data_8R1E
# 
_entry.id   8R1E 
# 
_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   8R1E         pdb_00008r1e 10.2210/pdb8r1e/pdb 
WWPDB D_1292134372 ?            ?                   
# 
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 2025-02-19 ? 
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                        8R1E 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-01 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        '8PNG is the same protein without mutation' 
_pdbx_database_related.db_id          8PNG 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              mw240@cam.ac.uk 
_pdbx_contact_author.name_first         Welch 
_pdbx_contact_author.name_last          Martin 
_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' 63699.270 2   ? 'M130G E296A Q303A' ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'     785.550   2   ? ?                   ? ? 
3 non-polymer syn GLYCEROL                          92.094    3   ? ?                   ? ? 
4 non-polymer nat 'TRIETHYLENE GLYCOL'              150.173   1   ? ?                   ? ? 
5 water       nat water                             18.015    852 ? ?                   ? ? 
# 
_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       
;GHMADYKAPLRDMRFVLNEVFEVSRLWAQLPALAEVVDAETAAAILEEAGKVTAGTIAPLNRPGDEEGCQWNAGAVSTPA
GFPEAYRTYAEGGWVGVGGDPAYGGMGMPKVISAQVEELVNSANLSFGLYPGLTAGACLALNAHASDELKDKYLPNMYAG
IWAGSMCLTEPHAGTDLGIIRTRAEPQADGSYKISGTKIFITGGEHDLTENIIHLVLAKLPDAPAGPKGISLFLVPKVLV
NADGSLGEKNSLGCGSIEHKMGIKASATCVMNFDGATGWLVGEVNKGLAAMFTMMNYARLGVGIAGLATGERSYQSAIEY
ARERIQSRAPTGPVAKDKAADPIIVHPDVRRMLLTMKALNEGGRAFSSYVAMQLDTAKYSEDAVTRKRAEELVALLTPVA
KAFLTDMGLETTIHGQQIFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALDLVGRKVIGSGGAFSRHFTDEIKAFVAS
ADEALGEFSKPLAAAVENLEELTAWLLDRAKGNPNEIGAASVEYLHVFGYTAYAYMWALMARTALAKQGEDDFYASKLGT
ARFYFARLLPRIHSLSASVRAGSESLYLLDAEQF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GHMADYKAPLRDMRFVLNEVFEVSRLWAQLPALAEVVDAETAAAILEEAGKVTAGTIAPLNRPGDEEGCQWNAGAVSTPA
GFPEAYRTYAEGGWVGVGGDPAYGGMGMPKVISAQVEELVNSANLSFGLYPGLTAGACLALNAHASDELKDKYLPNMYAG
IWAGSMCLTEPHAGTDLGIIRTRAEPQADGSYKISGTKIFITGGEHDLTENIIHLVLAKLPDAPAGPKGISLFLVPKVLV
NADGSLGEKNSLGCGSIEHKMGIKASATCVMNFDGATGWLVGEVNKGLAAMFTMMNYARLGVGIAGLATGERSYQSAIEY
ARERIQSRAPTGPVAKDKAADPIIVHPDVRRMLLTMKALNEGGRAFSSYVAMQLDTAKYSEDAVTRKRAEELVALLTPVA
KAFLTDMGLETTIHGQQIFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALDLVGRKVIGSGGAFSRHFTDEIKAFVAS
ADEALGEFSKPLAAAVENLEELTAWLLDRAKGNPNEIGAASVEYLHVFGYTAYAYMWALMARTALAKQGEDDFYASKLGT
ARFYFARLLPRIHSLSASVRAGSESLYLLDAEQF
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 GLYCEROL                      GOL 
4 'TRIETHYLENE GLYCOL'          PGE 
5 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   ALA 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  MET n 
1 14  ARG n 
1 15  PHE n 
1 16  VAL n 
1 17  LEU n 
1 18  ASN n 
1 19  GLU n 
1 20  VAL n 
1 21  PHE n 
1 22  GLU n 
1 23  VAL n 
1 24  SER n 
1 25  ARG n 
1 26  LEU n 
1 27  TRP n 
1 28  ALA n 
1 29  GLN n 
1 30  LEU n 
1 31  PRO n 
1 32  ALA n 
1 33  LEU n 
1 34  ALA n 
1 35  GLU n 
1 36  VAL n 
1 37  VAL n 
1 38  ASP n 
1 39  ALA n 
1 40  GLU n 
1 41  THR n 
1 42  ALA n 
1 43  ALA n 
1 44  ALA n 
1 45  ILE n 
1 46  LEU n 
1 47  GLU n 
1 48  GLU n 
1 49  ALA n 
1 50  GLY n 
1 51  LYS n 
1 52  VAL n 
1 53  THR n 
1 54  ALA n 
1 55  GLY n 
1 56  THR n 
1 57  ILE n 
1 58  ALA n 
1 59  PRO n 
1 60  LEU n 
1 61  ASN n 
1 62  ARG n 
1 63  PRO n 
1 64  GLY n 
1 65  ASP n 
1 66  GLU n 
1 67  GLU n 
1 68  GLY n 
1 69  CYS n 
1 70  GLN n 
1 71  TRP n 
1 72  ASN n 
1 73  ALA n 
1 74  GLY n 
1 75  ALA n 
1 76  VAL n 
1 77  SER n 
1 78  THR n 
1 79  PRO n 
1 80  ALA n 
1 81  GLY n 
1 82  PHE n 
1 83  PRO n 
1 84  GLU n 
1 85  ALA n 
1 86  TYR n 
1 87  ARG n 
1 88  THR n 
1 89  TYR n 
1 90  ALA n 
1 91  GLU n 
1 92  GLY n 
1 93  GLY n 
1 94  TRP n 
1 95  VAL n 
1 96  GLY n 
1 97  VAL n 
1 98  GLY n 
1 99  GLY n 
1 100 ASP n 
1 101 PRO n 
1 102 ALA n 
1 103 TYR n 
1 104 GLY n 
1 105 GLY n 
1 106 MET n 
1 107 GLY n 
1 108 MET n 
1 109 PRO n 
1 110 LYS n 
1 111 VAL n 
1 112 ILE n 
1 113 SER n 
1 114 ALA n 
1 115 GLN n 
1 116 VAL n 
1 117 GLU n 
1 118 GLU n 
1 119 LEU n 
1 120 VAL n 
1 121 ASN n 
1 122 SER n 
1 123 ALA n 
1 124 ASN n 
1 125 LEU n 
1 126 SER n 
1 127 PHE n 
1 128 GLY n 
1 129 LEU n 
1 130 TYR n 
1 131 PRO n 
1 132 GLY n 
1 133 LEU n 
1 134 THR n 
1 135 ALA n 
1 136 GLY n 
1 137 ALA n 
1 138 CYS n 
1 139 LEU n 
1 140 ALA n 
1 141 LEU n 
1 142 ASN n 
1 143 ALA n 
1 144 HIS n 
1 145 ALA n 
1 146 SER n 
1 147 ASP n 
1 148 GLU n 
1 149 LEU n 
1 150 LYS n 
1 151 ASP n 
1 152 LYS n 
1 153 TYR n 
1 154 LEU n 
1 155 PRO n 
1 156 ASN n 
1 157 MET n 
1 158 TYR n 
1 159 ALA n 
1 160 GLY n 
1 161 ILE n 
1 162 TRP n 
1 163 ALA n 
1 164 GLY n 
1 165 SER n 
1 166 MET n 
1 167 CYS n 
1 168 LEU n 
1 169 THR n 
1 170 GLU n 
1 171 PRO n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLY n 
1 179 ILE n 
1 180 ILE n 
1 181 ARG n 
1 182 THR n 
1 183 ARG n 
1 184 ALA n 
1 185 GLU n 
1 186 PRO n 
1 187 GLN n 
1 188 ALA n 
1 189 ASP n 
1 190 GLY n 
1 191 SER n 
1 192 TYR n 
1 193 LYS n 
1 194 ILE n 
1 195 SER n 
1 196 GLY n 
1 197 THR n 
1 198 LYS n 
1 199 ILE n 
1 200 PHE n 
1 201 ILE n 
1 202 THR n 
1 203 GLY n 
1 204 GLY n 
1 205 GLU n 
1 206 HIS n 
1 207 ASP n 
1 208 LEU n 
1 209 THR n 
1 210 GLU n 
1 211 ASN n 
1 212 ILE n 
1 213 ILE n 
1 214 HIS n 
1 215 LEU n 
1 216 VAL n 
1 217 LEU n 
1 218 ALA n 
1 219 LYS n 
1 220 LEU n 
1 221 PRO n 
1 222 ASP n 
1 223 ALA n 
1 224 PRO n 
1 225 ALA n 
1 226 GLY n 
1 227 PRO n 
1 228 LYS n 
1 229 GLY n 
1 230 ILE n 
1 231 SER n 
1 232 LEU n 
1 233 PHE n 
1 234 LEU n 
1 235 VAL n 
1 236 PRO n 
1 237 LYS n 
1 238 VAL n 
1 239 LEU n 
1 240 VAL n 
1 241 ASN n 
1 242 ALA n 
1 243 ASP n 
1 244 GLY n 
1 245 SER n 
1 246 LEU n 
1 247 GLY n 
1 248 GLU n 
1 249 LYS n 
1 250 ASN n 
1 251 SER n 
1 252 LEU n 
1 253 GLY n 
1 254 CYS n 
1 255 GLY n 
1 256 SER n 
1 257 ILE n 
1 258 GLU n 
1 259 HIS n 
1 260 LYS n 
1 261 MET n 
1 262 GLY n 
1 263 ILE n 
1 264 LYS n 
1 265 ALA n 
1 266 SER n 
1 267 ALA n 
1 268 THR n 
1 269 CYS n 
1 270 VAL n 
1 271 MET n 
1 272 ASN n 
1 273 PHE n 
1 274 ASP n 
1 275 GLY n 
1 276 ALA n 
1 277 THR n 
1 278 GLY n 
1 279 TRP n 
1 280 LEU n 
1 281 VAL n 
1 282 GLY n 
1 283 GLU n 
1 284 VAL n 
1 285 ASN n 
1 286 LYS n 
1 287 GLY n 
1 288 LEU n 
1 289 ALA n 
1 290 ALA n 
1 291 MET n 
1 292 PHE n 
1 293 THR n 
1 294 MET n 
1 295 MET n 
1 296 ASN n 
1 297 TYR n 
1 298 ALA n 
1 299 ARG n 
1 300 LEU n 
1 301 GLY n 
1 302 VAL n 
1 303 GLY n 
1 304 ILE n 
1 305 ALA n 
1 306 GLY n 
1 307 LEU n 
1 308 ALA n 
1 309 THR n 
1 310 GLY n 
1 311 GLU n 
1 312 ARG n 
1 313 SER n 
1 314 TYR n 
1 315 GLN n 
1 316 SER n 
1 317 ALA n 
1 318 ILE n 
1 319 GLU n 
1 320 TYR n 
1 321 ALA n 
1 322 ARG n 
1 323 GLU n 
1 324 ARG n 
1 325 ILE n 
1 326 GLN n 
1 327 SER n 
1 328 ARG n 
1 329 ALA n 
1 330 PRO n 
1 331 THR n 
1 332 GLY n 
1 333 PRO n 
1 334 VAL n 
1 335 ALA n 
1 336 LYS n 
1 337 ASP n 
1 338 LYS n 
1 339 ALA n 
1 340 ALA n 
1 341 ASP n 
1 342 PRO n 
1 343 ILE n 
1 344 ILE n 
1 345 VAL n 
1 346 HIS n 
1 347 PRO n 
1 348 ASP n 
1 349 VAL n 
1 350 ARG n 
1 351 ARG n 
1 352 MET n 
1 353 LEU n 
1 354 LEU n 
1 355 THR n 
1 356 MET n 
1 357 LYS n 
1 358 ALA n 
1 359 LEU n 
1 360 ASN n 
1 361 GLU n 
1 362 GLY n 
1 363 GLY n 
1 364 ARG n 
1 365 ALA n 
1 366 PHE n 
1 367 SER n 
1 368 SER n 
1 369 TYR n 
1 370 VAL n 
1 371 ALA n 
1 372 MET n 
1 373 GLN n 
1 374 LEU n 
1 375 ASP n 
1 376 THR n 
1 377 ALA n 
1 378 LYS n 
1 379 TYR n 
1 380 SER n 
1 381 GLU n 
1 382 ASP n 
1 383 ALA n 
1 384 VAL n 
1 385 THR n 
1 386 ARG n 
1 387 LYS n 
1 388 ARG n 
1 389 ALA n 
1 390 GLU n 
1 391 GLU n 
1 392 LEU n 
1 393 VAL n 
1 394 ALA n 
1 395 LEU n 
1 396 LEU n 
1 397 THR n 
1 398 PRO n 
1 399 VAL n 
1 400 ALA n 
1 401 LYS n 
1 402 ALA n 
1 403 PHE n 
1 404 LEU n 
1 405 THR n 
1 406 ASP n 
1 407 MET n 
1 408 GLY n 
1 409 LEU n 
1 410 GLU n 
1 411 THR n 
1 412 THR n 
1 413 ILE n 
1 414 HIS n 
1 415 GLY n 
1 416 GLN n 
1 417 GLN n 
1 418 ILE n 
1 419 PHE n 
1 420 GLY n 
1 421 GLY n 
1 422 HIS n 
1 423 GLY n 
1 424 PHE n 
1 425 ILE n 
1 426 ARG n 
1 427 GLU n 
1 428 TRP n 
1 429 GLY n 
1 430 GLN n 
1 431 GLU n 
1 432 GLN n 
1 433 LEU n 
1 434 VAL n 
1 435 ARG n 
1 436 ASP n 
1 437 CYS n 
1 438 ARG n 
1 439 ILE n 
1 440 THR n 
1 441 GLN n 
1 442 ILE n 
1 443 TYR n 
1 444 GLU n 
1 445 GLY n 
1 446 THR n 
1 447 ASN n 
1 448 GLY n 
1 449 ILE n 
1 450 GLN n 
1 451 ALA n 
1 452 LEU n 
1 453 ASP n 
1 454 LEU n 
1 455 VAL n 
1 456 GLY n 
1 457 ARG n 
1 458 LYS n 
1 459 VAL n 
1 460 ILE n 
1 461 GLY n 
1 462 SER n 
1 463 GLY n 
1 464 GLY n 
1 465 ALA n 
1 466 PHE n 
1 467 SER n 
1 468 ARG n 
1 469 HIS n 
1 470 PHE n 
1 471 THR n 
1 472 ASP n 
1 473 GLU n 
1 474 ILE n 
1 475 LYS n 
1 476 ALA n 
1 477 PHE n 
1 478 VAL n 
1 479 ALA n 
1 480 SER n 
1 481 ALA n 
1 482 ASP n 
1 483 GLU n 
1 484 ALA n 
1 485 LEU n 
1 486 GLY n 
1 487 GLU n 
1 488 PHE n 
1 489 SER n 
1 490 LYS n 
1 491 PRO n 
1 492 LEU n 
1 493 ALA n 
1 494 ALA n 
1 495 ALA n 
1 496 VAL n 
1 497 GLU n 
1 498 ASN n 
1 499 LEU n 
1 500 GLU n 
1 501 GLU n 
1 502 LEU n 
1 503 THR n 
1 504 ALA n 
1 505 TRP n 
1 506 LEU n 
1 507 LEU n 
1 508 ASP n 
1 509 ARG n 
1 510 ALA n 
1 511 LYS n 
1 512 GLY n 
1 513 ASN n 
1 514 PRO n 
1 515 ASN n 
1 516 GLU n 
1 517 ILE n 
1 518 GLY n 
1 519 ALA n 
1 520 ALA n 
1 521 SER n 
1 522 VAL n 
1 523 GLU n 
1 524 TYR n 
1 525 LEU n 
1 526 HIS n 
1 527 VAL n 
1 528 PHE n 
1 529 GLY n 
1 530 TYR n 
1 531 THR n 
1 532 ALA n 
1 533 TYR n 
1 534 ALA n 
1 535 TYR n 
1 536 MET n 
1 537 TRP n 
1 538 ALA n 
1 539 LEU n 
1 540 MET n 
1 541 ALA n 
1 542 ARG n 
1 543 THR n 
1 544 ALA n 
1 545 LEU n 
1 546 ALA n 
1 547 LYS n 
1 548 GLN n 
1 549 GLY n 
1 550 GLU n 
1 551 ASP n 
1 552 ASP n 
1 553 PHE n 
1 554 TYR n 
1 555 ALA n 
1 556 SER n 
1 557 LYS n 
1 558 LEU n 
1 559 GLY n 
1 560 THR n 
1 561 ALA n 
1 562 ARG n 
1 563 PHE n 
1 564 TYR n 
1 565 PHE n 
1 566 ALA n 
1 567 ARG n 
1 568 LEU n 
1 569 LEU n 
1 570 PRO n 
1 571 ARG n 
1 572 ILE n 
1 573 HIS n 
1 574 SER n 
1 575 LEU n 
1 576 SER n 
1 577 ALA n 
1 578 SER n 
1 579 VAL n 
1 580 ARG n 
1 581 ALA n 
1 582 GLY n 
1 583 SER n 
1 584 GLU n 
1 585 SER n 
1 586 LEU n 
1 587 TYR n 
1 588 LEU n 
1 589 LEU n 
1 590 ASP n 
1 591 ALA n 
1 592 GLU n 
1 593 GLN n 
1 594 PHE 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                   594 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PA0508 
_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               ? 
_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 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ?                               'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                     ?                               'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ?                               'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ?                               'C2 H5 N O2'        75.067  
GOL non-polymer         . GLYCEROL                      'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
HIS 'L-peptide linking' y HISTIDINE                     ?                               'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ?                               'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ?                               'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ?                               'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ?                               'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ?                               'C5 H11 N O2 S'     149.211 
PGE non-polymer         . 'TRIETHYLENE GLYCOL'          ?                               'C6 H14 O4'         150.173 
PHE 'L-peptide linking' y PHENYLALANINE                 ?                               'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ?                               'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ?                               'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                     ?                               'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ?                               'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ?                               'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ?                               'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -1  -1  GLY GLY B . n 
A 1 2   HIS 2   0   0   HIS HIS B . n 
A 1 3   MET 3   1   1   MET MET B . n 
A 1 4   ALA 4   2   2   ALA ALA 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  MET 13  11  11  MET MET 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  LEU 17  15  15  LEU LEU B . n 
A 1 18  ASN 18  16  16  ASN ASN B . n 
A 1 19  GLU 19  17  17  GLU GLU B . n 
A 1 20  VAL 20  18  18  VAL VAL B . n 
A 1 21  PHE 21  19  19  PHE PHE B . n 
A 1 22  GLU 22  20  20  GLU GLU B . n 
A 1 23  VAL 23  21  21  VAL VAL B . n 
A 1 24  SER 24  22  22  SER SER B . n 
A 1 25  ARG 25  23  23  ARG ARG B . n 
A 1 26  LEU 26  24  24  LEU LEU B . n 
A 1 27  TRP 27  25  25  TRP TRP B . n 
A 1 28  ALA 28  26  26  ALA ALA B . n 
A 1 29  GLN 29  27  27  GLN GLN 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  ALA 32  30  30  ALA ALA B . n 
A 1 33  LEU 33  31  31  LEU LEU B . n 
A 1 34  ALA 34  32  32  ALA ALA B . n 
A 1 35  GLU 35  33  33  GLU GLU B . n 
A 1 36  VAL 36  34  34  VAL VAL B . n 
A 1 37  VAL 37  35  35  VAL VAL B . n 
A 1 38  ASP 38  36  36  ASP ASP B . n 
A 1 39  ALA 39  37  37  ALA ALA B . n 
A 1 40  GLU 40  38  38  GLU GLU B . n 
A 1 41  THR 41  39  39  THR THR B . n 
A 1 42  ALA 42  40  40  ALA ALA B . n 
A 1 43  ALA 43  41  41  ALA ALA B . n 
A 1 44  ALA 44  42  42  ALA ALA B . n 
A 1 45  ILE 45  43  43  ILE ILE B . n 
A 1 46  LEU 46  44  44  LEU LEU B . n 
A 1 47  GLU 47  45  45  GLU GLU B . n 
A 1 48  GLU 48  46  46  GLU GLU B . n 
A 1 49  ALA 49  47  47  ALA ALA B . n 
A 1 50  GLY 50  48  48  GLY GLY B . n 
A 1 51  LYS 51  49  49  LYS LYS B . n 
A 1 52  VAL 52  50  50  VAL VAL B . n 
A 1 53  THR 53  51  51  THR THR B . n 
A 1 54  ALA 54  52  52  ALA ALA B . n 
A 1 55  GLY 55  53  53  GLY GLY B . n 
A 1 56  THR 56  54  54  THR THR B . n 
A 1 57  ILE 57  55  55  ILE ILE B . n 
A 1 58  ALA 58  56  56  ALA ALA B . n 
A 1 59  PRO 59  57  57  PRO PRO B . n 
A 1 60  LEU 60  58  58  LEU LEU B . n 
A 1 61  ASN 61  59  59  ASN ASN B . n 
A 1 62  ARG 62  60  60  ARG ARG B . n 
A 1 63  PRO 63  61  61  PRO PRO B . n 
A 1 64  GLY 64  62  62  GLY GLY B . n 
A 1 65  ASP 65  63  63  ASP ASP B . n 
A 1 66  GLU 66  64  64  GLU GLU B . n 
A 1 67  GLU 67  65  65  GLU GLU B . n 
A 1 68  GLY 68  66  66  GLY GLY B . n 
A 1 69  CYS 69  67  67  CYS CYS B . n 
A 1 70  GLN 70  68  68  GLN GLN B . n 
A 1 71  TRP 71  69  69  TRP TRP B . n 
A 1 72  ASN 72  70  70  ASN ASN B . n 
A 1 73  ALA 73  71  71  ALA ALA B . n 
A 1 74  GLY 74  72  72  GLY GLY B . n 
A 1 75  ALA 75  73  73  ALA ALA B . n 
A 1 76  VAL 76  74  74  VAL VAL B . n 
A 1 77  SER 77  75  75  SER SER B . n 
A 1 78  THR 78  76  76  THR THR B . n 
A 1 79  PRO 79  77  77  PRO PRO B . n 
A 1 80  ALA 80  78  78  ALA ALA B . n 
A 1 81  GLY 81  79  79  GLY GLY B . n 
A 1 82  PHE 82  80  80  PHE PHE B . n 
A 1 83  PRO 83  81  81  PRO PRO B . n 
A 1 84  GLU 84  82  82  GLU GLU B . n 
A 1 85  ALA 85  83  83  ALA ALA B . n 
A 1 86  TYR 86  84  84  TYR TYR B . n 
A 1 87  ARG 87  85  85  ARG ARG B . n 
A 1 88  THR 88  86  86  THR THR B . n 
A 1 89  TYR 89  87  87  TYR TYR B . n 
A 1 90  ALA 90  88  88  ALA ALA B . n 
A 1 91  GLU 91  89  89  GLU GLU B . n 
A 1 92  GLY 92  90  90  GLY GLY B . n 
A 1 93  GLY 93  91  91  GLY GLY B . n 
A 1 94  TRP 94  92  92  TRP TRP B . n 
A 1 95  VAL 95  93  93  VAL VAL B . n 
A 1 96  GLY 96  94  94  GLY GLY B . n 
A 1 97  VAL 97  95  95  VAL VAL B . n 
A 1 98  GLY 98  96  96  GLY GLY B . n 
A 1 99  GLY 99  97  97  GLY GLY B . n 
A 1 100 ASP 100 98  98  ASP ASP B . n 
A 1 101 PRO 101 99  99  PRO PRO B . n 
A 1 102 ALA 102 100 100 ALA ALA B . n 
A 1 103 TYR 103 101 101 TYR TYR B . n 
A 1 104 GLY 104 102 102 GLY GLY B . n 
A 1 105 GLY 105 103 103 GLY GLY B . n 
A 1 106 MET 106 104 104 MET MET B . n 
A 1 107 GLY 107 105 105 GLY GLY B . n 
A 1 108 MET 108 106 106 MET MET B . n 
A 1 109 PRO 109 107 107 PRO PRO B . n 
A 1 110 LYS 110 108 108 LYS LYS B . n 
A 1 111 VAL 111 109 109 VAL VAL B . n 
A 1 112 ILE 112 110 110 ILE ILE B . n 
A 1 113 SER 113 111 111 SER SER B . n 
A 1 114 ALA 114 112 112 ALA ALA B . n 
A 1 115 GLN 115 113 113 GLN GLN B . n 
A 1 116 VAL 116 114 114 VAL VAL B . n 
A 1 117 GLU 117 115 115 GLU GLU B . n 
A 1 118 GLU 118 116 116 GLU GLU B . n 
A 1 119 LEU 119 117 117 LEU LEU B . n 
A 1 120 VAL 120 118 118 VAL VAL B . n 
A 1 121 ASN 121 119 119 ASN ASN B . n 
A 1 122 SER 122 120 120 SER SER B . n 
A 1 123 ALA 123 121 121 ALA ALA B . n 
A 1 124 ASN 124 122 122 ASN ASN B . n 
A 1 125 LEU 125 123 123 LEU LEU B . n 
A 1 126 SER 126 124 124 SER SER B . n 
A 1 127 PHE 127 125 125 PHE PHE B . n 
A 1 128 GLY 128 126 126 GLY GLY B . n 
A 1 129 LEU 129 127 127 LEU LEU B . n 
A 1 130 TYR 130 128 128 TYR TYR B . n 
A 1 131 PRO 131 129 129 PRO PRO B . n 
A 1 132 GLY 132 130 130 GLY GLY B . n 
A 1 133 LEU 133 131 131 LEU LEU B . n 
A 1 134 THR 134 132 132 THR THR B . n 
A 1 135 ALA 135 133 133 ALA ALA B . n 
A 1 136 GLY 136 134 134 GLY GLY B . n 
A 1 137 ALA 137 135 135 ALA ALA B . n 
A 1 138 CYS 138 136 136 CYS CYS B . n 
A 1 139 LEU 139 137 137 LEU LEU B . n 
A 1 140 ALA 140 138 138 ALA ALA B . n 
A 1 141 LEU 141 139 139 LEU LEU B . n 
A 1 142 ASN 142 140 140 ASN ASN B . n 
A 1 143 ALA 143 141 141 ALA ALA B . n 
A 1 144 HIS 144 142 142 HIS HIS B . n 
A 1 145 ALA 145 143 143 ALA ALA B . n 
A 1 146 SER 146 144 144 SER SER B . n 
A 1 147 ASP 147 145 145 ASP ASP B . n 
A 1 148 GLU 148 146 146 GLU GLU B . n 
A 1 149 LEU 149 147 147 LEU LEU B . n 
A 1 150 LYS 150 148 148 LYS LYS B . n 
A 1 151 ASP 151 149 149 ASP ASP B . n 
A 1 152 LYS 152 150 150 LYS LYS B . n 
A 1 153 TYR 153 151 151 TYR TYR B . n 
A 1 154 LEU 154 152 152 LEU LEU B . n 
A 1 155 PRO 155 153 153 PRO PRO B . n 
A 1 156 ASN 156 154 154 ASN ASN B . n 
A 1 157 MET 157 155 155 MET MET B . n 
A 1 158 TYR 158 156 156 TYR TYR B . n 
A 1 159 ALA 159 157 157 ALA ALA B . n 
A 1 160 GLY 160 158 158 GLY GLY B . n 
A 1 161 ILE 161 159 159 ILE ILE B . n 
A 1 162 TRP 162 160 160 TRP TRP B . n 
A 1 163 ALA 163 161 161 ALA ALA B . n 
A 1 164 GLY 164 162 162 GLY GLY B . n 
A 1 165 SER 165 163 163 SER SER B . n 
A 1 166 MET 166 164 164 MET MET B . n 
A 1 167 CYS 167 165 165 CYS CYS B . n 
A 1 168 LEU 168 166 166 LEU LEU B . n 
A 1 169 THR 169 167 167 THR THR B . n 
A 1 170 GLU 170 168 168 GLU GLU B . n 
A 1 171 PRO 171 169 169 PRO PRO B . n 
A 1 172 HIS 172 170 170 HIS HIS B . n 
A 1 173 ALA 173 171 171 ALA ALA B . n 
A 1 174 GLY 174 172 172 GLY GLY B . n 
A 1 175 THR 175 173 173 THR THR B . n 
A 1 176 ASP 176 174 174 ASP ASP B . n 
A 1 177 LEU 177 175 175 LEU LEU B . n 
A 1 178 GLY 178 176 176 GLY GLY B . n 
A 1 179 ILE 179 177 177 ILE ILE B . n 
A 1 180 ILE 180 178 178 ILE ILE B . n 
A 1 181 ARG 181 179 179 ARG ARG B . n 
A 1 182 THR 182 180 180 THR THR B . n 
A 1 183 ARG 183 181 181 ARG ARG B . n 
A 1 184 ALA 184 182 182 ALA ALA B . n 
A 1 185 GLU 185 183 183 GLU GLU B . n 
A 1 186 PRO 186 184 184 PRO PRO B . n 
A 1 187 GLN 187 185 185 GLN GLN B . n 
A 1 188 ALA 188 186 186 ALA ALA B . n 
A 1 189 ASP 189 187 187 ASP ASP B . n 
A 1 190 GLY 190 188 188 GLY GLY B . n 
A 1 191 SER 191 189 189 SER SER B . n 
A 1 192 TYR 192 190 190 TYR TYR B . n 
A 1 193 LYS 193 191 191 LYS LYS B . n 
A 1 194 ILE 194 192 192 ILE ILE B . n 
A 1 195 SER 195 193 193 SER SER B . n 
A 1 196 GLY 196 194 194 GLY GLY B . n 
A 1 197 THR 197 195 195 THR THR B . n 
A 1 198 LYS 198 196 196 LYS LYS B . n 
A 1 199 ILE 199 197 197 ILE ILE B . n 
A 1 200 PHE 200 198 198 PHE PHE B . n 
A 1 201 ILE 201 199 199 ILE ILE B . n 
A 1 202 THR 202 200 200 THR THR B . n 
A 1 203 GLY 203 201 201 GLY GLY B . n 
A 1 204 GLY 204 202 202 GLY GLY B . n 
A 1 205 GLU 205 203 203 GLU GLU B . n 
A 1 206 HIS 206 204 204 HIS HIS B . n 
A 1 207 ASP 207 205 205 ASP ASP B . n 
A 1 208 LEU 208 206 206 LEU LEU B . n 
A 1 209 THR 209 207 207 THR THR B . n 
A 1 210 GLU 210 208 208 GLU GLU B . n 
A 1 211 ASN 211 209 209 ASN ASN B . n 
A 1 212 ILE 212 210 210 ILE ILE B . n 
A 1 213 ILE 213 211 211 ILE ILE B . n 
A 1 214 HIS 214 212 212 HIS HIS B . n 
A 1 215 LEU 215 213 213 LEU LEU B . n 
A 1 216 VAL 216 214 214 VAL VAL B . n 
A 1 217 LEU 217 215 215 LEU LEU B . n 
A 1 218 ALA 218 216 216 ALA ALA B . n 
A 1 219 LYS 219 217 217 LYS LYS B . n 
A 1 220 LEU 220 218 218 LEU LEU B . n 
A 1 221 PRO 221 219 219 PRO PRO B . n 
A 1 222 ASP 222 220 220 ASP ASP B . n 
A 1 223 ALA 223 221 221 ALA ALA B . n 
A 1 224 PRO 224 222 222 PRO PRO B . n 
A 1 225 ALA 225 223 223 ALA ALA B . n 
A 1 226 GLY 226 224 224 GLY GLY B . n 
A 1 227 PRO 227 225 225 PRO PRO B . n 
A 1 228 LYS 228 226 226 LYS LYS B . n 
A 1 229 GLY 229 227 227 GLY GLY B . n 
A 1 230 ILE 230 228 228 ILE ILE B . n 
A 1 231 SER 231 229 229 SER SER B . n 
A 1 232 LEU 232 230 230 LEU LEU B . n 
A 1 233 PHE 233 231 231 PHE PHE B . n 
A 1 234 LEU 234 232 232 LEU LEU B . n 
A 1 235 VAL 235 233 233 VAL VAL B . n 
A 1 236 PRO 236 234 234 PRO PRO B . n 
A 1 237 LYS 237 235 235 LYS LYS B . n 
A 1 238 VAL 238 236 236 VAL VAL B . n 
A 1 239 LEU 239 237 237 LEU LEU B . n 
A 1 240 VAL 240 238 238 VAL VAL B . n 
A 1 241 ASN 241 239 239 ASN ASN B . n 
A 1 242 ALA 242 240 240 ALA ALA B . n 
A 1 243 ASP 243 241 241 ASP ASP B . n 
A 1 244 GLY 244 242 242 GLY GLY B . n 
A 1 245 SER 245 243 243 SER SER B . n 
A 1 246 LEU 246 244 244 LEU LEU B . n 
A 1 247 GLY 247 245 245 GLY GLY B . n 
A 1 248 GLU 248 246 246 GLU GLU B . n 
A 1 249 LYS 249 247 247 LYS LYS B . n 
A 1 250 ASN 250 248 248 ASN ASN B . n 
A 1 251 SER 251 249 249 SER SER B . n 
A 1 252 LEU 252 250 250 LEU LEU B . n 
A 1 253 GLY 253 251 251 GLY GLY B . n 
A 1 254 CYS 254 252 252 CYS CYS B . n 
A 1 255 GLY 255 253 253 GLY GLY B . n 
A 1 256 SER 256 254 254 SER SER B . n 
A 1 257 ILE 257 255 255 ILE ILE B . n 
A 1 258 GLU 258 256 256 GLU GLU B . n 
A 1 259 HIS 259 257 257 HIS HIS B . n 
A 1 260 LYS 260 258 258 LYS LYS B . n 
A 1 261 MET 261 259 259 MET MET B . n 
A 1 262 GLY 262 260 260 GLY GLY B . n 
A 1 263 ILE 263 261 261 ILE ILE B . n 
A 1 264 LYS 264 262 262 LYS LYS B . n 
A 1 265 ALA 265 263 263 ALA ALA B . n 
A 1 266 SER 266 264 264 SER SER B . n 
A 1 267 ALA 267 265 265 ALA ALA B . n 
A 1 268 THR 268 266 266 THR THR B . n 
A 1 269 CYS 269 267 267 CYS CYS B . n 
A 1 270 VAL 270 268 268 VAL VAL B . n 
A 1 271 MET 271 269 269 MET MET B . n 
A 1 272 ASN 272 270 270 ASN ASN B . n 
A 1 273 PHE 273 271 271 PHE PHE B . n 
A 1 274 ASP 274 272 272 ASP ASP B . n 
A 1 275 GLY 275 273 273 GLY GLY B . n 
A 1 276 ALA 276 274 274 ALA ALA B . n 
A 1 277 THR 277 275 275 THR THR B . n 
A 1 278 GLY 278 276 276 GLY GLY B . n 
A 1 279 TRP 279 277 277 TRP TRP B . n 
A 1 280 LEU 280 278 278 LEU LEU B . n 
A 1 281 VAL 281 279 279 VAL VAL B . n 
A 1 282 GLY 282 280 280 GLY GLY B . n 
A 1 283 GLU 283 281 281 GLU GLU B . n 
A 1 284 VAL 284 282 282 VAL VAL B . n 
A 1 285 ASN 285 283 283 ASN ASN B . n 
A 1 286 LYS 286 284 284 LYS LYS B . n 
A 1 287 GLY 287 285 285 GLY GLY B . n 
A 1 288 LEU 288 286 286 LEU LEU B . n 
A 1 289 ALA 289 287 287 ALA ALA B . n 
A 1 290 ALA 290 288 288 ALA ALA B . n 
A 1 291 MET 291 289 289 MET MET B . n 
A 1 292 PHE 292 290 290 PHE PHE B . n 
A 1 293 THR 293 291 291 THR THR B . n 
A 1 294 MET 294 292 292 MET MET B . n 
A 1 295 MET 295 293 293 MET MET B . n 
A 1 296 ASN 296 294 294 ASN ASN B . n 
A 1 297 TYR 297 295 295 TYR TYR B . n 
A 1 298 ALA 298 296 296 ALA ALA B . n 
A 1 299 ARG 299 297 297 ARG ARG B . n 
A 1 300 LEU 300 298 298 LEU LEU B . n 
A 1 301 GLY 301 299 299 GLY GLY B . n 
A 1 302 VAL 302 300 300 VAL VAL B . n 
A 1 303 GLY 303 301 301 GLY GLY B . n 
A 1 304 ILE 304 302 302 ILE ILE B . n 
A 1 305 ALA 305 303 303 ALA ALA B . n 
A 1 306 GLY 306 304 304 GLY GLY B . n 
A 1 307 LEU 307 305 305 LEU LEU B . n 
A 1 308 ALA 308 306 306 ALA ALA B . n 
A 1 309 THR 309 307 307 THR THR B . n 
A 1 310 GLY 310 308 308 GLY GLY B . n 
A 1 311 GLU 311 309 309 GLU GLU B . n 
A 1 312 ARG 312 310 310 ARG ARG B . n 
A 1 313 SER 313 311 311 SER SER B . n 
A 1 314 TYR 314 312 312 TYR TYR B . n 
A 1 315 GLN 315 313 313 GLN GLN B . n 
A 1 316 SER 316 314 314 SER SER B . n 
A 1 317 ALA 317 315 315 ALA ALA B . n 
A 1 318 ILE 318 316 316 ILE ILE B . n 
A 1 319 GLU 319 317 317 GLU GLU B . n 
A 1 320 TYR 320 318 318 TYR TYR B . n 
A 1 321 ALA 321 319 319 ALA ALA B . n 
A 1 322 ARG 322 320 320 ARG ARG B . n 
A 1 323 GLU 323 321 321 GLU GLU B . n 
A 1 324 ARG 324 322 322 ARG ARG B . n 
A 1 325 ILE 325 323 323 ILE ILE B . n 
A 1 326 GLN 326 324 324 GLN GLN B . n 
A 1 327 SER 327 325 325 SER SER B . n 
A 1 328 ARG 328 326 326 ARG ARG B . n 
A 1 329 ALA 329 327 327 ALA ALA B . n 
A 1 330 PRO 330 328 328 PRO PRO B . n 
A 1 331 THR 331 329 329 THR THR B . n 
A 1 332 GLY 332 330 330 GLY GLY B . n 
A 1 333 PRO 333 331 331 PRO PRO B . n 
A 1 334 VAL 334 332 332 VAL VAL B . n 
A 1 335 ALA 335 333 333 ALA ALA B . n 
A 1 336 LYS 336 334 334 LYS LYS B . n 
A 1 337 ASP 337 335 335 ASP ASP B . n 
A 1 338 LYS 338 336 336 LYS LYS B . n 
A 1 339 ALA 339 337 337 ALA ALA B . n 
A 1 340 ALA 340 338 338 ALA ALA B . n 
A 1 341 ASP 341 339 339 ASP ASP B . n 
A 1 342 PRO 342 340 340 PRO PRO B . n 
A 1 343 ILE 343 341 341 ILE ILE B . n 
A 1 344 ILE 344 342 342 ILE ILE B . n 
A 1 345 VAL 345 343 343 VAL VAL B . n 
A 1 346 HIS 346 344 344 HIS HIS B . n 
A 1 347 PRO 347 345 345 PRO PRO B . n 
A 1 348 ASP 348 346 346 ASP ASP B . n 
A 1 349 VAL 349 347 347 VAL VAL B . n 
A 1 350 ARG 350 348 348 ARG ARG B . n 
A 1 351 ARG 351 349 349 ARG ARG B . n 
A 1 352 MET 352 350 350 MET MET B . n 
A 1 353 LEU 353 351 351 LEU LEU B . n 
A 1 354 LEU 354 352 352 LEU LEU B . n 
A 1 355 THR 355 353 353 THR THR B . n 
A 1 356 MET 356 354 354 MET MET B . n 
A 1 357 LYS 357 355 355 LYS LYS B . n 
A 1 358 ALA 358 356 356 ALA ALA B . n 
A 1 359 LEU 359 357 357 LEU LEU B . n 
A 1 360 ASN 360 358 358 ASN ASN B . n 
A 1 361 GLU 361 359 359 GLU GLU B . n 
A 1 362 GLY 362 360 360 GLY GLY B . n 
A 1 363 GLY 363 361 361 GLY GLY B . n 
A 1 364 ARG 364 362 362 ARG ARG B . n 
A 1 365 ALA 365 363 363 ALA ALA B . n 
A 1 366 PHE 366 364 364 PHE PHE B . n 
A 1 367 SER 367 365 365 SER SER B . n 
A 1 368 SER 368 366 366 SER SER B . n 
A 1 369 TYR 369 367 367 TYR TYR B . n 
A 1 370 VAL 370 368 368 VAL VAL B . n 
A 1 371 ALA 371 369 369 ALA ALA B . n 
A 1 372 MET 372 370 370 MET MET B . n 
A 1 373 GLN 373 371 371 GLN GLN B . n 
A 1 374 LEU 374 372 372 LEU LEU B . n 
A 1 375 ASP 375 373 373 ASP ASP B . n 
A 1 376 THR 376 374 374 THR THR B . n 
A 1 377 ALA 377 375 375 ALA ALA B . n 
A 1 378 LYS 378 376 376 LYS LYS B . n 
A 1 379 TYR 379 377 377 TYR TYR B . n 
A 1 380 SER 380 378 378 SER SER B . n 
A 1 381 GLU 381 379 379 GLU GLU B . n 
A 1 382 ASP 382 380 380 ASP ASP B . n 
A 1 383 ALA 383 381 381 ALA ALA B . n 
A 1 384 VAL 384 382 382 VAL VAL B . n 
A 1 385 THR 385 383 383 THR THR B . n 
A 1 386 ARG 386 384 384 ARG ARG B . n 
A 1 387 LYS 387 385 385 LYS LYS B . n 
A 1 388 ARG 388 386 386 ARG ARG B . n 
A 1 389 ALA 389 387 387 ALA ALA B . n 
A 1 390 GLU 390 388 388 GLU GLU B . n 
A 1 391 GLU 391 389 389 GLU GLU B . n 
A 1 392 LEU 392 390 390 LEU LEU B . n 
A 1 393 VAL 393 391 391 VAL VAL B . n 
A 1 394 ALA 394 392 392 ALA ALA B . n 
A 1 395 LEU 395 393 393 LEU LEU B . n 
A 1 396 LEU 396 394 394 LEU LEU B . n 
A 1 397 THR 397 395 395 THR THR B . n 
A 1 398 PRO 398 396 396 PRO PRO B . n 
A 1 399 VAL 399 397 397 VAL VAL B . n 
A 1 400 ALA 400 398 398 ALA ALA B . n 
A 1 401 LYS 401 399 399 LYS LYS B . n 
A 1 402 ALA 402 400 400 ALA ALA B . n 
A 1 403 PHE 403 401 401 PHE PHE B . n 
A 1 404 LEU 404 402 402 LEU LEU B . n 
A 1 405 THR 405 403 403 THR THR B . n 
A 1 406 ASP 406 404 404 ASP ASP B . n 
A 1 407 MET 407 405 405 MET MET B . n 
A 1 408 GLY 408 406 406 GLY GLY B . n 
A 1 409 LEU 409 407 407 LEU LEU B . n 
A 1 410 GLU 410 408 408 GLU GLU B . n 
A 1 411 THR 411 409 409 THR THR B . n 
A 1 412 THR 412 410 410 THR THR B . n 
A 1 413 ILE 413 411 411 ILE ILE B . n 
A 1 414 HIS 414 412 412 HIS HIS B . n 
A 1 415 GLY 415 413 413 GLY GLY B . n 
A 1 416 GLN 416 414 414 GLN GLN B . n 
A 1 417 GLN 417 415 415 GLN GLN B . n 
A 1 418 ILE 418 416 416 ILE ILE B . n 
A 1 419 PHE 419 417 417 PHE PHE B . n 
A 1 420 GLY 420 418 418 GLY GLY B . n 
A 1 421 GLY 421 419 419 GLY GLY B . n 
A 1 422 HIS 422 420 420 HIS HIS B . n 
A 1 423 GLY 423 421 421 GLY GLY B . n 
A 1 424 PHE 424 422 422 PHE PHE B . n 
A 1 425 ILE 425 423 423 ILE ILE B . n 
A 1 426 ARG 426 424 424 ARG ARG B . n 
A 1 427 GLU 427 425 425 GLU GLU B . n 
A 1 428 TRP 428 426 426 TRP TRP B . n 
A 1 429 GLY 429 427 427 GLY GLY B . n 
A 1 430 GLN 430 428 428 GLN GLN B . n 
A 1 431 GLU 431 429 429 GLU GLU B . n 
A 1 432 GLN 432 430 430 GLN GLN B . n 
A 1 433 LEU 433 431 431 LEU LEU B . n 
A 1 434 VAL 434 432 432 VAL VAL B . n 
A 1 435 ARG 435 433 433 ARG ARG B . n 
A 1 436 ASP 436 434 434 ASP ASP B . n 
A 1 437 CYS 437 435 435 CYS CYS B . n 
A 1 438 ARG 438 436 436 ARG ARG B . n 
A 1 439 ILE 439 437 437 ILE ILE B . n 
A 1 440 THR 440 438 438 THR THR B . n 
A 1 441 GLN 441 439 439 GLN GLN B . n 
A 1 442 ILE 442 440 440 ILE ILE B . n 
A 1 443 TYR 443 441 441 TYR TYR B . n 
A 1 444 GLU 444 442 442 GLU GLU B . n 
A 1 445 GLY 445 443 443 GLY GLY B . n 
A 1 446 THR 446 444 444 THR THR B . n 
A 1 447 ASN 447 445 445 ASN ASN B . n 
A 1 448 GLY 448 446 446 GLY GLY B . n 
A 1 449 ILE 449 447 447 ILE ILE B . n 
A 1 450 GLN 450 448 448 GLN GLN B . n 
A 1 451 ALA 451 449 449 ALA ALA B . n 
A 1 452 LEU 452 450 450 LEU LEU B . n 
A 1 453 ASP 453 451 451 ASP ASP B . n 
A 1 454 LEU 454 452 452 LEU LEU B . n 
A 1 455 VAL 455 453 453 VAL VAL B . n 
A 1 456 GLY 456 454 454 GLY GLY B . n 
A 1 457 ARG 457 455 455 ARG ARG B . n 
A 1 458 LYS 458 456 456 LYS LYS B . n 
A 1 459 VAL 459 457 457 VAL VAL B . n 
A 1 460 ILE 460 458 458 ILE ILE B . n 
A 1 461 GLY 461 459 459 GLY GLY B . n 
A 1 462 SER 462 460 460 SER SER B . n 
A 1 463 GLY 463 461 461 GLY GLY B . n 
A 1 464 GLY 464 462 462 GLY GLY B . n 
A 1 465 ALA 465 463 463 ALA ALA B . n 
A 1 466 PHE 466 464 464 PHE PHE B . n 
A 1 467 SER 467 465 465 SER SER B . n 
A 1 468 ARG 468 466 466 ARG ARG B . n 
A 1 469 HIS 469 467 467 HIS HIS B . n 
A 1 470 PHE 470 468 468 PHE PHE B . n 
A 1 471 THR 471 469 469 THR THR B . n 
A 1 472 ASP 472 470 470 ASP ASP B . n 
A 1 473 GLU 473 471 471 GLU GLU B . n 
A 1 474 ILE 474 472 472 ILE ILE B . n 
A 1 475 LYS 475 473 473 LYS LYS B . n 
A 1 476 ALA 476 474 474 ALA ALA B . n 
A 1 477 PHE 477 475 475 PHE PHE B . n 
A 1 478 VAL 478 476 476 VAL VAL B . n 
A 1 479 ALA 479 477 477 ALA ALA B . n 
A 1 480 SER 480 478 478 SER SER B . n 
A 1 481 ALA 481 479 479 ALA ALA B . n 
A 1 482 ASP 482 480 480 ASP ASP B . n 
A 1 483 GLU 483 481 481 GLU GLU B . n 
A 1 484 ALA 484 482 482 ALA ALA B . n 
A 1 485 LEU 485 483 483 LEU LEU B . n 
A 1 486 GLY 486 484 484 GLY GLY B . n 
A 1 487 GLU 487 485 485 GLU GLU B . n 
A 1 488 PHE 488 486 486 PHE PHE B . n 
A 1 489 SER 489 487 487 SER SER B . n 
A 1 490 LYS 490 488 488 LYS LYS B . n 
A 1 491 PRO 491 489 489 PRO PRO B . n 
A 1 492 LEU 492 490 490 LEU LEU B . n 
A 1 493 ALA 493 491 491 ALA ALA B . n 
A 1 494 ALA 494 492 492 ALA ALA B . n 
A 1 495 ALA 495 493 493 ALA ALA B . n 
A 1 496 VAL 496 494 494 VAL VAL B . n 
A 1 497 GLU 497 495 495 GLU GLU B . n 
A 1 498 ASN 498 496 496 ASN ASN B . n 
A 1 499 LEU 499 497 497 LEU LEU B . n 
A 1 500 GLU 500 498 498 GLU GLU B . n 
A 1 501 GLU 501 499 499 GLU GLU B . n 
A 1 502 LEU 502 500 500 LEU LEU B . n 
A 1 503 THR 503 501 501 THR THR B . n 
A 1 504 ALA 504 502 502 ALA ALA B . n 
A 1 505 TRP 505 503 503 TRP TRP B . n 
A 1 506 LEU 506 504 504 LEU LEU B . n 
A 1 507 LEU 507 505 505 LEU LEU B . n 
A 1 508 ASP 508 506 506 ASP ASP B . n 
A 1 509 ARG 509 507 507 ARG ARG B . n 
A 1 510 ALA 510 508 508 ALA ALA B . n 
A 1 511 LYS 511 509 509 LYS LYS B . n 
A 1 512 GLY 512 510 510 GLY GLY B . n 
A 1 513 ASN 513 511 511 ASN ASN B . n 
A 1 514 PRO 514 512 512 PRO PRO B . n 
A 1 515 ASN 515 513 513 ASN ASN B . n 
A 1 516 GLU 516 514 514 GLU GLU B . n 
A 1 517 ILE 517 515 515 ILE ILE B . n 
A 1 518 GLY 518 516 516 GLY GLY B . n 
A 1 519 ALA 519 517 517 ALA ALA B . n 
A 1 520 ALA 520 518 518 ALA ALA B . n 
A 1 521 SER 521 519 519 SER SER B . n 
A 1 522 VAL 522 520 520 VAL VAL B . n 
A 1 523 GLU 523 521 521 GLU GLU B . n 
A 1 524 TYR 524 522 522 TYR TYR B . n 
A 1 525 LEU 525 523 523 LEU LEU B . n 
A 1 526 HIS 526 524 524 HIS HIS B . n 
A 1 527 VAL 527 525 525 VAL VAL B . n 
A 1 528 PHE 528 526 526 PHE PHE B . n 
A 1 529 GLY 529 527 527 GLY GLY B . n 
A 1 530 TYR 530 528 528 TYR TYR B . n 
A 1 531 THR 531 529 529 THR THR B . n 
A 1 532 ALA 532 530 530 ALA ALA B . n 
A 1 533 TYR 533 531 531 TYR TYR B . n 
A 1 534 ALA 534 532 532 ALA ALA B . n 
A 1 535 TYR 535 533 533 TYR TYR B . n 
A 1 536 MET 536 534 534 MET MET B . n 
A 1 537 TRP 537 535 535 TRP TRP B . n 
A 1 538 ALA 538 536 536 ALA ALA B . n 
A 1 539 LEU 539 537 537 LEU LEU B . n 
A 1 540 MET 540 538 538 MET MET B . n 
A 1 541 ALA 541 539 539 ALA ALA B . n 
A 1 542 ARG 542 540 540 ARG ARG B . n 
A 1 543 THR 543 541 541 THR THR B . n 
A 1 544 ALA 544 542 542 ALA ALA B . n 
A 1 545 LEU 545 543 543 LEU LEU B . n 
A 1 546 ALA 546 544 544 ALA ALA B . n 
A 1 547 LYS 547 545 545 LYS LYS B . n 
A 1 548 GLN 548 546 546 GLN GLN B . n 
A 1 549 GLY 549 547 547 GLY GLY B . n 
A 1 550 GLU 550 548 548 GLU GLU B . n 
A 1 551 ASP 551 549 549 ASP ASP B . n 
A 1 552 ASP 552 550 550 ASP ASP B . n 
A 1 553 PHE 553 551 551 PHE PHE B . n 
A 1 554 TYR 554 552 552 TYR TYR B . n 
A 1 555 ALA 555 553 553 ALA ALA B . n 
A 1 556 SER 556 554 554 SER SER B . n 
A 1 557 LYS 557 555 555 LYS LYS B . n 
A 1 558 LEU 558 556 556 LEU LEU B . n 
A 1 559 GLY 559 557 557 GLY GLY B . n 
A 1 560 THR 560 558 558 THR THR B . n 
A 1 561 ALA 561 559 559 ALA ALA B . n 
A 1 562 ARG 562 560 560 ARG ARG B . n 
A 1 563 PHE 563 561 561 PHE PHE B . n 
A 1 564 TYR 564 562 562 TYR TYR B . n 
A 1 565 PHE 565 563 563 PHE PHE 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 LEU 568 566 566 LEU LEU B . n 
A 1 569 LEU 569 567 567 LEU LEU B . n 
A 1 570 PRO 570 568 568 PRO PRO B . n 
A 1 571 ARG 571 569 569 ARG ARG B . n 
A 1 572 ILE 572 570 570 ILE ILE B . n 
A 1 573 HIS 573 571 571 HIS HIS B . n 
A 1 574 SER 574 572 572 SER SER B . n 
A 1 575 LEU 575 573 573 LEU LEU B . n 
A 1 576 SER 576 574 574 SER SER B . n 
A 1 577 ALA 577 575 575 ALA ALA B . n 
A 1 578 SER 578 576 576 SER SER B . n 
A 1 579 VAL 579 577 577 VAL VAL B . n 
A 1 580 ARG 580 578 578 ARG ARG B . n 
A 1 581 ALA 581 579 579 ALA ALA B . n 
A 1 582 GLY 582 580 580 GLY GLY B . n 
A 1 583 SER 583 581 581 SER SER B . n 
A 1 584 GLU 584 582 582 GLU GLU B . n 
A 1 585 SER 585 583 583 SER SER B . n 
A 1 586 LEU 586 584 584 LEU LEU B . n 
A 1 587 TYR 587 585 585 TYR TYR B . n 
A 1 588 LEU 588 586 586 LEU LEU B . n 
A 1 589 LEU 589 587 587 LEU LEU B . n 
A 1 590 ASP 590 588 588 ASP ASP B . n 
A 1 591 ALA 591 589 589 ALA ALA B . n 
A 1 592 GLU 592 590 590 GLU GLU B . n 
A 1 593 GLN 593 591 591 GLN GLN B . n 
A 1 594 PHE 594 592 592 PHE PHE B . n 
B 1 1   GLY 1   -1  ?   ?   ?   A . n 
B 1 2   HIS 2   0   ?   ?   ?   A . n 
B 1 3   MET 3   1   ?   ?   ?   A . n 
B 1 4   ALA 4   2   2   ALA ALA A . n 
B 1 5   ASP 5   3   3   ASP ASP A . n 
B 1 6   TYR 6   4   4   TYR TYR A . n 
B 1 7   LYS 7   5   5   LYS LYS A . n 
B 1 8   ALA 8   6   6   ALA ALA A . n 
B 1 9   PRO 9   7   7   PRO PRO A . n 
B 1 10  LEU 10  8   8   LEU LEU A . n 
B 1 11  ARG 11  9   9   ARG ARG A . n 
B 1 12  ASP 12  10  10  ASP ASP A . n 
B 1 13  MET 13  11  11  MET MET A . n 
B 1 14  ARG 14  12  12  ARG ARG A . n 
B 1 15  PHE 15  13  13  PHE PHE A . n 
B 1 16  VAL 16  14  14  VAL VAL A . n 
B 1 17  LEU 17  15  15  LEU LEU A . n 
B 1 18  ASN 18  16  16  ASN ASN A . n 
B 1 19  GLU 19  17  17  GLU GLU A . n 
B 1 20  VAL 20  18  18  VAL VAL A . n 
B 1 21  PHE 21  19  19  PHE PHE A . n 
B 1 22  GLU 22  20  20  GLU GLU A . n 
B 1 23  VAL 23  21  21  VAL VAL A . n 
B 1 24  SER 24  22  22  SER SER A . n 
B 1 25  ARG 25  23  23  ARG ARG A . n 
B 1 26  LEU 26  24  24  LEU LEU A . n 
B 1 27  TRP 27  25  25  TRP TRP A . n 
B 1 28  ALA 28  26  26  ALA ALA A . n 
B 1 29  GLN 29  27  27  GLN GLN A . n 
B 1 30  LEU 30  28  28  LEU LEU A . n 
B 1 31  PRO 31  29  29  PRO PRO A . n 
B 1 32  ALA 32  30  30  ALA ALA A . n 
B 1 33  LEU 33  31  31  LEU LEU A . n 
B 1 34  ALA 34  32  32  ALA ALA A . n 
B 1 35  GLU 35  33  33  GLU GLU A . n 
B 1 36  VAL 36  34  34  VAL VAL A . n 
B 1 37  VAL 37  35  35  VAL VAL A . n 
B 1 38  ASP 38  36  36  ASP ASP A . n 
B 1 39  ALA 39  37  37  ALA ALA A . n 
B 1 40  GLU 40  38  38  GLU GLU A . n 
B 1 41  THR 41  39  39  THR THR A . n 
B 1 42  ALA 42  40  40  ALA ALA A . n 
B 1 43  ALA 43  41  41  ALA ALA A . n 
B 1 44  ALA 44  42  42  ALA ALA A . n 
B 1 45  ILE 45  43  43  ILE ILE A . n 
B 1 46  LEU 46  44  44  LEU LEU A . n 
B 1 47  GLU 47  45  45  GLU GLU A . n 
B 1 48  GLU 48  46  46  GLU GLU A . n 
B 1 49  ALA 49  47  47  ALA ALA A . n 
B 1 50  GLY 50  48  48  GLY GLY A . n 
B 1 51  LYS 51  49  49  LYS LYS A . n 
B 1 52  VAL 52  50  50  VAL VAL A . n 
B 1 53  THR 53  51  51  THR THR A . n 
B 1 54  ALA 54  52  52  ALA ALA A . n 
B 1 55  GLY 55  53  53  GLY GLY A . n 
B 1 56  THR 56  54  54  THR THR A . n 
B 1 57  ILE 57  55  55  ILE ILE A . n 
B 1 58  ALA 58  56  56  ALA ALA A . n 
B 1 59  PRO 59  57  57  PRO PRO A . n 
B 1 60  LEU 60  58  58  LEU LEU A . n 
B 1 61  ASN 61  59  59  ASN ASN A . n 
B 1 62  ARG 62  60  60  ARG ARG A . n 
B 1 63  PRO 63  61  61  PRO PRO A . n 
B 1 64  GLY 64  62  62  GLY GLY A . n 
B 1 65  ASP 65  63  63  ASP ASP A . n 
B 1 66  GLU 66  64  64  GLU GLU A . n 
B 1 67  GLU 67  65  65  GLU GLU A . n 
B 1 68  GLY 68  66  66  GLY GLY A . n 
B 1 69  CYS 69  67  67  CYS CYS A . n 
B 1 70  GLN 70  68  68  GLN GLN A . n 
B 1 71  TRP 71  69  69  TRP TRP A . n 
B 1 72  ASN 72  70  70  ASN ASN A . n 
B 1 73  ALA 73  71  71  ALA ALA A . n 
B 1 74  GLY 74  72  72  GLY GLY A . n 
B 1 75  ALA 75  73  73  ALA ALA A . n 
B 1 76  VAL 76  74  74  VAL VAL A . n 
B 1 77  SER 77  75  75  SER SER A . n 
B 1 78  THR 78  76  76  THR THR A . n 
B 1 79  PRO 79  77  77  PRO PRO A . n 
B 1 80  ALA 80  78  78  ALA ALA A . n 
B 1 81  GLY 81  79  79  GLY GLY A . n 
B 1 82  PHE 82  80  80  PHE PHE A . n 
B 1 83  PRO 83  81  81  PRO PRO A . n 
B 1 84  GLU 84  82  82  GLU GLU A . n 
B 1 85  ALA 85  83  83  ALA ALA A . n 
B 1 86  TYR 86  84  84  TYR TYR A . n 
B 1 87  ARG 87  85  85  ARG ARG A . n 
B 1 88  THR 88  86  86  THR THR A . n 
B 1 89  TYR 89  87  87  TYR TYR A . n 
B 1 90  ALA 90  88  88  ALA ALA A . n 
B 1 91  GLU 91  89  89  GLU GLU A . n 
B 1 92  GLY 92  90  90  GLY GLY A . n 
B 1 93  GLY 93  91  91  GLY GLY A . n 
B 1 94  TRP 94  92  92  TRP TRP A . n 
B 1 95  VAL 95  93  93  VAL VAL A . n 
B 1 96  GLY 96  94  94  GLY GLY A . n 
B 1 97  VAL 97  95  95  VAL VAL A . n 
B 1 98  GLY 98  96  96  GLY GLY A . n 
B 1 99  GLY 99  97  97  GLY GLY A . n 
B 1 100 ASP 100 98  98  ASP ASP A . n 
B 1 101 PRO 101 99  99  PRO PRO A . n 
B 1 102 ALA 102 100 100 ALA ALA A . n 
B 1 103 TYR 103 101 101 TYR TYR A . n 
B 1 104 GLY 104 102 102 GLY GLY A . n 
B 1 105 GLY 105 103 103 GLY GLY A . n 
B 1 106 MET 106 104 104 MET MET A . n 
B 1 107 GLY 107 105 105 GLY GLY A . n 
B 1 108 MET 108 106 106 MET MET A . n 
B 1 109 PRO 109 107 107 PRO PRO A . n 
B 1 110 LYS 110 108 108 LYS LYS A . n 
B 1 111 VAL 111 109 109 VAL VAL A . n 
B 1 112 ILE 112 110 110 ILE ILE A . n 
B 1 113 SER 113 111 111 SER SER A . n 
B 1 114 ALA 114 112 112 ALA ALA A . n 
B 1 115 GLN 115 113 113 GLN GLN A . n 
B 1 116 VAL 116 114 114 VAL VAL A . n 
B 1 117 GLU 117 115 115 GLU GLU A . n 
B 1 118 GLU 118 116 116 GLU GLU A . n 
B 1 119 LEU 119 117 117 LEU LEU A . n 
B 1 120 VAL 120 118 118 VAL VAL A . n 
B 1 121 ASN 121 119 119 ASN ASN A . n 
B 1 122 SER 122 120 120 SER SER A . n 
B 1 123 ALA 123 121 121 ALA ALA A . n 
B 1 124 ASN 124 122 122 ASN ASN A . n 
B 1 125 LEU 125 123 123 LEU LEU A . n 
B 1 126 SER 126 124 124 SER SER A . n 
B 1 127 PHE 127 125 125 PHE PHE A . n 
B 1 128 GLY 128 126 126 GLY GLY A . n 
B 1 129 LEU 129 127 127 LEU LEU A . n 
B 1 130 TYR 130 128 128 TYR TYR A . n 
B 1 131 PRO 131 129 129 PRO PRO A . n 
B 1 132 GLY 132 130 130 GLY GLY A . n 
B 1 133 LEU 133 131 131 LEU LEU A . n 
B 1 134 THR 134 132 132 THR THR A . n 
B 1 135 ALA 135 133 133 ALA ALA A . n 
B 1 136 GLY 136 134 134 GLY GLY A . n 
B 1 137 ALA 137 135 135 ALA ALA A . n 
B 1 138 CYS 138 136 136 CYS CYS A . n 
B 1 139 LEU 139 137 137 LEU LEU A . n 
B 1 140 ALA 140 138 138 ALA ALA A . n 
B 1 141 LEU 141 139 139 LEU LEU A . n 
B 1 142 ASN 142 140 140 ASN ASN A . n 
B 1 143 ALA 143 141 141 ALA ALA A . n 
B 1 144 HIS 144 142 142 HIS HIS A . n 
B 1 145 ALA 145 143 143 ALA ALA A . n 
B 1 146 SER 146 144 144 SER SER A . n 
B 1 147 ASP 147 145 145 ASP ASP A . n 
B 1 148 GLU 148 146 146 GLU GLU A . n 
B 1 149 LEU 149 147 147 LEU LEU A . n 
B 1 150 LYS 150 148 148 LYS LYS A . n 
B 1 151 ASP 151 149 149 ASP ASP A . n 
B 1 152 LYS 152 150 150 LYS LYS A . n 
B 1 153 TYR 153 151 151 TYR TYR A . n 
B 1 154 LEU 154 152 152 LEU LEU A . n 
B 1 155 PRO 155 153 153 PRO PRO A . n 
B 1 156 ASN 156 154 154 ASN ASN A . n 
B 1 157 MET 157 155 155 MET MET A . n 
B 1 158 TYR 158 156 156 TYR TYR A . n 
B 1 159 ALA 159 157 157 ALA ALA A . n 
B 1 160 GLY 160 158 158 GLY GLY A . n 
B 1 161 ILE 161 159 159 ILE ILE A . n 
B 1 162 TRP 162 160 160 TRP TRP A . n 
B 1 163 ALA 163 161 161 ALA ALA A . n 
B 1 164 GLY 164 162 162 GLY GLY A . n 
B 1 165 SER 165 163 163 SER SER A . n 
B 1 166 MET 166 164 164 MET MET A . n 
B 1 167 CYS 167 165 165 CYS CYS A . n 
B 1 168 LEU 168 166 166 LEU LEU A . n 
B 1 169 THR 169 167 167 THR THR A . n 
B 1 170 GLU 170 168 168 GLU GLU A . n 
B 1 171 PRO 171 169 169 PRO PRO A . n 
B 1 172 HIS 172 170 170 HIS HIS A . n 
B 1 173 ALA 173 171 171 ALA ALA A . n 
B 1 174 GLY 174 172 172 GLY GLY A . n 
B 1 175 THR 175 173 173 THR THR A . n 
B 1 176 ASP 176 174 174 ASP ASP A . n 
B 1 177 LEU 177 175 175 LEU LEU A . n 
B 1 178 GLY 178 176 176 GLY GLY A . n 
B 1 179 ILE 179 177 177 ILE ILE A . n 
B 1 180 ILE 180 178 178 ILE ILE A . n 
B 1 181 ARG 181 179 179 ARG ARG A . n 
B 1 182 THR 182 180 180 THR THR A . n 
B 1 183 ARG 183 181 181 ARG ARG A . n 
B 1 184 ALA 184 182 182 ALA ALA A . n 
B 1 185 GLU 185 183 183 GLU GLU A . n 
B 1 186 PRO 186 184 184 PRO PRO A . n 
B 1 187 GLN 187 185 185 GLN GLN A . n 
B 1 188 ALA 188 186 186 ALA ALA A . n 
B 1 189 ASP 189 187 187 ASP ASP A . n 
B 1 190 GLY 190 188 188 GLY GLY A . n 
B 1 191 SER 191 189 189 SER SER A . n 
B 1 192 TYR 192 190 190 TYR TYR A . n 
B 1 193 LYS 193 191 191 LYS LYS A . n 
B 1 194 ILE 194 192 192 ILE ILE A . n 
B 1 195 SER 195 193 193 SER SER A . n 
B 1 196 GLY 196 194 194 GLY GLY A . n 
B 1 197 THR 197 195 195 THR THR A . n 
B 1 198 LYS 198 196 196 LYS LYS A . n 
B 1 199 ILE 199 197 197 ILE ILE A . n 
B 1 200 PHE 200 198 198 PHE PHE A . n 
B 1 201 ILE 201 199 199 ILE ILE A . n 
B 1 202 THR 202 200 200 THR THR A . n 
B 1 203 GLY 203 201 201 GLY GLY A . n 
B 1 204 GLY 204 202 202 GLY GLY A . n 
B 1 205 GLU 205 203 203 GLU GLU A . n 
B 1 206 HIS 206 204 204 HIS HIS A . n 
B 1 207 ASP 207 205 205 ASP ASP A . n 
B 1 208 LEU 208 206 206 LEU LEU A . n 
B 1 209 THR 209 207 207 THR THR A . n 
B 1 210 GLU 210 208 208 GLU GLU A . n 
B 1 211 ASN 211 209 209 ASN ASN A . n 
B 1 212 ILE 212 210 210 ILE ILE A . n 
B 1 213 ILE 213 211 211 ILE ILE A . n 
B 1 214 HIS 214 212 212 HIS HIS A . n 
B 1 215 LEU 215 213 213 LEU LEU A . n 
B 1 216 VAL 216 214 214 VAL VAL A . n 
B 1 217 LEU 217 215 215 LEU LEU A . n 
B 1 218 ALA 218 216 216 ALA ALA A . n 
B 1 219 LYS 219 217 217 LYS LYS A . n 
B 1 220 LEU 220 218 218 LEU LEU A . n 
B 1 221 PRO 221 219 219 PRO PRO A . n 
B 1 222 ASP 222 220 220 ASP ASP A . n 
B 1 223 ALA 223 221 221 ALA ALA A . n 
B 1 224 PRO 224 222 222 PRO PRO A . n 
B 1 225 ALA 225 223 223 ALA ALA A . n 
B 1 226 GLY 226 224 224 GLY GLY A . n 
B 1 227 PRO 227 225 225 PRO PRO A . n 
B 1 228 LYS 228 226 226 LYS LYS A . n 
B 1 229 GLY 229 227 227 GLY GLY A . n 
B 1 230 ILE 230 228 228 ILE ILE A . n 
B 1 231 SER 231 229 229 SER SER A . n 
B 1 232 LEU 232 230 230 LEU LEU A . n 
B 1 233 PHE 233 231 231 PHE PHE A . n 
B 1 234 LEU 234 232 232 LEU LEU A . n 
B 1 235 VAL 235 233 233 VAL VAL A . n 
B 1 236 PRO 236 234 234 PRO PRO A . n 
B 1 237 LYS 237 235 235 LYS LYS A . n 
B 1 238 VAL 238 236 236 VAL VAL A . n 
B 1 239 LEU 239 237 237 LEU LEU A . n 
B 1 240 VAL 240 238 238 VAL VAL A . n 
B 1 241 ASN 241 239 239 ASN ASN A . n 
B 1 242 ALA 242 240 240 ALA ALA A . n 
B 1 243 ASP 243 241 241 ASP ASP A . n 
B 1 244 GLY 244 242 242 GLY GLY A . n 
B 1 245 SER 245 243 243 SER SER A . n 
B 1 246 LEU 246 244 244 LEU LEU A . n 
B 1 247 GLY 247 245 245 GLY GLY A . n 
B 1 248 GLU 248 246 246 GLU GLU A . n 
B 1 249 LYS 249 247 247 LYS LYS A . n 
B 1 250 ASN 250 248 248 ASN ASN A . n 
B 1 251 SER 251 249 249 SER SER A . n 
B 1 252 LEU 252 250 250 LEU LEU A . n 
B 1 253 GLY 253 251 251 GLY GLY A . n 
B 1 254 CYS 254 252 252 CYS CYS A . n 
B 1 255 GLY 255 253 253 GLY GLY A . n 
B 1 256 SER 256 254 254 SER SER A . n 
B 1 257 ILE 257 255 255 ILE ILE A . n 
B 1 258 GLU 258 256 256 GLU GLU A . n 
B 1 259 HIS 259 257 257 HIS HIS A . n 
B 1 260 LYS 260 258 258 LYS LYS A . n 
B 1 261 MET 261 259 259 MET MET A . n 
B 1 262 GLY 262 260 260 GLY GLY A . n 
B 1 263 ILE 263 261 261 ILE ILE A . n 
B 1 264 LYS 264 262 262 LYS LYS A . n 
B 1 265 ALA 265 263 263 ALA ALA A . n 
B 1 266 SER 266 264 264 SER SER A . n 
B 1 267 ALA 267 265 265 ALA ALA A . n 
B 1 268 THR 268 266 266 THR THR A . n 
B 1 269 CYS 269 267 267 CYS CYS A . n 
B 1 270 VAL 270 268 268 VAL VAL A . n 
B 1 271 MET 271 269 269 MET MET A . n 
B 1 272 ASN 272 270 270 ASN ASN A . n 
B 1 273 PHE 273 271 271 PHE PHE A . n 
B 1 274 ASP 274 272 272 ASP ASP A . n 
B 1 275 GLY 275 273 273 GLY GLY A . n 
B 1 276 ALA 276 274 274 ALA ALA A . n 
B 1 277 THR 277 275 275 THR THR A . n 
B 1 278 GLY 278 276 276 GLY GLY A . n 
B 1 279 TRP 279 277 277 TRP TRP A . n 
B 1 280 LEU 280 278 278 LEU LEU A . n 
B 1 281 VAL 281 279 279 VAL VAL A . n 
B 1 282 GLY 282 280 280 GLY GLY A . n 
B 1 283 GLU 283 281 281 GLU GLU A . n 
B 1 284 VAL 284 282 282 VAL VAL A . n 
B 1 285 ASN 285 283 283 ASN ASN A . n 
B 1 286 LYS 286 284 284 LYS LYS A . n 
B 1 287 GLY 287 285 285 GLY GLY A . n 
B 1 288 LEU 288 286 286 LEU LEU A . n 
B 1 289 ALA 289 287 287 ALA ALA A . n 
B 1 290 ALA 290 288 288 ALA ALA A . n 
B 1 291 MET 291 289 289 MET MET A . n 
B 1 292 PHE 292 290 290 PHE PHE A . n 
B 1 293 THR 293 291 291 THR THR A . n 
B 1 294 MET 294 292 292 MET MET A . n 
B 1 295 MET 295 293 293 MET MET A . n 
B 1 296 ASN 296 294 294 ASN ASN A . n 
B 1 297 TYR 297 295 295 TYR TYR A . n 
B 1 298 ALA 298 296 296 ALA ALA A . n 
B 1 299 ARG 299 297 297 ARG ARG A . n 
B 1 300 LEU 300 298 298 LEU LEU A . n 
B 1 301 GLY 301 299 299 GLY GLY A . n 
B 1 302 VAL 302 300 300 VAL VAL A . n 
B 1 303 GLY 303 301 301 GLY GLY A . n 
B 1 304 ILE 304 302 302 ILE ILE A . n 
B 1 305 ALA 305 303 303 ALA ALA A . n 
B 1 306 GLY 306 304 304 GLY GLY A . n 
B 1 307 LEU 307 305 305 LEU LEU A . n 
B 1 308 ALA 308 306 306 ALA ALA A . n 
B 1 309 THR 309 307 307 THR THR A . n 
B 1 310 GLY 310 308 308 GLY GLY A . n 
B 1 311 GLU 311 309 309 GLU GLU A . n 
B 1 312 ARG 312 310 310 ARG ARG A . n 
B 1 313 SER 313 311 311 SER SER A . n 
B 1 314 TYR 314 312 312 TYR TYR A . n 
B 1 315 GLN 315 313 313 GLN GLN A . n 
B 1 316 SER 316 314 314 SER SER A . n 
B 1 317 ALA 317 315 315 ALA ALA A . n 
B 1 318 ILE 318 316 316 ILE ILE A . n 
B 1 319 GLU 319 317 317 GLU GLU A . n 
B 1 320 TYR 320 318 318 TYR TYR A . n 
B 1 321 ALA 321 319 319 ALA ALA A . n 
B 1 322 ARG 322 320 320 ARG ARG A . n 
B 1 323 GLU 323 321 321 GLU GLU A . n 
B 1 324 ARG 324 322 322 ARG ARG A . n 
B 1 325 ILE 325 323 323 ILE ILE A . n 
B 1 326 GLN 326 324 324 GLN GLN A . n 
B 1 327 SER 327 325 325 SER SER A . n 
B 1 328 ARG 328 326 326 ARG ARG A . n 
B 1 329 ALA 329 327 327 ALA ALA A . n 
B 1 330 PRO 330 328 328 PRO PRO A . n 
B 1 331 THR 331 329 329 THR THR A . n 
B 1 332 GLY 332 330 330 GLY GLY A . n 
B 1 333 PRO 333 331 331 PRO PRO A . n 
B 1 334 VAL 334 332 332 VAL VAL A . n 
B 1 335 ALA 335 333 333 ALA ALA A . n 
B 1 336 LYS 336 334 334 LYS LYS A . n 
B 1 337 ASP 337 335 335 ASP ASP A . n 
B 1 338 LYS 338 336 336 LYS LYS A . n 
B 1 339 ALA 339 337 337 ALA ALA A . n 
B 1 340 ALA 340 338 338 ALA ALA A . n 
B 1 341 ASP 341 339 339 ASP ASP A . n 
B 1 342 PRO 342 340 340 PRO PRO A . n 
B 1 343 ILE 343 341 341 ILE ILE A . n 
B 1 344 ILE 344 342 342 ILE ILE A . n 
B 1 345 VAL 345 343 343 VAL VAL A . n 
B 1 346 HIS 346 344 344 HIS HIS A . n 
B 1 347 PRO 347 345 345 PRO PRO A . n 
B 1 348 ASP 348 346 346 ASP ASP A . n 
B 1 349 VAL 349 347 347 VAL VAL A . n 
B 1 350 ARG 350 348 348 ARG ARG A . n 
B 1 351 ARG 351 349 349 ARG ARG A . n 
B 1 352 MET 352 350 350 MET MET A . n 
B 1 353 LEU 353 351 351 LEU LEU A . n 
B 1 354 LEU 354 352 352 LEU LEU A . n 
B 1 355 THR 355 353 353 THR THR A . n 
B 1 356 MET 356 354 354 MET MET A . n 
B 1 357 LYS 357 355 355 LYS LYS A . n 
B 1 358 ALA 358 356 356 ALA ALA A . n 
B 1 359 LEU 359 357 357 LEU LEU A . n 
B 1 360 ASN 360 358 358 ASN ASN A . n 
B 1 361 GLU 361 359 359 GLU GLU A . n 
B 1 362 GLY 362 360 360 GLY GLY A . n 
B 1 363 GLY 363 361 361 GLY GLY A . n 
B 1 364 ARG 364 362 362 ARG ARG A . n 
B 1 365 ALA 365 363 363 ALA ALA A . n 
B 1 366 PHE 366 364 364 PHE PHE A . n 
B 1 367 SER 367 365 365 SER SER A . n 
B 1 368 SER 368 366 366 SER SER A . n 
B 1 369 TYR 369 367 367 TYR TYR A . n 
B 1 370 VAL 370 368 368 VAL VAL A . n 
B 1 371 ALA 371 369 369 ALA ALA A . n 
B 1 372 MET 372 370 370 MET MET A . n 
B 1 373 GLN 373 371 371 GLN GLN A . n 
B 1 374 LEU 374 372 372 LEU LEU A . n 
B 1 375 ASP 375 373 373 ASP ASP A . n 
B 1 376 THR 376 374 374 THR THR A . n 
B 1 377 ALA 377 375 375 ALA ALA A . n 
B 1 378 LYS 378 376 376 LYS LYS A . n 
B 1 379 TYR 379 377 377 TYR TYR A . n 
B 1 380 SER 380 378 378 SER SER A . n 
B 1 381 GLU 381 379 379 GLU GLU A . n 
B 1 382 ASP 382 380 380 ASP ASP A . n 
B 1 383 ALA 383 381 381 ALA ALA A . n 
B 1 384 VAL 384 382 382 VAL VAL A . n 
B 1 385 THR 385 383 383 THR THR A . n 
B 1 386 ARG 386 384 384 ARG ARG A . n 
B 1 387 LYS 387 385 385 LYS LYS A . n 
B 1 388 ARG 388 386 386 ARG ARG A . n 
B 1 389 ALA 389 387 387 ALA ALA A . n 
B 1 390 GLU 390 388 388 GLU GLU A . n 
B 1 391 GLU 391 389 389 GLU GLU A . n 
B 1 392 LEU 392 390 390 LEU LEU A . n 
B 1 393 VAL 393 391 391 VAL VAL A . n 
B 1 394 ALA 394 392 392 ALA ALA A . n 
B 1 395 LEU 395 393 393 LEU LEU A . n 
B 1 396 LEU 396 394 394 LEU LEU A . n 
B 1 397 THR 397 395 395 THR THR A . n 
B 1 398 PRO 398 396 396 PRO PRO A . n 
B 1 399 VAL 399 397 397 VAL VAL A . n 
B 1 400 ALA 400 398 398 ALA ALA A . n 
B 1 401 LYS 401 399 399 LYS LYS A . n 
B 1 402 ALA 402 400 400 ALA ALA A . n 
B 1 403 PHE 403 401 401 PHE PHE A . n 
B 1 404 LEU 404 402 402 LEU LEU A . n 
B 1 405 THR 405 403 403 THR THR A . n 
B 1 406 ASP 406 404 404 ASP ASP A . n 
B 1 407 MET 407 405 405 MET MET A . n 
B 1 408 GLY 408 406 406 GLY GLY A . n 
B 1 409 LEU 409 407 407 LEU LEU A . n 
B 1 410 GLU 410 408 408 GLU GLU A . n 
B 1 411 THR 411 409 409 THR THR A . n 
B 1 412 THR 412 410 410 THR THR A . n 
B 1 413 ILE 413 411 411 ILE ILE A . n 
B 1 414 HIS 414 412 412 HIS HIS A . n 
B 1 415 GLY 415 413 413 GLY GLY A . n 
B 1 416 GLN 416 414 414 GLN GLN A . n 
B 1 417 GLN 417 415 415 GLN GLN A . n 
B 1 418 ILE 418 416 416 ILE ILE A . n 
B 1 419 PHE 419 417 417 PHE PHE A . n 
B 1 420 GLY 420 418 418 GLY GLY A . n 
B 1 421 GLY 421 419 419 GLY GLY A . n 
B 1 422 HIS 422 420 420 HIS HIS A . n 
B 1 423 GLY 423 421 421 GLY GLY A . n 
B 1 424 PHE 424 422 422 PHE PHE A . n 
B 1 425 ILE 425 423 423 ILE ILE A . n 
B 1 426 ARG 426 424 424 ARG ARG A . n 
B 1 427 GLU 427 425 425 GLU GLU A . n 
B 1 428 TRP 428 426 426 TRP TRP A . n 
B 1 429 GLY 429 427 427 GLY GLY A . n 
B 1 430 GLN 430 428 428 GLN GLN A . n 
B 1 431 GLU 431 429 429 GLU GLU A . n 
B 1 432 GLN 432 430 430 GLN GLN A . n 
B 1 433 LEU 433 431 431 LEU LEU A . n 
B 1 434 VAL 434 432 432 VAL VAL A . n 
B 1 435 ARG 435 433 433 ARG ARG A . n 
B 1 436 ASP 436 434 434 ASP ASP A . n 
B 1 437 CYS 437 435 435 CYS CYS A . n 
B 1 438 ARG 438 436 436 ARG ARG A . n 
B 1 439 ILE 439 437 437 ILE ILE A . n 
B 1 440 THR 440 438 438 THR THR A . n 
B 1 441 GLN 441 439 439 GLN GLN A . n 
B 1 442 ILE 442 440 440 ILE ILE A . n 
B 1 443 TYR 443 441 441 TYR TYR A . n 
B 1 444 GLU 444 442 442 GLU GLU A . n 
B 1 445 GLY 445 443 443 GLY GLY A . n 
B 1 446 THR 446 444 444 THR THR A . n 
B 1 447 ASN 447 445 445 ASN ASN A . n 
B 1 448 GLY 448 446 446 GLY GLY A . n 
B 1 449 ILE 449 447 447 ILE ILE A . n 
B 1 450 GLN 450 448 448 GLN GLN A . n 
B 1 451 ALA 451 449 449 ALA ALA A . n 
B 1 452 LEU 452 450 450 LEU LEU A . n 
B 1 453 ASP 453 451 451 ASP ASP A . n 
B 1 454 LEU 454 452 452 LEU LEU A . n 
B 1 455 VAL 455 453 453 VAL VAL A . n 
B 1 456 GLY 456 454 454 GLY GLY A . n 
B 1 457 ARG 457 455 455 ARG ARG A . n 
B 1 458 LYS 458 456 456 LYS LYS A . n 
B 1 459 VAL 459 457 457 VAL VAL A . n 
B 1 460 ILE 460 458 458 ILE ILE A . n 
B 1 461 GLY 461 459 459 GLY GLY A . n 
B 1 462 SER 462 460 460 SER SER A . n 
B 1 463 GLY 463 461 461 GLY GLY A . n 
B 1 464 GLY 464 462 462 GLY GLY A . n 
B 1 465 ALA 465 463 463 ALA ALA A . n 
B 1 466 PHE 466 464 464 PHE PHE A . n 
B 1 467 SER 467 465 465 SER SER A . n 
B 1 468 ARG 468 466 466 ARG ARG A . n 
B 1 469 HIS 469 467 467 HIS HIS A . n 
B 1 470 PHE 470 468 468 PHE PHE A . n 
B 1 471 THR 471 469 469 THR THR A . n 
B 1 472 ASP 472 470 470 ASP ASP A . n 
B 1 473 GLU 473 471 471 GLU GLU A . n 
B 1 474 ILE 474 472 472 ILE ILE A . n 
B 1 475 LYS 475 473 473 LYS LYS A . n 
B 1 476 ALA 476 474 474 ALA ALA A . n 
B 1 477 PHE 477 475 475 PHE PHE A . n 
B 1 478 VAL 478 476 476 VAL VAL A . n 
B 1 479 ALA 479 477 477 ALA ALA A . n 
B 1 480 SER 480 478 478 SER SER A . n 
B 1 481 ALA 481 479 479 ALA ALA A . n 
B 1 482 ASP 482 480 480 ASP ASP A . n 
B 1 483 GLU 483 481 481 GLU GLU A . n 
B 1 484 ALA 484 482 482 ALA ALA A . n 
B 1 485 LEU 485 483 483 LEU LEU A . n 
B 1 486 GLY 486 484 484 GLY GLY A . n 
B 1 487 GLU 487 485 485 GLU GLU A . n 
B 1 488 PHE 488 486 486 PHE PHE A . n 
B 1 489 SER 489 487 487 SER SER A . n 
B 1 490 LYS 490 488 488 LYS LYS A . n 
B 1 491 PRO 491 489 489 PRO PRO A . n 
B 1 492 LEU 492 490 490 LEU LEU A . n 
B 1 493 ALA 493 491 491 ALA ALA A . n 
B 1 494 ALA 494 492 492 ALA ALA A . n 
B 1 495 ALA 495 493 493 ALA ALA A . n 
B 1 496 VAL 496 494 494 VAL VAL A . n 
B 1 497 GLU 497 495 495 GLU GLU A . n 
B 1 498 ASN 498 496 496 ASN ASN A . n 
B 1 499 LEU 499 497 497 LEU LEU A . n 
B 1 500 GLU 500 498 498 GLU GLU A . n 
B 1 501 GLU 501 499 499 GLU GLU A . n 
B 1 502 LEU 502 500 500 LEU LEU A . n 
B 1 503 THR 503 501 501 THR THR A . n 
B 1 504 ALA 504 502 502 ALA ALA A . n 
B 1 505 TRP 505 503 503 TRP TRP A . n 
B 1 506 LEU 506 504 504 LEU LEU A . n 
B 1 507 LEU 507 505 505 LEU LEU A . n 
B 1 508 ASP 508 506 506 ASP ASP A . n 
B 1 509 ARG 509 507 507 ARG ARG A . n 
B 1 510 ALA 510 508 508 ALA ALA A . n 
B 1 511 LYS 511 509 509 LYS LYS A . n 
B 1 512 GLY 512 510 510 GLY GLY A . n 
B 1 513 ASN 513 511 511 ASN ASN A . n 
B 1 514 PRO 514 512 512 PRO PRO A . n 
B 1 515 ASN 515 513 513 ASN ASN A . n 
B 1 516 GLU 516 514 514 GLU GLU A . n 
B 1 517 ILE 517 515 515 ILE ILE A . n 
B 1 518 GLY 518 516 516 GLY GLY A . n 
B 1 519 ALA 519 517 517 ALA ALA A . n 
B 1 520 ALA 520 518 518 ALA ALA A . n 
B 1 521 SER 521 519 519 SER SER A . n 
B 1 522 VAL 522 520 520 VAL VAL A . n 
B 1 523 GLU 523 521 521 GLU GLU A . n 
B 1 524 TYR 524 522 522 TYR TYR A . n 
B 1 525 LEU 525 523 523 LEU LEU A . n 
B 1 526 HIS 526 524 524 HIS HIS A . n 
B 1 527 VAL 527 525 525 VAL VAL A . n 
B 1 528 PHE 528 526 526 PHE PHE A . n 
B 1 529 GLY 529 527 527 GLY GLY A . n 
B 1 530 TYR 530 528 528 TYR TYR A . n 
B 1 531 THR 531 529 529 THR THR A . n 
B 1 532 ALA 532 530 530 ALA ALA A . n 
B 1 533 TYR 533 531 531 TYR TYR A . n 
B 1 534 ALA 534 532 532 ALA ALA A . n 
B 1 535 TYR 535 533 533 TYR TYR A . n 
B 1 536 MET 536 534 534 MET MET A . n 
B 1 537 TRP 537 535 535 TRP TRP A . n 
B 1 538 ALA 538 536 536 ALA ALA A . n 
B 1 539 LEU 539 537 537 LEU LEU A . n 
B 1 540 MET 540 538 538 MET MET A . n 
B 1 541 ALA 541 539 539 ALA ALA A . n 
B 1 542 ARG 542 540 540 ARG ARG A . n 
B 1 543 THR 543 541 541 THR THR A . n 
B 1 544 ALA 544 542 542 ALA ALA A . n 
B 1 545 LEU 545 543 543 LEU LEU A . n 
B 1 546 ALA 546 544 544 ALA ALA A . n 
B 1 547 LYS 547 545 545 LYS LYS A . n 
B 1 548 GLN 548 546 546 GLN GLN A . n 
B 1 549 GLY 549 547 547 GLY GLY A . n 
B 1 550 GLU 550 548 548 GLU GLU A . n 
B 1 551 ASP 551 549 549 ASP ASP A . n 
B 1 552 ASP 552 550 550 ASP ASP A . n 
B 1 553 PHE 553 551 551 PHE PHE A . n 
B 1 554 TYR 554 552 552 TYR TYR A . n 
B 1 555 ALA 555 553 553 ALA ALA A . n 
B 1 556 SER 556 554 554 SER SER A . n 
B 1 557 LYS 557 555 555 LYS LYS A . n 
B 1 558 LEU 558 556 556 LEU LEU A . n 
B 1 559 GLY 559 557 557 GLY GLY A . n 
B 1 560 THR 560 558 558 THR THR A . n 
B 1 561 ALA 561 559 559 ALA ALA A . n 
B 1 562 ARG 562 560 560 ARG ARG A . n 
B 1 563 PHE 563 561 561 PHE PHE A . n 
B 1 564 TYR 564 562 562 TYR TYR A . n 
B 1 565 PHE 565 563 563 PHE PHE A . n 
B 1 566 ALA 566 564 564 ALA ALA A . n 
B 1 567 ARG 567 565 565 ARG ARG A . n 
B 1 568 LEU 568 566 566 LEU LEU A . n 
B 1 569 LEU 569 567 567 LEU LEU A . n 
B 1 570 PRO 570 568 568 PRO PRO A . n 
B 1 571 ARG 571 569 569 ARG ARG A . n 
B 1 572 ILE 572 570 570 ILE ILE A . n 
B 1 573 HIS 573 571 571 HIS HIS A . n 
B 1 574 SER 574 572 572 SER SER A . n 
B 1 575 LEU 575 573 573 LEU LEU A . n 
B 1 576 SER 576 574 574 SER SER A . n 
B 1 577 ALA 577 575 575 ALA ALA A . n 
B 1 578 SER 578 576 576 SER SER A . n 
B 1 579 VAL 579 577 577 VAL VAL A . n 
B 1 580 ARG 580 578 578 ARG ARG A . n 
B 1 581 ALA 581 579 579 ALA ALA A . n 
B 1 582 GLY 582 580 580 GLY GLY A . n 
B 1 583 SER 583 581 581 SER SER A . n 
B 1 584 GLU 584 582 582 GLU GLU A . n 
B 1 585 SER 585 583 583 SER SER A . n 
B 1 586 LEU 586 584 584 LEU LEU A . n 
B 1 587 TYR 587 585 585 TYR TYR A . n 
B 1 588 LEU 588 586 586 LEU LEU A . n 
B 1 589 LEU 589 587 587 LEU LEU A . n 
B 1 590 ASP 590 588 588 ASP ASP A . n 
B 1 591 ALA 591 589 589 ALA ALA A . n 
B 1 592 GLU 592 590 590 GLU GLU A . n 
B 1 593 GLN 593 591 591 GLN GLN A . n 
B 1 594 PHE 594 592 592 PHE PHE A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        FAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   FAD 
_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 
C 2 FAD 1   601  601  FAD FAD B . 
D 3 GOL 1   602  602  GOL GOL B . 
E 2 FAD 1   601  601  FAD FAD A . 
F 3 GOL 1   602  1001 GOL GOL A . 
G 3 GOL 1   603  1002 GOL GOL A . 
H 4 PGE 1   604  1003 PGE PGE A . 
I 5 HOH 1   701  206  HOH HOH B . 
I 5 HOH 2   702  196  HOH HOH B . 
I 5 HOH 3   703  73   HOH HOH B . 
I 5 HOH 4   704  466  HOH HOH B . 
I 5 HOH 5   705  234  HOH HOH B . 
I 5 HOH 6   706  608  HOH HOH B . 
I 5 HOH 7   707  197  HOH HOH B . 
I 5 HOH 8   708  169  HOH HOH B . 
I 5 HOH 9   709  24   HOH HOH B . 
I 5 HOH 10  710  327  HOH HOH B . 
I 5 HOH 11  711  117  HOH HOH B . 
I 5 HOH 12  712  733  HOH HOH B . 
I 5 HOH 13  713  582  HOH HOH B . 
I 5 HOH 14  714  625  HOH HOH B . 
I 5 HOH 15  715  249  HOH HOH B . 
I 5 HOH 16  716  551  HOH HOH B . 
I 5 HOH 17  717  594  HOH HOH B . 
I 5 HOH 18  718  59   HOH HOH B . 
I 5 HOH 19  719  185  HOH HOH B . 
I 5 HOH 20  720  63   HOH HOH B . 
I 5 HOH 21  721  235  HOH HOH B . 
I 5 HOH 22  722  103  HOH HOH B . 
I 5 HOH 23  723  552  HOH HOH B . 
I 5 HOH 24  724  288  HOH HOH B . 
I 5 HOH 25  725  655  HOH HOH B . 
I 5 HOH 26  726  504  HOH HOH B . 
I 5 HOH 27  727  634  HOH HOH B . 
I 5 HOH 28  728  800  HOH HOH B . 
I 5 HOH 29  729  222  HOH HOH B . 
I 5 HOH 30  730  841  HOH HOH B . 
I 5 HOH 31  731  395  HOH HOH B . 
I 5 HOH 32  732  493  HOH HOH B . 
I 5 HOH 33  733  799  HOH HOH B . 
I 5 HOH 34  734  727  HOH HOH B . 
I 5 HOH 35  735  572  HOH HOH B . 
I 5 HOH 36  736  45   HOH HOH B . 
I 5 HOH 37  737  769  HOH HOH B . 
I 5 HOH 38  738  175  HOH HOH B . 
I 5 HOH 39  739  80   HOH HOH B . 
I 5 HOH 40  740  33   HOH HOH B . 
I 5 HOH 41  741  32   HOH HOH B . 
I 5 HOH 42  742  81   HOH HOH B . 
I 5 HOH 43  743  495  HOH HOH B . 
I 5 HOH 44  744  590  HOH HOH B . 
I 5 HOH 45  745  830  HOH HOH B . 
I 5 HOH 46  746  737  HOH HOH B . 
I 5 HOH 47  747  12   HOH HOH B . 
I 5 HOH 48  748  133  HOH HOH B . 
I 5 HOH 49  749  72   HOH HOH B . 
I 5 HOH 50  750  369  HOH HOH B . 
I 5 HOH 51  751  315  HOH HOH B . 
I 5 HOH 52  752  23   HOH HOH B . 
I 5 HOH 53  753  813  HOH HOH B . 
I 5 HOH 54  754  697  HOH HOH B . 
I 5 HOH 55  755  528  HOH HOH B . 
I 5 HOH 56  756  428  HOH HOH B . 
I 5 HOH 57  757  238  HOH HOH B . 
I 5 HOH 58  758  186  HOH HOH B . 
I 5 HOH 59  759  679  HOH HOH B . 
I 5 HOH 60  760  644  HOH HOH B . 
I 5 HOH 61  761  156  HOH HOH B . 
I 5 HOH 62  762  684  HOH HOH B . 
I 5 HOH 63  763  364  HOH HOH B . 
I 5 HOH 64  764  579  HOH HOH B . 
I 5 HOH 65  765  663  HOH HOH B . 
I 5 HOH 66  766  85   HOH HOH B . 
I 5 HOH 67  767  533  HOH HOH B . 
I 5 HOH 68  768  734  HOH HOH B . 
I 5 HOH 69  769  512  HOH HOH B . 
I 5 HOH 70  770  822  HOH HOH B . 
I 5 HOH 71  771  35   HOH HOH B . 
I 5 HOH 72  772  283  HOH HOH B . 
I 5 HOH 73  773  251  HOH HOH B . 
I 5 HOH 74  774  29   HOH HOH B . 
I 5 HOH 75  775  88   HOH HOH B . 
I 5 HOH 76  776  243  HOH HOH B . 
I 5 HOH 77  777  136  HOH HOH B . 
I 5 HOH 78  778  346  HOH HOH B . 
I 5 HOH 79  779  98   HOH HOH B . 
I 5 HOH 80  780  721  HOH HOH B . 
I 5 HOH 81  781  227  HOH HOH B . 
I 5 HOH 82  782  335  HOH HOH B . 
I 5 HOH 83  783  70   HOH HOH B . 
I 5 HOH 84  784  92   HOH HOH B . 
I 5 HOH 85  785  377  HOH HOH B . 
I 5 HOH 86  786  363  HOH HOH B . 
I 5 HOH 87  787  93   HOH HOH B . 
I 5 HOH 88  788  587  HOH HOH B . 
I 5 HOH 89  789  125  HOH HOH B . 
I 5 HOH 90  790  825  HOH HOH B . 
I 5 HOH 91  791  757  HOH HOH B . 
I 5 HOH 92  792  442  HOH HOH B . 
I 5 HOH 93  793  255  HOH HOH B . 
I 5 HOH 94  794  13   HOH HOH B . 
I 5 HOH 95  795  632  HOH HOH B . 
I 5 HOH 96  796  338  HOH HOH B . 
I 5 HOH 97  797  660  HOH HOH B . 
I 5 HOH 98  798  357  HOH HOH B . 
I 5 HOH 99  799  397  HOH HOH B . 
I 5 HOH 100 800  460  HOH HOH B . 
I 5 HOH 101 801  437  HOH HOH B . 
I 5 HOH 102 802  793  HOH HOH B . 
I 5 HOH 103 803  838  HOH HOH B . 
I 5 HOH 104 804  262  HOH HOH B . 
I 5 HOH 105 805  686  HOH HOH B . 
I 5 HOH 106 806  26   HOH HOH B . 
I 5 HOH 107 807  605  HOH HOH B . 
I 5 HOH 108 808  265  HOH HOH B . 
I 5 HOH 109 809  256  HOH HOH B . 
I 5 HOH 110 810  46   HOH HOH B . 
I 5 HOH 111 811  18   HOH HOH B . 
I 5 HOH 112 812  419  HOH HOH B . 
I 5 HOH 113 813  412  HOH HOH B . 
I 5 HOH 114 814  447  HOH HOH B . 
I 5 HOH 115 815  839  HOH HOH B . 
I 5 HOH 116 816  783  HOH HOH B . 
I 5 HOH 117 817  297  HOH HOH B . 
I 5 HOH 118 818  253  HOH HOH B . 
I 5 HOH 119 819  150  HOH HOH B . 
I 5 HOH 120 820  776  HOH HOH B . 
I 5 HOH 121 821  667  HOH HOH B . 
I 5 HOH 122 822  431  HOH HOH B . 
I 5 HOH 123 823  147  HOH HOH B . 
I 5 HOH 124 824  671  HOH HOH B . 
I 5 HOH 125 825  109  HOH HOH B . 
I 5 HOH 126 826  486  HOH HOH B . 
I 5 HOH 127 827  220  HOH HOH B . 
I 5 HOH 128 828  788  HOH HOH B . 
I 5 HOH 129 829  61   HOH HOH B . 
I 5 HOH 130 830  78   HOH HOH B . 
I 5 HOH 131 831  151  HOH HOH B . 
I 5 HOH 132 832  187  HOH HOH B . 
I 5 HOH 133 833  477  HOH HOH B . 
I 5 HOH 134 834  482  HOH HOH B . 
I 5 HOH 135 835  614  HOH HOH B . 
I 5 HOH 136 836  36   HOH HOH B . 
I 5 HOH 137 837  791  HOH HOH B . 
I 5 HOH 138 838  748  HOH HOH B . 
I 5 HOH 139 839  135  HOH HOH B . 
I 5 HOH 140 840  621  HOH HOH B . 
I 5 HOH 141 841  340  HOH HOH B . 
I 5 HOH 142 842  501  HOH HOH B . 
I 5 HOH 143 843  167  HOH HOH B . 
I 5 HOH 144 844  3    HOH HOH B . 
I 5 HOH 145 845  553  HOH HOH B . 
I 5 HOH 146 846  824  HOH HOH B . 
I 5 HOH 147 847  304  HOH HOH B . 
I 5 HOH 148 848  164  HOH HOH B . 
I 5 HOH 149 849  50   HOH HOH B . 
I 5 HOH 150 850  404  HOH HOH B . 
I 5 HOH 151 851  141  HOH HOH B . 
I 5 HOH 152 852  543  HOH HOH B . 
I 5 HOH 153 853  286  HOH HOH B . 
I 5 HOH 154 854  628  HOH HOH B . 
I 5 HOH 155 855  56   HOH HOH B . 
I 5 HOH 156 856  246  HOH HOH B . 
I 5 HOH 157 857  524  HOH HOH B . 
I 5 HOH 158 858  252  HOH HOH B . 
I 5 HOH 159 859  725  HOH HOH B . 
I 5 HOH 160 860  445  HOH HOH B . 
I 5 HOH 161 861  691  HOH HOH B . 
I 5 HOH 162 862  516  HOH HOH B . 
I 5 HOH 163 863  245  HOH HOH B . 
I 5 HOH 164 864  55   HOH HOH B . 
I 5 HOH 165 865  492  HOH HOH B . 
I 5 HOH 166 866  588  HOH HOH B . 
I 5 HOH 167 867  532  HOH HOH B . 
I 5 HOH 168 868  812  HOH HOH B . 
I 5 HOH 169 869  809  HOH HOH B . 
I 5 HOH 170 870  277  HOH HOH B . 
I 5 HOH 171 871  11   HOH HOH B . 
I 5 HOH 172 872  140  HOH HOH B . 
I 5 HOH 173 873  728  HOH HOH B . 
I 5 HOH 174 874  290  HOH HOH B . 
I 5 HOH 175 875  6    HOH HOH B . 
I 5 HOH 176 876  427  HOH HOH B . 
I 5 HOH 177 877  307  HOH HOH B . 
I 5 HOH 178 878  779  HOH HOH B . 
I 5 HOH 179 879  142  HOH HOH B . 
I 5 HOH 180 880  536  HOH HOH B . 
I 5 HOH 181 881  145  HOH HOH B . 
I 5 HOH 182 882  378  HOH HOH B . 
I 5 HOH 183 883  476  HOH HOH B . 
I 5 HOH 184 884  326  HOH HOH B . 
I 5 HOH 185 885  803  HOH HOH B . 
I 5 HOH 186 886  480  HOH HOH B . 
I 5 HOH 187 887  408  HOH HOH B . 
I 5 HOH 188 888  527  HOH HOH B . 
I 5 HOH 189 889  106  HOH HOH B . 
I 5 HOH 190 890  595  HOH HOH B . 
I 5 HOH 191 891  1    HOH HOH B . 
I 5 HOH 192 892  782  HOH HOH B . 
I 5 HOH 193 893  105  HOH HOH B . 
I 5 HOH 194 894  345  HOH HOH B . 
I 5 HOH 195 895  438  HOH HOH B . 
I 5 HOH 196 896  798  HOH HOH B . 
I 5 HOH 197 897  461  HOH HOH B . 
I 5 HOH 198 898  380  HOH HOH B . 
I 5 HOH 199 899  659  HOH HOH B . 
I 5 HOH 200 900  259  HOH HOH B . 
I 5 HOH 201 901  381  HOH HOH B . 
I 5 HOH 202 902  597  HOH HOH B . 
I 5 HOH 203 903  342  HOH HOH B . 
I 5 HOH 204 904  453  HOH HOH B . 
I 5 HOH 205 905  511  HOH HOH B . 
I 5 HOH 206 906  499  HOH HOH B . 
I 5 HOH 207 907  69   HOH HOH B . 
I 5 HOH 208 908  452  HOH HOH B . 
I 5 HOH 209 909  610  HOH HOH B . 
I 5 HOH 210 910  731  HOH HOH B . 
I 5 HOH 211 911  766  HOH HOH B . 
I 5 HOH 212 912  218  HOH HOH B . 
I 5 HOH 213 913  42   HOH HOH B . 
I 5 HOH 214 914  181  HOH HOH B . 
I 5 HOH 215 915  780  HOH HOH B . 
I 5 HOH 216 916  39   HOH HOH B . 
I 5 HOH 217 917  158  HOH HOH B . 
I 5 HOH 218 918  83   HOH HOH B . 
I 5 HOH 219 919  391  HOH HOH B . 
I 5 HOH 220 920  310  HOH HOH B . 
I 5 HOH 221 921  418  HOH HOH B . 
I 5 HOH 222 922  382  HOH HOH B . 
I 5 HOH 223 923  744  HOH HOH B . 
I 5 HOH 224 924  710  HOH HOH B . 
I 5 HOH 225 925  424  HOH HOH B . 
I 5 HOH 226 926  629  HOH HOH B . 
I 5 HOH 227 927  677  HOH HOH B . 
I 5 HOH 228 928  184  HOH HOH B . 
I 5 HOH 229 929  314  HOH HOH B . 
I 5 HOH 230 930  361  HOH HOH B . 
I 5 HOH 231 931  149  HOH HOH B . 
I 5 HOH 232 932  325  HOH HOH B . 
I 5 HOH 233 933  210  HOH HOH B . 
I 5 HOH 234 934  498  HOH HOH B . 
I 5 HOH 235 935  500  HOH HOH B . 
I 5 HOH 236 936  275  HOH HOH B . 
I 5 HOH 237 937  429  HOH HOH B . 
I 5 HOH 238 938  161  HOH HOH B . 
I 5 HOH 239 939  612  HOH HOH B . 
I 5 HOH 240 940  450  HOH HOH B . 
I 5 HOH 241 941  344  HOH HOH B . 
I 5 HOH 242 942  446  HOH HOH B . 
I 5 HOH 243 943  284  HOH HOH B . 
I 5 HOH 244 944  707  HOH HOH B . 
I 5 HOH 245 945  517  HOH HOH B . 
I 5 HOH 246 946  312  HOH HOH B . 
I 5 HOH 247 947  859  HOH HOH B . 
I 5 HOH 248 948  645  HOH HOH B . 
I 5 HOH 249 949  669  HOH HOH B . 
I 5 HOH 250 950  506  HOH HOH B . 
I 5 HOH 251 951  542  HOH HOH B . 
I 5 HOH 252 952  318  HOH HOH B . 
I 5 HOH 253 953  121  HOH HOH B . 
I 5 HOH 254 954  405  HOH HOH B . 
I 5 HOH 255 955  472  HOH HOH B . 
I 5 HOH 256 956  845  HOH HOH B . 
I 5 HOH 257 957  298  HOH HOH B . 
I 5 HOH 258 958  198  HOH HOH B . 
I 5 HOH 259 959  126  HOH HOH B . 
I 5 HOH 260 960  703  HOH HOH B . 
I 5 HOH 261 961  539  HOH HOH B . 
I 5 HOH 262 962  305  HOH HOH B . 
I 5 HOH 263 963  535  HOH HOH B . 
I 5 HOH 264 964  8    HOH HOH B . 
I 5 HOH 265 965  47   HOH HOH B . 
I 5 HOH 266 966  349  HOH HOH B . 
I 5 HOH 267 967  44   HOH HOH B . 
I 5 HOH 268 968  577  HOH HOH B . 
I 5 HOH 269 969  5    HOH HOH B . 
I 5 HOH 270 970  618  HOH HOH B . 
I 5 HOH 271 971  626  HOH HOH B . 
I 5 HOH 272 972  620  HOH HOH B . 
I 5 HOH 273 973  853  HOH HOH B . 
I 5 HOH 274 974  688  HOH HOH B . 
I 5 HOH 275 975  538  HOH HOH B . 
I 5 HOH 276 976  212  HOH HOH B . 
I 5 HOH 277 977  751  HOH HOH B . 
I 5 HOH 278 978  287  HOH HOH B . 
I 5 HOH 279 979  646  HOH HOH B . 
I 5 HOH 280 980  735  HOH HOH B . 
I 5 HOH 281 981  457  HOH HOH B . 
I 5 HOH 282 982  718  HOH HOH B . 
I 5 HOH 283 983  698  HOH HOH B . 
I 5 HOH 284 984  415  HOH HOH B . 
I 5 HOH 285 985  664  HOH HOH B . 
I 5 HOH 286 986  168  HOH HOH B . 
I 5 HOH 287 987  79   HOH HOH B . 
I 5 HOH 288 988  279  HOH HOH B . 
I 5 HOH 289 989  27   HOH HOH B . 
I 5 HOH 290 990  436  HOH HOH B . 
I 5 HOH 291 991  434  HOH HOH B . 
I 5 HOH 292 992  282  HOH HOH B . 
I 5 HOH 293 993  317  HOH HOH B . 
I 5 HOH 294 994  213  HOH HOH B . 
I 5 HOH 295 995  414  HOH HOH B . 
I 5 HOH 296 996  643  HOH HOH B . 
I 5 HOH 297 997  276  HOH HOH B . 
I 5 HOH 298 998  353  HOH HOH B . 
I 5 HOH 299 999  819  HOH HOH B . 
I 5 HOH 300 1000 430  HOH HOH B . 
I 5 HOH 301 1001 717  HOH HOH B . 
I 5 HOH 302 1002 90   HOH HOH B . 
I 5 HOH 303 1003 814  HOH HOH B . 
I 5 HOH 304 1004 2    HOH HOH B . 
I 5 HOH 305 1005 526  HOH HOH B . 
I 5 HOH 306 1006 64   HOH HOH B . 
I 5 HOH 307 1007 580  HOH HOH B . 
I 5 HOH 308 1008 564  HOH HOH B . 
I 5 HOH 309 1009 709  HOH HOH B . 
I 5 HOH 310 1010 747  HOH HOH B . 
I 5 HOH 311 1011 639  HOH HOH B . 
I 5 HOH 312 1012 591  HOH HOH B . 
I 5 HOH 313 1013 333  HOH HOH B . 
I 5 HOH 314 1014 603  HOH HOH B . 
I 5 HOH 315 1015 571  HOH HOH B . 
I 5 HOH 316 1016 350  HOH HOH B . 
I 5 HOH 317 1017 815  HOH HOH B . 
I 5 HOH 318 1018 124  HOH HOH B . 
I 5 HOH 319 1019 100  HOH HOH B . 
I 5 HOH 320 1020 96   HOH HOH B . 
I 5 HOH 321 1021 215  HOH HOH B . 
I 5 HOH 322 1022 720  HOH HOH B . 
I 5 HOH 323 1023 127  HOH HOH B . 
I 5 HOH 324 1024 786  HOH HOH B . 
I 5 HOH 325 1025 732  HOH HOH B . 
I 5 HOH 326 1026 118  HOH HOH B . 
I 5 HOH 327 1027 761  HOH HOH B . 
I 5 HOH 328 1028 856  HOH HOH B . 
I 5 HOH 329 1029 866  HOH HOH B . 
I 5 HOH 330 1030 690  HOH HOH B . 
I 5 HOH 331 1031 71   HOH HOH B . 
I 5 HOH 332 1032 573  HOH HOH B . 
I 5 HOH 333 1033 233  HOH HOH B . 
I 5 HOH 334 1034 237  HOH HOH B . 
I 5 HOH 335 1035 648  HOH HOH B . 
I 5 HOH 336 1036 22   HOH HOH B . 
I 5 HOH 337 1037 858  HOH HOH B . 
I 5 HOH 338 1038 764  HOH HOH B . 
I 5 HOH 339 1039 806  HOH HOH B . 
I 5 HOH 340 1040 239  HOH HOH B . 
I 5 HOH 341 1041 531  HOH HOH B . 
I 5 HOH 342 1042 193  HOH HOH B . 
I 5 HOH 343 1043 53   HOH HOH B . 
I 5 HOH 344 1044 496  HOH HOH B . 
I 5 HOH 345 1045 724  HOH HOH B . 
I 5 HOH 346 1046 599  HOH HOH B . 
I 5 HOH 347 1047 861  HOH HOH B . 
I 5 HOH 348 1048 874  HOH HOH B . 
I 5 HOH 349 1049 854  HOH HOH B . 
I 5 HOH 350 1050 94   HOH HOH B . 
I 5 HOH 351 1051 115  HOH HOH B . 
I 5 HOH 352 1052 790  HOH HOH B . 
I 5 HOH 353 1053 864  HOH HOH B . 
I 5 HOH 354 1054 163  HOH HOH B . 
I 5 HOH 355 1055 41   HOH HOH B . 
I 5 HOH 356 1056 881  HOH HOH B . 
I 5 HOH 357 1057 796  HOH HOH B . 
I 5 HOH 358 1058 515  HOH HOH B . 
I 5 HOH 359 1059 885  HOH HOH B . 
I 5 HOH 360 1060 592  HOH HOH B . 
I 5 HOH 361 1061 739  HOH HOH B . 
I 5 HOH 362 1062 711  HOH HOH B . 
I 5 HOH 363 1063 467  HOH HOH B . 
I 5 HOH 364 1064 752  HOH HOH B . 
I 5 HOH 365 1065 432  HOH HOH B . 
I 5 HOH 366 1066 738  HOH HOH B . 
I 5 HOH 367 1067 882  HOH HOH B . 
I 5 HOH 368 1068 708  HOH HOH B . 
I 5 HOH 369 1069 797  HOH HOH B . 
I 5 HOH 370 1070 742  HOH HOH B . 
I 5 HOH 371 1071 74   HOH HOH B . 
I 5 HOH 372 1072 857  HOH HOH B . 
I 5 HOH 373 1073 113  HOH HOH B . 
I 5 HOH 374 1074 835  HOH HOH B . 
I 5 HOH 375 1075 558  HOH HOH B . 
I 5 HOH 376 1076 653  HOH HOH B . 
I 5 HOH 377 1077 833  HOH HOH B . 
I 5 HOH 378 1078 231  HOH HOH B . 
I 5 HOH 379 1079 615  HOH HOH B . 
I 5 HOH 380 1080 116  HOH HOH B . 
I 5 HOH 381 1081 730  HOH HOH B . 
I 5 HOH 382 1082 837  HOH HOH B . 
I 5 HOH 383 1083 850  HOH HOH B . 
I 5 HOH 384 1084 870  HOH HOH B . 
I 5 HOH 385 1085 846  HOH HOH B . 
I 5 HOH 386 1086 557  HOH HOH B . 
I 5 HOH 387 1087 75   HOH HOH B . 
I 5 HOH 388 1088 549  HOH HOH B . 
I 5 HOH 389 1089 693  HOH HOH B . 
I 5 HOH 390 1090 137  HOH HOH B . 
I 5 HOH 391 1091 755  HOH HOH B . 
I 5 HOH 392 1092 852  HOH HOH B . 
I 5 HOH 393 1093 887  HOH HOH B . 
I 5 HOH 394 1094 468  HOH HOH B . 
I 5 HOH 395 1095 204  HOH HOH B . 
I 5 HOH 396 1096 808  HOH HOH B . 
I 5 HOH 397 1097 784  HOH HOH B . 
J 5 HOH 1   701  199  HOH HOH A . 
J 5 HOH 2   702  49   HOH HOH A . 
J 5 HOH 3   703  82   HOH HOH A . 
J 5 HOH 4   704  207  HOH HOH A . 
J 5 HOH 5   705  15   HOH HOH A . 
J 5 HOH 6   706  236  HOH HOH A . 
J 5 HOH 7   707  502  HOH HOH A . 
J 5 HOH 8   708  180  HOH HOH A . 
J 5 HOH 9   709  336  HOH HOH A . 
J 5 HOH 10  710  384  HOH HOH A . 
J 5 HOH 11  711  107  HOH HOH A . 
J 5 HOH 12  712  332  HOH HOH A . 
J 5 HOH 13  713  638  HOH HOH A . 
J 5 HOH 14  714  585  HOH HOH A . 
J 5 HOH 15  715  771  HOH HOH A . 
J 5 HOH 16  716  411  HOH HOH A . 
J 5 HOH 17  717  623  HOH HOH A . 
J 5 HOH 18  718  567  HOH HOH A . 
J 5 HOH 19  719  144  HOH HOH A . 
J 5 HOH 20  720  554  HOH HOH A . 
J 5 HOH 21  721  403  HOH HOH A . 
J 5 HOH 22  722  221  HOH HOH A . 
J 5 HOH 23  723  365  HOH HOH A . 
J 5 HOH 24  724  448  HOH HOH A . 
J 5 HOH 25  725  247  HOH HOH A . 
J 5 HOH 26  726  242  HOH HOH A . 
J 5 HOH 27  727  759  HOH HOH A . 
J 5 HOH 28  728  257  HOH HOH A . 
J 5 HOH 29  729  320  HOH HOH A . 
J 5 HOH 30  730  672  HOH HOH A . 
J 5 HOH 31  731  410  HOH HOH A . 
J 5 HOH 32  732  713  HOH HOH A . 
J 5 HOH 33  733  128  HOH HOH A . 
J 5 HOH 34  734  578  HOH HOH A . 
J 5 HOH 35  735  464  HOH HOH A . 
J 5 HOH 36  736  192  HOH HOH A . 
J 5 HOH 37  737  530  HOH HOH A . 
J 5 HOH 38  738  68   HOH HOH A . 
J 5 HOH 39  739  454  HOH HOH A . 
J 5 HOH 40  740  875  HOH HOH A . 
J 5 HOH 41  741  261  HOH HOH A . 
J 5 HOH 42  742  665  HOH HOH A . 
J 5 HOH 43  743  509  HOH HOH A . 
J 5 HOH 44  744  183  HOH HOH A . 
J 5 HOH 45  745  831  HOH HOH A . 
J 5 HOH 46  746  341  HOH HOH A . 
J 5 HOH 47  747  479  HOH HOH A . 
J 5 HOH 48  748  507  HOH HOH A . 
J 5 HOH 49  749  823  HOH HOH A . 
J 5 HOH 50  750  194  HOH HOH A . 
J 5 HOH 51  751  300  HOH HOH A . 
J 5 HOH 52  752  97   HOH HOH A . 
J 5 HOH 53  753  736  HOH HOH A . 
J 5 HOH 54  754  547  HOH HOH A . 
J 5 HOH 55  755  525  HOH HOH A . 
J 5 HOH 56  756  268  HOH HOH A . 
J 5 HOH 57  757  521  HOH HOH A . 
J 5 HOH 58  758  537  HOH HOH A . 
J 5 HOH 59  759  657  HOH HOH A . 
J 5 HOH 60  760  423  HOH HOH A . 
J 5 HOH 61  761  488  HOH HOH A . 
J 5 HOH 62  762  420  HOH HOH A . 
J 5 HOH 63  763  435  HOH HOH A . 
J 5 HOH 64  764  254  HOH HOH A . 
J 5 HOH 65  765  805  HOH HOH A . 
J 5 HOH 66  766  756  HOH HOH A . 
J 5 HOH 67  767  152  HOH HOH A . 
J 5 HOH 68  768  715  HOH HOH A . 
J 5 HOH 69  769  441  HOH HOH A . 
J 5 HOH 70  770  285  HOH HOH A . 
J 5 HOH 71  771  260  HOH HOH A . 
J 5 HOH 72  772  143  HOH HOH A . 
J 5 HOH 73  773  649  HOH HOH A . 
J 5 HOH 74  774  267  HOH HOH A . 
J 5 HOH 75  775  456  HOH HOH A . 
J 5 HOH 76  776  611  HOH HOH A . 
J 5 HOH 77  777  139  HOH HOH A . 
J 5 HOH 78  778  440  HOH HOH A . 
J 5 HOH 79  779  560  HOH HOH A . 
J 5 HOH 80  780  682  HOH HOH A . 
J 5 HOH 81  781  471  HOH HOH A . 
J 5 HOH 82  782  719  HOH HOH A . 
J 5 HOH 83  783  162  HOH HOH A . 
J 5 HOH 84  784  785  HOH HOH A . 
J 5 HOH 85  785  768  HOH HOH A . 
J 5 HOH 86  786  123  HOH HOH A . 
J 5 HOH 87  787  360  HOH HOH A . 
J 5 HOH 88  788  469  HOH HOH A . 
J 5 HOH 89  789  652  HOH HOH A . 
J 5 HOH 90  790  503  HOH HOH A . 
J 5 HOH 91  791  569  HOH HOH A . 
J 5 HOH 92  792  355  HOH HOH A . 
J 5 HOH 93  793  154  HOH HOH A . 
J 5 HOH 94  794  393  HOH HOH A . 
J 5 HOH 95  795  545  HOH HOH A . 
J 5 HOH 96  796  388  HOH HOH A . 
J 5 HOH 97  797  622  HOH HOH A . 
J 5 HOH 98  798  425  HOH HOH A . 
J 5 HOH 99  799  383  HOH HOH A . 
J 5 HOH 100 800  392  HOH HOH A . 
J 5 HOH 101 801  399  HOH HOH A . 
J 5 HOH 102 802  266  HOH HOH A . 
J 5 HOH 103 803  250  HOH HOH A . 
J 5 HOH 104 804  84   HOH HOH A . 
J 5 HOH 105 805  351  HOH HOH A . 
J 5 HOH 106 806  131  HOH HOH A . 
J 5 HOH 107 807  51   HOH HOH A . 
J 5 HOH 108 808  624  HOH HOH A . 
J 5 HOH 109 809  43   HOH HOH A . 
J 5 HOH 110 810  700  HOH HOH A . 
J 5 HOH 111 811  613  HOH HOH A . 
J 5 HOH 112 812  272  HOH HOH A . 
J 5 HOH 113 813  633  HOH HOH A . 
J 5 HOH 114 814  491  HOH HOH A . 
J 5 HOH 115 815  86   HOH HOH A . 
J 5 HOH 116 816  65   HOH HOH A . 
J 5 HOH 117 817  25   HOH HOH A . 
J 5 HOH 118 818  321  HOH HOH A . 
J 5 HOH 119 819  540  HOH HOH A . 
J 5 HOH 120 820  20   HOH HOH A . 
J 5 HOH 121 821  376  HOH HOH A . 
J 5 HOH 122 822  802  HOH HOH A . 
J 5 HOH 123 823  308  HOH HOH A . 
J 5 HOH 124 824  330  HOH HOH A . 
J 5 HOH 125 825  510  HOH HOH A . 
J 5 HOH 126 826  777  HOH HOH A . 
J 5 HOH 127 827  120  HOH HOH A . 
J 5 HOH 128 828  339  HOH HOH A . 
J 5 HOH 129 829  4    HOH HOH A . 
J 5 HOH 130 830  583  HOH HOH A . 
J 5 HOH 131 831  366  HOH HOH A . 
J 5 HOH 132 832  687  HOH HOH A . 
J 5 HOH 133 833  706  HOH HOH A . 
J 5 HOH 134 834  566  HOH HOH A . 
J 5 HOH 135 835  274  HOH HOH A . 
J 5 HOH 136 836  865  HOH HOH A . 
J 5 HOH 137 837  606  HOH HOH A . 
J 5 HOH 138 838  9    HOH HOH A . 
J 5 HOH 139 839  10   HOH HOH A . 
J 5 HOH 140 840  598  HOH HOH A . 
J 5 HOH 141 841  313  HOH HOH A . 
J 5 HOH 142 842  386  HOH HOH A . 
J 5 HOH 143 843  244  HOH HOH A . 
J 5 HOH 144 844  754  HOH HOH A . 
J 5 HOH 145 845  104  HOH HOH A . 
J 5 HOH 146 846  692  HOH HOH A . 
J 5 HOH 147 847  409  HOH HOH A . 
J 5 HOH 148 848  607  HOH HOH A . 
J 5 HOH 149 849  401  HOH HOH A . 
J 5 HOH 150 850  367  HOH HOH A . 
J 5 HOH 151 851  319  HOH HOH A . 
J 5 HOH 152 852  702  HOH HOH A . 
J 5 HOH 153 853  258  HOH HOH A . 
J 5 HOH 154 854  704  HOH HOH A . 
J 5 HOH 155 855  328  HOH HOH A . 
J 5 HOH 156 856  87   HOH HOH A . 
J 5 HOH 157 857  575  HOH HOH A . 
J 5 HOH 158 858  818  HOH HOH A . 
J 5 HOH 159 859  30   HOH HOH A . 
J 5 HOH 160 860  781  HOH HOH A . 
J 5 HOH 161 861  89   HOH HOH A . 
J 5 HOH 162 862  514  HOH HOH A . 
J 5 HOH 163 863  76   HOH HOH A . 
J 5 HOH 164 864  146  HOH HOH A . 
J 5 HOH 165 865  191  HOH HOH A . 
J 5 HOH 166 866  635  HOH HOH A . 
J 5 HOH 167 867  765  HOH HOH A . 
J 5 HOH 168 868  292  HOH HOH A . 
J 5 HOH 169 869  347  HOH HOH A . 
J 5 HOH 170 870  458  HOH HOH A . 
J 5 HOH 171 871  170  HOH HOH A . 
J 5 HOH 172 872  631  HOH HOH A . 
J 5 HOH 173 873  689  HOH HOH A . 
J 5 HOH 174 874  604  HOH HOH A . 
J 5 HOH 175 875  705  HOH HOH A . 
J 5 HOH 176 876  309  HOH HOH A . 
J 5 HOH 177 877  302  HOH HOH A . 
J 5 HOH 178 878  416  HOH HOH A . 
J 5 HOH 179 879  662  HOH HOH A . 
J 5 HOH 180 880  568  HOH HOH A . 
J 5 HOH 181 881  433  HOH HOH A . 
J 5 HOH 182 882  190  HOH HOH A . 
J 5 HOH 183 883  593  HOH HOH A . 
J 5 HOH 184 884  337  HOH HOH A . 
J 5 HOH 185 885  269  HOH HOH A . 
J 5 HOH 186 886  745  HOH HOH A . 
J 5 HOH 187 887  475  HOH HOH A . 
J 5 HOH 188 888  334  HOH HOH A . 
J 5 HOH 189 889  451  HOH HOH A . 
J 5 HOH 190 890  362  HOH HOH A . 
J 5 HOH 191 891  322  HOH HOH A . 
J 5 HOH 192 892  354  HOH HOH A . 
J 5 HOH 193 893  763  HOH HOH A . 
J 5 HOH 194 894  370  HOH HOH A . 
J 5 HOH 195 895  529  HOH HOH A . 
J 5 HOH 196 896  264  HOH HOH A . 
J 5 HOH 197 897  273  HOH HOH A . 
J 5 HOH 198 898  758  HOH HOH A . 
J 5 HOH 199 899  248  HOH HOH A . 
J 5 HOH 200 900  455  HOH HOH A . 
J 5 HOH 201 901  807  HOH HOH A . 
J 5 HOH 202 902  99   HOH HOH A . 
J 5 HOH 203 903  681  HOH HOH A . 
J 5 HOH 204 904  801  HOH HOH A . 
J 5 HOH 205 905  407  HOH HOH A . 
J 5 HOH 206 906  95   HOH HOH A . 
J 5 HOH 207 907  289  HOH HOH A . 
J 5 HOH 208 908  487  HOH HOH A . 
J 5 HOH 209 909  683  HOH HOH A . 
J 5 HOH 210 910  670  HOH HOH A . 
J 5 HOH 211 911  114  HOH HOH A . 
J 5 HOH 212 912  402  HOH HOH A . 
J 5 HOH 213 913  600  HOH HOH A . 
J 5 HOH 214 914  31   HOH HOH A . 
J 5 HOH 215 915  636  HOH HOH A . 
J 5 HOH 216 916  295  HOH HOH A . 
J 5 HOH 217 917  174  HOH HOH A . 
J 5 HOH 218 918  271  HOH HOH A . 
J 5 HOH 219 919  263  HOH HOH A . 
J 5 HOH 220 920  303  HOH HOH A . 
J 5 HOH 221 921  497  HOH HOH A . 
J 5 HOH 222 922  642  HOH HOH A . 
J 5 HOH 223 923  102  HOH HOH A . 
J 5 HOH 224 924  311  HOH HOH A . 
J 5 HOH 225 925  546  HOH HOH A . 
J 5 HOH 226 926  576  HOH HOH A . 
J 5 HOH 227 927  821  HOH HOH A . 
J 5 HOH 228 928  422  HOH HOH A . 
J 5 HOH 229 929  306  HOH HOH A . 
J 5 HOH 230 930  656  HOH HOH A . 
J 5 HOH 231 931  379  HOH HOH A . 
J 5 HOH 232 932  16   HOH HOH A . 
J 5 HOH 233 933  343  HOH HOH A . 
J 5 HOH 234 934  352  HOH HOH A . 
J 5 HOH 235 935  505  HOH HOH A . 
J 5 HOH 236 936  701  HOH HOH A . 
J 5 HOH 237 937  556  HOH HOH A . 
J 5 HOH 238 938  570  HOH HOH A . 
J 5 HOH 239 939  37   HOH HOH A . 
J 5 HOH 240 940  666  HOH HOH A . 
J 5 HOH 241 941  159  HOH HOH A . 
J 5 HOH 242 942  767  HOH HOH A . 
J 5 HOH 243 943  406  HOH HOH A . 
J 5 HOH 244 944  291  HOH HOH A . 
J 5 HOH 245 945  723  HOH HOH A . 
J 5 HOH 246 946  773  HOH HOH A . 
J 5 HOH 247 947  148  HOH HOH A . 
J 5 HOH 248 948  278  HOH HOH A . 
J 5 HOH 249 949  817  HOH HOH A . 
J 5 HOH 250 950  19   HOH HOH A . 
J 5 HOH 251 951  439  HOH HOH A . 
J 5 HOH 252 952  459  HOH HOH A . 
J 5 HOH 253 953  550  HOH HOH A . 
J 5 HOH 254 954  134  HOH HOH A . 
J 5 HOH 255 955  462  HOH HOH A . 
J 5 HOH 256 956  299  HOH HOH A . 
J 5 HOH 257 957  523  HOH HOH A . 
J 5 HOH 258 958  122  HOH HOH A . 
J 5 HOH 259 959  296  HOH HOH A . 
J 5 HOH 260 960  390  HOH HOH A . 
J 5 HOH 261 961  400  HOH HOH A . 
J 5 HOH 262 962  294  HOH HOH A . 
J 5 HOH 263 963  658  HOH HOH A . 
J 5 HOH 264 964  398  HOH HOH A . 
J 5 HOH 265 965  373  HOH HOH A . 
J 5 HOH 266 966  559  HOH HOH A . 
J 5 HOH 267 967  762  HOH HOH A . 
J 5 HOH 268 968  602  HOH HOH A . 
J 5 HOH 269 969  230  HOH HOH A . 
J 5 HOH 270 970  182  HOH HOH A . 
J 5 HOH 271 971  293  HOH HOH A . 
J 5 HOH 272 972  804  HOH HOH A . 
J 5 HOH 273 973  413  HOH HOH A . 
J 5 HOH 274 974  518  HOH HOH A . 
J 5 HOH 275 975  562  HOH HOH A . 
J 5 HOH 276 976  153  HOH HOH A . 
J 5 HOH 277 977  470  HOH HOH A . 
J 5 HOH 278 978  323  HOH HOH A . 
J 5 HOH 279 979  654  HOH HOH A . 
J 5 HOH 280 980  155  HOH HOH A . 
J 5 HOH 281 981  513  HOH HOH A . 
J 5 HOH 282 982  368  HOH HOH A . 
J 5 HOH 283 983  348  HOH HOH A . 
J 5 HOH 284 984  132  HOH HOH A . 
J 5 HOH 285 985  209  HOH HOH A . 
J 5 HOH 286 986  358  HOH HOH A . 
J 5 HOH 287 987  478  HOH HOH A . 
J 5 HOH 288 988  548  HOH HOH A . 
J 5 HOH 289 989  520  HOH HOH A . 
J 5 HOH 290 990  474  HOH HOH A . 
J 5 HOH 291 991  280  HOH HOH A . 
J 5 HOH 292 992  375  HOH HOH A . 
J 5 HOH 293 993  316  HOH HOH A . 
J 5 HOH 294 994  356  HOH HOH A . 
J 5 HOH 295 995  519  HOH HOH A . 
J 5 HOH 296 996  374  HOH HOH A . 
J 5 HOH 297 997  760  HOH HOH A . 
J 5 HOH 298 998  160  HOH HOH A . 
J 5 HOH 299 999  171  HOH HOH A . 
J 5 HOH 300 1000 820  HOH HOH A . 
J 5 HOH 301 1001 676  HOH HOH A . 
J 5 HOH 302 1002 696  HOH HOH A . 
J 5 HOH 303 1003 421  HOH HOH A . 
J 5 HOH 304 1004 21   HOH HOH A . 
J 5 HOH 305 1005 811  HOH HOH A . 
J 5 HOH 306 1006 584  HOH HOH A . 
J 5 HOH 307 1007 372  HOH HOH A . 
J 5 HOH 308 1008 563  HOH HOH A . 
J 5 HOH 309 1009 473  HOH HOH A . 
J 5 HOH 310 1010 508  HOH HOH A . 
J 5 HOH 311 1011 640  HOH HOH A . 
J 5 HOH 312 1012 176  HOH HOH A . 
J 5 HOH 313 1013 389  HOH HOH A . 
J 5 HOH 314 1014 28   HOH HOH A . 
J 5 HOH 315 1015 778  HOH HOH A . 
J 5 HOH 316 1016 301  HOH HOH A . 
J 5 HOH 317 1017 750  HOH HOH A . 
J 5 HOH 318 1018 270  HOH HOH A . 
J 5 HOH 319 1019 165  HOH HOH A . 
J 5 HOH 320 1020 481  HOH HOH A . 
J 5 HOH 321 1021 329  HOH HOH A . 
J 5 HOH 322 1022 712  HOH HOH A . 
J 5 HOH 323 1023 522  HOH HOH A . 
J 5 HOH 324 1024 426  HOH HOH A . 
J 5 HOH 325 1025 741  HOH HOH A . 
J 5 HOH 326 1026 617  HOH HOH A . 
J 5 HOH 327 1027 483  HOH HOH A . 
J 5 HOH 328 1028 7    HOH HOH A . 
J 5 HOH 329 1029 463  HOH HOH A . 
J 5 HOH 330 1030 795  HOH HOH A . 
J 5 HOH 331 1031 581  HOH HOH A . 
J 5 HOH 332 1032 661  HOH HOH A . 
J 5 HOH 333 1033 417  HOH HOH A . 
J 5 HOH 334 1034 178  HOH HOH A . 
J 5 HOH 335 1035 485  HOH HOH A . 
J 5 HOH 336 1036 616  HOH HOH A . 
J 5 HOH 337 1037 596  HOH HOH A . 
J 5 HOH 338 1038 195  HOH HOH A . 
J 5 HOH 339 1039 668  HOH HOH A . 
J 5 HOH 340 1040 359  HOH HOH A . 
J 5 HOH 341 1041 490  HOH HOH A . 
J 5 HOH 342 1042 371  HOH HOH A . 
J 5 HOH 343 1043 589  HOH HOH A . 
J 5 HOH 344 1044 729  HOH HOH A . 
J 5 HOH 345 1045 54   HOH HOH A . 
J 5 HOH 346 1046 641  HOH HOH A . 
J 5 HOH 347 1047 281  HOH HOH A . 
J 5 HOH 348 1048 396  HOH HOH A . 
J 5 HOH 349 1049 674  HOH HOH A . 
J 5 HOH 350 1050 38   HOH HOH A . 
J 5 HOH 351 1051 77   HOH HOH A . 
J 5 HOH 352 1052 157  HOH HOH A . 
J 5 HOH 353 1053 130  HOH HOH A . 
J 5 HOH 354 1054 770  HOH HOH A . 
J 5 HOH 355 1055 34   HOH HOH A . 
J 5 HOH 356 1056 574  HOH HOH A . 
J 5 HOH 357 1057 110  HOH HOH A . 
J 5 HOH 358 1058 129  HOH HOH A . 
J 5 HOH 359 1059 630  HOH HOH A . 
J 5 HOH 360 1060 774  HOH HOH A . 
J 5 HOH 361 1061 201  HOH HOH A . 
J 5 HOH 362 1062 699  HOH HOH A . 
J 5 HOH 363 1063 57   HOH HOH A . 
J 5 HOH 364 1064 586  HOH HOH A . 
J 5 HOH 365 1065 627  HOH HOH A . 
J 5 HOH 366 1066 561  HOH HOH A . 
J 5 HOH 367 1067 229  HOH HOH A . 
J 5 HOH 368 1068 619  HOH HOH A . 
J 5 HOH 369 1069 871  HOH HOH A . 
J 5 HOH 370 1070 794  HOH HOH A . 
J 5 HOH 371 1071 740  HOH HOH A . 
J 5 HOH 372 1072 775  HOH HOH A . 
J 5 HOH 373 1073 848  HOH HOH A . 
J 5 HOH 374 1074 722  HOH HOH A . 
J 5 HOH 375 1075 67   HOH HOH A . 
J 5 HOH 376 1076 189  HOH HOH A . 
J 5 HOH 377 1077 851  HOH HOH A . 
J 5 HOH 378 1078 166  HOH HOH A . 
J 5 HOH 379 1079 884  HOH HOH A . 
J 5 HOH 380 1080 228  HOH HOH A . 
J 5 HOH 381 1081 119  HOH HOH A . 
J 5 HOH 382 1082 494  HOH HOH A . 
J 5 HOH 383 1083 886  HOH HOH A . 
J 5 HOH 384 1084 108  HOH HOH A . 
J 5 HOH 385 1085 880  HOH HOH A . 
J 5 HOH 386 1086 489  HOH HOH A . 
J 5 HOH 387 1087 387  HOH HOH A . 
J 5 HOH 388 1088 637  HOH HOH A . 
J 5 HOH 389 1089 826  HOH HOH A . 
J 5 HOH 390 1090 565  HOH HOH A . 
J 5 HOH 391 1091 240  HOH HOH A . 
J 5 HOH 392 1092 844  HOH HOH A . 
J 5 HOH 393 1093 855  HOH HOH A . 
J 5 HOH 394 1094 17   HOH HOH A . 
J 5 HOH 395 1095 331  HOH HOH A . 
J 5 HOH 396 1096 863  HOH HOH A . 
J 5 HOH 397 1097 829  HOH HOH A . 
J 5 HOH 398 1098 138  HOH HOH A . 
J 5 HOH 399 1099 609  HOH HOH A . 
J 5 HOH 400 1100 714  HOH HOH A . 
J 5 HOH 401 1101 443  HOH HOH A . 
J 5 HOH 402 1102 860  HOH HOH A . 
J 5 HOH 403 1103 179  HOH HOH A . 
J 5 HOH 404 1104 832  HOH HOH A . 
J 5 HOH 405 1105 173  HOH HOH A . 
J 5 HOH 406 1106 58   HOH HOH A . 
J 5 HOH 407 1107 40   HOH HOH A . 
J 5 HOH 408 1108 746  HOH HOH A . 
J 5 HOH 409 1109 62   HOH HOH A . 
J 5 HOH 410 1110 877  HOH HOH A . 
J 5 HOH 411 1111 849  HOH HOH A . 
J 5 HOH 412 1112 867  HOH HOH A . 
J 5 HOH 413 1113 787  HOH HOH A . 
J 5 HOH 414 1114 650  HOH HOH A . 
J 5 HOH 415 1115 827  HOH HOH A . 
J 5 HOH 416 1116 91   HOH HOH A . 
J 5 HOH 417 1117 111  HOH HOH A . 
J 5 HOH 418 1118 678  HOH HOH A . 
J 5 HOH 419 1119 847  HOH HOH A . 
J 5 HOH 420 1120 836  HOH HOH A . 
J 5 HOH 421 1121 869  HOH HOH A . 
J 5 HOH 422 1122 675  HOH HOH A . 
J 5 HOH 423 1123 555  HOH HOH A . 
J 5 HOH 424 1124 792  HOH HOH A . 
J 5 HOH 425 1125 172  HOH HOH A . 
J 5 HOH 426 1126 14   HOH HOH A . 
J 5 HOH 427 1127 444  HOH HOH A . 
J 5 HOH 428 1128 651  HOH HOH A . 
J 5 HOH 429 1129 52   HOH HOH A . 
J 5 HOH 430 1130 647  HOH HOH A . 
J 5 HOH 431 1131 680  HOH HOH A . 
J 5 HOH 432 1132 753  HOH HOH A . 
J 5 HOH 433 1133 101  HOH HOH A . 
J 5 HOH 434 1134 484  HOH HOH A . 
J 5 HOH 435 1135 48   HOH HOH A . 
J 5 HOH 436 1136 716  HOH HOH A . 
J 5 HOH 437 1137 834  HOH HOH A . 
J 5 HOH 438 1138 816  HOH HOH A . 
J 5 HOH 439 1139 66   HOH HOH A . 
J 5 HOH 440 1140 541  HOH HOH A . 
J 5 HOH 441 1141 465  HOH HOH A . 
J 5 HOH 442 1142 868  HOH HOH A . 
J 5 HOH 443 1143 883  HOH HOH A . 
J 5 HOH 444 1144 544  HOH HOH A . 
J 5 HOH 445 1145 60   HOH HOH A . 
J 5 HOH 446 1146 872  HOH HOH A . 
J 5 HOH 447 1147 840  HOH HOH A . 
J 5 HOH 448 1148 188  HOH HOH A . 
J 5 HOH 449 1149 394  HOH HOH A . 
J 5 HOH 450 1150 772  HOH HOH A . 
J 5 HOH 451 1151 112  HOH HOH A . 
J 5 HOH 452 1152 449  HOH HOH A . 
J 5 HOH 453 1153 385  HOH HOH A . 
J 5 HOH 454 1154 862  HOH HOH A . 
J 5 HOH 455 1155 695  HOH HOH A . 
# 
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 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8R1E 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.892 
_cell.length_a_esd                 ? 
_cell.length_b                     64.756 
_cell.length_b_esd                 ? 
_cell.length_c                     287.954 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8R1E 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8R1E 
_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             2.26 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.69 
_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              7.0 
_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    '25% (w/v) PEG 1500 ; 0.1 M PCB (pH 7.0)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-23 
_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   0.9537 
_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' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9537 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8R1E 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.62 
_reflns.d_resolution_low                               71.99 
_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                                     147729 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.76 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.7 
_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                                0.150 
_reflns.pdbx_Rpim_I_all                                0.042 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.144 
_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                                    1.62 
_reflns_shell.d_res_low                                     1.65 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6871 
_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                               6.0 
_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                               2.884 
_reflns_shell.pdbx_Rpim_I_all                               1.143 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.310 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          94.93 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.632 
_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]                            -1.14 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            3.51 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -2.37 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               28.605 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.972 
_refine.correlation_coeff_Fo_to_Fc_free          0.961 
_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                                 8R1E 
_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                            1.62 
_refine.ls_d_res_low                             71.99 
_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                     144075 
_refine.ls_number_reflns_R_free                  2005 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.64 
_refine.ls_percent_reflns_R_free                 1.4 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19181 
_refine.ls_R_factor_R_free                       0.22358 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19135 
_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                      8PNG 
_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                       0.097 
_refine.pdbx_overall_ESU_R_Free                  0.096 
_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                             4.680 
_refine.overall_SU_ML                            0.130 
_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                       1.62 
_refine_hist.d_res_low                        71.99 
_refine_hist.number_atoms_solvent             852 
_refine_hist.number_atoms_total               9916 
_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        8930 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         134 
_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' ? 0.008  0.013  9261  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.015  8728  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.479  1.637  12560 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.416  1.574  20076 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.935  5.000  1183  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 32.176 22.096 439   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.777 15.000 1470  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 18.792 15.000 56    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.075  0.200  1198  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  10585 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  2081  ? 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' ? 1.892  2.832  4738  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.892  2.832  4737  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.551  4.240  5919  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.551  4.240  5920  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.928  3.153  4523  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.928  3.154  4524  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.414  4.600  6642  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.494  34.721 11047 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.424  34.319 10813 ? 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                       1.620 
_refine_ls_shell.d_res_low                        1.662 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             117 
_refine_ls_shell.number_reflns_R_work             8950 
_refine_ls_shell.percent_reflns_obs               83.90 
_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                  0.499 
_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                  0.503 
# 
_struct.entry_id                     8R1E 
_struct.title                        
'crystal structure of acyl-CoA dehydrogenase FadE2 mutant (PA0508 M130G E296A Q303A) from Pseudomonas aeruginosa' 
_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        8R1E 
_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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9I610_PSEAE 
_struct_ref.pdbx_db_accession          Q9I610 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MADYKAPLRDMRFVLNEVFEVSRLWAQLPALAEVVDAETAAAILEEAGKVTAGTIAPLNRPGDEEGCQWNAGAVSTPAGF
PEAYRTYAEGGWVGVGGDPAYGGMGMPKVISAQVEELVNSANLSFGLYPMLTAGACLALNAHASDELKDKYLPNMYAGIW
AGSMCLTEPHAGTDLGIIRTRAEPQADGSYKISGTKIFITGGEHDLTENIIHLVLAKLPDAPAGPKGISLFLVPKVLVNA
DGSLGEKNSLGCGSIEHKMGIKASATCVMNFDGATGWLVGEVNKGLAAMFTMMNYERLGVGIQGLATGERSYQSAIEYAR
ERIQSRAPTGPVAKDKAADPIIVHPDVRRMLLTMKALNEGGRAFSSYVAMQLDTAKYSEDAVTRKRAEELVALLTPVAKA
FLTDMGLETTIHGQQIFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALDLVGRKVIGSGGAFSRHFTDEIKAFVASAD
EALGEFSKPLAAAVENLEELTAWLLDRAKGNPNEIGAASVEYLHVFGYTAYAYMWALMARTALAKQGEDDFYASKLGTAR
FYFARLLPRIHSLSASVRAGSESLYLLDAEQF
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8R1E B 3 ? 594 ? Q9I610 1 ? 592 ? 1 592 
2 1 8R1E A 3 ? 594 ? Q9I610 1 ? 592 ? 1 592 
# 
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 8R1E GLY B 1   ? UNP Q9I610 ?   ?   'expression tag'      -1  1  
1 8R1E HIS B 2   ? UNP Q9I610 ?   ?   'expression tag'      0   2  
1 8R1E GLY B 132 ? UNP Q9I610 MET 130 'engineered mutation' 130 3  
1 8R1E ALA B 298 ? UNP Q9I610 GLU 296 'engineered mutation' 296 4  
1 8R1E ALA B 305 ? UNP Q9I610 GLN 303 'engineered mutation' 303 5  
2 8R1E GLY A 1   ? UNP Q9I610 ?   ?   'expression tag'      -1  6  
2 8R1E HIS A 2   ? UNP Q9I610 ?   ?   'expression tag'      0   7  
2 8R1E GLY A 132 ? UNP Q9I610 MET 130 'engineered mutation' 130 8  
2 8R1E ALA A 298 ? UNP Q9I610 GLU 296 'engineered mutation' 296 9  
2 8R1E ALA A 305 ? UNP Q9I610 GLN 303 'engineered mutation' 303 10 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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)' 12230 ? 
1 MORE         -60   ? 
1 'SSA (A^2)'  38630 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 GLU A 22  ? GLN A 29  ? GLU B 20  GLN B 27  1 ? 8  
HELX_P HELX_P3  AA3 LEU A 30  ? GLU A 35  ? LEU B 28  GLU B 33  1 ? 6  
HELX_P HELX_P4  AA4 ASP A 38  ? THR A 56  ? ASP B 36  THR B 54  1 ? 19 
HELX_P HELX_P5  AA5 ILE A 57  ? PRO A 59  ? ILE B 55  PRO B 57  5 ? 3  
HELX_P HELX_P6  AA6 LEU A 60  ? GLY A 68  ? LEU B 58  GLY B 66  1 ? 9  
HELX_P HELX_P7  AA7 GLY A 81  ? GLY A 92  ? GLY B 79  GLY B 90  1 ? 12 
HELX_P HELX_P8  AA8 GLY A 93  ? VAL A 97  ? GLY B 91  VAL B 95  5 ? 5  
HELX_P HELX_P9  AA9 ASP A 100 ? GLY A 104 ? ASP B 98  GLY B 102 5 ? 5  
HELX_P HELX_P10 AB1 PRO A 109 ? ASN A 124 ? PRO B 107 ASN B 122 1 ? 16 
HELX_P HELX_P11 AB2 ASN A 124 ? ALA A 145 ? ASN B 122 ALA B 143 1 ? 22 
HELX_P HELX_P12 AB3 SER A 146 ? ALA A 159 ? SER B 144 ALA B 157 1 ? 14 
HELX_P HELX_P13 AB4 ASP A 176 ? ILE A 180 ? ASP B 174 ILE B 178 5 ? 5  
HELX_P HELX_P14 AB5 ALA A 225 ? ILE A 230 ? ALA B 223 ILE B 228 5 ? 6  
HELX_P HELX_P15 AB6 LEU A 288 ? ALA A 290 ? LEU B 286 ALA B 288 5 ? 3  
HELX_P HELX_P16 AB7 MET A 291 ? ARG A 324 ? MET B 289 ARG B 322 1 ? 34 
HELX_P HELX_P17 AB8 PRO A 342 ? VAL A 345 ? PRO B 340 VAL B 343 5 ? 4  
HELX_P HELX_P18 AB9 HIS A 346 ? SER A 380 ? HIS B 344 SER B 378 1 ? 35 
HELX_P HELX_P19 AC1 ASP A 382 ? PHE A 419 ? ASP B 380 PHE B 417 1 ? 38 
HELX_P HELX_P20 AC2 GLY A 420 ? TRP A 428 ? GLY B 418 TRP B 426 5 ? 9  
HELX_P HELX_P21 AC3 GLY A 429 ? GLN A 441 ? GLY B 427 GLN B 439 1 ? 13 
HELX_P HELX_P22 AC4 THR A 446 ? ARG A 457 ? THR B 444 ARG B 455 1 ? 12 
HELX_P HELX_P23 AC5 VAL A 459 ? GLY A 463 ? VAL B 457 GLY B 461 5 ? 5  
HELX_P HELX_P24 AC6 GLY A 464 ? ALA A 481 ? GLY B 462 ALA B 479 1 ? 18 
HELX_P HELX_P25 AC7 LEU A 485 ? LYS A 511 ? LEU B 483 LYS B 509 1 ? 27 
HELX_P HELX_P26 AC8 PRO A 514 ? GLN A 548 ? PRO B 512 GLN B 546 1 ? 35 
HELX_P HELX_P27 AC9 ASP A 552 ? LEU A 568 ? ASP B 550 LEU B 566 1 ? 17 
HELX_P HELX_P28 AD1 ARG A 571 ? ALA A 581 ? ARG B 569 ALA B 579 1 ? 11 
HELX_P HELX_P29 AD2 GLY A 582 ? LEU A 588 ? GLY B 580 LEU B 586 5 ? 7  
HELX_P HELX_P30 AD3 ASP A 590 ? PHE A 594 ? ASP B 588 PHE B 592 5 ? 5  
HELX_P HELX_P31 AD4 PRO B 9   ? GLU B 19  ? PRO A 7   GLU A 17  1 ? 11 
HELX_P HELX_P32 AD5 GLU B 22  ? LEU B 30  ? GLU A 20  LEU A 28  1 ? 9  
HELX_P HELX_P33 AD6 LEU B 30  ? GLU B 35  ? LEU A 28  GLU A 33  1 ? 6  
HELX_P HELX_P34 AD7 ASP B 38  ? THR B 56  ? ASP A 36  THR A 54  1 ? 19 
HELX_P HELX_P35 AD8 ILE B 57  ? PRO B 59  ? ILE A 55  PRO A 57  5 ? 3  
HELX_P HELX_P36 AD9 LEU B 60  ? GLY B 68  ? LEU A 58  GLY A 66  1 ? 9  
HELX_P HELX_P37 AE1 GLY B 81  ? GLY B 92  ? GLY A 79  GLY A 90  1 ? 12 
HELX_P HELX_P38 AE2 GLY B 93  ? VAL B 97  ? GLY A 91  VAL A 95  5 ? 5  
HELX_P HELX_P39 AE3 ASP B 100 ? GLY B 104 ? ASP A 98  GLY A 102 5 ? 5  
HELX_P HELX_P40 AE4 PRO B 109 ? ASN B 124 ? PRO A 107 ASN A 122 1 ? 16 
HELX_P HELX_P41 AE5 ASN B 124 ? ALA B 145 ? ASN A 122 ALA A 143 1 ? 22 
HELX_P HELX_P42 AE6 SER B 146 ? ALA B 159 ? SER A 144 ALA A 157 1 ? 14 
HELX_P HELX_P43 AE7 ASP B 176 ? ILE B 180 ? ASP A 174 ILE A 178 5 ? 5  
HELX_P HELX_P44 AE8 GLY B 226 ? ILE B 230 ? GLY A 224 ILE A 228 5 ? 5  
HELX_P HELX_P45 AE9 LEU B 288 ? ALA B 290 ? LEU A 286 ALA A 288 5 ? 3  
HELX_P HELX_P46 AF1 MET B 291 ? ARG B 324 ? MET A 289 ARG A 322 1 ? 34 
HELX_P HELX_P47 AF2 PRO B 342 ? VAL B 345 ? PRO A 340 VAL A 343 5 ? 4  
HELX_P HELX_P48 AF3 HIS B 346 ? SER B 380 ? HIS A 344 SER A 378 1 ? 35 
HELX_P HELX_P49 AF4 ASP B 382 ? PHE B 419 ? ASP A 380 PHE A 417 1 ? 38 
HELX_P HELX_P50 AF5 GLY B 420 ? TRP B 428 ? GLY A 418 TRP A 426 5 ? 9  
HELX_P HELX_P51 AF6 GLY B 429 ? GLN B 441 ? GLY A 427 GLN A 439 1 ? 13 
HELX_P HELX_P52 AF7 THR B 446 ? ARG B 457 ? THR A 444 ARG A 455 1 ? 12 
HELX_P HELX_P53 AF8 VAL B 459 ? GLY B 463 ? VAL A 457 GLY A 461 5 ? 5  
HELX_P HELX_P54 AF9 GLY B 464 ? ALA B 481 ? GLY A 462 ALA A 479 1 ? 18 
HELX_P HELX_P55 AG1 LEU B 485 ? LYS B 511 ? LEU A 483 LYS A 509 1 ? 27 
HELX_P HELX_P56 AG2 PRO B 514 ? GLN B 548 ? PRO A 512 GLN A 546 1 ? 35 
HELX_P HELX_P57 AG3 ASP B 551 ? LEU B 568 ? ASP A 549 LEU A 566 1 ? 18 
HELX_P HELX_P58 AG4 ARG B 571 ? ALA B 581 ? ARG A 569 ALA A 579 1 ? 11 
HELX_P HELX_P59 AG5 GLY B 582 ? TYR B 587 ? GLY A 580 TYR A 585 5 ? 6  
HELX_P HELX_P60 AG6 ASP B 590 ? PHE B 594 ? ASP A 588 PHE A 592 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 ? 
AA5 ? 2 ? 
AA6 ? 6 ? 
AA7 ? 5 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-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 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN A 70  ? ASN A 72  ? GLN B 68  ASN B 70  
AA1 2 ALA A 75  ? SER A 77  ? ALA B 73  SER B 75  
AA2 1 TRP A 162 ? CYS A 167 ? TRP B 160 CYS B 165 
AA2 2 ASN A 211 ? ALA A 218 ? ASN B 209 ALA B 216 
AA2 3 SER A 231 ? PRO A 236 ? SER B 229 PRO B 234 
AA2 4 THR A 268 ? VAL A 281 ? THR B 266 VAL B 279 
AA2 5 TYR A 192 ? THR A 202 ? TYR B 190 THR B 200 
AA2 6 ARG A 183 ? PRO A 186 ? ARG B 181 PRO B 184 
AA3 1 TRP A 162 ? CYS A 167 ? TRP B 160 CYS B 165 
AA3 2 ASN A 211 ? ALA A 218 ? ASN B 209 ALA B 216 
AA3 3 SER A 231 ? PRO A 236 ? SER B 229 PRO B 234 
AA3 4 THR A 268 ? VAL A 281 ? THR B 266 VAL B 279 
AA3 5 LEU A 252 ? ILE A 257 ? LEU B 250 ILE B 255 
AA4 1 VAL A 238 ? VAL A 240 ? VAL B 236 VAL B 238 
AA4 2 LEU A 246 ? LYS A 249 ? LEU B 244 LYS B 247 
AA5 1 GLN B 70  ? ASN B 72  ? GLN A 68  ASN A 70  
AA5 2 ALA B 75  ? SER B 77  ? ALA A 73  SER A 75  
AA6 1 TRP B 162 ? CYS B 167 ? TRP A 160 CYS A 165 
AA6 2 ASN B 211 ? ALA B 218 ? ASN A 209 ALA A 216 
AA6 3 SER B 231 ? PRO B 236 ? SER A 229 PRO A 234 
AA6 4 THR B 268 ? VAL B 281 ? THR A 266 VAL A 279 
AA6 5 TYR B 192 ? THR B 202 ? TYR A 190 THR A 200 
AA6 6 ARG B 183 ? PRO B 186 ? ARG A 181 PRO A 184 
AA7 1 TRP B 162 ? CYS B 167 ? TRP A 160 CYS A 165 
AA7 2 ASN B 211 ? ALA B 218 ? ASN A 209 ALA A 216 
AA7 3 SER B 231 ? PRO B 236 ? SER A 229 PRO A 234 
AA7 4 THR B 268 ? VAL B 281 ? THR A 266 VAL A 279 
AA7 5 LEU B 252 ? ILE B 257 ? LEU A 250 ILE A 255 
AA8 1 VAL B 238 ? VAL B 240 ? VAL A 236 VAL A 238 
AA8 2 LEU B 246 ? LYS B 249 ? LEU A 244 LYS A 247 
# 
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 ASN A 72  ? N ASN B 70  O ALA A 75  ? O ALA B 73  
AA2 1 2 N CYS A 167 ? N CYS B 165 O LEU A 215 ? O LEU B 213 
AA2 2 3 N ALA A 218 ? N ALA B 216 O SER A 231 ? O SER B 229 
AA2 3 4 N LEU A 234 ? N LEU B 232 O TRP A 279 ? O TRP B 277 
AA2 4 5 O ALA A 276 ? O ALA B 274 N ILE A 194 ? N ILE B 192 
AA2 5 6 O LYS A 193 ? O LYS B 191 N GLU A 185 ? N GLU B 183 
AA3 1 2 N CYS A 167 ? N CYS B 165 O LEU A 215 ? O LEU B 213 
AA3 2 3 N ALA A 218 ? N ALA B 216 O SER A 231 ? O SER B 229 
AA3 3 4 N LEU A 234 ? N LEU B 232 O TRP A 279 ? O TRP B 277 
AA3 4 5 O ASN A 272 ? O ASN B 270 N GLY A 253 ? N GLY B 251 
AA4 1 2 N LEU A 239 ? N LEU B 237 O GLY A 247 ? O GLY B 245 
AA5 1 2 N ASN B 72  ? N ASN A 70  O ALA B 75  ? O ALA A 73  
AA6 1 2 N CYS B 167 ? N CYS A 165 O LEU B 215 ? O LEU A 213 
AA6 2 3 N HIS B 214 ? N HIS A 212 O VAL B 235 ? O VAL A 233 
AA6 3 4 N LEU B 232 ? N LEU A 230 O VAL B 281 ? O VAL A 279 
AA6 4 5 O ALA B 276 ? O ALA A 274 N ILE B 194 ? N ILE A 192 
AA6 5 6 O LYS B 193 ? O LYS A 191 N GLU B 185 ? N GLU A 183 
AA7 1 2 N CYS B 167 ? N CYS A 165 O LEU B 215 ? O LEU A 213 
AA7 2 3 N HIS B 214 ? N HIS A 212 O VAL B 235 ? O VAL A 233 
AA7 3 4 N LEU B 232 ? N LEU A 230 O VAL B 281 ? O VAL A 279 
AA7 4 5 O ASN B 272 ? O ASN A 270 N GLY B 253 ? N GLY A 251 
AA8 1 2 N LEU B 239 ? N LEU A 237 O GLY B 247 ? O GLY A 245 
# 
_pdbx_entry_details.entry_id                   8R1E 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   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 ASN B 122 ? ? -168.65 94.44   
2  1 HIS B 204 ? ? -171.43 -178.37 
3  1 ILE B 261 ? ? 24.88   59.29   
4  1 SER B 325 ? ? 64.87   -170.31 
5  1 VAL B 457 ? ? -97.53  -71.61  
6  1 ASN A 122 ? ? -173.72 92.60   
7  1 HIS A 204 ? ? -170.51 -177.49 
8  1 ILE A 261 ? ? 28.57   57.29   
9  1 SER A 325 ? ? 65.02   -167.75 
10 1 ALA A 333 ? ? -106.97 74.38   
11 1 VAL A 457 ? ? -102.56 -71.93  
12 1 ASP A 549 ? ? 175.67  136.79  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY -1 ? B GLY 1 
2 1 Y 1 A HIS 0  ? B HIS 2 
3 1 Y 1 A MET 1  ? B MET 3 
# 
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  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
GLN N      N N N 174 
GLN CA     C N S 175 
GLN C      C N N 176 
GLN O      O N N 177 
GLN CB     C N N 178 
GLN CG     C N N 179 
GLN CD     C N N 180 
GLN OE1    O N N 181 
GLN NE2    N N N 182 
GLN OXT    O N N 183 
GLN H      H N N 184 
GLN H2     H N N 185 
GLN HA     H N N 186 
GLN HB2    H N N 187 
GLN HB3    H N N 188 
GLN HG2    H N N 189 
GLN HG3    H N N 190 
GLN HE21   H N N 191 
GLN HE22   H N N 192 
GLN HXT    H N N 193 
GLU N      N N N 194 
GLU CA     C N S 195 
GLU C      C N N 196 
GLU O      O N N 197 
GLU CB     C N N 198 
GLU CG     C N N 199 
GLU CD     C N N 200 
GLU OE1    O N N 201 
GLU OE2    O N N 202 
GLU OXT    O N N 203 
GLU H      H N N 204 
GLU H2     H N N 205 
GLU HA     H N N 206 
GLU HB2    H N N 207 
GLU HB3    H N N 208 
GLU HG2    H N N 209 
GLU HG3    H N N 210 
GLU HE2    H N N 211 
GLU HXT    H N N 212 
GLY N      N N N 213 
GLY CA     C N N 214 
GLY C      C N N 215 
GLY O      O N N 216 
GLY OXT    O N N 217 
GLY H      H N N 218 
GLY H2     H N N 219 
GLY HA2    H N N 220 
GLY HA3    H N N 221 
GLY HXT    H N N 222 
GOL C1     C N N 223 
GOL O1     O N N 224 
GOL C2     C N N 225 
GOL O2     O N N 226 
GOL C3     C N N 227 
GOL O3     O N N 228 
GOL H11    H N N 229 
GOL H12    H N N 230 
GOL HO1    H N N 231 
GOL H2     H N N 232 
GOL HO2    H N N 233 
GOL H31    H N N 234 
GOL H32    H N N 235 
GOL HO3    H N N 236 
HIS N      N N N 237 
HIS CA     C N S 238 
HIS C      C N N 239 
HIS O      O N N 240 
HIS CB     C N N 241 
HIS CG     C Y N 242 
HIS ND1    N Y N 243 
HIS CD2    C Y N 244 
HIS CE1    C Y N 245 
HIS NE2    N Y N 246 
HIS OXT    O N N 247 
HIS H      H N N 248 
HIS H2     H N N 249 
HIS HA     H N N 250 
HIS HB2    H N N 251 
HIS HB3    H N N 252 
HIS HD1    H N N 253 
HIS HD2    H N N 254 
HIS HE1    H N N 255 
HIS HE2    H N N 256 
HIS HXT    H N N 257 
HOH O      O N N 258 
HOH H1     H N N 259 
HOH H2     H N N 260 
ILE N      N N N 261 
ILE CA     C N S 262 
ILE C      C N N 263 
ILE O      O N N 264 
ILE CB     C N S 265 
ILE CG1    C N N 266 
ILE CG2    C N N 267 
ILE CD1    C N N 268 
ILE OXT    O N N 269 
ILE H      H N N 270 
ILE H2     H N N 271 
ILE HA     H N N 272 
ILE HB     H N N 273 
ILE HG12   H N N 274 
ILE HG13   H N N 275 
ILE HG21   H N N 276 
ILE HG22   H N N 277 
ILE HG23   H N N 278 
ILE HD11   H N N 279 
ILE HD12   H N N 280 
ILE HD13   H N N 281 
ILE HXT    H N N 282 
LEU N      N N N 283 
LEU CA     C N S 284 
LEU C      C N N 285 
LEU O      O N N 286 
LEU CB     C N N 287 
LEU CG     C N N 288 
LEU CD1    C N N 289 
LEU CD2    C N N 290 
LEU OXT    O N N 291 
LEU H      H N N 292 
LEU H2     H N N 293 
LEU HA     H N N 294 
LEU HB2    H N N 295 
LEU HB3    H N N 296 
LEU HG     H N N 297 
LEU HD11   H N N 298 
LEU HD12   H N N 299 
LEU HD13   H N N 300 
LEU HD21   H N N 301 
LEU HD22   H N N 302 
LEU HD23   H N N 303 
LEU HXT    H N N 304 
LYS N      N N N 305 
LYS CA     C N S 306 
LYS C      C N N 307 
LYS O      O N N 308 
LYS CB     C N N 309 
LYS CG     C N N 310 
LYS CD     C N N 311 
LYS CE     C N N 312 
LYS NZ     N N N 313 
LYS OXT    O N N 314 
LYS H      H N N 315 
LYS H2     H N N 316 
LYS HA     H N N 317 
LYS HB2    H N N 318 
LYS HB3    H N N 319 
LYS HG2    H N N 320 
LYS HG3    H N N 321 
LYS HD2    H N N 322 
LYS HD3    H N N 323 
LYS HE2    H N N 324 
LYS HE3    H N N 325 
LYS HZ1    H N N 326 
LYS HZ2    H N N 327 
LYS HZ3    H N N 328 
LYS HXT    H N N 329 
MET N      N N N 330 
MET CA     C N S 331 
MET C      C N N 332 
MET O      O N N 333 
MET CB     C N N 334 
MET CG     C N N 335 
MET SD     S N N 336 
MET CE     C N N 337 
MET OXT    O N N 338 
MET H      H N N 339 
MET H2     H N N 340 
MET HA     H N N 341 
MET HB2    H N N 342 
MET HB3    H N N 343 
MET HG2    H N N 344 
MET HG3    H N N 345 
MET HE1    H N N 346 
MET HE2    H N N 347 
MET HE3    H N N 348 
MET HXT    H N N 349 
PGE C1     C N N 350 
PGE O1     O N N 351 
PGE C2     C N N 352 
PGE O2     O N N 353 
PGE C3     C N N 354 
PGE C4     C N N 355 
PGE O4     O N N 356 
PGE C6     C N N 357 
PGE C5     C N N 358 
PGE O3     O N N 359 
PGE H1     H N N 360 
PGE H12    H N N 361 
PGE HO1    H N N 362 
PGE H2     H N N 363 
PGE H22    H N N 364 
PGE H3     H N N 365 
PGE H32    H N N 366 
PGE H4     H N N 367 
PGE H42    H N N 368 
PGE HO4    H N N 369 
PGE H6     H N N 370 
PGE H62    H N N 371 
PGE H5     H N N 372 
PGE H52    H N N 373 
PHE N      N N N 374 
PHE CA     C N S 375 
PHE C      C N N 376 
PHE O      O N N 377 
PHE CB     C N N 378 
PHE CG     C Y N 379 
PHE CD1    C Y N 380 
PHE CD2    C Y N 381 
PHE CE1    C Y N 382 
PHE CE2    C Y N 383 
PHE CZ     C Y N 384 
PHE OXT    O N N 385 
PHE H      H N N 386 
PHE H2     H N N 387 
PHE HA     H N N 388 
PHE HB2    H N N 389 
PHE HB3    H N N 390 
PHE HD1    H N N 391 
PHE HD2    H N N 392 
PHE HE1    H N N 393 
PHE HE2    H N N 394 
PHE HZ     H N N 395 
PHE HXT    H N N 396 
PRO N      N N N 397 
PRO CA     C N S 398 
PRO C      C N N 399 
PRO O      O N N 400 
PRO CB     C N N 401 
PRO CG     C N N 402 
PRO CD     C N N 403 
PRO OXT    O N N 404 
PRO H      H N N 405 
PRO HA     H N N 406 
PRO HB2    H N N 407 
PRO HB3    H N N 408 
PRO HG2    H N N 409 
PRO HG3    H N N 410 
PRO HD2    H N N 411 
PRO HD3    H N N 412 
PRO HXT    H N N 413 
SER N      N N N 414 
SER CA     C N S 415 
SER C      C N N 416 
SER O      O N N 417 
SER CB     C N N 418 
SER OG     O N N 419 
SER OXT    O N N 420 
SER H      H N N 421 
SER H2     H N N 422 
SER HA     H N N 423 
SER HB2    H N N 424 
SER HB3    H N N 425 
SER HG     H N N 426 
SER HXT    H N N 427 
THR N      N N N 428 
THR CA     C N S 429 
THR C      C N N 430 
THR O      O N N 431 
THR CB     C N R 432 
THR OG1    O N N 433 
THR CG2    C N N 434 
THR OXT    O N N 435 
THR H      H N N 436 
THR H2     H N N 437 
THR HA     H N N 438 
THR HB     H N N 439 
THR HG1    H N N 440 
THR HG21   H N N 441 
THR HG22   H N N 442 
THR HG23   H N N 443 
THR HXT    H N N 444 
TRP N      N N N 445 
TRP CA     C N S 446 
TRP C      C N N 447 
TRP O      O N N 448 
TRP CB     C N N 449 
TRP CG     C Y N 450 
TRP CD1    C Y N 451 
TRP CD2    C Y N 452 
TRP NE1    N Y N 453 
TRP CE2    C Y N 454 
TRP CE3    C Y N 455 
TRP CZ2    C Y N 456 
TRP CZ3    C Y N 457 
TRP CH2    C Y N 458 
TRP OXT    O N N 459 
TRP H      H N N 460 
TRP H2     H N N 461 
TRP HA     H N N 462 
TRP HB2    H N N 463 
TRP HB3    H N N 464 
TRP HD1    H N N 465 
TRP HE1    H N N 466 
TRP HE3    H N N 467 
TRP HZ2    H N N 468 
TRP HZ3    H N N 469 
TRP HH2    H N N 470 
TRP HXT    H N N 471 
TYR N      N N N 472 
TYR CA     C N S 473 
TYR C      C N N 474 
TYR O      O N N 475 
TYR CB     C N N 476 
TYR CG     C Y N 477 
TYR CD1    C Y N 478 
TYR CD2    C Y N 479 
TYR CE1    C Y N 480 
TYR CE2    C Y N 481 
TYR CZ     C Y N 482 
TYR OH     O N N 483 
TYR OXT    O N N 484 
TYR H      H N N 485 
TYR H2     H N N 486 
TYR HA     H N N 487 
TYR HB2    H N N 488 
TYR HB3    H N N 489 
TYR HD1    H N N 490 
TYR HD2    H N N 491 
TYR HE1    H N N 492 
TYR HE2    H N N 493 
TYR HH     H N N 494 
TYR HXT    H N N 495 
VAL N      N N N 496 
VAL CA     C N S 497 
VAL C      C N N 498 
VAL O      O N N 499 
VAL CB     C N N 500 
VAL CG1    C N N 501 
VAL CG2    C N N 502 
VAL OXT    O N N 503 
VAL H      H N N 504 
VAL H2     H N N 505 
VAL HA     H N N 506 
VAL HB     H N N 507 
VAL HG11   H N N 508 
VAL HG12   H N N 509 
VAL HG13   H N N 510 
VAL HG21   H N N 511 
VAL HG22   H N N 512 
VAL HG23   H N N 513 
VAL HXT    H N N 514 
# 
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  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
GOL C1    O1     sing N N 220 
GOL C1    C2     sing N N 221 
GOL C1    H11    sing N N 222 
GOL C1    H12    sing N N 223 
GOL O1    HO1    sing N N 224 
GOL C2    O2     sing N N 225 
GOL C2    C3     sing N N 226 
GOL C2    H2     sing N N 227 
GOL O2    HO2    sing N N 228 
GOL C3    O3     sing N N 229 
GOL C3    H31    sing N N 230 
GOL C3    H32    sing N N 231 
GOL O3    HO3    sing N N 232 
HIS N     CA     sing N N 233 
HIS N     H      sing N N 234 
HIS N     H2     sing N N 235 
HIS CA    C      sing N N 236 
HIS CA    CB     sing N N 237 
HIS CA    HA     sing N N 238 
HIS C     O      doub N N 239 
HIS C     OXT    sing N N 240 
HIS CB    CG     sing N N 241 
HIS CB    HB2    sing N N 242 
HIS CB    HB3    sing N N 243 
HIS CG    ND1    sing Y N 244 
HIS CG    CD2    doub Y N 245 
HIS ND1   CE1    doub Y N 246 
HIS ND1   HD1    sing N N 247 
HIS CD2   NE2    sing Y N 248 
HIS CD2   HD2    sing N N 249 
HIS CE1   NE2    sing Y N 250 
HIS CE1   HE1    sing N N 251 
HIS NE2   HE2    sing N N 252 
HIS OXT   HXT    sing N N 253 
HOH O     H1     sing N N 254 
HOH O     H2     sing N N 255 
ILE N     CA     sing N N 256 
ILE N     H      sing N N 257 
ILE N     H2     sing N N 258 
ILE CA    C      sing N N 259 
ILE CA    CB     sing N N 260 
ILE CA    HA     sing N N 261 
ILE C     O      doub N N 262 
ILE C     OXT    sing N N 263 
ILE CB    CG1    sing N N 264 
ILE CB    CG2    sing N N 265 
ILE CB    HB     sing N N 266 
ILE CG1   CD1    sing N N 267 
ILE CG1   HG12   sing N N 268 
ILE CG1   HG13   sing N N 269 
ILE CG2   HG21   sing N N 270 
ILE CG2   HG22   sing N N 271 
ILE CG2   HG23   sing N N 272 
ILE CD1   HD11   sing N N 273 
ILE CD1   HD12   sing N N 274 
ILE CD1   HD13   sing N N 275 
ILE OXT   HXT    sing N N 276 
LEU N     CA     sing N N 277 
LEU N     H      sing N N 278 
LEU N     H2     sing N N 279 
LEU CA    C      sing N N 280 
LEU CA    CB     sing N N 281 
LEU CA    HA     sing N N 282 
LEU C     O      doub N N 283 
LEU C     OXT    sing N N 284 
LEU CB    CG     sing N N 285 
LEU CB    HB2    sing N N 286 
LEU CB    HB3    sing N N 287 
LEU CG    CD1    sing N N 288 
LEU CG    CD2    sing N N 289 
LEU CG    HG     sing N N 290 
LEU CD1   HD11   sing N N 291 
LEU CD1   HD12   sing N N 292 
LEU CD1   HD13   sing N N 293 
LEU CD2   HD21   sing N N 294 
LEU CD2   HD22   sing N N 295 
LEU CD2   HD23   sing N N 296 
LEU OXT   HXT    sing N N 297 
LYS N     CA     sing N N 298 
LYS N     H      sing N N 299 
LYS N     H2     sing N N 300 
LYS CA    C      sing N N 301 
LYS CA    CB     sing N N 302 
LYS CA    HA     sing N N 303 
LYS C     O      doub N N 304 
LYS C     OXT    sing N N 305 
LYS CB    CG     sing N N 306 
LYS CB    HB2    sing N N 307 
LYS CB    HB3    sing N N 308 
LYS CG    CD     sing N N 309 
LYS CG    HG2    sing N N 310 
LYS CG    HG3    sing N N 311 
LYS CD    CE     sing N N 312 
LYS CD    HD2    sing N N 313 
LYS CD    HD3    sing N N 314 
LYS CE    NZ     sing N N 315 
LYS CE    HE2    sing N N 316 
LYS CE    HE3    sing N N 317 
LYS NZ    HZ1    sing N N 318 
LYS NZ    HZ2    sing N N 319 
LYS NZ    HZ3    sing N N 320 
LYS OXT   HXT    sing N N 321 
MET N     CA     sing N N 322 
MET N     H      sing N N 323 
MET N     H2     sing N N 324 
MET CA    C      sing N N 325 
MET CA    CB     sing N N 326 
MET CA    HA     sing N N 327 
MET C     O      doub N N 328 
MET C     OXT    sing N N 329 
MET CB    CG     sing N N 330 
MET CB    HB2    sing N N 331 
MET CB    HB3    sing N N 332 
MET CG    SD     sing N N 333 
MET CG    HG2    sing N N 334 
MET CG    HG3    sing N N 335 
MET SD    CE     sing N N 336 
MET CE    HE1    sing N N 337 
MET CE    HE2    sing N N 338 
MET CE    HE3    sing N N 339 
MET OXT   HXT    sing N N 340 
PGE C1    O1     sing N N 341 
PGE C1    C2     sing N N 342 
PGE C1    H1     sing N N 343 
PGE C1    H12    sing N N 344 
PGE O1    HO1    sing N N 345 
PGE C2    O2     sing N N 346 
PGE C2    H2     sing N N 347 
PGE C2    H22    sing N N 348 
PGE O2    C3     sing N N 349 
PGE C3    C4     sing N N 350 
PGE C3    H3     sing N N 351 
PGE C3    H32    sing N N 352 
PGE C4    O3     sing N N 353 
PGE C4    H4     sing N N 354 
PGE C4    H42    sing N N 355 
PGE O4    C6     sing N N 356 
PGE O4    HO4    sing N N 357 
PGE C6    C5     sing N N 358 
PGE C6    H6     sing N N 359 
PGE C6    H62    sing N N 360 
PGE C5    O3     sing N N 361 
PGE C5    H5     sing N N 362 
PGE C5    H52    sing N N 363 
PHE N     CA     sing N N 364 
PHE N     H      sing N N 365 
PHE N     H2     sing N N 366 
PHE CA    C      sing N N 367 
PHE CA    CB     sing N N 368 
PHE CA    HA     sing N N 369 
PHE C     O      doub N N 370 
PHE C     OXT    sing N N 371 
PHE CB    CG     sing N N 372 
PHE CB    HB2    sing N N 373 
PHE CB    HB3    sing N N 374 
PHE CG    CD1    doub Y N 375 
PHE CG    CD2    sing Y N 376 
PHE CD1   CE1    sing Y N 377 
PHE CD1   HD1    sing N N 378 
PHE CD2   CE2    doub Y N 379 
PHE CD2   HD2    sing N N 380 
PHE CE1   CZ     doub Y N 381 
PHE CE1   HE1    sing N N 382 
PHE CE2   CZ     sing Y N 383 
PHE CE2   HE2    sing N N 384 
PHE CZ    HZ     sing N N 385 
PHE OXT   HXT    sing N N 386 
PRO N     CA     sing N N 387 
PRO N     CD     sing N N 388 
PRO N     H      sing N N 389 
PRO CA    C      sing N N 390 
PRO CA    CB     sing N N 391 
PRO CA    HA     sing N N 392 
PRO C     O      doub N N 393 
PRO C     OXT    sing N N 394 
PRO CB    CG     sing N N 395 
PRO CB    HB2    sing N N 396 
PRO CB    HB3    sing N N 397 
PRO CG    CD     sing N N 398 
PRO CG    HG2    sing N N 399 
PRO CG    HG3    sing N N 400 
PRO CD    HD2    sing N N 401 
PRO CD    HD3    sing N N 402 
PRO OXT   HXT    sing N N 403 
SER N     CA     sing N N 404 
SER N     H      sing N N 405 
SER N     H2     sing N N 406 
SER CA    C      sing N N 407 
SER CA    CB     sing N N 408 
SER CA    HA     sing N N 409 
SER C     O      doub N N 410 
SER C     OXT    sing N N 411 
SER CB    OG     sing N N 412 
SER CB    HB2    sing N N 413 
SER CB    HB3    sing N N 414 
SER OG    HG     sing N N 415 
SER OXT   HXT    sing N N 416 
THR N     CA     sing N N 417 
THR N     H      sing N N 418 
THR N     H2     sing N N 419 
THR CA    C      sing N N 420 
THR CA    CB     sing N N 421 
THR CA    HA     sing N N 422 
THR C     O      doub N N 423 
THR C     OXT    sing N N 424 
THR CB    OG1    sing N N 425 
THR CB    CG2    sing N N 426 
THR CB    HB     sing N N 427 
THR OG1   HG1    sing N N 428 
THR CG2   HG21   sing N N 429 
THR CG2   HG22   sing N N 430 
THR CG2   HG23   sing N N 431 
THR OXT   HXT    sing N N 432 
TRP N     CA     sing N N 433 
TRP N     H      sing N N 434 
TRP N     H2     sing N N 435 
TRP CA    C      sing N N 436 
TRP CA    CB     sing N N 437 
TRP CA    HA     sing N N 438 
TRP C     O      doub N N 439 
TRP C     OXT    sing N N 440 
TRP CB    CG     sing N N 441 
TRP CB    HB2    sing N N 442 
TRP CB    HB3    sing N N 443 
TRP CG    CD1    doub Y N 444 
TRP CG    CD2    sing Y N 445 
TRP CD1   NE1    sing Y N 446 
TRP CD1   HD1    sing N N 447 
TRP CD2   CE2    doub Y N 448 
TRP CD2   CE3    sing Y N 449 
TRP NE1   CE2    sing Y N 450 
TRP NE1   HE1    sing N N 451 
TRP CE2   CZ2    sing Y N 452 
TRP CE3   CZ3    doub Y N 453 
TRP CE3   HE3    sing N N 454 
TRP CZ2   CH2    doub Y N 455 
TRP CZ2   HZ2    sing N N 456 
TRP CZ3   CH2    sing Y N 457 
TRP CZ3   HZ3    sing N N 458 
TRP CH2   HH2    sing N N 459 
TRP OXT   HXT    sing N N 460 
TYR N     CA     sing N N 461 
TYR N     H      sing N N 462 
TYR N     H2     sing N N 463 
TYR CA    C      sing N N 464 
TYR CA    CB     sing N N 465 
TYR CA    HA     sing N N 466 
TYR C     O      doub N N 467 
TYR C     OXT    sing N N 468 
TYR CB    CG     sing N N 469 
TYR CB    HB2    sing N N 470 
TYR CB    HB3    sing N N 471 
TYR CG    CD1    doub Y N 472 
TYR CG    CD2    sing Y N 473 
TYR CD1   CE1    sing Y N 474 
TYR CD1   HD1    sing N N 475 
TYR CD2   CE2    doub Y N 476 
TYR CD2   HD2    sing N N 477 
TYR CE1   CZ     doub Y N 478 
TYR CE1   HE1    sing N N 479 
TYR CE2   CZ     sing Y N 480 
TYR CE2   HE2    sing N N 481 
TYR CZ    OH     sing N N 482 
TYR OH    HH     sing N N 483 
TYR OXT   HXT    sing N N 484 
VAL N     CA     sing N N 485 
VAL N     H      sing N N 486 
VAL N     H2     sing N N 487 
VAL CA    C      sing N N 488 
VAL CA    CB     sing N N 489 
VAL CA    HA     sing N N 490 
VAL C     O      doub N N 491 
VAL C     OXT    sing N N 492 
VAL CB    CG1    sing N N 493 
VAL CB    CG2    sing N N 494 
VAL CB    HB     sing N N 495 
VAL CG1   HG11   sing N N 496 
VAL CG1   HG12   sing N N 497 
VAL CG1   HG13   sing N N 498 
VAL CG2   HG21   sing N N 499 
VAL CG2   HG22   sing N N 500 
VAL CG2   HG23   sing N N 501 
VAL OXT   HXT    sing N N 502 
# 
_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 
# 
_pdbx_initial_refinement_model.accession_code   8PNG 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   1 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    8R1E 
_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.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.016157 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015443 
_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]   0.003473 
_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 
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     . GLY A 1 1   ? 1.041  -5.355  -43.073 1.00 49.96 ? -1   GLY B N     1 
ATOM   2    C CA    . GLY A 1 1   ? 1.763  -6.260  -42.141 1.00 51.18 ? -1   GLY B CA    1 
ATOM   3    C C     . GLY A 1 1   ? 1.242  -6.146  -40.717 1.00 49.45 ? -1   GLY B C     1 
ATOM   4    O O     . GLY A 1 1   ? 0.431  -5.243  -40.463 1.00 44.66 ? -1   GLY B O     1 
ATOM   5    N N     . HIS A 1 2   ? 1.771  -7.020  -39.857 1.00 50.64 ? 0    HIS B N     1 
ATOM   6    C CA    . HIS A 1 2   ? 1.351  -7.100  -38.446 1.00 55.40 ? 0    HIS B CA    1 
ATOM   7    C C     . HIS A 1 2   ? 2.385  -7.902  -37.649 1.00 56.88 ? 0    HIS B C     1 
ATOM   8    O O     . HIS A 1 2   ? 2.899  -8.895  -38.183 1.00 50.50 ? 0    HIS B O     1 
ATOM   9    C CB    . HIS A 1 2   ? 0.029  -7.860  -38.367 1.00 55.07 ? 0    HIS B CB    1 
ATOM   10   C CG    . HIS A 1 2   ? 0.207  -9.310  -38.667 1.00 58.82 ? 0    HIS B CG    1 
ATOM   11   N ND1   . HIS A 1 2   ? 0.226  -10.273 -37.679 1.00 67.12 ? 0    HIS B ND1   1 
ATOM   12   C CD2   . HIS A 1 2   ? 0.438  -9.958  -39.828 1.00 51.41 ? 0    HIS B CD2   1 
ATOM   13   C CE1   . HIS A 1 2   ? 0.425  -11.455 -38.226 1.00 65.64 ? 0    HIS B CE1   1 
ATOM   14   N NE2   . HIS A 1 2   ? 0.560  -11.286 -39.544 1.00 55.06 ? 0    HIS B NE2   1 
ATOM   15   N N     . MET A 1 3   ? 2.686  -7.486  -36.418 1.00 54.49 ? 1    MET B N     1 
ATOM   16   C CA    . MET A 1 3   ? 3.561  -8.300  -35.545 1.00 55.82 ? 1    MET B CA    1 
ATOM   17   C C     . MET A 1 3   ? 2.776  -9.559  -35.192 1.00 59.25 ? 1    MET B C     1 
ATOM   18   O O     . MET A 1 3   ? 1.653  -9.415  -34.694 1.00 66.73 ? 1    MET B O     1 
ATOM   19   C CB    . MET A 1 3   ? 3.888  -7.530  -34.268 1.00 58.50 ? 1    MET B CB    1 
ATOM   20   C CG    . MET A 1 3   ? 4.894  -8.215  -33.375 1.00 63.67 ? 1    MET B CG    1 
ATOM   21   S SD    . MET A 1 3   ? 5.570  -7.091  -32.127 1.00 61.58 ? 1    MET B SD    1 
ATOM   22   C CE    . MET A 1 3   ? 7.313  -7.225  -32.512 1.00 69.11 ? 1    MET B CE    1 
ATOM   23   N N     . ALA A 1 4   ? 3.324  -10.748 -35.433 1.00 62.18 ? 2    ALA B N     1 
ATOM   24   C CA    . ALA A 1 4   ? 2.525  -11.985 -35.236 1.00 58.15 ? 2    ALA B CA    1 
ATOM   25   C C     . ALA A 1 4   ? 2.071  -12.094 -33.785 1.00 51.93 ? 2    ALA B C     1 
ATOM   26   O O     . ALA A 1 4   ? 2.761  -11.562 -32.903 1.00 58.18 ? 2    ALA B O     1 
ATOM   27   C CB    . ALA A 1 4   ? 3.280  -13.213 -35.675 1.00 56.10 ? 2    ALA B CB    1 
ATOM   28   N N     . ASP A 1 5   ? 0.936  -12.757 -33.566 1.00 43.38 ? 3    ASP B N     1 
ATOM   29   C CA    . ASP A 1 5   ? 0.408  -12.855 -32.182 1.00 40.80 ? 3    ASP B CA    1 
ATOM   30   C C     . ASP A 1 5   ? 1.441  -13.567 -31.311 1.00 36.26 ? 3    ASP B C     1 
ATOM   31   O O     . ASP A 1 5   ? 1.957  -14.600 -31.723 1.00 35.99 ? 3    ASP B O     1 
ATOM   32   C CB    . ASP A 1 5   ? -0.934 -13.579 -32.107 1.00 39.06 ? 3    ASP B CB    1 
ATOM   33   C CG    . ASP A 1 5   ? -2.098 -12.795 -32.679 1.00 39.79 ? 3    ASP B CG    1 
ATOM   34   O OD1   . ASP A 1 5   ? -1.977 -11.568 -32.794 1.00 40.69 ? 3    ASP B OD1   1 
ATOM   35   O OD2   . ASP A 1 5   ? -3.115 -13.427 -33.001 1.00 41.66 ? 3    ASP B OD2   1 
ATOM   36   N N     . TYR A 1 6   ? 1.689  -13.024 -30.126 1.00 33.70 ? 4    TYR B N     1 
ATOM   37   C CA    . TYR A 1 6   ? 2.615  -13.700 -29.198 1.00 29.97 ? 4    TYR B CA    1 
ATOM   38   C C     . TYR A 1 6   ? 1.934  -14.900 -28.543 1.00 29.85 ? 4    TYR B C     1 
ATOM   39   O O     . TYR A 1 6   ? 0.817  -14.761 -28.051 1.00 30.55 ? 4    TYR B O     1 
ATOM   40   C CB    . TYR A 1 6   ? 3.096  -12.739 -28.113 1.00 30.50 ? 4    TYR B CB    1 
ATOM   41   C CG    . TYR A 1 6   ? 3.911  -13.428 -27.051 1.00 30.41 ? 4    TYR B CG    1 
ATOM   42   C CD1   . TYR A 1 6   ? 5.127  -14.009 -27.361 1.00 28.62 ? 4    TYR B CD1   1 
ATOM   43   C CD2   . TYR A 1 6   ? 3.452  -13.534 -25.750 1.00 29.69 ? 4    TYR B CD2   1 
ATOM   44   C CE1   . TYR A 1 6   ? 5.881  -14.661 -26.402 1.00 29.32 ? 4    TYR B CE1   1 
ATOM   45   C CE2   . TYR A 1 6   ? 4.195  -14.180 -24.777 1.00 29.51 ? 4    TYR B CE2   1 
ATOM   46   C CZ    . TYR A 1 6   ? 5.413  -14.745 -25.105 1.00 28.34 ? 4    TYR B CZ    1 
ATOM   47   O OH    . TYR A 1 6   ? 6.152  -15.388 -24.160 1.00 30.13 ? 4    TYR B OH    1 
ATOM   48   N N     . LYS A 1 7   ? 2.603  -16.044 -28.553 1.00 30.88 ? 5    LYS B N     1 
ATOM   49   C CA    . LYS A 1 7   ? 2.090  -17.217 -27.819 1.00 30.49 ? 5    LYS B CA    1 
ATOM   50   C C     . LYS A 1 7   ? 3.210  -17.686 -26.898 1.00 31.50 ? 5    LYS B C     1 
ATOM   51   O O     . LYS A 1 7   ? 4.291  -18.004 -27.397 1.00 28.51 ? 5    LYS B O     1 
ATOM   52   C CB    . LYS A 1 7   ? 1.633  -18.344 -28.743 1.00 35.28 ? 5    LYS B CB    1 
ATOM   53   C CG    . LYS A 1 7   ? 1.327  -19.660 -28.050 1.00 36.85 ? 5    LYS B CG    1 
ATOM   54   C CD    . LYS A 1 7   ? 0.918  -20.740 -29.015 1.00 44.65 ? 5    LYS B CD    1 
ATOM   55   C CE    . LYS A 1 7   ? 0.932  -22.117 -28.393 1.00 50.55 ? 5    LYS B CE    1 
ATOM   56   N NZ    . LYS A 1 7   ? -0.236 -22.919 -28.822 1.00 55.26 ? 5    LYS B NZ    1 
ATOM   57   N N     . ALA A 1 8   ? 2.934  -17.727 -25.599 1.00 31.28 ? 6    ALA B N     1 
ATOM   58   C CA    . ALA A 1 8   ? 3.950  -18.118 -24.608 1.00 27.98 ? 6    ALA B CA    1 
ATOM   59   C C     . ALA A 1 8   ? 4.420  -19.528 -24.940 1.00 27.79 ? 6    ALA B C     1 
ATOM   60   O O     . ALA A 1 8   ? 3.593  -20.390 -25.251 1.00 26.41 ? 6    ALA B O     1 
ATOM   61   C CB    . ALA A 1 8   ? 3.373  -18.006 -23.218 1.00 29.40 ? 6    ALA B CB    1 
ATOM   62   N N     . PRO A 1 9   ? 5.754  -19.785 -24.900 1.00 26.91 ? 7    PRO B N     1 
ATOM   63   C CA    . PRO A 1 9   ? 6.316  -21.097 -25.215 1.00 27.06 ? 7    PRO B CA    1 
ATOM   64   C C     . PRO A 1 9   ? 6.283  -22.080 -24.036 1.00 26.88 ? 7    PRO B C     1 
ATOM   65   O O     . PRO A 1 9   ? 7.320  -22.555 -23.583 1.00 24.70 ? 7    PRO B O     1 
ATOM   66   C CB    . PRO A 1 9   ? 7.763  -20.751 -25.607 1.00 31.07 ? 7    PRO B CB    1 
ATOM   67   C CG    . PRO A 1 9   ? 8.104  -19.552 -24.725 1.00 31.80 ? 7    PRO B CG    1 
ATOM   68   C CD    . PRO A 1 9   ? 6.804  -18.768 -24.677 1.00 30.26 ? 7    PRO B CD    1 
ATOM   69   N N     . LEU A 1 10  ? 5.074  -22.393 -23.564 1.00 28.01 ? 8    LEU B N     1 
ATOM   70   C CA    . LEU A 1 10  ? 4.906  -23.128 -22.279 1.00 26.91 ? 8    LEU B CA    1 
ATOM   71   C C     . LEU A 1 10  ? 5.380  -24.573 -22.444 1.00 27.43 ? 8    LEU B C     1 
ATOM   72   O O     . LEU A 1 10  ? 5.928  -25.108 -21.479 1.00 28.92 ? 8    LEU B O     1 
ATOM   73   C CB    . LEU A 1 10  ? 3.422  -23.078 -21.882 1.00 29.11 ? 8    LEU B CB    1 
ATOM   74   C CG    . LEU A 1 10  ? 2.863  -21.689 -21.579 1.00 27.80 ? 8    LEU B CG    1 
ATOM   75   C CD1   . LEU A 1 10  ? 1.502  -21.816 -20.922 1.00 30.60 ? 8    LEU B CD1   1 
ATOM   76   C CD2   . LEU A 1 10  ? 3.805  -20.892 -20.695 1.00 29.17 ? 8    LEU B CD2   1 
ATOM   77   N N     . ARG A 1 11  ? 5.159  -25.180 -23.625 1.00 27.23 ? 9    ARG B N     1 
ATOM   78   C CA    . ARG A 1 11  ? 5.567  -26.581 -23.877 1.00 28.19 ? 9    ARG B CA    1 
ATOM   79   C C     . ARG A 1 11  ? 7.090  -26.686 -23.740 1.00 26.16 ? 9    ARG B C     1 
ATOM   80   O O     . ARG A 1 11  ? 7.571  -27.635 -23.108 1.00 28.86 ? 9    ARG B O     1 
ATOM   81   C CB    . ARG A 1 11  ? 5.111  -27.070 -25.256 1.00 28.53 ? 9    ARG B CB    1 
ATOM   82   C CG    . ARG A 1 11  ? 5.624  -28.469 -25.574 1.00 29.14 ? 9    ARG B CG    1 
ATOM   83   C CD    . ARG A 1 11  ? 5.066  -29.490 -24.599 1.00 29.07 ? 9    ARG B CD    1 
ATOM   84   N NE    . ARG A 1 11  ? 5.575  -30.839 -24.811 1.00 31.56 ? 9    ARG B NE    1 
ATOM   85   C CZ    . ARG A 1 11  ? 6.595  -31.404 -24.153 1.00 34.13 ? 9    ARG B CZ    1 
ATOM   86   N NH1   . ARG A 1 11  ? 6.937  -32.658 -24.406 1.00 35.42 ? 9    ARG B NH1   1 
ATOM   87   N NH2   . ARG A 1 11  ? 7.274  -30.734 -23.236 1.00 34.28 ? 9    ARG B NH2   1 
ATOM   88   N N     . ASP A 1 12  ? 7.832  -25.752 -24.328 1.00 26.46 ? 10   ASP B N     1 
ATOM   89   C CA    . ASP A 1 12  ? 9.311  -25.758 -24.233 1.00 26.70 ? 10   ASP B CA    1 
ATOM   90   C C     . ASP A 1 12  ? 9.743  -25.515 -22.776 1.00 24.53 ? 10   ASP B C     1 
ATOM   91   O O     . ASP A 1 12  ? 10.684 -26.196 -22.311 1.00 23.71 ? 10   ASP B O     1 
ATOM   92   C CB    . ASP A 1 12  ? 9.961  -24.712 -25.142 1.00 25.67 ? 10   ASP B CB    1 
ATOM   93   C CG    . ASP A 1 12  ? 11.408 -25.080 -25.387 1.00 27.23 ? 10   ASP B CG    1 
ATOM   94   O OD1   . ASP A 1 12  ? 11.663 -26.264 -25.755 1.00 26.63 ? 10   ASP B OD1   1 
ATOM   95   O OD2   . ASP A 1 12  ? 12.278 -24.218 -25.149 1.00 28.70 ? 10   ASP B OD2   1 
ATOM   96   N N     . MET A 1 13  ? 9.127  -24.536 -22.124 1.00 25.42 ? 11   MET B N     1 
ATOM   97   C CA    . MET A 1 13  ? 9.379  -24.190 -20.696 1.00 28.39 ? 11   MET B CA    1 
ATOM   98   C C     . MET A 1 13  ? 9.135  -25.415 -19.787 1.00 27.14 ? 11   MET B C     1 
ATOM   99   O O     . MET A 1 13  ? 9.982  -25.671 -18.897 1.00 26.56 ? 11   MET B O     1 
ATOM   100  C CB    . MET A 1 13  ? 8.491  -23.015 -20.294 1.00 29.16 ? 11   MET B CB    1 
ATOM   101  C CG    . MET A 1 13  ? 9.080  -21.703 -20.737 1.00 28.53 ? 11   MET B CG    1 
ATOM   102  S SD    . MET A 1 13  ? 8.009  -20.299 -20.419 1.00 30.18 ? 11   MET B SD    1 
ATOM   103  C CE    . MET A 1 13  ? 9.097  -18.941 -20.864 1.00 30.21 ? 11   MET B CE    1 
ATOM   104  N N     . ARG A 1 14  ? 8.107  -26.224 -20.063 1.00 28.00 ? 12   ARG B N     1 
ATOM   105  C CA    . ARG A 1 14  ? 7.847  -27.478 -19.300 1.00 29.49 ? 12   ARG B CA    1 
ATOM   106  C C     . ARG A 1 14  ? 8.984  -28.463 -19.548 1.00 29.77 ? 12   ARG B C     1 
ATOM   107  O O     . ARG A 1 14  ? 9.453  -29.109 -18.589 1.00 31.34 ? 12   ARG B O     1 
ATOM   108  C CB    . ARG A 1 14  ? 6.536  -28.180 -19.695 1.00 35.48 ? 12   ARG B CB    1 
ATOM   109  C CG    . ARG A 1 14  ? 5.284  -27.579 -19.072 1.00 39.33 ? 12   ARG B CG    1 
ATOM   110  C CD    . ARG A 1 14  ? 4.064  -28.489 -19.141 1.00 40.16 ? 12   ARG B CD    1 
ATOM   111  N NE    . ARG A 1 14  ? 3.592  -28.710 -20.502 1.00 40.02 ? 12   ARG B NE    1 
ATOM   112  C CZ    . ARG A 1 14  ? 2.892  -27.833 -21.230 1.00 39.93 ? 12   ARG B CZ    1 
ATOM   113  N NH1   . ARG A 1 14  ? 2.521  -28.156 -22.455 1.00 35.67 ? 12   ARG B NH1   1 
ATOM   114  N NH2   . ARG A 1 14  ? 2.545  -26.648 -20.739 1.00 39.98 ? 12   ARG B NH2   1 
ATOM   115  N N     . PHE A 1 15  ? 9.394  -28.626 -20.803 1.00 29.45 ? 13   PHE B N     1 
ATOM   116  C CA    . PHE A 1 15  ? 10.479 -29.571 -21.166 1.00 26.16 ? 13   PHE B CA    1 
ATOM   117  C C     . PHE A 1 15  ? 11.761 -29.200 -20.400 1.00 25.30 ? 13   PHE B C     1 
ATOM   118  O O     . PHE A 1 15  ? 12.391 -30.058 -19.783 1.00 26.57 ? 13   PHE B O     1 
ATOM   119  C CB    . PHE A 1 15  ? 10.742 -29.529 -22.678 1.00 26.34 ? 13   PHE B CB    1 
ATOM   120  C CG    . PHE A 1 15  ? 11.975 -30.282 -23.088 1.00 25.34 ? 13   PHE B CG    1 
ATOM   121  C CD1   . PHE A 1 15  ? 11.986 -31.668 -23.088 1.00 26.10 ? 13   PHE B CD1   1 
ATOM   122  C CD2   . PHE A 1 15  ? 13.137 -29.618 -23.445 1.00 26.04 ? 13   PHE B CD2   1 
ATOM   123  C CE1   . PHE A 1 15  ? 13.123 -32.369 -23.453 1.00 26.26 ? 13   PHE B CE1   1 
ATOM   124  C CE2   . PHE A 1 15  ? 14.268 -30.323 -23.844 1.00 26.41 ? 13   PHE B CE2   1 
ATOM   125  C CZ    . PHE A 1 15  ? 14.271 -31.700 -23.820 1.00 26.74 ? 13   PHE B CZ    1 
ATOM   126  N N     . VAL A 1 16  ? 12.133 -27.920 -20.425 1.00 25.22 ? 14   VAL B N     1 
ATOM   127  C CA    . VAL A 1 16  ? 13.410 -27.444 -19.823 1.00 27.63 ? 14   VAL B CA    1 
ATOM   128  C C     . VAL A 1 16  ? 13.384 -27.693 -18.305 1.00 26.39 ? 14   VAL B C     1 
ATOM   129  O O     . VAL A 1 16  ? 14.300 -28.345 -17.795 1.00 28.75 ? 14   VAL B O     1 
ATOM   130  C CB    . VAL A 1 16  ? 13.663 -25.963 -20.167 1.00 24.69 ? 14   VAL B CB    1 
ATOM   131  C CG1   . VAL A 1 16  ? 14.858 -25.419 -19.398 1.00 24.11 ? 14   VAL B CG1   1 
ATOM   132  C CG2   . VAL A 1 16  ? 13.863 -25.786 -21.673 1.00 25.78 ? 14   VAL B CG2   1 
ATOM   133  N N     . LEU A 1 17  ? 12.378 -27.167 -17.613 1.00 28.02 ? 15   LEU B N     1 
ATOM   134  C CA    . LEU A 1 17  ? 12.282 -27.196 -16.125 1.00 31.54 ? 15   LEU B CA    1 
ATOM   135  C C     . LEU A 1 17  ? 11.867 -28.591 -15.624 1.00 30.53 ? 15   LEU B C     1 
ATOM   136  O O     . LEU A 1 17  ? 12.552 -29.124 -14.744 1.00 32.56 ? 15   LEU B O     1 
ATOM   137  C CB    . LEU A 1 17  ? 11.286 -26.128 -15.650 1.00 30.47 ? 15   LEU B CB    1 
ATOM   138  C CG    . LEU A 1 17  ? 11.850 -24.715 -15.537 1.00 35.49 ? 15   LEU B CG    1 
ATOM   139  C CD1   . LEU A 1 17  ? 10.962 -23.844 -14.666 1.00 37.56 ? 15   LEU B CD1   1 
ATOM   140  C CD2   . LEU A 1 17  ? 13.264 -24.710 -14.986 1.00 37.01 ? 15   LEU B CD2   1 
ATOM   141  N N     . ASN A 1 18  ? 10.775 -29.148 -16.124 1.00 31.79 ? 16   ASN B N     1 
ATOM   142  C CA    . ASN A 1 18  ? 10.178 -30.390 -15.550 1.00 32.75 ? 16   ASN B CA    1 
ATOM   143  C C     . ASN A 1 18  ? 10.923 -31.613 -16.072 1.00 34.31 ? 16   ASN B C     1 
ATOM   144  O O     . ASN A 1 18  ? 11.091 -32.554 -15.293 1.00 34.27 ? 16   ASN B O     1 
ATOM   145  C CB    . ASN A 1 18  ? 8.673  -30.479 -15.815 1.00 34.51 ? 16   ASN B CB    1 
ATOM   146  C CG    . ASN A 1 18  ? 7.951  -29.278 -15.242 1.00 36.89 ? 16   ASN B CG    1 
ATOM   147  O OD1   . ASN A 1 18  ? 8.504  -28.563 -14.417 1.00 43.28 ? 16   ASN B OD1   1 
ATOM   148  N ND2   . ASN A 1 18  ? 6.746  -29.013 -15.699 1.00 42.09 ? 16   ASN B ND2   1 
ATOM   149  N N     . GLU A 1 19  ? 11.337 -31.618 -17.343 1.00 32.07 ? 17   GLU B N     1 
ATOM   150  C CA    . GLU A 1 19  ? 11.856 -32.852 -17.975 1.00 33.14 ? 17   GLU B CA    1 
ATOM   151  C C     . GLU A 1 19  ? 13.385 -32.883 -17.899 1.00 34.93 ? 17   GLU B C     1 
ATOM   152  O O     . GLU A 1 19  ? 13.915 -33.955 -17.576 1.00 34.30 ? 17   GLU B O     1 
ATOM   153  C CB    . GLU A 1 19  ? 11.364 -32.985 -19.414 1.00 34.46 ? 17   GLU B CB    1 
ATOM   154  C CG    . GLU A 1 19  ? 9.854  -32.967 -19.539 1.00 33.11 ? 17   GLU B CG    1 
ATOM   155  C CD    . GLU A 1 19  ? 9.374  -33.326 -20.928 1.00 32.98 ? 17   GLU B CD    1 
ATOM   156  O OE1   . GLU A 1 19  ? 8.701  -32.489 -21.538 1.00 30.34 ? 17   GLU B OE1   1 
ATOM   157  O OE2   . GLU A 1 19  ? 9.701  -34.445 -21.395 1.00 33.19 ? 17   GLU B OE2   1 
ATOM   158  N N     . VAL A 1 20  ? 14.071 -31.787 -18.222 1.00 30.63 ? 18   VAL B N     1 
ATOM   159  C CA    . VAL A 1 20  ? 15.562 -31.786 -18.282 1.00 29.88 ? 18   VAL B CA    1 
ATOM   160  C C     . VAL A 1 20  ? 16.111 -31.573 -16.873 1.00 31.73 ? 18   VAL B C     1 
ATOM   161  O O     . VAL A 1 20  ? 16.893 -32.425 -16.393 1.00 31.46 ? 18   VAL B O     1 
ATOM   162  C CB    . VAL A 1 20  ? 16.090 -30.730 -19.270 1.00 29.66 ? 18   VAL B CB    1 
ATOM   163  C CG1   . VAL A 1 20  ? 17.608 -30.624 -19.215 1.00 30.67 ? 18   VAL B CG1   1 
ATOM   164  C CG2   . VAL A 1 20  ? 15.603 -31.012 -20.678 1.00 31.53 ? 18   VAL B CG2   1 
ATOM   165  N N     . PHE A 1 21  ? 15.720 -30.473 -16.235 1.00 28.38 ? 19   PHE B N     1 
ATOM   166  C CA    . PHE A 1 21  ? 16.233 -30.076 -14.902 1.00 29.63 ? 19   PHE B CA    1 
ATOM   167  C C     . PHE A 1 21  ? 15.447 -30.736 -13.758 1.00 31.97 ? 19   PHE B C     1 
ATOM   168  O O     . PHE A 1 21  ? 15.991 -30.767 -12.649 1.00 33.16 ? 19   PHE B O     1 
ATOM   169  C CB    . PHE A 1 21  ? 16.298 -28.549 -14.831 1.00 29.16 ? 19   PHE B CB    1 
ATOM   170  C CG    . PHE A 1 21  ? 17.354 -28.008 -15.759 1.00 28.41 ? 19   PHE B CG    1 
ATOM   171  C CD1   . PHE A 1 21  ? 18.636 -28.530 -15.733 1.00 28.33 ? 19   PHE B CD1   1 
ATOM   172  C CD2   . PHE A 1 21  ? 17.065 -27.009 -16.674 1.00 29.28 ? 19   PHE B CD2   1 
ATOM   173  C CE1   . PHE A 1 21  ? 19.615 -28.047 -16.587 1.00 30.91 ? 19   PHE B CE1   1 
ATOM   174  C CE2   . PHE A 1 21  ? 18.048 -26.530 -17.529 1.00 28.38 ? 19   PHE B CE2   1 
ATOM   175  C CZ    . PHE A 1 21  ? 19.313 -27.061 -17.494 1.00 29.12 ? 19   PHE B CZ    1 
ATOM   176  N N     . GLU A 1 22  ? 14.244 -31.270 -13.997 1.00 32.61 ? 20   GLU B N     1 
ATOM   177  C CA    . GLU A 1 22  ? 13.483 -32.035 -12.968 1.00 39.07 ? 20   GLU B CA    1 
ATOM   178  C C     . GLU A 1 22  ? 13.304 -31.187 -11.701 1.00 38.56 ? 20   GLU B C     1 
ATOM   179  O O     . GLU A 1 22  ? 13.554 -31.702 -10.617 1.00 39.22 ? 20   GLU B O     1 
ATOM   180  C CB    . GLU A 1 22  ? 14.194 -33.361 -12.690 1.00 40.02 ? 20   GLU B CB    1 
ATOM   181  C CG    . GLU A 1 22  ? 13.883 -34.388 -13.762 1.00 45.54 ? 20   GLU B CG    1 
ATOM   182  C CD    . GLU A 1 22  ? 14.550 -35.747 -13.654 1.00 50.02 ? 20   GLU B CD    1 
ATOM   183  O OE1   . GLU A 1 22  ? 15.497 -35.914 -12.847 1.00 54.41 ? 20   GLU B OE1   1 
ATOM   184  O OE2   . GLU A 1 22  ? 14.135 -36.631 -14.415 1.00 58.24 ? 20   GLU B OE2   1 
ATOM   185  N N     . VAL A 1 23  ? 12.844 -29.942 -11.845 1.00 37.89 ? 21   VAL B N     1 
ATOM   186  C CA    . VAL A 1 23  ? 12.945 -28.909 -10.776 1.00 42.05 ? 21   VAL B CA    1 
ATOM   187  C C     . VAL A 1 23  ? 12.048 -29.305 -9.605  1.00 46.96 ? 21   VAL B C     1 
ATOM   188  O O     . VAL A 1 23  ? 12.352 -28.849 -8.497  1.00 49.22 ? 21   VAL B O     1 
ATOM   189  C CB    . VAL A 1 23  ? 12.629 -27.476 -11.249 1.00 40.50 ? 21   VAL B CB    1 
ATOM   190  C CG1   . VAL A 1 23  ? 13.721 -26.955 -12.167 1.00 45.07 ? 21   VAL B CG1   1 
ATOM   191  C CG2   . VAL A 1 23  ? 11.256 -27.358 -11.886 1.00 41.08 ? 21   VAL B CG2   1 
ATOM   192  N N     . SER A 1 24  ? 11.009 -30.106 -9.835  1.00 46.94 ? 22   SER B N     1 
ATOM   193  C CA    . SER A 1 24  ? 10.103 -30.576 -8.754  1.00 52.09 ? 22   SER B CA    1 
ATOM   194  C C     . SER A 1 24  ? 10.885 -31.509 -7.811  1.00 53.53 ? 22   SER B C     1 
ATOM   195  O O     . SER A 1 24  ? 10.781 -31.308 -6.595  1.00 56.45 ? 22   SER B O     1 
ATOM   196  C CB    . SER A 1 24  ? 8.844  -31.188 -9.307  1.00 49.16 ? 22   SER B CB    1 
ATOM   197  O OG    . SER A 1 24  ? 9.080  -32.518 -9.712  1.00 59.23 ? 22   SER B OG    1 
ATOM   198  N N     . ARG A 1 25  ? 11.700 -32.435 -8.329  1.00 56.62 ? 23   ARG B N     1 
ATOM   199  C CA    . ARG A 1 25  ? 12.566 -33.311 -7.488  1.00 59.06 ? 23   ARG B CA    1 
ATOM   200  C C     . ARG A 1 25  ? 13.521 -32.445 -6.656  1.00 60.60 ? 23   ARG B C     1 
ATOM   201  O O     . ARG A 1 25  ? 13.882 -32.869 -5.550  1.00 60.84 ? 23   ARG B O     1 
ATOM   202  C CB    . ARG A 1 25  ? 13.381 -34.306 -8.318  1.00 60.64 ? 23   ARG B CB    1 
ATOM   203  C CG    . ARG A 1 25  ? 12.575 -35.468 -8.887  1.00 71.48 ? 23   ARG B CG    1 
ATOM   204  C CD    . ARG A 1 25  ? 13.440 -36.554 -9.515  1.00 79.43 ? 23   ARG B CD    1 
ATOM   205  N NE    . ARG A 1 25  ? 14.724 -36.003 -9.940  1.00 87.62 ? 23   ARG B NE    1 
ATOM   206  C CZ    . ARG A 1 25  ? 15.913 -36.252 -9.385  1.00 94.66 ? 23   ARG B CZ    1 
ATOM   207  N NH1   . ARG A 1 25  ? 16.992 -35.651 -9.862  1.00 96.46 ? 23   ARG B NH1   1 
ATOM   208  N NH2   . ARG A 1 25  ? 16.036 -37.101 -8.378  1.00 98.10 ? 23   ARG B NH2   1 
ATOM   209  N N     . LEU A 1 26  ? 13.924 -31.277 -7.159  1.00 59.72 ? 24   LEU B N     1 
ATOM   210  C CA    . LEU A 1 26  ? 14.841 -30.360 -6.423  1.00 58.14 ? 24   LEU B CA    1 
ATOM   211  C C     . LEU A 1 26  ? 14.057 -29.588 -5.346  1.00 52.29 ? 24   LEU B C     1 
ATOM   212  O O     . LEU A 1 26  ? 14.599 -29.425 -4.247  1.00 54.77 ? 24   LEU B O     1 
ATOM   213  C CB    . LEU A 1 26  ? 15.540 -29.422 -7.415  1.00 62.14 ? 24   LEU B CB    1 
ATOM   214  C CG    . LEU A 1 26  ? 16.262 -30.101 -8.584  1.00 66.66 ? 24   LEU B CG    1 
ATOM   215  C CD1   . LEU A 1 26  ? 16.708 -29.077 -9.618  1.00 68.41 ? 24   LEU B CD1   1 
ATOM   216  C CD2   . LEU A 1 26  ? 17.447 -30.931 -8.103  1.00 67.82 ? 24   LEU B CD2   1 
ATOM   217  N N     . TRP A 1 27  ? 12.829 -29.136 -5.637  1.00 50.10 ? 25   TRP B N     1 
ATOM   218  C CA    . TRP A 1 27  ? 11.950 -28.400 -4.678  1.00 51.61 ? 25   TRP B CA    1 
ATOM   219  C C     . TRP A 1 27  ? 11.497 -29.320 -3.529  1.00 56.34 ? 25   TRP B C     1 
ATOM   220  O O     . TRP A 1 27  ? 11.117 -28.779 -2.465  1.00 54.74 ? 25   TRP B O     1 
ATOM   221  C CB    . TRP A 1 27  ? 10.704 -27.815 -5.358  1.00 48.01 ? 25   TRP B CB    1 
ATOM   222  C CG    . TRP A 1 27  ? 10.928 -26.822 -6.460  1.00 42.05 ? 25   TRP B CG    1 
ATOM   223  C CD1   . TRP A 1 27  ? 11.996 -25.998 -6.667  1.00 38.85 ? 25   TRP B CD1   1 
ATOM   224  C CD2   . TRP A 1 27  ? 9.984  -26.524 -7.502  1.00 38.41 ? 25   TRP B CD2   1 
ATOM   225  N NE1   . TRP A 1 27  ? 11.785 -25.217 -7.775  1.00 37.61 ? 25   TRP B NE1   1 
ATOM   226  C CE2   . TRP A 1 27  ? 10.562 -25.526 -8.311  1.00 38.67 ? 25   TRP B CE2   1 
ATOM   227  C CE3   . TRP A 1 27  ? 8.716  -27.018 -7.828  1.00 37.61 ? 25   TRP B CE3   1 
ATOM   228  C CZ2   . TRP A 1 27  ? 9.906  -25.015 -9.431  1.00 39.34 ? 25   TRP B CZ2   1 
ATOM   229  C CZ3   . TRP A 1 27  ? 8.076  -26.526 -8.943  1.00 38.10 ? 25   TRP B CZ3   1 
ATOM   230  C CH2   . TRP A 1 27  ? 8.665  -25.529 -9.726  1.00 38.85 ? 25   TRP B CH2   1 
ATOM   231  N N     . ALA A 1 28  ? 11.429 -30.635 -3.779  1.00 61.09 ? 26   ALA B N     1 
ATOM   232  C CA    . ALA A 1 28  ? 11.094 -31.694 -2.793  1.00 66.70 ? 26   ALA B CA    1 
ATOM   233  C C     . ALA A 1 28  ? 12.012 -31.557 -1.577  1.00 67.62 ? 26   ALA B C     1 
ATOM   234  O O     . ALA A 1 28  ? 11.510 -31.253 -0.487  1.00 74.15 ? 26   ALA B O     1 
ATOM   235  C CB    . ALA A 1 28  ? 11.240 -33.062 -3.420  1.00 65.77 ? 26   ALA B CB    1 
ATOM   236  N N     . GLN A 1 29  ? 13.312 -31.746 -1.798  1.00 71.97 ? 27   GLN B N     1 
ATOM   237  C CA    . GLN A 1 29  ? 14.399 -31.577 -0.801  1.00 73.07 ? 27   GLN B CA    1 
ATOM   238  C C     . GLN A 1 29  ? 14.783 -30.093 -0.724  1.00 73.23 ? 27   GLN B C     1 
ATOM   239  O O     . GLN A 1 29  ? 15.953 -29.769 -0.954  1.00 77.71 ? 27   GLN B O     1 
ATOM   240  C CB    . GLN A 1 29  ? 15.586 -32.458 -1.190  1.00 74.67 ? 27   GLN B CB    1 
ATOM   241  C CG    . GLN A 1 29  ? 16.066 -32.236 -2.621  1.00 75.74 ? 27   GLN B CG    1 
ATOM   242  C CD    . GLN A 1 29  ? 17.269 -33.069 -2.988  1.00 77.04 ? 27   GLN B CD    1 
ATOM   243  O OE1   . GLN A 1 29  ? 17.939 -32.806 -3.985  1.00 80.02 ? 27   GLN B OE1   1 
ATOM   244  N NE2   . GLN A 1 29  ? 17.556 -34.085 -2.189  1.00 79.79 ? 27   GLN B NE2   1 
ATOM   245  N N     . LEU A 1 30  ? 13.815 -29.228 -0.418  1.00 73.19 ? 28   LEU B N     1 
ATOM   246  C CA    . LEU A 1 30  ? 14.007 -27.776 -0.159  1.00 69.56 ? 28   LEU B CA    1 
ATOM   247  C C     . LEU A 1 30  ? 12.797 -27.310 0.640   1.00 70.10 ? 28   LEU B C     1 
ATOM   248  O O     . LEU A 1 30  ? 11.767 -26.965 0.072   1.00 64.58 ? 28   LEU B O     1 
ATOM   249  C CB    . LEU A 1 30  ? 14.140 -27.007 -1.478  1.00 68.16 ? 28   LEU B CB    1 
ATOM   250  C CG    . LEU A 1 30  ? 15.505 -27.066 -2.167  1.00 68.16 ? 28   LEU B CG    1 
ATOM   251  C CD1   . LEU A 1 30  ? 15.514 -26.234 -3.449  1.00 62.03 ? 28   LEU B CD1   1 
ATOM   252  C CD2   . LEU A 1 30  ? 16.611 -26.606 -1.226  1.00 71.82 ? 28   LEU B CD2   1 
ATOM   253  N N     . PRO A 1 31  ? 12.862 -27.351 1.987   1.00 76.87 ? 29   PRO B N     1 
ATOM   254  C CA    . PRO A 1 31  ? 11.680 -27.127 2.819   1.00 71.02 ? 29   PRO B CA    1 
ATOM   255  C C     . PRO A 1 31  ? 10.977 -25.794 2.547   1.00 62.85 ? 29   PRO B C     1 
ATOM   256  O O     . PRO A 1 31  ? 9.750  -25.770 2.523   1.00 63.51 ? 29   PRO B O     1 
ATOM   257  C CB    . PRO A 1 31  ? 12.246 -27.130 4.248   1.00 78.26 ? 29   PRO B CB    1 
ATOM   258  C CG    . PRO A 1 31  ? 13.493 -27.978 4.141   1.00 80.78 ? 29   PRO B CG    1 
ATOM   259  C CD    . PRO A 1 31  ? 14.067 -27.644 2.779   1.00 78.29 ? 29   PRO B CD    1 
ATOM   260  N N     . ALA A 1 32  ? 11.757 -24.728 2.350   1.00 55.37 ? 30   ALA B N     1 
ATOM   261  C CA    . ALA A 1 32  ? 11.237 -23.347 2.205   1.00 52.76 ? 30   ALA B CA    1 
ATOM   262  C C     . ALA A 1 32  ? 10.397 -23.212 0.920   1.00 55.76 ? 30   ALA B C     1 
ATOM   263  O O     . ALA A 1 32  ? 9.608  -22.251 0.836   1.00 49.20 ? 30   ALA B O     1 
ATOM   264  C CB    . ALA A 1 32  ? 12.382 -22.363 2.234   1.00 52.15 ? 30   ALA B CB    1 
ATOM   265  N N     . LEU A 1 33  ? 10.547 -24.128 -0.047  1.00 55.78 ? 31   LEU B N     1 
ATOM   266  C CA    . LEU A 1 33  ? 9.813  -24.080 -1.343  1.00 59.46 ? 31   LEU B CA    1 
ATOM   267  C C     . LEU A 1 33  ? 8.634  -25.059 -1.343  1.00 63.04 ? 31   LEU B C     1 
ATOM   268  O O     . LEU A 1 33  ? 7.589  -24.693 -1.911  1.00 63.72 ? 31   LEU B O     1 
ATOM   269  C CB    . LEU A 1 33  ? 10.786 -24.383 -2.485  1.00 60.27 ? 31   LEU B CB    1 
ATOM   270  C CG    . LEU A 1 33  ? 11.842 -23.305 -2.724  1.00 58.77 ? 31   LEU B CG    1 
ATOM   271  C CD1   . LEU A 1 33  ? 12.892 -23.796 -3.701  1.00 62.17 ? 31   LEU B CD1   1 
ATOM   272  C CD2   . LEU A 1 33  ? 11.207 -22.009 -3.213  1.00 53.98 ? 31   LEU B CD2   1 
ATOM   273  N N     . ALA A 1 34  ? 8.789  -26.244 -0.740  1.00 63.46 ? 32   ALA B N     1 
ATOM   274  C CA    . ALA A 1 34  ? 7.711  -27.249 -0.563  1.00 62.66 ? 32   ALA B CA    1 
ATOM   275  C C     . ALA A 1 34  ? 6.401  -26.531 -0.222  1.00 60.51 ? 32   ALA B C     1 
ATOM   276  O O     . ALA A 1 34  ? 5.356  -26.874 -0.797  1.00 59.47 ? 32   ALA B O     1 
ATOM   277  C CB    . ALA A 1 34  ? 8.099  -28.227 0.518   1.00 62.13 ? 32   ALA B CB    1 
ATOM   278  N N     . GLU A 1 35  ? 6.485  -25.545 0.669   1.00 63.00 ? 33   GLU B N     1 
ATOM   279  C CA    . GLU A 1 35  ? 5.355  -24.726 1.178   1.00 65.84 ? 33   GLU B CA    1 
ATOM   280  C C     . GLU A 1 35  ? 4.683  -23.913 0.068   1.00 61.64 ? 33   GLU B C     1 
ATOM   281  O O     . GLU A 1 35  ? 3.463  -23.689 0.162   1.00 58.43 ? 33   GLU B O     1 
ATOM   282  C CB    . GLU A 1 35  ? 5.870  -23.756 2.245   1.00 73.14 ? 33   GLU B CB    1 
ATOM   283  C CG    . GLU A 1 35  ? 6.289  -24.445 3.529   1.00 84.49 ? 33   GLU B CG    1 
ATOM   284  C CD    . GLU A 1 35  ? 5.208  -25.328 4.132   1.00 91.05 ? 33   GLU B CD    1 
ATOM   285  O OE1   . GLU A 1 35  ? 5.136  -26.517 3.754   1.00 92.49 ? 33   GLU B OE1   1 
ATOM   286  O OE2   . GLU A 1 35  ? 4.425  -24.822 4.964   1.00 98.99 ? 33   GLU B OE2   1 
ATOM   287  N N     . VAL A 1 36  ? 5.433  -23.411 -0.913  1.00 55.73 ? 34   VAL B N     1 
ATOM   288  C CA    . VAL A 1 36  ? 4.912  -22.308 -1.775  1.00 51.56 ? 34   VAL B CA    1 
ATOM   289  C C     . VAL A 1 36  ? 4.720  -22.764 -3.227  1.00 44.16 ? 34   VAL B C     1 
ATOM   290  O O     . VAL A 1 36  ? 3.907  -22.115 -3.927  1.00 42.16 ? 34   VAL B O     1 
ATOM   291  C CB    . VAL A 1 36  ? 5.811  -21.059 -1.666  1.00 60.09 ? 34   VAL B CB    1 
ATOM   292  C CG1   . VAL A 1 36  ? 7.105  -21.192 -2.454  1.00 57.13 ? 34   VAL B CG1   1 
ATOM   293  C CG2   . VAL A 1 36  ? 5.059  -19.801 -2.076  1.00 65.97 ? 34   VAL B CG2   1 
ATOM   294  N N     . VAL A 1 37  ? 5.412  -23.817 -3.680  1.00 38.90 ? 35   VAL B N     1 
ATOM   295  C CA    . VAL A 1 37  ? 5.388  -24.215 -5.123  1.00 39.61 ? 35   VAL B CA    1 
ATOM   296  C C     . VAL A 1 37  ? 5.527  -25.733 -5.261  1.00 36.41 ? 35   VAL B C     1 
ATOM   297  O O     . VAL A 1 37  ? 6.235  -26.344 -4.448  1.00 32.74 ? 35   VAL B O     1 
ATOM   298  C CB    . VAL A 1 37  ? 6.482  -23.482 -5.936  1.00 41.26 ? 35   VAL B CB    1 
ATOM   299  C CG1   . VAL A 1 37  ? 7.887  -23.938 -5.565  1.00 38.82 ? 35   VAL B CG1   1 
ATOM   300  C CG2   . VAL A 1 37  ? 6.260  -23.611 -7.439  1.00 41.06 ? 35   VAL B CG2   1 
ATOM   301  N N     . ASP A 1 38  ? 4.862  -26.267 -6.290  1.00 36.94 ? 36   ASP B N     1 
ATOM   302  C CA    . ASP A 1 38  ? 4.962  -27.647 -6.832  1.00 36.43 ? 36   ASP B CA    1 
ATOM   303  C C     . ASP A 1 38  ? 4.662  -27.549 -8.334  1.00 35.82 ? 36   ASP B C     1 
ATOM   304  O O     . ASP A 1 38  ? 4.370  -26.423 -8.799  1.00 36.60 ? 36   ASP B O     1 
ATOM   305  C CB    . ASP A 1 38  ? 4.012  -28.606 -6.099  1.00 39.15 ? 36   ASP B CB    1 
ATOM   306  C CG    . ASP A 1 38  ? 2.532  -28.255 -6.189  1.00 43.24 ? 36   ASP B CG    1 
ATOM   307  O OD1   . ASP A 1 38  ? 2.061  -27.902 -7.300  1.00 45.15 ? 36   ASP B OD1   1 
ATOM   308  O OD2   . ASP A 1 38  ? 1.847  -28.339 -5.144  1.00 48.10 ? 36   ASP B OD2   1 
ATOM   309  N N     . ALA A 1 39  ? 4.696  -28.670 -9.058  1.00 38.24 ? 37   ALA B N     1 
ATOM   310  C CA    . ALA A 1 39  ? 4.513  -28.738 -10.528 1.00 39.74 ? 37   ALA B CA    1 
ATOM   311  C C     . ALA A 1 39  ? 3.163  -28.121 -10.925 1.00 39.56 ? 37   ALA B C     1 
ATOM   312  O O     . ALA A 1 39  ? 3.127  -27.266 -11.848 1.00 40.36 ? 37   ALA B O     1 
ATOM   313  C CB    . ALA A 1 39  ? 4.626  -30.172 -10.977 1.00 40.17 ? 37   ALA B CB    1 
ATOM   314  N N     . GLU A 1 40  ? 2.086  -28.492 -10.233 1.00 41.27 ? 38   GLU B N     1 
ATOM   315  C CA    . GLU A 1 40  ? 0.706  -28.045 -10.584 1.00 45.30 ? 38   GLU B CA    1 
ATOM   316  C C     . GLU A 1 40  ? 0.554  -26.537 -10.294 1.00 41.42 ? 38   GLU B C     1 
ATOM   317  O O     . GLU A 1 40  ? 0.016  -25.809 -11.147 1.00 39.76 ? 38   GLU B O     1 
ATOM   318  C CB    . GLU A 1 40  ? -0.329 -28.888 -9.831  1.00 49.88 ? 38   GLU B CB    1 
ATOM   319  C CG    . GLU A 1 40  ? -0.327 -30.363 -10.225 1.00 54.39 ? 38   GLU B CG    1 
ATOM   320  C CD    . GLU A 1 40  ? 0.896  -31.187 -9.828  1.00 54.51 ? 38   GLU B CD    1 
ATOM   321  O OE1   . GLU A 1 40  ? 1.320  -31.134 -8.642  1.00 48.69 ? 38   GLU B OE1   1 
ATOM   322  O OE2   . GLU A 1 40  ? 1.436  -31.883 -10.712 1.00 61.31 ? 38   GLU B OE2   1 
ATOM   323  N N     . THR A 1 41  ? 0.962  -26.084 -9.113  1.00 37.01 ? 39   THR B N     1 
ATOM   324  C CA    . THR A 1 41  ? 1.034  -24.640 -8.754  1.00 39.99 ? 39   THR B CA    1 
ATOM   325  C C     . THR A 1 41  ? 1.786  -23.871 -9.860  1.00 36.25 ? 39   THR B C     1 
ATOM   326  O O     . THR A 1 41  ? 1.288  -22.826 -10.339 1.00 33.02 ? 39   THR B O     1 
ATOM   327  C CB    . THR A 1 41  ? 1.714  -24.496 -7.385  1.00 40.62 ? 39   THR B CB    1 
ATOM   328  O OG1   . THR A 1 41  ? 0.850  -25.134 -6.447  1.00 51.05 ? 39   THR B OG1   1 
ATOM   329  C CG2   . THR A 1 41  ? 1.969  -23.067 -6.959  1.00 39.64 ? 39   THR B CG2   1 
ATOM   330  N N     . ALA A 1 42  ? 2.955  -24.377 -10.252 1.00 35.70 ? 40   ALA B N     1 
ATOM   331  C CA    . ALA A 1 42  ? 3.864  -23.714 -11.217 1.00 34.95 ? 40   ALA B CA    1 
ATOM   332  C C     . ALA A 1 42  ? 3.197  -23.669 -12.592 1.00 33.00 ? 40   ALA B C     1 
ATOM   333  O O     . ALA A 1 42  ? 3.232  -22.609 -13.203 1.00 30.38 ? 40   ALA B O     1 
ATOM   334  C CB    . ALA A 1 42  ? 5.196  -24.419 -11.271 1.00 35.96 ? 40   ALA B CB    1 
ATOM   335  N N     . ALA A 1 43  ? 2.614  -24.784 -13.040 1.00 35.30 ? 41   ALA B N     1 
ATOM   336  C CA    . ALA A 1 43  ? 1.948  -24.905 -14.356 1.00 38.19 ? 41   ALA B CA    1 
ATOM   337  C C     . ALA A 1 43  ? 0.775  -23.921 -14.426 1.00 37.13 ? 41   ALA B C     1 
ATOM   338  O O     . ALA A 1 43  ? 0.604  -23.281 -15.496 1.00 37.73 ? 41   ALA B O     1 
ATOM   339  C CB    . ALA A 1 43  ? 1.502  -26.328 -14.594 1.00 40.83 ? 41   ALA B CB    1 
ATOM   340  N N     . ALA A 1 44  ? 0.023  -23.754 -13.332 1.00 36.51 ? 42   ALA B N     1 
ATOM   341  C CA    . ALA A 1 44  ? -1.178 -22.876 -13.296 1.00 36.38 ? 42   ALA B CA    1 
ATOM   342  C C     . ALA A 1 44  ? -0.765 -21.399 -13.396 1.00 30.79 ? 42   ALA B C     1 
ATOM   343  O O     . ALA A 1 44  ? -1.480 -20.608 -14.042 1.00 33.07 ? 42   ALA B O     1 
ATOM   344  C CB    . ALA A 1 44  ? -1.991 -23.138 -12.039 1.00 37.13 ? 42   ALA B CB    1 
ATOM   345  N N     . ILE A 1 45  ? 0.329  -21.023 -12.743 1.00 31.46 ? 43   ILE B N     1 
ATOM   346  C CA    . ILE A 1 45  ? 0.918  -19.648 -12.796 1.00 33.56 ? 43   ILE B CA    1 
ATOM   347  C C     . ILE A 1 45  ? 1.379  -19.357 -14.235 1.00 29.77 ? 43   ILE B C     1 
ATOM   348  O O     . ILE A 1 45  ? 1.032  -18.284 -14.780 1.00 29.06 ? 43   ILE B O     1 
ATOM   349  C CB    . ILE A 1 45  ? 2.055  -19.539 -11.759 1.00 35.27 ? 43   ILE B CB    1 
ATOM   350  C CG1   . ILE A 1 45  ? 1.467  -19.537 -10.346 1.00 40.38 ? 43   ILE B CG1   1 
ATOM   351  C CG2   . ILE A 1 45  ? 2.954  -18.326 -12.011 1.00 35.14 ? 43   ILE B CG2   1 
ATOM   352  C CD1   . ILE A 1 45  ? 2.486  -19.672 -9.241  1.00 40.80 ? 43   ILE B CD1   1 
ATOM   353  N N     . LEU A 1 46  ? 2.094  -20.296 -14.847 1.00 31.34 ? 44   LEU B N     1 
ATOM   354  C CA    . LEU A 1 46  ? 2.577  -20.134 -16.244 1.00 32.08 ? 44   LEU B CA    1 
ATOM   355  C C     . LEU A 1 46  ? 1.374  -19.967 -17.187 1.00 30.99 ? 44   LEU B C     1 
ATOM   356  O O     . LEU A 1 46  ? 1.383  -18.999 -17.984 1.00 31.85 ? 44   LEU B O     1 
ATOM   357  C CB    . LEU A 1 46  ? 3.485  -21.308 -16.611 1.00 34.79 ? 44   LEU B CB    1 
ATOM   358  C CG    . LEU A 1 46  ? 4.987  -21.050 -16.423 1.00 37.92 ? 44   LEU B CG    1 
ATOM   359  C CD1   . LEU A 1 46  ? 5.399  -19.771 -17.133 1.00 42.31 ? 44   LEU B CD1   1 
ATOM   360  C CD2   . LEU A 1 46  ? 5.382  -20.942 -14.967 1.00 38.92 ? 44   LEU B CD2   1 
ATOM   361  N N     . GLU A 1 47  ? 0.332  -20.804 -17.068 1.00 31.58 ? 45   GLU B N     1 
ATOM   362  C CA    . GLU A 1 47  ? -0.878 -20.664 -17.918 1.00 33.46 ? 45   GLU B CA    1 
ATOM   363  C C     . GLU A 1 47  ? -1.427 -19.244 -17.756 1.00 31.03 ? 45   GLU B C     1 
ATOM   364  O O     . GLU A 1 47  ? -1.757 -18.619 -18.770 1.00 29.17 ? 45   GLU B O     1 
ATOM   365  C CB    . GLU A 1 47  ? -1.983 -21.673 -17.589 1.00 38.63 ? 45   GLU B CB    1 
ATOM   366  C CG    . GLU A 1 47  ? -1.729 -23.075 -18.125 1.00 44.07 ? 45   GLU B CG    1 
ATOM   367  C CD    . GLU A 1 47  ? -1.606 -23.304 -19.635 1.00 45.80 ? 45   GLU B CD    1 
ATOM   368  O OE1   . GLU A 1 47  ? -1.090 -24.367 -19.988 1.00 46.81 ? 45   GLU B OE1   1 
ATOM   369  O OE2   . GLU A 1 47  ? -2.034 -22.449 -20.463 1.00 45.52 ? 45   GLU B OE2   1 
ATOM   370  N N     . GLU A 1 48  ? -1.560 -18.760 -16.519 1.00 33.11 ? 46   GLU B N     1 
ATOM   371  C CA    . GLU A 1 48  ? -2.105 -17.402 -16.240 1.00 34.01 ? 46   GLU B CA    1 
ATOM   372  C C     . GLU A 1 48  ? -1.173 -16.337 -16.823 1.00 30.05 ? 46   GLU B C     1 
ATOM   373  O O     . GLU A 1 48  ? -1.680 -15.356 -17.400 1.00 27.61 ? 46   GLU B O     1 
ATOM   374  C CB    . GLU A 1 48  ? -2.280 -17.141 -14.740 1.00 40.94 ? 46   GLU B CB    1 
ATOM   375  C CG    . GLU A 1 48  ? -3.533 -17.770 -14.159 1.00 50.29 ? 46   GLU B CG    1 
ATOM   376  C CD    . GLU A 1 48  ? -4.722 -17.655 -15.099 1.00 56.39 ? 46   GLU B CD    1 
ATOM   377  O OE1   . GLU A 1 48  ? -5.157 -18.712 -15.650 1.00 60.55 ? 46   GLU B OE1   1 
ATOM   378  O OE2   . GLU A 1 48  ? -5.158 -16.506 -15.333 1.00 53.80 ? 46   GLU B OE2   1 
ATOM   379  N N     . ALA A 1 49  ? 0.140  -16.499 -16.670 1.00 31.59 ? 47   ALA B N     1 
ATOM   380  C CA    . ALA A 1 49  ? 1.103  -15.490 -17.176 1.00 33.84 ? 47   ALA B CA    1 
ATOM   381  C C     . ALA A 1 49  ? 1.001  -15.450 -18.708 1.00 29.17 ? 47   ALA B C     1 
ATOM   382  O O     . ALA A 1 49  ? 0.964  -14.371 -19.265 1.00 28.99 ? 47   ALA B O     1 
ATOM   383  C CB    . ALA A 1 49  ? 2.502  -15.793 -16.706 1.00 34.41 ? 47   ALA B CB    1 
ATOM   384  N N     . GLY A 1 50  ? 0.868  -16.604 -19.344 1.00 29.38 ? 48   GLY B N     1 
ATOM   385  C CA    . GLY A 1 50  ? 0.711  -16.686 -20.813 1.00 32.22 ? 48   GLY B CA    1 
ATOM   386  C C     . GLY A 1 50  ? -0.525 -15.951 -21.316 1.00 32.29 ? 48   GLY B C     1 
ATOM   387  O O     . GLY A 1 50  ? -0.435 -15.289 -22.362 1.00 29.14 ? 48   GLY B O     1 
ATOM   388  N N     . LYS A 1 51  ? -1.650 -16.040 -20.599 1.00 33.78 ? 49   LYS B N     1 
ATOM   389  C CA    . LYS A 1 51  ? -2.905 -15.350 -20.992 1.00 33.98 ? 49   LYS B CA    1 
ATOM   390  C C     . LYS A 1 51  ? -2.719 -13.842 -20.913 1.00 29.80 ? 49   LYS B C     1 
ATOM   391  O O     . LYS A 1 51  ? -3.127 -13.157 -21.844 1.00 31.21 ? 49   LYS B O     1 
ATOM   392  C CB    . LYS A 1 51  ? -4.080 -15.684 -20.064 1.00 38.69 ? 49   LYS B CB    1 
ATOM   393  C CG    . LYS A 1 51  ? -4.785 -17.001 -20.343 1.00 45.72 ? 49   LYS B CG    1 
ATOM   394  C CD    . LYS A 1 51  ? -6.009 -17.221 -19.454 1.00 54.39 ? 49   LYS B CD    1 
ATOM   395  C CE    . LYS A 1 51  ? -6.563 -18.635 -19.521 1.00 60.17 ? 49   LYS B CE    1 
ATOM   396  N NZ    . LYS A 1 51  ? -5.511 -19.659 -19.305 1.00 61.56 ? 49   LYS B NZ    1 
ATOM   397  N N     . VAL A 1 52  ? -2.225 -13.328 -19.788 1.00 30.86 ? 50   VAL B N     1 
ATOM   398  C CA    . VAL A 1 52  ? -2.160 -11.853 -19.588 1.00 30.09 ? 50   VAL B CA    1 
ATOM   399  C C     . VAL A 1 52  ? -1.103 -11.252 -20.538 1.00 27.27 ? 50   VAL B C     1 
ATOM   400  O O     . VAL A 1 52  ? -1.320 -10.114 -21.003 1.00 30.18 ? 50   VAL B O     1 
ATOM   401  C CB    . VAL A 1 52  ? -1.919 -11.480 -18.110 1.00 33.50 ? 50   VAL B CB    1 
ATOM   402  C CG1   . VAL A 1 52  ? -0.538 -11.883 -17.621 1.00 35.00 ? 50   VAL B CG1   1 
ATOM   403  C CG2   . VAL A 1 52  ? -2.159 -9.998  -17.862 1.00 36.60 ? 50   VAL B CG2   1 
ATOM   404  N N     . THR A 1 53  ? 0.000  -11.953 -20.812 1.00 29.04 ? 51   THR B N     1 
ATOM   405  C CA    . THR A 1 53  ? 1.110  -11.388 -21.647 1.00 28.99 ? 51   THR B CA    1 
ATOM   406  C C     . THR A 1 53  ? 0.639  -11.337 -23.103 1.00 28.46 ? 51   THR B C     1 
ATOM   407  O O     . THR A 1 53  ? 0.836  -10.299 -23.754 1.00 31.25 ? 51   THR B O     1 
ATOM   408  C CB    . THR A 1 53  ? 2.428  -12.151 -21.478 1.00 25.00 ? 51   THR B CB    1 
ATOM   409  O OG1   . THR A 1 53  ? 2.181  -13.537 -21.710 1.00 29.30 ? 51   THR B OG1   1 
ATOM   410  C CG2   . THR A 1 53  ? 3.050  -11.976 -20.108 1.00 27.32 ? 51   THR B CG2   1 
ATOM   411  N N     . ALA A 1 54  ? 0.015  -12.416 -23.576 1.00 28.61 ? 52   ALA B N     1 
ATOM   412  C CA    . ALA A 1 54  ? -0.517 -12.521 -24.949 1.00 29.52 ? 52   ALA B CA    1 
ATOM   413  C C     . ALA A 1 54  ? -1.744 -11.618 -25.104 1.00 31.08 ? 52   ALA B C     1 
ATOM   414  O O     . ALA A 1 54  ? -1.850 -10.937 -26.146 1.00 33.15 ? 52   ALA B O     1 
ATOM   415  C CB    . ALA A 1 54  ? -0.838 -13.953 -25.259 1.00 31.73 ? 52   ALA B CB    1 
ATOM   416  N N     . GLY A 1 55  ? -2.630 -11.595 -24.099 1.00 30.55 ? 53   GLY B N     1 
ATOM   417  C CA    . GLY A 1 55  ? -3.939 -10.918 -24.186 1.00 29.53 ? 53   GLY B CA    1 
ATOM   418  C C     . GLY A 1 55  ? -3.863 -9.404  -24.034 1.00 29.41 ? 53   GLY B C     1 
ATOM   419  O O     . GLY A 1 55  ? -4.541 -8.706  -24.794 1.00 29.67 ? 53   GLY B O     1 
ATOM   420  N N     . THR A 1 56  ? -3.129 -8.880  -23.058 1.00 28.46 ? 54   THR B N     1 
ATOM   421  C CA    . THR A 1 56  ? -3.241 -7.442  -22.676 1.00 30.38 ? 54   THR B CA    1 
ATOM   422  C C     . THR A 1 56  ? -1.911 -6.694  -22.889 1.00 27.23 ? 54   THR B C     1 
ATOM   423  O O     . THR A 1 56  ? -1.991 -5.502  -23.203 1.00 29.16 ? 54   THR B O     1 
ATOM   424  C CB    . THR A 1 56  ? -3.844 -7.308  -21.267 1.00 34.17 ? 54   THR B CB    1 
ATOM   425  O OG1   . THR A 1 56  ? -2.830 -7.499  -20.293 1.00 47.79 ? 54   THR B OG1   1 
ATOM   426  C CG2   . THR A 1 56  ? -4.926 -8.322  -20.985 1.00 33.66 ? 54   THR B CG2   1 
ATOM   427  N N     . ILE A 1 57  ? -0.760 -7.354  -22.782 1.00 28.57 ? 55   ILE B N     1 
ATOM   428  C CA    . ILE A 1 57  ? 0.567  -6.659  -22.896 1.00 28.37 ? 55   ILE B CA    1 
ATOM   429  C C     . ILE A 1 57  ? 1.054  -6.624  -24.361 1.00 26.79 ? 55   ILE B C     1 
ATOM   430  O O     . ILE A 1 57  ? 1.388  -5.542  -24.847 1.00 26.26 ? 55   ILE B O     1 
ATOM   431  C CB    . ILE A 1 57  ? 1.608  -7.342  -21.984 1.00 29.04 ? 55   ILE B CB    1 
ATOM   432  C CG1   . ILE A 1 57  ? 1.119  -7.466  -20.538 1.00 32.48 ? 55   ILE B CG1   1 
ATOM   433  C CG2   . ILE A 1 57  ? 2.957  -6.647  -22.069 1.00 27.80 ? 55   ILE B CG2   1 
ATOM   434  C CD1   . ILE A 1 57  ? 0.612  -6.176  -19.960 1.00 34.16 ? 55   ILE B CD1   1 
ATOM   435  N N     . ALA A 1 58  ? 1.087  -7.779  -25.024 1.00 26.14 ? 56   ALA B N     1 
ATOM   436  C CA    . ALA A 1 58  ? 1.588  -7.890  -26.420 1.00 27.04 ? 56   ALA B CA    1 
ATOM   437  C C     . ALA A 1 58  ? 0.929  -6.900  -27.393 1.00 26.85 ? 56   ALA B C     1 
ATOM   438  O O     . ALA A 1 58  ? 1.655  -6.289  -28.175 1.00 27.14 ? 56   ALA B O     1 
ATOM   439  C CB    . ALA A 1 58  ? 1.432  -9.306  -26.887 1.00 27.19 ? 56   ALA B CB    1 
ATOM   440  N N     . PRO A 1 59  ? -0.410 -6.752  -27.409 1.00 28.48 ? 57   PRO B N     1 
ATOM   441  C CA    . PRO A 1 59  ? -1.071 -5.827  -28.329 1.00 27.83 ? 57   PRO B CA    1 
ATOM   442  C C     . PRO A 1 59  ? -0.624 -4.363  -28.211 1.00 26.81 ? 57   PRO B C     1 
ATOM   443  O O     . PRO A 1 59  ? -0.886 -3.610  -29.095 1.00 25.69 ? 57   PRO B O     1 
ATOM   444  C CB    . PRO A 1 59  ? -2.540 -5.919  -27.904 1.00 30.83 ? 57   PRO B CB    1 
ATOM   445  C CG    . PRO A 1 59  ? -2.669 -7.317  -27.358 1.00 30.08 ? 57   PRO B CG    1 
ATOM   446  C CD    . PRO A 1 59  ? -1.373 -7.513  -26.608 1.00 29.03 ? 57   PRO B CD    1 
ATOM   447  N N     . LEU A 1 60  ? 0.052  -4.024  -27.118 1.00 26.14 ? 58   LEU B N     1 
ATOM   448  C CA    . LEU A 1 60  ? 0.484  -2.622  -26.893 1.00 25.89 ? 58   LEU B CA    1 
ATOM   449  C C     . LEU A 1 60  ? 1.923  -2.392  -27.386 1.00 24.84 ? 58   LEU B C     1 
ATOM   450  O O     . LEU A 1 60  ? 2.341  -1.243  -27.440 1.00 26.05 ? 58   LEU B O     1 
ATOM   451  C CB    . LEU A 1 60  ? 0.398  -2.356  -25.389 1.00 29.19 ? 58   LEU B CB    1 
ATOM   452  C CG    . LEU A 1 60  ? -1.004 -2.222  -24.804 1.00 30.86 ? 58   LEU B CG    1 
ATOM   453  C CD1   . LEU A 1 60  ? -0.931 -2.113  -23.293 1.00 32.94 ? 58   LEU B CD1   1 
ATOM   454  C CD2   . LEU A 1 60  ? -1.714 -1.014  -25.385 1.00 30.31 ? 58   LEU B CD2   1 
ATOM   455  N N     . ASN A 1 61  ? 2.638  -3.452  -27.726 1.00 24.55 ? 59   ASN B N     1 
ATOM   456  C CA    . ASN A 1 61  ? 4.066  -3.306  -28.111 1.00 24.73 ? 59   ASN B CA    1 
ATOM   457  C C     . ASN A 1 61  ? 4.241  -2.333  -29.285 1.00 26.46 ? 59   ASN B C     1 
ATOM   458  O O     . ASN A 1 61  ? 4.912  -1.318  -29.114 1.00 24.16 ? 59   ASN B O     1 
ATOM   459  C CB    . ASN A 1 61  ? 4.704  -4.659  -28.413 1.00 25.34 ? 59   ASN B CB    1 
ATOM   460  C CG    . ASN A 1 61  ? 6.198  -4.661  -28.175 1.00 25.90 ? 59   ASN B CG    1 
ATOM   461  O OD1   . ASN A 1 61  ? 6.730  -3.746  -27.557 1.00 23.56 ? 59   ASN B OD1   1 
ATOM   462  N ND2   . ASN A 1 61  ? 6.875  -5.684  -28.665 1.00 25.82 ? 59   ASN B ND2   1 
ATOM   463  N N     . ARG A 1 62  ? 3.656  -2.648  -30.439 1.00 27.49 ? 60   ARG B N     1 
ATOM   464  C CA    . ARG A 1 62  ? 3.832  -1.783  -31.636 1.00 25.12 ? 60   ARG B CA    1 
ATOM   465  C C     . ARG A 1 62  ? 3.300  -0.368  -31.366 1.00 25.43 ? 60   ARG B C     1 
ATOM   466  O O     . ARG A 1 62  ? 4.041  0.575   -31.586 1.00 25.68 ? 60   ARG B O     1 
ATOM   467  C CB    . ARG A 1 62  ? 3.158  -2.394  -32.868 1.00 25.71 ? 60   ARG B CB    1 
ATOM   468  C CG    . ARG A 1 62  ? 3.920  -3.547  -33.502 1.00 25.80 ? 60   ARG B CG    1 
ATOM   469  C CD    . ARG A 1 62  ? 4.734  -3.066  -34.685 1.00 26.41 ? 60   ARG B CD    1 
ATOM   470  N NE    . ARG A 1 62  ? 5.840  -2.232  -34.248 1.00 26.53 ? 60   ARG B NE    1 
ATOM   471  C CZ    . ARG A 1 62  ? 6.019  -0.969  -34.602 1.00 26.77 ? 60   ARG B CZ    1 
ATOM   472  N NH1   . ARG A 1 62  ? 5.163  -0.379  -35.415 1.00 27.14 ? 60   ARG B NH1   1 
ATOM   473  N NH2   . ARG A 1 62  ? 7.056  -0.298  -34.139 1.00 28.07 ? 60   ARG B NH2   1 
ATOM   474  N N     . PRO A 1 63  ? 2.039  -0.167  -30.934 1.00 25.49 ? 61   PRO B N     1 
ATOM   475  C CA    . PRO A 1 63  ? 1.564  1.198   -30.735 1.00 26.56 ? 61   PRO B CA    1 
ATOM   476  C C     . PRO A 1 63  ? 2.381  1.948   -29.675 1.00 25.99 ? 61   PRO B C     1 
ATOM   477  O O     . PRO A 1 63  ? 2.505  3.154   -29.771 1.00 28.03 ? 61   PRO B O     1 
ATOM   478  C CB    . PRO A 1 63  ? 0.083  1.053   -30.304 1.00 28.85 ? 61   PRO B CB    1 
ATOM   479  C CG    . PRO A 1 63  ? -0.147 -0.442  -30.063 1.00 27.37 ? 61   PRO B CG    1 
ATOM   480  C CD    . PRO A 1 63  ? 1.001  -1.189  -30.699 1.00 27.81 ? 61   PRO B CD    1 
ATOM   481  N N     . GLY A 1 64  ? 2.894  1.239   -28.675 1.00 28.12 ? 62   GLY B N     1 
ATOM   482  C CA    . GLY A 1 64  ? 3.754  1.844   -27.630 1.00 30.33 ? 62   GLY B CA    1 
ATOM   483  C C     . GLY A 1 64  ? 5.023  2.425   -28.241 1.00 27.99 ? 62   GLY B C     1 
ATOM   484  O O     . GLY A 1 64  ? 5.365  3.592   -27.946 1.00 26.75 ? 62   GLY B O     1 
ATOM   485  N N     . ASP A 1 65  ? 5.663  1.655   -29.126 1.00 27.62 ? 63   ASP B N     1 
ATOM   486  C CA    . ASP A 1 65  ? 6.862  2.103   -29.890 1.00 25.49 ? 63   ASP B CA    1 
ATOM   487  C C     . ASP A 1 65  ? 6.485  3.330   -30.718 1.00 26.03 ? 63   ASP B C     1 
ATOM   488  O O     . ASP A 1 65  ? 7.285  4.297   -30.760 1.00 26.36 ? 63   ASP B O     1 
ATOM   489  C CB    . ASP A 1 65  ? 7.442  1.018   -30.800 1.00 25.85 ? 63   ASP B CB    1 
ATOM   490  C CG    . ASP A 1 65  ? 8.626  1.538   -31.618 1.00 24.98 ? 63   ASP B CG    1 
ATOM   491  O OD1   . ASP A 1 65  ? 9.719  1.656   -31.025 1.00 23.76 ? 63   ASP B OD1   1 
ATOM   492  O OD2   . ASP A 1 65  ? 8.443  1.881   -32.834 1.00 25.11 ? 63   ASP B OD2   1 
ATOM   493  N N     . GLU A 1 66  ? 5.327  3.306   -31.381 1.00 26.22 ? 64   GLU B N     1 
ATOM   494  C CA    . GLU A 1 66  ? 4.971  4.384   -32.342 1.00 28.03 ? 64   GLU B CA    1 
ATOM   495  C C     . GLU A 1 66  ? 4.621  5.668   -31.585 1.00 28.13 ? 64   GLU B C     1 
ATOM   496  O O     . GLU A 1 66  ? 4.925  6.751   -32.122 1.00 26.46 ? 64   GLU B O     1 
ATOM   497  C CB    . GLU A 1 66  ? 3.837  3.968   -33.274 1.00 29.21 ? 64   GLU B CB    1 
ATOM   498  C CG    . GLU A 1 66  ? 4.269  2.899   -34.266 1.00 30.38 ? 64   GLU B CG    1 
ATOM   499  C CD    . GLU A 1 66  ? 5.344  3.313   -35.255 1.00 28.79 ? 64   GLU B CD    1 
ATOM   500  O OE1   . GLU A 1 66  ? 6.090  2.418   -35.704 1.00 29.51 ? 64   GLU B OE1   1 
ATOM   501  O OE2   . GLU A 1 66  ? 5.423  4.525   -35.595 1.00 28.81 ? 64   GLU B OE2   1 
ATOM   502  N N     . GLU A 1 67  ? 4.041  5.564   -30.389 1.00 26.94 ? 65   GLU B N     1 
ATOM   503  C CA    . GLU A 1 67  ? 3.627  6.773   -29.626 1.00 27.32 ? 65   GLU B CA    1 
ATOM   504  C C     . GLU A 1 67  ? 4.801  7.251   -28.752 1.00 27.87 ? 65   GLU B C     1 
ATOM   505  O O     . GLU A 1 67  ? 5.047  8.466   -28.723 1.00 28.41 ? 65   GLU B O     1 
ATOM   506  C CB    . GLU A 1 67  ? 2.386  6.483   -28.773 1.00 30.05 ? 65   GLU B CB    1 
ATOM   507  C CG    . GLU A 1 67  ? 2.033  7.621   -27.810 1.00 33.11 ? 65   GLU B CG    1 
ATOM   508  C CD    . GLU A 1 67  ? 0.669  7.507   -27.127 1.00 36.59 ? 65   GLU B CD    1 
ATOM   509  O OE1   . GLU A 1 67  ? 0.158  8.540   -26.702 1.00 38.60 ? 65   GLU B OE1   1 
ATOM   510  O OE2   . GLU A 1 67  ? 0.114  6.390   -27.038 1.00 34.62 ? 65   GLU B OE2   1 
ATOM   511  N N     . GLY A 1 68  ? 5.478  6.338   -28.046 1.00 25.50 ? 66   GLY B N     1 
ATOM   512  C CA    . GLY A 1 68  ? 6.516  6.697   -27.058 1.00 29.65 ? 66   GLY B CA    1 
ATOM   513  C C     . GLY A 1 68  ? 5.941  7.455   -25.858 1.00 31.06 ? 66   GLY B C     1 
ATOM   514  O O     . GLY A 1 68  ? 4.719  7.646   -25.775 1.00 30.21 ? 66   GLY B O     1 
ATOM   515  N N     . CYS A 1 69  ? 6.798  7.854   -24.931 1.00 31.88 ? 67   CYS B N     1 
ATOM   516  C CA    . CYS A 1 69  ? 6.407  8.586   -23.706 1.00 30.88 ? 67   CYS B CA    1 
ATOM   517  C C     . CYS A 1 69  ? 6.420  10.077  -24.021 1.00 31.10 ? 67   CYS B C     1 
ATOM   518  O O     . CYS A 1 69  ? 7.062  10.431  -24.991 1.00 28.23 ? 67   CYS B O     1 
ATOM   519  C CB    . CYS A 1 69  ? 7.352  8.260   -22.568 1.00 28.26 ? 67   CYS B CB    1 
ATOM   520  S SG    . CYS A 1 69  ? 7.258  6.523   -22.099 1.00 29.60 ? 67   CYS B SG    1 
ATOM   521  N N     . GLN A 1 70  ? 5.709  10.891  -23.246 1.00 31.73 ? 68   GLN B N     1 
ATOM   522  C CA    . GLN A 1 70  ? 5.699  12.371  -23.397 1.00 34.38 ? 68   GLN B CA    1 
ATOM   523  C C     . GLN A 1 70  ? 6.058  13.005  -22.063 1.00 33.00 ? 68   GLN B C     1 
ATOM   524  O O     . GLN A 1 70  ? 5.685  12.449  -20.995 1.00 28.62 ? 68   GLN B O     1 
ATOM   525  C CB    . GLN A 1 70  ? 4.327  12.971  -23.720 1.00 38.86 ? 68   GLN B CB    1 
ATOM   526  C CG    . GLN A 1 70  ? 3.420  12.074  -24.526 1.00 45.02 ? 68   GLN B CG    1 
ATOM   527  C CD    . GLN A 1 70  ? 3.965  11.881  -25.915 1.00 54.52 ? 68   GLN B CD    1 
ATOM   528  O OE1   . GLN A 1 70  ? 4.538  12.803  -26.506 1.00 61.32 ? 68   GLN B OE1   1 
ATOM   529  N NE2   . GLN A 1 70  ? 3.798  10.671  -26.432 1.00 62.66 ? 68   GLN B NE2   1 
ATOM   530  N N     . TRP A 1 71  ? 6.672  14.175  -22.159 1.00 33.58 ? 69   TRP B N     1 
ATOM   531  C CA    . TRP A 1 71  ? 7.037  15.026  -21.012 1.00 33.74 ? 69   TRP B CA    1 
ATOM   532  C C     . TRP A 1 71  ? 6.227  16.318  -21.114 1.00 36.11 ? 69   TRP B C     1 
ATOM   533  O O     . TRP A 1 71  ? 6.276  16.964  -22.179 1.00 35.14 ? 69   TRP B O     1 
ATOM   534  C CB    . TRP A 1 71  ? 8.542  15.258  -21.040 1.00 32.44 ? 69   TRP B CB    1 
ATOM   535  C CG    . TRP A 1 71  ? 9.060  15.955  -19.830 1.00 32.19 ? 69   TRP B CG    1 
ATOM   536  C CD1   . TRP A 1 71  ? 9.562  15.383  -18.701 1.00 30.90 ? 69   TRP B CD1   1 
ATOM   537  C CD2   . TRP A 1 71  ? 9.143  17.377  -19.646 1.00 32.98 ? 69   TRP B CD2   1 
ATOM   538  N NE1   . TRP A 1 71  ? 9.954  16.361  -17.829 1.00 31.43 ? 69   TRP B NE1   1 
ATOM   539  C CE2   . TRP A 1 71  ? 9.723  17.590  -18.382 1.00 29.93 ? 69   TRP B CE2   1 
ATOM   540  C CE3   . TRP A 1 71  ? 8.774  18.483  -20.426 1.00 36.08 ? 69   TRP B CE3   1 
ATOM   541  C CZ2   . TRP A 1 71  ? 9.951  18.869  -17.877 1.00 33.92 ? 69   TRP B CZ2   1 
ATOM   542  C CZ3   . TRP A 1 71  ? 9.004  19.752  -19.931 1.00 36.87 ? 69   TRP B CZ3   1 
ATOM   543  C CH2   . TRP A 1 71  ? 9.577  19.937  -18.665 1.00 36.85 ? 69   TRP B CH2   1 
ATOM   544  N N     . ASN A 1 72  ? 5.452  16.647  -20.078 1.00 37.57 ? 70   ASN B N     1 
ATOM   545  C CA    . ASN A 1 72  ? 4.653  17.905  -20.033 1.00 41.15 ? 70   ASN B CA    1 
ATOM   546  C C     . ASN A 1 72  ? 4.860  18.525  -18.653 1.00 37.91 ? 70   ASN B C     1 
ATOM   547  O O     . ASN A 1 72  ? 4.401  17.912  -17.681 1.00 37.12 ? 70   ASN B O     1 
ATOM   548  C CB    . ASN A 1 72  ? 3.168  17.665  -20.317 1.00 43.73 ? 70   ASN B CB    1 
ATOM   549  C CG    . ASN A 1 72  ? 2.923  17.218  -21.741 1.00 50.63 ? 70   ASN B CG    1 
ATOM   550  O OD1   . ASN A 1 72  ? 3.084  18.005  -22.674 1.00 48.64 ? 70   ASN B OD1   1 
ATOM   551  N ND2   . ASN A 1 72  ? 2.554  15.954  -21.918 1.00 51.15 ? 70   ASN B ND2   1 
ATOM   552  N N     . ALA A 1 73  ? 5.616  19.622  -18.586 1.00 39.06 ? 71   ALA B N     1 
ATOM   553  C CA    . ALA A 1 73  ? 5.953  20.363  -17.349 1.00 40.58 ? 71   ALA B CA    1 
ATOM   554  C C     . ALA A 1 73  ? 6.272  19.378  -16.215 1.00 39.02 ? 71   ALA B C     1 
ATOM   555  O O     . ALA A 1 73  ? 5.751  19.563  -15.129 1.00 35.95 ? 71   ALA B O     1 
ATOM   556  C CB    . ALA A 1 73  ? 4.805  21.290  -16.998 1.00 41.73 ? 71   ALA B CB    1 
ATOM   557  N N     . GLY A 1 74  ? 7.085  18.349  -16.475 1.00 37.13 ? 72   GLY B N     1 
ATOM   558  C CA    . GLY A 1 74  ? 7.645  17.468  -15.437 1.00 34.01 ? 72   GLY B CA    1 
ATOM   559  C C     . GLY A 1 74  ? 6.851  16.184  -15.260 1.00 33.08 ? 72   GLY B C     1 
ATOM   560  O O     . GLY A 1 74  ? 7.369  15.254  -14.632 1.00 35.32 ? 72   GLY B O     1 
ATOM   561  N N     . ALA A 1 75  ? 5.628  16.128  -15.766 1.00 32.74 ? 73   ALA B N     1 
ATOM   562  C CA    . ALA A 1 75  ? 4.798  14.901  -15.766 1.00 35.33 ? 73   ALA B CA    1 
ATOM   563  C C     . ALA A 1 75  ? 5.151  14.064  -17.001 1.00 31.72 ? 73   ALA B C     1 
ATOM   564  O O     . ALA A 1 75  ? 5.170  14.616  -18.138 1.00 30.94 ? 73   ALA B O     1 
ATOM   565  C CB    . ALA A 1 75  ? 3.333  15.274  -15.768 1.00 36.09 ? 73   ALA B CB    1 
ATOM   566  N N     . VAL A 1 76  ? 5.424  12.785  -16.791 1.00 29.87 ? 74   VAL B N     1 
ATOM   567  C CA    . VAL A 1 76  ? 5.725  11.836  -17.896 1.00 30.11 ? 74   VAL B CA    1 
ATOM   568  C C     . VAL A 1 76  ? 4.509  10.932  -18.087 1.00 30.69 ? 74   VAL B C     1 
ATOM   569  O O     . VAL A 1 76  ? 4.049  10.326  -17.104 1.00 30.55 ? 74   VAL B O     1 
ATOM   570  C CB    . VAL A 1 76  ? 7.003  11.031  -17.614 1.00 29.82 ? 74   VAL B CB    1 
ATOM   571  C CG1   . VAL A 1 76  ? 7.209  9.919   -18.633 1.00 30.37 ? 74   VAL B CG1   1 
ATOM   572  C CG2   . VAL A 1 76  ? 8.217  11.950  -17.544 1.00 30.29 ? 74   VAL B CG2   1 
ATOM   573  N N     . SER A 1 77  ? 4.040  10.818  -19.326 1.00 29.51 ? 75   SER B N     1 
ATOM   574  C CA    . SER A 1 77  ? 2.900  9.940   -19.684 1.00 30.50 ? 75   SER B CA    1 
ATOM   575  C C     . SER A 1 77  ? 3.410  8.823   -20.588 1.00 29.48 ? 75   SER B C     1 
ATOM   576  O O     . SER A 1 77  ? 4.199  9.118   -21.496 1.00 33.29 ? 75   SER B O     1 
ATOM   577  C CB    . SER A 1 77  ? 1.778  10.734  -20.295 1.00 31.55 ? 75   SER B CB    1 
ATOM   578  O OG    . SER A 1 77  ? 2.214  11.361  -21.490 1.00 38.94 ? 75   SER B OG    1 
ATOM   579  N N     . THR A 1 78  ? 3.050  7.583   -20.253 1.00 29.57 ? 76   THR B N     1 
ATOM   580  C CA    . THR A 1 78  ? 3.317  6.373   -21.055 1.00 29.17 ? 76   THR B CA    1 
ATOM   581  C C     . THR A 1 78  ? 2.309  6.340   -22.202 1.00 28.08 ? 76   THR B C     1 
ATOM   582  O O     . THR A 1 78  ? 1.333  7.086   -22.223 1.00 29.02 ? 76   THR B O     1 
ATOM   583  C CB    . THR A 1 78  ? 3.336  5.133   -20.151 1.00 29.15 ? 76   THR B CB    1 
ATOM   584  O OG1   . THR A 1 78  ? 2.068  4.979   -19.496 1.00 27.60 ? 76   THR B OG1   1 
ATOM   585  C CG2   . THR A 1 78  ? 4.455  5.191   -19.132 1.00 28.74 ? 76   THR B CG2   1 
ATOM   586  N N     . PRO A 1 79  ? 2.508  5.473   -23.209 1.00 26.84 ? 77   PRO B N     1 
ATOM   587  C CA    . PRO A 1 79  ? 1.551  5.367   -24.315 1.00 26.74 ? 77   PRO B CA    1 
ATOM   588  C C     . PRO A 1 79  ? 0.150  4.960   -23.842 1.00 25.97 ? 77   PRO B C     1 
ATOM   589  O O     . PRO A 1 79  ? 0.049  4.426   -22.780 1.00 27.04 ? 77   PRO B O     1 
ATOM   590  C CB    . PRO A 1 79  ? 2.173  4.290   -25.221 1.00 25.58 ? 77   PRO B CB    1 
ATOM   591  C CG    . PRO A 1 79  ? 3.656  4.353   -24.860 1.00 26.59 ? 77   PRO B CG    1 
ATOM   592  C CD    . PRO A 1 79  ? 3.682  4.607   -23.372 1.00 24.54 ? 77   PRO B CD    1 
ATOM   593  N N     . ALA A 1 80  ? -0.868 5.245   -24.659 1.00 29.32 ? 78   ALA B N     1 
ATOM   594  C CA    . ALA A 1 80  ? -2.279 4.824   -24.494 1.00 28.31 ? 78   ALA B CA    1 
ATOM   595  C C     . ALA A 1 80  ? -2.341 3.352   -24.084 1.00 28.10 ? 78   ALA B C     1 
ATOM   596  O O     . ALA A 1 80  ? -1.600 2.542   -24.664 1.00 26.70 ? 78   ALA B O     1 
ATOM   597  C CB    . ALA A 1 80  ? -3.041 5.103   -25.770 1.00 31.29 ? 78   ALA B CB    1 
ATOM   598  N N     . GLY A 1 81  ? -3.119 3.029   -23.038 1.00 26.44 ? 79   GLY B N     1 
ATOM   599  C CA    . GLY A 1 81  ? -3.318 1.637   -22.594 1.00 28.18 ? 79   GLY B CA    1 
ATOM   600  C C     . GLY A 1 81  ? -2.281 1.126   -21.590 1.00 27.94 ? 79   GLY B C     1 
ATOM   601  O O     . GLY A 1 81  ? -2.573 0.092   -20.912 1.00 30.04 ? 79   GLY B O     1 
ATOM   602  N N     . PHE A 1 82  ? -1.094 1.748   -21.478 1.00 26.66 ? 80   PHE B N     1 
ATOM   603  C CA    . PHE A 1 82  ? -0.044 1.247   -20.548 1.00 25.89 ? 80   PHE B CA    1 
ATOM   604  C C     . PHE A 1 82  ? -0.530 1.329   -19.097 1.00 24.17 ? 80   PHE B C     1 
ATOM   605  O O     . PHE A 1 82  ? -0.362 0.365   -18.370 1.00 24.06 ? 80   PHE B O     1 
ATOM   606  C CB    . PHE A 1 82  ? 1.311  1.929   -20.776 1.00 26.80 ? 80   PHE B CB    1 
ATOM   607  C CG    . PHE A 1 82  ? 2.134  1.296   -21.868 1.00 26.81 ? 80   PHE B CG    1 
ATOM   608  C CD1   . PHE A 1 82  ? 1.694  1.313   -23.184 1.00 28.09 ? 80   PHE B CD1   1 
ATOM   609  C CD2   . PHE A 1 82  ? 3.347  0.684   -21.589 1.00 29.32 ? 80   PHE B CD2   1 
ATOM   610  C CE1   . PHE A 1 82  ? 2.448  0.720   -24.193 1.00 32.21 ? 80   PHE B CE1   1 
ATOM   611  C CE2   . PHE A 1 82  ? 4.105  0.098   -22.601 1.00 27.63 ? 80   PHE B CE2   1 
ATOM   612  C CZ    . PHE A 1 82  ? 3.658  0.120   -23.898 1.00 28.49 ? 80   PHE B CZ    1 
ATOM   613  N N     . PRO A 1 83  ? -1.100 2.449   -18.590 1.00 24.28 ? 81   PRO B N     1 
ATOM   614  C CA    . PRO A 1 83  ? -1.557 2.487   -17.196 1.00 27.51 ? 81   PRO B CA    1 
ATOM   615  C C     . PRO A 1 83  ? -2.593 1.394   -16.888 1.00 27.15 ? 81   PRO B C     1 
ATOM   616  O O     . PRO A 1 83  ? -2.442 0.707   -15.905 1.00 29.51 ? 81   PRO B O     1 
ATOM   617  C CB    . PRO A 1 83  ? -2.124 3.901   -17.026 1.00 27.69 ? 81   PRO B CB    1 
ATOM   618  C CG    . PRO A 1 83  ? -1.402 4.721   -18.119 1.00 26.67 ? 81   PRO B CG    1 
ATOM   619  C CD    . PRO A 1 83  ? -1.242 3.749   -19.262 1.00 26.17 ? 81   PRO B CD    1 
ATOM   620  N N     . GLU A 1 84  ? -3.561 1.196   -17.778 1.00 28.89 ? 82   GLU B N     1 
ATOM   621  C CA    . GLU A 1 84  ? -4.668 0.224   -17.574 1.00 29.12 ? 82   GLU B CA    1 
ATOM   622  C C     . GLU A 1 84  ? -4.061 -1.170  -17.587 1.00 27.13 ? 82   GLU B C     1 
ATOM   623  O O     . GLU A 1 84  ? -4.402 -1.988  -16.726 1.00 24.96 ? 82   GLU B O     1 
ATOM   624  C CB    . GLU A 1 84  ? -5.739 0.348   -18.667 1.00 34.87 ? 82   GLU B CB    1 
ATOM   625  C CG    . GLU A 1 84  ? -6.479 1.679   -18.665 1.00 38.49 ? 82   GLU B CG    1 
ATOM   626  C CD    . GLU A 1 84  ? -5.758 2.909   -19.209 1.00 45.24 ? 82   GLU B CD    1 
ATOM   627  O OE1   . GLU A 1 84  ? -6.291 4.017   -18.978 1.00 47.41 ? 82   GLU B OE1   1 
ATOM   628  O OE2   . GLU A 1 84  ? -4.650 2.784   -19.844 1.00 39.00 ? 82   GLU B OE2   1 
ATOM   629  N N     . ALA A 1 85  ? -3.154 -1.446  -18.528 1.00 28.12 ? 83   ALA B N     1 
ATOM   630  C CA    . ALA A 1 85  ? -2.539 -2.790  -18.638 1.00 26.87 ? 83   ALA B CA    1 
ATOM   631  C C     . ALA A 1 85  ? -1.656 -3.045  -17.406 1.00 26.24 ? 83   ALA B C     1 
ATOM   632  O O     . ALA A 1 85  ? -1.617 -4.180  -16.923 1.00 26.99 ? 83   ALA B O     1 
ATOM   633  C CB    . ALA A 1 85  ? -1.744 -2.902  -19.917 1.00 29.24 ? 83   ALA B CB    1 
ATOM   634  N N     . TYR A 1 86  ? -0.938 -2.030  -16.936 1.00 24.79 ? 84   TYR B N     1 
ATOM   635  C CA    . TYR A 1 86  ? -0.102 -2.132  -15.717 1.00 26.26 ? 84   TYR B CA    1 
ATOM   636  C C     . TYR A 1 86  ? -0.989 -2.444  -14.490 1.00 27.04 ? 84   TYR B C     1 
ATOM   637  O O     . TYR A 1 86  ? -0.616 -3.312  -13.651 1.00 25.56 ? 84   TYR B O     1 
ATOM   638  C CB    . TYR A 1 86  ? 0.724  -0.855  -15.499 1.00 25.97 ? 84   TYR B CB    1 
ATOM   639  C CG    . TYR A 1 86  ? 1.564  -0.995  -14.261 1.00 25.83 ? 84   TYR B CG    1 
ATOM   640  C CD1   . TYR A 1 86  ? 2.767  -1.682  -14.278 1.00 27.13 ? 84   TYR B CD1   1 
ATOM   641  C CD2   . TYR A 1 86  ? 1.076  -0.573  -13.034 1.00 27.39 ? 84   TYR B CD2   1 
ATOM   642  C CE1   . TYR A 1 86  ? 3.493  -1.884  -13.111 1.00 28.49 ? 84   TYR B CE1   1 
ATOM   643  C CE2   . TYR A 1 86  ? 1.767  -0.795  -11.857 1.00 26.75 ? 84   TYR B CE2   1 
ATOM   644  C CZ    . TYR A 1 86  ? 2.988  -1.437  -11.895 1.00 27.83 ? 84   TYR B CZ    1 
ATOM   645  O OH    . TYR A 1 86  ? 3.647  -1.650  -10.727 1.00 25.77 ? 84   TYR B OH    1 
ATOM   646  N N     . ARG A 1 87  ? -2.105 -1.716  -14.348 1.00 28.52 ? 85   ARG B N     1 
ATOM   647  C CA    . ARG A 1 87  ? -3.096 -1.954  -13.254 1.00 31.99 ? 85   ARG B CA    1 
ATOM   648  C C     . ARG A 1 87  ? -3.493 -3.440  -13.285 1.00 29.50 ? 85   ARG B C     1 
ATOM   649  O O     . ARG A 1 87  ? -3.348 -4.102  -12.269 1.00 29.72 ? 85   ARG B O     1 
ATOM   650  C CB    . ARG A 1 87  ? -4.281 -0.979  -13.353 1.00 35.36 ? 85   ARG B CB    1 
ATOM   651  C CG    . ARG A 1 87  ? -5.155 -0.931  -12.098 1.00 44.95 ? 85   ARG B CG    1 
ATOM   652  C CD    . ARG A 1 87  ? -6.369 -0.008  -12.140 1.00 51.46 ? 85   ARG B CD    1 
ATOM   653  N NE    . ARG A 1 87  ? -6.139 1.180   -12.960 1.00 59.89 ? 85   ARG B NE    1 
ATOM   654  C CZ    . ARG A 1 87  ? -6.717 1.446   -14.143 1.00 69.77 ? 85   ARG B CZ    1 
ATOM   655  N NH1   . ARG A 1 87  ? -7.612 0.625   -14.675 1.00 68.34 ? 85   ARG B NH1   1 
ATOM   656  N NH2   . ARG A 1 87  ? -6.390 2.553   -14.795 1.00 70.34 ? 85   ARG B NH2   1 
ATOM   657  N N     . THR A 1 88  ? -3.961 -3.955  -14.423 1.00 31.74 ? 86   THR B N     1 
ATOM   658  C CA    . THR A 1 88  ? -4.355 -5.390  -14.586 1.00 30.21 ? 86   THR B CA    1 
ATOM   659  C C     . THR A 1 88  ? -3.180 -6.266  -14.145 1.00 29.53 ? 86   THR B C     1 
ATOM   660  O O     . THR A 1 88  ? -3.363 -7.188  -13.341 1.00 30.64 ? 86   THR B O     1 
ATOM   661  C CB    . THR A 1 88  ? -4.761 -5.679  -16.037 1.00 30.99 ? 86   THR B CB    1 
ATOM   662  O OG1   . THR A 1 88  ? -5.822 -4.800  -16.398 1.00 31.95 ? 86   THR B OG1   1 
ATOM   663  C CG2   . THR A 1 88  ? -5.194 -7.107  -16.287 1.00 34.55 ? 86   THR B CG2   1 
ATOM   664  N N     . TYR A 1 89  ? -1.989 -6.001  -14.674 1.00 27.56 ? 87   TYR B N     1 
ATOM   665  C CA    . TYR A 1 89  ? -0.794 -6.838  -14.391 1.00 28.02 ? 87   TYR B CA    1 
ATOM   666  C C     . TYR A 1 89  ? -0.529 -6.880  -12.872 1.00 25.57 ? 87   TYR B C     1 
ATOM   667  O O     . TYR A 1 89  ? -0.310 -7.960  -12.300 1.00 26.92 ? 87   TYR B O     1 
ATOM   668  C CB    . TYR A 1 89  ? 0.396  -6.291  -15.179 1.00 26.99 ? 87   TYR B CB    1 
ATOM   669  C CG    . TYR A 1 89  ? 1.629  -7.148  -15.199 1.00 27.15 ? 87   TYR B CG    1 
ATOM   670  C CD1   . TYR A 1 89  ? 1.701  -8.274  -16.013 1.00 29.71 ? 87   TYR B CD1   1 
ATOM   671  C CD2   . TYR A 1 89  ? 2.760  -6.789  -14.494 1.00 27.82 ? 87   TYR B CD2   1 
ATOM   672  C CE1   . TYR A 1 89  ? 2.852  -9.039  -16.096 1.00 29.54 ? 87   TYR B CE1   1 
ATOM   673  C CE2   . TYR A 1 89  ? 3.928  -7.540  -14.568 1.00 29.45 ? 87   TYR B CE2   1 
ATOM   674  C CZ    . TYR A 1 89  ? 3.970  -8.678  -15.358 1.00 31.58 ? 87   TYR B CZ    1 
ATOM   675  O OH    . TYR A 1 89  ? 5.106  -9.445  -15.431 1.00 33.83 ? 87   TYR B OH    1 
ATOM   676  N N     . ALA A 1 90  ? -0.505 -5.713  -12.242 1.00 26.41 ? 88   ALA B N     1 
ATOM   677  C CA    . ALA A 1 90  ? -0.177 -5.528  -10.804 1.00 28.74 ? 88   ALA B CA    1 
ATOM   678  C C     . ALA A 1 90  ? -1.239 -6.219  -9.929  1.00 29.61 ? 88   ALA B C     1 
ATOM   679  O O     . ALA A 1 90  ? -0.862 -6.979  -9.027  1.00 30.14 ? 88   ALA B O     1 
ATOM   680  C CB    . ALA A 1 90  ? -0.071 -4.047  -10.497 1.00 27.58 ? 88   ALA B CB    1 
ATOM   681  N N     . GLU A 1 91  ? -2.514 -6.022  -10.246 1.00 32.06 ? 89   GLU B N     1 
ATOM   682  C CA    . GLU A 1 91  ? -3.672 -6.625  -9.519  1.00 32.40 ? 89   GLU B CA    1 
ATOM   683  C C     . GLU A 1 91  ? -3.649 -8.153  -9.662  1.00 31.43 ? 89   GLU B C     1 
ATOM   684  O O     . GLU A 1 91  ? -4.208 -8.829  -8.803  1.00 31.83 ? 89   GLU B O     1 
ATOM   685  C CB    . GLU A 1 91  ? -4.988 -6.040  -10.051 1.00 35.41 ? 89   GLU B CB    1 
ATOM   686  C CG    . GLU A 1 91  ? -5.196 -4.562  -9.690  1.00 41.11 ? 89   GLU B CG    1 
ATOM   687  C CD    . GLU A 1 91  ? -6.487 -3.895  -10.191 1.00 45.11 ? 89   GLU B CD    1 
ATOM   688  O OE1   . GLU A 1 91  ? -6.748 -2.722  -9.790  1.00 41.00 ? 89   GLU B OE1   1 
ATOM   689  O OE2   . GLU A 1 91  ? -7.223 -4.529  -11.002 1.00 49.44 ? 89   GLU B OE2   1 
ATOM   690  N N     . GLY A 1 92  ? -3.008 -8.694  -10.702 1.00 31.17 ? 90   GLY B N     1 
ATOM   691  C CA    . GLY A 1 92  ? -2.830 -10.148 -10.879 1.00 29.37 ? 90   GLY B CA    1 
ATOM   692  C C     . GLY A 1 92  ? -1.707 -10.729 -10.037 1.00 30.75 ? 90   GLY B C     1 
ATOM   693  O O     . GLY A 1 92  ? -1.552 -11.970 -10.051 1.00 32.41 ? 90   GLY B O     1 
ATOM   694  N N     . GLY A 1 93  ? -0.914 -9.892  -9.354  1.00 31.42 ? 91   GLY B N     1 
ATOM   695  C CA    . GLY A 1 93  ? 0.213  -10.320 -8.505  1.00 31.92 ? 91   GLY B CA    1 
ATOM   696  C C     . GLY A 1 93  ? 1.521  -10.461 -9.283  1.00 31.73 ? 91   GLY B C     1 
ATOM   697  O O     . GLY A 1 93  ? 2.496  -10.976 -8.718  1.00 30.73 ? 91   GLY B O     1 
ATOM   698  N N     . TRP A 1 94  ? 1.573  -10.035 -10.540 1.00 30.47 ? 92   TRP B N     1 
ATOM   699  C CA    . TRP A 1 94  ? 2.745  -10.368 -11.400 1.00 28.99 ? 92   TRP B CA    1 
ATOM   700  C C     . TRP A 1 94  ? 3.981  -9.535  -11.025 1.00 29.97 ? 92   TRP B C     1 
ATOM   701  O O     . TRP A 1 94  ? 5.128  -9.991  -11.279 1.00 31.67 ? 92   TRP B O     1 
ATOM   702  C CB    . TRP A 1 94  ? 2.347  -10.229 -12.870 1.00 28.04 ? 92   TRP B CB    1 
ATOM   703  C CG    . TRP A 1 94  ? 1.248  -11.181 -13.210 1.00 28.29 ? 92   TRP B CG    1 
ATOM   704  C CD1   . TRP A 1 94  ? -0.027 -10.881 -13.574 1.00 27.70 ? 92   TRP B CD1   1 
ATOM   705  C CD2   . TRP A 1 94  ? 1.330  -12.614 -13.151 1.00 27.53 ? 92   TRP B CD2   1 
ATOM   706  N NE1   . TRP A 1 94  ? -0.741 -12.032 -13.751 1.00 29.22 ? 92   TRP B NE1   1 
ATOM   707  C CE2   . TRP A 1 94  ? 0.064  -13.109 -13.499 1.00 28.74 ? 92   TRP B CE2   1 
ATOM   708  C CE3   . TRP A 1 94  ? 2.351  -13.514 -12.845 1.00 28.78 ? 92   TRP B CE3   1 
ATOM   709  C CZ2   . TRP A 1 94  ? -0.204 -14.472 -13.562 1.00 32.45 ? 92   TRP B CZ2   1 
ATOM   710  C CZ3   . TRP A 1 94  ? 2.086  -14.863 -12.899 1.00 31.43 ? 92   TRP B CZ3   1 
ATOM   711  C CH2   . TRP A 1 94  ? 0.820  -15.335 -13.241 1.00 31.77 ? 92   TRP B CH2   1 
ATOM   712  N N     . VAL A 1 95  ? 3.791  -8.350  -10.449 1.00 28.73 ? 93   VAL B N     1 
ATOM   713  C CA    . VAL A 1 95  ? 4.930  -7.484  -10.029 1.00 30.61 ? 93   VAL B CA    1 
ATOM   714  C C     . VAL A 1 95  ? 5.671  -8.139  -8.852  1.00 31.87 ? 93   VAL B C     1 
ATOM   715  O O     . VAL A 1 95  ? 6.878  -7.882  -8.736  1.00 36.49 ? 93   VAL B O     1 
ATOM   716  C CB    . VAL A 1 95  ? 4.496  -6.049  -9.684  1.00 29.36 ? 93   VAL B CB    1 
ATOM   717  C CG1   . VAL A 1 95  ? 5.715  -5.168  -9.453  1.00 31.68 ? 93   VAL B CG1   1 
ATOM   718  C CG2   . VAL A 1 95  ? 3.603  -5.461  -10.753 1.00 30.34 ? 93   VAL B CG2   1 
ATOM   719  N N     . GLY A 1 96  ? 4.998  -8.961  -8.028  1.00 29.52 ? 94   GLY B N     1 
ATOM   720  C CA    . GLY A 1 96  ? 5.601  -9.576  -6.833  1.00 30.53 ? 94   GLY B CA    1 
ATOM   721  C C     . GLY A 1 96  ? 5.739  -11.083 -6.942  1.00 31.39 ? 94   GLY B C     1 
ATOM   722  O O     . GLY A 1 96  ? 5.947  -11.730 -5.917  1.00 28.89 ? 94   GLY B O     1 
ATOM   723  N N     . VAL A 1 97  ? 5.694  -11.638 -8.144  1.00 30.80 ? 95   VAL B N     1 
ATOM   724  C CA    . VAL A 1 97  ? 5.673  -13.118 -8.345  1.00 31.75 ? 95   VAL B CA    1 
ATOM   725  C C     . VAL A 1 97  ? 6.882  -13.769 -7.657  1.00 30.02 ? 95   VAL B C     1 
ATOM   726  O O     . VAL A 1 97  ? 6.710  -14.868 -7.135  1.00 29.88 ? 95   VAL B O     1 
ATOM   727  C CB    . VAL A 1 97  ? 5.624  -13.482 -9.850  1.00 35.20 ? 95   VAL B CB    1 
ATOM   728  C CG1   . VAL A 1 97  ? 6.911  -13.117 -10.560 1.00 35.59 ? 95   VAL B CG1   1 
ATOM   729  C CG2   . VAL A 1 97  ? 5.309  -14.958 -10.057 1.00 36.10 ? 95   VAL B CG2   1 
ATOM   730  N N     . GLY A 1 98  ? 8.068  -13.141 -7.707  1.00 29.18 ? 96   GLY B N     1 
ATOM   731  C CA    . GLY A 1 98  ? 9.311  -13.658 -7.099  1.00 29.41 ? 96   GLY B CA    1 
ATOM   732  C C     . GLY A 1 98  ? 9.618  -12.997 -5.759  1.00 29.29 ? 96   GLY B C     1 
ATOM   733  O O     . GLY A 1 98  ? 10.683 -13.243 -5.245  1.00 29.44 ? 96   GLY B O     1 
ATOM   734  N N     . GLY A 1 99  ? 8.730  -12.146 -5.235  1.00 28.74 ? 97   GLY B N     1 
ATOM   735  C CA    . GLY A 1 99  ? 8.981  -11.359 -4.013  1.00 29.04 ? 97   GLY B CA    1 
ATOM   736  C C     . GLY A 1 99  ? 8.773  -12.169 -2.738  1.00 31.66 ? 97   GLY B C     1 
ATOM   737  O O     . GLY A 1 99  ? 8.207  -13.296 -2.808  1.00 29.57 ? 97   GLY B O     1 
ATOM   738  N N     . ASP A 1 100 ? 9.194  -11.596 -1.605  1.00 31.19 ? 98   ASP B N     1 
ATOM   739  C CA    . ASP A 1 100 ? 9.169  -12.218 -0.248  1.00 32.85 ? 98   ASP B CA    1 
ATOM   740  C C     . ASP A 1 100 ? 7.739  -12.310 0.290   1.00 29.11 ? 98   ASP B C     1 
ATOM   741  O O     . ASP A 1 100 ? 7.053  -11.299 0.521   1.00 28.67 ? 98   ASP B O     1 
ATOM   742  C CB    . ASP A 1 100 ? 10.034 -11.420 0.716   1.00 33.25 ? 98   ASP B CB    1 
ATOM   743  C CG    . ASP A 1 100 ? 10.335 -12.107 2.037   1.00 34.67 ? 98   ASP B CG    1 
ATOM   744  O OD1   . ASP A 1 100 ? 9.586  -13.015 2.434   1.00 34.09 ? 98   ASP B OD1   1 
ATOM   745  O OD2   . ASP A 1 100 ? 11.337 -11.725 2.643   1.00 35.87 ? 98   ASP B OD2   1 
ATOM   746  N N     . PRO A 1 101 ? 7.224  -13.534 0.516   1.00 29.75 ? 99   PRO B N     1 
ATOM   747  C CA    . PRO A 1 101 ? 5.863  -13.690 1.051   1.00 31.59 ? 99   PRO B CA    1 
ATOM   748  C C     . PRO A 1 101 ? 5.645  -13.030 2.425   1.00 33.02 ? 99   PRO B C     1 
ATOM   749  O O     . PRO A 1 101 ? 4.513  -12.866 2.813   1.00 38.77 ? 99   PRO B O     1 
ATOM   750  C CB    . PRO A 1 101 ? 5.694  -15.215 1.177   1.00 32.47 ? 99   PRO B CB    1 
ATOM   751  C CG    . PRO A 1 101 ? 6.727  -15.795 0.222   1.00 33.63 ? 99   PRO B CG    1 
ATOM   752  C CD    . PRO A 1 101 ? 7.880  -14.821 0.245   1.00 30.02 ? 99   PRO B CD    1 
ATOM   753  N N     . ALA A 1 102 ? 6.711  -12.695 3.143   1.00 33.80 ? 100  ALA B N     1 
ATOM   754  C CA    . ALA A 1 102 ? 6.616  -12.007 4.455   1.00 36.27 ? 100  ALA B CA    1 
ATOM   755  C C     . ALA A 1 102 ? 6.026  -10.603 4.259   1.00 37.54 ? 100  ALA B C     1 
ATOM   756  O O     . ALA A 1 102 ? 5.486  -10.075 5.242   1.00 35.51 ? 100  ALA B O     1 
ATOM   757  C CB    . ALA A 1 102 ? 7.959  -11.963 5.123   1.00 36.33 ? 100  ALA B CB    1 
ATOM   758  N N     . TYR A 1 103 ? 6.096  -10.025 3.048   1.00 36.60 ? 101  TYR B N     1 
ATOM   759  C CA    . TYR A 1 103 ? 5.540  -8.678  2.730   1.00 34.92 ? 101  TYR B CA    1 
ATOM   760  C C     . TYR A 1 103 ? 4.543  -8.759  1.568   1.00 36.70 ? 101  TYR B C     1 
ATOM   761  O O     . TYR A 1 103 ? 4.215  -7.696  0.988   1.00 40.46 ? 101  TYR B O     1 
ATOM   762  C CB    . TYR A 1 103 ? 6.665  -7.680  2.456   1.00 33.37 ? 101  TYR B CB    1 
ATOM   763  C CG    . TYR A 1 103 ? 7.765  -7.690  3.476   1.00 33.19 ? 101  TYR B CG    1 
ATOM   764  C CD1   . TYR A 1 103 ? 8.805  -8.586  3.366   1.00 32.01 ? 101  TYR B CD1   1 
ATOM   765  C CD2   . TYR A 1 103 ? 7.774  -6.820  4.565   1.00 36.97 ? 101  TYR B CD2   1 
ATOM   766  C CE1   . TYR A 1 103 ? 9.842  -8.606  4.279   1.00 32.98 ? 101  TYR B CE1   1 
ATOM   767  C CE2   . TYR A 1 103 ? 8.799  -6.842  5.503   1.00 32.42 ? 101  TYR B CE2   1 
ATOM   768  C CZ    . TYR A 1 103 ? 9.829  -7.751  5.367   1.00 35.79 ? 101  TYR B CZ    1 
ATOM   769  O OH    . TYR A 1 103 ? 10.858 -7.823  6.268   1.00 37.99 ? 101  TYR B OH    1 
ATOM   770  N N     . GLY A 1 104 ? 4.024  -9.962  1.289   1.00 31.42 ? 102  GLY B N     1 
ATOM   771  C CA    . GLY A 1 104 ? 2.920  -10.195 0.346   1.00 30.91 ? 102  GLY B CA    1 
ATOM   772  C C     . GLY A 1 104 ? 3.378  -10.573 -1.068  1.00 32.13 ? 102  GLY B C     1 
ATOM   773  O O     . GLY A 1 104 ? 2.521  -10.616 -1.952  1.00 30.38 ? 102  GLY B O     1 
ATOM   774  N N     . GLY A 1 105 ? 4.667  -10.826 -1.293  1.00 32.06 ? 103  GLY B N     1 
ATOM   775  C CA    . GLY A 1 105 ? 5.142  -11.379 -2.574  1.00 32.13 ? 103  GLY B CA    1 
ATOM   776  C C     . GLY A 1 105 ? 4.694  -12.820 -2.684  1.00 33.02 ? 103  GLY B C     1 
ATOM   777  O O     . GLY A 1 105 ? 4.371  -13.405 -1.638  1.00 30.98 ? 103  GLY B O     1 
ATOM   778  N N     . MET A 1 106 ? 4.701  -13.395 -3.882  1.00 32.88 ? 104  MET B N     1 
ATOM   779  C CA    . MET A 1 106 ? 4.198  -14.777 -4.114  1.00 33.73 ? 104  MET B CA    1 
ATOM   780  C C     . MET A 1 106 ? 5.258  -15.799 -3.715  1.00 31.14 ? 104  MET B C     1 
ATOM   781  O O     . MET A 1 106 ? 4.916  -16.982 -3.557  1.00 35.48 ? 104  MET B O     1 
ATOM   782  C CB    . MET A 1 106 ? 3.843  -14.957 -5.587  1.00 39.71 ? 104  MET B CB    1 
ATOM   783  C CG    . MET A 1 106 ? 2.682  -15.892 -5.854  1.00 47.62 ? 104  MET B CG    1 
ATOM   784  S SD    . MET A 1 106 ? 2.366  -15.946 -7.658  1.00 55.43 ? 104  MET B SD    1 
ATOM   785  C CE    . MET A 1 106 ? 1.972  -14.230 -8.014  1.00 48.49 ? 104  MET B CE    1 
ATOM   786  N N     . GLY A 1 107 ? 6.517  -15.382 -3.612  1.00 27.81 ? 105  GLY B N     1 
ATOM   787  C CA    . GLY A 1 107 ? 7.627  -16.259 -3.200  1.00 28.55 ? 105  GLY B CA    1 
ATOM   788  C C     . GLY A 1 107 ? 8.002  -17.327 -4.214  1.00 28.96 ? 105  GLY B C     1 
ATOM   789  O O     . GLY A 1 107 ? 8.596  -18.332 -3.793  1.00 27.56 ? 105  GLY B O     1 
ATOM   790  N N     . MET A 1 108 ? 7.714  -17.139 -5.505  1.00 29.23 ? 106  MET B N     1 
ATOM   791  C CA    . MET A 1 108 ? 8.101  -18.149 -6.525  1.00 30.84 ? 106  MET B CA    1 
ATOM   792  C C     . MET A 1 108 ? 9.624  -18.180 -6.630  1.00 27.74 ? 106  MET B C     1 
ATOM   793  O O     . MET A 1 108 ? 10.276 -17.154 -6.539  1.00 24.84 ? 106  MET B O     1 
ATOM   794  C CB    . MET A 1 108 ? 7.501  -17.842 -7.897  1.00 31.82 ? 106  MET B CB    1 
ATOM   795  C CG    . MET A 1 108 ? 6.023  -18.137 -7.996  1.00 34.35 ? 106  MET B CG    1 
ATOM   796  S SD    . MET A 1 108 ? 5.611  -19.864 -7.615  1.00 36.37 ? 106  MET B SD    1 
ATOM   797  C CE    . MET A 1 108 ? 4.703  -19.640 -6.088  1.00 37.58 ? 106  MET B CE    1 
ATOM   798  N N     . PRO A 1 109 ? 10.246 -19.358 -6.815  1.00 26.84 ? 107  PRO B N     1 
ATOM   799  C CA    . PRO A 1 109 ? 11.681 -19.427 -7.053  1.00 27.35 ? 107  PRO B CA    1 
ATOM   800  C C     . PRO A 1 109 ? 12.029 -18.790 -8.417  1.00 27.09 ? 107  PRO B C     1 
ATOM   801  O O     . PRO A 1 109 ? 11.135 -18.555 -9.237  1.00 25.59 ? 107  PRO B O     1 
ATOM   802  C CB    . PRO A 1 109 ? 11.953 -20.937 -7.000  1.00 28.31 ? 107  PRO B CB    1 
ATOM   803  C CG    . PRO A 1 109 ? 10.680 -21.551 -7.521  1.00 29.28 ? 107  PRO B CG    1 
ATOM   804  C CD    . PRO A 1 109 ? 9.593  -20.666 -6.953  1.00 29.74 ? 107  PRO B CD    1 
ATOM   805  N N     . LYS A 1 110 ? 13.316 -18.505 -8.611  1.00 27.45 ? 108  LYS B N     1 
ATOM   806  C CA    . LYS A 1 110 ? 13.840 -17.749 -9.771  1.00 29.05 ? 108  LYS B CA    1 
ATOM   807  C C     . LYS A 1 110 ? 13.587 -18.556 -11.051 1.00 26.80 ? 108  LYS B C     1 
ATOM   808  O O     . LYS A 1 110 ? 13.293 -17.955 -12.086 1.00 27.01 ? 108  LYS B O     1 
ATOM   809  C CB    . LYS A 1 110 ? 15.327 -17.440 -9.595  1.00 27.49 ? 108  LYS B CB    1 
ATOM   810  C CG    . LYS A 1 110 ? 15.878 -16.539 -10.688 1.00 30.93 ? 108  LYS B CG    1 
ATOM   811  C CD    . LYS A 1 110 ? 15.020 -15.297 -10.863 1.00 33.73 ? 108  LYS B CD    1 
ATOM   812  C CE    . LYS A 1 110 ? 15.702 -14.183 -11.610 1.00 38.43 ? 108  LYS B CE    1 
ATOM   813  N NZ    . LYS A 1 110 ? 14.836 -12.988 -11.635 1.00 46.73 ? 108  LYS B NZ    1 
ATOM   814  N N     . VAL A 1 111 ? 13.642 -19.882 -10.985 1.00 25.79 ? 109  VAL B N     1 
ATOM   815  C CA    . VAL A 1 111 ? 13.334 -20.701 -12.186 1.00 27.61 ? 109  VAL B CA    1 
ATOM   816  C C     . VAL A 1 111 ? 11.940 -20.358 -12.706 1.00 26.91 ? 109  VAL B C     1 
ATOM   817  O O     . VAL A 1 111 ? 11.744 -20.485 -13.930 1.00 27.57 ? 109  VAL B O     1 
ATOM   818  C CB    . VAL A 1 111 ? 13.501 -22.215 -11.967 1.00 28.89 ? 109  VAL B CB    1 
ATOM   819  C CG1   . VAL A 1 111 ? 14.957 -22.584 -11.738 1.00 27.21 ? 109  VAL B CG1   1 
ATOM   820  C CG2   . VAL A 1 111 ? 12.605 -22.736 -10.865 1.00 30.83 ? 109  VAL B CG2   1 
ATOM   821  N N     . ILE A 1 112 ? 11.001 -19.958 -11.850 1.00 24.76 ? 110  ILE B N     1 
ATOM   822  C CA    . ILE A 1 112 ? 9.603  -19.683 -12.285 1.00 26.23 ? 110  ILE B CA    1 
ATOM   823  C C     . ILE A 1 112 ? 9.467  -18.197 -12.609 1.00 25.59 ? 110  ILE B C     1 
ATOM   824  O O     . ILE A 1 112 ? 8.877  -17.862 -13.643 1.00 26.36 ? 110  ILE B O     1 
ATOM   825  C CB    . ILE A 1 112 ? 8.581  -20.156 -11.224 1.00 27.54 ? 110  ILE B CB    1 
ATOM   826  C CG1   . ILE A 1 112 ? 8.667  -21.668 -11.000 1.00 29.82 ? 110  ILE B CG1   1 
ATOM   827  C CG2   . ILE A 1 112 ? 7.176  -19.706 -11.566 1.00 28.09 ? 110  ILE B CG2   1 
ATOM   828  C CD1   . ILE A 1 112 ? 8.381  -22.505 -12.221 1.00 32.71 ? 110  ILE B CD1   1 
ATOM   829  N N     . SER A 1 113 ? 10.005 -17.309 -11.785 1.00 26.63 ? 111  SER B N     1 
ATOM   830  C CA    . SER A 1 113 ? 9.871  -15.850 -12.036 1.00 26.73 ? 111  SER B CA    1 
ATOM   831  C C     . SER A 1 113 ? 10.685 -15.476 -13.299 1.00 26.90 ? 111  SER B C     1 
ATOM   832  O O     . SER A 1 113 ? 10.202 -14.637 -14.064 1.00 26.70 ? 111  SER B O     1 
ATOM   833  C CB    . SER A 1 113 ? 10.235 -15.061 -10.813 1.00 25.76 ? 111  SER B CB    1 
ATOM   834  O OG    . SER A 1 113 ? 11.601 -15.198 -10.546 1.00 28.29 ? 111  SER B OG    1 
ATOM   835  N N     . ALA A 1 114 ? 11.808 -16.158 -13.566 1.00 25.84 ? 112  ALA B N     1 
ATOM   836  C CA    . ALA A 1 114 ? 12.597 -16.014 -14.820 1.00 27.86 ? 112  ALA B CA    1 
ATOM   837  C C     . ALA A 1 114 ? 11.751 -16.360 -16.059 1.00 28.67 ? 112  ALA B C     1 
ATOM   838  O O     . ALA A 1 114 ? 11.877 -15.640 -17.075 1.00 29.52 ? 112  ALA B O     1 
ATOM   839  C CB    . ALA A 1 114 ? 13.854 -16.842 -14.752 1.00 27.64 ? 112  ALA B CB    1 
ATOM   840  N N     . GLN A 1 115 ? 10.902 -17.388 -15.987 1.00 28.10 ? 113  GLN B N     1 
ATOM   841  C CA    . GLN A 1 115 ? 9.970  -17.741 -17.093 1.00 25.83 ? 113  GLN B CA    1 
ATOM   842  C C     . GLN A 1 115 ? 8.918  -16.644 -17.272 1.00 27.30 ? 113  GLN B C     1 
ATOM   843  O O     . GLN A 1 115 ? 8.658  -16.242 -18.409 1.00 26.34 ? 113  GLN B O     1 
ATOM   844  C CB    . GLN A 1 115 ? 9.411  -19.136 -16.897 1.00 25.08 ? 113  GLN B CB    1 
ATOM   845  C CG    . GLN A 1 115 ? 10.481 -20.200 -16.994 1.00 27.61 ? 113  GLN B CG    1 
ATOM   846  C CD    . GLN A 1 115 ? 9.882  -21.587 -16.980 1.00 34.30 ? 113  GLN B CD    1 
ATOM   847  O OE1   . GLN A 1 115 ? 10.477 -22.563 -17.467 1.00 38.71 ? 113  GLN B OE1   1 
ATOM   848  N NE2   . GLN A 1 115 ? 8.681  -21.682 -16.430 1.00 33.29 ? 113  GLN B NE2   1 
ATOM   849  N N     . VAL A 1 116 ? 8.349  -16.131 -16.200 1.00 27.00 ? 114  VAL B N     1 
ATOM   850  C CA    . VAL A 1 116 ? 7.365  -15.025 -16.286 1.00 27.76 ? 114  VAL B CA    1 
ATOM   851  C C     . VAL A 1 116 ? 8.046  -13.790 -16.888 1.00 28.54 ? 114  VAL B C     1 
ATOM   852  O O     . VAL A 1 116 ? 7.398  -13.093 -17.694 1.00 26.42 ? 114  VAL B O     1 
ATOM   853  C CB    . VAL A 1 116 ? 6.745  -14.765 -14.901 1.00 28.07 ? 114  VAL B CB    1 
ATOM   854  C CG1   . VAL A 1 116 ? 5.810  -13.565 -14.914 1.00 27.35 ? 114  VAL B CG1   1 
ATOM   855  C CG2   . VAL A 1 116 ? 6.044  -16.020 -14.395 1.00 27.57 ? 114  VAL B CG2   1 
ATOM   856  N N     . GLU A 1 117 ? 9.304  -13.527 -16.531 1.00 28.31 ? 115  GLU B N     1 
ATOM   857  C CA    . GLU A 1 117 ? 10.065 -12.376 -17.080 1.00 30.85 ? 115  GLU B CA    1 
ATOM   858  C C     . GLU A 1 117 ? 10.192 -12.573 -18.598 1.00 24.38 ? 115  GLU B C     1 
ATOM   859  O O     . GLU A 1 117 ? 9.956  -11.627 -19.341 1.00 23.72 ? 115  GLU B O     1 
ATOM   860  C CB    . GLU A 1 117 ? 11.458 -12.256 -16.457 1.00 36.50 ? 115  GLU B CB    1 
ATOM   861  C CG    . GLU A 1 117 ? 11.457 -11.798 -15.003 1.00 46.54 ? 115  GLU B CG    1 
ATOM   862  C CD    . GLU A 1 117 ? 12.813 -11.937 -14.313 1.00 55.26 ? 115  GLU B CD    1 
ATOM   863  O OE1   . GLU A 1 117 ? 12.856 -12.513 -13.195 1.00 59.08 ? 115  GLU B OE1   1 
ATOM   864  O OE2   . GLU A 1 117 ? 13.834 -11.483 -14.906 1.00 55.64 ? 115  GLU B OE2   1 
ATOM   865  N N     . GLU A 1 118 ? 10.507 -13.782 -19.037 1.00 23.74 ? 116  GLU B N     1 
ATOM   866  C CA    . GLU A 1 118 ? 10.627 -14.069 -20.494 1.00 24.02 ? 116  GLU B CA    1 
ATOM   867  C C     . GLU A 1 118 ? 9.300  -13.747 -21.190 1.00 24.05 ? 116  GLU B C     1 
ATOM   868  O O     . GLU A 1 118 ? 9.325  -13.024 -22.212 1.00 25.78 ? 116  GLU B O     1 
ATOM   869  C CB    . GLU A 1 118 ? 11.055 -15.508 -20.763 1.00 24.36 ? 116  GLU B CB    1 
ATOM   870  C CG    . GLU A 1 118 ? 11.481 -15.698 -22.224 1.00 26.40 ? 116  GLU B CG    1 
ATOM   871  C CD    . GLU A 1 118 ? 11.498 -17.121 -22.734 1.00 25.65 ? 116  GLU B CD    1 
ATOM   872  O OE1   . GLU A 1 118 ? 12.216 -17.967 -22.156 1.00 25.55 ? 116  GLU B OE1   1 
ATOM   873  O OE2   . GLU A 1 118 ? 10.787 -17.372 -23.725 1.00 29.86 ? 116  GLU B OE2   1 
ATOM   874  N N     . LEU A 1 119 ? 8.171  -14.190 -20.637 1.00 23.61 ? 117  LEU B N     1 
ATOM   875  C CA    . LEU A 1 119 ? 6.860  -13.978 -21.287 1.00 25.48 ? 117  LEU B CA    1 
ATOM   876  C C     . LEU A 1 119 ? 6.579  -12.482 -21.436 1.00 26.21 ? 117  LEU B C     1 
ATOM   877  O O     . LEU A 1 119 ? 6.157  -12.059 -22.535 1.00 26.37 ? 117  LEU B O     1 
ATOM   878  C CB    . LEU A 1 119 ? 5.740  -14.615 -20.475 1.00 27.22 ? 117  LEU B CB    1 
ATOM   879  C CG    . LEU A 1 119 ? 5.798  -16.113 -20.208 1.00 30.30 ? 117  LEU B CG    1 
ATOM   880  C CD1   . LEU A 1 119 ? 4.400  -16.600 -19.842 1.00 30.77 ? 117  LEU B CD1   1 
ATOM   881  C CD2   . LEU A 1 119 ? 6.354  -16.915 -21.359 1.00 29.70 ? 117  LEU B CD2   1 
ATOM   882  N N     . VAL A 1 120 ? 6.722  -11.703 -20.365 1.00 25.90 ? 118  VAL B N     1 
ATOM   883  C CA    . VAL A 1 120 ? 6.301  -10.278 -20.424 1.00 25.29 ? 118  VAL B CA    1 
ATOM   884  C C     . VAL A 1 120 ? 7.286  -9.533  -21.337 1.00 23.11 ? 118  VAL B C     1 
ATOM   885  O O     . VAL A 1 120 ? 6.844  -8.669  -22.126 1.00 23.78 ? 118  VAL B O     1 
ATOM   886  C CB    . VAL A 1 120 ? 6.139  -9.632  -19.035 1.00 27.19 ? 118  VAL B CB    1 
ATOM   887  C CG1   . VAL A 1 120 ? 7.442  -9.467  -18.282 1.00 30.07 ? 118  VAL B CG1   1 
ATOM   888  C CG2   . VAL A 1 120 ? 5.456  -8.284  -19.166 1.00 29.80 ? 118  VAL B CG2   1 
ATOM   889  N N     . ASN A 1 121 ? 8.565  -9.886  -21.256 1.00 23.41 ? 119  ASN B N     1 
ATOM   890  C CA    . ASN A 1 121 ? 9.609  -9.188  -22.049 1.00 24.56 ? 119  ASN B CA    1 
ATOM   891  C C     . ASN A 1 121 ? 9.463  -9.528  -23.542 1.00 24.42 ? 119  ASN B C     1 
ATOM   892  O O     . ASN A 1 121 ? 9.764  -8.661  -24.360 1.00 24.35 ? 119  ASN B O     1 
ATOM   893  C CB    . ASN A 1 121 ? 11.004 -9.489  -21.504 1.00 25.51 ? 119  ASN B CB    1 
ATOM   894  C CG    . ASN A 1 121 ? 11.318 -8.725  -20.235 1.00 29.89 ? 119  ASN B CG    1 
ATOM   895  O OD1   . ASN A 1 121 ? 10.648 -7.752  -19.910 1.00 29.30 ? 119  ASN B OD1   1 
ATOM   896  N ND2   . ASN A 1 121 ? 12.338 -9.158  -19.517 1.00 32.29 ? 119  ASN B ND2   1 
ATOM   897  N N     . SER A 1 122 ? 9.042  -10.750 -23.864 1.00 22.59 ? 120  SER B N     1 
ATOM   898  C CA    . SER A 1 122 ? 8.790  -11.131 -25.277 1.00 22.32 ? 120  SER B CA    1 
ATOM   899  C C     . SER A 1 122 ? 7.582  -10.345 -25.792 1.00 24.94 ? 120  SER B C     1 
ATOM   900  O O     . SER A 1 122 ? 7.634  -9.865  -26.916 1.00 25.04 ? 120  SER B O     1 
ATOM   901  C CB    . SER A 1 122 ? 8.592  -12.626 -25.419 1.00 23.45 ? 120  SER B CB    1 
ATOM   902  O OG    . SER A 1 122 ? 9.807  -13.336 -25.337 1.00 23.72 ? 120  SER B OG    1 
ATOM   903  N N     . ALA A 1 123 ? 6.540  -10.212 -24.965 1.00 23.55 ? 121  ALA B N     1 
ATOM   904  C CA    . ALA A 1 123 ? 5.294  -9.541  -25.380 1.00 21.55 ? 121  ALA B CA    1 
ATOM   905  C C     . ALA A 1 123 ? 5.525  -8.048  -25.601 1.00 22.61 ? 121  ALA B C     1 
ATOM   906  O O     . ALA A 1 123 ? 4.986  -7.520  -26.565 1.00 22.86 ? 121  ALA B O     1 
ATOM   907  C CB    . ALA A 1 123 ? 4.259  -9.759  -24.312 1.00 23.01 ? 121  ALA B CB    1 
ATOM   908  N N     . ASN A 1 124 ? 6.312  -7.422  -24.735 1.00 21.68 ? 122  ASN B N     1 
ATOM   909  C CA    . ASN A 1 124 ? 6.475  -5.949  -24.788 1.00 20.64 ? 122  ASN B CA    1 
ATOM   910  C C     . ASN A 1 124 ? 7.640  -5.580  -23.869 1.00 22.86 ? 122  ASN B C     1 
ATOM   911  O O     . ASN A 1 124 ? 7.413  -5.420  -22.674 1.00 24.85 ? 122  ASN B O     1 
ATOM   912  C CB    . ASN A 1 124 ? 5.172  -5.268  -24.380 1.00 20.41 ? 122  ASN B CB    1 
ATOM   913  C CG    . ASN A 1 124 ? 5.151  -3.769  -24.571 1.00 21.33 ? 122  ASN B CG    1 
ATOM   914  O OD1   . ASN A 1 124 ? 6.183  -3.115  -24.507 1.00 22.68 ? 122  ASN B OD1   1 
ATOM   915  N ND2   . ASN A 1 124 ? 3.968  -3.222  -24.786 1.00 24.80 ? 122  ASN B ND2   1 
ATOM   916  N N     . LEU A 1 125 ? 8.839  -5.461  -24.430 1.00 23.49 ? 123  LEU B N     1 
ATOM   917  C CA    . LEU A 1 125 ? 10.034 -5.206  -23.593 1.00 22.79 ? 123  LEU B CA    1 
ATOM   918  C C     . LEU A 1 125 ? 9.883  -3.890  -22.808 1.00 21.38 ? 123  LEU B C     1 
ATOM   919  O O     . LEU A 1 125 ? 10.217 -3.872  -21.595 1.00 24.54 ? 123  LEU B O     1 
ATOM   920  C CB    . LEU A 1 125 ? 11.299 -5.209  -24.445 1.00 21.75 ? 123  LEU B CB    1 
ATOM   921  C CG    . LEU A 1 125 ? 12.574 -4.919  -23.642 1.00 22.92 ? 123  LEU B CG    1 
ATOM   922  C CD1   . LEU A 1 125 ? 12.733 -5.896  -22.479 1.00 23.69 ? 123  LEU B CD1   1 
ATOM   923  C CD2   . LEU A 1 125 ? 13.797 -4.938  -24.545 1.00 23.00 ? 123  LEU B CD2   1 
ATOM   924  N N     . SER A 1 126 ? 9.450  -2.807  -23.438 1.00 23.15 ? 124  SER B N     1 
ATOM   925  C CA    . SER A 1 126 ? 9.276  -1.507  -22.739 1.00 23.92 ? 124  SER B CA    1 
ATOM   926  C C     . SER A 1 126 ? 8.376  -1.706  -21.507 1.00 25.78 ? 124  SER B C     1 
ATOM   927  O O     . SER A 1 126 ? 8.722  -1.242  -20.395 1.00 25.73 ? 124  SER B O     1 
ATOM   928  C CB    . SER A 1 126 ? 8.702  -0.465  -23.634 1.00 25.03 ? 124  SER B CB    1 
ATOM   929  O OG    . SER A 1 126 ? 9.652  -0.047  -24.580 1.00 26.80 ? 124  SER B OG    1 
ATOM   930  N N     . PHE A 1 127 ? 7.280  -2.434  -21.680 1.00 28.08 ? 125  PHE B N     1 
ATOM   931  C CA    . PHE A 1 127 ? 6.337  -2.727  -20.576 1.00 28.70 ? 125  PHE B CA    1 
ATOM   932  C C     . PHE A 1 127 ? 7.072  -3.515  -19.487 1.00 28.20 ? 125  PHE B C     1 
ATOM   933  O O     . PHE A 1 127 ? 7.022  -3.111  -18.315 1.00 27.31 ? 125  PHE B O     1 
ATOM   934  C CB    . PHE A 1 127 ? 5.108  -3.494  -21.052 1.00 27.56 ? 125  PHE B CB    1 
ATOM   935  C CG    . PHE A 1 127 ? 4.171  -3.763  -19.908 1.00 28.90 ? 125  PHE B CG    1 
ATOM   936  C CD1   . PHE A 1 127 ? 3.217  -2.832  -19.545 1.00 30.05 ? 125  PHE B CD1   1 
ATOM   937  C CD2   . PHE A 1 127 ? 4.295  -4.914  -19.155 1.00 28.77 ? 125  PHE B CD2   1 
ATOM   938  C CE1   . PHE A 1 127 ? 2.377  -3.068  -18.465 1.00 30.58 ? 125  PHE B CE1   1 
ATOM   939  C CE2   . PHE A 1 127 ? 3.451  -5.152  -18.082 1.00 30.55 ? 125  PHE B CE2   1 
ATOM   940  C CZ    . PHE A 1 127 ? 2.495  -4.224  -17.737 1.00 29.83 ? 125  PHE B CZ    1 
ATOM   941  N N     . GLY A 1 128 ? 7.710  -4.619  -19.873 1.00 27.76 ? 126  GLY B N     1 
ATOM   942  C CA    . GLY A 1 128 ? 8.295  -5.597  -18.943 1.00 27.95 ? 126  GLY B CA    1 
ATOM   943  C C     . GLY A 1 128 ? 9.378  -4.982  -18.079 1.00 28.67 ? 126  GLY B C     1 
ATOM   944  O O     . GLY A 1 128 ? 9.536  -5.406  -16.916 1.00 27.31 ? 126  GLY B O     1 
ATOM   945  N N     . LEU A 1 129 ? 10.086 -3.978  -18.578 1.00 27.37 ? 127  LEU B N     1 
ATOM   946  C CA    . LEU A 1 129 ? 11.168 -3.357  -17.773 1.00 28.07 ? 127  LEU B CA    1 
ATOM   947  C C     . LEU A 1 129 ? 10.605 -2.640  -16.540 1.00 27.17 ? 127  LEU B C     1 
ATOM   948  O O     . LEU A 1 129 ? 11.356 -2.571  -15.528 1.00 26.63 ? 127  LEU B O     1 
ATOM   949  C CB    . LEU A 1 129 ? 11.981 -2.385  -18.624 1.00 28.42 ? 127  LEU B CB    1 
ATOM   950  C CG    . LEU A 1 129 ? 12.886 -3.040  -19.658 1.00 30.36 ? 127  LEU B CG    1 
ATOM   951  C CD1   . LEU A 1 129 ? 13.788 -1.983  -20.271 1.00 30.74 ? 127  LEU B CD1   1 
ATOM   952  C CD2   . LEU A 1 129 ? 13.687 -4.190  -19.061 1.00 31.32 ? 127  LEU B CD2   1 
ATOM   953  N N     . TYR A 1 130 ? 9.382  -2.102  -16.594 1.00 26.20 ? 128  TYR B N     1 
ATOM   954  C CA    . TYR A 1 130 ? 8.825  -1.295  -15.474 1.00 26.54 ? 128  TYR B CA    1 
ATOM   955  C C     . TYR A 1 130 ? 8.739  -2.163  -14.218 1.00 26.87 ? 128  TYR B C     1 
ATOM   956  O O     . TYR A 1 130 ? 9.341  -1.819  -13.210 1.00 28.70 ? 128  TYR B O     1 
ATOM   957  C CB    . TYR A 1 130 ? 7.483  -0.674  -15.843 1.00 25.81 ? 128  TYR B CB    1 
ATOM   958  C CG    . TYR A 1 130 ? 7.547  0.495   -16.792 1.00 24.53 ? 128  TYR B CG    1 
ATOM   959  C CD1   . TYR A 1 130 ? 8.030  1.714   -16.366 1.00 24.76 ? 128  TYR B CD1   1 
ATOM   960  C CD2   . TYR A 1 130 ? 7.073  0.401   -18.096 1.00 23.51 ? 128  TYR B CD2   1 
ATOM   961  C CE1   . TYR A 1 130 ? 8.056  2.813   -17.208 1.00 26.36 ? 128  TYR B CE1   1 
ATOM   962  C CE2   . TYR A 1 130 ? 7.131  1.481   -18.962 1.00 24.53 ? 128  TYR B CE2   1 
ATOM   963  C CZ    . TYR A 1 130 ? 7.610  2.700   -18.511 1.00 24.73 ? 128  TYR B CZ    1 
ATOM   964  O OH    . TYR A 1 130 ? 7.648  3.801   -19.313 1.00 22.68 ? 128  TYR B OH    1 
ATOM   965  N N     . PRO A 1 131 ? 8.021  -3.315  -14.239 1.00 26.13 ? 129  PRO B N     1 
ATOM   966  C CA    . PRO A 1 131 ? 7.938  -4.191  -13.074 1.00 26.16 ? 129  PRO B CA    1 
ATOM   967  C C     . PRO A 1 131 ? 9.292  -4.818  -12.736 1.00 27.02 ? 129  PRO B C     1 
ATOM   968  O O     . PRO A 1 131 ? 9.546  -5.097  -11.578 1.00 21.82 ? 129  PRO B O     1 
ATOM   969  C CB    . PRO A 1 131 ? 6.914  -5.264  -13.474 1.00 28.87 ? 129  PRO B CB    1 
ATOM   970  C CG    . PRO A 1 131 ? 6.898  -5.243  -14.997 1.00 24.46 ? 129  PRO B CG    1 
ATOM   971  C CD    . PRO A 1 131 ? 7.173  -3.797  -15.339 1.00 25.24 ? 129  PRO B CD    1 
ATOM   972  N N     . GLY A 1 132 ? 10.150 -5.006  -13.749 1.00 27.68 ? 130  GLY B N     1 
ATOM   973  C CA    . GLY A 1 132 ? 11.551 -5.419  -13.548 1.00 26.83 ? 130  GLY B CA    1 
ATOM   974  C C     . GLY A 1 132 ? 12.264 -4.520  -12.558 1.00 25.85 ? 130  GLY B C     1 
ATOM   975  O O     . GLY A 1 132 ? 12.911 -5.059  -11.633 1.00 27.78 ? 130  GLY B O     1 
ATOM   976  N N     . LEU A 1 133 ? 12.164 -3.197  -12.720 1.00 27.20 ? 131  LEU B N     1 
ATOM   977  C CA    . LEU A 1 133 ? 12.808 -2.225  -11.796 1.00 28.18 ? 131  LEU B CA    1 
ATOM   978  C C     . LEU A 1 133 ? 12.344 -2.473  -10.361 1.00 26.85 ? 131  LEU B C     1 
ATOM   979  O O     . LEU A 1 133 ? 13.159 -2.445  -9.462  1.00 25.95 ? 131  LEU B O     1 
ATOM   980  C CB    . LEU A 1 133 ? 12.373 -0.810  -12.158 1.00 30.36 ? 131  LEU B CB    1 
ATOM   981  C CG    . LEU A 1 133 ? 12.898 -0.255  -13.462 1.00 33.31 ? 131  LEU B CG    1 
ATOM   982  C CD1   . LEU A 1 133 ? 12.413 1.183   -13.607 1.00 37.05 ? 131  LEU B CD1   1 
ATOM   983  C CD2   . LEU A 1 133 ? 14.411 -0.347  -13.510 1.00 35.84 ? 131  LEU B CD2   1 
ATOM   984  N N     . THR A 1 134 ? 11.033 -2.609  -10.169 1.00 25.98 ? 132  THR B N     1 
ATOM   985  C CA    . THR A 1 134 ? 10.391 -2.673  -8.834  1.00 25.73 ? 132  THR B CA    1 
ATOM   986  C C     . THR A 1 134 ? 10.898 -3.923  -8.133  1.00 26.87 ? 132  THR B C     1 
ATOM   987  O O     . THR A 1 134 ? 11.362 -3.826  -6.961  1.00 27.32 ? 132  THR B O     1 
ATOM   988  C CB    . THR A 1 134 ? 8.871  -2.582  -8.996  1.00 25.80 ? 132  THR B CB    1 
ATOM   989  O OG1   . THR A 1 134 ? 8.661  -1.368  -9.722  1.00 25.54 ? 132  THR B OG1   1 
ATOM   990  C CG2   . THR A 1 134 ? 8.141  -2.604  -7.671  1.00 26.09 ? 132  THR B CG2   1 
ATOM   991  N N     . ALA A 1 135 ? 10.896 -5.040  -8.851  1.00 26.78 ? 133  ALA B N     1 
ATOM   992  C CA    . ALA A 1 135 ? 11.352 -6.345  -8.338  1.00 28.41 ? 133  ALA B CA    1 
ATOM   993  C C     . ALA A 1 135 ? 12.822 -6.265  -7.922  1.00 29.14 ? 133  ALA B C     1 
ATOM   994  O O     . ALA A 1 135 ? 13.171 -6.777  -6.835  1.00 29.77 ? 133  ALA B O     1 
ATOM   995  C CB    . ALA A 1 135 ? 11.103 -7.426  -9.350  1.00 30.39 ? 133  ALA B CB    1 
ATOM   996  N N     . GLY A 1 136 ? 13.651 -5.623  -8.732  1.00 28.82 ? 134  GLY B N     1 
ATOM   997  C CA    . GLY A 1 136 ? 15.074 -5.419  -8.419  1.00 26.75 ? 134  GLY B CA    1 
ATOM   998  C C     . GLY A 1 136 ? 15.244 -4.545  -7.182  1.00 28.25 ? 134  GLY B C     1 
ATOM   999  O O     . GLY A 1 136 ? 16.045 -4.907  -6.316  1.00 24.49 ? 134  GLY B O     1 
ATOM   1000 N N     . ALA A 1 137 ? 14.535 -3.411  -7.123  1.00 28.16 ? 135  ALA B N     1 
ATOM   1001 C CA    . ALA A 1 137 ? 14.558 -2.486  -5.966  1.00 29.56 ? 135  ALA B CA    1 
ATOM   1002 C C     . ALA A 1 137 ? 14.175 -3.259  -4.699  1.00 28.79 ? 135  ALA B C     1 
ATOM   1003 O O     . ALA A 1 137 ? 14.881 -3.124  -3.703  1.00 32.08 ? 135  ALA B O     1 
ATOM   1004 C CB    . ALA A 1 137 ? 13.651 -1.299  -6.200  1.00 28.11 ? 135  ALA B CB    1 
ATOM   1005 N N     . CYS A 1 138 ? 13.128 -4.085  -4.751  1.00 31.97 ? 136  CYS B N     1 
ATOM   1006 C CA    . CYS A 1 138 ? 12.678 -4.918  -3.599  1.00 30.05 ? 136  CYS B CA    1 
ATOM   1007 C C     . CYS A 1 138 ? 13.803 -5.829  -3.114  1.00 29.61 ? 136  CYS B C     1 
ATOM   1008 O O     . CYS A 1 138 ? 13.980 -5.915  -1.901  1.00 26.09 ? 136  CYS B O     1 
ATOM   1009 C CB    . CYS A 1 138 ? 11.466 -5.764  -3.924  1.00 28.77 ? 136  CYS B CB    1 
ATOM   1010 S SG    . CYS A 1 138 ? 9.997  -4.743  -4.088  1.00 31.20 ? 136  CYS B SG    1 
ATOM   1011 N N     . LEU A 1 139 ? 14.524 -6.486  -4.021  1.00 30.61 ? 137  LEU B N     1 
ATOM   1012 C CA    . LEU A 1 139 ? 15.670 -7.370  -3.673  1.00 31.78 ? 137  LEU B CA    1 
ATOM   1013 C C     . LEU A 1 139 ? 16.676 -6.619  -2.801  1.00 30.60 ? 137  LEU B C     1 
ATOM   1014 O O     . LEU A 1 139 ? 17.112 -7.191  -1.793  1.00 32.74 ? 137  LEU B O     1 
ATOM   1015 C CB    . LEU A 1 139 ? 16.364 -7.847  -4.946  1.00 35.21 ? 137  LEU B CB    1 
ATOM   1016 C CG    . LEU A 1 139 ? 15.795 -9.129  -5.539  1.00 38.65 ? 137  LEU B CG    1 
ATOM   1017 C CD1   . LEU A 1 139 ? 16.362 -9.375  -6.940  1.00 39.58 ? 137  LEU B CD1   1 
ATOM   1018 C CD2   . LEU A 1 139 ? 16.088 -10.296 -4.621  1.00 39.20 ? 137  LEU B CD2   1 
ATOM   1019 N N     . ALA A 1 140 ? 17.033 -5.398  -3.192  1.00 27.67 ? 138  ALA B N     1 
ATOM   1020 C CA    . ALA A 1 140 ? 18.012 -4.563  -2.464  1.00 29.52 ? 138  ALA B CA    1 
ATOM   1021 C C     . ALA A 1 140 ? 17.442 -4.206  -1.086  1.00 29.13 ? 138  ALA B C     1 
ATOM   1022 O O     . ALA A 1 140 ? 18.161 -4.370  -0.108  1.00 29.07 ? 138  ALA B O     1 
ATOM   1023 C CB    . ALA A 1 140 ? 18.364 -3.322  -3.251  1.00 30.36 ? 138  ALA B CB    1 
ATOM   1024 N N     . LEU A 1 141 ? 16.215 -3.691  -1.015  1.00 31.96 ? 139  LEU B N     1 
ATOM   1025 C CA    . LEU A 1 141 ? 15.623 -3.254  0.280   1.00 31.46 ? 139  LEU B CA    1 
ATOM   1026 C C     . LEU A 1 141 ? 15.491 -4.467  1.204   1.00 32.93 ? 139  LEU B C     1 
ATOM   1027 O O     . LEU A 1 141 ? 15.887 -4.383  2.385   1.00 33.12 ? 139  LEU B O     1 
ATOM   1028 C CB    . LEU A 1 141 ? 14.270 -2.602  0.035   1.00 29.88 ? 139  LEU B CB    1 
ATOM   1029 C CG    . LEU A 1 141 ? 14.304 -1.292  -0.749  1.00 30.66 ? 139  LEU B CG    1 
ATOM   1030 C CD1   . LEU A 1 141 ? 12.899 -0.762  -0.953  1.00 28.92 ? 139  LEU B CD1   1 
ATOM   1031 C CD2   . LEU A 1 141 ? 15.166 -0.252  -0.031  1.00 31.40 ? 139  LEU B CD2   1 
ATOM   1032 N N     . ASN A 1 142 ? 14.971 -5.572  0.688   1.00 31.61 ? 140  ASN B N     1 
ATOM   1033 C CA    . ASN A 1 142 ? 14.789 -6.800  1.499   1.00 34.53 ? 140  ASN B CA    1 
ATOM   1034 C C     . ASN A 1 142 ? 16.138 -7.202  2.098   1.00 35.30 ? 140  ASN B C     1 
ATOM   1035 O O     . ASN A 1 142 ? 16.202 -7.469  3.310   1.00 35.10 ? 140  ASN B O     1 
ATOM   1036 C CB    . ASN A 1 142 ? 14.169 -7.927  0.680   1.00 36.56 ? 140  ASN B CB    1 
ATOM   1037 C CG    . ASN A 1 142 ? 13.520 -8.957  1.568   1.00 38.03 ? 140  ASN B CG    1 
ATOM   1038 O OD1   . ASN A 1 142 ? 14.060 -9.315  2.605   1.00 49.47 ? 140  ASN B OD1   1 
ATOM   1039 N ND2   . ASN A 1 142 ? 12.362 -9.426  1.174   1.00 40.12 ? 140  ASN B ND2   1 
ATOM   1040 N N     . ALA A 1 143 ? 17.201 -7.176  1.298   1.00 34.79 ? 141  ALA B N     1 
ATOM   1041 C CA    . ALA A 1 143 ? 18.544 -7.637  1.716   1.00 33.83 ? 141  ALA B CA    1 
ATOM   1042 C C     . ALA A 1 143 ? 19.185 -6.687  2.748   1.00 35.25 ? 141  ALA B C     1 
ATOM   1043 O O     . ALA A 1 143 ? 19.993 -7.186  3.566   1.00 34.57 ? 141  ALA B O     1 
ATOM   1044 C CB    . ALA A 1 143 ? 19.419 -7.789  0.499   1.00 35.22 ? 141  ALA B CB    1 
ATOM   1045 N N     . HIS A 1 144 ? 18.936 -5.369  2.695   1.00 32.22 ? 142  HIS B N     1 
ATOM   1046 C CA    . HIS A 1 144 ? 19.835 -4.398  3.385   1.00 32.58 ? 142  HIS B CA    1 
ATOM   1047 C C     . HIS A 1 144 ? 19.121 -3.283  4.136   1.00 31.45 ? 142  HIS B C     1 
ATOM   1048 O O     . HIS A 1 144 ? 19.804 -2.613  4.919   1.00 29.03 ? 142  HIS B O     1 
ATOM   1049 C CB    . HIS A 1 144 ? 20.810 -3.780  2.381   1.00 33.51 ? 142  HIS B CB    1 
ATOM   1050 C CG    . HIS A 1 144 ? 21.843 -4.757  1.950   1.00 35.28 ? 142  HIS B CG    1 
ATOM   1051 N ND1   . HIS A 1 144 ? 22.776 -5.249  2.825   1.00 38.49 ? 142  HIS B ND1   1 
ATOM   1052 C CD2   . HIS A 1 144 ? 22.055 -5.373  0.765   1.00 38.12 ? 142  HIS B CD2   1 
ATOM   1053 C CE1   . HIS A 1 144 ? 23.543 -6.118  2.194   1.00 41.81 ? 142  HIS B CE1   1 
ATOM   1054 N NE2   . HIS A 1 144 ? 23.132 -6.203  0.925   1.00 35.80 ? 142  HIS B NE2   1 
ATOM   1055 N N     . ALA A 1 145 ? 17.847 -3.033  3.871   1.00 31.21 ? 143  ALA B N     1 
ATOM   1056 C CA    . ALA A 1 145 ? 17.111 -1.944  4.541   1.00 31.38 ? 143  ALA B CA    1 
ATOM   1057 C C     . ALA A 1 145 ? 16.751 -2.389  5.972   1.00 32.64 ? 143  ALA B C     1 
ATOM   1058 O O     . ALA A 1 145 ? 16.620 -3.603  6.230   1.00 29.05 ? 143  ALA B O     1 
ATOM   1059 C CB    . ALA A 1 145 ? 15.902 -1.559  3.733   1.00 32.49 ? 143  ALA B CB    1 
ATOM   1060 N N     . SER A 1 146 ? 16.607 -1.420  6.869   1.00 32.11 ? 144  SER B N     1 
ATOM   1061 C CA    . SER A 1 146 ? 16.115 -1.592  8.264   1.00 33.45 ? 144  SER B CA    1 
ATOM   1062 C C     . SER A 1 146 ? 14.709 -2.207  8.249   1.00 33.20 ? 144  SER B C     1 
ATOM   1063 O O     . SER A 1 146 ? 13.983 -2.024  7.242   1.00 31.32 ? 144  SER B O     1 
ATOM   1064 C CB    . SER A 1 146 ? 16.093 -0.252  8.946   1.00 31.96 ? 144  SER B CB    1 
ATOM   1065 O OG    . SER A 1 146 ? 15.053 0.540   8.388   1.00 31.09 ? 144  SER B OG    1 
ATOM   1066 N N     . ASP A 1 147 ? 14.298 -2.851  9.344   1.00 33.45 ? 145  ASP B N     1 
ATOM   1067 C CA    . ASP A 1 147 ? 12.904 -3.346  9.509   1.00 37.26 ? 145  ASP B CA    1 
ATOM   1068 C C     . ASP A 1 147 ? 11.918 -2.216  9.225   1.00 37.71 ? 145  ASP B C     1 
ATOM   1069 O O     . ASP A 1 147 ? 10.902 -2.471  8.545   1.00 37.81 ? 145  ASP B O     1 
ATOM   1070 C CB    . ASP A 1 147 ? 12.679 -3.958  10.892  1.00 39.65 ? 145  ASP B CB    1 
ATOM   1071 C CG    . ASP A 1 147 ? 13.381 -5.298  11.027  1.00 41.46 ? 145  ASP B CG    1 
ATOM   1072 O OD1   . ASP A 1 147 ? 13.991 -5.733  10.035  1.00 42.06 ? 145  ASP B OD1   1 
ATOM   1073 O OD2   . ASP A 1 147 ? 13.314 -5.890  12.113  1.00 45.01 ? 145  ASP B OD2   1 
ATOM   1074 N N     . GLU A 1 148 ? 12.199 -1.007  9.702   1.00 37.37 ? 146  GLU B N     1 
ATOM   1075 C CA    . GLU A 1 148 ? 11.249 0.129   9.601   1.00 38.07 ? 146  GLU B CA    1 
ATOM   1076 C C     . GLU A 1 148 ? 10.973 0.430   8.124   1.00 35.21 ? 146  GLU B C     1 
ATOM   1077 O O     . GLU A 1 148 ? 9.802  0.574   7.752   1.00 34.94 ? 146  GLU B O     1 
ATOM   1078 C CB    . GLU A 1 148 ? 11.811 1.348   10.344  1.00 45.83 ? 146  GLU B CB    1 
ATOM   1079 C CG    . GLU A 1 148 ? 10.820 2.500   10.490  1.00 53.56 ? 146  GLU B CG    1 
ATOM   1080 C CD    . GLU A 1 148 ? 11.303 3.693   11.314  1.00 58.14 ? 146  GLU B CD    1 
ATOM   1081 O OE1   . GLU A 1 148 ? 11.964 3.470   12.349  1.00 61.39 ? 146  GLU B OE1   1 
ATOM   1082 O OE2   . GLU A 1 148 ? 11.015 4.845   10.921  1.00 65.05 ? 146  GLU B OE2   1 
ATOM   1083 N N     . LEU A 1 149 ? 12.015 0.556   7.304   1.00 33.36 ? 147  LEU B N     1 
ATOM   1084 C CA    . LEU A 1 149 ? 11.869 0.841   5.850   1.00 32.84 ? 147  LEU B CA    1 
ATOM   1085 C C     . LEU A 1 149 ? 11.232 -0.347  5.133   1.00 33.05 ? 147  LEU B C     1 
ATOM   1086 O O     . LEU A 1 149 ? 10.339 -0.130  4.301   1.00 36.64 ? 147  LEU B O     1 
ATOM   1087 C CB    . LEU A 1 149 ? 13.247 1.116   5.244   1.00 34.94 ? 147  LEU B CB    1 
ATOM   1088 C CG    . LEU A 1 149 ? 13.893 2.418   5.680   1.00 32.61 ? 147  LEU B CG    1 
ATOM   1089 C CD1   . LEU A 1 149 ? 15.311 2.500   5.129   1.00 33.31 ? 147  LEU B CD1   1 
ATOM   1090 C CD2   . LEU A 1 149 ? 13.030 3.605   5.253   1.00 32.28 ? 147  LEU B CD2   1 
ATOM   1091 N N     . LYS A 1 150 ? 11.697 -1.560  5.399   1.00 31.46 ? 148  LYS B N     1 
ATOM   1092 C CA    . LYS A 1 150 ? 11.095 -2.757  4.757   1.00 33.48 ? 148  LYS B CA    1 
ATOM   1093 C C     . LYS A 1 150 ? 9.577  -2.755  4.997   1.00 36.23 ? 148  LYS B C     1 
ATOM   1094 O O     . LYS A 1 150 ? 8.785  -2.915  4.023   1.00 30.60 ? 148  LYS B O     1 
ATOM   1095 C CB    . LYS A 1 150 ? 11.719 -4.030  5.322   1.00 32.62 ? 148  LYS B CB    1 
ATOM   1096 C CG    . LYS A 1 150 ? 13.145 -4.292  4.887   1.00 33.91 ? 148  LYS B CG    1 
ATOM   1097 C CD    . LYS A 1 150 ? 13.581 -5.736  5.131   1.00 34.18 ? 148  LYS B CD    1 
ATOM   1098 C CE    . LYS A 1 150 ? 13.974 -5.972  6.576   1.00 35.49 ? 148  LYS B CE    1 
ATOM   1099 N NZ    . LYS A 1 150 ? 14.610 -7.291  6.769   1.00 33.16 ? 148  LYS B NZ    1 
ATOM   1100 N N     . ASP A 1 151 ? 9.174  -2.590  6.261   1.00 35.56 ? 149  ASP B N     1 
ATOM   1101 C CA    . ASP A 1 151 ? 7.758  -2.673  6.703   1.00 34.25 ? 149  ASP B CA    1 
ATOM   1102 C C     . ASP A 1 151 ? 6.950  -1.599  5.976   1.00 31.93 ? 149  ASP B C     1 
ATOM   1103 O O     . ASP A 1 151 ? 5.837  -1.874  5.566   1.00 30.88 ? 149  ASP B O     1 
ATOM   1104 C CB    . ASP A 1 151 ? 7.678  -2.580  8.237   1.00 35.43 ? 149  ASP B CB    1 
ATOM   1105 C CG    . ASP A 1 151 ? 8.269  -3.788  8.945   1.00 35.55 ? 149  ASP B CG    1 
ATOM   1106 O OD1   . ASP A 1 151 ? 8.528  -4.791  8.262   1.00 36.61 ? 149  ASP B OD1   1 
ATOM   1107 O OD2   . ASP A 1 151 ? 8.495  -3.715  10.169  1.00 38.60 ? 149  ASP B OD2   1 
ATOM   1108 N N     . LYS A 1 152 ? 7.517  -0.417  5.784   1.00 29.46 ? 150  LYS B N     1 
ATOM   1109 C CA    . LYS A 1 152 ? 6.764  0.757   5.286   1.00 32.30 ? 150  LYS B CA    1 
ATOM   1110 C C     . LYS A 1 152 ? 6.605  0.672   3.750   1.00 26.72 ? 150  LYS B C     1 
ATOM   1111 O O     . LYS A 1 152 ? 5.566  1.099   3.251   1.00 29.38 ? 150  LYS B O     1 
ATOM   1112 C CB    . LYS A 1 152 ? 7.517  1.988   5.799   1.00 34.26 ? 150  LYS B CB    1 
ATOM   1113 C CG    . LYS A 1 152 ? 6.909  3.337   5.480   1.00 42.31 ? 150  LYS B CG    1 
ATOM   1114 C CD    . LYS A 1 152 ? 7.555  4.457   6.280   1.00 47.48 ? 150  LYS B CD    1 
ATOM   1115 C CE    . LYS A 1 152 ? 7.304  5.831   5.688   1.00 57.02 ? 150  LYS B CE    1 
ATOM   1116 N NZ    . LYS A 1 152 ? 6.019  6.425   6.142   1.00 61.15 ? 150  LYS B NZ    1 
ATOM   1117 N N     . TYR A 1 153 ? 7.574  0.105   3.031   1.00 27.35 ? 151  TYR B N     1 
ATOM   1118 C CA    . TYR A 1 153 ? 7.702  0.285   1.554   1.00 28.56 ? 151  TYR B CA    1 
ATOM   1119 C C     . TYR A 1 153 ? 7.475  -1.030  0.793   1.00 26.28 ? 151  TYR B C     1 
ATOM   1120 O O     . TYR A 1 153 ? 6.832  -0.967  -0.263  1.00 27.86 ? 151  TYR B O     1 
ATOM   1121 C CB    . TYR A 1 153 ? 9.050  0.944   1.246   1.00 29.01 ? 151  TYR B CB    1 
ATOM   1122 C CG    . TYR A 1 153 ? 9.127  2.382   1.682   1.00 29.49 ? 151  TYR B CG    1 
ATOM   1123 C CD1   . TYR A 1 153 ? 8.440  3.364   0.986   1.00 30.16 ? 151  TYR B CD1   1 
ATOM   1124 C CD2   . TYR A 1 153 ? 9.838  2.760   2.811   1.00 30.54 ? 151  TYR B CD2   1 
ATOM   1125 C CE1   . TYR A 1 153 ? 8.469  4.692   1.385   1.00 31.92 ? 151  TYR B CE1   1 
ATOM   1126 C CE2   . TYR A 1 153 ? 9.874  4.085   3.226   1.00 31.58 ? 151  TYR B CE2   1 
ATOM   1127 C CZ    . TYR A 1 153 ? 9.162  5.047   2.530   1.00 31.56 ? 151  TYR B CZ    1 
ATOM   1128 O OH    . TYR A 1 153 ? 9.187  6.356   2.924   1.00 35.80 ? 151  TYR B OH    1 
ATOM   1129 N N     . LEU A 1 154 ? 7.979  -2.165  1.281   1.00 27.14 ? 152  LEU B N     1 
ATOM   1130 C CA    . LEU A 1 154 ? 7.971  -3.435  0.518   1.00 26.94 ? 152  LEU B CA    1 
ATOM   1131 C C     . LEU A 1 154 ? 6.556  -3.875  0.153   1.00 30.49 ? 152  LEU B C     1 
ATOM   1132 O O     . LEU A 1 154 ? 6.324  -4.217  -1.006  1.00 31.42 ? 152  LEU B O     1 
ATOM   1133 C CB    . LEU A 1 154 ? 8.744  -4.512  1.273   1.00 28.39 ? 152  LEU B CB    1 
ATOM   1134 C CG    . LEU A 1 154 ? 10.261 -4.397  1.168   1.00 28.91 ? 152  LEU B CG    1 
ATOM   1135 C CD1   . LEU A 1 154 ? 10.926 -5.556  1.883   1.00 29.41 ? 152  LEU B CD1   1 
ATOM   1136 C CD2   . LEU A 1 154 ? 10.702 -4.336  -0.290  1.00 30.25 ? 152  LEU B CD2   1 
ATOM   1137 N N     . PRO A 1 155 ? 5.544  -3.869  1.058   1.00 31.28 ? 153  PRO B N     1 
ATOM   1138 C CA    . PRO A 1 155 ? 4.226  -4.396  0.698   1.00 30.60 ? 153  PRO B CA    1 
ATOM   1139 C C     . PRO A 1 155 ? 3.607  -3.767  -0.556  1.00 32.20 ? 153  PRO B C     1 
ATOM   1140 O O     . PRO A 1 155 ? 3.058  -4.510  -1.366  1.00 29.69 ? 153  PRO B O     1 
ATOM   1141 C CB    . PRO A 1 155 ? 3.371  -4.144  1.956   1.00 34.51 ? 153  PRO B CB    1 
ATOM   1142 C CG    . PRO A 1 155 ? 4.390  -4.097  3.097   1.00 34.40 ? 153  PRO B CG    1 
ATOM   1143 C CD    . PRO A 1 155 ? 5.611  -3.446  2.472   1.00 34.87 ? 153  PRO B CD    1 
ATOM   1144 N N     . ASN A 1 156 ? 3.699  -2.440  -0.701  1.00 28.22 ? 154  ASN B N     1 
ATOM   1145 C CA    . ASN A 1 156 ? 3.079  -1.721  -1.839  1.00 30.36 ? 154  ASN B CA    1 
ATOM   1146 C C     . ASN A 1 156 ? 3.871  -2.016  -3.122  1.00 28.75 ? 154  ASN B C     1 
ATOM   1147 O O     . ASN A 1 156 ? 3.277  -1.983  -4.215  1.00 27.33 ? 154  ASN B O     1 
ATOM   1148 C CB    . ASN A 1 156 ? 2.954  -0.227  -1.550  1.00 29.89 ? 154  ASN B CB    1 
ATOM   1149 C CG    . ASN A 1 156 ? 1.680  0.083   -0.786  1.00 35.06 ? 154  ASN B CG    1 
ATOM   1150 O OD1   . ASN A 1 156 ? 0.660  -0.586  -0.975  1.00 33.51 ? 154  ASN B OD1   1 
ATOM   1151 N ND2   . ASN A 1 156 ? 1.726  1.101   0.053   1.00 32.02 ? 154  ASN B ND2   1 
ATOM   1152 N N     . MET A 1 157 ? 5.168  -2.236  -2.951  1.00 28.87 ? 155  MET B N     1 
ATOM   1153 C CA    . MET A 1 157 ? 6.132  -2.468  -4.037  1.00 28.19 ? 155  MET B CA    1 
ATOM   1154 C C     . MET A 1 157 ? 5.936  -3.894  -4.554  1.00 30.04 ? 155  MET B C     1 
ATOM   1155 O O     . MET A 1 157 ? 5.796  -4.036  -5.767  1.00 29.86 ? 155  MET B O     1 
ATOM   1156 C CB    . MET A 1 157 ? 7.554  -2.220  -3.542  1.00 28.44 ? 155  MET B CB    1 
ATOM   1157 C CG    . MET A 1 157 ? 7.828  -0.722  -3.328  1.00 29.02 ? 155  MET B CG    1 
ATOM   1158 S SD    . MET A 1 157 ? 9.490  -0.437  -2.693  1.00 29.33 ? 155  MET B SD    1 
ATOM   1159 C CE    . MET A 1 157 ? 10.418 -0.572  -4.228  1.00 34.04 ? 155  MET B CE    1 
ATOM   1160 N N     . TYR A 1 158 ? 5.797  -4.891  -3.685  1.00 29.60 ? 156  TYR B N     1 
ATOM   1161 C CA    . TYR A 1 158 ? 5.476  -6.274  -4.126  1.00 31.10 ? 156  TYR B CA    1 
ATOM   1162 C C     . TYR A 1 158 ? 4.092  -6.332  -4.780  1.00 34.86 ? 156  TYR B C     1 
ATOM   1163 O O     . TYR A 1 158 ? 3.929  -7.110  -5.737  1.00 36.08 ? 156  TYR B O     1 
ATOM   1164 C CB    . TYR A 1 158 ? 5.577  -7.264  -2.979  1.00 31.77 ? 156  TYR B CB    1 
ATOM   1165 C CG    . TYR A 1 158 ? 6.983  -7.553  -2.525  1.00 34.09 ? 156  TYR B CG    1 
ATOM   1166 C CD1   . TYR A 1 158 ? 7.976  -7.899  -3.423  1.00 33.53 ? 156  TYR B CD1   1 
ATOM   1167 C CD2   . TYR A 1 158 ? 7.317  -7.541  -1.181  1.00 34.43 ? 156  TYR B CD2   1 
ATOM   1168 C CE1   . TYR A 1 158 ? 9.253  -8.228  -3.007  1.00 32.53 ? 156  TYR B CE1   1 
ATOM   1169 C CE2   . TYR A 1 158 ? 8.603  -7.824  -0.755  1.00 34.01 ? 156  TYR B CE2   1 
ATOM   1170 C CZ    . TYR A 1 158 ? 9.580  -8.171  -1.668  1.00 31.96 ? 156  TYR B CZ    1 
ATOM   1171 O OH    . TYR A 1 158 ? 10.843 -8.479  -1.245  1.00 30.73 ? 156  TYR B OH    1 
ATOM   1172 N N     . ALA A 1 159 ? 3.140  -5.510  -4.339  1.00 34.52 ? 157  ALA B N     1 
ATOM   1173 C CA    . ALA A 1 159 ? 1.770  -5.464  -4.913  1.00 30.96 ? 157  ALA B CA    1 
ATOM   1174 C C     . ALA A 1 159 ? 1.763  -4.692  -6.226  1.00 30.14 ? 157  ALA B C     1 
ATOM   1175 O O     . ALA A 1 159 ? 0.706  -4.684  -6.880  1.00 30.20 ? 157  ALA B O     1 
ATOM   1176 C CB    . ALA A 1 159 ? 0.814  -4.810  -3.952  1.00 28.68 ? 157  ALA B CB    1 
ATOM   1177 N N     . GLY A 1 160 ? 2.827  -3.929  -6.497  1.00 29.79 ? 158  GLY B N     1 
ATOM   1178 C CA    . GLY A 1 160 ? 2.951  -3.091  -7.702  1.00 26.47 ? 158  GLY B CA    1 
ATOM   1179 C C     . GLY A 1 160 ? 2.166  -1.802  -7.594  1.00 29.68 ? 158  GLY B C     1 
ATOM   1180 O O     . GLY A 1 160 ? 2.011  -1.091  -8.627  1.00 27.09 ? 158  GLY B O     1 
ATOM   1181 N N     . ILE A 1 161 ? 1.708  -1.456  -6.389  1.00 30.38 ? 159  ILE B N     1 
ATOM   1182 C CA    . ILE A 1 161 ? 0.983  -0.177  -6.142  1.00 27.89 ? 159  ILE B CA    1 
ATOM   1183 C C     . ILE A 1 161 ? 2.015  0.965   -6.142  1.00 25.44 ? 159  ILE B C     1 
ATOM   1184 O O     . ILE A 1 161 ? 1.684  2.088   -6.618  1.00 24.51 ? 159  ILE B O     1 
ATOM   1185 C CB    . ILE A 1 161 ? 0.150  -0.308  -4.846  1.00 33.04 ? 159  ILE B CB    1 
ATOM   1186 C CG1   . ILE A 1 161 ? -1.021 -1.274  -5.084  1.00 37.08 ? 159  ILE B CG1   1 
ATOM   1187 C CG2   . ILE A 1 161 ? -0.320 1.045   -4.321  1.00 31.28 ? 159  ILE B CG2   1 
ATOM   1188 C CD1   . ILE A 1 161 ? -2.076 -1.277  -3.994  1.00 50.64 ? 159  ILE B CD1   1 
ATOM   1189 N N     . TRP A 1 162 ? 3.218  0.695   -5.655  1.00 26.22 ? 160  TRP B N     1 
ATOM   1190 C CA    . TRP A 1 162 ? 4.363  1.654   -5.713  1.00 27.86 ? 160  TRP B CA    1 
ATOM   1191 C C     . TRP A 1 162 ? 5.471  1.020   -6.555  1.00 27.52 ? 160  TRP B C     1 
ATOM   1192 O O     . TRP A 1 162 ? 5.766  -0.153  -6.341  1.00 27.40 ? 160  TRP B O     1 
ATOM   1193 C CB    . TRP A 1 162 ? 4.879  2.024   -4.312  1.00 26.64 ? 160  TRP B CB    1 
ATOM   1194 C CG    . TRP A 1 162 ? 3.903  2.789   -3.463  1.00 28.97 ? 160  TRP B CG    1 
ATOM   1195 C CD1   . TRP A 1 162 ? 2.759  3.426   -3.855  1.00 28.78 ? 160  TRP B CD1   1 
ATOM   1196 C CD2   . TRP A 1 162 ? 4.023  3.028   -2.045  1.00 29.25 ? 160  TRP B CD2   1 
ATOM   1197 N NE1   . TRP A 1 162 ? 2.164  4.034   -2.777  1.00 29.12 ? 160  TRP B NE1   1 
ATOM   1198 C CE2   . TRP A 1 162 ? 2.909  3.797   -1.655  1.00 28.42 ? 160  TRP B CE2   1 
ATOM   1199 C CE3   . TRP A 1 162 ? 4.968  2.674   -1.078  1.00 29.56 ? 160  TRP B CE3   1 
ATOM   1200 C CZ2   . TRP A 1 162 ? 2.714  4.202   -0.332  1.00 32.20 ? 160  TRP B CZ2   1 
ATOM   1201 C CZ3   . TRP A 1 162 ? 4.772  3.065   0.228   1.00 33.41 ? 160  TRP B CZ3   1 
ATOM   1202 C CH2   . TRP A 1 162 ? 3.670  3.838   0.593   1.00 30.01 ? 160  TRP B CH2   1 
ATOM   1203 N N     . ALA A 1 163 ? 6.016  1.763   -7.509  1.00 27.35 ? 161  ALA B N     1 
ATOM   1204 C CA    . ALA A 1 163 ? 7.128  1.287   -8.366  1.00 27.73 ? 161  ALA B CA    1 
ATOM   1205 C C     . ALA A 1 163 ? 8.441  1.618   -7.662  1.00 27.60 ? 161  ALA B C     1 
ATOM   1206 O O     . ALA A 1 163 ? 8.402  2.441   -6.715  1.00 26.23 ? 161  ALA B O     1 
ATOM   1207 C CB    . ALA A 1 163 ? 7.059  1.911   -9.735  1.00 27.08 ? 161  ALA B CB    1 
ATOM   1208 N N     . GLY A 1 164 ? 9.530  0.982   -8.117  1.00 27.39 ? 162  GLY B N     1 
ATOM   1209 C CA    . GLY A 1 164 ? 10.923 1.275   -7.736  1.00 26.39 ? 162  GLY B CA    1 
ATOM   1210 C C     . GLY A 1 164 ? 11.677 1.862   -8.915  1.00 26.91 ? 162  GLY B C     1 
ATOM   1211 O O     . GLY A 1 164 ? 11.151 1.820   -10.042 1.00 24.95 ? 162  GLY B O     1 
ATOM   1212 N N     . SER A 1 165 ? 12.834 2.473   -8.666  1.00 26.26 ? 163  SER B N     1 
ATOM   1213 C CA    . SER A 1 165 ? 13.789 2.926   -9.707  1.00 26.06 ? 163  SER B CA    1 
ATOM   1214 C C     . SER A 1 165 ? 15.196 2.730   -9.151  1.00 29.15 ? 163  SER B C     1 
ATOM   1215 O O     . SER A 1 165 ? 15.340 2.691   -7.926  1.00 30.13 ? 163  SER B O     1 
ATOM   1216 C CB    . SER A 1 165 ? 13.562 4.367   -10.111 1.00 28.05 ? 163  SER B CB    1 
ATOM   1217 O OG    . SER A 1 165 ? 14.261 5.251   -9.240  1.00 29.59 ? 163  SER B OG    1 
ATOM   1218 N N     . MET A 1 166 ? 16.177 2.589   -10.031 1.00 29.21 ? 164  MET B N     1 
ATOM   1219 C CA    . MET A 1 166 ? 17.624 2.546   -9.702  1.00 30.98 ? 164  MET B CA    1 
ATOM   1220 C C     . MET A 1 166 ? 18.223 3.862   -10.190 1.00 27.97 ? 164  MET B C     1 
ATOM   1221 O O     . MET A 1 166 ? 18.251 4.091   -11.409 1.00 22.17 ? 164  MET B O     1 
ATOM   1222 C CB    . MET A 1 166 ? 18.296 1.375   -10.410 1.00 37.40 ? 164  MET B CB    1 
ATOM   1223 C CG    . MET A 1 166 ? 17.524 0.085   -10.320 1.00 48.14 ? 164  MET B CG    1 
ATOM   1224 S SD    . MET A 1 166 ? 17.707 -0.689  -8.697  1.00 69.62 ? 164  MET B SD    1 
ATOM   1225 C CE    . MET A 1 166 ? 16.405 0.100   -7.757  1.00 68.53 ? 164  MET B CE    1 
ATOM   1226 N N     . CYS A 1 167 ? 18.569 4.751   -9.269  1.00 26.91 ? 165  CYS B N     1 
ATOM   1227 C CA    . CYS A 1 167 ? 19.067 6.100   -9.611  1.00 27.54 ? 165  CYS B CA    1 
ATOM   1228 C C     . CYS A 1 167 ? 20.576 6.102   -9.359  1.00 28.32 ? 165  CYS B C     1 
ATOM   1229 O O     . CYS A 1 167 ? 20.985 6.493   -8.253  1.00 28.04 ? 165  CYS B O     1 
ATOM   1230 C CB    . CYS A 1 167 ? 18.361 7.175   -8.805  1.00 26.45 ? 165  CYS B CB    1 
ATOM   1231 S SG    . CYS A 1 167 ? 16.653 7.498   -9.305  1.00 27.74 ? 165  CYS B SG    1 
ATOM   1232 N N     . LEU A 1 168 ? 21.369 5.634   -10.331 1.00 29.60 ? 166  LEU B N     1 
ATOM   1233 C CA    . LEU A 1 168 ? 22.835 5.435   -10.166 1.00 29.08 ? 166  LEU B CA    1 
ATOM   1234 C C     . LEU A 1 168 ? 23.587 6.432   -11.048 1.00 28.49 ? 166  LEU B C     1 
ATOM   1235 O O     . LEU A 1 168 ? 24.354 7.257   -10.506 1.00 28.37 ? 166  LEU B O     1 
ATOM   1236 C CB    . LEU A 1 168 ? 23.196 3.989   -10.518 1.00 29.30 ? 166  LEU B CB    1 
ATOM   1237 C CG    . LEU A 1 168 ? 22.191 2.922   -10.097 1.00 32.41 ? 166  LEU B CG    1 
ATOM   1238 C CD1   . LEU A 1 168 ? 22.778 1.539   -10.337 1.00 33.77 ? 166  LEU B CD1   1 
ATOM   1239 C CD2   . LEU A 1 168 ? 21.779 3.064   -8.634  1.00 34.96 ? 166  LEU B CD2   1 
ATOM   1240 N N     . THR A 1 169 ? 23.300 6.392   -12.351 1.00 28.23 ? 167  THR B N     1 
ATOM   1241 C CA    . THR A 1 169 ? 24.085 7.029   -13.425 1.00 27.16 ? 167  THR B CA    1 
ATOM   1242 C C     . THR A 1 169 ? 23.968 8.550   -13.308 1.00 27.83 ? 167  THR B C     1 
ATOM   1243 O O     . THR A 1 169 ? 22.868 9.040   -13.004 1.00 25.12 ? 167  THR B O     1 
ATOM   1244 C CB    . THR A 1 169 ? 23.610 6.534   -14.793 1.00 26.67 ? 167  THR B CB    1 
ATOM   1245 O OG1   . THR A 1 169 ? 23.743 5.107   -14.824 1.00 25.20 ? 167  THR B OG1   1 
ATOM   1246 C CG2   . THR A 1 169 ? 24.370 7.188   -15.923 1.00 26.52 ? 167  THR B CG2   1 
ATOM   1247 N N     . GLU A 1 170 ? 25.083 9.242   -13.545 1.00 26.51 ? 168  GLU B N     1 
ATOM   1248 C CA    . GLU A 1 170 ? 25.195 10.721  -13.639 1.00 28.68 ? 168  GLU B CA    1 
ATOM   1249 C C     . GLU A 1 170 ? 25.824 11.016  -15.001 1.00 31.58 ? 168  GLU B C     1 
ATOM   1250 O O     . GLU A 1 170 ? 26.349 10.101  -15.642 1.00 27.97 ? 168  GLU B O     1 
ATOM   1251 C CB    . GLU A 1 170 ? 26.027 11.276  -12.476 1.00 28.35 ? 168  GLU B CB    1 
ATOM   1252 C CG    . GLU A 1 170 ? 25.516 10.839  -11.110 1.00 31.15 ? 168  GLU B CG    1 
ATOM   1253 C CD    . GLU A 1 170 ? 26.190 11.478  -9.905  1.00 33.01 ? 168  GLU B CD    1 
ATOM   1254 O OE1   . GLU A 1 170 ? 27.254 12.099  -10.088 1.00 34.15 ? 168  GLU B OE1   1 
ATOM   1255 O OE2   . GLU A 1 170 ? 25.652 11.363  -8.781  1.00 32.50 ? 168  GLU B OE2   1 
ATOM   1256 N N     . PRO A 1 171 ? 25.743 12.263  -15.520 1.00 35.05 ? 169  PRO B N     1 
ATOM   1257 C CA    . PRO A 1 171 ? 26.310 12.567  -16.841 1.00 36.32 ? 169  PRO B CA    1 
ATOM   1258 C C     . PRO A 1 171 ? 27.751 12.034  -17.025 1.00 37.08 ? 169  PRO B C     1 
ATOM   1259 O O     . PRO A 1 171 ? 27.992 11.379  -18.027 1.00 38.37 ? 169  PRO B O     1 
ATOM   1260 C CB    . PRO A 1 171 ? 26.193 14.108  -16.927 1.00 36.21 ? 169  PRO B CB    1 
ATOM   1261 C CG    . PRO A 1 171 ? 25.021 14.452  -16.004 1.00 35.44 ? 169  PRO B CG    1 
ATOM   1262 C CD    . PRO A 1 171 ? 25.078 13.425  -14.893 1.00 35.61 ? 169  PRO B CD    1 
ATOM   1263 N N     . HIS A 1 172 ? 28.632 12.232  -16.041 1.00 34.11 ? 170  HIS B N     1 
ATOM   1264 C CA    . HIS A 1 172 ? 30.079 11.899  -16.104 1.00 36.92 ? 170  HIS B CA    1 
ATOM   1265 C C     . HIS A 1 172 ? 30.341 10.486  -15.599 1.00 35.56 ? 170  HIS B C     1 
ATOM   1266 O O     . HIS A 1 172 ? 31.500 10.095  -15.656 1.00 35.35 ? 170  HIS B O     1 
ATOM   1267 C CB    . HIS A 1 172 ? 30.958 12.881  -15.306 1.00 42.53 ? 170  HIS B CB    1 
ATOM   1268 C CG    . HIS A 1 172 ? 31.068 14.249  -15.895 1.00 51.79 ? 170  HIS B CG    1 
ATOM   1269 N ND1   . HIS A 1 172 ? 30.626 14.558  -17.179 1.00 62.54 ? 170  HIS B ND1   1 
ATOM   1270 C CD2   . HIS A 1 172 ? 31.618 15.386  -15.404 1.00 62.20 ? 170  HIS B CD2   1 
ATOM   1271 C CE1   . HIS A 1 172 ? 30.868 15.830  -17.438 1.00 65.12 ? 170  HIS B CE1   1 
ATOM   1272 N NE2   . HIS A 1 172 ? 31.477 16.363  -16.363 1.00 65.96 ? 170  HIS B NE2   1 
ATOM   1273 N N     . ALA A 1 173 ? 29.343 9.764   -15.077 1.00 34.55 ? 171  ALA B N     1 
ATOM   1274 C CA    . ALA A 1 173 ? 29.575 8.500   -14.329 1.00 32.37 ? 171  ALA B CA    1 
ATOM   1275 C C     . ALA A 1 173 ? 28.564 7.437   -14.761 1.00 31.76 ? 171  ALA B C     1 
ATOM   1276 O O     . ALA A 1 173 ? 27.384 7.509   -14.368 1.00 31.75 ? 171  ALA B O     1 
ATOM   1277 C CB    . ALA A 1 173 ? 29.509 8.753   -12.835 1.00 34.87 ? 171  ALA B CB    1 
ATOM   1278 N N     . GLY A 1 174 ? 29.008 6.477   -15.558 1.00 32.00 ? 172  GLY B N     1 
ATOM   1279 C CA    . GLY A 1 174 ? 28.168 5.353   -16.013 1.00 30.18 ? 172  GLY B CA    1 
ATOM   1280 C C     . GLY A 1 174 ? 28.715 4.052   -15.495 1.00 27.58 ? 172  GLY B C     1 
ATOM   1281 O O     . GLY A 1 174 ? 28.196 3.538   -14.501 1.00 27.54 ? 172  GLY B O     1 
ATOM   1282 N N     . THR A 1 175 ? 29.722 3.516   -16.172 1.00 27.04 ? 173  THR B N     1 
ATOM   1283 C CA    . THR A 1 175 ? 30.471 2.321   -15.722 1.00 27.43 ? 173  THR B CA    1 
ATOM   1284 C C     . THR A 1 175 ? 31.164 2.634   -14.386 1.00 28.98 ? 173  THR B C     1 
ATOM   1285 O O     . THR A 1 175 ? 31.159 1.780   -13.514 1.00 29.64 ? 173  THR B O     1 
ATOM   1286 C CB    . THR A 1 175 ? 31.490 1.885   -16.784 1.00 27.85 ? 173  THR B CB    1 
ATOM   1287 O OG1   . THR A 1 175 ? 30.787 1.636   -18.005 1.00 28.07 ? 173  THR B OG1   1 
ATOM   1288 C CG2   . THR A 1 175 ? 32.271 0.674   -16.332 1.00 27.68 ? 173  THR B CG2   1 
ATOM   1289 N N     . ASP A 1 176 ? 31.748 3.825   -14.260 1.00 29.64 ? 174  ASP B N     1 
ATOM   1290 C CA    . ASP A 1 176 ? 32.617 4.251   -13.128 1.00 32.83 ? 174  ASP B CA    1 
ATOM   1291 C C     . ASP A 1 176 ? 31.724 4.999   -12.114 1.00 31.63 ? 174  ASP B C     1 
ATOM   1292 O O     . ASP A 1 176 ? 31.677 6.259   -12.107 1.00 32.23 ? 174  ASP B O     1 
ATOM   1293 C CB    . ASP A 1 176 ? 33.784 5.039   -13.731 1.00 32.96 ? 174  ASP B CB    1 
ATOM   1294 C CG    . ASP A 1 176 ? 34.851 5.541   -12.776 1.00 38.48 ? 174  ASP B CG    1 
ATOM   1295 O OD1   . ASP A 1 176 ? 34.762 5.188   -11.593 1.00 35.15 ? 174  ASP B OD1   1 
ATOM   1296 O OD2   . ASP A 1 176 ? 35.744 6.320   -13.254 1.00 39.54 ? 174  ASP B OD2   1 
ATOM   1297 N N     . LEU A 1 177 ? 30.962 4.250   -11.327 1.00 31.61 ? 175  LEU B N     1 
ATOM   1298 C CA    . LEU A 1 177 ? 30.043 4.833   -10.312 1.00 33.91 ? 175  LEU B CA    1 
ATOM   1299 C C     . LEU A 1 177 ? 30.870 5.474   -9.184  1.00 35.52 ? 175  LEU B C     1 
ATOM   1300 O O     . LEU A 1 177 ? 30.395 6.448   -8.583  1.00 40.59 ? 175  LEU B O     1 
ATOM   1301 C CB    . LEU A 1 177 ? 29.091 3.729   -9.846  1.00 32.64 ? 175  LEU B CB    1 
ATOM   1302 C CG    . LEU A 1 177 ? 28.079 3.316   -10.913 1.00 35.74 ? 175  LEU B CG    1 
ATOM   1303 C CD1   . LEU A 1 177 ? 27.193 2.186   -10.442 1.00 38.56 ? 175  LEU B CD1   1 
ATOM   1304 C CD2   . LEU A 1 177 ? 27.240 4.503   -11.357 1.00 33.98 ? 175  LEU B CD2   1 
ATOM   1305 N N     . GLY A 1 178 ? 32.127 5.064   -9.048  1.00 32.13 ? 176  GLY B N     1 
ATOM   1306 C CA    . GLY A 1 178 ? 33.100 5.588   -8.077  1.00 34.49 ? 176  GLY B CA    1 
ATOM   1307 C C     . GLY A 1 178 ? 33.245 7.100   -8.099  1.00 35.96 ? 176  GLY B C     1 
ATOM   1308 O O     . GLY A 1 178 ? 33.572 7.653   -7.041  1.00 38.91 ? 176  GLY B O     1 
ATOM   1309 N N     . ILE A 1 179 ? 33.053 7.760   -9.239  1.00 35.15 ? 177  ILE B N     1 
ATOM   1310 C CA    . ILE A 1 179 ? 33.228 9.242   -9.357  1.00 37.55 ? 177  ILE B CA    1 
ATOM   1311 C C     . ILE A 1 179 ? 31.881 9.987   -9.242  1.00 36.42 ? 177  ILE B C     1 
ATOM   1312 O O     . ILE A 1 179 ? 31.849 11.173  -9.609  1.00 41.69 ? 177  ILE B O     1 
ATOM   1313 C CB    . ILE A 1 179 ? 33.998 9.602   -10.649 1.00 40.73 ? 177  ILE B CB    1 
ATOM   1314 C CG1   . ILE A 1 179 ? 33.272 9.171   -11.931 1.00 42.53 ? 177  ILE B CG1   1 
ATOM   1315 C CG2   . ILE A 1 179 ? 35.405 9.026   -10.597 1.00 45.67 ? 177  ILE B CG2   1 
ATOM   1316 C CD1   . ILE A 1 179 ? 33.781 9.858   -13.195 1.00 43.24 ? 177  ILE B CD1   1 
ATOM   1317 N N     . ILE A 1 180 ? 30.808 9.373   -8.738  1.00 35.22 ? 178  ILE B N     1 
ATOM   1318 C CA    . ILE A 1 180 ? 29.487 10.070  -8.629  1.00 38.34 ? 178  ILE B CA    1 
ATOM   1319 C C     . ILE A 1 180 ? 29.609 11.226  -7.627  1.00 38.60 ? 178  ILE B C     1 
ATOM   1320 O O     . ILE A 1 180 ? 30.475 11.120  -6.750  1.00 39.02 ? 178  ILE B O     1 
ATOM   1321 C CB    . ILE A 1 180 ? 28.340 9.123   -8.234  1.00 37.86 ? 178  ILE B CB    1 
ATOM   1322 C CG1   . ILE A 1 180 ? 28.558 8.462   -6.873  1.00 41.25 ? 178  ILE B CG1   1 
ATOM   1323 C CG2   . ILE A 1 180 ? 28.058 8.103   -9.332  1.00 39.60 ? 178  ILE B CG2   1 
ATOM   1324 C CD1   . ILE A 1 180 ? 27.282 8.363   -6.079  1.00 43.91 ? 178  ILE B CD1   1 
ATOM   1325 N N     . ARG A 1 181 ? 28.759 12.254  -7.766  1.00 35.80 ? 179  ARG B N     1 
ATOM   1326 C CA    . ARG A 1 181 ? 28.833 13.552  -7.036  1.00 42.02 ? 179  ARG B CA    1 
ATOM   1327 C C     . ARG A 1 181 ? 27.542 13.892  -6.272  1.00 35.92 ? 179  ARG B C     1 
ATOM   1328 O O     . ARG A 1 181 ? 27.565 14.880  -5.526  1.00 33.38 ? 179  ARG B O     1 
ATOM   1329 C CB    . ARG A 1 181 ? 29.111 14.689  -8.028  1.00 49.52 ? 179  ARG B CB    1 
ATOM   1330 C CG    . ARG A 1 181 ? 30.579 14.841  -8.407  1.00 63.35 ? 179  ARG B CG    1 
ATOM   1331 C CD    . ARG A 1 181 ? 31.517 14.617  -7.227  1.00 73.35 ? 179  ARG B CD    1 
ATOM   1332 N NE    . ARG A 1 181 ? 32.836 15.192  -7.455  1.00 83.84 ? 179  ARG B NE    1 
ATOM   1333 C CZ    . ARG A 1 181 ? 33.760 14.683  -8.269  1.00 88.53 ? 179  ARG B CZ    1 
ATOM   1334 N NH1   . ARG A 1 181 ? 33.534 13.565  -8.945  1.00 89.10 ? 179  ARG B NH1   1 
ATOM   1335 N NH2   . ARG A 1 181 ? 34.916 15.305  -8.411  1.00 88.92 ? 179  ARG B NH2   1 
ATOM   1336 N N     . THR A 1 182 ? 26.435 13.188  -6.492  1.00 33.40 ? 180  THR B N     1 
ATOM   1337 C CA    . THR A 1 182 ? 25.167 13.425  -5.746  1.00 30.98 ? 180  THR B CA    1 
ATOM   1338 C C     . THR A 1 182 ? 25.455 13.356  -4.245  1.00 32.48 ? 180  THR B C     1 
ATOM   1339 O O     . THR A 1 182 ? 26.115 12.389  -3.781  1.00 33.15 ? 180  THR B O     1 
ATOM   1340 C CB    . THR A 1 182 ? 24.079 12.421  -6.132  1.00 31.77 ? 180  THR B CB    1 
ATOM   1341 O OG1   . THR A 1 182 ? 23.792 12.646  -7.510  1.00 29.13 ? 180  THR B OG1   1 
ATOM   1342 C CG2   . THR A 1 182 ? 22.798 12.568  -5.333  1.00 34.75 ? 180  THR B CG2   1 
ATOM   1343 N N     . ARG A 1 183 ? 24.938 14.336  -3.510  1.00 32.87 ? 181  ARG B N     1 
ATOM   1344 C CA    . ARG A 1 183 ? 25.275 14.577  -2.091  1.00 36.89 ? 181  ARG B CA    1 
ATOM   1345 C C     . ARG A 1 183 ? 24.073 14.190  -1.217  1.00 32.58 ? 181  ARG B C     1 
ATOM   1346 O O     . ARG A 1 183 ? 22.923 14.399  -1.646  1.00 31.04 ? 181  ARG B O     1 
ATOM   1347 C CB    . ARG A 1 183 ? 25.694 16.043  -1.971  1.00 40.75 ? 181  ARG B CB    1 
ATOM   1348 C CG    . ARG A 1 183 ? 26.416 16.406  -0.685  1.00 48.22 ? 181  ARG B CG    1 
ATOM   1349 C CD    . ARG A 1 183 ? 26.868 17.853  -0.838  1.00 52.01 ? 181  ARG B CD    1 
ATOM   1350 N NE    . ARG A 1 183 ? 27.628 18.370  0.294   1.00 52.74 ? 181  ARG B NE    1 
ATOM   1351 C CZ    . ARG A 1 183 ? 28.932 18.182  0.498   1.00 52.80 ? 181  ARG B CZ    1 
ATOM   1352 N NH1   . ARG A 1 183 ? 29.661 17.455  -0.333  1.00 49.53 ? 181  ARG B NH1   1 
ATOM   1353 N NH2   . ARG A 1 183 ? 29.508 18.730  1.550   1.00 54.63 ? 181  ARG B NH2   1 
ATOM   1354 N N     . ALA A 1 184 ? 24.348 13.616  -0.053  1.00 34.31 ? 182  ALA B N     1 
ATOM   1355 C CA    . ALA A 1 184 ? 23.362 13.251  0.979   1.00 33.47 ? 182  ALA B CA    1 
ATOM   1356 C C     . ALA A 1 184 ? 23.724 13.960  2.294   1.00 36.61 ? 182  ALA B C     1 
ATOM   1357 O O     . ALA A 1 184 ? 24.697 13.547  2.916   1.00 37.54 ? 182  ALA B O     1 
ATOM   1358 C CB    . ALA A 1 184 ? 23.348 11.751  1.131   1.00 32.99 ? 182  ALA B CB    1 
ATOM   1359 N N     . GLU A 1 185 ? 22.956 14.979  2.685   1.00 37.26 ? 183  GLU B N     1 
ATOM   1360 C CA    . GLU A 1 185 ? 23.166 15.776  3.931   1.00 39.49 ? 183  GLU B CA    1 
ATOM   1361 C C     . GLU A 1 185 ? 22.401 15.133  5.085   1.00 36.97 ? 183  GLU B C     1 
ATOM   1362 O O     . GLU A 1 185 ? 21.179 15.009  5.004   1.00 34.52 ? 183  GLU B O     1 
ATOM   1363 C CB    . GLU A 1 185 ? 22.664 17.207  3.734   1.00 41.94 ? 183  GLU B CB    1 
ATOM   1364 C CG    . GLU A 1 185 ? 23.500 18.012  2.772   1.00 49.19 ? 183  GLU B CG    1 
ATOM   1365 C CD    . GLU A 1 185 ? 24.855 18.432  3.315   1.00 55.41 ? 183  GLU B CD    1 
ATOM   1366 O OE1   . GLU A 1 185 ? 25.753 18.681  2.484   1.00 63.32 ? 183  GLU B OE1   1 
ATOM   1367 O OE2   . GLU A 1 185 ? 25.008 18.510  4.560   1.00 55.58 ? 183  GLU B OE2   1 
ATOM   1368 N N     . PRO A 1 186 ? 23.060 14.711  6.194   1.00 34.97 ? 184  PRO B N     1 
ATOM   1369 C CA    . PRO A 1 186 ? 22.329 14.160  7.338   1.00 36.59 ? 184  PRO B CA    1 
ATOM   1370 C C     . PRO A 1 186 ? 21.434 15.228  8.003   1.00 34.82 ? 184  PRO B C     1 
ATOM   1371 O O     . PRO A 1 186 ? 21.840 16.372  8.121   1.00 33.48 ? 184  PRO B O     1 
ATOM   1372 C CB    . PRO A 1 186 ? 23.389 13.595  8.296   1.00 35.99 ? 184  PRO B CB    1 
ATOM   1373 C CG    . PRO A 1 186 ? 24.738 13.888  7.663   1.00 37.46 ? 184  PRO B CG    1 
ATOM   1374 C CD    . PRO A 1 186 ? 24.509 14.726  6.413   1.00 36.39 ? 184  PRO B CD    1 
ATOM   1375 N N     . GLN A 1 187 ? 20.206 14.839  8.360   1.00 34.91 ? 185  GLN B N     1 
ATOM   1376 C CA    . GLN A 1 187 ? 19.203 15.692  9.045   1.00 34.68 ? 185  GLN B CA    1 
ATOM   1377 C C     . GLN A 1 187 ? 19.078 15.223  10.502  1.00 35.93 ? 185  GLN B C     1 
ATOM   1378 O O     . GLN A 1 187 ? 19.331 14.018  10.781  1.00 34.36 ? 185  GLN B O     1 
ATOM   1379 C CB    . GLN A 1 187 ? 17.856 15.610  8.320   1.00 35.62 ? 185  GLN B CB    1 
ATOM   1380 C CG    . GLN A 1 187 ? 17.950 15.964  6.844   1.00 34.62 ? 185  GLN B CG    1 
ATOM   1381 C CD    . GLN A 1 187 ? 18.457 17.369  6.598   1.00 35.11 ? 185  GLN B CD    1 
ATOM   1382 O OE1   . GLN A 1 187 ? 17.838 18.354  6.984   1.00 36.63 ? 185  GLN B OE1   1 
ATOM   1383 N NE2   . GLN A 1 187 ? 19.584 17.476  5.914   1.00 34.78 ? 185  GLN B NE2   1 
ATOM   1384 N N     . ALA A 1 188 ? 18.690 16.111  11.418  1.00 36.41 ? 186  ALA B N     1 
ATOM   1385 C CA    . ALA A 1 188 ? 18.597 15.744  12.851  1.00 34.44 ? 186  ALA B CA    1 
ATOM   1386 C C     . ALA A 1 188 ? 17.527 14.660  13.035  1.00 36.05 ? 186  ALA B C     1 
ATOM   1387 O O     . ALA A 1 188 ? 17.700 13.836  13.937  1.00 37.72 ? 186  ALA B O     1 
ATOM   1388 C CB    . ALA A 1 188 ? 18.323 16.955  13.701  1.00 36.50 ? 186  ALA B CB    1 
ATOM   1389 N N     . ASP A 1 189 ? 16.478 14.625  12.200  1.00 34.77 ? 187  ASP B N     1 
ATOM   1390 C CA    . ASP A 1 189 ? 15.363 13.653  12.358  1.00 34.44 ? 187  ASP B CA    1 
ATOM   1391 C C     . ASP A 1 189 ? 15.760 12.235  11.917  1.00 32.89 ? 187  ASP B C     1 
ATOM   1392 O O     . ASP A 1 189 ? 14.865 11.386  11.901  1.00 37.07 ? 187  ASP B O     1 
ATOM   1393 C CB    . ASP A 1 189 ? 14.087 14.107  11.627  1.00 36.63 ? 187  ASP B CB    1 
ATOM   1394 C CG    . ASP A 1 189 ? 14.220 14.241  10.114  1.00 37.70 ? 187  ASP B CG    1 
ATOM   1395 O OD1   . ASP A 1 189 ? 15.244 13.800  9.565   1.00 35.39 ? 187  ASP B OD1   1 
ATOM   1396 O OD2   . ASP A 1 189 ? 13.294 14.798  9.491   1.00 34.40 ? 187  ASP B OD2   1 
ATOM   1397 N N     . GLY A 1 190 ? 17.011 11.961  11.551  1.00 34.18 ? 188  GLY B N     1 
ATOM   1398 C CA    . GLY A 1 190 ? 17.429 10.604  11.117  1.00 35.43 ? 188  GLY B CA    1 
ATOM   1399 C C     . GLY A 1 190 ? 17.374 10.414  9.594   1.00 34.35 ? 188  GLY B C     1 
ATOM   1400 O O     . GLY A 1 190 ? 18.004 9.469   9.094   1.00 35.65 ? 188  GLY B O     1 
ATOM   1401 N N     . SER A 1 191 ? 16.693 11.302  8.870   1.00 30.17 ? 189  SER B N     1 
ATOM   1402 C CA    . SER A 1 191 ? 16.642 11.327  7.381   1.00 31.29 ? 189  SER B CA    1 
ATOM   1403 C C     . SER A 1 191 ? 17.886 12.021  6.778   1.00 30.85 ? 189  SER B C     1 
ATOM   1404 O O     . SER A 1 191 ? 18.740 12.559  7.519   1.00 34.46 ? 189  SER B O     1 
ATOM   1405 C CB    . SER A 1 191 ? 15.365 11.987  6.915   1.00 30.87 ? 189  SER B CB    1 
ATOM   1406 O OG    . SER A 1 191 ? 15.507 13.395  6.881   1.00 29.60 ? 189  SER B OG    1 
ATOM   1407 N N     . TYR A 1 192 ? 18.006 11.966  5.456   1.00 29.90 ? 190  TYR B N     1 
ATOM   1408 C CA    . TYR A 1 192 ? 19.026 12.689  4.661   1.00 32.51 ? 190  TYR B CA    1 
ATOM   1409 C C     . TYR A 1 192 ? 18.312 13.542  3.623   1.00 32.58 ? 190  TYR B C     1 
ATOM   1410 O O     . TYR A 1 192 ? 17.152 13.224  3.305   1.00 33.18 ? 190  TYR B O     1 
ATOM   1411 C CB    . TYR A 1 192 ? 19.981 11.706  3.984   1.00 33.31 ? 190  TYR B CB    1 
ATOM   1412 C CG    . TYR A 1 192 ? 20.787 10.881  4.944   1.00 31.44 ? 190  TYR B CG    1 
ATOM   1413 C CD1   . TYR A 1 192 ? 20.205 9.839   5.623   1.00 31.11 ? 190  TYR B CD1   1 
ATOM   1414 C CD2   . TYR A 1 192 ? 22.119 11.170  5.199   1.00 35.38 ? 190  TYR B CD2   1 
ATOM   1415 C CE1   . TYR A 1 192 ? 20.927 9.079   6.525   1.00 34.87 ? 190  TYR B CE1   1 
ATOM   1416 C CE2   . TYR A 1 192 ? 22.862 10.419  6.097   1.00 35.61 ? 190  TYR B CE2   1 
ATOM   1417 C CZ    . TYR A 1 192 ? 22.252 9.377   6.774   1.00 35.95 ? 190  TYR B CZ    1 
ATOM   1418 O OH    . TYR A 1 192 ? 22.932 8.605   7.667   1.00 37.75 ? 190  TYR B OH    1 
ATOM   1419 N N     . LYS A 1 193 ? 18.967 14.610  3.169   1.00 32.60 ? 191  LYS B N     1 
ATOM   1420 C CA    . LYS A 1 193 ? 18.509 15.419  2.016   1.00 32.81 ? 191  LYS B CA    1 
ATOM   1421 C C     . LYS A 1 193 ? 19.481 15.167  0.864   1.00 34.00 ? 191  LYS B C     1 
ATOM   1422 O O     . LYS A 1 193 ? 20.710 15.331  1.049   1.00 31.23 ? 191  LYS B O     1 
ATOM   1423 C CB    . LYS A 1 193 ? 18.356 16.886  2.410   1.00 35.50 ? 191  LYS B CB    1 
ATOM   1424 C CG    . LYS A 1 193 ? 17.175 17.130  3.340   1.00 38.61 ? 191  LYS B CG    1 
ATOM   1425 C CD    . LYS A 1 193 ? 16.795 18.581  3.505   1.00 40.02 ? 191  LYS B CD    1 
ATOM   1426 C CE    . LYS A 1 193 ? 15.485 18.737  4.240   1.00 39.60 ? 191  LYS B CE    1 
ATOM   1427 N NZ    . LYS A 1 193 ? 15.285 20.135  4.668   1.00 42.54 ? 191  LYS B NZ    1 
ATOM   1428 N N     . ILE A 1 194 ? 18.936 14.703  -0.258  1.00 32.09 ? 192  ILE B N     1 
ATOM   1429 C CA    . ILE A 1 194 ? 19.718 14.308  -1.461  1.00 30.55 ? 192  ILE B CA    1 
ATOM   1430 C C     . ILE A 1 194 ? 19.649 15.441  -2.468  1.00 28.24 ? 192  ILE B C     1 
ATOM   1431 O O     . ILE A 1 194 ? 18.520 15.888  -2.778  1.00 27.85 ? 192  ILE B O     1 
ATOM   1432 C CB    . ILE A 1 194 ? 19.165 13.011  -2.069  1.00 31.88 ? 192  ILE B CB    1 
ATOM   1433 C CG1   . ILE A 1 194 ? 19.027 11.882  -1.041  1.00 33.63 ? 192  ILE B CG1   1 
ATOM   1434 C CG2   . ILE A 1 194 ? 19.987 12.614  -3.281  1.00 31.50 ? 192  ILE B CG2   1 
ATOM   1435 C CD1   . ILE A 1 194 ? 20.279 11.560  -0.281  1.00 37.95 ? 192  ILE B CD1   1 
ATOM   1436 N N     . SER A 1 195 ? 20.806 15.843  -2.999  1.00 29.12 ? 193  SER B N     1 
ATOM   1437 C CA    . SER A 1 195 ? 20.936 16.876  -4.055  1.00 30.96 ? 193  SER B CA    1 
ATOM   1438 C C     . SER A 1 195 ? 21.884 16.396  -5.154  1.00 29.14 ? 193  SER B C     1 
ATOM   1439 O O     . SER A 1 195 ? 22.981 15.900  -4.840  1.00 31.23 ? 193  SER B O     1 
ATOM   1440 C CB    . SER A 1 195 ? 21.369 18.201  -3.489  1.00 30.64 ? 193  SER B CB    1 
ATOM   1441 O OG    . SER A 1 195 ? 20.347 18.718  -2.683  1.00 31.43 ? 193  SER B OG    1 
ATOM   1442 N N     . GLY A 1 196 ? 21.449 16.522  -6.408  1.00 31.48 ? 194  GLY B N     1 
ATOM   1443 C CA    . GLY A 1 196 ? 22.196 16.006  -7.567  1.00 30.38 ? 194  GLY B CA    1 
ATOM   1444 C C     . GLY A 1 196 ? 21.282 15.672  -8.724  1.00 31.49 ? 194  GLY B C     1 
ATOM   1445 O O     . GLY A 1 196 ? 20.053 15.650  -8.550  1.00 31.53 ? 194  GLY B O     1 
ATOM   1446 N N     . THR A 1 197 ? 21.883 15.427  -9.880  1.00 32.37 ? 195  THR B N     1 
ATOM   1447 C CA    . THR A 1 197 ? 21.193 15.050  -11.127 1.00 30.75 ? 195  THR B CA    1 
ATOM   1448 C C     . THR A 1 197 ? 21.621 13.621  -11.506 1.00 33.16 ? 195  THR B C     1 
ATOM   1449 O O     . THR A 1 197 ? 22.843 13.321  -11.551 1.00 32.08 ? 195  THR B O     1 
ATOM   1450 C CB    . THR A 1 197 ? 21.483 16.096  -12.205 1.00 33.63 ? 195  THR B CB    1 
ATOM   1451 O OG1   . THR A 1 197 ? 20.795 17.275  -11.782 1.00 33.00 ? 195  THR B OG1   1 
ATOM   1452 C CG2   . THR A 1 197 ? 21.020 15.674  -13.584 1.00 33.41 ? 195  THR B CG2   1 
ATOM   1453 N N     . LYS A 1 198 ? 20.639 12.758  -11.731 1.00 27.58 ? 196  LYS B N     1 
ATOM   1454 C CA    . LYS A 1 198 ? 20.839 11.397  -12.279 1.00 28.71 ? 196  LYS B CA    1 
ATOM   1455 C C     . LYS A 1 198 ? 20.301 11.436  -13.712 1.00 28.47 ? 196  LYS B C     1 
ATOM   1456 O O     . LYS A 1 198 ? 19.351 12.259  -13.989 1.00 27.26 ? 196  LYS B O     1 
ATOM   1457 C CB    . LYS A 1 198 ? 20.151 10.374  -11.373 1.00 28.73 ? 196  LYS B CB    1 
ATOM   1458 C CG    . LYS A 1 198 ? 20.666 10.331  -9.943  1.00 29.57 ? 196  LYS B CG    1 
ATOM   1459 C CD    . LYS A 1 198 ? 22.111 9.853   -9.835  1.00 28.84 ? 196  LYS B CD    1 
ATOM   1460 C CE    . LYS A 1 198 ? 22.521 9.487   -8.426  1.00 29.03 ? 196  LYS B CE    1 
ATOM   1461 N NZ    . LYS A 1 198 ? 23.897 8.947   -8.372  1.00 29.73 ? 196  LYS B NZ    1 
ATOM   1462 N N     . ILE A 1 199 ? 20.904 10.658  -14.615 1.00 26.85 ? 197  ILE B N     1 
ATOM   1463 C CA    . ILE A 1 199 ? 20.388 10.551  -16.013 1.00 26.30 ? 197  ILE B CA    1 
ATOM   1464 C C     . ILE A 1 199 ? 20.170 9.087   -16.359 1.00 23.42 ? 197  ILE B C     1 
ATOM   1465 O O     . ILE A 1 199 ? 20.736 8.225   -15.660 1.00 23.54 ? 197  ILE B O     1 
ATOM   1466 C CB    . ILE A 1 199 ? 21.327 11.202  -17.041 1.00 26.56 ? 197  ILE B CB    1 
ATOM   1467 C CG1   . ILE A 1 199 ? 22.713 10.555  -17.042 1.00 29.38 ? 197  ILE B CG1   1 
ATOM   1468 C CG2   . ILE A 1 199 ? 21.390 12.702  -16.821 1.00 28.81 ? 197  ILE B CG2   1 
ATOM   1469 C CD1   . ILE A 1 199 ? 23.486 10.766  -18.327 1.00 31.08 ? 197  ILE B CD1   1 
ATOM   1470 N N     . PHE A 1 200 ? 19.432 8.873   -17.441 1.00 23.04 ? 198  PHE B N     1 
ATOM   1471 C CA    . PHE A 1 200 ? 19.126 7.543   -18.019 1.00 25.95 ? 198  PHE B CA    1 
ATOM   1472 C C     . PHE A 1 200 ? 18.346 6.715   -16.995 1.00 24.07 ? 198  PHE B C     1 
ATOM   1473 O O     . PHE A 1 200 ? 18.550 5.488   -16.921 1.00 27.41 ? 198  PHE B O     1 
ATOM   1474 C CB    . PHE A 1 200 ? 20.406 6.817   -18.478 1.00 26.12 ? 198  PHE B CB    1 
ATOM   1475 C CG    . PHE A 1 200 ? 21.218 7.467   -19.584 1.00 27.83 ? 198  PHE B CG    1 
ATOM   1476 C CD1   . PHE A 1 200 ? 20.690 8.466   -20.399 1.00 29.62 ? 198  PHE B CD1   1 
ATOM   1477 C CD2   . PHE A 1 200 ? 22.522 7.047   -19.836 1.00 31.75 ? 198  PHE B CD2   1 
ATOM   1478 C CE1   . PHE A 1 200 ? 21.430 9.028   -21.426 1.00 30.15 ? 198  PHE B CE1   1 
ATOM   1479 C CE2   . PHE A 1 200 ? 23.272 7.626   -20.856 1.00 31.53 ? 198  PHE B CE2   1 
ATOM   1480 C CZ    . PHE A 1 200 ? 22.731 8.626   -21.638 1.00 29.63 ? 198  PHE B CZ    1 
ATOM   1481 N N     . ILE A 1 201 ? 17.486 7.344   -16.194 1.00 23.92 ? 199  ILE B N     1 
ATOM   1482 C CA    . ILE A 1 201 ? 16.758 6.597   -15.129 1.00 24.86 ? 199  ILE B CA    1 
ATOM   1483 C C     . ILE A 1 201 ? 15.458 6.026   -15.724 1.00 23.92 ? 199  ILE B C     1 
ATOM   1484 O O     . ILE A 1 201 ? 14.533 6.788   -15.983 1.00 22.71 ? 199  ILE B O     1 
ATOM   1485 C CB    . ILE A 1 201 ? 16.520 7.489   -13.895 1.00 23.91 ? 199  ILE B CB    1 
ATOM   1486 C CG1   . ILE A 1 201 ? 17.821 8.160   -13.439 1.00 23.88 ? 199  ILE B CG1   1 
ATOM   1487 C CG2   . ILE A 1 201 ? 15.860 6.681   -12.788 1.00 23.59 ? 199  ILE B CG2   1 
ATOM   1488 C CD1   . ILE A 1 201 ? 18.954 7.201   -13.248 1.00 24.05 ? 199  ILE B CD1   1 
ATOM   1489 N N     . THR A 1 202 ? 15.430 4.717   -15.934 1.00 23.58 ? 200  THR B N     1 
ATOM   1490 C CA    . THR A 1 202 ? 14.263 3.974   -16.447 1.00 26.12 ? 200  THR B CA    1 
ATOM   1491 C C     . THR A 1 202 ? 13.144 4.117   -15.405 1.00 24.95 ? 200  THR B C     1 
ATOM   1492 O O     . THR A 1 202 ? 13.415 3.858   -14.223 1.00 26.13 ? 200  THR B O     1 
ATOM   1493 C CB    . THR A 1 202 ? 14.655 2.506   -16.696 1.00 25.68 ? 200  THR B CB    1 
ATOM   1494 O OG1   . THR A 1 202 ? 15.807 2.468   -17.548 1.00 27.66 ? 200  THR B OG1   1 
ATOM   1495 C CG2   . THR A 1 202 ? 13.529 1.690   -17.286 1.00 26.61 ? 200  THR B CG2   1 
ATOM   1496 N N     . GLY A 1 203 ? 11.944 4.520   -15.810 1.00 26.41 ? 201  GLY B N     1 
ATOM   1497 C CA    . GLY A 1 203 ? 10.802 4.691   -14.882 1.00 25.03 ? 201  GLY B CA    1 
ATOM   1498 C C     . GLY A 1 203 ? 11.105 5.670   -13.738 1.00 27.49 ? 201  GLY B C     1 
ATOM   1499 O O     . GLY A 1 203 ? 10.469 5.560   -12.684 1.00 27.88 ? 201  GLY B O     1 
ATOM   1500 N N     . GLY A 1 204 ? 12.023 6.612   -13.931 1.00 25.87 ? 202  GLY B N     1 
ATOM   1501 C CA    . GLY A 1 204 ? 12.272 7.682   -12.949 1.00 26.38 ? 202  GLY B CA    1 
ATOM   1502 C C     . GLY A 1 204 ? 10.993 8.444   -12.650 1.00 27.87 ? 202  GLY B C     1 
ATOM   1503 O O     . GLY A 1 204 ? 10.765 8.828   -11.485 1.00 27.28 ? 202  GLY B O     1 
ATOM   1504 N N     . GLU A 1 205 ? 10.186 8.649   -13.684 1.00 27.81 ? 203  GLU B N     1 
ATOM   1505 C CA    . GLU A 1 205 ? 8.883  9.341   -13.612 1.00 27.71 ? 203  GLU B CA    1 
ATOM   1506 C C     . GLU A 1 205 ? 7.965  8.712   -14.667 1.00 30.64 ? 203  GLU B C     1 
ATOM   1507 O O     . GLU A 1 205 ? 8.436  8.419   -15.786 1.00 26.95 ? 203  GLU B O     1 
ATOM   1508 C CB    . GLU A 1 205 ? 9.075  10.830  -13.866 1.00 29.56 ? 203  GLU B CB    1 
ATOM   1509 C CG    . GLU A 1 205 ? 7.791  11.617  -13.787 1.00 36.37 ? 203  GLU B CG    1 
ATOM   1510 C CD    . GLU A 1 205 ? 7.197  11.569  -12.381 1.00 37.71 ? 203  GLU B CD    1 
ATOM   1511 O OE1   . GLU A 1 205 ? 7.549  12.449  -11.571 1.00 40.14 ? 203  GLU B OE1   1 
ATOM   1512 O OE2   . GLU A 1 205 ? 6.436  10.611  -12.090 1.00 34.15 ? 203  GLU B OE2   1 
ATOM   1513 N N     . HIS A 1 206 ? 6.700  8.506   -14.316 1.00 27.79 ? 204  HIS B N     1 
ATOM   1514 C CA    . HIS A 1 206 ? 5.684  7.889   -15.200 1.00 26.94 ? 204  HIS B CA    1 
ATOM   1515 C C     . HIS A 1 206 ? 4.310  8.010   -14.543 1.00 28.48 ? 204  HIS B C     1 
ATOM   1516 O O     . HIS A 1 206 ? 4.231  8.554   -13.427 1.00 27.20 ? 204  HIS B O     1 
ATOM   1517 C CB    . HIS A 1 206 ? 6.052  6.438   -15.477 1.00 25.63 ? 204  HIS B CB    1 
ATOM   1518 C CG    . HIS A 1 206 ? 6.258  5.612   -14.261 1.00 27.65 ? 204  HIS B CG    1 
ATOM   1519 N ND1   . HIS A 1 206 ? 5.208  5.219   -13.452 1.00 31.14 ? 204  HIS B ND1   1 
ATOM   1520 C CD2   . HIS A 1 206 ? 7.361  5.014   -13.770 1.00 28.23 ? 204  HIS B CD2   1 
ATOM   1521 C CE1   . HIS A 1 206 ? 5.674  4.434   -12.500 1.00 30.18 ? 204  HIS B CE1   1 
ATOM   1522 N NE2   . HIS A 1 206 ? 6.993  4.307   -12.669 1.00 29.77 ? 204  HIS B NE2   1 
ATOM   1523 N N     . ASP A 1 207 ? 3.293  7.472   -15.199 1.00 27.65 ? 205  ASP B N     1 
ATOM   1524 C CA    . ASP A 1 207 ? 1.881  7.573   -14.774 1.00 26.46 ? 205  ASP B CA    1 
ATOM   1525 C C     . ASP A 1 207 ? 1.342  6.175   -14.477 1.00 25.77 ? 205  ASP B C     1 
ATOM   1526 O O     . ASP A 1 207 ? 0.137  6.006   -14.607 1.00 25.16 ? 205  ASP B O     1 
ATOM   1527 C CB    . ASP A 1 207 ? 1.061  8.264   -15.864 1.00 28.78 ? 205  ASP B CB    1 
ATOM   1528 C CG    . ASP A 1 207 ? 1.189  7.606   -17.244 1.00 30.40 ? 205  ASP B CG    1 
ATOM   1529 O OD1   . ASP A 1 207 ? 1.960  6.619   -17.391 1.00 27.82 ? 205  ASP B OD1   1 
ATOM   1530 O OD2   . ASP A 1 207 ? 0.548  8.104   -18.159 1.00 34.95 ? 205  ASP B OD2   1 
ATOM   1531 N N     . LEU A 1 208 ? 2.176  5.208   -14.103 1.00 24.86 ? 206  LEU B N     1 
ATOM   1532 C CA    . LEU A 1 208 ? 1.690  3.821   -13.885 1.00 26.31 ? 206  LEU B CA    1 
ATOM   1533 C C     . LEU A 1 208 ? 1.287  3.619   -12.416 1.00 28.23 ? 206  LEU B C     1 
ATOM   1534 O O     . LEU A 1 208 ? 0.455  2.736   -12.174 1.00 27.43 ? 206  LEU B O     1 
ATOM   1535 C CB    . LEU A 1 208 ? 2.755  2.791   -14.260 1.00 26.31 ? 206  LEU B CB    1 
ATOM   1536 C CG    . LEU A 1 208 ? 3.293  2.824   -15.686 1.00 26.74 ? 206  LEU B CG    1 
ATOM   1537 C CD1   . LEU A 1 208 ? 4.383  1.783   -15.841 1.00 28.48 ? 206  LEU B CD1   1 
ATOM   1538 C CD2   . LEU A 1 208 ? 2.194  2.571   -16.702 1.00 27.82 ? 206  LEU B CD2   1 
ATOM   1539 N N     . THR A 1 209 ? 1.932  4.320   -11.484 1.00 27.99 ? 207  THR B N     1 
ATOM   1540 C CA    . THR A 1 209 ? 1.778  4.133   -10.015 1.00 27.89 ? 207  THR B CA    1 
ATOM   1541 C C     . THR A 1 209 ? 1.611  5.488   -9.312  1.00 29.85 ? 207  THR B C     1 
ATOM   1542 O O     . THR A 1 209 ? 2.114  6.495   -9.827  1.00 26.63 ? 207  THR B O     1 
ATOM   1543 C CB    . THR A 1 209 ? 2.977  3.395   -9.419  1.00 29.34 ? 207  THR B CB    1 
ATOM   1544 O OG1   . THR A 1 209 ? 4.144  4.141   -9.766  1.00 28.57 ? 207  THR B OG1   1 
ATOM   1545 C CG2   . THR A 1 209 ? 3.082  1.955   -9.879  1.00 29.38 ? 207  THR B CG2   1 
ATOM   1546 N N     . GLU A 1 210 ? 0.952  5.510   -8.149  1.00 29.81 ? 208  GLU B N     1 
ATOM   1547 C CA    . GLU A 1 210 ? 0.761  6.755   -7.350  1.00 30.89 ? 208  GLU B CA    1 
ATOM   1548 C C     . GLU A 1 210 ? 2.059  7.164   -6.645  1.00 30.71 ? 208  GLU B C     1 
ATOM   1549 O O     . GLU A 1 210 ? 2.155  8.335   -6.199  1.00 31.43 ? 208  GLU B O     1 
ATOM   1550 C CB    . GLU A 1 210 ? -0.312 6.539   -6.285  1.00 33.81 ? 208  GLU B CB    1 
ATOM   1551 C CG    . GLU A 1 210 ? 0.096  5.536   -5.227  1.00 32.05 ? 208  GLU B CG    1 
ATOM   1552 C CD    . GLU A 1 210 ? -0.889 5.443   -4.077  1.00 36.09 ? 208  GLU B CD    1 
ATOM   1553 O OE1   . GLU A 1 210 ? -0.534 4.840   -3.051  1.00 35.86 ? 208  GLU B OE1   1 
ATOM   1554 O OE2   . GLU A 1 210 ? -2.019 5.969   -4.228  1.00 38.28 ? 208  GLU B OE2   1 
ATOM   1555 N N     . ASN A 1 211 ? 3.006  6.239   -6.488  1.00 29.65 ? 209  ASN B N     1 
ATOM   1556 C CA    . ASN A 1 211 ? 4.329  6.567   -5.904  1.00 29.71 ? 209  ASN B CA    1 
ATOM   1557 C C     . ASN A 1 211 ? 5.426  5.787   -6.632  1.00 30.21 ? 209  ASN B C     1 
ATOM   1558 O O     . ASN A 1 211 ? 5.142  4.713   -7.205  1.00 24.92 ? 209  ASN B O     1 
ATOM   1559 C CB    . ASN A 1 211 ? 4.386  6.285   -4.407  1.00 30.41 ? 209  ASN B CB    1 
ATOM   1560 C CG    . ASN A 1 211 ? 5.286  7.233   -3.631  1.00 32.15 ? 209  ASN B CG    1 
ATOM   1561 O OD1   . ASN A 1 211 ? 6.049  8.001   -4.214  1.00 29.46 ? 209  ASN B OD1   1 
ATOM   1562 N ND2   . ASN A 1 211 ? 5.214  7.166   -2.309  1.00 29.75 ? 209  ASN B ND2   1 
ATOM   1563 N N     . ILE A 1 212 ? 6.638  6.344   -6.596  1.00 30.99 ? 210  ILE B N     1 
ATOM   1564 C CA    . ILE A 1 212 ? 7.887  5.690   -7.082  1.00 28.21 ? 210  ILE B CA    1 
ATOM   1565 C C     . ILE A 1 212 ? 8.917  5.782   -5.959  1.00 27.75 ? 210  ILE B C     1 
ATOM   1566 O O     . ILE A 1 212 ? 9.124  6.905   -5.443  1.00 27.57 ? 210  ILE B O     1 
ATOM   1567 C CB    . ILE A 1 212 ? 8.369  6.350   -8.385  1.00 28.92 ? 210  ILE B CB    1 
ATOM   1568 C CG1   . ILE A 1 212 ? 7.264  6.313   -9.445  1.00 29.99 ? 210  ILE B CG1   1 
ATOM   1569 C CG2   . ILE A 1 212 ? 9.656  5.685   -8.879  1.00 29.37 ? 210  ILE B CG2   1 
ATOM   1570 C CD1   . ILE A 1 212 ? 7.515  7.207   -10.634 1.00 30.42 ? 210  ILE B CD1   1 
ATOM   1571 N N     . ILE A 1 213 ? 9.493  4.641   -5.587  1.00 25.52 ? 211  ILE B N     1 
ATOM   1572 C CA    . ILE A 1 213 ? 10.505 4.508   -4.506  1.00 27.34 ? 211  ILE B CA    1 
ATOM   1573 C C     . ILE A 1 213 ? 11.893 4.425   -5.157  1.00 26.33 ? 211  ILE B C     1 
ATOM   1574 O O     . ILE A 1 213 ? 12.296 3.341   -5.560  1.00 31.66 ? 211  ILE B O     1 
ATOM   1575 C CB    . ILE A 1 213 ? 10.211 3.294   -3.604  1.00 27.96 ? 211  ILE B CB    1 
ATOM   1576 C CG1   . ILE A 1 213 ? 8.759  3.296   -3.105  1.00 29.70 ? 211  ILE B CG1   1 
ATOM   1577 C CG2   . ILE A 1 213 ? 11.200 3.243   -2.453  1.00 30.11 ? 211  ILE B CG2   1 
ATOM   1578 C CD1   . ILE A 1 213 ? 8.270  4.662   -2.629  1.00 30.17 ? 211  ILE B CD1   1 
ATOM   1579 N N     . HIS A 1 214 ? 12.602 5.540   -5.219  1.00 26.41 ? 212  HIS B N     1 
ATOM   1580 C CA    . HIS A 1 214 ? 13.944 5.651   -5.853  1.00 25.81 ? 212  HIS B CA    1 
ATOM   1581 C C     . HIS A 1 214 ? 15.022 5.117   -4.916  1.00 25.98 ? 212  HIS B C     1 
ATOM   1582 O O     . HIS A 1 214 ? 15.046 5.516   -3.740  1.00 28.78 ? 212  HIS B O     1 
ATOM   1583 C CB    . HIS A 1 214 ? 14.248 7.103   -6.234  1.00 24.74 ? 212  HIS B CB    1 
ATOM   1584 C CG    . HIS A 1 214 ? 13.267 7.694   -7.173  1.00 26.93 ? 212  HIS B CG    1 
ATOM   1585 N ND1   . HIS A 1 214 ? 12.404 8.726   -6.793  1.00 32.38 ? 212  HIS B ND1   1 
ATOM   1586 C CD2   . HIS A 1 214 ? 13.013 7.444   -8.472  1.00 24.93 ? 212  HIS B CD2   1 
ATOM   1587 C CE1   . HIS A 1 214 ? 11.649 9.065   -7.814  1.00 26.90 ? 212  HIS B CE1   1 
ATOM   1588 N NE2   . HIS A 1 214 ? 11.996 8.284   -8.850  1.00 31.02 ? 212  HIS B NE2   1 
ATOM   1589 N N     . LEU A 1 215 ? 15.897 4.256   -5.423  1.00 26.31 ? 213  LEU B N     1 
ATOM   1590 C CA    . LEU A 1 215 ? 17.153 3.841   -4.739  1.00 25.47 ? 213  LEU B CA    1 
ATOM   1591 C C     . LEU A 1 215 ? 18.295 4.661   -5.332  1.00 27.01 ? 213  LEU B C     1 
ATOM   1592 O O     . LEU A 1 215 ? 18.656 4.438   -6.522  1.00 25.97 ? 213  LEU B O     1 
ATOM   1593 C CB    . LEU A 1 215 ? 17.380 2.340   -4.918  1.00 26.50 ? 213  LEU B CB    1 
ATOM   1594 C CG    . LEU A 1 215 ? 16.325 1.405   -4.330  1.00 28.01 ? 213  LEU B CG    1 
ATOM   1595 C CD1   . LEU A 1 215 ? 16.917 0.021   -4.088  1.00 29.40 ? 213  LEU B CD1   1 
ATOM   1596 C CD2   . LEU A 1 215 ? 15.737 1.939   -3.034  1.00 30.40 ? 213  LEU B CD2   1 
ATOM   1597 N N     . VAL A 1 216 ? 18.796 5.627   -4.559  1.00 26.16 ? 214  VAL B N     1 
ATOM   1598 C CA    . VAL A 1 216 ? 19.693 6.695   -5.065  1.00 28.61 ? 214  VAL B CA    1 
ATOM   1599 C C     . VAL A 1 216 ? 21.103 6.478   -4.495  1.00 28.92 ? 214  VAL B C     1 
ATOM   1600 O O     . VAL A 1 216 ? 21.239 6.312   -3.244  1.00 31.20 ? 214  VAL B O     1 
ATOM   1601 C CB    . VAL A 1 216 ? 19.106 8.086   -4.744  1.00 26.62 ? 214  VAL B CB    1 
ATOM   1602 C CG1   . VAL A 1 216 ? 19.910 9.184   -5.403  1.00 27.53 ? 214  VAL B CG1   1 
ATOM   1603 C CG2   . VAL A 1 216 ? 17.648 8.218   -5.174  1.00 26.23 ? 214  VAL B CG2   1 
ATOM   1604 N N     . LEU A 1 217 ? 22.126 6.446   -5.356  1.00 29.95 ? 215  LEU B N     1 
ATOM   1605 C CA    . LEU A 1 217 ? 23.549 6.420   -4.899  1.00 28.42 ? 215  LEU B CA    1 
ATOM   1606 C C     . LEU A 1 217 ? 23.966 7.866   -4.652  1.00 29.68 ? 215  LEU B C     1 
ATOM   1607 O O     . LEU A 1 217 ? 23.702 8.719   -5.530  1.00 29.34 ? 215  LEU B O     1 
ATOM   1608 C CB    . LEU A 1 217 ? 24.475 5.760   -5.925  1.00 30.02 ? 215  LEU B CB    1 
ATOM   1609 C CG    . LEU A 1 217 ? 24.385 4.237   -6.072  1.00 32.45 ? 215  LEU B CG    1 
ATOM   1610 C CD1   . LEU A 1 217 ? 25.423 3.754   -7.085  1.00 36.24 ? 215  LEU B CD1   1 
ATOM   1611 C CD2   . LEU A 1 217 ? 24.598 3.510   -4.759  1.00 31.38 ? 215  LEU B CD2   1 
ATOM   1612 N N     . ALA A 1 218 ? 24.520 8.145   -3.466  1.00 30.96 ? 216  ALA B N     1 
ATOM   1613 C CA    . ALA A 1 218 ? 24.968 9.499   -3.080  1.00 32.77 ? 216  ALA B CA    1 
ATOM   1614 C C     . ALA A 1 218 ? 26.055 9.421   -1.997  1.00 32.95 ? 216  ALA B C     1 
ATOM   1615 O O     . ALA A 1 218 ? 26.286 8.319   -1.450  1.00 33.35 ? 216  ALA B O     1 
ATOM   1616 C CB    . ALA A 1 218 ? 23.766 10.292  -2.648  1.00 31.56 ? 216  ALA B CB    1 
ATOM   1617 N N     . LYS A 1 219 ? 26.700 10.555  -1.713  1.00 35.48 ? 217  LYS B N     1 
ATOM   1618 C CA    . LYS A 1 219 ? 27.848 10.660  -0.772  1.00 36.69 ? 217  LYS B CA    1 
ATOM   1619 C C     . LYS A 1 219 ? 27.534 11.677  0.321   1.00 36.71 ? 217  LYS B C     1 
ATOM   1620 O O     . LYS A 1 219 ? 27.132 12.820  -0.023  1.00 33.99 ? 217  LYS B O     1 
ATOM   1621 C CB    . LYS A 1 219 ? 29.104 11.085  -1.528  1.00 38.67 ? 217  LYS B CB    1 
ATOM   1622 C CG    . LYS A 1 219 ? 29.369 10.239  -2.764  1.00 42.64 ? 217  LYS B CG    1 
ATOM   1623 C CD    . LYS A 1 219 ? 30.755 10.405  -3.325  1.00 44.03 ? 217  LYS B CD    1 
ATOM   1624 C CE    . LYS A 1 219 ? 31.741 9.482   -2.660  1.00 47.35 ? 217  LYS B CE    1 
ATOM   1625 N NZ    . LYS A 1 219 ? 33.128 9.812   -3.063  1.00 53.76 ? 217  LYS B NZ    1 
ATOM   1626 N N     . LEU A 1 220 ? 27.727 11.265  1.579   1.00 38.43 ? 218  LEU B N     1 
ATOM   1627 C CA    . LEU A 1 220 ? 27.689 12.154  2.775   1.00 38.93 ? 218  LEU B CA    1 
ATOM   1628 C C     . LEU A 1 220 ? 28.791 13.202  2.636   1.00 38.03 ? 218  LEU B C     1 
ATOM   1629 O O     . LEU A 1 220 ? 29.787 12.980  1.952   1.00 34.80 ? 218  LEU B O     1 
ATOM   1630 C CB    . LEU A 1 220 ? 27.879 11.336  4.060   1.00 36.65 ? 218  LEU B CB    1 
ATOM   1631 C CG    . LEU A 1 220 ? 26.639 10.654  4.642   1.00 42.36 ? 218  LEU B CG    1 
ATOM   1632 C CD1   . LEU A 1 220 ? 26.181 9.484   3.788   1.00 46.36 ? 218  LEU B CD1   1 
ATOM   1633 C CD2   . LEU A 1 220 ? 26.906 10.156  6.068   1.00 45.31 ? 218  LEU B CD2   1 
ATOM   1634 N N     . PRO A 1 221 ? 28.641 14.371  3.292   1.00 42.02 ? 219  PRO B N     1 
ATOM   1635 C CA    . PRO A 1 221 ? 29.640 15.446  3.234   1.00 41.46 ? 219  PRO B CA    1 
ATOM   1636 C C     . PRO A 1 221 ? 31.081 15.049  3.605   1.00 42.13 ? 219  PRO B C     1 
ATOM   1637 O O     . PRO A 1 221 ? 32.016 15.547  2.998   1.00 40.39 ? 219  PRO B O     1 
ATOM   1638 C CB    . PRO A 1 221 ? 29.136 16.413  4.311   1.00 44.80 ? 219  PRO B CB    1 
ATOM   1639 C CG    . PRO A 1 221 ? 27.639 16.212  4.321   1.00 46.24 ? 219  PRO B CG    1 
ATOM   1640 C CD    . PRO A 1 221 ? 27.477 14.720  4.121   1.00 44.69 ? 219  PRO B CD    1 
ATOM   1641 N N     . ASP A 1 222 ? 31.223 14.160  4.590   1.00 44.87 ? 220  ASP B N     1 
ATOM   1642 C CA    . ASP A 1 222 ? 32.524 13.729  5.172   1.00 48.36 ? 220  ASP B CA    1 
ATOM   1643 C C     . ASP A 1 222 ? 32.953 12.378  4.586   1.00 52.57 ? 220  ASP B C     1 
ATOM   1644 O O     . ASP A 1 222 ? 33.804 11.707  5.219   1.00 48.70 ? 220  ASP B O     1 
ATOM   1645 C CB    . ASP A 1 222 ? 32.448 13.661  6.704   1.00 49.97 ? 220  ASP B CB    1 
ATOM   1646 C CG    . ASP A 1 222 ? 31.357 12.765  7.273   1.00 52.23 ? 220  ASP B CG    1 
ATOM   1647 O OD1   . ASP A 1 222 ? 30.506 12.285  6.489   1.00 51.72 ? 220  ASP B OD1   1 
ATOM   1648 O OD2   . ASP A 1 222 ? 31.361 12.556  8.506   1.00 51.57 ? 220  ASP B OD2   1 
ATOM   1649 N N     . ALA A 1 223 ? 32.407 11.984  3.432   1.00 46.04 ? 221  ALA B N     1 
ATOM   1650 C CA    . ALA A 1 223 ? 32.638 10.639  2.855   1.00 45.33 ? 221  ALA B CA    1 
ATOM   1651 C C     . ALA A 1 223 ? 34.023 10.591  2.223   1.00 45.51 ? 221  ALA B C     1 
ATOM   1652 O O     . ALA A 1 223 ? 34.478 11.588  1.658   1.00 41.47 ? 221  ALA B O     1 
ATOM   1653 C CB    . ALA A 1 223 ? 31.574 10.316  1.831   1.00 49.11 ? 221  ALA B CB    1 
ATOM   1654 N N     . PRO A 1 224 ? 34.699 9.420   2.258   1.00 45.42 ? 222  PRO B N     1 
ATOM   1655 C CA    . PRO A 1 224 ? 35.908 9.185   1.465   1.00 46.06 ? 222  PRO B CA    1 
ATOM   1656 C C     . PRO A 1 224 ? 35.717 9.442   -0.035  1.00 50.26 ? 222  PRO B C     1 
ATOM   1657 O O     . PRO A 1 224 ? 34.594 9.324   -0.522  1.00 44.71 ? 222  PRO B O     1 
ATOM   1658 C CB    . PRO A 1 224 ? 36.210 7.682   1.619   1.00 44.73 ? 222  PRO B CB    1 
ATOM   1659 C CG    . PRO A 1 224 ? 35.468 7.262   2.871   1.00 46.50 ? 222  PRO B CG    1 
ATOM   1660 C CD    . PRO A 1 224 ? 34.334 8.252   3.074   1.00 46.56 ? 222  PRO B CD    1 
ATOM   1661 N N     . ALA A 1 225 ? 36.822 9.707   -0.740  1.00 46.43 ? 223  ALA B N     1 
ATOM   1662 C CA    . ALA A 1 225 ? 36.861 9.827   -2.215  1.00 46.89 ? 223  ALA B CA    1 
ATOM   1663 C C     . ALA A 1 225 ? 36.670 8.441   -2.847  1.00 43.08 ? 223  ALA B C     1 
ATOM   1664 O O     . ALA A 1 225 ? 36.988 7.434   -2.209  1.00 44.15 ? 223  ALA B O     1 
ATOM   1665 C CB    . ALA A 1 225 ? 38.157 10.474  -2.651  1.00 49.97 ? 223  ALA B CB    1 
ATOM   1666 N N     . GLY A 1 226 ? 36.125 8.396   -4.062  1.00 41.93 ? 224  GLY B N     1 
ATOM   1667 C CA    . GLY A 1 226 ? 35.987 7.146   -4.825  1.00 41.85 ? 224  GLY B CA    1 
ATOM   1668 C C     . GLY A 1 226 ? 34.832 6.303   -4.299  1.00 43.60 ? 224  GLY B C     1 
ATOM   1669 O O     . GLY A 1 226 ? 34.032 6.797   -3.499  1.00 42.03 ? 224  GLY B O     1 
ATOM   1670 N N     . PRO A 1 227 ? 34.746 5.023   -4.738  1.00 42.91 ? 225  PRO B N     1 
ATOM   1671 C CA    . PRO A 1 227 ? 33.571 4.179   -4.519  1.00 45.90 ? 225  PRO B CA    1 
ATOM   1672 C C     . PRO A 1 227 ? 33.346 3.803   -3.044  1.00 52.01 ? 225  PRO B C     1 
ATOM   1673 O O     . PRO A 1 227 ? 32.243 3.397   -2.684  1.00 52.61 ? 225  PRO B O     1 
ATOM   1674 C CB    . PRO A 1 227 ? 33.864 2.925   -5.361  1.00 43.16 ? 225  PRO B CB    1 
ATOM   1675 C CG    . PRO A 1 227 ? 35.372 2.874   -5.434  1.00 43.62 ? 225  PRO B CG    1 
ATOM   1676 C CD    . PRO A 1 227 ? 35.803 4.323   -5.489  1.00 42.28 ? 225  PRO B CD    1 
ATOM   1677 N N     . LYS A 1 228 ? 34.375 3.996   -2.222  1.00 50.64 ? 226  LYS B N     1 
ATOM   1678 C CA    . LYS A 1 228 ? 34.370 3.639   -0.784  1.00 52.79 ? 226  LYS B CA    1 
ATOM   1679 C C     . LYS A 1 228 ? 33.639 4.724   0.004   1.00 47.15 ? 226  LYS B C     1 
ATOM   1680 O O     . LYS A 1 228 ? 33.545 4.563   1.214   1.00 44.69 ? 226  LYS B O     1 
ATOM   1681 C CB    . LYS A 1 228 ? 35.810 3.472   -0.289  1.00 57.89 ? 226  LYS B CB    1 
ATOM   1682 C CG    . LYS A 1 228 ? 36.706 2.608   -1.173  1.00 66.44 ? 226  LYS B CG    1 
ATOM   1683 C CD    . LYS A 1 228 ? 35.970 1.489   -1.909  1.00 72.79 ? 226  LYS B CD    1 
ATOM   1684 C CE    . LYS A 1 228 ? 35.106 0.614   -1.021  1.00 73.83 ? 226  LYS B CE    1 
ATOM   1685 N NZ    . LYS A 1 228 ? 35.682 -0.742  -0.880  1.00 77.56 ? 226  LYS B NZ    1 
ATOM   1686 N N     . GLY A 1 229 ? 33.192 5.803   -0.650  1.00 41.91 ? 227  GLY B N     1 
ATOM   1687 C CA    . GLY A 1 229 ? 32.431 6.891   0.002   1.00 43.54 ? 227  GLY B CA    1 
ATOM   1688 C C     . GLY A 1 229 ? 30.954 6.856   -0.366  1.00 39.67 ? 227  GLY B C     1 
ATOM   1689 O O     . GLY A 1 229 ? 30.210 7.778   0.057   1.00 41.03 ? 227  GLY B O     1 
ATOM   1690 N N     . ILE A 1 230 ? 30.535 5.833   -1.114  1.00 37.34 ? 228  ILE B N     1 
ATOM   1691 C CA    . ILE A 1 230 ? 29.201 5.790   -1.777  1.00 36.61 ? 228  ILE B CA    1 
ATOM   1692 C C     . ILE A 1 230 ? 28.217 5.089   -0.851  1.00 32.40 ? 228  ILE B C     1 
ATOM   1693 O O     . ILE A 1 230 ? 28.505 3.955   -0.423  1.00 30.94 ? 228  ILE B O     1 
ATOM   1694 C CB    . ILE A 1 230 ? 29.260 5.096   -3.149  1.00 38.92 ? 228  ILE B CB    1 
ATOM   1695 C CG1   . ILE A 1 230 ? 30.134 5.888   -4.125  1.00 40.11 ? 228  ILE B CG1   1 
ATOM   1696 C CG2   . ILE A 1 230 ? 27.844 4.867   -3.681  1.00 38.19 ? 228  ILE B CG2   1 
ATOM   1697 C CD1   . ILE A 1 230 ? 30.144 5.345   -5.535  1.00 41.03 ? 228  ILE B CD1   1 
ATOM   1698 N N     . SER A 1 231 ? 27.059 5.724   -0.653  1.00 32.20 ? 229  SER B N     1 
ATOM   1699 C CA    . SER A 1 231 ? 25.935 5.198   0.163   1.00 32.34 ? 229  SER B CA    1 
ATOM   1700 C C     . SER A 1 231 ? 24.663 5.146   -0.692  1.00 28.03 ? 229  SER B C     1 
ATOM   1701 O O     . SER A 1 231 ? 24.618 5.783   -1.747  1.00 31.66 ? 229  SER B O     1 
ATOM   1702 C CB    . SER A 1 231 ? 25.753 6.001   1.426   1.00 30.65 ? 229  SER B CB    1 
ATOM   1703 O OG    . SER A 1 231 ? 26.974 6.094   2.156   1.00 30.12 ? 229  SER B OG    1 
ATOM   1704 N N     . LEU A 1 232 ? 23.701 4.340   -0.261  1.00 29.61 ? 230  LEU B N     1 
ATOM   1705 C CA    . LEU A 1 232 ? 22.415 4.120   -0.958  1.00 27.64 ? 230  LEU B CA    1 
ATOM   1706 C C     . LEU A 1 232 ? 21.296 4.653   -0.071  1.00 28.38 ? 230  LEU B C     1 
ATOM   1707 O O     . LEU A 1 232 ? 21.302 4.339   1.121   1.00 26.41 ? 230  LEU B O     1 
ATOM   1708 C CB    . LEU A 1 232 ? 22.243 2.625   -1.239  1.00 27.70 ? 230  LEU B CB    1 
ATOM   1709 C CG    . LEU A 1 232 ? 21.009 2.232   -2.060  1.00 29.01 ? 230  LEU B CG    1 
ATOM   1710 C CD1   . LEU A 1 232 ? 21.081 2.780   -3.474  1.00 29.68 ? 230  LEU B CD1   1 
ATOM   1711 C CD2   . LEU A 1 232 ? 20.849 0.714   -2.108  1.00 30.63 ? 230  LEU B CD2   1 
ATOM   1712 N N     . PHE A 1 233 ? 20.363 5.388   -0.675  1.00 28.55 ? 231  PHE B N     1 
ATOM   1713 C CA    . PHE A 1 233 ? 19.220 6.024   0.012   1.00 29.38 ? 231  PHE B CA    1 
ATOM   1714 C C     . PHE A 1 233 ? 17.914 5.625   -0.670  1.00 28.57 ? 231  PHE B C     1 
ATOM   1715 O O     . PHE A 1 233 ? 17.853 5.586   -1.929  1.00 29.02 ? 231  PHE B O     1 
ATOM   1716 C CB    . PHE A 1 233 ? 19.420 7.541   0.026   1.00 29.24 ? 231  PHE B CB    1 
ATOM   1717 C CG    . PHE A 1 233 ? 20.726 7.913   0.675   1.00 30.14 ? 231  PHE B CG    1 
ATOM   1718 C CD1   . PHE A 1 233 ? 21.899 7.951   -0.065  1.00 30.55 ? 231  PHE B CD1   1 
ATOM   1719 C CD2   . PHE A 1 233 ? 20.804 8.139   2.041   1.00 30.31 ? 231  PHE B CD2   1 
ATOM   1720 C CE1   . PHE A 1 233 ? 23.113 8.263   0.535   1.00 30.39 ? 231  PHE B CE1   1 
ATOM   1721 C CE2   . PHE A 1 233 ? 22.022 8.429   2.642   1.00 31.53 ? 231  PHE B CE2   1 
ATOM   1722 C CZ    . PHE A 1 233 ? 23.175 8.498   1.892   1.00 30.59 ? 231  PHE B CZ    1 
ATOM   1723 N N     . LEU A 1 234 ? 16.884 5.421   0.144   1.00 27.15 ? 232  LEU B N     1 
ATOM   1724 C CA    . LEU A 1 234 ? 15.476 5.287   -0.296  1.00 26.45 ? 232  LEU B CA    1 
ATOM   1725 C C     . LEU A 1 234 ? 14.875 6.688   -0.333  1.00 27.61 ? 232  LEU B C     1 
ATOM   1726 O O     . LEU A 1 234 ? 14.783 7.319   0.718   1.00 29.73 ? 232  LEU B O     1 
ATOM   1727 C CB    . LEU A 1 234 ? 14.759 4.364   0.687   1.00 28.47 ? 232  LEU B CB    1 
ATOM   1728 C CG    . LEU A 1 234 ? 13.344 3.969   0.283   1.00 27.22 ? 232  LEU B CG    1 
ATOM   1729 C CD1   . LEU A 1 234 ? 12.952 2.687   0.979   1.00 27.84 ? 232  LEU B CD1   1 
ATOM   1730 C CD2   . LEU A 1 234 ? 12.356 5.088   0.575   1.00 28.45 ? 232  LEU B CD2   1 
ATOM   1731 N N     . VAL A 1 235 ? 14.531 7.171   -1.520  1.00 26.15 ? 233  VAL B N     1 
ATOM   1732 C CA    . VAL A 1 235 ? 13.986 8.534   -1.742  1.00 26.07 ? 233  VAL B CA    1 
ATOM   1733 C C     . VAL A 1 235 ? 12.659 8.392   -2.467  1.00 26.58 ? 233  VAL B C     1 
ATOM   1734 O O     . VAL A 1 235 ? 12.641 8.168   -3.679  1.00 26.41 ? 233  VAL B O     1 
ATOM   1735 C CB    . VAL A 1 235 ? 14.969 9.395   -2.553  1.00 26.16 ? 233  VAL B CB    1 
ATOM   1736 C CG1   . VAL A 1 235 ? 14.440 10.809  -2.728  1.00 27.57 ? 233  VAL B CG1   1 
ATOM   1737 C CG2   . VAL A 1 235 ? 16.356 9.406   -1.945  1.00 27.07 ? 233  VAL B CG2   1 
ATOM   1738 N N     . PRO A 1 236 ? 11.513 8.514   -1.763  1.00 27.62 ? 234  PRO B N     1 
ATOM   1739 C CA    . PRO A 1 236 ? 10.210 8.414   -2.415  1.00 26.78 ? 234  PRO B CA    1 
ATOM   1740 C C     . PRO A 1 236 ? 9.832  9.665   -3.206  1.00 28.00 ? 234  PRO B C     1 
ATOM   1741 O O     . PRO A 1 236 ? 10.170 10.787  -2.791  1.00 25.66 ? 234  PRO B O     1 
ATOM   1742 C CB    . PRO A 1 236 ? 9.225  8.200   -1.253  1.00 29.34 ? 234  PRO B CB    1 
ATOM   1743 C CG    . PRO A 1 236 ? 9.918  8.767   -0.042  1.00 29.95 ? 234  PRO B CG    1 
ATOM   1744 C CD    . PRO A 1 236 ? 11.411 8.700   -0.308  1.00 30.38 ? 234  PRO B CD    1 
ATOM   1745 N N     . LYS A 1 237 ? 9.089  9.458   -4.307  1.00 27.46 ? 235  LYS B N     1 
ATOM   1746 C CA    . LYS A 1 237 ? 8.546  10.563  -5.130  1.00 28.29 ? 235  LYS B CA    1 
ATOM   1747 C C     . LYS A 1 237 ? 7.613  11.411  -4.243  1.00 28.70 ? 235  LYS B C     1 
ATOM   1748 O O     . LYS A 1 237 ? 7.595  12.665  -4.348  1.00 27.29 ? 235  LYS B O     1 
ATOM   1749 C CB    . LYS A 1 237 ? 7.818  10.005  -6.357  1.00 26.31 ? 235  LYS B CB    1 
ATOM   1750 C CG    . LYS A 1 237 ? 7.111  11.055  -7.199  1.00 26.93 ? 235  LYS B CG    1 
ATOM   1751 C CD    . LYS A 1 237 ? 6.292  10.442  -8.284  1.00 28.99 ? 235  LYS B CD    1 
ATOM   1752 C CE    . LYS A 1 237 ? 5.382  11.446  -8.947  1.00 29.91 ? 235  LYS B CE    1 
ATOM   1753 N NZ    . LYS A 1 237 ? 4.670  10.804  -10.067 1.00 33.85 ? 235  LYS B NZ    1 
ATOM   1754 N N     . VAL A 1 238 ? 6.834  10.716  -3.434  1.00 28.07 ? 236  VAL B N     1 
ATOM   1755 C CA    . VAL A 1 238 ? 5.812  11.317  -2.537  1.00 30.04 ? 236  VAL B CA    1 
ATOM   1756 C C     . VAL A 1 238 ? 6.089  10.760  -1.144  1.00 29.67 ? 236  VAL B C     1 
ATOM   1757 O O     . VAL A 1 238 ? 6.139  9.507   -1.012  1.00 28.07 ? 236  VAL B O     1 
ATOM   1758 C CB    . VAL A 1 238 ? 4.389  10.982  -3.016  1.00 28.91 ? 236  VAL B CB    1 
ATOM   1759 C CG1   . VAL A 1 238 ? 3.337  11.675  -2.149  1.00 29.74 ? 236  VAL B CG1   1 
ATOM   1760 C CG2   . VAL A 1 238 ? 4.188  11.315  -4.492  1.00 30.73 ? 236  VAL B CG2   1 
ATOM   1761 N N     . LEU A 1 239 ? 6.271  11.628  -0.147  1.00 29.89 ? 237  LEU B N     1 
ATOM   1762 C CA    . LEU A 1 239 ? 6.498  11.171  1.258   1.00 32.82 ? 237  LEU B CA    1 
ATOM   1763 C C     . LEU A 1 239 ? 5.221  10.485  1.749   1.00 32.15 ? 237  LEU B C     1 
ATOM   1764 O O     . LEU A 1 239 ? 4.137  10.844  1.265   1.00 31.53 ? 237  LEU B O     1 
ATOM   1765 C CB    . LEU A 1 239 ? 6.903  12.367  2.131   1.00 35.48 ? 237  LEU B CB    1 
ATOM   1766 C CG    . LEU A 1 239 ? 8.170  13.070  1.637   1.00 36.76 ? 237  LEU B CG    1 
ATOM   1767 C CD1   . LEU A 1 239 ? 8.311  14.465  2.226   1.00 39.85 ? 237  LEU B CD1   1 
ATOM   1768 C CD2   . LEU A 1 239 ? 9.401  12.220  1.929   1.00 36.85 ? 237  LEU B CD2   1 
ATOM   1769 N N     . VAL A 1 240 ? 5.362  9.489   2.613   1.00 33.04 ? 238  VAL B N     1 
ATOM   1770 C CA    . VAL A 1 240 ? 4.245  8.619   3.061   1.00 37.93 ? 238  VAL B CA    1 
ATOM   1771 C C     . VAL A 1 240 ? 3.945  8.949   4.535   1.00 44.10 ? 238  VAL B C     1 
ATOM   1772 O O     . VAL A 1 240 ? 4.895  8.999   5.343   1.00 36.94 ? 238  VAL B O     1 
ATOM   1773 C CB    . VAL A 1 240 ? 4.576  7.131   2.836   1.00 41.18 ? 238  VAL B CB    1 
ATOM   1774 C CG1   . VAL A 1 240 ? 3.391  6.232   3.177   1.00 42.12 ? 238  VAL B CG1   1 
ATOM   1775 C CG2   . VAL A 1 240 ? 5.040  6.882   1.399   1.00 41.37 ? 238  VAL B CG2   1 
ATOM   1776 N N     . ASN A 1 241 ? 2.665  9.204   4.842   1.00 46.94 ? 239  ASN B N     1 
ATOM   1777 C CA    . ASN A 1 241 ? 2.150  9.460   6.215   1.00 48.26 ? 239  ASN B CA    1 
ATOM   1778 C C     . ASN A 1 241 ? 2.244  8.150   7.006   1.00 48.58 ? 239  ASN B C     1 
ATOM   1779 O O     . ASN A 1 241 ? 2.383  7.096   6.364   1.00 45.20 ? 239  ASN B O     1 
ATOM   1780 C CB    . ASN A 1 241 ? 0.718  9.996   6.164   1.00 45.29 ? 239  ASN B CB    1 
ATOM   1781 C CG    . ASN A 1 241 ? 0.599  11.302  5.409   1.00 44.23 ? 239  ASN B CG    1 
ATOM   1782 O OD1   . ASN A 1 241 ? 1.379  12.227  5.631   1.00 48.23 ? 239  ASN B OD1   1 
ATOM   1783 N ND2   . ASN A 1 241 ? -0.367 11.386  4.506   1.00 46.88 ? 239  ASN B ND2   1 
ATOM   1784 N N     . ALA A 1 242 ? 2.215  8.220   8.342   1.00 55.28 ? 240  ALA B N     1 
ATOM   1785 C CA    . ALA A 1 242 ? 2.210  7.067   9.282   1.00 52.21 ? 240  ALA B CA    1 
ATOM   1786 C C     . ALA A 1 242 ? 1.203  6.011   8.821   1.00 52.23 ? 240  ALA B C     1 
ATOM   1787 O O     . ALA A 1 242 ? 1.552  4.823   8.771   1.00 50.45 ? 240  ALA B O     1 
ATOM   1788 C CB    . ALA A 1 242 ? 1.861  7.565   10.657  1.00 52.19 ? 240  ALA B CB    1 
ATOM   1789 N N     . ASP A 1 243 ? -0.001 6.456   8.450   1.00 52.95 ? 241  ASP B N     1 
ATOM   1790 C CA    . ASP A 1 243 ? -1.134 5.577   8.073   1.00 54.70 ? 241  ASP B CA    1 
ATOM   1791 C C     . ASP A 1 243 ? -0.928 5.004   6.664   1.00 55.41 ? 241  ASP B C     1 
ATOM   1792 O O     . ASP A 1 243 ? -1.808 4.227   6.244   1.00 51.79 ? 241  ASP B O     1 
ATOM   1793 C CB    . ASP A 1 243 ? -2.472 6.319   8.196   1.00 56.81 ? 241  ASP B CB    1 
ATOM   1794 C CG    . ASP A 1 243 ? -2.688 7.442   7.187   1.00 62.73 ? 241  ASP B CG    1 
ATOM   1795 O OD1   . ASP A 1 243 ? -1.824 7.624   6.280   1.00 56.36 ? 241  ASP B OD1   1 
ATOM   1796 O OD2   . ASP A 1 243 ? -3.727 8.137   7.313   1.00 55.02 ? 241  ASP B OD2   1 
ATOM   1797 N N     . GLY A 1 244 ? 0.146  5.387   5.950   1.00 47.44 ? 242  GLY B N     1 
ATOM   1798 C CA    . GLY A 1 244 ? 0.523  4.800   4.651   1.00 45.21 ? 242  GLY B CA    1 
ATOM   1799 C C     . GLY A 1 244 ? -0.121 5.554   3.498   1.00 48.79 ? 242  GLY B C     1 
ATOM   1800 O O     . GLY A 1 244 ? 0.081  5.161   2.329   1.00 46.64 ? 242  GLY B O     1 
ATOM   1801 N N     . SER A 1 245 ? -0.902 6.592   3.804   1.00 46.07 ? 243  SER B N     1 
ATOM   1802 C CA    . SER A 1 245 ? -1.511 7.482   2.787   1.00 42.63 ? 243  SER B CA    1 
ATOM   1803 C C     . SER A 1 245 ? -0.407 8.407   2.264   1.00 42.29 ? 243  SER B C     1 
ATOM   1804 O O     . SER A 1 245 ? 0.610  8.553   2.972   1.00 40.26 ? 243  SER B O     1 
ATOM   1805 C CB    . SER A 1 245 ? -2.694 8.252   3.345   1.00 43.16 ? 243  SER B CB    1 
ATOM   1806 O OG    . SER A 1 245 ? -2.277 9.347   4.152   1.00 40.16 ? 243  SER B OG    1 
ATOM   1807 N N     . LEU A 1 246 ? -0.604 8.990   1.079   1.00 40.18 ? 244  LEU B N     1 
ATOM   1808 C CA    . LEU A 1 246 ? 0.381  9.895   0.437   1.00 41.01 ? 244  LEU B CA    1 
ATOM   1809 C C     . LEU A 1 246 ? 0.381  11.234  1.191   1.00 40.88 ? 244  LEU B C     1 
ATOM   1810 O O     . LEU A 1 246 ? -0.703 11.813  1.378   1.00 38.09 ? 244  LEU B O     1 
ATOM   1811 C CB    . LEU A 1 246 ? 0.025  10.081  -1.044  1.00 42.48 ? 244  LEU B CB    1 
ATOM   1812 C CG    . LEU A 1 246 ? -0.014 8.811   -1.899  1.00 43.69 ? 244  LEU B CG    1 
ATOM   1813 C CD1   . LEU A 1 246 ? -0.121 9.178   -3.374  1.00 41.54 ? 244  LEU B CD1   1 
ATOM   1814 C CD2   . LEU A 1 246 ? 1.206  7.917   -1.642  1.00 43.29 ? 244  LEU B CD2   1 
ATOM   1815 N N     . GLY A 1 247 ? 1.554  11.677  1.639   1.00 40.64 ? 245  GLY B N     1 
ATOM   1816 C CA    . GLY A 1 247 ? 1.787  13.033  2.180   1.00 39.80 ? 245  GLY B CA    1 
ATOM   1817 C C     . GLY A 1 247 ? 2.303  13.987  1.111   1.00 36.41 ? 245  GLY B C     1 
ATOM   1818 O O     . GLY A 1 247 ? 1.778  13.978  -0.017  1.00 36.15 ? 245  GLY B O     1 
ATOM   1819 N N     . GLU A 1 248 ? 3.303  14.790  1.454   1.00 37.97 ? 246  GLU B N     1 
ATOM   1820 C CA    . GLU A 1 248 ? 3.789  15.886  0.592   1.00 41.47 ? 246  GLU B CA    1 
ATOM   1821 C C     . GLU A 1 248 ? 4.652  15.290  -0.526  1.00 35.06 ? 246  GLU B C     1 
ATOM   1822 O O     . GLU A 1 248 ? 5.353  14.291  -0.288  1.00 29.93 ? 246  GLU B O     1 
ATOM   1823 C CB    . GLU A 1 248 ? 4.517  16.924  1.443   1.00 50.69 ? 246  GLU B CB    1 
ATOM   1824 C CG    . GLU A 1 248 ? 3.633  17.463  2.559   1.00 60.84 ? 246  GLU B CG    1 
ATOM   1825 C CD    . GLU A 1 248 ? 3.850  18.929  2.882   1.00 67.35 ? 246  GLU B CD    1 
ATOM   1826 O OE1   . GLU A 1 248 ? 2.907  19.725  2.663   1.00 68.32 ? 246  GLU B OE1   1 
ATOM   1827 O OE2   . GLU A 1 248 ? 4.967  19.272  3.344   1.00 72.05 ? 246  GLU B OE2   1 
ATOM   1828 N N     . LYS A 1 249 ? 4.526  15.871  -1.710  1.00 36.13 ? 247  LYS B N     1 
ATOM   1829 C CA    . LYS A 1 249 ? 5.423  15.637  -2.864  1.00 38.35 ? 247  LYS B CA    1 
ATOM   1830 C C     . LYS A 1 249 ? 6.859  15.941  -2.412  1.00 36.41 ? 247  LYS B C     1 
ATOM   1831 O O     . LYS A 1 249 ? 7.128  17.047  -1.873  1.00 34.13 ? 247  LYS B O     1 
ATOM   1832 C CB    . LYS A 1 249 ? 4.923  16.496  -4.023  1.00 40.90 ? 247  LYS B CB    1 
ATOM   1833 C CG    . LYS A 1 249 ? 5.577  16.260  -5.371  1.00 46.98 ? 247  LYS B CG    1 
ATOM   1834 C CD    . LYS A 1 249 ? 6.021  17.556  -6.076  1.00 54.03 ? 247  LYS B CD    1 
ATOM   1835 C CE    . LYS A 1 249 ? 5.656  17.620  -7.548  1.00 54.86 ? 247  LYS B CE    1 
ATOM   1836 N NZ    . LYS A 1 249 ? 5.734  16.289  -8.192  1.00 56.66 ? 247  LYS B NZ    1 
ATOM   1837 N N     . ASN A 1 250 ? 7.761  14.984  -2.584  1.00 35.35 ? 248  ASN B N     1 
ATOM   1838 C CA    . ASN A 1 250 ? 9.197  15.183  -2.262  1.00 30.10 ? 248  ASN B CA    1 
ATOM   1839 C C     . ASN A 1 250 ? 9.832  16.168  -3.246  1.00 32.82 ? 248  ASN B C     1 
ATOM   1840 O O     . ASN A 1 250 ? 9.316  16.371  -4.356  1.00 31.94 ? 248  ASN B O     1 
ATOM   1841 C CB    . ASN A 1 250 ? 9.936  13.864  -2.279  1.00 29.73 ? 248  ASN B CB    1 
ATOM   1842 C CG    . ASN A 1 250 ? 11.126 13.837  -1.350  1.00 30.21 ? 248  ASN B CG    1 
ATOM   1843 O OD1   . ASN A 1 250 ? 11.558 14.870  -0.833  1.00 27.12 ? 248  ASN B OD1   1 
ATOM   1844 N ND2   . ASN A 1 250 ? 11.654 12.645  -1.142  1.00 28.88 ? 248  ASN B ND2   1 
ATOM   1845 N N     . SER A 1 251 ? 10.975 16.712  -2.853  1.00 32.59 ? 249  SER B N     1 
ATOM   1846 C CA    . SER A 1 251 ? 11.685 17.799  -3.544  1.00 33.39 ? 249  SER B CA    1 
ATOM   1847 C C     . SER A 1 251 ? 12.575 17.224  -4.668  1.00 30.87 ? 249  SER B C     1 
ATOM   1848 O O     . SER A 1 251 ? 13.813 17.333  -4.592  1.00 29.92 ? 249  SER B O     1 
ATOM   1849 C CB    . SER A 1 251 ? 12.441 18.575  -2.493  1.00 37.37 ? 249  SER B CB    1 
ATOM   1850 O OG    . SER A 1 251 ? 12.690 19.878  -2.959  1.00 46.71 ? 249  SER B OG    1 
ATOM   1851 N N     . LEU A 1 252 ? 11.948 16.628  -5.682  1.00 28.08 ? 250  LEU B N     1 
ATOM   1852 C CA    . LEU A 1 252 ? 12.608 16.005  -6.858  1.00 27.37 ? 250  LEU B CA    1 
ATOM   1853 C C     . LEU A 1 252 ? 11.653 16.037  -8.060  1.00 28.57 ? 250  LEU B C     1 
ATOM   1854 O O     . LEU A 1 252 ? 10.424 16.171  -7.881  1.00 26.57 ? 250  LEU B O     1 
ATOM   1855 C CB    . LEU A 1 252 ? 13.025 14.569  -6.518  1.00 28.97 ? 250  LEU B CB    1 
ATOM   1856 C CG    . LEU A 1 252 ? 11.887 13.592  -6.220  1.00 30.63 ? 250  LEU B CG    1 
ATOM   1857 C CD1   . LEU A 1 252 ? 11.386 12.908  -7.488  1.00 33.94 ? 250  LEU B CD1   1 
ATOM   1858 C CD2   . LEU A 1 252 ? 12.332 12.553  -5.204  1.00 31.50 ? 250  LEU B CD2   1 
ATOM   1859 N N     . GLY A 1 253 ? 12.201 15.918  -9.265  1.00 28.53 ? 251  GLY B N     1 
ATOM   1860 C CA    . GLY A 1 253 ? 11.371 15.892  -10.477 1.00 28.83 ? 251  GLY B CA    1 
ATOM   1861 C C     . GLY A 1 253 ? 12.154 15.432  -11.675 1.00 28.50 ? 251  GLY B C     1 
ATOM   1862 O O     . GLY A 1 253 ? 13.398 15.294  -11.587 1.00 26.64 ? 251  GLY B O     1 
ATOM   1863 N N     . CYS A 1 254 ? 11.425 15.144  -12.745 1.00 29.12 ? 252  CYS B N     1 
ATOM   1864 C CA    . CYS A 1 254 ? 12.004 14.736  -14.037 1.00 29.82 ? 252  CYS B CA    1 
ATOM   1865 C C     . CYS A 1 254 ? 12.176 15.988  -14.912 1.00 28.18 ? 252  CYS B C     1 
ATOM   1866 O O     . CYS A 1 254 ? 11.180 16.673  -15.175 1.00 28.03 ? 252  CYS B O     1 
ATOM   1867 C CB    . CYS A 1 254 ? 11.120 13.678  -14.672 1.00 29.49 ? 252  CYS B CB    1 
ATOM   1868 S SG    . CYS A 1 254 ? 11.689 13.328  -16.342 1.00 30.12 ? 252  CYS B SG    1 
ATOM   1869 N N     . GLY A 1 255 ? 13.410 16.333  -15.283 1.00 28.90 ? 253  GLY B N     1 
ATOM   1870 C CA    . GLY A 1 255 ? 13.690 17.518  -16.129 1.00 29.52 ? 253  GLY B CA    1 
ATOM   1871 C C     . GLY A 1 255 ? 13.383 17.287  -17.617 1.00 27.95 ? 253  GLY B C     1 
ATOM   1872 O O     . GLY A 1 255 ? 13.023 18.243  -18.310 1.00 27.66 ? 253  GLY B O     1 
ATOM   1873 N N     . SER A 1 256 ? 13.479 16.047  -18.085 1.00 27.33 ? 254  SER B N     1 
ATOM   1874 C CA    . SER A 1 256 ? 13.337 15.658  -19.512 1.00 27.68 ? 254  SER B CA    1 
ATOM   1875 C C     . SER A 1 256 ? 13.385 14.137  -19.607 1.00 25.36 ? 254  SER B C     1 
ATOM   1876 O O     . SER A 1 256 ? 13.786 13.483  -18.620 1.00 25.18 ? 254  SER B O     1 
ATOM   1877 C CB    . SER A 1 256 ? 14.448 16.257  -20.366 1.00 29.02 ? 254  SER B CB    1 
ATOM   1878 O OG    . SER A 1 256 ? 15.722 15.838  -19.894 1.00 27.06 ? 254  SER B OG    1 
ATOM   1879 N N     . ILE A 1 257 ? 12.993 13.616  -20.761 1.00 26.19 ? 255  ILE B N     1 
ATOM   1880 C CA    . ILE A 1 257 ? 13.156 12.181  -21.096 1.00 25.74 ? 255  ILE B CA    1 
ATOM   1881 C C     . ILE A 1 257 ? 13.975 12.084  -22.387 1.00 26.84 ? 255  ILE B C     1 
ATOM   1882 O O     . ILE A 1 257 ? 13.988 13.054  -23.182 1.00 26.50 ? 255  ILE B O     1 
ATOM   1883 C CB    . ILE A 1 257 ? 11.799 11.472  -21.193 1.00 27.29 ? 255  ILE B CB    1 
ATOM   1884 C CG1   . ILE A 1 257 ? 10.953 12.016  -22.348 1.00 28.46 ? 255  ILE B CG1   1 
ATOM   1885 C CG2   . ILE A 1 257 ? 11.094 11.545  -19.844 1.00 29.04 ? 255  ILE B CG2   1 
ATOM   1886 C CD1   . ILE A 1 257 ? 9.712  11.218  -22.624 1.00 28.44 ? 255  ILE B CD1   1 
ATOM   1887 N N     . GLU A 1 258 ? 14.617 10.937  -22.592 1.00 26.50 ? 256  GLU B N     1 
ATOM   1888 C CA    . GLU A 1 258 ? 15.545 10.751  -23.737 1.00 25.98 ? 256  GLU B CA    1 
ATOM   1889 C C     . GLU A 1 258 ? 14.758 10.404  -25.003 1.00 25.51 ? 256  GLU B C     1 
ATOM   1890 O O     . GLU A 1 258 ? 13.703 9.759   -24.903 1.00 25.01 ? 256  GLU B O     1 
ATOM   1891 C CB    . GLU A 1 258 ? 16.554 9.658   -23.404 1.00 26.42 ? 256  GLU B CB    1 
ATOM   1892 C CG    . GLU A 1 258 ? 17.497 10.021  -22.267 1.00 26.93 ? 256  GLU B CG    1 
ATOM   1893 C CD    . GLU A 1 258 ? 18.277 11.325  -22.400 1.00 32.08 ? 256  GLU B CD    1 
ATOM   1894 O OE1   . GLU A 1 258 ? 18.495 11.978  -21.361 1.00 31.34 ? 256  GLU B OE1   1 
ATOM   1895 O OE2   . GLU A 1 258 ? 18.685 11.688  -23.528 1.00 33.10 ? 256  GLU B OE2   1 
ATOM   1896 N N     . HIS A 1 259 ? 15.296 10.788  -26.165 1.00 26.97 ? 257  HIS B N     1 
ATOM   1897 C CA    . HIS A 1 259 ? 14.912 10.257  -27.503 1.00 27.48 ? 257  HIS B CA    1 
ATOM   1898 C C     . HIS A 1 259 ? 15.836 9.078   -27.832 1.00 26.81 ? 257  HIS B C     1 
ATOM   1899 O O     . HIS A 1 259 ? 17.059 9.292   -27.940 1.00 23.91 ? 257  HIS B O     1 
ATOM   1900 C CB    . HIS A 1 259 ? 15.022 11.359  -28.553 1.00 31.41 ? 257  HIS B CB    1 
ATOM   1901 C CG    . HIS A 1 259 ? 14.222 12.558  -28.212 1.00 36.19 ? 257  HIS B CG    1 
ATOM   1902 N ND1   . HIS A 1 259 ? 14.813 13.774  -27.935 1.00 42.23 ? 257  HIS B ND1   1 
ATOM   1903 C CD2   . HIS A 1 259 ? 12.895 12.724  -28.061 1.00 37.93 ? 257  HIS B CD2   1 
ATOM   1904 C CE1   . HIS A 1 259 ? 13.874 14.652  -27.638 1.00 43.28 ? 257  HIS B CE1   1 
ATOM   1905 N NE2   . HIS A 1 259 ? 12.689 14.038  -27.728 1.00 42.62 ? 257  HIS B NE2   1 
ATOM   1906 N N     . LYS A 1 260 ? 15.280 7.886   -27.973 1.00 22.64 ? 258  LYS B N     1 
ATOM   1907 C CA    . LYS A 1 260 ? 16.060 6.632   -27.985 1.00 23.79 ? 258  LYS B CA    1 
ATOM   1908 C C     . LYS A 1 260 ? 15.899 5.857   -29.305 1.00 23.88 ? 258  LYS B C     1 
ATOM   1909 O O     . LYS A 1 260 ? 14.955 6.099   -30.059 1.00 21.50 ? 258  LYS B O     1 
ATOM   1910 C CB    . LYS A 1 260 ? 15.613 5.774   -26.803 1.00 23.66 ? 258  LYS B CB    1 
ATOM   1911 C CG    . LYS A 1 260 ? 15.736 6.469   -25.452 1.00 23.43 ? 258  LYS B CG    1 
ATOM   1912 C CD    . LYS A 1 260 ? 15.698 5.530   -24.268 1.00 23.52 ? 258  LYS B CD    1 
ATOM   1913 C CE    . LYS A 1 260 ? 14.427 4.719   -24.187 1.00 24.63 ? 258  LYS B CE    1 
ATOM   1914 N NZ    . LYS A 1 260 ? 13.233 5.592   -24.224 1.00 24.89 ? 258  LYS B NZ    1 
ATOM   1915 N N     . MET A 1 261 ? 16.774 4.875   -29.511 1.00 23.18 ? 259  MET B N     1 
ATOM   1916 C CA    . MET A 1 261 ? 16.682 3.934   -30.657 1.00 23.38 ? 259  MET B CA    1 
ATOM   1917 C C     . MET A 1 261 ? 15.419 3.068   -30.531 1.00 22.22 ? 259  MET B C     1 
ATOM   1918 O O     . MET A 1 261 ? 14.755 2.808   -31.533 1.00 23.15 ? 259  MET B O     1 
ATOM   1919 C CB    . MET A 1 261 ? 17.908 3.022   -30.668 1.00 23.34 ? 259  MET B CB    1 
ATOM   1920 C CG    . MET A 1 261 ? 17.957 2.111   -31.853 1.00 23.89 ? 259  MET B CG    1 
ATOM   1921 S SD    . MET A 1 261 ? 19.280 0.919   -31.715 1.00 24.48 ? 259  MET B SD    1 
ATOM   1922 C CE    . MET A 1 261 ? 19.644 0.681   -33.455 1.00 24.83 ? 259  MET B CE    1 
ATOM   1923 N N     . GLY A 1 262 ? 15.153 2.591   -29.329 1.00 22.21 ? 260  GLY B N     1 
ATOM   1924 C CA    . GLY A 1 262 ? 14.136 1.574   -29.031 1.00 22.07 ? 260  GLY B CA    1 
ATOM   1925 C C     . GLY A 1 262 ? 13.656 1.718   -27.600 1.00 21.58 ? 260  GLY B C     1 
ATOM   1926 O O     . GLY A 1 262 ? 13.930 2.766   -26.975 1.00 22.14 ? 260  GLY B O     1 
ATOM   1927 N N     . ILE A 1 263 ? 13.019 0.666   -27.109 1.00 22.23 ? 261  ILE B N     1 
ATOM   1928 C CA    . ILE A 1 263 ? 12.137 0.676   -25.915 1.00 23.18 ? 261  ILE B CA    1 
ATOM   1929 C C     . ILE A 1 263 ? 11.585 2.093   -25.721 1.00 22.65 ? 261  ILE B C     1 
ATOM   1930 O O     . ILE A 1 263 ? 11.729 2.632   -24.632 1.00 25.18 ? 261  ILE B O     1 
ATOM   1931 C CB    . ILE A 1 263 ? 12.869 0.132   -24.674 1.00 23.71 ? 261  ILE B CB    1 
ATOM   1932 C CG1   . ILE A 1 263 ? 14.136 0.897   -24.282 1.00 24.08 ? 261  ILE B CG1   1 
ATOM   1933 C CG2   . ILE A 1 263 ? 13.156 -1.350  -24.854 1.00 25.98 ? 261  ILE B CG2   1 
ATOM   1934 C CD1   . ILE A 1 263 ? 14.535 0.726   -22.845 1.00 23.06 ? 261  ILE B CD1   1 
ATOM   1935 N N     . LYS A 1 264 ? 10.871 2.625   -26.710 1.00 22.68 ? 262  LYS B N     1 
ATOM   1936 C CA    . LYS A 1 264 ? 10.462 4.051   -26.711 1.00 23.68 ? 262  LYS B CA    1 
ATOM   1937 C C     . LYS A 1 264 ? 9.344  4.282   -25.682 1.00 24.47 ? 262  LYS B C     1 
ATOM   1938 O O     . LYS A 1 264 ? 9.172  5.423   -25.247 1.00 26.34 ? 262  LYS B O     1 
ATOM   1939 C CB    . LYS A 1 264 ? 10.024 4.490   -28.098 1.00 24.33 ? 262  LYS B CB    1 
ATOM   1940 C CG    . LYS A 1 264 ? 11.169 4.650   -29.097 1.00 25.96 ? 262  LYS B CG    1 
ATOM   1941 C CD    . LYS A 1 264 ? 10.660 5.244   -30.377 1.00 26.82 ? 262  LYS B CD    1 
ATOM   1942 C CE    . LYS A 1 264 ? 11.672 5.238   -31.498 1.00 26.97 ? 262  LYS B CE    1 
ATOM   1943 N NZ    . LYS A 1 264 ? 11.184 6.127   -32.577 1.00 27.90 ? 262  LYS B NZ    1 
ATOM   1944 N N     . ALA A 1 265 ? 8.623  3.239   -25.300 1.00 23.14 ? 263  ALA B N     1 
ATOM   1945 C CA    . ALA A 1 265 ? 7.537  3.342   -24.299 1.00 23.84 ? 263  ALA B CA    1 
ATOM   1946 C C     . ALA A 1 265 ? 8.138  3.262   -22.887 1.00 24.71 ? 263  ALA B C     1 
ATOM   1947 O O     . ALA A 1 265 ? 7.384  3.412   -21.923 1.00 25.41 ? 263  ALA B O     1 
ATOM   1948 C CB    . ALA A 1 265 ? 6.503  2.277   -24.575 1.00 23.04 ? 263  ALA B CB    1 
ATOM   1949 N N     . SER A 1 266 ? 9.466  3.098   -22.764 1.00 23.80 ? 264  SER B N     1 
ATOM   1950 C CA    . SER A 1 266 ? 10.202 3.048   -21.480 1.00 23.43 ? 264  SER B CA    1 
ATOM   1951 C C     . SER A 1 266 ? 10.736 4.448   -21.189 1.00 27.46 ? 264  SER B C     1 
ATOM   1952 O O     . SER A 1 266 ? 11.689 4.892   -21.868 1.00 26.03 ? 264  SER B O     1 
ATOM   1953 C CB    . SER A 1 266 ? 11.291 2.050   -21.529 1.00 22.93 ? 264  SER B CB    1 
ATOM   1954 O OG    . SER A 1 266 ? 12.006 1.956   -20.310 1.00 24.30 ? 264  SER B OG    1 
ATOM   1955 N N     . ALA A 1 267 ? 10.125 5.143   -20.235 1.00 26.83 ? 265  ALA B N     1 
ATOM   1956 C CA    . ALA A 1 267 ? 10.502 6.542   -19.922 1.00 27.10 ? 265  ALA B CA    1 
ATOM   1957 C C     . ALA A 1 267 ? 11.918 6.504   -19.343 1.00 25.52 ? 265  ALA B C     1 
ATOM   1958 O O     . ALA A 1 267 ? 12.133 5.772   -18.357 1.00 27.72 ? 265  ALA B O     1 
ATOM   1959 C CB    . ALA A 1 267 ? 9.523  7.171   -18.972 1.00 27.89 ? 265  ALA B CB    1 
ATOM   1960 N N     . THR A 1 268 ? 12.844 7.211   -19.991 1.00 25.01 ? 266  THR B N     1 
ATOM   1961 C CA    . THR A 1 268 ? 14.274 7.279   -19.620 1.00 24.39 ? 266  THR B CA    1 
ATOM   1962 C C     . THR A 1 268 ? 14.557 8.717   -19.174 1.00 24.16 ? 266  THR B C     1 
ATOM   1963 O O     . THR A 1 268 ? 14.566 9.607   -20.011 1.00 24.04 ? 266  THR B O     1 
ATOM   1964 C CB    . THR A 1 268 ? 15.121 6.740   -20.775 1.00 25.07 ? 266  THR B CB    1 
ATOM   1965 O OG1   . THR A 1 268 ? 14.606 5.438   -21.093 1.00 24.36 ? 266  THR B OG1   1 
ATOM   1966 C CG2   . THR A 1 268 ? 16.574 6.648   -20.381 1.00 24.81 ? 266  THR B CG2   1 
ATOM   1967 N N     . CYS A 1 269 ? 14.687 8.935   -17.863 1.00 26.56 ? 267  CYS B N     1 
ATOM   1968 C CA    . CYS A 1 269 ? 14.467 10.264  -17.240 1.00 25.47 ? 267  CYS B CA    1 
ATOM   1969 C C     . CYS A 1 269 ? 15.768 10.893  -16.743 1.00 23.78 ? 267  CYS B C     1 
ATOM   1970 O O     . CYS A 1 269 ? 16.582 10.196  -16.084 1.00 23.36 ? 267  CYS B O     1 
ATOM   1971 C CB    . CYS A 1 269 ? 13.507 10.114  -16.076 1.00 26.61 ? 267  CYS B CB    1 
ATOM   1972 S SG    . CYS A 1 269 ? 11.913 9.450   -16.613 1.00 28.55 ? 267  CYS B SG    1 
ATOM   1973 N N     . VAL A 1 270 ? 15.902 12.191  -16.972 1.00 24.94 ? 268  VAL B N     1 
ATOM   1974 C CA    . VAL A 1 270 ? 16.823 13.045  -16.170 1.00 27.38 ? 268  VAL B CA    1 
ATOM   1975 C C     . VAL A 1 270 ? 16.071 13.381  -14.874 1.00 26.29 ? 268  VAL B C     1 
ATOM   1976 O O     . VAL A 1 270 ? 15.011 14.038  -14.959 1.00 26.95 ? 268  VAL B O     1 
ATOM   1977 C CB    . VAL A 1 270 ? 17.238 14.323  -16.911 1.00 28.89 ? 268  VAL B CB    1 
ATOM   1978 C CG1   . VAL A 1 270 ? 17.935 15.289  -15.966 1.00 34.24 ? 268  VAL B CG1   1 
ATOM   1979 C CG2   . VAL A 1 270 ? 18.094 14.035  -18.157 1.00 31.57 ? 268  VAL B CG2   1 
ATOM   1980 N N     . MET A 1 271 ? 16.588 12.894  -13.751 1.00 27.02 ? 269  MET B N     1 
ATOM   1981 C CA    . MET A 1 271 ? 16.014 13.073  -12.391 1.00 27.82 ? 269  MET B CA    1 
ATOM   1982 C C     . MET A 1 271 ? 16.838 14.097  -11.589 1.00 26.99 ? 269  MET B C     1 
ATOM   1983 O O     . MET A 1 271 ? 18.047 13.894  -11.391 1.00 25.66 ? 269  MET B O     1 
ATOM   1984 C CB    . MET A 1 271 ? 15.966 11.728  -11.666 1.00 26.79 ? 269  MET B CB    1 
ATOM   1985 C CG    . MET A 1 271 ? 15.040 10.713  -12.339 1.00 26.98 ? 269  MET B CG    1 
ATOM   1986 S SD    . MET A 1 271 ? 13.321 11.303  -12.566 1.00 28.76 ? 269  MET B SD    1 
ATOM   1987 C CE    . MET A 1 271 ? 12.812 11.491  -10.860 1.00 30.01 ? 269  MET B CE    1 
ATOM   1988 N N     . ASN A 1 272 ? 16.196 15.204  -11.200 1.00 27.30 ? 270  ASN B N     1 
ATOM   1989 C CA    . ASN A 1 272 ? 16.779 16.299  -10.377 1.00 27.04 ? 270  ASN B CA    1 
ATOM   1990 C C     . ASN A 1 272 ? 16.270 16.171  -8.939  1.00 26.52 ? 270  ASN B C     1 
ATOM   1991 O O     . ASN A 1 272 ? 15.049 16.203  -8.730  1.00 27.24 ? 270  ASN B O     1 
ATOM   1992 C CB    . ASN A 1 272 ? 16.465 17.666  -10.981 1.00 26.85 ? 270  ASN B CB    1 
ATOM   1993 C CG    . ASN A 1 272 ? 16.990 17.730  -12.399 1.00 29.07 ? 270  ASN B CG    1 
ATOM   1994 O OD1   . ASN A 1 272 ? 18.193 17.571  -12.642 1.00 29.20 ? 270  ASN B OD1   1 
ATOM   1995 N ND2   . ASN A 1 272 ? 16.097 17.946  -13.336 1.00 29.35 ? 270  ASN B ND2   1 
ATOM   1996 N N     . PHE A 1 273 ? 17.188 15.945  -8.007  1.00 28.43 ? 271  PHE B N     1 
ATOM   1997 C CA    . PHE A 1 273 ? 16.946 15.923  -6.545  1.00 30.26 ? 271  PHE B CA    1 
ATOM   1998 C C     . PHE A 1 273 ? 17.386 17.280  -5.982  1.00 33.63 ? 271  PHE B C     1 
ATOM   1999 O O     . PHE A 1 273 ? 18.539 17.661  -6.200  1.00 32.83 ? 271  PHE B O     1 
ATOM   2000 C CB    . PHE A 1 273 ? 17.671 14.734  -5.921  1.00 29.15 ? 271  PHE B CB    1 
ATOM   2001 C CG    . PHE A 1 273 ? 17.269 13.402  -6.499  1.00 30.18 ? 271  PHE B CG    1 
ATOM   2002 C CD1   . PHE A 1 273 ? 17.870 12.907  -7.651  1.00 30.37 ? 271  PHE B CD1   1 
ATOM   2003 C CD2   . PHE A 1 273 ? 16.267 12.645  -5.901  1.00 31.33 ? 271  PHE B CD2   1 
ATOM   2004 C CE1   . PHE A 1 273 ? 17.490 11.678  -8.177  1.00 28.51 ? 271  PHE B CE1   1 
ATOM   2005 C CE2   . PHE A 1 273 ? 15.876 11.429  -6.440  1.00 29.59 ? 271  PHE B CE2   1 
ATOM   2006 C CZ    . PHE A 1 273 ? 16.497 10.937  -7.568  1.00 29.69 ? 271  PHE B CZ    1 
ATOM   2007 N N     . ASP A 1 274 ? 16.476 18.005  -5.330  1.00 34.03 ? 272  ASP B N     1 
ATOM   2008 C CA    . ASP A 1 274 ? 16.765 19.334  -4.730  1.00 35.15 ? 272  ASP B CA    1 
ATOM   2009 C C     . ASP A 1 274 ? 16.489 19.241  -3.224  1.00 34.30 ? 272  ASP B C     1 
ATOM   2010 O O     . ASP A 1 274 ? 15.382 19.615  -2.799  1.00 34.47 ? 272  ASP B O     1 
ATOM   2011 C CB    . ASP A 1 274 ? 15.953 20.430  -5.414  1.00 36.85 ? 272  ASP B CB    1 
ATOM   2012 C CG    . ASP A 1 274 ? 16.297 21.832  -4.923  1.00 41.47 ? 272  ASP B CG    1 
ATOM   2013 O OD1   . ASP A 1 274 ? 17.377 21.999  -4.344  1.00 41.32 ? 272  ASP B OD1   1 
ATOM   2014 O OD2   . ASP A 1 274 ? 15.469 22.749  -5.119  1.00 44.82 ? 272  ASP B OD2   1 
ATOM   2015 N N     . GLY A 1 275 ? 17.422 18.681  -2.464  1.00 31.56 ? 273  GLY B N     1 
ATOM   2016 C CA    . GLY A 1 275 ? 17.245 18.478  -1.014  1.00 33.90 ? 273  GLY B CA    1 
ATOM   2017 C C     . GLY A 1 275 ? 16.073 17.550  -0.727  1.00 34.08 ? 273  GLY B C     1 
ATOM   2018 O O     . GLY A 1 275 ? 15.307 17.795  0.229   1.00 32.72 ? 273  GLY B O     1 
ATOM   2019 N N     . ALA A 1 276 ? 15.964 16.484  -1.511  1.00 31.98 ? 274  ALA B N     1 
ATOM   2020 C CA    . ALA A 1 276 ? 14.893 15.474  -1.412  1.00 31.73 ? 274  ALA B CA    1 
ATOM   2021 C C     . ALA A 1 276 ? 15.138 14.640  -0.159  1.00 31.48 ? 274  ALA B C     1 
ATOM   2022 O O     . ALA A 1 276 ? 16.289 14.199  0.062   1.00 29.66 ? 274  ALA B O     1 
ATOM   2023 C CB    . ALA A 1 276 ? 14.861 14.608  -2.647  1.00 32.42 ? 274  ALA B CB    1 
ATOM   2024 N N     . THR A 1 277 ? 14.086 14.420  0.623   1.00 29.60 ? 275  THR B N     1 
ATOM   2025 C CA    . THR A 1 277 ? 14.134 13.570  1.829   1.00 30.65 ? 275  THR B CA    1 
ATOM   2026 C C     . THR A 1 277 ? 14.273 12.109  1.402   1.00 28.30 ? 275  THR B C     1 
ATOM   2027 O O     . THR A 1 277 ? 13.527 11.654  0.521   1.00 31.50 ? 275  THR B O     1 
ATOM   2028 C CB    . THR A 1 277 ? 12.879 13.744  2.699   1.00 32.05 ? 275  THR B CB    1 
ATOM   2029 O OG1   . THR A 1 277 ? 12.830 15.101  3.150   1.00 30.69 ? 275  THR B OG1   1 
ATOM   2030 C CG2   . THR A 1 277 ? 12.861 12.773  3.857   1.00 32.46 ? 275  THR B CG2   1 
ATOM   2031 N N     . GLY A 1 278 ? 15.181 11.405  2.048   1.00 28.35 ? 276  GLY B N     1 
ATOM   2032 C CA    . GLY A 1 278 ? 15.323 9.953   1.922   1.00 29.10 ? 276  GLY B CA    1 
ATOM   2033 C C     . GLY A 1 278 ? 16.022 9.385   3.124   1.00 29.36 ? 276  GLY B C     1 
ATOM   2034 O O     . GLY A 1 278 ? 16.382 10.156  4.034   1.00 32.56 ? 276  GLY B O     1 
ATOM   2035 N N     . TRP A 1 279 ? 16.196 8.069   3.138   1.00 28.76 ? 277  TRP B N     1 
ATOM   2036 C CA    . TRP A 1 279 ? 16.686 7.316   4.312   1.00 28.82 ? 277  TRP B CA    1 
ATOM   2037 C C     . TRP A 1 279 ? 17.753 6.364   3.828   1.00 30.54 ? 277  TRP B C     1 
ATOM   2038 O O     . TRP A 1 279 ? 17.623 5.866   2.698   1.00 27.51 ? 277  TRP B O     1 
ATOM   2039 C CB    . TRP A 1 279 ? 15.561 6.559   5.019   1.00 28.84 ? 277  TRP B CB    1 
ATOM   2040 C CG    . TRP A 1 279 ? 14.586 7.486   5.660   1.00 33.25 ? 277  TRP B CG    1 
ATOM   2041 C CD1   . TRP A 1 279 ? 14.607 7.950   6.946   1.00 32.23 ? 277  TRP B CD1   1 
ATOM   2042 C CD2   . TRP A 1 279 ? 13.469 8.123   5.015   1.00 31.23 ? 277  TRP B CD2   1 
ATOM   2043 N NE1   . TRP A 1 279 ? 13.564 8.815   7.142   1.00 31.38 ? 277  TRP B NE1   1 
ATOM   2044 C CE2   . TRP A 1 279 ? 12.854 8.946   5.980   1.00 31.52 ? 277  TRP B CE2   1 
ATOM   2045 C CE3   . TRP A 1 279 ? 12.932 8.076   3.724   1.00 35.60 ? 277  TRP B CE3   1 
ATOM   2046 C CZ2   . TRP A 1 279 ? 11.708 9.686   5.706   1.00 34.42 ? 277  TRP B CZ2   1 
ATOM   2047 C CZ3   . TRP A 1 279 ? 11.807 8.827   3.444   1.00 36.23 ? 277  TRP B CZ3   1 
ATOM   2048 C CH2   . TRP A 1 279 ? 11.206 9.621   4.427   1.00 36.65 ? 277  TRP B CH2   1 
ATOM   2049 N N     . LEU A 1 280 ? 18.758 6.157   4.661   1.00 30.79 ? 278  LEU B N     1 
ATOM   2050 C CA    . LEU A 1 280 ? 19.907 5.286   4.358   1.00 30.66 ? 278  LEU B CA    1 
ATOM   2051 C C     . LEU A 1 280 ? 19.396 3.852   4.240   1.00 30.88 ? 278  LEU B C     1 
ATOM   2052 O O     . LEU A 1 280 ? 18.582 3.425   5.071   1.00 30.40 ? 278  LEU B O     1 
ATOM   2053 C CB    . LEU A 1 280 ? 20.951 5.421   5.471   1.00 31.37 ? 278  LEU B CB    1 
ATOM   2054 C CG    . LEU A 1 280 ? 22.100 4.415   5.454   1.00 30.52 ? 278  LEU B CG    1 
ATOM   2055 C CD1   . LEU A 1 280 ? 23.102 4.741   4.358   1.00 31.19 ? 278  LEU B CD1   1 
ATOM   2056 C CD2   . LEU A 1 280 ? 22.801 4.382   6.818   1.00 33.93 ? 278  LEU B CD2   1 
ATOM   2057 N N     . VAL A 1 281 ? 19.886 3.148   3.227   1.00 31.08 ? 279  VAL B N     1 
ATOM   2058 C CA    . VAL A 1 281 ? 19.711 1.682   3.034   1.00 32.17 ? 279  VAL B CA    1 
ATOM   2059 C C     . VAL A 1 281 ? 21.062 1.033   3.336   1.00 30.21 ? 279  VAL B C     1 
ATOM   2060 O O     . VAL A 1 281 ? 22.059 1.428   2.677   1.00 33.41 ? 279  VAL B O     1 
ATOM   2061 C CB    . VAL A 1 281 ? 19.238 1.361   1.600   1.00 30.23 ? 279  VAL B CB    1 
ATOM   2062 C CG1   . VAL A 1 281 ? 19.064 -0.142  1.393   1.00 30.53 ? 279  VAL B CG1   1 
ATOM   2063 C CG2   . VAL A 1 281 ? 17.968 2.114   1.238   1.00 31.11 ? 279  VAL B CG2   1 
ATOM   2064 N N     . GLY A 1 282 ? 21.084 0.023   4.205   1.00 32.53 ? 280  GLY B N     1 
ATOM   2065 C CA    . GLY A 1 282 ? 22.318 -0.679  4.607   1.00 34.46 ? 280  GLY B CA    1 
ATOM   2066 C C     . GLY A 1 282 ? 23.250 0.270   5.354   1.00 36.92 ? 280  GLY B C     1 
ATOM   2067 O O     . GLY A 1 282 ? 22.756 1.047   6.218   1.00 34.68 ? 280  GLY B O     1 
ATOM   2068 N N     . GLU A 1 283 ? 24.528 0.304   4.985   1.00 34.45 ? 281  GLU B N     1 
ATOM   2069 C CA    . GLU A 1 283 ? 25.553 1.006   5.790   1.00 36.36 ? 281  GLU B CA    1 
ATOM   2070 C C     . GLU A 1 283 ? 26.168 2.162   5.007   1.00 34.74 ? 281  GLU B C     1 
ATOM   2071 O O     . GLU A 1 283 ? 26.334 2.040   3.785   1.00 35.80 ? 281  GLU B O     1 
ATOM   2072 C CB    . GLU A 1 283 ? 26.621 0.015   6.229   1.00 38.82 ? 281  GLU B CB    1 
ATOM   2073 C CG    . GLU A 1 283 ? 26.055 -1.226  6.887   1.00 42.75 ? 281  GLU B CG    1 
ATOM   2074 C CD    . GLU A 1 283 ? 27.149 -2.227  7.205   1.00 46.78 ? 281  GLU B CD    1 
ATOM   2075 O OE1   . GLU A 1 283 ? 28.090 -1.839  7.931   1.00 49.31 ? 281  GLU B OE1   1 
ATOM   2076 O OE2   . GLU A 1 283 ? 27.086 -3.368  6.697   1.00 48.41 ? 281  GLU B OE2   1 
ATOM   2077 N N     . VAL A 1 284 ? 26.547 3.231   5.710   1.00 36.60 ? 282  VAL B N     1 
ATOM   2078 C CA    . VAL A 1 284 ? 27.349 4.335   5.113   1.00 36.43 ? 282  VAL B CA    1 
ATOM   2079 C C     . VAL A 1 284 ? 28.550 3.694   4.416   1.00 33.66 ? 282  VAL B C     1 
ATOM   2080 O O     . VAL A 1 284 ? 29.093 2.683   4.941   1.00 31.75 ? 282  VAL B O     1 
ATOM   2081 C CB    . VAL A 1 284 ? 27.788 5.388   6.148   1.00 40.55 ? 282  VAL B CB    1 
ATOM   2082 C CG1   . VAL A 1 284 ? 26.594 6.095   6.759   1.00 41.34 ? 282  VAL B CG1   1 
ATOM   2083 C CG2   . VAL A 1 284 ? 28.670 4.788   7.229   1.00 45.81 ? 282  VAL B CG2   1 
ATOM   2084 N N     . ASN A 1 285 ? 28.861 4.212   3.231   1.00 33.03 ? 283  ASN B N     1 
ATOM   2085 C CA    . ASN A 1 285 ? 30.036 3.868   2.395   1.00 35.41 ? 283  ASN B CA    1 
ATOM   2086 C C     . ASN A 1 285 ? 29.916 2.459   1.794   1.00 33.83 ? 283  ASN B C     1 
ATOM   2087 O O     . ASN A 1 285 ? 30.891 2.055   1.138   1.00 33.54 ? 283  ASN B O     1 
ATOM   2088 C CB    . ASN A 1 285 ? 31.346 4.028   3.179   1.00 35.13 ? 283  ASN B CB    1 
ATOM   2089 C CG    . ASN A 1 285 ? 31.535 5.427   3.720   1.00 38.04 ? 283  ASN B CG    1 
ATOM   2090 O OD1   . ASN A 1 285 ? 31.168 6.413   3.089   1.00 40.12 ? 283  ASN B OD1   1 
ATOM   2091 N ND2   . ASN A 1 285 ? 32.086 5.524   4.914   1.00 42.99 ? 283  ASN B ND2   1 
ATOM   2092 N N     . LYS A 1 286 ? 28.796 1.741   1.962   1.00 36.60 ? 284  LYS B N     1 
ATOM   2093 C CA    . LYS A 1 286 ? 28.639 0.366   1.387   1.00 34.41 ? 284  LYS B CA    1 
ATOM   2094 C C     . LYS A 1 286 ? 27.435 0.326   0.435   1.00 28.94 ? 284  LYS B C     1 
ATOM   2095 O O     . LYS A 1 286 ? 26.844 -0.744  0.290   1.00 30.32 ? 284  LYS B O     1 
ATOM   2096 C CB    . LYS A 1 286 ? 28.526 -0.666  2.508   1.00 36.49 ? 284  LYS B CB    1 
ATOM   2097 C CG    . LYS A 1 286 ? 29.635 -0.520  3.538   1.00 42.03 ? 284  LYS B CG    1 
ATOM   2098 C CD    . LYS A 1 286 ? 29.883 -1.709  4.413   1.00 44.71 ? 284  LYS B CD    1 
ATOM   2099 C CE    . LYS A 1 286 ? 30.922 -1.388  5.478   1.00 49.32 ? 284  LYS B CE    1 
ATOM   2100 N NZ    . LYS A 1 286 ? 30.631 -2.045  6.775   1.00 48.33 ? 284  LYS B NZ    1 
ATOM   2101 N N     . GLY A 1 287 ? 27.148 1.443   -0.224  1.00 30.87 ? 285  GLY B N     1 
ATOM   2102 C CA    . GLY A 1 287 ? 26.055 1.593   -1.202  1.00 33.39 ? 285  GLY B CA    1 
ATOM   2103 C C     . GLY A 1 287 ? 26.200 0.664   -2.399  1.00 35.32 ? 285  GLY B C     1 
ATOM   2104 O O     . GLY A 1 287 ? 25.176 0.080   -2.829  1.00 33.57 ? 285  GLY B O     1 
ATOM   2105 N N     . LEU A 1 288 ? 27.411 0.493   -2.924  1.00 32.74 ? 286  LEU B N     1 
ATOM   2106 C CA    . LEU A 1 288 ? 27.633 -0.439  -4.063  1.00 35.88 ? 286  LEU B CA    1 
ATOM   2107 C C     . LEU A 1 288 ? 27.343 -1.862  -3.586  1.00 33.32 ? 286  LEU B C     1 
ATOM   2108 O O     . LEU A 1 288 ? 26.603 -2.613  -4.283  1.00 31.05 ? 286  LEU B O     1 
ATOM   2109 C CB    . LEU A 1 288 ? 29.056 -0.270  -4.606  1.00 35.32 ? 286  LEU B CB    1 
ATOM   2110 C CG    . LEU A 1 288 ? 29.368 1.130   -5.139  1.00 38.34 ? 286  LEU B CG    1 
ATOM   2111 C CD1   . LEU A 1 288 ? 30.817 1.241   -5.594  1.00 41.88 ? 286  LEU B CD1   1 
ATOM   2112 C CD2   . LEU A 1 288 ? 28.418 1.497   -6.275  1.00 39.96 ? 286  LEU B CD2   1 
ATOM   2113 N N     . ALA A 1 289 ? 27.843 -2.223  -2.411  1.00 32.77 ? 287  ALA B N     1 
ATOM   2114 C CA    . ALA A 1 289 ? 27.716 -3.614  -1.914  1.00 32.31 ? 287  ALA B CA    1 
ATOM   2115 C C     . ALA A 1 289 ? 26.243 -3.917  -1.621  1.00 32.07 ? 287  ALA B C     1 
ATOM   2116 O O     . ALA A 1 289 ? 25.848 -5.089  -1.681  1.00 29.61 ? 287  ALA B O     1 
ATOM   2117 C CB    . ALA A 1 289 ? 28.605 -3.825  -0.707  1.00 37.16 ? 287  ALA B CB    1 
ATOM   2118 N N     . ALA A 1 290 ? 25.438 -2.904  -1.305  1.00 30.92 ? 288  ALA B N     1 
ATOM   2119 C CA    . ALA A 1 290 ? 24.001 -3.094  -1.000  1.00 31.57 ? 288  ALA B CA    1 
ATOM   2120 C C     . ALA A 1 290 ? 23.239 -3.542  -2.272  1.00 32.90 ? 288  ALA B C     1 
ATOM   2121 O O     . ALA A 1 290 ? 22.086 -4.004  -2.162  1.00 35.47 ? 288  ALA B O     1 
ATOM   2122 C CB    . ALA A 1 290 ? 23.429 -1.822  -0.449  1.00 28.58 ? 288  ALA B CB    1 
ATOM   2123 N N     . MET A 1 291 ? 23.848 -3.406  -3.447  1.00 34.52 ? 289  MET B N     1 
ATOM   2124 C CA    . MET A 1 291 ? 23.226 -3.824  -4.730  1.00 37.33 ? 289  MET B CA    1 
ATOM   2125 C C     . MET A 1 291 ? 23.798 -5.150  -5.234  1.00 37.74 ? 289  MET B C     1 
ATOM   2126 O O     . MET A 1 291 ? 23.344 -5.572  -6.329  1.00 34.39 ? 289  MET B O     1 
ATOM   2127 C CB    . MET A 1 291 ? 23.417 -2.745  -5.792  1.00 37.01 ? 289  MET B CB    1 
ATOM   2128 C CG    . MET A 1 291 ? 22.955 -1.399  -5.305  1.00 39.31 ? 289  MET B CG    1 
ATOM   2129 S SD    . MET A 1 291 ? 22.906 -0.188  -6.614  1.00 46.88 ? 289  MET B SD    1 
ATOM   2130 C CE    . MET A 1 291 ? 21.128 0.014   -6.751  1.00 57.92 ? 289  MET B CE    1 
ATOM   2131 N N     . PHE A 1 292 ? 24.683 -5.827  -4.495  1.00 38.15 ? 290  PHE B N     1 
ATOM   2132 C CA    . PHE A 1 292 ? 25.378 -7.030  -5.037  1.00 43.17 ? 290  PHE B CA    1 
ATOM   2133 C C     . PHE A 1 292 ? 24.333 -8.117  -5.368  1.00 42.45 ? 290  PHE B C     1 
ATOM   2134 O O     . PHE A 1 292 ? 24.374 -8.622  -6.504  1.00 39.73 ? 290  PHE B O     1 
ATOM   2135 C CB    . PHE A 1 292 ? 26.534 -7.497  -4.137  1.00 47.72 ? 290  PHE B CB    1 
ATOM   2136 C CG    . PHE A 1 292 ? 27.815 -6.681  -4.213  1.00 53.50 ? 290  PHE B CG    1 
ATOM   2137 C CD1   . PHE A 1 292 ? 28.000 -5.670  -5.161  1.00 52.82 ? 290  PHE B CD1   1 
ATOM   2138 C CD2   . PHE A 1 292 ? 28.863 -6.928  -3.323  1.00 56.04 ? 290  PHE B CD2   1 
ATOM   2139 C CE1   . PHE A 1 292 ? 29.181 -4.933  -5.206  1.00 54.96 ? 290  PHE B CE1   1 
ATOM   2140 C CE2   . PHE A 1 292 ? 30.043 -6.190  -3.370  1.00 52.30 ? 290  PHE B CE2   1 
ATOM   2141 C CZ    . PHE A 1 292 ? 30.198 -5.189  -4.308  1.00 53.48 ? 290  PHE B CZ    1 
ATOM   2142 N N     . THR A 1 293 ? 23.400 -8.450  -4.467  1.00 39.99 ? 291  THR B N     1 
ATOM   2143 C CA    . THR A 1 293 ? 22.402 -9.528  -4.712  1.00 38.18 ? 291  THR B CA    1 
ATOM   2144 C C     . THR A 1 293 ? 21.488 -9.091  -5.851  1.00 36.14 ? 291  THR B C     1 
ATOM   2145 O O     . THR A 1 293 ? 21.184 -9.915  -6.736  1.00 34.21 ? 291  THR B O     1 
ATOM   2146 C CB    . THR A 1 293 ? 21.598 -9.901  -3.460  1.00 44.65 ? 291  THR B CB    1 
ATOM   2147 O OG1   . THR A 1 293 ? 22.542 -10.484 -2.567  1.00 47.48 ? 291  THR B OG1   1 
ATOM   2148 C CG2   . THR A 1 293 ? 20.487 -10.897 -3.726  1.00 46.23 ? 291  THR B CG2   1 
ATOM   2149 N N     . MET A 1 294 ? 21.078 -7.831  -5.843  1.00 33.90 ? 292  MET B N     1 
ATOM   2150 C CA    . MET A 1 294 ? 20.138 -7.297  -6.851  1.00 35.30 ? 292  MET B CA    1 
ATOM   2151 C C     . MET A 1 294 ? 20.763 -7.432  -8.245  1.00 36.31 ? 292  MET B C     1 
ATOM   2152 O O     . MET A 1 294 ? 20.042 -7.795  -9.171  1.00 32.61 ? 292  MET B O     1 
ATOM   2153 C CB    . MET A 1 294 ? 19.836 -5.831  -6.578  1.00 37.46 ? 292  MET B CB    1 
ATOM   2154 C CG    . MET A 1 294 ? 18.983 -5.220  -7.617  1.00 43.23 ? 292  MET B CG    1 
ATOM   2155 S SD    . MET A 1 294 ? 19.005 -3.476  -7.328  1.00 59.02 ? 292  MET B SD    1 
ATOM   2156 C CE    . MET A 1 294 ? 20.361 -3.053  -8.421  1.00 59.37 ? 292  MET B CE    1 
ATOM   2157 N N     . MET A 1 295 ? 22.064 -7.171  -8.366  1.00 36.36 ? 293  MET B N     1 
ATOM   2158 C CA    . MET A 1 295 ? 22.787 -7.150  -9.662  1.00 37.43 ? 293  MET B CA    1 
ATOM   2159 C C     . MET A 1 295 ? 23.050 -8.585  -10.155 1.00 35.26 ? 293  MET B C     1 
ATOM   2160 O O     . MET A 1 295 ? 23.067 -8.784  -11.380 1.00 34.23 ? 293  MET B O     1 
ATOM   2161 C CB    . MET A 1 295 ? 24.089 -6.350  -9.543  1.00 39.86 ? 293  MET B CB    1 
ATOM   2162 C CG    . MET A 1 295 ? 23.878 -4.833  -9.590  1.00 42.57 ? 293  MET B CG    1 
ATOM   2163 S SD    . MET A 1 295 ? 25.464 -3.885  -9.599  1.00 55.29 ? 293  MET B SD    1 
ATOM   2164 C CE    . MET A 1 295 ? 26.531 -4.900  -8.576  1.00 48.88 ? 293  MET B CE    1 
ATOM   2165 N N     . ASN A 1 296 ? 23.234 -9.567  -9.275  1.00 34.11 ? 294  ASN B N     1 
ATOM   2166 C CA    . ASN A 1 296 ? 23.338 -10.995 -9.697  1.00 37.88 ? 294  ASN B CA    1 
ATOM   2167 C C     . ASN A 1 296 ? 22.041 -11.450 -10.396 1.00 37.17 ? 294  ASN B C     1 
ATOM   2168 O O     . ASN A 1 296 ? 22.138 -12.214 -11.397 1.00 32.69 ? 294  ASN B O     1 
ATOM   2169 C CB    . ASN A 1 296 ? 23.580 -11.943 -8.524  1.00 41.05 ? 294  ASN B CB    1 
ATOM   2170 C CG    . ASN A 1 296 ? 24.993 -11.884 -7.981  1.00 47.49 ? 294  ASN B CG    1 
ATOM   2171 O OD1   . ASN A 1 296 ? 25.941 -11.584 -8.701  1.00 50.36 ? 294  ASN B OD1   1 
ATOM   2172 N ND2   . ASN A 1 296 ? 25.135 -12.191 -6.703  1.00 51.49 ? 294  ASN B ND2   1 
ATOM   2173 N N     . TYR A 1 297 ? 20.882 -11.065 -9.846  1.00 30.16 ? 295  TYR B N     1 
ATOM   2174 C CA    . TYR A 1 297 ? 19.547 -11.406 -10.399 1.00 32.17 ? 295  TYR B CA    1 
ATOM   2175 C C     . TYR A 1 297 ? 19.288 -10.576 -11.660 1.00 30.23 ? 295  TYR B C     1 
ATOM   2176 O O     . TYR A 1 297 ? 18.775 -11.164 -12.639 1.00 30.13 ? 295  TYR B O     1 
ATOM   2177 C CB    . TYR A 1 297 ? 18.428 -11.232 -9.359  1.00 32.23 ? 295  TYR B CB    1 
ATOM   2178 C CG    . TYR A 1 297 ? 18.332 -12.367 -8.369  1.00 31.89 ? 295  TYR B CG    1 
ATOM   2179 C CD1   . TYR A 1 297 ? 19.173 -12.426 -7.266  1.00 33.29 ? 295  TYR B CD1   1 
ATOM   2180 C CD2   . TYR A 1 297 ? 17.382 -13.372 -8.514  1.00 34.27 ? 295  TYR B CD2   1 
ATOM   2181 C CE1   . TYR A 1 297 ? 19.081 -13.458 -6.342  1.00 36.43 ? 295  TYR B CE1   1 
ATOM   2182 C CE2   . TYR A 1 297 ? 17.277 -14.416 -7.608  1.00 33.73 ? 295  TYR B CE2   1 
ATOM   2183 C CZ    . TYR A 1 297 ? 18.128 -14.457 -6.510  1.00 37.09 ? 295  TYR B CZ    1 
ATOM   2184 O OH    . TYR A 1 297 ? 18.068 -15.494 -5.620  1.00 34.85 ? 295  TYR B OH    1 
ATOM   2185 N N     . ALA A 1 298 ? 19.654 -9.290  -11.656 1.00 28.47 ? 296  ALA B N     1 
ATOM   2186 C CA    . ALA A 1 298 ? 19.393 -8.341  -12.764 1.00 30.53 ? 296  ALA B CA    1 
ATOM   2187 C C     . ALA A 1 298 ? 20.204 -8.768  -13.998 1.00 31.98 ? 296  ALA B C     1 
ATOM   2188 O O     . ALA A 1 298 ? 19.669 -8.679  -15.111 1.00 31.80 ? 296  ALA B O     1 
ATOM   2189 C CB    . ALA A 1 298 ? 19.717 -6.915  -12.352 1.00 30.51 ? 296  ALA B CB    1 
ATOM   2190 N N     . ARG A 1 299 ? 21.418 -9.272  -13.804 1.00 29.20 ? 297  ARG B N     1 
ATOM   2191 C CA    . ARG A 1 299 ? 22.283 -9.729  -14.918 1.00 32.71 ? 297  ARG B CA    1 
ATOM   2192 C C     . ARG A 1 299 ? 21.591 -10.876 -15.664 1.00 30.32 ? 297  ARG B C     1 
ATOM   2193 O O     . ARG A 1 299 ? 21.610 -10.868 -16.906 1.00 27.73 ? 297  ARG B O     1 
ATOM   2194 C CB    . ARG A 1 299 ? 23.635 -10.239 -14.409 1.00 35.71 ? 297  ARG B CB    1 
ATOM   2195 C CG    . ARG A 1 299 ? 24.688 -9.171  -14.190 1.00 40.78 ? 297  ARG B CG    1 
ATOM   2196 C CD    . ARG A 1 299 ? 25.968 -9.864  -13.742 1.00 48.55 ? 297  ARG B CD    1 
ATOM   2197 N NE    . ARG A 1 299 ? 26.717 -9.051  -12.792 1.00 58.47 ? 297  ARG B NE    1 
ATOM   2198 C CZ    . ARG A 1 299 ? 27.139 -9.441  -11.588 1.00 64.45 ? 297  ARG B CZ    1 
ATOM   2199 N NH1   . ARG A 1 299 ? 26.934 -10.674 -11.149 1.00 64.64 ? 297  ARG B NH1   1 
ATOM   2200 N NH2   . ARG A 1 299 ? 27.800 -8.583  -10.831 1.00 70.70 ? 297  ARG B NH2   1 
ATOM   2201 N N     . LEU A 1 300 ? 21.071 -11.875 -14.940 1.00 30.97 ? 298  LEU B N     1 
ATOM   2202 C CA    . LEU A 1 300 ? 20.269 -12.958 -15.562 1.00 28.27 ? 298  LEU B CA    1 
ATOM   2203 C C     . LEU A 1 300 ? 19.046 -12.306 -16.204 1.00 27.94 ? 298  LEU B C     1 
ATOM   2204 O O     . LEU A 1 300 ? 18.729 -12.634 -17.360 1.00 28.09 ? 298  LEU B O     1 
ATOM   2205 C CB    . LEU A 1 300 ? 19.875 -14.008 -14.522 1.00 30.06 ? 298  LEU B CB    1 
ATOM   2206 C CG    . LEU A 1 300 ? 18.954 -15.130 -15.020 1.00 32.98 ? 298  LEU B CG    1 
ATOM   2207 C CD1   . LEU A 1 300 ? 19.549 -15.865 -16.217 1.00 34.48 ? 298  LEU B CD1   1 
ATOM   2208 C CD2   . LEU A 1 300 ? 18.690 -16.138 -13.921 1.00 32.45 ? 298  LEU B CD2   1 
ATOM   2209 N N     . GLY A 1 301 ? 18.399 -11.383 -15.495 1.00 28.37 ? 299  GLY B N     1 
ATOM   2210 C CA    . GLY A 1 301 ? 17.166 -10.736 -15.990 1.00 25.69 ? 299  GLY B CA    1 
ATOM   2211 C C     . GLY A 1 301 ? 17.407 -10.073 -17.340 1.00 25.11 ? 299  GLY B C     1 
ATOM   2212 O O     . GLY A 1 301 ? 16.513 -10.158 -18.198 1.00 24.18 ? 299  GLY B O     1 
ATOM   2213 N N     . VAL A 1 302 ? 18.538 -9.380  -17.505 1.00 23.78 ? 300  VAL B N     1 
ATOM   2214 C CA    . VAL A 1 302 ? 18.852 -8.635  -18.757 1.00 26.16 ? 300  VAL B CA    1 
ATOM   2215 C C     . VAL A 1 302 ? 19.150 -9.650  -19.867 1.00 24.64 ? 300  VAL B C     1 
ATOM   2216 O O     . VAL A 1 302 ? 18.705 -9.413  -20.981 1.00 25.38 ? 300  VAL B O     1 
ATOM   2217 C CB    . VAL A 1 302 ? 19.982 -7.613  -18.560 1.00 28.64 ? 300  VAL B CB    1 
ATOM   2218 C CG1   . VAL A 1 302 ? 20.363 -6.944  -19.872 1.00 33.31 ? 300  VAL B CG1   1 
ATOM   2219 C CG2   . VAL A 1 302 ? 19.562 -6.565  -17.546 1.00 29.94 ? 300  VAL B CG2   1 
ATOM   2220 N N     . GLY A 1 303 ? 19.883 -10.724 -19.567 1.00 24.78 ? 301  GLY B N     1 
ATOM   2221 C CA    . GLY A 1 303 ? 20.034 -11.869 -20.478 1.00 25.04 ? 301  GLY B CA    1 
ATOM   2222 C C     . GLY A 1 303 ? 18.671 -12.324 -20.984 1.00 27.09 ? 301  GLY B C     1 
ATOM   2223 O O     . GLY A 1 303 ? 18.468 -12.439 -22.210 1.00 25.79 ? 301  GLY B O     1 
ATOM   2224 N N     . ILE A 1 304 ? 17.734 -12.523 -20.062 1.00 25.71 ? 302  ILE B N     1 
ATOM   2225 C CA    . ILE A 1 304 ? 16.364 -12.996 -20.387 1.00 25.69 ? 302  ILE B CA    1 
ATOM   2226 C C     . ILE A 1 304 ? 15.678 -11.948 -21.256 1.00 23.96 ? 302  ILE B C     1 
ATOM   2227 O O     . ILE A 1 304 ? 14.972 -12.355 -22.167 1.00 21.81 ? 302  ILE B O     1 
ATOM   2228 C CB    . ILE A 1 304 ? 15.585 -13.366 -19.114 1.00 26.52 ? 302  ILE B CB    1 
ATOM   2229 C CG1   . ILE A 1 304 ? 16.165 -14.650 -18.515 1.00 29.20 ? 302  ILE B CG1   1 
ATOM   2230 C CG2   . ILE A 1 304 ? 14.096 -13.514 -19.394 1.00 27.23 ? 302  ILE B CG2   1 
ATOM   2231 C CD1   . ILE A 1 304 ? 15.673 -14.933 -17.098 1.00 31.75 ? 302  ILE B CD1   1 
ATOM   2232 N N     . ALA A 1 305 ? 15.896 -10.655 -21.032 1.00 20.47 ? 303  ALA B N     1 
ATOM   2233 C CA    . ALA A 1 305 ? 15.282 -9.637  -21.909 1.00 21.30 ? 303  ALA B CA    1 
ATOM   2234 C C     . ALA A 1 305 ? 15.767 -9.787  -23.363 1.00 21.21 ? 303  ALA B C     1 
ATOM   2235 O O     . ALA A 1 305 ? 14.948 -9.664  -24.277 1.00 19.97 ? 303  ALA B O     1 
ATOM   2236 C CB    . ALA A 1 305 ? 15.581 -8.267  -21.376 1.00 22.80 ? 303  ALA B CB    1 
ATOM   2237 N N     . GLY A 1 306 ? 17.056 -10.031 -23.586 1.00 23.67 ? 304  GLY B N     1 
ATOM   2238 C CA    . GLY A 1 306 ? 17.582 -10.218 -24.953 1.00 24.27 ? 304  GLY B CA    1 
ATOM   2239 C C     . GLY A 1 306 ? 16.986 -11.471 -25.574 1.00 22.74 ? 304  GLY B C     1 
ATOM   2240 O O     . GLY A 1 306 ? 16.458 -11.383 -26.698 1.00 22.67 ? 304  GLY B O     1 
ATOM   2241 N N     . LEU A 1 307 ? 17.028 -12.585 -24.855 1.00 22.74 ? 305  LEU B N     1 
ATOM   2242 C CA    . LEU A 1 307 ? 16.416 -13.845 -25.351 1.00 23.99 ? 305  LEU B CA    1 
ATOM   2243 C C     . LEU A 1 307 ? 14.933 -13.634 -25.697 1.00 25.53 ? 305  LEU B C     1 
ATOM   2244 O O     . LEU A 1 307 ? 14.493 -14.155 -26.713 1.00 24.75 ? 305  LEU B O     1 
ATOM   2245 C CB    . LEU A 1 307 ? 16.595 -14.920 -24.281 1.00 25.27 ? 305  LEU B CB    1 
ATOM   2246 C CG    . LEU A 1 307 ? 15.646 -16.113 -24.362 1.00 29.17 ? 305  LEU B CG    1 
ATOM   2247 C CD1   . LEU A 1 307 ? 16.043 -17.042 -25.498 1.00 32.61 ? 305  LEU B CD1   1 
ATOM   2248 C CD2   . LEU A 1 307 ? 15.618 -16.869 -23.043 1.00 27.48 ? 305  LEU B CD2   1 
ATOM   2249 N N     . ALA A 1 308 ? 14.204 -12.895 -24.867 1.00 24.89 ? 306  ALA B N     1 
ATOM   2250 C CA    . ALA A 1 308 ? 12.764 -12.646 -25.106 1.00 24.72 ? 306  ALA B CA    1 
ATOM   2251 C C     . ALA A 1 308 ? 12.539 -12.004 -26.484 1.00 24.21 ? 306  ALA B C     1 
ATOM   2252 O O     . ALA A 1 308 ? 11.619 -12.416 -27.176 1.00 22.43 ? 306  ALA B O     1 
ATOM   2253 C CB    . ALA A 1 308 ? 12.218 -11.778 -24.006 1.00 24.11 ? 306  ALA B CB    1 
ATOM   2254 N N     . THR A 1 309 ? 13.333 -10.984 -26.819 1.00 23.54 ? 307  THR B N     1 
ATOM   2255 C CA    . THR A 1 309 ? 13.221 -10.326 -28.153 1.00 23.22 ? 307  THR B CA    1 
ATOM   2256 C C     . THR A 1 309 ? 13.457 -11.362 -29.257 1.00 21.38 ? 307  THR B C     1 
ATOM   2257 O O     . THR A 1 309 ? 12.761 -11.314 -30.265 1.00 21.08 ? 307  THR B O     1 
ATOM   2258 C CB    . THR A 1 309 ? 14.162 -9.115  -28.270 1.00 24.15 ? 307  THR B CB    1 
ATOM   2259 O OG1   . THR A 1 309 ? 15.524 -9.537  -28.236 1.00 24.98 ? 307  THR B OG1   1 
ATOM   2260 C CG2   . THR A 1 309 ? 13.912 -8.092  -27.183 1.00 23.32 ? 307  THR B CG2   1 
ATOM   2261 N N     . GLY A 1 310 ? 14.415 -12.255 -29.039 1.00 20.79 ? 308  GLY B N     1 
ATOM   2262 C CA    . GLY A 1 310 ? 14.729 -13.301 -30.027 1.00 23.10 ? 308  GLY B CA    1 
ATOM   2263 C C     . GLY A 1 310 ? 13.603 -14.307 -30.206 1.00 24.37 ? 308  GLY B C     1 
ATOM   2264 O O     . GLY A 1 310 ? 13.327 -14.700 -31.332 1.00 20.89 ? 308  GLY B O     1 
ATOM   2265 N N     . GLU A 1 311 ? 12.983 -14.695 -29.098 1.00 25.65 ? 309  GLU B N     1 
ATOM   2266 C CA    . GLU A 1 311 ? 11.865 -15.661 -29.164 1.00 25.51 ? 309  GLU B CA    1 
ATOM   2267 C C     . GLU A 1 311 ? 10.707 -14.995 -29.908 1.00 23.16 ? 309  GLU B C     1 
ATOM   2268 O O     . GLU A 1 311 ? 10.104 -15.649 -30.738 1.00 25.40 ? 309  GLU B O     1 
ATOM   2269 C CB    . GLU A 1 311 ? 11.502 -16.137 -27.756 1.00 25.59 ? 309  GLU B CB    1 
ATOM   2270 C CG    . GLU A 1 311 ? 10.116 -16.732 -27.659 1.00 23.78 ? 309  GLU B CG    1 
ATOM   2271 C CD    . GLU A 1 311 ? 10.004 -18.117 -28.268 1.00 25.24 ? 309  GLU B CD    1 
ATOM   2272 O OE1   . GLU A 1 311 ? 11.028 -18.810 -28.352 1.00 24.11 ? 309  GLU B OE1   1 
ATOM   2273 O OE2   . GLU A 1 311 ? 8.894  -18.488 -28.655 1.00 25.66 ? 309  GLU B OE2   1 
ATOM   2274 N N     . ARG A 1 312 ? 10.448 -13.721 -29.623 1.00 22.34 ? 310  ARG B N     1 
ATOM   2275 C CA    . ARG A 1 312 ? 9.316  -13.022 -30.273 1.00 22.08 ? 310  ARG B CA    1 
ATOM   2276 C C     . ARG A 1 312 ? 9.605  -12.936 -31.773 1.00 22.63 ? 310  ARG B C     1 
ATOM   2277 O O     . ARG A 1 312 ? 8.702  -13.191 -32.562 1.00 22.87 ? 310  ARG B O     1 
ATOM   2278 C CB    . ARG A 1 312 ? 9.088  -11.642 -29.648 1.00 23.24 ? 310  ARG B CB    1 
ATOM   2279 C CG    . ARG A 1 312 ? 7.896  -10.887 -30.214 1.00 24.08 ? 310  ARG B CG    1 
ATOM   2280 C CD    . ARG A 1 312 ? 6.610  -11.221 -29.485 1.00 30.58 ? 310  ARG B CD    1 
ATOM   2281 N NE    . ARG A 1 312 ? 5.425  -11.006 -30.299 1.00 33.75 ? 310  ARG B NE    1 
ATOM   2282 C CZ    . ARG A 1 312 ? 4.556  -10.020 -30.130 1.00 38.78 ? 310  ARG B CZ    1 
ATOM   2283 N NH1   . ARG A 1 312 ? 3.511  -9.925  -30.931 1.00 48.13 ? 310  ARG B NH1   1 
ATOM   2284 N NH2   . ARG A 1 312 ? 4.726  -9.136  -29.163 1.00 37.24 ? 310  ARG B NH2   1 
ATOM   2285 N N     . SER A 1 313 ? 10.847 -12.606 -32.122 1.00 21.70 ? 311  SER B N     1 
ATOM   2286 C CA    . SER A 1 313 ? 11.247 -12.497 -33.548 1.00 21.18 ? 311  SER B CA    1 
ATOM   2287 C C     . SER A 1 313 ? 11.045 -13.834 -34.272 1.00 21.36 ? 311  SER B C     1 
ATOM   2288 O O     . SER A 1 313 ? 10.591 -13.820 -35.404 1.00 22.89 ? 311  SER B O     1 
ATOM   2289 C CB    . SER A 1 313 ? 12.679 -12.011 -33.684 1.00 22.67 ? 311  SER B CB    1 
ATOM   2290 O OG    . SER A 1 313 ? 13.010 -11.756 -35.036 1.00 23.02 ? 311  SER B OG    1 
ATOM   2291 N N     . TYR A 1 314 ? 11.374 -14.936 -33.608 1.00 21.39 ? 312  TYR B N     1 
ATOM   2292 C CA    . TYR A 1 314 ? 11.219 -16.277 -34.227 1.00 23.16 ? 312  TYR B CA    1 
ATOM   2293 C C     . TYR A 1 314 ? 9.736  -16.582 -34.491 1.00 24.97 ? 312  TYR B C     1 
ATOM   2294 O O     . TYR A 1 314 ? 9.403  -17.072 -35.559 1.00 26.13 ? 312  TYR B O     1 
ATOM   2295 C CB    . TYR A 1 314 ? 11.865 -17.367 -33.376 1.00 22.22 ? 312  TYR B CB    1 
ATOM   2296 C CG    . TYR A 1 314 ? 11.742 -18.734 -33.995 1.00 23.67 ? 312  TYR B CG    1 
ATOM   2297 C CD1   . TYR A 1 314 ? 12.557 -19.113 -35.047 1.00 25.46 ? 312  TYR B CD1   1 
ATOM   2298 C CD2   . TYR A 1 314 ? 10.778 -19.628 -33.566 1.00 23.47 ? 312  TYR B CD2   1 
ATOM   2299 C CE1   . TYR A 1 314 ? 12.437 -20.359 -35.637 1.00 24.59 ? 312  TYR B CE1   1 
ATOM   2300 C CE2   . TYR A 1 314 ? 10.646 -20.879 -34.143 1.00 22.76 ? 312  TYR B CE2   1 
ATOM   2301 C CZ    . TYR A 1 314 ? 11.477 -21.244 -35.185 1.00 25.44 ? 312  TYR B CZ    1 
ATOM   2302 O OH    . TYR A 1 314 ? 11.353 -22.473 -35.758 1.00 26.61 ? 312  TYR B OH    1 
ATOM   2303 N N     . GLN A 1 315 ? 8.879  -16.269 -33.523 1.00 27.05 ? 313  GLN B N     1 
ATOM   2304 C CA    . GLN A 1 315 ? 7.430  -16.535 -33.699 1.00 26.49 ? 313  GLN B CA    1 
ATOM   2305 C C     . GLN A 1 315 ? 6.943  -15.823 -34.969 1.00 27.83 ? 313  GLN B C     1 
ATOM   2306 O O     . GLN A 1 315 ? 6.257  -16.456 -35.760 1.00 23.99 ? 313  GLN B O     1 
ATOM   2307 C CB    . GLN A 1 315 ? 6.653  -16.165 -32.432 1.00 25.16 ? 313  GLN B CB    1 
ATOM   2308 C CG    . GLN A 1 315 ? 6.887  -17.115 -31.269 1.00 24.93 ? 313  GLN B CG    1 
ATOM   2309 C CD    . GLN A 1 315 ? 5.988  -16.820 -30.093 1.00 26.44 ? 313  GLN B CD    1 
ATOM   2310 O OE1   . GLN A 1 315 ? 4.853  -16.381 -30.249 1.00 27.32 ? 313  GLN B OE1   1 
ATOM   2311 N NE2   . GLN A 1 315 ? 6.496  -17.059 -28.898 1.00 25.17 ? 313  GLN B NE2   1 
ATOM   2312 N N     . SER A 1 316 ? 7.338  -14.561 -35.154 1.00 26.71 ? 314  SER B N     1 
ATOM   2313 C CA    . SER A 1 316 ? 6.936  -13.805 -36.366 1.00 26.05 ? 314  SER B CA    1 
ATOM   2314 C C     . SER A 1 316 ? 7.595  -14.398 -37.628 1.00 24.50 ? 314  SER B C     1 
ATOM   2315 O O     . SER A 1 316 ? 6.921  -14.523 -38.643 1.00 22.87 ? 314  SER B O     1 
ATOM   2316 C CB    . SER A 1 316 ? 7.217  -12.317 -36.191 1.00 26.94 ? 314  SER B CB    1 
ATOM   2317 O OG    . SER A 1 316 ? 6.391  -11.752 -35.190 1.00 27.10 ? 314  SER B OG    1 
ATOM   2318 N N     . ALA A 1 317 ? 8.867  -14.781 -37.531 1.00 23.56 ? 315  ALA B N     1 
ATOM   2319 C CA    . ALA A 1 317 ? 9.612  -15.272 -38.710 1.00 23.94 ? 315  ALA B CA    1 
ATOM   2320 C C     . ALA A 1 317 ? 9.098  -16.637 -39.199 1.00 24.40 ? 315  ALA B C     1 
ATOM   2321 O O     . ALA A 1 317 ? 9.006  -16.814 -40.406 1.00 23.09 ? 315  ALA B O     1 
ATOM   2322 C CB    . ALA A 1 317 ? 11.073 -15.335 -38.375 1.00 24.98 ? 315  ALA B CB    1 
ATOM   2323 N N     . ILE A 1 318 ? 8.853  -17.572 -38.282 1.00 23.41 ? 316  ILE B N     1 
ATOM   2324 C CA    . ILE A 1 318 ? 8.404  -18.929 -38.717 1.00 24.41 ? 316  ILE B CA    1 
ATOM   2325 C C     . ILE A 1 318 ? 7.007  -18.837 -39.354 1.00 25.57 ? 316  ILE B C     1 
ATOM   2326 O O     . ILE A 1 318 ? 6.774  -19.513 -40.340 1.00 25.99 ? 316  ILE B O     1 
ATOM   2327 C CB    . ILE A 1 318 ? 8.453  -19.960 -37.574 1.00 24.16 ? 316  ILE B CB    1 
ATOM   2328 C CG1   . ILE A 1 318 ? 8.178  -21.374 -38.089 1.00 24.02 ? 316  ILE B CG1   1 
ATOM   2329 C CG2   . ILE A 1 318 ? 7.524  -19.580 -36.432 1.00 25.35 ? 316  ILE B CG2   1 
ATOM   2330 C CD1   . ILE A 1 318 ? 9.017  -21.755 -39.279 1.00 24.72 ? 316  ILE B CD1   1 
ATOM   2331 N N     . GLU A 1 319 ? 6.133  -17.999 -38.806 1.00 26.23 ? 317  GLU B N     1 
ATOM   2332 C CA    . GLU A 1 319 ? 4.796  -17.810 -39.423 1.00 28.64 ? 317  GLU B CA    1 
ATOM   2333 C C     . GLU A 1 319 ? 4.979  -17.232 -40.828 1.00 28.89 ? 317  GLU B C     1 
ATOM   2334 O O     . GLU A 1 319 ? 4.325  -17.703 -41.753 1.00 23.99 ? 317  GLU B O     1 
ATOM   2335 C CB    . GLU A 1 319 ? 3.939  -16.911 -38.535 1.00 31.60 ? 317  GLU B CB    1 
ATOM   2336 C CG    . GLU A 1 319 ? 2.571  -16.594 -39.093 1.00 36.43 ? 317  GLU B CG    1 
ATOM   2337 C CD    . GLU A 1 319 ? 1.668  -15.956 -38.054 1.00 40.39 ? 317  GLU B CD    1 
ATOM   2338 O OE1   . GLU A 1 319 ? 1.359  -14.764 -38.192 1.00 41.65 ? 317  GLU B OE1   1 
ATOM   2339 O OE2   . GLU A 1 319 ? 1.297  -16.653 -37.100 1.00 48.15 ? 317  GLU B OE2   1 
ATOM   2340 N N     . TYR A 1 320 ? 5.870  -16.249 -40.951 1.00 26.60 ? 318  TYR B N     1 
ATOM   2341 C CA    . TYR A 1 320 ? 6.062  -15.584 -42.263 1.00 28.48 ? 318  TYR B CA    1 
ATOM   2342 C C     . TYR A 1 320 ? 6.674  -16.583 -43.251 1.00 26.08 ? 318  TYR B C     1 
ATOM   2343 O O     . TYR A 1 320 ? 6.304  -16.597 -44.428 1.00 25.65 ? 318  TYR B O     1 
ATOM   2344 C CB    . TYR A 1 320 ? 6.941  -14.342 -42.120 1.00 27.46 ? 318  TYR B CB    1 
ATOM   2345 C CG    . TYR A 1 320 ? 6.952  -13.461 -43.338 1.00 27.40 ? 318  TYR B CG    1 
ATOM   2346 C CD1   . TYR A 1 320 ? 5.880  -12.628 -43.613 1.00 27.38 ? 318  TYR B CD1   1 
ATOM   2347 C CD2   . TYR A 1 320 ? 8.010  -13.486 -44.238 1.00 26.76 ? 318  TYR B CD2   1 
ATOM   2348 C CE1   . TYR A 1 320 ? 5.878  -11.804 -44.723 1.00 27.38 ? 318  TYR B CE1   1 
ATOM   2349 C CE2   . TYR A 1 320 ? 8.023  -12.669 -45.355 1.00 25.80 ? 318  TYR B CE2   1 
ATOM   2350 C CZ    . TYR A 1 320 ? 6.955  -11.820 -45.593 1.00 27.53 ? 318  TYR B CZ    1 
ATOM   2351 O OH    . TYR A 1 320 ? 6.922  -11.008 -46.687 1.00 27.50 ? 318  TYR B OH    1 
ATOM   2352 N N     . ALA A 1 321 ? 7.656  -17.351 -42.790 1.00 26.81 ? 319  ALA B N     1 
ATOM   2353 C CA    . ALA A 1 321 ? 8.407  -18.255 -43.691 1.00 27.26 ? 319  ALA B CA    1 
ATOM   2354 C C     . ALA A 1 321 ? 7.527  -19.403 -44.193 1.00 25.50 ? 319  ALA B C     1 
ATOM   2355 O O     . ALA A 1 321 ? 7.846  -19.972 -45.221 1.00 23.78 ? 319  ALA B O     1 
ATOM   2356 C CB    . ALA A 1 321 ? 9.622  -18.760 -42.971 1.00 26.34 ? 319  ALA B CB    1 
ATOM   2357 N N     . ARG A 1 322 ? 6.468  -19.713 -43.456 1.00 25.48 ? 320  ARG B N     1 
ATOM   2358 C CA    . ARG A 1 322 ? 5.524  -20.773 -43.885 1.00 26.17 ? 320  ARG B CA    1 
ATOM   2359 C C     . ARG A 1 322 ? 4.464  -20.178 -44.819 1.00 28.36 ? 320  ARG B C     1 
ATOM   2360 O O     . ARG A 1 322 ? 3.908  -20.930 -45.609 1.00 28.48 ? 320  ARG B O     1 
ATOM   2361 C CB    . ARG A 1 322 ? 4.855  -21.401 -42.658 1.00 25.71 ? 320  ARG B CB    1 
ATOM   2362 C CG    . ARG A 1 322 ? 5.765  -22.185 -41.727 1.00 26.25 ? 320  ARG B CG    1 
ATOM   2363 C CD    . ARG A 1 322 ? 4.988  -22.583 -40.484 1.00 26.73 ? 320  ARG B CD    1 
ATOM   2364 N NE    . ARG A 1 322 ? 5.605  -23.666 -39.735 1.00 28.97 ? 320  ARG B NE    1 
ATOM   2365 C CZ    . ARG A 1 322 ? 5.600  -23.763 -38.414 1.00 28.43 ? 320  ARG B CZ    1 
ATOM   2366 N NH1   . ARG A 1 322 ? 6.193  -24.784 -37.824 1.00 31.55 ? 320  ARG B NH1   1 
ATOM   2367 N NH2   . ARG A 1 322 ? 5.001  -22.841 -37.686 1.00 31.56 ? 320  ARG B NH2   1 
ATOM   2368 N N     . GLU A 1 323 ? 4.215  -18.873 -44.734 1.00 26.87 ? 321  GLU B N     1 
ATOM   2369 C CA    . GLU A 1 323 ? 3.125  -18.245 -45.521 1.00 30.80 ? 321  GLU B CA    1 
ATOM   2370 C C     . GLU A 1 323 ? 3.657  -17.553 -46.784 1.00 30.77 ? 321  GLU B C     1 
ATOM   2371 O O     . GLU A 1 323 ? 3.015  -17.670 -47.831 1.00 26.24 ? 321  GLU B O     1 
ATOM   2372 C CB    . GLU A 1 323 ? 2.395  -17.213 -44.668 1.00 38.08 ? 321  GLU B CB    1 
ATOM   2373 C CG    . GLU A 1 323 ? 0.965  -16.982 -45.098 1.00 50.34 ? 321  GLU B CG    1 
ATOM   2374 C CD    . GLU A 1 323 ? 0.035  -16.574 -43.971 1.00 60.03 ? 321  GLU B CD    1 
ATOM   2375 O OE1   . GLU A 1 323 ? 0.457  -16.649 -42.799 1.00 63.76 ? 321  GLU B OE1   1 
ATOM   2376 O OE2   . GLU A 1 323 ? -1.107 -16.180 -44.270 1.00 68.61 ? 321  GLU B OE2   1 
ATOM   2377 N N     . ARG A 1 324 ? 4.755  -16.813 -46.655 1.00 25.19 ? 322  ARG B N     1 
ATOM   2378 C CA    . ARG A 1 324 ? 5.311  -16.067 -47.811 1.00 25.44 ? 322  ARG B CA    1 
ATOM   2379 C C     . ARG A 1 324 ? 5.773  -17.087 -48.849 1.00 23.53 ? 322  ARG B C     1 
ATOM   2380 O O     . ARG A 1 324 ? 6.574  -17.949 -48.499 1.00 24.43 ? 322  ARG B O     1 
ATOM   2381 C CB    . ARG A 1 324 ? 6.468  -15.161 -47.373 1.00 24.23 ? 322  ARG B CB    1 
ATOM   2382 C CG    . ARG A 1 324 ? 7.202  -14.486 -48.525 1.00 23.87 ? 322  ARG B CG    1 
ATOM   2383 C CD    . ARG A 1 324 ? 6.349  -13.445 -49.203 1.00 25.33 ? 322  ARG B CD    1 
ATOM   2384 N NE    . ARG A 1 324 ? 7.116  -12.681 -50.173 1.00 25.01 ? 322  ARG B NE    1 
ATOM   2385 C CZ    . ARG A 1 324 ? 6.662  -11.603 -50.810 1.00 24.24 ? 322  ARG B CZ    1 
ATOM   2386 N NH1   . ARG A 1 324 ? 7.455  -10.939 -51.636 1.00 23.70 ? 322  ARG B NH1   1 
ATOM   2387 N NH2   . ARG A 1 324 ? 5.432  -11.172 -50.584 1.00 25.07 ? 322  ARG B NH2   1 
ATOM   2388 N N     . ILE A 1 325 ? 5.293  -16.986 -50.082 1.00 25.35 ? 323  ILE B N     1 
ATOM   2389 C CA    . ILE A 1 325 ? 5.815  -17.830 -51.199 1.00 24.10 ? 323  ILE B CA    1 
ATOM   2390 C C     . ILE A 1 325 ? 6.707  -16.968 -52.109 1.00 24.29 ? 323  ILE B C     1 
ATOM   2391 O O     . ILE A 1 325 ? 6.376  -15.788 -52.388 1.00 23.97 ? 323  ILE B O     1 
ATOM   2392 C CB    . ILE A 1 325 ? 4.690  -18.562 -51.958 1.00 26.24 ? 323  ILE B CB    1 
ATOM   2393 C CG1   . ILE A 1 325 ? 3.798  -17.605 -52.761 1.00 27.52 ? 323  ILE B CG1   1 
ATOM   2394 C CG2   . ILE A 1 325 ? 3.896  -19.432 -50.984 1.00 26.85 ? 323  ILE B CG2   1 
ATOM   2395 C CD1   . ILE A 1 325 ? 2.684  -18.292 -53.572 1.00 29.20 ? 323  ILE B CD1   1 
ATOM   2396 N N     . GLN A 1 326 ? 7.840  -17.536 -52.529 1.00 23.67 ? 324  GLN B N     1 
ATOM   2397 C CA    . GLN A 1 326 ? 8.813  -16.845 -53.415 1.00 23.44 ? 324  GLN B CA    1 
ATOM   2398 C C     . GLN A 1 326 ? 9.762  -17.890 -53.969 1.00 23.53 ? 324  GLN B C     1 
ATOM   2399 O O     . GLN A 1 326 ? 10.314 -18.643 -53.172 1.00 24.44 ? 324  GLN B O     1 
ATOM   2400 C CB    . GLN A 1 326 ? 9.569  -15.770 -52.643 1.00 23.72 ? 324  GLN B CB    1 
ATOM   2401 C CG    . GLN A 1 326 ? 10.098 -14.676 -53.549 1.00 23.39 ? 324  GLN B CG    1 
ATOM   2402 C CD    . GLN A 1 326 ? 9.035  -13.739 -54.053 1.00 22.31 ? 324  GLN B CD    1 
ATOM   2403 O OE1   . GLN A 1 326 ? 7.837  -13.848 -53.767 1.00 24.56 ? 324  GLN B OE1   1 
ATOM   2404 N NE2   . GLN A 1 326 ? 9.485  -12.792 -54.826 1.00 21.07 ? 324  GLN B NE2   1 
ATOM   2405 N N     . SER A 1 327 ? 9.905  -17.960 -55.290 1.00 24.45 ? 325  SER B N     1 
ATOM   2406 C CA    . SER A 1 327 ? 10.863 -18.850 -55.987 1.00 23.53 ? 325  SER B CA    1 
ATOM   2407 C C     . SER A 1 327 ? 10.469 -20.313 -55.728 1.00 24.82 ? 325  SER B C     1 
ATOM   2408 O O     . SER A 1 327 ? 9.366  -20.543 -55.222 1.00 26.45 ? 325  SER B O     1 
ATOM   2409 C CB    . SER A 1 327 ? 12.289 -18.537 -55.554 1.00 25.02 ? 325  SER B CB    1 
ATOM   2410 O OG    . SER A 1 327 ? 12.536 -17.131 -55.557 1.00 24.90 ? 325  SER B OG    1 
ATOM   2411 N N     . ARG A 1 328 ? 11.312 -21.273 -56.102 1.00 24.64 ? 326  ARG B N     1 
ATOM   2412 C CA    . ARG A 1 328 ? 11.029 -22.728 -55.941 1.00 24.52 ? 326  ARG B CA    1 
ATOM   2413 C C     . ARG A 1 328 ? 12.173 -23.367 -55.175 1.00 26.06 ? 326  ARG B C     1 
ATOM   2414 O O     . ARG A 1 328 ? 13.320 -22.912 -55.314 1.00 23.91 ? 326  ARG B O     1 
ATOM   2415 C CB    . ARG A 1 328 ? 10.902 -23.417 -57.312 1.00 26.14 ? 326  ARG B CB    1 
ATOM   2416 C CG    . ARG A 1 328 ? 9.762  -22.880 -58.174 1.00 25.90 ? 326  ARG B CG    1 
ATOM   2417 C CD    . ARG A 1 328 ? 8.429  -23.058 -57.465 1.00 27.87 ? 326  ARG B CD    1 
ATOM   2418 N NE    . ARG A 1 328 ? 7.332  -22.927 -58.404 1.00 26.48 ? 326  ARG B NE    1 
ATOM   2419 C CZ    . ARG A 1 328 ? 6.059  -23.217 -58.156 1.00 27.63 ? 326  ARG B CZ    1 
ATOM   2420 N NH1   . ARG A 1 328 ? 5.669  -23.649 -56.964 1.00 26.23 ? 326  ARG B NH1   1 
ATOM   2421 N NH2   . ARG A 1 328 ? 5.172  -23.086 -59.132 1.00 27.73 ? 326  ARG B NH2   1 
ATOM   2422 N N     . ALA A 1 329 ? 11.871 -24.405 -54.403 1.00 28.69 ? 327  ALA B N     1 
ATOM   2423 C CA    . ALA A 1 329 ? 12.891 -25.235 -53.741 1.00 26.35 ? 327  ALA B CA    1 
ATOM   2424 C C     . ALA A 1 329 ? 13.967 -25.570 -54.770 1.00 28.98 ? 327  ALA B C     1 
ATOM   2425 O O     . ALA A 1 329 ? 13.667 -25.841 -55.929 1.00 28.82 ? 327  ALA B O     1 
ATOM   2426 C CB    . ALA A 1 329 ? 12.265 -26.478 -53.184 1.00 27.53 ? 327  ALA B CB    1 
ATOM   2427 N N     . PRO A 1 330 ? 15.247 -25.587 -54.358 1.00 28.34 ? 328  PRO B N     1 
ATOM   2428 C CA    . PRO A 1 330 ? 16.346 -26.015 -55.220 1.00 30.18 ? 328  PRO B CA    1 
ATOM   2429 C C     . PRO A 1 330 ? 16.188 -27.410 -55.840 1.00 30.08 ? 328  PRO B C     1 
ATOM   2430 O O     . PRO A 1 330 ? 16.612 -27.574 -56.960 1.00 29.94 ? 328  PRO B O     1 
ATOM   2431 C CB    . PRO A 1 330 ? 17.552 -26.077 -54.273 1.00 31.95 ? 328  PRO B CB    1 
ATOM   2432 C CG    . PRO A 1 330 ? 17.200 -25.155 -53.142 1.00 30.30 ? 328  PRO B CG    1 
ATOM   2433 C CD    . PRO A 1 330 ? 15.697 -25.183 -53.022 1.00 29.78 ? 328  PRO B CD    1 
ATOM   2434 N N     . THR A 1 331 ? 15.611 -28.366 -55.113 1.00 29.68 ? 329  THR B N     1 
ATOM   2435 C CA    . THR A 1 331 ? 15.433 -29.762 -55.586 1.00 33.77 ? 329  THR B CA    1 
ATOM   2436 C C     . THR A 1 331 ? 14.186 -29.890 -56.472 1.00 36.84 ? 329  THR B C     1 
ATOM   2437 O O     . THR A 1 331 ? 13.920 -31.006 -56.906 1.00 39.91 ? 329  THR B O     1 
ATOM   2438 C CB    . THR A 1 331 ? 15.372 -30.768 -54.427 1.00 33.41 ? 329  THR B CB    1 
ATOM   2439 O OG1   . THR A 1 331 ? 14.294 -30.418 -53.544 1.00 33.23 ? 329  THR B OG1   1 
ATOM   2440 C CG2   . THR A 1 331 ? 16.688 -30.849 -53.684 1.00 29.48 ? 329  THR B CG2   1 
ATOM   2441 N N     . GLY A 1 332 ? 13.455 -28.809 -56.731 1.00 36.21 ? 330  GLY B N     1 
ATOM   2442 C CA    . GLY A 1 332 ? 12.317 -28.834 -57.664 1.00 37.08 ? 330  GLY B CA    1 
ATOM   2443 C C     . GLY A 1 332 ? 11.045 -28.287 -57.027 1.00 35.14 ? 330  GLY B C     1 
ATOM   2444 O O     . GLY A 1 332 ? 10.854 -28.382 -55.822 1.00 35.62 ? 330  GLY B O     1 
ATOM   2445 N N     . PRO A 1 333 ? 10.138 -27.714 -57.837 1.00 35.42 ? 331  PRO B N     1 
ATOM   2446 C CA    . PRO A 1 333 ? 8.922  -27.094 -57.318 1.00 36.07 ? 331  PRO B CA    1 
ATOM   2447 C C     . PRO A 1 333 ? 8.171  -28.001 -56.337 1.00 37.24 ? 331  PRO B C     1 
ATOM   2448 O O     . PRO A 1 333 ? 7.968  -29.148 -56.666 1.00 37.95 ? 331  PRO B O     1 
ATOM   2449 C CB    . PRO A 1 333 ? 8.104  -26.856 -58.595 1.00 36.13 ? 331  PRO B CB    1 
ATOM   2450 C CG    . PRO A 1 333 ? 9.137  -26.661 -59.659 1.00 37.72 ? 331  PRO B CG    1 
ATOM   2451 C CD    . PRO A 1 333 ? 10.238 -27.637 -59.308 1.00 37.41 ? 331  PRO B CD    1 
ATOM   2452 N N     . VAL A 1 334 ? 7.763  -27.465 -55.183 1.00 34.64 ? 332  VAL B N     1 
ATOM   2453 C CA    . VAL A 1 334 ? 7.033  -28.206 -54.109 1.00 40.47 ? 332  VAL B CA    1 
ATOM   2454 C C     . VAL A 1 334 ? 5.525  -27.897 -54.193 1.00 42.56 ? 332  VAL B C     1 
ATOM   2455 O O     . VAL A 1 334 ? 4.732  -28.843 -54.188 1.00 43.46 ? 332  VAL B O     1 
ATOM   2456 C CB    . VAL A 1 334 ? 7.605  -27.860 -52.721 1.00 42.20 ? 332  VAL B CB    1 
ATOM   2457 C CG1   . VAL A 1 334 ? 6.773  -28.455 -51.597 1.00 44.62 ? 332  VAL B CG1   1 
ATOM   2458 C CG2   . VAL A 1 334 ? 9.053  -28.294 -52.593 1.00 42.42 ? 332  VAL B CG2   1 
ATOM   2459 N N     . ALA A 1 335 ? 5.137  -26.623 -54.275 1.00 39.85 ? 333  ALA B N     1 
ATOM   2460 C CA    . ALA A 1 335 ? 3.718  -26.184 -54.324 1.00 40.15 ? 333  ALA B CA    1 
ATOM   2461 C C     . ALA A 1 335 ? 3.274  -26.148 -55.791 1.00 42.08 ? 333  ALA B C     1 
ATOM   2462 O O     . ALA A 1 335 ? 3.319  -25.077 -56.448 1.00 35.83 ? 333  ALA B O     1 
ATOM   2463 C CB    . ALA A 1 335 ? 3.550  -24.853 -53.634 1.00 39.45 ? 333  ALA B CB    1 
ATOM   2464 N N     . LYS A 1 336 ? 2.850  -27.301 -56.295 1.00 48.16 ? 334  LYS B N     1 
ATOM   2465 C CA    . LYS A 1 336 ? 2.626  -27.526 -57.746 1.00 56.62 ? 334  LYS B CA    1 
ATOM   2466 C C     . LYS A 1 336 ? 1.374  -26.765 -58.207 1.00 51.14 ? 334  LYS B C     1 
ATOM   2467 O O     . LYS A 1 336 ? 1.334  -26.338 -59.376 1.00 56.05 ? 334  LYS B O     1 
ATOM   2468 C CB    . LYS A 1 336 ? 2.589  -29.039 -57.988 1.00 62.45 ? 334  LYS B CB    1 
ATOM   2469 C CG    . LYS A 1 336 ? 3.918  -29.763 -57.754 1.00 64.99 ? 334  LYS B CG    1 
ATOM   2470 C CD    . LYS A 1 336 ? 5.151  -28.977 -58.199 1.00 67.51 ? 334  LYS B CD    1 
ATOM   2471 C CE    . LYS A 1 336 ? 5.099  -28.474 -59.633 1.00 71.75 ? 334  LYS B CE    1 
ATOM   2472 N NZ    . LYS A 1 336 ? 5.801  -29.394 -60.563 1.00 71.81 ? 334  LYS B NZ    1 
ATOM   2473 N N     . ASP A 1 337 ? 0.434  -26.556 -57.289 1.00 50.39 ? 335  ASP B N     1 
ATOM   2474 C CA    . ASP A 1 337 ? -0.853 -25.856 -57.512 1.00 54.44 ? 335  ASP B CA    1 
ATOM   2475 C C     . ASP A 1 337 ? -0.682 -24.342 -57.314 1.00 50.62 ? 335  ASP B C     1 
ATOM   2476 O O     . ASP A 1 337 ? -1.697 -23.623 -57.373 1.00 47.43 ? 335  ASP B O     1 
ATOM   2477 C CB    . ASP A 1 337 ? -1.900 -26.410 -56.543 1.00 62.27 ? 335  ASP B CB    1 
ATOM   2478 C CG    . ASP A 1 337 ? -1.474 -26.281 -55.086 1.00 74.00 ? 335  ASP B CG    1 
ATOM   2479 O OD1   . ASP A 1 337 ? -0.360 -26.758 -54.749 1.00 75.59 ? 335  ASP B OD1   1 
ATOM   2480 O OD2   . ASP A 1 337 ? -2.237 -25.674 -54.303 1.00 76.16 ? 335  ASP B OD2   1 
ATOM   2481 N N     . LYS A 1 338 ? 0.529  -23.854 -57.026 1.00 43.20 ? 336  LYS B N     1 
ATOM   2482 C CA    . LYS A 1 338 ? 0.759  -22.424 -56.691 1.00 39.87 ? 336  LYS B CA    1 
ATOM   2483 C C     . LYS A 1 338 ? 1.830  -21.838 -57.614 1.00 35.21 ? 336  LYS B C     1 
ATOM   2484 O O     . LYS A 1 338 ? 2.532  -22.612 -58.279 1.00 35.12 ? 336  LYS B O     1 
ATOM   2485 C CB    . LYS A 1 338 ? 1.162  -22.295 -55.223 1.00 44.99 ? 336  LYS B CB    1 
ATOM   2486 C CG    . LYS A 1 338 ? 0.023  -22.538 -54.247 1.00 51.65 ? 336  LYS B CG    1 
ATOM   2487 C CD    . LYS A 1 338 ? 0.499  -22.956 -52.884 1.00 60.87 ? 336  LYS B CD    1 
ATOM   2488 C CE    . LYS A 1 338 ? 1.290  -21.878 -52.171 1.00 62.71 ? 336  LYS B CE    1 
ATOM   2489 N NZ    . LYS A 1 338 ? 0.465  -21.210 -51.136 1.00 59.54 ? 336  LYS B NZ    1 
ATOM   2490 N N     . ALA A 1 339 ? 1.988  -20.517 -57.591 1.00 28.16 ? 337  ALA B N     1 
ATOM   2491 C CA    . ALA A 1 339 ? 2.928  -19.766 -58.451 1.00 30.58 ? 337  ALA B CA    1 
ATOM   2492 C C     . ALA A 1 339 ? 4.357  -19.849 -57.880 1.00 28.28 ? 337  ALA B C     1 
ATOM   2493 O O     . ALA A 1 339 ? 5.346  -19.581 -58.629 1.00 26.43 ? 337  ALA B O     1 
ATOM   2494 C CB    . ALA A 1 339 ? 2.422  -18.339 -58.571 1.00 31.35 ? 337  ALA B CB    1 
ATOM   2495 N N     . ALA A 1 340 ? 4.495  -20.238 -56.615 1.00 27.22 ? 338  ALA B N     1 
ATOM   2496 C CA    . ALA A 1 340 ? 5.796  -20.241 -55.896 1.00 27.18 ? 338  ALA B CA    1 
ATOM   2497 C C     . ALA A 1 340 ? 5.688  -21.095 -54.633 1.00 26.70 ? 338  ALA B C     1 
ATOM   2498 O O     . ALA A 1 340 ? 4.547  -21.449 -54.240 1.00 28.52 ? 338  ALA B O     1 
ATOM   2499 C CB    . ALA A 1 340 ? 6.239  -18.816 -55.583 1.00 26.02 ? 338  ALA B CB    1 
ATOM   2500 N N     . ASP A 1 341 ? 6.838  -21.425 -54.048 1.00 24.21 ? 339  ASP B N     1 
ATOM   2501 C CA    . ASP A 1 341 ? 6.953  -22.275 -52.837 1.00 24.97 ? 339  ASP B CA    1 
ATOM   2502 C C     . ASP A 1 341 ? 7.087  -21.412 -51.588 1.00 24.41 ? 339  ASP B C     1 
ATOM   2503 O O     . ASP A 1 341 ? 7.686  -20.339 -51.642 1.00 24.78 ? 339  ASP B O     1 
ATOM   2504 C CB    . ASP A 1 341 ? 8.147  -23.219 -52.945 1.00 25.80 ? 339  ASP B CB    1 
ATOM   2505 C CG    . ASP A 1 341 ? 7.995  -24.255 -54.048 1.00 28.96 ? 339  ASP B CG    1 
ATOM   2506 O OD1   . ASP A 1 341 ? 6.865  -24.381 -54.585 1.00 28.33 ? 339  ASP B OD1   1 
ATOM   2507 O OD2   . ASP A 1 341 ? 8.996  -24.918 -54.357 1.00 26.07 ? 339  ASP B OD2   1 
ATOM   2508 N N     . PRO A 1 342 ? 6.604  -21.909 -50.420 1.00 25.35 ? 340  PRO B N     1 
ATOM   2509 C CA    . PRO A 1 342 ? 6.844  -21.260 -49.129 1.00 25.51 ? 340  PRO B CA    1 
ATOM   2510 C C     . PRO A 1 342 ? 8.358  -21.090 -48.936 1.00 23.60 ? 340  PRO B C     1 
ATOM   2511 O O     . PRO A 1 342 ? 9.091  -22.025 -49.200 1.00 22.85 ? 340  PRO B O     1 
ATOM   2512 C CB    . PRO A 1 342 ? 6.298  -22.237 -48.075 1.00 25.87 ? 340  PRO B CB    1 
ATOM   2513 C CG    . PRO A 1 342 ? 5.321  -23.134 -48.855 1.00 29.28 ? 340  PRO B CG    1 
ATOM   2514 C CD    . PRO A 1 342 ? 5.845  -23.169 -50.279 1.00 26.57 ? 340  PRO B CD    1 
ATOM   2515 N N     . ILE A 1 343 ? 8.798  -19.913 -48.503 1.00 21.87 ? 341  ILE B N     1 
ATOM   2516 C CA    . ILE A 1 343 ? 10.262 -19.604 -48.461 1.00 21.68 ? 341  ILE B CA    1 
ATOM   2517 C C     . ILE A 1 343 ? 11.056 -20.519 -47.519 1.00 21.80 ? 341  ILE B C     1 
ATOM   2518 O O     . ILE A 1 343 ? 12.274 -20.534 -47.625 1.00 20.52 ? 341  ILE B O     1 
ATOM   2519 C CB    . ILE A 1 343 ? 10.472 -18.109 -48.139 1.00 21.57 ? 341  ILE B CB    1 
ATOM   2520 C CG1   . ILE A 1 343 ? 9.882  -17.717 -46.784 1.00 22.32 ? 341  ILE B CG1   1 
ATOM   2521 C CG2   . ILE A 1 343 ? 9.923  -17.251 -49.265 1.00 23.99 ? 341  ILE B CG2   1 
ATOM   2522 C CD1   . ILE A 1 343 ? 10.260 -16.329 -46.341 1.00 22.69 ? 341  ILE B CD1   1 
ATOM   2523 N N     . ILE A 1 344 ? 10.370 -21.221 -46.631 1.00 22.65 ? 342  ILE B N     1 
ATOM   2524 C CA    . ILE A 1 344 ? 11.042 -22.183 -45.707 1.00 25.56 ? 342  ILE B CA    1 
ATOM   2525 C C     . ILE A 1 344 ? 11.747 -23.301 -46.494 1.00 24.11 ? 342  ILE B C     1 
ATOM   2526 O O     . ILE A 1 344 ? 12.568 -23.992 -45.910 1.00 21.87 ? 342  ILE B O     1 
ATOM   2527 C CB    . ILE A 1 344 ? 10.020 -22.742 -44.696 1.00 26.07 ? 342  ILE B CB    1 
ATOM   2528 C CG1   . ILE A 1 344 ? 10.688 -23.553 -43.584 1.00 26.72 ? 342  ILE B CG1   1 
ATOM   2529 C CG2   . ILE A 1 344 ? 8.933  -23.531 -45.407 1.00 27.68 ? 342  ILE B CG2   1 
ATOM   2530 C CD1   . ILE A 1 344 ? 9.883  -23.610 -42.312 1.00 28.25 ? 342  ILE B CD1   1 
ATOM   2531 N N     . VAL A 1 345 ? 11.438 -23.440 -47.783 1.00 23.86 ? 343  VAL B N     1 
ATOM   2532 C CA    . VAL A 1 345 ? 12.064 -24.510 -48.616 1.00 23.61 ? 343  VAL B CA    1 
ATOM   2533 C C     . VAL A 1 345 ? 13.517 -24.146 -48.920 1.00 22.36 ? 343  VAL B C     1 
ATOM   2534 O O     . VAL A 1 345 ? 14.282 -25.054 -49.210 1.00 24.53 ? 343  VAL B O     1 
ATOM   2535 C CB    . VAL A 1 345 ? 11.276 -24.718 -49.925 1.00 23.92 ? 343  VAL B CB    1 
ATOM   2536 C CG1   . VAL A 1 345 ? 9.830  -25.113 -49.676 1.00 23.33 ? 343  VAL B CG1   1 
ATOM   2537 C CG2   . VAL A 1 345 ? 11.363 -23.513 -50.849 1.00 23.15 ? 343  VAL B CG2   1 
ATOM   2538 N N     . HIS A 1 346 ? 13.864 -22.866 -48.836 1.00 21.35 ? 344  HIS B N     1 
ATOM   2539 C CA    . HIS A 1 346 ? 15.202 -22.360 -49.254 1.00 21.34 ? 344  HIS B CA    1 
ATOM   2540 C C     . HIS A 1 346 ? 16.240 -22.618 -48.169 1.00 23.28 ? 344  HIS B C     1 
ATOM   2541 O O     . HIS A 1 346 ? 15.995 -22.280 -47.008 1.00 22.43 ? 344  HIS B O     1 
ATOM   2542 C CB    . HIS A 1 346 ? 15.121 -20.868 -49.642 1.00 21.29 ? 344  HIS B CB    1 
ATOM   2543 C CG    . HIS A 1 346 ? 14.263 -20.671 -50.846 1.00 22.38 ? 344  HIS B CG    1 
ATOM   2544 N ND1   . HIS A 1 346 ? 13.126 -19.879 -50.839 1.00 25.19 ? 344  HIS B ND1   1 
ATOM   2545 C CD2   . HIS A 1 346 ? 14.328 -21.254 -52.056 1.00 20.57 ? 344  HIS B CD2   1 
ATOM   2546 C CE1   . HIS A 1 346 ? 12.570 -19.936 -52.032 1.00 23.36 ? 344  HIS B CE1   1 
ATOM   2547 N NE2   . HIS A 1 346 ? 13.289 -20.794 -52.789 1.00 25.22 ? 344  HIS B NE2   1 
ATOM   2548 N N     . PRO A 1 347 ? 17.400 -23.239 -48.518 1.00 22.74 ? 345  PRO B N     1 
ATOM   2549 C CA    . PRO A 1 347 ? 18.468 -23.497 -47.553 1.00 21.60 ? 345  PRO B CA    1 
ATOM   2550 C C     . PRO A 1 347 ? 18.826 -22.273 -46.700 1.00 22.30 ? 345  PRO B C     1 
ATOM   2551 O O     . PRO A 1 347 ? 18.923 -22.418 -45.462 1.00 22.26 ? 345  PRO B O     1 
ATOM   2552 C CB    . PRO A 1 347 ? 19.660 -23.955 -48.410 1.00 21.71 ? 345  PRO B CB    1 
ATOM   2553 C CG    . PRO A 1 347 ? 19.019 -24.538 -49.666 1.00 22.59 ? 345  PRO B CG    1 
ATOM   2554 C CD    . PRO A 1 347 ? 17.738 -23.748 -49.860 1.00 21.58 ? 345  PRO B CD    1 
ATOM   2555 N N     . ASP A 1 348 ? 19.006 -21.106 -47.312 1.00 21.40 ? 346  ASP B N     1 
ATOM   2556 C CA    . ASP A 1 348 ? 19.429 -19.903 -46.545 1.00 21.79 ? 346  ASP B CA    1 
ATOM   2557 C C     . ASP A 1 348 ? 18.368 -19.486 -45.510 1.00 21.72 ? 346  ASP B C     1 
ATOM   2558 O O     . ASP A 1 348 ? 18.740 -19.040 -44.411 1.00 20.04 ? 346  ASP B O     1 
ATOM   2559 C CB    . ASP A 1 348 ? 19.719 -18.725 -47.458 1.00 22.03 ? 346  ASP B CB    1 
ATOM   2560 C CG    . ASP A 1 348 ? 20.342 -17.576 -46.699 1.00 23.26 ? 346  ASP B CG    1 
ATOM   2561 O OD1   . ASP A 1 348 ? 21.369 -17.835 -46.000 1.00 25.20 ? 346  ASP B OD1   1 
ATOM   2562 O OD2   . ASP A 1 348 ? 19.798 -16.436 -46.807 1.00 24.38 ? 346  ASP B OD2   1 
ATOM   2563 N N     . VAL A 1 349 ? 17.083 -19.622 -45.835 1.00 20.96 ? 347  VAL B N     1 
ATOM   2564 C CA    . VAL A 1 349 ? 15.990 -19.257 -44.888 1.00 20.83 ? 347  VAL B CA    1 
ATOM   2565 C C     . VAL A 1 349 ? 15.987 -20.245 -43.721 1.00 21.52 ? 347  VAL B C     1 
ATOM   2566 O O     . VAL A 1 349 ? 15.838 -19.815 -42.590 1.00 21.61 ? 347  VAL B O     1 
ATOM   2567 C CB    . VAL A 1 349 ? 14.628 -19.209 -45.603 1.00 19.82 ? 347  VAL B CB    1 
ATOM   2568 C CG1   . VAL A 1 349 ? 13.476 -18.950 -44.646 1.00 20.33 ? 347  VAL B CG1   1 
ATOM   2569 C CG2   . VAL A 1 349 ? 14.623 -18.204 -46.743 1.00 20.59 ? 347  VAL B CG2   1 
ATOM   2570 N N     . ARG A 1 350 ? 16.146 -21.527 -44.028 1.00 21.80 ? 348  ARG B N     1 
ATOM   2571 C CA    . ARG A 1 350 ? 16.227 -22.557 -42.970 1.00 22.10 ? 348  ARG B CA    1 
ATOM   2572 C C     . ARG A 1 350 ? 17.438 -22.287 -42.069 1.00 21.91 ? 348  ARG B C     1 
ATOM   2573 O O     . ARG A 1 350 ? 17.303 -22.397 -40.866 1.00 22.53 ? 348  ARG B O     1 
ATOM   2574 C CB    . ARG A 1 350 ? 16.294 -23.952 -43.599 1.00 22.13 ? 348  ARG B CB    1 
ATOM   2575 C CG    . ARG A 1 350 ? 14.922 -24.551 -43.867 1.00 23.39 ? 348  ARG B CG    1 
ATOM   2576 C CD    . ARG A 1 350 ? 14.903 -25.748 -44.795 1.00 23.10 ? 348  ARG B CD    1 
ATOM   2577 N NE    . ARG A 1 350 ? 13.594 -26.380 -44.781 1.00 24.12 ? 348  ARG B NE    1 
ATOM   2578 C CZ    . ARG A 1 350 ? 13.247 -27.376 -43.976 1.00 24.52 ? 348  ARG B CZ    1 
ATOM   2579 N NH1   . ARG A 1 350 ? 12.027 -27.879 -44.035 1.00 24.44 ? 348  ARG B NH1   1 
ATOM   2580 N NH2   . ARG A 1 350 ? 14.116 -27.870 -43.114 1.00 23.58 ? 348  ARG B NH2   1 
ATOM   2581 N N     . ARG A 1 351 ? 18.573 -21.941 -42.660 1.00 23.28 ? 349  ARG B N     1 
ATOM   2582 C CA    . ARG A 1 351 ? 19.779 -21.606 -41.858 1.00 22.79 ? 349  ARG B CA    1 
ATOM   2583 C C     . ARG A 1 351 ? 19.458 -20.483 -40.861 1.00 21.18 ? 349  ARG B C     1 
ATOM   2584 O O     . ARG A 1 351 ? 19.757 -20.636 -39.689 1.00 21.17 ? 349  ARG B O     1 
ATOM   2585 C CB    . ARG A 1 351 ? 20.929 -21.182 -42.768 1.00 22.88 ? 349  ARG B CB    1 
ATOM   2586 C CG    . ARG A 1 351 ? 22.247 -20.943 -42.050 1.00 24.81 ? 349  ARG B CG    1 
ATOM   2587 C CD    . ARG A 1 351 ? 23.286 -20.299 -42.949 1.00 23.81 ? 349  ARG B CD    1 
ATOM   2588 N NE    . ARG A 1 351 ? 22.840 -19.049 -43.542 1.00 25.98 ? 349  ARG B NE    1 
ATOM   2589 C CZ    . ARG A 1 351 ? 22.992 -17.856 -42.982 1.00 28.21 ? 349  ARG B CZ    1 
ATOM   2590 N NH1   . ARG A 1 351 ? 22.559 -16.770 -43.597 1.00 26.40 ? 349  ARG B NH1   1 
ATOM   2591 N NH2   . ARG A 1 351 ? 23.583 -17.752 -41.806 1.00 29.14 ? 349  ARG B NH2   1 
ATOM   2592 N N     . MET A 1 352 ? 18.867 -19.401 -41.351 1.00 20.85 ? 350  MET B N     1 
ATOM   2593 C CA    . MET A 1 352 ? 18.550 -18.255 -40.471 1.00 21.42 ? 350  MET B CA    1 
ATOM   2594 C C     . MET A 1 352 ? 17.537 -18.688 -39.399 1.00 23.80 ? 350  MET B C     1 
ATOM   2595 O O     . MET A 1 352 ? 17.751 -18.390 -38.232 1.00 20.33 ? 350  MET B O     1 
ATOM   2596 C CB    . MET A 1 352 ? 18.013 -17.088 -41.301 1.00 22.02 ? 350  MET B CB    1 
ATOM   2597 C CG    . MET A 1 352 ? 19.024 -16.522 -42.279 1.00 22.64 ? 350  MET B CG    1 
ATOM   2598 S SD    . MET A 1 352 ? 18.546 -14.921 -42.996 1.00 23.41 ? 350  MET B SD    1 
ATOM   2599 C CE    . MET A 1 352 ? 17.551 -15.468 -44.381 1.00 22.56 ? 350  MET B CE    1 
ATOM   2600 N N     . LEU A 1 353 ? 16.491 -19.410 -39.808 1.00 23.57 ? 351  LEU B N     1 
ATOM   2601 C CA    . LEU A 1 353 ? 15.458 -19.867 -38.849 1.00 23.73 ? 351  LEU B CA    1 
ATOM   2602 C C     . LEU A 1 353 ? 16.094 -20.783 -37.799 1.00 23.20 ? 351  LEU B C     1 
ATOM   2603 O O     . LEU A 1 353 ? 15.796 -20.622 -36.622 1.00 20.99 ? 351  LEU B O     1 
ATOM   2604 C CB    . LEU A 1 353 ? 14.359 -20.613 -39.614 1.00 23.10 ? 351  LEU B CB    1 
ATOM   2605 C CG    . LEU A 1 353 ? 13.373 -19.750 -40.395 1.00 24.77 ? 351  LEU B CG    1 
ATOM   2606 C CD1   . LEU A 1 353 ? 12.558 -20.609 -41.346 1.00 25.73 ? 351  LEU B CD1   1 
ATOM   2607 C CD2   . LEU A 1 353 ? 12.456 -18.985 -39.454 1.00 25.19 ? 351  LEU B CD2   1 
ATOM   2608 N N     . LEU A 1 354 ? 16.934 -21.718 -38.236 1.00 22.36 ? 352  LEU B N     1 
ATOM   2609 C CA    . LEU A 1 354 ? 17.490 -22.717 -37.287 1.00 23.47 ? 352  LEU B CA    1 
ATOM   2610 C C     . LEU A 1 354 ? 18.520 -22.059 -36.361 1.00 23.89 ? 352  LEU B C     1 
ATOM   2611 O O     . LEU A 1 354 ? 18.685 -22.533 -35.248 1.00 22.94 ? 352  LEU B O     1 
ATOM   2612 C CB    . LEU A 1 354 ? 18.078 -23.887 -38.075 1.00 21.72 ? 352  LEU B CB    1 
ATOM   2613 C CG    . LEU A 1 354 ? 17.056 -24.809 -38.734 1.00 23.83 ? 352  LEU B CG    1 
ATOM   2614 C CD1   . LEU A 1 354 ? 17.717 -25.687 -39.781 1.00 24.78 ? 352  LEU B CD1   1 
ATOM   2615 C CD2   . LEU A 1 354 ? 16.348 -25.660 -37.694 1.00 24.70 ? 352  LEU B CD2   1 
ATOM   2616 N N     . THR A 1 355 ? 19.168 -21.001 -36.838 1.00 25.40 ? 353  THR B N     1 
ATOM   2617 C CA    . THR A 1 355 ? 20.134 -20.265 -35.989 1.00 25.54 ? 353  THR B CA    1 
ATOM   2618 C C     . THR A 1 355 ? 19.337 -19.620 -34.850 1.00 23.71 ? 353  THR B C     1 
ATOM   2619 O O     . THR A 1 355 ? 19.714 -19.801 -33.697 1.00 21.89 ? 353  THR B O     1 
ATOM   2620 C CB    . THR A 1 355 ? 20.958 -19.283 -36.835 1.00 25.97 ? 353  THR B CB    1 
ATOM   2621 O OG1   . THR A 1 355 ? 21.651 -19.991 -37.861 1.00 24.07 ? 353  THR B OG1   1 
ATOM   2622 C CG2   . THR A 1 355 ? 21.940 -18.487 -36.004 1.00 26.77 ? 353  THR B CG2   1 
ATOM   2623 N N     . MET A 1 356 ? 18.252 -18.934 -35.195 1.00 23.60 ? 354  MET B N     1 
ATOM   2624 C CA    . MET A 1 356 ? 17.369 -18.331 -34.171 1.00 23.46 ? 354  MET B CA    1 
ATOM   2625 C C     . MET A 1 356 ? 16.835 -19.412 -33.227 1.00 23.62 ? 354  MET B C     1 
ATOM   2626 O O     . MET A 1 356 ? 16.928 -19.237 -32.022 1.00 22.23 ? 354  MET B O     1 
ATOM   2627 C CB    . MET A 1 356 ? 16.179 -17.654 -34.848 1.00 24.71 ? 354  MET B CB    1 
ATOM   2628 C CG    . MET A 1 356 ? 16.533 -16.597 -35.871 1.00 24.19 ? 354  MET B CG    1 
ATOM   2629 S SD    . MET A 1 356 ? 15.034 -15.984 -36.684 1.00 23.79 ? 354  MET B SD    1 
ATOM   2630 C CE    . MET A 1 356 ? 14.324 -15.003 -35.365 1.00 24.07 ? 354  MET B CE    1 
ATOM   2631 N N     . LYS A 1 357 ? 16.311 -20.495 -33.788 1.00 23.48 ? 355  LYS B N     1 
ATOM   2632 C CA    . LYS A 1 357 ? 15.689 -21.564 -32.969 1.00 24.06 ? 355  LYS B CA    1 
ATOM   2633 C C     . LYS A 1 357 ? 16.713 -22.135 -31.979 1.00 24.08 ? 355  LYS B C     1 
ATOM   2634 O O     . LYS A 1 357 ? 16.378 -22.274 -30.806 1.00 23.06 ? 355  LYS B O     1 
ATOM   2635 C CB    . LYS A 1 357 ? 15.138 -22.645 -33.898 1.00 24.31 ? 355  LYS B CB    1 
ATOM   2636 C CG    . LYS A 1 357 ? 14.108 -23.597 -33.311 1.00 26.47 ? 355  LYS B CG    1 
ATOM   2637 C CD    . LYS A 1 357 ? 13.625 -24.608 -34.335 1.00 26.75 ? 355  LYS B CD    1 
ATOM   2638 C CE    . LYS A 1 357 ? 12.470 -25.459 -33.852 1.00 26.65 ? 355  LYS B CE    1 
ATOM   2639 N NZ    . LYS A 1 357 ? 12.839 -26.240 -32.653 1.00 25.97 ? 355  LYS B NZ    1 
ATOM   2640 N N     . ALA A 1 358 ? 17.913 -22.446 -32.454 1.00 23.88 ? 356  ALA B N     1 
ATOM   2641 C CA    . ALA A 1 358 ? 18.920 -23.096 -31.591 1.00 22.71 ? 356  ALA B CA    1 
ATOM   2642 C C     . ALA A 1 358 ? 19.466 -22.114 -30.546 1.00 23.57 ? 356  ALA B C     1 
ATOM   2643 O O     . ALA A 1 358 ? 19.745 -22.535 -29.424 1.00 22.37 ? 356  ALA B O     1 
ATOM   2644 C CB    . ALA A 1 358 ? 20.001 -23.678 -32.451 1.00 25.50 ? 356  ALA B CB    1 
ATOM   2645 N N     . LEU A 1 359 ? 19.617 -20.855 -30.931 1.00 21.99 ? 357  LEU B N     1 
ATOM   2646 C CA    . LEU A 1 359 ? 20.071 -19.829 -29.951 1.00 22.84 ? 357  LEU B CA    1 
ATOM   2647 C C     . LEU A 1 359 ? 18.953 -19.567 -28.922 1.00 22.50 ? 357  LEU B C     1 
ATOM   2648 O O     . LEU A 1 359 ? 19.268 -19.457 -27.739 1.00 22.30 ? 357  LEU B O     1 
ATOM   2649 C CB    . LEU A 1 359 ? 20.485 -18.556 -30.687 1.00 21.23 ? 357  LEU B CB    1 
ATOM   2650 C CG    . LEU A 1 359 ? 21.800 -18.643 -31.470 1.00 21.35 ? 357  LEU B CG    1 
ATOM   2651 C CD1   . LEU A 1 359 ? 22.121 -17.318 -32.151 1.00 21.79 ? 357  LEU B CD1   1 
ATOM   2652 C CD2   . LEU A 1 359 ? 22.966 -19.090 -30.601 1.00 22.84 ? 357  LEU B CD2   1 
ATOM   2653 N N     . ASN A 1 360 ? 17.701 -19.441 -29.355 1.00 21.20 ? 358  ASN B N     1 
ATOM   2654 C CA    . ASN A 1 360 ? 16.569 -19.199 -28.422 1.00 21.76 ? 358  ASN B CA    1 
ATOM   2655 C C     . ASN A 1 360 ? 16.431 -20.378 -27.452 1.00 22.41 ? 358  ASN B C     1 
ATOM   2656 O O     . ASN A 1 360 ? 16.340 -20.128 -26.253 1.00 22.29 ? 358  ASN B O     1 
ATOM   2657 C CB    . ASN A 1 360 ? 15.260 -18.949 -29.147 1.00 22.86 ? 358  ASN B CB    1 
ATOM   2658 C CG    . ASN A 1 360 ? 15.177 -17.592 -29.801 1.00 22.32 ? 358  ASN B CG    1 
ATOM   2659 O OD1   . ASN A 1 360 ? 15.851 -16.651 -29.400 1.00 23.69 ? 358  ASN B OD1   1 
ATOM   2660 N ND2   . ASN A 1 360 ? 14.309 -17.483 -30.784 1.00 22.77 ? 358  ASN B ND2   1 
ATOM   2661 N N     . GLU A 1 361 ? 16.389 -21.611 -27.951 1.00 22.22 ? 359  GLU B N     1 
ATOM   2662 C CA    . GLU A 1 361 ? 16.175 -22.809 -27.105 1.00 23.52 ? 359  GLU B CA    1 
ATOM   2663 C C     . GLU A 1 361 ? 17.394 -23.076 -26.219 1.00 24.68 ? 359  GLU B C     1 
ATOM   2664 O O     . GLU A 1 361 ? 17.200 -23.364 -25.016 1.00 23.64 ? 359  GLU B O     1 
ATOM   2665 C CB    . GLU A 1 361 ? 15.781 -23.990 -27.972 1.00 24.01 ? 359  GLU B CB    1 
ATOM   2666 C CG    . GLU A 1 361 ? 14.370 -23.823 -28.496 1.00 24.86 ? 359  GLU B CG    1 
ATOM   2667 C CD    . GLU A 1 361 ? 13.881 -24.899 -29.436 1.00 25.60 ? 359  GLU B CD    1 
ATOM   2668 O OE1   . GLU A 1 361 ? 14.228 -26.086 -29.228 1.00 26.46 ? 359  GLU B OE1   1 
ATOM   2669 O OE2   . GLU A 1 361 ? 13.133 -24.543 -30.363 1.00 28.71 ? 359  GLU B OE2   1 
ATOM   2670 N N     . GLY A 1 362 ? 18.603 -22.942 -26.764 1.00 22.66 ? 360  GLY B N     1 
ATOM   2671 C CA    . GLY A 1 362 ? 19.841 -22.992 -25.981 1.00 23.76 ? 360  GLY B CA    1 
ATOM   2672 C C     . GLY A 1 362 ? 19.858 -21.957 -24.881 1.00 23.56 ? 360  GLY B C     1 
ATOM   2673 O O     . GLY A 1 362 ? 20.177 -22.323 -23.736 1.00 26.24 ? 360  GLY B O     1 
ATOM   2674 N N     . GLY A 1 363 ? 19.583 -20.703 -25.222 1.00 24.48 ? 361  GLY B N     1 
ATOM   2675 C CA    . GLY A 1 363 ? 19.527 -19.594 -24.255 1.00 24.95 ? 361  GLY B CA    1 
ATOM   2676 C C     . GLY A 1 363 ? 18.495 -19.866 -23.174 1.00 24.07 ? 361  GLY B C     1 
ATOM   2677 O O     . GLY A 1 363 ? 18.765 -19.599 -21.998 1.00 24.14 ? 361  GLY B O     1 
ATOM   2678 N N     . ARG A 1 364 ? 17.322 -20.367 -23.552 1.00 26.93 ? 362  ARG B N     1 
ATOM   2679 C CA    . ARG A 1 364 ? 16.231 -20.605 -22.578 1.00 25.44 ? 362  ARG B CA    1 
ATOM   2680 C C     . ARG A 1 364 ? 16.749 -21.607 -21.540 1.00 27.06 ? 362  ARG B C     1 
ATOM   2681 O O     . ARG A 1 364 ? 16.641 -21.329 -20.308 1.00 29.31 ? 362  ARG B O     1 
ATOM   2682 C CB    . ARG A 1 364 ? 14.930 -21.037 -23.271 1.00 26.03 ? 362  ARG B CB    1 
ATOM   2683 C CG    . ARG A 1 364 ? 13.833 -21.396 -22.272 1.00 25.40 ? 362  ARG B CG    1 
ATOM   2684 C CD    . ARG A 1 364 ? 12.450 -21.651 -22.850 1.00 24.74 ? 362  ARG B CD    1 
ATOM   2685 N NE    . ARG A 1 364 ? 12.088 -20.498 -23.648 1.00 26.33 ? 362  ARG B NE    1 
ATOM   2686 C CZ    . ARG A 1 364 ? 12.005 -20.483 -24.988 1.00 24.35 ? 362  ARG B CZ    1 
ATOM   2687 N NH1   . ARG A 1 364 ? 12.202 -21.578 -25.699 1.00 24.48 ? 362  ARG B NH1   1 
ATOM   2688 N NH2   . ARG A 1 364 ? 11.713 -19.363 -25.608 1.00 22.73 ? 362  ARG B NH2   1 
ATOM   2689 N N     . ALA A 1 365 ? 17.329 -22.709 -22.006 1.00 25.25 ? 363  ALA B N     1 
ATOM   2690 C CA    . ALA A 1 365 ? 17.955 -23.755 -21.174 1.00 25.89 ? 363  ALA B CA    1 
ATOM   2691 C C     . ALA A 1 365 ? 19.045 -23.136 -20.280 1.00 26.81 ? 363  ALA B C     1 
ATOM   2692 O O     . ALA A 1 365 ? 19.074 -23.458 -19.069 1.00 26.00 ? 363  ALA B O     1 
ATOM   2693 C CB    . ALA A 1 365 ? 18.507 -24.868 -22.045 1.00 25.34 ? 363  ALA B CB    1 
ATOM   2694 N N     . PHE A 1 366 ? 19.931 -22.293 -20.827 1.00 24.86 ? 364  PHE B N     1 
ATOM   2695 C CA    . PHE A 1 366 ? 21.019 -21.673 -20.031 1.00 23.18 ? 364  PHE B CA    1 
ATOM   2696 C C     . PHE A 1 366 ? 20.403 -20.754 -18.965 1.00 22.69 ? 364  PHE B C     1 
ATOM   2697 O O     . PHE A 1 366 ? 20.889 -20.804 -17.837 1.00 24.02 ? 364  PHE B O     1 
ATOM   2698 C CB    . PHE A 1 366 ? 22.031 -20.947 -20.913 1.00 23.65 ? 364  PHE B CB    1 
ATOM   2699 C CG    . PHE A 1 366 ? 23.256 -20.513 -20.178 1.00 23.15 ? 364  PHE B CG    1 
ATOM   2700 C CD1   . PHE A 1 366 ? 24.061 -21.444 -19.549 1.00 23.66 ? 364  PHE B CD1   1 
ATOM   2701 C CD2   . PHE A 1 366 ? 23.554 -19.168 -20.043 1.00 25.94 ? 364  PHE B CD2   1 
ATOM   2702 C CE1   . PHE A 1 366 ? 25.171 -21.040 -18.835 1.00 24.67 ? 364  PHE B CE1   1 
ATOM   2703 C CE2   . PHE A 1 366 ? 24.689 -18.764 -19.365 1.00 25.22 ? 364  PHE B CE2   1 
ATOM   2704 C CZ    . PHE A 1 366 ? 25.480 -19.700 -18.739 1.00 24.91 ? 364  PHE B CZ    1 
ATOM   2705 N N     . SER A 1 367 ? 19.374 -19.977 -19.287 1.00 22.80 ? 365  SER B N     1 
ATOM   2706 C CA    . SER A 1 367 ? 18.700 -19.044 -18.345 1.00 25.41 ? 365  SER B CA    1 
ATOM   2707 C C     . SER A 1 367 ? 18.100 -19.847 -17.179 1.00 28.04 ? 365  SER B C     1 
ATOM   2708 O O     . SER A 1 367 ? 18.332 -19.488 -16.000 1.00 25.95 ? 365  SER B O     1 
ATOM   2709 C CB    . SER A 1 367 ? 17.685 -18.167 -19.050 1.00 26.10 ? 365  SER B CB    1 
ATOM   2710 O OG    . SER A 1 367 ? 16.485 -18.866 -19.348 1.00 27.04 ? 365  SER B OG    1 
ATOM   2711 N N     . SER A 1 368 ? 17.454 -20.974 -17.471 1.00 28.11 ? 366  SER B N     1 
ATOM   2712 C CA    . SER A 1 368 ? 16.893 -21.884 -16.442 1.00 26.20 ? 366  SER B CA    1 
ATOM   2713 C C     . SER A 1 368 ? 18.011 -22.503 -15.607 1.00 29.12 ? 366  SER B C     1 
ATOM   2714 O O     . SER A 1 368 ? 17.811 -22.656 -14.384 1.00 29.51 ? 366  SER B O     1 
ATOM   2715 C CB    . SER A 1 368 ? 16.003 -22.931 -17.048 1.00 26.95 ? 366  SER B CB    1 
ATOM   2716 O OG    . SER A 1 368 ? 14.810 -22.319 -17.498 1.00 27.09 ? 366  SER B OG    1 
ATOM   2717 N N     . TYR A 1 369 ? 19.157 -22.826 -16.211 1.00 28.47 ? 367  TYR B N     1 
ATOM   2718 C CA    . TYR A 1 369 ? 20.312 -23.410 -15.481 1.00 25.42 ? 367  TYR B CA    1 
ATOM   2719 C C     . TYR A 1 369 ? 20.835 -22.393 -14.484 1.00 25.96 ? 367  TYR B C     1 
ATOM   2720 O O     . TYR A 1 369 ? 21.031 -22.726 -13.293 1.00 27.60 ? 367  TYR B O     1 
ATOM   2721 C CB    . TYR A 1 369 ? 21.416 -23.812 -16.448 1.00 26.14 ? 367  TYR B CB    1 
ATOM   2722 C CG    . TYR A 1 369 ? 22.611 -24.457 -15.805 1.00 25.14 ? 367  TYR B CG    1 
ATOM   2723 C CD1   . TYR A 1 369 ? 22.637 -25.819 -15.566 1.00 26.32 ? 367  TYR B CD1   1 
ATOM   2724 C CD2   . TYR A 1 369 ? 23.728 -23.720 -15.478 1.00 25.65 ? 367  TYR B CD2   1 
ATOM   2725 C CE1   . TYR A 1 369 ? 23.727 -26.433 -14.972 1.00 27.60 ? 367  TYR B CE1   1 
ATOM   2726 C CE2   . TYR A 1 369 ? 24.843 -24.323 -14.919 1.00 28.71 ? 367  TYR B CE2   1 
ATOM   2727 C CZ    . TYR A 1 369 ? 24.853 -25.690 -14.681 1.00 28.78 ? 367  TYR B CZ    1 
ATOM   2728 O OH    . TYR A 1 369 ? 25.948 -26.291 -14.121 1.00 27.88 ? 367  TYR B OH    1 
ATOM   2729 N N     . VAL A 1 370 ? 21.010 -21.156 -14.933 1.00 24.85 ? 368  VAL B N     1 
ATOM   2730 C CA    . VAL A 1 370 ? 21.524 -20.081 -14.039 1.00 24.71 ? 368  VAL B CA    1 
ATOM   2731 C C     . VAL A 1 370 ? 20.484 -19.831 -12.936 1.00 25.79 ? 368  VAL B C     1 
ATOM   2732 O O     . VAL A 1 370 ? 20.858 -19.878 -11.733 1.00 27.51 ? 368  VAL B O     1 
ATOM   2733 C CB    . VAL A 1 370 ? 21.931 -18.831 -14.833 1.00 26.16 ? 368  VAL B CB    1 
ATOM   2734 C CG1   . VAL A 1 370 ? 22.378 -17.688 -13.930 1.00 26.46 ? 368  VAL B CG1   1 
ATOM   2735 C CG2   . VAL A 1 370 ? 23.055 -19.175 -15.816 1.00 25.65 ? 368  VAL B CG2   1 
ATOM   2736 N N     . ALA A 1 371 ? 19.210 -19.684 -13.289 1.00 26.06 ? 369  ALA B N     1 
ATOM   2737 C CA    . ALA A 1 371 ? 18.110 -19.511 -12.314 1.00 26.43 ? 369  ALA B CA    1 
ATOM   2738 C C     . ALA A 1 371 ? 18.169 -20.625 -11.267 1.00 27.97 ? 369  ALA B C     1 
ATOM   2739 O O     . ALA A 1 371 ? 17.965 -20.342 -10.066 1.00 27.14 ? 369  ALA B O     1 
ATOM   2740 C CB    . ALA A 1 371 ? 16.792 -19.495 -13.028 1.00 28.29 ? 369  ALA B CB    1 
ATOM   2741 N N     . MET A 1 372 ? 18.428 -21.857 -11.703 1.00 26.83 ? 370  MET B N     1 
ATOM   2742 C CA    . MET A 1 372 ? 18.555 -23.020 -10.807 1.00 28.58 ? 370  MET B CA    1 
ATOM   2743 C C     . MET A 1 372 ? 19.723 -22.784 -9.832  1.00 29.61 ? 370  MET B C     1 
ATOM   2744 O O     . MET A 1 372 ? 19.564 -23.109 -8.649  1.00 29.23 ? 370  MET B O     1 
ATOM   2745 C CB    . MET A 1 372 ? 18.772 -24.288 -11.632 1.00 34.10 ? 370  MET B CB    1 
ATOM   2746 C CG    . MET A 1 372 ? 18.743 -25.571 -10.835 1.00 40.44 ? 370  MET B CG    1 
ATOM   2747 S SD    . MET A 1 372 ? 18.978 -27.028 -11.920 1.00 45.82 ? 370  MET B SD    1 
ATOM   2748 C CE    . MET A 1 372 ? 20.750 -26.934 -12.191 1.00 46.74 ? 370  MET B CE    1 
ATOM   2749 N N     . GLN A 1 373 ? 20.833 -22.189 -10.277 1.00 25.86 ? 371  GLN B N     1 
ATOM   2750 C CA    . GLN A 1 373 ? 22.000 -21.916 -9.396  1.00 28.51 ? 371  GLN B CA    1 
ATOM   2751 C C     . GLN A 1 373 ? 21.617 -20.850 -8.372  1.00 27.76 ? 371  GLN B C     1 
ATOM   2752 O O     . GLN A 1 373 ? 21.930 -21.048 -7.190  1.00 27.98 ? 371  GLN B O     1 
ATOM   2753 C CB    . GLN A 1 373 ? 23.252 -21.504 -10.180 1.00 27.05 ? 371  GLN B CB    1 
ATOM   2754 C CG    . GLN A 1 373 ? 23.762 -22.584 -11.120 1.00 28.41 ? 371  GLN B CG    1 
ATOM   2755 C CD    . GLN A 1 373 ? 23.995 -23.939 -10.503 1.00 29.16 ? 371  GLN B CD    1 
ATOM   2756 O OE1   . GLN A 1 373 ? 24.166 -24.096 -9.295  1.00 35.66 ? 371  GLN B OE1   1 
ATOM   2757 N NE2   . GLN A 1 373 ? 24.020 -24.949 -11.347 1.00 31.21 ? 371  GLN B NE2   1 
ATOM   2758 N N     . LEU A 1 374 ? 20.928 -19.794 -8.796  1.00 28.55 ? 372  LEU B N     1 
ATOM   2759 C CA    . LEU A 1 374 ? 20.435 -18.743 -7.872  1.00 29.57 ? 372  LEU B CA    1 
ATOM   2760 C C     . LEU A 1 374 ? 19.527 -19.371 -6.791  1.00 32.72 ? 372  LEU B C     1 
ATOM   2761 O O     . LEU A 1 374 ? 19.710 -19.045 -5.599  1.00 29.01 ? 372  LEU B O     1 
ATOM   2762 C CB    . LEU A 1 374 ? 19.724 -17.664 -8.688  1.00 28.00 ? 372  LEU B CB    1 
ATOM   2763 C CG    . LEU A 1 374 ? 20.642 -16.718 -9.472  1.00 29.70 ? 372  LEU B CG    1 
ATOM   2764 C CD1   . LEU A 1 374 ? 19.851 -15.921 -10.474 1.00 29.67 ? 372  LEU B CD1   1 
ATOM   2765 C CD2   . LEU A 1 374 ? 21.371 -15.742 -8.559  1.00 30.28 ? 372  LEU B CD2   1 
ATOM   2766 N N     . ASP A 1 375 ? 18.622 -20.276 -7.177  1.00 29.97 ? 373  ASP B N     1 
ATOM   2767 C CA    . ASP A 1 375 ? 17.678 -20.955 -6.255  1.00 31.19 ? 373  ASP B CA    1 
ATOM   2768 C C     . ASP A 1 375 ? 18.443 -21.848 -5.268  1.00 33.15 ? 373  ASP B C     1 
ATOM   2769 O O     . ASP A 1 375 ? 18.106 -21.833 -4.040  1.00 29.95 ? 373  ASP B O     1 
ATOM   2770 C CB    . ASP A 1 375 ? 16.638 -21.741 -7.054  1.00 29.24 ? 373  ASP B CB    1 
ATOM   2771 C CG    . ASP A 1 375 ? 15.538 -20.870 -7.633  1.00 31.28 ? 373  ASP B CG    1 
ATOM   2772 O OD1   . ASP A 1 375 ? 15.355 -19.717 -7.141  1.00 33.99 ? 373  ASP B OD1   1 
ATOM   2773 O OD2   . ASP A 1 375 ? 14.858 -21.337 -8.571  1.00 31.23 ? 373  ASP B OD2   1 
ATOM   2774 N N     . THR A 1 376 ? 19.397 -22.635 -5.768  1.00 31.21 ? 374  THR B N     1 
ATOM   2775 C CA    . THR A 1 376 ? 20.225 -23.529 -4.932  1.00 32.65 ? 374  THR B CA    1 
ATOM   2776 C C     . THR A 1 376 ? 20.989 -22.672 -3.912  1.00 35.46 ? 374  THR B C     1 
ATOM   2777 O O     . THR A 1 376 ? 20.960 -23.031 -2.722  1.00 34.15 ? 374  THR B O     1 
ATOM   2778 C CB    . THR A 1 376 ? 21.115 -24.429 -5.795  1.00 33.95 ? 374  THR B CB    1 
ATOM   2779 O OG1   . THR A 1 376 ? 20.278 -25.121 -6.720  1.00 30.66 ? 374  THR B OG1   1 
ATOM   2780 C CG2   . THR A 1 376 ? 21.877 -25.450 -4.979  1.00 35.03 ? 374  THR B CG2   1 
ATOM   2781 N N     . ALA A 1 377 ? 21.614 -21.572 -4.352  1.00 32.66 ? 375  ALA B N     1 
ATOM   2782 C CA    . ALA A 1 377 ? 22.372 -20.624 -3.510  1.00 31.65 ? 375  ALA B CA    1 
ATOM   2783 C C     . ALA A 1 377 ? 21.466 -20.080 -2.401  1.00 32.71 ? 375  ALA B C     1 
ATOM   2784 O O     . ALA A 1 377 ? 21.937 -19.963 -1.259  1.00 33.52 ? 375  ALA B O     1 
ATOM   2785 C CB    . ALA A 1 377 ? 22.952 -19.498 -4.337  1.00 32.67 ? 375  ALA B CB    1 
ATOM   2786 N N     . LYS A 1 378 ? 20.211 -19.771 -2.713  1.00 31.25 ? 376  LYS B N     1 
ATOM   2787 C CA    . LYS A 1 378 ? 19.280 -19.143 -1.748  1.00 34.45 ? 376  LYS B CA    1 
ATOM   2788 C C     . LYS A 1 378 ? 18.732 -20.190 -0.773  1.00 34.72 ? 376  LYS B C     1 
ATOM   2789 O O     . LYS A 1 378 ? 18.648 -19.876 0.422   1.00 32.51 ? 376  LYS B O     1 
ATOM   2790 C CB    . LYS A 1 378 ? 18.129 -18.454 -2.479  1.00 34.98 ? 376  LYS B CB    1 
ATOM   2791 C CG    . LYS A 1 378 ? 17.164 -17.695 -1.587  1.00 34.85 ? 376  LYS B CG    1 
ATOM   2792 C CD    . LYS A 1 378 ? 16.212 -16.857 -2.395  1.00 39.04 ? 376  LYS B CD    1 
ATOM   2793 C CE    . LYS A 1 378 ? 15.079 -16.309 -1.563  1.00 42.43 ? 376  LYS B CE    1 
ATOM   2794 N NZ    . LYS A 1 378 ? 15.543 -15.160 -0.759  1.00 45.65 ? 376  LYS B NZ    1 
ATOM   2795 N N     . TYR A 1 379 ? 18.337 -21.372 -1.239  1.00 32.22 ? 377  TYR B N     1 
ATOM   2796 C CA    . TYR A 1 379 ? 17.361 -22.224 -0.505  1.00 34.01 ? 377  TYR B CA    1 
ATOM   2797 C C     . TYR A 1 379 ? 18.002 -23.493 0.064   1.00 35.63 ? 377  TYR B C     1 
ATOM   2798 O O     . TYR A 1 379 ? 17.388 -24.085 0.952   1.00 35.44 ? 377  TYR B O     1 
ATOM   2799 C CB    . TYR A 1 379 ? 16.171 -22.593 -1.399  1.00 33.64 ? 377  TYR B CB    1 
ATOM   2800 C CG    . TYR A 1 379 ? 15.241 -21.452 -1.729  1.00 34.68 ? 377  TYR B CG    1 
ATOM   2801 C CD1   . TYR A 1 379 ? 14.496 -20.819 -0.746  1.00 36.25 ? 377  TYR B CD1   1 
ATOM   2802 C CD2   . TYR A 1 379 ? 15.095 -21.002 -3.036  1.00 36.18 ? 377  TYR B CD2   1 
ATOM   2803 C CE1   . TYR A 1 379 ? 13.641 -19.766 -1.044  1.00 36.98 ? 377  TYR B CE1   1 
ATOM   2804 C CE2   . TYR A 1 379 ? 14.247 -19.948 -3.352  1.00 38.84 ? 377  TYR B CE2   1 
ATOM   2805 C CZ    . TYR A 1 379 ? 13.511 -19.329 -2.352  1.00 41.06 ? 377  TYR B CZ    1 
ATOM   2806 O OH    . TYR A 1 379 ? 12.664 -18.299 -2.664  1.00 43.62 ? 377  TYR B OH    1 
ATOM   2807 N N     . SER A 1 380 ? 19.159 -23.931 -0.432  1.00 36.58 ? 378  SER B N     1 
ATOM   2808 C CA    . SER A 1 380 ? 19.766 -25.226 -0.020  1.00 36.95 ? 378  SER B CA    1 
ATOM   2809 C C     . SER A 1 380 ? 20.090 -25.184 1.481   1.00 39.62 ? 378  SER B C     1 
ATOM   2810 O O     . SER A 1 380 ? 20.551 -24.117 1.953   1.00 33.20 ? 378  SER B O     1 
ATOM   2811 C CB    . SER A 1 380 ? 20.980 -25.536 -0.844  1.00 38.28 ? 378  SER B CB    1 
ATOM   2812 O OG    . SER A 1 380 ? 21.652 -26.683 -0.355  1.00 38.64 ? 378  SER B OG    1 
ATOM   2813 N N     . GLU A 1 381 ? 19.850 -26.290 2.197   1.00 42.98 ? 379  GLU B N     1 
ATOM   2814 C CA    . GLU A 1 381 ? 20.214 -26.435 3.636   1.00 51.56 ? 379  GLU B CA    1 
ATOM   2815 C C     . GLU A 1 381 ? 21.690 -26.827 3.762   1.00 48.70 ? 379  GLU B C     1 
ATOM   2816 O O     . GLU A 1 381 ? 22.244 -26.683 4.856   1.00 51.42 ? 379  GLU B O     1 
ATOM   2817 C CB    . GLU A 1 381 ? 19.334 -27.466 4.348   1.00 55.72 ? 379  GLU B CB    1 
ATOM   2818 C CG    . GLU A 1 381 ? 18.512 -26.868 5.478   1.00 61.75 ? 379  GLU B CG    1 
ATOM   2819 C CD    . GLU A 1 381 ? 17.065 -26.578 5.124   1.00 71.36 ? 379  GLU B CD    1 
ATOM   2820 O OE1   . GLU A 1 381 ? 16.384 -27.524 4.691   1.00 73.58 ? 379  GLU B OE1   1 
ATOM   2821 O OE2   . GLU A 1 381 ? 16.621 -25.415 5.283   1.00 70.60 ? 379  GLU B OE2   1 
ATOM   2822 N N     . ASP A 1 382 ? 22.286 -27.308 2.678   1.00 50.20 ? 380  ASP B N     1 
ATOM   2823 C CA    . ASP A 1 382 ? 23.673 -27.837 2.629   1.00 56.76 ? 380  ASP B CA    1 
ATOM   2824 C C     . ASP A 1 382 ? 24.625 -26.680 2.261   1.00 52.97 ? 380  ASP B C     1 
ATOM   2825 O O     . ASP A 1 382 ? 24.517 -26.160 1.127   1.00 46.08 ? 380  ASP B O     1 
ATOM   2826 C CB    . ASP A 1 382 ? 23.697 -29.034 1.674   1.00 58.97 ? 380  ASP B CB    1 
ATOM   2827 C CG    . ASP A 1 382 ? 25.073 -29.585 1.354   1.00 69.16 ? 380  ASP B CG    1 
ATOM   2828 O OD1   . ASP A 1 382 ? 25.984 -29.486 2.214   1.00 85.23 ? 380  ASP B OD1   1 
ATOM   2829 O OD2   . ASP A 1 382 ? 25.224 -30.115 0.243   1.00 72.05 ? 380  ASP B OD2   1 
ATOM   2830 N N     . ALA A 1 383 ? 25.523 -26.289 3.176   1.00 45.50 ? 381  ALA B N     1 
ATOM   2831 C CA    . ALA A 1 383 ? 26.510 -25.197 2.978   1.00 43.81 ? 381  ALA B CA    1 
ATOM   2832 C C     . ALA A 1 383 ? 27.421 -25.504 1.785   1.00 41.85 ? 381  ALA B C     1 
ATOM   2833 O O     . ALA A 1 383 ? 27.675 -24.594 1.022   1.00 42.89 ? 381  ALA B O     1 
ATOM   2834 C CB    . ALA A 1 383 ? 27.299 -24.958 4.237   1.00 45.86 ? 381  ALA B CB    1 
ATOM   2835 N N     . VAL A 1 384 ? 27.866 -26.745 1.603   1.00 42.39 ? 382  VAL B N     1 
ATOM   2836 C CA    . VAL A 1 384 ? 28.722 -27.155 0.447   1.00 43.04 ? 382  VAL B CA    1 
ATOM   2837 C C     . VAL A 1 384 ? 27.971 -26.842 -0.858  1.00 40.95 ? 382  VAL B C     1 
ATOM   2838 O O     . VAL A 1 384 ? 28.554 -26.200 -1.756  1.00 37.42 ? 382  VAL B O     1 
ATOM   2839 C CB    . VAL A 1 384 ? 29.072 -28.653 0.531   1.00 45.46 ? 382  VAL B CB    1 
ATOM   2840 C CG1   . VAL A 1 384 ? 29.680 -29.190 -0.762  1.00 46.76 ? 382  VAL B CG1   1 
ATOM   2841 C CG2   . VAL A 1 384 ? 29.970 -28.940 1.706   1.00 42.92 ? 382  VAL B CG2   1 
ATOM   2842 N N     . THR A 1 385 ? 26.733 -27.324 -0.964  1.00 37.24 ? 383  THR B N     1 
ATOM   2843 C CA    . THR A 1 385 ? 25.824 -27.086 -2.113  1.00 38.20 ? 383  THR B CA    1 
ATOM   2844 C C     . THR A 1 385 ? 25.622 -25.580 -2.310  1.00 33.32 ? 383  THR B C     1 
ATOM   2845 O O     . THR A 1 385 ? 25.858 -25.104 -3.446  1.00 34.86 ? 383  THR B O     1 
ATOM   2846 C CB    . THR A 1 385 ? 24.507 -27.840 -1.905  1.00 42.56 ? 383  THR B CB    1 
ATOM   2847 O OG1   . THR A 1 385 ? 24.865 -29.220 -1.961  1.00 44.21 ? 383  THR B OG1   1 
ATOM   2848 C CG2   . THR A 1 385 ? 23.454 -27.521 -2.941  1.00 42.53 ? 383  THR B CG2   1 
ATOM   2849 N N     . ARG A 1 386 ? 25.221 -24.863 -1.261  1.00 32.10 ? 384  ARG B N     1 
ATOM   2850 C CA    . ARG A 1 386 ? 24.972 -23.398 -1.332  1.00 35.42 ? 384  ARG B CA    1 
ATOM   2851 C C     . ARG A 1 386 ? 26.229 -22.724 -1.878  1.00 34.80 ? 384  ARG B C     1 
ATOM   2852 O O     . ARG A 1 386 ? 26.088 -21.925 -2.820  1.00 33.13 ? 384  ARG B O     1 
ATOM   2853 C CB    . ARG A 1 386 ? 24.621 -22.755 0.011   1.00 38.63 ? 384  ARG B CB    1 
ATOM   2854 C CG    . ARG A 1 386 ? 23.149 -22.848 0.399   1.00 46.48 ? 384  ARG B CG    1 
ATOM   2855 C CD    . ARG A 1 386 ? 22.745 -21.796 1.429   1.00 47.53 ? 384  ARG B CD    1 
ATOM   2856 N NE    . ARG A 1 386 ? 23.663 -21.771 2.567   1.00 50.66 ? 384  ARG B NE    1 
ATOM   2857 C CZ    . ARG A 1 386 ? 23.638 -22.622 3.595   1.00 51.40 ? 384  ARG B CZ    1 
ATOM   2858 N NH1   . ARG A 1 386 ? 22.723 -23.575 3.679   1.00 49.27 ? 384  ARG B NH1   1 
ATOM   2859 N NH2   . ARG A 1 386 ? 24.534 -22.504 4.554   1.00 53.68 ? 384  ARG B NH2   1 
ATOM   2860 N N     . LYS A 1 387 ? 27.396 -23.008 -1.287  1.00 31.74 ? 385  LYS B N     1 
ATOM   2861 C CA    . LYS A 1 387 ? 28.667 -22.329 -1.654  1.00 35.64 ? 385  LYS B CA    1 
ATOM   2862 C C     . LYS A 1 387 ? 28.976 -22.576 -3.139  1.00 32.53 ? 385  LYS B C     1 
ATOM   2863 O O     . LYS A 1 387 ? 29.377 -21.626 -3.819  1.00 31.27 ? 385  LYS B O     1 
ATOM   2864 C CB    . LYS A 1 387 ? 29.843 -22.834 -0.812  1.00 36.46 ? 385  LYS B CB    1 
ATOM   2865 C CG    . LYS A 1 387 ? 29.884 -22.301 0.611   1.00 44.69 ? 385  LYS B CG    1 
ATOM   2866 C CD    . LYS A 1 387 ? 29.781 -20.794 0.731   1.00 47.84 ? 385  LYS B CD    1 
ATOM   2867 C CE    . LYS A 1 387 ? 30.721 -20.038 -0.184  1.00 55.52 ? 385  LYS B CE    1 
ATOM   2868 N NZ    . LYS A 1 387 ? 31.141 -18.760 0.443   1.00 58.03 ? 385  LYS B NZ    1 
ATOM   2869 N N     . ARG A 1 388 ? 28.878 -23.821 -3.599  1.00 30.78 ? 386  ARG B N     1 
ATOM   2870 C CA    . ARG A 1 388 ? 29.177 -24.157 -5.009  1.00 35.71 ? 386  ARG B CA    1 
ATOM   2871 C C     . ARG A 1 388 ? 28.200 -23.404 -5.915  1.00 34.64 ? 386  ARG B C     1 
ATOM   2872 O O     . ARG A 1 388 ? 28.666 -22.842 -6.937  1.00 34.16 ? 386  ARG B O     1 
ATOM   2873 C CB    . ARG A 1 388 ? 29.130 -25.657 -5.290  1.00 39.28 ? 386  ARG B CB    1 
ATOM   2874 C CG    . ARG A 1 388 ? 29.636 -25.982 -6.692  1.00 44.18 ? 386  ARG B CG    1 
ATOM   2875 C CD    . ARG A 1 388 ? 29.656 -27.464 -6.982  1.00 46.08 ? 386  ARG B CD    1 
ATOM   2876 N NE    . ARG A 1 388 ? 29.698 -27.735 -8.417  1.00 52.21 ? 386  ARG B NE    1 
ATOM   2877 C CZ    . ARG A 1 388 ? 28.629 -27.762 -9.218  1.00 56.95 ? 386  ARG B CZ    1 
ATOM   2878 N NH1   . ARG A 1 388 ? 28.776 -28.051 -10.504 1.00 58.85 ? 386  ARG B NH1   1 
ATOM   2879 N NH2   . ARG A 1 388 ? 27.420 -27.498 -8.738  1.00 52.23 ? 386  ARG B NH2   1 
ATOM   2880 N N     . ALA A 1 389 ? 26.910 -23.375 -5.561  1.00 31.23 ? 387  ALA B N     1 
ATOM   2881 C CA    . ALA A 1 389 ? 25.889 -22.651 -6.343  1.00 30.70 ? 387  ALA B CA    1 
ATOM   2882 C C     . ALA A 1 389 ? 26.287 -21.172 -6.406  1.00 29.71 ? 387  ALA B C     1 
ATOM   2883 O O     . ALA A 1 389 ? 26.192 -20.579 -7.488  1.00 27.75 ? 387  ALA B O     1 
ATOM   2884 C CB    . ALA A 1 389 ? 24.513 -22.846 -5.771  1.00 29.76 ? 387  ALA B CB    1 
ATOM   2885 N N     . GLU A 1 390 ? 26.769 -20.592 -5.312  1.00 27.98 ? 388  GLU B N     1 
ATOM   2886 C CA    . GLU A 1 390 ? 27.117 -19.143 -5.309  1.00 32.50 ? 388  GLU B CA    1 
ATOM   2887 C C     . GLU A 1 390 ? 28.282 -18.903 -6.276  1.00 29.18 ? 388  GLU B C     1 
ATOM   2888 O O     . GLU A 1 390 ? 28.360 -17.816 -6.870  1.00 28.55 ? 388  GLU B O     1 
ATOM   2889 C CB    . GLU A 1 390 ? 27.524 -18.645 -3.925  1.00 34.59 ? 388  GLU B CB    1 
ATOM   2890 C CG    . GLU A 1 390 ? 26.384 -18.599 -2.938  1.00 41.73 ? 388  GLU B CG    1 
ATOM   2891 C CD    . GLU A 1 390 ? 26.825 -18.231 -1.527  1.00 54.34 ? 388  GLU B CD    1 
ATOM   2892 O OE1   . GLU A 1 390 ? 26.027 -17.584 -0.818  1.00 69.09 ? 388  GLU B OE1   1 
ATOM   2893 O OE2   . GLU A 1 390 ? 27.965 -18.585 -1.136  1.00 56.00 ? 388  GLU B OE2   1 
ATOM   2894 N N     . GLU A 1 391 ? 29.193 -19.858 -6.344  1.00 29.16 ? 389  GLU B N     1 
ATOM   2895 C CA    . GLU A 1 391 ? 30.419 -19.761 -7.172  1.00 29.43 ? 389  GLU B CA    1 
ATOM   2896 C C     . GLU A 1 391 ? 30.003 -19.810 -8.657  1.00 29.94 ? 389  GLU B C     1 
ATOM   2897 O O     . GLU A 1 391 ? 30.578 -19.051 -9.460  1.00 28.41 ? 389  GLU B O     1 
ATOM   2898 C CB    . GLU A 1 391 ? 31.396 -20.861 -6.754  1.00 32.21 ? 389  GLU B CB    1 
ATOM   2899 C CG    . GLU A 1 391 ? 32.016 -20.604 -5.378  1.00 31.14 ? 389  GLU B CG    1 
ATOM   2900 C CD    . GLU A 1 391 ? 32.560 -21.830 -4.656  1.00 36.37 ? 389  GLU B CD    1 
ATOM   2901 O OE1   . GLU A 1 391 ? 32.783 -22.859 -5.328  1.00 39.26 ? 389  GLU B OE1   1 
ATOM   2902 O OE2   . GLU A 1 391 ? 32.760 -21.754 -3.397  1.00 37.96 ? 389  GLU B OE2   1 
ATOM   2903 N N     . LEU A 1 392 ? 29.052 -20.679 -9.003  1.00 29.35 ? 390  LEU B N     1 
ATOM   2904 C CA    . LEU A 1 392 ? 28.532 -20.812 -10.390 1.00 30.11 ? 390  LEU B CA    1 
ATOM   2905 C C     . LEU A 1 392 ? 27.693 -19.576 -10.736 1.00 32.05 ? 390  LEU B C     1 
ATOM   2906 O O     . LEU A 1 392 ? 27.788 -19.110 -11.883 1.00 27.23 ? 390  LEU B O     1 
ATOM   2907 C CB    . LEU A 1 392 ? 27.718 -22.093 -10.526 1.00 29.36 ? 390  LEU B CB    1 
ATOM   2908 C CG    . LEU A 1 392 ? 28.530 -23.377 -10.473 1.00 29.86 ? 390  LEU B CG    1 
ATOM   2909 C CD1   . LEU A 1 392 ? 27.620 -24.567 -10.683 1.00 30.43 ? 390  LEU B CD1   1 
ATOM   2910 C CD2   . LEU A 1 392 ? 29.672 -23.357 -11.477 1.00 30.28 ? 390  LEU B CD2   1 
ATOM   2911 N N     . VAL A 1 393 ? 26.916 -19.049 -9.788  1.00 30.06 ? 391  VAL B N     1 
ATOM   2912 C CA    . VAL A 1 393 ? 26.201 -17.761 -9.982  1.00 28.72 ? 391  VAL B CA    1 
ATOM   2913 C C     . VAL A 1 393 ? 27.233 -16.682 -10.348 1.00 30.67 ? 391  VAL B C     1 
ATOM   2914 O O     . VAL A 1 393 ? 27.015 -15.921 -11.327 1.00 29.60 ? 391  VAL B O     1 
ATOM   2915 C CB    . VAL A 1 393 ? 25.382 -17.383 -8.735  1.00 31.65 ? 391  VAL B CB    1 
ATOM   2916 C CG1   . VAL A 1 393 ? 24.883 -15.942 -8.820  1.00 32.00 ? 391  VAL B CG1   1 
ATOM   2917 C CG2   . VAL A 1 393 ? 24.216 -18.347 -8.538  1.00 32.50 ? 391  VAL B CG2   1 
ATOM   2918 N N     . ALA A 1 394 ? 28.321 -16.584 -9.589  1.00 27.74 ? 392  ALA B N     1 
ATOM   2919 C CA    . ALA A 1 394 ? 29.377 -15.571 -9.810  1.00 28.38 ? 392  ALA B CA    1 
ATOM   2920 C C     . ALA A 1 394 ? 29.969 -15.749 -11.214 1.00 24.21 ? 392  ALA B C     1 
ATOM   2921 O O     . ALA A 1 394 ? 30.129 -14.780 -11.925 1.00 25.87 ? 392  ALA B O     1 
ATOM   2922 C CB    . ALA A 1 394 ? 30.419 -15.685 -8.721  1.00 31.60 ? 392  ALA B CB    1 
ATOM   2923 N N     . LEU A 1 395 ? 30.246 -16.974 -11.607 1.00 25.12 ? 393  LEU B N     1 
ATOM   2924 C CA    . LEU A 1 395 ? 30.861 -17.306 -12.913 1.00 25.65 ? 393  LEU B CA    1 
ATOM   2925 C C     . LEU A 1 395 ? 29.855 -17.036 -14.032 1.00 25.58 ? 393  LEU B C     1 
ATOM   2926 O O     . LEU A 1 395 ? 30.244 -16.398 -15.031 1.00 28.35 ? 393  LEU B O     1 
ATOM   2927 C CB    . LEU A 1 395 ? 31.263 -18.783 -12.890 1.00 24.57 ? 393  LEU B CB    1 
ATOM   2928 C CG    . LEU A 1 395 ? 31.851 -19.327 -14.188 1.00 25.94 ? 393  LEU B CG    1 
ATOM   2929 C CD1   . LEU A 1 395 ? 33.191 -18.690 -14.525 1.00 26.93 ? 393  LEU B CD1   1 
ATOM   2930 C CD2   . LEU A 1 395 ? 32.002 -20.836 -14.097 1.00 25.52 ? 393  LEU B CD2   1 
ATOM   2931 N N     . LEU A 1 396 ? 28.627 -17.538 -13.899 1.00 24.48 ? 394  LEU B N     1 
ATOM   2932 C CA    . LEU A 1 396 ? 27.696 -17.692 -15.061 1.00 25.41 ? 394  LEU B CA    1 
ATOM   2933 C C     . LEU A 1 396 ? 26.808 -16.469 -15.273 1.00 26.40 ? 394  LEU B C     1 
ATOM   2934 O O     . LEU A 1 396 ? 26.341 -16.281 -16.428 1.00 26.17 ? 394  LEU B O     1 
ATOM   2935 C CB    . LEU A 1 396 ? 26.856 -18.951 -14.882 1.00 23.85 ? 394  LEU B CB    1 
ATOM   2936 C CG    . LEU A 1 396 ? 27.648 -20.255 -14.824 1.00 23.52 ? 394  LEU B CG    1 
ATOM   2937 C CD1   . LEU A 1 396 ? 26.686 -21.415 -14.625 1.00 26.40 ? 394  LEU B CD1   1 
ATOM   2938 C CD2   . LEU A 1 396 ? 28.471 -20.473 -16.097 1.00 25.21 ? 394  LEU B CD2   1 
ATOM   2939 N N     . THR A 1 397 ? 26.572 -15.632 -14.268 1.00 25.23 ? 395  THR B N     1 
ATOM   2940 C CA    . THR A 1 397 ? 25.670 -14.470 -14.468 1.00 26.98 ? 395  THR B CA    1 
ATOM   2941 C C     . THR A 1 397 ? 26.259 -13.494 -15.502 1.00 25.61 ? 395  THR B C     1 
ATOM   2942 O O     . THR A 1 397 ? 25.498 -12.980 -16.325 1.00 25.49 ? 395  THR B O     1 
ATOM   2943 C CB    . THR A 1 397 ? 25.190 -13.816 -13.164 1.00 27.18 ? 395  THR B CB    1 
ATOM   2944 O OG1   . THR A 1 397 ? 26.287 -13.454 -12.345 1.00 29.84 ? 395  THR B OG1   1 
ATOM   2945 C CG2   . THR A 1 397 ? 24.269 -14.712 -12.373 1.00 28.31 ? 395  THR B CG2   1 
ATOM   2946 N N     . PRO A 1 398 ? 27.575 -13.149 -15.529 1.00 27.51 ? 396  PRO B N     1 
ATOM   2947 C CA    . PRO A 1 398 ? 28.100 -12.297 -16.606 1.00 25.35 ? 396  PRO B CA    1 
ATOM   2948 C C     . PRO A 1 398 ? 27.960 -12.938 -17.996 1.00 23.31 ? 396  PRO B C     1 
ATOM   2949 O O     . PRO A 1 398 ? 27.720 -12.224 -18.936 1.00 23.27 ? 396  PRO B O     1 
ATOM   2950 C CB    . PRO A 1 398 ? 29.574 -12.043 -16.273 1.00 26.80 ? 396  PRO B CB    1 
ATOM   2951 C CG    . PRO A 1 398 ? 29.889 -12.991 -15.129 1.00 28.18 ? 396  PRO B CG    1 
ATOM   2952 C CD    . PRO A 1 398 ? 28.594 -13.428 -14.507 1.00 26.64 ? 396  PRO B CD    1 
ATOM   2953 N N     . VAL A 1 399 ? 28.070 -14.264 -18.091 1.00 22.99 ? 397  VAL B N     1 
ATOM   2954 C CA    . VAL A 1 399 ? 27.891 -15.000 -19.361 1.00 23.52 ? 397  VAL B CA    1 
ATOM   2955 C C     . VAL A 1 399 ? 26.421 -14.848 -19.770 1.00 27.30 ? 397  VAL B C     1 
ATOM   2956 O O     . VAL A 1 399 ? 26.156 -14.473 -20.924 1.00 23.75 ? 397  VAL B O     1 
ATOM   2957 C CB    . VAL A 1 399 ? 28.299 -16.476 -19.229 1.00 27.01 ? 397  VAL B CB    1 
ATOM   2958 C CG1   . VAL A 1 399 ? 28.110 -17.211 -20.550 1.00 26.89 ? 397  VAL B CG1   1 
ATOM   2959 C CG2   . VAL A 1 399 ? 29.736 -16.627 -18.723 1.00 26.65 ? 397  VAL B CG2   1 
ATOM   2960 N N     . ALA A 1 400 ? 25.493 -15.067 -18.841 1.00 24.38 ? 398  ALA B N     1 
ATOM   2961 C CA    . ALA A 1 400 ? 24.048 -14.929 -19.099 1.00 24.90 ? 398  ALA B CA    1 
ATOM   2962 C C     . ALA A 1 400 ? 23.772 -13.528 -19.625 1.00 23.78 ? 398  ALA B C     1 
ATOM   2963 O O     . ALA A 1 400 ? 23.053 -13.396 -20.635 1.00 25.81 ? 398  ALA B O     1 
ATOM   2964 C CB    . ALA A 1 400 ? 23.224 -15.196 -17.859 1.00 26.00 ? 398  ALA B CB    1 
ATOM   2965 N N     . LYS A 1 401 ? 24.331 -12.509 -18.996 1.00 22.41 ? 399  LYS B N     1 
ATOM   2966 C CA    . LYS A 1 401 ? 24.015 -11.107 -19.372 1.00 22.35 ? 399  LYS B CA    1 
ATOM   2967 C C     . LYS A 1 401 ? 24.490 -10.858 -20.811 1.00 23.65 ? 399  LYS B C     1 
ATOM   2968 O O     . LYS A 1 401 ? 23.655 -10.481 -21.648 1.00 25.09 ? 399  LYS B O     1 
ATOM   2969 C CB    . LYS A 1 401 ? 24.677 -10.156 -18.374 1.00 24.18 ? 399  LYS B CB    1 
ATOM   2970 C CG    . LYS A 1 401 ? 24.111 -8.744  -18.340 1.00 23.80 ? 399  LYS B CG    1 
ATOM   2971 C CD    . LYS A 1 401 ? 24.239 -7.970  -19.614 1.00 23.60 ? 399  LYS B CD    1 
ATOM   2972 C CE    . LYS A 1 401 ? 24.206 -6.479  -19.362 1.00 23.02 ? 399  LYS B CE    1 
ATOM   2973 N NZ    . LYS A 1 401 ? 24.245 -5.702  -20.617 1.00 22.39 ? 399  LYS B NZ    1 
ATOM   2974 N N     . ALA A 1 402 ? 25.784 -11.044 -21.084 1.00 22.45 ? 400  ALA B N     1 
ATOM   2975 C CA    . ALA A 1 402 ? 26.403 -10.625 -22.355 1.00 22.53 ? 400  ALA B CA    1 
ATOM   2976 C C     . ALA A 1 402 ? 26.101 -11.636 -23.465 1.00 21.70 ? 400  ALA B C     1 
ATOM   2977 O O     . ALA A 1 402 ? 25.821 -11.205 -24.544 1.00 22.71 ? 400  ALA B O     1 
ATOM   2978 C CB    . ALA A 1 402 ? 27.886 -10.379 -22.173 1.00 21.18 ? 400  ALA B CB    1 
ATOM   2979 N N     . PHE A 1 403 ? 26.144 -12.936 -23.214 1.00 21.72 ? 401  PHE B N     1 
ATOM   2980 C CA    . PHE A 1 403 ? 25.917 -13.948 -24.274 1.00 21.69 ? 401  PHE B CA    1 
ATOM   2981 C C     . PHE A 1 403 ? 24.442 -13.956 -24.691 1.00 23.13 ? 401  PHE B C     1 
ATOM   2982 O O     . PHE A 1 403 ? 24.168 -13.943 -25.921 1.00 20.64 ? 401  PHE B O     1 
ATOM   2983 C CB    . PHE A 1 403 ? 26.349 -15.354 -23.866 1.00 21.13 ? 401  PHE B CB    1 
ATOM   2984 C CG    . PHE A 1 403 ? 26.622 -16.270 -25.025 1.00 21.77 ? 401  PHE B CG    1 
ATOM   2985 C CD1   . PHE A 1 403 ? 27.615 -15.962 -25.953 1.00 23.67 ? 401  PHE B CD1   1 
ATOM   2986 C CD2   . PHE A 1 403 ? 25.882 -17.429 -25.215 1.00 24.82 ? 401  PHE B CD2   1 
ATOM   2987 C CE1   . PHE A 1 403 ? 27.848 -16.783 -27.044 1.00 23.53 ? 401  PHE B CE1   1 
ATOM   2988 C CE2   . PHE A 1 403 ? 26.126 -18.251 -26.309 1.00 24.45 ? 401  PHE B CE2   1 
ATOM   2989 C CZ    . PHE A 1 403 ? 27.120 -17.936 -27.210 1.00 22.93 ? 401  PHE B CZ    1 
ATOM   2990 N N     . LEU A 1 404 ? 23.492 -13.978 -23.749 1.00 21.37 ? 402  LEU B N     1 
ATOM   2991 C CA    . LEU A 1 404 ? 22.073 -14.076 -24.176 1.00 21.37 ? 402  LEU B CA    1 
ATOM   2992 C C     . LEU A 1 404 ? 21.715 -12.809 -24.946 1.00 20.13 ? 402  LEU B C     1 
ATOM   2993 O O     . LEU A 1 404 ? 20.849 -12.883 -25.841 1.00 20.61 ? 402  LEU B O     1 
ATOM   2994 C CB    . LEU A 1 404 ? 21.130 -14.297 -22.985 1.00 22.87 ? 402  LEU B CB    1 
ATOM   2995 C CG    . LEU A 1 404 ? 20.781 -15.751 -22.666 1.00 26.56 ? 402  LEU B CG    1 
ATOM   2996 C CD1   . LEU A 1 404 ? 22.014 -16.558 -22.325 1.00 30.12 ? 402  LEU B CD1   1 
ATOM   2997 C CD2   . LEU A 1 404 ? 19.808 -15.815 -21.500 1.00 32.26 ? 402  LEU B CD2   1 
ATOM   2998 N N     . THR A 1 405 ? 22.308 -11.668 -24.598 1.00 19.61 ? 403  THR B N     1 
ATOM   2999 C CA    . THR A 1 405 ? 21.937 -10.399 -25.256 1.00 19.39 ? 403  THR B CA    1 
ATOM   3000 C C     . THR A 1 405 ? 22.644 -10.333 -26.625 1.00 20.77 ? 403  THR B C     1 
ATOM   3001 O O     . THR A 1 405 ? 21.998 -9.887  -27.602 1.00 21.47 ? 403  THR B O     1 
ATOM   3002 C CB    . THR A 1 405 ? 22.199 -9.196  -24.350 1.00 20.01 ? 403  THR B CB    1 
ATOM   3003 O OG1   . THR A 1 405 ? 23.559 -9.175  -23.925 1.00 20.59 ? 403  THR B OG1   1 
ATOM   3004 C CG2   . THR A 1 405 ? 21.296 -9.194  -23.135 1.00 22.10 ? 403  THR B CG2   1 
ATOM   3005 N N     . ASP A 1 406 ? 23.905 -10.763 -26.700 1.00 20.49 ? 404  ASP B N     1 
ATOM   3006 C CA    . ASP A 1 406 ? 24.650 -10.743 -27.989 1.00 21.20 ? 404  ASP B CA    1 
ATOM   3007 C C     . ASP A 1 406 ? 23.955 -11.707 -28.959 1.00 21.45 ? 404  ASP B C     1 
ATOM   3008 O O     . ASP A 1 406 ? 23.747 -11.318 -30.123 1.00 20.35 ? 404  ASP B O     1 
ATOM   3009 C CB    . ASP A 1 406 ? 26.130 -11.034 -27.794 1.00 21.33 ? 404  ASP B CB    1 
ATOM   3010 C CG    . ASP A 1 406 ? 26.975 -9.850  -27.326 1.00 21.72 ? 404  ASP B CG    1 
ATOM   3011 O OD1   . ASP A 1 406 ? 26.445 -8.746  -27.194 1.00 19.75 ? 404  ASP B OD1   1 
ATOM   3012 O OD2   . ASP A 1 406 ? 28.188 -10.058 -27.128 1.00 22.96 ? 404  ASP B OD2   1 
ATOM   3013 N N     . MET A 1 407 ? 23.589 -12.903 -28.489 1.00 20.94 ? 405  MET B N     1 
ATOM   3014 C CA    . MET A 1 407 ? 22.911 -13.924 -29.320 1.00 22.50 ? 405  MET B CA    1 
ATOM   3015 C C     . MET A 1 407 ? 21.487 -13.470 -29.640 1.00 23.20 ? 405  MET B C     1 
ATOM   3016 O O     . MET A 1 407 ? 21.000 -13.715 -30.773 1.00 21.11 ? 405  MET B O     1 
ATOM   3017 C CB    . MET A 1 407 ? 22.866 -15.275 -28.603 1.00 22.41 ? 405  MET B CB    1 
ATOM   3018 C CG    . MET A 1 407 ? 24.208 -15.926 -28.451 1.00 23.10 ? 405  MET B CG    1 
ATOM   3019 S SD    . MET A 1 407 ? 25.154 -16.173 -29.974 1.00 24.65 ? 405  MET B SD    1 
ATOM   3020 C CE    . MET A 1 407 ? 26.202 -14.718 -29.948 1.00 26.80 ? 405  MET B CE    1 
ATOM   3021 N N     . GLY A 1 408 ? 20.841 -12.794 -28.699 1.00 23.55 ? 406  GLY B N     1 
ATOM   3022 C CA    . GLY A 1 408 ? 19.541 -12.157 -28.930 1.00 21.67 ? 406  GLY B CA    1 
ATOM   3023 C C     . GLY A 1 408 ? 19.607 -11.208 -30.116 1.00 23.12 ? 406  GLY B C     1 
ATOM   3024 O O     . GLY A 1 408 ? 18.706 -11.266 -30.960 1.00 20.16 ? 406  GLY B O     1 
ATOM   3025 N N     . LEU A 1 409 ? 20.638 -10.356 -30.180 1.00 21.74 ? 407  LEU B N     1 
ATOM   3026 C CA    . LEU A 1 409 ? 20.763 -9.372  -31.270 1.00 23.68 ? 407  LEU B CA    1 
ATOM   3027 C C     . LEU A 1 409 ? 20.863 -10.128 -32.599 1.00 23.64 ? 407  LEU B C     1 
ATOM   3028 O O     . LEU A 1 409 ? 20.105 -9.803  -33.502 1.00 23.94 ? 407  LEU B O     1 
ATOM   3029 C CB    . LEU A 1 409 ? 21.984 -8.467  -31.103 1.00 23.95 ? 407  LEU B CB    1 
ATOM   3030 C CG    . LEU A 1 409 ? 22.133 -7.481  -32.257 1.00 25.20 ? 407  LEU B CG    1 
ATOM   3031 C CD1   . LEU A 1 409 ? 21.001 -6.490  -32.238 1.00 25.20 ? 407  LEU B CD1   1 
ATOM   3032 C CD2   . LEU A 1 409 ? 23.450 -6.755  -32.217 1.00 26.98 ? 407  LEU B CD2   1 
ATOM   3033 N N     . GLU A 1 410 ? 21.795 -11.063 -32.711 1.00 23.74 ? 408  GLU B N     1 
ATOM   3034 C CA    . GLU A 1 410 ? 21.966 -11.871 -33.936 1.00 24.02 ? 408  GLU B CA    1 
ATOM   3035 C C     . GLU A 1 410 ? 20.625 -12.497 -34.322 1.00 21.73 ? 408  GLU B C     1 
ATOM   3036 O O     . GLU A 1 410 ? 20.257 -12.482 -35.533 1.00 20.39 ? 408  GLU B O     1 
ATOM   3037 C CB    . GLU A 1 410 ? 23.002 -12.976 -33.752 1.00 24.33 ? 408  GLU B CB    1 
ATOM   3038 C CG    . GLU A 1 410 ? 23.195 -13.706 -35.066 1.00 26.85 ? 408  GLU B CG    1 
ATOM   3039 C CD    . GLU A 1 410 ? 24.198 -14.835 -35.134 1.00 27.75 ? 408  GLU B CD    1 
ATOM   3040 O OE1   . GLU A 1 410 ? 24.179 -15.575 -36.160 1.00 26.27 ? 408  GLU B OE1   1 
ATOM   3041 O OE2   . GLU A 1 410 ? 24.983 -14.960 -34.188 1.00 28.67 ? 408  GLU B OE2   1 
ATOM   3042 N N     . THR A 1 411 ? 19.933 -13.079 -33.346 1.00 21.29 ? 409  THR B N     1 
ATOM   3043 C CA    . THR A 1 411 ? 18.608 -13.732 -33.529 1.00 21.38 ? 409  THR B CA    1 
ATOM   3044 C C     . THR A 1 411 ? 17.622 -12.727 -34.144 1.00 21.95 ? 409  THR B C     1 
ATOM   3045 O O     . THR A 1 411 ? 16.957 -13.069 -35.128 1.00 21.61 ? 409  THR B O     1 
ATOM   3046 C CB    . THR A 1 411 ? 18.117 -14.313 -32.200 1.00 21.26 ? 409  THR B CB    1 
ATOM   3047 O OG1   . THR A 1 411 ? 19.032 -15.315 -31.746 1.00 19.75 ? 409  THR B OG1   1 
ATOM   3048 C CG2   . THR A 1 411 ? 16.733 -14.920 -32.304 1.00 20.97 ? 409  THR B CG2   1 
ATOM   3049 N N     . THR A 1 412 ? 17.501 -11.516 -33.592 1.00 21.66 ? 410  THR B N     1 
ATOM   3050 C CA    . THR A 1 412 ? 16.532 -10.517 -34.093 1.00 21.21 ? 410  THR B CA    1 
ATOM   3051 C C     . THR A 1 412 ? 16.931 -10.047 -35.500 1.00 22.02 ? 410  THR B C     1 
ATOM   3052 O O     . THR A 1 412 ? 16.023 -9.776  -36.314 1.00 18.67 ? 410  THR B O     1 
ATOM   3053 C CB    . THR A 1 412 ? 16.368 -9.323  -33.146 1.00 22.13 ? 410  THR B CB    1 
ATOM   3054 O OG1   . THR A 1 412 ? 17.591 -8.584  -33.038 1.00 21.23 ? 410  THR B OG1   1 
ATOM   3055 C CG2   . THR A 1 412 ? 15.843 -9.740  -31.789 1.00 23.56 ? 410  THR B CG2   1 
ATOM   3056 N N     . ILE A 1 413 ? 18.232 -9.944  -35.777 1.00 20.93 ? 411  ILE B N     1 
ATOM   3057 C CA    . ILE A 1 413 ? 18.746 -9.586  -37.128 1.00 21.89 ? 411  ILE B CA    1 
ATOM   3058 C C     . ILE A 1 413 ? 18.310 -10.660 -38.140 1.00 20.34 ? 411  ILE B C     1 
ATOM   3059 O O     . ILE A 1 413 ? 17.715 -10.305 -39.177 1.00 21.11 ? 411  ILE B O     1 
ATOM   3060 C CB    . ILE A 1 413 ? 20.272 -9.412  -37.072 1.00 22.12 ? 411  ILE B CB    1 
ATOM   3061 C CG1   . ILE A 1 413 ? 20.620 -8.113  -36.345 1.00 23.33 ? 411  ILE B CG1   1 
ATOM   3062 C CG2   . ILE A 1 413 ? 20.861 -9.471  -38.484 1.00 22.87 ? 411  ILE B CG2   1 
ATOM   3063 C CD1   . ILE A 1 413 ? 22.044 -8.071  -35.863 1.00 25.21 ? 411  ILE B CD1   1 
ATOM   3064 N N     . HIS A 1 414 ? 18.565 -11.933 -37.845 1.00 20.25 ? 412  HIS B N     1 
ATOM   3065 C CA    . HIS A 1 414 ? 18.065 -13.055 -38.675 1.00 21.87 ? 412  HIS B CA    1 
ATOM   3066 C C     . HIS A 1 414 ? 16.555 -12.943 -38.860 1.00 23.48 ? 412  HIS B C     1 
ATOM   3067 O O     . HIS A 1 414 ? 16.087 -13.091 -39.995 1.00 20.73 ? 412  HIS B O     1 
ATOM   3068 C CB    . HIS A 1 414 ? 18.440 -14.420 -38.109 1.00 21.30 ? 412  HIS B CB    1 
ATOM   3069 C CG    . HIS A 1 414 ? 19.905 -14.702 -38.172 1.00 24.49 ? 412  HIS B CG    1 
ATOM   3070 N ND1   . HIS A 1 414 ? 20.667 -14.408 -39.269 1.00 26.16 ? 412  HIS B ND1   1 
ATOM   3071 C CD2   . HIS A 1 414 ? 20.740 -15.246 -37.259 1.00 24.13 ? 412  HIS B CD2   1 
ATOM   3072 C CE1   . HIS A 1 414 ? 21.914 -14.769 -39.046 1.00 24.81 ? 412  HIS B CE1   1 
ATOM   3073 N NE2   . HIS A 1 414 ? 21.987 -15.277 -37.817 1.00 24.79 ? 412  HIS B NE2   1 
ATOM   3074 N N     . GLY A 1 415 ? 15.804 -12.681 -37.792 1.00 22.79 ? 413  GLY B N     1 
ATOM   3075 C CA    . GLY A 1 415 ? 14.328 -12.633 -37.867 1.00 22.58 ? 413  GLY B CA    1 
ATOM   3076 C C     . GLY A 1 415 ? 13.836 -11.568 -38.810 1.00 20.78 ? 413  GLY B C     1 
ATOM   3077 O O     . GLY A 1 415 ? 12.834 -11.801 -39.509 1.00 23.03 ? 413  GLY B O     1 
ATOM   3078 N N     . GLN A 1 416 ? 14.508 -10.418 -38.828 1.00 19.97 ? 414  GLN B N     1 
ATOM   3079 C CA    . GLN A 1 416 ? 14.214 -9.320  -39.773 1.00 20.72 ? 414  GLN B CA    1 
ATOM   3080 C C     . GLN A 1 416 ? 14.661 -9.731  -41.190 1.00 20.67 ? 414  GLN B C     1 
ATOM   3081 O O     . GLN A 1 416 ? 13.869 -9.583  -42.155 1.00 20.13 ? 414  GLN B O     1 
ATOM   3082 C CB    . GLN A 1 416 ? 14.906 -8.047  -39.309 1.00 20.76 ? 414  GLN B CB    1 
ATOM   3083 C CG    . GLN A 1 416 ? 14.691 -6.902  -40.264 1.00 21.26 ? 414  GLN B CG    1 
ATOM   3084 C CD    . GLN A 1 416 ? 15.337 -5.603  -39.853 1.00 20.39 ? 414  GLN B CD    1 
ATOM   3085 O OE1   . GLN A 1 416 ? 14.844 -4.519  -40.142 1.00 26.26 ? 414  GLN B OE1   1 
ATOM   3086 N NE2   . GLN A 1 416 ? 16.489 -5.683  -39.249 1.00 20.67 ? 414  GLN B NE2   1 
ATOM   3087 N N     . GLN A 1 417 ? 15.881 -10.248 -41.327 1.00 22.58 ? 415  GLN B N     1 
ATOM   3088 C CA    . GLN A 1 417 ? 16.480 -10.563 -42.656 1.00 21.42 ? 415  GLN B CA    1 
ATOM   3089 C C     . GLN A 1 417 ? 15.638 -11.618 -43.402 1.00 22.89 ? 415  GLN B C     1 
ATOM   3090 O O     . GLN A 1 417 ? 15.494 -11.522 -44.641 1.00 20.51 ? 415  GLN B O     1 
ATOM   3091 C CB    . GLN A 1 417 ? 17.923 -11.012 -42.477 1.00 22.12 ? 415  GLN B CB    1 
ATOM   3092 C CG    . GLN A 1 417 ? 18.701 -10.975 -43.769 1.00 21.40 ? 415  GLN B CG    1 
ATOM   3093 C CD    . GLN A 1 417 ? 18.906 -9.578  -44.315 1.00 22.83 ? 415  GLN B CD    1 
ATOM   3094 O OE1   . GLN A 1 417 ? 18.685 -8.551  -43.651 1.00 21.09 ? 415  GLN B OE1   1 
ATOM   3095 N NE2   . GLN A 1 417 ? 19.355 -9.543  -45.565 1.00 23.50 ? 415  GLN B NE2   1 
ATOM   3096 N N     . ILE A 1 418 ? 15.032 -12.555 -42.674 1.00 23.99 ? 416  ILE B N     1 
ATOM   3097 C CA    . ILE A 1 418 ? 14.169 -13.615 -43.263 1.00 23.46 ? 416  ILE B CA    1 
ATOM   3098 C C     . ILE A 1 418 ? 13.058 -12.968 -44.082 1.00 23.89 ? 416  ILE B C     1 
ATOM   3099 O O     . ILE A 1 418 ? 12.730 -13.496 -45.158 1.00 22.83 ? 416  ILE B O     1 
ATOM   3100 C CB    . ILE A 1 418 ? 13.624 -14.539 -42.164 1.00 23.14 ? 416  ILE B CB    1 
ATOM   3101 C CG1   . ILE A 1 418 ? 14.721 -15.505 -41.732 1.00 22.41 ? 416  ILE B CG1   1 
ATOM   3102 C CG2   . ILE A 1 418 ? 12.356 -15.256 -42.622 1.00 23.07 ? 416  ILE B CG2   1 
ATOM   3103 C CD1   . ILE A 1 418 ? 14.497 -16.149 -40.374 1.00 23.15 ? 416  ILE B CD1   1 
ATOM   3104 N N     . PHE A 1 419 ? 12.514 -11.847 -43.628 1.00 23.22 ? 417  PHE B N     1 
ATOM   3105 C CA    . PHE A 1 419 ? 11.403 -11.169 -44.326 1.00 22.53 ? 417  PHE B CA    1 
ATOM   3106 C C     . PHE A 1 419 ? 11.892 -10.467 -45.604 1.00 21.97 ? 417  PHE B C     1 
ATOM   3107 O O     . PHE A 1 419 ? 11.067 -9.924  -46.298 1.00 25.35 ? 417  PHE B O     1 
ATOM   3108 C CB    . PHE A 1 419 ? 10.750 -10.135 -43.414 1.00 24.58 ? 417  PHE B CB    1 
ATOM   3109 C CG    . PHE A 1 419 ? 9.799  -10.662 -42.366 1.00 23.95 ? 417  PHE B CG    1 
ATOM   3110 C CD1   . PHE A 1 419 ? 10.237 -11.502 -41.357 1.00 24.25 ? 417  PHE B CD1   1 
ATOM   3111 C CD2   . PHE A 1 419 ? 8.479  -10.259 -42.357 1.00 26.08 ? 417  PHE B CD2   1 
ATOM   3112 C CE1   . PHE A 1 419 ? 9.366  -11.953 -40.375 1.00 24.57 ? 417  PHE B CE1   1 
ATOM   3113 C CE2   . PHE A 1 419 ? 7.606  -10.706 -41.371 1.00 26.97 ? 417  PHE B CE2   1 
ATOM   3114 C CZ    . PHE A 1 419 ? 8.057  -11.550 -40.387 1.00 25.02 ? 417  PHE B CZ    1 
ATOM   3115 N N     . GLY A 1 420 ? 13.195 -10.376 -45.853 1.00 23.03 ? 418  GLY B N     1 
ATOM   3116 C CA    . GLY A 1 420 ? 13.728 -9.527  -46.935 1.00 24.40 ? 418  GLY B CA    1 
ATOM   3117 C C     . GLY A 1 420 ? 13.350 -8.064  -46.742 1.00 23.68 ? 418  GLY B C     1 
ATOM   3118 O O     . GLY A 1 420 ? 13.330 -7.621  -45.591 1.00 22.57 ? 418  GLY B O     1 
ATOM   3119 N N     . GLY A 1 421 ? 13.043 -7.356  -47.830 1.00 21.68 ? 419  GLY B N     1 
ATOM   3120 C CA    . GLY A 1 421 ? 12.602 -5.942  -47.799 1.00 22.40 ? 419  GLY B CA    1 
ATOM   3121 C C     . GLY A 1 421 ? 11.446 -5.699  -46.853 1.00 22.52 ? 419  GLY B C     1 
ATOM   3122 O O     . GLY A 1 421 ? 11.442 -4.665  -46.165 1.00 20.83 ? 419  GLY B O     1 
ATOM   3123 N N     . HIS A 1 422 ? 10.488 -6.628  -46.771 1.00 22.66 ? 420  HIS B N     1 
ATOM   3124 C CA    . HIS A 1 422 ? 9.338  -6.494  -45.844 1.00 21.72 ? 420  HIS B CA    1 
ATOM   3125 C C     . HIS A 1 422 ? 9.841  -6.287  -44.403 1.00 20.30 ? 420  HIS B C     1 
ATOM   3126 O O     . HIS A 1 422 ? 9.145  -5.619  -43.636 1.00 21.78 ? 420  HIS B O     1 
ATOM   3127 C CB    . HIS A 1 422 ? 8.390  -7.691  -45.966 1.00 23.92 ? 420  HIS B CB    1 
ATOM   3128 C CG    . HIS A 1 422 ? 7.578  -7.652  -47.210 1.00 23.67 ? 420  HIS B CG    1 
ATOM   3129 N ND1   . HIS A 1 422 ? 6.229  -7.267  -47.207 1.00 28.51 ? 420  HIS B ND1   1 
ATOM   3130 C CD2   . HIS A 1 422 ? 7.932  -7.844  -48.499 1.00 22.06 ? 420  HIS B CD2   1 
ATOM   3131 C CE1   . HIS A 1 422 ? 5.774  -7.282  -48.451 1.00 25.77 ? 420  HIS B CE1   1 
ATOM   3132 N NE2   . HIS A 1 422 ? 6.811  -7.654  -49.270 1.00 26.12 ? 420  HIS B NE2   1 
ATOM   3133 N N     . GLY A 1 423 ? 10.973 -6.889  -44.031 1.00 19.97 ? 421  GLY B N     1 
ATOM   3134 C CA    . GLY A 1 423 ? 11.515 -6.831  -42.658 1.00 20.96 ? 421  GLY B CA    1 
ATOM   3135 C C     . GLY A 1 423 ? 11.923 -5.419  -42.260 1.00 20.09 ? 421  GLY B C     1 
ATOM   3136 O O     . GLY A 1 423 ? 12.030 -5.134  -41.052 1.00 22.93 ? 421  GLY B O     1 
ATOM   3137 N N     . PHE A 1 424 ? 12.116 -4.531  -43.227 1.00 19.30 ? 422  PHE B N     1 
ATOM   3138 C CA    . PHE A 1 424 ? 12.540 -3.137  -42.962 1.00 19.27 ? 422  PHE B CA    1 
ATOM   3139 C C     . PHE A 1 424 ? 11.316 -2.281  -42.621 1.00 20.34 ? 422  PHE B C     1 
ATOM   3140 O O     . PHE A 1 424 ? 11.462 -1.087  -42.262 1.00 21.25 ? 422  PHE B O     1 
ATOM   3141 C CB    . PHE A 1 424 ? 13.329 -2.608  -44.161 1.00 19.96 ? 422  PHE B CB    1 
ATOM   3142 C CG    . PHE A 1 424 ? 14.205 -1.419  -43.857 1.00 19.35 ? 422  PHE B CG    1 
ATOM   3143 C CD1   . PHE A 1 424 ? 15.366 -1.575  -43.118 1.00 19.53 ? 422  PHE B CD1   1 
ATOM   3144 C CD2   . PHE A 1 424 ? 13.884 -0.165  -44.331 1.00 19.13 ? 422  PHE B CD2   1 
ATOM   3145 C CE1   . PHE A 1 424 ? 16.197 -0.497  -42.870 1.00 20.31 ? 422  PHE B CE1   1 
ATOM   3146 C CE2   . PHE A 1 424 ? 14.702 0.920   -44.063 1.00 19.76 ? 422  PHE B CE2   1 
ATOM   3147 C CZ    . PHE A 1 424 ? 15.861 0.753   -43.350 1.00 20.14 ? 422  PHE B CZ    1 
ATOM   3148 N N     . ILE A 1 425 ? 10.119 -2.843  -42.775 1.00 20.97 ? 423  ILE B N     1 
ATOM   3149 C CA    . ILE A 1 425 ? 8.860  -2.060  -42.649 1.00 22.33 ? 423  ILE B CA    1 
ATOM   3150 C C     . ILE A 1 425 ? 8.326  -2.216  -41.215 1.00 20.31 ? 423  ILE B C     1 
ATOM   3151 O O     . ILE A 1 425 ? 8.175  -3.347  -40.756 1.00 21.86 ? 423  ILE B O     1 
ATOM   3152 C CB    . ILE A 1 425 ? 7.860  -2.531  -43.729 1.00 25.35 ? 423  ILE B CB    1 
ATOM   3153 C CG1   . ILE A 1 425 ? 8.454  -2.429  -45.145 1.00 25.02 ? 423  ILE B CG1   1 
ATOM   3154 C CG2   . ILE A 1 425 ? 6.529  -1.804  -43.593 1.00 23.69 ? 423  ILE B CG2   1 
ATOM   3155 C CD1   . ILE A 1 425 ? 8.994  -1.068  -45.543 1.00 24.12 ? 423  ILE B CD1   1 
ATOM   3156 N N     . ARG A 1 426 ? 8.015  -1.115  -40.543 1.00 20.33 ? 424  ARG B N     1 
ATOM   3157 C CA    . ARG A 1 426 ? 7.760  -1.116  -39.074 1.00 21.89 ? 424  ARG B CA    1 
ATOM   3158 C C     . ARG A 1 426 ? 6.547  -1.999  -38.741 1.00 21.32 ? 424  ARG B C     1 
ATOM   3159 O O     . ARG A 1 426 ? 6.584  -2.642  -37.700 1.00 20.92 ? 424  ARG B O     1 
ATOM   3160 C CB    . ARG A 1 426 ? 7.647  0.320   -38.550 1.00 22.05 ? 424  ARG B CB    1 
ATOM   3161 C CG    . ARG A 1 426 ? 8.958  1.092   -38.676 1.00 23.93 ? 424  ARG B CG    1 
ATOM   3162 C CD    . ARG A 1 426 ? 9.256  2.057   -37.566 1.00 24.63 ? 424  ARG B CD    1 
ATOM   3163 N NE    . ARG A 1 426 ? 8.198  3.040   -37.464 1.00 25.57 ? 424  ARG B NE    1 
ATOM   3164 C CZ    . ARG A 1 426 ? 8.132  4.175   -38.156 1.00 25.48 ? 424  ARG B CZ    1 
ATOM   3165 N NH1   . ARG A 1 426 ? 9.064  4.506   -39.040 1.00 24.56 ? 424  ARG B NH1   1 
ATOM   3166 N NH2   . ARG A 1 426 ? 7.098  4.975   -37.966 1.00 25.46 ? 424  ARG B NH2   1 
ATOM   3167 N N     . GLU A 1 427 ? 5.533  -2.062  -39.605 1.00 23.03 ? 425  GLU B N     1 
ATOM   3168 C CA    . GLU A 1 427 ? 4.252  -2.752  -39.296 1.00 24.55 ? 425  GLU B CA    1 
ATOM   3169 C C     . GLU A 1 427 ? 4.475  -4.231  -38.987 1.00 24.71 ? 425  GLU B C     1 
ATOM   3170 O O     . GLU A 1 427 ? 3.693  -4.757  -38.194 1.00 25.33 ? 425  GLU B O     1 
ATOM   3171 C CB    . GLU A 1 427 ? 3.236  -2.553  -40.424 1.00 28.45 ? 425  GLU B CB    1 
ATOM   3172 C CG    . GLU A 1 427 ? 2.614  -1.164  -40.391 1.00 30.73 ? 425  GLU B CG    1 
ATOM   3173 C CD    . GLU A 1 427 ? 3.383  -0.030  -41.076 1.00 36.02 ? 425  GLU B CD    1 
ATOM   3174 O OE1   . GLU A 1 427 ? 2.731  0.986   -41.365 1.00 39.97 ? 425  GLU B OE1   1 
ATOM   3175 O OE2   . GLU A 1 427 ? 4.638  -0.112  -41.266 1.00 33.25 ? 425  GLU B OE2   1 
ATOM   3176 N N     . TRP A 1 428 ? 5.504  -4.871  -39.552 1.00 22.65 ? 426  TRP B N     1 
ATOM   3177 C CA    . TRP A 1 428 ? 5.832  -6.312  -39.307 1.00 23.77 ? 426  TRP B CA    1 
ATOM   3178 C C     . TRP A 1 428 ? 6.455  -6.554  -37.931 1.00 24.00 ? 426  TRP B C     1 
ATOM   3179 O O     . TRP A 1 428 ? 6.514  -7.739  -37.526 1.00 25.87 ? 426  TRP B O     1 
ATOM   3180 C CB    . TRP A 1 428 ? 6.755  -6.853  -40.406 1.00 26.67 ? 426  TRP B CB    1 
ATOM   3181 C CG    . TRP A 1 428 ? 6.061  -6.907  -41.726 1.00 29.08 ? 426  TRP B CG    1 
ATOM   3182 C CD1   . TRP A 1 428 ? 6.159  -6.019  -42.753 1.00 30.53 ? 426  TRP B CD1   1 
ATOM   3183 C CD2   . TRP A 1 428 ? 5.079  -7.882  -42.121 1.00 30.48 ? 426  TRP B CD2   1 
ATOM   3184 N NE1   . TRP A 1 428 ? 5.339  -6.398  -43.784 1.00 31.86 ? 426  TRP B NE1   1 
ATOM   3185 C CE2   . TRP A 1 428 ? 4.659  -7.534  -43.420 1.00 31.27 ? 426  TRP B CE2   1 
ATOM   3186 C CE3   . TRP A 1 428 ? 4.541  -9.020  -41.508 1.00 32.02 ? 426  TRP B CE3   1 
ATOM   3187 C CZ2   . TRP A 1 428 ? 3.719  -8.287  -44.120 1.00 31.05 ? 426  TRP B CZ2   1 
ATOM   3188 C CZ3   . TRP A 1 428 ? 3.609  -9.764  -42.200 1.00 35.20 ? 426  TRP B CZ3   1 
ATOM   3189 C CH2   . TRP A 1 428 ? 3.216  -9.403  -43.493 1.00 31.37 ? 426  TRP B CH2   1 
ATOM   3190 N N     . GLY A 1 429 ? 6.946  -5.512  -37.252 1.00 23.90 ? 427  GLY B N     1 
ATOM   3191 C CA    . GLY A 1 429 ? 7.440  -5.622  -35.865 1.00 24.09 ? 427  GLY B CA    1 
ATOM   3192 C C     . GLY A 1 429 ? 8.864  -6.145  -35.733 1.00 23.73 ? 427  GLY B C     1 
ATOM   3193 O O     . GLY A 1 429 ? 9.385  -6.128  -34.607 1.00 23.30 ? 427  GLY B O     1 
ATOM   3194 N N     . GLN A 1 430 ? 9.490  -6.637  -36.805 1.00 23.39 ? 428  GLN B N     1 
ATOM   3195 C CA    . GLN A 1 430 ? 10.839 -7.267  -36.730 1.00 21.97 ? 428  GLN B CA    1 
ATOM   3196 C C     . GLN A 1 430 ? 11.889 -6.181  -36.491 1.00 21.39 ? 428  GLN B C     1 
ATOM   3197 O O     . GLN A 1 430 ? 12.839 -6.420  -35.702 1.00 22.45 ? 428  GLN B O     1 
ATOM   3198 C CB    . GLN A 1 430 ? 11.109 -8.086  -37.993 1.00 23.47 ? 428  GLN B CB    1 
ATOM   3199 C CG    . GLN A 1 430 ? 10.215 -9.313  -38.137 1.00 23.71 ? 428  GLN B CG    1 
ATOM   3200 C CD    . GLN A 1 430 ? 10.330 -10.296 -36.994 1.00 22.99 ? 428  GLN B CD    1 
ATOM   3201 O OE1   . GLN A 1 430 ? 9.820  -10.075 -35.895 1.00 22.82 ? 428  GLN B OE1   1 
ATOM   3202 N NE2   . GLN A 1 430 ? 10.952 -11.432 -37.251 1.00 22.47 ? 428  GLN B NE2   1 
ATOM   3203 N N     . GLU A 1 431 ? 11.728 -5.005  -37.090 1.00 22.30 ? 429  GLU B N     1 
ATOM   3204 C CA    . GLU A 1 431 ? 12.788 -3.964  -36.954 1.00 23.50 ? 429  GLU B CA    1 
ATOM   3205 C C     . GLU A 1 431 ? 12.734 -3.430  -35.508 1.00 23.50 ? 429  GLU B C     1 
ATOM   3206 O O     . GLU A 1 431 ? 13.796 -3.174  -34.920 1.00 22.44 ? 429  GLU B O     1 
ATOM   3207 C CB    . GLU A 1 431 ? 12.659 -2.914  -38.051 1.00 22.63 ? 429  GLU B CB    1 
ATOM   3208 C CG    . GLU A 1 431 ? 11.373 -2.110  -37.988 1.00 22.98 ? 429  GLU B CG    1 
ATOM   3209 C CD    . GLU A 1 431 ? 11.426 -0.966  -36.993 1.00 22.22 ? 429  GLU B CD    1 
ATOM   3210 O OE1   . GLU A 1 431 ? 12.495 -0.392  -36.847 1.00 20.74 ? 429  GLU B OE1   1 
ATOM   3211 O OE2   . GLU A 1 431 ? 10.377 -0.650  -36.395 1.00 22.33 ? 429  GLU B OE2   1 
ATOM   3212 N N     . GLN A 1 432 ? 11.551 -3.296  -34.910 1.00 22.68 ? 430  GLN B N     1 
ATOM   3213 C CA    . GLN A 1 432 ? 11.473 -2.854  -33.486 1.00 22.54 ? 430  GLN B CA    1 
ATOM   3214 C C     . GLN A 1 432 ? 12.253 -3.806  -32.574 1.00 21.89 ? 430  GLN B C     1 
ATOM   3215 O O     . GLN A 1 432 ? 12.942 -3.328  -31.692 1.00 24.05 ? 430  GLN B O     1 
ATOM   3216 C CB    . GLN A 1 432 ? 10.028 -2.748  -32.991 1.00 23.04 ? 430  GLN B CB    1 
ATOM   3217 C CG    . GLN A 1 432 ? 9.915  -2.253  -31.560 1.00 21.27 ? 430  GLN B CG    1 
ATOM   3218 C CD    . GLN A 1 432 ? 8.497  -2.319  -31.053 1.00 23.19 ? 430  GLN B CD    1 
ATOM   3219 O OE1   . GLN A 1 432 ? 7.545  -2.148  -31.805 1.00 24.67 ? 430  GLN B OE1   1 
ATOM   3220 N NE2   . GLN A 1 432 ? 8.352  -2.573  -29.765 1.00 23.59 ? 430  GLN B NE2   1 
ATOM   3221 N N     . LEU A 1 433 ? 12.123 -5.111  -32.796 1.00 20.90 ? 431  LEU B N     1 
ATOM   3222 C CA    . LEU A 1 433 ? 12.778 -6.098  -31.901 1.00 19.84 ? 431  LEU B CA    1 
ATOM   3223 C C     . LEU A 1 433 ? 14.302 -5.953  -31.967 1.00 21.10 ? 431  LEU B C     1 
ATOM   3224 O O     . LEU A 1 433 ? 14.949 -6.210  -30.963 1.00 21.06 ? 431  LEU B O     1 
ATOM   3225 C CB    . LEU A 1 433 ? 12.321 -7.506  -32.283 1.00 20.98 ? 431  LEU B CB    1 
ATOM   3226 C CG    . LEU A 1 433 ? 10.844 -7.796  -32.023 1.00 23.30 ? 431  LEU B CG    1 
ATOM   3227 C CD1   . LEU A 1 433 ? 10.475 -9.194  -32.486 1.00 23.84 ? 431  LEU B CD1   1 
ATOM   3228 C CD2   . LEU A 1 433 ? 10.507 -7.618  -30.550 1.00 24.14 ? 431  LEU B CD2   1 
ATOM   3229 N N     . VAL A 1 434 ? 14.828 -5.550  -33.119 1.00 21.06 ? 432  VAL B N     1 
ATOM   3230 C CA    . VAL A 1 434 ? 16.295 -5.304  -33.226 1.00 21.77 ? 432  VAL B CA    1 
ATOM   3231 C C     . VAL A 1 434 ? 16.619 -4.086  -32.361 1.00 21.68 ? 432  VAL B C     1 
ATOM   3232 O O     . VAL A 1 434 ? 17.571 -4.142  -31.587 1.00 19.20 ? 432  VAL B O     1 
ATOM   3233 C CB    . VAL A 1 434 ? 16.747 -5.068  -34.680 1.00 20.54 ? 432  VAL B CB    1 
ATOM   3234 C CG1   . VAL A 1 434 ? 18.216 -4.687  -34.754 1.00 20.34 ? 432  VAL B CG1   1 
ATOM   3235 C CG2   . VAL A 1 434 ? 16.462 -6.276  -35.557 1.00 22.73 ? 432  VAL B CG2   1 
ATOM   3236 N N     . ARG A 1 435 ? 15.813 -3.039  -32.512 1.00 21.09 ? 433  ARG B N     1 
ATOM   3237 C CA    . ARG A 1 435 ? 16.056 -1.788  -31.755 1.00 22.94 ? 433  ARG B CA    1 
ATOM   3238 C C     . ARG A 1 435 ? 15.895 -2.033  -30.247 1.00 24.57 ? 433  ARG B C     1 
ATOM   3239 O O     . ARG A 1 435 ? 16.716 -1.527  -29.483 1.00 26.35 ? 433  ARG B O     1 
ATOM   3240 C CB    . ARG A 1 435 ? 15.106 -0.700  -32.228 1.00 21.95 ? 433  ARG B CB    1 
ATOM   3241 C CG    . ARG A 1 435 ? 15.338 -0.331  -33.677 1.00 23.20 ? 433  ARG B CG    1 
ATOM   3242 C CD    . ARG A 1 435 ? 14.484 0.844   -34.067 1.00 22.69 ? 433  ARG B CD    1 
ATOM   3243 N NE    . ARG A 1 435 ? 13.085 0.542   -34.312 1.00 22.68 ? 433  ARG B NE    1 
ATOM   3244 C CZ    . ARG A 1 435 ? 12.043 0.904   -33.549 1.00 23.25 ? 433  ARG B CZ    1 
ATOM   3245 N NH1   . ARG A 1 435 ? 12.209 1.542   -32.392 1.00 22.55 ? 433  ARG B NH1   1 
ATOM   3246 N NH2   . ARG A 1 435 ? 10.817 0.626   -33.963 1.00 22.06 ? 433  ARG B NH2   1 
ATOM   3247 N N     . ASP A 1 436 ? 14.874 -2.783  -29.838 1.00 24.38 ? 434  ASP B N     1 
ATOM   3248 C CA    . ASP A 1 436 ? 14.607 -3.083  -28.406 1.00 24.52 ? 434  ASP B CA    1 
ATOM   3249 C C     . ASP A 1 436 ? 15.767 -3.940  -27.897 1.00 24.23 ? 434  ASP B C     1 
ATOM   3250 O O     . ASP A 1 436 ? 16.285 -3.693  -26.777 1.00 23.55 ? 434  ASP B O     1 
ATOM   3251 C CB    . ASP A 1 436 ? 13.228 -3.751  -28.240 1.00 23.92 ? 434  ASP B CB    1 
ATOM   3252 C CG    . ASP A 1 436 ? 12.008 -2.844  -28.420 1.00 25.42 ? 434  ASP B CG    1 
ATOM   3253 O OD1   . ASP A 1 436 ? 12.179 -1.633  -28.631 1.00 25.23 ? 434  ASP B OD1   1 
ATOM   3254 O OD2   . ASP A 1 436 ? 10.869 -3.361  -28.315 1.00 24.91 ? 434  ASP B OD2   1 
ATOM   3255 N N     . CYS A 1 437 ? 16.203 -4.918  -28.683 1.00 23.05 ? 435  CYS B N     1 
ATOM   3256 C CA    . CYS A 1 437 ? 17.272 -5.844  -28.260 1.00 21.94 ? 435  CYS B CA    1 
ATOM   3257 C C     . CYS A 1 437 ? 18.582 -5.081  -28.011 1.00 22.86 ? 435  CYS B C     1 
ATOM   3258 O O     . CYS A 1 437 ? 19.284 -5.401  -27.045 1.00 23.53 ? 435  CYS B O     1 
ATOM   3259 C CB    . CYS A 1 437 ? 17.493 -6.953  -29.274 1.00 22.77 ? 435  CYS B CB    1 
ATOM   3260 S SG    . CYS A 1 437 ? 18.514 -8.271  -28.576 1.00 26.45 ? 435  CYS B SG    1 
ATOM   3261 N N     . ARG A 1 438 ? 18.882 -4.053  -28.793 1.00 20.86 ? 436  ARG B N     1 
ATOM   3262 C CA    . ARG A 1 438 ? 20.142 -3.288  -28.603 1.00 23.83 ? 436  ARG B CA    1 
ATOM   3263 C C     . ARG A 1 438 ? 20.235 -2.722  -27.175 1.00 23.00 ? 436  ARG B C     1 
ATOM   3264 O O     . ARG A 1 438 ? 21.353 -2.610  -26.684 1.00 22.74 ? 436  ARG B O     1 
ATOM   3265 C CB    . ARG A 1 438 ? 20.286 -2.194  -29.659 1.00 22.68 ? 436  ARG B CB    1 
ATOM   3266 C CG    . ARG A 1 438 ? 20.676 -2.747  -31.025 1.00 23.39 ? 436  ARG B CG    1 
ATOM   3267 C CD    . ARG A 1 438 ? 22.082 -3.327  -31.041 1.00 23.76 ? 436  ARG B CD    1 
ATOM   3268 N NE    . ARG A 1 438 ? 23.124 -2.345  -30.815 1.00 24.12 ? 436  ARG B NE    1 
ATOM   3269 C CZ    . ARG A 1 438 ? 24.332 -2.609  -30.306 1.00 23.27 ? 436  ARG B CZ    1 
ATOM   3270 N NH1   . ARG A 1 438 ? 24.641 -3.814  -29.881 1.00 24.10 ? 436  ARG B NH1   1 
ATOM   3271 N NH2   . ARG A 1 438 ? 25.234 -1.660  -30.211 1.00 26.49 ? 436  ARG B NH2   1 
ATOM   3272 N N     . ILE A 1 439 ? 19.112 -2.420  -26.519 1.00 23.74 ? 437  ILE B N     1 
ATOM   3273 C CA    . ILE A 1 439 ? 19.136 -1.832  -25.146 1.00 22.95 ? 437  ILE B CA    1 
ATOM   3274 C C     . ILE A 1 439 ? 19.739 -2.844  -24.188 1.00 22.90 ? 437  ILE B C     1 
ATOM   3275 O O     . ILE A 1 439 ? 20.510 -2.426  -23.288 1.00 25.46 ? 437  ILE B O     1 
ATOM   3276 C CB    . ILE A 1 439 ? 17.745 -1.317  -24.712 1.00 23.05 ? 437  ILE B CB    1 
ATOM   3277 C CG1   . ILE A 1 439 ? 17.852 -0.010  -23.919 1.00 23.18 ? 437  ILE B CG1   1 
ATOM   3278 C CG2   . ILE A 1 439 ? 16.931 -2.380  -23.982 1.00 23.24 ? 437  ILE B CG2   1 
ATOM   3279 C CD1   . ILE A 1 439 ? 18.282 -0.173  -22.468 1.00 24.67 ? 437  ILE B CD1   1 
ATOM   3280 N N     . THR A 1 440 ? 19.506 -4.138  -24.420 1.00 22.74 ? 438  THR B N     1 
ATOM   3281 C CA    . THR A 1 440 ? 19.869 -5.176  -23.438 1.00 21.37 ? 438  THR B CA    1 
ATOM   3282 C C     . THR A 1 440 ? 21.386 -5.273  -23.356 1.00 22.52 ? 438  THR B C     1 
ATOM   3283 O O     . THR A 1 440 ? 21.872 -5.790  -22.342 1.00 22.22 ? 438  THR B O     1 
ATOM   3284 C CB    . THR A 1 440 ? 19.174 -6.510  -23.729 1.00 22.39 ? 438  THR B CB    1 
ATOM   3285 O OG1   . THR A 1 440 ? 19.710 -7.125  -24.892 1.00 21.79 ? 438  THR B OG1   1 
ATOM   3286 C CG2   . THR A 1 440 ? 17.675 -6.334  -23.894 1.00 21.99 ? 438  THR B CG2   1 
ATOM   3287 N N     . GLN A 1 441 ? 22.106 -4.877  -24.409 1.00 22.22 ? 439  GLN B N     1 
ATOM   3288 C CA    . GLN A 1 441 ? 23.580 -5.015  -24.463 1.00 22.41 ? 439  GLN B CA    1 
ATOM   3289 C C     . GLN A 1 441 ? 24.245 -3.845  -23.718 1.00 24.45 ? 439  GLN B C     1 
ATOM   3290 O O     . GLN A 1 441 ? 25.473 -3.867  -23.590 1.00 23.73 ? 439  GLN B O     1 
ATOM   3291 C CB    . GLN A 1 441 ? 24.031 -5.107  -25.923 1.00 23.53 ? 439  GLN B CB    1 
ATOM   3292 C CG    . GLN A 1 441 ? 23.543 -6.376  -26.600 1.00 23.61 ? 439  GLN B CG    1 
ATOM   3293 C CD    . GLN A 1 441 ? 23.636 -6.310  -28.103 1.00 26.30 ? 439  GLN B CD    1 
ATOM   3294 O OE1   . GLN A 1 441 ? 22.891 -5.580  -28.759 1.00 26.97 ? 439  GLN B OE1   1 
ATOM   3295 N NE2   . GLN A 1 441 ? 24.520 -7.126  -28.657 1.00 23.63 ? 439  GLN B NE2   1 
ATOM   3296 N N     . ILE A 1 442 ? 23.479 -2.845  -23.276 1.00 24.86 ? 440  ILE B N     1 
ATOM   3297 C CA    . ILE A 1 442 ? 24.018 -1.740  -22.429 1.00 27.63 ? 440  ILE B CA    1 
ATOM   3298 C C     . ILE A 1 442 ? 23.179 -1.532  -21.149 1.00 28.95 ? 440  ILE B C     1 
ATOM   3299 O O     . ILE A 1 442 ? 23.567 -0.658  -20.359 1.00 28.00 ? 440  ILE B O     1 
ATOM   3300 C CB    . ILE A 1 442 ? 24.195 -0.452  -23.259 1.00 27.54 ? 440  ILE B CB    1 
ATOM   3301 C CG1   . ILE A 1 442 ? 22.911 0.079   -23.897 1.00 27.05 ? 440  ILE B CG1   1 
ATOM   3302 C CG2   . ILE A 1 442 ? 25.270 -0.681  -24.315 1.00 29.14 ? 440  ILE B CG2   1 
ATOM   3303 C CD1   . ILE A 1 442 ? 21.879 0.589   -22.933 1.00 27.48 ? 440  ILE B CD1   1 
ATOM   3304 N N     . TYR A 1 443 ? 22.120 -2.322  -20.918 1.00 27.31 ? 441  TYR B N     1 
ATOM   3305 C CA    . TYR A 1 443 ? 21.258 -2.229  -19.709 1.00 26.13 ? 441  TYR B CA    1 
ATOM   3306 C C     . TYR A 1 443 ? 21.954 -2.981  -18.568 1.00 26.61 ? 441  TYR B C     1 
ATOM   3307 O O     . TYR A 1 443 ? 22.445 -4.084  -18.804 1.00 26.96 ? 441  TYR B O     1 
ATOM   3308 C CB    . TYR A 1 443 ? 19.856 -2.755  -20.021 1.00 28.15 ? 441  TYR B CB    1 
ATOM   3309 C CG    . TYR A 1 443 ? 18.773 -2.338  -19.052 1.00 26.74 ? 441  TYR B CG    1 
ATOM   3310 C CD1   . TYR A 1 443 ? 18.392 -1.011  -18.926 1.00 27.95 ? 441  TYR B CD1   1 
ATOM   3311 C CD2   . TYR A 1 443 ? 18.074 -3.284  -18.321 1.00 29.76 ? 441  TYR B CD2   1 
ATOM   3312 C CE1   . TYR A 1 443 ? 17.368 -0.631  -18.070 1.00 29.62 ? 441  TYR B CE1   1 
ATOM   3313 C CE2   . TYR A 1 443 ? 17.059 -2.924  -17.444 1.00 29.14 ? 441  TYR B CE2   1 
ATOM   3314 C CZ    . TYR A 1 443 ? 16.704 -1.590  -17.318 1.00 30.17 ? 441  TYR B CZ    1 
ATOM   3315 O OH    . TYR A 1 443 ? 15.688 -1.238  -16.469 1.00 32.18 ? 441  TYR B OH    1 
ATOM   3316 N N     . GLU A 1 444 ? 21.988 -2.411  -17.353 1.00 30.49 ? 442  GLU B N     1 
ATOM   3317 C CA    . GLU A 1 444 ? 22.749 -2.977  -16.201 1.00 32.93 ? 442  GLU B CA    1 
ATOM   3318 C C     . GLU A 1 444 ? 24.233 -3.101  -16.579 1.00 33.31 ? 442  GLU B C     1 
ATOM   3319 O O     . GLU A 1 444 ? 24.861 -4.117  -16.202 1.00 34.40 ? 442  GLU B O     1 
ATOM   3320 C CB    . GLU A 1 444 ? 22.249 -4.364  -15.798 1.00 40.58 ? 442  GLU B CB    1 
ATOM   3321 C CG    . GLU A 1 444 ? 20.770 -4.415  -15.442 1.00 55.10 ? 442  GLU B CG    1 
ATOM   3322 C CD    . GLU A 1 444 ? 20.374 -3.699  -14.160 1.00 62.03 ? 442  GLU B CD    1 
ATOM   3323 O OE1   . GLU A 1 444 ? 21.169 -3.789  -13.178 1.00 61.89 ? 442  GLU B OE1   1 
ATOM   3324 O OE2   . GLU A 1 444 ? 19.263 -3.084  -14.140 1.00 60.98 ? 442  GLU B OE2   1 
ATOM   3325 N N     . GLY A 1 445 ? 24.751 -2.138  -17.339 1.00 28.86 ? 443  GLY B N     1 
ATOM   3326 C CA    . GLY A 1 445 ? 26.164 -2.121  -17.744 1.00 30.44 ? 443  GLY B CA    1 
ATOM   3327 C C     . GLY A 1 445 ? 26.387 -2.670  -19.150 1.00 30.43 ? 443  GLY B C     1 
ATOM   3328 O O     . GLY A 1 445 ? 25.599 -3.490  -19.649 1.00 28.28 ? 443  GLY B O     1 
ATOM   3329 N N     . THR A 1 446 ? 27.480 -2.257  -19.763 1.00 26.88 ? 444  THR B N     1 
ATOM   3330 C CA    . THR A 1 446 ? 27.845 -2.698  -21.120 1.00 24.22 ? 444  THR B CA    1 
ATOM   3331 C C     . THR A 1 446 ? 28.263 -4.154  -21.042 1.00 22.04 ? 444  THR B C     1 
ATOM   3332 O O     . THR A 1 446 ? 28.787 -4.582  -20.005 1.00 23.90 ? 444  THR B O     1 
ATOM   3333 C CB    . THR A 1 446 ? 28.969 -1.843  -21.701 1.00 22.64 ? 444  THR B CB    1 
ATOM   3334 O OG1   . THR A 1 446 ? 30.151 -2.172  -20.970 1.00 23.40 ? 444  THR B OG1   1 
ATOM   3335 C CG2   . THR A 1 446 ? 28.656 -0.368  -21.633 1.00 23.20 ? 444  THR B CG2   1 
ATOM   3336 N N     . ASN A 1 447 ? 28.108 -4.854  -22.149 1.00 23.09 ? 445  ASN B N     1 
ATOM   3337 C CA    . ASN A 1 447 ? 28.513 -6.269  -22.279 1.00 22.40 ? 445  ASN B CA    1 
ATOM   3338 C C     . ASN A 1 447 ? 30.033 -6.383  -22.110 1.00 21.04 ? 445  ASN B C     1 
ATOM   3339 O O     . ASN A 1 447 ? 30.473 -7.382  -21.546 1.00 21.05 ? 445  ASN B O     1 
ATOM   3340 C CB    . ASN A 1 447 ? 27.987 -6.861  -23.585 1.00 23.52 ? 445  ASN B CB    1 
ATOM   3341 C CG    . ASN A 1 447 ? 26.528 -7.254  -23.460 1.00 24.75 ? 445  ASN B CG    1 
ATOM   3342 O OD1   . ASN A 1 447 ? 25.931 -7.071  -22.398 1.00 23.02 ? 445  ASN B OD1   1 
ATOM   3343 N ND2   . ASN A 1 447 ? 25.970 -7.827  -24.515 1.00 22.23 ? 445  ASN B ND2   1 
ATOM   3344 N N     . GLY A 1 448 ? 30.799 -5.417  -22.605 1.00 21.55 ? 446  GLY B N     1 
ATOM   3345 C CA    . GLY A 1 448 ? 32.264 -5.418  -22.457 1.00 21.80 ? 446  GLY B CA    1 
ATOM   3346 C C     . GLY A 1 448 ? 32.691 -5.390  -20.998 1.00 23.01 ? 446  GLY B C     1 
ATOM   3347 O O     . GLY A 1 448 ? 33.694 -6.041  -20.649 1.00 24.00 ? 446  GLY B O     1 
ATOM   3348 N N     . ILE A 1 449 ? 31.945 -4.690  -20.150 1.00 25.19 ? 447  ILE B N     1 
ATOM   3349 C CA    . ILE A 1 449 ? 32.182 -4.689  -18.679 1.00 24.55 ? 447  ILE B CA    1 
ATOM   3350 C C     . ILE A 1 449 ? 31.826 -6.058  -18.071 1.00 24.05 ? 447  ILE B C     1 
ATOM   3351 O O     . ILE A 1 449 ? 32.629 -6.566  -17.245 1.00 22.11 ? 447  ILE B O     1 
ATOM   3352 C CB    . ILE A 1 449 ? 31.446 -3.494  -18.053 1.00 27.29 ? 447  ILE B CB    1 
ATOM   3353 C CG1   . ILE A 1 449 ? 32.111 -2.190  -18.505 1.00 29.04 ? 447  ILE B CG1   1 
ATOM   3354 C CG2   . ILE A 1 449 ? 31.397 -3.617  -16.535 1.00 30.64 ? 447  ILE B CG2   1 
ATOM   3355 C CD1   . ILE A 1 449 ? 33.589 -2.118  -18.180 1.00 32.16 ? 447  ILE B CD1   1 
ATOM   3356 N N     . GLN A 1 450 ? 30.720 -6.687  -18.493 1.00 23.11 ? 448  GLN B N     1 
ATOM   3357 C CA    . GLN A 1 450 ? 30.407 -8.075  -18.075 1.00 23.93 ? 448  GLN B CA    1 
ATOM   3358 C C     . GLN A 1 450 ? 31.548 -9.024  -18.470 1.00 24.29 ? 448  GLN B C     1 
ATOM   3359 O O     . GLN A 1 450 ? 31.935 -9.899  -17.644 1.00 22.78 ? 448  GLN B O     1 
ATOM   3360 C CB    . GLN A 1 450 ? 29.097 -8.537  -18.696 1.00 26.02 ? 448  GLN B CB    1 
ATOM   3361 C CG    . GLN A 1 450 ? 27.904 -7.690  -18.253 1.00 27.70 ? 448  GLN B CG    1 
ATOM   3362 C CD    . GLN A 1 450 ? 27.654 -7.775  -16.762 1.00 29.19 ? 448  GLN B CD    1 
ATOM   3363 O OE1   . GLN A 1 450 ? 27.906 -8.792  -16.124 1.00 26.94 ? 448  GLN B OE1   1 
ATOM   3364 N NE2   . GLN A 1 450 ? 27.145 -6.690  -16.193 1.00 31.28 ? 448  GLN B NE2   1 
ATOM   3365 N N     . ALA A 1 451 ? 32.047 -8.916  -19.704 1.00 22.47 ? 449  ALA B N     1 
ATOM   3366 C CA    . ALA A 1 451 ? 33.123 -9.811  -20.186 1.00 23.68 ? 449  ALA B CA    1 
ATOM   3367 C C     . ALA A 1 451 ? 34.386 -9.606  -19.339 1.00 23.19 ? 449  ALA B C     1 
ATOM   3368 O O     . ALA A 1 451 ? 35.032 -10.591 -18.975 1.00 22.38 ? 449  ALA B O     1 
ATOM   3369 C CB    . ALA A 1 451 ? 33.370 -9.589  -21.665 1.00 24.31 ? 449  ALA B CB    1 
ATOM   3370 N N     . LEU A 1 452 ? 34.723 -8.362  -19.039 1.00 22.19 ? 450  LEU B N     1 
ATOM   3371 C CA    . LEU A 1 452 ? 35.897 -8.040  -18.189 1.00 24.41 ? 450  LEU B CA    1 
ATOM   3372 C C     . LEU A 1 452 ? 35.738 -8.652  -16.792 1.00 24.04 ? 450  LEU B C     1 
ATOM   3373 O O     . LEU A 1 452 ? 36.734 -9.164  -16.259 1.00 25.88 ? 450  LEU B O     1 
ATOM   3374 C CB    . LEU A 1 452 ? 36.039 -6.518  -18.107 1.00 24.68 ? 450  LEU B CB    1 
ATOM   3375 C CG    . LEU A 1 452 ? 37.274 -6.050  -17.333 1.00 24.14 ? 450  LEU B CG    1 
ATOM   3376 C CD1   . LEU A 1 452 ? 38.532 -6.531  -18.026 1.00 26.15 ? 450  LEU B CD1   1 
ATOM   3377 C CD2   . LEU A 1 452 ? 37.266 -4.528  -17.208 1.00 22.86 ? 450  LEU B CD2   1 
ATOM   3378 N N     . ASP A 1 453 ? 34.536 -8.581  -16.210 1.00 27.18 ? 451  ASP B N     1 
ATOM   3379 C CA    . ASP A 1 453 ? 34.219 -9.216  -14.904 1.00 27.18 ? 451  ASP B CA    1 
ATOM   3380 C C     . ASP A 1 453 ? 34.525 -10.712 -15.017 1.00 26.16 ? 451  ASP B C     1 
ATOM   3381 O O     . ASP A 1 453 ? 35.250 -11.250 -14.153 1.00 26.09 ? 451  ASP B O     1 
ATOM   3382 C CB    . ASP A 1 453 ? 32.757 -8.977  -14.503 1.00 30.38 ? 451  ASP B CB    1 
ATOM   3383 C CG    . ASP A 1 453 ? 32.396 -9.646  -13.184 1.00 34.84 ? 451  ASP B CG    1 
ATOM   3384 O OD1   . ASP A 1 453 ? 33.083 -9.355  -12.180 1.00 39.71 ? 451  ASP B OD1   1 
ATOM   3385 O OD2   . ASP A 1 453 ? 31.486 -10.500 -13.183 1.00 35.17 ? 451  ASP B OD2   1 
ATOM   3386 N N     . LEU A 1 454 ? 34.019 -11.373 -16.062 1.00 26.73 ? 452  LEU B N     1 
ATOM   3387 C CA    . LEU A 1 454 ? 34.180 -12.842 -16.221 1.00 26.96 ? 452  LEU B CA    1 
ATOM   3388 C C     . LEU A 1 454 ? 35.666 -13.195 -16.184 1.00 28.56 ? 452  LEU B C     1 
ATOM   3389 O O     . LEU A 1 454 ? 36.069 -14.070 -15.402 1.00 27.40 ? 452  LEU B O     1 
ATOM   3390 C CB    . LEU A 1 454 ? 33.587 -13.277 -17.558 1.00 26.63 ? 452  LEU B CB    1 
ATOM   3391 C CG    . LEU A 1 454 ? 33.893 -14.719 -17.950 1.00 28.19 ? 452  LEU B CG    1 
ATOM   3392 C CD1   . LEU A 1 454 ? 33.340 -15.667 -16.896 1.00 28.59 ? 452  LEU B CD1   1 
ATOM   3393 C CD2   . LEU A 1 454 ? 33.322 -15.049 -19.328 1.00 27.65 ? 452  LEU B CD2   1 
ATOM   3394 N N     . VAL A 1 455 ? 36.449 -12.601 -17.074 1.00 26.94 ? 453  VAL B N     1 
ATOM   3395 C CA    . VAL A 1 455 ? 37.864 -13.034 -17.259 1.00 27.41 ? 453  VAL B CA    1 
ATOM   3396 C C     . VAL A 1 455 ? 38.696 -12.495 -16.094 1.00 27.49 ? 453  VAL B C     1 
ATOM   3397 O O     . VAL A 1 455 ? 39.596 -13.220 -15.632 1.00 27.84 ? 453  VAL B O     1 
ATOM   3398 C CB    . VAL A 1 455 ? 38.433 -12.628 -18.632 1.00 29.85 ? 453  VAL B CB    1 
ATOM   3399 C CG1   . VAL A 1 455 ? 37.801 -13.464 -19.738 1.00 30.62 ? 453  VAL B CG1   1 
ATOM   3400 C CG2   . VAL A 1 455 ? 38.251 -11.143 -18.931 1.00 31.13 ? 453  VAL B CG2   1 
ATOM   3401 N N     . GLY A 1 456 ? 38.442 -11.264 -15.660 1.00 27.97 ? 454  GLY B N     1 
ATOM   3402 C CA    . GLY A 1 456 ? 39.253 -10.609 -14.613 1.00 30.49 ? 454  GLY B CA    1 
ATOM   3403 C C     . GLY A 1 456 ? 38.989 -11.192 -13.225 1.00 29.98 ? 454  GLY B C     1 
ATOM   3404 O O     . GLY A 1 456 ? 39.953 -11.592 -12.545 1.00 30.14 ? 454  GLY B O     1 
ATOM   3405 N N     . ARG A 1 457 ? 37.730 -11.229 -12.801 1.00 30.91 ? 455  ARG B N     1 
ATOM   3406 C CA    . ARG A 1 457 ? 37.359 -11.641 -11.426 1.00 31.07 ? 455  ARG B CA    1 
ATOM   3407 C C     . ARG A 1 457 ? 37.073 -13.136 -11.370 1.00 29.72 ? 455  ARG B C     1 
ATOM   3408 O O     . ARG A 1 457 ? 37.552 -13.776 -10.437 1.00 29.03 ? 455  ARG B O     1 
ATOM   3409 C CB    . ARG A 1 457 ? 36.109 -10.912 -10.942 1.00 37.60 ? 455  ARG B CB    1 
ATOM   3410 C CG    . ARG A 1 457 ? 36.249 -9.405  -10.933 1.00 44.36 ? 455  ARG B CG    1 
ATOM   3411 C CD    . ARG A 1 457 ? 36.333 -8.878  -9.521  1.00 58.58 ? 455  ARG B CD    1 
ATOM   3412 N NE    . ARG A 1 457 ? 35.890 -7.497  -9.530  1.00 65.51 ? 455  ARG B NE    1 
ATOM   3413 C CZ    . ARG A 1 457 ? 35.832 -6.715  -8.465  1.00 74.47 ? 455  ARG B CZ    1 
ATOM   3414 N NH1   . ARG A 1 457 ? 35.406 -5.470  -8.594  1.00 78.00 ? 455  ARG B NH1   1 
ATOM   3415 N NH2   . ARG A 1 457 ? 36.198 -7.172  -7.281  1.00 74.46 ? 455  ARG B NH2   1 
ATOM   3416 N N     . LYS A 1 458 ? 36.275 -13.672 -12.292 1.00 25.88 ? 456  LYS B N     1 
ATOM   3417 C CA    . LYS A 1 458 ? 35.689 -15.033 -12.134 1.00 25.58 ? 456  LYS B CA    1 
ATOM   3418 C C     . LYS A 1 458 ? 36.666 -16.093 -12.638 1.00 27.81 ? 456  LYS B C     1 
ATOM   3419 O O     . LYS A 1 458 ? 36.664 -17.221 -12.101 1.00 26.65 ? 456  LYS B O     1 
ATOM   3420 C CB    . LYS A 1 458 ? 34.307 -15.081 -12.799 1.00 26.67 ? 456  LYS B CB    1 
ATOM   3421 C CG    . LYS A 1 458 ? 33.378 -13.933 -12.419 1.00 27.43 ? 456  LYS B CG    1 
ATOM   3422 C CD    . LYS A 1 458 ? 33.189 -13.742 -10.894 1.00 31.02 ? 456  LYS B CD    1 
ATOM   3423 C CE    . LYS A 1 458 ? 32.490 -12.453 -10.505 1.00 32.43 ? 456  LYS B CE    1 
ATOM   3424 N NZ    . LYS A 1 458 ? 31.165 -12.323 -11.156 1.00 34.13 ? 456  LYS B NZ    1 
ATOM   3425 N N     . VAL A 1 459 ? 37.510 -15.754 -13.607 1.00 27.62 ? 457  VAL B N     1 
ATOM   3426 C CA    . VAL A 1 459 ? 38.538 -16.712 -14.108 1.00 27.61 ? 457  VAL B CA    1 
ATOM   3427 C C     . VAL A 1 459 ? 39.867 -16.405 -13.411 1.00 27.67 ? 457  VAL B C     1 
ATOM   3428 O O     . VAL A 1 459 ? 40.257 -17.201 -12.537 1.00 29.19 ? 457  VAL B O     1 
ATOM   3429 C CB    . VAL A 1 459 ? 38.607 -16.692 -15.653 1.00 29.28 ? 457  VAL B CB    1 
ATOM   3430 C CG1   . VAL A 1 459 ? 39.713 -17.581 -16.186 1.00 29.74 ? 457  VAL B CG1   1 
ATOM   3431 C CG2   . VAL A 1 459 ? 37.264 -17.100 -16.255 1.00 29.52 ? 457  VAL B CG2   1 
ATOM   3432 N N     . ILE A 1 460 ? 40.528 -15.293 -13.745 1.00 29.30 ? 458  ILE B N     1 
ATOM   3433 C CA    . ILE A 1 460 ? 41.861 -14.944 -13.172 1.00 31.31 ? 458  ILE B CA    1 
ATOM   3434 C C     . ILE A 1 460 ? 41.666 -14.885 -11.648 1.00 30.97 ? 458  ILE B C     1 
ATOM   3435 O O     . ILE A 1 460 ? 42.423 -15.561 -10.904 1.00 29.67 ? 458  ILE B O     1 
ATOM   3436 C CB    . ILE A 1 460 ? 42.451 -13.620 -13.717 1.00 34.92 ? 458  ILE B CB    1 
ATOM   3437 C CG1   . ILE A 1 460 ? 42.593 -13.544 -15.244 1.00 37.09 ? 458  ILE B CG1   1 
ATOM   3438 C CG2   . ILE A 1 460 ? 43.787 -13.323 -13.029 1.00 36.31 ? 458  ILE B CG2   1 
ATOM   3439 C CD1   . ILE A 1 460 ? 43.219 -14.742 -15.878 1.00 39.13 ? 458  ILE B CD1   1 
ATOM   3440 N N     . GLY A 1 461 ? 40.670 -14.119 -11.201 1.00 31.13 ? 459  GLY B N     1 
ATOM   3441 C CA    . GLY A 1 461 ? 40.376 -13.903 -9.770  1.00 30.90 ? 459  GLY B CA    1 
ATOM   3442 C C     . GLY A 1 461 ? 40.273 -15.204 -8.988  1.00 33.11 ? 459  GLY B C     1 
ATOM   3443 O O     . GLY A 1 461 ? 40.603 -15.173 -7.791  1.00 36.59 ? 459  GLY B O     1 
ATOM   3444 N N     . SER A 1 462 ? 39.817 -16.310 -9.595  1.00 29.93 ? 460  SER B N     1 
ATOM   3445 C CA    . SER A 1 462 ? 39.639 -17.612 -8.895  1.00 29.27 ? 460  SER B CA    1 
ATOM   3446 C C     . SER A 1 462 ? 40.728 -18.622 -9.277  1.00 27.95 ? 460  SER B C     1 
ATOM   3447 O O     . SER A 1 462 ? 40.564 -19.811 -8.909  1.00 27.63 ? 460  SER B O     1 
ATOM   3448 C CB    . SER A 1 462 ? 38.233 -18.174 -9.110  1.00 31.08 ? 460  SER B CB    1 
ATOM   3449 O OG    . SER A 1 462 ? 38.000 -18.644 -10.441 1.00 30.02 ? 460  SER B OG    1 
ATOM   3450 N N     . GLY A 1 463 ? 41.794 -18.199 -9.968  1.00 28.37 ? 461  GLY B N     1 
ATOM   3451 C CA    . GLY A 1 463 ? 42.766 -19.112 -10.612 1.00 29.70 ? 461  GLY B CA    1 
ATOM   3452 C C     . GLY A 1 463 ? 42.102 -20.189 -11.476 1.00 30.71 ? 461  GLY B C     1 
ATOM   3453 O O     . GLY A 1 463 ? 42.665 -21.300 -11.585 1.00 32.06 ? 461  GLY B O     1 
ATOM   3454 N N     . GLY A 1 464 ? 40.937 -19.902 -12.059 1.00 29.31 ? 462  GLY B N     1 
ATOM   3455 C CA    . GLY A 1 464 ? 40.176 -20.851 -12.900 1.00 31.31 ? 462  GLY B CA    1 
ATOM   3456 C C     . GLY A 1 464 ? 39.374 -21.876 -12.112 1.00 32.52 ? 462  GLY B C     1 
ATOM   3457 O O     . GLY A 1 464 ? 38.712 -22.730 -12.738 1.00 29.15 ? 462  GLY B O     1 
ATOM   3458 N N     . ALA A 1 465 ? 39.375 -21.808 -10.778 1.00 29.82 ? 463  ALA B N     1 
ATOM   3459 C CA    . ALA A 1 465 ? 38.680 -22.806 -9.935  1.00 29.02 ? 463  ALA B CA    1 
ATOM   3460 C C     . ALA A 1 465 ? 37.170 -22.783 -10.205 1.00 26.82 ? 463  ALA B C     1 
ATOM   3461 O O     . ALA A 1 465 ? 36.549 -23.866 -10.258 1.00 29.01 ? 463  ALA B O     1 
ATOM   3462 C CB    . ALA A 1 465 ? 38.967 -22.532 -8.476  1.00 30.12 ? 463  ALA B CB    1 
ATOM   3463 N N     . PHE A 1 466 ? 36.567 -21.599 -10.311 1.00 24.71 ? 464  PHE B N     1 
ATOM   3464 C CA    . PHE A 1 466 ? 35.120 -21.492 -10.599 1.00 26.82 ? 464  PHE B CA    1 
ATOM   3465 C C     . PHE A 1 466 ? 34.809 -22.243 -11.909 1.00 29.44 ? 464  PHE B C     1 
ATOM   3466 O O     . PHE A 1 466 ? 33.836 -22.989 -11.986 1.00 29.22 ? 464  PHE B O     1 
ATOM   3467 C CB    . PHE A 1 466 ? 34.693 -20.036 -10.738 1.00 28.98 ? 464  PHE B CB    1 
ATOM   3468 C CG    . PHE A 1 466 ? 34.649 -19.226 -9.472  1.00 28.62 ? 464  PHE B CG    1 
ATOM   3469 C CD1   . PHE A 1 466 ? 34.891 -19.795 -8.227  1.00 30.01 ? 464  PHE B CD1   1 
ATOM   3470 C CD2   . PHE A 1 466 ? 34.324 -17.882 -9.534  1.00 29.62 ? 464  PHE B CD2   1 
ATOM   3471 C CE1   . PHE A 1 466 ? 34.845 -19.024 -7.076  1.00 31.42 ? 464  PHE B CE1   1 
ATOM   3472 C CE2   . PHE A 1 466 ? 34.283 -17.111 -8.383  1.00 34.10 ? 464  PHE B CE2   1 
ATOM   3473 C CZ    . PHE A 1 466 ? 34.537 -17.684 -7.152  1.00 33.09 ? 464  PHE B CZ    1 
ATOM   3474 N N     . SER A 1 467 ? 35.622 -22.030 -12.938 1.00 29.20 ? 465  SER B N     1 
ATOM   3475 C CA    . SER A 1 467 ? 35.424 -22.657 -14.267 1.00 30.39 ? 465  SER B CA    1 
ATOM   3476 C C     . SER A 1 467 ? 35.536 -24.174 -14.132 1.00 29.42 ? 465  SER B C     1 
ATOM   3477 O O     . SER A 1 467 ? 34.685 -24.876 -14.689 1.00 27.42 ? 465  SER B O     1 
ATOM   3478 C CB    . SER A 1 467 ? 36.411 -22.114 -15.259 1.00 33.05 ? 465  SER B CB    1 
ATOM   3479 O OG    . SER A 1 467 ? 36.047 -20.785 -15.572 1.00 36.94 ? 465  SER B OG    1 
ATOM   3480 N N     . ARG A 1 468 ? 36.559 -24.637 -13.418 1.00 30.91 ? 466  ARG B N     1 
ATOM   3481 C CA    . ARG A 1 468 ? 36.817 -26.086 -13.185 1.00 32.48 ? 466  ARG B CA    1 
ATOM   3482 C C     . ARG A 1 468 ? 35.640 -26.705 -12.430 1.00 32.07 ? 466  ARG B C     1 
ATOM   3483 O O     . ARG A 1 468 ? 35.347 -27.873 -12.715 1.00 32.98 ? 466  ARG B O     1 
ATOM   3484 C CB    . ARG A 1 468 ? 38.159 -26.292 -12.472 1.00 36.09 ? 466  ARG B CB    1 
ATOM   3485 C CG    . ARG A 1 468 ? 39.364 -25.842 -13.296 1.00 34.98 ? 466  ARG B CG    1 
ATOM   3486 C CD    . ARG A 1 468 ? 40.680 -26.415 -12.796 1.00 38.48 ? 466  ARG B CD    1 
ATOM   3487 N NE    . ARG A 1 468 ? 40.738 -26.374 -11.338 1.00 38.19 ? 466  ARG B NE    1 
ATOM   3488 C CZ    . ARG A 1 468 ? 41.221 -25.374 -10.597 1.00 40.01 ? 466  ARG B CZ    1 
ATOM   3489 N NH1   . ARG A 1 468 ? 41.183 -25.466 -9.274  1.00 40.85 ? 466  ARG B NH1   1 
ATOM   3490 N NH2   . ARG A 1 468 ? 41.750 -24.301 -11.154 1.00 36.83 ? 466  ARG B NH2   1 
ATOM   3491 N N     . HIS A 1 469 ? 34.933 -25.953 -11.572 1.00 33.93 ? 467  HIS B N     1 
ATOM   3492 C CA    . HIS A 1 469 ? 33.685 -26.448 -10.937 1.00 37.36 ? 467  HIS B CA    1 
ATOM   3493 C C     . HIS A 1 469 ? 32.666 -26.752 -12.038 1.00 39.18 ? 467  HIS B C     1 
ATOM   3494 O O     . HIS A 1 469 ? 32.056 -27.827 -11.988 1.00 39.26 ? 467  HIS B O     1 
ATOM   3495 C CB    . HIS A 1 469 ? 33.041 -25.476 -9.937  1.00 40.34 ? 467  HIS B CB    1 
ATOM   3496 C CG    . HIS A 1 469 ? 33.907 -25.115 -8.780  1.00 49.20 ? 467  HIS B CG    1 
ATOM   3497 N ND1   . HIS A 1 469 ? 35.048 -25.839 -8.462  1.00 49.52 ? 467  HIS B ND1   1 
ATOM   3498 C CD2   . HIS A 1 469 ? 33.811 -24.109 -7.873  1.00 49.35 ? 467  HIS B CD2   1 
ATOM   3499 C CE1   . HIS A 1 469 ? 35.623 -25.284 -7.405  1.00 54.11 ? 467  HIS B CE1   1 
ATOM   3500 N NE2   . HIS A 1 469 ? 34.881 -24.226 -7.023  1.00 48.51 ? 467  HIS B NE2   1 
ATOM   3501 N N     . PHE A 1 470 ? 32.455 -25.799 -12.951 1.00 32.97 ? 468  PHE B N     1 
ATOM   3502 C CA    . PHE A 1 470 ? 31.491 -25.932 -14.068 1.00 30.59 ? 468  PHE B CA    1 
ATOM   3503 C C     . PHE A 1 470 ? 31.934 -27.109 -14.929 1.00 29.22 ? 468  PHE B C     1 
ATOM   3504 O O     . PHE A 1 470 ? 31.120 -28.012 -15.174 1.00 32.07 ? 468  PHE B O     1 
ATOM   3505 C CB    . PHE A 1 470 ? 31.400 -24.627 -14.863 1.00 29.85 ? 468  PHE B CB    1 
ATOM   3506 C CG    . PHE A 1 470 ? 30.345 -24.603 -15.934 1.00 28.49 ? 468  PHE B CG    1 
ATOM   3507 C CD1   . PHE A 1 470 ? 29.035 -24.952 -15.640 1.00 28.50 ? 468  PHE B CD1   1 
ATOM   3508 C CD2   . PHE A 1 470 ? 30.643 -24.182 -17.216 1.00 30.17 ? 468  PHE B CD2   1 
ATOM   3509 C CE1   . PHE A 1 470 ? 28.054 -24.920 -16.608 1.00 28.24 ? 468  PHE B CE1   1 
ATOM   3510 C CE2   . PHE A 1 470 ? 29.654 -24.151 -18.191 1.00 29.15 ? 468  PHE B CE2   1 
ATOM   3511 C CZ    . PHE A 1 470 ? 28.361 -24.508 -17.883 1.00 28.78 ? 468  PHE B CZ    1 
ATOM   3512 N N     . THR A 1 471 ? 33.181 -27.093 -15.396 1.00 30.35 ? 469  THR B N     1 
ATOM   3513 C CA    . THR A 1 471 ? 33.668 -28.111 -16.372 1.00 31.62 ? 469  THR B CA    1 
ATOM   3514 C C     . THR A 1 471 ? 33.732 -29.495 -15.705 1.00 34.13 ? 469  THR B C     1 
ATOM   3515 O O     . THR A 1 471 ? 33.496 -30.492 -16.409 1.00 30.31 ? 469  THR B O     1 
ATOM   3516 C CB    . THR A 1 471 ? 34.965 -27.662 -17.050 1.00 33.69 ? 469  THR B CB    1 
ATOM   3517 O OG1   . THR A 1 471 ? 36.007 -27.485 -16.098 1.00 32.12 ? 469  THR B OG1   1 
ATOM   3518 C CG2   . THR A 1 471 ? 34.765 -26.378 -17.820 1.00 33.62 ? 469  THR B CG2   1 
ATOM   3519 N N     . ASP A 1 472 ? 33.978 -29.569 -14.392 1.00 33.49 ? 470  ASP B N     1 
ATOM   3520 C CA    . ASP A 1 472 ? 33.935 -30.857 -13.658 1.00 33.48 ? 470  ASP B CA    1 
ATOM   3521 C C     . ASP A 1 472 ? 32.556 -31.487 -13.881 1.00 32.25 ? 470  ASP B C     1 
ATOM   3522 O O     . ASP A 1 472 ? 32.503 -32.706 -14.105 1.00 31.74 ? 470  ASP B O     1 
ATOM   3523 C CB    . ASP A 1 472 ? 34.141 -30.711 -12.146 1.00 34.81 ? 470  ASP B CB    1 
ATOM   3524 C CG    . ASP A 1 472 ? 35.584 -30.628 -11.691 1.00 40.68 ? 470  ASP B CG    1 
ATOM   3525 O OD1   . ASP A 1 472 ? 36.486 -30.804 -12.545 1.00 38.02 ? 470  ASP B OD1   1 
ATOM   3526 O OD2   . ASP A 1 472 ? 35.791 -30.358 -10.464 1.00 39.60 ? 470  ASP B OD2   1 
ATOM   3527 N N     . GLU A 1 473 ? 31.490 -30.692 -13.759 1.00 28.94 ? 471  GLU B N     1 
ATOM   3528 C CA    . GLU A 1 473 ? 30.093 -31.175 -13.879 1.00 29.24 ? 471  GLU B CA    1 
ATOM   3529 C C     . GLU A 1 473 ? 29.886 -31.670 -15.315 1.00 28.61 ? 471  GLU B C     1 
ATOM   3530 O O     . GLU A 1 473 ? 29.301 -32.764 -15.503 1.00 29.29 ? 471  GLU B O     1 
ATOM   3531 C CB    . GLU A 1 473 ? 29.095 -30.083 -13.506 1.00 28.59 ? 471  GLU B CB    1 
ATOM   3532 C CG    . GLU A 1 473 ? 27.646 -30.482 -13.698 1.00 32.99 ? 471  GLU B CG    1 
ATOM   3533 C CD    . GLU A 1 473 ? 26.674 -29.366 -13.349 1.00 34.80 ? 471  GLU B CD    1 
ATOM   3534 O OE1   . GLU A 1 473 ? 25.897 -28.954 -14.226 1.00 31.29 ? 471  GLU B OE1   1 
ATOM   3535 O OE2   . GLU A 1 473 ? 26.717 -28.896 -12.195 1.00 34.83 ? 471  GLU B OE2   1 
ATOM   3536 N N     . ILE A 1 474 ? 30.353 -30.897 -16.287 1.00 28.76 ? 472  ILE B N     1 
ATOM   3537 C CA    . ILE A 1 474 ? 30.174 -31.243 -17.726 1.00 26.81 ? 472  ILE B CA    1 
ATOM   3538 C C     . ILE A 1 474 ? 30.873 -32.577 -18.011 1.00 29.83 ? 472  ILE B C     1 
ATOM   3539 O O     . ILE A 1 474 ? 30.223 -33.431 -18.642 1.00 28.43 ? 472  ILE B O     1 
ATOM   3540 C CB    . ILE A 1 474 ? 30.661 -30.119 -18.649 1.00 28.14 ? 472  ILE B CB    1 
ATOM   3541 C CG1   . ILE A 1 474 ? 29.895 -28.823 -18.394 1.00 25.40 ? 472  ILE B CG1   1 
ATOM   3542 C CG2   . ILE A 1 474 ? 30.546 -30.553 -20.098 1.00 29.26 ? 472  ILE B CG2   1 
ATOM   3543 C CD1   . ILE A 1 474 ? 30.428 -27.678 -19.206 1.00 28.14 ? 472  ILE B CD1   1 
ATOM   3544 N N     . LYS A 1 475 ? 32.115 -32.763 -17.547 1.00 29.06 ? 473  LYS B N     1 
ATOM   3545 C CA    . LYS A 1 475 ? 32.903 -33.988 -17.830 1.00 32.98 ? 473  LYS B CA    1 
ATOM   3546 C C     . LYS A 1 475 ? 32.266 -35.182 -17.132 1.00 34.25 ? 473  LYS B C     1 
ATOM   3547 O O     . LYS A 1 475 ? 32.376 -36.300 -17.697 1.00 31.69 ? 473  LYS B O     1 
ATOM   3548 C CB    . LYS A 1 475 ? 34.357 -33.890 -17.370 1.00 35.63 ? 473  LYS B CB    1 
ATOM   3549 C CG    . LYS A 1 475 ? 35.194 -32.848 -18.090 1.00 38.44 ? 473  LYS B CG    1 
ATOM   3550 C CD    . LYS A 1 475 ? 36.620 -32.774 -17.561 1.00 42.66 ? 473  LYS B CD    1 
ATOM   3551 C CE    . LYS A 1 475 ? 37.195 -31.376 -17.582 1.00 45.91 ? 473  LYS B CE    1 
ATOM   3552 N NZ    . LYS A 1 475 ? 38.594 -31.365 -17.083 1.00 46.27 ? 473  LYS B NZ    1 
ATOM   3553 N N     . ALA A 1 476 ? 31.645 -34.981 -15.962 1.00 32.52 ? 474  ALA B N     1 
ATOM   3554 C CA    . ALA A 1 476 ? 30.971 -36.096 -15.262 1.00 35.35 ? 474  ALA B CA    1 
ATOM   3555 C C     . ALA A 1 476 ? 29.771 -36.487 -16.128 1.00 33.07 ? 474  ALA B C     1 
ATOM   3556 O O     . ALA A 1 476 ? 29.526 -37.695 -16.321 1.00 31.37 ? 474  ALA B O     1 
ATOM   3557 C CB    . ALA A 1 476 ? 30.596 -35.749 -13.840 1.00 34.50 ? 474  ALA B CB    1 
ATOM   3558 N N     . PHE A 1 477 ? 29.080 -35.500 -16.686 1.00 30.44 ? 475  PHE B N     1 
ATOM   3559 C CA    . PHE A 1 477 ? 27.939 -35.751 -17.602 1.00 32.32 ? 475  PHE B CA    1 
ATOM   3560 C C     . PHE A 1 477 ? 28.441 -36.549 -18.809 1.00 30.52 ? 475  PHE B C     1 
ATOM   3561 O O     . PHE A 1 477 ? 27.818 -37.557 -19.174 1.00 31.60 ? 475  PHE B O     1 
ATOM   3562 C CB    . PHE A 1 477 ? 27.283 -34.445 -18.038 1.00 34.23 ? 475  PHE B CB    1 
ATOM   3563 C CG    . PHE A 1 477 ? 26.361 -34.577 -19.221 1.00 31.08 ? 475  PHE B CG    1 
ATOM   3564 C CD1   . PHE A 1 477 ? 25.082 -35.099 -19.077 1.00 31.52 ? 475  PHE B CD1   1 
ATOM   3565 C CD2   . PHE A 1 477 ? 26.775 -34.182 -20.485 1.00 34.07 ? 475  PHE B CD2   1 
ATOM   3566 C CE1   . PHE A 1 477 ? 24.218 -35.191 -20.161 1.00 30.09 ? 475  PHE B CE1   1 
ATOM   3567 C CE2   . PHE A 1 477 ? 25.912 -34.274 -21.570 1.00 32.67 ? 475  PHE B CE2   1 
ATOM   3568 C CZ    . PHE A 1 477 ? 24.633 -34.774 -21.406 1.00 30.79 ? 475  PHE B CZ    1 
ATOM   3569 N N     . VAL A 1 478 ? 29.561 -36.129 -19.393 1.00 30.75 ? 476  VAL B N     1 
ATOM   3570 C CA    . VAL A 1 478 ? 30.141 -36.818 -20.581 1.00 29.38 ? 476  VAL B CA    1 
ATOM   3571 C C     . VAL A 1 478 ? 30.482 -38.271 -20.221 1.00 32.50 ? 476  VAL B C     1 
ATOM   3572 O O     . VAL A 1 478 ? 30.160 -39.176 -21.022 1.00 33.10 ? 476  VAL B O     1 
ATOM   3573 C CB    . VAL A 1 478 ? 31.369 -36.089 -21.139 1.00 28.82 ? 476  VAL B CB    1 
ATOM   3574 C CG1   . VAL A 1 478 ? 32.125 -36.978 -22.133 1.00 28.53 ? 476  VAL B CG1   1 
ATOM   3575 C CG2   . VAL A 1 478 ? 30.982 -34.768 -21.771 1.00 27.31 ? 476  VAL B CG2   1 
ATOM   3576 N N     . ALA A 1 479 ? 31.124 -38.494 -19.076 1.00 34.33 ? 477  ALA B N     1 
ATOM   3577 C CA    . ALA A 1 479 ? 31.556 -39.828 -18.602 1.00 35.58 ? 477  ALA B CA    1 
ATOM   3578 C C     . ALA A 1 479 ? 30.349 -40.756 -18.501 1.00 34.19 ? 477  ALA B C     1 
ATOM   3579 O O     . ALA A 1 479 ? 30.535 -41.966 -18.634 1.00 36.77 ? 477  ALA B O     1 
ATOM   3580 C CB    . ALA A 1 479 ? 32.270 -39.708 -17.278 1.00 36.43 ? 477  ALA B CB    1 
ATOM   3581 N N     . SER A 1 480 ? 29.175 -40.210 -18.209 1.00 33.21 ? 478  SER B N     1 
ATOM   3582 C CA    . SER A 1 480 ? 27.918 -40.961 -17.948 1.00 34.13 ? 478  SER B CA    1 
ATOM   3583 C C     . SER A 1 480 ? 27.202 -41.355 -19.246 1.00 36.09 ? 478  SER B C     1 
ATOM   3584 O O     . SER A 1 480 ? 26.268 -42.171 -19.171 1.00 32.60 ? 478  SER B O     1 
ATOM   3585 C CB    . SER A 1 480 ? 26.978 -40.137 -17.094 1.00 33.64 ? 478  SER B CB    1 
ATOM   3586 O OG    . SER A 1 480 ? 26.317 -39.133 -17.881 1.00 33.17 ? 478  SER B OG    1 
ATOM   3587 N N     . ALA A 1 481 ? 27.531 -40.728 -20.376 1.00 36.12 ? 479  ALA B N     1 
ATOM   3588 C CA    . ALA A 1 481 ? 26.722 -40.804 -21.620 1.00 36.82 ? 479  ALA B CA    1 
ATOM   3589 C C     . ALA A 1 481 ? 26.778 -42.230 -22.190 1.00 35.83 ? 479  ALA B C     1 
ATOM   3590 O O     . ALA A 1 481 ? 27.892 -42.777 -22.311 1.00 33.90 ? 479  ALA B O     1 
ATOM   3591 C CB    . ALA A 1 481 ? 27.237 -39.794 -22.629 1.00 33.69 ? 479  ALA B CB    1 
ATOM   3592 N N     . ASP A 1 482 ? 25.635 -42.779 -22.591 1.00 35.73 ? 480  ASP B N     1 
ATOM   3593 C CA    . ASP A 1 482 ? 25.567 -44.037 -23.391 1.00 38.98 ? 480  ASP B CA    1 
ATOM   3594 C C     . ASP A 1 482 ? 25.925 -43.734 -24.854 1.00 39.59 ? 480  ASP B C     1 
ATOM   3595 O O     . ASP A 1 482 ? 26.210 -42.550 -25.179 1.00 34.79 ? 480  ASP B O     1 
ATOM   3596 C CB    . ASP A 1 482 ? 24.201 -44.707 -23.262 1.00 39.86 ? 480  ASP B CB    1 
ATOM   3597 C CG    . ASP A 1 482 ? 23.074 -43.899 -23.881 1.00 41.78 ? 480  ASP B CG    1 
ATOM   3598 O OD1   . ASP A 1 482 ? 23.369 -42.901 -24.581 1.00 41.85 ? 480  ASP B OD1   1 
ATOM   3599 O OD2   . ASP A 1 482 ? 21.909 -44.265 -23.649 1.00 43.53 ? 480  ASP B OD2   1 
ATOM   3600 N N     . GLU A 1 483 ? 25.903 -44.770 -25.702 1.00 43.22 ? 481  GLU B N     1 
ATOM   3601 C CA    . GLU A 1 483 ? 26.399 -44.759 -27.110 1.00 45.13 ? 481  GLU B CA    1 
ATOM   3602 C C     . GLU A 1 483 ? 25.668 -43.672 -27.907 1.00 38.49 ? 481  GLU B C     1 
ATOM   3603 O O     . GLU A 1 483 ? 26.338 -42.842 -28.517 1.00 41.45 ? 481  GLU B O     1 
ATOM   3604 C CB    . GLU A 1 483 ? 26.238 -46.147 -27.754 1.00 52.13 ? 481  GLU B CB    1 
ATOM   3605 C CG    . GLU A 1 483 ? 27.239 -47.194 -27.258 1.00 54.00 ? 481  GLU B CG    1 
ATOM   3606 C CD    . GLU A 1 483 ? 27.008 -47.757 -25.858 1.00 59.45 ? 481  GLU B CD    1 
ATOM   3607 O OE1   . GLU A 1 483 ? 25.843 -47.692 -25.358 1.00 53.58 ? 481  GLU B OE1   1 
ATOM   3608 O OE2   . GLU A 1 483 ? 27.998 -48.253 -25.249 1.00 57.46 ? 481  GLU B OE2   1 
ATOM   3609 N N     . ALA A 1 484 ? 24.337 -43.666 -27.872 1.00 37.29 ? 482  ALA B N     1 
ATOM   3610 C CA    . ALA A 1 484 ? 23.464 -42.732 -28.624 1.00 37.82 ? 482  ALA B CA    1 
ATOM   3611 C C     . ALA A 1 484 ? 23.768 -41.277 -28.236 1.00 35.31 ? 482  ALA B C     1 
ATOM   3612 O O     . ALA A 1 484 ? 23.780 -40.411 -29.125 1.00 34.01 ? 482  ALA B O     1 
ATOM   3613 C CB    . ALA A 1 484 ? 22.007 -43.075 -28.365 1.00 37.30 ? 482  ALA B CB    1 
ATOM   3614 N N     . LEU A 1 485 ? 23.961 -41.008 -26.941 1.00 34.17 ? 483  LEU B N     1 
ATOM   3615 C CA    . LEU A 1 485 ? 24.192 -39.639 -26.418 1.00 32.75 ? 483  LEU B CA    1 
ATOM   3616 C C     . LEU A 1 485 ? 25.603 -39.207 -26.811 1.00 30.95 ? 483  LEU B C     1 
ATOM   3617 O O     . LEU A 1 485 ? 25.820 -37.977 -26.971 1.00 30.46 ? 483  LEU B O     1 
ATOM   3618 C CB    . LEU A 1 485 ? 23.950 -39.590 -24.897 1.00 35.03 ? 483  LEU B CB    1 
ATOM   3619 C CG    . LEU A 1 485 ? 24.215 -38.226 -24.245 1.00 33.83 ? 483  LEU B CG    1 
ATOM   3620 C CD1   . LEU A 1 485 ? 23.373 -37.138 -24.882 1.00 33.81 ? 483  LEU B CD1   1 
ATOM   3621 C CD2   . LEU A 1 485 ? 23.963 -38.271 -22.745 1.00 37.64 ? 483  LEU B CD2   1 
ATOM   3622 N N     . GLY A 1 486 ? 26.493 -40.175 -27.077 1.00 30.97 ? 484  GLY B N     1 
ATOM   3623 C CA    . GLY A 1 486 ? 27.848 -39.927 -27.605 1.00 31.22 ? 484  GLY B CA    1 
ATOM   3624 C C     . GLY A 1 486 ? 27.869 -39.029 -28.837 1.00 32.70 ? 484  GLY B C     1 
ATOM   3625 O O     . GLY A 1 486 ? 28.859 -38.289 -29.018 1.00 32.26 ? 484  GLY B O     1 
ATOM   3626 N N     . GLU A 1 487 ? 26.844 -39.111 -29.687 1.00 33.11 ? 485  GLU B N     1 
ATOM   3627 C CA    . GLU A 1 487 ? 26.664 -38.192 -30.841 1.00 32.89 ? 485  GLU B CA    1 
ATOM   3628 C C     . GLU A 1 487 ? 26.906 -36.750 -30.360 1.00 31.71 ? 485  GLU B C     1 
ATOM   3629 O O     . GLU A 1 487 ? 27.515 -35.965 -31.094 1.00 28.21 ? 485  GLU B O     1 
ATOM   3630 C CB    . GLU A 1 487 ? 25.250 -38.315 -31.416 1.00 32.51 ? 485  GLU B CB    1 
ATOM   3631 C CG    . GLU A 1 487 ? 24.985 -37.360 -32.569 1.00 32.97 ? 485  GLU B CG    1 
ATOM   3632 C CD    . GLU A 1 487 ? 23.600 -37.400 -33.207 1.00 32.14 ? 485  GLU B CD    1 
ATOM   3633 O OE1   . GLU A 1 487 ? 22.786 -38.269 -32.823 1.00 34.45 ? 485  GLU B OE1   1 
ATOM   3634 O OE2   . GLU A 1 487 ? 23.335 -36.559 -34.095 1.00 30.59 ? 485  GLU B OE2   1 
ATOM   3635 N N     . PHE A 1 488 ? 26.421 -36.403 -29.171 1.00 30.17 ? 486  PHE B N     1 
ATOM   3636 C CA    . PHE A 1 488 ? 26.451 -35.007 -28.662 1.00 30.25 ? 486  PHE B CA    1 
ATOM   3637 C C     . PHE A 1 488 ? 27.568 -34.815 -27.640 1.00 30.97 ? 486  PHE B C     1 
ATOM   3638 O O     . PHE A 1 488 ? 28.193 -33.732 -27.647 1.00 31.15 ? 486  PHE B O     1 
ATOM   3639 C CB    . PHE A 1 488 ? 25.086 -34.668 -28.090 1.00 31.11 ? 486  PHE B CB    1 
ATOM   3640 C CG    . PHE A 1 488 ? 23.999 -34.813 -29.113 1.00 30.28 ? 486  PHE B CG    1 
ATOM   3641 C CD1   . PHE A 1 488 ? 23.832 -33.855 -30.105 1.00 32.52 ? 486  PHE B CD1   1 
ATOM   3642 C CD2   . PHE A 1 488 ? 23.177 -35.920 -29.114 1.00 27.87 ? 486  PHE B CD2   1 
ATOM   3643 C CE1   . PHE A 1 488 ? 22.835 -33.992 -31.058 1.00 30.68 ? 486  PHE B CE1   1 
ATOM   3644 C CE2   . PHE A 1 488 ? 22.179 -36.052 -30.062 1.00 30.33 ? 486  PHE B CE2   1 
ATOM   3645 C CZ    . PHE A 1 488 ? 22.013 -35.093 -31.036 1.00 32.06 ? 486  PHE B CZ    1 
ATOM   3646 N N     . SER A 1 489 ? 27.798 -35.817 -26.783 1.00 32.93 ? 487  SER B N     1 
ATOM   3647 C CA    . SER A 1 489 ? 28.735 -35.713 -25.635 1.00 34.72 ? 487  SER B CA    1 
ATOM   3648 C C     . SER A 1 489 ? 30.172 -35.638 -26.154 1.00 34.76 ? 487  SER B C     1 
ATOM   3649 O O     . SER A 1 489 ? 30.974 -34.896 -25.558 1.00 31.60 ? 487  SER B O     1 
ATOM   3650 C CB    . SER A 1 489 ? 28.532 -36.835 -24.639 1.00 35.71 ? 487  SER B CB    1 
ATOM   3651 O OG    . SER A 1 489 ? 28.844 -38.099 -25.194 1.00 34.00 ? 487  SER B OG    1 
ATOM   3652 N N     . LYS A 1 490 ? 30.458 -36.324 -27.268 1.00 32.15 ? 488  LYS B N     1 
ATOM   3653 C CA    . LYS A 1 490 ? 31.822 -36.405 -27.855 1.00 33.76 ? 488  LYS B CA    1 
ATOM   3654 C C     . LYS A 1 490 ? 32.271 -35.011 -28.307 1.00 31.33 ? 488  LYS B C     1 
ATOM   3655 O O     . LYS A 1 490 ? 33.313 -34.518 -27.868 1.00 31.72 ? 488  LYS B O     1 
ATOM   3656 C CB    . LYS A 1 490 ? 31.793 -37.489 -28.932 1.00 40.41 ? 488  LYS B CB    1 
ATOM   3657 C CG    . LYS A 1 490 ? 33.075 -37.690 -29.712 1.00 51.21 ? 488  LYS B CG    1 
ATOM   3658 C CD    . LYS A 1 490 ? 32.829 -37.950 -31.197 1.00 57.76 ? 488  LYS B CD    1 
ATOM   3659 C CE    . LYS A 1 490 ? 34.114 -38.038 -31.989 1.00 57.70 ? 488  LYS B CE    1 
ATOM   3660 N NZ    . LYS A 1 490 ? 35.046 -39.010 -31.369 1.00 59.91 ? 488  LYS B NZ    1 
ATOM   3661 N N     . PRO A 1 491 ? 31.543 -34.299 -29.199 1.00 28.66 ? 489  PRO B N     1 
ATOM   3662 C CA    . PRO A 1 491 ? 31.909 -32.918 -29.522 1.00 28.64 ? 489  PRO B CA    1 
ATOM   3663 C C     . PRO A 1 491 ? 31.801 -31.943 -28.337 1.00 27.66 ? 489  PRO B C     1 
ATOM   3664 O O     . PRO A 1 491 ? 32.523 -30.953 -28.340 1.00 26.02 ? 489  PRO B O     1 
ATOM   3665 C CB    . PRO A 1 491 ? 30.935 -32.520 -30.635 1.00 27.92 ? 489  PRO B CB    1 
ATOM   3666 C CG    . PRO A 1 491 ? 29.778 -33.454 -30.449 1.00 29.73 ? 489  PRO B CG    1 
ATOM   3667 C CD    . PRO A 1 491 ? 30.411 -34.763 -30.010 1.00 29.57 ? 489  PRO B CD    1 
ATOM   3668 N N     . LEU A 1 492 ? 30.901 -32.195 -27.380 1.00 25.90 ? 490  LEU B N     1 
ATOM   3669 C CA    . LEU A 1 492 ? 30.854 -31.401 -26.122 1.00 26.84 ? 490  LEU B CA    1 
ATOM   3670 C C     . LEU A 1 492 ? 32.191 -31.520 -25.387 1.00 24.29 ? 490  LEU B C     1 
ATOM   3671 O O     . LEU A 1 492 ? 32.760 -30.466 -25.008 1.00 25.31 ? 490  LEU B O     1 
ATOM   3672 C CB    . LEU A 1 492 ? 29.702 -31.871 -25.228 1.00 27.48 ? 490  LEU B CB    1 
ATOM   3673 C CG    . LEU A 1 492 ? 29.662 -31.277 -23.821 1.00 27.36 ? 490  LEU B CG    1 
ATOM   3674 C CD1   . LEU A 1 492 ? 29.496 -29.769 -23.869 1.00 27.62 ? 490  LEU B CD1   1 
ATOM   3675 C CD2   . LEU A 1 492 ? 28.513 -31.909 -23.026 1.00 26.31 ? 490  LEU B CD2   1 
ATOM   3676 N N     . ALA A 1 493 ? 32.699 -32.732 -25.207 1.00 24.72 ? 491  ALA B N     1 
ATOM   3677 C CA    . ALA A 1 493 ? 34.000 -32.964 -24.525 1.00 28.45 ? 491  ALA B CA    1 
ATOM   3678 C C     . ALA A 1 493 ? 35.112 -32.196 -25.253 1.00 28.51 ? 491  ALA B C     1 
ATOM   3679 O O     . ALA A 1 493 ? 36.030 -31.645 -24.594 1.00 27.07 ? 491  ALA B O     1 
ATOM   3680 C CB    . ALA A 1 493 ? 34.305 -34.440 -24.463 1.00 30.57 ? 491  ALA B CB    1 
ATOM   3681 N N     . ALA A 1 494 ? 35.064 -32.154 -26.580 1.00 27.81 ? 492  ALA B N     1 
ATOM   3682 C CA    . ALA A 1 494 ? 36.117 -31.494 -27.384 1.00 27.73 ? 492  ALA B CA    1 
ATOM   3683 C C     . ALA A 1 494 ? 35.995 -29.981 -27.170 1.00 26.69 ? 492  ALA B C     1 
ATOM   3684 O O     . ALA A 1 494 ? 37.037 -29.311 -27.059 1.00 25.71 ? 492  ALA B O     1 
ATOM   3685 C CB    . ALA A 1 494 ? 36.023 -31.889 -28.843 1.00 28.24 ? 492  ALA B CB    1 
ATOM   3686 N N     . ALA A 1 495 ? 34.770 -29.470 -27.073 1.00 24.92 ? 493  ALA B N     1 
ATOM   3687 C CA    . ALA A 1 495 ? 34.512 -28.031 -26.817 1.00 25.82 ? 493  ALA B CA    1 
ATOM   3688 C C     . ALA A 1 495 ? 35.037 -27.683 -25.422 1.00 25.08 ? 493  ALA B C     1 
ATOM   3689 O O     . ALA A 1 495 ? 35.640 -26.587 -25.262 1.00 24.90 ? 493  ALA B O     1 
ATOM   3690 C CB    . ALA A 1 495 ? 33.047 -27.702 -26.958 1.00 25.26 ? 493  ALA B CB    1 
ATOM   3691 N N     . VAL A 1 496 ? 34.859 -28.590 -24.458 1.00 26.73 ? 494  VAL B N     1 
ATOM   3692 C CA    . VAL A 1 496 ? 35.270 -28.342 -23.042 1.00 26.67 ? 494  VAL B CA    1 
ATOM   3693 C C     . VAL A 1 496 ? 36.800 -28.307 -23.015 1.00 26.95 ? 494  VAL B C     1 
ATOM   3694 O O     . VAL A 1 496 ? 37.383 -27.357 -22.428 1.00 27.78 ? 494  VAL B O     1 
ATOM   3695 C CB    . VAL A 1 496 ? 34.693 -29.388 -22.072 1.00 28.82 ? 494  VAL B CB    1 
ATOM   3696 C CG1   . VAL A 1 496 ? 35.286 -29.214 -20.676 1.00 28.49 ? 494  VAL B CG1   1 
ATOM   3697 C CG2   . VAL A 1 496 ? 33.161 -29.337 -22.008 1.00 30.04 ? 494  VAL B CG2   1 
ATOM   3698 N N     . GLU A 1 497 ? 37.426 -29.260 -23.706 1.00 26.60 ? 495  GLU B N     1 
ATOM   3699 C CA    . GLU A 1 497 ? 38.906 -29.327 -23.825 1.00 27.46 ? 495  GLU B CA    1 
ATOM   3700 C C     . GLU A 1 497 ? 39.406 -28.008 -24.423 1.00 27.76 ? 495  GLU B C     1 
ATOM   3701 O O     . GLU A 1 497 ? 40.357 -27.429 -23.887 1.00 28.62 ? 495  GLU B O     1 
ATOM   3702 C CB    . GLU A 1 497 ? 39.358 -30.535 -24.641 1.00 29.37 ? 495  GLU B CB    1 
ATOM   3703 C CG    . GLU A 1 497 ? 40.871 -30.635 -24.759 1.00 35.21 ? 495  GLU B CG    1 
ATOM   3704 C CD    . GLU A 1 497 ? 41.611 -30.650 -23.425 1.00 42.61 ? 495  GLU B CD    1 
ATOM   3705 O OE1   . GLU A 1 497 ? 42.805 -30.303 -23.392 1.00 47.14 ? 495  GLU B OE1   1 
ATOM   3706 O OE2   . GLU A 1 497 ? 40.997 -31.047 -22.415 1.00 49.01 ? 495  GLU B OE2   1 
ATOM   3707 N N     . ASN A 1 498 ? 38.767 -27.527 -25.483 1.00 28.26 ? 496  ASN B N     1 
ATOM   3708 C CA    . ASN A 1 498 ? 39.185 -26.265 -26.136 1.00 26.76 ? 496  ASN B CA    1 
ATOM   3709 C C     . ASN A 1 498 ? 39.121 -25.114 -25.128 1.00 25.29 ? 496  ASN B C     1 
ATOM   3710 O O     . ASN A 1 498 ? 40.027 -24.261 -25.109 1.00 25.71 ? 496  ASN B O     1 
ATOM   3711 C CB    . ASN A 1 498 ? 38.321 -25.951 -27.354 1.00 26.20 ? 496  ASN B CB    1 
ATOM   3712 C CG    . ASN A 1 498 ? 38.754 -24.641 -27.966 1.00 25.93 ? 496  ASN B CG    1 
ATOM   3713 O OD1   . ASN A 1 498 ? 39.830 -24.549 -28.573 1.00 26.81 ? 496  ASN B OD1   1 
ATOM   3714 N ND2   . ASN A 1 498 ? 37.960 -23.614 -27.746 1.00 24.19 ? 496  ASN B ND2   1 
ATOM   3715 N N     . LEU A 1 499 ? 38.050 -25.058 -24.350 1.00 27.99 ? 497  LEU B N     1 
ATOM   3716 C CA    . LEU A 1 499 ? 37.793 -23.932 -23.410 1.00 28.73 ? 497  LEU B CA    1 
ATOM   3717 C C     . LEU A 1 499 ? 38.845 -23.974 -22.295 1.00 28.50 ? 497  LEU B C     1 
ATOM   3718 O O     . LEU A 1 499 ? 39.395 -22.923 -21.971 1.00 26.22 ? 497  LEU B O     1 
ATOM   3719 C CB    . LEU A 1 499 ? 36.368 -24.006 -22.852 1.00 26.57 ? 497  LEU B CB    1 
ATOM   3720 C CG    . LEU A 1 499 ? 36.061 -22.979 -21.760 1.00 28.14 ? 497  LEU B CG    1 
ATOM   3721 C CD1   . LEU A 1 499 ? 36.263 -21.564 -22.255 1.00 29.53 ? 497  LEU B CD1   1 
ATOM   3722 C CD2   . LEU A 1 499 ? 34.648 -23.149 -21.229 1.00 28.22 ? 497  LEU B CD2   1 
ATOM   3723 N N     . GLU A 1 500 ? 39.132 -25.168 -21.782 1.00 29.63 ? 498  GLU B N     1 
ATOM   3724 C CA    . GLU A 1 500 ? 40.114 -25.381 -20.686 1.00 32.54 ? 498  GLU B CA    1 
ATOM   3725 C C     . GLU A 1 500 ? 41.506 -24.956 -21.153 1.00 31.23 ? 498  GLU B C     1 
ATOM   3726 O O     . GLU A 1 500 ? 42.210 -24.319 -20.369 1.00 31.16 ? 498  GLU B O     1 
ATOM   3727 C CB    . GLU A 1 500 ? 40.071 -26.836 -20.228 1.00 35.39 ? 498  GLU B CB    1 
ATOM   3728 C CG    . GLU A 1 500 ? 38.780 -27.173 -19.504 1.00 43.74 ? 498  GLU B CG    1 
ATOM   3729 C CD    . GLU A 1 500 ? 38.833 -28.403 -18.611 1.00 49.27 ? 498  GLU B CD    1 
ATOM   3730 O OE1   . GLU A 1 500 ? 38.320 -28.323 -17.469 1.00 62.08 ? 498  GLU B OE1   1 
ATOM   3731 O OE2   . GLU A 1 500 ? 39.382 -29.435 -19.051 1.00 49.44 ? 498  GLU B OE2   1 
ATOM   3732 N N     . GLU A 1 501 ? 41.871 -25.273 -22.395 1.00 29.84 ? 499  GLU B N     1 
ATOM   3733 C CA    . GLU A 1 501 ? 43.186 -24.894 -22.961 1.00 30.11 ? 499  GLU B CA    1 
ATOM   3734 C C     . GLU A 1 501 ? 43.243 -23.376 -23.117 1.00 30.26 ? 499  GLU B C     1 
ATOM   3735 O O     . GLU A 1 501 ? 44.294 -22.792 -22.833 1.00 28.44 ? 499  GLU B O     1 
ATOM   3736 C CB    . GLU A 1 501 ? 43.419 -25.606 -24.288 1.00 34.32 ? 499  GLU B CB    1 
ATOM   3737 C CG    . GLU A 1 501 ? 43.695 -27.088 -24.110 1.00 39.53 ? 499  GLU B CG    1 
ATOM   3738 C CD    . GLU A 1 501 ? 43.898 -27.863 -25.401 1.00 45.89 ? 499  GLU B CD    1 
ATOM   3739 O OE1   . GLU A 1 501 ? 43.851 -29.108 -25.347 1.00 49.71 ? 499  GLU B OE1   1 
ATOM   3740 O OE2   . GLU A 1 501 ? 44.109 -27.225 -26.461 1.00 54.08 ? 499  GLU B OE2   1 
ATOM   3741 N N     . LEU A 1 502 ? 42.156 -22.758 -23.572 1.00 28.89 ? 500  LEU B N     1 
ATOM   3742 C CA    . LEU A 1 502 ? 42.104 -21.293 -23.754 1.00 28.33 ? 500  LEU B CA    1 
ATOM   3743 C C     . LEU A 1 502 ? 42.225 -20.623 -22.377 1.00 29.25 ? 500  LEU B C     1 
ATOM   3744 O O     . LEU A 1 502 ? 42.938 -19.612 -22.259 1.00 27.84 ? 500  LEU B O     1 
ATOM   3745 C CB    . LEU A 1 502 ? 40.793 -20.938 -24.466 1.00 28.44 ? 500  LEU B CB    1 
ATOM   3746 C CG    . LEU A 1 502 ? 40.694 -19.475 -24.895 1.00 29.53 ? 500  LEU B CG    1 
ATOM   3747 C CD1   . LEU A 1 502 ? 41.804 -19.142 -25.887 1.00 30.89 ? 500  LEU B CD1   1 
ATOM   3748 C CD2   . LEU A 1 502 ? 39.322 -19.171 -25.492 1.00 27.72 ? 500  LEU B CD2   1 
ATOM   3749 N N     . THR A 1 503 ? 41.548 -21.178 -21.367 1.00 30.25 ? 501  THR B N     1 
ATOM   3750 C CA    . THR A 1 503 ? 41.594 -20.689 -19.966 1.00 29.30 ? 501  THR B CA    1 
ATOM   3751 C C     . THR A 1 503 ? 43.048 -20.730 -19.467 1.00 28.68 ? 501  THR B C     1 
ATOM   3752 O O     . THR A 1 503 ? 43.561 -19.688 -18.977 1.00 30.35 ? 501  THR B O     1 
ATOM   3753 C CB    . THR A 1 503 ? 40.594 -21.469 -19.103 1.00 31.20 ? 501  THR B CB    1 
ATOM   3754 O OG1   . THR A 1 503 ? 39.265 -21.247 -19.591 1.00 26.68 ? 501  THR B OG1   1 
ATOM   3755 C CG2   . THR A 1 503 ? 40.651 -21.058 -17.644 1.00 32.48 ? 501  THR B CG2   1 
ATOM   3756 N N     . ALA A 1 504 ? 43.716 -21.873 -19.601 1.00 28.64 ? 502  ALA B N     1 
ATOM   3757 C CA    . ALA A 1 504 ? 45.147 -22.026 -19.216 1.00 28.35 ? 502  ALA B CA    1 
ATOM   3758 C C     . ALA A 1 504 ? 46.011 -21.020 -19.993 1.00 28.25 ? 502  ALA B C     1 
ATOM   3759 O O     . ALA A 1 504 ? 46.836 -20.326 -19.373 1.00 30.98 ? 502  ALA B O     1 
ATOM   3760 C CB    . ALA A 1 504 ? 45.577 -23.458 -19.415 1.00 29.21 ? 502  ALA B CB    1 
ATOM   3761 N N     . TRP A 1 505 ? 45.781 -20.846 -21.296 1.00 26.12 ? 503  TRP B N     1 
ATOM   3762 C CA    . TRP A 1 505 ? 46.539 -19.863 -22.111 1.00 26.01 ? 503  TRP B CA    1 
ATOM   3763 C C     . TRP A 1 505 ? 46.356 -18.489 -21.476 1.00 25.01 ? 503  TRP B C     1 
ATOM   3764 O O     . TRP A 1 505 ? 47.348 -17.719 -21.377 1.00 25.28 ? 503  TRP B O     1 
ATOM   3765 C CB    . TRP A 1 505 ? 46.090 -19.861 -23.590 1.00 26.99 ? 503  TRP B CB    1 
ATOM   3766 C CG    . TRP A 1 505 ? 46.727 -18.779 -24.404 1.00 27.69 ? 503  TRP B CG    1 
ATOM   3767 C CD1   . TRP A 1 505 ? 47.895 -18.869 -25.113 1.00 28.72 ? 503  TRP B CD1   1 
ATOM   3768 C CD2   . TRP A 1 505 ? 46.269 -17.420 -24.554 1.00 27.00 ? 503  TRP B CD2   1 
ATOM   3769 N NE1   . TRP A 1 505 ? 48.186 -17.660 -25.689 1.00 29.42 ? 503  TRP B NE1   1 
ATOM   3770 C CE2   . TRP A 1 505 ? 47.208 -16.756 -25.364 1.00 28.02 ? 503  TRP B CE2   1 
ATOM   3771 C CE3   . TRP A 1 505 ? 45.159 -16.705 -24.094 1.00 28.07 ? 503  TRP B CE3   1 
ATOM   3772 C CZ2   . TRP A 1 505 ? 47.077 -15.411 -25.708 1.00 29.32 ? 503  TRP B CZ2   1 
ATOM   3773 C CZ3   . TRP A 1 505 ? 45.027 -15.376 -24.436 1.00 27.90 ? 503  TRP B CZ3   1 
ATOM   3774 C CH2   . TRP A 1 505 ? 45.986 -14.736 -25.221 1.00 27.98 ? 503  TRP B CH2   1 
ATOM   3775 N N     . LEU A 1 506 ? 45.128 -18.172 -21.072 1.00 25.10 ? 504  LEU B N     1 
ATOM   3776 C CA    . LEU A 1 506 ? 44.795 -16.798 -20.627 1.00 27.71 ? 504  LEU B CA    1 
ATOM   3777 C C     . LEU A 1 506 ? 45.398 -16.531 -19.235 1.00 26.34 ? 504  LEU B C     1 
ATOM   3778 O O     . LEU A 1 506 ? 45.933 -15.423 -19.050 1.00 28.57 ? 504  LEU B O     1 
ATOM   3779 C CB    . LEU A 1 506 ? 43.279 -16.617 -20.619 1.00 30.74 ? 504  LEU B CB    1 
ATOM   3780 C CG    . LEU A 1 506 ? 42.816 -15.266 -20.076 1.00 33.30 ? 504  LEU B CG    1 
ATOM   3781 C CD1   . LEU A 1 506 ? 43.458 -14.129 -20.839 1.00 35.20 ? 504  LEU B CD1   1 
ATOM   3782 C CD2   . LEU A 1 506 ? 41.308 -15.149 -20.110 1.00 37.17 ? 504  LEU B CD2   1 
ATOM   3783 N N     . LEU A 1 507 ? 45.282 -17.480 -18.303 1.00 26.90 ? 505  LEU B N     1 
ATOM   3784 C CA    . LEU A 1 507 ? 45.856 -17.361 -16.922 1.00 29.51 ? 505  LEU B CA    1 
ATOM   3785 C C     . LEU A 1 507 ? 47.357 -17.070 -17.046 1.00 29.56 ? 505  LEU B C     1 
ATOM   3786 O O     . LEU A 1 507 ? 47.853 -16.157 -16.350 1.00 33.07 ? 505  LEU B O     1 
ATOM   3787 C CB    . LEU A 1 507 ? 45.615 -18.641 -16.105 1.00 31.05 ? 505  LEU B CB    1 
ATOM   3788 C CG    . LEU A 1 507 ? 44.180 -18.887 -15.623 1.00 33.69 ? 505  LEU B CG    1 
ATOM   3789 C CD1   . LEU A 1 507 ? 43.975 -20.345 -15.232 1.00 33.85 ? 505  LEU B CD1   1 
ATOM   3790 C CD2   . LEU A 1 507 ? 43.812 -17.988 -14.448 1.00 33.08 ? 505  LEU B CD2   1 
ATOM   3791 N N     . ASP A 1 508 ? 48.062 -17.785 -17.926 1.00 30.45 ? 506  ASP B N     1 
ATOM   3792 C CA    . ASP A 1 508 ? 49.515 -17.568 -18.153 1.00 31.06 ? 506  ASP B CA    1 
ATOM   3793 C C     . ASP A 1 508 ? 49.756 -16.196 -18.790 1.00 31.23 ? 506  ASP B C     1 
ATOM   3794 O O     . ASP A 1 508 ? 50.627 -15.474 -18.350 1.00 27.05 ? 506  ASP B O     1 
ATOM   3795 C CB    . ASP A 1 508 ? 50.107 -18.667 -19.032 1.00 33.62 ? 506  ASP B CB    1 
ATOM   3796 C CG    . ASP A 1 508 ? 51.561 -18.413 -19.388 1.00 38.87 ? 506  ASP B CG    1 
ATOM   3797 O OD1   . ASP A 1 508 ? 52.418 -18.686 -18.529 1.00 36.34 ? 506  ASP B OD1   1 
ATOM   3798 O OD2   . ASP A 1 508 ? 51.812 -17.871 -20.497 1.00 36.79 ? 506  ASP B OD2   1 
ATOM   3799 N N     . ARG A 1 509 ? 49.023 -15.859 -19.841 1.00 30.70 ? 507  ARG B N     1 
ATOM   3800 C CA    . ARG A 1 509 ? 49.309 -14.657 -20.653 1.00 29.58 ? 507  ARG B CA    1 
ATOM   3801 C C     . ARG A 1 509 ? 49.029 -13.385 -19.849 1.00 29.05 ? 507  ARG B C     1 
ATOM   3802 O O     . ARG A 1 509 ? 49.727 -12.392 -20.075 1.00 30.16 ? 507  ARG B O     1 
ATOM   3803 C CB    . ARG A 1 509 ? 48.467 -14.722 -21.930 1.00 32.05 ? 507  ARG B CB    1 
ATOM   3804 C CG    . ARG A 1 509 ? 48.831 -13.671 -22.958 1.00 35.02 ? 507  ARG B CG    1 
ATOM   3805 C CD    . ARG A 1 509 ? 50.126 -14.017 -23.654 1.00 38.41 ? 507  ARG B CD    1 
ATOM   3806 N NE    . ARG A 1 509 ? 50.154 -13.237 -24.876 1.00 42.63 ? 507  ARG B NE    1 
ATOM   3807 C CZ    . ARG A 1 509 ? 50.515 -13.695 -26.061 1.00 47.32 ? 507  ARG B CZ    1 
ATOM   3808 N NH1   . ARG A 1 509 ? 50.901 -14.958 -26.210 1.00 44.17 ? 507  ARG B NH1   1 
ATOM   3809 N NH2   . ARG A 1 509 ? 50.473 -12.874 -27.098 1.00 51.89 ? 507  ARG B NH2   1 
ATOM   3810 N N     . ALA A 1 510 ? 48.040 -13.398 -18.952 1.00 28.41 ? 508  ALA B N     1 
ATOM   3811 C CA    . ALA A 1 510 ? 47.634 -12.209 -18.173 1.00 30.70 ? 508  ALA B CA    1 
ATOM   3812 C C     . ALA A 1 510 ? 48.700 -11.854 -17.119 1.00 30.43 ? 508  ALA B C     1 
ATOM   3813 O O     . ALA A 1 510 ? 48.714 -10.698 -16.667 1.00 31.45 ? 508  ALA B O     1 
ATOM   3814 C CB    . ALA A 1 510 ? 46.297 -12.439 -17.500 1.00 29.95 ? 508  ALA B CB    1 
ATOM   3815 N N     . LYS A 1 511 ? 49.549 -12.789 -16.724 1.00 32.23 ? 509  LYS B N     1 
ATOM   3816 C CA    . LYS A 1 511 ? 50.527 -12.545 -15.618 1.00 34.52 ? 509  LYS B CA    1 
ATOM   3817 C C     . LYS A 1 511 ? 51.438 -11.372 -15.983 1.00 31.45 ? 509  LYS B C     1 
ATOM   3818 O O     . LYS A 1 511 ? 52.157 -11.474 -16.977 1.00 29.84 ? 509  LYS B O     1 
ATOM   3819 C CB    . LYS A 1 511 ? 51.373 -13.786 -15.341 1.00 35.28 ? 509  LYS B CB    1 
ATOM   3820 C CG    . LYS A 1 511 ? 50.661 -14.874 -14.559 1.00 38.58 ? 509  LYS B CG    1 
ATOM   3821 C CD    . LYS A 1 511 ? 51.194 -16.244 -14.903 1.00 46.90 ? 509  LYS B CD    1 
ATOM   3822 C CE    . LYS A 1 511 ? 52.034 -16.891 -13.825 1.00 51.87 ? 509  LYS B CE    1 
ATOM   3823 N NZ    . LYS A 1 511 ? 51.250 -17.944 -13.140 1.00 54.57 ? 509  LYS B NZ    1 
ATOM   3824 N N     . GLY A 1 512 ? 51.368 -10.289 -15.208 1.00 35.56 ? 510  GLY B N     1 
ATOM   3825 C CA    . GLY A 1 512 ? 52.142 -9.040  -15.389 1.00 33.78 ? 510  GLY B CA    1 
ATOM   3826 C C     . GLY A 1 512 ? 51.704 -8.234  -16.603 1.00 38.31 ? 510  GLY B C     1 
ATOM   3827 O O     . GLY A 1 512 ? 52.359 -7.202  -16.860 1.00 35.72 ? 510  GLY B O     1 
ATOM   3828 N N     . ASN A 1 513 ? 50.630 -8.639  -17.315 1.00 34.97 ? 511  ASN B N     1 
ATOM   3829 C CA    . ASN A 1 513 ? 50.212 -8.028  -18.614 1.00 34.39 ? 511  ASN B CA    1 
ATOM   3830 C C     . ASN A 1 513 ? 48.725 -7.670  -18.562 1.00 33.04 ? 511  ASN B C     1 
ATOM   3831 O O     . ASN A 1 513 ? 47.903 -8.375  -19.139 1.00 30.90 ? 511  ASN B O     1 
ATOM   3832 C CB    . ASN A 1 513 ? 50.518 -8.955  -19.795 1.00 35.59 ? 511  ASN B CB    1 
ATOM   3833 C CG    . ASN A 1 513 ? 52.001 -9.210  -19.990 1.00 41.88 ? 511  ASN B CG    1 
ATOM   3834 O OD1   . ASN A 1 513 ? 52.785 -8.274  -20.110 1.00 42.22 ? 511  ASN B OD1   1 
ATOM   3835 N ND2   . ASN A 1 513 ? 52.389 -10.475 -20.046 1.00 40.79 ? 511  ASN B ND2   1 
ATOM   3836 N N     . PRO A 1 514 ? 48.337 -6.590  -17.846 1.00 31.72 ? 512  PRO B N     1 
ATOM   3837 C CA    . PRO A 1 514 ? 46.925 -6.263  -17.630 1.00 34.08 ? 512  PRO B CA    1 
ATOM   3838 C C     . PRO A 1 514 ? 46.083 -6.086  -18.918 1.00 30.03 ? 512  PRO B C     1 
ATOM   3839 O O     . PRO A 1 514 ? 44.886 -6.304  -18.862 1.00 28.53 ? 512  PRO B O     1 
ATOM   3840 C CB    . PRO A 1 514 ? 46.969 -4.922  -16.871 1.00 34.31 ? 512  PRO B CB    1 
ATOM   3841 C CG    . PRO A 1 514 ? 48.343 -4.879  -16.223 1.00 37.47 ? 512  PRO B CG    1 
ATOM   3842 C CD    . PRO A 1 514 ? 49.244 -5.648  -17.166 1.00 35.64 ? 512  PRO B CD    1 
ATOM   3843 N N     . ASN A 1 515 ? 46.690 -5.678  -20.033 1.00 26.54 ? 513  ASN B N     1 
ATOM   3844 C CA    . ASN A 1 515 ? 45.942 -5.432  -21.298 1.00 26.96 ? 513  ASN B CA    1 
ATOM   3845 C C     . ASN A 1 515 ? 45.362 -6.760  -21.819 1.00 25.76 ? 513  ASN B C     1 
ATOM   3846 O O     . ASN A 1 515 ? 44.350 -6.727  -22.531 1.00 27.57 ? 513  ASN B O     1 
ATOM   3847 C CB    . ASN A 1 515 ? 46.802 -4.721  -22.342 1.00 26.38 ? 513  ASN B CB    1 
ATOM   3848 C CG    . ASN A 1 515 ? 47.027 -3.258  -22.024 1.00 27.58 ? 513  ASN B CG    1 
ATOM   3849 O OD1   . ASN A 1 515 ? 46.364 -2.693  -21.153 1.00 27.76 ? 513  ASN B OD1   1 
ATOM   3850 N ND2   . ASN A 1 515 ? 47.913 -2.620  -22.772 1.00 26.90 ? 513  ASN B ND2   1 
ATOM   3851 N N     . GLU A 1 516 ? 45.965 -7.895  -21.484 1.00 25.30 ? 514  GLU B N     1 
ATOM   3852 C CA    . GLU A 1 516 ? 45.568 -9.208  -22.035 1.00 27.09 ? 514  GLU B CA    1 
ATOM   3853 C C     . GLU A 1 516 ? 44.155 -9.562  -21.562 1.00 30.11 ? 514  GLU B C     1 
ATOM   3854 O O     . GLU A 1 516 ? 43.474 -10.358 -22.247 1.00 27.60 ? 514  GLU B O     1 
ATOM   3855 C CB    . GLU A 1 516 ? 46.574 -10.288 -21.638 1.00 29.17 ? 514  GLU B CB    1 
ATOM   3856 C CG    . GLU A 1 516 ? 47.969 -10.069 -22.234 1.00 30.55 ? 514  GLU B CG    1 
ATOM   3857 C CD    . GLU A 1 516 ? 48.086 -10.215 -23.746 1.00 31.75 ? 514  GLU B CD    1 
ATOM   3858 O OE1   . GLU A 1 516 ? 47.096 -10.594 -24.400 1.00 29.01 ? 514  GLU B OE1   1 
ATOM   3859 O OE2   . GLU A 1 516 ? 49.186 -10.000 -24.260 1.00 30.11 ? 514  GLU B OE2   1 
ATOM   3860 N N     . ILE A 1 517 ? 43.747 -9.064  -20.395 1.00 27.68 ? 515  ILE B N     1 
ATOM   3861 C CA    . ILE A 1 517 ? 42.468 -9.501  -19.776 1.00 27.64 ? 515  ILE B CA    1 
ATOM   3862 C C     . ILE A 1 517 ? 41.339 -8.907  -20.618 1.00 25.46 ? 515  ILE B C     1 
ATOM   3863 O O     . ILE A 1 517 ? 40.517 -9.677  -21.131 1.00 26.03 ? 515  ILE B O     1 
ATOM   3864 C CB    . ILE A 1 517 ? 42.401 -9.113  -18.277 1.00 28.93 ? 515  ILE B CB    1 
ATOM   3865 C CG1   . ILE A 1 517 ? 43.599 -9.678  -17.499 1.00 32.45 ? 515  ILE B CG1   1 
ATOM   3866 C CG2   . ILE A 1 517 ? 41.088 -9.561  -17.682 1.00 29.11 ? 515  ILE B CG2   1 
ATOM   3867 C CD1   . ILE A 1 517 ? 43.670 -9.268  -16.020 1.00 33.18 ? 515  ILE B CD1   1 
ATOM   3868 N N     . GLY A 1 518 ? 41.331 -7.585  -20.790 1.00 23.07 ? 516  GLY B N     1 
ATOM   3869 C CA    . GLY A 1 518 ? 40.309 -6.890  -21.583 1.00 23.01 ? 516  GLY B CA    1 
ATOM   3870 C C     . GLY A 1 518 ? 40.350 -7.282  -23.053 1.00 23.63 ? 516  GLY B C     1 
ATOM   3871 O O     . GLY A 1 518 ? 39.260 -7.341  -23.665 1.00 21.16 ? 516  GLY B O     1 
ATOM   3872 N N     . ALA A 1 519 ? 41.543 -7.543  -23.598 1.00 22.38 ? 517  ALA B N     1 
ATOM   3873 C CA    . ALA A 1 519 ? 41.755 -7.947  -25.006 1.00 22.28 ? 517  ALA B CA    1 
ATOM   3874 C C     . ALA A 1 519 ? 41.015 -9.259  -25.275 1.00 22.48 ? 517  ALA B C     1 
ATOM   3875 O O     . ALA A 1 519 ? 40.350 -9.359  -26.323 1.00 22.72 ? 517  ALA B O     1 
ATOM   3876 C CB    . ALA A 1 519 ? 43.237 -8.101  -25.308 1.00 23.46 ? 517  ALA B CB    1 
ATOM   3877 N N     . ALA A 1 520 ? 41.113 -10.214 -24.350 1.00 22.08 ? 518  ALA B N     1 
ATOM   3878 C CA    . ALA A 1 520 ? 40.501 -11.556 -24.470 1.00 23.65 ? 518  ALA B CA    1 
ATOM   3879 C C     . ALA A 1 520 ? 38.994 -11.505 -24.198 1.00 22.64 ? 518  ALA B C     1 
ATOM   3880 O O     . ALA A 1 520 ? 38.279 -12.367 -24.687 1.00 24.76 ? 518  ALA B O     1 
ATOM   3881 C CB    . ALA A 1 520 ? 41.171 -12.515 -23.534 1.00 23.77 ? 518  ALA B CB    1 
ATOM   3882 N N     . SER A 1 521 ? 38.536 -10.522 -23.435 1.00 25.08 ? 519  SER B N     1 
ATOM   3883 C CA    . SER A 1 521 ? 37.292 -10.618 -22.626 1.00 23.79 ? 519  SER B CA    1 
ATOM   3884 C C     . SER A 1 521 ? 36.082 -11.060 -23.470 1.00 22.90 ? 519  SER B C     1 
ATOM   3885 O O     . SER A 1 521 ? 35.530 -12.138 -23.184 1.00 22.73 ? 519  SER B O     1 
ATOM   3886 C CB    . SER A 1 521 ? 37.041 -9.337  -21.859 1.00 24.09 ? 519  SER B CB    1 
ATOM   3887 O OG    . SER A 1 521 ? 37.002 -8.196  -22.675 1.00 23.10 ? 519  SER B OG    1 
ATOM   3888 N N     . VAL A 1 522 ? 35.656 -10.254 -24.437 1.00 24.12 ? 520  VAL B N     1 
ATOM   3889 C CA    . VAL A 1 522 ? 34.342 -10.457 -25.122 1.00 22.11 ? 520  VAL B CA    1 
ATOM   3890 C C     . VAL A 1 522 ? 34.401 -11.762 -25.916 1.00 21.92 ? 520  VAL B C     1 
ATOM   3891 O O     . VAL A 1 522 ? 33.458 -12.560 -25.844 1.00 22.58 ? 520  VAL B O     1 
ATOM   3892 C CB    . VAL A 1 522 ? 33.976 -9.255  -25.999 1.00 23.34 ? 520  VAL B CB    1 
ATOM   3893 C CG1   . VAL A 1 522 ? 32.838 -9.568  -26.974 1.00 22.38 ? 520  VAL B CG1   1 
ATOM   3894 C CG2   . VAL A 1 522 ? 33.651 -8.049  -25.145 1.00 23.59 ? 520  VAL B CG2   1 
ATOM   3895 N N     . GLU A 1 523 ? 35.475 -11.990 -26.661 1.00 22.50 ? 521  GLU B N     1 
ATOM   3896 C CA    . GLU A 1 523 ? 35.515 -13.184 -27.533 1.00 22.51 ? 521  GLU B CA    1 
ATOM   3897 C C     . GLU A 1 523 ? 35.638 -14.432 -26.662 1.00 21.67 ? 521  GLU B C     1 
ATOM   3898 O O     . GLU A 1 523 ? 35.086 -15.491 -27.053 1.00 20.29 ? 521  GLU B O     1 
ATOM   3899 C CB    . GLU A 1 523 ? 36.606 -12.999 -28.592 1.00 25.70 ? 521  GLU B CB    1 
ATOM   3900 C CG    . GLU A 1 523 ? 36.155 -12.067 -29.728 1.00 26.06 ? 521  GLU B CG    1 
ATOM   3901 C CD    . GLU A 1 523 ? 37.253 -11.655 -30.695 1.00 28.01 ? 521  GLU B CD    1 
ATOM   3902 O OE1   . GLU A 1 523 ? 38.404 -11.579 -30.252 1.00 30.28 ? 521  GLU B OE1   1 
ATOM   3903 O OE2   . GLU A 1 523 ? 36.955 -11.432 -31.884 1.00 27.65 ? 521  GLU B OE2   1 
ATOM   3904 N N     . TYR A 1 524 ? 36.360 -14.351 -25.536 1.00 22.40 ? 522  TYR B N     1 
ATOM   3905 C CA    . TYR A 1 524 ? 36.491 -15.489 -24.594 1.00 21.51 ? 522  TYR B CA    1 
ATOM   3906 C C     . TYR A 1 524 ? 35.109 -15.809 -24.038 1.00 20.79 ? 522  TYR B C     1 
ATOM   3907 O O     . TYR A 1 524 ? 34.751 -16.995 -23.969 1.00 19.89 ? 522  TYR B O     1 
ATOM   3908 C CB    . TYR A 1 524 ? 37.475 -15.165 -23.467 1.00 24.48 ? 522  TYR B CB    1 
ATOM   3909 C CG    . TYR A 1 524 ? 37.580 -16.229 -22.416 1.00 24.02 ? 522  TYR B CG    1 
ATOM   3910 C CD1   . TYR A 1 524 ? 36.720 -16.232 -21.338 1.00 25.09 ? 522  TYR B CD1   1 
ATOM   3911 C CD2   . TYR A 1 524 ? 38.551 -17.218 -22.477 1.00 24.47 ? 522  TYR B CD2   1 
ATOM   3912 C CE1   . TYR A 1 524 ? 36.785 -17.215 -20.370 1.00 25.35 ? 522  TYR B CE1   1 
ATOM   3913 C CE2   . TYR A 1 524 ? 38.641 -18.203 -21.509 1.00 25.68 ? 522  TYR B CE2   1 
ATOM   3914 C CZ    . TYR A 1 524 ? 37.760 -18.187 -20.441 1.00 25.89 ? 522  TYR B CZ    1 
ATOM   3915 O OH    . TYR A 1 524 ? 37.819 -19.129 -19.458 1.00 27.21 ? 522  TYR B OH    1 
ATOM   3916 N N     . LEU A 1 525 ? 34.360 -14.781 -23.658 1.00 20.24 ? 523  LEU B N     1 
ATOM   3917 C CA    . LEU A 1 525 ? 32.984 -14.973 -23.127 1.00 21.37 ? 523  LEU B CA    1 
ATOM   3918 C C     . LEU A 1 525 ? 32.128 -15.661 -24.198 1.00 22.58 ? 523  LEU B C     1 
ATOM   3919 O O     . LEU A 1 525 ? 31.315 -16.525 -23.821 1.00 22.73 ? 523  LEU B O     1 
ATOM   3920 C CB    . LEU A 1 525 ? 32.393 -13.631 -22.680 1.00 21.26 ? 523  LEU B CB    1 
ATOM   3921 C CG    . LEU A 1 525 ? 30.981 -13.702 -22.085 1.00 22.00 ? 523  LEU B CG    1 
ATOM   3922 C CD1   . LEU A 1 525 ? 30.754 -12.623 -21.030 1.00 20.80 ? 523  LEU B CD1   1 
ATOM   3923 C CD2   . LEU A 1 525 ? 29.917 -13.577 -23.161 1.00 24.28 ? 523  LEU B CD2   1 
ATOM   3924 N N     . HIS A 1 526 ? 32.308 -15.338 -25.486 1.00 22.57 ? 524  HIS B N     1 
ATOM   3925 C CA    . HIS A 1 526 ? 31.544 -16.043 -26.559 1.00 23.10 ? 524  HIS B CA    1 
ATOM   3926 C C     . HIS A 1 526 ? 31.977 -17.511 -26.627 1.00 23.37 ? 524  HIS B C     1 
ATOM   3927 O O     . HIS A 1 526 ? 31.084 -18.388 -26.733 1.00 22.52 ? 524  HIS B O     1 
ATOM   3928 C CB    . HIS A 1 526 ? 31.657 -15.339 -27.916 1.00 24.09 ? 524  HIS B CB    1 
ATOM   3929 C CG    . HIS A 1 526 ? 30.749 -14.160 -28.040 1.00 24.91 ? 524  HIS B CG    1 
ATOM   3930 N ND1   . HIS A 1 526 ? 29.994 -13.921 -29.187 1.00 25.10 ? 524  HIS B ND1   1 
ATOM   3931 C CD2   . HIS A 1 526 ? 30.438 -13.180 -27.158 1.00 25.03 ? 524  HIS B CD2   1 
ATOM   3932 C CE1   . HIS A 1 526 ? 29.294 -12.813 -29.011 1.00 26.14 ? 524  HIS B CE1   1 
ATOM   3933 N NE2   . HIS A 1 526 ? 29.541 -12.348 -27.759 1.00 26.47 ? 524  HIS B NE2   1 
ATOM   3934 N N     . VAL A 1 527 ? 33.271 -17.804 -26.506 1.00 22.70 ? 525  VAL B N     1 
ATOM   3935 C CA    . VAL A 1 527 ? 33.726 -19.229 -26.543 1.00 23.38 ? 525  VAL B CA    1 
ATOM   3936 C C     . VAL A 1 527 ? 33.043 -19.968 -25.395 1.00 23.45 ? 525  VAL B C     1 
ATOM   3937 O O     . VAL A 1 527 ? 32.542 -21.132 -25.566 1.00 23.35 ? 525  VAL B O     1 
ATOM   3938 C CB    . VAL A 1 527 ? 35.252 -19.389 -26.441 1.00 23.18 ? 525  VAL B CB    1 
ATOM   3939 C CG1   . VAL A 1 527 ? 35.648 -20.868 -26.314 1.00 24.65 ? 525  VAL B CG1   1 
ATOM   3940 C CG2   . VAL A 1 527 ? 35.966 -18.729 -27.601 1.00 27.46 ? 525  VAL B CG2   1 
ATOM   3941 N N     . PHE A 1 528 ? 33.121 -19.368 -24.217 1.00 24.49 ? 526  PHE B N     1 
ATOM   3942 C CA    . PHE A 1 528 ? 32.458 -19.909 -23.002 1.00 24.88 ? 526  PHE B CA    1 
ATOM   3943 C C     . PHE A 1 528 ? 30.973 -20.133 -23.323 1.00 23.56 ? 526  PHE B C     1 
ATOM   3944 O O     . PHE A 1 528 ? 30.456 -21.271 -23.102 1.00 25.76 ? 526  PHE B O     1 
ATOM   3945 C CB    . PHE A 1 528 ? 32.701 -18.970 -21.819 1.00 26.23 ? 526  PHE B CB    1 
ATOM   3946 C CG    . PHE A 1 528 ? 32.335 -19.578 -20.503 1.00 27.10 ? 526  PHE B CG    1 
ATOM   3947 C CD1   . PHE A 1 528 ? 31.012 -19.879 -20.217 1.00 29.28 ? 526  PHE B CD1   1 
ATOM   3948 C CD2   . PHE A 1 528 ? 33.308 -19.874 -19.565 1.00 29.90 ? 526  PHE B CD2   1 
ATOM   3949 C CE1   . PHE A 1 528 ? 30.669 -20.441 -19.004 1.00 28.46 ? 526  PHE B CE1   1 
ATOM   3950 C CE2   . PHE A 1 528 ? 32.960 -20.459 -18.362 1.00 28.70 ? 526  PHE B CE2   1 
ATOM   3951 C CZ    . PHE A 1 528 ? 31.645 -20.743 -18.092 1.00 27.83 ? 526  PHE B CZ    1 
ATOM   3952 N N     . GLY A 1 529 ? 30.298 -19.098 -23.838 1.00 22.03 ? 527  GLY B N     1 
ATOM   3953 C CA    . GLY A 1 529 ? 28.870 -19.167 -24.211 1.00 21.85 ? 527  GLY B CA    1 
ATOM   3954 C C     . GLY A 1 529 ? 28.554 -20.369 -25.101 1.00 23.61 ? 527  GLY B C     1 
ATOM   3955 O O     . GLY A 1 529 ? 27.591 -21.108 -24.807 1.00 22.95 ? 527  GLY B O     1 
ATOM   3956 N N     . TYR A 1 530 ? 29.305 -20.587 -26.180 1.00 23.26 ? 528  TYR B N     1 
ATOM   3957 C CA    . TYR A 1 530 ? 28.964 -21.667 -27.143 1.00 22.84 ? 528  TYR B CA    1 
ATOM   3958 C C     . TYR A 1 530 ? 29.253 -23.015 -26.503 1.00 23.14 ? 528  TYR B C     1 
ATOM   3959 O O     . TYR A 1 530 ? 28.522 -23.966 -26.772 1.00 22.86 ? 528  TYR B O     1 
ATOM   3960 C CB    . TYR A 1 530 ? 29.732 -21.548 -28.459 1.00 22.95 ? 528  TYR B CB    1 
ATOM   3961 C CG    . TYR A 1 530 ? 29.266 -20.398 -29.309 1.00 22.62 ? 528  TYR B CG    1 
ATOM   3962 C CD1   . TYR A 1 530 ? 28.010 -20.397 -29.906 1.00 22.39 ? 528  TYR B CD1   1 
ATOM   3963 C CD2   . TYR A 1 530 ? 30.096 -19.316 -29.535 1.00 22.22 ? 528  TYR B CD2   1 
ATOM   3964 C CE1   . TYR A 1 530 ? 27.588 -19.331 -30.683 1.00 22.66 ? 528  TYR B CE1   1 
ATOM   3965 C CE2   . TYR A 1 530 ? 29.683 -18.243 -30.292 1.00 22.77 ? 528  TYR B CE2   1 
ATOM   3966 C CZ    . TYR A 1 530 ? 28.416 -18.240 -30.851 1.00 23.33 ? 528  TYR B CZ    1 
ATOM   3967 O OH    . TYR A 1 530 ? 28.044 -17.173 -31.608 1.00 22.96 ? 528  TYR B OH    1 
ATOM   3968 N N     . THR A 1 531 ? 30.236 -23.060 -25.606 1.00 23.17 ? 529  THR B N     1 
ATOM   3969 C CA    . THR A 1 531 ? 30.576 -24.288 -24.861 1.00 23.90 ? 529  THR B CA    1 
ATOM   3970 C C     . THR A 1 531 ? 29.435 -24.586 -23.878 1.00 23.58 ? 529  THR B C     1 
ATOM   3971 O O     . THR A 1 531 ? 28.988 -25.755 -23.794 1.00 23.38 ? 529  THR B O     1 
ATOM   3972 C CB    . THR A 1 531 ? 31.943 -24.148 -24.186 1.00 24.83 ? 529  THR B CB    1 
ATOM   3973 O OG1   . THR A 1 531 ? 32.851 -23.605 -25.147 1.00 25.56 ? 529  THR B OG1   1 
ATOM   3974 C CG2   . THR A 1 531 ? 32.444 -25.480 -23.675 1.00 25.59 ? 529  THR B CG2   1 
ATOM   3975 N N     . ALA A 1 532 ? 28.990 -23.570 -23.149 1.00 23.46 ? 530  ALA B N     1 
ATOM   3976 C CA    . ALA A 1 532 ? 27.829 -23.676 -22.228 1.00 24.88 ? 530  ALA B CA    1 
ATOM   3977 C C     . ALA A 1 532 ? 26.573 -24.125 -22.983 1.00 22.98 ? 530  ALA B C     1 
ATOM   3978 O O     . ALA A 1 532 ? 25.874 -25.000 -22.471 1.00 22.35 ? 530  ALA B O     1 
ATOM   3979 C CB    . ALA A 1 532 ? 27.590 -22.375 -21.494 1.00 24.94 ? 530  ALA B CB    1 
ATOM   3980 N N     . TYR A 1 533 ? 26.287 -23.550 -24.153 1.00 24.05 ? 531  TYR B N     1 
ATOM   3981 C CA    . TYR A 1 533 ? 25.121 -23.947 -24.987 1.00 22.69 ? 531  TYR B CA    1 
ATOM   3982 C C     . TYR A 1 533 ? 25.260 -25.410 -25.439 1.00 23.71 ? 531  TYR B C     1 
ATOM   3983 O O     . TYR A 1 533 ? 24.246 -26.093 -25.469 1.00 22.90 ? 531  TYR B O     1 
ATOM   3984 C CB    . TYR A 1 533 ? 24.927 -22.980 -26.156 1.00 22.33 ? 531  TYR B CB    1 
ATOM   3985 C CG    . TYR A 1 533 ? 24.212 -21.694 -25.799 1.00 23.77 ? 531  TYR B CG    1 
ATOM   3986 C CD1   . TYR A 1 533 ? 24.246 -21.163 -24.515 1.00 23.80 ? 531  TYR B CD1   1 
ATOM   3987 C CD2   . TYR A 1 533 ? 23.509 -20.997 -26.763 1.00 23.19 ? 531  TYR B CD2   1 
ATOM   3988 C CE1   . TYR A 1 533 ? 23.627 -19.954 -24.224 1.00 24.65 ? 531  TYR B CE1   1 
ATOM   3989 C CE2   . TYR A 1 533 ? 22.892 -19.796 -26.493 1.00 21.84 ? 531  TYR B CE2   1 
ATOM   3990 C CZ    . TYR A 1 533 ? 22.931 -19.280 -25.212 1.00 23.87 ? 531  TYR B CZ    1 
ATOM   3991 O OH    . TYR A 1 533 ? 22.322 -18.082 -24.991 1.00 22.04 ? 531  TYR B OH    1 
ATOM   3992 N N     . ALA A 1 534 ? 26.471 -25.883 -25.745 1.00 24.41 ? 532  ALA B N     1 
ATOM   3993 C CA    . ALA A 1 534 ? 26.743 -27.287 -26.135 1.00 23.76 ? 532  ALA B CA    1 
ATOM   3994 C C     . ALA A 1 534 ? 26.330 -28.188 -24.978 1.00 25.81 ? 532  ALA B C     1 
ATOM   3995 O O     . ALA A 1 534 ? 25.669 -29.224 -25.214 1.00 24.82 ? 532  ALA B O     1 
ATOM   3996 C CB    . ALA A 1 534 ? 28.196 -27.471 -26.475 1.00 23.71 ? 532  ALA B CB    1 
ATOM   3997 N N     . TYR A 1 535 ? 26.674 -27.774 -23.757 1.00 24.98 ? 533  TYR B N     1 
ATOM   3998 C CA    . TYR A 1 535 ? 26.267 -28.489 -22.525 1.00 24.09 ? 533  TYR B CA    1 
ATOM   3999 C C     . TYR A 1 535 ? 24.739 -28.490 -22.430 1.00 25.15 ? 533  TYR B C     1 
ATOM   4000 O O     . TYR A 1 535 ? 24.150 -29.566 -22.336 1.00 26.06 ? 533  TYR B O     1 
ATOM   4001 C CB    . TYR A 1 535 ? 26.966 -27.907 -21.297 1.00 24.95 ? 533  TYR B CB    1 
ATOM   4002 C CG    . TYR A 1 535 ? 26.605 -28.570 -19.992 1.00 26.69 ? 533  TYR B CG    1 
ATOM   4003 C CD1   . TYR A 1 535 ? 26.431 -29.947 -19.903 1.00 25.97 ? 533  TYR B CD1   1 
ATOM   4004 C CD2   . TYR A 1 535 ? 26.507 -27.822 -18.830 1.00 26.43 ? 533  TYR B CD2   1 
ATOM   4005 C CE1   . TYR A 1 535 ? 26.089 -30.546 -18.704 1.00 28.79 ? 533  TYR B CE1   1 
ATOM   4006 C CE2   . TYR A 1 535 ? 26.210 -28.410 -17.607 1.00 28.82 ? 533  TYR B CE2   1 
ATOM   4007 C CZ    . TYR A 1 535 ? 25.979 -29.778 -17.551 1.00 29.63 ? 533  TYR B CZ    1 
ATOM   4008 O OH    . TYR A 1 535 ? 25.662 -30.374 -16.368 1.00 26.20 ? 533  TYR B OH    1 
ATOM   4009 N N     . MET A 1 536 ? 24.097 -27.324 -22.521 1.00 23.69 ? 534  MET B N     1 
ATOM   4010 C CA    . MET A 1 536 ? 22.618 -27.267 -22.498 1.00 22.58 ? 534  MET B CA    1 
ATOM   4011 C C     . MET A 1 536 ? 22.030 -28.184 -23.584 1.00 23.90 ? 534  MET B C     1 
ATOM   4012 O O     . MET A 1 536 ? 21.022 -28.895 -23.302 1.00 25.37 ? 534  MET B O     1 
ATOM   4013 C CB    . MET A 1 536 ? 22.121 -25.839 -22.687 1.00 22.61 ? 534  MET B CB    1 
ATOM   4014 C CG    . MET A 1 536 ? 22.625 -24.855 -21.659 1.00 24.39 ? 534  MET B CG    1 
ATOM   4015 S SD    . MET A 1 536 ? 22.176 -25.253 -19.942 1.00 26.18 ? 534  MET B SD    1 
ATOM   4016 C CE    . MET A 1 536 ? 23.712 -25.945 -19.352 1.00 25.33 ? 534  MET B CE    1 
ATOM   4017 N N     . TRP A 1 537 ? 22.572 -28.150 -24.800 1.00 22.12 ? 535  TRP B N     1 
ATOM   4018 C CA    . TRP A 1 537 ? 22.004 -28.905 -25.940 1.00 22.55 ? 535  TRP B CA    1 
ATOM   4019 C C     . TRP A 1 537 ? 22.178 -30.414 -25.725 1.00 22.94 ? 535  TRP B C     1 
ATOM   4020 O O     . TRP A 1 537 ? 21.244 -31.137 -26.046 1.00 25.26 ? 535  TRP B O     1 
ATOM   4021 C CB    . TRP A 1 537 ? 22.597 -28.394 -27.267 1.00 23.42 ? 535  TRP B CB    1 
ATOM   4022 C CG    . TRP A 1 537 ? 21.762 -27.271 -27.795 1.00 22.97 ? 535  TRP B CG    1 
ATOM   4023 C CD1   . TRP A 1 537 ? 22.078 -25.949 -27.944 1.00 22.21 ? 535  TRP B CD1   1 
ATOM   4024 C CD2   . TRP A 1 537 ? 20.392 -27.405 -28.193 1.00 22.87 ? 535  TRP B CD2   1 
ATOM   4025 N NE1   . TRP A 1 537 ? 20.988 -25.260 -28.419 1.00 22.48 ? 535  TRP B NE1   1 
ATOM   4026 C CE2   . TRP A 1 537 ? 19.939 -26.126 -28.559 1.00 20.67 ? 535  TRP B CE2   1 
ATOM   4027 C CE3   . TRP A 1 537 ? 19.506 -28.491 -28.251 1.00 24.14 ? 535  TRP B CE3   1 
ATOM   4028 C CZ2   . TRP A 1 537 ? 18.644 -25.913 -28.999 1.00 22.79 ? 535  TRP B CZ2   1 
ATOM   4029 C CZ3   . TRP A 1 537 ? 18.232 -28.275 -28.709 1.00 22.26 ? 535  TRP B CZ3   1 
ATOM   4030 C CH2   . TRP A 1 537 ? 17.801 -26.999 -29.041 1.00 22.47 ? 535  TRP B CH2   1 
ATOM   4031 N N     . ALA A 1 538 ? 23.297 -30.867 -25.166 1.00 23.79 ? 536  ALA B N     1 
ATOM   4032 C CA    . ALA A 1 538 ? 23.536 -32.294 -24.850 1.00 24.76 ? 536  ALA B CA    1 
ATOM   4033 C C     . ALA A 1 538 ? 22.564 -32.749 -23.742 1.00 28.23 ? 536  ALA B C     1 
ATOM   4034 O O     . ALA A 1 538 ? 22.014 -33.882 -23.842 1.00 27.71 ? 536  ALA B O     1 
ATOM   4035 C CB    . ALA A 1 538 ? 24.985 -32.522 -24.493 1.00 24.82 ? 536  ALA B CB    1 
ATOM   4036 N N     . LEU A 1 539 ? 22.266 -31.891 -22.762 1.00 27.46 ? 537  LEU B N     1 
ATOM   4037 C CA    . LEU A 1 539 ? 21.303 -32.240 -21.687 1.00 27.81 ? 537  LEU B CA    1 
ATOM   4038 C C     . LEU A 1 539 ? 19.916 -32.401 -22.320 1.00 28.00 ? 537  LEU B C     1 
ATOM   4039 O O     . LEU A 1 539 ? 19.193 -33.348 -21.962 1.00 27.84 ? 537  LEU B O     1 
ATOM   4040 C CB    . LEU A 1 539 ? 21.283 -31.143 -20.620 1.00 27.16 ? 537  LEU B CB    1 
ATOM   4041 C CG    . LEU A 1 539 ? 22.487 -31.088 -19.684 1.00 27.09 ? 537  LEU B CG    1 
ATOM   4042 C CD1   . LEU A 1 539 ? 22.487 -29.775 -18.923 1.00 27.13 ? 537  LEU B CD1   1 
ATOM   4043 C CD2   . LEU A 1 539 ? 22.481 -32.258 -18.705 1.00 28.29 ? 537  LEU B CD2   1 
ATOM   4044 N N     . MET A 1 540 ? 19.532 -31.482 -23.200 1.00 26.41 ? 538  MET B N     1 
ATOM   4045 C CA    . MET A 1 540 ? 18.204 -31.558 -23.867 1.00 26.01 ? 538  MET B CA    1 
ATOM   4046 C C     . MET A 1 540 ? 18.167 -32.793 -24.783 1.00 28.10 ? 538  MET B C     1 
ATOM   4047 O O     . MET A 1 540 ? 17.113 -33.473 -24.853 1.00 26.75 ? 538  MET B O     1 
ATOM   4048 C CB    . MET A 1 540 ? 17.904 -30.264 -24.633 1.00 25.80 ? 538  MET B CB    1 
ATOM   4049 C CG    . MET A 1 540 ? 17.717 -29.117 -23.679 1.00 25.49 ? 538  MET B CG    1 
ATOM   4050 S SD    . MET A 1 540 ? 16.906 -27.641 -24.256 1.00 27.30 ? 538  MET B SD    1 
ATOM   4051 C CE    . MET A 1 540 ? 18.294 -26.881 -25.109 1.00 25.72 ? 538  MET B CE    1 
ATOM   4052 N N     . ALA A 1 541 ? 19.284 -33.098 -25.440 1.00 27.50 ? 539  ALA B N     1 
ATOM   4053 C CA    . ALA A 1 541 ? 19.391 -34.257 -26.342 1.00 28.72 ? 539  ALA B CA    1 
ATOM   4054 C C     . ALA A 1 541 ? 19.176 -35.543 -25.539 1.00 29.07 ? 539  ALA B C     1 
ATOM   4055 O O     . ALA A 1 541 ? 18.513 -36.461 -26.048 1.00 29.87 ? 539  ALA B O     1 
ATOM   4056 C CB    . ALA A 1 541 ? 20.723 -34.249 -27.038 1.00 30.34 ? 539  ALA B CB    1 
ATOM   4057 N N     . ARG A 1 542 ? 19.736 -35.625 -24.336 1.00 29.82 ? 540  ARG B N     1 
ATOM   4058 C CA    . ARG A 1 542 ? 19.663 -36.868 -23.527 1.00 31.16 ? 540  ARG B CA    1 
ATOM   4059 C C     . ARG A 1 542 ? 18.193 -37.157 -23.209 1.00 29.62 ? 540  ARG B C     1 
ATOM   4060 O O     . ARG A 1 542 ? 17.783 -38.306 -23.364 1.00 30.02 ? 540  ARG B O     1 
ATOM   4061 C CB    . ARG A 1 542 ? 20.485 -36.747 -22.250 1.00 31.50 ? 540  ARG B CB    1 
ATOM   4062 C CG    . ARG A 1 542 ? 20.310 -37.943 -21.319 1.00 33.87 ? 540  ARG B CG    1 
ATOM   4063 C CD    . ARG A 1 542 ? 21.276 -37.873 -20.166 1.00 33.98 ? 540  ARG B CD    1 
ATOM   4064 N NE    . ARG A 1 542 ? 20.944 -36.765 -19.288 1.00 35.00 ? 540  ARG B NE    1 
ATOM   4065 C CZ    . ARG A 1 542 ? 21.581 -36.508 -18.154 1.00 35.13 ? 540  ARG B CZ    1 
ATOM   4066 N NH1   . ARG A 1 542 ? 22.632 -37.235 -17.816 1.00 31.92 ? 540  ARG B NH1   1 
ATOM   4067 N NH2   . ARG A 1 542 ? 21.210 -35.485 -17.399 1.00 35.44 ? 540  ARG B NH2   1 
ATOM   4068 N N     . THR A 1 543 ? 17.432 -36.129 -22.847 1.00 27.81 ? 541  THR B N     1 
ATOM   4069 C CA    . THR A 1 543 ? 16.007 -36.251 -22.462 1.00 29.85 ? 541  THR B CA    1 
ATOM   4070 C C     . THR A 1 543 ? 15.195 -36.599 -23.711 1.00 32.83 ? 541  THR B C     1 
ATOM   4071 O O     . THR A 1 543 ? 14.338 -37.492 -23.644 1.00 36.87 ? 541  THR B O     1 
ATOM   4072 C CB    . THR A 1 543 ? 15.496 -34.986 -21.758 1.00 31.95 ? 541  THR B CB    1 
ATOM   4073 O OG1   . THR A 1 543 ? 16.329 -34.716 -20.633 1.00 31.83 ? 541  THR B OG1   1 
ATOM   4074 C CG2   . THR A 1 543 ? 14.074 -35.115 -21.261 1.00 30.75 ? 541  THR B CG2   1 
ATOM   4075 N N     . ALA A 1 544 ? 15.465 -35.927 -24.822 1.00 28.94 ? 542  ALA B N     1 
ATOM   4076 C CA    . ALA A 1 544 ? 14.731 -36.148 -26.082 1.00 29.02 ? 542  ALA B CA    1 
ATOM   4077 C C     . ALA A 1 544 ? 14.998 -37.576 -26.566 1.00 29.94 ? 542  ALA B C     1 
ATOM   4078 O O     . ALA A 1 544 ? 14.030 -38.209 -27.037 1.00 31.16 ? 542  ALA B O     1 
ATOM   4079 C CB    . ALA A 1 544 ? 15.125 -35.125 -27.101 1.00 27.59 ? 542  ALA B CB    1 
ATOM   4080 N N     . LEU A 1 545 ? 16.237 -38.068 -26.440 1.00 27.65 ? 543  LEU B N     1 
ATOM   4081 C CA    . LEU A 1 545 ? 16.590 -39.433 -26.913 1.00 30.18 ? 543  LEU B CA    1 
ATOM   4082 C C     . LEU A 1 545 ? 15.817 -40.443 -26.071 1.00 32.44 ? 543  LEU B C     1 
ATOM   4083 O O     . LEU A 1 545 ? 15.268 -41.371 -26.650 1.00 35.69 ? 543  LEU B O     1 
ATOM   4084 C CB    . LEU A 1 545 ? 18.089 -39.684 -26.783 1.00 31.79 ? 543  LEU B CB    1 
ATOM   4085 C CG    . LEU A 1 545 ? 18.966 -38.982 -27.809 1.00 30.74 ? 543  LEU B CG    1 
ATOM   4086 C CD1   . LEU A 1 545 ? 20.419 -39.075 -27.404 1.00 30.95 ? 543  LEU B CD1   1 
ATOM   4087 C CD2   . LEU A 1 545 ? 18.748 -39.570 -29.194 1.00 30.99 ? 543  LEU B CD2   1 
ATOM   4088 N N     . ALA A 1 546 ? 15.813 -40.249 -24.751 1.00 34.40 ? 544  ALA B N     1 
ATOM   4089 C CA    . ALA A 1 546 ? 15.114 -41.108 -23.774 1.00 35.14 ? 544  ALA B CA    1 
ATOM   4090 C C     . ALA A 1 546 ? 13.614 -41.138 -24.094 1.00 34.62 ? 544  ALA B C     1 
ATOM   4091 O O     . ALA A 1 546 ? 13.047 -42.208 -23.927 1.00 32.81 ? 544  ALA B O     1 
ATOM   4092 C CB    . ALA A 1 546 ? 15.387 -40.647 -22.362 1.00 34.04 ? 544  ALA B CB    1 
ATOM   4093 N N     . LYS A 1 547 ? 13.014 -40.037 -24.568 1.00 33.48 ? 545  LYS B N     1 
ATOM   4094 C CA    . LYS A 1 547 ? 11.538 -39.900 -24.728 1.00 36.23 ? 545  LYS B CA    1 
ATOM   4095 C C     . LYS A 1 547 ? 11.101 -39.916 -26.201 1.00 36.73 ? 545  LYS B C     1 
ATOM   4096 O O     . LYS A 1 547 ? 9.882  -39.870 -26.451 1.00 37.49 ? 545  LYS B O     1 
ATOM   4097 C CB    . LYS A 1 547 ? 11.034 -38.614 -24.065 1.00 38.58 ? 545  LYS B CB    1 
ATOM   4098 C CG    . LYS A 1 547 ? 11.176 -38.560 -22.544 1.00 41.66 ? 545  LYS B CG    1 
ATOM   4099 C CD    . LYS A 1 547 ? 10.745 -37.235 -21.940 1.00 44.30 ? 545  LYS B CD    1 
ATOM   4100 C CE    . LYS A 1 547 ? 10.327 -37.311 -20.485 1.00 46.34 ? 545  LYS B CE    1 
ATOM   4101 N NZ    . LYS A 1 547 ? 11.276 -38.141 -19.718 1.00 49.41 ? 545  LYS B NZ    1 
ATOM   4102 N N     . GLN A 1 548 ? 12.044 -39.956 -27.141 1.00 40.31 ? 546  GLN B N     1 
ATOM   4103 C CA    . GLN A 1 548 ? 11.767 -40.035 -28.602 1.00 44.42 ? 546  GLN B CA    1 
ATOM   4104 C C     . GLN A 1 548 ? 10.685 -41.091 -28.844 1.00 42.30 ? 546  GLN B C     1 
ATOM   4105 O O     . GLN A 1 548 ? 10.921 -42.249 -28.499 1.00 44.14 ? 546  GLN B O     1 
ATOM   4106 C CB    . GLN A 1 548 ? 13.050 -40.417 -29.341 1.00 44.29 ? 546  GLN B CB    1 
ATOM   4107 C CG    . GLN A 1 548 ? 12.903 -40.503 -30.848 1.00 47.04 ? 546  GLN B CG    1 
ATOM   4108 C CD    . GLN A 1 548 ? 14.121 -39.921 -31.521 1.00 45.81 ? 546  GLN B CD    1 
ATOM   4109 O OE1   . GLN A 1 548 ? 15.257 -40.279 -31.203 1.00 47.53 ? 546  GLN B OE1   1 
ATOM   4110 N NE2   . GLN A 1 548 ? 13.890 -38.993 -32.433 1.00 41.95 ? 546  GLN B NE2   1 
ATOM   4111 N N     . GLY A 1 549 ? 9.531  -40.710 -29.376 1.00 44.40 ? 547  GLY B N     1 
ATOM   4112 C CA    . GLY A 1 549 ? 8.457  -41.683 -29.641 1.00 50.09 ? 547  GLY B CA    1 
ATOM   4113 C C     . GLY A 1 549 ? 7.268  -41.042 -30.313 1.00 48.38 ? 547  GLY B C     1 
ATOM   4114 O O     . GLY A 1 549 ? 7.415  -40.594 -31.446 1.00 52.34 ? 547  GLY B O     1 
ATOM   4115 N N     . GLU A 1 550 ? 6.134  -40.985 -29.624 1.00 51.16 ? 548  GLU B N     1 
ATOM   4116 C CA    . GLU A 1 550 ? 4.838  -40.548 -30.211 1.00 55.80 ? 548  GLU B CA    1 
ATOM   4117 C C     . GLU A 1 550 ? 4.704  -39.025 -30.086 1.00 53.55 ? 548  GLU B C     1 
ATOM   4118 O O     . GLU A 1 550 ? 3.922  -38.465 -30.868 1.00 58.21 ? 548  GLU B O     1 
ATOM   4119 C CB    . GLU A 1 550 ? 3.653  -41.275 -29.562 1.00 65.71 ? 548  GLU B CB    1 
ATOM   4120 C CG    . GLU A 1 550 ? 3.858  -42.777 -29.398 1.00 73.47 ? 548  GLU B CG    1 
ATOM   4121 C CD    . GLU A 1 550 ? 4.567  -43.185 -28.111 1.00 86.52 ? 548  GLU B CD    1 
ATOM   4122 O OE1   . GLU A 1 550 ? 5.681  -43.762 -28.199 1.00 91.66 ? 548  GLU B OE1   1 
ATOM   4123 O OE2   . GLU A 1 550 ? 4.011  -42.918 -27.016 1.00 92.01 ? 548  GLU B OE2   1 
ATOM   4124 N N     . ASP A 1 551 ? 5.423  -38.377 -29.158 1.00 46.21 ? 549  ASP B N     1 
ATOM   4125 C CA    . ASP A 1 551 ? 5.435  -36.894 -29.037 1.00 43.58 ? 549  ASP B CA    1 
ATOM   4126 C C     . ASP A 1 551 ? 6.523  -36.332 -29.969 1.00 45.49 ? 549  ASP B C     1 
ATOM   4127 O O     . ASP A 1 551 ? 7.747  -36.491 -29.683 1.00 44.23 ? 549  ASP B O     1 
ATOM   4128 C CB    . ASP A 1 551 ? 5.609  -36.443 -27.587 1.00 42.90 ? 549  ASP B CB    1 
ATOM   4129 C CG    . ASP A 1 551 ? 5.380  -34.950 -27.372 1.00 44.65 ? 549  ASP B CG    1 
ATOM   4130 O OD1   . ASP A 1 551 ? 5.138  -34.233 -28.376 1.00 41.61 ? 549  ASP B OD1   1 
ATOM   4131 O OD2   . ASP A 1 551 ? 5.458  -34.499 -26.193 1.00 43.17 ? 549  ASP B OD2   1 
ATOM   4132 N N     . ASP A 1 552 ? 6.087  -35.683 -31.043 1.00 42.34 ? 550  ASP B N     1 
ATOM   4133 C CA    . ASP A 1 552 ? 6.961  -35.117 -32.103 1.00 41.98 ? 550  ASP B CA    1 
ATOM   4134 C C     . ASP A 1 552 ? 7.841  -33.993 -31.536 1.00 38.38 ? 550  ASP B C     1 
ATOM   4135 O O     . ASP A 1 552 ? 8.877  -33.687 -32.172 1.00 33.01 ? 550  ASP B O     1 
ATOM   4136 C CB    . ASP A 1 552 ? 6.131  -34.606 -33.278 1.00 45.91 ? 550  ASP B CB    1 
ATOM   4137 C CG    . ASP A 1 552 ? 6.963  -34.437 -34.539 1.00 47.16 ? 550  ASP B CG    1 
ATOM   4138 O OD1   . ASP A 1 552 ? 7.487  -35.456 -35.039 1.00 50.20 ? 550  ASP B OD1   1 
ATOM   4139 O OD2   . ASP A 1 552 ? 7.113  -33.291 -34.978 1.00 48.67 ? 550  ASP B OD2   1 
ATOM   4140 N N     . PHE A 1 553 ? 7.471  -33.404 -30.389 1.00 33.17 ? 551  PHE B N     1 
ATOM   4141 C CA    . PHE A 1 553 ? 8.305  -32.393 -29.685 1.00 31.56 ? 551  PHE B CA    1 
ATOM   4142 C C     . PHE A 1 553 ? 9.769  -32.855 -29.597 1.00 30.01 ? 551  PHE B C     1 
ATOM   4143 O O     . PHE A 1 553 ? 10.677 -32.050 -29.850 1.00 27.92 ? 551  PHE B O     1 
ATOM   4144 C CB    . PHE A 1 553 ? 7.774  -32.122 -28.285 1.00 32.44 ? 551  PHE B CB    1 
ATOM   4145 C CG    . PHE A 1 553 ? 8.583  -31.085 -27.556 1.00 28.56 ? 551  PHE B CG    1 
ATOM   4146 C CD1   . PHE A 1 553 ? 9.669  -31.460 -26.796 1.00 26.53 ? 551  PHE B CD1   1 
ATOM   4147 C CD2   . PHE A 1 553 ? 8.273  -29.737 -27.682 1.00 29.82 ? 551  PHE B CD2   1 
ATOM   4148 C CE1   . PHE A 1 553 ? 10.435 -30.504 -26.155 1.00 29.81 ? 551  PHE B CE1   1 
ATOM   4149 C CE2   . PHE A 1 553 ? 9.029  -28.784 -27.017 1.00 29.30 ? 551  PHE B CE2   1 
ATOM   4150 C CZ    . PHE A 1 553 ? 10.107 -29.171 -26.259 1.00 27.77 ? 551  PHE B CZ    1 
ATOM   4151 N N     . TYR A 1 554 ? 10.007 -34.125 -29.263 1.00 28.84 ? 552  TYR B N     1 
ATOM   4152 C CA    . TYR A 1 554 ? 11.365 -34.675 -29.025 1.00 28.92 ? 552  TYR B CA    1 
ATOM   4153 C C     . TYR A 1 554 ? 12.129 -34.763 -30.351 1.00 31.96 ? 552  TYR B C     1 
ATOM   4154 O O     . TYR A 1 554 ? 13.339 -34.441 -30.344 1.00 26.86 ? 552  TYR B O     1 
ATOM   4155 C CB    . TYR A 1 554 ? 11.271 -35.987 -28.250 1.00 29.30 ? 552  TYR B CB    1 
ATOM   4156 C CG    . TYR A 1 554 ? 10.542 -35.807 -26.938 1.00 31.20 ? 552  TYR B CG    1 
ATOM   4157 C CD1   . TYR A 1 554 ? 11.064 -35.016 -25.923 1.00 34.01 ? 552  TYR B CD1   1 
ATOM   4158 C CD2   . TYR A 1 554 ? 9.303  -36.390 -26.724 1.00 30.82 ? 552  TYR B CD2   1 
ATOM   4159 C CE1   . TYR A 1 554 ? 10.392 -34.833 -24.718 1.00 32.77 ? 552  TYR B CE1   1 
ATOM   4160 C CE2   . TYR A 1 554 ? 8.628  -36.234 -25.525 1.00 30.37 ? 552  TYR B CE2   1 
ATOM   4161 C CZ    . TYR A 1 554 ? 9.159  -35.436 -24.526 1.00 33.16 ? 552  TYR B CZ    1 
ATOM   4162 O OH    . TYR A 1 554 ? 8.459  -35.260 -23.365 1.00 34.17 ? 552  TYR B OH    1 
ATOM   4163 N N     . ALA A 1 555 ? 11.454 -35.113 -31.458 1.00 30.82 ? 553  ALA B N     1 
ATOM   4164 C CA    . ALA A 1 555 ? 12.061 -35.116 -32.811 1.00 29.46 ? 553  ALA B CA    1 
ATOM   4165 C C     . ALA A 1 555 ? 12.521 -33.694 -33.175 1.00 27.51 ? 553  ALA B C     1 
ATOM   4166 O O     . ALA A 1 555 ? 13.687 -33.525 -33.631 1.00 29.51 ? 553  ALA B O     1 
ATOM   4167 C CB    . ALA A 1 555 ? 11.099 -35.683 -33.837 1.00 30.06 ? 553  ALA B CB    1 
ATOM   4168 N N     . SER A 1 556 ? 11.657 -32.699 -33.001 1.00 27.71 ? 554  SER B N     1 
ATOM   4169 C CA    . SER A 1 556 ? 11.986 -31.263 -33.230 1.00 28.79 ? 554  SER B CA    1 
ATOM   4170 C C     . SER A 1 556 ? 13.221 -30.873 -32.405 1.00 29.73 ? 554  SER B C     1 
ATOM   4171 O O     . SER A 1 556 ? 14.147 -30.230 -32.946 1.00 26.94 ? 554  SER B O     1 
ATOM   4172 C CB    . SER A 1 556 ? 10.825 -30.385 -32.900 1.00 32.25 ? 554  SER B CB    1 
ATOM   4173 O OG    . SER A 1 556 ? 9.747  -30.638 -33.792 1.00 38.33 ? 554  SER B OG    1 
ATOM   4174 N N     . LYS A 1 557 ? 13.247 -31.260 -31.125 1.00 30.14 ? 555  LYS B N     1 
ATOM   4175 C CA    . LYS A 1 557 ? 14.332 -30.854 -30.198 1.00 27.29 ? 555  LYS B CA    1 
ATOM   4176 C C     . LYS A 1 557 ? 15.656 -31.434 -30.713 1.00 25.78 ? 555  LYS B C     1 
ATOM   4177 O O     . LYS A 1 557 ? 16.649 -30.671 -30.782 1.00 24.71 ? 555  LYS B O     1 
ATOM   4178 C CB    . LYS A 1 557 ? 13.987 -31.244 -28.754 1.00 26.24 ? 555  LYS B CB    1 
ATOM   4179 C CG    . LYS A 1 557 ? 14.990 -30.763 -27.712 1.00 27.22 ? 555  LYS B CG    1 
ATOM   4180 C CD    . LYS A 1 557 ? 15.088 -29.261 -27.545 1.00 27.12 ? 555  LYS B CD    1 
ATOM   4181 C CE    . LYS A 1 557 ? 13.829 -28.596 -27.037 1.00 29.05 ? 555  LYS B CE    1 
ATOM   4182 N NZ    . LYS A 1 557 ? 14.098 -27.215 -26.563 1.00 30.91 ? 555  LYS B NZ    1 
ATOM   4183 N N     . LEU A 1 558 ? 15.676 -32.711 -31.101 1.00 24.46 ? 556  LEU B N     1 
ATOM   4184 C CA    . LEU A 1 558 ? 16.905 -33.391 -31.575 1.00 26.82 ? 556  LEU B CA    1 
ATOM   4185 C C     . LEU A 1 558 ? 17.386 -32.796 -32.906 1.00 26.23 ? 556  LEU B C     1 
ATOM   4186 O O     . LEU A 1 558 ? 18.619 -32.648 -33.097 1.00 28.00 ? 556  LEU B O     1 
ATOM   4187 C CB    . LEU A 1 558 ? 16.620 -34.889 -31.693 1.00 28.04 ? 556  LEU B CB    1 
ATOM   4188 C CG    . LEU A 1 558 ? 16.655 -35.655 -30.372 1.00 31.23 ? 556  LEU B CG    1 
ATOM   4189 C CD1   . LEU A 1 558 ? 16.011 -37.025 -30.518 1.00 33.49 ? 556  LEU B CD1   1 
ATOM   4190 C CD2   . LEU A 1 558 ? 18.078 -35.803 -29.856 1.00 32.48 ? 556  LEU B CD2   1 
ATOM   4191 N N     . GLY A 1 559 ? 16.476 -32.494 -33.818 1.00 27.05 ? 557  GLY B N     1 
ATOM   4192 C CA    . GLY A 1 559 ? 16.839 -31.838 -35.093 1.00 27.52 ? 557  GLY B CA    1 
ATOM   4193 C C     . GLY A 1 559 ? 17.458 -30.470 -34.831 1.00 25.20 ? 557  GLY B C     1 
ATOM   4194 O O     . GLY A 1 559 ? 18.396 -30.072 -35.554 1.00 25.36 ? 557  GLY B O     1 
ATOM   4195 N N     . THR A 1 560 ? 16.970 -29.767 -33.818 1.00 24.59 ? 558  THR B N     1 
ATOM   4196 C CA    . THR A 1 560 ? 17.505 -28.433 -33.440 1.00 24.46 ? 558  THR B CA    1 
ATOM   4197 C C     . THR A 1 560 ? 18.895 -28.635 -32.817 1.00 26.60 ? 558  THR B C     1 
ATOM   4198 O O     . THR A 1 560 ? 19.831 -27.886 -33.185 1.00 26.15 ? 558  THR B O     1 
ATOM   4199 C CB    . THR A 1 560 ? 16.513 -27.661 -32.567 1.00 25.20 ? 558  THR B CB    1 
ATOM   4200 O OG1   . THR A 1 560 ? 15.187 -27.770 -33.089 1.00 22.66 ? 558  THR B OG1   1 
ATOM   4201 C CG2   . THR A 1 560 ? 16.918 -26.204 -32.471 1.00 24.37 ? 558  THR B CG2   1 
ATOM   4202 N N     . ALA A 1 561 ? 19.043 -29.630 -31.933 1.00 25.66 ? 559  ALA B N     1 
ATOM   4203 C CA    . ALA A 1 561 ? 20.327 -29.957 -31.282 1.00 24.91 ? 559  ALA B CA    1 
ATOM   4204 C C     . ALA A 1 561 ? 21.365 -30.196 -32.379 1.00 25.83 ? 559  ALA B C     1 
ATOM   4205 O O     . ALA A 1 561 ? 22.525 -29.748 -32.246 1.00 25.86 ? 559  ALA B O     1 
ATOM   4206 C CB    . ALA A 1 561 ? 20.179 -31.165 -30.390 1.00 23.90 ? 559  ALA B CB    1 
ATOM   4207 N N     . ARG A 1 562 ? 20.961 -30.942 -33.401 1.00 25.39 ? 560  ARG B N     1 
ATOM   4208 C CA    . ARG A 1 562 ? 21.867 -31.404 -34.474 1.00 25.62 ? 560  ARG B CA    1 
ATOM   4209 C C     . ARG A 1 562 ? 22.326 -30.190 -35.290 1.00 24.20 ? 560  ARG B C     1 
ATOM   4210 O O     . ARG A 1 562 ? 23.508 -30.123 -35.584 1.00 24.31 ? 560  ARG B O     1 
ATOM   4211 C CB    . ARG A 1 562 ? 21.184 -32.495 -35.297 1.00 26.55 ? 560  ARG B CB    1 
ATOM   4212 C CG    . ARG A 1 562 ? 21.348 -33.884 -34.684 1.00 28.91 ? 560  ARG B CG    1 
ATOM   4213 C CD    . ARG A 1 562 ? 20.428 -34.935 -35.269 1.00 30.66 ? 560  ARG B CD    1 
ATOM   4214 N NE    . ARG A 1 562 ? 20.580 -36.169 -34.517 1.00 30.44 ? 560  ARG B NE    1 
ATOM   4215 C CZ    . ARG A 1 562 ? 19.596 -36.984 -34.152 1.00 29.61 ? 560  ARG B CZ    1 
ATOM   4216 N NH1   . ARG A 1 562 ? 18.339 -36.723 -34.479 1.00 28.48 ? 560  ARG B NH1   1 
ATOM   4217 N NH2   . ARG A 1 562 ? 19.890 -38.066 -33.446 1.00 30.36 ? 560  ARG B NH2   1 
ATOM   4218 N N     . PHE A 1 563 ? 21.441 -29.238 -35.572 1.00 25.17 ? 561  PHE B N     1 
ATOM   4219 C CA    . PHE A 1 563 ? 21.839 -27.960 -36.210 1.00 24.99 ? 561  PHE B CA    1 
ATOM   4220 C C     . PHE A 1 563 ? 22.836 -27.227 -35.296 1.00 24.13 ? 561  PHE B C     1 
ATOM   4221 O O     . PHE A 1 563 ? 23.893 -26.770 -35.813 1.00 25.00 ? 561  PHE B O     1 
ATOM   4222 C CB    . PHE A 1 563 ? 20.632 -27.097 -36.579 1.00 24.03 ? 561  PHE B CB    1 
ATOM   4223 C CG    . PHE A 1 563 ? 21.033 -25.787 -37.205 1.00 24.74 ? 561  PHE B CG    1 
ATOM   4224 C CD1   . PHE A 1 563 ? 21.280 -25.693 -38.565 1.00 24.70 ? 561  PHE B CD1   1 
ATOM   4225 C CD2   . PHE A 1 563 ? 21.265 -24.671 -36.422 1.00 25.31 ? 561  PHE B CD2   1 
ATOM   4226 C CE1   . PHE A 1 563 ? 21.658 -24.490 -39.135 1.00 25.85 ? 561  PHE B CE1   1 
ATOM   4227 C CE2   . PHE A 1 563 ? 21.646 -23.468 -36.994 1.00 26.77 ? 561  PHE B CE2   1 
ATOM   4228 C CZ    . PHE A 1 563 ? 21.853 -23.378 -38.351 1.00 25.64 ? 561  PHE B CZ    1 
ATOM   4229 N N     . TYR A 1 564 ? 22.572 -27.125 -33.988 1.00 23.53 ? 562  TYR B N     1 
ATOM   4230 C CA    . TYR A 1 564 ? 23.484 -26.358 -33.086 1.00 21.62 ? 562  TYR B CA    1 
ATOM   4231 C C     . TYR A 1 564 ? 24.909 -26.912 -33.238 1.00 22.77 ? 562  TYR B C     1 
ATOM   4232 O O     . TYR A 1 564 ? 25.904 -26.155 -33.402 1.00 23.07 ? 562  TYR B O     1 
ATOM   4233 C CB    . TYR A 1 564 ? 23.080 -26.438 -31.605 1.00 22.65 ? 562  TYR B CB    1 
ATOM   4234 C CG    . TYR A 1 564 ? 24.050 -25.663 -30.760 1.00 21.39 ? 562  TYR B CG    1 
ATOM   4235 C CD1   . TYR A 1 564 ? 23.972 -24.280 -30.712 1.00 21.95 ? 562  TYR B CD1   1 
ATOM   4236 C CD2   . TYR A 1 564 ? 25.094 -26.282 -30.100 1.00 22.83 ? 562  TYR B CD2   1 
ATOM   4237 C CE1   . TYR A 1 564 ? 24.917 -23.534 -30.044 1.00 24.10 ? 562  TYR B CE1   1 
ATOM   4238 C CE2   . TYR A 1 564 ? 26.041 -25.547 -29.405 1.00 23.63 ? 562  TYR B CE2   1 
ATOM   4239 C CZ    . TYR A 1 564 ? 25.947 -24.168 -29.384 1.00 22.85 ? 562  TYR B CZ    1 
ATOM   4240 O OH    . TYR A 1 564 ? 26.866 -23.422 -28.730 1.00 24.35 ? 562  TYR B OH    1 
ATOM   4241 N N     . PHE A 1 565 ? 25.030 -28.234 -33.118 1.00 21.59 ? 563  PHE B N     1 
ATOM   4242 C CA    . PHE A 1 565 ? 26.325 -28.936 -33.117 1.00 24.33 ? 563  PHE B CA    1 
ATOM   4243 C C     . PHE A 1 565 ? 27.004 -28.827 -34.491 1.00 23.54 ? 563  PHE B C     1 
ATOM   4244 O O     . PHE A 1 565 ? 28.225 -28.665 -34.532 1.00 24.46 ? 563  PHE B O     1 
ATOM   4245 C CB    . PHE A 1 565 ? 26.137 -30.372 -32.621 1.00 24.32 ? 563  PHE B CB    1 
ATOM   4246 C CG    . PHE A 1 565 ? 26.247 -30.476 -31.117 1.00 26.06 ? 563  PHE B CG    1 
ATOM   4247 C CD1   . PHE A 1 565 ? 27.475 -30.677 -30.509 1.00 26.48 ? 563  PHE B CD1   1 
ATOM   4248 C CD2   . PHE A 1 565 ? 25.121 -30.376 -30.317 1.00 27.87 ? 563  PHE B CD2   1 
ATOM   4249 C CE1   . PHE A 1 565 ? 27.577 -30.766 -29.129 1.00 26.64 ? 563  PHE B CE1   1 
ATOM   4250 C CE2   . PHE A 1 565 ? 25.225 -30.481 -28.933 1.00 29.33 ? 563  PHE B CE2   1 
ATOM   4251 C CZ    . PHE A 1 565 ? 26.455 -30.666 -28.348 1.00 27.08 ? 563  PHE B CZ    1 
ATOM   4252 N N     . ALA A 1 566 ? 26.255 -28.916 -35.584 1.00 25.02 ? 564  ALA B N     1 
ATOM   4253 C CA    . ALA A 1 566 ? 26.849 -28.954 -36.945 1.00 24.50 ? 564  ALA B CA    1 
ATOM   4254 C C     . ALA A 1 566 ? 27.346 -27.552 -37.308 1.00 22.53 ? 564  ALA B C     1 
ATOM   4255 O O     . ALA A 1 566 ? 28.474 -27.417 -37.819 1.00 24.72 ? 564  ALA B O     1 
ATOM   4256 C CB    . ALA A 1 566 ? 25.847 -29.485 -37.947 1.00 24.44 ? 564  ALA B CB    1 
ATOM   4257 N N     . ARG A 1 567 ? 26.534 -26.536 -37.073 1.00 24.14 ? 565  ARG B N     1 
ATOM   4258 C CA    . ARG A 1 567 ? 26.709 -25.215 -37.726 1.00 24.93 ? 565  ARG B CA    1 
ATOM   4259 C C     . ARG A 1 567 ? 27.062 -24.098 -36.751 1.00 24.48 ? 565  ARG B C     1 
ATOM   4260 O O     . ARG A 1 567 ? 27.647 -23.105 -37.241 1.00 27.18 ? 565  ARG B O     1 
ATOM   4261 C CB    . ARG A 1 567 ? 25.434 -24.796 -38.452 1.00 25.41 ? 565  ARG B CB    1 
ATOM   4262 C CG    . ARG A 1 567 ? 24.927 -25.796 -39.477 1.00 29.70 ? 565  ARG B CG    1 
ATOM   4263 C CD    . ARG A 1 567 ? 25.654 -25.838 -40.797 1.00 29.00 ? 565  ARG B CD    1 
ATOM   4264 N NE    . ARG A 1 567 ? 25.678 -24.590 -41.571 1.00 28.54 ? 565  ARG B NE    1 
ATOM   4265 C CZ    . ARG A 1 567 ? 25.703 -24.504 -42.912 1.00 28.51 ? 565  ARG B CZ    1 
ATOM   4266 N NH1   . ARG A 1 567 ? 25.593 -25.587 -43.671 1.00 26.61 ? 565  ARG B NH1   1 
ATOM   4267 N NH2   . ARG A 1 567 ? 25.809 -23.317 -43.489 1.00 26.62 ? 565  ARG B NH2   1 
ATOM   4268 N N     . LEU A 1 568 ? 26.723 -24.186 -35.456 1.00 23.91 ? 566  LEU B N     1 
ATOM   4269 C CA    . LEU A 1 568 ? 27.024 -23.048 -34.543 1.00 23.18 ? 566  LEU B CA    1 
ATOM   4270 C C     . LEU A 1 568 ? 28.212 -23.356 -33.639 1.00 22.67 ? 566  LEU B C     1 
ATOM   4271 O O     . LEU A 1 568 ? 29.055 -22.478 -33.481 1.00 24.55 ? 566  LEU B O     1 
ATOM   4272 C CB    . LEU A 1 568 ? 25.777 -22.709 -33.738 1.00 24.80 ? 566  LEU B CB    1 
ATOM   4273 C CG    . LEU A 1 568 ? 24.556 -22.367 -34.582 1.00 24.47 ? 566  LEU B CG    1 
ATOM   4274 C CD1   . LEU A 1 568 ? 23.408 -21.926 -33.704 1.00 25.53 ? 566  LEU B CD1   1 
ATOM   4275 C CD2   . LEU A 1 568 ? 24.893 -21.301 -35.605 1.00 26.22 ? 566  LEU B CD2   1 
ATOM   4276 N N     . LEU A 1 569 ? 28.283 -24.551 -33.066 1.00 21.96 ? 567  LEU B N     1 
ATOM   4277 C CA    . LEU A 1 569 ? 29.386 -24.879 -32.126 1.00 22.17 ? 567  LEU B CA    1 
ATOM   4278 C C     . LEU A 1 569 ? 30.769 -24.602 -32.753 1.00 22.69 ? 567  LEU B C     1 
ATOM   4279 O O     . LEU A 1 569 ? 31.654 -24.195 -32.009 1.00 22.95 ? 567  LEU B O     1 
ATOM   4280 C CB    . LEU A 1 569 ? 29.270 -26.335 -31.666 1.00 21.73 ? 567  LEU B CB    1 
ATOM   4281 C CG    . LEU A 1 569 ? 30.295 -26.757 -30.616 1.00 23.09 ? 567  LEU B CG    1 
ATOM   4282 C CD1   . LEU A 1 569 ? 30.329 -25.765 -29.465 1.00 23.54 ? 567  LEU B CD1   1 
ATOM   4283 C CD2   . LEU A 1 569 ? 30.020 -28.166 -30.114 1.00 22.72 ? 567  LEU B CD2   1 
ATOM   4284 N N     . PRO A 1 570 ? 30.996 -24.817 -34.071 1.00 22.28 ? 568  PRO B N     1 
ATOM   4285 C CA    . PRO A 1 570 ? 32.311 -24.576 -34.675 1.00 21.56 ? 568  PRO B CA    1 
ATOM   4286 C C     . PRO A 1 570 ? 32.778 -23.115 -34.556 1.00 21.26 ? 568  PRO B C     1 
ATOM   4287 O O     . PRO A 1 570 ? 33.928 -22.870 -34.739 1.00 21.63 ? 568  PRO B O     1 
ATOM   4288 C CB    . PRO A 1 570 ? 32.108 -24.965 -36.140 1.00 22.80 ? 568  PRO B CB    1 
ATOM   4289 C CG    . PRO A 1 570 ? 31.006 -25.984 -36.097 1.00 23.09 ? 568  PRO B CG    1 
ATOM   4290 C CD    . PRO A 1 570 ? 30.082 -25.450 -35.028 1.00 24.13 ? 568  PRO B CD    1 
ATOM   4291 N N     . ARG A 1 571 ? 31.862 -22.215 -34.218 1.00 20.57 ? 569  ARG B N     1 
ATOM   4292 C CA    . ARG A 1 571 ? 32.220 -20.789 -34.015 1.00 20.86 ? 569  ARG B CA    1 
ATOM   4293 C C     . ARG A 1 571 ? 33.317 -20.634 -32.945 1.00 21.88 ? 569  ARG B C     1 
ATOM   4294 O O     . ARG A 1 571 ? 33.967 -19.596 -32.927 1.00 23.99 ? 569  ARG B O     1 
ATOM   4295 C CB    . ARG A 1 571 ? 30.952 -20.025 -33.642 1.00 21.58 ? 569  ARG B CB    1 
ATOM   4296 C CG    . ARG A 1 571 ? 30.013 -19.771 -34.811 1.00 22.36 ? 569  ARG B CG    1 
ATOM   4297 C CD    . ARG A 1 571 ? 28.662 -19.266 -34.350 1.00 24.05 ? 569  ARG B CD    1 
ATOM   4298 N NE    . ARG A 1 571 ? 27.823 -18.830 -35.453 1.00 24.08 ? 569  ARG B NE    1 
ATOM   4299 C CZ    . ARG A 1 571 ? 26.848 -17.938 -35.344 1.00 27.32 ? 569  ARG B CZ    1 
ATOM   4300 N NH1   . ARG A 1 571 ? 26.137 -17.600 -36.405 1.00 24.86 ? 569  ARG B NH1   1 
ATOM   4301 N NH2   . ARG A 1 571 ? 26.589 -17.382 -34.175 1.00 26.05 ? 569  ARG B NH2   1 
ATOM   4302 N N     . ILE A 1 572 ? 33.508 -21.641 -32.099 1.00 21.28 ? 570  ILE B N     1 
ATOM   4303 C CA    . ILE A 1 572 ? 34.514 -21.568 -30.999 1.00 23.04 ? 570  ILE B CA    1 
ATOM   4304 C C     . ILE A 1 572 ? 35.943 -21.445 -31.554 1.00 24.26 ? 570  ILE B C     1 
ATOM   4305 O O     . ILE A 1 572 ? 36.744 -20.766 -30.923 1.00 24.51 ? 570  ILE B O     1 
ATOM   4306 C CB    . ILE A 1 572 ? 34.366 -22.784 -30.056 1.00 22.11 ? 570  ILE B CB    1 
ATOM   4307 C CG1   . ILE A 1 572 ? 34.709 -24.105 -30.747 1.00 24.41 ? 570  ILE B CG1   1 
ATOM   4308 C CG2   . ILE A 1 572 ? 32.984 -22.815 -29.424 1.00 22.64 ? 570  ILE B CG2   1 
ATOM   4309 C CD1   . ILE A 1 572 ? 34.643 -25.301 -29.828 1.00 26.11 ? 570  ILE B CD1   1 
ATOM   4310 N N     . HIS A 1 573 ? 36.229 -22.039 -32.712 1.00 24.37 ? 571  HIS B N     1 
ATOM   4311 C CA    . HIS A 1 573 ? 37.632 -22.081 -33.214 1.00 24.25 ? 571  HIS B CA    1 
ATOM   4312 C C     . HIS A 1 573 ? 38.156 -20.689 -33.586 1.00 24.83 ? 571  HIS B C     1 
ATOM   4313 O O     . HIS A 1 573 ? 39.223 -20.319 -33.125 1.00 26.39 ? 571  HIS B O     1 
ATOM   4314 C CB    . HIS A 1 573 ? 37.723 -23.118 -34.334 1.00 26.69 ? 571  HIS B CB    1 
ATOM   4315 C CG    . HIS A 1 573 ? 37.219 -24.449 -33.893 1.00 26.48 ? 571  HIS B CG    1 
ATOM   4316 N ND1   . HIS A 1 573 ? 37.792 -25.136 -32.848 1.00 27.21 ? 571  HIS B ND1   1 
ATOM   4317 C CD2   . HIS A 1 573 ? 36.185 -25.202 -34.316 1.00 28.31 ? 571  HIS B CD2   1 
ATOM   4318 C CE1   . HIS A 1 573 ? 37.146 -26.264 -32.659 1.00 27.38 ? 571  HIS B CE1   1 
ATOM   4319 N NE2   . HIS A 1 573 ? 36.160 -26.328 -33.545 1.00 26.89 ? 571  HIS B NE2   1 
ATOM   4320 N N     . SER A 1 574 ? 37.412 -19.965 -34.407 1.00 24.78 ? 572  SER B N     1 
ATOM   4321 C CA    . SER A 1 574 ? 37.867 -18.623 -34.833 1.00 24.54 ? 572  SER B CA    1 
ATOM   4322 C C     . SER A 1 574 ? 37.963 -17.727 -33.595 1.00 24.18 ? 572  SER B C     1 
ATOM   4323 O O     . SER A 1 574 ? 38.938 -16.988 -33.477 1.00 23.42 ? 572  SER B O     1 
ATOM   4324 C CB    . SER A 1 574 ? 37.000 -18.047 -35.933 1.00 26.01 ? 572  SER B CB    1 
ATOM   4325 O OG    . SER A 1 574 ? 37.181 -18.742 -37.155 1.00 25.99 ? 572  SER B OG    1 
ATOM   4326 N N     . LEU A 1 575 ? 36.959 -17.796 -32.719 1.00 22.95 ? 573  LEU B N     1 
ATOM   4327 C CA    . LEU A 1 575 ? 37.004 -16.905 -31.522 1.00 22.70 ? 573  LEU B CA    1 
ATOM   4328 C C     . LEU A 1 575 ? 38.229 -17.257 -30.675 1.00 21.39 ? 573  LEU B C     1 
ATOM   4329 O O     . LEU A 1 575 ? 38.862 -16.336 -30.168 1.00 22.50 ? 573  LEU B O     1 
ATOM   4330 C CB    . LEU A 1 575 ? 35.696 -17.043 -30.751 1.00 22.81 ? 573  LEU B CB    1 
ATOM   4331 C CG    . LEU A 1 575 ? 34.509 -16.418 -31.463 1.00 23.10 ? 573  LEU B CG    1 
ATOM   4332 C CD1   . LEU A 1 575 ? 33.218 -16.942 -30.880 1.00 25.05 ? 573  LEU B CD1   1 
ATOM   4333 C CD2   . LEU A 1 575 ? 34.584 -14.893 -31.392 1.00 22.99 ? 573  LEU B CD2   1 
ATOM   4334 N N     . SER A 1 576 ? 38.561 -18.542 -30.548 1.00 21.51 ? 574  SER B N     1 
ATOM   4335 C CA    . SER A 1 576 ? 39.727 -19.008 -29.755 1.00 22.68 ? 574  SER B CA    1 
ATOM   4336 C C     . SER A 1 576 ? 41.019 -18.514 -30.390 1.00 22.24 ? 574  SER B C     1 
ATOM   4337 O O     . SER A 1 576 ? 41.928 -18.108 -29.647 1.00 22.81 ? 574  SER B O     1 
ATOM   4338 C CB    . SER A 1 576 ? 39.739 -20.509 -29.602 1.00 22.43 ? 574  SER B CB    1 
ATOM   4339 O OG    . SER A 1 576 ? 38.587 -20.931 -28.886 1.00 24.02 ? 574  SER B OG    1 
ATOM   4340 N N     . ALA A 1 577 ? 41.113 -18.544 -31.720 1.00 23.55 ? 575  ALA B N     1 
ATOM   4341 C CA    . ALA A 1 577 ? 42.298 -18.090 -32.472 1.00 21.64 ? 575  ALA B CA    1 
ATOM   4342 C C     . ALA A 1 577 ? 42.469 -16.581 -32.292 1.00 24.26 ? 575  ALA B C     1 
ATOM   4343 O O     . ALA A 1 577 ? 43.625 -16.145 -32.046 1.00 24.93 ? 575  ALA B O     1 
ATOM   4344 C CB    . ALA A 1 577 ? 42.185 -18.461 -33.944 1.00 23.12 ? 575  ALA B CB    1 
ATOM   4345 N N     . SER A 1 578 ? 41.380 -15.813 -32.387 1.00 22.02 ? 576  SER B N     1 
ATOM   4346 C CA    . SER A 1 578 ? 41.386 -14.333 -32.187 1.00 24.80 ? 576  SER B CA    1 
ATOM   4347 C C     . SER A 1 578 ? 41.855 -13.993 -30.773 1.00 24.31 ? 576  SER B C     1 
ATOM   4348 O O     . SER A 1 578 ? 42.624 -13.025 -30.592 1.00 26.48 ? 576  SER B O     1 
ATOM   4349 C CB    . SER A 1 578 ? 40.011 -13.722 -32.437 1.00 27.57 ? 576  SER B CB    1 
ATOM   4350 O OG    . SER A 1 578 ? 39.845 -13.488 -33.814 1.00 38.24 ? 576  SER B OG    1 
ATOM   4351 N N     . VAL A 1 579 ? 41.360 -14.733 -29.789 1.00 25.73 ? 577  VAL B N     1 
ATOM   4352 C CA    . VAL A 1 579 ? 41.744 -14.487 -28.375 1.00 24.82 ? 577  VAL B CA    1 
ATOM   4353 C C     . VAL A 1 579 ? 43.258 -14.723 -28.268 1.00 23.56 ? 577  VAL B C     1 
ATOM   4354 O O     . VAL A 1 579 ? 43.986 -13.848 -27.714 1.00 23.03 ? 577  VAL B O     1 
ATOM   4355 C CB    . VAL A 1 579 ? 40.950 -15.377 -27.402 1.00 24.06 ? 577  VAL B CB    1 
ATOM   4356 C CG1   . VAL A 1 579 ? 41.554 -15.316 -26.005 1.00 23.32 ? 577  VAL B CG1   1 
ATOM   4357 C CG2   . VAL A 1 579 ? 39.481 -14.997 -27.334 1.00 26.47 ? 577  VAL B CG2   1 
ATOM   4358 N N     . ARG A 1 580 ? 43.720 -15.861 -28.784 1.00 24.65 ? 578  ARG B N     1 
ATOM   4359 C CA    . ARG A 1 580 ? 45.150 -16.278 -28.694 1.00 26.06 ? 578  ARG B CA    1 
ATOM   4360 C C     . ARG A 1 580 ? 46.092 -15.321 -29.415 1.00 26.98 ? 578  ARG B C     1 
ATOM   4361 O O     . ARG A 1 580 ? 47.296 -15.450 -29.170 1.00 27.46 ? 578  ARG B O     1 
ATOM   4362 C CB    . ARG A 1 580 ? 45.331 -17.696 -29.227 1.00 27.22 ? 578  ARG B CB    1 
ATOM   4363 C CG    . ARG A 1 580 ? 44.766 -18.750 -28.286 1.00 28.05 ? 578  ARG B CG    1 
ATOM   4364 C CD    . ARG A 1 580 ? 44.880 -20.117 -28.920 1.00 28.99 ? 578  ARG B CD    1 
ATOM   4365 N NE    . ARG A 1 580 ? 44.426 -21.165 -28.031 1.00 30.10 ? 578  ARG B NE    1 
ATOM   4366 C CZ    . ARG A 1 580 ? 45.193 -21.822 -27.162 1.00 33.80 ? 578  ARG B CZ    1 
ATOM   4367 N NH1   . ARG A 1 580 ? 44.647 -22.745 -26.390 1.00 33.56 ? 578  ARG B NH1   1 
ATOM   4368 N NH2   . ARG A 1 580 ? 46.492 -21.563 -27.056 1.00 34.50 ? 578  ARG B NH2   1 
ATOM   4369 N N     . ALA A 1 581 ? 45.604 -14.414 -30.262 1.00 26.25 ? 579  ALA B N     1 
ATOM   4370 C CA    . ALA A 1 581 ? 46.423 -13.325 -30.852 1.00 26.57 ? 579  ALA B CA    1 
ATOM   4371 C C     . ALA A 1 581 ? 46.946 -12.389 -29.760 1.00 26.90 ? 579  ALA B C     1 
ATOM   4372 O O     . ALA A 1 581 ? 47.983 -11.759 -29.979 1.00 28.12 ? 579  ALA B O     1 
ATOM   4373 C CB    . ALA A 1 581 ? 45.641 -12.539 -31.870 1.00 27.41 ? 579  ALA B CB    1 
ATOM   4374 N N     . GLY A 1 582 ? 46.202 -12.228 -28.673 1.00 25.93 ? 580  GLY B N     1 
ATOM   4375 C CA    . GLY A 1 582 ? 46.596 -11.369 -27.546 1.00 26.59 ? 580  GLY B CA    1 
ATOM   4376 C C     . GLY A 1 582 ? 46.351 -9.895  -27.819 1.00 27.39 ? 580  GLY B C     1 
ATOM   4377 O O     . GLY A 1 582 ? 45.853 -9.540  -28.920 1.00 24.30 ? 580  GLY B O     1 
ATOM   4378 N N     . SER A 1 583 ? 46.737 -9.055  -26.857 1.00 24.59 ? 581  SER B N     1 
ATOM   4379 C CA    . SER A 1 583 ? 46.477 -7.594  -26.849 1.00 26.55 ? 581  SER B CA    1 
ATOM   4380 C C     . SER A 1 583 ? 47.415 -6.857  -27.806 1.00 24.31 ? 581  SER B C     1 
ATOM   4381 O O     . SER A 1 583 ? 47.171 -5.656  -28.050 1.00 23.44 ? 581  SER B O     1 
ATOM   4382 C CB    . SER A 1 583 ? 46.615 -7.019  -25.459 1.00 27.53 ? 581  SER B CB    1 
ATOM   4383 O OG    . SER A 1 583 ? 47.881 -7.355  -24.890 1.00 26.91 ? 581  SER B OG    1 
ATOM   4384 N N     . GLU A 1 584 ? 48.501 -7.484  -28.251 1.00 27.30 ? 582  GLU B N     1 
ATOM   4385 C CA    . GLU A 1 584 ? 49.534 -6.753  -29.047 1.00 30.05 ? 582  GLU B CA    1 
ATOM   4386 C C     . GLU A 1 584 ? 48.936 -5.914  -30.184 1.00 26.34 ? 582  GLU B C     1 
ATOM   4387 O O     . GLU A 1 584 ? 49.246 -4.730  -30.242 1.00 23.12 ? 582  GLU B O     1 
ATOM   4388 C CB    . GLU A 1 584 ? 50.591 -7.718  -29.589 1.00 33.33 ? 582  GLU B CB    1 
ATOM   4389 C CG    . GLU A 1 584 ? 51.724 -7.018  -30.309 1.00 37.08 ? 582  GLU B CG    1 
ATOM   4390 C CD    . GLU A 1 584 ? 52.888 -7.911  -30.696 1.00 42.79 ? 582  GLU B CD    1 
ATOM   4391 O OE1   . GLU A 1 584 ? 53.865 -7.387  -31.256 1.00 53.53 ? 582  GLU B OE1   1 
ATOM   4392 O OE2   . GLU A 1 584 ? 52.815 -9.124  -30.439 1.00 46.04 ? 582  GLU B OE2   1 
ATOM   4393 N N     . SER A 1 585 ? 48.136 -6.527  -31.052 1.00 25.97 ? 583  SER B N     1 
ATOM   4394 C CA    . SER A 1 585 ? 47.556 -5.826  -32.231 1.00 25.69 ? 583  SER B CA    1 
ATOM   4395 C C     . SER A 1 585 ? 46.687 -4.645  -31.797 1.00 26.03 ? 583  SER B C     1 
ATOM   4396 O O     . SER A 1 585 ? 46.448 -3.778  -32.625 1.00 26.92 ? 583  SER B O     1 
ATOM   4397 C CB    . SER A 1 585 ? 46.761 -6.779  -33.098 1.00 25.28 ? 583  SER B CB    1 
ATOM   4398 O OG    . SER A 1 585 ? 45.636 -7.290  -32.419 1.00 23.82 ? 583  SER B OG    1 
ATOM   4399 N N     . LEU A 1 586 ? 46.211 -4.646  -30.553 1.00 23.84 ? 584  LEU B N     1 
ATOM   4400 C CA    . LEU A 1 586 ? 45.283 -3.579  -30.096 1.00 24.03 ? 584  LEU B CA    1 
ATOM   4401 C C     . LEU A 1 586 ? 46.062 -2.328  -29.702 1.00 23.07 ? 584  LEU B C     1 
ATOM   4402 O O     . LEU A 1 586 ? 45.471 -1.264  -29.682 1.00 23.30 ? 584  LEU B O     1 
ATOM   4403 C CB    . LEU A 1 586 ? 44.491 -4.092  -28.893 1.00 26.56 ? 584  LEU B CB    1 
ATOM   4404 C CG    . LEU A 1 586 ? 43.253 -4.937  -29.182 1.00 29.23 ? 584  LEU B CG    1 
ATOM   4405 C CD1   . LEU A 1 586 ? 43.582 -6.101  -30.100 1.00 30.01 ? 584  LEU B CD1   1 
ATOM   4406 C CD2   . LEU A 1 586 ? 42.649 -5.446  -27.881 1.00 26.81 ? 584  LEU B CD2   1 
ATOM   4407 N N     . TYR A 1 587 ? 47.351 -2.477  -29.426 1.00 23.00 ? 585  TYR B N     1 
ATOM   4408 C CA    . TYR A 1 587 ? 48.124 -1.329  -28.893 1.00 25.55 ? 585  TYR B CA    1 
ATOM   4409 C C     . TYR A 1 587 ? 49.301 -0.934  -29.801 1.00 27.45 ? 585  TYR B C     1 
ATOM   4410 O O     . TYR A 1 587 ? 50.241 -0.318  -29.307 1.00 26.30 ? 585  TYR B O     1 
ATOM   4411 C CB    . TYR A 1 587 ? 48.547 -1.684  -27.468 1.00 26.20 ? 585  TYR B CB    1 
ATOM   4412 C CG    . TYR A 1 587 ? 47.395 -1.581  -26.505 1.00 25.54 ? 585  TYR B CG    1 
ATOM   4413 C CD1   . TYR A 1 587 ? 47.038 -0.359  -25.968 1.00 26.07 ? 585  TYR B CD1   1 
ATOM   4414 C CD2   . TYR A 1 587 ? 46.620 -2.683  -26.190 1.00 25.05 ? 585  TYR B CD2   1 
ATOM   4415 C CE1   . TYR A 1 587 ? 45.963 -0.237  -25.109 1.00 25.25 ? 585  TYR B CE1   1 
ATOM   4416 C CE2   . TYR A 1 587 ? 45.540 -2.579  -25.331 1.00 26.64 ? 585  TYR B CE2   1 
ATOM   4417 C CZ    . TYR A 1 587 ? 45.209 -1.349  -24.794 1.00 24.89 ? 585  TYR B CZ    1 
ATOM   4418 O OH    . TYR A 1 587 ? 44.150 -1.217  -23.951 1.00 23.67 ? 585  TYR B OH    1 
ATOM   4419 N N     . LEU A 1 588 ? 49.224 -1.258  -31.088 1.00 25.44 ? 586  LEU B N     1 
ATOM   4420 C CA    . LEU A 1 588 ? 50.300 -0.847  -32.019 1.00 25.05 ? 586  LEU B CA    1 
ATOM   4421 C C     . LEU A 1 588 ? 50.193 0.654   -32.278 1.00 27.30 ? 586  LEU B C     1 
ATOM   4422 O O     . LEU A 1 588 ? 51.225 1.281   -32.515 1.00 27.51 ? 586  LEU B O     1 
ATOM   4423 C CB    . LEU A 1 588 ? 50.166 -1.642  -33.317 1.00 25.07 ? 586  LEU B CB    1 
ATOM   4424 C CG    . LEU A 1 588 ? 50.311 -3.155  -33.177 1.00 23.57 ? 586  LEU B CG    1 
ATOM   4425 C CD1   . LEU A 1 588 ? 50.003 -3.848  -34.494 1.00 24.96 ? 586  LEU B CD1   1 
ATOM   4426 C CD2   . LEU A 1 588 ? 51.707 -3.517  -32.703 1.00 25.63 ? 586  LEU B CD2   1 
ATOM   4427 N N     . LEU A 1 589 ? 48.980 1.188   -32.200 1.00 25.22 ? 587  LEU B N     1 
ATOM   4428 C CA    . LEU A 1 589 ? 48.771 2.610   -32.544 1.00 26.00 ? 587  LEU B CA    1 
ATOM   4429 C C     . LEU A 1 589 ? 48.544 3.485   -31.316 1.00 28.67 ? 587  LEU B C     1 
ATOM   4430 O O     . LEU A 1 589 ? 47.913 3.039   -30.357 1.00 25.16 ? 587  LEU B O     1 
ATOM   4431 C CB    . LEU A 1 589 ? 47.545 2.714   -33.452 1.00 27.92 ? 587  LEU B CB    1 
ATOM   4432 C CG    . LEU A 1 589 ? 47.667 2.073   -34.833 1.00 30.22 ? 587  LEU B CG    1 
ATOM   4433 C CD1   . LEU A 1 589 ? 46.497 2.482   -35.712 1.00 32.07 ? 587  LEU B CD1   1 
ATOM   4434 C CD2   . LEU A 1 589 ? 48.983 2.446   -35.494 1.00 33.26 ? 587  LEU B CD2   1 
ATOM   4435 N N     . ASP A 1 590 ? 49.020 4.717   -31.407 1.00 30.63 ? 588  ASP B N     1 
ATOM   4436 C CA    . ASP A 1 590 ? 48.733 5.699   -30.350 1.00 31.73 ? 588  ASP B CA    1 
ATOM   4437 C C     . ASP A 1 590 ? 47.358 6.273   -30.679 1.00 29.54 ? 588  ASP B C     1 
ATOM   4438 O O     . ASP A 1 590 ? 46.955 6.192   -31.839 1.00 28.46 ? 588  ASP B O     1 
ATOM   4439 C CB    . ASP A 1 590 ? 49.777 6.811   -30.342 1.00 36.05 ? 588  ASP B CB    1 
ATOM   4440 C CG    . ASP A 1 590 ? 51.188 6.348   -30.040 1.00 42.43 ? 588  ASP B CG    1 
ATOM   4441 O OD1   . ASP A 1 590 ? 51.344 5.457   -29.191 1.00 40.09 ? 588  ASP B OD1   1 
ATOM   4442 O OD2   . ASP A 1 590 ? 52.116 6.897   -30.651 1.00 44.35 ? 588  ASP B OD2   1 
ATOM   4443 N N     . ALA A 1 591 ? 46.686 6.849   -29.691 1.00 28.87 ? 589  ALA B N     1 
ATOM   4444 C CA    . ALA A 1 591 ? 45.331 7.396   -29.893 1.00 27.81 ? 589  ALA B CA    1 
ATOM   4445 C C     . ALA A 1 591 ? 45.331 8.349   -31.083 1.00 29.39 ? 589  ALA B C     1 
ATOM   4446 O O     . ALA A 1 591 ? 44.348 8.372   -31.818 1.00 29.11 ? 589  ALA B O     1 
ATOM   4447 C CB    . ALA A 1 591 ? 44.890 8.107   -28.646 1.00 29.07 ? 589  ALA B CB    1 
ATOM   4448 N N     . GLU A 1 592 ? 46.415 9.100   -31.246 1.00 28.93 ? 590  GLU B N     1 
ATOM   4449 C CA    . GLU A 1 592 ? 46.479 10.121  -32.321 1.00 31.07 ? 590  GLU B CA    1 
ATOM   4450 C C     . GLU A 1 592 ? 46.525 9.472   -33.705 1.00 28.27 ? 590  GLU B C     1 
ATOM   4451 O O     . GLU A 1 592 ? 46.210 10.156  -34.673 1.00 26.86 ? 590  GLU B O     1 
ATOM   4452 C CB    . GLU A 1 592 ? 47.719 10.986  -32.119 1.00 36.41 ? 590  GLU B CB    1 
ATOM   4453 C CG    . GLU A 1 592 ? 47.664 11.837  -30.862 1.00 45.44 ? 590  GLU B CG    1 
ATOM   4454 C CD    . GLU A 1 592 ? 47.785 11.085  -29.547 1.00 50.50 ? 590  GLU B CD    1 
ATOM   4455 O OE1   . GLU A 1 592 ? 48.608 10.155  -29.471 1.00 46.54 ? 590  GLU B OE1   1 
ATOM   4456 O OE2   . GLU A 1 592 ? 47.048 11.432  -28.602 1.00 56.89 ? 590  GLU B OE2   1 
ATOM   4457 N N     . GLN A 1 593 ? 46.901 8.200   -33.773 1.00 27.01 ? 591  GLN B N     1 
ATOM   4458 C CA    . GLN A 1 593 ? 47.072 7.518   -35.078 1.00 28.89 ? 591  GLN B CA    1 
ATOM   4459 C C     . GLN A 1 593 ? 45.784 6.814   -35.523 1.00 30.22 ? 591  GLN B C     1 
ATOM   4460 O O     . GLN A 1 593 ? 45.818 6.203   -36.588 1.00 29.24 ? 591  GLN B O     1 
ATOM   4461 C CB    . GLN A 1 593 ? 48.212 6.508   -34.968 1.00 27.84 ? 591  GLN B CB    1 
ATOM   4462 C CG    . GLN A 1 593 ? 49.537 7.134   -34.570 1.00 28.25 ? 591  GLN B CG    1 
ATOM   4463 C CD    . GLN A 1 593 ? 50.615 6.091   -34.427 1.00 31.05 ? 591  GLN B CD    1 
ATOM   4464 O OE1   . GLN A 1 593 ? 50.538 5.203   -33.585 1.00 27.87 ? 591  GLN B OE1   1 
ATOM   4465 N NE2   . GLN A 1 593 ? 51.631 6.190   -35.266 1.00 36.68 ? 591  GLN B NE2   1 
ATOM   4466 N N     . PHE A 1 594 ? 44.713 6.891   -34.732 1.00 26.70 ? 592  PHE B N     1 
ATOM   4467 C CA    . PHE A 1 594 ? 43.412 6.286   -35.123 1.00 26.11 ? 592  PHE B CA    1 
ATOM   4468 C C     . PHE A 1 594 ? 42.694 7.178   -36.147 1.00 24.73 ? 592  PHE B C     1 
ATOM   4469 O O     . PHE A 1 594 ? 42.990 8.368   -36.143 1.00 33.73 ? 592  PHE B O     1 
ATOM   4470 C CB    . PHE A 1 594 ? 42.541 6.026   -33.893 1.00 23.77 ? 592  PHE B CB    1 
ATOM   4471 C CG    . PHE A 1 594 ? 42.852 4.751   -33.156 1.00 24.14 ? 592  PHE B CG    1 
ATOM   4472 C CD1   . PHE A 1 594 ? 41.992 3.669   -33.221 1.00 22.71 ? 592  PHE B CD1   1 
ATOM   4473 C CD2   . PHE A 1 594 ? 44.002 4.635   -32.395 1.00 24.83 ? 592  PHE B CD2   1 
ATOM   4474 C CE1   . PHE A 1 594 ? 42.276 2.498   -32.540 1.00 24.21 ? 592  PHE B CE1   1 
ATOM   4475 C CE2   . PHE A 1 594 ? 44.286 3.464   -31.715 1.00 26.97 ? 592  PHE B CE2   1 
ATOM   4476 C CZ    . PHE A 1 594 ? 43.423 2.397   -31.790 1.00 26.31 ? 592  PHE B CZ    1 
ATOM   4477 N N     . ALA B 1 4   ? 30.158 14.718  -33.869 1.00 43.80 ? 2    ALA A N     1 
ATOM   4478 C CA    . ALA B 1 4   ? 31.212 14.653  -34.913 1.00 41.63 ? 2    ALA A CA    1 
ATOM   4479 C C     . ALA B 1 4   ? 30.626 15.046  -36.270 1.00 34.95 ? 2    ALA A C     1 
ATOM   4480 O O     . ALA B 1 4   ? 29.726 14.394  -36.768 1.00 39.10 ? 2    ALA A O     1 
ATOM   4481 C CB    . ALA B 1 4   ? 31.856 13.294  -34.975 1.00 41.30 ? 2    ALA A CB    1 
ATOM   4482 N N     . ASP B 1 5   ? 31.181 16.090  -36.854 1.00 31.65 ? 3    ASP A N     1 
ATOM   4483 C CA    . ASP B 1 5   ? 30.921 16.532  -38.240 1.00 31.01 ? 3    ASP A CA    1 
ATOM   4484 C C     . ASP B 1 5   ? 31.535 15.524  -39.204 1.00 31.01 ? 3    ASP A C     1 
ATOM   4485 O O     . ASP B 1 5   ? 32.654 15.047  -38.921 1.00 30.66 ? 3    ASP A O     1 
ATOM   4486 C CB    . ASP B 1 5   ? 31.559 17.894  -38.489 1.00 32.57 ? 3    ASP A CB    1 
ATOM   4487 C CG    . ASP B 1 5   ? 30.954 18.989  -37.625 1.00 36.25 ? 3    ASP A CG    1 
ATOM   4488 O OD1   . ASP B 1 5   ? 29.748 18.917  -37.367 1.00 36.74 ? 3    ASP A OD1   1 
ATOM   4489 O OD2   . ASP B 1 5   ? 31.696 19.888  -37.229 1.00 39.59 ? 3    ASP A OD2   1 
ATOM   4490 N N     . TYR B 1 6   ? 30.860 15.272  -40.323 1.00 27.19 ? 4    TYR A N     1 
ATOM   4491 C CA    . TYR B 1 6   ? 31.400 14.443  -41.419 1.00 25.82 ? 4    TYR A CA    1 
ATOM   4492 C C     . TYR B 1 6   ? 32.564 15.195  -42.054 1.00 26.23 ? 4    TYR A C     1 
ATOM   4493 O O     . TYR B 1 6   ? 32.395 16.379  -42.364 1.00 25.24 ? 4    TYR A O     1 
ATOM   4494 C CB    . TYR B 1 6   ? 30.374 14.122  -42.495 1.00 25.64 ? 4    TYR A CB    1 
ATOM   4495 C CG    . TYR B 1 6   ? 30.983 13.346  -43.633 1.00 24.84 ? 4    TYR A CG    1 
ATOM   4496 C CD1   . TYR B 1 6   ? 31.471 12.061  -43.427 1.00 24.60 ? 4    TYR A CD1   1 
ATOM   4497 C CD2   . TYR B 1 6   ? 31.081 13.891  -44.907 1.00 25.42 ? 4    TYR A CD2   1 
ATOM   4498 C CE1   . TYR B 1 6   ? 32.025 11.335  -44.468 1.00 24.82 ? 4    TYR A CE1   1 
ATOM   4499 C CE2   . TYR B 1 6   ? 31.631 13.173  -45.957 1.00 23.71 ? 4    TYR A CE2   1 
ATOM   4500 C CZ    . TYR B 1 6   ? 32.136 11.907  -45.723 1.00 24.05 ? 4    TYR A CZ    1 
ATOM   4501 O OH    . TYR B 1 6   ? 32.657 11.167  -46.730 1.00 22.41 ? 4    TYR A OH    1 
ATOM   4502 N N     . LYS B 1 7   ? 33.703 14.511  -42.190 1.00 25.68 ? 5    LYS A N     1 
ATOM   4503 C CA    . LYS B 1 7   ? 34.874 14.967  -42.976 1.00 26.00 ? 5    LYS A CA    1 
ATOM   4504 C C     . LYS B 1 7   ? 35.227 13.892  -44.003 1.00 24.51 ? 5    LYS A C     1 
ATOM   4505 O O     . LYS B 1 7   ? 35.488 12.745  -43.598 1.00 25.16 ? 5    LYS A O     1 
ATOM   4506 C CB    . LYS B 1 7   ? 36.093 15.238  -42.095 1.00 30.17 ? 5    LYS A CB    1 
ATOM   4507 C CG    . LYS B 1 7   ? 37.246 15.832  -42.886 1.00 34.68 ? 5    LYS A CG    1 
ATOM   4508 C CD    . LYS B 1 7   ? 38.419 16.290  -42.061 1.00 41.77 ? 5    LYS A CD    1 
ATOM   4509 C CE    . LYS B 1 7   ? 39.411 17.032  -42.931 1.00 43.40 ? 5    LYS A CE    1 
ATOM   4510 N NZ    . LYS B 1 7   ? 40.784 16.666  -42.536 1.00 52.67 ? 5    LYS A NZ    1 
ATOM   4511 N N     . ALA B 1 8   ? 35.255 14.257  -45.282 1.00 26.39 ? 6    ALA A N     1 
ATOM   4512 C CA    . ALA B 1 8   ? 35.558 13.303  -46.378 1.00 25.21 ? 6    ALA A CA    1 
ATOM   4513 C C     . ALA B 1 8   ? 36.945 12.728  -46.148 1.00 25.23 ? 6    ALA A C     1 
ATOM   4514 O O     . ALA B 1 8   ? 37.877 13.480  -45.831 1.00 25.98 ? 6    ALA A O     1 
ATOM   4515 C CB    . ALA B 1 8   ? 35.421 13.989  -47.717 1.00 25.43 ? 6    ALA A CB    1 
ATOM   4516 N N     . PRO B 1 9   ? 37.105 11.381  -46.238 1.00 23.87 ? 7    PRO A N     1 
ATOM   4517 C CA    . PRO B 1 9   ? 38.392 10.733  -46.048 1.00 22.95 ? 7    PRO A CA    1 
ATOM   4518 C C     . PRO B 1 9   ? 39.277 10.815  -47.300 1.00 23.54 ? 7    PRO A C     1 
ATOM   4519 O O     . PRO B 1 9   ? 39.653 9.795   -47.833 1.00 24.46 ? 7    PRO A O     1 
ATOM   4520 C CB    . PRO B 1 9   ? 38.005 9.270   -45.788 1.00 24.04 ? 7    PRO A CB    1 
ATOM   4521 C CG    . PRO B 1 9   ? 36.739 9.079   -46.567 1.00 23.04 ? 7    PRO A CG    1 
ATOM   4522 C CD    . PRO B 1 9   ? 36.033 10.416  -46.514 1.00 23.79 ? 7    PRO A CD    1 
ATOM   4523 N N     . LEU B 1 10  ? 39.594 12.024  -47.732 1.00 22.24 ? 8    LEU A N     1 
ATOM   4524 C CA    . LEU B 1 10  ? 40.268 12.246  -49.028 1.00 23.78 ? 8    LEU A CA    1 
ATOM   4525 C C     . LEU B 1 10  ? 41.704 11.724  -48.944 1.00 24.77 ? 8    LEU A C     1 
ATOM   4526 O O     . LEU B 1 10  ? 42.197 11.272  -49.977 1.00 25.61 ? 8    LEU A O     1 
ATOM   4527 C CB    . LEU B 1 10  ? 40.260 13.737  -49.360 1.00 25.22 ? 8    LEU A CB    1 
ATOM   4528 C CG    . LEU B 1 10  ? 38.885 14.374  -49.513 1.00 26.18 ? 8    LEU A CG    1 
ATOM   4529 C CD1   . LEU B 1 10  ? 39.035 15.778  -50.051 1.00 28.34 ? 8    LEU A CD1   1 
ATOM   4530 C CD2   . LEU B 1 10  ? 37.952 13.552  -50.408 1.00 27.56 ? 8    LEU A CD2   1 
ATOM   4531 N N     . ARG B 1 11  ? 42.354 11.795  -47.777 1.00 23.42 ? 9    ARG A N     1 
ATOM   4532 C CA    . ARG B 1 11  ? 43.754 11.315  -47.628 1.00 22.73 ? 9    ARG A CA    1 
ATOM   4533 C C     . ARG B 1 11  ? 43.768 9.791   -47.857 1.00 24.16 ? 9    ARG A C     1 
ATOM   4534 O O     . ARG B 1 11  ? 44.657 9.284   -48.592 1.00 25.41 ? 9    ARG A O     1 
ATOM   4535 C CB    . ARG B 1 11  ? 44.364 11.675  -46.271 1.00 24.65 ? 9    ARG A CB    1 
ATOM   4536 C CG    . ARG B 1 11  ? 45.746 11.077  -46.046 1.00 26.95 ? 9    ARG A CG    1 
ATOM   4537 C CD    . ARG B 1 11  ? 46.775 11.706  -46.996 1.00 27.71 ? 9    ARG A CD    1 
ATOM   4538 N NE    . ARG B 1 11  ? 48.073 11.088  -46.940 1.00 28.80 ? 9    ARG A NE    1 
ATOM   4539 C CZ    . ARG B 1 11  ? 48.491 10.093  -47.721 1.00 30.13 ? 9    ARG A CZ    1 
ATOM   4540 N NH1   . ARG B 1 11  ? 49.720 9.635   -47.574 1.00 30.12 ? 9    ARG A NH1   1 
ATOM   4541 N NH2   . ARG B 1 11  ? 47.703 9.556   -48.640 1.00 28.76 ? 9    ARG A NH2   1 
ATOM   4542 N N     . ASP B 1 12  ? 42.830 9.056   -47.280 1.00 23.80 ? 10   ASP A N     1 
ATOM   4543 C CA    . ASP B 1 12  ? 42.825 7.581   -47.467 1.00 23.13 ? 10   ASP A CA    1 
ATOM   4544 C C     . ASP B 1 12  ? 42.480 7.284   -48.925 1.00 23.86 ? 10   ASP A C     1 
ATOM   4545 O O     . ASP B 1 12  ? 43.049 6.329   -49.489 1.00 24.13 ? 10   ASP A O     1 
ATOM   4546 C CB    . ASP B 1 12  ? 41.863 6.835   -46.542 1.00 22.90 ? 10   ASP A CB    1 
ATOM   4547 C CG    . ASP B 1 12  ? 42.196 5.353   -46.502 1.00 23.41 ? 10   ASP A CG    1 
ATOM   4548 O OD1   . ASP B 1 12  ? 43.368 5.049   -46.178 1.00 24.24 ? 10   ASP A OD1   1 
ATOM   4549 O OD2   . ASP B 1 12  ? 41.311 4.516   -46.832 1.00 21.69 ? 10   ASP A OD2   1 
ATOM   4550 N N     . MET B 1 13  ? 41.535 8.030   -49.475 1.00 23.04 ? 11   MET A N     1 
ATOM   4551 C CA    . MET B 1 13  ? 41.088 7.845   -50.864 1.00 25.10 ? 11   MET A CA    1 
ATOM   4552 C C     . MET B 1 13  ? 42.256 8.076   -51.847 1.00 25.00 ? 11   MET A C     1 
ATOM   4553 O O     . MET B 1 13  ? 42.336 7.317   -52.801 1.00 22.99 ? 11   MET A O     1 
ATOM   4554 C CB    . MET B 1 13  ? 39.903 8.760   -51.144 1.00 24.71 ? 11   MET A CB    1 
ATOM   4555 C CG    . MET B 1 13  ? 38.590 8.180   -50.579 1.00 26.60 ? 11   MET A CG    1 
ATOM   4556 S SD    . MET B 1 13  ? 37.242 9.304   -50.903 1.00 26.50 ? 11   MET A SD    1 
ATOM   4557 C CE    . MET B 1 13  ? 35.829 8.308   -50.406 1.00 28.86 ? 11   MET A CE    1 
ATOM   4558 N N     . ARG B 1 14  ? 43.097 9.089   -51.633 1.00 24.12 ? 12   ARG A N     1 
ATOM   4559 C CA    . ARG B 1 14  ? 44.337 9.304   -52.435 1.00 25.26 ? 12   ARG A CA    1 
ATOM   4560 C C     . ARG B 1 14  ? 45.264 8.091   -52.273 1.00 25.96 ? 12   ARG A C     1 
ATOM   4561 O O     . ARG B 1 14  ? 45.878 7.661   -53.265 1.00 26.28 ? 12   ARG A O     1 
ATOM   4562 C CB    . ARG B 1 14  ? 45.057 10.579  -51.995 1.00 26.78 ? 12   ARG A CB    1 
ATOM   4563 C CG    . ARG B 1 14  ? 44.327 11.867  -52.326 1.00 30.36 ? 12   ARG A CG    1 
ATOM   4564 C CD    . ARG B 1 14  ? 45.221 13.105  -52.310 1.00 34.04 ? 12   ARG A CD    1 
ATOM   4565 N NE    . ARG B 1 14  ? 45.661 13.504  -50.973 1.00 36.63 ? 12   ARG A NE    1 
ATOM   4566 C CZ    . ARG B 1 14  ? 44.938 14.205  -50.094 1.00 35.75 ? 12   ARG A CZ    1 
ATOM   4567 N NH1   . ARG B 1 14  ? 45.455 14.517  -48.919 1.00 36.02 ? 12   ARG A NH1   1 
ATOM   4568 N NH2   . ARG B 1 14  ? 43.712 14.588  -50.386 1.00 36.09 ? 12   ARG A NH2   1 
ATOM   4569 N N     . PHE B 1 15  ? 45.378 7.547   -51.061 1.00 23.22 ? 13   PHE A N     1 
ATOM   4570 C CA    . PHE B 1 15  ? 46.314 6.439   -50.799 1.00 24.28 ? 13   PHE A CA    1 
ATOM   4571 C C     . PHE B 1 15  ? 45.860 5.229   -51.612 1.00 24.71 ? 13   PHE A C     1 
ATOM   4572 O O     . PHE B 1 15  ? 46.675 4.598   -52.298 1.00 24.56 ? 13   PHE A O     1 
ATOM   4573 C CB    . PHE B 1 15  ? 46.462 6.176   -49.300 1.00 24.81 ? 13   PHE A CB    1 
ATOM   4574 C CG    . PHE B 1 15  ? 47.130 4.864   -48.989 1.00 23.70 ? 13   PHE A CG    1 
ATOM   4575 C CD1   . PHE B 1 15  ? 48.512 4.746   -49.029 1.00 22.80 ? 13   PHE A CD1   1 
ATOM   4576 C CD2   . PHE B 1 15  ? 46.379 3.743   -48.694 1.00 23.04 ? 13   PHE A CD2   1 
ATOM   4577 C CE1   . PHE B 1 15  ? 49.118 3.531   -48.777 1.00 21.82 ? 13   PHE A CE1   1 
ATOM   4578 C CE2   . PHE B 1 15  ? 46.995 2.540   -48.411 1.00 23.12 ? 13   PHE A CE2   1 
ATOM   4579 C CZ    . PHE B 1 15  ? 48.368 2.442   -48.446 1.00 23.01 ? 13   PHE A CZ    1 
ATOM   4580 N N     . VAL B 1 16  ? 44.573 4.911   -51.553 1.00 24.55 ? 14   VAL A N     1 
ATOM   4581 C CA    . VAL B 1 16  ? 44.025 3.712   -52.234 1.00 24.79 ? 14   VAL A CA    1 
ATOM   4582 C C     . VAL B 1 16  ? 44.197 3.850   -53.743 1.00 24.09 ? 14   VAL A C     1 
ATOM   4583 O O     . VAL B 1 16  ? 44.729 2.902   -54.350 1.00 23.68 ? 14   VAL A O     1 
ATOM   4584 C CB    . VAL B 1 16  ? 42.540 3.485   -51.895 1.00 24.71 ? 14   VAL A CB    1 
ATOM   4585 C CG1   . VAL B 1 16  ? 41.935 2.412   -52.792 1.00 23.87 ? 14   VAL A CG1   1 
ATOM   4586 C CG2   . VAL B 1 16  ? 42.379 3.141   -50.428 1.00 26.07 ? 14   VAL A CG2   1 
ATOM   4587 N N     . LEU B 1 17  ? 43.737 4.954   -54.322 1.00 23.86 ? 15   LEU A N     1 
ATOM   4588 C CA    . LEU B 1 17  ? 43.656 5.078   -55.799 1.00 25.90 ? 15   LEU A CA    1 
ATOM   4589 C C     . LEU B 1 17  ? 45.018 5.459   -56.405 1.00 27.90 ? 15   LEU A C     1 
ATOM   4590 O O     . LEU B 1 17  ? 45.397 4.865   -57.418 1.00 27.01 ? 15   LEU A O     1 
ATOM   4591 C CB    . LEU B 1 17  ? 42.593 6.118   -56.154 1.00 27.60 ? 15   LEU A CB    1 
ATOM   4592 C CG    . LEU B 1 17  ? 41.172 5.576   -56.239 1.00 30.24 ? 15   LEU A CG    1 
ATOM   4593 C CD1   . LEU B 1 17  ? 40.300 6.545   -56.998 1.00 31.74 ? 15   LEU A CD1   1 
ATOM   4594 C CD2   . LEU B 1 17  ? 41.140 4.213   -56.903 1.00 32.60 ? 15   LEU A CD2   1 
ATOM   4595 N N     . ASN B 1 18  ? 45.707 6.429   -55.818 1.00 29.25 ? 16   ASN A N     1 
ATOM   4596 C CA    . ASN B 1 18  ? 46.929 7.026   -56.405 1.00 30.02 ? 16   ASN A CA    1 
ATOM   4597 C C     . ASN B 1 18  ? 48.179 6.281   -55.951 1.00 28.69 ? 16   ASN A C     1 
ATOM   4598 O O     . ASN B 1 18  ? 49.114 6.264   -56.729 1.00 31.30 ? 16   ASN A O     1 
ATOM   4599 C CB    . ASN B 1 18  ? 47.045 8.516   -56.083 1.00 31.86 ? 16   ASN A CB    1 
ATOM   4600 C CG    . ASN B 1 18  ? 45.799 9.288   -56.445 1.00 33.69 ? 16   ASN A CG    1 
ATOM   4601 O OD1   . ASN B 1 18  ? 44.979 8.828   -57.245 1.00 36.77 ? 16   ASN A OD1   1 
ATOM   4602 N ND2   . ASN B 1 18  ? 45.637 10.460  -55.850 1.00 36.45 ? 16   ASN A ND2   1 
ATOM   4603 N N     . GLU B 1 19  ? 48.209 5.683   -54.756 1.00 26.18 ? 17   GLU A N     1 
ATOM   4604 C CA    . GLU B 1 19  ? 49.464 5.120   -54.210 1.00 27.23 ? 17   GLU A CA    1 
ATOM   4605 C C     . GLU B 1 19  ? 49.459 3.598   -54.331 1.00 27.02 ? 17   GLU A C     1 
ATOM   4606 O O     . GLU B 1 19  ? 50.511 3.040   -54.685 1.00 28.06 ? 17   GLU A O     1 
ATOM   4607 C CB    . GLU B 1 19  ? 49.689 5.579   -52.768 1.00 28.06 ? 17   GLU A CB    1 
ATOM   4608 C CG    . GLU B 1 19  ? 49.820 7.083   -52.620 1.00 26.67 ? 17   GLU A CG    1 
ATOM   4609 C CD    . GLU B 1 19  ? 50.150 7.470   -51.182 1.00 27.63 ? 17   GLU A CD    1 
ATOM   4610 O OE1   . GLU B 1 19  ? 49.346 8.175   -50.562 1.00 27.95 ? 17   GLU A OE1   1 
ATOM   4611 O OE2   . GLU B 1 19  ? 51.203 7.036   -50.679 1.00 29.21 ? 17   GLU A OE2   1 
ATOM   4612 N N     . VAL B 1 20  ? 48.341 2.938   -54.037 1.00 25.21 ? 18   VAL A N     1 
ATOM   4613 C CA    . VAL B 1 20  ? 48.240 1.452   -54.082 1.00 22.53 ? 18   VAL A CA    1 
ATOM   4614 C C     . VAL B 1 20  ? 47.933 1.051   -55.533 1.00 26.04 ? 18   VAL A C     1 
ATOM   4615 O O     . VAL B 1 20  ? 48.782 0.398   -56.158 1.00 24.78 ? 18   VAL A O     1 
ATOM   4616 C CB    . VAL B 1 20  ? 47.179 0.935   -53.090 1.00 23.69 ? 18   VAL A CB    1 
ATOM   4617 C CG1   . VAL B 1 20  ? 47.013 -0.583  -53.174 1.00 24.12 ? 18   VAL A CG1   1 
ATOM   4618 C CG2   . VAL B 1 20  ? 47.508 1.349   -51.671 1.00 22.49 ? 18   VAL A CG2   1 
ATOM   4619 N N     . PHE B 1 21  ? 46.778 1.441   -56.079 1.00 24.20 ? 19   PHE A N     1 
ATOM   4620 C CA    . PHE B 1 21  ? 46.357 0.989   -57.431 1.00 25.86 ? 19   PHE A CA    1 
ATOM   4621 C C     . PHE B 1 21  ? 46.946 1.871   -58.547 1.00 26.02 ? 19   PHE A C     1 
ATOM   4622 O O     . PHE B 1 21  ? 46.856 1.454   -59.716 1.00 24.67 ? 19   PHE A O     1 
ATOM   4623 C CB    . PHE B 1 21  ? 44.835 0.886   -57.506 1.00 25.66 ? 19   PHE A CB    1 
ATOM   4624 C CG    . PHE B 1 21  ? 44.286 -0.171  -56.601 1.00 23.71 ? 19   PHE A CG    1 
ATOM   4625 C CD1   . PHE B 1 21  ? 44.667 -1.485  -56.753 1.00 25.74 ? 19   PHE A CD1   1 
ATOM   4626 C CD2   . PHE B 1 21  ? 43.383 0.144   -55.603 1.00 24.37 ? 19   PHE A CD2   1 
ATOM   4627 C CE1   . PHE B 1 21  ? 44.193 -2.461  -55.890 1.00 24.55 ? 19   PHE A CE1   1 
ATOM   4628 C CE2   . PHE B 1 21  ? 42.904 -0.834  -54.745 1.00 23.06 ? 19   PHE A CE2   1 
ATOM   4629 C CZ    . PHE B 1 21  ? 43.306 -2.133  -54.888 1.00 23.72 ? 19   PHE A CZ    1 
ATOM   4630 N N     . GLU B 1 22  ? 47.442 3.075   -58.238 1.00 28.99 ? 20   GLU A N     1 
ATOM   4631 C CA    . GLU B 1 22  ? 48.096 3.969   -59.233 1.00 32.99 ? 20   GLU A CA    1 
ATOM   4632 C C     . GLU B 1 22  ? 47.219 4.068   -60.482 1.00 33.50 ? 20   GLU A C     1 
ATOM   4633 O O     . GLU B 1 22  ? 47.702 3.734   -61.596 1.00 30.85 ? 20   GLU A O     1 
ATOM   4634 C CB    . GLU B 1 22  ? 49.476 3.403   -59.593 1.00 35.31 ? 20   GLU A CB    1 
ATOM   4635 C CG    . GLU B 1 22  ? 50.428 3.326   -58.399 1.00 36.46 ? 20   GLU A CG    1 
ATOM   4636 C CD    . GLU B 1 22  ? 51.910 3.282   -58.760 1.00 38.85 ? 20   GLU A CD    1 
ATOM   4637 O OE1   . GLU B 1 22  ? 52.410 4.238   -59.384 1.00 40.64 ? 20   GLU A OE1   1 
ATOM   4638 O OE2   . GLU B 1 22  ? 52.561 2.318   -58.398 1.00 39.59 ? 20   GLU A OE2   1 
ATOM   4639 N N     . VAL B 1 23  ? 45.962 4.473   -60.325 1.00 32.44 ? 21   VAL A N     1 
ATOM   4640 C CA    . VAL B 1 23  ? 44.984 4.405   -61.448 1.00 35.37 ? 21   VAL A CA    1 
ATOM   4641 C C     . VAL B 1 23  ? 45.332 5.441   -62.522 1.00 35.69 ? 21   VAL A C     1 
ATOM   4642 O O     . VAL B 1 23  ? 44.901 5.238   -63.671 1.00 34.26 ? 21   VAL A O     1 
ATOM   4643 C CB    . VAL B 1 23  ? 43.522 4.570   -60.990 1.00 35.83 ? 21   VAL A CB    1 
ATOM   4644 C CG1   . VAL B 1 23  ? 43.096 3.455   -60.054 1.00 36.97 ? 21   VAL A CG1   1 
ATOM   4645 C CG2   . VAL B 1 23  ? 43.259 5.941   -60.387 1.00 34.50 ? 21   VAL A CG2   1 
ATOM   4646 N N     . SER B 1 24  ? 46.020 6.527   -62.176 1.00 37.53 ? 22   SER A N     1 
ATOM   4647 C CA    . SER B 1 24  ? 46.352 7.610   -63.134 1.00 40.08 ? 22   SER A CA    1 
ATOM   4648 C C     . SER B 1 24  ? 47.271 7.039   -64.229 1.00 42.12 ? 22   SER A C     1 
ATOM   4649 O O     . SER B 1 24  ? 47.109 7.428   -65.385 1.00 42.74 ? 22   SER A O     1 
ATOM   4650 C CB    . SER B 1 24  ? 46.944 8.802   -62.445 1.00 39.96 ? 22   SER A CB    1 
ATOM   4651 O OG    . SER B 1 24  ? 48.283 8.544   -62.067 1.00 41.83 ? 22   SER A OG    1 
ATOM   4652 N N     . ARG B 1 25  ? 48.137 6.079   -63.889 1.00 42.32 ? 23   ARG A N     1 
ATOM   4653 C CA    . ARG B 1 25  ? 48.943 5.308   -64.869 1.00 43.35 ? 23   ARG A CA    1 
ATOM   4654 C C     . ARG B 1 25  ? 48.024 4.661   -65.906 1.00 43.75 ? 23   ARG A C     1 
ATOM   4655 O O     . ARG B 1 25  ? 48.358 4.706   -67.089 1.00 47.57 ? 23   ARG A O     1 
ATOM   4656 C CB    . ARG B 1 25  ? 49.773 4.214   -64.197 1.00 43.94 ? 23   ARG A CB    1 
ATOM   4657 C CG    . ARG B 1 25  ? 50.944 4.730   -63.369 1.00 45.72 ? 23   ARG A CG    1 
ATOM   4658 C CD    . ARG B 1 25  ? 52.012 3.673   -63.100 1.00 48.02 ? 23   ARG A CD    1 
ATOM   4659 N NE    . ARG B 1 25  ? 51.420 2.362   -63.293 1.00 58.69 ? 23   ARG A NE    1 
ATOM   4660 C CZ    . ARG B 1 25  ? 51.751 1.473   -64.225 1.00 57.75 ? 23   ARG A CZ    1 
ATOM   4661 N NH1   . ARG B 1 25  ? 51.063 0.348   -64.301 1.00 54.59 ? 23   ARG A NH1   1 
ATOM   4662 N NH2   . ARG B 1 25  ? 52.760 1.679   -65.056 1.00 61.03 ? 23   ARG A NH2   1 
ATOM   4663 N N     . LEU B 1 26  ? 46.900 4.089   -65.484 1.00 43.28 ? 24   LEU A N     1 
ATOM   4664 C CA    . LEU B 1 26  ? 45.997 3.338   -66.391 1.00 44.46 ? 24   LEU A CA    1 
ATOM   4665 C C     . LEU B 1 26  ? 45.254 4.326   -67.296 1.00 46.71 ? 24   LEU A C     1 
ATOM   4666 O O     . LEU B 1 26  ? 45.229 4.107   -68.518 1.00 50.34 ? 24   LEU A O     1 
ATOM   4667 C CB    . LEU B 1 26  ? 45.070 2.471   -65.544 1.00 50.79 ? 24   LEU A CB    1 
ATOM   4668 C CG    . LEU B 1 26  ? 45.797 1.514   -64.594 1.00 54.19 ? 24   LEU A CG    1 
ATOM   4669 C CD1   . LEU B 1 26  ? 44.805 0.699   -63.771 1.00 55.27 ? 24   LEU A CD1   1 
ATOM   4670 C CD2   . LEU B 1 26  ? 46.754 0.598   -65.360 1.00 55.39 ? 24   LEU A CD2   1 
ATOM   4671 N N     . TRP B 1 27  ? 44.758 5.432   -66.743 1.00 41.40 ? 25   TRP A N     1 
ATOM   4672 C CA    . TRP B 1 27  ? 43.991 6.437   -67.523 1.00 43.27 ? 25   TRP A CA    1 
ATOM   4673 C C     . TRP B 1 27  ? 44.797 6.950   -68.722 1.00 48.77 ? 25   TRP A C     1 
ATOM   4674 O O     . TRP B 1 27  ? 44.184 7.122   -69.807 1.00 44.28 ? 25   TRP A O     1 
ATOM   4675 C CB    . TRP B 1 27  ? 43.614 7.614   -66.650 1.00 39.87 ? 25   TRP A CB    1 
ATOM   4676 C CG    . TRP B 1 27  ? 42.759 7.262   -65.481 1.00 37.45 ? 25   TRP A CG    1 
ATOM   4677 C CD1   . TRP B 1 27  ? 41.982 6.157   -65.294 1.00 36.80 ? 25   TRP A CD1   1 
ATOM   4678 C CD2   . TRP B 1 27  ? 42.583 8.092   -64.336 1.00 37.39 ? 25   TRP A CD2   1 
ATOM   4679 N NE1   . TRP B 1 27  ? 41.325 6.249   -64.098 1.00 37.19 ? 25   TRP A NE1   1 
ATOM   4680 C CE2   . TRP B 1 27  ? 41.676 7.426   -63.491 1.00 36.45 ? 25   TRP A CE2   1 
ATOM   4681 C CE3   . TRP B 1 27  ? 43.114 9.326   -63.954 1.00 36.12 ? 25   TRP A CE3   1 
ATOM   4682 C CZ2   . TRP B 1 27  ? 41.297 7.962   -62.268 1.00 35.44 ? 25   TRP A CZ2   1 
ATOM   4683 C CZ3   . TRP B 1 27  ? 42.743 9.850   -62.740 1.00 39.05 ? 25   TRP A CZ3   1 
ATOM   4684 C CH2   . TRP B 1 27  ? 41.834 9.181   -61.921 1.00 37.83 ? 25   TRP A CH2   1 
ATOM   4685 N N     . ALA B 1 28  ? 46.080 7.266   -68.487 1.00 50.92 ? 26   ALA A N     1 
ATOM   4686 C CA    . ALA B 1 28  ? 47.012 7.927   -69.434 1.00 50.72 ? 26   ALA A CA    1 
ATOM   4687 C C     . ALA B 1 28  ? 47.140 7.086   -70.710 1.00 52.56 ? 26   ALA A C     1 
ATOM   4688 O O     . ALA B 1 28  ? 47.216 7.703   -71.805 1.00 52.11 ? 26   ALA A O     1 
ATOM   4689 C CB    . ALA B 1 28  ? 48.355 8.140   -68.770 1.00 51.48 ? 26   ALA A CB    1 
ATOM   4690 N N     . GLN B 1 29  ? 47.107 5.752   -70.555 1.00 53.49 ? 27   GLN A N     1 
ATOM   4691 C CA    . GLN B 1 29  ? 47.155 4.714   -71.625 1.00 57.12 ? 27   GLN A CA    1 
ATOM   4692 C C     . GLN B 1 29  ? 45.835 4.631   -72.412 1.00 60.18 ? 27   GLN A C     1 
ATOM   4693 O O     . GLN B 1 29  ? 45.880 4.137   -73.547 1.00 64.58 ? 27   GLN A O     1 
ATOM   4694 C CB    . GLN B 1 29  ? 47.377 3.320   -71.033 1.00 60.28 ? 27   GLN A CB    1 
ATOM   4695 C CG    . GLN B 1 29  ? 48.553 3.217   -70.074 1.00 65.28 ? 27   GLN A CG    1 
ATOM   4696 C CD    . GLN B 1 29  ? 49.885 3.176   -70.779 1.00 71.79 ? 27   GLN A CD    1 
ATOM   4697 O OE1   . GLN B 1 29  ? 50.518 2.127   -70.890 1.00 82.17 ? 27   GLN A OE1   1 
ATOM   4698 N NE2   . GLN B 1 29  ? 50.328 4.327   -71.258 1.00 72.63 ? 27   GLN A NE2   1 
ATOM   4699 N N     . LEU B 1 30  ? 44.695 5.003   -71.819 1.00 59.95 ? 28   LEU A N     1 
ATOM   4700 C CA    . LEU B 1 30  ? 43.344 4.834   -72.423 1.00 57.89 ? 28   LEU A CA    1 
ATOM   4701 C C     . LEU B 1 30  ? 42.876 6.182   -72.945 1.00 62.40 ? 28   LEU A C     1 
ATOM   4702 O O     . LEU B 1 30  ? 42.486 7.049   -72.168 1.00 64.40 ? 28   LEU A O     1 
ATOM   4703 C CB    . LEU B 1 30  ? 42.386 4.268   -71.375 1.00 56.29 ? 28   LEU A CB    1 
ATOM   4704 C CG    . LEU B 1 30  ? 42.869 2.969   -70.734 1.00 58.44 ? 28   LEU A CG    1 
ATOM   4705 C CD1   . LEU B 1 30  ? 42.029 2.595   -69.517 1.00 55.83 ? 28   LEU A CD1   1 
ATOM   4706 C CD2   . LEU B 1 30  ? 42.888 1.845   -71.763 1.00 59.27 ? 28   LEU A CD2   1 
ATOM   4707 N N     . PRO B 1 31  ? 42.927 6.413   -74.276 1.00 70.33 ? 29   PRO A N     1 
ATOM   4708 C CA    . PRO B 1 31  ? 42.675 7.743   -74.830 1.00 66.73 ? 29   PRO A CA    1 
ATOM   4709 C C     . PRO B 1 31  ? 41.224 8.194   -74.611 1.00 60.50 ? 29   PRO A C     1 
ATOM   4710 O O     . PRO B 1 31  ? 40.992 9.382   -74.652 1.00 75.75 ? 29   PRO A O     1 
ATOM   4711 C CB    . PRO B 1 31  ? 42.989 7.608   -76.330 1.00 70.25 ? 29   PRO A CB    1 
ATOM   4712 C CG    . PRO B 1 31  ? 43.731 6.282   -76.452 1.00 73.45 ? 29   PRO A CG    1 
ATOM   4713 C CD    . PRO B 1 31  ? 43.216 5.417   -75.320 1.00 72.35 ? 29   PRO A CD    1 
ATOM   4714 N N     . ALA B 1 32  ? 40.304 7.250   -74.376 1.00 55.31 ? 30   ALA A N     1 
ATOM   4715 C CA    . ALA B 1 32  ? 38.888 7.513   -74.022 1.00 53.09 ? 30   ALA A CA    1 
ATOM   4716 C C     . ALA B 1 32  ? 38.801 8.291   -72.700 1.00 52.01 ? 30   ALA A C     1 
ATOM   4717 O O     . ALA B 1 32  ? 37.883 9.113   -72.557 1.00 51.60 ? 30   ALA A O     1 
ATOM   4718 C CB    . ALA B 1 32  ? 38.130 6.208   -73.952 1.00 56.57 ? 30   ALA A CB    1 
ATOM   4719 N N     . LEU B 1 33  ? 39.723 8.030   -71.762 1.00 48.91 ? 31   LEU A N     1 
ATOM   4720 C CA    . LEU B 1 33  ? 39.764 8.660   -70.414 1.00 43.07 ? 31   LEU A CA    1 
ATOM   4721 C C     . LEU B 1 33  ? 40.828 9.758   -70.382 1.00 45.52 ? 31   LEU A C     1 
ATOM   4722 O O     . LEU B 1 33  ? 40.642 10.714  -69.626 1.00 44.76 ? 31   LEU A O     1 
ATOM   4723 C CB    . LEU B 1 33  ? 40.098 7.609   -69.354 1.00 40.14 ? 31   LEU A CB    1 
ATOM   4724 C CG    . LEU B 1 33  ? 38.990 6.636   -68.987 1.00 36.88 ? 31   LEU A CG    1 
ATOM   4725 C CD1   . LEU B 1 33  ? 39.499 5.679   -67.928 1.00 37.98 ? 31   LEU A CD1   1 
ATOM   4726 C CD2   . LEU B 1 33  ? 37.756 7.378   -68.501 1.00 39.09 ? 31   LEU A CD2   1 
ATOM   4727 N N     . ALA B 1 34  ? 41.923 9.601   -71.126 1.00 44.92 ? 32   ALA A N     1 
ATOM   4728 C CA    . ALA B 1 34  ? 43.009 10.605  -71.183 1.00 49.09 ? 32   ALA A CA    1 
ATOM   4729 C C     . ALA B 1 34  ? 42.406 11.972  -71.545 1.00 43.66 ? 32   ALA A C     1 
ATOM   4730 O O     . ALA B 1 34  ? 42.854 12.951  -70.975 1.00 51.30 ? 32   ALA A O     1 
ATOM   4731 C CB    . ALA B 1 34  ? 44.091 10.161  -72.142 1.00 48.51 ? 32   ALA A CB    1 
ATOM   4732 N N     . GLU B 1 35  ? 41.370 12.002  -72.379 1.00 43.10 ? 33   GLU A N     1 
ATOM   4733 C CA    . GLU B 1 35  ? 40.615 13.220  -72.796 1.00 53.63 ? 33   GLU A CA    1 
ATOM   4734 C C     . GLU B 1 35  ? 39.851 13.866  -71.633 1.00 47.96 ? 33   GLU A C     1 
ATOM   4735 O O     . GLU B 1 35  ? 39.635 15.083  -71.709 1.00 45.39 ? 33   GLU A O     1 
ATOM   4736 C CB    . GLU B 1 35  ? 39.545 12.886  -73.845 1.00 60.31 ? 33   GLU A CB    1 
ATOM   4737 C CG    . GLU B 1 35  ? 40.093 12.398  -75.173 1.00 71.17 ? 33   GLU A CG    1 
ATOM   4738 C CD    . GLU B 1 35  ? 40.660 13.475  -76.085 1.00 75.35 ? 33   GLU A CD    1 
ATOM   4739 O OE1   . GLU B 1 35  ? 40.179 13.567  -77.229 1.00 76.76 ? 33   GLU A OE1   1 
ATOM   4740 O OE2   . GLU B 1 35  ? 41.596 14.202  -75.660 1.00 76.81 ? 33   GLU A OE2   1 
ATOM   4741 N N     . VAL B 1 36  ? 39.395 13.089  -70.644 1.00 43.73 ? 34   VAL A N     1 
ATOM   4742 C CA    . VAL B 1 36  ? 38.352 13.540  -69.670 1.00 44.24 ? 34   VAL A CA    1 
ATOM   4743 C C     . VAL B 1 36  ? 38.922 13.676  -68.247 1.00 39.69 ? 34   VAL A C     1 
ATOM   4744 O O     . VAL B 1 36  ? 38.363 14.474  -67.471 1.00 39.29 ? 34   VAL A O     1 
ATOM   4745 C CB    . VAL B 1 36  ? 37.109 12.624  -69.718 1.00 48.59 ? 34   VAL A CB    1 
ATOM   4746 C CG1   . VAL B 1 36  ? 36.709 12.286  -71.156 1.00 51.77 ? 34   VAL A CG1   1 
ATOM   4747 C CG2   . VAL B 1 36  ? 37.278 11.345  -68.913 1.00 52.42 ? 34   VAL A CG2   1 
ATOM   4748 N N     . VAL B 1 37  ? 39.957 12.920  -67.880 1.00 37.51 ? 35   VAL A N     1 
ATOM   4749 C CA    . VAL B 1 37  ? 40.449 12.895  -66.470 1.00 36.55 ? 35   VAL A CA    1 
ATOM   4750 C C     . VAL B 1 37  ? 41.967 12.710  -66.449 1.00 36.69 ? 35   VAL A C     1 
ATOM   4751 O O     . VAL B 1 37  ? 42.492 11.930  -67.252 1.00 32.96 ? 35   VAL A O     1 
ATOM   4752 C CB    . VAL B 1 37  ? 39.731 11.809  -65.634 1.00 34.69 ? 35   VAL A CB    1 
ATOM   4753 C CG1   . VAL B 1 37  ? 40.032 10.388  -66.079 1.00 34.56 ? 35   VAL A CG1   1 
ATOM   4754 C CG2   . VAL B 1 37  ? 40.034 11.945  -64.157 1.00 35.41 ? 35   VAL A CG2   1 
ATOM   4755 N N     . ASP B 1 38  ? 42.624 13.364  -65.501 1.00 37.15 ? 36   ASP A N     1 
ATOM   4756 C CA    . ASP B 1 38  ? 44.038 13.118  -65.134 1.00 37.45 ? 36   ASP A CA    1 
ATOM   4757 C C     . ASP B 1 38  ? 44.104 13.272  -63.610 1.00 39.64 ? 36   ASP A C     1 
ATOM   4758 O O     . ASP B 1 38  ? 43.045 13.521  -63.017 1.00 33.91 ? 36   ASP A O     1 
ATOM   4759 C CB    . ASP B 1 38  ? 44.965 14.033  -65.940 1.00 42.19 ? 36   ASP A CB    1 
ATOM   4760 C CG    . ASP B 1 38  ? 44.755 15.528  -65.706 1.00 46.34 ? 36   ASP A CG    1 
ATOM   4761 O OD1   . ASP B 1 38  ? 44.061 15.883  -64.726 1.00 43.93 ? 36   ASP A OD1   1 
ATOM   4762 O OD2   . ASP B 1 38  ? 45.297 16.341  -66.504 1.00 44.44 ? 36   ASP A OD2   1 
ATOM   4763 N N     . ALA B 1 39  ? 45.283 13.137  -62.996 1.00 38.21 ? 37   ALA A N     1 
ATOM   4764 C CA    . ALA B 1 39  ? 45.458 13.194  -61.525 1.00 39.79 ? 37   ALA A CA    1 
ATOM   4765 C C     . ALA B 1 39  ? 44.918 14.528  -61.002 1.00 39.78 ? 37   ALA A C     1 
ATOM   4766 O O     . ALA B 1 39  ? 44.185 14.515  -59.995 1.00 39.47 ? 37   ALA A O     1 
ATOM   4767 C CB    . ALA B 1 39  ? 46.912 13.017  -61.157 1.00 40.51 ? 37   ALA A CB    1 
ATOM   4768 N N     . GLU B 1 40  ? 45.266 15.624  -61.681 1.00 37.24 ? 38   GLU A N     1 
ATOM   4769 C CA    . GLU B 1 40  ? 44.924 17.018  -61.287 1.00 42.53 ? 38   GLU A CA    1 
ATOM   4770 C C     . GLU B 1 40  ? 43.394 17.196  -61.258 1.00 40.37 ? 38   GLU A C     1 
ATOM   4771 O O     . GLU B 1 40  ? 42.868 17.750  -60.278 1.00 34.56 ? 38   GLU A O     1 
ATOM   4772 C CB    . GLU B 1 40  ? 45.606 17.993  -62.253 1.00 44.34 ? 38   GLU A CB    1 
ATOM   4773 C CG    . GLU B 1 40  ? 45.132 19.435  -62.157 1.00 52.65 ? 38   GLU A CG    1 
ATOM   4774 C CD    . GLU B 1 40  ? 45.801 20.413  -63.125 1.00 59.96 ? 38   GLU A CD    1 
ATOM   4775 O OE1   . GLU B 1 40  ? 46.289 19.979  -64.195 1.00 61.52 ? 38   GLU A OE1   1 
ATOM   4776 O OE2   . GLU B 1 40  ? 45.832 21.622  -62.807 1.00 65.57 ? 38   GLU A OE2   1 
ATOM   4777 N N     . THR B 1 41  ? 42.724 16.787  -62.327 1.00 34.21 ? 39   THR A N     1 
ATOM   4778 C CA    . THR B 1 41  ? 41.251 16.860  -62.511 1.00 38.69 ? 39   THR A CA    1 
ATOM   4779 C C     . THR B 1 41  ? 40.536 16.059  -61.419 1.00 36.76 ? 39   THR A C     1 
ATOM   4780 O O     . THR B 1 41  ? 39.552 16.562  -60.842 1.00 33.95 ? 39   THR A O     1 
ATOM   4781 C CB    . THR B 1 41  ? 40.888 16.294  -63.885 1.00 38.32 ? 39   THR A CB    1 
ATOM   4782 O OG1   . THR B 1 41  ? 41.545 17.199  -64.755 1.00 43.08 ? 39   THR A OG1   1 
ATOM   4783 C CG2   . THR B 1 41  ? 39.406 16.213  -64.180 1.00 44.89 ? 39   THR A CG2   1 
ATOM   4784 N N     . ALA B 1 42  ? 40.964 14.815  -61.241 1.00 33.16 ? 40   ALA A N     1 
ATOM   4785 C CA    . ALA B 1 42  ? 40.418 13.877  -60.246 1.00 32.30 ? 40   ALA A CA    1 
ATOM   4786 C C     . ALA B 1 42  ? 40.523 14.525  -58.865 1.00 32.42 ? 40   ALA A C     1 
ATOM   4787 O O     . ALA B 1 42  ? 39.519 14.550  -58.140 1.00 33.02 ? 40   ALA A O     1 
ATOM   4788 C CB    . ALA B 1 42  ? 41.170 12.576  -60.322 1.00 31.96 ? 40   ALA A CB    1 
ATOM   4789 N N     . ALA B 1 43  ? 41.699 15.060  -58.517 1.00 32.95 ? 41   ALA A N     1 
ATOM   4790 C CA    . ALA B 1 43  ? 41.950 15.707  -57.212 1.00 30.73 ? 41   ALA A CA    1 
ATOM   4791 C C     . ALA B 1 43  ? 40.945 16.851  -57.008 1.00 30.83 ? 41   ALA A C     1 
ATOM   4792 O O     . ALA B 1 43  ? 40.389 16.938  -55.917 1.00 31.35 ? 41   ALA A O     1 
ATOM   4793 C CB    . ALA B 1 43  ? 43.372 16.204  -57.152 1.00 33.56 ? 41   ALA A CB    1 
ATOM   4794 N N     . ALA B 1 44  ? 40.716 17.703  -58.011 1.00 29.52 ? 42   ALA A N     1 
ATOM   4795 C CA    . ALA B 1 44  ? 39.818 18.880  -57.888 1.00 32.85 ? 42   ALA A CA    1 
ATOM   4796 C C     . ALA B 1 44  ? 38.374 18.394  -57.738 1.00 31.84 ? 42   ALA A C     1 
ATOM   4797 O O     . ALA B 1 44  ? 37.614 18.987  -56.977 1.00 28.74 ? 42   ALA A O     1 
ATOM   4798 C CB    . ALA B 1 44  ? 39.946 19.809  -59.068 1.00 34.44 ? 42   ALA A CB    1 
ATOM   4799 N N     . ILE B 1 45  ? 38.024 17.315  -58.424 1.00 31.41 ? 43   ILE A N     1 
ATOM   4800 C CA    . ILE B 1 45  ? 36.656 16.731  -58.309 1.00 31.44 ? 43   ILE A CA    1 
ATOM   4801 C C     . ILE B 1 45  ? 36.434 16.250  -56.863 1.00 28.19 ? 43   ILE A C     1 
ATOM   4802 O O     . ILE B 1 45  ? 35.443 16.652  -56.246 1.00 28.11 ? 43   ILE A O     1 
ATOM   4803 C CB    . ILE B 1 45  ? 36.492 15.643  -59.372 1.00 31.99 ? 43   ILE A CB    1 
ATOM   4804 C CG1   . ILE B 1 45  ? 36.253 16.318  -60.727 1.00 38.59 ? 43   ILE A CG1   1 
ATOM   4805 C CG2   . ILE B 1 45  ? 35.403 14.648  -58.987 1.00 33.44 ? 43   ILE A CG2   1 
ATOM   4806 C CD1   . ILE B 1 45  ? 36.129 15.373  -61.882 1.00 43.00 ? 43   ILE A CD1   1 
ATOM   4807 N N     . LEU B 1 46  ? 37.355 15.467  -56.314 1.00 28.89 ? 44   LEU A N     1 
ATOM   4808 C CA    . LEU B 1 46  ? 37.226 14.971  -54.913 1.00 28.06 ? 44   LEU A CA    1 
ATOM   4809 C C     . LEU B 1 46  ? 37.179 16.145  -53.923 1.00 26.82 ? 44   LEU A C     1 
ATOM   4810 O O     . LEU B 1 46  ? 36.377 16.064  -52.985 1.00 27.26 ? 44   LEU A O     1 
ATOM   4811 C CB    . LEU B 1 46  ? 38.357 14.000  -54.593 1.00 27.77 ? 44   LEU A CB    1 
ATOM   4812 C CG    . LEU B 1 46  ? 38.021 12.523  -54.801 1.00 30.38 ? 44   LEU A CG    1 
ATOM   4813 C CD1   . LEU B 1 46  ? 36.973 12.035  -53.803 1.00 29.48 ? 44   LEU A CD1   1 
ATOM   4814 C CD2   . LEU B 1 46  ? 37.564 12.251  -56.216 1.00 31.79 ? 44   LEU A CD2   1 
ATOM   4815 N N     . GLU B 1 47  ? 38.000 17.192  -54.087 1.00 29.45 ? 45   GLU A N     1 
ATOM   4816 C CA    . GLU B 1 47  ? 38.007 18.312  -53.110 1.00 30.73 ? 45   GLU A CA    1 
ATOM   4817 C C     . GLU B 1 47  ? 36.625 18.960  -53.112 1.00 28.50 ? 45   GLU A C     1 
ATOM   4818 O O     . GLU B 1 47  ? 36.127 19.300  -52.021 1.00 27.93 ? 45   GLU A O     1 
ATOM   4819 C CB    . GLU B 1 47  ? 39.044 19.393  -53.398 1.00 33.98 ? 45   GLU A CB    1 
ATOM   4820 C CG    . GLU B 1 47  ? 40.451 19.003  -53.012 1.00 41.35 ? 45   GLU A CG    1 
ATOM   4821 C CD    . GLU B 1 47  ? 40.734 18.818  -51.526 1.00 43.10 ? 45   GLU A CD    1 
ATOM   4822 O OE1   . GLU B 1 47  ? 40.184 19.587  -50.669 1.00 43.85 ? 45   GLU A OE1   1 
ATOM   4823 O OE2   . GLU B 1 47  ? 41.505 17.896  -51.228 1.00 41.50 ? 45   GLU A OE2   1 
ATOM   4824 N N     . GLU B 1 48  ? 36.048 19.161  -54.287 1.00 27.23 ? 46   GLU A N     1 
ATOM   4825 C CA    . GLU B 1 48  ? 34.714 19.804  -54.391 1.00 29.96 ? 46   GLU A CA    1 
ATOM   4826 C C     . GLU B 1 48  ? 33.655 18.874  -53.774 1.00 26.88 ? 46   GLU A C     1 
ATOM   4827 O O     . GLU B 1 48  ? 32.785 19.361  -53.026 1.00 27.12 ? 46   GLU A O     1 
ATOM   4828 C CB    . GLU B 1 48  ? 34.429 20.177  -55.846 1.00 30.85 ? 46   GLU A CB    1 
ATOM   4829 C CG    . GLU B 1 48  ? 33.128 20.936  -56.032 1.00 35.83 ? 46   GLU A CG    1 
ATOM   4830 C CD    . GLU B 1 48  ? 32.972 22.231  -55.242 1.00 40.58 ? 46   GLU A CD    1 
ATOM   4831 O OE1   . GLU B 1 48  ? 31.807 22.607  -54.980 1.00 45.63 ? 46   GLU A OE1   1 
ATOM   4832 O OE2   . GLU B 1 48  ? 33.999 22.859  -54.882 1.00 39.69 ? 46   GLU A OE2   1 
ATOM   4833 N N     . ALA B 1 49  ? 33.722 17.576  -54.052 1.00 26.41 ? 47   ALA A N     1 
ATOM   4834 C CA    . ALA B 1 49  ? 32.738 16.594  -53.549 1.00 26.85 ? 47   ALA A CA    1 
ATOM   4835 C C     . ALA B 1 49  ? 32.784 16.584  -52.019 1.00 29.45 ? 47   ALA A C     1 
ATOM   4836 O O     . ALA B 1 49  ? 31.713 16.545  -51.380 1.00 28.86 ? 47   ALA A O     1 
ATOM   4837 C CB    . ALA B 1 49  ? 33.032 15.226  -54.103 1.00 27.56 ? 47   ALA A CB    1 
ATOM   4838 N N     . GLY B 1 50  ? 33.994 16.572  -51.453 1.00 30.97 ? 48   GLY A N     1 
ATOM   4839 C CA    . GLY B 1 50  ? 34.202 16.632  -49.997 1.00 29.44 ? 48   GLY A CA    1 
ATOM   4840 C C     . GLY B 1 50  ? 33.570 17.872  -49.399 1.00 28.06 ? 48   GLY A C     1 
ATOM   4841 O O     . GLY B 1 50  ? 33.030 17.773  -48.291 1.00 27.70 ? 48   GLY A O     1 
ATOM   4842 N N     . LYS B 1 51  ? 33.651 18.998  -50.110 1.00 29.52 ? 49   LYS A N     1 
ATOM   4843 C CA    . LYS B 1 51  ? 33.113 20.328  -49.702 1.00 33.63 ? 49   LYS A CA    1 
ATOM   4844 C C     . LYS B 1 51  ? 31.580 20.282  -49.684 1.00 30.58 ? 49   LYS A C     1 
ATOM   4845 O O     . LYS B 1 51  ? 30.979 20.605  -48.650 1.00 27.12 ? 49   LYS A O     1 
ATOM   4846 C CB    . LYS B 1 51  ? 33.563 21.394  -50.703 1.00 38.18 ? 49   LYS A CB    1 
ATOM   4847 C CG    . LYS B 1 51  ? 33.604 22.836  -50.214 1.00 46.96 ? 49   LYS A CG    1 
ATOM   4848 C CD    . LYS B 1 51  ? 34.652 23.679  -50.960 1.00 53.20 ? 49   LYS A CD    1 
ATOM   4849 C CE    . LYS B 1 51  ? 36.083 23.219  -50.710 1.00 60.27 ? 49   LYS A CE    1 
ATOM   4850 N NZ    . LYS B 1 51  ? 37.064 23.776  -51.678 1.00 59.92 ? 49   LYS A NZ    1 
ATOM   4851 N N     . VAL B 1 52  ? 30.977 19.869  -50.788 1.00 30.04 ? 50   VAL A N     1 
ATOM   4852 C CA    . VAL B 1 52  ? 29.491 19.843  -50.904 1.00 31.31 ? 50   VAL A CA    1 
ATOM   4853 C C     . VAL B 1 52  ? 28.956 18.827  -49.888 1.00 28.86 ? 50   VAL A C     1 
ATOM   4854 O O     . VAL B 1 52  ? 27.939 19.129  -49.250 1.00 28.64 ? 50   VAL A O     1 
ATOM   4855 C CB    . VAL B 1 52  ? 29.025 19.547  -52.342 1.00 34.75 ? 50   VAL A CB    1 
ATOM   4856 C CG1   . VAL B 1 52  ? 27.527 19.741  -52.495 1.00 38.58 ? 50   VAL A CG1   1 
ATOM   4857 C CG2   . VAL B 1 52  ? 29.748 20.425  -53.347 1.00 40.33 ? 50   VAL A CG2   1 
ATOM   4858 N N     . THR B 1 53  ? 29.598 17.664  -49.731 1.00 25.89 ? 51   THR A N     1 
ATOM   4859 C CA    . THR B 1 53  ? 29.013 16.586  -48.893 1.00 29.48 ? 51   THR A CA    1 
ATOM   4860 C C     . THR B 1 53  ? 29.045 16.996  -47.419 1.00 29.60 ? 51   THR A C     1 
ATOM   4861 O O     . THR B 1 53  ? 27.992 16.857  -46.760 1.00 27.75 ? 51   THR A O     1 
ATOM   4862 C CB    . THR B 1 53  ? 29.633 15.214  -49.146 1.00 28.46 ? 51   THR A CB    1 
ATOM   4863 O OG1   . THR B 1 53  ? 31.056 15.256  -49.010 1.00 29.63 ? 51   THR A OG1   1 
ATOM   4864 C CG2   . THR B 1 53  ? 29.235 14.709  -50.514 1.00 28.36 ? 51   THR A CG2   1 
ATOM   4865 N N     . ALA B 1 54  ? 30.177 17.514  -46.937 1.00 28.37 ? 52   ALA A N     1 
ATOM   4866 C CA    . ALA B 1 54  ? 30.341 17.935  -45.530 1.00 31.89 ? 52   ALA A CA    1 
ATOM   4867 C C     . ALA B 1 54  ? 29.478 19.166  -45.266 1.00 30.84 ? 52   ALA A C     1 
ATOM   4868 O O     . ALA B 1 54  ? 28.949 19.286  -44.167 1.00 32.36 ? 52   ALA A O     1 
ATOM   4869 C CB    . ALA B 1 54  ? 31.798 18.206  -45.230 1.00 30.64 ? 52   ALA A CB    1 
ATOM   4870 N N     . GLY B 1 55  ? 29.366 20.064  -46.237 1.00 30.29 ? 53   GLY A N     1 
ATOM   4871 C CA    . GLY B 1 55  ? 28.849 21.421  -45.983 1.00 31.21 ? 53   GLY A CA    1 
ATOM   4872 C C     . GLY B 1 55  ? 27.349 21.496  -46.150 1.00 31.82 ? 53   GLY A C     1 
ATOM   4873 O O     . GLY B 1 55  ? 26.729 22.168  -45.369 1.00 33.83 ? 53   GLY A O     1 
ATOM   4874 N N     . THR B 1 56  ? 26.785 20.839  -47.162 1.00 32.75 ? 54   THR A N     1 
ATOM   4875 C CA    . THR B 1 56  ? 25.351 20.964  -47.525 1.00 29.52 ? 54   THR A CA    1 
ATOM   4876 C C     . THR B 1 56  ? 24.592 19.685  -47.171 1.00 28.98 ? 54   THR A C     1 
ATOM   4877 O O     . THR B 1 56  ? 23.431 19.803  -46.762 1.00 30.24 ? 54   THR A O     1 
ATOM   4878 C CB    . THR B 1 56  ? 25.237 21.276  -49.021 1.00 33.41 ? 54   THR A CB    1 
ATOM   4879 O OG1   . THR B 1 56  ? 26.056 22.421  -49.239 1.00 34.81 ? 54   THR A OG1   1 
ATOM   4880 C CG2   . THR B 1 56  ? 23.830 21.566  -49.488 1.00 34.47 ? 54   THR A CG2   1 
ATOM   4881 N N     . ILE B 1 57  ? 25.201 18.503  -47.322 1.00 29.42 ? 55   ILE A N     1 
ATOM   4882 C CA    . ILE B 1 57  ? 24.458 17.209  -47.257 1.00 26.95 ? 55   ILE A CA    1 
ATOM   4883 C C     . ILE B 1 57  ? 24.482 16.667  -45.820 1.00 24.58 ? 55   ILE A C     1 
ATOM   4884 O O     . ILE B 1 57  ? 23.395 16.319  -45.296 1.00 26.12 ? 55   ILE A O     1 
ATOM   4885 C CB    . ILE B 1 57  ? 24.999 16.188  -48.279 1.00 26.91 ? 55   ILE A CB    1 
ATOM   4886 C CG1   . ILE B 1 57  ? 25.068 16.746  -49.702 1.00 30.99 ? 55   ILE A CG1   1 
ATOM   4887 C CG2   . ILE B 1 57  ? 24.197 14.906  -48.225 1.00 24.88 ? 55   ILE A CG2   1 
ATOM   4888 C CD1   . ILE B 1 57  ? 23.752 17.251  -50.239 1.00 33.59 ? 55   ILE A CD1   1 
ATOM   4889 N N     . ALA B 1 58  ? 25.657 16.532  -45.220 1.00 23.74 ? 56   ALA A N     1 
ATOM   4890 C CA    . ALA B 1 58  ? 25.839 15.946  -43.871 1.00 25.65 ? 56   ALA A CA    1 
ATOM   4891 C C     . ALA B 1 58  ? 24.951 16.626  -42.822 1.00 25.26 ? 56   ALA A C     1 
ATOM   4892 O O     . ALA B 1 58  ? 24.366 15.935  -41.994 1.00 26.19 ? 56   ALA A O     1 
ATOM   4893 C CB    . ALA B 1 58  ? 27.290 15.962  -43.477 1.00 24.79 ? 56   ALA A CB    1 
ATOM   4894 N N     . PRO B 1 59  ? 24.813 17.972  -42.802 1.00 24.74 ? 57   PRO A N     1 
ATOM   4895 C CA    . PRO B 1 59  ? 24.015 18.619  -41.770 1.00 26.25 ? 57   PRO A CA    1 
ATOM   4896 C C     . PRO B 1 59  ? 22.523 18.244  -41.791 1.00 25.74 ? 57   PRO A C     1 
ATOM   4897 O O     . PRO B 1 59  ? 21.875 18.458  -40.805 1.00 25.39 ? 57   PRO A O     1 
ATOM   4898 C CB    . PRO B 1 59  ? 24.174 20.117  -42.084 1.00 28.39 ? 57   PRO A CB    1 
ATOM   4899 C CG    . PRO B 1 59  ? 25.457 20.212  -42.853 1.00 28.12 ? 57   PRO A CG    1 
ATOM   4900 C CD    . PRO B 1 59  ? 25.445 18.958  -43.691 1.00 26.97 ? 57   PRO A CD    1 
ATOM   4901 N N     . LEU B 1 60  ? 22.043 17.680  -42.896 1.00 25.35 ? 58   LEU A N     1 
ATOM   4902 C CA    . LEU B 1 60  ? 20.607 17.345  -43.043 1.00 25.70 ? 58   LEU A CA    1 
ATOM   4903 C C     . LEU B 1 60  ? 20.337 15.893  -42.615 1.00 24.54 ? 58   LEU A C     1 
ATOM   4904 O O     . LEU B 1 60  ? 19.173 15.510  -42.582 1.00 25.70 ? 58   LEU A O     1 
ATOM   4905 C CB    . LEU B 1 60  ? 20.234 17.539  -44.514 1.00 27.26 ? 58   LEU A CB    1 
ATOM   4906 C CG    . LEU B 1 60  ? 20.117 18.973  -45.019 1.00 28.46 ? 58   LEU A CG    1 
ATOM   4907 C CD1   . LEU B 1 60  ? 19.941 18.981  -46.528 1.00 28.71 ? 58   LEU A CD1   1 
ATOM   4908 C CD2   . LEU B 1 60  ? 18.951 19.680  -44.353 1.00 30.43 ? 58   LEU A CD2   1 
ATOM   4909 N N     . ASN B 1 61  ? 21.371 15.133  -42.283 1.00 22.93 ? 59   ASN A N     1 
ATOM   4910 C CA    . ASN B 1 61  ? 21.147 13.687  -41.993 1.00 24.23 ? 59   ASN A CA    1 
ATOM   4911 C C     . ASN B 1 61  ? 20.232 13.476  -40.776 1.00 24.01 ? 59   ASN A C     1 
ATOM   4912 O O     . ASN B 1 61  ? 19.212 12.816  -40.926 1.00 24.20 ? 59   ASN A O     1 
ATOM   4913 C CB    . ASN B 1 61  ? 22.455 12.929  -41.806 1.00 25.15 ? 59   ASN A CB    1 
ATOM   4914 C CG    . ASN B 1 61  ? 22.300 11.449  -42.079 1.00 26.95 ? 59   ASN A CG    1 
ATOM   4915 O OD1   . ASN B 1 61  ? 21.342 11.035  -42.721 1.00 26.26 ? 59   ASN A OD1   1 
ATOM   4916 N ND2   . ASN B 1 61  ? 23.235 10.653  -41.596 1.00 25.22 ? 59   ASN A ND2   1 
ATOM   4917 N N     . ARG B 1 62  ? 20.631 13.984  -39.612 1.00 26.23 ? 60   ARG A N     1 
ATOM   4918 C CA    . ARG B 1 62  ? 19.850 13.797  -38.359 1.00 27.44 ? 60   ARG A CA    1 
ATOM   4919 C C     . ARG B 1 62  ? 18.439 14.397  -38.495 1.00 26.30 ? 60   ARG A C     1 
ATOM   4920 O O     . ARG B 1 62  ? 17.481 13.676  -38.252 1.00 26.28 ? 60   ARG A O     1 
ATOM   4921 C CB    . ARG B 1 62  ? 20.627 14.353  -37.160 1.00 31.24 ? 60   ARG A CB    1 
ATOM   4922 C CG    . ARG B 1 62  ? 21.659 13.402  -36.576 1.00 37.21 ? 60   ARG A CG    1 
ATOM   4923 C CD    . ARG B 1 62  ? 21.097 12.629  -35.401 1.00 40.37 ? 60   ARG A CD    1 
ATOM   4924 N NE    . ARG B 1 62  ? 20.193 11.606  -35.890 1.00 38.03 ? 60   ARG A NE    1 
ATOM   4925 C CZ    . ARG B 1 62  ? 18.967 11.403  -35.435 1.00 34.30 ? 60   ARG A CZ    1 
ATOM   4926 N NH1   . ARG B 1 62  ? 18.223 10.450  -35.962 1.00 32.17 ? 60   ARG A NH1   1 
ATOM   4927 N NH2   . ARG B 1 62  ? 18.493 12.145  -34.453 1.00 31.56 ? 60   ARG A NH2   1 
ATOM   4928 N N     . PRO B 1 63  ? 18.273 15.684  -38.860 1.00 27.31 ? 61   PRO A N     1 
ATOM   4929 C CA    . PRO B 1 63  ? 16.938 16.255  -38.977 1.00 28.55 ? 61   PRO A CA    1 
ATOM   4930 C C     . PRO B 1 63  ? 16.081 15.530  -40.029 1.00 28.34 ? 61   PRO A C     1 
ATOM   4931 O O     . PRO B 1 63  ? 14.896 15.467  -39.865 1.00 26.22 ? 61   PRO A O     1 
ATOM   4932 C CB    . PRO B 1 63  ? 17.220 17.724  -39.350 1.00 29.95 ? 61   PRO A CB    1 
ATOM   4933 C CG    . PRO B 1 63  ? 18.610 17.724  -39.925 1.00 29.73 ? 61   PRO A CG    1 
ATOM   4934 C CD    . PRO B 1 63  ? 19.335 16.643  -39.158 1.00 28.42 ? 61   PRO A CD    1 
ATOM   4935 N N     . GLY B 1 64  ? 16.716 15.009  -41.078 1.00 26.22 ? 62   GLY A N     1 
ATOM   4936 C CA    . GLY B 1 64  ? 15.977 14.241  -42.093 1.00 25.72 ? 62   GLY A CA    1 
ATOM   4937 C C     . GLY B 1 64  ? 15.372 12.973  -41.513 1.00 23.57 ? 62   GLY A C     1 
ATOM   4938 O O     . GLY B 1 64  ? 14.215 12.681  -41.811 1.00 26.57 ? 62   GLY A O     1 
ATOM   4939 N N     . ASP B 1 65  ? 16.131 12.265  -40.690 1.00 24.83 ? 63   ASP A N     1 
ATOM   4940 C CA    . ASP B 1 65  ? 15.618 11.031  -40.042 1.00 26.11 ? 63   ASP A CA    1 
ATOM   4941 C C     . ASP B 1 65  ? 14.481 11.388  -39.082 1.00 27.40 ? 63   ASP A C     1 
ATOM   4942 O O     . ASP B 1 65  ? 13.501 10.651  -39.032 1.00 25.43 ? 63   ASP A O     1 
ATOM   4943 C CB    . ASP B 1 65  ? 16.715 10.298  -39.277 1.00 24.32 ? 63   ASP A CB    1 
ATOM   4944 C CG    . ASP B 1 65  ? 16.199 9.127   -38.464 1.00 26.69 ? 63   ASP A CG    1 
ATOM   4945 O OD1   . ASP B 1 65  ? 15.970 8.064   -39.060 1.00 27.45 ? 63   ASP A OD1   1 
ATOM   4946 O OD2   . ASP B 1 65  ? 16.029 9.292   -37.248 1.00 25.06 ? 63   ASP A OD2   1 
ATOM   4947 N N     . GLU B 1 66  ? 14.621 12.496  -38.362 1.00 27.30 ? 64   GLU A N     1 
ATOM   4948 C CA    . GLU B 1 66  ? 13.620 12.850  -37.323 1.00 25.46 ? 64   GLU A CA    1 
ATOM   4949 C C     . GLU B 1 66  ? 12.311 13.345  -37.968 1.00 28.73 ? 64   GLU A C     1 
ATOM   4950 O O     . GLU B 1 66  ? 11.258 13.113  -37.382 1.00 24.52 ? 64   GLU A O     1 
ATOM   4951 C CB    . GLU B 1 66  ? 14.241 13.862  -36.358 1.00 27.79 ? 64   GLU A CB    1 
ATOM   4952 C CG    . GLU B 1 66  ? 15.423 13.301  -35.595 1.00 28.28 ? 64   GLU A CG    1 
ATOM   4953 C CD    . GLU B 1 66  ? 15.037 12.280  -34.542 1.00 29.15 ? 64   GLU A CD    1 
ATOM   4954 O OE1   . GLU B 1 66  ? 13.884 12.322  -34.089 1.00 29.24 ? 64   GLU A OE1   1 
ATOM   4955 O OE2   . GLU B 1 66  ? 15.885 11.451  -34.186 1.00 25.73 ? 64   GLU A OE2   1 
ATOM   4956 N N     . GLU B 1 67  ? 12.398 13.988  -39.135 1.00 27.83 ? 65   GLU A N     1 
ATOM   4957 C CA    . GLU B 1 67  ? 11.193 14.516  -39.818 1.00 27.97 ? 65   GLU A CA    1 
ATOM   4958 C C     . GLU B 1 67  ? 10.584 13.450  -40.737 1.00 30.06 ? 65   GLU A C     1 
ATOM   4959 O O     . GLU B 1 67  ? 9.364  13.289  -40.715 1.00 25.83 ? 65   GLU A O     1 
ATOM   4960 C CB    . GLU B 1 67  ? 11.541 15.757  -40.635 1.00 31.72 ? 65   GLU A CB    1 
ATOM   4961 C CG    . GLU B 1 67  ? 10.383 16.259  -41.477 1.00 37.12 ? 65   GLU A CG    1 
ATOM   4962 C CD    . GLU B 1 67  ? 10.572 17.617  -42.133 1.00 36.82 ? 65   GLU A CD    1 
ATOM   4963 O OE1   . GLU B 1 67  ? 9.586  18.157  -42.653 1.00 39.10 ? 65   GLU A OE1   1 
ATOM   4964 O OE2   . GLU B 1 67  ? 11.698 18.121  -42.130 1.00 34.07 ? 65   GLU A OE2   1 
ATOM   4965 N N     . GLY B 1 68  ? 11.414 12.781  -41.539 1.00 27.62 ? 66   GLY A N     1 
ATOM   4966 C CA    . GLY B 1 68  ? 10.908 11.799  -42.507 1.00 25.60 ? 66   GLY A CA    1 
ATOM   4967 C C     . GLY B 1 68  ? 10.191 12.502  -43.643 1.00 28.84 ? 66   GLY A C     1 
ATOM   4968 O O     . GLY B 1 68  ? 10.203 13.742  -43.714 1.00 27.82 ? 66   GLY A O     1 
ATOM   4969 N N     . CYS B 1 69  ? 9.647  11.728  -44.564 1.00 27.41 ? 67   CYS A N     1 
ATOM   4970 C CA    . CYS B 1 69  ? 8.880  12.229  -45.715 1.00 28.47 ? 67   CYS A CA    1 
ATOM   4971 C C     . CYS B 1 69  ? 7.405  12.320  -45.318 1.00 28.08 ? 67   CYS A C     1 
ATOM   4972 O O     . CYS B 1 69  ? 6.995  11.606  -44.399 1.00 28.95 ? 67   CYS A O     1 
ATOM   4973 C CB    . CYS B 1 69  ? 9.073  11.330  -46.921 1.00 27.70 ? 67   CYS A CB    1 
ATOM   4974 S SG    . CYS B 1 69  ? 10.755 11.427  -47.584 1.00 26.00 ? 67   CYS A SG    1 
ATOM   4975 N N     . GLN B 1 70  ? 6.658  13.149  -46.033 1.00 31.68 ? 68   GLN A N     1 
ATOM   4976 C CA    . GLN B 1 70  ? 5.213  13.365  -45.827 1.00 31.41 ? 68   GLN A CA    1 
ATOM   4977 C C     . GLN B 1 70  ? 4.489  13.061  -47.138 1.00 27.85 ? 68   GLN A C     1 
ATOM   4978 O O     . GLN B 1 70  ? 5.030  13.335  -48.201 1.00 27.35 ? 68   GLN A O     1 
ATOM   4979 C CB    . GLN B 1 70  ? 4.954  14.820  -45.436 1.00 37.60 ? 68   GLN A CB    1 
ATOM   4980 C CG    . GLN B 1 70  ? 5.577  15.237  -44.120 1.00 44.41 ? 68   GLN A CG    1 
ATOM   4981 C CD    . GLN B 1 70  ? 4.600  15.000  -43.002 1.00 54.37 ? 68   GLN A CD    1 
ATOM   4982 O OE1   . GLN B 1 70  ? 3.814  15.884  -42.660 1.00 67.93 ? 68   GLN A OE1   1 
ATOM   4983 N NE2   . GLN B 1 70  ? 4.595  13.783  -42.475 1.00 55.83 ? 68   GLN A NE2   1 
ATOM   4984 N N     . TRP B 1 71  ? 3.261  12.581  -47.034 1.00 28.53 ? 69   TRP A N     1 
ATOM   4985 C CA    . TRP B 1 71  ? 2.371  12.264  -48.170 1.00 28.57 ? 69   TRP A CA    1 
ATOM   4986 C C     . TRP B 1 71  ? 1.132  13.145  -47.994 1.00 31.26 ? 69   TRP A C     1 
ATOM   4987 O O     . TRP B 1 71  ? 0.524  13.065  -46.915 1.00 29.41 ? 69   TRP A O     1 
ATOM   4988 C CB    . TRP B 1 71  ? 2.039  10.763  -48.149 1.00 27.87 ? 69   TRP A CB    1 
ATOM   4989 C CG    . TRP B 1 71  ? 1.265  10.264  -49.329 1.00 29.16 ? 69   TRP A CG    1 
ATOM   4990 C CD1   . TRP B 1 71  ? 1.775  9.648   -50.437 1.00 29.25 ? 69   TRP A CD1   1 
ATOM   4991 C CD2   . TRP B 1 71  ? -0.160 10.343  -49.540 1.00 29.03 ? 69   TRP A CD2   1 
ATOM   4992 N NE1   . TRP B 1 71  ? 0.773  9.343   -51.322 1.00 27.89 ? 69   TRP A NE1   1 
ATOM   4993 C CE2   . TRP B 1 71  ? -0.427 9.744   -50.796 1.00 28.55 ? 69   TRP A CE2   1 
ATOM   4994 C CE3   . TRP B 1 71  ? -1.234 10.873  -48.808 1.00 31.85 ? 69   TRP A CE3   1 
ATOM   4995 C CZ2   . TRP B 1 71  ? -1.725 9.611   -51.307 1.00 28.03 ? 69   TRP A CZ2   1 
ATOM   4996 C CZ3   . TRP B 1 71  ? -2.517 10.746  -49.314 1.00 29.54 ? 69   TRP A CZ3   1 
ATOM   4997 C CH2   . TRP B 1 71  ? -2.752 10.136  -50.555 1.00 28.64 ? 69   TRP A CH2   1 
ATOM   4998 N N     . ASN B 1 72  ? 0.822  13.981  -48.984 1.00 33.75 ? 70   ASN A N     1 
ATOM   4999 C CA    . ASN B 1 72  ? -0.330 14.921  -48.960 1.00 34.21 ? 70   ASN A CA    1 
ATOM   5000 C C     . ASN B 1 72  ? -1.019 14.813  -50.315 1.00 30.75 ? 70   ASN A C     1 
ATOM   5001 O O     . ASN B 1 72  ? -0.471 15.335  -51.329 1.00 28.88 ? 70   ASN A O     1 
ATOM   5002 C CB    . ASN B 1 72  ? 0.099  16.347  -48.598 1.00 37.41 ? 70   ASN A CB    1 
ATOM   5003 C CG    . ASN B 1 72  ? 0.706  16.427  -47.208 1.00 45.48 ? 70   ASN A CG    1 
ATOM   5004 O OD1   . ASN B 1 72  ? 1.928  16.497  -47.041 1.00 49.09 ? 70   ASN A OD1   1 
ATOM   5005 N ND2   . ASN B 1 72  ? -0.134 16.396  -46.191 1.00 43.84 ? 70   ASN A ND2   1 
ATOM   5006 N N     . ALA B 1 73  ? -2.153 14.114  -50.344 1.00 32.87 ? 71   ALA A N     1 
ATOM   5007 C CA    . ALA B 1 73  ? -2.993 13.959  -51.552 1.00 32.31 ? 71   ALA A CA    1 
ATOM   5008 C C     . ALA B 1 73  ? -2.108 13.578  -52.737 1.00 31.75 ? 71   ALA A C     1 
ATOM   5009 O O     . ALA B 1 73  ? -2.171 14.284  -53.774 1.00 31.97 ? 71   ALA A O     1 
ATOM   5010 C CB    . ALA B 1 73  ? -3.707 15.267  -51.832 1.00 35.61 ? 71   ALA A CB    1 
ATOM   5011 N N     . GLY B 1 74  ? -1.275 12.543  -52.597 1.00 30.22 ? 72   GLY A N     1 
ATOM   5012 C CA    . GLY B 1 74  ? -0.500 11.980  -53.722 1.00 28.57 ? 72   GLY A CA    1 
ATOM   5013 C C     . GLY B 1 74  ? 0.868  12.626  -53.867 1.00 29.08 ? 72   GLY A C     1 
ATOM   5014 O O     . GLY B 1 74  ? 1.720  12.017  -54.513 1.00 30.31 ? 72   GLY A O     1 
ATOM   5015 N N     . ALA B 1 75  ? 1.080  13.822  -53.309 1.00 27.18 ? 73   ALA A N     1 
ATOM   5016 C CA    . ALA B 1 75  ? 2.368  14.551  -53.387 1.00 27.67 ? 73   ALA A CA    1 
ATOM   5017 C C     . ALA B 1 75  ? 3.236  14.128  -52.201 1.00 27.96 ? 73   ALA A C     1 
ATOM   5018 O O     . ALA B 1 75  ? 2.738  14.076  -51.060 1.00 30.88 ? 73   ALA A O     1 
ATOM   5019 C CB    . ALA B 1 75  ? 2.164  16.053  -53.407 1.00 28.30 ? 73   ALA A CB    1 
ATOM   5020 N N     . VAL B 1 76  ? 4.503  13.827  -52.460 1.00 26.45 ? 74   VAL A N     1 
ATOM   5021 C CA    . VAL B 1 76  ? 5.461  13.449  -51.392 1.00 26.81 ? 74   VAL A CA    1 
ATOM   5022 C C     . VAL B 1 76  ? 6.477  14.565  -51.218 1.00 25.96 ? 74   VAL A C     1 
ATOM   5023 O O     . VAL B 1 76  ? 7.073  15.034  -52.204 1.00 29.33 ? 74   VAL A O     1 
ATOM   5024 C CB    . VAL B 1 76  ? 6.159  12.124  -51.706 1.00 26.75 ? 74   VAL A CB    1 
ATOM   5025 C CG1   . VAL B 1 76  ? 7.284  11.841  -50.727 1.00 28.79 ? 74   VAL A CG1   1 
ATOM   5026 C CG2   . VAL B 1 76  ? 5.155  10.986  -51.790 1.00 26.53 ? 74   VAL A CG2   1 
ATOM   5027 N N     . SER B 1 77  ? 6.679  14.965  -49.985 1.00 26.62 ? 75   SER A N     1 
ATOM   5028 C CA    . SER B 1 77  ? 7.642  16.034  -49.668 1.00 29.48 ? 75   SER A CA    1 
ATOM   5029 C C     . SER B 1 77  ? 8.759  15.376  -48.863 1.00 27.55 ? 75   SER A C     1 
ATOM   5030 O O     . SER B 1 77  ? 8.452  14.520  -48.001 1.00 26.77 ? 75   SER A O     1 
ATOM   5031 C CB    . SER B 1 77  ? 6.959  17.178  -48.970 1.00 30.19 ? 75   SER A CB    1 
ATOM   5032 O OG    . SER B 1 77  ? 6.389  16.708  -47.769 1.00 40.25 ? 75   SER A OG    1 
ATOM   5033 N N     . THR B 1 78  ? 10.006 15.702  -49.214 1.00 25.92 ? 76   THR A N     1 
ATOM   5034 C CA    . THR B 1 78  ? 11.224 15.321  -48.450 1.00 25.73 ? 76   THR A CA    1 
ATOM   5035 C C     . THR B 1 78  ? 11.382 16.266  -47.265 1.00 25.46 ? 76   THR A C     1 
ATOM   5036 O O     . THR B 1 78  ? 10.706 17.291  -47.205 1.00 26.00 ? 76   THR A O     1 
ATOM   5037 C CB    . THR B 1 78  ? 12.443 15.312  -49.383 1.00 24.69 ? 76   THR A CB    1 
ATOM   5038 O OG1   . THR B 1 78  ? 12.565 16.617  -49.952 1.00 24.17 ? 76   THR A OG1   1 
ATOM   5039 C CG2   . THR B 1 78  ? 12.304 14.261  -50.465 1.00 24.99 ? 76   THR A CG2   1 
ATOM   5040 N N     . PRO B 1 79  ? 12.256 15.955  -46.280 1.00 24.73 ? 77   PRO A N     1 
ATOM   5041 C CA    . PRO B 1 79  ? 12.488 16.850  -45.161 1.00 25.37 ? 77   PRO A CA    1 
ATOM   5042 C C     . PRO B 1 79  ? 12.984 18.231  -45.592 1.00 28.36 ? 77   PRO A C     1 
ATOM   5043 O O     . PRO B 1 79  ? 13.518 18.404  -46.714 1.00 25.68 ? 77   PRO A O     1 
ATOM   5044 C CB    . PRO B 1 79  ? 13.540 16.119  -44.318 1.00 25.82 ? 77   PRO A CB    1 
ATOM   5045 C CG    . PRO B 1 79  ? 13.312 14.664  -44.638 1.00 25.13 ? 77   PRO A CG    1 
ATOM   5046 C CD    . PRO B 1 79  ? 12.978 14.688  -46.115 1.00 25.10 ? 77   PRO A CD    1 
ATOM   5047 N N     . ALA B 1 80  ? 12.758 19.191  -44.704 1.00 28.97 ? 78   ALA A N     1 
ATOM   5048 C CA    . ALA B 1 80  ? 13.183 20.600  -44.856 1.00 31.00 ? 78   ALA A CA    1 
ATOM   5049 C C     . ALA B 1 80  ? 14.633 20.639  -45.364 1.00 27.66 ? 78   ALA A C     1 
ATOM   5050 O O     . ALA B 1 80  ? 15.501 19.905  -44.814 1.00 26.72 ? 78   ALA A O     1 
ATOM   5051 C CB    . ALA B 1 80  ? 13.036 21.288  -43.518 1.00 30.35 ? 78   ALA A CB    1 
ATOM   5052 N N     . GLY B 1 81  ? 14.901 21.449  -46.384 1.00 30.90 ? 79   GLY A N     1 
ATOM   5053 C CA    . GLY B 1 81  ? 16.263 21.656  -46.914 1.00 28.94 ? 79   GLY A CA    1 
ATOM   5054 C C     . GLY B 1 81  ? 16.696 20.613  -47.942 1.00 30.10 ? 79   GLY A C     1 
ATOM   5055 O O     . GLY B 1 81  ? 17.738 20.847  -48.577 1.00 27.04 ? 79   GLY A O     1 
ATOM   5056 N N     . PHE B 1 82  ? 15.973 19.498  -48.132 1.00 28.68 ? 80   PHE A N     1 
ATOM   5057 C CA    . PHE B 1 82  ? 16.409 18.430  -49.082 1.00 26.48 ? 80   PHE A CA    1 
ATOM   5058 C C     . PHE B 1 82  ? 16.300 18.929  -50.514 1.00 25.59 ? 80   PHE A C     1 
ATOM   5059 O O     . PHE B 1 82  ? 17.271 18.826  -51.262 1.00 27.64 ? 80   PHE A O     1 
ATOM   5060 C CB    . PHE B 1 82  ? 15.661 17.112  -48.872 1.00 25.63 ? 80   PHE A CB    1 
ATOM   5061 C CG    . PHE B 1 82  ? 16.327 16.179  -47.900 1.00 25.79 ? 80   PHE A CG    1 
ATOM   5062 C CD1   . PHE B 1 82  ? 16.496 16.545  -46.572 1.00 24.03 ? 80   PHE A CD1   1 
ATOM   5063 C CD2   . PHE B 1 82  ? 16.691 14.894  -48.285 1.00 25.19 ? 80   PHE A CD2   1 
ATOM   5064 C CE1   . PHE B 1 82  ? 17.076 15.679  -45.665 1.00 23.97 ? 80   PHE A CE1   1 
ATOM   5065 C CE2   . PHE B 1 82  ? 17.280 14.027  -47.377 1.00 24.91 ? 80   PHE A CE2   1 
ATOM   5066 C CZ    . PHE B 1 82  ? 17.473 14.419  -46.067 1.00 25.82 ? 80   PHE A CZ    1 
ATOM   5067 N N     . PRO B 1 83  ? 15.151 19.498  -50.951 1.00 25.28 ? 81   PRO A N     1 
ATOM   5068 C CA    . PRO B 1 83  ? 15.043 20.050  -52.297 1.00 28.37 ? 81   PRO A CA    1 
ATOM   5069 C C     . PRO B 1 83  ? 16.120 21.097  -52.632 1.00 28.46 ? 81   PRO A C     1 
ATOM   5070 O O     . PRO B 1 83  ? 16.623 21.083  -53.733 1.00 27.86 ? 81   PRO A O     1 
ATOM   5071 C CB    . PRO B 1 83  ? 13.638 20.672  -52.318 1.00 27.93 ? 81   PRO A CB    1 
ATOM   5072 C CG    . PRO B 1 83  ? 12.876 19.874  -51.301 1.00 27.25 ? 81   PRO A CG    1 
ATOM   5073 C CD    . PRO B 1 83  ? 13.886 19.607  -50.213 1.00 27.30 ? 81   PRO A CD    1 
ATOM   5074 N N     . GLU B 1 84  ? 16.469 21.964  -51.686 1.00 31.49 ? 82   GLU A N     1 
ATOM   5075 C CA    . GLU B 1 84  ? 17.491 23.036  -51.899 1.00 32.11 ? 82   GLU A CA    1 
ATOM   5076 C C     . GLU B 1 84  ? 18.857 22.348  -52.044 1.00 30.37 ? 82   GLU A C     1 
ATOM   5077 O O     . GLU B 1 84  ? 19.600 22.656  -52.973 1.00 27.66 ? 82   GLU A O     1 
ATOM   5078 C CB    . GLU B 1 84  ? 17.464 24.045  -50.746 1.00 35.31 ? 82   GLU A CB    1 
ATOM   5079 C CG    . GLU B 1 84  ? 16.128 24.799  -50.604 1.00 41.11 ? 82   GLU A CG    1 
ATOM   5080 C CD    . GLU B 1 84  ? 14.855 24.070  -50.111 1.00 43.35 ? 82   GLU A CD    1 
ATOM   5081 O OE1   . GLU B 1 84  ? 13.757 24.612  -50.369 1.00 50.38 ? 82   GLU A OE1   1 
ATOM   5082 O OE2   . GLU B 1 84  ? 14.917 22.960  -49.509 1.00 33.64 ? 82   GLU A OE2   1 
ATOM   5083 N N     . ALA B 1 85  ? 19.155 21.395  -51.170 1.00 29.30 ? 83   ALA A N     1 
ATOM   5084 C CA    . ALA B 1 85  ? 20.447 20.676  -51.194 1.00 29.45 ? 83   ALA A CA    1 
ATOM   5085 C C     . ALA B 1 85  ? 20.533 19.856  -52.476 1.00 26.97 ? 83   ALA A C     1 
ATOM   5086 O O     . ALA B 1 85  ? 21.606 19.841  -53.096 1.00 24.77 ? 83   ALA A O     1 
ATOM   5087 C CB    . ALA B 1 85  ? 20.606 19.823  -49.968 1.00 30.12 ? 83   ALA A CB    1 
ATOM   5088 N N     . TYR B 1 86  ? 19.421 19.275  -52.928 1.00 26.99 ? 84   TYR A N     1 
ATOM   5089 C CA    . TYR B 1 86  ? 19.409 18.512  -54.199 1.00 27.24 ? 84   TYR A CA    1 
ATOM   5090 C C     . TYR B 1 86  ? 19.723 19.460  -55.371 1.00 28.04 ? 84   TYR A C     1 
ATOM   5091 O O     . TYR B 1 86  ? 20.497 19.105  -56.260 1.00 29.20 ? 84   TYR A O     1 
ATOM   5092 C CB    . TYR B 1 86  ? 18.101 17.749  -54.429 1.00 26.37 ? 84   TYR A CB    1 
ATOM   5093 C CG    . TYR B 1 86  ? 18.169 17.019  -55.737 1.00 24.81 ? 84   TYR A CG    1 
ATOM   5094 C CD1   . TYR B 1 86  ? 18.747 15.757  -55.839 1.00 25.50 ? 84   TYR A CD1   1 
ATOM   5095 C CD2   . TYR B 1 86  ? 17.747 17.641  -56.896 1.00 25.90 ? 84   TYR A CD2   1 
ATOM   5096 C CE1   . TYR B 1 86  ? 18.860 15.123  -57.069 1.00 27.10 ? 84   TYR A CE1   1 
ATOM   5097 C CE2   . TYR B 1 86  ? 17.887 17.038  -58.132 1.00 24.77 ? 84   TYR A CE2   1 
ATOM   5098 C CZ    . TYR B 1 86  ? 18.411 15.760  -58.215 1.00 24.08 ? 84   TYR A CZ    1 
ATOM   5099 O OH    . TYR B 1 86  ? 18.504 15.198  -59.450 1.00 25.11 ? 84   TYR A OH    1 
ATOM   5100 N N     . ARG B 1 87  ? 19.156 20.654  -55.372 1.00 30.49 ? 85   ARG A N     1 
ATOM   5101 C CA    . ARG B 1 87  ? 19.311 21.614  -56.497 1.00 33.90 ? 85   ARG A CA    1 
ATOM   5102 C C     . ARG B 1 87  ? 20.799 22.005  -56.623 1.00 32.61 ? 85   ARG A C     1 
ATOM   5103 O O     . ARG B 1 87  ? 21.331 21.992  -57.748 1.00 29.89 ? 85   ARG A O     1 
ATOM   5104 C CB    . ARG B 1 87  ? 18.329 22.766  -56.275 1.00 38.12 ? 85   ARG A CB    1 
ATOM   5105 C CG    . ARG B 1 87  ? 18.520 23.978  -57.169 1.00 47.15 ? 85   ARG A CG    1 
ATOM   5106 C CD    . ARG B 1 87  ? 17.908 25.188  -56.481 1.00 55.13 ? 85   ARG A CD    1 
ATOM   5107 N NE    . ARG B 1 87  ? 17.366 26.120  -57.454 1.00 69.53 ? 85   ARG A NE    1 
ATOM   5108 C CZ    . ARG B 1 87  ? 17.800 27.360  -57.676 1.00 76.78 ? 85   ARG A CZ    1 
ATOM   5109 N NH1   . ARG B 1 87  ? 17.212 28.091  -58.609 1.00 79.47 ? 85   ARG A NH1   1 
ATOM   5110 N NH2   . ARG B 1 87  ? 18.805 27.870  -56.978 1.00 81.72 ? 85   ARG A NH2   1 
ATOM   5111 N N     . THR B 1 88  ? 21.463 22.307  -55.510 1.00 31.44 ? 86   THR A N     1 
ATOM   5112 C CA    . THR B 1 88  ? 22.910 22.641  -55.431 1.00 31.03 ? 86   THR A CA    1 
ATOM   5113 C C     . THR B 1 88  ? 23.719 21.454  -55.958 1.00 29.95 ? 86   THR A C     1 
ATOM   5114 O O     . THR B 1 88  ? 24.616 21.642  -56.786 1.00 31.77 ? 86   THR A O     1 
ATOM   5115 C CB    . THR B 1 88  ? 23.281 22.947  -53.975 1.00 32.67 ? 86   THR A CB    1 
ATOM   5116 O OG1   . THR B 1 88  ? 22.528 24.096  -53.603 1.00 38.67 ? 86   THR A OG1   1 
ATOM   5117 C CG2   . THR B 1 88  ? 24.752 23.211  -53.744 1.00 37.27 ? 86   THR A CG2   1 
ATOM   5118 N N     . TYR B 1 89  ? 23.427 20.269  -55.445 1.00 25.48 ? 87   TYR A N     1 
ATOM   5119 C CA    . TYR B 1 89  ? 24.105 19.022  -55.843 1.00 27.38 ? 87   TYR A CA    1 
ATOM   5120 C C     . TYR B 1 89  ? 24.031 18.879  -57.368 1.00 27.40 ? 87   TYR A C     1 
ATOM   5121 O O     . TYR B 1 89  ? 25.082 18.678  -57.992 1.00 28.09 ? 87   TYR A O     1 
ATOM   5122 C CB    . TYR B 1 89  ? 23.474 17.862  -55.084 1.00 25.77 ? 87   TYR A CB    1 
ATOM   5123 C CG    . TYR B 1 89  ? 24.225 16.559  -55.158 1.00 26.03 ? 87   TYR A CG    1 
ATOM   5124 C CD1   . TYR B 1 89  ? 25.370 16.348  -54.404 1.00 25.98 ? 87   TYR A CD1   1 
ATOM   5125 C CD2   . TYR B 1 89  ? 23.777 15.531  -55.977 1.00 25.96 ? 87   TYR A CD2   1 
ATOM   5126 C CE1   . TYR B 1 89  ? 26.056 15.149  -54.473 1.00 27.26 ? 87   TYR A CE1   1 
ATOM   5127 C CE2   . TYR B 1 89  ? 24.441 14.318  -56.037 1.00 25.58 ? 87   TYR A CE2   1 
ATOM   5128 C CZ    . TYR B 1 89  ? 25.581 14.132  -55.284 1.00 28.86 ? 87   TYR A CZ    1 
ATOM   5129 O OH    . TYR B 1 89  ? 26.256 12.951  -55.373 1.00 31.02 ? 87   TYR A OH    1 
ATOM   5130 N N     . ALA B 1 90  ? 22.832 19.024  -57.939 1.00 27.00 ? 88   ALA A N     1 
ATOM   5131 C CA    . ALA B 1 90  ? 22.546 18.756  -59.363 1.00 29.04 ? 88   ALA A CA    1 
ATOM   5132 C C     . ALA B 1 90  ? 23.225 19.822  -60.223 1.00 31.92 ? 88   ALA A C     1 
ATOM   5133 O O     . ALA B 1 90  ? 23.870 19.425  -61.215 1.00 29.25 ? 88   ALA A O     1 
ATOM   5134 C CB    . ALA B 1 90  ? 21.064 18.689  -59.619 1.00 30.45 ? 88   ALA A CB    1 
ATOM   5135 N N     . GLU B 1 91  ? 23.112 21.095  -59.826 1.00 33.04 ? 89   GLU A N     1 
ATOM   5136 C CA    . GLU B 1 91  ? 23.759 22.245  -60.510 1.00 36.70 ? 89   GLU A CA    1 
ATOM   5137 C C     . GLU B 1 91  ? 25.291 22.085  -60.474 1.00 34.98 ? 89   GLU A C     1 
ATOM   5138 O O     . GLU B 1 91  ? 25.952 22.476  -61.456 1.00 33.61 ? 89   GLU A O     1 
ATOM   5139 C CB    . GLU B 1 91  ? 23.264 23.559  -59.901 1.00 39.94 ? 89   GLU A CB    1 
ATOM   5140 C CG    . GLU B 1 91  ? 21.822 23.844  -60.288 1.00 47.99 ? 89   GLU A CG    1 
ATOM   5141 C CD    . GLU B 1 91  ? 21.193 25.139  -59.800 1.00 52.27 ? 89   GLU A CD    1 
ATOM   5142 O OE1   . GLU B 1 91  ? 19.982 25.355  -60.091 1.00 51.64 ? 89   GLU A OE1   1 
ATOM   5143 O OE2   . GLU B 1 91  ? 21.903 25.926  -59.143 1.00 57.18 ? 89   GLU A OE2   1 
ATOM   5144 N N     . GLY B 1 92  ? 25.840 21.515  -59.407 1.00 31.79 ? 90   GLY A N     1 
ATOM   5145 C CA    . GLY B 1 92  ? 27.273 21.174  -59.314 1.00 31.43 ? 90   GLY A CA    1 
ATOM   5146 C C     . GLY B 1 92  ? 27.708 20.084  -60.298 1.00 32.73 ? 90   GLY A C     1 
ATOM   5147 O O     . GLY B 1 92  ? 28.926 19.876  -60.413 1.00 33.43 ? 90   GLY A O     1 
ATOM   5148 N N     . GLY B 1 93  ? 26.783 19.388  -60.968 1.00 31.44 ? 91   GLY A N     1 
ATOM   5149 C CA    . GLY B 1 93  ? 27.079 18.294  -61.920 1.00 31.96 ? 91   GLY A CA    1 
ATOM   5150 C C     . GLY B 1 93  ? 27.170 16.915  -61.276 1.00 33.20 ? 91   GLY A C     1 
ATOM   5151 O O     . GLY B 1 93  ? 27.534 15.949  -61.988 1.00 31.28 ? 91   GLY A O     1 
ATOM   5152 N N     . TRP B 1 94  ? 26.824 16.787  -59.990 1.00 30.48 ? 92   TRP A N     1 
ATOM   5153 C CA    . TRP B 1 94  ? 27.127 15.566  -59.201 1.00 31.15 ? 92   TRP A CA    1 
ATOM   5154 C C     . TRP B 1 94  ? 26.211 14.409  -59.619 1.00 27.61 ? 92   TRP A C     1 
ATOM   5155 O O     . TRP B 1 94  ? 26.615 13.244  -59.443 1.00 28.92 ? 92   TRP A O     1 
ATOM   5156 C CB    . TRP B 1 94  ? 27.103 15.859  -57.687 1.00 30.62 ? 92   TRP A CB    1 
ATOM   5157 C CG    . TRP B 1 94  ? 28.167 16.844  -57.339 1.00 30.65 ? 92   TRP A CG    1 
ATOM   5158 C CD1   . TRP B 1 94  ? 28.018 18.148  -56.977 1.00 30.27 ? 92   TRP A CD1   1 
ATOM   5159 C CD2   . TRP B 1 94  ? 29.581 16.621  -57.479 1.00 30.24 ? 92   TRP A CD2   1 
ATOM   5160 N NE1   . TRP B 1 94  ? 29.241 18.742  -56.857 1.00 30.98 ? 92   TRP A NE1   1 
ATOM   5161 C CE2   . TRP B 1 94  ? 30.219 17.830  -57.159 1.00 31.26 ? 92   TRP A CE2   1 
ATOM   5162 C CE3   . TRP B 1 94  ? 30.355 15.513  -57.845 1.00 31.44 ? 92   TRP A CE3   1 
ATOM   5163 C CZ2   . TRP B 1 94  ? 31.608 17.956  -57.176 1.00 32.21 ? 92   TRP A CZ2   1 
ATOM   5164 C CZ3   . TRP B 1 94  ? 31.725 15.635  -57.867 1.00 31.62 ? 92   TRP A CZ3   1 
ATOM   5165 C CH2   . TRP B 1 94  ? 32.339 16.848  -57.547 1.00 33.09 ? 92   TRP A CH2   1 
ATOM   5166 N N     . VAL B 1 95  ? 25.027 14.677  -60.151 1.00 27.26 ? 93   VAL A N     1 
ATOM   5167 C CA    . VAL B 1 95  ? 24.136 13.555  -60.574 1.00 27.24 ? 93   VAL A CA    1 
ATOM   5168 C C     . VAL B 1 95  ? 24.714 12.849  -61.803 1.00 27.60 ? 93   VAL A C     1 
ATOM   5169 O O     . VAL B 1 95  ? 24.523 11.615  -61.931 1.00 30.68 ? 93   VAL A O     1 
ATOM   5170 C CB    . VAL B 1 95  ? 22.694 14.036  -60.797 1.00 29.36 ? 93   VAL A CB    1 
ATOM   5171 C CG1   . VAL B 1 95  ? 21.778 12.855  -61.119 1.00 27.95 ? 93   VAL A CG1   1 
ATOM   5172 C CG2   . VAL B 1 95  ? 22.198 14.799  -59.567 1.00 29.15 ? 93   VAL A CG2   1 
ATOM   5173 N N     . GLY B 1 96  ? 25.461 13.567  -62.642 1.00 27.50 ? 94   GLY A N     1 
ATOM   5174 C CA    . GLY B 1 96  ? 25.965 13.019  -63.917 1.00 30.91 ? 94   GLY A CA    1 
ATOM   5175 C C     . GLY B 1 96  ? 27.480 12.888  -63.954 1.00 30.56 ? 94   GLY A C     1 
ATOM   5176 O O     . GLY B 1 96  ? 28.033 12.791  -65.061 1.00 26.74 ? 94   GLY A O     1 
ATOM   5177 N N     . VAL B 1 97  ? 28.124 12.840  -62.790 1.00 31.14 ? 95   VAL A N     1 
ATOM   5178 C CA    . VAL B 1 97  ? 29.611 12.840  -62.668 1.00 30.12 ? 95   VAL A CA    1 
ATOM   5179 C C     . VAL B 1 97  ? 30.208 11.619  -63.393 1.00 26.41 ? 95   VAL A C     1 
ATOM   5180 O O     . VAL B 1 97  ? 31.252 11.779  -64.039 1.00 26.90 ? 95   VAL A O     1 
ATOM   5181 C CB    . VAL B 1 97  ? 30.024 12.924  -61.184 1.00 31.84 ? 95   VAL A CB    1 
ATOM   5182 C CG1   . VAL B 1 97  ? 29.801 11.622  -60.442 1.00 31.84 ? 95   VAL A CG1   1 
ATOM   5183 C CG2   . VAL B 1 97  ? 31.469 13.365  -61.039 1.00 35.91 ? 95   VAL A CG2   1 
ATOM   5184 N N     . GLY B 1 98  ? 29.574 10.449  -63.314 1.00 25.22 ? 96   GLY A N     1 
ATOM   5185 C CA    . GLY B 1 98  ? 29.984 9.246   -64.058 1.00 26.20 ? 96   GLY A CA    1 
ATOM   5186 C C     . GLY B 1 98  ? 29.158 9.043   -65.324 1.00 27.58 ? 96   GLY A C     1 
ATOM   5187 O O     . GLY B 1 98  ? 29.181 7.938   -65.858 1.00 27.86 ? 96   GLY A O     1 
ATOM   5188 N N     . GLY B 1 99  ? 28.437 10.070  -65.769 1.00 26.15 ? 97   GLY A N     1 
ATOM   5189 C CA    . GLY B 1 99  ? 27.513 10.013  -66.925 1.00 27.45 ? 97   GLY A CA    1 
ATOM   5190 C C     . GLY B 1 99  ? 28.230 10.047  -68.271 1.00 27.09 ? 97   GLY A C     1 
ATOM   5191 O O     . GLY B 1 99  ? 29.381 10.423  -68.341 1.00 24.79 ? 97   GLY A O     1 
ATOM   5192 N N     . ASP B 1 100 ? 27.556 9.608   -69.323 1.00 27.95 ? 98   ASP A N     1 
ATOM   5193 C CA    . ASP B 1 100 ? 28.071 9.655   -70.714 1.00 27.64 ? 98   ASP A CA    1 
ATOM   5194 C C     . ASP B 1 100 ? 28.188 11.106  -71.185 1.00 27.55 ? 98   ASP A C     1 
ATOM   5195 O O     . ASP B 1 100 ? 27.183 11.813  -71.284 1.00 27.71 ? 98   ASP A O     1 
ATOM   5196 C CB    . ASP B 1 100 ? 27.118 8.868   -71.596 1.00 26.27 ? 98   ASP A CB    1 
ATOM   5197 C CG    . ASP B 1 100 ? 27.601 8.628   -73.002 1.00 28.33 ? 98   ASP A CG    1 
ATOM   5198 O OD1   . ASP B 1 100 ? 28.588 9.263   -73.404 1.00 28.00 ? 98   ASP A OD1   1 
ATOM   5199 O OD2   . ASP B 1 100 ? 26.980 7.786   -73.661 1.00 30.49 ? 98   ASP A OD2   1 
ATOM   5200 N N     . PRO B 1 101 ? 29.400 11.603  -71.530 1.00 27.76 ? 99   PRO A N     1 
ATOM   5201 C CA    . PRO B 1 101 ? 29.543 12.948  -72.101 1.00 28.02 ? 99   PRO A CA    1 
ATOM   5202 C C     . PRO B 1 101 ? 28.766 13.158  -73.411 1.00 29.70 ? 99   PRO A C     1 
ATOM   5203 O O     . PRO B 1 101 ? 28.445 14.286  -73.732 1.00 29.17 ? 99   PRO A O     1 
ATOM   5204 C CB    . PRO B 1 101 ? 31.050 13.088  -72.372 1.00 30.63 ? 99   PRO A CB    1 
ATOM   5205 C CG    . PRO B 1 101 ? 31.695 12.059  -71.484 1.00 32.53 ? 99   PRO A CG    1 
ATOM   5206 C CD    . PRO B 1 101 ? 30.694 10.922  -71.362 1.00 30.48 ? 99   PRO A CD    1 
ATOM   5207 N N     . ALA B 1 102 ? 28.428 12.087  -74.131 1.00 27.85 ? 100  ALA A N     1 
ATOM   5208 C CA    . ALA B 1 102 ? 27.640 12.212  -75.379 1.00 31.77 ? 100  ALA A CA    1 
ATOM   5209 C C     . ALA B 1 102 ? 26.272 12.836  -75.090 1.00 31.57 ? 100  ALA A C     1 
ATOM   5210 O O     . ALA B 1 102 ? 25.683 13.355  -76.043 1.00 33.91 ? 100  ALA A O     1 
ATOM   5211 C CB    . ALA B 1 102 ? 27.503 10.889  -76.076 1.00 31.21 ? 100  ALA A CB    1 
ATOM   5212 N N     . TYR B 1 103 ? 25.782 12.791  -73.843 1.00 31.58 ? 101  TYR A N     1 
ATOM   5213 C CA    . TYR B 1 103 ? 24.460 13.353  -73.449 1.00 33.81 ? 101  TYR A CA    1 
ATOM   5214 C C     . TYR B 1 103 ? 24.618 14.338  -72.295 1.00 34.89 ? 101  TYR A C     1 
ATOM   5215 O O     . TYR B 1 103 ? 23.636 14.560  -71.585 1.00 36.53 ? 101  TYR A O     1 
ATOM   5216 C CB    . TYR B 1 103 ? 23.472 12.242  -73.076 1.00 32.49 ? 101  TYR A CB    1 
ATOM   5217 C CG    . TYR B 1 103 ? 23.273 11.200  -74.147 1.00 28.27 ? 101  TYR A CG    1 
ATOM   5218 C CD1   . TYR B 1 103 ? 24.097 10.093  -74.217 1.00 30.88 ? 101  TYR A CD1   1 
ATOM   5219 C CD2   . TYR B 1 103 ? 22.274 11.314  -75.094 1.00 30.18 ? 101  TYR A CD2   1 
ATOM   5220 C CE1   . TYR B 1 103 ? 23.944 9.122   -75.195 1.00 28.99 ? 101  TYR A CE1   1 
ATOM   5221 C CE2   . TYR B 1 103 ? 22.096 10.348  -76.071 1.00 30.04 ? 101  TYR A CE2   1 
ATOM   5222 C CZ    . TYR B 1 103 ? 22.931 9.246   -76.124 1.00 28.78 ? 101  TYR A CZ    1 
ATOM   5223 O OH    . TYR B 1 103 ? 22.788 8.291   -77.089 1.00 31.93 ? 101  TYR A OH    1 
ATOM   5224 N N     . GLY B 1 104 ? 25.814 14.895  -72.104 1.00 33.89 ? 102  GLY A N     1 
ATOM   5225 C CA    . GLY B 1 104 ? 26.029 15.977  -71.126 1.00 32.19 ? 102  GLY A CA    1 
ATOM   5226 C C     . GLY B 1 104 ? 26.592 15.491  -69.800 1.00 30.14 ? 102  GLY A C     1 
ATOM   5227 O O     . GLY B 1 104 ? 26.786 16.329  -68.923 1.00 32.23 ? 102  GLY A O     1 
ATOM   5228 N N     . GLY B 1 105 ? 26.889 14.203  -69.641 1.00 29.89 ? 103  GLY A N     1 
ATOM   5229 C CA    . GLY B 1 105 ? 27.542 13.694  -68.419 1.00 32.20 ? 103  GLY A CA    1 
ATOM   5230 C C     . GLY B 1 105 ? 29.010 14.066  -68.379 1.00 30.41 ? 103  GLY A C     1 
ATOM   5231 O O     . GLY B 1 105 ? 29.535 14.436  -69.409 1.00 30.82 ? 103  GLY A O     1 
ATOM   5232 N N     . MET B 1 106 ? 29.649 13.961  -67.222 1.00 33.08 ? 104  MET A N     1 
ATOM   5233 C CA    . MET B 1 106 ? 31.074 14.338  -67.015 1.00 34.64 ? 104  MET A CA    1 
ATOM   5234 C C     . MET B 1 106 ? 32.013 13.198  -67.455 1.00 32.55 ? 104  MET A C     1 
ATOM   5235 O O     . MET B 1 106 ? 33.162 13.466  -67.758 1.00 32.21 ? 104  MET A O     1 
ATOM   5236 C CB    . MET B 1 106 ? 31.299 14.678  -65.538 1.00 40.73 ? 104  MET A CB    1 
ATOM   5237 C CG    . MET B 1 106 ? 32.152 15.921  -65.323 1.00 50.93 ? 104  MET A CG    1 
ATOM   5238 S SD    . MET B 1 106 ? 32.373 16.316  -63.549 1.00 56.32 ? 104  MET A SD    1 
ATOM   5239 C CE    . MET B 1 106 ? 30.673 16.618  -63.070 1.00 47.98 ? 104  MET A CE    1 
ATOM   5240 N N     . GLY B 1 107 ? 31.566 11.945  -67.484 1.00 30.36 ? 105  GLY A N     1 
ATOM   5241 C CA    . GLY B 1 107 ? 32.379 10.841  -68.027 1.00 27.38 ? 105  GLY A CA    1 
ATOM   5242 C C     . GLY B 1 107 ? 33.487 10.413  -67.075 1.00 27.54 ? 105  GLY A C     1 
ATOM   5243 O O     . GLY B 1 107 ? 34.445 9.762   -67.538 1.00 27.27 ? 105  GLY A O     1 
ATOM   5244 N N     . MET B 1 108 ? 33.369 10.689  -65.773 1.00 26.06 ? 106  MET A N     1 
ATOM   5245 C CA    . MET B 1 108 ? 34.373 10.210  -64.802 1.00 26.04 ? 106  MET A CA    1 
ATOM   5246 C C     . MET B 1 108 ? 34.333 8.688   -64.788 1.00 24.58 ? 106  MET A C     1 
ATOM   5247 O O     . MET B 1 108 ? 33.273 8.087   -64.917 1.00 24.60 ? 106  MET A O     1 
ATOM   5248 C CB    . MET B 1 108 ? 34.153 10.777  -63.402 1.00 28.15 ? 106  MET A CB    1 
ATOM   5249 C CG    . MET B 1 108 ? 34.545 12.243  -63.276 1.00 28.83 ? 106  MET A CG    1 
ATOM   5250 S SD    . MET B 1 108 ? 36.264 12.547  -63.738 1.00 34.52 ? 106  MET A SD    1 
ATOM   5251 C CE    . MET B 1 108 ? 36.022 13.562  -65.187 1.00 31.72 ? 106  MET A CE    1 
ATOM   5252 N N     . PRO B 1 109 ? 35.490 8.019   -64.659 1.00 24.35 ? 107  PRO A N     1 
ATOM   5253 C CA    . PRO B 1 109 ? 35.509 6.568   -64.516 1.00 24.65 ? 107  PRO A CA    1 
ATOM   5254 C C     . PRO B 1 109 ? 34.893 6.172   -63.169 1.00 25.28 ? 107  PRO A C     1 
ATOM   5255 O O     . PRO B 1 109 ? 34.779 6.999   -62.278 1.00 22.32 ? 107  PRO A O     1 
ATOM   5256 C CB    . PRO B 1 109 ? 36.992 6.228   -64.601 1.00 24.99 ? 107  PRO A CB    1 
ATOM   5257 C CG    . PRO B 1 109 ? 37.661 7.471   -64.065 1.00 25.77 ? 107  PRO A CG    1 
ATOM   5258 C CD    . PRO B 1 109 ? 36.832 8.605   -64.620 1.00 26.45 ? 107  PRO A CD    1 
ATOM   5259 N N     . LYS B 1 110 ? 34.543 4.896   -63.039 1.00 26.10 ? 108  LYS A N     1 
ATOM   5260 C CA    . LYS B 1 110 ? 33.856 4.367   -61.850 1.00 25.51 ? 108  LYS A CA    1 
ATOM   5261 C C     . LYS B 1 110 ? 34.753 4.501   -60.619 1.00 25.17 ? 108  LYS A C     1 
ATOM   5262 O O     . LYS B 1 110 ? 34.200 4.658   -59.527 1.00 22.20 ? 108  LYS A O     1 
ATOM   5263 C CB    . LYS B 1 110 ? 33.445 2.906   -62.035 1.00 26.03 ? 108  LYS A CB    1 
ATOM   5264 C CG    . LYS B 1 110 ? 32.509 2.376   -60.961 1.00 26.41 ? 108  LYS A CG    1 
ATOM   5265 C CD    . LYS B 1 110 ? 31.261 3.216   -60.764 1.00 29.16 ? 108  LYS A CD    1 
ATOM   5266 C CE    . LYS B 1 110 ? 30.377 2.654   -59.677 1.00 33.35 ? 108  LYS A CE    1 
ATOM   5267 N NZ    . LYS B 1 110 ? 29.108 3.414   -59.556 1.00 36.84 ? 108  LYS A NZ    1 
ATOM   5268 N N     . VAL B 1 111 ? 36.082 4.446   -60.762 1.00 24.36 ? 109  VAL A N     1 
ATOM   5269 C CA    . VAL B 1 111 ? 36.976 4.557   -59.579 1.00 23.23 ? 109  VAL A CA    1 
ATOM   5270 C C     . VAL B 1 111 ? 36.776 5.950   -58.963 1.00 23.06 ? 109  VAL A C     1 
ATOM   5271 O O     . VAL B 1 111 ? 36.869 6.046   -57.734 1.00 22.91 ? 109  VAL A O     1 
ATOM   5272 C CB    . VAL B 1 111 ? 38.456 4.259   -59.915 1.00 24.69 ? 109  VAL A CB    1 
ATOM   5273 C CG1   . VAL B 1 111 ? 38.669 2.791   -60.255 1.00 23.96 ? 109  VAL A CG1   1 
ATOM   5274 C CG2   . VAL B 1 111 ? 39.011 5.156   -61.007 1.00 23.37 ? 109  VAL A CG2   1 
ATOM   5275 N N     . ILE B 1 112 ? 36.427 6.971   -59.756 1.00 20.23 ? 110  ILE A N     1 
ATOM   5276 C CA    . ILE B 1 112 ? 36.165 8.338   -59.214 1.00 23.26 ? 110  ILE A CA    1 
ATOM   5277 C C     . ILE B 1 112 ? 34.701 8.454   -58.738 1.00 23.40 ? 110  ILE A C     1 
ATOM   5278 O O     . ILE B 1 112 ? 34.466 8.875   -57.579 1.00 21.23 ? 110  ILE A O     1 
ATOM   5279 C CB    . ILE B 1 112 ? 36.550 9.420   -60.233 1.00 22.94 ? 110  ILE A CB    1 
ATOM   5280 C CG1   . ILE B 1 112 ? 38.056 9.412   -60.543 1.00 24.38 ? 110  ILE A CG1   1 
ATOM   5281 C CG2   . ILE B 1 112 ? 36.088 10.789  -59.774 1.00 23.36 ? 110  ILE A CG2   1 
ATOM   5282 C CD1   . ILE B 1 112 ? 38.964 9.532   -59.326 1.00 24.44 ? 110  ILE A CD1   1 
ATOM   5283 N N     . SER B 1 113 ? 33.741 8.063   -59.559 1.00 24.09 ? 111  SER A N     1 
ATOM   5284 C CA    . SER B 1 113 ? 32.305 8.236   -59.226 1.00 24.76 ? 111  SER A CA    1 
ATOM   5285 C C     . SER B 1 113 ? 31.963 7.394   -57.977 1.00 23.27 ? 111  SER A C     1 
ATOM   5286 O O     . SER B 1 113 ? 31.156 7.839   -57.186 1.00 21.75 ? 111  SER A O     1 
ATOM   5287 C CB    . SER B 1 113 ? 31.427 7.941   -60.410 1.00 25.20 ? 111  SER A CB    1 
ATOM   5288 O OG    . SER B 1 113 ? 31.483 6.569   -60.727 1.00 27.89 ? 111  SER A OG    1 
ATOM   5289 N N     . ALA B 1 114 ? 32.599 6.237   -57.784 1.00 22.63 ? 112  ALA A N     1 
ATOM   5290 C CA    . ALA B 1 114 ? 32.434 5.380   -56.600 1.00 23.03 ? 112  ALA A CA    1 
ATOM   5291 C C     . ALA B 1 114 ? 32.946 6.093   -55.340 1.00 24.23 ? 112  ALA A C     1 
ATOM   5292 O O     . ALA B 1 114 ? 32.377 5.877   -54.302 1.00 24.12 ? 112  ALA A O     1 
ATOM   5293 C CB    . ALA B 1 114 ? 33.130 4.053   -56.814 1.00 24.87 ? 112  ALA A CB    1 
ATOM   5294 N N     . GLN B 1 115 ? 33.993 6.912   -55.413 1.00 23.50 ? 113  GLN A N     1 
ATOM   5295 C CA    . GLN B 1 115 ? 34.492 7.658   -54.236 1.00 24.68 ? 113  GLN A CA    1 
ATOM   5296 C C     . GLN B 1 115 ? 33.461 8.746   -53.937 1.00 25.43 ? 113  GLN A C     1 
ATOM   5297 O O     . GLN B 1 115 ? 33.092 8.922   -52.758 1.00 23.88 ? 113  GLN A O     1 
ATOM   5298 C CB    . GLN B 1 115 ? 35.908 8.195   -54.471 1.00 24.93 ? 113  GLN A CB    1 
ATOM   5299 C CG    . GLN B 1 115 ? 36.949 7.088   -54.472 1.00 26.92 ? 113  GLN A CG    1 
ATOM   5300 C CD    . GLN B 1 115 ? 38.377 7.587   -54.421 1.00 27.90 ? 113  GLN A CD    1 
ATOM   5301 O OE1   . GLN B 1 115 ? 39.284 6.933   -53.889 1.00 30.01 ? 113  GLN A OE1   1 
ATOM   5302 N NE2   . GLN B 1 115 ? 38.581 8.759   -54.976 1.00 24.28 ? 113  GLN A NE2   1 
ATOM   5303 N N     . VAL B 1 116 ? 32.961 9.420   -54.960 1.00 24.34 ? 114  VAL A N     1 
ATOM   5304 C CA    . VAL B 1 116 ? 31.922 10.462  -54.741 1.00 25.64 ? 114  VAL A CA    1 
ATOM   5305 C C     . VAL B 1 116 ? 30.713 9.795   -54.069 1.00 27.07 ? 114  VAL A C     1 
ATOM   5306 O O     . VAL B 1 116 ? 30.148 10.346  -53.112 1.00 25.69 ? 114  VAL A O     1 
ATOM   5307 C CB    . VAL B 1 116 ? 31.537 11.146  -56.054 1.00 25.54 ? 114  VAL A CB    1 
ATOM   5308 C CG1   . VAL B 1 116 ? 30.307 12.029  -55.870 1.00 25.81 ? 114  VAL A CG1   1 
ATOM   5309 C CG2   . VAL B 1 116 ? 32.711 11.927  -56.625 1.00 27.68 ? 114  VAL A CG2   1 
ATOM   5310 N N     . GLU B 1 117 ? 30.349 8.609   -54.539 1.00 26.59 ? 115  GLU A N     1 
ATOM   5311 C CA    . GLU B 1 117 ? 29.218 7.860   -53.971 1.00 27.87 ? 115  GLU A CA    1 
ATOM   5312 C C     . GLU B 1 117 ? 29.470 7.628   -52.479 1.00 25.68 ? 115  GLU A C     1 
ATOM   5313 O O     . GLU B 1 117 ? 28.535 7.786   -51.692 1.00 21.16 ? 115  GLU A O     1 
ATOM   5314 C CB    . GLU B 1 117 ? 29.060 6.544   -54.724 1.00 32.62 ? 115  GLU A CB    1 
ATOM   5315 C CG    . GLU B 1 117 ? 27.735 5.929   -54.443 1.00 39.36 ? 115  GLU A CG    1 
ATOM   5316 C CD    . GLU B 1 117 ? 27.650 4.429   -54.594 1.00 49.77 ? 115  GLU A CD    1 
ATOM   5317 O OE1   . GLU B 1 117 ? 26.998 3.822   -53.676 1.00 46.16 ? 115  GLU A OE1   1 
ATOM   5318 O OE2   . GLU B 1 117 ? 28.187 3.884   -55.630 1.00 48.97 ? 115  GLU A OE2   1 
ATOM   5319 N N     . GLU B 1 118 ? 30.692 7.252   -52.102 1.00 22.92 ? 116  GLU A N     1 
ATOM   5320 C CA    . GLU B 1 118 ? 31.006 6.984   -50.680 1.00 22.75 ? 116  GLU A CA    1 
ATOM   5321 C C     . GLU B 1 118 ? 30.801 8.285   -49.915 1.00 22.47 ? 116  GLU A C     1 
ATOM   5322 O O     . GLU B 1 118 ? 30.193 8.237   -48.855 1.00 22.56 ? 116  GLU A O     1 
ATOM   5323 C CB    . GLU B 1 118 ? 32.403 6.387   -50.494 1.00 24.05 ? 116  GLU A CB    1 
ATOM   5324 C CG    . GLU B 1 118 ? 32.653 5.869   -49.091 1.00 24.18 ? 116  GLU A CG    1 
ATOM   5325 C CD    . GLU B 1 118 ? 34.093 5.846   -48.610 1.00 26.94 ? 116  GLU A CD    1 
ATOM   5326 O OE1   . GLU B 1 118 ? 34.888 5.160   -49.251 1.00 26.54 ? 116  GLU A OE1   1 
ATOM   5327 O OE2   . GLU B 1 118 ? 34.395 6.455   -47.536 1.00 27.91 ? 116  GLU A OE2   1 
ATOM   5328 N N     . LEU B 1 119 ? 31.265 9.414   -50.443 1.00 23.55 ? 117  LEU A N     1 
ATOM   5329 C CA    . LEU B 1 119 ? 31.195 10.695  -49.698 1.00 23.35 ? 117  LEU A CA    1 
ATOM   5330 C C     . LEU B 1 119 ? 29.727 11.034  -49.425 1.00 23.95 ? 117  LEU A C     1 
ATOM   5331 O O     . LEU B 1 119 ? 29.376 11.320  -48.272 1.00 23.39 ? 117  LEU A O     1 
ATOM   5332 C CB    . LEU B 1 119 ? 31.851 11.810  -50.511 1.00 25.08 ? 117  LEU A CB    1 
ATOM   5333 C CG    . LEU B 1 119 ? 33.348 11.648  -50.756 1.00 25.91 ? 117  LEU A CG    1 
ATOM   5334 C CD1   . LEU B 1 119 ? 33.914 12.909  -51.370 1.00 27.09 ? 117  LEU A CD1   1 
ATOM   5335 C CD2   . LEU B 1 119 ? 34.089 11.296  -49.492 1.00 27.21 ? 117  LEU A CD2   1 
ATOM   5336 N N     . VAL B 1 120 ? 28.888 10.972  -50.451 1.00 23.32 ? 118  VAL A N     1 
ATOM   5337 C CA    . VAL B 1 120 ? 27.485 11.435  -50.324 1.00 24.30 ? 118  VAL A CA    1 
ATOM   5338 C C     . VAL B 1 120 ? 26.742 10.494  -49.387 1.00 23.35 ? 118  VAL A C     1 
ATOM   5339 O O     . VAL B 1 120 ? 25.956 11.004  -48.568 1.00 24.95 ? 118  VAL A O     1 
ATOM   5340 C CB    . VAL B 1 120 ? 26.762 11.541  -51.673 1.00 26.09 ? 118  VAL A CB    1 
ATOM   5341 C CG1   . VAL B 1 120 ? 25.422 12.224  -51.485 1.00 26.55 ? 118  VAL A CG1   1 
ATOM   5342 C CG2   . VAL B 1 120 ? 27.617 12.309  -52.651 1.00 33.20 ? 118  VAL A CG2   1 
ATOM   5343 N N     . ASN B 1 121 ? 26.996 9.191   -49.506 1.00 21.98 ? 119  ASN A N     1 
ATOM   5344 C CA    . ASN B 1 121 ? 26.258 8.157   -48.742 1.00 23.07 ? 119  ASN A CA    1 
ATOM   5345 C C     . ASN B 1 121 ? 26.691 8.183   -47.270 1.00 25.54 ? 119  ASN A C     1 
ATOM   5346 O O     . ASN B 1 121 ? 25.839 7.914   -46.415 1.00 24.25 ? 119  ASN A O     1 
ATOM   5347 C CB    . ASN B 1 121 ? 26.414 6.784   -49.383 1.00 21.79 ? 119  ASN A CB    1 
ATOM   5348 C CG    . ASN B 1 121 ? 25.565 6.632   -50.625 1.00 24.69 ? 119  ASN A CG    1 
ATOM   5349 O OD1   . ASN B 1 121 ? 24.635 7.382   -50.865 1.00 27.68 ? 119  ASN A OD1   1 
ATOM   5350 N ND2   . ASN B 1 121 ? 25.856 5.616   -51.405 1.00 27.87 ? 119  ASN A ND2   1 
ATOM   5351 N N     . SER B 1 122 ? 27.966 8.473   -46.984 1.00 24.09 ? 120  SER A N     1 
ATOM   5352 C CA    . SER B 1 122 ? 28.476 8.708   -45.609 1.00 23.01 ? 120  SER A CA    1 
ATOM   5353 C C     . SER B 1 122 ? 27.773 9.902   -44.982 1.00 22.93 ? 120  SER A C     1 
ATOM   5354 O O     . SER B 1 122 ? 27.363 9.812   -43.804 1.00 21.90 ? 120  SER A O     1 
ATOM   5355 C CB    . SER B 1 122 ? 29.976 8.927   -45.583 1.00 24.16 ? 120  SER A CB    1 
ATOM   5356 O OG    . SER B 1 122 ? 30.646 7.711   -45.398 1.00 25.17 ? 120  SER A OG    1 
ATOM   5357 N N     . ALA B 1 123 ? 27.710 11.004  -45.723 1.00 24.12 ? 121  ALA A N     1 
ATOM   5358 C CA    . ALA B 1 123 ? 27.147 12.280  -45.247 1.00 23.08 ? 121  ALA A CA    1 
ATOM   5359 C C     . ALA B 1 123 ? 25.668 12.087  -44.888 1.00 24.84 ? 121  ALA A C     1 
ATOM   5360 O O     . ALA B 1 123 ? 25.238 12.612  -43.849 1.00 25.09 ? 121  ALA A O     1 
ATOM   5361 C CB    . ALA B 1 123 ? 27.341 13.322  -46.295 1.00 24.28 ? 121  ALA A CB    1 
ATOM   5362 N N     . ASN B 1 124 ? 24.926 11.333  -45.702 1.00 22.93 ? 122  ASN A N     1 
ATOM   5363 C CA    . ASN B 1 124 ? 23.443 11.248  -45.602 1.00 21.91 ? 122  ASN A CA    1 
ATOM   5364 C C     . ASN B 1 124 ? 22.949 10.187  -46.574 1.00 20.89 ? 122  ASN A C     1 
ATOM   5365 O O     . ASN B 1 124 ? 22.781 10.487  -47.780 1.00 21.58 ? 122  ASN A O     1 
ATOM   5366 C CB    . ASN B 1 124 ? 22.856 12.627  -45.871 1.00 22.58 ? 122  ASN A CB    1 
ATOM   5367 C CG    . ASN B 1 124 ? 21.373 12.797  -45.643 1.00 23.52 ? 122  ASN A CG    1 
ATOM   5368 O OD1   . ASN B 1 124 ? 20.930 13.931  -45.420 1.00 28.72 ? 122  ASN A OD1   1 
ATOM   5369 N ND2   . ASN B 1 124 ? 20.596 11.736  -45.747 1.00 20.73 ? 122  ASN A ND2   1 
ATOM   5370 N N     . LEU B 1 125 ? 22.808 8.958   -46.098 1.00 21.16 ? 123  LEU A N     1 
ATOM   5371 C CA    . LEU B 1 125 ? 22.454 7.838   -46.990 1.00 22.90 ? 123  LEU A CA    1 
ATOM   5372 C C     . LEU B 1 125 ? 21.117 8.143   -47.685 1.00 23.21 ? 123  LEU A C     1 
ATOM   5373 O O     . LEU B 1 125 ? 21.047 7.943   -48.908 1.00 23.58 ? 123  LEU A O     1 
ATOM   5374 C CB    . LEU B 1 125 ? 22.416 6.527   -46.211 1.00 22.07 ? 123  LEU A CB    1 
ATOM   5375 C CG    . LEU B 1 125 ? 22.066 5.326   -47.074 1.00 22.96 ? 123  LEU A CG    1 
ATOM   5376 C CD1   . LEU B 1 125 ? 23.089 5.179   -48.213 1.00 24.57 ? 123  LEU A CD1   1 
ATOM   5377 C CD2   . LEU B 1 125 ? 22.003 4.061   -46.243 1.00 23.87 ? 123  LEU A CD2   1 
ATOM   5378 N N     . SER B 1 126 ? 20.107 8.630   -46.960 1.00 23.21 ? 124  SER A N     1 
ATOM   5379 C CA    . SER B 1 126 ? 18.780 8.944   -47.547 1.00 24.79 ? 124  SER A CA    1 
ATOM   5380 C C     . SER B 1 126 ? 18.960 9.874   -48.742 1.00 23.28 ? 124  SER A C     1 
ATOM   5381 O O     . SER B 1 126 ? 18.365 9.611   -49.815 1.00 25.24 ? 124  SER A O     1 
ATOM   5382 C CB    . SER B 1 126 ? 17.787 9.527   -46.555 1.00 24.20 ? 124  SER A CB    1 
ATOM   5383 O OG    . SER B 1 126 ? 17.332 8.558   -45.638 1.00 24.91 ? 124  SER A OG    1 
ATOM   5384 N N     . PHE B 1 127 ? 19.775 10.916  -48.590 1.00 24.54 ? 125  PHE A N     1 
ATOM   5385 C CA    . PHE B 1 127 ? 20.017 11.878  -49.690 1.00 23.53 ? 125  PHE A CA    1 
ATOM   5386 C C     . PHE B 1 127 ? 20.687 11.144  -50.850 1.00 23.31 ? 125  PHE A C     1 
ATOM   5387 O O     . PHE B 1 127 ? 20.277 11.318  -52.019 1.00 21.54 ? 125  PHE A O     1 
ATOM   5388 C CB    . PHE B 1 127 ? 20.859 13.056  -49.220 1.00 23.21 ? 125  PHE A CB    1 
ATOM   5389 C CG    . PHE B 1 127 ? 21.052 14.079  -50.300 1.00 22.45 ? 125  PHE A CG    1 
ATOM   5390 C CD1   . PHE B 1 127 ? 22.082 13.950  -51.220 1.00 26.01 ? 125  PHE A CD1   1 
ATOM   5391 C CD2   . PHE B 1 127 ? 20.206 15.167  -50.396 1.00 23.47 ? 125  PHE A CD2   1 
ATOM   5392 C CE1   . PHE B 1 127 ? 22.239 14.880  -52.240 1.00 26.71 ? 125  PHE A CE1   1 
ATOM   5393 C CE2   . PHE B 1 127 ? 20.353 16.089  -51.416 1.00 24.26 ? 125  PHE A CE2   1 
ATOM   5394 C CZ    . PHE B 1 127 ? 21.374 15.948  -52.328 1.00 27.64 ? 125  PHE A CZ    1 
ATOM   5395 N N     . GLY B 1 128 ? 21.681 10.316  -50.531 1.00 23.86 ? 126  GLY A N     1 
ATOM   5396 C CA    . GLY B 1 128 ? 22.571 9.700   -51.534 1.00 25.70 ? 126  GLY A CA    1 
ATOM   5397 C C     . GLY B 1 128 ? 21.823 8.761   -52.451 1.00 24.52 ? 126  GLY A C     1 
ATOM   5398 O O     . GLY B 1 128 ? 22.127 8.700   -53.666 1.00 23.34 ? 126  GLY A O     1 
ATOM   5399 N N     . LEU B 1 129 ? 20.823 8.066   -51.921 1.00 26.37 ? 127  LEU A N     1 
ATOM   5400 C CA    . LEU B 1 129 ? 20.103 7.050   -52.730 1.00 24.66 ? 127  LEU A CA    1 
ATOM   5401 C C     . LEU B 1 129 ? 19.350 7.741   -53.874 1.00 24.38 ? 127  LEU A C     1 
ATOM   5402 O O     . LEU B 1 129 ? 19.236 7.117   -54.933 1.00 22.99 ? 127  LEU A O     1 
ATOM   5403 C CB    . LEU B 1 129 ? 19.194 6.251   -51.806 1.00 25.76 ? 127  LEU A CB    1 
ATOM   5404 C CG    . LEU B 1 129 ? 19.939 5.339   -50.827 1.00 26.91 ? 127  LEU A CG    1 
ATOM   5405 C CD1   . LEU B 1 129 ? 18.950 4.498   -50.010 1.00 27.04 ? 127  LEU A CD1   1 
ATOM   5406 C CD2   . LEU B 1 129 ? 20.936 4.444   -51.550 1.00 28.47 ? 127  LEU A CD2   1 
ATOM   5407 N N     . TYR B 1 130 ? 18.915 9.000   -53.706 1.00 22.32 ? 128  TYR A N     1 
ATOM   5408 C CA    . TYR B 1 130 ? 18.116 9.733   -54.714 1.00 22.05 ? 128  TYR A CA    1 
ATOM   5409 C C     . TYR B 1 130 ? 18.885 9.868   -56.040 1.00 24.37 ? 128  TYR A C     1 
ATOM   5410 O O     . TYR B 1 130 ? 18.411 9.376   -57.062 1.00 24.88 ? 128  TYR A O     1 
ATOM   5411 C CB    . TYR B 1 130 ? 17.644 11.072  -54.158 1.00 21.89 ? 128  TYR A CB    1 
ATOM   5412 C CG    . TYR B 1 130 ? 16.498 11.000  -53.186 1.00 21.56 ? 128  TYR A CG    1 
ATOM   5413 C CD1   . TYR B 1 130 ? 15.242 10.577  -53.578 1.00 22.29 ? 128  TYR A CD1   1 
ATOM   5414 C CD2   . TYR B 1 130 ? 16.656 11.411  -51.878 1.00 23.05 ? 128  TYR A CD2   1 
ATOM   5415 C CE1   . TYR B 1 130 ? 14.187 10.540  -52.691 1.00 22.61 ? 128  TYR A CE1   1 
ATOM   5416 C CE2   . TYR B 1 130 ? 15.601 11.387  -50.974 1.00 22.98 ? 128  TYR A CE2   1 
ATOM   5417 C CZ    . TYR B 1 130 ? 14.359 10.950  -51.383 1.00 23.65 ? 128  TYR A CZ    1 
ATOM   5418 O OH    . TYR B 1 130 ? 13.303 10.940  -50.512 1.00 23.55 ? 128  TYR A OH    1 
ATOM   5419 N N     . PRO B 1 131 ? 20.056 10.542  -56.118 1.00 23.40 ? 129  PRO A N     1 
ATOM   5420 C CA    . PRO B 1 131 ? 20.827 10.606  -57.363 1.00 24.70 ? 129  PRO A CA    1 
ATOM   5421 C C     . PRO B 1 131 ? 21.370 9.251   -57.844 1.00 25.54 ? 129  PRO A C     1 
ATOM   5422 O O     . PRO B 1 131 ? 21.489 9.073   -59.038 1.00 24.70 ? 129  PRO A O     1 
ATOM   5423 C CB    . PRO B 1 131 ? 22.006 11.526  -57.035 1.00 24.89 ? 129  PRO A CB    1 
ATOM   5424 C CG    . PRO B 1 131 ? 22.127 11.437  -55.530 1.00 25.25 ? 129  PRO A CG    1 
ATOM   5425 C CD    . PRO B 1 131 ? 20.690 11.340  -55.058 1.00 24.90 ? 129  PRO A CD    1 
ATOM   5426 N N     . GLY B 1 132 ? 21.651 8.313   -56.937 1.00 27.36 ? 130  GLY A N     1 
ATOM   5427 C CA    . GLY B 1 132 ? 22.028 6.929   -57.309 1.00 24.53 ? 130  GLY A CA    1 
ATOM   5428 C C     . GLY B 1 132 ? 20.971 6.274   -58.202 1.00 24.62 ? 130  GLY A C     1 
ATOM   5429 O O     . GLY B 1 132 ? 21.356 5.576   -59.160 1.00 24.19 ? 130  GLY A O     1 
ATOM   5430 N N     . LEU B 1 133 ? 19.677 6.487   -57.943 1.00 24.21 ? 131  LEU A N     1 
ATOM   5431 C CA    . LEU B 1 133 ? 18.584 5.933   -58.775 1.00 26.54 ? 131  LEU A CA    1 
ATOM   5432 C C     . LEU B 1 133 ? 18.732 6.448   -60.201 1.00 26.95 ? 131  LEU A C     1 
ATOM   5433 O O     . LEU B 1 133 ? 18.588 5.689   -61.151 1.00 24.71 ? 131  LEU A O     1 
ATOM   5434 C CB    . LEU B 1 133 ? 17.232 6.414   -58.256 1.00 29.69 ? 131  LEU A CB    1 
ATOM   5435 C CG    . LEU B 1 133 ? 16.758 5.836   -56.933 1.00 33.17 ? 131  LEU A CG    1 
ATOM   5436 C CD1   . LEU B 1 133 ? 15.402 6.431   -56.580 1.00 35.61 ? 131  LEU A CD1   1 
ATOM   5437 C CD2   . LEU B 1 133 ? 16.681 4.321   -57.006 1.00 36.48 ? 131  LEU A CD2   1 
ATOM   5438 N N     . THR B 1 134 ? 18.924 7.754   -60.325 1.00 25.58 ? 132  THR A N     1 
ATOM   5439 C CA    . THR B 1 134 ? 18.958 8.463   -61.620 1.00 24.79 ? 132  THR A CA    1 
ATOM   5440 C C     . THR B 1 134 ? 20.150 7.945   -62.399 1.00 23.40 ? 132  THR A C     1 
ATOM   5441 O O     . THR B 1 134 ? 19.986 7.610   -63.563 1.00 24.01 ? 132  THR A O     1 
ATOM   5442 C CB    . THR B 1 134 ? 19.010 9.977   -61.383 1.00 23.76 ? 132  THR A CB    1 
ATOM   5443 O OG1   . THR B 1 134 ? 17.884 10.236  -60.545 1.00 23.10 ? 132  THR A OG1   1 
ATOM   5444 C CG2   . THR B 1 134 ? 18.983 10.750  -62.679 1.00 24.79 ? 132  THR A CG2   1 
ATOM   5445 N N     . ALA B 1 135 ? 21.315 7.885   -61.758 1.00 23.28 ? 133  ALA A N     1 
ATOM   5446 C CA    . ALA B 1 135 ? 22.546 7.378   -62.392 1.00 22.26 ? 133  ALA A CA    1 
ATOM   5447 C C     . ALA B 1 135 ? 22.314 5.928   -62.837 1.00 22.71 ? 133  ALA A C     1 
ATOM   5448 O O     . ALA B 1 135 ? 22.765 5.571   -63.931 1.00 22.89 ? 133  ALA A O     1 
ATOM   5449 C CB    . ALA B 1 135 ? 23.732 7.489   -61.466 1.00 22.24 ? 133  ALA A CB    1 
ATOM   5450 N N     . GLY B 1 136 ? 21.678 5.112   -62.009 1.00 21.61 ? 134  GLY A N     1 
ATOM   5451 C CA    . GLY B 1 136 ? 21.363 3.715   -62.367 1.00 24.61 ? 134  GLY A CA    1 
ATOM   5452 C C     . GLY B 1 136 ? 20.487 3.621   -63.609 1.00 23.94 ? 134  GLY A C     1 
ATOM   5453 O O     . GLY B 1 136 ? 20.865 2.916   -64.583 1.00 25.78 ? 134  GLY A O     1 
ATOM   5454 N N     . ALA B 1 137 ? 19.362 4.341   -63.611 1.00 24.37 ? 135  ALA A N     1 
ATOM   5455 C CA    . ALA B 1 137 ? 18.374 4.346   -64.710 1.00 23.83 ? 135  ALA A CA    1 
ATOM   5456 C C     . ALA B 1 137 ? 19.093 4.769   -65.998 1.00 23.72 ? 135  ALA A C     1 
ATOM   5457 O O     . ALA B 1 137 ? 18.841 4.144   -67.041 1.00 21.98 ? 135  ALA A O     1 
ATOM   5458 C CB    . ALA B 1 137 ? 17.197 5.228   -64.358 1.00 22.63 ? 135  ALA A CB    1 
ATOM   5459 N N     . CYS B 1 138 ? 20.011 5.749   -65.922 1.00 24.72 ? 136  CYS A N     1 
ATOM   5460 C CA    . CYS B 1 138 ? 20.770 6.215   -67.113 1.00 24.12 ? 136  CYS A CA    1 
ATOM   5461 C C     . CYS B 1 138 ? 21.570 5.058   -67.713 1.00 23.98 ? 136  CYS A C     1 
ATOM   5462 O O     . CYS B 1 138 ? 21.620 4.946   -68.944 1.00 26.87 ? 136  CYS A O     1 
ATOM   5463 C CB    . CYS B 1 138 ? 21.676 7.390   -66.812 1.00 23.16 ? 136  CYS A CB    1 
ATOM   5464 S SG    . CYS B 1 138 ? 20.748 8.918   -66.547 1.00 26.09 ? 136  CYS A SG    1 
ATOM   5465 N N     . LEU B 1 139 ? 22.211 4.256   -66.882 1.00 26.04 ? 137  LEU A N     1 
ATOM   5466 C CA    . LEU B 1 139 ? 23.013 3.107   -67.362 1.00 26.05 ? 137  LEU A CA    1 
ATOM   5467 C C     . LEU B 1 139 ? 22.149 2.200   -68.234 1.00 24.82 ? 137  LEU A C     1 
ATOM   5468 O O     . LEU B 1 139 ? 22.602 1.832   -69.326 1.00 23.26 ? 137  LEU A O     1 
ATOM   5469 C CB    . LEU B 1 139 ? 23.539 2.313   -66.174 1.00 28.11 ? 137  LEU A CB    1 
ATOM   5470 C CG    . LEU B 1 139 ? 24.813 2.825   -65.530 1.00 30.88 ? 137  LEU A CG    1 
ATOM   5471 C CD1   . LEU B 1 139 ? 25.182 1.932   -64.355 1.00 30.46 ? 137  LEU A CD1   1 
ATOM   5472 C CD2   . LEU B 1 139 ? 25.968 2.918   -66.525 1.00 30.91 ? 137  LEU A CD2   1 
ATOM   5473 N N     . ALA B 1 140 ? 20.943 1.864   -67.765 1.00 23.12 ? 138  ALA A N     1 
ATOM   5474 C CA    . ALA B 1 140 ? 20.021 0.939   -68.454 1.00 22.43 ? 138  ALA A CA    1 
ATOM   5475 C C     . ALA B 1 140 ? 19.524 1.585   -69.752 1.00 23.64 ? 138  ALA A C     1 
ATOM   5476 O O     . ALA B 1 140 ? 19.511 0.911   -70.773 1.00 22.19 ? 138  ALA A O     1 
ATOM   5477 C CB    . ALA B 1 140 ? 18.874 0.574   -67.549 1.00 24.39 ? 138  ALA A CB    1 
ATOM   5478 N N     . LEU B 1 141 ? 19.172 2.870   -69.725 1.00 23.94 ? 139  LEU A N     1 
ATOM   5479 C CA    . LEU B 1 141 ? 18.666 3.560   -70.937 1.00 23.92 ? 139  LEU A CA    1 
ATOM   5480 C C     . LEU B 1 141 ? 19.791 3.694   -71.946 1.00 24.35 ? 139  LEU A C     1 
ATOM   5481 O O     . LEU B 1 141 ? 19.534 3.365   -73.109 1.00 25.02 ? 139  LEU A O     1 
ATOM   5482 C CB    . LEU B 1 141 ? 18.109 4.932   -70.583 1.00 24.37 ? 139  LEU A CB    1 
ATOM   5483 C CG    . LEU B 1 141 ? 16.867 4.920   -69.702 1.00 23.82 ? 139  LEU A CG    1 
ATOM   5484 C CD1   . LEU B 1 141 ? 16.432 6.344   -69.459 1.00 24.77 ? 139  LEU A CD1   1 
ATOM   5485 C CD2   . LEU B 1 141 ? 15.734 4.126   -70.338 1.00 25.56 ? 139  LEU A CD2   1 
ATOM   5486 N N     . ASN B 1 142 ? 20.993 4.105   -71.514 1.00 24.99 ? 140  ASN A N     1 
ATOM   5487 C CA    . ASN B 1 142 ? 22.169 4.194   -72.422 1.00 26.50 ? 140  ASN A CA    1 
ATOM   5488 C C     . ASN B 1 142 ? 22.423 2.826   -73.083 1.00 26.72 ? 140  ASN A C     1 
ATOM   5489 O O     . ASN B 1 142 ? 22.636 2.761   -74.289 1.00 27.16 ? 140  ASN A O     1 
ATOM   5490 C CB    . ASN B 1 142 ? 23.407 4.745   -71.700 1.00 28.19 ? 140  ASN A CB    1 
ATOM   5491 C CG    . ASN B 1 142 ? 24.358 5.458   -72.643 1.00 29.12 ? 140  ASN A CG    1 
ATOM   5492 O OD1   . ASN B 1 142 ? 24.677 4.943   -73.698 1.00 39.31 ? 140  ASN A OD1   1 
ATOM   5493 N ND2   . ASN B 1 142 ? 24.788 6.653   -72.298 1.00 29.29 ? 140  ASN A ND2   1 
ATOM   5494 N N     . ALA B 1 143 ? 22.423 1.741   -72.327 1.00 28.40 ? 141  ALA A N     1 
ATOM   5495 C CA    . ALA B 1 143 ? 22.776 0.407   -72.865 1.00 28.15 ? 141  ALA A CA    1 
ATOM   5496 C C     . ALA B 1 143 ? 21.684 -0.135  -73.807 1.00 27.90 ? 141  ALA A C     1 
ATOM   5497 O O     . ALA B 1 143 ? 22.041 -0.844  -74.749 1.00 26.16 ? 141  ALA A O     1 
ATOM   5498 C CB    . ALA B 1 143 ? 23.070 -0.538  -71.729 1.00 27.97 ? 141  ALA A CB    1 
ATOM   5499 N N     . HIS B 1 144 ? 20.392 0.157   -73.603 1.00 27.93 ? 142  HIS A N     1 
ATOM   5500 C CA    . HIS B 1 144 ? 19.309 -0.611  -74.283 1.00 28.24 ? 142  HIS A CA    1 
ATOM   5501 C C     . HIS B 1 144 ? 18.186 0.249   -74.884 1.00 26.00 ? 142  HIS A C     1 
ATOM   5502 O O     . HIS B 1 144 ? 17.431 -0.282  -75.678 1.00 26.61 ? 142  HIS A O     1 
ATOM   5503 C CB    . HIS B 1 144 ? 18.788 -1.668  -73.300 1.00 30.00 ? 142  HIS A CB    1 
ATOM   5504 C CG    . HIS B 1 144 ? 19.774 -2.761  -73.065 1.00 31.20 ? 142  HIS A CG    1 
ATOM   5505 N ND1   . HIS B 1 144 ? 19.925 -3.809  -73.953 1.00 32.42 ? 142  HIS A ND1   1 
ATOM   5506 C CD2   . HIS B 1 144 ? 20.668 -2.970  -72.073 1.00 33.10 ? 142  HIS A CD2   1 
ATOM   5507 C CE1   . HIS B 1 144 ? 20.878 -4.614  -73.521 1.00 33.38 ? 142  HIS A CE1   1 
ATOM   5508 N NE2   . HIS B 1 144 ? 21.350 -4.125  -72.361 1.00 31.09 ? 142  HIS A NE2   1 
ATOM   5509 N N     . ALA B 1 145 ? 18.009 1.514   -74.524 1.00 24.14 ? 143  ALA A N     1 
ATOM   5510 C CA    . ALA B 1 145 ? 16.883 2.290   -75.074 1.00 25.54 ? 143  ALA A CA    1 
ATOM   5511 C C     . ALA B 1 145 ? 17.202 2.683   -76.526 1.00 26.44 ? 143  ALA A C     1 
ATOM   5512 O O     . ALA B 1 145 ? 18.391 2.772   -76.881 1.00 26.04 ? 143  ALA A O     1 
ATOM   5513 C CB    . ALA B 1 145 ? 16.583 3.494   -74.219 1.00 27.20 ? 143  ALA A CB    1 
ATOM   5514 N N     . SER B 1 146 ? 16.162 2.915   -77.323 1.00 26.53 ? 144  SER A N     1 
ATOM   5515 C CA    . SER B 1 146 ? 16.246 3.450   -78.706 1.00 27.01 ? 144  SER A CA    1 
ATOM   5516 C C     . SER B 1 146 ? 16.848 4.866   -78.678 1.00 30.60 ? 144  SER A C     1 
ATOM   5517 O O     . SER B 1 146 ? 16.792 5.544   -77.632 1.00 24.95 ? 144  SER A O     1 
ATOM   5518 C CB    . SER B 1 146 ? 14.896 3.505   -79.337 1.00 27.21 ? 144  SER A CB    1 
ATOM   5519 O OG    . SER B 1 146 ? 14.120 4.512   -78.700 1.00 26.91 ? 144  SER A OG    1 
ATOM   5520 N N     . ASP B 1 147 ? 17.362 5.317   -79.821 1.00 32.03 ? 145  ASP A N     1 
ATOM   5521 C CA    . ASP B 1 147 ? 17.970 6.659   -79.966 1.00 31.25 ? 145  ASP A CA    1 
ATOM   5522 C C     . ASP B 1 147 ? 16.926 7.712   -79.603 1.00 31.14 ? 145  ASP A C     1 
ATOM   5523 O O     . ASP B 1 147 ? 17.291 8.700   -78.950 1.00 31.46 ? 145  ASP A O     1 
ATOM   5524 C CB    . ASP B 1 147 ? 18.524 6.860   -81.376 1.00 32.35 ? 145  ASP A CB    1 
ATOM   5525 C CG    . ASP B 1 147 ? 19.781 6.077   -81.678 1.00 36.52 ? 145  ASP A CG    1 
ATOM   5526 O OD1   . ASP B 1 147 ? 20.389 5.527   -80.733 1.00 34.53 ? 145  ASP A OD1   1 
ATOM   5527 O OD2   . ASP B 1 147 ? 20.168 6.059   -82.868 1.00 41.25 ? 145  ASP A OD2   1 
ATOM   5528 N N     . GLU B 1 148 ? 15.666 7.529   -79.998 1.00 30.93 ? 146  GLU A N     1 
ATOM   5529 C CA    . GLU B 1 148 ? 14.626 8.535   -79.663 1.00 34.50 ? 146  GLU A CA    1 
ATOM   5530 C C     . GLU B 1 148 ? 14.500 8.668   -78.148 1.00 31.35 ? 146  GLU A C     1 
ATOM   5531 O O     . GLU B 1 148 ? 14.433 9.793   -77.670 1.00 30.10 ? 146  GLU A O     1 
ATOM   5532 C CB    . GLU B 1 148 ? 13.243 8.158   -80.171 1.00 40.31 ? 146  GLU A CB    1 
ATOM   5533 C CG    . GLU B 1 148 ? 13.054 8.362   -81.651 1.00 48.15 ? 146  GLU A CG    1 
ATOM   5534 C CD    . GLU B 1 148 ? 11.725 7.781   -82.095 1.00 53.09 ? 146  GLU A CD    1 
ATOM   5535 O OE1   . GLU B 1 148 ? 11.745 6.827   -82.903 1.00 61.70 ? 146  GLU A OE1   1 
ATOM   5536 O OE2   . GLU B 1 148 ? 10.682 8.241   -81.578 1.00 50.89 ? 146  GLU A OE2   1 
ATOM   5537 N N     . LEU B 1 149 ? 14.401 7.554   -77.425 1.00 29.97 ? 147  LEU A N     1 
ATOM   5538 C CA    . LEU B 1 149 ? 14.250 7.607   -75.947 1.00 28.08 ? 147  LEU A CA    1 
ATOM   5539 C C     . LEU B 1 149 ? 15.507 8.221   -75.324 1.00 29.33 ? 147  LEU A C     1 
ATOM   5540 O O     . LEU B 1 149 ? 15.368 9.196   -74.548 1.00 30.93 ? 147  LEU A O     1 
ATOM   5541 C CB    . LEU B 1 149 ? 13.983 6.199   -75.414 1.00 28.63 ? 147  LEU A CB    1 
ATOM   5542 C CG    . LEU B 1 149 ? 12.643 5.588   -75.822 1.00 26.27 ? 147  LEU A CG    1 
ATOM   5543 C CD1   . LEU B 1 149 ? 12.453 4.237   -75.152 1.00 26.71 ? 147  LEU A CD1   1 
ATOM   5544 C CD2   . LEU B 1 149 ? 11.476 6.495   -75.469 1.00 25.50 ? 147  LEU A CD2   1 
ATOM   5545 N N     . LYS B 1 150 ? 16.689 7.709   -75.656 1.00 26.08 ? 148  LYS A N     1 
ATOM   5546 C CA    . LYS B 1 150 ? 17.965 8.260   -75.126 1.00 28.58 ? 148  LYS A CA    1 
ATOM   5547 C C     . LYS B 1 150 ? 18.012 9.781   -75.341 1.00 30.81 ? 148  LYS A C     1 
ATOM   5548 O O     . LYS B 1 150 ? 18.384 10.494  -74.397 1.00 26.76 ? 148  LYS A O     1 
ATOM   5549 C CB    . LYS B 1 150 ? 19.168 7.580   -75.775 1.00 27.40 ? 148  LYS A CB    1 
ATOM   5550 C CG    . LYS B 1 150 ? 19.433 6.181   -75.258 1.00 27.88 ? 148  LYS A CG    1 
ATOM   5551 C CD    . LYS B 1 150 ? 20.759 5.627   -75.654 1.00 29.62 ? 148  LYS A CD    1 
ATOM   5552 C CE    . LYS B 1 150 ? 20.938 5.558   -77.158 1.00 30.51 ? 148  LYS A CE    1 
ATOM   5553 N NZ    . LYS B 1 150 ? 21.958 4.547   -77.497 1.00 32.89 ? 148  LYS A NZ    1 
ATOM   5554 N N     . ASP B 1 151 ? 17.637 10.275  -76.523 1.00 33.69 ? 149  ASP A N     1 
ATOM   5555 C CA    . ASP B 1 151 ? 17.797 11.717  -76.873 1.00 32.99 ? 149  ASP A CA    1 
ATOM   5556 C C     . ASP B 1 151 ? 16.746 12.537  -76.143 1.00 31.09 ? 149  ASP A C     1 
ATOM   5557 O O     . ASP B 1 151 ? 17.032 13.677  -75.788 1.00 33.97 ? 149  ASP A O     1 
ATOM   5558 C CB    . ASP B 1 151 ? 17.692 11.989  -78.375 1.00 33.98 ? 149  ASP A CB    1 
ATOM   5559 C CG    . ASP B 1 151 ? 18.808 11.375  -79.194 1.00 34.95 ? 149  ASP A CG    1 
ATOM   5560 O OD1   . ASP B 1 151 ? 19.899 11.191  -78.650 1.00 42.22 ? 149  ASP A OD1   1 
ATOM   5561 O OD2   . ASP B 1 151 ? 18.571 11.067  -80.373 1.00 43.74 ? 149  ASP A OD2   1 
ATOM   5562 N N     . LYS B 1 152 ? 15.575 11.973  -75.894 1.00 30.46 ? 150  LYS A N     1 
ATOM   5563 C CA    . LYS B 1 152 ? 14.495 12.714  -75.215 1.00 33.03 ? 150  LYS A CA    1 
ATOM   5564 C C     . LYS B 1 152 ? 14.764 12.803  -73.700 1.00 28.69 ? 150  LYS A C     1 
ATOM   5565 O O     . LYS B 1 152 ? 14.438 13.857  -73.129 1.00 27.05 ? 150  LYS A O     1 
ATOM   5566 C CB    . LYS B 1 152 ? 13.139 12.096  -75.567 1.00 33.55 ? 150  LYS A CB    1 
ATOM   5567 C CG    . LYS B 1 152 ? 11.933 12.854  -75.044 1.00 41.30 ? 150  LYS A CG    1 
ATOM   5568 C CD    . LYS B 1 152 ? 10.650 12.565  -75.824 1.00 47.29 ? 150  LYS A CD    1 
ATOM   5569 C CE    . LYS B 1 152 ? 10.385 13.568  -76.931 1.00 54.04 ? 150  LYS A CE    1 
ATOM   5570 N NZ    . LYS B 1 152 ? 9.032  14.164  -76.821 1.00 61.64 ? 150  LYS A NZ    1 
ATOM   5571 N N     . TYR B 1 153 ? 15.324 11.775  -73.056 1.00 25.69 ? 151  TYR A N     1 
ATOM   5572 C CA    . TYR B 1 153 ? 15.353 11.664  -71.568 1.00 25.54 ? 151  TYR A CA    1 
ATOM   5573 C C     . TYR B 1 153 ? 16.769 11.777  -70.965 1.00 25.04 ? 151  TYR A C     1 
ATOM   5574 O O     . TYR B 1 153 ? 16.864 12.335  -69.851 1.00 25.17 ? 151  TYR A O     1 
ATOM   5575 C CB    . TYR B 1 153 ? 14.640 10.374  -71.131 1.00 25.21 ? 151  TYR A CB    1 
ATOM   5576 C CG    . TYR B 1 153 ? 13.184 10.376  -71.512 1.00 25.61 ? 151  TYR A CG    1 
ATOM   5577 C CD1   . TYR B 1 153 ? 12.259 11.047  -70.732 1.00 27.01 ? 151  TYR A CD1   1 
ATOM   5578 C CD2   . TYR B 1 153 ? 12.745 9.747   -72.663 1.00 27.65 ? 151  TYR A CD2   1 
ATOM   5579 C CE1   . TYR B 1 153 ? 10.920 11.082  -71.082 1.00 29.50 ? 151  TYR A CE1   1 
ATOM   5580 C CE2   . TYR B 1 153 ? 11.416 9.802   -73.052 1.00 27.55 ? 151  TYR A CE2   1 
ATOM   5581 C CZ    . TYR B 1 153 ? 10.504 10.458  -72.251 1.00 28.98 ? 151  TYR A CZ    1 
ATOM   5582 O OH    . TYR B 1 153 ? 9.199  10.507  -72.620 1.00 31.22 ? 151  TYR A OH    1 
ATOM   5583 N N     . LEU B 1 154 ? 17.825 11.243  -71.596 1.00 24.51 ? 152  LEU A N     1 
ATOM   5584 C CA    . LEU B 1 154 ? 19.166 11.163  -70.936 1.00 24.23 ? 152  LEU A CA    1 
ATOM   5585 C C     . LEU B 1 154 ? 19.700 12.546  -70.572 1.00 26.34 ? 152  LEU A C     1 
ATOM   5586 O O     . LEU B 1 154 ? 20.174 12.729  -69.450 1.00 24.87 ? 152  LEU A O     1 
ATOM   5587 C CB    . LEU B 1 154 ? 20.175 10.362  -71.767 1.00 24.17 ? 152  LEU A CB    1 
ATOM   5588 C CG    . LEU B 1 154 ? 20.011 8.844   -71.669 1.00 23.53 ? 152  LEU A CG    1 
ATOM   5589 C CD1   . LEU B 1 154 ? 21.111 8.107   -72.418 1.00 24.58 ? 152  LEU A CD1   1 
ATOM   5590 C CD2   . LEU B 1 154 ? 19.987 8.428   -70.211 1.00 24.23 ? 152  LEU A CD2   1 
ATOM   5591 N N     . PRO B 1 155 ? 19.656 13.583  -71.433 1.00 26.15 ? 153  PRO A N     1 
ATOM   5592 C CA    . PRO B 1 155 ? 20.296 14.855  -71.068 1.00 25.35 ? 153  PRO A CA    1 
ATOM   5593 C C     . PRO B 1 155 ? 19.741 15.407  -69.758 1.00 23.59 ? 153  PRO A C     1 
ATOM   5594 O O     . PRO B 1 155 ? 20.543 15.775  -68.934 1.00 24.89 ? 153  PRO A O     1 
ATOM   5595 C CB    . PRO B 1 155 ? 20.057 15.760  -72.299 1.00 26.69 ? 153  PRO A CB    1 
ATOM   5596 C CG    . PRO B 1 155 ? 19.898 14.780  -73.427 1.00 24.36 ? 153  PRO A CG    1 
ATOM   5597 C CD    . PRO B 1 155 ? 19.131 13.618  -72.799 1.00 26.57 ? 153  PRO A CD    1 
ATOM   5598 N N     . ASN B 1 156 ? 18.423 15.426  -69.552 1.00 23.25 ? 154  ASN A N     1 
ATOM   5599 C CA    . ASN B 1 156 ? 17.837 16.009  -68.313 1.00 25.14 ? 154  ASN A CA    1 
ATOM   5600 C C     . ASN B 1 156 ? 18.170 15.115  -67.109 1.00 25.95 ? 154  ASN A C     1 
ATOM   5601 O O     . ASN B 1 156 ? 18.252 15.629  -65.987 1.00 23.56 ? 154  ASN A O     1 
ATOM   5602 C CB    . ASN B 1 156 ? 16.332 16.221  -68.424 1.00 28.13 ? 154  ASN A CB    1 
ATOM   5603 C CG    . ASN B 1 156 ? 15.984 17.519  -69.121 1.00 35.64 ? 154  ASN A CG    1 
ATOM   5604 O OD1   . ASN B 1 156 ? 16.661 18.532  -68.934 1.00 38.48 ? 154  ASN A OD1   1 
ATOM   5605 N ND2   . ASN B 1 156 ? 14.931 17.495  -69.924 1.00 34.28 ? 154  ASN A ND2   1 
ATOM   5606 N N     . MET B 1 157 ? 18.329 13.810  -67.323 1.00 24.21 ? 155  MET A N     1 
ATOM   5607 C CA    . MET B 1 157 ? 18.651 12.865  -66.223 1.00 24.51 ? 155  MET A CA    1 
ATOM   5608 C C     . MET B 1 157 ? 20.129 13.025  -65.827 1.00 23.88 ? 155  MET A C     1 
ATOM   5609 O O     . MET B 1 157 ? 20.395 13.083  -64.616 1.00 22.51 ? 155  MET A O     1 
ATOM   5610 C CB    . MET B 1 157 ? 18.338 11.421  -66.627 1.00 22.48 ? 155  MET A CB    1 
ATOM   5611 C CG    . MET B 1 157 ? 16.834 11.227  -66.795 1.00 23.18 ? 155  MET A CG    1 
ATOM   5612 S SD    . MET B 1 157 ? 16.339 9.637   -67.472 1.00 23.72 ? 155  MET A SD    1 
ATOM   5613 C CE    . MET B 1 157 ? 16.649 8.624   -66.033 1.00 24.50 ? 155  MET A CE    1 
ATOM   5614 N N     . TYR B 1 158 ? 21.056 13.123  -66.783 1.00 24.17 ? 156  TYR A N     1 
ATOM   5615 C CA    . TYR B 1 158 ? 22.493 13.330  -66.451 1.00 25.48 ? 156  TYR A CA    1 
ATOM   5616 C C     . TYR B 1 158 ? 22.659 14.699  -65.776 1.00 26.10 ? 156  TYR A C     1 
ATOM   5617 O O     . TYR B 1 158 ? 23.495 14.814  -64.899 1.00 29.58 ? 156  TYR A O     1 
ATOM   5618 C CB    . TYR B 1 158 ? 23.403 13.178  -67.668 1.00 24.03 ? 156  TYR A CB    1 
ATOM   5619 C CG    . TYR B 1 158 ? 23.586 11.766  -68.171 1.00 24.78 ? 156  TYR A CG    1 
ATOM   5620 C CD1   . TYR B 1 158 ? 24.006 10.747  -67.341 1.00 26.02 ? 156  TYR A CD1   1 
ATOM   5621 C CD2   . TYR B 1 158 ? 23.338 11.453  -69.501 1.00 26.28 ? 156  TYR A CD2   1 
ATOM   5622 C CE1   . TYR B 1 158 ? 24.216 9.461   -67.818 1.00 27.07 ? 156  TYR A CE1   1 
ATOM   5623 C CE2   . TYR B 1 158 ? 23.516 10.167  -69.987 1.00 26.58 ? 156  TYR A CE2   1 
ATOM   5624 C CZ    . TYR B 1 158 ? 23.988 9.177   -69.155 1.00 25.75 ? 156  TYR A CZ    1 
ATOM   5625 O OH    . TYR B 1 158 ? 24.148 7.925   -69.643 1.00 25.56 ? 156  TYR A OH    1 
ATOM   5626 N N     . ALA B 1 159 ? 21.835 15.693  -66.105 1.00 29.10 ? 157  ALA A N     1 
ATOM   5627 C CA    . ALA B 1 159 ? 21.882 17.026  -65.450 1.00 27.35 ? 157  ALA A CA    1 
ATOM   5628 C C     . ALA B 1 159 ? 21.180 16.987  -64.096 1.00 29.43 ? 157  ALA A C     1 
ATOM   5629 O O     . ALA B 1 159 ? 21.248 17.995  -63.360 1.00 28.36 ? 157  ALA A O     1 
ATOM   5630 C CB    . ALA B 1 159 ? 21.237 18.053  -66.338 1.00 29.35 ? 157  ALA A CB    1 
ATOM   5631 N N     . GLY B 1 160 ? 20.450 15.913  -63.791 1.00 25.87 ? 158  GLY A N     1 
ATOM   5632 C CA    . GLY B 1 160 ? 19.704 15.836  -62.519 1.00 29.93 ? 158  GLY A CA    1 
ATOM   5633 C C     . GLY B 1 160 ? 18.468 16.734  -62.492 1.00 28.23 ? 158  GLY A C     1 
ATOM   5634 O O     . GLY B 1 160 ? 17.909 16.925  -61.407 1.00 28.58 ? 158  GLY A O     1 
ATOM   5635 N N     . ILE B 1 161 ? 18.010 17.231  -63.647 1.00 27.59 ? 159  ILE A N     1 
ATOM   5636 C CA    . ILE B 1 161 ? 16.739 18.018  -63.753 1.00 26.43 ? 159  ILE A CA    1 
ATOM   5637 C C     . ILE B 1 161 ? 15.552 17.062  -63.672 1.00 25.66 ? 159  ILE A C     1 
ATOM   5638 O O     . ILE B 1 161 ? 14.555 17.416  -63.039 1.00 22.88 ? 159  ILE A O     1 
ATOM   5639 C CB    . ILE B 1 161 ? 16.727 18.826  -65.057 1.00 28.74 ? 159  ILE A CB    1 
ATOM   5640 C CG1   . ILE B 1 161 ? 17.864 19.854  -65.059 1.00 31.65 ? 159  ILE A CG1   1 
ATOM   5641 C CG2   . ILE B 1 161 ? 15.353 19.463  -65.299 1.00 28.06 ? 159  ILE A CG2   1 
ATOM   5642 C CD1   . ILE B 1 161 ? 17.611 21.058  -64.188 1.00 34.50 ? 159  ILE A CD1   1 
ATOM   5643 N N     . TRP B 1 162 ? 15.690 15.885  -64.282 1.00 25.59 ? 160  TRP A N     1 
ATOM   5644 C CA    . TRP B 1 162 ? 14.708 14.773  -64.154 1.00 28.29 ? 160  TRP A CA    1 
ATOM   5645 C C     . TRP B 1 162 ? 15.362 13.613  -63.394 1.00 26.00 ? 160  TRP A C     1 
ATOM   5646 O O     . TRP B 1 162 ? 16.505 13.289  -63.703 1.00 24.89 ? 160  TRP A O     1 
ATOM   5647 C CB    . TRP B 1 162 ? 14.201 14.308  -65.530 1.00 27.07 ? 160  TRP A CB    1 
ATOM   5648 C CG    . TRP B 1 162 ? 13.418 15.331  -66.297 1.00 26.99 ? 160  TRP A CG    1 
ATOM   5649 C CD1   . TRP B 1 162 ? 12.898 16.498  -65.825 1.00 25.90 ? 160  TRP A CD1   1 
ATOM   5650 C CD2   . TRP B 1 162 ? 13.048 15.266  -67.685 1.00 25.80 ? 160  TRP A CD2   1 
ATOM   5651 N NE1   . TRP B 1 162 ? 12.261 17.167  -66.834 1.00 25.45 ? 160  TRP A NE1   1 
ATOM   5652 C CE2   . TRP B 1 162 ? 12.317 16.437  -67.981 1.00 25.83 ? 160  TRP A CE2   1 
ATOM   5653 C CE3   . TRP B 1 162 ? 13.267 14.347  -68.714 1.00 26.03 ? 160  TRP A CE3   1 
ATOM   5654 C CZ2   . TRP B 1 162 ? 11.792 16.705  -69.252 1.00 25.99 ? 160  TRP A CZ2   1 
ATOM   5655 C CZ3   . TRP B 1 162 ? 12.775 14.620  -69.971 1.00 27.01 ? 160  TRP A CZ3   1 
ATOM   5656 C CH2   . TRP B 1 162 ? 12.058 15.790  -70.241 1.00 26.48 ? 160  TRP A CH2   1 
ATOM   5657 N N     . ALA B 1 163 ? 14.673 13.040  -62.405 1.00 24.56 ? 161  ALA A N     1 
ATOM   5658 C CA    . ALA B 1 163 ? 15.166 11.872  -61.641 1.00 25.82 ? 161  ALA A CA    1 
ATOM   5659 C C     . ALA B 1 163 ? 14.757 10.595  -62.365 1.00 23.55 ? 161  ALA A C     1 
ATOM   5660 O O     . ALA B 1 163 ? 13.936 10.677  -63.304 1.00 24.67 ? 161  ALA A O     1 
ATOM   5661 C CB    . ALA B 1 163 ? 14.638 11.867  -60.226 1.00 26.93 ? 161  ALA A CB    1 
ATOM   5662 N N     . GLY B 1 164 ? 15.356 9.481   -61.946 1.00 24.06 ? 162  GLY A N     1 
ATOM   5663 C CA    . GLY B 1 164 ? 14.965 8.113   -62.338 1.00 23.27 ? 162  GLY A CA    1 
ATOM   5664 C C     . GLY B 1 164 ? 14.374 7.351   -61.178 1.00 21.56 ? 162  GLY A C     1 
ATOM   5665 O O     . GLY B 1 164 ? 14.537 7.788   -60.010 1.00 21.62 ? 162  GLY A O     1 
ATOM   5666 N N     . SER B 1 165 ? 13.691 6.238   -61.476 1.00 22.60 ? 163  SER A N     1 
ATOM   5667 C CA    . SER B 1 165 ? 13.270 5.232   -60.476 1.00 21.68 ? 163  SER A CA    1 
ATOM   5668 C C     . SER B 1 165 ? 13.398 3.865   -61.130 1.00 22.53 ? 163  SER A C     1 
ATOM   5669 O O     . SER B 1 165 ? 13.460 3.816   -62.379 1.00 22.79 ? 163  SER A O     1 
ATOM   5670 C CB    . SER B 1 165 ? 11.877 5.471   -59.924 1.00 24.56 ? 163  SER A CB    1 
ATOM   5671 O OG    . SER B 1 165 ? 10.906 4.885   -60.775 1.00 26.99 ? 163  SER A OG    1 
ATOM   5672 N N     . MET B 1 166 ? 13.514 2.828   -60.305 1.00 21.53 ? 164  MET A N     1 
ATOM   5673 C CA    . MET B 1 166 ? 13.466 1.404   -60.691 1.00 24.48 ? 164  MET A CA    1 
ATOM   5674 C C     . MET B 1 166 ? 12.177 0.823   -60.105 1.00 23.53 ? 164  MET A C     1 
ATOM   5675 O O     . MET B 1 166 ? 12.078 0.682   -58.881 1.00 22.07 ? 164  MET A O     1 
ATOM   5676 C CB    . MET B 1 166 ? 14.701 0.681   -60.136 1.00 31.80 ? 164  MET A CB    1 
ATOM   5677 C CG    . MET B 1 166 ? 16.022 1.403   -60.425 1.00 36.98 ? 164  MET A CG    1 
ATOM   5678 S SD    . MET B 1 166 ? 16.307 1.626   -62.210 1.00 58.33 ? 164  MET A SD    1 
ATOM   5679 C CE    . MET B 1 166 ? 15.877 0.001   -62.843 1.00 58.99 ? 164  MET A CE    1 
ATOM   5680 N N     . CYS B 1 167 ? 11.175 0.568   -60.938 1.00 22.43 ? 165  CYS A N     1 
ATOM   5681 C CA    . CYS B 1 167 ? 9.865  0.033   -60.509 1.00 22.21 ? 165  CYS A CA    1 
ATOM   5682 C C     . CYS B 1 167 ? 9.808  -1.457  -60.844 1.00 22.19 ? 165  CYS A C     1 
ATOM   5683 O O     . CYS B 1 167 ? 9.240  -1.807  -61.906 1.00 21.59 ? 165  CYS A O     1 
ATOM   5684 C CB    . CYS B 1 167 ? 8.692  0.776   -61.129 1.00 21.32 ? 165  CYS A CB    1 
ATOM   5685 S SG    . CYS B 1 167 ? 8.610  2.524   -60.644 1.00 24.00 ? 165  CYS A SG    1 
ATOM   5686 N N     . LEU B 1 168 ? 10.338 -2.289  -59.950 1.00 21.60 ? 166  LEU A N     1 
ATOM   5687 C CA    . LEU B 1 168 ? 10.428 -3.772  -60.154 1.00 21.53 ? 166  LEU A CA    1 
ATOM   5688 C C     . LEU B 1 168 ? 9.439  -4.496  -59.227 1.00 20.54 ? 166  LEU A C     1 
ATOM   5689 O O     . LEU B 1 168 ? 8.550  -5.263  -59.723 1.00 21.22 ? 166  LEU A O     1 
ATOM   5690 C CB    . LEU B 1 168 ? 11.870 -4.262  -59.941 1.00 21.93 ? 166  LEU A CB    1 
ATOM   5691 C CG    . LEU B 1 168 ? 13.018 -3.372  -60.440 1.00 25.94 ? 166  LEU A CG    1 
ATOM   5692 C CD1   . LEU B 1 168 ? 14.351 -4.120  -60.311 1.00 28.91 ? 166  LEU A CD1   1 
ATOM   5693 C CD2   . LEU B 1 168 ? 12.831 -2.903  -61.871 1.00 27.92 ? 166  LEU A CD2   1 
ATOM   5694 N N     . THR B 1 169 ? 9.561  -4.246  -57.934 1.00 19.63 ? 167  THR A N     1 
ATOM   5695 C CA    . THR B 1 169 ? 8.968  -5.050  -56.849 1.00 19.58 ? 167  THR A CA    1 
ATOM   5696 C C     . THR B 1 169 ? 7.454  -4.845  -56.797 1.00 19.70 ? 167  THR A C     1 
ATOM   5697 O O     . THR B 1 169 ? 6.969  -3.683  -56.942 1.00 18.89 ? 167  THR A O     1 
ATOM   5698 C CB    . THR B 1 169 ? 9.610  -4.656  -55.519 1.00 18.55 ? 167  THR A CB    1 
ATOM   5699 O OG1   . THR B 1 169 ? 11.008 -4.890  -55.672 1.00 19.14 ? 167  THR A OG1   1 
ATOM   5700 C CG2   . THR B 1 169 ? 9.028  -5.389  -54.342 1.00 18.71 ? 167  THR A CG2   1 
ATOM   5701 N N     . GLU B 1 170 ? 6.743  -5.944  -56.578 1.00 19.57 ? 168  GLU A N     1 
ATOM   5702 C CA    . GLU B 1 170 ? 5.269  -5.940  -56.406 1.00 21.20 ? 168  GLU A CA    1 
ATOM   5703 C C     . GLU B 1 170 ? 4.965  -6.555  -55.048 1.00 21.14 ? 168  GLU A C     1 
ATOM   5704 O O     . GLU B 1 170 ? 5.823  -7.171  -54.466 1.00 19.78 ? 168  GLU A O     1 
ATOM   5705 C CB    . GLU B 1 170 ? 4.608  -6.664  -57.576 1.00 21.73 ? 168  GLU A CB    1 
ATOM   5706 C CG    . GLU B 1 170 ? 4.862  -5.956  -58.895 1.00 24.43 ? 168  GLU A CG    1 
ATOM   5707 C CD    . GLU B 1 170 ? 4.192  -6.586  -60.096 1.00 24.61 ? 168  GLU A CD    1 
ATOM   5708 O OE1   . GLU B 1 170 ? 3.470  -7.575  -59.876 1.00 25.33 ? 168  GLU A OE1   1 
ATOM   5709 O OE2   . GLU B 1 170 ? 4.415  -6.098  -61.252 1.00 23.03 ? 168  GLU A OE2   1 
ATOM   5710 N N     . PRO B 1 171 ? 3.725  -6.457  -54.528 1.00 22.35 ? 169  PRO A N     1 
ATOM   5711 C CA    . PRO B 1 171 ? 3.404  -7.022  -53.219 1.00 24.42 ? 169  PRO A CA    1 
ATOM   5712 C C     . PRO B 1 171 ? 3.836  -8.484  -53.025 1.00 23.89 ? 169  PRO A C     1 
ATOM   5713 O O     . PRO B 1 171 ? 4.290  -8.793  -51.961 1.00 25.86 ? 169  PRO A O     1 
ATOM   5714 C CB    . PRO B 1 171 ? 1.875  -6.843  -53.136 1.00 24.36 ? 169  PRO A CB    1 
ATOM   5715 C CG    . PRO B 1 171 ? 1.641  -5.580  -53.945 1.00 24.46 ? 169  PRO A CG    1 
ATOM   5716 C CD    . PRO B 1 171 ? 2.596  -5.735  -55.131 1.00 22.97 ? 169  PRO A CD    1 
ATOM   5717 N N     . HIS B 1 172 ? 3.718  -9.301  -54.064 1.00 23.87 ? 170  HIS A N     1 
ATOM   5718 C CA    . HIS B 1 172 ? 3.931  -10.774 -54.041 1.00 23.98 ? 170  HIS A CA    1 
ATOM   5719 C C     . HIS B 1 172 ? 5.262  -11.146 -54.719 1.00 23.81 ? 170  HIS A C     1 
ATOM   5720 O O     . HIS B 1 172 ? 5.609  -12.382 -54.752 1.00 25.99 ? 170  HIS A O     1 
ATOM   5721 C CB    . HIS B 1 172 ? 2.754  -11.448 -54.757 1.00 26.36 ? 170  HIS A CB    1 
ATOM   5722 C CG    . HIS B 1 172 ? 2.778  -11.170 -56.225 1.00 30.89 ? 170  HIS A CG    1 
ATOM   5723 N ND1   . HIS B 1 172 ? 2.623  -9.871  -56.741 1.00 31.79 ? 170  HIS A ND1   1 
ATOM   5724 C CD2   . HIS B 1 172 ? 3.020  -11.982 -57.286 1.00 32.80 ? 170  HIS A CD2   1 
ATOM   5725 C CE1   . HIS B 1 172 ? 2.724  -9.913  -58.050 1.00 31.43 ? 170  HIS A CE1   1 
ATOM   5726 N NE2   . HIS B 1 172 ? 2.970  -11.214 -58.419 1.00 33.82 ? 170  HIS A NE2   1 
ATOM   5727 N N     . ALA B 1 173 ? 5.992  -10.165 -55.264 1.00 22.00 ? 171  ALA A N     1 
ATOM   5728 C CA    . ALA B 1 173 ? 7.191  -10.435 -56.102 1.00 23.38 ? 171  ALA A CA    1 
ATOM   5729 C C     . ALA B 1 173 ? 8.329  -9.462  -55.800 1.00 22.97 ? 171  ALA A C     1 
ATOM   5730 O O     . ALA B 1 173 ? 8.241  -8.306  -56.231 1.00 23.94 ? 171  ALA A O     1 
ATOM   5731 C CB    . ALA B 1 173 ? 6.851  -10.409 -57.576 1.00 23.53 ? 171  ALA A CB    1 
ATOM   5732 N N     . GLY B 1 174 ? 9.397  -9.973  -55.175 1.00 23.49 ? 172  GLY A N     1 
ATOM   5733 C CA    . GLY B 1 174 ? 10.651 -9.234  -54.957 1.00 23.66 ? 172  GLY A CA    1 
ATOM   5734 C C     . GLY B 1 174 ? 11.817 -9.936  -55.617 1.00 23.98 ? 172  GLY A C     1 
ATOM   5735 O O     . GLY B 1 174 ? 12.328 -9.425  -56.623 1.00 23.19 ? 172  GLY A O     1 
ATOM   5736 N N     . THR B 1 175 ? 12.241 -11.055 -55.033 1.00 24.24 ? 173  THR A N     1 
ATOM   5737 C CA    . THR B 1 175 ? 13.315 -11.909 -55.590 1.00 23.53 ? 173  THR A CA    1 
ATOM   5738 C C     . THR B 1 175 ? 12.799 -12.505 -56.903 1.00 24.32 ? 173  THR A C     1 
ATOM   5739 O O     . THR B 1 175 ? 13.558 -12.523 -57.881 1.00 25.24 ? 173  THR A O     1 
ATOM   5740 C CB    . THR B 1 175 ? 13.710 -12.991 -54.583 1.00 23.22 ? 173  THR A CB    1 
ATOM   5741 O OG1   . THR B 1 175 ? 14.184 -12.329 -53.402 1.00 22.92 ? 173  THR A OG1   1 
ATOM   5742 C CG2   . THR B 1 175 ? 14.735 -13.946 -55.147 1.00 22.93 ? 173  THR A CG2   1 
ATOM   5743 N N     . ASP B 1 176 ? 11.554 -12.981 -56.909 1.00 24.45 ? 174  ASP A N     1 
ATOM   5744 C CA    . ASP B 1 176 ? 10.971 -13.838 -57.982 1.00 25.67 ? 174  ASP A CA    1 
ATOM   5745 C C     . ASP B 1 176 ? 10.232 -12.915 -58.958 1.00 26.66 ? 174  ASP A C     1 
ATOM   5746 O O     . ASP B 1 176 ? 8.999  -12.868 -58.940 1.00 25.13 ? 174  ASP A O     1 
ATOM   5747 C CB    . ASP B 1 176 ? 10.114 -14.951 -57.366 1.00 26.60 ? 174  ASP A CB    1 
ATOM   5748 C CG    . ASP B 1 176 ? 9.548  -16.003 -58.320 1.00 29.11 ? 174  ASP A CG    1 
ATOM   5749 O OD1   . ASP B 1 176 ? 9.735  -15.845 -59.563 1.00 26.87 ? 174  ASP A OD1   1 
ATOM   5750 O OD2   . ASP B 1 176 ? 8.897  -16.968 -57.813 1.00 27.39 ? 174  ASP A OD2   1 
ATOM   5751 N N     . LEU B 1 177 ? 10.967 -12.207 -59.812 1.00 26.24 ? 175  LEU A N     1 
ATOM   5752 C CA    . LEU B 1 177 ? 10.343 -11.179 -60.681 1.00 26.04 ? 175  LEU A CA    1 
ATOM   5753 C C     . LEU B 1 177 ? 9.561  -11.858 -61.814 1.00 25.75 ? 175  LEU A C     1 
ATOM   5754 O O     . LEU B 1 177 ? 8.674  -11.199 -62.368 1.00 26.26 ? 175  LEU A O     1 
ATOM   5755 C CB    . LEU B 1 177 ? 11.428 -10.221 -61.172 1.00 25.84 ? 175  LEU A CB    1 
ATOM   5756 C CG    . LEU B 1 177 ? 11.936 -9.259  -60.105 1.00 26.82 ? 175  LEU A CG    1 
ATOM   5757 C CD1   . LEU B 1 177 ? 13.087 -8.426  -60.643 1.00 29.92 ? 175  LEU A CD1   1 
ATOM   5758 C CD2   . LEU B 1 177 ? 10.809 -8.371  -59.571 1.00 27.02 ? 175  LEU A CD2   1 
ATOM   5759 N N     . GLY B 1 178 ? 9.808  -13.151 -62.058 1.00 23.84 ? 176  GLY A N     1 
ATOM   5760 C CA    . GLY B 1 178 ? 9.097  -13.962 -63.070 1.00 25.03 ? 176  GLY A CA    1 
ATOM   5761 C C     . GLY B 1 178 ? 7.591  -13.973 -62.877 1.00 25.07 ? 176  GLY A C     1 
ATOM   5762 O O     . GLY B 1 178 ? 6.862  -14.203 -63.880 1.00 25.02 ? 176  GLY A O     1 
ATOM   5763 N N     . ILE B 1 179 ? 7.124  -13.713 -61.655 1.00 24.73 ? 177  ILE A N     1 
ATOM   5764 C CA    . ILE B 1 179 ? 5.662  -13.778 -61.344 1.00 24.28 ? 177  ILE A CA    1 
ATOM   5765 C C     . ILE B 1 179 ? 5.052  -12.372 -61.234 1.00 24.23 ? 177  ILE A C     1 
ATOM   5766 O O     . ILE B 1 179 ? 3.953  -12.256 -60.714 1.00 24.61 ? 177  ILE A O     1 
ATOM   5767 C CB    . ILE B 1 179 ? 5.412  -14.585 -60.057 1.00 26.09 ? 177  ILE A CB    1 
ATOM   5768 C CG1   . ILE B 1 179 ? 6.059  -13.938 -58.830 1.00 25.18 ? 177  ILE A CG1   1 
ATOM   5769 C CG2   . ILE B 1 179 ? 5.864  -16.024 -60.238 1.00 27.80 ? 177  ILE A CG2   1 
ATOM   5770 C CD1   . ILE B 1 179 ? 5.840  -14.708 -57.550 1.00 27.77 ? 177  ILE A CD1   1 
ATOM   5771 N N     . ILE B 1 180 ? 5.727  -11.361 -61.751 1.00 23.10 ? 178  ILE A N     1 
ATOM   5772 C CA    . ILE B 1 180 ? 5.108  -10.006 -61.737 1.00 22.87 ? 178  ILE A CA    1 
ATOM   5773 C C     . ILE B 1 180 ? 3.741  -10.025 -62.438 1.00 24.40 ? 178  ILE A C     1 
ATOM   5774 O O     . ILE B 1 180 ? 3.561  -10.825 -63.351 1.00 23.00 ? 178  ILE A O     1 
ATOM   5775 C CB    . ILE B 1 180 ? 6.046  -8.941  -62.334 1.00 23.02 ? 178  ILE A CB    1 
ATOM   5776 C CG1   . ILE B 1 180 ? 6.527  -9.312  -63.738 1.00 23.50 ? 178  ILE A CG1   1 
ATOM   5777 C CG2   . ILE B 1 180 ? 7.202  -8.649  -61.388 1.00 23.03 ? 178  ILE A CG2   1 
ATOM   5778 C CD1   . ILE B 1 180 ? 7.073  -8.139  -64.512 1.00 26.21 ? 178  ILE A CD1   1 
ATOM   5779 N N     . ARG B 1 181 ? 2.862  -9.104  -62.050 1.00 23.42 ? 179  ARG A N     1 
ATOM   5780 C CA    . ARG B 1 181 ? 1.487  -9.037  -62.590 1.00 23.63 ? 179  ARG A CA    1 
ATOM   5781 C C     . ARG B 1 181 ? 1.273  -7.757  -63.403 1.00 22.68 ? 179  ARG A C     1 
ATOM   5782 O O     . ARG B 1 181 ? 0.276  -7.677  -64.093 1.00 22.12 ? 179  ARG A O     1 
ATOM   5783 C CB    . ARG B 1 181 ? 0.529  -9.039  -61.402 1.00 26.36 ? 179  ARG A CB    1 
ATOM   5784 C CG    . ARG B 1 181 ? 0.413  -10.385 -60.704 1.00 27.25 ? 179  ARG A CG    1 
ATOM   5785 C CD    . ARG B 1 181 ? -0.367 -10.306 -59.407 1.00 28.93 ? 179  ARG A CD    1 
ATOM   5786 N NE    . ARG B 1 181 ? -0.222 -11.522 -58.625 1.00 29.28 ? 179  ARG A NE    1 
ATOM   5787 C CZ    . ARG B 1 181 ? -0.761 -11.717 -57.430 1.00 33.34 ? 179  ARG A CZ    1 
ATOM   5788 N NH1   . ARG B 1 181 ? -1.486 -10.767 -56.870 1.00 33.76 ? 179  ARG A NH1   1 
ATOM   5789 N NH2   . ARG B 1 181 ? -0.565 -12.856 -56.795 1.00 34.81 ? 179  ARG A NH2   1 
ATOM   5790 N N     . THR B 1 182 ? 2.174  -6.786  -63.258 1.00 21.52 ? 180  THR A N     1 
ATOM   5791 C CA    . THR B 1 182 ? 2.025  -5.502  -63.987 1.00 21.40 ? 180  THR A CA    1 
ATOM   5792 C C     . THR B 1 182 ? 2.024  -5.793  -65.493 1.00 22.19 ? 180  THR A C     1 
ATOM   5793 O O     . THR B 1 182 ? 2.894  -6.532  -65.948 1.00 20.97 ? 180  THR A O     1 
ATOM   5794 C CB    . THR B 1 182 ? 3.048  -4.456  -63.524 1.00 21.76 ? 180  THR A CB    1 
ATOM   5795 O OG1   . THR B 1 182 ? 2.846  -4.154  -62.145 1.00 22.60 ? 180  THR A OG1   1 
ATOM   5796 C CG2   . THR B 1 182 ? 2.981  -3.186  -64.343 1.00 21.90 ? 180  THR A CG2   1 
ATOM   5797 N N     . ARG B 1 183 ? 1.076  -5.205  -66.207 1.00 22.62 ? 181  ARG A N     1 
ATOM   5798 C CA    . ARG B 1 183 ? 0.911  -5.503  -67.648 1.00 25.58 ? 181  ARG A CA    1 
ATOM   5799 C C     . ARG B 1 183 ? 1.197  -4.285  -68.528 1.00 23.43 ? 181  ARG A C     1 
ATOM   5800 O O     . ARG B 1 183 ? 0.947  -3.168  -68.082 1.00 25.21 ? 181  ARG A O     1 
ATOM   5801 C CB    . ARG B 1 183 ? -0.510 -6.006  -67.916 1.00 30.46 ? 181  ARG A CB    1 
ATOM   5802 C CG    . ARG B 1 183 ? -0.621 -6.835  -69.187 1.00 42.12 ? 181  ARG A CG    1 
ATOM   5803 C CD    . ARG B 1 183 ? -1.866 -7.692  -69.266 1.00 45.75 ? 181  ARG A CD    1 
ATOM   5804 N NE    . ARG B 1 183 ? -1.973 -8.655  -68.188 1.00 48.94 ? 181  ARG A NE    1 
ATOM   5805 C CZ    . ARG B 1 183 ? -3.109 -9.231  -67.818 1.00 54.77 ? 181  ARG A CZ    1 
ATOM   5806 N NH1   . ARG B 1 183 ? -3.116 -10.102 -66.825 1.00 53.45 ? 181  ARG A NH1   1 
ATOM   5807 N NH2   . ARG B 1 183 ? -4.233 -8.932  -68.444 1.00 53.05 ? 181  ARG A NH2   1 
ATOM   5808 N N     . ALA B 1 184 ? 1.687  -4.539  -69.735 1.00 21.44 ? 182  ALA A N     1 
ATOM   5809 C CA    . ALA B 1 184 ? 1.959  -3.470  -70.712 1.00 23.08 ? 182  ALA A CA    1 
ATOM   5810 C C     . ALA B 1 184 ? 1.140  -3.787  -71.966 1.00 25.59 ? 182  ALA A C     1 
ATOM   5811 O O     . ALA B 1 184 ? 1.433  -4.792  -72.617 1.00 25.04 ? 182  ALA A O     1 
ATOM   5812 C CB    . ALA B 1 184 ? 3.430  -3.367  -71.006 1.00 20.58 ? 182  ALA A CB    1 
ATOM   5813 N N     . GLU B 1 185 ? 0.149  -2.957  -72.257 1.00 25.59 ? 183  GLU A N     1 
ATOM   5814 C CA    . GLU B 1 185 ? -0.774 -3.173  -73.405 1.00 25.25 ? 183  GLU A CA    1 
ATOM   5815 C C     . GLU B 1 185 ? -0.268 -2.399  -74.614 1.00 24.18 ? 183  GLU A C     1 
ATOM   5816 O O     . GLU B 1 185 ? -0.199 -1.172  -74.568 1.00 25.07 ? 183  GLU A O     1 
ATOM   5817 C CB    . GLU B 1 185 ? -2.187 -2.756  -73.003 1.00 28.82 ? 183  GLU A CB    1 
ATOM   5818 C CG    . GLU B 1 185 ? -3.215 -3.049  -74.065 1.00 34.37 ? 183  GLU A CG    1 
ATOM   5819 C CD    . GLU B 1 185 ? -3.383 -4.549  -74.305 1.00 38.66 ? 183  GLU A CD    1 
ATOM   5820 O OE1   . GLU B 1 185 ? -3.317 -5.313  -73.329 1.00 40.50 ? 183  GLU A OE1   1 
ATOM   5821 O OE2   . GLU B 1 185 ? -3.567 -4.948  -75.466 1.00 51.59 ? 183  GLU A OE2   1 
ATOM   5822 N N     . PRO B 1 186 ? 0.111  -3.064  -75.725 1.00 24.17 ? 184  PRO A N     1 
ATOM   5823 C CA    . PRO B 1 186 ? 0.621  -2.357  -76.893 1.00 26.69 ? 184  PRO A CA    1 
ATOM   5824 C C     . PRO B 1 186 ? -0.444 -1.436  -77.492 1.00 29.78 ? 184  PRO A C     1 
ATOM   5825 O O     . PRO B 1 186 ? -1.618 -1.785  -77.519 1.00 29.42 ? 184  PRO A O     1 
ATOM   5826 C CB    . PRO B 1 186 ? 1.095  -3.420  -77.876 1.00 26.67 ? 184  PRO A CB    1 
ATOM   5827 C CG    . PRO B 1 186 ? 0.523  -4.717  -77.360 1.00 30.44 ? 184  PRO A CG    1 
ATOM   5828 C CD    . PRO B 1 186 ? 0.173  -4.518  -75.898 1.00 26.69 ? 184  PRO A CD    1 
ATOM   5829 N N     . GLN B 1 187 ? -0.014 -0.234  -77.864 1.00 29.64 ? 185  GLN A N     1 
ATOM   5830 C CA    . GLN B 1 187 ? -0.897 0.792   -78.467 1.00 28.98 ? 185  GLN A CA    1 
ATOM   5831 C C     . GLN B 1 187 ? -0.526 0.950   -79.944 1.00 29.69 ? 185  GLN A C     1 
ATOM   5832 O O     . GLN B 1 187 ? 0.651  0.757   -80.327 1.00 27.97 ? 185  GLN A O     1 
ATOM   5833 C CB    . GLN B 1 187 ? -0.812 2.128   -77.734 1.00 29.21 ? 185  GLN A CB    1 
ATOM   5834 C CG    . GLN B 1 187 ? -1.061 2.053   -76.237 1.00 30.14 ? 185  GLN A CG    1 
ATOM   5835 C CD    . GLN B 1 187 ? -2.453 1.603   -75.864 1.00 31.18 ? 185  GLN A CD    1 
ATOM   5836 O OE1   . GLN B 1 187 ? -3.430 2.260   -76.174 1.00 32.65 ? 185  GLN A OE1   1 
ATOM   5837 N NE2   . GLN B 1 187 ? -2.554 0.503   -75.135 1.00 30.64 ? 185  GLN A NE2   1 
ATOM   5838 N N     . ALA B 1 188 ? -1.506 1.339   -80.754 1.00 32.92 ? 186  ALA A N     1 
ATOM   5839 C CA    . ALA B 1 188 ? -1.283 1.507   -82.203 1.00 33.74 ? 186  ALA A CA    1 
ATOM   5840 C C     . ALA B 1 188 ? -0.212 2.564   -82.476 1.00 32.81 ? 186  ALA A C     1 
ATOM   5841 O O     . ALA B 1 188 ? 0.475  2.438   -83.486 1.00 35.53 ? 186  ALA A O     1 
ATOM   5842 C CB    . ALA B 1 188 ? -2.591 1.883   -82.828 1.00 35.35 ? 186  ALA A CB    1 
ATOM   5843 N N     . ASP B 1 189 ? -0.096 3.562   -81.602 1.00 33.83 ? 187  ASP A N     1 
ATOM   5844 C CA    . ASP B 1 189 ? 0.885  4.663   -81.792 1.00 35.18 ? 187  ASP A CA    1 
ATOM   5845 C C     . ASP B 1 189 ? 2.320  4.242   -81.421 1.00 38.24 ? 187  ASP A C     1 
ATOM   5846 O O     . ASP B 1 189 ? 3.185  5.110   -81.423 1.00 39.42 ? 187  ASP A O     1 
ATOM   5847 C CB    . ASP B 1 189 ? 0.435  5.908   -81.029 1.00 37.58 ? 187  ASP A CB    1 
ATOM   5848 C CG    . ASP B 1 189 ? 0.528  5.796   -79.519 1.00 40.48 ? 187  ASP A CG    1 
ATOM   5849 O OD1   . ASP B 1 189 ? 0.925  4.729   -79.030 1.00 37.08 ? 187  ASP A OD1   1 
ATOM   5850 O OD2   . ASP B 1 189 ? 0.197  6.784   -78.852 1.00 34.46 ? 187  ASP A OD2   1 
ATOM   5851 N N     . GLY B 1 190 ? 2.555  2.964   -81.111 1.00 36.53 ? 188  GLY A N     1 
ATOM   5852 C CA    . GLY B 1 190 ? 3.909  2.474   -80.796 1.00 31.66 ? 188  GLY A CA    1 
ATOM   5853 C C     . GLY B 1 190 ? 4.207  2.476   -79.306 1.00 29.38 ? 188  GLY A C     1 
ATOM   5854 O O     . GLY B 1 190 ? 5.214  1.885   -78.914 1.00 29.07 ? 188  GLY A O     1 
ATOM   5855 N N     . SER B 1 191 ? 3.370  3.139   -78.526 1.00 27.35 ? 189  SER A N     1 
ATOM   5856 C CA    . SER B 1 191 ? 3.523  3.176   -77.056 1.00 27.99 ? 189  SER A CA    1 
ATOM   5857 C C     . SER B 1 191 ? 2.881  1.957   -76.388 1.00 26.80 ? 189  SER A C     1 
ATOM   5858 O O     . SER B 1 191 ? 2.369  1.092   -77.093 1.00 26.26 ? 189  SER A O     1 
ATOM   5859 C CB    . SER B 1 191 ? 2.910  4.430   -76.483 1.00 28.84 ? 189  SER A CB    1 
ATOM   5860 O OG    . SER B 1 191 ? 1.498  4.371   -76.516 1.00 26.74 ? 189  SER A OG    1 
ATOM   5861 N N     . TYR B 1 192 ? 2.942  1.934   -75.062 1.00 25.33 ? 190  TYR A N     1 
ATOM   5862 C CA    . TYR B 1 192 ? 2.301  0.869   -74.268 1.00 24.47 ? 190  TYR A CA    1 
ATOM   5863 C C     . TYR B 1 192 ? 1.591  1.534   -73.096 1.00 25.25 ? 190  TYR A C     1 
ATOM   5864 O O     . TYR B 1 192 ? 2.020  2.611   -72.677 1.00 24.21 ? 190  TYR A O     1 
ATOM   5865 C CB    . TYR B 1 192 ? 3.337  -0.111  -73.720 1.00 24.64 ? 190  TYR A CB    1 
ATOM   5866 C CG    . TYR B 1 192 ? 4.009  -1.001  -74.730 1.00 23.80 ? 190  TYR A CG    1 
ATOM   5867 C CD1   . TYR B 1 192 ? 5.067  -0.540  -75.492 1.00 23.90 ? 190  TYR A CD1   1 
ATOM   5868 C CD2   . TYR B 1 192 ? 3.609  -2.314  -74.897 1.00 23.84 ? 190  TYR A CD2   1 
ATOM   5869 C CE1   . TYR B 1 192 ? 5.697  -1.355  -76.415 1.00 25.08 ? 190  TYR A CE1   1 
ATOM   5870 C CE2   . TYR B 1 192 ? 4.232  -3.144  -75.810 1.00 24.17 ? 190  TYR A CE2   1 
ATOM   5871 C CZ    . TYR B 1 192 ? 5.278  -2.662  -76.573 1.00 25.94 ? 190  TYR A CZ    1 
ATOM   5872 O OH    . TYR B 1 192 ? 5.899  -3.471  -77.473 1.00 26.37 ? 190  TYR A OH    1 
ATOM   5873 N N     . LYS B 1 193 ? 0.499  0.940   -72.649 1.00 23.80 ? 191  LYS A N     1 
ATOM   5874 C CA    . LYS B 1 193 ? -0.213 1.410   -71.453 1.00 24.49 ? 191  LYS A CA    1 
ATOM   5875 C C     . LYS B 1 193 ? 0.060  0.411   -70.340 1.00 25.08 ? 191  LYS A C     1 
ATOM   5876 O O     . LYS B 1 193 ? -0.249 -0.798  -70.509 1.00 24.51 ? 191  LYS A O     1 
ATOM   5877 C CB    . LYS B 1 193 ? -1.686 1.642   -71.742 1.00 26.90 ? 191  LYS A CB    1 
ATOM   5878 C CG    . LYS B 1 193 ? -1.951 2.919   -72.514 1.00 28.75 ? 191  LYS A CG    1 
ATOM   5879 C CD    . LYS B 1 193 ? -3.417 3.257   -72.656 1.00 30.77 ? 191  LYS A CD    1 
ATOM   5880 C CE    . LYS B 1 193 ? -3.587 4.453   -73.563 1.00 34.24 ? 191  LYS A CE    1 
ATOM   5881 N NZ    . LYS B 1 193 ? -4.921 5.050   -73.384 1.00 38.82 ? 191  LYS A NZ    1 
ATOM   5882 N N     . ILE B 1 194 ? 0.693  0.931   -69.294 1.00 23.49 ? 192  ILE A N     1 
ATOM   5883 C CA    . ILE B 1 194 ? 1.136  0.074   -68.170 1.00 25.64 ? 192  ILE A CA    1 
ATOM   5884 C C     . ILE B 1 194 ? 0.111  0.124   -67.038 1.00 24.62 ? 192  ILE A C     1 
ATOM   5885 O O     . ILE B 1 194 ? -0.250 1.220   -66.609 1.00 25.04 ? 192  ILE A O     1 
ATOM   5886 C CB    . ILE B 1 194 ? 2.531  0.523   -67.678 1.00 27.86 ? 192  ILE A CB    1 
ATOM   5887 C CG1   . ILE B 1 194 ? 3.466  0.900   -68.831 1.00 30.09 ? 192  ILE A CG1   1 
ATOM   5888 C CG2   . ILE B 1 194 ? 3.138  -0.521  -66.753 1.00 28.00 ? 192  ILE A CG2   1 
ATOM   5889 C CD1   . ILE B 1 194 ? 3.671  -0.187  -69.844 1.00 33.96 ? 192  ILE A CD1   1 
ATOM   5890 N N     . SER B 1 195 ? -0.298 -1.051  -66.583 1.00 22.76 ? 193  SER A N     1 
ATOM   5891 C CA    . SER B 1 195 ? -1.273 -1.142  -65.484 1.00 25.11 ? 193  SER A CA    1 
ATOM   5892 C C     . SER B 1 195 ? -0.775 -2.149  -64.443 1.00 24.46 ? 193  SER A C     1 
ATOM   5893 O O     . SER B 1 195 ? -0.422 -3.268  -64.811 1.00 24.40 ? 193  SER A O     1 
ATOM   5894 C CB    . SER B 1 195 ? -2.651 -1.467  -66.022 1.00 24.71 ? 193  SER A CB    1 
ATOM   5895 O OG    . SER B 1 195 ? -3.095 -0.469  -66.923 1.00 23.06 ? 193  SER A OG    1 
ATOM   5896 N N     . GLY B 1 196 ? -0.739 -1.724  -63.188 1.00 24.40 ? 194  GLY A N     1 
ATOM   5897 C CA    . GLY B 1 196 ? -0.302 -2.601  -62.099 1.00 23.25 ? 194  GLY A CA    1 
ATOM   5898 C C     . GLY B 1 196 ? 0.121  -1.816  -60.871 1.00 24.54 ? 194  GLY A C     1 
ATOM   5899 O O     . GLY B 1 196 ? 0.011  -0.582  -60.871 1.00 24.12 ? 194  GLY A O     1 
ATOM   5900 N N     . THR B 1 197 ? 0.580  -2.534  -59.859 1.00 22.47 ? 195  THR A N     1 
ATOM   5901 C CA    . THR B 1 197 ? 1.000  -1.878  -58.601 1.00 25.21 ? 195  THR A CA    1 
ATOM   5902 C C     . THR B 1 197 ? 2.420  -2.317  -58.229 1.00 23.07 ? 195  THR A C     1 
ATOM   5903 O O     . THR B 1 197 ? 2.683  -3.517  -58.207 1.00 21.21 ? 195  THR A O     1 
ATOM   5904 C CB    . THR B 1 197 ? -0.006 -2.116  -57.464 1.00 27.81 ? 195  THR A CB    1 
ATOM   5905 O OG1   . THR B 1 197 ? -1.171 -1.340  -57.734 1.00 33.97 ? 195  THR A OG1   1 
ATOM   5906 C CG2   . THR B 1 197 ? 0.543  -1.747  -56.104 1.00 28.50 ? 195  THR A CG2   1 
ATOM   5907 N N     . LYS B 1 198 ? 3.266  -1.342  -57.936 1.00 21.20 ? 196  LYS A N     1 
ATOM   5908 C CA    . LYS B 1 198 ? 4.646  -1.627  -57.496 1.00 19.66 ? 196  LYS A CA    1 
ATOM   5909 C C     . LYS B 1 198 ? 4.784  -1.112  -56.059 1.00 22.21 ? 196  LYS A C     1 
ATOM   5910 O O     . LYS B 1 198 ? 4.128  -0.123  -55.729 1.00 21.75 ? 196  LYS A O     1 
ATOM   5911 C CB    . LYS B 1 198 ? 5.632  -0.944  -58.442 1.00 20.43 ? 196  LYS A CB    1 
ATOM   5912 C CG    . LYS B 1 198 ? 5.569  -1.383  -59.896 1.00 20.24 ? 196  LYS A CG    1 
ATOM   5913 C CD    . LYS B 1 198 ? 6.089  -2.781  -60.107 1.00 20.11 ? 196  LYS A CD    1 
ATOM   5914 C CE    . LYS B 1 198 ? 6.271  -3.130  -61.566 1.00 19.00 ? 196  LYS A CE    1 
ATOM   5915 N NZ    . LYS B 1 198 ? 6.599  -4.562  -61.744 1.00 20.67 ? 196  LYS A NZ    1 
ATOM   5916 N N     . ILE B 1 199 ? 5.619  -1.760  -55.261 1.00 20.17 ? 197  ILE A N     1 
ATOM   5917 C CA    . ILE B 1 199 ? 5.845  -1.356  -53.846 1.00 21.31 ? 197  ILE A CA    1 
ATOM   5918 C C     . ILE B 1 199 ? 7.346  -1.179  -53.621 1.00 22.19 ? 197  ILE A C     1 
ATOM   5919 O O     . ILE B 1 199 ? 8.132  -1.685  -54.418 1.00 21.39 ? 197  ILE A O     1 
ATOM   5920 C CB    . ILE B 1 199 ? 5.217  -2.343  -52.845 1.00 22.65 ? 197  ILE A CB    1 
ATOM   5921 C CG1   . ILE B 1 199 ? 5.889  -3.718  -52.882 1.00 22.48 ? 197  ILE A CG1   1 
ATOM   5922 C CG2   . ILE B 1 199 ? 3.713  -2.428  -53.078 1.00 22.80 ? 197  ILE A CG2   1 
ATOM   5923 C CD1   . ILE B 1 199 ? 5.610  -4.535  -51.648 1.00 23.69 ? 197  ILE A CD1   1 
ATOM   5924 N N     . PHE B 1 200 ? 7.687  -0.440  -52.574 1.00 22.59 ? 198  PHE A N     1 
ATOM   5925 C CA    . PHE B 1 200 ? 9.066  -0.252  -52.069 1.00 22.86 ? 198  PHE A CA    1 
ATOM   5926 C C     . PHE B 1 200 ? 9.873  0.522   -53.115 1.00 23.28 ? 198  PHE A C     1 
ATOM   5927 O O     . PHE B 1 200 ? 11.121 0.331   -53.200 1.00 23.38 ? 198  PHE A O     1 
ATOM   5928 C CB    . PHE B 1 200 ? 9.716  -1.606  -51.750 1.00 23.27 ? 198  PHE A CB    1 
ATOM   5929 C CG    . PHE B 1 200 ? 9.067  -2.440  -50.669 1.00 23.84 ? 198  PHE A CG    1 
ATOM   5930 C CD1   . PHE B 1 200 ? 8.150  -1.907  -49.773 1.00 24.50 ? 198  PHE A CD1   1 
ATOM   5931 C CD2   . PHE B 1 200 ? 9.421  -3.771  -50.515 1.00 24.33 ? 198  PHE A CD2   1 
ATOM   5932 C CE1   . PHE B 1 200 ? 7.572  -2.692  -48.784 1.00 25.59 ? 198  PHE A CE1   1 
ATOM   5933 C CE2   . PHE B 1 200 ? 8.867  -4.545  -49.501 1.00 25.22 ? 198  PHE A CE2   1 
ATOM   5934 C CZ    . PHE B 1 200 ? 7.941  -4.010  -48.637 1.00 23.81 ? 198  PHE A CZ    1 
ATOM   5935 N N     . ILE B 1 201 ? 9.215  1.410   -53.856 1.00 21.45 ? 199  ILE A N     1 
ATOM   5936 C CA    . ILE B 1 201 ? 9.883  2.158   -54.950 1.00 22.23 ? 199  ILE A CA    1 
ATOM   5937 C C     . ILE B 1 201 ? 10.531 3.397   -54.336 1.00 20.94 ? 199  ILE A C     1 
ATOM   5938 O O     . ILE B 1 201 ? 9.828  4.321   -53.983 1.00 19.79 ? 199  ILE A O     1 
ATOM   5939 C CB    . ILE B 1 201 ? 8.931  2.476   -56.120 1.00 22.58 ? 199  ILE A CB    1 
ATOM   5940 C CG1   . ILE B 1 201 ? 8.215  1.226   -56.640 1.00 23.22 ? 199  ILE A CG1   1 
ATOM   5941 C CG2   . ILE B 1 201 ? 9.681  3.197   -57.208 1.00 23.96 ? 199  ILE A CG2   1 
ATOM   5942 C CD1   . ILE B 1 201 ? 9.097  0.027   -56.858 1.00 23.21 ? 199  ILE A CD1   1 
ATOM   5943 N N     . THR B 1 202 ? 11.850 3.342   -54.158 1.00 21.55 ? 200  THR A N     1 
ATOM   5944 C CA    . THR B 1 202 ? 12.684 4.462   -53.674 1.00 20.48 ? 200  THR A CA    1 
ATOM   5945 C C     . THR B 1 202 ? 12.499 5.616   -54.658 1.00 19.52 ? 200  THR A C     1 
ATOM   5946 O O     . THR B 1 202 ? 12.741 5.432   -55.858 1.00 20.69 ? 200  THR A O     1 
ATOM   5947 C CB    . THR B 1 202 ? 14.158 4.042   -53.546 1.00 20.98 ? 200  THR A CB    1 
ATOM   5948 O OG1   . THR B 1 202 ? 14.213 2.883   -52.729 1.00 21.70 ? 200  THR A OG1   1 
ATOM   5949 C CG2   . THR B 1 202 ? 15.044 5.113   -52.972 1.00 21.94 ? 200  THR A CG2   1 
ATOM   5950 N N     . GLY B 1 203 ? 12.148 6.789   -54.152 1.00 21.48 ? 201  GLY A N     1 
ATOM   5951 C CA    . GLY B 1 203 ? 12.043 7.996   -54.983 1.00 21.49 ? 201  GLY A CA    1 
ATOM   5952 C C     . GLY B 1 203 ? 10.975 7.839   -56.056 1.00 22.06 ? 201  GLY A C     1 
ATOM   5953 O O     . GLY B 1 203 ? 11.087 8.541   -57.089 1.00 21.29 ? 201  GLY A O     1 
ATOM   5954 N N     . GLY B 1 204 ? 9.982  6.952   -55.860 1.00 21.99 ? 202  GLY A N     1 
ATOM   5955 C CA    . GLY B 1 204 ? 8.831  6.830   -56.792 1.00 22.24 ? 202  GLY A CA    1 
ATOM   5956 C C     . GLY B 1 204 ? 8.099  8.156   -56.975 1.00 22.18 ? 202  GLY A C     1 
ATOM   5957 O O     . GLY B 1 204 ? 7.578  8.448   -58.080 1.00 22.71 ? 202  GLY A O     1 
ATOM   5958 N N     . GLU B 1 205 ? 8.087  8.960   -55.921 1.00 24.19 ? 203  GLU A N     1 
ATOM   5959 C CA    . GLU B 1 205 ? 7.474  10.294  -55.902 1.00 23.95 ? 203  GLU A CA    1 
ATOM   5960 C C     . GLU B 1 205 ? 8.203  11.100  -54.836 1.00 23.80 ? 203  GLU A C     1 
ATOM   5961 O O     . GLU B 1 205 ? 8.529  10.532  -53.785 1.00 23.89 ? 203  GLU A O     1 
ATOM   5962 C CB    . GLU B 1 205 ? 5.976  10.127  -55.626 1.00 28.48 ? 203  GLU A CB    1 
ATOM   5963 C CG    . GLU B 1 205 ? 5.235  11.437  -55.571 1.00 32.40 ? 203  GLU A CG    1 
ATOM   5964 C CD    . GLU B 1 205 ? 5.233  12.117  -56.921 1.00 34.97 ? 203  GLU A CD    1 
ATOM   5965 O OE1   . GLU B 1 205 ? 4.376  11.767  -57.782 1.00 43.33 ? 203  GLU A OE1   1 
ATOM   5966 O OE2   . GLU B 1 205 ? 6.128  12.926  -57.137 1.00 34.92 ? 203  GLU A OE2   1 
ATOM   5967 N N     . HIS B 1 206 ? 8.469  12.366  -55.127 1.00 23.59 ? 204  HIS A N     1 
ATOM   5968 C CA    . HIS B 1 206 ? 9.193  13.304  -54.241 1.00 25.78 ? 204  HIS A CA    1 
ATOM   5969 C C     . HIS B 1 206 ? 9.075  14.699  -54.844 1.00 25.60 ? 204  HIS A C     1 
ATOM   5970 O O     . HIS B 1 206 ? 8.441  14.826  -55.906 1.00 27.48 ? 204  HIS A O     1 
ATOM   5971 C CB    . HIS B 1 206 ? 10.664 12.897  -54.069 1.00 24.02 ? 204  HIS A CB    1 
ATOM   5972 C CG    . HIS B 1 206 ? 11.387 12.722  -55.364 1.00 23.63 ? 204  HIS A CG    1 
ATOM   5973 N ND1   . HIS B 1 206 ? 11.697 13.792  -56.179 1.00 22.84 ? 204  HIS A ND1   1 
ATOM   5974 C CD2   . HIS B 1 206 ? 11.858 11.610  -55.985 1.00 23.22 ? 204  HIS A CD2   1 
ATOM   5975 C CE1   . HIS B 1 206 ? 12.337 13.356  -57.244 1.00 23.24 ? 204  HIS A CE1   1 
ATOM   5976 N NE2   . HIS B 1 206 ? 12.443 12.003  -57.166 1.00 22.73 ? 204  HIS A NE2   1 
ATOM   5977 N N     . ASP B 1 207 ? 9.711  15.674  -54.210 1.00 27.08 ? 205  ASP A N     1 
ATOM   5978 C CA    . ASP B 1 207 ? 9.666  17.099  -54.626 1.00 27.01 ? 205  ASP A CA    1 
ATOM   5979 C C     . ASP B 1 207 ? 11.073 17.584  -55.001 1.00 28.28 ? 205  ASP A C     1 
ATOM   5980 O O     . ASP B 1 207 ? 11.295 18.804  -54.940 1.00 25.92 ? 205  ASP A O     1 
ATOM   5981 C CB    . ASP B 1 207 ? 9.051  17.937  -53.494 1.00 29.21 ? 205  ASP A CB    1 
ATOM   5982 C CG    . ASP B 1 207 ? 9.789  17.747  -52.174 1.00 28.12 ? 205  ASP A CG    1 
ATOM   5983 O OD1   . ASP B 1 207 ? 10.726 16.912  -52.133 1.00 29.91 ? 205  ASP A OD1   1 
ATOM   5984 O OD2   . ASP B 1 207 ? 9.442  18.427  -51.202 1.00 29.72 ? 205  ASP A OD2   1 
ATOM   5985 N N     . LEU B 1 208 ? 11.995 16.701  -55.410 1.00 25.05 ? 206  LEU A N     1 
ATOM   5986 C CA    . LEU B 1 208 ? 13.370 17.143  -55.757 1.00 25.20 ? 206  LEU A CA    1 
ATOM   5987 C C     . LEU B 1 208 ? 13.477 17.593  -57.220 1.00 25.57 ? 206  LEU A C     1 
ATOM   5988 O O     . LEU B 1 208 ? 14.415 18.363  -57.514 1.00 25.99 ? 206  LEU A O     1 
ATOM   5989 C CB    . LEU B 1 208 ? 14.348 16.007  -55.477 1.00 25.30 ? 206  LEU A CB    1 
ATOM   5990 C CG    . LEU B 1 208 ? 14.286 15.454  -54.057 1.00 26.03 ? 206  LEU A CG    1 
ATOM   5991 C CD1   . LEU B 1 208 ? 15.219 14.248  -53.912 1.00 26.32 ? 206  LEU A CD1   1 
ATOM   5992 C CD2   . LEU B 1 208 ? 14.629 16.544  -53.058 1.00 25.69 ? 206  LEU A CD2   1 
ATOM   5993 N N     . THR B 1 209 ? 12.640 17.066  -58.114 1.00 25.11 ? 207  THR A N     1 
ATOM   5994 C CA    . THR B 1 209 ? 12.745 17.272  -59.581 1.00 24.94 ? 207  THR A CA    1 
ATOM   5995 C C     . THR B 1 209 ? 11.347 17.482  -60.158 1.00 27.41 ? 207  THR A C     1 
ATOM   5996 O O     . THR B 1 209 ? 10.394 16.950  -59.566 1.00 25.23 ? 207  THR A O     1 
ATOM   5997 C CB    . THR B 1 209 ? 13.451 16.095  -60.275 1.00 27.94 ? 207  THR A CB    1 
ATOM   5998 O OG1   . THR B 1 209 ? 12.729 14.882  -60.063 1.00 26.79 ? 207  THR A OG1   1 
ATOM   5999 C CG2   . THR B 1 209 ? 14.869 15.905  -59.780 1.00 27.70 ? 207  THR A CG2   1 
ATOM   6000 N N     . GLU B 1 210 ? 11.257 18.184  -61.287 1.00 26.69 ? 208  GLU A N     1 
ATOM   6001 C CA    . GLU B 1 210 ? 9.983  18.466  -62.002 1.00 28.74 ? 208  GLU A CA    1 
ATOM   6002 C C     . GLU B 1 210 ? 9.452  17.195  -62.687 1.00 28.75 ? 208  GLU A C     1 
ATOM   6003 O O     . GLU B 1 210 ? 8.261  17.142  -63.049 1.00 27.79 ? 208  GLU A O     1 
ATOM   6004 C CB    . GLU B 1 210 ? 10.207 19.604  -62.992 1.00 29.66 ? 208  GLU A CB    1 
ATOM   6005 C CG    . GLU B 1 210 ? 11.059 19.210  -64.200 1.00 32.03 ? 208  GLU A CG    1 
ATOM   6006 C CD    . GLU B 1 210 ? 11.184 20.263  -65.295 1.00 32.01 ? 208  GLU A CD    1 
ATOM   6007 O OE1   . GLU B 1 210 ? 11.593 19.909  -66.431 1.00 26.32 ? 208  GLU A OE1   1 
ATOM   6008 O OE2   . GLU B 1 210 ? 10.876 21.432  -65.009 1.00 35.79 ? 208  GLU A OE2   1 
ATOM   6009 N N     . ASN B 1 211 ? 10.280 16.182  -62.871 1.00 26.97 ? 209  ASN A N     1 
ATOM   6010 C CA    . ASN B 1 211 ? 9.818  14.933  -63.522 1.00 26.56 ? 209  ASN A CA    1 
ATOM   6011 C C     . ASN B 1 211 ? 10.626 13.765  -62.979 1.00 24.91 ? 209  ASN A C     1 
ATOM   6012 O O     . ASN B 1 211 ? 11.718 13.987  -62.471 1.00 24.27 ? 209  ASN A O     1 
ATOM   6013 C CB    . ASN B 1 211 ? 9.916  15.006  -65.049 1.00 26.45 ? 209  ASN A CB    1 
ATOM   6014 C CG    . ASN B 1 211 ? 8.923  14.121  -65.773 1.00 26.87 ? 209  ASN A CG    1 
ATOM   6015 O OD1   . ASN B 1 211 ? 8.191  13.346  -65.163 1.00 26.51 ? 209  ASN A OD1   1 
ATOM   6016 N ND2   . ASN B 1 211 ? 8.903  14.219  -67.095 1.00 27.76 ? 209  ASN A ND2   1 
ATOM   6017 N N     . ILE B 1 212 ? 10.074 12.565  -63.113 1.00 25.78 ? 210  ILE A N     1 
ATOM   6018 C CA    . ILE B 1 212 ? 10.686 11.297  -62.640 1.00 24.92 ? 210  ILE A CA    1 
ATOM   6019 C C     . ILE B 1 212 ? 10.450 10.291  -63.750 1.00 24.10 ? 210  ILE A C     1 
ATOM   6020 O O     . ILE B 1 212 ? 9.289  10.159  -64.182 1.00 23.15 ? 210  ILE A O     1 
ATOM   6021 C CB    . ILE B 1 212 ? 10.071 10.811  -61.314 1.00 25.71 ? 210  ILE A CB    1 
ATOM   6022 C CG1   . ILE B 1 212 ? 10.173 11.854  -60.197 1.00 25.75 ? 210  ILE A CG1   1 
ATOM   6023 C CG2   . ILE B 1 212 ? 10.707 9.483   -60.939 1.00 26.70 ? 210  ILE A CG2   1 
ATOM   6024 C CD1   . ILE B 1 212 ? 9.488  11.477  -58.904 1.00 23.89 ? 210  ILE A CD1   1 
ATOM   6025 N N     . ILE B 1 213 ? 11.518 9.676   -64.230 1.00 22.42 ? 211  ILE A N     1 
ATOM   6026 C CA    . ILE B 1 213 ? 11.467 8.734   -65.367 1.00 23.28 ? 211  ILE A CA    1 
ATOM   6027 C C     . ILE B 1 213 ? 11.537 7.323   -64.775 1.00 23.45 ? 211  ILE A C     1 
ATOM   6028 O O     . ILE B 1 213 ? 12.614 6.908   -64.336 1.00 22.96 ? 211  ILE A O     1 
ATOM   6029 C CB    . ILE B 1 213 ? 12.595 9.048   -66.362 1.00 24.33 ? 211  ILE A CB    1 
ATOM   6030 C CG1   . ILE B 1 213 ? 12.624 10.528  -66.777 1.00 26.39 ? 211  ILE A CG1   1 
ATOM   6031 C CG2   . ILE B 1 213 ? 12.480 8.164   -67.567 1.00 22.85 ? 211  ILE A CG2   1 
ATOM   6032 C CD1   . ILE B 1 213 ? 11.291 11.066  -67.276 1.00 25.93 ? 211  ILE A CD1   1 
ATOM   6033 N N     . HIS B 1 214 ? 10.410 6.621   -64.740 1.00 23.60 ? 212  HIS A N     1 
ATOM   6034 C CA    . HIS B 1 214 ? 10.302 5.298   -64.081 1.00 23.01 ? 212  HIS A CA    1 
ATOM   6035 C C     . HIS B 1 214 ? 10.751 4.260   -65.072 1.00 21.33 ? 212  HIS A C     1 
ATOM   6036 O O     . HIS B 1 214 ? 10.290 4.319   -66.226 1.00 22.54 ? 212  HIS A O     1 
ATOM   6037 C CB    . HIS B 1 214 ? 8.880  5.005   -63.594 1.00 22.83 ? 212  HIS A CB    1 
ATOM   6038 C CG    . HIS B 1 214 ? 8.381  6.010   -62.629 1.00 24.18 ? 212  HIS A CG    1 
ATOM   6039 N ND1   . HIS B 1 214 ? 7.389  6.933   -62.948 1.00 27.01 ? 212  HIS A ND1   1 
ATOM   6040 C CD2   . HIS B 1 214 ? 8.723  6.246   -61.351 1.00 24.16 ? 212  HIS A CD2   1 
ATOM   6041 C CE1   . HIS B 1 214 ? 7.145  7.682   -61.888 1.00 22.77 ? 212  HIS A CE1   1 
ATOM   6042 N NE2   . HIS B 1 214 ? 7.952  7.273   -60.899 1.00 26.66 ? 212  HIS A NE2   1 
ATOM   6043 N N     . LEU B 1 215 ? 11.634 3.366   -64.656 1.00 22.57 ? 213  LEU A N     1 
ATOM   6044 C CA    . LEU B 1 215 ? 11.864 2.114   -65.422 1.00 23.38 ? 213  LEU A CA    1 
ATOM   6045 C C     . LEU B 1 215 ? 11.018 1.007   -64.794 1.00 24.00 ? 213  LEU A C     1 
ATOM   6046 O O     . LEU B 1 215 ? 11.318 0.585   -63.667 1.00 21.46 ? 213  LEU A O     1 
ATOM   6047 C CB    . LEU B 1 215 ? 13.348 1.770   -65.436 1.00 23.31 ? 213  LEU A CB    1 
ATOM   6048 C CG    . LEU B 1 215 ? 14.258 2.833   -66.055 1.00 26.67 ? 213  LEU A CG    1 
ATOM   6049 C CD1   . LEU B 1 215 ? 15.680 2.320   -66.137 1.00 28.63 ? 213  LEU A CD1   1 
ATOM   6050 C CD2   . LEU B 1 215 ? 13.789 3.243   -67.441 1.00 30.54 ? 213  LEU A CD2   1 
ATOM   6051 N N     . VAL B 1 216 ? 9.972  0.595   -65.506 1.00 23.24 ? 214  VAL A N     1 
ATOM   6052 C CA    . VAL B 1 216 ? 8.919  -0.306  -64.983 1.00 21.51 ? 214  VAL A CA    1 
ATOM   6053 C C     . VAL B 1 216 ? 9.024  -1.688  -65.612 1.00 20.76 ? 214  VAL A C     1 
ATOM   6054 O O     . VAL B 1 216 ? 9.011  -1.767  -66.859 1.00 21.77 ? 214  VAL A O     1 
ATOM   6055 C CB    . VAL B 1 216 ? 7.539  0.305   -65.235 1.00 20.66 ? 214  VAL A CB    1 
ATOM   6056 C CG1   . VAL B 1 216 ? 6.492  -0.510  -64.515 1.00 20.38 ? 214  VAL A CG1   1 
ATOM   6057 C CG2   . VAL B 1 216 ? 7.494  1.746   -64.766 1.00 21.62 ? 214  VAL A CG2   1 
ATOM   6058 N N     . LEU B 1 217 ? 9.105  -2.735  -64.789 1.00 21.04 ? 215  LEU A N     1 
ATOM   6059 C CA    . LEU B 1 217 ? 9.077  -4.138  -65.284 1.00 21.41 ? 215  LEU A CA    1 
ATOM   6060 C C     . LEU B 1 217 ? 7.608  -4.526  -65.421 1.00 21.53 ? 215  LEU A C     1 
ATOM   6061 O O     . LEU B 1 217 ? 6.833  -4.308  -64.472 1.00 20.11 ? 215  LEU A O     1 
ATOM   6062 C CB    . LEU B 1 217 ? 9.776  -5.119  -64.340 1.00 23.63 ? 215  LEU A CB    1 
ATOM   6063 C CG    . LEU B 1 217 ? 11.294 -5.240  -64.378 1.00 30.02 ? 215  LEU A CG    1 
ATOM   6064 C CD1   . LEU B 1 217 ? 11.717 -6.424  -63.494 1.00 32.54 ? 215  LEU A CD1   1 
ATOM   6065 C CD2   . LEU B 1 217 ? 11.843 -5.396  -65.778 1.00 27.84 ? 215  LEU A CD2   1 
ATOM   6066 N N     . ALA B 1 218 ? 7.272  -5.019  -66.604 1.00 21.11 ? 216  ALA A N     1 
ATOM   6067 C CA    . ALA B 1 218 ? 5.883  -5.391  -66.900 1.00 21.54 ? 216  ALA A CA    1 
ATOM   6068 C C     . ALA B 1 218 ? 5.905  -6.496  -67.953 1.00 22.22 ? 216  ALA A C     1 
ATOM   6069 O O     . ALA B 1 218 ? 6.961  -6.739  -68.538 1.00 21.79 ? 216  ALA A O     1 
ATOM   6070 C CB    . ALA B 1 218 ? 5.137  -4.175  -67.391 1.00 21.23 ? 216  ALA A CB    1 
ATOM   6071 N N     . LYS B 1 219 ? 4.750  -7.100  -68.183 1.00 22.04 ? 217  LYS A N     1 
ATOM   6072 C CA    . LYS B 1 219 ? 4.659  -8.167  -69.189 1.00 20.95 ? 217  LYS A CA    1 
ATOM   6073 C C     . LYS B 1 219 ? 3.571  -7.831  -70.206 1.00 22.26 ? 217  LYS A C     1 
ATOM   6074 O O     . LYS B 1 219 ? 2.515  -7.345  -69.799 1.00 22.77 ? 217  LYS A O     1 
ATOM   6075 C CB    . LYS B 1 219 ? 4.345  -9.503  -68.517 1.00 22.46 ? 217  LYS A CB    1 
ATOM   6076 C CG    . LYS B 1 219 ? 5.421  -10.086 -67.615 1.00 24.21 ? 217  LYS A CG    1 
ATOM   6077 C CD    . LYS B 1 219 ? 5.112  -11.517 -67.228 1.00 24.92 ? 217  LYS A CD    1 
ATOM   6078 C CE    . LYS B 1 219 ? 6.306  -12.287 -66.709 1.00 25.07 ? 217  LYS A CE    1 
ATOM   6079 N NZ    . LYS B 1 219 ? 6.012  -13.735 -66.596 1.00 25.59 ? 217  LYS A NZ    1 
ATOM   6080 N N     . LEU B 1 220 ? 3.860  -8.052  -71.481 1.00 20.36 ? 218  LEU A N     1 
ATOM   6081 C CA    . LEU B 1 220 ? 2.800  -7.906  -72.498 1.00 23.09 ? 218  LEU A CA    1 
ATOM   6082 C C     . LEU B 1 220 ? 1.736  -8.964  -72.191 1.00 24.29 ? 218  LEU A C     1 
ATOM   6083 O O     . LEU B 1 220 ? 2.067  -9.957  -71.556 1.00 24.13 ? 218  LEU A O     1 
ATOM   6084 C CB    . LEU B 1 220 ? 3.382  -8.110  -73.899 1.00 23.86 ? 218  LEU A CB    1 
ATOM   6085 C CG    . LEU B 1 220 ? 3.921  -6.856  -74.581 1.00 27.17 ? 218  LEU A CG    1 
ATOM   6086 C CD1   . LEU B 1 220 ? 5.049  -6.244  -73.770 1.00 26.94 ? 218  LEU A CD1   1 
ATOM   6087 C CD2   . LEU B 1 220 ? 4.397  -7.181  -75.986 1.00 28.84 ? 218  LEU A CD2   1 
ATOM   6088 N N     . PRO B 1 221 ? 0.490  -8.785  -72.657 1.00 24.12 ? 219  PRO A N     1 
ATOM   6089 C CA    . PRO B 1 221 ? -0.585 -9.714  -72.334 1.00 24.00 ? 219  PRO A CA    1 
ATOM   6090 C C     . PRO B 1 221 ? -0.340 -11.136 -72.848 1.00 25.56 ? 219  PRO A C     1 
ATOM   6091 O O     . PRO B 1 221 ? -0.897 -12.036 -72.308 1.00 24.57 ? 219  PRO A O     1 
ATOM   6092 C CB    . PRO B 1 221 ? -1.764 -9.137  -73.118 1.00 27.98 ? 219  PRO A CB    1 
ATOM   6093 C CG    . PRO B 1 221 ? -1.432 -7.683  -73.326 1.00 28.76 ? 219  PRO A CG    1 
ATOM   6094 C CD    . PRO B 1 221 ? 0.068  -7.665  -73.491 1.00 26.07 ? 219  PRO A CD    1 
ATOM   6095 N N     . ASP B 1 222 ? 0.485  -11.261 -73.879 1.00 24.74 ? 220  ASP A N     1 
ATOM   6096 C CA    . ASP B 1 222 ? 0.747  -12.577 -74.507 1.00 27.97 ? 220  ASP A CA    1 
ATOM   6097 C C     . ASP B 1 222 ? 2.113  -13.095 -74.060 1.00 27.81 ? 220  ASP A C     1 
ATOM   6098 O O     . ASP B 1 222 ? 2.622  -14.023 -74.690 1.00 26.23 ? 220  ASP A O     1 
ATOM   6099 C CB    . ASP B 1 222 ? 0.640  -12.465 -76.029 1.00 29.92 ? 220  ASP A CB    1 
ATOM   6100 C CG    . ASP B 1 222 ? 1.575  -11.445 -76.654 1.00 32.27 ? 220  ASP A CG    1 
ATOM   6101 O OD1   . ASP B 1 222 ? 2.169  -10.650 -75.913 1.00 30.78 ? 220  ASP A OD1   1 
ATOM   6102 O OD2   . ASP B 1 222 ? 1.696  -11.461 -77.883 1.00 35.27 ? 220  ASP A OD2   1 
ATOM   6103 N N     . ALA B 1 223 ? 2.656  -12.518 -72.995 1.00 28.51 ? 221  ALA A N     1 
ATOM   6104 C CA    . ALA B 1 223 ? 4.013  -12.877 -72.549 1.00 27.40 ? 221  ALA A CA    1 
ATOM   6105 C C     . ALA B 1 223 ? 4.051  -14.283 -71.967 1.00 28.35 ? 221  ALA A C     1 
ATOM   6106 O O     . ALA B 1 223 ? 3.048  -14.726 -71.417 1.00 27.67 ? 221  ALA A O     1 
ATOM   6107 C CB    . ALA B 1 223 ? 4.483  -11.887 -71.528 1.00 28.27 ? 221  ALA A CB    1 
ATOM   6108 N N     . PRO B 1 224 ? 5.194  -14.979 -72.074 1.00 26.52 ? 222  PRO A N     1 
ATOM   6109 C CA    . PRO B 1 224 ? 5.338  -16.262 -71.432 1.00 27.91 ? 222  PRO A CA    1 
ATOM   6110 C C     . PRO B 1 224 ? 5.376  -16.097 -69.906 1.00 26.84 ? 222  PRO A C     1 
ATOM   6111 O O     . PRO B 1 224 ? 5.608  -15.022 -69.427 1.00 25.01 ? 222  PRO A O     1 
ATOM   6112 C CB    . PRO B 1 224 ? 6.717  -16.745 -71.902 1.00 30.31 ? 222  PRO A CB    1 
ATOM   6113 C CG    . PRO B 1 224 ? 7.043  -15.908 -73.113 1.00 31.24 ? 222  PRO A CG    1 
ATOM   6114 C CD    . PRO B 1 224 ? 6.363  -14.585 -72.853 1.00 29.08 ? 222  PRO A CD    1 
ATOM   6115 N N     . ALA B 1 225 ? 5.139  -17.188 -69.193 1.00 25.88 ? 223  ALA A N     1 
ATOM   6116 C CA    . ALA B 1 225 ? 5.247  -17.162 -67.726 1.00 27.50 ? 223  ALA A CA    1 
ATOM   6117 C C     . ALA B 1 225 ? 6.720  -17.106 -67.325 1.00 27.14 ? 223  ALA A C     1 
ATOM   6118 O O     . ALA B 1 225 ? 7.570  -17.465 -68.140 1.00 27.47 ? 223  ALA A O     1 
ATOM   6119 C CB    . ALA B 1 225 ? 4.574  -18.377 -67.156 1.00 32.43 ? 223  ALA A CB    1 
ATOM   6120 N N     . GLY B 1 226 ? 6.985  -16.663 -66.102 1.00 25.92 ? 224  GLY A N     1 
ATOM   6121 C CA    . GLY B 1 226 ? 8.355  -16.615 -65.588 1.00 25.94 ? 224  GLY A CA    1 
ATOM   6122 C C     . GLY B 1 226 ? 9.194  -15.474 -66.172 1.00 25.91 ? 224  GLY A C     1 
ATOM   6123 O O     . GLY B 1 226 ? 8.696  -14.578 -66.864 1.00 25.40 ? 224  GLY A O     1 
ATOM   6124 N N     . PRO B 1 227 ? 10.497 -15.489 -65.840 1.00 26.17 ? 225  PRO A N     1 
ATOM   6125 C CA    . PRO B 1 227 ? 11.407 -14.374 -66.105 1.00 28.55 ? 225  PRO A CA    1 
ATOM   6126 C C     . PRO B 1 227 ? 11.657 -14.107 -67.602 1.00 28.71 ? 225  PRO A C     1 
ATOM   6127 O O     . PRO B 1 227 ? 11.967 -12.986 -67.968 1.00 25.67 ? 225  PRO A O     1 
ATOM   6128 C CB    . PRO B 1 227 ? 12.694 -14.792 -65.371 1.00 29.40 ? 225  PRO A CB    1 
ATOM   6129 C CG    . PRO B 1 227 ? 12.635 -16.303 -65.332 1.00 29.95 ? 225  PRO A CG    1 
ATOM   6130 C CD    . PRO B 1 227 ? 11.164 -16.607 -65.138 1.00 29.65 ? 225  PRO A CD    1 
ATOM   6131 N N     . LYS B 1 228 ? 11.388 -15.094 -68.448 1.00 27.49 ? 226  LYS A N     1 
ATOM   6132 C CA    . LYS B 1 228 ? 11.568 -14.967 -69.908 1.00 30.00 ? 226  LYS A CA    1 
ATOM   6133 C C     . LYS B 1 228 ? 10.354 -14.293 -70.546 1.00 26.49 ? 226  LYS A C     1 
ATOM   6134 O O     . LYS B 1 228 ? 10.309 -14.240 -71.769 1.00 28.70 ? 226  LYS A O     1 
ATOM   6135 C CB    . LYS B 1 228 ? 11.792 -16.353 -70.494 1.00 37.30 ? 226  LYS A CB    1 
ATOM   6136 C CG    . LYS B 1 228 ? 12.901 -17.129 -69.813 1.00 44.95 ? 226  LYS A CG    1 
ATOM   6137 C CD    . LYS B 1 228 ? 12.991 -18.536 -70.330 1.00 51.86 ? 226  LYS A CD    1 
ATOM   6138 C CE    . LYS B 1 228 ? 13.768 -18.589 -71.623 1.00 56.40 ? 226  LYS A CE    1 
ATOM   6139 N NZ    . LYS B 1 228 ? 15.176 -18.175 -71.405 1.00 64.94 ? 226  LYS A NZ    1 
ATOM   6140 N N     . GLY B 1 229 ? 9.399  -13.820 -69.742 1.00 23.28 ? 227  GLY A N     1 
ATOM   6141 C CA    . GLY B 1 229 ? 8.253  -13.028 -70.207 1.00 22.43 ? 227  GLY A CA    1 
ATOM   6142 C C     . GLY B 1 229 ? 8.385  -11.571 -69.814 1.00 20.94 ? 227  GLY A C     1 
ATOM   6143 O O     . GLY B 1 229 ? 7.465  -10.797 -70.095 1.00 22.57 ? 227  GLY A O     1 
ATOM   6144 N N     . ILE B 1 230 ? 9.470  -11.200 -69.157 1.00 22.38 ? 228  ILE A N     1 
ATOM   6145 C CA    . ILE B 1 230 ? 9.589  -9.842  -68.554 1.00 21.89 ? 228  ILE A CA    1 
ATOM   6146 C C     . ILE B 1 230 ? 10.104 -8.843  -69.592 1.00 21.67 ? 228  ILE A C     1 
ATOM   6147 O O     . ILE B 1 230 ? 11.084 -9.152  -70.319 1.00 21.03 ? 228  ILE A O     1 
ATOM   6148 C CB    . ILE B 1 230 ? 10.488 -9.883  -67.313 1.00 22.53 ? 228  ILE A CB    1 
ATOM   6149 C CG1   . ILE B 1 230 ? 9.856  -10.712 -66.196 1.00 24.73 ? 228  ILE A CG1   1 
ATOM   6150 C CG2   . ILE B 1 230 ? 10.807 -8.467  -66.849 1.00 23.19 ? 228  ILE A CG2   1 
ATOM   6151 C CD1   . ILE B 1 230 ? 10.813 -11.015 -65.089 1.00 27.98 ? 228  ILE A CD1   1 
ATOM   6152 N N     . SER B 1 231 ? 9.500  -7.657  -69.604 1.00 22.35 ? 229  SER A N     1 
ATOM   6153 C CA    . SER B 1 231 ? 9.923  -6.518  -70.447 1.00 21.52 ? 229  SER A CA    1 
ATOM   6154 C C     . SER B 1 231 ? 10.104 -5.281  -69.562 1.00 21.41 ? 229  SER A C     1 
ATOM   6155 O O     . SER B 1 231 ? 9.564  -5.244  -68.415 1.00 21.71 ? 229  SER A O     1 
ATOM   6156 C CB    . SER B 1 231 ? 8.939  -6.275  -71.602 1.00 21.40 ? 229  SER A CB    1 
ATOM   6157 O OG    . SER B 1 231 ? 8.786  -7.452  -72.394 1.00 23.69 ? 229  SER A OG    1 
ATOM   6158 N N     . LEU B 1 232 ? 10.818 -4.294  -70.085 1.00 20.85 ? 230  LEU A N     1 
ATOM   6159 C CA    . LEU B 1 232 ? 11.150 -3.048  -69.357 1.00 21.64 ? 230  LEU A CA    1 
ATOM   6160 C C     . LEU B 1 232 ? 10.617 -1.863  -70.136 1.00 21.63 ? 230  LEU A C     1 
ATOM   6161 O O     . LEU B 1 232 ? 10.808 -1.821  -71.367 1.00 21.28 ? 230  LEU A O     1 
ATOM   6162 C CB    . LEU B 1 232 ? 12.671 -2.953  -69.210 1.00 21.98 ? 230  LEU A CB    1 
ATOM   6163 C CG    . LEU B 1 232 ? 13.173 -1.748  -68.419 1.00 23.04 ? 230  LEU A CG    1 
ATOM   6164 C CD1   . LEU B 1 232 ? 12.688 -1.785  -66.990 1.00 23.89 ? 230  LEU A CD1   1 
ATOM   6165 C CD2   . LEU B 1 232 ? 14.700 -1.657  -68.475 1.00 23.60 ? 230  LEU A CD2   1 
ATOM   6166 N N     . PHE B 1 233 ? 10.028 -0.906  -69.417 1.00 21.50 ? 231  PHE A N     1 
ATOM   6167 C CA    . PHE B 1 233 ? 9.360  0.268   -70.001 1.00 20.73 ? 231  PHE A CA    1 
ATOM   6168 C C     . PHE B 1 233 ? 9.866  1.539   -69.338 1.00 21.05 ? 231  PHE A C     1 
ATOM   6169 O O     . PHE B 1 233 ? 10.076 1.545   -68.128 1.00 22.84 ? 231  PHE A O     1 
ATOM   6170 C CB    . PHE B 1 233 ? 7.847  0.112   -69.894 1.00 21.05 ? 231  PHE A CB    1 
ATOM   6171 C CG    . PHE B 1 233 ? 7.378  -1.121  -70.608 1.00 21.23 ? 231  PHE A CG    1 
ATOM   6172 C CD1   . PHE B 1 233 ? 7.338  -2.342  -69.953 1.00 19.45 ? 231  PHE A CD1   1 
ATOM   6173 C CD2   . PHE B 1 233 ? 7.092  -1.082  -71.968 1.00 21.39 ? 231  PHE A CD2   1 
ATOM   6174 C CE1   . PHE B 1 233 ? 6.968  -3.488  -70.635 1.00 19.02 ? 231  PHE A CE1   1 
ATOM   6175 C CE2   . PHE B 1 233 ? 6.738  -2.239  -72.648 1.00 20.52 ? 231  PHE A CE2   1 
ATOM   6176 C CZ    . PHE B 1 233 ? 6.707  -3.445  -71.983 1.00 19.26 ? 231  PHE A CZ    1 
ATOM   6177 N N     . LEU B 1 234 ? 10.008 2.579   -70.151 1.00 22.60 ? 232  LEU A N     1 
ATOM   6178 C CA    . LEU B 1 234 ? 10.219 3.969   -69.699 1.00 21.95 ? 232  LEU A CA    1 
ATOM   6179 C C     . LEU B 1 234 ? 8.848  4.627   -69.554 1.00 21.42 ? 232  LEU A C     1 
ATOM   6180 O O     . LEU B 1 234 ? 8.131  4.753   -70.563 1.00 20.72 ? 232  LEU A O     1 
ATOM   6181 C CB    . LEU B 1 234 ? 11.129 4.663   -70.704 1.00 21.79 ? 232  LEU A CB    1 
ATOM   6182 C CG    . LEU B 1 234 ? 11.595 6.056   -70.295 1.00 23.48 ? 232  LEU A CG    1 
ATOM   6183 C CD1   . LEU B 1 234 ? 12.814 6.480   -71.113 1.00 24.20 ? 232  LEU A CD1   1 
ATOM   6184 C CD2   . LEU B 1 234 ? 10.458 7.061   -70.441 1.00 23.04 ? 232  LEU A CD2   1 
ATOM   6185 N N     . VAL B 1 235 ? 8.483  4.986   -68.333 1.00 20.67 ? 233  VAL A N     1 
ATOM   6186 C CA    . VAL B 1 235 ? 7.144  5.542   -67.993 1.00 22.80 ? 233  VAL A CA    1 
ATOM   6187 C C     . VAL B 1 235 ? 7.348  6.833   -67.214 1.00 23.69 ? 233  VAL A C     1 
ATOM   6188 O O     . VAL B 1 235 ? 7.679  6.814   -66.028 1.00 23.89 ? 233  VAL A O     1 
ATOM   6189 C CB    . VAL B 1 235 ? 6.308  4.545   -67.175 1.00 23.35 ? 233  VAL A CB    1 
ATOM   6190 C CG1   . VAL B 1 235 ? 4.916  5.075   -66.910 1.00 23.77 ? 233  VAL A CG1   1 
ATOM   6191 C CG2   . VAL B 1 235 ? 6.260  3.170   -67.823 1.00 24.15 ? 233  VAL A CG2   1 
ATOM   6192 N N     . PRO B 1 236 ? 7.217  8.000   -67.867 1.00 24.88 ? 234  PRO A N     1 
ATOM   6193 C CA    . PRO B 1 236 ? 7.423  9.269   -67.180 1.00 25.53 ? 234  PRO A CA    1 
ATOM   6194 C C     . PRO B 1 236 ? 6.264  9.662   -66.263 1.00 25.37 ? 234  PRO A C     1 
ATOM   6195 O O     . PRO B 1 236 ? 5.121  9.350   -66.552 1.00 23.57 ? 234  PRO A O     1 
ATOM   6196 C CB    . PRO B 1 236 ? 7.576  10.277  -68.321 1.00 27.28 ? 234  PRO A CB    1 
ATOM   6197 C CG    . PRO B 1 236 ? 6.846  9.660   -69.479 1.00 29.36 ? 234  PRO A CG    1 
ATOM   6198 C CD    . PRO B 1 236 ? 6.932  8.156   -69.302 1.00 27.25 ? 234  PRO A CD    1 
ATOM   6199 N N     . LYS B 1 237 ? 6.595  10.323  -65.159 1.00 24.84 ? 235  LYS A N     1 
ATOM   6200 C CA    . LYS B 1 237 ? 5.583  10.839  -64.218 1.00 28.19 ? 235  LYS A CA    1 
ATOM   6201 C C     . LYS B 1 237 ? 4.735  11.867  -64.984 1.00 27.77 ? 235  LYS A C     1 
ATOM   6202 O O     . LYS B 1 237 ? 3.491  11.874  -64.843 1.00 26.95 ? 235  LYS A O     1 
ATOM   6203 C CB    . LYS B 1 237 ? 6.283  11.459  -63.009 1.00 28.31 ? 235  LYS A CB    1 
ATOM   6204 C CG    . LYS B 1 237 ? 5.369  12.266  -62.109 1.00 28.20 ? 235  LYS A CG    1 
ATOM   6205 C CD    . LYS B 1 237 ? 6.079  12.970  -60.985 1.00 28.88 ? 235  LYS A CD    1 
ATOM   6206 C CE    . LYS B 1 237 ? 5.258  14.132  -60.459 1.00 29.24 ? 235  LYS A CE    1 
ATOM   6207 N NZ    . LYS B 1 237 ? 5.867  14.696  -59.238 1.00 28.44 ? 235  LYS A NZ    1 
ATOM   6208 N N     . VAL B 1 238 ? 5.425  12.697  -65.757 1.00 26.74 ? 236  VAL A N     1 
ATOM   6209 C CA    . VAL B 1 238 ? 4.833  13.775  -66.581 1.00 26.77 ? 236  VAL A CA    1 
ATOM   6210 C C     . VAL B 1 238 ? 5.246  13.532  -68.023 1.00 27.04 ? 236  VAL A C     1 
ATOM   6211 O O     . VAL B 1 238 ? 6.453  13.442  -68.317 1.00 26.76 ? 236  VAL A O     1 
ATOM   6212 C CB    . VAL B 1 238 ? 5.234  15.180  -66.109 1.00 29.35 ? 236  VAL A CB    1 
ATOM   6213 C CG1   . VAL B 1 238 ? 4.438  16.236  -66.865 1.00 31.36 ? 236  VAL A CG1   1 
ATOM   6214 C CG2   . VAL B 1 238 ? 5.066  15.337  -64.612 1.00 29.30 ? 236  VAL A CG2   1 
ATOM   6215 N N     . LEU B 1 239 ? 4.249  13.389  -68.891 1.00 25.10 ? 237  LEU A N     1 
ATOM   6216 C CA    . LEU B 1 239 ? 4.509  13.218  -70.330 1.00 28.19 ? 237  LEU A CA    1 
ATOM   6217 C C     . LEU B 1 239 ? 5.168  14.499  -70.830 1.00 28.89 ? 237  LEU A C     1 
ATOM   6218 O O     . LEU B 1 239 ? 4.932  15.570  -70.256 1.00 31.26 ? 237  LEU A O     1 
ATOM   6219 C CB    . LEU B 1 239 ? 3.207  12.900  -71.062 1.00 29.25 ? 237  LEU A CB    1 
ATOM   6220 C CG    . LEU B 1 239 ? 2.528  11.620  -70.592 1.00 30.58 ? 237  LEU A CG    1 
ATOM   6221 C CD1   . LEU B 1 239 ? 1.123  11.535  -71.146 1.00 36.03 ? 237  LEU A CD1   1 
ATOM   6222 C CD2   . LEU B 1 239 ? 3.336  10.401  -71.006 1.00 30.24 ? 237  LEU A CD2   1 
ATOM   6223 N N     . VAL B 1 240 ? 6.038  14.342  -71.804 1.00 30.58 ? 238  VAL A N     1 
ATOM   6224 C CA    . VAL B 1 240 ? 6.916  15.420  -72.319 1.00 32.90 ? 238  VAL A CA    1 
ATOM   6225 C C     . VAL B 1 240 ? 6.326  15.829  -73.656 1.00 33.33 ? 238  VAL A C     1 
ATOM   6226 O O     . VAL B 1 240 ? 6.182  14.940  -74.504 1.00 33.66 ? 238  VAL A O     1 
ATOM   6227 C CB    . VAL B 1 240 ? 8.376  14.934  -72.425 1.00 33.01 ? 238  VAL A CB    1 
ATOM   6228 C CG1   . VAL B 1 240 ? 9.300  16.010  -72.970 1.00 34.72 ? 238  VAL A CG1   1 
ATOM   6229 C CG2   . VAL B 1 240 ? 8.895  14.454  -71.081 1.00 32.41 ? 238  VAL A CG2   1 
ATOM   6230 N N     . ASN B 1 241 ? 5.941  17.100  -73.799 1.00 31.28 ? 239  ASN A N     1 
ATOM   6231 C CA    . ASN B 1 241 ? 5.468  17.669  -75.090 1.00 36.09 ? 239  ASN A CA    1 
ATOM   6232 C C     . ASN B 1 241 ? 6.585  17.518  -76.135 1.00 36.94 ? 239  ASN A C     1 
ATOM   6233 O O     . ASN B 1 241 ? 7.734  17.354  -75.745 1.00 36.82 ? 239  ASN A O     1 
ATOM   6234 C CB    . ASN B 1 241 ? 4.979  19.107  -74.906 1.00 34.44 ? 239  ASN A CB    1 
ATOM   6235 C CG    . ASN B 1 241 ? 3.736  19.162  -74.041 1.00 33.97 ? 239  ASN A CG    1 
ATOM   6236 O OD1   . ASN B 1 241 ? 2.840  18.337  -74.172 1.00 34.42 ? 239  ASN A OD1   1 
ATOM   6237 N ND2   . ASN B 1 241 ? 3.667  20.122  -73.146 1.00 36.35 ? 239  ASN A ND2   1 
ATOM   6238 N N     . ALA B 1 242 ? 6.215  17.525  -77.416 1.00 43.65 ? 240  ALA A N     1 
ATOM   6239 C CA    . ALA B 1 242 ? 7.115  17.424  -78.591 1.00 46.17 ? 240  ALA A CA    1 
ATOM   6240 C C     . ALA B 1 242 ? 8.304  18.373  -78.438 1.00 48.87 ? 240  ALA A C     1 
ATOM   6241 O O     . ALA B 1 242 ? 9.434  17.955  -78.760 1.00 44.95 ? 240  ALA A O     1 
ATOM   6242 C CB    . ALA B 1 242 ? 6.334  17.734  -79.843 1.00 46.81 ? 240  ALA A CB    1 
ATOM   6243 N N     . ASP B 1 243 ? 8.055  19.592  -77.944 1.00 47.90 ? 241  ASP A N     1 
ATOM   6244 C CA    . ASP B 1 243 ? 9.073  20.672  -77.797 1.00 45.72 ? 241  ASP A CA    1 
ATOM   6245 C C     . ASP B 1 243 ? 9.888  20.534  -76.509 1.00 43.58 ? 241  ASP A C     1 
ATOM   6246 O O     . ASP B 1 243 ? 10.632 21.481  -76.195 1.00 42.73 ? 241  ASP A O     1 
ATOM   6247 C CB    . ASP B 1 243 ? 8.421  22.055  -77.795 1.00 46.45 ? 241  ASP A CB    1 
ATOM   6248 C CG    . ASP B 1 243 ? 7.432  22.303  -76.662 1.00 48.85 ? 241  ASP A CG    1 
ATOM   6249 O OD1   . ASP B 1 243 ? 7.462  21.563  -75.627 1.00 45.67 ? 241  ASP A OD1   1 
ATOM   6250 O OD2   . ASP B 1 243 ? 6.650  23.257  -76.805 1.00 47.40 ? 241  ASP A OD2   1 
ATOM   6251 N N     . GLY B 1 244 ? 9.756  19.428  -75.773 1.00 42.28 ? 242  GLY A N     1 
ATOM   6252 C CA    . GLY B 1 244 ? 10.560 19.179  -74.562 1.00 38.10 ? 242  GLY A CA    1 
ATOM   6253 C C     . GLY B 1 244 ? 9.946  19.765  -73.302 1.00 38.36 ? 242  GLY A C     1 
ATOM   6254 O O     . GLY B 1 244 ? 10.430 19.401  -72.219 1.00 38.33 ? 242  GLY A O     1 
ATOM   6255 N N     . SER B 1 245 ? 8.924  20.635  -73.398 1.00 36.74 ? 243  SER A N     1 
ATOM   6256 C CA    . SER B 1 245 ? 8.220  21.172  -72.203 1.00 34.56 ? 243  SER A CA    1 
ATOM   6257 C C     . SER B 1 245 ? 7.479  20.017  -71.524 1.00 30.98 ? 243  SER A C     1 
ATOM   6258 O O     . SER B 1 245 ? 7.190  19.026  -72.197 1.00 31.66 ? 243  SER A O     1 
ATOM   6259 C CB    . SER B 1 245 ? 7.275  22.343  -72.530 1.00 34.33 ? 243  SER A CB    1 
ATOM   6260 O OG    . SER B 1 245 ? 6.198  21.951  -73.386 1.00 35.21 ? 243  SER A OG    1 
ATOM   6261 N N     . LEU B 1 246 ? 7.149  20.183  -70.254 1.00 29.50 ? 244  LEU A N     1 
ATOM   6262 C CA    . LEU B 1 246 ? 6.292  19.245  -69.500 1.00 31.47 ? 244  LEU A CA    1 
ATOM   6263 C C     . LEU B 1 246 ? 4.844  19.352  -69.983 1.00 33.29 ? 244  LEU A C     1 
ATOM   6264 O O     . LEU B 1 246 ? 4.343  20.491  -70.155 1.00 30.02 ? 244  LEU A O     1 
ATOM   6265 C CB    . LEU B 1 246 ? 6.395  19.587  -68.021 1.00 32.32 ? 244  LEU A CB    1 
ATOM   6266 C CG    . LEU B 1 246 ? 7.767  19.349  -67.398 1.00 33.47 ? 244  LEU A CG    1 
ATOM   6267 C CD1   . LEU B 1 246 ? 7.654  19.468  -65.889 1.00 34.69 ? 244  LEU A CD1   1 
ATOM   6268 C CD2   . LEU B 1 246 ? 8.330  17.997  -67.808 1.00 33.02 ? 244  LEU A CD2   1 
ATOM   6269 N N     . GLY B 1 247 ? 4.210  18.199  -70.196 1.00 30.18 ? 245  GLY A N     1 
ATOM   6270 C CA    . GLY B 1 247 ? 2.824  18.108  -70.692 1.00 28.75 ? 245  GLY A CA    1 
ATOM   6271 C C     . GLY B 1 247 ? 1.919  17.503  -69.648 1.00 27.00 ? 245  GLY A C     1 
ATOM   6272 O O     . GLY B 1 247 ? 2.058  17.828  -68.463 1.00 25.80 ? 245  GLY A O     1 
ATOM   6273 N N     . GLU B 1 248 ? 1.053  16.595  -70.074 1.00 28.55 ? 246  GLU A N     1 
ATOM   6274 C CA    . GLU B 1 248 ? -0.032 16.002  -69.253 1.00 30.99 ? 246  GLU A CA    1 
ATOM   6275 C C     . GLU B 1 248 ? 0.588  15.076  -68.194 1.00 28.66 ? 246  GLU A C     1 
ATOM   6276 O O     . GLU B 1 248 ? 1.504  14.314  -68.551 1.00 30.17 ? 246  GLU A O     1 
ATOM   6277 C CB    . GLU B 1 248 ? -0.970 15.268  -70.219 1.00 31.69 ? 246  GLU A CB    1 
ATOM   6278 C CG    . GLU B 1 248 ? -2.234 14.726  -69.584 1.00 36.29 ? 246  GLU A CG    1 
ATOM   6279 C CD    . GLU B 1 248 ? -3.132 13.897  -70.503 1.00 34.57 ? 246  GLU A CD    1 
ATOM   6280 O OE1   . GLU B 1 248 ? -2.680 13.497  -71.609 1.00 36.61 ? 246  GLU A OE1   1 
ATOM   6281 O OE2   . GLU B 1 248 ? -4.285 13.662  -70.110 1.00 39.49 ? 246  GLU A OE2   1 
ATOM   6282 N N     . LYS B 1 249 ? 0.135  15.167  -66.944 1.00 29.95 ? 247  LYS A N     1 
ATOM   6283 C CA    . LYS B 1 249 ? 0.457  14.199  -65.867 1.00 33.62 ? 247  LYS A CA    1 
ATOM   6284 C C     . LYS B 1 249 ? 0.090  12.797  -66.366 1.00 31.27 ? 247  LYS A C     1 
ATOM   6285 O O     . LYS B 1 249 ? -1.012 12.619  -66.924 1.00 25.82 ? 247  LYS A O     1 
ATOM   6286 C CB    . LYS B 1 249 ? -0.291 14.509  -64.569 1.00 37.76 ? 247  LYS A CB    1 
ATOM   6287 C CG    . LYS B 1 249 ? 0.371  15.558  -63.684 1.00 47.47 ? 247  LYS A CG    1 
ATOM   6288 C CD    . LYS B 1 249 ? -0.387 15.809  -62.376 1.00 54.59 ? 247  LYS A CD    1 
ATOM   6289 C CE    . LYS B 1 249 ? 0.239  16.883  -61.506 1.00 60.51 ? 247  LYS A CE    1 
ATOM   6290 N NZ    . LYS B 1 249 ? 1.631  16.527  -61.132 1.00 64.38 ? 247  LYS A NZ    1 
ATOM   6291 N N     . ASN B 1 250 ? 0.997  11.843  -66.204 1.00 27.38 ? 248  ASN A N     1 
ATOM   6292 C CA    . ASN B 1 250 ? 0.757  10.469  -66.681 1.00 25.70 ? 248  ASN A CA    1 
ATOM   6293 C C     . ASN B 1 250 ? -0.249 9.844   -65.723 1.00 24.28 ? 248  ASN A C     1 
ATOM   6294 O O     . ASN B 1 250 ? -0.405 10.322  -64.576 1.00 22.76 ? 248  ASN A O     1 
ATOM   6295 C CB    . ASN B 1 250 ? 2.058  9.683   -66.833 1.00 25.64 ? 248  ASN A CB    1 
ATOM   6296 C CG    . ASN B 1 250 ? 1.994  8.588   -67.877 1.00 25.99 ? 248  ASN A CG    1 
ATOM   6297 O OD1   . ASN B 1 250 ? 0.933  8.241   -68.389 1.00 26.51 ? 248  ASN A OD1   1 
ATOM   6298 N ND2   . ASN B 1 250 ? 3.142  8.033   -68.210 1.00 24.33 ? 248  ASN A ND2   1 
ATOM   6299 N N     . SER B 1 251 ? -0.893 8.788   -66.187 1.00 23.82 ? 249  SER A N     1 
ATOM   6300 C CA    . SER B 1 251 ? -1.945 8.040   -65.473 1.00 26.75 ? 249  SER A CA    1 
ATOM   6301 C C     . SER B 1 251 ? -1.299 7.097   -64.450 1.00 26.80 ? 249  SER A C     1 
ATOM   6302 O O     . SER B 1 251 ? -1.410 5.852   -64.566 1.00 22.23 ? 249  SER A O     1 
ATOM   6303 C CB    . SER B 1 251 ? -2.820 7.320   -66.481 1.00 29.38 ? 249  SER A CB    1 
ATOM   6304 O OG    . SER B 1 251 ? -3.990 6.930   -65.803 1.00 36.92 ? 249  SER A OG    1 
ATOM   6305 N N     . LEU B 1 252 ? -0.629 7.683   -63.463 1.00 27.23 ? 250  LEU A N     1 
ATOM   6306 C CA    . LEU B 1 252 ? 0.078  6.929   -62.407 1.00 28.03 ? 250  LEU A CA    1 
ATOM   6307 C C     . LEU B 1 252 ? 0.121  7.798   -61.162 1.00 28.77 ? 250  LEU A C     1 
ATOM   6308 O O     . LEU B 1 252 ? -0.041 9.014   -61.284 1.00 28.76 ? 250  LEU A O     1 
ATOM   6309 C CB    . LEU B 1 252 ? 1.476  6.526   -62.894 1.00 27.04 ? 250  LEU A CB    1 
ATOM   6310 C CG    . LEU B 1 252 ? 2.471  7.660   -63.150 1.00 25.44 ? 250  LEU A CG    1 
ATOM   6311 C CD1   . LEU B 1 252 ? 3.241  8.029   -61.891 1.00 26.43 ? 250  LEU A CD1   1 
ATOM   6312 C CD2   . LEU B 1 252 ? 3.450  7.274   -64.241 1.00 27.15 ? 250  LEU A CD2   1 
ATOM   6313 N N     . GLY B 1 253 ? 0.326  7.201   -60.006 1.00 25.66 ? 251  GLY A N     1 
ATOM   6314 C CA    . GLY B 1 253 ? 0.488  8.001   -58.791 1.00 26.55 ? 251  GLY A CA    1 
ATOM   6315 C C     . GLY B 1 253 ? 1.038  7.198   -57.648 1.00 25.65 ? 251  GLY A C     1 
ATOM   6316 O O     . GLY B 1 253 ? 1.014  5.931   -57.690 1.00 24.74 ? 251  GLY A O     1 
ATOM   6317 N N     . CYS B 1 254 ? 1.442  7.930   -56.609 1.00 24.38 ? 252  CYS A N     1 
ATOM   6318 C CA    . CYS B 1 254 ? 1.932  7.304   -55.363 1.00 25.47 ? 252  CYS A CA    1 
ATOM   6319 C C     . CYS B 1 254 ? 0.754  7.187   -54.387 1.00 25.24 ? 252  CYS A C     1 
ATOM   6320 O O     . CYS B 1 254 ? 0.221  8.211   -53.970 1.00 24.58 ? 252  CYS A O     1 
ATOM   6321 C CB    . CYS B 1 254 ? 3.045  8.140   -54.736 1.00 24.65 ? 252  CYS A CB    1 
ATOM   6322 S SG    . CYS B 1 254 ? 3.526  7.613   -53.076 1.00 26.14 ? 252  CYS A SG    1 
ATOM   6323 N N     . GLY B 1 255 ? 0.351  5.964   -54.076 1.00 24.33 ? 253  GLY A N     1 
ATOM   6324 C CA    . GLY B 1 255 ? -0.764 5.774   -53.138 1.00 24.42 ? 253  GLY A CA    1 
ATOM   6325 C C     . GLY B 1 255 ? -0.369 5.978   -51.688 1.00 24.08 ? 253  GLY A C     1 
ATOM   6326 O O     . GLY B 1 255 ? -1.251 6.312   -50.895 1.00 24.95 ? 253  GLY A O     1 
ATOM   6327 N N     . SER B 1 256 ? 0.906  5.797   -51.362 1.00 23.61 ? 254  SER A N     1 
ATOM   6328 C CA    . SER B 1 256 ? 1.370  5.875   -49.958 1.00 22.35 ? 254  SER A CA    1 
ATOM   6329 C C     . SER B 1 256 ? 2.890  5.735   -49.849 1.00 24.26 ? 254  SER A C     1 
ATOM   6330 O O     . SER B 1 256 ? 3.492  5.282   -50.814 1.00 22.55 ? 254  SER A O     1 
ATOM   6331 C CB    . SER B 1 256 ? 0.752  4.773   -49.169 1.00 22.40 ? 254  SER A CB    1 
ATOM   6332 O OG    . SER B 1 256 ? 1.176  3.512   -49.645 1.00 23.61 ? 254  SER A OG    1 
ATOM   6333 N N     . ILE B 1 257 ? 3.466  6.138   -48.711 1.00 24.76 ? 255  ILE A N     1 
ATOM   6334 C CA    . ILE B 1 257 ? 4.899  5.844   -48.415 1.00 25.36 ? 255  ILE A CA    1 
ATOM   6335 C C     . ILE B 1 257 ? 4.962  4.951   -47.186 1.00 26.32 ? 255  ILE A C     1 
ATOM   6336 O O     . ILE B 1 257 ? 4.018  4.996   -46.360 1.00 25.18 ? 255  ILE A O     1 
ATOM   6337 C CB    . ILE B 1 257 ? 5.726  7.124   -48.224 1.00 27.79 ? 255  ILE A CB    1 
ATOM   6338 C CG1   . ILE B 1 257 ? 5.224  7.953   -47.038 1.00 32.05 ? 255  ILE A CG1   1 
ATOM   6339 C CG2   . ILE B 1 257 ? 5.759  7.913   -49.522 1.00 29.05 ? 255  ILE A CG2   1 
ATOM   6340 C CD1   . ILE B 1 257 ? 5.908  9.302   -46.913 1.00 34.54 ? 255  ILE A CD1   1 
ATOM   6341 N N     . GLU B 1 258 ? 6.029  4.163   -47.093 1.00 24.86 ? 256  GLU A N     1 
ATOM   6342 C CA    . GLU B 1 258 ? 6.237  3.174   -46.015 1.00 25.83 ? 256  GLU A CA    1 
ATOM   6343 C C     . GLU B 1 258 ? 6.745  3.883   -44.759 1.00 25.65 ? 256  GLU A C     1 
ATOM   6344 O O     . GLU B 1 258 ? 7.409  4.940   -44.870 1.00 27.38 ? 256  GLU A O     1 
ATOM   6345 C CB    . GLU B 1 258 ? 7.247  2.094   -46.407 1.00 25.77 ? 256  GLU A CB    1 
ATOM   6346 C CG    . GLU B 1 258 ? 6.823  1.266   -47.607 1.00 27.15 ? 256  GLU A CG    1 
ATOM   6347 C CD    . GLU B 1 258 ? 5.520  0.488   -47.466 1.00 27.51 ? 256  GLU A CD    1 
ATOM   6348 O OE1   . GLU B 1 258 ? 4.814  0.291   -48.494 1.00 26.64 ? 256  GLU A OE1   1 
ATOM   6349 O OE2   . GLU B 1 258 ? 5.197  0.116   -46.337 1.00 26.39 ? 256  GLU A OE2   1 
ATOM   6350 N N     . HIS B 1 259 ? 6.399  3.308   -43.612 1.00 25.96 ? 257  HIS A N     1 
ATOM   6351 C CA    . HIS B 1 259 ? 7.001  3.580   -42.282 1.00 26.61 ? 257  HIS A CA    1 
ATOM   6352 C C     . HIS B 1 259 ? 8.121  2.572   -42.099 1.00 23.87 ? 257  HIS A C     1 
ATOM   6353 O O     . HIS B 1 259 ? 7.840  1.369   -42.126 1.00 22.26 ? 257  HIS A O     1 
ATOM   6354 C CB    . HIS B 1 259 ? 5.950  3.500   -41.169 1.00 29.70 ? 257  HIS A CB    1 
ATOM   6355 C CG    . HIS B 1 259 ? 4.757  4.339   -41.464 1.00 34.32 ? 257  HIS A CG    1 
ATOM   6356 N ND1   . HIS B 1 259 ? 4.845  5.706   -41.600 1.00 38.08 ? 257  HIS A ND1   1 
ATOM   6357 C CD2   . HIS B 1 259 ? 3.469  4.011   -41.695 1.00 34.82 ? 257  HIS A CD2   1 
ATOM   6358 C CE1   . HIS B 1 259 ? 3.654  6.192   -41.896 1.00 40.99 ? 257  HIS A CE1   1 
ATOM   6359 N NE2   . HIS B 1 259 ? 2.800  5.176   -41.958 1.00 38.31 ? 257  HIS A NE2   1 
ATOM   6360 N N     . LYS B 1 260 ? 9.358  3.053   -42.026 1.00 23.99 ? 258  LYS A N     1 
ATOM   6361 C CA    . LYS B 1 260 ? 10.551 2.195   -42.136 1.00 22.69 ? 258  LYS A CA    1 
ATOM   6362 C C     . LYS B 1 260 ? 11.410 2.268   -40.865 1.00 23.04 ? 258  LYS A C     1 
ATOM   6363 O O     . LYS B 1 260 ? 11.275 3.224   -40.087 1.00 21.41 ? 258  LYS A O     1 
ATOM   6364 C CB    . LYS B 1 260 ? 11.351 2.628   -43.362 1.00 21.86 ? 258  LYS A CB    1 
ATOM   6365 C CG    . LYS B 1 260 ? 10.572 2.598   -44.666 1.00 22.70 ? 258  LYS A CG    1 
ATOM   6366 C CD    . LYS B 1 260 ? 11.400 2.776   -45.915 1.00 21.92 ? 258  LYS A CD    1 
ATOM   6367 C CE    . LYS B 1 260 ? 12.342 3.955   -45.891 1.00 22.19 ? 258  LYS A CE    1 
ATOM   6368 N NZ    . LYS B 1 260 ? 11.630 5.243   -45.798 1.00 23.19 ? 258  LYS A NZ    1 
ATOM   6369 N N     . MET B 1 261 ? 12.272 1.266   -40.691 1.00 23.45 ? 259  MET A N     1 
ATOM   6370 C CA    . MET B 1 261 ? 13.312 1.237   -39.632 1.00 23.25 ? 259  MET A CA    1 
ATOM   6371 C C     . MET B 1 261 ? 14.233 2.460   -39.757 1.00 23.23 ? 259  MET A C     1 
ATOM   6372 O O     . MET B 1 261 ? 14.620 3.011   -38.715 1.00 24.22 ? 259  MET A O     1 
ATOM   6373 C CB    . MET B 1 261 ? 14.157 -0.027  -39.756 1.00 23.48 ? 259  MET A CB    1 
ATOM   6374 C CG    . MET B 1 261 ? 15.315 -0.095  -38.784 1.00 23.41 ? 259  MET A CG    1 
ATOM   6375 S SD    . MET B 1 261 ? 16.271 -1.610  -39.005 1.00 23.22 ? 259  MET A SD    1 
ATOM   6376 C CE    . MET B 1 261 ? 16.548 -2.057  -37.291 1.00 24.68 ? 259  MET A CE    1 
ATOM   6377 N N     . GLY B 1 262 ? 14.641 2.780   -40.985 1.00 22.49 ? 260  GLY A N     1 
ATOM   6378 C CA    . GLY B 1 262 ? 15.709 3.738   -41.304 1.00 23.55 ? 260  GLY A CA    1 
ATOM   6379 C C     . GLY B 1 262 ? 15.547 4.324   -42.685 1.00 24.39 ? 260  GLY A C     1 
ATOM   6380 O O     . GLY B 1 262 ? 14.442 4.163   -43.285 1.00 22.22 ? 260  GLY A O     1 
ATOM   6381 N N     . ILE B 1 263 ? 16.601 4.996   -43.162 1.00 22.00 ? 261  ILE A N     1 
ATOM   6382 C CA    . ILE B 1 263 ? 16.555 5.948   -44.310 1.00 23.42 ? 261  ILE A CA    1 
ATOM   6383 C C     . ILE B 1 263 ? 15.159 6.576   -44.389 1.00 22.25 ? 261  ILE A C     1 
ATOM   6384 O O     . ILE B 1 263 ? 14.513 6.492   -45.456 1.00 20.84 ? 261  ILE A O     1 
ATOM   6385 C CB    . ILE B 1 263 ? 16.986 5.310   -45.646 1.00 24.10 ? 261  ILE A CB    1 
ATOM   6386 C CG1   . ILE B 1 263 ? 16.220 4.026   -46.001 1.00 23.81 ? 261  ILE A CG1   1 
ATOM   6387 C CG2   . ILE B 1 263 ? 18.484 5.053   -45.659 1.00 24.91 ? 261  ILE A CG2   1 
ATOM   6388 C CD1   . ILE B 1 263 ? 16.360 3.654   -47.492 1.00 23.67 ? 261  ILE A CD1   1 
ATOM   6389 N N     . LYS B 1 264 ? 14.723 7.220   -43.313 1.00 21.18 ? 262  LYS A N     1 
ATOM   6390 C CA    . LYS B 1 264 ? 13.331 7.732   -43.218 1.00 20.80 ? 262  LYS A CA    1 
ATOM   6391 C C     . LYS B 1 264 ? 13.136 8.905   -44.181 1.00 22.58 ? 262  LYS A C     1 
ATOM   6392 O O     . LYS B 1 264 ? 11.990 9.090   -44.641 1.00 20.91 ? 262  LYS A O     1 
ATOM   6393 C CB    . LYS B 1 264 ? 13.005 8.109   -41.772 1.00 22.22 ? 262  LYS A CB    1 
ATOM   6394 C CG    . LYS B 1 264 ? 13.052 6.961   -40.788 1.00 21.88 ? 262  LYS A CG    1 
ATOM   6395 C CD    . LYS B 1 264 ? 12.296 7.293   -39.529 1.00 24.18 ? 262  LYS A CD    1 
ATOM   6396 C CE    . LYS B 1 264 ? 12.413 6.201   -38.507 1.00 23.99 ? 262  LYS A CE    1 
ATOM   6397 N NZ    . LYS B 1 264 ? 11.669 6.589   -37.302 1.00 25.41 ? 262  LYS A NZ    1 
ATOM   6398 N N     . ALA B 1 265 ? 14.211 9.598   -44.576 1.00 20.50 ? 263  ALA A N     1 
ATOM   6399 C CA    . ALA B 1 265 ? 14.121 10.718  -45.543 1.00 23.16 ? 263  ALA A CA    1 
ATOM   6400 C C     . ALA B 1 265 ? 14.097 10.213  -47.003 1.00 22.89 ? 263  ALA A C     1 
ATOM   6401 O O     . ALA B 1 265 ? 13.959 11.041  -47.891 1.00 21.49 ? 263  ALA A O     1 
ATOM   6402 C CB    . ALA B 1 265 ? 15.216 11.728  -45.284 1.00 20.48 ? 263  ALA A CB    1 
ATOM   6403 N N     . SER B 1 266 ? 14.192 8.898   -47.213 1.00 22.33 ? 264  SER A N     1 
ATOM   6404 C CA    . SER B 1 266 ? 14.065 8.219   -48.514 1.00 22.58 ? 264  SER A CA    1 
ATOM   6405 C C     . SER B 1 266 ? 12.598 7.796   -48.711 1.00 22.53 ? 264  SER A C     1 
ATOM   6406 O O     . SER B 1 266 ? 12.157 6.784   -48.127 1.00 24.18 ? 264  SER A O     1 
ATOM   6407 C CB    . SER B 1 266 ? 15.005 7.045   -48.583 1.00 22.07 ? 264  SER A CB    1 
ATOM   6408 O OG    . SER B 1 266 ? 14.952 6.423   -49.852 1.00 21.77 ? 264  SER A OG    1 
ATOM   6409 N N     . ALA B 1 267 ? 11.880 8.520   -49.560 1.00 23.88 ? 265  ALA A N     1 
ATOM   6410 C CA    . ALA B 1 267 ? 10.471 8.246   -49.918 1.00 24.75 ? 265  ALA A CA    1 
ATOM   6411 C C     . ALA B 1 267 ? 10.385 6.849   -50.546 1.00 24.68 ? 265  ALA A C     1 
ATOM   6412 O O     . ALA B 1 267 ? 11.007 6.642   -51.607 1.00 25.09 ? 265  ALA A O     1 
ATOM   6413 C CB    . ALA B 1 267 ? 9.960  9.313   -50.842 1.00 23.79 ? 265  ALA A CB    1 
ATOM   6414 N N     . THR B 1 268 ? 9.690  5.926   -49.871 1.00 22.12 ? 266  THR A N     1 
ATOM   6415 C CA    . THR B 1 268 ? 9.526  4.508   -50.291 1.00 22.15 ? 266  THR A CA    1 
ATOM   6416 C C     . THR B 1 268 ? 8.051  4.281   -50.659 1.00 23.78 ? 266  THR A C     1 
ATOM   6417 O O     . THR B 1 268 ? 7.196  4.221   -49.729 1.00 23.33 ? 266  THR A O     1 
ATOM   6418 C CB    . THR B 1 268 ? 10.076 3.566   -49.222 1.00 22.11 ? 266  THR A CB    1 
ATOM   6419 O OG1   . THR B 1 268 ? 11.402 3.988   -48.875 1.00 23.36 ? 266  THR A OG1   1 
ATOM   6420 C CG2   . THR B 1 268 ? 10.098 2.135   -49.706 1.00 23.10 ? 266  THR A CG2   1 
ATOM   6421 N N     . CYS B 1 269 ? 7.767  4.220   -51.968 1.00 21.94 ? 267  CYS A N     1 
ATOM   6422 C CA    . CYS B 1 269 ? 6.432  4.515   -52.541 1.00 23.27 ? 267  CYS A CA    1 
ATOM   6423 C C     . CYS B 1 269 ? 5.709  3.256   -53.008 1.00 21.67 ? 267  CYS A C     1 
ATOM   6424 O O     . CYS B 1 269 ? 6.331  2.385   -53.662 1.00 22.18 ? 267  CYS A O     1 
ATOM   6425 C CB    . CYS B 1 269 ? 6.573  5.505   -53.683 1.00 23.98 ? 267  CYS A CB    1 
ATOM   6426 S SG    . CYS B 1 269 ? 7.326  7.050   -53.117 1.00 27.72 ? 267  CYS A SG    1 
ATOM   6427 N N     . VAL B 1 270 ? 4.423  3.167   -52.672 1.00 23.29 ? 268  VAL A N     1 
ATOM   6428 C CA    . VAL B 1 270 ? 3.462  2.323   -53.435 1.00 22.75 ? 268  VAL A CA    1 
ATOM   6429 C C     . VAL B 1 270 ? 3.126  3.109   -54.700 1.00 23.01 ? 268  VAL A C     1 
ATOM   6430 O O     . VAL B 1 270 ? 2.627  4.239   -54.577 1.00 23.69 ? 268  VAL A O     1 
ATOM   6431 C CB    . VAL B 1 270 ? 2.210  1.975   -52.613 1.00 23.59 ? 268  VAL A CB    1 
ATOM   6432 C CG1   . VAL B 1 270 ? 1.207  1.173   -53.429 1.00 23.99 ? 268  VAL A CG1   1 
ATOM   6433 C CG2   . VAL B 1 270 ? 2.575  1.258   -51.326 1.00 24.11 ? 268  VAL A CG2   1 
ATOM   6434 N N     . MET B 1 271 ? 3.490  2.562   -55.846 1.00 23.10 ? 269  MET A N     1 
ATOM   6435 C CA    . MET B 1 271 ? 3.254  3.272   -57.117 1.00 23.53 ? 269  MET A CA    1 
ATOM   6436 C C     . MET B 1 271 ? 2.145  2.548   -57.884 1.00 24.36 ? 269  MET A C     1 
ATOM   6437 O O     . MET B 1 271 ? 2.273  1.345   -58.116 1.00 24.21 ? 269  MET A O     1 
ATOM   6438 C CB    . MET B 1 271 ? 4.543  3.371   -57.937 1.00 24.77 ? 269  MET A CB    1 
ATOM   6439 C CG    . MET B 1 271 ? 5.630  4.164   -57.258 1.00 23.20 ? 269  MET A CG    1 
ATOM   6440 S SD    . MET B 1 271 ? 5.145  5.883   -56.993 1.00 24.46 ? 269  MET A SD    1 
ATOM   6441 C CE    . MET B 1 271 ? 4.788  6.389   -58.674 1.00 24.54 ? 269  MET A CE    1 
ATOM   6442 N N     . ASN B 1 272 ? 1.080  3.275   -58.200 1.00 22.81 ? 270  ASN A N     1 
ATOM   6443 C CA    . ASN B 1 272 ? -0.058 2.686   -58.941 1.00 25.08 ? 270  ASN A CA    1 
ATOM   6444 C C     . ASN B 1 272 ? -0.054 3.186   -60.387 1.00 25.41 ? 270  ASN A C     1 
ATOM   6445 O O     . ASN B 1 272 ? -0.002 4.403   -60.585 1.00 26.05 ? 270  ASN A O     1 
ATOM   6446 C CB    . ASN B 1 272 ? -1.390 2.961   -58.246 1.00 24.68 ? 270  ASN A CB    1 
ATOM   6447 C CG    . ASN B 1 272 ? -1.382 2.558   -56.790 1.00 24.75 ? 270  ASN A CG    1 
ATOM   6448 O OD1   . ASN B 1 272 ? -1.237 1.385   -56.472 1.00 26.27 ? 270  ASN A OD1   1 
ATOM   6449 N ND2   . ASN B 1 272 ? -1.531 3.527   -55.906 1.00 24.35 ? 270  ASN A ND2   1 
ATOM   6450 N N     . PHE B 1 273 ? -0.098 2.258   -61.335 1.00 23.28 ? 271  PHE A N     1 
ATOM   6451 C CA    . PHE B 1 273 ? -0.120 2.614   -62.773 1.00 25.25 ? 271  PHE A CA    1 
ATOM   6452 C C     . PHE B 1 273 ? -1.481 2.233   -63.360 1.00 26.47 ? 271  PHE A C     1 
ATOM   6453 O O     . PHE B 1 273 ? -1.844 1.058   -63.307 1.00 23.80 ? 271  PHE A O     1 
ATOM   6454 C CB    . PHE B 1 273 ? 1.011  1.907   -63.520 1.00 25.77 ? 271  PHE A CB    1 
ATOM   6455 C CG    . PHE B 1 273 ? 2.393  2.243   -63.027 1.00 25.65 ? 271  PHE A CG    1 
ATOM   6456 C CD1   . PHE B 1 273 ? 2.960  1.540   -61.979 1.00 25.41 ? 271  PHE A CD1   1 
ATOM   6457 C CD2   . PHE B 1 273 ? 3.121  3.268   -63.606 1.00 24.06 ? 271  PHE A CD2   1 
ATOM   6458 C CE1   . PHE B 1 273 ? 4.229  1.853   -61.522 1.00 25.41 ? 271  PHE A CE1   1 
ATOM   6459 C CE2   . PHE B 1 273 ? 4.390  3.578   -63.150 1.00 24.30 ? 271  PHE A CE2   1 
ATOM   6460 C CZ    . PHE B 1 273 ? 4.939  2.872   -62.108 1.00 24.34 ? 271  PHE A CZ    1 
ATOM   6461 N N     . ASP B 1 274 ? -2.191 3.226   -63.883 1.00 25.76 ? 272  ASP A N     1 
ATOM   6462 C CA    . ASP B 1 274 ? -3.524 2.963   -64.472 1.00 27.28 ? 272  ASP A CA    1 
ATOM   6463 C C     . ASP B 1 274 ? -3.484 3.319   -65.958 1.00 26.55 ? 272  ASP A C     1 
ATOM   6464 O O     . ASP B 1 274 ? -3.846 4.434   -66.308 1.00 26.80 ? 272  ASP A O     1 
ATOM   6465 C CB    . ASP B 1 274 ? -4.643 3.632   -63.673 1.00 30.45 ? 272  ASP A CB    1 
ATOM   6466 C CG    . ASP B 1 274 ? -6.018 3.299   -64.225 1.00 35.73 ? 272  ASP A CG    1 
ATOM   6467 O OD1   . ASP B 1 274 ? -6.120 2.326   -64.988 1.00 34.25 ? 272  ASP A OD1   1 
ATOM   6468 O OD2   . ASP B 1 274 ? -6.970 4.015   -63.892 1.00 37.51 ? 272  ASP A OD2   1 
ATOM   6469 N N     . GLY B 1 275 ? -3.055 2.367   -66.782 1.00 24.23 ? 273  GLY A N     1 
ATOM   6470 C CA    . GLY B 1 275 ? -2.930 2.652   -68.213 1.00 24.54 ? 273  GLY A CA    1 
ATOM   6471 C C     . GLY B 1 275 ? -1.966 3.787   -68.446 1.00 24.24 ? 273  GLY A C     1 
ATOM   6472 O O     . GLY B 1 275 ? -2.225 4.586   -69.329 1.00 23.05 ? 273  GLY A O     1 
ATOM   6473 N N     . ALA B 1 276 ? -0.875 3.797   -67.686 1.00 23.80 ? 274  ALA A N     1 
ATOM   6474 C CA    . ALA B 1 276 ? 0.156  4.838   -67.850 1.00 23.70 ? 274  ALA A CA    1 
ATOM   6475 C C     . ALA B 1 276 ? 0.897  4.628   -69.170 1.00 22.97 ? 274  ALA A C     1 
ATOM   6476 O O     . ALA B 1 276 ? 1.270  3.494   -69.475 1.00 21.21 ? 274  ALA A O     1 
ATOM   6477 C CB    . ALA B 1 276 ? 1.101  4.827   -66.685 1.00 23.73 ? 274  ALA A CB    1 
ATOM   6478 N N     . THR B 1 277 ? 1.113  5.717   -69.892 1.00 22.57 ? 275  THR A N     1 
ATOM   6479 C CA    . THR B 1 277 ? 1.821  5.641   -71.188 1.00 24.70 ? 275  THR A CA    1 
ATOM   6480 C C     . THR B 1 277 ? 3.319  5.421   -70.955 1.00 25.20 ? 275  THR A C     1 
ATOM   6481 O O     . THR B 1 277 ? 3.893  6.111   -70.119 1.00 26.49 ? 275  THR A O     1 
ATOM   6482 C CB    . THR B 1 277 ? 1.563  6.884   -72.053 1.00 24.72 ? 275  THR A CB    1 
ATOM   6483 O OG1   . THR B 1 277 ? 0.194  6.875   -72.453 1.00 28.26 ? 275  THR A OG1   1 
ATOM   6484 C CG2   . THR B 1 277 ? 2.460  6.949   -73.268 1.00 25.37 ? 275  THR A CG2   1 
ATOM   6485 N N     . GLY B 1 278 ? 3.891  4.472   -71.683 1.00 23.49 ? 276  GLY A N     1 
ATOM   6486 C CA    . GLY B 1 278 ? 5.328  4.194   -71.589 1.00 24.22 ? 276  GLY A CA    1 
ATOM   6487 C C     . GLY B 1 278 ? 5.876  3.628   -72.878 1.00 22.82 ? 276  GLY A C     1 
ATOM   6488 O O     . GLY B 1 278 ? 5.098  3.349   -73.786 1.00 25.42 ? 276  GLY A O     1 
ATOM   6489 N N     . TRP B 1 279 ? 7.186  3.456   -72.931 1.00 23.43 ? 277  TRP A N     1 
ATOM   6490 C CA    . TRP B 1 279 ? 7.841  2.962   -74.159 1.00 22.46 ? 277  TRP A CA    1 
ATOM   6491 C C     . TRP B 1 279 ? 8.808  1.827   -73.829 1.00 23.61 ? 277  TRP A C     1 
ATOM   6492 O O     . TRP B 1 279 ? 9.501  1.889   -72.820 1.00 20.93 ? 277  TRP A O     1 
ATOM   6493 C CB    . TRP B 1 279 ? 8.541  4.117   -74.873 1.00 26.41 ? 277  TRP A CB    1 
ATOM   6494 C CG    . TRP B 1 279 ? 7.586  5.139   -75.394 1.00 25.56 ? 277  TRP A CG    1 
ATOM   6495 C CD1   . TRP B 1 279 ? 7.028  5.187   -76.636 1.00 27.82 ? 277  TRP A CD1   1 
ATOM   6496 C CD2   . TRP B 1 279 ? 7.051  6.256   -74.667 1.00 27.35 ? 277  TRP A CD2   1 
ATOM   6497 N NE1   . TRP B 1 279 ? 6.194  6.265   -76.737 1.00 26.76 ? 277  TRP A NE1   1 
ATOM   6498 C CE2   . TRP B 1 279 ? 6.188  6.939   -75.547 1.00 27.83 ? 277  TRP A CE2   1 
ATOM   6499 C CE3   . TRP B 1 279 ? 7.227  6.749   -73.371 1.00 27.58 ? 277  TRP A CE3   1 
ATOM   6500 C CZ2   . TRP B 1 279 ? 5.501  8.088   -75.166 1.00 29.11 ? 277  TRP A CZ2   1 
ATOM   6501 C CZ3   . TRP B 1 279 ? 6.545  7.882   -72.996 1.00 31.18 ? 277  TRP A CZ3   1 
ATOM   6502 C CH2   . TRP B 1 279 ? 5.693  8.539   -73.882 1.00 28.13 ? 277  TRP A CH2   1 
ATOM   6503 N N     . LEU B 1 280 ? 8.816  0.830   -74.694 1.00 22.53 ? 278  LEU A N     1 
ATOM   6504 C CA    . LEU B 1 280 ? 9.707  -0.324  -74.475 1.00 23.61 ? 278  LEU A CA    1 
ATOM   6505 C C     . LEU B 1 280 ? 11.181 0.081   -74.475 1.00 22.95 ? 278  LEU A C     1 
ATOM   6506 O O     . LEU B 1 280 ? 11.565 0.871   -75.335 1.00 23.70 ? 278  LEU A O     1 
ATOM   6507 C CB    . LEU B 1 280 ? 9.460  -1.374  -75.562 1.00 23.93 ? 278  LEU A CB    1 
ATOM   6508 C CG    . LEU B 1 280 ? 10.361 -2.606  -75.520 1.00 23.59 ? 278  LEU A CG    1 
ATOM   6509 C CD1   . LEU B 1 280 ? 10.021 -3.487  -74.331 1.00 25.50 ? 278  LEU A CD1   1 
ATOM   6510 C CD2   . LEU B 1 280 ? 10.250 -3.393  -76.814 1.00 25.71 ? 278  LEU A CD2   1 
ATOM   6511 N N     . VAL B 1 281 ? 11.933 -0.404  -73.501 1.00 21.22 ? 279  VAL A N     1 
ATOM   6512 C CA    . VAL B 1 281 ? 13.406 -0.295  -73.428 1.00 20.52 ? 279  VAL A CA    1 
ATOM   6513 C C     . VAL B 1 281 ? 13.978 -1.661  -73.772 1.00 22.12 ? 279  VAL A C     1 
ATOM   6514 O O     . VAL B 1 281 ? 13.626 -2.639  -73.100 1.00 22.89 ? 279  VAL A O     1 
ATOM   6515 C CB    . VAL B 1 281 ? 13.856 0.157   -72.039 1.00 22.59 ? 279  VAL A CB    1 
ATOM   6516 C CG1   . VAL B 1 281 ? 15.368 0.243   -71.969 1.00 22.04 ? 279  VAL A CG1   1 
ATOM   6517 C CG2   . VAL B 1 281 ? 13.193 1.468   -71.628 1.00 22.22 ? 279  VAL A CG2   1 
ATOM   6518 N N     . GLY B 1 282 ? 14.830 -1.724  -74.785 1.00 23.74 ? 280  GLY A N     1 
ATOM   6519 C CA    . GLY B 1 282 ? 15.422 -2.999  -75.218 1.00 23.94 ? 280  GLY A CA    1 
ATOM   6520 C C     . GLY B 1 282 ? 14.409 -3.816  -75.988 1.00 23.68 ? 280  GLY A C     1 
ATOM   6521 O O     . GLY B 1 282 ? 13.691 -3.267  -76.816 1.00 23.06 ? 280  GLY A O     1 
ATOM   6522 N N     . GLU B 1 283 ? 14.388 -5.112  -75.747 1.00 25.07 ? 281  GLU A N     1 
ATOM   6523 C CA    . GLU B 1 283 ? 13.586 -6.076  -76.518 1.00 25.16 ? 281  GLU A CA    1 
ATOM   6524 C C     . GLU B 1 283 ? 12.534 -6.688  -75.605 1.00 25.51 ? 281  GLU A C     1 
ATOM   6525 O O     . GLU B 1 283 ? 12.802 -6.844  -74.404 1.00 24.01 ? 281  GLU A O     1 
ATOM   6526 C CB    . GLU B 1 283 ? 14.481 -7.185  -77.067 1.00 28.15 ? 281  GLU A CB    1 
ATOM   6527 C CG    . GLU B 1 283 ? 15.390 -6.735  -78.186 1.00 32.82 ? 281  GLU A CG    1 
ATOM   6528 C CD    . GLU B 1 283 ? 16.328 -7.866  -78.560 1.00 38.42 ? 281  GLU A CD    1 
ATOM   6529 O OE1   . GLU B 1 283 ? 15.853 -8.876  -79.122 1.00 45.13 ? 281  GLU A OE1   1 
ATOM   6530 O OE2   . GLU B 1 283 ? 17.489 -7.787  -78.160 1.00 41.05 ? 281  GLU A OE2   1 
ATOM   6531 N N     . VAL B 1 284 ? 11.400 -7.050  -76.188 1.00 23.20 ? 282  VAL A N     1 
ATOM   6532 C CA    . VAL B 1 284 ? 10.300 -7.775  -75.507 1.00 24.38 ? 282  VAL A CA    1 
ATOM   6533 C C     . VAL B 1 284 ? 10.882 -9.074  -74.949 1.00 23.35 ? 282  VAL A C     1 
ATOM   6534 O O     . VAL B 1 284 ? 11.717 -9.669  -75.625 1.00 22.68 ? 282  VAL A O     1 
ATOM   6535 C CB    . VAL B 1 284 ? 9.141  -8.007  -76.488 1.00 27.17 ? 282  VAL A CB    1 
ATOM   6536 C CG1   . VAL B 1 284 ? 8.120  -8.978  -75.935 1.00 34.14 ? 282  VAL A CG1   1 
ATOM   6537 C CG2   . VAL B 1 284 ? 8.479  -6.684  -76.832 1.00 29.24 ? 282  VAL A CG2   1 
ATOM   6538 N N     . ASN B 1 285 ? 10.489 -9.433  -73.723 1.00 22.37 ? 283  ASN A N     1 
ATOM   6539 C CA    . ASN B 1 285 ? 10.904 -10.670 -73.009 1.00 23.88 ? 283  ASN A CA    1 
ATOM   6540 C C     . ASN B 1 285 ? 12.358 -10.615 -72.528 1.00 23.49 ? 283  ASN A C     1 
ATOM   6541 O O     . ASN B 1 285 ? 12.771 -11.588 -71.891 1.00 24.15 ? 283  ASN A O     1 
ATOM   6542 C CB    . ASN B 1 285 ? 10.713 -11.911 -73.870 1.00 24.47 ? 283  ASN A CB    1 
ATOM   6543 C CG    . ASN B 1 285 ? 9.259  -12.141 -74.175 1.00 25.89 ? 283  ASN A CG    1 
ATOM   6544 O OD1   . ASN B 1 285 ? 8.401  -11.874 -73.335 1.00 23.82 ? 283  ASN A OD1   1 
ATOM   6545 N ND2   . ASN B 1 285 ? 8.993  -12.672 -75.360 1.00 25.34 ? 283  ASN A ND2   1 
ATOM   6546 N N     . LYS B 1 286 ? 13.069 -9.511  -72.745 1.00 23.27 ? 284  LYS A N     1 
ATOM   6547 C CA    . LYS B 1 286 ? 14.503 -9.381  -72.365 1.00 26.51 ? 284  LYS A CA    1 
ATOM   6548 C C     . LYS B 1 286 ? 14.671 -8.184  -71.433 1.00 23.83 ? 284  LYS A C     1 
ATOM   6549 O O     . LYS B 1 286 ? 15.740 -7.547  -71.450 1.00 24.89 ? 284  LYS A O     1 
ATOM   6550 C CB    . LYS B 1 286 ? 15.329 -9.331  -73.650 1.00 29.47 ? 284  LYS A CB    1 
ATOM   6551 C CG    . LYS B 1 286 ? 15.184 -10.597 -74.492 1.00 34.28 ? 284  LYS A CG    1 
ATOM   6552 C CD    . LYS B 1 286 ? 16.364 -10.929 -75.385 1.00 37.95 ? 284  LYS A CD    1 
ATOM   6553 C CE    . LYS B 1 286 ? 16.023 -11.978 -76.425 1.00 41.15 ? 284  LYS A CE    1 
ATOM   6554 N NZ    . LYS B 1 286 ? 17.233 -12.672 -76.940 1.00 44.89 ? 284  LYS A NZ    1 
ATOM   6555 N N     . GLY B 1 287 ? 13.667 -7.952  -70.583 1.00 22.67 ? 285  GLY A N     1 
ATOM   6556 C CA    . GLY B 1 287 ? 13.668 -6.879  -69.574 1.00 23.43 ? 285  GLY A CA    1 
ATOM   6557 C C     . GLY B 1 287 ? 14.783 -7.083  -68.565 1.00 23.97 ? 285  GLY A C     1 
ATOM   6558 O O     . GLY B 1 287 ? 15.453 -6.079  -68.204 1.00 24.36 ? 285  GLY A O     1 
ATOM   6559 N N     . LEU B 1 288 ? 15.037 -8.321  -68.139 1.00 23.00 ? 286  LEU A N     1 
ATOM   6560 C CA    . LEU B 1 288 ? 16.097 -8.553  -67.111 1.00 25.25 ? 286  LEU A CA    1 
ATOM   6561 C C     . LEU B 1 288 ? 17.469 -8.267  -67.739 1.00 25.87 ? 286  LEU A C     1 
ATOM   6562 O O     . LEU B 1 288 ? 18.289 -7.600  -67.097 1.00 24.25 ? 286  LEU A O     1 
ATOM   6563 C CB    . LEU B 1 288 ? 16.017 -9.980  -66.557 1.00 26.82 ? 286  LEU A CB    1 
ATOM   6564 C CG    . LEU B 1 288 ? 14.741 -10.333 -65.801 1.00 29.32 ? 286  LEU A CG    1 
ATOM   6565 C CD1   . LEU B 1 288 ? 14.805 -11.754 -65.263 1.00 31.78 ? 286  LEU A CD1   1 
ATOM   6566 C CD2   . LEU B 1 288 ? 14.472 -9.353  -64.668 1.00 30.31 ? 286  LEU A CD2   1 
ATOM   6567 N N     . ALA B 1 289 ? 17.688 -8.670  -68.989 1.00 25.52 ? 287  ALA A N     1 
ATOM   6568 C CA    . ALA B 1 289 ? 18.969 -8.438  -69.687 1.00 26.50 ? 287  ALA A CA    1 
ATOM   6569 C C     . ALA B 1 289 ? 19.150 -6.928  -69.883 1.00 24.46 ? 287  ALA A C     1 
ATOM   6570 O O     . ALA B 1 289 ? 20.296 -6.446  -69.803 1.00 24.35 ? 287  ALA A O     1 
ATOM   6571 C CB    . ALA B 1 289 ? 19.020 -9.221  -70.990 1.00 27.19 ? 287  ALA A CB    1 
ATOM   6572 N N     . ALA B 1 290 ? 18.064 -6.174  -70.038 1.00 24.06 ? 288  ALA A N     1 
ATOM   6573 C CA    . ALA B 1 290 ? 18.160 -4.708  -70.212 1.00 22.98 ? 288  ALA A CA    1 
ATOM   6574 C C     . ALA B 1 290 ? 18.759 -4.055  -68.958 1.00 25.44 ? 288  ALA A C     1 
ATOM   6575 O O     . ALA B 1 290 ? 19.206 -2.900  -69.068 1.00 24.74 ? 288  ALA A O     1 
ATOM   6576 C CB    . ALA B 1 290 ? 16.840 -4.110  -70.555 1.00 24.42 ? 288  ALA A CB    1 
ATOM   6577 N N     . MET B 1 291 ? 18.698 -4.731  -67.799 1.00 25.05 ? 289  MET A N     1 
ATOM   6578 C CA    . MET B 1 291 ? 19.215 -4.211  -66.499 1.00 26.89 ? 289  MET A CA    1 
ATOM   6579 C C     . MET B 1 291 ? 20.576 -4.837  -66.126 1.00 26.51 ? 289  MET A C     1 
ATOM   6580 O O     . MET B 1 291 ? 21.086 -4.560  -65.014 1.00 24.85 ? 289  MET A O     1 
ATOM   6581 C CB    . MET B 1 291 ? 18.196 -4.476  -65.393 1.00 26.27 ? 289  MET A CB    1 
ATOM   6582 C CG    . MET B 1 291 ? 16.853 -3.853  -65.695 1.00 28.03 ? 289  MET A CG    1 
ATOM   6583 S SD    . MET B 1 291 ? 15.736 -3.959  -64.294 1.00 30.08 ? 289  MET A SD    1 
ATOM   6584 C CE    . MET B 1 291 ? 15.518 -5.735  -64.209 1.00 28.96 ? 289  MET A CE    1 
ATOM   6585 N N     . PHE B 1 292 ? 21.184 -5.637  -66.997 1.00 26.03 ? 290  PHE A N     1 
ATOM   6586 C CA    . PHE B 1 292 ? 22.403 -6.412  -66.629 1.00 30.14 ? 290  PHE A CA    1 
ATOM   6587 C C     . PHE B 1 292 ? 23.521 -5.438  -66.203 1.00 27.53 ? 290  PHE A C     1 
ATOM   6588 O O     . PHE B 1 292 ? 24.044 -5.592  -65.080 1.00 29.57 ? 290  PHE A O     1 
ATOM   6589 C CB    . PHE B 1 292 ? 22.768 -7.387  -67.754 1.00 33.52 ? 290  PHE A CB    1 
ATOM   6590 C CG    . PHE B 1 292 ? 24.125 -8.026  -67.615 1.00 36.06 ? 290  PHE A CG    1 
ATOM   6591 C CD1   . PHE B 1 292 ? 24.299 -9.156  -66.822 1.00 39.86 ? 290  PHE A CD1   1 
ATOM   6592 C CD2   . PHE B 1 292 ? 25.228 -7.491  -68.271 1.00 34.82 ? 290  PHE A CD2   1 
ATOM   6593 C CE1   . PHE B 1 292 ? 25.555 -9.736  -66.693 1.00 41.43 ? 290  PHE A CE1   1 
ATOM   6594 C CE2   . PHE B 1 292 ? 26.484 -8.063  -68.124 1.00 37.47 ? 290  PHE A CE2   1 
ATOM   6595 C CZ    . PHE B 1 292 ? 26.644 -9.187  -67.346 1.00 36.33 ? 290  PHE A CZ    1 
ATOM   6596 N N     . THR B 1 293 ? 23.852 -4.436  -67.014 1.00 27.67 ? 291  THR A N     1 
ATOM   6597 C CA    . THR B 1 293 ? 24.945 -3.450  -66.731 1.00 29.43 ? 291  THR A CA    1 
ATOM   6598 C C     . THR B 1 293 ? 24.567 -2.648  -65.481 1.00 28.30 ? 291  THR A C     1 
ATOM   6599 O O     . THR B 1 293 ? 25.381 -2.558  -64.549 1.00 25.26 ? 291  THR A O     1 
ATOM   6600 C CB    . THR B 1 293 ? 25.204 -2.540  -67.938 1.00 32.32 ? 291  THR A CB    1 
ATOM   6601 O OG1   . THR B 1 293 ? 25.717 -3.416  -68.934 1.00 34.93 ? 291  THR A OG1   1 
ATOM   6602 C CG2   . THR B 1 293 ? 26.201 -1.436  -67.692 1.00 33.36 ? 291  THR A CG2   1 
ATOM   6603 N N     . MET B 1 294 ? 23.354 -2.119  -65.466 1.00 25.44 ? 292  MET A N     1 
ATOM   6604 C CA    . MET B 1 294 ? 22.832 -1.311  -64.350 1.00 28.05 ? 292  MET A CA    1 
ATOM   6605 C C     . MET B 1 294 ? 23.080 -2.066  -63.041 1.00 27.39 ? 292  MET A C     1 
ATOM   6606 O O     . MET B 1 294 ? 23.588 -1.458  -62.115 1.00 25.02 ? 292  MET A O     1 
ATOM   6607 C CB    . MET B 1 294 ? 21.339 -1.032  -64.526 1.00 30.31 ? 292  MET A CB    1 
ATOM   6608 C CG    . MET B 1 294 ? 20.666 -0.554  -63.263 1.00 34.53 ? 292  MET A CG    1 
ATOM   6609 S SD    . MET B 1 294 ? 18.895 -0.439  -63.559 1.00 49.47 ? 292  MET A SD    1 
ATOM   6610 C CE    . MET B 1 294 ? 18.797 1.141   -64.374 1.00 52.98 ? 292  MET A CE    1 
ATOM   6611 N N     . MET B 1 295 ? 22.754 -3.353  -62.984 1.00 26.01 ? 293  MET A N     1 
ATOM   6612 C CA    . MET B 1 295 ? 22.817 -4.146  -61.727 1.00 27.01 ? 293  MET A CA    1 
ATOM   6613 C C     . MET B 1 295 ? 24.264 -4.494  -61.380 1.00 26.95 ? 293  MET A C     1 
ATOM   6614 O O     . MET B 1 295 ? 24.531 -4.552  -60.197 1.00 23.31 ? 293  MET A O     1 
ATOM   6615 C CB    . MET B 1 295 ? 21.971 -5.419  -61.806 1.00 29.59 ? 293  MET A CB    1 
ATOM   6616 C CG    . MET B 1 295 ? 20.496 -5.115  -61.603 1.00 36.98 ? 293  MET A CG    1 
ATOM   6617 S SD    . MET B 1 295 ? 19.461 -6.612  -61.698 1.00 51.59 ? 293  MET A SD    1 
ATOM   6618 C CE    . MET B 1 295 ? 17.906 -5.918  -61.137 1.00 50.82 ? 293  MET A CE    1 
ATOM   6619 N N     . ASN B 1 296 ? 25.171 -4.676  -62.348 1.00 26.97 ? 294  ASN A N     1 
ATOM   6620 C CA    . ASN B 1 296 ? 26.614 -4.841  -62.027 1.00 27.20 ? 294  ASN A CA    1 
ATOM   6621 C C     . ASN B 1 296 ? 27.097 -3.626  -61.225 1.00 27.41 ? 294  ASN A C     1 
ATOM   6622 O O     . ASN B 1 296 ? 27.781 -3.807  -60.176 1.00 24.21 ? 294  ASN A O     1 
ATOM   6623 C CB    . ASN B 1 296 ? 27.494 -4.958  -63.268 1.00 30.75 ? 294  ASN A CB    1 
ATOM   6624 C CG    . ASN B 1 296 ? 27.308 -6.244  -64.039 1.00 32.98 ? 294  ASN A CG    1 
ATOM   6625 O OD1   . ASN B 1 296 ? 26.932 -7.262  -63.475 1.00 31.92 ? 294  ASN A OD1   1 
ATOM   6626 N ND2   . ASN B 1 296 ? 27.591 -6.194  -65.335 1.00 35.62 ? 294  ASN A ND2   1 
ATOM   6627 N N     . TYR B 1 297 ? 26.782 -2.428  -61.714 1.00 23.64 ? 295  TYR A N     1 
ATOM   6628 C CA    . TYR B 1 297 ? 27.195 -1.147  -61.089 1.00 25.51 ? 295  TYR A CA    1 
ATOM   6629 C C     . TYR B 1 297 ? 26.442 -0.951  -59.761 1.00 24.92 ? 295  TYR A C     1 
ATOM   6630 O O     . TYR B 1 297 ? 27.051 -0.446  -58.800 1.00 23.13 ? 295  TYR A O     1 
ATOM   6631 C CB    . TYR B 1 297 ? 26.989 0.027   -62.062 1.00 24.92 ? 295  TYR A CB    1 
ATOM   6632 C CG    . TYR B 1 297 ? 28.063 0.146   -63.117 1.00 26.98 ? 295  TYR A CG    1 
ATOM   6633 C CD1   . TYR B 1 297 ? 28.060 -0.666  -64.249 1.00 27.30 ? 295  TYR A CD1   1 
ATOM   6634 C CD2   . TYR B 1 297 ? 29.112 1.044   -62.978 1.00 27.25 ? 295  TYR A CD2   1 
ATOM   6635 C CE1   . TYR B 1 297 ? 29.071 -0.590  -65.196 1.00 27.11 ? 295  TYR A CE1   1 
ATOM   6636 C CE2   . TYR B 1 297 ? 30.135 1.119   -63.915 1.00 28.18 ? 295  TYR A CE2   1 
ATOM   6637 C CZ    . TYR B 1 297 ? 30.099 0.325   -65.049 1.00 27.65 ? 295  TYR A CZ    1 
ATOM   6638 O OH    . TYR B 1 297 ? 31.093 0.409   -65.992 1.00 26.82 ? 295  TYR A OH    1 
ATOM   6639 N N     . ALA B 1 298 ? 25.159 -1.308  -59.710 1.00 23.24 ? 296  ALA A N     1 
ATOM   6640 C CA    . ALA B 1 298 ? 24.311 -1.154  -58.507 1.00 24.62 ? 296  ALA A CA    1 
ATOM   6641 C C     . ALA B 1 298 ? 24.815 -2.069  -57.381 1.00 25.44 ? 296  ALA A C     1 
ATOM   6642 O O     . ALA B 1 298 ? 24.771 -1.619  -56.229 1.00 25.08 ? 296  ALA A O     1 
ATOM   6643 C CB    . ALA B 1 298 ? 22.839 -1.383  -58.805 1.00 23.78 ? 296  ALA A CB    1 
ATOM   6644 N N     . ARG B 1 299 ? 25.250 -3.300  -57.675 1.00 24.48 ? 297  ARG A N     1 
ATOM   6645 C CA    . ARG B 1 299 ? 25.786 -4.216  -56.637 1.00 25.10 ? 297  ARG A CA    1 
ATOM   6646 C C     . ARG B 1 299 ? 26.966 -3.553  -55.917 1.00 24.41 ? 297  ARG A C     1 
ATOM   6647 O O     . ARG B 1 299 ? 26.998 -3.571  -54.641 1.00 23.73 ? 297  ARG A O     1 
ATOM   6648 C CB    . ARG B 1 299 ? 26.180 -5.578  -57.223 1.00 27.86 ? 297  ARG A CB    1 
ATOM   6649 C CG    . ARG B 1 299 ? 24.961 -6.416  -57.582 1.00 34.12 ? 297  ARG A CG    1 
ATOM   6650 C CD    . ARG B 1 299 ? 25.223 -7.882  -57.882 1.00 38.65 ? 297  ARG A CD    1 
ATOM   6651 N NE    . ARG B 1 299 ? 25.886 -8.066  -59.147 1.00 46.45 ? 297  ARG A NE    1 
ATOM   6652 C CZ    . ARG B 1 299 ? 25.292 -8.160  -60.335 1.00 51.64 ? 297  ARG A CZ    1 
ATOM   6653 N NH1   . ARG B 1 299 ? 26.043 -8.305  -61.414 1.00 48.67 ? 297  ARG A NH1   1 
ATOM   6654 N NH2   . ARG B 1 299 ? 23.973 -8.105  -60.455 1.00 53.16 ? 297  ARG A NH2   1 
ATOM   6655 N N     . LEU B 1 300 ? 27.913 -2.980  -56.661 1.00 21.00 ? 298  LEU A N     1 
ATOM   6656 C CA    . LEU B 1 300 ? 29.048 -2.261  -56.031 1.00 21.83 ? 298  LEU A CA    1 
ATOM   6657 C C     . LEU B 1 300 ? 28.502 -1.041  -55.271 1.00 21.16 ? 298  LEU A C     1 
ATOM   6658 O O     . LEU B 1 300 ? 28.912 -0.818  -54.133 1.00 22.73 ? 298  LEU A O     1 
ATOM   6659 C CB    . LEU B 1 300 ? 30.062 -1.839  -57.095 1.00 22.51 ? 298  LEU A CB    1 
ATOM   6660 C CG    . LEU B 1 300 ? 31.181 -0.941  -56.562 1.00 24.67 ? 298  LEU A CG    1 
ATOM   6661 C CD1   . LEU B 1 300 ? 31.972 -1.688  -55.481 1.00 24.69 ? 298  LEU A CD1   1 
ATOM   6662 C CD2   . LEU B 1 300 ? 32.106 -0.463  -57.687 1.00 25.85 ? 298  LEU A CD2   1 
ATOM   6663 N N     . GLY B 1 301 ? 27.600 -0.273  -55.876 1.00 21.33 ? 299  GLY A N     1 
ATOM   6664 C CA    . GLY B 1 301 ? 27.027 0.944   -55.271 1.00 22.85 ? 299  GLY A CA    1 
ATOM   6665 C C     . GLY B 1 301 ? 26.357 0.650   -53.928 1.00 24.35 ? 299  GLY A C     1 
ATOM   6666 O O     . GLY B 1 301 ? 26.522 1.444   -52.993 1.00 21.99 ? 299  GLY A O     1 
ATOM   6667 N N     . VAL B 1 302 ? 25.687 -0.498  -53.795 1.00 24.13 ? 300  VAL A N     1 
ATOM   6668 C CA    . VAL B 1 302 ? 25.011 -0.872  -52.520 1.00 23.63 ? 300  VAL A CA    1 
ATOM   6669 C C     . VAL B 1 302 ? 26.061 -1.246  -51.459 1.00 23.22 ? 300  VAL A C     1 
ATOM   6670 O O     . VAL B 1 302 ? 25.924 -0.818  -50.286 1.00 20.19 ? 300  VAL A O     1 
ATOM   6671 C CB    . VAL B 1 302 ? 23.982 -1.986  -52.769 1.00 25.27 ? 300  VAL A CB    1 
ATOM   6672 C CG1   . VAL B 1 302 ? 23.401 -2.489  -51.468 1.00 27.71 ? 300  VAL A CG1   1 
ATOM   6673 C CG2   . VAL B 1 302 ? 22.892 -1.484  -53.687 1.00 26.54 ? 300  VAL A CG2   1 
ATOM   6674 N N     . GLY B 1 303 ? 27.088 -1.998  -51.842 1.00 20.48 ? 301  GLY A N     1 
ATOM   6675 C CA    . GLY B 1 303 ? 28.256 -2.253  -50.980 1.00 22.27 ? 301  GLY A CA    1 
ATOM   6676 C C     . GLY B 1 303 ? 28.833 -0.948  -50.457 1.00 21.56 ? 301  GLY A C     1 
ATOM   6677 O O     . GLY B 1 303 ? 29.075 -0.836  -49.256 1.00 20.68 ? 301  GLY A O     1 
ATOM   6678 N N     . ILE B 1 304 ? 29.023 0.012   -51.353 1.00 22.35 ? 302  ILE A N     1 
ATOM   6679 C CA    . ILE B 1 304 ? 29.614 1.325   -51.007 1.00 21.97 ? 302  ILE A CA    1 
ATOM   6680 C C     . ILE B 1 304 ? 28.693 2.009   -50.005 1.00 23.66 ? 302  ILE A C     1 
ATOM   6681 O O     . ILE B 1 304 ? 29.239 2.603   -49.089 1.00 22.13 ? 302  ILE A O     1 
ATOM   6682 C CB    . ILE B 1 304 ? 29.907 2.169   -52.246 1.00 22.00 ? 302  ILE A CB    1 
ATOM   6683 C CG1   . ILE B 1 304 ? 31.135 1.631   -52.984 1.00 23.56 ? 302  ILE A CG1   1 
ATOM   6684 C CG2   . ILE B 1 304 ? 30.099 3.624   -51.870 1.00 22.41 ? 302  ILE A CG2   1 
ATOM   6685 C CD1   . ILE B 1 304 ? 31.323 2.229   -54.360 1.00 25.65 ? 302  ILE A CD1   1 
ATOM   6686 N N     . ALA B 1 305 ? 27.368 1.876   -50.140 1.00 22.01 ? 303  ALA A N     1 
ATOM   6687 C CA    . ALA B 1 305 ? 26.403 2.498   -49.209 1.00 22.84 ? 303  ALA A CA    1 
ATOM   6688 C C     . ALA B 1 305 ? 26.598 1.939   -47.795 1.00 22.99 ? 303  ALA A C     1 
ATOM   6689 O O     . ALA B 1 305 ? 26.593 2.734   -46.868 1.00 21.39 ? 303  ALA A O     1 
ATOM   6690 C CB    . ALA B 1 305 ? 24.986 2.315   -49.695 1.00 23.57 ? 303  ALA A CB    1 
ATOM   6691 N N     . GLY B 1 306 ? 26.715 0.613   -47.648 1.00 22.55 ? 304  GLY A N     1 
ATOM   6692 C CA    . GLY B 1 306 ? 26.989 -0.044  -46.362 1.00 22.35 ? 304  GLY A CA    1 
ATOM   6693 C C     . GLY B 1 306 ? 28.304 0.449   -45.763 1.00 24.51 ? 304  GLY A C     1 
ATOM   6694 O O     . GLY B 1 306 ? 28.315 0.876   -44.597 1.00 24.18 ? 304  GLY A O     1 
ATOM   6695 N N     . LEU B 1 307 ? 29.376 0.397   -46.541 1.00 21.95 ? 305  LEU A N     1 
ATOM   6696 C CA    . LEU B 1 307 ? 30.705 0.912   -46.160 1.00 23.50 ? 305  LEU A CA    1 
ATOM   6697 C C     . LEU B 1 307 ? 30.581 2.364   -45.678 1.00 22.68 ? 305  LEU A C     1 
ATOM   6698 O O     . LEU B 1 307 ? 31.212 2.694   -44.648 1.00 22.93 ? 305  LEU A O     1 
ATOM   6699 C CB    . LEU B 1 307 ? 31.629 0.827   -47.378 1.00 23.12 ? 305  LEU A CB    1 
ATOM   6700 C CG    . LEU B 1 307 ? 32.913 1.646   -47.289 1.00 24.13 ? 305  LEU A CG    1 
ATOM   6701 C CD1   . LEU B 1 307 ? 33.798 1.150   -46.169 1.00 25.10 ? 305  LEU A CD1   1 
ATOM   6702 C CD2   . LEU B 1 307 ? 33.652 1.640   -48.616 1.00 25.59 ? 305  LEU A CD2   1 
ATOM   6703 N N     . ALA B 1 308 ? 29.861 3.197   -46.431 1.00 20.97 ? 306  ALA A N     1 
ATOM   6704 C CA    . ALA B 1 308 ? 29.708 4.645   -46.157 1.00 22.97 ? 306  ALA A CA    1 
ATOM   6705 C C     . ALA B 1 308 ? 29.116 4.854   -44.749 1.00 22.98 ? 306  ALA A C     1 
ATOM   6706 O O     . ALA B 1 308 ? 29.547 5.781   -44.040 1.00 21.24 ? 306  ALA A O     1 
ATOM   6707 C CB    . ALA B 1 308 ? 28.867 5.280   -47.222 1.00 22.34 ? 306  ALA A CB    1 
ATOM   6708 N N     . THR B 1 309 ? 28.181 4.008   -44.321 1.00 24.58 ? 307  THR A N     1 
ATOM   6709 C CA    . THR B 1 309 ? 27.593 4.142   -42.959 1.00 23.65 ? 307  THR A CA    1 
ATOM   6710 C C     . THR B 1 309 ? 28.642 3.738   -41.911 1.00 22.12 ? 307  THR A C     1 
ATOM   6711 O O     . THR B 1 309 ? 28.682 4.379   -40.877 1.00 23.71 ? 307  THR A O     1 
ATOM   6712 C CB    . THR B 1 309 ? 26.273 3.390   -42.766 1.00 23.27 ? 307  THR A CB    1 
ATOM   6713 O OG1   . THR B 1 309 ? 26.560 1.988   -42.807 1.00 23.16 ? 307  THR A OG1   1 
ATOM   6714 C CG2   . THR B 1 309 ? 25.229 3.782   -43.785 1.00 23.02 ? 307  THR A CG2   1 
ATOM   6715 N N     . GLY B 1 310 ? 29.397 2.668   -42.145 1.00 21.67 ? 308  GLY A N     1 
ATOM   6716 C CA    . GLY B 1 310 ? 30.531 2.287   -41.295 1.00 21.46 ? 308  GLY A CA    1 
ATOM   6717 C C     . GLY B 1 310 ? 31.553 3.411   -41.180 1.00 20.96 ? 308  GLY A C     1 
ATOM   6718 O O     . GLY B 1 310 ? 32.018 3.657   -40.063 1.00 20.89 ? 308  GLY A O     1 
ATOM   6719 N N     . GLU B 1 311 ? 31.915 4.054   -42.288 1.00 20.33 ? 309  GLU A N     1 
ATOM   6720 C CA    . GLU B 1 311 ? 32.907 5.155   -42.269 1.00 21.46 ? 309  GLU A CA    1 
ATOM   6721 C C     . GLU B 1 311 ? 32.350 6.288   -41.405 1.00 21.94 ? 309  GLU A C     1 
ATOM   6722 O O     . GLU B 1 311 ? 33.083 6.771   -40.526 1.00 20.42 ? 309  GLU A O     1 
ATOM   6723 C CB    . GLU B 1 311 ? 33.276 5.601   -43.682 1.00 23.86 ? 309  GLU A CB    1 
ATOM   6724 C CG    . GLU B 1 311 ? 33.991 6.939   -43.715 1.00 24.05 ? 309  GLU A CG    1 
ATOM   6725 C CD    . GLU B 1 311 ? 35.399 6.934   -43.143 1.00 24.93 ? 309  GLU A CD    1 
ATOM   6726 O OE1   . GLU B 1 311 ? 36.040 5.858   -43.118 1.00 25.25 ? 309  GLU A OE1   1 
ATOM   6727 O OE2   . GLU B 1 311 ? 35.848 7.999   -42.721 1.00 25.07 ? 309  GLU A OE2   1 
ATOM   6728 N N     . ARG B 1 312 ? 31.080 6.651   -41.584 1.00 20.83 ? 310  ARG A N     1 
ATOM   6729 C CA    . ARG B 1 312 ? 30.468 7.758   -40.824 1.00 22.09 ? 310  ARG A CA    1 
ATOM   6730 C C     . ARG B 1 312 ? 30.442 7.408   -39.325 1.00 21.80 ? 310  ARG A C     1 
ATOM   6731 O O     . ARG B 1 312 ? 30.736 8.281   -38.498 1.00 22.89 ? 310  ARG A O     1 
ATOM   6732 C CB    . ARG B 1 312 ? 29.068 8.061   -41.360 1.00 23.15 ? 310  ARG A CB    1 
ATOM   6733 C CG    . ARG B 1 312 ? 28.417 9.245   -40.659 1.00 25.36 ? 310  ARG A CG    1 
ATOM   6734 C CD    . ARG B 1 312 ? 29.079 10.554  -41.049 1.00 29.10 ? 310  ARG A CD    1 
ATOM   6735 N NE    . ARG B 1 312 ? 28.577 11.695  -40.266 1.00 32.46 ? 310  ARG A NE    1 
ATOM   6736 C CZ    . ARG B 1 312 ? 28.975 11.974  -39.020 1.00 39.46 ? 310  ARG A CZ    1 
ATOM   6737 N NH1   . ARG B 1 312 ? 28.464 13.029  -38.404 1.00 43.39 ? 310  ARG A NH1   1 
ATOM   6738 N NH2   . ARG B 1 312 ? 29.874 11.215  -38.387 1.00 35.78 ? 310  ARG A NH2   1 
ATOM   6739 N N     . SER B 1 313 ? 30.150 6.149   -38.984 1.00 22.91 ? 311  SER A N     1 
ATOM   6740 C CA    . SER B 1 313 ? 30.102 5.695   -37.565 1.00 23.75 ? 311  SER A CA    1 
ATOM   6741 C C     . SER B 1 313 ? 31.490 5.773   -36.923 1.00 24.86 ? 311  SER A C     1 
ATOM   6742 O O     . SER B 1 313 ? 31.573 6.136   -35.759 1.00 22.41 ? 311  SER A O     1 
ATOM   6743 C CB    . SER B 1 313 ? 29.519 4.290   -37.415 1.00 22.83 ? 311  SER A CB    1 
ATOM   6744 O OG    . SER B 1 313 ? 29.424 3.912   -36.056 1.00 22.28 ? 311  SER A OG    1 
ATOM   6745 N N     . TYR B 1 314 ? 32.530 5.398   -37.676 1.00 23.58 ? 312  TYR A N     1 
ATOM   6746 C CA    . TYR B 1 314 ? 33.908 5.434   -37.129 1.00 22.38 ? 312  TYR A CA    1 
ATOM   6747 C C     . TYR B 1 314 ? 34.286 6.878   -36.787 1.00 22.13 ? 312  TYR A C     1 
ATOM   6748 O O     . TYR B 1 314 ? 34.872 7.104   -35.747 1.00 25.26 ? 312  TYR A O     1 
ATOM   6749 C CB    . TYR B 1 314 ? 34.940 4.851   -38.095 1.00 22.67 ? 312  TYR A CB    1 
ATOM   6750 C CG    . TYR B 1 314 ? 36.337 4.862   -37.533 1.00 21.64 ? 312  TYR A CG    1 
ATOM   6751 C CD1   . TYR B 1 314 ? 36.749 3.898   -36.632 1.00 22.97 ? 312  TYR A CD1   1 
ATOM   6752 C CD2   . TYR B 1 314 ? 37.232 5.864   -37.863 1.00 24.93 ? 312  TYR A CD2   1 
ATOM   6753 C CE1   . TYR B 1 314 ? 38.023 3.912   -36.093 1.00 22.95 ? 312  TYR A CE1   1 
ATOM   6754 C CE2   . TYR B 1 314 ? 38.509 5.895   -37.333 1.00 23.68 ? 312  TYR A CE2   1 
ATOM   6755 C CZ    . TYR B 1 314 ? 38.906 4.915   -36.444 1.00 24.33 ? 312  TYR A CZ    1 
ATOM   6756 O OH    . TYR B 1 314 ? 40.164 4.939   -35.920 1.00 27.11 ? 312  TYR A OH    1 
ATOM   6757 N N     . GLN B 1 315 ? 33.957 7.807   -37.669 1.00 21.73 ? 313  GLN A N     1 
ATOM   6758 C CA    . GLN B 1 315 ? 34.332 9.223   -37.434 1.00 22.93 ? 313  GLN A CA    1 
ATOM   6759 C C     . GLN B 1 315 ? 33.710 9.688   -36.112 1.00 26.14 ? 313  GLN A C     1 
ATOM   6760 O O     . GLN B 1 315 ? 34.386 10.377  -35.353 1.00 21.74 ? 313  GLN A O     1 
ATOM   6761 C CB    . GLN B 1 315 ? 33.889 10.091  -38.608 1.00 24.75 ? 313  GLN A CB    1 
ATOM   6762 C CG    . GLN B 1 315 ? 34.755 9.925   -39.848 1.00 26.00 ? 313  GLN A CG    1 
ATOM   6763 C CD    . GLN B 1 315 ? 34.413 10.908  -40.941 1.00 23.91 ? 313  GLN A CD    1 
ATOM   6764 O OE1   . GLN B 1 315 ? 34.044 12.050  -40.687 1.00 25.18 ? 313  GLN A OE1   1 
ATOM   6765 N NE2   . GLN B 1 315 ? 34.543 10.466  -42.179 1.00 26.88 ? 313  GLN A NE2   1 
ATOM   6766 N N     . SER B 1 316 ? 32.448 9.335   -35.886 1.00 24.57 ? 314  SER A N     1 
ATOM   6767 C CA    . SER B 1 316 ? 31.779 9.664   -34.595 1.00 23.53 ? 314  SER A CA    1 
ATOM   6768 C C     . SER B 1 316 ? 32.449 8.920   -33.446 1.00 23.45 ? 314  SER A C     1 
ATOM   6769 O O     . SER B 1 316 ? 32.584 9.528   -32.343 1.00 24.14 ? 314  SER A O     1 
ATOM   6770 C CB    . SER B 1 316 ? 30.301 9.379   -34.653 1.00 23.40 ? 314  SER A CB    1 
ATOM   6771 O OG    . SER B 1 316 ? 29.656 10.338  -35.489 1.00 22.24 ? 314  SER A OG    1 
ATOM   6772 N N     . ALA B 1 317 ? 32.768 7.646   -33.651 1.00 20.40 ? 315  ALA A N     1 
ATOM   6773 C CA    . ALA B 1 317 ? 33.284 6.810   -32.551 1.00 20.69 ? 315  ALA A CA    1 
ATOM   6774 C C     . ALA B 1 317 ? 34.686 7.226   -32.103 1.00 20.35 ? 315  ALA A C     1 
ATOM   6775 O O     . ALA B 1 317 ? 34.938 7.176   -30.909 1.00 23.14 ? 315  ALA A O     1 
ATOM   6776 C CB    . ALA B 1 317 ? 33.270 5.366   -32.959 1.00 20.16 ? 315  ALA A CB    1 
ATOM   6777 N N     . ILE B 1 318 ? 35.564 7.570   -33.034 1.00 21.29 ? 316  ILE A N     1 
ATOM   6778 C CA    . ILE B 1 318 ? 36.963 7.888   -32.625 1.00 22.39 ? 316  ILE A CA    1 
ATOM   6779 C C     . ILE B 1 318 ? 36.965 9.232   -31.874 1.00 22.68 ? 316  ILE A C     1 
ATOM   6780 O O     . ILE B 1 318 ? 37.704 9.370   -30.911 1.00 20.73 ? 316  ILE A O     1 
ATOM   6781 C CB    . ILE B 1 318 ? 37.932 7.877   -33.829 1.00 22.81 ? 316  ILE A CB    1 
ATOM   6782 C CG1   . ILE B 1 318 ? 39.381 8.053   -33.370 1.00 22.26 ? 316  ILE A CG1   1 
ATOM   6783 C CG2   . ILE B 1 318 ? 37.535 8.895   -34.886 1.00 21.08 ? 316  ILE A CG2   1 
ATOM   6784 C CD1   . ILE B 1 318 ? 39.781 7.111   -32.266 1.00 23.25 ? 316  ILE A CD1   1 
ATOM   6785 N N     . GLU B 1 319 ? 36.147 10.172  -32.334 1.00 23.82 ? 317  GLU A N     1 
ATOM   6786 C CA    . GLU B 1 319 ? 36.070 11.488  -31.663 1.00 26.53 ? 317  GLU A CA    1 
ATOM   6787 C C     . GLU B 1 319 ? 35.547 11.273  -30.244 1.00 26.35 ? 317  GLU A C     1 
ATOM   6788 O O     . GLU B 1 319 ? 36.108 11.848  -29.322 1.00 25.61 ? 317  GLU A O     1 
ATOM   6789 C CB    . GLU B 1 319 ? 35.169 12.422  -32.461 1.00 30.29 ? 317  GLU A CB    1 
ATOM   6790 C CG    . GLU B 1 319 ? 35.062 13.809  -31.867 1.00 35.11 ? 317  GLU A CG    1 
ATOM   6791 C CD    . GLU B 1 319 ? 34.362 14.798  -32.778 1.00 38.37 ? 317  GLU A CD    1 
ATOM   6792 O OE1   . GLU B 1 319 ? 33.319 15.330  -32.372 1.00 48.06 ? 317  GLU A OE1   1 
ATOM   6793 O OE2   . GLU B 1 319 ? 34.856 15.018  -33.893 1.00 45.74 ? 317  GLU A OE2   1 
ATOM   6794 N N     . TYR B 1 320 ? 34.529 10.428  -30.110 1.00 24.00 ? 318  TYR A N     1 
ATOM   6795 C CA    . TYR B 1 320 ? 33.931 10.121  -28.793 1.00 25.10 ? 318  TYR A CA    1 
ATOM   6796 C C     . TYR B 1 320 ? 34.923 9.371   -27.911 1.00 26.63 ? 318  TYR A C     1 
ATOM   6797 O O     . TYR B 1 320 ? 35.000 9.687   -26.725 1.00 25.79 ? 318  TYR A O     1 
ATOM   6798 C CB    . TYR B 1 320 ? 32.680 9.258   -28.940 1.00 24.31 ? 318  TYR A CB    1 
ATOM   6799 C CG    . TYR B 1 320 ? 31.839 9.247   -27.692 1.00 23.56 ? 318  TYR A CG    1 
ATOM   6800 C CD1   . TYR B 1 320 ? 31.075 10.354  -27.336 1.00 24.29 ? 318  TYR A CD1   1 
ATOM   6801 C CD2   . TYR B 1 320 ? 31.839 8.151   -26.847 1.00 22.08 ? 318  TYR A CD2   1 
ATOM   6802 C CE1   . TYR B 1 320 ? 30.307 10.354  -26.178 1.00 24.30 ? 318  TYR A CE1   1 
ATOM   6803 C CE2   . TYR B 1 320 ? 31.067 8.132   -25.702 1.00 23.08 ? 318  TYR A CE2   1 
ATOM   6804 C CZ    . TYR B 1 320 ? 30.304 9.241   -25.358 1.00 23.68 ? 318  TYR A CZ    1 
ATOM   6805 O OH    . TYR B 1 320 ? 29.555 9.214   -24.202 1.00 25.48 ? 318  TYR A OH    1 
ATOM   6806 N N     . ALA B 1 321 ? 35.648 8.404   -28.466 1.00 24.59 ? 319  ALA A N     1 
ATOM   6807 C CA    . ALA B 1 321 ? 36.567 7.583   -27.653 1.00 24.77 ? 319  ALA A CA    1 
ATOM   6808 C C     . ALA B 1 321 ? 37.744 8.425   -27.132 1.00 25.88 ? 319  ALA A C     1 
ATOM   6809 O O     . ALA B 1 321 ? 38.351 8.028   -26.151 1.00 23.37 ? 319  ALA A O     1 
ATOM   6810 C CB    . ALA B 1 321 ? 37.032 6.383   -28.442 1.00 23.28 ? 319  ALA A CB    1 
ATOM   6811 N N     . ARG B 1 322 ? 38.018 9.551   -27.782 1.00 26.47 ? 320  ARG A N     1 
ATOM   6812 C CA    . ARG B 1 322 ? 39.125 10.436  -27.346 1.00 29.54 ? 320  ARG A CA    1 
ATOM   6813 C C     . ARG B 1 322 ? 38.611 11.466  -26.336 1.00 31.88 ? 320  ARG A C     1 
ATOM   6814 O O     . ARG B 1 322 ? 39.429 11.993  -25.590 1.00 32.54 ? 320  ARG A O     1 
ATOM   6815 C CB    . ARG B 1 322 ? 39.720 11.148  -28.566 1.00 30.91 ? 320  ARG A CB    1 
ATOM   6816 C CG    . ARG B 1 322 ? 40.497 10.247  -29.515 1.00 29.87 ? 320  ARG A CG    1 
ATOM   6817 C CD    . ARG B 1 322 ? 40.772 10.936  -30.838 1.00 30.73 ? 320  ARG A CD    1 
ATOM   6818 N NE    . ARG B 1 322 ? 41.812 10.304  -31.638 1.00 29.99 ? 320  ARG A NE    1 
ATOM   6819 C CZ    . ARG B 1 322 ? 41.921 10.419  -32.956 1.00 29.18 ? 320  ARG A CZ    1 
ATOM   6820 N NH1   . ARG B 1 322 ? 42.901 9.806   -33.596 1.00 28.26 ? 320  ARG A NH1   1 
ATOM   6821 N NH2   . ARG B 1 322 ? 41.055 11.151  -33.630 1.00 28.49 ? 320  ARG A NH2   1 
ATOM   6822 N N     . GLU B 1 323 ? 37.305 11.714  -26.316 1.00 30.00 ? 321  GLU A N     1 
ATOM   6823 C CA    . GLU B 1 323 ? 36.735 12.786  -25.462 1.00 36.02 ? 321  GLU A CA    1 
ATOM   6824 C C     . GLU B 1 323 ? 36.067 12.199  -24.209 1.00 33.55 ? 321  GLU A C     1 
ATOM   6825 O O     . GLU B 1 323 ? 36.282 12.745  -23.131 1.00 31.15 ? 321  GLU A O     1 
ATOM   6826 C CB    . GLU B 1 323 ? 35.762 13.618  -26.289 1.00 41.14 ? 321  GLU A CB    1 
ATOM   6827 C CG    . GLU B 1 323 ? 36.431 14.322  -27.453 1.00 50.01 ? 321  GLU A CG    1 
ATOM   6828 C CD    . GLU B 1 323 ? 35.555 15.267  -28.259 1.00 52.77 ? 321  GLU A CD    1 
ATOM   6829 O OE1   . GLU B 1 323 ? 36.088 15.923  -29.174 1.00 52.78 ? 321  GLU A OE1   1 
ATOM   6830 O OE2   . GLU B 1 323 ? 34.346 15.341  -27.973 1.00 51.35 ? 321  GLU A OE2   1 
ATOM   6831 N N     . ARG B 1 324 ? 35.301 11.122  -24.362 1.00 31.05 ? 322  ARG A N     1 
ATOM   6832 C CA    . ARG B 1 324 ? 34.647 10.462  -23.189 1.00 30.42 ? 322  ARG A CA    1 
ATOM   6833 C C     . ARG B 1 324 ? 35.717 9.897   -22.252 1.00 30.30 ? 322  ARG A C     1 
ATOM   6834 O O     . ARG B 1 324 ? 36.519 9.062   -22.700 1.00 30.16 ? 322  ARG A O     1 
ATOM   6835 C CB    . ARG B 1 324 ? 33.698 9.350   -23.636 1.00 30.20 ? 322  ARG A CB    1 
ATOM   6836 C CG    . ARG B 1 324 ? 32.939 8.655   -22.510 1.00 29.54 ? 322  ARG A CG    1 
ATOM   6837 C CD    . ARG B 1 324 ? 32.074 9.559   -21.626 1.00 27.33 ? 322  ARG A CD    1 
ATOM   6838 N NE    . ARG B 1 324 ? 31.362 8.739   -20.646 1.00 27.98 ? 322  ARG A NE    1 
ATOM   6839 C CZ    . ARG B 1 324 ? 30.372 9.169   -19.848 1.00 29.43 ? 322  ARG A CZ    1 
ATOM   6840 N NH1   . ARG B 1 324 ? 29.751 8.323   -19.050 1.00 27.54 ? 322  ARG A NH1   1 
ATOM   6841 N NH2   . ARG B 1 324 ? 29.995 10.436  -19.863 1.00 30.68 ? 322  ARG A NH2   1 
ATOM   6842 N N     . ILE B 1 325 ? 35.705 10.309  -20.977 1.00 28.70 ? 323  ILE A N     1 
ATOM   6843 C CA    . ILE B 1 325 ? 36.610 9.739   -19.940 1.00 29.21 ? 323  ILE A CA    1 
ATOM   6844 C C     . ILE B 1 325 ? 35.782 8.846   -19.032 1.00 28.63 ? 323  ILE A C     1 
ATOM   6845 O O     . ILE B 1 325 ? 34.642 9.226   -18.670 1.00 30.35 ? 323  ILE A O     1 
ATOM   6846 C CB    . ILE B 1 325 ? 37.395 10.832  -19.175 1.00 32.56 ? 323  ILE A CB    1 
ATOM   6847 C CG1   . ILE B 1 325 ? 36.493 11.792  -18.387 1.00 33.74 ? 323  ILE A CG1   1 
ATOM   6848 C CG2   . ILE B 1 325 ? 38.309 11.562  -20.156 1.00 31.73 ? 323  ILE A CG2   1 
ATOM   6849 C CD1   . ILE B 1 325 ? 37.237 12.721  -17.418 1.00 38.11 ? 323  ILE A CD1   1 
ATOM   6850 N N     . GLN B 1 326 ? 36.323 7.676   -18.709 1.00 26.77 ? 324  GLN A N     1 
ATOM   6851 C CA    . GLN B 1 326 ? 35.640 6.690   -17.852 1.00 27.27 ? 324  GLN A CA    1 
ATOM   6852 C C     . GLN B 1 326 ? 36.649 5.628   -17.419 1.00 28.08 ? 324  GLN A C     1 
ATOM   6853 O O     . GLN B 1 326 ? 37.261 5.030   -18.295 1.00 29.05 ? 324  GLN A O     1 
ATOM   6854 C CB    . GLN B 1 326 ? 34.448 6.090   -18.613 1.00 27.77 ? 324  GLN A CB    1 
ATOM   6855 C CG    . GLN B 1 326 ? 33.426 5.445   -17.698 1.00 25.42 ? 324  GLN A CG    1 
ATOM   6856 C CD    . GLN B 1 326 ? 32.598 6.473   -16.966 1.00 25.00 ? 324  GLN A CD    1 
ATOM   6857 O OE1   . GLN B 1 326 ? 32.685 7.696   -17.155 1.00 26.58 ? 324  GLN A OE1   1 
ATOM   6858 N NE2   . GLN B 1 326 ? 31.732 5.968   -16.131 1.00 26.61 ? 324  GLN A NE2   1 
ATOM   6859 N N     . SER B 1 327 ? 36.808 5.418   -16.112 1.00 26.63 ? 325  SER A N     1 
ATOM   6860 C CA    . SER B 1 327 ? 37.700 4.411   -15.508 1.00 27.00 ? 325  SER A CA    1 
ATOM   6861 C C     . SER B 1 327 ? 39.152 4.783   -15.849 1.00 29.59 ? 325  SER A C     1 
ATOM   6862 O O     . SER B 1 327 ? 39.387 5.918   -16.336 1.00 33.72 ? 325  SER A O     1 
ATOM   6863 C CB    . SER B 1 327 ? 37.345 3.014   -15.961 1.00 30.04 ? 325  SER A CB    1 
ATOM   6864 O OG    . SER B 1 327 ? 35.928 2.788   -15.982 1.00 35.58 ? 325  SER A OG    1 
ATOM   6865 N N     . ARG B 1 328 ? 40.080 3.862   -15.606 1.00 29.90 ? 326  ARG A N     1 
ATOM   6866 C CA    . ARG B 1 328 ? 41.544 4.039   -15.777 1.00 30.61 ? 326  ARG A CA    1 
ATOM   6867 C C     . ARG B 1 328 ? 42.062 2.882   -16.637 1.00 30.00 ? 326  ARG A C     1 
ATOM   6868 O O     . ARG B 1 328 ? 41.534 1.778   -16.518 1.00 25.76 ? 326  ARG A O     1 
ATOM   6869 C CB    . ARG B 1 328 ? 42.212 4.096   -14.392 1.00 32.56 ? 326  ARG A CB    1 
ATOM   6870 C CG    . ARG B 1 328 ? 41.774 5.295   -13.546 1.00 31.20 ? 326  ARG A CG    1 
ATOM   6871 C CD    . ARG B 1 328 ? 42.169 6.618   -14.195 1.00 33.00 ? 326  ARG A CD    1 
ATOM   6872 N NE    . ARG B 1 328 ? 42.228 7.751   -13.269 1.00 35.01 ? 326  ARG A NE    1 
ATOM   6873 C CZ    . ARG B 1 328 ? 42.524 9.006   -13.595 1.00 36.59 ? 326  ARG A CZ    1 
ATOM   6874 N NH1   . ARG B 1 328 ? 42.799 9.332   -14.846 1.00 36.76 ? 326  ARG A NH1   1 
ATOM   6875 N NH2   . ARG B 1 328 ? 42.541 9.942   -12.656 1.00 37.99 ? 326  ARG A NH2   1 
ATOM   6876 N N     . ALA B 1 329 ? 43.072 3.137   -17.463 1.00 28.73 ? 327  ALA A N     1 
ATOM   6877 C CA    . ALA B 1 329 ? 43.757 2.094   -18.249 1.00 31.28 ? 327  ALA A CA    1 
ATOM   6878 C C     . ALA B 1 329 ? 44.167 0.964   -17.318 1.00 31.30 ? 327  ALA A C     1 
ATOM   6879 O O     . ALA B 1 329 ? 44.605 1.199   -16.194 1.00 29.87 ? 327  ALA A O     1 
ATOM   6880 C CB    . ALA B 1 329 ? 44.957 2.663   -18.968 1.00 31.80 ? 327  ALA A CB    1 
ATOM   6881 N N     . PRO B 1 330 ? 44.106 -0.295  -17.781 1.00 29.73 ? 328  PRO A N     1 
ATOM   6882 C CA    . PRO B 1 330 ? 44.532 -1.422  -16.962 1.00 30.97 ? 328  PRO A CA    1 
ATOM   6883 C C     . PRO B 1 330 ? 46.000 -1.341  -16.503 1.00 30.15 ? 328  PRO A C     1 
ATOM   6884 O O     . PRO B 1 330 ? 46.268 -1.872  -15.448 1.00 27.83 ? 328  PRO A O     1 
ATOM   6885 C CB    . PRO B 1 330 ? 44.373 -2.656  -17.870 1.00 30.96 ? 328  PRO A CB    1 
ATOM   6886 C CG    . PRO B 1 330 ? 43.512 -2.204  -19.029 1.00 31.65 ? 328  PRO A CG    1 
ATOM   6887 C CD    . PRO B 1 330 ? 43.656 -0.697  -19.124 1.00 33.59 ? 328  PRO A CD    1 
ATOM   6888 N N     . THR B 1 331 ? 46.905 -0.725  -17.286 1.00 29.87 ? 329  THR A N     1 
ATOM   6889 C CA    . THR B 1 331 ? 48.346 -0.592  -16.918 1.00 34.07 ? 329  THR A CA    1 
ATOM   6890 C C     . THR B 1 331 ? 48.555 0.651   -16.033 1.00 39.47 ? 329  THR A C     1 
ATOM   6891 O O     . THR B 1 331 ? 49.710 0.901   -15.639 1.00 39.27 ? 329  THR A O     1 
ATOM   6892 C CB    . THR B 1 331 ? 49.284 -0.576  -18.128 1.00 31.98 ? 329  THR A CB    1 
ATOM   6893 O OG1   . THR B 1 331 ? 49.003 0.578   -18.916 1.00 32.86 ? 329  THR A OG1   1 
ATOM   6894 C CG2   . THR B 1 331 ? 49.198 -1.833  -18.960 1.00 29.96 ? 329  THR A CG2   1 
ATOM   6895 N N     . GLY B 1 332 ? 47.480 1.366   -15.684 1.00 35.81 ? 330  GLY A N     1 
ATOM   6896 C CA    . GLY B 1 332 ? 47.532 2.473   -14.714 1.00 37.00 ? 330  GLY A CA    1 
ATOM   6897 C C     . GLY B 1 332 ? 47.124 3.801   -15.338 1.00 36.12 ? 330  GLY A C     1 
ATOM   6898 O O     . GLY B 1 332 ? 47.181 3.972   -16.567 1.00 36.61 ? 330  GLY A O     1 
ATOM   6899 N N     . PRO B 1 333 ? 46.716 4.780   -14.493 1.00 40.33 ? 331  PRO A N     1 
ATOM   6900 C CA    . PRO B 1 333 ? 46.193 6.064   -14.967 1.00 38.91 ? 331  PRO A CA    1 
ATOM   6901 C C     . PRO B 1 333 ? 47.068 6.660   -16.076 1.00 40.17 ? 331  PRO A C     1 
ATOM   6902 O O     . PRO B 1 333 ? 48.274 6.746   -15.894 1.00 39.03 ? 331  PRO A O     1 
ATOM   6903 C CB    . PRO B 1 333 ? 46.190 6.941   -13.704 1.00 41.11 ? 331  PRO A CB    1 
ATOM   6904 C CG    . PRO B 1 333 ? 45.999 5.947   -12.570 1.00 42.19 ? 331  PRO A CG    1 
ATOM   6905 C CD    . PRO B 1 333 ? 46.743 4.706   -13.018 1.00 40.99 ? 331  PRO A CD    1 
ATOM   6906 N N     . VAL B 1 334 ? 46.432 7.005   -17.199 1.00 37.28 ? 332  VAL A N     1 
ATOM   6907 C CA    . VAL B 1 334 ? 47.079 7.603   -18.399 1.00 38.75 ? 332  VAL A CA    1 
ATOM   6908 C C     . VAL B 1 334 ? 46.915 9.125   -18.354 1.00 39.22 ? 332  VAL A C     1 
ATOM   6909 O O     . VAL B 1 334 ? 47.858 9.802   -18.769 1.00 38.06 ? 332  VAL A O     1 
ATOM   6910 C CB    . VAL B 1 334 ? 46.482 7.002   -19.687 1.00 40.01 ? 332  VAL A CB    1 
ATOM   6911 C CG1   . VAL B 1 334 ? 46.770 7.863   -20.911 1.00 40.81 ? 332  VAL A CG1   1 
ATOM   6912 C CG2   . VAL B 1 334 ? 46.965 5.570   -19.906 1.00 37.78 ? 332  VAL A CG2   1 
ATOM   6913 N N     . ALA B 1 335 ? 45.742 9.628   -17.938 1.00 40.08 ? 333  ALA A N     1 
ATOM   6914 C CA    . ALA B 1 335 ? 45.374 11.067  -17.885 1.00 40.00 ? 333  ALA A CA    1 
ATOM   6915 C C     . ALA B 1 335 ? 45.361 11.527  -16.421 1.00 38.50 ? 333  ALA A C     1 
ATOM   6916 O O     . ALA B 1 335 ? 44.269 11.729  -15.835 1.00 37.08 ? 333  ALA A O     1 
ATOM   6917 C CB    . ALA B 1 335 ? 44.037 11.295  -18.559 1.00 39.46 ? 333  ALA A CB    1 
ATOM   6918 N N     . LYS B 1 336 ? 46.555 11.690  -15.860 1.00 43.40 ? 334  LYS A N     1 
ATOM   6919 C CA    . LYS B 1 336 ? 46.799 12.011  -14.429 1.00 49.57 ? 334  LYS A CA    1 
ATOM   6920 C C     . LYS B 1 336 ? 46.169 13.367  -14.072 1.00 44.26 ? 334  LYS A C     1 
ATOM   6921 O O     . LYS B 1 336 ? 45.753 13.549  -12.921 1.00 48.60 ? 334  LYS A O     1 
ATOM   6922 C CB    . LYS B 1 336 ? 48.311 11.988  -14.187 1.00 54.96 ? 334  LYS A CB    1 
ATOM   6923 C CG    . LYS B 1 336 ? 48.966 10.617  -14.315 1.00 60.96 ? 334  LYS A CG    1 
ATOM   6924 C CD    . LYS B 1 336 ? 48.820 9.765   -13.059 1.00 66.17 ? 334  LYS A CD    1 
ATOM   6925 C CE    . LYS B 1 336 ? 50.122 9.155   -12.575 1.00 68.76 ? 334  LYS A CE    1 
ATOM   6926 N NZ    . LYS B 1 336 ? 50.832 8.436   -13.659 1.00 71.73 ? 334  LYS A NZ    1 
ATOM   6927 N N     . ASP B 1 337 ? 46.079 14.278  -15.037 1.00 45.10 ? 335  ASP A N     1 
ATOM   6928 C CA    . ASP B 1 337 ? 45.495 15.642  -14.881 1.00 46.43 ? 335  ASP A CA    1 
ATOM   6929 C C     . ASP B 1 337 ? 43.958 15.599  -14.765 1.00 45.86 ? 335  ASP A C     1 
ATOM   6930 O O     . ASP B 1 337 ? 43.355 16.667  -14.519 1.00 39.51 ? 335  ASP A O     1 
ATOM   6931 C CB    . ASP B 1 337 ? 45.942 16.530  -16.049 1.00 50.51 ? 335  ASP A CB    1 
ATOM   6932 C CG    . ASP B 1 337 ? 45.687 15.920  -17.426 1.00 52.24 ? 335  ASP A CG    1 
ATOM   6933 O OD1   . ASP B 1 337 ? 45.906 14.704  -17.596 1.00 52.63 ? 335  ASP A OD1   1 
ATOM   6934 O OD2   . ASP B 1 337 ? 45.267 16.664  -18.312 1.00 56.01 ? 335  ASP A OD2   1 
ATOM   6935 N N     . LYS B 1 338 ? 43.326 14.427  -14.920 1.00 46.51 ? 336  LYS A N     1 
ATOM   6936 C CA    . LYS B 1 338 ? 41.845 14.308  -15.016 1.00 45.77 ? 336  LYS A CA    1 
ATOM   6937 C C     . LYS B 1 338 ? 41.344 13.244  -14.046 1.00 43.96 ? 336  LYS A C     1 
ATOM   6938 O O     . LYS B 1 338 ? 42.190 12.485  -13.544 1.00 43.60 ? 336  LYS A O     1 
ATOM   6939 C CB    . LYS B 1 338 ? 41.421 13.904  -16.430 1.00 49.86 ? 336  LYS A CB    1 
ATOM   6940 C CG    . LYS B 1 338 ? 41.746 14.902  -17.536 1.00 52.95 ? 336  LYS A CG    1 
ATOM   6941 C CD    . LYS B 1 338 ? 40.778 14.781  -18.700 1.00 56.51 ? 336  LYS A CD    1 
ATOM   6942 C CE    . LYS B 1 338 ? 41.415 14.339  -19.998 1.00 64.95 ? 336  LYS A CE    1 
ATOM   6943 N NZ    . LYS B 1 338 ? 41.722 15.515  -20.841 1.00 67.54 ? 336  LYS A NZ    1 
ATOM   6944 N N     . ALA B 1 339 ? 40.017 13.150  -13.877 1.00 42.00 ? 337  ALA A N     1 
ATOM   6945 C CA    . ALA B 1 339 ? 39.338 12.223  -12.942 1.00 38.48 ? 337  ALA A CA    1 
ATOM   6946 C C     . ALA B 1 339 ? 39.248 10.812  -13.525 1.00 37.05 ? 337  ALA A C     1 
ATOM   6947 O O     . ALA B 1 339 ? 38.846 9.891   -12.791 1.00 38.58 ? 337  ALA A O     1 
ATOM   6948 C CB    . ALA B 1 339 ? 37.963 12.744  -12.605 1.00 40.20 ? 337  ALA A CB    1 
ATOM   6949 N N     . ALA B 1 340 ? 39.512 10.648  -14.821 1.00 36.28 ? 338  ALA A N     1 
ATOM   6950 C CA    . ALA B 1 340 ? 39.404 9.347   -15.521 1.00 31.37 ? 338  ALA A CA    1 
ATOM   6951 C C     . ALA B 1 340 ? 40.158 9.430   -16.847 1.00 29.61 ? 338  ALA A C     1 
ATOM   6952 O O     . ALA B 1 340 ? 40.526 10.554  -17.268 1.00 27.51 ? 338  ALA A O     1 
ATOM   6953 C CB    . ALA B 1 340 ? 37.953 8.971   -15.723 1.00 30.90 ? 338  ALA A CB    1 
ATOM   6954 N N     . ASP B 1 341 ? 40.364 8.281   -17.493 1.00 28.56 ? 339  ASP A N     1 
ATOM   6955 C CA    . ASP B 1 341 ? 41.116 8.199   -18.770 1.00 28.03 ? 339  ASP A CA    1 
ATOM   6956 C C     . ASP B 1 341 ? 40.162 8.181   -19.958 1.00 26.72 ? 339  ASP A C     1 
ATOM   6957 O O     . ASP B 1 341 ? 39.069 7.626   -19.877 1.00 27.89 ? 339  ASP A O     1 
ATOM   6958 C CB    . ASP B 1 341 ? 41.985 6.945   -18.814 1.00 29.11 ? 339  ASP A CB    1 
ATOM   6959 C CG    . ASP B 1 341 ? 43.125 6.985   -17.822 1.00 31.65 ? 339  ASP A CG    1 
ATOM   6960 O OD1   . ASP B 1 341 ? 43.387 8.085   -17.292 1.00 29.83 ? 339  ASP A OD1   1 
ATOM   6961 O OD2   . ASP B 1 341 ? 43.733 5.912   -17.592 1.00 32.76 ? 339  ASP A OD2   1 
ATOM   6962 N N     . PRO B 1 342 ? 40.574 8.761   -21.103 1.00 27.59 ? 340  PRO A N     1 
ATOM   6963 C CA    . PRO B 1 342 ? 39.801 8.655   -22.339 1.00 25.90 ? 340  PRO A CA    1 
ATOM   6964 C C     . PRO B 1 342 ? 39.582 7.162   -22.634 1.00 24.84 ? 340  PRO A C     1 
ATOM   6965 O O     . PRO B 1 342 ? 40.490 6.363   -22.421 1.00 24.83 ? 340  PRO A O     1 
ATOM   6966 C CB    . PRO B 1 342 ? 40.644 9.390   -23.395 1.00 29.04 ? 340  PRO A CB    1 
ATOM   6967 C CG    . PRO B 1 342 ? 42.009 9.639   -22.770 1.00 32.38 ? 340  PRO A CG    1 
ATOM   6968 C CD    . PRO B 1 342 ? 41.823 9.533   -21.272 1.00 32.02 ? 340  PRO A CD    1 
ATOM   6969 N N     . ILE B 1 343 ? 38.356 6.791   -23.006 1.00 23.06 ? 341  ILE A N     1 
ATOM   6970 C CA    . ILE B 1 343 ? 37.989 5.342   -23.120 1.00 23.06 ? 341  ILE A CA    1 
ATOM   6971 C C     . ILE B 1 343 ? 38.806 4.589   -24.179 1.00 22.33 ? 341  ILE A C     1 
ATOM   6972 O O     . ILE B 1 343 ? 38.798 3.357   -24.137 1.00 21.55 ? 341  ILE A O     1 
ATOM   6973 C CB    . ILE B 1 343 ? 36.472 5.208   -23.342 1.00 24.59 ? 341  ILE A CB    1 
ATOM   6974 C CG1   . ILE B 1 343 ? 35.990 6.066   -24.513 1.00 23.89 ? 341  ILE A CG1   1 
ATOM   6975 C CG2   . ILE B 1 343 ? 35.714 5.526   -22.064 1.00 25.02 ? 341  ILE A CG2   1 
ATOM   6976 C CD1   . ILE B 1 343 ? 34.597 5.732   -24.981 1.00 26.71 ? 341  ILE A CD1   1 
ATOM   6977 N N     . ILE B 1 344 ? 39.507 5.307   -25.049 1.00 23.99 ? 342  ILE A N     1 
ATOM   6978 C CA    . ILE B 1 344 ? 40.387 4.650   -26.062 1.00 23.91 ? 342  ILE A CA    1 
ATOM   6979 C C     . ILE B 1 344 ? 41.487 3.830   -25.367 1.00 25.30 ? 342  ILE A C     1 
ATOM   6980 O O     . ILE B 1 344 ? 42.072 2.971   -26.010 1.00 23.65 ? 342  ILE A O     1 
ATOM   6981 C CB    . ILE B 1 344 ? 40.963 5.688   -27.040 1.00 25.51 ? 342  ILE A CB    1 
ATOM   6982 C CG1   . ILE B 1 344 ? 41.676 5.020   -28.219 1.00 25.99 ? 342  ILE A CG1   1 
ATOM   6983 C CG2   . ILE B 1 344 ? 41.859 6.678   -26.315 1.00 26.11 ? 342  ILE A CG2   1 
ATOM   6984 C CD1   . ILE B 1 344 ? 41.835 5.917   -29.417 1.00 30.64 ? 342  ILE A CD1   1 
ATOM   6985 N N     . VAL B 1 345 ? 41.736 4.084   -24.082 1.00 25.00 ? 343  VAL A N     1 
ATOM   6986 C CA    . VAL B 1 345 ? 42.802 3.352   -23.347 1.00 22.96 ? 343  VAL A CA    1 
ATOM   6987 C C     . VAL B 1 345 ? 42.383 1.903   -23.113 1.00 22.70 ? 343  VAL A C     1 
ATOM   6988 O O     . VAL B 1 345 ? 43.264 1.080   -22.896 1.00 21.47 ? 343  VAL A O     1 
ATOM   6989 C CB    . VAL B 1 345 ? 43.108 4.035   -21.999 1.00 25.82 ? 343  VAL A CB    1 
ATOM   6990 C CG1   . VAL B 1 345 ? 43.516 5.488   -22.173 1.00 24.31 ? 343  VAL A CG1   1 
ATOM   6991 C CG2   . VAL B 1 345 ? 41.956 3.906   -21.015 1.00 25.57 ? 343  VAL A CG2   1 
ATOM   6992 N N     . HIS B 1 346 ? 41.087 1.619   -23.197 1.00 22.49 ? 344  HIS A N     1 
ATOM   6993 C CA    . HIS B 1 346 ? 40.589 0.281   -22.777 1.00 23.53 ? 344  HIS A CA    1 
ATOM   6994 C C     . HIS B 1 346 ? 40.719 -0.704  -23.925 1.00 23.91 ? 344  HIS A C     1 
ATOM   6995 O O     . HIS B 1 346 ? 40.346 -0.388  -25.045 1.00 23.79 ? 344  HIS A O     1 
ATOM   6996 C CB    . HIS B 1 346 ? 39.147 0.351   -22.243 1.00 25.07 ? 344  HIS A CB    1 
ATOM   6997 C CG    . HIS B 1 346 ? 39.050 1.179   -21.017 1.00 27.21 ? 344  HIS A CG    1 
ATOM   6998 N ND1   . HIS B 1 346 ? 38.306 2.361   -20.973 1.00 27.97 ? 344  HIS A ND1   1 
ATOM   6999 C CD2   . HIS B 1 346 ? 39.688 1.081   -19.834 1.00 26.87 ? 344  HIS A CD2   1 
ATOM   7000 C CE1   . HIS B 1 346 ? 38.463 2.919   -19.790 1.00 25.86 ? 344  HIS A CE1   1 
ATOM   7001 N NE2   . HIS B 1 346 ? 39.288 2.163   -19.079 1.00 27.81 ? 344  HIS A NE2   1 
ATOM   7002 N N     . PRO B 1 347 ? 41.300 -1.896  -23.666 1.00 23.57 ? 345  PRO A N     1 
ATOM   7003 C CA    . PRO B 1 347 ? 41.459 -2.931  -24.668 1.00 23.51 ? 345  PRO A CA    1 
ATOM   7004 C C     . PRO B 1 347 ? 40.205 -3.181  -25.513 1.00 23.90 ? 345  PRO A C     1 
ATOM   7005 O O     . PRO B 1 347 ? 40.327 -3.206  -26.718 1.00 23.22 ? 345  PRO A O     1 
ATOM   7006 C CB    . PRO B 1 347 ? 41.767 -4.177  -23.831 1.00 24.28 ? 345  PRO A CB    1 
ATOM   7007 C CG    . PRO B 1 347 ? 42.480 -3.654  -22.635 1.00 23.85 ? 345  PRO A CG    1 
ATOM   7008 C CD    . PRO B 1 347 ? 41.891 -2.283  -22.380 1.00 23.41 ? 345  PRO A CD    1 
ATOM   7009 N N     . ASP B 1 348 ? 39.036 -3.336  -24.883 1.00 23.28 ? 346  ASP A N     1 
ATOM   7010 C CA    . ASP B 1 348 ? 37.795 -3.687  -25.615 1.00 21.22 ? 346  ASP A CA    1 
ATOM   7011 C C     . ASP B 1 348 ? 37.370 -2.538  -26.521 1.00 21.46 ? 346  ASP A C     1 
ATOM   7012 O O     . ASP B 1 348 ? 36.819 -2.802  -27.623 1.00 21.87 ? 346  ASP A O     1 
ATOM   7013 C CB    . ASP B 1 348 ? 36.680 -4.098  -24.668 1.00 23.27 ? 346  ASP A CB    1 
ATOM   7014 C CG    . ASP B 1 348 ? 35.445 -4.588  -25.381 1.00 23.45 ? 346  ASP A CG    1 
ATOM   7015 O OD1   . ASP B 1 348 ? 35.543 -5.607  -26.112 1.00 23.64 ? 346  ASP A OD1   1 
ATOM   7016 O OD2   . ASP B 1 348 ? 34.399 -3.968  -25.166 1.00 27.47 ? 346  ASP A OD2   1 
ATOM   7017 N N     . VAL B 1 349 ? 37.605 -1.300  -26.100 1.00 21.16 ? 347  VAL A N     1 
ATOM   7018 C CA    . VAL B 1 349 ? 37.258 -0.118  -26.935 1.00 21.80 ? 347  VAL A CA    1 
ATOM   7019 C C     . VAL B 1 349 ? 38.169 -0.102  -28.170 1.00 22.83 ? 347  VAL A C     1 
ATOM   7020 O O     . VAL B 1 349 ? 37.680 0.108   -29.267 1.00 22.83 ? 347  VAL A O     1 
ATOM   7021 C CB    . VAL B 1 349 ? 37.363 1.189   -26.129 1.00 21.82 ? 347  VAL A CB    1 
ATOM   7022 C CG1   . VAL B 1 349 ? 37.138 2.411   -27.003 1.00 21.22 ? 347  VAL A CG1   1 
ATOM   7023 C CG2   . VAL B 1 349 ? 36.409 1.185   -24.944 1.00 21.78 ? 347  VAL A CG2   1 
ATOM   7024 N N     . ARG B 1 350 ? 39.454 -0.352  -27.959 1.00 23.56 ? 348  ARG A N     1 
ATOM   7025 C CA    . ARG B 1 350 ? 40.406 -0.409  -29.091 1.00 25.07 ? 348  ARG A CA    1 
ATOM   7026 C C     . ARG B 1 350 ? 40.002 -1.562  -30.025 1.00 24.02 ? 348  ARG A C     1 
ATOM   7027 O O     . ARG B 1 350 ? 40.035 -1.364  -31.228 1.00 24.07 ? 348  ARG A O     1 
ATOM   7028 C CB    . ARG B 1 350 ? 41.835 -0.528  -28.554 1.00 23.99 ? 348  ARG A CB    1 
ATOM   7029 C CG    . ARG B 1 350 ? 42.451 0.810   -28.175 1.00 24.96 ? 348  ARG A CG    1 
ATOM   7030 C CD    . ARG B 1 350 ? 43.721 0.703   -27.357 1.00 25.62 ? 348  ARG A CD    1 
ATOM   7031 N NE    . ARG B 1 350 ? 44.407 1.985   -27.318 1.00 26.01 ? 348  ARG A NE    1 
ATOM   7032 C CZ    . ARG B 1 350 ? 45.387 2.338   -28.139 1.00 27.21 ? 348  ARG A CZ    1 
ATOM   7033 N NH1   . ARG B 1 350 ? 45.811 1.496   -29.065 1.00 27.89 ? 348  ARG A NH1   1 
ATOM   7034 N NH2   . ARG B 1 350 ? 45.940 3.532   -28.033 1.00 24.68 ? 348  ARG A NH2   1 
ATOM   7035 N N     . ARG B 1 351 ? 39.616 -2.704  -29.460 1.00 22.90 ? 349  ARG A N     1 
ATOM   7036 C CA    . ARG B 1 351 ? 39.172 -3.846  -30.296 1.00 23.19 ? 349  ARG A CA    1 
ATOM   7037 C C     . ARG B 1 351 ? 38.037 -3.408  -31.226 1.00 24.85 ? 349  ARG A C     1 
ATOM   7038 O O     . ARG B 1 351 ? 38.117 -3.670  -32.421 1.00 23.97 ? 349  ARG A O     1 
ATOM   7039 C CB    . ARG B 1 351 ? 38.685 -5.015  -29.445 1.00 24.77 ? 349  ARG A CB    1 
ATOM   7040 C CG    . ARG B 1 351 ? 38.372 -6.272  -30.240 1.00 25.41 ? 349  ARG A CG    1 
ATOM   7041 C CD    . ARG B 1 351 ? 37.729 -7.328  -29.365 1.00 25.95 ? 349  ARG A CD    1 
ATOM   7042 N NE    . ARG B 1 351 ? 36.526 -6.846  -28.707 1.00 25.50 ? 349  ARG A NE    1 
ATOM   7043 C CZ    . ARG B 1 351 ? 35.315 -6.874  -29.243 1.00 26.99 ? 349  ARG A CZ    1 
ATOM   7044 N NH1   . ARG B 1 351 ? 34.279 -6.422  -28.561 1.00 27.44 ? 349  ARG A NH1   1 
ATOM   7045 N NH2   . ARG B 1 351 ? 35.141 -7.354  -30.460 1.00 28.68 ? 349  ARG A NH2   1 
ATOM   7046 N N     . MET B 1 352 ? 37.020 -2.761  -30.668 1.00 23.80 ? 350  MET A N     1 
ATOM   7047 C CA    . MET B 1 352 ? 35.849 -2.337  -31.473 1.00 23.55 ? 350  MET A CA    1 
ATOM   7048 C C     . MET B 1 352 ? 36.271 -1.296  -32.520 1.00 23.58 ? 350  MET A C     1 
ATOM   7049 O O     . MET B 1 352 ? 35.899 -1.435  -33.681 1.00 19.91 ? 350  MET A O     1 
ATOM   7050 C CB    . MET B 1 352 ? 34.776 -1.770  -30.538 1.00 24.42 ? 350  MET A CB    1 
ATOM   7051 C CG    . MET B 1 352 ? 34.105 -2.842  -29.694 1.00 24.38 ? 350  MET A CG    1 
ATOM   7052 S SD    . MET B 1 352 ? 32.682 -2.276  -28.719 1.00 24.00 ? 350  MET A SD    1 
ATOM   7053 C CE    . MET B 1 352 ? 33.515 -1.443  -27.370 1.00 27.60 ? 350  MET A CE    1 
ATOM   7054 N N     . LEU B 1 353 ? 37.039 -0.296  -32.097 1.00 23.58 ? 351  LEU A N     1 
ATOM   7055 C CA    . LEU B 1 353 ? 37.481 0.775   -33.021 1.00 24.05 ? 351  LEU A CA    1 
ATOM   7056 C C     . LEU B 1 353 ? 38.305 0.169   -34.166 1.00 23.93 ? 351  LEU A C     1 
ATOM   7057 O O     . LEU B 1 353 ? 38.086 0.539   -35.308 1.00 22.45 ? 351  LEU A O     1 
ATOM   7058 C CB    . LEU B 1 353 ? 38.328 1.783   -32.245 1.00 25.95 ? 351  LEU A CB    1 
ATOM   7059 C CG    . LEU B 1 353 ? 37.587 2.827   -31.417 1.00 25.64 ? 351  LEU A CG    1 
ATOM   7060 C CD1   . LEU B 1 353 ? 38.540 3.488   -30.434 1.00 27.11 ? 351  LEU A CD1   1 
ATOM   7061 C CD2   . LEU B 1 353 ? 36.945 3.869   -32.314 1.00 24.84 ? 351  LEU A CD2   1 
ATOM   7062 N N     . LEU B 1 354 ? 39.237 -0.714  -33.835 1.00 22.65 ? 352  LEU A N     1 
ATOM   7063 C CA    . LEU B 1 354 ? 40.133 -1.289  -34.867 1.00 23.13 ? 352  LEU A CA    1 
ATOM   7064 C C     . LEU B 1 354 ? 39.356 -2.238  -35.789 1.00 23.97 ? 352  LEU A C     1 
ATOM   7065 O O     . LEU B 1 354 ? 39.719 -2.356  -36.946 1.00 21.57 ? 352  LEU A O     1 
ATOM   7066 C CB    . LEU B 1 354 ? 41.285 -2.000  -34.157 1.00 23.78 ? 352  LEU A CB    1 
ATOM   7067 C CG    . LEU B 1 354 ? 42.339 -1.071  -33.554 1.00 24.39 ? 352  LEU A CG    1 
ATOM   7068 C CD1   . LEU B 1 354 ? 43.273 -1.826  -32.624 1.00 23.83 ? 352  LEU A CD1   1 
ATOM   7069 C CD2   . LEU B 1 354 ? 43.126 -0.368  -34.647 1.00 23.38 ? 352  LEU A CD2   1 
ATOM   7070 N N     . THR B 1 355 ? 38.327 -2.890  -35.256 1.00 24.66 ? 353  THR A N     1 
ATOM   7071 C CA    . THR B 1 355 ? 37.496 -3.764  -36.116 1.00 24.16 ? 353  THR A CA    1 
ATOM   7072 C C     . THR B 1 355 ? 36.837 -2.865  -37.162 1.00 23.98 ? 353  THR A C     1 
ATOM   7073 O O     . THR B 1 355 ? 36.941 -3.167  -38.335 1.00 22.80 ? 353  THR A O     1 
ATOM   7074 C CB    . THR B 1 355 ? 36.553 -4.628  -35.264 1.00 25.53 ? 353  THR A CB    1 
ATOM   7075 O OG1   . THR B 1 355 ? 37.318 -5.427  -34.363 1.00 22.99 ? 353  THR A OG1   1 
ATOM   7076 C CG2   . THR B 1 355 ? 35.660 -5.507  -36.113 1.00 24.28 ? 353  THR A CG2   1 
ATOM   7077 N N     . MET B 1 356 ? 36.235 -1.763  -36.716 1.00 24.34 ? 354  MET A N     1 
ATOM   7078 C CA    . MET B 1 356 ? 35.625 -0.787  -37.647 1.00 23.51 ? 354  MET A CA    1 
ATOM   7079 C C     . MET B 1 356 ? 36.677 -0.285  -38.641 1.00 24.15 ? 354  MET A C     1 
ATOM   7080 O O     . MET B 1 356 ? 36.418 -0.322  -39.837 1.00 19.35 ? 354  MET A O     1 
ATOM   7081 C CB    . MET B 1 356 ? 35.091 0.422   -36.875 1.00 22.98 ? 354  MET A CB    1 
ATOM   7082 C CG    . MET B 1 356 ? 34.041 0.102   -35.825 1.00 23.85 ? 354  MET A CG    1 
ATOM   7083 S SD    . MET B 1 356 ? 33.547 1.595   -34.911 1.00 22.98 ? 354  MET A SD    1 
ATOM   7084 C CE    . MET B 1 356 ? 32.556 2.422   -36.151 1.00 22.12 ? 354  MET A CE    1 
ATOM   7085 N N     . LYS B 1 357 ? 37.818 0.177   -38.132 1.00 23.70 ? 355  LYS A N     1 
ATOM   7086 C CA    . LYS B 1 357 ? 38.866 0.784   -38.994 1.00 22.52 ? 355  LYS A CA    1 
ATOM   7087 C C     . LYS B 1 357 ? 39.356 -0.203  -40.058 1.00 21.68 ? 355  LYS A C     1 
ATOM   7088 O O     . LYS B 1 357 ? 39.481 0.192   -41.212 1.00 23.79 ? 355  LYS A O     1 
ATOM   7089 C CB    . LYS B 1 357 ? 40.008 1.268   -38.098 1.00 23.66 ? 355  LYS A CB    1 
ATOM   7090 C CG    . LYS B 1 357 ? 40.938 2.318   -38.685 1.00 24.84 ? 355  LYS A CG    1 
ATOM   7091 C CD    . LYS B 1 357 ? 42.043 2.691   -37.718 1.00 25.36 ? 355  LYS A CD    1 
ATOM   7092 C CE    . LYS B 1 357 ? 42.896 3.849   -38.187 1.00 26.34 ? 355  LYS A CE    1 
ATOM   7093 N NZ    . LYS B 1 357 ? 43.714 3.483   -39.363 1.00 25.61 ? 355  LYS A NZ    1 
ATOM   7094 N N     . ALA B 1 358 ? 39.615 -1.442  -39.664 1.00 21.70 ? 356  ALA A N     1 
ATOM   7095 C CA    . ALA B 1 358 ? 40.152 -2.444  -40.610 1.00 22.09 ? 356  ALA A CA    1 
ATOM   7096 C C     . ALA B 1 358 ? 39.084 -2.828  -41.644 1.00 22.13 ? 356  ALA A C     1 
ATOM   7097 O O     . ALA B 1 358 ? 39.438 -3.050  -42.796 1.00 21.26 ? 356  ALA A O     1 
ATOM   7098 C CB    . ALA B 1 358 ? 40.641 -3.645  -39.854 1.00 21.52 ? 356  ALA A CB    1 
ATOM   7099 N N     . LEU B 1 359 ? 37.829 -2.910  -41.207 1.00 21.27 ? 357  LEU A N     1 
ATOM   7100 C CA    . LEU B 1 359 ? 36.721 -3.235  -42.141 1.00 20.34 ? 357  LEU A CA    1 
ATOM   7101 C C     . LEU B 1 359 ? 36.468 -2.039  -43.051 1.00 19.25 ? 357  LEU A C     1 
ATOM   7102 O O     . LEU B 1 359 ? 36.259 -2.249  -44.253 1.00 21.71 ? 357  LEU A O     1 
ATOM   7103 C CB    . LEU B 1 359 ? 35.459 -3.642  -41.362 1.00 21.54 ? 357  LEU A CB    1 
ATOM   7104 C CG    . LEU B 1 359 ? 35.581 -4.966  -40.628 1.00 21.83 ? 357  LEU A CG    1 
ATOM   7105 C CD1   . LEU B 1 359 ? 34.338 -5.248  -39.787 1.00 23.90 ? 357  LEU A CD1   1 
ATOM   7106 C CD2   . LEU B 1 359 ? 35.831 -6.100  -41.618 1.00 22.80 ? 357  LEU A CD2   1 
ATOM   7107 N N     . ASN B 1 360 ? 36.463 -0.822  -42.527 1.00 20.32 ? 358  ASN A N     1 
ATOM   7108 C CA    . ASN B 1 360 ? 36.207 0.354   -43.389 1.00 19.23 ? 358  ASN A CA    1 
ATOM   7109 C C     . ASN B 1 360 ? 37.320 0.462   -44.440 1.00 19.81 ? 358  ASN A C     1 
ATOM   7110 O O     . ASN B 1 360 ? 37.017 0.656   -45.603 1.00 19.59 ? 358  ASN A O     1 
ATOM   7111 C CB    . ASN B 1 360 ? 36.119 1.634   -42.565 1.00 19.42 ? 358  ASN A CB    1 
ATOM   7112 C CG    . ASN B 1 360 ? 34.834 1.755   -41.764 1.00 21.44 ? 358  ASN A CG    1 
ATOM   7113 O OD1   . ASN B 1 360 ? 33.814 1.133   -42.089 1.00 20.79 ? 358  ASN A OD1   1 
ATOM   7114 N ND2   . ASN B 1 360 ? 34.872 2.590   -40.743 1.00 19.95 ? 358  ASN A ND2   1 
ATOM   7115 N N     . GLU B 1 361 ? 38.582 0.425   -44.012 1.00 20.92 ? 359  GLU A N     1 
ATOM   7116 C CA    . GLU B 1 361 ? 39.731 0.668   -44.919 1.00 21.52 ? 359  GLU A CA    1 
ATOM   7117 C C     . GLU B 1 361 ? 39.861 -0.504  -45.892 1.00 20.10 ? 359  GLU A C     1 
ATOM   7118 O O     . GLU B 1 361 ? 40.134 -0.229  -47.026 1.00 22.49 ? 359  GLU A O     1 
ATOM   7119 C CB    . GLU B 1 361 ? 40.981 0.952   -44.095 1.00 22.88 ? 359  GLU A CB    1 
ATOM   7120 C CG    . GLU B 1 361 ? 40.970 2.386   -43.571 1.00 24.03 ? 359  GLU A CG    1 
ATOM   7121 C CD    . GLU B 1 361 ? 42.130 2.738   -42.655 1.00 27.53 ? 359  GLU A CD    1 
ATOM   7122 O OE1   . GLU B 1 361 ? 43.282 2.322   -42.966 1.00 24.85 ? 359  GLU A OE1   1 
ATOM   7123 O OE2   . GLU B 1 361 ? 41.868 3.384   -41.623 1.00 27.00 ? 359  GLU A OE2   1 
ATOM   7124 N N     . GLY B 1 362 ? 39.648 -1.741  -45.450 1.00 20.31 ? 360  GLY A N     1 
ATOM   7125 C CA    . GLY B 1 362 ? 39.671 -2.922  -46.327 1.00 21.38 ? 360  GLY A CA    1 
ATOM   7126 C C     . GLY B 1 362 ? 38.540 -2.851  -47.327 1.00 21.07 ? 360  GLY A C     1 
ATOM   7127 O O     . GLY B 1 362 ? 38.766 -3.107  -48.524 1.00 19.11 ? 360  GLY A O     1 
ATOM   7128 N N     . GLY B 1 363 ? 37.343 -2.474  -46.857 1.00 24.20 ? 361  GLY A N     1 
ATOM   7129 C CA    . GLY B 1 363 ? 36.162 -2.319  -47.722 1.00 22.20 ? 361  GLY A CA    1 
ATOM   7130 C C     . GLY B 1 363 ? 36.371 -1.237  -48.765 1.00 23.09 ? 361  GLY A C     1 
ATOM   7131 O O     . GLY B 1 363 ? 35.924 -1.418  -49.914 1.00 20.43 ? 361  GLY A O     1 
ATOM   7132 N N     . ARG B 1 364 ? 37.002 -0.126  -48.377 1.00 23.07 ? 362  ARG A N     1 
ATOM   7133 C CA    . ARG B 1 364 ? 37.257 0.986   -49.310 1.00 21.97 ? 362  ARG A CA    1 
ATOM   7134 C C     . ARG B 1 364 ? 38.216 0.494   -50.409 1.00 23.58 ? 362  ARG A C     1 
ATOM   7135 O O     . ARG B 1 364 ? 37.948 0.765   -51.610 1.00 21.49 ? 362  ARG A O     1 
ATOM   7136 C CB    . ARG B 1 364 ? 37.859 2.199   -48.598 1.00 23.26 ? 362  ARG A CB    1 
ATOM   7137 C CG    . ARG B 1 364 ? 38.190 3.327   -49.563 1.00 23.47 ? 362  ARG A CG    1 
ATOM   7138 C CD    . ARG B 1 364 ? 38.533 4.633   -48.879 1.00 23.79 ? 362  ARG A CD    1 
ATOM   7139 N NE    . ARG B 1 364 ? 37.467 5.047   -47.993 1.00 25.81 ? 362  ARG A NE    1 
ATOM   7140 C CZ    . ARG B 1 364 ? 37.536 5.126   -46.661 1.00 26.79 ? 362  ARG A CZ    1 
ATOM   7141 N NH1   . ARG B 1 364 ? 38.618 4.765   -45.982 1.00 25.19 ? 362  ARG A NH1   1 
ATOM   7142 N NH2   . ARG B 1 364 ? 36.459 5.492   -45.991 1.00 29.40 ? 362  ARG A NH2   1 
ATOM   7143 N N     . ALA B 1 365 ? 39.302 -0.195  -50.023 1.00 23.27 ? 363  ALA A N     1 
ATOM   7144 C CA    . ALA B 1 365 ? 40.261 -0.786  -50.982 1.00 22.12 ? 363  ALA A CA    1 
ATOM   7145 C C     . ALA B 1 365 ? 39.501 -1.729  -51.909 1.00 21.32 ? 363  ALA A C     1 
ATOM   7146 O O     . ALA B 1 365 ? 39.661 -1.598  -53.114 1.00 19.53 ? 363  ALA A O     1 
ATOM   7147 C CB    . ALA B 1 365 ? 41.396 -1.497  -50.281 1.00 23.66 ? 363  ALA A CB    1 
ATOM   7148 N N     . PHE B 1 366 ? 38.671 -2.619  -51.380 1.00 19.84 ? 364  PHE A N     1 
ATOM   7149 C CA    . PHE B 1 366 ? 37.975 -3.620  -52.221 1.00 21.78 ? 364  PHE A CA    1 
ATOM   7150 C C     . PHE B 1 366 ? 36.981 -2.934  -53.158 1.00 20.80 ? 364  PHE A C     1 
ATOM   7151 O O     . PHE B 1 366 ? 36.923 -3.313  -54.331 1.00 21.40 ? 364  PHE A O     1 
ATOM   7152 C CB    . PHE B 1 366 ? 37.279 -4.674  -51.375 1.00 22.56 ? 364  PHE A CB    1 
ATOM   7153 C CG    . PHE B 1 366 ? 36.699 -5.819  -52.166 1.00 21.91 ? 364  PHE A CG    1 
ATOM   7154 C CD1   . PHE B 1 366 ? 37.514 -6.683  -52.872 1.00 24.13 ? 364  PHE A CD1   1 
ATOM   7155 C CD2   . PHE B 1 366 ? 35.334 -6.043  -52.189 1.00 23.04 ? 364  PHE A CD2   1 
ATOM   7156 C CE1   . PHE B 1 366 ? 36.990 -7.763  -53.563 1.00 23.14 ? 364  PHE A CE1   1 
ATOM   7157 C CE2   . PHE B 1 366 ? 34.807 -7.137  -52.871 1.00 23.38 ? 364  PHE A CE2   1 
ATOM   7158 C CZ    . PHE B 1 366 ? 35.639 -8.007  -53.536 1.00 23.31 ? 364  PHE A CZ    1 
ATOM   7159 N N     . SER B 1 367 ? 36.306 -1.889  -52.696 1.00 20.82 ? 365  SER A N     1 
ATOM   7160 C CA    . SER B 1 367 ? 35.363 -1.105  -53.531 1.00 21.98 ? 365  SER A CA    1 
ATOM   7161 C C     . SER B 1 367 ? 36.118 -0.515  -54.739 1.00 21.47 ? 365  SER A C     1 
ATOM   7162 O O     . SER B 1 367 ? 35.610 -0.601  -55.902 1.00 20.08 ? 365  SER A O     1 
ATOM   7163 C CB    . SER B 1 367 ? 34.630 -0.082  -52.696 1.00 21.43 ? 365  SER A CB    1 
ATOM   7164 O OG    . SER B 1 367 ? 35.402 1.076   -52.466 1.00 26.58 ? 365  SER A OG    1 
ATOM   7165 N N     . SER B 1 368 ? 37.305 0.035   -54.512 1.00 21.83 ? 366  SER A N     1 
ATOM   7166 C CA    . SER B 1 368 ? 38.152 0.627   -55.572 1.00 22.21 ? 366  SER A CA    1 
ATOM   7167 C C     . SER B 1 368 ? 38.645 -0.466  -56.530 1.00 22.94 ? 366  SER A C     1 
ATOM   7168 O O     . SER B 1 368 ? 38.627 -0.246  -57.746 1.00 20.96 ? 366  SER A O     1 
ATOM   7169 C CB    . SER B 1 368 ? 39.289 1.418   -54.982 1.00 24.44 ? 366  SER A CB    1 
ATOM   7170 O OG    . SER B 1 368 ? 38.805 2.662   -54.489 1.00 24.49 ? 366  SER A OG    1 
ATOM   7171 N N     . TYR B 1 369 ? 39.059 -1.611  -56.006 1.00 22.27 ? 367  TYR A N     1 
ATOM   7172 C CA    . TYR B 1 369 ? 39.504 -2.756  -56.820 1.00 23.09 ? 367  TYR A CA    1 
ATOM   7173 C C     . TYR B 1 369 ? 38.381 -3.194  -57.765 1.00 24.03 ? 367  TYR A C     1 
ATOM   7174 O O     . TYR B 1 369 ? 38.617 -3.476  -58.969 1.00 26.14 ? 367  TYR A O     1 
ATOM   7175 C CB    . TYR B 1 369 ? 39.970 -3.877  -55.900 1.00 24.70 ? 367  TYR A CB    1 
ATOM   7176 C CG    . TYR B 1 369 ? 40.465 -5.088  -56.629 1.00 25.73 ? 367  TYR A CG    1 
ATOM   7177 C CD1   . TYR B 1 369 ? 41.774 -5.170  -57.064 1.00 26.20 ? 367  TYR A CD1   1 
ATOM   7178 C CD2   . TYR B 1 369 ? 39.615 -6.141  -56.910 1.00 28.74 ? 367  TYR A CD2   1 
ATOM   7179 C CE1   . TYR B 1 369 ? 42.240 -6.289  -57.732 1.00 25.17 ? 367  TYR A CE1   1 
ATOM   7180 C CE2   . TYR B 1 369 ? 40.073 -7.269  -57.572 1.00 28.00 ? 367  TYR A CE2   1 
ATOM   7181 C CZ    . TYR B 1 369 ? 41.385 -7.333  -58.003 1.00 26.82 ? 367  TYR A CZ    1 
ATOM   7182 O OH    . TYR B 1 369 ? 41.817 -8.450  -58.661 1.00 28.67 ? 367  TYR A OH    1 
ATOM   7183 N N     . VAL B 1 370 ? 37.165 -3.293  -57.241 1.00 21.16 ? 368  VAL A N     1 
ATOM   7184 C CA    . VAL B 1 370 ? 36.002 -3.719  -58.055 1.00 21.46 ? 368  VAL A CA    1 
ATOM   7185 C C     . VAL B 1 370 ? 35.686 -2.610  -59.072 1.00 20.63 ? 368  VAL A C     1 
ATOM   7186 O O     . VAL B 1 370 ? 35.447 -2.956  -60.272 1.00 21.90 ? 368  VAL A O     1 
ATOM   7187 C CB    . VAL B 1 370 ? 34.794 -4.144  -57.196 1.00 20.92 ? 368  VAL A CB    1 
ATOM   7188 C CG1   . VAL B 1 370 ? 33.595 -4.510  -58.061 1.00 21.30 ? 368  VAL A CG1   1 
ATOM   7189 C CG2   . VAL B 1 370 ? 35.130 -5.313  -56.266 1.00 22.41 ? 368  VAL A CG2   1 
ATOM   7190 N N     . ALA B 1 371 ? 35.687 -1.335  -58.671 1.00 20.36 ? 369  ALA A N     1 
ATOM   7191 C CA    . ALA B 1 371 ? 35.472 -0.198  -59.599 1.00 22.24 ? 369  ALA A CA    1 
ATOM   7192 C C     . ALA B 1 371 ? 36.491 -0.277  -60.741 1.00 23.38 ? 369  ALA A C     1 
ATOM   7193 O O     . ALA B 1 371 ? 36.141 0.021   -61.874 1.00 22.20 ? 369  ALA A O     1 
ATOM   7194 C CB    . ALA B 1 371 ? 35.583 1.123   -58.863 1.00 21.18 ? 369  ALA A CB    1 
ATOM   7195 N N     . MET B 1 372 ? 37.730 -0.650  -60.419 1.00 25.72 ? 370  MET A N     1 
ATOM   7196 C CA    . MET B 1 372 ? 38.839 -0.775  -61.393 1.00 28.61 ? 370  MET A CA    1 
ATOM   7197 C C     . MET B 1 372 ? 38.505 -1.878  -62.412 1.00 26.65 ? 370  MET A C     1 
ATOM   7198 O O     . MET B 1 372 ? 38.768 -1.678  -63.631 1.00 26.05 ? 370  MET A O     1 
ATOM   7199 C CB    . MET B 1 372 ? 40.134 -1.076  -60.635 1.00 31.14 ? 370  MET A CB    1 
ATOM   7200 C CG    . MET B 1 372 ? 41.391 -0.847  -61.430 1.00 39.56 ? 370  MET A CG    1 
ATOM   7201 S SD    . MET B 1 372 ? 42.865 -1.104  -60.379 1.00 49.62 ? 370  MET A SD    1 
ATOM   7202 C CE    . MET B 1 372 ? 42.824 -2.888  -60.193 1.00 47.06 ? 370  MET A CE    1 
ATOM   7203 N N     . GLN B 1 373 ? 37.890 -2.975  -61.979 1.00 25.45 ? 371  GLN A N     1 
ATOM   7204 C CA    . GLN B 1 373 ? 37.468 -4.048  -62.903 1.00 24.94 ? 371  GLN A CA    1 
ATOM   7205 C C     . GLN B 1 373 ? 36.362 -3.518  -63.824 1.00 27.05 ? 371  GLN A C     1 
ATOM   7206 O O     . GLN B 1 373 ? 36.372 -3.868  -65.047 1.00 23.85 ? 371  GLN A O     1 
ATOM   7207 C CB    . GLN B 1 373 ? 36.988 -5.294  -62.177 1.00 26.08 ? 371  GLN A CB    1 
ATOM   7208 C CG    . GLN B 1 373 ? 38.020 -5.900  -61.240 1.00 27.82 ? 371  GLN A CG    1 
ATOM   7209 C CD    . GLN B 1 373 ? 39.315 -6.200  -61.956 1.00 33.12 ? 371  GLN A CD    1 
ATOM   7210 O OE1   . GLN B 1 373 ? 39.327 -6.482  -63.159 1.00 34.49 ? 371  GLN A OE1   1 
ATOM   7211 N NE2   . GLN B 1 373 ? 40.416 -6.097  -61.230 1.00 34.80 ? 371  GLN A NE2   1 
ATOM   7212 N N     . LEU B 1 374 ? 35.434 -2.715  -63.295 1.00 25.57 ? 372  LEU A N     1 
ATOM   7213 C CA    . LEU B 1 374 ? 34.332 -2.178  -64.132 1.00 25.98 ? 372  LEU A CA    1 
ATOM   7214 C C     . LEU B 1 374 ? 34.921 -1.246  -65.186 1.00 26.14 ? 372  LEU A C     1 
ATOM   7215 O O     . LEU B 1 374 ? 34.487 -1.335  -66.356 1.00 26.50 ? 372  LEU A O     1 
ATOM   7216 C CB    . LEU B 1 374 ? 33.303 -1.460  -63.265 1.00 24.38 ? 372  LEU A CB    1 
ATOM   7217 C CG    . LEU B 1 374 ? 32.413 -2.383  -62.456 1.00 24.74 ? 372  LEU A CG    1 
ATOM   7218 C CD1   . LEU B 1 374 ? 31.732 -1.616  -61.332 1.00 24.70 ? 372  LEU A CD1   1 
ATOM   7219 C CD2   . LEU B 1 374 ? 31.413 -3.098  -63.340 1.00 24.38 ? 372  LEU A CD2   1 
ATOM   7220 N N     . ASP B 1 375 ? 35.867 -0.403  -64.787 1.00 24.81 ? 373  ASP A N     1 
ATOM   7221 C CA    . ASP B 1 375 ? 36.535 0.532   -65.718 1.00 27.44 ? 373  ASP A CA    1 
ATOM   7222 C C     . ASP B 1 375 ? 37.330 -0.255  -66.776 1.00 29.16 ? 373  ASP A C     1 
ATOM   7223 O O     . ASP B 1 375 ? 37.267 0.130   -67.934 1.00 26.73 ? 373  ASP A O     1 
ATOM   7224 C CB    . ASP B 1 375 ? 37.441 1.497   -64.970 1.00 29.54 ? 373  ASP A CB    1 
ATOM   7225 C CG    . ASP B 1 375 ? 36.676 2.569   -64.227 1.00 30.00 ? 373  ASP A CG    1 
ATOM   7226 O OD1   . ASP B 1 375 ? 35.483 2.824   -64.596 1.00 31.51 ? 373  ASP A OD1   1 
ATOM   7227 O OD2   . ASP B 1 375 ? 37.295 3.179   -63.327 1.00 27.55 ? 373  ASP A OD2   1 
ATOM   7228 N N     . THR B 1 376 ? 38.052 -1.314  -66.402 1.00 29.11 ? 374  THR A N     1 
ATOM   7229 C CA    . THR B 1 376 ? 38.789 -2.172  -67.374 1.00 29.37 ? 374  THR A CA    1 
ATOM   7230 C C     . THR B 1 376 ? 37.795 -2.786  -68.363 1.00 30.51 ? 374  THR A C     1 
ATOM   7231 O O     . THR B 1 376 ? 38.060 -2.705  -69.590 1.00 30.41 ? 374  THR A O     1 
ATOM   7232 C CB    . THR B 1 376 ? 39.668 -3.203  -66.658 1.00 27.92 ? 374  THR A CB    1 
ATOM   7233 O OG1   . THR B 1 376 ? 40.509 -2.383  -65.846 1.00 26.85 ? 374  THR A OG1   1 
ATOM   7234 C CG2   . THR B 1 376 ? 40.484 -4.062  -67.600 1.00 29.33 ? 374  THR A CG2   1 
ATOM   7235 N N     . ALA B 1 377 ? 36.698 -3.369  -67.868 1.00 29.65 ? 375  ALA A N     1 
ATOM   7236 C CA    . ALA B 1 377 ? 35.659 -4.027  -68.687 1.00 30.39 ? 375  ALA A CA    1 
ATOM   7237 C C     . ALA B 1 377 ? 35.129 -3.027  -69.715 1.00 32.03 ? 375  ALA A C     1 
ATOM   7238 O O     . ALA B 1 377 ? 34.915 -3.426  -70.860 1.00 33.70 ? 375  ALA A O     1 
ATOM   7239 C CB    . ALA B 1 377 ? 34.543 -4.573  -67.835 1.00 29.55 ? 375  ALA A CB    1 
ATOM   7240 N N     . LYS B 1 378 ? 34.954 -1.771  -69.310 1.00 30.82 ? 376  LYS A N     1 
ATOM   7241 C CA    . LYS B 1 378 ? 34.363 -0.705  -70.151 1.00 33.30 ? 376  LYS A CA    1 
ATOM   7242 C C     . LYS B 1 378 ? 35.411 -0.137  -71.117 1.00 34.18 ? 376  LYS A C     1 
ATOM   7243 O O     . LYS B 1 378 ? 35.083 0.033   -72.269 1.00 33.40 ? 376  LYS A O     1 
ATOM   7244 C CB    . LYS B 1 378 ? 33.809 0.413   -69.270 1.00 34.28 ? 376  LYS A CB    1 
ATOM   7245 C CG    . LYS B 1 378 ? 33.070 1.523   -70.013 1.00 38.12 ? 376  LYS A CG    1 
ATOM   7246 C CD    . LYS B 1 378 ? 32.268 2.414   -69.068 1.00 40.97 ? 376  LYS A CD    1 
ATOM   7247 C CE    . LYS B 1 378 ? 31.825 3.732   -69.670 1.00 40.41 ? 376  LYS A CE    1 
ATOM   7248 N NZ    . LYS B 1 378 ? 30.864 3.499   -70.768 1.00 43.08 ? 376  LYS A NZ    1 
ATOM   7249 N N     . TYR B 1 379 ? 36.613 0.199   -70.654 1.00 34.95 ? 377  TYR A N     1 
ATOM   7250 C CA    . TYR B 1 379 ? 37.512 1.151   -71.357 1.00 35.31 ? 377  TYR A CA    1 
ATOM   7251 C C     . TYR B 1 379 ? 38.682 0.457   -72.064 1.00 38.39 ? 377  TYR A C     1 
ATOM   7252 O O     . TYR B 1 379 ? 39.243 1.096   -72.974 1.00 40.12 ? 377  TYR A O     1 
ATOM   7253 C CB    . TYR B 1 379 ? 38.034 2.212   -70.396 1.00 33.77 ? 377  TYR A CB    1 
ATOM   7254 C CG    . TYR B 1 379 ? 36.981 3.180   -69.933 1.00 36.34 ? 377  TYR A CG    1 
ATOM   7255 C CD1   . TYR B 1 379 ? 36.447 4.120   -70.801 1.00 35.71 ? 377  TYR A CD1   1 
ATOM   7256 C CD2   . TYR B 1 379 ? 36.550 3.186   -68.613 1.00 33.46 ? 377  TYR A CD2   1 
ATOM   7257 C CE1   . TYR B 1 379 ? 35.476 5.011   -70.377 1.00 39.39 ? 377  TYR A CE1   1 
ATOM   7258 C CE2   . TYR B 1 379 ? 35.598 4.087   -68.172 1.00 35.22 ? 377  TYR A CE2   1 
ATOM   7259 C CZ    . TYR B 1 379 ? 35.053 4.997   -69.057 1.00 38.87 ? 377  TYR A CZ    1 
ATOM   7260 O OH    . TYR B 1 379 ? 34.093 5.873   -68.630 1.00 39.05 ? 377  TYR A OH    1 
ATOM   7261 N N     . SER B 1 380 ? 39.044 -0.775  -71.702 1.00 37.95 ? 378  SER A N     1 
ATOM   7262 C CA    . SER B 1 380 ? 40.244 -1.445  -72.270 1.00 41.24 ? 378  SER A CA    1 
ATOM   7263 C C     . SER B 1 380 ? 40.035 -1.676  -73.775 1.00 41.85 ? 378  SER A C     1 
ATOM   7264 O O     . SER B 1 380 ? 38.948 -2.163  -74.155 1.00 37.80 ? 378  SER A O     1 
ATOM   7265 C CB    . SER B 1 380 ? 40.567 -2.745  -71.575 1.00 44.45 ? 378  SER A CB    1 
ATOM   7266 O OG    . SER B 1 380 ? 41.653 -3.402  -72.219 1.00 42.64 ? 378  SER A OG    1 
ATOM   7267 N N     . GLU B 1 381 ? 41.073 -1.380  -74.563 1.00 44.37 ? 379  GLU A N     1 
ATOM   7268 C CA    . GLU B 1 381 ? 41.161 -1.591  -76.038 1.00 47.77 ? 379  GLU A CA    1 
ATOM   7269 C C     . GLU B 1 381 ? 41.429 -3.071  -76.353 1.00 43.79 ? 379  GLU A C     1 
ATOM   7270 O O     . GLU B 1 381 ? 41.198 -3.455  -77.491 1.00 45.12 ? 379  GLU A O     1 
ATOM   7271 C CB    . GLU B 1 381 ? 42.305 -0.761  -76.639 1.00 54.56 ? 379  GLU A CB    1 
ATOM   7272 C CG    . GLU B 1 381 ? 42.361 0.698   -76.191 1.00 60.60 ? 379  GLU A CG    1 
ATOM   7273 C CD    . GLU B 1 381 ? 41.623 1.662   -77.107 1.00 64.17 ? 379  GLU A CD    1 
ATOM   7274 O OE1   . GLU B 1 381 ? 42.229 2.687   -77.505 1.00 64.56 ? 379  GLU A OE1   1 
ATOM   7275 O OE2   . GLU B 1 381 ? 40.454 1.373   -77.441 1.00 59.07 ? 379  GLU A OE2   1 
ATOM   7276 N N     . ASP B 1 382 ? 41.898 -3.862  -75.383 1.00 43.43 ? 380  ASP A N     1 
ATOM   7277 C CA    . ASP B 1 382 ? 42.279 -5.299  -75.532 1.00 41.00 ? 380  ASP A CA    1 
ATOM   7278 C C     . ASP B 1 382 ? 41.072 -6.163  -75.155 1.00 41.17 ? 380  ASP A C     1 
ATOM   7279 O O     . ASP B 1 382 ? 40.624 -6.072  -73.996 1.00 35.77 ? 380  ASP A O     1 
ATOM   7280 C CB    . ASP B 1 382 ? 43.522 -5.583  -74.684 1.00 39.49 ? 380  ASP A CB    1 
ATOM   7281 C CG    . ASP B 1 382 ? 44.104 -6.994  -74.703 1.00 45.17 ? 380  ASP A CG    1 
ATOM   7282 O OD1   . ASP B 1 382 ? 43.351 -7.977  -74.593 1.00 41.71 ? 380  ASP A OD1   1 
ATOM   7283 O OD2   . ASP B 1 382 ? 45.344 -7.097  -74.764 1.00 53.25 ? 380  ASP A OD2   1 
ATOM   7284 N N     . ALA B 1 383 ? 40.587 -6.997  -76.084 1.00 37.63 ? 381  ALA A N     1 
ATOM   7285 C CA    . ALA B 1 383 ? 39.407 -7.870  -75.897 1.00 38.20 ? 381  ALA A CA    1 
ATOM   7286 C C     . ALA B 1 383 ? 39.668 -8.917  -74.804 1.00 36.74 ? 381  ALA A C     1 
ATOM   7287 O O     . ALA B 1 383 ? 38.739 -9.156  -74.030 1.00 36.70 ? 381  ALA A O     1 
ATOM   7288 C CB    . ALA B 1 383 ? 38.999 -8.513  -77.199 1.00 39.10 ? 381  ALA A CB    1 
ATOM   7289 N N     . VAL B 1 384 ? 40.853 -9.530  -74.735 1.00 31.29 ? 382  VAL A N     1 
ATOM   7290 C CA    . VAL B 1 384 ? 41.148 -10.555 -73.694 1.00 33.88 ? 382  VAL A CA    1 
ATOM   7291 C C     . VAL B 1 384 ? 41.181 -9.864  -72.315 1.00 34.75 ? 382  VAL A C     1 
ATOM   7292 O O     . VAL B 1 384 ? 40.726 -10.504 -71.356 1.00 31.90 ? 382  VAL A O     1 
ATOM   7293 C CB    . VAL B 1 384 ? 42.427 -11.349 -74.001 1.00 34.71 ? 382  VAL A CB    1 
ATOM   7294 C CG1   . VAL B 1 384 ? 42.944 -12.135 -72.810 1.00 36.89 ? 382  VAL A CG1   1 
ATOM   7295 C CG2   . VAL B 1 384 ? 42.184 -12.283 -75.174 1.00 37.76 ? 382  VAL A CG2   1 
ATOM   7296 N N     . THR B 1 385 ? 41.675 -8.621  -72.231 1.00 31.66 ? 383  THR A N     1 
ATOM   7297 C CA    . THR B 1 385 ? 41.730 -7.821  -70.977 1.00 34.91 ? 383  THR A CA    1 
ATOM   7298 C C     . THR B 1 385 ? 40.294 -7.505  -70.544 1.00 32.42 ? 383  THR A C     1 
ATOM   7299 O O     . THR B 1 385 ? 39.973 -7.785  -69.373 1.00 30.13 ? 383  THR A O     1 
ATOM   7300 C CB    . THR B 1 385 ? 42.555 -6.538  -71.148 1.00 37.21 ? 383  THR A CB    1 
ATOM   7301 O OG1   . THR B 1 385 ? 43.881 -6.926  -71.513 1.00 40.73 ? 383  THR A OG1   1 
ATOM   7302 C CG2   . THR B 1 385 ? 42.613 -5.692  -69.892 1.00 34.34 ? 383  THR A CG2   1 
ATOM   7303 N N     . ARG B 1 386 ? 39.465 -7.021  -71.472 1.00 31.23 ? 384  ARG A N     1 
ATOM   7304 C CA    . ARG B 1 386 ? 38.036 -6.681  -71.215 1.00 34.15 ? 384  ARG A CA    1 
ATOM   7305 C C     . ARG B 1 386 ? 37.307 -7.909  -70.672 1.00 33.01 ? 384  ARG A C     1 
ATOM   7306 O O     . ARG B 1 386 ? 36.553 -7.765  -69.696 1.00 28.86 ? 384  ARG A O     1 
ATOM   7307 C CB    . ARG B 1 386 ? 37.302 -6.179  -72.464 1.00 36.93 ? 384  ARG A CB    1 
ATOM   7308 C CG    . ARG B 1 386 ? 37.440 -4.681  -72.719 1.00 40.71 ? 384  ARG A CG    1 
ATOM   7309 C CD    . ARG B 1 386 ? 36.387 -4.147  -73.679 1.00 41.36 ? 384  ARG A CD    1 
ATOM   7310 N NE    . ARG B 1 386 ? 36.285 -4.978  -74.879 1.00 44.06 ? 384  ARG A NE    1 
ATOM   7311 C CZ    . ARG B 1 386 ? 36.995 -4.806  -76.002 1.00 45.28 ? 384  ARG A CZ    1 
ATOM   7312 N NH1   . ARG B 1 386 ? 37.882 -3.829  -76.116 1.00 40.43 ? 384  ARG A NH1   1 
ATOM   7313 N NH2   . ARG B 1 386 ? 36.814 -5.627  -77.019 1.00 50.91 ? 384  ARG A NH2   1 
ATOM   7314 N N     . LYS B 1 387 ? 37.519 -9.066  -71.295 1.00 31.17 ? 385  LYS A N     1 
ATOM   7315 C CA    . LYS B 1 387 ? 36.807 -10.322 -70.954 1.00 33.36 ? 385  LYS A CA    1 
ATOM   7316 C C     . LYS B 1 387 ? 37.224 -10.797 -69.554 1.00 31.11 ? 385  LYS A C     1 
ATOM   7317 O O     . LYS B 1 387 ? 36.355 -11.205 -68.780 1.00 27.48 ? 385  LYS A O     1 
ATOM   7318 C CB    . LYS B 1 387 ? 37.082 -11.390 -72.012 1.00 36.14 ? 385  LYS A CB    1 
ATOM   7319 C CG    . LYS B 1 387 ? 36.026 -12.471 -72.127 1.00 45.82 ? 385  LYS A CG    1 
ATOM   7320 C CD    . LYS B 1 387 ? 34.815 -12.081 -72.979 1.00 48.14 ? 385  LYS A CD    1 
ATOM   7321 C CE    . LYS B 1 387 ? 33.760 -13.170 -73.029 1.00 53.38 ? 385  LYS A CE    1 
ATOM   7322 N NZ    . LYS B 1 387 ? 33.460 -13.715 -71.677 1.00 57.90 ? 385  LYS A NZ    1 
ATOM   7323 N N     . ARG B 1 388 ? 38.509 -10.786 -69.240 1.00 29.60 ? 386  ARG A N     1 
ATOM   7324 C CA    . ARG B 1 388 ? 38.963 -11.123 -67.873 1.00 30.71 ? 386  ARG A CA    1 
ATOM   7325 C C     . ARG B 1 388 ? 38.318 -10.140 -66.879 1.00 28.18 ? 386  ARG A C     1 
ATOM   7326 O O     . ARG B 1 388 ? 37.841 -10.595 -65.861 1.00 28.26 ? 386  ARG A O     1 
ATOM   7327 C CB    . ARG B 1 388 ? 40.488 -11.101 -67.762 1.00 34.97 ? 386  ARG A CB    1 
ATOM   7328 C CG    . ARG B 1 388 ? 41.002 -11.639 -66.429 1.00 37.58 ? 386  ARG A CG    1 
ATOM   7329 C CD    . ARG B 1 388 ? 42.510 -11.671 -66.288 1.00 41.16 ? 386  ARG A CD    1 
ATOM   7330 N NE    . ARG B 1 388 ? 42.887 -11.826 -64.882 1.00 44.42 ? 386  ARG A NE    1 
ATOM   7331 C CZ    . ARG B 1 388 ? 43.065 -10.827 -64.013 1.00 44.93 ? 386  ARG A CZ    1 
ATOM   7332 N NH1   . ARG B 1 388 ? 42.880 -9.563  -64.370 1.00 42.66 ? 386  ARG A NH1   1 
ATOM   7333 N NH2   . ARG B 1 388 ? 43.405 -11.102 -62.765 1.00 49.43 ? 386  ARG A NH2   1 
ATOM   7334 N N     . ALA B 1 389 ? 38.299 -8.848  -67.175 1.00 24.44 ? 387  ALA A N     1 
ATOM   7335 C CA    . ALA B 1 389 ? 37.688 -7.845  -66.284 1.00 27.00 ? 387  ALA A CA    1 
ATOM   7336 C C     . ALA B 1 389 ? 36.188 -8.145  -66.102 1.00 27.79 ? 387  ALA A C     1 
ATOM   7337 O O     . ALA B 1 389 ? 35.747 -8.128  -64.948 1.00 26.16 ? 387  ALA A O     1 
ATOM   7338 C CB    . ALA B 1 389 ? 37.955 -6.456  -66.803 1.00 26.17 ? 387  ALA A CB    1 
ATOM   7339 N N     . GLU B 1 390 ? 35.457 -8.488  -67.176 1.00 26.63 ? 388  GLU A N     1 
ATOM   7340 C CA    . GLU B 1 390 ? 34.021 -8.858  -67.149 1.00 28.69 ? 388  GLU A CA    1 
ATOM   7341 C C     . GLU B 1 390 ? 33.815 -10.048 -66.196 1.00 28.14 ? 388  GLU A C     1 
ATOM   7342 O O     . GLU B 1 390 ? 32.828 -10.010 -65.416 1.00 24.38 ? 388  GLU A O     1 
ATOM   7343 C CB    . GLU B 1 390 ? 33.478 -9.145  -68.560 1.00 32.88 ? 388  GLU A CB    1 
ATOM   7344 C CG    . GLU B 1 390 ? 33.201 -7.882  -69.371 1.00 37.34 ? 388  GLU A CG    1 
ATOM   7345 C CD    . GLU B 1 390 ? 33.086 -8.050  -70.889 1.00 46.23 ? 388  GLU A CD    1 
ATOM   7346 O OE1   . GLU B 1 390 ? 33.314 -7.033  -71.607 1.00 51.53 ? 388  GLU A OE1   1 
ATOM   7347 O OE2   . GLU B 1 390 ? 32.789 -9.184  -71.359 1.00 43.37 ? 388  GLU A OE2   1 
ATOM   7348 N N     . GLU B 1 391 ? 34.696 -11.052 -66.242 1.00 26.32 ? 389  GLU A N     1 
ATOM   7349 C CA    . GLU B 1 391 ? 34.585 -12.270 -65.403 1.00 27.87 ? 389  GLU A CA    1 
ATOM   7350 C C     . GLU B 1 391 ? 34.854 -11.879 -63.943 1.00 25.72 ? 389  GLU A C     1 
ATOM   7351 O O     . GLU B 1 391 ? 34.170 -12.402 -63.070 1.00 27.83 ? 389  GLU A O     1 
ATOM   7352 C CB    . GLU B 1 391 ? 35.532 -13.376 -65.882 1.00 31.11 ? 389  GLU A CB    1 
ATOM   7353 C CG    . GLU B 1 391 ? 35.134 -13.944 -67.243 1.00 33.16 ? 389  GLU A CG    1 
ATOM   7354 C CD    . GLU B 1 391 ? 36.255 -14.658 -67.994 1.00 37.33 ? 389  GLU A CD    1 
ATOM   7355 O OE1   . GLU B 1 391 ? 37.390 -14.762 -67.441 1.00 37.31 ? 389  GLU A OE1   1 
ATOM   7356 O OE2   . GLU B 1 391 ? 36.003 -15.067 -69.158 1.00 40.44 ? 389  GLU A OE2   1 
ATOM   7357 N N     . LEU B 1 392 ? 35.805 -10.986 -63.686 1.00 23.54 ? 390  LEU A N     1 
ATOM   7358 C CA    . LEU B 1 392 ? 36.065 -10.542 -62.302 1.00 25.53 ? 390  LEU A CA    1 
ATOM   7359 C C     . LEU B 1 392 ? 34.901 -9.658  -61.818 1.00 25.56 ? 390  LEU A C     1 
ATOM   7360 O O     . LEU B 1 392 ? 34.558 -9.759  -60.641 1.00 26.95 ? 390  LEU A O     1 
ATOM   7361 C CB    . LEU B 1 392 ? 37.401 -9.823  -62.218 1.00 26.71 ? 390  LEU A CB    1 
ATOM   7362 C CG    . LEU B 1 392 ? 38.618 -10.741 -62.271 1.00 27.46 ? 390  LEU A CG    1 
ATOM   7363 C CD1   . LEU B 1 392 ? 39.886 -9.930  -62.160 1.00 27.12 ? 390  LEU A CD1   1 
ATOM   7364 C CD2   . LEU B 1 392 ? 38.573 -11.792 -61.188 1.00 27.73 ? 390  LEU A CD2   1 
ATOM   7365 N N     . VAL B 1 393 ? 34.287 -8.865  -62.693 1.00 24.26 ? 391  VAL A N     1 
ATOM   7366 C CA    . VAL B 1 393 ? 33.075 -8.094  -62.319 1.00 25.68 ? 391  VAL A CA    1 
ATOM   7367 C C     . VAL B 1 393 ? 32.007 -9.097  -61.889 1.00 25.73 ? 391  VAL A C     1 
ATOM   7368 O O     . VAL B 1 393 ? 31.410 -8.909  -60.812 1.00 24.88 ? 391  VAL A O     1 
ATOM   7369 C CB    . VAL B 1 393 ? 32.581 -7.179  -63.449 1.00 24.53 ? 391  VAL A CB    1 
ATOM   7370 C CG1   . VAL B 1 393 ? 31.177 -6.680  -63.152 1.00 26.39 ? 391  VAL A CG1   1 
ATOM   7371 C CG2   . VAL B 1 393 ? 33.515 -6.013  -63.674 1.00 23.77 ? 391  VAL A CG2   1 
ATOM   7372 N N     . ALA B 1 394 ? 31.786 -10.154 -62.666 1.00 24.80 ? 392  ALA A N     1 
ATOM   7373 C CA    . ALA B 1 394 ? 30.685 -11.110 -62.405 1.00 23.94 ? 392  ALA A CA    1 
ATOM   7374 C C     . ALA B 1 394 ? 30.937 -11.838 -61.086 1.00 23.19 ? 392  ALA A C     1 
ATOM   7375 O O     . ALA B 1 394 ? 29.967 -12.072 -60.340 1.00 22.36 ? 392  ALA A O     1 
ATOM   7376 C CB    . ALA B 1 394 ? 30.507 -12.089 -63.529 1.00 25.71 ? 392  ALA A CB    1 
ATOM   7377 N N     . LEU B 1 395 ? 32.188 -12.185 -60.812 1.00 24.25 ? 393  LEU A N     1 
ATOM   7378 C CA    . LEU B 1 395 ? 32.594 -12.891 -59.578 1.00 23.66 ? 393  LEU A CA    1 
ATOM   7379 C C     . LEU B 1 395 ? 32.491 -11.954 -58.361 1.00 22.73 ? 393  LEU A C     1 
ATOM   7380 O O     . LEU B 1 395 ? 31.975 -12.389 -57.318 1.00 20.68 ? 393  LEU A O     1 
ATOM   7381 C CB    . LEU B 1 395 ? 34.022 -13.413 -59.720 1.00 24.95 ? 393  LEU A CB    1 
ATOM   7382 C CG    . LEU B 1 395 ? 34.563 -14.068 -58.452 1.00 23.96 ? 393  LEU A CG    1 
ATOM   7383 C CD1   . LEU B 1 395 ? 33.872 -15.394 -58.206 1.00 26.67 ? 393  LEU A CD1   1 
ATOM   7384 C CD2   . LEU B 1 395 ? 36.056 -14.272 -58.533 1.00 25.11 ? 393  LEU A CD2   1 
ATOM   7385 N N     . LEU B 1 396 ? 32.961 -10.718 -58.492 1.00 22.96 ? 394  LEU A N     1 
ATOM   7386 C CA    . LEU B 1 396 ? 33.280 -9.875  -57.321 1.00 23.01 ? 394  LEU A CA    1 
ATOM   7387 C C     . LEU B 1 396 ? 32.123 -8.939  -56.972 1.00 23.90 ? 394  LEU A C     1 
ATOM   7388 O O     . LEU B 1 396 ? 32.058 -8.591  -55.797 1.00 21.28 ? 394  LEU A O     1 
ATOM   7389 C CB    . LEU B 1 396 ? 34.563 -9.092  -57.582 1.00 23.07 ? 394  LEU A CB    1 
ATOM   7390 C CG    . LEU B 1 396 ? 35.849 -9.928  -57.698 1.00 23.94 ? 394  LEU A CG    1 
ATOM   7391 C CD1   . LEU B 1 396 ? 37.056 -9.032  -57.897 1.00 22.43 ? 394  LEU A CD1   1 
ATOM   7392 C CD2   . LEU B 1 396 ? 36.041 -10.803 -56.478 1.00 25.02 ? 394  LEU A CD2   1 
ATOM   7393 N N     . THR B 1 397 ? 31.244 -8.545  -57.905 1.00 22.34 ? 395  THR A N     1 
ATOM   7394 C CA    . THR B 1 397 ? 30.138 -7.600  -57.560 1.00 22.83 ? 395  THR A CA    1 
ATOM   7395 C C     . THR B 1 397 ? 29.204 -8.196  -56.506 1.00 22.46 ? 395  THR A C     1 
ATOM   7396 O O     . THR B 1 397 ? 28.816 -7.478  -55.591 1.00 22.07 ? 395  THR A O     1 
ATOM   7397 C CB    . THR B 1 397 ? 29.404 -7.022  -58.775 1.00 22.72 ? 395  THR A CB    1 
ATOM   7398 O OG1   . THR B 1 397 ? 29.027 -8.061  -59.667 1.00 26.14 ? 395  THR A OG1   1 
ATOM   7399 C CG2   . THR B 1 397 ? 30.261 -6.009  -59.503 1.00 23.77 ? 395  THR A CG2   1 
ATOM   7400 N N     . PRO B 1 398 ? 28.801 -9.488  -56.527 1.00 21.71 ? 396  PRO A N     1 
ATOM   7401 C CA    . PRO B 1 398 ? 27.978 -10.012 -55.439 1.00 21.50 ? 396  PRO A CA    1 
ATOM   7402 C C     . PRO B 1 398 ? 28.707 -9.972  -54.102 1.00 21.77 ? 396  PRO A C     1 
ATOM   7403 O O     . PRO B 1 398 ? 28.081 -9.748  -53.091 1.00 20.42 ? 396  PRO A O     1 
ATOM   7404 C CB    . PRO B 1 398 ? 27.622 -11.465 -55.792 1.00 21.75 ? 396  PRO A CB    1 
ATOM   7405 C CG    . PRO B 1 398 ? 28.382 -11.761 -57.102 1.00 23.33 ? 396  PRO A CG    1 
ATOM   7406 C CD    . PRO B 1 398 ? 28.966 -10.456 -57.621 1.00 22.98 ? 396  PRO A CD    1 
ATOM   7407 N N     . VAL B 1 399 ? 30.007 -10.241 -54.130 1.00 22.21 ? 397  VAL A N     1 
ATOM   7408 C CA    . VAL B 1 399 ? 30.839 -10.169 -52.913 1.00 21.89 ? 397  VAL A CA    1 
ATOM   7409 C C     . VAL B 1 399 ? 30.801 -8.723  -52.411 1.00 21.87 ? 397  VAL A C     1 
ATOM   7410 O O     . VAL B 1 399 ? 30.545 -8.532  -51.217 1.00 21.95 ? 397  VAL A O     1 
ATOM   7411 C CB    . VAL B 1 399 ? 32.271 -10.671 -53.146 1.00 20.98 ? 397  VAL A CB    1 
ATOM   7412 C CG1   . VAL B 1 399 ? 33.065 -10.563 -51.859 1.00 22.93 ? 397  VAL A CG1   1 
ATOM   7413 C CG2   . VAL B 1 399 ? 32.280 -12.109 -53.661 1.00 22.62 ? 397  VAL A CG2   1 
ATOM   7414 N N     . ALA B 1 400 ? 31.042 -7.737  -53.264 1.00 21.42 ? 398  ALA A N     1 
ATOM   7415 C CA    . ALA B 1 400 ? 31.002 -6.314  -52.842 1.00 21.86 ? 398  ALA A CA    1 
ATOM   7416 C C     . ALA B 1 400 ? 29.641 -5.993  -52.210 1.00 22.55 ? 398  ALA A C     1 
ATOM   7417 O O     . ALA B 1 400 ? 29.583 -5.352  -51.129 1.00 26.40 ? 398  ALA A O     1 
ATOM   7418 C CB    . ALA B 1 400 ? 31.267 -5.423  -54.017 1.00 22.42 ? 398  ALA A CB    1 
ATOM   7419 N N     . LYS B 1 401 ? 28.559 -6.416  -52.859 1.00 21.80 ? 399  LYS A N     1 
ATOM   7420 C CA    . LYS B 1 401 ? 27.187 -6.159  -52.374 1.00 20.21 ? 399  LYS A CA    1 
ATOM   7421 C C     . LYS B 1 401 ? 27.016 -6.726  -50.961 1.00 18.81 ? 399  LYS A C     1 
ATOM   7422 O O     . LYS B 1 401 ? 26.746 -5.943  -50.035 1.00 17.58 ? 399  LYS A O     1 
ATOM   7423 C CB    . LYS B 1 401 ? 26.173 -6.739  -53.351 1.00 20.48 ? 399  LYS A CB    1 
ATOM   7424 C CG    . LYS B 1 401 ? 24.793 -6.111  -53.231 1.00 22.00 ? 399  LYS A CG    1 
ATOM   7425 C CD    . LYS B 1 401 ? 24.071 -6.401  -51.933 1.00 20.46 ? 399  LYS A CD    1 
ATOM   7426 C CE    . LYS B 1 401 ? 22.587 -6.141  -52.060 1.00 20.41 ? 399  LYS A CE    1 
ATOM   7427 N NZ    . LYS B 1 401 ? 21.881 -6.215  -50.760 1.00 21.17 ? 399  LYS A NZ    1 
ATOM   7428 N N     . ALA B 1 402 ? 27.133 -8.043  -50.788 1.00 18.30 ? 400  ALA A N     1 
ATOM   7429 C CA    . ALA B 1 402 ? 26.789 -8.718  -49.524 1.00 18.14 ? 400  ALA A CA    1 
ATOM   7430 C C     . ALA B 1 402 ? 27.845 -8.494  -48.450 1.00 18.19 ? 400  ALA A C     1 
ATOM   7431 O O     . ALA B 1 402 ? 27.467 -8.323  -47.254 1.00 19.68 ? 400  ALA A O     1 
ATOM   7432 C CB    . ALA B 1 402 ? 26.555 -10.195 -49.740 1.00 18.95 ? 400  ALA A CB    1 
ATOM   7433 N N     . PHE B 1 403 ? 29.129 -8.532  -48.807 1.00 18.88 ? 401  PHE A N     1 
ATOM   7434 C CA    . PHE B 1 403 ? 30.201 -8.476  -47.796 1.00 18.65 ? 401  PHE A CA    1 
ATOM   7435 C C     . PHE B 1 403 ? 30.347 -7.057  -47.259 1.00 18.75 ? 401  PHE A C     1 
ATOM   7436 O O     . PHE B 1 403 ? 30.427 -6.908  -46.038 1.00 19.08 ? 401  PHE A O     1 
ATOM   7437 C CB    . PHE B 1 403 ? 31.534 -9.023  -48.300 1.00 19.23 ? 401  PHE A CB    1 
ATOM   7438 C CG    . PHE B 1 403 ? 32.477 -9.377  -47.176 1.00 19.45 ? 401  PHE A CG    1 
ATOM   7439 C CD1   . PHE B 1 403 ? 32.167 -10.383 -46.287 1.00 20.80 ? 401  PHE A CD1   1 
ATOM   7440 C CD2   . PHE B 1 403 ? 33.684 -8.705  -47.011 1.00 20.77 ? 401  PHE A CD2   1 
ATOM   7441 C CE1   . PHE B 1 403 ? 33.031 -10.725 -45.254 1.00 21.13 ? 401  PHE A CE1   1 
ATOM   7442 C CE2   . PHE B 1 403 ? 34.557 -9.063  -45.996 1.00 20.33 ? 401  PHE A CE2   1 
ATOM   7443 C CZ    . PHE B 1 403 ? 34.230 -10.068 -45.115 1.00 21.69 ? 401  PHE A CZ    1 
ATOM   7444 N N     . LEU B 1 404 ? 30.373 -6.039  -48.103 1.00 21.06 ? 402  LEU A N     1 
ATOM   7445 C CA    . LEU B 1 404 ? 30.541 -4.655  -47.584 1.00 21.16 ? 402  LEU A CA    1 
ATOM   7446 C C     . LEU B 1 404 ? 29.328 -4.264  -46.729 1.00 22.42 ? 402  LEU A C     1 
ATOM   7447 O O     . LEU B 1 404 ? 29.509 -3.504  -45.762 1.00 22.65 ? 402  LEU A O     1 
ATOM   7448 C CB    . LEU B 1 404 ? 30.756 -3.666  -48.725 1.00 22.10 ? 402  LEU A CB    1 
ATOM   7449 C CG    . LEU B 1 404 ? 32.214 -3.406  -49.118 1.00 25.30 ? 402  LEU A CG    1 
ATOM   7450 C CD1   . LEU B 1 404 ? 32.872 -4.651  -49.697 1.00 25.60 ? 402  LEU A CD1   1 
ATOM   7451 C CD2   . LEU B 1 404 ? 32.292 -2.270  -50.106 1.00 27.22 ? 402  LEU A CD2   1 
ATOM   7452 N N     . THR B 1 405 ? 28.132 -4.741  -47.054 1.00 22.37 ? 403  THR A N     1 
ATOM   7453 C CA    . THR B 1 405 ? 26.895 -4.402  -46.279 1.00 21.31 ? 403  THR A CA    1 
ATOM   7454 C C     . THR B 1 405 ? 26.887 -5.174  -44.946 1.00 21.36 ? 403  THR A C     1 
ATOM   7455 O O     . THR B 1 405 ? 26.611 -4.547  -43.880 1.00 19.36 ? 403  THR A O     1 
ATOM   7456 C CB    . THR B 1 405 ? 25.636 -4.573  -47.144 1.00 20.19 ? 403  THR A CB    1 
ATOM   7457 O OG1   . THR B 1 405 ? 25.526 -5.927  -47.583 1.00 19.18 ? 403  THR A OG1   1 
ATOM   7458 C CG2   . THR B 1 405 ? 25.640 -3.642  -48.334 1.00 19.95 ? 403  THR A CG2   1 
ATOM   7459 N N     . ASP B 1 406 ? 27.210 -6.475  -44.954 1.00 21.15 ? 404  ASP A N     1 
ATOM   7460 C CA    . ASP B 1 406 ? 27.307 -7.277  -43.712 1.00 21.38 ? 404  ASP A CA    1 
ATOM   7461 C C     . ASP B 1 406 ? 28.419 -6.719  -42.796 1.00 22.17 ? 404  ASP A C     1 
ATOM   7462 O O     . ASP B 1 406 ? 28.184 -6.604  -41.579 1.00 18.15 ? 404  ASP A O     1 
ATOM   7463 C CB    . ASP B 1 406 ? 27.535 -8.756  -44.014 1.00 21.85 ? 404  ASP A CB    1 
ATOM   7464 C CG    . ASP B 1 406 ? 26.294 -9.486  -44.474 1.00 22.21 ? 404  ASP A CG    1 
ATOM   7465 O OD1   . ASP B 1 406 ? 25.215 -8.854  -44.573 1.00 21.56 ? 404  ASP A OD1   1 
ATOM   7466 O OD2   . ASP B 1 406 ? 26.411 -10.695 -44.725 1.00 25.09 ? 404  ASP A OD2   1 
ATOM   7467 N N     . MET B 1 407 ? 29.574 -6.344  -43.348 1.00 21.60 ? 405  MET A N     1 
ATOM   7468 C CA    . MET B 1 407 ? 30.683 -5.755  -42.545 1.00 21.57 ? 405  MET A CA    1 
ATOM   7469 C C     . MET B 1 407 ? 30.318 -4.325  -42.114 1.00 20.75 ? 405  MET A C     1 
ATOM   7470 O O     . MET B 1 407 ? 30.671 -3.899  -40.974 1.00 21.23 ? 405  MET A O     1 
ATOM   7471 C CB    . MET B 1 407 ? 31.999 -5.755  -43.327 1.00 21.68 ? 405  MET A CB    1 
ATOM   7472 C CG    . MET B 1 407 ? 32.530 -7.131  -43.652 1.00 21.90 ? 405  MET A CG    1 
ATOM   7473 S SD    . MET B 1 407 ? 32.850 -8.140  -42.181 1.00 25.76 ? 405  MET A SD    1 
ATOM   7474 C CE    . MET B 1 407 ? 31.427 -9.228  -42.207 1.00 26.28 ? 405  MET A CE    1 
ATOM   7475 N N     . GLY B 1 408 ? 29.620 -3.593  -42.960 1.00 19.97 ? 406  GLY A N     1 
ATOM   7476 C CA    . GLY B 1 408 ? 29.128 -2.257  -42.579 1.00 20.67 ? 406  GLY A CA    1 
ATOM   7477 C C     . GLY B 1 408 ? 28.202 -2.365  -41.372 1.00 22.26 ? 406  GLY A C     1 
ATOM   7478 O O     . GLY B 1 408 ? 28.298 -1.510  -40.469 1.00 22.12 ? 406  GLY A O     1 
ATOM   7479 N N     . LEU B 1 409 ? 27.351 -3.406  -41.315 1.00 22.80 ? 407  LEU A N     1 
ATOM   7480 C CA    . LEU B 1 409 ? 26.399 -3.529  -40.195 1.00 23.78 ? 407  LEU A CA    1 
ATOM   7481 C C     . LEU B 1 409 ? 27.191 -3.778  -38.911 1.00 23.05 ? 407  LEU A C     1 
ATOM   7482 O O     . LEU B 1 409 ? 26.941 -3.076  -37.914 1.00 21.34 ? 407  LEU A O     1 
ATOM   7483 C CB    . LEU B 1 409 ? 25.374 -4.647  -40.386 1.00 24.80 ? 407  LEU A CB    1 
ATOM   7484 C CG    . LEU B 1 409 ? 24.416 -4.769  -39.191 1.00 24.31 ? 407  LEU A CG    1 
ATOM   7485 C CD1   . LEU B 1 409 ? 23.645 -3.476  -38.984 1.00 24.71 ? 407  LEU A CD1   1 
ATOM   7486 C CD2   . LEU B 1 409 ? 23.471 -5.940  -39.356 1.00 25.22 ? 407  LEU A CD2   1 
ATOM   7487 N N     . GLU B 1 410 ? 28.118 -4.728  -38.946 1.00 23.01 ? 408  GLU A N     1 
ATOM   7488 C CA    . GLU B 1 410 ? 28.962 -5.014  -37.769 1.00 23.03 ? 408  GLU A CA    1 
ATOM   7489 C C     . GLU B 1 410 ? 29.671 -3.714  -37.351 1.00 22.57 ? 408  GLU A C     1 
ATOM   7490 O O     . GLU B 1 410 ? 29.739 -3.417  -36.125 1.00 20.76 ? 408  GLU A O     1 
ATOM   7491 C CB    . GLU B 1 410 ? 29.936 -6.143  -38.068 1.00 23.80 ? 408  GLU A CB    1 
ATOM   7492 C CG    . GLU B 1 410 ? 30.735 -6.449  -36.848 1.00 24.29 ? 408  GLU A CG    1 
ATOM   7493 C CD    . GLU B 1 410 ? 31.863 -7.438  -36.946 1.00 26.54 ? 408  GLU A CD    1 
ATOM   7494 O OE1   . GLU B 1 410 ? 32.632 -7.525  -35.940 1.00 26.44 ? 408  GLU A OE1   1 
ATOM   7495 O OE2   . GLU B 1 410 ? 31.964 -8.122  -37.980 1.00 27.25 ? 408  GLU A OE2   1 
ATOM   7496 N N     . THR B 1 411 ? 30.157 -2.958  -38.323 1.00 21.02 ? 409  THR A N     1 
ATOM   7497 C CA    . THR B 1 411 ? 30.934 -1.712  -38.087 1.00 21.76 ? 409  THR A CA    1 
ATOM   7498 C C     . THR B 1 411 ? 30.020 -0.726  -37.358 1.00 21.46 ? 409  THR A C     1 
ATOM   7499 O O     . THR B 1 411 ? 30.457 -0.210  -36.315 1.00 20.88 ? 409  THR A O     1 
ATOM   7500 C CB    . THR B 1 411 ? 31.516 -1.147  -39.387 1.00 21.25 ? 409  THR A CB    1 
ATOM   7501 O OG1   . THR B 1 411 ? 32.405 -2.124  -39.919 1.00 20.13 ? 409  THR A OG1   1 
ATOM   7502 C CG2   . THR B 1 411 ? 32.210 0.177   -39.187 1.00 21.30 ? 409  THR A CG2   1 
ATOM   7503 N N     . THR B 1 412 ? 28.778 -0.545  -37.814 1.00 19.81 ? 410  THR A N     1 
ATOM   7504 C CA    . THR B 1 412 ? 27.854 0.457   -37.207 1.00 20.97 ? 410  THR A CA    1 
ATOM   7505 C C     . THR B 1 412 ? 27.489 0.029   -35.780 1.00 19.80 ? 410  THR A C     1 
ATOM   7506 O O     . THR B 1 412 ? 27.322 0.903   -34.938 1.00 20.25 ? 410  THR A O     1 
ATOM   7507 C CB    . THR B 1 412 ? 26.601 0.717   -38.057 1.00 20.32 ? 410  THR A CB    1 
ATOM   7508 O OG1   . THR B 1 412 ? 25.879 -0.516  -38.185 1.00 21.97 ? 410  THR A OG1   1 
ATOM   7509 C CG2   . THR B 1 412 ? 26.948 1.302   -39.403 1.00 20.41 ? 410  THR A CG2   1 
ATOM   7510 N N     . ILE B 1 413 ? 27.427 -1.267  -35.522 1.00 19.71 ? 411  ILE A N     1 
ATOM   7511 C CA    . ILE B 1 413 ? 27.058 -1.844  -34.209 1.00 22.89 ? 411  ILE A CA    1 
ATOM   7512 C C     . ILE B 1 413 ? 28.216 -1.608  -33.236 1.00 22.51 ? 411  ILE A C     1 
ATOM   7513 O O     . ILE B 1 413 ? 27.950 -1.127  -32.122 1.00 21.04 ? 411  ILE A O     1 
ATOM   7514 C CB    . ILE B 1 413 ? 26.687 -3.328  -34.366 1.00 24.76 ? 411  ILE A CB    1 
ATOM   7515 C CG1   . ILE B 1 413 ? 25.297 -3.462  -35.000 1.00 25.65 ? 411  ILE A CG1   1 
ATOM   7516 C CG2   . ILE B 1 413 ? 26.795 -4.055  -33.027 1.00 25.61 ? 411  ILE A CG2   1 
ATOM   7517 C CD1   . ILE B 1 413 ? 24.949 -4.894  -35.339 1.00 27.65 ? 411  ILE A CD1   1 
ATOM   7518 N N     . HIS B 1 414 ? 29.460 -1.857  -33.657 1.00 21.54 ? 412  HIS A N     1 
ATOM   7519 C CA    . HIS B 1 414 ? 30.659 -1.500  -32.849 1.00 20.91 ? 412  HIS A CA    1 
ATOM   7520 C C     . HIS B 1 414 ? 30.647 0.004   -32.570 1.00 21.23 ? 412  HIS A C     1 
ATOM   7521 O O     . HIS B 1 414 ? 30.925 0.377   -31.411 1.00 23.67 ? 412  HIS A O     1 
ATOM   7522 C CB    . HIS B 1 414 ? 31.973 -1.904  -33.518 1.00 20.53 ? 412  HIS A CB    1 
ATOM   7523 C CG    . HIS B 1 414 ? 32.187 -3.363  -33.589 1.00 19.64 ? 412  HIS A CG    1 
ATOM   7524 N ND1   . HIS B 1 414 ? 31.933 -4.186  -32.533 1.00 22.35 ? 412  HIS A ND1   1 
ATOM   7525 C CD2   . HIS B 1 414 ? 32.616 -4.146  -34.602 1.00 24.09 ? 412  HIS A CD2   1 
ATOM   7526 C CE1   . HIS B 1 414 ? 32.162 -5.435  -32.879 1.00 25.62 ? 412  HIS A CE1   1 
ATOM   7527 N NE2   . HIS B 1 414 ? 32.593 -5.446  -34.156 1.00 23.25 ? 412  HIS A NE2   1 
ATOM   7528 N N     . GLY B 1 415 ? 30.346 0.823   -33.579 1.00 19.01 ? 413  GLY A N     1 
ATOM   7529 C CA    . GLY B 1 415 ? 30.344 2.293   -33.469 1.00 19.32 ? 413  GLY A CA    1 
ATOM   7530 C C     . GLY B 1 415 ? 29.368 2.769   -32.405 1.00 22.31 ? 413  GLY A C     1 
ATOM   7531 O O     . GLY B 1 415 ? 29.696 3.695   -31.626 1.00 23.63 ? 413  GLY A O     1 
ATOM   7532 N N     . GLN B 1 416 ? 28.186 2.162   -32.370 1.00 21.40 ? 414  GLN A N     1 
ATOM   7533 C CA    . GLN B 1 416 ? 27.180 2.423   -31.320 1.00 21.61 ? 414  GLN A CA    1 
ATOM   7534 C C     . GLN B 1 416 ? 27.680 1.876   -29.966 1.00 20.95 ? 414  GLN A C     1 
ATOM   7535 O O     . GLN B 1 416 ? 27.606 2.597   -28.961 1.00 20.99 ? 414  GLN A O     1 
ATOM   7536 C CB    . GLN B 1 416 ? 25.840 1.834   -31.758 1.00 21.02 ? 414  GLN A CB    1 
ATOM   7537 C CG    . GLN B 1 416 ? 24.779 2.008   -30.671 1.00 23.78 ? 414  GLN A CG    1 
ATOM   7538 C CD    . GLN B 1 416 ? 23.421 1.504   -31.080 1.00 22.70 ? 414  GLN A CD    1 
ATOM   7539 O OE1   . GLN B 1 416 ? 22.384 2.088   -30.762 1.00 29.28 ? 414  GLN A OE1   1 
ATOM   7540 N NE2   . GLN B 1 416 ? 23.409 0.364   -31.720 1.00 20.90 ? 414  GLN A NE2   1 
ATOM   7541 N N     . GLN B 1 417 ? 28.121 0.623   -29.908 1.00 21.69 ? 415  GLN A N     1 
ATOM   7542 C CA    . GLN B 1 417 ? 28.508 -0.039  -28.642 1.00 21.49 ? 415  GLN A CA    1 
ATOM   7543 C C     . GLN B 1 417 ? 29.674 0.697   -27.961 1.00 22.58 ? 415  GLN A C     1 
ATOM   7544 O O     . GLN B 1 417 ? 29.704 0.745   -26.711 1.00 21.54 ? 415  GLN A O     1 
ATOM   7545 C CB    . GLN B 1 417 ? 28.836 -1.499  -28.930 1.00 22.17 ? 415  GLN A CB    1 
ATOM   7546 C CG    . GLN B 1 417 ? 28.822 -2.365  -27.691 1.00 23.55 ? 415  GLN A CG    1 
ATOM   7547 C CD    . GLN B 1 417 ? 27.446 -2.530  -27.084 1.00 24.29 ? 415  GLN A CD    1 
ATOM   7548 O OE1   . GLN B 1 417 ? 26.422 -2.246  -27.703 1.00 24.55 ? 415  GLN A OE1   1 
ATOM   7549 N NE2   . GLN B 1 417 ? 27.427 -2.972  -25.835 1.00 23.97 ? 415  GLN A NE2   1 
ATOM   7550 N N     . ILE B 1 418 ? 30.593 1.266   -28.725 1.00 22.25 ? 416  ILE A N     1 
ATOM   7551 C CA    . ILE B 1 418 ? 31.690 2.102   -28.154 1.00 25.02 ? 416  ILE A CA    1 
ATOM   7552 C C     . ILE B 1 418 ? 31.115 3.195   -27.242 1.00 25.40 ? 416  ILE A C     1 
ATOM   7553 O O     . ILE B 1 418 ? 31.724 3.460   -26.223 1.00 25.44 ? 416  ILE A O     1 
ATOM   7554 C CB    . ILE B 1 418 ? 32.582 2.663   -29.269 1.00 24.52 ? 416  ILE A CB    1 
ATOM   7555 C CG1   . ILE B 1 418 ? 33.533 1.578   -29.780 1.00 23.24 ? 416  ILE A CG1   1 
ATOM   7556 C CG2   . ILE B 1 418 ? 33.351 3.890   -28.807 1.00 25.06 ? 416  ILE A CG2   1 
ATOM   7557 C CD1   . ILE B 1 418 ? 34.035 1.821   -31.171 1.00 25.34 ? 416  ILE A CD1   1 
ATOM   7558 N N     . PHE B 1 419 ? 29.957 3.757   -27.562 1.00 25.49 ? 417  PHE A N     1 
ATOM   7559 C CA    . PHE B 1 419 ? 29.344 4.868   -26.796 1.00 25.89 ? 417  PHE A CA    1 
ATOM   7560 C C     . PHE B 1 419 ? 28.678 4.360   -25.498 1.00 24.19 ? 417  PHE A C     1 
ATOM   7561 O O     . PHE B 1 419 ? 28.226 5.190   -24.702 1.00 23.30 ? 417  PHE A O     1 
ATOM   7562 C CB    . PHE B 1 419 ? 28.308 5.608   -27.646 1.00 23.76 ? 417  PHE A CB    1 
ATOM   7563 C CG    . PHE B 1 419 ? 28.839 6.611   -28.629 1.00 24.29 ? 417  PHE A CG    1 
ATOM   7564 C CD1   . PHE B 1 419 ? 29.624 6.211   -29.704 1.00 24.50 ? 417  PHE A CD1   1 
ATOM   7565 C CD2   . PHE B 1 419 ? 28.498 7.947   -28.521 1.00 24.07 ? 417  PHE A CD2   1 
ATOM   7566 C CE1   . PHE B 1 419 ? 30.077 7.128   -30.638 1.00 22.46 ? 417  PHE A CE1   1 
ATOM   7567 C CE2   . PHE B 1 419 ? 28.964 8.865   -29.444 1.00 24.39 ? 417  PHE A CE2   1 
ATOM   7568 C CZ    . PHE B 1 419 ? 29.756 8.454   -30.496 1.00 23.60 ? 417  PHE A CZ    1 
ATOM   7569 N N     . GLY B 1 420 ? 28.618 3.045   -25.282 1.00 23.36 ? 418  GLY A N     1 
ATOM   7570 C CA    . GLY B 1 420 ? 27.803 2.433   -24.227 1.00 22.39 ? 418  GLY A CA    1 
ATOM   7571 C C     . GLY B 1 420 ? 26.350 2.880   -24.328 1.00 23.59 ? 418  GLY A C     1 
ATOM   7572 O O     . GLY B 1 420 ? 25.811 2.959   -25.456 1.00 22.48 ? 418  GLY A O     1 
ATOM   7573 N N     . GLY B 1 421 ? 25.750 3.239   -23.190 1.00 24.26 ? 419  GLY A N     1 
ATOM   7574 C CA    . GLY B 1 421 ? 24.341 3.664   -23.122 1.00 24.28 ? 419  GLY A CA    1 
ATOM   7575 C C     . GLY B 1 421 ? 24.099 4.931   -23.910 1.00 24.75 ? 419  GLY A C     1 
ATOM   7576 O O     . GLY B 1 421 ? 23.005 5.078   -24.489 1.00 23.35 ? 419  GLY A O     1 
ATOM   7577 N N     . HIS B 1 422 ? 25.079 5.831   -23.978 1.00 23.72 ? 420  HIS A N     1 
ATOM   7578 C CA    . HIS B 1 422 ? 24.949 7.072   -24.790 1.00 24.19 ? 420  HIS A CA    1 
ATOM   7579 C C     . HIS B 1 422 ? 24.686 6.728   -26.270 1.00 21.08 ? 420  HIS A C     1 
ATOM   7580 O O     . HIS B 1 422 ? 24.032 7.515   -26.938 1.00 23.82 ? 420  HIS A O     1 
ATOM   7581 C CB    . HIS B 1 422 ? 26.188 7.970   -24.635 1.00 24.70 ? 420  HIS A CB    1 
ATOM   7582 C CG    . HIS B 1 422 ? 26.277 8.635   -23.307 1.00 24.34 ? 420  HIS A CG    1 
ATOM   7583 N ND1   . HIS B 1 422 ? 26.066 9.992   -23.146 1.00 31.16 ? 420  HIS A ND1   1 
ATOM   7584 C CD2   . HIS B 1 422 ? 26.587 8.154   -22.095 1.00 24.57 ? 420  HIS A CD2   1 
ATOM   7585 C CE1   . HIS B 1 422 ? 26.217 10.301  -21.875 1.00 29.07 ? 420  HIS A CE1   1 
ATOM   7586 N NE2   . HIS B 1 422 ? 26.532 9.203   -21.213 1.00 28.75 ? 420  HIS A NE2   1 
ATOM   7587 N N     . GLY B 1 423 ? 25.152 5.581   -26.764 1.00 23.44 ? 421  GLY A N     1 
ATOM   7588 C CA    . GLY B 1 423 ? 24.991 5.176   -28.181 1.00 22.78 ? 421  GLY A CA    1 
ATOM   7589 C C     . GLY B 1 423 ? 23.537 4.844   -28.506 1.00 20.83 ? 421  GLY A C     1 
ATOM   7590 O O     . GLY B 1 423 ? 23.153 4.874   -29.715 1.00 20.65 ? 421  GLY A O     1 
ATOM   7591 N N     . PHE B 1 424 ? 22.719 4.635   -27.474 1.00 22.11 ? 422  PHE A N     1 
ATOM   7592 C CA    . PHE B 1 424 ? 21.276 4.298   -27.629 1.00 22.15 ? 422  PHE A CA    1 
ATOM   7593 C C     . PHE B 1 424 ? 20.481 5.595   -27.767 1.00 24.23 ? 422  PHE A C     1 
ATOM   7594 O O     . PHE B 1 424 ? 19.269 5.549   -28.101 1.00 22.93 ? 422  PHE A O     1 
ATOM   7595 C CB    . PHE B 1 424 ? 20.801 3.416   -26.475 1.00 23.15 ? 422  PHE A CB    1 
ATOM   7596 C CG    . PHE B 1 424 ? 19.554 2.608   -26.754 1.00 23.64 ? 422  PHE A CG    1 
ATOM   7597 C CD1   . PHE B 1 424 ? 19.606 1.445   -27.511 1.00 22.35 ? 422  PHE A CD1   1 
ATOM   7598 C CD2   . PHE B 1 424 ? 18.326 2.994   -26.235 1.00 22.73 ? 422  PHE A CD2   1 
ATOM   7599 C CE1   . PHE B 1 424 ? 18.471 0.685   -27.739 1.00 23.35 ? 422  PHE A CE1   1 
ATOM   7600 C CE2   . PHE B 1 424 ? 17.188 2.232   -26.467 1.00 21.23 ? 422  PHE A CE2   1 
ATOM   7601 C CZ    . PHE B 1 424 ? 17.257 1.081   -27.214 1.00 22.93 ? 422  PHE A CZ    1 
ATOM   7602 N N     . ILE B 1 425 ? 21.142 6.733   -27.563 1.00 24.40 ? 423  ILE A N     1 
ATOM   7603 C CA    . ILE B 1 425 ? 20.449 8.053   -27.634 1.00 24.22 ? 423  ILE A CA    1 
ATOM   7604 C C     . ILE B 1 425 ? 20.550 8.588   -29.068 1.00 25.52 ? 423  ILE A C     1 
ATOM   7605 O O     . ILE B 1 425 ? 21.655 8.601   -29.600 1.00 25.10 ? 423  ILE A O     1 
ATOM   7606 C CB    . ILE B 1 425 ? 21.011 9.023   -26.576 1.00 26.44 ? 423  ILE A CB    1 
ATOM   7607 C CG1   . ILE B 1 425 ? 21.067 8.378   -25.190 1.00 27.23 ? 423  ILE A CG1   1 
ATOM   7608 C CG2   . ILE B 1 425 ? 20.228 10.325  -26.560 1.00 26.10 ? 423  ILE A CG2   1 
ATOM   7609 C CD1   . ILE B 1 425 ? 19.778 7.726   -24.765 1.00 28.01 ? 423  ILE A CD1   1 
ATOM   7610 N N     . ARG B 1 426 ? 19.435 9.054   -29.637 1.00 22.86 ? 424  ARG A N     1 
ATOM   7611 C CA    . ARG B 1 426 ? 19.415 9.437   -31.075 1.00 24.63 ? 424  ARG A CA    1 
ATOM   7612 C C     . ARG B 1 426 ? 20.300 10.653  -31.393 1.00 25.56 ? 424  ARG A C     1 
ATOM   7613 O O     . ARG B 1 426 ? 20.827 10.700  -32.502 1.00 24.68 ? 424  ARG A O     1 
ATOM   7614 C CB    . ARG B 1 426 ? 17.967 9.637   -31.536 1.00 23.41 ? 424  ARG A CB    1 
ATOM   7615 C CG    . ARG B 1 426 ? 17.082 8.416   -31.340 1.00 23.22 ? 424  ARG A CG    1 
ATOM   7616 C CD    . ARG B 1 426 ? 15.986 8.298   -32.381 1.00 23.69 ? 424  ARG A CD    1 
ATOM   7617 N NE    . ARG B 1 426 ? 15.095 9.446   -32.398 1.00 25.28 ? 424  ARG A NE    1 
ATOM   7618 C CZ    . ARG B 1 426 ? 14.001 9.562   -31.657 1.00 24.98 ? 424  ARG A CZ    1 
ATOM   7619 N NH1   . ARG B 1 426 ? 13.255 10.648  -31.748 1.00 25.90 ? 424  ARG A NH1   1 
ATOM   7620 N NH2   . ARG B 1 426 ? 13.652 8.594   -30.832 1.00 24.61 ? 424  ARG A NH2   1 
ATOM   7621 N N     . GLU B 1 427 ? 20.442 11.588  -30.459 1.00 25.13 ? 425  GLU A N     1 
ATOM   7622 C CA    . GLU B 1 427 ? 21.216 12.831  -30.716 1.00 24.86 ? 425  GLU A CA    1 
ATOM   7623 C C     . GLU B 1 427 ? 22.685 12.534  -31.080 1.00 24.05 ? 425  GLU A C     1 
ATOM   7624 O O     . GLU B 1 427 ? 23.309 13.400  -31.671 1.00 23.05 ? 425  GLU A O     1 
ATOM   7625 C CB    . GLU B 1 427 ? 21.126 13.776  -29.517 1.00 26.92 ? 425  GLU A CB    1 
ATOM   7626 C CG    . GLU B 1 427 ? 19.812 14.527  -29.426 1.00 31.78 ? 425  GLU A CG    1 
ATOM   7627 C CD    . GLU B 1 427 ? 18.690 13.828  -28.676 1.00 33.76 ? 425  GLU A CD    1 
ATOM   7628 O OE1   . GLU B 1 427 ? 17.688 14.499  -28.381 1.00 38.46 ? 425  GLU A OE1   1 
ATOM   7629 O OE2   . GLU B 1 427 ? 18.811 12.621  -28.406 1.00 27.53 ? 425  GLU A OE2   1 
ATOM   7630 N N     . TRP B 1 428 ? 23.200 11.358  -30.720 1.00 23.88 ? 426  TRP A N     1 
ATOM   7631 C CA    . TRP B 1 428 ? 24.613 10.999  -31.019 1.00 25.68 ? 426  TRP A CA    1 
ATOM   7632 C C     . TRP B 1 428 ? 24.748 10.445  -32.445 1.00 24.82 ? 426  TRP A C     1 
ATOM   7633 O O     . TRP B 1 428 ? 25.877 10.350  -32.906 1.00 25.11 ? 426  TRP A O     1 
ATOM   7634 C CB    . TRP B 1 428 ? 25.182 10.065  -29.951 1.00 26.61 ? 426  TRP A CB    1 
ATOM   7635 C CG    . TRP B 1 428 ? 25.333 10.718  -28.616 1.00 29.71 ? 426  TRP A CG    1 
ATOM   7636 C CD1   . TRP B 1 428 ? 24.518 10.578  -27.532 1.00 31.90 ? 426  TRP A CD1   1 
ATOM   7637 C CD2   . TRP B 1 428 ? 26.367 11.636  -28.228 1.00 30.60 ? 426  TRP A CD2   1 
ATOM   7638 N NE1   . TRP B 1 428 ? 24.977 11.341  -26.496 1.00 33.65 ? 426  TRP A NE1   1 
ATOM   7639 C CE2   . TRP B 1 428 ? 26.110 12.001  -26.892 1.00 33.88 ? 426  TRP A CE2   1 
ATOM   7640 C CE3   . TRP B 1 428 ? 27.481 12.179  -28.876 1.00 33.25 ? 426  TRP A CE3   1 
ATOM   7641 C CZ2   . TRP B 1 428 ? 26.931 12.884  -26.195 1.00 33.29 ? 426  TRP A CZ2   1 
ATOM   7642 C CZ3   . TRP B 1 428 ? 28.292 13.051  -28.186 1.00 33.53 ? 426  TRP A CZ3   1 
ATOM   7643 C CH2   . TRP B 1 428 ? 28.016 13.398  -26.865 1.00 34.92 ? 426  TRP A CH2   1 
ATOM   7644 N N     . GLY B 1 429 ? 23.640 10.078  -33.097 1.00 23.12 ? 427  GLY A N     1 
ATOM   7645 C CA    . GLY B 1 429 ? 23.673 9.679   -34.519 1.00 22.51 ? 427  GLY A CA    1 
ATOM   7646 C C     . GLY B 1 429 ? 24.063 8.236   -34.802 1.00 20.24 ? 427  GLY A C     1 
ATOM   7647 O O     . GLY B 1 429 ? 23.814 7.786   -35.920 1.00 21.21 ? 427  GLY A O     1 
ATOM   7648 N N     . GLN B 1 430 ? 24.633 7.550   -33.827 1.00 19.35 ? 428  GLN A N     1 
ATOM   7649 C CA    . GLN B 1 430 ? 25.143 6.173   -34.051 1.00 20.26 ? 428  GLN A CA    1 
ATOM   7650 C C     . GLN B 1 430 ? 23.993 5.181   -34.287 1.00 22.12 ? 428  GLN A C     1 
ATOM   7651 O O     . GLN B 1 430 ? 24.142 4.290   -35.120 1.00 22.47 ? 428  GLN A O     1 
ATOM   7652 C CB    . GLN B 1 430 ? 26.014 5.760   -32.868 1.00 21.79 ? 428  GLN A CB    1 
ATOM   7653 C CG    . GLN B 1 430 ? 27.267 6.610   -32.704 1.00 21.10 ? 428  GLN A CG    1 
ATOM   7654 C CD    . GLN B 1 430 ? 28.197 6.506   -33.889 1.00 21.82 ? 428  GLN A CD    1 
ATOM   7655 O OE1   . GLN B 1 430 ? 27.935 7.049   -34.956 1.00 22.49 ? 428  GLN A OE1   1 
ATOM   7656 N NE2   . GLN B 1 430 ? 29.301 5.801   -33.706 1.00 22.75 ? 428  GLN A NE2   1 
ATOM   7657 N N     . GLU B 1 431 ? 22.901 5.337   -33.551 1.00 22.45 ? 429  GLU A N     1 
ATOM   7658 C CA    . GLU B 1 431 ? 21.766 4.388   -33.671 1.00 20.86 ? 429  GLU A CA    1 
ATOM   7659 C C     . GLU B 1 431 ? 21.139 4.516   -35.075 1.00 21.35 ? 429  GLU A C     1 
ATOM   7660 O O     . GLU B 1 431 ? 20.751 3.499   -35.635 1.00 20.94 ? 429  GLU A O     1 
ATOM   7661 C CB    . GLU B 1 431 ? 20.788 4.590   -32.508 1.00 20.36 ? 429  GLU A CB    1 
ATOM   7662 C CG    . GLU B 1 431 ? 20.093 5.937   -32.499 1.00 21.58 ? 429  GLU A CG    1 
ATOM   7663 C CD    . GLU B 1 431 ? 18.844 5.998   -33.361 1.00 21.42 ? 429  GLU A CD    1 
ATOM   7664 O OE1   . GLU B 1 431 ? 18.177 4.963   -33.502 1.00 20.72 ? 429  GLU A OE1   1 
ATOM   7665 O OE2   . GLU B 1 431 ? 18.559 7.070   -33.900 1.00 22.22 ? 429  GLU A OE2   1 
ATOM   7666 N N     . GLN B 1 432 ? 21.082 5.733   -35.615 1.00 21.17 ? 430  GLN A N     1 
ATOM   7667 C CA    . GLN B 1 432 ? 20.502 5.949   -36.963 1.00 21.21 ? 430  GLN A CA    1 
ATOM   7668 C C     . GLN B 1 432 ? 21.334 5.216   -38.023 1.00 23.27 ? 430  GLN A C     1 
ATOM   7669 O O     . GLN B 1 432 ? 20.746 4.666   -38.945 1.00 20.84 ? 430  GLN A O     1 
ATOM   7670 C CB    . GLN B 1 432 ? 20.434 7.435   -37.314 1.00 21.40 ? 430  GLN A CB    1 
ATOM   7671 C CG    . GLN B 1 432 ? 19.850 7.683   -38.695 1.00 23.42 ? 430  GLN A CG    1 
ATOM   7672 C CD    . GLN B 1 432 ? 20.040 9.103   -39.160 1.00 23.25 ? 430  GLN A CD    1 
ATOM   7673 O OE1   . GLN B 1 432 ? 19.995 10.039  -38.374 1.00 23.73 ? 430  GLN A OE1   1 
ATOM   7674 N NE2   . GLN B 1 432 ? 20.248 9.268   -40.453 1.00 24.01 ? 430  GLN A NE2   1 
ATOM   7675 N N     . LEU B 1 433 ? 22.660 5.231   -37.866 1.00 23.01 ? 431  LEU A N     1 
ATOM   7676 C CA    . LEU B 1 433 ? 23.551 4.622   -38.886 1.00 20.87 ? 431  LEU A CA    1 
ATOM   7677 C C     . LEU B 1 433 ? 23.333 3.107   -38.903 1.00 21.63 ? 431  LEU A C     1 
ATOM   7678 O O     . LEU B 1 433 ? 23.400 2.528   -39.974 1.00 20.96 ? 431  LEU A O     1 
ATOM   7679 C CB    . LEU B 1 433 ? 24.995 4.991   -38.566 1.00 21.61 ? 431  LEU A CB    1 
ATOM   7680 C CG    . LEU B 1 433 ? 25.318 6.474   -38.715 1.00 21.81 ? 431  LEU A CG    1 
ATOM   7681 C CD1   . LEU B 1 433 ? 26.717 6.778   -38.206 1.00 23.71 ? 431  LEU A CD1   1 
ATOM   7682 C CD2   . LEU B 1 433 ? 25.160 6.914   -40.161 1.00 20.96 ? 431  LEU A CD2   1 
ATOM   7683 N N     . VAL B 1 434 ? 23.075 2.518   -37.743 1.00 20.04 ? 432  VAL A N     1 
ATOM   7684 C CA    . VAL B 1 434 ? 22.727 1.067   -37.711 1.00 20.45 ? 432  VAL A CA    1 
ATOM   7685 C C     . VAL B 1 434 ? 21.437 0.865   -38.519 1.00 22.78 ? 432  VAL A C     1 
ATOM   7686 O O     . VAL B 1 434 ? 21.394 -0.039  -39.341 1.00 21.91 ? 432  VAL A O     1 
ATOM   7687 C CB    . VAL B 1 434 ? 22.557 0.555   -36.269 1.00 21.35 ? 432  VAL A CB    1 
ATOM   7688 C CG1   . VAL B 1 434 ? 22.044 -0.875  -36.236 1.00 20.96 ? 432  VAL A CG1   1 
ATOM   7689 C CG2   . VAL B 1 434 ? 23.833 0.690   -35.455 1.00 21.10 ? 432  VAL A CG2   1 
ATOM   7690 N N     . ARG B 1 435 ? 20.418 1.676   -38.235 1.00 25.00 ? 433  ARG A N     1 
ATOM   7691 C CA    . ARG B 1 435 ? 19.096 1.544   -38.909 1.00 23.44 ? 433  ARG A CA    1 
ATOM   7692 C C     . ARG B 1 435 ? 19.260 1.752   -40.420 1.00 23.09 ? 433  ARG A C     1 
ATOM   7693 O O     . ARG B 1 435 ? 18.701 0.979   -41.184 1.00 20.81 ? 433  ARG A O     1 
ATOM   7694 C CB    . ARG B 1 435 ? 18.128 2.548   -38.284 1.00 21.92 ? 433  ARG A CB    1 
ATOM   7695 C CG    . ARG B 1 435 ? 17.870 2.314   -36.804 1.00 21.64 ? 433  ARG A CG    1 
ATOM   7696 C CD    . ARG B 1 435 ? 16.734 3.169   -36.285 1.00 21.52 ? 433  ARG A CD    1 
ATOM   7697 N NE    . ARG B 1 435 ? 17.124 4.540   -36.002 1.00 21.10 ? 433  ARG A NE    1 
ATOM   7698 C CZ    . ARG B 1 435 ? 16.745 5.589   -36.715 1.00 21.99 ? 433  ARG A CZ    1 
ATOM   7699 N NH1   . ARG B 1 435 ? 15.976 5.428   -37.776 1.00 22.28 ? 433  ARG A NH1   1 
ATOM   7700 N NH2   . ARG B 1 435 ? 17.147 6.798   -36.374 1.00 23.65 ? 433  ARG A NH2   1 
ATOM   7701 N N     . ASP B 1 436 ? 19.987 2.797   -40.806 1.00 23.30 ? 434  ASP A N     1 
ATOM   7702 C CA    . ASP B 1 436 ? 20.263 3.080   -42.235 1.00 23.70 ? 434  ASP A CA    1 
ATOM   7703 C C     . ASP B 1 436 ? 21.019 1.894   -42.853 1.00 23.41 ? 434  ASP A C     1 
ATOM   7704 O O     . ASP B 1 436 ? 20.618 1.430   -43.911 1.00 22.59 ? 434  ASP A O     1 
ATOM   7705 C CB    . ASP B 1 436 ? 21.056 4.381   -42.346 1.00 23.01 ? 434  ASP A CB    1 
ATOM   7706 C CG    . ASP B 1 436 ? 20.236 5.642   -42.110 1.00 25.08 ? 434  ASP A CG    1 
ATOM   7707 O OD1   . ASP B 1 436 ? 19.045 5.518   -41.788 1.00 24.73 ? 434  ASP A OD1   1 
ATOM   7708 O OD2   . ASP B 1 436 ? 20.804 6.738   -42.249 1.00 24.97 ? 434  ASP A OD2   1 
ATOM   7709 N N     . CYS B 1 437 ? 22.068 1.433   -42.179 1.00 23.58 ? 435  CYS A N     1 
ATOM   7710 C CA    . CYS B 1 437 ? 22.918 0.342   -42.722 1.00 23.23 ? 435  CYS A CA    1 
ATOM   7711 C C     . CYS B 1 437 ? 22.095 -0.919  -43.002 1.00 22.56 ? 435  CYS A C     1 
ATOM   7712 O O     . CYS B 1 437 ? 22.312 -1.564  -44.081 1.00 23.81 ? 435  CYS A O     1 
ATOM   7713 C CB    . CYS B 1 437 ? 24.082 0.012   -41.810 1.00 24.09 ? 435  CYS A CB    1 
ATOM   7714 S SG    . CYS B 1 437 ? 25.271 -1.066  -42.642 1.00 23.49 ? 435  CYS A SG    1 
ATOM   7715 N N     . ARG B 1 438 ? 21.127 -1.248  -42.144 1.00 21.85 ? 436  ARG A N     1 
ATOM   7716 C CA    . ARG B 1 438 ? 20.249 -2.438  -42.349 1.00 20.76 ? 436  ARG A CA    1 
ATOM   7717 C C     . ARG B 1 438 ? 19.586 -2.405  -43.747 1.00 20.63 ? 436  ARG A C     1 
ATOM   7718 O O     . ARG B 1 438 ? 19.395 -3.483  -44.316 1.00 21.78 ? 436  ARG A O     1 
ATOM   7719 C CB    . ARG B 1 438 ? 19.183 -2.549  -41.245 1.00 21.47 ? 436  ARG A CB    1 
ATOM   7720 C CG    . ARG B 1 438 ? 19.699 -3.121  -39.938 1.00 22.23 ? 436  ARG A CG    1 
ATOM   7721 C CD    . ARG B 1 438 ? 20.197 -4.555  -40.112 1.00 23.22 ? 436  ARG A CD    1 
ATOM   7722 N NE    . ARG B 1 438 ? 19.144 -5.531  -40.337 1.00 23.63 ? 436  ARG A NE    1 
ATOM   7723 C CZ    . ARG B 1 438 ? 19.310 -6.737  -40.881 1.00 26.53 ? 436  ARG A CZ    1 
ATOM   7724 N NH1   . ARG B 1 438 ? 20.472 -7.110  -41.396 1.00 27.42 ? 436  ARG A NH1   1 
ATOM   7725 N NH2   . ARG B 1 438 ? 18.292 -7.570  -40.954 1.00 27.45 ? 436  ARG A NH2   1 
ATOM   7726 N N     . ILE B 1 439 ? 19.248 -1.247  -44.312 1.00 20.11 ? 437  ILE A N     1 
ATOM   7727 C CA    . ILE B 1 439 ? 18.589 -1.180  -45.661 1.00 20.51 ? 437  ILE A CA    1 
ATOM   7728 C C     . ILE B 1 439 ? 19.509 -1.767  -46.747 1.00 20.84 ? 437  ILE A C     1 
ATOM   7729 O O     . ILE B 1 439 ? 19.003 -2.478  -47.636 1.00 19.33 ? 437  ILE A O     1 
ATOM   7730 C CB    . ILE B 1 439 ? 18.123 0.251   -45.991 1.00 21.44 ? 437  ILE A CB    1 
ATOM   7731 C CG1   . ILE B 1 439 ? 16.788 0.224   -46.747 1.00 22.86 ? 437  ILE A CG1   1 
ATOM   7732 C CG2   . ILE B 1 439 ? 19.185 1.080   -46.704 1.00 20.39 ? 437  ILE A CG2   1 
ATOM   7733 C CD1   . ILE B 1 439 ? 16.899 -0.141  -48.188 1.00 21.36 ? 437  ILE A CD1   1 
ATOM   7734 N N     . THR B 1 440 ? 20.835 -1.585  -46.620 1.00 19.64 ? 438  THR A N     1 
ATOM   7735 C CA    . THR B 1 440 ? 21.812 -1.978  -47.656 1.00 19.97 ? 438  THR A CA    1 
ATOM   7736 C C     . THR B 1 440 ? 21.848 -3.496  -47.787 1.00 20.18 ? 438  THR A C     1 
ATOM   7737 O O     . THR B 1 440 ? 22.215 -3.954  -48.865 1.00 19.99 ? 438  THR A O     1 
ATOM   7738 C CB    . THR B 1 440 ? 23.184 -1.375  -47.376 1.00 19.44 ? 438  THR A CB    1 
ATOM   7739 O OG1   . THR B 1 440 ? 23.800 -1.971  -46.237 1.00 20.25 ? 438  THR A OG1   1 
ATOM   7740 C CG2   . THR B 1 440 ? 23.079 0.120   -47.183 1.00 21.32 ? 438  THR A CG2   1 
ATOM   7741 N N     . GLN B 1 441 ? 21.446 -4.235  -46.759 1.00 19.93 ? 439  GLN A N     1 
ATOM   7742 C CA    . GLN B 1 441 ? 21.474 -5.729  -46.808 1.00 19.73 ? 439  GLN A CA    1 
ATOM   7743 C C     . GLN B 1 441 ? 20.241 -6.287  -47.531 1.00 20.56 ? 439  GLN A C     1 
ATOM   7744 O O     . GLN B 1 441 ? 20.232 -7.514  -47.809 1.00 21.27 ? 439  GLN A O     1 
ATOM   7745 C CB    . GLN B 1 441 ? 21.658 -6.283  -45.402 1.00 19.41 ? 439  GLN A CB    1 
ATOM   7746 C CG    . GLN B 1 441 ? 23.021 -5.950  -44.813 1.00 21.27 ? 439  GLN A CG    1 
ATOM   7747 C CD    . GLN B 1 441 ? 23.040 -6.072  -43.309 1.00 22.58 ? 439  GLN A CD    1 
ATOM   7748 O OE1   . GLN B 1 441 ? 22.454 -5.249  -42.612 1.00 25.43 ? 439  GLN A OE1   1 
ATOM   7749 N NE2   . GLN B 1 441 ? 23.672 -7.120  -42.802 1.00 23.02 ? 439  GLN A NE2   1 
ATOM   7750 N N     . ILE B 1 442 ? 19.256 -5.451  -47.887 1.00 22.62 ? 440  ILE A N     1 
ATOM   7751 C CA    . ILE B 1 442 ? 18.061 -5.901  -48.677 1.00 24.18 ? 440  ILE A CA    1 
ATOM   7752 C C     . ILE B 1 442 ? 17.866 -5.015  -49.915 1.00 25.61 ? 440  ILE A C     1 
ATOM   7753 O O     . ILE B 1 442 ? 17.026 -5.360  -50.760 1.00 25.68 ? 440  ILE A O     1 
ATOM   7754 C CB    . ILE B 1 442 ? 16.788 -6.008  -47.796 1.00 26.07 ? 440  ILE A CB    1 
ATOM   7755 C CG1   . ILE B 1 442 ? 16.437 -4.722  -47.034 1.00 27.51 ? 440  ILE A CG1   1 
ATOM   7756 C CG2   . ILE B 1 442 ? 16.902 -7.185  -46.838 1.00 24.90 ? 440  ILE A CG2   1 
ATOM   7757 C CD1   . ILE B 1 442 ? 15.839 -3.632  -47.887 1.00 26.92 ? 440  ILE A CD1   1 
ATOM   7758 N N     . TYR B 1 443 ? 18.645 -3.950  -50.080 1.00 23.99 ? 441  TYR A N     1 
ATOM   7759 C CA    . TYR B 1 443 ? 18.521 -3.020  -51.232 1.00 25.23 ? 441  TYR A CA    1 
ATOM   7760 C C     . TYR B 1 443 ? 19.200 -3.663  -52.438 1.00 25.62 ? 441  TYR A C     1 
ATOM   7761 O O     . TYR B 1 443 ? 20.260 -4.264  -52.249 1.00 22.86 ? 441  TYR A O     1 
ATOM   7762 C CB    . TYR B 1 443 ? 19.132 -1.683  -50.849 1.00 25.19 ? 441  TYR A CB    1 
ATOM   7763 C CG    . TYR B 1 443 ? 18.830 -0.543  -51.778 1.00 28.00 ? 441  TYR A CG    1 
ATOM   7764 C CD1   . TYR B 1 443 ? 17.561 0.003   -51.828 1.00 25.92 ? 441  TYR A CD1   1 
ATOM   7765 C CD2   . TYR B 1 443 ? 19.828 0.048   -52.547 1.00 28.23 ? 441  TYR A CD2   1 
ATOM   7766 C CE1   . TYR B 1 443 ? 17.286 1.103   -52.618 1.00 26.78 ? 441  TYR A CE1   1 
ATOM   7767 C CE2   . TYR B 1 443 ? 19.555 1.123   -53.386 1.00 28.20 ? 441  TYR A CE2   1 
ATOM   7768 C CZ    . TYR B 1 443 ? 18.284 1.668   -53.395 1.00 28.15 ? 441  TYR A CZ    1 
ATOM   7769 O OH    . TYR B 1 443 ? 17.964 2.751   -54.151 1.00 29.80 ? 441  TYR A OH    1 
ATOM   7770 N N     . GLU B 1 444 ? 18.578 -3.597  -53.618 1.00 26.42 ? 442  GLU A N     1 
ATOM   7771 C CA    . GLU B 1 444 ? 19.023 -4.342  -54.827 1.00 28.29 ? 442  GLU A CA    1 
ATOM   7772 C C     . GLU B 1 444 ? 19.039 -5.832  -54.474 1.00 27.65 ? 442  GLU A C     1 
ATOM   7773 O O     . GLU B 1 444 ? 20.030 -6.524  -54.800 1.00 26.88 ? 442  GLU A O     1 
ATOM   7774 C CB    . GLU B 1 444 ? 20.422 -3.920  -55.277 1.00 36.15 ? 442  GLU A CB    1 
ATOM   7775 C CG    . GLU B 1 444 ? 20.531 -2.455  -55.647 1.00 44.89 ? 442  GLU A CG    1 
ATOM   7776 C CD    . GLU B 1 444 ? 19.862 -2.054  -56.948 1.00 54.63 ? 442  GLU A CD    1 
ATOM   7777 O OE1   . GLU B 1 444 ? 19.813 -2.927  -57.875 1.00 48.73 ? 442  GLU A OE1   1 
ATOM   7778 O OE2   . GLU B 1 444 ? 19.429 -0.857  -57.036 1.00 53.94 ? 442  GLU A OE2   1 
ATOM   7779 N N     . GLY B 1 445 ? 18.015 -6.260  -53.743 1.00 27.28 ? 443  GLY A N     1 
ATOM   7780 C CA    . GLY B 1 445 ? 17.766 -7.654  -53.354 1.00 28.12 ? 443  GLY A CA    1 
ATOM   7781 C C     . GLY B 1 445 ? 18.492 -8.025  -52.066 1.00 27.63 ? 443  GLY A C     1 
ATOM   7782 O O     . GLY B 1 445 ? 19.392 -7.273  -51.607 1.00 27.16 ? 443  GLY A O     1 
ATOM   7783 N N     . THR B 1 446 ? 18.169 -9.201  -51.548 1.00 24.22 ? 444  THR A N     1 
ATOM   7784 C CA    . THR B 1 446 ? 18.668 -9.677  -50.240 1.00 23.38 ? 444  THR A CA    1 
ATOM   7785 C C     . THR B 1 446 ? 20.109 -10.138 -50.444 1.00 21.44 ? 444  THR A C     1 
ATOM   7786 O O     . THR B 1 446 ? 20.476 -10.508 -51.563 1.00 21.74 ? 444  THR A O     1 
ATOM   7787 C CB    . THR B 1 446 ? 17.758 -10.769 -49.667 1.00 24.92 ? 444  THR A CB    1 
ATOM   7788 O OG1   . THR B 1 446 ? 17.988 -11.961 -50.405 1.00 22.05 ? 444  THR A OG1   1 
ATOM   7789 C CG2   . THR B 1 446 ? 16.295 -10.379 -49.697 1.00 25.80 ? 444  THR A CG2   1 
ATOM   7790 N N     . ASN B 1 447 ? 20.903 -10.115 -49.390 1.00 20.92 ? 445  ASN A N     1 
ATOM   7791 C CA    . ASN B 1 447 ? 22.298 -10.604 -49.445 1.00 20.06 ? 445  ASN A CA    1 
ATOM   7792 C C     . ASN B 1 447 ? 22.286 -12.110 -49.670 1.00 19.91 ? 445  ASN A C     1 
ATOM   7793 O O     . ASN B 1 447 ? 23.259 -12.625 -50.231 1.00 21.16 ? 445  ASN A O     1 
ATOM   7794 C CB    . ASN B 1 447 ? 23.048 -10.210 -48.178 1.00 20.88 ? 445  ASN A CB    1 
ATOM   7795 C CG    . ASN B 1 447 ? 23.459 -8.757  -48.211 1.00 21.07 ? 445  ASN A CG    1 
ATOM   7796 O OD1   . ASN B 1 447 ? 23.295 -8.060  -49.221 1.00 21.61 ? 445  ASN A OD1   1 
ATOM   7797 N ND2   . ASN B 1 447 ? 24.082 -8.330  -47.140 1.00 21.88 ? 445  ASN A ND2   1 
ATOM   7798 N N     . GLY B 1 448 ? 21.251 -12.805 -49.211 1.00 20.38 ? 446  GLY A N     1 
ATOM   7799 C CA    . GLY B 1 448 ? 21.182 -14.274 -49.370 1.00 22.19 ? 446  GLY A CA    1 
ATOM   7800 C C     . GLY B 1 448 ? 21.157 -14.646 -50.857 1.00 22.63 ? 446  GLY A C     1 
ATOM   7801 O O     . GLY B 1 448 ? 21.754 -15.684 -51.229 1.00 22.66 ? 446  GLY A O     1 
ATOM   7802 N N     . ILE B 1 449 ? 20.475 -13.822 -51.658 1.00 21.95 ? 447  ILE A N     1 
ATOM   7803 C CA    . ILE B 1 449 ? 20.337 -13.983 -53.138 1.00 23.59 ? 447  ILE A CA    1 
ATOM   7804 C C     . ILE B 1 449 ? 21.666 -13.643 -53.800 1.00 23.27 ? 447  ILE A C     1 
ATOM   7805 O O     . ILE B 1 449 ? 22.103 -14.428 -54.684 1.00 22.72 ? 447  ILE A O     1 
ATOM   7806 C CB    . ILE B 1 449 ? 19.170 -13.135 -53.671 1.00 24.44 ? 447  ILE A CB    1 
ATOM   7807 C CG1   . ILE B 1 449 ? 17.858 -13.640 -53.069 1.00 24.98 ? 447  ILE A CG1   1 
ATOM   7808 C CG2   . ILE B 1 449 ? 19.139 -13.097 -55.201 1.00 25.37 ? 447  ILE A CG2   1 
ATOM   7809 C CD1   . ILE B 1 449 ? 17.620 -15.114 -53.262 1.00 26.85 ? 447  ILE A CD1   1 
ATOM   7810 N N     . GLN B 1 450 ? 22.336 -12.576 -53.354 1.00 22.00 ? 448  GLN A N     1 
ATOM   7811 C CA    . GLN B 1 450 ? 23.702 -12.273 -53.832 1.00 21.80 ? 448  GLN A CA    1 
ATOM   7812 C C     . GLN B 1 450 ? 24.630 -13.480 -53.588 1.00 22.35 ? 448  GLN A C     1 
ATOM   7813 O O     . GLN B 1 450 ? 25.382 -13.846 -54.504 1.00 21.19 ? 448  GLN A O     1 
ATOM   7814 C CB    . GLN B 1 450 ? 24.218 -11.015 -53.159 1.00 22.92 ? 448  GLN A CB    1 
ATOM   7815 C CG    . GLN B 1 450 ? 23.473 -9.769  -53.553 1.00 24.93 ? 448  GLN A CG    1 
ATOM   7816 C CD    . GLN B 1 450 ? 23.527 -9.497  -55.040 1.00 27.96 ? 448  GLN A CD    1 
ATOM   7817 O OE1   . GLN B 1 450 ? 24.513 -9.781  -55.725 1.00 28.10 ? 448  GLN A OE1   1 
ATOM   7818 N NE2   . GLN B 1 450 ? 22.465 -8.906  -55.552 1.00 29.69 ? 448  GLN A NE2   1 
ATOM   7819 N N     . ALA B 1 451 ? 24.635 -14.072 -52.395 1.00 21.28 ? 449  ALA A N     1 
ATOM   7820 C CA    . ALA B 1 451 ? 25.543 -15.193 -52.040 1.00 22.05 ? 449  ALA A CA    1 
ATOM   7821 C C     . ALA B 1 451 ? 25.177 -16.423 -52.871 1.00 21.97 ? 449  ALA A C     1 
ATOM   7822 O O     . ALA B 1 451 ? 26.087 -17.163 -53.285 1.00 22.17 ? 449  ALA A O     1 
ATOM   7823 C CB    . ALA B 1 451 ? 25.471 -15.529 -50.569 1.00 21.65 ? 449  ALA A CB    1 
ATOM   7824 N N     . LEU B 1 452 ? 23.890 -16.630 -53.133 1.00 21.77 ? 450  LEU A N     1 
ATOM   7825 C CA    . LEU B 1 452 ? 23.454 -17.770 -53.974 1.00 22.71 ? 450  LEU A CA    1 
ATOM   7826 C C     . LEU B 1 452 ? 23.956 -17.559 -55.407 1.00 23.26 ? 450  LEU A C     1 
ATOM   7827 O O     . LEU B 1 452 ? 24.446 -18.515 -56.001 1.00 23.44 ? 450  LEU A O     1 
ATOM   7828 C CB    . LEU B 1 452 ? 21.937 -17.872 -53.923 1.00 22.33 ? 450  LEU A CB    1 
ATOM   7829 C CG    . LEU B 1 452 ? 21.293 -18.976 -54.748 1.00 23.64 ? 450  LEU A CG    1 
ATOM   7830 C CD1   . LEU B 1 452 ? 21.737 -20.353 -54.277 1.00 24.24 ? 450  LEU A CD1   1 
ATOM   7831 C CD2   . LEU B 1 452 ? 19.761 -18.853 -54.694 1.00 23.97 ? 450  LEU A CD2   1 
ATOM   7832 N N     . ASP B 1 453 ? 23.930 -16.329 -55.904 1.00 22.69 ? 451  ASP A N     1 
ATOM   7833 C CA    . ASP B 1 453 ? 24.497 -16.026 -57.243 1.00 25.29 ? 451  ASP A CA    1 
ATOM   7834 C C     . ASP B 1 453 ? 25.993 -16.366 -57.239 1.00 24.97 ? 451  ASP A C     1 
ATOM   7835 O O     . ASP B 1 453 ? 26.463 -17.016 -58.180 1.00 24.90 ? 451  ASP A O     1 
ATOM   7836 C CB    . ASP B 1 453 ? 24.269 -14.565 -57.633 1.00 26.76 ? 451  ASP A CB    1 
ATOM   7837 C CG    . ASP B 1 453 ? 24.926 -14.218 -58.960 1.00 29.95 ? 451  ASP A CG    1 
ATOM   7838 O OD1   . ASP B 1 453 ? 24.602 -14.886 -59.973 1.00 28.89 ? 451  ASP A OD1   1 
ATOM   7839 O OD2   . ASP B 1 453 ? 25.790 -13.323 -58.953 1.00 30.44 ? 451  ASP A OD2   1 
ATOM   7840 N N     . LEU B 1 454 ? 26.742 -15.932 -56.222 1.00 23.70 ? 452  LEU A N     1 
ATOM   7841 C CA    . LEU B 1 454 ? 28.194 -16.197 -56.173 1.00 22.92 ? 452  LEU A CA    1 
ATOM   7842 C C     . LEU B 1 454 ? 28.436 -17.708 -56.279 1.00 23.25 ? 452  LEU A C     1 
ATOM   7843 O O     . LEU B 1 454 ? 29.226 -18.114 -57.153 1.00 22.98 ? 452  LEU A O     1 
ATOM   7844 C CB    . LEU B 1 454 ? 28.810 -15.619 -54.895 1.00 24.44 ? 452  LEU A CB    1 
ATOM   7845 C CG    . LEU B 1 454 ? 30.230 -16.093 -54.608 1.00 25.51 ? 452  LEU A CG    1 
ATOM   7846 C CD1   . LEU B 1 454 ? 31.192 -15.511 -55.624 1.00 26.26 ? 452  LEU A CD1   1 
ATOM   7847 C CD2   . LEU B 1 454 ? 30.645 -15.719 -53.196 1.00 27.38 ? 452  LEU A CD2   1 
ATOM   7848 N N     . VAL B 1 455 ? 27.886 -18.516 -55.382 1.00 23.03 ? 453  VAL A N     1 
ATOM   7849 C CA    . VAL B 1 455 ? 28.266 -19.962 -55.325 1.00 25.22 ? 453  VAL A CA    1 
ATOM   7850 C C     . VAL B 1 455 ? 27.646 -20.703 -56.516 1.00 26.06 ? 453  VAL A C     1 
ATOM   7851 O O     . VAL B 1 455 ? 28.342 -21.572 -57.060 1.00 28.99 ? 453  VAL A O     1 
ATOM   7852 C CB    . VAL B 1 455 ? 27.929 -20.652 -53.985 1.00 26.55 ? 453  VAL A CB    1 
ATOM   7853 C CG1   . VAL B 1 455 ? 28.815 -20.129 -52.872 1.00 30.02 ? 453  VAL A CG1   1 
ATOM   7854 C CG2   . VAL B 1 455 ? 26.479 -20.516 -53.567 1.00 27.16 ? 453  VAL A CG2   1 
ATOM   7855 N N     . GLY B 1 456 ? 26.399 -20.380 -56.882 1.00 27.92 ? 454  GLY A N     1 
ATOM   7856 C CA    . GLY B 1 456 ? 25.600 -21.057 -57.930 1.00 26.99 ? 454  GLY A CA    1 
ATOM   7857 C C     . GLY B 1 456 ? 26.161 -20.792 -59.313 1.00 28.77 ? 454  GLY A C     1 
ATOM   7858 O O     . GLY B 1 456 ? 26.614 -21.752 -59.974 1.00 29.68 ? 454  GLY A O     1 
ATOM   7859 N N     . ARG B 1 457 ? 26.184 -19.524 -59.715 1.00 28.38 ? 455  ARG A N     1 
ATOM   7860 C CA    . ARG B 1 457 ? 26.514 -19.098 -61.094 1.00 30.28 ? 455  ARG A CA    1 
ATOM   7861 C C     . ARG B 1 457 ? 28.013 -18.791 -61.207 1.00 31.08 ? 455  ARG A C     1 
ATOM   7862 O O     . ARG B 1 457 ? 28.646 -19.298 -62.150 1.00 26.95 ? 455  ARG A O     1 
ATOM   7863 C CB    . ARG B 1 457 ? 25.648 -17.904 -61.488 1.00 34.29 ? 455  ARG A CB    1 
ATOM   7864 C CG    . ARG B 1 457 ? 24.155 -18.197 -61.398 1.00 48.83 ? 455  ARG A CG    1 
ATOM   7865 C CD    . ARG B 1 457 ? 23.366 -17.888 -62.662 1.00 56.63 ? 455  ARG A CD    1 
ATOM   7866 N NE    . ARG B 1 457 ? 23.553 -16.506 -63.082 1.00 65.30 ? 455  ARG A NE    1 
ATOM   7867 C CZ    . ARG B 1 457 ? 24.363 -16.100 -64.056 1.00 75.36 ? 455  ARG A CZ    1 
ATOM   7868 N NH1   . ARG B 1 457 ? 25.067 -16.975 -64.757 1.00 81.06 ? 455  ARG A NH1   1 
ATOM   7869 N NH2   . ARG B 1 457 ? 24.458 -14.810 -64.337 1.00 80.19 ? 455  ARG A NH2   1 
ATOM   7870 N N     . LYS B 1 458 ? 28.593 -18.048 -60.261 1.00 25.86 ? 456  LYS A N     1 
ATOM   7871 C CA    . LYS B 1 458 ? 29.988 -17.557 -60.429 1.00 25.50 ? 456  LYS A CA    1 
ATOM   7872 C C     . LYS B 1 458 ? 31.015 -18.634 -60.048 1.00 25.04 ? 456  LYS A C     1 
ATOM   7873 O O     . LYS B 1 458 ? 32.101 -18.655 -60.656 1.00 25.24 ? 456  LYS A O     1 
ATOM   7874 C CB    . LYS B 1 458 ? 30.163 -16.247 -59.665 1.00 25.61 ? 456  LYS A CB    1 
ATOM   7875 C CG    . LYS B 1 458 ? 29.095 -15.204 -59.971 1.00 25.02 ? 456  LYS A CG    1 
ATOM   7876 C CD    . LYS B 1 458 ? 28.904 -14.973 -61.457 1.00 26.50 ? 456  LYS A CD    1 
ATOM   7877 C CE    . LYS B 1 458 ? 27.610 -14.271 -61.812 1.00 26.69 ? 456  LYS A CE    1 
ATOM   7878 N NZ    . LYS B 1 458 ? 27.529 -12.946 -61.153 1.00 27.62 ? 456  LYS A NZ    1 
ATOM   7879 N N     . VAL B 1 459 ? 30.692 -19.545 -59.145 1.00 22.51 ? 457  VAL A N     1 
ATOM   7880 C CA    . VAL B 1 459 ? 31.676 -20.572 -58.731 1.00 24.05 ? 457  VAL A CA    1 
ATOM   7881 C C     . VAL B 1 459 ? 31.299 -21.872 -59.441 1.00 26.25 ? 457  VAL A C     1 
ATOM   7882 O O     . VAL B 1 459 ? 32.002 -22.205 -60.425 1.00 28.07 ? 457  VAL A O     1 
ATOM   7883 C CB    . VAL B 1 459 ? 31.813 -20.670 -57.201 1.00 25.28 ? 457  VAL A CB    1 
ATOM   7884 C CG1   . VAL B 1 459 ? 32.779 -21.776 -56.804 1.00 27.06 ? 457  VAL A CG1   1 
ATOM   7885 C CG2   . VAL B 1 459 ? 32.263 -19.338 -56.600 1.00 24.59 ? 457  VAL A CG2   1 
ATOM   7886 N N     . ILE B 1 460 ? 30.213 -22.538 -59.051 1.00 28.57 ? 458  ILE A N     1 
ATOM   7887 C CA    . ILE B 1 460 ? 29.782 -23.830 -59.675 1.00 29.39 ? 458  ILE A CA    1 
ATOM   7888 C C     . ILE B 1 460 ? 29.647 -23.604 -61.193 1.00 28.08 ? 458  ILE A C     1 
ATOM   7889 O O     . ILE B 1 460 ? 30.173 -24.425 -61.970 1.00 28.54 ? 458  ILE A O     1 
ATOM   7890 C CB    . ILE B 1 460 ? 28.481 -24.390 -59.056 1.00 33.20 ? 458  ILE A CB    1 
ATOM   7891 C CG1   . ILE B 1 460 ? 28.578 -24.648 -57.548 1.00 38.06 ? 458  ILE A CG1   1 
ATOM   7892 C CG2   . ILE B 1 460 ? 27.990 -25.632 -59.791 1.00 32.71 ? 458  ILE A CG2   1 
ATOM   7893 C CD1   . ILE B 1 460 ? 29.847 -25.297 -57.114 1.00 42.54 ? 458  ILE A CD1   1 
ATOM   7894 N N     . GLY B 1 461 ? 29.024 -22.506 -61.605 1.00 27.14 ? 459  GLY A N     1 
ATOM   7895 C CA    . GLY B 1 461 ? 28.665 -22.246 -63.006 1.00 26.03 ? 459  GLY A CA    1 
ATOM   7896 C C     . GLY B 1 461 ? 29.891 -22.096 -63.890 1.00 28.34 ? 459  GLY A C     1 
ATOM   7897 O O     . GLY B 1 461 ? 29.775 -22.415 -65.065 1.00 32.40 ? 459  GLY A O     1 
ATOM   7898 N N     . SER B 1 462 ? 31.036 -21.643 -63.368 1.00 26.61 ? 460  SER A N     1 
ATOM   7899 C CA    . SER B 1 462 ? 32.296 -21.503 -64.155 1.00 25.38 ? 460  SER A CA    1 
ATOM   7900 C C     . SER B 1 462 ? 33.273 -22.640 -63.840 1.00 26.36 ? 460  SER A C     1 
ATOM   7901 O O     . SER B 1 462 ? 34.453 -22.530 -64.258 1.00 25.07 ? 460  SER A O     1 
ATOM   7902 C CB    . SER B 1 462 ? 32.952 -20.177 -63.926 1.00 25.01 ? 460  SER A CB    1 
ATOM   7903 O OG    . SER B 1 462 ? 33.503 -20.092 -62.610 1.00 26.81 ? 460  SER A OG    1 
ATOM   7904 N N     . GLY B 1 463 ? 32.846 -23.661 -63.095 1.00 25.85 ? 461  GLY A N     1 
ATOM   7905 C CA    . GLY B 1 463 ? 33.747 -24.742 -62.641 1.00 24.75 ? 461  GLY A CA    1 
ATOM   7906 C C     . GLY B 1 463 ? 34.862 -24.192 -61.777 1.00 28.34 ? 461  GLY A C     1 
ATOM   7907 O O     . GLY B 1 463 ? 35.924 -24.850 -61.684 1.00 28.61 ? 461  GLY A O     1 
ATOM   7908 N N     . GLY B 1 464 ? 34.667 -23.004 -61.187 1.00 23.35 ? 462  GLY A N     1 
ATOM   7909 C CA    . GLY B 1 464 ? 35.693 -22.362 -60.361 1.00 24.28 ? 462  GLY A CA    1 
ATOM   7910 C C     . GLY B 1 464 ? 36.657 -21.517 -61.156 1.00 24.32 ? 462  GLY A C     1 
ATOM   7911 O O     . GLY B 1 464 ? 37.513 -20.903 -60.536 1.00 26.29 ? 462  GLY A O     1 
ATOM   7912 N N     . ALA B 1 465 ? 36.553 -21.475 -62.479 1.00 23.60 ? 463  ALA A N     1 
ATOM   7913 C CA    . ALA B 1 465 ? 37.526 -20.765 -63.343 1.00 24.16 ? 463  ALA A CA    1 
ATOM   7914 C C     . ALA B 1 465 ? 37.556 -19.266 -63.005 1.00 24.95 ? 463  ALA A C     1 
ATOM   7915 O O     . ALA B 1 465 ? 38.655 -18.683 -63.019 1.00 26.60 ? 463  ALA A O     1 
ATOM   7916 C CB    . ALA B 1 465 ? 37.169 -20.980 -64.794 1.00 25.14 ? 463  ALA A CB    1 
ATOM   7917 N N     . PHE B 1 466 ? 36.405 -18.649 -62.739 1.00 23.34 ? 464  PHE A N     1 
ATOM   7918 C CA    . PHE B 1 466 ? 36.326 -17.186 -62.464 1.00 24.41 ? 464  PHE A CA    1 
ATOM   7919 C C     . PHE B 1 466 ? 37.125 -16.886 -61.193 1.00 24.28 ? 464  PHE A C     1 
ATOM   7920 O O     . PHE B 1 466 ? 37.927 -15.937 -61.181 1.00 26.70 ? 464  PHE A O     1 
ATOM   7921 C CB    . PHE B 1 466 ? 34.882 -16.694 -62.319 1.00 26.13 ? 464  PHE A CB    1 
ATOM   7922 C CG    . PHE B 1 466 ? 34.042 -16.689 -63.573 1.00 27.79 ? 464  PHE A CG    1 
ATOM   7923 C CD1   . PHE B 1 466 ? 34.574 -16.996 -64.817 1.00 27.73 ? 464  PHE A CD1   1 
ATOM   7924 C CD2   . PHE B 1 466 ? 32.708 -16.331 -63.509 1.00 31.18 ? 464  PHE A CD2   1 
ATOM   7925 C CE1   . PHE B 1 466 ? 33.780 -16.989 -65.953 1.00 31.25 ? 464  PHE A CE1   1 
ATOM   7926 C CE2   . PHE B 1 466 ? 31.921 -16.308 -64.653 1.00 32.98 ? 464  PHE A CE2   1 
ATOM   7927 C CZ    . PHE B 1 466 ? 32.462 -16.621 -65.872 1.00 31.27 ? 464  PHE A CZ    1 
ATOM   7928 N N     . SER B 1 467 ? 36.978 -17.726 -60.170 1.00 26.15 ? 465  SER A N     1 
ATOM   7929 C CA    . SER B 1 467 ? 37.704 -17.606 -58.876 1.00 25.81 ? 465  SER A CA    1 
ATOM   7930 C C     . SER B 1 467 ? 39.210 -17.755 -59.099 1.00 26.96 ? 465  SER A C     1 
ATOM   7931 O O     . SER B 1 467 ? 39.976 -16.962 -58.510 1.00 24.51 ? 465  SER A O     1 
ATOM   7932 C CB    . SER B 1 467 ? 37.208 -18.630 -57.886 1.00 28.54 ? 465  SER A CB    1 
ATOM   7933 O OG    . SER B 1 467 ? 35.873 -18.348 -57.548 1.00 30.88 ? 465  SER A OG    1 
ATOM   7934 N N     . ARG B 1 468 ? 39.620 -18.727 -59.916 1.00 26.10 ? 466  ARG A N     1 
ATOM   7935 C CA    . ARG B 1 468 ? 41.060 -18.958 -60.232 1.00 27.74 ? 466  ARG A CA    1 
ATOM   7936 C C     . ARG B 1 468 ? 41.666 -17.716 -60.909 1.00 29.17 ? 466  ARG A C     1 
ATOM   7937 O O     . ARG B 1 468 ? 42.864 -17.456 -60.693 1.00 28.66 ? 466  ARG A O     1 
ATOM   7938 C CB    . ARG B 1 468 ? 41.216 -20.239 -61.057 1.00 27.22 ? 466  ARG A CB    1 
ATOM   7939 C CG    . ARG B 1 468 ? 40.912 -21.490 -60.248 1.00 27.70 ? 466  ARG A CG    1 
ATOM   7940 C CD    . ARG B 1 468 ? 41.487 -22.740 -60.876 1.00 30.24 ? 466  ARG A CD    1 
ATOM   7941 N NE    . ARG B 1 468 ? 41.269 -22.750 -62.321 1.00 30.12 ? 466  ARG A NE    1 
ATOM   7942 C CZ    . ARG B 1 468 ? 40.256 -23.336 -62.951 1.00 32.71 ? 466  ARG A CZ    1 
ATOM   7943 N NH1   . ARG B 1 468 ? 40.195 -23.259 -64.269 1.00 35.55 ? 466  ARG A NH1   1 
ATOM   7944 N NH2   . ARG B 1 468 ? 39.309 -23.983 -62.285 1.00 31.52 ? 466  ARG A NH2   1 
ATOM   7945 N N     . HIS B 1 469 ? 40.904 -16.932 -61.673 1.00 29.88 ? 467  HIS A N     1 
ATOM   7946 C CA    . HIS B 1 469 ? 41.461 -15.686 -62.264 1.00 32.59 ? 467  HIS A CA    1 
ATOM   7947 C C     . HIS B 1 469 ? 41.863 -14.755 -61.124 1.00 33.20 ? 467  HIS A C     1 
ATOM   7948 O O     . HIS B 1 469 ? 42.939 -14.138 -61.195 1.00 34.31 ? 467  HIS A O     1 
ATOM   7949 C CB    . HIS B 1 469 ? 40.533 -15.013 -63.284 1.00 38.34 ? 467  HIS A CB    1 
ATOM   7950 C CG    . HIS B 1 469 ? 40.143 -15.914 -64.402 1.00 43.53 ? 467  HIS A CG    1 
ATOM   7951 N ND1   . HIS B 1 469 ? 40.858 -17.066 -64.703 1.00 49.09 ? 467  HIS A ND1   1 
ATOM   7952 C CD2   . HIS B 1 469 ? 39.098 -15.872 -65.257 1.00 47.83 ? 467  HIS A CD2   1 
ATOM   7953 C CE1   . HIS B 1 469 ? 40.262 -17.707 -65.686 1.00 45.61 ? 467  HIS A CE1   1 
ATOM   7954 N NE2   . HIS B 1 469 ? 39.183 -16.988 -66.055 1.00 50.30 ? 467  HIS A NE2   1 
ATOM   7955 N N     . PHE B 1 470 ? 41.057 -14.702 -60.065 1.00 30.60 ? 468  PHE A N     1 
ATOM   7956 C CA    . PHE B 1 470 ? 41.301 -13.826 -58.903 1.00 28.26 ? 468  PHE A CA    1 
ATOM   7957 C C     . PHE B 1 470 ? 42.463 -14.361 -58.073 1.00 28.38 ? 468  PHE A C     1 
ATOM   7958 O O     . PHE B 1 470 ? 43.382 -13.591 -57.761 1.00 30.59 ? 468  PHE A O     1 
ATOM   7959 C CB    . PHE B 1 470 ? 40.045 -13.765 -58.041 1.00 29.59 ? 468  PHE A CB    1 
ATOM   7960 C CG    . PHE B 1 470 ? 40.111 -12.775 -56.917 1.00 27.80 ? 468  PHE A CG    1 
ATOM   7961 C CD1   . PHE B 1 470 ? 40.500 -11.467 -57.149 1.00 26.35 ? 468  PHE A CD1   1 
ATOM   7962 C CD2   . PHE B 1 470 ? 39.747 -13.148 -55.630 1.00 27.32 ? 468  PHE A CD2   1 
ATOM   7963 C CE1   . PHE B 1 470 ? 40.555 -10.551 -56.109 1.00 26.46 ? 468  PHE A CE1   1 
ATOM   7964 C CE2   . PHE B 1 470 ? 39.765 -12.224 -54.599 1.00 27.52 ? 468  PHE A CE2   1 
ATOM   7965 C CZ    . PHE B 1 470 ? 40.181 -10.927 -54.841 1.00 28.22 ? 468  PHE A CZ    1 
ATOM   7966 N N     . THR B 1 471 ? 42.415 -15.633 -57.690 1.00 27.00 ? 469  THR A N     1 
ATOM   7967 C CA    . THR B 1 471 ? 43.430 -16.237 -56.799 1.00 27.42 ? 469  THR A CA    1 
ATOM   7968 C C     . THR B 1 471 ? 44.764 -16.415 -57.540 1.00 29.43 ? 469  THR A C     1 
ATOM   7969 O O     . THR B 1 471 ? 45.788 -16.359 -56.863 1.00 31.93 ? 469  THR A O     1 
ATOM   7970 C CB    . THR B 1 471 ? 42.955 -17.543 -56.166 1.00 28.67 ? 469  THR A CB    1 
ATOM   7971 O OG1   . THR B 1 471 ? 42.708 -18.490 -57.200 1.00 29.11 ? 469  THR A OG1   1 
ATOM   7972 C CG2   . THR B 1 471 ? 41.744 -17.335 -55.279 1.00 28.75 ? 469  THR A CG2   1 
ATOM   7973 N N     . ASP B 1 472 ? 44.775 -16.550 -58.866 1.00 27.48 ? 470  ASP A N     1 
ATOM   7974 C CA    . ASP B 1 472 ? 46.034 -16.539 -59.647 1.00 29.91 ? 470  ASP A CA    1 
ATOM   7975 C C     . ASP B 1 472 ? 46.716 -15.175 -59.471 1.00 30.08 ? 470  ASP A C     1 
ATOM   7976 O O     . ASP B 1 472 ? 47.964 -15.129 -59.302 1.00 30.59 ? 470  ASP A O     1 
ATOM   7977 C CB    . ASP B 1 472 ? 45.782 -16.863 -61.122 1.00 32.25 ? 470  ASP A CB    1 
ATOM   7978 C CG    . ASP B 1 472 ? 45.557 -18.345 -61.407 1.00 32.72 ? 470  ASP A CG    1 
ATOM   7979 O OD1   . ASP B 1 472 ? 45.863 -19.174 -60.533 1.00 34.51 ? 470  ASP A OD1   1 
ATOM   7980 O OD2   . ASP B 1 472 ? 45.059 -18.647 -62.509 1.00 39.76 ? 470  ASP A OD2   1 
ATOM   7981 N N     . GLU B 1 473 ? 45.955 -14.086 -59.547 1.00 28.15 ? 471  GLU A N     1 
ATOM   7982 C CA    . GLU B 1 473 ? 46.527 -12.728 -59.391 1.00 26.24 ? 471  GLU A CA    1 
ATOM   7983 C C     . GLU B 1 473 ? 47.099 -12.603 -57.976 1.00 25.74 ? 471  GLU A C     1 
ATOM   7984 O O     . GLU B 1 473 ? 48.214 -12.052 -57.827 1.00 24.91 ? 471  GLU A O     1 
ATOM   7985 C CB    . GLU B 1 473 ? 45.484 -11.668 -59.680 1.00 26.46 ? 471  GLU A CB    1 
ATOM   7986 C CG    . GLU B 1 473 ? 45.973 -10.263 -59.461 1.00 27.48 ? 471  GLU A CG    1 
ATOM   7987 C CD    . GLU B 1 473 ? 44.873 -9.237  -59.651 1.00 31.00 ? 471  GLU A CD    1 
ATOM   7988 O OE1   . GLU B 1 473 ? 44.550 -8.491  -58.697 1.00 27.85 ? 471  GLU A OE1   1 
ATOM   7989 O OE2   . GLU B 1 473 ? 44.335 -9.188  -60.769 1.00 29.73 ? 471  GLU A OE2   1 
ATOM   7990 N N     . ILE B 1 474 ? 46.391 -13.131 -56.980 1.00 25.36 ? 472  ILE A N     1 
ATOM   7991 C CA    . ILE B 1 474 ? 46.853 -13.068 -55.565 1.00 25.36 ? 472  ILE A CA    1 
ATOM   7992 C C     . ILE B 1 474 ? 48.152 -13.858 -55.427 1.00 25.52 ? 472  ILE A C     1 
ATOM   7993 O O     . ILE B 1 474 ? 49.070 -13.360 -54.781 1.00 24.28 ? 472  ILE A O     1 
ATOM   7994 C CB    . ILE B 1 474 ? 45.788 -13.568 -54.571 1.00 24.81 ? 472  ILE A CB    1 
ATOM   7995 C CG1   . ILE B 1 474 ? 44.525 -12.704 -54.572 1.00 25.15 ? 472  ILE A CG1   1 
ATOM   7996 C CG2   . ILE B 1 474 ? 46.400 -13.644 -53.196 1.00 27.33 ? 472  ILE A CG2   1 
ATOM   7997 C CD1   . ILE B 1 474 ? 43.376 -13.314 -53.772 1.00 25.27 ? 472  ILE A CD1   1 
ATOM   7998 N N     . LYS B 1 475 ? 48.208 -15.064 -55.985 1.00 26.55 ? 473  LYS A N     1 
ATOM   7999 C CA    . LYS B 1 475 ? 49.404 -15.939 -55.892 1.00 28.37 ? 473  LYS A CA    1 
ATOM   8000 C C     . LYS B 1 475 ? 50.599 -15.277 -56.593 1.00 26.14 ? 473  LYS A C     1 
ATOM   8001 O O     . LYS B 1 475 ? 51.718 -15.476 -56.129 1.00 24.92 ? 473  LYS A O     1 
ATOM   8002 C CB    . LYS B 1 475 ? 49.103 -17.301 -56.515 1.00 30.95 ? 473  LYS A CB    1 
ATOM   8003 C CG    . LYS B 1 475 ? 48.209 -18.211 -55.694 1.00 34.27 ? 473  LYS A CG    1 
ATOM   8004 C CD    . LYS B 1 475 ? 47.684 -19.341 -56.567 1.00 35.85 ? 473  LYS A CD    1 
ATOM   8005 C CE    . LYS B 1 475 ? 46.983 -20.390 -55.748 1.00 37.52 ? 473  LYS A CE    1 
ATOM   8006 N NZ    . LYS B 1 475 ? 46.562 -21.511 -56.609 1.00 39.72 ? 473  LYS A NZ    1 
ATOM   8007 N N     . ALA B 1 476 ? 50.389 -14.571 -57.705 1.00 27.87 ? 474  ALA A N     1 
ATOM   8008 C CA    . ALA B 1 476 ? 51.506 -13.906 -58.421 1.00 29.62 ? 474  ALA A CA    1 
ATOM   8009 C C     . ALA B 1 476 ? 52.022 -12.787 -57.507 1.00 28.10 ? 474  ALA A C     1 
ATOM   8010 O O     . ALA B 1 476 ? 53.248 -12.644 -57.334 1.00 27.12 ? 474  ALA A O     1 
ATOM   8011 C CB    . ALA B 1 476 ? 51.075 -13.391 -59.769 1.00 27.72 ? 474  ALA A CB    1 
ATOM   8012 N N     . PHE B 1 477 ? 51.104 -12.063 -56.880 1.00 27.16 ? 475  PHE A N     1 
ATOM   8013 C CA    . PHE B 1 477 ? 51.439 -11.046 -55.849 1.00 27.91 ? 475  PHE A CA    1 
ATOM   8014 C C     . PHE B 1 477 ? 52.320 -11.680 -54.764 1.00 27.54 ? 475  PHE A C     1 
ATOM   8015 O O     . PHE B 1 477 ? 53.404 -11.152 -54.483 1.00 25.83 ? 475  PHE A O     1 
ATOM   8016 C CB    . PHE B 1 477 ? 50.168 -10.407 -55.276 1.00 28.23 ? 475  PHE A CB    1 
ATOM   8017 C CG    . PHE B 1 477 ? 50.407 -9.552  -54.057 1.00 26.50 ? 475  PHE A CG    1 
ATOM   8018 C CD1   . PHE B 1 477 ? 50.904 -8.269  -54.185 1.00 25.29 ? 475  PHE A CD1   1 
ATOM   8019 C CD2   . PHE B 1 477 ? 50.125 -10.034 -52.786 1.00 27.07 ? 475  PHE A CD2   1 
ATOM   8020 C CE1   . PHE B 1 477 ? 51.133 -7.483  -53.069 1.00 25.33 ? 475  PHE A CE1   1 
ATOM   8021 C CE2   . PHE B 1 477 ? 50.378 -9.258  -51.673 1.00 28.18 ? 475  PHE A CE2   1 
ATOM   8022 C CZ    . PHE B 1 477 ? 50.869 -7.976  -51.819 1.00 26.26 ? 475  PHE A CZ    1 
ATOM   8023 N N     . VAL B 1 478 ? 51.868 -12.773 -54.153 1.00 26.98 ? 476  VAL A N     1 
ATOM   8024 C CA    . VAL B 1 478 ? 52.633 -13.488 -53.089 1.00 27.45 ? 476  VAL A CA    1 
ATOM   8025 C C     . VAL B 1 478 ? 54.040 -13.833 -53.606 1.00 28.88 ? 476  VAL A C     1 
ATOM   8026 O O     . VAL B 1 478 ? 55.019 -13.531 -52.902 1.00 26.14 ? 476  VAL A O     1 
ATOM   8027 C CB    . VAL B 1 478 ? 51.881 -14.748 -52.622 1.00 27.79 ? 476  VAL A CB    1 
ATOM   8028 C CG1   . VAL B 1 478 ? 52.762 -15.639 -51.749 1.00 25.99 ? 476  VAL A CG1   1 
ATOM   8029 C CG2   . VAL B 1 478 ? 50.586 -14.388 -51.898 1.00 28.79 ? 476  VAL A CG2   1 
ATOM   8030 N N     . ALA B 1 479 ? 54.144 -14.421 -54.801 1.00 29.78 ? 477  ALA A N     1 
ATOM   8031 C CA    . ALA B 1 479 ? 55.431 -14.861 -55.392 1.00 30.26 ? 477  ALA A CA    1 
ATOM   8032 C C     . ALA B 1 479 ? 56.368 -13.654 -55.542 1.00 28.63 ? 477  ALA A C     1 
ATOM   8033 O O     . ALA B 1 479 ? 57.568 -13.840 -55.414 1.00 30.61 ? 477  ALA A O     1 
ATOM   8034 C CB    . ALA B 1 479 ? 55.222 -15.581 -56.705 1.00 28.80 ? 477  ALA A CB    1 
ATOM   8035 N N     . SER B 1 480 ? 55.833 -12.451 -55.725 1.00 27.43 ? 478  SER A N     1 
ATOM   8036 C CA    . SER B 1 480 ? 56.607 -11.204 -55.907 1.00 26.82 ? 478  SER A CA    1 
ATOM   8037 C C     . SER B 1 480 ? 57.114 -10.649 -54.567 1.00 30.19 ? 478  SER A C     1 
ATOM   8038 O O     . SER B 1 480 ? 58.040 -9.808  -54.596 1.00 28.90 ? 478  SER A O     1 
ATOM   8039 C CB    . SER B 1 480 ? 55.783 -10.190 -56.623 1.00 28.17 ? 478  SER A CB    1 
ATOM   8040 O OG    . SER B 1 480 ? 54.893 -9.522  -55.744 1.00 26.85 ? 478  SER A OG    1 
ATOM   8041 N N     . ALA B 1 481 ? 56.549 -11.078 -53.431 1.00 30.39 ? 479  ALA A N     1 
ATOM   8042 C CA    . ALA B 1 481 ? 56.732 -10.399 -52.126 1.00 30.29 ? 479  ALA A CA    1 
ATOM   8043 C C     . ALA B 1 481 ? 58.203 -10.425 -51.683 1.00 30.21 ? 479  ALA A C     1 
ATOM   8044 O O     . ALA B 1 481 ? 58.825 -11.503 -51.750 1.00 30.87 ? 479  ALA A O     1 
ATOM   8045 C CB    . ALA B 1 481 ? 55.849 -11.047 -51.088 1.00 29.05 ? 479  ALA A CB    1 
ATOM   8046 N N     . ASP B 1 482 ? 58.724 -9.296  -51.186 1.00 31.47 ? 480  ASP A N     1 
ATOM   8047 C CA    . ASP B 1 482 ? 60.035 -9.265  -50.466 1.00 32.30 ? 480  ASP A CA    1 
ATOM   8048 C C     . ASP B 1 482 ? 59.863 -9.825  -49.037 1.00 34.13 ? 480  ASP A C     1 
ATOM   8049 O O     . ASP B 1 482 ? 58.712 -10.096 -48.611 1.00 28.21 ? 480  ASP A O     1 
ATOM   8050 C CB    . ASP B 1 482 ? 60.651 -7.865  -50.479 1.00 32.21 ? 480  ASP A CB    1 
ATOM   8051 C CG    . ASP B 1 482 ? 59.983 -6.849  -49.570 1.00 35.33 ? 480  ASP A CG    1 
ATOM   8052 O OD1   . ASP B 1 482 ? 58.979 -7.181  -48.930 1.00 35.51 ? 480  ASP A OD1   1 
ATOM   8053 O OD2   . ASP B 1 482 ? 60.480 -5.732  -49.517 1.00 40.78 ? 480  ASP A OD2   1 
ATOM   8054 N N     . GLU B 1 483 ? 60.962 -9.931  -48.287 1.00 34.24 ? 481  GLU A N     1 
ATOM   8055 C CA    . GLU B 1 483 ? 60.966 -10.550 -46.936 1.00 37.30 ? 481  GLU A CA    1 
ATOM   8056 C C     . GLU B 1 483 ? 60.026 -9.750  -46.025 1.00 32.67 ? 481  GLU A C     1 
ATOM   8057 O O     . GLU B 1 483 ? 59.295 -10.388 -45.279 1.00 33.90 ? 481  GLU A O     1 
ATOM   8058 C CB    . GLU B 1 483 ? 62.380 -10.690 -46.358 1.00 43.00 ? 481  GLU A CB    1 
ATOM   8059 C CG    . GLU B 1 483 ? 62.432 -11.580 -45.109 1.00 54.48 ? 481  GLU A CG    1 
ATOM   8060 C CD    . GLU B 1 483 ? 62.070 -10.930 -43.763 1.00 60.05 ? 481  GLU A CD    1 
ATOM   8061 O OE1   . GLU B 1 483 ? 61.980 -9.671  -43.705 1.00 68.25 ? 481  GLU A OE1   1 
ATOM   8062 O OE2   . GLU B 1 483 ? 61.894 -11.669 -42.754 1.00 50.73 ? 481  GLU A OE2   1 
ATOM   8063 N N     . ALA B 1 484 ? 60.003 -8.415  -46.095 1.00 26.72 ? 482  ALA A N     1 
ATOM   8064 C CA    . ALA B 1 484 ? 59.198 -7.597  -45.155 1.00 28.05 ? 482  ALA A CA    1 
ATOM   8065 C C     . ALA B 1 484 ? 57.711 -7.867  -45.409 1.00 27.82 ? 482  ALA A C     1 
ATOM   8066 O O     . ALA B 1 484 ? 56.945 -8.057  -44.449 1.00 25.78 ? 482  ALA A O     1 
ATOM   8067 C CB    . ALA B 1 484 ? 59.542 -6.136  -45.309 1.00 28.00 ? 482  ALA A CB    1 
ATOM   8068 N N     . LEU B 1 485 ? 57.312 -7.903  -46.677 1.00 28.06 ? 483  LEU A N     1 
ATOM   8069 C CA    . LEU B 1 485 ? 55.901 -8.113  -47.064 1.00 28.64 ? 483  LEU A CA    1 
ATOM   8070 C C     . LEU B 1 485 ? 55.469 -9.542  -46.717 1.00 28.56 ? 483  LEU A C     1 
ATOM   8071 O O     . LEU B 1 485 ? 54.226 -9.771  -46.546 1.00 27.16 ? 483  LEU A O     1 
ATOM   8072 C CB    . LEU B 1 485 ? 55.775 -7.793  -48.551 1.00 28.56 ? 483  LEU A CB    1 
ATOM   8073 C CG    . LEU B 1 485 ? 54.371 -7.870  -49.123 1.00 30.35 ? 483  LEU A CG    1 
ATOM   8074 C CD1   . LEU B 1 485 ? 53.441 -6.927  -48.365 1.00 30.96 ? 483  LEU A CD1   1 
ATOM   8075 C CD2   . LEU B 1 485 ? 54.392 -7.539  -50.605 1.00 31.17 ? 483  LEU A CD2   1 
ATOM   8076 N N     . GLY B 1 486 ? 56.430 -10.446 -46.556 1.00 26.96 ? 484  GLY A N     1 
ATOM   8077 C CA    . GLY B 1 486 ? 56.130 -11.832 -46.143 1.00 29.57 ? 484  GLY A CA    1 
ATOM   8078 C C     . GLY B 1 486 ? 55.314 -11.918 -44.860 1.00 28.61 ? 484  GLY A C     1 
ATOM   8079 O O     . GLY B 1 486 ? 54.583 -12.893 -44.703 1.00 29.02 ? 484  GLY A O     1 
ATOM   8080 N N     . GLU B 1 487 ? 55.466 -10.948 -43.964 1.00 26.09 ? 485  GLU A N     1 
ATOM   8081 C CA    . GLU B 1 487 ? 54.627 -10.885 -42.742 1.00 26.25 ? 485  GLU A CA    1 
ATOM   8082 C C     . GLU B 1 487 ? 53.157 -11.008 -43.143 1.00 25.72 ? 485  GLU A C     1 
ATOM   8083 O O     . GLU B 1 487 ? 52.402 -11.648 -42.413 1.00 26.56 ? 485  GLU A O     1 
ATOM   8084 C CB    . GLU B 1 487 ? 54.854 -9.545  -42.047 1.00 27.64 ? 485  GLU A CB    1 
ATOM   8085 C CG    . GLU B 1 487 ? 54.022 -9.363  -40.792 1.00 29.50 ? 485  GLU A CG    1 
ATOM   8086 C CD    . GLU B 1 487 ? 54.157 -8.006  -40.122 1.00 31.25 ? 485  GLU A CD    1 
ATOM   8087 O OE1   . GLU B 1 487 ? 55.051 -7.242  -40.514 1.00 28.00 ? 485  GLU A OE1   1 
ATOM   8088 O OE2   . GLU B 1 487 ? 53.368 -7.723  -39.209 1.00 29.87 ? 485  GLU A OE2   1 
ATOM   8089 N N     . PHE B 1 488 ? 52.790 -10.404 -44.264 1.00 23.88 ? 486  PHE A N     1 
ATOM   8090 C CA    . PHE B 1 488 ? 51.376 -10.386 -44.701 1.00 24.09 ? 486  PHE A CA    1 
ATOM   8091 C C     . PHE B 1 488 ? 51.128 -11.401 -45.824 1.00 27.17 ? 486  PHE A C     1 
ATOM   8092 O O     . PHE B 1 488 ? 50.068 -12.017 -45.823 1.00 26.06 ? 486  PHE A O     1 
ATOM   8093 C CB    . PHE B 1 488 ? 51.031 -8.960  -45.115 1.00 23.71 ? 486  PHE A CB    1 
ATOM   8094 C CG    . PHE B 1 488 ? 51.332 -7.933  -44.054 1.00 24.25 ? 486  PHE A CG    1 
ATOM   8095 C CD1   . PHE B 1 488 ? 50.471 -7.743  -42.987 1.00 26.45 ? 486  PHE A CD1   1 
ATOM   8096 C CD2   . PHE B 1 488 ? 52.486 -7.171  -44.112 1.00 24.76 ? 486  PHE A CD2   1 
ATOM   8097 C CE1   . PHE B 1 488 ? 50.749 -6.802  -42.010 1.00 24.88 ? 486  PHE A CE1   1 
ATOM   8098 C CE2   . PHE B 1 488 ? 52.765 -6.232  -43.134 1.00 25.79 ? 486  PHE A CE2   1 
ATOM   8099 C CZ    . PHE B 1 488 ? 51.897 -6.049  -42.085 1.00 27.08 ? 486  PHE A CZ    1 
ATOM   8100 N N     . SER B 1 489 ? 52.081 -11.559 -46.743 1.00 26.33 ? 487  SER A N     1 
ATOM   8101 C CA    . SER B 1 489 ? 51.913 -12.455 -47.915 1.00 26.90 ? 487  SER A CA    1 
ATOM   8102 C C     . SER B 1 489 ? 51.779 -13.906 -47.462 1.00 27.16 ? 487  SER A C     1 
ATOM   8103 O O     . SER B 1 489 ? 51.069 -14.662 -48.109 1.00 28.79 ? 487  SER A O     1 
ATOM   8104 C CB    . SER B 1 489 ? 53.080 -12.297 -48.865 1.00 28.06 ? 487  SER A CB    1 
ATOM   8105 O OG    . SER B 1 489 ? 54.280 -12.760 -48.288 1.00 29.37 ? 487  SER A OG    1 
ATOM   8106 N N     . LYS B 1 490 ? 52.462 -14.265 -46.384 1.00 29.72 ? 488  LYS A N     1 
ATOM   8107 C CA    . LYS B 1 490 ? 52.464 -15.678 -45.923 1.00 31.85 ? 488  LYS A CA    1 
ATOM   8108 C C     . LYS B 1 490 ? 51.074 -16.075 -45.406 1.00 30.98 ? 488  LYS A C     1 
ATOM   8109 O O     . LYS B 1 490 ? 50.530 -17.090 -45.822 1.00 27.80 ? 488  LYS A O     1 
ATOM   8110 C CB    . LYS B 1 490 ? 53.583 -15.876 -44.902 1.00 36.09 ? 488  LYS A CB    1 
ATOM   8111 C CG    . LYS B 1 490 ? 53.680 -17.277 -44.331 1.00 47.15 ? 488  LYS A CG    1 
ATOM   8112 C CD    . LYS B 1 490 ? 54.981 -17.525 -43.581 1.00 57.52 ? 488  LYS A CD    1 
ATOM   8113 C CE    . LYS B 1 490 ? 54.883 -18.704 -42.631 1.00 63.49 ? 488  LYS A CE    1 
ATOM   8114 N NZ    . LYS B 1 490 ? 56.222 -19.164 -42.186 1.00 71.18 ? 488  LYS A NZ    1 
ATOM   8115 N N     . PRO B 1 491 ? 50.450 -15.341 -44.461 1.00 29.75 ? 489  PRO A N     1 
ATOM   8116 C CA    . PRO B 1 491 ? 49.076 -15.662 -44.048 1.00 29.60 ? 489  PRO A CA    1 
ATOM   8117 C C     . PRO B 1 491 ? 48.028 -15.475 -45.158 1.00 25.92 ? 489  PRO A C     1 
ATOM   8118 O O     . PRO B 1 491 ? 47.058 -16.230 -45.227 1.00 26.58 ? 489  PRO A O     1 
ATOM   8119 C CB    . PRO B 1 491 ? 48.820 -14.745 -42.838 1.00 29.09 ? 489  PRO A CB    1 
ATOM   8120 C CG    . PRO B 1 491 ? 49.861 -13.654 -42.923 1.00 30.30 ? 489  PRO A CG    1 
ATOM   8121 C CD    . PRO B 1 491 ? 51.047 -14.283 -43.629 1.00 31.62 ? 489  PRO A CD    1 
ATOM   8122 N N     . LEU B 1 492 ? 48.238 -14.491 -46.020 1.00 27.41 ? 490  LEU A N     1 
ATOM   8123 C CA    . LEU B 1 492 ? 47.427 -14.335 -47.255 1.00 24.48 ? 490  LEU A CA    1 
ATOM   8124 C C     . LEU B 1 492 ? 47.444 -15.639 -48.073 1.00 26.67 ? 490  LEU A C     1 
ATOM   8125 O O     . LEU B 1 492 ? 46.357 -16.125 -48.472 1.00 24.73 ? 490  LEU A O     1 
ATOM   8126 C CB    . LEU B 1 492 ? 47.966 -13.173 -48.068 1.00 24.19 ? 490  LEU A CB    1 
ATOM   8127 C CG    . LEU B 1 492 ? 47.281 -12.997 -49.415 1.00 23.76 ? 490  LEU A CG    1 
ATOM   8128 C CD1   . LEU B 1 492 ? 45.776 -12.836 -49.213 1.00 24.38 ? 490  LEU A CD1   1 
ATOM   8129 C CD2   . LEU B 1 492 ? 47.867 -11.806 -50.154 1.00 24.32 ? 490  LEU A CD2   1 
ATOM   8130 N N     . ALA B 1 493 ? 48.621 -16.196 -48.345 1.00 25.92 ? 491  ALA A N     1 
ATOM   8131 C CA    . ALA B 1 493 ? 48.744 -17.442 -49.138 1.00 24.62 ? 491  ALA A CA    1 
ATOM   8132 C C     . ALA B 1 493 ? 47.977 -18.566 -48.448 1.00 23.23 ? 491  ALA A C     1 
ATOM   8133 O O     . ALA B 1 493 ? 47.278 -19.324 -49.174 1.00 27.87 ? 491  ALA A O     1 
ATOM   8134 C CB    . ALA B 1 493 ? 50.193 -17.812 -49.334 1.00 26.54 ? 491  ALA A CB    1 
ATOM   8135 N N     . ALA B 1 494 ? 48.079 -18.674 -47.113 1.00 22.30 ? 492  ALA A N     1 
ATOM   8136 C CA    . ALA B 1 494 ? 47.384 -19.723 -46.329 1.00 23.56 ? 492  ALA A CA    1 
ATOM   8137 C C     . ALA B 1 494 ? 45.867 -19.521 -46.474 1.00 23.99 ? 492  ALA A C     1 
ATOM   8138 O O     . ALA B 1 494 ? 45.150 -20.514 -46.619 1.00 24.36 ? 492  ALA A O     1 
ATOM   8139 C CB    . ALA B 1 494 ? 47.811 -19.728 -44.876 1.00 26.71 ? 492  ALA A CB    1 
ATOM   8140 N N     . ALA B 1 495 ? 45.397 -18.279 -46.446 1.00 21.80 ? 493  ALA A N     1 
ATOM   8141 C CA    . ALA B 1 495 ? 43.968 -17.947 -46.614 1.00 22.42 ? 493  ALA A CA    1 
ATOM   8142 C C     . ALA B 1 495 ? 43.501 -18.356 -48.028 1.00 23.99 ? 493  ALA A C     1 
ATOM   8143 O O     . ALA B 1 495 ? 42.392 -18.949 -48.165 1.00 22.80 ? 493  ALA A O     1 
ATOM   8144 C CB    . ALA B 1 495 ? 43.766 -16.473 -46.330 1.00 23.16 ? 493  ALA A CB    1 
ATOM   8145 N N     . VAL B 1 496 ? 44.299 -18.056 -49.055 1.00 23.44 ? 494  VAL A N     1 
ATOM   8146 C CA    . VAL B 1 496 ? 43.977 -18.429 -50.461 1.00 24.30 ? 494  VAL A CA    1 
ATOM   8147 C C     . VAL B 1 496 ? 43.844 -19.955 -50.564 1.00 23.94 ? 494  VAL A C     1 
ATOM   8148 O O     . VAL B 1 496 ? 42.847 -20.408 -51.155 1.00 24.55 ? 494  VAL A O     1 
ATOM   8149 C CB    . VAL B 1 496 ? 44.999 -17.853 -51.454 1.00 24.84 ? 494  VAL A CB    1 
ATOM   8150 C CG1   . VAL B 1 496 ? 44.867 -18.487 -52.835 1.00 25.53 ? 494  VAL A CG1   1 
ATOM   8151 C CG2   . VAL B 1 496 ? 44.830 -16.349 -51.546 1.00 27.08 ? 494  VAL A CG2   1 
ATOM   8152 N N     . GLU B 1 497 ? 44.770 -20.704 -49.970 1.00 24.19 ? 495  GLU A N     1 
ATOM   8153 C CA    . GLU B 1 497 ? 44.742 -22.194 -49.961 1.00 24.54 ? 495  GLU A CA    1 
ATOM   8154 C C     . GLU B 1 497 ? 43.471 -22.661 -49.255 1.00 24.95 ? 495  GLU A C     1 
ATOM   8155 O O     . GLU B 1 497 ? 42.823 -23.637 -49.747 1.00 23.33 ? 495  GLU A O     1 
ATOM   8156 C CB    . GLU B 1 497 ? 46.005 -22.750 -49.312 1.00 27.58 ? 495  GLU A CB    1 
ATOM   8157 C CG    . GLU B 1 497 ? 46.065 -24.263 -49.231 1.00 33.58 ? 495  GLU A CG    1 
ATOM   8158 C CD    . GLU B 1 497 ? 46.024 -25.004 -50.565 1.00 41.65 ? 495  GLU A CD    1 
ATOM   8159 O OE1   . GLU B 1 497 ? 46.500 -24.446 -51.562 1.00 46.45 ? 495  GLU A OE1   1 
ATOM   8160 O OE2   . GLU B 1 497 ? 45.508 -26.150 -50.606 1.00 45.06 ? 495  GLU A OE2   1 
ATOM   8161 N N     . ASN B 1 498 ? 43.096 -22.005 -48.145 1.00 24.47 ? 496  ASN A N     1 
ATOM   8162 C CA    . ASN B 1 498 ? 41.873 -22.410 -47.401 1.00 23.27 ? 496  ASN A CA    1 
ATOM   8163 C C     . ASN B 1 498 ? 40.661 -22.223 -48.330 1.00 22.95 ? 496  ASN A C     1 
ATOM   8164 O O     . ASN B 1 498 ? 39.827 -23.130 -48.415 1.00 23.43 ? 496  ASN A O     1 
ATOM   8165 C CB    . ASN B 1 498 ? 41.675 -21.663 -46.073 1.00 24.07 ? 496  ASN A CB    1 
ATOM   8166 C CG    . ASN B 1 498 ? 40.365 -22.061 -45.411 1.00 24.68 ? 496  ASN A CG    1 
ATOM   8167 O OD1   . ASN B 1 498 ? 40.234 -23.174 -44.914 1.00 23.08 ? 496  ASN A OD1   1 
ATOM   8168 N ND2   . ASN B 1 498 ? 39.356 -21.205 -45.499 1.00 24.65 ? 496  ASN A ND2   1 
ATOM   8169 N N     . LEU B 1 499 ? 40.593 -21.106 -49.048 1.00 24.28 ? 497  LEU A N     1 
ATOM   8170 C CA    . LEU B 1 499 ? 39.436 -20.779 -49.930 1.00 25.83 ? 497  LEU A CA    1 
ATOM   8171 C C     . LEU B 1 499 ? 39.390 -21.762 -51.118 1.00 25.67 ? 497  LEU A C     1 
ATOM   8172 O O     . LEU B 1 499 ? 38.271 -22.189 -51.485 1.00 24.29 ? 497  LEU A O     1 
ATOM   8173 C CB    . LEU B 1 499 ? 39.526 -19.313 -50.376 1.00 22.69 ? 497  LEU A CB    1 
ATOM   8174 C CG    . LEU B 1 499 ? 38.534 -18.905 -51.460 1.00 24.45 ? 497  LEU A CG    1 
ATOM   8175 C CD1   . LEU B 1 499 ? 37.109 -19.039 -50.952 1.00 26.45 ? 497  LEU A CD1   1 
ATOM   8176 C CD2   . LEU B 1 499 ? 38.778 -17.482 -51.944 1.00 23.76 ? 497  LEU A CD2   1 
ATOM   8177 N N     . GLU B 1 500 ? 40.553 -22.117 -51.679 1.00 26.15 ? 498  GLU A N     1 
ATOM   8178 C CA    . GLU B 1 500 ? 40.653 -23.066 -52.821 1.00 27.75 ? 498  GLU A CA    1 
ATOM   8179 C C     . GLU B 1 500 ? 40.159 -24.443 -52.397 1.00 26.07 ? 498  GLU A C     1 
ATOM   8180 O O     . GLU B 1 500 ? 39.376 -25.011 -53.141 1.00 25.16 ? 498  GLU A O     1 
ATOM   8181 C CB    . GLU B 1 500 ? 42.073 -23.149 -53.363 1.00 30.38 ? 498  GLU A CB    1 
ATOM   8182 C CG    . GLU B 1 500 ? 42.508 -21.836 -53.970 1.00 36.57 ? 498  GLU A CG    1 
ATOM   8183 C CD    . GLU B 1 500 ? 43.630 -21.916 -54.988 1.00 46.18 ? 498  GLU A CD    1 
ATOM   8184 O OE1   . GLU B 1 500 ? 43.371 -21.515 -56.155 1.00 57.46 ? 498  GLU A OE1   1 
ATOM   8185 O OE2   . GLU B 1 500 ? 44.744 -22.354 -54.619 1.00 47.03 ? 498  GLU A OE2   1 
ATOM   8186 N N     . GLU B 1 501 ? 40.591 -24.941 -51.239 1.00 26.40 ? 499  GLU A N     1 
ATOM   8187 C CA    . GLU B 1 501 ? 40.139 -26.251 -50.698 1.00 27.29 ? 499  GLU A CA    1 
ATOM   8188 C C     . GLU B 1 501 ? 38.625 -26.221 -50.443 1.00 26.38 ? 499  GLU A C     1 
ATOM   8189 O O     . GLU B 1 501 ? 37.986 -27.204 -50.727 1.00 24.06 ? 499  GLU A O     1 
ATOM   8190 C CB    . GLU B 1 501 ? 40.909 -26.628 -49.433 1.00 27.97 ? 499  GLU A CB    1 
ATOM   8191 C CG    . GLU B 1 501 ? 42.359 -26.955 -49.712 1.00 33.01 ? 499  GLU A CG    1 
ATOM   8192 C CD    . GLU B 1 501 ? 43.179 -27.261 -48.466 1.00 42.94 ? 499  GLU A CD    1 
ATOM   8193 O OE1   . GLU B 1 501 ? 44.425 -27.155 -48.533 1.00 46.85 ? 499  GLU A OE1   1 
ATOM   8194 O OE2   . GLU B 1 501 ? 42.571 -27.600 -47.422 1.00 47.18 ? 499  GLU A OE2   1 
ATOM   8195 N N     . LEU B 1 502 ? 38.092 -25.130 -49.894 1.00 25.90 ? 500  LEU A N     1 
ATOM   8196 C CA    . LEU B 1 502 ? 36.646 -24.990 -49.612 1.00 25.34 ? 500  LEU A CA    1 
ATOM   8197 C C     . LEU B 1 502 ? 35.905 -24.966 -50.958 1.00 26.00 ? 500  LEU A C     1 
ATOM   8198 O O     . LEU B 1 502 ? 34.833 -25.608 -51.066 1.00 25.32 ? 500  LEU A O     1 
ATOM   8199 C CB    . LEU B 1 502 ? 36.399 -23.716 -48.803 1.00 23.92 ? 500  LEU A CB    1 
ATOM   8200 C CG    . LEU B 1 502 ? 34.951 -23.544 -48.342 1.00 23.35 ? 500  LEU A CG    1 
ATOM   8201 C CD1   . LEU B 1 502 ? 34.522 -24.692 -47.435 1.00 25.18 ? 500  LEU A CD1   1 
ATOM   8202 C CD2   . LEU B 1 502 ? 34.766 -22.226 -47.643 1.00 23.48 ? 500  LEU A CD2   1 
ATOM   8203 N N     . THR B 1 503 ? 36.455 -24.274 -51.959 1.00 25.32 ? 501  THR A N     1 
ATOM   8204 C CA    . THR B 1 503 ? 35.864 -24.254 -53.321 1.00 25.91 ? 501  THR A CA    1 
ATOM   8205 C C     . THR B 1 503 ? 35.799 -25.684 -53.877 1.00 25.86 ? 501  THR A C     1 
ATOM   8206 O O     . THR B 1 503 ? 34.705 -26.089 -54.331 1.00 24.59 ? 501  THR A O     1 
ATOM   8207 C CB    . THR B 1 503 ? 36.605 -23.285 -54.230 1.00 27.37 ? 501  THR A CB    1 
ATOM   8208 O OG1   . THR B 1 503 ? 36.546 -21.998 -53.615 1.00 27.06 ? 501  THR A OG1   1 
ATOM   8209 C CG2   . THR B 1 503 ? 36.023 -23.252 -55.627 1.00 29.67 ? 501  THR A CG2   1 
ATOM   8210 N N     . ALA B 1 504 ? 36.899 -26.444 -53.798 1.00 26.52 ? 502  ALA A N     1 
ATOM   8211 C CA    . ALA B 1 504 ? 36.950 -27.840 -54.282 1.00 27.21 ? 502  ALA A CA    1 
ATOM   8212 C C     . ALA B 1 504 ? 35.960 -28.695 -53.488 1.00 27.33 ? 502  ALA A C     1 
ATOM   8213 O O     . ALA B 1 504 ? 35.228 -29.477 -54.121 1.00 28.79 ? 502  ALA A O     1 
ATOM   8214 C CB    . ALA B 1 504 ? 38.355 -28.388 -54.271 1.00 27.38 ? 502  ALA A CB    1 
ATOM   8215 N N     . TRP B 1 505 ? 35.896 -28.547 -52.166 1.00 27.85 ? 503  TRP A N     1 
ATOM   8216 C CA    . TRP B 1 505 ? 34.885 -29.253 -51.345 1.00 27.72 ? 503  TRP A CA    1 
ATOM   8217 C C     . TRP B 1 505 ? 33.491 -28.994 -51.928 1.00 26.94 ? 503  TRP A C     1 
ATOM   8218 O O     . TRP B 1 505 ? 32.709 -29.941 -52.060 1.00 25.45 ? 503  TRP A O     1 
ATOM   8219 C CB    . TRP B 1 505 ? 34.965 -28.829 -49.869 1.00 27.48 ? 503  TRP A CB    1 
ATOM   8220 C CG    . TRP B 1 505 ? 33.905 -29.489 -49.049 1.00 26.93 ? 503  TRP A CG    1 
ATOM   8221 C CD1   . TRP B 1 505 ? 33.997 -30.698 -48.424 1.00 27.95 ? 503  TRP A CD1   1 
ATOM   8222 C CD2   . TRP B 1 505 ? 32.584 -28.991 -48.776 1.00 24.84 ? 503  TRP A CD2   1 
ATOM   8223 N NE1   . TRP B 1 505 ? 32.827 -30.992 -47.793 1.00 26.87 ? 503  TRP A NE1   1 
ATOM   8224 C CE2   . TRP B 1 505 ? 31.941 -29.964 -47.988 1.00 26.85 ? 503  TRP A CE2   1 
ATOM   8225 C CE3   . TRP B 1 505 ? 31.895 -27.823 -49.110 1.00 27.14 ? 503  TRP A CE3   1 
ATOM   8226 C CZ2   . TRP B 1 505 ? 30.630 -29.809 -47.542 1.00 27.76 ? 503  TRP A CZ2   1 
ATOM   8227 C CZ3   . TRP B 1 505 ? 30.584 -27.680 -48.697 1.00 27.26 ? 503  TRP A CZ3   1 
ATOM   8228 C CH2   . TRP B 1 505 ? 29.956 -28.673 -47.948 1.00 28.09 ? 503  TRP A CH2   1 
ATOM   8229 N N     . LEU B 1 506 ? 33.190 -27.745 -52.272 1.00 25.81 ? 504  LEU A N     1 
ATOM   8230 C CA    . LEU B 1 506 ? 31.813 -27.334 -52.633 1.00 28.08 ? 504  LEU A CA    1 
ATOM   8231 C C     . LEU B 1 506 ? 31.458 -27.850 -54.040 1.00 28.83 ? 504  LEU A C     1 
ATOM   8232 O O     . LEU B 1 506 ? 30.346 -28.374 -54.210 1.00 27.06 ? 504  LEU A O     1 
ATOM   8233 C CB    . LEU B 1 506 ? 31.708 -25.810 -52.553 1.00 29.49 ? 504  LEU A CB    1 
ATOM   8234 C CG    . LEU B 1 506 ? 30.388 -25.249 -53.068 1.00 32.61 ? 504  LEU A CG    1 
ATOM   8235 C CD1   . LEU B 1 506 ? 29.214 -25.753 -52.230 1.00 32.02 ? 504  LEU A CD1   1 
ATOM   8236 C CD2   . LEU B 1 506 ? 30.426 -23.728 -53.106 1.00 36.42 ? 504  LEU A CD2   1 
ATOM   8237 N N     . LEU B 1 507 ? 32.362 -27.710 -55.012 1.00 29.50 ? 505  LEU A N     1 
ATOM   8238 C CA    . LEU B 1 507 ? 32.161 -28.247 -56.387 1.00 29.84 ? 505  LEU A CA    1 
ATOM   8239 C C     . LEU B 1 507 ? 31.799 -29.734 -56.293 1.00 29.09 ? 505  LEU A C     1 
ATOM   8240 O O     . LEU B 1 507 ? 30.809 -30.141 -56.912 1.00 31.28 ? 505  LEU A O     1 
ATOM   8241 C CB    . LEU B 1 507 ? 33.423 -28.011 -57.223 1.00 32.71 ? 505  LEU A CB    1 
ATOM   8242 C CG    . LEU B 1 507 ? 33.625 -26.568 -57.693 1.00 36.30 ? 505  LEU A CG    1 
ATOM   8243 C CD1   . LEU B 1 507 ? 35.052 -26.321 -58.172 1.00 39.84 ? 505  LEU A CD1   1 
ATOM   8244 C CD2   . LEU B 1 507 ? 32.646 -26.226 -58.801 1.00 40.53 ? 505  LEU A CD2   1 
ATOM   8245 N N     . ASP B 1 508 ? 32.524 -30.503 -55.485 1.00 29.67 ? 506  ASP A N     1 
ATOM   8246 C CA    . ASP B 1 508 ? 32.276 -31.951 -55.273 1.00 29.58 ? 506  ASP A CA    1 
ATOM   8247 C C     . ASP B 1 508 ? 30.920 -32.146 -54.581 1.00 30.79 ? 506  ASP A C     1 
ATOM   8248 O O     . ASP B 1 508 ? 30.109 -32.963 -55.073 1.00 29.63 ? 506  ASP A O     1 
ATOM   8249 C CB    . ASP B 1 508 ? 33.387 -32.607 -54.454 1.00 33.56 ? 506  ASP A CB    1 
ATOM   8250 C CG    . ASP B 1 508 ? 33.154 -34.095 -54.237 1.00 37.23 ? 506  ASP A CG    1 
ATOM   8251 O OD1   . ASP B 1 508 ? 33.197 -34.836 -55.229 1.00 40.91 ? 506  ASP A OD1   1 
ATOM   8252 O OD2   . ASP B 1 508 ? 32.875 -34.490 -53.090 1.00 39.12 ? 506  ASP A OD2   1 
ATOM   8253 N N     . ARG B 1 509 ? 30.667 -31.436 -53.479 1.00 29.44 ? 507  ARG A N     1 
ATOM   8254 C CA    . ARG B 1 509 ? 29.487 -31.714 -52.622 1.00 31.81 ? 507  ARG A CA    1 
ATOM   8255 C C     . ARG B 1 509 ? 28.187 -31.324 -53.347 1.00 31.11 ? 507  ARG A C     1 
ATOM   8256 O O     . ARG B 1 509 ? 27.163 -32.003 -53.110 1.00 34.39 ? 507  ARG A O     1 
ATOM   8257 C CB    . ARG B 1 509 ? 29.667 -31.008 -51.277 1.00 35.68 ? 507  ARG A CB    1 
ATOM   8258 C CG    . ARG B 1 509 ? 28.458 -31.113 -50.362 1.00 39.80 ? 507  ARG A CG    1 
ATOM   8259 C CD    . ARG B 1 509 ? 28.162 -32.537 -49.940 1.00 45.67 ? 507  ARG A CD    1 
ATOM   8260 N NE    . ARG B 1 509 ? 29.190 -32.990 -49.026 1.00 47.41 ? 507  ARG A NE    1 
ATOM   8261 C CZ    . ARG B 1 509 ? 29.068 -33.116 -47.704 1.00 47.14 ? 507  ARG A CZ    1 
ATOM   8262 N NH1   . ARG B 1 509 ? 30.104 -33.536 -46.999 1.00 46.94 ? 507  ARG A NH1   1 
ATOM   8263 N NH2   . ARG B 1 509 ? 27.939 -32.823 -47.086 1.00 47.68 ? 507  ARG A NH2   1 
ATOM   8264 N N     . ALA B 1 510 ? 28.202 -30.266 -54.163 1.00 29.06 ? 508  ALA A N     1 
ATOM   8265 C CA    . ALA B 1 510 ? 27.029 -29.739 -54.908 1.00 29.58 ? 508  ALA A CA    1 
ATOM   8266 C C     . ALA B 1 510 ? 26.573 -30.687 -56.033 1.00 31.72 ? 508  ALA A C     1 
ATOM   8267 O O     . ALA B 1 510 ? 25.423 -30.553 -56.473 1.00 31.93 ? 508  ALA A O     1 
ATOM   8268 C CB    . ALA B 1 510 ? 27.337 -28.390 -55.501 1.00 27.55 ? 508  ALA A CB    1 
ATOM   8269 N N     . LYS B 1 511 ? 27.429 -31.575 -56.534 1.00 34.39 ? 509  LYS A N     1 
ATOM   8270 C CA    . LYS B 1 511 ? 27.046 -32.513 -57.628 1.00 36.36 ? 509  LYS A CA    1 
ATOM   8271 C C     . LYS B 1 511 ? 25.865 -33.378 -57.187 1.00 35.11 ? 509  LYS A C     1 
ATOM   8272 O O     . LYS B 1 511 ? 26.022 -34.179 -56.232 1.00 34.45 ? 509  LYS A O     1 
ATOM   8273 C CB    . LYS B 1 511 ? 28.208 -33.430 -58.005 1.00 41.07 ? 509  LYS A CB    1 
ATOM   8274 C CG    . LYS B 1 511 ? 29.242 -32.778 -58.895 1.00 46.01 ? 509  LYS A CG    1 
ATOM   8275 C CD    . LYS B 1 511 ? 30.169 -33.785 -59.540 1.00 50.70 ? 509  LYS A CD    1 
ATOM   8276 C CE    . LYS B 1 511 ? 31.623 -33.392 -59.404 1.00 55.71 ? 509  LYS A CE    1 
ATOM   8277 N NZ    . LYS B 1 511 ? 31.849 -31.980 -59.798 1.00 57.07 ? 509  LYS A NZ    1 
ATOM   8278 N N     . GLY B 1 512 ? 24.732 -33.228 -57.873 1.00 37.83 ? 510  GLY A N     1 
ATOM   8279 C CA    . GLY B 1 512 ? 23.498 -33.992 -57.609 1.00 37.49 ? 510  GLY A CA    1 
ATOM   8280 C C     . GLY B 1 512 ? 22.819 -33.611 -56.297 1.00 38.57 ? 510  GLY A C     1 
ATOM   8281 O O     . GLY B 1 512 ? 21.879 -34.309 -55.896 1.00 38.49 ? 510  GLY A O     1 
ATOM   8282 N N     . ASN B 1 513 ? 23.255 -32.547 -55.625 1.00 36.35 ? 511  ASN A N     1 
ATOM   8283 C CA    . ASN B 1 513 ? 22.665 -32.135 -54.324 1.00 36.21 ? 511  ASN A CA    1 
ATOM   8284 C C     . ASN B 1 513 ? 22.445 -30.629 -54.330 1.00 31.86 ? 511  ASN A C     1 
ATOM   8285 O O     . ASN B 1 513 ? 23.249 -29.883 -53.771 1.00 28.09 ? 511  ASN A O     1 
ATOM   8286 C CB    . ASN B 1 513 ? 23.548 -32.560 -53.157 1.00 37.95 ? 511  ASN A CB    1 
ATOM   8287 C CG    . ASN B 1 513 ? 23.906 -34.028 -53.203 1.00 41.74 ? 511  ASN A CG    1 
ATOM   8288 O OD1   . ASN B 1 513 ? 23.021 -34.885 -53.168 1.00 42.91 ? 511  ASN A OD1   1 
ATOM   8289 N ND2   . ASN B 1 513 ? 25.198 -34.318 -53.227 1.00 41.10 ? 511  ASN A ND2   1 
ATOM   8290 N N     . PRO B 1 514 ? 21.373 -30.157 -54.997 1.00 31.97 ? 512  PRO A N     1 
ATOM   8291 C CA    . PRO B 1 514 ? 21.092 -28.724 -55.119 1.00 30.99 ? 512  PRO A CA    1 
ATOM   8292 C C     . PRO B 1 514 ? 21.047 -27.975 -53.776 1.00 27.40 ? 512  PRO A C     1 
ATOM   8293 O O     . PRO B 1 514 ? 21.335 -26.811 -53.740 1.00 27.07 ? 512  PRO A O     1 
ATOM   8294 C CB    . PRO B 1 514 ? 19.693 -28.687 -55.755 1.00 33.66 ? 512  PRO A CB    1 
ATOM   8295 C CG    . PRO B 1 514 ? 19.581 -29.995 -56.496 1.00 35.58 ? 512  PRO A CG    1 
ATOM   8296 C CD    . PRO B 1 514 ? 20.362 -30.989 -55.659 1.00 34.18 ? 512  PRO A CD    1 
ATOM   8297 N N     . ASN B 1 515 ? 20.632 -28.619 -52.692 1.00 25.49 ? 513  ASN A N     1 
ATOM   8298 C CA    . ASN B 1 515 ? 20.469 -27.872 -51.405 1.00 26.17 ? 513  ASN A CA    1 
ATOM   8299 C C     . ASN B 1 515 ? 21.834 -27.383 -50.908 1.00 25.41 ? 513  ASN A C     1 
ATOM   8300 O O     . ASN B 1 515 ? 21.864 -26.402 -50.170 1.00 25.42 ? 513  ASN A O     1 
ATOM   8301 C CB    . ASN B 1 515 ? 19.817 -28.708 -50.308 1.00 25.77 ? 513  ASN A CB    1 
ATOM   8302 C CG    . ASN B 1 515 ? 18.331 -28.872 -50.522 1.00 26.78 ? 513  ASN A CG    1 
ATOM   8303 O OD1   . ASN B 1 515 ? 17.702 -28.084 -51.221 1.00 29.32 ? 513  ASN A OD1   1 
ATOM   8304 N ND2   . ASN B 1 515 ? 17.772 -29.903 -49.931 1.00 26.83 ? 513  ASN A ND2   1 
ATOM   8305 N N     . GLU B 1 516 ? 22.910 -28.082 -51.264 1.00 24.36 ? 514  GLU A N     1 
ATOM   8306 C CA    . GLU B 1 516 ? 24.283 -27.753 -50.804 1.00 26.28 ? 514  GLU A CA    1 
ATOM   8307 C C     . GLU B 1 516 ? 24.644 -26.328 -51.220 1.00 27.25 ? 514  GLU A C     1 
ATOM   8308 O O     . GLU B 1 516 ? 25.452 -25.684 -50.530 1.00 26.12 ? 514  GLU A O     1 
ATOM   8309 C CB    . GLU B 1 516 ? 25.269 -28.774 -51.354 1.00 24.78 ? 514  GLU A CB    1 
ATOM   8310 C CG    . GLU B 1 516 ? 25.006 -30.163 -50.776 1.00 27.20 ? 514  GLU A CG    1 
ATOM   8311 C CD    . GLU B 1 516 ? 25.277 -30.349 -49.286 1.00 27.77 ? 514  GLU A CD    1 
ATOM   8312 O OE1   . GLU B 1 516 ? 25.694 -29.390 -48.610 1.00 24.67 ? 514  GLU A OE1   1 
ATOM   8313 O OE2   . GLU B 1 516 ? 25.168 -31.492 -48.829 1.00 34.39 ? 514  GLU A OE2   1 
ATOM   8314 N N     . ILE B 1 517 ? 24.112 -25.875 -52.350 1.00 22.87 ? 515  ILE A N     1 
ATOM   8315 C CA    . ILE B 1 517 ? 24.538 -24.574 -52.914 1.00 24.92 ? 515  ILE A CA    1 
ATOM   8316 C C     . ILE B 1 517 ? 24.064 -23.469 -51.961 1.00 21.01 ? 515  ILE A C     1 
ATOM   8317 O O     . ILE B 1 517 ? 24.910 -22.730 -51.443 1.00 23.14 ? 515  ILE A O     1 
ATOM   8318 C CB    . ILE B 1 517 ? 24.063 -24.402 -54.373 1.00 24.96 ? 515  ILE A CB    1 
ATOM   8319 C CG1   . ILE B 1 517 ? 24.585 -25.538 -55.263 1.00 29.68 ? 515  ILE A CG1   1 
ATOM   8320 C CG2   . ILE B 1 517 ? 24.509 -23.051 -54.883 1.00 24.95 ? 515  ILE A CG2   1 
ATOM   8321 C CD1   . ILE B 1 517 ? 24.139 -25.477 -56.727 1.00 30.50 ? 515  ILE A CD1   1 
ATOM   8322 N N     . GLY B 1 518 ? 22.772 -23.359 -51.725 1.00 20.35 ? 516  GLY A N     1 
ATOM   8323 C CA    . GLY B 1 518 ? 22.216 -22.336 -50.819 1.00 22.41 ? 516  GLY A CA    1 
ATOM   8324 C C     . GLY B 1 518 ? 22.769 -22.473 -49.406 1.00 21.64 ? 516  GLY A C     1 
ATOM   8325 O O     . GLY B 1 518 ? 22.946 -21.450 -48.764 1.00 20.14 ? 516  GLY A O     1 
ATOM   8326 N N     . ALA B 1 519 ? 23.002 -23.711 -48.934 1.00 23.24 ? 517  ALA A N     1 
ATOM   8327 C CA    . ALA B 1 519 ? 23.473 -24.024 -47.564 1.00 21.73 ? 517  ALA A CA    1 
ATOM   8328 C C     . ALA B 1 519 ? 24.839 -23.373 -47.335 1.00 22.45 ? 517  ALA A C     1 
ATOM   8329 O O     . ALA B 1 519 ? 25.054 -22.763 -46.266 1.00 21.29 ? 517  ALA A O     1 
ATOM   8330 C CB    . ALA B 1 519 ? 23.522 -25.522 -47.337 1.00 22.33 ? 517  ALA A CB    1 
ATOM   8331 N N     . ALA B 1 520 ? 25.721 -23.461 -48.333 1.00 21.33 ? 518  ALA A N     1 
ATOM   8332 C CA    . ALA B 1 520 ? 27.091 -22.922 -48.253 1.00 21.70 ? 518  ALA A CA    1 
ATOM   8333 C C     . ALA B 1 520 ? 27.081 -21.399 -48.438 1.00 22.37 ? 518  ALA A C     1 
ATOM   8334 O O     . ALA B 1 520 ? 27.993 -20.752 -47.925 1.00 23.16 ? 518  ALA A O     1 
ATOM   8335 C CB    . ALA B 1 520 ? 27.969 -23.591 -49.281 1.00 22.00 ? 518  ALA A CB    1 
ATOM   8336 N N     . SER B 1 521 ? 26.117 -20.880 -49.193 1.00 21.79 ? 519  SER A N     1 
ATOM   8337 C CA    . SER B 1 521 ? 26.196 -19.579 -49.904 1.00 22.66 ? 519  SER A CA    1 
ATOM   8338 C C     . SER B 1 521 ? 26.712 -18.453 -48.986 1.00 22.78 ? 519  SER A C     1 
ATOM   8339 O O     . SER B 1 521 ? 27.789 -17.890 -49.278 1.00 21.58 ? 519  SER A O     1 
ATOM   8340 C CB    . SER B 1 521 ? 24.879 -19.248 -50.565 1.00 21.69 ? 519  SER A CB    1 
ATOM   8341 O OG    . SER B 1 521 ? 23.818 -19.178 -49.643 1.00 23.78 ? 519  SER A OG    1 
ATOM   8342 N N     . VAL B 1 522 ? 25.973 -18.068 -47.952 1.00 22.00 ? 520  VAL A N     1 
ATOM   8343 C CA    . VAL B 1 522 ? 26.304 -16.833 -47.185 1.00 21.42 ? 520  VAL A CA    1 
ATOM   8344 C C     . VAL B 1 522 ? 27.656 -17.012 -46.468 1.00 21.45 ? 520  VAL A C     1 
ATOM   8345 O O     . VAL B 1 522 ? 28.502 -16.107 -46.557 1.00 22.12 ? 520  VAL A O     1 
ATOM   8346 C CB    . VAL B 1 522 ? 25.182 -16.451 -46.211 1.00 23.05 ? 520  VAL A CB    1 
ATOM   8347 C CG1   . VAL B 1 522 ? 25.665 -15.445 -45.148 1.00 21.50 ? 520  VAL A CG1   1 
ATOM   8348 C CG2   . VAL B 1 522 ? 23.965 -15.934 -46.987 1.00 25.27 ? 520  VAL A CG2   1 
ATOM   8349 N N     . GLU B 1 523 ? 27.883 -18.135 -45.797 1.00 22.29 ? 521  GLU A N     1 
ATOM   8350 C CA    . GLU B 1 523 ? 29.146 -18.320 -45.029 1.00 23.32 ? 521  GLU A CA    1 
ATOM   8351 C C     . GLU B 1 523 ? 30.316 -18.455 -46.000 1.00 22.46 ? 521  GLU A C     1 
ATOM   8352 O O     . GLU B 1 523 ? 31.390 -17.953 -45.697 1.00 21.44 ? 521  GLU A O     1 
ATOM   8353 C CB    . GLU B 1 523 ? 29.020 -19.485 -44.064 1.00 23.27 ? 521  GLU A CB    1 
ATOM   8354 C CG    . GLU B 1 523 ? 28.146 -19.092 -42.886 1.00 26.23 ? 521  GLU A CG    1 
ATOM   8355 C CD    . GLU B 1 523 ? 27.805 -20.197 -41.912 1.00 27.84 ? 521  GLU A CD    1 
ATOM   8356 O OE1   . GLU B 1 523 ? 27.692 -21.339 -42.347 1.00 34.50 ? 521  GLU A OE1   1 
ATOM   8357 O OE2   . GLU B 1 523 ? 27.665 -19.897 -40.709 1.00 30.35 ? 521  GLU A OE2   1 
ATOM   8358 N N     . TYR B 1 524 ? 30.110 -19.080 -47.155 1.00 22.16 ? 522  TYR A N     1 
ATOM   8359 C CA    . TYR B 1 524 ? 31.183 -19.152 -48.158 1.00 21.31 ? 522  TYR A CA    1 
ATOM   8360 C C     . TYR B 1 524 ? 31.525 -17.734 -48.614 1.00 20.56 ? 522  TYR A C     1 
ATOM   8361 O O     . TYR B 1 524 ? 32.721 -17.389 -48.732 1.00 21.10 ? 522  TYR A O     1 
ATOM   8362 C CB    . TYR B 1 524 ? 30.765 -20.045 -49.316 1.00 23.20 ? 522  TYR A CB    1 
ATOM   8363 C CG    . TYR B 1 524 ? 31.767 -20.080 -50.435 1.00 22.37 ? 522  TYR A CG    1 
ATOM   8364 C CD1   . TYR B 1 524 ? 31.847 -19.070 -51.374 1.00 22.73 ? 522  TYR A CD1   1 
ATOM   8365 C CD2   . TYR B 1 524 ? 32.648 -21.137 -50.528 1.00 22.95 ? 522  TYR A CD2   1 
ATOM   8366 C CE1   . TYR B 1 524 ? 32.750 -19.144 -52.420 1.00 24.05 ? 522  TYR A CE1   1 
ATOM   8367 C CE2   . TYR B 1 524 ? 33.547 -21.232 -51.566 1.00 24.94 ? 522  TYR A CE2   1 
ATOM   8368 C CZ    . TYR B 1 524 ? 33.608 -20.230 -52.507 1.00 25.01 ? 522  TYR A CZ    1 
ATOM   8369 O OH    . TYR B 1 524 ? 34.504 -20.381 -53.515 1.00 24.42 ? 522  TYR A OH    1 
ATOM   8370 N N     . LEU B 1 525 ? 30.507 -16.942 -48.927 1.00 20.85 ? 523  LEU A N     1 
ATOM   8371 C CA    . LEU B 1 525 ? 30.743 -15.555 -49.382 1.00 21.57 ? 523  LEU A CA    1 
ATOM   8372 C C     . LEU B 1 525 ? 31.582 -14.804 -48.337 1.00 21.88 ? 523  LEU A C     1 
ATOM   8373 O O     . LEU B 1 525 ? 32.488 -14.025 -48.750 1.00 22.73 ? 523  LEU A O     1 
ATOM   8374 C CB    . LEU B 1 525 ? 29.424 -14.865 -49.698 1.00 20.58 ? 523  LEU A CB    1 
ATOM   8375 C CG    . LEU B 1 525 ? 29.555 -13.499 -50.368 1.00 20.14 ? 523  LEU A CG    1 
ATOM   8376 C CD1   . LEU B 1 525 ? 28.379 -13.208 -51.258 1.00 21.35 ? 523  LEU A CD1   1 
ATOM   8377 C CD2   . LEU B 1 525 ? 29.705 -12.397 -49.325 1.00 21.86 ? 523  LEU A CD2   1 
ATOM   8378 N N     . HIS B 1 526 ? 31.356 -15.047 -47.044 1.00 21.04 ? 524  HIS A N     1 
ATOM   8379 C CA    . HIS B 1 526 ? 32.149 -14.404 -45.969 1.00 21.73 ? 524  HIS A CA    1 
ATOM   8380 C C     . HIS B 1 526 ? 33.585 -14.899 -46.032 1.00 21.70 ? 524  HIS A C     1 
ATOM   8381 O O     . HIS B 1 526 ? 34.488 -14.031 -45.943 1.00 19.59 ? 524  HIS A O     1 
ATOM   8382 C CB    . HIS B 1 526 ? 31.509 -14.564 -44.572 1.00 20.79 ? 524  HIS A CB    1 
ATOM   8383 C CG    . HIS B 1 526 ? 30.419 -13.577 -44.319 1.00 21.93 ? 524  HIS A CG    1 
ATOM   8384 N ND1   . HIS B 1 526 ? 30.306 -12.878 -43.133 1.00 24.20 ? 524  HIS A ND1   1 
ATOM   8385 C CD2   . HIS B 1 526 ? 29.401 -13.161 -45.088 1.00 23.65 ? 524  HIS A CD2   1 
ATOM   8386 C CE1   . HIS B 1 526 ? 29.249 -12.086 -43.188 1.00 24.14 ? 524  HIS A CE1   1 
ATOM   8387 N NE2   . HIS B 1 526 ? 28.676 -12.232 -44.374 1.00 23.88 ? 524  HIS A NE2   1 
ATOM   8388 N N     . VAL B 1 527 ? 33.807 -16.216 -46.194 1.00 21.45 ? 525  VAL A N     1 
ATOM   8389 C CA    . VAL B 1 527 ? 35.203 -16.734 -46.291 1.00 22.36 ? 525  VAL A CA    1 
ATOM   8390 C C     . VAL B 1 527 ? 35.891 -16.003 -47.450 1.00 22.49 ? 525  VAL A C     1 
ATOM   8391 O O     . VAL B 1 527 ? 37.013 -15.493 -47.279 1.00 23.44 ? 525  VAL A O     1 
ATOM   8392 C CB    . VAL B 1 527 ? 35.258 -18.260 -46.467 1.00 22.49 ? 525  VAL A CB    1 
ATOM   8393 C CG1   . VAL B 1 527 ? 36.676 -18.709 -46.729 1.00 22.70 ? 525  VAL A CG1   1 
ATOM   8394 C CG2   . VAL B 1 527 ? 34.682 -18.988 -45.254 1.00 22.48 ? 525  VAL A CG2   1 
ATOM   8395 N N     . PHE B 1 528 ? 35.214 -15.925 -48.597 1.00 22.43 ? 526  PHE A N     1 
ATOM   8396 C CA    . PHE B 1 528 ? 35.710 -15.221 -49.798 1.00 21.45 ? 526  PHE A CA    1 
ATOM   8397 C C     . PHE B 1 528 ? 36.071 -13.780 -49.392 1.00 20.88 ? 526  PHE A C     1 
ATOM   8398 O O     . PHE B 1 528 ? 37.210 -13.337 -49.691 1.00 20.81 ? 526  PHE A O     1 
ATOM   8399 C CB    . PHE B 1 528 ? 34.683 -15.298 -50.939 1.00 20.40 ? 526  PHE A CB    1 
ATOM   8400 C CG    . PHE B 1 528 ? 35.229 -14.867 -52.282 1.00 21.61 ? 526  PHE A CG    1 
ATOM   8401 C CD1   . PHE B 1 528 ? 35.548 -13.536 -52.523 1.00 22.70 ? 526  PHE A CD1   1 
ATOM   8402 C CD2   . PHE B 1 528 ? 35.481 -15.797 -53.279 1.00 20.81 ? 526  PHE A CD2   1 
ATOM   8403 C CE1   . PHE B 1 528 ? 36.079 -13.137 -53.743 1.00 24.27 ? 526  PHE A CE1   1 
ATOM   8404 C CE2   . PHE B 1 528 ? 36.020 -15.398 -54.498 1.00 23.05 ? 526  PHE A CE2   1 
ATOM   8405 C CZ    . PHE B 1 528 ? 36.312 -14.069 -54.733 1.00 22.71 ? 526  PHE A CZ    1 
ATOM   8406 N N     . GLY B 1 529 ? 35.137 -13.085 -48.747 1.00 19.20 ? 527  GLY A N     1 
ATOM   8407 C CA    . GLY B 1 529 ? 35.288 -11.673 -48.317 1.00 19.91 ? 527  GLY A CA    1 
ATOM   8408 C C     . GLY B 1 529 ? 36.545 -11.454 -47.463 1.00 20.06 ? 527  GLY A C     1 
ATOM   8409 O O     . GLY B 1 529 ? 37.334 -10.592 -47.796 1.00 21.35 ? 527  GLY A O     1 
ATOM   8410 N N     . TYR B 1 530 ? 36.746 -12.224 -46.405 1.00 21.24 ? 528  TYR A N     1 
ATOM   8411 C CA    . TYR B 1 530 ? 37.921 -12.073 -45.504 1.00 21.74 ? 528  TYR A CA    1 
ATOM   8412 C C     . TYR B 1 530 ? 39.208 -12.390 -46.272 1.00 22.36 ? 528  TYR A C     1 
ATOM   8413 O O     . TYR B 1 530 ? 40.260 -11.815 -45.940 1.00 21.24 ? 528  TYR A O     1 
ATOM   8414 C CB    . TYR B 1 530 ? 37.782 -12.966 -44.272 1.00 22.49 ? 528  TYR A CB    1 
ATOM   8415 C CG    . TYR B 1 530 ? 36.721 -12.509 -43.307 1.00 22.24 ? 528  TYR A CG    1 
ATOM   8416 C CD1   . TYR B 1 530 ? 36.828 -11.291 -42.659 1.00 22.74 ? 528  TYR A CD1   1 
ATOM   8417 C CD2   . TYR B 1 530 ? 35.598 -13.278 -43.048 1.00 23.28 ? 528  TYR A CD2   1 
ATOM   8418 C CE1   . TYR B 1 530 ? 35.846 -10.841 -41.789 1.00 21.34 ? 528  TYR A CE1   1 
ATOM   8419 C CE2   . TYR B 1 530 ? 34.609 -12.845 -42.181 1.00 22.16 ? 528  TYR A CE2   1 
ATOM   8420 C CZ    . TYR B 1 530 ? 34.739 -11.621 -41.548 1.00 23.00 ? 528  TYR A CZ    1 
ATOM   8421 O OH    . TYR B 1 530 ? 33.788 -11.178 -40.674 1.00 21.20 ? 528  TYR A OH    1 
ATOM   8422 N N     . THR B 1 531 ? 39.141 -13.329 -47.223 1.00 21.77 ? 529  THR A N     1 
ATOM   8423 C CA    . THR B 1 531 ? 40.288 -13.680 -48.096 1.00 22.00 ? 529  THR A CA    1 
ATOM   8424 C C     . THR B 1 531 ? 40.600 -12.494 -49.009 1.00 20.91 ? 529  THR A C     1 
ATOM   8425 O O     . THR B 1 531 ? 41.785 -12.079 -49.071 1.00 19.65 ? 529  THR A O     1 
ATOM   8426 C CB    . THR B 1 531 ? 40.047 -14.988 -48.847 1.00 22.16 ? 529  THR A CB    1 
ATOM   8427 O OG1   . THR B 1 531 ? 39.628 -15.932 -47.862 1.00 22.50 ? 529  THR A OG1   1 
ATOM   8428 C CG2   . THR B 1 531 ? 41.291 -15.457 -49.572 1.00 23.34 ? 529  THR A CG2   1 
ATOM   8429 N N     . ALA B 1 532 ? 39.585 -11.909 -49.641 1.00 22.07 ? 530  ALA A N     1 
ATOM   8430 C CA    . ALA B 1 532 ? 39.729 -10.714 -50.503 1.00 20.97 ? 530  ALA A CA    1 
ATOM   8431 C C     . ALA B 1 532 ? 40.282 -9.531  -49.694 1.00 21.35 ? 530  ALA A C     1 
ATOM   8432 O O     . ALA B 1 532 ? 41.235 -8.823  -50.178 1.00 21.60 ? 530  ALA A O     1 
ATOM   8433 C CB    . ALA B 1 532 ? 38.412 -10.385 -51.200 1.00 22.11 ? 530  ALA A CB    1 
ATOM   8434 N N     . TYR B 1 533 ? 39.800 -9.316  -48.477 1.00 20.27 ? 531  TYR A N     1 
ATOM   8435 C CA    . TYR B 1 533 ? 40.296 -8.194  -47.629 1.00 19.96 ? 531  TYR A CA    1 
ATOM   8436 C C     . TYR B 1 533 ? 41.754 -8.448  -47.213 1.00 20.81 ? 531  TYR A C     1 
ATOM   8437 O O     . TYR B 1 533 ? 42.477 -7.490  -47.068 1.00 21.17 ? 531  TYR A O     1 
ATOM   8438 C CB    . TYR B 1 533 ? 39.407 -8.014  -46.399 1.00 20.22 ? 531  TYR A CB    1 
ATOM   8439 C CG    . TYR B 1 533 ? 38.142 -7.215  -46.594 1.00 21.34 ? 531  TYR A CG    1 
ATOM   8440 C CD1   . TYR B 1 533 ? 37.477 -7.170  -47.807 1.00 22.41 ? 531  TYR A CD1   1 
ATOM   8441 C CD2   . TYR B 1 533 ? 37.564 -6.529  -45.534 1.00 21.62 ? 531  TYR A CD2   1 
ATOM   8442 C CE1   . TYR B 1 533 ? 36.301 -6.448  -47.969 1.00 23.54 ? 531  TYR A CE1   1 
ATOM   8443 C CE2   . TYR B 1 533 ? 36.370 -5.834  -45.675 1.00 24.51 ? 531  TYR A CE2   1 
ATOM   8444 C CZ    . TYR B 1 533 ? 35.722 -5.790  -46.898 1.00 23.11 ? 531  TYR A CZ    1 
ATOM   8445 O OH    . TYR B 1 533 ? 34.551 -5.078  -47.057 1.00 22.80 ? 531  TYR A OH    1 
ATOM   8446 N N     . ALA B 1 534 ? 42.169 -9.702  -47.022 1.00 18.92 ? 532  ALA A N     1 
ATOM   8447 C CA    . ALA B 1 534 ? 43.575 -10.049 -46.727 1.00 20.50 ? 532  ALA A CA    1 
ATOM   8448 C C     . ALA B 1 534 ? 44.419 -9.596  -47.916 1.00 23.42 ? 532  ALA A C     1 
ATOM   8449 O O     . ALA B 1 534 ? 45.522 -9.058  -47.700 1.00 24.73 ? 532  ALA A O     1 
ATOM   8450 C CB    . ALA B 1 534 ? 43.720 -11.526 -46.439 1.00 21.15 ? 532  ALA A CB    1 
ATOM   8451 N N     . TYR B 1 535 ? 43.899 -9.757  -49.141 1.00 23.54 ? 533  TYR A N     1 
ATOM   8452 C CA    . TYR B 1 535 ? 44.631 -9.380  -50.367 1.00 22.60 ? 533  TYR A CA    1 
ATOM   8453 C C     . TYR B 1 535 ? 44.720 -7.850  -50.387 1.00 22.22 ? 533  TYR A C     1 
ATOM   8454 O O     . TYR B 1 535 ? 45.824 -7.336  -50.581 1.00 21.65 ? 533  TYR A O     1 
ATOM   8455 C CB    . TYR B 1 535 ? 43.993 -10.003 -51.608 1.00 22.85 ? 533  TYR A CB    1 
ATOM   8456 C CG    . TYR B 1 535 ? 44.570 -9.540  -52.927 1.00 23.48 ? 533  TYR A CG    1 
ATOM   8457 C CD1   . TYR B 1 535 ? 45.947 -9.437  -53.126 1.00 25.79 ? 533  TYR A CD1   1 
ATOM   8458 C CD2   . TYR B 1 535 ? 43.752 -9.272  -54.008 1.00 23.11 ? 533  TYR A CD2   1 
ATOM   8459 C CE1   . TYR B 1 535 ? 46.464 -9.057  -54.359 1.00 25.66 ? 533  TYR A CE1   1 
ATOM   8460 C CE2   . TYR B 1 535 ? 44.253 -8.890  -55.245 1.00 22.65 ? 533  TYR A CE2   1 
ATOM   8461 C CZ    . TYR B 1 535 ? 45.624 -8.758  -55.412 1.00 25.43 ? 533  TYR A CZ    1 
ATOM   8462 O OH    . TYR B 1 535 ? 46.153 -8.403  -56.629 1.00 25.33 ? 533  TYR A OH    1 
ATOM   8463 N N     . MET B 1 536 ? 43.596 -7.162  -50.150 1.00 22.45 ? 534  MET A N     1 
ATOM   8464 C CA    . MET B 1 536 ? 43.529 -5.676  -50.087 1.00 20.94 ? 534  MET A CA    1 
ATOM   8465 C C     . MET B 1 536 ? 44.531 -5.157  -49.042 1.00 21.45 ? 534  MET A C     1 
ATOM   8466 O O     . MET B 1 536 ? 45.244 -4.136  -49.326 1.00 22.54 ? 534  MET A O     1 
ATOM   8467 C CB    . MET B 1 536 ? 42.115 -5.180  -49.742 1.00 22.68 ? 534  MET A CB    1 
ATOM   8468 C CG    . MET B 1 536 ? 41.040 -5.453  -50.806 1.00 21.63 ? 534  MET A CG    1 
ATOM   8469 S SD    . MET B 1 536 ? 41.450 -4.919  -52.511 1.00 23.81 ? 534  MET A SD    1 
ATOM   8470 C CE    . MET B 1 536 ? 42.056 -6.458  -53.207 1.00 23.47 ? 534  MET A CE    1 
ATOM   8471 N N     . TRP B 1 537 ? 44.553 -5.768  -47.858 1.00 21.34 ? 535  TRP A N     1 
ATOM   8472 C CA    . TRP B 1 537 ? 45.405 -5.331  -46.718 1.00 21.88 ? 535  TRP A CA    1 
ATOM   8473 C C     . TRP B 1 537 ? 46.878 -5.598  -47.052 1.00 21.74 ? 535  TRP A C     1 
ATOM   8474 O O     . TRP B 1 537 ? 47.720 -4.796  -46.651 1.00 23.10 ? 535  TRP A O     1 
ATOM   8475 C CB    . TRP B 1 537 ? 44.954 -5.967  -45.386 1.00 22.02 ? 535  TRP A CB    1 
ATOM   8476 C CG    . TRP B 1 537 ? 43.931 -5.113  -44.714 1.00 21.50 ? 535  TRP A CG    1 
ATOM   8477 C CD1   . TRP B 1 537 ? 42.601 -5.358  -44.493 1.00 22.15 ? 535  TRP A CD1   1 
ATOM   8478 C CD2   . TRP B 1 537 ? 44.159 -3.764  -44.293 1.00 21.48 ? 535  TRP A CD2   1 
ATOM   8479 N NE1   . TRP B 1 537 ? 42.011 -4.264  -43.914 1.00 21.47 ? 535  TRP A NE1   1 
ATOM   8480 C CE2   . TRP B 1 537 ? 42.939 -3.270  -43.786 1.00 22.08 ? 535  TRP A CE2   1 
ATOM   8481 C CE3   . TRP B 1 537 ? 45.292 -2.955  -44.248 1.00 22.50 ? 535  TRP A CE3   1 
ATOM   8482 C CZ2   . TRP B 1 537 ? 42.834 -1.990  -43.261 1.00 22.19 ? 535  TRP A CZ2   1 
ATOM   8483 C CZ3   . TRP B 1 537 ? 45.168 -1.673  -43.773 1.00 23.38 ? 535  TRP A CZ3   1 
ATOM   8484 C CH2   . TRP B 1 537 ? 43.966 -1.215  -43.259 1.00 22.32 ? 535  TRP A CH2   1 
ATOM   8485 N N     . ALA B 1 538 ? 47.189 -6.713  -47.713 1.00 22.07 ? 536  ALA A N     1 
ATOM   8486 C CA    . ALA B 1 538 ? 48.582 -7.010  -48.118 1.00 23.62 ? 536  ALA A CA    1 
ATOM   8487 C C     . ALA B 1 538 ? 49.014 -5.971  -49.160 1.00 24.99 ? 536  ALA A C     1 
ATOM   8488 O O     . ALA B 1 538 ? 50.162 -5.479  -49.051 1.00 24.29 ? 536  ALA A O     1 
ATOM   8489 C CB    . ALA B 1 538 ? 48.704 -8.417  -48.612 1.00 24.93 ? 536  ALA A CB    1 
ATOM   8490 N N     . LEU B 1 539 ? 48.125 -5.603  -50.094 1.00 23.09 ? 537  LEU A N     1 
ATOM   8491 C CA    . LEU B 1 539 ? 48.447 -4.579  -51.119 1.00 24.00 ? 537  LEU A CA    1 
ATOM   8492 C C     . LEU B 1 539 ? 48.707 -3.241  -50.430 1.00 23.26 ? 537  LEU A C     1 
ATOM   8493 O O     . LEU B 1 539 ? 49.645 -2.528  -50.832 1.00 24.50 ? 537  LEU A O     1 
ATOM   8494 C CB    . LEU B 1 539 ? 47.316 -4.428  -52.128 1.00 23.80 ? 537  LEU A CB    1 
ATOM   8495 C CG    . LEU B 1 539 ? 47.204 -5.521  -53.179 1.00 24.82 ? 537  LEU A CG    1 
ATOM   8496 C CD1   . LEU B 1 539 ? 45.842 -5.445  -53.816 1.00 24.35 ? 537  LEU A CD1   1 
ATOM   8497 C CD2   . LEU B 1 539 ? 48.303 -5.381  -54.242 1.00 25.19 ? 537  LEU A CD2   1 
ATOM   8498 N N     . MET B 1 540 ? 47.921 -2.893  -49.422 1.00 21.80 ? 538  MET A N     1 
ATOM   8499 C CA    . MET B 1 540 ? 48.113 -1.584  -48.754 1.00 20.90 ? 538  MET A CA    1 
ATOM   8500 C C     . MET B 1 540 ? 49.360 -1.675  -47.878 1.00 21.67 ? 538  MET A C     1 
ATOM   8501 O O     . MET B 1 540 ? 50.054 -0.670  -47.789 1.00 22.20 ? 538  MET A O     1 
ATOM   8502 C CB    . MET B 1 540 ? 46.879 -1.165  -47.955 1.00 20.90 ? 538  MET A CB    1 
ATOM   8503 C CG    . MET B 1 540 ? 45.695 -0.930  -48.863 1.00 22.33 ? 538  MET A CG    1 
ATOM   8504 S SD    . MET B 1 540 ? 44.289 -0.094  -48.073 1.00 22.68 ? 538  MET A SD    1 
ATOM   8505 C CE    . MET B 1 540 ? 43.580 -1.478  -47.187 1.00 24.06 ? 538  MET A CE    1 
ATOM   8506 N N     . ALA B 1 541 ? 49.671 -2.853  -47.316 1.00 22.93 ? 539  ALA A N     1 
ATOM   8507 C CA    . ALA B 1 541 ? 50.861 -3.038  -46.446 1.00 24.49 ? 539  ALA A CA    1 
ATOM   8508 C C     . ALA B 1 541 ? 52.123 -2.881  -47.298 1.00 23.67 ? 539  ALA A C     1 
ATOM   8509 O O     . ALA B 1 541 ? 53.133 -2.365  -46.798 1.00 24.51 ? 539  ALA A O     1 
ATOM   8510 C CB    . ALA B 1 541 ? 50.862 -4.382  -45.765 1.00 24.39 ? 539  ALA A CB    1 
ATOM   8511 N N     . ARG B 1 542 ? 52.067 -3.341  -48.537 1.00 25.57 ? 540  ARG A N     1 
ATOM   8512 C CA    . ARG B 1 542 ? 53.240 -3.269  -49.446 1.00 26.12 ? 540  ARG A CA    1 
ATOM   8513 C C     . ARG B 1 542 ? 53.589 -1.794  -49.644 1.00 25.63 ? 540  ARG A C     1 
ATOM   8514 O O     . ARG B 1 542 ? 54.752 -1.441  -49.452 1.00 25.68 ? 540  ARG A O     1 
ATOM   8515 C CB    . ARG B 1 542 ? 52.976 -3.943  -50.793 1.00 27.45 ? 540  ARG A CB    1 
ATOM   8516 C CG    . ARG B 1 542 ? 54.162 -3.801  -51.745 1.00 26.68 ? 540  ARG A CG    1 
ATOM   8517 C CD    . ARG B 1 542 ? 54.012 -4.586  -53.029 1.00 28.40 ? 540  ARG A CD    1 
ATOM   8518 N NE    . ARG B 1 542 ? 52.842 -4.235  -53.822 1.00 26.42 ? 540  ARG A NE    1 
ATOM   8519 C CZ    . ARG B 1 542 ? 52.538 -4.803  -54.987 1.00 29.74 ? 540  ARG A CZ    1 
ATOM   8520 N NH1   . ARG B 1 542 ? 51.440 -4.451  -55.632 1.00 29.99 ? 540  ARG A NH1   1 
ATOM   8521 N NH2   . ARG B 1 542 ? 53.290 -5.777  -55.473 1.00 28.24 ? 540  ARG A NH2   1 
ATOM   8522 N N     . THR B 1 543 ? 52.605 -0.958  -49.957 1.00 24.15 ? 541  THR A N     1 
ATOM   8523 C CA    . THR B 1 543 ? 52.832 0.488   -50.189 1.00 25.25 ? 541  THR A CA    1 
ATOM   8524 C C     . THR B 1 543 ? 53.322 1.171   -48.906 1.00 27.24 ? 541  THR A C     1 
ATOM   8525 O O     . THR B 1 543 ? 54.284 1.989   -48.954 1.00 26.95 ? 541  THR A O     1 
ATOM   8526 C CB    . THR B 1 543 ? 51.568 1.156   -50.718 1.00 26.45 ? 541  THR A CB    1 
ATOM   8527 O OG1   . THR B 1 543 ? 51.056 0.350   -51.781 1.00 24.69 ? 541  THR A OG1   1 
ATOM   8528 C CG2   . THR B 1 543 ? 51.817 2.574   -51.183 1.00 27.51 ? 541  THR A CG2   1 
ATOM   8529 N N     . ALA B 1 544 ? 52.667 0.882   -47.786 1.00 27.81 ? 542  ALA A N     1 
ATOM   8530 C CA    . ALA B 1 544 ? 52.997 1.488   -46.482 1.00 26.14 ? 542  ALA A CA    1 
ATOM   8531 C C     . ALA B 1 544 ? 54.422 1.109   -46.061 1.00 25.76 ? 542  ALA A C     1 
ATOM   8532 O O     . ALA B 1 544 ? 55.100 1.991   -45.524 1.00 28.80 ? 542  ALA A O     1 
ATOM   8533 C CB    . ALA B 1 544 ? 51.981 1.079   -45.459 1.00 26.14 ? 542  ALA A CB    1 
ATOM   8534 N N     . LEU B 1 545 ? 54.841 -0.147  -46.264 1.00 25.02 ? 543  LEU A N     1 
ATOM   8535 C CA    . LEU B 1 545 ? 56.226 -0.614  -45.979 1.00 26.17 ? 543  LEU A CA    1 
ATOM   8536 C C     . LEU B 1 545 ? 57.233 0.186   -46.792 1.00 24.95 ? 543  LEU A C     1 
ATOM   8537 O O     . LEU B 1 545 ? 58.290 0.535   -46.240 1.00 25.68 ? 543  LEU A O     1 
ATOM   8538 C CB    . LEU B 1 545 ? 56.380 -2.108  -46.270 1.00 26.71 ? 543  LEU A CB    1 
ATOM   8539 C CG    . LEU B 1 545 ? 55.774 -3.022  -45.209 1.00 26.32 ? 543  LEU A CG    1 
ATOM   8540 C CD1   . LEU B 1 545 ? 55.653 -4.454  -45.692 1.00 25.16 ? 543  LEU A CD1   1 
ATOM   8541 C CD2   . LEU B 1 545 ? 56.592 -2.950  -43.945 1.00 27.82 ? 543  LEU A CD2   1 
ATOM   8542 N N     . ALA B 1 546 ? 56.941 0.418   -48.061 1.00 24.82 ? 544  ALA A N     1 
ATOM   8543 C CA    . ALA B 1 546 ? 57.803 1.195   -48.967 1.00 25.72 ? 544  ALA A CA    1 
ATOM   8544 C C     . ALA B 1 546 ? 57.921 2.647   -48.486 1.00 25.67 ? 544  ALA A C     1 
ATOM   8545 O O     . ALA B 1 546 ? 58.980 3.233   -48.715 1.00 25.71 ? 544  ALA A O     1 
ATOM   8546 C CB    . ALA B 1 546 ? 57.270 1.118   -50.381 1.00 26.61 ? 544  ALA A CB    1 
ATOM   8547 N N     . LYS B 1 547 ? 56.879 3.219   -47.874 1.00 26.52 ? 545  LYS A N     1 
ATOM   8548 C CA    . LYS B 1 547 ? 56.827 4.671   -47.555 1.00 27.00 ? 545  LYS A CA    1 
ATOM   8549 C C     . LYS B 1 547 ? 56.942 4.909   -46.049 1.00 29.17 ? 545  LYS A C     1 
ATOM   8550 O O     . LYS B 1 547 ? 56.771 6.056   -45.613 1.00 29.74 ? 545  LYS A O     1 
ATOM   8551 C CB    . LYS B 1 547 ? 55.540 5.260   -48.108 1.00 27.42 ? 545  LYS A CB    1 
ATOM   8552 C CG    . LYS B 1 547 ? 55.485 5.209   -49.628 1.00 28.61 ? 545  LYS A CG    1 
ATOM   8553 C CD    . LYS B 1 547 ? 54.338 5.985   -50.222 1.00 29.44 ? 545  LYS A CD    1 
ATOM   8554 C CE    . LYS B 1 547 ? 54.369 5.933   -51.730 1.00 29.47 ? 545  LYS A CE    1 
ATOM   8555 N NZ    . LYS B 1 547 ? 53.539 7.012   -52.305 1.00 33.53 ? 545  LYS A NZ    1 
ATOM   8556 N N     . GLN B 1 548 ? 57.237 3.864   -45.287 1.00 30.15 ? 546  GLN A N     1 
ATOM   8557 C CA    . GLN B 1 548 ? 57.302 3.932   -43.811 1.00 33.07 ? 546  GLN A CA    1 
ATOM   8558 C C     . GLN B 1 548 ? 58.370 4.958   -43.420 1.00 36.57 ? 546  GLN A C     1 
ATOM   8559 O O     . GLN B 1 548 ? 59.476 4.954   -44.024 1.00 29.52 ? 546  GLN A O     1 
ATOM   8560 C CB    . GLN B 1 548 ? 57.590 2.543   -43.241 1.00 35.80 ? 546  GLN A CB    1 
ATOM   8561 C CG    . GLN B 1 548 ? 57.738 2.534   -41.730 1.00 42.68 ? 546  GLN A CG    1 
ATOM   8562 C CD    . GLN B 1 548 ? 57.279 1.244   -41.089 1.00 46.04 ? 546  GLN A CD    1 
ATOM   8563 O OE1   . GLN B 1 548 ? 57.778 0.146   -41.387 1.00 43.85 ? 546  GLN A OE1   1 
ATOM   8564 N NE2   . GLN B 1 548 ? 56.311 1.379   -40.193 1.00 48.68 ? 546  GLN A NE2   1 
ATOM   8565 N N     . GLY B 1 549 ? 58.035 5.817   -42.457 1.00 36.06 ? 547  GLY A N     1 
ATOM   8566 C CA    . GLY B 1 549 ? 58.948 6.850   -41.949 1.00 41.50 ? 547  GLY A CA    1 
ATOM   8567 C C     . GLY B 1 549 ? 58.754 8.138   -42.708 1.00 43.73 ? 547  GLY A C     1 
ATOM   8568 O O     . GLY B 1 549 ? 59.176 9.183   -42.192 1.00 46.54 ? 547  GLY A O     1 
ATOM   8569 N N     . GLU B 1 550 ? 58.070 8.083   -43.855 1.00 44.67 ? 548  GLU A N     1 
ATOM   8570 C CA    . GLU B 1 550 ? 57.827 9.283   -44.707 1.00 46.44 ? 548  GLU A CA    1 
ATOM   8571 C C     . GLU B 1 550 ? 56.663 10.107  -44.142 1.00 45.19 ? 548  GLU A C     1 
ATOM   8572 O O     . GLU B 1 550 ? 56.588 11.310  -44.451 1.00 51.56 ? 548  GLU A O     1 
ATOM   8573 C CB    . GLU B 1 550 ? 57.663 8.878   -46.176 1.00 48.34 ? 548  GLU A CB    1 
ATOM   8574 C CG    . GLU B 1 550 ? 58.911 8.149   -46.671 1.00 52.08 ? 548  GLU A CG    1 
ATOM   8575 C CD    . GLU B 1 550 ? 58.933 7.640   -48.104 1.00 50.36 ? 548  GLU A CD    1 
ATOM   8576 O OE1   . GLU B 1 550 ? 57.857 7.714   -48.782 1.00 43.41 ? 548  GLU A OE1   1 
ATOM   8577 O OE2   . GLU B 1 550 ? 60.035 7.174   -48.526 1.00 36.41 ? 548  GLU A OE2   1 
ATOM   8578 N N     . ASP B 1 551 ? 55.851 9.549   -43.246 1.00 41.63 ? 549  ASP A N     1 
ATOM   8579 C CA    . ASP B 1 551 ? 54.559 10.180  -42.871 1.00 37.20 ? 549  ASP A CA    1 
ATOM   8580 C C     . ASP B 1 551 ? 53.872 9.207   -41.918 1.00 34.08 ? 549  ASP A C     1 
ATOM   8581 O O     . ASP B 1 551 ? 53.960 7.979   -42.140 1.00 31.61 ? 549  ASP A O     1 
ATOM   8582 C CB    . ASP B 1 551 ? 53.818 10.525  -44.176 1.00 40.41 ? 549  ASP A CB    1 
ATOM   8583 C CG    . ASP B 1 551 ? 52.378 10.995  -44.113 1.00 41.87 ? 549  ASP A CG    1 
ATOM   8584 O OD1   . ASP B 1 551 ? 51.845 11.126  -43.012 1.00 37.14 ? 549  ASP A OD1   1 
ATOM   8585 O OD2   . ASP B 1 551 ? 51.798 11.206  -45.213 1.00 52.13 ? 549  ASP A OD2   1 
ATOM   8586 N N     . ASP B 1 552 ? 53.296 9.729   -40.848 1.00 34.69 ? 550  ASP A N     1 
ATOM   8587 C CA    . ASP B 1 552 ? 52.594 8.934   -39.806 1.00 36.66 ? 550  ASP A CA    1 
ATOM   8588 C C     . ASP B 1 552 ? 51.448 8.111   -40.428 1.00 32.53 ? 550  ASP A C     1 
ATOM   8589 O O     . ASP B 1 552 ? 51.107 7.069   -39.878 1.00 29.46 ? 550  ASP A O     1 
ATOM   8590 C CB    . ASP B 1 552 ? 52.030 9.864   -38.733 1.00 44.29 ? 550  ASP A CB    1 
ATOM   8591 C CG    . ASP B 1 552 ? 51.979 9.227   -37.363 1.00 48.12 ? 550  ASP A CG    1 
ATOM   8592 O OD1   . ASP B 1 552 ? 52.858 8.388   -37.094 1.00 53.34 ? 550  ASP A OD1   1 
ATOM   8593 O OD2   . ASP B 1 552 ? 51.076 9.592   -36.582 1.00 57.46 ? 550  ASP A OD2   1 
ATOM   8594 N N     . PHE B 1 553 ? 50.871 8.574   -41.538 1.00 28.94 ? 551  PHE A N     1 
ATOM   8595 C CA    . PHE B 1 553 ? 49.790 7.868   -42.272 1.00 28.23 ? 551  PHE A CA    1 
ATOM   8596 C C     . PHE B 1 553 ? 50.186 6.401   -42.507 1.00 26.57 ? 551  PHE A C     1 
ATOM   8597 O O     . PHE B 1 553 ? 49.358 5.490   -42.288 1.00 24.39 ? 551  PHE A O     1 
ATOM   8598 C CB    . PHE B 1 553 ? 49.476 8.595   -43.575 1.00 28.54 ? 551  PHE A CB    1 
ATOM   8599 C CG    . PHE B 1 553 ? 48.392 7.904   -44.350 1.00 29.44 ? 551  PHE A CG    1 
ATOM   8600 C CD1   . PHE B 1 553 ? 48.692 6.824   -45.169 1.00 26.92 ? 551  PHE A CD1   1 
ATOM   8601 C CD2   . PHE B 1 553 ? 47.062 8.256   -44.165 1.00 29.06 ? 551  PHE A CD2   1 
ATOM   8602 C CE1   . PHE B 1 553 ? 47.687 6.138   -45.825 1.00 27.28 ? 551  PHE A CE1   1 
ATOM   8603 C CE2   . PHE B 1 553 ? 46.061 7.580   -44.842 1.00 28.34 ? 551  PHE A CE2   1 
ATOM   8604 C CZ    . PHE B 1 553 ? 46.377 6.530   -45.672 1.00 28.31 ? 551  PHE A CZ    1 
ATOM   8605 N N     . TYR B 1 554 ? 51.439 6.144   -42.893 1.00 24.12 ? 552  TYR A N     1 
ATOM   8606 C CA    . TYR B 1 554 ? 51.891 4.777   -43.263 1.00 24.95 ? 552  TYR A CA    1 
ATOM   8607 C C     . TYR B 1 554 ? 52.022 3.909   -42.017 1.00 25.18 ? 552  TYR A C     1 
ATOM   8608 O O     . TYR B 1 554 ? 51.696 2.719   -42.102 1.00 23.85 ? 552  TYR A O     1 
ATOM   8609 C CB    . TYR B 1 554 ? 53.167 4.833   -44.109 1.00 24.81 ? 552  TYR A CB    1 
ATOM   8610 C CG    . TYR B 1 554 ? 52.953 5.692   -45.322 1.00 24.43 ? 552  TYR A CG    1 
ATOM   8611 C CD1   . TYR B 1 554 ? 52.109 5.265   -46.333 1.00 25.72 ? 552  TYR A CD1   1 
ATOM   8612 C CD2   . TYR B 1 554 ? 53.474 6.977   -45.408 1.00 27.12 ? 552  TYR A CD2   1 
ATOM   8613 C CE1   . TYR B 1 554 ? 51.810 6.071   -47.413 1.00 26.07 ? 552  TYR A CE1   1 
ATOM   8614 C CE2   . TYR B 1 554 ? 53.212 7.788   -46.501 1.00 26.96 ? 552  TYR A CE2   1 
ATOM   8615 C CZ    . TYR B 1 554 ? 52.370 7.333   -47.500 1.00 25.78 ? 552  TYR A CZ    1 
ATOM   8616 O OH    . TYR B 1 554 ? 52.058 8.099   -48.567 1.00 24.06 ? 552  TYR A OH    1 
ATOM   8617 N N     . ALA B 1 555 ? 52.445 4.472   -40.881 1.00 28.45 ? 553  ALA A N     1 
ATOM   8618 C CA    . ALA B 1 555 ? 52.501 3.709   -39.607 1.00 30.36 ? 553  ALA A CA    1 
ATOM   8619 C C     . ALA B 1 555 ? 51.073 3.291   -39.191 1.00 27.10 ? 553  ALA A C     1 
ATOM   8620 O O     . ALA B 1 555 ? 50.883 2.118   -38.803 1.00 28.83 ? 553  ALA A O     1 
ATOM   8621 C CB    . ALA B 1 555 ? 53.207 4.497   -38.535 1.00 31.43 ? 553  ALA A CB    1 
ATOM   8622 N N     . SER B 1 556 ? 50.118 4.213   -39.258 1.00 26.85 ? 554  SER A N     1 
ATOM   8623 C CA    . SER B 1 556 ? 48.674 3.969   -38.993 1.00 27.64 ? 554  SER A CA    1 
ATOM   8624 C C     . SER B 1 556 ? 48.194 2.830   -39.894 1.00 24.91 ? 554  SER A C     1 
ATOM   8625 O O     . SER B 1 556 ? 47.603 1.850   -39.382 1.00 24.29 ? 554  SER A O     1 
ATOM   8626 C CB    . SER B 1 556 ? 47.847 5.211   -39.208 1.00 28.24 ? 554  SER A CB    1 
ATOM   8627 O OG    . SER B 1 556 ? 48.191 6.213   -38.285 1.00 31.70 ? 554  SER A OG    1 
ATOM   8628 N N     . LYS B 1 557 ? 48.517 2.901   -41.183 1.00 23.38 ? 555  LYS A N     1 
ATOM   8629 C CA    . LYS B 1 557 ? 48.054 1.867   -42.144 1.00 23.77 ? 555  LYS A CA    1 
ATOM   8630 C C     . LYS B 1 557 ? 48.582 0.489   -41.734 1.00 23.57 ? 555  LYS A C     1 
ATOM   8631 O O     . LYS B 1 557 ? 47.807 -0.466  -41.755 1.00 22.99 ? 555  LYS A O     1 
ATOM   8632 C CB    . LYS B 1 557 ? 48.467 2.258   -43.569 1.00 22.93 ? 555  LYS A CB    1 
ATOM   8633 C CG    . LYS B 1 557 ? 47.875 1.411   -44.685 1.00 24.93 ? 555  LYS A CG    1 
ATOM   8634 C CD    . LYS B 1 557 ? 46.366 1.441   -44.729 1.00 23.66 ? 555  LYS A CD    1 
ATOM   8635 C CE    . LYS B 1 557 ? 45.801 2.801   -45.075 1.00 24.60 ? 555  LYS A CE    1 
ATOM   8636 N NZ    . LYS B 1 557 ? 44.377 2.712   -45.469 1.00 25.49 ? 555  LYS A NZ    1 
ATOM   8637 N N     . LEU B 1 558 ? 49.856 0.411   -41.355 1.00 25.25 ? 556  LEU A N     1 
ATOM   8638 C CA    . LEU B 1 558 ? 50.471 -0.903  -41.025 1.00 24.48 ? 556  LEU A CA    1 
ATOM   8639 C C     . LEU B 1 558 ? 49.923 -1.463  -39.705 1.00 22.10 ? 556  LEU A C     1 
ATOM   8640 O O     . LEU B 1 558 ? 49.751 -2.675  -39.617 1.00 23.27 ? 556  LEU A O     1 
ATOM   8641 C CB    . LEU B 1 558 ? 51.990 -0.741  -40.982 1.00 25.53 ? 556  LEU A CB    1 
ATOM   8642 C CG    . LEU B 1 558 ? 52.664 -0.696  -42.350 1.00 31.03 ? 556  LEU A CG    1 
ATOM   8643 C CD1   . LEU B 1 558 ? 54.075 -0.143  -42.246 1.00 32.90 ? 556  LEU A CD1   1 
ATOM   8644 C CD2   . LEU B 1 558 ? 52.671 -2.076  -42.989 1.00 30.81 ? 556  LEU A CD2   1 
ATOM   8645 N N     . GLY B 1 559 ? 49.700 -0.611  -38.715 1.00 23.73 ? 557  GLY A N     1 
ATOM   8646 C CA    . GLY B 1 559 ? 49.076 -1.093  -37.471 1.00 23.18 ? 557  GLY A CA    1 
ATOM   8647 C C     . GLY B 1 559 ? 47.681 -1.631  -37.738 1.00 23.13 ? 557  GLY A C     1 
ATOM   8648 O O     . GLY B 1 559 ? 47.326 -2.667  -37.184 1.00 24.96 ? 557  GLY A O     1 
ATOM   8649 N N     . THR B 1 560 ? 46.937 -0.949  -38.601 1.00 24.67 ? 558  THR A N     1 
ATOM   8650 C CA    . THR B 1 560 ? 45.558 -1.383  -38.931 1.00 23.37 ? 558  THR A CA    1 
ATOM   8651 C C     . THR B 1 560 ? 45.647 -2.734  -39.652 1.00 23.44 ? 558  THR A C     1 
ATOM   8652 O O     . THR B 1 560 ? 44.916 -3.638  -39.286 1.00 24.08 ? 558  THR A O     1 
ATOM   8653 C CB    . THR B 1 560 ? 44.824 -0.243  -39.650 1.00 23.30 ? 558  THR A CB    1 
ATOM   8654 O OG1   . THR B 1 560 ? 45.057 0.986   -38.966 1.00 20.61 ? 558  THR A OG1   1 
ATOM   8655 C CG2   . THR B 1 560 ? 43.338 -0.495  -39.774 1.00 23.58 ? 558  THR A CG2   1 
ATOM   8656 N N     . ALA B 1 561 ? 46.573 -2.861  -40.602 1.00 25.59 ? 559  ALA A N     1 
ATOM   8657 C CA    . ALA B 1 561 ? 46.795 -4.140  -41.317 1.00 22.96 ? 559  ALA A CA    1 
ATOM   8658 C C     . ALA B 1 561 ? 47.094 -5.266  -40.330 1.00 24.17 ? 559  ALA A C     1 
ATOM   8659 O O     . ALA B 1 561 ? 46.568 -6.365  -40.487 1.00 20.66 ? 559  ALA A O     1 
ATOM   8660 C CB    . ALA B 1 561 ? 47.959 -3.984  -42.258 1.00 24.15 ? 559  ALA A CB    1 
ATOM   8661 N N     . ARG B 1 562 ? 47.954 -4.978  -39.359 1.00 24.42 ? 560  ARG A N     1 
ATOM   8662 C CA    . ARG B 1 562 ? 48.384 -6.033  -38.412 1.00 23.18 ? 560  ARG A CA    1 
ATOM   8663 C C     . ARG B 1 562 ? 47.183 -6.487  -37.570 1.00 21.70 ? 560  ARG A C     1 
ATOM   8664 O O     . ARG B 1 562 ? 47.065 -7.673  -37.302 1.00 21.52 ? 560  ARG A O     1 
ATOM   8665 C CB    . ARG B 1 562 ? 49.568 -5.487  -37.615 1.00 22.68 ? 560  ARG A CB    1 
ATOM   8666 C CG    . ARG B 1 562 ? 50.850 -5.409  -38.432 1.00 23.34 ? 560  ARG A CG    1 
ATOM   8667 C CD    . ARG B 1 562 ? 52.057 -4.820  -37.732 1.00 24.40 ? 560  ARG A CD    1 
ATOM   8668 N NE    . ARG B 1 562 ? 53.244 -4.994  -38.555 1.00 25.01 ? 560  ARG A NE    1 
ATOM   8669 C CZ    . ARG B 1 562 ? 54.106 -4.036  -38.869 1.00 29.16 ? 560  ARG A CZ    1 
ATOM   8670 N NH1   . ARG B 1 562 ? 53.934 -2.805  -38.420 1.00 27.72 ? 560  ARG A NH1   1 
ATOM   8671 N NH2   . ARG B 1 562 ? 55.144 -4.315  -39.634 1.00 29.88 ? 560  ARG A NH2   1 
ATOM   8672 N N     . PHE B 1 563 ? 46.317 -5.551  -37.209 1.00 22.14 ? 561  PHE A N     1 
ATOM   8673 C CA    . PHE B 1 563 ? 45.088 -5.942  -36.472 1.00 23.26 ? 561  PHE A CA    1 
ATOM   8674 C C     . PHE B 1 563 ? 44.239 -6.853  -37.359 1.00 22.59 ? 561  PHE A C     1 
ATOM   8675 O O     . PHE B 1 563 ? 43.766 -7.879  -36.884 1.00 23.62 ? 561  PHE A O     1 
ATOM   8676 C CB    . PHE B 1 563 ? 44.259 -4.728  -36.051 1.00 24.29 ? 561  PHE A CB    1 
ATOM   8677 C CG    . PHE B 1 563 ? 42.980 -5.102  -35.348 1.00 22.93 ? 561  PHE A CG    1 
ATOM   8678 C CD1   . PHE B 1 563 ? 42.969 -5.358  -33.987 1.00 23.09 ? 561  PHE A CD1   1 
ATOM   8679 C CD2   . PHE B 1 563 ? 41.793 -5.227  -36.050 1.00 24.96 ? 561  PHE A CD2   1 
ATOM   8680 C CE1   . PHE B 1 563 ? 41.796 -5.714  -33.342 1.00 23.36 ? 561  PHE A CE1   1 
ATOM   8681 C CE2   . PHE B 1 563 ? 40.621 -5.581  -35.404 1.00 22.70 ? 561  PHE A CE2   1 
ATOM   8682 C CZ    . PHE B 1 563 ? 40.625 -5.825  -34.052 1.00 24.50 ? 561  PHE A CZ    1 
ATOM   8683 N N     . TYR B 1 564 ? 44.077 -6.461  -38.620 1.00 22.66 ? 562  TYR A N     1 
ATOM   8684 C CA    . TYR B 1 564 ? 43.215 -7.254  -39.530 1.00 19.60 ? 562  TYR A CA    1 
ATOM   8685 C C     . TYR B 1 564 ? 43.710 -8.696  -39.564 1.00 21.35 ? 562  TYR A C     1 
ATOM   8686 O O     . TYR B 1 564 ? 42.906 -9.603  -39.379 1.00 23.45 ? 562  TYR A O     1 
ATOM   8687 C CB    . TYR B 1 564 ? 43.193 -6.727  -40.964 1.00 21.02 ? 562  TYR A CB    1 
ATOM   8688 C CG    . TYR B 1 564 ? 42.322 -7.601  -41.826 1.00 20.45 ? 562  TYR A CG    1 
ATOM   8689 C CD1   . TYR B 1 564 ? 40.946 -7.481  -41.782 1.00 20.51 ? 562  TYR A CD1   1 
ATOM   8690 C CD2   . TYR B 1 564 ? 42.862 -8.614  -42.599 1.00 21.66 ? 562  TYR A CD2   1 
ATOM   8691 C CE1   . TYR B 1 564 ? 40.126 -8.310  -42.524 1.00 21.12 ? 562  TYR A CE1   1 
ATOM   8692 C CE2   . TYR B 1 564 ? 42.056 -9.456  -43.346 1.00 22.22 ? 562  TYR A CE2   1 
ATOM   8693 C CZ    . TYR B 1 564 ? 40.683 -9.303  -43.306 1.00 21.93 ? 562  TYR A CZ    1 
ATOM   8694 O OH    . TYR B 1 564 ? 39.876 -10.121 -44.033 1.00 21.76 ? 562  TYR A OH    1 
ATOM   8695 N N     . PHE B 1 565 ? 45.005 -8.871  -39.793 1.00 20.72 ? 563  PHE A N     1 
ATOM   8696 C CA    . PHE B 1 565 ? 45.549 -10.243 -39.941 1.00 21.73 ? 563  PHE A CA    1 
ATOM   8697 C C     . PHE B 1 565 ? 45.518 -10.991 -38.604 1.00 22.56 ? 563  PHE A C     1 
ATOM   8698 O O     . PHE B 1 565 ? 45.333 -12.200 -38.611 1.00 22.33 ? 563  PHE A O     1 
ATOM   8699 C CB    . PHE B 1 565 ? 46.956 -10.182 -40.542 1.00 22.00 ? 563  PHE A CB    1 
ATOM   8700 C CG    . PHE B 1 565 ? 46.988 -10.110 -42.047 1.00 21.26 ? 563  PHE A CG    1 
ATOM   8701 C CD1   . PHE B 1 565 ? 46.908 -8.893  -42.701 1.00 21.35 ? 563  PHE A CD1   1 
ATOM   8702 C CD2   . PHE B 1 565 ? 47.090 -11.262 -42.808 1.00 23.36 ? 563  PHE A CD2   1 
ATOM   8703 C CE1   . PHE B 1 565 ? 46.932 -8.834  -44.085 1.00 22.63 ? 563  PHE A CE1   1 
ATOM   8704 C CE2   . PHE B 1 565 ? 47.114 -11.201 -44.191 1.00 23.79 ? 563  PHE A CE2   1 
ATOM   8705 C CZ    . PHE B 1 565 ? 47.034 -9.986  -44.826 1.00 22.66 ? 563  PHE A CZ    1 
ATOM   8706 N N     . ALA B 1 566 ? 45.709 -10.281 -37.498 1.00 23.63 ? 564  ALA A N     1 
ATOM   8707 C CA    . ALA B 1 566 ? 45.798 -10.958 -36.185 1.00 24.27 ? 564  ALA A CA    1 
ATOM   8708 C C     . ALA B 1 566 ? 44.425 -11.368 -35.647 1.00 24.78 ? 564  ALA A C     1 
ATOM   8709 O O     . ALA B 1 566 ? 44.299 -12.495 -35.172 1.00 22.07 ? 564  ALA A O     1 
ATOM   8710 C CB    . ALA B 1 566 ? 46.466 -10.044 -35.199 1.00 25.68 ? 564  ALA A CB    1 
ATOM   8711 N N     . ARG B 1 567 ? 43.436 -10.492 -35.770 1.00 24.32 ? 565  ARG A N     1 
ATOM   8712 C CA    . ARG B 1 567 ? 42.154 -10.750 -35.070 1.00 25.36 ? 565  ARG A CA    1 
ATOM   8713 C C     . ARG B 1 567 ? 40.951 -10.952 -36.001 1.00 22.33 ? 565  ARG A C     1 
ATOM   8714 O O     . ARG B 1 567 ? 39.964 -11.472 -35.516 1.00 24.77 ? 565  ARG A O     1 
ATOM   8715 C CB    . ARG B 1 567 ? 41.908 -9.561  -34.137 1.00 25.92 ? 565  ARG A CB    1 
ATOM   8716 C CG    . ARG B 1 567 ? 43.100 -9.165  -33.278 1.00 31.07 ? 565  ARG A CG    1 
ATOM   8717 C CD    . ARG B 1 567 ? 43.144 -9.807  -31.906 1.00 28.40 ? 565  ARG A CD    1 
ATOM   8718 N NE    . ARG B 1 567 ? 41.889 -9.816  -31.167 1.00 27.56 ? 565  ARG A NE    1 
ATOM   8719 C CZ    . ARG B 1 567 ? 41.792 -9.893  -29.844 1.00 27.77 ? 565  ARG A CZ    1 
ATOM   8720 N NH1   . ARG B 1 567 ? 42.882 -9.949  -29.099 1.00 26.83 ? 565  ARG A NH1   1 
ATOM   8721 N NH2   . ARG B 1 567 ? 40.605 -9.912  -29.268 1.00 27.22 ? 565  ARG A NH2   1 
ATOM   8722 N N     . LEU B 1 568 ? 41.023 -10.515 -37.252 1.00 22.38 ? 566  LEU A N     1 
ATOM   8723 C CA    . LEU B 1 568 ? 39.833 -10.613 -38.146 1.00 23.03 ? 566  LEU A CA    1 
ATOM   8724 C C     . LEU B 1 568 ? 40.002 -11.767 -39.141 1.00 25.54 ? 566  LEU A C     1 
ATOM   8725 O O     . LEU B 1 568 ? 39.056 -12.565 -39.230 1.00 22.77 ? 566  LEU A O     1 
ATOM   8726 C CB    . LEU B 1 568 ? 39.558 -9.274  -38.815 1.00 22.76 ? 566  LEU A CB    1 
ATOM   8727 C CG    . LEU B 1 568 ? 39.266 -8.122  -37.858 1.00 23.94 ? 566  LEU A CG    1 
ATOM   8728 C CD1   . LEU B 1 568 ? 38.796 -6.901  -38.607 1.00 23.35 ? 566  LEU A CD1   1 
ATOM   8729 C CD2   . LEU B 1 568 ? 38.235 -8.516  -36.805 1.00 26.86 ? 566  LEU A CD2   1 
ATOM   8730 N N     . LEU B 1 569 ? 41.180 -11.918 -39.769 1.00 25.21 ? 567  LEU A N     1 
ATOM   8731 C CA    . LEU B 1 569 ? 41.397 -12.949 -40.811 1.00 24.60 ? 567  LEU A CA    1 
ATOM   8732 C C     . LEU B 1 569 ? 41.098 -14.326 -40.243 1.00 23.28 ? 567  LEU A C     1 
ATOM   8733 O O     . LEU B 1 569 ? 40.557 -15.156 -40.954 1.00 25.81 ? 567  LEU A O     1 
ATOM   8734 C CB    . LEU B 1 569 ? 42.825 -12.910 -41.367 1.00 24.57 ? 567  LEU A CB    1 
ATOM   8735 C CG    . LEU B 1 569 ? 43.099 -13.910 -42.500 1.00 24.52 ? 567  LEU A CG    1 
ATOM   8736 C CD1   . LEU B 1 569 ? 42.051 -13.828 -43.625 1.00 23.20 ? 567  LEU A CD1   1 
ATOM   8737 C CD2   . LEU B 1 569 ? 44.488 -13.662 -43.067 1.00 24.45 ? 567  LEU A CD2   1 
ATOM   8738 N N     . PRO B 1 570 ? 41.404 -14.650 -38.964 1.00 23.57 ? 568  PRO A N     1 
ATOM   8739 C CA    . PRO B 1 570 ? 41.114 -15.996 -38.459 1.00 22.48 ? 568  PRO A CA    1 
ATOM   8740 C C     . PRO B 1 570 ? 39.622 -16.366 -38.463 1.00 21.18 ? 568  PRO A C     1 
ATOM   8741 O O     . PRO B 1 570 ? 39.295 -17.545 -38.347 1.00 20.82 ? 568  PRO A O     1 
ATOM   8742 C CB    . PRO B 1 570 ? 41.700 -15.954 -37.037 1.00 24.00 ? 568  PRO A CB    1 
ATOM   8743 C CG    . PRO B 1 570 ? 42.793 -14.922 -37.147 1.00 25.48 ? 568  PRO A CG    1 
ATOM   8744 C CD    . PRO B 1 570 ? 42.158 -13.844 -37.993 1.00 24.80 ? 568  PRO A CD    1 
ATOM   8745 N N     . ARG B 1 571 ? 38.745 -15.390 -38.682 1.00 20.04 ? 569  ARG A N     1 
ATOM   8746 C CA    . ARG B 1 571 ? 37.292 -15.651 -38.861 1.00 21.55 ? 569  ARG A CA    1 
ATOM   8747 C C     . ARG B 1 571 ? 37.039 -16.689 -39.967 1.00 22.38 ? 569  ARG A C     1 
ATOM   8748 O O     . ARG B 1 571 ? 35.974 -17.316 -39.940 1.00 21.13 ? 569  ARG A O     1 
ATOM   8749 C CB    . ARG B 1 571 ? 36.572 -14.335 -39.126 1.00 21.87 ? 569  ARG A CB    1 
ATOM   8750 C CG    . ARG B 1 571 ? 36.498 -13.459 -37.881 1.00 22.71 ? 569  ARG A CG    1 
ATOM   8751 C CD    . ARG B 1 571 ? 35.779 -12.173 -38.183 1.00 22.25 ? 569  ARG A CD    1 
ATOM   8752 N NE    . ARG B 1 571 ? 35.576 -11.356 -37.000 1.00 23.95 ? 569  ARG A NE    1 
ATOM   8753 C CZ    . ARG B 1 571 ? 34.834 -10.254 -37.001 1.00 24.58 ? 569  ARG A CZ    1 
ATOM   8754 N NH1   . ARG B 1 571 ? 34.696 -9.549  -35.896 1.00 25.49 ? 569  ARG A NH1   1 
ATOM   8755 N NH2   . ARG B 1 571 ? 34.208 -9.870  -38.105 1.00 23.63 ? 569  ARG A NH2   1 
ATOM   8756 N N     . ILE B 1 572 ? 37.981 -16.903 -40.889 1.00 20.91 ? 570  ILE A N     1 
ATOM   8757 C CA    . ILE B 1 572 ? 37.753 -17.826 -42.029 1.00 20.94 ? 570  ILE A CA    1 
ATOM   8758 C C     . ILE B 1 572 ? 37.574 -19.260 -41.510 1.00 21.05 ? 570  ILE A C     1 
ATOM   8759 O O     . ILE B 1 572 ? 36.841 -20.017 -42.151 1.00 22.56 ? 570  ILE A O     1 
ATOM   8760 C CB    . ILE B 1 572 ? 38.872 -17.728 -43.079 1.00 22.12 ? 570  ILE A CB    1 
ATOM   8761 C CG1   . ILE B 1 572 ? 40.225 -18.188 -42.522 1.00 23.36 ? 570  ILE A CG1   1 
ATOM   8762 C CG2   . ILE B 1 572 ? 38.938 -16.330 -43.667 1.00 22.17 ? 570  ILE A CG2   1 
ATOM   8763 C CD1   . ILE B 1 572 ? 41.361 -18.003 -43.483 1.00 23.02 ? 570  ILE A CD1   1 
ATOM   8764 N N     . HIS B 1 573 ? 38.169 -19.648 -40.387 1.00 21.97 ? 571  HIS A N     1 
ATOM   8765 C CA    . HIS B 1 573 ? 38.246 -21.094 -40.017 1.00 23.28 ? 571  HIS A CA    1 
ATOM   8766 C C     . HIS B 1 573 ? 36.879 -21.642 -39.569 1.00 23.33 ? 571  HIS A C     1 
ATOM   8767 O O     . HIS B 1 573 ? 36.494 -22.727 -40.038 1.00 23.44 ? 571  HIS A O     1 
ATOM   8768 C CB    . HIS B 1 573 ? 39.372 -21.312 -39.015 1.00 25.36 ? 571  HIS A CB    1 
ATOM   8769 C CG    . HIS B 1 573 ? 40.690 -20.964 -39.619 1.00 27.84 ? 571  HIS A CG    1 
ATOM   8770 N ND1   . HIS B 1 573 ? 41.441 -19.878 -39.188 1.00 33.35 ? 571  HIS A ND1   1 
ATOM   8771 C CD2   . HIS B 1 573 ? 41.354 -21.499 -40.663 1.00 28.04 ? 571  HIS A CD2   1 
ATOM   8772 C CE1   . HIS B 1 573 ? 42.549 -19.796 -39.921 1.00 31.30 ? 571  HIS A CE1   1 
ATOM   8773 N NE2   . HIS B 1 573 ? 42.520 -20.785 -40.820 1.00 31.58 ? 571  HIS A NE2   1 
ATOM   8774 N N     . SER B 1 574 ? 36.190 -20.951 -38.676 1.00 21.74 ? 572  SER A N     1 
ATOM   8775 C CA    . SER B 1 574 ? 34.840 -21.329 -38.193 1.00 22.46 ? 572  SER A CA    1 
ATOM   8776 C C     . SER B 1 574 ? 33.834 -21.292 -39.358 1.00 21.48 ? 572  SER A C     1 
ATOM   8777 O O     . SER B 1 574 ? 32.964 -22.149 -39.444 1.00 22.24 ? 572  SER A O     1 
ATOM   8778 C CB    . SER B 1 574 ? 34.392 -20.448 -37.042 1.00 21.55 ? 572  SER A CB    1 
ATOM   8779 O OG    . SER B 1 574 ? 35.068 -20.793 -35.833 1.00 21.14 ? 572  SER A OG    1 
ATOM   8780 N N     . LEU B 1 575 ? 33.943 -20.312 -40.231 1.00 23.23 ? 573  LEU A N     1 
ATOM   8781 C CA    . LEU B 1 575 ? 33.002 -20.157 -41.366 1.00 22.07 ? 573  LEU A CA    1 
ATOM   8782 C C     . LEU B 1 575 ? 33.202 -21.338 -42.320 1.00 22.50 ? 573  LEU A C     1 
ATOM   8783 O O     . LEU B 1 575 ? 32.190 -21.951 -42.759 1.00 22.17 ? 573  LEU A O     1 
ATOM   8784 C CB    . LEU B 1 575 ? 33.274 -18.801 -42.004 1.00 20.23 ? 573  LEU A CB    1 
ATOM   8785 C CG    . LEU B 1 575 ? 32.743 -17.604 -41.224 1.00 22.11 ? 573  LEU A CG    1 
ATOM   8786 C CD1   . LEU B 1 575 ? 33.253 -16.308 -41.837 1.00 22.71 ? 573  LEU A CD1   1 
ATOM   8787 C CD2   . LEU B 1 575 ? 31.196 -17.594 -41.160 1.00 22.48 ? 573  LEU A CD2   1 
ATOM   8788 N N     . SER B 1 576 ? 34.455 -21.703 -42.558 1.00 22.33 ? 574  SER A N     1 
ATOM   8789 C CA    . SER B 1 576 ? 34.776 -22.843 -43.453 1.00 23.13 ? 574  SER A CA    1 
ATOM   8790 C C     . SER B 1 576 ? 34.254 -24.160 -42.860 1.00 23.78 ? 574  SER A C     1 
ATOM   8791 O O     . SER B 1 576 ? 33.746 -24.988 -43.605 1.00 23.04 ? 574  SER A O     1 
ATOM   8792 C CB    . SER B 1 576 ? 36.252 -22.875 -43.737 1.00 22.60 ? 574  SER A CB    1 
ATOM   8793 O OG    . SER B 1 576 ? 36.692 -21.648 -44.292 1.00 23.04 ? 574  SER A OG    1 
ATOM   8794 N N     . ALA B 1 577 ? 34.364 -24.317 -41.544 1.00 25.06 ? 575  ALA A N     1 
ATOM   8795 C CA    . ALA B 1 577 ? 33.889 -25.555 -40.887 1.00 24.66 ? 575  ALA A CA    1 
ATOM   8796 C C     . ALA B 1 577 ? 32.362 -25.624 -40.962 1.00 24.47 ? 575  ALA A C     1 
ATOM   8797 O O     . ALA B 1 577 ? 31.837 -26.694 -41.248 1.00 24.57 ? 575  ALA A O     1 
ATOM   8798 C CB    . ALA B 1 577 ? 34.386 -25.595 -39.470 1.00 25.82 ? 575  ALA A CB    1 
ATOM   8799 N N     . SER B 1 578 ? 31.695 -24.497 -40.724 1.00 24.14 ? 576  SER A N     1 
ATOM   8800 C CA    . SER B 1 578 ? 30.212 -24.449 -40.805 1.00 27.40 ? 576  SER A CA    1 
ATOM   8801 C C     . SER B 1 578 ? 29.768 -24.818 -42.225 1.00 26.54 ? 576  SER A C     1 
ATOM   8802 O O     . SER B 1 578 ? 28.864 -25.641 -42.357 1.00 27.24 ? 576  SER A O     1 
ATOM   8803 C CB    . SER B 1 578 ? 29.686 -23.104 -40.384 1.00 29.29 ? 576  SER A CB    1 
ATOM   8804 O OG    . SER B 1 578 ? 29.923 -22.885 -39.005 1.00 42.70 ? 576  SER A OG    1 
ATOM   8805 N N     . VAL B 1 579 ? 30.382 -24.202 -43.235 1.00 25.19 ? 577  VAL A N     1 
ATOM   8806 C CA    . VAL B 1 579 ? 30.081 -24.547 -44.659 1.00 24.11 ? 577  VAL A CA    1 
ATOM   8807 C C     . VAL B 1 579 ? 30.273 -26.072 -44.826 1.00 25.56 ? 577  VAL A C     1 
ATOM   8808 O O     . VAL B 1 579 ? 29.338 -26.733 -45.346 1.00 23.32 ? 577  VAL A O     1 
ATOM   8809 C CB    . VAL B 1 579 ? 30.954 -23.730 -45.626 1.00 22.86 ? 577  VAL A CB    1 
ATOM   8810 C CG1   . VAL B 1 579 ? 30.893 -24.271 -47.054 1.00 22.69 ? 577  VAL A CG1   1 
ATOM   8811 C CG2   . VAL B 1 579 ? 30.628 -22.245 -45.592 1.00 23.37 ? 577  VAL A CG2   1 
ATOM   8812 N N     . ARG B 1 580 ? 31.410 -26.618 -44.374 1.00 25.29 ? 578  ARG A N     1 
ATOM   8813 C CA    . ARG B 1 580 ? 31.769 -28.047 -44.599 1.00 26.68 ? 578  ARG A CA    1 
ATOM   8814 C C     . ARG B 1 580 ? 30.809 -28.998 -43.881 1.00 27.02 ? 578  ARG A C     1 
ATOM   8815 O O     . ARG B 1 580 ? 30.866 -30.189 -44.195 1.00 27.25 ? 578  ARG A O     1 
ATOM   8816 C CB    . ARG B 1 580 ? 33.193 -28.349 -44.124 1.00 28.30 ? 578  ARG A CB    1 
ATOM   8817 C CG    . ARG B 1 580 ? 34.274 -27.900 -45.084 1.00 28.51 ? 578  ARG A CG    1 
ATOM   8818 C CD    . ARG B 1 580 ? 35.653 -28.001 -44.460 1.00 29.28 ? 578  ARG A CD    1 
ATOM   8819 N NE    . ARG B 1 580 ? 36.662 -27.538 -45.409 1.00 32.17 ? 578  ARG A NE    1 
ATOM   8820 C CZ    . ARG B 1 580 ? 37.179 -28.277 -46.395 1.00 33.50 ? 578  ARG A CZ    1 
ATOM   8821 N NH1   . ARG B 1 580 ? 38.098 -27.771 -47.193 1.00 34.09 ? 578  ARG A NH1   1 
ATOM   8822 N NH2   . ARG B 1 580 ? 36.772 -29.519 -46.586 1.00 35.02 ? 578  ARG A NH2   1 
ATOM   8823 N N     . ALA B 1 581 ? 29.984 -28.529 -42.933 1.00 25.72 ? 579  ALA A N     1 
ATOM   8824 C CA    . ALA B 1 581 ? 28.953 -29.367 -42.288 1.00 26.97 ? 579  ALA A CA    1 
ATOM   8825 C C     . ALA B 1 581 ? 27.896 -29.742 -43.327 1.00 27.69 ? 579  ALA A C     1 
ATOM   8826 O O     . ALA B 1 581 ? 27.207 -30.749 -43.130 1.00 26.46 ? 579  ALA A O     1 
ATOM   8827 C CB    . ALA B 1 581 ? 28.342 -28.650 -41.109 1.00 30.46 ? 579  ALA A CB    1 
ATOM   8828 N N     . GLY B 1 582 ? 27.780 -28.956 -44.410 1.00 25.97 ? 580  GLY A N     1 
ATOM   8829 C CA    . GLY B 1 582 ? 26.819 -29.207 -45.494 1.00 26.11 ? 580  GLY A CA    1 
ATOM   8830 C C     . GLY B 1 582 ? 25.380 -28.928 -45.095 1.00 25.56 ? 580  GLY A C     1 
ATOM   8831 O O     . GLY B 1 582 ? 25.117 -28.494 -43.936 1.00 26.42 ? 580  GLY A O     1 
ATOM   8832 N N     . SER B 1 583 ? 24.456 -29.250 -45.996 1.00 24.71 ? 581  SER A N     1 
ATOM   8833 C CA    . SER B 1 583 ? 23.013 -28.914 -45.895 1.00 26.60 ? 581  SER A CA    1 
ATOM   8834 C C     . SER B 1 583 ? 22.257 -29.881 -44.974 1.00 27.11 ? 581  SER A C     1 
ATOM   8835 O O     . SER B 1 583 ? 21.089 -29.590 -44.641 1.00 25.50 ? 581  SER A O     1 
ATOM   8836 C CB    . SER B 1 583 ? 22.380 -28.877 -47.265 1.00 27.86 ? 581  SER A CB    1 
ATOM   8837 O OG    . SER B 1 583 ? 22.380 -30.160 -47.866 1.00 26.30 ? 581  SER A OG    1 
ATOM   8838 N N     . GLU B 1 584 ? 22.852 -31.015 -44.609 1.00 28.67 ? 582  GLU A N     1 
ATOM   8839 C CA    . GLU B 1 584 ? 22.085 -32.109 -43.948 1.00 30.80 ? 582  GLU A CA    1 
ATOM   8840 C C     . GLU B 1 584 ? 21.324 -31.569 -42.727 1.00 27.12 ? 582  GLU A C     1 
ATOM   8841 O O     . GLU B 1 584 ? 20.107 -31.784 -42.626 1.00 25.59 ? 582  GLU A O     1 
ATOM   8842 C CB    . GLU B 1 584 ? 23.011 -33.238 -43.509 1.00 34.17 ? 582  GLU A CB    1 
ATOM   8843 C CG    . GLU B 1 584 ? 22.259 -34.507 -43.168 1.00 43.51 ? 582  GLU A CG    1 
ATOM   8844 C CD    . GLU B 1 584 ? 23.086 -35.544 -42.434 1.00 45.55 ? 582  GLU A CD    1 
ATOM   8845 O OE1   . GLU B 1 584 ? 24.322 -35.444 -42.486 1.00 48.33 ? 582  GLU A OE1   1 
ATOM   8846 O OE2   . GLU B 1 584 ? 22.487 -36.427 -41.800 1.00 55.16 ? 582  GLU A OE2   1 
ATOM   8847 N N     . SER B 1 585 ? 22.005 -30.853 -41.831 1.00 27.02 ? 583  SER A N     1 
ATOM   8848 C CA    . SER B 1 585 ? 21.391 -30.367 -40.568 1.00 28.58 ? 583  SER A CA    1 
ATOM   8849 C C     . SER B 1 585 ? 20.354 -29.267 -40.850 1.00 28.86 ? 583  SER A C     1 
ATOM   8850 O O     . SER B 1 585 ? 19.577 -28.980 -39.921 1.00 26.70 ? 583  SER A O     1 
ATOM   8851 C CB    . SER B 1 585 ? 22.420 -29.897 -39.589 1.00 28.07 ? 583  SER A CB    1 
ATOM   8852 O OG    . SER B 1 585 ? 22.852 -28.596 -39.931 1.00 28.50 ? 583  SER A OG    1 
ATOM   8853 N N     . LEU B 1 586 ? 20.292 -28.696 -42.061 1.00 25.58 ? 584  LEU A N     1 
ATOM   8854 C CA    . LEU B 1 586 ? 19.251 -27.674 -42.384 1.00 24.72 ? 584  LEU A CA    1 
ATOM   8855 C C     . LEU B 1 586 ? 17.911 -28.344 -42.701 1.00 23.65 ? 584  LEU A C     1 
ATOM   8856 O O     . LEU B 1 586 ? 16.903 -27.629 -42.685 1.00 24.54 ? 584  LEU A O     1 
ATOM   8857 C CB    . LEU B 1 586 ? 19.700 -26.836 -43.580 1.00 26.03 ? 584  LEU A CB    1 
ATOM   8858 C CG    . LEU B 1 586 ? 20.659 -25.694 -43.272 1.00 26.68 ? 584  LEU A CG    1 
ATOM   8859 C CD1   . LEU B 1 586 ? 21.880 -26.186 -42.537 1.00 28.34 ? 584  LEU A CD1   1 
ATOM   8860 C CD2   . LEU B 1 586 ? 21.047 -25.000 -44.558 1.00 27.55 ? 584  LEU A CD2   1 
ATOM   8861 N N     . TYR B 1 587 ? 17.913 -29.628 -43.072 1.00 23.83 ? 585  TYR A N     1 
ATOM   8862 C CA    . TYR B 1 587 ? 16.766 -30.338 -43.685 1.00 27.08 ? 585  TYR A CA    1 
ATOM   8863 C C     . TYR B 1 587 ? 16.319 -31.525 -42.816 1.00 29.74 ? 585  TYR A C     1 
ATOM   8864 O O     . TYR B 1 587 ? 15.429 -32.267 -43.262 1.00 30.61 ? 585  TYR A O     1 
ATOM   8865 C CB    . TYR B 1 587 ? 17.070 -30.725 -45.140 1.00 27.75 ? 585  TYR A CB    1 
ATOM   8866 C CG    . TYR B 1 587 ? 16.936 -29.527 -46.048 1.00 26.74 ? 585  TYR A CG    1 
ATOM   8867 C CD1   . TYR B 1 587 ? 15.704 -29.129 -46.545 1.00 24.93 ? 585  TYR A CD1   1 
ATOM   8868 C CD2   . TYR B 1 587 ? 18.024 -28.705 -46.282 1.00 25.17 ? 585  TYR A CD2   1 
ATOM   8869 C CE1   . TYR B 1 587 ? 15.574 -27.967 -47.291 1.00 26.31 ? 585  TYR A CE1   1 
ATOM   8870 C CE2   . TYR B 1 587 ? 17.913 -27.551 -47.037 1.00 26.09 ? 585  TYR A CE2   1 
ATOM   8871 C CZ    . TYR B 1 587 ? 16.685 -27.176 -47.541 1.00 24.25 ? 585  TYR A CZ    1 
ATOM   8872 O OH    . TYR B 1 587 ? 16.604 -26.040 -48.283 1.00 26.40 ? 585  TYR A OH    1 
ATOM   8873 N N     . LEU B 1 588 ? 16.814 -31.636 -41.590 1.00 28.86 ? 586  LEU A N     1 
ATOM   8874 C CA    . LEU B 1 588 ? 16.344 -32.719 -40.685 1.00 29.35 ? 586  LEU A CA    1 
ATOM   8875 C C     . LEU B 1 588 ? 14.866 -32.518 -40.321 1.00 28.32 ? 586  LEU A C     1 
ATOM   8876 O O     . LEU B 1 588 ? 14.183 -33.520 -40.102 1.00 28.94 ? 586  LEU A O     1 
ATOM   8877 C CB    . LEU B 1 588 ? 17.217 -32.722 -39.429 1.00 28.11 ? 586  LEU A CB    1 
ATOM   8878 C CG    . LEU B 1 588 ? 18.705 -32.959 -39.656 1.00 28.24 ? 586  LEU A CG    1 
ATOM   8879 C CD1   . LEU B 1 588 ? 19.477 -32.775 -38.362 1.00 28.51 ? 586  LEU A CD1   1 
ATOM   8880 C CD2   . LEU B 1 588 ? 18.942 -34.347 -40.225 1.00 31.22 ? 586  LEU A CD2   1 
ATOM   8881 N N     . LEU B 1 589 ? 14.412 -31.271 -40.246 1.00 26.39 ? 587  LEU A N     1 
ATOM   8882 C CA    . LEU B 1 589 ? 13.024 -30.997 -39.792 1.00 26.46 ? 587  LEU A CA    1 
ATOM   8883 C C     . LEU B 1 589 ? 12.077 -30.599 -40.925 1.00 27.40 ? 587  LEU A C     1 
ATOM   8884 O O     . LEU B 1 589 ? 12.475 -29.826 -41.799 1.00 25.49 ? 587  LEU A O     1 
ATOM   8885 C CB    . LEU B 1 589 ? 13.041 -29.878 -38.743 1.00 26.47 ? 587  LEU A CB    1 
ATOM   8886 C CG    . LEU B 1 589 ? 13.772 -30.184 -37.440 1.00 27.07 ? 587  LEU A CG    1 
ATOM   8887 C CD1   . LEU B 1 589 ? 13.555 -29.064 -36.437 1.00 28.85 ? 587  LEU A CD1   1 
ATOM   8888 C CD2   . LEU B 1 589 ? 13.315 -31.513 -36.864 1.00 29.04 ? 587  LEU A CD2   1 
ATOM   8889 N N     . ASP B 1 590 ? 10.846 -31.096 -40.857 1.00 28.66 ? 588  ASP A N     1 
ATOM   8890 C CA    . ASP B 1 590 ? 9.803  -30.653 -41.801 1.00 28.88 ? 588  ASP A CA    1 
ATOM   8891 C C     . ASP B 1 590 ? 9.328  -29.281 -41.336 1.00 28.70 ? 588  ASP A C     1 
ATOM   8892 O O     . ASP B 1 590 ? 9.526  -28.955 -40.169 1.00 29.37 ? 588  ASP A O     1 
ATOM   8893 C CB    . ASP B 1 590 ? 8.636  -31.632 -41.831 1.00 32.10 ? 588  ASP A CB    1 
ATOM   8894 C CG    . ASP B 1 590 ? 9.016  -33.018 -42.311 1.00 36.09 ? 588  ASP A CG    1 
ATOM   8895 O OD1   . ASP B 1 590 ? 9.846  -33.111 -43.227 1.00 36.90 ? 588  ASP A OD1   1 
ATOM   8896 O OD2   . ASP B 1 590 ? 8.475  -33.991 -41.761 1.00 45.40 ? 588  ASP A OD2   1 
ATOM   8897 N N     . ALA B 1 591 ? 8.673  -28.540 -42.215 1.00 27.84 ? 589  ALA A N     1 
ATOM   8898 C CA    . ALA B 1 591 ? 8.240  -27.163 -41.878 1.00 29.71 ? 589  ALA A CA    1 
ATOM   8899 C C     . ALA B 1 591 ? 7.348  -27.150 -40.626 1.00 31.07 ? 589  ALA A C     1 
ATOM   8900 O O     . ALA B 1 591 ? 7.380  -26.168 -39.892 1.00 27.98 ? 589  ALA A O     1 
ATOM   8901 C CB    . ALA B 1 591 ? 7.535  -26.575 -43.064 1.00 30.55 ? 589  ALA A CB    1 
ATOM   8902 N N     . GLU B 1 592 ? 6.566  -28.206 -40.427 1.00 29.63 ? 590  GLU A N     1 
ATOM   8903 C CA    . GLU B 1 592 ? 5.618  -28.267 -39.285 1.00 33.47 ? 590  GLU A CA    1 
ATOM   8904 C C     . GLU B 1 592 ? 6.366  -28.488 -37.964 1.00 28.82 ? 590  GLU A C     1 
ATOM   8905 O O     . GLU B 1 592 ? 5.768  -28.250 -36.921 1.00 29.86 ? 590  GLU A O     1 
ATOM   8906 C CB    . GLU B 1 592 ? 4.600  -29.381 -39.536 1.00 36.97 ? 590  GLU A CB    1 
ATOM   8907 C CG    . GLU B 1 592 ? 3.686  -29.113 -40.716 1.00 44.47 ? 590  GLU A CG    1 
ATOM   8908 C CD    . GLU B 1 592 ? 4.348  -29.144 -42.083 1.00 50.67 ? 590  GLU A CD    1 
ATOM   8909 O OE1   . GLU B 1 592 ? 5.286  -29.944 -42.272 1.00 43.08 ? 590  GLU A OE1   1 
ATOM   8910 O OE2   . GLU B 1 592 ? 3.925  -28.359 -42.954 1.00 52.60 ? 590  GLU A OE2   1 
ATOM   8911 N N     . GLN B 1 593 ? 7.624  -28.907 -38.026 1.00 27.25 ? 591  GLN A N     1 
ATOM   8912 C CA    . GLN B 1 593 ? 8.401  -29.217 -36.799 1.00 30.02 ? 591  GLN A CA    1 
ATOM   8913 C C     . GLN B 1 593 ? 9.137  -27.971 -36.278 1.00 29.23 ? 591  GLN A C     1 
ATOM   8914 O O     . GLN B 1 593 ? 9.786  -28.080 -35.243 1.00 29.57 ? 591  GLN A O     1 
ATOM   8915 C CB    . GLN B 1 593 ? 9.347  -30.380 -37.082 1.00 30.39 ? 591  GLN A CB    1 
ATOM   8916 C CG    . GLN B 1 593 ? 8.625  -31.670 -37.425 1.00 31.03 ? 591  GLN A CG    1 
ATOM   8917 C CD    . GLN B 1 593 ? 9.591  -32.791 -37.710 1.00 32.59 ? 591  GLN A CD    1 
ATOM   8918 O OE1   . GLN B 1 593 ? 10.325 -32.767 -38.692 1.00 30.12 ? 591  GLN A OE1   1 
ATOM   8919 N NE2   . GLN B 1 593 ? 9.597  -33.785 -36.840 1.00 34.66 ? 591  GLN A NE2   1 
ATOM   8920 N N     . PHE B 1 594 ? 9.014  -26.844 -36.969 1.00 28.55 ? 592  PHE A N     1 
ATOM   8921 C CA    . PHE B 1 594 ? 9.726  -25.600 -36.583 1.00 27.95 ? 592  PHE A CA    1 
ATOM   8922 C C     . PHE B 1 594 ? 8.961  -24.835 -35.494 1.00 31.39 ? 592  PHE A C     1 
ATOM   8923 O O     . PHE B 1 594 ? 7.745  -25.046 -35.436 1.00 31.57 ? 592  PHE A O     1 
ATOM   8924 C CB    . PHE B 1 594 ? 9.929  -24.706 -37.805 1.00 28.13 ? 592  PHE A CB    1 
ATOM   8925 C CG    . PHE B 1 594 ? 11.130 -25.041 -38.650 1.00 27.63 ? 592  PHE A CG    1 
ATOM   8926 C CD1   . PHE B 1 594 ? 11.139 -26.165 -39.458 1.00 26.75 ? 592  PHE A CD1   1 
ATOM   8927 C CD2   . PHE B 1 594 ? 12.251 -24.228 -38.640 1.00 29.57 ? 592  PHE A CD2   1 
ATOM   8928 C CE1   . PHE B 1 594 ? 12.244 -26.470 -40.235 1.00 27.37 ? 592  PHE A CE1   1 
ATOM   8929 C CE2   . PHE B 1 594 ? 13.355 -24.533 -39.420 1.00 29.67 ? 592  PHE A CE2   1 
ATOM   8930 C CZ    . PHE B 1 594 ? 13.350 -25.654 -40.214 1.00 28.55 ? 592  PHE A CZ    1 
HETATM 8931 P PA    . FAD C 2 .   ? 30.626 4.659   -20.230 1.00 32.08 ? 601  FAD B PA    1 
HETATM 8932 O O1A   . FAD C 2 .   ? 30.538 4.067   -18.869 1.00 28.81 ? 601  FAD B O1A   1 
HETATM 8933 O O2A   . FAD C 2 .   ? 31.030 6.083   -20.381 1.00 29.96 ? 601  FAD B O2A   1 
HETATM 8934 O O5B   . FAD C 2 .   ? 31.549 3.740   -21.139 1.00 28.65 ? 601  FAD B O5B   1 
HETATM 8935 C C5B   . FAD C 2 .   ? 31.843 4.165   -22.482 1.00 29.63 ? 601  FAD B C5B   1 
HETATM 8936 C C4B   . FAD C 2 .   ? 32.567 3.048   -23.184 1.00 29.04 ? 601  FAD B C4B   1 
HETATM 8937 O O4B   . FAD C 2 .   ? 33.783 2.747   -22.454 1.00 26.25 ? 601  FAD B O4B   1 
HETATM 8938 C C3B   . FAD C 2 .   ? 31.798 1.724   -23.271 1.00 29.04 ? 601  FAD B C3B   1 
HETATM 8939 O O3B   . FAD C 2 .   ? 32.068 1.069   -24.500 1.00 32.42 ? 601  FAD B O3B   1 
HETATM 8940 C C2B   . FAD C 2 .   ? 32.337 0.950   -22.067 1.00 25.64 ? 601  FAD B C2B   1 
HETATM 8941 O O2B   . FAD C 2 .   ? 32.184 -0.446  -22.182 1.00 22.50 ? 601  FAD B O2B   1 
HETATM 8942 C C1B   . FAD C 2 .   ? 33.795 1.394   -22.068 1.00 26.82 ? 601  FAD B C1B   1 
HETATM 8943 N N9A   . FAD C 2 .   ? 34.430 1.304   -20.766 1.00 25.26 ? 601  FAD B N9A   1 
HETATM 8944 C C8A   . FAD C 2 .   ? 34.273 2.145   -19.696 1.00 26.91 ? 601  FAD B C8A   1 
HETATM 8945 N N7A   . FAD C 2 .   ? 34.988 1.781   -18.658 1.00 26.66 ? 601  FAD B N7A   1 
HETATM 8946 C C5A   . FAD C 2 .   ? 35.651 0.635   -19.075 1.00 28.03 ? 601  FAD B C5A   1 
HETATM 8947 C C6A   . FAD C 2 .   ? 36.560 -0.226  -18.436 1.00 28.88 ? 601  FAD B C6A   1 
HETATM 8948 N N6A   . FAD C 2 .   ? 36.973 -0.066  -17.184 1.00 32.06 ? 601  FAD B N6A   1 
HETATM 8949 N N1A   . FAD C 2 .   ? 37.022 -1.281  -19.147 1.00 27.92 ? 601  FAD B N1A   1 
HETATM 8950 C C2A   . FAD C 2 .   ? 36.603 -1.436  -20.408 1.00 28.87 ? 601  FAD B C2A   1 
HETATM 8951 N N3A   . FAD C 2 .   ? 35.751 -0.696  -21.107 1.00 26.44 ? 601  FAD B N3A   1 
HETATM 8952 C C4A   . FAD C 2 .   ? 35.310 0.336   -20.375 1.00 27.65 ? 601  FAD B C4A   1 
HETATM 8953 N N1    . FAD C 2 .   ? 21.402 3.532   -15.130 1.00 29.70 ? 601  FAD B N1    1 
HETATM 8954 C C2    . FAD C 2 .   ? 20.764 3.550   -13.948 1.00 31.51 ? 601  FAD B C2    1 
HETATM 8955 O O2    . FAD C 2 .   ? 21.384 3.726   -12.910 1.00 28.74 ? 601  FAD B O2    1 
HETATM 8956 N N3    . FAD C 2 .   ? 19.430 3.329   -13.842 1.00 30.19 ? 601  FAD B N3    1 
HETATM 8957 C C4    . FAD C 2 .   ? 18.644 3.101   -14.941 1.00 29.41 ? 601  FAD B C4    1 
HETATM 8958 O O4    . FAD C 2 .   ? 17.444 2.936   -14.805 1.00 29.71 ? 601  FAD B O4    1 
HETATM 8959 C C4X   . FAD C 2 .   ? 19.262 3.140   -16.201 1.00 27.70 ? 601  FAD B C4X   1 
HETATM 8960 N N5    . FAD C 2 .   ? 18.523 2.982   -17.269 1.00 24.78 ? 601  FAD B N5    1 
HETATM 8961 C C5X   . FAD C 2 .   ? 19.138 3.120   -18.484 1.00 26.96 ? 601  FAD B C5X   1 
HETATM 8962 C C6    . FAD C 2 .   ? 18.354 3.031   -19.644 1.00 24.50 ? 601  FAD B C6    1 
HETATM 8963 C C7    . FAD C 2 .   ? 18.905 3.206   -20.890 1.00 28.65 ? 601  FAD B C7    1 
HETATM 8964 C C7M   . FAD C 2 .   ? 18.035 3.138   -22.118 1.00 29.01 ? 601  FAD B C7M   1 
HETATM 8965 C C8    . FAD C 2 .   ? 20.292 3.431   -21.012 1.00 26.38 ? 601  FAD B C8    1 
HETATM 8966 C C8M   . FAD C 2 .   ? 20.917 3.600   -22.370 1.00 30.14 ? 601  FAD B C8M   1 
HETATM 8967 C C9    . FAD C 2 .   ? 21.079 3.452   -19.892 1.00 25.62 ? 601  FAD B C9    1 
HETATM 8968 C C9A   . FAD C 2 .   ? 20.523 3.335   -18.611 1.00 27.09 ? 601  FAD B C9A   1 
HETATM 8969 N N10   . FAD C 2 .   ? 21.283 3.427   -17.452 1.00 26.96 ? 601  FAD B N10   1 
HETATM 8970 C C10   . FAD C 2 .   ? 20.681 3.378   -16.215 1.00 27.50 ? 601  FAD B C10   1 
HETATM 8971 C "C1'" . FAD C 2 .   ? 22.737 3.625   -17.555 1.00 27.87 ? 601  FAD B "C1'" 1 
HETATM 8972 C "C2'" . FAD C 2 .   ? 23.391 2.302   -17.963 1.00 29.33 ? 601  FAD B "C2'" 1 
HETATM 8973 O "O2'" . FAD C 2 .   ? 22.999 1.253   -17.102 1.00 30.70 ? 601  FAD B "O2'" 1 
HETATM 8974 C "C3'" . FAD C 2 .   ? 24.919 2.323   -17.979 1.00 37.41 ? 601  FAD B "C3'" 1 
HETATM 8975 O "O3'" . FAD C 2 .   ? 25.445 3.286   -17.083 1.00 32.73 ? 601  FAD B "O3'" 1 
HETATM 8976 C "C4'" . FAD C 2 .   ? 25.405 2.629   -19.387 1.00 34.68 ? 601  FAD B "C4'" 1 
HETATM 8977 O "O4'" . FAD C 2 .   ? 24.901 1.642   -20.287 1.00 31.25 ? 601  FAD B "O4'" 1 
HETATM 8978 C "C5'" . FAD C 2 .   ? 26.907 2.705   -19.467 1.00 31.92 ? 601  FAD B "C5'" 1 
HETATM 8979 O "O5'" . FAD C 2 .   ? 27.109 3.412   -20.696 1.00 28.85 ? 601  FAD B "O5'" 1 
HETATM 8980 P P     . FAD C 2 .   ? 27.722 4.875   -20.660 1.00 30.92 ? 601  FAD B P     1 
HETATM 8981 O O1P   . FAD C 2 .   ? 27.153 5.589   -21.830 1.00 32.06 ? 601  FAD B O1P   1 
HETATM 8982 O O2P   . FAD C 2 .   ? 27.613 5.462   -19.297 1.00 33.02 ? 601  FAD B O2P   1 
HETATM 8983 O O3P   . FAD C 2 .   ? 29.232 4.476   -20.978 1.00 32.84 ? 601  FAD B O3P   1 
HETATM 8984 C C1    . GOL D 3 .   ? 11.530 -28.117 -30.009 1.00 42.14 ? 602  GOL B C1    1 
HETATM 8985 O O1    . GOL D 3 .   ? 12.888 -28.048 -30.429 1.00 36.12 ? 602  GOL B O1    1 
HETATM 8986 C C2    . GOL D 3 .   ? 10.768 -26.892 -30.462 1.00 44.02 ? 602  GOL B C2    1 
HETATM 8987 O O2    . GOL D 3 .   ? 10.002 -27.170 -31.633 1.00 38.11 ? 602  GOL B O2    1 
HETATM 8988 C C3    . GOL D 3 .   ? 9.926  -26.253 -29.381 1.00 40.76 ? 602  GOL B C3    1 
HETATM 8989 O O3    . GOL D 3 .   ? 9.276  -25.075 -29.847 1.00 38.13 ? 602  GOL B O3    1 
HETATM 8990 P PA    . FAD E 2 .   ? 11.158 -11.890 -50.992 1.00 24.42 ? 601  FAD A PA    1 
HETATM 8991 O O1A   . FAD E 2 .   ? 11.742 -11.775 -52.366 1.00 26.01 ? 601  FAD A O1A   1 
HETATM 8992 O O2A   . FAD E 2 .   ? 9.743  -12.348 -50.878 1.00 26.53 ? 601  FAD A O2A   1 
HETATM 8993 O O5B   . FAD E 2 .   ? 12.133 -12.764 -50.092 1.00 23.20 ? 601  FAD A O5B   1 
HETATM 8994 C C5B   . FAD E 2 .   ? 11.694 -13.280 -48.816 1.00 23.49 ? 601  FAD A C5B   1 
HETATM 8995 C C4B   . FAD E 2 .   ? 12.783 -14.152 -48.269 1.00 23.81 ? 601  FAD A C4B   1 
HETATM 8996 O O4B   . FAD E 2 .   ? 12.933 -15.313 -49.127 1.00 25.58 ? 601  FAD A O4B   1 
HETATM 8997 C C3B   . FAD E 2 .   ? 14.175 -13.507 -48.191 1.00 23.80 ? 601  FAD A C3B   1 
HETATM 8998 O O3B   . FAD E 2 .   ? 14.871 -13.967 -47.044 1.00 23.67 ? 601  FAD A O3B   1 
HETATM 8999 C C2B   . FAD E 2 .   ? 14.858 -14.015 -49.463 1.00 24.99 ? 601  FAD A C2B   1 
HETATM 9000 O O2B   . FAD E 2 .   ? 16.263 -13.906 -49.374 1.00 22.00 ? 601  FAD A O2B   1 
HETATM 9001 C C1B   . FAD E 2 .   ? 14.292 -15.436 -49.499 1.00 25.62 ? 601  FAD A C1B   1 
HETATM 9002 N N9A   . FAD E 2 .   ? 14.313 -16.010 -50.813 1.00 25.89 ? 601  FAD A N9A   1 
HETATM 9003 C C8A   . FAD E 2 .   ? 13.440 -15.731 -51.824 1.00 23.78 ? 601  FAD A C8A   1 
HETATM 9004 N N7A   . FAD E 2 .   ? 13.720 -16.392 -52.918 1.00 23.93 ? 601  FAD A N7A   1 
HETATM 9005 C C5A   . FAD E 2 .   ? 14.841 -17.137 -52.607 1.00 22.40 ? 601  FAD A C5A   1 
HETATM 9006 C C6A   . FAD E 2 .   ? 15.617 -18.034 -53.354 1.00 23.57 ? 601  FAD A C6A   1 
HETATM 9007 N N6A   . FAD E 2 .   ? 15.389 -18.313 -54.633 1.00 24.43 ? 601  FAD A N6A   1 
HETATM 9008 N N1A   . FAD E 2 .   ? 16.676 -18.606 -52.732 1.00 24.62 ? 601  FAD A N1A   1 
HETATM 9009 C C2A   . FAD E 2 .   ? 16.907 -18.292 -51.449 1.00 24.03 ? 601  FAD A C2A   1 
HETATM 9010 N N3A   . FAD E 2 .   ? 16.255 -17.450 -50.656 1.00 24.66 ? 601  FAD A N3A   1 
HETATM 9011 C C4A   . FAD E 2 .   ? 15.217 -16.907 -51.303 1.00 25.16 ? 601  FAD A C4A   1 
HETATM 9012 N N1    . FAD E 2 .   ? 12.606 -2.642  -55.266 1.00 22.82 ? 601  FAD A N1    1 
HETATM 9013 C C2    . FAD E 2 .   ? 12.356 -1.923  -56.379 1.00 21.84 ? 601  FAD A C2    1 
HETATM 9014 O O2    . FAD E 2 .   ? 11.890 -2.455  -57.398 1.00 20.54 ? 601  FAD A O2    1 
HETATM 9015 N N3    . FAD E 2 .   ? 12.717 -0.603  -56.474 1.00 22.10 ? 601  FAD A N3    1 
HETATM 9016 C C4    . FAD E 2 .   ? 13.311 0.069   -55.431 1.00 23.42 ? 601  FAD A C4    1 
HETATM 9017 O O4    . FAD E 2 .   ? 13.510 1.279   -55.540 1.00 21.13 ? 601  FAD A O4    1 
HETATM 9018 C C4X   . FAD E 2 .   ? 13.352 -0.601  -54.190 1.00 23.48 ? 601  FAD A C4X   1 
HETATM 9019 N N5    . FAD E 2 .   ? 13.757 0.052   -53.115 1.00 24.74 ? 601  FAD A N5    1 
HETATM 9020 C C5X   . FAD E 2 .   ? 13.537 -0.560  -51.904 1.00 22.94 ? 601  FAD A C5X   1 
HETATM 9021 C C6    . FAD E 2 .   ? 13.666 0.200   -50.738 1.00 23.49 ? 601  FAD A C6    1 
HETATM 9022 C C7    . FAD E 2 .   ? 13.288 -0.303  -49.512 1.00 22.36 ? 601  FAD A C7    1 
HETATM 9023 C C7M   . FAD E 2 .   ? 13.392 0.581   -48.289 1.00 22.89 ? 601  FAD A C7M   1 
HETATM 9024 C C8    . FAD E 2 .   ? 12.950 -1.684  -49.405 1.00 22.69 ? 601  FAD A C8    1 
HETATM 9025 C C8M   . FAD E 2 .   ? 12.658 -2.309  -48.067 1.00 25.41 ? 601  FAD A C8M   1 
HETATM 9026 C C9    . FAD E 2 .   ? 13.013 -2.494  -50.532 1.00 24.52 ? 601  FAD A C9    1 
HETATM 9027 C C9A   . FAD E 2 .   ? 13.194 -1.926  -51.801 1.00 23.92 ? 601  FAD A C9A   1 
HETATM 9028 N N10   . FAD E 2 .   ? 13.060 -2.654  -52.978 1.00 24.55 ? 601  FAD A N10   1 
HETATM 9029 C C10   . FAD E 2 .   ? 12.985 -1.992  -54.192 1.00 23.73 ? 601  FAD A C10   1 
HETATM 9030 C "C1'" . FAD E 2 .   ? 12.729 -4.088  -52.895 1.00 25.45 ? 601  FAD A "C1'" 1 
HETATM 9031 C "C2'" . FAD E 2 .   ? 13.972 -4.843  -52.410 1.00 28.01 ? 601  FAD A "C2'" 1 
HETATM 9032 O "O2'" . FAD E 2 .   ? 14.925 -5.066  -53.456 1.00 26.45 ? 601  FAD A "O2'" 1 
HETATM 9033 C "C3'" . FAD E 2 .   ? 13.612 -6.148  -51.680 1.00 29.08 ? 601  FAD A "C3'" 1 
HETATM 9034 O "O3'" . FAD E 2 .   ? 14.674 -6.541  -50.840 1.00 30.85 ? 601  FAD A "O3'" 1 
HETATM 9035 C "C4'" . FAD E 2 .   ? 13.277 -7.327  -52.579 1.00 29.81 ? 601  FAD A "C4'" 1 
HETATM 9036 O "O4'" . FAD E 2 .   ? 12.015 -7.061  -53.213 1.00 30.98 ? 601  FAD A "O4'" 1 
HETATM 9037 C "C5'" . FAD E 2 .   ? 13.240 -8.627  -51.800 1.00 24.55 ? 601  FAD A "C5'" 1 
HETATM 9038 O "O5'" . FAD E 2 .   ? 12.515 -8.506  -50.550 1.00 24.80 ? 601  FAD A "O5'" 1 
HETATM 9039 P P     . FAD E 2 .   ? 10.982 -9.027  -50.449 1.00 23.75 ? 601  FAD A P     1 
HETATM 9040 O O1P   . FAD E 2 .   ? 10.443 -8.459  -49.180 1.00 22.84 ? 601  FAD A O1P   1 
HETATM 9041 O O2P   . FAD E 2 .   ? 10.222 -8.867  -51.722 1.00 23.83 ? 601  FAD A O2P   1 
HETATM 9042 O O3P   . FAD E 2 .   ? 11.309 -10.554 -50.172 1.00 23.51 ? 601  FAD A O3P   1 
HETATM 9043 C C1    . GOL F 3 .   ? 42.064 10.839  -57.782 1.00 39.78 ? 602  GOL A C1    1 
HETATM 9044 O O1    . GOL F 3 .   ? 42.784 9.615   -57.732 1.00 37.08 ? 602  GOL A O1    1 
HETATM 9045 C C2    . GOL F 3 .   ? 41.712 11.300  -56.391 1.00 38.90 ? 602  GOL A C2    1 
HETATM 9046 O O2    . GOL F 3 .   ? 42.509 12.453  -56.058 1.00 38.54 ? 602  GOL A O2    1 
HETATM 9047 C C3    . GOL F 3 .   ? 41.917 10.166  -55.397 1.00 40.48 ? 602  GOL A C3    1 
HETATM 9048 O O3    . GOL F 3 .   ? 40.802 9.966   -54.534 1.00 34.09 ? 602  GOL A O3    1 
HETATM 9049 C C1    . GOL G 3 .   ? 43.447 6.160   -42.289 1.00 41.39 ? 603  GOL A C1    1 
HETATM 9050 O O1    . GOL G 3 .   ? 42.729 7.326   -41.896 1.00 37.01 ? 603  GOL A O1    1 
HETATM 9051 C C2    . GOL G 3 .   ? 44.789 6.069   -41.594 1.00 39.38 ? 603  GOL A C2    1 
HETATM 9052 O O2    . GOL G 3 .   ? 44.625 6.026   -40.177 1.00 36.36 ? 603  GOL A O2    1 
HETATM 9053 C C3    . GOL G 3 .   ? 45.651 4.918   -42.077 1.00 39.29 ? 603  GOL A C3    1 
HETATM 9054 O O3    . GOL G 3 .   ? 45.153 3.654   -41.648 1.00 29.09 ? 603  GOL A O3    1 
HETATM 9055 C C1    . PGE H 4 .   ? -3.980 -0.394  -60.801 1.00 66.98 ? 604  PGE A C1    1 
HETATM 9056 O O1    . PGE H 4 .   ? -3.521 0.938   -60.747 1.00 61.27 ? 604  PGE A O1    1 
HETATM 9057 C C2    . PGE H 4 .   ? -3.006 -1.349  -60.193 1.00 65.41 ? 604  PGE A C2    1 
HETATM 9058 O O2    . PGE H 4 .   ? -3.689 -2.363  -59.466 1.00 66.69 ? 604  PGE A O2    1 
HETATM 9059 C C3    . PGE H 4 .   ? -3.029 -3.622  -59.518 1.00 62.49 ? 604  PGE A C3    1 
HETATM 9060 C C4    . PGE H 4 .   ? -3.288 -4.276  -60.837 1.00 63.86 ? 604  PGE A C4    1 
HETATM 9061 O O4    . PGE H 4 .   ? -2.309 -5.488  -64.266 1.00 65.00 ? 604  PGE A O4    1 
HETATM 9062 C C6    . PGE H 4 .   ? -2.672 -6.234  -63.128 1.00 64.36 ? 604  PGE A C6    1 
HETATM 9063 C C5    . PGE H 4 .   ? -1.881 -5.847  -61.923 1.00 64.11 ? 604  PGE A C5    1 
HETATM 9064 O O3    . PGE H 4 .   ? -2.756 -5.595  -60.831 1.00 66.53 ? 604  PGE A O3    1 
HETATM 9065 O O     . HOH I 5 .   ? 18.698 -40.488 -23.124 1.00 41.72 ? 701  HOH B O     1 
HETATM 9066 O O     . HOH I 5 .   ? 37.230 -29.832 -14.612 1.00 38.93 ? 702  HOH B O     1 
HETATM 9067 O O     . HOH I 5 .   ? 38.752 -30.965 -20.797 1.00 40.97 ? 703  HOH B O     1 
HETATM 9068 O O     . HOH I 5 .   ? 45.807 -16.560 -33.018 1.00 28.74 ? 704  HOH B O     1 
HETATM 9069 O O     . HOH I 5 .   ? -0.509 10.291  -18.056 1.00 46.14 ? 705  HOH B O     1 
HETATM 9070 O O     . HOH I 5 .   ? 45.009 12.276  -34.626 1.00 36.30 ? 706  HOH B O     1 
HETATM 9071 O O     . HOH I 5 .   ? -0.406 4.583   -28.624 1.00 41.42 ? 707  HOH B O     1 
HETATM 9072 O O     . HOH I 5 .   ? 24.764 -34.562 -34.319 1.00 32.55 ? 708  HOH B O     1 
HETATM 9073 O O     . HOH I 5 .   ? 12.568 -18.776 -19.848 1.00 44.68 ? 709  HOH B O     1 
HETATM 9074 O O     . HOH I 5 .   ? 17.216 -5.914  5.579   1.00 29.84 ? 710  HOH B O     1 
HETATM 9075 O O     . HOH I 5 .   ? 20.823 0.143   -16.702 1.00 39.89 ? 711  HOH B O     1 
HETATM 9076 O O     . HOH I 5 .   ? 34.154 -34.451 -13.501 1.00 47.81 ? 712  HOH B O     1 
HETATM 9077 O O     . HOH I 5 .   ? 7.863  -1.621  11.347  1.00 38.65 ? 713  HOH B O     1 
HETATM 9078 O O     . HOH I 5 .   ? 14.564 -8.070  9.410   1.00 41.85 ? 714  HOH B O     1 
HETATM 9079 O O     . HOH I 5 .   ? 14.714 3.124   -20.177 1.00 27.52 ? 715  HOH B O     1 
HETATM 9080 O O     . HOH I 5 .   ? 35.101 -10.187 -33.002 1.00 41.68 ? 716  HOH B O     1 
HETATM 9081 O O     . HOH I 5 .   ? 22.201 -40.424 -31.060 1.00 35.46 ? 717  HOH B O     1 
HETATM 9082 O O     . HOH I 5 .   ? 46.522 -23.928 -22.897 1.00 41.60 ? 718  HOH B O     1 
HETATM 9083 O O     . HOH I 5 .   ? 33.566 14.159  1.605   1.00 36.26 ? 719  HOH B O     1 
HETATM 9084 O O     . HOH I 5 .   ? 12.235 -9.357  -3.144  1.00 36.85 ? 720  HOH B O     1 
HETATM 9085 O O     . HOH I 5 .   ? 8.039  0.659   9.545   1.00 39.78 ? 721  HOH B O     1 
HETATM 9086 O O     . HOH I 5 .   ? 26.921 -13.676 -33.195 1.00 42.80 ? 722  HOH B O     1 
HETATM 9087 O O     . HOH I 5 .   ? 8.557  15.097  -12.406 1.00 36.99 ? 723  HOH B O     1 
HETATM 9088 O O     . HOH I 5 .   ? 28.454 8.359   1.786   1.00 30.60 ? 724  HOH B O     1 
HETATM 9089 O O     . HOH I 5 .   ? 9.479  -38.077 -30.640 1.00 40.61 ? 725  HOH B O     1 
HETATM 9090 O O     . HOH I 5 .   ? 13.901 -20.801 -15.678 1.00 27.16 ? 726  HOH B O     1 
HETATM 9091 O O     . HOH I 5 .   ? 12.009 -12.526 4.958   1.00 37.76 ? 727  HOH B O     1 
HETATM 9092 O O     . HOH I 5 .   ? 35.567 -35.681 -27.699 1.00 45.32 ? 728  HOH B O     1 
HETATM 9093 O O     . HOH I 5 .   ? 4.089  -23.464 -45.510 1.00 40.22 ? 729  HOH B O     1 
HETATM 9094 O O     . HOH I 5 .   ? 47.512 -8.877  -15.355 1.00 41.50 ? 730  HOH B O     1 
HETATM 9095 O O     . HOH I 5 .   ? 29.519 -15.099 -31.704 1.00 26.11 ? 731  HOH B O     1 
HETATM 9096 O O     . HOH I 5 .   ? 33.254 -24.976 -3.988  1.00 48.01 ? 732  HOH B O     1 
HETATM 9097 O O     . HOH I 5 .   ? 30.025 -39.233 -14.348 1.00 43.49 ? 733  HOH B O     1 
HETATM 9098 O O     . HOH I 5 .   ? 42.489 -5.430  -18.937 1.00 32.18 ? 734  HOH B O     1 
HETATM 9099 O O     . HOH I 5 .   ? 25.420 -9.859  -31.390 1.00 29.64 ? 735  HOH B O     1 
HETATM 9100 O O     . HOH I 5 .   ? 27.474 -15.527 -6.155  1.00 33.77 ? 736  HOH B O     1 
HETATM 9101 O O     . HOH I 5 .   ? 13.596 -16.539 -57.812 1.00 41.74 ? 737  HOH B O     1 
HETATM 9102 O O     . HOH I 5 .   ? 14.538 -23.877 -8.386  1.00 34.41 ? 738  HOH B O     1 
HETATM 9103 O O     . HOH I 5 .   ? 11.642 -30.265 -54.263 1.00 35.83 ? 739  HOH B O     1 
HETATM 9104 O O     . HOH I 5 .   ? 34.009 -1.814  -23.365 1.00 27.61 ? 740  HOH B O     1 
HETATM 9105 O O     . HOH I 5 .   ? 14.450 -35.319 -35.309 1.00 31.90 ? 741  HOH B O     1 
HETATM 9106 O O     . HOH I 5 .   ? 13.175 17.207  1.552   1.00 33.78 ? 742  HOH B O     1 
HETATM 9107 O O     . HOH I 5 .   ? 12.794 -36.274 -17.453 1.00 52.66 ? 743  HOH B O     1 
HETATM 9108 O O     . HOH I 5 .   ? 5.869  -12.235 -32.524 1.00 32.48 ? 744  HOH B O     1 
HETATM 9109 O O     . HOH I 5 .   ? 46.585 -1.952  -34.446 1.00 21.46 ? 745  HOH B O     1 
HETATM 9110 O O     . HOH I 5 .   ? 42.249 -10.489 -12.119 1.00 47.37 ? 746  HOH B O     1 
HETATM 9111 O O     . HOH I 5 .   ? 7.562  -20.578 -29.385 1.00 27.91 ? 747  HOH B O     1 
HETATM 9112 O O     . HOH I 5 .   ? 30.310 -0.829  -24.509 1.00 32.62 ? 748  HOH B O     1 
HETATM 9113 O O     . HOH I 5 .   ? 0.640  4.408   -31.053 1.00 35.65 ? 749  HOH B O     1 
HETATM 9114 O O     . HOH I 5 .   ? 11.736 -22.406 -30.788 1.00 25.36 ? 750  HOH B O     1 
HETATM 9115 O O     . HOH I 5 .   ? 20.528 -14.299 -45.538 1.00 23.62 ? 751  HOH B O     1 
HETATM 9116 O O     . HOH I 5 .   ? 30.076 -29.433 -38.113 1.00 28.65 ? 752  HOH B O     1 
HETATM 9117 O O     . HOH I 5 .   ? -1.442 -15.975 -28.444 1.00 33.30 ? 753  HOH B O     1 
HETATM 9118 O O     . HOH I 5 .   ? 31.717 -9.314  -9.971  1.00 44.78 ? 754  HOH B O     1 
HETATM 9119 O O     . HOH I 5 .   ? 11.015 -21.410 -28.381 1.00 28.80 ? 755  HOH B O     1 
HETATM 9120 O O     . HOH I 5 .   ? 16.866 -9.703  -1.166  1.00 37.45 ? 756  HOH B O     1 
HETATM 9121 O O     . HOH I 5 .   ? 10.013 -7.922  -16.459 1.00 42.44 ? 757  HOH B O     1 
HETATM 9122 O O     . HOH I 5 .   ? 26.076 -6.589  -13.351 1.00 40.92 ? 758  HOH B O     1 
HETATM 9123 O O     . HOH I 5 .   ? 39.409 -29.825 -28.008 1.00 40.47 ? 759  HOH B O     1 
HETATM 9124 O O     . HOH I 5 .   ? -0.551 2.844   1.315   1.00 39.19 ? 760  HOH B O     1 
HETATM 9125 O O     . HOH I 5 .   ? 44.635 -11.458 -24.325 1.00 25.35 ? 761  HOH B O     1 
HETATM 9126 O O     . HOH I 5 .   ? 13.219 20.702  -17.454 1.00 36.36 ? 762  HOH B O     1 
HETATM 9127 O O     . HOH I 5 .   ? 9.587  3.266   -11.801 1.00 27.72 ? 763  HOH B O     1 
HETATM 9128 O O     . HOH I 5 .   ? 51.394 -16.985 -24.632 1.00 39.92 ? 764  HOH B O     1 
HETATM 9129 O O     . HOH I 5 .   ? 11.907 -15.496 -7.738  1.00 45.39 ? 765  HOH B O     1 
HETATM 9130 O O     . HOH I 5 .   ? 4.967  -10.472 -37.894 1.00 43.08 ? 766  HOH B O     1 
HETATM 9131 O O     . HOH I 5 .   ? 34.520 -36.889 -19.082 1.00 32.61 ? 767  HOH B O     1 
HETATM 9132 O O     . HOH I 5 .   ? 19.189 18.659  -14.809 1.00 36.33 ? 768  HOH B O     1 
HETATM 9133 O O     . HOH I 5 .   ? 14.722 15.293  5.250   1.00 28.66 ? 769  HOH B O     1 
HETATM 9134 O O     . HOH I 5 .   ? 3.883  6.649   -35.663 1.00 46.10 ? 770  HOH B O     1 
HETATM 9135 O O     . HOH I 5 .   ? -0.439 2.999   -7.864  1.00 28.06 ? 771  HOH B O     1 
HETATM 9136 O O     . HOH I 5 .   ? 7.418  -9.198  -35.294 1.00 26.33 ? 772  HOH B O     1 
HETATM 9137 O O     . HOH I 5 .   ? 20.704 -17.269 -26.896 1.00 22.92 ? 773  HOH B O     1 
HETATM 9138 O O     . HOH I 5 .   ? 20.354 -16.556 -4.872  1.00 31.48 ? 774  HOH B O     1 
HETATM 9139 O O     . HOH I 5 .   ? 47.922 -21.399 -17.232 1.00 33.07 ? 775  HOH B O     1 
HETATM 9140 O O     . HOH I 5 .   ? 8.683  -2.832  -36.126 1.00 27.43 ? 776  HOH B O     1 
HETATM 9141 O O     . HOH I 5 .   ? 17.284 14.276  -21.792 1.00 43.64 ? 777  HOH B O     1 
HETATM 9142 O O     . HOH I 5 .   ? 29.703 -9.085  -25.204 1.00 24.98 ? 778  HOH B O     1 
HETATM 9143 O O     . HOH I 5 .   ? 36.111 -20.742 -18.206 1.00 34.97 ? 779  HOH B O     1 
HETATM 9144 O O     . HOH I 5 .   ? 31.868 18.189  2.611   1.00 37.18 ? 780  HOH B O     1 
HETATM 9145 O O     . HOH I 5 .   ? -4.021 -20.939 -14.786 1.00 42.44 ? 781  HOH B O     1 
HETATM 9146 O O     . HOH I 5 .   ? 2.552  -11.748 -6.188  1.00 36.21 ? 782  HOH B O     1 
HETATM 9147 O O     . HOH I 5 .   ? 21.038 12.868  -23.799 1.00 34.76 ? 783  HOH B O     1 
HETATM 9148 O O     . HOH I 5 .   ? 3.560  -17.554 -32.240 1.00 30.67 ? 784  HOH B O     1 
HETATM 9149 O O     . HOH I 5 .   ? 10.301 8.602   -32.244 1.00 39.85 ? 785  HOH B O     1 
HETATM 9150 O O     . HOH I 5 .   ? 33.272 -17.717 -34.663 1.00 25.68 ? 786  HOH B O     1 
HETATM 9151 O O     . HOH I 5 .   ? 36.636 -32.503 -22.160 1.00 37.42 ? 787  HOH B O     1 
HETATM 9152 O O     . HOH I 5 .   ? 30.027 8.643   3.957   1.00 40.60 ? 788  HOH B O     1 
HETATM 9153 O O     . HOH I 5 .   ? 17.446 -7.529  -9.690  1.00 41.16 ? 789  HOH B O     1 
HETATM 9154 O O     . HOH I 5 .   ? 35.096 3.514   3.108   1.00 45.31 ? 790  HOH B O     1 
HETATM 9155 O O     . HOH I 5 .   ? 4.357  -10.601 -47.284 1.00 33.66 ? 791  HOH B O     1 
HETATM 9156 O O     . HOH I 5 .   ? 1.703  -6.645  -0.525  1.00 27.11 ? 792  HOH B O     1 
HETATM 9157 O O     . HOH I 5 .   ? 35.391 -24.230 -26.486 1.00 23.49 ? 793  HOH B O     1 
HETATM 9158 O O     . HOH I 5 .   ? 4.369  -14.270 -53.276 1.00 26.52 ? 794  HOH B O     1 
HETATM 9159 O O     . HOH I 5 .   ? 24.458 2.229   1.826   1.00 32.90 ? 795  HOH B O     1 
HETATM 9160 O O     . HOH I 5 .   ? 18.128 -15.298 -29.068 1.00 25.27 ? 796  HOH B O     1 
HETATM 9161 O O     . HOH I 5 .   ? -0.726 7.398   -20.396 1.00 32.29 ? 797  HOH B O     1 
HETATM 9162 O O     . HOH I 5 .   ? 28.079 -20.533 -37.815 1.00 28.21 ? 798  HOH B O     1 
HETATM 9163 O O     . HOH I 5 .   ? 4.921  -20.214 -28.759 1.00 26.48 ? 799  HOH B O     1 
HETATM 9164 O O     . HOH I 5 .   ? 33.492 -29.454 -30.329 1.00 30.00 ? 800  HOH B O     1 
HETATM 9165 O O     . HOH I 5 .   ? -4.468 -1.422  -22.035 1.00 32.07 ? 801  HOH B O     1 
HETATM 9166 O O     . HOH I 5 .   ? 46.712 -14.829 -14.327 1.00 37.47 ? 802  HOH B O     1 
HETATM 9167 O O     . HOH I 5 .   ? 19.000 -28.558 1.057   1.00 46.54 ? 803  HOH B O     1 
HETATM 9168 O O     . HOH I 5 .   ? 8.738  -15.841 -24.690 1.00 25.04 ? 804  HOH B O     1 
HETATM 9169 O O     . HOH I 5 .   ? 12.733 -4.257  14.156  1.00 48.34 ? 805  HOH B O     1 
HETATM 9170 O O     . HOH I 5 .   ? 11.987 -8.966  -5.838  1.00 27.66 ? 806  HOH B O     1 
HETATM 9171 O O     . HOH I 5 .   ? 24.957 -27.459 -10.771 1.00 31.04 ? 807  HOH B O     1 
HETATM 9172 O O     . HOH I 5 .   ? 36.983 -19.692 -13.309 1.00 33.02 ? 808  HOH B O     1 
HETATM 9173 O O     . HOH I 5 .   ? 10.242 0.454   -18.958 1.00 22.21 ? 809  HOH B O     1 
HETATM 9174 O O     . HOH I 5 .   ? 10.200 -18.113 -1.618  1.00 40.74 ? 810  HOH B O     1 
HETATM 9175 O O     . HOH I 5 .   ? 5.243  -19.628 -61.311 1.00 29.81 ? 811  HOH B O     1 
HETATM 9176 O O     . HOH I 5 .   ? 8.723  -22.980 -28.262 1.00 29.19 ? 812  HOH B O     1 
HETATM 9177 O O     . HOH I 5 .   ? 1.005  -21.039 -24.947 1.00 26.03 ? 813  HOH B O     1 
HETATM 9178 O O     . HOH I 5 .   ? 41.758 -26.316 -29.186 1.00 40.85 ? 814  HOH B O     1 
HETATM 9179 O O     . HOH I 5 .   ? 29.797 1.907   7.418   1.00 42.34 ? 815  HOH B O     1 
HETATM 9180 O O     . HOH I 5 .   ? 4.022  21.234  4.923   1.00 44.64 ? 816  HOH B O     1 
HETATM 9181 O O     . HOH I 5 .   ? 10.335 0.458   -28.695 1.00 23.14 ? 817  HOH B O     1 
HETATM 9182 O O     . HOH I 5 .   ? 13.515 -9.144  -35.445 1.00 20.58 ? 818  HOH B O     1 
HETATM 9183 O O     . HOH I 5 .   ? 43.074 -11.563 -26.622 1.00 25.01 ? 819  HOH B O     1 
HETATM 9184 O O     . HOH I 5 .   ? 4.345  8.159   -10.447 1.00 44.91 ? 820  HOH B O     1 
HETATM 9185 O O     . HOH I 5 .   ? 16.167 -17.405 -6.026  1.00 32.30 ? 821  HOH B O     1 
HETATM 9186 O O     . HOH I 5 .   ? 6.426  -1.528  -11.215 1.00 24.79 ? 822  HOH B O     1 
HETATM 9187 O O     . HOH I 5 .   ? 9.280  -10.965 -48.023 1.00 23.61 ? 823  HOH B O     1 
HETATM 9188 O O     . HOH I 5 .   ? -2.012 -19.828 -21.164 1.00 29.17 ? 824  HOH B O     1 
HETATM 9189 O O     . HOH I 5 .   ? 1.727  -3.592  -36.760 1.00 35.66 ? 825  HOH B O     1 
HETATM 9190 O O     . HOH I 5 .   ? 7.504  6.970   -31.056 1.00 41.15 ? 826  HOH B O     1 
HETATM 9191 O O     . HOH I 5 .   ? -1.358 -6.662  -6.393  1.00 37.54 ? 827  HOH B O     1 
HETATM 9192 O O     . HOH I 5 .   ? 14.201 -18.705 -17.914 1.00 41.40 ? 828  HOH B O     1 
HETATM 9193 O O     . HOH I 5 .   ? -4.055 -3.880  -23.843 1.00 32.35 ? 829  HOH B O     1 
HETATM 9194 O O     . HOH I 5 .   ? 14.051 -3.192  -15.570 1.00 29.66 ? 830  HOH B O     1 
HETATM 9195 O O     . HOH I 5 .   ? 17.895 10.632  -19.092 1.00 28.86 ? 831  HOH B O     1 
HETATM 9196 O O     . HOH I 5 .   ? 33.922 -5.658  -15.046 1.00 34.72 ? 832  HOH B O     1 
HETATM 9197 O O     . HOH I 5 .   ? 9.234  4.250   -33.881 1.00 31.98 ? 833  HOH B O     1 
HETATM 9198 O O     . HOH I 5 .   ? -0.637 2.275   -27.184 1.00 37.77 ? 834  HOH B O     1 
HETATM 9199 O O     . HOH I 5 .   ? 3.510  2.510   4.317   1.00 36.13 ? 835  HOH B O     1 
HETATM 9200 O O     . HOH I 5 .   ? 13.920 -10.459 -17.456 1.00 39.49 ? 836  HOH B O     1 
HETATM 9201 O O     . HOH I 5 .   ? 41.329 -22.008 -32.809 1.00 39.62 ? 837  HOH B O     1 
HETATM 9202 O O     . HOH I 5 .   ? 26.937 -32.123 -0.417  1.00 42.92 ? 838  HOH B O     1 
HETATM 9203 O O     . HOH I 5 .   ? 13.840 16.597  7.520   1.00 43.19 ? 839  HOH B O     1 
HETATM 9204 O O     . HOH I 5 .   ? 16.075 -42.054 -29.163 1.00 42.56 ? 840  HOH B O     1 
HETATM 9205 O O     . HOH I 5 .   ? 1.787  -7.417  -8.553  1.00 30.56 ? 841  HOH B O     1 
HETATM 9206 O O     . HOH I 5 .   ? 25.145 14.770  -11.351 1.00 41.46 ? 842  HOH B O     1 
HETATM 9207 O O     . HOH I 5 .   ? 39.689 -1.689  -18.728 1.00 28.24 ? 843  HOH B O     1 
HETATM 9208 O O     . HOH I 5 .   ? 12.750 -22.031 -19.267 1.00 33.68 ? 844  HOH B O     1 
HETATM 9209 O O     . HOH I 5 .   ? 16.812 18.051  -18.723 1.00 32.77 ? 845  HOH B O     1 
HETATM 9210 O O     . HOH I 5 .   ? 10.214 -15.003 4.199   1.00 46.92 ? 846  HOH B O     1 
HETATM 9211 O O     . HOH I 5 .   ? 46.665 -0.077  -20.408 1.00 31.15 ? 847  HOH B O     1 
HETATM 9212 O O     . HOH I 5 .   ? 27.737 -6.332  -27.168 1.00 23.24 ? 848  HOH B O     1 
HETATM 9213 O O     . HOH I 5 .   ? -1.046 1.666   -10.149 1.00 29.96 ? 849  HOH B O     1 
HETATM 9214 O O     . HOH I 5 .   ? 26.877 -33.801 -32.647 1.00 31.39 ? 850  HOH B O     1 
HETATM 9215 O O     . HOH I 5 .   ? 19.336 -15.062 -26.525 1.00 19.91 ? 851  HOH B O     1 
HETATM 9216 O O     . HOH I 5 .   ? 8.139  14.518  -6.295  1.00 33.27 ? 852  HOH B O     1 
HETATM 9217 O O     . HOH I 5 .   ? 36.180 -5.708  -21.758 1.00 21.44 ? 853  HOH B O     1 
HETATM 9218 O O     . HOH I 5 .   ? 1.264  -19.717 -48.351 1.00 44.08 ? 854  HOH B O     1 
HETATM 9219 O O     . HOH I 5 .   ? 19.263 -34.393 -19.423 1.00 34.46 ? 855  HOH B O     1 
HETATM 9220 O O     . HOH I 5 .   ? 47.250 -9.233  -31.336 1.00 25.08 ? 856  HOH B O     1 
HETATM 9221 O O     . HOH I 5 .   ? 6.110  21.048  -20.884 1.00 43.21 ? 857  HOH B O     1 
HETATM 9222 O O     . HOH I 5 .   ? 15.560 2.910   -12.786 1.00 24.78 ? 858  HOH B O     1 
HETATM 9223 O O     . HOH I 5 .   ? -1.815 1.910   -13.492 1.00 36.49 ? 859  HOH B O     1 
HETATM 9224 O O     . HOH I 5 .   ? 4.697  -12.949 -39.029 1.00 28.17 ? 860  HOH B O     1 
HETATM 9225 O O     . HOH I 5 .   ? 13.362 -25.603 -58.659 1.00 46.88 ? 861  HOH B O     1 
HETATM 9226 O O     . HOH I 5 .   ? 15.629 -37.858 -34.254 1.00 39.31 ? 862  HOH B O     1 
HETATM 9227 O O     . HOH I 5 .   ? 9.856  -5.148  -39.348 1.00 23.62 ? 863  HOH B O     1 
HETATM 9228 O O     . HOH I 5 .   ? 15.372 18.391  8.230   1.00 36.64 ? 864  HOH B O     1 
HETATM 9229 O O     . HOH I 5 .   ? 17.977 -39.958 -32.806 1.00 39.38 ? 865  HOH B O     1 
HETATM 9230 O O     . HOH I 5 .   ? 33.977 -27.966 -34.003 1.00 40.60 ? 866  HOH B O     1 
HETATM 9231 O O     . HOH I 5 .   ? -4.457 -14.439 -23.905 1.00 34.02 ? 867  HOH B O     1 
HETATM 9232 O O     . HOH I 5 .   ? 49.097 -17.463 -28.550 1.00 39.20 ? 868  HOH B O     1 
HETATM 9233 O O     . HOH I 5 .   ? 29.424 14.900  -3.470  1.00 43.30 ? 869  HOH B O     1 
HETATM 9234 O O     . HOH I 5 .   ? 9.681  10.313  -9.408  1.00 23.45 ? 870  HOH B O     1 
HETATM 9235 O O     . HOH I 5 .   ? 23.622 -1.239  -27.501 1.00 30.05 ? 871  HOH B O     1 
HETATM 9236 O O     . HOH I 5 .   ? 23.309 -19.726 -46.597 1.00 21.76 ? 872  HOH B O     1 
HETATM 9237 O O     . HOH I 5 .   ? 21.620 6.700   9.204   1.00 38.00 ? 873  HOH B O     1 
HETATM 9238 O O     . HOH I 5 .   ? 5.987  -0.849  -26.596 1.00 23.30 ? 874  HOH B O     1 
HETATM 9239 O O     . HOH I 5 .   ? 15.252 4.475   -33.699 1.00 28.96 ? 875  HOH B O     1 
HETATM 9240 O O     . HOH I 5 .   ? -4.304 5.054   -21.409 1.00 40.41 ? 876  HOH B O     1 
HETATM 9241 O O     . HOH I 5 .   ? 13.420 -27.573 -50.010 1.00 28.77 ? 877  HOH B O     1 
HETATM 9242 O O     . HOH I 5 .   ? 1.358  -8.262  -2.866  1.00 46.90 ? 878  HOH B O     1 
HETATM 9243 O O     . HOH I 5 .   ? 7.550  -8.247  -52.325 1.00 23.47 ? 879  HOH B O     1 
HETATM 9244 O O     . HOH I 5 .   ? 49.879 -9.738  -26.940 1.00 38.85 ? 880  HOH B O     1 
HETATM 9245 O O     . HOH I 5 .   ? 10.086 -8.193  -27.084 1.00 25.26 ? 881  HOH B O     1 
HETATM 9246 O O     . HOH I 5 .   ? 2.590  -13.391 -40.278 1.00 36.50 ? 882  HOH B O     1 
HETATM 9247 O O     . HOH I 5 .   ? 18.081 7.358   7.280   1.00 29.97 ? 883  HOH B O     1 
HETATM 9248 O O     . HOH I 5 .   ? 8.459  0.811   -12.966 1.00 31.56 ? 884  HOH B O     1 
HETATM 9249 O O     . HOH I 5 .   ? 10.414 18.632  -13.350 1.00 49.52 ? 885  HOH B O     1 
HETATM 9250 O O     . HOH I 5 .   ? 49.831 -18.283 -22.505 1.00 30.61 ? 886  HOH B O     1 
HETATM 9251 O O     . HOH I 5 .   ? 28.782 -0.295  -17.906 1.00 26.89 ? 887  HOH B O     1 
HETATM 9252 O O     . HOH I 5 .   ? 15.592 3.204   8.999   1.00 33.16 ? 888  HOH B O     1 
HETATM 9253 O O     . HOH I 5 .   ? 21.203 17.848  -0.040  1.00 32.41 ? 889  HOH B O     1 
HETATM 9254 O O     . HOH I 5 .   ? 40.263 -28.508 -15.480 1.00 50.89 ? 890  HOH B O     1 
HETATM 9255 O O     . HOH I 5 .   ? 17.822 -5.904  -43.508 1.00 26.68 ? 891  HOH B O     1 
HETATM 9256 O O     . HOH I 5 .   ? 23.058 -34.777 -15.435 1.00 46.58 ? 892  HOH B O     1 
HETATM 9257 O O     . HOH I 5 .   ? 37.744 -23.277 -18.431 1.00 31.02 ? 893  HOH B O     1 
HETATM 9258 O O     . HOH I 5 .   ? 4.720  -18.473 -34.597 1.00 27.33 ? 894  HOH B O     1 
HETATM 9259 O O     . HOH I 5 .   ? 39.854 -24.029 -31.315 1.00 31.64 ? 895  HOH B O     1 
HETATM 9260 O O     . HOH I 5 .   ? 17.575 -25.673 -58.765 1.00 48.87 ? 896  HOH B O     1 
HETATM 9261 O O     . HOH I 5 .   ? 17.491 12.564  -25.898 1.00 25.23 ? 897  HOH B O     1 
HETATM 9262 O O     . HOH I 5 .   ? 20.535 11.599  9.434   1.00 44.60 ? 898  HOH B O     1 
HETATM 9263 O O     . HOH I 5 .   ? 13.758 -13.526 0.641   1.00 48.02 ? 899  HOH B O     1 
HETATM 9264 O O     . HOH I 5 .   ? 14.942 -25.073 -24.976 1.00 25.80 ? 900  HOH B O     1 
HETATM 9265 O O     . HOH I 5 .   ? 30.096 -30.454 -33.470 1.00 28.77 ? 901  HOH B O     1 
HETATM 9266 O O     . HOH I 5 .   ? 29.710 -11.558 -8.890  1.00 45.14 ? 902  HOH B O     1 
HETATM 9267 O O     . HOH I 5 .   ? 0.299  -16.946 -24.497 1.00 27.40 ? 903  HOH B O     1 
HETATM 9268 O O     . HOH I 5 .   ? 25.112 -14.157 -38.388 1.00 35.61 ? 904  HOH B O     1 
HETATM 9269 O O     . HOH I 5 .   ? 12.166 18.955  -20.881 1.00 42.64 ? 905  HOH B O     1 
HETATM 9270 O O     . HOH I 5 .   ? 49.414 -5.006  -24.837 1.00 32.20 ? 906  HOH B O     1 
HETATM 9271 O O     . HOH I 5 .   ? 27.131 -33.926 -14.155 1.00 31.73 ? 907  HOH B O     1 
HETATM 9272 O O     . HOH I 5 .   ? 1.972  -5.013  -30.655 1.00 22.86 ? 908  HOH B O     1 
HETATM 9273 O O     . HOH I 5 .   ? 9.475  -23.632 -32.247 1.00 26.51 ? 909  HOH B O     1 
HETATM 9274 O O     . HOH I 5 .   ? 10.605 15.911  4.660   1.00 34.97 ? 910  HOH B O     1 
HETATM 9275 O O     . HOH I 5 .   ? 24.989 -32.937 -15.436 1.00 38.04 ? 911  HOH B O     1 
HETATM 9276 O O     . HOH I 5 .   ? 16.091 -3.015  11.501  1.00 38.86 ? 912  HOH B O     1 
HETATM 9277 O O     . HOH I 5 .   ? 49.440 -5.398  -20.561 1.00 30.14 ? 913  HOH B O     1 
HETATM 9278 O O     . HOH I 5 .   ? 30.159 1.766   -1.719  1.00 34.75 ? 914  HOH B O     1 
HETATM 9279 O O     . HOH I 5 .   ? 18.763 -30.415 -12.275 1.00 51.40 ? 915  HOH B O     1 
HETATM 9280 O O     . HOH I 5 .   ? 4.839  -4.270  6.668   1.00 37.47 ? 916  HOH B O     1 
HETATM 9281 O O     . HOH I 5 .   ? 27.000 8.738   -18.049 1.00 27.28 ? 917  HOH B O     1 
HETATM 9282 O O     . HOH I 5 .   ? 41.959 -23.314 -27.191 1.00 37.17 ? 918  HOH B O     1 
HETATM 9283 O O     . HOH I 5 .   ? 21.201 -6.441  -3.282  1.00 31.55 ? 919  HOH B O     1 
HETATM 9284 O O     . HOH I 5 .   ? 8.965  -2.526  -26.330 1.00 21.43 ? 920  HOH B O     1 
HETATM 9285 O O     . HOH I 5 .   ? 8.213  0.678   -26.905 1.00 26.20 ? 921  HOH B O     1 
HETATM 9286 O O     . HOH I 5 .   ? 28.792 13.682  -13.614 1.00 39.28 ? 922  HOH B O     1 
HETATM 9287 O O     . HOH I 5 .   ? 8.070  9.002   3.284   1.00 37.97 ? 923  HOH B O     1 
HETATM 9288 O O     . HOH I 5 .   ? 13.623 -16.637 -4.753  1.00 46.46 ? 924  HOH B O     1 
HETATM 9289 O O     . HOH I 5 .   ? 3.894  -0.491  1.594   1.00 29.15 ? 925  HOH B O     1 
HETATM 9290 O O     . HOH I 5 .   ? 2.972  -15.051 3.775   1.00 39.89 ? 926  HOH B O     1 
HETATM 9291 O O     . HOH I 5 .   ? 49.881 4.598   -26.908 1.00 47.39 ? 927  HOH B O     1 
HETATM 9292 O O     . HOH I 5 .   ? 4.225  -31.858 -27.104 1.00 39.29 ? 928  HOH B O     1 
HETATM 9293 O O     . HOH I 5 .   ? 9.587  -5.730  -27.389 1.00 22.62 ? 929  HOH B O     1 
HETATM 9294 O O     . HOH I 5 .   ? 51.454 -3.500  -28.926 1.00 24.76 ? 930  HOH B O     1 
HETATM 9295 O O     . HOH I 5 .   ? 46.456 -0.136  -32.159 1.00 21.37 ? 931  HOH B O     1 
HETATM 9296 O O     . HOH I 5 .   ? 13.576 6.338   -34.117 1.00 27.96 ? 932  HOH B O     1 
HETATM 9297 O O     . HOH I 5 .   ? 31.389 -26.068 -2.046  1.00 39.83 ? 933  HOH B O     1 
HETATM 9298 O O     . HOH I 5 .   ? 4.564  11.702  -14.293 1.00 39.15 ? 934  HOH B O     1 
HETATM 9299 O O     . HOH I 5 .   ? 13.230 -20.632 -58.121 1.00 34.40 ? 935  HOH B O     1 
HETATM 9300 O O     . HOH I 5 .   ? 27.261 -4.903  -29.529 1.00 25.02 ? 936  HOH B O     1 
HETATM 9301 O O     . HOH I 5 .   ? 48.298 -19.962 -28.603 1.00 27.42 ? 937  HOH B O     1 
HETATM 9302 O O     . HOH I 5 .   ? 24.844 -32.590 -36.174 1.00 25.12 ? 938  HOH B O     1 
HETATM 9303 O O     . HOH I 5 .   ? 2.931  14.000  -19.829 1.00 40.08 ? 939  HOH B O     1 
HETATM 9304 O O     . HOH I 5 .   ? 17.101 -35.015 -36.431 1.00 29.42 ? 940  HOH B O     1 
HETATM 9305 O O     . HOH I 5 .   ? 18.478 0.747   6.113   1.00 29.49 ? 941  HOH B O     1 
HETATM 9306 O O     . HOH I 5 .   ? -0.870 9.142   9.009   1.00 54.33 ? 942  HOH B O     1 
HETATM 9307 O O     . HOH I 5 .   ? 6.838  -24.166 -26.525 1.00 29.13 ? 943  HOH B O     1 
HETATM 9308 O O     . HOH I 5 .   ? 26.815 -8.482  -8.118  1.00 39.87 ? 944  HOH B O     1 
HETATM 9309 O O     . HOH I 5 .   ? 24.101 -19.831 -39.385 1.00 29.29 ? 945  HOH B O     1 
HETATM 9310 O O     . HOH I 5 .   ? 26.134 2.802   8.540   1.00 34.55 ? 946  HOH B O     1 
HETATM 9311 O O     . HOH I 5 .   ? 11.078 10.286  -25.997 1.00 43.88 ? 947  HOH B O     1 
HETATM 9312 O O     . HOH I 5 .   ? 5.283  -23.930 -18.916 1.00 30.18 ? 948  HOH B O     1 
HETATM 9313 O O     . HOH I 5 .   ? 17.738 4.554   7.601   1.00 33.21 ? 949  HOH B O     1 
HETATM 9314 O O     . HOH I 5 .   ? 7.554  6.115   -34.441 1.00 37.92 ? 950  HOH B O     1 
HETATM 9315 O O     . HOH I 5 .   ? 23.068 -7.495  -1.670  1.00 44.30 ? 951  HOH B O     1 
HETATM 9316 O O     . HOH I 5 .   ? 12.643 8.163   -22.723 1.00 23.10 ? 952  HOH B O     1 
HETATM 9317 O O     . HOH I 5 .   ? 12.568 -19.806 -30.737 1.00 29.66 ? 953  HOH B O     1 
HETATM 9318 O O     . HOH I 5 .   ? 47.863 6.624   -27.046 1.00 27.70 ? 954  HOH B O     1 
HETATM 9319 O O     . HOH I 5 .   ? 37.326 -14.704 -34.605 1.00 27.44 ? 955  HOH B O     1 
HETATM 9320 O O     . HOH I 5 .   ? 37.593 -10.079 -27.222 1.00 24.54 ? 956  HOH B O     1 
HETATM 9321 O O     . HOH I 5 .   ? -7.477 -6.737  -12.877 1.00 45.45 ? 957  HOH B O     1 
HETATM 9322 O O     . HOH I 5 .   ? 20.268 0.373   7.575   1.00 44.37 ? 958  HOH B O     1 
HETATM 9323 O O     . HOH I 5 .   ? 7.324  14.924  -24.900 1.00 40.60 ? 959  HOH B O     1 
HETATM 9324 O O     . HOH I 5 .   ? 29.599 -8.882  -29.395 1.00 35.53 ? 960  HOH B O     1 
HETATM 9325 O O     . HOH I 5 .   ? 13.446 18.847  -12.494 1.00 36.91 ? 961  HOH B O     1 
HETATM 9326 O O     . HOH I 5 .   ? 19.388 -20.527 -50.154 1.00 19.27 ? 962  HOH B O     1 
HETATM 9327 O O     . HOH I 5 .   ? 36.570 -32.596 -8.748  1.00 47.62 ? 963  HOH B O     1 
HETATM 9328 O O     . HOH I 5 .   ? 30.162 -3.419  -24.660 1.00 24.19 ? 964  HOH B O     1 
HETATM 9329 O O     . HOH I 5 .   ? 41.160 10.632  -36.527 1.00 33.41 ? 965  HOH B O     1 
HETATM 9330 O O     . HOH I 5 .   ? 4.428  -25.738 -41.451 1.00 37.80 ? 966  HOH B O     1 
HETATM 9331 O O     . HOH I 5 .   ? 25.171 -15.495 -40.799 1.00 32.19 ? 967  HOH B O     1 
HETATM 9332 O O     . HOH I 5 .   ? 23.729 -39.826 -19.093 1.00 37.83 ? 968  HOH B O     1 
HETATM 9333 O O     . HOH I 5 .   ? 8.455  -6.652  -6.573  1.00 31.69 ? 969  HOH B O     1 
HETATM 9334 O O     . HOH I 5 .   ? -3.608 -12.413 -14.315 1.00 36.50 ? 970  HOH B O     1 
HETATM 9335 O O     . HOH I 5 .   ? 7.147  -8.839  -13.392 1.00 45.67 ? 971  HOH B O     1 
HETATM 9336 O O     . HOH I 5 .   ? -0.138 -19.047 -56.155 1.00 39.55 ? 972  HOH B O     1 
HETATM 9337 O O     . HOH I 5 .   ? 7.375  -27.050 -32.987 1.00 44.04 ? 973  HOH B O     1 
HETATM 9338 O O     . HOH I 5 .   ? 48.508 -22.374 -25.045 1.00 51.20 ? 974  HOH B O     1 
HETATM 9339 O O     . HOH I 5 .   ? 25.037 -1.414  2.625   1.00 33.00 ? 975  HOH B O     1 
HETATM 9340 O O     . HOH I 5 .   ? 7.439  -25.795 -14.346 1.00 36.46 ? 976  HOH B O     1 
HETATM 9341 O O     . HOH I 5 .   ? 49.376 -0.038  -22.869 1.00 38.15 ? 977  HOH B O     1 
HETATM 9342 O O     . HOH I 5 .   ? 10.553 -27.046 -46.475 1.00 25.92 ? 978  HOH B O     1 
HETATM 9343 O O     . HOH I 5 .   ? 19.301 19.481  -8.423  1.00 47.41 ? 979  HOH B O     1 
HETATM 9344 O O     . HOH I 5 .   ? 16.351 14.460  -24.312 1.00 47.08 ? 980  HOH B O     1 
HETATM 9345 O O     . HOH I 5 .   ? 24.688 16.402  -9.708  1.00 47.10 ? 981  HOH B O     1 
HETATM 9346 O O     . HOH I 5 .   ? 32.619 8.088   6.332   1.00 46.63 ? 982  HOH B O     1 
HETATM 9347 O O     . HOH I 5 .   ? 8.835  -10.463 -8.765  1.00 34.06 ? 983  HOH B O     1 
HETATM 9348 O O     . HOH I 5 .   ? 3.302  -24.141 -25.713 1.00 30.01 ? 984  HOH B O     1 
HETATM 9349 O O     . HOH I 5 .   ? 25.647 -26.519 -6.062  1.00 38.59 ? 985  HOH B O     1 
HETATM 9350 O O     . HOH I 5 .   ? 30.184 -0.778  -1.255  1.00 30.60 ? 986  HOH B O     1 
HETATM 9351 O O     . HOH I 5 .   ? 3.234  -14.849 -50.403 1.00 32.78 ? 987  HOH B O     1 
HETATM 9352 O O     . HOH I 5 .   ? 16.460 -37.191 -18.966 1.00 42.18 ? 988  HOH B O     1 
HETATM 9353 O O     . HOH I 5 .   ? 20.905 -12.353 -41.426 1.00 25.79 ? 989  HOH B O     1 
HETATM 9354 O O     . HOH I 5 .   ? 25.405 -21.852 -40.404 1.00 29.34 ? 990  HOH B O     1 
HETATM 9355 O O     . HOH I 5 .   ? -3.042 8.072   -0.396  1.00 39.01 ? 991  HOH B O     1 
HETATM 9356 O O     . HOH I 5 .   ? 3.042  -20.687 -38.445 1.00 38.15 ? 992  HOH B O     1 
HETATM 9357 O O     . HOH I 5 .   ? 10.535 6.573   5.610   1.00 38.16 ? 993  HOH B O     1 
HETATM 9358 O O     . HOH I 5 .   ? 7.395  -24.384 -16.836 1.00 36.30 ? 994  HOH B O     1 
HETATM 9359 O O     . HOH I 5 .   ? 20.024 -2.188  7.903   1.00 46.07 ? 995  HOH B O     1 
HETATM 9360 O O     . HOH I 5 .   ? 7.068  -26.538 -28.343 1.00 42.76 ? 996  HOH B O     1 
HETATM 9361 O O     . HOH I 5 .   ? 2.365  -0.918  -36.496 1.00 28.03 ? 997  HOH B O     1 
HETATM 9362 O O     . HOH I 5 .   ? 11.754 15.780  -22.528 1.00 32.38 ? 998  HOH B O     1 
HETATM 9363 O O     . HOH I 5 .   ? 23.267 -41.497 -21.145 1.00 43.95 ? 999  HOH B O     1 
HETATM 9364 O O     . HOH I 5 .   ? 23.080 -13.950 -42.538 1.00 25.33 ? 1000 HOH B O     1 
HETATM 9365 O O     . HOH I 5 .   ? 23.754 1.560   9.062   1.00 47.93 ? 1001 HOH B O     1 
HETATM 9366 O O     . HOH I 5 .   ? 17.008 18.446  -16.221 1.00 38.25 ? 1002 HOH B O     1 
HETATM 9367 O O     . HOH I 5 .   ? 13.518 4.782   9.150   1.00 48.17 ? 1003 HOH B O     1 
HETATM 9368 O O     . HOH I 5 .   ? 15.009 -6.067  -43.545 1.00 25.40 ? 1004 HOH B O     1 
HETATM 9369 O O     . HOH I 5 .   ? -7.923 -2.890  -13.503 1.00 48.90 ? 1005 HOH B O     1 
HETATM 9370 O O     . HOH I 5 .   ? 18.875 19.087  10.664  1.00 41.57 ? 1006 HOH B O     1 
HETATM 9371 O O     . HOH I 5 .   ? 49.479 2.090   -27.548 1.00 45.39 ? 1007 HOH B O     1 
HETATM 9372 O O     . HOH I 5 .   ? 30.315 9.212   6.557   1.00 38.62 ? 1008 HOH B O     1 
HETATM 9373 O O     . HOH I 5 .   ? 22.746 -45.773 -26.202 1.00 45.80 ? 1009 HOH B O     1 
HETATM 9374 O O     . HOH I 5 .   ? 31.191 -1.301  -13.484 1.00 46.77 ? 1010 HOH B O     1 
HETATM 9375 O O     . HOH I 5 .   ? -2.137 -20.565 -57.556 1.00 50.67 ? 1011 HOH B O     1 
HETATM 9376 O O     . HOH I 5 .   ? 2.566  -19.283 -36.065 1.00 43.16 ? 1012 HOH B O     1 
HETATM 9377 O O     . HOH I 5 .   ? 51.491 9.209   -32.619 1.00 47.98 ? 1013 HOH B O     1 
HETATM 9378 O O     . HOH I 5 .   ? 42.263 -22.965 -29.673 1.00 43.19 ? 1014 HOH B O     1 
HETATM 9379 O O     . HOH I 5 .   ? 2.919  -12.237 -49.054 1.00 46.52 ? 1015 HOH B O     1 
HETATM 9380 O O     . HOH I 5 .   ? 2.698  -2.787  -43.815 1.00 47.52 ? 1016 HOH B O     1 
HETATM 9381 O O     . HOH I 5 .   ? 25.181 -26.770 6.266   1.00 47.58 ? 1017 HOH B O     1 
HETATM 9382 O O     . HOH I 5 .   ? 21.062 0.599   -13.752 1.00 53.51 ? 1018 HOH B O     1 
HETATM 9383 O O     . HOH I 5 .   ? 26.243 12.660  -20.361 1.00 40.55 ? 1019 HOH B O     1 
HETATM 9384 O O     . HOH I 5 .   ? 49.141 -10.516 -32.679 1.00 31.63 ? 1020 HOH B O     1 
HETATM 9385 O O     . HOH I 5 .   ? 14.336 -0.785  12.114  1.00 34.90 ? 1021 HOH B O     1 
HETATM 9386 O O     . HOH I 5 .   ? 14.282 -44.669 -22.207 1.00 47.81 ? 1022 HOH B O     1 
HETATM 9387 O O     . HOH I 5 .   ? 26.920 -7.540  -30.808 1.00 28.03 ? 1023 HOH B O     1 
HETATM 9388 O O     . HOH I 5 .   ? -1.567 -3.373  -42.988 1.00 40.05 ? 1024 HOH B O     1 
HETATM 9389 O O     . HOH I 5 .   ? 48.371 -16.969 -31.937 1.00 41.94 ? 1025 HOH B O     1 
HETATM 9390 O O     . HOH I 5 .   ? 33.789 -34.510 -31.682 1.00 38.63 ? 1026 HOH B O     1 
HETATM 9391 O O     . HOH I 5 .   ? 4.576  14.077  -11.870 1.00 47.73 ? 1027 HOH B O     1 
HETATM 9392 O O     . HOH I 5 .   ? 9.347  -8.989  -6.349  1.00 34.25 ? 1028 HOH B O     1 
HETATM 9393 O O     . HOH I 5 .   ? 37.755 -34.238 -26.455 1.00 45.59 ? 1029 HOH B O     1 
HETATM 9394 O O     . HOH I 5 .   ? 0.969  0.463   -34.169 1.00 39.45 ? 1030 HOH B O     1 
HETATM 9395 O O     . HOH I 5 .   ? 15.505 -13.812 -3.998  1.00 51.96 ? 1031 HOH B O     1 
HETATM 9396 O O     . HOH I 5 .   ? 26.723 -36.433 -14.310 1.00 40.73 ? 1032 HOH B O     1 
HETATM 9397 O O     . HOH I 5 .   ? 27.283 -10.584 -4.472  1.00 47.81 ? 1033 HOH B O     1 
HETATM 9398 O O     . HOH I 5 .   ? 43.180 -21.502 -31.287 1.00 42.92 ? 1034 HOH B O     1 
HETATM 9399 O O     . HOH I 5 .   ? 50.555 -6.792  -22.622 1.00 45.90 ? 1035 HOH B O     1 
HETATM 9400 O O     . HOH I 5 .   ? 33.090 -27.424 -5.919  1.00 34.30 ? 1036 HOH B O     1 
HETATM 9401 O O     . HOH I 5 .   ? 12.560 -15.801 1.180   1.00 46.31 ? 1037 HOH B O     1 
HETATM 9402 O O     . HOH I 5 .   ? 17.783 -13.025 -2.763  1.00 50.07 ? 1038 HOH B O     1 
HETATM 9403 O O     . HOH I 5 .   ? 34.632 -27.887 -36.528 1.00 43.21 ? 1039 HOH B O     1 
HETATM 9404 O O     . HOH I 5 .   ? 4.430  -22.851 -27.908 1.00 36.60 ? 1040 HOH B O     1 
HETATM 9405 O O     . HOH I 5 .   ? 27.378 -32.396 -36.284 1.00 29.79 ? 1041 HOH B O     1 
HETATM 9406 O O     . HOH I 5 .   ? 5.915  0.551   -12.716 1.00 41.62 ? 1042 HOH B O     1 
HETATM 9407 O O     . HOH I 5 .   ? -2.769 1.143   -27.923 1.00 34.65 ? 1043 HOH B O     1 
HETATM 9408 O O     . HOH I 5 .   ? 36.137 -28.759 -30.653 1.00 37.17 ? 1044 HOH B O     1 
HETATM 9409 O O     . HOH I 5 .   ? 11.199 -15.154 -1.234  1.00 51.49 ? 1045 HOH B O     1 
HETATM 9410 O O     . HOH I 5 .   ? -3.133 -4.826  -41.626 1.00 38.05 ? 1046 HOH B O     1 
HETATM 9411 O O     . HOH I 5 .   ? 37.151 -26.964 -37.154 1.00 40.12 ? 1047 HOH B O     1 
HETATM 9412 O O     . HOH I 5 .   ? 32.020 18.811  5.083   1.00 45.33 ? 1048 HOH B O     1 
HETATM 9413 O O     . HOH I 5 .   ? -3.103 -25.119 -15.195 1.00 49.22 ? 1049 HOH B O     1 
HETATM 9414 O O     . HOH I 5 .   ? 17.164 -36.834 -38.214 1.00 38.58 ? 1050 HOH B O     1 
HETATM 9415 O O     . HOH I 5 .   ? 0.066  -19.175 -22.870 1.00 37.13 ? 1051 HOH B O     1 
HETATM 9416 O O     . HOH I 5 .   ? 11.118 -11.309 -9.478  1.00 47.35 ? 1052 HOH B O     1 
HETATM 9417 O O     . HOH I 5 .   ? 2.550  -24.501 -50.299 1.00 44.66 ? 1053 HOH B O     1 
HETATM 9418 O O     . HOH I 5 .   ? 40.236 -3.842  -19.850 1.00 26.22 ? 1054 HOH B O     1 
HETATM 9419 O O     . HOH I 5 .   ? -1.828 -17.153 -26.163 1.00 32.36 ? 1055 HOH B O     1 
HETATM 9420 O O     . HOH I 5 .   ? 13.075 -11.021 -7.617  1.00 39.56 ? 1056 HOH B O     1 
HETATM 9421 O O     . HOH I 5 .   ? 27.671 -11.625 -31.558 1.00 46.85 ? 1057 HOH B O     1 
HETATM 9422 O O     . HOH I 5 .   ? 30.472 -6.746  -26.602 1.00 27.17 ? 1058 HOH B O     1 
HETATM 9423 O O     . HOH I 5 .   ? 18.682 -43.571 -26.799 1.00 42.03 ? 1059 HOH B O     1 
HETATM 9424 O O     . HOH I 5 .   ? 31.119 -15.827 -33.905 1.00 36.87 ? 1060 HOH B O     1 
HETATM 9425 O O     . HOH I 5 .   ? 41.787 -5.554  -16.334 1.00 36.83 ? 1061 HOH B O     1 
HETATM 9426 O O     . HOH I 5 .   ? 2.684  -24.190 -43.489 1.00 43.31 ? 1062 HOH B O     1 
HETATM 9427 O O     . HOH I 5 .   ? 34.805 -15.495 -35.309 1.00 25.31 ? 1063 HOH B O     1 
HETATM 9428 O O     . HOH I 5 .   ? 1.329  -21.976 -42.593 1.00 48.18 ? 1064 HOH B O     1 
HETATM 9429 O O     . HOH I 5 .   ? 28.883 -32.715 -34.036 1.00 29.58 ? 1065 HOH B O     1 
HETATM 9430 O O     . HOH I 5 .   ? 50.102 -20.810 -22.902 1.00 41.73 ? 1066 HOH B O     1 
HETATM 9431 O O     . HOH I 5 .   ? 22.766 -15.332 -5.327  1.00 44.79 ? 1067 HOH B O     1 
HETATM 9432 O O     . HOH I 5 .   ? 11.850 -28.904 -48.116 1.00 44.60 ? 1068 HOH B O     1 
HETATM 9433 O O     . HOH I 5 .   ? 16.183 20.032  -20.496 1.00 46.57 ? 1069 HOH B O     1 
HETATM 9434 O O     . HOH I 5 .   ? 0.227  2.890   -33.356 1.00 42.81 ? 1070 HOH B O     1 
HETATM 9435 O O     . HOH I 5 .   ? 1.906  -1.376  3.523   1.00 39.45 ? 1071 HOH B O     1 
HETATM 9436 O O     . HOH I 5 .   ? 9.899  -20.340 -60.642 1.00 40.11 ? 1072 HOH B O     1 
HETATM 9437 O O     . HOH I 5 .   ? -3.831 -16.733 -24.568 1.00 34.00 ? 1073 HOH B O     1 
HETATM 9438 O O     . HOH I 5 .   ? 33.978 -37.936 -24.986 1.00 48.03 ? 1074 HOH B O     1 
HETATM 9439 O O     . HOH I 5 .   ? 0.704  -23.461 -24.341 1.00 38.01 ? 1075 HOH B O     1 
HETATM 9440 O O     . HOH I 5 .   ? 3.842  -20.407 -31.497 1.00 33.10 ? 1076 HOH B O     1 
HETATM 9441 O O     . HOH I 5 .   ? 19.469 16.765  -21.910 1.00 47.53 ? 1077 HOH B O     1 
HETATM 9442 O O     . HOH I 5 .   ? -0.305 -8.401  -4.846  1.00 37.31 ? 1078 HOH B O     1 
HETATM 9443 O O     . HOH I 5 .   ? 20.099 -41.952 -31.452 1.00 34.73 ? 1079 HOH B O     1 
HETATM 9444 O O     . HOH I 5 .   ? 32.498 -29.720 -32.540 1.00 33.36 ? 1080 HOH B O     1 
HETATM 9445 O O     . HOH I 5 .   ? 45.216 -20.515 -32.311 1.00 47.57 ? 1081 HOH B O     1 
HETATM 9446 O O     . HOH I 5 .   ? 31.591 -28.555 -3.958  1.00 47.10 ? 1082 HOH B O     1 
HETATM 9447 O O     . HOH I 5 .   ? 28.523 -31.742 -38.906 1.00 31.69 ? 1083 HOH B O     1 
HETATM 9448 O O     . HOH I 5 .   ? -1.502 -17.353 -31.037 1.00 37.77 ? 1084 HOH B O     1 
HETATM 9449 O O     . HOH I 5 .   ? 19.878 19.847  1.623   1.00 41.97 ? 1085 HOH B O     1 
HETATM 9450 O O     . HOH I 5 .   ? 7.789  -21.182 -32.056 1.00 32.30 ? 1086 HOH B O     1 
HETATM 9451 O O     . HOH I 5 .   ? -3.492 7.134   -20.558 1.00 37.98 ? 1087 HOH B O     1 
HETATM 9452 O O     . HOH I 5 .   ? -5.703 -0.361  -24.412 1.00 42.07 ? 1088 HOH B O     1 
HETATM 9453 O O     . HOH I 5 .   ? 51.450 -4.367  -26.340 1.00 42.30 ? 1089 HOH B O     1 
HETATM 9454 O O     . HOH I 5 .   ? 9.982  13.370  6.276   1.00 51.55 ? 1090 HOH B O     1 
HETATM 9455 O O     . HOH I 5 .   ? 35.399 -35.386 -21.048 1.00 40.16 ? 1091 HOH B O     1 
HETATM 9456 O O     . HOH I 5 .   ? 18.500 -43.367 -29.817 1.00 38.41 ? 1092 HOH B O     1 
HETATM 9457 O O     . HOH I 5 .   ? 40.276 -23.902 -36.631 1.00 37.26 ? 1093 HOH B O     1 
HETATM 9458 O O     . HOH I 5 .   ? 5.672  -20.675 -33.442 1.00 28.69 ? 1094 HOH B O     1 
HETATM 9459 O O     . HOH I 5 .   ? 34.023 -32.205 -32.791 1.00 41.84 ? 1095 HOH B O     1 
HETATM 9460 O O     . HOH I 5 .   ? 4.461  -27.560 -28.923 1.00 46.80 ? 1096 HOH B O     1 
HETATM 9461 O O     . HOH I 5 .   ? 35.936 -37.187 -22.912 1.00 44.46 ? 1097 HOH B O     1 
HETATM 9462 O O     . HOH J 5 .   ? 43.030 -7.553  -61.867 1.00 38.75 ? 701  HOH A O     1 
HETATM 9463 O O     . HOH J 5 .   ? 56.065 9.283   -48.982 1.00 39.85 ? 702  HOH A O     1 
HETATM 9464 O O     . HOH J 5 .   ? 51.669 6.359   -60.203 1.00 40.45 ? 703  HOH A O     1 
HETATM 9465 O O     . HOH J 5 .   ? 48.076 8.532   -38.865 1.00 41.00 ? 704  HOH A O     1 
HETATM 9466 O O     . HOH J 5 .   ? 8.303  -19.179 -58.652 1.00 25.74 ? 705  HOH A O     1 
HETATM 9467 O O     . HOH J 5 .   ? 13.744 18.521  -40.860 1.00 42.61 ? 706  HOH A O     1 
HETATM 9468 O O     . HOH J 5 .   ? 52.499 -17.503 -55.003 1.00 31.70 ? 707  HOH A O     1 
HETATM 9469 O O     . HOH J 5 .   ? 60.376 4.771   -46.300 1.00 37.75 ? 708  HOH A O     1 
HETATM 9470 O O     . HOH J 5 .   ? -6.922 6.448   -63.467 1.00 42.02 ? 709  HOH A O     1 
HETATM 9471 O O     . HOH J 5 .   ? 32.285 -28.961 -40.360 1.00 32.33 ? 710  HOH A O     1 
HETATM 9472 O O     . HOH J 5 .   ? 49.036 3.028   -18.426 1.00 35.04 ? 711  HOH A O     1 
HETATM 9473 O O     . HOH J 5 .   ? 13.920 19.518  -61.834 1.00 24.88 ? 712  HOH A O     1 
HETATM 9474 O O     . HOH J 5 .   ? 22.059 21.780  -46.047 1.00 36.31 ? 713  HOH A O     1 
HETATM 9475 O O     . HOH J 5 .   ? 30.963 -26.808 -61.953 1.00 40.65 ? 714  HOH A O     1 
HETATM 9476 O O     . HOH J 5 .   ? 11.730 -34.662 -39.595 1.00 41.72 ? 715  HOH A O     1 
HETATM 9477 O O     . HOH J 5 .   ? -1.798 6.772   -70.536 1.00 30.80 ? 716  HOH A O     1 
HETATM 9478 O O     . HOH J 5 .   ? 54.948 -15.092 -49.025 1.00 47.14 ? 717  HOH A O     1 
HETATM 9479 O O     . HOH J 5 .   ? 13.953 -13.789 -72.326 1.00 36.16 ? 718  HOH A O     1 
HETATM 9480 O O     . HOH J 5 .   ? 26.720 -27.065 -48.549 1.00 24.41 ? 719  HOH A O     1 
HETATM 9481 O O     . HOH J 5 .   ? 12.486 -10.471 -77.916 1.00 38.31 ? 720  HOH A O     1 
HETATM 9482 O O     . HOH J 5 .   ? 1.780  11.394  -63.019 1.00 31.33 ? 721  HOH A O     1 
HETATM 9483 O O     . HOH J 5 .   ? 7.561  -2.340  -79.046 1.00 35.41 ? 722  HOH A O     1 
HETATM 9484 O O     . HOH J 5 .   ? 26.661 -8.241  -40.340 1.00 28.39 ? 723  HOH A O     1 
HETATM 9485 O O     . HOH J 5 .   ? 10.469 19.361  -48.687 1.00 32.83 ? 724  HOH A O     1 
HETATM 9486 O O     . HOH J 5 .   ? 41.942 2.049   -47.071 1.00 24.92 ? 725  HOH A O     1 
HETATM 9487 O O     . HOH J 5 .   ? 33.015 8.651   -46.441 1.00 20.48 ? 726  HOH A O     1 
HETATM 9488 O O     . HOH J 5 .   ? 55.148 -0.046  -38.415 1.00 39.80 ? 727  HOH A O     1 
HETATM 9489 O O     . HOH J 5 .   ? 26.826 3.372   -35.394 1.00 21.81 ? 728  HOH A O     1 
HETATM 9490 O O     . HOH J 5 .   ? 16.368 11.119  -81.677 1.00 34.39 ? 729  HOH A O     1 
HETATM 9491 O O     . HOH J 5 .   ? 38.736 -29.652 -50.797 1.00 34.24 ? 730  HOH A O     1 
HETATM 9492 O O     . HOH J 5 .   ? 13.871 17.258  -38.334 1.00 35.95 ? 731  HOH A O     1 
HETATM 9493 O O     . HOH J 5 .   ? 42.683 16.845  -49.196 1.00 42.79 ? 732  HOH A O     1 
HETATM 9494 O O     . HOH J 5 .   ? 59.101 -0.333  -43.957 1.00 35.54 ? 733  HOH A O     1 
HETATM 9495 O O     . HOH J 5 .   ? -5.658 0.085   -66.173 1.00 38.58 ? 734  HOH A O     1 
HETATM 9496 O O     . HOH J 5 .   ? 14.714 -8.895  -57.440 1.00 45.77 ? 735  HOH A O     1 
HETATM 9497 O O     . HOH J 5 .   ? 12.427 -6.853  -56.779 1.00 34.95 ? 736  HOH A O     1 
HETATM 9498 O O     . HOH J 5 .   ? 27.475 3.736   -61.527 1.00 37.70 ? 737  HOH A O     1 
HETATM 9499 O O     . HOH J 5 .   ? 51.181 -9.070  -38.964 1.00 33.56 ? 738  HOH A O     1 
HETATM 9500 O O     . HOH J 5 .   ? 17.499 -15.955 -48.407 1.00 24.88 ? 739  HOH A O     1 
HETATM 9501 O O     . HOH J 5 .   ? 27.445 7.044   -76.091 1.00 30.37 ? 740  HOH A O     1 
HETATM 9502 O O     . HOH J 5 .   ? 29.607 6.910   -23.032 1.00 28.29 ? 741  HOH A O     1 
HETATM 9503 O O     . HOH J 5 .   ? 32.577 -31.946 -45.013 1.00 40.61 ? 742  HOH A O     1 
HETATM 9504 O O     . HOH J 5 .   ? 51.688 -19.327 -46.413 1.00 35.29 ? 743  HOH A O     1 
HETATM 9505 O O     . HOH J 5 .   ? 34.044 8.440   -69.728 1.00 33.74 ? 744  HOH A O     1 
HETATM 9506 O O     . HOH J 5 .   ? 26.724 -17.835 -39.451 1.00 36.94 ? 745  HOH A O     1 
HETATM 9507 O O     . HOH J 5 .   ? 46.257 -14.193 -35.106 1.00 27.04 ? 746  HOH A O     1 
HETATM 9508 O O     . HOH J 5 .   ? 25.456 6.385   -68.017 1.00 30.23 ? 747  HOH A O     1 
HETATM 9509 O O     . HOH J 5 .   ? 43.643 19.691  -58.736 1.00 36.78 ? 748  HOH A O     1 
HETATM 9510 O O     . HOH J 5 .   ? 51.358 0.101   -55.963 1.00 44.62 ? 749  HOH A O     1 
HETATM 9511 O O     . HOH J 5 .   ? 2.557  2.211   -47.866 1.00 44.95 ? 750  HOH A O     1 
HETATM 9512 O O     . HOH J 5 .   ? 27.093 9.497   -35.211 1.00 22.72 ? 751  HOH A O     1 
HETATM 9513 O O     . HOH J 5 .   ? 23.919 -7.780  -63.675 1.00 33.30 ? 752  HOH A O     1 
HETATM 9514 O O     . HOH J 5 .   ? 24.170 -11.149 -57.916 1.00 37.10 ? 753  HOH A O     1 
HETATM 9515 O O     . HOH J 5 .   ? 54.826 -13.048 -59.368 1.00 36.59 ? 754  HOH A O     1 
HETATM 9516 O O     . HOH J 5 .   ? 29.820 21.599  -56.335 1.00 36.00 ? 755  HOH A O     1 
HETATM 9517 O O     . HOH J 5 .   ? 23.248 7.074   -31.112 1.00 19.45 ? 756  HOH A O     1 
HETATM 9518 O O     . HOH J 5 .   ? 19.524 22.557  -47.741 1.00 32.21 ? 757  HOH A O     1 
HETATM 9519 O O     . HOH J 5 .   ? 38.660 15.944  -46.205 1.00 32.09 ? 758  HOH A O     1 
HETATM 9520 O O     . HOH J 5 .   ? 52.638 -0.299  -53.757 1.00 34.86 ? 759  HOH A O     1 
HETATM 9521 O O     . HOH J 5 .   ? 15.432 19.729  -59.497 1.00 28.87 ? 760  HOH A O     1 
HETATM 9522 O O     . HOH J 5 .   ? 57.085 -6.702  -42.218 1.00 30.62 ? 761  HOH A O     1 
HETATM 9523 O O     . HOH J 5 .   ? 26.569 13.028  -41.278 1.00 32.23 ? 762  HOH A O     1 
HETATM 9524 O O     . HOH J 5 .   ? 20.875 2.084   -76.445 1.00 29.15 ? 763  HOH A O     1 
HETATM 9525 O O     . HOH J 5 .   ? 40.155 -18.484 -46.890 1.00 29.82 ? 764  HOH A O     1 
HETATM 9526 O O     . HOH J 5 .   ? 3.050  -9.955  -79.540 1.00 36.28 ? 765  HOH A O     1 
HETATM 9527 O O     . HOH J 5 .   ? 38.431 7.309   -12.902 1.00 40.73 ? 766  HOH A O     1 
HETATM 9528 O O     . HOH J 5 .   ? 27.027 -25.794 -46.145 1.00 23.61 ? 767  HOH A O     1 
HETATM 9529 O O     . HOH J 5 .   ? 15.809 18.614  -42.554 1.00 36.39 ? 768  HOH A O     1 
HETATM 9530 O O     . HOH J 5 .   ? 16.829 -12.236 -46.826 1.00 27.32 ? 769  HOH A O     1 
HETATM 9531 O O     . HOH J 5 .   ? 33.967 -3.555  -45.003 1.00 24.18 ? 770  HOH A O     1 
HETATM 9532 O O     . HOH J 5 .   ? 18.244 12.427  -59.148 1.00 24.98 ? 771  HOH A O     1 
HETATM 9533 O O     . HOH J 5 .   ? 13.297 9.388   -58.221 1.00 23.12 ? 772  HOH A O     1 
HETATM 9534 O O     . HOH J 5 .   ? 37.330 19.340  -49.688 1.00 29.78 ? 773  HOH A O     1 
HETATM 9535 O O     . HOH J 5 .   ? 31.671 -12.736 -40.707 1.00 23.04 ? 774  HOH A O     1 
HETATM 9536 O O     . HOH J 5 .   ? 31.166 11.694  -31.879 1.00 27.91 ? 775  HOH A O     1 
HETATM 9537 O O     . HOH J 5 .   ? 28.400 -9.387  -63.985 1.00 38.61 ? 776  HOH A O     1 
HETATM 9538 O O     . HOH J 5 .   ? 37.274 -7.570  -25.824 1.00 26.21 ? 777  HOH A O     1 
HETATM 9539 O O     . HOH J 5 .   ? 4.496  -5.127  -78.969 1.00 33.78 ? 778  HOH A O     1 
HETATM 9540 O O     . HOH J 5 .   ? 11.261 4.465   -35.794 1.00 27.61 ? 779  HOH A O     1 
HETATM 9541 O O     . HOH J 5 .   ? 36.072 -18.695 -54.805 1.00 29.22 ? 780  HOH A O     1 
HETATM 9542 O O     . HOH J 5 .   ? 10.882 -15.694 -73.897 1.00 29.99 ? 781  HOH A O     1 
HETATM 9543 O O     . HOH J 5 .   ? 41.210 -6.875  -64.968 1.00 35.69 ? 782  HOH A O     1 
HETATM 9544 O O     . HOH J 5 .   ? 38.010 9.330   -41.995 1.00 23.85 ? 783  HOH A O     1 
HETATM 9545 O O     . HOH J 5 .   ? 3.578  -26.772 -36.891 1.00 43.75 ? 784  HOH A O     1 
HETATM 9546 O O     . HOH J 5 .   ? 48.727 1.445   -62.434 1.00 38.74 ? 785  HOH A O     1 
HETATM 9547 O O     . HOH J 5 .   ? 23.411 1.071   -61.344 1.00 33.98 ? 786  HOH A O     1 
HETATM 9548 O O     . HOH J 5 .   ? 5.208  22.955  -69.704 1.00 38.54 ? 787  HOH A O     1 
HETATM 9549 O O     . HOH J 5 .   ? 46.810 -14.040 -39.819 1.00 27.30 ? 788  HOH A O     1 
HETATM 9550 O O     . HOH J 5 .   ? -4.355 12.799  -73.544 1.00 36.37 ? 789  HOH A O     1 
HETATM 9551 O O     . HOH J 5 .   ? 38.586 -25.274 -46.441 1.00 32.53 ? 790  HOH A O     1 
HETATM 9552 O O     . HOH J 5 .   ? -1.576 -9.500  -64.630 1.00 35.69 ? 791  HOH A O     1 
HETATM 9553 O O     . HOH J 5 .   ? 49.504 -10.102 -59.088 1.00 27.96 ? 792  HOH A O     1 
HETATM 9554 O O     . HOH J 5 .   ? 17.707 -29.074 -38.036 1.00 25.08 ? 793  HOH A O     1 
HETATM 9555 O O     . HOH J 5 .   ? 20.595 -24.290 -53.340 1.00 25.46 ? 794  HOH A O     1 
HETATM 9556 O O     . HOH J 5 .   ? 37.483 -11.881 -34.655 1.00 33.38 ? 795  HOH A O     1 
HETATM 9557 O O     . HOH J 5 .   ? 32.438 -1.077  -42.626 1.00 21.60 ? 796  HOH A O     1 
HETATM 9558 O O     . HOH J 5 .   ? 53.468 -13.699 -41.100 1.00 44.24 ? 797  HOH A O     1 
HETATM 9559 O O     . HOH J 5 .   ? 36.373 11.833  -36.358 1.00 32.52 ? 798  HOH A O     1 
HETATM 9560 O O     . HOH J 5 .   ? 17.062 7.607   -41.446 1.00 24.73 ? 799  HOH A O     1 
HETATM 9561 O O     . HOH J 5 .   ? -2.641 -1.410  -69.374 1.00 23.72 ? 800  HOH A O     1 
HETATM 9562 O O     . HOH J 5 .   ? 39.837 4.939   -40.876 1.00 26.53 ? 801  HOH A O     1 
HETATM 9563 O O     . HOH J 5 .   ? 16.460 8.114   -51.258 1.00 22.00 ? 802  HOH A O     1 
HETATM 9564 O O     . HOH J 5 .   ? 6.029  0.997   -50.762 1.00 23.40 ? 803  HOH A O     1 
HETATM 9565 O O     . HOH J 5 .   ? -0.954 14.112  -73.549 1.00 36.21 ? 804  HOH A O     1 
HETATM 9566 O O     . HOH J 5 .   ? 24.097 16.861  -61.927 1.00 35.00 ? 805  HOH A O     1 
HETATM 9567 O O     . HOH J 5 .   ? 49.662 -16.898 -60.362 1.00 34.38 ? 806  HOH A O     1 
HETATM 9568 O O     . HOH J 5 .   ? 48.950 10.580  -51.656 1.00 35.08 ? 807  HOH A O     1 
HETATM 9569 O O     . HOH J 5 .   ? 38.154 21.467  -56.135 1.00 35.81 ? 808  HOH A O     1 
HETATM 9570 O O     . HOH J 5 .   ? 48.069 12.700  -50.131 1.00 35.44 ? 809  HOH A O     1 
HETATM 9571 O O     . HOH J 5 .   ? 47.102 15.280  -68.171 1.00 43.96 ? 810  HOH A O     1 
HETATM 9572 O O     . HOH J 5 .   ? 9.609  8.359   -45.621 1.00 39.97 ? 811  HOH A O     1 
HETATM 9573 O O     . HOH J 5 .   ? 6.603  -8.933  -71.938 1.00 20.63 ? 812  HOH A O     1 
HETATM 9574 O O     . HOH J 5 .   ? 18.597 7.137   -84.752 1.00 46.92 ? 813  HOH A O     1 
HETATM 9575 O O     . HOH J 5 .   ? 41.913 -25.262 -44.840 1.00 45.37 ? 814  HOH A O     1 
HETATM 9576 O O     . HOH J 5 .   ? 25.467 11.330  -57.359 1.00 47.09 ? 815  HOH A O     1 
HETATM 9577 O O     . HOH J 5 .   ? 7.221  7.329   -43.660 1.00 44.36 ? 816  HOH A O     1 
HETATM 9578 O O     . HOH J 5 .   ? 50.664 -2.404  -53.313 1.00 26.91 ? 817  HOH A O     1 
HETATM 9579 O O     . HOH J 5 .   ? 32.009 -4.503  -26.268 1.00 25.05 ? 818  HOH A O     1 
HETATM 9580 O O     . HOH J 5 .   ? 6.292  18.851  -62.401 1.00 34.46 ? 819  HOH A O     1 
HETATM 9581 O O     . HOH J 5 .   ? 33.107 2.242   -65.709 1.00 26.18 ? 820  HOH A O     1 
HETATM 9582 O O     . HOH J 5 .   ? 31.952 -1.988  -66.968 1.00 25.78 ? 821  HOH A O     1 
HETATM 9583 O O     . HOH J 5 .   ? 39.950 -25.078 -55.767 1.00 38.21 ? 822  HOH A O     1 
HETATM 9584 O O     . HOH J 5 .   ? 21.292 -18.212 -50.438 1.00 24.20 ? 823  HOH A O     1 
HETATM 9585 O O     . HOH J 5 .   ? -1.095 2.345   -50.489 1.00 22.20 ? 824  HOH A O     1 
HETATM 9586 O O     . HOH J 5 .   ? 3.760  -2.141  -46.063 1.00 46.77 ? 825  HOH A O     1 
HETATM 9587 O O     . HOH J 5 .   ? 46.449 -1.126  -60.371 1.00 43.81 ? 826  HOH A O     1 
HETATM 9588 O O     . HOH J 5 .   ? 5.385  14.542  -55.115 1.00 38.99 ? 827  HOH A O     1 
HETATM 9589 O O     . HOH J 5 .   ? 16.835 9.653   -43.228 1.00 26.22 ? 828  HOH A O     1 
HETATM 9590 O O     . HOH J 5 .   ? 19.800 4.502   -55.247 1.00 28.81 ? 829  HOH A O     1 
HETATM 9591 O O     . HOH J 5 .   ? 13.085 16.052  -73.908 1.00 34.19 ? 830  HOH A O     1 
HETATM 9592 O O     . HOH J 5 .   ? -0.202 5.266   -74.625 1.00 31.87 ? 831  HOH A O     1 
HETATM 9593 O O     . HOH J 5 .   ? 44.825 10.910  -68.138 1.00 35.46 ? 832  HOH A O     1 
HETATM 9594 O O     . HOH J 5 .   ? 15.271 20.594  -56.014 1.00 34.58 ? 833  HOH A O     1 
HETATM 9595 O O     . HOH J 5 .   ? 36.134 -27.469 -62.298 1.00 42.88 ? 834  HOH A O     1 
HETATM 9596 O O     . HOH J 5 .   ? 34.600 -19.247 -59.753 1.00 29.66 ? 835  HOH A O     1 
HETATM 9597 O O     . HOH J 5 .   ? -0.782 11.327  -45.313 1.00 43.29 ? 836  HOH A O     1 
HETATM 9598 O O     . HOH J 5 .   ? 7.643  11.381  -41.786 1.00 39.01 ? 837  HOH A O     1 
HETATM 9599 O O     . HOH J 5 .   ? 36.917 3.801   -56.050 1.00 30.08 ? 838  HOH A O     1 
HETATM 9600 O O     . HOH J 5 .   ? 49.365 -9.050  -36.964 1.00 21.25 ? 839  HOH A O     1 
HETATM 9601 O O     . HOH J 5 .   ? 33.784 18.649  -41.896 1.00 35.01 ? 840  HOH A O     1 
HETATM 9602 O O     . HOH J 5 .   ? 34.122 -16.675 -38.078 1.00 22.41 ? 841  HOH A O     1 
HETATM 9603 O O     . HOH J 5 .   ? 13.701 8.547   -36.093 1.00 27.20 ? 842  HOH A O     1 
HETATM 9604 O O     . HOH J 5 .   ? 20.785 8.578   -34.195 1.00 22.94 ? 843  HOH A O     1 
HETATM 9605 O O     . HOH J 5 .   ? 40.840 19.359  -48.053 1.00 50.14 ? 844  HOH A O     1 
HETATM 9606 O O     . HOH J 5 .   ? 42.120 11.777  -25.792 1.00 37.03 ? 845  HOH A O     1 
HETATM 9607 O O     . HOH J 5 .   ? 48.563 -7.771  -57.689 1.00 33.68 ? 846  HOH A O     1 
HETATM 9608 O O     . HOH J 5 .   ? 61.105 -8.159  -41.636 1.00 45.63 ? 847  HOH A O     1 
HETATM 9609 O O     . HOH J 5 .   ? 36.605 22.596  -54.189 1.00 46.76 ? 848  HOH A O     1 
HETATM 9610 O O     . HOH J 5 .   ? 38.668 4.703   -52.472 1.00 27.82 ? 849  HOH A O     1 
HETATM 9611 O O     . HOH J 5 .   ? 16.097 -10.403 -53.411 1.00 25.39 ? 850  HOH A O     1 
HETATM 9612 O O     . HOH J 5 .   ? 12.676 -5.100  -72.326 1.00 19.39 ? 851  HOH A O     1 
HETATM 9613 O O     . HOH J 5 .   ? 30.427 -10.137 -38.958 1.00 39.46 ? 852  HOH A O     1 
HETATM 9614 O O     . HOH J 5 .   ? 13.803 3.832   -50.137 1.00 22.52 ? 853  HOH A O     1 
HETATM 9615 O O     . HOH J 5 .   ? 10.909 10.312  -38.291 1.00 44.57 ? 854  HOH A O     1 
HETATM 9616 O O     . HOH J 5 .   ? 15.103 -28.302 -51.984 1.00 29.30 ? 855  HOH A O     1 
HETATM 9617 O O     . HOH J 5 .   ? 45.793 1.694   -22.113 1.00 31.45 ? 856  HOH A O     1 
HETATM 9618 O O     . HOH J 5 .   ? 35.910 4.938   -51.760 1.00 35.95 ? 857  HOH A O     1 
HETATM 9619 O O     . HOH J 5 .   ? 1.476  4.907   -45.399 1.00 47.74 ? 858  HOH A O     1 
HETATM 9620 O O     . HOH J 5 .   ? 33.174 -32.451 -51.123 1.00 34.69 ? 859  HOH A O     1 
HETATM 9621 O O     . HOH J 5 .   ? 38.015 14.707  -22.390 1.00 45.22 ? 860  HOH A O     1 
HETATM 9622 O O     . HOH J 5 .   ? 31.506 6.352   -63.439 1.00 38.36 ? 861  HOH A O     1 
HETATM 9623 O O     . HOH J 5 .   ? -1.931 8.783   -55.534 1.00 36.87 ? 862  HOH A O     1 
HETATM 9624 O O     . HOH J 5 .   ? 25.248 1.979   -69.953 1.00 33.35 ? 863  HOH A O     1 
HETATM 9625 O O     . HOH J 5 .   ? 15.843 10.289  -56.994 1.00 24.65 ? 864  HOH A O     1 
HETATM 9626 O O     . HOH J 5 .   ? 25.450 16.673  -64.496 1.00 40.72 ? 865  HOH A O     1 
HETATM 9627 O O     . HOH J 5 .   ? 33.124 11.271  -17.693 1.00 35.48 ? 866  HOH A O     1 
HETATM 9628 O O     . HOH J 5 .   ? 32.128 -33.980 -48.774 1.00 41.63 ? 867  HOH A O     1 
HETATM 9629 O O     . HOH J 5 .   ? 6.169  -10.483 -74.062 1.00 26.57 ? 868  HOH A O     1 
HETATM 9630 O O     . HOH J 5 .   ? -5.035 -11.749 -65.793 1.00 36.67 ? 869  HOH A O     1 
HETATM 9631 O O     . HOH J 5 .   ? 29.598 11.793  -23.303 1.00 30.80 ? 870  HOH A O     1 
HETATM 9632 O O     . HOH J 5 .   ? 0.535  -8.278  -55.989 1.00 33.96 ? 871  HOH A O     1 
HETATM 9633 O O     . HOH J 5 .   ? 17.011 -0.613  -78.358 1.00 48.09 ? 872  HOH A O     1 
HETATM 9634 O O     . HOH J 5 .   ? -0.625 9.303   -73.411 1.00 40.44 ? 873  HOH A O     1 
HETATM 9635 O O     . HOH J 5 .   ? 0.459  -13.981 -70.931 1.00 32.32 ? 874  HOH A O     1 
HETATM 9636 O O     . HOH J 5 .   ? 50.475 -5.994  -57.681 1.00 35.79 ? 875  HOH A O     1 
HETATM 9637 O O     . HOH J 5 .   ? 37.115 4.166   -40.769 1.00 25.11 ? 876  HOH A O     1 
HETATM 9638 O O     . HOH J 5 .   ? 16.330 15.136  -71.612 1.00 28.73 ? 877  HOH A O     1 
HETATM 9639 O O     . HOH J 5 .   ? 24.778 -30.046 -41.698 1.00 28.53 ? 878  HOH A O     1 
HETATM 9640 O O     . HOH J 5 .   ? 36.856 -7.830  -33.120 1.00 31.05 ? 879  HOH A O     1 
HETATM 9641 O O     . HOH J 5 .   ? 24.987 -32.353 -46.229 1.00 38.09 ? 880  HOH A O     1 
HETATM 9642 O O     . HOH J 5 .   ? 4.924  -16.394 -64.306 1.00 30.11 ? 881  HOH A O     1 
HETATM 9643 O O     . HOH J 5 .   ? 2.917  -1.695  -48.556 1.00 44.38 ? 882  HOH A O     1 
HETATM 9644 O O     . HOH J 5 .   ? 46.448 15.237  -10.868 1.00 40.50 ? 883  HOH A O     1 
HETATM 9645 O O     . HOH J 5 .   ? 48.073 -19.918 -51.738 1.00 33.80 ? 884  HOH A O     1 
HETATM 9646 O O     . HOH J 5 .   ? 5.947  9.612   -59.964 1.00 23.69 ? 885  HOH A O     1 
HETATM 9647 O O     . HOH J 5 .   ? 44.494 1.371   -13.451 1.00 48.10 ? 886  HOH A O     1 
HETATM 9648 O O     . HOH J 5 .   ? 18.837 -33.856 -43.915 1.00 29.69 ? 887  HOH A O     1 
HETATM 9649 O O     . HOH J 5 .   ? 25.105 -12.136 -46.674 1.00 26.30 ? 888  HOH A O     1 
HETATM 9650 O O     . HOH J 5 .   ? 2.893  -0.594  -79.206 1.00 34.35 ? 889  HOH A O     1 
HETATM 9651 O O     . HOH J 5 .   ? 25.733 7.503   -43.693 1.00 22.13 ? 890  HOH A O     1 
HETATM 9652 O O     . HOH J 5 .   ? 21.637 -2.191  -67.981 1.00 25.67 ? 891  HOH A O     1 
HETATM 9653 O O     . HOH J 5 .   ? 20.027 -31.595 -47.920 1.00 28.95 ? 892  HOH A O     1 
HETATM 9654 O O     . HOH J 5 .   ? 13.419 -31.450 -44.967 1.00 47.23 ? 893  HOH A O     1 
HETATM 9655 O O     . HOH J 5 .   ? 8.513  9.378   -75.047 1.00 37.21 ? 894  HOH A O     1 
HETATM 9656 O O     . HOH J 5 .   ? 35.467 13.305  -38.678 1.00 28.85 ? 895  HOH A O     1 
HETATM 9657 O O     . HOH J 5 .   ? 14.054 1.327   -76.500 1.00 23.65 ? 896  HOH A O     1 
HETATM 9658 O O     . HOH J 5 .   ? 39.888 -23.395 -42.180 1.00 24.57 ? 897  HOH A O     1 
HETATM 9659 O O     . HOH J 5 .   ? -3.449 4.663   -77.542 1.00 35.89 ? 898  HOH A O     1 
HETATM 9660 O O     . HOH J 5 .   ? 13.445 3.285   -57.454 1.00 23.44 ? 899  HOH A O     1 
HETATM 9661 O O     . HOH J 5 .   ? 1.205  10.742  -56.914 1.00 32.94 ? 900  HOH A O     1 
HETATM 9662 O O     . HOH J 5 .   ? 30.863 21.501  -59.284 1.00 43.95 ? 901  HOH A O     1 
HETATM 9663 O O     . HOH J 5 .   ? -4.527 3.424   -60.056 1.00 36.68 ? 902  HOH A O     1 
HETATM 9664 O O     . HOH J 5 .   ? 55.411 8.910   -51.554 1.00 44.22 ? 903  HOH A O     1 
HETATM 9665 O O     . HOH J 5 .   ? 29.451 -28.666 -58.824 1.00 39.93 ? 904  HOH A O     1 
HETATM 9666 O O     . HOH J 5 .   ? 16.216 -2.204  -54.020 1.00 32.16 ? 905  HOH A O     1 
HETATM 9667 O O     . HOH J 5 .   ? 25.209 -11.868 -42.519 1.00 32.06 ? 906  HOH A O     1 
HETATM 9668 O O     . HOH J 5 .   ? 34.024 -34.223 -57.804 1.00 48.43 ? 907  HOH A O     1 
HETATM 9669 O O     . HOH J 5 .   ? 40.006 3.599   -63.741 1.00 27.85 ? 908  HOH A O     1 
HETATM 9670 O O     . HOH J 5 .   ? 59.755 -12.581 -54.260 1.00 37.81 ? 909  HOH A O     1 
HETATM 9671 O O     . HOH J 5 .   ? -3.516 13.686  -47.965 1.00 37.04 ? 910  HOH A O     1 
HETATM 9672 O O     . HOH J 5 .   ? 45.720 -22.934 -45.383 1.00 40.71 ? 911  HOH A O     1 
HETATM 9673 O O     . HOH J 5 .   ? 8.928  -17.136 -61.885 1.00 28.62 ? 912  HOH A O     1 
HETATM 9674 O O     . HOH J 5 .   ? 30.286 -9.084  -66.042 1.00 28.28 ? 913  HOH A O     1 
HETATM 9675 O O     . HOH J 5 .   ? 50.357 -10.898 -40.689 1.00 31.78 ? 914  HOH A O     1 
HETATM 9676 O O     . HOH J 5 .   ? -0.182 18.025  -51.963 1.00 48.27 ? 915  HOH A O     1 
HETATM 9677 O O     . HOH J 5 .   ? 4.561  1.168   -43.844 1.00 26.32 ? 916  HOH A O     1 
HETATM 9678 O O     . HOH J 5 .   ? 52.783 0.915   -37.168 1.00 27.27 ? 917  HOH A O     1 
HETATM 9679 O O     . HOH J 5 .   ? 38.813 5.769   -43.312 1.00 23.61 ? 918  HOH A O     1 
HETATM 9680 O O     . HOH J 5 .   ? 31.773 -2.007  -45.147 1.00 20.84 ? 919  HOH A O     1 
HETATM 9681 O O     . HOH J 5 .   ? 3.366  -7.356  -49.759 1.00 29.10 ? 920  HOH A O     1 
HETATM 9682 O O     . HOH J 5 .   ? -2.265 4.426   -80.078 1.00 39.78 ? 921  HOH A O     1 
HETATM 9683 O O     . HOH J 5 .   ? 41.522 -7.916  -67.058 1.00 29.99 ? 922  HOH A O     1 
HETATM 9684 O O     . HOH J 5 .   ? 11.398 3.962   -78.959 1.00 31.40 ? 923  HOH A O     1 
HETATM 9685 O O     . HOH J 5 .   ? 27.911 15.940  -64.753 1.00 39.75 ? 924  HOH A O     1 
HETATM 9686 O O     . HOH J 5 .   ? 32.214 22.102  -46.643 1.00 36.31 ? 925  HOH A O     1 
HETATM 9687 O O     . HOH J 5 .   ? 41.556 16.210  -53.453 1.00 41.56 ? 926  HOH A O     1 
HETATM 9688 O O     . HOH J 5 .   ? 1.699  8.160   -76.940 1.00 46.10 ? 927  HOH A O     1 
HETATM 9689 O O     . HOH J 5 .   ? 11.816 -14.921 -61.253 1.00 33.77 ? 928  HOH A O     1 
HETATM 9690 O O     . HOH J 5 .   ? 16.858 -21.347 -53.249 1.00 27.56 ? 929  HOH A O     1 
HETATM 9691 O O     . HOH J 5 .   ? 20.113 -9.551  -54.186 1.00 39.66 ? 930  HOH A O     1 
HETATM 9692 O O     . HOH J 5 .   ? 45.410 -17.194 -43.184 1.00 31.29 ? 931  HOH A O     1 
HETATM 9693 O O     . HOH J 5 .   ? 40.863 12.074  -52.302 1.00 30.26 ? 932  HOH A O     1 
HETATM 9694 O O     . HOH J 5 .   ? 10.292 1.901   -77.604 1.00 24.85 ? 933  HOH A O     1 
HETATM 9695 O O     . HOH J 5 .   ? 1.173  -8.204  -76.840 1.00 29.02 ? 934  HOH A O     1 
HETATM 9696 O O     . HOH J 5 .   ? 8.636  -29.450 -44.863 1.00 33.99 ? 935  HOH A O     1 
HETATM 9697 O O     . HOH J 5 .   ? 38.141 -24.846 -40.851 1.00 40.05 ? 936  HOH A O     1 
HETATM 9698 O O     . HOH J 5 .   ? 36.132 -30.678 -56.489 1.00 33.73 ? 937  HOH A O     1 
HETATM 9699 O O     . HOH J 5 .   ? 35.078 3.474   -53.887 1.00 30.53 ? 938  HOH A O     1 
HETATM 9700 O O     . HOH J 5 .   ? 37.269 13.948  -34.846 1.00 28.91 ? 939  HOH A O     1 
HETATM 9701 O O     . HOH J 5 .   ? 26.832 -11.157 -63.202 1.00 34.93 ? 940  HOH A O     1 
HETATM 9702 O O     . HOH J 5 .   ? 13.600 -11.034 -69.159 1.00 23.70 ? 941  HOH A O     1 
HETATM 9703 O O     . HOH J 5 .   ? 31.471 -8.689  -33.660 1.00 42.50 ? 942  HOH A O     1 
HETATM 9704 O O     . HOH J 5 .   ? 20.082 8.795   -44.024 1.00 23.84 ? 943  HOH A O     1 
HETATM 9705 O O     . HOH J 5 .   ? 39.268 -9.350  -32.078 1.00 25.59 ? 944  HOH A O     1 
HETATM 9706 O O     . HOH J 5 .   ? 22.333 -7.556  -71.398 1.00 44.47 ? 945  HOH A O     1 
HETATM 9707 O O     . HOH J 5 .   ? 24.252 5.843   -76.503 1.00 42.42 ? 946  HOH A O     1 
HETATM 9708 O O     . HOH J 5 .   ? 15.905 -28.888 -40.096 1.00 25.62 ? 947  HOH A O     1 
HETATM 9709 O O     . HOH J 5 .   ? 37.881 11.880  -42.389 1.00 23.65 ? 948  HOH A O     1 
HETATM 9710 O O     . HOH J 5 .   ? 15.722 21.168  -68.605 1.00 40.91 ? 949  HOH A O     1 
HETATM 9711 O O     . HOH J 5 .   ? 12.889 2.408   -36.574 1.00 32.92 ? 950  HOH A O     1 
HETATM 9712 O O     . HOH J 5 .   ? 16.286 -5.971  -73.722 1.00 26.90 ? 951  HOH A O     1 
HETATM 9713 O O     . HOH J 5 .   ? 18.106 -6.976  -75.532 1.00 42.28 ? 952  HOH A O     1 
HETATM 9714 O O     . HOH J 5 .   ? 3.487  16.368  -49.386 1.00 37.11 ? 953  HOH A O     1 
HETATM 9715 O O     . HOH J 5 .   ? 20.318 -31.384 -52.169 1.00 29.19 ? 954  HOH A O     1 
HETATM 9716 O O     . HOH J 5 .   ? 20.750 -15.604 -56.877 1.00 27.48 ? 955  HOH A O     1 
HETATM 9717 O O     . HOH J 5 .   ? 57.243 -2.594  -50.152 1.00 31.21 ? 956  HOH A O     1 
HETATM 9718 O O     . HOH J 5 .   ? -2.499 0.164   -54.249 1.00 30.04 ? 957  HOH A O     1 
HETATM 9719 O O     . HOH J 5 .   ? 40.316 -13.297 -71.105 1.00 30.83 ? 958  HOH A O     1 
HETATM 9720 O O     . HOH J 5 .   ? 10.487 -17.750 -68.035 1.00 36.19 ? 959  HOH A O     1 
HETATM 9721 O O     . HOH J 5 .   ? 23.066 15.431  -39.478 1.00 25.24 ? 960  HOH A O     1 
HETATM 9722 O O     . HOH J 5 .   ? 8.109  22.581  -69.073 1.00 37.07 ? 961  HOH A O     1 
HETATM 9723 O O     . HOH J 5 .   ? 18.439 11.935  -43.514 1.00 21.77 ? 962  HOH A O     1 
HETATM 9724 O O     . HOH J 5 .   ? -2.376 10.672  -71.644 1.00 39.90 ? 963  HOH A O     1 
HETATM 9725 O O     . HOH J 5 .   ? 4.970  -10.726 -76.389 1.00 25.82 ? 964  HOH A O     1 
HETATM 9726 O O     . HOH J 5 .   ? -2.344 6.213   -56.390 1.00 28.21 ? 965  HOH A O     1 
HETATM 9727 O O     . HOH J 5 .   ? -3.872 6.788   -51.910 1.00 32.67 ? 966  HOH A O     1 
HETATM 9728 O O     . HOH J 5 .   ? 19.850 2.989   -79.547 1.00 35.90 ? 967  HOH A O     1 
HETATM 9729 O O     . HOH J 5 .   ? 58.901 12.529  -45.596 1.00 44.69 ? 968  HOH A O     1 
HETATM 9730 O O     . HOH J 5 .   ? 60.644 -8.771  -54.033 1.00 36.91 ? 969  HOH A O     1 
HETATM 9731 O O     . HOH J 5 .   ? 2.581  11.555  -44.453 1.00 40.18 ? 970  HOH A O     1 
HETATM 9732 O O     . HOH J 5 .   ? 26.939 9.822   -62.387 1.00 31.23 ? 971  HOH A O     1 
HETATM 9733 O O     . HOH J 5 .   ? 2.456  18.899  -65.837 1.00 45.77 ? 972  HOH A O     1 
HETATM 9734 O O     . HOH J 5 .   ? 23.176 8.091   -43.127 1.00 23.90 ? 973  HOH A O     1 
HETATM 9735 O O     . HOH J 5 .   ? 38.007 13.834  -30.148 1.00 43.02 ? 974  HOH A O     1 
HETATM 9736 O O     . HOH J 5 .   ? 55.763 -7.090  -54.493 1.00 32.40 ? 975  HOH A O     1 
HETATM 9737 O O     . HOH J 5 .   ? 25.879 -20.136 -45.327 1.00 24.38 ? 976  HOH A O     1 
HETATM 9738 O O     . HOH J 5 .   ? 6.534  11.629  -72.601 1.00 30.63 ? 977  HOH A O     1 
HETATM 9739 O O     . HOH J 5 .   ? 34.740 16.997  -46.115 1.00 27.90 ? 978  HOH A O     1 
HETATM 9740 O O     . HOH J 5 .   ? -1.508 6.339   -76.581 1.00 35.59 ? 979  HOH A O     1 
HETATM 9741 O O     . HOH J 5 .   ? 30.888 -20.286 -38.242 1.00 28.68 ? 980  HOH A O     1 
HETATM 9742 O O     . HOH J 5 .   ? 32.913 -8.822  -31.536 1.00 34.12 ? 981  HOH A O     1 
HETATM 9743 O O     . HOH J 5 .   ? 38.498 -20.299 -54.872 1.00 28.17 ? 982  HOH A O     1 
HETATM 9744 O O     . HOH J 5 .   ? 5.725  -23.083 -34.818 1.00 32.90 ? 983  HOH A O     1 
HETATM 9745 O O     . HOH J 5 .   ? 9.011  5.977   -47.038 1.00 21.77 ? 984  HOH A O     1 
HETATM 9746 O O     . HOH J 5 .   ? 7.532  1.509   -77.191 1.00 24.70 ? 985  HOH A O     1 
HETATM 9747 O O     . HOH J 5 .   ? 11.303 -6.388  -79.002 1.00 27.16 ? 986  HOH A O     1 
HETATM 9748 O O     . HOH J 5 .   ? 35.153 -31.373 -45.063 1.00 31.76 ? 987  HOH A O     1 
HETATM 9749 O O     . HOH J 5 .   ? 47.540 12.080  -64.468 1.00 39.05 ? 988  HOH A O     1 
HETATM 9750 O O     . HOH J 5 .   ? 16.825 -19.552 -56.824 1.00 36.70 ? 989  HOH A O     1 
HETATM 9751 O O     . HOH J 5 .   ? 3.899  -13.480 -64.476 1.00 33.78 ? 990  HOH A O     1 
HETATM 9752 O O     . HOH J 5 .   ? 52.403 -1.540  -36.296 1.00 25.88 ? 991  HOH A O     1 
HETATM 9753 O O     . HOH J 5 .   ? 25.057 6.765   -65.264 1.00 27.63 ? 992  HOH A O     1 
HETATM 9754 O O     . HOH J 5 .   ? 22.636 -10.204 -44.639 1.00 20.33 ? 993  HOH A O     1 
HETATM 9755 O O     . HOH J 5 .   ? 19.536 -12.292 -46.912 1.00 22.69 ? 994  HOH A O     1 
HETATM 9756 O O     . HOH J 5 .   ? 30.039 -4.567  -30.348 1.00 28.80 ? 995  HOH A O     1 
HETATM 9757 O O     . HOH J 5 .   ? 38.578 -3.919  -22.062 1.00 22.89 ? 996  HOH A O     1 
HETATM 9758 O O     . HOH J 5 .   ? 49.134 12.123  -44.427 1.00 37.75 ? 997  HOH A O     1 
HETATM 9759 O O     . HOH J 5 .   ? 40.294 8.066   -43.329 1.00 24.17 ? 998  HOH A O     1 
HETATM 9760 O O     . HOH J 5 .   ? 14.166 -0.722  -78.169 1.00 35.78 ? 999  HOH A O     1 
HETATM 9761 O O     . HOH J 5 .   ? 35.324 1.364   -13.501 1.00 44.22 ? 1000 HOH A O     1 
HETATM 9762 O O     . HOH J 5 .   ? 2.753  21.089  -67.774 1.00 47.90 ? 1001 HOH A O     1 
HETATM 9763 O O     . HOH J 5 .   ? 18.365 -4.120  -76.410 1.00 50.71 ? 1002 HOH A O     1 
HETATM 9764 O O     . HOH J 5 .   ? 1.399  -14.950 -57.401 1.00 38.05 ? 1003 HOH A O     1 
HETATM 9765 O O     . HOH J 5 .   ? 41.082 7.089   -39.476 1.00 27.96 ? 1004 HOH A O     1 
HETATM 9766 O O     . HOH J 5 .   ? 57.400 -2.490  -40.142 1.00 43.13 ? 1005 HOH A O     1 
HETATM 9767 O O     . HOH J 5 .   ? -2.147 16.940  -66.405 1.00 38.73 ? 1006 HOH A O     1 
HETATM 9768 O O     . HOH J 5 .   ? 41.500 10.070  -44.862 1.00 24.02 ? 1007 HOH A O     1 
HETATM 9769 O O     . HOH J 5 .   ? 22.032 -7.755  -58.225 1.00 32.49 ? 1008 HOH A O     1 
HETATM 9770 O O     . HOH J 5 .   ? 17.579 3.294   -81.950 1.00 34.17 ? 1009 HOH A O     1 
HETATM 9771 O O     . HOH J 5 .   ? -5.097 -0.067  -73.757 1.00 34.98 ? 1010 HOH A O     1 
HETATM 9772 O O     . HOH J 5 .   ? 37.669 -25.116 -64.458 1.00 39.50 ? 1011 HOH A O     1 
HETATM 9773 O O     . HOH J 5 .   ? 57.231 -5.106  -50.091 1.00 36.78 ? 1012 HOH A O     1 
HETATM 9774 O O     . HOH J 5 .   ? 21.504 -9.828  -41.925 1.00 21.87 ? 1013 HOH A O     1 
HETATM 9775 O O     . HOH J 5 .   ? 22.670 10.609  -64.002 1.00 33.04 ? 1014 HOH A O     1 
HETATM 9776 O O     . HOH J 5 .   ? 9.240  8.251   -37.585 1.00 42.41 ? 1015 HOH A O     1 
HETATM 9777 O O     . HOH J 5 .   ? 22.999 -4.105  -69.899 1.00 22.57 ? 1016 HOH A O     1 
HETATM 9778 O O     . HOH J 5 .   ? 28.471 11.733  -32.511 1.00 36.83 ? 1017 HOH A O     1 
HETATM 9779 O O     . HOH J 5 .   ? 45.359 4.869   -25.449 1.00 24.18 ? 1018 HOH A O     1 
HETATM 9780 O O     . HOH J 5 .   ? 16.125 -11.006 -69.955 1.00 26.96 ? 1019 HOH A O     1 
HETATM 9781 O O     . HOH J 5 .   ? 31.434 -6.755  -29.354 1.00 27.19 ? 1020 HOH A O     1 
HETATM 9782 O O     . HOH J 5 .   ? 14.947 5.695   -82.228 1.00 33.64 ? 1021 HOH A O     1 
HETATM 9783 O O     . HOH J 5 .   ? 4.400  7.672   -78.655 1.00 44.61 ? 1022 HOH A O     1 
HETATM 9784 O O     . HOH J 5 .   ? 0.937  -5.498  -59.783 1.00 40.50 ? 1023 HOH A O     1 
HETATM 9785 O O     . HOH J 5 .   ? 11.990 10.289  -35.184 1.00 37.50 ? 1024 HOH A O     1 
HETATM 9786 O O     . HOH J 5 .   ? 23.410 11.880  -24.009 1.00 42.78 ? 1025 HOH A O     1 
HETATM 9787 O O     . HOH J 5 .   ? 6.287  -13.291 -76.470 1.00 35.21 ? 1026 HOH A O     1 
HETATM 9788 O O     . HOH J 5 .   ? 41.476 13.590  -45.553 1.00 30.13 ? 1027 HOH A O     1 
HETATM 9789 O O     . HOH J 5 .   ? 23.953 1.581   -27.358 1.00 29.37 ? 1028 HOH A O     1 
HETATM 9790 O O     . HOH J 5 .   ? 57.506 -6.789  -52.289 1.00 28.37 ? 1029 HOH A O     1 
HETATM 9791 O O     . HOH J 5 .   ? 46.351 10.285  -65.887 1.00 40.97 ? 1030 HOH A O     1 
HETATM 9792 O O     . HOH J 5 .   ? -2.751 -8.223  -57.846 1.00 30.74 ? 1031 HOH A O     1 
HETATM 9793 O O     . HOH J 5 .   ? 12.855 -4.164  -79.561 1.00 38.59 ? 1032 HOH A O     1 
HETATM 9794 O O     . HOH J 5 .   ? 1.608  7.362   -46.686 1.00 26.13 ? 1033 HOH A O     1 
HETATM 9795 O O     . HOH J 5 .   ? 16.924 -0.055  -58.498 1.00 41.44 ? 1034 HOH A O     1 
HETATM 9796 O O     . HOH J 5 .   ? 63.455 -9.545  -49.931 1.00 31.74 ? 1035 HOH A O     1 
HETATM 9797 O O     . HOH J 5 .   ? 29.429 -4.097  -66.488 1.00 43.48 ? 1036 HOH A O     1 
HETATM 9798 O O     . HOH J 5 .   ? 11.908 14.560  -33.620 1.00 47.56 ? 1037 HOH A O     1 
HETATM 9799 O O     . HOH J 5 .   ? 1.247  15.600  -72.927 1.00 34.61 ? 1038 HOH A O     1 
HETATM 9800 O O     . HOH J 5 .   ? 47.440 15.867  -63.775 1.00 43.28 ? 1039 HOH A O     1 
HETATM 9801 O O     . HOH J 5 .   ? 3.232  17.677  -78.014 1.00 40.44 ? 1040 HOH A O     1 
HETATM 9802 O O     . HOH J 5 .   ? -4.289 7.192   -62.754 1.00 40.33 ? 1041 HOH A O     1 
HETATM 9803 O O     . HOH J 5 .   ? 44.070 11.532  -29.947 1.00 32.02 ? 1042 HOH A O     1 
HETATM 9804 O O     . HOH J 5 .   ? 38.264 18.935  -62.321 1.00 41.33 ? 1043 HOH A O     1 
HETATM 9805 O O     . HOH J 5 .   ? 25.823 -31.855 -40.606 1.00 38.08 ? 1044 HOH A O     1 
HETATM 9806 O O     . HOH J 5 .   ? -4.439 1.355   -79.796 1.00 38.80 ? 1045 HOH A O     1 
HETATM 9807 O O     . HOH J 5 .   ? 47.670 -21.690 -59.493 1.00 45.24 ? 1046 HOH A O     1 
HETATM 9808 O O     . HOH J 5 .   ? -2.266 2.666   -53.023 1.00 24.66 ? 1047 HOH A O     1 
HETATM 9809 O O     . HOH J 5 .   ? 40.324 -20.372 -56.579 1.00 35.80 ? 1048 HOH A O     1 
HETATM 9810 O O     . HOH J 5 .   ? -2.890 5.454   -61.072 1.00 43.97 ? 1049 HOH A O     1 
HETATM 9811 O O     . HOH J 5 .   ? 33.723 12.639  -20.400 1.00 29.87 ? 1050 HOH A O     1 
HETATM 9812 O O     . HOH J 5 .   ? 44.081 -25.017 -46.286 1.00 43.88 ? 1051 HOH A O     1 
HETATM 9813 O O     . HOH J 5 .   ? 9.922  6.044   -42.720 1.00 27.61 ? 1052 HOH A O     1 
HETATM 9814 O O     . HOH J 5 .   ? 38.913 13.259  -32.751 1.00 35.82 ? 1053 HOH A O     1 
HETATM 9815 O O     . HOH J 5 .   ? 35.521 16.119  -38.233 1.00 44.72 ? 1054 HOH A O     1 
HETATM 9816 O O     . HOH J 5 .   ? 19.118 14.886  -33.046 1.00 32.94 ? 1055 HOH A O     1 
HETATM 9817 O O     . HOH J 5 .   ? 48.203 11.095  -54.135 1.00 36.97 ? 1056 HOH A O     1 
HETATM 9818 O O     . HOH J 5 .   ? 24.198 -9.661  -41.006 1.00 31.29 ? 1057 HOH A O     1 
HETATM 9819 O O     . HOH J 5 .   ? 44.854 -19.720 -42.676 1.00 34.79 ? 1058 HOH A O     1 
HETATM 9820 O O     . HOH J 5 .   ? 42.150 13.956  -53.089 1.00 35.08 ? 1059 HOH A O     1 
HETATM 9821 O O     . HOH J 5 .   ? 40.528 -22.751 -56.939 1.00 44.70 ? 1060 HOH A O     1 
HETATM 9822 O O     . HOH J 5 .   ? 5.488  16.904  -54.260 1.00 48.78 ? 1061 HOH A O     1 
HETATM 9823 O O     . HOH J 5 .   ? 32.363 4.580   -66.204 1.00 46.31 ? 1062 HOH A O     1 
HETATM 9824 O O     . HOH J 5 .   ? 32.064 -24.413 -66.287 1.00 38.71 ? 1063 HOH A O     1 
HETATM 9825 O O     . HOH J 5 .   ? 2.486  2.501   -44.822 1.00 44.04 ? 1064 HOH A O     1 
HETATM 9826 O O     . HOH J 5 .   ? 32.050 13.426  -29.983 1.00 45.71 ? 1065 HOH A O     1 
HETATM 9827 O O     . HOH J 5 .   ? 13.860 -13.054 -61.183 1.00 41.70 ? 1066 HOH A O     1 
HETATM 9828 O O     . HOH J 5 .   ? 10.107 6.274   -78.973 1.00 44.63 ? 1067 HOH A O     1 
HETATM 9829 O O     . HOH J 5 .   ? 21.573 -32.428 -50.154 1.00 40.68 ? 1068 HOH A O     1 
HETATM 9830 O O     . HOH J 5 .   ? 0.048  -2.006  -82.107 1.00 57.54 ? 1069 HOH A O     1 
HETATM 9831 O O     . HOH J 5 .   ? 17.744 20.107  -60.378 1.00 45.77 ? 1070 HOH A O     1 
HETATM 9832 O O     . HOH J 5 .   ? -2.955 7.056   -59.237 1.00 36.85 ? 1071 HOH A O     1 
HETATM 9833 O O     . HOH J 5 .   ? 12.383 -35.657 -37.204 1.00 44.91 ? 1072 HOH A O     1 
HETATM 9834 O O     . HOH J 5 .   ? 6.523  -18.174 -63.014 1.00 33.62 ? 1073 HOH A O     1 
HETATM 9835 O O     . HOH J 5 .   ? 50.018 -21.492 -47.773 1.00 43.32 ? 1074 HOH A O     1 
HETATM 9836 O O     . HOH J 5 .   ? 13.522 22.029  -62.822 1.00 39.54 ? 1075 HOH A O     1 
HETATM 9837 O O     . HOH J 5 .   ? 15.786 13.575  -31.381 1.00 48.21 ? 1076 HOH A O     1 
HETATM 9838 O O     . HOH J 5 .   ? 44.039 -17.503 -39.316 1.00 36.92 ? 1077 HOH A O     1 
HETATM 9839 O O     . HOH J 5 .   ? 25.252 9.259   -64.489 1.00 28.34 ? 1078 HOH A O     1 
HETATM 9840 O O     . HOH J 5 .   ? 30.958 -19.709 -66.998 1.00 36.31 ? 1079 HOH A O     1 
HETATM 9841 O O     . HOH J 5 .   ? 11.187 20.635  -58.739 1.00 47.23 ? 1080 HOH A O     1 
HETATM 9842 O O     . HOH J 5 .   ? 51.971 -9.358  -59.013 1.00 36.91 ? 1081 HOH A O     1 
HETATM 9843 O O     . HOH J 5 .   ? 32.655 -31.635 -41.467 1.00 40.80 ? 1082 HOH A O     1 
HETATM 9844 O O     . HOH J 5 .   ? 16.686 22.910  -43.282 1.00 42.16 ? 1083 HOH A O     1 
HETATM 9845 O O     . HOH J 5 .   ? 52.273 -17.226 -59.205 1.00 35.52 ? 1084 HOH A O     1 
HETATM 9846 O O     . HOH J 5 .   ? 17.093 20.812  -41.696 1.00 38.41 ? 1085 HOH A O     1 
HETATM 9847 O O     . HOH J 5 .   ? 40.360 12.464  -43.366 1.00 29.76 ? 1086 HOH A O     1 
HETATM 9848 O O     . HOH J 5 .   ? 15.961 9.005   -83.317 1.00 47.18 ? 1087 HOH A O     1 
HETATM 9849 O O     . HOH J 5 .   ? 42.950 12.877  -36.249 1.00 47.94 ? 1088 HOH A O     1 
HETATM 9850 O O     . HOH J 5 .   ? 21.429 14.033  -26.091 1.00 43.72 ? 1089 HOH A O     1 
HETATM 9851 O O     . HOH J 5 .   ? 57.647 -12.589 -59.036 1.00 38.69 ? 1090 HOH A O     1 
HETATM 9852 O O     . HOH J 5 .   ? -2.478 -4.449  -56.028 1.00 47.35 ? 1091 HOH A O     1 
HETATM 9853 O O     . HOH J 5 .   ? 51.758 10.599  -52.176 1.00 45.08 ? 1092 HOH A O     1 
HETATM 9854 O O     . HOH J 5 .   ? 59.972 -6.527  -53.462 1.00 36.26 ? 1093 HOH A O     1 
HETATM 9855 O O     . HOH J 5 .   ? 16.154 12.845  -57.254 1.00 32.44 ? 1094 HOH A O     1 
HETATM 9856 O O     . HOH J 5 .   ? 19.210 -22.133 -52.357 1.00 28.46 ? 1095 HOH A O     1 
HETATM 9857 O O     . HOH J 5 .   ? 11.176 16.963  -37.074 1.00 43.32 ? 1096 HOH A O     1 
HETATM 9858 O O     . HOH J 5 .   ? 21.797 -11.625 -58.153 1.00 49.41 ? 1097 HOH A O     1 
HETATM 9859 O O     . HOH J 5 .   ? 31.719 14.616  -75.703 1.00 42.67 ? 1098 HOH A O     1 
HETATM 9860 O O     . HOH J 5 .   ? 52.756 -19.018 -57.189 1.00 45.73 ? 1099 HOH A O     1 
HETATM 9861 O O     . HOH J 5 .   ? 26.570 4.397   -69.719 1.00 36.81 ? 1100 HOH A O     1 
HETATM 9862 O O     . HOH J 5 .   ? 16.923 17.493  -73.242 1.00 32.88 ? 1101 HOH A O     1 
HETATM 9863 O O     . HOH J 5 .   ? 16.310 -15.233 -58.364 1.00 42.64 ? 1102 HOH A O     1 
HETATM 9864 O O     . HOH J 5 .   ? 27.994 -10.361 -40.572 1.00 37.32 ? 1103 HOH A O     1 
HETATM 9865 O O     . HOH J 5 .   ? 27.443 5.266   -63.549 1.00 42.48 ? 1104 HOH A O     1 
HETATM 9866 O O     . HOH J 5 .   ? 49.382 -11.676 -36.897 1.00 29.04 ? 1105 HOH A O     1 
HETATM 9867 O O     . HOH J 5 .   ? 36.961 17.324  -47.861 1.00 35.99 ? 1106 HOH A O     1 
HETATM 9868 O O     . HOH J 5 .   ? 49.167 -13.119 -39.214 1.00 30.36 ? 1107 HOH A O     1 
HETATM 9869 O O     . HOH J 5 .   ? 13.194 -14.925 -74.462 1.00 43.34 ? 1108 HOH A O     1 
HETATM 9870 O O     . HOH J 5 .   ? 26.342 -7.950  -37.330 1.00 39.45 ? 1109 HOH A O     1 
HETATM 9871 O O     . HOH J 5 .   ? 41.581 -27.080 -55.790 1.00 50.04 ? 1110 HOH A O     1 
HETATM 9872 O O     . HOH J 5 .   ? -0.546 -6.553  -57.612 1.00 41.18 ? 1111 HOH A O     1 
HETATM 9873 O O     . HOH J 5 .   ? 44.390 -18.477 -36.838 1.00 47.58 ? 1112 HOH A O     1 
HETATM 9874 O O     . HOH J 5 .   ? 31.170 -6.616  -67.134 1.00 43.81 ? 1113 HOH A O     1 
HETATM 9875 O O     . HOH J 5 .   ? 57.093 -6.185  -56.805 1.00 36.96 ? 1114 HOH A O     1 
HETATM 9876 O O     . HOH J 5 .   ? 29.528 -11.323 -67.363 1.00 46.42 ? 1115 HOH A O     1 
HETATM 9877 O O     . HOH J 5 .   ? 35.796 -32.808 -50.834 1.00 40.84 ? 1116 HOH A O     1 
HETATM 9878 O O     . HOH J 5 .   ? 2.340  -15.044 -54.990 1.00 40.26 ? 1117 HOH A O     1 
HETATM 9879 O O     . HOH J 5 .   ? 37.997 12.665  -39.833 1.00 36.99 ? 1118 HOH A O     1 
HETATM 9880 O O     . HOH J 5 .   ? 31.919 -18.140 -37.414 1.00 26.65 ? 1119 HOH A O     1 
HETATM 9881 O O     . HOH J 5 .   ? 32.438 -14.554 -38.737 1.00 38.89 ? 1120 HOH A O     1 
HETATM 9882 O O     . HOH J 5 .   ? 31.351 -13.386 -67.278 1.00 47.06 ? 1121 HOH A O     1 
HETATM 9883 O O     . HOH J 5 .   ? 55.046 2.596   -52.983 1.00 35.29 ? 1122 HOH A O     1 
HETATM 9884 O O     . HOH J 5 .   ? 57.007 -1.834  -52.913 1.00 38.17 ? 1123 HOH A O     1 
HETATM 9885 O O     . HOH J 5 .   ? 31.718 13.220  -24.273 1.00 41.87 ? 1124 HOH A O     1 
HETATM 9886 O O     . HOH J 5 .   ? -4.455 4.103   -53.013 1.00 40.49 ? 1125 HOH A O     1 
HETATM 9887 O O     . HOH J 5 .   ? -0.806 -0.090  -50.270 1.00 33.29 ? 1126 HOH A O     1 
HETATM 9888 O O     . HOH J 5 .   ? 22.857 -12.828 -45.121 1.00 27.16 ? 1127 HOH A O     1 
HETATM 9889 O O     . HOH J 5 .   ? 56.526 -0.669  -35.927 1.00 38.84 ? 1128 HOH A O     1 
HETATM 9890 O O     . HOH J 5 .   ? 19.373 -11.229 -73.589 1.00 41.46 ? 1129 HOH A O     1 
HETATM 9891 O O     . HOH J 5 .   ? 54.456 -1.762  -34.351 1.00 39.55 ? 1130 HOH A O     1 
HETATM 9892 O O     . HOH J 5 .   ? 53.765 -17.878 -48.788 1.00 39.74 ? 1131 HOH A O     1 
HETATM 9893 O O     . HOH J 5 .   ? -3.517 -4.110  -69.113 1.00 41.72 ? 1132 HOH A O     1 
HETATM 9894 O O     . HOH J 5 .   ? 50.248 -8.099  -34.456 1.00 33.67 ? 1133 HOH A O     1 
HETATM 9895 O O     . HOH J 5 .   ? 35.167 18.996  -44.367 1.00 33.48 ? 1134 HOH A O     1 
HETATM 9896 O O     . HOH J 5 .   ? 48.518 -12.859 -34.387 1.00 29.06 ? 1135 HOH A O     1 
HETATM 9897 O O     . HOH J 5 .   ? 19.209 -33.518 -46.470 1.00 45.44 ? 1136 HOH A O     1 
HETATM 9898 O O     . HOH J 5 .   ? 50.948 -18.452 -53.097 1.00 46.70 ? 1137 HOH A O     1 
HETATM 9899 O O     . HOH J 5 .   ? 35.315 18.379  -39.707 1.00 45.74 ? 1138 HOH A O     1 
HETATM 9900 O O     . HOH J 5 .   ? 20.524 -23.263 -56.106 1.00 31.98 ? 1139 HOH A O     1 
HETATM 9901 O O     . HOH J 5 .   ? 16.930 -10.386 -56.174 1.00 36.52 ? 1140 HOH A O     1 
HETATM 9902 O O     . HOH J 5 .   ? 5.520  -9.630  -78.828 1.00 30.44 ? 1141 HOH A O     1 
HETATM 9903 O O     . HOH J 5 .   ? 55.215 0.093   -53.496 1.00 37.27 ? 1142 HOH A O     1 
HETATM 9904 O O     . HOH J 5 .   ? -6.091 1.590   -69.835 1.00 43.29 ? 1143 HOH A O     1 
HETATM 9905 O O     . HOH J 5 .   ? 15.479 17.673  -36.078 1.00 44.38 ? 1144 HOH A O     1 
HETATM 9906 O O     . HOH J 5 .   ? -4.708 -0.181  -71.054 1.00 36.11 ? 1145 HOH A O     1 
HETATM 9907 O O     . HOH J 5 .   ? 15.108 -3.868  -81.034 1.00 54.19 ? 1146 HOH A O     1 
HETATM 9908 O O     . HOH J 5 .   ? 35.865 -28.706 -41.102 1.00 47.22 ? 1147 HOH A O     1 
HETATM 9909 O O     . HOH J 5 .   ? 38.758 8.865   -39.354 1.00 36.27 ? 1148 HOH A O     1 
HETATM 9910 O O     . HOH J 5 .   ? 46.098 -16.427 -40.698 1.00 34.37 ? 1149 HOH A O     1 
HETATM 9911 O O     . HOH J 5 .   ? 10.644 -19.239 -62.728 1.00 47.25 ? 1150 HOH A O     1 
HETATM 9912 O O     . HOH J 5 .   ? 2.601  -6.929  -79.107 1.00 38.25 ? 1151 HOH A O     1 
HETATM 9913 O O     . HOH J 5 .   ? 38.588 10.794  -37.733 1.00 26.65 ? 1152 HOH A O     1 
HETATM 9914 O O     . HOH J 5 .   ? 8.860  -6.123  -80.291 1.00 40.87 ? 1153 HOH A O     1 
HETATM 9915 O O     . HOH J 5 .   ? 6.043  -26.052 -46.699 1.00 46.58 ? 1154 HOH A O     1 
HETATM 9916 O O     . HOH J 5 .   ? 52.814 -19.337 -50.820 1.00 42.29 ? 1155 HOH A O     1 
# 
