582 580 580 ALA ALA B . n 
A 1 583 ALA 583 581 581 ALA ALA B . n 
A 1 584 MET 584 582 582 MET MET B . n 
A 1 585 LEU 585 583 583 LEU LEU B . n 
A 1 586 SER 586 584 584 SER SER B . n 
A 1 587 GLY 587 585 585 GLY GLY B . n 
A 1 588 ALA 588 586 586 ALA ALA B . n 
A 1 589 ASN 589 587 587 ASN ASN B . n 
A 1 590 ASN 590 588 588 ASN ASN B . n 
A 1 591 LEU 591 589 589 LEU LEU B . n 
A 1 592 MET 592 590 590 MET MET B . n 
A 1 593 GLU 593 591 591 GLU GLU B . n 
A 1 594 MET 594 592 592 MET MET B . n 
A 1 595 ALA 595 593 593 ALA ALA B . n 
A 1 596 GLU 596 594 594 GLU GLU B . n 
A 1 597 GLU 597 595 595 GLU GLU B . n 
A 1 598 ASP 598 596 596 ASP ASP B . n 
A 1 599 PHE 599 597 597 PHE PHE B . n 
A 1 600 ALA 600 598 598 ALA ALA B . n 
A 1 601 LEU 601 599 599 LEU LEU B . n 
A 1 602 GLY 602 600 600 GLY GLY B . n 
A 1 603 TYR 603 601 601 TYR TYR B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        PKZ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   PKZ 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 PKZ 1   701  710 PKZ PKZ B . 
C 3 EDO 1   702  711 EDO EDO B . 
D 3 EDO 1   703  712 EDO EDO B . 
E 4 PGE 1   704  713 PGE PGE B . 
F 3 EDO 1   705  715 EDO EDO B . 
G 3 EDO 1   706  717 EDO EDO B . 
H 5 NO3 1   707  718 NO3 NO3 B . 
I 5 NO3 1   708  719 NO3 NO3 B . 
J 6 TRS 1   709  720 TRS TRS B . 
K 7 HOH 1   801  450 HOH HOH B . 
K 7 HOH 2   802  289 HOH HOH B . 
K 7 HOH 3   803  77  HOH HOH B . 
K 7 HOH 4   804  147 HOH HOH B . 
K 7 HOH 5   805  117 HOH HOH B . 
K 7 HOH 6   806  291 HOH HOH B . 
K 7 HOH 7   807  127 HOH HOH B . 
K 7 HOH 8   808  222 HOH HOH B . 
K 7 HOH 9   809  231 HOH HOH B . 
K 7 HOH 10  810  163 HOH HOH B . 
K 7 HOH 11  811  210 HOH HOH B . 
K 7 HOH 12  812  173 HOH HOH B . 
K 7 HOH 13  813  191 HOH HOH B . 
K 7 HOH 14  814  16  HOH HOH B . 
K 7 HOH 15  815  211 HOH HOH B . 
K 7 HOH 16  816  74  HOH HOH B . 
K 7 HOH 17  817  304 HOH HOH B . 
K 7 HOH 18  818  322 HOH HOH B . 
K 7 HOH 19  819  281 HOH HOH B . 
K 7 HOH 20  820  62  HOH HOH B . 
K 7 HOH 21  821  106 HOH HOH B . 
K 7 HOH 22  822  68  HOH HOH B . 
K 7 HOH 23  823  341 HOH HOH B . 
K 7 HOH 24  824  169 HOH HOH B . 
K 7 HOH 25  825  263 HOH HOH B . 
K 7 HOH 26  826  362 HOH HOH B . 
K 7 HOH 27  828  383 HOH HOH B . 
K 7 HOH 28  829  59  HOH HOH B . 
K 7 HOH 29  830  61  HOH HOH B . 
K 7 HOH 30  831  21  HOH HOH B . 
K 7 HOH 31  832  135 HOH HOH B . 
K 7 HOH 32  833  80  HOH HOH B . 
K 7 HOH 33  834  35  HOH HOH B . 
K 7 HOH 34  835  325 HOH HOH B . 
K 7 HOH 35  836  335 HOH HOH B . 
K 7 HOH 36  837  48  HOH HOH B . 
K 7 HOH 37  838  141 HOH HOH B . 
K 7 HOH 38  839  149 HOH HOH B . 
K 7 HOH 39  840  198 HOH HOH B . 
K 7 HOH 40  841  192 HOH HOH B . 
K 7 HOH 41  842  239 HOH HOH B . 
K 7 HOH 42  843  73  HOH HOH B . 
K 7 HOH 43  844  355 HOH HOH B . 
K 7 HOH 44  845  206 HOH HOH B . 
K 7 HOH 45  846  205 HOH HOH B . 
K 7 HOH 46  847  331 HOH HOH B . 
K 7 HOH 47  848  274 HOH HOH B . 
K 7 HOH 48  849  119 HOH HOH B . 
K 7 HOH 49  850  223 HOH HOH B . 
K 7 HOH 50  851  243 HOH HOH B . 
K 7 HOH 51  852  137 HOH HOH B . 
K 7 HOH 52  853  49  HOH HOH B . 
K 7 HOH 53  854  282 HOH HOH B . 
K 7 HOH 54  855  26  HOH HOH B . 
K 7 HOH 55  856  203 HOH HOH B . 
K 7 HOH 56  857  268 HOH HOH B . 
K 7 HOH 57  858  255 HOH HOH B . 
K 7 HOH 58  859  240 HOH HOH B . 
K 7 HOH 59  860  209 HOH HOH B . 
K 7 HOH 60  861  235 HOH HOH B . 
K 7 HOH 61  862  108 HOH HOH B . 
K 7 HOH 62  863  290 HOH HOH B . 
K 7 HOH 63  864  245 HOH HOH B . 
K 7 HOH 64  865  332 HOH HOH B . 
K 7 HOH 65  866  130 HOH HOH B . 
K 7 HOH 66  867  314 HOH HOH B . 
K 7 HOH 67  868  371 HOH HOH B . 
K 7 HOH 68  869  11  HOH HOH B . 
K 7 HOH 69  870  28  HOH HOH B . 
K 7 HOH 70  871  313 HOH HOH B . 
K 7 HOH 71  872  7   HOH HOH B . 
K 7 HOH 72  873  333 HOH HOH B . 
K 7 HOH 73  874  125 HOH HOH B . 
K 7 HOH 74  875  309 HOH HOH B . 
K 7 HOH 75  876  9   HOH HOH B . 
K 7 HOH 76  877  234 HOH HOH B . 
K 7 HOH 77  878  67  HOH HOH B . 
K 7 HOH 78  879  51  HOH HOH B . 
K 7 HOH 79  880  47  HOH HOH B . 
K 7 HOH 80  881  199 HOH HOH B . 
K 7 HOH 81  882  115 HOH HOH B . 
K 7 HOH 82  883  120 HOH HOH B . 
K 7 HOH 83  884  86  HOH HOH B . 
K 7 HOH 84  885  213 HOH HOH B . 
K 7 HOH 85  886  116 HOH HOH B . 
K 7 HOH 86  887  38  HOH HOH B . 
K 7 HOH 87  888  129 HOH HOH B . 
K 7 HOH 88  889  93  HOH HOH B . 
K 7 HOH 89  890  100 HOH HOH B . 
K 7 HOH 90  891  432 HOH HOH B . 
K 7 HOH 91  892  44  HOH HOH B . 
K 7 HOH 92  893  162 HOH HOH B . 
K 7 HOH 93  894  167 HOH HOH B . 
K 7 HOH 94  895  23  HOH HOH B . 
K 7 HOH 95  896  182 HOH HOH B . 
K 7 HOH 96  897  226 HOH HOH B . 
K 7 HOH 97  898  430 HOH HOH B . 
K 7 HOH 98  899  242 HOH HOH B . 
K 7 HOH 99  900  446 HOH HOH B . 
K 7 HOH 100 901  267 HOH HOH B . 
K 7 HOH 101 902  161 HOH HOH B . 
K 7 HOH 102 903  269 HOH HOH B . 
K 7 HOH 103 904  217 HOH HOH B . 
K 7 HOH 104 905  246 HOH HOH B . 
K 7 HOH 105 906  251 HOH HOH B . 
K 7 HOH 106 907  82  HOH HOH B . 
K 7 HOH 107 908  220 HOH HOH B . 
K 7 HOH 108 909  275 HOH HOH B . 
K 7 HOH 109 910  348 HOH HOH B . 
K 7 HOH 110 911  18  HOH HOH B . 
K 7 HOH 111 912  3   HOH HOH B . 
K 7 HOH 112 913  303 HOH HOH B . 
K 7 HOH 113 914  99  HOH HOH B . 
K 7 HOH 114 915  207 HOH HOH B . 
K 7 HOH 115 916  5   HOH HOH B . 
K 7 HOH 116 917  144 HOH HOH B . 
K 7 HOH 117 918  131 HOH HOH B . 
K 7 HOH 118 919  145 HOH HOH B . 
K 7 HOH 119 920  295 HOH HOH B . 
K 7 HOH 120 921  31  HOH HOH B . 
K 7 HOH 121 922  184 HOH HOH B . 
K 7 HOH 122 923  30  HOH HOH B . 
K 7 HOH 123 924  288 HOH HOH B . 
K 7 HOH 124 925  232 HOH HOH B . 
K 7 HOH 125 926  298 HOH HOH B . 
K 7 HOH 126 927  1   HOH HOH B . 
K 7 HOH 127 928  224 HOH HOH B . 
K 7 HOH 128 929  90  HOH HOH B . 
K 7 HOH 129 930  122 HOH HOH B . 
K 7 HOH 130 931  435 HOH HOH B . 
K 7 HOH 131 932  212 HOH HOH B . 
K 7 HOH 132 933  329 HOH HOH B . 
K 7 HOH 133 934  71  HOH HOH B . 
K 7 HOH 134 935  308 HOH HOH B . 
K 7 HOH 135 936  146 HOH HOH B . 
K 7 HOH 136 937  425 HOH HOH B . 
K 7 HOH 137 938  261 HOH HOH B . 
K 7 HOH 138 939  195 HOH HOH B . 
K 7 HOH 139 940  436 HOH HOH B . 
K 7 HOH 140 941  81  HOH HOH B . 
K 7 HOH 141 942  97  HOH HOH B . 
K 7 HOH 142 943  124 HOH HOH B . 
K 7 HOH 143 944  41  HOH HOH B . 
K 7 HOH 144 945  102 HOH HOH B . 
K 7 HOH 145 946  160 HOH HOH B . 
K 7 HOH 146 947  277 HOH HOH B . 
K 7 HOH 147 948  183 HOH HOH B . 
K 7 HOH 148 949  45  HOH HOH B . 
K 7 HOH 149 950  360 HOH HOH B . 
K 7 HOH 150 951  27  HOH HOH B . 
K 7 HOH 151 952  39  HOH HOH B . 
K 7 HOH 152 954  37  HOH HOH B . 
K 7 HOH 153 955  22  HOH HOH B . 
K 7 HOH 154 956  140 HOH HOH B . 
K 7 HOH 155 957  126 HOH HOH B . 
K 7 HOH 156 958  431 HOH HOH B . 
K 7 HOH 157 959  352 HOH HOH B . 
K 7 HOH 158 960  13  HOH HOH B . 
K 7 HOH 159 961  218 HOH HOH B . 
K 7 HOH 160 963  256 HOH HOH B . 
K 7 HOH 161 964  4   HOH HOH B . 
K 7 HOH 162 965  56  HOH HOH B . 
K 7 HOH 163 966  176 HOH HOH B . 
K 7 HOH 164 967  15  HOH HOH B . 
K 7 HOH 165 968  219 HOH HOH B . 
K 7 HOH 166 969  152 HOH HOH B . 
K 7 HOH 167 970  54  HOH HOH B . 
K 7 HOH 168 971  426 HOH HOH B . 
K 7 HOH 169 972  339 HOH HOH B . 
K 7 HOH 170 973  187 HOH HOH B . 
K 7 HOH 171 974  50  HOH HOH B . 
K 7 HOH 172 975  168 HOH HOH B . 
K 7 HOH 173 976  64  HOH HOH B . 
K 7 HOH 174 977  334 HOH HOH B . 
K 7 HOH 175 978  76  HOH HOH B . 
K 7 HOH 176 979  6   HOH HOH B . 
K 7 HOH 177 980  438 HOH HOH B . 
K 7 HOH 178 981  172 HOH HOH B . 
K 7 HOH 179 982  427 HOH HOH B . 
K 7 HOH 180 983  422 HOH HOH B . 
K 7 HOH 181 984  252 HOH HOH B . 
K 7 HOH 182 985  8   HOH HOH B . 
K 7 HOH 183 986  84  HOH HOH B . 
K 7 HOH 184 987  378 HOH HOH B . 
K 7 HOH 185 988  315 HOH HOH B . 
K 7 HOH 186 989  107 HOH HOH B . 
K 7 HOH 187 990  237 HOH HOH B . 
K 7 HOH 188 991  19  HOH HOH B . 
K 7 HOH 189 992  46  HOH HOH B . 
K 7 HOH 190 993  43  HOH HOH B . 
K 7 HOH 191 994  271 HOH HOH B . 
K 7 HOH 192 995  241 HOH HOH B . 
K 7 HOH 193 996  201 HOH HOH B . 
K 7 HOH 194 997  55  HOH HOH B . 
K 7 HOH 195 998  361 HOH HOH B . 
K 7 HOH 196 999  72  HOH HOH B . 
K 7 HOH 197 1000 180 HOH HOH B . 
K 7 HOH 198 1001 319 HOH HOH B . 
K 7 HOH 199 1002 58  HOH HOH B . 
K 7 HOH 200 1003 418 HOH HOH B . 
K 7 HOH 201 1004 444 HOH HOH B . 
K 7 HOH 202 1005 280 HOH HOH B . 
K 7 HOH 203 1006 254 HOH HOH B . 
K 7 HOH 204 1007 78  HOH HOH B . 
K 7 HOH 205 1008 197 HOH HOH B . 
K 7 HOH 206 1009 110 HOH HOH B . 
K 7 HOH 207 1010 344 HOH HOH B . 
K 7 HOH 208 1011 123 HOH HOH B . 
K 7 HOH 209 1012 29  HOH HOH B . 
K 7 HOH 210 1013 375 HOH HOH B . 
K 7 HOH 211 1014 42  HOH HOH B . 
K 7 HOH 212 1015 287 HOH HOH B . 
K 7 HOH 213 1016 98  HOH HOH B . 
K 7 HOH 214 1017 95  HOH HOH B . 
K 7 HOH 215 1018 434 HOH HOH B . 
K 7 HOH 216 1019 364 HOH HOH B . 
K 7 HOH 217 1020 189 HOH HOH B . 
K 7 HOH 218 1021 63  HOH HOH B . 
K 7 HOH 219 1022 171 HOH HOH B . 
K 7 HOH 220 1023 305 HOH HOH B . 
K 7 HOH 221 1024 202 HOH HOH B . 
K 7 HOH 222 1025 301 HOH HOH B . 
K 7 HOH 223 1026 138 HOH HOH B . 
K 7 HOH 224 1027 221 HOH HOH B . 
K 7 HOH 225 1028 421 HOH HOH B . 
K 7 HOH 226 1029 279 HOH HOH B . 
K 7 HOH 227 1030 14  HOH HOH B . 
K 7 HOH 228 1031 142 HOH HOH B . 
K 7 HOH 229 1032 60  HOH HOH B . 
K 7 HOH 230 1033 257 HOH HOH B . 
K 7 HOH 231 1034 276 HOH HOH B . 
K 7 HOH 232 1035 259 HOH HOH B . 
K 7 HOH 233 1036 368 HOH HOH B . 
K 7 HOH 234 1037 423 HOH HOH B . 
K 7 HOH 235 1038 428 HOH HOH B . 
K 7 HOH 236 1039 419 HOH HOH B . 
K 7 HOH 237 1040 2   HOH HOH B . 
K 7 HOH 238 1041 85  HOH HOH B . 
K 7 HOH 239 1043 283 HOH HOH B . 
K 7 HOH 240 1044 349 HOH HOH B . 
K 7 HOH 241 1045 302 HOH HOH B . 
K 7 HOH 242 1046 253 HOH HOH B . 
K 7 HOH 243 1047 118 HOH HOH B . 
K 7 HOH 244 1048 128 HOH HOH B . 
K 7 HOH 245 1049 40  HOH HOH B . 
K 7 HOH 246 1050 156 HOH HOH B . 
K 7 HOH 247 1051 278 HOH HOH B . 
K 7 HOH 248 1052 155 HOH HOH B . 
K 7 HOH 249 1053 185 HOH HOH B . 
K 7 HOH 250 1054 350 HOH HOH B . 
K 7 HOH 251 1055 94  HOH HOH B . 
K 7 HOH 252 1056 354 HOH HOH B . 
K 7 HOH 253 1057 157 HOH HOH B . 
K 7 HOH 254 1058 53  HOH HOH B . 
K 7 HOH 255 1059 109 HOH HOH B . 
K 7 HOH 256 1060 272 HOH HOH B . 
K 7 HOH 257 1061 34  HOH HOH B . 
K 7 HOH 258 1062 300 HOH HOH B . 
K 7 HOH 259 1063 17  HOH HOH B . 
K 7 HOH 260 1064 437 HOH HOH B . 
K 7 HOH 261 1065 101 HOH HOH B . 
K 7 HOH 262 1066 200 HOH HOH B . 
K 7 HOH 263 1067 170 HOH HOH B . 
K 7 HOH 264 1068 244 HOH HOH B . 
K 7 HOH 265 1069 439 HOH HOH B . 
K 7 HOH 266 1070 188 HOH HOH B . 
K 7 HOH 267 1071 25  HOH HOH B . 
K 7 HOH 268 1072 177 HOH HOH B . 
K 7 HOH 269 1073 164 HOH HOH B . 
K 7 HOH 270 1074 12  HOH HOH B . 
K 7 HOH 271 1075 132 HOH HOH B . 
K 7 HOH 272 1076 384 HOH HOH B . 
K 7 HOH 273 1077 249 HOH HOH B . 
K 7 HOH 274 1078 323 HOH HOH B . 
K 7 HOH 275 1079 346 HOH HOH B . 
K 7 HOH 276 1080 250 HOH HOH B . 
K 7 HOH 277 1081 193 HOH HOH B . 
K 7 HOH 278 1082 324 HOH HOH B . 
K 7 HOH 279 1083 447 HOH HOH B . 
K 7 HOH 280 1084 194 HOH HOH B . 
K 7 HOH 281 1085 196 HOH HOH B . 
K 7 HOH 282 1086 134 HOH HOH B . 
K 7 HOH 283 1087 312 HOH HOH B . 
K 7 HOH 284 1088 91  HOH HOH B . 
K 7 HOH 285 1089 75  HOH HOH B . 
K 7 HOH 286 1090 443 HOH HOH B . 
K 7 HOH 287 1091 306 HOH HOH B . 
K 7 HOH 288 1092 233 HOH HOH B . 
K 7 HOH 289 1093 178 HOH HOH B . 
K 7 HOH 290 1094 65  HOH HOH B . 
K 7 HOH 291 1095 36  HOH HOH B . 
K 7 HOH 292 1096 328 HOH HOH B . 
K 7 HOH 293 1097 227 HOH HOH B . 
K 7 HOH 294 1098 441 HOH HOH B . 
K 7 HOH 295 1099 10  HOH HOH B . 
K 7 HOH 296 1100 347 HOH HOH B . 
K 7 HOH 297 1101 345 HOH HOH B . 
K 7 HOH 298 1102 297 HOH HOH B . 
K 7 HOH 299 1103 374 HOH HOH B . 
K 7 HOH 300 1104 113 HOH HOH B . 
K 7 HOH 301 1105 186 HOH HOH B . 
K 7 HOH 302 1106 216 HOH HOH B . 
K 7 HOH 303 1107 174 HOH HOH B . 
K 7 HOH 304 1108 52  HOH HOH B . 
K 7 HOH 305 1109 104 HOH HOH B . 
K 7 HOH 306 1110 33  HOH HOH B . 
K 7 HOH 307 1111 175 HOH HOH B . 
K 7 HOH 308 1112 236 HOH HOH B . 
K 7 HOH 309 1113 114 HOH HOH B . 
K 7 HOH 310 1114 158 HOH HOH B . 
K 7 HOH 311 1115 307 HOH HOH B . 
K 7 HOH 312 1116 190 HOH HOH B . 
K 7 HOH 313 1117 208 HOH HOH B . 
K 7 HOH 314 1118 92  HOH HOH B . 
K 7 HOH 315 1119 204 HOH HOH B . 
K 7 HOH 316 1120 20  HOH HOH B . 
K 7 HOH 317 1121 358 HOH HOH B . 
K 7 HOH 318 1122 105 HOH HOH B . 
K 7 HOH 319 1123 112 HOH HOH B . 
K 7 HOH 320 1124 32  HOH HOH B . 
K 7 HOH 321 1125 111 HOH HOH B . 
K 7 HOH 322 1126 179 HOH HOH B . 
K 7 HOH 323 1127 342 HOH HOH B . 
K 7 HOH 324 1128 136 HOH HOH B . 
K 7 HOH 325 1129 89  HOH HOH B . 
K 7 HOH 326 1130 154 HOH HOH B . 
K 7 HOH 327 1131 57  HOH HOH B . 
K 7 HOH 328 1132 433 HOH HOH B . 
K 7 HOH 329 1133 165 HOH HOH B . 
K 7 HOH 330 1134 270 HOH HOH B . 
K 7 HOH 331 1135 442 HOH HOH B . 
K 7 HOH 332 1136 420 HOH HOH B . 
K 7 HOH 333 1137 229 HOH HOH B . 
K 7 HOH 334 1138 159 HOH HOH B . 
K 7 HOH 335 1139 66  HOH HOH B . 
K 7 HOH 336 1140 417 HOH HOH B . 
K 7 HOH 337 1141 153 HOH HOH B . 
K 7 HOH 338 1142 286 HOH HOH B . 
K 7 HOH 339 1143 379 HOH HOH B . 
K 7 HOH 340 1144 24  HOH HOH B . 
K 7 HOH 341 1145 83  HOH HOH B . 
K 7 HOH 342 1146 393 HOH HOH B . 
K 7 HOH 343 1147 79  HOH HOH B . 
K 7 HOH 344 1148 410 HOH HOH B . 
K 7 HOH 345 1149 151 HOH HOH B . 
K 7 HOH 346 1150 284 HOH HOH B . 
K 7 HOH 347 1151 337 HOH HOH B . 
K 7 HOH 348 1152 294 HOH HOH B . 
K 7 HOH 349 1153 351 HOH HOH B . 
K 7 HOH 350 1154 293 HOH HOH B . 
K 7 HOH 351 1155 407 HOH HOH B . 
K 7 HOH 352 1156 166 HOH HOH B . 
K 7 HOH 353 1157 87  HOH HOH B . 
K 7 HOH 354 1158 228 HOH HOH B . 
K 7 HOH 355 1159 88  HOH HOH B . 
K 7 HOH 356 1160 359 HOH HOH B . 
K 7 HOH 357 1161 386 HOH HOH B . 
K 7 HOH 358 1162 139 HOH HOH B . 
K 7 HOH 359 1163 317 HOH HOH B . 
K 7 HOH 360 1164 148 HOH HOH B . 
K 7 HOH 361 1165 376 HOH HOH B . 
K 7 HOH 362 1166 440 HOH HOH B . 
K 7 HOH 363 1167 326 HOH HOH B . 
K 7 HOH 364 1168 390 HOH HOH B . 
K 7 HOH 365 1169 318 HOH HOH B . 
K 7 HOH 366 1170 143 HOH HOH B . 
K 7 HOH 367 1171 316 HOH HOH B . 
K 7 HOH 368 1172 181 HOH HOH B . 
K 7 HOH 369 1173 238 HOH HOH B . 
K 7 HOH 370 1174 392 HOH HOH B . 
K 7 HOH 371 1175 69  HOH HOH B . 
K 7 HOH 372 1176 389 HOH HOH B . 
K 7 HOH 373 1177 396 HOH HOH B . 
K 7 HOH 374 1178 415 HOH HOH B . 
K 7 HOH 375 1179 248 HOH HOH B . 
K 7 HOH 376 1180 388 HOH HOH B . 
K 7 HOH 377 1181 260 HOH HOH B . 
K 7 HOH 378 1182 400 HOH HOH B . 
K 7 HOH 379 1183 445 HOH HOH B . 
K 7 HOH 380 1184 327 HOH HOH B . 
K 7 HOH 381 1185 121 HOH HOH B . 
K 7 HOH 382 1186 414 HOH HOH B . 
K 7 HOH 383 1187 449 HOH HOH B . 
K 7 HOH 384 1188 343 HOH HOH B . 
K 7 HOH 385 1189 391 HOH HOH B . 
K 7 HOH 386 1190 405 HOH HOH B . 
K 7 HOH 387 1191 70  HOH HOH B . 
K 7 HOH 388 1192 397 HOH HOH B . 
K 7 HOH 389 1193 403 HOH HOH B . 
K 7 HOH 390 1194 150 HOH HOH B . 
K 7 HOH 391 1195 394 HOH HOH B . 
K 7 HOH 392 1196 402 HOH HOH B . 
K 7 HOH 393 1197 215 HOH HOH B . 
K 7 HOH 394 1198 225 HOH HOH B . 
K 7 HOH 395 1199 399 HOH HOH B . 
K 7 HOH 396 1200 377 HOH HOH B . 
K 7 HOH 397 1203 398 HOH HOH B . 
K 7 HOH 398 1205 401 HOH HOH B . 
K 7 HOH 399 1206 230 HOH HOH B . 
K 7 HOH 400 1207 395 HOH HOH B . 
K 7 HOH 401 1208 356 HOH HOH B . 
K 7 HOH 402 1209 448 HOH HOH B . 
K 7 HOH 403 1210 273 HOH HOH B . 
K 7 HOH 404 1211 412 HOH HOH B . 
K 7 HOH 405 1212 372 HOH HOH B . 
K 7 HOH 406 1213 264 HOH HOH B . 
K 7 HOH 407 1214 258 HOH HOH B . 
K 7 HOH 408 1215 103 HOH HOH B . 
K 7 HOH 409 1216 133 HOH HOH B . 
K 7 HOH 410 1217 247 HOH HOH B . 
K 7 HOH 411 1218 296 HOH HOH B . 
K 7 HOH 412 1219 292 HOH HOH B . 
K 7 HOH 413 1220 262 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0267 1 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? 3.3.3    3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? 3.3.3    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8PU5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     92.955 
_cell.length_a_esd                 ? 
_cell.length_b                     92.955 
_cell.length_b_esd                 ? 
_cell.length_c                     128.782 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8PU5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                151 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 31 1 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8PU5 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.74 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.1M Bis Tris Propane pH 6.5, 0.2M sodium nitrate, 20% w/v PEG 3350, 10% v/v ethylene glycol, 5mM C16CoA' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-29 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.92 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          15.100 
_reflns.entry_id                                       8PU5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.44 
_reflns.d_resolution_low                               128.78 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     114956 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                38.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.197 
_reflns.pdbx_Rpim_I_all                                0.031 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.194 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.44 
_reflns_shell.d_res_low                                     1.46 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5683 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               29.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               4.529 
_reflns_shell.pdbx_Rpim_I_all                               0.834 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.3 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  4.451 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.32 
_refine.aniso_B[1][2]                            -0.16 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.32 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            1.02 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.810 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.971 
_refine.correlation_coeff_Fo_to_Fc_free          0.959 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8PU5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.44 
_refine.ls_d_res_low                             80.63 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     109044 
_refine.ls_number_reflns_R_free                  5767 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.92 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18610 
_refine.ls_R_factor_R_free                       0.21378 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18462 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.065 
_refine.pdbx_overall_ESU_R_Free                  0.068 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.010 
_refine.overall_SU_ML                            0.069 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.44 
_refine_hist.d_res_low                        80.63 
_refine_hist.number_atoms_solvent             421 
_refine_hist.number_atoms_total               5091 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4563 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         107 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.013  4824  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  4546  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.629  1.646  6510  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.506  1.575  10484 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.931  5.000  612   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 33.731 22.700 237   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.711 15.000 793   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.008 15.000 25    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.087  0.200  609   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  5500  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1085  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.632  2.134  2415  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.631  2.134  2414  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.289  3.197  3023  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.289  3.197  3024  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.004  2.497  2405  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.003  2.495  2400  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.449  3.609  3473  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.706  26.676 5512  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.596  26.205 5436  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.440 
_refine_ls_shell.d_res_low                        1.477 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             393 
_refine_ls_shell.number_reflns_R_work             8004 
_refine_ls_shell.percent_reflns_obs               99.03 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.375 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.379 
# 
_struct.entry_id                     8PU5 
_struct.title                        
'Crystal structure of the Acyl-CoA dehydrogenase FadE1(PA0506) E441A from Pseudomonas aeruginosa complexed with C16CoA' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8PU5 
_struct_keywords.text            'acyl-CoA dehydrogenase, beta-oxidation, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 ? 
E N N 4 ? 
F N N 3 ? 
G N N 3 ? 
H N N 5 ? 
I N N 5 ? 
J N N 6 ? 
K N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9I612_PSEAE 
_struct_ref.pdbx_db_accession          Q9I612 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPDYKAPLRDIRFVRDELLGYEAHYQSLPGAEDATPDMVNAILEEGAKFCEQVIAPLNRVGDLEGCTWSADGVKTPTGFK
EAYQQFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVGQANWSWGMYPGLSHGAMNTLHAHGTAEQQATYLTKLVSGEWT
GTMCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAGEHDMADNIVHIVLARLPDAPQGTKGISLFIVPKFLPNAE
GNAGERNAVSCGSIEHKMGIHGNATCVMNFDAATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARE
RLQMRSLTGPKAPEKPADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDIVQRSQDEEQKKAADSMLAFLTPIAKAF
MTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQALDLLGRKVLMTQGEALKGFTKIVHKFCQANEA
NEAVKEFVAPLAQLNKEWGDLTMKVGMAAMKDREEVGAASVDYLMYSGYACLAYFWADMARLAAEKLAAGTGEEAFYKAK
LQTARFYFQRILPRTRAHVAAMLSGANNLMEMAEEDFALGY
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8PU5 
_struct_ref_seq.pdbx_strand_id                B 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 603 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9I612 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  601 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       601 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8PU5 GLY B 1   ? UNP Q9I612 ?   ?   'expression tag'      -1  1 
1 8PU5 HIS B 2   ? UNP Q9I612 ?   ?   'expression tag'      0   2 
1 8PU5 ALA B 443 ? UNP Q9I612 GLU 441 'engineered mutation' 441 3 
# 
_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)' 13370 ? 
1 MORE         3     ? 
1 'SSA (A^2)'  40080 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                
;PISA prediction indicated this is most likely to be dimer.
Its wild type form is analyzed by AUC (analytic ultracentrifuge) to be dimer.
;
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z      1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 6_545 x,x-y-1,-z 0.5000000000 0.8660254038 0.0000000000 46.4775000000 0.8660254038 -0.5000000000 
0.0000000000 -80.5013914088 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 9   ? GLU A 19  ? PRO B 7   GLU B 17  1 ? 11 
HELX_P HELX_P2  AA2 GLY A 22  ? SER A 29  ? GLY B 20  SER B 27  1 ? 8  
HELX_P HELX_P3  AA3 THR A 37  ? VAL A 55  ? THR B 35  VAL B 53  1 ? 19 
HELX_P HELX_P4  AA4 ILE A 56  ? PRO A 58  ? ILE B 54  PRO B 56  5 ? 3  
HELX_P HELX_P5  AA5 LEU A 59  ? GLY A 67  ? LEU B 57  GLY B 65  1 ? 9  
HELX_P HELX_P6  AA6 GLY A 80  ? GLY A 91  ? GLY B 78  GLY B 89  1 ? 12 
HELX_P HELX_P7  AA7 GLY A 92  ? LEU A 96  ? GLY B 90  LEU B 94  5 ? 5  
HELX_P HELX_P8  AA8 ASP A 99  ? GLY A 103 ? ASP B 97  GLY B 101 5 ? 5  
HELX_P HELX_P9  AA9 PRO A 108 ? ASN A 123 ? PRO B 106 ASN B 121 1 ? 16 
HELX_P HELX_P10 AB1 ASN A 123 ? GLY A 144 ? ASN B 121 GLY B 142 1 ? 22 
HELX_P HELX_P11 AB2 THR A 145 ? TYR A 152 ? THR B 143 TYR B 150 1 ? 8  
HELX_P HELX_P12 AB3 TYR A 152 ? SER A 158 ? TYR B 150 SER B 156 1 ? 7  
HELX_P HELX_P13 AB4 ASP A 175 ? LEU A 179 ? ASP B 173 LEU B 177 5 ? 5  
HELX_P HELX_P14 AB5 GLN A 224 ? LYS A 227 ? GLN B 222 LYS B 225 5 ? 4  
HELX_P HELX_P15 AB6 LYS A 285 ? ARG A 323 ? LYS B 283 ARG B 321 1 ? 39 
HELX_P HELX_P16 AB7 PRO A 341 ? VAL A 344 ? PRO B 339 VAL B 342 5 ? 4  
HELX_P HELX_P17 AB8 HIS A 345 ? SER A 379 ? HIS B 343 SER B 377 1 ? 35 
HELX_P HELX_P18 AB9 ASP A 381 ? PHE A 418 ? ASP B 379 PHE B 416 1 ? 38 
HELX_P HELX_P19 AC1 GLY A 419 ? HIS A 427 ? GLY B 417 HIS B 425 5 ? 9  
HELX_P HELX_P20 AC2 GLY A 428 ? ILE A 438 ? GLY B 426 ILE B 436 1 ? 11 
HELX_P HELX_P21 AC3 SER A 439 ? LEU A 441 ? SER B 437 LEU B 439 5 ? 3  
HELX_P HELX_P22 AC4 THR A 445 ? GLY A 455 ? THR B 443 GLY B 453 1 ? 11 
HELX_P HELX_P23 AC5 VAL A 458 ? GLN A 462 ? VAL B 456 GLN B 460 5 ? 5  
HELX_P HELX_P24 AC6 GLY A 463 ? GLU A 481 ? GLY B 461 GLU B 479 1 ? 19 
HELX_P HELX_P25 AC7 VAL A 486 ? ASP A 514 ? VAL B 484 ASP B 512 1 ? 29 
HELX_P HELX_P26 AC8 ARG A 515 ? ALA A 551 ? ARG B 513 ALA B 549 1 ? 37 
HELX_P HELX_P27 AC9 GLU A 555 ? ILE A 573 ? GLU B 553 ILE B 571 1 ? 19 
HELX_P HELX_P28 AD1 PRO A 575 ? SER A 586 ? PRO B 573 SER B 584 1 ? 12 
HELX_P HELX_P29 AD2 ALA A 588 ? GLU A 593 ? ALA B 586 GLU B 591 1 ? 6  
HELX_P HELX_P30 AD3 ALA A 595 ? PHE A 599 ? ALA B 593 PHE B 597 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 6 ? 
AA3 ? 5 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 69  ? SER A 71  ? THR B 67  SER B 69  
AA1 2 GLY A 74  ? LYS A 76  ? GLY B 72  LYS B 74  
AA2 1 THR A 162 ? CYS A 166 ? THR B 160 CYS B 164 
AA2 2 ILE A 211 ? ARG A 218 ? ILE B 209 ARG B 216 
AA2 3 LYS A 182 ? PRO A 185 ? LYS B 180 PRO B 183 
AA2 4 TYR A 191 ? SER A 201 ? TYR B 189 SER B 199 
AA2 5 THR A 267 ? ILE A 280 ? THR B 265 ILE B 278 
AA2 6 VAL A 251 ? ILE A 256 ? VAL B 249 ILE B 254 
AA3 1 THR A 162 ? CYS A 166 ? THR B 160 CYS B 164 
AA3 2 ILE A 211 ? ARG A 218 ? ILE B 209 ARG B 216 
AA3 3 ILE A 229 ? PRO A 235 ? ILE B 227 PRO B 233 
AA3 4 THR A 267 ? ILE A 280 ? THR B 265 ILE B 278 
AA3 5 VAL A 251 ? ILE A 256 ? VAL B 249 ILE B 254 
AA4 1 PHE A 237 ? PRO A 239 ? PHE B 235 PRO B 237 
AA4 2 ALA A 245 ? ARG A 248 ? ALA B 243 ARG B 246 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N THR A 69  ? N THR B 67  O LYS A 76  ? O LYS B 74  
AA2 1 2 N CYS A 166 ? N CYS B 164 O ILE A 214 ? O ILE B 212 
AA2 2 3 O ARG A 218 ? O ARG B 216 N ALA A 183 ? N ALA B 181 
AA2 3 4 N GLU A 184 ? N GLU B 182 O LYS A 192 ? O LYS B 190 
AA2 4 5 N VAL A 193 ? N VAL B 191 O ALA A 275 ? O ALA B 273 
AA2 5 6 O ASN A 271 ? O ASN B 269 N SER A 252 ? N SER B 250 
AA3 1 2 N CYS A 166 ? N CYS B 164 O ILE A 214 ? O ILE B 212 
AA3 2 3 N VAL A 215 ? N VAL B 213 O PHE A 232 ? O PHE B 230 
AA3 3 4 N ILE A 233 ? N ILE B 231 O PHE A 278 ? O PHE B 276 
AA3 4 5 O ASN A 271 ? O ASN B 269 N SER A 252 ? N SER B 250 
AA4 1 2 N LEU A 238 ? N LEU B 236 O GLU A 247 ? O GLU B 245 
# 
_pdbx_entry_details.entry_id                   8PU5 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE B ARG 319 ? B CZ B ARG 319 ? B NH1 B ARG 319 ? B 124.76 120.30 4.46  0.50 N 
2 1 NE B ARG 319 ? B CZ B ARG 319 ? B NH2 B ARG 319 ? B 116.18 120.30 -4.12 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA B 95  ? ? -108.55 42.06   
2 1 ASN B 121 ? ? -163.20 86.84   
3 1 ILE B 260 ? ? 34.86   51.98   
4 1 ASP B 271 ? ? -105.14 70.90   
5 1 MET B 324 ? ? 65.70   -168.74 
6 1 VAL B 456 ? ? -98.90  -62.83  
7 1 GLU B 553 ? ? -111.07 51.32   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     1185 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   K 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 B GLY -1 ? A GLY 1 
2 1 Y 1 B HIS 0  ? A HIS 2 
3 1 Y 1 B MET 1  ? A MET 3 
4 1 Y 1 B PRO 2  ? A PRO 4 
# 
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  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
NO3 N    N N N 260 
NO3 O1   O N N 261 
NO3 O2   O N N 262 
NO3 O3   O N N 263 
PGE C1   C N N 264 
PGE O1   O N N 265 
PGE C2   C N N 266 
PGE O2   O N N 267 
PGE C3   C N N 268 
PGE C4   C N N 269 
PGE O4   O N N 270 
PGE C6   C N N 271 
PGE C5   C N N 272 
PGE O3   O N N 273 
PGE H1   H N N 274 
PGE H12  H N N 275 
PGE HO1  H N N 276 
PGE H2   H N N 277 
PGE H22  H N N 278 
PGE H3   H N N 279 
PGE H32  H N N 280 
PGE H4   H N N 281 
PGE H42  H N N 282 
PGE HO4  H N N 283 
PGE H6   H N N 284 
PGE H62  H N N 285 
PGE H5   H N N 286 
PGE H52  H N N 287 
PHE N    N N N 288 
PHE CA   C N S 289 
PHE C    C N N 290 
PHE O    O N N 291 
PHE CB   C N N 292 
PHE CG   C Y N 293 
PHE CD1  C Y N 294 
PHE CD2  C Y N 295 
PHE CE1  C Y N 296 
PHE CE2  C Y N 297 
PHE CZ   C Y N 298 
PHE OXT  O N N 299 
PHE H    H N N 300 
PHE H2   H N N 301 
PHE HA   H N N 302 
PHE HB2  H N N 303 
PHE HB3  H N N 304 
PHE HD1  H N N 305 
PHE HD2  H N N 306 
PHE HE1  H N N 307 
PHE HE2  H N N 308 
PHE HZ   H N N 309 
PHE HXT  H N N 310 
PKZ C3   C N N 311 
PKZ C1   C N N 312 
PKZ C10  C N N 313 
PKZ C8   C N N 314 
PKZ C7   C N N 315 
PKZ C5   C N N 316 
PKZ C11  C N N 317 
PKZ C13  C N N 318 
PKZ C16  C N N 319 
PKZ C15  C N N 320 
PKZ C14  C N N 321 
PKZ N1A  N Y N 322 
PKZ C2A  C Y N 323 
PKZ N3A  N Y N 324 
PKZ C4A  C Y N 325 
PKZ C5A  C Y N 326 
PKZ C6A  C Y N 327 
PKZ N6A  N N N 328 
PKZ N7A  N Y N 329 
PKZ C8A  C Y N 330 
PKZ N9A  N Y N 331 
PKZ C1B  C N R 332 
PKZ C2B  C N R 333 
PKZ O2B  O N N 334 
PKZ C3B  C N S 335 
PKZ O3B  O N N 336 
PKZ P3B  P N N 337 
PKZ O7A  O N N 338 
PKZ O8A  O N N 339 
PKZ O9A  O N N 340 
PKZ C4B  C N R 341 
PKZ O4B  O N N 342 
PKZ C5B  C N N 343 
PKZ O5B  O N N 344 
PKZ P1A  P N N 345 
PKZ O1A  O N N 346 
PKZ O2A  O N N 347 
PKZ O3A  O N N 348 
PKZ P2A  P N N 349 
PKZ O4A  O N N 350 
PKZ O5A  O N N 351 
PKZ O6A  O N N 352 
PKZ CBP  C N N 353 
PKZ CCP  C N N 354 
PKZ CDP  C N N 355 
PKZ CEP  C N N 356 
PKZ CAP  C N R 357 
PKZ OAP  O N N 358 
PKZ C9P  C N N 359 
PKZ O9P  O N N 360 
PKZ N8P  N N N 361 
PKZ C7P  C N N 362 
PKZ C6P  C N N 363 
PKZ C5P  C N N 364 
PKZ O5P  O N N 365 
PKZ N4P  N N N 366 
PKZ C3P  C N N 367 
PKZ C2P  C N N 368 
PKZ S1P  S N N 369 
PKZ O1   O N N 370 
PKZ C2   C N N 371 
PKZ C4   C N N 372 
PKZ C6   C N N 373 
PKZ C9   C N N 374 
PKZ C12  C N N 375 
PKZ H1   H N N 376 
PKZ H2   H N N 377 
PKZ H3   H N N 378 
PKZ H4   H N N 379 
PKZ H5   H N N 380 
PKZ H6   H N N 381 
PKZ H7   H N N 382 
PKZ H8   H N N 383 
PKZ H9   H N N 384 
PKZ H10  H N N 385 
PKZ H11  H N N 386 
PKZ H12  H N N 387 
PKZ H13  H N N 388 
PKZ H14  H N N 389 
PKZ H15  H N N 390 
PKZ H16  H N N 391 
PKZ H17  H N N 392 
PKZ H18  H N N 393 
PKZ H19  H N N 394 
PKZ H20  H N N 395 
PKZ H21  H N N 396 
PKZ H22  H N N 397 
PKZ H23  H N N 398 
PKZ H24  H N N 399 
PKZ H25  H N N 400 
PKZ H26  H N N 401 
PKZ H27  H N N 402 
PKZ H28  H N N 403 
PKZ H29  H N N 404 
PKZ H30  H N N 405 
PKZ H31  H N N 406 
PKZ H32  H N N 407 
PKZ H33  H N N 408 
PKZ H34  H N N 409 
PKZ H35  H N N 410 
PKZ H36  H N N 411 
PKZ H37  H N N 412 
PKZ H38  H N N 413 
PKZ H39  H N N 414 
PKZ H40  H N N 415 
PKZ H41  H N N 416 
PKZ H42  H N N 417 
PKZ H43  H N N 418 
PKZ H44  H N N 419 
PKZ H45  H N N 420 
PKZ H46  H N N 421 
PKZ H47  H N N 422 
PKZ H48  H N N 423 
PKZ H49  H N N 424 
PKZ H50  H N N 425 
PKZ H51  H N N 426 
PKZ H52  H N N 427 
PKZ H53  H N N 428 
PKZ H54  H N N 429 
PKZ H55  H N N 430 
PKZ H56  H N N 431 
PKZ H57  H N N 432 
PKZ H58  H N N 433 
PKZ H59  H N N 434 
PKZ H60  H N N 435 
PKZ H61  H N N 436 
PKZ H62  H N N 437 
PKZ H63  H N N 438 
PKZ H64  H N N 439 
PKZ H65  H N N 440 
PKZ H66  H N N 441 
PRO N    N N N 442 
PRO CA   C N S 443 
PRO C    C N N 444 
PRO O    O N N 445 
PRO CB   C N N 446 
PRO CG   C N N 447 
PRO CD   C N N 448 
PRO OXT  O N N 449 
PRO H    H N N 450 
PRO HA   H N N 451 
PRO HB2  H N N 452 
PRO HB3  H N N 453 
PRO HG2  H N N 454 
PRO HG3  H N N 455 
PRO HD2  H N N 456 
PRO HD3  H N N 457 
PRO HXT  H N N 458 
SER N    N N N 459 
SER CA   C N S 460 
SER C    C N N 461 
SER O    O N N 462 
SER CB   C N N 463 
SER OG   O N N 464 
SER OXT  O N N 465 
SER H    H N N 466 
SER H2   H N N 467 
SER HA   H N N 468 
SER HB2  H N N 469 
SER HB3  H N N 470 
SER HG   H N N 471 
SER HXT  H N N 472 
THR N    N N N 473 
THR CA   C N S 474 
THR C    C N N 475 
THR O    O N N 476 
THR CB   C N R 477 
THR OG1  O N N 478 
THR CG2  C N N 479 
THR OXT  O N N 480 
THR H    H N N 481 
THR H2   H N N 482 
THR HA   H N N 483 
THR HB   H N N 484 
THR HG1  H N N 485 
THR HG21 H N N 486 
THR HG22 H N N 487 
THR HG23 H N N 488 
THR HXT  H N N 489 
TRP N    N N N 490 
TRP CA   C N S 491 
TRP C    C N N 492 
TRP O    O N N 493 
TRP CB   C N N 494 
TRP CG   C Y N 495 
TRP CD1  C Y N 496 
TRP CD2  C Y N 497 
TRP NE1  N Y N 498 
TRP CE2  C Y N 499 
TRP CE3  C Y N 500 
TRP CZ2  C Y N 501 
TRP CZ3  C Y N 502 
TRP CH2  C Y N 503 
TRP OXT  O N N 504 
TRP H    H N N 505 
TRP H2   H N N 506 
TRP HA   H N N 507 
TRP HB2  H N N 508 
TRP HB3  H N N 509 
TRP HD1  H N N 510 
TRP HE1  H N N 511 
TRP HE3  H N N 512 
TRP HZ2  H N N 513 
TRP HZ3  H N N 514 
TRP HH2  H N N 515 
TRP HXT  H N N 516 
TRS C    C N N 517 
TRS C1   C N N 518 
TRS C2   C N N 519 
TRS C3   C N N 520 
TRS N    N N N 521 
TRS O1   O N N 522 
TRS O2   O N N 523 
TRS O3   O N N 524 
TRS H11  H N N 525 
TRS H12  H N N 526 
TRS H21  H N N 527 
TRS H22  H N N 528 
TRS H31  H N N 529 
TRS H32  H N N 530 
TRS HN1  H N N 531 
TRS HN2  H N N 532 
TRS HN3  H N N 533 
TRS HO1  H N N 534 
TRS HO2  H N N 535 
TRS HO3  H N N 536 
TYR N    N N N 537 
TYR CA   C N S 538 
TYR C    C N N 539 
TYR O    O N N 540 
TYR CB   C N N 541 
TYR CG   C Y N 542 
TYR CD1  C Y N 543 
TYR CD2  C Y N 544 
TYR CE1  C Y N 545 
TYR CE2  C Y N 546 
TYR CZ   C Y N 547 
TYR OH   O N N 548 
TYR OXT  O N N 549 
TYR H    H N N 550 
TYR H2   H N N 551 
TYR HA   H N N 552 
TYR HB2  H N N 553 
TYR HB3  H N N 554 
TYR HD1  H N N 555 
TYR HD2  H N N 556 
TYR HE1  H N N 557 
TYR HE2  H N N 558 
TYR HH   H N N 559 
TYR HXT  H N N 560 
VAL N    N N N 561 
VAL CA   C N S 562 
VAL C    C N N 563 
VAL O    O N N 564 
VAL CB   C N N 565 
VAL CG1  C N N 566 
VAL CG2  C N N 567 
VAL OXT  O N N 568 
VAL H    H N N 569 
VAL H2   H N N 570 
VAL HA   H N N 571 
VAL HB   H N N 572 
VAL HG11 H N N 573 
VAL HG12 H N N 574 
VAL HG13 H N N 575 
VAL HG21 H N N 576 
VAL HG22 H N N 577 
VAL HG23 H N N 578 
VAL HXT  H N N 579 
# 
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  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
NO3 N   O1   doub N N 246 
NO3 N   O2   sing N N 247 
NO3 N   O3   sing N N 248 
PGE C1  O1   sing N N 249 
PGE C1  C2   sing N N 250 
PGE C1  H1   sing N N 251 
PGE C1  H12  sing N N 252 
PGE O1  HO1  sing N N 253 
PGE C2  O2   sing N N 254 
PGE C2  H2   sing N N 255 
PGE C2  H22  sing N N 256 
PGE O2  C3   sing N N 257 
PGE C3  C4   sing N N 258 
PGE C3  H3   sing N N 259 
PGE C3  H32  sing N N 260 
PGE C4  O3   sing N N 261 
PGE C4  H4   sing N N 262 
PGE C4  H42  sing N N 263 
PGE O4  C6   sing N N 264 
PGE O4  HO4  sing N N 265 
PGE C6  C5   sing N N 266 
PGE C6  H6   sing N N 267 
PGE C6  H62  sing N N 268 
PGE C5  O3   sing N N 269 
PGE C5  H5   sing N N 270 
PGE C5  H52  sing N N 271 
PHE N   CA   sing N N 272 
PHE N   H    sing N N 273 
PHE N   H2   sing N N 274 
PHE CA  C    sing N N 275 
PHE CA  CB   sing N N 276 
PHE CA  HA   sing N N 277 
PHE C   O    doub N N 278 
PHE C   OXT  sing N N 279 
PHE CB  CG   sing N N 280 
PHE CB  HB2  sing N N 281 
PHE CB  HB3  sing N N 282 
PHE CG  CD1  doub Y N 283 
PHE CG  CD2  sing Y N 284 
PHE CD1 CE1  sing Y N 285 
PHE CD1 HD1  sing N N 286 
PHE CD2 CE2  doub Y N 287 
PHE CD2 HD2  sing N N 288 
PHE CE1 CZ   doub Y N 289 
PHE CE1 HE1  sing N N 290 
PHE CE2 CZ   sing Y N 291 
PHE CE2 HE2  sing N N 292 
PHE CZ  HZ   sing N N 293 
PHE OXT HXT  sing N N 294 
PKZ O9A P3B  doub N N 295 
PKZ O2B C2B  sing N N 296 
PKZ P3B O3B  sing N N 297 
PKZ P3B O7A  sing N N 298 
PKZ P3B O8A  sing N N 299 
PKZ O3B C3B  sing N N 300 
PKZ C2B C3B  sing N N 301 
PKZ C2B C1B  sing N N 302 
PKZ C3B C4B  sing N N 303 
PKZ C8A N7A  doub Y N 304 
PKZ C8A N9A  sing Y N 305 
PKZ C1B N9A  sing N N 306 
PKZ C1B O4B  sing N N 307 
PKZ N7A C5A  sing Y N 308 
PKZ C4B C5B  sing N N 309 
PKZ C4B O4B  sing N N 310 
PKZ N9A C4A  sing Y N 311 
PKZ C5B O5B  sing N N 312 
PKZ C5A C4A  doub Y N 313 
PKZ C5A C6A  sing Y N 314 
PKZ C16 C15  sing N N 315 
PKZ C4A N3A  sing Y N 316 
PKZ N6A C6A  sing N N 317 
PKZ C6A N1A  doub Y N 318 
PKZ O5B P1A  sing N N 319 
PKZ N3A C2A  doub Y N 320 
PKZ O5A P2A  doub N N 321 
PKZ O4A P2A  sing N N 322 
PKZ C14 C15  sing N N 323 
PKZ C14 C13  sing N N 324 
PKZ N1A C2A  sing Y N 325 
PKZ P2A O3A  sing N N 326 
PKZ P2A O6A  sing N N 327 
PKZ P1A O3A  sing N N 328 
PKZ P1A O2A  doub N N 329 
PKZ P1A O1A  sing N N 330 
PKZ C13 C12  sing N N 331 
PKZ O6A CCP  sing N N 332 
PKZ C12 C11  sing N N 333 
PKZ CEP CBP  sing N N 334 
PKZ CCP CBP  sing N N 335 
PKZ CAP CBP  sing N N 336 
PKZ CAP OAP  sing N N 337 
PKZ CAP C9P  sing N N 338 
PKZ CBP CDP  sing N N 339 
PKZ O9P C9P  doub N N 340 
PKZ C11 C10  sing N N 341 
PKZ C9P N8P  sing N N 342 
PKZ C10 C9   sing N N 343 
PKZ N8P C7P  sing N N 344 
PKZ C9  C8   sing N N 345 
PKZ C7P C6P  sing N N 346 
PKZ C6P C5P  sing N N 347 
PKZ C8  C7   sing N N 348 
PKZ C6  C7   sing N N 349 
PKZ C6  C5   sing N N 350 
PKZ C4  C5   sing N N 351 
PKZ C4  C3   sing N N 352 
PKZ C5P N4P  sing N N 353 
PKZ C5P O5P  doub N N 354 
PKZ N4P C3P  sing N N 355 
PKZ O1  C1   doub N N 356 
PKZ C2P C3P  sing N N 357 
PKZ C2P S1P  sing N N 358 
PKZ C3  C2   sing N N 359 
PKZ C1  S1P  sing N N 360 
PKZ C1  C2   sing N N 361 
PKZ C3  H1   sing N N 362 
PKZ C3  H2   sing N N 363 
PKZ C10 H3   sing N N 364 
PKZ C10 H4   sing N N 365 
PKZ C8  H5   sing N N 366 
PKZ C8  H6   sing N N 367 
PKZ C7  H7   sing N N 368 
PKZ C7  H8   sing N N 369 
PKZ C5  H9   sing N N 370 
PKZ C5  H10  sing N N 371 
PKZ C11 H11  sing N N 372 
PKZ C11 H12  sing N N 373 
PKZ C13 H13  sing N N 374 
PKZ C13 H14  sing N N 375 
PKZ C16 H15  sing N N 376 
PKZ C16 H16  sing N N 377 
PKZ C16 H17  sing N N 378 
PKZ C15 H18  sing N N 379 
PKZ C15 H19  sing N N 380 
PKZ C14 H20  sing N N 381 
PKZ C14 H21  sing N N 382 
PKZ C2A H22  sing N N 383 
PKZ N6A H23  sing N N 384 
PKZ N6A H24  sing N N 385 
PKZ C8A H25  sing N N 386 
PKZ C1B H26  sing N N 387 
PKZ C2B H27  sing N N 388 
PKZ O2B H28  sing N N 389 
PKZ C3B H29  sing N N 390 
PKZ O7A H30  sing N N 391 
PKZ O8A H31  sing N N 392 
PKZ C4B H32  sing N N 393 
PKZ C5B H33  sing N N 394 
PKZ C5B H34  sing N N 395 
PKZ O1A H35  sing N N 396 
PKZ O4A H36  sing N N 397 
PKZ CCP H37  sing N N 398 
PKZ CCP H38  sing N N 399 
PKZ CDP H39  sing N N 400 
PKZ CDP H40  sing N N 401 
PKZ CDP H41  sing N N 402 
PKZ CEP H42  sing N N 403 
PKZ CEP H43  sing N N 404 
PKZ CEP H44  sing N N 405 
PKZ CAP H45  sing N N 406 
PKZ OAP H46  sing N N 407 
PKZ N8P H47  sing N N 408 
PKZ C7P H48  sing N N 409 
PKZ C7P H49  sing N N 410 
PKZ C6P H50  sing N N 411 
PKZ C6P H51  sing N N 412 
PKZ N4P H52  sing N N 413 
PKZ C3P H53  sing N N 414 
PKZ C3P H54  sing N N 415 
PKZ C2P H55  sing N N 416 
PKZ C2P H56  sing N N 417 
PKZ C2  H57  sing N N 418 
PKZ C2  H58  sing N N 419 
PKZ C4  H59  sing N N 420 
PKZ C4  H60  sing N N 421 
PKZ C6  H61  sing N N 422 
PKZ C6  H62  sing N N 423 
PKZ C9  H63  sing N N 424 
PKZ C9  H64  sing N N 425 
PKZ C12 H65  sing N N 426 
PKZ C12 H66  sing N N 427 
PRO N   CA   sing N N 428 
PRO N   CD   sing N N 429 
PRO N   H    sing N N 430 
PRO CA  C    sing N N 431 
PRO CA  CB   sing N N 432 
PRO CA  HA   sing N N 433 
PRO C   O    doub N N 434 
PRO C   OXT  sing N N 435 
PRO CB  CG   sing N N 436 
PRO CB  HB2  sing N N 437 
PRO CB  HB3  sing N N 438 
PRO CG  CD   sing N N 439 
PRO CG  HG2  sing N N 440 
PRO CG  HG3  sing N N 441 
PRO CD  HD2  sing N N 442 
PRO CD  HD3  sing N N 443 
PRO OXT HXT  sing N N 444 
SER N   CA   sing N N 445 
SER N   H    sing N N 446 
SER N   H2   sing N N 447 
SER CA  C    sing N N 448 
SER CA  CB   sing N N 449 
SER CA  HA   sing N N 450 
SER C   O    doub N N 451 
SER C   OXT  sing N N 452 
SER CB  OG   sing N N 453 
SER CB  HB2  sing N N 454 
SER CB  HB3  sing N N 455 
SER OG  HG   sing N N 456 
SER OXT HXT  sing N N 457 
THR N   CA   sing N N 458 
THR N   H    sing N N 459 
THR N   H2   sing N N 460 
THR CA  C    sing N N 461 
THR CA  CB   sing N N 462 
THR CA  HA   sing N N 463 
THR C   O    doub N N 464 
THR C   OXT  sing N N 465 
THR CB  OG1  sing N N 466 
THR CB  CG2  sing N N 467 
THR CB  HB   sing N N 468 
THR OG1 HG1  sing N N 469 
THR CG2 HG21 sing N N 470 
THR CG2 HG22 sing N N 471 
THR CG2 HG23 sing N N 472 
THR OXT HXT  sing N N 473 
TRP N   CA   sing N N 474 
TRP N   H    sing N N 475 
TRP N   H2   sing N N 476 
TRP CA  C    sing N N 477 
TRP CA  CB   sing N N 478 
TRP CA  HA   sing N N 479 
TRP C   O    doub N N 480 
TRP C   OXT  sing N N 481 
TRP CB  CG   sing N N 482 
TRP CB  HB2  sing N N 483 
TRP CB  HB3  sing N N 484 
TRP CG  CD1  doub Y N 485 
TRP CG  CD2  sing Y N 486 
TRP CD1 NE1  sing Y N 487 
TRP CD1 HD1  sing N N 488 
TRP CD2 CE2  doub Y N 489 
TRP CD2 CE3  sing Y N 490 
TRP NE1 CE2  sing Y N 491 
TRP NE1 HE1  sing N N 492 
TRP CE2 CZ2  sing Y N 493 
TRP CE3 CZ3  doub Y N 494 
TRP CE3 HE3  sing N N 495 
TRP CZ2 CH2  doub Y N 496 
TRP CZ2 HZ2  sing N N 497 
TRP CZ3 CH2  sing Y N 498 
TRP CZ3 HZ3  sing N N 499 
TRP CH2 HH2  sing N N 500 
TRP OXT HXT  sing N N 501 
TRS C   C1   sing N N 502 
TRS C   C2   sing N N 503 
TRS C   C3   sing N N 504 
TRS C   N    sing N N 505 
TRS C1  O1   sing N N 506 
TRS C1  H11  sing N N 507 
TRS C1  H12  sing N N 508 
TRS C2  O2   sing N N 509 
TRS C2  H21  sing N N 510 
TRS C2  H22  sing N N 511 
TRS C3  O3   sing N N 512 
TRS C3  H31  sing N N 513 
TRS C3  H32  sing N N 514 
TRS N   HN1  sing N N 515 
TRS N   HN2  sing N N 516 
TRS N   HN3  sing N N 517 
TRS O1  HO1  sing N N 518 
TRS O2  HO2  sing N N 519 
TRS O3  HO3  sing N N 520 
TYR N   CA   sing N N 521 
TYR N   H    sing N N 522 
TYR N   H2   sing N N 523 
TYR CA  C    sing N N 524 
TYR CA  CB   sing N N 525 
TYR CA  HA   sing N N 526 
TYR C   O    doub N N 527 
TYR C   OXT  sing N N 528 
TYR CB  CG   sing N N 529 
TYR CB  HB2  sing N N 530 
TYR CB  HB3  sing N N 531 
TYR CG  CD1  doub Y N 532 
TYR CG  CD2  sing Y N 533 
TYR CD1 CE1  sing Y N 534 
TYR CD1 HD1  sing N N 535 
TYR CD2 CE2  doub Y N 536 
TYR CD2 HD2  sing N N 537 
TYR CE1 CZ   doub Y N 538 
TYR CE1 HE1  sing N N 539 
TYR CE2 CZ   sing Y N 540 
TYR CE2 HE2  sing N N 541 
TYR CZ  OH   sing N N 542 
TYR OH  HH   sing N N 543 
TYR OXT HXT  sing N N 544 
VAL N   CA   sing N N 545 
VAL N   H    sing N N 546 
VAL N   H2   sing N N 547 
VAL CA  C    sing N N 548 
VAL CA  CB   sing N N 549 
VAL CA  HA   sing N N 550 
VAL C   O    doub N N 551 
VAL C   OXT  sing N N 552 
VAL CB  CG1  sing N N 553 
VAL CB  CG2  sing N N 554 
VAL CB  HB   sing N N 555 
VAL CG1 HG11 sing N N 556 
VAL CG1 HG12 sing N N 557 
VAL CG1 HG13 sing N N 558 
VAL CG2 HG21 sing N N 559 
VAL CG2 HG22 sing N N 560 
VAL CG2 HG23 sing N N 561 
VAL OXT HXT  sing N N 562 
# 
_pdbx_audit_support.funding_organization   'Cystic Fibrosis Trust' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           SRC017 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 6KPT ? 
2 ? 'experimental model' PDB 6IJC ? 
# 
_atom_sites.entry_id                    8PU5 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.010758 
_atom_sites.fract_transf_matrix[1][2]   0.006211 
_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]   0.012422 
_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]   0.007765 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP A 1 5   ? 32.030  -18.182 -16.662 1.00 37.55 ? 3    ASP B N   1 
ATOM   2    C CA  . ASP A 1 5   ? 31.418  -19.461 -17.081 1.00 36.49 ? 3    ASP B CA  1 
ATOM   3    C C   . ASP A 1 5   ? 30.197  -19.793 -16.196 1.00 29.43 ? 3    ASP B C   1 
ATOM   4    O O   . ASP A 1 5   ? 29.252  -20.270 -16.795 1.00 29.07 ? 3    ASP B O   1 
ATOM   5    C CB  . ASP A 1 5   ? 32.460  -20.570 -17.194 1.00 39.10 ? 3    ASP B CB  1 
ATOM   6    C CG  . ASP A 1 5   ? 31.915  -21.966 -17.062 1.00 36.46 ? 3    ASP B CG  1 
ATOM   7    O OD1 . ASP A 1 5   ? 31.861  -22.455 -15.914 1.00 33.20 ? 3    ASP B OD1 1 
ATOM   8    O OD2 . ASP A 1 5   ? 31.570  -22.562 -18.111 1.00 52.76 ? 3    ASP B OD2 1 
ATOM   9    N N   . TYR A 1 6   ? 30.179  -19.371 -14.936 1.00 21.40 ? 4    TYR B N   1 
ATOM   10   C CA  . TYR A 1 6   ? 28.906  -19.382 -14.194 1.00 20.38 ? 4    TYR B CA  1 
ATOM   11   C C   . TYR A 1 6   ? 27.915  -18.502 -14.976 1.00 18.97 ? 4    TYR B C   1 
ATOM   12   O O   . TYR A 1 6   ? 28.296  -17.425 -15.419 1.00 18.71 ? 4    TYR B O   1 
ATOM   13   C CB  . TYR A 1 6   ? 29.027  -18.784 -12.786 1.00 19.21 ? 4    TYR B CB  1 
ATOM   14   C CG  . TYR A 1 6   ? 27.708  -18.409 -12.160 1.00 17.34 ? 4    TYR B CG  1 
ATOM   15   C CD1 . TYR A 1 6   ? 26.797  -19.383 -11.794 1.00 16.47 ? 4    TYR B CD1 1 
ATOM   16   C CD2 . TYR A 1 6   ? 27.355  -17.086 -11.959 1.00 16.08 ? 4    TYR B CD2 1 
ATOM   17   C CE1 . TYR A 1 6   ? 25.574  -19.057 -11.237 1.00 16.63 ? 4    TYR B CE1 1 
ATOM   18   C CE2 . TYR A 1 6   ? 26.134  -16.742 -11.404 1.00 16.02 ? 4    TYR B CE2 1 
ATOM   19   C CZ  . TYR A 1 6   ? 25.241  -17.731 -11.039 1.00 15.98 ? 4    TYR B CZ  1 
ATOM   20   O OH  . TYR A 1 6   ? 24.035  -17.413 -10.491 1.00 16.25 ? 4    TYR B OH  1 
ATOM   21   N N   . LYS A 1 7   ? 26.700  -18.987 -15.179 1.00 18.79 ? 5    LYS B N   1 
ATOM   22   C CA  . LYS A 1 7   ? 25.601  -18.199 -15.782 1.00 20.16 ? 5    LYS B CA  1 
ATOM   23   C C   . LYS A 1 7   ? 24.447  -18.161 -14.784 1.00 18.22 ? 5    LYS B C   1 
ATOM   24   O O   . LYS A 1 7   ? 24.057  -19.227 -14.277 1.00 17.20 ? 5    LYS B O   1 
ATOM   25   C CB  . LYS A 1 7   ? 25.233  -18.785 -17.147 1.00 25.57 ? 5    LYS B CB  1 
ATOM   26   C CG  . LYS A 1 7   ? 24.060  -18.101 -17.823 1.00 32.44 ? 5    LYS B CG  1 
ATOM   27   C CD  . LYS A 1 7   ? 24.041  -18.250 -19.347 1.00 38.11 ? 5    LYS B CD  1 
ATOM   28   C CE  . LYS A 1 7   ? 23.167  -17.212 -20.028 1.00 37.88 ? 5    LYS B CE  1 
ATOM   29   N NZ  . LYS A 1 7   ? 23.917  -15.955 -20.275 1.00 42.92 ? 5    LYS B NZ  1 
ATOM   30   N N   . ALA A 1 8   ? 23.911  -16.975 -14.498 1.00 17.09 ? 6    ALA B N   1 
ATOM   31   C CA  . ALA A 1 8   ? 22.758  -16.866 -13.585 1.00 17.50 ? 6    ALA B CA  1 
ATOM   32   C C   . ALA A 1 8   ? 21.551  -17.516 -14.254 1.00 17.27 ? 6    ALA B C   1 
ATOM   33   O O   . ALA A 1 8   ? 21.288  -17.280 -15.436 1.00 16.72 ? 6    ALA B O   1 
ATOM   34   C CB  . ALA A 1 8   ? 22.451  -15.426 -13.234 1.00 17.72 ? 6    ALA B CB  1 
ATOM   35   N N   . PRO A 1 9   ? 20.760  -18.331 -13.510 1.00 16.16 ? 7    PRO B N   1 
ATOM   36   C CA  . PRO A 1 9   ? 19.542  -18.970 -14.036 1.00 16.17 ? 7    PRO B CA  1 
ATOM   37   C C   . PRO A 1 9   ? 18.357  -17.993 -14.000 1.00 17.17 ? 7    PRO B C   1 
ATOM   38   O O   . PRO A 1 9   ? 17.363  -18.293 -13.421 1.00 16.76 ? 7    PRO B O   1 
ATOM   39   C CB  . PRO A 1 9   ? 19.358  -20.170 -13.099 1.00 15.50 ? 7    PRO B CB  1 
ATOM   40   C CG  . PRO A 1 9   ? 19.835  -19.663 -11.768 1.00 14.70 ? 7    PRO B CG  1 
ATOM   41   C CD  . PRO A 1 9   ? 20.982  -18.738 -12.107 1.00 16.31 ? 7    PRO B CD  1 
ATOM   42   N N   . LEU A 1 10  ? 18.474  -16.913 -14.765 1.00 17.77 ? 8    LEU B N   1 
ATOM   43   C CA  . LEU A 1 10  ? 17.484  -15.823 -14.686 1.00 17.92 ? 8    LEU B CA  1 
ATOM   44   C C   . LEU A 1 10  ? 16.125  -16.272 -15.231 1.00 17.43 ? 8    LEU B C   1 
ATOM   45   O O   . LEU A 1 10  ? 15.113  -15.877 -14.640 1.00 17.47 ? 8    LEU B O   1 
ATOM   46   C CB  . LEU A 1 10  ? 18.004  -14.602 -15.452 1.00 21.30 ? 8    LEU B CB  1 
ATOM   47   C CG  . LEU A 1 10  ? 19.008  -13.736 -14.726 1.00 25.06 ? 8    LEU B CG  1 
ATOM   48   C CD1 . LEU A 1 10  ? 19.459  -12.599 -15.626 1.00 27.90 ? 8    LEU B CD1 1 
ATOM   49   C CD2 . LEU A 1 10  ? 18.445  -13.206 -13.437 1.00 26.49 ? 8    LEU B CD2 1 
ATOM   50   N N   . ARG A 1 11  ? 16.089  -17.015 -16.344 1.00 17.48 ? 9    ARG B N   1 
ATOM   51   C CA  . ARG A 1 11  ? 14.809  -17.469 -16.923 1.00 17.74 ? 9    ARG B CA  1 
ATOM   52   C C   . ARG A 1 11  ? 14.066  -18.316 -15.876 1.00 17.35 ? 9    ARG B C   1 
ATOM   53   O O   . ARG A 1 11  ? 12.852  -18.184 -15.738 1.00 17.93 ? 9    ARG B O   1 
ATOM   54   C CB  . ARG A 1 11  ? 15.003  -18.200 -18.245 1.00 18.53 ? 9    ARG B CB  1 
ATOM   55   C CG  . ARG A 1 11  ? 13.726  -18.782 -18.839 1.00 19.49 ? 9    ARG B CG  1 
ATOM   56   C CD  . ARG A 1 11  ? 12.788  -17.680 -19.334 1.00 23.49 ? 9    ARG B CD  1 
ATOM   57   N NE  . ARG A 1 11  ? 11.471  -18.123 -19.793 1.00 22.67 ? 9    ARG B NE  1 
ATOM   58   C CZ  . ARG A 1 11  ? 10.384  -18.235 -19.051 1.00 24.15 ? 9    ARG B CZ  1 
ATOM   59   N NH1 . ARG A 1 11  ? 10.417  -18.034 -17.739 1.00 24.17 ? 9    ARG B NH1 1 
ATOM   60   N NH2 . ARG A 1 11  ? 9.259   -18.605 -19.619 1.00 26.85 ? 9    ARG B NH2 1 
ATOM   61   N N   . ASP A 1 12  ? 14.777  -19.161 -15.131 1.00 17.26 ? 10   ASP B N   1 
ATOM   62   C CA  . ASP A 1 12  ? 14.100  -20.034 -14.136 1.00 14.82 ? 10   ASP B CA  1 
ATOM   63   C C   . ASP A 1 12  ? 13.651  -19.205 -12.923 1.00 15.24 ? 10   ASP B C   1 
ATOM   64   O O   . ASP A 1 12  ? 12.578  -19.453 -12.413 1.00 15.62 ? 10   ASP B O   1 
ATOM   65   C CB  . ASP A 1 12  ? 14.990  -21.199 -13.703 1.00 15.26 ? 10   ASP B CB  1 
ATOM   66   C CG  . ASP A 1 12  ? 14.170  -22.376 -13.208 1.00 16.47 ? 10   ASP B CG  1 
ATOM   67   O OD1 . ASP A 1 12  ? 13.400  -22.911 -14.008 1.00 18.08 ? 10   ASP B OD1 1 
ATOM   68   O OD2 . ASP A 1 12  ? 14.281  -22.713 -12.022 1.00 16.51 ? 10   ASP B OD2 1 
ATOM   69   N N   . ILE A 1 13  ? 14.498  -18.283 -12.497 1.00 15.53 ? 11   ILE B N   1 
ATOM   70   C CA  . ILE A 1 13  ? 14.134  -17.370 -11.375 1.00 16.88 ? 11   ILE B CA  1 
ATOM   71   C C   . ILE A 1 13  ? 12.848  -16.611 -11.751 1.00 17.89 ? 11   ILE B C   1 
ATOM   72   O O   . ILE A 1 13  ? 11.936  -16.602 -10.946 1.00 17.50 ? 11   ILE B O   1 
ATOM   73   C CB  . ILE A 1 13  ? 15.329  -16.453 -11.050 1.00 16.70 ? 11   ILE B CB  1 
ATOM   74   C CG1 . ILE A 1 13  ? 16.477  -17.238 -10.409 1.00 18.33 ? 11   ILE B CG1 1 
ATOM   75   C CG2 . ILE A 1 13  ? 14.902  -15.277 -10.190 1.00 18.44 ? 11   ILE B CG2 1 
ATOM   76   C CD1 . ILE A 1 13  ? 17.778  -16.478 -10.338 1.00 18.08 ? 11   ILE B CD1 1 
ATOM   77   N N   . ARG A 1 14  ? 12.798  -16.040 -12.957 1.00 17.07 ? 12   ARG B N   1 
ATOM   78   C CA  . ARG A 1 14  ? 11.552  -15.376 -13.436 1.00 17.95 ? 12   ARG B CA  1 
ATOM   79   C C   . ARG A 1 14  ? 10.367  -16.340 -13.521 1.00 18.53 ? 12   ARG B C   1 
ATOM   80   O O   . ARG A 1 14  ? 9.236   -15.964 -13.104 1.00 19.45 ? 12   ARG B O   1 
ATOM   81   C CB  . ARG A 1 14  ? 11.850  -14.710 -14.773 1.00 20.61 ? 12   ARG B CB  1 
ATOM   82   C CG  . ARG A 1 14  ? 12.709  -13.476 -14.592 1.00 23.15 ? 12   ARG B CG  1 
ATOM   83   C CD  . ARG A 1 14  ? 13.242  -12.921 -15.890 1.00 30.69 ? 12   ARG B CD  1 
ATOM   84   N NE  . ARG A 1 14  ? 14.024  -11.730 -15.586 1.00 34.12 ? 12   ARG B NE  1 
ATOM   85   C CZ  . ARG A 1 14  ? 15.071  -11.290 -16.270 1.00 39.26 ? 12   ARG B CZ  1 
ATOM   86   N NH1 . ARG A 1 14  ? 15.527  -11.948 -17.329 1.00 40.76 ? 12   ARG B NH1 1 
ATOM   87   N NH2 . ARG A 1 14  ? 15.658  -10.174 -15.890 1.00 41.69 ? 12   ARG B NH2 1 
ATOM   88   N N   . PHE A 1 15  ? 10.571  -17.562 -14.020 1.00 17.31 ? 13   PHE B N   1 
ATOM   89   C CA  . PHE A 1 15  ? 9.531   -18.608 -14.068 1.00 17.34 ? 13   PHE B CA  1 
ATOM   90   C C   . PHE A 1 15  ? 8.950   -18.820 -12.676 1.00 17.01 ? 13   PHE B C   1 
ATOM   91   O O   . PHE A 1 15  ? 7.712   -18.793 -12.472 1.00 16.54 ? 13   PHE B O   1 
ATOM   92   C CB  . PHE A 1 15  ? 10.068  -19.913 -14.670 1.00 17.84 ? 13   PHE B CB  1 
ATOM   93   C CG  . PHE A 1 15  ? 9.119   -21.069 -14.460 1.00 19.21 ? 13   PHE B CG  1 
ATOM   94   C CD1 . PHE A 1 15  ? 7.932   -21.171 -15.179 1.00 19.25 ? 13   PHE B CD1 1 
ATOM   95   C CD2 . PHE A 1 15  ? 9.373   -22.005 -13.471 1.00 18.44 ? 13   PHE B CD2 1 
ATOM   96   C CE1 . PHE A 1 15  ? 7.039   -22.204 -14.940 1.00 20.73 ? 13   PHE B CE1 1 
ATOM   97   C CE2 . PHE A 1 15  ? 8.488   -23.040 -13.234 1.00 18.87 ? 13   PHE B CE2 1 
ATOM   98   C CZ  . PHE A 1 15  ? 7.322   -23.140 -13.953 1.00 19.24 ? 13   PHE B CZ  1 
ATOM   99   N N   . VAL A 1 16  ? 9.817   -19.086 -11.716 1.00 15.78 ? 14   VAL B N   1 
ATOM   100  C CA  . VAL A 1 16  ? 9.331   -19.392 -10.345 1.00 16.16 ? 14   VAL B CA  1 
ATOM   101  C C   . VAL A 1 16  ? 8.635   -18.175 -9.729  1.00 16.42 ? 14   VAL B C   1 
ATOM   102  O O   . VAL A 1 16  ? 7.541   -18.351 -9.206  1.00 16.58 ? 14   VAL B O   1 
ATOM   103  C CB  . VAL A 1 16  ? 10.518  -19.831 -9.467  1.00 16.08 ? 14   VAL B CB  1 
ATOM   104  C CG1 . VAL A 1 16  ? 10.177  -19.846 -7.985  1.00 16.03 ? 14   VAL B CG1 1 
ATOM   105  C CG2 . VAL A 1 16  ? 11.082  -21.171 -9.908  1.00 15.63 ? 14   VAL B CG2 1 
ATOM   106  N N   . ARG A 1 17  ? 9.277   -17.012 -9.795  1.00 16.05 ? 15   ARG B N   1 
ATOM   107  C CA  . ARG A 1 17  ? 8.757   -15.822 -9.100  1.00 17.48 ? 15   ARG B CA  1 
ATOM   108  C C   . ARG A 1 17  ? 7.461   -15.367 -9.806  1.00 19.57 ? 15   ARG B C   1 
ATOM   109  O O   . ARG A 1 17  ? 6.426   -15.248 -9.156  1.00 21.11 ? 15   ARG B O   1 
ATOM   110  C CB  . ARG A 1 17  ? 9.842   -14.749 -9.044  1.00 18.87 ? 15   ARG B CB  1 
ATOM   111  C CG  . ARG A 1 17  ? 10.975  -15.048 -8.083  1.00 18.81 ? 15   ARG B CG  1 
ATOM   112  C CD  . ARG A 1 17  ? 12.145  -14.121 -8.313  1.00 21.01 ? 15   ARG B CD  1 
ATOM   113  N NE  . ARG A 1 17  ? 11.769  -12.726 -8.085  1.00 21.33 ? 15   ARG B NE  1 
ATOM   114  C CZ  . ARG A 1 17  ? 11.914  -12.105 -6.924  1.00 21.35 ? 15   ARG B CZ  1 
ATOM   115  N NH1 . ARG A 1 17  ? 12.409  -12.762 -5.888  1.00 20.77 ? 15   ARG B NH1 1 
ATOM   116  N NH2 . ARG A 1 17  ? 11.531  -10.841 -6.784  1.00 21.33 ? 15   ARG B NH2 1 
ATOM   117  N N   . ASP A 1 18  ? 7.552   -15.086 -11.094 1.00 18.93 ? 16   ASP B N   1 
ATOM   118  C CA  . ASP A 1 18  ? 6.427   -14.400 -11.775 1.00 20.94 ? 16   ASP B CA  1 
ATOM   119  C C   . ASP A 1 18  ? 5.321   -15.337 -12.233 1.00 22.79 ? 16   ASP B C   1 
ATOM   120  O O   . ASP A 1 18  ? 4.161   -14.962 -12.127 1.00 24.01 ? 16   ASP B O   1 
ATOM   121  C CB  . ASP A 1 18  ? 6.992   -13.602 -12.953 1.00 21.40 ? 16   ASP B CB  1 
ATOM   122  C CG  . ASP A 1 18  ? 8.121   -12.665 -12.568 1.00 25.98 ? 16   ASP B CG  1 
ATOM   123  O OD1 . ASP A 1 18  ? 8.148   -12.222 -11.409 1.00 28.59 ? 16   ASP B OD1 1 
ATOM   124  O OD2 . ASP A 1 18  ? 8.956   -12.382 -13.435 1.00 30.65 ? 16   ASP B OD2 1 
ATOM   125  N N   . GLU A 1 19  ? 5.681   -16.515 -12.687 1.00 21.11 ? 17   GLU B N   1 
ATOM   126  C CA  . GLU A 1 19  ? 4.672   -17.420 -13.273 1.00 20.14 ? 17   GLU B CA  1 
ATOM   127  C C   . GLU A 1 19  ? 4.126   -18.363 -12.202 1.00 21.14 ? 17   GLU B C   1 
ATOM   128  O O   . GLU A 1 19  ? 2.897   -18.488 -12.057 1.00 22.61 ? 17   GLU B O   1 
ATOM   129  C CB  . GLU A 1 19  ? 5.253   -18.202 -14.442 1.00 21.24 ? 17   GLU B CB  1 
ATOM   130  C CG  . GLU A 1 19  ? 5.883   -17.308 -15.493 1.00 22.84 ? 17   GLU B CG  1 
ATOM   131  C CD  . GLU A 1 19  ? 6.458   -18.107 -16.653 1.00 23.79 ? 17   GLU B CD  1 
ATOM   132  O OE1 . GLU A 1 19  ? 7.613   -17.782 -17.084 1.00 25.17 ? 17   GLU B OE1 1 
ATOM   133  O OE2 . GLU A 1 19  ? 5.784   -19.087 -17.082 1.00 23.39 ? 17   GLU B OE2 1 
ATOM   134  N N   . LEU A 1 20  ? 5.022   -19.037 -11.482 1.00 19.26 ? 18   LEU B N   1 
ATOM   135  C CA  . LEU A 1 20  ? 4.575   -20.010 -10.476 1.00 19.07 ? 18   LEU B CA  1 
ATOM   136  C C   . LEU A 1 20  ? 3.966   -19.288 -9.266  1.00 18.21 ? 18   LEU B C   1 
ATOM   137  O O   . LEU A 1 20  ? 2.945   -19.758 -8.781  1.00 19.25 ? 18   LEU B O   1 
ATOM   138  C CB  . LEU A 1 20  ? 5.733   -20.926 -10.061 1.00 17.59 ? 18   LEU B CB  1 
ATOM   139  C CG  . LEU A 1 20  ? 5.318   -22.085 -9.147  1.00 19.10 ? 18   LEU B CG  1 
ATOM   140  C CD1 . LEU A 1 20  ? 4.506   -23.114 -9.917  1.00 19.69 ? 18   LEU B CD1 1 
ATOM   141  C CD2 . LEU A 1 20  ? 6.548   -22.722 -8.513  1.00 19.20 ? 18   LEU B CD2 1 
ATOM   142  N N   . LEU A 1 21  ? 4.598   -18.257 -8.738  1.00 17.22 ? 19   LEU B N   1 
ATOM   143  C CA  . LEU A 1 21  ? 4.265   -17.735 -7.381  1.00 18.73 ? 19   LEU B CA  1 
ATOM   144  C C   . LEU A 1 21  ? 3.657   -16.335 -7.479  1.00 20.42 ? 19   LEU B C   1 
ATOM   145  O O   . LEU A 1 21  ? 3.468   -15.727 -6.410  1.00 22.33 ? 19   LEU B O   1 
ATOM   146  C CB  . LEU A 1 21  ? 5.541   -17.719 -6.540  1.00 18.92 ? 19   LEU B CB  1 
ATOM   147  C CG  . LEU A 1 21  ? 6.146   -19.101 -6.259  1.00 17.61 ? 19   LEU B CG  1 
ATOM   148  C CD1 . LEU A 1 21  ? 7.437   -18.964 -5.476  1.00 18.35 ? 19   LEU B CD1 1 
ATOM   149  C CD2 . LEU A 1 21  ? 5.134   -20.007 -5.571  1.00 17.15 ? 19   LEU B CD2 1 
ATOM   150  N N   . GLY A 1 22  ? 3.324   -15.850 -8.675  1.00 21.97 ? 20   GLY B N   1 
ATOM   151  C CA  . GLY A 1 22  ? 2.588   -14.570 -8.809  1.00 22.16 ? 20   GLY B CA  1 
ATOM   152  C C   . GLY A 1 22  ? 3.237   -13.400 -8.105  1.00 21.29 ? 20   GLY B C   1 
ATOM   153  O O   . GLY A 1 22  ? 2.530   -12.685 -7.394  1.00 23.75 ? 20   GLY B O   1 
ATOM   154  N N   . TYR A 1 23  ? 4.520   -13.171 -8.355  1.00 19.65 ? 21   TYR B N   1 
ATOM   155  C CA  . TYR A 1 23  ? 5.244   -12.121 -7.600  1.00 19.07 ? 21   TYR B CA  1 
ATOM   156  C C   . TYR A 1 23  ? 4.693   -10.724 -7.924  1.00 20.55 ? 21   TYR B C   1 
ATOM   157  O O   . TYR A 1 23  ? 4.713   -9.877  -7.047  1.00 21.83 ? 21   TYR B O   1 
ATOM   158  C CB  . TYR A 1 23  ? 6.757   -12.253 -7.787  1.00 19.00 ? 21   TYR B CB  1 
ATOM   159  C CG  . TYR A 1 23  ? 7.464   -12.911 -6.628  1.00 18.33 ? 21   TYR B CG  1 
ATOM   160  C CD1 . TYR A 1 23  ? 7.184   -14.218 -6.273  1.00 18.95 ? 21   TYR B CD1 1 
ATOM   161  C CD2 . TYR A 1 23  ? 8.401   -12.225 -5.877  1.00 18.32 ? 21   TYR B CD2 1 
ATOM   162  C CE1 . TYR A 1 23  ? 7.821   -14.828 -5.206  1.00 18.27 ? 21   TYR B CE1 1 
ATOM   163  C CE2 . TYR A 1 23  ? 9.047   -12.819 -4.807  1.00 19.24 ? 21   TYR B CE2 1 
ATOM   164  C CZ  . TYR A 1 23  ? 8.757   -14.128 -4.468  1.00 18.17 ? 21   TYR B CZ  1 
ATOM   165  O OH  . TYR A 1 23  ? 9.385   -14.725 -3.417  1.00 17.68 ? 21   TYR B OH  1 
ATOM   166  N N   . GLU A 1 24  ? 4.234   -10.511 -9.149  1.00 22.00 ? 22   GLU B N   1 
ATOM   167  C CA  . GLU A 1 24  ? 3.753   -9.150  -9.507  1.00 25.12 ? 22   GLU B CA  1 
ATOM   168  C C   . GLU A 1 24  ? 2.557   -8.802  -8.615  1.00 25.83 ? 22   GLU B C   1 
ATOM   169  O O   . GLU A 1 24  ? 2.587   -7.757  -7.977  1.00 26.31 ? 22   GLU B O   1 
ATOM   170  C CB  . GLU A 1 24  ? 3.379   -9.080  -10.986 1.00 25.85 ? 22   GLU B CB  1 
ATOM   171  C CG  . GLU A 1 24  ? 2.888   -7.704  -11.389 1.00 28.82 ? 22   GLU B CG  1 
ATOM   172  C CD  . GLU A 1 24  ? 2.748   -7.474  -12.881 1.00 33.37 ? 22   GLU B CD  1 
ATOM   173  O OE1 . GLU A 1 24  ? 2.527   -6.318  -13.275 1.00 37.34 ? 22   GLU B OE1 1 
ATOM   174  O OE2 . GLU A 1 24  ? 2.858   -8.444  -13.638 1.00 31.73 ? 22   GLU B OE2 1 
ATOM   175  N N   . ALA A 1 25  ? 1.567   -9.674  -8.548  1.00 24.93 ? 23   ALA B N   1 
ATOM   176  C CA  . ALA A 1 25  ? 0.396   -9.421  -7.685  1.00 25.58 ? 23   ALA B CA  1 
ATOM   177  C C   . ALA A 1 25  ? 0.806   -9.406  -6.210  1.00 26.09 ? 23   ALA B C   1 
ATOM   178  O O   . ALA A 1 25  ? 0.227   -8.652  -5.430  1.00 26.12 ? 23   ALA B O   1 
ATOM   179  C CB  . ALA A 1 25  ? -0.641  -10.467 -7.964  1.00 25.44 ? 23   ALA B CB  1 
ATOM   180  N N   . HIS A 1 26  ? 1.788   -10.224 -5.857  1.00 22.58 ? 24   HIS B N   1 
ATOM   181  C CA  . HIS A 1 26  ? 2.288   -10.224 -4.465  1.00 20.88 ? 24   HIS B CA  1 
ATOM   182  C C   . HIS A 1 26  ? 2.806   -8.819  -4.107  1.00 22.97 ? 24   HIS B C   1 
ATOM   183  O O   . HIS A 1 26  ? 2.443   -8.314  -3.059  1.00 24.86 ? 24   HIS B O   1 
ATOM   184  C CB  . HIS A 1 26  ? 3.360   -11.321 -4.323  1.00 20.01 ? 24   HIS B CB  1 
ATOM   185  C CG  . HIS A 1 26  ? 4.152   -11.287 -3.067  1.00 18.96 ? 24   HIS B CG  1 
ATOM   186  N ND1 . HIS A 1 26  ? 3.644   -11.690 -1.838  1.00 19.11 ? 24   HIS B ND1 1 
ATOM   187  C CD2 . HIS A 1 26  ? 5.465   -11.043 -2.884  1.00 18.33 ? 24   HIS B CD2 1 
ATOM   188  C CE1 . HIS A 1 26  ? 4.603   -11.600 -0.944  1.00 20.71 ? 24   HIS B CE1 1 
ATOM   189  N NE2 . HIS A 1 26  ? 5.723   -11.182 -1.564  1.00 18.77 ? 24   HIS B NE2 1 
ATOM   190  N N   . TYR A 1 27  ? 3.686   -8.255  -4.917  1.00 22.53 ? 25   TYR B N   1 
ATOM   191  C CA  . TYR A 1 27  ? 4.321   -6.950  -4.632  1.00 24.16 ? 25   TYR B CA  1 
ATOM   192  C C   . TYR A 1 27  ? 3.213   -5.880  -4.686  1.00 26.76 ? 25   TYR B C   1 
ATOM   193  O O   . TYR A 1 27  ? 3.279   -4.934  -3.878  1.00 24.77 ? 25   TYR B O   1 
ATOM   194  C CB  . TYR A 1 27  ? 5.489   -6.664  -5.576  1.00 26.67 ? 25   TYR B CB  1 
ATOM   195  C CG  . TYR A 1 27  ? 6.774   -7.421  -5.294  1.00 22.26 ? 25   TYR B CG  1 
ATOM   196  C CD1 . TYR A 1 27  ? 6.996   -8.059  -4.089  1.00 22.42 ? 25   TYR B CD1 1 
ATOM   197  C CD2 . TYR A 1 27  ? 7.792   -7.438  -6.227  1.00 22.48 ? 25   TYR B CD2 1 
ATOM   198  C CE1 . TYR A 1 27  ? 8.185   -8.735  -3.841  1.00 21.83 ? 25   TYR B CE1 1 
ATOM   199  C CE2 . TYR A 1 27  ? 9.002   -8.061  -5.975  1.00 22.62 ? 25   TYR B CE2 1 
ATOM   200  C CZ  . TYR A 1 27  ? 9.184   -8.743  -4.790  1.00 22.04 ? 25   TYR B CZ  1 
ATOM   201  O OH  . TYR A 1 27  ? 10.358  -9.399  -4.535  1.00 19.00 ? 25   TYR B OH  1 
ATOM   202  N N   . GLN A 1 28  ? 2.237   -6.062  -5.574  1.00 27.40 ? 26   GLN B N   1 
ATOM   203  C CA  . GLN A 1 28  ? 1.104   -5.101  -5.752  1.00 31.94 ? 26   GLN B CA  1 
ATOM   204  C C   . GLN A 1 28  ? 0.315   -5.009  -4.438  1.00 31.68 ? 26   GLN B C   1 
ATOM   205  O O   . GLN A 1 28  ? -0.160  -3.895  -4.101  1.00 32.34 ? 26   GLN B O   1 
ATOM   206  C CB  . GLN A 1 28  ? 0.227   -5.494  -6.938  1.00 34.97 ? 26   GLN B CB  1 
ATOM   207  C CG  . GLN A 1 28  ? 0.795   -5.074  -8.284  1.00 38.91 ? 26   GLN B CG  1 
ATOM   208  C CD  . GLN A 1 28  ? 0.051   -5.595  -9.504  1.00 50.23 ? 26   GLN B CD  1 
ATOM   209  O OE1 . GLN A 1 28  ? 0.111   -5.005  -10.587 1.00 57.80 ? 26   GLN B OE1 1 
ATOM   210  N NE2 . GLN A 1 28  ? -0.618  -6.736  -9.384  1.00 48.85 ? 26   GLN B NE2 1 
ATOM   211  N N   . SER A 1 29  ? 0.214   -6.109  -3.699  1.00 28.45 ? 27   SER B N   1 
ATOM   212  C CA  . SER A 1 29  ? -0.637  -6.277  -2.493  1.00 28.93 ? 27   SER B CA  1 
ATOM   213  C C   . SER A 1 29  ? 0.088   -5.780  -1.233  1.00 29.01 ? 27   SER B C   1 
ATOM   214  O O   . SER A 1 29  ? -0.547  -5.724  -0.176  1.00 31.60 ? 27   SER B O   1 
ATOM   215  C CB  . SER A 1 29  ? -1.052  -7.714  -2.323  1.00 29.76 ? 27   SER B CB  1 
ATOM   216  O OG  . SER A 1 29  ? 0.015   -8.482  -1.735  1.00 29.71 ? 27   SER B OG  1 
ATOM   217  N N   . LEU A 1 30  ? 1.378   -5.468  -1.294  1.00 28.84 ? 28   LEU B N   1 
ATOM   218  C CA  . LEU A 1 30  ? 2.130   -5.276  -0.032  1.00 32.33 ? 28   LEU B CA  1 
ATOM   219  C C   . LEU A 1 30  ? 2.602   -3.836  0.100   1.00 30.50 ? 28   LEU B C   1 
ATOM   220  O O   . LEU A 1 30  ? 3.253   -3.309  -0.803  1.00 31.79 ? 28   LEU B O   1 
ATOM   221  C CB  . LEU A 1 30  ? 3.305   -6.255  0.025   1.00 36.56 ? 28   LEU B CB  1 
ATOM   222  C CG  . LEU A 1 30  ? 2.925   -7.687  0.406   1.00 38.29 ? 28   LEU B CG  1 
ATOM   223  C CD1 . LEU A 1 30  ? 4.170   -8.568  0.473   1.00 35.93 ? 28   LEU B CD1 1 
ATOM   224  C CD2 . LEU A 1 30  ? 2.175   -7.740  1.725   1.00 37.48 ? 28   LEU B CD2 1 
ATOM   225  N N   . PRO A 1 31  ? 2.344   -3.217  1.272   1.00 30.77 ? 29   PRO B N   1 
ATOM   226  C CA  . PRO A 1 31  ? 2.812   -1.863  1.550   1.00 31.33 ? 29   PRO B CA  1 
ATOM   227  C C   . PRO A 1 31  ? 4.308   -1.744  1.248   1.00 35.10 ? 29   PRO B C   1 
ATOM   228  O O   . PRO A 1 31  ? 5.057   -2.655  1.649   1.00 34.98 ? 29   PRO B O   1 
ATOM   229  C CB  . PRO A 1 31  ? 2.583   -1.695  3.060   1.00 32.30 ? 29   PRO B CB  1 
ATOM   230  C CG  . PRO A 1 31  ? 1.453   -2.651  3.381   1.00 33.78 ? 29   PRO B CG  1 
ATOM   231  C CD  . PRO A 1 31  ? 1.612   -3.802  2.410   1.00 30.30 ? 29   PRO B CD  1 
ATOM   232  N N   . GLY A 1 32  ? 4.693   -0.687  0.529   1.00 31.79 ? 30   GLY B N   1 
ATOM   233  C CA  . GLY A 1 32  ? 6.092   -0.312  0.282   1.00 34.36 ? 30   GLY B CA  1 
ATOM   234  C C   . GLY A 1 32  ? 6.636   -0.913  -0.993  1.00 36.25 ? 30   GLY B C   1 
ATOM   235  O O   . GLY A 1 32  ? 7.695   -0.443  -1.441  1.00 37.59 ? 30   GLY B O   1 
ATOM   236  N N   . ALA A 1 33  ? 5.958   -1.919  -1.551  1.00 37.95 ? 31   ALA B N   1 
ATOM   237  C CA  . ALA A 1 33  ? 6.452   -2.751  -2.672  1.00 39.98 ? 31   ALA B CA  1 
ATOM   238  C C   . ALA A 1 33  ? 5.838   -2.267  -3.984  1.00 46.80 ? 31   ALA B C   1 
ATOM   239  O O   . ALA A 1 33  ? 6.248   -2.784  -5.034  1.00 43.76 ? 31   ALA B O   1 
ATOM   240  C CB  . ALA A 1 33  ? 6.102   -4.202  -2.416  1.00 38.73 ? 31   ALA B CB  1 
ATOM   241  N N   . GLU A 1 34  ? 4.862   -1.352  -3.923  1.00 49.98 ? 32   GLU B N   1 
ATOM   242  C CA  . GLU A 1 34  ? 3.996   -0.999  -5.082  1.00 57.31 ? 32   GLU B CA  1 
ATOM   243  C C   . GLU A 1 34  ? 4.876   -0.441  -6.215  1.00 60.63 ? 32   GLU B C   1 
ATOM   244  O O   . GLU A 1 34  ? 4.486   -0.620  -7.379  1.00 62.00 ? 32   GLU B O   1 
ATOM   245  C CB  . GLU A 1 34  ? 2.877   -0.037  -4.662  1.00 58.12 ? 32   GLU B CB  1 
ATOM   246  C CG  . GLU A 1 34  ? 1.949   -0.581  -3.569  1.00 58.86 ? 32   GLU B CG  1 
ATOM   247  C CD  . GLU A 1 34  ? 2.219   -0.108  -2.142  1.00 60.13 ? 32   GLU B CD  1 
ATOM   248  O OE1 . GLU A 1 34  ? 3.343   0.360   -1.874  1.00 60.17 ? 32   GLU B OE1 1 
ATOM   249  O OE2 . GLU A 1 34  ? 1.303   -0.210  -1.290  1.00 55.67 ? 32   GLU B OE2 1 
ATOM   250  N N   . ASP A 1 35  ? 6.030   0.163   -5.888  1.00 64.55 ? 33   ASP B N   1 
ATOM   251  C CA  . ASP A 1 35  ? 7.029   0.704   -6.857  1.00 66.22 ? 33   ASP B CA  1 
ATOM   252  C C   . ASP A 1 35  ? 7.955   -0.396  -7.405  1.00 66.77 ? 33   ASP B C   1 
ATOM   253  O O   . ASP A 1 35  ? 8.655   -0.114  -8.396  1.00 70.60 ? 33   ASP B O   1 
ATOM   254  C CB  . ASP A 1 35  ? 7.907   1.790   -6.226  1.00 71.73 ? 33   ASP B CB  1 
ATOM   255  C CG  . ASP A 1 35  ? 8.882   1.270   -5.179  1.00 77.11 ? 33   ASP B CG  1 
ATOM   256  O OD1 . ASP A 1 35  ? 8.417   0.896   -4.079  1.00 76.55 ? 33   ASP B OD1 1 
ATOM   257  O OD2 . ASP A 1 35  ? 10.100  1.231   -5.472  1.00 79.62 ? 33   ASP B OD2 1 
ATOM   258  N N   . ALA A 1 36  ? 8.025   -1.573  -6.767  1.00 59.83 ? 34   ALA B N   1 
ATOM   259  C CA  . ALA A 1 36  ? 8.826   -2.729  -7.243  1.00 53.70 ? 34   ALA B CA  1 
ATOM   260  C C   . ALA A 1 36  ? 8.127   -3.323  -8.469  1.00 44.96 ? 34   ALA B C   1 
ATOM   261  O O   . ALA A 1 36  ? 7.619   -4.452  -8.382  1.00 37.25 ? 34   ALA B O   1 
ATOM   262  C CB  . ALA A 1 36  ? 9.029   -3.752  -6.143  1.00 52.38 ? 34   ALA B CB  1 
ATOM   263  N N   . THR A 1 37  ? 8.105   -2.562  -9.568  1.00 47.13 ? 35   THR B N   1 
ATOM   264  C CA  . THR A 1 37  ? 7.404   -2.899  -10.839 1.00 50.00 ? 35   THR B CA  1 
ATOM   265  C C   . THR A 1 37  ? 8.211   -3.921  -11.629 1.00 47.06 ? 35   THR B C   1 
ATOM   266  O O   . THR A 1 37  ? 9.431   -4.004  -11.478 1.00 44.53 ? 35   THR B O   1 
ATOM   267  C CB  . THR A 1 37  ? 7.208   -1.669  -11.733 1.00 50.51 ? 35   THR B CB  1 
ATOM   268  O OG1 . THR A 1 37  ? 8.481   -1.364  -12.301 1.00 49.55 ? 35   THR B OG1 1 
ATOM   269  C CG2 . THR A 1 37  ? 6.640   -0.480  -10.992 1.00 51.50 ? 35   THR B CG2 1 
ATOM   270  N N   . PRO A 1 38  ? 7.561   -4.708  -12.511 1.00 44.74 ? 36   PRO B N   1 
ATOM   271  C CA  . PRO A 1 38  ? 8.258   -5.734  -13.280 1.00 42.85 ? 36   PRO B CA  1 
ATOM   272  C C   . PRO A 1 38  ? 9.506   -5.214  -14.005 1.00 40.07 ? 36   PRO B C   1 
ATOM   273  O O   . PRO A 1 38  ? 10.496  -5.906  -13.947 1.00 38.07 ? 36   PRO B O   1 
ATOM   274  C CB  . PRO A 1 38  ? 7.194   -6.222  -14.271 1.00 45.69 ? 36   PRO B CB  1 
ATOM   275  C CG  . PRO A 1 38  ? 5.898   -5.996  -13.535 1.00 44.28 ? 36   PRO B CG  1 
ATOM   276  C CD  . PRO A 1 38  ? 6.111   -4.701  -12.782 1.00 46.87 ? 36   PRO B CD  1 
ATOM   277  N N   . ASP A 1 39  ? 9.455   -4.030  -14.634 1.00 35.71 ? 37   ASP B N   1 
ATOM   278  C CA  . ASP A 1 39  ? 10.599  -3.528  -15.440 1.00 35.61 ? 37   ASP B CA  1 
ATOM   279  C C   . ASP A 1 39  ? 11.765  -3.180  -14.506 1.00 30.72 ? 37   ASP B C   1 
ATOM   280  O O   . ASP A 1 39  ? 12.918  -3.499  -14.856 1.00 30.92 ? 37   ASP B O   1 
ATOM   281  C CB  . ASP A 1 39  ? 10.227  -2.324  -16.308 1.00 40.80 ? 37   ASP B CB  1 
ATOM   282  C CG  . ASP A 1 39  ? 9.364   -2.639  -17.521 1.00 43.08 ? 37   ASP B CG  1 
ATOM   283  O OD1 . ASP A 1 39  ? 9.056   -3.842  -17.773 1.00 42.81 ? 37   ASP B OD1 1 
ATOM   284  O OD2 . ASP A 1 39  ? 9.005   -1.665  -18.213 1.00 45.80 ? 37   ASP B OD2 1 
ATOM   285  N N   . MET A 1 40  ? 11.484  -2.524  -13.382 1.00 31.03 ? 38   MET B N   1 
ATOM   286  C CA  . MET A 1 40  ? 12.508  -2.149  -12.375 1.00 30.80 ? 38   MET B CA  1 
ATOM   287  C C   . MET A 1 40  ? 13.139  -3.434  -11.812 1.00 26.19 ? 38   MET B C   1 
ATOM   288  O O   . MET A 1 40  ? 14.390  -3.504  -11.747 1.00 26.35 ? 38   MET B O   1 
ATOM   289  C CB  . MET A 1 40  ? 11.894  -1.326  -11.238 1.00 38.41 ? 38   MET B CB  1 
ATOM   290  C CG  . MET A 1 40  ? 12.928  -0.736  -10.292 1.00 48.51 ? 38   MET B CG  1 
ATOM   291  S SD  . MET A 1 40  ? 12.251  -0.392  -8.633  1.00 65.04 ? 38   MET B SD  1 
ATOM   292  C CE  . MET A 1 40  ? 13.480  0.763   -8.021  1.00 63.51 ? 38   MET B CE  1 
ATOM   293  N N   . VAL A 1 41  ? 12.304  -4.360  -11.341 1.00 27.00 ? 39   VAL B N   1 
ATOM   294  C CA  . VAL A 1 41  ? 12.752  -5.670  -10.785 1.00 27.82 ? 39   VAL B CA  1 
ATOM   295  C C   . VAL A 1 41  ? 13.624  -6.410  -11.810 1.00 27.66 ? 39   VAL B C   1 
ATOM   296  O O   . VAL A 1 41  ? 14.733  -6.848  -11.452 1.00 24.15 ? 39   VAL B O   1 
ATOM   297  C CB  . VAL A 1 41  ? 11.568  -6.535  -10.312 1.00 29.50 ? 39   VAL B CB  1 
ATOM   298  C CG1 . VAL A 1 41  ? 12.013  -7.965  -10.029 1.00 32.16 ? 39   VAL B CG1 1 
ATOM   299  C CG2 . VAL A 1 41  ? 10.884  -5.924  -9.112  1.00 30.73 ? 39   VAL B CG2 1 
ATOM   300  N N   . ASN A 1 42  ? 13.186  -6.533  -13.066 1.00 29.16 ? 40   ASN B N   1 
ATOM   301  C CA  . ASN A 1 42  ? 13.985  -7.253  -14.091 1.00 27.82 ? 40   ASN B CA  1 
ATOM   302  C C   . ASN A 1 42  ? 15.312  -6.538  -14.327 1.00 26.27 ? 40   ASN B C   1 
ATOM   303  O O   . ASN A 1 42  ? 16.300  -7.244  -14.507 1.00 24.15 ? 40   ASN B O   1 
ATOM   304  C CB  . ASN A 1 42  ? 13.242  -7.425  -15.419 1.00 32.78 ? 40   ASN B CB  1 
ATOM   305  C CG  . ASN A 1 42  ? 12.241  -8.553  -15.320 1.00 35.33 ? 40   ASN B CG  1 
ATOM   306  O OD1 . ASN A 1 42  ? 12.516  -9.562  -14.678 1.00 37.29 ? 40   ASN B OD1 1 
ATOM   307  N ND2 . ASN A 1 42  ? 11.058  -8.366  -15.880 1.00 38.29 ? 40   ASN B ND2 1 
ATOM   308  N N   . ALA A 1 43  ? 15.370  -5.203  -14.306 1.00 23.98 ? 41   ALA B N   1 
ATOM   309  C CA  . ALA A 1 43  ? 16.649  -4.473  -14.498 1.00 24.86 ? 41   ALA B CA  1 
ATOM   310  C C   . ALA A 1 43  ? 17.593  -4.779  -13.331 1.00 21.91 ? 41   ALA B C   1 
ATOM   311  O O   . ALA A 1 43  ? 18.780  -4.984  -13.568 1.00 22.23 ? 41   ALA B O   1 
ATOM   312  C CB  . ALA A 1 43  ? 16.415  -2.992  -14.610 1.00 24.43 ? 41   ALA B CB  1 
ATOM   313  N N   . ILE A 1 44  ? 17.079  -4.734  -12.106 1.00 20.62 ? 42   ILE B N   1 
ATOM   314  C CA  . ILE A 1 44  ? 17.849  -5.062  -10.870 1.00 20.90 ? 42   ILE B CA  1 
ATOM   315  C C   . ILE A 1 44  ? 18.381  -6.503  -10.971 1.00 21.44 ? 42   ILE B C   1 
ATOM   316  O O   . ILE A 1 44  ? 19.587  -6.705  -10.775 1.00 21.80 ? 42   ILE B O   1 
ATOM   317  C CB  . ILE A 1 44  ? 16.999  -4.823  -9.623  1.00 22.21 ? 42   ILE B CB  1 
ATOM   318  C CG1 . ILE A 1 44  ? 16.646  -3.336  -9.485  1.00 25.54 ? 42   ILE B CG1 1 
ATOM   319  C CG2 . ILE A 1 44  ? 17.756  -5.308  -8.386  1.00 22.84 ? 42   ILE B CG2 1 
ATOM   320  C CD1 . ILE A 1 44  ? 15.719  -3.018  -8.333  1.00 25.48 ? 42   ILE B CD1 1 
ATOM   321  N N   . LEU A 1 45  ? 17.537  -7.467  -11.330 1.00 22.28 ? 43   LEU B N   1 
ATOM   322  C CA  . LEU A 1 45  ? 18.030  -8.876  -11.469 1.00 21.91 ? 43   LEU B CA  1 
ATOM   323  C C   . LEU A 1 45  ? 19.157  -8.949  -12.509 1.00 21.27 ? 43   LEU B C   1 
ATOM   324  O O   . LEU A 1 45  ? 20.191  -9.636  -12.270 1.00 19.68 ? 43   LEU B O   1 
ATOM   325  C CB  . LEU A 1 45  ? 16.879  -9.788  -11.869 1.00 25.08 ? 43   LEU B CB  1 
ATOM   326  C CG  . LEU A 1 45  ? 15.808  -9.960  -10.806 1.00 27.98 ? 43   LEU B CG  1 
ATOM   327  C CD1 . LEU A 1 45  ? 14.641  -10.708 -11.386 1.00 28.65 ? 43   LEU B CD1 1 
ATOM   328  C CD2 . LEU A 1 45  ? 16.376  -10.660 -9.583  1.00 28.39 ? 43   LEU B CD2 1 
ATOM   329  N N   . GLU A 1 46  ? 18.966  -8.313  -13.671 1.00 21.46 ? 44   GLU B N   1 
ATOM   330  C CA  . GLU A 1 46  ? 19.968  -8.333  -14.769 1.00 25.33 ? 44   GLU B CA  1 
ATOM   331  C C   . GLU A 1 46  ? 21.270  -7.705  -14.284 1.00 21.03 ? 44   GLU B C   1 
ATOM   332  O O   . GLU A 1 46  ? 22.343  -8.232  -14.607 1.00 22.21 ? 44   GLU B O   1 
ATOM   333  C CB  . GLU A 1 46  ? 19.420  -7.618  -16.013 1.00 28.58 ? 44   GLU B CB  1 
ATOM   334  C CG  . GLU A 1 46  ? 18.527  -8.528  -16.841 1.00 35.45 ? 44   GLU B CG  1 
ATOM   335  C CD  . GLU A 1 46  ? 17.622  -7.818  -17.828 1.00 41.57 ? 44   GLU B CD  1 
ATOM   336  O OE1 . GLU A 1 46  ? 16.700  -8.477  -18.370 1.00 48.41 ? 44   GLU B OE1 1 
ATOM   337  O OE2 . GLU A 1 46  ? 17.841  -6.615  -18.044 1.00 44.68 ? 44   GLU B OE2 1 
ATOM   338  N N   . GLU A 1 47  ? 21.215  -6.588  -13.555 1.00 22.08 ? 45   GLU B N   1 
ATOM   339  C CA  . GLU A 1 47  ? 22.459  -5.938  -13.077 1.00 23.20 ? 45   GLU B CA  1 
ATOM   340  C C   . GLU A 1 47  ? 23.130  -6.854  -12.039 1.00 20.19 ? 45   GLU B C   1 
ATOM   341  O O   . GLU A 1 47  ? 24.366  -6.914  -12.015 1.00 20.77 ? 45   GLU B O   1 
ATOM   342  C CB  . GLU A 1 47  ? 22.170  -4.566  -12.489 1.00 25.49 ? 45   GLU B CB  1 
ATOM   343  C CG  . GLU A 1 47  ? 21.684  -3.559  -13.515 1.00 30.42 ? 45   GLU B CG  1 
ATOM   344  C CD  . GLU A 1 47  ? 21.202  -2.226  -12.940 1.00 40.72 ? 45   GLU B CD  1 
ATOM   345  O OE1 . GLU A 1 47  ? 20.515  -1.463  -13.683 1.00 47.59 ? 45   GLU B OE1 1 
ATOM   346  O OE2 . GLU A 1 47  ? 21.514  -1.932  -11.759 1.00 43.89 ? 45   GLU B OE2 1 
ATOM   347  N N   . GLY A 1 48  ? 22.317  -7.537  -11.229 1.00 19.42 ? 46   GLY B N   1 
ATOM   348  C CA  . GLY A 1 48  ? 22.789  -8.491  -10.215 1.00 20.65 ? 46   GLY B CA  1 
ATOM   349  C C   . GLY A 1 48  ? 23.533  -9.631  -10.873 1.00 18.62 ? 46   GLY B C   1 
ATOM   350  O O   . GLY A 1 48  ? 24.687  -9.923  -10.489 1.00 21.05 ? 46   GLY B O   1 
ATOM   351  N N   . ALA A 1 49  ? 22.910  -10.214 -11.896 1.00 18.67 ? 47   ALA B N   1 
ATOM   352  C CA  . ALA A 1 49  ? 23.485  -11.312 -12.686 1.00 19.50 ? 47   ALA B CA  1 
ATOM   353  C C   . ALA A 1 49  ? 24.830  -10.846 -13.245 1.00 20.50 ? 47   ALA B C   1 
ATOM   354  O O   . ALA A 1 49  ? 25.788  -11.572 -13.182 1.00 19.96 ? 47   ALA B O   1 
ATOM   355  C CB  . ALA A 1 49  ? 22.529  -11.767 -13.755 1.00 20.48 ? 47   ALA B CB  1 
ATOM   356  N N   . LYS A 1 50  ? 24.929  -9.633  -13.773 1.00 21.52 ? 48   LYS B N   1 
ATOM   357  C CA  . LYS A 1 50  ? 26.213  -9.240  -14.407 1.00 24.68 ? 48   LYS B CA  1 
ATOM   358  C C   . LYS A 1 50  ? 27.325  -9.140  -13.354 1.00 20.81 ? 48   LYS B C   1 
ATOM   359  O O   . LYS A 1 50  ? 28.425  -9.576  -13.622 1.00 21.49 ? 48   LYS B O   1 
ATOM   360  C CB  . LYS A 1 50  ? 26.057  -7.929  -15.181 1.00 30.71 ? 48   LYS B CB  1 
ATOM   361  C CG  . LYS A 1 50  ? 25.007  -7.960  -16.278 1.00 39.22 ? 48   LYS B CG  1 
ATOM   362  C CD  . LYS A 1 50  ? 24.921  -9.285  -16.997 1.00 46.20 ? 48   LYS B CD  1 
ATOM   363  C CE  . LYS A 1 50  ? 23.751  -9.361  -17.955 1.00 49.93 ? 48   LYS B CE  1 
ATOM   364  N NZ  . LYS A 1 50  ? 22.588  -10.069 -17.367 1.00 51.40 ? 48   LYS B NZ  1 
ATOM   365  N N   . PHE A 1 51  ? 27.016  -8.541  -12.214 1.00 19.83 ? 49   PHE B N   1 
ATOM   366  C CA  . PHE A 1 51  ? 28.013  -8.451  -11.121 1.00 19.62 ? 49   PHE B CA  1 
ATOM   367  C C   . PHE A 1 51  ? 28.496  -9.861  -10.769 1.00 19.40 ? 49   PHE B C   1 
ATOM   368  O O   . PHE A 1 51  ? 29.686  -10.092 -10.643 1.00 19.12 ? 49   PHE B O   1 
ATOM   369  C CB  . PHE A 1 51  ? 27.419  -7.788  -9.880  1.00 20.70 ? 49   PHE B CB  1 
ATOM   370  C CG  . PHE A 1 51  ? 28.392  -7.736  -8.731  1.00 21.42 ? 49   PHE B CG  1 
ATOM   371  C CD1 . PHE A 1 51  ? 29.339  -6.728  -8.648  1.00 22.83 ? 49   PHE B CD1 1 
ATOM   372  C CD2 . PHE A 1 51  ? 28.398  -8.723  -7.760  1.00 22.17 ? 49   PHE B CD2 1 
ATOM   373  C CE1 . PHE A 1 51  ? 30.249  -6.693  -7.603  1.00 22.77 ? 49   PHE B CE1 1 
ATOM   374  C CE2 . PHE A 1 51  ? 29.312  -8.690  -6.719  1.00 22.23 ? 49   PHE B CE2 1 
ATOM   375  C CZ  . PHE A 1 51  ? 30.234  -7.674  -6.641  1.00 24.14 ? 49   PHE B CZ  1 
ATOM   376  N N   . CYS A 1 52  ? 27.533  -10.764 -10.623 1.00 18.52 ? 50   CYS B N   1 
ATOM   377  C CA  . CYS A 1 52  ? 27.901  -12.136 -10.219 1.00 17.08 ? 50   CYS B CA  1 
ATOM   378  C C   . CYS A 1 52  ? 28.752  -12.798 -11.289 1.00 18.33 ? 50   CYS B C   1 
ATOM   379  O O   . CYS A 1 52  ? 29.818  -13.396 -10.927 1.00 17.71 ? 50   CYS B O   1 
ATOM   380  C CB  . CYS A 1 52  ? 26.634  -12.925 -9.881  1.00 17.71 ? 50   CYS B CB  1 
ATOM   381  S SG  . CYS A 1 52  ? 25.822  -12.332 -8.381  1.00 18.87 ? 50   CYS B SG  1 
ATOM   382  N N   . GLU A 1 53  ? 28.322  -12.744 -12.551 1.00 16.73 ? 51   GLU B N   1 
ATOM   383  C CA  . GLU A 1 53  ? 29.024  -13.408 -13.664 1.00 18.18 ? 51   GLU B CA  1 
ATOM   384  C C   . GLU A 1 53  ? 30.391  -12.785 -13.913 1.00 18.45 ? 51   GLU B C   1 
ATOM   385  O O   . GLU A 1 53  ? 31.329  -13.533 -14.222 1.00 20.04 ? 51   GLU B O   1 
ATOM   386  C CB  . GLU A 1 53  ? 28.175  -13.381 -14.936 1.00 20.18 ? 51   GLU B CB  1 
ATOM   387  C CG  . GLU A 1 53  ? 26.908  -14.185 -14.803 1.00 20.46 ? 51   GLU B CG  1 
ATOM   388  C CD  . GLU A 1 53  ? 25.899  -14.025 -15.920 1.00 23.94 ? 51   GLU B CD  1 
ATOM   389  O OE1 . GLU A 1 53  ? 24.815  -14.638 -15.843 1.00 21.36 ? 51   GLU B OE1 1 
ATOM   390  O OE2 . GLU A 1 53  ? 26.175  -13.236 -16.840 1.00 26.93 ? 51   GLU B OE2 1 
ATOM   391  N N   . GLN A 1 54  ? 30.511  -11.466 -13.821 1.00 20.90 ? 52   GLN B N   1 
ATOM   392  C CA  . GLN A 1 54  ? 31.716  -10.754 -14.328 1.00 21.94 ? 52   GLN B CA  1 
ATOM   393  C C   . GLN A 1 54  ? 32.725  -10.462 -13.217 1.00 21.54 ? 52   GLN B C   1 
ATOM   394  O O   . GLN A 1 54  ? 33.909  -10.372 -13.504 1.00 23.77 ? 52   GLN B O   1 
ATOM   395  C CB  . GLN A 1 54  ? 31.261  -9.483  -15.028 1.00 23.78 ? 52   GLN B CB  1 
ATOM   396  C CG  . GLN A 1 54  ? 30.398  -9.848  -16.207 1.00 27.47 ? 52   GLN B CG  1 
ATOM   397  C CD  . GLN A 1 54  ? 30.043  -8.692  -17.093 1.00 37.17 ? 52   GLN B CD  1 
ATOM   398  O OE1 . GLN A 1 54  ? 30.364  -7.542  -16.810 1.00 47.20 ? 52   GLN B OE1 1 
ATOM   399  N NE2 . GLN A 1 54  ? 29.364  -9.009  -18.181 1.00 41.27 ? 52   GLN B NE2 1 
ATOM   400  N N   . VAL A 1 55  ? 32.250  -10.241 -12.001 1.00 21.13 ? 53   VAL B N   1 
ATOM   401  C CA  . VAL A 1 55  ? 33.162  -9.749  -10.929 1.00 21.22 ? 53   VAL B CA  1 
ATOM   402  C C   . VAL A 1 55  ? 33.501  -10.838 -9.916  1.00 20.08 ? 53   VAL B C   1 
ATOM   403  O O   . VAL A 1 55  ? 34.680  -11.056 -9.682  1.00 20.80 ? 53   VAL B O   1 
ATOM   404  C CB  . VAL A 1 55  ? 32.545  -8.522  -10.225 1.00 23.54 ? 53   VAL B CB  1 
ATOM   405  C CG1 . VAL A 1 55  ? 33.440  -7.975  -9.130  1.00 23.18 ? 53   VAL B CG1 1 
ATOM   406  C CG2 . VAL A 1 55  ? 32.161  -7.437  -11.215 1.00 24.24 ? 53   VAL B CG2 1 
ATOM   407  N N   . ILE A 1 56  ? 32.486  -11.508 -9.363  1.00 19.03 ? 54   ILE B N   1 
ATOM   408  C CA  . ILE A 1 56  ? 32.828  -12.449 -8.256  1.00 17.57 ? 54   ILE B CA  1 
ATOM   409  C C   . ILE A 1 56  ? 32.958  -13.902 -8.756  1.00 17.35 ? 54   ILE B C   1 
ATOM   410  O O   . ILE A 1 56  ? 33.757  -14.626 -8.142  1.00 16.57 ? 54   ILE B O   1 
ATOM   411  C CB  . ILE A 1 56  ? 31.889  -12.318 -7.044  1.00 17.48 ? 54   ILE B CB  1 
ATOM   412  C CG1 . ILE A 1 56  ? 30.427  -12.424 -7.444  1.00 16.28 ? 54   ILE B CG1 1 
ATOM   413  C CG2 . ILE A 1 56  ? 32.169  -11.021 -6.288  1.00 16.64 ? 54   ILE B CG2 1 
ATOM   414  C CD1 . ILE A 1 56  ? 29.517  -12.658 -6.281  1.00 17.79 ? 54   ILE B CD1 1 
ATOM   415  N N   . ALA A 1 57  ? 32.268  -14.355 -9.804  1.00 16.91 ? 55   ALA B N   1 
ATOM   416  C CA  . ALA A 1 57  ? 32.396  -15.764 -10.246 1.00 17.27 ? 55   ALA B CA  1 
ATOM   417  C C   . ALA A 1 57  ? 33.846  -16.034 -10.675 1.00 19.13 ? 55   ALA B C   1 
ATOM   418  O O   . ALA A 1 57  ? 34.431  -17.051 -10.295 1.00 18.24 ? 55   ALA B O   1 
ATOM   419  C CB  . ALA A 1 57  ? 31.389  -16.119 -11.319 1.00 17.84 ? 55   ALA B CB  1 
ATOM   420  N N   . PRO A 1 58  ? 34.551  -15.117 -11.386 1.00 17.74 ? 56   PRO B N   1 
ATOM   421  C CA  . PRO A 1 58  ? 35.951  -15.367 -11.730 1.00 19.34 ? 56   PRO B CA  1 
ATOM   422  C C   . PRO A 1 58  ? 36.927  -15.450 -10.544 1.00 18.38 ? 56   PRO B C   1 
ATOM   423  O O   . PRO A 1 58  ? 38.037  -15.939 -10.736 1.00 24.36 ? 56   PRO B O   1 
ATOM   424  C CB  . PRO A 1 58  ? 36.311  -14.211 -12.696 1.00 19.57 ? 56   PRO B CB  1 
ATOM   425  C CG  . PRO A 1 58  ? 34.978  -13.723 -13.198 1.00 19.97 ? 56   PRO B CG  1 
ATOM   426  C CD  . PRO A 1 58  ? 34.023  -13.895 -12.018 1.00 19.76 ? 56   PRO B CD  1 
ATOM   427  N N   . LEU A 1 59  ? 36.514  -15.030 -9.357  1.00 17.27 ? 57   LEU B N   1 
ATOM   428  C CA  . LEU A 1 59  ? 37.302  -15.074 -8.108  1.00 17.27 ? 57   LEU B CA  1 
ATOM   429  C C   . LEU A 1 59  ? 37.044  -16.362 -7.299  1.00 17.99 ? 57   LEU B C   1 
ATOM   430  O O   . LEU A 1 59  ? 37.684  -16.527 -6.253  1.00 17.93 ? 57   LEU B O   1 
ATOM   431  C CB  . LEU A 1 59  ? 36.947  -13.834 -7.300  1.00 17.60 ? 57   LEU B CB  1 
ATOM   432  C CG  . LEU A 1 59  ? 37.303  -12.498 -7.961  1.00 18.79 ? 57   LEU B CG  1 
ATOM   433  C CD1 . LEU A 1 59  ? 36.990  -11.338 -7.039  1.00 20.31 ? 57   LEU B CD1 1 
ATOM   434  C CD2 . LEU A 1 59  ? 38.752  -12.469 -8.378  1.00 19.37 ? 57   LEU B CD2 1 
ATOM   435  N N   . ASN A 1 60  ? 36.135  -17.233 -7.724  1.00 17.86 ? 58   ASN B N   1 
ATOM   436  C CA  . ASN A 1 60  ? 35.781  -18.410 -6.878  1.00 16.87 ? 58   ASN B CA  1 
ATOM   437  C C   . ASN A 1 60  ? 36.983  -19.360 -6.716  1.00 17.32 ? 58   ASN B C   1 
ATOM   438  O O   . ASN A 1 60  ? 37.289  -19.727 -5.589  1.00 16.30 ? 58   ASN B O   1 
ATOM   439  C CB  . ASN A 1 60  ? 34.508  -19.104 -7.381  1.00 16.68 ? 58   ASN B CB  1 
ATOM   440  C CG  . ASN A 1 60  ? 33.860  -19.979 -6.330  1.00 18.58 ? 58   ASN B CG  1 
ATOM   441  O OD1 . ASN A 1 60  ? 34.005  -19.742 -5.140  1.00 18.39 ? 58   ASN B OD1 1 
ATOM   442  N ND2 . ASN A 1 60  ? 33.141  -20.999 -6.760  1.00 24.71 ? 58   ASN B ND2 1 
ATOM   443  N N   . ARG A 1 61  ? 37.627  -19.721 -7.823  1.00 17.60 ? 59   ARG B N   1 
ATOM   444  C CA  . ARG A 1 61  ? 38.812  -20.615 -7.746  1.00 18.88 ? 59   ARG B CA  1 
ATOM   445  C C   . ARG A 1 61  ? 39.948  -19.916 -6.989  1.00 19.05 ? 59   ARG B C   1 
ATOM   446  O O   . ARG A 1 61  ? 40.569  -20.569 -6.176  1.00 18.07 ? 59   ARG B O   1 
ATOM   447  C CB  . ARG A 1 61  ? 39.263  -21.033 -9.149  1.00 20.97 ? 59   ARG B CB  1 
ATOM   448  C CG  . ARG A 1 61  ? 38.394  -22.086 -9.822  1.00 25.81 ? 59   ARG B CG  1 
ATOM   449  C CD  . ARG A 1 61  ? 39.025  -23.466 -9.774  1.00 31.04 ? 59   ARG B CD  1 
ATOM   450  N NE  . ARG A 1 61  ? 38.858  -23.950 -8.422  1.00 32.36 ? 59   ARG B NE  1 
ATOM   451  C CZ  . ARG A 1 61  ? 39.783  -24.539 -7.680  1.00 27.90 ? 59   ARG B CZ  1 
ATOM   452  N NH1 . ARG A 1 61  ? 39.477  -24.895 -6.449  1.00 26.18 ? 59   ARG B NH1 1 
ATOM   453  N NH2 . ARG A 1 61  ? 40.988  -24.783 -8.156  1.00 28.17 ? 59   ARG B NH2 1 
ATOM   454  N N   . VAL A 1 62  ? 40.188  -18.632 -7.288  1.00 20.67 ? 60   VAL B N   1 
ATOM   455  C CA  . VAL A 1 62  ? 41.247  -17.842 -6.579  1.00 21.00 ? 60   VAL B CA  1 
ATOM   456  C C   . VAL A 1 62  ? 41.014  -17.941 -5.064  1.00 19.27 ? 60   VAL B C   1 
ATOM   457  O O   . VAL A 1 62  ? 41.996  -18.141 -4.273  1.00 17.79 ? 60   VAL B O   1 
ATOM   458  C CB  . VAL A 1 62  ? 41.215  -16.355 -7.033  1.00 24.54 ? 60   VAL B CB  1 
ATOM   459  C CG1 . VAL A 1 62  ? 42.179  -15.483 -6.258  1.00 30.99 ? 60   VAL B CG1 1 
ATOM   460  C CG2 . VAL A 1 62  ? 41.466  -16.203 -8.518  1.00 28.89 ? 60   VAL B CG2 1 
ATOM   461  N N   . GLY A 1 63  ? 39.762  -17.785 -4.623  1.00 18.30 ? 61   GLY B N   1 
ATOM   462  C CA  . GLY A 1 63  ? 39.429  -17.835 -3.186  1.00 17.79 ? 61   GLY B CA  1 
ATOM   463  C C   . GLY A 1 63  ? 39.825  -19.166 -2.572  1.00 18.59 ? 61   GLY B C   1 
ATOM   464  O O   . GLY A 1 63  ? 40.365  -19.197 -1.447  1.00 18.18 ? 61   GLY B O   1 
ATOM   465  N N   . ASP A 1 64  ? 39.552  -20.263 -3.279  1.00 16.25 ? 62   ASP B N   1 
ATOM   466  C CA  . ASP A 1 64  ? 39.861  -21.621 -2.791  1.00 16.01 ? 62   ASP B CA  1 
ATOM   467  C C   . ASP A 1 64  ? 41.373  -21.857 -2.786  1.00 16.35 ? 62   ASP B C   1 
ATOM   468  O O   . ASP A 1 64  ? 41.865  -22.499 -1.849  1.00 18.24 ? 62   ASP B O   1 
ATOM   469  C CB  . ASP A 1 64  ? 39.189  -22.647 -3.697  1.00 15.63 ? 62   ASP B CB  1 
ATOM   470  C CG  . ASP A 1 64  ? 39.459  -24.045 -3.207  1.00 16.31 ? 62   ASP B CG  1 
ATOM   471  O OD1 . ASP A 1 64  ? 39.002  -24.353 -2.098  1.00 18.11 ? 62   ASP B OD1 1 
ATOM   472  O OD2 . ASP A 1 64  ? 40.067  -24.810 -3.971  1.00 17.01 ? 62   ASP B OD2 1 
ATOM   473  N N   . LEU A 1 65  ? 42.065  -21.407 -3.840  1.00 17.27 ? 63   LEU B N   1 
ATOM   474  C CA  . LEU A 1 65  ? 43.520  -21.679 -4.020  1.00 19.12 ? 63   LEU B CA  1 
ATOM   475  C C   . LEU A 1 65  ? 44.331  -20.865 -3.012  1.00 19.65 ? 63   LEU B C   1 
ATOM   476  O O   . LEU A 1 65  ? 45.223  -21.431 -2.383  1.00 20.63 ? 63   LEU B O   1 
ATOM   477  C CB  . LEU A 1 65  ? 43.923  -21.343 -5.452  1.00 20.55 ? 63   LEU B CB  1 
ATOM   478  C CG  . LEU A 1 65  ? 43.441  -22.348 -6.507  1.00 24.05 ? 63   LEU B CG  1 
ATOM   479  C CD1 . LEU A 1 65  ? 43.585  -21.799 -7.920  1.00 26.77 ? 63   LEU B CD1 1 
ATOM   480  C CD2 . LEU A 1 65  ? 44.165  -23.693 -6.384  1.00 26.76 ? 63   LEU B CD2 1 
ATOM   481  N N   . GLU A 1 66  ? 44.019  -19.581 -2.841  1.00 19.55 ? 64   GLU B N   1 
ATOM   482  C CA  . GLU A 1 66  ? 44.830  -18.703 -1.954  1.00 20.12 ? 64   GLU B CA  1 
ATOM   483  C C   . GLU A 1 66  ? 44.354  -18.763 -0.504  1.00 20.96 ? 64   GLU B C   1 
ATOM   484  O O   . GLU A 1 66  ? 45.197  -18.763 0.387   1.00 21.93 ? 64   GLU B O   1 
ATOM   485  C CB  . GLU A 1 66  ? 44.705  -17.242 -2.405  1.00 20.65 ? 64   GLU B CB  1 
ATOM   486  C CG  . GLU A 1 66  ? 45.218  -16.954 -3.797  1.00 22.65 ? 64   GLU B CG  1 
ATOM   487  C CD  . GLU A 1 66  ? 45.353  -15.467 -4.084  1.00 24.43 ? 64   GLU B CD  1 
ATOM   488  O OE1 . GLU A 1 66  ? 45.868  -15.123 -5.157  1.00 28.27 ? 64   GLU B OE1 1 
ATOM   489  O OE2 . GLU A 1 66  ? 44.950  -14.664 -3.228  1.00 24.44 ? 64   GLU B OE2 1 
ATOM   490  N N   . GLY A 1 67  ? 43.049  -18.849 -0.292  1.00 19.77 ? 65   GLY B N   1 
ATOM   491  C CA  . GLY A 1 67  ? 42.515  -18.721 1.060   1.00 20.17 ? 65   GLY B CA  1 
ATOM   492  C C   . GLY A 1 67  ? 42.875  -17.371 1.649   1.00 20.63 ? 65   GLY B C   1 
ATOM   493  O O   . GLY A 1 67  ? 43.307  -16.459 0.909   1.00 20.29 ? 65   GLY B O   1 
ATOM   494  N N   . CYS A 1 68  ? 42.692  -17.256 2.956   1.00 20.82 ? 66   CYS B N   1 
ATOM   495  C CA  . CYS A 1 68  ? 42.997  -16.029 3.729   1.00 20.35 ? 66   CYS B CA  1 
ATOM   496  C C   . CYS A 1 68  ? 44.365  -16.198 4.408   1.00 22.36 ? 66   CYS B C   1 
ATOM   497  O O   . CYS A 1 68  ? 44.825  -17.347 4.578   1.00 22.74 ? 66   CYS B O   1 
ATOM   498  C CB  . CYS A 1 68  ? 41.882  -15.759 4.731   1.00 20.21 ? 66   CYS B CB  1 
ATOM   499  S SG  . CYS A 1 68  ? 40.320  -15.362 3.903   1.00 19.17 ? 66   CYS B SG  1 
ATOM   500  N N   . THR A 1 69  ? 45.016  -15.090 4.745   1.00 22.70 ? 67   THR B N   1 
ATOM   501  C CA  . THR A 1 69  ? 46.383  -15.084 5.341   1.00 21.94 ? 67   THR B CA  1 
ATOM   502  C C   . THR A 1 69  ? 46.342  -14.290 6.646   1.00 21.79 ? 67   THR B C   1 
ATOM   503  O O   . THR A 1 69  ? 46.064  -13.098 6.620   1.00 22.20 ? 67   THR B O   1 
ATOM   504  C CB  . THR A 1 69  ? 47.412  -14.527 4.365   1.00 24.61 ? 67   THR B CB  1 
ATOM   505  O OG1 . THR A 1 69  ? 47.399  -15.346 3.200   1.00 25.75 ? 67   THR B OG1 1 
ATOM   506  C CG2 . THR A 1 69  ? 48.821  -14.544 4.933   1.00 28.21 ? 67   THR B CG2 1 
ATOM   507  N N   . TRP A 1 70  ? 46.571  -14.972 7.759   1.00 22.48 ? 68   TRP B N   1 
ATOM   508  C CA  . TRP A 1 70  ? 46.614  -14.339 9.095   1.00 24.89 ? 68   TRP B CA  1 
ATOM   509  C C   . TRP A 1 70  ? 47.961  -13.626 9.308   1.00 28.02 ? 68   TRP B C   1 
ATOM   510  O O   . TRP A 1 70  ? 49.016  -14.162 8.902   1.00 25.59 ? 68   TRP B O   1 
ATOM   511  C CB  . TRP A 1 70  ? 46.407  -15.402 10.165  1.00 25.17 ? 68   TRP B CB  1 
ATOM   512  C CG  . TRP A 1 70  ? 46.375  -14.851 11.548  1.00 28.21 ? 68   TRP B CG  1 
ATOM   513  C CD1 . TRP A 1 70  ? 45.276  -14.439 12.242  1.00 27.65 ? 68   TRP B CD1 1 
ATOM   514  C CD2 . TRP A 1 70  ? 47.495  -14.692 12.432  1.00 30.48 ? 68   TRP B CD2 1 
ATOM   515  N NE1 . TRP A 1 70  ? 45.637  -14.014 13.489  1.00 30.99 ? 68   TRP B NE1 1 
ATOM   516  C CE2 . TRP A 1 70  ? 46.992  -14.158 13.635  1.00 29.22 ? 68   TRP B CE2 1 
ATOM   517  C CE3 . TRP A 1 70  ? 48.868  -14.922 12.309  1.00 31.81 ? 68   TRP B CE3 1 
ATOM   518  C CZ2 . TRP A 1 70  ? 47.821  -13.860 14.717  1.00 34.39 ? 68   TRP B CZ2 1 
ATOM   519  C CZ3 . TRP A 1 70  ? 49.681  -14.644 13.381  1.00 34.98 ? 68   TRP B CZ3 1 
ATOM   520  C CH2 . TRP A 1 70  ? 49.162  -14.127 14.572  1.00 38.09 ? 68   TRP B CH2 1 
ATOM   521  N N   . SER A 1 71  ? 47.898  -12.460 9.932   1.00 27.85 ? 69   SER B N   1 
ATOM   522  C CA  . SER A 1 71  ? 49.017  -11.821 10.678  1.00 31.95 ? 69   SER B CA  1 
ATOM   523  C C   . SER A 1 71  ? 48.451  -11.251 11.994  1.00 34.75 ? 69   SER B C   1 
ATOM   524  O O   . SER A 1 71  ? 47.231  -11.123 12.105  1.00 36.08 ? 69   SER B O   1 
ATOM   525  C CB  . SER A 1 71  ? 49.711  -10.815 9.798   1.00 30.84 ? 69   SER B CB  1 
ATOM   526  O OG  . SER A 1 71  ? 48.872  -9.739  9.419   1.00 37.52 ? 69   SER B OG  1 
ATOM   527  N N   . ALA A 1 72  ? 49.253  -10.994 13.032  1.00 39.76 ? 70   ALA B N   1 
ATOM   528  C CA  . ALA A 1 72  ? 48.705  -10.429 14.292  1.00 40.73 ? 70   ALA B CA  1 
ATOM   529  C C   . ALA A 1 72  ? 47.950  -9.121  13.987  1.00 42.55 ? 70   ALA B C   1 
ATOM   530  O O   . ALA A 1 72  ? 46.890  -8.881  14.595  1.00 49.25 ? 70   ALA B O   1 
ATOM   531  C CB  . ALA A 1 72  ? 49.811  -10.235 15.293  1.00 47.17 ? 70   ALA B CB  1 
ATOM   532  N N   . ASP A 1 73  ? 48.512  -8.339  13.063  1.00 40.13 ? 71   ASP B N   1 
ATOM   533  C CA  . ASP A 1 73  ? 48.007  -7.121  12.365  1.00 43.20 ? 71   ASP B CA  1 
ATOM   534  C C   . ASP A 1 73  ? 46.575  -7.265  11.791  1.00 44.43 ? 71   ASP B C   1 
ATOM   535  O O   . ASP A 1 73  ? 45.853  -6.253  11.742  1.00 43.03 ? 71   ASP B O   1 
ATOM   536  C CB  . ASP A 1 73  ? 48.991  -6.862  11.224  1.00 45.41 ? 71   ASP B CB  1 
ATOM   537  C CG  . ASP A 1 73  ? 48.669  -5.693  10.323  1.00 51.32 ? 71   ASP B CG  1 
ATOM   538  O OD1 . ASP A 1 73  ? 47.748  -5.830  9.491   1.00 61.99 ? 71   ASP B OD1 1 
ATOM   539  O OD2 . ASP A 1 73  ? 49.366  -4.657  10.443  1.00 59.36 ? 71   ASP B OD2 1 
ATOM   540  N N   . GLY A 1 74  ? 46.185  -8.429  11.265  1.00 36.03 ? 72   GLY B N   1 
ATOM   541  C CA  . GLY A 1 74  ? 44.871  -8.578  10.594  1.00 32.17 ? 72   GLY B CA  1 
ATOM   542  C C   . GLY A 1 74  ? 44.845  -9.741  9.613   1.00 26.79 ? 72   GLY B C   1 
ATOM   543  O O   . GLY A 1 74  ? 45.738  -10.564 9.645   1.00 24.15 ? 72   GLY B O   1 
ATOM   544  N N   . VAL A 1 75  ? 43.836  -9.812  8.750   1.00 22.55 ? 73   VAL B N   1 
ATOM   545  C CA  . VAL A 1 75  ? 43.637  -11.019 7.899   1.00 21.48 ? 73   VAL B CA  1 
ATOM   546  C C   . VAL A 1 75  ? 43.481  -10.527 6.460   1.00 20.24 ? 73   VAL B C   1 
ATOM   547  O O   . VAL A 1 75  ? 42.568  -9.707  6.193   1.00 20.53 ? 73   VAL B O   1 
ATOM   548  C CB  . VAL A 1 75  ? 42.428  -11.867 8.359   1.00 21.17 ? 73   VAL B CB  1 
ATOM   549  C CG1 . VAL A 1 75  ? 42.157  -12.995 7.382   1.00 22.75 ? 73   VAL B CG1 1 
ATOM   550  C CG2 . VAL A 1 75  ? 42.549  -12.407 9.776   1.00 21.11 ? 73   VAL B CG2 1 
ATOM   551  N N   . LYS A 1 76  ? 44.316  -11.065 5.578   1.00 19.82 ? 74   LYS B N   1 
ATOM   552  C CA  . LYS A 1 76  ? 44.250  -10.704 4.149   1.00 22.95 ? 74   LYS B CA  1 
ATOM   553  C C   . LYS A 1 76  ? 43.328  -11.665 3.400   1.00 20.19 ? 74   LYS B C   1 
ATOM   554  O O   . LYS A 1 76  ? 43.476  -12.868 3.573   1.00 22.51 ? 74   LYS B O   1 
ATOM   555  C CB  . LYS A 1 76  ? 45.637  -10.743 3.513   1.00 25.93 ? 74   LYS B CB  1 
ATOM   556  C CG  . LYS A 1 76  ? 45.717  -10.012 2.178   1.00 31.38 ? 74   LYS B CG  1 
ATOM   557  C CD  . LYS A 1 76  ? 46.774  -10.538 1.241   1.00 37.11 ? 74   LYS B CD  1 
ATOM   558  C CE  . LYS A 1 76  ? 46.671  -9.954  -0.151  1.00 38.03 ? 74   LYS B CE  1 
ATOM   559  N NZ  . LYS A 1 76  ? 45.409  -10.341 -0.823  1.00 37.81 ? 74   LYS B NZ  1 
ATOM   560  N N   . THR A 1 77  ? 42.434  -11.101 2.598   1.00 20.30 ? 75   THR B N   1 
ATOM   561  C CA  . THR A 1 77  ? 41.491  -11.914 1.799   1.00 19.73 ? 75   THR B CA  1 
ATOM   562  C C   . THR A 1 77  ? 42.147  -12.245 0.454   1.00 20.71 ? 75   THR B C   1 
ATOM   563  O O   . THR A 1 77  ? 43.125  -11.605 0.090   1.00 20.20 ? 75   THR B O   1 
ATOM   564  C CB  . THR A 1 77  ? 40.146  -11.184 1.671   1.00 20.97 ? 75   THR B CB  1 
ATOM   565  O OG1 . THR A 1 77  ? 40.355  -9.886  1.116   1.00 18.63 ? 75   THR B OG1 1 
ATOM   566  C CG2 . THR A 1 77  ? 39.426  -11.080 2.997   1.00 21.28 ? 75   THR B CG2 1 
ATOM   567  N N   . PRO A 1 78  ? 41.616  -13.231 -0.290  1.00 19.53 ? 76   PRO B N   1 
ATOM   568  C CA  . PRO A 1 78  ? 42.159  -13.576 -1.591  1.00 19.35 ? 76   PRO B CA  1 
ATOM   569  C C   . PRO A 1 78  ? 42.197  -12.431 -2.616  1.00 19.13 ? 76   PRO B C   1 
ATOM   570  O O   . PRO A 1 78  ? 41.372  -11.565 -2.559  1.00 19.73 ? 76   PRO B O   1 
ATOM   571  C CB  . PRO A 1 78  ? 41.202  -14.679 -2.086  1.00 19.15 ? 76   PRO B CB  1 
ATOM   572  C CG  . PRO A 1 78  ? 40.636  -15.276 -0.825  1.00 19.11 ? 76   PRO B CG  1 
ATOM   573  C CD  . PRO A 1 78  ? 40.508  -14.100 0.114   1.00 19.31 ? 76   PRO B CD  1 
ATOM   574  N N   . THR A 1 79  ? 43.177  -12.496 -3.505  1.00 19.21 ? 77   THR B N   1 
ATOM   575  C CA  . THR A 1 79  ? 43.332  -11.497 -4.581  1.00 20.90 ? 77   THR B CA  1 
ATOM   576  C C   . THR A 1 79  ? 41.993  -11.185 -5.240  1.00 20.34 ? 77   THR B C   1 
ATOM   577  O O   . THR A 1 79  ? 41.349  -12.115 -5.723  1.00 20.82 ? 77   THR B O   1 
ATOM   578  C CB  . THR A 1 79  ? 44.374  -11.996 -5.591  1.00 22.79 ? 77   THR B CB  1 
ATOM   579  O OG1 . THR A 1 79  ? 45.571  -12.300 -4.880  1.00 23.57 ? 77   THR B OG1 1 
ATOM   580  C CG2 . THR A 1 79  ? 44.642  -10.991 -6.689  1.00 24.10 ? 77   THR B CG2 1 
ATOM   581  N N   . GLY A 1 80  ? 41.603  -9.917  -5.224  1.00 19.55 ? 78   GLY B N   1 
ATOM   582  C CA  . GLY A 1 80  ? 40.388  -9.426  -5.893  1.00 20.89 ? 78   GLY B CA  1 
ATOM   583  C C   . GLY A 1 80  ? 39.175  -9.361  -4.989  1.00 18.87 ? 78   GLY B C   1 
ATOM   584  O O   . GLY A 1 80  ? 38.213  -8.676  -5.376  1.00 19.53 ? 78   GLY B O   1 
ATOM   585  N N   . PHE A 1 81  ? 39.150  -10.069 -3.866  1.00 19.06 ? 79   PHE B N   1 
ATOM   586  C CA  . PHE A 1 81  ? 37.940  -10.110 -3.000  1.00 18.44 ? 79   PHE B CA  1 
ATOM   587  C C   . PHE A 1 81  ? 37.598  -8.689  -2.538  1.00 19.21 ? 79   PHE B C   1 
ATOM   588  O O   . PHE A 1 81  ? 36.420  -8.259  -2.598  1.00 17.93 ? 79   PHE B O   1 
ATOM   589  C CB  . PHE A 1 81  ? 38.139  -11.050 -1.807  1.00 17.42 ? 79   PHE B CB  1 
ATOM   590  C CG  . PHE A 1 81  ? 37.688  -12.486 -1.987  1.00 17.51 ? 79   PHE B CG  1 
ATOM   591  C CD1 . PHE A 1 81  ? 37.888  -13.173 -3.168  1.00 17.38 ? 79   PHE B CD1 1 
ATOM   592  C CD2 . PHE A 1 81  ? 37.048  -13.133 -0.941  1.00 17.52 ? 79   PHE B CD2 1 
ATOM   593  C CE1 . PHE A 1 81  ? 37.503  -14.498 -3.285  1.00 17.64 ? 79   PHE B CE1 1 
ATOM   594  C CE2 . PHE A 1 81  ? 36.645  -14.441 -1.067  1.00 16.42 ? 79   PHE B CE2 1 
ATOM   595  C CZ  . PHE A 1 81  ? 36.888  -15.128 -2.234  1.00 16.76 ? 79   PHE B CZ  1 
ATOM   596  N N   . LYS A 1 82  ? 38.591  -7.946  -2.034  1.00 18.31 ? 80   LYS B N   1 
ATOM   597  C CA  . LYS A 1 82  ? 38.284  -6.631  -1.413  1.00 21.87 ? 80   LYS B CA  1 
ATOM   598  C C   . LYS A 1 82  ? 37.899  -5.593  -2.486  1.00 20.56 ? 80   LYS B C   1 
ATOM   599  O O   . LYS A 1 82  ? 36.990  -4.776  -2.212  1.00 21.50 ? 80   LYS B O   1 
ATOM   600  C CB  . LYS A 1 82  ? 39.434  -6.157  -0.521  1.00 24.56 ? 80   LYS B CB  1 
ATOM   601  C CG  . LYS A 1 82  ? 40.732  -5.795  -1.193  1.00 29.73 ? 80   LYS B CG  1 
ATOM   602  C CD  . LYS A 1 82  ? 41.683  -5.107  -0.190  1.00 36.99 ? 80   LYS B CD  1 
ATOM   603  C CE  . LYS A 1 82  ? 41.192  -3.744  0.246   1.00 44.06 ? 80   LYS B CE  1 
ATOM   604  N NZ  . LYS A 1 82  ? 41.580  -3.421  1.641   1.00 50.26 ? 80   LYS B NZ  1 
ATOM   605  N N   . GLU A 1 83  ? 38.493  -5.689  -3.663  1.00 20.75 ? 81   GLU B N   1 
ATOM   606  C CA  . GLU A 1 83  ? 38.170  -4.843  -4.828  1.00 22.88 ? 81   GLU B CA  1 
ATOM   607  C C   . GLU A 1 83  ? 36.730  -5.128  -5.248  1.00 22.66 ? 81   GLU B C   1 
ATOM   608  O O   . GLU A 1 83  ? 36.009  -4.188  -5.541  1.00 21.36 ? 81   GLU B O   1 
ATOM   609  C CB  . GLU A 1 83  ? 39.149  -5.131  -5.966  1.00 26.44 ? 81   GLU B CB  1 
ATOM   610  C CG  . GLU A 1 83  ? 40.616  -4.822  -5.612  1.00 31.84 ? 81   GLU B CG  1 
ATOM   611  C CD  . GLU A 1 83  ? 41.383  -5.714  -4.615  1.00 37.82 ? 81   GLU B CD  1 
ATOM   612  O OE1 . GLU A 1 83  ? 42.428  -5.224  -4.128  1.00 41.12 ? 81   GLU B OE1 1 
ATOM   613  O OE2 . GLU A 1 83  ? 40.971  -6.902  -4.287  1.00 30.25 ? 81   GLU B OE2 1 
ATOM   614  N N   . ALA A 1 84  ? 36.347  -6.416  -5.316  1.00 21.03 ? 82   ALA B N   1 
ATOM   615  C CA  . ALA A 1 84  ? 34.959  -6.803  -5.642  1.00 19.70 ? 82   ALA B CA  1 
ATOM   616  C C   . ALA A 1 84  ? 33.999  -6.258  -4.590  1.00 17.31 ? 82   ALA B C   1 
ATOM   617  O O   . ALA A 1 84  ? 32.911  -5.828  -4.946  1.00 18.95 ? 82   ALA B O   1 
ATOM   618  C CB  . ALA A 1 84  ? 34.868  -8.315  -5.775  1.00 18.69 ? 82   ALA B CB  1 
ATOM   619  N N   . TYR A 1 85  ? 34.386  -6.256  -3.321  1.00 18.59 ? 83   TYR B N   1 
ATOM   620  C CA  . TYR A 1 85  ? 33.515  -5.729  -2.250  1.00 19.53 ? 83   TYR B CA  1 
ATOM   621  C C   . TYR A 1 85  ? 33.379  -4.194  -2.395  1.00 18.47 ? 83   TYR B C   1 
ATOM   622  O O   . TYR A 1 85  ? 32.250  -3.679  -2.224  1.00 19.51 ? 83   TYR B O   1 
ATOM   623  C CB  . TYR A 1 85  ? 34.015  -6.150  -0.862  1.00 19.91 ? 83   TYR B CB  1 
ATOM   624  C CG  . TYR A 1 85  ? 33.032  -5.731  0.191   1.00 21.10 ? 83   TYR B CG  1 
ATOM   625  C CD1 . TYR A 1 85  ? 31.807  -6.364  0.281   1.00 20.49 ? 83   TYR B CD1 1 
ATOM   626  C CD2 . TYR A 1 85  ? 33.281  -4.673  1.058   1.00 20.90 ? 83   TYR B CD2 1 
ATOM   627  C CE1 . TYR A 1 85  ? 30.837  -5.938  1.166   1.00 21.42 ? 83   TYR B CE1 1 
ATOM   628  C CE2 . TYR A 1 85  ? 32.333  -4.259  1.985   1.00 21.99 ? 83   TYR B CE2 1 
ATOM   629  C CZ  . TYR A 1 85  ? 31.109  -4.902  2.043   1.00 23.13 ? 83   TYR B CZ  1 
ATOM   630  O OH  . TYR A 1 85  ? 30.114  -4.519  2.889   1.00 22.38 ? 83   TYR B OH  1 
ATOM   631  N N   . GLN A 1 86  ? 34.465  -3.519  -2.773  1.00 22.21 ? 84   GLN B N   1 
ATOM   632  C CA  . GLN A 1 86  ? 34.421  -2.062  -3.074  1.00 24.73 ? 84   GLN B CA  1 
ATOM   633  C C   . GLN A 1 86  ? 33.400  -1.820  -4.198  1.00 22.83 ? 84   GLN B C   1 
ATOM   634  O O   . GLN A 1 86  ? 32.574  -0.894  -4.048  1.00 25.33 ? 84   GLN B O   1 
ATOM   635  C CB  . GLN A 1 86  ? 35.805  -1.514  -3.439  1.00 27.19 ? 84   GLN B CB  1 
ATOM   636  C CG  . GLN A 1 86  ? 35.808  0.008   -3.552  1.00 34.78 ? 84   GLN B CG  1 
ATOM   637  C CD  . GLN A 1 86  ? 37.190  0.592   -3.732  1.00 38.54 ? 84   GLN B CD  1 
ATOM   638  O OE1 . GLN A 1 86  ? 37.440  1.749   -3.399  1.00 50.17 ? 84   GLN B OE1 1 
ATOM   639  N NE2 . GLN A 1 86  ? 38.090  -0.182  -4.314  1.00 45.96 ? 84   GLN B NE2 1 
ATOM   640  N N   . GLN A 1 87  ? 33.431  -2.610  -5.271  1.00 22.72 ? 85   GLN B N   1 
ATOM   641  C CA  . GLN A 1 87  ? 32.479  -2.463  -6.408  1.00 24.31 ? 85   GLN B CA  1 
ATOM   642  C C   . GLN A 1 87  ? 31.052  -2.756  -5.945  1.00 24.99 ? 85   GLN B C   1 
ATOM   643  O O   . GLN A 1 87  ? 30.119  -2.013  -6.315  1.00 23.26 ? 85   GLN B O   1 
ATOM   644  C CB  . GLN A 1 87  ? 32.841  -3.351  -7.581  1.00 26.15 ? 85   GLN B CB  1 
ATOM   645  C CG  . GLN A 1 87  ? 34.122  -2.974  -8.301  1.00 31.84 ? 85   GLN B CG  1 
ATOM   646  C CD  . GLN A 1 87  ? 34.346  -3.998  -9.383  1.00 35.17 ? 85   GLN B CD  1 
ATOM   647  O OE1 . GLN A 1 87  ? 33.533  -4.120  -10.296 1.00 40.10 ? 85   GLN B OE1 1 
ATOM   648  N NE2 . GLN A 1 87  ? 35.404  -4.784  -9.254  1.00 37.79 ? 85   GLN B NE2 1 
ATOM   649  N N   . PHE A 1 88  ? 30.865  -3.769  -5.095  1.00 21.00 ? 86   PHE B N   1 
ATOM   650  C CA  . PHE A 1 88  ? 29.527  -4.129  -4.561  1.00 20.73 ? 86   PHE B CA  1 
ATOM   651  C C   . PHE A 1 88  ? 28.942  -2.930  -3.783  1.00 20.57 ? 86   PHE B C   1 
ATOM   652  O O   . PHE A 1 88  ? 27.744  -2.572  -3.927  1.00 22.87 ? 86   PHE B O   1 
ATOM   653  C CB  . PHE A 1 88  ? 29.674  -5.354  -3.657  1.00 20.48 ? 86   PHE B CB  1 
ATOM   654  C CG  . PHE A 1 88  ? 28.405  -6.056  -3.231  1.00 19.67 ? 86   PHE B CG  1 
ATOM   655  C CD1 . PHE A 1 88  ? 27.655  -6.778  -4.136  1.00 20.21 ? 86   PHE B CD1 1 
ATOM   656  C CD2 . PHE A 1 88  ? 28.005  -6.042  -1.907  1.00 19.97 ? 86   PHE B CD2 1 
ATOM   657  C CE1 . PHE A 1 88  ? 26.516  -7.462  -3.725  1.00 19.13 ? 86   PHE B CE1 1 
ATOM   658  C CE2 . PHE A 1 88  ? 26.881  -6.739  -1.501  1.00 20.53 ? 86   PHE B CE2 1 
ATOM   659  C CZ  . PHE A 1 88  ? 26.144  -7.449  -2.410  1.00 21.09 ? 86   PHE B CZ  1 
ATOM   660  N N   . VAL A 1 89  ? 29.775  -2.331  -2.928  1.00 21.58 ? 87   VAL B N   1 
ATOM   661  C CA  . VAL A 1 89  ? 29.368  -1.179  -2.081  1.00 22.28 ? 87   VAL B CA  1 
ATOM   662  C C   . VAL A 1 89  ? 29.088  0.020   -3.007  1.00 23.40 ? 87   VAL B C   1 
ATOM   663  O O   . VAL A 1 89  ? 28.048  0.680   -2.822  1.00 24.01 ? 87   VAL B O   1 
ATOM   664  C CB  . VAL A 1 89  ? 30.435  -0.871  -1.007  1.00 22.95 ? 87   VAL B CB  1 
ATOM   665  C CG1 . VAL A 1 89  ? 30.157  0.476   -0.324  1.00 23.38 ? 87   VAL B CG1 1 
ATOM   666  C CG2 . VAL A 1 89  ? 30.529  -1.992  0.031   1.00 23.60 ? 87   VAL B CG2 1 
ATOM   667  N N   . GLU A 1 90  ? 29.946  0.276   -3.988  1.00 25.10 ? 88   GLU B N   1 
ATOM   668  C CA  . GLU A 1 90  ? 29.781  1.435   -4.920  1.00 28.64 ? 88   GLU B CA  1 
ATOM   669  C C   . GLU A 1 90  ? 28.482  1.272   -5.717  1.00 29.75 ? 88   GLU B C   1 
ATOM   670  O O   . GLU A 1 90  ? 27.892  2.306   -6.086  1.00 29.14 ? 88   GLU B O   1 
ATOM   671  C CB  . GLU A 1 90  ? 30.987  1.581   -5.848  1.00 32.25 ? 88   GLU B CB  1 
ATOM   672  C CG  . GLU A 1 90  ? 32.125  2.329   -5.193  1.00 39.91 ? 88   GLU B CG  1 
ATOM   673  C CD  . GLU A 1 90  ? 33.492  2.307   -5.864  1.00 46.22 ? 88   GLU B CD  1 
ATOM   674  O OE1 . GLU A 1 90  ? 34.477  2.642   -5.163  1.00 51.80 ? 88   GLU B OE1 1 
ATOM   675  O OE2 . GLU A 1 90  ? 33.584  1.937   -7.058  1.00 54.16 ? 88   GLU B OE2 1 
ATOM   676  N N   . GLY A 1 91  ? 28.068  0.036   -6.010  1.00 25.47 ? 89   GLY B N   1 
ATOM   677  C CA  . GLY A 1 91  ? 26.859  -0.281  -6.790  1.00 24.21 ? 89   GLY B CA  1 
ATOM   678  C C   . GLY A 1 91  ? 25.601  -0.209  -5.955  1.00 22.57 ? 89   GLY B C   1 
ATOM   679  O O   . GLY A 1 91  ? 24.503  -0.331  -6.543  1.00 25.83 ? 89   GLY B O   1 
ATOM   680  N N   . GLY A 1 92  ? 25.723  -0.011  -4.637  1.00 21.71 ? 90   GLY B N   1 
ATOM   681  C CA  . GLY A 1 92  ? 24.612  0.192   -3.696  1.00 21.31 ? 90   GLY B CA  1 
ATOM   682  C C   . GLY A 1 92  ? 23.967  -1.104  -3.223  1.00 21.63 ? 90   GLY B C   1 
ATOM   683  O O   . GLY A 1 92  ? 22.935  -1.070  -2.510  1.00 21.19 ? 90   GLY B O   1 
ATOM   684  N N   . TRP A 1 93  ? 24.570  -2.248  -3.533  1.00 20.84 ? 91   TRP B N   1 
ATOM   685  C CA  . TRP A 1 93  ? 23.858  -3.534  -3.317  1.00 19.65 ? 91   TRP B CA  1 
ATOM   686  C C   . TRP A 1 93  ? 23.534  -3.745  -1.843  1.00 19.02 ? 91   TRP B C   1 
ATOM   687  O O   . TRP A 1 93  ? 22.476  -4.279  -1.537  1.00 18.28 ? 91   TRP B O   1 
ATOM   688  C CB  . TRP A 1 93  ? 24.645  -4.701  -3.921  1.00 19.69 ? 91   TRP B CB  1 
ATOM   689  C CG  . TRP A 1 93  ? 24.664  -4.627  -5.420  1.00 18.47 ? 91   TRP B CG  1 
ATOM   690  C CD1 . TRP A 1 93  ? 25.700  -4.240  -6.226  1.00 21.70 ? 91   TRP B CD1 1 
ATOM   691  C CD2 . TRP A 1 93  ? 23.572  -4.921  -6.288  1.00 19.84 ? 91   TRP B CD2 1 
ATOM   692  N NE1 . TRP A 1 93  ? 25.323  -4.286  -7.538  1.00 22.15 ? 91   TRP B NE1 1 
ATOM   693  C CE2 . TRP A 1 93  ? 24.024  -4.702  -7.603  1.00 20.34 ? 91   TRP B CE2 1 
ATOM   694  C CE3 . TRP A 1 93  ? 22.261  -5.353  -6.087  1.00 20.02 ? 91   TRP B CE3 1 
ATOM   695  C CZ2 . TRP A 1 93  ? 23.195  -4.907  -8.700  1.00 20.31 ? 91   TRP B CZ2 1 
ATOM   696  C CZ3 . TRP A 1 93  ? 21.428  -5.519  -7.169  1.00 20.10 ? 91   TRP B CZ3 1 
ATOM   697  C CH2 . TRP A 1 93  ? 21.904  -5.314  -8.457  1.00 19.76 ? 91   TRP B CH2 1 
ATOM   698  N N   . PRO A 1 94  ? 24.437  -3.438  -0.880  1.00 20.46 ? 92   PRO B N   1 
ATOM   699  C CA  . PRO A 1 94  ? 24.137  -3.706  0.523   1.00 20.51 ? 92   PRO B CA  1 
ATOM   700  C C   . PRO A 1 94  ? 22.824  -3.057  0.988   1.00 21.88 ? 92   PRO B C   1 
ATOM   701  O O   . PRO A 1 94  ? 22.158  -3.614  1.870   1.00 20.62 ? 92   PRO B O   1 
ATOM   702  C CB  . PRO A 1 94  ? 25.358  -3.147  1.256   1.00 21.49 ? 92   PRO B CB  1 
ATOM   703  C CG  . PRO A 1 94  ? 26.480  -3.291  0.249   1.00 21.88 ? 92   PRO B CG  1 
ATOM   704  C CD  . PRO A 1 94  ? 25.815  -2.970  -1.075  1.00 21.88 ? 92   PRO B CD  1 
ATOM   705  N N   . SER A 1 95  ? 22.458  -1.906  0.395   1.00 21.21 ? 93   SER B N   1 
ATOM   706  C CA  . SER A 1 95  ? 21.297  -1.109  0.878   1.00 21.62 ? 93   SER B CA  1 
ATOM   707  C C   . SER A 1 95  ? 19.972  -1.532  0.237   1.00 22.63 ? 93   SER B C   1 
ATOM   708  O O   . SER A 1 95  ? 18.897  -1.059  0.704   1.00 22.16 ? 93   SER B O   1 
ATOM   709  C CB  . SER A 1 95  ? 21.575  0.334   0.632   1.00 19.74 ? 93   SER B CB  1 
ATOM   710  O OG  . SER A 1 95  ? 21.670  0.621   -0.744  1.00 21.84 ? 93   SER B OG  1 
ATOM   711  N N   . LEU A 1 96  ? 20.034  -2.406  -0.769  1.00 21.63 ? 94   LEU B N   1 
ATOM   712  C CA  . LEU A 1 96  ? 18.893  -2.739  -1.666  1.00 22.96 ? 94   LEU B CA  1 
ATOM   713  C C   . LEU A 1 96  ? 17.615  -3.018  -0.882  1.00 22.57 ? 94   LEU B C   1 
ATOM   714  O O   . LEU A 1 96  ? 16.586  -2.380  -1.175  1.00 23.09 ? 94   LEU B O   1 
ATOM   715  C CB  . LEU A 1 96  ? 19.244  -3.947  -2.539  1.00 23.30 ? 94   LEU B CB  1 
ATOM   716  C CG  . LEU A 1 96  ? 18.246  -4.243  -3.663  1.00 23.51 ? 94   LEU B CG  1 
ATOM   717  C CD1 . LEU A 1 96  ? 18.326  -3.170  -4.748  1.00 27.22 ? 94   LEU B CD1 1 
ATOM   718  C CD2 . LEU A 1 96  ? 18.524  -5.606  -4.267  1.00 22.87 ? 94   LEU B CD2 1 
ATOM   719  N N   . ALA A 1 97  ? 17.603  -4.000  0.010   1.00 23.41 ? 95   ALA B N   1 
ATOM   720  C CA  . ALA A 1 97  ? 16.375  -4.439  0.694   1.00 22.86 ? 95   ALA B CA  1 
ATOM   721  C C   . ALA A 1 97  ? 16.373  -4.027  2.165   1.00 27.61 ? 95   ALA B C   1 
ATOM   722  O O   . ALA A 1 97  ? 15.963  -4.817  3.000   1.00 31.61 ? 95   ALA B O   1 
ATOM   723  C CB  . ALA A 1 97  ? 16.200  -5.944  0.542   1.00 27.79 ? 95   ALA B CB  1 
ATOM   724  N N   . HIS A 1 98  ? 16.802  -2.809  2.491   1.00 25.69 ? 96   HIS B N   1 
ATOM   725  C CA  . HIS A 1 98  ? 16.789  -2.297  3.886   1.00 23.81 ? 96   HIS B CA  1 
ATOM   726  C C   . HIS A 1 98  ? 15.953  -1.005  3.926   1.00 24.92 ? 96   HIS B C   1 
ATOM   727  O O   . HIS A 1 98  ? 15.719  -0.397  2.854   1.00 22.79 ? 96   HIS B O   1 
ATOM   728  C CB  . HIS A 1 98  ? 18.225  -2.139  4.394   1.00 24.75 ? 96   HIS B CB  1 
ATOM   729  C CG  . HIS A 1 98  ? 18.851  -3.473  4.584   1.00 25.46 ? 96   HIS B CG  1 
ATOM   730  N ND1 . HIS A 1 98  ? 18.466  -4.295  5.600   1.00 27.56 ? 96   HIS B ND1 1 
ATOM   731  C CD2 . HIS A 1 98  ? 19.749  -4.156  3.842   1.00 27.36 ? 96   HIS B CD2 1 
ATOM   732  C CE1 . HIS A 1 98  ? 19.106  -5.454  5.478   1.00 26.66 ? 96   HIS B CE1 1 
ATOM   733  N NE2 . HIS A 1 98  ? 19.902  -5.387  4.419   1.00 26.87 ? 96   HIS B NE2 1 
ATOM   734  N N   . ASP A 1 99  ? 15.470  -0.666  5.114   1.00 25.83 ? 97   ASP B N   1 
ATOM   735  C CA  . ASP A 1 99  ? 14.583  0.506   5.360   1.00 27.26 ? 97   ASP B CA  1 
ATOM   736  C C   . ASP A 1 99  ? 15.225  1.808   4.882   1.00 25.95 ? 97   ASP B C   1 
ATOM   737  O O   . ASP A 1 99  ? 16.332  2.120   5.303   1.00 23.92 ? 97   ASP B O   1 
ATOM   738  C CB  . ASP A 1 99  ? 14.294  0.709   6.844   1.00 30.67 ? 97   ASP B CB  1 
ATOM   739  C CG  . ASP A 1 99  ? 13.135  -0.108  7.332   1.00 37.90 ? 97   ASP B CG  1 
ATOM   740  O OD1 . ASP A 1 99  ? 12.679  -0.972  6.558   1.00 44.28 ? 97   ASP B OD1 1 
ATOM   741  O OD2 . ASP A 1 99  ? 12.687  0.154   8.456   1.00 43.35 ? 97   ASP B OD2 1 
ATOM   742  N N   . VAL A 1 100 ? 14.460  2.593   4.124   1.00 27.46 ? 98   VAL B N   1 
ATOM   743  C CA  . VAL A 1 100 ? 14.783  3.987   3.714   1.00 27.22 ? 98   VAL B CA  1 
ATOM   744  C C   . VAL A 1 100 ? 15.214  4.818   4.931   1.00 24.94 ? 98   VAL B C   1 
ATOM   745  O O   . VAL A 1 100 ? 16.205  5.554   4.790   1.00 27.82 ? 98   VAL B O   1 
ATOM   746  C CB  . VAL A 1 100 ? 13.577  4.588   2.965   1.00 31.09 ? 98   VAL B CB  1 
ATOM   747  C CG1 . VAL A 1 100 ? 13.673  6.095   2.784   1.00 33.36 ? 98   VAL B CG1 1 
ATOM   748  C CG2 . VAL A 1 100 ? 13.419  3.891   1.625   1.00 31.23 ? 98   VAL B CG2 1 
ATOM   749  N N   . GLU A 1 101 ? 14.581  4.616   6.085   1.00 26.27 ? 99   GLU B N   1 
ATOM   750  C CA  . GLU A 1 101 ? 14.860  5.359   7.342   1.00 30.59 ? 99   GLU B CA  1 
ATOM   751  C C   . GLU A 1 101 ? 16.349  5.225   7.702   1.00 32.97 ? 99   GLU B C   1 
ATOM   752  O O   . GLU A 1 101 ? 16.933  6.186   8.231   1.00 30.67 ? 99   GLU B O   1 
ATOM   753  C CB  . GLU A 1 101 ? 13.911  4.843   8.420   1.00 33.45 ? 99   GLU B CB  1 
ATOM   754  C CG  . GLU A 1 101 ? 14.225  5.351   9.812   1.00 41.82 ? 99   GLU B CG  1 
ATOM   755  C CD  . GLU A 1 101 ? 13.356  4.760   10.910  1.00 46.94 ? 99   GLU B CD  1 
ATOM   756  O OE1 . GLU A 1 101 ? 13.494  5.195   12.078  1.00 53.99 ? 99   GLU B OE1 1 
ATOM   757  O OE2 . GLU A 1 101 ? 12.547  3.861   10.597  1.00 53.74 ? 99   GLU B OE2 1 
ATOM   758  N N   . HIS A 1 102 ? 16.995  4.094   7.386   1.00 29.06 ? 100  HIS B N   1 
ATOM   759  C CA  . HIS A 1 102 ? 18.409  3.848   7.753   1.00 27.72 ? 100  HIS B CA  1 
ATOM   760  C C   . HIS A 1 102 ? 19.367  3.889   6.559   1.00 28.66 ? 100  HIS B C   1 
ATOM   761  O O   . HIS A 1 102 ? 20.497  3.375   6.706   1.00 26.62 ? 100  HIS B O   1 
ATOM   762  C CB  . HIS A 1 102 ? 18.507  2.517   8.482   1.00 29.74 ? 100  HIS B CB  1 
ATOM   763  C CG  . HIS A 1 102 ? 17.569  2.401   9.626   1.00 30.86 ? 100  HIS B CG  1 
ATOM   764  N ND1 . HIS A 1 102 ? 17.638  3.242   10.713  1.00 30.87 ? 100  HIS B ND1 1 
ATOM   765  C CD2 . HIS A 1 102 ? 16.561  1.535   9.864   1.00 30.73 ? 100  HIS B CD2 1 
ATOM   766  C CE1 . HIS A 1 102 ? 16.701  2.908   11.568  1.00 29.41 ? 100  HIS B CE1 1 
ATOM   767  N NE2 . HIS A 1 102 ? 16.031  1.868   11.069  1.00 31.63 ? 100  HIS B NE2 1 
ATOM   768  N N   . GLY A 1 103 ? 18.979  4.536   5.464   1.00 25.57 ? 101  GLY B N   1 
ATOM   769  C CA  . GLY A 1 103 ? 19.819  4.708   4.262   1.00 26.89 ? 101  GLY B CA  1 
ATOM   770  C C   . GLY A 1 103 ? 19.576  3.630   3.222   1.00 22.76 ? 101  GLY B C   1 
ATOM   771  O O   . GLY A 1 103 ? 20.345  3.565   2.269   1.00 24.81 ? 101  GLY B O   1 
ATOM   772  N N   . GLY A 1 104 ? 18.554  2.812   3.421   1.00 23.64 ? 102  GLY B N   1 
ATOM   773  C CA  . GLY A 1 104 ? 18.190  1.700   2.515   1.00 23.81 ? 102  GLY B CA  1 
ATOM   774  C C   . GLY A 1 104 ? 17.452  2.134   1.264   1.00 26.11 ? 102  GLY B C   1 
ATOM   775  O O   . GLY A 1 104 ? 16.996  3.297   1.180   1.00 25.64 ? 102  GLY B O   1 
ATOM   776  N N   . GLN A 1 105 ? 17.323  1.241   0.290   1.00 24.73 ? 103  GLN B N   1 
ATOM   777  C CA  . GLN A 1 105 ? 16.548  1.511   -0.947  1.00 21.51 ? 103  GLN B CA  1 
ATOM   778  C C   . GLN A 1 105 ? 15.097  1.066   -0.773  1.00 23.02 ? 103  GLN B C   1 
ATOM   779  O O   . GLN A 1 105 ? 14.295  1.423   -1.642  1.00 23.90 ? 103  GLN B O   1 
ATOM   780  C CB  . GLN A 1 105 ? 17.191  0.858   -2.165  1.00 22.57 ? 103  GLN B CB  1 
ATOM   781  C CG  . GLN A 1 105 ? 18.621  1.264   -2.355  1.00 22.74 ? 103  GLN B CG  1 
ATOM   782  C CD  . GLN A 1 105 ? 19.223  0.634   -3.585  1.00 24.38 ? 103  GLN B CD  1 
ATOM   783  O OE1 . GLN A 1 105 ? 18.663  0.658   -4.687  1.00 26.42 ? 103  GLN B OE1 1 
ATOM   784  N NE2 . GLN A 1 105 ? 20.401  0.064   -3.411  1.00 26.22 ? 103  GLN B NE2 1 
ATOM   785  N N   . GLY A 1 106 ? 14.787  0.262   0.249   1.00 22.18 ? 104  GLY B N   1 
ATOM   786  C CA  . GLY A 1 106 ? 13.413  -0.070  0.670   1.00 22.39 ? 104  GLY B CA  1 
ATOM   787  C C   . GLY A 1 106 ? 12.752  -1.140  -0.177  1.00 24.09 ? 104  GLY B C   1 
ATOM   788  O O   . GLY A 1 106 ? 11.520  -1.305  -0.082  1.00 24.53 ? 104  GLY B O   1 
ATOM   789  N N   . LEU A 1 107 ? 13.509  -1.865  -0.995  1.00 23.15 ? 105  LEU B N   1 
ATOM   790  C CA  . LEU A 1 107 ? 12.901  -2.913  -1.864  1.00 24.01 ? 105  LEU B CA  1 
ATOM   791  C C   . LEU A 1 107 ? 12.634  -4.177  -1.049  1.00 21.67 ? 105  LEU B C   1 
ATOM   792  O O   . LEU A 1 107 ? 13.190  -4.340  0.029   1.00 21.33 ? 105  LEU B O   1 
ATOM   793  C CB  . LEU A 1 107 ? 13.828  -3.167  -3.042  1.00 26.46 ? 105  LEU B CB  1 
ATOM   794  C CG  . LEU A 1 107 ? 13.783  -2.032  -4.066  1.00 30.71 ? 105  LEU B CG  1 
ATOM   795  C CD1 . LEU A 1 107 ? 15.155  -1.697  -4.600  1.00 30.53 ? 105  LEU B CD1 1 
ATOM   796  C CD2 . LEU A 1 107 ? 12.822  -2.387  -5.186  1.00 31.98 ? 105  LEU B CD2 1 
ATOM   797  N N   . PRO A 1 108 ? 11.725  -5.073  -1.510  1.00 21.66 ? 106  PRO B N   1 
ATOM   798  C CA  . PRO A 1 108 ? 11.345  -6.243  -0.724  1.00 19.89 ? 106  PRO B CA  1 
ATOM   799  C C   . PRO A 1 108 ? 12.521  -7.205  -0.454  1.00 18.84 ? 106  PRO B C   1 
ATOM   800  O O   . PRO A 1 108 ? 13.401  -7.340  -1.314  1.00 18.17 ? 106  PRO B O   1 
ATOM   801  C CB  . PRO A 1 108 ? 10.306  -6.979  -1.608  1.00 22.32 ? 106  PRO B CB  1 
ATOM   802  C CG  . PRO A 1 108 ? 9.820   -5.916  -2.603  1.00 22.59 ? 106  PRO B CG  1 
ATOM   803  C CD  . PRO A 1 108 ? 10.989  -4.977  -2.779  1.00 22.53 ? 106  PRO B CD  1 
ATOM   804  N N   . GLU A 1 109 ? 12.550  -7.764  0.751   1.00 19.71 ? 107  GLU B N   1 
ATOM   805  C CA  . GLU A 1 109 ? 13.561  -8.783  1.152   1.00 20.06 ? 107  GLU B CA  1 
ATOM   806  C C   . GLU A 1 109 ? 13.628  -9.886  0.084   1.00 19.57 ? 107  GLU B C   1 
ATOM   807  O O   . GLU A 1 109 ? 14.743  -10.344 -0.221  1.00 19.24 ? 107  GLU B O   1 
ATOM   808  C CB  . GLU A 1 109 ? 13.212  -9.365  2.509   1.00 25.49 ? 107  GLU B CB  1 
ATOM   809  C CG  . GLU A 1 109 ? 14.194  -10.428 2.957   1.00 32.46 ? 107  GLU B CG  1 
ATOM   810  C CD  . GLU A 1 109 ? 15.103  -9.985  4.077   1.00 40.95 ? 107  GLU B CD  1 
ATOM   811  O OE1 . GLU A 1 109 ? 15.718  -8.921  3.933   1.00 53.56 ? 107  GLU B OE1 1 
ATOM   812  O OE2 . GLU A 1 109 ? 15.156  -10.691 5.110   1.00 52.52 ? 107  GLU B OE2 1 
ATOM   813  N N   . SER A 1 110 ? 12.496  -10.280 -0.484  1.00 18.48 ? 108  SER B N   1 
ATOM   814  C CA  . SER A 1 110 ? 12.453  -11.379 -1.484  1.00 18.73 ? 108  SER B CA  1 
ATOM   815  C C   . SER A 1 110 ? 13.175  -10.997 -2.777  1.00 20.15 ? 108  SER B C   1 
ATOM   816  O O   . SER A 1 110 ? 13.616  -11.897 -3.459  1.00 17.80 ? 108  SER B O   1 
ATOM   817  C CB  . SER A 1 110 ? 11.063  -11.821 -1.749  1.00 17.59 ? 108  SER B CB  1 
ATOM   818  O OG  . SER A 1 110 ? 10.316  -10.764 -2.329  1.00 18.45 ? 108  SER B OG  1 
ATOM   819  N N   . LEU A 1 111 ? 13.289  -9.707  -3.117  1.00 18.99 ? 109  LEU B N   1 
ATOM   820  C CA  . LEU A 1 111 ? 14.108  -9.258  -4.253  1.00 19.01 ? 109  LEU B CA  1 
ATOM   821  C C   . LEU A 1 111 ? 15.585  -9.309  -3.853  1.00 18.50 ? 109  LEU B C   1 
ATOM   822  O O   . LEU A 1 111 ? 16.409  -9.798  -4.662  1.00 20.30 ? 109  LEU B O   1 
ATOM   823  C CB  . LEU A 1 111 ? 13.708  -7.848  -4.676  1.00 21.04 ? 109  LEU B CB  1 
ATOM   824  C CG  . LEU A 1 111 ? 14.559  -7.278  -5.803  1.00 23.03 ? 109  LEU B CG  1 
ATOM   825  C CD1 . LEU A 1 111 ? 14.591  -8.210  -6.998  1.00 24.65 ? 109  LEU B CD1 1 
ATOM   826  C CD2 . LEU A 1 111 ? 14.038  -5.896  -6.207  1.00 25.85 ? 109  LEU B CD2 1 
ATOM   827  N N   . GLY A 1 112 ? 15.927  -8.867  -2.636  1.00 18.39 ? 110  GLY B N   1 
ATOM   828  C CA  . GLY A 1 112 ? 17.304  -9.028  -2.128  1.00 19.41 ? 110  GLY B CA  1 
ATOM   829  C C   . GLY A 1 112 ? 17.705  -10.492 -2.192  1.00 19.40 ? 110  GLY B C   1 
ATOM   830  O O   . GLY A 1 112 ? 18.876  -10.791 -2.518  1.00 19.56 ? 110  GLY B O   1 
ATOM   831  N N   . LEU A 1 113 ? 16.784  -11.376 -1.851  1.00 17.01 ? 111  LEU B N   1 
ATOM   832  C CA  . LEU A 1 113 ? 17.121  -12.824 -1.770  1.00 18.01 ? 111  LEU B CA  1 
ATOM   833  C C   . LEU A 1 113 ? 17.492  -13.342 -3.161  1.00 18.40 ? 111  LEU B C   1 
ATOM   834  O O   . LEU A 1 113 ? 18.364  -14.249 -3.263  1.00 17.60 ? 111  LEU B O   1 
ATOM   835  C CB  . LEU A 1 113 ? 15.934  -13.574 -1.185  1.00 20.44 ? 111  LEU B CB  1 
ATOM   836  C CG  . LEU A 1 113 ? 16.242  -15.022 -0.850  1.00 24.51 ? 111  LEU B CG  1 
ATOM   837  C CD1 . LEU A 1 113 ? 17.013  -15.104 0.470   1.00 28.98 ? 111  LEU B CD1 1 
ATOM   838  C CD2 . LEU A 1 113 ? 14.954  -15.794 -0.808  1.00 28.18 ? 111  LEU B CD2 1 
ATOM   839  N N   . ALA A 1 114 ? 16.892  -12.813 -4.232  1.00 16.85 ? 112  ALA B N   1 
ATOM   840  C CA  . ALA A 1 114 ? 17.259  -13.239 -5.604  1.00 17.02 ? 112  ALA B CA  1 
ATOM   841  C C   . ALA A 1 114 ? 18.689  -12.820 -5.944  1.00 17.41 ? 112  ALA B C   1 
ATOM   842  O O   . ALA A 1 114 ? 19.381  -13.576 -6.640  1.00 18.05 ? 112  ALA B O   1 
ATOM   843  C CB  . ALA A 1 114 ? 16.271  -12.736 -6.634  1.00 17.73 ? 112  ALA B CB  1 
ATOM   844  N N   . ILE A 1 115 ? 19.133  -11.652 -5.493  1.00 17.19 ? 113  ILE B N   1 
ATOM   845  C CA  . ILE A 1 115 ? 20.532  -11.219 -5.691  1.00 17.16 ? 113  ILE B CA  1 
ATOM   846  C C   . ILE A 1 115 ? 21.397  -12.193 -4.898  1.00 16.29 ? 113  ILE B C   1 
ATOM   847  O O   . ILE A 1 115 ? 22.385  -12.706 -5.446  1.00 16.02 ? 113  ILE B O   1 
ATOM   848  C CB  . ILE A 1 115 ? 20.713  -9.749  -5.250  1.00 17.98 ? 113  ILE B CB  1 
ATOM   849  C CG1 . ILE A 1 115 ? 19.740  -8.848  -6.021  1.00 17.61 ? 113  ILE B CG1 1 
ATOM   850  C CG2 . ILE A 1 115 ? 22.161  -9.316  -5.390  1.00 18.59 ? 113  ILE B CG2 1 
ATOM   851  C CD1 . ILE A 1 115 ? 19.913  -8.903  -7.511  1.00 19.29 ? 113  ILE B CD1 1 
ATOM   852  N N   . SER A 1 116 ? 21.010  -12.461 -3.659  1.00 17.32 ? 114  SER B N   1 
ATOM   853  C CA  . SER A 1 116 ? 21.759  -13.385 -2.775  1.00 15.70 ? 114  SER B CA  1 
ATOM   854  C C   . SER A 1 116 ? 21.865  -14.769 -3.455  1.00 16.42 ? 114  SER B C   1 
ATOM   855  O O   . SER A 1 116 ? 22.923  -15.422 -3.296  1.00 16.80 ? 114  SER B O   1 
ATOM   856  C CB  . SER A 1 116 ? 21.115  -13.476 -1.433  1.00 17.13 ? 114  SER B CB  1 
ATOM   857  O OG  . SER A 1 116 ? 21.211  -12.230 -0.717  1.00 17.72 ? 114  SER B OG  1 
ATOM   858  N N   . GLU A 1 117 ? 20.826  -15.205 -4.164  1.00 17.74 ? 115  GLU B N   1 
ATOM   859  C CA  . GLU A 1 117 ? 20.860  -16.550 -4.798  1.00 16.60 ? 115  GLU B CA  1 
ATOM   860  C C   . GLU A 1 117 ? 22.019  -16.587 -5.794  1.00 15.99 ? 115  GLU B C   1 
ATOM   861  O O   . GLU A 1 117 ? 22.801  -17.520 -5.754  1.00 15.74 ? 115  GLU B O   1 
ATOM   862  C CB  . GLU A 1 117 ? 19.549  -16.885 -5.518  1.00 16.44 ? 115  GLU B CB  1 
ATOM   863  C CG  . GLU A 1 117 ? 19.617  -18.214 -6.253  1.00 16.67 ? 115  GLU B CG  1 
ATOM   864  C CD  . GLU A 1 117 ? 18.477  -18.637 -7.167  1.00 17.86 ? 115  GLU B CD  1 
ATOM   865  O OE1 . GLU A 1 117 ? 18.708  -19.520 -8.004  1.00 16.48 ? 115  GLU B OE1 1 
ATOM   866  O OE2 . GLU A 1 117 ? 17.371  -18.109 -7.028  1.00 17.57 ? 115  GLU B OE2 1 
ATOM   867  N N   . MET A 1 118 ? 22.110  -15.555 -6.626  1.00 16.56 ? 116  MET B N   1 
ATOM   868  C CA  . MET A 1 118 ? 23.140  -15.505 -7.673  1.00 16.35 ? 116  MET B CA  1 
ATOM   869  C C   . MET A 1 118 ? 24.517  -15.292 -7.036  1.00 14.79 ? 116  MET B C   1 
ATOM   870  O O   . MET A 1 118 ? 25.499  -15.901 -7.523  1.00 15.05 ? 116  MET B O   1 
ATOM   871  C CB  . MET A 1 118 ? 22.803  -14.404 -8.675  1.00 17.10 ? 116  MET B CB  1 
ATOM   872  C CG  . MET A 1 118 ? 21.466  -14.634 -9.325  1.00 18.24 ? 116  MET B CG  1 
ATOM   873  S SD  . MET A 1 118 ? 21.090  -13.467 -10.654 1.00 20.02 ? 116  MET B SD  1 
ATOM   874  C CE  . MET A 1 118 ? 20.568  -12.067 -9.668  1.00 21.27 ? 116  MET B CE  1 
ATOM   875  N N   . VAL A 1 119 ? 24.613  -14.468 -5.989  1.00 15.47 ? 117  VAL B N   1 
ATOM   876  C CA  . VAL A 1 119 ? 25.909  -14.251 -5.289  1.00 15.65 ? 117  VAL B CA  1 
ATOM   877  C C   . VAL A 1 119 ? 26.413  -15.589 -4.727  1.00 15.71 ? 117  VAL B C   1 
ATOM   878  O O   . VAL A 1 119 ? 27.605  -15.884 -4.910  1.00 14.83 ? 117  VAL B O   1 
ATOM   879  C CB  . VAL A 1 119 ? 25.794  -13.165 -4.207  1.00 15.45 ? 117  VAL B CB  1 
ATOM   880  C CG1 . VAL A 1 119 ? 27.000  -13.128 -3.312  1.00 15.77 ? 117  VAL B CG1 1 
ATOM   881  C CG2 . VAL A 1 119 ? 25.570  -11.813 -4.867  1.00 15.52 ? 117  VAL B CG2 1 
ATOM   882  N N   . GLY A 1 120 ? 25.529  -16.320 -4.058  1.00 16.35 ? 118  GLY B N   1 
ATOM   883  C CA  . GLY A 1 120 ? 25.931  -17.592 -3.437  1.00 17.38 ? 118  GLY B CA  1 
ATOM   884  C C   . GLY A 1 120 ? 26.409  -18.605 -4.477  1.00 16.56 ? 118  GLY B C   1 
ATOM   885  O O   . GLY A 1 120 ? 27.308  -19.392 -4.152  1.00 16.18 ? 118  GLY B O   1 
ATOM   886  N N   . GLN A 1 121 ? 25.821  -18.589 -5.667  1.00 15.02 ? 119  GLN B N   1 
ATOM   887  C CA  . GLN A 1 121 ? 26.229  -19.503 -6.759  1.00 15.26 ? 119  GLN B CA  1 
ATOM   888  C C   . GLN A 1 121 ? 27.581  -19.080 -7.340  1.00 15.82 ? 119  GLN B C   1 
ATOM   889  O O   . GLN A 1 121 ? 28.416  -19.939 -7.562  1.00 16.80 ? 119  GLN B O   1 
ATOM   890  C CB  . GLN A 1 121 ? 25.152  -19.486 -7.846  1.00 15.40 ? 119  GLN B CB  1 
ATOM   891  C CG  . GLN A 1 121 ? 23.925  -20.292 -7.439  1.00 14.86 ? 119  GLN B CG  1 
ATOM   892  C CD  . GLN A 1 121 ? 22.661  -19.953 -8.187  1.00 16.09 ? 119  GLN B CD  1 
ATOM   893  O OE1 . GLN A 1 121 ? 22.691  -19.336 -9.242  1.00 16.28 ? 119  GLN B OE1 1 
ATOM   894  N NE2 . GLN A 1 121 ? 21.534  -20.385 -7.645  1.00 14.89 ? 119  GLN B NE2 1 
ATOM   895  N N   . ALA A 1 122 ? 27.757  -17.785 -7.554  1.00 15.99 ? 120  ALA B N   1 
ATOM   896  C CA  . ALA A 1 122 ? 28.994  -17.296 -8.198  1.00 16.49 ? 120  ALA B CA  1 
ATOM   897  C C   . ALA A 1 122 ? 30.206  -17.498 -7.291  1.00 14.58 ? 120  ALA B C   1 
ATOM   898  O O   . ALA A 1 122 ? 31.248  -17.886 -7.782  1.00 15.89 ? 120  ALA B O   1 
ATOM   899  C CB  . ALA A 1 122 ? 28.831  -15.839 -8.541  1.00 17.45 ? 120  ALA B CB  1 
ATOM   900  N N   . ASN A 1 123 ? 30.041  -17.189 -6.015  1.00 15.16 ? 121  ASN B N   1 
ATOM   901  C CA  . ASN A 1 123 ? 31.203  -17.253 -5.095  1.00 14.67 ? 121  ASN B CA  1 
ATOM   902  C C   . ASN A 1 123 ? 30.690  -17.269 -3.653  1.00 15.63 ? 121  ASN B C   1 
ATOM   903  O O   . ASN A 1 123 ? 30.606  -16.211 -3.042  1.00 15.85 ? 121  ASN B O   1 
ATOM   904  C CB  . ASN A 1 123 ? 32.153  -16.079 -5.352  1.00 15.41 ? 121  ASN B CB  1 
ATOM   905  C CG  . ASN A 1 123 ? 33.499  -16.213 -4.675  1.00 16.95 ? 121  ASN B CG  1 
ATOM   906  O OD1 . ASN A 1 123 ? 33.615  -16.826 -3.621  1.00 15.87 ? 121  ASN B OD1 1 
ATOM   907  N ND2 . ASN A 1 123 ? 34.516  -15.613 -5.266  1.00 16.37 ? 121  ASN B ND2 1 
ATOM   908  N N   . TRP A 1 124 ? 30.389  -18.459 -3.151  1.00 15.75 ? 122  TRP B N   1 
ATOM   909  C CA  . TRP A 1 124 ? 29.791  -18.556 -1.795  1.00 15.78 ? 122  TRP B CA  1 
ATOM   910  C C   . TRP A 1 124 ? 30.693  -17.922 -0.727  1.00 15.24 ? 122  TRP B C   1 
ATOM   911  O O   . TRP A 1 124 ? 30.191  -17.167 0.089   1.00 14.74 ? 122  TRP B O   1 
ATOM   912  C CB  . TRP A 1 124 ? 29.451  -20.016 -1.441  1.00 14.98 ? 122  TRP B CB  1 
ATOM   913  C CG  . TRP A 1 124 ? 28.905  -20.047 -0.049  1.00 14.63 ? 122  TRP B CG  1 
ATOM   914  C CD1 . TRP A 1 124 ? 29.584  -20.339 1.095   1.00 15.16 ? 122  TRP B CD1 1 
ATOM   915  C CD2 . TRP A 1 124 ? 27.589  -19.639 0.358   1.00 14.75 ? 122  TRP B CD2 1 
ATOM   916  N NE1 . TRP A 1 124 ? 28.769  -20.181 2.180   1.00 15.17 ? 122  TRP B NE1 1 
ATOM   917  C CE2 . TRP A 1 124 ? 27.540  -19.752 1.762   1.00 15.18 ? 122  TRP B CE2 1 
ATOM   918  C CE3 . TRP A 1 124 ? 26.443  -19.220 -0.324  1.00 16.92 ? 122  TRP B CE3 1 
ATOM   919  C CZ2 . TRP A 1 124 ? 26.392  -19.456 2.492   1.00 16.60 ? 122  TRP B CZ2 1 
ATOM   920  C CZ3 . TRP A 1 124 ? 25.310  -18.924 0.398   1.00 16.84 ? 122  TRP B CZ3 1 
ATOM   921  C CH2 . TRP A 1 124 ? 25.288  -19.041 1.786   1.00 16.53 ? 122  TRP B CH2 1 
ATOM   922  N N   . SER A 1 125 ? 31.977  -18.255 -0.751  1.00 14.62 ? 123  SER B N   1 
ATOM   923  C CA  . SER A 1 125 ? 32.911  -17.730 0.278   1.00 15.32 ? 123  SER B CA  1 
ATOM   924  C C   . SER A 1 125 ? 32.897  -16.194 0.286   1.00 14.75 ? 123  SER B C   1 
ATOM   925  O O   . SER A 1 125 ? 32.867  -15.628 1.365   1.00 16.32 ? 123  SER B O   1 
ATOM   926  C CB  . SER A 1 125 ? 34.297  -18.260 0.044   1.00 16.14 ? 123  SER B CB  1 
ATOM   927  O OG  . SER A 1 125 ? 34.347  -19.662 0.219   1.00 17.25 ? 123  SER B OG  1 
ATOM   928  N N   . TRP A 1 126 ? 32.913  -15.588 -0.896  1.00 14.08 ? 124  TRP B N   1 
ATOM   929  C CA  . TRP A 1 126 ? 32.864  -14.109 -1.017  1.00 15.87 ? 124  TRP B CA  1 
ATOM   930  C C   . TRP A 1 126 ? 31.521  -13.633 -0.465  1.00 16.58 ? 124  TRP B C   1 
ATOM   931  O O   . TRP A 1 126 ? 31.497  -12.661 0.321   1.00 15.84 ? 124  TRP B O   1 
ATOM   932  C CB  . TRP A 1 126 ? 33.096  -13.687 -2.477  1.00 14.94 ? 124  TRP B CB  1 
ATOM   933  C CG  . TRP A 1 126 ? 33.155  -12.197 -2.613  1.00 16.19 ? 124  TRP B CG  1 
ATOM   934  C CD1 . TRP A 1 126 ? 34.253  -11.402 -2.494  1.00 17.89 ? 124  TRP B CD1 1 
ATOM   935  C CD2 . TRP A 1 126 ? 32.036  -11.309 -2.758  1.00 15.18 ? 124  TRP B CD2 1 
ATOM   936  N NE1 . TRP A 1 126 ? 33.907  -10.083 -2.670  1.00 17.59 ? 124  TRP B NE1 1 
ATOM   937  C CE2 . TRP A 1 126 ? 32.556  -9.998  -2.821  1.00 17.51 ? 124  TRP B CE2 1 
ATOM   938  C CE3 . TRP A 1 126 ? 30.662  -11.490 -2.951  1.00 16.89 ? 124  TRP B CE3 1 
ATOM   939  C CZ2 . TRP A 1 126 ? 31.737  -8.882  -2.988  1.00 16.97 ? 124  TRP B CZ2 1 
ATOM   940  C CZ3 . TRP A 1 126 ? 29.856  -10.396 -3.145  1.00 17.07 ? 124  TRP B CZ3 1 
ATOM   941  C CH2 . TRP A 1 126 ? 30.393  -9.099  -3.157  1.00 17.77 ? 124  TRP B CH2 1 
ATOM   942  N N   . GLY A 1 127 ? 30.419  -14.301 -0.852  1.00 16.26 ? 125  GLY B N   1 
ATOM   943  C CA  . GLY A 1 127 ? 29.063  -13.884 -0.492  1.00 15.04 ? 125  GLY B CA  1 
ATOM   944  C C   . GLY A 1 127 ? 28.808  -13.909 1.005   1.00 16.32 ? 125  GLY B C   1 
ATOM   945  O O   . GLY A 1 127 ? 27.897  -13.215 1.483   1.00 16.03 ? 125  GLY B O   1 
ATOM   946  N N   . MET A 1 128 ? 29.564  -14.713 1.753   1.00 16.54 ? 126  MET B N   1 
ATOM   947  C CA  . MET A 1 128 ? 29.398  -14.778 3.212   1.00 16.90 ? 126  MET B CA  1 
ATOM   948  C C   . MET A 1 128 ? 29.649  -13.409 3.846   1.00 16.23 ? 126  MET B C   1 
ATOM   949  O O   . MET A 1 128 ? 29.022  -13.138 4.874   1.00 17.69 ? 126  MET B O   1 
ATOM   950  C CB  . MET A 1 128 ? 30.350  -15.843 3.773   1.00 17.09 ? 126  MET B CB  1 
ATOM   951  C CG  . MET A 1 128 ? 29.831  -17.215 3.529   1.00 16.28 ? 126  MET B CG  1 
ATOM   952  S SD  . MET A 1 128 ? 30.966  -18.516 4.061   1.00 16.09 ? 126  MET B SD  1 
ATOM   953  C CE  . MET A 1 128 ? 30.759  -18.404 5.835   1.00 16.77 ? 126  MET B CE  1 
ATOM   954  N N   . TYR A 1 129 ? 30.586  -12.619 3.314   1.00 16.63 ? 127  TYR B N   1 
ATOM   955  C CA  . TYR A 1 129 ? 30.946  -11.312 3.931   1.00 16.74 ? 127  TYR B CA  1 
ATOM   956  C C   . TYR A 1 129 ? 29.707  -10.414 3.937   1.00 16.13 ? 127  TYR B C   1 
ATOM   957  O O   . TYR A 1 129 ? 29.248  -10.019 5.019   1.00 17.73 ? 127  TYR B O   1 
ATOM   958  C CB  . TYR A 1 129 ? 32.198  -10.728 3.285   1.00 17.04 ? 127  TYR B CB  1 
ATOM   959  C CG  . TYR A 1 129 ? 33.471  -11.515 3.470   1.00 17.68 ? 127  TYR B CG  1 
ATOM   960  C CD1 . TYR A 1 129 ? 34.282  -11.344 4.587   1.00 17.38 ? 127  TYR B CD1 1 
ATOM   961  C CD2 . TYR A 1 129 ? 33.881  -12.460 2.541   1.00 17.52 ? 127  TYR B CD2 1 
ATOM   962  C CE1 . TYR A 1 129 ? 35.461  -12.034 4.738   1.00 17.33 ? 127  TYR B CE1 1 
ATOM   963  C CE2 . TYR A 1 129 ? 35.069  -13.155 2.674   1.00 18.01 ? 127  TYR B CE2 1 
ATOM   964  C CZ  . TYR A 1 129 ? 35.849  -12.975 3.800   1.00 17.62 ? 127  TYR B CZ  1 
ATOM   965  O OH  . TYR A 1 129 ? 37.033  -13.642 3.930   1.00 17.67 ? 127  TYR B OH  1 
ATOM   966  N N   . PRO A 1 130 ? 29.077  -10.054 2.785   1.00 15.62 ? 128  PRO B N   1 
ATOM   967  C CA  . PRO A 1 130 ? 27.831  -9.297  2.849   1.00 17.15 ? 128  PRO B CA  1 
ATOM   968  C C   . PRO A 1 130 ? 26.653  -10.068 3.448   1.00 18.15 ? 128  PRO B C   1 
ATOM   969  O O   . PRO A 1 130 ? 25.784  -9.473  4.035   1.00 18.48 ? 128  PRO B O   1 
ATOM   970  C CB  . PRO A 1 130 ? 27.509  -8.923  1.380   1.00 16.97 ? 128  PRO B CB  1 
ATOM   971  C CG  . PRO A 1 130 ? 28.314  -9.904  0.564   1.00 17.23 ? 128  PRO B CG  1 
ATOM   972  C CD  . PRO A 1 130 ? 29.523  -10.221 1.408   1.00 15.97 ? 128  PRO B CD  1 
ATOM   973  N N   . GLY A 1 131 ? 26.621  -11.397 3.294   1.00 17.82 ? 129  GLY B N   1 
ATOM   974  C CA  . GLY A 1 131 ? 25.493  -12.182 3.799   1.00 17.08 ? 129  GLY B CA  1 
ATOM   975  C C   . GLY A 1 131 ? 25.370  -12.149 5.310   1.00 15.95 ? 129  GLY B C   1 
ATOM   976  O O   . GLY A 1 131 ? 24.266  -11.938 5.825   1.00 18.71 ? 129  GLY B O   1 
ATOM   977  N N   . LEU A 1 132 ? 26.468  -12.363 6.026   1.00 16.44 ? 130  LEU B N   1 
ATOM   978  C CA  . LEU A 1 132 ? 26.445  -12.266 7.505   1.00 17.38 ? 130  LEU B CA  1 
ATOM   979  C C   . LEU A 1 132 ? 26.068  -10.829 7.894   1.00 18.80 ? 130  LEU B C   1 
ATOM   980  O O   . LEU A 1 132 ? 25.339  -10.685 8.884   1.00 18.93 ? 130  LEU B O   1 
ATOM   981  C CB  . LEU A 1 132 ? 27.805  -12.679 8.059   1.00 19.03 ? 130  LEU B CB  1 
ATOM   982  C CG  . LEU A 1 132 ? 28.021  -14.188 8.033   1.00 18.93 ? 130  LEU B CG  1 
ATOM   983  C CD1 . LEU A 1 132 ? 29.490  -14.547 7.951   1.00 21.23 ? 130  LEU B CD1 1 
ATOM   984  C CD2 . LEU A 1 132 ? 27.347  -14.830 9.241   1.00 20.55 ? 130  LEU B CD2 1 
ATOM   985  N N   . SER A 1 133 ? 26.522  -9.844  7.132   1.00 17.76 ? 131  SER B N   1 
ATOM   986  C CA  . SER A 1 133 ? 26.218  -8.420  7.445   1.00 18.14 ? 131  SER B CA  1 
ATOM   987  C C   . SER A 1 133 ? 24.700  -8.220  7.414   1.00 20.27 ? 131  SER B C   1 
ATOM   988  O O   . SER A 1 133 ? 24.181  -7.501  8.271   1.00 20.50 ? 131  SER B O   1 
ATOM   989  C CB  . SER A 1 133 ? 26.921  -7.476  6.525   1.00 18.32 ? 131  SER B CB  1 
ATOM   990  O OG  . SER A 1 133 ? 28.340  -7.621  6.609   1.00 18.93 ? 131  SER B OG  1 
ATOM   991  N N   . HIS A 1 134 ? 23.972  -8.863  6.486   1.00 20.61 ? 132  HIS B N   1 
ATOM   992  C CA  . HIS A 1 134 ? 22.491  -8.773  6.399   1.00 21.94 ? 132  HIS B CA  1 
ATOM   993  C C   . HIS A 1 134 ? 21.868  -9.313  7.688   1.00 20.55 ? 132  HIS B C   1 
ATOM   994  O O   . HIS A 1 134 ? 20.875  -8.716  8.187   1.00 20.51 ? 132  HIS B O   1 
ATOM   995  C CB  . HIS A 1 134 ? 21.979  -9.494  5.129   1.00 25.37 ? 132  HIS B CB  1 
ATOM   996  C CG  . HIS A 1 134 ? 22.101  -8.654  3.903   1.00 33.15 ? 132  HIS B CG  1 
ATOM   997  N ND1 . HIS A 1 134 ? 22.577  -9.131  2.689   1.00 34.48 ? 132  HIS B ND1 1 
ATOM   998  C CD2 . HIS A 1 134 ? 21.787  -7.352  3.704   1.00 33.73 ? 132  HIS B CD2 1 
ATOM   999  C CE1 . HIS A 1 134 ? 22.572  -8.137  1.806   1.00 34.64 ? 132  HIS B CE1 1 
ATOM   1000 N NE2 . HIS A 1 134 ? 22.072  -7.024  2.414   1.00 32.38 ? 132  HIS B NE2 1 
ATOM   1001 N N   . GLY A 1 135 ? 22.372  -10.434 8.236   1.00 18.66 ? 133  GLY B N   1 
ATOM   1002 C CA  . GLY A 1 135 ? 21.893  -10.967 9.519   1.00 18.79 ? 133  GLY B CA  1 
ATOM   1003 C C   . GLY A 1 135 ? 22.085  -9.948  10.644  1.00 20.73 ? 133  GLY B C   1 
ATOM   1004 O O   . GLY A 1 135 ? 21.196  -9.823  11.510  1.00 21.31 ? 133  GLY B O   1 
ATOM   1005 N N   . ALA A 1 136 ? 23.226  -9.277  10.649  1.00 20.84 ? 134  ALA B N   1 
ATOM   1006 C CA  . ALA A 1 136 ? 23.530  -8.278  11.695  1.00 20.35 ? 134  ALA B CA  1 
ATOM   1007 C C   . ALA A 1 136 ? 22.531  -7.116  11.553  1.00 19.10 ? 134  ALA B C   1 
ATOM   1008 O O   . ALA A 1 136 ? 21.997  -6.659  12.573  1.00 20.72 ? 134  ALA B O   1 
ATOM   1009 C CB  . ALA A 1 136 ? 24.929  -7.803  11.571  1.00 19.33 ? 134  ALA B CB  1 
ATOM   1010 N N   . MET A 1 137 ? 22.274  -6.696  10.327  1.00 19.28 ? 135  MET B N   1 
ATOM   1011 C CA  . MET A 1 137 ? 21.281  -5.619  10.030  1.00 18.55 ? 135  MET B CA  1 
ATOM   1012 C C   . MET A 1 137 ? 19.900  -6.012  10.542  1.00 20.87 ? 135  MET B C   1 
ATOM   1013 O O   . MET A 1 137 ? 19.227  -5.190  11.259  1.00 19.55 ? 135  MET B O   1 
ATOM   1014 C CB  . MET A 1 137 ? 21.232  -5.284  8.544   1.00 19.25 ? 135  MET B CB  1 
ATOM   1015 C CG  . MET A 1 137 ? 22.502  -4.644  8.086   1.00 21.12 ? 135  MET B CG  1 
ATOM   1016 S SD  . MET A 1 137 ? 22.443  -4.050  6.400   1.00 26.16 ? 135  MET B SD  1 
ATOM   1017 C CE  . MET A 1 137 ? 23.670  -5.041  5.540   1.00 26.71 ? 135  MET B CE  1 
ATOM   1018 N N   . ASN A 1 138 ? 19.462  -7.242  10.264  1.00 19.51 ? 136  ASN B N   1 
ATOM   1019 C CA  . ASN A 1 138 ? 18.127  -7.708  10.681  1.00 21.14 ? 136  ASN B CA  1 
ATOM   1020 C C   . ASN A 1 138 ? 18.031  -7.668  12.207  1.00 20.38 ? 136  ASN B C   1 
ATOM   1021 O O   . ASN A 1 138 ? 16.944  -7.310  12.720  1.00 21.67 ? 136  ASN B O   1 
ATOM   1022 C CB  . ASN A 1 138 ? 17.825  -9.108  10.160  1.00 21.98 ? 136  ASN B CB  1 
ATOM   1023 C CG  . ASN A 1 138 ? 17.725  -9.128  8.651   1.00 24.33 ? 136  ASN B CG  1 
ATOM   1024 O OD1 . ASN A 1 138 ? 17.597  -8.078  7.978   1.00 25.84 ? 136  ASN B OD1 1 
ATOM   1025 N ND2 . ASN A 1 138 ? 17.840  -10.332 8.121   1.00 23.26 ? 136  ASN B ND2 1 
ATOM   1026 N N   . THR A 1 139 ? 19.101  -8.031  12.909  1.00 19.51 ? 137  THR B N   1 
ATOM   1027 C CA  . THR A 1 139 ? 19.154  -8.046  14.390  1.00 19.17 ? 137  THR B CA  1 
ATOM   1028 C C   . THR A 1 139 ? 19.053  -6.579  14.885  1.00 19.23 ? 137  THR B C   1 
ATOM   1029 O O   . THR A 1 139 ? 18.310  -6.331  15.836  1.00 21.17 ? 137  THR B O   1 
ATOM   1030 C CB  . THR A 1 139 ? 20.440  -8.730  14.886  1.00 21.38 ? 137  THR B CB  1 
ATOM   1031 O OG1 . THR A 1 139 ? 20.519  -10.019 14.252  1.00 22.45 ? 137  THR B OG1 1 
ATOM   1032 C CG2 . THR A 1 139 ? 20.486  -8.953  16.382  1.00 21.13 ? 137  THR B CG2 1 
ATOM   1033 N N   . LEU A 1 140 ? 19.830  -5.677  14.299  1.00 20.09 ? 138  LEU B N   1 
ATOM   1034 C CA  . LEU A 1 140 ? 19.793  -4.249  14.761  1.00 21.33 ? 138  LEU B CA  1 
ATOM   1035 C C   . LEU A 1 140 ? 18.422  -3.653  14.471  1.00 24.74 ? 138  LEU B C   1 
ATOM   1036 O O   . LEU A 1 140 ? 17.934  -2.861  15.314  1.00 23.50 ? 138  LEU B O   1 
ATOM   1037 C CB  . LEU A 1 140 ? 20.896  -3.455  14.087  1.00 21.96 ? 138  LEU B CB  1 
ATOM   1038 C CG  . LEU A 1 140 ? 22.250  -3.593  14.769  1.00 26.12 ? 138  LEU B CG  1 
ATOM   1039 C CD1 . LEU A 1 140 ? 23.354  -3.272  13.790  1.00 28.82 ? 138  LEU B CD1 1 
ATOM   1040 C CD2 . LEU A 1 140 ? 22.305  -2.698  16.010  1.00 28.71 ? 138  LEU B CD2 1 
ATOM   1041 N N   . HIS A 1 141 ? 17.840  -3.973  13.319  1.00 23.02 ? 139  HIS B N   1 
ATOM   1042 C CA  . HIS A 1 141 ? 16.483  -3.489  12.950  1.00 25.70 ? 139  HIS B CA  1 
ATOM   1043 C C   . HIS A 1 141 ? 15.455  -3.957  13.981  1.00 25.90 ? 139  HIS B C   1 
ATOM   1044 O O   . HIS A 1 141 ? 14.666  -3.132  14.463  1.00 23.34 ? 139  HIS B O   1 
ATOM   1045 C CB  . HIS A 1 141 ? 16.109  -3.922  11.541  1.00 25.69 ? 139  HIS B CB  1 
ATOM   1046 C CG  . HIS A 1 141 ? 14.936  -3.188  11.010  1.00 28.96 ? 139  HIS B CG  1 
ATOM   1047 N ND1 . HIS A 1 141 ? 13.661  -3.698  11.091  1.00 35.46 ? 139  HIS B ND1 1 
ATOM   1048 C CD2 . HIS A 1 141 ? 14.842  -1.984  10.406  1.00 33.35 ? 139  HIS B CD2 1 
ATOM   1049 C CE1 . HIS A 1 141 ? 12.819  -2.851  10.533  1.00 35.59 ? 139  HIS B CE1 1 
ATOM   1050 N NE2 . HIS A 1 141 ? 13.521  -1.787  10.109  1.00 33.35 ? 139  HIS B NE2 1 
ATOM   1051 N N   . ALA A 1 142 ? 15.477  -5.233  14.339  1.00 24.86 ? 140  ALA B N   1 
ATOM   1052 C CA  . ALA A 1 142 ? 14.452  -5.795  15.242  1.00 23.52 ? 140  ALA B CA  1 
ATOM   1053 C C   . ALA A 1 142 ? 14.659  -5.452  16.718  1.00 23.50 ? 140  ALA B C   1 
ATOM   1054 O O   . ALA A 1 142 ? 13.656  -5.307  17.413  1.00 24.58 ? 140  ALA B O   1 
ATOM   1055 C CB  . ALA A 1 142 ? 14.477  -7.291  15.090  1.00 23.33 ? 140  ALA B CB  1 
ATOM   1056 N N   . HIS A 1 143 ? 15.900  -5.325  17.175  1.00 21.00 ? 141  HIS B N   1 
ATOM   1057 C CA  . HIS A 1 143 ? 16.141  -5.192  18.635  1.00 22.48 ? 141  HIS B CA  1 
ATOM   1058 C C   . HIS A 1 143 ? 16.962  -3.966  19.042  1.00 21.72 ? 141  HIS B C   1 
ATOM   1059 O O   . HIS A 1 143 ? 17.064  -3.730  20.242  1.00 25.25 ? 141  HIS B O   1 
ATOM   1060 C CB  . HIS A 1 143 ? 16.885  -6.443  19.093  1.00 21.97 ? 141  HIS B CB  1 
ATOM   1061 C CG  . HIS A 1 143 ? 16.204  -7.703  18.670  1.00 23.29 ? 141  HIS B CG  1 
ATOM   1062 N ND1 . HIS A 1 143 ? 14.970  -8.069  19.158  1.00 23.94 ? 141  HIS B ND1 1 
ATOM   1063 C CD2 . HIS A 1 143 ? 16.562  -8.664  17.793  1.00 26.38 ? 141  HIS B CD2 1 
ATOM   1064 C CE1 . HIS A 1 143 ? 14.601  -9.208  18.613  1.00 23.59 ? 141  HIS B CE1 1 
ATOM   1065 N NE2 . HIS A 1 143 ? 15.559  -9.593  17.772  1.00 24.59 ? 141  HIS B NE2 1 
ATOM   1066 N N   . GLY A 1 144 ? 17.531  -3.248  18.093  1.00 21.59 ? 142  GLY B N   1 
ATOM   1067 C CA  . GLY A 1 144 ? 18.432  -2.114  18.405  1.00 21.20 ? 142  GLY B CA  1 
ATOM   1068 C C   . GLY A 1 144 ? 17.632  -0.906  18.893  1.00 23.01 ? 142  GLY B C   1 
ATOM   1069 O O   . GLY A 1 144 ? 16.453  -0.803  18.531  1.00 24.00 ? 142  GLY B O   1 
ATOM   1070 N N   . THR A 1 145 ? 18.230  -0.105  19.776  1.00 24.38 ? 143  THR B N   1 
ATOM   1071 C CA  . THR A 1 145 ? 17.721  1.247   20.137  1.00 24.31 ? 143  THR B CA  1 
ATOM   1072 C C   . THR A 1 145 ? 17.868  2.160   18.917  1.00 23.45 ? 143  THR B C   1 
ATOM   1073 O O   . THR A 1 145 ? 18.673  1.875   17.979  1.00 22.12 ? 143  THR B O   1 
ATOM   1074 C CB  . THR A 1 145 ? 18.491  1.803   21.348  1.00 24.75 ? 143  THR B CB  1 
ATOM   1075 O OG1 . THR A 1 145 ? 19.873  1.944   21.007  1.00 26.25 ? 143  THR B OG1 1 
ATOM   1076 C CG2 . THR A 1 145 ? 18.385  0.958   22.598  1.00 26.27 ? 143  THR B CG2 1 
ATOM   1077 N N   . ALA A 1 146 ? 17.173  3.305   18.931  1.00 23.21 ? 144  ALA B N   1 
ATOM   1078 C CA  . ALA A 1 146 ? 17.381  4.375   17.952  1.00 23.63 ? 144  ALA B CA  1 
ATOM   1079 C C   . ALA A 1 146 ? 18.870  4.672   17.809  1.00 21.90 ? 144  ALA B C   1 
ATOM   1080 O O   . ALA A 1 146 ? 19.333  4.829   16.658  1.00 22.89 ? 144  ALA B O   1 
ATOM   1081 C CB  . ALA A 1 146 ? 16.584  5.601   18.392  1.00 23.14 ? 144  ALA B CB  1 
ATOM   1082 N N   . GLU A 1 147 ? 19.609  4.814   18.910  1.00 22.55 ? 145  GLU B N   1 
ATOM   1083 C CA  . GLU A 1 147 ? 21.043  5.207   18.823  1.00 23.18 ? 145  GLU B CA  1 
ATOM   1084 C C   . GLU A 1 147 ? 21.861  4.045   18.207  1.00 21.90 ? 145  GLU B C   1 
ATOM   1085 O O   . GLU A 1 147 ? 22.753  4.284   17.344  1.00 22.36 ? 145  GLU B O   1 
ATOM   1086 C CB  . GLU A 1 147 ? 21.582  5.607   20.201  1.00 26.02 ? 145  GLU B CB  1 
ATOM   1087 C CG  . GLU A 1 147 ? 23.022  6.080   20.142  1.00 28.84 ? 145  GLU B CG  1 
ATOM   1088 C CD  . GLU A 1 147 ? 23.697  6.291   21.488  1.00 36.66 ? 145  GLU B CD  1 
ATOM   1089 O OE1 . GLU A 1 147 ? 24.945  6.307   21.512  1.00 43.94 ? 145  GLU B OE1 1 
ATOM   1090 O OE2 . GLU A 1 147 ? 22.978  6.437   22.517  1.00 44.45 ? 145  GLU B OE2 1 
ATOM   1091 N N   . GLN A 1 148 ? 21.577  2.818   18.603  1.00 20.93 ? 146  GLN B N   1 
ATOM   1092 C CA  . GLN A 1 148 ? 22.315  1.663   18.022  1.00 22.33 ? 146  GLN B CA  1 
ATOM   1093 C C   . GLN A 1 148 ? 22.062  1.597   16.507  1.00 22.19 ? 146  GLN B C   1 
ATOM   1094 O O   . GLN A 1 148 ? 22.984  1.276   15.765  1.00 21.35 ? 146  GLN B O   1 
ATOM   1095 C CB  . GLN A 1 148 ? 21.922  0.385   18.760  1.00 21.58 ? 146  GLN B CB  1 
ATOM   1096 C CG  . GLN A 1 148 ? 22.485  0.325   20.172  1.00 23.41 ? 146  GLN B CG  1 
ATOM   1097 C CD  . GLN A 1 148 ? 21.860  -0.758  21.016  1.00 21.23 ? 146  GLN B CD  1 
ATOM   1098 O OE1 . GLN A 1 148 ? 20.840  -1.334  20.663  1.00 21.44 ? 146  GLN B OE1 1 
ATOM   1099 N NE2 . GLN A 1 148 ? 22.479  -1.041  22.148  1.00 23.54 ? 146  GLN B NE2 1 
ATOM   1100 N N   . GLN A 1 149 ? 20.848  1.918   16.090  1.00 20.61 ? 147  GLN B N   1 
ATOM   1101 C CA  . GLN A 1 149 ? 20.502  1.942   14.650  1.00 21.69 ? 147  GLN B CA  1 
ATOM   1102 C C   . GLN A 1 149 ? 21.204  3.108   13.963  1.00 23.11 ? 147  GLN B C   1 
ATOM   1103 O O   . GLN A 1 149 ? 21.747  2.929   12.885  1.00 22.04 ? 147  GLN B O   1 
ATOM   1104 C CB  . GLN A 1 149 ? 18.989  1.967   14.456  1.00 24.54 ? 147  GLN B CB  1 
ATOM   1105 C CG  . GLN A 1 149 ? 18.286  0.720   14.960  1.00 25.48 ? 147  GLN B CG  1 
ATOM   1106 C CD  . GLN A 1 149 ? 16.791  0.812   14.790  1.00 29.27 ? 147  GLN B CD  1 
ATOM   1107 O OE1 . GLN A 1 149 ? 16.219  1.897   14.685  1.00 30.75 ? 147  GLN B OE1 1 
ATOM   1108 N NE2 . GLN A 1 149 ? 16.128  -0.324  14.831  1.00 27.57 ? 147  GLN B NE2 1 
ATOM   1109 N N   . ALA A 1 150 ? 21.188  4.313   14.549  1.00 25.22 ? 148  ALA B N   1 
ATOM   1110 C CA  . ALA A 1 150 ? 21.834  5.469   13.899  1.00 24.80 ? 148  ALA B CA  1 
ATOM   1111 C C   . ALA A 1 150 ? 23.334  5.221   13.740  1.00 21.91 ? 148  ALA B C   1 
ATOM   1112 O O   . ALA A 1 150 ? 23.900  5.597   12.727  1.00 23.94 ? 148  ALA B O   1 
ATOM   1113 C CB  . ALA A 1 150 ? 21.539  6.742   14.693  1.00 25.11 ? 148  ALA B CB  1 
ATOM   1114 N N   . THR A 1 151 ? 23.971  4.624   14.741  1.00 22.70 ? 149  THR B N   1 
ATOM   1115 C CA  . THR A 1 151 ? 25.433  4.396   14.785  1.00 21.47 ? 149  THR B CA  1 
ATOM   1116 C C   . THR A 1 151 ? 25.836  3.184   13.921  1.00 21.00 ? 149  THR B C   1 
ATOM   1117 O O   . THR A 1 151 ? 26.718  3.347   13.054  1.00 20.55 ? 149  THR B O   1 
ATOM   1118 C CB  . THR A 1 151 ? 25.881  4.257   16.237  1.00 24.03 ? 149  THR B CB  1 
ATOM   1119 O OG1 . THR A 1 151 ? 25.691  5.539   16.852  1.00 25.52 ? 149  THR B OG1 1 
ATOM   1120 C CG2 . THR A 1 151 ? 27.333  3.862   16.346  1.00 23.11 ? 149  THR B CG2 1 
ATOM   1121 N N   . TYR A 1 152 ? 25.210  2.032   14.138  1.00 22.39 ? 150  TYR B N   1 
ATOM   1122 C CA  . TYR A 1 152 ? 25.702  0.739   13.580  1.00 21.64 ? 150  TYR B CA  1 
ATOM   1123 C C   . TYR A 1 152 ? 24.878  0.342   12.355  1.00 22.06 ? 150  TYR B C   1 
ATOM   1124 O O   . TYR A 1 152 ? 25.471  -0.024  11.343  1.00 22.09 ? 150  TYR B O   1 
ATOM   1125 C CB  . TYR A 1 152 ? 25.703  -0.335  14.664  1.00 22.08 ? 150  TYR B CB  1 
ATOM   1126 C CG  . TYR A 1 152 ? 26.632  0.006   15.800  1.00 21.35 ? 150  TYR B CG  1 
ATOM   1127 C CD1 . TYR A 1 152 ? 28.012  -0.130  15.672  1.00 20.92 ? 150  TYR B CD1 1 
ATOM   1128 C CD2 . TYR A 1 152 ? 26.138  0.522   16.981  1.00 22.09 ? 150  TYR B CD2 1 
ATOM   1129 C CE1 . TYR A 1 152 ? 28.877  0.205   16.709  1.00 21.90 ? 150  TYR B CE1 1 
ATOM   1130 C CE2 . TYR A 1 152 ? 26.983  0.849   18.031  1.00 23.41 ? 150  TYR B CE2 1 
ATOM   1131 C CZ  . TYR A 1 152 ? 28.355  0.711   17.894  1.00 24.05 ? 150  TYR B CZ  1 
ATOM   1132 O OH  . TYR A 1 152 ? 29.181  1.062   18.920  1.00 27.64 ? 150  TYR B OH  1 
ATOM   1133 N N   . LEU A 1 153 ? 23.559  0.412   12.427  1.00 21.74 ? 151  LEU B N   1 
ATOM   1134 C CA  . LEU A 1 153 ? 22.713  -0.053  11.292  1.00 22.06 ? 151  LEU B CA  1 
ATOM   1135 C C   . LEU A 1 153 ? 22.974  0.792   10.048  1.00 22.19 ? 151  LEU B C   1 
ATOM   1136 O O   . LEU A 1 153 ? 23.110  0.223   8.972   1.00 19.95 ? 151  LEU B O   1 
ATOM   1137 C CB  . LEU A 1 153 ? 21.248  -0.068  11.697  1.00 21.48 ? 151  LEU B CB  1 
ATOM   1138 C CG  . LEU A 1 153 ? 20.278  -0.598  10.649  1.00 21.68 ? 151  LEU B CG  1 
ATOM   1139 C CD1 . LEU A 1 153 ? 20.750  -1.970  10.135  1.00 21.72 ? 151  LEU B CD1 1 
ATOM   1140 C CD2 . LEU A 1 153 ? 18.890  -0.710  11.226  1.00 21.39 ? 151  LEU B CD2 1 
ATOM   1141 N N   . THR A 1 154 ? 23.071  2.123   10.139  1.00 22.32 ? 152  THR B N   1 
ATOM   1142 C CA  . THR A 1 154 ? 23.327  2.938   8.920   1.00 22.08 ? 152  THR B CA  1 
ATOM   1143 C C   . THR A 1 154 ? 24.632  2.517   8.229   1.00 20.94 ? 152  THR B C   1 
ATOM   1144 O O   . THR A 1 154 ? 24.708  2.511   6.998   1.00 21.37 ? 152  THR B O   1 
ATOM   1145 C CB  . THR A 1 154 ? 23.347  4.435   9.274   1.00 23.03 ? 152  THR B CB  1 
ATOM   1146 O OG1 . THR A 1 154 ? 24.379  4.608   10.251  1.00 23.93 ? 152  THR B OG1 1 
ATOM   1147 C CG2 . THR A 1 154 ? 22.004  4.894   9.793   1.00 23.91 ? 152  THR B CG2 1 
ATOM   1148 N N   . LYS A 1 155 ? 25.660  2.194   9.005   1.00 19.92 ? 153  LYS B N   1 
ATOM   1149 C CA  A LYS A 1 155 ? 26.995  1.853   8.473   0.50 21.04 ? 153  LYS B CA  1 
ATOM   1150 C CA  B LYS A 1 155 ? 26.999  1.847   8.482   0.50 20.89 ? 153  LYS B CA  1 
ATOM   1151 C C   . LYS A 1 155 ? 26.932  0.464   7.820   1.00 20.15 ? 153  LYS B C   1 
ATOM   1152 O O   . LYS A 1 155 ? 27.577  0.312   6.810   1.00 23.41 ? 153  LYS B O   1 
ATOM   1153 C CB  A LYS A 1 155 ? 28.040  1.947   9.587   0.50 22.18 ? 153  LYS B CB  1 
ATOM   1154 C CB  B LYS A 1 155 ? 28.033  1.900   9.608   0.50 21.78 ? 153  LYS B CB  1 
ATOM   1155 C CG  A LYS A 1 155 ? 28.432  3.373   9.963   0.50 22.56 ? 153  LYS B CG  1 
ATOM   1156 C CG  B LYS A 1 155 ? 28.481  3.306   9.998   0.50 22.01 ? 153  LYS B CG  1 
ATOM   1157 C CD  A LYS A 1 155 ? 29.235  4.070   8.884   0.50 22.33 ? 153  LYS B CD  1 
ATOM   1158 C CD  B LYS A 1 155 ? 29.443  3.919   9.001   0.50 21.37 ? 153  LYS B CD  1 
ATOM   1159 C CE  A LYS A 1 155 ? 29.797  5.427   9.270   0.50 23.09 ? 153  LYS B CE  1 
ATOM   1160 C CE  B LYS A 1 155 ? 30.058  5.234   9.439   0.50 22.17 ? 153  LYS B CE  1 
ATOM   1161 N NZ  A LYS A 1 155 ? 28.724  6.405   9.563   0.50 23.56 ? 153  LYS B NZ  1 
ATOM   1162 N NZ  B LYS A 1 155 ? 31.067  5.718   8.466   0.50 22.89 ? 153  LYS B NZ  1 
ATOM   1163 N N   . LEU A 1 156 ? 26.167  -0.465  8.399   1.00 21.90 ? 154  LEU B N   1 
ATOM   1164 C CA  . LEU A 1 156 ? 25.994  -1.838  7.811   1.00 21.08 ? 154  LEU B CA  1 
ATOM   1165 C C   . LEU A 1 156 ? 25.181  -1.701  6.517   1.00 20.52 ? 154  LEU B C   1 
ATOM   1166 O O   . LEU A 1 156 ? 25.572  -2.277  5.495   1.00 20.69 ? 154  LEU B O   1 
ATOM   1167 C CB  . LEU A 1 156 ? 25.299  -2.755  8.809   1.00 20.72 ? 154  LEU B CB  1 
ATOM   1168 C CG  . LEU A 1 156 ? 26.145  -3.194  9.999   1.00 22.25 ? 154  LEU B CG  1 
ATOM   1169 C CD1 . LEU A 1 156 ? 25.257  -3.670  11.122  1.00 24.18 ? 154  LEU B CD1 1 
ATOM   1170 C CD2 . LEU A 1 156 ? 27.115  -4.282  9.571   1.00 22.60 ? 154  LEU B CD2 1 
ATOM   1171 N N   . VAL A 1 157 ? 24.139  -0.874  6.508   1.00 19.86 ? 155  VAL B N   1 
ATOM   1172 C CA  . VAL A 1 157 ? 23.255  -0.706  5.316   1.00 20.91 ? 155  VAL B CA  1 
ATOM   1173 C C   . VAL A 1 157 ? 24.029  -0.135  4.129   1.00 21.96 ? 155  VAL B C   1 
ATOM   1174 O O   . VAL A 1 157 ? 23.772  -0.562  2.993   1.00 23.47 ? 155  VAL B O   1 
ATOM   1175 C CB  . VAL A 1 157 ? 22.011  0.155   5.655   1.00 22.18 ? 155  VAL B CB  1 
ATOM   1176 C CG1 . VAL A 1 157 ? 21.279  0.602   4.403   1.00 23.53 ? 155  VAL B CG1 1 
ATOM   1177 C CG2 . VAL A 1 157 ? 21.059  -0.589  6.571   1.00 20.39 ? 155  VAL B CG2 1 
ATOM   1178 N N   . SER A 1 158 ? 24.973  0.780   4.352   1.00 22.45 ? 156  SER B N   1 
ATOM   1179 C CA  . SER A 1 158 ? 25.818  1.378   3.291   1.00 25.29 ? 156  SER B CA  1 
ATOM   1180 C C   . SER A 1 158 ? 26.854  0.362   2.797   1.00 26.30 ? 156  SER B C   1 
ATOM   1181 O O   . SER A 1 158 ? 27.394  0.565   1.687   1.00 26.29 ? 156  SER B O   1 
ATOM   1182 C CB  . SER A 1 158 ? 26.494  2.619   3.765   1.00 25.64 ? 156  SER B CB  1 
ATOM   1183 O OG  . SER A 1 158 ? 27.458  2.282   4.736   1.00 25.78 ? 156  SER B OG  1 
ATOM   1184 N N   . GLY A 1 159 ? 27.160  -0.649  3.615   1.00 24.76 ? 157  GLY B N   1 
ATOM   1185 C CA  . GLY A 1 159 ? 28.201  -1.641  3.318   1.00 24.59 ? 157  GLY B CA  1 
ATOM   1186 C C   . GLY A 1 159 ? 29.566  -1.185  3.785   1.00 26.00 ? 157  GLY B C   1 
ATOM   1187 O O   . GLY A 1 159 ? 30.510  -1.964  3.666   1.00 24.82 ? 157  GLY B O   1 
ATOM   1188 N N   . GLU A 1 160 ? 29.669  0.030   4.346   1.00 25.14 ? 158  GLU B N   1 
ATOM   1189 C CA  . GLU A 1 160 ? 30.949  0.574   4.852   1.00 26.37 ? 158  GLU B CA  1 
ATOM   1190 C C   . GLU A 1 160 ? 31.513  -0.315  5.963   1.00 21.60 ? 158  GLU B C   1 
ATOM   1191 O O   . GLU A 1 160 ? 32.744  -0.442  6.009   1.00 19.93 ? 158  GLU B O   1 
ATOM   1192 C CB  . GLU A 1 160 ? 30.722  1.980   5.401   1.00 30.05 ? 158  GLU B CB  1 
ATOM   1193 C CG  . GLU A 1 160 ? 30.399  3.018   4.329   1.00 35.93 ? 158  GLU B CG  1 
ATOM   1194 C CD  . GLU A 1 160 ? 30.054  4.340   5.004   1.00 38.22 ? 158  GLU B CD  1 
ATOM   1195 O OE1 . GLU A 1 160 ? 31.002  5.049   5.364   1.00 39.90 ? 158  GLU B OE1 1 
ATOM   1196 O OE2 . GLU A 1 160 ? 28.853  4.598   5.261   1.00 39.86 ? 158  GLU B OE2 1 
ATOM   1197 N N   . TRP A 1 161 ? 30.653  -0.794  6.862   1.00 20.53 ? 159  TRP B N   1 
ATOM   1198 C CA  . TRP A 1 161 ? 30.976  -1.754  7.950   1.00 20.65 ? 159  TRP B CA  1 
ATOM   1199 C C   . TRP A 1 161 ? 30.316  -3.103  7.660   1.00 20.94 ? 159  TRP B C   1 
ATOM   1200 O O   . TRP A 1 161 ? 29.214  -3.123  7.082   1.00 20.66 ? 159  TRP B O   1 
ATOM   1201 C CB  . TRP A 1 161 ? 30.506  -1.245  9.314   1.00 20.76 ? 159  TRP B CB  1 
ATOM   1202 C CG  . TRP A 1 161 ? 31.143  0.057   9.701   1.00 21.07 ? 159  TRP B CG  1 
ATOM   1203 C CD1 . TRP A 1 161 ? 32.072  0.766   9.005   1.00 21.60 ? 159  TRP B CD1 1 
ATOM   1204 C CD2 . TRP A 1 161 ? 30.900  0.792   10.915  1.00 22.75 ? 159  TRP B CD2 1 
ATOM   1205 N NE1 . TRP A 1 161 ? 32.423  1.892   9.700   1.00 22.73 ? 159  TRP B NE1 1 
ATOM   1206 C CE2 . TRP A 1 161 ? 31.720  1.936   10.867  1.00 19.75 ? 159  TRP B CE2 1 
ATOM   1207 C CE3 . TRP A 1 161 ? 30.069  0.607   12.017  1.00 20.74 ? 159  TRP B CE3 1 
ATOM   1208 C CZ2 . TRP A 1 161 ? 31.732  2.892   11.883  1.00 20.37 ? 159  TRP B CZ2 1 
ATOM   1209 C CZ3 . TRP A 1 161 ? 30.093  1.534   13.035  1.00 22.27 ? 159  TRP B CZ3 1 
ATOM   1210 C CH2 . TRP A 1 161 ? 30.912  2.661   12.961  1.00 21.39 ? 159  TRP B CH2 1 
ATOM   1211 N N   . THR A 1 162 ? 30.935  -4.191  8.114   1.00 19.62 ? 160  THR B N   1 
ATOM   1212 C CA  . THR A 1 162 ? 30.351  -5.538  7.973   1.00 17.90 ? 160  THR B CA  1 
ATOM   1213 C C   . THR A 1 162 ? 29.951  -6.027  9.352   1.00 18.62 ? 160  THR B C   1 
ATOM   1214 O O   . THR A 1 162 ? 30.325  -5.352  10.342  1.00 20.03 ? 160  THR B O   1 
ATOM   1215 C CB  . THR A 1 162 ? 31.313  -6.491  7.262   1.00 18.40 ? 160  THR B CB  1 
ATOM   1216 O OG1 . THR A 1 162 ? 32.543  -6.510  7.998   1.00 20.05 ? 160  THR B OG1 1 
ATOM   1217 C CG2 . THR A 1 162 ? 31.618  -6.137  5.828   1.00 18.75 ? 160  THR B CG2 1 
ATOM   1218 N N   . GLY A 1 163 ? 29.233  -7.156  9.429   1.00 17.11 ? 161  GLY B N   1 
ATOM   1219 C CA  . GLY A 1 163 ? 28.736  -7.687  10.696  1.00 16.94 ? 161  GLY B CA  1 
ATOM   1220 C C   . GLY A 1 163 ? 28.961  -9.177  10.842  1.00 17.30 ? 161  GLY B C   1 
ATOM   1221 O O   . GLY A 1 163 ? 28.983  -9.889  9.832   1.00 20.17 ? 161  GLY B O   1 
ATOM   1222 N N   . THR A 1 164 ? 29.056  -9.651  12.060  1.00 17.76 ? 162  THR B N   1 
ATOM   1223 C CA  . THR A 1 164 ? 29.356  -11.084 12.335  1.00 18.54 ? 162  THR B CA  1 
ATOM   1224 C C   . THR A 1 164 ? 28.430  -11.567 13.428  1.00 18.83 ? 162  THR B C   1 
ATOM   1225 O O   . THR A 1 164 ? 27.874  -10.714 14.194  1.00 20.00 ? 162  THR B O   1 
ATOM   1226 C CB  . THR A 1 164 ? 30.787  -11.307 12.835  1.00 18.53 ? 162  THR B CB  1 
ATOM   1227 O OG1 . THR A 1 164 ? 30.858  -10.684 14.134  1.00 21.53 ? 162  THR B OG1 1 
ATOM   1228 C CG2 . THR A 1 164 ? 31.827  -10.779 11.891  1.00 18.33 ? 162  THR B CG2 1 
ATOM   1229 N N   . MET A 1 165 ? 28.262  -12.880 13.529  1.00 17.42 ? 163  MET B N   1 
ATOM   1230 C CA  . MET A 1 165 ? 27.514  -13.494 14.638  1.00 19.93 ? 163  MET B CA  1 
ATOM   1231 C C   . MET A 1 165 ? 28.514  -14.317 15.462  1.00 22.67 ? 163  MET B C   1 
ATOM   1232 O O   . MET A 1 165 ? 29.180  -15.245 14.905  1.00 21.43 ? 163  MET B O   1 
ATOM   1233 C CB  . MET A 1 165 ? 26.355  -14.335 14.107  1.00 21.80 ? 163  MET B CB  1 
ATOM   1234 C CG  . MET A 1 165 ? 26.767  -15.393 13.117  1.00 23.61 ? 163  MET B CG  1 
ATOM   1235 S SD  . MET A 1 165 ? 25.353  -16.035 12.160  1.00 28.77 ? 163  MET B SD  1 
ATOM   1236 C CE  . MET A 1 165 ? 24.217  -16.441 13.489  1.00 23.60 ? 163  MET B CE  1 
ATOM   1237 N N   . CYS A 1 166 ? 28.661  -13.981 16.748  1.00 20.75 ? 164  CYS B N   1 
ATOM   1238 C CA  . CYS A 1 166 ? 29.689  -14.576 17.638  1.00 20.39 ? 164  CYS B CA  1 
ATOM   1239 C C   . CYS A 1 166 ? 28.988  -15.371 18.728  1.00 23.50 ? 164  CYS B C   1 
ATOM   1240 O O   . CYS A 1 166 ? 28.553  -14.769 19.763  1.00 22.28 ? 164  CYS B O   1 
ATOM   1241 C CB  . CYS A 1 166 ? 30.579  -13.493 18.236  1.00 20.69 ? 164  CYS B CB  1 
ATOM   1242 S SG  . CYS A 1 166 ? 31.647  -12.666 17.039  1.00 21.11 ? 164  CYS B SG  1 
ATOM   1243 N N   . LEU A 1 167 ? 28.866  -16.689 18.533  1.00 21.96 ? 165  LEU B N   1 
ATOM   1244 C CA  . LEU A 1 167 ? 28.141  -17.576 19.463  1.00 22.13 ? 165  LEU B CA  1 
ATOM   1245 C C   . LEU A 1 167 ? 29.118  -18.620 20.011  1.00 22.05 ? 165  LEU B C   1 
ATOM   1246 O O   . LEU A 1 167 ? 29.281  -18.720 21.245  1.00 23.30 ? 165  LEU B O   1 
ATOM   1247 C CB  . LEU A 1 167 ? 26.993  -18.261 18.711  1.00 23.22 ? 165  LEU B CB  1 
ATOM   1248 C CG  . LEU A 1 167 ? 25.902  -17.352 18.152  1.00 25.74 ? 165  LEU B CG  1 
ATOM   1249 C CD1 . LEU A 1 167 ? 26.277  -16.803 16.790  1.00 25.46 ? 165  LEU B CD1 1 
ATOM   1250 C CD2 . LEU A 1 167 ? 24.583  -18.120 18.094  1.00 27.52 ? 165  LEU B CD2 1 
ATOM   1251 N N   . THR A 1 168 ? 29.752  -19.357 19.099  1.00 23.51 ? 166  THR B N   1 
ATOM   1252 C CA  . THR A 1 168 ? 30.470  -20.626 19.363  1.00 22.55 ? 166  THR B CA  1 
ATOM   1253 C C   . THR A 1 168 ? 31.710  -20.397 20.235  1.00 22.51 ? 166  THR B C   1 
ATOM   1254 O O   . THR A 1 168 ? 32.423  -19.416 20.012  1.00 20.92 ? 166  THR B O   1 
ATOM   1255 C CB  . THR A 1 168 ? 30.799  -21.283 18.012  1.00 22.60 ? 166  THR B CB  1 
ATOM   1256 O OG1 . THR A 1 168 ? 29.551  -21.315 17.304  1.00 22.56 ? 166  THR B OG1 1 
ATOM   1257 C CG2 . THR A 1 168 ? 31.414  -22.656 18.171  1.00 22.25 ? 166  THR B CG2 1 
ATOM   1258 N N   . GLU A 1 169 ? 31.923  -21.279 21.210  1.00 21.58 ? 167  GLU B N   1 
ATOM   1259 C CA  . GLU A 1 169 ? 33.147  -21.358 22.031  1.00 22.15 ? 167  GLU B CA  1 
ATOM   1260 C C   . GLU A 1 169 ? 33.692  -22.767 21.868  1.00 25.55 ? 167  GLU B C   1 
ATOM   1261 O O   . GLU A 1 169 ? 33.015  -23.641 21.325  1.00 26.58 ? 167  GLU B O   1 
ATOM   1262 C CB  . GLU A 1 169 ? 32.840  -20.991 23.485  1.00 24.19 ? 167  GLU B CB  1 
ATOM   1263 C CG  . GLU A 1 169 ? 32.194  -19.611 23.607  1.00 22.14 ? 167  GLU B CG  1 
ATOM   1264 C CD  . GLU A 1 169 ? 31.844  -19.145 25.008  1.00 24.60 ? 167  GLU B CD  1 
ATOM   1265 O OE1 . GLU A 1 169 ? 31.369  -17.977 25.158  1.00 24.83 ? 167  GLU B OE1 1 
ATOM   1266 O OE2 . GLU A 1 169 ? 32.017  -19.930 25.951  1.00 26.39 ? 167  GLU B OE2 1 
ATOM   1267 N N   . PRO A 1 170 ? 34.946  -22.999 22.274  1.00 24.61 ? 168  PRO B N   1 
ATOM   1268 C CA  . PRO A 1 170 ? 35.565  -24.310 22.089  1.00 28.13 ? 168  PRO B CA  1 
ATOM   1269 C C   . PRO A 1 170 ? 34.704  -25.498 22.551  1.00 30.10 ? 168  PRO B C   1 
ATOM   1270 O O   . PRO A 1 170 ? 34.651  -26.521 21.858  1.00 29.49 ? 168  PRO B O   1 
ATOM   1271 C CB  . PRO A 1 170 ? 36.818  -24.208 22.966  1.00 28.01 ? 168  PRO B CB  1 
ATOM   1272 C CG  . PRO A 1 170 ? 37.193  -22.737 22.874  1.00 29.27 ? 168  PRO B CG  1 
ATOM   1273 C CD  . PRO A 1 170 ? 35.857  -22.017 22.897  1.00 28.51 ? 168  PRO B CD  1 
ATOM   1274 N N   . HIS A 1 171 ? 34.016  -25.340 23.683  1.00 30.98 ? 169  HIS B N   1 
ATOM   1275 C CA  . HIS A 1 171 ? 33.216  -26.423 24.314  1.00 30.77 ? 169  HIS B CA  1 
ATOM   1276 C C   . HIS A 1 171 ? 31.746  -26.394 23.880  1.00 30.79 ? 169  HIS B C   1 
ATOM   1277 O O   . HIS A 1 171 ? 31.007  -27.308 24.319  1.00 28.95 ? 169  HIS B O   1 
ATOM   1278 C CB  . HIS A 1 171 ? 33.272  -26.306 25.836  1.00 31.27 ? 169  HIS B CB  1 
ATOM   1279 C CG  . HIS A 1 171 ? 32.606  -25.068 26.337  1.00 31.34 ? 169  HIS B CG  1 
ATOM   1280 N ND1 . HIS A 1 171 ? 33.199  -23.813 26.209  1.00 32.92 ? 169  HIS B ND1 1 
ATOM   1281 C CD2 . HIS A 1 171 ? 31.428  -24.870 26.971  1.00 35.65 ? 169  HIS B CD2 1 
ATOM   1282 C CE1 . HIS A 1 171 ? 32.399  -22.903 26.736  1.00 34.95 ? 169  HIS B CE1 1 
ATOM   1283 N NE2 . HIS A 1 171 ? 31.313  -23.521 27.212  1.00 32.39 ? 169  HIS B NE2 1 
ATOM   1284 N N   . CYS A 1 172 ? 31.296  -25.415 23.079  1.00 29.49 ? 170  CYS B N   1 
ATOM   1285 C CA  . CYS A 1 172 ? 29.850  -25.350 22.755  1.00 30.69 ? 170  CYS B CA  1 
ATOM   1286 C C   . CYS A 1 172 ? 29.568  -24.647 21.422  1.00 32.04 ? 170  CYS B C   1 
ATOM   1287 O O   . CYS A 1 172 ? 30.005  -23.484 21.216  1.00 28.36 ? 170  CYS B O   1 
ATOM   1288 C CB  . CYS A 1 172 ? 29.073  -24.694 23.889  1.00 31.35 ? 170  CYS B CB  1 
ATOM   1289 S SG  . CYS A 1 172 ? 29.598  -22.999 24.272  1.00 32.98 ? 170  CYS B SG  1 
ATOM   1290 N N   . GLY A 1 173 ? 28.787  -25.331 20.583  1.00 30.45 ? 171  GLY B N   1 
ATOM   1291 C CA  . GLY A 1 173 ? 28.206  -24.815 19.334  1.00 28.70 ? 171  GLY B CA  1 
ATOM   1292 C C   . GLY A 1 173 ? 26.697  -24.895 19.419  1.00 30.79 ? 171  GLY B C   1 
ATOM   1293 O O   . GLY A 1 173 ? 26.026  -23.840 19.514  1.00 27.76 ? 171  GLY B O   1 
ATOM   1294 N N   . THR A 1 174 ? 26.177  -26.115 19.488  1.00 30.76 ? 172  THR B N   1 
ATOM   1295 C CA  . THR A 1 174 ? 24.714  -26.303 19.626  1.00 28.85 ? 172  THR B CA  1 
ATOM   1296 C C   . THR A 1 174 ? 24.258  -25.876 21.025  1.00 31.27 ? 172  THR B C   1 
ATOM   1297 O O   . THR A 1 174 ? 23.196  -25.258 21.122  1.00 31.44 ? 172  THR B O   1 
ATOM   1298 C CB  . THR A 1 174 ? 24.331  -27.771 19.385  1.00 27.42 ? 172  THR B CB  1 
ATOM   1299 O OG1 . THR A 1 174 ? 24.741  -28.134 18.066  1.00 26.09 ? 172  THR B OG1 1 
ATOM   1300 C CG2 . THR A 1 174 ? 22.850  -28.017 19.567  1.00 27.31 ? 172  THR B CG2 1 
ATOM   1301 N N   . ASP A 1 175 ? 25.043  -26.189 22.055  1.00 29.79 ? 173  ASP B N   1 
ATOM   1302 C CA  . ASP A 1 175 ? 24.606  -25.946 23.457  1.00 30.55 ? 173  ASP B CA  1 
ATOM   1303 C C   . ASP A 1 175 ? 24.990  -24.540 23.913  1.00 27.82 ? 173  ASP B C   1 
ATOM   1304 O O   . ASP A 1 175 ? 25.924  -24.417 24.709  1.00 32.10 ? 173  ASP B O   1 
ATOM   1305 C CB  . ASP A 1 175 ? 25.199  -27.002 24.393  1.00 27.38 ? 173  ASP B CB  1 
ATOM   1306 C CG  . ASP A 1 175 ? 24.506  -27.121 25.740  1.00 30.48 ? 173  ASP B CG  1 
ATOM   1307 O OD1 . ASP A 1 175 ? 23.773  -26.193 26.113  1.00 31.97 ? 173  ASP B OD1 1 
ATOM   1308 O OD2 . ASP A 1 175 ? 24.710  -28.148 26.404  1.00 28.07 ? 173  ASP B OD2 1 
ATOM   1309 N N   . LEU A 1 176 ? 24.253  -23.539 23.449  1.00 28.37 ? 174  LEU B N   1 
ATOM   1310 C CA  . LEU A 1 176 ? 24.592  -22.133 23.784  1.00 30.00 ? 174  LEU B CA  1 
ATOM   1311 C C   . LEU A 1 176 ? 24.450  -21.903 25.298  1.00 30.95 ? 174  LEU B C   1 
ATOM   1312 O O   . LEU A 1 176 ? 25.110  -21.003 25.810  1.00 30.49 ? 174  LEU B O   1 
ATOM   1313 C CB  . LEU A 1 176 ? 23.691  -21.211 22.958  1.00 31.27 ? 174  LEU B CB  1 
ATOM   1314 C CG  . LEU A 1 176 ? 23.921  -21.299 21.451  1.00 31.60 ? 174  LEU B CG  1 
ATOM   1315 C CD1 . LEU A 1 176 ? 22.944  -20.416 20.692  1.00 33.68 ? 174  LEU B CD1 1 
ATOM   1316 C CD2 . LEU A 1 176 ? 25.356  -20.941 21.100  1.00 30.95 ? 174  LEU B CD2 1 
ATOM   1317 N N   . GLY A 1 177 ? 23.631  -22.707 25.966  1.00 31.25 ? 175  GLY B N   1 
ATOM   1318 C CA  . GLY A 1 177 ? 23.409  -22.505 27.409  1.00 32.91 ? 175  GLY B CA  1 
ATOM   1319 C C   . GLY A 1 177 ? 24.675  -22.697 28.225  1.00 31.73 ? 175  GLY B C   1 
ATOM   1320 O O   . GLY A 1 177 ? 24.695  -22.263 29.377  1.00 34.05 ? 175  GLY B O   1 
ATOM   1321 N N   . MET A 1 178 ? 25.688  -23.336 27.652  1.00 30.85 ? 176  MET B N   1 
ATOM   1322 C CA  . MET A 1 178 ? 27.001  -23.541 28.329  1.00 28.75 ? 176  MET B CA  1 
ATOM   1323 C C   . MET A 1 178 ? 28.005  -22.408 28.035  1.00 27.44 ? 176  MET B C   1 
ATOM   1324 O O   . MET A 1 178 ? 29.154  -22.535 28.531  1.00 27.00 ? 176  MET B O   1 
ATOM   1325 C CB  . MET A 1 178 ? 27.655  -24.854 27.873  1.00 30.66 ? 176  MET B CB  1 
ATOM   1326 C CG  . MET A 1 178 ? 27.063  -26.109 28.481  1.00 34.17 ? 176  MET B CG  1 
ATOM   1327 S SD  . MET A 1 178 ? 28.284  -27.465 28.314  1.00 37.32 ? 176  MET B SD  1 
ATOM   1328 C CE  . MET A 1 178 ? 28.097  -27.790 26.559  1.00 30.35 ? 176  MET B CE  1 
ATOM   1329 N N   . LEU A 1 179 ? 27.684  -21.369 27.243  1.00 28.02 ? 177  LEU B N   1 
ATOM   1330 C CA  . LEU A 1 179 ? 28.733  -20.367 26.888  1.00 28.86 ? 177  LEU B CA  1 
ATOM   1331 C C   . LEU A 1 179 ? 29.198  -19.643 28.156  1.00 25.72 ? 177  LEU B C   1 
ATOM   1332 O O   . LEU A 1 179 ? 28.393  -19.482 29.082  1.00 27.22 ? 177  LEU B O   1 
ATOM   1333 C CB  . LEU A 1 179 ? 28.293  -19.387 25.791  1.00 29.06 ? 177  LEU B CB  1 
ATOM   1334 C CG  . LEU A 1 179 ? 27.163  -18.413 26.119  1.00 30.37 ? 177  LEU B CG  1 
ATOM   1335 C CD1 . LEU A 1 179 ? 27.682  -17.159 26.800  1.00 32.40 ? 177  LEU B CD1 1 
ATOM   1336 C CD2 . LEU A 1 179 ? 26.437  -18.001 24.840  1.00 33.26 ? 177  LEU B CD2 1 
ATOM   1337 N N   . ARG A 1 180 ? 30.465  -19.257 28.179  1.00 26.35 ? 178  ARG B N   1 
ATOM   1338 C CA  . ARG A 1 180 ? 31.115  -18.670 29.382  1.00 28.23 ? 178  ARG B CA  1 
ATOM   1339 C C   . ARG A 1 180 ? 31.618  -17.250 29.120  1.00 27.34 ? 178  ARG B C   1 
ATOM   1340 O O   . ARG A 1 180 ? 32.072  -16.623 30.094  1.00 24.86 ? 178  ARG B O   1 
ATOM   1341 C CB  . ARG A 1 180 ? 32.274  -19.566 29.822  1.00 31.63 ? 178  ARG B CB  1 
ATOM   1342 C CG  . ARG A 1 180 ? 31.805  -20.931 30.316  1.00 38.31 ? 178  ARG B CG  1 
ATOM   1343 C CD  . ARG A 1 180 ? 32.870  -21.766 31.012  1.00 45.20 ? 178  ARG B CD  1 
ATOM   1344 N NE  . ARG A 1 180 ? 34.227  -21.292 30.764  1.00 56.47 ? 178  ARG B NE  1 
ATOM   1345 C CZ  . ARG A 1 180 ? 35.005  -20.636 31.637  1.00 62.95 ? 178  ARG B CZ  1 
ATOM   1346 N NH1 . ARG A 1 180 ? 34.588  -20.371 32.869  1.00 62.58 ? 178  ARG B NH1 1 
ATOM   1347 N NH2 . ARG A 1 180 ? 36.213  -20.244 31.263  1.00 64.34 ? 178  ARG B NH2 1 
ATOM   1348 N N   . THR A 1 181 ? 31.621  -16.767 27.875  1.00 24.18 ? 179  THR B N   1 
ATOM   1349 C CA  . THR A 1 181 ? 32.029  -15.364 27.583  1.00 22.97 ? 179  THR B CA  1 
ATOM   1350 C C   . THR A 1 181 ? 31.240  -14.464 28.526  1.00 23.41 ? 179  THR B C   1 
ATOM   1351 O O   . THR A 1 181 ? 30.001  -14.655 28.644  1.00 22.14 ? 179  THR B O   1 
ATOM   1352 C CB  . THR A 1 181 ? 31.827  -14.975 26.115  1.00 24.18 ? 179  THR B CB  1 
ATOM   1353 O OG1 . THR A 1 181 ? 32.742  -15.684 25.280  1.00 23.86 ? 179  THR B OG1 1 
ATOM   1354 C CG2 . THR A 1 181 ? 32.065  -13.495 25.903  1.00 25.21 ? 179  THR B CG2 1 
ATOM   1355 N N   . LYS A 1 182 ? 31.931  -13.516 29.180  1.00 23.62 ? 180  LYS B N   1 
ATOM   1356 C CA  . LYS A 1 182 ? 31.318  -12.687 30.252  1.00 26.98 ? 180  LYS B CA  1 
ATOM   1357 C C   . LYS A 1 182 ? 31.177  -11.249 29.779  1.00 23.19 ? 180  LYS B C   1 
ATOM   1358 O O   . LYS A 1 182 ? 32.013  -10.810 29.037  1.00 26.49 ? 180  LYS B O   1 
ATOM   1359 C CB  . LYS A 1 182 ? 32.195  -12.722 31.503  1.00 31.34 ? 180  LYS B CB  1 
ATOM   1360 C CG  . LYS A 1 182 ? 31.998  -13.971 32.347  1.00 38.72 ? 180  LYS B CG  1 
ATOM   1361 C CD  . LYS A 1 182 ? 33.017  -14.082 33.471  1.00 45.56 ? 180  LYS B CD  1 
ATOM   1362 C CE  . LYS A 1 182 ? 34.221  -14.923 33.109  1.00 49.91 ? 180  LYS B CE  1 
ATOM   1363 N NZ  . LYS A 1 182 ? 34.761  -15.618 34.302  1.00 54.85 ? 180  LYS B NZ  1 
ATOM   1364 N N   . ALA A 1 183 ? 30.101  -10.586 30.194  1.00 25.73 ? 181  ALA B N   1 
ATOM   1365 C CA  . ALA A 1 183 ? 29.871  -9.136  29.984  1.00 24.07 ? 181  ALA B CA  1 
ATOM   1366 C C   . ALA A 1 183 ? 29.800  -8.470  31.376  1.00 26.94 ? 181  ALA B C   1 
ATOM   1367 O O   . ALA A 1 183 ? 28.836  -8.732  32.109  1.00 26.52 ? 181  ALA B O   1 
ATOM   1368 C CB  . ALA A 1 183 ? 28.597  -8.958  29.203  1.00 23.68 ? 181  ALA B CB  1 
ATOM   1369 N N   . GLU A 1 184 ? 30.820  -7.695  31.726  1.00 27.45 ? 182  GLU B N   1 
ATOM   1370 C CA  . GLU A 1 184 ? 30.931  -7.020  33.049  1.00 28.50 ? 182  GLU B CA  1 
ATOM   1371 C C   . GLU A 1 184 ? 30.376  -5.602  32.904  1.00 25.80 ? 182  GLU B C   1 
ATOM   1372 O O   . GLU A 1 184 ? 30.921  -4.836  32.128  1.00 23.82 ? 182  GLU B O   1 
ATOM   1373 C CB  . GLU A 1 184 ? 32.387  -7.043  33.498  1.00 33.67 ? 182  GLU B CB  1 
ATOM   1374 C CG  . GLU A 1 184 ? 32.636  -6.307  34.810  1.00 43.13 ? 182  GLU B CG  1 
ATOM   1375 C CD  . GLU A 1 184 ? 34.013  -6.536  35.410  1.00 52.53 ? 182  GLU B CD  1 
ATOM   1376 O OE1 . GLU A 1 184 ? 34.204  -6.180  36.596  1.00 63.49 ? 182  GLU B OE1 1 
ATOM   1377 O OE2 . GLU A 1 184 ? 34.896  -7.068  34.685  1.00 65.15 ? 182  GLU B OE2 1 
ATOM   1378 N N   . PRO A 1 185 ? 29.284  -5.239  33.610  1.00 27.00 ? 183  PRO B N   1 
ATOM   1379 C CA  . PRO A 1 185 ? 28.696  -3.901  33.503  1.00 27.38 ? 183  PRO B CA  1 
ATOM   1380 C C   . PRO A 1 185 ? 29.663  -2.824  34.004  1.00 26.65 ? 183  PRO B C   1 
ATOM   1381 O O   . PRO A 1 185 ? 30.347  -3.044  34.997  1.00 24.68 ? 183  PRO B O   1 
ATOM   1382 C CB  . PRO A 1 185 ? 27.427  -3.910  34.362  1.00 24.97 ? 183  PRO B CB  1 
ATOM   1383 C CG  . PRO A 1 185 ? 27.467  -5.216  35.141  1.00 30.74 ? 183  PRO B CG  1 
ATOM   1384 C CD  . PRO A 1 185 ? 28.518  -6.104  34.519  1.00 28.25 ? 183  PRO B CD  1 
ATOM   1385 N N   . GLN A 1 186 ? 29.735  -1.728  33.248  1.00 27.04 ? 184  GLN B N   1 
ATOM   1386 C CA  . GLN A 1 186 ? 30.568  -0.536  33.527  1.00 26.08 ? 184  GLN B CA  1 
ATOM   1387 C C   . GLN A 1 186 ? 29.633  0.574   34.008  1.00 25.12 ? 184  GLN B C   1 
ATOM   1388 O O   . GLN A 1 186 ? 28.423  0.570   33.676  1.00 24.42 ? 184  GLN B O   1 
ATOM   1389 C CB  . GLN A 1 186 ? 31.356  -0.109  32.284  1.00 26.22 ? 184  GLN B CB  1 
ATOM   1390 C CG  . GLN A 1 186 ? 32.247  -1.216  31.692  1.00 25.31 ? 184  GLN B CG  1 
ATOM   1391 C CD  . GLN A 1 186 ? 33.271  -1.751  32.665  1.00 28.60 ? 184  GLN B CD  1 
ATOM   1392 O OE1 . GLN A 1 186 ? 34.183  -1.045  33.075  1.00 31.93 ? 184  GLN B OE1 1 
ATOM   1393 N NE2 . GLN A 1 186 ? 33.137  -3.017  33.044  1.00 28.05 ? 184  GLN B NE2 1 
ATOM   1394 N N   . ALA A 1 187 ? 30.177  1.529   34.759  1.00 25.28 ? 185  ALA B N   1 
ATOM   1395 C CA  . ALA A 1 187 ? 29.374  2.658   35.270  1.00 26.81 ? 185  ALA B CA  1 
ATOM   1396 C C   . ALA A 1 187 ? 28.735  3.425   34.104  1.00 22.36 ? 185  ALA B C   1 
ATOM   1397 O O   . ALA A 1 187 ? 27.622  3.959   34.283  1.00 23.43 ? 185  ALA B O   1 
ATOM   1398 C CB  . ALA A 1 187 ? 30.252  3.540   36.126  1.00 27.12 ? 185  ALA B CB  1 
ATOM   1399 N N   . ASP A 1 188 ? 29.408  3.519   32.953  1.00 23.23 ? 186  ASP B N   1 
ATOM   1400 C CA  . ASP A 1 188 ? 28.918  4.331   31.809  1.00 23.79 ? 186  ASP B CA  1 
ATOM   1401 C C   . ASP A 1 188 ? 27.775  3.630   31.071  1.00 24.24 ? 186  ASP B C   1 
ATOM   1402 O O   . ASP A 1 188 ? 27.356  4.180   30.061  1.00 23.76 ? 186  ASP B O   1 
ATOM   1403 C CB  . ASP A 1 188 ? 30.069  4.736   30.890  1.00 24.17 ? 186  ASP B CB  1 
ATOM   1404 C CG  . ASP A 1 188 ? 30.689  3.607   30.049  1.00 26.14 ? 186  ASP B CG  1 
ATOM   1405 O OD1 . ASP A 1 188 ? 30.263  2.445   30.202  1.00 24.13 ? 186  ASP B OD1 1 
ATOM   1406 O OD2 . ASP A 1 188 ? 31.610  3.897   29.287  1.00 27.02 ? 186  ASP B OD2 1 
ATOM   1407 N N   . GLY A 1 189 ? 27.292  2.471   31.544  1.00 25.54 ? 187  GLY B N   1 
ATOM   1408 C CA  . GLY A 1 189 ? 26.150  1.768   30.940  1.00 24.36 ? 187  GLY B CA  1 
ATOM   1409 C C   . GLY A 1 189 ? 26.592  0.769   29.858  1.00 25.91 ? 187  GLY B C   1 
ATOM   1410 O O   . GLY A 1 189 ? 25.709  0.058   29.316  1.00 25.84 ? 187  GLY B O   1 
ATOM   1411 N N   . SER A 1 190 ? 27.880  0.749   29.533  1.00 24.84 ? 188  SER B N   1 
ATOM   1412 C CA  . SER A 1 190 ? 28.483  -0.224  28.586  1.00 24.77 ? 188  SER B CA  1 
ATOM   1413 C C   . SER A 1 190 ? 28.883  -1.475  29.362  1.00 26.06 ? 188  SER B C   1 
ATOM   1414 O O   . SER A 1 190 ? 28.712  -1.527  30.594  1.00 25.30 ? 188  SER B O   1 
ATOM   1415 C CB  . SER A 1 190 ? 29.643  0.357   27.843  1.00 23.38 ? 188  SER B CB  1 
ATOM   1416 O OG  . SER A 1 190 ? 30.823  0.446   28.635  1.00 24.73 ? 188  SER B OG  1 
ATOM   1417 N N   . TYR A 1 191 ? 29.427  -2.461  28.652  1.00 23.24 ? 189  TYR B N   1 
ATOM   1418 C CA  . TYR A 1 191 ? 29.865  -3.750  29.243  1.00 23.15 ? 189  TYR B CA  1 
ATOM   1419 C C   . TYR A 1 191 ? 31.277  -3.999  28.752  1.00 24.26 ? 189  TYR B C   1 
ATOM   1420 O O   . TYR A 1 191 ? 31.637  -3.547  27.621  1.00 25.58 ? 189  TYR B O   1 
ATOM   1421 C CB  . TYR A 1 191 ? 28.883  -4.864  28.856  1.00 23.00 ? 189  TYR B CB  1 
ATOM   1422 C CG  . TYR A 1 191 ? 27.501  -4.623  29.400  1.00 22.81 ? 189  TYR B CG  1 
ATOM   1423 C CD1 . TYR A 1 191 ? 26.645  -3.741  28.771  1.00 22.03 ? 189  TYR B CD1 1 
ATOM   1424 C CD2 . TYR A 1 191 ? 27.080  -5.213  30.576  1.00 23.23 ? 189  TYR B CD2 1 
ATOM   1425 C CE1 . TYR A 1 191 ? 25.387  -3.468  29.278  1.00 24.04 ? 189  TYR B CE1 1 
ATOM   1426 C CE2 . TYR A 1 191 ? 25.825  -4.953  31.102  1.00 26.66 ? 189  TYR B CE2 1 
ATOM   1427 C CZ  . TYR A 1 191 ? 24.976  -4.076  30.451  1.00 24.53 ? 189  TYR B CZ  1 
ATOM   1428 O OH  . TYR A 1 191 ? 23.741  -3.804  30.942  1.00 31.72 ? 189  TYR B OH  1 
ATOM   1429 N N   . LYS A 1 192 ? 32.091  -4.633  29.583  1.00 25.47 ? 190  LYS B N   1 
ATOM   1430 C CA  . LYS A 1 192 ? 33.414  -5.122  29.128  1.00 25.38 ? 190  LYS B CA  1 
ATOM   1431 C C   . LYS A 1 192 ? 33.277  -6.635  28.890  1.00 24.93 ? 190  LYS B C   1 
ATOM   1432 O O   . LYS A 1 192 ? 32.907  -7.378  29.820  1.00 24.31 ? 190  LYS B O   1 
ATOM   1433 C CB  . LYS A 1 192 ? 34.526  -4.750  30.100  1.00 28.69 ? 190  LYS B CB  1 
ATOM   1434 C CG  . LYS A 1 192 ? 35.118  -3.384  29.804  1.00 31.45 ? 190  LYS B CG  1 
ATOM   1435 C CD  . LYS A 1 192 ? 36.240  -2.936  30.679  1.00 34.61 ? 190  LYS B CD  1 
ATOM   1436 C CE  . LYS A 1 192 ? 36.612  -1.508  30.330  1.00 35.68 ? 190  LYS B CE  1 
ATOM   1437 N NZ  . LYS A 1 192 ? 37.782  -1.034  31.106  1.00 38.93 ? 190  LYS B NZ  1 
ATOM   1438 N N   . VAL A 1 193 ? 33.531  -7.041  27.653  1.00 23.74 ? 191  VAL B N   1 
ATOM   1439 C CA  . VAL A 1 193 ? 33.235  -8.420  27.176  1.00 22.21 ? 191  VAL B CA  1 
ATOM   1440 C C   . VAL A 1 193 ? 34.563  -9.172  27.109  1.00 20.11 ? 191  VAL B C   1 
ATOM   1441 O O   . VAL A 1 193 ? 35.506  -8.728  26.434  1.00 23.74 ? 191  VAL B O   1 
ATOM   1442 C CB  . VAL A 1 193 ? 32.506  -8.415  25.811  1.00 22.44 ? 191  VAL B CB  1 
ATOM   1443 C CG1 . VAL A 1 193 ? 32.250  -9.850  25.339  1.00 22.69 ? 191  VAL B CG1 1 
ATOM   1444 C CG2 . VAL A 1 193 ? 31.202  -7.636  25.840  1.00 23.54 ? 191  VAL B CG2 1 
ATOM   1445 N N   . THR A 1 194 ? 34.638  -10.292 27.810  1.00 22.79 ? 192  THR B N   1 
ATOM   1446 C CA  . THR A 1 194 ? 35.869  -11.110 27.920  1.00 23.16 ? 192  THR B CA  1 
ATOM   1447 C C   . THR A 1 194 ? 35.531  -12.578 27.614  1.00 21.76 ? 192  THR B C   1 
ATOM   1448 O O   . THR A 1 194 ? 34.685  -13.182 28.310  1.00 21.86 ? 192  THR B O   1 
ATOM   1449 C CB  . THR A 1 194 ? 36.531  -11.024 29.304  1.00 26.30 ? 192  THR B CB  1 
ATOM   1450 O OG1 . THR A 1 194 ? 36.969  -9.681  29.528  1.00 27.87 ? 192  THR B OG1 1 
ATOM   1451 C CG2 . THR A 1 194 ? 37.736  -11.939 29.395  1.00 26.50 ? 192  THR B CG2 1 
ATOM   1452 N N   . GLY A 1 195 ? 36.204  -13.116 26.602  1.00 23.67 ? 193  GLY B N   1 
ATOM   1453 C CA  . GLY A 1 195 ? 36.056  -14.538 26.247  1.00 24.44 ? 193  GLY B CA  1 
ATOM   1454 C C   . GLY A 1 195 ? 36.597  -14.810 24.866  1.00 25.28 ? 193  GLY B C   1 
ATOM   1455 O O   . GLY A 1 195 ? 36.895  -13.875 24.133  1.00 23.77 ? 193  GLY B O   1 
ATOM   1456 N N   . THR A 1 196 ? 36.761  -16.088 24.542  1.00 22.66 ? 194  THR B N   1 
ATOM   1457 C CA  . THR A 1 196 ? 37.245  -16.522 23.216  1.00 23.15 ? 194  THR B CA  1 
ATOM   1458 C C   . THR A 1 196 ? 36.049  -17.144 22.476  1.00 22.30 ? 194  THR B C   1 
ATOM   1459 O O   . THR A 1 196 ? 35.410  -18.052 23.022  1.00 21.07 ? 194  THR B O   1 
ATOM   1460 C CB  . THR A 1 196 ? 38.437  -17.474 23.365  1.00 23.43 ? 194  THR B CB  1 
ATOM   1461 O OG1 . THR A 1 196 ? 39.522  -16.737 23.916  1.00 27.40 ? 194  THR B OG1 1 
ATOM   1462 C CG2 . THR A 1 196 ? 38.878  -18.048 22.039  1.00 23.46 ? 194  THR B CG2 1 
ATOM   1463 N N   . LYS A 1 197 ? 35.755  -16.626 21.285  1.00 20.34 ? 195  LYS B N   1 
ATOM   1464 C CA  . LYS A 1 197 ? 34.763  -17.203 20.355  1.00 20.91 ? 195  LYS B CA  1 
ATOM   1465 C C   . LYS A 1 197 ? 35.555  -17.894 19.241  1.00 18.93 ? 195  LYS B C   1 
ATOM   1466 O O   . LYS A 1 197 ? 36.652  -17.426 18.873  1.00 20.80 ? 195  LYS B O   1 
ATOM   1467 C CB  . LYS A 1 197 ? 33.825  -16.106 19.851  1.00 21.90 ? 195  LYS B CB  1 
ATOM   1468 C CG  . LYS A 1 197 ? 32.988  -15.451 20.949  1.00 20.31 ? 195  LYS B CG  1 
ATOM   1469 C CD  . LYS A 1 197 ? 32.000  -16.375 21.629  1.00 21.02 ? 195  LYS B CD  1 
ATOM   1470 C CE  . LYS A 1 197 ? 30.913  -15.642 22.389  1.00 20.66 ? 195  LYS B CE  1 
ATOM   1471 N NZ  . LYS A 1 197 ? 29.972  -16.534 23.110  1.00 21.12 ? 195  LYS B NZ  1 
ATOM   1472 N N   . ILE A 1 198 ? 35.061  -19.021 18.760  1.00 19.15 ? 196  ILE B N   1 
ATOM   1473 C CA  . ILE A 1 198 ? 35.723  -19.731 17.633  1.00 19.36 ? 196  ILE B CA  1 
ATOM   1474 C C   . ILE A 1 198 ? 34.762  -19.826 16.455  1.00 18.98 ? 196  ILE B C   1 
ATOM   1475 O O   . ILE A 1 198 ? 33.553  -19.634 16.639  1.00 20.86 ? 196  ILE B O   1 
ATOM   1476 C CB  . ILE A 1 198 ? 36.235  -21.133 18.042  1.00 21.32 ? 196  ILE B CB  1 
ATOM   1477 C CG1 . ILE A 1 198 ? 35.107  -22.100 18.373  1.00 21.49 ? 196  ILE B CG1 1 
ATOM   1478 C CG2 . ILE A 1 198 ? 37.249  -21.016 19.170  1.00 22.59 ? 196  ILE B CG2 1 
ATOM   1479 C CD1 . ILE A 1 198 ? 35.559  -23.568 18.333  1.00 22.84 ? 196  ILE B CD1 1 
ATOM   1480 N N   . PHE A 1 199 ? 35.330  -20.137 15.292  1.00 19.79 ? 197  PHE B N   1 
ATOM   1481 C CA  . PHE A 1 199 ? 34.585  -20.379 14.035  1.00 19.61 ? 197  PHE B CA  1 
ATOM   1482 C C   . PHE A 1 199 ? 33.752  -19.136 13.708  1.00 18.64 ? 197  PHE B C   1 
ATOM   1483 O O   . PHE A 1 199 ? 32.584  -19.249 13.307  1.00 19.70 ? 197  PHE B O   1 
ATOM   1484 C CB  . PHE A 1 199 ? 33.714  -21.629 14.200  1.00 21.28 ? 197  PHE B CB  1 
ATOM   1485 C CG  . PHE A 1 199 ? 34.433  -22.930 14.464  1.00 19.50 ? 197  PHE B CG  1 
ATOM   1486 C CD1 . PHE A 1 199 ? 35.772  -23.092 14.180  1.00 20.81 ? 197  PHE B CD1 1 
ATOM   1487 C CD2 . PHE A 1 199 ? 33.728  -24.012 14.979  1.00 22.26 ? 197  PHE B CD2 1 
ATOM   1488 C CE1 . PHE A 1 199 ? 36.388  -24.315 14.372  1.00 21.34 ? 197  PHE B CE1 1 
ATOM   1489 C CE2 . PHE A 1 199 ? 34.340  -25.241 15.165  1.00 20.95 ? 197  PHE B CE2 1 
ATOM   1490 C CZ  . PHE A 1 199 ? 35.673  -25.375 14.877  1.00 22.03 ? 197  PHE B CZ  1 
ATOM   1491 N N   . ILE A 1 200 ? 34.315  -17.951 13.958  1.00 18.23 ? 198  ILE B N   1 
ATOM   1492 C CA  . ILE A 1 200 ? 33.626  -16.682 13.602  1.00 17.70 ? 198  ILE B CA  1 
ATOM   1493 C C   . ILE A 1 200 ? 33.906  -16.408 12.143  1.00 16.79 ? 198  ILE B C   1 
ATOM   1494 O O   . ILE A 1 200 ? 35.028  -15.985 11.777  1.00 16.94 ? 198  ILE B O   1 
ATOM   1495 C CB  . ILE A 1 200 ? 34.036  -15.510 14.494  1.00 19.06 ? 198  ILE B CB  1 
ATOM   1496 C CG1 . ILE A 1 200 ? 33.859  -15.891 15.957  1.00 19.64 ? 198  ILE B CG1 1 
ATOM   1497 C CG2 . ILE A 1 200 ? 33.245  -14.273 14.102  1.00 19.36 ? 198  ILE B CG2 1 
ATOM   1498 C CD1 . ILE A 1 200 ? 32.514  -16.483 16.254  1.00 21.35 ? 198  ILE B CD1 1 
ATOM   1499 N N   . SER A 1 201 ? 32.880  -16.654 11.323  1.00 17.20 ? 199  SER B N   1 
ATOM   1500 C CA  . SER A 1 201 ? 32.955  -16.362 9.879   1.00 16.85 ? 199  SER B CA  1 
ATOM   1501 C C   . SER A 1 201 ? 33.130  -14.849 9.696   1.00 16.47 ? 199  SER B C   1 
ATOM   1502 O O   . SER A 1 201 ? 32.355  -14.119 10.321  1.00 17.23 ? 199  SER B O   1 
ATOM   1503 C CB  . SER A 1 201 ? 31.715  -16.895 9.184   1.00 17.90 ? 199  SER B CB  1 
ATOM   1504 O OG  . SER A 1 201 ? 31.739  -18.341 9.213   1.00 20.20 ? 199  SER B OG  1 
ATOM   1505 N N   . ALA A 1 202 ? 34.107  -14.414 8.898   1.00 17.37 ? 200  ALA B N   1 
ATOM   1506 C CA  . ALA A 1 202 ? 34.361  -12.982 8.611   1.00 17.09 ? 200  ALA B CA  1 
ATOM   1507 C C   . ALA A 1 202 ? 34.680  -12.224 9.912   1.00 18.50 ? 200  ALA B C   1 
ATOM   1508 O O   . ALA A 1 202 ? 34.492  -10.976 9.941   1.00 18.25 ? 200  ALA B O   1 
ATOM   1509 C CB  . ALA A 1 202 ? 33.194  -12.413 7.860   1.00 16.92 ? 200  ALA B CB  1 
ATOM   1510 N N   . GLY A 1 203 ? 35.255  -12.893 10.907  1.00 18.37 ? 201  GLY B N   1 
ATOM   1511 C CA  . GLY A 1 203 ? 35.604  -12.251 12.196  1.00 19.32 ? 201  GLY B CA  1 
ATOM   1512 C C   . GLY A 1 203 ? 36.621  -11.136 12.005  1.00 19.91 ? 201  GLY B C   1 
ATOM   1513 O O   . GLY A 1 203 ? 36.524  -10.120 12.699  1.00 21.92 ? 201  GLY B O   1 
ATOM   1514 N N   . GLU A 1 204 ? 37.559  -11.310 11.101  1.00 18.40 ? 202  GLU B N   1 
ATOM   1515 C CA  . GLU A 1 204 ? 38.639  -10.337 10.802  1.00 19.10 ? 202  GLU B CA  1 
ATOM   1516 C C   . GLU A 1 204 ? 38.915  -10.432 9.306   1.00 19.46 ? 202  GLU B C   1 
ATOM   1517 O O   . GLU A 1 204 ? 38.928  -11.587 8.750   1.00 20.60 ? 202  GLU B O   1 
ATOM   1518 C CB  . GLU A 1 204 ? 39.862  -10.664 11.660  1.00 18.93 ? 202  GLU B CB  1 
ATOM   1519 C CG  . GLU A 1 204 ? 41.028  -9.738  11.437  1.00 20.43 ? 202  GLU B CG  1 
ATOM   1520 C CD  . GLU A 1 204 ? 40.708  -8.297  11.817  1.00 23.84 ? 202  GLU B CD  1 
ATOM   1521 O OE1 . GLU A 1 204 ? 40.063  -7.596  11.003  1.00 22.08 ? 202  GLU B OE1 1 
ATOM   1522 O OE2 . GLU A 1 204 ? 41.107  -7.892  12.920  1.00 26.15 ? 202  GLU B OE2 1 
ATOM   1523 N N   . HIS A 1 205 ? 39.118  -9.302  8.646   1.00 17.86 ? 203  HIS B N   1 
ATOM   1524 C CA  . HIS A 1 205 ? 39.408  -9.263  7.199   1.00 18.27 ? 203  HIS B CA  1 
ATOM   1525 C C   . HIS A 1 205 ? 39.729  -7.822  6.824   1.00 19.47 ? 203  HIS B C   1 
ATOM   1526 O O   . HIS A 1 205 ? 39.637  -6.947  7.706   1.00 21.28 ? 203  HIS B O   1 
ATOM   1527 C CB  . HIS A 1 205 ? 38.221  -9.802  6.392   1.00 19.46 ? 203  HIS B CB  1 
ATOM   1528 C CG  . HIS A 1 205 ? 36.972  -9.011  6.596   1.00 19.81 ? 203  HIS B CG  1 
ATOM   1529 N ND1 . HIS A 1 205 ? 36.738  -7.820  5.933   1.00 20.22 ? 203  HIS B ND1 1 
ATOM   1530 C CD2 . HIS A 1 205 ? 35.890  -9.236  7.381   1.00 18.83 ? 203  HIS B CD2 1 
ATOM   1531 C CE1 . HIS A 1 205 ? 35.547  -7.352  6.294   1.00 20.51 ? 203  HIS B CE1 1 
ATOM   1532 N NE2 . HIS A 1 205 ? 34.993  -8.213  7.163   1.00 19.75 ? 203  HIS B NE2 1 
ATOM   1533 N N   . ASP A 1 206 ? 40.092  -7.625  5.575   1.00 18.51 ? 204  ASP B N   1 
ATOM   1534 C CA  . ASP A 1 206 ? 40.664  -6.344  5.087   1.00 20.83 ? 204  ASP B CA  1 
ATOM   1535 C C   . ASP A 1 206 ? 39.719  -5.659  4.099   1.00 22.77 ? 204  ASP B C   1 
ATOM   1536 O O   . ASP A 1 206 ? 40.224  -4.881  3.297   1.00 23.54 ? 204  ASP B O   1 
ATOM   1537 C CB  . ASP A 1 206 ? 42.008  -6.638  4.429   1.00 22.32 ? 204  ASP B CB  1 
ATOM   1538 C CG  . ASP A 1 206 ? 41.919  -7.619  3.265   1.00 22.52 ? 204  ASP B CG  1 
ATOM   1539 O OD1 . ASP A 1 206 ? 40.789  -8.132  3.030   1.00 20.43 ? 204  ASP B OD1 1 
ATOM   1540 O OD2 . ASP A 1 206 ? 42.945  -7.828  2.583   1.00 24.44 ? 204  ASP B OD2 1 
ATOM   1541 N N   . MET A 1 207 ? 38.430  -5.968  4.119   1.00 20.09 ? 205  MET B N   1 
ATOM   1542 C CA  . MET A 1 207 ? 37.492  -5.557  3.049   1.00 22.76 ? 205  MET B CA  1 
ATOM   1543 C C   . MET A 1 207 ? 36.693  -4.299  3.426   1.00 22.88 ? 205  MET B C   1 
ATOM   1544 O O   . MET A 1 207 ? 36.133  -3.717  2.500   1.00 23.36 ? 205  MET B O   1 
ATOM   1545 C CB  . MET A 1 207 ? 36.528  -6.699  2.709   1.00 24.06 ? 205  MET B CB  1 
ATOM   1546 C CG  . MET A 1 207 ? 37.258  -7.972  2.449   1.00 25.37 ? 205  MET B CG  1 
ATOM   1547 S SD  . MET A 1 207 ? 36.567  -8.755  1.020   1.00 27.34 ? 205  MET B SD  1 
ATOM   1548 C CE  . MET A 1 207 ? 34.835  -8.892  1.452   1.00 27.81 ? 205  MET B CE  1 
ATOM   1549 N N   . ALA A 1 208 ? 36.618  -3.912  4.706   1.00 22.16 ? 206  ALA B N   1 
ATOM   1550 C CA  . ALA A 1 208 ? 35.692  -2.849  5.168   1.00 23.13 ? 206  ALA B CA  1 
ATOM   1551 C C   . ALA A 1 208 ? 36.402  -1.857  6.103   1.00 23.73 ? 206  ALA B C   1 
ATOM   1552 O O   . ALA A 1 208 ? 37.573  -1.994  6.364   1.00 23.67 ? 206  ALA B O   1 
ATOM   1553 C CB  . ALA A 1 208 ? 34.485  -3.457  5.839   1.00 23.05 ? 206  ALA B CB  1 
ATOM   1554 N N   . ASP A 1 209 ? 35.665  -0.871  6.590   1.00 24.48 ? 207  ASP B N   1 
ATOM   1555 C CA  . ASP A 1 209 ? 36.207  0.192   7.477   1.00 25.06 ? 207  ASP B CA  1 
ATOM   1556 C C   . ASP A 1 209 ? 36.036  -0.182  8.948   1.00 25.92 ? 207  ASP B C   1 
ATOM   1557 O O   . ASP A 1 209 ? 36.749  0.400   9.782   1.00 27.44 ? 207  ASP B O   1 
ATOM   1558 C CB  . ASP A 1 209 ? 35.470  1.509   7.244   1.00 25.39 ? 207  ASP B CB  1 
ATOM   1559 C CG  . ASP A 1 209 ? 35.705  2.086   5.866   1.00 30.94 ? 207  ASP B CG  1 
ATOM   1560 O OD1 . ASP A 1 209 ? 36.792  1.858   5.324   1.00 30.95 ? 207  ASP B OD1 1 
ATOM   1561 O OD2 . ASP A 1 209 ? 34.805  2.811   5.381   1.00 36.71 ? 207  ASP B OD2 1 
ATOM   1562 N N   . ASN A 1 210 ? 35.142  -1.130  9.256   1.00 23.40 ? 208  ASN B N   1 
ATOM   1563 C CA  . ASN A 1 210 ? 34.890  -1.597  10.635  1.00 21.38 ? 208  ASN B CA  1 
ATOM   1564 C C   . ASN A 1 210 ? 34.150  -2.931  10.545  1.00 22.40 ? 208  ASN B C   1 
ATOM   1565 O O   . ASN A 1 210 ? 33.535  -3.231  9.482   1.00 19.29 ? 208  ASN B O   1 
ATOM   1566 C CB  . ASN A 1 210 ? 34.073  -0.577  11.434  1.00 22.55 ? 208  ASN B CB  1 
ATOM   1567 C CG  . ASN A 1 210 ? 34.221  -0.644  12.941  1.00 22.30 ? 208  ASN B CG  1 
ATOM   1568 O OD1 . ASN A 1 210 ? 34.859  -1.543  13.479  1.00 20.44 ? 208  ASN B OD1 1 
ATOM   1569 N ND2 . ASN A 1 210 ? 33.563  0.280   13.642  1.00 22.23 ? 208  ASN B ND2 1 
ATOM   1570 N N   . ILE A 1 211 ? 34.179  -3.652  11.644  1.00 19.65 ? 209  ILE B N   1 
ATOM   1571 C CA  . ILE A 1 211 ? 33.447  -4.929  11.808  1.00 20.22 ? 209  ILE B CA  1 
ATOM   1572 C C   . ILE A 1 211 ? 32.611  -4.830  13.073  1.00 20.02 ? 209  ILE B C   1 
ATOM   1573 O O   . ILE A 1 211 ? 33.169  -4.527  14.166  1.00 23.50 ? 209  ILE B O   1 
ATOM   1574 C CB  . ILE A 1 211 ? 34.383  -6.144  11.846  1.00 18.16 ? 209  ILE B CB  1 
ATOM   1575 C CG1 . ILE A 1 211 ? 35.158  -6.280  10.538  1.00 19.06 ? 209  ILE B CG1 1 
ATOM   1576 C CG2 . ILE A 1 211 ? 33.522  -7.371  12.151  1.00 18.67 ? 209  ILE B CG2 1 
ATOM   1577 C CD1 . ILE A 1 211 ? 36.356  -7.228  10.579  1.00 18.80 ? 209  ILE B CD1 1 
ATOM   1578 N N   . VAL A 1 212 ? 31.327  -5.116  12.943  1.00 20.74 ? 210  VAL B N   1 
ATOM   1579 C CA  . VAL A 1 212 ? 30.371  -5.049  14.064  1.00 19.37 ? 210  VAL B CA  1 
ATOM   1580 C C   . VAL A 1 212 ? 30.078  -6.492  14.478  1.00 20.26 ? 210  VAL B C   1 
ATOM   1581 O O   . VAL A 1 212 ? 29.329  -7.182  13.793  1.00 20.99 ? 210  VAL B O   1 
ATOM   1582 C CB  . VAL A 1 212 ? 29.119  -4.262  13.634  1.00 22.16 ? 210  VAL B CB  1 
ATOM   1583 C CG1 . VAL A 1 212 ? 28.128  -4.121  14.772  1.00 21.86 ? 210  VAL B CG1 1 
ATOM   1584 C CG2 . VAL A 1 212 ? 29.505  -2.916  13.053  1.00 23.41 ? 210  VAL B CG2 1 
ATOM   1585 N N   . HIS A 1 213 ? 30.630  -6.921  15.602  1.00 19.91 ? 211  HIS B N   1 
ATOM   1586 C CA  . HIS A 1 213 ? 30.363  -8.268  16.148  1.00 21.27 ? 211  HIS B CA  1 
ATOM   1587 C C   . HIS A 1 213 ? 29.077  -8.230  16.953  1.00 21.25 ? 211  HIS B C   1 
ATOM   1588 O O   . HIS A 1 213 ? 28.920  -7.329  17.821  1.00 20.87 ? 211  HIS B O   1 
ATOM   1589 C CB  . HIS A 1 213 ? 31.508  -8.730  17.040  1.00 18.72 ? 211  HIS B CB  1 
ATOM   1590 C CG  . HIS A 1 213 ? 32.793  -8.739  16.329  1.00 20.60 ? 211  HIS B CG  1 
ATOM   1591 N ND1 . HIS A 1 213 ? 33.111  -9.729  15.422  1.00 20.66 ? 211  HIS B ND1 1 
ATOM   1592 C CD2 . HIS A 1 213 ? 33.835  -7.891  16.350  1.00 20.87 ? 211  HIS B CD2 1 
ATOM   1593 C CE1 . HIS A 1 213 ? 34.312  -9.500  14.945  1.00 20.17 ? 211  HIS B CE1 1 
ATOM   1594 N NE2 . HIS A 1 213 ? 34.779  -8.366  15.495  1.00 20.79 ? 211  HIS B NE2 1 
ATOM   1595 N N   . ILE A 1 214 ? 28.200  -9.202  16.730  1.00 19.07 ? 212  ILE B N   1 
ATOM   1596 C CA  . ILE A 1 214 ? 26.992  -9.406  17.561  1.00 19.53 ? 212  ILE B CA  1 
ATOM   1597 C C   . ILE A 1 214 ? 27.251  -10.639 18.417  1.00 21.84 ? 212  ILE B C   1 
ATOM   1598 O O   . ILE A 1 214 ? 27.410  -11.737 17.831  1.00 20.16 ? 212  ILE B O   1 
ATOM   1599 C CB  . ILE A 1 214 ? 25.734  -9.540  16.691  1.00 20.13 ? 212  ILE B CB  1 
ATOM   1600 C CG1 . ILE A 1 214 ? 25.585  -8.400  15.681  1.00 20.62 ? 212  ILE B CG1 1 
ATOM   1601 C CG2 . ILE A 1 214 ? 24.520  -9.725  17.554  1.00 21.24 ? 212  ILE B CG2 1 
ATOM   1602 C CD1 . ILE A 1 214 ? 25.500  -6.997  16.296  1.00 20.96 ? 212  ILE B CD1 1 
ATOM   1603 N N   . VAL A 1 215 ? 27.350  -10.453 19.734  1.00 19.38 ? 213  VAL B N   1 
ATOM   1604 C CA  . VAL A 1 215 ? 28.083  -11.409 20.613  1.00 20.57 ? 213  VAL B CA  1 
ATOM   1605 C C   . VAL A 1 215 ? 27.161  -11.900 21.714  1.00 21.69 ? 213  VAL B C   1 
ATOM   1606 O O   . VAL A 1 215 ? 26.555  -11.046 22.398  1.00 21.80 ? 213  VAL B O   1 
ATOM   1607 C CB  . VAL A 1 215 ? 29.354  -10.767 21.214  1.00 20.01 ? 213  VAL B CB  1 
ATOM   1608 C CG1 . VAL A 1 215 ? 30.127  -11.763 22.057  1.00 20.14 ? 213  VAL B CG1 1 
ATOM   1609 C CG2 . VAL A 1 215 ? 30.238  -10.178 20.143  1.00 20.90 ? 213  VAL B CG2 1 
ATOM   1610 N N   . LEU A 1 216 ? 27.114  -13.217 21.942  1.00 20.01 ? 214  LEU B N   1 
ATOM   1611 C CA  . LEU A 1 216 ? 26.388  -13.822 23.085  1.00 19.65 ? 214  LEU B CA  1 
ATOM   1612 C C   . LEU A 1 216 ? 27.323  -13.892 24.288  1.00 21.93 ? 214  LEU B C   1 
ATOM   1613 O O   . LEU A 1 216 ? 28.440  -14.417 24.161  1.00 20.84 ? 214  LEU B O   1 
ATOM   1614 C CB  . LEU A 1 216 ? 25.857  -15.215 22.717  1.00 21.51 ? 214  LEU B CB  1 
ATOM   1615 C CG  . LEU A 1 216 ? 24.609  -15.236 21.843  1.00 24.49 ? 214  LEU B CG  1 
ATOM   1616 C CD1 . LEU A 1 216 ? 24.270  -16.667 21.432  1.00 25.89 ? 214  LEU B CD1 1 
ATOM   1617 C CD2 . LEU A 1 216 ? 23.431  -14.596 22.561  1.00 26.37 ? 214  LEU B CD2 1 
ATOM   1618 N N   . ALA A 1 217 ? 26.913  -13.330 25.420  1.00 20.96 ? 215  ALA B N   1 
ATOM   1619 C CA  . ALA A 1 217 ? 27.731  -13.333 26.655  1.00 21.14 ? 215  ALA B CA  1 
ATOM   1620 C C   . ALA A 1 217 ? 26.804  -13.344 27.881  1.00 22.90 ? 215  ALA B C   1 
ATOM   1621 O O   . ALA A 1 217 ? 25.578  -13.131 27.727  1.00 26.22 ? 215  ALA B O   1 
ATOM   1622 C CB  . ALA A 1 217 ? 28.680  -12.165 26.661  1.00 20.71 ? 215  ALA B CB  1 
ATOM   1623 N N   . ARG A 1 218 ? 27.379  -13.597 29.057  1.00 24.78 ? 216  ARG B N   1 
ATOM   1624 C CA  . ARG A 1 218 ? 26.618  -13.785 30.326  1.00 26.41 ? 216  ARG B CA  1 
ATOM   1625 C C   . ARG A 1 218 ? 26.877  -12.586 31.246  1.00 23.27 ? 216  ARG B C   1 
ATOM   1626 O O   . ARG A 1 218 ? 28.042  -12.286 31.468  1.00 26.36 ? 216  ARG B O   1 
ATOM   1627 C CB  . ARG A 1 218 ? 27.071  -15.003 31.133  1.00 31.03 ? 216  ARG B CB  1 
ATOM   1628 C CG  . ARG A 1 218 ? 27.233  -16.310 30.381  1.00 35.70 ? 216  ARG B CG  1 
ATOM   1629 C CD  . ARG A 1 218 ? 27.337  -17.437 31.404  1.00 36.34 ? 216  ARG B CD  1 
ATOM   1630 N NE  . ARG A 1 218 ? 25.998  -17.743 31.857  1.00 37.08 ? 216  ARG B NE  1 
ATOM   1631 C CZ  . ARG A 1 218 ? 25.149  -18.550 31.213  1.00 37.39 ? 216  ARG B CZ  1 
ATOM   1632 N NH1 . ARG A 1 218 ? 23.925  -18.694 31.676  1.00 37.03 ? 216  ARG B NH1 1 
ATOM   1633 N NH2 . ARG A 1 218 ? 25.518  -19.206 30.109  1.00 39.35 ? 216  ARG B NH2 1 
ATOM   1634 N N   . LEU A 1 219 ? 25.811  -11.946 31.712  1.00 26.98 ? 217  LEU B N   1 
ATOM   1635 C CA  . LEU A 1 219 ? 25.852  -10.942 32.816  1.00 29.58 ? 217  LEU B CA  1 
ATOM   1636 C C   . LEU A 1 219 ? 26.231  -11.644 34.115  1.00 31.58 ? 217  LEU B C   1 
ATOM   1637 O O   . LEU A 1 219 ? 25.957  -12.833 34.279  1.00 28.63 ? 217  LEU B O   1 
ATOM   1638 C CB  . LEU A 1 219 ? 24.484  -10.267 32.933  1.00 30.14 ? 217  LEU B CB  1 
ATOM   1639 C CG  . LEU A 1 219 ? 24.071  -9.449  31.714  1.00 29.95 ? 217  LEU B CG  1 
ATOM   1640 C CD1 . LEU A 1 219 ? 22.613  -8.971  31.783  1.00 32.60 ? 217  LEU B CD1 1 
ATOM   1641 C CD2 . LEU A 1 219 ? 25.019  -8.285  31.523  1.00 30.32 ? 217  LEU B CD2 1 
ATOM   1642 N N   . PRO A 1 220 ? 26.914  -10.947 35.056  1.00 34.50 ? 218  PRO B N   1 
ATOM   1643 C CA  . PRO A 1 220 ? 27.235  -11.530 36.364  1.00 38.08 ? 218  PRO B CA  1 
ATOM   1644 C C   . PRO A 1 220 ? 25.933  -11.911 37.077  1.00 33.61 ? 218  PRO B C   1 
ATOM   1645 O O   . PRO A 1 220 ? 24.957  -11.207 36.932  1.00 35.61 ? 218  PRO B O   1 
ATOM   1646 C CB  . PRO A 1 220 ? 28.001  -10.412 37.104  1.00 38.14 ? 218  PRO B CB  1 
ATOM   1647 C CG  . PRO A 1 220 ? 28.455  -9.460  36.009  1.00 36.57 ? 218  PRO B CG  1 
ATOM   1648 C CD  . PRO A 1 220 ? 27.371  -9.552  34.951  1.00 35.75 ? 218  PRO B CD  1 
ATOM   1649 N N   . ASP A 1 221 ? 25.927  -13.066 37.733  1.00 38.99 ? 219  ASP B N   1 
ATOM   1650 C CA  . ASP A 1 221 ? 24.772  -13.585 38.508  1.00 42.57 ? 219  ASP B CA  1 
ATOM   1651 C C   . ASP A 1 221 ? 23.523  -13.683 37.624  1.00 41.81 ? 219  ASP B C   1 
ATOM   1652 O O   . ASP A 1 221 ? 22.428  -13.463 38.162  1.00 42.12 ? 219  ASP B O   1 
ATOM   1653 C CB  . ASP A 1 221 ? 24.491  -12.703 39.727  1.00 45.63 ? 219  ASP B CB  1 
ATOM   1654 C CG  . ASP A 1 221 ? 25.750  -12.230 40.427  1.00 48.86 ? 219  ASP B CG  1 
ATOM   1655 O OD1 . ASP A 1 221 ? 26.483  -13.093 40.947  1.00 48.58 ? 219  ASP B OD1 1 
ATOM   1656 O OD2 . ASP A 1 221 ? 26.006  -11.001 40.406  1.00 56.75 ? 219  ASP B OD2 1 
ATOM   1657 N N   . ALA A 1 222 ? 23.663  -13.997 36.328  1.00 37.22 ? 220  ALA B N   1 
ATOM   1658 C CA  . ALA A 1 222 ? 22.517  -14.368 35.459  1.00 37.27 ? 220  ALA B CA  1 
ATOM   1659 C C   . ALA A 1 222 ? 22.108  -15.820 35.745  1.00 36.56 ? 220  ALA B C   1 
ATOM   1660 O O   . ALA A 1 222 ? 22.904  -16.606 36.248  1.00 39.38 ? 220  ALA B O   1 
ATOM   1661 C CB  . ALA A 1 222 ? 22.870  -14.153 34.004  1.00 36.37 ? 220  ALA B CB  1 
ATOM   1662 N N   . PRO A 1 223 ? 20.855  -16.233 35.450  1.00 35.79 ? 221  PRO B N   1 
ATOM   1663 C CA  . PRO A 1 223 ? 20.458  -17.643 35.563  1.00 36.95 ? 221  PRO B CA  1 
ATOM   1664 C C   . PRO A 1 223 ? 21.338  -18.621 34.758  1.00 42.36 ? 221  PRO B C   1 
ATOM   1665 O O   . PRO A 1 223 ? 22.022  -18.194 33.826  1.00 39.47 ? 221  PRO B O   1 
ATOM   1666 C CB  . PRO A 1 223 ? 19.029  -17.662 34.997  1.00 37.58 ? 221  PRO B CB  1 
ATOM   1667 C CG  . PRO A 1 223 ? 18.531  -16.235 35.108  1.00 38.26 ? 221  PRO B CG  1 
ATOM   1668 C CD  . PRO A 1 223 ? 19.762  -15.364 34.994  1.00 36.19 ? 221  PRO B CD  1 
ATOM   1669 N N   . GLN A 1 224 ? 21.331  -19.904 35.152  1.00 46.27 ? 222  GLN B N   1 
ATOM   1670 C CA  . GLN A 1 224 ? 22.007  -21.034 34.453  1.00 46.14 ? 222  GLN B CA  1 
ATOM   1671 C C   . GLN A 1 224 ? 21.478  -21.149 33.021  1.00 37.86 ? 222  GLN B C   1 
ATOM   1672 O O   . GLN A 1 224 ? 20.270  -20.965 32.819  1.00 38.00 ? 222  GLN B O   1 
ATOM   1673 C CB  . GLN A 1 224 ? 21.703  -22.379 35.127  1.00 54.15 ? 222  GLN B CB  1 
ATOM   1674 C CG  . GLN A 1 224 ? 22.305  -22.540 36.515  1.00 64.64 ? 222  GLN B CG  1 
ATOM   1675 C CD  . GLN A 1 224 ? 23.801  -22.351 36.500  1.00 69.03 ? 222  GLN B CD  1 
ATOM   1676 O OE1 . GLN A 1 224 ? 24.497  -22.833 35.609  1.00 76.24 ? 222  GLN B OE1 1 
ATOM   1677 N NE2 . GLN A 1 224 ? 24.306  -21.631 37.489  1.00 75.15 ? 222  GLN B NE2 1 
ATOM   1678 N N   . GLY A 1 225 ? 22.334  -21.514 32.074  1.00 32.92 ? 223  GLY B N   1 
ATOM   1679 C CA  . GLY A 1 225 ? 21.881  -21.963 30.747  1.00 31.58 ? 223  GLY B CA  1 
ATOM   1680 C C   . GLY A 1 225 ? 21.413  -20.811 29.873  1.00 30.85 ? 223  GLY B C   1 
ATOM   1681 O O   . GLY A 1 225 ? 21.882  -19.676 30.069  1.00 30.49 ? 223  GLY B O   1 
ATOM   1682 N N   . THR A 1 226 ? 20.519  -21.103 28.933  1.00 31.97 ? 224  THR B N   1 
ATOM   1683 C CA  . THR A 1 226 ? 20.083  -20.106 27.925  1.00 32.21 ? 224  THR B CA  1 
ATOM   1684 C C   . THR A 1 226 ? 19.312  -18.946 28.563  1.00 33.32 ? 224  THR B C   1 
ATOM   1685 O O   . THR A 1 226 ? 19.235  -17.886 27.946  1.00 31.30 ? 224  THR B O   1 
ATOM   1686 C CB  . THR A 1 226 ? 19.272  -20.815 26.836  1.00 33.76 ? 224  THR B CB  1 
ATOM   1687 O OG1 . THR A 1 226 ? 18.172  -21.491 27.437  1.00 33.90 ? 224  THR B OG1 1 
ATOM   1688 C CG2 . THR A 1 226 ? 20.114  -21.788 26.040  1.00 33.54 ? 224  THR B CG2 1 
ATOM   1689 N N   . LYS A 1 227 ? 18.773  -19.160 29.756  1.00 34.25 ? 225  LYS B N   1 
ATOM   1690 C CA  . LYS A 1 227 ? 17.984  -18.107 30.439  1.00 33.74 ? 225  LYS B CA  1 
ATOM   1691 C C   . LYS A 1 227 ? 18.940  -17.070 31.037  1.00 30.38 ? 225  LYS B C   1 
ATOM   1692 O O   . LYS A 1 227 ? 18.456  -16.090 31.585  1.00 33.89 ? 225  LYS B O   1 
ATOM   1693 C CB  . LYS A 1 227 ? 17.031  -18.767 31.439  1.00 37.55 ? 225  LYS B CB  1 
ATOM   1694 C CG  . LYS A 1 227 ? 15.821  -19.428 30.794  1.00 42.37 ? 225  LYS B CG  1 
ATOM   1695 C CD  . LYS A 1 227 ? 14.916  -20.137 31.773  1.00 46.25 ? 225  LYS B CD  1 
ATOM   1696 C CE  . LYS A 1 227 ? 15.673  -20.768 32.921  1.00 51.26 ? 225  LYS B CE  1 
ATOM   1697 N NZ  . LYS A 1 227 ? 14.861  -21.790 33.624  1.00 58.88 ? 225  LYS B NZ  1 
ATOM   1698 N N   . GLY A 1 228 ? 20.239  -17.253 30.849  1.00 29.70 ? 226  GLY B N   1 
ATOM   1699 C CA  . GLY A 1 228 ? 21.236  -16.343 31.424  1.00 29.16 ? 226  GLY B CA  1 
ATOM   1700 C C   . GLY A 1 228 ? 22.083  -15.673 30.369  1.00 30.13 ? 226  GLY B C   1 
ATOM   1701 O O   . GLY A 1 228 ? 23.113  -15.116 30.744  1.00 28.36 ? 226  GLY B O   1 
ATOM   1702 N N   . ILE A 1 229 ? 21.717  -15.772 29.088  1.00 28.87 ? 227  ILE B N   1 
ATOM   1703 C CA  . ILE A 1 229 ? 22.578  -15.209 28.013  1.00 26.65 ? 227  ILE B CA  1 
ATOM   1704 C C   . ILE A 1 229 ? 21.931  -13.927 27.496  1.00 23.88 ? 227  ILE B C   1 
ATOM   1705 O O   . ILE A 1 229 ? 20.696  -13.874 27.382  1.00 26.62 ? 227  ILE B O   1 
ATOM   1706 C CB  . ILE A 1 229 ? 22.913  -16.225 26.893  1.00 31.10 ? 227  ILE B CB  1 
ATOM   1707 C CG1 . ILE A 1 229 ? 21.691  -16.731 26.131  1.00 34.43 ? 227  ILE B CG1 1 
ATOM   1708 C CG2 . ILE A 1 229 ? 23.719  -17.383 27.467  1.00 31.98 ? 227  ILE B CG2 1 
ATOM   1709 C CD1 . ILE A 1 229 ? 22.059  -17.658 24.973  1.00 38.03 ? 227  ILE B CD1 1 
ATOM   1710 N N   . SER A 1 230 ? 22.791  -12.961 27.220  1.00 23.16 ? 228  SER B N   1 
ATOM   1711 C CA  . SER A 1 230 ? 22.480  -11.617 26.700  1.00 22.47 ? 228  SER B CA  1 
ATOM   1712 C C   . SER A 1 230 ? 23.286  -11.369 25.425  1.00 23.06 ? 228  SER B C   1 
ATOM   1713 O O   . SER A 1 230 ? 24.338  -12.051 25.184  1.00 21.96 ? 228  SER B O   1 
ATOM   1714 C CB  . SER A 1 230 ? 22.790  -10.580 27.770  1.00 24.28 ? 228  SER B CB  1 
ATOM   1715 O OG  . SER A 1 230 ? 21.991  -10.805 28.946  1.00 24.95 ? 228  SER B OG  1 
ATOM   1716 N N   . LEU A 1 231 ? 22.847  -10.369 24.668  1.00 23.12 ? 229  LEU B N   1 
ATOM   1717 C CA  . LEU A 1 231 ? 23.382  -10.044 23.335  1.00 21.79 ? 229  LEU B CA  1 
ATOM   1718 C C   . LEU A 1 231 ? 24.077  -8.684  23.405  1.00 22.75 ? 229  LEU B C   1 
ATOM   1719 O O   . LEU A 1 231 ? 23.513  -7.790  24.046  1.00 23.57 ? 229  LEU B O   1 
ATOM   1720 C CB  . LEU A 1 231 ? 22.227  -10.022 22.334  1.00 21.41 ? 229  LEU B CB  1 
ATOM   1721 C CG  . LEU A 1 231 ? 22.662  -10.133 20.879  1.00 23.30 ? 229  LEU B CG  1 
ATOM   1722 C CD1 . LEU A 1 231 ? 23.384  -11.464 20.663  1.00 24.84 ? 229  LEU B CD1 1 
ATOM   1723 C CD2 . LEU A 1 231 ? 21.470  -10.022 19.945  1.00 23.67 ? 229  LEU B CD2 1 
ATOM   1724 N N   . PHE A 1 232 ? 25.245  -8.554  22.783  1.00 20.64 ? 230  PHE B N   1 
ATOM   1725 C CA  . PHE A 1 232 ? 26.064  -7.316  22.824  1.00 20.44 ? 230  PHE B CA  1 
ATOM   1726 C C   . PHE A 1 232 ? 26.530  -6.970  21.424  1.00 23.47 ? 230  PHE B C   1 
ATOM   1727 O O   . PHE A 1 232 ? 26.904  -7.886  20.654  1.00 20.51 ? 230  PHE B O   1 
ATOM   1728 C CB  . PHE A 1 232 ? 27.224  -7.483  23.801  1.00 20.12 ? 230  PHE B CB  1 
ATOM   1729 C CG  . PHE A 1 232 ? 26.761  -7.812  25.189  1.00 20.57 ? 230  PHE B CG  1 
ATOM   1730 C CD1 . PHE A 1 232 ? 26.538  -9.128  25.572  1.00 20.85 ? 230  PHE B CD1 1 
ATOM   1731 C CD2 . PHE A 1 232 ? 26.450  -6.805  26.089  1.00 22.01 ? 230  PHE B CD2 1 
ATOM   1732 C CE1 . PHE A 1 232 ? 26.043  -9.436  26.827  1.00 21.46 ? 230  PHE B CE1 1 
ATOM   1733 C CE2 . PHE A 1 232 ? 25.973  -7.117  27.351  1.00 20.69 ? 230  PHE B CE2 1 
ATOM   1734 C CZ  . PHE A 1 232 ? 25.763  -8.417  27.727  1.00 22.04 ? 230  PHE B CZ  1 
ATOM   1735 N N   . ILE A 1 233 ? 26.578  -5.671  21.150  1.00 19.56 ? 231  ILE B N   1 
ATOM   1736 C CA  . ILE A 1 233 ? 27.237  -5.056  19.972  1.00 19.80 ? 231  ILE B CA  1 
ATOM   1737 C C   . ILE A 1 233 ? 28.663  -4.743  20.404  1.00 21.82 ? 231  ILE B C   1 
ATOM   1738 O O   . ILE A 1 233 ? 28.840  -3.943  21.364  1.00 22.71 ? 231  ILE B O   1 
ATOM   1739 C CB  . ILE A 1 233 ? 26.524  -3.774  19.505  1.00 20.11 ? 231  ILE B CB  1 
ATOM   1740 C CG1 . ILE A 1 233 ? 25.030  -3.993  19.296  1.00 21.04 ? 231  ILE B CG1 1 
ATOM   1741 C CG2 . ILE A 1 233 ? 27.237  -3.201  18.284  1.00 20.81 ? 231  ILE B CG2 1 
ATOM   1742 C CD1 . ILE A 1 233 ? 24.220  -2.722  19.133  1.00 21.81 ? 231  ILE B CD1 1 
ATOM   1743 N N   . VAL A 1 234 ? 29.648  -5.372  19.768  1.00 20.21 ? 232  VAL B N   1 
ATOM   1744 C CA  . VAL A 1 234 ? 31.075  -5.185  20.106  1.00 20.61 ? 232  VAL B CA  1 
ATOM   1745 C C   . VAL A 1 234 ? 31.808  -4.864  18.812  1.00 22.49 ? 232  VAL B C   1 
ATOM   1746 O O   . VAL A 1 234 ? 32.165  -5.772  18.033  1.00 22.80 ? 232  VAL B O   1 
ATOM   1747 C CB  . VAL A 1 234 ? 31.684  -6.426  20.776  1.00 21.63 ? 232  VAL B CB  1 
ATOM   1748 C CG1 . VAL A 1 234 ? 33.115  -6.129  21.165  1.00 23.22 ? 232  VAL B CG1 1 
ATOM   1749 C CG2 . VAL A 1 234 ? 30.860  -6.948  21.948  1.00 22.11 ? 232  VAL B CG2 1 
ATOM   1750 N N   . PRO A 1 235 ? 32.022  -3.574  18.491  1.00 20.70 ? 233  PRO B N   1 
ATOM   1751 C CA  . PRO A 1 235 ? 32.675  -3.214  17.238  1.00 20.70 ? 233  PRO B CA  1 
ATOM   1752 C C   . PRO A 1 235 ? 34.197  -3.338  17.337  1.00 21.25 ? 233  PRO B C   1 
ATOM   1753 O O   . PRO A 1 235 ? 34.748  -3.116  18.403  1.00 23.08 ? 233  PRO B O   1 
ATOM   1754 C CB  . PRO A 1 235 ? 32.246  -1.748  17.082  1.00 20.87 ? 233  PRO B CB  1 
ATOM   1755 C CG  . PRO A 1 235 ? 32.207  -1.239  18.489  1.00 21.08 ? 233  PRO B CG  1 
ATOM   1756 C CD  . PRO A 1 235 ? 31.598  -2.382  19.274  1.00 22.66 ? 233  PRO B CD  1 
ATOM   1757 N N   . LYS A 1 236 ? 34.857  -3.638  16.221  1.00 19.73 ? 234  LYS B N   1 
ATOM   1758 C CA  . LYS A 1 236 ? 36.341  -3.676  16.146  1.00 20.81 ? 234  LYS B CA  1 
ATOM   1759 C C   . LYS A 1 236 ? 36.909  -2.288  16.477  1.00 22.33 ? 234  LYS B C   1 
ATOM   1760 O O   . LYS A 1 236 ? 37.910  -2.226  17.214  1.00 21.89 ? 234  LYS B O   1 
ATOM   1761 C CB  . LYS A 1 236 ? 36.797  -4.074  14.743  1.00 20.94 ? 234  LYS B CB  1 
ATOM   1762 C CG  . LYS A 1 236 ? 38.288  -4.207  14.576  1.00 22.05 ? 234  LYS B CG  1 
ATOM   1763 C CD  . LYS A 1 236 ? 38.659  -4.563  13.164  1.00 24.07 ? 234  LYS B CD  1 
ATOM   1764 C CE  . LYS A 1 236 ? 40.152  -4.655  12.976  1.00 22.91 ? 234  LYS B CE  1 
ATOM   1765 N NZ  . LYS A 1 236 ? 40.501  -4.895  11.549  1.00 23.97 ? 234  LYS B NZ  1 
ATOM   1766 N N   . PHE A 1 237 ? 36.331  -1.250  15.893  1.00 20.18 ? 235  PHE B N   1 
ATOM   1767 C CA  . PHE A 1 237 ? 36.664  0.165   16.204  1.00 23.14 ? 235  PHE B CA  1 
ATOM   1768 C C   . PHE A 1 237 ? 35.454  0.827   16.854  1.00 23.68 ? 235  PHE B C   1 
ATOM   1769 O O   . PHE A 1 237 ? 34.337  0.755   16.329  1.00 21.83 ? 235  PHE B O   1 
ATOM   1770 C CB  . PHE A 1 237 ? 37.111  0.928   14.957  1.00 22.69 ? 235  PHE B CB  1 
ATOM   1771 C CG  . PHE A 1 237 ? 38.356  0.422   14.279  1.00 25.92 ? 235  PHE B CG  1 
ATOM   1772 C CD1 . PHE A 1 237 ? 39.617  0.819   14.702  1.00 25.36 ? 235  PHE B CD1 1 
ATOM   1773 C CD2 . PHE A 1 237 ? 38.269  -0.424  13.183  1.00 25.14 ? 235  PHE B CD2 1 
ATOM   1774 C CE1 . PHE A 1 237 ? 40.755  0.358   14.070  1.00 25.63 ? 235  PHE B CE1 1 
ATOM   1775 C CE2 . PHE A 1 237 ? 39.413  -0.880  12.547  1.00 26.20 ? 235  PHE B CE2 1 
ATOM   1776 C CZ  . PHE A 1 237 ? 40.656  -0.489  12.991  1.00 26.99 ? 235  PHE B CZ  1 
ATOM   1777 N N   . LEU A 1 238 ? 35.670  1.471   17.997  1.00 23.56 ? 236  LEU B N   1 
ATOM   1778 C CA  . LEU A 1 238 ? 34.589  2.206   18.682  1.00 24.23 ? 236  LEU B CA  1 
ATOM   1779 C C   . LEU A 1 238 ? 34.275  3.450   17.861  1.00 23.65 ? 236  LEU B C   1 
ATOM   1780 O O   . LEU A 1 238 ? 35.187  4.050   17.284  1.00 25.08 ? 236  LEU B O   1 
ATOM   1781 C CB  . LEU A 1 238 ? 35.052  2.497   20.109  1.00 26.98 ? 236  LEU B CB  1 
ATOM   1782 C CG  . LEU A 1 238 ? 35.059  1.238   20.962  1.00 26.98 ? 236  LEU B CG  1 
ATOM   1783 C CD1 . LEU A 1 238 ? 36.044  1.337   22.127  1.00 30.61 ? 236  LEU B CD1 1 
ATOM   1784 C CD2 . LEU A 1 238 ? 33.652  0.935   21.419  1.00 27.12 ? 236  LEU B CD2 1 
ATOM   1785 N N   . PRO A 1 239 ? 32.987  3.808   17.695  1.00 26.74 ? 237  PRO B N   1 
ATOM   1786 C CA  . PRO A 1 239 ? 32.614  4.983   16.912  1.00 26.85 ? 237  PRO B CA  1 
ATOM   1787 C C   . PRO A 1 239 ? 33.243  6.256   17.493  1.00 27.10 ? 237  PRO B C   1 
ATOM   1788 O O   . PRO A 1 239 ? 33.212  6.376   18.670  1.00 28.52 ? 237  PRO B O   1 
ATOM   1789 C CB  . PRO A 1 239 ? 31.100  5.101   17.084  1.00 26.66 ? 237  PRO B CB  1 
ATOM   1790 C CG  . PRO A 1 239 ? 30.659  3.717   17.473  1.00 31.74 ? 237  PRO B CG  1 
ATOM   1791 C CD  . PRO A 1 239 ? 31.819  3.114   18.235  1.00 28.36 ? 237  PRO B CD  1 
ATOM   1792 N N   . ASN A 1 240 ? 33.729  7.159   16.652  1.00 27.93 ? 238  ASN B N   1 
ATOM   1793 C CA  . ASN A 1 240 ? 34.178  8.518   17.084  1.00 28.72 ? 238  ASN B CA  1 
ATOM   1794 C C   . ASN A 1 240 ? 32.955  9.438   17.190  1.00 31.14 ? 238  ASN B C   1 
ATOM   1795 O O   . ASN A 1 240 ? 31.814  8.979   16.997  1.00 28.12 ? 238  ASN B O   1 
ATOM   1796 C CB  . ASN A 1 240 ? 35.318  9.047   16.206  1.00 29.43 ? 238  ASN B CB  1 
ATOM   1797 C CG  . ASN A 1 240 ? 34.952  9.347   14.768  1.00 27.08 ? 238  ASN B CG  1 
ATOM   1798 O OD1 . ASN A 1 240 ? 33.785  9.489   14.410  1.00 28.99 ? 238  ASN B OD1 1 
ATOM   1799 N ND2 . ASN A 1 240 ? 35.964  9.443   13.923  1.00 32.22 ? 238  ASN B ND2 1 
ATOM   1800 N N   . ALA A 1 241 ? 33.173  10.713  17.532  1.00 32.79 ? 239  ALA B N   1 
ATOM   1801 C CA  . ALA A 1 241 ? 32.094  11.723  17.661  1.00 31.77 ? 239  ALA B CA  1 
ATOM   1802 C C   . ALA A 1 241 ? 31.322  11.872  16.342  1.00 32.09 ? 239  ALA B C   1 
ATOM   1803 O O   . ALA A 1 241 ? 30.117  12.186  16.407  1.00 37.12 ? 239  ALA B O   1 
ATOM   1804 C CB  . ALA A 1 241 ? 32.699  13.033  18.117  1.00 34.37 ? 239  ALA B CB  1 
ATOM   1805 N N   . GLU A 1 242 ? 31.959  11.656  15.186  1.00 33.08 ? 240  GLU B N   1 
ATOM   1806 C CA  . GLU A 1 242 ? 31.316  11.787  13.844  1.00 34.75 ? 240  GLU B CA  1 
ATOM   1807 C C   . GLU A 1 242 ? 30.707  10.445  13.408  1.00 35.02 ? 240  GLU B C   1 
ATOM   1808 O O   . GLU A 1 242 ? 30.240  10.378  12.266  1.00 32.86 ? 240  GLU B O   1 
ATOM   1809 C CB  . GLU A 1 242 ? 32.310  12.232  12.770  1.00 40.54 ? 240  GLU B CB  1 
ATOM   1810 C CG  . GLU A 1 242 ? 32.783  13.666  12.921  1.00 47.51 ? 240  GLU B CG  1 
ATOM   1811 C CD  . GLU A 1 242 ? 33.709  13.860  14.110  1.00 55.90 ? 240  GLU B CD  1 
ATOM   1812 O OE1 . GLU A 1 242 ? 34.656  13.043  14.271  1.00 55.37 ? 240  GLU B OE1 1 
ATOM   1813 O OE2 . GLU A 1 242 ? 33.461  14.796  14.899  1.00 63.46 ? 240  GLU B OE2 1 
ATOM   1814 N N   . GLY A 1 243 ? 30.718  9.430   14.280  1.00 33.91 ? 241  GLY B N   1 
ATOM   1815 C CA  . GLY A 1 243 ? 30.123  8.101   14.019  1.00 31.84 ? 241  GLY B CA  1 
ATOM   1816 C C   . GLY A 1 243 ? 31.002  7.221   13.130  1.00 30.03 ? 241  GLY B C   1 
ATOM   1817 O O   . GLY A 1 243 ? 30.527  6.132   12.722  1.00 29.19 ? 241  GLY B O   1 
ATOM   1818 N N   . ASN A 1 244 ? 32.227  7.636   12.823  1.00 28.44 ? 242  ASN B N   1 
ATOM   1819 C CA  . ASN A 1 244 ? 33.140  6.869   11.941  1.00 29.29 ? 242  ASN B CA  1 
ATOM   1820 C C   . ASN A 1 244 ? 34.043  5.988   12.803  1.00 28.14 ? 242  ASN B C   1 
ATOM   1821 O O   . ASN A 1 244 ? 34.007  6.100   14.031  1.00 25.74 ? 242  ASN B O   1 
ATOM   1822 C CB  . ASN A 1 244 ? 33.959  7.779   11.031  1.00 29.45 ? 242  ASN B CB  1 
ATOM   1823 C CG  . ASN A 1 244 ? 33.086  8.568   10.087  1.00 31.45 ? 242  ASN B CG  1 
ATOM   1824 O OD1 . ASN A 1 244 ? 32.101  8.051   9.559   1.00 31.90 ? 242  ASN B OD1 1 
ATOM   1825 N ND2 . ASN A 1 244 ? 33.406  9.847   9.930   1.00 36.23 ? 242  ASN B ND2 1 
ATOM   1826 N N   . ALA A 1 245 ? 34.808  5.100   12.181  1.00 26.81 ? 243  ALA B N   1 
ATOM   1827 C CA  . ALA A 1 245 ? 35.646  4.152   12.948  1.00 25.60 ? 243  ALA B CA  1 
ATOM   1828 C C   . ALA A 1 245 ? 36.641  4.959   13.792  1.00 26.32 ? 243  ALA B C   1 
ATOM   1829 O O   . ALA A 1 245 ? 37.342  5.795   13.235  1.00 28.45 ? 243  ALA B O   1 
ATOM   1830 C CB  . ALA A 1 245 ? 36.313  3.184   12.004  1.00 26.59 ? 243  ALA B CB  1 
ATOM   1831 N N   . GLY A 1 246 ? 36.709  4.709   15.098  1.00 26.73 ? 244  GLY B N   1 
ATOM   1832 C CA  . GLY A 1 246 ? 37.551  5.500   16.021  1.00 30.02 ? 244  GLY B CA  1 
ATOM   1833 C C   . GLY A 1 246 ? 38.611  4.662   16.706  1.00 25.70 ? 244  GLY B C   1 
ATOM   1834 O O   . GLY A 1 246 ? 39.378  4.001   16.018  1.00 29.12 ? 244  GLY B O   1 
ATOM   1835 N N   . GLU A 1 247 ? 38.624  4.682   18.036  1.00 27.11 ? 245  GLU B N   1 
ATOM   1836 C CA  . GLU A 1 247 ? 39.609  3.974   18.887  1.00 27.27 ? 245  GLU B CA  1 
ATOM   1837 C C   . GLU A 1 247 ? 39.503  2.464   18.619  1.00 26.10 ? 245  GLU B C   1 
ATOM   1838 O O   . GLU A 1 247 ? 38.370  1.952   18.670  1.00 26.15 ? 245  GLU B O   1 
ATOM   1839 C CB  . GLU A 1 247 ? 39.296  4.207   20.364  1.00 30.84 ? 245  GLU B CB  1 
ATOM   1840 C CG  . GLU A 1 247 ? 40.333  3.590   21.293  1.00 37.37 ? 245  GLU B CG  1 
ATOM   1841 C CD  . GLU A 1 247 ? 39.999  3.538   22.780  1.00 44.23 ? 245  GLU B CD  1 
ATOM   1842 O OE1 . GLU A 1 247 ? 38.823  3.701   23.153  1.00 48.65 ? 245  GLU B OE1 1 
ATOM   1843 O OE2 . GLU A 1 247 ? 40.929  3.299   23.569  1.00 51.94 ? 245  GLU B OE2 1 
ATOM   1844 N N   . ARG A 1 248 ? 40.635  1.805   18.386  1.00 27.55 ? 246  ARG B N   1 
ATOM   1845 C CA  . ARG A 1 248 ? 40.714  0.320   18.304  1.00 27.31 ? 246  ARG B CA  1 
ATOM   1846 C C   . ARG A 1 248 ? 40.154  -0.276  19.605  1.00 27.50 ? 246  ARG B C   1 
ATOM   1847 O O   . ARG A 1 248 ? 40.649  0.048   20.713  1.00 25.53 ? 246  ARG B O   1 
ATOM   1848 C CB  . ARG A 1 248 ? 42.146  -0.134  18.015  1.00 27.02 ? 246  ARG B CB  1 
ATOM   1849 C CG  . ARG A 1 248 ? 42.300  -1.645  17.867  1.00 29.06 ? 246  ARG B CG  1 
ATOM   1850 C CD  . ARG A 1 248 ? 41.323  -2.252  16.879  1.00 31.94 ? 246  ARG B CD  1 
ATOM   1851 N NE  . ARG A 1 248 ? 41.345  -3.721  16.922  1.00 33.47 ? 246  ARG B NE  1 
ATOM   1852 C CZ  . ARG A 1 248 ? 42.139  -4.465  16.183  1.00 35.15 ? 246  ARG B CZ  1 
ATOM   1853 N NH1 . ARG A 1 248 ? 42.965  -3.893  15.326  1.00 38.13 ? 246  ARG B NH1 1 
ATOM   1854 N NH2 . ARG A 1 248 ? 42.090  -5.782  16.278  1.00 32.80 ? 246  ARG B NH2 1 
ATOM   1855 N N   . ASN A 1 249 ? 39.169  -1.165  19.493  1.00 24.19 ? 247  ASN B N   1 
ATOM   1856 C CA  . ASN A 1 249 ? 38.581  -1.856  20.665  1.00 22.48 ? 247  ASN B CA  1 
ATOM   1857 C C   . ASN A 1 249 ? 39.454  -3.088  20.924  1.00 22.42 ? 247  ASN B C   1 
ATOM   1858 O O   . ASN A 1 249 ? 40.195  -3.465  20.010  1.00 23.02 ? 247  ASN B O   1 
ATOM   1859 C CB  . ASN A 1 249 ? 37.113  -2.178  20.386  1.00 24.23 ? 247  ASN B CB  1 
ATOM   1860 C CG  . ASN A 1 249 ? 36.263  -2.510  21.580  1.00 22.31 ? 247  ASN B CG  1 
ATOM   1861 O OD1 . ASN A 1 249 ? 36.686  -2.405  22.732  1.00 24.09 ? 247  ASN B OD1 1 
ATOM   1862 N ND2 . ASN A 1 249 ? 35.025  -2.887  21.303  1.00 22.33 ? 247  ASN B ND2 1 
ATOM   1863 N N   . ALA A 1 250 ? 39.329  -3.722  22.089  1.00 22.33 ? 248  ALA B N   1 
ATOM   1864 C CA  . ALA A 1 250 ? 40.150  -4.877  22.518  1.00 23.04 ? 248  ALA B CA  1 
ATOM   1865 C C   . ALA A 1 250 ? 39.503  -6.153  21.969  1.00 22.90 ? 248  ALA B C   1 
ATOM   1866 O O   . ALA A 1 250 ? 39.074  -6.999  22.756  1.00 26.17 ? 248  ALA B O   1 
ATOM   1867 C CB  . ALA A 1 250 ? 40.281  -4.908  24.022  1.00 24.44 ? 248  ALA B CB  1 
ATOM   1868 N N   . VAL A 1 251 ? 39.416  -6.225  20.653  1.00 25.04 ? 249  VAL B N   1 
ATOM   1869 C CA  . VAL A 1 251 ? 38.907  -7.392  19.873  1.00 27.50 ? 249  VAL B CA  1 
ATOM   1870 C C   . VAL A 1 251 ? 39.970  -7.728  18.865  1.00 25.13 ? 249  VAL B C   1 
ATOM   1871 O O   . VAL A 1 251 ? 40.318  -6.850  18.083  1.00 26.65 ? 249  VAL B O   1 
ATOM   1872 C CB  . VAL A 1 251 ? 37.606  -7.102  19.110  1.00 31.05 ? 249  VAL B CB  1 
ATOM   1873 C CG1 . VAL A 1 251 ? 37.041  -8.403  18.532  1.00 30.22 ? 249  VAL B CG1 1 
ATOM   1874 C CG2 . VAL A 1 251 ? 36.576  -6.388  19.945  1.00 32.36 ? 249  VAL B CG2 1 
ATOM   1875 N N   . SER A 1 252 ? 40.400  -8.986  18.795  1.00 23.34 ? 250  SER B N   1 
ATOM   1876 C CA  . SER A 1 252 ? 41.476  -9.363  17.861  1.00 23.99 ? 250  SER B CA  1 
ATOM   1877 C C   . SER A 1 252 ? 41.345  -10.831 17.487  1.00 22.04 ? 250  SER B C   1 
ATOM   1878 O O   . SER A 1 252 ? 40.718  -11.618 18.225  1.00 22.83 ? 250  SER B O   1 
ATOM   1879 C CB  . SER A 1 252 ? 42.847  -9.034  18.409  1.00 25.04 ? 250  SER B CB  1 
ATOM   1880 O OG  . SER A 1 252 ? 43.121  -9.803  19.557  1.00 25.69 ? 250  SER B OG  1 
ATOM   1881 N N   . CYS A 1 253 ? 41.853  -11.127 16.310  1.00 24.07 ? 251  CYS B N   1 
ATOM   1882 C CA  . CYS A 1 253 ? 41.810  -12.485 15.734  1.00 21.62 ? 251  CYS B CA  1 
ATOM   1883 C C   . CYS A 1 253 ? 43.100  -13.200 16.114  1.00 21.27 ? 251  CYS B C   1 
ATOM   1884 O O   . CYS A 1 253 ? 44.158  -12.747 15.675  1.00 25.25 ? 251  CYS B O   1 
ATOM   1885 C CB  . CYS A 1 253 ? 41.660  -12.404 14.229  1.00 21.72 ? 251  CYS B CB  1 
ATOM   1886 S SG  . CYS A 1 253 ? 41.679  -14.047 13.483  1.00 22.74 ? 251  CYS B SG  1 
ATOM   1887 N N   . GLY A 1 254 ? 42.978  -14.260 16.907  1.00 22.80 ? 252  GLY B N   1 
ATOM   1888 C CA  . GLY A 1 254 ? 44.120  -15.053 17.394  1.00 22.47 ? 252  GLY B CA  1 
ATOM   1889 C C   . GLY A 1 254 ? 44.652  -15.953 16.296  1.00 24.41 ? 252  GLY B C   1 
ATOM   1890 O O   . GLY A 1 254 ? 45.871  -16.230 16.258  1.00 25.06 ? 252  GLY B O   1 
ATOM   1891 N N   . SER A 1 255 ? 43.776  -16.426 15.411  1.00 23.24 ? 253  SER B N   1 
ATOM   1892 C CA  . SER A 1 255 ? 44.164  -17.410 14.374  1.00 21.35 ? 253  SER B CA  1 
ATOM   1893 C C   . SER A 1 255 ? 42.982  -17.617 13.417  1.00 21.05 ? 253  SER B C   1 
ATOM   1894 O O   . SER A 1 255 ? 41.829  -17.228 13.743  1.00 20.83 ? 253  SER B O   1 
ATOM   1895 C CB  . SER A 1 255 ? 44.579  -18.723 15.005  1.00 21.87 ? 253  SER B CB  1 
ATOM   1896 O OG  . SER A 1 255 ? 43.494  -19.346 15.691  1.00 22.57 ? 253  SER B OG  1 
ATOM   1897 N N   . ILE A 1 256 ? 43.263  -18.219 12.275  1.00 19.51 ? 254  ILE B N   1 
ATOM   1898 C CA  . ILE A 1 256 ? 42.187  -18.655 11.346  1.00 19.33 ? 254  ILE B CA  1 
ATOM   1899 C C   . ILE A 1 256 ? 42.337  -20.154 11.126  1.00 19.86 ? 254  ILE B C   1 
ATOM   1900 O O   . ILE A 1 256 ? 43.484  -20.689 11.180  1.00 20.27 ? 254  ILE B O   1 
ATOM   1901 C CB  . ILE A 1 256 ? 42.213  -17.866 10.034  1.00 21.48 ? 254  ILE B CB  1 
ATOM   1902 C CG1 . ILE A 1 256 ? 43.505  -18.079 9.245   1.00 20.58 ? 254  ILE B CG1 1 
ATOM   1903 C CG2 . ILE A 1 256 ? 41.927  -16.396 10.315  1.00 20.93 ? 254  ILE B CG2 1 
ATOM   1904 C CD1 . ILE A 1 256 ? 43.527  -17.405 7.867   1.00 22.29 ? 254  ILE B CD1 1 
ATOM   1905 N N   . GLU A 1 257 ? 41.229  -20.792 10.833  1.00 18.02 ? 255  GLU B N   1 
ATOM   1906 C CA  . GLU A 1 257 ? 41.200  -22.270 10.667  1.00 18.81 ? 255  GLU B CA  1 
ATOM   1907 C C   . GLU A 1 257 ? 41.706  -22.685 9.276   1.00 18.49 ? 255  GLU B C   1 
ATOM   1908 O O   . GLU A 1 257 ? 41.565  -21.944 8.246   1.00 18.96 ? 255  GLU B O   1 
ATOM   1909 C CB  . GLU A 1 257 ? 39.768  -22.783 10.846  1.00 18.46 ? 255  GLU B CB  1 
ATOM   1910 C CG  . GLU A 1 257 ? 39.182  -22.472 12.205  1.00 19.28 ? 255  GLU B CG  1 
ATOM   1911 C CD  . GLU A 1 257 ? 39.849  -23.051 13.434  1.00 23.07 ? 255  GLU B CD  1 
ATOM   1912 O OE1 . GLU A 1 257 ? 39.711  -22.436 14.501  1.00 23.40 ? 255  GLU B OE1 1 
ATOM   1913 O OE2 . GLU A 1 257 ? 40.455  -24.164 13.345  1.00 22.62 ? 255  GLU B OE2 1 
ATOM   1914 N N   . HIS A 1 258 ? 42.221  -23.919 9.282   1.00 19.03 ? 256  HIS B N   1 
ATOM   1915 C CA  . HIS A 1 258 ? 42.584  -24.631 8.043   1.00 18.88 ? 256  HIS B CA  1 
ATOM   1916 C C   . HIS A 1 258 ? 41.406  -25.585 7.831   1.00 18.88 ? 256  HIS B C   1 
ATOM   1917 O O   . HIS A 1 258 ? 41.197  -26.437 8.693   1.00 19.84 ? 256  HIS B O   1 
ATOM   1918 C CB  . HIS A 1 258 ? 43.893  -25.383 8.273   1.00 21.45 ? 256  HIS B CB  1 
ATOM   1919 C CG  . HIS A 1 258 ? 44.377  -26.195 7.118   1.00 25.87 ? 256  HIS B CG  1 
ATOM   1920 N ND1 . HIS A 1 258 ? 43.872  -26.060 5.841   1.00 33.96 ? 256  HIS B ND1 1 
ATOM   1921 C CD2 . HIS A 1 258 ? 45.333  -27.146 7.047   1.00 25.68 ? 256  HIS B CD2 1 
ATOM   1922 C CE1 . HIS A 1 258 ? 44.494  -26.895 5.035   1.00 30.41 ? 256  HIS B CE1 1 
ATOM   1923 N NE2 . HIS A 1 258 ? 45.394  -27.573 5.751   1.00 29.22 ? 256  HIS B NE2 1 
ATOM   1924 N N   . LYS A 1 259 ? 40.672  -25.426 6.742   1.00 18.48 ? 257  LYS B N   1 
ATOM   1925 C CA  . LYS A 1 259 ? 39.422  -26.182 6.541   1.00 18.06 ? 257  LYS B CA  1 
ATOM   1926 C C   . LYS A 1 259 ? 39.378  -26.936 5.213   1.00 17.03 ? 257  LYS B C   1 
ATOM   1927 O O   . LYS A 1 259 ? 40.205  -26.685 4.352   1.00 18.17 ? 257  LYS B O   1 
ATOM   1928 C CB  . LYS A 1 259 ? 38.259  -25.190 6.514   1.00 19.51 ? 257  LYS B CB  1 
ATOM   1929 C CG  . LYS A 1 259 ? 38.240  -24.158 7.630   1.00 21.46 ? 257  LYS B CG  1 
ATOM   1930 C CD  . LYS A 1 259 ? 37.394  -22.959 7.286   1.00 25.93 ? 257  LYS B CD  1 
ATOM   1931 C CE  . LYS A 1 259 ? 37.813  -22.301 5.991   1.00 25.04 ? 257  LYS B CE  1 
ATOM   1932 N NZ  . LYS A 1 259 ? 37.706  -20.827 6.059   1.00 23.14 ? 257  LYS B NZ  1 
ATOM   1933 N N   . MET A 1 260 ? 38.394  -27.818 5.089   1.00 15.74 ? 258  MET B N   1 
ATOM   1934 C CA  . MET A 1 260 ? 38.177  -28.579 3.837   1.00 16.25 ? 258  MET B CA  1 
ATOM   1935 C C   . MET A 1 260 ? 37.824  -27.633 2.693   1.00 16.45 ? 258  MET B C   1 
ATOM   1936 O O   . MET A 1 260 ? 38.234  -27.890 1.576   1.00 15.39 ? 258  MET B O   1 
ATOM   1937 C CB  . MET A 1 260 ? 36.983  -29.508 4.072   1.00 15.96 ? 258  MET B CB  1 
ATOM   1938 C CG  . MET A 1 260 ? 36.600  -30.395 2.914   1.00 17.40 ? 258  MET B CG  1 
ATOM   1939 S SD  . MET A 1 260 ? 35.110  -31.297 3.409   1.00 19.25 ? 258  MET B SD  1 
ATOM   1940 C CE  . MET A 1 260 ? 35.165  -32.672 2.263   1.00 21.39 ? 258  MET B CE  1 
ATOM   1941 N N   . GLY A 1 261 ? 37.079  -26.579 3.001   1.00 14.76 ? 259  GLY B N   1 
ATOM   1942 C CA  . GLY A 1 261 ? 36.591  -25.681 1.939   1.00 15.88 ? 259  GLY B CA  1 
ATOM   1943 C C   . GLY A 1 261 ? 36.233  -24.309 2.498   1.00 14.89 ? 259  GLY B C   1 
ATOM   1944 O O   . GLY A 1 261 ? 36.723  -23.978 3.591   1.00 15.02 ? 259  GLY B O   1 
ATOM   1945 N N   . ILE A 1 262 ? 35.437  -23.585 1.744   1.00 14.11 ? 260  ILE B N   1 
ATOM   1946 C CA  . ILE A 1 262 ? 35.184  -22.119 1.911   1.00 14.90 ? 260  ILE B CA  1 
ATOM   1947 C C   . ILE A 1 262 ? 36.463  -21.419 2.390   1.00 15.48 ? 260  ILE B C   1 
ATOM   1948 O O   . ILE A 1 262 ? 36.407  -20.596 3.342   1.00 15.88 ? 260  ILE B O   1 
ATOM   1949 C CB  . ILE A 1 262 ? 33.939  -21.821 2.776   1.00 14.55 ? 260  ILE B CB  1 
ATOM   1950 C CG1 . ILE A 1 262 ? 33.994  -22.395 4.184   1.00 14.15 ? 260  ILE B CG1 1 
ATOM   1951 C CG2 . ILE A 1 262 ? 32.699  -22.303 2.043   1.00 16.38 ? 260  ILE B CG2 1 
ATOM   1952 C CD1 . ILE A 1 262 ? 33.028  -21.731 5.174   1.00 15.92 ? 260  ILE B CD1 1 
ATOM   1953 N N   . HIS A 1 263 ? 37.565  -21.642 1.685   1.00 15.85 ? 261  HIS B N   1 
ATOM   1954 C CA  . HIS A 1 263 ? 38.867  -21.065 2.099   1.00 15.92 ? 261  HIS B CA  1 
ATOM   1955 C C   . HIS A 1 263 ? 38.843  -19.535 2.014   1.00 16.75 ? 261  HIS B C   1 
ATOM   1956 O O   . HIS A 1 263 ? 39.577  -18.914 2.770   1.00 18.83 ? 261  HIS B O   1 
ATOM   1957 C CB  . HIS A 1 263 ? 39.998  -21.626 1.225   1.00 16.10 ? 261  HIS B CB  1 
ATOM   1958 C CG  . HIS A 1 263 ? 40.211  -23.098 1.345   1.00 16.09 ? 261  HIS B CG  1 
ATOM   1959 N ND1 . HIS A 1 263 ? 40.852  -23.827 0.369   1.00 16.02 ? 261  HIS B ND1 1 
ATOM   1960 C CD2 . HIS A 1 263 ? 39.890  -23.974 2.318   1.00 17.40 ? 261  HIS B CD2 1 
ATOM   1961 C CE1 . HIS A 1 263 ? 40.916  -25.089 0.732   1.00 16.70 ? 261  HIS B CE1 1 
ATOM   1962 N NE2 . HIS A 1 263 ? 40.335  -25.204 1.921   1.00 17.26 ? 261  HIS B NE2 1 
ATOM   1963 N N   . GLY A 1 264 ? 38.030  -18.975 1.116   1.00 16.15 ? 262  GLY B N   1 
ATOM   1964 C CA  . GLY A 1 264 ? 38.045  -17.512 0.891   1.00 18.00 ? 262  GLY B CA  1 
ATOM   1965 C C   . GLY A 1 264 ? 37.385  -16.760 2.027   1.00 18.73 ? 262  GLY B C   1 
ATOM   1966 O O   . GLY A 1 264 ? 37.466  -15.523 2.040   1.00 18.09 ? 262  GLY B O   1 
ATOM   1967 N N   . ASN A 1 265 ? 36.638  -17.452 2.880   1.00 17.37 ? 263  ASN B N   1 
ATOM   1968 C CA  . ASN A 1 265 ? 35.939  -16.860 4.044   1.00 17.33 ? 263  ASN B CA  1 
ATOM   1969 C C   . ASN A 1 265 ? 36.750  -17.152 5.310   1.00 18.37 ? 263  ASN B C   1 
ATOM   1970 O O   . ASN A 1 265 ? 36.863  -18.301 5.707   1.00 17.50 ? 263  ASN B O   1 
ATOM   1971 C CB  . ASN A 1 265 ? 34.490  -17.320 4.239   1.00 18.03 ? 263  ASN B CB  1 
ATOM   1972 C CG  . ASN A 1 265 ? 33.819  -16.418 5.258   1.00 18.99 ? 263  ASN B CG  1 
ATOM   1973 O OD1 . ASN A 1 265 ? 33.689  -16.772 6.410   1.00 20.70 ? 263  ASN B OD1 1 
ATOM   1974 N ND2 . ASN A 1 265 ? 33.433  -15.218 4.850   1.00 20.14 ? 263  ASN B ND2 1 
ATOM   1975 N N   . ALA A 1 266 ? 37.323  -16.109 5.905   1.00 17.81 ? 264  ALA B N   1 
ATOM   1976 C CA  . ALA A 1 266 ? 38.165  -16.233 7.100   1.00 17.63 ? 264  ALA B CA  1 
ATOM   1977 C C   . ALA A 1 266 ? 37.332  -16.800 8.259   1.00 18.58 ? 264  ALA B C   1 
ATOM   1978 O O   . ALA A 1 266 ? 36.299  -16.228 8.609   1.00 17.90 ? 264  ALA B O   1 
ATOM   1979 C CB  . ALA A 1 266 ? 38.773  -14.898 7.438   1.00 17.81 ? 264  ALA B CB  1 
ATOM   1980 N N   . THR A 1 267 ? 37.769  -17.920 8.820   1.00 17.00 ? 265  THR B N   1 
ATOM   1981 C CA  . THR A 1 267 ? 37.110  -18.616 9.936   1.00 16.46 ? 265  THR B CA  1 
ATOM   1982 C C   . THR A 1 267 ? 37.967  -18.387 11.174  1.00 17.39 ? 265  THR B C   1 
ATOM   1983 O O   . THR A 1 267 ? 39.048  -18.948 11.278  1.00 16.66 ? 265  THR B O   1 
ATOM   1984 C CB  . THR A 1 267 ? 36.924  -20.109 9.667   1.00 17.62 ? 265  THR B CB  1 
ATOM   1985 O OG1 . THR A 1 267 ? 36.273  -20.288 8.403   1.00 20.35 ? 265  THR B OG1 1 
ATOM   1986 C CG2 . THR A 1 267 ? 36.091  -20.781 10.727  1.00 19.16 ? 265  THR B CG2 1 
ATOM   1987 N N   . CYS A 1 268 ? 37.529  -17.470 12.021  1.00 18.28 ? 266  CYS B N   1 
ATOM   1988 C CA  . CYS A 1 268 ? 38.424  -16.746 12.938  1.00 17.86 ? 266  CYS B CA  1 
ATOM   1989 C C   . CYS A 1 268 ? 38.167  -17.178 14.379  1.00 17.40 ? 266  CYS B C   1 
ATOM   1990 O O   . CYS A 1 268 ? 37.011  -17.251 14.801  1.00 18.52 ? 266  CYS B O   1 
ATOM   1991 C CB  . CYS A 1 268 ? 38.209  -15.237 12.833  1.00 17.75 ? 266  CYS B CB  1 
ATOM   1992 S SG  . CYS A 1 268 ? 38.593  -14.587 11.198  1.00 20.91 ? 266  CYS B SG  1 
ATOM   1993 N N   . VAL A 1 269 ? 39.257  -17.399 15.114  1.00 17.01 ? 267  VAL B N   1 
ATOM   1994 C CA  . VAL A 1 269 ? 39.247  -17.377 16.608  1.00 19.04 ? 267  VAL B CA  1 
ATOM   1995 C C   . VAL A 1 269 ? 39.295  -15.905 17.027  1.00 17.34 ? 267  VAL B C   1 
ATOM   1996 O O   . VAL A 1 269 ? 40.286  -15.224 16.651  1.00 20.30 ? 267  VAL B O   1 
ATOM   1997 C CB  . VAL A 1 269 ? 40.421  -18.139 17.242  1.00 20.37 ? 267  VAL B CB  1 
ATOM   1998 C CG1 . VAL A 1 269 ? 40.437  -17.974 18.770  1.00 21.05 ? 267  VAL B CG1 1 
ATOM   1999 C CG2 . VAL A 1 269 ? 40.386  -19.623 16.887  1.00 20.05 ? 267  VAL B CG2 1 
ATOM   2000 N N   . MET A 1 270 ? 38.256  -15.441 17.709  1.00 18.93 ? 268  MET B N   1 
ATOM   2001 C CA  . MET A 1 270 ? 38.149  -14.002 18.081  1.00 20.29 ? 268  MET B CA  1 
ATOM   2002 C C   . MET A 1 270 ? 38.314  -13.898 19.600  1.00 19.51 ? 268  MET B C   1 
ATOM   2003 O O   . MET A 1 270 ? 37.572  -14.516 20.346  1.00 20.62 ? 268  MET B O   1 
ATOM   2004 C CB  . MET A 1 270 ? 36.819  -13.402 17.628  1.00 20.05 ? 268  MET B CB  1 
ATOM   2005 C CG  . MET A 1 270 ? 36.677  -13.328 16.110  1.00 19.57 ? 268  MET B CG  1 
ATOM   2006 S SD  . MET A 1 270 ? 37.954  -12.523 15.222  1.00 21.47 ? 268  MET B SD  1 
ATOM   2007 C CE  . MET A 1 270 ? 37.874  -10.830 15.849  1.00 20.35 ? 268  MET B CE  1 
ATOM   2008 N N   . ASN A 1 271 ? 39.304  -13.127 20.018  1.00 20.02 ? 269  ASN B N   1 
ATOM   2009 C CA  . ASN A 1 271 ? 39.571  -12.909 21.457  1.00 19.92 ? 269  ASN B CA  1 
ATOM   2010 C C   . ASN A 1 271 ? 38.962  -11.549 21.839  1.00 20.80 ? 269  ASN B C   1 
ATOM   2011 O O   . ASN A 1 271 ? 39.376  -10.534 21.232  1.00 21.72 ? 269  ASN B O   1 
ATOM   2012 C CB  . ASN A 1 271 ? 41.080  -12.950 21.716  1.00 20.62 ? 269  ASN B CB  1 
ATOM   2013 C CG  . ASN A 1 271 ? 41.648  -14.337 21.466  1.00 24.50 ? 269  ASN B CG  1 
ATOM   2014 O OD1 . ASN A 1 271 ? 41.076  -15.311 21.944  1.00 25.44 ? 269  ASN B OD1 1 
ATOM   2015 N ND2 . ASN A 1 271 ? 42.747  -14.428 20.728  1.00 26.95 ? 269  ASN B ND2 1 
ATOM   2016 N N   . PHE A 1 272 ? 38.060  -11.570 22.806  1.00 21.77 ? 270  PHE B N   1 
ATOM   2017 C CA  . PHE A 1 272 ? 37.444  -10.389 23.442  1.00 21.41 ? 270  PHE B CA  1 
ATOM   2018 C C   . PHE A 1 272 ? 38.191  -10.177 24.763  1.00 22.96 ? 270  PHE B C   1 
ATOM   2019 O O   . PHE A 1 272 ? 38.020  -11.005 25.667  1.00 24.34 ? 270  PHE B O   1 
ATOM   2020 C CB  . PHE A 1 272 ? 35.932  -10.569 23.546  1.00 21.65 ? 270  PHE B CB  1 
ATOM   2021 C CG  . PHE A 1 272 ? 35.223  -10.653 22.203  1.00 23.46 ? 270  PHE B CG  1 
ATOM   2022 C CD1 . PHE A 1 272 ? 35.068  -11.874 21.569  1.00 23.62 ? 270  PHE B CD1 1 
ATOM   2023 C CD2 . PHE A 1 272 ? 34.715  -9.518  21.576  1.00 22.92 ? 270  PHE B CD2 1 
ATOM   2024 C CE1 . PHE A 1 272 ? 34.425  -11.965 20.339  1.00 22.20 ? 270  PHE B CE1 1 
ATOM   2025 C CE2 . PHE A 1 272 ? 34.083  -9.601  20.338  1.00 24.38 ? 270  PHE B CE2 1 
ATOM   2026 C CZ  . PHE A 1 272 ? 33.952  -10.829 19.710  1.00 22.26 ? 270  PHE B CZ  1 
ATOM   2027 N N   . ASP A 1 273 ? 39.044  -9.145  24.807  1.00 24.99 ? 271  ASP B N   1 
ATOM   2028 C CA  . ASP A 1 273 ? 39.952  -8.846  25.955  1.00 25.91 ? 271  ASP B CA  1 
ATOM   2029 C C   . ASP A 1 273 ? 39.395  -7.645  26.734  1.00 23.16 ? 271  ASP B C   1 
ATOM   2030 O O   . ASP A 1 273 ? 39.987  -6.546  26.617  1.00 24.65 ? 271  ASP B O   1 
ATOM   2031 C CB  . ASP A 1 273 ? 41.376  -8.663  25.442  1.00 26.71 ? 271  ASP B CB  1 
ATOM   2032 C CG  . ASP A 1 273 ? 41.922  -9.930  24.794  1.00 30.28 ? 271  ASP B CG  1 
ATOM   2033 O OD1 . ASP A 1 273 ? 41.570  -11.028 25.259  1.00 36.04 ? 271  ASP B OD1 1 
ATOM   2034 O OD2 . ASP A 1 273 ? 42.680  -9.821  23.836  1.00 33.32 ? 271  ASP B OD2 1 
ATOM   2035 N N   . ALA A 1 274 ? 38.289  -7.849  27.439  1.00 24.00 ? 272  ALA B N   1 
ATOM   2036 C CA  . ALA A 1 274 ? 37.463  -6.807  28.108  1.00 27.23 ? 272  ALA B CA  1 
ATOM   2037 C C   . ALA A 1 274 ? 37.138  -5.715  27.076  1.00 26.32 ? 272  ALA B C   1 
ATOM   2038 O O   . ALA A 1 274 ? 37.353  -4.513  27.347  1.00 27.19 ? 272  ALA B O   1 
ATOM   2039 C CB  . ALA A 1 274 ? 38.165  -6.254  29.337  1.00 26.68 ? 272  ALA B CB  1 
ATOM   2040 N N   . ALA A 1 275 ? 36.718  -6.122  25.881  1.00 23.89 ? 273  ALA B N   1 
ATOM   2041 C CA  . ALA A 1 275 ? 36.289  -5.232  24.780  1.00 23.21 ? 273  ALA B CA  1 
ATOM   2042 C C   . ALA A 1 275 ? 35.040  -4.473  25.208  1.00 21.92 ? 273  ALA B C   1 
ATOM   2043 O O   . ALA A 1 275 ? 34.156  -5.056  25.882  1.00 22.87 ? 273  ALA B O   1 
ATOM   2044 C CB  . ALA A 1 275 ? 36.007  -6.019  23.499  1.00 23.93 ? 273  ALA B CB  1 
ATOM   2045 N N   . THR A 1 276 ? 34.933  -3.206  24.792  1.00 22.41 ? 274  THR B N   1 
ATOM   2046 C CA  . THR A 1 276 ? 33.706  -2.434  25.081  1.00 22.05 ? 274  THR B CA  1 
ATOM   2047 C C   . THR A 1 276 ? 32.564  -2.924  24.189  1.00 21.73 ? 274  THR B C   1 
ATOM   2048 O O   . THR A 1 276 ? 32.758  -3.005  22.949  1.00 22.09 ? 274  THR B O   1 
ATOM   2049 C CB  . THR A 1 276 ? 33.925  -0.924  24.955  1.00 25.18 ? 274  THR B CB  1 
ATOM   2050 O OG1 . THR A 1 276 ? 34.847  -0.566  25.988  1.00 25.23 ? 274  THR B OG1 1 
ATOM   2051 C CG2 . THR A 1 276 ? 32.647  -0.135  25.133  1.00 25.45 ? 274  THR B CG2 1 
ATOM   2052 N N   . GLY A 1 277 ? 31.456  -3.294  24.823  1.00 20.46 ? 275  GLY B N   1 
ATOM   2053 C CA  . GLY A 1 277 ? 30.211  -3.704  24.144  1.00 22.59 ? 275  GLY B CA  1 
ATOM   2054 C C   . GLY A 1 277 ? 28.968  -3.045  24.696  1.00 22.41 ? 275  GLY B C   1 
ATOM   2055 O O   . GLY A 1 277 ? 28.997  -2.508  25.840  1.00 23.60 ? 275  GLY B O   1 
ATOM   2056 N N   . PHE A 1 278 ? 27.903  -3.105  23.904  1.00 21.06 ? 276  PHE B N   1 
ATOM   2057 C CA  . PHE A 1 278 ? 26.625  -2.465  24.282  1.00 22.29 ? 276  PHE B CA  1 
ATOM   2058 C C   . PHE A 1 278 ? 25.499  -3.489  24.236  1.00 24.07 ? 276  PHE B C   1 
ATOM   2059 O O   . PHE A 1 278 ? 25.340  -4.168  23.222  1.00 22.83 ? 276  PHE B O   1 
ATOM   2060 C CB  . PHE A 1 278 ? 26.360  -1.290  23.349  1.00 23.05 ? 276  PHE B CB  1 
ATOM   2061 C CG  . PHE A 1 278 ? 27.543  -0.364  23.249  1.00 24.06 ? 276  PHE B CG  1 
ATOM   2062 C CD1 . PHE A 1 278 ? 27.761  0.605   24.214  1.00 24.00 ? 276  PHE B CD1 1 
ATOM   2063 C CD2 . PHE A 1 278 ? 28.466  -0.493  22.226  1.00 23.81 ? 276  PHE B CD2 1 
ATOM   2064 C CE1 . PHE A 1 278 ? 28.862  1.441   24.143  1.00 23.80 ? 276  PHE B CE1 1 
ATOM   2065 C CE2 . PHE A 1 278 ? 29.567  0.345   22.158  1.00 25.87 ? 276  PHE B CE2 1 
ATOM   2066 C CZ  . PHE A 1 278 ? 29.760  1.312   23.114  1.00 24.14 ? 276  PHE B CZ  1 
ATOM   2067 N N   . LEU A 1 279 ? 24.771  -3.591  25.331  1.00 22.16 ? 277  LEU B N   1 
ATOM   2068 C CA  . LEU A 1 279 ? 23.609  -4.509  25.423  1.00 23.07 ? 277  LEU B CA  1 
ATOM   2069 C C   . LEU A 1 279 ? 22.606  -4.182  24.311  1.00 24.23 ? 277  LEU B C   1 
ATOM   2070 O O   . LEU A 1 279 ? 22.208  -2.980  24.151  1.00 23.26 ? 277  LEU B O   1 
ATOM   2071 C CB  . LEU A 1 279 ? 22.932  -4.381  26.794  1.00 24.82 ? 277  LEU B CB  1 
ATOM   2072 C CG  . LEU A 1 279 ? 21.718  -5.281  27.008  1.00 24.43 ? 277  LEU B CG  1 
ATOM   2073 C CD1 . LEU A 1 279 ? 22.124  -6.745  27.068  1.00 27.03 ? 277  LEU B CD1 1 
ATOM   2074 C CD2 . LEU A 1 279 ? 20.976  -4.902  28.273  1.00 26.83 ? 277  LEU B CD2 1 
ATOM   2075 N N   . ILE A 1 280 ? 22.201  -5.201  23.546  1.00 22.47 ? 278  ILE B N   1 
ATOM   2076 C CA  . ILE A 1 280 ? 21.110  -5.081  22.544  1.00 22.86 ? 278  ILE B CA  1 
ATOM   2077 C C   . ILE A 1 280 ? 20.007  -6.066  22.933  1.00 24.33 ? 278  ILE B C   1 
ATOM   2078 O O   . ILE A 1 280 ? 20.301  -7.255  23.169  1.00 24.56 ? 278  ILE B O   1 
ATOM   2079 C CB  . ILE A 1 280 ? 21.598  -5.283  21.094  1.00 20.38 ? 278  ILE B CB  1 
ATOM   2080 C CG1 . ILE A 1 280 ? 20.412  -5.463  20.146  1.00 22.62 ? 278  ILE B CG1 1 
ATOM   2081 C CG2 . ILE A 1 280 ? 22.583  -6.431  20.987  1.00 20.19 ? 278  ILE B CG2 1 
ATOM   2082 C CD1 . ILE A 1 280 ? 20.720  -5.145  18.713  1.00 22.67 ? 278  ILE B CD1 1 
ATOM   2083 N N   . GLY A 1 281 ? 18.781  -5.564  23.031  1.00 23.10 ? 279  GLY B N   1 
ATOM   2084 C CA  . GLY A 1 281 ? 17.638  -6.312  23.548  1.00 23.56 ? 279  GLY B CA  1 
ATOM   2085 C C   . GLY A 1 281 ? 17.703  -6.421  25.064  1.00 24.41 ? 279  GLY B C   1 
ATOM   2086 O O   . GLY A 1 281 ? 18.640  -5.944  25.705  1.00 25.34 ? 279  GLY B O   1 
ATOM   2087 N N   . PRO A 1 282 ? 16.683  -7.048  25.673  1.00 25.28 ? 280  PRO B N   1 
ATOM   2088 C CA  . PRO A 1 282 ? 16.631  -7.105  27.108  1.00 27.14 ? 280  PRO B CA  1 
ATOM   2089 C C   . PRO A 1 282 ? 17.672  -8.028  27.735  1.00 30.35 ? 280  PRO B C   1 
ATOM   2090 O O   . PRO A 1 282 ? 18.056  -8.997  27.126  1.00 26.82 ? 280  PRO B O   1 
ATOM   2091 C CB  . PRO A 1 282 ? 15.255  -7.721  27.399  1.00 27.85 ? 280  PRO B CB  1 
ATOM   2092 C CG  . PRO A 1 282 ? 14.479  -7.603  26.116  1.00 27.28 ? 280  PRO B CG  1 
ATOM   2093 C CD  . PRO A 1 282 ? 15.534  -7.714  25.045  1.00 26.41 ? 280  PRO B CD  1 
ATOM   2094 N N   . PRO A 1 283 ? 18.108  -7.732  28.970  1.00 29.00 ? 281  PRO B N   1 
ATOM   2095 C CA  . PRO A 1 283 ? 19.009  -8.625  29.680  1.00 28.19 ? 281  PRO B CA  1 
ATOM   2096 C C   . PRO A 1 283 ? 18.369  -10.021 29.771  1.00 26.99 ? 281  PRO B C   1 
ATOM   2097 O O   . PRO A 1 283 ? 17.158  -10.151 29.924  1.00 26.52 ? 281  PRO B O   1 
ATOM   2098 C CB  . PRO A 1 283 ? 19.207  -8.002  31.079  1.00 30.27 ? 281  PRO B CB  1 
ATOM   2099 C CG  . PRO A 1 283 ? 18.389  -6.733  31.109  1.00 31.00 ? 281  PRO B CG  1 
ATOM   2100 C CD  . PRO A 1 283 ? 17.695  -6.563  29.777  1.00 29.29 ? 281  PRO B CD  1 
ATOM   2101 N N   . ASN A 1 284 ? 19.202  -11.038 29.556  1.00 27.88 ? 282  ASN B N   1 
ATOM   2102 C CA  . ASN A 1 284 ? 18.768  -12.456 29.666  1.00 28.79 ? 282  ASN B CA  1 
ATOM   2103 C C   . ASN A 1 284 ? 17.870  -12.892 28.491  1.00 26.94 ? 282  ASN B C   1 
ATOM   2104 O O   . ASN A 1 284 ? 17.365  -14.009 28.552  1.00 27.28 ? 282  ASN B O   1 
ATOM   2105 C CB  . ASN A 1 284 ? 18.171  -12.739 31.049  1.00 29.86 ? 282  ASN B CB  1 
ATOM   2106 C CG  . ASN A 1 284 ? 19.153  -12.518 32.178  1.00 33.70 ? 282  ASN B CG  1 
ATOM   2107 O OD1 . ASN A 1 284 ? 20.360  -12.656 32.001  1.00 34.87 ? 282  ASN B OD1 1 
ATOM   2108 N ND2 . ASN A 1 284 ? 18.642  -12.180 33.349  1.00 36.83 ? 282  ASN B ND2 1 
ATOM   2109 N N   . LYS A 1 285 ? 17.716  -12.056 27.465  1.00 25.77 ? 283  LYS B N   1 
ATOM   2110 C CA  . LYS A 1 285 ? 16.910  -12.432 26.269  1.00 26.52 ? 283  LYS B CA  1 
ATOM   2111 C C   . LYS A 1 285 ? 17.826  -12.514 25.039  1.00 22.85 ? 283  LYS B C   1 
ATOM   2112 O O   . LYS A 1 285 ? 17.327  -12.395 23.938  1.00 24.37 ? 283  LYS B O   1 
ATOM   2113 C CB  . LYS A 1 285 ? 15.753  -11.452 26.073  1.00 28.31 ? 283  LYS B CB  1 
ATOM   2114 C CG  . LYS A 1 285 ? 14.867  -11.235 27.291  1.00 32.15 ? 283  LYS B CG  1 
ATOM   2115 C CD  . LYS A 1 285 ? 14.277  -12.506 27.856  1.00 37.15 ? 283  LYS B CD  1 
ATOM   2116 C CE  . LYS A 1 285 ? 13.479  -13.297 26.843  1.00 42.15 ? 283  LYS B CE  1 
ATOM   2117 N NZ  . LYS A 1 285 ? 12.344  -14.019 27.465  1.00 48.66 ? 283  LYS B NZ  1 
ATOM   2118 N N   . GLY A 1 286 ? 19.111  -12.757 25.261  1.00 24.09 ? 284  GLY B N   1 
ATOM   2119 C CA  . GLY A 1 286 ? 20.104  -12.819 24.166  1.00 24.47 ? 284  GLY B CA  1 
ATOM   2120 C C   . GLY A 1 286 ? 19.761  -13.896 23.135  1.00 24.46 ? 284  GLY B C   1 
ATOM   2121 O O   . GLY A 1 286 ? 19.912  -13.635 21.934  1.00 26.04 ? 284  GLY B O   1 
ATOM   2122 N N   . LEU A 1 287 ? 19.293  -15.050 23.578  1.00 25.54 ? 285  LEU B N   1 
ATOM   2123 C CA  . LEU A 1 287 ? 18.946  -16.150 22.634  1.00 27.38 ? 285  LEU B CA  1 
ATOM   2124 C C   . LEU A 1 287 ? 17.793  -15.702 21.724  1.00 26.08 ? 285  LEU B C   1 
ATOM   2125 O O   . LEU A 1 287 ? 17.932  -15.794 20.464  1.00 23.58 ? 285  LEU B O   1 
ATOM   2126 C CB  . LEU A 1 287 ? 18.586  -17.409 23.419  1.00 29.18 ? 285  LEU B CB  1 
ATOM   2127 C CG  . LEU A 1 287 ? 18.340  -18.647 22.553  1.00 31.26 ? 285  LEU B CG  1 
ATOM   2128 C CD1 . LEU A 1 287 ? 19.471  -18.831 21.557  1.00 33.63 ? 285  LEU B CD1 1 
ATOM   2129 C CD2 . LEU A 1 287 ? 18.174  -19.878 23.421  1.00 30.62 ? 285  LEU B CD2 1 
ATOM   2130 N N   . ASN A 1 288 ? 16.711  -15.195 22.325  1.00 25.00 ? 286  ASN B N   1 
ATOM   2131 C CA  . ASN A 1 288 ? 15.537  -14.709 21.569  1.00 26.64 ? 286  ASN B CA  1 
ATOM   2132 C C   . ASN A 1 288 ? 16.032  -13.716 20.525  1.00 25.25 ? 286  ASN B C   1 
ATOM   2133 O O   . ASN A 1 288 ? 15.595  -13.798 19.368  1.00 24.63 ? 286  ASN B O   1 
ATOM   2134 C CB  . ASN A 1 288 ? 14.477  -14.060 22.462  1.00 31.08 ? 286  ASN B CB  1 
ATOM   2135 C CG  . ASN A 1 288 ? 13.313  -13.530 21.650  1.00 36.44 ? 286  ASN B CG  1 
ATOM   2136 O OD1 . ASN A 1 288 ? 12.487  -14.301 21.169  1.00 48.91 ? 286  ASN B OD1 1 
ATOM   2137 N ND2 . ASN A 1 288 ? 13.238  -12.214 21.496  1.00 41.95 ? 286  ASN B ND2 1 
ATOM   2138 N N   . CYS A 1 289 ? 16.905  -12.792 20.909  1.00 22.39 ? 287  CYS B N   1 
ATOM   2139 C CA  . CYS A 1 289 ? 17.318  -11.731 19.962  1.00 22.71 ? 287  CYS B CA  1 
ATOM   2140 C C   . CYS A 1 289 ? 18.286  -12.286 18.905  1.00 21.57 ? 287  CYS B C   1 
ATOM   2141 O O   . CYS A 1 289 ? 18.180  -11.889 17.753  1.00 23.07 ? 287  CYS B O   1 
ATOM   2142 C CB  . CYS A 1 289 ? 17.961  -10.588 20.734  1.00 22.80 ? 287  CYS B CB  1 
ATOM   2143 S SG  . CYS A 1 289 ? 16.803  -9.733  21.837  1.00 25.40 ? 287  CYS B SG  1 
ATOM   2144 N N   . MET A 1 290 ? 19.180  -13.174 19.317  1.00 23.31 ? 288  MET B N   1 
ATOM   2145 C CA  . MET A 1 290 ? 20.186  -13.741 18.393  1.00 21.16 ? 288  MET B CA  1 
ATOM   2146 C C   . MET A 1 290 ? 19.454  -14.621 17.370  1.00 22.46 ? 288  MET B C   1 
ATOM   2147 O O   . MET A 1 290 ? 19.942  -14.749 16.242  1.00 19.15 ? 288  MET B O   1 
ATOM   2148 C CB  . MET A 1 290 ? 21.247  -14.536 19.153  1.00 23.34 ? 288  MET B CB  1 
ATOM   2149 C CG  . MET A 1 290 ? 22.404  -15.016 18.251  1.00 23.12 ? 288  MET B CG  1 
ATOM   2150 S SD  . MET A 1 290 ? 23.229  -13.807 17.209  1.00 24.16 ? 288  MET B SD  1 
ATOM   2151 C CE  . MET A 1 290 ? 24.830  -13.642 18.001  1.00 25.77 ? 288  MET B CE  1 
ATOM   2152 N N   . PHE A 1 291 ? 18.261  -15.110 17.685  1.00 20.45 ? 289  PHE B N   1 
ATOM   2153 C CA  . PHE A 1 291 ? 17.508  -15.943 16.722  1.00 22.14 ? 289  PHE B CA  1 
ATOM   2154 C C   . PHE A 1 291 ? 17.150  -15.150 15.473  1.00 19.62 ? 289  PHE B C   1 
ATOM   2155 O O   . PHE A 1 291 ? 16.893  -15.771 14.433  1.00 20.18 ? 289  PHE B O   1 
ATOM   2156 C CB  . PHE A 1 291 ? 16.301  -16.624 17.355  1.00 23.73 ? 289  PHE B CB  1 
ATOM   2157 C CG  . PHE A 1 291 ? 16.548  -18.103 17.530  1.00 24.22 ? 289  PHE B CG  1 
ATOM   2158 C CD1 . PHE A 1 291 ? 16.586  -18.928 16.413  1.00 25.57 ? 289  PHE B CD1 1 
ATOM   2159 C CD2 . PHE A 1 291 ? 16.736  -18.665 18.785  1.00 26.15 ? 289  PHE B CD2 1 
ATOM   2160 C CE1 . PHE A 1 291 ? 16.819  -20.295 16.540  1.00 27.56 ? 289  PHE B CE1 1 
ATOM   2161 C CE2 . PHE A 1 291 ? 16.973  -20.031 18.908  1.00 30.24 ? 289  PHE B CE2 1 
ATOM   2162 C CZ  . PHE A 1 291 ? 17.039  -20.835 17.783  1.00 27.81 ? 289  PHE B CZ  1 
ATOM   2163 N N   . THR A 1 292 ? 17.057  -13.818 15.542  1.00 19.74 ? 290  THR B N   1 
ATOM   2164 C CA  . THR A 1 292 ? 16.832  -13.007 14.330  1.00 19.88 ? 290  THR B CA  1 
ATOM   2165 C C   . THR A 1 292 ? 17.967  -13.289 13.354  1.00 20.20 ? 290  THR B C   1 
ATOM   2166 O O   . THR A 1 292 ? 17.697  -13.517 12.162  1.00 20.03 ? 290  THR B O   1 
ATOM   2167 C CB  . THR A 1 292 ? 16.730  -11.516 14.690  1.00 20.64 ? 290  THR B CB  1 
ATOM   2168 O OG1 . THR A 1 292 ? 15.542  -11.430 15.474  1.00 22.00 ? 290  THR B OG1 1 
ATOM   2169 C CG2 . THR A 1 292 ? 16.655  -10.652 13.463  1.00 21.28 ? 290  THR B CG2 1 
ATOM   2170 N N   . PHE A 1 293 ? 19.190  -13.227 13.859  1.00 19.25 ? 291  PHE B N   1 
ATOM   2171 C CA  . PHE A 1 293 ? 20.429  -13.449 13.085  1.00 17.89 ? 291  PHE B CA  1 
ATOM   2172 C C   . PHE A 1 293 ? 20.434  -14.921 12.652  1.00 17.42 ? 291  PHE B C   1 
ATOM   2173 O O   . PHE A 1 293 ? 20.685  -15.208 11.493  1.00 17.54 ? 291  PHE B O   1 
ATOM   2174 C CB  . PHE A 1 293 ? 21.630  -13.114 13.967  1.00 18.32 ? 291  PHE B CB  1 
ATOM   2175 C CG  . PHE A 1 293 ? 22.844  -12.613 13.252  1.00 19.78 ? 291  PHE B CG  1 
ATOM   2176 C CD1 . PHE A 1 293 ? 23.228  -13.128 12.026  1.00 20.77 ? 291  PHE B CD1 1 
ATOM   2177 C CD2 . PHE A 1 293 ? 23.615  -11.607 13.810  1.00 19.24 ? 291  PHE B CD2 1 
ATOM   2178 C CE1 . PHE A 1 293 ? 24.366  -12.657 11.391  1.00 19.52 ? 291  PHE B CE1 1 
ATOM   2179 C CE2 . PHE A 1 293 ? 24.744  -11.143 13.161  1.00 20.62 ? 291  PHE B CE2 1 
ATOM   2180 C CZ  . PHE A 1 293 ? 25.127  -11.674 11.962  1.00 20.00 ? 291  PHE B CZ  1 
ATOM   2181 N N   . MET A 1 294 ? 20.198  -15.815 13.592  1.00 18.42 ? 292  MET B N   1 
ATOM   2182 C CA  . MET A 1 294 ? 20.306  -17.272 13.292  1.00 18.81 ? 292  MET B CA  1 
ATOM   2183 C C   . MET A 1 294 ? 19.296  -17.681 12.211  1.00 20.51 ? 292  MET B C   1 
ATOM   2184 O O   . MET A 1 294 ? 19.656  -18.449 11.334  1.00 18.81 ? 292  MET B O   1 
ATOM   2185 C CB  . MET A 1 294 ? 20.091  -18.080 14.575  1.00 21.42 ? 292  MET B CB  1 
ATOM   2186 C CG  . MET A 1 294 ? 21.184  -17.847 15.592  1.00 23.49 ? 292  MET B CG  1 
ATOM   2187 S SD  . MET A 1 294 ? 20.683  -18.252 17.279  1.00 30.41 ? 292  MET B SD  1 
ATOM   2188 C CE  . MET A 1 294 ? 20.370  -20.005 17.105  1.00 28.72 ? 292  MET B CE  1 
ATOM   2189 N N   . ASN A 1 295 ? 18.081  -17.143 12.269  1.00 17.22 ? 293  ASN B N   1 
ATOM   2190 C CA  . ASN A 1 295 ? 17.075  -17.463 11.216  1.00 18.46 ? 293  ASN B CA  1 
ATOM   2191 C C   . ASN A 1 295 ? 17.498  -16.874 9.863   1.00 17.88 ? 293  ASN B C   1 
ATOM   2192 O O   . ASN A 1 295 ? 17.234  -17.524 8.856   1.00 17.09 ? 293  ASN B O   1 
ATOM   2193 C CB  . ASN A 1 295 ? 15.647  -17.128 11.647  1.00 18.43 ? 293  ASN B CB  1 
ATOM   2194 C CG  . ASN A 1 295 ? 15.120  -18.128 12.653  1.00 20.74 ? 293  ASN B CG  1 
ATOM   2195 O OD1 . ASN A 1 295 ? 15.461  -19.306 12.599  1.00 23.00 ? 293  ASN B OD1 1 
ATOM   2196 N ND2 . ASN A 1 295 ? 14.304  -17.669 13.583  1.00 23.39 ? 293  ASN B ND2 1 
ATOM   2197 N N   . THR A 1 296 ? 18.098  -15.680 9.843   1.00 17.18 ? 294  THR B N   1 
ATOM   2198 C CA  . THR A 1 296 ? 18.652  -15.185 8.569   1.00 17.01 ? 294  THR B CA  1 
ATOM   2199 C C   . THR A 1 296 ? 19.715  -16.184 8.067   1.00 17.05 ? 294  THR B C   1 
ATOM   2200 O O   . THR A 1 296 ? 19.781  -16.454 6.862   1.00 16.46 ? 294  THR B O   1 
ATOM   2201 C CB  . THR A 1 296 ? 19.217  -13.775 8.719   1.00 20.48 ? 294  THR B CB  1 
ATOM   2202 O OG1 . THR A 1 296 ? 18.119  -12.964 9.186   1.00 21.66 ? 294  THR B OG1 1 
ATOM   2203 C CG2 . THR A 1 296 ? 19.779  -13.267 7.411   1.00 20.21 ? 294  THR B CG2 1 
ATOM   2204 N N   . ALA A 1 297 ? 20.558  -16.670 8.966   1.00 16.94 ? 295  ALA B N   1 
ATOM   2205 C CA  . ALA A 1 297 ? 21.658  -17.567 8.556   1.00 15.98 ? 295  ALA B CA  1 
ATOM   2206 C C   . ALA A 1 297 ? 21.099  -18.897 8.043   1.00 17.17 ? 295  ALA B C   1 
ATOM   2207 O O   . ALA A 1 297 ? 21.680  -19.459 7.127   1.00 16.94 ? 295  ALA B O   1 
ATOM   2208 C CB  . ALA A 1 297 ? 22.569  -17.789 9.727   1.00 16.78 ? 295  ALA B CB  1 
ATOM   2209 N N   . ARG A 1 298 ? 20.019  -19.372 8.654   1.00 15.65 ? 296  ARG B N   1 
ATOM   2210 C CA  . ARG A 1 298 ? 19.405  -20.664 8.233   1.00 15.60 ? 296  ARG B CA  1 
ATOM   2211 C C   . ARG A 1 298 ? 18.804  -20.554 6.819   1.00 15.92 ? 296  ARG B C   1 
ATOM   2212 O O   . ARG A 1 298 ? 19.009  -21.445 6.018   1.00 16.64 ? 296  ARG B O   1 
ATOM   2213 C CB  . ARG A 1 298 ? 18.421  -21.126 9.310   1.00 15.05 ? 296  ARG B CB  1 
ATOM   2214 C CG  . ARG A 1 298 ? 19.123  -21.489 10.610  1.00 16.20 ? 296  ARG B CG  1 
ATOM   2215 C CD  . ARG A 1 298 ? 18.269  -21.930 11.781  1.00 18.41 ? 296  ARG B CD  1 
ATOM   2216 N NE  . ARG A 1 298 ? 19.163  -22.202 12.897  1.00 20.50 ? 296  ARG B NE  1 
ATOM   2217 C CZ  . ARG A 1 298 ? 18.826  -22.809 14.028  1.00 20.93 ? 296  ARG B CZ  1 
ATOM   2218 N NH1 . ARG A 1 298 ? 19.734  -22.996 14.968  1.00 24.41 ? 296  ARG B NH1 1 
ATOM   2219 N NH2 . ARG A 1 298 ? 17.589  -23.221 14.224  1.00 20.93 ? 296  ARG B NH2 1 
ATOM   2220 N N   . LEU A 1 299 ? 18.085  -19.476 6.545   1.00 16.38 ? 297  LEU B N   1 
ATOM   2221 C CA  . LEU A 1 299 ? 17.546  -19.288 5.175   1.00 16.14 ? 297  LEU B CA  1 
ATOM   2222 C C   . LEU A 1 299 ? 18.697  -19.055 4.186   1.00 15.60 ? 297  LEU B C   1 
ATOM   2223 O O   . LEU A 1 299 ? 18.604  -19.496 3.061   1.00 16.76 ? 297  LEU B O   1 
ATOM   2224 C CB  . LEU A 1 299 ? 16.573  -18.106 5.178   1.00 17.49 ? 297  LEU B CB  1 
ATOM   2225 C CG  . LEU A 1 299 ? 15.261  -18.339 5.919   1.00 23.45 ? 297  LEU B CG  1 
ATOM   2226 C CD1 . LEU A 1 299 ? 14.417  -17.075 5.905   1.00 27.20 ? 297  LEU B CD1 1 
ATOM   2227 C CD2 . LEU A 1 299 ? 14.493  -19.496 5.300   1.00 25.03 ? 297  LEU B CD2 1 
ATOM   2228 N N   . GLY A 1 300 ? 19.733  -18.364 4.632   1.00 15.83 ? 298  GLY B N   1 
ATOM   2229 C CA  . GLY A 1 300 ? 20.880  -18.103 3.750   1.00 16.19 ? 298  GLY B CA  1 
ATOM   2230 C C   . GLY A 1 300 ? 21.628  -19.378 3.433   1.00 14.67 ? 298  GLY B C   1 
ATOM   2231 O O   . GLY A 1 300 ? 22.113  -19.512 2.329   1.00 15.93 ? 298  GLY B O   1 
ATOM   2232 N N   . THR A 1 301 ? 21.726  -20.259 4.417   1.00 15.01 ? 299  THR B N   1 
ATOM   2233 C CA  A THR A 1 301 ? 22.412  -21.566 4.198   0.50 14.58 ? 299  THR B CA  1 
ATOM   2234 C CA  B THR A 1 301 ? 22.406  -21.568 4.206   0.50 14.58 ? 299  THR B CA  1 
ATOM   2235 C C   . THR A 1 301 ? 21.569  -22.520 3.303   1.00 15.35 ? 299  THR B C   1 
ATOM   2236 O O   . THR A 1 301 ? 22.006  -23.430 2.493   1.00 14.18 ? 299  THR B O   1 
ATOM   2237 C CB  A THR A 1 301 ? 22.884  -22.151 5.542   0.50 14.54 ? 299  THR B CB  1 
ATOM   2238 C CB  B THR A 1 301 ? 22.826  -22.155 5.564   0.50 14.54 ? 299  THR B CB  1 
ATOM   2239 O OG1 A THR A 1 301 ? 21.799  -22.192 6.464   0.50 13.27 ? 299  THR B OG1 1 
ATOM   2240 O OG1 B THR A 1 301 ? 23.720  -21.217 6.162   0.50 13.27 ? 299  THR B OG1 1 
ATOM   2241 C CG2 A THR A 1 301 ? 24.014  -21.343 6.141   0.50 14.05 ? 299  THR B CG2 1 
ATOM   2242 C CG2 B THR A 1 301 ? 23.518  -23.491 5.435   0.50 14.05 ? 299  THR B CG2 1 
ATOM   2243 N N   . ALA A 1 302 ? 20.249  -22.341 3.392   1.00 14.45 ? 300  ALA B N   1 
ATOM   2244 C CA  . ALA A 1 302 ? 19.367  -23.106 2.474   1.00 14.50 ? 300  ALA B CA  1 
ATOM   2245 C C   . ALA A 1 302 ? 19.695  -22.647 1.053   1.00 14.77 ? 300  ALA B C   1 
ATOM   2246 O O   . ALA A 1 302 ? 19.759  -23.467 0.145   1.00 14.26 ? 300  ALA B O   1 
ATOM   2247 C CB  . ALA A 1 302 ? 17.920  -22.828 2.812   1.00 14.81 ? 300  ALA B CB  1 
ATOM   2248 N N   . LEU A 1 303 ? 19.919  -21.348 0.906   1.00 14.43 ? 301  LEU B N   1 
ATOM   2249 C CA  . LEU A 1 303 ? 20.285  -20.783 -0.410  1.00 15.49 ? 301  LEU B CA  1 
ATOM   2250 C C   . LEU A 1 303 ? 21.651  -21.353 -0.834  1.00 14.66 ? 301  LEU B C   1 
ATOM   2251 O O   . LEU A 1 303 ? 21.869  -21.533 -2.016  1.00 15.25 ? 301  LEU B O   1 
ATOM   2252 C CB  . LEU A 1 303 ? 20.268  -19.258 -0.243  1.00 18.58 ? 301  LEU B CB  1 
ATOM   2253 C CG  . LEU A 1 303 ? 20.624  -18.411 -1.459  1.00 19.13 ? 301  LEU B CG  1 
ATOM   2254 C CD1 . LEU A 1 303 ? 19.866  -17.094 -1.404  1.00 19.57 ? 301  LEU B CD1 1 
ATOM   2255 C CD2 . LEU A 1 303 ? 22.119  -18.147 -1.497  1.00 18.27 ? 301  LEU B CD2 1 
ATOM   2256 N N   . GLN A 1 304 ? 22.533  -21.608 0.134   1.00 14.23 ? 302  GLN B N   1 
ATOM   2257 C CA  . GLN A 1 304 ? 23.834  -22.262 -0.174  1.00 14.31 ? 302  GLN B CA  1 
ATOM   2258 C C   . GLN A 1 304 ? 23.569  -23.670 -0.721  1.00 13.65 ? 302  GLN B C   1 
ATOM   2259 O O   . GLN A 1 304 ? 24.214  -24.041 -1.680  1.00 13.44 ? 302  GLN B O   1 
ATOM   2260 C CB  . GLN A 1 304 ? 24.748  -22.324 1.057   1.00 13.87 ? 302  GLN B CB  1 
ATOM   2261 C CG  . GLN A 1 304 ? 26.100  -22.945 0.749   1.00 14.26 ? 302  GLN B CG  1 
ATOM   2262 C CD  . GLN A 1 304 ? 26.989  -23.103 1.957   1.00 14.22 ? 302  GLN B CD  1 
ATOM   2263 O OE1 . GLN A 1 304 ? 26.641  -22.709 3.064   1.00 14.67 ? 302  GLN B OE1 1 
ATOM   2264 N NE2 . GLN A 1 304 ? 28.151  -23.693 1.740   1.00 15.20 ? 302  GLN B NE2 1 
ATOM   2265 N N   . GLY A 1 305 ? 22.654  -24.401 -0.088  1.00 13.45 ? 303  GLY B N   1 
ATOM   2266 C CA  . GLY A 1 305 ? 22.286  -25.743 -0.577  1.00 12.94 ? 303  GLY B CA  1 
ATOM   2267 C C   . GLY A 1 305 ? 21.809  -25.661 -2.016  1.00 14.23 ? 303  GLY B C   1 
ATOM   2268 O O   . GLY A 1 305 ? 22.225  -26.482 -2.825  1.00 14.06 ? 303  GLY B O   1 
ATOM   2269 N N   . LEU A 1 306 ? 20.941  -24.699 -2.304  1.00 13.42 ? 304  LEU B N   1 
ATOM   2270 C CA  . LEU A 1 306 ? 20.473  -24.480 -3.695  1.00 13.26 ? 304  LEU B CA  1 
ATOM   2271 C C   . LEU A 1 306 ? 21.669  -24.195 -4.609  1.00 13.28 ? 304  LEU B C   1 
ATOM   2272 O O   . LEU A 1 306 ? 21.699  -24.754 -5.689  1.00 14.67 ? 304  LEU B O   1 
ATOM   2273 C CB  . LEU A 1 306 ? 19.498  -23.292 -3.679  1.00 14.87 ? 304  LEU B CB  1 
ATOM   2274 C CG  . LEU A 1 306 ? 19.100  -22.760 -5.056  1.00 14.84 ? 304  LEU B CG  1 
ATOM   2275 C CD1 . LEU A 1 306 ? 18.470  -23.854 -5.905  1.00 15.90 ? 304  LEU B CD1 1 
ATOM   2276 C CD2 . LEU A 1 306 ? 18.154  -21.576 -4.930  1.00 14.50 ? 304  LEU B CD2 1 
ATOM   2277 N N   . ALA A 1 307 ? 22.603  -23.374 -4.160  1.00 13.93 ? 305  ALA B N   1 
ATOM   2278 C CA  . ALA A 1 307 ? 23.786  -22.957 -4.946  1.00 13.37 ? 305  ALA B CA  1 
ATOM   2279 C C   . ALA A 1 307 ? 24.621  -24.169 -5.352  1.00 13.67 ? 305  ALA B C   1 
ATOM   2280 O O   . ALA A 1 307 ? 25.042  -24.263 -6.520  1.00 14.14 ? 305  ALA B O   1 
ATOM   2281 C CB  . ALA A 1 307 ? 24.581  -21.969 -4.146  1.00 14.21 ? 305  ALA B CB  1 
ATOM   2282 N N   . HIS A 1 308 ? 24.813  -25.116 -4.447  1.00 13.85 ? 306  HIS B N   1 
ATOM   2283 C CA  . HIS A 1 308 ? 25.685  -26.273 -4.773  1.00 14.33 ? 306  HIS B CA  1 
ATOM   2284 C C   . HIS A 1 308 ? 25.013  -27.179 -5.820  1.00 12.63 ? 306  HIS B C   1 
ATOM   2285 O O   . HIS A 1 308 ? 25.718  -27.767 -6.625  1.00 13.84 ? 306  HIS B O   1 
ATOM   2286 C CB  . HIS A 1 308 ? 26.064  -26.973 -3.465  1.00 14.37 ? 306  HIS B CB  1 
ATOM   2287 C CG  . HIS A 1 308 ? 26.939  -26.118 -2.610  1.00 12.89 ? 306  HIS B CG  1 
ATOM   2288 N ND1 . HIS A 1 308 ? 28.140  -25.612 -3.062  1.00 14.11 ? 306  HIS B ND1 1 
ATOM   2289 C CD2 . HIS A 1 308 ? 26.784  -25.653 -1.354  1.00 13.86 ? 306  HIS B CD2 1 
ATOM   2290 C CE1 . HIS A 1 308 ? 28.694  -24.887 -2.115  1.00 13.77 ? 306  HIS B CE1 1 
ATOM   2291 N NE2 . HIS A 1 308 ? 27.880  -24.892 -1.063  1.00 14.63 ? 306  HIS B NE2 1 
ATOM   2292 N N   . ALA A 1 309 ? 23.695  -27.293 -5.746  1.00 12.80 ? 307  ALA B N   1 
ATOM   2293 C CA  . ALA A 1 309 ? 22.953  -28.070 -6.763  1.00 13.12 ? 307  ALA B CA  1 
ATOM   2294 C C   . ALA A 1 309 ? 23.046  -27.354 -8.103  1.00 13.04 ? 307  ALA B C   1 
ATOM   2295 O O   . ALA A 1 309 ? 23.226  -27.984 -9.137  1.00 14.78 ? 307  ALA B O   1 
ATOM   2296 C CB  . ALA A 1 309 ? 21.530  -28.268 -6.355  1.00 13.19 ? 307  ALA B CB  1 
ATOM   2297 N N   . GLU A 1 310 ? 22.856  -26.045 -8.081  1.00 14.48 ? 308  GLU B N   1 
ATOM   2298 C CA  . GLU A 1 310 ? 22.893  -25.252 -9.333  1.00 13.59 ? 308  GLU B CA  1 
ATOM   2299 C C   . GLU A 1 310 ? 24.272  -25.361 -10.003 1.00 14.06 ? 308  GLU B C   1 
ATOM   2300 O O   . GLU A 1 310 ? 24.326  -25.558 -11.207 1.00 15.07 ? 308  GLU B O   1 
ATOM   2301 C CB  . GLU A 1 310 ? 22.570  -23.798 -8.998  1.00 13.86 ? 308  GLU B CB  1 
ATOM   2302 C CG  . GLU A 1 310 ? 22.638  -22.874 -10.196 1.00 14.82 ? 308  GLU B CG  1 
ATOM   2303 C CD  . GLU A 1 310 ? 21.673  -23.231 -11.312 1.00 15.54 ? 308  GLU B CD  1 
ATOM   2304 O OE1 . GLU A 1 310 ? 22.042  -23.054 -12.472 1.00 18.23 ? 308  GLU B OE1 1 
ATOM   2305 O OE2 . GLU A 1 310 ? 20.563  -23.689 -11.009 1.00 17.23 ? 308  GLU B OE2 1 
ATOM   2306 N N   . VAL A 1 311 ? 25.333  -25.167 -9.223  1.00 15.93 ? 309  VAL B N   1 
ATOM   2307 C CA  . VAL A 1 311 ? 26.714  -25.218 -9.791  1.00 17.13 ? 309  VAL B CA  1 
ATOM   2308 C C   . VAL A 1 311 ? 27.013  -26.646 -10.273 1.00 15.50 ? 309  VAL B C   1 
ATOM   2309 O O   . VAL A 1 311 ? 27.604  -26.794 -11.328 1.00 16.41 ? 309  VAL B O   1 
ATOM   2310 C CB  . VAL A 1 311 ? 27.740  -24.713 -8.759  1.00 17.84 ? 309  VAL B CB  1 
ATOM   2311 C CG1 . VAL A 1 311 ? 29.163  -25.079 -9.139  1.00 20.31 ? 309  VAL B CG1 1 
ATOM   2312 C CG2 . VAL A 1 311 ? 27.605  -23.214 -8.558  1.00 19.75 ? 309  VAL B CG2 1 
ATOM   2313 N N   . GLY A 1 312 ? 26.614  -27.643 -9.498  1.00 15.70 ? 310  GLY B N   1 
ATOM   2314 C CA  . GLY A 1 312 ? 26.759  -29.053 -9.908  1.00 14.05 ? 310  GLY B CA  1 
ATOM   2315 C C   . GLY A 1 312 ? 26.141  -29.235 -11.283 1.00 14.66 ? 310  GLY B C   1 
ATOM   2316 O O   . GLY A 1 312 ? 26.755  -29.868 -12.163 1.00 14.73 ? 310  GLY B O   1 
ATOM   2317 N N   . PHE A 1 313 ? 24.921  -28.736 -11.430 1.00 13.85 ? 311  PHE B N   1 
ATOM   2318 C CA  . PHE A 1 313 ? 24.164  -28.929 -12.676 1.00 15.24 ? 311  PHE B CA  1 
ATOM   2319 C C   . PHE A 1 313 ? 24.898  -28.220 -13.812 1.00 15.08 ? 311  PHE B C   1 
ATOM   2320 O O   . PHE A 1 313 ? 25.021  -28.807 -14.909 1.00 15.95 ? 311  PHE B O   1 
ATOM   2321 C CB  . PHE A 1 313 ? 22.730  -28.413 -12.554 1.00 15.24 ? 311  PHE B CB  1 
ATOM   2322 C CG  . PHE A 1 313 ? 21.972  -28.618 -13.832 1.00 16.35 ? 311  PHE B CG  1 
ATOM   2323 C CD1 . PHE A 1 313 ? 21.582  -29.892 -14.217 1.00 16.36 ? 311  PHE B CD1 1 
ATOM   2324 C CD2 . PHE A 1 313 ? 21.747  -27.559 -14.703 1.00 19.31 ? 311  PHE B CD2 1 
ATOM   2325 C CE1 . PHE A 1 313 ? 20.960  -30.098 -15.434 1.00 18.17 ? 311  PHE B CE1 1 
ATOM   2326 C CE2 . PHE A 1 313 ? 21.137  -27.776 -15.924 1.00 19.31 ? 311  PHE B CE2 1 
ATOM   2327 C CZ  . PHE A 1 313 ? 20.743  -29.037 -16.279 1.00 18.52 ? 311  PHE B CZ  1 
ATOM   2328 N N   . GLN A 1 314 ? 25.308  -26.960 -13.606 1.00 15.57 ? 312  GLN B N   1 
ATOM   2329 C CA  . GLN A 1 314 ? 25.927  -26.165 -14.695 1.00 15.92 ? 312  GLN B CA  1 
ATOM   2330 C C   . GLN A 1 314 ? 27.174  -26.896 -15.209 1.00 17.00 ? 312  GLN B C   1 
ATOM   2331 O O   . GLN A 1 314 ? 27.390  -26.972 -16.445 1.00 17.18 ? 312  GLN B O   1 
ATOM   2332 C CB  . GLN A 1 314 ? 26.273  -24.753 -14.241 1.00 15.56 ? 312  GLN B CB  1 
ATOM   2333 C CG  . GLN A 1 314 ? 25.028  -23.903 -14.090 1.00 16.22 ? 312  GLN B CG  1 
ATOM   2334 C CD  . GLN A 1 314 ? 25.322  -22.433 -13.907 1.00 16.22 ? 312  GLN B CD  1 
ATOM   2335 O OE1 . GLN A 1 314 ? 26.278  -21.887 -14.461 1.00 18.69 ? 312  GLN B OE1 1 
ATOM   2336 N NE2 . GLN A 1 314 ? 24.445  -21.779 -13.175 1.00 17.26 ? 312  GLN B NE2 1 
ATOM   2337 N N   . GLY A 1 315 ? 28.008  -27.364 -14.311 1.00 15.83 ? 313  GLY B N   1 
ATOM   2338 C CA  . GLY A 1 315 ? 29.224  -28.101 -14.693 1.00 17.55 ? 313  GLY B CA  1 
ATOM   2339 C C   . GLY A 1 315 ? 28.865  -29.415 -15.380 1.00 17.29 ? 313  GLY B C   1 
ATOM   2340 O O   . GLY A 1 315 ? 29.385  -29.728 -16.485 1.00 16.64 ? 313  GLY B O   1 
ATOM   2341 N N   . GLY A 1 316 ? 27.962  -30.186 -14.775 1.00 15.97 ? 314  GLY B N   1 
ATOM   2342 C CA  . GLY A 1 316 ? 27.559  -31.498 -15.320 1.00 15.45 ? 314  GLY B CA  1 
ATOM   2343 C C   . GLY A 1 316 ? 26.959  -31.425 -16.715 1.00 16.65 ? 314  GLY B C   1 
ATOM   2344 O O   . GLY A 1 316 ? 27.306  -32.269 -17.530 1.00 16.36 ? 314  GLY B O   1 
ATOM   2345 N N   . ILE A 1 317 ? 26.045  -30.499 -16.990 1.00 15.96 ? 315  ILE B N   1 
ATOM   2346 C CA  . ILE A 1 317 ? 25.408  -30.446 -18.333 1.00 15.98 ? 315  ILE B CA  1 
ATOM   2347 C C   . ILE A 1 317 ? 26.450  -30.060 -19.391 1.00 17.02 ? 315  ILE B C   1 
ATOM   2348 O O   . ILE A 1 317 ? 26.389  -30.661 -20.514 1.00 18.03 ? 315  ILE B O   1 
ATOM   2349 C CB  . ILE A 1 317 ? 24.138  -29.566 -18.382 1.00 15.93 ? 315  ILE B CB  1 
ATOM   2350 C CG1 . ILE A 1 317 ? 23.380  -29.796 -19.703 1.00 17.41 ? 315  ILE B CG1 1 
ATOM   2351 C CG2 . ILE A 1 317 ? 24.409  -28.079 -18.157 1.00 16.24 ? 315  ILE B CG2 1 
ATOM   2352 C CD1 . ILE A 1 317 ? 22.930  -31.240 -19.947 1.00 17.48 ? 315  ILE B CD1 1 
ATOM   2353 N N   . ALA A 1 318 ? 27.337  -29.116 -19.091 1.00 17.30 ? 316  ALA B N   1 
ATOM   2354 C CA  . ALA A 1 318 ? 28.399  -28.714 -20.044 1.00 20.46 ? 316  ALA B CA  1 
ATOM   2355 C C   . ALA A 1 318 ? 29.253  -29.933 -20.389 1.00 19.73 ? 316  ALA B C   1 
ATOM   2356 O O   . ALA A 1 318 ? 29.514  -30.221 -21.589 1.00 20.67 ? 316  ALA B O   1 
ATOM   2357 C CB  . ALA A 1 318 ? 29.253  -27.619 -19.485 1.00 19.69 ? 316  ALA B CB  1 
ATOM   2358 N N   . TYR A 1 319 ? 29.692  -30.665 -19.384 1.00 18.41 ? 317  TYR B N   1 
ATOM   2359 C CA  . TYR A 1 319 ? 30.598  -31.820 -19.613 1.00 19.54 ? 317  TYR B CA  1 
ATOM   2360 C C   . TYR A 1 319 ? 29.844  -32.924 -20.363 1.00 19.46 ? 317  TYR B C   1 
ATOM   2361 O O   . TYR A 1 319 ? 30.435  -33.548 -21.252 1.00 20.26 ? 317  TYR B O   1 
ATOM   2362 C CB  . TYR A 1 319 ? 31.162  -32.325 -18.287 1.00 21.45 ? 317  TYR B CB  1 
ATOM   2363 C CG  . TYR A 1 319 ? 32.347  -33.244 -18.464 1.00 20.37 ? 317  TYR B CG  1 
ATOM   2364 C CD1 . TYR A 1 319 ? 33.560  -32.706 -18.870 1.00 25.50 ? 317  TYR B CD1 1 
ATOM   2365 C CD2 . TYR A 1 319 ? 32.253  -34.614 -18.301 1.00 19.18 ? 317  TYR B CD2 1 
ATOM   2366 C CE1 . TYR A 1 319 ? 34.675  -33.511 -19.053 1.00 25.79 ? 317  TYR B CE1 1 
ATOM   2367 C CE2 . TYR A 1 319 ? 33.363  -35.426 -18.470 1.00 23.01 ? 317  TYR B CE2 1 
ATOM   2368 C CZ  . TYR A 1 319 ? 34.573  -34.874 -18.841 1.00 23.81 ? 317  TYR B CZ  1 
ATOM   2369 O OH  . TYR A 1 319 ? 35.687  -35.641 -19.035 1.00 27.21 ? 317  TYR B OH  1 
ATOM   2370 N N   . ALA A 1 320 ? 28.581  -33.193 -20.005 1.00 17.82 ? 318  ALA B N   1 
ATOM   2371 C CA  . ALA A 1 320 ? 27.780  -34.291 -20.593 1.00 17.61 ? 318  ALA B CA  1 
ATOM   2372 C C   . ALA A 1 320 ? 27.507  -34.058 -22.084 1.00 18.53 ? 318  ALA B C   1 
ATOM   2373 O O   . ALA A 1 320 ? 27.361  -35.060 -22.800 1.00 19.95 ? 318  ALA B O   1 
ATOM   2374 C CB  . ALA A 1 320 ? 26.522  -34.493 -19.831 1.00 17.13 ? 318  ALA B CB  1 
ATOM   2375 N N   A ARG A 1 321 ? 27.491  -32.807 -22.534 0.50 18.88 ? 319  ARG B N   1 
ATOM   2376 N N   B ARG A 1 321 ? 27.461  -32.796 -22.536 0.50 19.65 ? 319  ARG B N   1 
ATOM   2377 C CA  A ARG A 1 321 ? 27.232  -32.510 -23.963 0.50 19.91 ? 319  ARG B CA  1 
ATOM   2378 C CA  B ARG A 1 321 ? 27.165  -32.461 -23.960 0.50 21.39 ? 319  ARG B CA  1 
ATOM   2379 C C   A ARG A 1 321 ? 28.537  -32.560 -24.747 0.50 21.83 ? 319  ARG B C   1 
ATOM   2380 C C   B ARG A 1 321 ? 28.486  -32.274 -24.741 0.50 23.35 ? 319  ARG B C   1 
ATOM   2381 O O   A ARG A 1 321 ? 28.476  -32.900 -25.944 0.50 21.34 ? 319  ARG B O   1 
ATOM   2382 O O   B ARG A 1 321 ? 28.404  -32.173 -25.988 0.50 23.73 ? 319  ARG B O   1 
ATOM   2383 C CB  A ARG A 1 321 ? 26.490  -31.181 -24.082 0.50 18.37 ? 319  ARG B CB  1 
ATOM   2384 C CB  B ARG A 1 321 ? 26.147  -31.300 -24.046 0.50 20.22 ? 319  ARG B CB  1 
ATOM   2385 C CG  A ARG A 1 321 ? 25.098  -31.288 -23.486 0.50 18.37 ? 319  ARG B CG  1 
ATOM   2386 C CG  B ARG A 1 321 ? 24.750  -31.639 -23.505 0.50 20.40 ? 319  ARG B CG  1 
ATOM   2387 C CD  A ARG A 1 321 ? 24.215  -30.167 -23.944 0.50 18.82 ? 319  ARG B CD  1 
ATOM   2388 C CD  B ARG A 1 321 ? 23.517  -30.748 -23.807 0.50 21.87 ? 319  ARG B CD  1 
ATOM   2389 N NE  A ARG A 1 321 ? 23.728  -30.405 -25.288 0.50 17.41 ? 319  ARG B NE  1 
ATOM   2390 N NE  B ARG A 1 321 ? 23.672  -29.358 -23.381 0.50 21.41 ? 319  ARG B NE  1 
ATOM   2391 C CZ  A ARG A 1 321 ? 23.147  -29.450 -25.996 0.50 17.92 ? 319  ARG B CZ  1 
ATOM   2392 C CZ  B ARG A 1 321 ? 22.734  -28.457 -23.022 0.50 20.18 ? 319  ARG B CZ  1 
ATOM   2393 N NH1 A ARG A 1 321 ? 22.962  -28.265 -25.444 0.50 16.84 ? 319  ARG B NH1 1 
ATOM   2394 N NH1 B ARG A 1 321 ? 21.421  -28.706 -22.961 0.50 20.05 ? 319  ARG B NH1 1 
ATOM   2395 N NH2 A ARG A 1 321 ? 22.743  -29.678 -27.225 0.50 19.02 ? 319  ARG B NH2 1 
ATOM   2396 N NH2 B ARG A 1 321 ? 23.175  -27.263 -22.681 0.50 16.33 ? 319  ARG B NH2 1 
ATOM   2397 N N   . GLU A 1 322 ? 29.659  -32.286 -24.086 1.00 22.51 ? 320  GLU B N   1 
ATOM   2398 C CA  . GLU A 1 322 ? 30.966  -32.100 -24.757 1.00 29.96 ? 320  GLU B CA  1 
ATOM   2399 C C   . GLU A 1 322 ? 31.777  -33.404 -24.718 1.00 35.00 ? 320  GLU B C   1 
ATOM   2400 O O   . GLU A 1 322 ? 32.468  -33.689 -25.717 1.00 33.57 ? 320  GLU B O   1 
ATOM   2401 C CB  . GLU A 1 322 ? 31.721  -30.957 -24.086 1.00 36.99 ? 320  GLU B CB  1 
ATOM   2402 C CG  . GLU A 1 322 ? 33.151  -30.827 -24.554 1.00 45.60 ? 320  GLU B CG  1 
ATOM   2403 C CD  . GLU A 1 322 ? 33.823  -29.527 -24.157 1.00 54.32 ? 320  GLU B CD  1 
ATOM   2404 O OE1 . GLU A 1 322 ? 35.058  -29.548 -23.958 1.00 65.73 ? 320  GLU B OE1 1 
ATOM   2405 O OE2 . GLU A 1 322 ? 33.115  -28.496 -24.048 1.00 63.58 ? 320  GLU B OE2 1 
ATOM   2406 N N   . ARG A 1 323 ? 31.771  -34.135 -23.590 1.00 28.76 ? 321  ARG B N   1 
ATOM   2407 C CA  . ARG A 1 323 ? 32.677  -35.306 -23.391 1.00 28.78 ? 321  ARG B CA  1 
ATOM   2408 C C   . ARG A 1 323 ? 32.107  -36.465 -24.211 1.00 29.51 ? 321  ARG B C   1 
ATOM   2409 O O   . ARG A 1 323 ? 30.899  -36.777 -24.005 1.00 25.55 ? 321  ARG B O   1 
ATOM   2410 C CB  . ARG A 1 323 ? 32.793  -35.687 -21.911 1.00 26.88 ? 321  ARG B CB  1 
ATOM   2411 C CG  . ARG A 1 323 ? 33.592  -36.963 -21.649 1.00 27.65 ? 321  ARG B CG  1 
ATOM   2412 C CD  . ARG A 1 323 ? 35.075  -36.865 -21.995 1.00 28.03 ? 321  ARG B CD  1 
ATOM   2413 N NE  . ARG A 1 323 ? 35.766  -38.047 -21.458 1.00 28.15 ? 321  ARG B NE  1 
ATOM   2414 C CZ  . ARG A 1 323 ? 37.083  -38.202 -21.336 1.00 27.35 ? 321  ARG B CZ  1 
ATOM   2415 N NH1 . ARG A 1 323 ? 37.922  -37.248 -21.693 1.00 29.45 ? 321  ARG B NH1 1 
ATOM   2416 N NH2 . ARG A 1 323 ? 37.558  -39.310 -20.792 1.00 29.91 ? 321  ARG B NH2 1 
ATOM   2417 N N   . LEU A 1 324 ? 32.889  -37.026 -25.150 1.00 28.21 ? 322  LEU B N   1 
ATOM   2418 C CA  . LEU A 1 324 ? 32.496  -38.234 -25.922 1.00 26.68 ? 322  LEU B CA  1 
ATOM   2419 C C   . LEU A 1 324 ? 33.071  -39.486 -25.225 1.00 26.78 ? 322  LEU B C   1 
ATOM   2420 O O   . LEU A 1 324 ? 34.293  -39.486 -24.954 1.00 28.45 ? 322  LEU B O   1 
ATOM   2421 C CB  . LEU A 1 324 ? 33.067  -38.152 -27.349 1.00 27.31 ? 322  LEU B CB  1 
ATOM   2422 C CG  . LEU A 1 324 ? 32.856  -36.843 -28.103 1.00 28.74 ? 322  LEU B CG  1 
ATOM   2423 C CD1 . LEU A 1 324 ? 33.394  -36.975 -29.525 1.00 31.68 ? 322  LEU B CD1 1 
ATOM   2424 C CD2 . LEU A 1 324 ? 31.369  -36.471 -28.131 1.00 28.03 ? 322  LEU B CD2 1 
ATOM   2425 N N   . GLN A 1 325 ? 32.269  -40.530 -24.993 1.00 26.97 ? 323  GLN B N   1 
ATOM   2426 C CA  . GLN A 1 325 ? 32.740  -41.758 -24.279 1.00 26.91 ? 323  GLN B CA  1 
ATOM   2427 C C   . GLN A 1 325 ? 31.709  -42.872 -24.467 1.00 29.76 ? 323  GLN B C   1 
ATOM   2428 O O   . GLN A 1 325 ? 30.554  -42.700 -24.035 1.00 27.49 ? 323  GLN B O   1 
ATOM   2429 C CB  . GLN A 1 325 ? 32.993  -41.480 -22.787 1.00 25.37 ? 323  GLN B CB  1 
ATOM   2430 C CG  . GLN A 1 325 ? 34.016  -42.411 -22.129 1.00 25.74 ? 323  GLN B CG  1 
ATOM   2431 C CD  . GLN A 1 325 ? 35.440  -42.117 -22.550 1.00 28.23 ? 323  GLN B CD  1 
ATOM   2432 O OE1 . GLN A 1 325 ? 35.747  -41.174 -23.292 1.00 28.52 ? 323  GLN B OE1 1 
ATOM   2433 N NE2 . GLN A 1 325 ? 36.341  -42.935 -22.058 1.00 26.11 ? 323  GLN B NE2 1 
ATOM   2434 N N   . MET A 1 326 ? 32.142  -43.995 -25.052 1.00 28.93 ? 324  MET B N   1 
ATOM   2435 C CA  . MET A 1 326 ? 31.324  -45.209 -25.289 1.00 30.04 ? 324  MET B CA  1 
ATOM   2436 C C   . MET A 1 326 ? 30.227  -44.855 -26.294 1.00 30.56 ? 324  MET B C   1 
ATOM   2437 O O   . MET A 1 326 ? 30.292  -43.757 -26.904 1.00 29.50 ? 324  MET B O   1 
ATOM   2438 C CB  . MET A 1 326 ? 30.729  -45.780 -23.991 1.00 32.52 ? 324  MET B CB  1 
ATOM   2439 C CG  . MET A 1 326 ? 31.785  -46.148 -22.933 1.00 32.22 ? 324  MET B CG  1 
ATOM   2440 S SD  . MET A 1 326 ? 32.953  -47.453 -23.501 1.00 36.30 ? 324  MET B SD  1 
ATOM   2441 C CE  . MET A 1 326 ? 31.900  -48.908 -23.430 1.00 36.97 ? 324  MET B CE  1 
ATOM   2442 N N   . ARG A 1 327 ? 29.261  -45.752 -26.451 1.00 33.82 ? 325  ARG B N   1 
ATOM   2443 C CA  . ARG A 1 327 ? 28.167  -45.530 -27.420 1.00 33.14 ? 325  ARG B CA  1 
ATOM   2444 C C   . ARG A 1 327 ? 26.821  -45.819 -26.757 1.00 30.91 ? 325  ARG B C   1 
ATOM   2445 O O   . ARG A 1 327 ? 26.797  -46.583 -25.796 1.00 32.45 ? 325  ARG B O   1 
ATOM   2446 C CB  . ARG A 1 327 ? 28.359  -46.448 -28.635 1.00 34.39 ? 325  ARG B CB  1 
ATOM   2447 C CG  . ARG A 1 327 ? 29.604  -46.149 -29.455 1.00 34.30 ? 325  ARG B CG  1 
ATOM   2448 C CD  . ARG A 1 327 ? 29.464  -44.868 -30.251 1.00 35.82 ? 325  ARG B CD  1 
ATOM   2449 N NE  . ARG A 1 327 ? 30.448  -44.810 -31.320 1.00 37.28 ? 325  ARG B NE  1 
ATOM   2450 C CZ  . ARG A 1 327 ? 30.635  -43.771 -32.125 1.00 37.97 ? 325  ARG B CZ  1 
ATOM   2451 N NH1 . ARG A 1 327 ? 29.901  -42.681 -31.990 1.00 31.37 ? 325  ARG B NH1 1 
ATOM   2452 N NH2 . ARG A 1 327 ? 31.560  -43.831 -33.065 1.00 39.33 ? 325  ARG B NH2 1 
ATOM   2453 N N   . SER A 1 328 ? 25.748  -45.236 -27.289 1.00 30.23 ? 326  SER B N   1 
ATOM   2454 C CA  . SER A 1 328 ? 24.381  -45.504 -26.785 1.00 29.89 ? 326  SER B CA  1 
ATOM   2455 C C   . SER A 1 328 ? 24.061  -46.999 -26.852 1.00 30.83 ? 326  SER B C   1 
ATOM   2456 O O   . SER A 1 328 ? 24.522  -47.664 -27.782 1.00 32.69 ? 326  SER B O   1 
ATOM   2457 C CB  . SER A 1 328 ? 23.353  -44.703 -27.562 1.00 31.95 ? 326  SER B CB  1 
ATOM   2458 O OG  . SER A 1 328 ? 22.067  -45.289 -27.468 1.00 32.65 ? 326  SER B OG  1 
ATOM   2459 N N   . LEU A 1 329 ? 23.272  -47.476 -25.902 1.00 31.70 ? 327  LEU B N   1 
ATOM   2460 C CA  . LEU A 1 329 ? 22.839  -48.896 -25.878 1.00 33.50 ? 327  LEU B CA  1 
ATOM   2461 C C   . LEU A 1 329 ? 21.930  -49.209 -27.068 1.00 34.70 ? 327  LEU B C   1 
ATOM   2462 O O   . LEU A 1 329 ? 21.784  -50.387 -27.382 1.00 34.02 ? 327  LEU B O   1 
ATOM   2463 C CB  . LEU A 1 329 ? 22.089  -49.102 -24.563 1.00 32.25 ? 327  LEU B CB  1 
ATOM   2464 C CG  . LEU A 1 329 ? 22.955  -49.021 -23.306 1.00 32.26 ? 327  LEU B CG  1 
ATOM   2465 C CD1 . LEU A 1 329 ? 22.112  -48.753 -22.067 1.00 28.37 ? 327  LEU B CD1 1 
ATOM   2466 C CD2 . LEU A 1 329 ? 23.768  -50.294 -23.135 1.00 34.66 ? 327  LEU B CD2 1 
ATOM   2467 N N   . THR A 1 330 ? 21.348  -48.187 -27.691 1.00 33.01 ? 328  THR B N   1 
ATOM   2468 C CA  . THR A 1 330 ? 20.439  -48.377 -28.856 1.00 33.82 ? 328  THR B CA  1 
ATOM   2469 C C   . THR A 1 330 ? 21.146  -48.012 -30.168 1.00 35.84 ? 328  THR B C   1 
ATOM   2470 O O   . THR A 1 330 ? 20.441  -47.653 -31.110 1.00 41.08 ? 328  THR B O   1 
ATOM   2471 C CB  . THR A 1 330 ? 19.136  -47.602 -28.630 1.00 32.83 ? 328  THR B CB  1 
ATOM   2472 O OG1 . THR A 1 330 ? 19.437  -46.257 -28.265 1.00 32.88 ? 328  THR B OG1 1 
ATOM   2473 C CG2 . THR A 1 330 ? 18.273  -48.239 -27.563 1.00 33.35 ? 328  THR B CG2 1 
ATOM   2474 N N   . GLY A 1 331 ? 22.474  -48.073 -30.208 1.00 34.63 ? 329  GLY B N   1 
ATOM   2475 C CA  . GLY A 1 331 ? 23.273  -47.843 -31.426 1.00 36.64 ? 329  GLY B CA  1 
ATOM   2476 C C   . GLY A 1 331 ? 23.959  -46.481 -31.421 1.00 37.24 ? 329  GLY B C   1 
ATOM   2477 O O   . GLY A 1 331 ? 23.451  -45.525 -30.823 1.00 39.37 ? 329  GLY B O   1 
ATOM   2478 N N   . PRO A 1 332 ? 25.152  -46.346 -32.051 1.00 38.91 ? 330  PRO B N   1 
ATOM   2479 C CA  . PRO A 1 332 ? 25.854  -45.059 -32.074 1.00 38.85 ? 330  PRO B CA  1 
ATOM   2480 C C   . PRO A 1 332 ? 24.934  -43.887 -32.451 1.00 38.37 ? 330  PRO B C   1 
ATOM   2481 O O   . PRO A 1 332 ? 24.309  -43.943 -33.479 1.00 36.52 ? 330  PRO B O   1 
ATOM   2482 C CB  . PRO A 1 332 ? 26.939  -45.293 -33.136 1.00 39.66 ? 330  PRO B CB  1 
ATOM   2483 C CG  . PRO A 1 332 ? 27.260  -46.757 -32.994 1.00 37.17 ? 330  PRO B CG  1 
ATOM   2484 C CD  . PRO A 1 332 ? 25.921  -47.416 -32.720 1.00 37.81 ? 330  PRO B CD  1 
ATOM   2485 N N   . LYS A 1 333 ? 24.891  -42.834 -31.635 1.00 34.35 ? 331  LYS B N   1 
ATOM   2486 C CA  . LYS A 1 333 ? 24.002  -41.670 -31.906 1.00 35.12 ? 331  LYS B CA  1 
ATOM   2487 C C   . LYS A 1 333 ? 24.813  -40.628 -32.679 1.00 35.67 ? 331  LYS B C   1 
ATOM   2488 O O   . LYS A 1 333 ? 24.189  -39.826 -33.383 1.00 39.46 ? 331  LYS B O   1 
ATOM   2489 C CB  . LYS A 1 333 ? 23.430  -41.144 -30.585 1.00 34.83 ? 331  LYS B CB  1 
ATOM   2490 C CG  . LYS A 1 333 ? 22.515  -42.107 -29.845 1.00 36.36 ? 331  LYS B CG  1 
ATOM   2491 C CD  . LYS A 1 333 ? 21.155  -42.231 -30.484 1.00 36.85 ? 331  LYS B CD  1 
ATOM   2492 C CE  . LYS A 1 333 ? 20.286  -43.279 -29.824 1.00 37.80 ? 331  LYS B CE  1 
ATOM   2493 N NZ  . LYS A 1 333 ? 20.781  -44.648 -30.091 1.00 37.94 ? 331  LYS B NZ  1 
ATOM   2494 N N   . ALA A 1 334 ? 26.132  -40.648 -32.544 1.00 36.73 ? 332  ALA B N   1 
ATOM   2495 C CA  . ALA A 1 334 ? 27.099  -39.772 -33.248 1.00 37.94 ? 332  ALA B CA  1 
ATOM   2496 C C   . ALA A 1 334 ? 28.108  -40.641 -33.997 1.00 40.22 ? 332  ALA B C   1 
ATOM   2497 O O   . ALA A 1 334 ? 29.310  -40.578 -33.730 1.00 38.57 ? 332  ALA B O   1 
ATOM   2498 C CB  . ALA A 1 334 ? 27.778  -38.857 -32.251 1.00 40.06 ? 332  ALA B CB  1 
ATOM   2499 N N   . PRO A 1 335 ? 27.658  -41.452 -34.986 1.00 44.81 ? 333  PRO B N   1 
ATOM   2500 C CA  . PRO A 1 335 ? 28.532  -42.415 -35.663 1.00 46.56 ? 333  PRO B CA  1 
ATOM   2501 C C   . PRO A 1 335 ? 29.664  -41.744 -36.457 1.00 48.89 ? 333  PRO B C   1 
ATOM   2502 O O   . PRO A 1 335 ? 30.632  -42.412 -36.788 1.00 52.44 ? 333  PRO B O   1 
ATOM   2503 C CB  . PRO A 1 335 ? 27.566  -43.167 -36.600 1.00 47.86 ? 333  PRO B CB  1 
ATOM   2504 C CG  . PRO A 1 335 ? 26.464  -42.171 -36.880 1.00 47.31 ? 333  PRO B CG  1 
ATOM   2505 C CD  . PRO A 1 335 ? 26.307  -41.411 -35.578 1.00 47.26 ? 333  PRO B CD  1 
ATOM   2506 N N   . GLU A 1 336 ? 29.517  -40.446 -36.738 1.00 50.31 ? 334  GLU B N   1 
ATOM   2507 C CA  . GLU A 1 336 ? 30.545  -39.580 -37.378 1.00 51.74 ? 334  GLU B CA  1 
ATOM   2508 C C   . GLU A 1 336 ? 31.715  -39.334 -36.410 1.00 50.80 ? 334  GLU B C   1 
ATOM   2509 O O   . GLU A 1 336 ? 32.837  -39.088 -36.904 1.00 47.37 ? 334  GLU B O   1 
ATOM   2510 C CB  . GLU A 1 336 ? 29.912  -38.268 -37.857 1.00 53.76 ? 334  GLU B CB  1 
ATOM   2511 C CG  . GLU A 1 336 ? 29.546  -37.281 -36.744 1.00 58.86 ? 334  GLU B CG  1 
ATOM   2512 C CD  . GLU A 1 336 ? 28.134  -37.364 -36.167 1.00 57.72 ? 334  GLU B CD  1 
ATOM   2513 O OE1 . GLU A 1 336 ? 27.677  -36.358 -35.547 1.00 62.58 ? 334  GLU B OE1 1 
ATOM   2514 O OE2 . GLU A 1 336 ? 27.486  -38.410 -36.333 1.00 46.39 ? 334  GLU B OE2 1 
ATOM   2515 N N   . LYS A 1 337 ? 31.474  -39.384 -35.093 1.00 43.94 ? 335  LYS B N   1 
ATOM   2516 C CA  . LYS A 1 337 ? 32.490  -39.076 -34.050 1.00 43.11 ? 335  LYS B CA  1 
ATOM   2517 C C   . LYS A 1 337 ? 33.067  -40.387 -33.529 1.00 41.49 ? 335  LYS B C   1 
ATOM   2518 O O   . LYS A 1 337 ? 32.459  -41.443 -33.708 1.00 38.50 ? 335  LYS B O   1 
ATOM   2519 C CB  . LYS A 1 337 ? 31.876  -38.247 -32.920 1.00 40.76 ? 335  LYS B CB  1 
ATOM   2520 C CG  . LYS A 1 337 ? 31.112  -37.029 -33.418 1.00 42.10 ? 335  LYS B CG  1 
ATOM   2521 C CD  . LYS A 1 337 ? 30.953  -35.913 -32.415 1.00 41.78 ? 335  LYS B CD  1 
ATOM   2522 C CE  . LYS A 1 337 ? 30.084  -34.802 -32.962 1.00 42.75 ? 335  LYS B CE  1 
ATOM   2523 N NZ  . LYS A 1 337 ? 29.882  -33.710 -31.979 1.00 46.20 ? 335  LYS B NZ  1 
ATOM   2524 N N   . PRO A 1 338 ? 34.285  -40.358 -32.930 1.00 36.78 ? 336  PRO B N   1 
ATOM   2525 C CA  . PRO A 1 338 ? 34.879  -41.550 -32.322 1.00 38.67 ? 336  PRO B CA  1 
ATOM   2526 C C   . PRO A 1 338 ? 34.000  -42.185 -31.225 1.00 35.91 ? 336  PRO B C   1 
ATOM   2527 O O   . PRO A 1 338 ? 34.094  -43.379 -31.015 1.00 35.25 ? 336  PRO B O   1 
ATOM   2528 C CB  . PRO A 1 338 ? 36.211  -41.049 -31.730 1.00 37.27 ? 336  PRO B CB  1 
ATOM   2529 C CG  . PRO A 1 338 ? 36.101  -39.540 -31.709 1.00 37.98 ? 336  PRO B CG  1 
ATOM   2530 C CD  . PRO A 1 338 ? 35.160  -39.180 -32.839 1.00 37.19 ? 336  PRO B CD  1 
ATOM   2531 N N   . ALA A 1 339 ? 33.166  -41.387 -30.546 1.00 34.94 ? 337  ALA B N   1 
ATOM   2532 C CA  . ALA A 1 339 ? 32.256  -41.843 -29.454 1.00 32.08 ? 337  ALA B CA  1 
ATOM   2533 C C   . ALA A 1 339 ? 31.046  -40.902 -29.362 1.00 30.74 ? 337  ALA B C   1 
ATOM   2534 O O   . ALA A 1 339 ? 31.074  -39.815 -29.980 1.00 28.12 ? 337  ALA B O   1 
ATOM   2535 C CB  . ALA A 1 339 ? 33.020  -41.875 -28.161 1.00 30.18 ? 337  ALA B CB  1 
ATOM   2536 N N   . ASP A 1 340 ? 30.031  -41.282 -28.582 1.00 30.38 ? 338  ASP B N   1 
ATOM   2537 C CA  . ASP A 1 340 ? 28.802  -40.459 -28.396 1.00 29.81 ? 338  ASP B CA  1 
ATOM   2538 C C   . ASP A 1 340 ? 29.073  -39.476 -27.259 1.00 27.30 ? 338  ASP B C   1 
ATOM   2539 O O   . ASP A 1 340 ? 29.813  -39.810 -26.335 1.00 27.50 ? 338  ASP B O   1 
ATOM   2540 C CB  . ASP A 1 340 ? 27.584  -41.352 -28.117 1.00 27.08 ? 338  ASP B CB  1 
ATOM   2541 C CG  . ASP A 1 340 ? 27.103  -42.166 -29.309 1.00 31.68 ? 338  ASP B CG  1 
ATOM   2542 O OD1 . ASP A 1 340 ? 27.528  -41.840 -30.439 1.00 32.51 ? 338  ASP B OD1 1 
ATOM   2543 O OD2 . ASP A 1 340 ? 26.309  -43.125 -29.109 1.00 28.17 ? 338  ASP B OD2 1 
ATOM   2544 N N   . PRO A 1 341 ? 28.444  -38.279 -27.218 1.00 24.29 ? 339  PRO B N   1 
ATOM   2545 C CA  . PRO A 1 341 ? 28.499  -37.460 -26.007 1.00 23.17 ? 339  PRO B CA  1 
ATOM   2546 C C   . PRO A 1 341 ? 27.848  -38.274 -24.882 1.00 19.37 ? 339  PRO B C   1 
ATOM   2547 O O   . PRO A 1 341 ? 26.880  -38.963 -25.107 1.00 21.28 ? 339  PRO B O   1 
ATOM   2548 C CB  . PRO A 1 341 ? 27.688  -36.200 -26.306 1.00 25.12 ? 339  PRO B CB  1 
ATOM   2549 C CG  . PRO A 1 341 ? 26.821  -36.588 -27.495 1.00 25.90 ? 339  PRO B CG  1 
ATOM   2550 C CD  . PRO A 1 341 ? 27.518  -37.725 -28.213 1.00 26.31 ? 339  PRO B CD  1 
ATOM   2551 N N   . ILE A 1 342 ? 28.375  -38.151 -23.672 1.00 19.01 ? 340  ILE B N   1 
ATOM   2552 C CA  . ILE A 1 342 ? 27.982  -39.073 -22.568 1.00 18.39 ? 340  ILE B CA  1 
ATOM   2553 C C   . ILE A 1 342 ? 26.546  -38.795 -22.106 1.00 17.72 ? 340  ILE B C   1 
ATOM   2554 O O   . ILE A 1 342 ? 25.965  -39.666 -21.435 1.00 17.19 ? 340  ILE B O   1 
ATOM   2555 C CB  . ILE A 1 342 ? 29.007  -39.036 -21.421 1.00 18.85 ? 340  ILE B CB  1 
ATOM   2556 C CG1 . ILE A 1 342 ? 29.108  -37.665 -20.743 1.00 19.19 ? 340  ILE B CG1 1 
ATOM   2557 C CG2 . ILE A 1 342 ? 30.362  -39.524 -21.925 1.00 18.61 ? 340  ILE B CG2 1 
ATOM   2558 C CD1 . ILE A 1 342 ? 29.871  -37.701 -19.418 1.00 20.38 ? 340  ILE B CD1 1 
ATOM   2559 N N   . ILE A 1 343 ? 25.934  -37.678 -22.507 1.00 16.99 ? 341  ILE B N   1 
ATOM   2560 C CA  . ILE A 1 343 ? 24.486  -37.488 -22.222 1.00 17.18 ? 341  ILE B CA  1 
ATOM   2561 C C   . ILE A 1 343 ? 23.624  -38.606 -22.858 1.00 17.19 ? 341  ILE B C   1 
ATOM   2562 O O   . ILE A 1 343 ? 22.486  -38.808 -22.402 1.00 17.72 ? 341  ILE B O   1 
ATOM   2563 C CB  . ILE A 1 343 ? 24.057  -36.087 -22.673 1.00 18.17 ? 341  ILE B CB  1 
ATOM   2564 C CG1 . ILE A 1 343 ? 22.682  -35.701 -22.125 1.00 20.53 ? 341  ILE B CG1 1 
ATOM   2565 C CG2 . ILE A 1 343 ? 24.127  -35.952 -24.189 1.00 20.33 ? 341  ILE B CG2 1 
ATOM   2566 C CD1 . ILE A 1 343 ? 22.445  -34.215 -22.175 1.00 21.09 ? 341  ILE B CD1 1 
ATOM   2567 N N   . VAL A 1 344 ? 24.140  -39.372 -23.813 1.00 18.28 ? 342  VAL B N   1 
ATOM   2568 C CA  . VAL A 1 344 ? 23.337  -40.495 -24.391 1.00 19.00 ? 342  VAL B CA  1 
ATOM   2569 C C   . VAL A 1 344 ? 23.162  -41.633 -23.384 1.00 20.48 ? 342  VAL B C   1 
ATOM   2570 O O   . VAL A 1 344 ? 22.306  -42.488 -23.614 1.00 20.30 ? 342  VAL B O   1 
ATOM   2571 C CB  . VAL A 1 344 ? 23.952  -41.040 -25.694 1.00 19.74 ? 342  VAL B CB  1 
ATOM   2572 C CG1 . VAL A 1 344 ? 24.125  -39.938 -26.727 1.00 20.06 ? 342  VAL B CG1 1 
ATOM   2573 C CG2 . VAL A 1 344 ? 25.272  -41.745 -25.435 1.00 19.98 ? 342  VAL B CG2 1 
ATOM   2574 N N   . HIS A 1 345 ? 23.965  -41.633 -22.326 1.00 19.78 ? 343  HIS B N   1 
ATOM   2575 C CA  . HIS A 1 345 ? 23.892  -42.724 -21.325 1.00 18.97 ? 343  HIS B CA  1 
ATOM   2576 C C   . HIS A 1 345 ? 22.789  -42.443 -20.303 1.00 18.74 ? 343  HIS B C   1 
ATOM   2577 O O   . HIS A 1 345 ? 22.765  -41.389 -19.711 1.00 16.78 ? 343  HIS B O   1 
ATOM   2578 C CB  . HIS A 1 345 ? 25.252  -42.954 -20.665 1.00 20.08 ? 343  HIS B CB  1 
ATOM   2579 C CG  . HIS A 1 345 ? 26.332  -43.230 -21.653 1.00 21.81 ? 343  HIS B CG  1 
ATOM   2580 N ND1 . HIS A 1 345 ? 26.267  -44.286 -22.534 1.00 25.97 ? 343  HIS B ND1 1 
ATOM   2581 C CD2 . HIS A 1 345 ? 27.485  -42.584 -21.919 1.00 22.63 ? 343  HIS B CD2 1 
ATOM   2582 C CE1 . HIS A 1 345 ? 27.340  -44.285 -23.294 1.00 26.11 ? 343  HIS B CE1 1 
ATOM   2583 N NE2 . HIS A 1 345 ? 28.100  -43.253 -22.939 1.00 24.25 ? 343  HIS B NE2 1 
ATOM   2584 N N   . PRO A 1 346 ? 21.871  -43.397 -20.114 1.00 17.35 ? 344  PRO B N   1 
ATOM   2585 C CA  . PRO A 1 346 ? 20.817  -43.235 -19.131 1.00 16.78 ? 344  PRO B CA  1 
ATOM   2586 C C   . PRO A 1 346 ? 21.336  -42.856 -17.735 1.00 15.65 ? 344  PRO B C   1 
ATOM   2587 O O   . PRO A 1 346 ? 20.718  -42.072 -17.100 1.00 15.55 ? 344  PRO B O   1 
ATOM   2588 C CB  . PRO A 1 346 ? 20.194  -44.635 -19.090 1.00 17.72 ? 344  PRO B CB  1 
ATOM   2589 C CG  . PRO A 1 346 ? 20.448  -45.214 -20.462 1.00 17.24 ? 344  PRO B CG  1 
ATOM   2590 C CD  . PRO A 1 346 ? 21.790  -44.647 -20.869 1.00 17.29 ? 344  PRO B CD  1 
ATOM   2591 N N   . ASP A 1 347 ? 22.445  -43.460 -17.316 1.00 16.12 ? 345  ASP B N   1 
ATOM   2592 C CA  . ASP A 1 347 ? 22.916  -43.201 -15.938 1.00 15.28 ? 345  ASP B CA  1 
ATOM   2593 C C   . ASP A 1 347 ? 23.379  -41.730 -15.842 1.00 15.03 ? 345  ASP B C   1 
ATOM   2594 O O   . ASP A 1 347 ? 23.211  -41.111 -14.779 1.00 15.63 ? 345  ASP B O   1 
ATOM   2595 C CB  . ASP A 1 347 ? 24.066  -44.098 -15.530 1.00 17.20 ? 345  ASP B CB  1 
ATOM   2596 C CG  . ASP A 1 347 ? 24.359  -43.975 -14.040 1.00 18.65 ? 345  ASP B CG  1 
ATOM   2597 O OD1 . ASP A 1 347 ? 23.416  -44.157 -13.222 1.00 18.90 ? 345  ASP B OD1 1 
ATOM   2598 O OD2 . ASP A 1 347 ? 25.521  -43.656 -13.718 1.00 18.46 ? 345  ASP B OD2 1 
ATOM   2599 N N   . VAL A 1 348 ? 23.994  -41.194 -16.888 1.00 14.94 ? 346  VAL B N   1 
ATOM   2600 C CA  . VAL A 1 348 ? 24.415  -39.765 -16.914 1.00 16.14 ? 346  VAL B CA  1 
ATOM   2601 C C   . VAL A 1 348 ? 23.146  -38.893 -16.862 1.00 15.43 ? 346  VAL B C   1 
ATOM   2602 O O   . VAL A 1 348 ? 23.092  -37.921 -16.103 1.00 14.89 ? 346  VAL B O   1 
ATOM   2603 C CB  . VAL A 1 348 ? 25.279  -39.463 -18.147 1.00 15.31 ? 346  VAL B CB  1 
ATOM   2604 C CG1 . VAL A 1 348 ? 25.484  -37.975 -18.285 1.00 16.20 ? 346  VAL B CG1 1 
ATOM   2605 C CG2 . VAL A 1 348 ? 26.605  -40.210 -18.054 1.00 16.55 ? 346  VAL B CG2 1 
ATOM   2606 N N   . ARG A 1 349 ? 22.146  -39.251 -17.636 1.00 15.17 ? 347  ARG B N   1 
ATOM   2607 C CA  . ARG A 1 349 ? 20.846  -38.521 -17.607 1.00 14.85 ? 347  ARG B CA  1 
ATOM   2608 C C   . ARG A 1 349 ? 20.239  -38.587 -16.195 1.00 14.09 ? 347  ARG B C   1 
ATOM   2609 O O   . ARG A 1 349 ? 19.698  -37.541 -15.710 1.00 14.48 ? 347  ARG B O   1 
ATOM   2610 C CB  . ARG A 1 349 ? 19.916  -39.082 -18.691 1.00 14.80 ? 347  ARG B CB  1 
ATOM   2611 C CG  . ARG A 1 349 ? 20.259  -38.570 -20.077 1.00 15.92 ? 347  ARG B CG  1 
ATOM   2612 C CD  . ARG A 1 349 ? 19.617  -39.397 -21.189 1.00 16.58 ? 347  ARG B CD  1 
ATOM   2613 N NE  . ARG A 1 349 ? 19.611  -38.621 -22.428 1.00 16.87 ? 347  ARG B NE  1 
ATOM   2614 C CZ  . ARG A 1 349 ? 18.683  -37.731 -22.782 1.00 16.64 ? 347  ARG B CZ  1 
ATOM   2615 N NH1 . ARG A 1 349 ? 18.855  -37.018 -23.898 1.00 17.43 ? 347  ARG B NH1 1 
ATOM   2616 N NH2 . ARG A 1 349 ? 17.582  -37.594 -22.077 1.00 15.71 ? 347  ARG B NH2 1 
ATOM   2617 N N   . ARG A 1 350 ? 20.319  -39.745 -15.527 1.00 14.71 ? 348  ARG B N   1 
ATOM   2618 C CA  . ARG A 1 350 ? 19.795  -39.847 -14.138 1.00 14.33 ? 348  ARG B CA  1 
ATOM   2619 C C   . ARG A 1 350 ? 20.506  -38.829 -13.258 1.00 14.14 ? 348  ARG B C   1 
ATOM   2620 O O   . ARG A 1 350 ? 19.835  -38.111 -12.483 1.00 14.09 ? 348  ARG B O   1 
ATOM   2621 C CB  . ARG A 1 350 ? 19.997  -41.262 -13.597 1.00 14.81 ? 348  ARG B CB  1 
ATOM   2622 C CG  . ARG A 1 350 ? 19.512  -41.453 -12.173 1.00 15.67 ? 348  ARG B CG  1 
ATOM   2623 C CD  . ARG A 1 350 ? 19.970  -42.793 -11.653 1.00 17.05 ? 348  ARG B CD  1 
ATOM   2624 N NE  . ARG A 1 350 ? 21.424  -42.971 -11.600 1.00 16.62 ? 348  ARG B NE  1 
ATOM   2625 C CZ  . ARG A 1 350 ? 22.246  -42.582 -10.611 1.00 17.21 ? 348  ARG B CZ  1 
ATOM   2626 N NH1 . ARG A 1 350 ? 21.815  -41.960 -9.530  1.00 19.37 ? 348  ARG B NH1 1 
ATOM   2627 N NH2 . ARG A 1 350 ? 23.543  -42.848 -10.674 1.00 17.06 ? 348  ARG B NH2 1 
ATOM   2628 N N   . MET A 1 351 ? 21.822  -38.730 -13.336 1.00 14.03 ? 349  MET B N   1 
ATOM   2629 C CA  . MET A 1 351 ? 22.558  -37.790 -12.448 1.00 13.30 ? 349  MET B CA  1 
ATOM   2630 C C   . MET A 1 351 ? 22.241  -36.315 -12.816 1.00 13.40 ? 349  MET B C   1 
ATOM   2631 O O   . MET A 1 351 ? 22.016  -35.459 -11.923 1.00 14.53 ? 349  MET B O   1 
ATOM   2632 C CB  . MET A 1 351 ? 24.049  -38.099 -12.561 1.00 13.96 ? 349  MET B CB  1 
ATOM   2633 C CG  . MET A 1 351 ? 24.373  -39.446 -11.915 1.00 14.65 ? 349  MET B CG  1 
ATOM   2634 S SD  . MET A 1 351 ? 26.155  -39.750 -11.817 1.00 17.48 ? 349  MET B SD  1 
ATOM   2635 C CE  . MET A 1 351 ? 26.511  -40.172 -13.513 1.00 16.64 ? 349  MET B CE  1 
ATOM   2636 N N   . LEU A 1 352 ? 22.193  -35.991 -14.104 1.00 13.48 ? 350  LEU B N   1 
ATOM   2637 C CA  . LEU A 1 352 ? 21.759  -34.631 -14.551 1.00 13.93 ? 350  LEU B CA  1 
ATOM   2638 C C   . LEU A 1 352 ? 20.365  -34.278 -14.042 1.00 12.67 ? 350  LEU B C   1 
ATOM   2639 O O   . LEU A 1 352 ? 20.177  -33.158 -13.461 1.00 13.72 ? 350  LEU B O   1 
ATOM   2640 C CB  . LEU A 1 352 ? 21.753  -34.609 -16.083 1.00 14.95 ? 350  LEU B CB  1 
ATOM   2641 C CG  . LEU A 1 352 ? 23.120  -34.584 -16.737 1.00 14.53 ? 350  LEU B CG  1 
ATOM   2642 C CD1 . LEU A 1 352 ? 22.923  -34.811 -18.254 1.00 15.80 ? 350  LEU B CD1 1 
ATOM   2643 C CD2 . LEU A 1 352 ? 23.918  -33.326 -16.451 1.00 16.24 ? 350  LEU B CD2 1 
ATOM   2644 N N   . LEU A 1 353 ? 19.402  -35.181 -14.209 1.00 13.80 ? 351  LEU B N   1 
ATOM   2645 C CA  . LEU A 1 353 ? 17.978  -34.913 -13.840 1.00 14.88 ? 351  LEU B CA  1 
ATOM   2646 C C   . LEU A 1 353 ? 17.855  -34.809 -12.323 1.00 14.46 ? 351  LEU B C   1 
ATOM   2647 O O   . LEU A 1 353 ? 16.984  -34.093 -11.852 1.00 13.97 ? 351  LEU B O   1 
ATOM   2648 C CB  . LEU A 1 353 ? 17.061  -35.982 -14.430 1.00 14.86 ? 351  LEU B CB  1 
ATOM   2649 C CG  . LEU A 1 353 ? 16.902  -35.886 -15.950 1.00 15.87 ? 351  LEU B CG  1 
ATOM   2650 C CD1 . LEU A 1 353 ? 16.201  -37.118 -16.496 1.00 17.39 ? 351  LEU B CD1 1 
ATOM   2651 C CD2 . LEU A 1 353 ? 16.141  -34.623 -16.339 1.00 17.86 ? 351  LEU B CD2 1 
ATOM   2652 N N   . THR A 1 354 ? 18.670  -35.549 -11.566 1.00 14.07 ? 352  THR B N   1 
ATOM   2653 C CA  . THR A 1 354 ? 18.658  -35.440 -10.078 1.00 12.85 ? 352  THR B CA  1 
ATOM   2654 C C   . THR A 1 354 ? 19.049  -34.007 -9.690  1.00 13.37 ? 352  THR B C   1 
ATOM   2655 O O   . THR A 1 354 ? 18.319  -33.374 -8.897  1.00 13.75 ? 352  THR B O   1 
ATOM   2656 C CB  . THR A 1 354 ? 19.563  -36.505 -9.438  1.00 12.93 ? 352  THR B CB  1 
ATOM   2657 O OG1 . THR A 1 354 ? 19.137  -37.827 -9.808  1.00 14.07 ? 352  THR B OG1 1 
ATOM   2658 C CG2 . THR A 1 354 ? 19.492  -36.370 -7.921  1.00 14.00 ? 352  THR B CG2 1 
ATOM   2659 N N   . MET A 1 355 ? 20.145  -33.494 -10.237 1.00 12.66 ? 353  MET B N   1 
ATOM   2660 C CA  . MET A 1 355 ? 20.630  -32.138 -9.905  1.00 13.23 ? 353  MET B CA  1 
ATOM   2661 C C   . MET A 1 355 ? 19.578  -31.113 -10.335 1.00 13.56 ? 353  MET B C   1 
ATOM   2662 O O   . MET A 1 355 ? 19.264  -30.199 -9.582  1.00 13.18 ? 353  MET B O   1 
ATOM   2663 C CB  . MET A 1 355 ? 21.940  -31.833 -10.592 1.00 13.80 ? 353  MET B CB  1 
ATOM   2664 C CG  . MET A 1 355 ? 23.069  -32.799 -10.145 1.00 14.44 ? 353  MET B CG  1 
ATOM   2665 S SD  . MET A 1 355 ? 24.689  -32.328 -10.780 1.00 14.59 ? 353  MET B SD  1 
ATOM   2666 C CE  . MET A 1 355 ? 24.445  -32.711 -12.514 1.00 13.85 ? 353  MET B CE  1 
ATOM   2667 N N   . LYS A 1 356 ? 19.011  -31.316 -11.515 1.00 13.82 ? 354  LYS B N   1 
ATOM   2668 C CA  . LYS A 1 356 ? 17.983  -30.383 -12.045 1.00 15.00 ? 354  LYS B CA  1 
ATOM   2669 C C   . LYS A 1 356 ? 16.722  -30.397 -11.165 1.00 13.46 ? 354  LYS B C   1 
ATOM   2670 O O   . LYS A 1 356 ? 16.215  -29.337 -10.838 1.00 14.42 ? 354  LYS B O   1 
ATOM   2671 C CB  . LYS A 1 356 ? 17.667  -30.796 -13.487 1.00 15.27 ? 354  LYS B CB  1 
ATOM   2672 C CG  . LYS A 1 356 ? 16.825  -29.820 -14.292 1.00 15.34 ? 354  LYS B CG  1 
ATOM   2673 C CD  . LYS A 1 356 ? 16.710  -30.239 -15.738 1.00 17.69 ? 354  LYS B CD  1 
ATOM   2674 C CE  . LYS A 1 356 ? 15.753  -29.376 -16.528 1.00 18.13 ? 354  LYS B CE  1 
ATOM   2675 N NZ  . LYS A 1 356 ? 16.254  -27.990 -16.656 1.00 19.84 ? 354  LYS B NZ  1 
ATOM   2676 N N   . ALA A 1 357 ? 16.239  -31.590 -10.827 1.00 14.28 ? 355  ALA B N   1 
ATOM   2677 C CA  . ALA A 1 357 ? 15.040  -31.683 -9.966  1.00 14.38 ? 355  ALA B CA  1 
ATOM   2678 C C   . ALA A 1 357 ? 15.252  -30.991 -8.609  1.00 13.72 ? 355  ALA B C   1 
ATOM   2679 O O   . ALA A 1 357 ? 14.332  -30.313 -8.110  1.00 13.21 ? 355  ALA B O   1 
ATOM   2680 C CB  . ALA A 1 357 ? 14.688  -33.109 -9.731  1.00 15.26 ? 355  ALA B CB  1 
ATOM   2681 N N   . PHE A 1 358 ? 16.430  -31.126 -8.019  1.00 12.88 ? 356  PHE B N   1 
ATOM   2682 C CA  . PHE A 1 358 ? 16.687  -30.486 -6.710  1.00 12.65 ? 356  PHE B CA  1 
ATOM   2683 C C   . PHE A 1 358 ? 16.888  -28.984 -6.883  1.00 13.38 ? 356  PHE B C   1 
ATOM   2684 O O   . PHE A 1 358 ? 16.337  -28.250 -6.077  1.00 13.96 ? 356  PHE B O   1 
ATOM   2685 C CB  . PHE A 1 358 ? 17.880  -31.150 -6.004  1.00 13.35 ? 356  PHE B CB  1 
ATOM   2686 C CG  . PHE A 1 358 ? 17.610  -32.521 -5.458  1.00 13.01 ? 356  PHE B CG  1 
ATOM   2687 C CD1 . PHE A 1 358 ? 16.456  -32.769 -4.721  1.00 13.35 ? 356  PHE B CD1 1 
ATOM   2688 C CD2 . PHE A 1 358 ? 18.547  -33.537 -5.565  1.00 11.71 ? 356  PHE B CD2 1 
ATOM   2689 C CE1 . PHE A 1 358 ? 16.186  -34.019 -4.205  1.00 13.08 ? 356  PHE B CE1 1 
ATOM   2690 C CE2 . PHE A 1 358 ? 18.287  -34.771 -5.006  1.00 12.36 ? 356  PHE B CE2 1 
ATOM   2691 C CZ  . PHE A 1 358 ? 17.139  -35.010 -4.324  1.00 13.26 ? 356  PHE B CZ  1 
ATOM   2692 N N   . ALA A 1 359 ? 17.649  -28.548 -7.874  1.00 13.07 ? 357  ALA B N   1 
ATOM   2693 C CA  . ALA A 1 359 ? 17.878  -27.098 -8.010  1.00 14.50 ? 357  ALA B CA  1 
ATOM   2694 C C   . ALA A 1 359 ? 16.546  -26.386 -8.295  1.00 13.93 ? 357  ALA B C   1 
ATOM   2695 O O   . ALA A 1 359 ? 16.215  -25.441 -7.600  1.00 13.94 ? 357  ALA B O   1 
ATOM   2696 C CB  . ALA A 1 359 ? 18.878  -26.846 -9.109  1.00 14.87 ? 357  ALA B CB  1 
ATOM   2697 N N   . GLU A 1 360 ? 15.839  -26.844 -9.315  1.00 14.43 ? 358  GLU B N   1 
ATOM   2698 C CA  . GLU A 1 360 ? 14.583  -26.167 -9.719  1.00 15.39 ? 358  GLU B CA  1 
ATOM   2699 C C   . GLU A 1 360 ? 13.511  -26.323 -8.625  1.00 15.16 ? 358  GLU B C   1 
ATOM   2700 O O   . GLU A 1 360 ? 12.801  -25.368 -8.368  1.00 14.74 ? 358  GLU B O   1 
ATOM   2701 C CB  . GLU A 1 360 ? 14.171  -26.691 -11.097 1.00 15.73 ? 358  GLU B CB  1 
ATOM   2702 C CG  . GLU A 1 360 ? 15.012  -26.111 -12.215 1.00 16.52 ? 358  GLU B CG  1 
ATOM   2703 C CD  . GLU A 1 360 ? 14.699  -26.624 -13.609 1.00 17.34 ? 358  GLU B CD  1 
ATOM   2704 O OE1 . GLU A 1 360 ? 15.575  -26.521 -14.469 1.00 20.52 ? 358  GLU B OE1 1 
ATOM   2705 O OE2 . GLU A 1 360 ? 13.588  -27.121 -13.820 1.00 19.01 ? 358  GLU B OE2 1 
ATOM   2706 N N   . GLY A 1 361 ? 13.414  -27.504 -8.010  1.00 13.25 ? 359  GLY B N   1 
ATOM   2707 C CA  . GLY A 1 361 ? 12.429  -27.687 -6.932  1.00 14.09 ? 359  GLY B CA  1 
ATOM   2708 C C   . GLY A 1 361 ? 12.723  -26.827 -5.707  1.00 14.47 ? 359  GLY B C   1 
ATOM   2709 O O   . GLY A 1 361 ? 11.824  -26.187 -5.184  1.00 14.53 ? 359  GLY B O   1 
ATOM   2710 N N   . ASN A 1 362 ? 13.983  -26.812 -5.298  1.00 14.49 ? 360  ASN B N   1 
ATOM   2711 C CA  . ASN A 1 362 ? 14.370  -26.003 -4.120  1.00 13.77 ? 360  ASN B CA  1 
ATOM   2712 C C   . ASN A 1 362 ? 14.190  -24.505 -4.430  1.00 13.34 ? 360  ASN B C   1 
ATOM   2713 O O   . ASN A 1 362 ? 13.827  -23.773 -3.538  1.00 14.53 ? 360  ASN B O   1 
ATOM   2714 C CB  . ASN A 1 362 ? 15.778  -26.380 -3.645  1.00 13.57 ? 360  ASN B CB  1 
ATOM   2715 C CG  . ASN A 1 362 ? 15.800  -27.723 -2.947  1.00 14.84 ? 360  ASN B CG  1 
ATOM   2716 O OD1 . ASN A 1 362 ? 14.783  -28.166 -2.431  1.00 15.40 ? 360  ASN B OD1 1 
ATOM   2717 N ND2 . ASN A 1 362 ? 16.948  -28.377 -2.938  1.00 15.46 ? 360  ASN B ND2 1 
ATOM   2718 N N   . ARG A 1 363 ? 14.448  -24.102 -5.671  1.00 14.41 ? 361  ARG B N   1 
ATOM   2719 C CA  . ARG A 1 363 ? 14.248  -22.680 -6.058  1.00 14.83 ? 361  ARG B CA  1 
ATOM   2720 C C   . ARG A 1 363 ? 12.782  -22.310 -5.813  1.00 14.42 ? 361  ARG B C   1 
ATOM   2721 O O   . ARG A 1 363 ? 12.529  -21.217 -5.283  1.00 14.44 ? 361  ARG B O   1 
ATOM   2722 C CB  . ARG A 1 363 ? 14.655  -22.463 -7.517  1.00 13.25 ? 361  ARG B CB  1 
ATOM   2723 C CG  . ARG A 1 363 ? 14.560  -21.016 -7.983  1.00 14.32 ? 361  ARG B CG  1 
ATOM   2724 C CD  . ARG A 1 363 ? 15.230  -20.756 -9.322  1.00 14.73 ? 361  ARG B CD  1 
ATOM   2725 N NE  . ARG A 1 363 ? 16.659  -20.989 -9.197  1.00 16.35 ? 361  ARG B NE  1 
ATOM   2726 C CZ  . ARG A 1 363 ? 17.334  -21.954 -9.808  1.00 15.31 ? 361  ARG B CZ  1 
ATOM   2727 N NH1 . ARG A 1 363 ? 18.628  -22.085 -9.587  1.00 16.25 ? 361  ARG B NH1 1 
ATOM   2728 N NH2 . ARG A 1 363 ? 16.722  -22.781 -10.636 1.00 15.73 ? 361  ARG B NH2 1 
ATOM   2729 N N   . ALA A 1 364 ? 11.873  -23.204 -6.201  1.00 14.16 ? 362  ALA B N   1 
ATOM   2730 C CA  . ALA A 1 364 ? 10.431  -22.953 -5.981  1.00 13.74 ? 362  ALA B CA  1 
ATOM   2731 C C   . ALA A 1 364 ? 10.141  -22.810 -4.475  1.00 15.23 ? 362  ALA B C   1 
ATOM   2732 O O   . ALA A 1 364 ? 9.507   -21.845 -4.070  1.00 15.08 ? 362  ALA B O   1 
ATOM   2733 C CB  . ALA A 1 364 ? 9.621   -24.044 -6.635  1.00 16.23 ? 362  ALA B CB  1 
ATOM   2734 N N   . MET A 1 365 ? 10.644  -23.747 -3.684  1.00 15.13 ? 363  MET B N   1 
ATOM   2735 C CA  . MET A 1 365 ? 10.422  -23.680 -2.218  1.00 16.28 ? 363  MET B CA  1 
ATOM   2736 C C   . MET A 1 365 ? 11.030  -22.389 -1.637  1.00 15.25 ? 363  MET B C   1 
ATOM   2737 O O   . MET A 1 365 ? 10.408  -21.790 -0.774  1.00 17.26 ? 363  MET B O   1 
ATOM   2738 C CB  . MET A 1 365 ? 11.037  -24.905 -1.536  1.00 16.50 ? 363  MET B CB  1 
ATOM   2739 C CG  . MET A 1 365 ? 10.876  -24.892 -0.034  1.00 16.99 ? 363  MET B CG  1 
ATOM   2740 S SD  . MET A 1 365 ? 10.793  -26.564 0.660   1.00 20.59 ? 363  MET B SD  1 
ATOM   2741 C CE  . MET A 1 365 ? 12.457  -27.140 0.333   1.00 22.92 ? 363  MET B CE  1 
ATOM   2742 N N   . LEU A 1 366 ? 12.226  -22.020 -2.075  1.00 15.20 ? 364  LEU B N   1 
ATOM   2743 C CA  . LEU A 1 366 ? 12.899  -20.805 -1.552  1.00 16.70 ? 364  LEU B CA  1 
ATOM   2744 C C   . LEU A 1 366 ? 12.038  -19.547 -1.779  1.00 16.39 ? 364  LEU B C   1 
ATOM   2745 O O   . LEU A 1 366 ? 11.878  -18.782 -0.836  1.00 18.49 ? 364  LEU B O   1 
ATOM   2746 C CB  . LEU A 1 366 ? 14.249  -20.671 -2.253  1.00 18.28 ? 364  LEU B CB  1 
ATOM   2747 C CG  . LEU A 1 366 ? 15.141  -19.544 -1.741  1.00 22.93 ? 364  LEU B CG  1 
ATOM   2748 C CD1 . LEU A 1 366 ? 15.536  -19.789 -0.293  1.00 26.35 ? 364  LEU B CD1 1 
ATOM   2749 C CD2 . LEU A 1 366 ? 16.374  -19.398 -2.615  1.00 26.39 ? 364  LEU B CD2 1 
ATOM   2750 N N   . TYR A 1 367 ? 11.524  -19.365 -2.995  1.00 15.32 ? 365  TYR B N   1 
ATOM   2751 C CA  . TYR A 1 367 ? 10.762  -18.120 -3.286  1.00 16.31 ? 365  TYR B CA  1 
ATOM   2752 C C   . TYR A 1 367 ? 9.368   -18.208 -2.660  1.00 17.51 ? 365  TYR B C   1 
ATOM   2753 O O   . TYR A 1 367 ? 8.781   -17.161 -2.386  1.00 17.25 ? 365  TYR B O   1 
ATOM   2754 C CB  . TYR A 1 367 ? 10.837  -17.781 -4.773  1.00 16.19 ? 365  TYR B CB  1 
ATOM   2755 C CG  . TYR A 1 367 ? 12.217  -17.321 -5.162  1.00 15.58 ? 365  TYR B CG  1 
ATOM   2756 C CD1 . TYR A 1 367 ? 12.751  -16.156 -4.636  1.00 17.12 ? 365  TYR B CD1 1 
ATOM   2757 C CD2 . TYR A 1 367 ? 13.013  -18.076 -6.002  1.00 15.55 ? 365  TYR B CD2 1 
ATOM   2758 C CE1 . TYR A 1 367 ? 14.030  -15.739 -4.956  1.00 16.29 ? 365  TYR B CE1 1 
ATOM   2759 C CE2 . TYR A 1 367 ? 14.294  -17.674 -6.333  1.00 16.64 ? 365  TYR B CE2 1 
ATOM   2760 C CZ  . TYR A 1 367 ? 14.805  -16.502 -5.808  1.00 16.40 ? 365  TYR B CZ  1 
ATOM   2761 O OH  . TYR A 1 367 ? 16.068  -16.105 -6.118  1.00 18.56 ? 365  TYR B OH  1 
ATOM   2762 N N   . PHE A 1 368 ? 8.858   -19.416 -2.452  1.00 15.88 ? 366  PHE B N   1 
ATOM   2763 C CA  . PHE A 1 368 ? 7.622   -19.570 -1.659  1.00 16.65 ? 366  PHE B CA  1 
ATOM   2764 C C   . PHE A 1 368 ? 7.883   -19.071 -0.236  1.00 18.21 ? 366  PHE B C   1 
ATOM   2765 O O   . PHE A 1 368 ? 7.068   -18.292 0.320   1.00 16.76 ? 366  PHE B O   1 
ATOM   2766 C CB  . PHE A 1 368 ? 7.110   -21.005 -1.736  1.00 17.96 ? 366  PHE B CB  1 
ATOM   2767 C CG  . PHE A 1 368 ? 5.847   -21.222 -0.953  1.00 19.34 ? 366  PHE B CG  1 
ATOM   2768 C CD1 . PHE A 1 368 ? 4.639   -20.762 -1.448  1.00 22.45 ? 366  PHE B CD1 1 
ATOM   2769 C CD2 . PHE A 1 368 ? 5.870   -21.773 0.316   1.00 18.92 ? 366  PHE B CD2 1 
ATOM   2770 C CE1 . PHE A 1 368 ? 3.467   -20.952 -0.737  1.00 25.34 ? 366  PHE B CE1 1 
ATOM   2771 C CE2 . PHE A 1 368 ? 4.694   -21.982 1.016   1.00 20.14 ? 366  PHE B CE2 1 
ATOM   2772 C CZ  . PHE A 1 368 ? 3.495   -21.539 0.503   1.00 23.60 ? 366  PHE B CZ  1 
ATOM   2773 N N   . ALA A 1 369 ? 9.000   -19.502 0.366   1.00 15.83 ? 367  ALA B N   1 
ATOM   2774 C CA  . ALA A 1 369 ? 9.381   -19.067 1.724   1.00 16.62 ? 367  ALA B CA  1 
ATOM   2775 C C   . ALA A 1 369 ? 9.612   -17.546 1.717   1.00 17.38 ? 367  ALA B C   1 
ATOM   2776 O O   . ALA A 1 369 ? 9.160   -16.892 2.668   1.00 16.69 ? 367  ALA B O   1 
ATOM   2777 C CB  . ALA A 1 369 ? 10.594  -19.822 2.191   1.00 17.73 ? 367  ALA B CB  1 
ATOM   2778 N N   . ALA A 1 370 ? 10.208  -16.986 0.667   1.00 15.65 ? 368  ALA B N   1 
ATOM   2779 C CA  . ALA A 1 370 ? 10.578  -15.555 0.571   1.00 17.02 ? 368  ALA B CA  1 
ATOM   2780 C C   . ALA A 1 370 ? 9.298   -14.694 0.599   1.00 17.75 ? 368  ALA B C   1 
ATOM   2781 O O   . ALA A 1 370 ? 9.353   -13.598 1.185   1.00 18.93 ? 368  ALA B O   1 
ATOM   2782 C CB  . ALA A 1 370 ? 11.465  -15.279 -0.643  1.00 16.02 ? 368  ALA B CB  1 
ATOM   2783 N N   . LYS A 1 371 ? 8.192   -15.204 0.068   1.00 17.86 ? 369  LYS B N   1 
ATOM   2784 C CA  . LYS A 1 371 ? 6.891   -14.475 0.067   1.00 19.28 ? 369  LYS B CA  1 
ATOM   2785 C C   . LYS A 1 371 ? 6.431   -14.341 1.508   1.00 21.79 ? 369  LYS B C   1 
ATOM   2786 O O   . LYS A 1 371 ? 5.921   -13.278 1.847   1.00 19.47 ? 369  LYS B O   1 
ATOM   2787 C CB  . LYS A 1 371 ? 5.799   -15.151 -0.766  1.00 21.64 ? 369  LYS B CB  1 
ATOM   2788 C CG  . LYS A 1 371 ? 5.902   -14.946 -2.253  1.00 22.28 ? 369  LYS B CG  1 
ATOM   2789 C CD  . LYS A 1 371 ? 4.847   -15.723 -3.020  1.00 25.40 ? 369  LYS B CD  1 
ATOM   2790 C CE  . LYS A 1 371 ? 3.440   -15.181 -2.962  1.00 27.13 ? 369  LYS B CE  1 
ATOM   2791 N NZ  . LYS A 1 371 ? 2.575   -16.022 -3.832  1.00 23.99 ? 369  LYS B NZ  1 
ATOM   2792 N N   . GLN A 1 372 ? 6.610   -15.374 2.324   1.00 19.19 ? 370  GLN B N   1 
ATOM   2793 C CA  . GLN A 1 372 ? 6.238   -15.345 3.746   1.00 19.51 ? 370  GLN B CA  1 
ATOM   2794 C C   . GLN A 1 372 ? 7.049   -14.261 4.456   1.00 19.14 ? 370  GLN B C   1 
ATOM   2795 O O   . GLN A 1 372 ? 6.437   -13.511 5.263   1.00 20.68 ? 370  GLN B O   1 
ATOM   2796 C CB  . GLN A 1 372 ? 6.416   -16.716 4.409   1.00 19.43 ? 370  GLN B CB  1 
ATOM   2797 C CG  . GLN A 1 372 ? 5.858   -17.861 3.601   1.00 18.80 ? 370  GLN B CG  1 
ATOM   2798 C CD  . GLN A 1 372 ? 4.462   -17.650 3.091   1.00 20.38 ? 370  GLN B CD  1 
ATOM   2799 O OE1 . GLN A 1 372 ? 3.572   -17.248 3.825   1.00 21.06 ? 370  GLN B OE1 1 
ATOM   2800 N NE2 . GLN A 1 372 ? 4.282   -17.871 1.804   1.00 21.50 ? 370  GLN B NE2 1 
ATOM   2801 N N   . VAL A 1 373 ? 8.360   -14.171 4.206   1.00 19.05 ? 371  VAL B N   1 
ATOM   2802 C CA  . VAL A 1 373 ? 9.242   -13.133 4.781   1.00 18.90 ? 371  VAL B CA  1 
ATOM   2803 C C   . VAL A 1 373 ? 8.605   -11.760 4.469   1.00 19.96 ? 371  VAL B C   1 
ATOM   2804 O O   . VAL A 1 373 ? 8.374   -10.969 5.433   1.00 21.75 ? 371  VAL B O   1 
ATOM   2805 C CB  . VAL A 1 373 ? 10.696  -13.218 4.286   1.00 19.01 ? 371  VAL B CB  1 
ATOM   2806 C CG1 . VAL A 1 373 ? 11.507  -12.052 4.804   1.00 21.29 ? 371  VAL B CG1 1 
ATOM   2807 C CG2 . VAL A 1 373 ? 11.363  -14.534 4.679   1.00 19.53 ? 371  VAL B CG2 1 
ATOM   2808 N N   . ASP A 1 374 ? 8.300   -11.496 3.198   1.00 19.67 ? 372  ASP B N   1 
ATOM   2809 C CA  . ASP A 1 374 ? 7.694   -10.193 2.775   1.00 20.35 ? 372  ASP B CA  1 
ATOM   2810 C C   . ASP A 1 374 ? 6.390   -9.947  3.538   1.00 21.36 ? 372  ASP B C   1 
ATOM   2811 O O   . ASP A 1 374 ? 6.176   -8.783  4.017   1.00 21.77 ? 372  ASP B O   1 
ATOM   2812 C CB  . ASP A 1 374 ? 7.390   -10.141 1.282   1.00 19.47 ? 372  ASP B CB  1 
ATOM   2813 C CG  . ASP A 1 374 ? 8.569   -10.161 0.352   1.00 17.60 ? 372  ASP B CG  1 
ATOM   2814 O OD1 . ASP A 1 374 ? 9.693   -9.800  0.782   1.00 18.60 ? 372  ASP B OD1 1 
ATOM   2815 O OD2 . ASP A 1 374 ? 8.332   -10.531 -0.823  1.00 20.12 ? 372  ASP B OD2 1 
ATOM   2816 N N   . ILE A 1 375 ? 5.526   -10.948 3.661   1.00 21.04 ? 373  ILE B N   1 
ATOM   2817 C CA  . ILE A 1 375 ? 4.214   -10.786 4.358   1.00 22.96 ? 373  ILE B CA  1 
ATOM   2818 C C   . ILE A 1 375 ? 4.443   -10.453 5.834   1.00 23.53 ? 373  ILE B C   1 
ATOM   2819 O O   . ILE A 1 375 ? 3.810   -9.470  6.341   1.00 24.09 ? 373  ILE B O   1 
ATOM   2820 C CB  . ILE A 1 375 ? 3.306   -11.998 4.156   1.00 20.89 ? 373  ILE B CB  1 
ATOM   2821 C CG1 . ILE A 1 375 ? 2.954   -12.180 2.692   1.00 20.64 ? 373  ILE B CG1 1 
ATOM   2822 C CG2 . ILE A 1 375 ? 2.060   -11.885 5.019   1.00 22.51 ? 373  ILE B CG2 1 
ATOM   2823 C CD1 . ILE A 1 375 ? 2.462   -13.575 2.359   1.00 22.60 ? 373  ILE B CD1 1 
ATOM   2824 N N   . VAL A 1 376 ? 5.390   -11.123 6.492   1.00 24.41 ? 374  VAL B N   1 
ATOM   2825 C CA  . VAL A 1 376 ? 5.630   -10.878 7.940   1.00 26.03 ? 374  VAL B CA  1 
ATOM   2826 C C   . VAL A 1 376 ? 6.133   -9.441  8.112   1.00 27.58 ? 374  VAL B C   1 
ATOM   2827 O O   . VAL A 1 376 ? 5.673   -8.738  9.046   1.00 27.34 ? 374  VAL B O   1 
ATOM   2828 C CB  . VAL A 1 376 ? 6.564   -11.931 8.556   1.00 25.65 ? 374  VAL B CB  1 
ATOM   2829 C CG1 . VAL A 1 376 ? 7.020   -11.504 9.944   1.00 26.18 ? 374  VAL B CG1 1 
ATOM   2830 C CG2 . VAL A 1 376 ? 5.868   -13.281 8.608   1.00 25.58 ? 374  VAL B CG2 1 
ATOM   2831 N N   . GLN A 1 377 ? 7.020   -8.998  7.232   1.00 26.79 ? 375  GLN B N   1 
ATOM   2832 C CA  . GLN A 1 377 ? 7.663   -7.675  7.347   1.00 26.92 ? 375  GLN B CA  1 
ATOM   2833 C C   . GLN A 1 377 ? 6.678   -6.552  7.053   1.00 27.65 ? 375  GLN B C   1 
ATOM   2834 O O   . GLN A 1 377 ? 6.856   -5.478  7.668   1.00 31.88 ? 375  GLN B O   1 
ATOM   2835 C CB  . GLN A 1 377 ? 8.834   -7.562  6.383   1.00 28.81 ? 375  GLN B CB  1 
ATOM   2836 C CG  . GLN A 1 377 ? 9.957   -8.482  6.785   1.00 29.66 ? 375  GLN B CG  1 
ATOM   2837 C CD  . GLN A 1 377 ? 11.175  -8.281  5.933   1.00 31.53 ? 375  GLN B CD  1 
ATOM   2838 O OE1 . GLN A 1 377 ? 11.114  -7.706  4.837   1.00 34.49 ? 375  GLN B OE1 1 
ATOM   2839 N NE2 . GLN A 1 377 ? 12.296  -8.734  6.470   1.00 33.24 ? 375  GLN B NE2 1 
ATOM   2840 N N   . ARG A 1 378 ? 5.755   -6.736  6.113   1.00 26.98 ? 376  ARG B N   1 
ATOM   2841 C CA  . ARG A 1 378 ? 5.069   -5.573  5.475   1.00 28.64 ? 376  ARG B CA  1 
ATOM   2842 C C   . ARG A 1 378 ? 3.542   -5.598  5.627   1.00 31.67 ? 376  ARG B C   1 
ATOM   2843 O O   . ARG A 1 378 ? 2.941   -4.497  5.482   1.00 29.84 ? 376  ARG B O   1 
ATOM   2844 C CB  . ARG A 1 378 ? 5.373   -5.495  3.975   1.00 27.63 ? 376  ARG B CB  1 
ATOM   2845 C CG  . ARG A 1 378 ? 6.821   -5.168  3.656   1.00 26.97 ? 376  ARG B CG  1 
ATOM   2846 C CD  . ARG A 1 378 ? 7.155   -5.368  2.191   1.00 28.77 ? 376  ARG B CD  1 
ATOM   2847 N NE  . ARG A 1 378 ? 8.557   -5.022  1.996   1.00 30.95 ? 376  ARG B NE  1 
ATOM   2848 C CZ  . ARG A 1 378 ? 9.008   -3.829  1.587   1.00 30.69 ? 376  ARG B CZ  1 
ATOM   2849 N NH1 . ARG A 1 378 ? 8.159   -2.861  1.273   1.00 35.57 ? 376  ARG B NH1 1 
ATOM   2850 N NH2 . ARG A 1 378 ? 10.308  -3.607  1.502   1.00 27.83 ? 376  ARG B NH2 1 
ATOM   2851 N N   . SER A 1 379 ? 2.896   -6.739  5.854   1.00 26.73 ? 377  SER B N   1 
ATOM   2852 C CA  . SER A 1 379 ? 1.419   -6.828  5.812   1.00 31.50 ? 377  SER B CA  1 
ATOM   2853 C C   . SER A 1 379 ? 0.808   -6.050  6.987   1.00 33.74 ? 377  SER B C   1 
ATOM   2854 O O   . SER A 1 379 ? 1.405   -6.061  8.085   1.00 31.94 ? 377  SER B O   1 
ATOM   2855 C CB  . SER A 1 379 ? 0.949   -8.231  5.819   1.00 32.29 ? 377  SER B CB  1 
ATOM   2856 O OG  . SER A 1 379 ? -0.460  -8.275  5.810   1.00 33.60 ? 377  SER B OG  1 
ATOM   2857 N N   . GLN A 1 380 ? -0.361  -5.441  6.760   1.00 37.26 ? 378  GLN B N   1 
ATOM   2858 C CA  . GLN A 1 380 ? -1.149  -4.777  7.832   1.00 43.00 ? 378  GLN B CA  1 
ATOM   2859 C C   . GLN A 1 380 ? -2.235  -5.728  8.358   1.00 42.33 ? 378  GLN B C   1 
ATOM   2860 O O   . GLN A 1 380 ? -2.903  -5.364  9.339   1.00 44.21 ? 378  GLN B O   1 
ATOM   2861 C CB  . GLN A 1 380 ? -1.716  -3.462  7.288   1.00 47.02 ? 378  GLN B CB  1 
ATOM   2862 C CG  . GLN A 1 380 ? -0.635  -2.438  6.964   1.00 52.00 ? 378  GLN B CG  1 
ATOM   2863 C CD  . GLN A 1 380 ? 0.057   -1.914  8.203   1.00 56.63 ? 378  GLN B CD  1 
ATOM   2864 O OE1 . GLN A 1 380 ? 0.226   -2.614  9.201   1.00 61.31 ? 378  GLN B OE1 1 
ATOM   2865 N NE2 . GLN A 1 380 ? 0.457   -0.652  8.155   1.00 62.63 ? 378  GLN B NE2 1 
ATOM   2866 N N   . ASP A 1 381 ? -2.394  -6.903  7.741   1.00 35.82 ? 379  ASP B N   1 
ATOM   2867 C CA  . ASP A 1 381 ? -3.447  -7.893  8.080   1.00 35.87 ? 379  ASP B CA  1 
ATOM   2868 C C   . ASP A 1 381 ? -2.841  -8.848  9.112   1.00 41.07 ? 379  ASP B C   1 
ATOM   2869 O O   . ASP A 1 381 ? -1.935  -9.629  8.744   1.00 35.48 ? 379  ASP B O   1 
ATOM   2870 C CB  . ASP A 1 381 ? -3.947  -8.522  6.782   1.00 35.66 ? 379  ASP B CB  1 
ATOM   2871 C CG  . ASP A 1 381 ? -5.016  -9.585  6.892   1.00 39.09 ? 379  ASP B CG  1 
ATOM   2872 O OD1 . ASP A 1 381 ? -5.110  -10.207 7.931   1.00 39.20 ? 379  ASP B OD1 1 
ATOM   2873 O OD2 . ASP A 1 381 ? -5.710  -9.806  5.883   1.00 49.53 ? 379  ASP B OD2 1 
ATOM   2874 N N   . GLU A 1 382 ? -3.267  -8.739  10.368  1.00 38.85 ? 380  GLU B N   1 
ATOM   2875 C CA  . GLU A 1 382 ? -2.704  -9.531  11.490  1.00 42.16 ? 380  GLU B CA  1 
ATOM   2876 C C   . GLU A 1 382 ? -2.871  -11.028 11.213  1.00 37.59 ? 380  GLU B C   1 
ATOM   2877 O O   . GLU A 1 382 ? -1.946  -11.767 11.569  1.00 32.79 ? 380  GLU B O   1 
ATOM   2878 C CB  . GLU A 1 382 ? -3.351  -9.147  12.821  1.00 46.03 ? 380  GLU B CB  1 
ATOM   2879 C CG  . GLU A 1 382 ? -2.803  -7.850  13.383  1.00 54.29 ? 380  GLU B CG  1 
ATOM   2880 C CD  . GLU A 1 382 ? -1.290  -7.707  13.303  1.00 55.46 ? 380  GLU B CD  1 
ATOM   2881 O OE1 . GLU A 1 382 ? -0.824  -6.697  12.733  1.00 61.90 ? 380  GLU B OE1 1 
ATOM   2882 O OE2 . GLU A 1 382 ? -0.585  -8.599  13.815  1.00 53.38 ? 380  GLU B OE2 1 
ATOM   2883 N N   . GLU A 1 383 ? -4.005  -11.437 10.642  1.00 33.83 ? 381  GLU B N   1 
ATOM   2884 C CA  . GLU A 1 383 ? -4.321  -12.854 10.322  1.00 41.40 ? 381  GLU B CA  1 
ATOM   2885 C C   . GLU A 1 383 ? -3.375  -13.359 9.220   1.00 39.90 ? 381  GLU B C   1 
ATOM   2886 O O   . GLU A 1 383 ? -2.833  -14.469 9.390   1.00 34.64 ? 381  GLU B O   1 
ATOM   2887 C CB  . GLU A 1 383 ? -5.778  -13.018 9.893   1.00 45.80 ? 381  GLU B CB  1 
ATOM   2888 C CG  . GLU A 1 383 ? -6.764  -12.833 11.037  1.00 51.34 ? 381  GLU B CG  1 
ATOM   2889 C CD  . GLU A 1 383 ? -6.378  -13.611 12.277  1.00 56.09 ? 381  GLU B CD  1 
ATOM   2890 O OE1 . GLU A 1 383 ? -5.990  -12.977 13.274  1.00 58.47 ? 381  GLU B OE1 1 
ATOM   2891 O OE2 . GLU A 1 383 ? -6.435  -14.852 12.222  1.00 67.87 ? 381  GLU B OE2 1 
ATOM   2892 N N   . GLN A 1 384 ? -3.183  -12.577 8.145   1.00 34.91 ? 382  GLN B N   1 
ATOM   2893 C CA  . GLN A 1 384 ? -2.220  -12.895 7.061   1.00 34.00 ? 382  GLN B CA  1 
ATOM   2894 C C   . GLN A 1 384 ? -0.811  -13.003 7.662   1.00 31.24 ? 382  GLN B C   1 
ATOM   2895 O O   . GLN A 1 384 ? -0.039  -13.914 7.230   1.00 28.73 ? 382  GLN B O   1 
ATOM   2896 C CB  . GLN A 1 384 ? -2.277  -11.836 5.961   1.00 37.58 ? 382  GLN B CB  1 
ATOM   2897 C CG  . GLN A 1 384 ? -1.640  -12.301 4.661   1.00 44.50 ? 382  GLN B CG  1 
ATOM   2898 C CD  . GLN A 1 384 ? -1.430  -11.176 3.683   1.00 46.22 ? 382  GLN B CD  1 
ATOM   2899 O OE1 . GLN A 1 384 ? -1.490  -10.005 4.042   1.00 52.26 ? 382  GLN B OE1 1 
ATOM   2900 N NE2 . GLN A 1 384 ? -1.195  -11.531 2.431   1.00 51.93 ? 382  GLN B NE2 1 
ATOM   2901 N N   . LYS A 1 385 ? -0.441  -12.083 8.552   1.00 28.94 ? 383  LYS B N   1 
ATOM   2902 C CA  . LYS A 1 385 ? 0.900   -12.046 9.177   1.00 29.23 ? 383  LYS B CA  1 
ATOM   2903 C C   . LYS A 1 385 ? 1.109   -13.303 10.037  1.00 29.25 ? 383  LYS B C   1 
ATOM   2904 O O   . LYS A 1 385 ? 2.192   -13.914 9.962   1.00 25.29 ? 383  LYS B O   1 
ATOM   2905 C CB  . LYS A 1 385 ? 1.091   -10.794 10.030  1.00 33.54 ? 383  LYS B CB  1 
ATOM   2906 C CG  . LYS A 1 385 ? 2.538   -10.549 10.424  1.00 39.74 ? 383  LYS B CG  1 
ATOM   2907 C CD  . LYS A 1 385 ? 2.753   -9.697  11.642  1.00 43.85 ? 383  LYS B CD  1 
ATOM   2908 C CE  . LYS A 1 385 ? 2.780   -8.217  11.343  1.00 48.70 ? 383  LYS B CE  1 
ATOM   2909 N NZ  . LYS A 1 385 ? 3.774   -7.533  12.208  1.00 51.77 ? 383  LYS B NZ  1 
ATOM   2910 N N   . LYS A 1 386 ? 0.129   -13.673 10.858  1.00 27.88 ? 384  LYS B N   1 
ATOM   2911 C CA  . LYS A 1 386 ? 0.236   -14.891 11.706  1.00 29.25 ? 384  LYS B CA  1 
ATOM   2912 C C   . LYS A 1 386 ? 0.449   -16.123 10.812  1.00 29.09 ? 384  LYS B C   1 
ATOM   2913 O O   . LYS A 1 386 ? 1.292   -16.996 11.171  1.00 26.41 ? 384  LYS B O   1 
ATOM   2914 C CB  . LYS A 1 386 ? -1.018  -15.065 12.569  1.00 36.25 ? 384  LYS B CB  1 
ATOM   2915 C CG  . LYS A 1 386 ? -0.882  -16.103 13.676  1.00 44.04 ? 384  LYS B CG  1 
ATOM   2916 C CD  . LYS A 1 386 ? -2.198  -16.574 14.316  1.00 48.80 ? 384  LYS B CD  1 
ATOM   2917 C CE  . LYS A 1 386 ? -1.963  -17.621 15.390  1.00 52.59 ? 384  LYS B CE  1 
ATOM   2918 N NZ  . LYS A 1 386 ? -3.187  -17.905 16.176  1.00 55.19 ? 384  LYS B NZ  1 
ATOM   2919 N N   . ALA A 1 387 ? -0.324  -16.248 9.730   1.00 26.76 ? 385  ALA B N   1 
ATOM   2920 C CA  . ALA A 1 387 ? -0.266  -17.429 8.834   1.00 25.98 ? 385  ALA B CA  1 
ATOM   2921 C C   . ALA A 1 387 ? 1.122   -17.496 8.188   1.00 24.99 ? 385  ALA B C   1 
ATOM   2922 O O   . ALA A 1 387 ? 1.679   -18.613 8.070   1.00 24.55 ? 385  ALA B O   1 
ATOM   2923 C CB  . ALA A 1 387 ? -1.365  -17.386 7.813   1.00 27.61 ? 385  ALA B CB  1 
ATOM   2924 N N   . ALA A 1 388 ? 1.648   -16.353 7.751   1.00 23.03 ? 386  ALA B N   1 
ATOM   2925 C CA  . ALA A 1 388 ? 2.956   -16.261 7.071   1.00 22.66 ? 386  ALA B CA  1 
ATOM   2926 C C   . ALA A 1 388 ? 4.043   -16.599 8.083   1.00 23.54 ? 386  ALA B C   1 
ATOM   2927 O O   . ALA A 1 388 ? 5.000   -17.312 7.694   1.00 20.80 ? 386  ALA B O   1 
ATOM   2928 C CB  . ALA A 1 388 ? 3.158   -14.900 6.452   1.00 21.84 ? 386  ALA B CB  1 
ATOM   2929 N N   . ASP A 1 389 ? 3.897   -16.141 9.332   1.00 20.43 ? 387  ASP B N   1 
ATOM   2930 C CA  . ASP A 1 389 ? 4.929   -16.379 10.357  1.00 23.83 ? 387  ASP B CA  1 
ATOM   2931 C C   . ASP A 1 389 ? 4.986   -17.888 10.642  1.00 21.81 ? 387  ASP B C   1 
ATOM   2932 O O   . ASP A 1 389 ? 6.105   -18.448 10.751  1.00 21.76 ? 387  ASP B O   1 
ATOM   2933 C CB  . ASP A 1 389 ? 4.651   -15.573 11.622  1.00 27.36 ? 387  ASP B CB  1 
ATOM   2934 C CG  . ASP A 1 389 ? 5.892   -15.493 12.484  1.00 35.26 ? 387  ASP B CG  1 
ATOM   2935 O OD1 . ASP A 1 389 ? 6.932   -15.049 11.971  1.00 39.08 ? 387  ASP B OD1 1 
ATOM   2936 O OD2 . ASP A 1 389 ? 5.829   -15.979 13.615  1.00 46.26 ? 387  ASP B OD2 1 
ATOM   2937 N N   . SER A 1 390 ? 3.828   -18.521 10.779  1.00 20.97 ? 388  SER B N   1 
ATOM   2938 C CA  . SER A 1 390 ? 3.722   -19.978 11.030  1.00 23.53 ? 388  SER B CA  1 
ATOM   2939 C C   . SER A 1 390 ? 4.364   -20.722 9.839   1.00 21.70 ? 388  SER B C   1 
ATOM   2940 O O   . SER A 1 390 ? 5.172   -21.656 10.060  1.00 20.57 ? 388  SER B O   1 
ATOM   2941 C CB  . SER A 1 390 ? 2.272   -20.360 11.225  1.00 25.73 ? 388  SER B CB  1 
ATOM   2942 O OG  . SER A 1 390 ? 2.099   -21.767 11.184  1.00 26.71 ? 388  SER B OG  1 
ATOM   2943 N N   . MET A 1 391 ? 4.039   -20.326 8.621   1.00 18.63 ? 389  MET B N   1 
ATOM   2944 C CA  . MET A 1 391 ? 4.542   -21.033 7.410   1.00 19.20 ? 389  MET B CA  1 
ATOM   2945 C C   . MET A 1 391 ? 6.060   -20.855 7.353   1.00 19.26 ? 389  MET B C   1 
ATOM   2946 O O   . MET A 1 391 ? 6.756   -21.862 7.072   1.00 18.91 ? 389  MET B O   1 
ATOM   2947 C CB  . MET A 1 391 ? 3.927   -20.491 6.123   1.00 20.21 ? 389  MET B CB  1 
ATOM   2948 C CG  . MET A 1 391 ? 4.410   -21.192 4.862   1.00 20.17 ? 389  MET B CG  1 
ATOM   2949 S SD  . MET A 1 391 ? 3.956   -22.968 4.810   1.00 22.15 ? 389  MET B SD  1 
ATOM   2950 C CE  . MET A 1 391 ? 2.170   -22.862 4.710   1.00 22.55 ? 389  MET B CE  1 
ATOM   2951 N N   . LEU A 1 392 ? 6.573   -19.659 7.613   1.00 18.07 ? 390  LEU B N   1 
ATOM   2952 C CA  . LEU A 1 392 ? 8.041   -19.431 7.562   1.00 18.24 ? 390  LEU B CA  1 
ATOM   2953 C C   . LEU A 1 392 ? 8.749   -20.268 8.649   1.00 18.65 ? 390  LEU B C   1 
ATOM   2954 O O   . LEU A 1 392 ? 9.796   -20.830 8.353   1.00 18.77 ? 390  LEU B O   1 
ATOM   2955 C CB  . LEU A 1 392 ? 8.326   -17.933 7.702   1.00 17.94 ? 390  LEU B CB  1 
ATOM   2956 C CG  . LEU A 1 392 ? 9.789   -17.509 7.641   1.00 18.90 ? 390  LEU B CG  1 
ATOM   2957 C CD1 . LEU A 1 392 ? 10.400  -17.885 6.301   1.00 19.65 ? 390  LEU B CD1 1 
ATOM   2958 C CD2 . LEU A 1 392 ? 9.912   -16.013 7.886   1.00 20.57 ? 390  LEU B CD2 1 
ATOM   2959 N N   . ALA A 1 393 ? 8.197   -20.318 9.858   1.00 18.37 ? 391  ALA B N   1 
ATOM   2960 C CA  . ALA A 1 393 ? 8.800   -21.088 10.973  1.00 19.31 ? 391  ALA B CA  1 
ATOM   2961 C C   . ALA A 1 393 ? 8.865   -22.572 10.606  1.00 19.57 ? 391  ALA B C   1 
ATOM   2962 O O   . ALA A 1 393 ? 9.829   -23.220 10.993  1.00 19.17 ? 391  ALA B O   1 
ATOM   2963 C CB  . ALA A 1 393 ? 7.964   -20.891 12.203  1.00 21.93 ? 391  ALA B CB  1 
ATOM   2964 N N   . PHE A 1 394 ? 7.861   -23.045 9.878   1.00 18.76 ? 392  PHE B N   1 
ATOM   2965 C CA  . PHE A 1 394 ? 7.760   -24.458 9.442   1.00 18.42 ? 392  PHE B CA  1 
ATOM   2966 C C   . PHE A 1 394 ? 8.821   -24.704 8.362   1.00 19.16 ? 392  PHE B C   1 
ATOM   2967 O O   . PHE A 1 394 ? 9.630   -25.681 8.471   1.00 17.38 ? 392  PHE B O   1 
ATOM   2968 C CB  . PHE A 1 394 ? 6.348   -24.760 8.956   1.00 19.91 ? 392  PHE B CB  1 
ATOM   2969 C CG  . PHE A 1 394 ? 6.192   -26.082 8.273   1.00 17.89 ? 392  PHE B CG  1 
ATOM   2970 C CD1 . PHE A 1 394 ? 6.185   -27.257 9.005   1.00 17.98 ? 392  PHE B CD1 1 
ATOM   2971 C CD2 . PHE A 1 394 ? 6.011   -26.156 6.899   1.00 18.27 ? 392  PHE B CD2 1 
ATOM   2972 C CE1 . PHE A 1 394 ? 5.959   -28.476 8.380   1.00 17.76 ? 392  PHE B CE1 1 
ATOM   2973 C CE2 . PHE A 1 394 ? 5.835   -27.379 6.274   1.00 17.66 ? 392  PHE B CE2 1 
ATOM   2974 C CZ  . PHE A 1 394 ? 5.805   -28.534 7.022   1.00 18.21 ? 392  PHE B CZ  1 
ATOM   2975 N N   . LEU A 1 395 ? 8.894   -23.824 7.365   1.00 17.36 ? 393  LEU B N   1 
ATOM   2976 C CA  . LEU A 1 395 ? 9.773   -24.068 6.194   1.00 18.24 ? 393  LEU B CA  1 
ATOM   2977 C C   . LEU A 1 395 ? 11.247  -23.822 6.530   1.00 17.02 ? 393  LEU B C   1 
ATOM   2978 O O   . LEU A 1 395 ? 12.062  -24.376 5.820   1.00 16.51 ? 393  LEU B O   1 
ATOM   2979 C CB  . LEU A 1 395 ? 9.352   -23.181 5.036   1.00 19.16 ? 393  LEU B CB  1 
ATOM   2980 C CG  . LEU A 1 395 ? 7.996   -23.528 4.439   1.00 19.84 ? 393  LEU B CG  1 
ATOM   2981 C CD1 . LEU A 1 395 ? 7.643   -22.482 3.408   1.00 23.10 ? 393  LEU B CD1 1 
ATOM   2982 C CD2 . LEU A 1 395 ? 8.000   -24.928 3.846   1.00 22.46 ? 393  LEU B CD2 1 
ATOM   2983 N N   . THR A 1 396 ? 11.565  -22.957 7.486   1.00 15.66 ? 394  THR B N   1 
ATOM   2984 C CA  . THR A 1 396 ? 12.987  -22.571 7.710   1.00 15.34 ? 394  THR B CA  1 
ATOM   2985 C C   . THR A 1 396 ? 13.872  -23.812 7.959   1.00 15.67 ? 394  THR B C   1 
ATOM   2986 O O   . THR A 1 396 ? 14.883  -23.946 7.264   1.00 15.01 ? 394  THR B O   1 
ATOM   2987 C CB  . THR A 1 396 ? 13.112  -21.460 8.773   1.00 17.52 ? 394  THR B CB  1 
ATOM   2988 O OG1 . THR A 1 396 ? 12.485  -20.272 8.299   1.00 17.97 ? 394  THR B OG1 1 
ATOM   2989 C CG2 . THR A 1 396 ? 14.550  -21.172 9.141   1.00 17.33 ? 394  THR B CG2 1 
ATOM   2990 N N   . PRO A 1 397 ? 13.561  -24.704 8.919   1.00 14.72 ? 395  PRO B N   1 
ATOM   2991 C CA  . PRO A 1 397 ? 14.424  -25.875 9.154   1.00 14.85 ? 395  PRO B CA  1 
ATOM   2992 C C   . PRO A 1 397 ? 14.396  -26.842 7.967   1.00 15.23 ? 395  PRO B C   1 
ATOM   2993 O O   . PRO A 1 397 ? 15.448  -27.443 7.677   1.00 15.26 ? 395  PRO B O   1 
ATOM   2994 C CB  . PRO A 1 397 ? 13.845  -26.546 10.398  1.00 15.18 ? 395  PRO B CB  1 
ATOM   2995 C CG  . PRO A 1 397 ? 12.428  -25.988 10.512  1.00 16.66 ? 395  PRO B CG  1 
ATOM   2996 C CD  . PRO A 1 397 ? 12.525  -24.585 9.962   1.00 16.40 ? 395  PRO B CD  1 
ATOM   2997 N N   . ILE A 1 398 ? 13.240  -27.024 7.326   1.00 15.02 ? 396  ILE B N   1 
ATOM   2998 C CA  . ILE A 1 398 ? 13.145  -27.885 6.114   1.00 15.32 ? 396  ILE B CA  1 
ATOM   2999 C C   . ILE A 1 398 ? 14.064  -27.329 5.031   1.00 15.03 ? 396  ILE B C   1 
ATOM   3000 O O   . ILE A 1 398 ? 14.934  -28.083 4.510   1.00 14.72 ? 396  ILE B O   1 
ATOM   3001 C CB  . ILE A 1 398 ? 11.700  -28.017 5.596   1.00 14.06 ? 396  ILE B CB  1 
ATOM   3002 C CG1 . ILE A 1 398 ? 10.831  -28.725 6.622   1.00 14.55 ? 396  ILE B CG1 1 
ATOM   3003 C CG2 . ILE A 1 398 ? 11.679  -28.722 4.241   1.00 15.88 ? 396  ILE B CG2 1 
ATOM   3004 C CD1 . ILE A 1 398 ? 9.333   -28.622 6.344   1.00 15.15 ? 396  ILE B CD1 1 
ATOM   3005 N N   . ALA A 1 399 ? 13.967  -26.036 4.716   1.00 13.83 ? 397  ALA B N   1 
ATOM   3006 C CA  . ALA A 1 399 ? 14.813  -25.419 3.679   1.00 14.75 ? 397  ALA B CA  1 
ATOM   3007 C C   . ALA A 1 399 ? 16.294  -25.580 4.064   1.00 14.50 ? 397  ALA B C   1 
ATOM   3008 O O   . ALA A 1 399 ? 17.066  -26.060 3.253   1.00 13.75 ? 397  ALA B O   1 
ATOM   3009 C CB  . ALA A 1 399 ? 14.442  -23.978 3.440   1.00 14.15 ? 397  ALA B CB  1 
ATOM   3010 N N   . LYS A 1 400 ? 16.669  -25.217 5.272   1.00 13.71 ? 398  LYS B N   1 
ATOM   3011 C CA  . LYS A 1 400 ? 18.113  -25.285 5.589   1.00 13.19 ? 398  LYS B CA  1 
ATOM   3012 C C   . LYS A 1 400 ? 18.660  -26.719 5.448   1.00 13.14 ? 398  LYS B C   1 
ATOM   3013 O O   . LYS A 1 400 ? 19.607  -26.910 4.703   1.00 13.67 ? 398  LYS B O   1 
ATOM   3014 C CB  . LYS A 1 400 ? 18.340  -24.799 7.022   1.00 15.06 ? 398  LYS B CB  1 
ATOM   3015 C CG  . LYS A 1 400 ? 19.783  -24.448 7.363   1.00 14.58 ? 398  LYS B CG  1 
ATOM   3016 C CD  . LYS A 1 400 ? 20.662  -25.644 7.658   1.00 15.29 ? 398  LYS B CD  1 
ATOM   3017 C CE  . LYS A 1 400 ? 22.058  -25.250 8.085   1.00 15.53 ? 398  LYS B CE  1 
ATOM   3018 N NZ  . LYS A 1 400 ? 22.914  -26.430 8.356   1.00 14.65 ? 398  LYS B NZ  1 
ATOM   3019 N N   . ALA A 1 401 ? 18.066  -27.666 6.162   1.00 13.22 ? 399  ALA B N   1 
ATOM   3020 C CA  . ALA A 1 401 ? 18.633  -29.036 6.223   1.00 12.18 ? 399  ALA B CA  1 
ATOM   3021 C C   . ALA A 1 401 ? 18.386  -29.746 4.895   1.00 13.63 ? 399  ALA B C   1 
ATOM   3022 O O   . ALA A 1 401 ? 19.310  -30.419 4.393   1.00 13.61 ? 399  ALA B O   1 
ATOM   3023 C CB  . ALA A 1 401 ? 18.078  -29.810 7.369   1.00 12.92 ? 399  ALA B CB  1 
ATOM   3024 N N   . PHE A 1 402 ? 17.151  -29.732 4.373   1.00 12.91 ? 400  PHE B N   1 
ATOM   3025 C CA  . PHE A 1 402 ? 16.887  -30.476 3.119   1.00 13.29 ? 400  PHE B CA  1 
ATOM   3026 C C   . PHE A 1 402 ? 17.719  -29.895 1.966   1.00 12.78 ? 400  PHE B C   1 
ATOM   3027 O O   . PHE A 1 402 ? 18.332  -30.678 1.201   1.00 12.72 ? 400  PHE B O   1 
ATOM   3028 C CB  . PHE A 1 402 ? 15.395  -30.482 2.799   1.00 13.22 ? 400  PHE B CB  1 
ATOM   3029 C CG  . PHE A 1 402 ? 15.019  -31.244 1.555   1.00 13.67 ? 400  PHE B CG  1 
ATOM   3030 C CD1 . PHE A 1 402 ? 14.859  -32.627 1.570   1.00 12.99 ? 400  PHE B CD1 1 
ATOM   3031 C CD2 . PHE A 1 402 ? 14.873  -30.587 0.355   1.00 13.52 ? 400  PHE B CD2 1 
ATOM   3032 C CE1 . PHE A 1 402 ? 14.496  -33.315 0.419   1.00 14.26 ? 400  PHE B CE1 1 
ATOM   3033 C CE2 . PHE A 1 402 ? 14.524  -31.273 -0.796  1.00 14.81 ? 400  PHE B CE2 1 
ATOM   3034 C CZ  . PHE A 1 402 ? 14.345  -32.644 -0.765  1.00 14.83 ? 400  PHE B CZ  1 
ATOM   3035 N N   . MET A 1 403 ? 17.714  -28.581 1.763   1.00 12.85 ? 401  MET B N   1 
ATOM   3036 C CA  . MET A 1 403 ? 18.411  -28.049 0.559   1.00 12.99 ? 401  MET B CA  1 
ATOM   3037 C C   . MET A 1 403 ? 19.930  -28.307 0.653   1.00 13.37 ? 401  MET B C   1 
ATOM   3038 O O   . MET A 1 403 ? 20.539  -28.536 -0.361  1.00 13.83 ? 401  MET B O   1 
ATOM   3039 C CB  . MET A 1 403 ? 18.140  -26.549 0.378   1.00 14.15 ? 401  MET B CB  1 
ATOM   3040 C CG  . MET A 1 403 ? 16.682  -26.218 0.157   1.00 14.98 ? 401  MET B CG  1 
ATOM   3041 S SD  . MET A 1 403 ? 16.456  -24.508 -0.400  1.00 16.36 ? 401  MET B SD  1 
ATOM   3042 C CE  . MET A 1 403 ? 14.667  -24.413 -0.421  1.00 18.65 ? 401  MET B CE  1 
ATOM   3043 N N   . THR A 1 404 ? 20.480  -28.227 1.865   1.00 11.94 ? 402  THR B N   1 
ATOM   3044 C CA  . THR A 1 404 ? 21.932  -28.493 2.047   1.00 12.27 ? 402  THR B CA  1 
ATOM   3045 C C   . THR A 1 404 ? 22.244  -29.980 1.818   1.00 12.36 ? 402  THR B C   1 
ATOM   3046 O O   . THR A 1 404 ? 23.227  -30.251 1.148   1.00 12.66 ? 402  THR B O   1 
ATOM   3047 C CB  . THR A 1 404 ? 22.448  -27.990 3.408   1.00 13.16 ? 402  THR B CB  1 
ATOM   3048 O OG1 . THR A 1 404 ? 21.677  -28.517 4.481   1.00 13.12 ? 402  THR B OG1 1 
ATOM   3049 C CG2 . THR A 1 404 ? 22.449  -26.478 3.471   1.00 12.87 ? 402  THR B CG2 1 
ATOM   3050 N N   . GLU A 1 405 ? 21.445  -30.870 2.407   1.00 12.74 ? 403  GLU B N   1 
ATOM   3051 C CA  . GLU A 1 405 ? 21.716  -32.312 2.259   1.00 12.65 ? 403  GLU B CA  1 
ATOM   3052 C C   . GLU A 1 405 ? 21.632  -32.675 0.760   1.00 12.35 ? 403  GLU B C   1 
ATOM   3053 O O   . GLU A 1 405 ? 22.542  -33.366 0.238   1.00 12.92 ? 403  GLU B O   1 
ATOM   3054 C CB  . GLU A 1 405 ? 20.766  -33.123 3.124   1.00 12.45 ? 403  GLU B CB  1 
ATOM   3055 C CG  . GLU A 1 405 ? 21.024  -33.012 4.611   1.00 12.28 ? 403  GLU B CG  1 
ATOM   3056 C CD  . GLU A 1 405 ? 22.220  -33.812 5.081   1.00 14.77 ? 403  GLU B CD  1 
ATOM   3057 O OE1 . GLU A 1 405 ? 22.690  -33.533 6.176   1.00 15.06 ? 403  GLU B OE1 1 
ATOM   3058 O OE2 . GLU A 1 405 ? 22.645  -34.739 4.375   1.00 15.77 ? 403  GLU B OE2 1 
ATOM   3059 N N   . VAL A 1 406 ? 20.569  -32.311 0.073   1.00 11.83 ? 404  VAL B N   1 
ATOM   3060 C CA  . VAL A 1 406 ? 20.438  -32.691 -1.367  1.00 12.51 ? 404  VAL B CA  1 
ATOM   3061 C C   . VAL A 1 406 ? 21.354  -31.826 -2.236  1.00 12.97 ? 404  VAL B C   1 
ATOM   3062 O O   . VAL A 1 406 ? 21.707  -32.278 -3.354  1.00 12.78 ? 404  VAL B O   1 
ATOM   3063 C CB  . VAL A 1 406 ? 18.966  -32.699 -1.841  1.00 13.44 ? 404  VAL B CB  1 
ATOM   3064 C CG1 . VAL A 1 406 ? 18.130  -33.569 -0.918  1.00 14.28 ? 404  VAL B CG1 1 
ATOM   3065 C CG2 . VAL A 1 406 ? 18.383  -31.299 -2.008  1.00 13.69 ? 404  VAL B CG2 1 
ATOM   3066 N N   . GLY A 1 407 ? 21.798  -30.660 -1.761  1.00 12.06 ? 405  GLY B N   1 
ATOM   3067 C CA  . GLY A 1 407 ? 22.787  -29.864 -2.525  1.00 11.86 ? 405  GLY B CA  1 
ATOM   3068 C C   . GLY A 1 407 ? 24.156  -30.534 -2.527  1.00 12.26 ? 405  GLY B C   1 
ATOM   3069 O O   . GLY A 1 407 ? 24.839  -30.481 -3.524  1.00 13.34 ? 405  GLY B O   1 
ATOM   3070 N N   . PHE A 1 408 ? 24.508  -31.163 -1.410  1.00 12.72 ? 406  PHE B N   1 
ATOM   3071 C CA  . PHE A 1 408 ? 25.778  -31.929 -1.323  1.00 13.21 ? 406  PHE B CA  1 
ATOM   3072 C C   . PHE A 1 408 ? 25.687  -33.172 -2.221  1.00 13.01 ? 406  PHE B C   1 
ATOM   3073 O O   . PHE A 1 408 ? 26.645  -33.455 -2.919  1.00 12.65 ? 406  PHE B O   1 
ATOM   3074 C CB  . PHE A 1 408 ? 26.055  -32.274 0.143   1.00 12.86 ? 406  PHE B CB  1 
ATOM   3075 C CG  . PHE A 1 408 ? 27.359  -32.993 0.372   1.00 12.16 ? 406  PHE B CG  1 
ATOM   3076 C CD1 . PHE A 1 408 ? 28.565  -32.322 0.262   1.00 12.33 ? 406  PHE B CD1 1 
ATOM   3077 C CD2 . PHE A 1 408 ? 27.382  -34.342 0.682   1.00 13.00 ? 406  PHE B CD2 1 
ATOM   3078 C CE1 . PHE A 1 408 ? 29.766  -32.981 0.464   1.00 12.06 ? 406  PHE B CE1 1 
ATOM   3079 C CE2 . PHE A 1 408 ? 28.584  -34.999 0.885   1.00 13.35 ? 406  PHE B CE2 1 
ATOM   3080 C CZ  . PHE A 1 408 ? 29.772  -34.318 0.780   1.00 12.83 ? 406  PHE B CZ  1 
ATOM   3081 N N   . GLU A 1 409 ? 24.558  -33.884 -2.163  1.00 12.41 ? 407  GLU B N   1 
ATOM   3082 C CA  . GLU A 1 409 ? 24.354  -35.011 -3.070  1.00 12.86 ? 407  GLU B CA  1 
ATOM   3083 C C   . GLU A 1 409 ? 24.521  -34.492 -4.497  1.00 12.40 ? 407  GLU B C   1 
ATOM   3084 O O   . GLU A 1 409 ? 25.243  -35.122 -5.278  1.00 13.22 ? 407  GLU B O   1 
ATOM   3085 C CB  . GLU A 1 409 ? 22.965  -35.600 -2.894  1.00 12.71 ? 407  GLU B CB  1 
ATOM   3086 C CG  . GLU A 1 409 ? 22.698  -36.727 -3.852  1.00 12.93 ? 407  GLU B CG  1 
ATOM   3087 C CD  . GLU A 1 409 ? 21.271  -37.221 -3.910  1.00 14.73 ? 407  GLU B CD  1 
ATOM   3088 O OE1 . GLU A 1 409 ? 20.881  -37.798 -4.920  1.00 15.03 ? 407  GLU B OE1 1 
ATOM   3089 O OE2 . GLU A 1 409 ? 20.573  -37.053 -2.922  1.00 16.48 ? 407  GLU B OE2 1 
ATOM   3090 N N   . SER A 1 410 ? 23.853  -33.385 -4.842  1.00 12.81 ? 408  SER B N   1 
ATOM   3091 C CA  . SER A 1 410 ? 23.866  -32.809 -6.215  1.00 12.26 ? 408  SER B CA  1 
ATOM   3092 C C   . SER A 1 410 ? 25.298  -32.420 -6.618  1.00 12.13 ? 408  SER B C   1 
ATOM   3093 O O   . SER A 1 410 ? 25.712  -32.697 -7.771  1.00 12.91 ? 408  SER B O   1 
ATOM   3094 C CB  . SER A 1 410 ? 22.936  -31.642 -6.317  1.00 12.45 ? 408  SER B CB  1 
ATOM   3095 O OG  . SER A 1 410 ? 21.596  -32.087 -6.117  1.00 13.61 ? 408  SER B OG  1 
ATOM   3096 N N   . ALA A 1 411 ? 26.063  -31.809 -5.721  1.00 11.75 ? 409  ALA B N   1 
ATOM   3097 C CA  . ALA A 1 411 ? 27.485  -31.442 -5.963  1.00 12.54 ? 409  ALA B CA  1 
ATOM   3098 C C   . ALA A 1 411 ? 28.262  -32.718 -6.323  1.00 12.47 ? 409  ALA B C   1 
ATOM   3099 O O   . ALA A 1 411 ? 29.072  -32.704 -7.256  1.00 13.30 ? 409  ALA B O   1 
ATOM   3100 C CB  . ALA A 1 411 ? 28.078  -30.740 -4.798  1.00 12.90 ? 409  ALA B CB  1 
ATOM   3101 N N   . ASN A 1 412 ? 27.986  -33.791 -5.605  1.00 12.52 ? 410  ASN B N   1 
ATOM   3102 C CA  . ASN A 1 412 ? 28.677  -35.087 -5.832  1.00 12.23 ? 410  ASN B CA  1 
ATOM   3103 C C   . ASN A 1 412 ? 28.235  -35.705 -7.160  1.00 12.15 ? 410  ASN B C   1 
ATOM   3104 O O   . ASN A 1 412 ? 29.110  -36.279 -7.820  1.00 13.49 ? 410  ASN B O   1 
ATOM   3105 C CB  . ASN A 1 412 ? 28.519  -35.997 -4.648  1.00 12.31 ? 410  ASN B CB  1 
ATOM   3106 C CG  . ASN A 1 412 ? 29.505  -35.631 -3.583  1.00 12.29 ? 410  ASN B CG  1 
ATOM   3107 O OD1 . ASN A 1 412 ? 30.708  -35.765 -3.771  1.00 12.43 ? 410  ASN B OD1 1 
ATOM   3108 N ND2 . ASN A 1 412 ? 29.001  -35.126 -2.472  1.00 13.16 ? 410  ASN B ND2 1 
ATOM   3109 N N   . HIS A 1 413 ? 26.980  -35.572 -7.584  1.00 12.46 ? 411  HIS B N   1 
ATOM   3110 C CA  . HIS A 1 413 ? 26.575  -36.023 -8.942  1.00 12.83 ? 411  HIS B CA  1 
ATOM   3111 C C   . HIS A 1 413 ? 27.367  -35.256 -9.994  1.00 14.18 ? 411  HIS B C   1 
ATOM   3112 O O   . HIS A 1 413 ? 27.785  -35.859 -11.009 1.00 13.65 ? 411  HIS B O   1 
ATOM   3113 C CB  . HIS A 1 413 ? 25.087  -35.862 -9.165  1.00 13.98 ? 411  HIS B CB  1 
ATOM   3114 C CG  . HIS A 1 413 ? 24.261  -36.783 -8.349  1.00 14.37 ? 411  HIS B CG  1 
ATOM   3115 N ND1 . HIS A 1 413 ? 24.515  -38.156 -8.295  1.00 16.84 ? 411  HIS B ND1 1 
ATOM   3116 C CD2 . HIS A 1 413 ? 23.137  -36.571 -7.632  1.00 15.32 ? 411  HIS B CD2 1 
ATOM   3117 C CE1 . HIS A 1 413 ? 23.589  -38.715 -7.514  1.00 16.71 ? 411  HIS B CE1 1 
ATOM   3118 N NE2 . HIS A 1 413 ? 22.726  -37.754 -7.099  1.00 15.80 ? 411  HIS B NE2 1 
ATOM   3119 N N   . GLY A 1 414 ? 27.619  -33.974 -9.754  1.00 14.37 ? 412  GLY B N   1 
ATOM   3120 C CA  . GLY A 1 414 ? 28.401  -33.142 -10.679 1.00 15.00 ? 412  GLY B CA  1 
ATOM   3121 C C   . GLY A 1 414 ? 29.809  -33.693 -10.883 1.00 15.13 ? 412  GLY B C   1 
ATOM   3122 O O   . GLY A 1 414 ? 30.216  -33.920 -12.026 1.00 13.14 ? 412  GLY B O   1 
ATOM   3123 N N   . VAL A 1 415 ? 30.497  -33.971 -9.787  1.00 13.91 ? 413  VAL B N   1 
ATOM   3124 C CA  . VAL A 1 415 ? 31.803  -34.671 -9.817  1.00 13.77 ? 413  VAL B CA  1 
ATOM   3125 C C   . VAL A 1 415 ? 31.675  -35.995 -10.565 1.00 13.47 ? 413  VAL B C   1 
ATOM   3126 O O   . VAL A 1 415 ? 32.531  -36.252 -11.447 1.00 14.16 ? 413  VAL B O   1 
ATOM   3127 C CB  . VAL A 1 415 ? 32.366  -34.835 -8.395  1.00 13.74 ? 413  VAL B CB  1 
ATOM   3128 C CG1 . VAL A 1 415 ? 33.539  -35.815 -8.394  1.00 14.05 ? 413  VAL B CG1 1 
ATOM   3129 C CG2 . VAL A 1 415 ? 32.782  -33.474 -7.866  1.00 15.00 ? 413  VAL B CG2 1 
ATOM   3130 N N   . GLN A 1 416 ? 30.638  -36.795 -10.265 1.00 13.82 ? 414  GLN B N   1 
ATOM   3131 C CA  . GLN A 1 416 ? 30.539  -38.185 -10.774 1.00 12.97 ? 414  GLN B CA  1 
ATOM   3132 C C   . GLN A 1 416 ? 30.461  -38.169 -12.303 1.00 14.15 ? 414  GLN B C   1 
ATOM   3133 O O   . GLN A 1 416 ? 31.083  -39.028 -12.957 1.00 14.40 ? 414  GLN B O   1 
ATOM   3134 C CB  . GLN A 1 416 ? 29.365  -38.931 -10.162 1.00 14.15 ? 414  GLN B CB  1 
ATOM   3135 C CG  . GLN A 1 416 ? 29.413  -40.430 -10.397 1.00 12.88 ? 414  GLN B CG  1 
ATOM   3136 C CD  . GLN A 1 416 ? 30.521  -41.069 -9.592  1.00 15.24 ? 414  GLN B CD  1 
ATOM   3137 O OE1 . GLN A 1 416 ? 31.017  -40.539 -8.606  1.00 13.38 ? 414  GLN B OE1 1 
ATOM   3138 N NE2 . GLN A 1 416 ? 30.946  -42.244 -10.029 1.00 14.62 ? 414  GLN B NE2 1 
ATOM   3139 N N   . ILE A 1 417 ? 29.745  -37.207 -12.877 1.00 14.75 ? 415  ILE B N   1 
ATOM   3140 C CA  . ILE A 1 417 ? 29.609  -37.078 -14.363 1.00 16.06 ? 415  ILE B CA  1 
ATOM   3141 C C   . ILE A 1 417 ? 30.973  -36.865 -15.036 1.00 16.54 ? 415  ILE B C   1 
ATOM   3142 O O   . ILE A 1 417 ? 31.155  -37.344 -16.204 1.00 16.60 ? 415  ILE B O   1 
ATOM   3143 C CB  . ILE A 1 417 ? 28.624  -35.946 -14.681 1.00 14.95 ? 415  ILE B CB  1 
ATOM   3144 C CG1 . ILE A 1 417 ? 27.207  -36.397 -14.333 1.00 15.55 ? 415  ILE B CG1 1 
ATOM   3145 C CG2 . ILE A 1 417 ? 28.701  -35.522 -16.142 1.00 15.64 ? 415  ILE B CG2 1 
ATOM   3146 C CD1 . ILE A 1 417 ? 26.227  -35.279 -14.325 1.00 16.00 ? 415  ILE B CD1 1 
ATOM   3147 N N   . PHE A 1 418 ? 31.890  -36.184 -14.359 1.00 15.92 ? 416  PHE B N   1 
ATOM   3148 C CA  . PHE A 1 418 ? 33.257  -35.939 -14.878 1.00 17.54 ? 416  PHE B CA  1 
ATOM   3149 C C   . PHE A 1 418 ? 34.169  -37.171 -14.772 1.00 17.85 ? 416  PHE B C   1 
ATOM   3150 O O   . PHE A 1 418 ? 35.277  -37.084 -15.303 1.00 20.03 ? 416  PHE B O   1 
ATOM   3151 C CB  . PHE A 1 418 ? 33.897  -34.755 -14.152 1.00 17.74 ? 416  PHE B CB  1 
ATOM   3152 C CG  . PHE A 1 418 ? 33.443  -33.404 -14.638 1.00 18.11 ? 416  PHE B CG  1 
ATOM   3153 C CD1 . PHE A 1 418 ? 32.134  -32.991 -14.470 1.00 18.75 ? 416  PHE B CD1 1 
ATOM   3154 C CD2 . PHE A 1 418 ? 34.347  -32.501 -15.171 1.00 19.38 ? 416  PHE B CD2 1 
ATOM   3155 C CE1 . PHE A 1 418 ? 31.723  -31.738 -14.893 1.00 18.56 ? 416  PHE B CE1 1 
ATOM   3156 C CE2 . PHE A 1 418 ? 33.933  -31.235 -15.568 1.00 20.18 ? 416  PHE B CE2 1 
ATOM   3157 C CZ  . PHE A 1 418 ? 32.620  -30.847 -15.389 1.00 18.78 ? 416  PHE B CZ  1 
ATOM   3158 N N   . GLY A 1 419 ? 33.763  -38.255 -14.115 1.00 17.89 ? 417  GLY B N   1 
ATOM   3159 C CA  . GLY A 1 419 ? 34.647  -39.406 -13.884 1.00 18.74 ? 417  GLY B CA  1 
ATOM   3160 C C   . GLY A 1 419 ? 35.905  -38.983 -13.154 1.00 18.89 ? 417  GLY B C   1 
ATOM   3161 O O   . GLY A 1 419 ? 35.841  -38.104 -12.281 1.00 17.70 ? 417  GLY B O   1 
ATOM   3162 N N   . GLY A 1 420 ? 37.058  -39.576 -13.453 1.00 18.86 ? 418  GLY B N   1 
ATOM   3163 C CA  . GLY A 1 420 ? 38.302  -39.184 -12.758 1.00 20.22 ? 418  GLY B CA  1 
ATOM   3164 C C   . GLY A 1 420 ? 38.627  -37.696 -12.831 1.00 18.59 ? 418  GLY B C   1 
ATOM   3165 O O   . GLY A 1 420 ? 39.205  -37.135 -11.872 1.00 18.36 ? 418  GLY B O   1 
ATOM   3166 N N   . HIS A 1 421 ? 38.316  -37.036 -13.941 1.00 19.37 ? 419  HIS B N   1 
ATOM   3167 C CA  . HIS A 1 421 ? 38.503  -35.576 -14.126 1.00 19.19 ? 419  HIS B CA  1 
ATOM   3168 C C   . HIS A 1 421 ? 37.776  -34.775 -13.032 1.00 19.31 ? 419  HIS B C   1 
ATOM   3169 O O   . HIS A 1 421 ? 38.243  -33.680 -12.684 1.00 19.55 ? 419  HIS B O   1 
ATOM   3170 C CB  . HIS A 1 421 ? 38.053  -35.184 -15.529 1.00 20.51 ? 419  HIS B CB  1 
ATOM   3171 C CG  . HIS A 1 421 ? 39.000  -35.679 -16.574 1.00 22.23 ? 419  HIS B CG  1 
ATOM   3172 N ND1 . HIS A 1 421 ? 38.774  -36.820 -17.298 1.00 27.65 ? 419  HIS B ND1 1 
ATOM   3173 C CD2 . HIS A 1 421 ? 40.192  -35.198 -16.975 1.00 24.87 ? 419  HIS B CD2 1 
ATOM   3174 C CE1 . HIS A 1 421 ? 39.772  -37.003 -18.155 1.00 23.69 ? 419  HIS B CE1 1 
ATOM   3175 N NE2 . HIS A 1 421 ? 40.664  -36.037 -17.962 1.00 29.36 ? 419  HIS B NE2 1 
ATOM   3176 N N   . GLY A 1 422 ? 36.707  -35.333 -12.448 1.00 18.57 ? 420  GLY B N   1 
ATOM   3177 C CA  . GLY A 1 422 ? 35.915  -34.612 -11.431 1.00 17.56 ? 420  GLY B CA  1 
ATOM   3178 C C   . GLY A 1 422 ? 36.690  -34.402 -10.152 1.00 16.70 ? 420  GLY B C   1 
ATOM   3179 O O   . GLY A 1 422 ? 36.351  -33.484 -9.430  1.00 16.63 ? 420  GLY B O   1 
ATOM   3180 N N   . PHE A 1 423 ? 37.739  -35.209 -9.896  1.00 15.94 ? 421  PHE B N   1 
ATOM   3181 C CA  . PHE A 1 423 ? 38.562  -35.157 -8.658  1.00 15.02 ? 421  PHE B CA  1 
ATOM   3182 C C   . PHE A 1 423 ? 39.669  -34.102 -8.762  1.00 15.09 ? 421  PHE B C   1 
ATOM   3183 O O   . PHE A 1 423 ? 40.316  -33.821 -7.765  1.00 15.02 ? 421  PHE B O   1 
ATOM   3184 C CB  . PHE A 1 423 ? 39.197  -36.539 -8.453  1.00 15.47 ? 421  PHE B CB  1 
ATOM   3185 C CG  . PHE A 1 423 ? 39.679  -36.842 -7.063  1.00 16.35 ? 421  PHE B CG  1 
ATOM   3186 C CD1 . PHE A 1 423 ? 38.777  -36.948 -6.014  1.00 15.14 ? 421  PHE B CD1 1 
ATOM   3187 C CD2 . PHE A 1 423 ? 41.018  -37.122 -6.808  1.00 16.73 ? 421  PHE B CD2 1 
ATOM   3188 C CE1 . PHE A 1 423 ? 39.209  -37.252 -4.739  1.00 15.31 ? 421  PHE B CE1 1 
ATOM   3189 C CE2 . PHE A 1 423 ? 41.447  -37.447 -5.536  1.00 15.10 ? 421  PHE B CE2 1 
ATOM   3190 C CZ  . PHE A 1 423 ? 40.539  -37.510 -4.496  1.00 16.55 ? 421  PHE B CZ  1 
ATOM   3191 N N   . ILE A 1 424 ? 39.855  -33.562 -9.969  1.00 16.23 ? 422  ILE B N   1 
ATOM   3192 C CA  . ILE A 1 424 ? 40.980  -32.632 -10.267 1.00 18.22 ? 422  ILE B CA  1 
ATOM   3193 C C   . ILE A 1 424 ? 40.591  -31.178 -9.985  1.00 18.13 ? 422  ILE B C   1 
ATOM   3194 O O   . ILE A 1 424 ? 39.541  -30.752 -10.419 1.00 18.65 ? 422  ILE B O   1 
ATOM   3195 C CB  . ILE A 1 424 ? 41.471  -32.862 -11.715 1.00 19.91 ? 422  ILE B CB  1 
ATOM   3196 C CG1 . ILE A 1 424 ? 41.753  -34.340 -11.993 1.00 21.86 ? 422  ILE B CG1 1 
ATOM   3197 C CG2 . ILE A 1 424 ? 42.672  -31.989 -12.030 1.00 21.18 ? 422  ILE B CG2 1 
ATOM   3198 C CD1 . ILE A 1 424 ? 42.767  -34.952 -11.063 1.00 22.87 ? 422  ILE B CD1 1 
ATOM   3199 N N   . ALA A 1 425 ? 41.498  -30.451 -9.361  1.00 18.57 ? 423  ALA B N   1 
ATOM   3200 C CA  . ALA A 1 425 ? 41.189  -29.084 -8.895  1.00 21.40 ? 423  ALA B CA  1 
ATOM   3201 C C   . ALA A 1 425 ? 40.802  -28.128 -10.014 1.00 23.58 ? 423  ALA B C   1 
ATOM   3202 O O   . ALA A 1 425 ? 39.890  -27.325 -9.812  1.00 24.39 ? 423  ALA B O   1 
ATOM   3203 C CB  . ALA A 1 425 ? 42.417  -28.562 -8.200  1.00 22.94 ? 423  ALA B CB  1 
ATOM   3204 N N   . GLU A 1 426 ? 41.462  -28.239 -11.150 1.00 24.63 ? 424  GLU B N   1 
ATOM   3205 C CA  . GLU A 1 426 ? 41.274  -27.205 -12.203 1.00 30.27 ? 424  GLU B CA  1 
ATOM   3206 C C   . GLU A 1 426 ? 39.787  -27.053 -12.562 1.00 30.60 ? 424  GLU B C   1 
ATOM   3207 O O   . GLU A 1 426 ? 39.392  -25.913 -12.879 1.00 32.41 ? 424  GLU B O   1 
ATOM   3208 C CB  . GLU A 1 426 ? 42.069  -27.519 -13.469 1.00 35.46 ? 424  GLU B CB  1 
ATOM   3209 C CG  . GLU A 1 426 ? 43.574  -27.419 -13.257 1.00 45.79 ? 424  GLU B CG  1 
ATOM   3210 C CD  . GLU A 1 426 ? 44.209  -28.731 -12.803 1.00 46.07 ? 424  GLU B CD  1 
ATOM   3211 O OE1 . GLU A 1 426 ? 44.118  -29.078 -11.576 1.00 29.45 ? 424  GLU B OE1 1 
ATOM   3212 O OE2 . GLU A 1 426 ? 44.753  -29.433 -13.697 1.00 59.94 ? 424  GLU B OE2 1 
ATOM   3213 N N   . HIS A 1 427 ? 38.992  -28.122 -12.503 1.00 26.09 ? 425  HIS B N   1 
ATOM   3214 C CA  . HIS A 1 427 ? 37.582  -28.062 -13.001 1.00 25.10 ? 425  HIS B CA  1 
ATOM   3215 C C   . HIS A 1 427 ? 36.571  -27.435 -12.026 1.00 26.63 ? 425  HIS B C   1 
ATOM   3216 O O   . HIS A 1 427 ? 35.463  -27.146 -12.484 1.00 30.22 ? 425  HIS B O   1 
ATOM   3217 C CB  . HIS A 1 427 ? 37.144  -29.447 -13.468 1.00 26.62 ? 425  HIS B CB  1 
ATOM   3218 C CG  . HIS A 1 427 ? 38.160  -30.073 -14.361 1.00 31.15 ? 425  HIS B CG  1 
ATOM   3219 N ND1 . HIS A 1 427 ? 38.646  -29.428 -15.477 1.00 34.94 ? 425  HIS B ND1 1 
ATOM   3220 C CD2 . HIS A 1 427 ? 38.813  -31.250 -14.289 1.00 31.74 ? 425  HIS B CD2 1 
ATOM   3221 C CE1 . HIS A 1 427 ? 39.542  -30.191 -16.066 1.00 35.30 ? 425  HIS B CE1 1 
ATOM   3222 N NE2 . HIS A 1 427 ? 39.660  -31.315 -15.359 1.00 32.75 ? 425  HIS B NE2 1 
ATOM   3223 N N   . GLY A 1 428 ? 36.906  -27.236 -10.757 1.00 23.20 ? 426  GLY B N   1 
ATOM   3224 C CA  . GLY A 1 428 ? 35.966  -26.538 -9.850  1.00 20.55 ? 426  GLY B CA  1 
ATOM   3225 C C   . GLY A 1 428 ? 34.864  -27.415 -9.260  1.00 18.69 ? 426  GLY B C   1 
ATOM   3226 O O   . GLY A 1 428 ? 34.204  -26.988 -8.335  1.00 17.36 ? 426  GLY B O   1 
ATOM   3227 N N   . MET A 1 429 ? 34.680  -28.607 -9.809  1.00 17.24 ? 427  MET B N   1 
ATOM   3228 C CA  . MET A 1 429 ? 33.568  -29.470 -9.349  1.00 15.98 ? 427  MET B CA  1 
ATOM   3229 C C   . MET A 1 429 ? 33.863  -30.023 -7.946  1.00 15.48 ? 427  MET B C   1 
ATOM   3230 O O   . MET A 1 429 ? 32.944  -30.151 -7.168  1.00 14.69 ? 427  MET B O   1 
ATOM   3231 C CB  . MET A 1 429 ? 33.318  -30.606 -10.346 1.00 18.19 ? 427  MET B CB  1 
ATOM   3232 C CG  . MET A 1 429 ? 33.016  -30.117 -11.750 1.00 17.73 ? 427  MET B CG  1 
ATOM   3233 S SD  . MET A 1 429 ? 31.526  -29.084 -11.841 1.00 19.39 ? 427  MET B SD  1 
ATOM   3234 C CE  . MET A 1 429 ? 30.251  -30.293 -11.503 1.00 16.53 ? 427  MET B CE  1 
ATOM   3235 N N   . GLU A 1 430 ? 35.123  -30.343 -7.679  1.00 13.98 ? 428  GLU B N   1 
ATOM   3236 C CA  . GLU A 1 430 ? 35.493  -30.866 -6.339  1.00 14.77 ? 428  GLU B CA  1 
ATOM   3237 C C   . GLU A 1 430 ? 35.456  -29.717 -5.307  1.00 13.98 ? 428  GLU B C   1 
ATOM   3238 O O   . GLU A 1 430 ? 35.076  -29.956 -4.179  1.00 14.90 ? 428  GLU B O   1 
ATOM   3239 C CB  . GLU A 1 430 ? 36.816  -31.644 -6.418  1.00 15.79 ? 428  GLU B CB  1 
ATOM   3240 C CG  . GLU A 1 430 ? 38.021  -30.816 -6.812  1.00 16.50 ? 428  GLU B CG  1 
ATOM   3241 C CD  . GLU A 1 430 ? 38.716  -30.132 -5.650  1.00 18.18 ? 428  GLU B CD  1 
ATOM   3242 O OE1 . GLU A 1 430 ? 39.297  -29.063 -5.868  1.00 18.91 ? 428  GLU B OE1 1 
ATOM   3243 O OE2 . GLU A 1 430 ? 38.653  -30.661 -4.536  1.00 19.14 ? 428  GLU B OE2 1 
ATOM   3244 N N   . GLN A 1 431 ? 35.809  -28.504 -5.714  1.00 13.55 ? 429  GLN B N   1 
ATOM   3245 C CA  . GLN A 1 431 ? 35.674  -27.356 -4.782  1.00 14.19 ? 429  GLN B CA  1 
ATOM   3246 C C   . GLN A 1 431 ? 34.200  -27.198 -4.405  1.00 13.46 ? 429  GLN B C   1 
ATOM   3247 O O   . GLN A 1 431 ? 33.909  -26.932 -3.259  1.00 14.32 ? 429  GLN B O   1 
ATOM   3248 C CB  . GLN A 1 431 ? 36.172  -26.059 -5.413  1.00 13.91 ? 429  GLN B CB  1 
ATOM   3249 C CG  . GLN A 1 431 ? 36.037  -24.871 -4.469  1.00 15.51 ? 429  GLN B CG  1 
ATOM   3250 C CD  . GLN A 1 431 ? 36.185  -23.519 -5.122  1.00 17.16 ? 429  GLN B CD  1 
ATOM   3251 O OE1 . GLN A 1 431 ? 36.767  -23.382 -6.190  1.00 16.77 ? 429  GLN B OE1 1 
ATOM   3252 N NE2 . GLN A 1 431 ? 35.663  -22.499 -4.462  1.00 17.26 ? 429  GLN B NE2 1 
ATOM   3253 N N   . ASN A 1 432 ? 33.325  -27.356 -5.392  1.00 12.95 ? 430  ASN B N   1 
ATOM   3254 C CA  . ASN A 1 432 ? 31.870  -27.207 -5.111  1.00 13.93 ? 430  ASN B CA  1 
ATOM   3255 C C   . ASN A 1 432 ? 31.462  -28.215 -4.020  1.00 14.04 ? 430  ASN B C   1 
ATOM   3256 O O   . ASN A 1 432 ? 30.734  -27.882 -3.118  1.00 13.67 ? 430  ASN B O   1 
ATOM   3257 C CB  . ASN A 1 432 ? 31.055  -27.406 -6.384  1.00 14.16 ? 430  ASN B CB  1 
ATOM   3258 C CG  . ASN A 1 432 ? 29.583  -27.105 -6.203  1.00 13.36 ? 430  ASN B CG  1 
ATOM   3259 O OD1 . ASN A 1 432 ? 29.215  -26.101 -5.590  1.00 14.00 ? 430  ASN B OD1 1 
ATOM   3260 N ND2 . ASN A 1 432 ? 28.747  -27.984 -6.700  1.00 14.41 ? 430  ASN B ND2 1 
ATOM   3261 N N   . VAL A 1 433 ? 31.954  -29.457 -4.089  1.00 13.66 ? 431  VAL B N   1 
ATOM   3262 C CA  . VAL A 1 433 ? 31.707  -30.461 -3.016  1.00 13.63 ? 431  VAL B CA  1 
ATOM   3263 C C   . VAL A 1 433 ? 32.318  -29.988 -1.682  1.00 12.87 ? 431  VAL B C   1 
ATOM   3264 O O   . VAL A 1 433 ? 31.677  -30.158 -0.643  1.00 13.65 ? 431  VAL B O   1 
ATOM   3265 C CB  . VAL A 1 433 ? 32.261  -31.844 -3.462  1.00 13.97 ? 431  VAL B CB  1 
ATOM   3266 C CG1 . VAL A 1 433 ? 32.143  -32.871 -2.342  1.00 16.28 ? 431  VAL B CG1 1 
ATOM   3267 C CG2 . VAL A 1 433 ? 31.502  -32.360 -4.683  1.00 14.28 ? 431  VAL B CG2 1 
ATOM   3268 N N   . ARG A 1 434 ? 33.571  -29.530 -1.683  1.00 13.53 ? 432  ARG B N   1 
ATOM   3269 C CA  . ARG A 1 434 ? 34.233  -29.165 -0.406  1.00 13.92 ? 432  ARG B CA  1 
ATOM   3270 C C   . ARG A 1 434 ? 33.540  -27.952 0.233   1.00 13.31 ? 432  ARG B C   1 
ATOM   3271 O O   . ARG A 1 434 ? 33.342  -27.955 1.431   1.00 13.43 ? 432  ARG B O   1 
ATOM   3272 C CB  . ARG A 1 434 ? 35.710  -28.891 -0.679  1.00 13.70 ? 432  ARG B CB  1 
ATOM   3273 C CG  . ARG A 1 434 ? 36.533  -30.148 -0.919  1.00 14.15 ? 432  ARG B CG  1 
ATOM   3274 C CD  . ARG A 1 434 ? 38.014  -29.833 -1.007  1.00 14.51 ? 432  ARG B CD  1 
ATOM   3275 N NE  . ARG A 1 434 ? 38.351  -29.165 -2.255  1.00 13.82 ? 432  ARG B NE  1 
ATOM   3276 C CZ  . ARG A 1 434 ? 38.653  -27.878 -2.363  1.00 14.74 ? 432  ARG B CZ  1 
ATOM   3277 N NH1 . ARG A 1 434 ? 38.664  -27.108 -1.289  1.00 14.91 ? 432  ARG B NH1 1 
ATOM   3278 N NH2 . ARG A 1 434 ? 38.945  -27.364 -3.542  1.00 15.01 ? 432  ARG B NH2 1 
ATOM   3279 N N   . ASP A 1 435 ? 33.186  -26.975 -0.588  1.00 14.27 ? 433  ASP B N   1 
ATOM   3280 C CA  . ASP A 1 435 ? 32.457  -25.798 -0.060  1.00 13.49 ? 433  ASP B CA  1 
ATOM   3281 C C   . ASP A 1 435 ? 31.077  -26.228 0.470   1.00 14.40 ? 433  ASP B C   1 
ATOM   3282 O O   . ASP A 1 435 ? 30.622  -25.678 1.473   1.00 14.49 ? 433  ASP B O   1 
ATOM   3283 C CB  . ASP A 1 435 ? 32.351  -24.731 -1.151  1.00 13.75 ? 433  ASP B CB  1 
ATOM   3284 C CG  . ASP A 1 435 ? 33.648  -24.022 -1.498  1.00 15.12 ? 433  ASP B CG  1 
ATOM   3285 O OD1 . ASP A 1 435 ? 34.647  -24.246 -0.806  1.00 16.36 ? 433  ASP B OD1 1 
ATOM   3286 O OD2 . ASP A 1 435 ? 33.631  -23.244 -2.456  1.00 15.98 ? 433  ASP B OD2 1 
ATOM   3287 N N   . SER A 1 436 ? 30.442  -27.193 -0.184  1.00 13.32 ? 434  SER B N   1 
ATOM   3288 C CA  . SER A 1 436 ? 29.105  -27.668 0.245   1.00 12.27 ? 434  SER B CA  1 
ATOM   3289 C C   . SER A 1 436 ? 29.136  -28.376 1.604   1.00 13.19 ? 434  SER B C   1 
ATOM   3290 O O   . SER A 1 436 ? 28.168  -28.271 2.331   1.00 12.62 ? 434  SER B O   1 
ATOM   3291 C CB  . SER A 1 436 ? 28.523  -28.595 -0.808  1.00 12.98 ? 434  SER B CB  1 
ATOM   3292 O OG  . SER A 1 436 ? 27.318  -29.194 -0.372  1.00 13.55 ? 434  SER B OG  1 
ATOM   3293 N N   . ARG A 1 437 ? 30.236  -29.048 1.932   1.00 13.21 ? 435  ARG B N   1 
ATOM   3294 C CA  . ARG A 1 437 ? 30.195  -29.921 3.137   1.00 13.45 ? 435  ARG B CA  1 
ATOM   3295 C C   . ARG A 1 437 ? 29.922  -29.113 4.423   1.00 15.03 ? 435  ARG B C   1 
ATOM   3296 O O   . ARG A 1 437 ? 29.263  -29.653 5.322   1.00 13.43 ? 435  ARG B O   1 
ATOM   3297 C CB  . ARG A 1 437 ? 31.467  -30.751 3.258   1.00 14.54 ? 435  ARG B CB  1 
ATOM   3298 C CG  . ARG A 1 437 ? 31.381  -31.777 4.391   1.00 14.12 ? 435  ARG B CG  1 
ATOM   3299 C CD  . ARG A 1 437 ? 30.361  -32.829 4.131   1.00 14.12 ? 435  ARG B CD  1 
ATOM   3300 N NE  . ARG A 1 437 ? 30.112  -33.720 5.238   1.00 13.77 ? 435  ARG B NE  1 
ATOM   3301 C CZ  . ARG A 1 437 ? 29.310  -33.480 6.257   1.00 14.27 ? 435  ARG B CZ  1 
ATOM   3302 N NH1 . ARG A 1 437 ? 28.750  -32.295 6.380   1.00 13.81 ? 435  ARG B NH1 1 
ATOM   3303 N NH2 . ARG A 1 437 ? 29.032  -34.447 7.131   1.00 14.10 ? 435  ARG B NH2 1 
ATOM   3304 N N   . ILE A 1 438 ? 30.382  -27.879 4.525   1.00 14.78 ? 436  ILE B N   1 
ATOM   3305 C CA  . ILE A 1 438 ? 30.171  -27.090 5.768   1.00 15.24 ? 436  ILE B CA  1 
ATOM   3306 C C   . ILE A 1 438 ? 28.673  -26.773 5.904   1.00 13.78 ? 436  ILE B C   1 
ATOM   3307 O O   . ILE A 1 438 ? 28.223  -26.528 7.036   1.00 12.87 ? 436  ILE B O   1 
ATOM   3308 C CB  . ILE A 1 438 ? 31.010  -25.786 5.766   1.00 15.11 ? 436  ILE B CB  1 
ATOM   3309 C CG1 . ILE A 1 438 ? 30.918  -25.025 7.092   1.00 15.64 ? 436  ILE B CG1 1 
ATOM   3310 C CG2 . ILE A 1 438 ? 30.597  -24.860 4.653   1.00 16.84 ? 436  ILE B CG2 1 
ATOM   3311 C CD1 . ILE A 1 438 ? 31.297  -25.783 8.320   1.00 17.44 ? 436  ILE B CD1 1 
ATOM   3312 N N   . SER A 1 439 ? 27.931  -26.734 4.794   1.00 13.66 ? 437  SER B N   1 
ATOM   3313 C CA  . SER A 1 439 ? 26.511  -26.276 4.810   1.00 13.22 ? 437  SER B CA  1 
ATOM   3314 C C   . SER A 1 439 ? 25.608  -27.130 5.723   1.00 14.57 ? 437  SER B C   1 
ATOM   3315 O O   . SER A 1 439 ? 24.609  -26.610 6.193   1.00 15.15 ? 437  SER B O   1 
ATOM   3316 C CB  . SER A 1 439 ? 25.978  -26.179 3.384   1.00 13.19 ? 437  SER B CB  1 
ATOM   3317 O OG  . SER A 1 439 ? 25.727  -27.448 2.814   1.00 13.33 ? 437  SER B OG  1 
ATOM   3318 N N   . MET A 1 440 ? 25.983  -28.391 5.943   1.00 13.08 ? 438  MET B N   1 
ATOM   3319 C CA  A MET A 1 440 ? 25.153  -29.269 6.812   0.50 13.10 ? 438  MET B CA  1 
ATOM   3320 C CA  B MET A 1 440 ? 25.178  -29.299 6.796   0.50 14.70 ? 438  MET B CA  1 
ATOM   3321 C C   . MET A 1 440 ? 25.631  -29.204 8.266   1.00 13.09 ? 438  MET B C   1 
ATOM   3322 O O   . MET A 1 440 ? 25.008  -29.880 9.110   1.00 15.25 ? 438  MET B O   1 
ATOM   3323 C CB  A MET A 1 440 ? 25.206  -30.731 6.343   0.50 12.80 ? 438  MET B CB  1 
ATOM   3324 C CB  B MET A 1 440 ? 25.328  -30.738 6.271   0.50 16.64 ? 438  MET B CB  1 
ATOM   3325 C CG  A MET A 1 440 ? 24.613  -30.933 4.974   0.50 13.08 ? 438  MET B CG  1 
ATOM   3326 C CG  B MET A 1 440 ? 24.761  -30.928 4.860   0.50 19.28 ? 438  MET B CG  1 
ATOM   3327 S SD  A MET A 1 440 ? 25.842  -30.779 3.699   0.50 13.04 ? 438  MET B SD  1 
ATOM   3328 S SD  B MET A 1 440 ? 25.575  -32.228 3.883   0.50 24.48 ? 438  MET B SD  1 
ATOM   3329 C CE  A MET A 1 440 ? 26.508  -32.432 3.622   0.50 11.53 ? 438  MET B CE  1 
ATOM   3330 C CE  B MET A 1 440 ? 26.943  -31.260 3.284   0.50 24.84 ? 438  MET B CE  1 
ATOM   3331 N N   . LEU A 1 441 ? 26.719  -28.476 8.517   1.00 14.08 ? 439  LEU B N   1 
ATOM   3332 C CA  . LEU A 1 441 ? 27.354  -28.408 9.858   1.00 15.04 ? 439  LEU B CA  1 
ATOM   3333 C C   . LEU A 1 441 ? 27.061  -27.059 10.526  1.00 15.55 ? 439  LEU B C   1 
ATOM   3334 O O   . LEU A 1 441 ? 26.647  -27.070 11.682  1.00 19.77 ? 439  LEU B O   1 
ATOM   3335 C CB  . LEU A 1 441 ? 28.866  -28.603 9.702   1.00 15.46 ? 439  LEU B CB  1 
ATOM   3336 C CG  . LEU A 1 441 ? 29.301  -29.899 9.024   1.00 15.95 ? 439  LEU B CG  1 
ATOM   3337 C CD1 . LEU A 1 441 ? 30.802  -29.903 8.790   1.00 17.21 ? 439  LEU B CD1 1 
ATOM   3338 C CD2 . LEU A 1 441 ? 28.891  -31.105 9.853   1.00 16.87 ? 439  LEU B CD2 1 
ATOM   3339 N N   . TYR A 1 442 ? 27.278  -25.965 9.814   1.00 15.62 ? 440  TYR B N   1 
ATOM   3340 C CA  . TYR A 1 442 ? 27.081  -24.644 10.454  1.00 15.39 ? 440  TYR B CA  1 
ATOM   3341 C C   . TYR A 1 442 ? 25.627  -24.165 10.326  1.00 16.28 ? 440  TYR B C   1 
ATOM   3342 O O   . TYR A 1 442 ? 24.845  -24.801 9.638   1.00 16.13 ? 440  TYR B O   1 
ATOM   3343 C CB  . TYR A 1 442 ? 28.153  -23.628 10.017  1.00 15.48 ? 440  TYR B CB  1 
ATOM   3344 C CG  . TYR A 1 442 ? 28.149  -23.108 8.602   1.00 13.93 ? 440  TYR B CG  1 
ATOM   3345 C CD1 . TYR A 1 442 ? 27.161  -23.421 7.683   1.00 14.82 ? 440  TYR B CD1 1 
ATOM   3346 C CD2 . TYR A 1 442 ? 29.163  -22.262 8.193   1.00 14.60 ? 440  TYR B CD2 1 
ATOM   3347 C CE1 . TYR A 1 442 ? 27.195  -22.916 6.394   1.00 15.10 ? 440  TYR B CE1 1 
ATOM   3348 C CE2 . TYR A 1 442 ? 29.214  -21.753 6.911   1.00 14.79 ? 440  TYR B CE2 1 
ATOM   3349 C CZ  . TYR A 1 442 ? 28.224  -22.076 6.008   1.00 14.61 ? 440  TYR B CZ  1 
ATOM   3350 O OH  . TYR A 1 442 ? 28.297  -21.558 4.750   1.00 16.38 ? 440  TYR B OH  1 
ATOM   3351 N N   . ALA A 1 443 ? 25.308  -23.080 11.041  1.00 16.86 ? 441  ALA B N   1 
ATOM   3352 C CA  . ALA A 1 443 ? 23.941  -22.497 11.046  1.00 18.06 ? 441  ALA B CA  1 
ATOM   3353 C C   . ALA A 1 443 ? 22.929  -23.512 11.588  1.00 15.96 ? 441  ALA B C   1 
ATOM   3354 O O   . ALA A 1 443 ? 21.770  -23.445 11.212  1.00 17.61 ? 441  ALA B O   1 
ATOM   3355 C CB  . ALA A 1 443 ? 23.580  -21.980 9.674   1.00 17.47 ? 441  ALA B CB  1 
ATOM   3356 N N   . GLY A 1 444 ? 23.393  -24.386 12.479  1.00 15.14 ? 442  GLY B N   1 
ATOM   3357 C CA  . GLY A 1 444 ? 22.513  -25.433 13.022  1.00 16.59 ? 442  GLY B CA  1 
ATOM   3358 C C   . GLY A 1 444 ? 22.626  -26.694 12.193  1.00 16.40 ? 442  GLY B C   1 
ATOM   3359 O O   . GLY A 1 444 ? 22.163  -26.698 11.062  1.00 16.59 ? 442  GLY B O   1 
ATOM   3360 N N   . THR A 1 445 ? 23.218  -27.720 12.774  1.00 15.17 ? 443  THR B N   1 
ATOM   3361 C CA  . THR A 1 445 ? 23.429  -28.962 12.017  1.00 15.42 ? 443  THR B CA  1 
ATOM   3362 C C   . THR A 1 445 ? 22.120  -29.527 11.485  1.00 14.85 ? 443  THR B C   1 
ATOM   3363 O O   . THR A 1 445 ? 21.076  -29.165 11.983  1.00 15.15 ? 443  THR B O   1 
ATOM   3364 C CB  . THR A 1 445 ? 24.029  -30.050 12.917  1.00 16.17 ? 443  THR B CB  1 
ATOM   3365 O OG1 . THR A 1 445 ? 23.061  -30.424 13.895  1.00 16.14 ? 443  THR B OG1 1 
ATOM   3366 C CG2 . THR A 1 445 ? 25.312  -29.602 13.584  1.00 17.83 ? 443  THR B CG2 1 
ATOM   3367 N N   . THR A 1 446 ? 22.227  -30.382 10.475  1.00 13.92 ? 444  THR B N   1 
ATOM   3368 C CA  . THR A 1 446 ? 21.026  -31.121 10.030  1.00 14.77 ? 444  THR B CA  1 
ATOM   3369 C C   . THR A 1 446 ? 20.245  -31.654 11.231  1.00 14.43 ? 444  THR B C   1 
ATOM   3370 O O   . THR A 1 446 ? 19.003  -31.530 11.236  1.00 14.83 ? 444  THR B O   1 
ATOM   3371 C CB  . THR A 1 446 ? 21.420  -32.256 9.074   1.00 14.21 ? 444  THR B CB  1 
ATOM   3372 O OG1 . THR A 1 446 ? 22.046  -31.648 7.950   1.00 14.72 ? 444  THR B OG1 1 
ATOM   3373 C CG2 . THR A 1 446 ? 20.265  -33.115 8.615   1.00 14.43 ? 444  THR B CG2 1 
ATOM   3374 N N   . GLY A 1 447 ? 20.901  -32.305 12.208  1.00 14.81 ? 445  GLY B N   1 
ATOM   3375 C CA  . GLY A 1 447 ? 20.167  -32.882 13.342  1.00 15.30 ? 445  GLY B CA  1 
ATOM   3376 C C   . GLY A 1 447 ? 19.452  -31.820 14.187  1.00 15.03 ? 445  GLY B C   1 
ATOM   3377 O O   . GLY A 1 447 ? 18.361  -32.081 14.654  1.00 16.64 ? 445  GLY B O   1 
ATOM   3378 N N   . VAL A 1 448 ? 20.070  -30.668 14.362  1.00 14.66 ? 446  VAL B N   1 
ATOM   3379 C CA  . VAL A 1 448 ? 19.429  -29.548 15.111  1.00 15.55 ? 446  VAL B CA  1 
ATOM   3380 C C   . VAL A 1 448 ? 18.208  -29.045 14.320  1.00 15.34 ? 446  VAL B C   1 
ATOM   3381 O O   . VAL A 1 448 ? 17.168  -28.836 14.927  1.00 16.02 ? 446  VAL B O   1 
ATOM   3382 C CB  . VAL A 1 448 ? 20.464  -28.437 15.368  1.00 17.91 ? 446  VAL B CB  1 
ATOM   3383 C CG1 . VAL A 1 448 ? 19.821  -27.106 15.719  1.00 19.96 ? 446  VAL B CG1 1 
ATOM   3384 C CG2 . VAL A 1 448 ? 21.479  -28.840 16.423  1.00 19.65 ? 446  VAL B CG2 1 
ATOM   3385 N N   . GLN A 1 449 ? 18.353  -28.908 13.001  1.00 15.38 ? 447  GLN B N   1 
ATOM   3386 C CA  . GLN A 1 449 ? 17.204  -28.458 12.179  1.00 15.16 ? 447  GLN B CA  1 
ATOM   3387 C C   . GLN A 1 449 ? 16.069  -29.461 12.387  1.00 14.64 ? 447  GLN B C   1 
ATOM   3388 O O   . GLN A 1 449 ? 14.859  -29.065 12.427  1.00 14.99 ? 447  GLN B O   1 
ATOM   3389 C CB  . GLN A 1 449 ? 17.531  -28.289 10.696  1.00 15.65 ? 447  GLN B CB  1 
ATOM   3390 C CG  . GLN A 1 449 ? 18.702  -27.368 10.368  1.00 16.13 ? 447  GLN B CG  1 
ATOM   3391 C CD  . GLN A 1 449 ? 18.489  -25.953 10.862  1.00 16.04 ? 447  GLN B CD  1 
ATOM   3392 O OE1 . GLN A 1 449 ? 17.351  -25.513 10.959  1.00 17.21 ? 447  GLN B OE1 1 
ATOM   3393 N NE2 . GLN A 1 449 ? 19.567  -25.272 11.168  1.00 17.16 ? 447  GLN B NE2 1 
ATOM   3394 N N   . ALA A 1 450 ? 16.417  -30.759 12.364  1.00 14.83 ? 448  ALA B N   1 
ATOM   3395 C CA  . ALA A 1 450 ? 15.393  -31.811 12.416  1.00 14.66 ? 448  ALA B CA  1 
ATOM   3396 C C   . ALA A 1 450 ? 14.641  -31.757 13.767  1.00 15.08 ? 448  ALA B C   1 
ATOM   3397 O O   . ALA A 1 450 ? 13.405  -31.965 13.796  1.00 15.41 ? 448  ALA B O   1 
ATOM   3398 C CB  . ALA A 1 450 ? 16.039  -33.148 12.169  1.00 15.18 ? 448  ALA B CB  1 
ATOM   3399 N N   . LEU A 1 451 ? 15.374  -31.556 14.854  1.00 16.28 ? 449  LEU B N   1 
ATOM   3400 C CA  . LEU A 1 451 ? 14.748  -31.417 16.191  1.00 17.23 ? 449  LEU B CA  1 
ATOM   3401 C C   . LEU A 1 451 ? 13.877  -30.167 16.216  1.00 18.23 ? 449  LEU B C   1 
ATOM   3402 O O   . LEU A 1 451 ? 12.751  -30.212 16.777  1.00 18.34 ? 449  LEU B O   1 
ATOM   3403 C CB  . LEU A 1 451 ? 15.838  -31.321 17.245  1.00 19.01 ? 449  LEU B CB  1 
ATOM   3404 C CG  . LEU A 1 451 ? 16.442  -32.650 17.663  1.00 22.07 ? 449  LEU B CG  1 
ATOM   3405 C CD1 . LEU A 1 451 ? 17.482  -32.384 18.736  1.00 25.89 ? 449  LEU B CD1 1 
ATOM   3406 C CD2 . LEU A 1 451 ? 15.369  -33.614 18.170  1.00 22.93 ? 449  LEU B CD2 1 
ATOM   3407 N N   . ASP A 1 452 ? 14.326  -29.085 15.601  1.00 17.20 ? 450  ASP B N   1 
ATOM   3408 C CA  . ASP A 1 452 ? 13.525  -27.841 15.548  1.00 17.96 ? 450  ASP B CA  1 
ATOM   3409 C C   . ASP A 1 452 ? 12.214  -28.110 14.800  1.00 18.23 ? 450  ASP B C   1 
ATOM   3410 O O   . ASP A 1 452 ? 11.146  -27.747 15.313  1.00 18.21 ? 450  ASP B O   1 
ATOM   3411 C CB  . ASP A 1 452 ? 14.321  -26.715 14.910  1.00 16.58 ? 450  ASP B CB  1 
ATOM   3412 C CG  . ASP A 1 452 ? 13.540  -25.422 14.830  1.00 18.98 ? 450  ASP B CG  1 
ATOM   3413 O OD1 . ASP A 1 452 ? 13.131  -24.933 15.908  1.00 20.18 ? 450  ASP B OD1 1 
ATOM   3414 O OD2 . ASP A 1 452 ? 13.297  -24.965 13.695  1.00 19.23 ? 450  ASP B OD2 1 
ATOM   3415 N N   . LEU A 1 453 ? 12.273  -28.726 13.624  1.00 17.45 ? 451  LEU B N   1 
ATOM   3416 C CA  . LEU A 1 453 ? 11.065  -28.998 12.834  1.00 16.74 ? 451  LEU B CA  1 
ATOM   3417 C C   . LEU A 1 453 ? 10.124  -29.915 13.627  1.00 17.58 ? 451  LEU B C   1 
ATOM   3418 O O   . LEU A 1 453 ? 8.933   -29.550 13.793  1.00 17.40 ? 451  LEU B O   1 
ATOM   3419 C CB  . LEU A 1 453 ? 11.423  -29.655 11.500  1.00 17.11 ? 451  LEU B CB  1 
ATOM   3420 C CG  . LEU A 1 453 ? 10.220  -30.126 10.704  1.00 16.81 ? 451  LEU B CG  1 
ATOM   3421 C CD1 . LEU A 1 453 ? 9.370   -28.918 10.278  1.00 17.17 ? 451  LEU B CD1 1 
ATOM   3422 C CD2 . LEU A 1 453 ? 10.673  -30.964 9.500   1.00 16.30 ? 451  LEU B CD2 1 
ATOM   3423 N N   . LEU A 1 454 ? 10.582  -31.101 14.006  1.00 17.87 ? 452  LEU B N   1 
ATOM   3424 C CA  . LEU A 1 454 ? 9.652   -32.107 14.558  1.00 18.12 ? 452  LEU B CA  1 
ATOM   3425 C C   . LEU A 1 454 ? 9.239   -31.679 15.975  1.00 19.06 ? 452  LEU B C   1 
ATOM   3426 O O   . LEU A 1 454 ? 8.008   -31.726 16.240  1.00 19.69 ? 452  LEU B O   1 
ATOM   3427 C CB  . LEU A 1 454 ? 10.263  -33.506 14.536  1.00 17.79 ? 452  LEU B CB  1 
ATOM   3428 C CG  . LEU A 1 454 ? 9.376   -34.625 15.098  1.00 18.58 ? 452  LEU B CG  1 
ATOM   3429 C CD1 . LEU A 1 454 ? 8.086   -34.748 14.293  1.00 19.43 ? 452  LEU B CD1 1 
ATOM   3430 C CD2 . LEU A 1 454 ? 10.140  -35.938 15.079  1.00 18.05 ? 452  LEU B CD2 1 
ATOM   3431 N N   . GLY A 1 455 ? 10.176  -31.293 16.840  1.00 18.65 ? 453  GLY B N   1 
ATOM   3432 C CA  . GLY A 1 455 ? 9.850   -30.962 18.254  1.00 20.88 ? 453  GLY B CA  1 
ATOM   3433 C C   . GLY A 1 455 ? 9.110   -29.633 18.350  1.00 22.18 ? 453  GLY B C   1 
ATOM   3434 O O   . GLY A 1 455 ? 7.908   -29.593 18.716  1.00 23.67 ? 453  GLY B O   1 
ATOM   3435 N N   . ARG A 1 456 ? 9.753   -28.572 17.917  1.00 22.13 ? 454  ARG B N   1 
ATOM   3436 C CA  . ARG A 1 456 ? 9.301   -27.197 18.208  1.00 23.22 ? 454  ARG B CA  1 
ATOM   3437 C C   . ARG A 1 456 ? 8.223   -26.781 17.201  1.00 23.89 ? 454  ARG B C   1 
ATOM   3438 O O   . ARG A 1 456 ? 7.218   -26.171 17.617  1.00 25.93 ? 454  ARG B O   1 
ATOM   3439 C CB  . ARG A 1 456 ? 10.494  -26.239 18.239  1.00 24.96 ? 454  ARG B CB  1 
ATOM   3440 C CG  . ARG A 1 456 ? 10.111  -24.824 18.659  1.00 30.31 ? 454  ARG B CG  1 
ATOM   3441 C CD  . ARG A 1 456 ? 11.276  -23.872 18.746  1.00 33.98 ? 454  ARG B CD  1 
ATOM   3442 N NE  . ARG A 1 456 ? 10.813  -22.503 18.983  1.00 43.57 ? 454  ARG B NE  1 
ATOM   3443 C CZ  . ARG A 1 456 ? 10.461  -22.002 20.175  1.00 42.46 ? 454  ARG B CZ  1 
ATOM   3444 N NH1 . ARG A 1 456 ? 10.514  -22.747 21.265  1.00 39.65 ? 454  ARG B NH1 1 
ATOM   3445 N NH2 . ARG A 1 456 ? 10.067  -20.740 20.259  1.00 44.46 ? 454  ARG B NH2 1 
ATOM   3446 N N   . LYS A 1 457 ? 8.404   -27.037 15.918  1.00 20.48 ? 455  LYS B N   1 
ATOM   3447 C CA  . LYS A 1 457 ? 7.506   -26.472 14.887  1.00 20.87 ? 455  LYS B CA  1 
ATOM   3448 C C   . LYS A 1 457 ? 6.266   -27.344 14.689  1.00 22.43 ? 455  LYS B C   1 
ATOM   3449 O O   . LYS A 1 457 ? 5.178   -26.753 14.520  1.00 25.96 ? 455  LYS B O   1 
ATOM   3450 C CB  . LYS A 1 457 ? 8.228   -26.232 13.559  1.00 21.93 ? 455  LYS B CB  1 
ATOM   3451 C CG  . LYS A 1 457 ? 9.443   -25.322 13.644  1.00 21.43 ? 455  LYS B CG  1 
ATOM   3452 C CD  . LYS A 1 457 ? 9.211   -23.972 14.291  1.00 21.59 ? 455  LYS B CD  1 
ATOM   3453 C CE  . LYS A 1 457 ? 10.464  -23.159 14.545  1.00 20.43 ? 455  LYS B CE  1 
ATOM   3454 N NZ  . LYS A 1 457 ? 11.271  -22.943 13.312  1.00 20.31 ? 455  LYS B NZ  1 
ATOM   3455 N N   . VAL A 1 458 ? 6.380   -28.665 14.698  1.00 18.49 ? 456  VAL B N   1 
ATOM   3456 C CA  . VAL A 1 458 ? 5.243   -29.547 14.379  1.00 19.05 ? 456  VAL B CA  1 
ATOM   3457 C C   . VAL A 1 458 ? 4.602   -30.060 15.672  1.00 20.50 ? 456  VAL B C   1 
ATOM   3458 O O   . VAL A 1 458 ? 3.425   -29.739 15.893  1.00 20.49 ? 456  VAL B O   1 
ATOM   3459 C CB  . VAL A 1 458 ? 5.690   -30.677 13.441  1.00 19.16 ? 456  VAL B CB  1 
ATOM   3460 C CG1 . VAL A 1 458 ? 4.618   -31.713 13.257  1.00 19.51 ? 456  VAL B CG1 1 
ATOM   3461 C CG2 . VAL A 1 458 ? 6.181   -30.103 12.122  1.00 18.90 ? 456  VAL B CG2 1 
ATOM   3462 N N   . LEU A 1 459 ? 5.312   -30.822 16.505  1.00 20.47 ? 457  LEU B N   1 
ATOM   3463 C CA  . LEU A 1 459 ? 4.639   -31.489 17.659  1.00 21.40 ? 457  LEU B CA  1 
ATOM   3464 C C   . LEU A 1 459 ? 4.161   -30.418 18.658  1.00 24.14 ? 457  LEU B C   1 
ATOM   3465 O O   . LEU A 1 459 ? 2.988   -30.533 19.067  1.00 24.60 ? 457  LEU B O   1 
ATOM   3466 C CB  . LEU A 1 459 ? 5.586   -32.505 18.308  1.00 22.54 ? 457  LEU B CB  1 
ATOM   3467 C CG  . LEU A 1 459 ? 5.855   -33.734 17.453  1.00 20.38 ? 457  LEU B CG  1 
ATOM   3468 C CD1 . LEU A 1 459 ? 6.719   -34.722 18.201  1.00 22.27 ? 457  LEU B CD1 1 
ATOM   3469 C CD2 . LEU A 1 459 ? 4.569   -34.386 16.970  1.00 20.36 ? 457  LEU B CD2 1 
ATOM   3470 N N   . MET A 1 460 ? 4.950   -29.380 18.926  1.00 24.34 ? 458  MET B N   1 
ATOM   3471 C CA  A MET A 1 460 ? 4.601   -28.359 19.961  0.50 28.51 ? 458  MET B CA  1 
ATOM   3472 C CA  B MET A 1 460 ? 4.629   -28.334 19.948  0.50 27.71 ? 458  MET B CA  1 
ATOM   3473 C C   . MET A 1 460 ? 3.554   -27.363 19.431  1.00 27.49 ? 458  MET B C   1 
ATOM   3474 O O   . MET A 1 460 ? 3.062   -26.579 20.228  1.00 28.29 ? 458  MET B O   1 
ATOM   3475 C CB  A MET A 1 460 ? 5.840   -27.607 20.456  0.50 30.65 ? 458  MET B CB  1 
ATOM   3476 C CB  B MET A 1 460 ? 5.877   -27.545 20.363  0.50 28.77 ? 458  MET B CB  1 
ATOM   3477 C CG  A MET A 1 460 ? 6.690   -28.422 21.435  0.50 35.71 ? 458  MET B CG  1 
ATOM   3478 C CG  B MET A 1 460 ? 6.760   -28.308 21.344  0.50 32.60 ? 458  MET B CG  1 
ATOM   3479 S SD  A MET A 1 460 ? 5.731   -29.251 22.750  0.50 39.50 ? 458  MET B SD  1 
ATOM   3480 S SD  B MET A 1 460 ? 8.150   -27.352 22.020  0.50 34.96 ? 458  MET B SD  1 
ATOM   3481 C CE  A MET A 1 460 ? 5.881   -30.962 22.243  0.50 39.31 ? 458  MET B CE  1 
ATOM   3482 C CE  B MET A 1 460 ? 7.501   -25.679 21.962  0.50 32.27 ? 458  MET B CE  1 
ATOM   3483 N N   . THR A 1 461 ? 3.191   -27.394 18.150  1.00 25.88 ? 459  THR B N   1 
ATOM   3484 C CA  . THR A 1 461 ? 2.063   -26.552 17.643  1.00 26.85 ? 459  THR B CA  1 
ATOM   3485 C C   . THR A 1 461 ? 0.852   -27.430 17.366  1.00 26.82 ? 459  THR B C   1 
ATOM   3486 O O   . THR A 1 461 ? -0.073  -26.934 16.725  1.00 27.45 ? 459  THR B O   1 
ATOM   3487 C CB  . THR A 1 461 ? 2.397   -25.737 16.387  1.00 25.10 ? 459  THR B CB  1 
ATOM   3488 O OG1 . THR A 1 461 ? 2.570   -26.603 15.249  1.00 24.33 ? 459  THR B OG1 1 
ATOM   3489 C CG2 . THR A 1 461 ? 3.585   -24.833 16.610  1.00 26.35 ? 459  THR B CG2 1 
ATOM   3490 N N   . GLN A 1 462 ? 0.867   -28.687 17.810  1.00 27.03 ? 460  GLN B N   1 
ATOM   3491 C CA  . GLN A 1 462 ? -0.201  -29.678 17.524  1.00 31.90 ? 460  GLN B CA  1 
ATOM   3492 C C   . GLN A 1 462 ? -0.344  -29.862 16.011  1.00 31.59 ? 460  GLN B C   1 
ATOM   3493 O O   . GLN A 1 462 ? -1.487  -30.166 15.558  1.00 30.49 ? 460  GLN B O   1 
ATOM   3494 C CB  . GLN A 1 462 ? -1.533  -29.195 18.099  1.00 36.11 ? 460  GLN B CB  1 
ATOM   3495 C CG  . GLN A 1 462 ? -2.223  -30.215 18.988  1.00 45.64 ? 460  GLN B CG  1 
ATOM   3496 C CD  . GLN A 1 462 ? -1.907  -29.977 20.439  1.00 48.41 ? 460  GLN B CD  1 
ATOM   3497 O OE1 . GLN A 1 462 ? -2.487  -30.597 21.320  1.00 57.17 ? 460  GLN B OE1 1 
ATOM   3498 N NE2 . GLN A 1 462 ? -1.000  -29.047 20.690  1.00 58.86 ? 460  GLN B NE2 1 
ATOM   3499 N N   . GLY A 1 463 ? 0.747   -29.686 15.255  1.00 29.01 ? 461  GLY B N   1 
ATOM   3500 C CA  . GLY A 1 463 ? 0.755   -29.842 13.788  1.00 30.83 ? 461  GLY B CA  1 
ATOM   3501 C C   . GLY A 1 463 ? 0.134   -28.679 13.035  1.00 28.73 ? 461  GLY B C   1 
ATOM   3502 O O   . GLY A 1 463 ? -0.047  -28.821 11.823  1.00 28.80 ? 461  GLY B O   1 
ATOM   3503 N N   . GLU A 1 464 ? -0.212  -27.577 13.706  1.00 29.89 ? 462  GLU B N   1 
ATOM   3504 C CA  . GLU A 1 464 ? -0.876  -26.425 13.043  1.00 33.39 ? 462  GLU B CA  1 
ATOM   3505 C C   . GLU A 1 464 ? 0.052   -25.896 11.948  1.00 30.42 ? 462  GLU B C   1 
ATOM   3506 O O   . GLU A 1 464 ? -0.437  -25.525 10.867  1.00 27.25 ? 462  GLU B O   1 
ATOM   3507 C CB  . GLU A 1 464 ? -1.228  -25.322 14.041  1.00 37.08 ? 462  GLU B CB  1 
ATOM   3508 C CG  . GLU A 1 464 ? -2.293  -25.720 15.064  1.00 47.11 ? 462  GLU B CG  1 
ATOM   3509 C CD  . GLU A 1 464 ? -3.526  -26.495 14.604  1.00 52.46 ? 462  GLU B CD  1 
ATOM   3510 O OE1 . GLU A 1 464 ? -3.917  -27.423 15.348  1.00 59.64 ? 462  GLU B OE1 1 
ATOM   3511 O OE2 . GLU A 1 464 ? -4.123  -26.160 13.533  1.00 51.23 ? 462  GLU B OE2 1 
ATOM   3512 N N   . ALA A 1 465 ? 1.362   -25.910 12.189  1.00 30.00 ? 463  ALA B N   1 
ATOM   3513 C CA  . ALA A 1 465 ? 2.343   -25.398 11.221  1.00 31.12 ? 463  ALA B CA  1 
ATOM   3514 C C   . ALA A 1 465 ? 2.328   -26.318 9.972   1.00 28.76 ? 463  ALA B C   1 
ATOM   3515 O O   . ALA A 1 465 ? 2.152   -25.827 8.830   1.00 31.58 ? 463  ALA B O   1 
ATOM   3516 C CB  . ALA A 1 465 ? 3.686   -25.290 11.931  1.00 32.53 ? 463  ALA B CB  1 
ATOM   3517 N N   . LEU A 1 466 ? 2.318   -27.625 10.180  1.00 24.05 ? 464  LEU B N   1 
ATOM   3518 C CA  . LEU A 1 466 ? 2.203   -28.602 9.072   1.00 21.73 ? 464  LEU B CA  1 
ATOM   3519 C C   . LEU A 1 466 ? 0.870   -28.446 8.334   1.00 22.20 ? 464  LEU B C   1 
ATOM   3520 O O   . LEU A 1 466 ? 0.848   -28.573 7.100   1.00 21.50 ? 464  LEU B O   1 
ATOM   3521 C CB  . LEU A 1 466 ? 2.334   -30.008 9.643   1.00 18.66 ? 464  LEU B CB  1 
ATOM   3522 C CG  . LEU A 1 466 ? 2.066   -31.134 8.662   1.00 18.18 ? 464  LEU B CG  1 
ATOM   3523 C CD1 . LEU A 1 466 ? 3.106   -31.161 7.533   1.00 17.73 ? 464  LEU B CD1 1 
ATOM   3524 C CD2 . LEU A 1 466 ? 1.988   -32.471 9.411   1.00 20.19 ? 464  LEU B CD2 1 
ATOM   3525 N N   . LYS A 1 467 ? -0.230  -28.257 9.074   1.00 22.69 ? 465  LYS B N   1 
ATOM   3526 C CA  . LYS A 1 467 ? -1.595  -28.206 8.505   1.00 24.77 ? 465  LYS B CA  1 
ATOM   3527 C C   . LYS A 1 467 ? -1.699  -27.040 7.509   1.00 21.63 ? 465  LYS B C   1 
ATOM   3528 O O   . LYS A 1 467 ? -2.463  -27.214 6.548   1.00 22.16 ? 465  LYS B O   1 
ATOM   3529 C CB  . LYS A 1 467 ? -2.643  -28.073 9.620   1.00 29.92 ? 465  LYS B CB  1 
ATOM   3530 C CG  . LYS A 1 467 ? -3.848  -28.992 9.503   1.00 43.38 ? 465  LYS B CG  1 
ATOM   3531 C CD  . LYS A 1 467 ? -4.440  -29.382 10.854  1.00 48.76 ? 465  LYS B CD  1 
ATOM   3532 C CE  . LYS A 1 467 ? -5.895  -29.810 10.772  1.00 58.06 ? 465  LYS B CE  1 
ATOM   3533 N NZ  . LYS A 1 467 ? -6.039  -31.283 10.668  1.00 62.57 ? 465  LYS B NZ  1 
ATOM   3534 N N   . GLY A 1 468 ? -0.988  -25.922 7.760   1.00 21.50 ? 466  GLY B N   1 
ATOM   3535 C CA  . GLY A 1 468 ? -0.876  -24.761 6.856   1.00 22.24 ? 466  GLY B CA  1 
ATOM   3536 C C   . GLY A 1 468 ? -0.462  -25.196 5.453   1.00 24.49 ? 466  GLY B C   1 
ATOM   3537 O O   . GLY A 1 468 ? -1.124  -24.845 4.457   1.00 25.57 ? 466  GLY B O   1 
ATOM   3538 N N   . PHE A 1 469 ? 0.536   -26.071 5.386   1.00 21.70 ? 467  PHE B N   1 
ATOM   3539 C CA  . PHE A 1 469 ? 1.066   -26.555 4.102   1.00 19.29 ? 467  PHE B CA  1 
ATOM   3540 C C   . PHE A 1 469 ? 0.196   -27.690 3.541   1.00 19.68 ? 467  PHE B C   1 
ATOM   3541 O O   . PHE A 1 469 ? -0.093  -27.734 2.314   1.00 18.28 ? 467  PHE B O   1 
ATOM   3542 C CB  . PHE A 1 469 ? 2.538   -26.913 4.297   1.00 19.37 ? 467  PHE B CB  1 
ATOM   3543 C CG  . PHE A 1 469 ? 3.232   -27.080 2.980   1.00 16.89 ? 467  PHE B CG  1 
ATOM   3544 C CD1 . PHE A 1 469 ? 3.866   -26.015 2.362   1.00 19.40 ? 467  PHE B CD1 1 
ATOM   3545 C CD2 . PHE A 1 469 ? 3.292   -28.313 2.383   1.00 16.22 ? 467  PHE B CD2 1 
ATOM   3546 C CE1 . PHE A 1 469 ? 4.502   -26.201 1.145   1.00 18.25 ? 467  PHE B CE1 1 
ATOM   3547 C CE2 . PHE A 1 469 ? 3.884   -28.489 1.144   1.00 16.09 ? 467  PHE B CE2 1 
ATOM   3548 C CZ  . PHE A 1 469 ? 4.527   -27.443 0.552   1.00 16.42 ? 467  PHE B CZ  1 
ATOM   3549 N N   . THR A 1 470 ? -0.226  -28.654 4.361   1.00 18.93 ? 468  THR B N   1 
ATOM   3550 C CA  . THR A 1 470 ? -0.987  -29.804 3.820   1.00 18.56 ? 468  THR B CA  1 
ATOM   3551 C C   . THR A 1 470 ? -2.361  -29.332 3.315   1.00 17.37 ? 468  THR B C   1 
ATOM   3552 O O   . THR A 1 470 ? -2.923  -29.996 2.456   1.00 18.25 ? 468  THR B O   1 
ATOM   3553 C CB  . THR A 1 470 ? -1.086  -30.976 4.786   1.00 19.99 ? 468  THR B CB  1 
ATOM   3554 O OG1 . THR A 1 470 ? -1.799  -30.573 5.957   1.00 21.01 ? 468  THR B OG1 1 
ATOM   3555 C CG2 . THR A 1 470 ? 0.295   -31.506 5.120   1.00 20.94 ? 468  THR B CG2 1 
ATOM   3556 N N   . LYS A 1 471 ? -2.876  -28.226 3.850   1.00 19.22 ? 469  LYS B N   1 
ATOM   3557 C CA  . LYS A 1 471 ? -4.110  -27.617 3.309   1.00 19.81 ? 469  LYS B CA  1 
ATOM   3558 C C   . LYS A 1 471 ? -3.883  -27.146 1.865   1.00 17.66 ? 469  LYS B C   1 
ATOM   3559 O O   . LYS A 1 471 ? -4.767  -27.412 1.006   1.00 18.38 ? 469  LYS B O   1 
ATOM   3560 C CB  . LYS A 1 471 ? -4.568  -26.434 4.147   1.00 22.75 ? 469  LYS B CB  1 
ATOM   3561 C CG  . LYS A 1 471 ? -5.923  -25.928 3.671   1.00 26.52 ? 469  LYS B CG  1 
ATOM   3562 C CD  . LYS A 1 471 ? -6.572  -24.977 4.634   1.00 31.07 ? 469  LYS B CD  1 
ATOM   3563 C CE  . LYS A 1 471 ? -8.038  -24.797 4.317   1.00 36.48 ? 469  LYS B CE  1 
ATOM   3564 N NZ  . LYS A 1 471 ? -8.683  -23.951 5.347   1.00 41.50 ? 469  LYS B NZ  1 
ATOM   3565 N N   . ILE A 1 472 ? -2.739  -26.531 1.593   1.00 18.12 ? 470  ILE B N   1 
ATOM   3566 C CA  . ILE A 1 472 ? -2.390  -26.058 0.233   1.00 18.69 ? 470  ILE B CA  1 
ATOM   3567 C C   . ILE A 1 472 ? -2.355  -27.284 -0.668  1.00 17.82 ? 470  ILE B C   1 
ATOM   3568 O O   . ILE A 1 472 ? -2.890  -27.261 -1.769  1.00 18.33 ? 470  ILE B O   1 
ATOM   3569 C CB  . ILE A 1 472 ? -1.074  -25.264 0.219   1.00 19.42 ? 470  ILE B CB  1 
ATOM   3570 C CG1 . ILE A 1 472 ? -1.216  -23.962 1.019   1.00 21.98 ? 470  ILE B CG1 1 
ATOM   3571 C CG2 . ILE A 1 472 ? -0.675  -25.005 -1.228  1.00 19.79 ? 470  ILE B CG2 1 
ATOM   3572 C CD1 . ILE A 1 472 ? 0.068   -23.205 1.244   1.00 24.25 ? 470  ILE B CD1 1 
ATOM   3573 N N   . VAL A 1 473 ? -1.695  -28.348 -0.219  1.00 18.63 ? 471  VAL B N   1 
ATOM   3574 C CA  . VAL A 1 473 ? -1.518  -29.553 -1.053  1.00 19.33 ? 471  VAL B CA  1 
ATOM   3575 C C   . VAL A 1 473 ? -2.899  -30.152 -1.312  1.00 18.39 ? 471  VAL B C   1 
ATOM   3576 O O   . VAL A 1 473 ? -3.158  -30.573 -2.471  1.00 19.36 ? 471  VAL B O   1 
ATOM   3577 C CB  . VAL A 1 473 ? -0.557  -30.558 -0.383  1.00 17.95 ? 471  VAL B CB  1 
ATOM   3578 C CG1 . VAL A 1 473 ? -0.499  -31.829 -1.228  1.00 19.17 ? 471  VAL B CG1 1 
ATOM   3579 C CG2 . VAL A 1 473 ? 0.807   -29.926 -0.181  1.00 18.27 ? 471  VAL B CG2 1 
ATOM   3580 N N   . HIS A 1 474 ? -3.726  -30.241 -0.264  1.00 18.56 ? 472  HIS B N   1 
ATOM   3581 C CA  . HIS A 1 474 ? -5.079  -30.844 -0.346  1.00 18.99 ? 472  HIS B CA  1 
ATOM   3582 C C   . HIS A 1 474 ? -5.893  -30.080 -1.405  1.00 18.95 ? 472  HIS B C   1 
ATOM   3583 O O   . HIS A 1 474 ? -6.499  -30.732 -2.284  1.00 21.67 ? 472  HIS B O   1 
ATOM   3584 C CB  . HIS A 1 474 ? -5.757  -30.797 1.034   1.00 20.01 ? 472  HIS B CB  1 
ATOM   3585 C CG  . HIS A 1 474 ? -7.164  -31.255 0.983   1.00 23.27 ? 472  HIS B CG  1 
ATOM   3586 N ND1 . HIS A 1 474 ? -7.513  -32.561 0.722   1.00 25.94 ? 472  HIS B ND1 1 
ATOM   3587 C CD2 . HIS A 1 474 ? -8.311  -30.564 1.132   1.00 28.75 ? 472  HIS B CD2 1 
ATOM   3588 C CE1 . HIS A 1 474 ? -8.829  -32.655 0.695   1.00 26.33 ? 472  HIS B CE1 1 
ATOM   3589 N NE2 . HIS A 1 474 ? -9.329  -31.453 0.929   1.00 27.00 ? 472  HIS B NE2 1 
ATOM   3590 N N   . LYS A 1 475 ? -5.907  -28.761 -1.309  1.00 20.37 ? 473  LYS B N   1 
ATOM   3591 C CA  . LYS A 1 475 ? -6.707  -27.910 -2.238  1.00 21.26 ? 473  LYS B CA  1 
ATOM   3592 C C   . LYS A 1 475 ? -6.171  -28.131 -3.653  1.00 21.96 ? 473  LYS B C   1 
ATOM   3593 O O   . LYS A 1 475 ? -6.985  -28.283 -4.571  1.00 23.36 ? 473  LYS B O   1 
ATOM   3594 C CB  . LYS A 1 475 ? -6.708  -26.446 -1.812  1.00 24.01 ? 473  LYS B CB  1 
ATOM   3595 C CG  . LYS A 1 475 ? -7.479  -26.191 -0.526  1.00 29.63 ? 473  LYS B CG  1 
ATOM   3596 C CD  . LYS A 1 475 ? -7.753  -24.746 -0.232  1.00 38.88 ? 473  LYS B CD  1 
ATOM   3597 C CE  . LYS A 1 475 ? -8.917  -24.210 -1.043  1.00 45.72 ? 473  LYS B CE  1 
ATOM   3598 N NZ  . LYS A 1 475 ? -9.994  -23.666 -0.178  1.00 53.69 ? 473  LYS B NZ  1 
ATOM   3599 N N   . PHE A 1 476 ? -4.843  -28.234 -3.821  1.00 19.71 ? 474  PHE B N   1 
ATOM   3600 C CA  . PHE A 1 476 ? -4.219  -28.492 -5.146  1.00 20.57 ? 474  PHE B CA  1 
ATOM   3601 C C   . PHE A 1 476 ? -4.695  -29.824 -5.711  1.00 20.16 ? 474  PHE B C   1 
ATOM   3602 O O   . PHE A 1 476 ? -4.993  -29.916 -6.936  1.00 19.76 ? 474  PHE B O   1 
ATOM   3603 C CB  . PHE A 1 476 ? -2.676  -28.416 -5.046  1.00 18.68 ? 474  PHE B CB  1 
ATOM   3604 C CG  . PHE A 1 476 ? -1.997  -28.844 -6.320  1.00 18.50 ? 474  PHE B CG  1 
ATOM   3605 C CD1 . PHE A 1 476 ? -1.727  -30.183 -6.589  1.00 17.99 ? 474  PHE B CD1 1 
ATOM   3606 C CD2 . PHE A 1 476 ? -1.594  -27.898 -7.245  1.00 18.41 ? 474  PHE B CD2 1 
ATOM   3607 C CE1 . PHE A 1 476 ? -1.161  -30.558 -7.803  1.00 18.18 ? 474  PHE B CE1 1 
ATOM   3608 C CE2 . PHE A 1 476 ? -0.969  -28.268 -8.422  1.00 18.31 ? 474  PHE B CE2 1 
ATOM   3609 C CZ  . PHE A 1 476 ? -0.765  -29.595 -8.717  1.00 17.93 ? 474  PHE B CZ  1 
ATOM   3610 N N   . CYS A 1 477 ? -4.715  -30.893 -4.906  1.00 19.57 ? 475  CYS B N   1 
ATOM   3611 C CA  . CYS A 1 477 ? -5.166  -32.229 -5.353  1.00 19.22 ? 475  CYS B CA  1 
ATOM   3612 C C   . CYS A 1 477 ? -6.662  -32.164 -5.736  1.00 20.14 ? 475  CYS B C   1 
ATOM   3613 O O   . CYS A 1 477 ? -7.021  -32.709 -6.770  1.00 22.25 ? 475  CYS B O   1 
ATOM   3614 C CB  . CYS A 1 477 ? -4.904  -33.287 -4.295  1.00 19.16 ? 475  CYS B CB  1 
ATOM   3615 S SG  . CYS A 1 477 ? -3.133  -33.584 -4.009  1.00 20.77 ? 475  CYS B SG  1 
ATOM   3616 N N   . GLN A 1 478 ? -7.499  -31.501 -4.949  1.00 21.31 ? 476  GLN B N   1 
ATOM   3617 C CA  . GLN A 1 478 ? -8.963  -31.388 -5.249  1.00 21.97 ? 476  GLN B CA  1 
ATOM   3618 C C   . GLN A 1 478 ? -9.128  -30.689 -6.598  1.00 23.26 ? 476  GLN B C   1 
ATOM   3619 O O   . GLN A 1 478 ? -9.958  -31.129 -7.416  1.00 23.82 ? 476  GLN B O   1 
ATOM   3620 C CB  . GLN A 1 478 ? -9.664  -30.605 -4.145  1.00 25.30 ? 476  GLN B CB  1 
ATOM   3621 C CG  . GLN A 1 478 ? -9.903  -31.449 -2.911  1.00 30.74 ? 476  GLN B CG  1 
ATOM   3622 C CD  . GLN A 1 478 ? -10.716 -30.684 -1.901  1.00 38.45 ? 476  GLN B CD  1 
ATOM   3623 O OE1 . GLN A 1 478 ? -10.449 -29.515 -1.610  1.00 48.39 ? 476  GLN B OE1 1 
ATOM   3624 N NE2 . GLN A 1 478 ? -11.720 -31.347 -1.359  1.00 44.24 ? 476  GLN B NE2 1 
ATOM   3625 N N   . ALA A 1 479 ? -8.333  -29.651 -6.842  1.00 21.68 ? 477  ALA B N   1 
ATOM   3626 C CA  . ALA A 1 479 ? -8.400  -28.845 -8.077  1.00 21.41 ? 477  ALA B CA  1 
ATOM   3627 C C   . ALA A 1 479 ? -7.873  -29.636 -9.274  1.00 22.33 ? 477  ALA B C   1 
ATOM   3628 O O   . ALA A 1 479 ? -8.403  -29.434 -10.397 1.00 22.06 ? 477  ALA B O   1 
ATOM   3629 C CB  . ALA A 1 479 ? -7.671  -27.547 -7.884  1.00 22.31 ? 477  ALA B CB  1 
ATOM   3630 N N   . ASN A 1 480 ? -6.907  -30.559 -9.097  1.00 20.76 ? 478  ASN B N   1 
ATOM   3631 C CA  . ASN A 1 480 ? -6.183  -31.125 -10.258 1.00 20.20 ? 478  ASN B CA  1 
ATOM   3632 C C   . ASN A 1 480 ? -6.367  -32.626 -10.413 1.00 21.64 ? 478  ASN B C   1 
ATOM   3633 O O   . ASN A 1 480 ? -5.797  -33.159 -11.368 1.00 21.81 ? 478  ASN B O   1 
ATOM   3634 C CB  . ASN A 1 480 ? -4.701  -30.718 -10.208 1.00 20.45 ? 478  ASN B CB  1 
ATOM   3635 C CG  . ASN A 1 480 ? -4.527  -29.239 -10.457 1.00 20.17 ? 478  ASN B CG  1 
ATOM   3636 O OD1 . ASN A 1 480 ? -4.560  -28.780 -11.609 1.00 20.62 ? 478  ASN B OD1 1 
ATOM   3637 N ND2 . ASN A 1 480 ? -4.361  -28.481 -9.399  1.00 20.14 ? 478  ASN B ND2 1 
ATOM   3638 N N   . GLU A 1 481 ? -7.210  -33.267 -9.595  1.00 24.13 ? 479  GLU B N   1 
ATOM   3639 C CA  . GLU A 1 481 ? -7.367  -34.754 -9.598  1.00 26.03 ? 479  GLU B CA  1 
ATOM   3640 C C   . GLU A 1 481 ? -7.962  -35.285 -10.920 1.00 25.37 ? 479  GLU B C   1 
ATOM   3641 O O   . GLU A 1 481 ? -7.699  -36.479 -11.202 1.00 23.52 ? 479  GLU B O   1 
ATOM   3642 C CB  . GLU A 1 481 ? -8.168  -35.231 -8.393  1.00 29.09 ? 479  GLU B CB  1 
ATOM   3643 C CG  . GLU A 1 481 ? -9.568  -34.654 -8.296  1.00 30.04 ? 479  GLU B CG  1 
ATOM   3644 C CD  . GLU A 1 481 ? -10.345 -35.167 -7.094  1.00 36.41 ? 479  GLU B CD  1 
ATOM   3645 O OE1 . GLU A 1 481 ? -9.704  -35.636 -6.143  1.00 35.82 ? 479  GLU B OE1 1 
ATOM   3646 O OE2 . GLU A 1 481 ? -11.592 -35.067 -7.102  1.00 37.38 ? 479  GLU B OE2 1 
ATOM   3647 N N   . ALA A 1 482 ? -8.660  -34.459 -11.721 1.00 24.46 ? 480  ALA B N   1 
ATOM   3648 C CA  . ALA A 1 482 ? -9.212  -34.863 -13.049 1.00 26.75 ? 480  ALA B CA  1 
ATOM   3649 C C   . ALA A 1 482 ? -8.584  -34.043 -14.174 1.00 28.61 ? 480  ALA B C   1 
ATOM   3650 O O   . ALA A 1 482 ? -9.094  -34.086 -15.311 1.00 28.87 ? 480  ALA B O   1 
ATOM   3651 C CB  . ALA A 1 482 ? -10.715 -34.698 -13.096 1.00 29.31 ? 480  ALA B CB  1 
ATOM   3652 N N   . ASN A 1 483 ? -7.532  -33.286 -13.879 1.00 24.09 ? 481  ASN B N   1 
ATOM   3653 C CA  . ASN A 1 483 ? -6.784  -32.522 -14.899 1.00 24.03 ? 481  ASN B CA  1 
ATOM   3654 C C   . ASN A 1 483 ? -5.894  -33.502 -15.660 1.00 28.25 ? 481  ASN B C   1 
ATOM   3655 O O   . ASN A 1 483 ? -4.849  -33.957 -15.085 1.00 26.68 ? 481  ASN B O   1 
ATOM   3656 C CB  . ASN A 1 483 ? -6.006  -31.409 -14.213 1.00 24.57 ? 481  ASN B CB  1 
ATOM   3657 C CG  . ASN A 1 483 ? -5.123  -30.630 -15.144 1.00 25.50 ? 481  ASN B CG  1 
ATOM   3658 O OD1 . ASN A 1 483 ? -4.918  -31.005 -16.301 1.00 27.28 ? 481  ASN B OD1 1 
ATOM   3659 N ND2 . ASN A 1 483 ? -4.556  -29.574 -14.611 1.00 25.01 ? 481  ASN B ND2 1 
ATOM   3660 N N   . GLU A 1 484 ? -6.237  -33.826 -16.911 1.00 29.32 ? 482  GLU B N   1 
ATOM   3661 C CA  . GLU A 1 484 ? -5.589  -34.959 -17.635 1.00 30.41 ? 482  GLU B CA  1 
ATOM   3662 C C   . GLU A 1 484 ? -4.065  -34.788 -17.635 1.00 28.90 ? 482  GLU B C   1 
ATOM   3663 O O   . GLU A 1 484 ? -3.356  -35.802 -17.436 1.00 29.83 ? 482  GLU B O   1 
ATOM   3664 C CB  . GLU A 1 484 ? -6.101  -35.107 -19.071 1.00 35.14 ? 482  GLU B CB  1 
ATOM   3665 C CG  . GLU A 1 484 ? -7.450  -35.792 -19.164 1.00 44.00 ? 482  GLU B CG  1 
ATOM   3666 C CD  . GLU A 1 484 ? -7.549  -37.198 -18.585 1.00 49.69 ? 482  GLU B CD  1 
ATOM   3667 O OE1 . GLU A 1 484 ? -6.708  -38.046 -18.930 1.00 55.65 ? 482  GLU B OE1 1 
ATOM   3668 O OE2 . GLU A 1 484 ? -8.481  -37.442 -17.791 1.00 57.98 ? 482  GLU B OE2 1 
ATOM   3669 N N   . ALA A 1 485 ? -3.565  -33.573 -17.854 1.00 26.55 ? 483  ALA B N   1 
ATOM   3670 C CA  . ALA A 1 485 ? -2.114  -33.256 -17.904 1.00 28.91 ? 483  ALA B CA  1 
ATOM   3671 C C   . ALA A 1 485 ? -1.378  -33.627 -16.604 1.00 26.73 ? 483  ALA B C   1 
ATOM   3672 O O   . ALA A 1 485 ? -0.194  -33.953 -16.688 1.00 28.23 ? 483  ALA B O   1 
ATOM   3673 C CB  . ALA A 1 485 ? -1.907  -31.801 -18.237 1.00 30.19 ? 483  ALA B CB  1 
ATOM   3674 N N   . VAL A 1 486 ? -1.982  -33.575 -15.431 1.00 26.06 ? 484  VAL B N   1 
ATOM   3675 C CA  . VAL A 1 486 ? -1.198  -33.821 -14.181 1.00 25.96 ? 484  VAL B CA  1 
ATOM   3676 C C   . VAL A 1 486 ? -1.869  -34.824 -13.245 1.00 25.09 ? 484  VAL B C   1 
ATOM   3677 O O   . VAL A 1 486 ? -1.382  -34.987 -12.091 1.00 24.18 ? 484  VAL B O   1 
ATOM   3678 C CB  . VAL A 1 486 ? -0.862  -32.500 -13.475 1.00 26.95 ? 484  VAL B CB  1 
ATOM   3679 C CG1 . VAL A 1 486 ? 0.082   -31.673 -14.331 1.00 29.20 ? 484  VAL B CG1 1 
ATOM   3680 C CG2 . VAL A 1 486 ? -2.101  -31.702 -13.108 1.00 27.69 ? 484  VAL B CG2 1 
ATOM   3681 N N   . LYS A 1 487 ? -2.926  -35.517 -13.679 1.00 25.32 ? 485  LYS B N   1 
ATOM   3682 C CA  . LYS A 1 487 ? -3.616  -36.440 -12.748 1.00 26.53 ? 485  LYS B CA  1 
ATOM   3683 C C   . LYS A 1 487 ? -2.630  -37.542 -12.321 1.00 24.36 ? 485  LYS B C   1 
ATOM   3684 O O   . LYS A 1 487 ? -2.801  -38.078 -11.216 1.00 23.03 ? 485  LYS B O   1 
ATOM   3685 C CB  . LYS A 1 487 ? -4.921  -36.956 -13.355 1.00 26.61 ? 485  LYS B CB  1 
ATOM   3686 C CG  . LYS A 1 487 ? -4.787  -37.829 -14.584 1.00 31.57 ? 485  LYS B CG  1 
ATOM   3687 C CD  . LYS A 1 487 ? -6.127  -38.312 -15.126 1.00 35.28 ? 485  LYS B CD  1 
ATOM   3688 C CE  . LYS A 1 487 ? -7.042  -38.865 -14.054 1.00 42.41 ? 485  LYS B CE  1 
ATOM   3689 N NZ  . LYS A 1 487 ? -8.228  -39.531 -14.652 1.00 52.29 ? 485  LYS B NZ  1 
ATOM   3690 N N   . GLU A 1 488 ? -1.631  -37.856 -13.145 1.00 24.67 ? 486  GLU B N   1 
ATOM   3691 C CA  . GLU A 1 488 ? -0.594  -38.871 -12.815 1.00 26.09 ? 486  GLU B CA  1 
ATOM   3692 C C   . GLU A 1 488 ? 0.223   -38.409 -11.594 1.00 25.31 ? 486  GLU B C   1 
ATOM   3693 O O   . GLU A 1 488 ? 0.706   -39.307 -10.843 1.00 25.64 ? 486  GLU B O   1 
ATOM   3694 C CB  . GLU A 1 488 ? 0.326   -39.166 -14.004 1.00 29.85 ? 486  GLU B CB  1 
ATOM   3695 C CG  . GLU A 1 488 ? 1.268   -38.008 -14.398 1.00 32.60 ? 486  GLU B CG  1 
ATOM   3696 C CD  . GLU A 1 488 ? 2.117   -38.207 -15.655 1.00 39.74 ? 486  GLU B CD  1 
ATOM   3697 O OE1 . GLU A 1 488 ? 1.660   -37.804 -16.739 1.00 44.23 ? 486  GLU B OE1 1 
ATOM   3698 O OE2 . GLU A 1 488 ? 3.243   -38.746 -15.551 1.00 37.28 ? 486  GLU B OE2 1 
ATOM   3699 N N   . PHE A 1 489 ? 0.406   -37.088 -11.406 1.00 21.47 ? 487  PHE B N   1 
ATOM   3700 C CA  . PHE A 1 489 ? 1.138   -36.522 -10.237 1.00 20.77 ? 487  PHE B CA  1 
ATOM   3701 C C   . PHE A 1 489 ? 0.196   -36.443 -9.034  1.00 21.66 ? 487  PHE B C   1 
ATOM   3702 O O   . PHE A 1 489 ? 0.615   -36.665 -7.886  1.00 20.19 ? 487  PHE B O   1 
ATOM   3703 C CB  . PHE A 1 489 ? 1.707   -35.135 -10.533 1.00 21.59 ? 487  PHE B CB  1 
ATOM   3704 C CG  . PHE A 1 489 ? 2.638   -35.088 -11.714 1.00 22.08 ? 487  PHE B CG  1 
ATOM   3705 C CD1 . PHE A 1 489 ? 3.953   -35.484 -11.617 1.00 23.54 ? 487  PHE B CD1 1 
ATOM   3706 C CD2 . PHE A 1 489 ? 2.210   -34.611 -12.938 1.00 21.89 ? 487  PHE B CD2 1 
ATOM   3707 C CE1 . PHE A 1 489 ? 4.801   -35.423 -12.712 1.00 24.16 ? 487  PHE B CE1 1 
ATOM   3708 C CE2 . PHE A 1 489 ? 3.056   -34.545 -14.024 1.00 21.34 ? 487  PHE B CE2 1 
ATOM   3709 C CZ  . PHE A 1 489 ? 4.344   -35.000 -13.934 1.00 22.82 ? 487  PHE B CZ  1 
ATOM   3710 N N   . VAL A 1 490 ? -1.070  -36.076 -9.254  1.00 20.66 ? 488  VAL B N   1 
ATOM   3711 C CA  . VAL A 1 490 ? -2.014  -35.825 -8.127  1.00 20.12 ? 488  VAL B CA  1 
ATOM   3712 C C   . VAL A 1 490 ? -2.267  -37.100 -7.327  1.00 20.12 ? 488  VAL B C   1 
ATOM   3713 O O   . VAL A 1 490 ? -2.307  -36.997 -6.089  1.00 22.67 ? 488  VAL B O   1 
ATOM   3714 C CB  . VAL A 1 490 ? -3.340  -35.200 -8.608  1.00 20.34 ? 488  VAL B CB  1 
ATOM   3715 C CG1 . VAL A 1 490 ? -4.331  -35.059 -7.467  1.00 21.02 ? 488  VAL B CG1 1 
ATOM   3716 C CG2 . VAL A 1 490 ? -3.055  -33.889 -9.279  1.00 21.34 ? 488  VAL B CG2 1 
ATOM   3717 N N   . ALA A 1 491 ? -2.486  -38.240 -7.981  1.00 20.24 ? 489  ALA B N   1 
ATOM   3718 C CA  . ALA A 1 491 ? -2.804  -39.498 -7.281  1.00 21.32 ? 489  ALA B CA  1 
ATOM   3719 C C   . ALA A 1 491 ? -1.731  -39.781 -6.219  1.00 21.29 ? 489  ALA B C   1 
ATOM   3720 O O   . ALA A 1 491 ? -2.068  -39.884 -5.025  1.00 20.50 ? 489  ALA B O   1 
ATOM   3721 C CB  . ALA A 1 491 ? -2.978  -40.602 -8.294  1.00 23.99 ? 489  ALA B CB  1 
ATOM   3722 N N   . PRO A 1 492 ? -0.427  -39.929 -6.573  1.00 19.19 ? 490  PRO B N   1 
ATOM   3723 C CA  . PRO A 1 492 ? 0.598   -40.165 -5.544  1.00 19.95 ? 490  PRO B CA  1 
ATOM   3724 C C   . PRO A 1 492 ? 0.728   -38.991 -4.554  1.00 18.09 ? 490  PRO B C   1 
ATOM   3725 O O   . PRO A 1 492 ? 0.948   -39.220 -3.369  1.00 19.01 ? 490  PRO B O   1 
ATOM   3726 C CB  . PRO A 1 492 ? 1.902   -40.394 -6.322  1.00 19.91 ? 490  PRO B CB  1 
ATOM   3727 C CG  . PRO A 1 492 ? 1.628   -39.794 -7.713  1.00 21.08 ? 490  PRO B CG  1 
ATOM   3728 C CD  . PRO A 1 492 ? 0.144   -40.004 -7.923  1.00 19.95 ? 490  PRO B CD  1 
ATOM   3729 N N   . LEU A 1 493 ? 0.618   -37.750 -5.016  1.00 16.60 ? 491  LEU B N   1 
ATOM   3730 C CA  . LEU A 1 493 ? 0.710   -36.577 -4.125  1.00 16.56 ? 491  LEU B CA  1 
ATOM   3731 C C   . LEU A 1 493 ? -0.393  -36.618 -3.060  1.00 16.65 ? 491  LEU B C   1 
ATOM   3732 O O   . LEU A 1 493 ? -0.111  -36.290 -1.890  1.00 17.18 ? 491  LEU B O   1 
ATOM   3733 C CB  . LEU A 1 493 ? 0.610   -35.289 -4.949  1.00 16.16 ? 491  LEU B CB  1 
ATOM   3734 C CG  . LEU A 1 493 ? 0.699   -34.008 -4.139  1.00 15.32 ? 491  LEU B CG  1 
ATOM   3735 C CD1 . LEU A 1 493 ? 2.015   -33.929 -3.345  1.00 16.51 ? 491  LEU B CD1 1 
ATOM   3736 C CD2 . LEU A 1 493 ? 0.567   -32.792 -5.056  1.00 16.86 ? 491  LEU B CD2 1 
ATOM   3737 N N   . ALA A 1 494 ? -1.630  -36.945 -3.440  1.00 17.69 ? 492  ALA B N   1 
ATOM   3738 C CA  . ALA A 1 494 ? -2.738  -37.003 -2.463  1.00 17.83 ? 492  ALA B CA  1 
ATOM   3739 C C   . ALA A 1 494 ? -2.484  -38.143 -1.464  1.00 17.16 ? 492  ALA B C   1 
ATOM   3740 O O   . ALA A 1 494 ? -2.757  -37.940 -0.286  1.00 17.84 ? 492  ALA B O   1 
ATOM   3741 C CB  . ALA A 1 494 ? -4.080  -37.162 -3.169  1.00 18.89 ? 492  ALA B CB  1 
ATOM   3742 N N   . GLN A 1 495 ? -1.996  -39.296 -1.917  1.00 19.29 ? 493  GLN B N   1 
ATOM   3743 C CA  . GLN A 1 495 ? -1.638  -40.431 -1.025  1.00 19.97 ? 493  GLN B CA  1 
ATOM   3744 C C   . GLN A 1 495 ? -0.566  -39.916 -0.049  1.00 18.21 ? 493  GLN B C   1 
ATOM   3745 O O   . GLN A 1 495 ? -0.689  -40.132 1.183   1.00 16.78 ? 493  GLN B O   1 
ATOM   3746 C CB  . GLN A 1 495 ? -1.189  -41.607 -1.901  1.00 25.90 ? 493  GLN B CB  1 
ATOM   3747 C CG  . GLN A 1 495 ? -1.334  -43.008 -1.318  1.00 38.68 ? 493  GLN B CG  1 
ATOM   3748 C CD  . GLN A 1 495 ? -1.085  -44.017 -2.420  1.00 45.13 ? 493  GLN B CD  1 
ATOM   3749 O OE1 . GLN A 1 495 ? -0.129  -44.796 -2.394  1.00 53.13 ? 493  GLN B OE1 1 
ATOM   3750 N NE2 . GLN A 1 495 ? -1.899  -43.935 -3.465  1.00 48.79 ? 493  GLN B NE2 1 
ATOM   3751 N N   . LEU A 1 496 ? 0.449   -39.226 -0.573  1.00 16.06 ? 494  LEU B N   1 
ATOM   3752 C CA  . LEU A 1 496 ? 1.566   -38.755 0.267   1.00 15.08 ? 494  LEU B CA  1 
ATOM   3753 C C   . LEU A 1 496 ? 1.036   -37.741 1.266   1.00 16.54 ? 494  LEU B C   1 
ATOM   3754 O O   . LEU A 1 496 ? 1.422   -37.762 2.460   1.00 17.33 ? 494  LEU B O   1 
ATOM   3755 C CB  . LEU A 1 496 ? 2.654   -38.191 -0.641  1.00 16.84 ? 494  LEU B CB  1 
ATOM   3756 C CG  . LEU A 1 496 ? 3.941   -37.811 0.070   1.00 16.53 ? 494  LEU B CG  1 
ATOM   3757 C CD1 . LEU A 1 496 ? 4.750   -39.056 0.376   1.00 17.86 ? 494  LEU B CD1 1 
ATOM   3758 C CD2 . LEU A 1 496 ? 4.746   -36.806 -0.733  1.00 17.27 ? 494  LEU B CD2 1 
ATOM   3759 N N   . ASN A 1 497 ? 0.143   -36.839 0.828   1.00 16.67 ? 495  ASN B N   1 
ATOM   3760 C CA  . ASN A 1 497 ? -0.341  -35.771 1.729   1.00 17.72 ? 495  ASN B CA  1 
ATOM   3761 C C   . ASN A 1 497 ? -1.087  -36.383 2.917   1.00 17.71 ? 495  ASN B C   1 
ATOM   3762 O O   . ASN A 1 497 ? -0.878  -35.927 4.062   1.00 20.19 ? 495  ASN B O   1 
ATOM   3763 C CB  . ASN A 1 497 ? -1.221  -34.781 0.956   1.00 18.26 ? 495  ASN B CB  1 
ATOM   3764 C CG  . ASN A 1 497 ? -1.347  -33.450 1.666   1.00 17.66 ? 495  ASN B CG  1 
ATOM   3765 O OD1 . ASN A 1 497 ? -0.361  -32.865 2.110   1.00 19.19 ? 495  ASN B OD1 1 
ATOM   3766 N ND2 . ASN A 1 497 ? -2.558  -32.921 1.708   1.00 18.94 ? 495  ASN B ND2 1 
ATOM   3767 N N   . LYS A 1 498 ? -1.912  -37.399 2.659   1.00 18.97 ? 496  LYS B N   1 
ATOM   3768 C CA  . LYS A 1 498 ? -2.669  -38.081 3.731   1.00 21.23 ? 496  LYS B CA  1 
ATOM   3769 C C   . LYS A 1 498 ? -1.652  -38.773 4.640   1.00 18.55 ? 496  LYS B C   1 
ATOM   3770 O O   . LYS A 1 498 ? -1.735  -38.637 5.880   1.00 17.69 ? 496  LYS B O   1 
ATOM   3771 C CB  . LYS A 1 498 ? -3.683  -39.052 3.128   1.00 26.09 ? 496  LYS B CB  1 
ATOM   3772 C CG  . LYS A 1 498 ? -4.352  -39.955 4.159   1.00 32.53 ? 496  LYS B CG  1 
ATOM   3773 C CD  . LYS A 1 498 ? -5.599  -40.655 3.640   1.00 40.71 ? 496  LYS B CD  1 
ATOM   3774 C CE  . LYS A 1 498 ? -5.368  -41.477 2.387   1.00 48.40 ? 496  LYS B CE  1 
ATOM   3775 N NZ  . LYS A 1 498 ? -5.395  -42.937 2.660   1.00 55.86 ? 496  LYS B NZ  1 
ATOM   3776 N N   . GLU A 1 499 ? -0.680  -39.455 4.032   1.00 17.33 ? 497  GLU B N   1 
ATOM   3777 C CA  . GLU A 1 499 ? 0.359   -40.171 4.827   1.00 17.44 ? 497  GLU B CA  1 
ATOM   3778 C C   . GLU A 1 499 ? 1.124   -39.210 5.732   1.00 17.92 ? 497  GLU B C   1 
ATOM   3779 O O   . GLU A 1 499 ? 1.396   -39.538 6.913   1.00 18.04 ? 497  GLU B O   1 
ATOM   3780 C CB  . GLU A 1 499 ? 1.293   -40.918 3.895   1.00 15.76 ? 497  GLU B CB  1 
ATOM   3781 C CG  . GLU A 1 499 ? 2.349   -41.687 4.644   1.00 15.90 ? 497  GLU B CG  1 
ATOM   3782 C CD  . GLU A 1 499 ? 3.400   -42.277 3.740   1.00 17.53 ? 497  GLU B CD  1 
ATOM   3783 O OE1 . GLU A 1 499 ? 3.596   -43.493 3.812   1.00 18.29 ? 497  GLU B OE1 1 
ATOM   3784 O OE2 . GLU A 1 499 ? 3.994   -41.517 2.945   1.00 16.13 ? 497  GLU B OE2 1 
ATOM   3785 N N   . TRP A 1 500 ? 1.435   -38.011 5.248   1.00 16.90 ? 498  TRP B N   1 
ATOM   3786 C CA  . TRP A 1 500 ? 2.236   -37.031 6.009   1.00 16.88 ? 498  TRP B CA  1 
ATOM   3787 C C   . TRP A 1 500 ? 1.548   -36.722 7.343   1.00 17.02 ? 498  TRP B C   1 
ATOM   3788 O O   . TRP A 1 500 ? 2.190   -36.731 8.383   1.00 17.17 ? 498  TRP B O   1 
ATOM   3789 C CB  . TRP A 1 500 ? 2.430   -35.791 5.152   1.00 16.78 ? 498  TRP B CB  1 
ATOM   3790 C CG  . TRP A 1 500 ? 3.484   -34.806 5.546   1.00 17.00 ? 498  TRP B CG  1 
ATOM   3791 C CD1 . TRP A 1 500 ? 4.416   -34.838 6.555   1.00 17.36 ? 498  TRP B CD1 1 
ATOM   3792 C CD2 . TRP A 1 500 ? 3.800   -33.647 4.755   1.00 16.50 ? 498  TRP B CD2 1 
ATOM   3793 N NE1 . TRP A 1 500 ? 5.265   -33.777 6.439   1.00 17.06 ? 498  TRP B NE1 1 
ATOM   3794 C CE2 . TRP A 1 500 ? 4.949   -33.051 5.318   1.00 16.75 ? 498  TRP B CE2 1 
ATOM   3795 C CE3 . TRP A 1 500 ? 3.271   -33.131 3.573   1.00 17.39 ? 498  TRP B CE3 1 
ATOM   3796 C CZ2 . TRP A 1 500 ? 5.496   -31.876 4.807   1.00 17.30 ? 498  TRP B CZ2 1 
ATOM   3797 C CZ3 . TRP A 1 500 ? 3.813   -31.971 3.063   1.00 17.35 ? 498  TRP B CZ3 1 
ATOM   3798 C CH2 . TRP A 1 500 ? 4.945   -31.385 3.648   1.00 18.34 ? 498  TRP B CH2 1 
ATOM   3799 N N   . GLY A 1 501 ? 0.243   -36.493 7.346   1.00 19.08 ? 499  GLY B N   1 
ATOM   3800 C CA  . GLY A 1 501 ? -0.482  -36.292 8.612   1.00 17.62 ? 499  GLY B CA  1 
ATOM   3801 C C   . GLY A 1 501 ? -0.510  -37.547 9.463   1.00 18.60 ? 499  GLY B C   1 
ATOM   3802 O O   . GLY A 1 501 ? -0.297  -37.432 10.685  1.00 20.42 ? 499  GLY B O   1 
ATOM   3803 N N   . ASP A 1 502 ? -0.773  -38.696 8.863   1.00 19.95 ? 500  ASP B N   1 
ATOM   3804 C CA  . ASP A 1 502 ? -0.834  -39.988 9.593   1.00 20.58 ? 500  ASP B CA  1 
ATOM   3805 C C   . ASP A 1 502 ? 0.507   -40.275 10.264  1.00 21.19 ? 500  ASP B C   1 
ATOM   3806 O O   . ASP A 1 502 ? 0.510   -40.659 11.455  1.00 19.71 ? 500  ASP B O   1 
ATOM   3807 C CB  . ASP A 1 502 ? -1.224  -41.131 8.672   1.00 22.03 ? 500  ASP B CB  1 
ATOM   3808 C CG  . ASP A 1 502 ? -2.667  -41.028 8.191   1.00 27.95 ? 500  ASP B CG  1 
ATOM   3809 O OD1 . ASP A 1 502 ? -3.441  -40.300 8.831   1.00 30.75 ? 500  ASP B OD1 1 
ATOM   3810 O OD2 . ASP A 1 502 ? -2.978  -41.647 7.163   1.00 29.54 ? 500  ASP B OD2 1 
ATOM   3811 N N   . LEU A 1 503 ? 1.609   -40.061 9.544   1.00 19.03 ? 501  LEU B N   1 
ATOM   3812 C CA  . LEU A 1 503 ? 2.984   -40.286 10.086  1.00 19.70 ? 501  LEU B CA  1 
ATOM   3813 C C   . LEU A 1 503 ? 3.195   -39.363 11.274  1.00 18.37 ? 501  LEU B C   1 
ATOM   3814 O O   . LEU A 1 503 ? 3.785   -39.770 12.288  1.00 19.24 ? 501  LEU B O   1 
ATOM   3815 C CB  . LEU A 1 503 ? 4.031   -39.963 9.019   1.00 21.76 ? 501  LEU B CB  1 
ATOM   3816 C CG  . LEU A 1 503 ? 4.176   -40.977 7.897   1.00 28.44 ? 501  LEU B CG  1 
ATOM   3817 C CD1 . LEU A 1 503 ? 5.133   -40.447 6.835   1.00 32.10 ? 501  LEU B CD1 1 
ATOM   3818 C CD2 . LEU A 1 503 ? 4.662   -42.309 8.452   1.00 30.07 ? 501  LEU B CD2 1 
ATOM   3819 N N   . THR A 1 504 ? 2.820   -38.101 11.128  1.00 17.77 ? 502  THR B N   1 
ATOM   3820 C CA  . THR A 1 504 ? 3.013   -37.102 12.187  1.00 17.91 ? 502  THR B CA  1 
ATOM   3821 C C   . THR A 1 504 ? 2.298   -37.589 13.451  1.00 19.17 ? 502  THR B C   1 
ATOM   3822 O O   . THR A 1 504 ? 2.852   -37.448 14.535  1.00 19.06 ? 502  THR B O   1 
ATOM   3823 C CB  . THR A 1 504 ? 2.595   -35.704 11.730  1.00 20.76 ? 502  THR B CB  1 
ATOM   3824 O OG1 . THR A 1 504 ? 3.300   -35.386 10.527  1.00 18.53 ? 502  THR B OG1 1 
ATOM   3825 C CG2 . THR A 1 504 ? 2.868   -34.689 12.812  1.00 20.32 ? 502  THR B CG2 1 
ATOM   3826 N N   . MET A 1 505 ? 1.074   -38.103 13.305  1.00 20.12 ? 503  MET B N   1 
ATOM   3827 C CA  . MET A 1 505 ? 0.269   -38.599 14.445  1.00 20.75 ? 503  MET B CA  1 
ATOM   3828 C C   . MET A 1 505 ? 0.971   -39.807 15.077  1.00 20.19 ? 503  MET B C   1 
ATOM   3829 O O   . MET A 1 505 ? 1.099   -39.850 16.293  1.00 20.37 ? 503  MET B O   1 
ATOM   3830 C CB  . MET A 1 505 ? -1.115  -39.026 13.950  1.00 26.31 ? 503  MET B CB  1 
ATOM   3831 C CG  . MET A 1 505 ? -1.965  -37.879 13.449  1.00 31.98 ? 503  MET B CG  1 
ATOM   3832 S SD  . MET A 1 505 ? -2.556  -36.734 14.730  1.00 42.65 ? 503  MET B SD  1 
ATOM   3833 C CE  . MET A 1 505 ? -2.613  -37.772 16.185  1.00 40.18 ? 503  MET B CE  1 
ATOM   3834 N N   . LYS A 1 506 ? 1.500   -40.720 14.258  1.00 19.05 ? 504  LYS B N   1 
ATOM   3835 C CA  . LYS A 1 506 ? 2.193   -41.938 14.759  1.00 19.76 ? 504  LYS B CA  1 
ATOM   3836 C C   . LYS A 1 506 ? 3.480   -41.548 15.485  1.00 19.75 ? 504  LYS B C   1 
ATOM   3837 O O   . LYS A 1 506 ? 3.754   -42.086 16.568  1.00 19.79 ? 504  LYS B O   1 
ATOM   3838 C CB  . LYS A 1 506 ? 2.475   -42.916 13.626  1.00 20.41 ? 504  LYS B CB  1 
ATOM   3839 C CG  . LYS A 1 506 ? 1.241   -43.638 13.140  1.00 21.66 ? 504  LYS B CG  1 
ATOM   3840 C CD  . LYS A 1 506 ? 1.445   -44.594 12.017  1.00 25.07 ? 504  LYS B CD  1 
ATOM   3841 C CE  . LYS A 1 506 ? 0.148   -45.283 11.646  1.00 31.78 ? 504  LYS B CE  1 
ATOM   3842 N NZ  . LYS A 1 506 ? 0.248   -45.921 10.321  1.00 37.29 ? 504  LYS B NZ  1 
ATOM   3843 N N   . VAL A 1 507 ? 4.241   -40.634 14.911  1.00 19.64 ? 505  VAL B N   1 
ATOM   3844 C CA  . VAL A 1 507 ? 5.489   -40.161 15.578  1.00 20.21 ? 505  VAL B CA  1 
ATOM   3845 C C   . VAL A 1 507 ? 5.136   -39.438 16.885  1.00 19.91 ? 505  VAL B C   1 
ATOM   3846 O O   . VAL A 1 507 ? 5.833   -39.701 17.905  1.00 20.90 ? 505  VAL B O   1 
ATOM   3847 C CB  . VAL A 1 507 ? 6.339   -39.333 14.622  1.00 20.89 ? 505  VAL B CB  1 
ATOM   3848 C CG1 . VAL A 1 507 ? 7.486   -38.655 15.357  1.00 21.20 ? 505  VAL B CG1 1 
ATOM   3849 C CG2 . VAL A 1 507 ? 6.847   -40.232 13.510  1.00 21.06 ? 505  VAL B CG2 1 
ATOM   3850 N N   . GLY A 1 508 ? 4.108   -38.600 16.888  1.00 18.31 ? 506  GLY B N   1 
ATOM   3851 C CA  . GLY A 1 508 ? 3.700   -37.921 18.128  1.00 19.95 ? 506  GLY B CA  1 
ATOM   3852 C C   . GLY A 1 508 ? 3.332   -38.901 19.229  1.00 19.03 ? 506  GLY B C   1 
ATOM   3853 O O   . GLY A 1 508 ? 3.724   -38.666 20.360  1.00 20.44 ? 506  GLY B O   1 
ATOM   3854 N N   . MET A 1 509 ? 2.601   -39.953 18.880  1.00 20.56 ? 507  MET B N   1 
ATOM   3855 C CA  . MET A 1 509 ? 2.170   -40.965 19.878  1.00 23.05 ? 507  MET B CA  1 
ATOM   3856 C C   . MET A 1 509 ? 3.405   -41.654 20.469  1.00 24.97 ? 507  MET B C   1 
ATOM   3857 O O   . MET A 1 509 ? 3.443   -41.885 21.669  1.00 22.55 ? 507  MET B O   1 
ATOM   3858 C CB  . MET A 1 509 ? 1.251   -42.012 19.245  1.00 24.61 ? 507  MET B CB  1 
ATOM   3859 C CG  . MET A 1 509 ? -0.135  -41.521 18.919  1.00 30.11 ? 507  MET B CG  1 
ATOM   3860 S SD  . MET A 1 509 ? -1.190  -42.892 18.377  1.00 40.33 ? 507  MET B SD  1 
ATOM   3861 C CE  . MET A 1 509 ? -0.574  -43.155 16.716  1.00 41.79 ? 507  MET B CE  1 
ATOM   3862 N N   . ALA A 1 510 ? 4.365   -41.975 19.618  1.00 22.51 ? 508  ALA B N   1 
ATOM   3863 C CA  . ALA A 1 510 ? 5.595   -42.626 20.105  1.00 23.85 ? 508  ALA B CA  1 
ATOM   3864 C C   . ALA A 1 510 ? 6.340   -41.687 21.046  1.00 23.04 ? 508  ALA B C   1 
ATOM   3865 O O   . ALA A 1 510 ? 6.882   -42.179 22.036  1.00 22.80 ? 508  ALA B O   1 
ATOM   3866 C CB  . ALA A 1 510 ? 6.451   -42.982 18.928  1.00 26.03 ? 508  ALA B CB  1 
ATOM   3867 N N   . ALA A 1 511 ? 6.358   -40.402 20.715  1.00 23.09 ? 509  ALA B N   1 
ATOM   3868 C CA  . ALA A 1 511 ? 7.089   -39.399 21.517  1.00 23.25 ? 509  ALA B CA  1 
ATOM   3869 C C   . ALA A 1 511 ? 6.433   -39.231 22.888  1.00 25.05 ? 509  ALA B C   1 
ATOM   3870 O O   . ALA A 1 511 ? 7.126   -38.899 23.841  1.00 24.96 ? 509  ALA B O   1 
ATOM   3871 C CB  . ALA A 1 511 ? 7.137   -38.089 20.786  1.00 25.83 ? 509  ALA B CB  1 
ATOM   3872 N N   . MET A 1 512 ? 5.132   -39.459 22.941  1.00 24.04 ? 510  MET B N   1 
ATOM   3873 C CA  . MET A 1 512 ? 4.409   -39.330 24.227  1.00 25.90 ? 510  MET B CA  1 
ATOM   3874 C C   . MET A 1 512 ? 4.791   -40.513 25.125  1.00 27.11 ? 510  MET B C   1 
ATOM   3875 O O   . MET A 1 512 ? 4.795   -40.342 26.332  1.00 30.23 ? 510  MET B O   1 
ATOM   3876 C CB  . MET A 1 512 ? 2.905   -39.308 23.943  1.00 27.19 ? 510  MET B CB  1 
ATOM   3877 C CG  . MET A 1 512 ? 2.462   -38.004 23.302  1.00 32.70 ? 510  MET B CG  1 
ATOM   3878 S SD  . MET A 1 512 ? 0.695   -37.899 22.935  1.00 37.92 ? 510  MET B SD  1 
ATOM   3879 C CE  . MET A 1 512 ? 0.063   -37.633 24.587  1.00 36.66 ? 510  MET B CE  1 
ATOM   3880 N N   . LYS A 1 513 ? 5.095   -41.659 24.523  1.00 26.81 ? 511  LYS B N   1 
ATOM   3881 C CA  . LYS A 1 513 ? 5.445   -42.885 25.289  1.00 30.93 ? 511  LYS B CA  1 
ATOM   3882 C C   . LYS A 1 513 ? 6.934   -42.854 25.636  1.00 33.01 ? 511  LYS B C   1 
ATOM   3883 O O   . LYS A 1 513 ? 7.283   -43.343 26.703  1.00 30.68 ? 511  LYS B O   1 
ATOM   3884 C CB  . LYS A 1 513 ? 5.078   -44.122 24.462  1.00 34.27 ? 511  LYS B CB  1 
ATOM   3885 C CG  . LYS A 1 513 ? 5.351   -45.467 25.118  1.00 39.19 ? 511  LYS B CG  1 
ATOM   3886 C CD  . LYS A 1 513 ? 4.696   -46.622 24.390  1.00 41.15 ? 511  LYS B CD  1 
ATOM   3887 C CE  . LYS A 1 513 ? 4.889   -47.951 25.091  1.00 47.09 ? 511  LYS B CE  1 
ATOM   3888 N NZ  . LYS A 1 513 ? 4.455   -49.089 24.246  1.00 51.20 ? 511  LYS B NZ  1 
ATOM   3889 N N   . ASP A 1 514 ? 7.754   -42.236 24.788  1.00 28.08 ? 512  ASP B N   1 
ATOM   3890 C CA  . ASP A 1 514 ? 9.225   -42.200 24.979  1.00 29.53 ? 512  ASP B CA  1 
ATOM   3891 C C   . ASP A 1 514 ? 9.785   -40.971 24.256  1.00 28.37 ? 512  ASP B C   1 
ATOM   3892 O O   . ASP A 1 514 ? 9.722   -40.946 23.036  1.00 24.90 ? 512  ASP B O   1 
ATOM   3893 C CB  . ASP A 1 514 ? 9.805   -43.508 24.446  1.00 30.19 ? 512  ASP B CB  1 
ATOM   3894 C CG  . ASP A 1 514 ? 11.320  -43.578 24.380  1.00 28.94 ? 512  ASP B CG  1 
ATOM   3895 O OD1 . ASP A 1 514 ? 11.972  -42.756 25.028  1.00 27.03 ? 512  ASP B OD1 1 
ATOM   3896 O OD2 . ASP A 1 514 ? 11.821  -44.474 23.683  1.00 33.17 ? 512  ASP B OD2 1 
ATOM   3897 N N   . ARG A 1 515 ? 10.290  -39.994 24.996  1.00 27.52 ? 513  ARG B N   1 
ATOM   3898 C CA  . ARG A 1 515 ? 10.757  -38.728 24.369  1.00 30.23 ? 513  ARG B CA  1 
ATOM   3899 C C   . ARG A 1 515 ? 11.965  -38.974 23.432  1.00 26.23 ? 513  ARG B C   1 
ATOM   3900 O O   . ARG A 1 515 ? 12.225  -38.104 22.576  1.00 25.39 ? 513  ARG B O   1 
ATOM   3901 C CB  . ARG A 1 515 ? 11.122  -37.671 25.407  1.00 37.68 ? 513  ARG B CB  1 
ATOM   3902 C CG  . ARG A 1 515 ? 9.984   -37.264 26.332  1.00 49.56 ? 513  ARG B CG  1 
ATOM   3903 C CD  . ARG A 1 515 ? 8.949   -36.346 25.698  1.00 57.18 ? 513  ARG B CD  1 
ATOM   3904 N NE  . ARG A 1 515 ? 7.934   -35.949 26.676  1.00 67.06 ? 513  ARG B NE  1 
ATOM   3905 C CZ  . ARG A 1 515 ? 7.322   -34.760 26.731  1.00 74.01 ? 513  ARG B CZ  1 
ATOM   3906 N NH1 . ARG A 1 515 ? 7.607   -33.805 25.858  1.00 76.84 ? 513  ARG B NH1 1 
ATOM   3907 N NH2 . ARG A 1 515 ? 6.423   -34.525 27.674  1.00 73.82 ? 513  ARG B NH2 1 
ATOM   3908 N N   . GLU A 1 516 ? 12.671  -40.108 23.554  1.00 24.35 ? 514  GLU B N   1 
ATOM   3909 C CA  . GLU A 1 516 ? 13.820  -40.423 22.655  1.00 23.11 ? 514  GLU B CA  1 
ATOM   3910 C C   . GLU A 1 516 ? 13.285  -40.528 21.228  1.00 20.12 ? 514  GLU B C   1 
ATOM   3911 O O   . GLU A 1 516 ? 14.092  -40.370 20.274  1.00 19.03 ? 514  GLU B O   1 
ATOM   3912 C CB  . GLU A 1 516 ? 14.463  -41.785 22.947  1.00 24.80 ? 514  GLU B CB  1 
ATOM   3913 C CG  . GLU A 1 516 ? 15.058  -41.984 24.330  1.00 28.78 ? 514  GLU B CG  1 
ATOM   3914 C CD  . GLU A 1 516 ? 16.282  -41.175 24.650  1.00 30.07 ? 514  GLU B CD  1 
ATOM   3915 O OE1 . GLU A 1 516 ? 16.656  -40.323 23.801  1.00 31.09 ? 514  GLU B OE1 1 
ATOM   3916 O OE2 . GLU A 1 516 ? 16.877  -41.411 25.743  1.00 30.80 ? 514  GLU B OE2 1 
ATOM   3917 N N   . GLU A 1 517 ? 11.995  -40.847 21.079  1.00 19.95 ? 515  GLU B N   1 
ATOM   3918 C CA  . GLU A 1 517 ? 11.352  -41.006 19.758  1.00 20.10 ? 515  GLU B CA  1 
ATOM   3919 C C   . GLU A 1 517 ? 11.437  -39.700 18.949  1.00 18.95 ? 515  GLU B C   1 
ATOM   3920 O O   . GLU A 1 517 ? 11.431  -39.782 17.720  1.00 19.57 ? 515  GLU B O   1 
ATOM   3921 C CB  . GLU A 1 517 ? 9.920   -41.480 19.954  1.00 22.93 ? 515  GLU B CB  1 
ATOM   3922 C CG  . GLU A 1 517 ? 9.891   -42.951 20.319  1.00 26.51 ? 515  GLU B CG  1 
ATOM   3923 C CD  . GLU A 1 517 ? 10.135  -43.889 19.146  1.00 25.66 ? 515  GLU B CD  1 
ATOM   3924 O OE1 . GLU A 1 517 ? 10.112  -45.079 19.404  1.00 31.95 ? 515  GLU B OE1 1 
ATOM   3925 O OE2 . GLU A 1 517 ? 10.233  -43.427 17.943  1.00 36.69 ? 515  GLU B OE2 1 
ATOM   3926 N N   . VAL A 1 518 ? 11.495  -38.541 19.599  1.00 18.72 ? 516  VAL B N   1 
ATOM   3927 C CA  . VAL A 1 518 ? 11.627  -37.252 18.875  1.00 19.08 ? 516  VAL B CA  1 
ATOM   3928 C C   . VAL A 1 518 ? 12.971  -37.250 18.117  1.00 18.78 ? 516  VAL B C   1 
ATOM   3929 O O   . VAL A 1 518 ? 12.985  -37.057 16.894  1.00 19.66 ? 516  VAL B O   1 
ATOM   3930 C CB  . VAL A 1 518 ? 11.456  -36.059 19.833  1.00 20.82 ? 516  VAL B CB  1 
ATOM   3931 C CG1 . VAL A 1 518 ? 11.705  -34.746 19.114  1.00 22.05 ? 516  VAL B CG1 1 
ATOM   3932 C CG2 . VAL A 1 518 ? 10.070  -36.079 20.469  1.00 22.49 ? 516  VAL B CG2 1 
ATOM   3933 N N   . GLY A 1 519 ? 14.087  -37.494 18.796  1.00 18.19 ? 517  GLY B N   1 
ATOM   3934 C CA  . GLY A 1 519 ? 15.393  -37.534 18.118  1.00 17.12 ? 517  GLY B CA  1 
ATOM   3935 C C   . GLY A 1 519 ? 15.463  -38.686 17.150  1.00 16.77 ? 517  GLY B C   1 
ATOM   3936 O O   . GLY A 1 519 ? 16.019  -38.501 16.052  1.00 16.66 ? 517  GLY B O   1 
ATOM   3937 N N   . ALA A 1 520 ? 14.908  -39.844 17.508  1.00 16.67 ? 518  ALA B N   1 
ATOM   3938 C CA  . ALA A 1 520 ? 15.016  -41.057 16.675  1.00 16.74 ? 518  ALA B CA  1 
ATOM   3939 C C   . ALA A 1 520 ? 14.340  -40.843 15.306  1.00 18.10 ? 518  ALA B C   1 
ATOM   3940 O O   . ALA A 1 520 ? 14.869  -41.357 14.279  1.00 19.11 ? 518  ALA B O   1 
ATOM   3941 C CB  . ALA A 1 520 ? 14.427  -42.217 17.405  1.00 16.28 ? 518  ALA B CB  1 
ATOM   3942 N N   . ALA A 1 521 ? 13.218  -40.112 15.264  1.00 16.73 ? 519  ALA B N   1 
ATOM   3943 C CA  . ALA A 1 521 ? 12.421  -39.912 14.033  1.00 15.49 ? 519  ALA B CA  1 
ATOM   3944 C C   . ALA A 1 521 ? 12.873  -38.652 13.287  1.00 14.19 ? 519  ALA B C   1 
ATOM   3945 O O   . ALA A 1 521 ? 12.524  -38.518 12.086  1.00 14.00 ? 519  ALA B O   1 
ATOM   3946 C CB  . ALA A 1 521 ? 10.962  -39.808 14.353  1.00 16.97 ? 519  ALA B CB  1 
ATOM   3947 N N   . SER A 1 522 ? 13.604  -37.765 13.946  1.00 14.66 ? 520  SER B N   1 
ATOM   3948 C CA  . SER A 1 522 ? 13.751  -36.350 13.517  1.00 14.52 ? 520  SER B CA  1 
ATOM   3949 C C   . SER A 1 522 ? 14.321  -36.225 12.093  1.00 14.45 ? 520  SER B C   1 
ATOM   3950 O O   . SER A 1 522 ? 13.705  -35.583 11.248  1.00 13.57 ? 520  SER B O   1 
ATOM   3951 C CB  . SER A 1 522 ? 14.543  -35.544 14.498  1.00 14.65 ? 520  SER B CB  1 
ATOM   3952 O OG  . SER A 1 522 ? 15.839  -36.064 14.720  1.00 15.06 ? 520  SER B OG  1 
ATOM   3953 N N   . VAL A 1 523 ? 15.487  -36.797 11.808  1.00 14.13 ? 521  VAL B N   1 
ATOM   3954 C CA  . VAL A 1 523 ? 16.136  -36.495 10.496  1.00 14.02 ? 521  VAL B CA  1 
ATOM   3955 C C   . VAL A 1 523 ? 15.333  -37.177 9.389   1.00 14.42 ? 521  VAL B C   1 
ATOM   3956 O O   . VAL A 1 523 ? 15.111  -36.550 8.335   1.00 13.45 ? 521  VAL B O   1 
ATOM   3957 C CB  . VAL A 1 523 ? 17.629  -36.873 10.464  1.00 14.65 ? 521  VAL B CB  1 
ATOM   3958 C CG1 . VAL A 1 523 ? 18.179  -36.823 9.040   1.00 15.45 ? 521  VAL B CG1 1 
ATOM   3959 C CG2 . VAL A 1 523 ? 18.417  -35.974 11.387  1.00 14.28 ? 521  VAL B CG2 1 
ATOM   3960 N N   . ASP A 1 524 ? 14.805  -38.381 9.608   1.00 14.44 ? 522  ASP B N   1 
ATOM   3961 C CA  . ASP A 1 524 ? 13.956  -39.034 8.577   1.00 14.55 ? 522  ASP B CA  1 
ATOM   3962 C C   . ASP A 1 524 ? 12.689  -38.195 8.343   1.00 14.72 ? 522  ASP B C   1 
ATOM   3963 O O   . ASP A 1 524 ? 12.244  -38.118 7.168   1.00 14.54 ? 522  ASP B O   1 
ATOM   3964 C CB  . ASP A 1 524 ? 13.587  -40.464 8.957   1.00 14.81 ? 522  ASP B CB  1 
ATOM   3965 C CG  . ASP A 1 524 ? 14.762  -41.409 8.829   1.00 16.79 ? 522  ASP B CG  1 
ATOM   3966 O OD1 . ASP A 1 524 ? 15.327  -41.506 7.726   1.00 16.21 ? 522  ASP B OD1 1 
ATOM   3967 O OD2 . ASP A 1 524 ? 15.160  -41.997 9.859   1.00 16.98 ? 522  ASP B OD2 1 
ATOM   3968 N N   . TYR A 1 525 ? 12.117  -37.634 9.415   1.00 13.86 ? 523  TYR B N   1 
ATOM   3969 C CA  . TYR A 1 525 ? 10.871  -36.843 9.338   1.00 14.37 ? 523  TYR B CA  1 
ATOM   3970 C C   . TYR A 1 525 ? 11.160  -35.570 8.529   1.00 13.07 ? 523  TYR B C   1 
ATOM   3971 O O   . TYR A 1 525 ? 10.368  -35.212 7.627   1.00 14.59 ? 523  TYR B O   1 
ATOM   3972 C CB  . TYR A 1 525 ? 10.310  -36.540 10.724  1.00 14.98 ? 523  TYR B CB  1 
ATOM   3973 C CG  . TYR A 1 525 ? 9.009   -35.788 10.642  1.00 14.51 ? 523  TYR B CG  1 
ATOM   3974 C CD1 . TYR A 1 525 ? 7.815   -36.458 10.502  1.00 15.20 ? 523  TYR B CD1 1 
ATOM   3975 C CD2 . TYR A 1 525 ? 8.983   -34.407 10.596  1.00 15.34 ? 523  TYR B CD2 1 
ATOM   3976 C CE1 . TYR A 1 525 ? 6.611   -35.773 10.452  1.00 15.95 ? 523  TYR B CE1 1 
ATOM   3977 C CE2 . TYR A 1 525 ? 7.800   -33.699 10.479  1.00 15.28 ? 523  TYR B CE2 1 
ATOM   3978 C CZ  . TYR A 1 525 ? 6.604   -34.391 10.410  1.00 16.16 ? 523  TYR B CZ  1 
ATOM   3979 O OH  . TYR A 1 525 ? 5.395   -33.740 10.286  1.00 17.07 ? 523  TYR B OH  1 
ATOM   3980 N N   . LEU A 1 526 ? 12.318  -34.955 8.751   1.00 13.31 ? 524  LEU B N   1 
ATOM   3981 C CA  . LEU A 1 526 ? 12.657  -33.716 8.015   1.00 12.68 ? 524  LEU B CA  1 
ATOM   3982 C C   . LEU A 1 526 ? 12.882  -34.056 6.548   1.00 13.31 ? 524  LEU B C   1 
ATOM   3983 O O   . LEU A 1 526 ? 12.383  -33.335 5.666   1.00 13.39 ? 524  LEU B O   1 
ATOM   3984 C CB  . LEU A 1 526 ? 13.883  -33.033 8.588   1.00 13.52 ? 524  LEU B CB  1 
ATOM   3985 C CG  . LEU A 1 526 ? 14.213  -31.712 7.913   1.00 14.73 ? 524  LEU B CG  1 
ATOM   3986 C CD1 . LEU A 1 526 ? 14.731  -30.708 8.923   1.00 14.74 ? 524  LEU B CD1 1 
ATOM   3987 C CD2 . LEU A 1 526 ? 15.219  -31.894 6.765   1.00 14.10 ? 524  LEU B CD2 1 
ATOM   3988 N N   . MET A 1 527 ? 13.638  -35.098 6.257   1.00 13.44 ? 525  MET B N   1 
ATOM   3989 C CA  . MET A 1 527 ? 13.921  -35.419 4.834   1.00 13.47 ? 525  MET B CA  1 
ATOM   3990 C C   . MET A 1 527 ? 12.601  -35.780 4.149   1.00 12.99 ? 525  MET B C   1 
ATOM   3991 O O   . MET A 1 527 ? 12.398  -35.324 3.041   1.00 14.32 ? 525  MET B O   1 
ATOM   3992 C CB  . MET A 1 527 ? 14.932  -36.563 4.716   1.00 13.98 ? 525  MET B CB  1 
ATOM   3993 C CG  . MET A 1 527 ? 16.346  -36.196 5.164   1.00 14.37 ? 525  MET B CG  1 
ATOM   3994 S SD  . MET A 1 527 ? 17.044  -34.773 4.314   1.00 15.94 ? 525  MET B SD  1 
ATOM   3995 C CE  . MET A 1 527 ? 17.112  -35.379 2.647   1.00 16.76 ? 525  MET B CE  1 
ATOM   3996 N N   . TYR A 1 528 ? 11.767  -36.630 4.730   1.00 13.63 ? 526  TYR B N   1 
ATOM   3997 C CA  . TYR A 1 528 ? 10.425  -36.957 4.217   1.00 13.61 ? 526  TYR B CA  1 
ATOM   3998 C C   . TYR A 1 528 ? 9.683   -35.636 3.923   1.00 13.61 ? 526  TYR B C   1 
ATOM   3999 O O   . TYR A 1 528 ? 9.143   -35.474 2.789   1.00 14.18 ? 526  TYR B O   1 
ATOM   4000 C CB  . TYR A 1 528 ? 9.615   -37.729 5.246   1.00 13.88 ? 526  TYR B CB  1 
ATOM   4001 C CG  . TYR A 1 528 ? 8.212   -38.062 4.797   1.00 14.03 ? 526  TYR B CG  1 
ATOM   4002 C CD1 . TYR A 1 528 ? 7.193   -37.147 4.958   1.00 14.45 ? 526  TYR B CD1 1 
ATOM   4003 C CD2 . TYR A 1 528 ? 7.900   -39.283 4.261   1.00 13.43 ? 526  TYR B CD2 1 
ATOM   4004 C CE1 . TYR A 1 528 ? 5.916   -37.425 4.523   1.00 16.10 ? 526  TYR B CE1 1 
ATOM   4005 C CE2 . TYR A 1 528 ? 6.614   -39.605 3.857   1.00 14.36 ? 526  TYR B CE2 1 
ATOM   4006 C CZ  . TYR A 1 528 ? 5.617   -38.655 3.967   1.00 14.16 ? 526  TYR B CZ  1 
ATOM   4007 O OH  . TYR A 1 528 ? 4.327   -38.951 3.638   1.00 16.19 ? 526  TYR B OH  1 
ATOM   4008 N N   . SER A 1 529 ? 9.686   -34.712 4.878   1.00 14.54 ? 527  SER B N   1 
ATOM   4009 C CA  . SER A 1 529 ? 8.970   -33.407 4.733   1.00 13.33 ? 527  SER B CA  1 
ATOM   4010 C C   . SER A 1 529 ? 9.512   -32.641 3.519   1.00 15.28 ? 527  SER B C   1 
ATOM   4011 O O   . SER A 1 529 ? 8.710   -32.083 2.734   1.00 13.58 ? 527  SER B O   1 
ATOM   4012 C CB  . SER A 1 529 ? 9.051   -32.614 5.979   1.00 14.69 ? 527  SER B CB  1 
ATOM   4013 O OG  . SER A 1 529 ? 8.363   -33.256 7.027   1.00 14.77 ? 527  SER B OG  1 
ATOM   4014 N N   . GLY A 1 530 ? 10.847  -32.559 3.347   1.00 13.47 ? 528  GLY B N   1 
ATOM   4015 C CA  . GLY A 1 530 ? 11.409  -31.860 2.182   1.00 13.63 ? 528  GLY B CA  1 
ATOM   4016 C C   . GLY A 1 530 ? 11.001  -32.518 0.876   1.00 14.15 ? 528  GLY B C   1 
ATOM   4017 O O   . GLY A 1 530 ? 10.646  -31.818 -0.109  1.00 14.24 ? 528  GLY B O   1 
ATOM   4018 N N   . TYR A 1 531 ? 11.073  -33.857 0.786   1.00 13.62 ? 529  TYR B N   1 
ATOM   4019 C CA  . TYR A 1 531 ? 10.606  -34.590 -0.416  1.00 13.43 ? 529  TYR B CA  1 
ATOM   4020 C C   . TYR A 1 531 ? 9.120   -34.311 -0.707  1.00 14.39 ? 529  TYR B C   1 
ATOM   4021 O O   . TYR A 1 531 ? 8.774   -34.190 -1.878  1.00 13.35 ? 529  TYR B O   1 
ATOM   4022 C CB  . TYR A 1 531 ? 10.871  -36.095 -0.302  1.00 13.25 ? 529  TYR B CB  1 
ATOM   4023 C CG  . TYR A 1 531 ? 12.330  -36.469 -0.378  1.00 13.27 ? 529  TYR B CG  1 
ATOM   4024 C CD1 . TYR A 1 531 ? 13.119  -36.131 -1.485  1.00 13.19 ? 529  TYR B CD1 1 
ATOM   4025 C CD2 . TYR A 1 531 ? 12.946  -37.153 0.667   1.00 13.31 ? 529  TYR B CD2 1 
ATOM   4026 C CE1 . TYR A 1 531 ? 14.471  -36.464 -1.538  1.00 13.12 ? 529  TYR B CE1 1 
ATOM   4027 C CE2 . TYR A 1 531 ? 14.297  -37.490 0.624   1.00 12.25 ? 529  TYR B CE2 1 
ATOM   4028 C CZ  . TYR A 1 531 ? 15.066  -37.131 -0.470  1.00 13.99 ? 529  TYR B CZ  1 
ATOM   4029 O OH  . TYR A 1 531 ? 16.409  -37.435 -0.506  1.00 12.62 ? 529  TYR B OH  1 
ATOM   4030 N N   . ALA A 1 532 ? 8.288   -34.254 0.324   1.00 14.55 ? 530  ALA B N   1 
ATOM   4031 C CA  . ALA A 1 532 ? 6.840   -33.968 0.188   1.00 14.06 ? 530  ALA B CA  1 
ATOM   4032 C C   . ALA A 1 532 ? 6.650   -32.534 -0.298  1.00 14.83 ? 530  ALA B C   1 
ATOM   4033 O O   . ALA A 1 532 ? 5.804   -32.296 -1.177  1.00 14.95 ? 530  ALA B O   1 
ATOM   4034 C CB  . ALA A 1 532 ? 6.161   -34.187 1.509   1.00 14.84 ? 530  ALA B CB  1 
ATOM   4035 N N   . CYS A 1 533 ? 7.362   -31.583 0.276   1.00 14.05 ? 531  CYS B N   1 
ATOM   4036 C CA  . CYS A 1 533 ? 7.315   -30.171 -0.206  1.00 15.06 ? 531  CYS B CA  1 
ATOM   4037 C C   . CYS A 1 533 ? 7.650   -30.121 -1.699  1.00 16.44 ? 531  CYS B C   1 
ATOM   4038 O O   . CYS A 1 533 ? 6.907   -29.487 -2.490  1.00 14.75 ? 531  CYS B O   1 
ATOM   4039 C CB  . CYS A 1 533 ? 8.256   -29.276 0.568   1.00 15.04 ? 531  CYS B CB  1 
ATOM   4040 S SG  . CYS A 1 533 ? 7.737   -28.920 2.276   1.00 16.99 ? 531  CYS B SG  1 
ATOM   4041 N N   . LEU A 1 534 ? 8.726   -30.801 -2.125  1.00 15.11 ? 532  LEU B N   1 
ATOM   4042 C CA  . LEU A 1 534 ? 9.122   -30.746 -3.554  1.00 14.59 ? 532  LEU B CA  1 
ATOM   4043 C C   . LEU A 1 534 ? 8.111   -31.521 -4.403  1.00 14.99 ? 532  LEU B C   1 
ATOM   4044 O O   . LEU A 1 534 ? 7.971   -31.180 -5.593  1.00 14.23 ? 532  LEU B O   1 
ATOM   4045 C CB  . LEU A 1 534 ? 10.560  -31.236 -3.749  1.00 14.77 ? 532  LEU B CB  1 
ATOM   4046 C CG  . LEU A 1 534 ? 11.581  -30.106 -3.875  1.00 16.50 ? 532  LEU B CG  1 
ATOM   4047 C CD1 . LEU A 1 534 ? 11.587  -29.259 -2.653  1.00 17.26 ? 532  LEU B CD1 1 
ATOM   4048 C CD2 . LEU A 1 534 ? 12.970  -30.632 -4.204  1.00 16.08 ? 532  LEU B CD2 1 
ATOM   4049 N N   . ALA A 1 535 ? 7.469   -32.580 -3.891  1.00 14.21 ? 533  ALA B N   1 
ATOM   4050 C CA  . ALA A 1 535 ? 6.390   -33.234 -4.651  1.00 13.96 ? 533  ALA B CA  1 
ATOM   4051 C C   . ALA A 1 535 ? 5.314   -32.183 -4.963  1.00 13.35 ? 533  ALA B C   1 
ATOM   4052 O O   . ALA A 1 535 ? 4.821   -32.156 -6.110  1.00 14.48 ? 533  ALA B O   1 
ATOM   4053 C CB  . ALA A 1 535 ? 5.779   -34.392 -3.905  1.00 14.41 ? 533  ALA B CB  1 
ATOM   4054 N N   . TYR A 1 536 ? 4.906   -31.402 -3.986  1.00 14.24 ? 534  TYR B N   1 
ATOM   4055 C CA  . TYR A 1 536 ? 3.911   -30.327 -4.215  1.00 15.04 ? 534  TYR B CA  1 
ATOM   4056 C C   . TYR A 1 536 ? 4.440   -29.342 -5.261  1.00 14.88 ? 534  TYR B C   1 
ATOM   4057 O O   . TYR A 1 536 ? 3.786   -29.099 -6.260  1.00 16.10 ? 534  TYR B O   1 
ATOM   4058 C CB  . TYR A 1 536 ? 3.526   -29.616 -2.932  1.00 15.73 ? 534  TYR B CB  1 
ATOM   4059 C CG  . TYR A 1 536 ? 2.806   -28.319 -3.221  1.00 15.74 ? 534  TYR B CG  1 
ATOM   4060 C CD1 . TYR A 1 536 ? 1.522   -28.331 -3.742  1.00 16.86 ? 534  TYR B CD1 1 
ATOM   4061 C CD2 . TYR A 1 536 ? 3.451   -27.109 -3.102  1.00 16.83 ? 534  TYR B CD2 1 
ATOM   4062 C CE1 . TYR A 1 536 ? 0.880   -27.148 -4.103  1.00 16.54 ? 534  TYR B CE1 1 
ATOM   4063 C CE2 . TYR A 1 536 ? 2.825   -25.914 -3.436  1.00 17.40 ? 534  TYR B CE2 1 
ATOM   4064 C CZ  . TYR A 1 536 ? 1.533   -25.941 -3.947  1.00 19.72 ? 534  TYR B CZ  1 
ATOM   4065 O OH  . TYR A 1 536 ? 0.905   -24.746 -4.251  1.00 20.11 ? 534  TYR B OH  1 
ATOM   4066 N N   . PHE A 1 537 ? 5.625   -28.790 -5.079  1.00 13.77 ? 535  PHE B N   1 
ATOM   4067 C CA  . PHE A 1 537 ? 6.133   -27.761 -6.001  1.00 14.59 ? 535  PHE B CA  1 
ATOM   4068 C C   . PHE A 1 537 ? 6.301   -28.351 -7.404  1.00 14.73 ? 535  PHE B C   1 
ATOM   4069 O O   . PHE A 1 537 ? 5.997   -27.641 -8.383  1.00 14.87 ? 535  PHE B O   1 
ATOM   4070 C CB  . PHE A 1 537 ? 7.403   -27.099 -5.483  1.00 14.74 ? 535  PHE B CB  1 
ATOM   4071 C CG  . PHE A 1 537 ? 7.170   -26.220 -4.285  1.00 14.59 ? 535  PHE B CG  1 
ATOM   4072 C CD1 . PHE A 1 537 ? 6.358   -25.094 -4.384  1.00 17.11 ? 535  PHE B CD1 1 
ATOM   4073 C CD2 . PHE A 1 537 ? 7.681   -26.543 -3.053  1.00 17.10 ? 535  PHE B CD2 1 
ATOM   4074 C CE1 . PHE A 1 537 ? 6.085   -24.299 -3.284  1.00 17.76 ? 535  PHE B CE1 1 
ATOM   4075 C CE2 . PHE A 1 537 ? 7.418   -25.735 -1.951  1.00 17.24 ? 535  PHE B CE2 1 
ATOM   4076 C CZ  . PHE A 1 537 ? 6.615   -24.623 -2.067  1.00 17.85 ? 535  PHE B CZ  1 
ATOM   4077 N N   . TRP A 1 538 ? 6.785   -29.600 -7.544  1.00 14.24 ? 536  TRP B N   1 
ATOM   4078 C CA  . TRP A 1 538 ? 6.934   -30.204 -8.886  1.00 13.15 ? 536  TRP B CA  1 
ATOM   4079 C C   . TRP A 1 538 ? 5.557   -30.408 -9.522  1.00 14.11 ? 536  TRP B C   1 
ATOM   4080 O O   . TRP A 1 538 ? 5.477   -30.205 -10.756 1.00 15.81 ? 536  TRP B O   1 
ATOM   4081 C CB  . TRP A 1 538 ? 7.786   -31.479 -8.864  1.00 13.82 ? 536  TRP B CB  1 
ATOM   4082 C CG  . TRP A 1 538 ? 9.223   -31.119 -9.017  1.00 13.69 ? 536  TRP B CG  1 
ATOM   4083 C CD1 . TRP A 1 538 ? 10.260  -31.287 -8.142  1.00 14.00 ? 536  TRP B CD1 1 
ATOM   4084 C CD2 . TRP A 1 538 ? 9.775   -30.429 -10.156 1.00 14.00 ? 536  TRP B CD2 1 
ATOM   4085 N NE1 . TRP A 1 538 ? 11.409  -30.765 -8.669  1.00 15.60 ? 536  TRP B NE1 1 
ATOM   4086 C CE2 . TRP A 1 538 ? 11.145  -30.228 -9.904  1.00 13.94 ? 536  TRP B CE2 1 
ATOM   4087 C CE3 . TRP A 1 538 ? 9.262   -29.965 -11.378 1.00 14.22 ? 536  TRP B CE3 1 
ATOM   4088 C CZ2 . TRP A 1 538 ? 11.971  -29.546 -10.797 1.00 13.76 ? 536  TRP B CZ2 1 
ATOM   4089 C CZ3 . TRP A 1 538 ? 10.089  -29.309 -12.265 1.00 14.19 ? 536  TRP B CZ3 1 
ATOM   4090 C CH2 . TRP A 1 538 ? 11.424  -29.085 -11.972 1.00 13.86 ? 536  TRP B CH2 1 
ATOM   4091 N N   . ALA A 1 539 ? 4.572   -30.886 -8.768  1.00 14.57 ? 537  ALA B N   1 
ATOM   4092 C CA  . ALA A 1 539 ? 3.200   -31.076 -9.305  1.00 14.91 ? 537  ALA B CA  1 
ATOM   4093 C C   . ALA A 1 539 ? 2.645   -29.726 -9.770  1.00 16.12 ? 537  ALA B C   1 
ATOM   4094 O O   . ALA A 1 539 ? 2.020   -29.651 -10.875 1.00 16.28 ? 537  ALA B O   1 
ATOM   4095 C CB  . ALA A 1 539 ? 2.338   -31.739 -8.287  1.00 15.19 ? 537  ALA B CB  1 
ATOM   4096 N N   . ASP A 1 540 ? 2.909   -28.675 -9.015  1.00 15.59 ? 538  ASP B N   1 
ATOM   4097 C CA  . ASP A 1 540 ? 2.402   -27.315 -9.358  1.00 16.28 ? 538  ASP B CA  1 
ATOM   4098 C C   . ASP A 1 540 ? 3.138   -26.792 -10.582 1.00 18.08 ? 538  ASP B C   1 
ATOM   4099 O O   . ASP A 1 540 ? 2.487   -26.183 -11.455 1.00 18.03 ? 538  ASP B O   1 
ATOM   4100 C CB  . ASP A 1 540 ? 2.484   -26.338 -8.190  1.00 17.21 ? 538  ASP B CB  1 
ATOM   4101 C CG  . ASP A 1 540 ? 1.587   -25.108 -8.367  1.00 19.21 ? 538  ASP B CG  1 
ATOM   4102 O OD1 . ASP A 1 540 ? 0.533   -25.256 -8.992  1.00 20.63 ? 538  ASP B OD1 1 
ATOM   4103 O OD2 . ASP A 1 540 ? 1.975   -24.025 -7.896  1.00 22.24 ? 538  ASP B OD2 1 
ATOM   4104 N N   . MET A 1 541 ? 4.463   -26.980 -10.665 1.00 15.80 ? 539  MET B N   1 
ATOM   4105 C CA  . MET A 1 541 ? 5.190   -26.547 -11.869 1.00 16.96 ? 539  MET B CA  1 
ATOM   4106 C C   . MET A 1 541 ? 4.683   -27.333 -13.091 1.00 17.15 ? 539  MET B C   1 
ATOM   4107 O O   . MET A 1 541 ? 4.638   -26.763 -14.223 1.00 17.29 ? 539  MET B O   1 
ATOM   4108 C CB  . MET A 1 541 ? 6.703   -26.717 -11.679 1.00 16.64 ? 539  MET B CB  1 
ATOM   4109 C CG  . MET A 1 541 ? 7.238   -25.733 -10.672 1.00 16.00 ? 539  MET B CG  1 
ATOM   4110 S SD  . MET A 1 541 ? 9.024   -25.506 -10.611 1.00 17.25 ? 539  MET B SD  1 
ATOM   4111 C CE  . MET A 1 541 ? 9.506   -26.831 -9.514  1.00 17.87 ? 539  MET B CE  1 
ATOM   4112 N N   . ALA A 1 542 ? 4.401   -28.629 -12.956 1.00 16.32 ? 540  ALA B N   1 
ATOM   4113 C CA  . ALA A 1 542 ? 3.864   -29.448 -14.064 1.00 17.52 ? 540  ALA B CA  1 
ATOM   4114 C C   . ALA A 1 542 ? 2.493   -28.882 -14.480 1.00 18.18 ? 540  ALA B C   1 
ATOM   4115 O O   . ALA A 1 542 ? 2.237   -28.727 -15.694 1.00 18.51 ? 540  ALA B O   1 
ATOM   4116 C CB  . ALA A 1 542 ? 3.761   -30.884 -13.640 1.00 18.31 ? 540  ALA B CB  1 
ATOM   4117 N N   . ARG A 1 543 ? 1.658   -28.543 -13.515 1.00 17.57 ? 541  ARG B N   1 
ATOM   4118 C CA  . ARG A 1 543 ? 0.311   -27.957 -13.772 1.00 19.14 ? 541  ARG B CA  1 
ATOM   4119 C C   . ARG A 1 543 ? 0.490   -26.669 -14.580 1.00 17.51 ? 541  ARG B C   1 
ATOM   4120 O O   . ARG A 1 543 ? -0.152  -26.530 -15.678 1.00 19.89 ? 541  ARG B O   1 
ATOM   4121 C CB  . ARG A 1 543 ? -0.402  -27.688 -12.449 1.00 20.02 ? 541  ARG B CB  1 
ATOM   4122 C CG  . ARG A 1 543 ? -1.776  -27.040 -12.646 1.00 22.77 ? 541  ARG B CG  1 
ATOM   4123 C CD  . ARG A 1 543 ? -2.160  -26.129 -11.524 1.00 24.48 ? 541  ARG B CD  1 
ATOM   4124 N NE  . ARG A 1 543 ? -1.215  -25.049 -11.231 1.00 25.29 ? 541  ARG B NE  1 
ATOM   4125 C CZ  . ARG A 1 543 ? -1.101  -23.878 -11.837 1.00 28.65 ? 541  ARG B CZ  1 
ATOM   4126 N NH1 . ARG A 1 543 ? -1.832  -23.554 -12.892 1.00 34.66 ? 541  ARG B NH1 1 
ATOM   4127 N NH2 . ARG A 1 543 ? -0.222  -23.022 -11.379 1.00 30.38 ? 541  ARG B NH2 1 
ATOM   4128 N N   . LEU A 1 544 ? 1.355   -25.779 -14.113 1.00 16.53 ? 542  LEU B N   1 
ATOM   4129 C CA  . LEU A 1 544 ? 1.631   -24.494 -14.784 1.00 18.93 ? 542  LEU B CA  1 
ATOM   4130 C C   . LEU A 1 544 ? 2.212   -24.730 -16.186 1.00 19.40 ? 542  LEU B C   1 
ATOM   4131 O O   . LEU A 1 544 ? 1.741   -24.059 -17.147 1.00 19.70 ? 542  LEU B O   1 
ATOM   4132 C CB  . LEU A 1 544 ? 2.543   -23.644 -13.904 1.00 18.95 ? 542  LEU B CB  1 
ATOM   4133 C CG  . LEU A 1 544 ? 2.957   -22.306 -14.508 1.00 23.47 ? 542  LEU B CG  1 
ATOM   4134 C CD1 . LEU A 1 544 ? 1.727   -21.487 -14.877 1.00 25.12 ? 542  LEU B CD1 1 
ATOM   4135 C CD2 . LEU A 1 544 ? 3.852   -21.513 -13.555 1.00 25.26 ? 542  LEU B CD2 1 
ATOM   4136 N N   . ALA A 1 545 ? 3.167   -25.652 -16.349 1.00 17.55 ? 543  ALA B N   1 
ATOM   4137 C CA  . ALA A 1 545 ? 3.729   -25.990 -17.677 1.00 16.97 ? 543  ALA B CA  1 
ATOM   4138 C C   . ALA A 1 545 ? 2.591   -26.407 -18.625 1.00 20.01 ? 543  ALA B C   1 
ATOM   4139 O O   . ALA A 1 545 ? 2.610   -25.956 -19.788 1.00 19.29 ? 543  ALA B O   1 
ATOM   4140 C CB  . ALA A 1 545 ? 4.839   -27.021 -17.574 1.00 17.83 ? 543  ALA B CB  1 
ATOM   4141 N N   . ALA A 1 546 ? 1.681   -27.286 -18.209 1.00 19.75 ? 544  ALA B N   1 
ATOM   4142 C CA  . ALA A 1 546 ? 0.597   -27.772 -19.095 1.00 20.69 ? 544  ALA B CA  1 
ATOM   4143 C C   . ALA A 1 546 ? -0.319  -26.591 -19.468 1.00 22.09 ? 544  ALA B C   1 
ATOM   4144 O O   . ALA A 1 546 ? -0.785  -26.549 -20.637 1.00 23.45 ? 544  ALA B O   1 
ATOM   4145 C CB  . ALA A 1 546 ? -0.202  -28.864 -18.445 1.00 21.96 ? 544  ALA B CB  1 
ATOM   4146 N N   . GLU A 1 547 ? -0.564  -25.694 -18.525 1.00 21.63 ? 545  GLU B N   1 
ATOM   4147 C CA  . GLU A 1 547 ? -1.391  -24.481 -18.781 1.00 24.05 ? 545  GLU B CA  1 
ATOM   4148 C C   . GLU A 1 547 ? -0.713  -23.642 -19.878 1.00 23.91 ? 545  GLU B C   1 
ATOM   4149 O O   . GLU A 1 547 ? -1.407  -23.227 -20.863 1.00 23.78 ? 545  GLU B O   1 
ATOM   4150 C CB  . GLU A 1 547 ? -1.660  -23.788 -17.443 1.00 26.73 ? 545  GLU B CB  1 
ATOM   4151 C CG  . GLU A 1 547 ? -2.351  -22.444 -17.537 1.00 31.68 ? 545  GLU B CG  1 
ATOM   4152 C CD  . GLU A 1 547 ? -2.327  -21.760 -16.182 1.00 36.35 ? 545  GLU B CD  1 
ATOM   4153 O OE1 . GLU A 1 547 ? -2.875  -22.358 -15.229 1.00 40.86 ? 545  GLU B OE1 1 
ATOM   4154 O OE2 . GLU A 1 547 ? -1.692  -20.676 -16.066 1.00 45.30 ? 545  GLU B OE2 1 
ATOM   4155 N N   . LYS A 1 548 ? 0.605   -23.427 -19.796 1.00 20.55 ? 546  LYS B N   1 
ATOM   4156 C CA  . LYS A 1 548 ? 1.344   -22.564 -20.741 1.00 19.96 ? 546  LYS B CA  1 
ATOM   4157 C C   . LYS A 1 548 ? 1.327   -23.210 -22.126 1.00 21.42 ? 546  LYS B C   1 
ATOM   4158 O O   . LYS A 1 548 ? 1.214   -22.451 -23.143 1.00 20.84 ? 546  LYS B O   1 
ATOM   4159 C CB  . LYS A 1 548 ? 2.740   -22.255 -20.214 1.00 20.69 ? 546  LYS B CB  1 
ATOM   4160 C CG  . LYS A 1 548 ? 2.772   -21.333 -19.010 1.00 22.09 ? 546  LYS B CG  1 
ATOM   4161 C CD  . LYS A 1 548 ? 2.399   -19.903 -19.254 1.00 26.59 ? 546  LYS B CD  1 
ATOM   4162 C CE  . LYS A 1 548 ? 2.357   -19.120 -17.958 1.00 28.79 ? 546  LYS B CE  1 
ATOM   4163 N NZ  . LYS A 1 548 ? 2.179   -17.673 -18.196 1.00 32.89 ? 546  LYS B NZ  1 
ATOM   4164 N N   . LEU A 1 549 ? 1.452   -24.540 -22.196 1.00 19.70 ? 547  LEU B N   1 
ATOM   4165 C CA  . LEU A 1 549 ? 1.442   -25.261 -23.473 1.00 20.65 ? 547  LEU B CA  1 
ATOM   4166 C C   . LEU A 1 549 ? 0.033   -25.129 -24.080 1.00 21.84 ? 547  LEU B C   1 
ATOM   4167 O O   . LEU A 1 549 ? -0.042  -24.872 -25.293 1.00 23.58 ? 547  LEU B O   1 
ATOM   4168 C CB  . LEU A 1 549 ? 1.868   -26.704 -23.266 1.00 22.11 ? 547  LEU B CB  1 
ATOM   4169 C CG  . LEU A 1 549 ? 3.350   -26.860 -22.902 1.00 22.15 ? 547  LEU B CG  1 
ATOM   4170 C CD1 . LEU A 1 549 ? 3.630   -28.269 -22.384 1.00 22.68 ? 547  LEU B CD1 1 
ATOM   4171 C CD2 . LEU A 1 549 ? 4.251   -26.515 -24.078 1.00 21.85 ? 547  LEU B CD2 1 
ATOM   4172 N N   . ALA A 1 550 ? -1.016  -25.257 -23.281 1.00 22.75 ? 548  ALA B N   1 
ATOM   4173 C CA  . ALA A 1 550 ? -2.427  -25.130 -23.745 1.00 24.74 ? 548  ALA B CA  1 
ATOM   4174 C C   . ALA A 1 550 ? -2.671  -23.702 -24.248 1.00 24.14 ? 548  ALA B C   1 
ATOM   4175 O O   . ALA A 1 550 ? -3.455  -23.535 -25.199 1.00 23.94 ? 548  ALA B O   1 
ATOM   4176 C CB  . ALA A 1 550 ? -3.393  -25.491 -22.648 1.00 24.49 ? 548  ALA B CB  1 
ATOM   4177 N N   . ALA A 1 551 ? -2.033  -22.708 -23.647 1.00 22.29 ? 549  ALA B N   1 
ATOM   4178 C CA  . ALA A 1 551 ? -2.182  -21.274 -24.011 1.00 24.03 ? 549  ALA B CA  1 
ATOM   4179 C C   . ALA A 1 551 ? -1.422  -20.954 -25.304 1.00 27.83 ? 549  ALA B C   1 
ATOM   4180 O O   . ALA A 1 551 ? -1.637  -19.855 -25.845 1.00 29.31 ? 549  ALA B O   1 
ATOM   4181 C CB  . ALA A 1 551 ? -1.714  -20.386 -22.892 1.00 25.99 ? 549  ALA B CB  1 
ATOM   4182 N N   . GLY A 1 552 ? -0.505  -21.814 -25.741 1.00 27.53 ? 550  GLY B N   1 
ATOM   4183 C CA  . GLY A 1 552 ? 0.217   -21.657 -27.020 1.00 28.09 ? 550  GLY B CA  1 
ATOM   4184 C C   . GLY A 1 552 ? 1.451   -20.799 -26.879 1.00 34.49 ? 550  GLY B C   1 
ATOM   4185 O O   . GLY A 1 552 ? 1.792   -20.051 -27.790 1.00 36.30 ? 550  GLY B O   1 
ATOM   4186 N N   . THR A 1 553 ? 2.150   -20.957 -25.768 1.00 39.69 ? 551  THR B N   1 
ATOM   4187 C CA  . THR A 1 553 ? 3.493   -20.385 -25.521 1.00 35.11 ? 551  THR B CA  1 
ATOM   4188 C C   . THR A 1 553 ? 4.418   -20.530 -26.736 1.00 32.78 ? 551  THR B C   1 
ATOM   4189 O O   . THR A 1 553 ? 4.413   -21.607 -27.382 1.00 35.13 ? 551  THR B O   1 
ATOM   4190 C CB  . THR A 1 553 ? 4.139   -21.099 -24.329 1.00 33.83 ? 551  THR B CB  1 
ATOM   4191 O OG1 . THR A 1 553 ? 5.401   -20.456 -24.203 1.00 34.29 ? 551  THR B OG1 1 
ATOM   4192 C CG2 . THR A 1 553 ? 4.273   -22.595 -24.535 1.00 31.59 ? 551  THR B CG2 1 
ATOM   4193 N N   . GLY A 1 554 ? 5.283   -19.538 -26.956 1.00 30.43 ? 552  GLY B N   1 
ATOM   4194 C CA  . GLY A 1 554 ? 6.411   -19.653 -27.903 1.00 30.44 ? 552  GLY B CA  1 
ATOM   4195 C C   . GLY A 1 554 ? 7.637   -20.310 -27.276 1.00 31.90 ? 552  GLY B C   1 
ATOM   4196 O O   . GLY A 1 554 ? 8.634   -20.495 -27.980 1.00 32.96 ? 552  GLY B O   1 
ATOM   4197 N N   . GLU A 1 555 ? 7.582   -20.664 -25.992 1.00 26.88 ? 553  GLU B N   1 
ATOM   4198 C CA  . GLU A 1 555 ? 8.711   -21.351 -25.293 1.00 27.21 ? 553  GLU B CA  1 
ATOM   4199 C C   . GLU A 1 555 ? 8.306   -22.794 -24.968 1.00 24.25 ? 553  GLU B C   1 
ATOM   4200 O O   . GLU A 1 555 ? 8.425   -23.217 -23.779 1.00 21.91 ? 553  GLU B O   1 
ATOM   4201 C CB  . GLU A 1 555 ? 9.020   -20.558 -24.033 1.00 27.95 ? 553  GLU B CB  1 
ATOM   4202 C CG  . GLU A 1 555 ? 9.776   -19.289 -24.321 1.00 29.69 ? 553  GLU B CG  1 
ATOM   4203 C CD  . GLU A 1 555 ? 10.143  -18.564 -23.047 1.00 32.30 ? 553  GLU B CD  1 
ATOM   4204 O OE1 . GLU A 1 555 ? 11.275  -18.757 -22.590 1.00 29.84 ? 553  GLU B OE1 1 
ATOM   4205 O OE2 . GLU A 1 555 ? 9.284   -17.854 -22.500 1.00 30.63 ? 553  GLU B OE2 1 
ATOM   4206 N N   . GLU A 1 556 ? 7.819   -23.535 -25.961 1.00 22.68 ? 554  GLU B N   1 
ATOM   4207 C CA  . GLU A 1 556 ? 7.296   -24.908 -25.757 1.00 23.19 ? 554  GLU B CA  1 
ATOM   4208 C C   . GLU A 1 556 ? 8.328   -25.775 -25.006 1.00 20.65 ? 554  GLU B C   1 
ATOM   4209 O O   . GLU A 1 556 ? 7.948   -26.442 -24.045 1.00 22.01 ? 554  GLU B O   1 
ATOM   4210 C CB  . GLU A 1 556 ? 6.976   -25.564 -27.104 1.00 28.06 ? 554  GLU B CB  1 
ATOM   4211 C CG  . GLU A 1 556 ? 5.665   -25.064 -27.664 1.00 35.93 ? 554  GLU B CG  1 
ATOM   4212 C CD  . GLU A 1 556 ? 5.290   -25.650 -29.018 1.00 40.97 ? 554  GLU B CD  1 
ATOM   4213 O OE1 . GLU A 1 556 ? 4.243   -25.231 -29.567 1.00 48.12 ? 554  GLU B OE1 1 
ATOM   4214 O OE2 . GLU A 1 556 ? 6.035   -26.519 -29.514 1.00 41.95 ? 554  GLU B OE2 1 
ATOM   4215 N N   . ALA A 1 557 ? 9.565   -25.769 -25.448 1.00 18.61 ? 555  ALA B N   1 
ATOM   4216 C CA  . ALA A 1 557 ? 10.628  -26.664 -24.912 1.00 19.72 ? 555  ALA B CA  1 
ATOM   4217 C C   . ALA A 1 557 ? 10.840  -26.401 -23.413 1.00 19.78 ? 555  ALA B C   1 
ATOM   4218 O O   . ALA A 1 557 ? 11.036  -27.353 -22.681 1.00 19.35 ? 555  ALA B O   1 
ATOM   4219 C CB  . ALA A 1 557 ? 11.907  -26.491 -25.688 1.00 22.19 ? 555  ALA B CB  1 
ATOM   4220 N N   . PHE A 1 558 ? 10.808  -25.149 -22.985 1.00 19.19 ? 556  PHE B N   1 
ATOM   4221 C CA  . PHE A 1 558 ? 11.039  -24.806 -21.557 1.00 18.09 ? 556  PHE B CA  1 
ATOM   4222 C C   . PHE A 1 558 ? 9.997   -25.507 -20.680 1.00 19.54 ? 556  PHE B C   1 
ATOM   4223 O O   . PHE A 1 558 ? 10.357  -26.087 -19.655 1.00 18.57 ? 556  PHE B O   1 
ATOM   4224 C CB  . PHE A 1 558 ? 11.035  -23.281 -21.367 1.00 17.33 ? 556  PHE B CB  1 
ATOM   4225 C CG  . PHE A 1 558 ? 11.166  -22.861 -19.928 1.00 17.63 ? 556  PHE B CG  1 
ATOM   4226 C CD1 . PHE A 1 558 ? 10.049  -22.729 -19.122 1.00 18.67 ? 556  PHE B CD1 1 
ATOM   4227 C CD2 . PHE A 1 558 ? 12.411  -22.636 -19.370 1.00 16.45 ? 556  PHE B CD2 1 
ATOM   4228 C CE1 . PHE A 1 558 ? 10.175  -22.366 -17.793 1.00 18.86 ? 556  PHE B CE1 1 
ATOM   4229 C CE2 . PHE A 1 558 ? 12.535  -22.268 -18.042 1.00 16.89 ? 556  PHE B CE2 1 
ATOM   4230 C CZ  . PHE A 1 558 ? 11.418  -22.134 -17.256 1.00 19.07 ? 556  PHE B CZ  1 
ATOM   4231 N N   . TYR A 1 559 ? 8.739   -25.428 -21.078 1.00 17.78 ? 557  TYR B N   1 
ATOM   4232 C CA  . TYR A 1 559 ? 7.618   -26.014 -20.306 1.00 16.61 ? 557  TYR B CA  1 
ATOM   4233 C C   . TYR A 1 559 ? 7.610   -27.541 -20.466 1.00 17.98 ? 557  TYR B C   1 
ATOM   4234 O O   . TYR A 1 559 ? 7.300   -28.259 -19.508 1.00 17.83 ? 557  TYR B O   1 
ATOM   4235 C CB  . TYR A 1 559 ? 6.317   -25.315 -20.733 1.00 16.80 ? 557  TYR B CB  1 
ATOM   4236 C CG  . TYR A 1 559 ? 6.321   -23.846 -20.408 1.00 18.48 ? 557  TYR B CG  1 
ATOM   4237 C CD1 . TYR A 1 559 ? 6.285   -23.410 -19.098 1.00 18.17 ? 557  TYR B CD1 1 
ATOM   4238 C CD2 . TYR A 1 559 ? 6.359   -22.873 -21.402 1.00 21.22 ? 557  TYR B CD2 1 
ATOM   4239 C CE1 . TYR A 1 559 ? 6.349   -22.071 -18.763 1.00 19.29 ? 557  TYR B CE1 1 
ATOM   4240 C CE2 . TYR A 1 559 ? 6.420   -21.525 -21.089 1.00 21.21 ? 557  TYR B CE2 1 
ATOM   4241 C CZ  . TYR A 1 559 ? 6.372   -21.117 -19.771 1.00 21.78 ? 557  TYR B CZ  1 
ATOM   4242 O OH  . TYR A 1 559 ? 6.416   -19.791 -19.427 1.00 21.87 ? 557  TYR B OH  1 
ATOM   4243 N N   . LYS A 1 560 ? 7.892   -28.060 -21.647 1.00 17.89 ? 558  LYS B N   1 
ATOM   4244 C CA  . LYS A 1 560 ? 7.988   -29.538 -21.830 1.00 18.72 ? 558  LYS B CA  1 
ATOM   4245 C C   . LYS A 1 560 ? 9.087   -30.097 -20.912 1.00 17.15 ? 558  LYS B C   1 
ATOM   4246 O O   . LYS A 1 560 ? 8.886   -31.187 -20.352 1.00 17.21 ? 558  LYS B O   1 
ATOM   4247 C CB  . LYS A 1 560 ? 8.234   -29.865 -23.297 1.00 20.58 ? 558  LYS B CB  1 
ATOM   4248 C CG  . LYS A 1 560 ? 6.942   -29.759 -24.107 1.00 23.87 ? 558  LYS B CG  1 
ATOM   4249 C CD  . LYS A 1 560 ? 7.110   -29.971 -25.594 1.00 28.58 ? 558  LYS B CD  1 
ATOM   4250 C CE  . LYS A 1 560 ? 5.773   -29.875 -26.311 1.00 32.86 ? 558  LYS B CE  1 
ATOM   4251 N NZ  . LYS A 1 560 ? 5.956   -29.985 -27.777 1.00 39.29 ? 558  LYS B NZ  1 
ATOM   4252 N N   . ALA A 1 561 ? 10.176  -29.368 -20.733 1.00 17.89 ? 559  ALA B N   1 
ATOM   4253 C CA  . ALA A 1 561 ? 11.268  -29.848 -19.857 1.00 15.95 ? 559  ALA B CA  1 
ATOM   4254 C C   . ALA A 1 561 ? 10.796  -29.874 -18.400 1.00 15.79 ? 559  ALA B C   1 
ATOM   4255 O O   . ALA A 1 561 ? 11.205  -30.767 -17.675 1.00 17.49 ? 559  ALA B O   1 
ATOM   4256 C CB  . ALA A 1 561 ? 12.468  -28.970 -20.047 1.00 17.43 ? 559  ALA B CB  1 
ATOM   4257 N N   . LYS A 1 562 ? 9.984   -28.899 -18.005 1.00 16.29 ? 560  LYS B N   1 
ATOM   4258 C CA  . LYS A 1 562 ? 9.416   -28.884 -16.630 1.00 16.40 ? 560  LYS B CA  1 
ATOM   4259 C C   . LYS A 1 562 ? 8.600   -30.168 -16.398 1.00 15.68 ? 560  LYS B C   1 
ATOM   4260 O O   . LYS A 1 562 ? 8.707   -30.738 -15.321 1.00 16.09 ? 560  LYS B O   1 
ATOM   4261 C CB  . LYS A 1 562 ? 8.578   -27.616 -16.396 1.00 16.49 ? 560  LYS B CB  1 
ATOM   4262 C CG  . LYS A 1 562 ? 9.364   -26.327 -16.220 1.00 18.20 ? 560  LYS B CG  1 
ATOM   4263 C CD  . LYS A 1 562 ? 10.079  -26.236 -14.893 1.00 16.95 ? 560  LYS B CD  1 
ATOM   4264 C CE  . LYS A 1 562 ? 10.969  -25.018 -14.802 1.00 16.82 ? 560  LYS B CE  1 
ATOM   4265 N NZ  . LYS A 1 562 ? 11.723  -24.978 -13.529 1.00 17.12 ? 560  LYS B NZ  1 
ATOM   4266 N N   . LEU A 1 563 ? 7.769   -30.550 -17.373 1.00 16.69 ? 561  LEU B N   1 
ATOM   4267 C CA  . LEU A 1 563 ? 6.969   -31.771 -17.238 1.00 16.87 ? 561  LEU B CA  1 
ATOM   4268 C C   . LEU A 1 563 ? 7.881   -33.009 -17.151 1.00 16.76 ? 561  LEU B C   1 
ATOM   4269 O O   . LEU A 1 563 ? 7.570   -33.908 -16.335 1.00 17.22 ? 561  LEU B O   1 
ATOM   4270 C CB  . LEU A 1 563 ? 5.967   -31.876 -18.388 1.00 18.27 ? 561  LEU B CB  1 
ATOM   4271 C CG  . LEU A 1 563 ? 4.762   -30.953 -18.245 1.00 18.56 ? 561  LEU B CG  1 
ATOM   4272 C CD1 . LEU A 1 563 ? 4.117   -30.700 -19.604 1.00 21.33 ? 561  LEU B CD1 1 
ATOM   4273 C CD2 . LEU A 1 563 ? 3.765   -31.570 -17.309 1.00 19.71 ? 561  LEU B CD2 1 
ATOM   4274 N N   . GLN A 1 564 ? 8.975   -33.057 -17.914 1.00 15.52 ? 562  GLN B N   1 
ATOM   4275 C CA  . GLN A 1 564 ? 9.905   -34.219 -17.859 1.00 17.09 ? 562  GLN B CA  1 
ATOM   4276 C C   . GLN A 1 564 ? 10.568  -34.269 -16.481 1.00 16.37 ? 562  GLN B C   1 
ATOM   4277 O O   . GLN A 1 564 ? 10.708  -35.364 -15.925 1.00 16.39 ? 562  GLN B O   1 
ATOM   4278 C CB  . GLN A 1 564 ? 10.961  -34.120 -18.952 1.00 17.69 ? 562  GLN B CB  1 
ATOM   4279 C CG  . GLN A 1 564 ? 10.372  -34.279 -20.347 1.00 18.81 ? 562  GLN B CG  1 
ATOM   4280 C CD  . GLN A 1 564 ? 9.947   -35.695 -20.592 1.00 22.59 ? 562  GLN B CD  1 
ATOM   4281 O OE1 . GLN A 1 564 ? 10.616  -36.649 -20.161 1.00 25.54 ? 562  GLN B OE1 1 
ATOM   4282 N NE2 . GLN A 1 564 ? 8.813   -35.844 -21.250 1.00 24.28 ? 562  GLN B NE2 1 
ATOM   4283 N N   . THR A 1 565 ? 11.022  -33.126 -15.992 1.00 15.19 ? 563  THR B N   1 
ATOM   4284 C CA  . THR A 1 565 ? 11.729  -33.060 -14.685 1.00 15.29 ? 563  THR B CA  1 
ATOM   4285 C C   . THR A 1 565 ? 10.760  -33.484 -13.573 1.00 16.32 ? 563  THR B C   1 
ATOM   4286 O O   . THR A 1 565 ? 11.148  -34.202 -12.631 1.00 16.38 ? 563  THR B O   1 
ATOM   4287 C CB  . THR A 1 565 ? 12.347  -31.680 -14.465 1.00 15.85 ? 563  THR B CB  1 
ATOM   4288 O OG1 . THR A 1 565 ? 13.149  -31.271 -15.583 1.00 16.07 ? 563  THR B OG1 1 
ATOM   4289 C CG2 . THR A 1 565 ? 13.222  -31.689 -13.232 1.00 15.44 ? 563  THR B CG2 1 
ATOM   4290 N N   . ALA A 1 566 ? 9.529   -33.000 -13.619 1.00 15.39 ? 564  ALA B N   1 
ATOM   4291 C CA  . ALA A 1 566 ? 8.496   -33.328 -12.625 1.00 14.95 ? 564  ALA B CA  1 
ATOM   4292 C C   . ALA A 1 566 ? 8.258   -34.836 -12.631 1.00 15.06 ? 564  ALA B C   1 
ATOM   4293 O O   . ALA A 1 566 ? 8.243   -35.452 -11.547 1.00 15.48 ? 564  ALA B O   1 
ATOM   4294 C CB  . ALA A 1 566 ? 7.221   -32.532 -12.902 1.00 15.15 ? 564  ALA B CB  1 
ATOM   4295 N N   . ARG A 1 567 ? 8.178   -35.454 -13.807 1.00 14.70 ? 565  ARG B N   1 
ATOM   4296 C CA  . ARG A 1 567 ? 7.928   -36.912 -13.866 1.00 16.70 ? 565  ARG B CA  1 
ATOM   4297 C C   . ARG A 1 567 ? 9.148   -37.681 -13.320 1.00 15.72 ? 565  ARG B C   1 
ATOM   4298 O O   . ARG A 1 567 ? 8.974   -38.628 -12.522 1.00 15.60 ? 565  ARG B O   1 
ATOM   4299 C CB  . ARG A 1 567 ? 7.590   -37.362 -15.286 1.00 17.93 ? 565  ARG B CB  1 
ATOM   4300 C CG  . ARG A 1 567 ? 7.424   -38.865 -15.340 1.00 19.81 ? 565  ARG B CG  1 
ATOM   4301 C CD  . ARG A 1 567 ? 6.974   -39.374 -16.709 1.00 21.61 ? 565  ARG B CD  1 
ATOM   4302 N NE  . ARG A 1 567 ? 8.013   -39.071 -17.682 1.00 25.15 ? 565  ARG B NE  1 
ATOM   4303 C CZ  . ARG A 1 567 ? 8.056   -39.541 -18.924 1.00 28.44 ? 565  ARG B CZ  1 
ATOM   4304 N NH1 . ARG A 1 567 ? 7.129   -40.388 -19.340 1.00 30.15 ? 565  ARG B NH1 1 
ATOM   4305 N NH2 . ARG A 1 567 ? 9.047   -39.188 -19.728 1.00 28.14 ? 565  ARG B NH2 1 
ATOM   4306 N N   . PHE A 1 568 ? 10.357  -37.230 -13.631 1.00 15.29 ? 566  PHE B N   1 
ATOM   4307 C CA  . PHE A 1 568 ? 11.605  -37.825 -13.102 1.00 15.30 ? 566  PHE B CA  1 
ATOM   4308 C C   . PHE A 1 568 ? 11.595  -37.746 -11.577 1.00 15.56 ? 566  PHE B C   1 
ATOM   4309 O O   . PHE A 1 568 ? 11.809  -38.748 -10.910 1.00 15.08 ? 566  PHE B O   1 
ATOM   4310 C CB  . PHE A 1 568 ? 12.824  -37.148 -13.714 1.00 15.08 ? 566  PHE B CB  1 
ATOM   4311 C CG  . PHE A 1 568 ? 14.079  -37.543 -12.987 1.00 15.57 ? 566  PHE B CG  1 
ATOM   4312 C CD1 . PHE A 1 568 ? 14.759  -38.694 -13.348 1.00 17.09 ? 566  PHE B CD1 1 
ATOM   4313 C CD2 . PHE A 1 568 ? 14.486  -36.830 -11.867 1.00 15.70 ? 566  PHE B CD2 1 
ATOM   4314 C CE1 . PHE A 1 568 ? 15.862  -39.107 -12.614 1.00 17.12 ? 566  PHE B CE1 1 
ATOM   4315 C CE2 . PHE A 1 568 ? 15.613  -37.218 -11.170 1.00 15.57 ? 566  PHE B CE2 1 
ATOM   4316 C CZ  . PHE A 1 568 ? 16.278  -38.354 -11.529 1.00 15.37 ? 566  PHE B CZ  1 
ATOM   4317 N N   . TYR A 1 569 ? 11.264  -36.586 -11.027 1.00 13.73 ? 567  TYR B N   1 
ATOM   4318 C CA  . TYR A 1 569 ? 11.201  -36.402 -9.561  1.00 14.59 ? 567  TYR B CA  1 
ATOM   4319 C C   . TYR A 1 569 ? 10.248  -37.409 -8.934  1.00 14.48 ? 567  TYR B C   1 
ATOM   4320 O O   . TYR A 1 569 ? 10.600  -38.139 -7.987  1.00 15.30 ? 567  TYR B O   1 
ATOM   4321 C CB  . TYR A 1 569 ? 10.833  -34.962 -9.180  1.00 14.55 ? 567  TYR B CB  1 
ATOM   4322 C CG  . TYR A 1 569 ? 10.788  -34.800 -7.687  1.00 13.23 ? 567  TYR B CG  1 
ATOM   4323 C CD1 . TYR A 1 569 ? 11.977  -34.644 -6.993  1.00 14.13 ? 567  TYR B CD1 1 
ATOM   4324 C CD2 . TYR A 1 569 ? 9.608   -34.903 -6.963  1.00 14.39 ? 567  TYR B CD2 1 
ATOM   4325 C CE1 . TYR A 1 569 ? 11.983  -34.568 -5.605  1.00 14.17 ? 567  TYR B CE1 1 
ATOM   4326 C CE2 . TYR A 1 569 ? 9.597   -34.808 -5.579  1.00 14.41 ? 567  TYR B CE2 1 
ATOM   4327 C CZ  . TYR A 1 569 ? 10.796  -34.641 -4.897  1.00 13.50 ? 567  TYR B CZ  1 
ATOM   4328 O OH  . TYR A 1 569 ? 10.868  -34.614 -3.527  1.00 13.89 ? 567  TYR B OH  1 
ATOM   4329 N N   . PHE A 1 570 ? 9.026   -37.493 -9.429  1.00 14.41 ? 568  PHE B N   1 
ATOM   4330 C CA  . PHE A 1 570 ? 8.004   -38.366 -8.821  1.00 14.75 ? 568  PHE B CA  1 
ATOM   4331 C C   . PHE A 1 570 ? 8.394   -39.848 -8.933  1.00 15.21 ? 568  PHE B C   1 
ATOM   4332 O O   . PHE A 1 570 ? 8.069   -40.651 -8.039  1.00 16.40 ? 568  PHE B O   1 
ATOM   4333 C CB  . PHE A 1 570 ? 6.633   -38.120 -9.451  1.00 15.57 ? 568  PHE B CB  1 
ATOM   4334 C CG  . PHE A 1 570 ? 5.821   -37.089 -8.713  1.00 14.62 ? 568  PHE B CG  1 
ATOM   4335 C CD1 . PHE A 1 570 ? 6.107   -35.740 -8.861  1.00 15.83 ? 568  PHE B CD1 1 
ATOM   4336 C CD2 . PHE A 1 570 ? 4.756   -37.456 -7.913  1.00 16.35 ? 568  PHE B CD2 1 
ATOM   4337 C CE1 . PHE A 1 570 ? 5.400   -34.777 -8.160  1.00 15.91 ? 568  PHE B CE1 1 
ATOM   4338 C CE2 . PHE A 1 570 ? 4.034   -36.486 -7.212  1.00 15.21 ? 568  PHE B CE2 1 
ATOM   4339 C CZ  . PHE A 1 570 ? 4.364   -35.160 -7.334  1.00 15.99 ? 568  PHE B CZ  1 
ATOM   4340 N N   . GLN A 1 571 ? 8.975   -40.260 -10.039 1.00 15.66 ? 569  GLN B N   1 
ATOM   4341 C CA  . GLN A 1 571 ? 9.185   -41.704 -10.344 1.00 15.73 ? 569  GLN B CA  1 
ATOM   4342 C C   . GLN A 1 571 ? 10.511  -42.213 -9.757  1.00 16.55 ? 569  GLN B C   1 
ATOM   4343 O O   . GLN A 1 571 ? 10.600  -43.414 -9.447  1.00 16.43 ? 569  GLN B O   1 
ATOM   4344 C CB  . GLN A 1 571 ? 9.085   -41.922 -11.859 1.00 16.44 ? 569  GLN B CB  1 
ATOM   4345 C CG  . GLN A 1 571 ? 7.656   -41.664 -12.314 1.00 18.58 ? 569  GLN B CG  1 
ATOM   4346 C CD  . GLN A 1 571 ? 7.349   -42.109 -13.718 1.00 19.43 ? 569  GLN B CD  1 
ATOM   4347 O OE1 . GLN A 1 571 ? 8.196   -42.594 -14.455 1.00 20.78 ? 569  GLN B OE1 1 
ATOM   4348 N NE2 . GLN A 1 571 ? 6.108   -41.865 -14.109 1.00 23.02 ? 569  GLN B NE2 1 
ATOM   4349 N N   . ARG A 1 572 ? 11.514  -41.359 -9.621  1.00 14.92 ? 570  ARG B N   1 
ATOM   4350 C CA  . ARG A 1 572 ? 12.882  -41.828 -9.237  1.00 16.11 ? 570  ARG B CA  1 
ATOM   4351 C C   . ARG A 1 572 ? 13.394  -41.183 -7.940  1.00 17.58 ? 570  ARG B C   1 
ATOM   4352 O O   . ARG A 1 572 ? 14.275  -41.777 -7.296  1.00 19.13 ? 570  ARG B O   1 
ATOM   4353 C CB  . ARG A 1 572 ? 13.880  -41.623 -10.366 1.00 15.55 ? 570  ARG B CB  1 
ATOM   4354 C CG  . ARG A 1 572 ? 13.664  -42.572 -11.542 1.00 15.35 ? 570  ARG B CG  1 
ATOM   4355 C CD  . ARG A 1 572 ? 14.674  -42.433 -12.629 1.00 16.40 ? 570  ARG B CD  1 
ATOM   4356 N NE  . ARG A 1 572 ? 14.425  -43.405 -13.690 1.00 16.22 ? 570  ARG B NE  1 
ATOM   4357 C CZ  . ARG A 1 572 ? 14.984  -44.582 -13.805 1.00 18.10 ? 570  ARG B CZ  1 
ATOM   4358 N NH1 . ARG A 1 572 ? 15.906  -44.986 -12.949 1.00 18.85 ? 570  ARG B NH1 1 
ATOM   4359 N NH2 . ARG A 1 572 ? 14.637  -45.338 -14.816 1.00 19.91 ? 570  ARG B NH2 1 
ATOM   4360 N N   . ILE A 1 573 ? 12.914  -40.016 -7.542  1.00 15.12 ? 571  ILE B N   1 
ATOM   4361 C CA  . ILE A 1 573 ? 13.445  -39.389 -6.293  1.00 14.18 ? 571  ILE B CA  1 
ATOM   4362 C C   . ILE A 1 573 ? 12.431  -39.544 -5.159  1.00 13.61 ? 571  ILE B C   1 
ATOM   4363 O O   . ILE A 1 573 ? 12.807  -40.014 -4.036  1.00 13.48 ? 571  ILE B O   1 
ATOM   4364 C CB  . ILE A 1 573 ? 13.783  -37.892 -6.493  1.00 14.05 ? 571  ILE B CB  1 
ATOM   4365 C CG1 . ILE A 1 573 ? 14.786  -37.636 -7.622  1.00 15.04 ? 571  ILE B CG1 1 
ATOM   4366 C CG2 . ILE A 1 573 ? 14.261  -37.280 -5.180  1.00 14.37 ? 571  ILE B CG2 1 
ATOM   4367 C CD1 . ILE A 1 573 ? 16.101  -38.377 -7.504  1.00 16.63 ? 571  ILE B CD1 1 
ATOM   4368 N N   . LEU A 1 574 ? 11.167  -39.189 -5.391  1.00 13.37 ? 572  LEU B N   1 
ATOM   4369 C CA  . LEU A 1 574 ? 10.143  -39.236 -4.325  1.00 13.91 ? 572  LEU B CA  1 
ATOM   4370 C C   . LEU A 1 574 ? 10.045  -40.595 -3.634  1.00 13.25 ? 572  LEU B C   1 
ATOM   4371 O O   . LEU A 1 574 ? 9.734   -40.614 -2.442  1.00 15.18 ? 572  LEU B O   1 
ATOM   4372 C CB  . LEU A 1 574 ? 8.803   -38.805 -4.932  1.00 14.47 ? 572  LEU B CB  1 
ATOM   4373 C CG  . LEU A 1 574 ? 7.671   -38.619 -3.940  1.00 15.39 ? 572  LEU B CG  1 
ATOM   4374 C CD1 . LEU A 1 574 ? 8.022   -37.598 -2.871  1.00 15.12 ? 572  LEU B CD1 1 
ATOM   4375 C CD2 . LEU A 1 574 ? 6.436   -38.172 -4.701  1.00 16.25 ? 572  LEU B CD2 1 
ATOM   4376 N N   . PRO A 1 575 ? 10.258  -41.764 -4.296  1.00 13.98 ? 573  PRO B N   1 
ATOM   4377 C CA  . PRO A 1 575 ? 10.202  -43.039 -3.577  1.00 14.56 ? 573  PRO B CA  1 
ATOM   4378 C C   . PRO A 1 575 ? 11.226  -43.205 -2.433  1.00 14.68 ? 573  PRO B C   1 
ATOM   4379 O O   . PRO A 1 575 ? 11.040  -44.101 -1.619  1.00 15.20 ? 573  PRO B O   1 
ATOM   4380 C CB  . PRO A 1 575 ? 10.436  -44.064 -4.681  1.00 15.60 ? 573  PRO B CB  1 
ATOM   4381 C CG  . PRO A 1 575 ? 9.883   -43.349 -5.923  1.00 15.47 ? 573  PRO B CG  1 
ATOM   4382 C CD  . PRO A 1 575 ? 10.446  -41.963 -5.743  1.00 14.68 ? 573  PRO B CD  1 
ATOM   4383 N N   . ARG A 1 576 ? 12.197  -42.301 -2.327  1.00 13.85 ? 574  ARG B N   1 
ATOM   4384 C CA  . ARG A 1 576 ? 13.057  -42.256 -1.123  1.00 13.17 ? 574  ARG B CA  1 
ATOM   4385 C C   . ARG A 1 576 ? 12.193  -42.139 0.133   1.00 13.35 ? 574  ARG B C   1 
ATOM   4386 O O   . ARG A 1 576 ? 12.643  -42.568 1.235   1.00 13.85 ? 574  ARG B O   1 
ATOM   4387 C CB  . ARG A 1 576 ? 14.050  -41.112 -1.201  1.00 14.13 ? 574  ARG B CB  1 
ATOM   4388 C CG  . ARG A 1 576 ? 15.044  -41.270 -2.323  1.00 13.46 ? 574  ARG B CG  1 
ATOM   4389 C CD  . ARG A 1 576 ? 15.865  -39.991 -2.473  1.00 13.97 ? 574  ARG B CD  1 
ATOM   4390 N NE  . ARG A 1 576 ? 16.843  -40.128 -3.535  1.00 15.34 ? 574  ARG B NE  1 
ATOM   4391 C CZ  . ARG A 1 576 ? 17.865  -39.295 -3.738  1.00 15.10 ? 574  ARG B CZ  1 
ATOM   4392 N NH1 . ARG A 1 576 ? 18.066  -38.262 -2.949  1.00 13.89 ? 574  ARG B NH1 1 
ATOM   4393 N NH2 . ARG A 1 576 ? 18.697  -39.532 -4.726  1.00 15.76 ? 574  ARG B NH2 1 
ATOM   4394 N N   . THR A 1 577 ? 10.994  -41.536 0.033   1.00 13.28 ? 575  THR B N   1 
ATOM   4395 C CA  . THR A 1 577 ? 10.089  -41.391 1.195   1.00 13.73 ? 575  THR B CA  1 
ATOM   4396 C C   . THR A 1 577 ? 9.779   -42.767 1.812   1.00 14.50 ? 575  THR B C   1 
ATOM   4397 O O   . THR A 1 577 ? 9.594   -42.836 3.042   1.00 15.29 ? 575  THR B O   1 
ATOM   4398 C CB  . THR A 1 577 ? 8.793   -40.652 0.841   1.00 14.49 ? 575  THR B CB  1 
ATOM   4399 O OG1 . THR A 1 577 ? 8.138   -41.280 -0.261  1.00 14.86 ? 575  THR B OG1 1 
ATOM   4400 C CG2 . THR A 1 577 ? 9.065   -39.203 0.525   1.00 15.36 ? 575  THR B CG2 1 
ATOM   4401 N N   . ARG A 1 578 ? 9.729   -43.836 1.017   1.00 15.00 ? 576  ARG B N   1 
ATOM   4402 C CA  . ARG A 1 578 ? 9.380   -45.178 1.533   1.00 15.24 ? 576  ARG B CA  1 
ATOM   4403 C C   . ARG A 1 578 ? 10.409  -45.609 2.605   1.00 15.62 ? 576  ARG B C   1 
ATOM   4404 O O   . ARG A 1 578 ? 9.980   -46.145 3.686   1.00 16.44 ? 576  ARG B O   1 
ATOM   4405 C CB  . ARG A 1 578 ? 9.383   -46.219 0.412   1.00 16.18 ? 576  ARG B CB  1 
ATOM   4406 C CG  . ARG A 1 578 ? 8.378   -46.000 -0.704  1.00 16.55 ? 576  ARG B CG  1 
ATOM   4407 C CD  . ARG A 1 578 ? 6.958   -45.799 -0.234  1.00 17.18 ? 576  ARG B CD  1 
ATOM   4408 N NE  . ARG A 1 578 ? 6.679   -44.389 0.036   1.00 17.47 ? 576  ARG B NE  1 
ATOM   4409 C CZ  . ARG A 1 578 ? 5.947   -43.907 1.024   1.00 18.91 ? 576  ARG B CZ  1 
ATOM   4410 N NH1 . ARG A 1 578 ? 5.366   -44.709 1.914   1.00 18.08 ? 576  ARG B NH1 1 
ATOM   4411 N NH2 . ARG A 1 578 ? 5.787   -42.590 1.108   1.00 16.29 ? 576  ARG B NH2 1 
ATOM   4412 N N   . ALA A 1 579 ? 11.695  -45.327 2.399   1.00 16.10 ? 577  ALA B N   1 
ATOM   4413 C CA  . ALA A 1 579 ? 12.754  -45.689 3.367   1.00 15.99 ? 577  ALA B CA  1 
ATOM   4414 C C   . ALA A 1 579 ? 12.701  -44.781 4.600   1.00 15.82 ? 577  ALA B C   1 
ATOM   4415 O O   . ALA A 1 579 ? 12.819  -45.293 5.718   1.00 14.84 ? 577  ALA B O   1 
ATOM   4416 C CB  . ALA A 1 579 ? 14.118  -45.634 2.720   1.00 17.97 ? 577  ALA B CB  1 
ATOM   4417 N N   . HIS A 1 580 ? 12.510  -43.454 4.434   1.00 14.42 ? 578  HIS B N   1 
ATOM   4418 C CA  . HIS A 1 580 ? 12.300  -42.549 5.595   1.00 15.11 ? 578  HIS B CA  1 
ATOM   4419 C C   . HIS A 1 580 ? 11.083  -42.954 6.441   1.00 13.96 ? 578  HIS B C   1 
ATOM   4420 O O   . HIS A 1 580 ? 11.161  -42.925 7.693   1.00 14.86 ? 578  HIS B O   1 
ATOM   4421 C CB  . HIS A 1 580 ? 12.240  -41.082 5.135   1.00 15.21 ? 578  HIS B CB  1 
ATOM   4422 C CG  . HIS A 1 580 ? 13.543  -40.632 4.549   1.00 15.25 ? 578  HIS B CG  1 
ATOM   4423 N ND1 . HIS A 1 580 ? 14.713  -40.588 5.285   1.00 13.91 ? 578  HIS B ND1 1 
ATOM   4424 C CD2 . HIS A 1 580 ? 13.864  -40.233 3.292   1.00 14.80 ? 578  HIS B CD2 1 
ATOM   4425 C CE1 . HIS A 1 580 ? 15.684  -40.159 4.495   1.00 16.11 ? 578  HIS B CE1 1 
ATOM   4426 N NE2 . HIS A 1 580 ? 15.180  -39.908 3.273   1.00 15.11 ? 578  HIS B NE2 1 
ATOM   4427 N N   . VAL A 1 581 ? 10.003  -43.349 5.815   1.00 13.72 ? 579  VAL B N   1 
ATOM   4428 C CA  . VAL A 1 581 ? 8.813   -43.824 6.557   1.00 14.40 ? 579  VAL B CA  1 
ATOM   4429 C C   . VAL A 1 581 ? 9.159   -45.050 7.407   1.00 14.82 ? 579  VAL B C   1 
ATOM   4430 O O   . VAL A 1 581 ? 8.882   -45.043 8.621   1.00 15.11 ? 579  VAL B O   1 
ATOM   4431 C CB  . VAL A 1 581 ? 7.644   -44.133 5.607   1.00 16.62 ? 579  VAL B CB  1 
ATOM   4432 C CG1 . VAL A 1 581 ? 6.562   -44.921 6.333   1.00 18.84 ? 579  VAL B CG1 1 
ATOM   4433 C CG2 . VAL A 1 581 ? 7.096   -42.825 5.063   1.00 17.01 ? 579  VAL B CG2 1 
ATOM   4434 N N   . ALA A 1 582 ? 9.688   -46.086 6.791   1.00 15.39 ? 580  ALA B N   1 
ATOM   4435 C CA  . ALA A 1 582 ? 10.019  -47.335 7.511   1.00 16.11 ? 580  ALA B CA  1 
ATOM   4436 C C   . ALA A 1 582 ? 10.968  -47.002 8.659   1.00 15.67 ? 580  ALA B C   1 
ATOM   4437 O O   . ALA A 1 582 ? 10.745  -47.487 9.788   1.00 15.54 ? 580  ALA B O   1 
ATOM   4438 C CB  . ALA A 1 582 ? 10.624  -48.340 6.563   1.00 15.96 ? 580  ALA B CB  1 
ATOM   4439 N N   . ALA A 1 583 ? 12.032  -46.266 8.391   1.00 15.60 ? 581  ALA B N   1 
ATOM   4440 C CA  . ALA A 1 583 ? 13.034  -45.943 9.441   1.00 15.87 ? 581  ALA B CA  1 
ATOM   4441 C C   . ALA A 1 583 ? 12.373  -45.176 10.579  1.00 18.13 ? 581  ALA B C   1 
ATOM   4442 O O   . ALA A 1 583 ? 12.564  -45.517 11.753  1.00 18.11 ? 581  ALA B O   1 
ATOM   4443 C CB  . ALA A 1 583 ? 14.208  -45.159 8.885   1.00 16.19 ? 581  ALA B CB  1 
ATOM   4444 N N   . MET A 1 584 ? 11.597  -44.151 10.264  1.00 18.87 ? 582  MET B N   1 
ATOM   4445 C CA  . MET A 1 584 ? 11.077  -43.261 11.331  1.00 17.70 ? 582  MET B CA  1 
ATOM   4446 C C   . MET A 1 584 ? 10.070  -44.031 12.204  1.00 17.99 ? 582  MET B C   1 
ATOM   4447 O O   . MET A 1 584 ? 9.941   -43.674 13.390  1.00 19.84 ? 582  MET B O   1 
ATOM   4448 C CB  . MET A 1 584 ? 10.536  -41.930 10.770  1.00 19.96 ? 582  MET B CB  1 
ATOM   4449 C CG  . MET A 1 584 ? 9.150   -41.974 10.304  1.00 20.74 ? 582  MET B CG  1 
ATOM   4450 S SD  . MET A 1 584 ? 8.626   -40.251 9.810   1.00 21.51 ? 582  MET B SD  1 
ATOM   4451 C CE  . MET A 1 584 ? 9.323   -40.096 8.155   1.00 18.35 ? 582  MET B CE  1 
ATOM   4452 N N   . LEU A 1 585 ? 9.330   -44.976 11.648  1.00 19.31 ? 583  LEU B N   1 
ATOM   4453 C CA  . LEU A 1 585 ? 8.305   -45.735 12.405  1.00 20.33 ? 583  LEU B CA  1 
ATOM   4454 C C   . LEU A 1 585 ? 8.958   -46.934 13.108  1.00 21.87 ? 583  LEU B C   1 
ATOM   4455 O O   . LEU A 1 585 ? 8.219   -47.621 13.824  1.00 21.46 ? 583  LEU B O   1 
ATOM   4456 C CB  . LEU A 1 585 ? 7.200   -46.231 11.471  1.00 20.87 ? 583  LEU B CB  1 
ATOM   4457 C CG  . LEU A 1 585 ? 6.335   -45.130 10.848  1.00 22.11 ? 583  LEU B CG  1 
ATOM   4458 C CD1 . LEU A 1 585 ? 5.297   -45.762 9.937   1.00 23.64 ? 583  LEU B CD1 1 
ATOM   4459 C CD2 . LEU A 1 585 ? 5.697   -44.240 11.911  1.00 23.45 ? 583  LEU B CD2 1 
ATOM   4460 N N   . SER A 1 586 ? 10.254  -47.209 12.894  1.00 19.95 ? 584  SER B N   1 
ATOM   4461 C CA  . SER A 1 586 ? 10.906  -48.439 13.432  1.00 19.09 ? 584  SER B CA  1 
ATOM   4462 C C   . SER A 1 586 ? 11.139  -48.311 14.939  1.00 19.04 ? 584  SER B C   1 
ATOM   4463 O O   . SER A 1 586 ? 11.338  -49.374 15.561  1.00 21.17 ? 584  SER B O   1 
ATOM   4464 C CB  . SER A 1 586 ? 12.187  -48.789 12.707  1.00 17.76 ? 584  SER B CB  1 
ATOM   4465 O OG  . SER A 1 586 ? 13.221  -47.876 13.028  1.00 17.89 ? 584  SER B OG  1 
ATOM   4466 N N   . GLY A 1 587 ? 11.130  -47.105 15.500  1.00 19.87 ? 585  GLY B N   1 
ATOM   4467 C CA  . GLY A 1 587 ? 11.190  -46.899 16.963  1.00 22.34 ? 585  GLY B CA  1 
ATOM   4468 C C   . GLY A 1 587 ? 12.600  -46.630 17.471  1.00 21.18 ? 585  GLY B C   1 
ATOM   4469 O O   . GLY A 1 587 ? 13.596  -47.053 16.814  1.00 20.09 ? 585  GLY B O   1 
ATOM   4470 N N   . ALA A 1 588 ? 12.687  -45.893 18.583  1.00 19.38 ? 586  ALA B N   1 
ATOM   4471 C CA  . ALA A 1 588 ? 13.943  -45.463 19.218  1.00 18.76 ? 586  ALA B CA  1 
ATOM   4472 C C   . ALA A 1 588 ? 14.711  -46.662 19.779  1.00 17.99 ? 586  ALA B C   1 
ATOM   4473 O O   . ALA A 1 588 ? 15.946  -46.518 19.916  1.00 17.12 ? 586  ALA B O   1 
ATOM   4474 C CB  . ALA A 1 588 ? 13.685  -44.435 20.285  1.00 18.14 ? 586  ALA B CB  1 
ATOM   4475 N N   . ASN A 1 589 ? 14.066  -47.783 20.123  1.00 17.82 ? 587  ASN B N   1 
ATOM   4476 C CA  . ASN A 1 589 ? 14.800  -48.861 20.828  1.00 20.18 ? 587  ASN B CA  1 
ATOM   4477 C C   . ASN A 1 589 ? 15.956  -49.408 19.985  1.00 18.86 ? 587  ASN B C   1 
ATOM   4478 O O   . ASN A 1 589 ? 16.988  -49.761 20.581  1.00 18.31 ? 587  ASN B O   1 
ATOM   4479 C CB  . ASN A 1 589 ? 13.923  -50.019 21.267  1.00 24.07 ? 587  ASN B CB  1 
ATOM   4480 C CG  . ASN A 1 589 ? 13.905  -49.969 22.768  1.00 38.82 ? 587  ASN B CG  1 
ATOM   4481 O OD1 . ASN A 1 589 ? 14.750  -50.600 23.417  1.00 41.96 ? 587  ASN B OD1 1 
ATOM   4482 N ND2 . ASN A 1 589 ? 13.108  -49.045 23.289  1.00 40.14 ? 587  ASN B ND2 1 
ATOM   4483 N N   . ASN A 1 590 ? 15.786  -49.466 18.657  1.00 16.81 ? 588  ASN B N   1 
ATOM   4484 C CA  . ASN A 1 590 ? 16.850  -50.023 17.791  1.00 15.93 ? 588  ASN B CA  1 
ATOM   4485 C C   . ASN A 1 590 ? 18.063  -49.086 17.764  1.00 16.11 ? 588  ASN B C   1 
ATOM   4486 O O   . ASN A 1 590 ? 19.135  -49.547 17.333  1.00 17.59 ? 588  ASN B O   1 
ATOM   4487 C CB  . ASN A 1 590 ? 16.305  -50.440 16.440  1.00 15.29 ? 588  ASN B CB  1 
ATOM   4488 C CG  . ASN A 1 590 ? 15.827  -49.271 15.608  1.00 15.79 ? 588  ASN B CG  1 
ATOM   4489 O OD1 . ASN A 1 590 ? 16.389  -48.184 15.677  1.00 16.37 ? 588  ASN B OD1 1 
ATOM   4490 N ND2 . ASN A 1 590 ? 14.873  -49.540 14.735  1.00 16.77 ? 588  ASN B ND2 1 
ATOM   4491 N N   . LEU A 1 591 ? 17.951  -47.857 18.272  1.00 14.99 ? 589  LEU B N   1 
ATOM   4492 C CA  . LEU A 1 591 ? 19.086  -46.893 18.393  1.00 15.38 ? 589  LEU B CA  1 
ATOM   4493 C C   . LEU A 1 591 ? 19.650  -46.888 19.812  1.00 16.77 ? 589  LEU B C   1 
ATOM   4494 O O   . LEU A 1 591 ? 20.850  -46.602 19.976  1.00 16.88 ? 589  LEU B O   1 
ATOM   4495 C CB  . LEU A 1 591 ? 18.655  -45.457 18.047  1.00 15.64 ? 589  LEU B CB  1 
ATOM   4496 C CG  . LEU A 1 591 ? 18.095  -45.207 16.635  1.00 14.69 ? 589  LEU B CG  1 
ATOM   4497 C CD1 . LEU A 1 591 ? 17.666  -43.746 16.475  1.00 15.27 ? 589  LEU B CD1 1 
ATOM   4498 C CD2 . LEU A 1 591 ? 19.102  -45.554 15.579  1.00 15.56 ? 589  LEU B CD2 1 
ATOM   4499 N N   . MET A 1 592 ? 18.802  -47.075 20.822  1.00 17.46 ? 590  MET B N   1 
ATOM   4500 C CA  . MET A 1 592 ? 19.122  -46.714 22.220  1.00 18.80 ? 590  MET B CA  1 
ATOM   4501 C C   . MET A 1 592 ? 19.542  -47.960 23.009  1.00 19.21 ? 590  MET B C   1 
ATOM   4502 O O   . MET A 1 592 ? 20.149  -47.779 24.059  1.00 20.28 ? 590  MET B O   1 
ATOM   4503 C CB  . MET A 1 592 ? 17.912  -46.104 22.933  1.00 19.44 ? 590  MET B CB  1 
ATOM   4504 C CG  . MET A 1 592 ? 17.391  -44.833 22.265  1.00 19.79 ? 590  MET B CG  1 
ATOM   4505 S SD  . MET A 1 592 ? 18.651  -43.644 21.793  1.00 21.27 ? 590  MET B SD  1 
ATOM   4506 C CE  . MET A 1 592 ? 19.397  -43.249 23.366  1.00 21.77 ? 590  MET B CE  1 
ATOM   4507 N N   . GLU A 1 593 ? 19.232  -49.155 22.526  1.00 19.21 ? 591  GLU B N   1 
ATOM   4508 C CA  . GLU A 1 593 ? 19.464  -50.404 23.298  1.00 21.01 ? 591  GLU B CA  1 
ATOM   4509 C C   . GLU A 1 593 ? 20.964  -50.683 23.421  1.00 20.90 ? 591  GLU B C   1 
ATOM   4510 O O   . GLU A 1 593 ? 21.382  -51.162 24.500  1.00 24.09 ? 591  GLU B O   1 
ATOM   4511 C CB  . GLU A 1 593 ? 18.738  -51.561 22.630  1.00 26.48 ? 591  GLU B CB  1 
ATOM   4512 C CG  . GLU A 1 593 ? 18.290  -52.640 23.587  1.00 37.70 ? 591  GLU B CG  1 
ATOM   4513 C CD  . GLU A 1 593 ? 16.887  -53.126 23.254  1.00 43.56 ? 591  GLU B CD  1 
ATOM   4514 O OE1 . GLU A 1 593 ? 16.705  -53.609 22.126  1.00 45.45 ? 591  GLU B OE1 1 
ATOM   4515 O OE2 . GLU A 1 593 ? 15.966  -52.953 24.083  1.00 50.69 ? 591  GLU B OE2 1 
ATOM   4516 N N   . MET A 1 594 ? 21.773  -50.397 22.395  1.00 19.48 ? 592  MET B N   1 
ATOM   4517 C CA  A MET A 1 594 ? 23.232  -50.671 22.479  0.50 19.82 ? 592  MET B CA  1 
ATOM   4518 C CA  B MET A 1 594 ? 23.247  -50.622 22.435  0.50 18.70 ? 592  MET B CA  1 
ATOM   4519 C C   . MET A 1 594 ? 23.850  -49.839 23.602  1.00 19.78 ? 592  MET B C   1 
ATOM   4520 O O   . MET A 1 594 ? 23.715  -48.609 23.617  1.00 19.41 ? 592  MET B O   1 
ATOM   4521 C CB  A MET A 1 594 ? 23.972  -50.382 21.175  0.50 19.88 ? 592  MET B CB  1 
ATOM   4522 C CB  B MET A 1 594 ? 23.913  -50.161 21.134  0.50 17.42 ? 592  MET B CB  1 
ATOM   4523 C CG  A MET A 1 594 ? 25.410  -50.874 21.209  0.50 20.79 ? 592  MET B CG  1 
ATOM   4524 C CG  B MET A 1 594 ? 25.408  -50.437 21.059  0.50 16.99 ? 592  MET B CG  1 
ATOM   4525 S SD  A MET A 1 594 ? 26.147  -50.837 19.569  0.50 21.14 ? 592  MET B SD  1 
ATOM   4526 S SD  B MET A 1 594 ? 25.781  -52.129 20.515  0.50 15.21 ? 592  MET B SD  1 
ATOM   4527 C CE  A MET A 1 594 ? 25.166  -52.091 18.744  0.50 19.70 ? 592  MET B CE  1 
ATOM   4528 C CE  B MET A 1 594 ? 25.637  -51.925 18.740  0.50 15.03 ? 592  MET B CE  1 
ATOM   4529 N N   . ALA A 1 595 ? 24.577  -50.493 24.505  1.00 19.92 ? 593  ALA B N   1 
ATOM   4530 C CA  . ALA A 1 595 ? 25.295  -49.771 25.568  1.00 20.26 ? 593  ALA B CA  1 
ATOM   4531 C C   . ALA A 1 595 ? 26.436  -48.957 24.964  1.00 18.92 ? 593  ALA B C   1 
ATOM   4532 O O   . ALA A 1 595 ? 27.090  -49.445 24.004  1.00 17.86 ? 593  ALA B O   1 
ATOM   4533 C CB  . ALA A 1 595 ? 25.821  -50.774 26.582  1.00 21.61 ? 593  ALA B CB  1 
ATOM   4534 N N   . GLU A 1 596 ? 26.726  -47.789 25.542  1.00 19.51 ? 594  GLU B N   1 
ATOM   4535 C CA  . GLU A 1 596 ? 27.819  -46.912 25.093  1.00 20.96 ? 594  GLU B CA  1 
ATOM   4536 C C   . GLU A 1 596 ? 29.127  -47.723 24.996  1.00 20.70 ? 594  GLU B C   1 
ATOM   4537 O O   . GLU A 1 596 ? 29.867  -47.602 23.994  1.00 20.57 ? 594  GLU B O   1 
ATOM   4538 C CB  . GLU A 1 596 ? 27.958  -45.730 26.058  1.00 24.30 ? 594  GLU B CB  1 
ATOM   4539 C CG  . GLU A 1 596 ? 26.689  -44.889 26.228  1.00 28.54 ? 594  GLU B CG  1 
ATOM   4540 C CD  . GLU A 1 596 ? 26.810  -43.771 27.271  1.00 27.50 ? 594  GLU B CD  1 
ATOM   4541 O OE1 . GLU A 1 596 ? 27.921  -43.567 27.808  1.00 28.65 ? 594  GLU B OE1 1 
ATOM   4542 O OE2 . GLU A 1 596 ? 25.812  -43.091 27.516  1.00 30.09 ? 594  GLU B OE2 1 
ATOM   4543 N N   . GLU A 1 597 ? 29.370  -48.576 25.993  1.00 21.21 ? 595  GLU B N   1 
ATOM   4544 C CA  A GLU A 1 597 ? 30.681  -49.281 26.109  0.50 21.04 ? 595  GLU B CA  1 
ATOM   4545 C CA  B GLU A 1 597 ? 30.624  -49.361 26.183  0.50 22.00 ? 595  GLU B CA  1 
ATOM   4546 C C   . GLU A 1 597 ? 30.740  -50.466 25.128  1.00 20.55 ? 595  GLU B C   1 
ATOM   4547 O O   . GLU A 1 597 ? 31.797  -51.114 25.056  1.00 22.29 ? 595  GLU B O   1 
ATOM   4548 C CB  A GLU A 1 597 ? 30.917  -49.711 27.561  0.50 22.84 ? 595  GLU B CB  1 
ATOM   4549 C CB  B GLU A 1 597 ? 30.610  -50.029 27.565  0.50 24.39 ? 595  GLU B CB  1 
ATOM   4550 C CG  A GLU A 1 597 ? 29.900  -50.708 28.082  0.50 21.88 ? 595  GLU B CG  1 
ATOM   4551 C CG  B GLU A 1 597 ? 30.541  -49.049 28.721  0.50 25.95 ? 595  GLU B CG  1 
ATOM   4552 C CD  A GLU A 1 597 ? 28.707  -50.102 28.797  0.50 24.15 ? 595  GLU B CD  1 
ATOM   4553 C CD  B GLU A 1 597 ? 29.132  -48.655 29.127  0.50 28.22 ? 595  GLU B CD  1 
ATOM   4554 O OE1 A GLU A 1 597 ? 28.410  -48.914 28.541  0.50 25.46 ? 595  GLU B OE1 1 
ATOM   4555 O OE1 B GLU A 1 597 ? 28.180  -49.025 28.409  0.50 28.58 ? 595  GLU B OE1 1 
ATOM   4556 O OE2 A GLU A 1 597 ? 28.059  -50.823 29.582  0.50 25.87 ? 595  GLU B OE2 1 
ATOM   4557 O OE2 B GLU A 1 597 ? 28.984  -47.997 30.162  0.50 29.69 ? 595  GLU B OE2 1 
ATOM   4558 N N   . ASP A 1 598 ? 29.688  -50.738 24.349  1.00 18.98 ? 596  ASP B N   1 
ATOM   4559 C CA  . ASP A 1 598 ? 29.604  -51.956 23.498  1.00 18.88 ? 596  ASP B CA  1 
ATOM   4560 C C   . ASP A 1 598 ? 29.678  -51.597 22.001  1.00 17.69 ? 596  ASP B C   1 
ATOM   4561 O O   . ASP A 1 598 ? 29.558  -52.489 21.186  1.00 16.43 ? 596  ASP B O   1 
ATOM   4562 C CB  . ASP A 1 598 ? 28.325  -52.728 23.817  1.00 19.32 ? 596  ASP B CB  1 
ATOM   4563 C CG  . ASP A 1 598 ? 28.316  -53.378 25.190  1.00 20.24 ? 596  ASP B CG  1 
ATOM   4564 O OD1 . ASP A 1 598 ? 29.360  -53.360 25.852  1.00 22.02 ? 596  ASP B OD1 1 
ATOM   4565 O OD2 . ASP A 1 598 ? 27.263  -53.902 25.574  1.00 21.45 ? 596  ASP B OD2 1 
ATOM   4566 N N   . PHE A 1 599 ? 29.868  -50.319 21.684  1.00 17.45 ? 597  PHE B N   1 
ATOM   4567 C CA  . PHE A 1 599 ? 29.846  -49.879 20.265  1.00 18.27 ? 597  PHE B CA  1 
ATOM   4568 C C   . PHE A 1 599 ? 31.119  -50.271 19.515  1.00 17.79 ? 597  PHE B C   1 
ATOM   4569 O O   . PHE A 1 599 ? 31.044  -50.367 18.300  1.00 17.20 ? 597  PHE B O   1 
ATOM   4570 C CB  . PHE A 1 599 ? 29.700  -48.355 20.195  1.00 18.13 ? 597  PHE B CB  1 
ATOM   4571 C CG  . PHE A 1 599 ? 28.285  -47.859 20.049  1.00 18.13 ? 597  PHE B CG  1 
ATOM   4572 C CD1 . PHE A 1 599 ? 27.483  -47.671 21.160  1.00 18.50 ? 597  PHE B CD1 1 
ATOM   4573 C CD2 . PHE A 1 599 ? 27.758  -47.583 18.800  1.00 18.82 ? 597  PHE B CD2 1 
ATOM   4574 C CE1 . PHE A 1 599 ? 26.180  -47.224 21.026  1.00 18.85 ? 597  PHE B CE1 1 
ATOM   4575 C CE2 . PHE A 1 599 ? 26.455  -47.130 18.668  1.00 18.66 ? 597  PHE B CE2 1 
ATOM   4576 C CZ  . PHE A 1 599 ? 25.669  -46.953 19.781  1.00 18.26 ? 597  PHE B CZ  1 
ATOM   4577 N N   . ALA A 1 600 ? 32.232  -50.471 20.220  1.00 15.67 ? 598  ALA B N   1 
ATOM   4578 C CA  . ALA A 1 600 ? 33.537  -50.680 19.545  1.00 17.54 ? 598  ALA B CA  1 
ATOM   4579 C C   . ALA A 1 600 ? 34.305  -51.861 20.161  1.00 18.23 ? 598  ALA B C   1 
ATOM   4580 O O   . ALA A 1 600 ? 35.415  -51.669 20.623  1.00 19.63 ? 598  ALA B O   1 
ATOM   4581 C CB  . ALA A 1 600 ? 34.312  -49.386 19.612  1.00 17.12 ? 598  ALA B CB  1 
ATOM   4582 N N   . LEU A 1 601 ? 33.712  -53.044 20.090  1.00 18.31 ? 599  LEU B N   1 
ATOM   4583 C CA  . LEU A 1 601 ? 34.337  -54.250 20.687  1.00 18.79 ? 599  LEU B CA  1 
ATOM   4584 C C   . LEU A 1 601 ? 35.089  -55.076 19.628  1.00 19.54 ? 599  LEU B C   1 
ATOM   4585 O O   . LEU A 1 601 ? 35.524  -56.165 19.961  1.00 20.82 ? 599  LEU B O   1 
ATOM   4586 C CB  . LEU A 1 601 ? 33.225  -55.053 21.372  1.00 17.13 ? 599  LEU B CB  1 
ATOM   4587 C CG  . LEU A 1 601 ? 32.537  -54.339 22.532  1.00 18.50 ? 599  LEU B CG  1 
ATOM   4588 C CD1 . LEU A 1 601 ? 31.359  -55.148 23.045  1.00 17.13 ? 599  LEU B CD1 1 
ATOM   4589 C CD2 . LEU A 1 601 ? 33.522  -54.058 23.653  1.00 20.59 ? 599  LEU B CD2 1 
ATOM   4590 N N   . GLY A 1 602 ? 35.276  -54.539 18.424  1.00 19.48 ? 600  GLY B N   1 
ATOM   4591 C CA  . GLY A 1 602 ? 35.939  -55.292 17.334  1.00 20.35 ? 600  GLY B CA  1 
ATOM   4592 C C   . GLY A 1 602 ? 37.437  -55.038 17.214  1.00 18.68 ? 600  GLY B C   1 
ATOM   4593 O O   . GLY A 1 602 ? 37.984  -55.406 16.195  1.00 18.45 ? 600  GLY B O   1 
ATOM   4594 N N   . TYR A 1 603 ? 38.067  -54.488 18.251  1.00 18.29 ? 601  TYR B N   1 
ATOM   4595 C CA  . TYR A 1 603 ? 39.517  -54.128 18.246  1.00 20.24 ? 601  TYR B CA  1 
ATOM   4596 C C   . TYR A 1 603 ? 40.281  -55.142 19.143  1.00 23.31 ? 601  TYR B C   1 
ATOM   4597 O O   . TYR A 1 603 ? 40.897  -56.039 18.449  1.00 23.98 ? 601  TYR B O   1 
ATOM   4598 C CB  . TYR A 1 603 ? 39.668  -52.634 18.574  1.00 22.77 ? 601  TYR B CB  1 
ATOM   4599 C CG  . TYR A 1 603 ? 38.834  -51.796 17.633  1.00 21.82 ? 601  TYR B CG  1 
ATOM   4600 C CD1 . TYR A 1 603 ? 39.347  -51.355 16.432  1.00 21.92 ? 601  TYR B CD1 1 
ATOM   4601 C CD2 . TYR A 1 603 ? 37.490  -51.557 17.892  1.00 22.84 ? 601  TYR B CD2 1 
ATOM   4602 C CE1 . TYR A 1 603 ? 38.545  -50.710 15.502  1.00 23.40 ? 601  TYR B CE1 1 
ATOM   4603 C CE2 . TYR A 1 603 ? 36.665  -50.928 16.969  1.00 22.58 ? 601  TYR B CE2 1 
ATOM   4604 C CZ  . TYR A 1 603 ? 37.198  -50.493 15.768  1.00 21.64 ? 601  TYR B CZ  1 
ATOM   4605 O OH  . TYR A 1 603 ? 36.386  -49.858 14.868  1.00 21.92 ? 601  TYR B OH  1 
HETATM 4606 C C3  . PKZ B 2 .   ? 27.642  -20.100 10.951  1.00 41.25 ? 701  PKZ B C3  1 
HETATM 4607 C C1  . PKZ B 2 .   ? 26.887  -19.463 13.258  1.00 41.10 ? 701  PKZ B C1  1 
HETATM 4608 C C10 . PKZ B 2 .   ? 23.942  -15.607 4.649   1.00 38.47 ? 701  PKZ B C10 1 
HETATM 4609 C C8  . PKZ B 2 .   ? 25.247  -17.487 5.736   1.00 38.40 ? 701  PKZ B C8  1 
HETATM 4610 C C7  . PKZ B 2 .   ? 26.410  -17.684 6.680   1.00 36.49 ? 701  PKZ B C7  1 
HETATM 4611 C C5  . PKZ B 2 .   ? 27.259  -18.902 8.739   1.00 32.57 ? 701  PKZ B C5  1 
HETATM 4612 C C11 . PKZ B 2 .   ? 22.563  -15.018 4.784   1.00 38.95 ? 701  PKZ B C11 1 
HETATM 4613 C C13 . PKZ B 2 .   ? 21.170  -14.104 2.872   1.00 42.52 ? 701  PKZ B C13 1 
HETATM 4614 C C16 . PKZ B 2 .   ? 17.452  -13.757 3.916   1.00 42.05 ? 701  PKZ B C16 1 
HETATM 4615 C C15 . PKZ B 2 .   ? 18.797  -14.392 3.663   1.00 43.98 ? 701  PKZ B C15 1 
HETATM 4616 C C14 . PKZ B 2 .   ? 19.868  -13.435 3.217   1.00 43.49 ? 701  PKZ B C14 1 
HETATM 4617 N N1A . PKZ B 2 .   ? 13.140  -19.721 15.935  1.00 24.80 ? 701  PKZ B N1A 1 
HETATM 4618 C C2A . PKZ B 2 .   ? 13.103  -18.661 16.750  1.00 27.75 ? 701  PKZ B C2A 1 
HETATM 4619 N N3A . PKZ B 2 .   ? 13.328  -18.598 18.058  1.00 28.11 ? 701  PKZ B N3A 1 
HETATM 4620 C C4A . PKZ B 2 .   ? 13.615  -19.812 18.546  1.00 28.56 ? 701  PKZ B C4A 1 
HETATM 4621 C C5A . PKZ B 2 .   ? 13.681  -20.993 17.843  1.00 27.60 ? 701  PKZ B C5A 1 
HETATM 4622 C C6A . PKZ B 2 .   ? 13.421  -20.935 16.461  1.00 26.99 ? 701  PKZ B C6A 1 
HETATM 4623 N N6A . PKZ B 2 .   ? 13.465  -21.986 15.649  1.00 22.60 ? 701  PKZ B N6A 1 
HETATM 4624 N N7A . PKZ B 2 .   ? 14.012  -22.035 18.698  1.00 30.73 ? 701  PKZ B N7A 1 
HETATM 4625 C C8A . PKZ B 2 .   ? 14.138  -21.471 19.877  1.00 32.98 ? 701  PKZ B C8A 1 
HETATM 4626 N N9A . PKZ B 2 .   ? 13.900  -20.123 19.846  1.00 32.70 ? 701  PKZ B N9A 1 
HETATM 4627 C C1B . PKZ B 2 .   ? 13.983  -19.160 20.944  1.00 38.10 ? 701  PKZ B C1B 1 
HETATM 4628 C C2B . PKZ B 2 .   ? 12.670  -18.848 21.657  1.00 42.10 ? 701  PKZ B C2B 1 
HETATM 4629 O O2B . PKZ B 2 .   ? 12.702  -17.523 22.143  1.00 47.48 ? 701  PKZ B O2B 1 
HETATM 4630 C C3B . PKZ B 2 .   ? 12.694  -19.844 22.812  1.00 44.40 ? 701  PKZ B C3B 1 
HETATM 4631 O O3B . PKZ B 2 .   ? 11.923  -19.374 23.916  1.00 48.71 ? 701  PKZ B O3B 1 
HETATM 4632 P P3B . PKZ B 2 .   ? 10.456  -20.046 23.966  1.00 50.99 ? 701  PKZ B P3B 1 
HETATM 4633 O O7A . PKZ B 2 .   ? 9.663   -19.436 22.839  1.00 44.72 ? 701  PKZ B O7A 1 
HETATM 4634 O O8A . PKZ B 2 .   ? 10.621  -21.536 23.804  1.00 51.22 ? 701  PKZ B O8A 1 
HETATM 4635 O O9A . PKZ B 2 .   ? 9.886   -19.689 25.316  1.00 55.29 ? 701  PKZ B O9A 1 
HETATM 4636 C C4B . PKZ B 2 .   ? 14.172  -19.861 23.173  1.00 43.25 ? 701  PKZ B C4B 1 
HETATM 4637 O O4B . PKZ B 2 .   ? 14.865  -19.677 21.914  1.00 40.19 ? 701  PKZ B O4B 1 
HETATM 4638 C C5B . PKZ B 2 .   ? 14.641  -21.150 23.795  1.00 41.91 ? 701  PKZ B C5B 1 
HETATM 4639 O O5B . PKZ B 2 .   ? 14.120  -22.241 23.012  1.00 40.56 ? 701  PKZ B O5B 1 
HETATM 4640 P P1A . PKZ B 2 .   ? 14.425  -23.727 23.506  1.00 45.51 ? 701  PKZ B P1A 1 
HETATM 4641 O O1A . PKZ B 2 .   ? 13.782  -24.696 22.572  1.00 40.39 ? 701  PKZ B O1A 1 
HETATM 4642 O O2A . PKZ B 2 .   ? 14.121  -23.832 24.960  1.00 43.09 ? 701  PKZ B O2A 1 
HETATM 4643 O O3A . PKZ B 2 .   ? 16.006  -23.767 23.292  1.00 44.81 ? 701  PKZ B O3A 1 
HETATM 4644 P P2A . PKZ B 2 .   ? 17.249  -24.046 24.252  1.00 44.61 ? 701  PKZ B P2A 1 
HETATM 4645 O O4A . PKZ B 2 .   ? 17.287  -25.499 24.572  1.00 43.68 ? 701  PKZ B O4A 1 
HETATM 4646 O O5A . PKZ B 2 .   ? 17.252  -23.053 25.361  1.00 46.54 ? 701  PKZ B O5A 1 
HETATM 4647 O O6A . PKZ B 2 .   ? 18.474  -23.721 23.272  1.00 37.19 ? 701  PKZ B O6A 1 
HETATM 4648 C CBP . PKZ B 2 .   ? 19.282  -23.994 21.015  1.00 33.85 ? 701  PKZ B CBP 1 
HETATM 4649 C CCP . PKZ B 2 .   ? 18.880  -24.714 22.299  1.00 34.01 ? 701  PKZ B CCP 1 
HETATM 4650 C CDP . PKZ B 2 .   ? 18.065  -23.259 20.447  1.00 37.21 ? 701  PKZ B CDP 1 
HETATM 4651 C CEP . PKZ B 2 .   ? 20.376  -22.971 21.326  1.00 33.38 ? 701  PKZ B CEP 1 
HETATM 4652 C CAP . PKZ B 2 .   ? 19.798  -25.018 19.997  1.00 35.86 ? 701  PKZ B CAP 1 
HETATM 4653 O OAP . PKZ B 2 .   ? 18.743  -25.885 19.635  1.00 33.80 ? 701  PKZ B OAP 1 
HETATM 4654 C C9P . PKZ B 2 .   ? 20.435  -24.444 18.745  1.00 36.48 ? 701  PKZ B C9P 1 
HETATM 4655 O O9P . PKZ B 2 .   ? 19.729  -23.903 17.901  1.00 31.37 ? 701  PKZ B O9P 1 
HETATM 4656 N N8P . PKZ B 2 .   ? 21.739  -24.634 18.593  1.00 41.65 ? 701  PKZ B N8P 1 
HETATM 4657 C C7P . PKZ B 2 .   ? 22.725  -23.570 18.450  1.00 44.81 ? 701  PKZ B C7P 1 
HETATM 4658 C C6P . PKZ B 2 .   ? 22.272  -22.482 17.520  1.00 42.50 ? 701  PKZ B C6P 1 
HETATM 4659 C C5P . PKZ B 2 .   ? 22.964  -22.457 16.176  1.00 42.09 ? 701  PKZ B C5P 1 
HETATM 4660 O O5P . PKZ B 2 .   ? 22.331  -22.333 15.133  1.00 32.61 ? 701  PKZ B O5P 1 
HETATM 4661 N N4P . PKZ B 2 .   ? 24.291  -22.538 16.181  1.00 42.57 ? 701  PKZ B N4P 1 
HETATM 4662 C C3P . PKZ B 2 .   ? 25.081  -22.147 15.031  1.00 46.21 ? 701  PKZ B C3P 1 
HETATM 4663 C C2P . PKZ B 2 .   ? 24.985  -20.671 14.787  1.00 49.20 ? 701  PKZ B C2P 1 
HETATM 4664 S S1P . PKZ B 2 .   ? 26.671  -20.032 14.892  1.00 60.36 ? 701  PKZ B S1P 1 
HETATM 4665 O O1  . PKZ B 2 .   ? 26.916  -18.297 12.980  1.00 60.70 ? 701  PKZ B O1  1 
HETATM 4666 C C2  . PKZ B 2 .   ? 27.032  -20.560 12.245  1.00 41.33 ? 701  PKZ B C2  1 
HETATM 4667 C C4  . PKZ B 2 .   ? 26.664  -19.381 10.040  1.00 34.38 ? 701  PKZ B C4  1 
HETATM 4668 C C6  . PKZ B 2 .   ? 26.294  -18.890 7.579   1.00 36.75 ? 701  PKZ B C6  1 
HETATM 4669 C C9  . PKZ B 2 .   ? 24.493  -16.195 5.925   1.00 37.36 ? 701  PKZ B C9  1 
HETATM 4670 C C12 . PKZ B 2 .   ? 22.276  -13.862 3.862   1.00 43.20 ? 701  PKZ B C12 1 
HETATM 4671 C C1  . EDO C 3 .   ? 16.660  -44.179 -6.254  1.00 24.90 ? 702  EDO B C1  1 
HETATM 4672 O O1  . EDO C 3 .   ? 17.880  -44.004 -6.950  1.00 26.89 ? 702  EDO B O1  1 
HETATM 4673 C C2  . EDO C 3 .   ? 16.463  -43.315 -5.106  1.00 26.30 ? 702  EDO B C2  1 
HETATM 4674 O O2  . EDO C 3 .   ? 16.156  -42.028 -5.523  1.00 23.21 ? 702  EDO B O2  1 
HETATM 4675 C C1  . EDO D 3 .   ? 29.921  -22.157 -5.119  1.00 31.27 ? 703  EDO B C1  1 
HETATM 4676 O O1  . EDO D 3 .   ? 30.145  -20.762 -5.175  1.00 23.00 ? 703  EDO B O1  1 
HETATM 4677 C C2  . EDO D 3 .   ? 30.895  -22.876 -4.258  1.00 29.32 ? 703  EDO B C2  1 
HETATM 4678 O O2  . EDO D 3 .   ? 32.140  -23.163 -4.874  1.00 28.19 ? 703  EDO B O2  1 
HETATM 4679 C C1  . PGE E 4 .   ? 2.847   -46.188 -5.133  1.00 53.30 ? 704  PGE B C1  1 
HETATM 4680 O O1  . PGE E 4 .   ? 2.142   -47.316 -4.683  1.00 60.44 ? 704  PGE B O1  1 
HETATM 4681 C C2  . PGE E 4 .   ? 2.021   -44.952 -5.064  1.00 55.44 ? 704  PGE B C2  1 
HETATM 4682 O O2  . PGE E 4 .   ? 2.865   -43.806 -4.974  1.00 53.02 ? 704  PGE B O2  1 
HETATM 4683 C C3  . PGE E 4 .   ? 3.398   -43.583 -3.672  1.00 41.82 ? 704  PGE B C3  1 
HETATM 4684 C C4  . PGE E 4 .   ? 2.865   -42.320 -3.083  1.00 41.72 ? 704  PGE B C4  1 
HETATM 4685 O O4  . PGE E 4 .   ? 1.228   -44.276 0.909   1.00 40.70 ? 704  PGE B O4  1 
HETATM 4686 C C6  . PGE E 4 .   ? 2.117   -43.288 0.373   1.00 37.21 ? 704  PGE B C6  1 
HETATM 4687 C C5  . PGE E 4 .   ? 1.953   -43.162 -1.076  1.00 34.87 ? 704  PGE B C5  1 
HETATM 4688 O O3  . PGE E 4 .   ? 2.983   -42.378 -1.662  1.00 43.00 ? 704  PGE B O3  1 
HETATM 4689 C C1  . EDO F 3 .   ? 1.716   -19.407 -4.953  1.00 45.37 ? 705  EDO B C1  1 
HETATM 4690 O O1  . EDO F 3 .   ? 1.369   -20.678 -5.486  1.00 45.66 ? 705  EDO B O1  1 
HETATM 4691 C C2  . EDO F 3 .   ? 2.178   -19.573 -3.574  1.00 40.40 ? 705  EDO B C2  1 
HETATM 4692 O O2  . EDO F 3 .   ? 2.424   -18.405 -2.826  1.00 37.39 ? 705  EDO B O2  1 
HETATM 4693 C C1  . EDO G 3 .   ? 26.208  -15.677 -0.503  1.00 31.76 ? 706  EDO B C1  1 
HETATM 4694 O O1  . EDO G 3 .   ? 27.248  -16.371 0.212   1.00 31.10 ? 706  EDO B O1  1 
HETATM 4695 C C2  . EDO G 3 .   ? 25.079  -15.067 0.315   1.00 34.77 ? 706  EDO B C2  1 
HETATM 4696 O O2  . EDO G 3 .   ? 25.165  -13.608 0.417   1.00 35.55 ? 706  EDO B O2  1 
HETATM 4697 N N   . NO3 H 5 .   ? 6.628   -42.554 -3.069  1.00 31.41 ? 707  NO3 B N   1 
HETATM 4698 O O1  . NO3 H 5 .   ? 7.051   -43.608 -2.655  1.00 27.67 ? 707  NO3 B O1  1 
HETATM 4699 O O2  . NO3 H 5 .   ? 6.107   -41.746 -2.312  1.00 36.72 ? 707  NO3 B O2  1 
HETATM 4700 O O3  . NO3 H 5 .   ? 6.720   -42.286 -4.264  1.00 33.95 ? 707  NO3 B O3  1 
HETATM 4701 N N   . NO3 I 5 .   ? 17.063  -2.210  7.907   1.00 42.02 ? 708  NO3 B N   1 
HETATM 4702 O O1  . NO3 I 5 .   ? 16.255  -2.692  7.113   1.00 40.36 ? 708  NO3 B O1  1 
HETATM 4703 O O2  . NO3 I 5 .   ? 17.790  -2.950  8.586   1.00 40.84 ? 708  NO3 B O2  1 
HETATM 4704 O O3  . NO3 I 5 .   ? 17.153  -0.987  8.019   1.00 42.17 ? 708  NO3 B O3  1 
HETATM 4705 C C   . TRS J 6 .   ? 21.004  -0.838  -8.176  1.00 20.00 ? 709  TRS B C   1 
HETATM 4706 C C1  . TRS J 6 .   ? 19.916  0.113   -7.691  1.00 20.00 ? 709  TRS B C1  1 
HETATM 4707 C C2  . TRS J 6 .   ? 22.154  -0.041  -8.780  1.00 20.00 ? 709  TRS B C2  1 
HETATM 4708 C C3  . TRS J 6 .   ? 21.495  -1.724  -7.036  1.00 20.00 ? 709  TRS B C3  1 
HETATM 4709 N N   . TRS J 6 .   ? 20.423  -1.708  -9.247  1.00 20.00 ? 709  TRS B N   1 
HETATM 4710 O O1  . TRS J 6 .   ? 18.932  -0.547  -6.912  1.00 20.00 ? 709  TRS B O1  1 
HETATM 4711 O O2  . TRS J 6 .   ? 23.234  -0.867  -9.183  1.00 20.00 ? 709  TRS B O2  1 
HETATM 4712 O O3  . TRS J 6 .   ? 21.920  -0.959  -5.922  1.00 20.00 ? 709  TRS B O3  1 
HETATM 4713 H H11 . TRS J 6 .   ? 19.439  0.575   -8.554  1.00 20.00 ? 709  TRS B H11 1 
HETATM 4714 H H12 . TRS J 6 .   ? 20.374  0.902   -7.097  1.00 20.00 ? 709  TRS B H12 1 
HETATM 4715 H H21 . TRS J 6 .   ? 22.509  0.680   -8.045  1.00 20.00 ? 709  TRS B H21 1 
HETATM 4716 H H22 . TRS J 6 .   ? 21.786  0.512   -9.642  1.00 20.00 ? 709  TRS B H22 1 
HETATM 4717 H H31 . TRS J 6 .   ? 22.322  -2.338  -7.389  1.00 20.00 ? 709  TRS B H31 1 
HETATM 4718 H H32 . TRS J 6 .   ? 20.690  -2.391  -6.730  1.00 20.00 ? 709  TRS B H32 1 
HETATM 4719 H HN1 . TRS J 6 .   ? 20.594  -2.706  -9.030  1.00 20.00 ? 709  TRS B HN1 1 
HETATM 4720 H HN2 . TRS J 6 .   ? 20.856  -1.492  -10.163 1.00 20.00 ? 709  TRS B HN2 1 
HETATM 4721 H HN3 . TRS J 6 .   ? 19.402  -1.558  -9.327  1.00 20.00 ? 709  TRS B HN3 1 
HETATM 4722 H HO1 . TRS J 6 .   ? 18.742  -1.411  -7.310  1.00 20.00 ? 709  TRS B HO1 1 
HETATM 4723 H HO2 . TRS J 6 .   ? 22.891  -1.732  -9.454  1.00 20.00 ? 709  TRS B HO2 1 
HETATM 4724 H HO3 . TRS J 6 .   ? 22.741  -0.499  -6.156  1.00 20.00 ? 709  TRS B HO3 1 
HETATM 4725 O O   . HOH K 7 .   ? 3.917   -39.590 -13.597 1.00 30.00 ? 801  HOH B O   1 
HETATM 4726 O O   . HOH K 7 .   ? 16.960  -55.943 21.842  1.00 44.46 ? 802  HOH B O   1 
HETATM 4727 O O   . HOH K 7 .   ? 30.131  -43.375 26.850  1.00 28.60 ? 803  HOH B O   1 
HETATM 4728 O O   . HOH K 7 .   ? 6.495   -6.179  -9.750  1.00 46.26 ? 804  HOH B O   1 
HETATM 4729 O O   . HOH K 7 .   ? 39.437  -17.780 -9.843  1.00 32.57 ? 805  HOH B O   1 
HETATM 4730 O O   . HOH K 7 .   ? 36.319  -6.487  32.717  1.00 40.26 ? 806  HOH B O   1 
HETATM 4731 O O   . HOH K 7 .   ? 43.176  -7.989  -3.846  1.00 29.06 ? 807  HOH B O   1 
HETATM 4732 O O   . HOH K 7 .   ? 38.594  2.057   9.390   1.00 42.04 ? 808  HOH B O   1 
HETATM 4733 O O   . HOH K 7 .   ? 23.834  7.885   24.387  1.00 52.45 ? 809  HOH B O   1 
HETATM 4734 O O   . HOH K 7 .   ? 33.165  3.995   6.889   1.00 44.82 ? 810  HOH B O   1 
HETATM 4735 O O   . HOH K 7 .   ? -2.876  -23.031 4.328   1.00 32.97 ? 811  HOH B O   1 
HETATM 4736 O O   . HOH K 7 .   ? 4.292   -18.562 -22.954 1.00 44.49 ? 812  HOH B O   1 
HETATM 4737 O O   . HOH K 7 .   ? 35.707  -23.490 26.103  1.00 48.69 ? 813  HOH B O   1 
HETATM 4738 O O   . HOH K 7 .   ? 23.052  -12.583 30.830  1.00 26.34 ? 814  HOH B O   1 
HETATM 4739 O O   . HOH K 7 .   ? 45.041  -6.397  2.834   1.00 42.08 ? 815  HOH B O   1 
HETATM 4740 O O   . HOH K 7 .   ? 12.764  -20.625 -23.521 1.00 26.89 ? 816  HOH B O   1 
HETATM 4741 O O   . HOH K 7 .   ? 34.856  -10.758 -15.857 1.00 50.39 ? 817  HOH B O   1 
HETATM 4742 O O   . HOH K 7 .   ? -8.643  -25.131 7.626   1.00 51.10 ? 818  HOH B O   1 
HETATM 4743 O O   . HOH K 7 .   ? 26.669  -21.934 17.918  1.00 34.54 ? 819  HOH B O   1 
HETATM 4744 O O   . HOH K 7 .   ? 1.004   -17.235 4.008   1.00 28.52 ? 820  HOH B O   1 
HETATM 4745 O O   . HOH K 7 .   ? -0.398  -15.198 5.018   1.00 31.82 ? 821  HOH B O   1 
HETATM 4746 O O   . HOH K 7 .   ? 7.322   -45.458 -4.441  1.00 26.38 ? 822  HOH B O   1 
HETATM 4747 O O   . HOH K 7 .   ? 11.804  1.353   -2.343  1.00 47.14 ? 823  HOH B O   1 
HETATM 4748 O O   . HOH K 7 .   ? 13.773  -42.252 12.111  1.00 34.20 ? 824  HOH B O   1 
HETATM 4749 O O   . HOH K 7 .   ? 25.500  4.831   33.082  1.00 38.71 ? 825  HOH B O   1 
HETATM 4750 O O   . HOH K 7 .   ? -6.433  -9.825  10.125  1.00 47.30 ? 826  HOH B O   1 
HETATM 4751 O O   . HOH K 7 .   ? 9.855   -6.268  -17.323 1.00 48.71 ? 828  HOH B O   1 
HETATM 4752 O O   . HOH K 7 .   ? 10.104  -7.460  2.458   1.00 25.41 ? 829  HOH B O   1 
HETATM 4753 O O   . HOH K 7 .   ? 27.527  -43.460 -15.358 1.00 25.96 ? 830  HOH B O   1 
HETATM 4754 O O   . HOH K 7 .   ? 18.461  -24.661 -12.192 1.00 21.13 ? 831  HOH B O   1 
HETATM 4755 O O   . HOH K 7 .   ? 41.749  -8.850  21.551  1.00 33.60 ? 832  HOH B O   1 
HETATM 4756 O O   . HOH K 7 .   ? 14.630  -24.619 18.011  1.00 27.36 ? 833  HOH B O   1 
HETATM 4757 O O   . HOH K 7 .   ? -1.535  -24.518 -5.126  1.00 23.43 ? 834  HOH B O   1 
HETATM 4758 O O   . HOH K 7 .   ? 18.067  -48.635 -31.533 1.00 55.71 ? 835  HOH B O   1 
HETATM 4759 O O   . HOH K 7 .   ? 32.057  -24.605 -14.458 1.00 47.53 ? 836  HOH B O   1 
HETATM 4760 O O   . HOH K 7 .   ? 34.021  -19.092 7.866   1.00 19.80 ? 837  HOH B O   1 
HETATM 4761 O O   . HOH K 7 .   ? 23.653  -11.484 0.329   1.00 33.14 ? 838  HOH B O   1 
HETATM 4762 O O   . HOH K 7 .   ? 26.423  -32.960 -27.561 1.00 40.32 ? 839  HOH B O   1 
HETATM 4763 O O   . HOH K 7 .   ? 17.153  -5.456  8.178   1.00 46.85 ? 840  HOH B O   1 
HETATM 4764 O O   . HOH K 7 .   ? 31.109  -17.091 32.484  1.00 42.84 ? 841  HOH B O   1 
HETATM 4765 O O   . HOH K 7 .   ? 20.650  -45.742 25.631  1.00 42.01 ? 842  HOH B O   1 
HETATM 4766 O O   . HOH K 7 .   ? -5.665  -26.547 -12.426 1.00 27.66 ? 843  HOH B O   1 
HETATM 4767 O O   . HOH K 7 .   ? 35.850  1.854   25.827  1.00 44.81 ? 844  HOH B O   1 
HETATM 4768 O O   . HOH K 7 .   ? 8.761   -12.981 -15.983 1.00 41.25 ? 845  HOH B O   1 
HETATM 4769 O O   . HOH K 7 .   ? 26.124  0.649   -0.610  1.00 36.97 ? 846  HOH B O   1 
HETATM 4770 O O   . HOH K 7 .   ? 29.435  -12.091 33.688  1.00 50.94 ? 847  HOH B O   1 
HETATM 4771 O O   . HOH K 7 .   ? 23.611  -28.964 28.649  1.00 55.10 ? 848  HOH B O   1 
HETATM 4772 O O   . HOH K 7 .   ? -9.278  -27.005 -4.725  1.00 30.06 ? 849  HOH B O   1 
HETATM 4773 O O   . HOH K 7 .   ? 3.307   -44.604 17.187  1.00 36.25 ? 850  HOH B O   1 
HETATM 4774 O O   . HOH K 7 .   ? 37.789  6.535   10.748  1.00 47.35 ? 851  HOH B O   1 
HETATM 4775 O O   . HOH K 7 .   ? 2.286   -16.255 -15.980 1.00 35.26 ? 852  HOH B O   1 
HETATM 4776 O O   . HOH K 7 .   ? 27.192  -4.352  5.643   1.00 22.94 ? 853  HOH B O   1 
HETATM 4777 O O   . HOH K 7 .   ? 11.541  -23.803 25.504  1.00 48.43 ? 854  HOH B O   1 
HETATM 4778 O O   . HOH K 7 .   ? 26.811  -43.372 -11.435 1.00 19.74 ? 855  HOH B O   1 
HETATM 4779 O O   . HOH K 7 .   ? 51.507  -13.489 8.327   1.00 42.50 ? 856  HOH B O   1 
HETATM 4780 O O   . HOH K 7 .   ? 0.362   -41.929 -10.875 1.00 35.92 ? 857  HOH B O   1 
HETATM 4781 O O   . HOH K 7 .   ? 26.121  -4.963  -12.346 1.00 32.50 ? 858  HOH B O   1 
HETATM 4782 O O   . HOH K 7 .   ? 36.694  -1.338  33.865  1.00 38.48 ? 859  HOH B O   1 
HETATM 4783 O O   . HOH K 7 .   ? 36.793  -9.665  -10.467 1.00 34.10 ? 860  HOH B O   1 
HETATM 4784 O O   . HOH K 7 .   ? 36.728  -3.181  -0.026  1.00 27.34 ? 861  HOH B O   1 
HETATM 4785 O O   . HOH K 7 .   ? 11.933  -43.749 15.137  1.00 24.75 ? 862  HOH B O   1 
HETATM 4786 O O   . HOH K 7 .   ? 22.360  -0.844  25.714  1.00 38.37 ? 863  HOH B O   1 
HETATM 4787 O O   . HOH K 7 .   ? 42.105  -4.980  26.925  1.00 45.04 ? 864  HOH B O   1 
HETATM 4788 O O   . HOH K 7 .   ? 1.938   -23.207 8.477   1.00 46.39 ? 865  HOH B O   1 
HETATM 4789 O O   . HOH K 7 .   ? 44.128  -11.845 22.912  1.00 34.54 ? 866  HOH B O   1 
HETATM 4790 O O   . HOH K 7 .   ? -10.398 -36.310 -16.344 1.00 45.64 ? 867  HOH B O   1 
HETATM 4791 O O   . HOH K 7 .   ? 51.789  -11.781 12.964  1.00 39.20 ? 868  HOH B O   1 
HETATM 4792 O O   . HOH K 7 .   ? 38.029  -20.380 14.510  1.00 21.59 ? 869  HOH B O   1 
HETATM 4793 O O   . HOH K 7 .   ? 10.808  -37.776 -17.035 1.00 21.23 ? 870  HOH B O   1 
HETATM 4794 O O   . HOH K 7 .   ? -3.944  -43.395 -5.074  1.00 49.88 ? 871  HOH B O   1 
HETATM 4795 O O   . HOH K 7 .   ? 17.152  -39.107 1.423   1.00 16.03 ? 872  HOH B O   1 
HETATM 4796 O O   . HOH K 7 .   ? 18.635  -28.542 19.573  1.00 38.02 ? 873  HOH B O   1 
HETATM 4797 O O   . HOH K 7 .   ? 36.603  -38.409 -25.717 1.00 29.79 ? 874  HOH B O   1 
HETATM 4798 O O   . HOH K 7 .   ? -3.983  -16.623 10.448  1.00 44.10 ? 875  HOH B O   1 
HETATM 4799 O O   . HOH K 7 .   ? 37.061  -22.947 -0.941  1.00 16.00 ? 876  HOH B O   1 
HETATM 4800 O O   . HOH K 7 .   ? 18.370  -21.577 31.051  1.00 47.95 ? 877  HOH B O   1 
HETATM 4801 O O   . HOH K 7 .   ? 35.622  -38.052 -17.896 1.00 25.49 ? 878  HOH B O   1 
HETATM 4802 O O   . HOH K 7 .   ? 15.811  -40.113 11.633  1.00 22.41 ? 879  HOH B O   1 
HETATM 4803 O O   . HOH K 7 .   ? 8.348   -44.835 -9.263  1.00 19.06 ? 880  HOH B O   1 
HETATM 4804 O O   . HOH K 7 .   ? -2.249  -7.701  -5.744  1.00 34.18 ? 881  HOH B O   1 
HETATM 4805 O O   . HOH K 7 .   ? 33.269  -50.545 22.892  1.00 25.91 ? 882  HOH B O   1 
HETATM 4806 O O   . HOH K 7 .   ? 23.009  3.898   5.459   1.00 31.91 ? 883  HOH B O   1 
HETATM 4807 O O   . HOH K 7 .   ? 44.191  -18.951 18.248  1.00 28.63 ? 884  HOH B O   1 
HETATM 4808 O O   . HOH K 7 .   ? 1.029   -21.792 -9.039  1.00 34.29 ? 885  HOH B O   1 
HETATM 4809 O O   . HOH K 7 .   ? -1.226  -28.851 -21.940 1.00 32.55 ? 886  HOH B O   1 
HETATM 4810 O O   . HOH K 7 .   ? 27.479  -22.368 -16.811 1.00 24.84 ? 887  HOH B O   1 
HETATM 4811 O O   . HOH K 7 .   ? 41.985  -58.193 19.623  1.00 34.57 ? 888  HOH B O   1 
HETATM 4812 O O   . HOH K 7 .   ? 31.891  6.525   28.807  1.00 32.52 ? 889  HOH B O   1 
HETATM 4813 O O   . HOH K 7 .   ? -4.573  -40.718 -4.521  1.00 32.29 ? 890  HOH B O   1 
HETATM 4814 O O   . HOH K 7 .   ? 20.854  -43.045 -25.807 1.00 30.00 ? 891  HOH B O   1 
HETATM 4815 O O   . HOH K 7 .   ? 24.938  -53.441 24.304  1.00 22.86 ? 892  HOH B O   1 
HETATM 4816 O O   . HOH K 7 .   ? 1.826   -25.674 -27.055 1.00 35.52 ? 893  HOH B O   1 
HETATM 4817 O O   . HOH K 7 .   ? 31.531  -54.404 27.057  1.00 34.18 ? 894  HOH B O   1 
HETATM 4818 O O   . HOH K 7 .   ? 17.020  -43.851 10.460  1.00 18.58 ? 895  HOH B O   1 
HETATM 4819 O O   . HOH K 7 .   ? 42.488  -21.477 14.385  1.00 42.64 ? 896  HOH B O   1 
HETATM 4820 O O   . HOH K 7 .   ? 29.579  8.914   10.060  1.00 39.49 ? 897  HOH B O   1 
HETATM 4821 O O   . HOH K 7 .   ? 3.625   -12.383 -11.536 1.00 30.00 ? 898  HOH B O   1 
HETATM 4822 O O   . HOH K 7 .   ? 43.455  -8.129  -0.051  1.00 34.56 ? 899  HOH B O   1 
HETATM 4823 O O   . HOH K 7 .   ? 21.792  -24.743 24.985  1.00 30.00 ? 900  HOH B O   1 
HETATM 4824 O O   . HOH K 7 .   ? 8.635   -15.282 -17.167 1.00 40.50 ? 901  HOH B O   1 
HETATM 4825 O O   . HOH K 7 .   ? 23.928  -12.252 -18.228 1.00 47.73 ? 902  HOH B O   1 
HETATM 4826 O O   . HOH K 7 .   ? 47.756  -17.929 0.136   1.00 43.65 ? 903  HOH B O   1 
HETATM 4827 O O   . HOH K 7 .   ? 27.867  5.725   12.460  1.00 27.50 ? 904  HOH B O   1 
HETATM 4828 O O   . HOH K 7 .   ? 36.212  -57.201 22.362  1.00 34.55 ? 905  HOH B O   1 
HETATM 4829 O O   . HOH K 7 .   ? 14.659  3.315   -3.541  1.00 48.16 ? 906  HOH B O   1 
HETATM 4830 O O   . HOH K 7 .   ? 28.020  2.888   20.545  1.00 31.97 ? 907  HOH B O   1 
HETATM 4831 O O   . HOH K 7 .   ? 37.209  -1.809  26.434  1.00 30.73 ? 908  HOH B O   1 
HETATM 4832 O O   . HOH K 7 .   ? 35.001  -8.477  31.137  1.00 30.36 ? 909  HOH B O   1 
HETATM 4833 O O   . HOH K 7 .   ? 45.271  -21.666 9.396   1.00 42.81 ? 910  HOH B O   1 
HETATM 4834 O O   . HOH K 7 .   ? 18.491  -15.785 26.405  1.00 27.77 ? 911  HOH B O   1 
HETATM 4835 O O   . HOH K 7 .   ? 36.850  -30.854 -10.111 1.00 16.72 ? 912  HOH B O   1 
HETATM 4836 O O   . HOH K 7 .   ? 10.134  -15.472 -21.520 1.00 47.20 ? 913  HOH B O   1 
HETATM 4837 O O   . HOH K 7 .   ? 1.181   -12.678 -1.268  1.00 28.04 ? 914  HOH B O   1 
HETATM 4838 O O   . HOH K 7 .   ? 27.246  -24.887 -18.177 1.00 35.47 ? 915  HOH B O   1 
HETATM 4839 O O   . HOH K 7 .   ? 32.676  -9.084  8.855   1.00 18.19 ? 916  HOH B O   1 
HETATM 4840 O O   . HOH K 7 .   ? 16.687  -43.908 26.796  1.00 38.37 ? 917  HOH B O   1 
HETATM 4841 O O   . HOH K 7 .   ? 14.317  -2.162  17.541  1.00 34.71 ? 918  HOH B O   1 
HETATM 4842 O O   . HOH K 7 .   ? 5.760   -41.417 -6.826  1.00 28.27 ? 919  HOH B O   1 
HETATM 4843 O O   . HOH K 7 .   ? 13.333  -10.336 23.460  1.00 47.29 ? 920  HOH B O   1 
HETATM 4844 O O   . HOH K 7 .   ? 46.002  -31.025 -11.812 1.00 21.41 ? 921  HOH B O   1 
HETATM 4845 O O   . HOH K 7 .   ? 17.382  -41.967 -8.682  1.00 30.59 ? 922  HOH B O   1 
HETATM 4846 O O   . HOH K 7 .   ? -1.743  -24.226 -7.916  1.00 20.97 ? 923  HOH B O   1 
HETATM 4847 O O   . HOH K 7 .   ? 5.382   -17.502 -20.473 1.00 43.05 ? 924  HOH B O   1 
HETATM 4848 O O   . HOH K 7 .   ? 26.817  5.658   6.723   1.00 52.21 ? 925  HOH B O   1 
HETATM 4849 O O   . HOH K 7 .   ? 20.913  1.121   -12.924 1.00 48.39 ? 926  HOH B O   1 
HETATM 4850 O O   . HOH K 7 .   ? 30.165  -30.311 -7.957  1.00 14.72 ? 927  HOH B O   1 
HETATM 4851 O O   . HOH K 7 .   ? 15.234  -13.424 11.004  1.00 32.82 ? 928  HOH B O   1 
HETATM 4852 O O   . HOH K 7 .   ? -9.434  -31.616 -11.659 1.00 26.63 ? 929  HOH B O   1 
HETATM 4853 O O   . HOH K 7 .   ? 17.735  5.574   14.579  1.00 33.66 ? 930  HOH B O   1 
HETATM 4854 O O   . HOH K 7 .   ? 19.448  -40.281 -8.662  1.00 30.00 ? 931  HOH B O   1 
HETATM 4855 O O   . HOH K 7 .   ? -3.671  -37.021 6.919   1.00 37.79 ? 932  HOH B O   1 
HETATM 4856 O O   . HOH K 7 .   ? 12.731  -5.957  12.306  1.00 46.52 ? 933  HOH B O   1 
HETATM 4857 O O   . HOH K 7 .   ? 18.510  -3.405  26.696  1.00 32.14 ? 934  HOH B O   1 
HETATM 4858 O O   . HOH K 7 .   ? 6.441   -8.089  12.421  1.00 48.81 ? 935  HOH B O   1 
HETATM 4859 O O   . HOH K 7 .   ? 20.924  -37.127 -0.212  1.00 30.11 ? 936  HOH B O   1 
HETATM 4860 O O   . HOH K 7 .   ? 37.963  -27.638 -7.782  1.00 30.00 ? 937  HOH B O   1 
HETATM 4861 O O   . HOH K 7 .   ? 14.817  -8.871  30.525  1.00 40.20 ? 938  HOH B O   1 
HETATM 4862 O O   . HOH K 7 .   ? 42.206  -12.391 -8.308  1.00 36.94 ? 939  HOH B O   1 
HETATM 4863 O O   . HOH K 7 .   ? 25.202  -1.190  26.932  1.00 30.00 ? 940  HOH B O   1 
HETATM 4864 O O   . HOH K 7 .   ? 9.155   -49.633 10.397  1.00 26.99 ? 941  HOH B O   1 
HETATM 4865 O O   . HOH K 7 .   ? 21.541  2.981   22.917  1.00 27.61 ? 942  HOH B O   1 
HETATM 4866 O O   . HOH K 7 .   ? 22.110  -6.983  -1.278  1.00 40.29 ? 943  HOH B O   1 
HETATM 4867 O O   . HOH K 7 .   ? 13.940  -21.583 12.734  1.00 21.78 ? 944  HOH B O   1 
HETATM 4868 O O   . HOH K 7 .   ? 30.856  -16.156 -14.871 1.00 30.21 ? 945  HOH B O   1 
HETATM 4869 O O   . HOH K 7 .   ? 32.672  -33.541 -28.449 1.00 55.27 ? 946  HOH B O   1 
HETATM 4870 O O   . HOH K 7 .   ? 34.424  1.563   32.256  1.00 31.87 ? 947  HOH B O   1 
HETATM 4871 O O   . HOH K 7 .   ? 19.118  5.227   11.900  1.00 36.04 ? 948  HOH B O   1 
HETATM 4872 O O   . HOH K 7 .   ? 26.741  -39.768 -8.248  1.00 20.60 ? 949  HOH B O   1 
HETATM 4873 O O   . HOH K 7 .   ? 28.181  -16.295 -17.924 1.00 54.87 ? 950  HOH B O   1 
HETATM 4874 O O   . HOH K 7 .   ? 41.283  -9.062  -1.339  1.00 21.61 ? 951  HOH B O   1 
HETATM 4875 O O   . HOH K 7 .   ? 23.814  -43.384 25.648  1.00 24.08 ? 952  HOH B O   1 
HETATM 4876 O O   . HOH K 7 .   ? 42.896  -9.043  14.665  1.00 28.96 ? 954  HOH B O   1 
HETATM 4877 O O   . HOH K 7 .   ? 21.611  -46.206 -13.556 1.00 17.74 ? 955  HOH B O   1 
HETATM 4878 O O   . HOH K 7 .   ? -11.304 -31.476 -9.793  1.00 29.16 ? 956  HOH B O   1 
HETATM 4879 O O   . HOH K 7 .   ? -2.443  -34.301 5.640   1.00 27.50 ? 957  HOH B O   1 
HETATM 4880 O O   . HOH K 7 .   ? 31.850  -19.477 -9.953  1.00 30.00 ? 958  HOH B O   1 
HETATM 4881 O O   . HOH K 7 .   ? 14.716  -50.923 26.156  1.00 48.02 ? 959  HOH B O   1 
HETATM 4882 O O   . HOH K 7 .   ? 30.537  -10.155 7.568   1.00 21.04 ? 960  HOH B O   1 
HETATM 4883 O O   . HOH K 7 .   ? 10.397  -16.056 21.575  1.00 57.04 ? 961  HOH B O   1 
HETATM 4884 O O   . HOH K 7 .   ? 8.662   -17.145 11.485  1.00 39.78 ? 963  HOH B O   1 
HETATM 4885 O O   . HOH K 7 .   ? 21.948  -28.974 7.267   1.00 14.88 ? 964  HOH B O   1 
HETATM 4886 O O   . HOH K 7 .   ? -2.732  -27.451 -16.033 1.00 22.21 ? 965  HOH B O   1 
HETATM 4887 O O   . HOH K 7 .   ? 19.605  -10.426 0.624   1.00 44.43 ? 966  HOH B O   1 
HETATM 4888 O O   . HOH K 7 .   ? 12.771  -28.144 -16.253 1.00 17.12 ? 967  HOH B O   1 
HETATM 4889 O O   . HOH K 7 .   ? 32.496  4.958   20.932  1.00 43.49 ? 968  HOH B O   1 
HETATM 4890 O O   . HOH K 7 .   ? 25.123  -34.750 6.665   1.00 37.85 ? 969  HOH B O   1 
HETATM 4891 O O   . HOH K 7 .   ? 18.186  -34.856 15.545  1.00 22.53 ? 970  HOH B O   1 
HETATM 4892 O O   . HOH K 7 .   ? 13.261  -37.288 -19.662 1.00 30.00 ? 971  HOH B O   1 
HETATM 4893 O O   . HOH K 7 .   ? -2.889  -24.318 10.434  1.00 47.58 ? 972  HOH B O   1 
HETATM 4894 O O   . HOH K 7 .   ? 2.334   -22.471 13.850  1.00 44.20 ? 973  HOH B O   1 
HETATM 4895 O O   . HOH K 7 .   ? 25.853  -25.392 13.735  1.00 21.23 ? 974  HOH B O   1 
HETATM 4896 O O   . HOH K 7 .   ? 3.657   -11.093 -13.767 1.00 37.96 ? 975  HOH B O   1 
HETATM 4897 O O   . HOH K 7 .   ? 7.833   -47.890 3.848   1.00 25.04 ? 976  HOH B O   1 
HETATM 4898 O O   . HOH K 7 .   ? 46.549  -10.128 -3.463  1.00 45.31 ? 977  HOH B O   1 
HETATM 4899 O O   . HOH K 7 .   ? 0.431   -21.007 7.429   1.00 27.91 ? 978  HOH B O   1 
HETATM 4900 O O   . HOH K 7 .   ? 12.056  -24.015 -10.948 1.00 15.90 ? 979  HOH B O   1 
HETATM 4901 O O   . HOH K 7 .   ? 45.466  -14.707 1.313   1.00 30.00 ? 980  HOH B O   1 
HETATM 4902 O O   . HOH K 7 .   ? 16.078  -15.409 25.021  1.00 35.97 ? 981  HOH B O   1 
HETATM 4903 O O   . HOH K 7 .   ? 30.830  -53.812 19.092  1.00 30.00 ? 982  HOH B O   1 
HETATM 4904 O O   . HOH K 7 .   ? 24.785  -28.137 0.217   1.00 30.00 ? 983  HOH B O   1 
HETATM 4905 O O   . HOH K 7 .   ? 35.210  -4.205  34.479  1.00 45.39 ? 984  HOH B O   1 
HETATM 4906 O O   . HOH K 7 .   ? 36.711  -20.180 -1.169  1.00 16.00 ? 985  HOH B O   1 
HETATM 4907 O O   . HOH K 7 .   ? 8.281   -43.112 15.562  1.00 27.31 ? 986  HOH B O   1 
HETATM 4908 O O   . HOH K 7 .   ? 15.362  -15.763 29.391  1.00 59.02 ? 987  HOH B O   1 
HETATM 4909 O O   . HOH K 7 .   ? 27.649  6.723   28.946  1.00 35.74 ? 988  HOH B O   1 
HETATM 4910 O O   . HOH K 7 .   ? 5.255   -47.472 2.302   1.00 30.00 ? 989  HOH B O   1 
HETATM 4911 O O   . HOH K 7 .   ? 4.086   -6.449  9.265   1.00 38.19 ? 990  HOH B O   1 
HETATM 4912 O O   . HOH K 7 .   ? 12.166  -33.289 11.670  1.00 27.36 ? 991  HOH B O   1 
HETATM 4913 O O   . HOH K 7 .   ? 39.617  -7.642  15.272  1.00 28.69 ? 992  HOH B O   1 
HETATM 4914 O O   . HOH K 7 .   ? 37.202  -7.735  13.993  1.00 23.15 ? 993  HOH B O   1 
HETATM 4915 O O   . HOH K 7 .   ? 24.045  2.097   -0.849  1.00 33.52 ? 994  HOH B O   1 
HETATM 4916 O O   . HOH K 7 .   ? 4.661   -18.414 14.350  1.00 47.66 ? 995  HOH B O   1 
HETATM 4917 O O   . HOH K 7 .   ? 10.474  -51.848 14.577  1.00 35.79 ? 996  HOH B O   1 
HETATM 4918 O O   . HOH K 7 .   ? 18.704  -2.692  22.259  1.00 24.21 ? 997  HOH B O   1 
HETATM 4919 O O   . HOH K 7 .   ? 25.945  -27.597 -22.447 1.00 47.63 ? 998  HOH B O   1 
HETATM 4920 O O   . HOH K 7 .   ? 32.775  0.985   35.658  1.00 30.95 ? 999  HOH B O   1 
HETATM 4921 O O   . HOH K 7 .   ? 29.274  -31.455 -33.529 1.00 38.30 ? 1000 HOH B O   1 
HETATM 4922 O O   . HOH K 7 .   ? 0.771   -20.093 -11.180 1.00 40.09 ? 1001 HOH B O   1 
HETATM 4923 O O   . HOH K 7 .   ? 23.946  -35.234 1.789   1.00 20.08 ? 1002 HOH B O   1 
HETATM 4924 O O   . HOH K 7 .   ? 33.084  -20.355 -2.562  1.00 30.00 ? 1003 HOH B O   1 
HETATM 4925 O O   . HOH K 7 .   ? -5.729  -37.897 -9.792  1.00 30.00 ? 1004 HOH B O   1 
HETATM 4926 O O   . HOH K 7 .   ? 42.818  1.665   21.466  1.00 45.88 ? 1005 HOH B O   1 
HETATM 4927 O O   . HOH K 7 .   ? 45.449  -19.774 2.999   1.00 39.32 ? 1006 HOH B O   1 
HETATM 4928 O O   . HOH K 7 .   ? 10.764  -11.670 -10.536 1.00 28.60 ? 1007 HOH B O   1 
HETATM 4929 O O   . HOH K 7 .   ? 3.109   -23.084 -5.499  1.00 32.27 ? 1008 HOH B O   1 
HETATM 4930 O O   . HOH K 7 .   ? -2.064  -42.414 2.092   1.00 28.72 ? 1009 HOH B O   1 
HETATM 4931 O O   . HOH K 7 .   ? 7.892   2.382   -1.746  1.00 48.26 ? 1010 HOH B O   1 
HETATM 4932 O O   . HOH K 7 .   ? 29.214  -18.192 16.177  1.00 29.38 ? 1011 HOH B O   1 
HETATM 4933 O O   . HOH K 7 .   ? -3.575  -25.026 -3.345  1.00 20.60 ? 1012 HOH B O   1 
HETATM 4934 O O   . HOH K 7 .   ? 15.562  4.632   14.887  1.00 53.53 ? 1013 HOH B O   1 
HETATM 4935 O O   . HOH K 7 .   ? 15.478  -23.844 12.248  1.00 19.30 ? 1014 HOH B O   1 
HETATM 4936 O O   . HOH K 7 .   ? 44.066  -21.571 6.996   1.00 49.86 ? 1015 HOH B O   1 
HETATM 4937 O O   . HOH K 7 .   ? -8.494  -32.671 -18.150 1.00 33.71 ? 1016 HOH B O   1 
HETATM 4938 O O   . HOH K 7 .   ? -1.239  -37.134 -15.848 1.00 28.87 ? 1017 HOH B O   1 
HETATM 4939 O O   . HOH K 7 .   ? 11.253  -20.013 13.852  1.00 30.00 ? 1018 HOH B O   1 
HETATM 4940 O O   . HOH K 7 .   ? 22.680  -24.529 -23.205 1.00 46.42 ? 1019 HOH B O   1 
HETATM 4941 O O   . HOH K 7 .   ? 40.921  -25.724 15.658  1.00 46.47 ? 1020 HOH B O   1 
HETATM 4942 O O   . HOH K 7 .   ? 27.720  -5.887  3.531   1.00 25.16 ? 1021 HOH B O   1 
HETATM 4943 O O   . HOH K 7 .   ? 37.956  -34.390 -20.177 1.00 47.41 ? 1022 HOH B O   1 
HETATM 4944 O O   . HOH K 7 .   ? 38.295  1.817   25.202  1.00 53.74 ? 1023 HOH B O   1 
HETATM 4945 O O   . HOH K 7 .   ? 39.817  -23.460 17.141  1.00 43.49 ? 1024 HOH B O   1 
HETATM 4946 O O   . HOH K 7 .   ? 27.214  -15.221 35.147  1.00 46.52 ? 1025 HOH B O   1 
HETATM 4947 O O   . HOH K 7 .   ? 42.490  -17.737 22.337  1.00 35.06 ? 1026 HOH B O   1 
HETATM 4948 O O   . HOH K 7 .   ? 44.294  -12.385 19.498  1.00 37.58 ? 1027 HOH B O   1 
HETATM 4949 O O   . HOH K 7 .   ? 24.381  -26.859 15.557  1.00 30.00 ? 1028 HOH B O   1 
HETATM 4950 O O   . HOH K 7 .   ? 23.040  8.043   11.566  1.00 43.30 ? 1029 HOH B O   1 
HETATM 4951 O O   . HOH K 7 .   ? 36.134  -18.544 -3.274  1.00 16.04 ? 1030 HOH B O   1 
HETATM 4952 O O   . HOH K 7 .   ? 43.055  3.301   18.345  1.00 37.14 ? 1031 HOH B O   1 
HETATM 4953 O O   . HOH K 7 .   ? 32.240  3.242   32.995  1.00 27.58 ? 1032 HOH B O   1 
HETATM 4954 O O   . HOH K 7 .   ? 37.409  -35.211 -23.615 1.00 34.33 ? 1033 HOH B O   1 
HETATM 4955 O O   . HOH K 7 .   ? 13.144  -10.942 14.016  1.00 40.05 ? 1034 HOH B O   1 
HETATM 4956 O O   . HOH K 7 .   ? 9.950   -40.519 27.776  1.00 40.44 ? 1035 HOH B O   1 
HETATM 4957 O O   . HOH K 7 .   ? 12.316  -5.099  2.867   1.00 43.46 ? 1036 HOH B O   1 
HETATM 4958 O O   . HOH K 7 .   ? 18.559  -38.211 24.006  1.00 30.00 ? 1037 HOH B O   1 
HETATM 4959 O O   . HOH K 7 .   ? 12.829  -25.977 -18.239 1.00 30.00 ? 1038 HOH B O   1 
HETATM 4960 O O   . HOH K 7 .   ? 13.628  -6.442  21.077  1.00 30.00 ? 1039 HOH B O   1 
HETATM 4961 O O   . HOH K 7 .   ? 19.860  -28.112 -3.098  1.00 13.21 ? 1040 HOH B O   1 
HETATM 4962 O O   . HOH K 7 .   ? 11.250  -48.175 20.352  1.00 29.04 ? 1041 HOH B O   1 
HETATM 4963 O O   . HOH K 7 .   ? 23.178  3.667   2.599   1.00 39.26 ? 1043 HOH B O   1 
HETATM 4964 O O   . HOH K 7 .   ? 14.437  -7.802  11.437  1.00 48.19 ? 1044 HOH B O   1 
HETATM 4965 O O   . HOH K 7 .   ? 49.810  -16.859 8.382   1.00 48.25 ? 1045 HOH B O   1 
HETATM 4966 O O   . HOH K 7 .   ? -5.172  -6.813  11.285  1.00 45.73 ? 1046 HOH B O   1 
HETATM 4967 O O   . HOH K 7 .   ? 33.551  -0.412  28.571  1.00 30.91 ? 1047 HOH B O   1 
HETATM 4968 O O   . HOH K 7 .   ? 16.985  -27.711 17.555  1.00 31.02 ? 1048 HOH B O   1 
HETATM 4969 O O   . HOH K 7 .   ? 39.960  -19.641 7.675   1.00 20.26 ? 1049 HOH B O   1 
HETATM 4970 O O   . HOH K 7 .   ? 13.410  -15.186 14.698  1.00 38.24 ? 1050 HOH B O   1 
HETATM 4971 O O   . HOH K 7 .   ? 19.851  -5.716  0.489   1.00 32.89 ? 1051 HOH B O   1 
HETATM 4972 O O   . HOH K 7 .   ? -2.458  -45.898 9.368   1.00 55.63 ? 1052 HOH B O   1 
HETATM 4973 O O   . HOH K 7 .   ? 25.942  -41.172 29.647  1.00 39.43 ? 1053 HOH B O   1 
HETATM 4974 O O   . HOH K 7 .   ? -4.253  -39.120 -19.961 1.00 55.81 ? 1054 HOH B O   1 
HETATM 4975 O O   . HOH K 7 .   ? 7.370   -33.155 -21.792 1.00 28.36 ? 1055 HOH B O   1 
HETATM 4976 O O   . HOH K 7 .   ? 10.201  0.939   -18.007 1.00 52.33 ? 1056 HOH B O   1 
HETATM 4977 O O   . HOH K 7 .   ? 13.577  1.411   12.496  1.00 40.74 ? 1057 HOH B O   1 
HETATM 4978 O O   . HOH K 7 .   ? 41.136  -19.027 5.185   1.00 24.25 ? 1058 HOH B O   1 
HETATM 4979 O O   . HOH K 7 .   ? 37.938  -7.829  -8.114  1.00 26.41 ? 1059 HOH B O   1 
HETATM 4980 O O   . HOH K 7 .   ? 40.312  -2.733  5.872   1.00 48.63 ? 1060 HOH B O   1 
HETATM 4981 O O   . HOH K 7 .   ? 42.383  -7.336  8.979   1.00 24.83 ? 1061 HOH B O   1 
HETATM 4982 O O   . HOH K 7 .   ? 17.054  -10.970 1.383   1.00 48.36 ? 1062 HOH B O   1 
HETATM 4983 O O   . HOH K 7 .   ? 20.128  -9.400  25.089  1.00 24.02 ? 1063 HOH B O   1 
HETATM 4984 O O   . HOH K 7 .   ? 37.866  -4.682  7.477   1.00 30.00 ? 1064 HOH B O   1 
HETATM 4985 O O   . HOH K 7 .   ? 26.444  -1.167  32.496  1.00 27.79 ? 1065 HOH B O   1 
HETATM 4986 O O   . HOH K 7 .   ? -1.331  -5.157  4.057   1.00 37.51 ? 1066 HOH B O   1 
HETATM 4987 O O   . HOH K 7 .   ? 7.619   -23.066 -28.816 1.00 43.89 ? 1067 HOH B O   1 
HETATM 4988 O O   . HOH K 7 .   ? 20.027  -23.950 28.977  1.00 48.19 ? 1068 HOH B O   1 
HETATM 4989 O O   . HOH K 7 .   ? -7.053  -36.185 -5.130  1.00 30.00 ? 1069 HOH B O   1 
HETATM 4990 O O   . HOH K 7 .   ? 47.732  -10.705 6.943   1.00 33.36 ? 1070 HOH B O   1 
HETATM 4991 O O   . HOH K 7 .   ? 14.318  -24.498 -16.245 1.00 19.87 ? 1071 HOH B O   1 
HETATM 4992 O O   . HOH K 7 .   ? 14.216  -46.079 23.447  1.00 35.70 ? 1072 HOH B O   1 
HETATM 4993 O O   . HOH K 7 .   ? 31.485  3.216   26.478  1.00 39.86 ? 1073 HOH B O   1 
HETATM 4994 O O   . HOH K 7 .   ? 23.581  -33.396 12.219  1.00 15.62 ? 1074 HOH B O   1 
HETATM 4995 O O   . HOH K 7 .   ? 10.446  -24.419 -27.851 1.00 34.21 ? 1075 HOH B O   1 
HETATM 4996 O O   . HOH K 7 .   ? 37.580  -3.057  -8.441  1.00 49.82 ? 1076 HOH B O   1 
HETATM 4997 O O   . HOH K 7 .   ? 33.938  2.216   29.654  1.00 51.40 ? 1077 HOH B O   1 
HETATM 4998 O O   . HOH K 7 .   ? 15.769  -15.370 32.391  1.00 46.96 ? 1078 HOH B O   1 
HETATM 4999 O O   . HOH K 7 .   ? 13.363  -4.531  -17.526 1.00 52.66 ? 1079 HOH B O   1 
HETATM 5000 O O   . HOH K 7 .   ? 35.544  11.132  19.144  1.00 35.72 ? 1080 HOH B O   1 
HETATM 5001 O O   . HOH K 7 .   ? 35.645  10.945  11.462  1.00 35.30 ? 1081 HOH B O   1 
HETATM 5002 O O   . HOH K 7 .   ? 19.941  -4.106  -16.078 1.00 47.35 ? 1082 HOH B O   1 
HETATM 5003 O O   . HOH K 7 .   ? 30.131  -21.009 -9.644  1.00 30.00 ? 1083 HOH B O   1 
HETATM 5004 O O   . HOH K 7 .   ? 9.295   -0.195  1.434   1.00 40.67 ? 1084 HOH B O   1 
HETATM 5005 O O   . HOH K 7 .   ? 30.186  -20.105 14.701  1.00 34.81 ? 1085 HOH B O   1 
HETATM 5006 O O   . HOH K 7 .   ? 7.798   -46.593 18.521  1.00 34.50 ? 1086 HOH B O   1 
HETATM 5007 O O   . HOH K 7 .   ? 17.608  5.973   2.128   1.00 48.91 ? 1087 HOH B O   1 
HETATM 5008 O O   . HOH K 7 .   ? 37.568  -53.561 21.103  1.00 31.29 ? 1088 HOH B O   1 
HETATM 5009 O O   . HOH K 7 .   ? 47.338  -17.767 7.543   1.00 28.00 ? 1089 HOH B O   1 
HETATM 5010 O O   . HOH K 7 .   ? 0.532   -13.827 -5.616  1.00 30.00 ? 1090 HOH B O   1 
HETATM 5011 O O   . HOH K 7 .   ? 29.886  -48.565 -26.051 1.00 35.45 ? 1091 HOH B O   1 
HETATM 5012 O O   . HOH K 7 .   ? -4.970  -21.518 -13.393 1.00 50.67 ? 1092 HOH B O   1 
HETATM 5013 O O   . HOH K 7 .   ? 39.822  -3.103  30.921  1.00 46.14 ? 1093 HOH B O   1 
HETATM 5014 O O   . HOH K 7 .   ? 32.292  -25.876 19.598  1.00 26.57 ? 1094 HOH B O   1 
HETATM 5015 O O   . HOH K 7 .   ? 33.353  -52.971 16.892  1.00 22.37 ? 1095 HOH B O   1 
HETATM 5016 O O   . HOH K 7 .   ? 35.105  -22.825 -8.524  1.00 46.96 ? 1096 HOH B O   1 
HETATM 5017 O O   . HOH K 7 .   ? 44.440  -10.866 12.924  1.00 39.02 ? 1097 HOH B O   1 
HETATM 5018 O O   . HOH K 7 .   ? 46.305  -13.526 -0.904  1.00 30.00 ? 1098 HOH B O   1 
HETATM 5019 O O   . HOH K 7 .   ? 21.729  -20.163 -4.599  1.00 15.57 ? 1099 HOH B O   1 
HETATM 5020 O O   . HOH K 7 .   ? 44.666  -7.324  15.692  1.00 42.88 ? 1100 HOH B O   1 
HETATM 5021 O O   . HOH K 7 .   ? 13.283  -0.741  13.479  1.00 44.62 ? 1101 HOH B O   1 
HETATM 5022 O O   . HOH K 7 .   ? 13.752  -13.858 17.088  1.00 43.84 ? 1102 HOH B O   1 
HETATM 5023 O O   . HOH K 7 .   ? 42.248  -26.262 -5.299  1.00 42.61 ? 1103 HOH B O   1 
HETATM 5024 O O   . HOH K 7 .   ? 17.042  -24.692 16.708  1.00 27.00 ? 1104 HOH B O   1 
HETATM 5025 O O   . HOH K 7 .   ? 2.251   -17.549 13.895  1.00 38.13 ? 1105 HOH B O   1 
HETATM 5026 O O   . HOH K 7 .   ? 4.171   -5.569  -9.139  1.00 32.04 ? 1106 HOH B O   1 
HETATM 5027 O O   . HOH K 7 .   ? 11.709  1.567   3.865   1.00 36.04 ? 1107 HOH B O   1 
HETATM 5028 O O   . HOH K 7 .   ? 41.689  -23.369 4.891   1.00 25.47 ? 1108 HOH B O   1 
HETATM 5029 O O   . HOH K 7 .   ? 32.976  -24.462 -7.433  1.00 28.00 ? 1109 HOH B O   1 
HETATM 5030 O O   . HOH K 7 .   ? 36.424  -19.238 -10.509 1.00 22.11 ? 1110 HOH B O   1 
HETATM 5031 O O   . HOH K 7 .   ? 18.597  -8.767  4.645   1.00 45.63 ? 1111 HOH B O   1 
HETATM 5032 O O   . HOH K 7 .   ? 29.920  -41.319 -14.454 1.00 31.72 ? 1112 HOH B O   1 
HETATM 5033 O O   . HOH K 7 .   ? 14.438  -14.388 -18.637 1.00 32.98 ? 1113 HOH B O   1 
HETATM 5034 O O   . HOH K 7 .   ? 9.670   -10.005 -8.957  1.00 36.32 ? 1114 HOH B O   1 
HETATM 5035 O O   . HOH K 7 .   ? 23.502  -25.764 29.052  1.00 46.41 ? 1115 HOH B O   1 
HETATM 5036 O O   . HOH K 7 .   ? 11.853  3.487   6.518   1.00 51.41 ? 1116 HOH B O   1 
HETATM 5037 O O   . HOH K 7 .   ? 1.752   -17.579 0.231   1.00 30.85 ? 1117 HOH B O   1 
HETATM 5038 O O   . HOH K 7 .   ? 42.344  -25.931 -2.379  1.00 27.52 ? 1118 HOH B O   1 
HETATM 5039 O O   . HOH K 7 .   ? 44.244  -16.966 20.164  1.00 30.31 ? 1119 HOH B O   1 
HETATM 5040 O O   . HOH K 7 .   ? 23.982  -45.736 -18.554 1.00 22.36 ? 1120 HOH B O   1 
HETATM 5041 O O   . HOH K 7 .   ? 44.153  -3.755  3.177   1.00 49.58 ? 1121 HOH B O   1 
HETATM 5042 O O   . HOH K 7 .   ? -4.109  -25.567 -8.660  1.00 31.27 ? 1122 HOH B O   1 
HETATM 5043 O O   . HOH K 7 .   ? 36.345  6.077   19.442  1.00 32.08 ? 1123 HOH B O   1 
HETATM 5044 O O   . HOH K 7 .   ? 46.203  -18.750 11.813  1.00 27.63 ? 1124 HOH B O   1 
HETATM 5045 O O   . HOH K 7 .   ? 15.453  3.860   21.362  1.00 32.03 ? 1125 HOH B O   1 
HETATM 5046 O O   . HOH K 7 .   ? -1.659  -43.119 4.850   1.00 42.85 ? 1126 HOH B O   1 
HETATM 5047 O O   . HOH K 7 .   ? 25.932  -20.153 35.259  1.00 49.50 ? 1127 HOH B O   1 
HETATM 5048 O O   . HOH K 7 .   ? 27.047  -3.522  -9.950  1.00 36.09 ? 1128 HOH B O   1 
HETATM 5049 O O   . HOH K 7 .   ? 35.726  -35.942 -25.547 1.00 29.73 ? 1129 HOH B O   1 
HETATM 5050 O O   . HOH K 7 .   ? 24.043  3.494   20.702  1.00 43.28 ? 1130 HOH B O   1 
HETATM 5051 O O   . HOH K 7 .   ? 18.481  5.310   21.736  1.00 27.65 ? 1131 HOH B O   1 
HETATM 5052 O O   . HOH K 7 .   ? 1.072   -11.932 -10.588 1.00 30.00 ? 1132 HOH B O   1 
HETATM 5053 O O   . HOH K 7 .   ? -1.262  -20.411 -13.024 1.00 47.96 ? 1133 HOH B O   1 
HETATM 5054 O O   . HOH K 7 .   ? -11.674 -32.672 -16.236 1.00 45.19 ? 1134 HOH B O   1 
HETATM 5055 O O   . HOH K 7 .   ? 38.744  -3.358  9.524   1.00 30.00 ? 1135 HOH B O   1 
HETATM 5056 O O   . HOH K 7 .   ? 24.404  1.352   22.503  1.00 30.00 ? 1136 HOH B O   1 
HETATM 5057 O O   . HOH K 7 .   ? 27.706  3.636   27.033  1.00 39.83 ? 1137 HOH B O   1 
HETATM 5058 O O   . HOH K 7 .   ? 42.833  -2.961  10.905  1.00 46.08 ? 1138 HOH B O   1 
HETATM 5059 O O   . HOH K 7 .   ? 11.745  -22.899 -24.936 1.00 24.73 ? 1139 HOH B O   1 
HETATM 5060 O O   . HOH K 7 .   ? 24.328  -1.996  33.428  1.00 51.04 ? 1140 HOH B O   1 
HETATM 5061 O O   . HOH K 7 .   ? 40.111  -13.717 25.922  1.00 45.99 ? 1141 HOH B O   1 
HETATM 5062 O O   . HOH K 7 .   ? 6.812   -2.429  -15.193 1.00 47.33 ? 1142 HOH B O   1 
HETATM 5063 O O   . HOH K 7 .   ? 39.123  -26.815 -17.173 1.00 57.10 ? 1143 HOH B O   1 
HETATM 5064 O O   . HOH K 7 .   ? 34.184  4.512   9.141   1.00 21.75 ? 1144 HOH B O   1 
HETATM 5065 O O   . HOH K 7 .   ? 34.109  -40.092 -19.693 1.00 25.18 ? 1145 HOH B O   1 
HETATM 5066 O O   . HOH K 7 .   ? -0.032  -17.465 -20.459 1.00 44.29 ? 1146 HOH B O   1 
HETATM 5067 O O   . HOH K 7 .   ? -5.043  -34.559 0.589   1.00 33.80 ? 1147 HOH B O   1 
HETATM 5068 O O   . HOH K 7 .   ? 32.530  -19.496 -12.746 1.00 33.29 ? 1148 HOH B O   1 
HETATM 5069 O O   . HOH K 7 .   ? 25.259  -6.590  2.536   1.00 32.65 ? 1149 HOH B O   1 
HETATM 5070 O O   . HOH K 7 .   ? 12.920  -2.505  3.049   1.00 43.99 ? 1150 HOH B O   1 
HETATM 5071 O O   . HOH K 7 .   ? 24.736  3.062   -6.143  1.00 44.43 ? 1151 HOH B O   1 
HETATM 5072 O O   . HOH K 7 .   ? -0.385  -43.182 -6.659  1.00 50.54 ? 1152 HOH B O   1 
HETATM 5073 O O   . HOH K 7 .   ? 0.171   -17.401 -24.681 1.00 51.05 ? 1153 HOH B O   1 
HETATM 5074 O O   . HOH K 7 .   ? 11.119  -7.361  17.494  1.00 51.11 ? 1154 HOH B O   1 
HETATM 5075 O O   . HOH K 7 .   ? 22.777  2.385   -7.352  1.00 43.05 ? 1155 HOH B O   1 
HETATM 5076 O O   . HOH K 7 .   ? -3.701  -37.174 9.924   1.00 53.07 ? 1156 HOH B O   1 
HETATM 5077 O O   . HOH K 7 .   ? 33.531  -17.053 -13.908 1.00 34.03 ? 1157 HOH B O   1 
HETATM 5078 O O   . HOH K 7 .   ? 39.401  -1.645  24.716  1.00 41.13 ? 1158 HOH B O   1 
HETATM 5079 O O   . HOH K 7 .   ? 37.305  -40.606 -16.643 1.00 37.20 ? 1159 HOH B O   1 
HETATM 5080 O O   . HOH K 7 .   ? 7.225   -39.580 28.546  1.00 53.73 ? 1160 HOH B O   1 
HETATM 5081 O O   . HOH K 7 .   ? 44.430  -24.704 -1.897  1.00 48.35 ? 1161 HOH B O   1 
HETATM 5082 O O   . HOH K 7 .   ? 21.373  -40.918 -6.337  1.00 28.61 ? 1162 HOH B O   1 
HETATM 5083 O O   . HOH K 7 .   ? 24.259  -25.076 31.214  1.00 42.78 ? 1163 HOH B O   1 
HETATM 5084 O O   . HOH K 7 .   ? 26.560  -37.377 -1.741  1.00 31.65 ? 1164 HOH B O   1 
HETATM 5085 O O   . HOH K 7 .   ? 26.831  8.190   11.815  1.00 44.87 ? 1165 HOH B O   1 
HETATM 5086 O O   . HOH K 7 .   ? -4.245  -25.541 -14.331 1.00 30.00 ? 1166 HOH B O   1 
HETATM 5087 O O   . HOH K 7 .   ? 17.465  -46.092 -31.877 1.00 54.64 ? 1167 HOH B O   1 
HETATM 5088 O O   . HOH K 7 .   ? 30.509  -25.294 -12.442 1.00 46.66 ? 1168 HOH B O   1 
HETATM 5089 O O   . HOH K 7 .   ? -1.572  -21.567 -8.483  1.00 38.47 ? 1169 HOH B O   1 
HETATM 5090 O O   . HOH K 7 .   ? 16.576  -48.529 25.593  1.00 47.41 ? 1170 HOH B O   1 
HETATM 5091 O O   . HOH K 7 .   ? 48.116  -20.883 -0.462  1.00 51.33 ? 1171 HOH B O   1 
HETATM 5092 O O   . HOH K 7 .   ? 3.565   -45.878 -1.601  1.00 44.42 ? 1172 HOH B O   1 
HETATM 5093 O O   . HOH K 7 .   ? -3.697  -21.370 -10.787 1.00 54.24 ? 1173 HOH B O   1 
HETATM 5094 O O   . HOH K 7 .   ? 10.621  -14.641 -18.842 1.00 40.59 ? 1174 HOH B O   1 
HETATM 5095 O O   . HOH K 7 .   ? -5.364  -25.307 -5.810  1.00 29.31 ? 1175 HOH B O   1 
HETATM 5096 O O   . HOH K 7 .   ? 35.716  -23.546 -12.518 1.00 43.73 ? 1176 HOH B O   1 
HETATM 5097 O O   . HOH K 7 .   ? -4.777  -25.031 8.319   1.00 39.88 ? 1177 HOH B O   1 
HETATM 5098 O O   . HOH K 7 .   ? 4.301   -40.148 -11.432 1.00 39.91 ? 1178 HOH B O   1 
HETATM 5099 O O   . HOH K 7 .   ? 1.480   -18.808 -22.812 1.00 41.55 ? 1179 HOH B O   1 
HETATM 5100 O O   . HOH K 7 .   ? 14.457  -15.127 9.030   1.00 48.41 ? 1180 HOH B O   1 
HETATM 5101 O O   . HOH K 7 .   ? 3.544   -45.567 19.696  1.00 40.00 ? 1181 HOH B O   1 
HETATM 5102 O O   . HOH K 7 .   ? 46.473  -12.311 18.548  1.00 53.61 ? 1182 HOH B O   1 
HETATM 5103 O O   . HOH K 7 .   ? 11.038  -18.042 11.758  1.00 30.00 ? 1183 HOH B O   1 
HETATM 5104 O O   . HOH K 7 .   ? 22.379  -5.105  -16.821 1.00 49.96 ? 1184 HOH B O   1 
HETATM 5105 O O   . HOH K 7 .   ? 15.483  -44.728 0.000   0.50 30.99 ? 1185 HOH B O   1 
HETATM 5106 O O   . HOH K 7 .   ? 42.966  -5.144  7.743   1.00 58.66 ? 1186 HOH B O   1 
HETATM 5107 O O   . HOH K 7 .   ? 29.013  -5.351  -12.874 1.00 30.00 ? 1187 HOH B O   1 
HETATM 5108 O O   . HOH K 7 .   ? 15.179  5.146   -1.940  1.00 60.60 ? 1188 HOH B O   1 
HETATM 5109 O O   . HOH K 7 .   ? 26.448  4.552   24.606  1.00 47.52 ? 1189 HOH B O   1 
HETATM 5110 O O   . HOH K 7 .   ? 1.688   -43.341 -8.661  1.00 36.56 ? 1190 HOH B O   1 
HETATM 5111 O O   . HOH K 7 .   ? 6.697   -45.036 -7.055  1.00 27.62 ? 1191 HOH B O   1 
HETATM 5112 O O   . HOH K 7 .   ? 17.172  -37.310 -27.444 1.00 51.30 ? 1192 HOH B O   1 
HETATM 5113 O O   . HOH K 7 .   ? 25.582  -25.025 -24.914 1.00 47.93 ? 1193 HOH B O   1 
HETATM 5114 O O   . HOH K 7 .   ? 34.671  -21.465 -10.424 1.00 34.96 ? 1194 HOH B O   1 
HETATM 5115 O O   . HOH K 7 .   ? 24.075  -6.548  -18.634 1.00 50.53 ? 1195 HOH B O   1 
HETATM 5116 O O   . HOH K 7 .   ? 4.354   -41.860 -9.175  1.00 36.16 ? 1196 HOH B O   1 
HETATM 5117 O O   . HOH K 7 .   ? 7.821   -8.297  -9.918  1.00 53.33 ? 1197 HOH B O   1 
HETATM 5118 O O   . HOH K 7 .   ? 6.800   -45.386 -11.698 1.00 41.19 ? 1198 HOH B O   1 
HETATM 5119 O O   . HOH K 7 .   ? 0.571   -15.289 -0.242  1.00 47.46 ? 1199 HOH B O   1 
HETATM 5120 O O   . HOH K 7 .   ? -6.438  -27.015 7.849   1.00 42.67 ? 1200 HOH B O   1 
HETATM 5121 O O   . HOH K 7 .   ? 37.389  4.692   8.481   1.00 39.19 ? 1203 HOH B O   1 
HETATM 5122 O O   . HOH K 7 .   ? 19.905  -40.414 -26.565 1.00 35.86 ? 1205 HOH B O   1 
HETATM 5123 O O   . HOH K 7 .   ? 20.513  8.026   11.427  1.00 46.71 ? 1206 HOH B O   1 
HETATM 5124 O O   . HOH K 7 .   ? 40.141  2.844   11.618  1.00 44.75 ? 1207 HOH B O   1 
HETATM 5125 O O   . HOH K 7 .   ? 23.332  3.165   33.614  1.00 53.60 ? 1208 HOH B O   1 
HETATM 5126 O O   . HOH K 7 .   ? -0.922  -13.746 -9.952  1.00 30.00 ? 1209 HOH B O   1 
HETATM 5127 O O   . HOH K 7 .   ? 15.509  -46.017 25.593  1.00 39.95 ? 1210 HOH B O   1 
HETATM 5128 O O   . HOH K 7 .   ? 40.801  5.389   10.485  1.00 51.59 ? 1211 HOH B O   1 
HETATM 5129 O O   . HOH K 7 .   ? 50.640  -17.664 11.110  1.00 52.82 ? 1212 HOH B O   1 
HETATM 5130 O O   . HOH K 7 .   ? -4.486  -22.619 6.471   1.00 45.87 ? 1213 HOH B O   1 
HETATM 5131 O O   . HOH K 7 .   ? 52.878  -13.058 11.009  1.00 53.90 ? 1214 HOH B O   1 
HETATM 5132 O O   . HOH K 7 .   ? 6.828   -48.030 -3.651  1.00 30.16 ? 1215 HOH B O   1 
HETATM 5133 O O   . HOH K 7 .   ? -4.499  -23.012 -1.818  1.00 35.50 ? 1216 HOH B O   1 
HETATM 5134 O O   . HOH K 7 .   ? 44.345  -13.631 -9.220  1.00 43.56 ? 1217 HOH B O   1 
HETATM 5135 O O   . HOH K 7 .   ? 36.924  2.961   33.357  1.00 51.37 ? 1218 HOH B O   1 
HETATM 5136 O O   . HOH K 7 .   ? 21.102  -0.804  28.322  1.00 45.41 ? 1219 HOH B O   1 
HETATM 5137 O O   . HOH K 7 .   ? 33.199  -56.359 26.524  1.00 46.52 ? 1220 HOH B O   1 
# 
