data_8UNI
# 
_entry.id   8UNI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   8UNI         pdb_00008uni 10.2210/pdb8uni/pdb 
WWPDB D_1000278477 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-05 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8UNI 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              andrea.mattevi@unipv.it 
_pdbx_contact_author.name_first         Andrea 
_pdbx_contact_author.name_last          Mattevi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9523-7128 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Caroli, J.'  1 0000-0001-8954-8045 
'Mattevi, A.' 2 0000-0002-9523-7128 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Distal drug resistance mutations promote covalent inhibitor-adduct Grob fragmentation in LSD1' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Caroli, J.'  1 0000-0001-8954-8045 
primary 'Mattevi, A.' 2 0000-0002-9523-7128 
# 
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 'Lysine-specific histone demethylase 1A' 95051.633 1 1.14.99.66 ?   ?                                        ? 
2 polymer     man 'REST corepressor 1' 16459.742 1 ?          ?   ?                                        ? 
3 polymer     man 'Histone H3 (Fragment)' 2263.666  1 ?          K4M 'residues 1-21 (2-22 Uniprot numbering)' ? 
4 non-polymer syn 
;[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-[5-methanoyl-7,8-dimethyl-2,4-bis(oxidanylidene)-1H-benzo[g]pteridin-10-yl]-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate
;
815.576   1 ?          ?   ?                                        ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;BRAF35-HDAC complex protein BHC110,Flavin-containing amine oxidase domain-containing protein 2,[histone H3]-dimethyl-L-lysine(4) FAD-dependent demethylase 1A
;
2 'Protein CoREST' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GSSHHHHHHSSGLVPRGSHMLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPR
KKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEER
NAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLW
LDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFG
MDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQE
FNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQ
YKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANA
TPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAV
LCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAP
ILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPIT
PGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM
;
;GSSHHHHHHSSGLVPRGSHMLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPR
KKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEER
NAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLW
LDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFG
MDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQE
FNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQ
YKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANA
TPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAV
LCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAP
ILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPIT
PGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM
;
A ? 
2 'polypeptide(L)' no no 
;GPLGSPEFRAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVI
QKCNARWTTEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAE
;
;GPLGSPEFRAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVI
QKCNARWTTEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAE
;
B ? 
3 'polypeptide(L)' no no ARTMQTARKSTGGKAPRKQLA ARTMQTARKSTGGKAPRKQLA C ? 
# 
_pdbx_entity_nonpoly.entity_id   4 
_pdbx_entity_nonpoly.name        
;[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-[5-methanoyl-7,8-dimethyl-2,4-bis(oxidanylidene)-1H-benzo[g]pteridin-10-yl]-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate
;
_pdbx_entity_nonpoly.comp_id     HUF 
# 
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   SER n 
1 3   SER n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  SER n 
1 11  SER n 
1 12  GLY n 
1 13  LEU n 
1 14  VAL n 
1 15  PRO n 
1 16  ARG n 
1 17  GLY n 
1 18  SER n 
1 19  HIS n 
1 20  MET n 
1 21  LEU n 
1 22  SER n 
1 23  GLY n 
1 24  LYS n 
1 25  LYS n 
1 26  ALA n 
1 27  ALA n 
1 28  ALA n 
1 29  ALA n 
1 30  ALA n 
1 31  ALA n 
1 32  ALA n 
1 33  ALA n 
1 34  ALA n 
1 35  ALA n 
1 36  ALA n 
1 37  ALA n 
1 38  THR n 
1 39  GLY n 
1 40  THR n 
1 41  GLU n 
1 42  ALA n 
1 43  GLY n 
1 44  PRO n 
1 45  GLY n 
1 46  THR n 
1 47  ALA n 
1 48  GLY n 
1 49  GLY n 
1 50  SER n 
1 51  GLU n 
1 52  ASN n 
1 53  GLY n 
1 54  SER n 
1 55  GLU n 
1 56  VAL n 
1 57  ALA n 
1 58  ALA n 
1 59  GLN n 
1 60  PRO n 
1 61  ALA n 
1 62  GLY n 
1 63  LEU n 
1 64  SER n 
1 65  GLY n 
1 66  PRO n 
1 67  ALA n 
1 68  GLU n 
1 69  VAL n 
1 70  GLY n 
1 71  PRO n 
1 72  GLY n 
1 73  ALA n 
1 74  VAL n 
1 75  GLY n 
1 76  GLU n 
1 77  ARG n 
1 78  THR n 
1 79  PRO n 
1 80  ARG n 
1 81  LYS n 
1 82  LYS n 
1 83  GLU n 
1 84  PRO n 
1 85  PRO n 
1 86  ARG n 
1 87  ALA n 
1 88  SER n 
1 89  PRO n 
1 90  PRO n 
1 91  GLY n 
1 92  GLY n 
1 93  LEU n 
1 94  ALA n 
1 95  GLU n 
1 96  PRO n 
1 97  PRO n 
1 98  GLY n 
1 99  SER n 
1 100 ALA n 
1 101 GLY n 
1 102 PRO n 
1 103 GLN n 
1 104 ALA n 
1 105 GLY n 
1 106 PRO n 
1 107 THR n 
1 108 VAL n 
1 109 VAL n 
1 110 PRO n 
1 111 GLY n 
1 112 SER n 
1 113 ALA n 
1 114 THR n 
1 115 PRO n 
1 116 MET n 
1 117 GLU n 
1 118 THR n 
1 119 GLY n 
1 120 ILE n 
1 121 ALA n 
1 122 GLU n 
1 123 THR n 
1 124 PRO n 
1 125 GLU n 
1 126 GLY n 
1 127 ARG n 
1 128 ARG n 
1 129 THR n 
1 130 SER n 
1 131 ARG n 
1 132 ARG n 
1 133 LYS n 
1 134 ARG n 
1 135 ALA n 
1 136 LYS n 
1 137 VAL n 
1 138 GLU n 
1 139 TYR n 
1 140 ARG n 
1 141 GLU n 
1 142 MET n 
1 143 ASP n 
1 144 GLU n 
1 145 SER n 
1 146 LEU n 
1 147 ALA n 
1 148 ASN n 
1 149 LEU n 
1 150 SER n 
1 151 GLU n 
1 152 ASP n 
1 153 GLU n 
1 154 TYR n 
1 155 TYR n 
1 156 SER n 
1 157 GLU n 
1 158 GLU n 
1 159 GLU n 
1 160 ARG n 
1 161 ASN n 
1 162 ALA n 
1 163 LYS n 
1 164 ALA n 
1 165 GLU n 
1 166 LYS n 
1 167 GLU n 
1 168 LYS n 
1 169 LYS n 
1 170 LEU n 
1 171 PRO n 
1 172 PRO n 
1 173 PRO n 
1 174 PRO n 
1 175 PRO n 
1 176 GLN n 
1 177 ALA n 
1 178 PRO n 
1 179 PRO n 
1 180 GLU n 
1 181 GLU n 
1 182 GLU n 
1 183 ASN n 
1 184 GLU n 
1 185 SER n 
1 186 GLU n 
1 187 PRO n 
1 188 GLU n 
1 189 GLU n 
1 190 PRO n 
1 191 SER n 
1 192 GLY n 
1 193 VAL n 
1 194 GLU n 
1 195 GLY n 
1 196 ALA n 
1 197 ALA n 
1 198 PHE n 
1 199 GLN n 
1 200 SER n 
1 201 ARG n 
1 202 LEU n 
1 203 PRO n 
1 204 HIS n 
1 205 ASP n 
1 206 ARG n 
1 207 MET n 
1 208 THR n 
1 209 SER n 
1 210 GLN n 
1 211 GLU n 
1 212 ALA n 
1 213 ALA n 
1 214 CYS n 
1 215 PHE n 
1 216 PRO n 
1 217 ASP n 
1 218 ILE n 
1 219 ILE n 
1 220 SER n 
1 221 GLY n 
1 222 PRO n 
1 223 GLN n 
1 224 GLN n 
1 225 THR n 
1 226 GLN n 
1 227 LYS n 
1 228 VAL n 
1 229 PHE n 
1 230 LEU n 
1 231 PHE n 
1 232 ILE n 
1 233 ARG n 
1 234 ASN n 
1 235 ARG n 
1 236 THR n 
1 237 LEU n 
1 238 GLN n 
1 239 LEU n 
1 240 TRP n 
1 241 LEU n 
1 242 ASP n 
1 243 ASN n 
1 244 PRO n 
1 245 LYS n 
1 246 ILE n 
1 247 GLN n 
1 248 LEU n 
1 249 THR n 
1 250 PHE n 
1 251 GLU n 
1 252 ALA n 
1 253 THR n 
1 254 LEU n 
1 255 GLN n 
1 256 GLN n 
1 257 LEU n 
1 258 GLU n 
1 259 ALA n 
1 260 PRO n 
1 261 TYR n 
1 262 ASN n 
1 263 SER n 
1 264 ASP n 
1 265 THR n 
1 266 VAL n 
1 267 LEU n 
1 268 VAL n 
1 269 HIS n 
1 270 ARG n 
1 271 VAL n 
1 272 HIS n 
1 273 SER n 
1 274 TYR n 
1 275 LEU n 
1 276 GLU n 
1 277 ARG n 
1 278 HIS n 
1 279 GLY n 
1 280 LEU n 
1 281 ILE n 
1 282 ASN n 
1 283 PHE n 
1 284 GLY n 
1 285 ILE n 
1 286 TYR n 
1 287 LYS n 
1 288 ARG n 
1 289 ILE n 
1 290 LYS n 
1 291 PRO n 
1 292 LEU n 
1 293 PRO n 
1 294 THR n 
1 295 LYS n 
1 296 LYS n 
1 297 THR n 
1 298 GLY n 
1 299 LYS n 
1 300 VAL n 
1 301 ILE n 
1 302 ILE n 
1 303 ILE n 
1 304 GLY n 
1 305 SER n 
1 306 GLY n 
1 307 VAL n 
1 308 SER n 
1 309 GLY n 
1 310 LEU n 
1 311 ALA n 
1 312 ALA n 
1 313 ALA n 
1 314 ARG n 
1 315 GLN n 
1 316 LEU n 
1 317 GLN n 
1 318 SER n 
1 319 PHE n 
1 320 GLY n 
1 321 MET n 
1 322 ASP n 
1 323 VAL n 
1 324 THR n 
1 325 LEU n 
1 326 LEU n 
1 327 GLU n 
1 328 ALA n 
1 329 ARG n 
1 330 ASP n 
1 331 ARG n 
1 332 VAL n 
1 333 GLY n 
1 334 GLY n 
1 335 ARG n 
1 336 VAL n 
1 337 ALA n 
1 338 THR n 
1 339 PHE n 
1 340 ARG n 
1 341 LYS n 
1 342 GLY n 
1 343 ASN n 
1 344 TYR n 
1 345 VAL n 
1 346 ALA n 
1 347 ASP n 
1 348 LEU n 
1 349 GLY n 
1 350 ALA n 
1 351 MET n 
1 352 VAL n 
1 353 VAL n 
1 354 THR n 
1 355 GLY n 
1 356 LEU n 
1 357 GLY n 
1 358 GLY n 
1 359 ASN n 
1 360 PRO n 
1 361 MET n 
1 362 ALA n 
1 363 VAL n 
1 364 VAL n 
1 365 SER n 
1 366 LYS n 
1 367 GLN n 
1 368 VAL n 
1 369 ASN n 
1 370 MET n 
1 371 GLU n 
1 372 LEU n 
1 373 ALA n 
1 374 LYS n 
1 375 ILE n 
1 376 LYS n 
1 377 GLN n 
1 378 LYS n 
1 379 CYS n 
1 380 PRO n 
1 381 LEU n 
1 382 TYR n 
1 383 GLU n 
1 384 ALA n 
1 385 ASN n 
1 386 GLY n 
1 387 GLN n 
1 388 ALA n 
1 389 VAL n 
1 390 PRO n 
1 391 LYS n 
1 392 GLU n 
1 393 LYS n 
1 394 ASP n 
1 395 GLU n 
1 396 MET n 
1 397 VAL n 
1 398 GLU n 
1 399 GLN n 
1 400 GLU n 
1 401 PHE n 
1 402 ASN n 
1 403 ARG n 
1 404 LEU n 
1 405 LEU n 
1 406 GLU n 
1 407 ALA n 
1 408 THR n 
1 409 SER n 
1 410 TYR n 
1 411 LEU n 
1 412 SER n 
1 413 HIS n 
1 414 GLN n 
1 415 LEU n 
1 416 ASP n 
1 417 PHE n 
1 418 ASN n 
1 419 VAL n 
1 420 LEU n 
1 421 ASN n 
1 422 ASN n 
1 423 LYS n 
1 424 PRO n 
1 425 VAL n 
1 426 SER n 
1 427 LEU n 
1 428 GLY n 
1 429 GLN n 
1 430 ALA n 
1 431 LEU n 
1 432 GLU n 
1 433 VAL n 
1 434 VAL n 
1 435 ILE n 
1 436 GLN n 
1 437 LEU n 
1 438 GLN n 
1 439 GLU n 
1 440 LYS n 
1 441 HIS n 
1 442 VAL n 
1 443 LYS n 
1 444 ASP n 
1 445 GLU n 
1 446 GLN n 
1 447 ILE n 
1 448 GLU n 
1 449 HIS n 
1 450 TRP n 
1 451 LYS n 
1 452 LYS n 
1 453 ILE n 
1 454 VAL n 
1 455 LYS n 
1 456 THR n 
1 457 GLN n 
1 458 GLU n 
1 459 GLU n 
1 460 LEU n 
1 461 LYS n 
1 462 GLU n 
1 463 LEU n 
1 464 LEU n 
1 465 ASN n 
1 466 LYS n 
1 467 MET n 
1 468 VAL n 
1 469 ASN n 
1 470 LEU n 
1 471 LYS n 
1 472 GLU n 
1 473 LYS n 
1 474 ILE n 
1 475 LYS n 
1 476 GLU n 
1 477 LEU n 
1 478 HIS n 
1 479 GLN n 
1 480 GLN n 
1 481 TYR n 
1 482 LYS n 
1 483 GLU n 
1 484 ALA n 
1 485 SER n 
1 486 GLU n 
1 487 VAL n 
1 488 LYS n 
1 489 PRO n 
1 490 PRO n 
1 491 ARG n 
1 492 ASP n 
1 493 ILE n 
1 494 THR n 
1 495 ALA n 
1 496 GLU n 
1 497 PHE n 
1 498 LEU n 
1 499 VAL n 
1 500 LYS n 
1 501 SER n 
1 502 LYS n 
1 503 HIS n 
1 504 ARG n 
1 505 ASP n 
1 506 LEU n 
1 507 THR n 
1 508 ALA n 
1 509 LEU n 
1 510 CYS n 
1 511 LYS n 
1 512 GLU n 
1 513 TYR n 
1 514 ASP n 
1 515 GLU n 
1 516 LEU n 
1 517 ALA n 
1 518 GLU n 
1 519 THR n 
1 520 GLN n 
1 521 GLY n 
1 522 LYS n 
1 523 LEU n 
1 524 GLU n 
1 525 GLU n 
1 526 LYS n 
1 527 LEU n 
1 528 GLN n 
1 529 GLU n 
1 530 LEU n 
1 531 GLU n 
1 532 ALA n 
1 533 ASN n 
1 534 PRO n 
1 535 PRO n 
1 536 SER n 
1 537 ASP n 
1 538 VAL n 
1 539 TYR n 
1 540 LEU n 
1 541 SER n 
1 542 SER n 
1 543 ARG n 
1 544 ASP n 
1 545 ARG n 
1 546 GLN n 
1 547 ILE n 
1 548 LEU n 
1 549 ASP n 
1 550 TRP n 
1 551 HIS n 
1 552 PHE n 
1 553 ALA n 
1 554 ASN n 
1 555 LEU n 
1 556 GLU n 
1 557 PHE n 
1 558 ALA n 
1 559 ASN n 
1 560 ALA n 
1 561 THR n 
1 562 PRO n 
1 563 LEU n 
1 564 SER n 
1 565 THR n 
1 566 LEU n 
1 567 SER n 
1 568 LEU n 
1 569 LYS n 
1 570 HIS n 
1 571 TRP n 
1 572 ASP n 
1 573 GLN n 
1 574 ASP n 
1 575 ASP n 
1 576 ASP n 
1 577 PHE n 
1 578 GLU n 
1 579 PHE n 
1 580 THR n 
1 581 GLY n 
1 582 SER n 
1 583 HIS n 
1 584 LEU n 
1 585 THR n 
1 586 VAL n 
1 587 ARG n 
1 588 ASN n 
1 589 GLY n 
1 590 TYR n 
1 591 SER n 
1 592 CYS n 
1 593 VAL n 
1 594 PRO n 
1 595 VAL n 
1 596 ALA n 
1 597 LEU n 
1 598 ALA n 
1 599 GLU n 
1 600 GLY n 
1 601 LEU n 
1 602 ASP n 
1 603 ILE n 
1 604 LYS n 
1 605 LEU n 
1 606 ASN n 
1 607 THR n 
1 608 ALA n 
1 609 VAL n 
1 610 ARG n 
1 611 GLN n 
1 612 VAL n 
1 613 ARG n 
1 614 TYR n 
1 615 THR n 
1 616 ALA n 
1 617 SER n 
1 618 GLY n 
1 619 CYS n 
1 620 GLU n 
1 621 VAL n 
1 622 ILE n 
1 623 ALA n 
1 624 VAL n 
1 625 ASN n 
1 626 THR n 
1 627 ARG n 
1 628 SER n 
1 629 THR n 
1 630 SER n 
1 631 GLN n 
1 632 THR n 
1 633 PHE n 
1 634 ILE n 
1 635 TYR n 
1 636 LYS n 
1 637 CYS n 
1 638 ASP n 
1 639 ALA n 
1 640 VAL n 
1 641 LEU n 
1 642 CYS n 
1 643 THR n 
1 644 LEU n 
1 645 PRO n 
1 646 LEU n 
1 647 GLY n 
1 648 VAL n 
1 649 LEU n 
1 650 LYS n 
1 651 GLN n 
1 652 GLN n 
1 653 PRO n 
1 654 PRO n 
1 655 ALA n 
1 656 VAL n 
1 657 GLN n 
1 658 PHE n 
1 659 VAL n 
1 660 PRO n 
1 661 PRO n 
1 662 LEU n 
1 663 PRO n 
1 664 GLU n 
1 665 TRP n 
1 666 LYS n 
1 667 THR n 
1 668 SER n 
1 669 ALA n 
1 670 VAL n 
1 671 GLN n 
1 672 ARG n 
1 673 MET n 
1 674 GLY n 
1 675 PHE n 
1 676 GLY n 
1 677 ASN n 
1 678 LEU n 
1 679 ASN n 
1 680 LYS n 
1 681 VAL n 
1 682 VAL n 
1 683 LEU n 
1 684 CYS n 
1 685 PHE n 
1 686 ASP n 
1 687 ARG n 
1 688 VAL n 
1 689 PHE n 
1 690 TRP n 
1 691 ASP n 
1 692 PRO n 
1 693 SER n 
1 694 VAL n 
1 695 ASN n 
1 696 LEU n 
1 697 PHE n 
1 698 GLY n 
1 699 HIS n 
1 700 VAL n 
1 701 GLY n 
1 702 SER n 
1 703 THR n 
1 704 THR n 
1 705 ALA n 
1 706 SER n 
1 707 ARG n 
1 708 GLY n 
1 709 GLU n 
1 710 LEU n 
1 711 PHE n 
1 712 LEU n 
1 713 PHE n 
1 714 TRP n 
1 715 ASN n 
1 716 LEU n 
1 717 TYR n 
1 718 LYS n 
1 719 ALA n 
1 720 PRO n 
1 721 ILE n 
1 722 LEU n 
1 723 LEU n 
1 724 ALA n 
1 725 LEU n 
1 726 VAL n 
1 727 ALA n 
1 728 GLY n 
1 729 GLU n 
1 730 ALA n 
1 731 ALA n 
1 732 GLY n 
1 733 ILE n 
1 734 MET n 
1 735 GLU n 
1 736 ASN n 
1 737 ILE n 
1 738 SER n 
1 739 ASP n 
1 740 ASP n 
1 741 VAL n 
1 742 ILE n 
1 743 VAL n 
1 744 GLY n 
1 745 ARG n 
1 746 CYS n 
1 747 LEU n 
1 748 ALA n 
1 749 ILE n 
1 750 LEU n 
1 751 LYS n 
1 752 GLY n 
1 753 ILE n 
1 754 PHE n 
1 755 GLY n 
1 756 SER n 
1 757 SER n 
1 758 ALA n 
1 759 VAL n 
1 760 PRO n 
1 761 GLN n 
1 762 PRO n 
1 763 LYS n 
1 764 GLU n 
1 765 THR n 
1 766 VAL n 
1 767 VAL n 
1 768 SER n 
1 769 ARG n 
1 770 TRP n 
1 771 ARG n 
1 772 ALA n 
1 773 ASP n 
1 774 PRO n 
1 775 TRP n 
1 776 ALA n 
1 777 ARG n 
1 778 GLY n 
1 779 SER n 
1 780 TYR n 
1 781 SER n 
1 782 TYR n 
1 783 VAL n 
1 784 ALA n 
1 785 ALA n 
1 786 GLY n 
1 787 SER n 
1 788 SER n 
1 789 GLY n 
1 790 ASN n 
1 791 ASP n 
1 792 TYR n 
1 793 ASP n 
1 794 LEU n 
1 795 MET n 
1 796 ALA n 
1 797 GLN n 
1 798 PRO n 
1 799 ILE n 
1 800 THR n 
1 801 PRO n 
1 802 GLY n 
1 803 PRO n 
1 804 SER n 
1 805 ILE n 
1 806 PRO n 
1 807 GLY n 
1 808 ALA n 
1 809 PRO n 
1 810 GLN n 
1 811 PRO n 
1 812 ILE n 
1 813 PRO n 
1 814 ARG n 
1 815 LEU n 
1 816 PHE n 
1 817 PHE n 
1 818 ALA n 
1 819 GLY n 
1 820 GLU n 
1 821 HIS n 
1 822 THR n 
1 823 ILE n 
1 824 ARG n 
1 825 ASN n 
1 826 TYR n 
1 827 PRO n 
1 828 ALA n 
1 829 THR n 
1 830 VAL n 
1 831 HIS n 
1 832 GLY n 
1 833 ALA n 
1 834 LEU n 
1 835 LEU n 
1 836 SER n 
1 837 GLY n 
1 838 LEU n 
1 839 ARG n 
1 840 GLU n 
1 841 ALA n 
1 842 GLY n 
1 843 ARG n 
1 844 ILE n 
1 845 ALA n 
1 846 ASP n 
1 847 GLN n 
1 848 PHE n 
1 849 LEU n 
1 850 GLY n 
1 851 ALA n 
1 852 MET n 
1 853 TYR n 
1 854 THR n 
1 855 LEU n 
1 856 PRO n 
1 857 ARG n 
1 858 GLN n 
1 859 ALA n 
1 860 THR n 
1 861 PRO n 
1 862 GLY n 
1 863 VAL n 
1 864 PRO n 
1 865 ALA n 
1 866 GLN n 
1 867 GLN n 
1 868 SER n 
1 869 PRO n 
1 870 SER n 
1 871 MET n 
2 1   GLY n 
2 2   PRO n 
2 3   LEU n 
2 4   GLY n 
2 5   SER n 
2 6   PRO n 
2 7   GLU n 
2 8   PHE n 
2 9   ARG n 
2 10  ALA n 
2 11  LYS n 
2 12  ARG n 
2 13  LYS n 
2 14  PRO n 
2 15  PRO n 
2 16  LYS n 
2 17  GLY n 
2 18  MET n 
2 19  PHE n 
2 20  LEU n 
2 21  SER n 
2 22  GLN n 
2 23  GLU n 
2 24  ASP n 
2 25  VAL n 
2 26  GLU n 
2 27  ALA n 
2 28  VAL n 
2 29  SER n 
2 30  ALA n 
2 31  ASN n 
2 32  ALA n 
2 33  THR n 
2 34  ALA n 
2 35  ALA n 
2 36  THR n 
2 37  THR n 
2 38  VAL n 
2 39  LEU n 
2 40  ARG n 
2 41  GLN n 
2 42  LEU n 
2 43  ASP n 
2 44  MET n 
2 45  GLU n 
2 46  LEU n 
2 47  VAL n 
2 48  SER n 
2 49  VAL n 
2 50  LYS n 
2 51  ARG n 
2 52  GLN n 
2 53  ILE n 
2 54  GLN n 
2 55  ASN n 
2 56  ILE n 
2 57  LYS n 
2 58  GLN n 
2 59  THR n 
2 60  ASN n 
2 61  SER n 
2 62  ALA n 
2 63  LEU n 
2 64  LYS n 
2 65  GLU n 
2 66  LYS n 
2 67  LEU n 
2 68  ASP n 
2 69  GLY n 
2 70  GLY n 
2 71  ILE n 
2 72  GLU n 
2 73  PRO n 
2 74  TYR n 
2 75  ARG n 
2 76  LEU n 
2 77  PRO n 
2 78  GLU n 
2 79  VAL n 
2 80  ILE n 
2 81  GLN n 
2 82  LYS n 
2 83  CYS n 
2 84  ASN n 
2 85  ALA n 
2 86  ARG n 
2 87  TRP n 
2 88  THR n 
2 89  THR n 
2 90  GLU n 
2 91  GLU n 
2 92  GLN n 
2 93  LEU n 
2 94  LEU n 
2 95  ALA n 
2 96  VAL n 
2 97  GLN n 
2 98  ALA n 
2 99  ILE n 
2 100 ARG n 
2 101 LYS n 
2 102 TYR n 
2 103 GLY n 
2 104 ARG n 
2 105 ASP n 
2 106 PHE n 
2 107 GLN n 
2 108 ALA n 
2 109 ILE n 
2 110 SER n 
2 111 ASP n 
2 112 VAL n 
2 113 ILE n 
2 114 GLY n 
2 115 ASN n 
2 116 LYS n 
2 117 SER n 
2 118 VAL n 
2 119 VAL n 
2 120 GLN n 
2 121 VAL n 
2 122 LYS n 
2 123 ASN n 
2 124 PHE n 
2 125 PHE n 
2 126 VAL n 
2 127 ASN n 
2 128 TYR n 
2 129 ARG n 
2 130 ARG n 
2 131 ARG n 
2 132 PHE n 
2 133 ASN n 
2 134 ILE n 
2 135 ASP n 
2 136 GLU n 
2 137 VAL n 
2 138 LEU n 
2 139 GLN n 
2 140 GLU n 
2 141 TRP n 
2 142 GLU n 
2 143 ALA n 
2 144 GLU n 
3 1   ALA n 
3 2   ARG n 
3 3   THR n 
3 4   MET n 
3 5   GLN n 
3 6   THR n 
3 7   ALA n 
3 8   ARG n 
3 9   LYS n 
3 10  SER n 
3 11  THR n 
3 12  GLY n 
3 13  GLY n 
3 14  LYS n 
3 15  ALA n 
3 16  PRO n 
3 17  ARG n 
3 18  LYS n 
3 19  GLN n 
3 20  LEU n 
3 21  ALA n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 871 human ? 'KDM1A, AOF2, KDM1, KIAA0601, LSD1' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 144 human ? 'RCOR1, KIAA0071, RCOR'             ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 21  human ? ?                                   ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'    156.162 
HUF non-polymer         . 
;[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-[5-methanoyl-7,8-dimethyl-2,4-bis(oxidanylidene)-1H-benzo[g]pteridin-10-yl]-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate
;
? 'C28 H35 N9 O16 P2' 815.576 
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -18 ?   ?   ?   A . n 
A 1 2   SER 2   -17 ?   ?   ?   A . n 
A 1 3   SER 3   -16 ?   ?   ?   A . n 
A 1 4   HIS 4   -15 ?   ?   ?   A . n 
A 1 5   HIS 5   -14 ?   ?   ?   A . n 
A 1 6   HIS 6   -13 ?   ?   ?   A . n 
A 1 7   HIS 7   -12 ?   ?   ?   A . n 
A 1 8   HIS 8   -11 ?   ?   ?   A . n 
A 1 9   HIS 9   -10 ?   ?   ?   A . n 
A 1 10  SER 10  -9  ?   ?   ?   A . n 
A 1 11  SER 11  -8  ?   ?   ?   A . n 
A 1 12  GLY 12  -7  ?   ?   ?   A . n 
A 1 13  LEU 13  -6  ?   ?   ?   A . n 
A 1 14  VAL 14  -5  ?   ?   ?   A . n 
A 1 15  PRO 15  -4  ?   ?   ?   A . n 
A 1 16  ARG 16  -3  ?   ?   ?   A . n 
A 1 17  GLY 17  -2  ?   ?   ?   A . n 
A 1 18  SER 18  -1  ?   ?   ?   A . n 
A 1 19  HIS 19  0   ?   ?   ?   A . n 
A 1 20  MET 20  1   ?   ?   ?   A . n 
A 1 21  LEU 21  2   ?   ?   ?   A . n 
A 1 22  SER 22  3   ?   ?   ?   A . n 
A 1 23  GLY 23  4   ?   ?   ?   A . n 
A 1 24  LYS 24  5   ?   ?   ?   A . n 
A 1 25  LYS 25  6   ?   ?   ?   A . n 
A 1 26  ALA 26  7   ?   ?   ?   A . n 
A 1 27  ALA 27  8   ?   ?   ?   A . n 
A 1 28  ALA 28  9   ?   ?   ?   A . n 
A 1 29  ALA 29  10  ?   ?   ?   A . n 
A 1 30  ALA 30  11  ?   ?   ?   A . n 
A 1 31  ALA 31  12  ?   ?   ?   A . n 
A 1 32  ALA 32  13  ?   ?   ?   A . n 
A 1 33  ALA 33  14  ?   ?   ?   A . n 
A 1 34  ALA 34  15  ?   ?   ?   A . n 
A 1 35  ALA 35  16  ?   ?   ?   A . n 
A 1 36  ALA 36  17  ?   ?   ?   A . n 
A 1 37  ALA 37  18  ?   ?   ?   A . n 
A 1 38  THR 38  19  ?   ?   ?   A . n 
A 1 39  GLY 39  20  ?   ?   ?   A . n 
A 1 40  THR 40  21  ?   ?   ?   A . n 
A 1 41  GLU 41  22  ?   ?   ?   A . n 
A 1 42  ALA 42  23  ?   ?   ?   A . n 
A 1 43  GLY 43  24  ?   ?   ?   A . n 
A 1 44  PRO 44  25  ?   ?   ?   A . n 
A 1 45  GLY 45  26  ?   ?   ?   A . n 
A 1 46  THR 46  27  ?   ?   ?   A . n 
A 1 47  ALA 47  28  ?   ?   ?   A . n 
A 1 48  GLY 48  29  ?   ?   ?   A . n 
A 1 49  GLY 49  30  ?   ?   ?   A . n 
A 1 50  SER 50  31  ?   ?   ?   A . n 
A 1 51  GLU 51  32  ?   ?   ?   A . n 
A 1 52  ASN 52  33  ?   ?   ?   A . n 
A 1 53  GLY 53  34  ?   ?   ?   A . n 
A 1 54  SER 54  35  ?   ?   ?   A . n 
A 1 55  GLU 55  36  ?   ?   ?   A . n 
A 1 56  VAL 56  37  ?   ?   ?   A . n 
A 1 57  ALA 57  38  ?   ?   ?   A . n 
A 1 58  ALA 58  39  ?   ?   ?   A . n 
A 1 59  GLN 59  40  ?   ?   ?   A . n 
A 1 60  PRO 60  41  ?   ?   ?   A . n 
A 1 61  ALA 61  42  ?   ?   ?   A . n 
A 1 62  GLY 62  43  ?   ?   ?   A . n 
A 1 63  LEU 63  44  ?   ?   ?   A . n 
A 1 64  SER 64  45  ?   ?   ?   A . n 
A 1 65  GLY 65  46  ?   ?   ?   A . n 
A 1 66  PRO 66  47  ?   ?   ?   A . n 
A 1 67  ALA 67  48  ?   ?   ?   A . n 
A 1 68  GLU 68  49  ?   ?   ?   A . n 
A 1 69  VAL 69  50  ?   ?   ?   A . n 
A 1 70  GLY 70  51  ?   ?   ?   A . n 
A 1 71  PRO 71  52  ?   ?   ?   A . n 
A 1 72  GLY 72  53  ?   ?   ?   A . n 
A 1 73  ALA 73  54  ?   ?   ?   A . n 
A 1 74  VAL 74  55  ?   ?   ?   A . n 
A 1 75  GLY 75  56  ?   ?   ?   A . n 
A 1 76  GLU 76  57  ?   ?   ?   A . n 
A 1 77  ARG 77  58  ?   ?   ?   A . n 
A 1 78  THR 78  59  ?   ?   ?   A . n 
A 1 79  PRO 79  60  ?   ?   ?   A . n 
A 1 80  ARG 80  61  ?   ?   ?   A . n 
A 1 81  LYS 81  62  ?   ?   ?   A . n 
A 1 82  LYS 82  63  ?   ?   ?   A . n 
A 1 83  GLU 83  64  ?   ?   ?   A . n 
A 1 84  PRO 84  65  ?   ?   ?   A . n 
A 1 85  PRO 85  66  ?   ?   ?   A . n 
A 1 86  ARG 86  67  ?   ?   ?   A . n 
A 1 87  ALA 87  68  ?   ?   ?   A . n 
A 1 88  SER 88  69  ?   ?   ?   A . n 
A 1 89  PRO 89  70  ?   ?   ?   A . n 
A 1 90  PRO 90  71  ?   ?   ?   A . n 
A 1 91  GLY 91  72  ?   ?   ?   A . n 
A 1 92  GLY 92  73  ?   ?   ?   A . n 
A 1 93  LEU 93  74  ?   ?   ?   A . n 
A 1 94  ALA 94  75  ?   ?   ?   A . n 
A 1 95  GLU 95  76  ?   ?   ?   A . n 
A 1 96  PRO 96  77  ?   ?   ?   A . n 
A 1 97  PRO 97  78  ?   ?   ?   A . n 
A 1 98  GLY 98  79  ?   ?   ?   A . n 
A 1 99  SER 99  80  ?   ?   ?   A . n 
A 1 100 ALA 100 81  ?   ?   ?   A . n 
A 1 101 GLY 101 82  ?   ?   ?   A . n 
A 1 102 PRO 102 83  ?   ?   ?   A . n 
A 1 103 GLN 103 84  ?   ?   ?   A . n 
A 1 104 ALA 104 85  ?   ?   ?   A . n 
A 1 105 GLY 105 86  ?   ?   ?   A . n 
A 1 106 PRO 106 87  ?   ?   ?   A . n 
A 1 107 THR 107 88  ?   ?   ?   A . n 
A 1 108 VAL 108 89  ?   ?   ?   A . n 
A 1 109 VAL 109 90  ?   ?   ?   A . n 
A 1 110 PRO 110 91  ?   ?   ?   A . n 
A 1 111 GLY 111 92  ?   ?   ?   A . n 
A 1 112 SER 112 93  ?   ?   ?   A . n 
A 1 113 ALA 113 94  ?   ?   ?   A . n 
A 1 114 THR 114 95  ?   ?   ?   A . n 
A 1 115 PRO 115 96  ?   ?   ?   A . n 
A 1 116 MET 116 97  ?   ?   ?   A . n 
A 1 117 GLU 117 98  ?   ?   ?   A . n 
A 1 118 THR 118 99  ?   ?   ?   A . n 
A 1 119 GLY 119 100 ?   ?   ?   A . n 
A 1 120 ILE 120 101 ?   ?   ?   A . n 
A 1 121 ALA 121 102 ?   ?   ?   A . n 
A 1 122 GLU 122 103 ?   ?   ?   A . n 
A 1 123 THR 123 104 ?   ?   ?   A . n 
A 1 124 PRO 124 105 ?   ?   ?   A . n 
A 1 125 GLU 125 106 ?   ?   ?   A . n 
A 1 126 GLY 126 107 ?   ?   ?   A . n 
A 1 127 ARG 127 108 ?   ?   ?   A . n 
A 1 128 ARG 128 109 ?   ?   ?   A . n 
A 1 129 THR 129 110 ?   ?   ?   A . n 
A 1 130 SER 130 111 ?   ?   ?   A . n 
A 1 131 ARG 131 112 ?   ?   ?   A . n 
A 1 132 ARG 132 113 ?   ?   ?   A . n 
A 1 133 LYS 133 114 ?   ?   ?   A . n 
A 1 134 ARG 134 115 ?   ?   ?   A . n 
A 1 135 ALA 135 116 ?   ?   ?   A . n 
A 1 136 LYS 136 117 ?   ?   ?   A . n 
A 1 137 VAL 137 118 ?   ?   ?   A . n 
A 1 138 GLU 138 119 ?   ?   ?   A . n 
A 1 139 TYR 139 120 ?   ?   ?   A . n 
A 1 140 ARG 140 121 ?   ?   ?   A . n 
A 1 141 GLU 141 122 ?   ?   ?   A . n 
A 1 142 MET 142 123 ?   ?   ?   A . n 
A 1 143 ASP 143 124 ?   ?   ?   A . n 
A 1 144 GLU 144 125 ?   ?   ?   A . n 
A 1 145 SER 145 126 ?   ?   ?   A . n 
A 1 146 LEU 146 127 ?   ?   ?   A . n 
A 1 147 ALA 147 128 ?   ?   ?   A . n 
A 1 148 ASN 148 129 ?   ?   ?   A . n 
A 1 149 LEU 149 130 ?   ?   ?   A . n 
A 1 150 SER 150 131 ?   ?   ?   A . n 
A 1 151 GLU 151 132 ?   ?   ?   A . n 
A 1 152 ASP 152 133 ?   ?   ?   A . n 
A 1 153 GLU 153 134 ?   ?   ?   A . n 
A 1 154 TYR 154 135 ?   ?   ?   A . n 
A 1 155 TYR 155 136 ?   ?   ?   A . n 
A 1 156 SER 156 137 ?   ?   ?   A . n 
A 1 157 GLU 157 138 ?   ?   ?   A . n 
A 1 158 GLU 158 139 ?   ?   ?   A . n 
A 1 159 GLU 159 140 ?   ?   ?   A . n 
A 1 160 ARG 160 141 ?   ?   ?   A . n 
A 1 161 ASN 161 142 ?   ?   ?   A . n 
A 1 162 ALA 162 143 ?   ?   ?   A . n 
A 1 163 LYS 163 144 ?   ?   ?   A . n 
A 1 164 ALA 164 145 ?   ?   ?   A . n 
A 1 165 GLU 165 146 ?   ?   ?   A . n 
A 1 166 LYS 166 147 ?   ?   ?   A . n 
A 1 167 GLU 167 148 ?   ?   ?   A . n 
A 1 168 LYS 168 149 ?   ?   ?   A . n 
A 1 169 LYS 169 150 ?   ?   ?   A . n 
A 1 170 LEU 170 151 ?   ?   ?   A . n 
A 1 171 PRO 171 152 ?   ?   ?   A . n 
A 1 172 PRO 172 153 ?   ?   ?   A . n 
A 1 173 PRO 173 154 ?   ?   ?   A . n 
A 1 174 PRO 174 155 ?   ?   ?   A . n 
A 1 175 PRO 175 156 ?   ?   ?   A . n 
A 1 176 GLN 176 157 ?   ?   ?   A . n 
A 1 177 ALA 177 158 ?   ?   ?   A . n 
A 1 178 PRO 178 159 ?   ?   ?   A . n 
A 1 179 PRO 179 160 ?   ?   ?   A . n 
A 1 180 GLU 180 161 ?   ?   ?   A . n 
A 1 181 GLU 181 162 ?   ?   ?   A . n 
A 1 182 GLU 182 163 ?   ?   ?   A . n 
A 1 183 ASN 183 164 ?   ?   ?   A . n 
A 1 184 GLU 184 165 ?   ?   ?   A . n 
A 1 185 SER 185 166 ?   ?   ?   A . n 
A 1 186 GLU 186 167 ?   ?   ?   A . n 
A 1 187 PRO 187 168 ?   ?   ?   A . n 
A 1 188 GLU 188 169 ?   ?   ?   A . n 
A 1 189 GLU 189 170 ?   ?   ?   A . n 
A 1 190 PRO 190 171 171 PRO PRO A . n 
A 1 191 SER 191 172 172 SER SER A . n 
A 1 192 GLY 192 173 173 GLY GLY A . n 
A 1 193 VAL 193 174 174 VAL VAL A . n 
A 1 194 GLU 194 175 175 GLU GLU A . n 
A 1 195 GLY 195 176 176 GLY GLY A . n 
A 1 196 ALA 196 177 177 ALA ALA A . n 
A 1 197 ALA 197 178 178 ALA ALA A . n 
A 1 198 PHE 198 179 179 PHE PHE A . n 
A 1 199 GLN 199 180 180 GLN GLN A . n 
A 1 200 SER 200 181 181 SER SER A . n 
A 1 201 ARG 201 182 182 ARG ARG A . n 
A 1 202 LEU 202 183 183 LEU LEU A . n 
A 1 203 PRO 203 184 184 PRO PRO A . n 
A 1 204 HIS 204 185 185 HIS HIS A . n 
A 1 205 ASP 205 186 186 ASP ASP A . n 
A 1 206 ARG 206 187 187 ARG ARG A . n 
A 1 207 MET 207 188 188 MET MET A . n 
A 1 208 THR 208 189 189 THR THR A . n 
A 1 209 SER 209 190 190 SER SER A . n 
A 1 210 GLN 210 191 191 GLN GLN A . n 
A 1 211 GLU 211 192 192 GLU GLU A . n 
A 1 212 ALA 212 193 193 ALA ALA A . n 
A 1 213 ALA 213 194 194 ALA ALA A . n 
A 1 214 CYS 214 195 195 CYS CYS A . n 
A 1 215 PHE 215 196 196 PHE PHE A . n 
A 1 216 PRO 216 197 197 PRO PRO A . n 
A 1 217 ASP 217 198 198 ASP ASP A . n 
A 1 218 ILE 218 199 199 ILE ILE A . n 
A 1 219 ILE 219 200 200 ILE ILE A . n 
A 1 220 SER 220 201 201 SER SER A . n 
A 1 221 GLY 221 202 202 GLY GLY A . n 
A 1 222 PRO 222 203 203 PRO PRO A . n 
A 1 223 GLN 223 204 204 GLN GLN A . n 
A 1 224 GLN 224 205 205 GLN GLN A . n 
A 1 225 THR 225 206 206 THR THR A . n 
A 1 226 GLN 226 207 207 GLN GLN A . n 
A 1 227 LYS 227 208 208 LYS LYS A . n 
A 1 228 VAL 228 209 209 VAL VAL A . n 
A 1 229 PHE 229 210 210 PHE PHE A . n 
A 1 230 LEU 230 211 211 LEU LEU A . n 
A 1 231 PHE 231 212 212 PHE PHE A . n 
A 1 232 ILE 232 213 213 ILE ILE A . n 
A 1 233 ARG 233 214 214 ARG ARG A . n 
A 1 234 ASN 234 215 215 ASN ASN A . n 
A 1 235 ARG 235 216 216 ARG ARG A . n 
A 1 236 THR 236 217 217 THR THR A . n 
A 1 237 LEU 237 218 218 LEU LEU A . n 
A 1 238 GLN 238 219 219 GLN GLN A . n 
A 1 239 LEU 239 220 220 LEU LEU A . n 
A 1 240 TRP 240 221 221 TRP TRP A . n 
A 1 241 LEU 241 222 222 LEU LEU A . n 
A 1 242 ASP 242 223 223 ASP ASP A . n 
A 1 243 ASN 243 224 224 ASN ASN A . n 
A 1 244 PRO 244 225 225 PRO PRO A . n 
A 1 245 LYS 245 226 226 LYS LYS A . n 
A 1 246 ILE 246 227 227 ILE ILE A . n 
A 1 247 GLN 247 228 228 GLN GLN A . n 
A 1 248 LEU 248 229 229 LEU LEU A . n 
A 1 249 THR 249 230 230 THR THR A . n 
A 1 250 PHE 250 231 231 PHE PHE A . n 
A 1 251 GLU 251 232 232 GLU GLU A . n 
A 1 252 ALA 252 233 233 ALA ALA A . n 
A 1 253 THR 253 234 234 THR THR A . n 
A 1 254 LEU 254 235 235 LEU LEU A . n 
A 1 255 GLN 255 236 236 GLN GLN A . n 
A 1 256 GLN 256 237 237 GLN GLN A . n 
A 1 257 LEU 257 238 238 LEU LEU A . n 
A 1 258 GLU 258 239 239 GLU GLU A . n 
A 1 259 ALA 259 240 240 ALA ALA A . n 
A 1 260 PRO 260 241 241 PRO PRO A . n 
A 1 261 TYR 261 242 242 TYR TYR A . n 
A 1 262 ASN 262 243 243 ASN ASN A . n 
A 1 263 SER 263 244 244 SER SER A . n 
A 1 264 ASP 264 245 245 ASP ASP A . n 
A 1 265 THR 265 246 246 THR THR A . n 
A 1 266 VAL 266 247 247 VAL VAL A . n 
A 1 267 LEU 267 248 248 LEU LEU A . n 
A 1 268 VAL 268 249 249 VAL VAL A . n 
A 1 269 HIS 269 250 250 HIS HIS A . n 
A 1 270 ARG 270 251 251 ARG ARG A . n 
A 1 271 VAL 271 252 252 VAL VAL A . n 
A 1 272 HIS 272 253 253 HIS HIS A . n 
A 1 273 SER 273 254 254 SER SER A . n 
A 1 274 TYR 274 255 255 TYR TYR A . n 
A 1 275 LEU 275 256 256 LEU LEU A . n 
A 1 276 GLU 276 257 257 GLU GLU A . n 
A 1 277 ARG 277 258 258 ARG ARG A . n 
A 1 278 HIS 278 259 259 HIS HIS A . n 
A 1 279 GLY 279 260 260 GLY GLY A . n 
A 1 280 LEU 280 261 261 LEU LEU A . n 
A 1 281 ILE 281 262 262 ILE ILE A . n 
A 1 282 ASN 282 263 263 ASN ASN A . n 
A 1 283 PHE 283 264 264 PHE PHE A . n 
A 1 284 GLY 284 265 265 GLY GLY A . n 
A 1 285 ILE 285 266 266 ILE ILE A . n 
A 1 286 TYR 286 267 267 TYR TYR A . n 
A 1 287 LYS 287 268 268 LYS LYS A . n 
A 1 288 ARG 288 269 269 ARG ARG A . n 
A 1 289 ILE 289 270 270 ILE ILE A . n 
A 1 290 LYS 290 271 271 LYS LYS A . n 
A 1 291 PRO 291 272 272 PRO PRO A . n 
A 1 292 LEU 292 273 273 LEU LEU A . n 
A 1 293 PRO 293 274 274 PRO PRO A . n 
A 1 294 THR 294 275 275 THR THR A . n 
A 1 295 LYS 295 276 276 LYS LYS A . n 
A 1 296 LYS 296 277 277 LYS LYS A . n 
A 1 297 THR 297 278 278 THR THR A . n 
A 1 298 GLY 298 279 279 GLY GLY A . n 
A 1 299 LYS 299 280 280 LYS LYS A . n 
A 1 300 VAL 300 281 281 VAL VAL A . n 
A 1 301 ILE 301 282 282 ILE ILE A . n 
A 1 302 ILE 302 283 283 ILE ILE A . n 
A 1 303 ILE 303 284 284 ILE ILE A . n 
A 1 304 GLY 304 285 285 GLY GLY A . n 
A 1 305 SER 305 286 286 SER SER A . n 
A 1 306 GLY 306 287 287 GLY GLY A . n 
A 1 307 VAL 307 288 288 VAL VAL A . n 
A 1 308 SER 308 289 289 SER SER A . n 
A 1 309 GLY 309 290 290 GLY GLY A . n 
A 1 310 LEU 310 291 291 LEU LEU A . n 
A 1 311 ALA 311 292 292 ALA ALA A . n 
A 1 312 ALA 312 293 293 ALA ALA A . n 
A 1 313 ALA 313 294 294 ALA ALA A . n 
A 1 314 ARG 314 295 295 ARG ARG A . n 
A 1 315 GLN 315 296 296 GLN GLN A . n 
A 1 316 LEU 316 297 297 LEU LEU A . n 
A 1 317 GLN 317 298 298 GLN GLN A . n 
A 1 318 SER 318 299 299 SER SER A . n 
A 1 319 PHE 319 300 300 PHE PHE A . n 
A 1 320 GLY 320 301 301 GLY GLY A . n 
A 1 321 MET 321 302 302 MET MET A . n 
A 1 322 ASP 322 303 303 ASP ASP A . n 
A 1 323 VAL 323 304 304 VAL VAL A . n 
A 1 324 THR 324 305 305 THR THR A . n 
A 1 325 LEU 325 306 306 LEU LEU A . n 
A 1 326 LEU 326 307 307 LEU LEU A . n 
A 1 327 GLU 327 308 308 GLU GLU A . n 
A 1 328 ALA 328 309 309 ALA ALA A . n 
A 1 329 ARG 329 310 310 ARG ARG A . n 
A 1 330 ASP 330 311 311 ASP ASP A . n 
A 1 331 ARG 331 312 312 ARG ARG A . n 
A 1 332 VAL 332 313 313 VAL VAL A . n 
A 1 333 GLY 333 314 314 GLY GLY A . n 
A 1 334 GLY 334 315 315 GLY GLY A . n 
A 1 335 ARG 335 316 316 ARG ARG A . n 
A 1 336 VAL 336 317 317 VAL VAL A . n 
A 1 337 ALA 337 318 318 ALA ALA A . n 
A 1 338 THR 338 319 319 THR THR A . n 
A 1 339 PHE 339 320 320 PHE PHE A . n 
A 1 340 ARG 340 321 321 ARG ARG A . n 
A 1 341 LYS 341 322 322 LYS LYS A . n 
A 1 342 GLY 342 323 323 GLY GLY A . n 
A 1 343 ASN 343 324 324 ASN ASN A . n 
A 1 344 TYR 344 325 325 TYR TYR A . n 
A 1 345 VAL 345 326 326 VAL VAL A . n 
A 1 346 ALA 346 327 327 ALA ALA A . n 
A 1 347 ASP 347 328 328 ASP ASP A . n 
A 1 348 LEU 348 329 329 LEU LEU A . n 
A 1 349 GLY 349 330 330 GLY GLY A . n 
A 1 350 ALA 350 331 331 ALA ALA A . n 
A 1 351 MET 351 332 332 MET MET A . n 
A 1 352 VAL 352 333 333 VAL VAL A . n 
A 1 353 VAL 353 334 334 VAL VAL A . n 
A 1 354 THR 354 335 335 THR THR A . n 
A 1 355 GLY 355 336 336 GLY GLY A . n 
A 1 356 LEU 356 337 337 LEU LEU A . n 
A 1 357 GLY 357 338 338 GLY GLY A . n 
A 1 358 GLY 358 339 339 GLY GLY A . n 
A 1 359 ASN 359 340 340 ASN ASN A . n 
A 1 360 PRO 360 341 341 PRO PRO A . n 
A 1 361 MET 361 342 342 MET MET A . n 
A 1 362 ALA 362 343 343 ALA ALA A . n 
A 1 363 VAL 363 344 344 VAL VAL A . n 
A 1 364 VAL 364 345 345 VAL VAL A . n 
A 1 365 SER 365 346 346 SER SER A . n 
A 1 366 LYS 366 347 347 LYS LYS A . n 
A 1 367 GLN 367 348 348 GLN GLN A . n 
A 1 368 VAL 368 349 349 VAL VAL A . n 
A 1 369 ASN 369 350 350 ASN ASN A . n 
A 1 370 MET 370 351 351 MET MET A . n 
A 1 371 GLU 371 352 352 GLU GLU A . n 
A 1 372 LEU 372 353 353 LEU LEU A . n 
A 1 373 ALA 373 354 354 ALA ALA A . n 
A 1 374 LYS 374 355 355 LYS LYS A . n 
A 1 375 ILE 375 356 356 ILE ILE A . n 
A 1 376 LYS 376 357 357 LYS LYS A . n 
A 1 377 GLN 377 358 358 GLN GLN A . n 
A 1 378 LYS 378 359 359 LYS LYS A . n 
A 1 379 CYS 379 360 360 CYS CYS A . n 
A 1 380 PRO 380 361 361 PRO PRO A . n 
A 1 381 LEU 381 362 362 LEU LEU A . n 
A 1 382 TYR 382 363 363 TYR TYR A . n 
A 1 383 GLU 383 364 364 GLU GLU A . n 
A 1 384 ALA 384 365 365 ALA ALA A . n 
A 1 385 ASN 385 366 366 ASN ASN A . n 
A 1 386 GLY 386 367 367 GLY GLY A . n 
A 1 387 GLN 387 368 368 GLN GLN A . n 
A 1 388 ALA 388 369 369 ALA ALA A . n 
A 1 389 VAL 389 370 370 VAL VAL A . n 
A 1 390 PRO 390 371 371 PRO PRO A . n 
A 1 391 LYS 391 372 372 LYS LYS A . n 
A 1 392 GLU 392 373 373 GLU GLU A . n 
A 1 393 LYS 393 374 374 LYS LYS A . n 
A 1 394 ASP 394 375 375 ASP ASP A . n 
A 1 395 GLU 395 376 376 GLU GLU A . n 
A 1 396 MET 396 377 377 MET MET A . n 
A 1 397 VAL 397 378 378 VAL VAL A . n 
A 1 398 GLU 398 379 379 GLU GLU A . n 
A 1 399 GLN 399 380 380 GLN GLN A . n 
A 1 400 GLU 400 381 381 GLU GLU A . n 
A 1 401 PHE 401 382 382 PHE PHE A . n 
A 1 402 ASN 402 383 383 ASN ASN A . n 
A 1 403 ARG 403 384 384 ARG ARG A . n 
A 1 404 LEU 404 385 385 LEU LEU A . n 
A 1 405 LEU 405 386 386 LEU LEU A . n 
A 1 406 GLU 406 387 387 GLU GLU A . n 
A 1 407 ALA 407 388 388 ALA ALA A . n 
A 1 408 THR 408 389 389 THR THR A . n 
A 1 409 SER 409 390 390 SER SER A . n 
A 1 410 TYR 410 391 391 TYR TYR A . n 
A 1 411 LEU 411 392 392 LEU LEU A . n 
A 1 412 SER 412 393 393 SER SER A . n 
A 1 413 HIS 413 394 394 HIS HIS A . n 
A 1 414 GLN 414 395 395 GLN GLN A . n 
A 1 415 LEU 415 396 396 LEU LEU A . n 
A 1 416 ASP 416 397 397 ASP ASP A . n 
A 1 417 PHE 417 398 398 PHE PHE A . n 
A 1 418 ASN 418 399 399 ASN ASN A . n 
A 1 419 VAL 419 400 400 VAL VAL A . n 
A 1 420 LEU 420 401 401 LEU LEU A . n 
A 1 421 ASN 421 402 402 ASN ASN A . n 
A 1 422 ASN 422 403 403 ASN ASN A . n 
A 1 423 LYS 423 404 404 LYS LYS A . n 
A 1 424 PRO 424 405 405 PRO PRO A . n 
A 1 425 VAL 425 406 406 VAL VAL A . n 
A 1 426 SER 426 407 407 SER SER A . n 
A 1 427 LEU 427 408 408 LEU LEU A . n 
A 1 428 GLY 428 409 409 GLY GLY A . n 
A 1 429 GLN 429 410 410 GLN GLN A . n 
A 1 430 ALA 430 411 411 ALA ALA A . n 
A 1 431 LEU 431 412 412 LEU LEU A . n 
A 1 432 GLU 432 413 413 GLU GLU A . n 
A 1 433 VAL 433 414 414 VAL VAL A . n 
A 1 434 VAL 434 415 415 VAL VAL A . n 
A 1 435 ILE 435 416 416 ILE ILE A . n 
A 1 436 GLN 436 417 417 GLN GLN A . n 
A 1 437 LEU 437 418 418 LEU LEU A . n 
A 1 438 GLN 438 419 419 GLN GLN A . n 
A 1 439 GLU 439 420 420 GLU GLU A . n 
A 1 440 LYS 440 421 421 LYS LYS A . n 
A 1 441 HIS 441 422 422 HIS HIS A . n 
A 1 442 VAL 442 423 423 VAL VAL A . n 
A 1 443 LYS 443 424 424 LYS LYS A . n 
A 1 444 ASP 444 425 425 ASP ASP A . n 
A 1 445 GLU 445 426 426 GLU GLU A . n 
A 1 446 GLN 446 427 427 GLN GLN A . n 
A 1 447 ILE 447 428 428 ILE ILE A . n 
A 1 448 GLU 448 429 429 GLU GLU A . n 
A 1 449 HIS 449 430 430 HIS HIS A . n 
A 1 450 TRP 450 431 431 TRP TRP A . n 
A 1 451 LYS 451 432 432 LYS LYS A . n 
A 1 452 LYS 452 433 433 LYS LYS A . n 
A 1 453 ILE 453 434 434 ILE ILE A . n 
A 1 454 VAL 454 435 435 VAL VAL A . n 
A 1 455 LYS 455 436 436 LYS LYS A . n 
A 1 456 THR 456 437 437 THR THR A . n 
A 1 457 GLN 457 438 438 GLN GLN A . n 
A 1 458 GLU 458 439 439 GLU GLU A . n 
A 1 459 GLU 459 440 440 GLU GLU A . n 
A 1 460 LEU 460 441 441 LEU LEU A . n 
A 1 461 LYS 461 442 442 LYS LYS A . n 
A 1 462 GLU 462 443 443 GLU GLU A . n 
A 1 463 LEU 463 444 444 LEU LEU A . n 
A 1 464 LEU 464 445 445 LEU LEU A . n 
A 1 465 ASN 465 446 446 ASN ASN A . n 
A 1 466 LYS 466 447 447 LYS LYS A . n 
A 1 467 MET 467 448 448 MET MET A . n 
A 1 468 VAL 468 449 449 VAL VAL A . n 
A 1 469 ASN 469 450 450 ASN ASN A . n 
A 1 470 LEU 470 451 451 LEU LEU A . n 
A 1 471 LYS 471 452 452 LYS LYS A . n 
A 1 472 GLU 472 453 453 GLU GLU A . n 
A 1 473 LYS 473 454 454 LYS LYS A . n 
A 1 474 ILE 474 455 455 ILE ILE A . n 
A 1 475 LYS 475 456 456 LYS LYS A . n 
A 1 476 GLU 476 457 457 GLU GLU A . n 
A 1 477 LEU 477 458 458 LEU LEU A . n 
A 1 478 HIS 478 459 459 HIS HIS A . n 
A 1 479 GLN 479 460 460 GLN GLN A . n 
A 1 480 GLN 480 461 461 GLN GLN A . n 
A 1 481 TYR 481 462 462 TYR TYR A . n 
A 1 482 LYS 482 463 463 LYS LYS A . n 
A 1 483 GLU 483 464 464 GLU GLU A . n 
A 1 484 ALA 484 465 465 ALA ALA A . n 
A 1 485 SER 485 466 466 SER SER A . n 
A 1 486 GLU 486 467 467 GLU GLU A . n 
A 1 487 VAL 487 468 468 VAL VAL A . n 
A 1 488 LYS 488 469 469 LYS LYS A . n 
A 1 489 PRO 489 470 470 PRO PRO A . n 
A 1 490 PRO 490 471 471 PRO PRO A . n 
A 1 491 ARG 491 472 472 ARG ARG A . n 
A 1 492 ASP 492 473 473 ASP ASP A . n 
A 1 493 ILE 493 474 474 ILE ILE A . n 
A 1 494 THR 494 475 475 THR THR A . n 
A 1 495 ALA 495 476 476 ALA ALA A . n 
A 1 496 GLU 496 477 477 GLU GLU A . n 
A 1 497 PHE 497 478 478 PHE PHE A . n 
A 1 498 LEU 498 479 479 LEU LEU A . n 
A 1 499 VAL 499 480 480 VAL VAL A . n 
A 1 500 LYS 500 481 481 LYS LYS A . n 
A 1 501 SER 501 482 482 SER SER A . n 
A 1 502 LYS 502 483 483 LYS LYS A . n 
A 1 503 HIS 503 484 484 HIS HIS A . n 
A 1 504 ARG 504 485 485 ARG ARG A . n 
A 1 505 ASP 505 486 486 ASP ASP A . n 
A 1 506 LEU 506 487 487 LEU LEU A . n 
A 1 507 THR 507 488 488 THR THR A . n 
A 1 508 ALA 508 489 489 ALA ALA A . n 
A 1 509 LEU 509 490 490 LEU LEU A . n 
A 1 510 CYS 510 491 491 CYS CYS A . n 
A 1 511 LYS 511 492 492 LYS LYS A . n 
A 1 512 GLU 512 493 493 GLU GLU A . n 
A 1 513 TYR 513 494 494 TYR TYR A . n 
A 1 514 ASP 514 495 495 ASP ASP A . n 
A 1 515 GLU 515 496 496 GLU GLU A . n 
A 1 516 LEU 516 497 497 LEU LEU A . n 
A 1 517 ALA 517 498 498 ALA ALA A . n 
A 1 518 GLU 518 499 499 GLU GLU A . n 
A 1 519 THR 519 500 500 THR THR A . n 
A 1 520 GLN 520 501 501 GLN GLN A . n 
A 1 521 GLY 521 502 502 GLY GLY A . n 
A 1 522 LYS 522 503 503 LYS LYS A . n 
A 1 523 LEU 523 504 504 LEU LEU A . n 
A 1 524 GLU 524 505 505 GLU GLU A . n 
A 1 525 GLU 525 506 506 GLU GLU A . n 
A 1 526 LYS 526 507 507 LYS LYS A . n 
A 1 527 LEU 527 508 508 LEU LEU A . n 
A 1 528 GLN 528 509 509 GLN GLN A . n 
A 1 529 GLU 529 510 510 GLU GLU A . n 
A 1 530 LEU 530 511 511 LEU LEU A . n 
A 1 531 GLU 531 512 512 GLU GLU A . n 
A 1 532 ALA 532 513 513 ALA ALA A . n 
A 1 533 ASN 533 514 514 ASN ASN A . n 
A 1 534 PRO 534 515 515 PRO PRO A . n 
A 1 535 PRO 535 516 516 PRO PRO A . n 
A 1 536 SER 536 517 517 SER SER A . n 
A 1 537 ASP 537 518 518 ASP ASP A . n 
A 1 538 VAL 538 519 519 VAL VAL A . n 
A 1 539 TYR 539 520 520 TYR TYR A . n 
A 1 540 LEU 540 521 521 LEU LEU A . n 
A 1 541 SER 541 522 522 SER SER A . n 
A 1 542 SER 542 523 523 SER SER A . n 
A 1 543 ARG 543 524 524 ARG ARG A . n 
A 1 544 ASP 544 525 525 ASP ASP A . n 
A 1 545 ARG 545 526 526 ARG ARG A . n 
A 1 546 GLN 546 527 527 GLN GLN A . n 
A 1 547 ILE 547 528 528 ILE ILE A . n 
A 1 548 LEU 548 529 529 LEU LEU A . n 
A 1 549 ASP 549 530 530 ASP ASP A . n 
A 1 550 TRP 550 531 531 TRP TRP A . n 
A 1 551 HIS 551 532 532 HIS HIS A . n 
A 1 552 PHE 552 533 533 PHE PHE A . n 
A 1 553 ALA 553 534 534 ALA ALA A . n 
A 1 554 ASN 554 535 535 ASN ASN A . n 
A 1 555 LEU 555 536 536 LEU LEU A . n 
A 1 556 GLU 556 537 537 GLU GLU A . n 
A 1 557 PHE 557 538 538 PHE PHE A . n 
A 1 558 ALA 558 539 539 ALA ALA A . n 
A 1 559 ASN 559 540 540 ASN ASN A . n 
A 1 560 ALA 560 541 541 ALA ALA A . n 
A 1 561 THR 561 542 542 THR THR A . n 
A 1 562 PRO 562 543 543 PRO PRO A . n 
A 1 563 LEU 563 544 544 LEU LEU A . n 
A 1 564 SER 564 545 545 SER SER A . n 
A 1 565 THR 565 546 546 THR THR A . n 
A 1 566 LEU 566 547 547 LEU LEU A . n 
A 1 567 SER 567 548 548 SER SER A . n 
A 1 568 LEU 568 549 549 LEU LEU A . n 
A 1 569 LYS 569 550 550 LYS LYS A . n 
A 1 570 HIS 570 551 551 HIS HIS A . n 
A 1 571 TRP 571 552 552 TRP TRP A . n 
A 1 572 ASP 572 553 553 ASP ASP A . n 
A 1 573 GLN 573 554 554 GLN GLN A . n 
A 1 574 ASP 574 555 555 ASP ASP A . n 
A 1 575 ASP 575 556 556 ASP ASP A . n 
A 1 576 ASP 576 557 557 ASP ASP A . n 
A 1 577 PHE 577 558 558 PHE PHE A . n 
A 1 578 GLU 578 559 559 GLU GLU A . n 
A 1 579 PHE 579 560 560 PHE PHE A . n 
A 1 580 THR 580 561 561 THR THR A . n 
A 1 581 GLY 581 562 562 GLY GLY A . n 
A 1 582 SER 582 563 563 SER SER A . n 
A 1 583 HIS 583 564 564 HIS HIS A . n 
A 1 584 LEU 584 565 565 LEU LEU A . n 
A 1 585 THR 585 566 566 THR THR A . n 
A 1 586 VAL 586 567 567 VAL VAL A . n 
A 1 587 ARG 587 568 568 ARG ARG A . n 
A 1 588 ASN 588 569 569 ASN ASN A . n 
A 1 589 GLY 589 570 570 GLY GLY A . n 
A 1 590 TYR 590 571 571 TYR TYR A . n 
A 1 591 SER 591 572 572 SER SER A . n 
A 1 592 CYS 592 573 573 CYS CYS A . n 
A 1 593 VAL 593 574 574 VAL VAL A . n 
A 1 594 PRO 594 575 575 PRO PRO A . n 
A 1 595 VAL 595 576 576 VAL VAL A . n 
A 1 596 ALA 596 577 577 ALA ALA A . n 
A 1 597 LEU 597 578 578 LEU LEU A . n 
A 1 598 ALA 598 579 579 ALA ALA A . n 
A 1 599 GLU 599 580 580 GLU GLU A . n 
A 1 600 GLY 600 581 581 GLY GLY A . n 
A 1 601 LEU 601 582 582 LEU LEU A . n 
A 1 602 ASP 602 583 583 ASP ASP A . n 
A 1 603 ILE 603 584 584 ILE ILE A . n 
A 1 604 LYS 604 585 585 LYS LYS A . n 
A 1 605 LEU 605 586 586 LEU LEU A . n 
A 1 606 ASN 606 587 587 ASN ASN A . n 
A 1 607 THR 607 588 588 THR THR A . n 
A 1 608 ALA 608 589 589 ALA ALA A . n 
A 1 609 VAL 609 590 590 VAL VAL A . n 
A 1 610 ARG 610 591 591 ARG ARG A . n 
A 1 611 GLN 611 592 592 GLN GLN A . n 
A 1 612 VAL 612 593 593 VAL VAL A . n 
A 1 613 ARG 613 594 594 ARG ARG A . n 
A 1 614 TYR 614 595 595 TYR TYR A . n 
A 1 615 THR 615 596 596 THR THR A . n 
A 1 616 ALA 616 597 597 ALA ALA A . n 
A 1 617 SER 617 598 598 SER SER A . n 
A 1 618 GLY 618 599 599 GLY GLY A . n 
A 1 619 CYS 619 600 600 CYS CYS A . n 
A 1 620 GLU 620 601 601 GLU GLU A . n 
A 1 621 VAL 621 602 602 VAL VAL A . n 
A 1 622 ILE 622 603 603 ILE ILE A . n 
A 1 623 ALA 623 604 604 ALA ALA A . n 
A 1 624 VAL 624 605 605 VAL VAL A . n 
A 1 625 ASN 625 606 606 ASN ASN A . n 
A 1 626 THR 626 607 607 THR THR A . n 
A 1 627 ARG 627 608 608 ARG ARG A . n 
A 1 628 SER 628 609 609 SER SER A . n 
A 1 629 THR 629 610 610 THR THR A . n 
A 1 630 SER 630 611 611 SER SER A . n 
A 1 631 GLN 631 612 612 GLN GLN A . n 
A 1 632 THR 632 613 613 THR THR A . n 
A 1 633 PHE 633 614 614 PHE PHE A . n 
A 1 634 ILE 634 615 615 ILE ILE A . n 
A 1 635 TYR 635 616 616 TYR TYR A . n 
A 1 636 LYS 636 617 617 LYS LYS A . n 
A 1 637 CYS 637 618 618 CYS CYS A . n 
A 1 638 ASP 638 619 619 ASP ASP A . n 
A 1 639 ALA 639 620 620 ALA ALA A . n 
A 1 640 VAL 640 621 621 VAL VAL A . n 
A 1 641 LEU 641 622 622 LEU LEU A . n 
A 1 642 CYS 642 623 623 CYS CYS A . n 
A 1 643 THR 643 624 624 THR THR A . n 
A 1 644 LEU 644 625 625 LEU LEU A . n 
A 1 645 PRO 645 626 626 PRO PRO A . n 
A 1 646 LEU 646 627 627 LEU LEU A . n 
A 1 647 GLY 647 628 628 GLY GLY A . n 
A 1 648 VAL 648 629 629 VAL VAL A . n 
A 1 649 LEU 649 630 630 LEU LEU A . n 
A 1 650 LYS 650 631 631 LYS LYS A . n 
A 1 651 GLN 651 632 632 GLN GLN A . n 
A 1 652 GLN 652 633 633 GLN GLN A . n 
A 1 653 PRO 653 634 634 PRO PRO A . n 
A 1 654 PRO 654 635 635 PRO PRO A . n 
A 1 655 ALA 655 636 636 ALA ALA A . n 
A 1 656 VAL 656 637 637 VAL VAL A . n 
A 1 657 GLN 657 638 638 GLN GLN A . n 
A 1 658 PHE 658 639 639 PHE PHE A . n 
A 1 659 VAL 659 640 640 VAL VAL A . n 
A 1 660 PRO 660 641 641 PRO PRO A . n 
A 1 661 PRO 661 642 642 PRO PRO A . n 
A 1 662 LEU 662 643 643 LEU LEU A . n 
A 1 663 PRO 663 644 644 PRO PRO A . n 
A 1 664 GLU 664 645 645 GLU GLU A . n 
A 1 665 TRP 665 646 646 TRP TRP A . n 
A 1 666 LYS 666 647 647 LYS LYS A . n 
A 1 667 THR 667 648 648 THR THR A . n 
A 1 668 SER 668 649 649 SER SER A . n 
A 1 669 ALA 669 650 650 ALA ALA A . n 
A 1 670 VAL 670 651 651 VAL VAL A . n 
A 1 671 GLN 671 652 652 GLN GLN A . n 
A 1 672 ARG 672 653 653 ARG ARG A . n 
A 1 673 MET 673 654 654 MET MET A . n 
A 1 674 GLY 674 655 655 GLY GLY A . n 
A 1 675 PHE 675 656 656 PHE PHE A . n 
A 1 676 GLY 676 657 657 GLY GLY A . n 
A 1 677 ASN 677 658 658 ASN ASN A . n 
A 1 678 LEU 678 659 659 LEU LEU A . n 
A 1 679 ASN 679 660 660 ASN ASN A . n 
A 1 680 LYS 680 661 661 LYS LYS A . n 
A 1 681 VAL 681 662 662 VAL VAL A . n 
A 1 682 VAL 682 663 663 VAL VAL A . n 
A 1 683 LEU 683 664 664 LEU LEU A . n 
A 1 684 CYS 684 665 665 CYS CYS A . n 
A 1 685 PHE 685 666 666 PHE PHE A . n 
A 1 686 ASP 686 667 667 ASP ASP A . n 
A 1 687 ARG 687 668 668 ARG ARG A . n 
A 1 688 VAL 688 669 669 VAL VAL A . n 
A 1 689 PHE 689 670 670 PHE PHE A . n 
A 1 690 TRP 690 671 671 TRP TRP A . n 
A 1 691 ASP 691 672 672 ASP ASP A . n 
A 1 692 PRO 692 673 673 PRO PRO A . n 
A 1 693 SER 693 674 674 SER SER A . n 
A 1 694 VAL 694 675 675 VAL VAL A . n 
A 1 695 ASN 695 676 676 ASN ASN A . n 
A 1 696 LEU 696 677 677 LEU LEU A . n 
A 1 697 PHE 697 678 678 PHE PHE A . n 
A 1 698 GLY 698 679 679 GLY GLY A . n 
A 1 699 HIS 699 680 680 HIS HIS A . n 
A 1 700 VAL 700 681 681 VAL VAL A . n 
A 1 701 GLY 701 682 682 GLY GLY A . n 
A 1 702 SER 702 683 683 SER SER A . n 
A 1 703 THR 703 684 684 THR THR A . n 
A 1 704 THR 704 685 685 THR THR A . n 
A 1 705 ALA 705 686 686 ALA ALA A . n 
A 1 706 SER 706 687 687 SER SER A . n 
A 1 707 ARG 707 688 688 ARG ARG A . n 
A 1 708 GLY 708 689 689 GLY GLY A . n 
A 1 709 GLU 709 690 690 GLU GLU A . n 
A 1 710 LEU 710 691 691 LEU LEU A . n 
A 1 711 PHE 711 692 692 PHE PHE A . n 
A 1 712 LEU 712 693 693 LEU LEU A . n 
A 1 713 PHE 713 694 694 PHE PHE A . n 
A 1 714 TRP 714 695 695 TRP TRP A . n 
A 1 715 ASN 715 696 696 ASN ASN A . n 
A 1 716 LEU 716 697 697 LEU LEU A . n 
A 1 717 TYR 717 698 698 TYR TYR A . n 
A 1 718 LYS 718 699 699 LYS LYS A . n 
A 1 719 ALA 719 700 700 ALA ALA A . n 
A 1 720 PRO 720 701 701 PRO PRO A . n 
A 1 721 ILE 721 702 702 ILE ILE A . n 
A 1 722 LEU 722 703 703 LEU LEU A . n 
A 1 723 LEU 723 704 704 LEU LEU A . n 
A 1 724 ALA 724 705 705 ALA ALA A . n 
A 1 725 LEU 725 706 706 LEU LEU A . n 
A 1 726 VAL 726 707 707 VAL VAL A . n 
A 1 727 ALA 727 708 708 ALA ALA A . n 
A 1 728 GLY 728 709 709 GLY GLY A . n 
A 1 729 GLU 729 710 710 GLU GLU A . n 
A 1 730 ALA 730 711 711 ALA ALA A . n 
A 1 731 ALA 731 712 712 ALA ALA A . n 
A 1 732 GLY 732 713 713 GLY GLY A . n 
A 1 733 ILE 733 714 714 ILE ILE A . n 
A 1 734 MET 734 715 715 MET MET A . n 
A 1 735 GLU 735 716 716 GLU GLU A . n 
A 1 736 ASN 736 717 717 ASN ASN A . n 
A 1 737 ILE 737 718 718 ILE ILE A . n 
A 1 738 SER 738 719 719 SER SER A . n 
A 1 739 ASP 739 720 720 ASP ASP A . n 
A 1 740 ASP 740 721 721 ASP ASP A . n 
A 1 741 VAL 741 722 722 VAL VAL A . n 
A 1 742 ILE 742 723 723 ILE ILE A . n 
A 1 743 VAL 743 724 724 VAL VAL A . n 
A 1 744 GLY 744 725 725 GLY GLY A . n 
A 1 745 ARG 745 726 726 ARG ARG A . n 
A 1 746 CYS 746 727 727 CYS CYS A . n 
A 1 747 LEU 747 728 728 LEU LEU A . n 
A 1 748 ALA 748 729 729 ALA ALA A . n 
A 1 749 ILE 749 730 730 ILE ILE A . n 
A 1 750 LEU 750 731 731 LEU LEU A . n 
A 1 751 LYS 751 732 732 LYS LYS A . n 
A 1 752 GLY 752 733 733 GLY GLY A . n 
A 1 753 ILE 753 734 734 ILE ILE A . n 
A 1 754 PHE 754 735 735 PHE PHE A . n 
A 1 755 GLY 755 736 736 GLY GLY A . n 
A 1 756 SER 756 737 737 SER SER A . n 
A 1 757 SER 757 738 738 SER SER A . n 
A 1 758 ALA 758 739 739 ALA ALA A . n 
A 1 759 VAL 759 740 740 VAL VAL A . n 
A 1 760 PRO 760 741 741 PRO PRO A . n 
A 1 761 GLN 761 742 742 GLN GLN A . n 
A 1 762 PRO 762 743 743 PRO PRO A . n 
A 1 763 LYS 763 744 744 LYS LYS A . n 
A 1 764 GLU 764 745 745 GLU GLU A . n 
A 1 765 THR 765 746 746 THR THR A . n 
A 1 766 VAL 766 747 747 VAL VAL A . n 
A 1 767 VAL 767 748 748 VAL VAL A . n 
A 1 768 SER 768 749 749 SER SER A . n 
A 1 769 ARG 769 750 750 ARG ARG A . n 
A 1 770 TRP 770 751 751 TRP TRP A . n 
A 1 771 ARG 771 752 752 ARG ARG A . n 
A 1 772 ALA 772 753 753 ALA ALA A . n 
A 1 773 ASP 773 754 754 ASP ASP A . n 
A 1 774 PRO 774 755 755 PRO PRO A . n 
A 1 775 TRP 775 756 756 TRP TRP A . n 
A 1 776 ALA 776 757 757 ALA ALA A . n 
A 1 777 ARG 777 758 758 ARG ARG A . n 
A 1 778 GLY 778 759 759 GLY GLY A . n 
A 1 779 SER 779 760 760 SER SER A . n 
A 1 780 TYR 780 761 761 TYR TYR A . n 
A 1 781 SER 781 762 762 SER SER A . n 
A 1 782 TYR 782 763 763 TYR TYR A . n 
A 1 783 VAL 783 764 764 VAL VAL A . n 
A 1 784 ALA 784 765 765 ALA ALA A . n 
A 1 785 ALA 785 766 766 ALA ALA A . n 
A 1 786 GLY 786 767 767 GLY GLY A . n 
A 1 787 SER 787 768 768 SER SER A . n 
A 1 788 SER 788 769 769 SER SER A . n 
A 1 789 GLY 789 770 770 GLY GLY A . n 
A 1 790 ASN 790 771 771 ASN ASN A . n 
A 1 791 ASP 791 772 772 ASP ASP A . n 
A 1 792 TYR 792 773 773 TYR TYR A . n 
A 1 793 ASP 793 774 774 ASP ASP A . n 
A 1 794 LEU 794 775 775 LEU LEU A . n 
A 1 795 MET 795 776 776 MET MET A . n 
A 1 796 ALA 796 777 777 ALA ALA A . n 
A 1 797 GLN 797 778 778 GLN GLN A . n 
A 1 798 PRO 798 779 779 PRO PRO A . n 
A 1 799 ILE 799 780 780 ILE ILE A . n 
A 1 800 THR 800 781 781 THR THR A . n 
A 1 801 PRO 801 782 782 PRO PRO A . n 
A 1 802 GLY 802 783 783 GLY GLY A . n 
A 1 803 PRO 803 784 784 PRO PRO A . n 
A 1 804 SER 804 785 785 SER SER A . n 
A 1 805 ILE 805 786 786 ILE ILE A . n 
A 1 806 PRO 806 787 787 PRO PRO A . n 
A 1 807 GLY 807 788 788 GLY GLY A . n 
A 1 808 ALA 808 789 789 ALA ALA A . n 
A 1 809 PRO 809 790 790 PRO PRO A . n 
A 1 810 GLN 810 791 791 GLN GLN A . n 
A 1 811 PRO 811 792 792 PRO PRO A . n 
A 1 812 ILE 812 793 793 ILE ILE A . n 
A 1 813 PRO 813 794 794 PRO PRO A . n 
A 1 814 ARG 814 795 795 ARG ARG A . n 
A 1 815 LEU 815 796 796 LEU LEU A . n 
A 1 816 PHE 816 797 797 PHE PHE A . n 
A 1 817 PHE 817 798 798 PHE PHE A . n 
A 1 818 ALA 818 799 799 ALA ALA A . n 
A 1 819 GLY 819 800 800 GLY GLY A . n 
A 1 820 GLU 820 801 801 GLU GLU A . n 
A 1 821 HIS 821 802 802 HIS HIS A . n 
A 1 822 THR 822 803 803 THR THR A . n 
A 1 823 ILE 823 804 804 ILE ILE A . n 
A 1 824 ARG 824 805 805 ARG ARG A . n 
A 1 825 ASN 825 806 806 ASN ASN A . n 
A 1 826 TYR 826 807 807 TYR TYR A . n 
A 1 827 PRO 827 808 808 PRO PRO A . n 
A 1 828 ALA 828 809 809 ALA ALA A . n 
A 1 829 THR 829 810 810 THR THR A . n 
A 1 830 VAL 830 811 811 VAL VAL A . n 
A 1 831 HIS 831 812 812 HIS HIS A . n 
A 1 832 GLY 832 813 813 GLY GLY A . n 
A 1 833 ALA 833 814 814 ALA ALA A . n 
A 1 834 LEU 834 815 815 LEU LEU A . n 
A 1 835 LEU 835 816 816 LEU LEU A . n 
A 1 836 SER 836 817 817 SER SER A . n 
A 1 837 GLY 837 818 818 GLY GLY A . n 
A 1 838 LEU 838 819 819 LEU LEU A . n 
A 1 839 ARG 839 820 820 ARG ARG A . n 
A 1 840 GLU 840 821 821 GLU GLU A . n 
A 1 841 ALA 841 822 822 ALA ALA A . n 
A 1 842 GLY 842 823 823 GLY GLY A . n 
A 1 843 ARG 843 824 824 ARG ARG A . n 
A 1 844 ILE 844 825 825 ILE ILE A . n 
A 1 845 ALA 845 826 826 ALA ALA A . n 
A 1 846 ASP 846 827 827 ASP ASP A . n 
A 1 847 GLN 847 828 828 GLN GLN A . n 
A 1 848 PHE 848 829 829 PHE PHE A . n 
A 1 849 LEU 849 830 830 LEU LEU A . n 
A 1 850 GLY 850 831 831 GLY GLY A . n 
A 1 851 ALA 851 832 832 ALA ALA A . n 
A 1 852 MET 852 833 833 MET MET A . n 
A 1 853 TYR 853 834 834 TYR TYR A . n 
A 1 854 THR 854 835 835 THR THR A . n 
A 1 855 LEU 855 836 836 LEU LEU A . n 
A 1 856 PRO 856 837 ?   ?   ?   A . n 
A 1 857 ARG 857 838 ?   ?   ?   A . n 
A 1 858 GLN 858 839 ?   ?   ?   A . n 
A 1 859 ALA 859 840 ?   ?   ?   A . n 
A 1 860 THR 860 841 ?   ?   ?   A . n 
A 1 861 PRO 861 842 ?   ?   ?   A . n 
A 1 862 GLY 862 843 ?   ?   ?   A . n 
A 1 863 VAL 863 844 ?   ?   ?   A . n 
A 1 864 PRO 864 845 ?   ?   ?   A . n 
A 1 865 ALA 865 846 ?   ?   ?   A . n 
A 1 866 GLN 866 847 ?   ?   ?   A . n 
A 1 867 GLN 867 848 ?   ?   ?   A . n 
A 1 868 SER 868 849 ?   ?   ?   A . n 
A 1 869 PRO 869 850 ?   ?   ?   A . n 
A 1 870 SER 870 851 ?   ?   ?   A . n 
A 1 871 MET 871 852 ?   ?   ?   A . n 
B 2 1   GLY 1   297 ?   ?   ?   B . n 
B 2 2   PRO 2   298 ?   ?   ?   B . n 
B 2 3   LEU 3   299 ?   ?   ?   B . n 
B 2 4   GLY 4   300 ?   ?   ?   B . n 
B 2 5   SER 5   301 ?   ?   ?   B . n 
B 2 6   PRO 6   302 ?   ?   ?   B . n 
B 2 7   GLU 7   303 ?   ?   ?   B . n 
B 2 8   PHE 8   304 ?   ?   ?   B . n 
B 2 9   ARG 9   305 ?   ?   ?   B . n 
B 2 10  ALA 10  306 ?   ?   ?   B . n 
B 2 11  LYS 11  307 ?   ?   ?   B . n 
B 2 12  ARG 12  308 308 ARG ARG B . n 
B 2 13  LYS 13  309 309 LYS LYS B . n 
B 2 14  PRO 14  310 310 PRO PRO B . n 
B 2 15  PRO 15  311 311 PRO PRO B . n 
B 2 16  LYS 16  312 312 LYS LYS B . n 
B 2 17  GLY 17  313 313 GLY GLY B . n 
B 2 18  MET 18  314 314 MET MET B . n 
B 2 19  PHE 19  315 315 PHE PHE B . n 
B 2 20  LEU 20  316 316 LEU LEU B . n 
B 2 21  SER 21  317 317 SER SER B . n 
B 2 22  GLN 22  318 318 GLN GLN B . n 
B 2 23  GLU 23  319 319 GLU GLU B . n 
B 2 24  ASP 24  320 320 ASP ASP B . n 
B 2 25  VAL 25  321 321 VAL VAL B . n 
B 2 26  GLU 26  322 322 GLU GLU B . n 
B 2 27  ALA 27  323 323 ALA ALA B . n 
B 2 28  VAL 28  324 324 VAL VAL B . n 
B 2 29  SER 29  325 325 SER SER B . n 
B 2 30  ALA 30  326 326 ALA ALA B . n 
B 2 31  ASN 31  327 327 ASN ASN B . n 
B 2 32  ALA 32  328 328 ALA ALA B . n 
B 2 33  THR 33  329 329 THR THR B . n 
B 2 34  ALA 34  330 330 ALA ALA B . n 
B 2 35  ALA 35  331 331 ALA ALA B . n 
B 2 36  THR 36  332 332 THR THR B . n 
B 2 37  THR 37  333 333 THR THR B . n 
B 2 38  VAL 38  334 334 VAL VAL B . n 
B 2 39  LEU 39  335 335 LEU LEU B . n 
B 2 40  ARG 40  336 336 ARG ARG B . n 
B 2 41  GLN 41  337 337 GLN GLN B . n 
B 2 42  LEU 42  338 338 LEU LEU B . n 
B 2 43  ASP 43  339 339 ASP ASP B . n 
B 2 44  MET 44  340 340 MET MET B . n 
B 2 45  GLU 45  341 341 GLU GLU B . n 
B 2 46  LEU 46  342 342 LEU LEU B . n 
B 2 47  VAL 47  343 343 VAL VAL B . n 
B 2 48  SER 48  344 344 SER SER B . n 
B 2 49  VAL 49  345 345 VAL VAL B . n 
B 2 50  LYS 50  346 346 LYS LYS B . n 
B 2 51  ARG 51  347 347 ARG ARG B . n 
B 2 52  GLN 52  348 348 GLN GLN B . n 
B 2 53  ILE 53  349 349 ILE ILE B . n 
B 2 54  GLN 54  350 350 GLN GLN B . n 
B 2 55  ASN 55  351 351 ASN ASN B . n 
B 2 56  ILE 56  352 352 ILE ILE B . n 
B 2 57  LYS 57  353 353 LYS LYS B . n 
B 2 58  GLN 58  354 354 GLN GLN B . n 
B 2 59  THR 59  355 355 THR THR B . n 
B 2 60  ASN 60  356 356 ASN ASN B . n 
B 2 61  SER 61  357 357 SER SER B . n 
B 2 62  ALA 62  358 358 ALA ALA B . n 
B 2 63  LEU 63  359 359 LEU LEU B . n 
B 2 64  LYS 64  360 360 LYS LYS B . n 
B 2 65  GLU 65  361 361 GLU GLU B . n 
B 2 66  LYS 66  362 362 LYS LYS B . n 
B 2 67  LEU 67  363 363 LEU LEU B . n 
B 2 68  ASP 68  364 364 ASP ASP B . n 
B 2 69  GLY 69  365 365 GLY GLY B . n 
B 2 70  GLY 70  366 366 GLY GLY B . n 
B 2 71  ILE 71  367 367 ILE ILE B . n 
B 2 72  GLU 72  368 368 GLU GLU B . n 
B 2 73  PRO 73  369 369 PRO PRO B . n 
B 2 74  TYR 74  370 370 TYR TYR B . n 
B 2 75  ARG 75  371 371 ARG ARG B . n 
B 2 76  LEU 76  372 372 LEU LEU B . n 
B 2 77  PRO 77  373 373 PRO PRO B . n 
B 2 78  GLU 78  374 374 GLU GLU B . n 
B 2 79  VAL 79  375 375 VAL VAL B . n 
B 2 80  ILE 80  376 376 ILE ILE B . n 
B 2 81  GLN 81  377 377 GLN GLN B . n 
B 2 82  LYS 82  378 378 LYS LYS B . n 
B 2 83  CYS 83  379 379 CYS CYS B . n 
B 2 84  ASN 84  380 380 ASN ASN B . n 
B 2 85  ALA 85  381 381 ALA ALA B . n 
B 2 86  ARG 86  382 382 ARG ARG B . n 
B 2 87  TRP 87  383 383 TRP TRP B . n 
B 2 88  THR 88  384 384 THR THR B . n 
B 2 89  THR 89  385 385 THR THR B . n 
B 2 90  GLU 90  386 386 GLU GLU B . n 
B 2 91  GLU 91  387 387 GLU GLU B . n 
B 2 92  GLN 92  388 388 GLN GLN B . n 
B 2 93  LEU 93  389 389 LEU LEU B . n 
B 2 94  LEU 94  390 390 LEU LEU B . n 
B 2 95  ALA 95  391 391 ALA ALA B . n 
B 2 96  VAL 96  392 392 VAL VAL B . n 
B 2 97  GLN 97  393 393 GLN GLN B . n 
B 2 98  ALA 98  394 394 ALA ALA B . n 
B 2 99  ILE 99  395 395 ILE ILE B . n 
B 2 100 ARG 100 396 396 ARG ARG B . n 
B 2 101 LYS 101 397 397 LYS LYS B . n 
B 2 102 TYR 102 398 398 TYR TYR B . n 
B 2 103 GLY 103 399 399 GLY GLY B . n 
B 2 104 ARG 104 400 400 ARG ARG B . n 
B 2 105 ASP 105 401 401 ASP ASP B . n 
B 2 106 PHE 106 402 402 PHE PHE B . n 
B 2 107 GLN 107 403 403 GLN GLN B . n 
B 2 108 ALA 108 404 404 ALA ALA B . n 
B 2 109 ILE 109 405 405 ILE ILE B . n 
B 2 110 SER 110 406 406 SER SER B . n 
B 2 111 ASP 111 407 407 ASP ASP B . n 
B 2 112 VAL 112 408 408 VAL VAL B . n 
B 2 113 ILE 113 409 409 ILE ILE B . n 
B 2 114 GLY 114 410 410 GLY GLY B . n 
B 2 115 ASN 115 411 411 ASN ASN B . n 
B 2 116 LYS 116 412 412 LYS LYS B . n 
B 2 117 SER 117 413 413 SER SER B . n 
B 2 118 VAL 118 414 414 VAL VAL B . n 
B 2 119 VAL 119 415 415 VAL VAL B . n 
B 2 120 GLN 120 416 416 GLN GLN B . n 
B 2 121 VAL 121 417 417 VAL VAL B . n 
B 2 122 LYS 122 418 418 LYS LYS B . n 
B 2 123 ASN 123 419 419 ASN ASN B . n 
B 2 124 PHE 124 420 420 PHE PHE B . n 
B 2 125 PHE 125 421 421 PHE PHE B . n 
B 2 126 VAL 126 422 422 VAL VAL B . n 
B 2 127 ASN 127 423 423 ASN ASN B . n 
B 2 128 TYR 128 424 424 TYR TYR B . n 
B 2 129 ARG 129 425 425 ARG ARG B . n 
B 2 130 ARG 130 426 426 ARG ARG B . n 
B 2 131 ARG 131 427 427 ARG ARG B . n 
B 2 132 PHE 132 428 428 PHE PHE B . n 
B 2 133 ASN 133 429 429 ASN ASN B . n 
B 2 134 ILE 134 430 430 ILE ILE B . n 
B 2 135 ASP 135 431 431 ASP ASP B . n 
B 2 136 GLU 136 432 432 GLU GLU B . n 
B 2 137 VAL 137 433 433 VAL VAL B . n 
B 2 138 LEU 138 434 434 LEU LEU B . n 
B 2 139 GLN 139 435 435 GLN GLN B . n 
B 2 140 GLU 140 436 436 GLU GLU B . n 
B 2 141 TRP 141 437 437 TRP TRP B . n 
B 2 142 GLU 142 438 438 GLU GLU B . n 
B 2 143 ALA 143 439 439 ALA ALA B . n 
B 2 144 GLU 144 440 440 GLU GLU B . n 
C 3 1   ALA 1   1   1   ALA ALA C . n 
C 3 2   ARG 2   2   2   ARG ARG C . n 
C 3 3   THR 3   3   3   THR THR C . n 
C 3 4   MET 4   4   4   MET MET C . n 
C 3 5   GLN 5   5   5   GLN GLN C . n 
C 3 6   THR 6   6   6   THR THR C . n 
C 3 7   ALA 7   7   7   ALA ALA C . n 
C 3 8   ARG 8   8   8   ARG ARG C . n 
C 3 9   LYS 9   9   9   LYS LYS C . n 
C 3 10  SER 10  10  10  SER SER C . n 
C 3 11  THR 11  11  11  THR THR C . n 
C 3 12  GLY 12  12  12  GLY GLY C . n 
C 3 13  GLY 13  13  13  GLY GLY C . n 
C 3 14  LYS 14  14  14  LYS LYS C . n 
C 3 15  ALA 15  15  15  ALA ALA C . n 
C 3 16  PRO 16  16  16  PRO PRO C . n 
C 3 17  ARG 17  17  ?   ?   ?   C . n 
C 3 18  LYS 18  18  ?   ?   ?   C . n 
C 3 19  GLN 19  19  ?   ?   ?   C . n 
C 3 20  LEU 20  20  ?   ?   ?   C . n 
C 3 21  ALA 21  21  ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HUF 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HUF 
_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        ? 
# 
_pdbx_nonpoly_scheme.asym_id         D 
_pdbx_nonpoly_scheme.entity_id       4 
_pdbx_nonpoly_scheme.mon_id          HUF 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     901 
_pdbx_nonpoly_scheme.auth_seq_num    901 
_pdbx_nonpoly_scheme.pdb_mon_id      HUF 
_pdbx_nonpoly_scheme.auth_mon_id     DRG 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.18.2_3874 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           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                     8UNI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     117.782 
_cell.length_a_esd                 ? 
_cell.length_b                     178.172 
_cell.length_b_esd                 ? 
_cell.length_c                     234.190 
_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                         8UNI 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8UNI 
_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             5.40 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          77.22 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.2 M Sodium Potassium Tartrate, 100 mM ADA pH 6.5' 
_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 EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-02-02 
_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   0.999998 
_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                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.999998 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8UNI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.40 
_reflns.d_resolution_low                               49.13 
_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                                     34222 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.07 
_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                                0.305 
_reflns.pdbx_Rpim_I_all                                0.116 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       233960 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.281 
_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                                    3.40 
_reflns_shell.d_res_low                                     3.57 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           31984 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4507 
_reflns_shell.percent_possible_obs                          99.8 
_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                               7.1 
_reflns_shell.pdbx_chi_squared                              1.15 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.7 
_reflns_shell.pdbx_Rrim_I_all                               3.512 
_reflns_shell.pdbx_Rpim_I_all                               1.311 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.495 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  3.254 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 8UNI 
_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                            3.40 
_refine.ls_d_res_low                             49.13 
_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                     33732 
_refine.ls_number_reflns_R_free                  1972 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.39 
_refine.ls_percent_reflns_R_free                 5.85 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2233 
_refine.ls_R_factor_R_free                       0.2524 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2215 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.33 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 31.27 
_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                             ? 
_refine.overall_SU_ML                            0.52 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.40 
_refine_hist.d_res_low                        49.13 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               6462 
_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        6407 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         55 
_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' ? 0.012  ? 6596 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.476  ? 8945 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.699 ? 922  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.074  ? 1003 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 1155 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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 
_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 
'X-RAY DIFFRACTION' 3.40 3.49  . . 119 1932 85.00  . . . . 0.4694 . . . . . . . . . . . 0.4960 
'X-RAY DIFFRACTION' 3.49 3.58  . . 142 2269 100.00 . . . . 0.3703 . . . . . . . . . . . 0.4144 
'X-RAY DIFFRACTION' 3.58 3.68  . . 140 2254 98.00  . . . . 0.3965 . . . . . . . . . . . 0.4057 
'X-RAY DIFFRACTION' 3.68 3.80  . . 139 2231 99.00  . . . . 0.3271 . . . . . . . . . . . 0.3624 
'X-RAY DIFFRACTION' 3.80 3.94  . . 138 2235 98.00  . . . . 0.3322 . . . . . . . . . . . 0.3355 
'X-RAY DIFFRACTION' 3.94 4.10  . . 142 2288 100.00 . . . . 0.2581 . . . . . . . . . . . 0.2853 
'X-RAY DIFFRACTION' 4.10 4.28  . . 143 2293 100.00 . . . . 0.2172 . . . . . . . . . . . 0.2462 
'X-RAY DIFFRACTION' 4.28 4.51  . . 141 2291 100.00 . . . . 0.1920 . . . . . . . . . . . 0.2235 
'X-RAY DIFFRACTION' 4.51 4.79  . . 141 2273 99.00  . . . . 0.1899 . . . . . . . . . . . 0.2475 
'X-RAY DIFFRACTION' 4.79 5.16  . . 143 2291 100.00 . . . . 0.1851 . . . . . . . . . . . 0.2208 
'X-RAY DIFFRACTION' 5.16 5.68  . . 144 2311 100.00 . . . . 0.1884 . . . . . . . . . . . 0.2153 
'X-RAY DIFFRACTION' 5.68 6.50  . . 142 2313 100.00 . . . . 0.1947 . . . . . . . . . . . 0.2148 
'X-RAY DIFFRACTION' 6.50 8.18  . . 147 2343 100.00 . . . . 0.1938 . . . . . . . . . . . 0.2121 
'X-RAY DIFFRACTION' 8.18 49.13 . . 151 2436 99.00  . . . . 0.1705 . . . . . . . . . . . 0.2091 
# 
_struct.entry_id                     8UNI 
_struct.title                        'LSD1-CoREST with N-formyl-FAD in complex with H3K4M histone tail' 
_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        8UNI 
_struct_keywords.text            
'Epigenetics, Histone demethylase, Drug resistance, Covalent inhibitor, OXIDOREDUCTASE, OXIDOREDUCTASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP KDM1A_HUMAN  O60341 ? 1 
;MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGS
AGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPP
EEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEA
PYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATF
RKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNV
LNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLV
KSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEF
TGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFV
PPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISD
DVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAG
EHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM
;
1   
2 UNP RCOR1_HUMAN  Q9UKL0 ? 2 
;RAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWT
TEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAE
;
308 
3 UNP V9H1G0_HUMAN V9H1G0 ? 3 ARTKQTARKSTGGKAPRKQLA 2   
# 
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 8UNI A 20 ? 871 ? O60341 1   ? 852 ? 1   852 
2 2 8UNI B 9  ? 144 ? Q9UKL0 308 ? 443 ? 305 440 
3 3 8UNI C 1  ? 21  ? V9H1G0 2   ? 22  ? 1   21  
# 
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 8UNI GLY A 1  ? UNP O60341 ?   ? 'expression tag'      -18 1  
1 8UNI SER A 2  ? UNP O60341 ?   ? 'expression tag'      -17 2  
1 8UNI SER A 3  ? UNP O60341 ?   ? 'expression tag'      -16 3  
1 8UNI HIS A 4  ? UNP O60341 ?   ? 'expression tag'      -15 4  
1 8UNI HIS A 5  ? UNP O60341 ?   ? 'expression tag'      -14 5  
1 8UNI HIS A 6  ? UNP O60341 ?   ? 'expression tag'      -13 6  
1 8UNI HIS A 7  ? UNP O60341 ?   ? 'expression tag'      -12 7  
1 8UNI HIS A 8  ? UNP O60341 ?   ? 'expression tag'      -11 8  
1 8UNI HIS A 9  ? UNP O60341 ?   ? 'expression tag'      -10 9  
1 8UNI SER A 10 ? UNP O60341 ?   ? 'expression tag'      -9  10 
1 8UNI SER A 11 ? UNP O60341 ?   ? 'expression tag'      -8  11 
1 8UNI GLY A 12 ? UNP O60341 ?   ? 'expression tag'      -7  12 
1 8UNI LEU A 13 ? UNP O60341 ?   ? 'expression tag'      -6  13 
1 8UNI VAL A 14 ? UNP O60341 ?   ? 'expression tag'      -5  14 
1 8UNI PRO A 15 ? UNP O60341 ?   ? 'expression tag'      -4  15 
1 8UNI ARG A 16 ? UNP O60341 ?   ? 'expression tag'      -3  16 
1 8UNI GLY A 17 ? UNP O60341 ?   ? 'expression tag'      -2  17 
1 8UNI SER A 18 ? UNP O60341 ?   ? 'expression tag'      -1  18 
1 8UNI HIS A 19 ? UNP O60341 ?   ? 'expression tag'      0   19 
2 8UNI GLY B 1  ? UNP Q9UKL0 ?   ? 'expression tag'      297 20 
2 8UNI PRO B 2  ? UNP Q9UKL0 ?   ? 'expression tag'      298 21 
2 8UNI LEU B 3  ? UNP Q9UKL0 ?   ? 'expression tag'      299 22 
2 8UNI GLY B 4  ? UNP Q9UKL0 ?   ? 'expression tag'      300 23 
2 8UNI SER B 5  ? UNP Q9UKL0 ?   ? 'expression tag'      301 24 
2 8UNI PRO B 6  ? UNP Q9UKL0 ?   ? 'expression tag'      302 25 
2 8UNI GLU B 7  ? UNP Q9UKL0 ?   ? 'expression tag'      303 26 
2 8UNI PHE B 8  ? UNP Q9UKL0 ?   ? 'expression tag'      304 27 
3 8UNI MET C 4  ? UNP V9H1G0 LYS 5 'engineered mutation' 4   28 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
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)' 7570  ? 
1 MORE         -46   ? 
1 'SSA (A^2)'  37770 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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 GLY A 192 ? SER A 200 ? GLY A 173 SER A 181 1 ? 9  
HELX_P HELX_P2  AA2 THR A 208 ? PHE A 215 ? THR A 189 PHE A 196 1 ? 8  
HELX_P HELX_P3  AA3 PHE A 215 ? SER A 220 ? PHE A 196 SER A 201 1 ? 6  
HELX_P HELX_P4  AA4 PRO A 222 ? ASN A 243 ? PRO A 203 ASN A 224 1 ? 22 
HELX_P HELX_P5  AA5 THR A 249 ? LEU A 257 ? THR A 230 LEU A 238 1 ? 9  
HELX_P HELX_P6  AA6 ASP A 264 ? HIS A 278 ? ASP A 245 HIS A 259 1 ? 15 
HELX_P HELX_P7  AA7 GLY A 306 ? GLY A 320 ? GLY A 287 GLY A 301 1 ? 15 
HELX_P HELX_P8  AA8 ASN A 359 ? VAL A 368 ? ASN A 340 VAL A 349 1 ? 10 
HELX_P HELX_P9  AA9 PRO A 390 ? GLN A 414 ? PRO A 371 GLN A 395 1 ? 25 
HELX_P HELX_P10 AB1 SER A 426 ? GLU A 486 ? SER A 407 GLU A 467 1 ? 61 
HELX_P HELX_P11 AB2 ASP A 492 ? ASN A 533 ? ASP A 473 ASN A 514 1 ? 42 
HELX_P HELX_P12 AB3 SER A 541 ? ASN A 559 ? SER A 522 ASN A 540 1 ? 19 
HELX_P HELX_P13 AB4 ASP A 574 ? GLU A 578 ? ASP A 555 GLU A 559 5 ? 5  
HELX_P HELX_P14 AB5 SER A 591 ? ALA A 598 ? SER A 572 ALA A 579 1 ? 8  
HELX_P HELX_P15 AB6 PRO A 645 ? GLN A 651 ? PRO A 626 GLN A 632 1 ? 7  
HELX_P HELX_P16 AB7 PRO A 663 ? MET A 673 ? PRO A 644 MET A 654 1 ? 11 
HELX_P HELX_P17 AB8 ALA A 727 ? MET A 734 ? ALA A 708 MET A 715 1 ? 8  
HELX_P HELX_P18 AB9 GLU A 735 ? ILE A 737 ? GLU A 716 ILE A 718 5 ? 3  
HELX_P HELX_P19 AC1 SER A 738 ? GLY A 755 ? SER A 719 GLY A 736 1 ? 18 
HELX_P HELX_P20 AC2 SER A 788 ? MET A 795 ? SER A 769 MET A 776 1 ? 8  
HELX_P HELX_P21 AC3 GLY A 819 ? ILE A 823 ? GLY A 800 ILE A 804 5 ? 5  
HELX_P HELX_P22 AC4 THR A 829 ? GLY A 850 ? THR A 810 GLY A 831 1 ? 22 
HELX_P HELX_P23 AC5 SER B 21  ? ALA B 30  ? SER B 317 ALA B 326 1 ? 10 
HELX_P HELX_P24 AC6 THR B 33  ? LEU B 39  ? THR B 329 LEU B 335 1 ? 7  
HELX_P HELX_P25 AC7 LEU B 39  ? GLN B 58  ? LEU B 335 GLN B 354 1 ? 20 
HELX_P HELX_P26 AC8 GLN B 58  ? LEU B 67  ? GLN B 354 LEU B 363 1 ? 10 
HELX_P HELX_P27 AC9 ILE B 71  ? ARG B 75  ? ILE B 367 ARG B 371 5 ? 5  
HELX_P HELX_P28 AD1 THR B 88  ? GLY B 103 ? THR B 384 GLY B 399 1 ? 16 
HELX_P HELX_P29 AD2 ASP B 105 ? ILE B 113 ? ASP B 401 ILE B 409 1 ? 9  
HELX_P HELX_P30 AD3 SER B 117 ? ARG B 129 ? SER B 413 ARG B 425 1 ? 13 
HELX_P HELX_P31 AD4 ASN B 133 ? ALA B 143 ? ASN B 429 ALA B 439 1 ? 11 
HELX_P HELX_P32 AD5 ALA C 1   ? GLN C 5   ? ALA C 1   GLN C 5   5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 259 A . ? ALA 240 A PRO 260 A ? PRO 241 A 1 15.18 
2 PRO 489 A . ? PRO 470 A PRO 490 A ? PRO 471 A 1 -8.09 
3 GLN 652 A . ? GLN 633 A PRO 653 A ? PRO 634 A 1 -5.93 
4 VAL 659 A . ? VAL 640 A PRO 660 A ? PRO 641 A 1 3.96  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? 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 ASP A 602 ? LYS A 604 ? ASP A 583 LYS A 585 
AA1 2 ASP A 322 ? LEU A 326 ? ASP A 303 LEU A 307 
AA1 3 LYS A 299 ? ILE A 303 ? LYS A 280 ILE A 284 
AA1 4 ALA A 639 ? CYS A 642 ? ALA A 620 CYS A 623 
AA1 5 LEU A 815 ? PHE A 817 ? LEU A 796 PHE A 798 
AA2 1 PHE A 339 ? LYS A 341 ? PHE A 320 LYS A 322 
AA2 2 TYR A 344 ? ALA A 346 ? TYR A 325 ALA A 327 
AA3 1 VAL A 352 ? THR A 354 ? VAL A 333 THR A 335 
AA3 2 HIS A 583 ? VAL A 586 ? HIS A 564 VAL A 567 
AA3 3 LEU A 372 ? LYS A 374 ? LEU A 353 LYS A 355 
AA4 1 VAL A 419 ? LEU A 420 ? VAL A 400 LEU A 401 
AA4 2 LYS A 423 ? PRO A 424 ? LYS A 404 PRO A 405 
AA5 1 THR A 632 ? CYS A 637 ? THR A 613 CYS A 618 
AA5 2 GLY A 618 ? ASN A 625 ? GLY A 599 ASN A 606 
AA5 3 THR A 607 ? THR A 615 ? THR A 588 THR A 596 
AA5 4 GLN A 657 ? VAL A 659 ? GLN A 638 VAL A 640 
AA6 1 GLY A 674 ? PHE A 675 ? GLY A 655 PHE A 656 
AA6 2 SER A 781 ? TYR A 782 ? SER A 762 TYR A 763 
AA7 1 LEU A 696 ? GLY A 698 ? LEU A 677 GLY A 679 
AA7 2 LEU A 712 ? TRP A 714 ? LEU A 693 TRP A 695 
AA7 3 ILE A 721 ? VAL A 726 ? ILE A 702 VAL A 707 
AA7 4 ASN A 679 ? CYS A 684 ? ASN A 660 CYS A 665 
AA7 5 GLU A 764 ? VAL A 767 ? GLU A 745 VAL A 748 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LYS A 604 ? O LYS A 585 N LEU A 325 ? N LEU A 306 
AA1 2 3 O LEU A 326 ? O LEU A 307 N ILE A 302 ? N ILE A 283 
AA1 3 4 N ILE A 303 ? N ILE A 284 O LEU A 641 ? O LEU A 622 
AA1 4 5 N VAL A 640 ? N VAL A 621 O PHE A 816 ? O PHE A 797 
AA2 1 2 N PHE A 339 ? N PHE A 320 O ALA A 346 ? O ALA A 327 
AA3 1 2 N VAL A 353 ? N VAL A 334 O LEU A 584 ? O LEU A 565 
AA3 2 3 O THR A 585 ? O THR A 566 N ALA A 373 ? N ALA A 354 
AA4 1 2 N LEU A 420 ? N LEU A 401 O LYS A 423 ? O LYS A 404 
AA5 1 2 O TYR A 635 ? O TYR A 616 N VAL A 621 ? N VAL A 602 
AA5 2 3 O GLY A 618 ? O GLY A 599 N THR A 615 ? N THR A 596 
AA5 3 4 N VAL A 612 ? N VAL A 593 O VAL A 659 ? O VAL A 640 
AA6 1 2 N GLY A 674 ? N GLY A 655 O TYR A 782 ? O TYR A 763 
AA7 1 2 N PHE A 697 ? N PHE A 678 O PHE A 713 ? O PHE A 694 
AA7 2 3 N LEU A 712 ? N LEU A 693 O LEU A 725 ? O LEU A 706 
AA7 3 4 O LEU A 722 ? O LEU A 703 N LEU A 683 ? N LEU A 664 
AA7 4 5 N VAL A 682 ? N VAL A 663 O VAL A 766 ? O VAL A 747 
# 
_pdbx_entry_details.entry_id                   8UNI 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B ARG 400 ? ? CD2 B PHE 402 ? ? 1.82 
2  1 O   A GLY 265 ? ? NH1 A ARG 295 ? ? 1.86 
3  1 CE2 A TYR 325 ? ? CB  A CYS 665 ? ? 1.86 
4  1 O   A PHE 670 ? ? CE1 A PHE 735 ? ? 1.93 
5  1 NH1 A ARG 316 ? ? O2A A HUF 901 ? ? 1.96 
6  1 O   A PHE 670 ? ? CD1 A PHE 735 ? ? 1.99 
7  1 OD2 A ASP 556 ? ? NH1 C ARG 2   ? ? 2.01 
8  1 O   A ALA 318 ? ? OD1 A ASP 328 ? ? 2.01 
9  1 O   B VAL 414 ? ? CG2 B VAL 417 ? ? 2.02 
10 1 OH  A TYR 325 ? ? O   A PHE 666 ? ? 2.03 
11 1 OD1 A ASP 486 ? ? OH  B TYR 398 ? ? 2.04 
12 1 O   A GLY 339 ? ? CE1 A PHE 560 ? ? 2.05 
13 1 OE1 B GLU 368 ? ? NH1 B ARG 371 ? ? 2.05 
14 1 OE2 A GLU 716 ? ? CA  A ARG 750 ? ? 2.06 
15 1 CG  A PRO 203 ? ? OG1 A THR 206 ? ? 2.06 
16 1 OE2 A GLU 381 ? ? OH  A TYR 520 ? ? 2.06 
17 1 OG  B SER 406 ? ? O   B LYS 412 ? ? 2.08 
18 1 NZ  A LYS 322 ? ? CD  A GLU 745 ? ? 2.12 
19 1 C   B VAL 414 ? ? CG2 B VAL 417 ? ? 2.17 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 224 ? ? -150.93 89.72   
2  1 SER A 244 ? ? -121.29 -54.97  
3  1 ILE A 270 ? ? -76.31  -70.75  
4  1 SER A 286 ? ? -85.87  39.78   
5  1 ASP A 397 ? ? 37.98   46.90   
6  1 LEU A 401 ? ? -167.95 117.30  
7  1 ASN A 403 ? ? 79.12   -9.26   
8  1 THR A 624 ? ? -85.68  43.66   
9  1 LEU A 677 ? ? -170.16 149.64  
10 1 HIS A 680 ? ? -166.02 118.27  
11 1 ALA A 708 ? ? -96.06  -158.72 
12 1 ALA A 757 ? ? -129.17 -70.06  
13 1 ARG A 758 ? ? 71.70   33.86   
14 1 SER A 760 ? ? -109.74 -76.37  
15 1 SER A 785 ? ? -71.49  -70.14  
16 1 PRO A 792 ? ? -83.85  -157.10 
17 1 TYR A 807 ? ? -148.57 46.12   
18 1 GLN B 337 ? ? -49.24  -18.03  
19 1 SER B 406 ? ? -86.95  41.52   
20 1 ASP B 407 ? ? -130.33 -46.97  
21 1 LYS C 9   ? ? -37.09  129.61  
22 1 ALA C 15  ? ? -111.17 69.58   
# 
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 -18 ? A GLY 1   
2   1 Y 1 A SER -17 ? A SER 2   
3   1 Y 1 A SER -16 ? A SER 3   
4   1 Y 1 A HIS -15 ? A HIS 4   
5   1 Y 1 A HIS -14 ? A HIS 5   
6   1 Y 1 A HIS -13 ? A HIS 6   
7   1 Y 1 A HIS -12 ? A HIS 7   
8   1 Y 1 A HIS -11 ? A HIS 8   
9   1 Y 1 A HIS -10 ? A HIS 9   
10  1 Y 1 A SER -9  ? A SER 10  
11  1 Y 1 A SER -8  ? A SER 11  
12  1 Y 1 A GLY -7  ? A GLY 12  
13  1 Y 1 A LEU -6  ? A LEU 13  
14  1 Y 1 A VAL -5  ? A VAL 14  
15  1 Y 1 A PRO -4  ? A PRO 15  
16  1 Y 1 A ARG -3  ? A ARG 16  
17  1 Y 1 A GLY -2  ? A GLY 17  
18  1 Y 1 A SER -1  ? A SER 18  
19  1 Y 1 A HIS 0   ? A HIS 19  
20  1 Y 1 A MET 1   ? A MET 20  
21  1 Y 1 A LEU 2   ? A LEU 21  
22  1 Y 1 A SER 3   ? A SER 22  
23  1 Y 1 A GLY 4   ? A GLY 23  
24  1 Y 1 A LYS 5   ? A LYS 24  
25  1 Y 1 A LYS 6   ? A LYS 25  
26  1 Y 1 A ALA 7   ? A ALA 26  
27  1 Y 1 A ALA 8   ? A ALA 27  
28  1 Y 1 A ALA 9   ? A ALA 28  
29  1 Y 1 A ALA 10  ? A ALA 29  
30  1 Y 1 A ALA 11  ? A ALA 30  
31  1 Y 1 A ALA 12  ? A ALA 31  
32  1 Y 1 A ALA 13  ? A ALA 32  
33  1 Y 1 A ALA 14  ? A ALA 33  
34  1 Y 1 A ALA 15  ? A ALA 34  
35  1 Y 1 A ALA 16  ? A ALA 35  
36  1 Y 1 A ALA 17  ? A ALA 36  
37  1 Y 1 A ALA 18  ? A ALA 37  
38  1 Y 1 A THR 19  ? A THR 38  
39  1 Y 1 A GLY 20  ? A GLY 39  
40  1 Y 1 A THR 21  ? A THR 40  
41  1 Y 1 A GLU 22  ? A GLU 41  
42  1 Y 1 A ALA 23  ? A ALA 42  
43  1 Y 1 A GLY 24  ? A GLY 43  
44  1 Y 1 A PRO 25  ? A PRO 44  
45  1 Y 1 A GLY 26  ? A GLY 45  
46  1 Y 1 A THR 27  ? A THR 46  
47  1 Y 1 A ALA 28  ? A ALA 47  
48  1 Y 1 A GLY 29  ? A GLY 48  
49  1 Y 1 A GLY 30  ? A GLY 49  
50  1 Y 1 A SER 31  ? A SER 50  
51  1 Y 1 A GLU 32  ? A GLU 51  
52  1 Y 1 A ASN 33  ? A ASN 52  
53  1 Y 1 A GLY 34  ? A GLY 53  
54  1 Y 1 A SER 35  ? A SER 54  
55  1 Y 1 A GLU 36  ? A GLU 55  
56  1 Y 1 A VAL 37  ? A VAL 56  
57  1 Y 1 A ALA 38  ? A ALA 57  
58  1 Y 1 A ALA 39  ? A ALA 58  
59  1 Y 1 A GLN 40  ? A GLN 59  
60  1 Y 1 A PRO 41  ? A PRO 60  
61  1 Y 1 A ALA 42  ? A ALA 61  
62  1 Y 1 A GLY 43  ? A GLY 62  
63  1 Y 1 A LEU 44  ? A LEU 63  
64  1 Y 1 A SER 45  ? A SER 64  
65  1 Y 1 A GLY 46  ? A GLY 65  
66  1 Y 1 A PRO 47  ? A PRO 66  
67  1 Y 1 A ALA 48  ? A ALA 67  
68  1 Y 1 A GLU 49  ? A GLU 68  
69  1 Y 1 A VAL 50  ? A VAL 69  
70  1 Y 1 A GLY 51  ? A GLY 70  
71  1 Y 1 A PRO 52  ? A PRO 71  
72  1 Y 1 A GLY 53  ? A GLY 72  
73  1 Y 1 A ALA 54  ? A ALA 73  
74  1 Y 1 A VAL 55  ? A VAL 74  
75  1 Y 1 A GLY 56  ? A GLY 75  
76  1 Y 1 A GLU 57  ? A GLU 76  
77  1 Y 1 A ARG 58  ? A ARG 77  
78  1 Y 1 A THR 59  ? A THR 78  
79  1 Y 1 A PRO 60  ? A PRO 79  
80  1 Y 1 A ARG 61  ? A ARG 80  
81  1 Y 1 A LYS 62  ? A LYS 81  
82  1 Y 1 A LYS 63  ? A LYS 82  
83  1 Y 1 A GLU 64  ? A GLU 83  
84  1 Y 1 A PRO 65  ? A PRO 84  
85  1 Y 1 A PRO 66  ? A PRO 85  
86  1 Y 1 A ARG 67  ? A ARG 86  
87  1 Y 1 A ALA 68  ? A ALA 87  
88  1 Y 1 A SER 69  ? A SER 88  
89  1 Y 1 A PRO 70  ? A PRO 89  
90  1 Y 1 A PRO 71  ? A PRO 90  
91  1 Y 1 A GLY 72  ? A GLY 91  
92  1 Y 1 A GLY 73  ? A GLY 92  
93  1 Y 1 A LEU 74  ? A LEU 93  
94  1 Y 1 A ALA 75  ? A ALA 94  
95  1 Y 1 A GLU 76  ? A GLU 95  
96  1 Y 1 A PRO 77  ? A PRO 96  
97  1 Y 1 A PRO 78  ? A PRO 97  
98  1 Y 1 A GLY 79  ? A GLY 98  
99  1 Y 1 A SER 80  ? A SER 99  
100 1 Y 1 A ALA 81  ? A ALA 100 
101 1 Y 1 A GLY 82  ? A GLY 101 
102 1 Y 1 A PRO 83  ? A PRO 102 
103 1 Y 1 A GLN 84  ? A GLN 103 
104 1 Y 1 A ALA 85  ? A ALA 104 
105 1 Y 1 A GLY 86  ? A GLY 105 
106 1 Y 1 A PRO 87  ? A PRO 106 
107 1 Y 1 A THR 88  ? A THR 107 
108 1 Y 1 A VAL 89  ? A VAL 108 
109 1 Y 1 A VAL 90  ? A VAL 109 
110 1 Y 1 A PRO 91  ? A PRO 110 
111 1 Y 1 A GLY 92  ? A GLY 111 
112 1 Y 1 A SER 93  ? A SER 112 
113 1 Y 1 A ALA 94  ? A ALA 113 
114 1 Y 1 A THR 95  ? A THR 114 
115 1 Y 1 A PRO 96  ? A PRO 115 
116 1 Y 1 A MET 97  ? A MET 116 
117 1 Y 1 A GLU 98  ? A GLU 117 
118 1 Y 1 A THR 99  ? A THR 118 
119 1 Y 1 A GLY 100 ? A GLY 119 
120 1 Y 1 A ILE 101 ? A ILE 120 
121 1 Y 1 A ALA 102 ? A ALA 121 
122 1 Y 1 A GLU 103 ? A GLU 122 
123 1 Y 1 A THR 104 ? A THR 123 
124 1 Y 1 A PRO 105 ? A PRO 124 
125 1 Y 1 A GLU 106 ? A GLU 125 
126 1 Y 1 A GLY 107 ? A GLY 126 
127 1 Y 1 A ARG 108 ? A ARG 127 
128 1 Y 1 A ARG 109 ? A ARG 128 
129 1 Y 1 A THR 110 ? A THR 129 
130 1 Y 1 A SER 111 ? A SER 130 
131 1 Y 1 A ARG 112 ? A ARG 131 
132 1 Y 1 A ARG 113 ? A ARG 132 
133 1 Y 1 A LYS 114 ? A LYS 133 
134 1 Y 1 A ARG 115 ? A ARG 134 
135 1 Y 1 A ALA 116 ? A ALA 135 
136 1 Y 1 A LYS 117 ? A LYS 136 
137 1 Y 1 A VAL 118 ? A VAL 137 
138 1 Y 1 A GLU 119 ? A GLU 138 
139 1 Y 1 A TYR 120 ? A TYR 139 
140 1 Y 1 A ARG 121 ? A ARG 140 
141 1 Y 1 A GLU 122 ? A GLU 141 
142 1 Y 1 A MET 123 ? A MET 142 
143 1 Y 1 A ASP 124 ? A ASP 143 
144 1 Y 1 A GLU 125 ? A GLU 144 
145 1 Y 1 A SER 126 ? A SER 145 
146 1 Y 1 A LEU 127 ? A LEU 146 
147 1 Y 1 A ALA 128 ? A ALA 147 
148 1 Y 1 A ASN 129 ? A ASN 148 
149 1 Y 1 A LEU 130 ? A LEU 149 
150 1 Y 1 A SER 131 ? A SER 150 
151 1 Y 1 A GLU 132 ? A GLU 151 
152 1 Y 1 A ASP 133 ? A ASP 152 
153 1 Y 1 A GLU 134 ? A GLU 153 
154 1 Y 1 A TYR 135 ? A TYR 154 
155 1 Y 1 A TYR 136 ? A TYR 155 
156 1 Y 1 A SER 137 ? A SER 156 
157 1 Y 1 A GLU 138 ? A GLU 157 
158 1 Y 1 A GLU 139 ? A GLU 158 
159 1 Y 1 A GLU 140 ? A GLU 159 
160 1 Y 1 A ARG 141 ? A ARG 160 
161 1 Y 1 A ASN 142 ? A ASN 161 
162 1 Y 1 A ALA 143 ? A ALA 162 
163 1 Y 1 A LYS 144 ? A LYS 163 
164 1 Y 1 A ALA 145 ? A ALA 164 
165 1 Y 1 A GLU 146 ? A GLU 165 
166 1 Y 1 A LYS 147 ? A LYS 166 
167 1 Y 1 A GLU 148 ? A GLU 167 
168 1 Y 1 A LYS 149 ? A LYS 168 
169 1 Y 1 A LYS 150 ? A LYS 169 
170 1 Y 1 A LEU 151 ? A LEU 170 
171 1 Y 1 A PRO 152 ? A PRO 171 
172 1 Y 1 A PRO 153 ? A PRO 172 
173 1 Y 1 A PRO 154 ? A PRO 173 
174 1 Y 1 A PRO 155 ? A PRO 174 
175 1 Y 1 A PRO 156 ? A PRO 175 
176 1 Y 1 A GLN 157 ? A GLN 176 
177 1 Y 1 A ALA 158 ? A ALA 177 
178 1 Y 1 A PRO 159 ? A PRO 178 
179 1 Y 1 A PRO 160 ? A PRO 179 
180 1 Y 1 A GLU 161 ? A GLU 180 
181 1 Y 1 A GLU 162 ? A GLU 181 
182 1 Y 1 A GLU 163 ? A GLU 182 
183 1 Y 1 A ASN 164 ? A ASN 183 
184 1 Y 1 A GLU 165 ? A GLU 184 
185 1 Y 1 A SER 166 ? A SER 185 
186 1 Y 1 A GLU 167 ? A GLU 186 
187 1 Y 1 A PRO 168 ? A PRO 187 
188 1 Y 1 A GLU 169 ? A GLU 188 
189 1 Y 1 A GLU 170 ? A GLU 189 
190 1 Y 1 A PRO 837 ? A PRO 856 
191 1 Y 1 A ARG 838 ? A ARG 857 
192 1 Y 1 A GLN 839 ? A GLN 858 
193 1 Y 1 A ALA 840 ? A ALA 859 
194 1 Y 1 A THR 841 ? A THR 860 
195 1 Y 1 A PRO 842 ? A PRO 861 
196 1 Y 1 A GLY 843 ? A GLY 862 
197 1 Y 1 A VAL 844 ? A VAL 863 
198 1 Y 1 A PRO 845 ? A PRO 864 
199 1 Y 1 A ALA 846 ? A ALA 865 
200 1 Y 1 A GLN 847 ? A GLN 866 
201 1 Y 1 A GLN 848 ? A GLN 867 
202 1 Y 1 A SER 849 ? A SER 868 
203 1 Y 1 A PRO 850 ? A PRO 869 
204 1 Y 1 A SER 851 ? A SER 870 
205 1 Y 1 A MET 852 ? A MET 871 
206 1 Y 1 B GLY 297 ? B GLY 1   
207 1 Y 1 B PRO 298 ? B PRO 2   
208 1 Y 1 B LEU 299 ? B LEU 3   
209 1 Y 1 B GLY 300 ? B GLY 4   
210 1 Y 1 B SER 301 ? B SER 5   
211 1 Y 1 B PRO 302 ? B PRO 6   
212 1 Y 1 B GLU 303 ? B GLU 7   
213 1 Y 1 B PHE 304 ? B PHE 8   
214 1 Y 1 B ARG 305 ? B ARG 9   
215 1 Y 1 B ALA 306 ? B ALA 10  
216 1 Y 1 B LYS 307 ? B LYS 11  
217 1 Y 1 C ARG 17  ? C ARG 17  
218 1 Y 1 C LYS 18  ? C LYS 18  
219 1 Y 1 C GLN 19  ? C GLN 19  
220 1 Y 1 C LEU 20  ? C LEU 20  
221 1 Y 1 C ALA 21  ? C ALA 21  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N     N N N 1   
ALA CA    C N S 2   
ALA C     C N N 3   
ALA O     O N N 4   
ALA CB    C N N 5   
ALA OXT   O N N 6   
ALA H     H N N 7   
ALA H2    H N N 8   
ALA HA    H N N 9   
ALA HB1   H N N 10  
ALA HB2   H N N 11  
ALA HB3   H N N 12  
ALA HXT   H N N 13  
ARG N     N N N 14  
ARG CA    C N S 15  
ARG C     C N N 16  
ARG O     O N N 17  
ARG CB    C N N 18  
ARG CG    C N N 19  
ARG CD    C N N 20  
ARG NE    N N N 21  
ARG CZ    C N N 22  
ARG NH1   N N N 23  
ARG NH2   N N N 24  
ARG OXT   O N N 25  
ARG H     H N N 26  
ARG H2    H N N 27  
ARG HA    H N N 28  
ARG HB2   H N N 29  
ARG HB3   H N N 30  
ARG HG2   H N N 31  
ARG HG3   H N N 32  
ARG HD2   H N N 33  
ARG HD3   H N N 34  
ARG HE    H N N 35  
ARG HH11  H N N 36  
ARG HH12  H N N 37  
ARG HH21  H N N 38  
ARG HH22  H N N 39  
ARG HXT   H N N 40  
ASN N     N N N 41  
ASN CA    C N S 42  
ASN C     C N N 43  
ASN O     O N N 44  
ASN CB    C N N 45  
ASN CG    C N N 46  
ASN OD1   O N N 47  
ASN ND2   N N N 48  
ASN OXT   O N N 49  
ASN H     H N N 50  
ASN H2    H N N 51  
ASN HA    H N N 52  
ASN HB2   H N N 53  
ASN HB3   H N N 54  
ASN HD21  H N N 55  
ASN HD22  H N N 56  
ASN HXT   H N N 57  
ASP N     N N N 58  
ASP CA    C N S 59  
ASP C     C N N 60  
ASP O     O N N 61  
ASP CB    C N N 62  
ASP CG    C N N 63  
ASP OD1   O N N 64  
ASP OD2   O N N 65  
ASP OXT   O N N 66  
ASP H     H N N 67  
ASP H2    H N N 68  
ASP HA    H N N 69  
ASP HB2   H N N 70  
ASP HB3   H N N 71  
ASP HD2   H N N 72  
ASP HXT   H N N 73  
CYS N     N N N 74  
CYS CA    C N R 75  
CYS C     C N N 76  
CYS O     O N N 77  
CYS CB    C N N 78  
CYS SG    S N N 79  
CYS OXT   O N N 80  
CYS H     H N N 81  
CYS H2    H N N 82  
CYS HA    H N N 83  
CYS HB2   H N N 84  
CYS HB3   H N N 85  
CYS HG    H N N 86  
CYS HXT   H N N 87  
GLN N     N N N 88  
GLN CA    C N S 89  
GLN C     C N N 90  
GLN O     O N N 91  
GLN CB    C N N 92  
GLN CG    C N N 93  
GLN CD    C N N 94  
GLN OE1   O N N 95  
GLN NE2   N N N 96  
GLN OXT   O N N 97  
GLN H     H N N 98  
GLN H2    H N N 99  
GLN HA    H N N 100 
GLN HB2   H N N 101 
GLN HB3   H N N 102 
GLN HG2   H N N 103 
GLN HG3   H N N 104 
GLN HE21  H N N 105 
GLN HE22  H N N 106 
GLN HXT   H N N 107 
GLU N     N N N 108 
GLU CA    C N S 109 
GLU C     C N N 110 
GLU O     O N N 111 
GLU CB    C N N 112 
GLU CG    C N N 113 
GLU CD    C N N 114 
GLU OE1   O N N 115 
GLU OE2   O N N 116 
GLU OXT   O N N 117 
GLU H     H N N 118 
GLU H2    H N N 119 
GLU HA    H N N 120 
GLU HB2   H N N 121 
GLU HB3   H N N 122 
GLU HG2   H N N 123 
GLU HG3   H N N 124 
GLU HE2   H N N 125 
GLU HXT   H N N 126 
GLY N     N N N 127 
GLY CA    C N N 128 
GLY C     C N N 129 
GLY O     O N N 130 
GLY OXT   O N N 131 
GLY H     H N N 132 
GLY H2    H N N 133 
GLY HA2   H N N 134 
GLY HA3   H N N 135 
GLY HXT   H N N 136 
HIS N     N N N 137 
HIS CA    C N S 138 
HIS C     C N N 139 
HIS O     O N N 140 
HIS CB    C N N 141 
HIS CG    C Y N 142 
HIS ND1   N Y N 143 
HIS CD2   C Y N 144 
HIS CE1   C Y N 145 
HIS NE2   N Y N 146 
HIS OXT   O N N 147 
HIS H     H N N 148 
HIS H2    H N N 149 
HIS HA    H N N 150 
HIS HB2   H N N 151 
HIS HB3   H N N 152 
HIS HD1   H N N 153 
HIS HD2   H N N 154 
HIS HE1   H N N 155 
HIS HE2   H N N 156 
HIS HXT   H N N 157 
HUF O2A   O N N 158 
HUF PA    P N N 159 
HUF O1A   O N N 160 
HUF O3A   O N N 161 
HUF PB    P N N 162 
HUF O3B   O N N 163 
HUF O2B   O N N 164 
HUF O1B   O N N 165 
HUF "O5'" O N N 166 
HUF "C5'" C N N 167 
HUF "C4'" C N R 168 
HUF "C3'" C N S 169 
HUF "O3'" O N N 170 
HUF "C2'" C N R 171 
HUF "O2'" O N N 172 
HUF "C1'" C N R 173 
HUF "O4'" O N N 174 
HUF N9    N Y N 175 
HUF C4    C Y N 176 
HUF C5    C Y N 177 
HUF N7    N Y N 178 
HUF C8    C Y N 179 
HUF N3    N Y N 180 
HUF C2    C Y N 181 
HUF N1    N Y N 182 
HUF C6    C Y N 183 
HUF N6    N N N 184 
HUF C11   C N N 185 
HUF C12   C Y N 186 
HUF C13   C Y N 187 
HUF C14   C Y N 188 
HUF C15   C Y N 189 
HUF C16   C Y N 190 
HUF C17   C Y N 191 
HUF C18   C N N 192 
HUF C19   C N N 193 
HUF C20   C N N 194 
HUF C21   C N N 195 
HUF C22   C N N 196 
HUF C23   C N N 197 
HUF C24   C N N 198 
HUF C25   C N S 199 
HUF C26   C N S 200 
HUF C27   C N R 201 
HUF C28   C N N 202 
HUF N29   N N N 203 
HUF N30   N N N 204 
HUF N31   N N N 205 
HUF N32   N N N 206 
HUF O33   O N N 207 
HUF O34   O N N 208 
HUF O35   O N N 209 
HUF O36   O N N 210 
HUF O37   O N N 211 
HUF O38   O N N 212 
HUF H1    H N N 213 
HUF H2    H N N 214 
HUF H3    H N N 215 
HUF H4    H N N 216 
HUF H5    H N N 217 
HUF H6    H N N 218 
HUF H7    H N N 219 
HUF H8    H N N 220 
HUF H9    H N N 221 
HUF H10   H N N 222 
HUF H11   H N N 223 
HUF H12   H N N 224 
HUF H13   H N N 225 
HUF H14   H N N 226 
HUF H15   H N N 227 
HUF H16   H N N 228 
HUF H17   H N N 229 
HUF H18   H N N 230 
HUF H19   H N N 231 
HUF H20   H N N 232 
HUF H21   H N N 233 
HUF H22   H N N 234 
HUF H23   H N N 235 
HUF H24   H N N 236 
HUF H25   H N N 237 
HUF H26   H N N 238 
HUF H27   H N N 239 
HUF H28   H N N 240 
HUF H29   H N N 241 
HUF H30   H N N 242 
HUF H31   H N N 243 
HUF H32   H N N 244 
HUF H33   H N N 245 
HUF H34   H N N 246 
HUF H35   H N N 247 
ILE N     N N N 248 
ILE CA    C N S 249 
ILE C     C N N 250 
ILE O     O N N 251 
ILE CB    C N S 252 
ILE CG1   C N N 253 
ILE CG2   C N N 254 
ILE CD1   C N N 255 
ILE OXT   O N N 256 
ILE H     H N N 257 
ILE H2    H N N 258 
ILE HA    H N N 259 
ILE HB    H N N 260 
ILE HG12  H N N 261 
ILE HG13  H N N 262 
ILE HG21  H N N 263 
ILE HG22  H N N 264 
ILE HG23  H N N 265 
ILE HD11  H N N 266 
ILE HD12  H N N 267 
ILE HD13  H N N 268 
ILE HXT   H N N 269 
LEU N     N N N 270 
LEU CA    C N S 271 
LEU C     C N N 272 
LEU O     O N N 273 
LEU CB    C N N 274 
LEU CG    C N N 275 
LEU CD1   C N N 276 
LEU CD2   C N N 277 
LEU OXT   O N N 278 
LEU H     H N N 279 
LEU H2    H N N 280 
LEU HA    H N N 281 
LEU HB2   H N N 282 
LEU HB3   H N N 283 
LEU HG    H N N 284 
LEU HD11  H N N 285 
LEU HD12  H N N 286 
LEU HD13  H N N 287 
LEU HD21  H N N 288 
LEU HD22  H N N 289 
LEU HD23  H N N 290 
LEU HXT   H N N 291 
LYS N     N N N 292 
LYS CA    C N S 293 
LYS C     C N N 294 
LYS O     O N N 295 
LYS CB    C N N 296 
LYS CG    C N N 297 
LYS CD    C N N 298 
LYS CE    C N N 299 
LYS NZ    N N N 300 
LYS OXT   O N N 301 
LYS H     H N N 302 
LYS H2    H N N 303 
LYS HA    H N N 304 
LYS HB2   H N N 305 
LYS HB3   H N N 306 
LYS HG2   H N N 307 
LYS HG3   H N N 308 
LYS HD2   H N N 309 
LYS HD3   H N N 310 
LYS HE2   H N N 311 
LYS HE3   H N N 312 
LYS HZ1   H N N 313 
LYS HZ2   H N N 314 
LYS HZ3   H N N 315 
LYS HXT   H N N 316 
MET N     N N N 317 
MET CA    C N S 318 
MET C     C N N 319 
MET O     O N N 320 
MET CB    C N N 321 
MET CG    C N N 322 
MET SD    S N N 323 
MET CE    C N N 324 
MET OXT   O N N 325 
MET H     H N N 326 
MET H2    H N N 327 
MET HA    H N N 328 
MET HB2   H N N 329 
MET HB3   H N N 330 
MET HG2   H N N 331 
MET HG3   H N N 332 
MET HE1   H N N 333 
MET HE2   H N N 334 
MET HE3   H N N 335 
MET HXT   H N N 336 
PHE N     N N N 337 
PHE CA    C N S 338 
PHE C     C N N 339 
PHE O     O N N 340 
PHE CB    C N N 341 
PHE CG    C Y N 342 
PHE CD1   C Y N 343 
PHE CD2   C Y N 344 
PHE CE1   C Y N 345 
PHE CE2   C Y N 346 
PHE CZ    C Y N 347 
PHE OXT   O N N 348 
PHE H     H N N 349 
PHE H2    H N N 350 
PHE HA    H N N 351 
PHE HB2   H N N 352 
PHE HB3   H N N 353 
PHE HD1   H N N 354 
PHE HD2   H N N 355 
PHE HE1   H N N 356 
PHE HE2   H N N 357 
PHE HZ    H N N 358 
PHE HXT   H N N 359 
PRO N     N N N 360 
PRO CA    C N S 361 
PRO C     C N N 362 
PRO O     O N N 363 
PRO CB    C N N 364 
PRO CG    C N N 365 
PRO CD    C N N 366 
PRO OXT   O N N 367 
PRO H     H N N 368 
PRO HA    H N N 369 
PRO HB2   H N N 370 
PRO HB3   H N N 371 
PRO HG2   H N N 372 
PRO HG3   H N N 373 
PRO HD2   H N N 374 
PRO HD3   H N N 375 
PRO HXT   H N N 376 
SER N     N N N 377 
SER CA    C N S 378 
SER C     C N N 379 
SER O     O N N 380 
SER CB    C N N 381 
SER OG    O N N 382 
SER OXT   O N N 383 
SER H     H N N 384 
SER H2    H N N 385 
SER HA    H N N 386 
SER HB2   H N N 387 
SER HB3   H N N 388 
SER HG    H N N 389 
SER HXT   H N N 390 
THR N     N N N 391 
THR CA    C N S 392 
THR C     C N N 393 
THR O     O N N 394 
THR CB    C N R 395 
THR OG1   O N N 396 
THR CG2   C N N 397 
THR OXT   O N N 398 
THR H     H N N 399 
THR H2    H N N 400 
THR HA    H N N 401 
THR HB    H N N 402 
THR HG1   H N N 403 
THR HG21  H N N 404 
THR HG22  H N N 405 
THR HG23  H N N 406 
THR HXT   H N N 407 
TRP N     N N N 408 
TRP CA    C N S 409 
TRP C     C N N 410 
TRP O     O N N 411 
TRP CB    C N N 412 
TRP CG    C Y N 413 
TRP CD1   C Y N 414 
TRP CD2   C Y N 415 
TRP NE1   N Y N 416 
TRP CE2   C Y N 417 
TRP CE3   C Y N 418 
TRP CZ2   C Y N 419 
TRP CZ3   C Y N 420 
TRP CH2   C Y N 421 
TRP OXT   O N N 422 
TRP H     H N N 423 
TRP H2    H N N 424 
TRP HA    H N N 425 
TRP HB2   H N N 426 
TRP HB3   H N N 427 
TRP HD1   H N N 428 
TRP HE1   H N N 429 
TRP HE3   H N N 430 
TRP HZ2   H N N 431 
TRP HZ3   H N N 432 
TRP HH2   H N N 433 
TRP HXT   H N N 434 
TYR N     N N N 435 
TYR CA    C N S 436 
TYR C     C N N 437 
TYR O     O N N 438 
TYR CB    C N N 439 
TYR CG    C Y N 440 
TYR CD1   C Y N 441 
TYR CD2   C Y N 442 
TYR CE1   C Y N 443 
TYR CE2   C Y N 444 
TYR CZ    C Y N 445 
TYR OH    O N N 446 
TYR OXT   O N N 447 
TYR H     H N N 448 
TYR H2    H N N 449 
TYR HA    H N N 450 
TYR HB2   H N N 451 
TYR HB3   H N N 452 
TYR HD1   H N N 453 
TYR HD2   H N N 454 
TYR HE1   H N N 455 
TYR HE2   H N N 456 
TYR HH    H N N 457 
TYR HXT   H N N 458 
VAL N     N N N 459 
VAL CA    C N S 460 
VAL C     C N N 461 
VAL O     O N N 462 
VAL CB    C N N 463 
VAL CG1   C N N 464 
VAL CG2   C N N 465 
VAL OXT   O N N 466 
VAL H     H N N 467 
VAL H2    H N N 468 
VAL HA    H N N 469 
VAL HB    H N N 470 
VAL HG11  H N N 471 
VAL HG12  H N N 472 
VAL HG13  H N N 473 
VAL HG21  H N N 474 
VAL HG22  H N N 475 
VAL HG23  H N N 476 
VAL HXT   H N N 477 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA    sing N N 1   
ALA N     H     sing N N 2   
ALA N     H2    sing N N 3   
ALA CA    C     sing N N 4   
ALA CA    CB    sing N N 5   
ALA CA    HA    sing N N 6   
ALA C     O     doub N N 7   
ALA C     OXT   sing N N 8   
ALA CB    HB1   sing N N 9   
ALA CB    HB2   sing N N 10  
ALA CB    HB3   sing N N 11  
ALA OXT   HXT   sing N N 12  
ARG N     CA    sing N N 13  
ARG N     H     sing N N 14  
ARG N     H2    sing N N 15  
ARG CA    C     sing N N 16  
ARG CA    CB    sing N N 17  
ARG CA    HA    sing N N 18  
ARG C     O     doub N N 19  
ARG C     OXT   sing N N 20  
ARG CB    CG    sing N N 21  
ARG CB    HB2   sing N N 22  
ARG CB    HB3   sing N N 23  
ARG CG    CD    sing N N 24  
ARG CG    HG2   sing N N 25  
ARG CG    HG3   sing N N 26  
ARG CD    NE    sing N N 27  
ARG CD    HD2   sing N N 28  
ARG CD    HD3   sing N N 29  
ARG NE    CZ    sing N N 30  
ARG NE    HE    sing N N 31  
ARG CZ    NH1   sing N N 32  
ARG CZ    NH2   doub N N 33  
ARG NH1   HH11  sing N N 34  
ARG NH1   HH12  sing N N 35  
ARG NH2   HH21  sing N N 36  
ARG NH2   HH22  sing N N 37  
ARG OXT   HXT   sing N N 38  
ASN N     CA    sing N N 39  
ASN N     H     sing N N 40  
ASN N     H2    sing N N 41  
ASN CA    C     sing N N 42  
ASN CA    CB    sing N N 43  
ASN CA    HA    sing N N 44  
ASN C     O     doub N N 45  
ASN C     OXT   sing N N 46  
ASN CB    CG    sing N N 47  
ASN CB    HB2   sing N N 48  
ASN CB    HB3   sing N N 49  
ASN CG    OD1   doub N N 50  
ASN CG    ND2   sing N N 51  
ASN ND2   HD21  sing N N 52  
ASN ND2   HD22  sing N N 53  
ASN OXT   HXT   sing N N 54  
ASP N     CA    sing N N 55  
ASP N     H     sing N N 56  
ASP N     H2    sing N N 57  
ASP CA    C     sing N N 58  
ASP CA    CB    sing N N 59  
ASP CA    HA    sing N N 60  
ASP C     O     doub N N 61  
ASP C     OXT   sing N N 62  
ASP CB    CG    sing N N 63  
ASP CB    HB2   sing N N 64  
ASP CB    HB3   sing N N 65  
ASP CG    OD1   doub N N 66  
ASP CG    OD2   sing N N 67  
ASP OD2   HD2   sing N N 68  
ASP OXT   HXT   sing N N 69  
CYS N     CA    sing N N 70  
CYS N     H     sing N N 71  
CYS N     H2    sing N N 72  
CYS CA    C     sing N N 73  
CYS CA    CB    sing N N 74  
CYS CA    HA    sing N N 75  
CYS C     O     doub N N 76  
CYS C     OXT   sing N N 77  
CYS CB    SG    sing N N 78  
CYS CB    HB2   sing N N 79  
CYS CB    HB3   sing N N 80  
CYS SG    HG    sing N N 81  
CYS OXT   HXT   sing N N 82  
GLN N     CA    sing N N 83  
GLN N     H     sing N N 84  
GLN N     H2    sing N N 85  
GLN CA    C     sing N N 86  
GLN CA    CB    sing N N 87  
GLN CA    HA    sing N N 88  
GLN C     O     doub N N 89  
GLN C     OXT   sing N N 90  
GLN CB    CG    sing N N 91  
GLN CB    HB2   sing N N 92  
GLN CB    HB3   sing N N 93  
GLN CG    CD    sing N N 94  
GLN CG    HG2   sing N N 95  
GLN CG    HG3   sing N N 96  
GLN CD    OE1   doub N N 97  
GLN CD    NE2   sing N N 98  
GLN NE2   HE21  sing N N 99  
GLN NE2   HE22  sing N N 100 
GLN OXT   HXT   sing N N 101 
GLU N     CA    sing N N 102 
GLU N     H     sing N N 103 
GLU N     H2    sing N N 104 
GLU CA    C     sing N N 105 
GLU CA    CB    sing N N 106 
GLU CA    HA    sing N N 107 
GLU C     O     doub N N 108 
GLU C     OXT   sing N N 109 
GLU CB    CG    sing N N 110 
GLU CB    HB2   sing N N 111 
GLU CB    HB3   sing N N 112 
GLU CG    CD    sing N N 113 
GLU CG    HG2   sing N N 114 
GLU CG    HG3   sing N N 115 
GLU CD    OE1   doub N N 116 
GLU CD    OE2   sing N N 117 
GLU OE2   HE2   sing N N 118 
GLU OXT   HXT   sing N N 119 
GLY N     CA    sing N N 120 
GLY N     H     sing N N 121 
GLY N     H2    sing N N 122 
GLY CA    C     sing N N 123 
GLY CA    HA2   sing N N 124 
GLY CA    HA3   sing N N 125 
GLY C     O     doub N N 126 
GLY C     OXT   sing N N 127 
GLY OXT   HXT   sing N N 128 
HIS N     CA    sing N N 129 
HIS N     H     sing N N 130 
HIS N     H2    sing N N 131 
HIS CA    C     sing N N 132 
HIS CA    CB    sing N N 133 
HIS CA    HA    sing N N 134 
HIS C     O     doub N N 135 
HIS C     OXT   sing N N 136 
HIS CB    CG    sing N N 137 
HIS CB    HB2   sing N N 138 
HIS CB    HB3   sing N N 139 
HIS CG    ND1   sing Y N 140 
HIS CG    CD2   doub Y N 141 
HIS ND1   CE1   doub Y N 142 
HIS ND1   HD1   sing N N 143 
HIS CD2   NE2   sing Y N 144 
HIS CD2   HD2   sing N N 145 
HIS CE1   NE2   sing Y N 146 
HIS CE1   HE1   sing N N 147 
HIS NE2   HE2   sing N N 148 
HIS OXT   HXT   sing N N 149 
HUF O33   C19   doub N N 150 
HUF C19   N29   sing N N 151 
HUF O37   C26   sing N N 152 
HUF C24   N32   sing N N 153 
HUF C24   C25   sing N N 154 
HUF N29   C15   sing N N 155 
HUF N29   C20   sing N N 156 
HUF N32   C21   sing N N 157 
HUF N32   C14   sing N N 158 
HUF C15   C14   doub Y N 159 
HUF C15   C16   sing Y N 160 
HUF C20   C21   doub N N 161 
HUF C20   C23   sing N N 162 
HUF C21   N30   sing N N 163 
HUF C14   C13   sing Y N 164 
HUF C16   C17   doub Y N 165 
HUF N30   C22   sing N N 166 
HUF C13   C12   doub Y N 167 
HUF C23   N31   sing N N 168 
HUF C23   O35   doub N N 169 
HUF C22   N31   sing N N 170 
HUF C22   O34   doub N N 171 
HUF C17   C12   sing Y N 172 
HUF C17   C18   sing N N 173 
HUF C12   C11   sing N N 174 
HUF C26   C25   sing N N 175 
HUF C26   C27   sing N N 176 
HUF C25   O36   sing N N 177 
HUF O2B   PB    doub N N 178 
HUF C28   C27   sing N N 179 
HUF C28   O1B   sing N N 180 
HUF C27   O38   sing N N 181 
HUF PB    O3A   sing N N 182 
HUF PB    O1B   sing N N 183 
HUF PB    O3B   sing N N 184 
HUF O3A   PA    sing N N 185 
HUF O2A   PA    doub N N 186 
HUF PA    O1A   sing N N 187 
HUF PA    "O5'" sing N N 188 
HUF "C5'" "O5'" sing N N 189 
HUF "C5'" "C4'" sing N N 190 
HUF N7    C8    doub Y N 191 
HUF N7    C5    sing Y N 192 
HUF C8    N9    sing Y N 193 
HUF N6    C6    sing N N 194 
HUF "O4'" "C4'" sing N N 195 
HUF "O4'" "C1'" sing N N 196 
HUF C5    C6    doub Y N 197 
HUF C5    C4    sing Y N 198 
HUF "C4'" "C3'" sing N N 199 
HUF N9    "C1'" sing N N 200 
HUF N9    C4    sing Y N 201 
HUF C6    N1    sing Y N 202 
HUF "C2'" "C3'" sing N N 203 
HUF "C2'" "C1'" sing N N 204 
HUF "C2'" "O2'" sing N N 205 
HUF "C3'" "O3'" sing N N 206 
HUF C4    N3    doub Y N 207 
HUF N1    C2    doub Y N 208 
HUF N3    C2    sing Y N 209 
HUF O1A   H1    sing N N 210 
HUF O3B   H2    sing N N 211 
HUF "C5'" H3    sing N N 212 
HUF "C5'" H4    sing N N 213 
HUF "C4'" H5    sing N N 214 
HUF "C3'" H6    sing N N 215 
HUF "O3'" H7    sing N N 216 
HUF "C2'" H8    sing N N 217 
HUF "O2'" H9    sing N N 218 
HUF "C1'" H10   sing N N 219 
HUF C8    H11   sing N N 220 
HUF C2    H12   sing N N 221 
HUF N6    H13   sing N N 222 
HUF N6    H14   sing N N 223 
HUF C11   H15   sing N N 224 
HUF C11   H16   sing N N 225 
HUF C11   H17   sing N N 226 
HUF C13   H18   sing N N 227 
HUF C16   H19   sing N N 228 
HUF C18   H20   sing N N 229 
HUF C18   H21   sing N N 230 
HUF C18   H22   sing N N 231 
HUF C19   H23   sing N N 232 
HUF C24   H24   sing N N 233 
HUF C24   H25   sing N N 234 
HUF C25   H26   sing N N 235 
HUF C26   H27   sing N N 236 
HUF C27   H28   sing N N 237 
HUF C28   H29   sing N N 238 
HUF C28   H30   sing N N 239 
HUF N30   H31   sing N N 240 
HUF N31   H32   sing N N 241 
HUF O36   H33   sing N N 242 
HUF O37   H34   sing N N 243 
HUF O38   H35   sing N N 244 
ILE N     CA    sing N N 245 
ILE N     H     sing N N 246 
ILE N     H2    sing N N 247 
ILE CA    C     sing N N 248 
ILE CA    CB    sing N N 249 
ILE CA    HA    sing N N 250 
ILE C     O     doub N N 251 
ILE C     OXT   sing N N 252 
ILE CB    CG1   sing N N 253 
ILE CB    CG2   sing N N 254 
ILE CB    HB    sing N N 255 
ILE CG1   CD1   sing N N 256 
ILE CG1   HG12  sing N N 257 
ILE CG1   HG13  sing N N 258 
ILE CG2   HG21  sing N N 259 
ILE CG2   HG22  sing N N 260 
ILE CG2   HG23  sing N N 261 
ILE CD1   HD11  sing N N 262 
ILE CD1   HD12  sing N N 263 
ILE CD1   HD13  sing N N 264 
ILE OXT   HXT   sing N N 265 
LEU N     CA    sing N N 266 
LEU N     H     sing N N 267 
LEU N     H2    sing N N 268 
LEU CA    C     sing N N 269 
LEU CA    CB    sing N N 270 
LEU CA    HA    sing N N 271 
LEU C     O     doub N N 272 
LEU C     OXT   sing N N 273 
LEU CB    CG    sing N N 274 
LEU CB    HB2   sing N N 275 
LEU CB    HB3   sing N N 276 
LEU CG    CD1   sing N N 277 
LEU CG    CD2   sing N N 278 
LEU CG    HG    sing N N 279 
LEU CD1   HD11  sing N N 280 
LEU CD1   HD12  sing N N 281 
LEU CD1   HD13  sing N N 282 
LEU CD2   HD21  sing N N 283 
LEU CD2   HD22  sing N N 284 
LEU CD2   HD23  sing N N 285 
LEU OXT   HXT   sing N N 286 
LYS N     CA    sing N N 287 
LYS N     H     sing N N 288 
LYS N     H2    sing N N 289 
LYS CA    C     sing N N 290 
LYS CA    CB    sing N N 291 
LYS CA    HA    sing N N 292 
LYS C     O     doub N N 293 
LYS C     OXT   sing N N 294 
LYS CB    CG    sing N N 295 
LYS CB    HB2   sing N N 296 
LYS CB    HB3   sing N N 297 
LYS CG    CD    sing N N 298 
LYS CG    HG2   sing N N 299 
LYS CG    HG3   sing N N 300 
LYS CD    CE    sing N N 301 
LYS CD    HD2   sing N N 302 
LYS CD    HD3   sing N N 303 
LYS CE    NZ    sing N N 304 
LYS CE    HE2   sing N N 305 
LYS CE    HE3   sing N N 306 
LYS NZ    HZ1   sing N N 307 
LYS NZ    HZ2   sing N N 308 
LYS NZ    HZ3   sing N N 309 
LYS OXT   HXT   sing N N 310 
MET N     CA    sing N N 311 
MET N     H     sing N N 312 
MET N     H2    sing N N 313 
MET CA    C     sing N N 314 
MET CA    CB    sing N N 315 
MET CA    HA    sing N N 316 
MET C     O     doub N N 317 
MET C     OXT   sing N N 318 
MET CB    CG    sing N N 319 
MET CB    HB2   sing N N 320 
MET CB    HB3   sing N N 321 
MET CG    SD    sing N N 322 
MET CG    HG2   sing N N 323 
MET CG    HG3   sing N N 324 
MET SD    CE    sing N N 325 
MET CE    HE1   sing N N 326 
MET CE    HE2   sing N N 327 
MET CE    HE3   sing N N 328 
MET OXT   HXT   sing N N 329 
PHE N     CA    sing N N 330 
PHE N     H     sing N N 331 
PHE N     H2    sing N N 332 
PHE CA    C     sing N N 333 
PHE CA    CB    sing N N 334 
PHE CA    HA    sing N N 335 
PHE C     O     doub N N 336 
PHE C     OXT   sing N N 337 
PHE CB    CG    sing N N 338 
PHE CB    HB2   sing N N 339 
PHE CB    HB3   sing N N 340 
PHE CG    CD1   doub Y N 341 
PHE CG    CD2   sing Y N 342 
PHE CD1   CE1   sing Y N 343 
PHE CD1   HD1   sing N N 344 
PHE CD2   CE2   doub Y N 345 
PHE CD2   HD2   sing N N 346 
PHE CE1   CZ    doub Y N 347 
PHE CE1   HE1   sing N N 348 
PHE CE2   CZ    sing Y N 349 
PHE CE2   HE2   sing N N 350 
PHE CZ    HZ    sing N N 351 
PHE OXT   HXT   sing N N 352 
PRO N     CA    sing N N 353 
PRO N     CD    sing N N 354 
PRO N     H     sing N N 355 
PRO CA    C     sing N N 356 
PRO CA    CB    sing N N 357 
PRO CA    HA    sing N N 358 
PRO C     O     doub N N 359 
PRO C     OXT   sing N N 360 
PRO CB    CG    sing N N 361 
PRO CB    HB2   sing N N 362 
PRO CB    HB3   sing N N 363 
PRO CG    CD    sing N N 364 
PRO CG    HG2   sing N N 365 
PRO CG    HG3   sing N N 366 
PRO CD    HD2   sing N N 367 
PRO CD    HD3   sing N N 368 
PRO OXT   HXT   sing N N 369 
SER N     CA    sing N N 370 
SER N     H     sing N N 371 
SER N     H2    sing N N 372 
SER CA    C     sing N N 373 
SER CA    CB    sing N N 374 
SER CA    HA    sing N N 375 
SER C     O     doub N N 376 
SER C     OXT   sing N N 377 
SER CB    OG    sing N N 378 
SER CB    HB2   sing N N 379 
SER CB    HB3   sing N N 380 
SER OG    HG    sing N N 381 
SER OXT   HXT   sing N N 382 
THR N     CA    sing N N 383 
THR N     H     sing N N 384 
THR N     H2    sing N N 385 
THR CA    C     sing N N 386 
THR CA    CB    sing N N 387 
THR CA    HA    sing N N 388 
THR C     O     doub N N 389 
THR C     OXT   sing N N 390 
THR CB    OG1   sing N N 391 
THR CB    CG2   sing N N 392 
THR CB    HB    sing N N 393 
THR OG1   HG1   sing N N 394 
THR CG2   HG21  sing N N 395 
THR CG2   HG22  sing N N 396 
THR CG2   HG23  sing N N 397 
THR OXT   HXT   sing N N 398 
TRP N     CA    sing N N 399 
TRP N     H     sing N N 400 
TRP N     H2    sing N N 401 
TRP CA    C     sing N N 402 
TRP CA    CB    sing N N 403 
TRP CA    HA    sing N N 404 
TRP C     O     doub N N 405 
TRP C     OXT   sing N N 406 
TRP CB    CG    sing N N 407 
TRP CB    HB2   sing N N 408 
TRP CB    HB3   sing N N 409 
TRP CG    CD1   doub Y N 410 
TRP CG    CD2   sing Y N 411 
TRP CD1   NE1   sing Y N 412 
TRP CD1   HD1   sing N N 413 
TRP CD2   CE2   doub Y N 414 
TRP CD2   CE3   sing Y N 415 
TRP NE1   CE2   sing Y N 416 
TRP NE1   HE1   sing N N 417 
TRP CE2   CZ2   sing Y N 418 
TRP CE3   CZ3   doub Y N 419 
TRP CE3   HE3   sing N N 420 
TRP CZ2   CH2   doub Y N 421 
TRP CZ2   HZ2   sing N N 422 
TRP CZ3   CH2   sing Y N 423 
TRP CZ3   HZ3   sing N N 424 
TRP CH2   HH2   sing N N 425 
TRP OXT   HXT   sing N N 426 
TYR N     CA    sing N N 427 
TYR N     H     sing N N 428 
TYR N     H2    sing N N 429 
TYR CA    C     sing N N 430 
TYR CA    CB    sing N N 431 
TYR CA    HA    sing N N 432 
TYR C     O     doub N N 433 
TYR C     OXT   sing N N 434 
TYR CB    CG    sing N N 435 
TYR CB    HB2   sing N N 436 
TYR CB    HB3   sing N N 437 
TYR CG    CD1   doub Y N 438 
TYR CG    CD2   sing Y N 439 
TYR CD1   CE1   sing Y N 440 
TYR CD1   HD1   sing N N 441 
TYR CD2   CE2   doub Y N 442 
TYR CD2   HD2   sing N N 443 
TYR CE1   CZ    doub Y N 444 
TYR CE1   HE1   sing N N 445 
TYR CE2   CZ    sing Y N 446 
TYR CE2   HE2   sing N N 447 
TYR CZ    OH    sing N N 448 
TYR OH    HH    sing N N 449 
TYR OXT   HXT   sing N N 450 
VAL N     CA    sing N N 451 
VAL N     H     sing N N 452 
VAL N     H2    sing N N 453 
VAL CA    C     sing N N 454 
VAL CA    CB    sing N N 455 
VAL CA    HA    sing N N 456 
VAL C     O     doub N N 457 
VAL C     OXT   sing N N 458 
VAL CB    CG1   sing N N 459 
VAL CB    CG2   sing N N 460 
VAL CB    HB    sing N N 461 
VAL CG1   HG11  sing N N 462 
VAL CG1   HG12  sing N N 463 
VAL CG1   HG13  sing N N 464 
VAL CG2   HG21  sing N N 465 
VAL CG2   HG22  sing N N 466 
VAL CG2   HG23  sing N N 467 
VAL OXT   HXT   sing N N 468 
# 
_pdbx_audit_support.funding_organization   'Italian Association for Cancer Research' 
_pdbx_audit_support.country                Italy 
_pdbx_audit_support.grant_number           IG19808 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2v1d 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8UNI 
_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]   0.008490 
_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]   0.005613 
_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]   0.004270 
_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     . PRO A 1 190 ? -16.210 37.869  98.429  1.00 167.41 ?  171 PRO A N     1 
ATOM   2    C CA    . PRO A 1 190 ? -16.682 37.850  99.823  1.00 167.12 ?  171 PRO A CA    1 
ATOM   3    C C     . PRO A 1 190 ? -18.022 38.597  100.069 1.00 169.92 ?  171 PRO A C     1 
ATOM   4    O O     . PRO A 1 190 ? -18.290 39.648  99.463  1.00 165.32 ?  171 PRO A O     1 
ATOM   5    C CB    . PRO A 1 190 ? -15.522 38.516  100.585 1.00 156.17 ?  171 PRO A CB    1 
ATOM   6    C CG    . PRO A 1 190 ? -14.302 38.176  99.761  1.00 153.98 ?  171 PRO A CG    1 
ATOM   7    C CD    . PRO A 1 190 ? -14.772 38.191  98.326  1.00 159.49 ?  171 PRO A CD    1 
ATOM   8    N N     . SER A 1 191 ? -18.854 38.026  100.951 1.00 172.59 ?  172 SER A N     1 
ATOM   9    C CA    . SER A 1 191 ? -20.122 38.610  101.385 1.00 168.94 ?  172 SER A CA    1 
ATOM   10   C C     . SER A 1 191 ? -20.195 38.586  102.912 1.00 163.88 ?  172 SER A C     1 
ATOM   11   O O     . SER A 1 191 ? -19.453 37.857  103.583 1.00 161.95 ?  172 SER A O     1 
ATOM   12   C CB    . SER A 1 191 ? -21.332 37.871  100.779 1.00 167.80 ?  172 SER A CB    1 
ATOM   13   O OG    . SER A 1 191 ? -21.423 36.532  101.248 1.00 166.11 ?  172 SER A OG    1 
ATOM   14   N N     . GLY A 1 192 ? -21.107 39.390  103.462 1.00 157.37 ?  173 GLY A N     1 
ATOM   15   C CA    . GLY A 1 192 ? -21.231 39.521  104.905 1.00 152.44 ?  173 GLY A CA    1 
ATOM   16   C C     . GLY A 1 192 ? -20.373 40.651  105.443 1.00 144.82 ?  173 GLY A C     1 
ATOM   17   O O     . GLY A 1 192 ? -19.971 41.567  104.715 1.00 139.78 ?  173 GLY A O     1 
ATOM   18   N N     . VAL A 1 193 ? -20.088 40.581  106.751 1.00 145.88 ?  174 VAL A N     1 
ATOM   19   C CA    . VAL A 1 193 ? -19.216 41.583  107.368 1.00 138.33 ?  174 VAL A CA    1 
ATOM   20   C C     . VAL A 1 193 ? -17.830 41.556  106.727 1.00 136.71 ?  174 VAL A C     1 
ATOM   21   O O     . VAL A 1 193 ? -17.243 42.609  106.460 1.00 133.97 ?  174 VAL A O     1 
ATOM   22   C CB    . VAL A 1 193 ? -19.142 41.402  108.900 1.00 135.35 ?  174 VAL A CB    1 
ATOM   23   C CG1   . VAL A 1 193 ? -20.457 41.758  109.557 1.00 128.83 ?  174 VAL A CG1   1 
ATOM   24   C CG2   . VAL A 1 193 ? -18.772 39.968  109.250 1.00 142.92 ?  174 VAL A CG2   1 
ATOM   25   N N     . GLU A 1 194 ? -17.288 40.361  106.454 1.00 137.53 ?  175 GLU A N     1 
ATOM   26   C CA    . GLU A 1 194 ? -15.994 40.291  105.774 1.00 136.85 ?  175 GLU A CA    1 
ATOM   27   C C     . GLU A 1 194 ? -16.047 40.821  104.341 1.00 137.74 ?  175 GLU A C     1 
ATOM   28   O O     . GLU A 1 194 ? -14.990 41.114  103.759 1.00 134.09 ?  175 GLU A O     1 
ATOM   29   C CB    . GLU A 1 194 ? -15.466 38.862  105.737 1.00 139.79 ?  175 GLU A CB    1 
ATOM   30   C CG    . GLU A 1 194 ? -15.094 38.250  107.052 1.00 136.98 ?  175 GLU A CG    1 
ATOM   31   C CD    . GLU A 1 194 ? -14.554 36.828  106.868 1.00 149.92 ?  175 GLU A CD    1 
ATOM   32   O OE1   . GLU A 1 194 ? -14.428 36.357  105.704 1.00 149.91 ?  175 GLU A OE1   1 
ATOM   33   O OE2   . GLU A 1 194 ? -14.264 36.169  107.890 1.00 157.65 ?  175 GLU A OE2   1 
ATOM   34   N N     . GLY A 1 195 ? -17.237 40.910  103.743 1.00 137.59 ?  176 GLY A N     1 
ATOM   35   C CA    . GLY A 1 195 ? -17.345 41.594  102.467 1.00 135.86 ?  176 GLY A CA    1 
ATOM   36   C C     . GLY A 1 195 ? -17.086 43.082  102.611 1.00 126.42 ?  176 GLY A C     1 
ATOM   37   O O     . GLY A 1 195 ? -16.275 43.663  101.878 1.00 121.25 ?  176 GLY A O     1 
ATOM   38   N N     . ALA A 1 196 ? -17.752 43.711  103.586 1.00 122.57 ?  177 ALA A N     1 
ATOM   39   C CA    . ALA A 1 196 ? -17.596 45.145  103.803 1.00 115.66 ?  177 ALA A CA    1 
ATOM   40   C C     . ALA A 1 196 ? -16.137 45.527  104.048 1.00 112.14 ?  177 ALA A C     1 
ATOM   41   O O     . ALA A 1 196 ? -15.688 46.589  103.607 1.00 113.72 ?  177 ALA A O     1 
ATOM   42   C CB    . ALA A 1 196 ? -18.476 45.591  104.967 1.00 112.02 ?  177 ALA A CB    1 
ATOM   43   N N     . ALA A 1 197 ? -15.378 44.676  104.742 1.00 112.48 ?  178 ALA A N     1 
ATOM   44   C CA    . ALA A 1 197 ? -13.969 44.981  104.990 1.00 108.81 ?  178 ALA A CA    1 
ATOM   45   C C     . ALA A 1 197 ? -13.178 45.014  103.694 1.00 110.39 ?  178 ALA A C     1 
ATOM   46   O O     . ALA A 1 197 ? -12.259 45.828  103.536 1.00 106.68 ?  178 ALA A O     1 
ATOM   47   C CB    . ALA A 1 197 ? -13.360 43.958  105.948 1.00 114.85 ?  178 ALA A CB    1 
ATOM   48   N N     . PHE A 1 198 ? -13.522 44.131  102.755 1.00 116.05 ?  179 PHE A N     1 
ATOM   49   C CA    . PHE A 1 198 ? -12.840 44.120  101.467 1.00 119.15 ?  179 PHE A CA    1 
ATOM   50   C C     . PHE A 1 198 ? -13.310 45.272  100.567 1.00 115.83 ?  179 PHE A C     1 
ATOM   51   O O     . PHE A 1 198 ? -12.484 46.001  99.993  1.00 110.20 ?  179 PHE A O     1 
ATOM   52   C CB    . PHE A 1 198 ? -13.033 42.761  100.791 1.00 122.49 ?  179 PHE A CB    1 
ATOM   53   C CG    . PHE A 1 198 ? -12.747 42.796  99.327  1.00 125.20 ?  179 PHE A CG    1 
ATOM   54   C CD1   . PHE A 1 198 ? -11.460 43.084  98.868  1.00 124.51 ?  179 PHE A CD1   1 
ATOM   55   C CD2   . PHE A 1 198 ? -13.767 42.580  98.407  1.00 118.96 ?  179 PHE A CD2   1 
ATOM   56   C CE1   . PHE A 1 198 ? -11.193 43.151  97.519  1.00 122.17 ?  179 PHE A CE1   1 
ATOM   57   C CE2   . PHE A 1 198 ? -13.511 42.642  97.063  1.00 114.71 ?  179 PHE A CE2   1 
ATOM   58   C CZ    . PHE A 1 198 ? -12.219 42.929  96.611  1.00 117.80 ?  179 PHE A CZ    1 
ATOM   59   N N     . GLN A 1 199 ? -14.633 45.459  100.433 1.00 110.56 ?  180 GLN A N     1 
ATOM   60   C CA    . GLN A 1 199 ? -15.175 46.628  99.740  1.00 106.60 ?  180 GLN A CA    1 
ATOM   61   C C     . GLN A 1 199 ? -14.594 47.950  100.261 1.00 108.45 ?  180 GLN A C     1 
ATOM   62   O O     . GLN A 1 199 ? -14.639 48.971  99.558  1.00 105.85 ?  180 GLN A O     1 
ATOM   63   C CB    . GLN A 1 199 ? -16.703 46.608  99.861  1.00 102.63 ?  180 GLN A CB    1 
ATOM   64   C CG    . GLN A 1 199 ? -17.439 47.749  99.160  1.00 110.24 ?  180 GLN A CG    1 
ATOM   65   C CD    . GLN A 1 199 ? -17.226 47.804  97.642  1.00 120.76 ?  180 GLN A CD    1 
ATOM   66   O OE1   . GLN A 1 199 ? -17.105 46.768  96.972  1.00 123.07 ?  180 GLN A OE1   1 
ATOM   67   N NE2   . GLN A 1 199 ? -17.191 49.028  97.093  1.00 115.52 ?  180 GLN A NE2   1 
ATOM   68   N N     . SER A 1 200 ? -14.034 47.952  101.470 1.00 110.69 ?  181 SER A N     1 
ATOM   69   C CA    . SER A 1 200 ? -13.389 49.127  102.042 1.00 108.39 ?  181 SER A CA    1 
ATOM   70   C C     . SER A 1 200 ? -11.869 49.016  102.046 1.00 103.81 ?  181 SER A C     1 
ATOM   71   O O     . SER A 1 200 ? -11.204 49.793  102.742 1.00 104.60 ?  181 SER A O     1 
ATOM   72   C CB    . SER A 1 200 ? -13.907 49.387  103.464 1.00 104.56 ?  181 SER A CB    1 
ATOM   73   O OG    . SER A 1 200 ? -15.303 49.660  103.457 1.00 101.80 ?  181 SER A OG    1 
ATOM   74   N N     . ARG A 1 201 ? -11.307 48.073  101.290 1.00 99.05  ?  182 ARG A N     1 
ATOM   75   C CA    . ARG A 1 201 ? -9.866  48.019  101.057 1.00 100.92 ?  182 ARG A CA    1 
ATOM   76   C C     . ARG A 1 201 ? -9.099  47.739  102.356 1.00 102.15 ?  182 ARG A C     1 
ATOM   77   O O     . ARG A 1 201 ? -8.056  48.345  102.625 1.00 102.75 ?  182 ARG A O     1 
ATOM   78   C CB    . ARG A 1 201 ? -9.383  49.312  100.376 1.00 99.50  ?  182 ARG A CB    1 
ATOM   79   C CG    . ARG A 1 201 ? -10.197 49.640  99.115  1.00 93.74  ?  182 ARG A CG    1 
ATOM   80   C CD    . ARG A 1 201 ? -10.223 51.095  98.682  1.00 91.97  ?  182 ARG A CD    1 
ATOM   81   N NE    . ARG A 1 201 ? -10.812 52.062  99.609  1.00 100.21 ?  182 ARG A NE    1 
ATOM   82   C CZ    . ARG A 1 201 ? -12.119 52.290  99.764  1.00 98.97  ?  182 ARG A CZ    1 
ATOM   83   N NH1   . ARG A 1 201 ? -13.014 51.584  99.077  1.00 96.05  ?  182 ARG A NH1   1 
ATOM   84   N NH2   . ARG A 1 201 ? -12.530 53.221  100.632 1.00 95.47  ?  182 ARG A NH2   1 
ATOM   85   N N     . LEU A 1 202 ? -9.610  46.781  103.149 1.00 105.04 ?  183 LEU A N     1 
ATOM   86   C CA    . LEU A 1 202 ? -9.202  46.528  104.552 1.00 104.72 ?  183 LEU A CA    1 
ATOM   87   C C     . LEU A 1 202 ? -9.276  45.051  104.927 1.00 101.97 ?  183 LEU A C     1 
ATOM   88   O O     . LEU A 1 202 ? -10.345 44.429  104.768 1.00 99.97  ?  183 LEU A O     1 
ATOM   89   C CB    . LEU A 1 202 ? -10.105 47.328  105.496 1.00 106.55 ?  183 LEU A CB    1 
ATOM   90   C CG    . LEU A 1 202 ? -10.102 48.849  105.533 1.00 102.36 ?  183 LEU A CG    1 
ATOM   91   C CD1   . LEU A 1 202 ? -11.218 49.345  106.437 1.00 94.31  ?  183 LEU A CD1   1 
ATOM   92   C CD2   . LEU A 1 202 ? -8.754  49.326  106.058 1.00 101.91 ?  183 LEU A CD2   1 
ATOM   93   N N     . PRO A 1 203 ? -8.202  44.472  105.471 1.00 104.45 ?  184 PRO A N     1 
ATOM   94   C CA    . PRO A 1 203 ? -8.260  43.057  105.890 1.00 108.30 ?  184 PRO A CA    1 
ATOM   95   C C     . PRO A 1 203 ? -9.210  42.890  107.067 1.00 114.11 ?  184 PRO A C     1 
ATOM   96   O O     . PRO A 1 203 ? -9.033  43.512  108.116 1.00 118.00 ?  184 PRO A O     1 
ATOM   97   C CB    . PRO A 1 203 ? -6.806  42.728  106.268 1.00 103.11 ?  184 PRO A CB    1 
ATOM   98   C CG    . PRO A 1 203 ? -6.196  44.032  106.609 1.00 102.91 ?  184 PRO A CG    1 
ATOM   99   C CD    . PRO A 1 203 ? -6.881  45.077  105.738 1.00 103.48 ?  184 PRO A CD    1 
ATOM   100  N N     . HIS A 1 204 ? -10.240 42.058  106.877 1.00 118.13 ?  185 HIS A N     1 
ATOM   101  C CA    . HIS A 1 204 ? -11.220 41.789  107.932 1.00 119.53 ?  185 HIS A CA    1 
ATOM   102  C C     . HIS A 1 204 ? -10.601 41.170  109.192 1.00 122.64 ?  185 HIS A C     1 
ATOM   103  O O     . HIS A 1 204 ? -11.135 41.364  110.292 1.00 118.87 ?  185 HIS A O     1 
ATOM   104  C CB    . HIS A 1 204 ? -12.305 40.866  107.372 1.00 121.38 ?  185 HIS A CB    1 
ATOM   105  C CG    . HIS A 1 204 ? -11.762 39.549  106.923 1.00 127.69 ?  185 HIS A CG    1 
ATOM   106  N ND1   . HIS A 1 204 ? -11.518 38.509  107.793 1.00 127.48 ?  185 HIS A ND1   1 
ATOM   107  C CD2   . HIS A 1 204 ? -11.336 39.130  105.708 1.00 134.70 ?  185 HIS A CD2   1 
ATOM   108  C CE1   . HIS A 1 204 ? -10.999 37.493  107.128 1.00 128.66 ?  185 HIS A CE1   1 
ATOM   109  N NE2   . HIS A 1 204 ? -10.877 37.843  105.861 1.00 134.45 ?  185 HIS A NE2   1 
ATOM   110  N N     . ASP A 1 205 ? -9.485  40.441  109.066 1.00 123.91 ?  186 ASP A N     1 
ATOM   111  C CA    . ASP A 1 205 ? -8.936  39.628  110.150 1.00 119.27 ?  186 ASP A CA    1 
ATOM   112  C C     . ASP A 1 205 ? -7.615  40.170  110.694 1.00 115.13 ?  186 ASP A C     1 
ATOM   113  O O     . ASP A 1 205 ? -6.775  39.401  111.172 1.00 114.38 ?  186 ASP A O     1 
ATOM   114  C CB    . ASP A 1 205 ? -8.742  38.187  109.679 1.00 125.59 ?  186 ASP A CB    1 
ATOM   115  C CG    . ASP A 1 205 ? -7.771  38.071  108.492 1.00 127.51 ?  186 ASP A CG    1 
ATOM   116  O OD1   . ASP A 1 205 ? -7.439  39.093  107.846 1.00 125.58 ?  186 ASP A OD1   1 
ATOM   117  O OD2   . ASP A 1 205 ? -7.321  36.940  108.218 1.00 130.58 ?  186 ASP A OD2   1 
ATOM   118  N N     . ARG A 1 206 ? -7.411  41.482  110.635 1.00 114.39 ?  187 ARG A N     1 
ATOM   119  C CA    . ARG A 1 206 ? -6.138  42.048  111.063 1.00 118.27 ?  187 ARG A CA    1 
ATOM   120  C C     . ARG A 1 206 ? -6.280  43.565  111.141 1.00 114.45 ?  187 ARG A C     1 
ATOM   121  O O     . ARG A 1 206 ? -7.112  44.161  110.448 1.00 112.48 ?  187 ARG A O     1 
ATOM   122  C CB    . ARG A 1 206 ? -5.011  41.640  110.097 1.00 120.35 ?  187 ARG A CB    1 
ATOM   123  C CG    . ARG A 1 206 ? -3.574  41.896  110.570 1.00 126.64 ?  187 ARG A CG    1 
ATOM   124  C CD    . ARG A 1 206 ? -2.610  41.442  109.468 1.00 130.20 ?  187 ARG A CD    1 
ATOM   125  N NE    . ARG A 1 206 ? -2.675  42.340  108.317 1.00 134.48 ?  187 ARG A NE    1 
ATOM   126  C CZ    . ARG A 1 206 ? -3.193  42.014  107.135 1.00 130.84 ?  187 ARG A CZ    1 
ATOM   127  N NH1   . ARG A 1 206 ? -3.728  40.808  106.952 1.00 128.76 ?  187 ARG A NH1   1 
ATOM   128  N NH2   . ARG A 1 206 ? -3.209  42.912  106.150 1.00 123.65 ?  187 ARG A NH2   1 
ATOM   129  N N     . MET A 1 207 ? -5.482  44.181  112.005 1.00 108.97 ?  188 MET A N     1 
ATOM   130  C CA    . MET A 1 207 ? -5.502  45.628  112.134 1.00 105.86 ?  188 MET A CA    1 
ATOM   131  C C     . MET A 1 207 ? -4.463  46.235  111.194 1.00 105.99 ?  188 MET A C     1 
ATOM   132  O O     . MET A 1 207 ? -3.326  45.741  111.117 1.00 100.66 ?  188 MET A O     1 
ATOM   133  C CB    . MET A 1 207 ? -5.226  46.054  113.585 1.00 112.74 ?  188 MET A CB    1 
ATOM   134  C CG    . MET A 1 207 ? -6.291  45.669  114.659 1.00 109.05 ?  188 MET A CG    1 
ATOM   135  S SD    . MET A 1 207 ? -5.888  46.115  116.402 1.00 102.92 ?  188 MET A SD    1 
ATOM   136  C CE    . MET A 1 207 ? -5.827  47.909  116.352 1.00 104.95 ?  188 MET A CE    1 
ATOM   137  N N     . THR A 1 208 ? -4.873  47.299  110.468 1.00 106.37 ?  189 THR A N     1 
ATOM   138  C CA    . THR A 1 208 ? -4.002  48.036  109.550 1.00 101.33 ?  189 THR A CA    1 
ATOM   139  C C     . THR A 1 208 ? -3.042  48.910  110.337 1.00 100.40 ?  189 THR A C     1 
ATOM   140  O O     . THR A 1 208 ? -3.236  49.173  111.524 1.00 105.15 ?  189 THR A O     1 
ATOM   141  C CB    . THR A 1 208 ? -4.780  48.931  108.556 1.00 101.37 ?  189 THR A CB    1 
ATOM   142  O OG1   . THR A 1 208 ? -5.338  50.078  109.209 1.00 101.79 ?  189 THR A OG1   1 
ATOM   143  C CG2   . THR A 1 208 ? -5.900  48.171  107.883 1.00 106.68 ?  189 THR A CG2   1 
ATOM   144  N N     . SER A 1 209 ? -1.995  49.370  109.659 1.00 100.57 ?  190 SER A N     1 
ATOM   145  C CA    . SER A 1 209 ? -1.023  50.223  110.332 1.00 101.07 ?  190 SER A CA    1 
ATOM   146  C C     . SER A 1 209 ? -1.638  51.552  110.771 1.00 103.89 ?  190 SER A C     1 
ATOM   147  O O     . SER A 1 209 ? -1.133  52.194  111.703 1.00 105.35 ?  190 SER A O     1 
ATOM   148  C CB    . SER A 1 209 ? 0.179   50.443  109.415 1.00 108.22 ?  190 SER A CB    1 
ATOM   149  O OG    . SER A 1 209 ? 1.107   51.343  109.981 1.00 107.45 ?  190 SER A OG    1 
ATOM   150  N N     . GLN A 1 210 ? -2.736  51.973  110.136 1.00 107.31 ?  191 GLN A N     1 
ATOM   151  C CA    . GLN A 1 210 ? -3.394  53.198  110.576 1.00 107.70 ?  191 GLN A CA    1 
ATOM   152  C C     . GLN A 1 210 ? -4.240  52.956  111.823 1.00 107.07 ?  191 GLN A C     1 
ATOM   153  O O     . GLN A 1 210 ? -4.215  53.762  112.763 1.00 110.53 ?  191 GLN A O     1 
ATOM   154  C CB    . GLN A 1 210 ? -4.235  53.792  109.444 1.00 112.87 ?  191 GLN A CB    1 
ATOM   155  C CG    . GLN A 1 210 ? -4.845  55.122  109.844 1.00 118.54 ?  191 GLN A CG    1 
ATOM   156  C CD    . GLN A 1 210 ? -3.919  56.299  109.517 1.00 131.23 ?  191 GLN A CD    1 
ATOM   157  O OE1   . GLN A 1 210 ? -3.033  56.192  108.656 1.00 140.46 ?  191 GLN A OE1   1 
ATOM   158  N NE2   . GLN A 1 210 ? -4.081  57.407  110.249 1.00 123.52 ?  191 GLN A NE2   1 
ATOM   159  N N     . GLU A 1 211 ? -4.973  51.842  111.862 1.00 106.31 ?  192 GLU A N     1 
ATOM   160  C CA    . GLU A 1 211 ? -5.688  51.470  113.081 1.00 104.50 ?  192 GLU A CA    1 
ATOM   161  C C     . GLU A 1 211 ? -4.747  51.363  114.277 1.00 102.62 ?  192 GLU A C     1 
ATOM   162  O O     . GLU A 1 211 ? -5.143  51.675  115.406 1.00 103.66 ?  192 GLU A O     1 
ATOM   163  C CB    . GLU A 1 211 ? -6.432  50.156  112.853 1.00 99.93  ?  192 GLU A CB    1 
ATOM   164  C CG    . GLU A 1 211 ? -7.570  50.331  111.879 1.00 103.86 ?  192 GLU A CG    1 
ATOM   165  C CD    . GLU A 1 211 ? -8.008  49.048  111.173 1.00 109.26 ?  192 GLU A CD    1 
ATOM   166  O OE1   . GLU A 1 211 ? -7.227  48.071  111.016 1.00 106.04 ?  192 GLU A OE1   1 
ATOM   167  O OE2   . GLU A 1 211 ? -9.163  49.042  110.732 1.00 107.19 ?  192 GLU A OE2   1 
ATOM   168  N N     . ALA A 1 212 ? -3.499  50.953  114.049 1.00 100.31 ?  193 ALA A N     1 
ATOM   169  C CA    . ALA A 1 212 ? -2.543  50.834  115.142 1.00 97.05  ?  193 ALA A CA    1 
ATOM   170  C C     . ALA A 1 212 ? -2.192  52.196  115.730 1.00 104.55 ?  193 ALA A C     1 
ATOM   171  O O     . ALA A 1 212 ? -2.112  52.348  116.955 1.00 109.88 ?  193 ALA A O     1 
ATOM   172  C CB    . ALA A 1 212 ? -1.283  50.123  114.664 1.00 95.33  ?  193 ALA A CB    1 
ATOM   173  N N     . ALA A 1 213 ? -1.967  53.204  114.897 1.00 102.26 ?  194 ALA A N     1 
ATOM   174  C CA    . ALA A 1 213 ? -1.595  54.472  115.504 1.00 101.36 ?  194 ALA A CA    1 
ATOM   175  C C     . ALA A 1 213 ? -2.779  55.137  116.185 1.00 101.20 ?  194 ALA A C     1 
ATOM   176  O O     . ALA A 1 213 ? -2.580  55.945  117.098 1.00 106.47 ?  194 ALA A O     1 
ATOM   177  C CB    . ALA A 1 213 ? -0.991  55.399  114.470 1.00 107.91 ?  194 ALA A CB    1 
ATOM   178  N N     . CYS A 1 214 ? -4.010  54.821  115.761 1.00 97.96  ?  195 CYS A N     1 
ATOM   179  C CA    . CYS A 1 214 ? -5.186  55.330  116.467 1.00 105.63 ?  195 CYS A CA    1 
ATOM   180  C C     . CYS A 1 214 ? -5.569  54.492  117.686 1.00 106.85 ?  195 CYS A C     1 
ATOM   181  O O     . CYS A 1 214 ? -6.128  55.018  118.656 1.00 110.90 ?  195 CYS A O     1 
ATOM   182  C CB    . CYS A 1 214 ? -6.386  55.415  115.527 1.00 103.22 ?  195 CYS A CB    1 
ATOM   183  S SG    . CYS A 1 214 ? -6.282  56.664  114.302 1.00 113.91 ?  195 CYS A SG    1 
ATOM   184  N N     . PHE A 1 215 ? -5.290  53.204  117.663 1.00 101.06 ?  196 PHE A N     1 
ATOM   185  C CA    . PHE A 1 215 ? -5.773  52.294  118.694 1.00 96.27  ?  196 PHE A CA    1 
ATOM   186  C C     . PHE A 1 215 ? -4.617  51.461  119.247 1.00 98.92  ?  196 PHE A C     1 
ATOM   187  O O     . PHE A 1 215 ? -4.707  50.237  119.337 1.00 101.87 ?  196 PHE A O     1 
ATOM   188  C CB    . PHE A 1 215 ? -6.851  51.405  118.085 1.00 99.11  ?  196 PHE A CB    1 
ATOM   189  C CG    . PHE A 1 215 ? -8.085  52.144  117.638 1.00 97.47  ?  196 PHE A CG    1 
ATOM   190  C CD1   . PHE A 1 215 ? -8.130  52.747  116.412 1.00 102.59 ?  196 PHE A CD1   1 
ATOM   191  C CD2   . PHE A 1 215 ? -9.240  52.122  118.384 1.00 101.61 ?  196 PHE A CD2   1 
ATOM   192  C CE1   . PHE A 1 215 ? -9.274  53.406  115.986 1.00 106.09 ?  196 PHE A CE1   1 
ATOM   193  C CE2   . PHE A 1 215 ? -10.396 52.762  117.947 1.00 100.71 ?  196 PHE A CE2   1 
ATOM   194  C CZ    . PHE A 1 215 ? -10.412 53.396  116.757 1.00 99.72  ?  196 PHE A CZ    1 
ATOM   195  N N     . PRO A 1 216 ? -3.500  52.095  119.620 1.00 95.06  ?  197 PRO A N     1 
ATOM   196  C CA    . PRO A 1 216 ? -2.330  51.312  120.035 1.00 95.22  ?  197 PRO A CA    1 
ATOM   197  C C     . PRO A 1 216 ? -2.489  50.683  121.391 1.00 105.79 ?  197 PRO A C     1 
ATOM   198  O O     . PRO A 1 216 ? -1.685  49.807  121.733 1.00 109.76 ?  197 PRO A O     1 
ATOM   199  C CB    . PRO A 1 216 ? -1.204  52.343  120.040 1.00 95.34  ?  197 PRO A CB    1 
ATOM   200  C CG    . PRO A 1 216 ? -1.869  53.539  120.422 1.00 99.13  ?  197 PRO A CG    1 
ATOM   201  C CD    . PRO A 1 216 ? -3.244  53.528  119.794 1.00 99.61  ?  197 PRO A CD    1 
ATOM   202  N N     . ASP A 1 217 ? -3.541  51.044  122.098 1.00 109.65 ?  198 ASP A N     1 
ATOM   203  C CA    . ASP A 1 217 ? -3.745  50.318  123.365 1.00 106.38 ?  198 ASP A CA    1 
ATOM   204  C C     . ASP A 1 217 ? -4.395  48.986  123.012 1.00 108.46 ?  198 ASP A C     1 
ATOM   205  O O     . ASP A 1 217 ? -4.267  48.066  123.801 1.00 114.55 ?  198 ASP A O     1 
ATOM   206  C CB    . ASP A 1 217 ? -4.734  51.050  124.262 1.00 108.21 ?  198 ASP A CB    1 
ATOM   207  C CG    . ASP A 1 217 ? -5.972  51.432  123.491 1.00 108.93 ?  198 ASP A CG    1 
ATOM   208  O OD1   . ASP A 1 217 ? -5.799  51.898  122.379 1.00 112.66 ?  198 ASP A OD1   1 
ATOM   209  O OD2   . ASP A 1 217 ? -7.073  51.164  123.949 1.00 108.27 ?  198 ASP A OD2   1 
ATOM   210  N N     . ILE A 1 218 ? -4.991  48.877  121.827 1.00 103.11 ?  199 ILE A N     1 
ATOM   211  C CA    . ILE A 1 218 ? -5.788  47.678  121.481 1.00 100.65 ?  199 ILE A CA    1 
ATOM   212  C C     . ILE A 1 218 ? -4.923  46.722  120.705 1.00 103.30 ?  199 ILE A C     1 
ATOM   213  O O     . ILE A 1 218 ? -4.730  45.619  121.157 1.00 111.96 ?  199 ILE A O     1 
ATOM   214  C CB    . ILE A 1 218 ? -6.973  48.104  120.628 1.00 93.44  ?  199 ILE A CB    1 
ATOM   215  C CG1   . ILE A 1 218 ? -8.004  48.828  121.478 1.00 92.98  ?  199 ILE A CG1   1 
ATOM   216  C CG2   . ILE A 1 218 ? -7.569  46.897  119.962 1.00 98.50  ?  199 ILE A CG2   1 
ATOM   217  C CD1   . ILE A 1 218 ? -9.397  48.485  121.094 1.00 94.17  ?  199 ILE A CD1   1 
ATOM   218  N N     . ILE A 1 219 ? -4.257  47.229  119.668 1.00 102.61 ?  200 ILE A N     1 
ATOM   219  C CA    . ILE A 1 219 ? -3.372  46.405  118.790 1.00 104.49 ?  200 ILE A CA    1 
ATOM   220  C C     . ILE A 1 219 ? -2.333  45.670  119.620 1.00 105.10 ?  200 ILE A C     1 
ATOM   221  O O     . ILE A 1 219 ? -2.104  44.504  119.367 1.00 109.99 ?  200 ILE A O     1 
ATOM   222  C CB    . ILE A 1 219 ? -2.776  47.193  117.598 1.00 100.19 ?  200 ILE A CB    1 
ATOM   223  C CG1   . ILE A 1 219 ? -2.401  46.278  116.440 1.00 97.24  ?  200 ILE A CG1   1 
ATOM   224  C CG2   . ILE A 1 219 ? -1.615  48.103  117.933 1.00 101.76 ?  200 ILE A CG2   1 
ATOM   225  C CD1   . ILE A 1 219 ? -2.647  44.840  116.741 1.00 104.14 ?  200 ILE A CD1   1 
ATOM   226  N N     . SER A 1 220 ? -1.761  46.336  120.599 1.00 104.51 ?  201 SER A N     1 
ATOM   227  C CA    . SER A 1 220 ? -0.717  45.723  121.448 1.00 108.34 ?  201 SER A CA    1 
ATOM   228  C C     . SER A 1 220 ? -1.378  45.093  122.668 1.00 110.95 ?  201 SER A C     1 
ATOM   229  O O     . SER A 1 220 ? -0.651  44.686  123.558 1.00 112.54 ?  201 SER A O     1 
ATOM   230  C CB    . SER A 1 220 ? 0.218   46.764  121.926 1.00 106.81 ?  201 SER A CB    1 
ATOM   231  O OG    . SER A 1 220 ? -0.389  47.512  122.963 1.00 110.44 ?  201 SER A OG    1 
ATOM   232  N N     . GLY A 1 221 ? -2.705  45.064  122.714 1.00 108.28 ?  202 GLY A N     1 
ATOM   233  C CA    . GLY A 1 221 ? -3.417  44.531  123.884 1.00 112.96 ?  202 GLY A CA    1 
ATOM   234  C C     . GLY A 1 221 ? -3.555  43.026  123.885 1.00 123.66 ?  202 GLY A C     1 
ATOM   235  O O     . GLY A 1 221 ? -2.537  42.333  123.839 1.00 126.64 ?  202 GLY A O     1 
ATOM   236  N N     . PRO A 1 222 ? -4.788  42.497  123.978 1.00 129.73 ?  203 PRO A N     1 
ATOM   237  C CA    . PRO A 1 222 ? -5.046  41.078  124.059 1.00 131.41 ?  203 PRO A CA    1 
ATOM   238  C C     . PRO A 1 222 ? -5.802  40.591  122.824 1.00 122.09 ?  203 PRO A C     1 
ATOM   239  O O     . PRO A 1 222 ? -6.777  41.193  122.466 1.00 116.48 ?  203 PRO A O     1 
ATOM   240  C CB    . PRO A 1 222 ? -6.012  41.134  125.233 1.00 125.41 ?  203 PRO A CB    1 
ATOM   241  C CG    . PRO A 1 222 ? -6.884  42.326  124.911 1.00 121.74 ?  203 PRO A CG    1 
ATOM   242  C CD    . PRO A 1 222 ? -6.029  43.238  124.059 1.00 125.50 ?  203 PRO A CD    1 
ATOM   243  N N     . GLN A 1 223 ? -5.327  39.483  122.266 1.00 117.94 ?  204 GLN A N     1 
ATOM   244  C CA    . GLN A 1 223 ? -5.846  38.876  121.021 1.00 123.04 ?  204 GLN A CA    1 
ATOM   245  C C     . GLN A 1 223 ? -7.366  38.868  121.002 1.00 121.59 ?  204 GLN A C     1 
ATOM   246  O O     . GLN A 1 223 ? -7.912  39.040  119.932 1.00 123.73 ?  204 GLN A O     1 
ATOM   247  C CB    . GLN A 1 223 ? -5.244  37.495  120.811 1.00 130.88 ?  204 GLN A CB    1 
ATOM   248  C CG    . GLN A 1 223 ? -3.879  37.551  120.150 1.00 132.53 ?  204 GLN A CG    1 
ATOM   249  C CD    . GLN A 1 223 ? -4.005  37.522  118.649 1.00 136.09 ?  204 GLN A CD    1 
ATOM   250  O OE1   . GLN A 1 223 ? -5.039  37.874  118.090 1.00 131.29 ?  204 GLN A OE1   1 
ATOM   251  N NE2   . GLN A 1 223 ? -2.947  37.090  117.984 1.00 139.13 ?  204 GLN A NE2   1 
ATOM   252  N N     . GLN A 1 224 ? -8.020  38.697  122.139 1.00 118.61 ?  205 GLN A N     1 
ATOM   253  C CA    . GLN A 1 224 ? -9.491  38.770  122.015 1.00 122.70 ?  205 GLN A CA    1 
ATOM   254  C C     . GLN A 1 224 ? -9.896  40.217  121.767 1.00 119.43 ?  205 GLN A C     1 
ATOM   255  O O     . GLN A 1 224 ? -10.798 40.421  120.960 1.00 119.43 ?  205 GLN A O     1 
ATOM   256  C CB    . GLN A 1 224 ? -10.180 38.224  123.256 1.00 132.47 ?  205 GLN A CB    1 
ATOM   257  C CG    . GLN A 1 224 ? -11.693 38.327  123.174 1.00 133.86 ?  205 GLN A CG    1 
ATOM   258  C CD    . GLN A 1 224 ? -12.258 37.427  122.107 1.00 136.42 ?  205 GLN A CD    1 
ATOM   259  O OE1   . GLN A 1 224 ? -12.040 36.223  122.105 1.00 140.36 ?  205 GLN A OE1   1 
ATOM   260  N NE2   . GLN A 1 224 ? -12.997 38.011  121.186 1.00 133.59 ?  205 GLN A NE2   1 
ATOM   261  N N     . THR A 1 225 ? -9.256  41.153  122.463 1.00 119.59 ?  206 THR A N     1 
ATOM   262  C CA    . THR A 1 225 ? -9.533  42.574  122.279 1.00 121.21 ?  206 THR A CA    1 
ATOM   263  C C     . THR A 1 225 ? -9.572  42.943  120.804 1.00 119.94 ?  206 THR A C     1 
ATOM   264  O O     . THR A 1 225 ? -10.582 43.451  120.292 1.00 115.96 ?  206 THR A O     1 
ATOM   265  C CB    . THR A 1 225 ? -8.469  43.399  123.019 1.00 121.97 ?  206 THR A CB    1 
ATOM   266  O OG1   . THR A 1 225 ? -8.648  43.278  124.440 1.00 122.90 ?  206 THR A OG1   1 
ATOM   267  C CG2   . THR A 1 225 ? -8.493  44.850  122.598 1.00 117.58 ?  206 THR A CG2   1 
ATOM   268  N N     . GLN A 1 226 ? -8.458  42.675  120.111 1.00 119.40 ?  207 GLN A N     1 
ATOM   269  C CA    . GLN A 1 226 ? -8.341  42.973  118.692 1.00 110.18 ?  207 GLN A CA    1 
ATOM   270  C C     . GLN A 1 226 ? -9.533  42.419  117.921 1.00 113.41 ?  207 GLN A C     1 
ATOM   271  O O     . GLN A 1 226 ? -10.084 43.096  117.048 1.00 112.63 ?  207 GLN A O     1 
ATOM   272  C CB    . GLN A 1 226 ? -7.018  42.405  118.176 1.00 102.74 ?  207 GLN A CB    1 
ATOM   273  C CG    . GLN A 1 226 ? -5.804  42.878  118.987 1.00 104.56 ?  207 GLN A CG    1 
ATOM   274  C CD    . GLN A 1 226 ? -4.477  42.264  118.523 1.00 111.28 ?  207 GLN A CD    1 
ATOM   275  O OE1   . GLN A 1 226 ? -4.438  41.470  117.584 1.00 120.36 ?  207 GLN A OE1   1 
ATOM   276  N NE2   . GLN A 1 226 ? -3.392  42.607  119.208 1.00 109.19 ?  207 GLN A NE2   1 
ATOM   277  N N     . LYS A 1 227 ? -9.985  41.207  118.271 1.00 118.01 ?  208 LYS A N     1 
ATOM   278  C CA    . LYS A 1 227 ? -11.137 40.629  117.578 1.00 119.27 ?  208 LYS A CA    1 
ATOM   279  C C     . LYS A 1 227 ? -12.395 41.468  117.780 1.00 117.25 ?  208 LYS A C     1 
ATOM   280  O O     . LYS A 1 227 ? -13.140 41.720  116.820 1.00 114.32 ?  208 LYS A O     1 
ATOM   281  C CB    . LYS A 1 227 ? -11.369 39.175  118.018 1.00 119.32 ?  208 LYS A CB    1 
ATOM   282  C CG    . LYS A 1 227 ? -10.323 38.208  117.449 1.00 126.23 ?  208 LYS A CG    1 
ATOM   283  C CD    . LYS A 1 227 ? -10.642 36.725  117.686 1.00 128.05 ?  208 LYS A CD    1 
ATOM   284  C CE    . LYS A 1 227 ? -9.538  35.840  117.083 1.00 122.44 ?  208 LYS A CE    1 
ATOM   285  N NZ    . LYS A 1 227 ? -9.787  34.382  117.247 1.00 123.61 ?  208 LYS A NZ    1 
ATOM   286  N N     . VAL A 1 228 ? -12.644 41.925  119.013 1.00 120.14 ?  209 VAL A N     1 
ATOM   287  C CA    . VAL A 1 228 ? -13.861 42.688  119.278 1.00 120.64 ?  209 VAL A CA    1 
ATOM   288  C C     . VAL A 1 228 ? -13.873 43.954  118.437 1.00 122.01 ?  209 VAL A C     1 
ATOM   289  O O     . VAL A 1 228 ? -14.904 44.348  117.870 1.00 123.99 ?  209 VAL A O     1 
ATOM   290  C CB    . VAL A 1 228 ? -13.967 43.035  120.768 1.00 110.36 ?  209 VAL A CB    1 
ATOM   291  C CG1   . VAL A 1 228 ? -15.304 43.738  121.028 1.00 108.83 ?  209 VAL A CG1   1 
ATOM   292  C CG2   . VAL A 1 228 ? -13.742 41.818  121.614 1.00 114.89 ?  209 VAL A CG2   1 
ATOM   293  N N     . PHE A 1 229 ? -12.716 44.606  118.349 1.00 118.56 ?  210 PHE A N     1 
ATOM   294  C CA    . PHE A 1 229 ? -12.594 45.854  117.609 1.00 117.31 ?  210 PHE A CA    1 
ATOM   295  C C     . PHE A 1 229 ? -12.801 45.650  116.112 1.00 114.88 ?  210 PHE A C     1 
ATOM   296  O O     . PHE A 1 229 ? -13.516 46.425  115.462 1.00 109.44 ?  210 PHE A O     1 
ATOM   297  C CB    . PHE A 1 229 ? -11.220 46.447  117.906 1.00 118.40 ?  210 PHE A CB    1 
ATOM   298  C CG    . PHE A 1 229 ? -10.680 47.290  116.812 1.00 111.60 ?  210 PHE A CG    1 
ATOM   299  C CD1   . PHE A 1 229 ? -11.288 48.490  116.484 1.00 109.10 ?  210 PHE A CD1   1 
ATOM   300  C CD2   . PHE A 1 229 ? -9.542  46.891  116.131 1.00 104.14 ?  210 PHE A CD2   1 
ATOM   301  C CE1   . PHE A 1 229 ? -10.786 49.256  115.493 1.00 110.71 ?  210 PHE A CE1   1 
ATOM   302  C CE2   . PHE A 1 229 ? -9.036  47.651  115.137 1.00 105.57 ?  210 PHE A CE2   1 
ATOM   303  C CZ    . PHE A 1 229 ? -9.650  48.839  114.811 1.00 111.26 ?  210 PHE A CZ    1 
ATOM   304  N N     . LEU A 1 230 ? -12.159 44.620  115.548 1.00 115.14 ?  211 LEU A N     1 
ATOM   305  C CA    . LEU A 1 230 ? -12.306 44.344  114.129 1.00 105.43 ?  211 LEU A CA    1 
ATOM   306  C C     . LEU A 1 230 ? -13.756 44.079  113.784 1.00 110.99 ?  211 LEU A C     1 
ATOM   307  O O     . LEU A 1 230 ? -14.212 44.441  112.696 1.00 116.60 ?  211 LEU A O     1 
ATOM   308  C CB    . LEU A 1 230 ? -11.450 43.153  113.711 1.00 99.06  ?  211 LEU A CB    1 
ATOM   309  C CG    . LEU A 1 230 ? -9.943  43.299  113.883 1.00 101.25 ?  211 LEU A CG    1 
ATOM   310  C CD1   . LEU A 1 230 ? -9.219  42.148  113.235 1.00 109.21 ?  211 LEU A CD1   1 
ATOM   311  C CD2   . LEU A 1 230 ? -9.463  44.599  113.325 1.00 104.03 ?  211 LEU A CD2   1 
ATOM   312  N N     . PHE A 1 231 ? -14.505 43.443  114.690 1.00 113.24 ?  212 PHE A N     1 
ATOM   313  C CA    . PHE A 1 231 ? -15.921 43.267  114.397 1.00 115.18 ?  212 PHE A CA    1 
ATOM   314  C C     . PHE A 1 231 ? -16.669 44.587  114.426 1.00 115.51 ?  212 PHE A C     1 
ATOM   315  O O     . PHE A 1 231 ? -17.592 44.800  113.630 1.00 115.56 ?  212 PHE A O     1 
ATOM   316  C CB    . PHE A 1 231 ? -16.594 42.268  115.331 1.00 115.58 ?  212 PHE A CB    1 
ATOM   317  C CG    . PHE A 1 231 ? -18.028 42.016  114.946 1.00 122.17 ?  212 PHE A CG    1 
ATOM   318  C CD1   . PHE A 1 231 ? -18.362 41.015  114.052 1.00 128.61 ?  212 PHE A CD1   1 
ATOM   319  C CD2   . PHE A 1 231 ? -19.051 42.796  115.475 1.00 125.12 ?  212 PHE A CD2   1 
ATOM   320  C CE1   . PHE A 1 231 ? -19.691 40.809  113.682 1.00 132.40 ?  212 PHE A CE1   1 
ATOM   321  C CE2   . PHE A 1 231 ? -20.381 42.589  115.115 1.00 125.69 ?  212 PHE A CE2   1 
ATOM   322  C CZ    . PHE A 1 231 ? -20.700 41.595  114.223 1.00 128.28 ?  212 PHE A CZ    1 
ATOM   323  N N     . ILE A 1 232 ? -16.309 45.481  115.337 1.00 116.05 ?  213 ILE A N     1 
ATOM   324  C CA    . ILE A 1 232 ? -17.009 46.757  115.381 1.00 119.98 ?  213 ILE A CA    1 
ATOM   325  C C     . ILE A 1 232 ? -16.746 47.546  114.097 1.00 120.35 ?  213 ILE A C     1 
ATOM   326  O O     . ILE A 1 232 ? -17.674 48.066  113.459 1.00 115.60 ?  213 ILE A O     1 
ATOM   327  C CB    . ILE A 1 232 ? -16.613 47.527  116.652 1.00 112.56 ?  213 ILE A CB    1 
ATOM   328  C CG1   . ILE A 1 232 ? -16.875 46.643  117.864 1.00 110.34 ?  213 ILE A CG1   1 
ATOM   329  C CG2   . ILE A 1 232 ? -17.432 48.788  116.780 1.00 114.17 ?  213 ILE A CG2   1 
ATOM   330  C CD1   . ILE A 1 232 ? -16.765 47.358  119.155 1.00 116.80 ?  213 ILE A CD1   1 
ATOM   331  N N     . ARG A 1 233 ? -15.482 47.588  113.668 1.00 119.77 ?  214 ARG A N     1 
ATOM   332  C CA    . ARG A 1 233 ? -15.131 48.212  112.396 1.00 113.10 ?  214 ARG A CA    1 
ATOM   333  C C     . ARG A 1 233 ? -15.912 47.629  111.216 1.00 115.87 ?  214 ARG A C     1 
ATOM   334  O O     . ARG A 1 233 ? -16.600 48.360  110.490 1.00 113.94 ?  214 ARG A O     1 
ATOM   335  C CB    . ARG A 1 233 ? -13.627 48.095  112.147 1.00 108.14 ?  214 ARG A CB    1 
ATOM   336  C CG    . ARG A 1 233 ? -13.367 48.413  110.701 1.00 110.14 ?  214 ARG A CG    1 
ATOM   337  C CD    . ARG A 1 233 ? -11.957 48.643  110.282 1.00 107.94 ?  214 ARG A CD    1 
ATOM   338  N NE    . ARG A 1 233 ? -10.952 47.621  110.582 1.00 95.65  ?  214 ARG A NE    1 
ATOM   339  C CZ    . ARG A 1 233 ? -10.814 46.469  109.944 1.00 93.32  ?  214 ARG A CZ    1 
ATOM   340  N NH1   . ARG A 1 233 ? -11.705 46.095  109.044 1.00 98.19  ?  214 ARG A NH1   1 
ATOM   341  N NH2   . ARG A 1 233 ? -9.813  45.664  110.266 1.00 97.64  ?  214 ARG A NH2   1 
ATOM   342  N N     . ASN A 1 234 ? -15.770 46.321  110.969 1.00 116.35 ?  215 ASN A N     1 
ATOM   343  C CA    . ASN A 1 234 ? -16.421 45.737  109.801 1.00 110.40 ?  215 ASN A CA    1 
ATOM   344  C C     . ASN A 1 234 ? -17.925 45.926  109.876 1.00 115.44 ?  215 ASN A C     1 
ATOM   345  O O     . ASN A 1 234 ? -18.565 46.296  108.885 1.00 118.29 ?  215 ASN A O     1 
ATOM   346  C CB    . ASN A 1 234 ? -16.070 44.259  109.670 1.00 104.86 ?  215 ASN A CB    1 
ATOM   347  C CG    . ASN A 1 234 ? -14.576 44.027  109.655 1.00 106.90 ?  215 ASN A CG    1 
ATOM   348  O OD1   . ASN A 1 234 ? -13.796 44.915  109.306 1.00 104.10 ?  215 ASN A OD1   1 
ATOM   349  N ND2   . ASN A 1 234 ? -14.170 42.818  109.983 1.00 112.33 ?  215 ASN A ND2   1 
ATOM   350  N N     . ARG A 1 235 ? -18.495 45.748  111.068 1.00 120.81 ?  216 ARG A N     1 
ATOM   351  C CA    . ARG A 1 235 ? -19.938 45.884  111.225 1.00 123.88 ?  216 ARG A CA    1 
ATOM   352  C C     . ARG A 1 235 ? -20.411 47.296  110.884 1.00 119.10 ?  216 ARG A C     1 
ATOM   353  O O     . ARG A 1 235 ? -21.465 47.470  110.261 1.00 119.00 ?  216 ARG A O     1 
ATOM   354  C CB    . ARG A 1 235 ? -20.350 45.487  112.645 1.00 120.57 ?  216 ARG A CB    1 
ATOM   355  C CG    . ARG A 1 235 ? -21.840 45.455  112.800 1.00 123.06 ?  216 ARG A CG    1 
ATOM   356  C CD    . ARG A 1 235 ? -22.457 44.291  112.045 1.00 127.46 ?  216 ARG A CD    1 
ATOM   357  N NE    . ARG A 1 235 ? -23.906 44.295  112.208 1.00 133.03 ?  216 ARG A NE    1 
ATOM   358  C CZ    . ARG A 1 235 ? -24.739 44.818  111.312 1.00 129.98 ?  216 ARG A CZ    1 
ATOM   359  N NH1   . ARG A 1 235 ? -24.249 45.358  110.209 1.00 128.21 ?  216 ARG A NH1   1 
ATOM   360  N NH2   . ARG A 1 235 ? -26.052 44.806  111.512 1.00 134.36 ?  216 ARG A NH2   1 
ATOM   361  N N     . THR A 1 236 ? -19.641 48.318  111.261 1.00 117.97 ?  217 THR A N     1 
ATOM   362  C CA    . THR A 1 236 ? -20.028 49.682  110.901 1.00 122.97 ?  217 THR A CA    1 
ATOM   363  C C     . THR A 1 236 ? -19.926 49.902  109.392 1.00 124.68 ?  217 THR A C     1 
ATOM   364  O O     . THR A 1 236 ? -20.878 50.376  108.755 1.00 122.73 ?  217 THR A O     1 
ATOM   365  C CB    . THR A 1 236 ? -19.158 50.714  111.626 1.00 123.32 ?  217 THR A CB    1 
ATOM   366  O OG1   . THR A 1 236 ? -19.243 50.535  113.045 1.00 121.14 ?  217 THR A OG1   1 
ATOM   367  C CG2   . THR A 1 236 ? -19.624 52.130  111.255 1.00 118.44 ?  217 THR A CG2   1 
ATOM   368  N N     . LEU A 1 237 ? -18.751 49.611  108.815 1.00 121.43 ?  218 LEU A N     1 
ATOM   369  C CA    . LEU A 1 237 ? -18.585 49.703  107.374 1.00 107.01 ?  218 LEU A CA    1 
ATOM   370  C C     . LEU A 1 237 ? -19.781 49.086  106.689 1.00 110.20 ?  218 LEU A C     1 
ATOM   371  O O     . LEU A 1 237 ? -20.424 49.725  105.855 1.00 114.05 ?  218 LEU A O     1 
ATOM   372  C CB    . LEU A 1 237 ? -17.290 49.015  106.957 1.00 101.84 ?  218 LEU A CB    1 
ATOM   373  C CG    . LEU A 1 237 ? -16.084 49.734  107.547 1.00 100.49 ?  218 LEU A CG    1 
ATOM   374  C CD1   . LEU A 1 237 ? -14.854 48.862  107.539 1.00 100.70 ?  218 LEU A CD1   1 
ATOM   375  C CD2   . LEU A 1 237 ? -15.840 51.009  106.767 1.00 99.10  ?  218 LEU A CD2   1 
ATOM   376  N N     . GLN A 1 238 ? -20.161 47.882  107.126 1.00 112.25 ?  219 GLN A N     1 
ATOM   377  C CA    . GLN A 1 238 ? -21.309 47.194  106.543 1.00 120.54 ?  219 GLN A CA    1 
ATOM   378  C C     . GLN A 1 238 ? -22.565 48.054  106.618 1.00 120.64 ?  219 GLN A C     1 
ATOM   379  O O     . GLN A 1 238 ? -23.336 48.125  105.655 1.00 124.06 ?  219 GLN A O     1 
ATOM   380  C CB    . GLN A 1 238 ? -21.528 45.846  107.245 1.00 127.26 ?  219 GLN A CB    1 
ATOM   381  C CG    . GLN A 1 238 ? -22.505 44.864  106.547 1.00 130.03 ?  219 GLN A CG    1 
ATOM   382  C CD    . GLN A 1 238 ? -22.715 43.563  107.336 1.00 133.20 ?  219 GLN A CD    1 
ATOM   383  O OE1   . GLN A 1 238 ? -22.664 43.549  108.567 1.00 132.33 ?  219 GLN A OE1   1 
ATOM   384  N NE2   . GLN A 1 238 ? -22.938 42.465  106.619 1.00 137.50 ?  219 GLN A NE2   1 
ATOM   385  N N     . LEU A 1 239 ? -22.712 48.772  107.714 1.00 117.54 ?  220 LEU A N     1 
ATOM   386  C CA    . LEU A 1 239 ? -23.946 49.571  107.807 1.00 119.97 ?  220 LEU A CA    1 
ATOM   387  C C     . LEU A 1 239 ? -23.874 50.691  106.785 1.00 119.43 ?  220 LEU A C     1 
ATOM   388  O O     . LEU A 1 239 ? -24.834 50.872  106.057 1.00 120.32 ?  220 LEU A O     1 
ATOM   389  C CB    . LEU A 1 239 ? -24.054 50.149  109.212 1.00 122.74 ?  220 LEU A CB    1 
ATOM   390  C CG    . LEU A 1 239 ? -24.655 49.207  110.240 1.00 118.36 ?  220 LEU A CG    1 
ATOM   391  C CD1   . LEU A 1 239 ? -23.840 49.246  111.509 1.00 124.08 ?  220 LEU A CD1   1 
ATOM   392  C CD2   . LEU A 1 239 ? -26.096 49.579  110.524 1.00 121.12 ?  220 LEU A CD2   1 
ATOM   393  N N     . TRP A 1 240 ? -22.768 51.415  106.755 1.00 117.16 ?  221 TRP A N     1 
ATOM   394  C CA    . TRP A 1 240 ? -22.705 52.556  105.815 1.00 117.81 ?  221 TRP A CA    1 
ATOM   395  C C     . TRP A 1 240 ? -22.851 52.027  104.400 1.00 117.73 ?  221 TRP A C     1 
ATOM   396  O O     . TRP A 1 240 ? -23.701 52.513  103.656 1.00 116.10 ?  221 TRP A O     1 
ATOM   397  C CB    . TRP A 1 240 ? -21.370 53.267  106.037 1.00 118.15 ?  221 TRP A CB    1 
ATOM   398  C CG    . TRP A 1 240 ? -20.773 54.007  104.887 1.00 110.87 ?  221 TRP A CG    1 
ATOM   399  C CD1   . TRP A 1 240 ? -19.563 53.768  104.320 1.00 108.55 ?  221 TRP A CD1   1 
ATOM   400  C CD2   . TRP A 1 240 ? -21.305 55.155  104.221 1.00 111.37 ?  221 TRP A CD2   1 
ATOM   401  N NE1   . TRP A 1 240 ? -19.324 54.661  103.321 1.00 109.45 ?  221 TRP A NE1   1 
ATOM   402  C CE2   . TRP A 1 240 ? -20.376 55.523  103.239 1.00 112.91 ?  221 TRP A CE2   1 
ATOM   403  C CE3   . TRP A 1 240 ? -22.477 55.892  104.341 1.00 114.93 ?  221 TRP A CE3   1 
ATOM   404  C CZ2   . TRP A 1 240 ? -20.583 56.593  102.383 1.00 115.92 ?  221 TRP A CZ2   1 
ATOM   405  C CZ3   . TRP A 1 240 ? -22.664 56.972  103.518 1.00 118.72 ?  221 TRP A CZ3   1 
ATOM   406  C CH2   . TRP A 1 240 ? -21.748 57.297  102.530 1.00 117.93 ?  221 TRP A CH2   1 
ATOM   407  N N     . LEU A 1 241 ? -21.960 51.120  104.012 1.00 118.22 ?  222 LEU A N     1 
ATOM   408  C CA    . LEU A 1 241 ? -22.047 50.523  102.657 1.00 112.68 ?  222 LEU A CA    1 
ATOM   409  C C     . LEU A 1 241 ? -23.439 49.942  102.505 1.00 117.79 ?  222 LEU A C     1 
ATOM   410  O O     . LEU A 1 241 ? -23.996 50.014  101.431 1.00 122.29 ?  222 LEU A O     1 
ATOM   411  C CB    . LEU A 1 241 ? -21.051 49.374  102.581 1.00 104.71 ?  222 LEU A CB    1 
ATOM   412  C CG    . LEU A 1 241 ? -19.597 49.800  102.587 1.00 103.36 ?  222 LEU A CG    1 
ATOM   413  C CD1   . LEU A 1 241 ? -18.696 48.613  102.349 1.00 103.20 ?  222 LEU A CD1   1 
ATOM   414  C CD2   . LEU A 1 241 ? -19.378 50.835  101.516 1.00 113.32 ?  222 LEU A CD2   1 
ATOM   415  N N     . ASP A 1 242 ? -24.113 49.447  103.557 1.00 117.47 ?  223 ASP A N     1 
ATOM   416  C CA    . ASP A 1 242 ? -25.454 48.834  103.278 1.00 120.28 ?  223 ASP A CA    1 
ATOM   417  C C     . ASP A 1 242 ? -26.436 49.852  102.742 1.00 124.29 ?  223 ASP A C     1 
ATOM   418  O O     . ASP A 1 242 ? -27.260 49.470  101.919 1.00 126.85 ?  223 ASP A O     1 
ATOM   419  C CB    . ASP A 1 242 ? -26.233 48.196  104.416 1.00 120.02 ?  223 ASP A CB    1 
ATOM   420  C CG    . ASP A 1 242 ? -26.256 46.705  104.207 1.00 135.43 ?  223 ASP A CG    1 
ATOM   421  O OD1   . ASP A 1 242 ? -27.183 46.238  103.539 1.00 142.40 ?  223 ASP A OD1   1 
ATOM   422  O OD2   . ASP A 1 242 ? -25.311 46.045  104.654 1.00 138.43 ?  223 ASP A OD2   1 
ATOM   423  N N     . ASN A 1 243 ? -26.363 51.077  103.227 1.00 118.04 ?  224 ASN A N     1 
ATOM   424  C CA    . ASN A 1 243 ? -27.237 52.043  102.507 1.00 120.27 ?  224 ASN A CA    1 
ATOM   425  C C     . ASN A 1 243 ? -26.554 53.395  102.631 1.00 121.40 ?  224 ASN A C     1 
ATOM   426  O O     . ASN A 1 243 ? -26.871 54.109  103.551 1.00 128.73 ?  224 ASN A O     1 
ATOM   427  C CB    . ASN A 1 243 ? -28.641 52.117  103.098 1.00 125.09 ?  224 ASN A CB    1 
ATOM   428  C CG    . ASN A 1 243 ? -29.359 53.411  102.782 1.00 131.53 ?  224 ASN A CG    1 
ATOM   429  O OD1   . ASN A 1 243 ? -29.009 54.117  101.842 1.00 128.24 ?  224 ASN A OD1   1 
ATOM   430  N ND2   . ASN A 1 243 ? -30.370 53.731  103.569 1.00 130.20 ?  224 ASN A ND2   1 
ATOM   431  N N     . PRO A 1 244 ? -25.663 53.806  101.720 1.00 118.17 ?  225 PRO A N     1 
ATOM   432  C CA    . PRO A 1 244 ? -24.870 54.991  101.916 1.00 116.74 ?  225 PRO A CA    1 
ATOM   433  C C     . PRO A 1 244 ? -25.496 56.272  101.389 1.00 124.84 ?  225 PRO A C     1 
ATOM   434  O O     . PRO A 1 244 ? -24.771 57.162  101.098 1.00 127.69 ?  225 PRO A O     1 
ATOM   435  C CB    . PRO A 1 244 ? -23.710 54.749  100.976 1.00 114.20 ?  225 PRO A CB    1 
ATOM   436  C CG    . PRO A 1 244 ? -24.423 54.183  99.812  1.00 116.70 ?  225 PRO A CG    1 
ATOM   437  C CD    . PRO A 1 244 ? -25.386 53.199  100.441 1.00 121.07 ?  225 PRO A CD    1 
ATOM   438  N N     . LYS A 1 245 ? -26.793 56.267  101.141 1.00 126.20 ?  226 LYS A N     1 
ATOM   439  C CA    . LYS A 1 245 ? -27.394 57.535  100.682 1.00 128.47 ?  226 LYS A CA    1 
ATOM   440  C C     . LYS A 1 245 ? -27.437 58.504  101.860 1.00 128.74 ?  226 LYS A C     1 
ATOM   441  O O     . LYS A 1 245 ? -27.245 59.685  101.629 1.00 129.55 ?  226 LYS A O     1 
ATOM   442  C CB    . LYS A 1 245 ? -28.793 57.297  100.116 1.00 130.60 ?  226 LYS A CB    1 
ATOM   443  C CG    . LYS A 1 245 ? -28.832 56.759  98.694  1.00 130.79 ?  226 LYS A CG    1 
ATOM   444  C CD    . LYS A 1 245 ? -29.221 57.797  97.672  1.00 129.51 ?  226 LYS A CD    1 
ATOM   445  C CE    . LYS A 1 245 ? -30.335 57.329  96.765  1.00 139.74 ?  226 LYS A CE    1 
ATOM   446  N NZ    . LYS A 1 245 ? -31.135 56.261  97.408  1.00 144.79 ?  226 LYS A NZ    1 
ATOM   447  N N     . ILE A 1 246 ? -27.667 58.023  103.083 1.00 129.16 ?  227 ILE A N     1 
ATOM   448  C CA    . ILE A 1 246 ? -27.763 58.979  104.226 1.00 128.59 ?  227 ILE A CA    1 
ATOM   449  C C     . ILE A 1 246 ? -26.729 58.703  105.317 1.00 124.45 ?  227 ILE A C     1 
ATOM   450  O O     . ILE A 1 246 ? -26.391 57.554  105.559 1.00 120.04 ?  227 ILE A O     1 
ATOM   451  C CB    . ILE A 1 246 ? -29.175 58.980  104.817 1.00 124.84 ?  227 ILE A CB    1 
ATOM   452  C CG1   . ILE A 1 246 ? -29.374 57.796  105.755 1.00 121.98 ?  227 ILE A CG1   1 
ATOM   453  C CG2   . ILE A 1 246 ? -30.225 58.988  103.726 1.00 128.50 ?  227 ILE A CG2   1 
ATOM   454  C CD1   . ILE A 1 246 ? -30.801 57.323  105.794 1.00 122.46 ?  227 ILE A CD1   1 
ATOM   455  N N     . GLN A 1 247 ? -26.351 59.765  106.023 1.00 123.00 ?  228 GLN A N     1 
ATOM   456  C CA    . GLN A 1 247 ? -25.329 59.809  107.100 1.00 124.74 ?  228 GLN A CA    1 
ATOM   457  C C     . GLN A 1 247 ? -25.479 58.685  108.117 1.00 126.67 ?  228 GLN A C     1 
ATOM   458  O O     . GLN A 1 247 ? -26.584 58.338  108.486 1.00 130.12 ?  228 GLN A O     1 
ATOM   459  C CB    . GLN A 1 247 ? -25.481 61.126  107.858 1.00 129.22 ?  228 GLN A CB    1 
ATOM   460  C CG    . GLN A 1 247 ? -24.372 61.432  108.852 1.00 124.75 ?  228 GLN A CG    1 
ATOM   461  C CD    . GLN A 1 247 ? -24.622 62.724  109.580 1.00 121.55 ?  228 GLN A CD    1 
ATOM   462  O OE1   . GLN A 1 247 ? -25.759 63.120  109.811 1.00 124.61 ?  228 GLN A OE1   1 
ATOM   463  N NE2   . GLN A 1 247 ? -23.546 63.402  109.929 1.00 117.17 ?  228 GLN A NE2   1 
ATOM   464  N N     . LEU A 1 248 ? -24.357 58.210  108.624 1.00 126.52 ?  229 LEU A N     1 
ATOM   465  C CA    . LEU A 1 248 ? -24.364 57.176  109.652 1.00 124.02 ?  229 LEU A CA    1 
ATOM   466  C C     . LEU A 1 248 ? -24.025 57.844  110.976 1.00 127.30 ?  229 LEU A C     1 
ATOM   467  O O     . LEU A 1 248 ? -22.853 58.104  111.278 1.00 124.96 ?  229 LEU A O     1 
ATOM   468  C CB    . LEU A 1 248 ? -23.380 56.062  109.323 1.00 119.29 ?  229 LEU A CB    1 
ATOM   469  C CG    . LEU A 1 248 ? -23.514 54.908  110.300 1.00 116.95 ?  229 LEU A CG    1 
ATOM   470  C CD1   . LEU A 1 248 ? -24.981 54.497  110.369 1.00 116.68 ?  229 LEU A CD1   1 
ATOM   471  C CD2   . LEU A 1 248 ? -22.628 53.749  109.877 1.00 113.98 ?  229 LEU A CD2   1 
ATOM   472  N N     . THR A 1 249 ? -25.058 58.137  111.758 1.00 131.91 ?  230 THR A N     1 
ATOM   473  C CA    . THR A 1 249 ? -24.832 58.641  113.102 1.00 129.62 ?  230 THR A CA    1 
ATOM   474  C C     . THR A 1 249 ? -24.233 57.563  113.987 1.00 125.44 ?  230 THR A C     1 
ATOM   475  O O     . THR A 1 249 ? -24.450 56.362  113.792 1.00 125.27 ?  230 THR A O     1 
ATOM   476  C CB    . THR A 1 249 ? -26.127 59.168  113.725 1.00 129.82 ?  230 THR A CB    1 
ATOM   477  O OG1   . THR A 1 249 ? -27.071 58.099  113.891 1.00 127.94 ?  230 THR A OG1   1 
ATOM   478  C CG2   . THR A 1 249 ? -26.712 60.268  112.873 1.00 133.80 ?  230 THR A CG2   1 
ATOM   479  N N     . PHE A 1 250 ? -23.450 58.019  114.959 1.00 127.74 ?  231 PHE A N     1 
ATOM   480  C CA    . PHE A 1 250 ? -22.940 57.140  116.007 1.00 130.94 ?  231 PHE A CA    1 
ATOM   481  C C     . PHE A 1 250 ? -24.073 56.501  116.812 1.00 130.24 ?  231 PHE A C     1 
ATOM   482  O O     . PHE A 1 250 ? -23.936 55.370  117.290 1.00 126.79 ?  231 PHE A O     1 
ATOM   483  C CB    . PHE A 1 250 ? -21.974 57.968  116.868 1.00 130.88 ?  231 PHE A CB    1 
ATOM   484  C CG    . PHE A 1 250 ? -21.561 57.337  118.169 1.00 122.62 ?  231 PHE A CG    1 
ATOM   485  C CD1   . PHE A 1 250 ? -21.028 56.059  118.210 1.00 124.24 ?  231 PHE A CD1   1 
ATOM   486  C CD2   . PHE A 1 250 ? -21.545 58.092  119.324 1.00 118.60 ?  231 PHE A CD2   1 
ATOM   487  C CE1   . PHE A 1 250 ? -20.603 55.499  119.404 1.00 117.47 ?  231 PHE A CE1   1 
ATOM   488  C CE2   . PHE A 1 250 ? -21.101 57.550  120.500 1.00 118.51 ?  231 PHE A CE2   1 
ATOM   489  C CZ    . PHE A 1 250 ? -20.634 56.245  120.540 1.00 114.01 ?  231 PHE A CZ    1 
ATOM   490  N N     . GLU A 1 251 ? -25.211 57.191  116.931 1.00 136.26 ?  232 GLU A N     1 
ATOM   491  C CA    . GLU A 1 251 ? -26.389 56.610  117.568 1.00 129.90 ?  232 GLU A CA    1 
ATOM   492  C C     . GLU A 1 251 ? -26.906 55.424  116.762 1.00 133.38 ?  232 GLU A C     1 
ATOM   493  O O     . GLU A 1 251 ? -27.167 54.346  117.312 1.00 135.73 ?  232 GLU A O     1 
ATOM   494  C CB    . GLU A 1 251 ? -27.491 57.666  117.694 1.00 133.32 ?  232 GLU A CB    1 
ATOM   495  C CG    . GLU A 1 251 ? -27.200 58.785  118.691 1.00 143.21 ?  232 GLU A CG    1 
ATOM   496  C CD    . GLU A 1 251 ? -26.155 59.810  118.200 1.00 150.08 ?  232 GLU A CD    1 
ATOM   497  O OE1   . GLU A 1 251 ? -25.846 59.857  116.977 1.00 146.37 ?  232 GLU A OE1   1 
ATOM   498  O OE2   . GLU A 1 251 ? -25.625 60.557  119.057 1.00 153.52 ?  232 GLU A OE2   1 
ATOM   499  N N     . ALA A 1 252 ? -27.066 55.618  115.447 1.00 133.61 ?  233 ALA A N     1 
ATOM   500  C CA    . ALA A 1 252 ? -27.619 54.577  114.584 1.00 129.55 ?  233 ALA A CA    1 
ATOM   501  C C     . ALA A 1 252 ? -26.745 53.328  114.608 1.00 126.83 ?  233 ALA A C     1 
ATOM   502  O O     . ALA A 1 252 ? -27.246 52.200  114.713 1.00 125.62 ?  233 ALA A O     1 
ATOM   503  C CB    . ALA A 1 252 ? -27.771 55.120  113.160 1.00 122.10 ?  233 ALA A CB    1 
ATOM   504  N N     . THR A 1 253 ? -25.428 53.521  114.514 1.00 124.51 ?  234 THR A N     1 
ATOM   505  C CA    . THR A 1 253 ? -24.478 52.420  114.625 1.00 123.53 ?  234 THR A CA    1 
ATOM   506  C C     . THR A 1 253 ? -24.742 51.588  115.863 1.00 128.72 ?  234 THR A C     1 
ATOM   507  O O     . THR A 1 253 ? -25.048 50.392  115.786 1.00 130.22 ?  234 THR A O     1 
ATOM   508  C CB    . THR A 1 253 ? -23.056 52.976  114.673 1.00 122.79 ?  234 THR A CB    1 
ATOM   509  O OG1   . THR A 1 253 ? -22.742 53.609  113.428 1.00 125.17 ?  234 THR A OG1   1 
ATOM   510  C CG2   . THR A 1 253 ? -22.057 51.877  114.970 1.00 120.19 ?  234 THR A CG2   1 
ATOM   511  N N     . LEU A 1 254 ? -24.640 52.234  117.022 1.00 133.11 ?  235 LEU A N     1 
ATOM   512  C CA    . LEU A 1 254 ? -24.680 51.549  118.308 1.00 134.77 ?  235 LEU A CA    1 
ATOM   513  C C     . LEU A 1 254 ? -26.053 50.960  118.607 1.00 135.77 ?  235 LEU A C     1 
ATOM   514  O O     . LEU A 1 254 ? -26.146 49.915  119.268 1.00 136.41 ?  235 LEU A O     1 
ATOM   515  C CB    . LEU A 1 254 ? -24.246 52.535  119.382 1.00 130.70 ?  235 LEU A CB    1 
ATOM   516  C CG    . LEU A 1 254 ? -23.845 51.943  120.709 1.00 130.86 ?  235 LEU A CG    1 
ATOM   517  C CD1   . LEU A 1 254 ? -22.939 50.759  120.452 1.00 134.40 ?  235 LEU A CD1   1 
ATOM   518  C CD2   . LEU A 1 254 ? -23.075 53.033  121.420 1.00 121.10 ?  235 LEU A CD2   1 
ATOM   519  N N     . GLN A 1 255 ? -27.116 51.629  118.149 1.00 134.80 ?  236 GLN A N     1 
ATOM   520  C CA    . GLN A 1 255 ? -28.441 51.026  118.045 1.00 139.33 ?  236 GLN A CA    1 
ATOM   521  C C     . GLN A 1 255 ? -28.394 49.580  117.533 1.00 143.82 ?  236 GLN A C     1 
ATOM   522  O O     . GLN A 1 255 ? -28.997 48.674  118.125 1.00 144.70 ?  236 GLN A O     1 
ATOM   523  C CB    . GLN A 1 255 ? -29.301 51.898  117.119 1.00 138.64 ?  236 GLN A CB    1 
ATOM   524  C CG    . GLN A 1 255 ? -30.694 51.356  116.787 1.00 147.94 ?  236 GLN A CG    1 
ATOM   525  C CD    . GLN A 1 255 ? -31.638 51.320  117.978 1.00 154.42 ?  236 GLN A CD    1 
ATOM   526  O OE1   . GLN A 1 255 ? -31.619 52.216  118.824 1.00 151.90 ?  236 GLN A OE1   1 
ATOM   527  N NE2   . GLN A 1 255 ? -32.479 50.282  118.042 1.00 157.39 ?  236 GLN A NE2   1 
ATOM   528  N N     . GLN A 1 256 ? -27.852 49.473  116.319 1.00 141.76 ?  237 GLN A N     1 
ATOM   529  C CA    . GLN A 1 256 ? -27.825 48.217  115.533 1.00 141.41 ?  237 GLN A CA    1 
ATOM   530  C C     . GLN A 1 256 ? -26.686 47.328  115.993 1.00 140.12 ?  237 GLN A C     1 
ATOM   531  O O     . GLN A 1 256 ? -26.638 46.173  115.581 1.00 140.18 ?  237 GLN A O     1 
ATOM   532  C CB    . GLN A 1 256 ? -27.623 48.538  114.059 1.00 137.65 ?  237 GLN A CB    1 
ATOM   533  C CG    . GLN A 1 256 ? -28.402 49.753  113.599 1.00 139.87 ?  237 GLN A CG    1 
ATOM   534  C CD    . GLN A 1 256 ? -29.394 49.370  112.533 1.00 145.66 ?  237 GLN A CD    1 
ATOM   535  O OE1   . GLN A 1 256 ? -29.640 48.194  112.294 1.00 146.20 ?  237 GLN A OE1   1 
ATOM   536  N NE2   . GLN A 1 256 ? -29.973 50.364  111.882 1.00 148.36 ?  237 GLN A NE2   1 
ATOM   537  N N     . LEU A 1 257 ? -25.808 47.845  116.835 1.00 135.96 ?  238 LEU A N     1 
ATOM   538  C CA    . LEU A 1 257 ? -24.722 46.949  117.281 1.00 139.82 ?  238 LEU A CA    1 
ATOM   539  C C     . LEU A 1 257 ? -25.324 45.827  118.125 1.00 149.79 ?  238 LEU A C     1 
ATOM   540  O O     . LEU A 1 257 ? -26.250 46.092  118.912 1.00 150.00 ?  238 LEU A O     1 
ATOM   541  C CB    . LEU A 1 257 ? -23.685 47.756  118.053 1.00 136.40 ?  238 LEU A CB    1 
ATOM   542  C CG    . LEU A 1 257 ? -22.261 47.487  117.590 1.00 132.19 ?  238 LEU A CG    1 
ATOM   543  C CD1   . LEU A 1 257 ? -21.329 47.342  118.776 1.00 127.63 ?  238 LEU A CD1   1 
ATOM   544  C CD2   . LEU A 1 257 ? -22.237 46.227  116.752 1.00 128.45 ?  238 LEU A CD2   1 
ATOM   545  N N     . GLU A 1 258 ? -24.765 44.626  118.015 1.00 151.82 ?  239 GLU A N     1 
ATOM   546  C CA    . GLU A 1 258 ? -25.348 43.470  118.738 1.00 153.44 ?  239 GLU A CA    1 
ATOM   547  C C     . GLU A 1 258 ? -24.488 43.057  119.932 1.00 145.18 ?  239 GLU A C     1 
ATOM   548  O O     . GLU A 1 258 ? -23.264 43.070  119.826 1.00 141.80 ?  239 GLU A O     1 
ATOM   549  C CB    . GLU A 1 258 ? -25.590 42.315  117.769 1.00 158.84 ?  239 GLU A CB    1 
ATOM   550  C CG    . GLU A 1 258 ? -27.021 41.824  117.812 1.00 163.81 ?  239 GLU A CG    1 
ATOM   551  C CD    . GLU A 1 258 ? -27.707 42.169  119.119 1.00 170.27 ?  239 GLU A CD    1 
ATOM   552  O OE1   . GLU A 1 258 ? -27.940 41.246  119.920 1.00 169.17 ?  239 GLU A OE1   1 
ATOM   553  O OE2   . GLU A 1 258 ? -27.982 43.364  119.341 1.00 170.48 ?  239 GLU A OE2   1 
ATOM   554  N N     . ALA A 1 259 ? -25.145 42.719  121.039 1.00 142.34 ?  240 ALA A N     1 
ATOM   555  C CA    . ALA A 1 259 ? -24.430 42.273  122.249 1.00 138.55 ?  240 ALA A CA    1 
ATOM   556  C C     . ALA A 1 259 ? -23.717 40.959  121.944 1.00 139.48 ?  240 ALA A C     1 
ATOM   557  O O     . ALA A 1 259 ? -24.295 40.131  121.246 1.00 140.28 ?  240 ALA A O     1 
ATOM   558  C CB    . ALA A 1 259 ? -25.405 42.114  123.377 1.00 134.90 ?  240 ALA A CB    1 
ATOM   559  N N     . PRO A 1 260 ? -22.483 40.733  122.433 1.00 134.49 ?  241 PRO A N     1 
ATOM   560  C CA    . PRO A 1 260 ? -21.905 41.533  123.503 1.00 132.31 ?  241 PRO A CA    1 
ATOM   561  C C     . PRO A 1 260 ? -21.154 42.745  122.956 1.00 136.75 ?  241 PRO A C     1 
ATOM   562  O O     . PRO A 1 260 ? -20.669 43.539  123.717 1.00 135.88 ?  241 PRO A O     1 
ATOM   563  C CB    . PRO A 1 260 ? -20.828 40.587  124.019 1.00 124.44 ?  241 PRO A CB    1 
ATOM   564  C CG    . PRO A 1 260 ? -20.341 39.921  122.778 1.00 125.29 ?  241 PRO A CG    1 
ATOM   565  C CD    . PRO A 1 260 ? -21.600 39.670  121.984 1.00 129.54 ?  241 PRO A CD    1 
ATOM   566  N N     . TYR A 1 261 ? -21.113 42.864  121.637 1.00 140.71 ?  242 TYR A N     1 
ATOM   567  C CA    . TYR A 1 261 ? -20.339 43.971  121.040 1.00 137.51 ?  242 TYR A CA    1 
ATOM   568  C C     . TYR A 1 261 ? -20.924 45.311  121.469 1.00 137.18 ?  242 TYR A C     1 
ATOM   569  O O     . TYR A 1 261 ? -20.138 46.145  121.892 1.00 133.10 ?  242 TYR A O     1 
ATOM   570  C CB    . TYR A 1 261 ? -20.134 43.738  119.547 1.00 135.28 ?  242 TYR A CB    1 
ATOM   571  C CG    . TYR A 1 261 ? -19.640 42.348  119.258 1.00 133.00 ?  242 TYR A CG    1 
ATOM   572  C CD1   . TYR A 1 261 ? -18.358 41.966  119.598 1.00 127.60 ?  242 TYR A CD1   1 
ATOM   573  C CD2   . TYR A 1 261 ? -20.467 41.402  118.690 1.00 135.28 ?  242 TYR A CD2   1 
ATOM   574  C CE1   . TYR A 1 261 ? -17.897 40.686  119.357 1.00 128.51 ?  242 TYR A CE1   1 
ATOM   575  C CE2   . TYR A 1 261 ? -20.024 40.116  118.442 1.00 136.85 ?  242 TYR A CE2   1 
ATOM   576  C CZ    . TYR A 1 261 ? -18.734 39.756  118.774 1.00 135.69 ?  242 TYR A CZ    1 
ATOM   577  O OH    . TYR A 1 261 ? -18.298 38.489  118.526 1.00 137.14 ?  242 TYR A OH    1 
ATOM   578  N N     . ASN A 1 262 ? -22.243 45.481  121.549 1.00 140.28 ?  243 ASN A N     1 
ATOM   579  C CA    . ASN A 1 262 ? -22.761 46.828  121.918 1.00 138.23 ?  243 ASN A CA    1 
ATOM   580  C C     . ASN A 1 262 ? -22.793 47.047  123.431 1.00 132.95 ?  243 ASN A C     1 
ATOM   581  O O     . ASN A 1 262 ? -23.846 47.400  123.943 1.00 132.20 ?  243 ASN A O     1 
ATOM   582  C CB    . ASN A 1 262 ? -24.155 47.070  121.348 1.00 142.16 ?  243 ASN A CB    1 
ATOM   583  C CG    . ASN A 1 262 ? -25.210 46.176  121.955 1.00 145.38 ?  243 ASN A CG    1 
ATOM   584  O OD1   . ASN A 1 262 ? -24.923 45.388  122.846 1.00 145.98 ?  243 ASN A OD1   1 
ATOM   585  N ND2   . ASN A 1 262 ? -26.432 46.279  121.465 1.00 141.12 ?  243 ASN A ND2   1 
ATOM   586  N N     . SER A 1 263 ? -21.640 46.981  124.085 1.00 133.72 ?  244 SER A N     1 
ATOM   587  C CA    . SER A 1 263 ? -21.510 47.143  125.543 1.00 137.16 ?  244 SER A CA    1 
ATOM   588  C C     . SER A 1 263 ? -20.573 48.310  125.786 1.00 134.02 ?  244 SER A C     1 
ATOM   589  O O     . SER A 1 263 ? -20.981 49.286  126.405 1.00 131.72 ?  244 SER A O     1 
ATOM   590  C CB    . SER A 1 263 ? -20.876 45.914  126.084 1.00 133.54 ?  244 SER A CB    1 
ATOM   591  O OG    . SER A 1 263 ? -19.657 45.676  125.405 1.00 130.18 ?  244 SER A OG    1 
ATOM   592  N N     . ASP A 1 264 ? -19.388 48.220  125.199 1.00 130.13 ?  245 ASP A N     1 
ATOM   593  C CA    . ASP A 1 264 ? -18.363 49.257  125.427 1.00 126.86 ?  245 ASP A CA    1 
ATOM   594  C C     . ASP A 1 264 ? -18.664 50.417  124.499 1.00 126.03 ?  245 ASP A C     1 
ATOM   595  O O     . ASP A 1 264 ? -17.984 50.546  123.499 1.00 128.91 ?  245 ASP A O     1 
ATOM   596  C CB    . ASP A 1 264 ? -16.979 48.704  125.123 1.00 119.66 ?  245 ASP A CB    1 
ATOM   597  C CG    . ASP A 1 264 ? -15.887 49.698  125.426 1.00 120.20 ?  245 ASP A CG    1 
ATOM   598  O OD1   . ASP A 1 264 ? -16.103 50.884  125.185 1.00 117.06 ?  245 ASP A OD1   1 
ATOM   599  O OD2   . ASP A 1 264 ? -14.839 49.268  125.906 1.00 119.77 ?  245 ASP A OD2   1 
ATOM   600  N N     . THR A 1 265 ? -19.527 51.326  124.930 1.00 123.62 ?  246 THR A N     1 
ATOM   601  C CA    . THR A 1 265 ? -19.910 52.462  124.066 1.00 119.93 ?  246 THR A CA    1 
ATOM   602  C C     . THR A 1 265 ? -18.681 53.294  123.713 1.00 118.78 ?  246 THR A C     1 
ATOM   603  O O     . THR A 1 265 ? -18.571 53.681  122.565 1.00 125.58 ?  246 THR A O     1 
ATOM   604  C CB    . THR A 1 265 ? -21.002 53.296  124.729 1.00 121.99 ?  246 THR A CB    1 
ATOM   605  O OG1   . THR A 1 265 ? -20.354 54.337  125.451 1.00 126.92 ?  246 THR A OG1   1 
ATOM   606  C CG2   . THR A 1 265 ? -21.849 52.477  125.672 1.00 119.94 ?  246 THR A CG2   1 
ATOM   607  N N     . VAL A 1 266 ? -17.756 53.504  124.640 1.00 113.76 ?  247 VAL A N     1 
ATOM   608  C CA    . VAL A 1 266 ? -16.564 54.329  124.311 1.00 115.92 ?  247 VAL A CA    1 
ATOM   609  C C     . VAL A 1 266 ? -15.798 53.685  123.160 1.00 119.10 ?  247 VAL A C     1 
ATOM   610  O O     . VAL A 1 266 ? -15.377 54.415  122.267 1.00 118.93 ?  247 VAL A O     1 
ATOM   611  C CB    . VAL A 1 266 ? -15.651 54.512  125.526 1.00 109.47 ?  247 VAL A CB    1 
ATOM   612  C CG1   . VAL A 1 266 ? -15.536 55.979  125.888 1.00 109.52 ?  247 VAL A CG1   1 
ATOM   613  C CG2   . VAL A 1 266 ? -16.143 53.707  126.713 1.00 112.78 ?  247 VAL A CG2   1 
ATOM   614  N N     . LEU A 1 267 ? -15.645 52.367  123.143 1.00 118.06 ?  248 LEU A N     1 
ATOM   615  C CA    . LEU A 1 267 ? -14.927 51.785  121.988 1.00 113.07 ?  248 LEU A CA    1 
ATOM   616  C C     . LEU A 1 267 ? -15.700 52.069  120.709 1.00 108.40 ?  248 LEU A C     1 
ATOM   617  O O     . LEU A 1 267 ? -15.082 52.478  119.755 1.00 114.27 ?  248 LEU A O     1 
ATOM   618  C CB    . LEU A 1 267 ? -14.798 50.282  122.159 1.00 108.83 ?  248 LEU A CB    1 
ATOM   619  C CG    . LEU A 1 267 ? -13.935 49.648  121.086 1.00 88.65  ?  248 LEU A CG    1 
ATOM   620  C CD1   . LEU A 1 267 ? -12.509 50.111  121.241 1.00 93.40  ?  248 LEU A CD1   1 
ATOM   621  C CD2   . LEU A 1 267 ? -13.999 48.151  121.196 1.00 98.36  ?  248 LEU A CD2   1 
ATOM   622  N N     . VAL A 1 268 ? -17.020 51.949  120.727 1.00 105.90 ?  249 VAL A N     1 
ATOM   623  C CA    . VAL A 1 268 ? -17.796 52.212  119.490 1.00 107.84 ?  249 VAL A CA    1 
ATOM   624  C C     . VAL A 1 268 ? -17.557 53.651  119.054 1.00 108.62 ?  249 VAL A C     1 
ATOM   625  O O     . VAL A 1 268 ? -17.329 53.867  117.877 1.00 112.87 ?  249 VAL A O     1 
ATOM   626  C CB    . VAL A 1 268 ? -19.290 52.001  119.735 1.00 111.38 ?  249 VAL A CB    1 
ATOM   627  C CG1   . VAL A 1 268 ? -20.109 52.927  118.867 1.00 109.17 ?  249 VAL A CG1   1 
ATOM   628  C CG2   . VAL A 1 268 ? -19.692 50.566  119.491 1.00 115.56 ?  249 VAL A CG2   1 
ATOM   629  N N     . HIS A 1 269 ? -17.563 54.598  119.977 1.00 109.27 ?  250 HIS A N     1 
ATOM   630  C CA    . HIS A 1 269 ? -17.305 55.987  119.555 1.00 109.84 ?  250 HIS A CA    1 
ATOM   631  C C     . HIS A 1 269 ? -15.901 56.050  118.970 1.00 111.87 ?  250 HIS A C     1 
ATOM   632  O O     . HIS A 1 269 ? -15.756 56.509  117.845 1.00 112.38 ?  250 HIS A O     1 
ATOM   633  C CB    . HIS A 1 269 ? -17.358 56.864  120.795 1.00 110.55 ?  250 HIS A CB    1 
ATOM   634  C CG    . HIS A 1 269 ? -17.539 58.307  120.509 1.00 110.93 ?  250 HIS A CG    1 
ATOM   635  N ND1   . HIS A 1 269 ? -18.663 58.792  119.903 1.00 110.59 ?  250 HIS A ND1   1 
ATOM   636  C CD2   . HIS A 1 269 ? -16.753 59.364  120.767 1.00 110.23 ?  250 HIS A CD2   1 
ATOM   637  C CE1   . HIS A 1 269 ? -18.559 60.092  119.778 1.00 110.57 ?  250 HIS A CE1   1 
ATOM   638  N NE2   . HIS A 1 269 ? -17.400 60.464  120.300 1.00 113.54 ?  250 HIS A NE2   1 
ATOM   639  N N     . ARG A 1 270 ? -14.940 55.455  119.661 1.00 111.12 ?  251 ARG A N     1 
ATOM   640  C CA    . ARG A 1 270 ? -13.529 55.498  119.220 1.00 113.79 ?  251 ARG A CA    1 
ATOM   641  C C     . ARG A 1 270 ? -13.399 54.935  117.806 1.00 114.05 ?  251 ARG A C     1 
ATOM   642  O O     . ARG A 1 270 ? -12.481 55.326  117.114 1.00 117.95 ?  251 ARG A O     1 
ATOM   643  C CB    . ARG A 1 270 ? -12.699 54.661  120.187 1.00 107.78 ?  251 ARG A CB    1 
ATOM   644  C CG    . ARG A 1 270 ? -11.727 55.453  121.039 1.00 104.93 ?  251 ARG A CG    1 
ATOM   645  C CD    . ARG A 1 270 ? -10.935 54.457  121.846 1.00 107.10 ?  251 ARG A CD    1 
ATOM   646  N NE    . ARG A 1 270 ? -9.508  54.574  121.641 1.00 108.59 ?  251 ARG A NE    1 
ATOM   647  C CZ    . ARG A 1 270 ? -8.629  53.729  122.142 1.00 109.21 ?  251 ARG A CZ    1 
ATOM   648  N NH1   . ARG A 1 270 ? -9.033  52.707  122.866 1.00 98.17  ?  251 ARG A NH1   1 
ATOM   649  N NH2   . ARG A 1 270 ? -7.343  53.898  121.927 1.00 116.39 ?  251 ARG A NH2   1 
ATOM   650  N N     . VAL A 1 271 ? -14.299 54.046  117.410 1.00 110.67 ?  252 VAL A N     1 
ATOM   651  C CA    . VAL A 1 271 ? -14.275 53.380  116.115 1.00 105.11 ?  252 VAL A CA    1 
ATOM   652  C C     . VAL A 1 271 ? -15.133 54.133  115.094 1.00 108.14 ?  252 VAL A C     1 
ATOM   653  O O     . VAL A 1 271 ? -14.663 54.446  113.994 1.00 110.56 ?  252 VAL A O     1 
ATOM   654  C CB    . VAL A 1 271 ? -14.687 51.907  116.294 1.00 101.05 ?  252 VAL A CB    1 
ATOM   655  C CG1   . VAL A 1 271 ? -15.166 51.303  115.001 1.00 110.05 ?  252 VAL A CG1   1 
ATOM   656  C CG2   . VAL A 1 271 ? -13.480 51.124  116.788 1.00 96.46  ?  252 VAL A CG2   1 
ATOM   657  N N     . HIS A 1 272 ? -16.377 54.489  115.445 1.00 107.07 ?  253 HIS A N     1 
ATOM   658  C CA    . HIS A 1 272 ? -17.188 55.307  114.540 1.00 102.90 ?  253 HIS A CA    1 
ATOM   659  C C     . HIS A 1 272 ? -16.499 56.623  114.210 1.00 106.25 ?  253 HIS A C     1 
ATOM   660  O O     . HIS A 1 272 ? -16.702 57.163  113.120 1.00 110.91 ?  253 HIS A O     1 
ATOM   661  C CB    . HIS A 1 272 ? -18.572 55.567  115.144 1.00 109.85 ?  253 HIS A CB    1 
ATOM   662  C CG    . HIS A 1 272 ? -19.486 56.408  114.297 1.00 109.93 ?  253 HIS A CG    1 
ATOM   663  N ND1   . HIS A 1 272 ? -19.436 57.786  114.280 1.00 115.41 ?  253 HIS A ND1   1 
ATOM   664  C CD2   . HIS A 1 272 ? -20.519 56.065  113.490 1.00 113.17 ?  253 HIS A CD2   1 
ATOM   665  C CE1   . HIS A 1 272 ? -20.374 58.253  113.471 1.00 119.24 ?  253 HIS A CE1   1 
ATOM   666  N NE2   . HIS A 1 272 ? -21.045 57.228  112.978 1.00 116.83 ?  253 HIS A NE2   1 
ATOM   667  N N     . SER A 1 273 ? -15.668 57.149  115.118 1.00 110.41 ?  254 SER A N     1 
ATOM   668  C CA    . SER A 1 273 ? -14.910 58.357  114.793 1.00 115.41 ?  254 SER A CA    1 
ATOM   669  C C     . SER A 1 273 ? -13.769 58.060  113.822 1.00 116.75 ?  254 SER A C     1 
ATOM   670  O O     . SER A 1 273 ? -13.685 58.685  112.759 1.00 121.43 ?  254 SER A O     1 
ATOM   671  C CB    . SER A 1 273 ? -14.394 59.039  116.058 1.00 110.60 ?  254 SER A CB    1 
ATOM   672  O OG    . SER A 1 273 ? -15.489 59.432  116.865 1.00 114.07 ?  254 SER A OG    1 
ATOM   673  N N     . TYR A 1 274 ? -12.891 57.103  114.153 1.00 111.92 ?  255 TYR A N     1 
ATOM   674  C CA    . TYR A 1 274 ? -11.818 56.730  113.227 1.00 110.25 ?  255 TYR A CA    1 
ATOM   675  C C     . TYR A 1 274 ? -12.325 56.472  111.807 1.00 107.18 ?  255 TYR A C     1 
ATOM   676  O O     . TYR A 1 274 ? -11.615 56.757  110.838 1.00 107.85 ?  255 TYR A O     1 
ATOM   677  C CB    . TYR A 1 274 ? -11.066 55.505  113.744 1.00 111.98 ?  255 TYR A CB    1 
ATOM   678  C CG    . TYR A 1 274 ? -10.288 54.735  112.681 1.00 111.65 ?  255 TYR A CG    1 
ATOM   679  C CD1   . TYR A 1 274 ? -9.019  55.144  112.255 1.00 113.12 ?  255 TYR A CD1   1 
ATOM   680  C CD2   . TYR A 1 274 ? -10.843 53.586  112.095 1.00 109.70 ?  255 TYR A CD2   1 
ATOM   681  C CE1   . TYR A 1 274 ? -8.314  54.407  111.271 1.00 117.84 ?  255 TYR A CE1   1 
ATOM   682  C CE2   . TYR A 1 274 ? -10.164 52.844  111.121 1.00 113.70 ?  255 TYR A CE2   1 
ATOM   683  C CZ    . TYR A 1 274 ? -8.896  53.252  110.705 1.00 123.03 ?  255 TYR A CZ    1 
ATOM   684  O OH    . TYR A 1 274 ? -8.235  52.501  109.723 1.00 120.14 ?  255 TYR A OH    1 
ATOM   685  N N     . LEU A 1 275 ? -13.541 55.938  111.652 1.00 102.92 ?  256 LEU A N     1 
ATOM   686  C CA    . LEU A 1 275 ? -14.059 55.740  110.301 1.00 98.11  ?  256 LEU A CA    1 
ATOM   687  C C     . LEU A 1 275 ? -14.495 57.059  109.679 1.00 105.40 ?  256 LEU A C     1 
ATOM   688  O O     . LEU A 1 275 ? -13.914 57.513  108.687 1.00 111.53 ?  256 LEU A O     1 
ATOM   689  C CB    . LEU A 1 275 ? -15.208 54.736  110.278 1.00 93.91  ?  256 LEU A CB    1 
ATOM   690  C CG    . LEU A 1 275 ? -14.905 53.362  110.888 1.00 99.31  ?  256 LEU A CG    1 
ATOM   691  C CD1   . LEU A 1 275 ? -16.107 52.439  110.701 1.00 98.05  ?  256 LEU A CD1   1 
ATOM   692  C CD2   . LEU A 1 275 ? -13.600 52.717  110.376 1.00 94.20  ?  256 LEU A CD2   1 
ATOM   693  N N     . GLU A 1 276 ? -15.513 57.699  110.254 1.00 108.15 ?  257 GLU A N     1 
ATOM   694  C CA    . GLU A 1 276 ? -16.023 58.962  109.711 1.00 114.15 ?  257 GLU A CA    1 
ATOM   695  C C     . GLU A 1 276 ? -14.906 59.990  109.480 1.00 110.06 ?  257 GLU A C     1 
ATOM   696  O O     . GLU A 1 276 ? -14.978 60.791  108.532 1.00 101.20 ?  257 GLU A O     1 
ATOM   697  C CB    . GLU A 1 276 ? -17.111 59.477  110.672 1.00 114.93 ?  257 GLU A CB    1 
ATOM   698  C CG    . GLU A 1 276 ? -18.032 60.600  110.188 1.00 119.38 ?  257 GLU A CG    1 
ATOM   699  C CD    . GLU A 1 276 ? -19.095 60.942  111.242 1.00 120.92 ?  257 GLU A CD    1 
ATOM   700  O OE1   . GLU A 1 276 ? -18.771 60.871  112.448 1.00 121.99 ?  257 GLU A OE1   1 
ATOM   701  O OE2   . GLU A 1 276 ? -20.263 61.228  110.868 1.00 120.10 ?  257 GLU A OE2   1 
ATOM   702  N N     . ARG A 1 277 ? -13.841 59.924  110.297 1.00 108.38 ?  258 ARG A N     1 
ATOM   703  C CA    . ARG A 1 277 ? -12.749 60.893  110.253 1.00 106.04 ?  258 ARG A CA    1 
ATOM   704  C C     . ARG A 1 277 ? -11.834 60.657  109.067 1.00 103.91 ?  258 ARG A C     1 
ATOM   705  O O     . ARG A 1 277 ? -11.495 61.594  108.338 1.00 105.69 ?  258 ARG A O     1 
ATOM   706  C CB    . ARG A 1 277 ? -11.947 60.837  111.554 1.00 109.23 ?  258 ARG A CB    1 
ATOM   707  C CG    . ARG A 1 277 ? -10.659 61.647  111.557 1.00 105.82 ?  258 ARG A CG    1 
ATOM   708  C CD    . ARG A 1 277 ? -10.921 63.043  111.082 1.00 105.88 ?  258 ARG A CD    1 
ATOM   709  N NE    . ARG A 1 277 ? -11.847 63.810  111.910 1.00 98.09  ?  258 ARG A NE    1 
ATOM   710  C CZ    . ARG A 1 277 ? -11.455 64.723  112.785 1.00 96.14  ?  258 ARG A CZ    1 
ATOM   711  N NH1   . ARG A 1 277 ? -10.158 64.977  112.933 1.00 94.59  ?  258 ARG A NH1   1 
ATOM   712  N NH2   . ARG A 1 277 ? -12.357 65.398  113.486 1.00 99.43  ?  258 ARG A NH2   1 
ATOM   713  N N     . HIS A 1 278 ? -11.380 59.432  108.876 1.00 103.37 ?  259 HIS A N     1 
ATOM   714  C CA    . HIS A 1 278 ? -10.621 59.141  107.672 1.00 109.02 ?  259 HIS A CA    1 
ATOM   715  C C     . HIS A 1 278 ? -11.513 58.752  106.503 1.00 106.76 ?  259 HIS A C     1 
ATOM   716  O O     . HIS A 1 278 ? -11.029 58.129  105.547 1.00 98.49  ?  259 HIS A O     1 
ATOM   717  C CB    . HIS A 1 278 ? -9.589  58.058  107.945 1.00 116.49 ?  259 HIS A CB    1 
ATOM   718  C CG    . HIS A 1 278 ? -8.553  58.463  108.940 1.00 119.90 ?  259 HIS A CG    1 
ATOM   719  N ND1   . HIS A 1 278 ? -8.850  58.741  110.257 1.00 117.54 ?  259 HIS A ND1   1 
ATOM   720  C CD2   . HIS A 1 278 ? -7.216  58.636  108.807 1.00 124.17 ?  259 HIS A CD2   1 
ATOM   721  C CE1   . HIS A 1 278 ? -7.738  59.064  110.894 1.00 121.02 ?  259 HIS A CE1   1 
ATOM   722  N NE2   . HIS A 1 278 ? -6.732  59.005  110.037 1.00 126.36 ?  259 HIS A NE2   1 
ATOM   723  N N     . GLY A 1 279 ? -12.798 59.101  106.575 1.00 110.61 ?  260 GLY A N     1 
ATOM   724  C CA    . GLY A 1 279 ? -13.734 58.961  105.468 1.00 105.21 ?  260 GLY A CA    1 
ATOM   725  C C     . GLY A 1 279 ? -13.868 57.560  104.914 1.00 104.07 ?  260 GLY A C     1 
ATOM   726  O O     . GLY A 1 279 ? -13.948 57.392  103.690 1.00 108.63 ?  260 GLY A O     1 
ATOM   727  N N     . LEU A 1 280 ? -13.849 56.541  105.778 1.00 97.74  ?  261 LEU A N     1 
ATOM   728  C CA    . LEU A 1 280 ? -14.290 55.212  105.382 1.00 96.04  ?  261 LEU A CA    1 
ATOM   729  C C     . LEU A 1 280 ? -15.795 55.059  105.513 1.00 100.21 ?  261 LEU A C     1 
ATOM   730  O O     . LEU A 1 280 ? -16.352 54.060  105.043 1.00 102.75 ?  261 LEU A O     1 
ATOM   731  C CB    . LEU A 1 280 ? -13.551 54.146  106.195 1.00 87.37  ?  261 LEU A CB    1 
ATOM   732  C CG    . LEU A 1 280 ? -12.050 54.066  105.894 1.00 90.99  ?  261 LEU A CG    1 
ATOM   733  C CD1   . LEU A 1 280 ? -11.276 53.283  106.935 1.00 98.19  ?  261 LEU A CD1   1 
ATOM   734  C CD2   . LEU A 1 280 ? -11.837 53.409  104.526 1.00 97.57  ?  261 LEU A CD2   1 
ATOM   735  N N     . ILE A 1 281 ? -16.457 56.039  106.131 1.00 104.61 ?  262 ILE A N     1 
ATOM   736  C CA    . ILE A 1 281 ? -17.908 56.157  106.153 1.00 109.33 ?  262 ILE A CA    1 
ATOM   737  C C     . ILE A 1 281 ? -18.257 57.632  106.032 1.00 110.70 ?  262 ILE A C     1 
ATOM   738  O O     . ILE A 1 281 ? -17.460 58.520  106.359 1.00 109.44 ?  262 ILE A O     1 
ATOM   739  C CB    . ILE A 1 281 ? -18.562 55.569  107.432 1.00 112.71 ?  262 ILE A CB    1 
ATOM   740  C CG1   . ILE A 1 281 ? -18.139 56.337  108.686 1.00 106.00 ?  262 ILE A CG1   1 
ATOM   741  C CG2   . ILE A 1 281 ? -18.241 54.092  107.599 1.00 115.68 ?  262 ILE A CG2   1 
ATOM   742  C CD1   . ILE A 1 281 ? -18.854 55.881  109.896 1.00 103.64 ?  262 ILE A CD1   1 
ATOM   743  N N     . ASN A 1 282 ? -19.465 57.879  105.542 1.00 111.73 ?  263 ASN A N     1 
ATOM   744  C CA    . ASN A 1 282 ? -20.017 59.222  105.462 1.00 113.35 ?  263 ASN A CA    1 
ATOM   745  C C     . ASN A 1 282 ? -19.081 60.141  104.674 1.00 115.09 ?  263 ASN A C     1 
ATOM   746  O O     . ASN A 1 282 ? -18.595 61.169  105.165 1.00 111.97 ?  263 ASN A O     1 
ATOM   747  C CB    . ASN A 1 282 ? -20.294 59.738  106.866 1.00 113.27 ?  263 ASN A CB    1 
ATOM   748  C CG    . ASN A 1 282 ? -21.342 58.911  107.563 1.00 116.91 ?  263 ASN A CG    1 
ATOM   749  O OD1   . ASN A 1 282 ? -22.335 58.510  106.948 1.00 118.01 ?  263 ASN A OD1   1 
ATOM   750  N ND2   . ASN A 1 282 ? -21.108 58.602  108.838 1.00 120.73 ?  263 ASN A ND2   1 
ATOM   751  N N     . PHE A 1 283 ? -18.796 59.688  103.441 1.00 116.52 ?  264 PHE A N     1 
ATOM   752  C CA    . PHE A 1 283 ? -18.125 60.435  102.376 1.00 117.26 ?  264 PHE A CA    1 
ATOM   753  C C     . PHE A 1 283 ? -19.011 60.470  101.135 1.00 112.60 ?  264 PHE A C     1 
ATOM   754  O O     . PHE A 1 283 ? -19.723 59.506  100.832 1.00 113.89 ?  264 PHE A O     1 
ATOM   755  C CB    . PHE A 1 283 ? -16.733 59.833  102.012 1.00 109.77 ?  264 PHE A CB    1 
ATOM   756  C CG    . PHE A 1 283 ? -16.789 58.392  101.537 1.00 115.10 ?  264 PHE A CG    1 
ATOM   757  C CD1   . PHE A 1 283 ? -16.960 58.076  100.194 1.00 111.76 ?  264 PHE A CD1   1 
ATOM   758  C CD2   . PHE A 1 283 ? -16.625 57.343  102.445 1.00 117.04 ?  264 PHE A CD2   1 
ATOM   759  C CE1   . PHE A 1 283 ? -17.011 56.737  99.762  1.00 110.21 ?  264 PHE A CE1   1 
ATOM   760  C CE2   . PHE A 1 283 ? -16.655 55.997  102.021 1.00 116.17 ?  264 PHE A CE2   1 
ATOM   761  C CZ    . PHE A 1 283 ? -16.851 55.700  100.678 1.00 113.49 ?  264 PHE A CZ    1 
ATOM   762  N N     . GLY A 1 284 ? -18.979 61.590  100.429 1.00 104.83 ?  265 GLY A N     1 
ATOM   763  C CA    . GLY A 1 284 ? -19.737 61.678  99.200  1.00 107.18 ?  265 GLY A CA    1 
ATOM   764  C C     . GLY A 1 284 ? -20.920 62.620  99.212  1.00 111.73 ?  265 GLY A C     1 
ATOM   765  O O     . GLY A 1 284 ? -20.815 63.772  99.648  1.00 114.28 ?  265 GLY A O     1 
ATOM   766  N N     . ILE A 1 285 ? -22.051 62.138  98.718  1.00 112.31 ?  266 ILE A N     1 
ATOM   767  C CA    . ILE A 1 285 ? -23.273 62.930  98.632  1.00 116.47 ?  266 ILE A CA    1 
ATOM   768  C C     . ILE A 1 285 ? -24.351 62.187  99.413  1.00 124.44 ?  266 ILE A C     1 
ATOM   769  O O     . ILE A 1 285 ? -25.101 61.363  98.865  1.00 122.66 ?  266 ILE A O     1 
ATOM   770  C CB    . ILE A 1 285 ? -23.694 63.185  97.192  1.00 107.50 ?  266 ILE A CB    1 
ATOM   771  C CG1   . ILE A 1 285 ? -22.584 63.957  96.509  1.00 108.72 ?  266 ILE A CG1   1 
ATOM   772  C CG2   . ILE A 1 285 ? -24.985 63.992  97.160  1.00 111.41 ?  266 ILE A CG2   1 
ATOM   773  C CD1   . ILE A 1 285 ? -22.889 64.262  95.096  1.00 113.97 ?  266 ILE A CD1   1 
ATOM   774  N N     . TYR A 1 286 ? -24.447 62.513  100.703 1.00 122.15 ?  267 TYR A N     1 
ATOM   775  C CA    . TYR A 1 286 ? -25.345 61.870  101.649 1.00 121.92 ?  267 TYR A CA    1 
ATOM   776  C C     . TYR A 1 286 ? -26.126 62.939  102.388 1.00 123.20 ?  267 TYR A C     1 
ATOM   777  O O     . TYR A 1 286 ? -25.573 63.994  102.713 1.00 126.65 ?  267 TYR A O     1 
ATOM   778  C CB    . TYR A 1 286 ? -24.534 60.951  102.574 1.00 122.10 ?  267 TYR A CB    1 
ATOM   779  C CG    . TYR A 1 286 ? -23.424 61.645  103.337 1.00 120.74 ?  267 TYR A CG    1 
ATOM   780  C CD1   . TYR A 1 286 ? -22.187 61.830  102.725 1.00 120.45 ?  267 TYR A CD1   1 
ATOM   781  C CD2   . TYR A 1 286 ? -23.540 61.986  104.680 1.00 114.38 ?  267 TYR A CD2   1 
ATOM   782  C CE1   . TYR A 1 286 ? -21.135 62.435  103.376 1.00 118.62 ?  267 TYR A CE1   1 
ATOM   783  C CE2   . TYR A 1 286 ? -22.465 62.580  105.353 1.00 114.25 ?  267 TYR A CE2   1 
ATOM   784  C CZ    . TYR A 1 286 ? -21.262 62.798  104.687 1.00 112.90 ?  267 TYR A CZ    1 
ATOM   785  O OH    . TYR A 1 286 ? -20.165 63.380  105.290 1.00 108.32 ?  267 TYR A OH    1 
ATOM   786  N N     . LYS A 1 287 ? -27.431 62.696  102.568 1.00 127.51 ?  268 LYS A N     1 
ATOM   787  C CA    . LYS A 1 287 ? -28.279 63.631  103.297 1.00 130.47 ?  268 LYS A CA    1 
ATOM   788  C C     . LYS A 1 287 ? -27.894 63.580  104.761 1.00 127.79 ?  268 LYS A C     1 
ATOM   789  O O     . LYS A 1 287 ? -27.821 62.501  105.358 1.00 124.22 ?  268 LYS A O     1 
ATOM   790  C CB    . LYS A 1 287 ? -29.774 63.325  103.098 1.00 129.19 ?  268 LYS A CB    1 
ATOM   791  C CG    . LYS A 1 287 ? -30.285 63.738  101.689 1.00 140.77 ?  268 LYS A CG    1 
ATOM   792  C CD    . LYS A 1 287 ? -31.801 63.575  101.431 1.00 144.33 ?  268 LYS A CD    1 
ATOM   793  C CE    . LYS A 1 287 ? -32.156 64.042  99.992  1.00 135.56 ?  268 LYS A CE    1 
ATOM   794  N NZ    . LYS A 1 287 ? -33.596 63.893  99.597  1.00 128.81 ?  268 LYS A NZ    1 
ATOM   795  N N     . ARG A 1 288 ? -27.587 64.749  105.313 1.00 131.99 ?  269 ARG A N     1 
ATOM   796  C CA    . ARG A 1 288 ? -26.978 64.837  106.630 1.00 134.59 ?  269 ARG A CA    1 
ATOM   797  C C     . ARG A 1 288 ? -28.028 64.764  107.729 1.00 137.53 ?  269 ARG A C     1 
ATOM   798  O O     . ARG A 1 288 ? -29.026 65.493  107.692 1.00 140.15 ?  269 ARG A O     1 
ATOM   799  C CB    . ARG A 1 288 ? -26.176 66.128  106.756 1.00 133.16 ?  269 ARG A CB    1 
ATOM   800  C CG    . ARG A 1 288 ? -25.352 66.160  108.027 1.00 135.70 ?  269 ARG A CG    1 
ATOM   801  C CD    . ARG A 1 288 ? -24.456 67.366  108.054 1.00 138.93 ?  269 ARG A CD    1 
ATOM   802  N NE    . ARG A 1 288 ? -23.551 67.363  106.917 1.00 145.25 ?  269 ARG A NE    1 
ATOM   803  C CZ    . ARG A 1 288 ? -22.347 66.798  106.933 1.00 138.48 ?  269 ARG A CZ    1 
ATOM   804  N NH1   . ARG A 1 288 ? -21.906 66.196  108.040 1.00 130.23 ?  269 ARG A NH1   1 
ATOM   805  N NH2   . ARG A 1 288 ? -21.581 66.838  105.842 1.00 140.52 ?  269 ARG A NH2   1 
ATOM   806  N N     . ILE A 1 289 ? -27.795 63.893  108.717 1.00 135.60 ?  270 ILE A N     1 
ATOM   807  C CA    . ILE A 1 289 ? -28.677 63.799  109.877 1.00 136.06 ?  270 ILE A CA    1 
ATOM   808  C C     . ILE A 1 289 ? -28.428 64.962  110.831 1.00 139.22 ?  270 ILE A C     1 
ATOM   809  O O     . ILE A 1 289 ? -29.274 65.855  110.956 1.00 140.49 ?  270 ILE A O     1 
ATOM   810  C CB    . ILE A 1 289 ? -28.529 62.455  110.605 1.00 130.76 ?  270 ILE A CB    1 
ATOM   811  C CG1   . ILE A 1 289 ? -29.006 61.316  109.698 1.00 133.11 ?  270 ILE A CG1   1 
ATOM   812  C CG2   . ILE A 1 289 ? -29.311 62.492  111.894 1.00 130.37 ?  270 ILE A CG2   1 
ATOM   813  C CD1   . ILE A 1 289 ? -29.052 59.932  110.371 1.00 136.30 ?  270 ILE A CD1   1 
ATOM   814  N N     . LYS A 1 290 ? -27.271 64.959  111.516 1.00 137.50 ?  271 LYS A N     1 
ATOM   815  C CA    . LYS A 1 290 ? -26.875 66.058  112.398 1.00 139.72 ?  271 LYS A CA    1 
ATOM   816  C C     . LYS A 1 290 ? -26.468 67.277  111.572 1.00 144.32 ?  271 LYS A C     1 
ATOM   817  O O     . LYS A 1 290 ? -25.353 67.288  111.034 1.00 145.93 ?  271 LYS A O     1 
ATOM   818  C CB    . LYS A 1 290 ? -25.708 65.638  113.300 1.00 138.89 ?  271 LYS A CB    1 
ATOM   819  C CG    . LYS A 1 290 ? -25.910 64.354  114.101 1.00 133.94 ?  271 LYS A CG    1 
ATOM   820  C CD    . LYS A 1 290 ? -24.652 64.012  114.904 1.00 131.55 ?  271 LYS A CD    1 
ATOM   821  C CE    . LYS A 1 290 ? -24.856 62.775  115.764 1.00 133.82 ?  271 LYS A CE    1 
ATOM   822  N NZ    . LYS A 1 290 ? -25.860 63.052  116.826 1.00 141.19 ?  271 LYS A NZ    1 
ATOM   823  N N     . PRO A 1 291 ? -27.307 68.319  111.456 1.00 147.61 ?  272 PRO A N     1 
ATOM   824  C CA    . PRO A 1 291 ? -27.025 69.385  110.475 1.00 148.16 ?  272 PRO A CA    1 
ATOM   825  C C     . PRO A 1 291 ? -25.718 70.115  110.780 1.00 147.92 ?  272 PRO A C     1 
ATOM   826  O O     . PRO A 1 291 ? -25.193 70.066  111.898 1.00 146.09 ?  272 PRO A O     1 
ATOM   827  C CB    . PRO A 1 291 ? -28.238 70.320  110.602 1.00 144.35 ?  272 PRO A CB    1 
ATOM   828  C CG    . PRO A 1 291 ? -29.329 69.457  111.198 1.00 141.06 ?  272 PRO A CG    1 
ATOM   829  C CD    . PRO A 1 291 ? -28.596 68.536  112.144 1.00 141.17 ?  272 PRO A CD    1 
ATOM   830  N N     . LEU A 1 292 ? -25.189 70.796  109.753 1.00 146.67 ?  273 LEU A N     1 
ATOM   831  C CA    . LEU A 1 292 ? -23.843 71.366  109.826 1.00 148.03 ?  273 LEU A CA    1 
ATOM   832  C C     . LEU A 1 292 ? -23.725 72.391  110.956 1.00 147.38 ?  273 LEU A C     1 
ATOM   833  O O     . LEU A 1 292 ? -24.672 73.139  111.223 1.00 145.31 ?  273 LEU A O     1 
ATOM   834  C CB    . LEU A 1 292 ? -23.448 72.029  108.504 1.00 144.15 ?  273 LEU A CB    1 
ATOM   835  C CG    . LEU A 1 292 ? -22.898 71.172  107.362 1.00 137.72 ?  273 LEU A CG    1 
ATOM   836  C CD1   . LEU A 1 292 ? -22.675 72.043  106.141 1.00 134.90 ?  273 LEU A CD1   1 
ATOM   837  C CD2   . LEU A 1 292 ? -21.602 70.451  107.755 1.00 128.99 ?  273 LEU A CD2   1 
ATOM   838  N N     . PRO A 1 293 ? -22.558 72.460  111.616 1.00 151.46 ?  274 PRO A N     1 
ATOM   839  C CA    . PRO A 1 293 ? -22.400 73.372  112.762 1.00 156.55 ?  274 PRO A CA    1 
ATOM   840  C C     . PRO A 1 293 ? -22.593 74.836  112.383 1.00 157.81 ?  274 PRO A C     1 
ATOM   841  O O     . PRO A 1 293 ? -22.165 75.297  111.318 1.00 153.21 ?  274 PRO A O     1 
ATOM   842  C CB    . PRO A 1 293 ? -20.967 73.101  113.250 1.00 152.27 ?  274 PRO A CB    1 
ATOM   843  C CG    . PRO A 1 293 ? -20.619 71.754  112.718 1.00 152.27 ?  274 PRO A CG    1 
ATOM   844  C CD    . PRO A 1 293 ? -21.365 71.618  111.413 1.00 148.53 ?  274 PRO A CD    1 
ATOM   845  N N     . THR A 1 294 ? -23.252 75.562  113.292 1.00 159.42 ?  275 THR A N     1 
ATOM   846  C CA    . THR A 1 294 ? -23.613 76.952  113.047 1.00 156.75 ?  275 THR A CA    1 
ATOM   847  C C     . THR A 1 294 ? -22.391 77.777  112.636 1.00 153.72 ?  275 THR A C     1 
ATOM   848  O O     . THR A 1 294 ? -22.384 78.424  111.578 1.00 144.33 ?  275 THR A O     1 
ATOM   849  C CB    . THR A 1 294 ? -24.322 77.502  114.301 1.00 157.30 ?  275 THR A CB    1 
ATOM   850  O OG1   . THR A 1 294 ? -24.754 78.855  114.089 1.00 165.36 ?  275 THR A OG1   1 
ATOM   851  C CG2   . THR A 1 294 ? -23.474 77.352  115.597 1.00 149.88 ?  275 THR A CG2   1 
ATOM   852  N N     . LYS A 1 295 ? -21.260 77.595  113.325 1.00 152.95 ?  276 LYS A N     1 
ATOM   853  C CA    . LYS A 1 295 ? -20.043 78.408  113.087 1.00 147.74 ?  276 LYS A CA    1 
ATOM   854  C C     . LYS A 1 295 ? -18.847 77.484  112.908 1.00 134.71 ?  276 LYS A C     1 
ATOM   855  O O     . LYS A 1 295 ? -18.513 76.740  113.823 1.00 131.36 ?  276 LYS A O     1 
ATOM   856  C CB    . LYS A 1 295 ? -19.807 79.363  114.258 1.00 151.56 ?  276 LYS A CB    1 
ATOM   857  C CG    . LYS A 1 295 ? -19.350 80.767  113.879 1.00 148.04 ?  276 LYS A CG    1 
ATOM   858  C CD    . LYS A 1 295 ? -20.155 81.871  114.543 1.00 140.91 ?  276 LYS A CD    1 
ATOM   859  C CE    . LYS A 1 295 ? -21.167 81.359  115.548 1.00 146.42 ?  276 LYS A CE    1 
ATOM   860  N NZ    . LYS A 1 295 ? -22.188 82.379  115.884 1.00 153.47 ?  276 LYS A NZ    1 
ATOM   861  N N     . LYS A 1 296 ? -18.219 77.590  111.751 1.00 122.63 ?  277 LYS A N     1 
ATOM   862  C CA    . LYS A 1 296 ? -17.078 76.739  111.367 1.00 115.20 ?  277 LYS A CA    1 
ATOM   863  C C     . LYS A 1 296 ? -15.814 77.204  112.071 1.00 106.83 ?  277 LYS A C     1 
ATOM   864  O O     . LYS A 1 296 ? -15.774 78.326  112.525 1.00 113.62 ?  277 LYS A O     1 
ATOM   865  C CB    . LYS A 1 296 ? -16.923 76.826  109.851 1.00 120.15 ?  277 LYS A CB    1 
ATOM   866  C CG    . LYS A 1 296 ? -18.237 76.811  109.082 1.00 121.81 ?  277 LYS A CG    1 
ATOM   867  C CD    . LYS A 1 296 ? -18.428 77.988  108.162 1.00 120.45 ?  277 LYS A CD    1 
ATOM   868  C CE    . LYS A 1 296 ? -19.876 78.183  107.771 1.00 128.74 ?  277 LYS A CE    1 
ATOM   869  N NZ    . LYS A 1 296 ? -20.644 76.922  107.884 1.00 127.42 ?  277 LYS A NZ    1 
ATOM   870  N N     . THR A 1 297 ? -14.823 76.334  112.136 1.00 102.41 ?  278 THR A N     1 
ATOM   871  C CA    . THR A 1 297 ? -13.538 76.678  112.764 1.00 104.32 ?  278 THR A CA    1 
ATOM   872  C C     . THR A 1 297 ? -12.444 76.425  111.747 1.00 106.27 ?  278 THR A C     1 
ATOM   873  O O     . THR A 1 297 ? -12.555 75.439  111.069 1.00 111.63 ?  278 THR A O     1 
ATOM   874  C CB    . THR A 1 297 ? -13.180 75.624  113.802 1.00 101.82 ?  278 THR A CB    1 
ATOM   875  O OG1   . THR A 1 297 ? -14.367 75.374  114.543 1.00 110.19 ?  278 THR A OG1   1 
ATOM   876  C CG2   . THR A 1 297 ? -12.072 76.077  114.721 1.00 101.79 ?  278 THR A CG2   1 
ATOM   877  N N     . GLY A 1 298 ? -11.485 77.331  111.592 1.00 106.65 ?  279 GLY A N     1 
ATOM   878  C CA    . GLY A 1 298 ? -10.334 77.116  110.694 1.00 99.51  ?  279 GLY A CA    1 
ATOM   879  C C     . GLY A 1 298 ? -10.590 77.452  109.242 1.00 106.36 ?  279 GLY A C     1 
ATOM   880  O O     . GLY A 1 298 ? -11.672 77.179  108.739 1.00 109.01 ?  279 GLY A O     1 
ATOM   881  N N     . LYS A 1 299 ? -9.591  78.004  108.565 1.00 105.19 ?  280 LYS A N     1 
ATOM   882  C CA    . LYS A 1 299 ? -9.776  78.315  107.153 1.00 101.64 ?  280 LYS A CA    1 
ATOM   883  C C     . LYS A 1 299 ? -8.836  77.461  106.329 1.00 107.79 ?  280 LYS A C     1 
ATOM   884  O O     . LYS A 1 299 ? -7.633  77.413  106.621 1.00 105.60 ?  280 LYS A O     1 
ATOM   885  C CB    . LYS A 1 299 ? -9.498  79.782  106.862 1.00 99.80  ?  280 LYS A CB    1 
ATOM   886  C CG    . LYS A 1 299 ? -9.576  80.130  105.393 1.00 104.42 ?  280 LYS A CG    1 
ATOM   887  C CD    . LYS A 1 299 ? -11.013 80.072  104.891 1.00 109.26 ?  280 LYS A CD    1 
ATOM   888  C CE    . LYS A 1 299 ? -11.161 80.772  103.538 1.00 104.57 ?  280 LYS A CE    1 
ATOM   889  N NZ    . LYS A 1 299 ? -12.598 80.912  103.161 1.00 105.24 ?  280 LYS A NZ    1 
ATOM   890  N N     . VAL A 1 300 ? -9.384  76.804  105.301 1.00 107.82 ?  281 VAL A N     1 
ATOM   891  C CA    . VAL A 1 300 ? -8.616  75.980  104.373 1.00 99.04  ?  281 VAL A CA    1 
ATOM   892  C C     . VAL A 1 300 ? -8.897  76.411  102.946 1.00 100.71 ?  281 VAL A C     1 
ATOM   893  O O     . VAL A 1 300 ? -10.028 76.273  102.450 1.00 100.69 ?  281 VAL A O     1 
ATOM   894  C CB    . VAL A 1 300 ? -8.893  74.490  104.544 1.00 97.36  ?  281 VAL A CB    1 
ATOM   895  C CG1   . VAL A 1 300 ? -8.218  73.753  103.442 1.00 98.33  ?  281 VAL A CG1   1 
ATOM   896  C CG2   . VAL A 1 300 ? -8.275  74.039  105.847 1.00 95.49  ?  281 VAL A CG2   1 
ATOM   897  N N     . ILE A 1 301 ? -7.866  76.948  102.300 1.00 100.66 ?  282 ILE A N     1 
ATOM   898  C CA    . ILE A 1 301 ? -7.807  77.097  100.854 1.00 93.43  ?  282 ILE A CA    1 
ATOM   899  C C     . ILE A 1 301 ? -7.355  75.789  100.227 1.00 96.95  ?  282 ILE A C     1 
ATOM   900  O O     . ILE A 1 301 ? -6.336  75.206  100.630 1.00 92.79  ?  282 ILE A O     1 
ATOM   901  C CB    . ILE A 1 301 ? -6.890  78.272  100.472 1.00 90.09  ?  282 ILE A CB    1 
ATOM   902  C CG1   . ILE A 1 301 ? -7.617  79.601  100.708 1.00 92.35  ?  282 ILE A CG1   1 
ATOM   903  C CG2   . ILE A 1 301 ? -6.233  78.096  99.147  1.00 93.46  ?  282 ILE A CG2   1 
ATOM   904  C CD1   . ILE A 1 301 ? -8.889  79.737  99.881  1.00 89.47  ?  282 ILE A CD1   1 
ATOM   905  N N     . ILE A 1 302 ? -8.161  75.308  99.271  1.00 102.73 ?  283 ILE A N     1 
ATOM   906  C CA    . ILE A 1 302 ? -7.884  74.156  98.407  1.00 95.87  ?  283 ILE A CA    1 
ATOM   907  C C     . ILE A 1 302 ? -7.530  74.644  97.010  1.00 91.08  ?  283 ILE A C     1 
ATOM   908  O O     . ILE A 1 302 ? -8.365  75.242  96.321  1.00 90.66  ?  283 ILE A O     1 
ATOM   909  C CB    . ILE A 1 302 ? -9.074  73.187  98.349  1.00 89.81  ?  283 ILE A CB    1 
ATOM   910  C CG1   . ILE A 1 302 ? -9.145  72.358  99.622  1.00 90.10  ?  283 ILE A CG1   1 
ATOM   911  C CG2   . ILE A 1 302 ? -9.045  72.358  97.100  1.00 94.00  ?  283 ILE A CG2   1 
ATOM   912  C CD1   . ILE A 1 302 ? -10.268 71.365  99.601  1.00 94.03  ?  283 ILE A CD1   1 
ATOM   913  N N     . ILE A 1 303 ? -6.296  74.364  96.595  1.00 89.76  ?  284 ILE A N     1 
ATOM   914  C CA    . ILE A 1 303 ? -5.799  74.703  95.266  1.00 91.84  ?  284 ILE A CA    1 
ATOM   915  C C     . ILE A 1 303 ? -6.282  73.647  94.280  1.00 91.13  ?  284 ILE A C     1 
ATOM   916  O O     . ILE A 1 303 ? -5.717  72.553  94.208  1.00 93.16  ?  284 ILE A O     1 
ATOM   917  C CB    . ILE A 1 303 ? -4.272  74.776  95.240  1.00 90.33  ?  284 ILE A CB    1 
ATOM   918  C CG1   . ILE A 1 303 ? -3.737  75.895  96.134  1.00 83.57  ?  284 ILE A CG1   1 
ATOM   919  C CG2   . ILE A 1 303 ? -3.832  74.956  93.815  1.00 90.77  ?  284 ILE A CG2   1 
ATOM   920  C CD1   . ILE A 1 303 ? -2.203  75.909  96.211  1.00 74.90  ?  284 ILE A CD1   1 
ATOM   921  N N     . GLY A 1 304 ? -7.300  73.980  93.497  1.00 88.90  ?  285 GLY A N     1 
ATOM   922  C CA    . GLY A 1 304 ? -7.760  73.079  92.458  1.00 94.32  ?  285 GLY A CA    1 
ATOM   923  C C     . GLY A 1 304 ? -9.053  72.382  92.808  1.00 92.36  ?  285 GLY A C     1 
ATOM   924  O O     . GLY A 1 304 ? -9.113  71.673  93.813  1.00 92.38  ?  285 GLY A O     1 
ATOM   925  N N     . SER A 1 305 ? -10.022 72.623  91.946  1.00 93.99  ?  286 SER A N     1 
ATOM   926  C CA    . SER A 1 305 ? -11.357 72.027  92.060  1.00 95.05  ?  286 SER A CA    1 
ATOM   927  C C     . SER A 1 305 ? -11.257 70.686  91.374  1.00 98.21  ?  286 SER A C     1 
ATOM   928  O O     . SER A 1 305 ? -12.185 70.324  90.716  1.00 97.74  ?  286 SER A O     1 
ATOM   929  C CB    . SER A 1 305 ? -12.356 72.870  91.381  1.00 93.53  ?  286 SER A CB    1 
ATOM   930  O OG    . SER A 1 305 ? -13.431 72.074  90.939  1.00 98.18  ?  286 SER A OG    1 
ATOM   931  N N     . GLY A 1 306 ? -10.146 69.997  91.571  1.00 98.49  ?  287 GLY A N     1 
ATOM   932  C CA    . GLY A 1 306 ? -9.928  68.661  91.000  1.00 99.15  ?  287 GLY A CA    1 
ATOM   933  C C     . GLY A 1 306 ? -10.649 67.604  91.802  1.00 94.97  ?  287 GLY A C     1 
ATOM   934  O O     . GLY A 1 306 ? -11.116 67.889  92.890  1.00 93.69  ?  287 GLY A O     1 
ATOM   935  N N     . VAL A 1 307 ? -10.669 66.376  91.312  1.00 99.64  ?  288 VAL A N     1 
ATOM   936  C CA    . VAL A 1 307 ? -11.403 65.307  92.038  1.00 98.79  ?  288 VAL A CA    1 
ATOM   937  C C     . VAL A 1 307 ? -10.796 65.135  93.417  1.00 101.63 ?  288 VAL A C     1 
ATOM   938  O O     . VAL A 1 307 ? -11.556 65.055  94.360  1.00 99.83  ?  288 VAL A O     1 
ATOM   939  C CB    . VAL A 1 307 ? -11.344 63.980  91.282  1.00 97.76  ?  288 VAL A CB    1 
ATOM   940  C CG1   . VAL A 1 307 ? -12.740 63.453  91.048  1.00 89.81  ?  288 VAL A CG1   1 
ATOM   941  C CG2   . VAL A 1 307 ? -10.579 64.115  89.977  1.00 92.99  ?  288 VAL A CG2   1 
ATOM   942  N N     . SER A 1 308 ? -9.474  65.144  93.528  1.00 99.69  ?  289 SER A N     1 
ATOM   943  C CA    . SER A 1 308 ? -8.897  65.017  94.879  1.00 92.57  ?  289 SER A CA    1 
ATOM   944  C C     . SER A 1 308 ? -9.345  66.228  95.672  1.00 94.05  ?  289 SER A C     1 
ATOM   945  O O     . SER A 1 308 ? -9.935  66.050  96.721  1.00 96.83  ?  289 SER A O     1 
ATOM   946  C CB    . SER A 1 308 ? -7.427  65.011  94.790  1.00 86.95  ?  289 SER A CB    1 
ATOM   947  O OG    . SER A 1 308 ? -7.012  66.269  94.330  1.00 90.55  ?  289 SER A OG    1 
ATOM   948  N N     . GLY A 1 309 ? -9.227  67.405  95.082  1.00 92.88  ?  290 GLY A N     1 
ATOM   949  C CA    . GLY A 1 309 ? -9.603  68.613  95.825  1.00 96.60  ?  290 GLY A CA    1 
ATOM   950  C C     . GLY A 1 309 ? -11.056 68.598  96.223  1.00 95.35  ?  290 GLY A C     1 
ATOM   951  O O     . GLY A 1 309 ? -11.333 68.817  97.381  1.00 93.13  ?  290 GLY A O     1 
ATOM   952  N N     . LEU A 1 310 ? -11.946 68.196  95.331  1.00 95.52  ?  291 LEU A N     1 
ATOM   953  C CA    . LEU A 1 310 ? -13.381 68.210  95.683  1.00 95.06  ?  291 LEU A CA    1 
ATOM   954  C C     . LEU A 1 310 ? -13.617 67.248  96.829  1.00 93.47  ?  291 LEU A C     1 
ATOM   955  O O     . LEU A 1 310 ? -14.368 67.574  97.713  1.00 93.75  ?  291 LEU A O     1 
ATOM   956  C CB    . LEU A 1 310 ? -14.171 67.740  94.472  1.00 95.86  ?  291 LEU A CB    1 
ATOM   957  C CG    . LEU A 1 310 ? -14.433 68.805  93.424  1.00 93.86  ?  291 LEU A CG    1 
ATOM   958  C CD1   . LEU A 1 310 ? -14.199 68.226  92.054  1.00 94.45  ?  291 LEU A CD1   1 
ATOM   959  C CD2   . LEU A 1 310 ? -15.853 69.305  93.542  1.00 94.54  ?  291 LEU A CD2   1 
ATOM   960  N N     . ALA A 1 311 ? -12.990 66.092  96.765  1.00 91.18  ?  292 ALA A N     1 
ATOM   961  C CA    . ALA A 1 311 ? -13.142 65.112  97.845  1.00 97.29  ?  292 ALA A CA    1 
ATOM   962  C C     . ALA A 1 311 ? -12.750 65.764  99.160  1.00 97.06  ?  292 ALA A C     1 
ATOM   963  O O     . ALA A 1 311 ? -13.455 65.567  100.128 1.00 95.57  ?  292 ALA A O     1 
ATOM   964  C CB    . ALA A 1 311 ? -12.238 63.959  97.552  1.00 98.11  ?  292 ALA A CB    1 
ATOM   965  N N     . ALA A 1 312 ? -11.674 66.535  99.184  1.00 96.01  ?  293 ALA A N     1 
ATOM   966  C CA    . ALA A 1 312 ? -11.326 67.075  100.505 1.00 92.81  ?  293 ALA A CA    1 
ATOM   967  C C     . ALA A 1 312 ? -12.394 68.059  100.942 1.00 92.74  ?  293 ALA A C     1 
ATOM   968  O O     . ALA A 1 312 ? -12.899 67.901  102.029 1.00 95.99  ?  293 ALA A O     1 
ATOM   969  C CB    . ALA A 1 312 ? -10.007 67.767  100.407 1.00 90.23  ?  293 ALA A CB    1 
ATOM   970  N N     . ALA A 1 313 ? -12.728 68.995  100.065 1.00 93.48  ?  294 ALA A N     1 
ATOM   971  C CA    . ALA A 1 313 ? -13.719 70.057  100.332 1.00 95.32  ?  294 ALA A CA    1 
ATOM   972  C C     . ALA A 1 313 ? -14.945 69.508  101.038 1.00 95.37  ?  294 ALA A C     1 
ATOM   973  O O     . ALA A 1 313 ? -15.226 69.974  102.099 1.00 101.99 ?  294 ALA A O     1 
ATOM   974  C CB    . ALA A 1 313 ? -14.116 70.709  99.045  1.00 94.42  ?  294 ALA A CB    1 
ATOM   975  N N     . ARG A 1 314 ? -15.561 68.473  100.508 1.00 93.35  ?  295 ARG A N     1 
ATOM   976  C CA    . ARG A 1 314 ? -16.787 68.010  101.181 1.00 94.14  ?  295 ARG A CA    1 
ATOM   977  C C     . ARG A 1 314 ? -16.452 67.467  102.557 1.00 98.29  ?  295 ARG A C     1 
ATOM   978  O O     . ARG A 1 314 ? -17.206 67.738  103.451 1.00 102.38 ?  295 ARG A O     1 
ATOM   979  C CB    . ARG A 1 314 ? -17.511 66.968  100.342 1.00 94.04  ?  295 ARG A CB    1 
ATOM   980  C CG    . ARG A 1 314 ? -17.909 67.503  98.984  1.00 93.02  ?  295 ARG A CG    1 
ATOM   981  C CD    . ARG A 1 314 ? -18.931 66.593  98.382  1.00 93.03  ?  295 ARG A CD    1 
ATOM   982  N NE    . ARG A 1 314 ? -20.204 67.258  98.389  1.00 100.80 ?  295 ARG A NE    1 
ATOM   983  C CZ    . ARG A 1 314 ? -21.260 66.760  98.982  1.00 109.24 ?  295 ARG A CZ    1 
ATOM   984  N NH1   . ARG A 1 314 ? -21.169 65.598  99.596  1.00 113.17 ?  295 ARG A NH1   1 
ATOM   985  N NH2   . ARG A 1 314 ? -22.401 67.414  98.958  1.00 112.28 ?  295 ARG A NH2   1 
ATOM   986  N N     . GLN A 1 315 ? -15.365 66.729  102.712 1.00 99.46  ?  296 GLN A N     1 
ATOM   987  C CA    . GLN A 1 315 ? -15.129 66.177  104.065 1.00 99.57  ?  296 GLN A CA    1 
ATOM   988  C C     . GLN A 1 315 ? -14.884 67.311  105.055 1.00 97.34  ?  296 GLN A C     1 
ATOM   989  O O     . GLN A 1 315 ? -15.639 67.406  106.030 1.00 102.27 ?  296 GLN A O     1 
ATOM   990  C CB    . GLN A 1 315 ? -13.912 65.255  104.055 1.00 99.49  ?  296 GLN A CB    1 
ATOM   991  C CG    . GLN A 1 315 ? -14.224 63.788  103.788 1.00 98.67  ?  296 GLN A CG    1 
ATOM   992  C CD    . GLN A 1 315 ? -15.611 63.369  104.192 1.00 106.34 ?  296 GLN A CD    1 
ATOM   993  O OE1   . GLN A 1 315 ? -16.603 63.937  103.767 1.00 107.04 ?  296 GLN A OE1   1 
ATOM   994  N NE2   . GLN A 1 315 ? -15.690 62.346  105.016 1.00 105.97 ?  296 GLN A NE2   1 
ATOM   995  N N     . LEU A 1 316 ? -13.995 68.238  104.717 1.00 93.09  ?  297 LEU A N     1 
ATOM   996  C CA    . LEU A 1 316 ? -13.670 69.328  105.664 1.00 89.05  ?  297 LEU A CA    1 
ATOM   997  C C     . LEU A 1 316 ? -14.932 70.138  105.906 1.00 95.50  ?  297 LEU A C     1 
ATOM   998  O O     . LEU A 1 316 ? -15.266 70.361  107.042 1.00 101.56 ?  297 LEU A O     1 
ATOM   999  C CB    . LEU A 1 316 ? -12.566 70.191  105.069 1.00 84.05  ?  297 LEU A CB    1 
ATOM   1000 C CG    . LEU A 1 316 ? -11.254 69.458  104.850 1.00 87.23  ?  297 LEU A CG    1 
ATOM   1001 C CD1   . LEU A 1 316 ? -10.291 70.311  104.071 1.00 85.98  ?  297 LEU A CD1   1 
ATOM   1002 C CD2   . LEU A 1 316 ? -10.631 69.089  106.164 1.00 81.81  ?  297 LEU A CD2   1 
ATOM   1003 N N     . GLN A 1 317 ? -15.686 70.432  104.864 1.00 94.08  ?  298 GLN A N     1 
ATOM   1004 C CA    . GLN A 1 317 ? -16.955 71.150  105.076 1.00 97.22  ?  298 GLN A CA    1 
ATOM   1005 C C     . GLN A 1 317 ? -17.871 70.273  105.924 1.00 100.13 ?  298 GLN A C     1 
ATOM   1006 O O     . GLN A 1 317 ? -18.486 70.804  106.810 1.00 104.04 ?  298 GLN A O     1 
ATOM   1007 C CB    . GLN A 1 317 ? -17.587 71.428  103.728 1.00 100.61 ?  298 GLN A CB    1 
ATOM   1008 C CG    . GLN A 1 317 ? -18.091 72.841  103.572 1.00 108.48 ?  298 GLN A CG    1 
ATOM   1009 C CD    . GLN A 1 317 ? -19.418 72.764  102.873 1.00 111.01 ?  298 GLN A CD    1 
ATOM   1010 O OE1   . GLN A 1 317 ? -20.031 71.705  102.790 1.00 115.82 ?  298 GLN A OE1   1 
ATOM   1011 N NE2   . GLN A 1 317 ? -19.862 73.893  102.362 1.00 99.79  ?  298 GLN A NE2   1 
ATOM   1012 N N     . SER A 1 318 ? -17.917 68.959  105.696 1.00 103.95 ?  299 SER A N     1 
ATOM   1013 C CA    . SER A 1 318 ? -18.751 68.060  106.536 1.00 108.77 ?  299 SER A CA    1 
ATOM   1014 C C     . SER A 1 318 ? -18.228 68.086  107.964 1.00 106.17 ?  299 SER A C     1 
ATOM   1015 O O     . SER A 1 318 ? -19.027 68.018  108.875 1.00 109.22 ?  299 SER A O     1 
ATOM   1016 C CB    . SER A 1 318 ? -18.777 66.656  106.021 1.00 113.30 ?  299 SER A CB    1 
ATOM   1017 O OG    . SER A 1 318 ? -18.895 65.713  107.073 1.00 114.29 ?  299 SER A OG    1 
ATOM   1018 N N     . PHE A 1 319 ? -16.915 68.158  108.136 1.00 102.81 ?  300 PHE A N     1 
ATOM   1019 C CA    . PHE A 1 319 ? -16.282 68.208  109.473 1.00 105.44 ?  300 PHE A CA    1 
ATOM   1020 C C     . PHE A 1 319 ? -16.607 69.488  110.243 1.00 106.26 ?  300 PHE A C     1 
ATOM   1021 O O     . PHE A 1 319 ? -16.418 69.481  111.448 1.00 103.15 ?  300 PHE A O     1 
ATOM   1022 C CB    . PHE A 1 319 ? -14.781 68.012  109.340 1.00 102.14 ?  300 PHE A CB    1 
ATOM   1023 C CG    . PHE A 1 319 ? -14.441 66.597  108.984 1.00 98.34  ?  300 PHE A CG    1 
ATOM   1024 C CD1   . PHE A 1 319 ? -15.447 65.668  108.833 1.00 99.06  ?  300 PHE A CD1   1 
ATOM   1025 C CD2   . PHE A 1 319 ? -13.134 66.199  108.814 1.00 92.73  ?  300 PHE A CD2   1 
ATOM   1026 C CE1   . PHE A 1 319 ? -15.149 64.358  108.518 1.00 103.62 ?  300 PHE A CE1   1 
ATOM   1027 C CE2   . PHE A 1 319 ? -12.840 64.893  108.486 1.00 98.09  ?  300 PHE A CE2   1 
ATOM   1028 C CZ    . PHE A 1 319 ? -13.846 63.976  108.345 1.00 105.74 ?  300 PHE A CZ    1 
ATOM   1029 N N     . GLY A 1 320 ? -17.009 70.564  109.578 1.00 110.58 ?  301 GLY A N     1 
ATOM   1030 C CA    . GLY A 1 320 ? -17.325 71.794  110.310 1.00 105.21 ?  301 GLY A CA    1 
ATOM   1031 C C     . GLY A 1 320 ? -16.291 72.848  110.031 1.00 103.20 ?  301 GLY A C     1 
ATOM   1032 O O     . GLY A 1 320 ? -16.094 73.695  110.876 1.00 111.43 ?  301 GLY A O     1 
ATOM   1033 N N     . MET A 1 321 ? -15.608 72.761  108.902 1.00 96.79  ?  302 MET A N     1 
ATOM   1034 C CA    . MET A 1 321 ? -14.576 73.778  108.643 1.00 95.15  ?  302 MET A CA    1 
ATOM   1035 C C     . MET A 1 321 ? -15.019 74.742  107.550 1.00 100.43 ?  302 MET A C     1 
ATOM   1036 O O     . MET A 1 321 ? -16.089 74.560  107.012 1.00 100.30 ?  302 MET A O     1 
ATOM   1037 C CB    . MET A 1 321 ? -13.316 73.073  108.174 1.00 84.99  ?  302 MET A CB    1 
ATOM   1038 C CG    . MET A 1 321 ? -12.171 73.339  109.058 1.00 86.82  ?  302 MET A CG    1 
ATOM   1039 S SD    . MET A 1 321 ? -11.178 71.892  109.062 1.00 95.67  ?  302 MET A SD    1 
ATOM   1040 C CE    . MET A 1 321 ? -9.567  72.620  109.304 1.00 89.56  ?  302 MET A CE    1 
ATOM   1041 N N     . ASP A 1 322 ? -14.215 75.775  107.321 1.00 102.40 ?  303 ASP A N     1 
ATOM   1042 C CA    . ASP A 1 322 ? -14.384 76.729  106.245 1.00 105.40 ?  303 ASP A CA    1 
ATOM   1043 C C     . ASP A 1 322 ? -13.466 76.308  105.110 1.00 110.04 ?  303 ASP A C     1 
ATOM   1044 O O     . ASP A 1 322 ? -12.234 76.391  105.234 1.00 106.77 ?  303 ASP A O     1 
ATOM   1045 C CB    . ASP A 1 322 ? -14.047 78.138  106.698 1.00 106.34 ?  303 ASP A CB    1 
ATOM   1046 C CG    . ASP A 1 322 ? -14.460 79.152  105.684 1.00 113.23 ?  303 ASP A CG    1 
ATOM   1047 O OD1   . ASP A 1 322 ? -15.201 78.758  104.755 1.00 121.98 ?  303 ASP A OD1   1 
ATOM   1048 O OD2   . ASP A 1 322 ? -14.025 80.315  105.776 1.00 114.16 ?  303 ASP A OD2   1 
ATOM   1049 N N     . VAL A 1 323 ? -14.063 75.866  104.004 1.00 110.34 ?  304 VAL A N     1 
ATOM   1050 C CA    . VAL A 1 323 ? -13.307 75.374  102.867 1.00 104.72 ?  304 VAL A CA    1 
ATOM   1051 C C     . VAL A 1 323 ? -13.609 76.251  101.665 1.00 101.83 ?  304 VAL A C     1 
ATOM   1052 O O     . VAL A 1 323 ? -14.777 76.537  101.370 1.00 100.38 ?  304 VAL A O     1 
ATOM   1053 C CB    . VAL A 1 323 ? -13.630 73.906  102.557 1.00 102.82 ?  304 VAL A CB    1 
ATOM   1054 C CG1   . VAL A 1 323 ? -12.677 73.426  101.505 1.00 106.96 ?  304 VAL A CG1   1 
ATOM   1055 C CG2   . VAL A 1 323 ? -13.496 73.052  103.786 1.00 96.04  ?  304 VAL A CG2   1 
ATOM   1056 N N     . THR A 1 324 ? -12.553 76.659  100.969 1.00 98.71  ?  305 THR A N     1 
ATOM   1057 C CA    . THR A 1 324 ? -12.678 77.452  99.757  1.00 103.06 ?  305 THR A CA    1 
ATOM   1058 C C     . THR A 1 324 ? -11.663 76.994  98.725  1.00 106.64 ?  305 THR A C     1 
ATOM   1059 O O     . THR A 1 324 ? -10.483 76.825  99.061  1.00 102.01 ?  305 THR A O     1 
ATOM   1060 C CB    . THR A 1 324 ? -12.487 78.922  100.074 1.00 106.44 ?  305 THR A CB    1 
ATOM   1061 O OG1   . THR A 1 324 ? -13.633 79.366  100.812 1.00 120.86 ?  305 THR A OG1   1 
ATOM   1062 C CG2   . THR A 1 324 ? -12.299 79.738  98.803  1.00 100.55 ?  305 THR A CG2   1 
ATOM   1063 N N     . LEU A 1 325 ? -12.130 76.827  97.472  1.00 106.04 ?  306 LEU A N     1 
ATOM   1064 C CA    . LEU A 1 325 ? -11.409 76.145  96.400  1.00 95.99  ?  306 LEU A CA    1 
ATOM   1065 C C     . LEU A 1 325 ? -11.066 77.115  95.268  1.00 99.11  ?  306 LEU A C     1 
ATOM   1066 O O     . LEU A 1 325 ? -11.950 77.787  94.722  1.00 98.97  ?  306 LEU A O     1 
ATOM   1067 C CB    . LEU A 1 325 ? -12.236 74.997  95.813  1.00 95.36  ?  306 LEU A CB    1 
ATOM   1068 C CG    . LEU A 1 325 ? -12.369 73.657  96.527  1.00 94.76  ?  306 LEU A CG    1 
ATOM   1069 C CD1   . LEU A 1 325 ? -13.310 73.828  97.662  1.00 102.01 ?  306 LEU A CD1   1 
ATOM   1070 C CD2   . LEU A 1 325 ? -12.848 72.561  95.614  1.00 98.78  ?  306 LEU A CD2   1 
ATOM   1071 N N     . LEU A 1 326 ? -9.798  77.131  94.869  1.00 95.80  ?  307 LEU A N     1 
ATOM   1072 C CA    . LEU A 1 326 ? -9.316  77.974  93.780  1.00 92.61  ?  307 LEU A CA    1 
ATOM   1073 C C     . LEU A 1 326 ? -9.060  77.135  92.532  1.00 98.70  ?  307 LEU A C     1 
ATOM   1074 O O     . LEU A 1 326 ? -8.079  76.382  92.484  1.00 101.59 ?  307 LEU A O     1 
ATOM   1075 C CB    . LEU A 1 326 ? -8.028  78.660  94.205  1.00 91.57  ?  307 LEU A CB    1 
ATOM   1076 C CG    . LEU A 1 326 ? -8.243  79.398  95.502  1.00 95.65  ?  307 LEU A CG    1 
ATOM   1077 C CD1   . LEU A 1 326 ? -6.966  80.146  95.831  1.00 99.13  ?  307 LEU A CD1   1 
ATOM   1078 C CD2   . LEU A 1 326 ? -9.456  80.331  95.360  1.00 98.73  ?  307 LEU A CD2   1 
ATOM   1079 N N     . GLU A 1 327 ? -9.894  77.299  91.501  1.00 99.29  ?  308 GLU A N     1 
ATOM   1080 C CA    . GLU A 1 327 ? -9.753  76.536  90.263  1.00 96.72  ?  308 GLU A CA    1 
ATOM   1081 C C     . GLU A 1 327 ? -9.347  77.436  89.111  1.00 99.19  ?  308 GLU A C     1 
ATOM   1082 O O     . GLU A 1 327 ? -9.925  78.517  88.933  1.00 102.28 ?  308 GLU A O     1 
ATOM   1083 C CB    . GLU A 1 327 ? -11.053 75.824  89.919  1.00 94.56  ?  308 GLU A CB    1 
ATOM   1084 C CG    . GLU A 1 327 ? -11.081 75.199  88.549  1.00 100.13 ?  308 GLU A CG    1 
ATOM   1085 C CD    . GLU A 1 327 ? -10.081 74.057  88.378  1.00 102.06 ?  308 GLU A CD    1 
ATOM   1086 O OE1   . GLU A 1 327 ? -9.477  73.591  89.381  1.00 102.47 ?  308 GLU A OE1   1 
ATOM   1087 O OE2   . GLU A 1 327 ? -9.982  73.549  87.235  1.00 99.08  ?  308 GLU A OE2   1 
ATOM   1088 N N     . ALA A 1 328 ? -8.384  76.969  88.305  1.00 97.07  ?  309 ALA A N     1 
ATOM   1089 C CA    . ALA A 1 328 ? -7.871  77.794  87.209  1.00 100.21 ?  309 ALA A CA    1 
ATOM   1090 C C     . ALA A 1 328 ? -8.754  77.763  85.965  1.00 99.73  ?  309 ALA A C     1 
ATOM   1091 O O     . ALA A 1 328 ? -8.620  78.645  85.101  1.00 97.74  ?  309 ALA A O     1 
ATOM   1092 C CB    . ALA A 1 328 ? -6.452  77.365  86.827  1.00 96.23  ?  309 ALA A CB    1 
ATOM   1093 N N     . ARG A 1 329 ? -9.621  76.765  85.874  1.00 99.70  ?  310 ARG A N     1 
ATOM   1094 C CA    . ARG A 1 329 ? -10.485 76.606  84.684  1.00 97.07  ?  310 ARG A CA    1 
ATOM   1095 C C     . ARG A 1 329 ? -11.829 77.265  84.925  1.00 99.28  ?  310 ARG A C     1 
ATOM   1096 O O     . ARG A 1 329 ? -11.989 77.901  85.945  1.00 102.49 ?  310 ARG A O     1 
ATOM   1097 C CB    . ARG A 1 329 ? -10.797 75.124  84.494  1.00 93.17  ?  310 ARG A CB    1 
ATOM   1098 C CG    . ARG A 1 329 ? -9.621  74.313  83.979  1.00 95.65  ?  310 ARG A CG    1 
ATOM   1099 C CD    . ARG A 1 329 ? -9.970  72.877  83.671  1.00 97.66  ?  310 ARG A CD    1 
ATOM   1100 N NE    . ARG A 1 329 ? -8.831  72.058  84.007  1.00 99.99  ?  310 ARG A NE    1 
ATOM   1101 C CZ    . ARG A 1 329 ? -7.959  71.611  83.136  1.00 95.64  ?  310 ARG A CZ    1 
ATOM   1102 N NH1   . ARG A 1 329 ? -8.099  71.888  81.860  1.00 95.09  ?  310 ARG A NH1   1 
ATOM   1103 N NH2   . ARG A 1 329 ? -6.946  70.882  83.544  1.00 93.55  ?  310 ARG A NH2   1 
ATOM   1104 N N     . ASP A 1 330 ? -12.728 77.138  83.960  1.00 95.81  ?  311 ASP A N     1 
ATOM   1105 C CA    . ASP A 1 330 ? -14.108 77.646  84.113  1.00 94.79  ?  311 ASP A CA    1 
ATOM   1106 C C     . ASP A 1 330 ? -15.027 76.455  84.327  1.00 96.80  ?  311 ASP A C     1 
ATOM   1107 O O     . ASP A 1 330 ? -16.229 76.648  84.216  1.00 96.57  ?  311 ASP A O     1 
ATOM   1108 C CB    . ASP A 1 330 ? -14.586 78.296  82.828  1.00 103.24 ?  311 ASP A CB    1 
ATOM   1109 C CG    . ASP A 1 330 ? -13.893 77.666  81.647  1.00 120.45 ?  311 ASP A CG    1 
ATOM   1110 O OD1   . ASP A 1 330 ? -12.857 77.038  81.873  1.00 113.66 ?  311 ASP A OD1   1 
ATOM   1111 O OD2   . ASP A 1 330 ? -14.394 77.807  80.525  1.00 123.21 ?  311 ASP A OD2   1 
ATOM   1112 N N     . ARG A 1 331 ? -14.467 75.262  84.529  1.00 93.18  ?  312 ARG A N     1 
ATOM   1113 C CA    . ARG A 1 331 ? -15.285 74.043  84.741  1.00 93.96  ?  312 ARG A CA    1 
ATOM   1114 C C     . ARG A 1 331 ? -14.726 73.297  85.946  1.00 98.98  ?  312 ARG A C     1 
ATOM   1115 O O     . ARG A 1 331 ? -13.529 73.338  86.149  1.00 99.48  ?  312 ARG A O     1 
ATOM   1116 C CB    . ARG A 1 331 ? -15.451 73.244  83.447  1.00 102.32 ?  312 ARG A CB    1 
ATOM   1117 C CG    . ARG A 1 331 ? -14.499 72.074  83.268  1.00 99.49  ?  312 ARG A CG    1 
ATOM   1118 C CD    . ARG A 1 331 ? -13.907 71.988  81.882  1.00 88.94  ?  312 ARG A CD    1 
ATOM   1119 N NE    . ARG A 1 331 ? -12.558 71.497  82.036  1.00 91.23  ?  312 ARG A NE    1 
ATOM   1120 C CZ    . ARG A 1 331 ? -12.291 70.369  82.645  1.00 95.43  ?  312 ARG A CZ    1 
ATOM   1121 N NH1   . ARG A 1 331 ? -13.283 69.645  83.112  1.00 96.33  ?  312 ARG A NH1   1 
ATOM   1122 N NH2   . ARG A 1 331 ? -11.054 69.950  82.780  1.00 93.80  ?  312 ARG A NH2   1 
ATOM   1123 N N     . VAL A 1 332 ? -15.603 72.665  86.714  1.00 95.19  ?  313 VAL A N     1 
ATOM   1124 C CA    . VAL A 1 332 ? -15.213 72.048  88.009  1.00 98.11  ?  313 VAL A CA    1 
ATOM   1125 C C     . VAL A 1 332 ? -14.247 70.884  87.892  1.00 98.41  ?  313 VAL A C     1 
ATOM   1126 O O     . VAL A 1 332 ? -13.143 71.031  88.368  1.00 95.90  ?  313 VAL A O     1 
ATOM   1127 C CB    . VAL A 1 332 ? -16.481 71.541  88.699  1.00 102.64 ?  313 VAL A CB    1 
ATOM   1128 C CG1   . VAL A 1 332 ? -17.084 72.613  89.576  1.00 99.57  ?  313 VAL A CG1   1 
ATOM   1129 C CG2   . VAL A 1 332 ? -17.490 71.088  87.665  1.00 99.65  ?  313 VAL A CG2   1 
ATOM   1130 N N     . GLY A 1 333 ? -14.586 69.767  87.251  1.00 95.87  ?  314 GLY A N     1 
ATOM   1131 C CA    . GLY A 1 333 ? -13.721 68.565  87.209  1.00 93.01  ?  314 GLY A CA    1 
ATOM   1132 C C     . GLY A 1 333 ? -12.295 68.831  86.782  1.00 92.24  ?  314 GLY A C     1 
ATOM   1133 O O     . GLY A 1 333 ? -12.099 69.637  85.897  1.00 93.40  ?  314 GLY A O     1 
ATOM   1134 N N     . GLY A 1 334 ? -11.327 68.073  87.274  1.00 94.38  ?  315 GLY A N     1 
ATOM   1135 C CA    . GLY A 1 334 ? -9.967  68.440  86.856  1.00 98.39  ?  315 GLY A CA    1 
ATOM   1136 C C     . GLY A 1 334 ? -9.577  67.736  85.587  1.00 101.39 ?  315 GLY A C     1 
ATOM   1137 O O     . GLY A 1 334 ? -9.780  68.279  84.514  1.00 100.45 ?  315 GLY A O     1 
ATOM   1138 N N     . ARG A 1 335 ? -9.178  66.483  85.698  1.00 96.28  ?  316 ARG A N     1 
ATOM   1139 C CA    . ARG A 1 335 ? -8.860  65.723  84.476  1.00 85.75  ?  316 ARG A CA    1 
ATOM   1140 C C     . ARG A 1 335 ? -10.078 64.888  84.122  1.00 83.12  ?  316 ARG A C     1 
ATOM   1141 O O     . ARG A 1 335 ? -9.920  63.992  83.361  1.00 85.92  ?  316 ARG A O     1 
ATOM   1142 C CB    . ARG A 1 335 ? -7.624  64.852  84.652  1.00 86.81  ?  316 ARG A CB    1 
ATOM   1143 C CG    . ARG A 1 335 ? -6.334  65.646  84.683  1.00 85.62  ?  316 ARG A CG    1 
ATOM   1144 C CD    . ARG A 1 335 ? -5.074  64.830  84.594  1.00 91.04  ?  316 ARG A CD    1 
ATOM   1145 N NE    . ARG A 1 335 ? -4.439  64.242  85.761  1.00 97.82  ?  316 ARG A NE    1 
ATOM   1146 C CZ    . ARG A 1 335 ? -4.060  64.875  86.850  1.00 101.02 ?  316 ARG A CZ    1 
ATOM   1147 N NH1   . ARG A 1 335 ? -4.294  66.159  86.988  1.00 95.45  ?  316 ARG A NH1   1 
ATOM   1148 N NH2   . ARG A 1 335 ? -3.463  64.214  87.816  1.00 100.81 ?  316 ARG A NH2   1 
ATOM   1149 N N     . VAL A 1 336 ? -11.198 65.079  84.797  1.00 84.02  ?  317 VAL A N     1 
ATOM   1150 C CA    . VAL A 1 336 ? -12.424 64.376  84.384  1.00 85.45  ?  317 VAL A CA    1 
ATOM   1151 C C     . VAL A 1 336 ? -13.106 65.370  83.472  1.00 98.73  ?  317 VAL A C     1 
ATOM   1152 O O     . VAL A 1 336 ? -13.811 66.221  83.977  1.00 98.23  ?  317 VAL A O     1 
ATOM   1153 C CB    . VAL A 1 336 ? -13.320 64.092  85.583  1.00 85.14  ?  317 VAL A CB    1 
ATOM   1154 C CG1   . VAL A 1 336 ? -14.771 63.998  85.161  1.00 83.13  ?  317 VAL A CG1   1 
ATOM   1155 C CG2   . VAL A 1 336 ? -12.887 62.823  86.267  1.00 84.44  ?  317 VAL A CG2   1 
ATOM   1156 N N     . ALA A 1 337 ? -12.894 65.238  82.172  1.00 108.36 ?  318 ALA A N     1 
ATOM   1157 C CA    . ALA A 1 337 ? -13.486 66.193  81.224  1.00 101.78 ?  318 ALA A CA    1 
ATOM   1158 C C     . ALA A 1 337 ? -14.619 65.502  80.503  1.00 100.36 ?  318 ALA A C     1 
ATOM   1159 O O     . ALA A 1 337 ? -14.514 64.318  80.257  1.00 100.67 ?  318 ALA A O     1 
ATOM   1160 C CB    . ALA A 1 337 ? -12.447 66.651  80.256  1.00 92.23  ?  318 ALA A CB    1 
ATOM   1161 N N     . THR A 1 338 ? -15.663 66.255  80.222  1.00 100.74 ?  319 THR A N     1 
ATOM   1162 C CA    . THR A 1 338 ? -16.858 65.717  79.525  1.00 106.60 ?  319 THR A CA    1 
ATOM   1163 C C     . THR A 1 338 ? -17.248 66.548  78.336  1.00 114.88 ?  319 THR A C     1 
ATOM   1164 O O     . THR A 1 338 ? -17.896 67.585  78.552  1.00 116.47 ?  319 THR A O     1 
ATOM   1165 C CB    . THR A 1 338 ? -18.049 65.565  80.472  1.00 110.31 ?  319 THR A CB    1 
ATOM   1166 O OG1   . THR A 1 338 ? -18.007 64.245  80.996  1.00 114.87 ?  319 THR A OG1   1 
ATOM   1167 C CG2   . THR A 1 338 ? -19.386 65.726  79.790  1.00 111.48 ?  319 THR A CG2   1 
ATOM   1168 N N     . PHE A 1 339 ? -16.884 66.093  77.142  1.00 112.20 ?  320 PHE A N     1 
ATOM   1169 C CA    . PHE A 1 339 ? -17.356 66.990  76.069  1.00 106.58 ?  320 PHE A CA    1 
ATOM   1170 C C     . PHE A 1 339 ? -18.844 66.763  75.865  1.00 110.37 ?  320 PHE A C     1 
ATOM   1171 O O     . PHE A 1 339 ? -19.224 65.624  75.729  1.00 111.51 ?  320 PHE A O     1 
ATOM   1172 C CB    . PHE A 1 339 ? -16.602 66.643  74.791  1.00 108.57 ?  320 PHE A CB    1 
ATOM   1173 C CG    . PHE A 1 339 ? -17.260 67.107  73.523  1.00 119.03 ?  320 PHE A CG    1 
ATOM   1174 C CD1   . PHE A 1 339 ? -16.675 68.090  72.758  1.00 117.66 ?  320 PHE A CD1   1 
ATOM   1175 C CD2   . PHE A 1 339 ? -18.436 66.540  73.071  1.00 119.27 ?  320 PHE A CD2   1 
ATOM   1176 C CE1   . PHE A 1 339 ? -17.275 68.521  71.591  1.00 115.87 ?  320 PHE A CE1   1 
ATOM   1177 C CE2   . PHE A 1 339 ? -19.045 66.979  71.912  1.00 114.69 ?  320 PHE A CE2   1 
ATOM   1178 C CZ    . PHE A 1 339 ? -18.459 67.968  71.174  1.00 116.50 ?  320 PHE A CZ    1 
ATOM   1179 N N     . ARG A 1 340 ? -19.639 67.821  75.791  1.00 112.09 ?  321 ARG A N     1 
ATOM   1180 C CA    . ARG A 1 340 ? -21.082 67.621  75.527  1.00 114.93 ?  321 ARG A CA    1 
ATOM   1181 C C     . ARG A 1 340 ? -21.534 68.552  74.405  1.00 121.93 ?  321 ARG A C     1 
ATOM   1182 O O     . ARG A 1 340 ? -21.259 69.741  74.505  1.00 122.69 ?  321 ARG A O     1 
ATOM   1183 C CB    . ARG A 1 340 ? -21.891 67.921  76.785  1.00 112.90 ?  321 ARG A CB    1 
ATOM   1184 C CG    . ARG A 1 340 ? -22.717 66.746  77.276  1.00 117.08 ?  321 ARG A CG    1 
ATOM   1185 C CD    . ARG A 1 340 ? -23.326 66.992  78.636  1.00 117.60 ?  321 ARG A CD    1 
ATOM   1186 N NE    . ARG A 1 340 ? -22.394 66.812  79.730  1.00 116.15 ?  321 ARG A NE    1 
ATOM   1187 C CZ    . ARG A 1 340 ? -22.325 65.730  80.483  1.00 119.06 ?  321 ARG A CZ    1 
ATOM   1188 N NH1   . ARG A 1 340 ? -23.125 64.708  80.259  1.00 115.16 ?  321 ARG A NH1   1 
ATOM   1189 N NH2   . ARG A 1 340 ? -21.468 65.674  81.475  1.00 123.96 ?  321 ARG A NH2   1 
ATOM   1190 N N     . LYS A 1 341 ? -22.165 68.005  73.368  1.00 122.23 ?  322 LYS A N     1 
ATOM   1191 C CA    . LYS A 1 341 ? -22.739 68.803  72.256  1.00 117.52 ?  322 LYS A CA    1 
ATOM   1192 C C     . LYS A 1 341 ? -23.972 68.053  71.771  1.00 112.72 ?  322 LYS A C     1 
ATOM   1193 O O     . LYS A 1 341 ? -23.827 66.868  71.518  1.00 111.99 ?  322 LYS A O     1 
ATOM   1194 C CB    . LYS A 1 341 ? -21.715 68.942  71.132  1.00 105.42 ?  322 LYS A CB    1 
ATOM   1195 C CG    . LYS A 1 341 ? -21.804 70.217  70.308  1.00 111.37 ?  322 LYS A CG    1 
ATOM   1196 C CD    . LYS A 1 341 ? -20.482 70.611  69.683  1.00 116.70 ?  322 LYS A CD    1 
ATOM   1197 C CE    . LYS A 1 341 ? -20.612 71.624  68.565  1.00 126.13 ?  322 LYS A CE    1 
ATOM   1198 N NZ    . LYS A 1 341 ? -19.827 71.246  67.365  1.00 126.88 ?  322 LYS A NZ    1 
ATOM   1199 N N     . GLY A 1 342 ? -25.114 68.722  71.645  1.00 112.95 ?  323 GLY A N     1 
ATOM   1200 C CA    . GLY A 1 342 ? -26.330 68.025  71.196  1.00 116.94 ?  323 GLY A CA    1 
ATOM   1201 C C     . GLY A 1 342 ? -26.564 66.854  72.112  1.00 119.75 ?  323 GLY A C     1 
ATOM   1202 O O     . GLY A 1 342 ? -26.676 67.075  73.303  1.00 118.28 ?  323 GLY A O     1 
ATOM   1203 N N     . ASN A 1 343 ? -26.668 65.657  71.547  1.00 128.21 ?  324 ASN A N     1 
ATOM   1204 C CA    . ASN A 1 343 ? -26.707 64.437  72.385  1.00 125.17 ?  324 ASN A CA    1 
ATOM   1205 C C     . ASN A 1 343 ? -25.331 63.782  72.321  1.00 120.83 ?  324 ASN A C     1 
ATOM   1206 O O     . ASN A 1 343 ? -25.129 62.788  72.996  1.00 114.62 ?  324 ASN A O     1 
ATOM   1207 C CB    . ASN A 1 343 ? -27.778 63.459  71.931  1.00 134.01 ?  324 ASN A CB    1 
ATOM   1208 C CG    . ASN A 1 343 ? -28.857 64.162  71.150  1.00 140.35 ?  324 ASN A CG    1 
ATOM   1209 O OD1   . ASN A 1 343 ? -29.844 64.607  71.723  1.00 138.86 ?  324 ASN A OD1   1 
ATOM   1210 N ND2   . ASN A 1 343 ? -28.662 64.279  69.850  1.00 141.53 ?  324 ASN A ND2   1 
ATOM   1211 N N     . TYR A 1 344 ? -24.394 64.337  71.558  1.00 122.80 ?  325 TYR A N     1 
ATOM   1212 C CA    . TYR A 1 344 ? -23.069 63.679  71.532  1.00 125.63 ?  325 TYR A CA    1 
ATOM   1213 C C     . TYR A 1 344 ? -22.463 63.835  72.923  1.00 125.00 ?  325 TYR A C     1 
ATOM   1214 O O     . TYR A 1 344 ? -22.583 64.918  73.489  1.00 127.30 ?  325 TYR A O     1 
ATOM   1215 C CB    . TYR A 1 344 ? -22.137 64.336  70.514  1.00 122.55 ?  325 TYR A CB    1 
ATOM   1216 C CG    . TYR A 1 344 ? -22.308 63.917  69.079  1.00 123.56 ?  325 TYR A CG    1 
ATOM   1217 C CD1   . TYR A 1 344 ? -23.560 63.693  68.544  1.00 124.43 ?  325 TYR A CD1   1 
ATOM   1218 C CD2   . TYR A 1 344 ? -21.213 63.778  68.249  1.00 128.03 ?  325 TYR A CD2   1 
ATOM   1219 C CE1   . TYR A 1 344 ? -23.727 63.329  67.221  1.00 126.99 ?  325 TYR A CE1   1 
ATOM   1220 C CE2   . TYR A 1 344 ? -21.357 63.409  66.925  1.00 127.97 ?  325 TYR A CE2   1 
ATOM   1221 C CZ    . TYR A 1 344 ? -22.620 63.185  66.410  1.00 128.28 ?  325 TYR A CZ    1 
ATOM   1222 O OH    . TYR A 1 344 ? -22.775 62.808  65.110  1.00 129.95 ?  325 TYR A OH    1 
ATOM   1223 N N     . VAL A 1 345 ? -21.830 62.794  73.455  1.00 120.48 ?  326 VAL A N     1 
ATOM   1224 C CA    . VAL A 1 345 ? -21.213 62.921  74.803  1.00 111.99 ?  326 VAL A CA    1 
ATOM   1225 C C     . VAL A 1 345 ? -19.920 62.123  74.870  1.00 113.53 ?  326 VAL A C     1 
ATOM   1226 O O     . VAL A 1 345 ? -19.992 60.934  74.658  1.00 121.76 ?  326 VAL A O     1 
ATOM   1227 C CB    . VAL A 1 345 ? -22.181 62.324  75.819  1.00 110.09 ?  326 VAL A CB    1 
ATOM   1228 C CG1   . VAL A 1 345 ? -21.421 61.872  77.038  1.00 118.92 ?  326 VAL A CG1   1 
ATOM   1229 C CG2   . VAL A 1 345 ? -23.286 63.289  76.175  1.00 110.44 ?  326 VAL A CG2   1 
ATOM   1230 N N     . ALA A 1 346 ? -18.804 62.715  75.269  1.00 109.64 ?  327 ALA A N     1 
ATOM   1231 C CA    . ALA A 1 346 ? -17.596 61.868  75.347  1.00 113.14 ?  327 ALA A CA    1 
ATOM   1232 C C     . ALA A 1 346 ? -16.620 62.397  76.391  1.00 110.02 ?  327 ALA A C     1 
ATOM   1233 O O     . ALA A 1 346 ? -16.488 63.601  76.510  1.00 109.07 ?  327 ALA A O     1 
ATOM   1234 C CB    . ALA A 1 346 ? -16.961 61.796  73.998  1.00 114.59 ?  327 ALA A CB    1 
ATOM   1235 N N     . ASP A 1 347 ? -15.895 61.505  77.029  1.00 106.43 ?  328 ASP A N     1 
ATOM   1236 C CA    . ASP A 1 347 ? -14.973 61.974  78.075  1.00 108.16 ?  328 ASP A CA    1 
ATOM   1237 C C     . ASP A 1 347 ? -13.571 62.025  77.496  1.00 101.47 ?  328 ASP A C     1 
ATOM   1238 O O     . ASP A 1 347 ? -13.123 61.017  77.015  1.00 103.24 ?  328 ASP A O     1 
ATOM   1239 C CB    . ASP A 1 347 ? -15.088 61.042  79.265  1.00 114.59 ?  328 ASP A CB    1 
ATOM   1240 C CG    . ASP A 1 347 ? -15.825 61.670  80.425  1.00 114.51 ?  328 ASP A CG    1 
ATOM   1241 O OD1   . ASP A 1 347 ? -15.941 62.909  80.443  1.00 105.75 ?  328 ASP A OD1   1 
ATOM   1242 O OD2   . ASP A 1 347 ? -16.288 60.922  81.285  1.00 120.77 ?  328 ASP A OD2   1 
ATOM   1243 N N     . LEU A 1 348 ? -12.914 63.168  77.582  1.00 97.72  ?  329 LEU A N     1 
ATOM   1244 C CA    . LEU A 1 348 ? -11.545 63.294  77.036  1.00 97.23  ?  329 LEU A CA    1 
ATOM   1245 C C     . LEU A 1 348 ? -10.588 63.114  78.194  1.00 100.19 ?  329 LEU A C     1 
ATOM   1246 O O     . LEU A 1 348 ? -9.407  63.359  78.026  1.00 95.32  ?  329 LEU A O     1 
ATOM   1247 C CB    . LEU A 1 348 ? -11.368 64.687  76.455  1.00 98.71  ?  329 LEU A CB    1 
ATOM   1248 C CG    . LEU A 1 348 ? -12.393 65.053  75.398  1.00 100.47 ?  329 LEU A CG    1 
ATOM   1249 C CD1   . LEU A 1 348 ? -13.761 65.237  76.021  1.00 103.22 ?  329 LEU A CD1   1 
ATOM   1250 C CD2   . LEU A 1 348 ? -11.962 66.305  74.675  1.00 100.63 ?  329 LEU A CD2   1 
ATOM   1251 N N     . GLY A 1 349 ? -11.151 62.747  79.332  1.00 104.13 ?  330 GLY A N     1 
ATOM   1252 C CA    . GLY A 1 349 ? -10.418 62.533  80.579  1.00 95.87  ?  330 GLY A CA    1 
ATOM   1253 C C     . GLY A 1 349 ? -10.725 61.166  81.105  1.00 95.07  ?  330 GLY A C     1 
ATOM   1254 O O     . GLY A 1 349 ? -10.491 60.217  80.399  1.00 104.26 ?  330 GLY A O     1 
ATOM   1255 N N     . ALA A 1 350 ? -11.165 61.043  82.336  1.00 98.87  ?  331 ALA A N     1 
ATOM   1256 C CA    . ALA A 1 350 ? -11.406 59.674  82.810  1.00 101.06 ?  331 ALA A CA    1 
ATOM   1257 C C     . ALA A 1 350 ? -12.541 59.054  82.020  1.00 102.62 ?  331 ALA A C     1 
ATOM   1258 O O     . ALA A 1 350 ? -13.519 59.754  81.716  1.00 95.59  ?  331 ALA A O     1 
ATOM   1259 C CB    . ALA A 1 350 ? -11.663 59.648  84.282  1.00 97.89  ?  331 ALA A CB    1 
ATOM   1260 N N     . MET A 1 351 ? -12.398 57.774  81.699  1.00 105.31 ?  332 MET A N     1 
ATOM   1261 C CA    . MET A 1 351 ? -13.480 57.143  80.915  1.00 106.88 ?  332 MET A CA    1 
ATOM   1262 C C     . MET A 1 351 ? -13.984 55.857  81.549  1.00 105.15 ?  332 MET A C     1 
ATOM   1263 O O     . MET A 1 351 ? -15.178 55.611  81.447  1.00 102.66 ?  332 MET A O     1 
ATOM   1264 C CB    . MET A 1 351 ? -12.955 56.784  79.532  1.00 108.95 ?  332 MET A CB    1 
ATOM   1265 C CG    . MET A 1 351 ? -13.985 56.871  78.467  1.00 108.42 ?  332 MET A CG    1 
ATOM   1266 S SD    . MET A 1 351 ? -13.033 56.730  76.999  1.00 104.00 ?  332 MET A SD    1 
ATOM   1267 C CE    . MET A 1 351 ? -11.841 55.507  77.517  1.00 101.41 ?  332 MET A CE    1 
ATOM   1268 N N     . VAL A 1 352 ? -13.110 55.084  82.183  1.00 100.70 ?  333 VAL A N     1 
ATOM   1269 C CA    . VAL A 1 352 ? -13.586 53.758  82.657  1.00 104.35 ?  333 VAL A CA    1 
ATOM   1270 C C     . VAL A 1 352 ? -13.370 53.593  84.148  1.00 105.78 ?  333 VAL A C     1 
ATOM   1271 O O     . VAL A 1 352 ? -12.351 54.027  84.640  1.00 109.89 ?  333 VAL A O     1 
ATOM   1272 C CB    . VAL A 1 352 ? -12.841 52.650  81.913  1.00 105.81 ?  333 VAL A CB    1 
ATOM   1273 C CG1   . VAL A 1 352 ? -13.033 52.795  80.425  1.00 110.20 ?  333 VAL A CG1   1 
ATOM   1274 C CG2   . VAL A 1 352 ? -11.366 52.693  82.238  1.00 105.84 ?  333 VAL A CG2   1 
ATOM   1275 N N     . VAL A 1 353 ? -14.308 52.919  84.796  1.00 102.96 ?  334 VAL A N     1 
ATOM   1276 C CA    . VAL A 1 353 ? -14.223 52.664  86.251  1.00 103.21 ?  334 VAL A CA    1 
ATOM   1277 C C     . VAL A 1 353 ? -13.541 51.316  86.353  1.00 99.80  ?  334 VAL A C     1 
ATOM   1278 O O     . VAL A 1 353 ? -14.166 50.349  85.999  1.00 102.95 ?  334 VAL A O     1 
ATOM   1279 C CB    . VAL A 1 353 ? -15.640 52.546  86.814  1.00 96.63  ?  334 VAL A CB    1 
ATOM   1280 C CG1   . VAL A 1 353 ? -15.622 51.873  88.158  1.00 96.81  ?  334 VAL A CG1   1 
ATOM   1281 C CG2   . VAL A 1 353 ? -16.340 53.881  86.891  1.00 86.40  ?  334 VAL A CG2   1 
ATOM   1282 N N     . THR A 1 354 ? -12.367 51.226  86.944  1.00 94.16  ?  335 THR A N     1 
ATOM   1283 C CA    . THR A 1 354 ? -11.710 49.910  86.853  1.00 96.92  ?  335 THR A CA    1 
ATOM   1284 C C     . THR A 1 354 ? -12.193 48.931  87.908  1.00 96.49  ?  335 THR A C     1 
ATOM   1285 O O     . THR A 1 354 ? -11.405 48.631  88.773  1.00 95.29  ?  335 THR A O     1 
ATOM   1286 C CB    . THR A 1 354 ? -10.192 50.053  86.863  1.00 96.88  ?  335 THR A CB    1 
ATOM   1287 O OG1   . THR A 1 354 ? -9.656  49.563  88.087  1.00 93.86  ?  335 THR A OG1   1 
ATOM   1288 C CG2   . THR A 1 354 ? -9.759  51.481  86.668  1.00 96.26  ?  335 THR A CG2   1 
ATOM   1289 N N     . GLY A 1 355 ? -13.412 48.422  87.790  1.00 97.48  ?  336 GLY A N     1 
ATOM   1290 C CA    . GLY A 1 355 ? -13.887 47.368  88.702  1.00 102.06 ?  336 GLY A CA    1 
ATOM   1291 C C     . GLY A 1 355 ? -14.508 47.886  89.972  1.00 104.02 ?  336 GLY A C     1 
ATOM   1292 O O     . GLY A 1 355 ? -13.882 48.691  90.633  1.00 110.20 ?  336 GLY A O     1 
ATOM   1293 N N     . LEU A 1 356 ? -15.677 47.370  90.321  1.00 101.59 ?  337 LEU A N     1 
ATOM   1294 C CA    . LEU A 1 356 ? -16.391 47.808  91.539  1.00 102.04 ?  337 LEU A CA    1 
ATOM   1295 C C     . LEU A 1 356 ? -15.946 46.966  92.726  1.00 113.79 ?  337 LEU A C     1 
ATOM   1296 O O     . LEU A 1 356 ? -16.403 47.229  93.833  1.00 114.55 ?  337 LEU A O     1 
ATOM   1297 C CB    . LEU A 1 356 ? -17.884 47.639  91.306  1.00 93.24  ?  337 LEU A CB    1 
ATOM   1298 C CG    . LEU A 1 356 ? -18.382 48.446  90.129  1.00 90.00  ?  337 LEU A CG    1 
ATOM   1299 C CD1   . LEU A 1 356 ? -19.798 48.911  90.362  1.00 81.67  ?  337 LEU A CD1   1 
ATOM   1300 C CD2   . LEU A 1 356 ? -17.461 49.621  89.945  1.00 101.09 ?  337 LEU A CD2   1 
ATOM   1301 N N     . GLY A 1 357 ? -15.089 45.978  92.517  1.00 111.95 ?  338 GLY A N     1 
ATOM   1302 C CA    . GLY A 1 357 ? -14.703 45.217  93.712  1.00 111.54 ?  338 GLY A CA    1 
ATOM   1303 C C     . GLY A 1 357 ? -13.840 46.088  94.592  1.00 110.38 ?  338 GLY A C     1 
ATOM   1304 O O     . GLY A 1 357 ? -12.792 46.517  94.142  1.00 112.38 ?  338 GLY A O     1 
ATOM   1305 N N     . GLY A 1 358 ? -14.306 46.368  95.799  1.00 108.35 ?  339 GLY A N     1 
ATOM   1306 C CA    . GLY A 1 358 ? -13.523 47.201  96.720  1.00 110.66 ?  339 GLY A CA    1 
ATOM   1307 C C     . GLY A 1 358 ? -13.256 48.540  96.090  1.00 105.74 ?  339 GLY A C     1 
ATOM   1308 O O     . GLY A 1 358 ? -12.123 48.990  96.092  1.00 105.10 ?  339 GLY A O     1 
ATOM   1309 N N     . ASN A 1 359 ? -14.283 49.163  95.549  1.00 104.03 ?  340 ASN A N     1 
ATOM   1310 C CA    . ASN A 1 359 ? -13.991 50.466  94.928  1.00 104.96 ?  340 ASN A CA    1 
ATOM   1311 C C     . ASN A 1 359 ? -14.866 51.537  95.552  1.00 105.33 ?  340 ASN A C     1 
ATOM   1312 O O     . ASN A 1 359 ? -16.073 51.401  95.545  1.00 103.58 ?  340 ASN A O     1 
ATOM   1313 C CB    . ASN A 1 359 ? -14.089 50.405  93.411  1.00 105.20 ?  340 ASN A CB    1 
ATOM   1314 C CG    . ASN A 1 359 ? -13.666 51.708  92.791  1.00 103.05 ?  340 ASN A CG    1 
ATOM   1315 O OD1   . ASN A 1 359 ? -13.917 52.749  93.364  1.00 108.21 ?  340 ASN A OD1   1 
ATOM   1316 N ND2   . ASN A 1 359 ? -12.997 51.659  91.659  1.00 100.44 ?  340 ASN A ND2   1 
ATOM   1317 N N     . PRO A 1 360 ? -14.276 52.680  95.925  1.00 106.42 ?  341 PRO A N     1 
ATOM   1318 C CA    . PRO A 1 360 ? -14.984 53.777  96.535  1.00 103.08 ?  341 PRO A CA    1 
ATOM   1319 C C     . PRO A 1 360 ? -16.003 54.352  95.558  1.00 103.81 ?  341 PRO A C     1 
ATOM   1320 O O     . PRO A 1 360 ? -17.101 54.577  95.944  1.00 104.71 ?  341 PRO A O     1 
ATOM   1321 C CB    . PRO A 1 360 ? -13.893 54.796  96.828  1.00 98.15  ?  341 PRO A CB    1 
ATOM   1322 C CG    . PRO A 1 360 ? -12.834 54.485  95.843  1.00 90.92  ?  341 PRO A CG    1 
ATOM   1323 C CD    . PRO A 1 360 ? -12.883 52.986  95.721  1.00 103.73 ?  341 PRO A CD    1 
ATOM   1324 N N     . MET A 1 361 ? -15.675 54.375  94.268  1.00 104.99 ?  342 MET A N     1 
ATOM   1325 C CA    . MET A 1 361 ? -16.543 54.937  93.205  1.00 102.02 ?  342 MET A CA    1 
ATOM   1326 C C     . MET A 1 361 ? -17.900 54.236  93.176  1.00 104.69 ?  342 MET A C     1 
ATOM   1327 O O     . MET A 1 361 ? -18.887 54.910  92.921  1.00 101.43 ?  342 MET A O     1 
ATOM   1328 C CB    . MET A 1 361 ? -15.872 54.815  91.842  1.00 98.29  ?  342 MET A CB    1 
ATOM   1329 C CG    . MET A 1 361 ? -14.506 55.451  91.782  1.00 101.60 ?  342 MET A CG    1 
ATOM   1330 S SD    . MET A 1 361 ? -14.582 57.210  91.877  1.00 105.26 ?  342 MET A SD    1 
ATOM   1331 C CE    . MET A 1 361 ? -16.355 57.408  91.788  1.00 102.39 ?  342 MET A CE    1 
ATOM   1332 N N     . ALA A 1 362 ? -17.974 52.950  93.506  1.00 104.93 ?  343 ALA A N     1 
ATOM   1333 C CA    . ALA A 1 362 ? -19.257 52.227  93.544  1.00 108.08 ?  343 ALA A CA    1 
ATOM   1334 C C     . ALA A 1 362 ? -20.212 52.948  94.481  1.00 113.91 ?  343 ALA A C     1 
ATOM   1335 O O     . ALA A 1 362 ? -21.303 53.280  94.049  1.00 114.53 ?  343 ALA A O     1 
ATOM   1336 C CB    . ALA A 1 362 ? -18.976 50.881  94.131  1.00 110.77 ?  343 ALA A CB    1 
ATOM   1337 N N     . VAL A 1 363 ? -19.737 53.350  95.654  1.00 114.92 ?  344 VAL A N     1 
ATOM   1338 C CA    . VAL A 1 363 ? -20.589 54.049  96.648  1.00 115.46 ?  344 VAL A CA    1 
ATOM   1339 C C     . VAL A 1 363 ? -21.140 55.317  96.012  1.00 112.06 ?  344 VAL A C     1 
ATOM   1340 O O     . VAL A 1 363 ? -22.344 55.517  96.046  1.00 111.35 ?  344 VAL A O     1 
ATOM   1341 C CB    . VAL A 1 363 ? -19.714 54.430  97.847  1.00 117.50 ?  344 VAL A CB    1 
ATOM   1342 C CG1   . VAL A 1 363 ? -20.261 55.641  98.567  1.00 113.31 ?  344 VAL A CG1   1 
ATOM   1343 C CG2   . VAL A 1 363 ? -19.536 53.269  98.799  1.00 113.80 ?  344 VAL A CG2   1 
ATOM   1344 N N     . VAL A 1 364 ? -20.301 56.052  95.298  1.00 111.16 ?  345 VAL A N     1 
ATOM   1345 C CA    . VAL A 1 364 ? -20.737 57.317  94.662  1.00 111.71 ?  345 VAL A CA    1 
ATOM   1346 C C     . VAL A 1 364 ? -21.877 57.025  93.696  1.00 116.75 ?  345 VAL A C     1 
ATOM   1347 O O     . VAL A 1 364 ? -22.897 57.716  93.766  1.00 117.98 ?  345 VAL A O     1 
ATOM   1348 C CB    . VAL A 1 364 ? -19.553 57.909  93.898  1.00 103.32 ?  345 VAL A CB    1 
ATOM   1349 C CG1   . VAL A 1 364 ? -19.748 59.385  93.656  1.00 98.29  ?  345 VAL A CG1   1 
ATOM   1350 C CG2   . VAL A 1 364 ? -18.260 57.653  94.630  1.00 95.00  ?  345 VAL A CG2   1 
ATOM   1351 N N     . SER A 1 365 ? -21.764 55.952  92.920  1.00 115.71 ?  346 SER A N     1 
ATOM   1352 C CA    . SER A 1 365 ? -22.820 55.634  91.938  1.00 118.40 ?  346 SER A CA    1 
ATOM   1353 C C     . SER A 1 365 ? -24.138 55.411  92.670  1.00 119.98 ?  346 SER A C     1 
ATOM   1354 O O     . SER A 1 365 ? -25.164 55.849  92.169  1.00 123.44 ?  346 SER A O     1 
ATOM   1355 C CB    . SER A 1 365 ? -22.440 54.424  91.194  1.00 114.88 ?  346 SER A CB    1 
ATOM   1356 O OG    . SER A 1 365 ? -22.746 53.291  91.973  1.00 116.28 ?  346 SER A OG    1 
ATOM   1357 N N     . LYS A 1 366 ? -24.114 54.717  93.796  1.00 114.35 ?  347 LYS A N     1 
ATOM   1358 C CA    . LYS A 1 366 ? -25.384 54.532  94.516  1.00 111.86 ?  347 LYS A CA    1 
ATOM   1359 C C     . LYS A 1 366 ? -25.911 55.914  94.907  1.00 118.38 ?  347 LYS A C     1 
ATOM   1360 O O     . LYS A 1 366 ? -27.110 56.112  94.812  1.00 122.67 ?  347 LYS A O     1 
ATOM   1361 C CB    . LYS A 1 366 ? -25.160 53.559  95.672  1.00 113.49 ?  347 LYS A CB    1 
ATOM   1362 C CG    . LYS A 1 366 ? -24.196 52.419  95.359  1.00 117.00 ?  347 LYS A CG    1 
ATOM   1363 C CD    . LYS A 1 366 ? -24.222 51.255  96.349  1.00 121.21 ?  347 LYS A CD    1 
ATOM   1364 C CE    . LYS A 1 366 ? -23.008 50.346  96.279  1.00 109.81 ?  347 LYS A CE    1 
ATOM   1365 N NZ    . LYS A 1 366 ? -22.739 49.644  97.556  1.00 89.04  ?  347 LYS A NZ    1 
ATOM   1366 N N     . GLN A 1 367 ? -25.030 56.849  95.262  1.00 121.42 ?  348 GLN A N     1 
ATOM   1367 C CA    . GLN A 1 367 ? -25.430 58.189  95.689  1.00 122.75 ?  348 GLN A CA    1 
ATOM   1368 C C     . GLN A 1 367 ? -25.773 59.077  94.500  1.00 118.75 ?  348 GLN A C     1 
ATOM   1369 O O     . GLN A 1 367 ? -26.823 59.726  94.485  1.00 117.90 ?  348 GLN A O     1 
ATOM   1370 C CB    . GLN A 1 367 ? -24.301 58.842  96.503  1.00 120.22 ?  348 GLN A CB    1 
ATOM   1371 C CG    . GLN A 1 367 ? -23.928 58.128  97.808  1.00 120.32 ?  348 GLN A CG    1 
ATOM   1372 C CD    . GLN A 1 367 ? -22.793 58.823  98.570  1.00 120.43 ?  348 GLN A CD    1 
ATOM   1373 O OE1   . GLN A 1 367 ? -22.328 59.894  98.178  1.00 119.76 ?  348 GLN A OE1   1 
ATOM   1374 N NE2   . GLN A 1 367 ? -22.329 58.196  99.648  1.00 122.29 ?  348 GLN A NE2   1 
ATOM   1375 N N     . VAL A 1 368 ? -24.875 59.112  93.509  1.00 119.50 ?  349 VAL A N     1 
ATOM   1376 C CA    . VAL A 1 368 ? -24.997 59.898  92.284  1.00 127.72 ?  349 VAL A CA    1 
ATOM   1377 C C     . VAL A 1 368 ? -25.832 59.133  91.258  1.00 138.26 ?  349 VAL A C     1 
ATOM   1378 O O     . VAL A 1 368 ? -25.899 57.894  91.264  1.00 139.69 ?  349 VAL A O     1 
ATOM   1379 C CB    . VAL A 1 368 ? -23.591 60.226  91.729  1.00 119.24 ?  349 VAL A CB    1 
ATOM   1380 C CG1   . VAL A 1 368 ? -23.659 61.229  90.586  1.00 121.65 ?  349 VAL A CG1   1 
ATOM   1381 C CG2   . VAL A 1 368 ? -22.701 60.726  92.831  1.00 114.48 ?  349 VAL A CG2   1 
ATOM   1382 N N     . ASN A 1 369 ? -26.478 59.869  90.352  1.00 142.78 ?  350 ASN A N     1 
ATOM   1383 C CA    . ASN A 1 369 ? -27.109 59.242  89.194  1.00 149.92 ?  350 ASN A CA    1 
ATOM   1384 C C     . ASN A 1 369 ? -26.025 58.904  88.177  1.00 144.64 ?  350 ASN A C     1 
ATOM   1385 O O     . ASN A 1 369 ? -25.442 59.800  87.552  1.00 139.37 ?  350 ASN A O     1 
ATOM   1386 C CB    . ASN A 1 369 ? -28.165 60.155  88.577  1.00 156.10 ?  350 ASN A CB    1 
ATOM   1387 C CG    . ASN A 1 369 ? -28.837 59.520  87.361  1.00 160.36 ?  350 ASN A CG    1 
ATOM   1388 O OD1   . ASN A 1 369 ? -28.841 58.286  87.209  1.00 157.36 ?  350 ASN A OD1   1 
ATOM   1389 N ND2   . ASN A 1 369 ? -29.404 60.358  86.488  1.00 156.72 ?  350 ASN A ND2   1 
ATOM   1390 N N     . MET A 1 370 ? -25.741 57.620  88.000  1.00 142.61 ?  351 MET A N     1 
ATOM   1391 C CA    . MET A 1 370 ? -24.719 57.246  87.035  1.00 144.68 ?  351 MET A CA    1 
ATOM   1392 C C     . MET A 1 370 ? -25.154 56.037  86.232  1.00 145.94 ?  351 MET A C     1 
ATOM   1393 O O     . MET A 1 370 ? -25.422 54.968  86.794  1.00 148.94 ?  351 MET A O     1 
ATOM   1394 C CB    . MET A 1 370 ? -23.397 56.960  87.716  1.00 138.45 ?  351 MET A CB    1 
ATOM   1395 C CG    . MET A 1 370 ? -22.827 58.121  88.425  1.00 134.28 ?  351 MET A CG    1 
ATOM   1396 S SD    . MET A 1 370 ? -21.260 57.487  88.949  1.00 137.62 ?  351 MET A SD    1 
ATOM   1397 C CE    . MET A 1 370 ? -20.568 57.167  87.343  1.00 127.49 ?  351 MET A CE    1 
ATOM   1398 N N     . GLU A 1 371 ? -25.194 56.218  84.917  1.00 140.98 ?  352 GLU A N     1 
ATOM   1399 C CA    . GLU A 1 371 ? -25.356 55.141  83.951  1.00 140.55 ?  352 GLU A CA    1 
ATOM   1400 C C     . GLU A 1 371 ? -24.019 54.421  83.813  1.00 138.80 ?  352 GLU A C     1 
ATOM   1401 O O     . GLU A 1 371 ? -23.185 54.769  82.974  1.00 138.32 ?  352 GLU A O     1 
ATOM   1402 C CB    . GLU A 1 371 ? -25.826 55.710  82.620  1.00 144.59 ?  352 GLU A CB    1 
ATOM   1403 C CG    . GLU A 1 371 ? -26.453 54.721  81.654  1.00 149.41 ?  352 GLU A CG    1 
ATOM   1404 C CD    . GLU A 1 371 ? -27.277 55.422  80.579  1.00 156.90 ?  352 GLU A CD    1 
ATOM   1405 O OE1   . GLU A 1 371 ? -27.397 56.674  80.638  1.00 150.28 ?  352 GLU A OE1   1 
ATOM   1406 O OE2   . GLU A 1 371 ? -27.748 54.728  79.643  1.00 161.14 ?  352 GLU A OE2   1 
ATOM   1407 N N     . LEU A 1 372 ? -23.805 53.411  84.656  1.00 132.25 ?  353 LEU A N     1 
ATOM   1408 C CA    . LEU A 1 372 ? -22.646 52.531  84.540  1.00 126.46 ?  353 LEU A CA    1 
ATOM   1409 C C     . LEU A 1 372 ? -22.986 51.348  83.645  1.00 131.89 ?  353 LEU A C     1 
ATOM   1410 O O     . LEU A 1 372 ? -23.824 50.515  84.013  1.00 139.49 ?  353 LEU A O     1 
ATOM   1411 C CB    . LEU A 1 372 ? -22.210 52.024  85.904  1.00 122.03 ?  353 LEU A CB    1 
ATOM   1412 C CG    . LEU A 1 372 ? -21.651 52.939  86.958  1.00 116.45 ?  353 LEU A CG    1 
ATOM   1413 C CD1   . LEU A 1 372 ? -21.473 52.068  88.158  1.00 108.04 ?  353 LEU A CD1   1 
ATOM   1414 C CD2   . LEU A 1 372 ? -20.310 53.440  86.480  1.00 110.39 ?  353 LEU A CD2   1 
ATOM   1415 N N     . ALA A 1 373 ? -22.317 51.249  82.490  1.00 129.12 ?  354 ALA A N     1 
ATOM   1416 C CA    . ALA A 1 373 ? -22.466 50.109  81.586  1.00 126.55 ?  354 ALA A CA    1 
ATOM   1417 C C     . ALA A 1 373 ? -21.142 49.364  81.469  1.00 123.96 ?  354 ALA A C     1 
ATOM   1418 O O     . ALA A 1 373 ? -20.076 49.988  81.378  1.00 125.10 ?  354 ALA A O     1 
ATOM   1419 C CB    . ALA A 1 373 ? -22.940 50.550  80.201  1.00 125.78 ?  354 ALA A CB    1 
ATOM   1420 N N     . LYS A 1 374 ? -21.205 48.030  81.478  1.00 114.48 ?  355 LYS A N     1 
ATOM   1421 C CA    . LYS A 1 374 ? -19.976 47.256  81.415  1.00 113.71 ?  355 LYS A CA    1 
ATOM   1422 C C     . LYS A 1 374 ? -19.311 47.392  80.042  1.00 116.57 ?  355 LYS A C     1 
ATOM   1423 O O     . LYS A 1 374 ? -19.963 47.617  79.015  1.00 113.84 ?  355 LYS A O     1 
ATOM   1424 C CB    . LYS A 1 374 ? -20.243 45.784  81.720  1.00 112.20 ?  355 LYS A CB    1 
ATOM   1425 C CG    . LYS A 1 374 ? -20.832 45.474  83.094  1.00 114.92 ?  355 LYS A CG    1 
ATOM   1426 C CD    . LYS A 1 374 ? -20.819 43.936  83.332  1.00 123.92 ?  355 LYS A CD    1 
ATOM   1427 C CE    . LYS A 1 374 ? -21.295 43.476  84.738  1.00 117.89 ?  355 LYS A CE    1 
ATOM   1428 N NZ    . LYS A 1 374 ? -21.153 41.989  84.984  1.00 102.68 ?  355 LYS A NZ    1 
ATOM   1429 N N     . ILE A 1 375 ? -17.992 47.283  80.039  1.00 116.18 ?  356 ILE A N     1 
ATOM   1430 C CA    . ILE A 1 375 ? -17.242 47.074  78.810  1.00 116.00 ?  356 ILE A CA    1 
ATOM   1431 C C     . ILE A 1 375 ? -17.064 45.578  78.593  1.00 127.64 ?  356 ILE A C     1 
ATOM   1432 O O     . ILE A 1 375 ? -16.630 44.850  79.505  1.00 126.50 ?  356 ILE A O     1 
ATOM   1433 C CB    . ILE A 1 375 ? -15.882 47.788  78.850  1.00 112.52 ?  356 ILE A CB    1 
ATOM   1434 C CG1   . ILE A 1 375 ? -16.058 49.292  78.826  1.00 110.80 ?  356 ILE A CG1   1 
ATOM   1435 C CG2   . ILE A 1 375 ? -14.981 47.340  77.718  1.00 123.94 ?  356 ILE A CG2   1 
ATOM   1436 C CD1   . ILE A 1 375 ? -14.760 49.987  79.037  1.00 110.63 ?  356 ILE A CD1   1 
ATOM   1437 N N     . LYS A 1 376 ? -17.365 45.130  77.374  1.00 128.77 ?  357 LYS A N     1 
ATOM   1438 C CA    . LYS A 1 376 ? -17.141 43.722  76.972  1.00 124.28 ?  357 LYS A CA    1 
ATOM   1439 C C     . LYS A 1 376 ? -15.687 43.657  76.530  1.00 121.63 ?  357 LYS A C     1 
ATOM   1440 O O     . LYS A 1 376 ? -15.372 44.291  75.545  1.00 118.12 ?  357 LYS A O     1 
ATOM   1441 C CB    . LYS A 1 376 ? -18.020 43.385  75.772  1.00 124.71 ?  357 LYS A CB    1 
ATOM   1442 C CG    . LYS A 1 376 ? -19.455 43.878  75.864  1.00 126.97 ?  357 LYS A CG    1 
ATOM   1443 C CD    . LYS A 1 376 ? -20.436 42.953  75.180  1.00 133.56 ?  357 LYS A CD    1 
ATOM   1444 C CE    . LYS A 1 376 ? -21.880 43.263  75.510  1.00 138.13 ?  357 LYS A CE    1 
ATOM   1445 N NZ    . LYS A 1 376 ? -22.627 43.764  74.332  1.00 136.37 ?  357 LYS A NZ    1 
ATOM   1446 N N     . GLN A 1 377 ? -14.879 42.802  77.144  1.00 123.87 ?  358 GLN A N     1 
ATOM   1447 C CA    . GLN A 1 377 ? -13.411 42.776  76.902  1.00 126.84 ?  358 GLN A CA    1 
ATOM   1448 C C     . GLN A 1 377 ? -13.007 42.405  75.468  1.00 127.86 ?  358 GLN A C     1 
ATOM   1449 O O     . GLN A 1 377 ? -11.850 42.664  75.134  1.00 123.50 ?  358 GLN A O     1 
ATOM   1450 C CB    . GLN A 1 377 ? -12.686 41.968  77.980  1.00 130.84 ?  358 GLN A CB    1 
ATOM   1451 C CG    . GLN A 1 377 ? -13.352 42.021  79.353  1.00 144.68 ?  358 GLN A CG    1 
ATOM   1452 C CD    . GLN A 1 377 ? -12.865 43.086  80.313  1.00 142.58 ?  358 GLN A CD    1 
ATOM   1453 O OE1   . GLN A 1 377 ? -11.709 43.505  80.297  1.00 142.69 ?  358 GLN A OE1   1 
ATOM   1454 N NE2   . GLN A 1 377 ? -13.754 43.521  81.191  1.00 117.85 ?  358 GLN A NE2   1 
ATOM   1455 N N     . LYS A 1 378 ? -13.861 41.736  74.696  1.00 129.66 ?  359 LYS A N     1 
ATOM   1456 C CA    . LYS A 1 378 ? -13.540 41.344  73.298  1.00 126.71 ?  359 LYS A CA    1 
ATOM   1457 C C     . LYS A 1 378 ? -12.932 42.511  72.522  1.00 122.33 ?  359 LYS A C     1 
ATOM   1458 O O     . LYS A 1 378 ? -13.592 43.528  72.423  1.00 122.94 ?  359 LYS A O     1 
ATOM   1459 C CB    . LYS A 1 378 ? -14.827 40.941  72.579  1.00 126.08 ?  359 LYS A CB    1 
ATOM   1460 C CG    . LYS A 1 378 ? -14.679 40.675  71.089  1.00 128.51 ?  359 LYS A CG    1 
ATOM   1461 C CD    . LYS A 1 378 ? -15.592 39.575  70.587  1.00 135.39 ?  359 LYS A CD    1 
ATOM   1462 C CE    . LYS A 1 378 ? -15.394 39.232  69.125  1.00 130.31 ?  359 LYS A CE    1 
ATOM   1463 N NZ    . LYS A 1 378 ? -16.638 38.719  68.507  1.00 121.27 ?  359 LYS A NZ    1 
ATOM   1464 N N     . CYS A 1 379 ? -11.730 42.327  71.976  1.00 117.09 ?  360 CYS A N     1 
ATOM   1465 C CA    . CYS A 1 379 ? -11.021 43.322  71.176  1.00 118.36 ?  360 CYS A CA    1 
ATOM   1466 C C     . CYS A 1 379 ? -10.430 42.636  69.948  1.00 117.08 ?  360 CYS A C     1 
ATOM   1467 O O     . CYS A 1 379 ? -9.411  41.936  70.040  1.00 119.10 ?  360 CYS A O     1 
ATOM   1468 C CB    . CYS A 1 379 ? -9.951  44.009  72.024  1.00 119.20 ?  360 CYS A CB    1 
ATOM   1469 S SG    . CYS A 1 379 ? -8.876  45.298  71.268  1.00 117.07 ?  360 CYS A SG    1 
ATOM   1470 N N     . PRO A 1 380 ? -11.039 42.795  68.775  1.00 108.15 ?  361 PRO A N     1 
ATOM   1471 C CA    . PRO A 1 380 ? -10.353 42.435  67.527  1.00 107.52 ?  361 PRO A CA    1 
ATOM   1472 C C     . PRO A 1 380 ? -9.109  43.280  67.285  1.00 104.94 ?  361 PRO A C     1 
ATOM   1473 O O     . PRO A 1 380 ? -8.814  44.221  68.011  1.00 111.59 ?  361 PRO A O     1 
ATOM   1474 C CB    . PRO A 1 380 ? -11.420 42.677  66.458  1.00 107.05 ?  361 PRO A CB    1 
ATOM   1475 C CG    . PRO A 1 380 ? -12.396 43.609  67.084  1.00 108.28 ?  361 PRO A CG    1 
ATOM   1476 C CD    . PRO A 1 380 ? -12.425 43.245  68.545  1.00 107.15 ?  361 PRO A CD    1 
ATOM   1477 N N     . LEU A 1 381 ? -8.371  42.929  66.233  1.00 107.21 ?  362 LEU A N     1 
ATOM   1478 C CA    . LEU A 1 381 ? -7.180  43.653  65.784  1.00 109.89 ?  362 LEU A CA    1 
ATOM   1479 C C     . LEU A 1 381 ? -7.196  43.760  64.261  1.00 116.46 ?  362 LEU A C     1 
ATOM   1480 O O     . LEU A 1 381 ? -7.810  42.940  63.574  1.00 122.35 ?  362 LEU A O     1 
ATOM   1481 C CB    . LEU A 1 381 ? -5.890  42.949  66.240  1.00 108.92 ?  362 LEU A CB    1 
ATOM   1482 C CG    . LEU A 1 381 ? -5.685  42.849  67.741  1.00 106.13 ?  362 LEU A CG    1 
ATOM   1483 C CD1   . LEU A 1 381 ? -4.346  42.227  68.040  1.00 109.35 ?  362 LEU A CD1   1 
ATOM   1484 C CD2   . LEU A 1 381 ? -5.693  44.260  68.240  1.00 108.80 ?  362 LEU A CD2   1 
ATOM   1485 N N     . TYR A 1 382 ? -6.557  44.791  63.719  1.00 113.21 ?  363 TYR A N     1 
ATOM   1486 C CA    . TYR A 1 382 ? -6.618  45.011  62.273  1.00 111.19 ?  363 TYR A CA    1 
ATOM   1487 C C     . TYR A 1 382 ? -5.310  45.640  61.856  1.00 117.56 ?  363 TYR A C     1 
ATOM   1488 O O     . TYR A 1 382 ? -5.040  46.788  62.230  1.00 120.28 ?  363 TYR A O     1 
ATOM   1489 C CB    . TYR A 1 382 ? -7.782  45.920  61.875  1.00 106.01 ?  363 TYR A CB    1 
ATOM   1490 C CG    . TYR A 1 382 ? -9.131  45.378  62.248  1.00 102.70 ?  363 TYR A CG    1 
ATOM   1491 C CD1   . TYR A 1 382 ? -9.611  45.482  63.537  1.00 110.55 ?  363 TYR A CD1   1 
ATOM   1492 C CD2   . TYR A 1 382 ? -9.926  44.771  61.316  1.00 112.34 ?  363 TYR A CD2   1 
ATOM   1493 C CE1   . TYR A 1 382 ? -10.835 44.974  63.889  1.00 109.22 ?  363 TYR A CE1   1 
ATOM   1494 C CE2   . TYR A 1 382 ? -11.160 44.278  61.648  1.00 109.40 ?  363 TYR A CE2   1 
ATOM   1495 C CZ    . TYR A 1 382 ? -11.612 44.387  62.932  1.00 106.64 ?  363 TYR A CZ    1 
ATOM   1496 O OH    . TYR A 1 382 ? -12.846 43.896  63.277  1.00 111.05 ?  363 TYR A OH    1 
ATOM   1497 N N     . GLU A 1 383 ? -4.597  44.997  60.945  1.00 118.31 ?  364 GLU A N     1 
ATOM   1498 C CA    . GLU A 1 383 ? -3.280  45.532  60.531  1.00 115.64 ?  364 GLU A CA    1 
ATOM   1499 C C     . GLU A 1 383 ? -3.416  46.705  59.558  1.00 120.11 ?  364 GLU A C     1 
ATOM   1500 O O     . GLU A 1 383 ? -4.533  47.070  59.146  1.00 118.62 ?  364 GLU A O     1 
ATOM   1501 C CB    . GLU A 1 383 ? -2.421  44.408  59.964  1.00 110.96 ?  364 GLU A CB    1 
ATOM   1502 C CG    . GLU A 1 383 ? -2.530  43.133  60.771  1.00 122.40 ?  364 GLU A CG    1 
ATOM   1503 C CD    . GLU A 1 383 ? -3.155  41.926  60.090  1.00 138.16 ?  364 GLU A CD    1 
ATOM   1504 O OE1   . GLU A 1 383 ? -2.472  41.310  59.257  1.00 142.59 ?  364 GLU A OE1   1 
ATOM   1505 O OE2   . GLU A 1 383 ? -4.308  41.580  60.417  1.00 138.38 ?  364 GLU A OE2   1 
ATOM   1506 N N     . ALA A 1 384 ? -2.285  47.133  59.010  1.00 120.50 ?  365 ALA A N     1 
ATOM   1507 C CA    . ALA A 1 384 ? -2.244  48.317  58.126  1.00 120.98 ?  365 ALA A CA    1 
ATOM   1508 C C     . ALA A 1 384 ? -3.171  48.146  56.917  1.00 130.55 ?  365 ALA A C     1 
ATOM   1509 O O     . ALA A 1 384 ? -3.869  49.101  56.584  1.00 132.79 ?  365 ALA A O     1 
ATOM   1510 C CB    . ALA A 1 384 ? -0.822  48.557  57.707  1.00 113.20 ?  365 ALA A CB    1 
ATOM   1511 N N     . ASN A 1 385 ? -3.264  46.939  56.363  1.00 129.83 ?  366 ASN A N     1 
ATOM   1512 C CA    . ASN A 1 385 ? -4.104  46.608  55.189  1.00 122.05 ?  366 ASN A CA    1 
ATOM   1513 C C     . ASN A 1 385 ? -5.601  46.812  55.446  1.00 124.59 ?  366 ASN A C     1 
ATOM   1514 O O     . ASN A 1 385 ? -6.321  46.963  54.463  1.00 121.73 ?  366 ASN A O     1 
ATOM   1515 C CB    . ASN A 1 385 ? -3.891  45.151  54.804  1.00 118.63 ?  366 ASN A CB    1 
ATOM   1516 C CG    . ASN A 1 385 ? -4.180  44.219  55.953  1.00 127.57 ?  366 ASN A CG    1 
ATOM   1517 O OD1   . ASN A 1 385 ? -4.744  44.626  56.957  1.00 132.48 ?  366 ASN A OD1   1 
ATOM   1518 N ND2   . ASN A 1 385 ? -3.813  42.961  55.807  1.00 123.13 ?  366 ASN A ND2   1 
ATOM   1519 N N     . GLY A 1 386 ? -6.073  46.780  56.690  1.00 128.67 ?  367 GLY A N     1 
ATOM   1520 C CA    . GLY A 1 386 ? -7.520  46.884  56.937  1.00 127.28 ?  367 GLY A CA    1 
ATOM   1521 C C     . GLY A 1 386 ? -8.143  45.504  56.959  1.00 124.03 ?  367 GLY A C     1 
ATOM   1522 O O     . GLY A 1 386 ? -9.368  45.408  57.011  1.00 117.25 ?  367 GLY A O     1 
ATOM   1523 N N     . GLN A 1 387 ? -7.307  44.470  56.903  1.00 124.69 ?  368 GLN A N     1 
ATOM   1524 C CA    . GLN A 1 387 ? -7.787  43.073  56.952  1.00 124.10 ?  368 GLN A CA    1 
ATOM   1525 C C     . GLN A 1 387 ? -7.685  42.625  58.405  1.00 119.10 ?  368 GLN A C     1 
ATOM   1526 O O     . GLN A 1 387 ? -6.662  42.879  59.014  1.00 120.36 ?  368 GLN A O     1 
ATOM   1527 C CB    . GLN A 1 387 ? -6.960  42.183  56.024  1.00 129.12 ?  368 GLN A CB    1 
ATOM   1528 C CG    . GLN A 1 387 ? -6.893  42.698  54.593  1.00 139.13 ?  368 GLN A CG    1 
ATOM   1529 C CD    . GLN A 1 387 ? -7.505  41.795  53.549  1.00 151.55 ?  368 GLN A CD    1 
ATOM   1530 O OE1   . GLN A 1 387 ? -7.019  40.702  53.278  1.00 156.28 ?  368 GLN A OE1   1 
ATOM   1531 N NE2   . GLN A 1 387 ? -8.571  42.265  52.922  1.00 149.91 ?  368 GLN A NE2   1 
ATOM   1532 N N     . ALA A 1 388 ? -8.718  41.968  58.916  1.00 112.45 ?  369 ALA A N     1 
ATOM   1533 C CA    . ALA A 1 388 ? -8.749  41.528  60.323  1.00 114.36 ?  369 ALA A CA    1 
ATOM   1534 C C     . ALA A 1 388 ? -7.652  40.507  60.602  1.00 119.07 ?  369 ALA A C     1 
ATOM   1535 O O     . ALA A 1 388 ? -7.333  39.724  59.732  1.00 121.61 ?  369 ALA A O     1 
ATOM   1536 C CB    . ALA A 1 388 ? -10.091 40.931  60.613  1.00 111.36 ?  369 ALA A CB    1 
ATOM   1537 N N     . VAL A 1 389 ? -7.103  40.535  61.808  1.00 122.08 ?  370 VAL A N     1 
ATOM   1538 C CA    . VAL A 1 389 ? -6.060  39.556  62.205  1.00 125.76 ?  370 VAL A CA    1 
ATOM   1539 C C     . VAL A 1 389 ? -6.724  38.210  62.430  1.00 134.72 ?  370 VAL A C     1 
ATOM   1540 O O     . VAL A 1 389 ? -7.888  38.185  62.814  1.00 136.57 ?  370 VAL A O     1 
ATOM   1541 C CB    . VAL A 1 389 ? -5.359  39.997  63.487  1.00 122.88 ?  370 VAL A CB    1 
ATOM   1542 C CG1   . VAL A 1 389 ? -3.902  39.594  63.452  1.00 126.93 ?  370 VAL A CG1   1 
ATOM   1543 C CG2   . VAL A 1 389 ? -5.513  41.492  63.684  1.00 124.06 ?  370 VAL A CG2   1 
ATOM   1544 N N     . PRO A 1 390 ? -5.978  37.103  62.306  1.00 136.22 ?  371 PRO A N     1 
ATOM   1545 C CA    . PRO A 1 390 ? -6.532  35.770  62.426  1.00 131.55 ?  371 PRO A CA    1 
ATOM   1546 C C     . PRO A 1 390 ? -6.220  35.135  63.780  1.00 128.54 ?  371 PRO A C     1 
ATOM   1547 O O     . PRO A 1 390 ? -5.115  35.293  64.249  1.00 127.14 ?  371 PRO A O     1 
ATOM   1548 C CB    . PRO A 1 390 ? -5.650  35.081  61.395  1.00 134.47 ?  371 PRO A CB    1 
ATOM   1549 C CG    . PRO A 1 390 ? -4.289  35.642  61.699  1.00 132.21 ?  371 PRO A CG    1 
ATOM   1550 C CD    . PRO A 1 390 ? -4.549  37.087  62.057  1.00 131.04 ?  371 PRO A CD    1 
ATOM   1551 N N     . LYS A 1 391 ? -7.220  34.450  64.333  1.00 127.48 ?  372 LYS A N     1 
ATOM   1552 C CA    . LYS A 1 391 ? -7.152  33.760  65.645  1.00 131.32 ?  372 LYS A CA    1 
ATOM   1553 C C     . LYS A 1 391 ? -5.809  33.050  65.810  1.00 129.39 ?  372 LYS A C     1 
ATOM   1554 O O     . LYS A 1 391 ? -5.328  33.023  66.923  1.00 128.03 ?  372 LYS A O     1 
ATOM   1555 C CB    . LYS A 1 391 ? -8.326  32.794  65.798  1.00 128.89 ?  372 LYS A CB    1 
ATOM   1556 C CG    . LYS A 1 391 ? -9.551  33.373  66.489  1.00 134.61 ?  372 LYS A CG    1 
ATOM   1557 C CD    . LYS A 1 391 ? -10.278 32.387  67.373  1.00 128.67 ?  372 LYS A CD    1 
ATOM   1558 C CE    . LYS A 1 391 ? -11.060 33.057  68.483  1.00 134.88 ?  372 LYS A CE    1 
ATOM   1559 N NZ    . LYS A 1 391 ? -12.490 33.248  68.135  1.00 123.55 ?  372 LYS A NZ    1 
ATOM   1560 N N     . GLU A 1 392 ? -5.269  32.470  64.741  1.00 141.27 ?  373 GLU A N     1 
ATOM   1561 C CA    . GLU A 1 392 ? -3.950  31.849  64.796  1.00 143.17 ?  373 GLU A CA    1 
ATOM   1562 C C     . GLU A 1 392 ? -2.939  32.845  65.358  1.00 133.49 ?  373 GLU A C     1 
ATOM   1563 O O     . GLU A 1 392 ? -2.386  32.642  66.441  1.00 129.14 ?  373 GLU A O     1 
ATOM   1564 C CB    . GLU A 1 392 ? -3.531  31.374  63.389  1.00 152.90 ?  373 GLU A CB    1 
ATOM   1565 C CG    . GLU A 1 392 ? -4.130  30.027  62.889  1.00 156.25 ?  373 GLU A CG    1 
ATOM   1566 C CD    . GLU A 1 392 ? -3.314  28.781  63.262  1.00 167.14 ?  373 GLU A CD    1 
ATOM   1567 O OE1   . GLU A 1 392 ? -2.183  28.920  63.784  1.00 166.59 ?  373 GLU A OE1   1 
ATOM   1568 O OE2   . GLU A 1 392 ? -3.805  27.653  63.005  1.00 166.14 ?  373 GLU A OE2   1 
ATOM   1569 N N     . LYS A 1 393 ? -2.746  33.972  64.659  1.00 133.97 ?  374 LYS A N     1 
ATOM   1570 C CA    . LYS A 1 393 ? -1.694  34.919  65.020  1.00 133.64 ?  374 LYS A CA    1 
ATOM   1571 C C     . LYS A 1 393 ? -2.058  35.779  66.233  1.00 135.60 ?  374 LYS A C     1 
ATOM   1572 O O     . LYS A 1 393 ? -1.194  36.044  67.081  1.00 133.02 ?  374 LYS A O     1 
ATOM   1573 C CB    . LYS A 1 393 ? -1.345  35.797  63.821  1.00 125.81 ?  374 LYS A CB    1 
ATOM   1574 C CG    . LYS A 1 393 ? -0.219  35.213  63.013  1.00 132.06 ?  374 LYS A CG    1 
ATOM   1575 C CD    . LYS A 1 393 ? 0.649   36.293  62.404  1.00 136.70 ?  374 LYS A CD    1 
ATOM   1576 C CE    . LYS A 1 393 ? 1.797   35.674  61.626  1.00 140.53 ?  374 LYS A CE    1 
ATOM   1577 N NZ    . LYS A 1 393 ? 2.672   34.929  62.583  1.00 138.10 ?  374 LYS A NZ    1 
ATOM   1578 N N     . ASP A 1 394 ? -3.314  36.236  66.327  1.00 136.57 ?  375 ASP A N     1 
ATOM   1579 C CA    . ASP A 1 394 ? -3.753  37.019  67.485  1.00 128.47 ?  375 ASP A CA    1 
ATOM   1580 C C     . ASP A 1 394 ? -3.320  36.351  68.790  1.00 125.60 ?  375 ASP A C     1 
ATOM   1581 O O     . ASP A 1 394 ? -2.670  36.976  69.637  1.00 126.05 ?  375 ASP A O     1 
ATOM   1582 C CB    . ASP A 1 394 ? -5.278  37.196  67.434  1.00 125.50 ?  375 ASP A CB    1 
ATOM   1583 C CG    . ASP A 1 394 ? -5.778  38.371  68.266  1.00 126.08 ?  375 ASP A CG    1 
ATOM   1584 O OD1   . ASP A 1 394 ? -4.953  39.084  68.897  1.00 126.37 ?  375 ASP A OD1   1 
ATOM   1585 O OD2   . ASP A 1 394 ? -7.017  38.568  68.294  1.00 124.33 ?  375 ASP A OD2   1 
ATOM   1586 N N     . GLU A 1 395 ? -3.625  35.057  68.934  1.00 122.27 ?  376 GLU A N     1 
ATOM   1587 C CA    . GLU A 1 395 ? -3.290  34.319  70.149  1.00 120.86 ?  376 GLU A CA    1 
ATOM   1588 C C     . GLU A 1 395 ? -1.802  33.985  70.225  1.00 120.47 ?  376 GLU A C     1 
ATOM   1589 O O     . GLU A 1 395 ? -1.212  34.023  71.308  1.00 118.61 ?  376 GLU A O     1 
ATOM   1590 C CB    . GLU A 1 395 ? -4.111  33.034  70.214  1.00 122.30 ?  376 GLU A CB    1 
ATOM   1591 C CG    . GLU A 1 395 ? -5.622  33.232  70.222  1.00 126.11 ?  376 GLU A CG    1 
ATOM   1592 C CD    . GLU A 1 395 ? -6.385  31.919  70.441  1.00 130.74 ?  376 GLU A CD    1 
ATOM   1593 O OE1   . GLU A 1 395 ? -5.740  30.865  70.667  1.00 125.39 ?  376 GLU A OE1   1 
ATOM   1594 O OE2   . GLU A 1 395 ? -7.635  31.943  70.383  1.00 136.57 ?  376 GLU A OE2   1 
ATOM   1595 N N     . MET A 1 396 ? -1.191  33.607  69.095  1.00 127.99 ?  377 MET A N     1 
ATOM   1596 C CA    . MET A 1 396 ? 0.249   33.339  69.067  1.00 128.57 ?  377 MET A CA    1 
ATOM   1597 C C     . MET A 1 396 ? 1.034   34.542  69.584  1.00 126.34 ?  377 MET A C     1 
ATOM   1598 O O     . MET A 1 396 ? 1.982   34.386  70.365  1.00 123.58 ?  377 MET A O     1 
ATOM   1599 C CB    . MET A 1 396 ? 0.707   32.978  67.638  1.00 135.32 ?  377 MET A CB    1 
ATOM   1600 C CG    . MET A 1 396 ? 0.455   31.507  67.131  1.00 149.18 ?  377 MET A CG    1 
ATOM   1601 S SD    . MET A 1 396 ? 0.713   31.165  65.317  1.00 175.61 ?  377 MET A SD    1 
ATOM   1602 C CE    . MET A 1 396 ? 0.559   29.365  65.220  1.00 153.56 ?  377 MET A CE    1 
ATOM   1603 N N     . VAL A 1 397 ? 0.630   35.753  69.171  1.00 126.62 ?  378 VAL A N     1 
ATOM   1604 C CA    . VAL A 1 397 ? 1.322   36.984  69.568  1.00 122.91 ?  378 VAL A CA    1 
ATOM   1605 C C     . VAL A 1 397 ? 1.104   37.277  71.048  1.00 124.66 ?  378 VAL A C     1 
ATOM   1606 O O     . VAL A 1 397 ? 2.060   37.410  71.830  1.00 117.35 ?  378 VAL A O     1 
ATOM   1607 C CB    . VAL A 1 397 ? 0.850   38.167  68.703  1.00 117.17 ?  378 VAL A CB    1 
ATOM   1608 C CG1   . VAL A 1 397 ? 1.343   39.490  69.281  1.00 118.99 ?  378 VAL A CG1   1 
ATOM   1609 C CG2   . VAL A 1 397 ? 1.359   38.012  67.293  1.00 121.28 ?  378 VAL A CG2   1 
ATOM   1610 N N     . GLU A 1 398 ? -0.167  37.385  71.446  1.00 126.63 ?  379 GLU A N     1 
ATOM   1611 C CA    . GLU A 1 398 ? -0.498  37.911  72.764  1.00 120.60 ?  379 GLU A CA    1 
ATOM   1612 C C     . GLU A 1 398 ? 0.138   37.077  73.865  1.00 116.84 ?  379 GLU A C     1 
ATOM   1613 O O     . GLU A 1 398 ? 0.757   37.629  74.777  1.00 119.70 ?  379 GLU A O     1 
ATOM   1614 C CB    . GLU A 1 398 ? -2.019  38.004  72.920  1.00 121.25 ?  379 GLU A CB    1 
ATOM   1615 C CG    . GLU A 1 398 ? -2.503  38.432  74.291  1.00 121.34 ?  379 GLU A CG    1 
ATOM   1616 C CD    . GLU A 1 398 ? -3.975  38.816  74.275  1.00 128.18 ?  379 GLU A CD    1 
ATOM   1617 O OE1   . GLU A 1 398 ? -4.483  39.117  73.169  1.00 130.43 ?  379 GLU A OE1   1 
ATOM   1618 O OE2   . GLU A 1 398 ? -4.614  38.838  75.355  1.00 128.49 ?  379 GLU A OE2   1 
ATOM   1619 N N     . GLN A 1 399 ? 0.043   35.742  73.779  1.00 118.61 ?  380 GLN A N     1 
ATOM   1620 C CA    . GLN A 1 399 ? 0.655   34.910  74.815  1.00 121.62 ?  380 GLN A CA    1 
ATOM   1621 C C     . GLN A 1 399 ? 2.165   35.113  74.870  1.00 123.27 ?  380 GLN A C     1 
ATOM   1622 O O     . GLN A 1 399 ? 2.764   35.079  75.956  1.00 125.03 ?  380 GLN A O     1 
ATOM   1623 C CB    . GLN A 1 399 ? 0.363   33.427  74.603  1.00 127.02 ?  380 GLN A CB    1 
ATOM   1624 C CG    . GLN A 1 399 ? 1.222   32.574  75.559  1.00 138.68 ?  380 GLN A CG    1 
ATOM   1625 C CD    . GLN A 1 399 ? 1.130   31.077  75.338  1.00 141.65 ?  380 GLN A CD    1 
ATOM   1626 O OE1   . GLN A 1 399 ? 0.418   30.612  74.446  1.00 132.90 ?  380 GLN A OE1   1 
ATOM   1627 N NE2   . GLN A 1 399 ? 1.846   30.309  76.170  1.00 137.48 ?  380 GLN A NE2   1 
ATOM   1628 N N     . GLU A 1 400 ? 2.804   35.313  73.711  1.00 120.08 ?  381 GLU A N     1 
ATOM   1629 C CA    . GLU A 1 400 ? 4.243   35.551  73.727  1.00 122.17 ?  381 GLU A CA    1 
ATOM   1630 C C     . GLU A 1 400 ? 4.571   36.913  74.331  1.00 120.33 ?  381 GLU A C     1 
ATOM   1631 O O     . GLU A 1 400 ? 5.607   37.070  74.994  1.00 119.22 ?  381 GLU A O     1 
ATOM   1632 C CB    . GLU A 1 400 ? 4.824   35.406  72.318  1.00 117.10 ?  381 GLU A CB    1 
ATOM   1633 C CG    . GLU A 1 400 ? 6.349   35.575  72.270  1.00 116.68 ?  381 GLU A CG    1 
ATOM   1634 C CD    . GLU A 1 400 ? 7.116   34.381  72.861  1.00 125.80 ?  381 GLU A CD    1 
ATOM   1635 O OE1   . GLU A 1 400 ? 6.486   33.336  73.177  1.00 126.05 ?  381 GLU A OE1   1 
ATOM   1636 O OE2   . GLU A 1 400 ? 8.355   34.503  73.028  1.00 125.01 ?  381 GLU A OE2   1 
ATOM   1637 N N     . PHE A 1 401 ? 3.689   37.892  74.144  1.00 117.90 ?  382 PHE A N     1 
ATOM   1638 C CA    . PHE A 1 401 ? 3.809   39.156  74.864  1.00 117.96 ?  382 PHE A CA    1 
ATOM   1639 C C     . PHE A 1 401 ? 3.897   38.928  76.377  1.00 116.88 ?  382 PHE A C     1 
ATOM   1640 O O     . PHE A 1 401 ? 4.931   39.207  76.997  1.00 115.37 ?  382 PHE A O     1 
ATOM   1641 C CB    . PHE A 1 401 ? 2.641   40.063  74.426  1.00 118.27 ?  382 PHE A CB    1 
ATOM   1642 C CG    . PHE A 1 401 ? 2.305   41.196  75.353  1.00 111.90 ?  382 PHE A CG    1 
ATOM   1643 C CD1   . PHE A 1 401 ? 3.156   42.269  75.507  1.00 108.90 ?  382 PHE A CD1   1 
ATOM   1644 C CD2   . PHE A 1 401 ? 1.039   41.272  75.914  1.00 114.15 ?  382 PHE A CD2   1 
ATOM   1645 C CE1   . PHE A 1 401 ? 2.807   43.318  76.316  1.00 107.59 ?  382 PHE A CE1   1 
ATOM   1646 C CE2   . PHE A 1 401 ? 0.675   42.334  76.705  1.00 112.22 ?  382 PHE A CE2   1 
ATOM   1647 C CZ    . PHE A 1 401 ? 1.558   43.347  76.906  1.00 110.67 ?  382 PHE A CZ    1 
ATOM   1648 N N     . ASN A 1 402 ? 2.852   38.344  76.973  1.00 116.41 ?  383 ASN A N     1 
ATOM   1649 C CA    . ASN A 1 402 ? 2.820   38.156  78.422  1.00 111.54 ?  383 ASN A CA    1 
ATOM   1650 C C     . ASN A 1 402 ? 4.013   37.350  78.898  1.00 112.94 ?  383 ASN A C     1 
ATOM   1651 O O     . ASN A 1 402 ? 4.571   37.615  79.967  1.00 117.45 ?  383 ASN A O     1 
ATOM   1652 C CB    . ASN A 1 402 ? 1.535   37.451  78.820  1.00 112.17 ?  383 ASN A CB    1 
ATOM   1653 C CG    . ASN A 1 402 ? 0.309   38.143  78.277  1.00 113.22 ?  383 ASN A CG    1 
ATOM   1654 O OD1   . ASN A 1 402 ? -0.338  38.916  78.969  1.00 119.18 ?  383 ASN A OD1   1 
ATOM   1655 N ND2   . ASN A 1 402 ? -0.035  37.846  77.037  1.00 115.86 ?  383 ASN A ND2   1 
ATOM   1656 N N     . ARG A 1 403 ? 4.400   36.348  78.117  1.00 115.10 ?  384 ARG A N     1 
ATOM   1657 C CA    . ARG A 1 403 ? 5.582   35.553  78.426  1.00 120.83 ?  384 ARG A CA    1 
ATOM   1658 C C     . ARG A 1 403 ? 6.828   36.428  78.482  1.00 116.29 ?  384 ARG A C     1 
ATOM   1659 O O     . ARG A 1 403 ? 7.709   36.224  79.328  1.00 113.19 ?  384 ARG A O     1 
ATOM   1660 C CB    . ARG A 1 403 ? 5.727   34.450  77.372  1.00 126.28 ?  384 ARG A CB    1 
ATOM   1661 C CG    . ARG A 1 403 ? 4.823   33.223  77.582  1.00 129.72 ?  384 ARG A CG    1 
ATOM   1662 C CD    . ARG A 1 403 ? 4.854   32.265  76.385  1.00 131.87 ?  384 ARG A CD    1 
ATOM   1663 N NE    . ARG A 1 403 ? 6.223   32.033  75.930  1.00 138.43 ?  384 ARG A NE    1 
ATOM   1664 C CZ    . ARG A 1 403 ? 7.008   31.051  76.365  1.00 139.88 ?  384 ARG A CZ    1 
ATOM   1665 N NH1   . ARG A 1 403 ? 6.576   30.212  77.307  1.00 137.32 ?  384 ARG A NH1   1 
ATOM   1666 N NH2   . ARG A 1 403 ? 8.245   30.936  75.884  1.00 136.29 ?  384 ARG A NH2   1 
ATOM   1667 N N     . LEU A 1 404 ? 6.913   37.408  77.582  1.00 114.21 ?  385 LEU A N     1 
ATOM   1668 C CA    . LEU A 1 404 ? 8.011   38.364  77.612  1.00 114.19 ?  385 LEU A CA    1 
ATOM   1669 C C     . LEU A 1 404 ? 7.944   39.240  78.856  1.00 119.05 ?  385 LEU A C     1 
ATOM   1670 O O     . LEU A 1 404 ? 8.981   39.596  79.430  1.00 122.01 ?  385 LEU A O     1 
ATOM   1671 C CB    . LEU A 1 404 ? 7.978   39.220  76.351  1.00 109.80 ?  385 LEU A CB    1 
ATOM   1672 C CG    . LEU A 1 404 ? 8.329   38.624  74.995  1.00 108.79 ?  385 LEU A CG    1 
ATOM   1673 C CD1   . LEU A 1 404 ? 7.838   39.530  73.886  1.00 102.09 ?  385 LEU A CD1   1 
ATOM   1674 C CD2   . LEU A 1 404 ? 9.825   38.510  74.903  1.00 106.52 ?  385 LEU A CD2   1 
ATOM   1675 N N     . LEU A 1 405 ? 6.735   39.617  79.278  1.00 117.82 ?  386 LEU A N     1 
ATOM   1676 C CA    . LEU A 1 405 ? 6.597   40.370  80.518  1.00 114.86 ?  386 LEU A CA    1 
ATOM   1677 C C     . LEU A 1 405 ? 7.192   39.585  81.680  1.00 116.36 ?  386 LEU A C     1 
ATOM   1678 O O     . LEU A 1 405 ? 8.130   40.044  82.339  1.00 116.39 ?  386 LEU A O     1 
ATOM   1679 C CB    . LEU A 1 405 ? 5.124   40.700  80.765  1.00 115.31 ?  386 LEU A CB    1 
ATOM   1680 C CG    . LEU A 1 405 ? 4.660   41.990  80.088  1.00 113.15 ?  386 LEU A CG    1 
ATOM   1681 C CD1   . LEU A 1 405 ? 3.189   42.280  80.350  1.00 109.94 ?  386 LEU A CD1   1 
ATOM   1682 C CD2   . LEU A 1 405 ? 5.542   43.148  80.524  1.00 108.80 ?  386 LEU A CD2   1 
ATOM   1683 N N     . GLU A 1 406 ? 6.687   38.368  81.911  1.00 117.16 ?  387 GLU A N     1 
ATOM   1684 C CA    . GLU A 1 406 ? 7.228   37.526  82.973  1.00 118.85 ?  387 GLU A CA    1 
ATOM   1685 C C     . GLU A 1 406 ? 8.728   37.342  82.851  1.00 117.56 ?  387 GLU A C     1 
ATOM   1686 O O     . GLU A 1 406 ? 9.405   37.132  83.861  1.00 122.04 ?  387 GLU A O     1 
ATOM   1687 C CB    . GLU A 1 406 ? 6.551   36.159  82.982  1.00 124.90 ?  387 GLU A CB    1 
ATOM   1688 C CG    . GLU A 1 406 ? 5.073   36.234  83.221  1.00 131.79 ?  387 GLU A CG    1 
ATOM   1689 C CD    . GLU A 1 406 ? 4.386   34.887  83.299  1.00 143.07 ?  387 GLU A CD    1 
ATOM   1690 O OE1   . GLU A 1 406 ? 5.077   33.846  83.173  1.00 143.92 ?  387 GLU A OE1   1 
ATOM   1691 O OE2   . GLU A 1 406 ? 3.145   34.881  83.496  1.00 143.76 ?  387 GLU A OE2   1 
ATOM   1692 N N     . ALA A 1 407 ? 9.272   37.393  81.637  1.00 117.37 ?  388 ALA A N     1 
ATOM   1693 C CA    . ALA A 1 407 ? 10.719  37.290  81.510  1.00 119.51 ?  388 ALA A CA    1 
ATOM   1694 C C     . ALA A 1 407 ? 11.399  38.481  82.181  1.00 119.84 ?  388 ALA A C     1 
ATOM   1695 O O     . ALA A 1 407 ? 12.274  38.310  83.037  1.00 122.18 ?  388 ALA A O     1 
ATOM   1696 C CB    . ALA A 1 407 ? 11.115  37.165  80.036  1.00 117.74 ?  388 ALA A CB    1 
ATOM   1697 N N     . THR A 1 408 ? 10.976  39.700  81.834  1.00 118.03 ?  389 THR A N     1 
ATOM   1698 C CA    . THR A 1 408 ? 11.519  40.893  82.479  1.00 117.74 ?  389 THR A CA    1 
ATOM   1699 C C     . THR A 1 408 ? 11.356  40.824  83.988  1.00 119.89 ?  389 THR A C     1 
ATOM   1700 O O     . THR A 1 408 ? 12.291  41.111  84.744  1.00 120.36 ?  389 THR A O     1 
ATOM   1701 C CB    . THR A 1 408 ? 10.829  42.142  81.927  1.00 116.25 ?  389 THR A CB    1 
ATOM   1702 O OG1   . THR A 1 408 ? 9.407   42.044  82.117  1.00 113.88 ?  389 THR A OG1   1 
ATOM   1703 C CG2   . THR A 1 408 ? 11.133  42.294  80.454  1.00 114.94 ?  389 THR A CG2   1 
ATOM   1704 N N     . SER A 1 409 ? 10.157  40.443  84.437  1.00 119.12 ?  390 SER A N     1 
ATOM   1705 C CA    . SER A 1 409 ? 9.884   40.311  85.861  1.00 117.11 ?  390 SER A CA    1 
ATOM   1706 C C     . SER A 1 409 ? 10.906  39.392  86.520  1.00 119.63 ?  390 SER A C     1 
ATOM   1707 O O     . SER A 1 409 ? 11.397  39.672  87.619  1.00 122.84 ?  390 SER A O     1 
ATOM   1708 C CB    . SER A 1 409 ? 8.452   39.796  86.046  1.00 115.04 ?  390 SER A CB    1 
ATOM   1709 O OG    . SER A 1 409 ? 8.078   39.703  87.408  1.00 121.37 ?  390 SER A OG    1 
ATOM   1710 N N     . TYR A 1 410 ? 11.256  38.303  85.837  1.00 122.48 ?  391 TYR A N     1 
ATOM   1711 C CA    . TYR A 1 410 ? 12.328  37.423  86.289  1.00 125.06 ?  391 TYR A CA    1 
ATOM   1712 C C     . TYR A 1 410 ? 13.668  38.164  86.344  1.00 126.37 ?  391 TYR A C     1 
ATOM   1713 O O     . TYR A 1 410 ? 14.360  38.132  87.365  1.00 129.66 ?  391 TYR A O     1 
ATOM   1714 C CB    . TYR A 1 410 ? 12.384  36.207  85.358  1.00 125.73 ?  391 TYR A CB    1 
ATOM   1715 C CG    . TYR A 1 410 ? 13.478  35.198  85.612  1.00 130.96 ?  391 TYR A CG    1 
ATOM   1716 C CD1   . TYR A 1 410 ? 14.745  35.385  85.064  1.00 136.18 ?  391 TYR A CD1   1 
ATOM   1717 C CD2   . TYR A 1 410 ? 13.234  34.019  86.295  1.00 132.96 ?  391 TYR A CD2   1 
ATOM   1718 C CE1   . TYR A 1 410 ? 15.763  34.471  85.256  1.00 134.31 ?  391 TYR A CE1   1 
ATOM   1719 C CE2   . TYR A 1 410 ? 14.252  33.087  86.486  1.00 136.77 ?  391 TYR A CE2   1 
ATOM   1720 C CZ    . TYR A 1 410 ? 15.513  33.325  85.958  1.00 134.53 ?  391 TYR A CZ    1 
ATOM   1721 O OH    . TYR A 1 410 ? 16.540  32.428  86.120  1.00 134.17 ?  391 TYR A OH    1 
ATOM   1722 N N     . LEU A 1 411 ? 14.054  38.838  85.254  1.00 123.38 ?  392 LEU A N     1 
ATOM   1723 C CA    . LEU A 1 411 ? 15.283  39.635  85.269  1.00 124.47 ?  392 LEU A CA    1 
ATOM   1724 C C     . LEU A 1 411 ? 15.331  40.603  86.437  1.00 126.30 ?  392 LEU A C     1 
ATOM   1725 O O     . LEU A 1 411 ? 16.406  40.866  86.992  1.00 127.49 ?  392 LEU A O     1 
ATOM   1726 C CB    . LEU A 1 411 ? 15.420  40.426  83.972  1.00 125.43 ?  392 LEU A CB    1 
ATOM   1727 C CG    . LEU A 1 411 ? 16.035  39.786  82.741  1.00 124.02 ?  392 LEU A CG    1 
ATOM   1728 C CD1   . LEU A 1 411 ? 15.152  38.705  82.196  1.00 124.65 ?  392 LEU A CD1   1 
ATOM   1729 C CD2   . LEU A 1 411 ? 16.206  40.895  81.705  1.00 121.29 ?  392 LEU A CD2   1 
ATOM   1730 N N     . SER A 1 412 ? 14.178  41.140  86.817  1.00 125.45 ?  393 SER A N     1 
ATOM   1731 C CA    . SER A 1 412 ? 14.117  42.212  87.796  1.00 124.56 ?  393 SER A CA    1 
ATOM   1732 C C     . SER A 1 412 ? 14.319  41.685  89.219  1.00 130.85 ?  393 SER A C     1 
ATOM   1733 O O     . SER A 1 412 ? 15.076  42.274  90.009  1.00 130.10 ?  393 SER A O     1 
ATOM   1734 C CB    . SER A 1 412 ? 12.770  42.928  87.634  1.00 120.11 ?  393 SER A CB    1 
ATOM   1735 O OG    . SER A 1 412 ? 12.640  44.058  88.470  1.00 123.82 ?  393 SER A OG    1 
ATOM   1736 N N     . HIS A 1 413 ? 13.677  40.558  89.552  1.00 133.42 ?  394 HIS A N     1 
ATOM   1737 C CA    . HIS A 1 413 ? 13.664  40.051  90.916  1.00 130.64 ?  394 HIS A CA    1 
ATOM   1738 C C     . HIS A 1 413 ? 14.539  38.825  91.113  1.00 132.37 ?  394 HIS A C     1 
ATOM   1739 O O     . HIS A 1 413 ? 14.835  38.477  92.258  1.00 136.94 ?  394 HIS A O     1 
ATOM   1740 C CB    . HIS A 1 413 ? 12.225  39.722  91.347  1.00 125.05 ?  394 HIS A CB    1 
ATOM   1741 C CG    . HIS A 1 413 ? 11.291  40.886  91.217  1.00 128.67 ?  394 HIS A CG    1 
ATOM   1742 N ND1   . HIS A 1 413 ? 10.878  41.373  89.994  1.00 131.72 ?  394 HIS A ND1   1 
ATOM   1743 C CD2   . HIS A 1 413 ? 10.779  41.729  92.145  1.00 132.18 ?  394 HIS A CD2   1 
ATOM   1744 C CE1   . HIS A 1 413 ? 10.098  42.425  90.177  1.00 129.54 ?  394 HIS A CE1   1 
ATOM   1745 N NE2   . HIS A 1 413 ? 10.030  42.668  91.473  1.00 131.23 ?  394 HIS A NE2   1 
ATOM   1746 N N     . GLN A 1 414 ? 14.973  38.180  90.032  1.00 134.19 ?  395 GLN A N     1 
ATOM   1747 C CA    . GLN A 1 414 ? 15.789  36.975  90.105  1.00 137.49 ?  395 GLN A CA    1 
ATOM   1748 C C     . GLN A 1 414 ? 17.259  37.247  89.797  1.00 139.62 ?  395 GLN A C     1 
ATOM   1749 O O     . GLN A 1 414 ? 18.136  36.755  90.512  1.00 144.27 ?  395 GLN A O     1 
ATOM   1750 C CB    . GLN A 1 414 ? 15.249  35.916  89.135  1.00 139.83 ?  395 GLN A CB    1 
ATOM   1751 C CG    . GLN A 1 414 ? 13.831  35.440  89.439  1.00 139.96 ?  395 GLN A CG    1 
ATOM   1752 C CD    . GLN A 1 414 ? 13.718  34.678  90.734  1.00 142.29 ?  395 GLN A CD    1 
ATOM   1753 O OE1   . GLN A 1 414 ? 14.351  33.633  90.917  1.00 146.15 ?  395 GLN A OE1   1 
ATOM   1754 N NE2   . GLN A 1 414 ? 12.906  35.195  91.647  1.00 142.31 ?  395 GLN A NE2   1 
ATOM   1755 N N     . LEU A 1 415 ? 17.551  38.015  88.743  1.00 135.58 ?  396 LEU A N     1 
ATOM   1756 C CA    . LEU A 1 415 ? 18.922  38.319  88.346  1.00 134.12 ?  396 LEU A CA    1 
ATOM   1757 C C     . LEU A 1 415 ? 19.381  39.710  88.782  1.00 137.93 ?  396 LEU A C     1 
ATOM   1758 O O     . LEU A 1 415 ? 20.464  40.148  88.362  1.00 133.67 ?  396 LEU A O     1 
ATOM   1759 C CB    . LEU A 1 415 ? 19.071  38.173  86.832  1.00 137.46 ?  396 LEU A CB    1 
ATOM   1760 C CG    . LEU A 1 415 ? 18.664  36.834  86.217  1.00 141.88 ?  396 LEU A CG    1 
ATOM   1761 C CD1   . LEU A 1 415 ? 18.837  36.854  84.695  1.00 142.05 ?  396 LEU A CD1   1 
ATOM   1762 C CD2   . LEU A 1 415 ? 19.490  35.721  86.837  1.00 143.63 ?  396 LEU A CD2   1 
ATOM   1763 N N     . ASP A 1 416 ? 18.594  40.391  89.635  1.00 138.10 ?  397 ASP A N     1 
ATOM   1764 C CA    . ASP A 1 416 ? 18.804  41.774  90.073  1.00 137.36 ?  397 ASP A CA    1 
ATOM   1765 C C     . ASP A 1 416 ? 19.326  42.656  88.936  1.00 139.35 ?  397 ASP A C     1 
ATOM   1766 O O     . ASP A 1 416 ? 20.287  43.418  89.112  1.00 139.75 ?  397 ASP A O     1 
ATOM   1767 C CB    . ASP A 1 416 ? 19.755  41.839  91.277  1.00 134.45 ?  397 ASP A CB    1 
ATOM   1768 C CG    . ASP A 1 416 ? 19.447  43.022  92.210  1.00 142.78 ?  397 ASP A CG    1 
ATOM   1769 O OD1   . ASP A 1 416 ? 18.873  44.037  91.749  1.00 140.64 ?  397 ASP A OD1   1 
ATOM   1770 O OD2   . ASP A 1 416 ? 19.796  42.951  93.410  1.00 148.05 ?  397 ASP A OD2   1 
ATOM   1771 N N     . PHE A 1 417 ? 18.691  42.549  87.768  1.00 133.75 ?  398 PHE A N     1 
ATOM   1772 C CA    . PHE A 1 417 ? 19.008  43.355  86.589  1.00 131.03 ?  398 PHE A CA    1 
ATOM   1773 C C     . PHE A 1 417 ? 18.277  44.695  86.713  1.00 133.21 ?  398 PHE A C     1 
ATOM   1774 O O     . PHE A 1 417 ? 17.173  44.876  86.190  1.00 133.84 ?  398 PHE A O     1 
ATOM   1775 C CB    . PHE A 1 417 ? 18.624  42.579  85.324  1.00 130.82 ?  398 PHE A CB    1 
ATOM   1776 C CG    . PHE A 1 417 ? 19.065  43.219  84.009  1.00 131.76 ?  398 PHE A CG    1 
ATOM   1777 C CD1   . PHE A 1 417 ? 20.414  43.443  83.728  1.00 132.63 ?  398 PHE A CD1   1 
ATOM   1778 C CD2   . PHE A 1 417 ? 18.127  43.497  83.011  1.00 128.56 ?  398 PHE A CD2   1 
ATOM   1779 C CE1   . PHE A 1 417 ? 20.812  44.009  82.510  1.00 131.66 ?  398 PHE A CE1   1 
ATOM   1780 C CE2   . PHE A 1 417 ? 18.515  44.049  81.791  1.00 125.09 ?  398 PHE A CE2   1 
ATOM   1781 C CZ    . PHE A 1 417 ? 19.863  44.306  81.543  1.00 128.43 ?  398 PHE A CZ    1 
ATOM   1782 N N     . ASN A 1 418 ? 18.897  45.657  87.435  1.00 128.79 ?  399 ASN A N     1 
ATOM   1783 C CA    . ASN A 1 418 ? 18.341  47.007  87.511  1.00 124.24 ?  399 ASN A CA    1 
ATOM   1784 C C     . ASN A 1 418 ? 19.377  48.125  87.404  1.00 125.62 ?  399 ASN A C     1 
ATOM   1785 O O     . ASN A 1 418 ? 19.026  49.291  87.623  1.00 120.90 ?  399 ASN A O     1 
ATOM   1786 C CB    . ASN A 1 418 ? 17.533  47.183  88.793  1.00 124.82 ?  399 ASN A CB    1 
ATOM   1787 C CG    . ASN A 1 418 ? 16.397  46.185  88.919  1.00 122.06 ?  399 ASN A CG    1 
ATOM   1788 O OD1   . ASN A 1 418 ? 15.320  46.389  88.346  1.00 118.41 ?  399 ASN A OD1   1 
ATOM   1789 N ND2   . ASN A 1 418 ? 16.621  45.111  89.676  1.00 123.29 ?  399 ASN A ND2   1 
ATOM   1790 N N     . VAL A 1 419 ? 20.627  47.819  87.055  1.00 133.33 ?  400 VAL A N     1 
ATOM   1791 C CA    . VAL A 1 419 ? 21.664  48.812  86.783  1.00 136.97 ?  400 VAL A CA    1 
ATOM   1792 C C     . VAL A 1 419 ? 22.372  48.412  85.488  1.00 144.28 ?  400 VAL A C     1 
ATOM   1793 O O     . VAL A 1 419 ? 22.487  47.221  85.178  1.00 150.62 ?  400 VAL A O     1 
ATOM   1794 C CB    . VAL A 1 419 ? 22.668  48.896  87.962  1.00 127.77 ?  400 VAL A CB    1 
ATOM   1795 C CG1   . VAL A 1 419 ? 23.891  49.777  87.629  1.00 129.43 ?  400 VAL A CG1   1 
ATOM   1796 C CG2   . VAL A 1 419 ? 21.968  49.347  89.208  1.00 123.42 ?  400 VAL A CG2   1 
ATOM   1797 N N     . LEU A 1 420 ? 22.847  49.403  84.721  1.00 141.63 ?  401 LEU A N     1 
ATOM   1798 C CA    . LEU A 1 420 ? 23.676  49.100  83.553  1.00 145.14 ?  401 LEU A CA    1 
ATOM   1799 C C     . LEU A 1 420 ? 24.363  50.329  82.974  1.00 150.71 ?  401 LEU A C     1 
ATOM   1800 O O     . LEU A 1 420 ? 23.695  51.234  82.458  1.00 150.17 ?  401 LEU A O     1 
ATOM   1801 C CB    . LEU A 1 420 ? 22.852  48.425  82.460  1.00 146.78 ?  401 LEU A CB    1 
ATOM   1802 C CG    . LEU A 1 420 ? 23.681  48.185  81.208  1.00 150.33 ?  401 LEU A CG    1 
ATOM   1803 C CD1   . LEU A 1 420 ? 24.873  47.286  81.501  1.00 152.02 ?  401 LEU A CD1   1 
ATOM   1804 C CD2   . LEU A 1 420 ? 22.777  47.539  80.201  1.00 151.80 ?  401 LEU A CD2   1 
ATOM   1805 N N     . ASN A 1 421 ? 25.701  50.330  82.997  1.00 154.26 ?  402 ASN A N     1 
ATOM   1806 C CA    . ASN A 1 421 ? 26.489  51.555  82.820  1.00 157.10 ?  402 ASN A CA    1 
ATOM   1807 C C     . ASN A 1 421 ? 25.972  52.653  83.755  1.00 155.28 ?  402 ASN A C     1 
ATOM   1808 O O     . ASN A 1 421 ? 25.897  53.831  83.391  1.00 159.22 ?  402 ASN A O     1 
ATOM   1809 C CB    . ASN A 1 421 ? 26.525  52.034  81.350  1.00 161.06 ?  402 ASN A CB    1 
ATOM   1810 C CG    . ASN A 1 421 ? 26.800  50.895  80.334  1.00 166.03 ?  402 ASN A CG    1 
ATOM   1811 O OD1   . ASN A 1 421 ? 26.014  50.668  79.407  1.00 160.27 ?  402 ASN A OD1   1 
ATOM   1812 N ND2   . ASN A 1 421 ? 27.921  50.190  80.508  1.00 168.10 ?  402 ASN A ND2   1 
ATOM   1813 N N     . ASN A 1 422 ? 25.576  52.241  84.968  1.00 151.70 ?  403 ASN A N     1 
ATOM   1814 C CA    . ASN A 1 422 ? 25.222  53.021  86.155  1.00 147.84 ?  403 ASN A CA    1 
ATOM   1815 C C     . ASN A 1 422 ? 23.804  53.633  86.145  1.00 141.91 ?  403 ASN A C     1 
ATOM   1816 O O     . ASN A 1 422 ? 23.376  54.129  87.184  1.00 145.35 ?  403 ASN A O     1 
ATOM   1817 C CB    . ASN A 1 422 ? 26.242  54.138  86.468  1.00 150.26 ?  403 ASN A CB    1 
ATOM   1818 C CG    . ASN A 1 422 ? 27.560  53.597  87.033  1.00 156.54 ?  403 ASN A CG    1 
ATOM   1819 O OD1   . ASN A 1 422 ? 27.569  52.706  87.897  1.00 153.38 ?  403 ASN A OD1   1 
ATOM   1820 N ND2   . ASN A 1 422 ? 28.679  54.133  86.540  1.00 151.48 ?  403 ASN A ND2   1 
ATOM   1821 N N     . LYS A 1 423 ? 23.059  53.600  85.045  1.00 138.34 ?  404 LYS A N     1 
ATOM   1822 C CA    . LYS A 1 423 ? 21.702  54.145  85.024  1.00 129.63 ?  404 LYS A CA    1 
ATOM   1823 C C     . LYS A 1 423 ? 20.699  53.117  85.569  1.00 125.16 ?  404 LYS A C     1 
ATOM   1824 O O     . LYS A 1 423 ? 21.055  51.966  85.848  1.00 127.86 ?  404 LYS A O     1 
ATOM   1825 C CB    . LYS A 1 423 ? 21.359  54.590  83.596  1.00 134.83 ?  404 LYS A CB    1 
ATOM   1826 C CG    . LYS A 1 423 ? 22.170  55.806  83.123  1.00 137.99 ?  404 LYS A CG    1 
ATOM   1827 C CD    . LYS A 1 423 ? 21.649  56.478  81.841  1.00 141.08 ?  404 LYS A CD    1 
ATOM   1828 C CE    . LYS A 1 423 ? 21.944  55.707  80.564  1.00 147.18 ?  404 LYS A CE    1 
ATOM   1829 N NZ    . LYS A 1 423 ? 21.507  56.506  79.360  1.00 145.67 ?  404 LYS A NZ    1 
ATOM   1830 N N     . PRO A 1 424 ? 19.435  53.507  85.779  1.00 119.09 ?  405 PRO A N     1 
ATOM   1831 C CA    . PRO A 1 424 ? 18.390  52.514  86.069  1.00 120.95 ?  405 PRO A CA    1 
ATOM   1832 C C     . PRO A 1 424 ? 17.891  51.839  84.801  1.00 123.47 ?  405 PRO A C     1 
ATOM   1833 O O     . PRO A 1 424 ? 17.939  52.397  83.702  1.00 126.46 ?  405 PRO A O     1 
ATOM   1834 C CB    . PRO A 1 424 ? 17.260  53.342  86.699  1.00 113.77 ?  405 PRO A CB    1 
ATOM   1835 C CG    . PRO A 1 424 ? 17.428  54.680  86.142  1.00 110.70 ?  405 PRO A CG    1 
ATOM   1836 C CD    . PRO A 1 424 ? 18.935  54.872  86.014  1.00 120.75 ?  405 PRO A CD    1 
ATOM   1837 N N     . VAL A 1 425 ? 17.310  50.663  84.977  1.00 121.60 ?  406 VAL A N     1 
ATOM   1838 C CA    . VAL A 1 425 ? 16.828  49.889  83.809  1.00 116.81 ?  406 VAL A CA    1 
ATOM   1839 C C     . VAL A 1 425 ? 15.355  50.173  83.581  1.00 112.32 ?  406 VAL A C     1 
ATOM   1840 O O     . VAL A 1 425 ? 14.577  50.026  84.514  1.00 109.18 ?  406 VAL A O     1 
ATOM   1841 C CB    . VAL A 1 425 ? 17.058  48.402  84.066  1.00 119.66 ?  406 VAL A CB    1 
ATOM   1842 C CG1   . VAL A 1 425 ? 16.900  47.619  82.787  1.00 115.44 ?  406 VAL A CG1   1 
ATOM   1843 C CG2   . VAL A 1 425 ? 18.421  48.174  84.693  1.00 121.17 ?  406 VAL A CG2   1 
ATOM   1844 N N     . SER A 1 426 ? 15.032  50.598  82.369  1.00 104.93 ?  407 SER A N     1 
ATOM   1845 C CA    . SER A 1 426 ? 13.641  50.899  81.976  1.00 102.80 ?  407 SER A CA    1 
ATOM   1846 C C     . SER A 1 426 ? 12.953  49.596  81.630  1.00 98.30  ?  407 SER A C     1 
ATOM   1847 O O     . SER A 1 426 ? 13.625  48.642  81.311  1.00 96.81  ?  407 SER A O     1 
ATOM   1848 C CB    . SER A 1 426 ? 13.619  51.797  80.791  1.00 105.05 ?  407 SER A CB    1 
ATOM   1849 O OG    . SER A 1 426 ? 14.637  51.429  79.886  1.00 97.85  ?  407 SER A OG    1 
ATOM   1850 N N     . LEU A 1 427 ? 11.636  49.595  81.621  1.00 95.71  ?  408 LEU A N     1 
ATOM   1851 C CA    . LEU A 1 427 ? 10.940  48.355  81.240  1.00 95.73  ?  408 LEU A CA    1 
ATOM   1852 C C     . LEU A 1 427 ? 11.280  48.041  79.793  1.00 104.59 ?  408 LEU A C     1 
ATOM   1853 O O     . LEU A 1 427 ? 11.604  46.901  79.497  1.00 108.70 ?  408 LEU A O     1 
ATOM   1854 C CB    . LEU A 1 427 ? 9.445   48.597  81.331  1.00 90.81  ?  408 LEU A CB    1 
ATOM   1855 C CG    . LEU A 1 427 ? 8.674   47.445  80.733  1.00 88.99  ?  408 LEU A CG    1 
ATOM   1856 C CD1   . LEU A 1 427 ? 9.460   46.187  80.981  1.00 97.69  ?  408 LEU A CD1   1 
ATOM   1857 C CD2   . LEU A 1 427 ? 7.313   47.332  81.363  1.00 88.80  ?  408 LEU A CD2   1 
ATOM   1858 N N     . GLY A 1 428 ? 11.287  49.053  78.933  1.00 100.93 ?  409 GLY A N     1 
ATOM   1859 C CA    . GLY A 1 428 ? 11.594  48.811  77.518  1.00 94.26  ?  409 GLY A CA    1 
ATOM   1860 C C     . GLY A 1 428 ? 12.964  48.202  77.371  1.00 96.67  ?  409 GLY A C     1 
ATOM   1861 O O     . GLY A 1 428 ? 13.055  47.183  76.727  1.00 103.53 ?  409 GLY A O     1 
ATOM   1862 N N     . GLN A 1 429 ? 13.958  48.689  78.104  1.00 96.14  ?  410 GLN A N     1 
ATOM   1863 C CA    . GLN A 1 429 ? 15.317  48.115  77.998  1.00 98.77  ?  410 GLN A CA    1 
ATOM   1864 C C     . GLN A 1 429 ? 15.269  46.646  78.391  1.00 106.94 ?  410 GLN A C     1 
ATOM   1865 O O     . GLN A 1 429 ? 15.869  45.841  77.707  1.00 111.55 ?  410 GLN A O     1 
ATOM   1866 C CB    . GLN A 1 429 ? 16.253  48.803  78.980  1.00 103.73 ?  410 GLN A CB    1 
ATOM   1867 C CG    . GLN A 1 429 ? 17.044  49.933  78.359  1.00 108.88 ?  410 GLN A CG    1 
ATOM   1868 C CD    . GLN A 1 429 ? 17.751  50.771  79.389  1.00 115.58 ?  410 GLN A CD    1 
ATOM   1869 O OE1   . GLN A 1 429 ? 18.822  50.420  79.865  1.00 117.71 ?  410 GLN A OE1   1 
ATOM   1870 N NE2   . GLN A 1 429 ? 17.157  51.902  79.726  1.00 105.78 ?  410 GLN A NE2   1 
ATOM   1871 N N     . ALA A 1 430 ? 14.530  46.302  79.435  1.00 108.84 ?  411 ALA A N     1 
ATOM   1872 C CA    . ALA A 1 430 ? 14.453  44.881  79.808  1.00 107.22 ?  411 ALA A CA    1 
ATOM   1873 C C     . ALA A 1 430 ? 13.831  44.109  78.661  1.00 104.76 ?  411 ALA A C     1 
ATOM   1874 O O     . ALA A 1 430 ? 14.375  43.081  78.310  1.00 110.52 ?  411 ALA A O     1 
ATOM   1875 C CB    . ALA A 1 430 ? 13.576  44.745  81.009  1.00 111.30 ?  411 ALA A CB    1 
ATOM   1876 N N     . LEU A 1 431 ? 12.758  44.632  78.090  1.00 99.42  ?  412 LEU A N     1 
ATOM   1877 C CA    . LEU A 1 431 ? 12.088  43.905  76.997  1.00 99.71  ?  412 LEU A CA    1 
ATOM   1878 C C     . LEU A 1 431 ? 13.071  43.633  75.875  1.00 106.61 ?  412 LEU A C     1 
ATOM   1879 O O     . LEU A 1 431 ? 13.222  42.474  75.514  1.00 113.57 ?  412 LEU A O     1 
ATOM   1880 C CB    . LEU A 1 431 ? 10.938  44.760  76.493  1.00 90.84  ?  412 LEU A CB    1 
ATOM   1881 C CG    . LEU A 1 431 ? 9.703   44.654  77.363  1.00 91.26  ?  412 LEU A CG    1 
ATOM   1882 C CD1   . LEU A 1 431 ? 8.469   44.569  76.504  1.00 90.85  ?  412 LEU A CD1   1 
ATOM   1883 C CD2   . LEU A 1 431 ? 9.812   43.426  78.229  1.00 100.12 ?  412 LEU A CD2   1 
ATOM   1884 N N     . GLU A 1 432 ? 13.769  44.651  75.401  1.00 105.02 ?  413 GLU A N     1 
ATOM   1885 C CA    . GLU A 1 432 ? 14.640  44.323  74.282  1.00 111.42 ?  413 GLU A CA    1 
ATOM   1886 C C     . GLU A 1 432 ? 15.762  43.367  74.669  1.00 114.48 ?  413 GLU A C     1 
ATOM   1887 O O     . GLU A 1 432 ? 16.180  42.561  73.829  1.00 120.68 ?  413 GLU A O     1 
ATOM   1888 C CB    . GLU A 1 432 ? 15.203  45.541  73.560  1.00 116.22 ?  413 GLU A CB    1 
ATOM   1889 C CG    . GLU A 1 432 ? 14.194  46.204  72.645  1.00 118.88 ?  413 GLU A CG    1 
ATOM   1890 C CD    . GLU A 1 432 ? 14.847  47.287  71.828  1.00 138.83 ?  413 GLU A CD    1 
ATOM   1891 O OE1   . GLU A 1 432 ? 16.027  47.599  72.109  1.00 143.11 ?  413 GLU A OE1   1 
ATOM   1892 O OE2   . GLU A 1 432 ? 14.219  47.761  70.856  1.00 148.24 ?  413 GLU A OE2   1 
ATOM   1893 N N     . VAL A 1 433 ? 16.233  43.372  75.916  1.00 108.78 ?  414 VAL A N     1 
ATOM   1894 C CA    . VAL A 1 433 ? 17.216  42.337  76.231  1.00 114.98 ?  414 VAL A CA    1 
ATOM   1895 C C     . VAL A 1 433 ? 16.553  40.954  76.316  1.00 115.84 ?  414 VAL A C     1 
ATOM   1896 O O     . VAL A 1 433 ? 17.182  39.939  75.998  1.00 118.06 ?  414 VAL A O     1 
ATOM   1897 C CB    . VAL A 1 433 ? 18.009  42.703  77.498  1.00 116.49 ?  414 VAL A CB    1 
ATOM   1898 C CG1   . VAL A 1 433 ? 18.788  41.497  78.043  1.00 115.45 ?  414 VAL A CG1   1 
ATOM   1899 C CG2   . VAL A 1 433 ? 18.975  43.809  77.156  1.00 116.17 ?  414 VAL A CG2   1 
ATOM   1900 N N     . VAL A 1 434 ? 15.272  40.882  76.687  1.00 115.34 ?  415 VAL A N     1 
ATOM   1901 C CA    . VAL A 1 434 ? 14.569  39.601  76.624  1.00 111.77 ?  415 VAL A CA    1 
ATOM   1902 C C     . VAL A 1 434 ? 14.372  39.173  75.179  1.00 111.57 ?  415 VAL A C     1 
ATOM   1903 O O     . VAL A 1 434 ? 14.634  38.019  74.827  1.00 119.42 ?  415 VAL A O     1 
ATOM   1904 C CB    . VAL A 1 434 ? 13.226  39.661  77.369  1.00 109.59 ?  415 VAL A CB    1 
ATOM   1905 C CG1   . VAL A 1 434 ? 12.419  38.419  77.069  1.00 107.37 ?  415 VAL A CG1   1 
ATOM   1906 C CG2   . VAL A 1 434 ? 13.468  39.774  78.851  1.00 114.16 ?  415 VAL A CG2   1 
ATOM   1907 N N     . ILE A 1 435 ? 13.897  40.086  74.325  1.00 109.90 ?  416 ILE A N     1 
ATOM   1908 C CA    . ILE A 1 435 ? 13.739  39.765  72.903  1.00 111.72 ?  416 ILE A CA    1 
ATOM   1909 C C     . ILE A 1 435 ? 15.081  39.455  72.259  1.00 114.54 ?  416 ILE A C     1 
ATOM   1910 O O     . ILE A 1 435 ? 15.212  38.479  71.515  1.00 116.53 ?  416 ILE A O     1 
ATOM   1911 C CB    . ILE A 1 435 ? 13.004  40.885  72.151  1.00 101.90 ?  416 ILE A CB    1 
ATOM   1912 C CG1   . ILE A 1 435 ? 11.512  40.843  72.493  1.00 100.96 ?  416 ILE A CG1   1 
ATOM   1913 C CG2   . ILE A 1 435 ? 13.298  40.806  70.683  1.00 103.24 ?  416 ILE A CG2   1 
ATOM   1914 C CD1   . ILE A 1 435 ? 10.662  41.749  71.647  1.00 98.87  ?  416 ILE A CD1   1 
ATOM   1915 N N     . GLN A 1 436 ? 16.102  40.264  72.544  1.00 115.04 ?  417 GLN A N     1 
ATOM   1916 C CA    . GLN A 1 436 ? 17.418  39.979  71.981  1.00 115.70 ?  417 GLN A CA    1 
ATOM   1917 C C     . GLN A 1 436 ? 18.022  38.676  72.515  1.00 119.24 ?  417 GLN A C     1 
ATOM   1918 O O     . GLN A 1 436 ? 18.845  38.066  71.835  1.00 129.10 ?  417 GLN A O     1 
ATOM   1919 C CB    . GLN A 1 436 ? 18.363  41.152  72.213  1.00 116.42 ?  417 GLN A CB    1 
ATOM   1920 C CG    . GLN A 1 436 ? 18.150  42.250  71.197  1.00 126.55 ?  417 GLN A CG    1 
ATOM   1921 C CD    . GLN A 1 436 ? 18.752  43.585  71.618  1.00 137.85 ?  417 GLN A CD    1 
ATOM   1922 O OE1   . GLN A 1 436 ? 19.474  43.683  72.626  1.00 133.86 ?  417 GLN A OE1   1 
ATOM   1923 N NE2   . GLN A 1 436 ? 18.445  44.630  70.846  1.00 138.95 ?  417 GLN A NE2   1 
ATOM   1924 N N     . LEU A 1 437 ? 17.641  38.201  73.696  1.00 118.58 ?  418 LEU A N     1 
ATOM   1925 C CA    . LEU A 1 437 ? 18.083  36.844  74.016  1.00 120.37 ?  418 LEU A CA    1 
ATOM   1926 C C     . LEU A 1 437 ? 17.238  35.762  73.357  1.00 119.50 ?  418 LEU A C     1 
ATOM   1927 O O     . LEU A 1 437 ? 17.682  34.612  73.287  1.00 122.34 ?  418 LEU A O     1 
ATOM   1928 C CB    . LEU A 1 437 ? 18.159  36.603  75.530  1.00 121.67 ?  418 LEU A CB    1 
ATOM   1929 C CG    . LEU A 1 437 ? 19.538  36.945  76.112  1.00 126.67 ?  418 LEU A CG    1 
ATOM   1930 C CD1   . LEU A 1 437 ? 19.851  38.422  76.130  1.00 133.39 ?  418 LEU A CD1   1 
ATOM   1931 C CD2   . LEU A 1 437 ? 19.695  36.353  77.505  1.00 138.95 ?  418 LEU A CD2   1 
ATOM   1932 N N     . GLN A 1 438 ? 16.050  36.082  72.857  1.00 113.19 ?  419 GLN A N     1 
ATOM   1933 C CA    . GLN A 1 438 ? 15.316  35.041  72.157  1.00 113.44 ?  419 GLN A CA    1 
ATOM   1934 C C     . GLN A 1 438 ? 15.761  34.958  70.706  1.00 122.06 ?  419 GLN A C     1 
ATOM   1935 O O     . GLN A 1 438 ? 15.967  33.861  70.178  1.00 125.79 ?  419 GLN A O     1 
ATOM   1936 C CB    . GLN A 1 438 ? 13.818  35.279  72.257  1.00 109.32 ?  419 GLN A CB    1 
ATOM   1937 C CG    . GLN A 1 438 ? 13.280  35.297  73.669  1.00 116.61 ?  419 GLN A CG    1 
ATOM   1938 C CD    . GLN A 1 438 ? 13.793  34.158  74.535  1.00 125.86 ?  419 GLN A CD    1 
ATOM   1939 O OE1   . GLN A 1 438 ? 14.733  34.309  75.337  1.00 123.04 ?  419 GLN A OE1   1 
ATOM   1940 N NE2   . GLN A 1 438 ? 13.167  33.003  74.378  1.00 127.71 ?  419 GLN A NE2   1 
ATOM   1941 N N     . GLU A 1 439 ? 15.941  36.106  70.053  1.00 125.51 ?  420 GLU A N     1 
ATOM   1942 C CA    . GLU A 1 439 ? 16.561  36.111  68.732  1.00 119.58 ?  420 GLU A CA    1 
ATOM   1943 C C     . GLU A 1 439 ? 17.959  35.512  68.777  1.00 119.44 ?  420 GLU A C     1 
ATOM   1944 O O     . GLU A 1 439 ? 18.416  34.959  67.777  1.00 129.35 ?  420 GLU A O     1 
ATOM   1945 C CB    . GLU A 1 439 ? 16.607  37.531  68.173  1.00 116.94 ?  420 GLU A CB    1 
ATOM   1946 C CG    . GLU A 1 439 ? 15.265  37.992  67.651  1.00 121.84 ?  420 GLU A CG    1 
ATOM   1947 C CD    . GLU A 1 439 ? 15.305  39.404  67.136  1.00 129.74 ?  420 GLU A CD    1 
ATOM   1948 O OE1   . GLU A 1 439 ? 16.395  40.020  67.226  1.00 126.81 ?  420 GLU A OE1   1 
ATOM   1949 O OE2   . GLU A 1 439 ? 14.244  39.900  66.677  1.00 131.26 ?  420 GLU A OE2   1 
ATOM   1950 N N     . LYS A 1 440 ? 18.652  35.595  69.916  1.00 117.73 ?  421 LYS A N     1 
ATOM   1951 C CA    . LYS A 1 440 ? 19.912  34.872  70.039  1.00 116.11 ?  421 LYS A CA    1 
ATOM   1952 C C     . LYS A 1 440 ? 19.673  33.377  70.080  1.00 122.03 ?  421 LYS A C     1 
ATOM   1953 O O     . LYS A 1 440 ? 20.386  32.605  69.438  1.00 129.50 ?  421 LYS A O     1 
ATOM   1954 C CB    . LYS A 1 440 ? 20.674  35.275  71.290  1.00 115.85 ?  421 LYS A CB    1 
ATOM   1955 C CG    . LYS A 1 440 ? 22.025  34.576  71.376  1.00 116.99 ?  421 LYS A CG    1 
ATOM   1956 C CD    . LYS A 1 440 ? 22.327  34.095  72.785  1.00 126.31 ?  421 LYS A CD    1 
ATOM   1957 C CE    . LYS A 1 440 ? 23.668  33.381  72.858  1.00 129.40 ?  421 LYS A CE    1 
ATOM   1958 N NZ    . LYS A 1 440 ? 23.911  32.798  74.207  1.00 135.80 ?  421 LYS A NZ    1 
ATOM   1959 N N     . HIS A 1 441 ? 18.692  32.943  70.855  1.00 123.30 ?  422 HIS A N     1 
ATOM   1960 C CA    . HIS A 1 441 ? 18.476  31.510  70.968  1.00 124.88 ?  422 HIS A CA    1 
ATOM   1961 C C     . HIS A 1 441 ? 17.937  30.890  69.683  1.00 124.62 ?  422 HIS A C     1 
ATOM   1962 O O     . HIS A 1 441 ? 18.224  29.720  69.426  1.00 130.02 ?  422 HIS A O     1 
ATOM   1963 C CB    . HIS A 1 441 ? 17.558  31.220  72.146  1.00 130.86 ?  422 HIS A CB    1 
ATOM   1964 C CG    . HIS A 1 441 ? 17.157  29.789  72.264  1.00 128.30 ?  422 HIS A CG    1 
ATOM   1965 N ND1   . HIS A 1 441 ? 15.996  29.292  71.704  1.00 125.30 ?  422 HIS A ND1   1 
ATOM   1966 C CD2   . HIS A 1 441 ? 17.795  28.734  72.817  1.00 126.90 ?  422 HIS A CD2   1 
ATOM   1967 C CE1   . HIS A 1 441 ? 15.904  28.002  71.970  1.00 130.36 ?  422 HIS A CE1   1 
ATOM   1968 N NE2   . HIS A 1 441 ? 16.990  27.637  72.631  1.00 132.27 ?  422 HIS A NE2   1 
ATOM   1969 N N     . VAL A 1 442 ? 17.172  31.626  68.861  1.00 123.98 ?  423 VAL A N     1 
ATOM   1970 C CA    . VAL A 1 442 ? 16.748  31.055  67.585  1.00 121.98 ?  423 VAL A CA    1 
ATOM   1971 C C     . VAL A 1 442 ? 17.974  30.720  66.748  1.00 122.09 ?  423 VAL A C     1 
ATOM   1972 O O     . VAL A 1 442 ? 18.053  29.646  66.135  1.00 122.03 ?  423 VAL A O     1 
ATOM   1973 C CB    . VAL A 1 442 ? 15.782  32.002  66.848  1.00 119.68 ?  423 VAL A CB    1 
ATOM   1974 C CG1   . VAL A 1 442 ? 15.431  31.402  65.486  1.00 129.47 ?  423 VAL A CG1   1 
ATOM   1975 C CG2   . VAL A 1 442 ? 14.539  32.359  67.718  1.00 126.28 ?  423 VAL A CG2   1 
ATOM   1976 N N     . LYS A 1 443 ? 18.976  31.603  66.773  1.00 119.80 ?  424 LYS A N     1 
ATOM   1977 C CA    . LYS A 1 443 ? 20.169  31.403  65.962  1.00 120.84 ?  424 LYS A CA    1 
ATOM   1978 C C     . LYS A 1 443 ? 21.061  30.297  66.533  1.00 124.56 ?  424 LYS A C     1 
ATOM   1979 O O     . LYS A 1 443 ? 21.549  29.448  65.780  1.00 131.22 ?  424 LYS A O     1 
ATOM   1980 C CB    . LYS A 1 443 ? 20.966  32.708  65.814  1.00 115.06 ?  424 LYS A CB    1 
ATOM   1981 C CG    . LYS A 1 443 ? 20.184  33.876  65.238  1.00 113.05 ?  424 LYS A CG    1 
ATOM   1982 C CD    . LYS A 1 443 ? 21.075  35.094  65.034  1.00 120.85 ?  424 LYS A CD    1 
ATOM   1983 C CE    . LYS A 1 443 ? 20.217  36.287  64.601  1.00 126.01 ?  424 LYS A CE    1 
ATOM   1984 N NZ    . LYS A 1 443 ? 19.485  36.146  63.307  1.00 129.43 ?  424 LYS A NZ    1 
ATOM   1985 N N     . ASP A 1 444 ? 21.267  30.263  67.857  1.00 124.70 ?  425 ASP A N     1 
ATOM   1986 C CA    . ASP A 1 444 ? 22.007  29.152  68.461  1.00 129.32 ?  425 ASP A CA    1 
ATOM   1987 C C     . ASP A 1 444 ? 21.380  27.802  68.128  1.00 129.85 ?  425 ASP A C     1 
ATOM   1988 O O     . ASP A 1 444 ? 22.081  26.784  68.067  1.00 129.30 ?  425 ASP A O     1 
ATOM   1989 C CB    . ASP A 1 444 ? 22.059  29.291  69.985  1.00 136.90 ?  425 ASP A CB    1 
ATOM   1990 C CG    . ASP A 1 444 ? 22.925  30.445  70.460  1.00 139.27 ?  425 ASP A CG    1 
ATOM   1991 O OD1   . ASP A 1 444 ? 22.363  31.511  70.788  1.00 137.69 ?  425 ASP A OD1   1 
ATOM   1992 O OD2   . ASP A 1 444 ? 24.166  30.284  70.518  1.00 142.67 ?  425 ASP A OD2   1 
ATOM   1993 N N     . GLU A 1 445 ? 20.056  27.774  67.949  1.00 130.07 ?  426 GLU A N     1 
ATOM   1994 C CA    . GLU A 1 445 ? 19.310  26.533  67.784  1.00 131.12 ?  426 GLU A CA    1 
ATOM   1995 C C     . GLU A 1 445 ? 19.423  26.030  66.356  1.00 134.53 ?  426 GLU A C     1 
ATOM   1996 O O     . GLU A 1 445 ? 19.561  24.823  66.121  1.00 135.42 ?  426 GLU A O     1 
ATOM   1997 C CB    . GLU A 1 445 ? 17.845  26.769  68.178  1.00 131.43 ?  426 GLU A CB    1 
ATOM   1998 C CG    . GLU A 1 445 ? 16.923  25.554  68.233  1.00 132.83 ?  426 GLU A CG    1 
ATOM   1999 C CD    . GLU A 1 445 ? 17.251  24.615  69.389  1.00 137.02 ?  426 GLU A CD    1 
ATOM   2000 O OE1   . GLU A 1 445 ? 17.826  25.073  70.401  1.00 130.93 ?  426 GLU A OE1   1 
ATOM   2001 O OE2   . GLU A 1 445 ? 16.901  23.419  69.299  1.00 148.16 ?  426 GLU A OE2   1 
ATOM   2002 N N     . GLN A 1 446 ? 19.385  26.945  65.393  1.00 132.11 ?  427 GLN A N     1 
ATOM   2003 C CA    . GLN A 1 446 ? 19.673  26.542  64.029  1.00 131.35 ?  427 GLN A CA    1 
ATOM   2004 C C     . GLN A 1 446 ? 21.128  26.112  63.882  1.00 131.14 ?  427 GLN A C     1 
ATOM   2005 O O     . GLN A 1 446 ? 21.400  25.065  63.289  1.00 135.89 ?  427 GLN A O     1 
ATOM   2006 C CB    . GLN A 1 446 ? 19.310  27.666  63.077  1.00 128.07 ?  427 GLN A CB    1 
ATOM   2007 C CG    . GLN A 1 446 ? 17.852  28.022  63.227  1.00 132.16 ?  427 GLN A CG    1 
ATOM   2008 C CD    . GLN A 1 446 ? 17.473  29.274  62.472  1.00 144.87 ?  427 GLN A CD    1 
ATOM   2009 O OE1   . GLN A 1 446 ? 18.337  30.034  62.016  1.00 145.53 ?  427 GLN A OE1   1 
ATOM   2010 N NE2   . GLN A 1 446 ? 16.169  29.518  62.358  1.00 145.81 ?  427 GLN A NE2   1 
ATOM   2011 N N     . ILE A 1 447 ? 22.074  26.861  64.465  1.00 128.30 ?  428 ILE A N     1 
ATOM   2012 C CA    . ILE A 1 447 ? 23.490  26.541  64.257  1.00 128.79 ?  428 ILE A CA    1 
ATOM   2013 C C     . ILE A 1 447 ? 23.859  25.168  64.821  1.00 129.87 ?  428 ILE A C     1 
ATOM   2014 O O     . ILE A 1 447 ? 24.671  24.450  64.231  1.00 131.66 ?  428 ILE A O     1 
ATOM   2015 C CB    . ILE A 1 447 ? 24.415  27.645  64.810  1.00 127.80 ?  428 ILE A CB    1 
ATOM   2016 C CG1   . ILE A 1 447 ? 24.347  28.900  63.934  1.00 129.89 ?  428 ILE A CG1   1 
ATOM   2017 C CG2   . ILE A 1 447 ? 25.863  27.151  64.955  1.00 126.39 ?  428 ILE A CG2   1 
ATOM   2018 C CD1   . ILE A 1 447 ? 25.135  30.072  64.491  1.00 132.01 ?  428 ILE A CD1   1 
ATOM   2019 N N     . GLU A 1 448 ? 23.293  24.761  65.951  1.00 133.78 ?  429 GLU A N     1 
ATOM   2020 C CA    . GLU A 1 448 ? 23.642  23.419  66.400  1.00 137.70 ?  429 GLU A CA    1 
ATOM   2021 C C     . GLU A 1 448 ? 22.728  22.363  65.782  1.00 137.81 ?  429 GLU A C     1 
ATOM   2022 O O     . GLU A 1 448 ? 22.726  21.211  66.230  1.00 141.49 ?  429 GLU A O     1 
ATOM   2023 C CB    . GLU A 1 448 ? 23.709  23.350  67.941  1.00 142.15 ?  429 GLU A CB    1 
ATOM   2024 C CG    . GLU A 1 448 ? 22.460  23.622  68.826  1.00 146.70 ?  429 GLU A CG    1 
ATOM   2025 C CD    . GLU A 1 448 ? 21.637  22.367  69.164  1.00 150.95 ?  429 GLU A CD    1 
ATOM   2026 O OE1   . GLU A 1 448 ? 22.182  21.249  69.029  1.00 150.15 ?  429 GLU A OE1   1 
ATOM   2027 O OE2   . GLU A 1 448 ? 20.480  22.495  69.640  1.00 151.31 ?  429 GLU A OE2   1 
ATOM   2028 N N     . HIS A 1 449 ? 22.000  22.729  64.721  1.00 132.44 ?  430 HIS A N     1 
ATOM   2029 C CA    . HIS A 1 449 ? 21.219  21.806  63.905  1.00 131.90 ?  430 HIS A CA    1 
ATOM   2030 C C     . HIS A 1 449 ? 21.872  21.536  62.561  1.00 131.34 ?  430 HIS A C     1 
ATOM   2031 O O     . HIS A 1 449 ? 22.092  20.378  62.208  1.00 134.28 ?  430 HIS A O     1 
ATOM   2032 C CB    . HIS A 1 449 ? 19.802  22.353  63.694  1.00 134.69 ?  430 HIS A CB    1 
ATOM   2033 C CG    . HIS A 1 449 ? 18.992  21.586  62.691  1.00 136.82 ?  430 HIS A CG    1 
ATOM   2034 N ND1   . HIS A 1 449 ? 18.936  21.929  61.356  1.00 136.36 ?  430 HIS A ND1   1 
ATOM   2035 C CD2   . HIS A 1 449 ? 18.194  20.499  62.834  1.00 134.71 ?  430 HIS A CD2   1 
ATOM   2036 C CE1   . HIS A 1 449 ? 18.134  21.091  60.722  1.00 138.61 ?  430 HIS A CE1   1 
ATOM   2037 N NE2   . HIS A 1 449 ? 17.672  20.213  61.596  1.00 135.60 ?  430 HIS A NE2   1 
ATOM   2038 N N     . TRP A 1 450 ? 22.187  22.581  61.793  1.00 131.32 ?  431 TRP A N     1 
ATOM   2039 C CA    . TRP A 1 450 ? 22.986  22.390  60.590  1.00 130.29 ?  431 TRP A CA    1 
ATOM   2040 C C     . TRP A 1 450 ? 24.409  21.973  60.910  1.00 132.47 ?  431 TRP A C     1 
ATOM   2041 O O     . TRP A 1 450 ? 25.095  21.445  60.031  1.00 140.52 ?  431 TRP A O     1 
ATOM   2042 C CB    . TRP A 1 450 ? 22.991  23.655  59.741  1.00 128.64 ?  431 TRP A CB    1 
ATOM   2043 C CG    . TRP A 1 450 ? 21.621  24.101  59.438  1.00 136.17 ?  431 TRP A CG    1 
ATOM   2044 C CD1   . TRP A 1 450 ? 20.891  25.017  60.129  1.00 140.40 ?  431 TRP A CD1   1 
ATOM   2045 C CD2   . TRP A 1 450 ? 20.794  23.659  58.356  1.00 140.19 ?  431 TRP A CD2   1 
ATOM   2046 N NE1   . TRP A 1 450 ? 19.650  25.168  59.552  1.00 143.46 ?  431 TRP A NE1   1 
ATOM   2047 C CE2   . TRP A 1 450 ? 19.569  24.348  58.458  1.00 142.27 ?  431 TRP A CE2   1 
ATOM   2048 C CE3   . TRP A 1 450 ? 20.968  22.749  57.314  1.00 142.96 ?  431 TRP A CE3   1 
ATOM   2049 C CZ2   . TRP A 1 450 ? 18.526  24.157  57.555  1.00 142.78 ?  431 TRP A CZ2   1 
ATOM   2050 C CZ3   . TRP A 1 450 ? 19.928  22.556  56.420  1.00 149.02 ?  431 TRP A CZ3   1 
ATOM   2051 C CH2   . TRP A 1 450 ? 18.724  23.259  56.546  1.00 146.71 ?  431 TRP A CH2   1 
ATOM   2052 N N     . LYS A 1 451 ? 24.870  22.189  62.138  1.00 128.30 ?  432 LYS A N     1 
ATOM   2053 C CA    . LYS A 1 451 ? 26.158  21.646  62.529  1.00 128.01 ?  432 LYS A CA    1 
ATOM   2054 C C     . LYS A 1 451 ? 26.050  20.155  62.838  1.00 135.65 ?  432 LYS A C     1 
ATOM   2055 O O     . LYS A 1 451 ? 27.074  19.460  62.861  1.00 136.71 ?  432 LYS A O     1 
ATOM   2056 C CB    . LYS A 1 451 ? 26.687  22.430  63.726  1.00 132.00 ?  432 LYS A CB    1 
ATOM   2057 C CG    . LYS A 1 451 ? 28.118  22.207  64.133  1.00 137.35 ?  432 LYS A CG    1 
ATOM   2058 C CD    . LYS A 1 451 ? 28.402  23.073  65.368  1.00 141.58 ?  432 LYS A CD    1 
ATOM   2059 C CE    . LYS A 1 451 ? 28.421  24.579  65.038  1.00 142.93 ?  432 LYS A CE    1 
ATOM   2060 N NZ    . LYS A 1 451 ? 29.547  25.039  64.161  1.00 145.35 ?  432 LYS A NZ    1 
ATOM   2061 N N     . LYS A 1 452 ? 24.826  19.655  63.075  1.00 137.64 ?  433 LYS A N     1 
ATOM   2062 C CA    . LYS A 1 452 ? 24.572  18.214  63.100  1.00 133.73 ?  433 LYS A CA    1 
ATOM   2063 C C     . LYS A 1 452 ? 24.566  17.620  61.700  1.00 132.26 ?  433 LYS A C     1 
ATOM   2064 O O     . LYS A 1 452 ? 25.080  16.518  61.493  1.00 137.59 ?  433 LYS A O     1 
ATOM   2065 C CB    . LYS A 1 452 ? 23.240  17.891  63.788  1.00 134.87 ?  433 LYS A CB    1 
ATOM   2066 C CG    . LYS A 1 452 ? 23.297  17.776  65.302  1.00 139.25 ?  433 LYS A CG    1 
ATOM   2067 C CD    . LYS A 1 452 ? 22.003  17.172  65.858  1.00 139.31 ?  433 LYS A CD    1 
ATOM   2068 C CE    . LYS A 1 452 ? 22.164  16.714  67.318  1.00 142.12 ?  433 LYS A CE    1 
ATOM   2069 N NZ    . LYS A 1 452 ? 22.364  17.830  68.300  1.00 140.52 ?  433 LYS A NZ    1 
ATOM   2070 N N     . ILE A 1 453 ? 23.980  18.316  60.729  1.00 129.65 ?  434 ILE A N     1 
ATOM   2071 C CA    . ILE A 1 453 ? 24.010  17.806  59.364  1.00 128.25 ?  434 ILE A CA    1 
ATOM   2072 C C     . ILE A 1 453 ? 25.450  17.648  58.868  1.00 130.05 ?  434 ILE A C     1 
ATOM   2073 O O     . ILE A 1 453 ? 25.829  16.564  58.412  1.00 134.37 ?  434 ILE A O     1 
ATOM   2074 C CB    . ILE A 1 453 ? 23.137  18.674  58.439  1.00 126.09 ?  434 ILE A CB    1 
ATOM   2075 C CG1   . ILE A 1 453 ? 21.656  18.472  58.799  1.00 125.11 ?  434 ILE A CG1   1 
ATOM   2076 C CG2   . ILE A 1 453 ? 23.424  18.398  56.981  1.00 131.37 ?  434 ILE A CG2   1 
ATOM   2077 C CD1   . ILE A 1 453 ? 20.699  19.405  58.094  1.00 128.73 ?  434 ILE A CD1   1 
ATOM   2078 N N     . VAL A 1 454 ? 26.294  18.683  59.002  1.00 126.95 ?  435 VAL A N     1 
ATOM   2079 C CA    . VAL A 1 454 ? 27.692  18.517  58.564  1.00 128.65 ?  435 VAL A CA    1 
ATOM   2080 C C     . VAL A 1 454 ? 28.448  17.442  59.348  1.00 135.64 ?  435 VAL A C     1 
ATOM   2081 O O     . VAL A 1 454 ? 29.482  16.961  58.875  1.00 141.41 ?  435 VAL A O     1 
ATOM   2082 C CB    . VAL A 1 454 ? 28.544  19.811  58.622  1.00 126.62 ?  435 VAL A CB    1 
ATOM   2083 C CG1   . VAL A 1 454 ? 28.051  20.857  57.693  1.00 123.68 ?  435 VAL A CG1   1 
ATOM   2084 C CG2   . VAL A 1 454 ? 28.615  20.341  60.029  1.00 138.55 ?  435 VAL A CG2   1 
ATOM   2085 N N     . LYS A 1 455 ? 28.000  17.064  60.547  1.00 135.07 ?  436 LYS A N     1 
ATOM   2086 C CA    . LYS A 1 455 ? 28.681  15.942  61.186  1.00 137.48 ?  436 LYS A CA    1 
ATOM   2087 C C     . LYS A 1 455 ? 28.307  14.636  60.503  1.00 137.85 ?  436 LYS A C     1 
ATOM   2088 O O     . LYS A 1 455 ? 29.136  13.727  60.405  1.00 142.86 ?  436 LYS A O     1 
ATOM   2089 C CB    . LYS A 1 455 ? 28.378  15.885  62.691  1.00 141.10 ?  436 LYS A CB    1 
ATOM   2090 C CG    . LYS A 1 455 ? 29.053  14.706  63.438  1.00 143.02 ?  436 LYS A CG    1 
ATOM   2091 C CD    . LYS A 1 455 ? 28.572  14.582  64.896  1.00 152.08 ?  436 LYS A CD    1 
ATOM   2092 C CE    . LYS A 1 455 ? 29.182  13.371  65.637  1.00 158.33 ?  436 LYS A CE    1 
ATOM   2093 N NZ    . LYS A 1 455 ? 28.679  13.214  67.056  1.00 146.36 ?  436 LYS A NZ    1 
ATOM   2094 N N     . THR A 1 456 ? 27.086  14.543  59.981  1.00 133.77 ?  437 THR A N     1 
ATOM   2095 C CA    . THR A 1 456 ? 26.675  13.340  59.279  1.00 138.46 ?  437 THR A CA    1 
ATOM   2096 C C     . THR A 1 456 ? 26.987  13.396  57.777  1.00 137.65 ?  437 THR A C     1 
ATOM   2097 O O     . THR A 1 456 ? 27.192  12.339  57.170  1.00 139.16 ?  437 THR A O     1 
ATOM   2098 C CB    . THR A 1 456 ? 25.185  13.072  59.566  1.00 137.04 ?  437 THR A CB    1 
ATOM   2099 O OG1   . THR A 1 456 ? 24.990  12.993  60.985  1.00 136.95 ?  437 THR A OG1   1 
ATOM   2100 C CG2   . THR A 1 456 ? 24.737  11.746  58.982  1.00 137.34 ?  437 THR A CG2   1 
ATOM   2101 N N     . GLN A 1 457 ? 27.085  14.589  57.165  1.00 135.67 ?  438 GLN A N     1 
ATOM   2102 C CA    . GLN A 1 457 ? 27.676  14.672  55.826  1.00 128.95 ?  438 GLN A CA    1 
ATOM   2103 C C     . GLN A 1 457 ? 29.102  14.160  55.831  1.00 130.35 ?  438 GLN A C     1 
ATOM   2104 O O     . GLN A 1 457 ? 29.542  13.521  54.873  1.00 136.41 ?  438 GLN A O     1 
ATOM   2105 C CB    . GLN A 1 457 ? 27.703  16.101  55.283  1.00 129.54 ?  438 GLN A CB    1 
ATOM   2106 C CG    . GLN A 1 457 ? 26.390  16.711  54.874  1.00 132.64 ?  438 GLN A CG    1 
ATOM   2107 C CD    . GLN A 1 457 ? 25.686  15.930  53.802  1.00 132.61 ?  438 GLN A CD    1 
ATOM   2108 O OE1   . GLN A 1 457 ? 24.619  15.373  54.043  1.00 127.50 ?  438 GLN A OE1   1 
ATOM   2109 N NE2   . GLN A 1 457 ? 26.300  15.831  52.627  1.00 138.36 ?  438 GLN A NE2   1 
ATOM   2110 N N     . GLU A 1 458 ? 29.854  14.470  56.879  1.00 132.51 ?  439 GLU A N     1 
ATOM   2111 C CA    . GLU A 1 458 ? 31.241  14.047  56.934  1.00 133.81 ?  439 GLU A CA    1 
ATOM   2112 C C     . GLU A 1 458 ? 31.396  12.605  57.377  1.00 136.44 ?  439 GLU A C     1 
ATOM   2113 O O     . GLU A 1 458 ? 32.428  12.003  57.077  1.00 141.79 ?  439 GLU A O     1 
ATOM   2114 C CB    . GLU A 1 458 ? 32.038  14.972  57.846  1.00 142.54 ?  439 GLU A CB    1 
ATOM   2115 C CG    . GLU A 1 458 ? 32.232  16.342  57.232  1.00 147.64 ?  439 GLU A CG    1 
ATOM   2116 C CD    . GLU A 1 458 ? 33.025  17.298  58.112  1.00 160.22 ?  439 GLU A CD    1 
ATOM   2117 O OE1   . GLU A 1 458 ? 33.310  16.955  59.286  1.00 159.10 ?  439 GLU A OE1   1 
ATOM   2118 O OE2   . GLU A 1 458 ? 33.353  18.405  57.625  1.00 162.61 ?  439 GLU A OE2   1 
ATOM   2119 N N     . GLU A 1 459 ? 30.405  12.027  58.067  1.00 137.03 ?  440 GLU A N     1 
ATOM   2120 C CA    . GLU A 1 459 ? 30.442  10.580  58.277  1.00 140.01 ?  440 GLU A CA    1 
ATOM   2121 C C     . GLU A 1 459 ? 30.168  9.830   56.975  1.00 135.51 ?  440 GLU A C     1 
ATOM   2122 O O     . GLU A 1 459 ? 30.686  8.726   56.773  1.00 135.84 ?  440 GLU A O     1 
ATOM   2123 C CB    . GLU A 1 459 ? 29.459  10.162  59.380  1.00 139.02 ?  440 GLU A CB    1 
ATOM   2124 C CG    . GLU A 1 459 ? 29.902  10.627  60.782  1.00 152.39 ?  440 GLU A CG    1 
ATOM   2125 C CD    . GLU A 1 459 ? 29.043  10.084  61.929  1.00 159.87 ?  440 GLU A CD    1 
ATOM   2126 O OE1   . GLU A 1 459 ? 28.228  9.161   61.677  1.00 159.23 ?  440 GLU A OE1   1 
ATOM   2127 O OE2   . GLU A 1 459 ? 29.196  10.581  63.079  1.00 152.79 ?  440 GLU A OE2   1 
ATOM   2128 N N     . LEU A 1 460 ? 29.399  10.432  56.071  1.00 130.25 ?  441 LEU A N     1 
ATOM   2129 C CA    . LEU A 1 460 ? 29.124  9.842   54.769  1.00 124.71 ?  441 LEU A CA    1 
ATOM   2130 C C     . LEU A 1 460 ? 30.307  10.030  53.820  1.00 127.07 ?  441 LEU A C     1 
ATOM   2131 O O     . LEU A 1 460 ? 30.701  9.090   53.124  1.00 127.18 ?  441 LEU A O     1 
ATOM   2132 C CB    . LEU A 1 460 ? 27.857  10.481  54.197  1.00 126.81 ?  441 LEU A CB    1 
ATOM   2133 C CG    . LEU A 1 460 ? 27.095  9.924   53.005  1.00 120.58 ?  441 LEU A CG    1 
ATOM   2134 C CD1   . LEU A 1 460 ? 26.348  8.725   53.500  1.00 128.16 ?  441 LEU A CD1   1 
ATOM   2135 C CD2   . LEU A 1 460 ? 26.128  10.952  52.447  1.00 115.07 ?  441 LEU A CD2   1 
ATOM   2136 N N     . LYS A 1 461 ? 30.875  11.246  53.769  1.00 130.61 ?  442 LYS A N     1 
ATOM   2137 C CA    . LYS A 1 461 ? 32.071  11.491  52.962  1.00 126.28 ?  442 LYS A CA    1 
ATOM   2138 C C     . LYS A 1 461 ? 33.187  10.534  53.342  1.00 131.13 ?  442 LYS A C     1 
ATOM   2139 O O     . LYS A 1 461 ? 33.850  9.974   52.465  1.00 139.17 ?  442 LYS A O     1 
ATOM   2140 C CB    . LYS A 1 461 ? 32.545  12.942  53.110  1.00 122.47 ?  442 LYS A CB    1 
ATOM   2141 C CG    . LYS A 1 461 ? 33.817  13.293  52.332  1.00 119.75 ?  442 LYS A CG    1 
ATOM   2142 C CD    . LYS A 1 461 ? 34.211  14.759  52.541  1.00 127.91 ?  442 LYS A CD    1 
ATOM   2143 C CE    . LYS A 1 461 ? 35.465  15.167  51.761  1.00 129.72 ?  442 LYS A CE    1 
ATOM   2144 N NZ    . LYS A 1 461 ? 35.875  16.584  52.051  1.00 125.26 ?  442 LYS A NZ    1 
ATOM   2145 N N     . GLU A 1 462 ? 33.409  10.324  54.643  1.00 129.28 ?  443 GLU A N     1 
ATOM   2146 C CA    . GLU A 1 462 ? 34.307  9.254   55.067  1.00 133.15 ?  443 GLU A CA    1 
ATOM   2147 C C     . GLU A 1 462 ? 33.836  7.895   54.560  1.00 130.92 ?  443 GLU A C     1 
ATOM   2148 O O     . GLU A 1 462 ? 34.661  7.048   54.194  1.00 129.36 ?  443 GLU A O     1 
ATOM   2149 C CB    . GLU A 1 462 ? 34.420  9.220   56.596  1.00 140.55 ?  443 GLU A CB    1 
ATOM   2150 C CG    . GLU A 1 462 ? 35.094  10.442  57.244  1.00 149.73 ?  443 GLU A CG    1 
ATOM   2151 C CD    . GLU A 1 462 ? 35.394  10.244  58.745  1.00 159.74 ?  443 GLU A CD    1 
ATOM   2152 O OE1   . GLU A 1 462 ? 35.587  9.079   59.165  1.00 161.07 ?  443 GLU A OE1   1 
ATOM   2153 O OE2   . GLU A 1 462 ? 35.425  11.249  59.507  1.00 159.90 ?  443 GLU A OE2   1 
ATOM   2154 N N     . LEU A 1 463 ? 32.517  7.672   54.525  1.00 130.48 ?  444 LEU A N     1 
ATOM   2155 C CA    . LEU A 1 463 ? 31.995  6.342   54.216  1.00 128.37 ?  444 LEU A CA    1 
ATOM   2156 C C     . LEU A 1 463 ? 32.198  5.998   52.752  1.00 128.15 ?  444 LEU A C     1 
ATOM   2157 O O     . LEU A 1 463 ? 32.666  4.903   52.421  1.00 129.16 ?  444 LEU A O     1 
ATOM   2158 C CB    . LEU A 1 463 ? 30.509  6.254   54.542  1.00 128.43 ?  444 LEU A CB    1 
ATOM   2159 C CG    . LEU A 1 463 ? 30.035  4.817   54.718  1.00 120.06 ?  444 LEU A CG    1 
ATOM   2160 C CD1   . LEU A 1 463 ? 30.664  4.249   55.990  1.00 111.03 ?  444 LEU A CD1   1 
ATOM   2161 C CD2   . LEU A 1 463 ? 28.518  4.711   54.700  1.00 122.03 ?  444 LEU A CD2   1 
ATOM   2162 N N     . LEU A 1 464 ? 31.804  6.907   51.855  1.00 131.19 ?  445 LEU A N     1 
ATOM   2163 C CA    . LEU A 1 464 ? 32.006  6.657   50.434  1.00 128.55 ?  445 LEU A CA    1 
ATOM   2164 C C     . LEU A 1 464 ? 33.479  6.411   50.127  1.00 127.94 ?  445 LEU A C     1 
ATOM   2165 O O     . LEU A 1 464 ? 33.806  5.497   49.363  1.00 131.12 ?  445 LEU A O     1 
ATOM   2166 C CB    . LEU A 1 464 ? 31.449  7.809   49.590  1.00 121.35 ?  445 LEU A CB    1 
ATOM   2167 C CG    . LEU A 1 464 ? 29.967  8.118   49.837  1.00 122.42 ?  445 LEU A CG    1 
ATOM   2168 C CD1   . LEU A 1 464 ? 29.461  9.105   48.821  1.00 126.45 ?  445 LEU A CD1   1 
ATOM   2169 C CD2   . LEU A 1 464 ? 29.089  6.871   49.859  1.00 120.87 ?  445 LEU A CD2   1 
ATOM   2170 N N     . ASN A 1 465 ? 34.368  7.171   50.758  1.00 127.76 ?  446 ASN A N     1 
ATOM   2171 C CA    . ASN A 1 465 ? 35.818  7.011   50.478  1.00 124.47 ?  446 ASN A CA    1 
ATOM   2172 C C     . ASN A 1 465 ? 36.231  5.573   50.745  1.00 128.85 ?  446 ASN A C     1 
ATOM   2173 O O     . ASN A 1 465 ? 36.971  5.017   49.949  1.00 130.40 ?  446 ASN A O     1 
ATOM   2174 C CB    . ASN A 1 465 ? 36.669  8.008   51.246  1.00 124.31 ?  446 ASN A CB    1 
ATOM   2175 C CG    . ASN A 1 465 ? 36.741  9.312   50.495  1.00 125.56 ?  446 ASN A CG    1 
ATOM   2176 O OD1   . ASN A 1 465 ? 35.832  9.630   49.739  1.00 120.64 ?  446 ASN A OD1   1 
ATOM   2177 N ND2   . ASN A 1 465 ? 37.815  10.057  50.684  1.00 137.05 ?  446 ASN A ND2   1 
ATOM   2178 N N     . LYS A 1 466 ? 35.731  4.982   51.815  1.00 131.56 ?  447 LYS A N     1 
ATOM   2179 C CA    . LYS A 1 466 ? 36.086  3.560   51.997  1.00 131.08 ?  447 LYS A CA    1 
ATOM   2180 C C     . LYS A 1 466 ? 35.416  2.760   50.883  1.00 126.46 ?  447 LYS A C     1 
ATOM   2181 O O     . LYS A 1 466 ? 36.086  1.921   50.291  1.00 127.20 ?  447 LYS A O     1 
ATOM   2182 C CB    . LYS A 1 466 ? 35.739  3.072   53.403  1.00 132.23 ?  447 LYS A CB    1 
ATOM   2183 C CG    . LYS A 1 466 ? 36.786  3.397   54.460  1.00 134.25 ?  447 LYS A CG    1 
ATOM   2184 C CD    . LYS A 1 466 ? 36.604  2.642   55.759  1.00 138.06 ?  447 LYS A CD    1 
ATOM   2185 C CE    . LYS A 1 466 ? 36.617  3.548   56.972  1.00 147.91 ?  447 LYS A CE    1 
ATOM   2186 N NZ    . LYS A 1 466 ? 36.713  2.787   58.240  1.00 142.37 ?  447 LYS A NZ    1 
ATOM   2187 N N     . MET A 1 467 ? 34.169  3.079   50.553  1.00 124.90 ?  448 MET A N     1 
ATOM   2188 C CA    . MET A 1 467 ? 33.483  2.264   49.527  1.00 125.68 ?  448 MET A CA    1 
ATOM   2189 C C     . MET A 1 467 ? 34.221  2.356   48.202  1.00 125.95 ?  448 MET A C     1 
ATOM   2190 O O     . MET A 1 467 ? 34.482  1.316   47.610  1.00 127.31 ?  448 MET A O     1 
ATOM   2191 C CB    . MET A 1 467 ? 32.074  2.789   49.295  1.00 122.23 ?  448 MET A CB    1 
ATOM   2192 C CG    . MET A 1 467 ? 31.438  3.272   50.545  1.00 122.33 ?  448 MET A CG    1 
ATOM   2193 S SD    . MET A 1 467 ? 29.896  2.394   50.671  1.00 134.38 ?  448 MET A SD    1 
ATOM   2194 C CE    . MET A 1 467 ? 29.307  2.576   48.995  1.00 131.39 ?  448 MET A CE    1 
ATOM   2195 N N     . VAL A 1 468 ? 34.594  3.553   47.782  1.00 124.16 ?  449 VAL A N     1 
ATOM   2196 C CA    . VAL A 1 468 ? 35.297  3.625   46.475  1.00 121.75 ?  449 VAL A CA    1 
ATOM   2197 C C     . VAL A 1 468 ? 36.619  2.876   46.586  1.00 126.42 ?  449 VAL A C     1 
ATOM   2198 O O     . VAL A 1 468 ? 36.883  2.034   45.741  1.00 132.04 ?  449 VAL A O     1 
ATOM   2199 C CB    . VAL A 1 468 ? 35.529  5.074   46.041  1.00 115.10 ?  449 VAL A CB    1 
ATOM   2200 C CG1   . VAL A 1 468 ? 36.827  5.203   45.271  1.00 115.66 ?  449 VAL A CG1   1 
ATOM   2201 C CG2   . VAL A 1 468 ? 34.360  5.579   45.223  1.00 111.91 ?  449 VAL A CG2   1 
ATOM   2202 N N     . ASN A 1 469 ? 37.370  3.076   47.662  1.00 123.81 ?  450 ASN A N     1 
ATOM   2203 C CA    . ASN A 1 469 ? 38.655  2.345   47.755  1.00 124.55 ?  450 ASN A CA    1 
ATOM   2204 C C     . ASN A 1 469 ? 38.379  0.847   47.838  1.00 128.33 ?  450 ASN A C     1 
ATOM   2205 O O     . ASN A 1 469 ? 39.133  0.091   47.255  1.00 128.65 ?  450 ASN A O     1 
ATOM   2206 C CB    . ASN A 1 469 ? 39.607  2.938   48.785  1.00 127.76 ?  450 ASN A CB    1 
ATOM   2207 C CG    . ASN A 1 469 ? 40.416  4.063   48.183  1.00 134.71 ?  450 ASN A CG    1 
ATOM   2208 O OD1   . ASN A 1 469 ? 39.856  5.040   47.706  1.00 135.07 ?  450 ASN A OD1   1 
ATOM   2209 N ND2   . ASN A 1 469 ? 41.729  3.930   48.177  1.00 137.44 ?  450 ASN A ND2   1 
ATOM   2210 N N     . LEU A 1 470 ? 37.343  0.438   48.557  1.00 127.73 ?  451 LEU A N     1 
ATOM   2211 C CA    . LEU A 1 470 ? 37.023  -1.002  48.609  1.00 125.26 ?  451 LEU A CA    1 
ATOM   2212 C C     . LEU A 1 470 ? 36.658  -1.500  47.214  1.00 127.43 ?  451 LEU A C     1 
ATOM   2213 O O     . LEU A 1 470 ? 37.095  -2.593  46.859  1.00 131.40 ?  451 LEU A O     1 
ATOM   2214 C CB    . LEU A 1 470 ? 35.826  -1.196  49.528  1.00 120.72 ?  451 LEU A CB    1 
ATOM   2215 C CG    . LEU A 1 470 ? 35.818  -2.536  50.243  1.00 121.59 ?  451 LEU A CG    1 
ATOM   2216 C CD1   . LEU A 1 470 ? 36.900  -2.560  51.308  1.00 118.98 ?  451 LEU A CD1   1 
ATOM   2217 C CD2   . LEU A 1 470 ? 34.448  -2.824  50.831  1.00 121.52 ?  451 LEU A CD2   1 
ATOM   2218 N N     . LYS A 1 471 ? 35.897  -0.724  46.448  1.00 126.23 ?  452 LYS A N     1 
ATOM   2219 C CA    . LYS A 1 471 ? 35.480  -1.239  45.124  1.00 124.84 ?  452 LYS A CA    1 
ATOM   2220 C C     . LYS A 1 471 ? 36.723  -1.505  44.286  1.00 126.75 ?  452 LYS A C     1 
ATOM   2221 O O     . LYS A 1 471 ? 36.828  -2.623  43.779  1.00 131.91 ?  452 LYS A O     1 
ATOM   2222 C CB    . LYS A 1 471 ? 34.588  -0.229  44.409  1.00 121.14 ?  452 LYS A CB    1 
ATOM   2223 C CG    . LYS A 1 471 ? 34.093  -0.653  43.037  1.00 115.02 ?  452 LYS A CG    1 
ATOM   2224 C CD    . LYS A 1 471 ? 32.631  -0.333  42.802  1.00 119.06 ?  452 LYS A CD    1 
ATOM   2225 C CE    . LYS A 1 471 ? 32.295  0.094   41.389  1.00 124.05 ?  452 LYS A CE    1 
ATOM   2226 N NZ    . LYS A 1 471 ? 30.856  -0.092  41.089  1.00 129.20 ?  452 LYS A NZ    1 
ATOM   2227 N N     . GLU A 1 472 ? 37.665  -0.566  44.275  1.00 125.33 ?  453 GLU A N     1 
ATOM   2228 C CA    . GLU A 1 472 ? 38.914  -0.758  43.507  1.00 123.31 ?  453 GLU A CA    1 
ATOM   2229 C C     . GLU A 1 472 ? 39.567  -2.034  44.011  1.00 125.37 ?  453 GLU A C     1 
ATOM   2230 O O     . GLU A 1 472 ? 39.950  -2.843  43.181  1.00 124.66 ?  453 GLU A O     1 
ATOM   2231 C CB    . GLU A 1 472 ? 39.827  0.446   43.670  1.00 127.79 ?  453 GLU A CB    1 
ATOM   2232 C CG    . GLU A 1 472 ? 39.114  1.745   43.375  1.00 133.62 ?  453 GLU A CG    1 
ATOM   2233 C CD    . GLU A 1 472 ? 38.717  1.931   41.924  1.00 146.39 ?  453 GLU A CD    1 
ATOM   2234 O OE1   . GLU A 1 472 ? 39.615  1.855   41.068  1.00 155.65 ?  453 GLU A OE1   1 
ATOM   2235 O OE2   . GLU A 1 472 ? 37.513  2.158   41.652  1.00 143.55 ?  453 GLU A OE2   1 
ATOM   2236 N N     . LYS A 1 473 ? 39.614  -2.243  45.323  1.00 127.72 ?  454 LYS A N     1 
ATOM   2237 C CA    . LYS A 1 473 ? 40.197  -3.529  45.717  1.00 128.86 ?  454 LYS A CA    1 
ATOM   2238 C C     . LYS A 1 473 ? 39.348  -4.707  45.233  1.00 128.34 ?  454 LYS A C     1 
ATOM   2239 O O     . LYS A 1 473 ? 39.894  -5.757  44.876  1.00 126.24 ?  454 LYS A O     1 
ATOM   2240 C CB    . LYS A 1 473 ? 40.396  -3.619  47.244  1.00 128.35 ?  454 LYS A CB    1 
ATOM   2241 C CG    . LYS A 1 473 ? 41.235  -2.497  47.897  1.00 135.22 ?  454 LYS A CG    1 
ATOM   2242 C CD    . LYS A 1 473 ? 41.469  -2.722  49.421  1.00 138.69 ?  454 LYS A CD    1 
ATOM   2243 C CE    . LYS A 1 473 ? 42.311  -1.587  50.064  1.00 137.91 ?  454 LYS A CE    1 
ATOM   2244 N NZ    . LYS A 1 473 ? 42.645  -1.767  51.526  1.00 126.20 ?  454 LYS A NZ    1 
ATOM   2245 N N     . ILE A 1 474 ? 38.017  -4.569  45.223  1.00 126.87 ?  455 ILE A N     1 
ATOM   2246 C CA    . ILE A 1 474 ? 37.184  -5.630  44.660  1.00 120.29 ?  455 ILE A CA    1 
ATOM   2247 C C     . ILE A 1 474 ? 37.408  -5.758  43.169  1.00 124.79 ?  455 ILE A C     1 
ATOM   2248 O O     . ILE A 1 474 ? 37.476  -6.873  42.639  1.00 130.91 ?  455 ILE A O     1 
ATOM   2249 C CB    . ILE A 1 474 ? 35.695  -5.413  44.983  1.00 123.63 ?  455 ILE A CB    1 
ATOM   2250 C CG1   . ILE A 1 474 ? 35.423  -5.747  46.452  1.00 131.91 ?  455 ILE A CG1   1 
ATOM   2251 C CG2   . ILE A 1 474 ? 34.788  -6.171  44.023  1.00 123.04 ?  455 ILE A CG2   1 
ATOM   2252 C CD1   . ILE A 1 474 ? 34.023  -5.427  46.891  1.00 135.20 ?  455 ILE A CD1   1 
ATOM   2253 N N     . LYS A 1 475 ? 37.532  -4.629  42.466  1.00 131.44 ?  456 LYS A N     1 
ATOM   2254 C CA    . LYS A 1 475 ? 37.709  -4.686  41.017  1.00 128.81 ?  456 LYS A CA    1 
ATOM   2255 C C     . LYS A 1 475 ? 38.994  -5.434  40.665  1.00 126.15 ?  456 LYS A C     1 
ATOM   2256 O O     . LYS A 1 475 ? 39.003  -6.259  39.745  1.00 127.74 ?  456 LYS A O     1 
ATOM   2257 C CB    . LYS A 1 475 ? 37.683  -3.265  40.427  1.00 127.52 ?  456 LYS A CB    1 
ATOM   2258 C CG    . LYS A 1 475 ? 37.747  -3.171  38.904  1.00 131.90 ?  456 LYS A CG    1 
ATOM   2259 C CD    . LYS A 1 475 ? 38.255  -1.797  38.426  1.00 142.71 ?  456 LYS A CD    1 
ATOM   2260 C CE    . LYS A 1 475 ? 38.801  -1.847  36.977  1.00 157.36 ?  456 LYS A CE    1 
ATOM   2261 N NZ    . LYS A 1 475 ? 39.393  -0.552  36.473  1.00 154.43 ?  456 LYS A NZ    1 
ATOM   2262 N N     . GLU A 1 476 ? 40.064  -5.233  41.443  1.00 122.28 ?  457 GLU A N     1 
ATOM   2263 C CA    . GLU A 1 476 ? 41.323  -5.883  41.105  1.00 118.37 ?  457 GLU A CA    1 
ATOM   2264 C C     . GLU A 1 476 ? 41.371  -7.348  41.553  1.00 121.71 ?  457 GLU A C     1 
ATOM   2265 O O     . GLU A 1 476 ? 41.841  -8.201  40.797  1.00 121.81 ?  457 GLU A O     1 
ATOM   2266 C CB    . GLU A 1 476 ? 42.492  -5.119  41.700  1.00 117.16 ?  457 GLU A CB    1 
ATOM   2267 C CG    . GLU A 1 476 ? 43.797  -5.731  41.281  1.00 125.88 ?  457 GLU A CG    1 
ATOM   2268 C CD    . GLU A 1 476 ? 44.997  -5.025  41.849  1.00 137.19 ?  457 GLU A CD    1 
ATOM   2269 O OE1   . GLU A 1 476 ? 44.870  -4.410  42.932  1.00 141.36 ?  457 GLU A OE1   1 
ATOM   2270 O OE2   . GLU A 1 476 ? 46.056  -5.044  41.179  1.00 141.03 ?  457 GLU A OE2   1 
ATOM   2271 N N     . LEU A 1 477 ? 40.923  -7.678  42.773  1.00 127.42 ?  458 LEU A N     1 
ATOM   2272 C CA    . LEU A 1 477 ? 40.830  -9.097  43.130  1.00 124.33 ?  458 LEU A CA    1 
ATOM   2273 C C     . LEU A 1 477 ? 39.977  -9.867  42.143  1.00 124.08 ?  458 LEU A C     1 
ATOM   2274 O O     . LEU A 1 477 ? 40.232  -11.050 41.904  1.00 126.54 ?  458 LEU A O     1 
ATOM   2275 C CB    . LEU A 1 477 ? 40.253  -9.323  44.527  1.00 119.02 ?  458 LEU A CB    1 
ATOM   2276 C CG    . LEU A 1 477 ? 41.095  -9.211  45.785  1.00 123.48 ?  458 LEU A CG    1 
ATOM   2277 C CD1   . LEU A 1 477 ? 40.324  -9.851  46.930  1.00 117.76 ?  458 LEU A CD1   1 
ATOM   2278 C CD2   . LEU A 1 477 ? 42.438  -9.887  45.586  1.00 120.17 ?  458 LEU A CD2   1 
ATOM   2279 N N     . HIS A 1 478 ? 38.947  -9.232  41.582  1.00 122.48 ?  459 HIS A N     1 
ATOM   2280 C CA    . HIS A 1 478 ? 38.118  -9.923  40.607  1.00 122.06 ?  459 HIS A CA    1 
ATOM   2281 C C     . HIS A 1 478 ? 38.923  -10.259 39.364  1.00 121.74 ?  459 HIS A C     1 
ATOM   2282 O O     . HIS A 1 478 ? 38.764  -11.336 38.775  1.00 120.18 ?  459 HIS A O     1 
ATOM   2283 C CB    . HIS A 1 478 ? 36.911  -9.071  40.244  1.00 124.59 ?  459 HIS A CB    1 
ATOM   2284 C CG    . HIS A 1 478 ? 36.082  -9.656  39.146  1.00 129.35 ?  459 HIS A CG    1 
ATOM   2285 N ND1   . HIS A 1 478 ? 35.082  -10.578 39.380  1.00 132.49 ?  459 HIS A ND1   1 
ATOM   2286 C CD2   . HIS A 1 478 ? 36.115  -9.466  37.805  1.00 126.51 ?  459 HIS A CD2   1 
ATOM   2287 C CE1   . HIS A 1 478 ? 34.525  -10.919 38.231  1.00 132.26 ?  459 HIS A CE1   1 
ATOM   2288 N NE2   . HIS A 1 478 ? 35.132  -10.258 37.261  1.00 131.42 ?  459 HIS A NE2   1 
ATOM   2289 N N     . GLN A 1 479 ? 39.797  -9.342  38.956  1.00 123.52 ?  460 GLN A N     1 
ATOM   2290 C CA    . GLN A 1 479 ? 40.725  -9.607  37.864  1.00 122.08 ?  460 GLN A CA    1 
ATOM   2291 C C     . GLN A 1 479 ? 41.605  -10.810 38.165  1.00 119.20 ?  460 GLN A C     1 
ATOM   2292 O O     . GLN A 1 479 ? 41.650  -11.783 37.402  1.00 121.84 ?  460 GLN A O     1 
ATOM   2293 C CB    . GLN A 1 479 ? 41.586  -8.370  37.607  1.00 121.34 ?  460 GLN A CB    1 
ATOM   2294 C CG    . GLN A 1 479 ? 42.533  -8.601  36.496  1.00 124.31 ?  460 GLN A CG    1 
ATOM   2295 C CD    . GLN A 1 479 ? 41.771  -8.990  35.252  1.00 129.26 ?  460 GLN A CD    1 
ATOM   2296 O OE1   . GLN A 1 479 ? 40.653  -8.517  35.015  1.00 131.31 ?  460 GLN A OE1   1 
ATOM   2297 N NE2   . GLN A 1 479 ? 42.341  -9.896  34.475  1.00 122.64 ?  460 GLN A NE2   1 
ATOM   2298 N N     . GLN A 1 480 ? 42.325  -10.740 39.279  1.00 118.29 ?  461 GLN A N     1 
ATOM   2299 C CA    . GLN A 1 480 ? 43.236  -11.798 39.691  1.00 116.68 ?  461 GLN A CA    1 
ATOM   2300 C C     . GLN A 1 480 ? 42.543  -13.156 39.730  1.00 114.93 ?  461 GLN A C     1 
ATOM   2301 O O     . GLN A 1 480 ? 43.130  -14.174 39.344  1.00 108.94 ?  461 GLN A O     1 
ATOM   2302 C CB    . GLN A 1 480 ? 43.784  -11.411 41.054  1.00 117.07 ?  461 GLN A CB    1 
ATOM   2303 C CG    . GLN A 1 480 ? 44.404  -10.037 41.008  1.00 116.78 ?  461 GLN A CG    1 
ATOM   2304 C CD    . GLN A 1 480 ? 44.869  -9.567  42.355  1.00 126.11 ?  461 GLN A CD    1 
ATOM   2305 O OE1   . GLN A 1 480 ? 44.764  -10.293 43.344  1.00 131.79 ?  461 GLN A OE1   1 
ATOM   2306 N NE2   . GLN A 1 480 ? 45.373  -8.339  42.414  1.00 127.22 ?  461 GLN A NE2   1 
ATOM   2307 N N     . TYR A 1 481 ? 41.292  -13.194 40.194  1.00 117.07 ?  462 TYR A N     1 
ATOM   2308 C CA    . TYR A 1 481 ? 40.565  -14.455 40.213  1.00 111.78 ?  462 TYR A CA    1 
ATOM   2309 C C     . TYR A 1 481 ? 40.343  -14.951 38.799  1.00 117.62 ?  462 TYR A C     1 
ATOM   2310 O O     . TYR A 1 481 ? 40.582  -16.126 38.499  1.00 123.94 ?  462 TYR A O     1 
ATOM   2311 C CB    . TYR A 1 481 ? 39.226  -14.303 40.922  1.00 114.37 ?  462 TYR A CB    1 
ATOM   2312 C CG    . TYR A 1 481 ? 38.310  -15.495 40.735  1.00 117.24 ?  462 TYR A CG    1 
ATOM   2313 C CD1   . TYR A 1 481 ? 37.255  -15.474 39.819  1.00 121.92 ?  462 TYR A CD1   1 
ATOM   2314 C CD2   . TYR A 1 481 ? 38.505  -16.654 41.482  1.00 120.21 ?  462 TYR A CD2   1 
ATOM   2315 C CE1   . TYR A 1 481 ? 36.414  -16.593 39.661  1.00 125.50 ?  462 TYR A CE1   1 
ATOM   2316 C CE2   . TYR A 1 481 ? 37.678  -17.762 41.338  1.00 121.85 ?  462 TYR A CE2   1 
ATOM   2317 C CZ    . TYR A 1 481 ? 36.636  -17.736 40.434  1.00 124.37 ?  462 TYR A CZ    1 
ATOM   2318 O OH    . TYR A 1 481 ? 35.840  -18.865 40.323  1.00 119.96 ?  462 TYR A OH    1 
ATOM   2319 N N     . LYS A 1 482 ? 39.892  -14.061 37.907  1.00 119.26 ?  463 LYS A N     1 
ATOM   2320 C CA    . LYS A 1 482 ? 39.658  -14.474 36.524  1.00 122.78 ?  463 LYS A CA    1 
ATOM   2321 C C     . LYS A 1 482 ? 40.961  -14.934 35.867  1.00 117.25 ?  463 LYS A C     1 
ATOM   2322 O O     . LYS A 1 482 ? 40.951  -15.886 35.077  1.00 116.55 ?  463 LYS A O     1 
ATOM   2323 C CB    . LYS A 1 482 ? 39.021  -13.325 35.727  1.00 121.22 ?  463 LYS A CB    1 
ATOM   2324 C CG    . LYS A 1 482 ? 37.768  -13.701 34.916  1.00 120.71 ?  463 LYS A CG    1 
ATOM   2325 C CD    . LYS A 1 482 ? 36.668  -14.192 35.876  1.00 125.68 ?  463 LYS A CD    1 
ATOM   2326 C CE    . LYS A 1 482 ? 35.337  -14.487 35.190  1.00 130.55 ?  463 LYS A CE    1 
ATOM   2327 N NZ    . LYS A 1 482 ? 34.341  -15.015 36.179  1.00 127.37 ?  463 LYS A NZ    1 
ATOM   2328 N N     . GLU A 1 483 ? 42.094  -14.308 36.230  1.00 111.52 ?  464 GLU A N     1 
ATOM   2329 C CA    . GLU A 1 483 ? 43.379  -14.632 35.617  1.00 104.60 ?  464 GLU A CA    1 
ATOM   2330 C C     . GLU A 1 483 ? 43.884  -15.995 36.054  1.00 114.74 ?  464 GLU A C     1 
ATOM   2331 O O     . GLU A 1 483 ? 44.481  -16.715 35.253  1.00 127.30 ?  464 GLU A O     1 
ATOM   2332 C CB    . GLU A 1 483 ? 44.434  -13.607 35.982  1.00 104.66 ?  464 GLU A CB    1 
ATOM   2333 C CG    . GLU A 1 483 ? 44.195  -12.250 35.420  1.00 117.50 ?  464 GLU A CG    1 
ATOM   2334 C CD    . GLU A 1 483 ? 45.358  -11.304 35.690  1.00 125.82 ?  464 GLU A CD    1 
ATOM   2335 O OE1   . GLU A 1 483 ? 46.309  -11.726 36.389  1.00 128.99 ?  464 GLU A OE1   1 
ATOM   2336 O OE2   . GLU A 1 483 ? 45.290  -10.124 35.264  1.00 124.50 ?  464 GLU A OE2   1 
ATOM   2337 N N     . ALA A 1 484 ? 43.731  -16.345 37.331  1.00 118.02 ?  465 ALA A N     1 
ATOM   2338 C CA    . ALA A 1 484 ? 44.199  -17.658 37.751  1.00 109.36 ?  465 ALA A CA    1 
ATOM   2339 C C     . ALA A 1 484 ? 43.145  -18.728 37.576  1.00 111.73 ?  465 ALA A C     1 
ATOM   2340 O O     . ALA A 1 484 ? 43.462  -19.899 37.765  1.00 119.18 ?  465 ALA A O     1 
ATOM   2341 C CB    . ALA A 1 484 ? 44.671  -17.647 39.198  1.00 107.25 ?  465 ALA A CB    1 
ATOM   2342 N N     . SER A 1 485 ? 41.909  -18.363 37.227  1.00 111.15 ?  466 SER A N     1 
ATOM   2343 C CA    . SER A 1 485 ? 40.981  -19.359 36.702  1.00 118.87 ?  466 SER A CA    1 
ATOM   2344 C C     . SER A 1 485 ? 41.317  -19.758 35.267  1.00 127.08 ?  466 SER A C     1 
ATOM   2345 O O     . SER A 1 485 ? 40.863  -20.818 34.814  1.00 127.35 ?  466 SER A O     1 
ATOM   2346 C CB    . SER A 1 485 ? 39.539  -18.857 36.769  1.00 120.12 ?  466 SER A CB    1 
ATOM   2347 O OG    . SER A 1 485 ? 39.059  -18.873 38.095  1.00 120.59 ?  466 SER A OG    1 
ATOM   2348 N N     . GLU A 1 486 ? 42.091  -18.929 34.547  1.00 126.59 ?  467 GLU A N     1 
ATOM   2349 C CA    . GLU A 1 486 ? 42.567  -19.298 33.211  1.00 124.16 ?  467 GLU A CA    1 
ATOM   2350 C C     . GLU A 1 486 ? 43.408  -20.569 33.244  1.00 124.94 ?  467 GLU A C     1 
ATOM   2351 O O     . GLU A 1 486 ? 43.342  -21.378 32.308  1.00 134.07 ?  467 GLU A O     1 
ATOM   2352 C CB    . GLU A 1 486 ? 43.365  -18.151 32.568  1.00 123.40 ?  467 GLU A CB    1 
ATOM   2353 C CG    . GLU A 1 486 ? 42.529  -16.923 32.222  1.00 125.12 ?  467 GLU A CG    1 
ATOM   2354 C CD    . GLU A 1 486 ? 41.398  -17.236 31.239  1.00 136.55 ?  467 GLU A CD    1 
ATOM   2355 O OE1   . GLU A 1 486 ? 41.626  -18.002 30.261  1.00 136.69 ?  467 GLU A OE1   1 
ATOM   2356 O OE2   . GLU A 1 486 ? 40.264  -16.758 31.483  1.00 137.45 ?  467 GLU A OE2   1 
ATOM   2357 N N     . VAL A 1 487 ? 44.212  -20.765 34.290  1.00 114.58 ?  468 VAL A N     1 
ATOM   2358 C CA    . VAL A 1 487 ? 44.913  -22.041 34.416  1.00 112.56 ?  468 VAL A CA    1 
ATOM   2359 C C     . VAL A 1 487 ? 43.874  -23.140 34.611  1.00 114.53 ?  468 VAL A C     1 
ATOM   2360 O O     . VAL A 1 487 ? 43.131  -23.142 35.593  1.00 116.18 ?  468 VAL A O     1 
ATOM   2361 C CB    . VAL A 1 487 ? 45.945  -22.020 35.543  1.00 99.20  ?  468 VAL A CB    1 
ATOM   2362 C CG1   . VAL A 1 487 ? 46.635  -23.348 35.630  1.00 99.63  ?  468 VAL A CG1   1 
ATOM   2363 C CG2   . VAL A 1 487 ? 46.983  -20.987 35.210  1.00 98.96  ?  468 VAL A CG2   1 
ATOM   2364 N N     . LYS A 1 488 ? 43.801  -24.053 33.649  1.00 117.56 ?  469 LYS A N     1 
ATOM   2365 C CA    . LYS A 1 488 ? 42.777  -25.073 33.528  1.00 118.31 ?  469 LYS A CA    1 
ATOM   2366 C C     . LYS A 1 488 ? 43.113  -26.296 34.367  1.00 117.05 ?  469 LYS A C     1 
ATOM   2367 O O     . LYS A 1 488 ? 44.287  -26.586 34.623  1.00 113.08 ?  469 LYS A O     1 
ATOM   2368 C CB    . LYS A 1 488 ? 42.609  -25.497 32.066  1.00 128.65 ?  469 LYS A CB    1 
ATOM   2369 C CG    . LYS A 1 488 ? 42.170  -24.406 31.061  1.00 132.37 ?  469 LYS A CG    1 
ATOM   2370 C CD    . LYS A 1 488 ? 40.695  -23.998 31.268  1.00 135.46 ?  469 LYS A CD    1 
ATOM   2371 C CE    . LYS A 1 488 ? 40.517  -22.793 32.184  1.00 133.94 ?  469 LYS A CE    1 
ATOM   2372 N NZ    . LYS A 1 488 ? 39.095  -22.357 32.278  1.00 139.53 ?  469 LYS A NZ    1 
ATOM   2373 N N     . PRO A 1 489 ? 42.089  -27.022 34.803  1.00 119.86 ?  470 PRO A N     1 
ATOM   2374 C CA    . PRO A 1 489 ? 42.305  -28.302 35.479  1.00 122.08 ?  470 PRO A CA    1 
ATOM   2375 C C     . PRO A 1 489 ? 42.812  -29.338 34.494  1.00 126.28 ?  470 PRO A C     1 
ATOM   2376 O O     . PRO A 1 489 ? 42.573  -29.215 33.282  1.00 124.94 ?  470 PRO A O     1 
ATOM   2377 C CB    . PRO A 1 489 ? 40.904  -28.674 35.997  1.00 121.36 ?  470 PRO A CB    1 
ATOM   2378 C CG    . PRO A 1 489 ? 40.105  -27.394 35.938  1.00 117.83 ?  470 PRO A CG    1 
ATOM   2379 C CD    . PRO A 1 489 ? 40.666  -26.643 34.772  1.00 120.68 ?  470 PRO A CD    1 
ATOM   2380 N N     . PRO A 1 490 ? 43.547  -30.362 34.968  1.00 125.98 ?  471 PRO A N     1 
ATOM   2381 C CA    . PRO A 1 490 ? 44.011  -30.410 36.354  1.00 122.70 ?  471 PRO A CA    1 
ATOM   2382 C C     . PRO A 1 490 ? 45.215  -29.492 36.537  1.00 124.79 ?  471 PRO A C     1 
ATOM   2383 O O     . PRO A 1 490 ? 46.035  -29.321 35.602  1.00 120.56 ?  471 PRO A O     1 
ATOM   2384 C CB    . PRO A 1 490 ? 44.393  -31.879 36.541  1.00 113.96 ?  471 PRO A CB    1 
ATOM   2385 C CG    . PRO A 1 490 ? 44.915  -32.255 35.218  1.00 114.01 ?  471 PRO A CG    1 
ATOM   2386 C CD    . PRO A 1 490 ? 44.032  -31.528 34.208  1.00 121.13 ?  471 PRO A CD    1 
ATOM   2387 N N     . ARG A 1 491 ? 45.290  -28.885 37.720  1.00 119.59 ?  472 ARG A N     1 
ATOM   2388 C CA    . ARG A 1 491 ? 46.399  -28.030 38.098  1.00 115.88 ?  472 ARG A CA    1 
ATOM   2389 C C     . ARG A 1 491 ? 46.935  -28.533 39.419  1.00 112.58 ?  472 ARG A C     1 
ATOM   2390 O O     . ARG A 1 491 ? 46.248  -29.262 40.140  1.00 115.54 ?  472 ARG A O     1 
ATOM   2391 C CB    . ARG A 1 491 ? 45.959  -26.570 38.195  1.00 115.44 ?  472 ARG A CB    1 
ATOM   2392 C CG    . ARG A 1 491 ? 44.726  -26.379 39.041  1.00 114.63 ?  472 ARG A CG    1 
ATOM   2393 C CD    . ARG A 1 491 ? 44.028  -25.083 38.660  1.00 113.48 ?  472 ARG A CD    1 
ATOM   2394 N NE    . ARG A 1 491 ? 42.669  -25.033 39.199  1.00 117.33 ?  472 ARG A NE    1 
ATOM   2395 C CZ    . ARG A 1 491 ? 41.710  -24.219 38.765  1.00 112.01 ?  472 ARG A CZ    1 
ATOM   2396 N NH1   . ARG A 1 491 ? 41.941  -23.405 37.748  1.00 112.50 ?  472 ARG A NH1   1 
ATOM   2397 N NH2   . ARG A 1 491 ? 40.509  -24.238 39.332  1.00 112.79 ?  472 ARG A NH2   1 
ATOM   2398 N N     . ASP A 1 492 ? 48.178  -28.165 39.725  1.00 112.78 ?  473 ASP A N     1 
ATOM   2399 C CA    . ASP A 1 492 ? 48.719  -28.578 41.008  1.00 113.93 ?  473 ASP A CA    1 
ATOM   2400 C C     . ASP A 1 492 ? 48.034  -27.777 42.107  1.00 115.70 ?  473 ASP A C     1 
ATOM   2401 O O     . ASP A 1 492 ? 47.250  -26.854 41.854  1.00 114.92 ?  473 ASP A O     1 
ATOM   2402 C CB    . ASP A 1 492 ? 50.233  -28.379 41.101  1.00 113.23 ?  473 ASP A CB    1 
ATOM   2403 C CG    . ASP A 1 492 ? 50.670  -26.949 40.840  1.00 110.62 ?  473 ASP A CG    1 
ATOM   2404 O OD1   . ASP A 1 492 ? 49.800  -26.061 40.751  1.00 113.87 ?  473 ASP A OD1   1 
ATOM   2405 O OD2   . ASP A 1 492 ? 51.902  -26.709 40.776  1.00 109.97 ?  473 ASP A OD2   1 
ATOM   2406 N N     . ILE A 1 493 ? 48.376  -28.096 43.354  1.00 119.97 ?  474 ILE A N     1 
ATOM   2407 C CA    . ILE A 1 493 ? 47.634  -27.500 44.451  1.00 115.93 ?  474 ILE A CA    1 
ATOM   2408 C C     . ILE A 1 493 ? 48.013  -26.045 44.727  1.00 113.46 ?  474 ILE A C     1 
ATOM   2409 O O     . ILE A 1 493 ? 47.175  -25.302 45.255  1.00 113.92 ?  474 ILE A O     1 
ATOM   2410 C CB    . ILE A 1 493 ? 47.771  -28.370 45.704  1.00 103.48 ?  474 ILE A CB    1 
ATOM   2411 C CG1   . ILE A 1 493 ? 46.545  -28.130 46.586  1.00 108.67 ?  474 ILE A CG1   1 
ATOM   2412 C CG2   . ILE A 1 493 ? 49.113  -28.107 46.386  1.00 102.19 ?  474 ILE A CG2   1 
ATOM   2413 C CD1   . ILE A 1 493 ? 45.231  -28.444 45.890  1.00 110.23 ?  474 ILE A CD1   1 
ATOM   2414 N N     . THR A 1 494 ? 49.223  -25.590 44.365  1.00 110.40 ?  475 THR A N     1 
ATOM   2415 C CA    . THR A 1 494 ? 49.550  -24.185 44.615  1.00 109.48 ?  475 THR A CA    1 
ATOM   2416 C C     . THR A 1 494 ? 48.658  -23.250 43.794  1.00 110.52 ?  475 THR A C     1 
ATOM   2417 O O     . THR A 1 494 ? 48.243  -22.191 44.279  1.00 114.66 ?  475 THR A O     1 
ATOM   2418 C CB    . THR A 1 494 ? 51.031  -23.891 44.338  1.00 103.27 ?  475 THR A CB    1 
ATOM   2419 O OG1   . THR A 1 494 ? 51.349  -24.251 42.992  1.00 120.54 ?  475 THR A OG1   1 
ATOM   2420 C CG2   . THR A 1 494 ? 51.938  -24.641 45.284  1.00 94.27  ?  475 THR A CG2   1 
ATOM   2421 N N     . ALA A 1 495 ? 48.345  -23.617 42.554  1.00 109.55 ?  476 ALA A N     1 
ATOM   2422 C CA    . ALA A 1 495 ? 47.434  -22.773 41.793  1.00 110.64 ?  476 ALA A CA    1 
ATOM   2423 C C     . ALA A 1 495 ? 45.980  -23.092 42.110  1.00 112.86 ?  476 ALA A C     1 
ATOM   2424 O O     . ALA A 1 495 ? 45.113  -22.224 41.959  1.00 116.25 ?  476 ALA A O     1 
ATOM   2425 C CB    . ALA A 1 495 ? 47.693  -22.904 40.290  1.00 108.73 ?  476 ALA A CB    1 
ATOM   2426 N N     . GLU A 1 496 ? 45.684  -24.319 42.538  1.00 110.34 ?  477 GLU A N     1 
ATOM   2427 C CA    . GLU A 1 496 ? 44.332  -24.594 42.999  1.00 109.50 ?  477 GLU A CA    1 
ATOM   2428 C C     . GLU A 1 496 ? 44.020  -23.794 44.249  1.00 115.86 ?  477 GLU A C     1 
ATOM   2429 O O     . GLU A 1 496 ? 42.878  -23.364 44.444  1.00 119.45 ?  477 GLU A O     1 
ATOM   2430 C CB    . GLU A 1 496 ? 44.149  -26.095 43.227  1.00 112.11 ?  477 GLU A CB    1 
ATOM   2431 C CG    . GLU A 1 496 ? 42.766  -26.511 43.723  1.00 118.31 ?  477 GLU A CG    1 
ATOM   2432 C CD    . GLU A 1 496 ? 41.678  -26.452 42.661  1.00 123.69 ?  477 GLU A CD    1 
ATOM   2433 O OE1   . GLU A 1 496 ? 41.994  -26.223 41.471  1.00 123.36 ?  477 GLU A OE1   1 
ATOM   2434 O OE2   . GLU A 1 496 ? 40.493  -26.658 43.028  1.00 127.15 ?  477 GLU A OE2   1 
ATOM   2435 N N     . PHE A 1 497 ? 45.030  -23.554 45.085  1.00 118.01 ?  478 PHE A N     1 
ATOM   2436 C CA    . PHE A 1 497 ? 44.845  -22.695 46.249  1.00 117.25 ?  478 PHE A CA    1 
ATOM   2437 C C     . PHE A 1 497 ? 44.656  -21.242 45.822  1.00 113.64 ?  478 PHE A C     1 
ATOM   2438 O O     . PHE A 1 497 ? 43.847  -20.521 46.413  1.00 114.47 ?  478 PHE A O     1 
ATOM   2439 C CB    . PHE A 1 497 ? 46.048  -22.864 47.190  1.00 116.11 ?  478 PHE A CB    1 
ATOM   2440 C CG    . PHE A 1 497 ? 46.164  -21.807 48.251  1.00 120.21 ?  478 PHE A CG    1 
ATOM   2441 C CD1   . PHE A 1 497 ? 45.304  -21.811 49.348  1.00 120.80 ?  478 PHE A CD1   1 
ATOM   2442 C CD2   . PHE A 1 497 ? 47.132  -20.814 48.160  1.00 119.22 ?  478 PHE A CD2   1 
ATOM   2443 C CE1   . PHE A 1 497 ? 45.407  -20.845 50.331  1.00 120.34 ?  478 PHE A CE1   1 
ATOM   2444 C CE2   . PHE A 1 497 ? 47.244  -19.838 49.148  1.00 119.65 ?  478 PHE A CE2   1 
ATOM   2445 C CZ    . PHE A 1 497 ? 46.383  -19.853 50.231  1.00 120.07 ?  478 PHE A CZ    1 
ATOM   2446 N N     . LEU A 1 498 ? 45.343  -20.819 44.758  1.00 115.28 ?  479 LEU A N     1 
ATOM   2447 C CA    . LEU A 1 498 ? 45.282  -19.433 44.308  1.00 114.54 ?  479 LEU A CA    1 
ATOM   2448 C C     . LEU A 1 498 ? 43.933  -19.044 43.715  1.00 111.89 ?  479 LEU A C     1 
ATOM   2449 O O     . LEU A 1 498 ? 43.646  -17.850 43.603  1.00 110.42 ?  479 LEU A O     1 
ATOM   2450 C CB    . LEU A 1 498 ? 46.364  -19.156 43.268  1.00 108.27 ?  479 LEU A CB    1 
ATOM   2451 C CG    . LEU A 1 498 ? 46.796  -17.711 43.442  1.00 104.43 ?  479 LEU A CG    1 
ATOM   2452 C CD1   . LEU A 1 498 ? 47.262  -17.540 44.899  1.00 118.21 ?  479 LEU A CD1   1 
ATOM   2453 C CD2   . LEU A 1 498 ? 47.862  -17.310 42.471  1.00 94.41  ?  479 LEU A CD2   1 
ATOM   2454 N N     . VAL A 1 499 ? 43.120  -20.003 43.291  1.00 113.98 ?  480 VAL A N     1 
ATOM   2455 C CA    . VAL A 1 499 ? 41.756  -19.683 42.884  1.00 114.06 ?  480 VAL A CA    1 
ATOM   2456 C C     . VAL A 1 499 ? 40.820  -19.708 44.084  1.00 119.02 ?  480 VAL A C     1 
ATOM   2457 O O     . VAL A 1 499 ? 40.019  -18.787 44.270  1.00 123.27 ?  480 VAL A O     1 
ATOM   2458 C CB    . VAL A 1 499 ? 41.291  -20.648 41.773  1.00 113.16 ?  480 VAL A CB    1 
ATOM   2459 C CG1   . VAL A 1 499 ? 39.833  -20.382 41.387  1.00 110.72 ?  480 VAL A CG1   1 
ATOM   2460 C CG2   . VAL A 1 499 ? 42.190  -20.512 40.573  1.00 112.40 ?  480 VAL A CG2   1 
ATOM   2461 N N     . LYS A 1 500 ? 40.932  -20.756 44.907  1.00 115.70 ?  481 LYS A N     1 
ATOM   2462 C CA    . LYS A 1 500 ? 40.195  -20.816 46.162  1.00 114.90 ?  481 LYS A CA    1 
ATOM   2463 C C     . LYS A 1 500 ? 40.460  -19.568 47.001  1.00 119.24 ?  481 LYS A C     1 
ATOM   2464 O O     . LYS A 1 500 ? 39.528  -18.947 47.534  1.00 118.76 ?  481 LYS A O     1 
ATOM   2465 C CB    . LYS A 1 500 ? 40.608  -22.077 46.921  1.00 115.55 ?  481 LYS A CB    1 
ATOM   2466 C CG    . LYS A 1 500 ? 40.200  -23.380 46.282  1.00 109.58 ?  481 LYS A CG    1 
ATOM   2467 C CD    . LYS A 1 500 ? 38.697  -23.519 46.269  1.00 114.22 ?  481 LYS A CD    1 
ATOM   2468 C CE    . LYS A 1 500 ? 38.310  -24.918 45.862  1.00 119.68 ?  481 LYS A CE    1 
ATOM   2469 N NZ    . LYS A 1 500 ? 38.844  -25.894 46.857  1.00 124.71 ?  481 LYS A NZ    1 
ATOM   2470 N N     . SER A 1 501 ? 41.742  -19.189 47.111  1.00 118.44 ?  482 SER A N     1 
ATOM   2471 C CA    . SER A 1 501 ? 42.172  -18.028 47.889  1.00 116.41 ?  482 SER A CA    1 
ATOM   2472 C C     . SER A 1 501 ? 41.518  -16.748 47.389  1.00 117.19 ?  482 SER A C     1 
ATOM   2473 O O     . SER A 1 501 ? 40.766  -16.094 48.116  1.00 123.18 ?  482 SER A O     1 
ATOM   2474 C CB    . SER A 1 501 ? 43.701  -17.911 47.833  1.00 115.45 ?  482 SER A CB    1 
ATOM   2475 O OG    . SER A 1 501 ? 44.171  -16.668 48.329  1.00 116.79 ?  482 SER A OG    1 
ATOM   2476 N N     . LYS A 1 502 ? 41.815  -16.357 46.153  1.00 112.75 ?  483 LYS A N     1 
ATOM   2477 C CA    . LYS A 1 502 ? 41.215  -15.143 45.624  1.00 112.55 ?  483 LYS A CA    1 
ATOM   2478 C C     . LYS A 1 502 ? 39.693  -15.190 45.679  1.00 116.05 ?  483 LYS A C     1 
ATOM   2479 O O     . LYS A 1 502 ? 39.057  -14.140 45.771  1.00 122.16 ?  483 LYS A O     1 
ATOM   2480 C CB    . LYS A 1 502 ? 41.665  -14.901 44.185  1.00 114.16 ?  483 LYS A CB    1 
ATOM   2481 C CG    . LYS A 1 502 ? 43.156  -14.791 43.974  1.00 107.87 ?  483 LYS A CG    1 
ATOM   2482 C CD    . LYS A 1 502 ? 43.771  -13.617 44.680  1.00 107.36 ?  483 LYS A CD    1 
ATOM   2483 C CE    . LYS A 1 502 ? 45.238  -13.530 44.295  1.00 107.09 ?  483 LYS A CE    1 
ATOM   2484 N NZ    . LYS A 1 502 ? 45.977  -12.388 44.909  1.00 111.10 ?  483 LYS A NZ    1 
ATOM   2485 N N     . HIS A 1 503 ? 39.083  -16.378 45.604  1.00 116.63 ?  484 HIS A N     1 
ATOM   2486 C CA    . HIS A 1 503 ? 37.628  -16.443 45.757  1.00 123.60 ?  484 HIS A CA    1 
ATOM   2487 C C     . HIS A 1 503 ? 37.198  -16.128 47.182  1.00 129.95 ?  484 HIS A C     1 
ATOM   2488 O O     . HIS A 1 503 ? 36.181  -15.453 47.399  1.00 132.05 ?  484 HIS A O     1 
ATOM   2489 C CB    . HIS A 1 503 ? 37.081  -17.806 45.342  1.00 126.63 ?  484 HIS A CB    1 
ATOM   2490 C CG    . HIS A 1 503 ? 35.582  -17.871 45.343  1.00 132.43 ?  484 HIS A CG    1 
ATOM   2491 N ND1   . HIS A 1 503 ? 34.841  -17.829 46.506  1.00 136.50 ?  484 HIS A ND1   1 
ATOM   2492 C CD2   . HIS A 1 503 ? 34.685  -17.927 44.329  1.00 133.83 ?  484 HIS A CD2   1 
ATOM   2493 C CE1   . HIS A 1 503 ? 33.553  -17.886 46.208  1.00 141.03 ?  484 HIS A CE1   1 
ATOM   2494 N NE2   . HIS A 1 503 ? 33.431  -17.940 44.893  1.00 138.34 ?  484 HIS A NE2   1 
ATOM   2495 N N     . ARG A 1 504 ? 37.941  -16.615 48.169  1.00 130.11 ?  485 ARG A N     1 
ATOM   2496 C CA    . ARG A 1 504 ? 37.591  -16.288 49.543  1.00 129.78 ?  485 ARG A CA    1 
ATOM   2497 C C     . ARG A 1 504 ? 37.912  -14.828 49.860  1.00 128.21 ?  485 ARG A C     1 
ATOM   2498 O O     . ARG A 1 504 ? 37.164  -14.167 50.588  1.00 129.95 ?  485 ARG A O     1 
ATOM   2499 C CB    . ARG A 1 504 ? 38.324  -17.222 50.491  1.00 130.42 ?  485 ARG A CB    1 
ATOM   2500 C CG    . ARG A 1 504 ? 37.768  -17.192 51.874  1.00 138.16 ?  485 ARG A CG    1 
ATOM   2501 C CD    . ARG A 1 504 ? 38.886  -17.183 52.875  1.00 139.96 ?  485 ARG A CD    1 
ATOM   2502 N NE    . ARG A 1 504 ? 39.480  -15.858 52.993  1.00 137.09 ?  485 ARG A NE    1 
ATOM   2503 C CZ    . ARG A 1 504 ? 39.012  -14.919 53.810  1.00 136.78 ?  485 ARG A CZ    1 
ATOM   2504 N NH1   . ARG A 1 504 ? 37.951  -15.164 54.584  1.00 134.53 ?  485 ARG A NH1   1 
ATOM   2505 N NH2   . ARG A 1 504 ? 39.608  -13.738 53.858  1.00 136.97 ?  485 ARG A NH2   1 
ATOM   2506 N N     . ASP A 1 505 ? 39.023  -14.310 49.320  1.00 127.36 ?  486 ASP A N     1 
ATOM   2507 C CA    . ASP A 1 505 ? 39.349  -12.894 49.481  1.00 125.39 ?  486 ASP A CA    1 
ATOM   2508 C C     . ASP A 1 505 ? 38.321  -11.996 48.801  1.00 126.31 ?  486 ASP A C     1 
ATOM   2509 O O     . ASP A 1 505 ? 37.999  -10.919 49.313  1.00 130.94 ?  486 ASP A O     1 
ATOM   2510 C CB    . ASP A 1 505 ? 40.750  -12.587 48.933  1.00 121.11 ?  486 ASP A CB    1 
ATOM   2511 C CG    . ASP A 1 505 ? 41.855  -13.287 49.694  1.00 120.87 ?  486 ASP A CG    1 
ATOM   2512 O OD1   . ASP A 1 505 ? 41.541  -14.105 50.592  1.00 125.38 ?  486 ASP A OD1   1 
ATOM   2513 O OD2   . ASP A 1 505 ? 43.042  -12.982 49.409  1.00 112.87 ?  486 ASP A OD2   1 
ATOM   2514 N N     . LEU A 1 506 ? 37.820  -12.398 47.634  1.00 126.51 ?  487 LEU A N     1 
ATOM   2515 C CA    . LEU A 1 506 ? 36.846  -11.563 46.940  1.00 125.43 ?  487 LEU A CA    1 
ATOM   2516 C C     . LEU A 1 506 ? 35.478  -11.638 47.601  1.00 124.62 ?  487 LEU A C     1 
ATOM   2517 O O     . LEU A 1 506 ? 34.725  -10.662 47.555  1.00 125.29 ?  487 LEU A O     1 
ATOM   2518 C CB    . LEU A 1 506 ? 36.726  -11.971 45.468  1.00 127.89 ?  487 LEU A CB    1 
ATOM   2519 C CG    . LEU A 1 506 ? 35.965  -11.040 44.519  1.00 122.92 ?  487 LEU A CG    1 
ATOM   2520 C CD1   . LEU A 1 506 ? 36.851  -9.874  44.159  1.00 124.12 ?  487 LEU A CD1   1 
ATOM   2521 C CD2   . LEU A 1 506 ? 35.440  -11.749 43.277  1.00 122.94 ?  487 LEU A CD2   1 
ATOM   2522 N N     . THR A 1 507 ? 35.132  -12.780 48.203  1.00 121.80 ?  488 THR A N     1 
ATOM   2523 C CA    . THR A 1 507 ? 33.911  -12.849 48.998  1.00 128.15 ?  488 THR A CA    1 
ATOM   2524 C C     . THR A 1 507 ? 34.059  -12.102 50.319  1.00 132.78 ?  488 THR A C     1 
ATOM   2525 O O     . THR A 1 507 ? 33.055  -11.661 50.894  1.00 132.77 ?  488 THR A O     1 
ATOM   2526 C CB    . THR A 1 507 ? 33.530  -14.310 49.248  1.00 129.04 ?  488 THR A CB    1 
ATOM   2527 O OG1   . THR A 1 507 ? 33.346  -14.963 47.990  1.00 127.86 ?  488 THR A OG1   1 
ATOM   2528 C CG2   . THR A 1 507 ? 32.235  -14.429 50.075  1.00 127.10 ?  488 THR A CG2   1 
ATOM   2529 N N     . ALA A 1 508 ? 35.295  -11.926 50.794  1.00 132.49 ?  489 ALA A N     1 
ATOM   2530 C CA    . ALA A 1 508 ? 35.529  -11.171 52.021  1.00 131.39 ?  489 ALA A CA    1 
ATOM   2531 C C     . ALA A 1 508 ? 35.331  -9.668  51.824  1.00 131.22 ?  489 ALA A C     1 
ATOM   2532 O O     . ALA A 1 508 ? 34.865  -8.984  52.745  1.00 132.59 ?  489 ALA A O     1 
ATOM   2533 C CB    . ALA A 1 508 ? 36.936  -11.465 52.545  1.00 131.65 ?  489 ALA A CB    1 
ATOM   2534 N N     . LEU A 1 509 ? 35.680  -9.133  50.650  1.00 128.53 ?  490 LEU A N     1 
ATOM   2535 C CA    . LEU A 1 509 ? 35.499  -7.712  50.396  1.00 124.02 ?  490 LEU A CA    1 
ATOM   2536 C C     . LEU A 1 509 ? 34.144  -7.391  49.788  1.00 126.39 ?  490 LEU A C     1 
ATOM   2537 O O     . LEU A 1 509 ? 33.702  -6.242  49.871  1.00 126.51 ?  490 LEU A O     1 
ATOM   2538 C CB    . LEU A 1 509 ? 36.570  -7.168  49.452  1.00 122.30 ?  490 LEU A CB    1 
ATOM   2539 C CG    . LEU A 1 509 ? 38.045  -7.422  49.760  1.00 122.61 ?  490 LEU A CG    1 
ATOM   2540 C CD1   . LEU A 1 509 ? 38.923  -6.517  48.865  1.00 123.46 ?  490 LEU A CD1   1 
ATOM   2541 C CD2   . LEU A 1 509 ? 38.402  -7.367  51.246  1.00 118.52 ?  490 LEU A CD2   1 
ATOM   2542 N N     . CYS A 1 510 ? 33.491  -8.357  49.139  1.00 132.52 ?  491 CYS A N     1 
ATOM   2543 C CA    . CYS A 1 510 ? 32.089  -8.158  48.793  1.00 137.34 ?  491 CYS A CA    1 
ATOM   2544 C C     . CYS A 1 510 ? 31.200  -8.149  50.022  1.00 137.26 ?  491 CYS A C     1 
ATOM   2545 O O     . CYS A 1 510 ? 30.121  -7.549  49.984  1.00 140.66 ?  491 CYS A O     1 
ATOM   2546 C CB    . CYS A 1 510 ? 31.594  -9.226  47.811  1.00 137.26 ?  491 CYS A CB    1 
ATOM   2547 S SG    . CYS A 1 510 ? 32.430  -9.244  46.227  1.00 134.61 ?  491 CYS A SG    1 
ATOM   2548 N N     . LYS A 1 511 ? 31.630  -8.786  51.109  1.00 133.97 ?  492 LYS A N     1 
ATOM   2549 C CA    . LYS A 1 511 ? 30.839  -8.777  52.331  1.00 136.74 ?  492 LYS A CA    1 
ATOM   2550 C C     . LYS A 1 511 ? 31.037  -7.488  53.126  1.00 139.42 ?  492 LYS A C     1 
ATOM   2551 O O     . LYS A 1 511 ? 30.086  -7.010  53.755  1.00 142.91 ?  492 LYS A O     1 
ATOM   2552 C CB    . LYS A 1 511 ? 31.177  -10.031 53.144  1.00 140.69 ?  492 LYS A CB    1 
ATOM   2553 C CG    . LYS A 1 511 ? 30.097  -10.503 54.118  1.00 143.88 ?  492 LYS A CG    1 
ATOM   2554 C CD    . LYS A 1 511 ? 30.300  -11.999 54.454  1.00 145.50 ?  492 LYS A CD    1 
ATOM   2555 C CE    . LYS A 1 511 ? 30.211  -12.853 53.149  1.00 143.72 ?  492 LYS A CE    1 
ATOM   2556 N NZ    . LYS A 1 511 ? 30.342  -14.346 53.264  1.00 134.91 ?  492 LYS A NZ    1 
ATOM   2557 N N     . GLU A 1 512 ? 32.239  -6.894  53.083  1.00 138.48 ?  493 GLU A N     1 
ATOM   2558 C CA    . GLU A 1 512 ? 32.446  -5.569  53.672  1.00 132.51 ?  493 GLU A CA    1 
ATOM   2559 C C     . GLU A 1 512 ? 31.646  -4.506  52.937  1.00 131.64 ?  493 GLU A C     1 
ATOM   2560 O O     . GLU A 1 512 ? 30.985  -3.676  53.568  1.00 135.63 ?  493 GLU A O     1 
ATOM   2561 C CB    . GLU A 1 512 ? 33.923  -5.186  53.637  1.00 126.83 ?  493 GLU A CB    1 
ATOM   2562 C CG    . GLU A 1 512 ? 34.822  -6.031  54.501  1.00 130.76 ?  493 GLU A CG    1 
ATOM   2563 C CD    . GLU A 1 512 ? 36.228  -5.457  54.589  1.00 135.52 ?  493 GLU A CD    1 
ATOM   2564 O OE1   . GLU A 1 512 ? 36.403  -4.245  54.284  1.00 126.87 ?  493 GLU A OE1   1 
ATOM   2565 O OE2   . GLU A 1 512 ? 37.157  -6.234  54.930  1.00 139.36 ?  493 GLU A OE2   1 
ATOM   2566 N N     . TYR A 1 513 ? 31.711  -4.507  51.602  1.00 133.72 ?  494 TYR A N     1 
ATOM   2567 C CA    . TYR A 1 513 ? 31.042  -3.494  50.789  1.00 134.54 ?  494 TYR A CA    1 
ATOM   2568 C C     . TYR A 1 513 ? 29.522  -3.528  50.934  1.00 137.31 ?  494 TYR A C     1 
ATOM   2569 O O     . TYR A 1 513 ? 28.854  -2.551  50.581  1.00 136.58 ?  494 TYR A O     1 
ATOM   2570 C CB    . TYR A 1 513 ? 31.423  -3.667  49.316  1.00 131.65 ?  494 TYR A CB    1 
ATOM   2571 C CG    . TYR A 1 513 ? 30.875  -2.594  48.406  1.00 128.23 ?  494 TYR A CG    1 
ATOM   2572 C CD1   . TYR A 1 513 ? 31.626  -1.472  48.086  1.00 122.62 ?  494 TYR A CD1   1 
ATOM   2573 C CD2   . TYR A 1 513 ? 29.586  -2.700  47.875  1.00 130.16 ?  494 TYR A CD2   1 
ATOM   2574 C CE1   . TYR A 1 513 ? 31.104  -0.492  47.245  1.00 127.69 ?  494 TYR A CE1   1 
ATOM   2575 C CE2   . TYR A 1 513 ? 29.054  -1.729  47.055  1.00 126.54 ?  494 TYR A CE2   1 
ATOM   2576 C CZ    . TYR A 1 513 ? 29.808  -0.630  46.733  1.00 127.49 ?  494 TYR A CZ    1 
ATOM   2577 O OH    . TYR A 1 513 ? 29.247  0.326   45.903  1.00 127.56 ?  494 TYR A OH    1 
ATOM   2578 N N     . ASP A 1 514 ? 28.949  -4.615  51.437  1.00 138.51 ?  495 ASP A N     1 
ATOM   2579 C CA    . ASP A 1 514 ? 27.508  -4.578  51.639  1.00 139.02 ?  495 ASP A CA    1 
ATOM   2580 C C     . ASP A 1 514 ? 27.147  -4.012  53.004  1.00 139.66 ?  495 ASP A C     1 
ATOM   2581 O O     . ASP A 1 514 ? 26.135  -3.313  53.140  1.00 140.31 ?  495 ASP A O     1 
ATOM   2582 C CB    . ASP A 1 514 ? 26.914  -5.972  51.448  1.00 142.00 ?  495 ASP A CB    1 
ATOM   2583 C CG    . ASP A 1 514 ? 27.220  -6.535  50.076  1.00 145.12 ?  495 ASP A CG    1 
ATOM   2584 O OD1   . ASP A 1 514 ? 27.299  -5.730  49.118  1.00 142.40 ?  495 ASP A OD1   1 
ATOM   2585 O OD2   . ASP A 1 514 ? 27.358  -7.772  49.948  1.00 143.60 ?  495 ASP A OD2   1 
ATOM   2586 N N     . GLU A 1 515 ? 27.977  -4.281  54.013  1.00 139.48 ?  496 GLU A N     1 
ATOM   2587 C CA    . GLU A 1 515 ? 27.791  -3.672  55.320  1.00 140.45 ?  496 GLU A CA    1 
ATOM   2588 C C     . GLU A 1 515 ? 28.140  -2.189  55.314  1.00 139.77 ?  496 GLU A C     1 
ATOM   2589 O O     . GLU A 1 515 ? 27.815  -1.488  56.278  1.00 145.33 ?  496 GLU A O     1 
ATOM   2590 C CB    . GLU A 1 515 ? 28.622  -4.429  56.360  1.00 141.33 ?  496 GLU A CB    1 
ATOM   2591 C CG    . GLU A 1 515 ? 28.219  -5.899  56.467  1.00 148.66 ?  496 GLU A CG    1 
ATOM   2592 C CD    . GLU A 1 515 ? 28.762  -6.600  57.699  1.00 159.01 ?  496 GLU A CD    1 
ATOM   2593 O OE1   . GLU A 1 515 ? 29.086  -5.916  58.698  1.00 170.25 ?  496 GLU A OE1   1 
ATOM   2594 O OE2   . GLU A 1 515 ? 28.859  -7.846  57.661  1.00 153.58 ?  496 GLU A OE2   1 
ATOM   2595 N N     . LEU A 1 516 ? 28.793  -1.698  54.260  1.00 133.89 ?  497 LEU A N     1 
ATOM   2596 C CA    . LEU A 1 516 ? 28.968  -0.271  54.047  1.00 127.12 ?  497 LEU A CA    1 
ATOM   2597 C C     . LEU A 1 516 ? 27.909  0.309   53.116  1.00 132.06 ?  497 LEU A C     1 
ATOM   2598 O O     . LEU A 1 516 ? 27.930  1.513   52.859  1.00 137.50 ?  497 LEU A O     1 
ATOM   2599 C CB    . LEU A 1 516 ? 30.368  0.034   53.488  1.00 122.72 ?  497 LEU A CB    1 
ATOM   2600 C CG    . LEU A 1 516 ? 31.498  0.390   54.469  1.00 118.01 ?  497 LEU A CG    1 
ATOM   2601 C CD1   . LEU A 1 516 ? 31.650  -0.667  55.558  1.00 114.92 ?  497 LEU A CD1   1 
ATOM   2602 C CD2   . LEU A 1 516 ? 32.845  0.710   53.780  1.00 114.80 ?  497 LEU A CD2   1 
ATOM   2603 N N     . ALA A 1 517 ? 26.997  -0.510  52.591  1.00 134.11 ?  498 ALA A N     1 
ATOM   2604 C CA    . ALA A 1 517 ? 25.817  -0.006  51.896  1.00 135.80 ?  498 ALA A CA    1 
ATOM   2605 C C     . ALA A 1 517 ? 24.552  -0.171  52.723  1.00 137.91 ?  498 ALA A C     1 
ATOM   2606 O O     . ALA A 1 517 ? 23.520  0.426   52.392  1.00 137.64 ?  498 ALA A O     1 
ATOM   2607 C CB    . ALA A 1 517 ? 25.646  -0.710  50.547  1.00 140.71 ?  498 ALA A CB    1 
ATOM   2608 N N     . GLU A 1 518 ? 24.614  -1.014  53.753  1.00 138.91 ?  499 GLU A N     1 
ATOM   2609 C CA    . GLU A 1 518 ? 23.711  -0.904  54.889  1.00 142.05 ?  499 GLU A CA    1 
ATOM   2610 C C     . GLU A 1 518 ? 23.930  0.404   55.644  1.00 144.69 ?  499 GLU A C     1 
ATOM   2611 O O     . GLU A 1 518 ? 22.966  1.057   56.059  1.00 148.69 ?  499 GLU A O     1 
ATOM   2612 C CB    . GLU A 1 518 ? 23.929  -2.103  55.813  1.00 148.26 ?  499 GLU A CB    1 
ATOM   2613 C CG    . GLU A 1 518 ? 23.385  -1.965  57.237  1.00 160.28 ?  499 GLU A CG    1 
ATOM   2614 C CD    . GLU A 1 518 ? 21.975  -2.496  57.409  1.00 167.52 ?  499 GLU A CD    1 
ATOM   2615 O OE1   . GLU A 1 518 ? 21.462  -3.147  56.467  1.00 164.21 ?  499 GLU A OE1   1 
ATOM   2616 O OE2   . GLU A 1 518 ? 21.402  -2.289  58.512  1.00 167.82 ?  499 GLU A OE2   1 
ATOM   2617 N N     . THR A 1 519 ? 25.196  0.805   55.826  1.00 142.90 ?  500 THR A N     1 
ATOM   2618 C CA    . THR A 1 519 ? 25.523  1.996   56.615  1.00 139.25 ?  500 THR A CA    1 
ATOM   2619 C C     . THR A 1 519 ? 25.253  3.292   55.854  1.00 139.04 ?  500 THR A C     1 
ATOM   2620 O O     . THR A 1 519 ? 24.804  4.277   56.450  1.00 141.20 ?  500 THR A O     1 
ATOM   2621 C CB    . THR A 1 519 ? 26.979  1.923   57.080  1.00 133.74 ?  500 THR A CB    1 
ATOM   2622 O OG1   . THR A 1 519 ? 27.135  0.810   57.972  1.00 133.49 ?  500 THR A OG1   1 
ATOM   2623 C CG2   . THR A 1 519 ? 27.431  3.216   57.742  1.00 126.91 ?  500 THR A CG2   1 
ATOM   2624 N N     . GLN A 1 520 ? 25.530  3.328   54.546  1.00 137.99 ?  501 GLN A N     1 
ATOM   2625 C CA    . GLN A 1 520 ? 25.008  4.418   53.726  1.00 136.93 ?  501 GLN A CA    1 
ATOM   2626 C C     . GLN A 1 520 ? 23.482  4.421   53.705  1.00 141.55 ?  501 GLN A C     1 
ATOM   2627 O O     . GLN A 1 520 ? 22.871  5.460   53.437  1.00 140.49 ?  501 GLN A O     1 
ATOM   2628 C CB    . GLN A 1 520 ? 25.558  4.329   52.298  1.00 136.10 ?  501 GLN A CB    1 
ATOM   2629 C CG    . GLN A 1 520 ? 24.848  5.240   51.298  1.00 139.96 ?  501 GLN A CG    1 
ATOM   2630 C CD    . GLN A 1 520 ? 25.297  5.023   49.871  1.00 140.81 ?  501 GLN A CD    1 
ATOM   2631 O OE1   . GLN A 1 520 ? 26.036  4.084   49.587  1.00 143.76 ?  501 GLN A OE1   1 
ATOM   2632 N NE2   . GLN A 1 520 ? 24.835  5.882   48.957  1.00 136.83 ?  501 GLN A NE2   1 
ATOM   2633 N N     . GLY A 1 521 ? 22.851  3.282   53.993  1.00 144.29 ?  502 GLY A N     1 
ATOM   2634 C CA    . GLY A 1 521 ? 21.401  3.262   54.094  1.00 144.83 ?  502 GLY A CA    1 
ATOM   2635 C C     . GLY A 1 521 ? 20.894  4.095   55.256  1.00 148.82 ?  502 GLY A C     1 
ATOM   2636 O O     . GLY A 1 521 ? 19.979  4.908   55.099  1.00 151.90 ?  502 GLY A O     1 
ATOM   2637 N N     . LYS A 1 522 ? 21.499  3.916   56.438  1.00 149.25 ?  503 LYS A N     1 
ATOM   2638 C CA    . LYS A 1 522 ? 21.063  4.645   57.629  1.00 148.64 ?  503 LYS A CA    1 
ATOM   2639 C C     . LYS A 1 522 ? 21.402  6.137   57.539  1.00 150.40 ?  503 LYS A C     1 
ATOM   2640 O O     . LYS A 1 522 ? 20.580  6.983   57.912  1.00 152.27 ?  503 LYS A O     1 
ATOM   2641 C CB    . LYS A 1 522 ? 21.682  4.023   58.890  1.00 145.97 ?  503 LYS A CB    1 
ATOM   2642 C CG    . LYS A 1 522 ? 21.355  2.543   59.112  1.00 145.67 ?  503 LYS A CG    1 
ATOM   2643 C CD    . LYS A 1 522 ? 22.042  2.011   60.370  1.00 153.20 ?  503 LYS A CD    1 
ATOM   2644 C CE    . LYS A 1 522 ? 21.701  0.542   60.644  1.00 154.77 ?  503 LYS A CE    1 
ATOM   2645 N NZ    . LYS A 1 522 ? 22.371  0.026   61.881  1.00 153.25 ?  503 LYS A NZ    1 
ATOM   2646 N N     . LEU A 1 523 ? 22.601  6.487   57.047  1.00 146.76 ?  504 LEU A N     1 
ATOM   2647 C CA    . LEU A 1 523 ? 22.996  7.896   57.014  1.00 141.20 ?  504 LEU A CA    1 
ATOM   2648 C C     . LEU A 1 523 ? 22.262  8.668   55.924  1.00 144.14 ?  504 LEU A C     1 
ATOM   2649 O O     . LEU A 1 523 ? 21.920  9.839   56.116  1.00 145.49 ?  504 LEU A O     1 
ATOM   2650 C CB    . LEU A 1 523 ? 24.504  8.045   56.822  1.00 135.84 ?  504 LEU A CB    1 
ATOM   2651 C CG    . LEU A 1 523 ? 25.468  7.471   57.859  1.00 140.26 ?  504 LEU A CG    1 
ATOM   2652 C CD1   . LEU A 1 523 ? 26.883  7.958   57.539  1.00 137.00 ?  504 LEU A CD1   1 
ATOM   2653 C CD2   . LEU A 1 523 ? 25.059  7.806   59.305  1.00 144.83 ?  504 LEU A CD2   1 
ATOM   2654 N N     . GLU A 1 524 ? 22.036  8.047   54.761  1.00 150.92 ?  505 GLU A N     1 
ATOM   2655 C CA    . GLU A 1 524 ? 21.265  8.702   53.705  1.00 153.86 ?  505 GLU A CA    1 
ATOM   2656 C C     . GLU A 1 524 ? 19.835  8.972   54.167  1.00 152.44 ?  505 GLU A C     1 
ATOM   2657 O O     . GLU A 1 524 ? 19.178  9.885   53.650  1.00 150.69 ?  505 GLU A O     1 
ATOM   2658 C CB    . GLU A 1 524 ? 21.296  7.829   52.435  1.00 150.56 ?  505 GLU A CB    1 
ATOM   2659 C CG    . GLU A 1 524 ? 21.224  8.548   51.081  1.00 149.68 ?  505 GLU A CG    1 
ATOM   2660 C CD    . GLU A 1 524 ? 21.453  7.579   49.910  1.00 154.79 ?  505 GLU A CD    1 
ATOM   2661 O OE1   . GLU A 1 524 ? 21.247  6.361   50.107  1.00 156.15 ?  505 GLU A OE1   1 
ATOM   2662 O OE2   . GLU A 1 524 ? 21.847  8.023   48.803  1.00 152.10 ?  505 GLU A OE2   1 
ATOM   2663 N N     . GLU A 1 525 ? 19.361  8.212   55.157  1.00 151.42 ?  506 GLU A N     1 
ATOM   2664 C CA    . GLU A 1 525 ? 18.048  8.343   55.775  1.00 152.99 ?  506 GLU A CA    1 
ATOM   2665 C C     . GLU A 1 525 ? 18.068  9.390   56.890  1.00 156.99 ?  506 GLU A C     1 
ATOM   2666 O O     . GLU A 1 525 ? 17.275  10.338  56.865  1.00 157.59 ?  506 GLU A O     1 
ATOM   2667 C CB    . GLU A 1 525 ? 17.614  6.970   56.310  1.00 159.45 ?  506 GLU A CB    1 
ATOM   2668 C CG    . GLU A 1 525 ? 16.204  6.860   56.903  1.00 167.96 ?  506 GLU A CG    1 
ATOM   2669 C CD    . GLU A 1 525 ? 15.875  5.432   57.397  1.00 175.28 ?  506 GLU A CD    1 
ATOM   2670 O OE1   . GLU A 1 525 ? 16.763  4.547   57.330  1.00 172.54 ?  506 GLU A OE1   1 
ATOM   2671 O OE2   . GLU A 1 525 ? 14.718  5.179   57.814  1.00 176.50 ?  506 GLU A OE2   1 
ATOM   2672 N N     . LYS A 1 526 ? 18.988  9.233   57.861  1.00 156.46 ?  507 LYS A N     1 
ATOM   2673 C CA    . LYS A 1 526 ? 19.214  10.200  58.940  1.00 147.70 ?  507 LYS A CA    1 
ATOM   2674 C C     . LYS A 1 526 ? 19.443  11.626  58.441  1.00 149.00 ?  507 LYS A C     1 
ATOM   2675 O O     . LYS A 1 526 ? 19.279  12.567  59.222  1.00 150.96 ?  507 LYS A O     1 
ATOM   2676 C CB    . LYS A 1 526 ? 20.422  9.761   59.782  1.00 142.39 ?  507 LYS A CB    1 
ATOM   2677 C CG    . LYS A 1 526 ? 20.614  10.482  61.113  1.00 143.15 ?  507 LYS A CG    1 
ATOM   2678 C CD    . LYS A 1 526 ? 21.741  9.833   61.921  1.00 147.40 ?  507 LYS A CD    1 
ATOM   2679 C CE    . LYS A 1 526 ? 21.839  10.406  63.339  1.00 147.64 ?  507 LYS A CE    1 
ATOM   2680 N NZ    . LYS A 1 526 ? 22.870  9.719   64.190  1.00 145.02 ?  507 LYS A NZ    1 
ATOM   2681 N N     . LEU A 1 527 ? 19.835  11.812  57.169  1.00 149.92 ?  508 LEU A N     1 
ATOM   2682 C CA    . LEU A 1 527 ? 20.072  13.132  56.579  1.00 143.61 ?  508 LEU A CA    1 
ATOM   2683 C C     . LEU A 1 527 ? 18.895  13.670  55.774  1.00 144.86 ?  508 LEU A C     1 
ATOM   2684 O O     . LEU A 1 527 ? 18.936  14.830  55.348  1.00 144.43 ?  508 LEU A O     1 
ATOM   2685 C CB    . LEU A 1 527 ? 21.329  13.115  55.694  1.00 136.61 ?  508 LEU A CB    1 
ATOM   2686 C CG    . LEU A 1 527 ? 22.675  13.002  56.407  1.00 134.29 ?  508 LEU A CG    1 
ATOM   2687 C CD1   . LEU A 1 527 ? 23.798  12.929  55.429  1.00 134.64 ?  508 LEU A CD1   1 
ATOM   2688 C CD2   . LEU A 1 527 ? 22.875  14.217  57.257  1.00 136.18 ?  508 LEU A CD2   1 
ATOM   2689 N N     . GLN A 1 528 ? 17.864  12.868  55.536  1.00 149.62 ?  509 GLN A N     1 
ATOM   2690 C CA    . GLN A 1 528 ? 16.577  13.429  55.149  1.00 152.22 ?  509 GLN A CA    1 
ATOM   2691 C C     . GLN A 1 528 ? 15.707  13.688  56.373  1.00 153.22 ?  509 GLN A C     1 
ATOM   2692 O O     . GLN A 1 528 ? 14.835  14.564  56.333  1.00 152.81 ?  509 GLN A O     1 
ATOM   2693 C CB    . GLN A 1 528 ? 15.890  12.504  54.137  1.00 155.00 ?  509 GLN A CB    1 
ATOM   2694 C CG    . GLN A 1 528 ? 16.838  12.123  52.988  1.00 161.62 ?  509 GLN A CG    1 
ATOM   2695 C CD    . GLN A 1 528 ? 16.222  11.215  51.925  1.00 171.76 ?  509 GLN A CD    1 
ATOM   2696 O OE1   . GLN A 1 528 ? 15.002  11.046  51.859  1.00 176.80 ?  509 GLN A OE1   1 
ATOM   2697 N NE2   . GLN A 1 528 ? 17.074  10.647  51.066  1.00 168.47 ?  509 GLN A NE2   1 
ATOM   2698 N N     . GLU A 1 529 ? 15.956  12.942  57.458  1.00 153.30 ?  510 GLU A N     1 
ATOM   2699 C CA    . GLU A 1 529 ? 15.495  13.289  58.803  1.00 151.10 ?  510 GLU A CA    1 
ATOM   2700 C C     . GLU A 1 529 ? 15.765  14.758  59.136  1.00 149.19 ?  510 GLU A C     1 
ATOM   2701 O O     . GLU A 1 529 ? 14.835  15.551  59.323  1.00 147.58 ?  510 GLU A O     1 
ATOM   2702 C CB    . GLU A 1 529 ? 16.196  12.362  59.812  1.00 154.56 ?  510 GLU A CB    1 
ATOM   2703 C CG    . GLU A 1 529 ? 15.935  12.552  61.334  1.00 163.32 ?  510 GLU A CG    1 
ATOM   2704 C CD    . GLU A 1 529 ? 14.525  12.210  61.808  1.00 168.13 ?  510 GLU A CD    1 
ATOM   2705 O OE1   . GLU A 1 529 ? 13.837  11.418  61.118  1.00 164.56 ?  510 GLU A OE1   1 
ATOM   2706 O OE2   . GLU A 1 529 ? 14.133  12.707  62.903  1.00 165.33 ?  510 GLU A OE2   1 
ATOM   2707 N N     . LEU A 1 530 ? 17.044  15.138  59.200  1.00 145.90 ?  511 LEU A N     1 
ATOM   2708 C CA    . LEU A 1 530 ? 17.406  16.434  59.764  1.00 142.66 ?  511 LEU A CA    1 
ATOM   2709 C C     . LEU A 1 530 ? 16.995  17.599  58.868  1.00 146.67 ?  511 LEU A C     1 
ATOM   2710 O O     . LEU A 1 530 ? 16.834  18.723  59.356  1.00 152.82 ?  511 LEU A O     1 
ATOM   2711 C CB    . LEU A 1 530 ? 18.907  16.502  60.023  1.00 138.68 ?  511 LEU A CB    1 
ATOM   2712 C CG    . LEU A 1 530 ? 19.528  15.366  60.828  1.00 140.64 ?  511 LEU A CG    1 
ATOM   2713 C CD1   . LEU A 1 530 ? 20.960  15.749  61.216  1.00 138.25 ?  511 LEU A CD1   1 
ATOM   2714 C CD2   . LEU A 1 530 ? 18.671  14.959  62.028  1.00 140.94 ?  511 LEU A CD2   1 
ATOM   2715 N N     . GLU A 1 531 ? 16.677  17.267  57.622  1.00 144.63 ?  512 GLU A N     1 
ATOM   2716 C CA    . GLU A 1 531 ? 16.257  18.284  56.637  1.00 145.66 ?  512 GLU A CA    1 
ATOM   2717 C C     . GLU A 1 531 ? 14.738  18.380  56.660  1.00 143.75 ?  512 GLU A C     1 
ATOM   2718 O O     . GLU A 1 531 ? 14.214  19.389  56.199  1.00 141.35 ?  512 GLU A O     1 
ATOM   2719 C CB    . GLU A 1 531 ? 16.657  17.835  55.238  1.00 148.16 ?  512 GLU A CB    1 
ATOM   2720 C CG    . GLU A 1 531 ? 17.996  18.371  54.790  1.00 149.22 ?  512 GLU A CG    1 
ATOM   2721 C CD    . GLU A 1 531 ? 18.067  18.614  53.296  1.00 153.47 ?  512 GLU A CD    1 
ATOM   2722 O OE1   . GLU A 1 531 ? 17.047  18.394  52.614  1.00 153.38 ?  512 GLU A OE1   1 
ATOM   2723 O OE2   . GLU A 1 531 ? 19.138  19.025  52.822  1.00 154.23 ?  512 GLU A OE2   1 
ATOM   2724 N N     . ALA A 1 532 ? 14.064  17.329  57.116  1.00 141.29 ?  513 ALA A N     1 
ATOM   2725 C CA    . ALA A 1 532 ? 12.587  17.377  57.134  1.00 139.95 ?  513 ALA A CA    1 
ATOM   2726 C C     . ALA A 1 532 ? 12.100  17.880  58.487  1.00 144.85 ?  513 ALA A C     1 
ATOM   2727 O O     . ALA A 1 532 ? 10.911  18.168  58.610  1.00 143.98 ?  513 ALA A O     1 
ATOM   2728 C CB    . ALA A 1 532 ? 12.028  16.020  56.832  1.00 143.27 ?  513 ALA A CB    1 
ATOM   2729 N N     . ASN A 1 533 ? 13.016  18.022  59.440  1.00 150.80 ?  514 ASN A N     1 
ATOM   2730 C CA    . ASN A 1 533 ? 12.647  18.506  60.791  1.00 151.37 ?  514 ASN A CA    1 
ATOM   2731 C C     . ASN A 1 533 ? 13.579  19.658  61.150  1.00 147.57 ?  514 ASN A C     1 
ATOM   2732 O O     . ASN A 1 533 ? 14.394  19.515  62.063  1.00 145.65 ?  514 ASN A O     1 
ATOM   2733 C CB    . ASN A 1 533 ? 12.818  17.414  61.843  1.00 152.00 ?  514 ASN A CB    1 
ATOM   2734 C CG    . ASN A 1 533 ? 11.609  16.518  61.949  1.00 150.34 ?  514 ASN A CG    1 
ATOM   2735 O OD1   . ASN A 1 533 ? 10.617  16.727  61.261  1.00 147.82 ?  514 ASN A OD1   1 
ATOM   2736 N ND2   . ASN A 1 533 ? 11.687  15.523  62.813  1.00 147.82 ?  514 ASN A ND2   1 
ATOM   2737 N N     . PRO A 1 534 ? 13.481  20.805  60.465  1.00 145.65 ?  515 PRO A N     1 
ATOM   2738 C CA    . PRO A 1 534 ? 14.306  21.945  60.782  1.00 150.30 ?  515 PRO A CA    1 
ATOM   2739 C C     . PRO A 1 534 ? 13.628  22.666  61.949  1.00 156.42 ?  515 PRO A C     1 
ATOM   2740 O O     . PRO A 1 534 ? 12.460  22.488  62.189  1.00 158.64 ?  515 PRO A O     1 
ATOM   2741 C CB    . PRO A 1 534 ? 14.158  22.793  59.527  1.00 143.14 ?  515 PRO A CB    1 
ATOM   2742 C CG    . PRO A 1 534 ? 12.722  22.574  59.157  1.00 142.93 ?  515 PRO A CG    1 
ATOM   2743 C CD    . PRO A 1 534 ? 12.490  21.109  59.446  1.00 143.26 ?  515 PRO A CD    1 
ATOM   2744 N N     . PRO A 1 535 ? 14.335  23.555  62.657  1.00 151.34 ?  516 PRO A N     1 
ATOM   2745 C CA    . PRO A 1 535 ? 13.762  24.269  63.778  1.00 153.30 ?  516 PRO A CA    1 
ATOM   2746 C C     . PRO A 1 535 ? 13.017  25.543  63.353  1.00 156.53 ?  516 PRO A C     1 
ATOM   2747 O O     . PRO A 1 535 ? 12.745  25.731  62.191  1.00 153.57 ?  516 PRO A O     1 
ATOM   2748 C CB    . PRO A 1 535 ? 15.022  24.611  64.567  1.00 152.03 ?  516 PRO A CB    1 
ATOM   2749 C CG    . PRO A 1 535 ? 16.021  24.912  63.499  1.00 145.61 ?  516 PRO A CG    1 
ATOM   2750 C CD    . PRO A 1 535 ? 15.713  23.916  62.406  1.00 148.34 ?  516 PRO A CD    1 
ATOM   2751 N N     . SER A 1 536 ? 12.672  26.385  64.324  1.00 152.67 ?  517 SER A N     1 
ATOM   2752 C CA    . SER A 1 536 ? 11.929  27.620  63.985  1.00 146.59 ?  517 SER A CA    1 
ATOM   2753 C C     . SER A 1 536 ? 12.780  28.443  63.027  1.00 143.31 ?  517 SER A C     1 
ATOM   2754 O O     . SER A 1 536 ? 13.964  28.616  63.290  1.00 139.09 ?  517 SER A O     1 
ATOM   2755 C CB    . SER A 1 536 ? 11.600  28.396  65.222  1.00 152.33 ?  517 SER A CB    1 
ATOM   2756 O OG    . SER A 1 536 ? 10.522  27.801  65.927  1.00 156.41 ?  517 SER A OG    1 
ATOM   2757 N N     . ASP A 1 537 ? 12.162  28.935  61.961  1.00 146.30 ?  518 ASP A N     1 
ATOM   2758 C CA    . ASP A 1 537 ? 12.899  29.717  60.942  1.00 150.60 ?  518 ASP A CA    1 
ATOM   2759 C C     . ASP A 1 537 ? 13.441  31.018  61.538  1.00 148.37 ?  518 ASP A C     1 
ATOM   2760 O O     . ASP A 1 537 ? 14.624  31.278  61.306  1.00 142.14 ?  518 ASP A O     1 
ATOM   2761 C CB    . ASP A 1 537 ? 12.032  29.937  59.704  1.00 155.03 ?  518 ASP A CB    1 
ATOM   2762 C CG    . ASP A 1 537 ? 12.664  30.867  58.687  1.00 161.21 ?  518 ASP A CG    1 
ATOM   2763 O OD1   . ASP A 1 537 ? 13.839  31.229  58.879  1.00 161.80 ?  518 ASP A OD1   1 
ATOM   2764 O OD2   . ASP A 1 537 ? 11.973  31.223  57.713  1.00 162.46 ?  518 ASP A OD2   1 
ATOM   2765 N N     . VAL A 1 538 ? 12.622  31.766  62.276  1.00 150.13 ?  519 VAL A N     1 
ATOM   2766 C CA    . VAL A 1 538 ? 13.070  33.061  62.860  1.00 145.75 ?  519 VAL A CA    1 
ATOM   2767 C C     . VAL A 1 538 ? 12.297  33.311  64.148  1.00 143.61 ?  519 VAL A C     1 
ATOM   2768 O O     . VAL A 1 538 ? 11.265  32.671  64.349  1.00 141.29 ?  519 VAL A O     1 
ATOM   2769 C CB    . VAL A 1 538 ? 12.757  34.193  61.880  1.00 141.09 ?  519 VAL A CB    1 
ATOM   2770 C CG1   . VAL A 1 538 ? 13.859  34.363  60.851  1.00 149.29 ?  519 VAL A CG1   1 
ATOM   2771 C CG2   . VAL A 1 538 ? 11.414  33.948  61.218  1.00 132.96 ?  519 VAL A CG2   1 
ATOM   2772 N N     . TYR A 1 539 ? 12.751  34.261  64.958  1.00 140.26 ?  520 TYR A N     1 
ATOM   2773 C CA    . TYR A 1 539 ? 11.999  34.504  66.207  1.00 136.06 ?  520 TYR A CA    1 
ATOM   2774 C C     . TYR A 1 539 ? 10.670  35.179  65.888  1.00 132.80 ?  520 TYR A C     1 
ATOM   2775 O O     . TYR A 1 539 ? 9.643   34.707  66.363  1.00 127.68 ?  520 TYR A O     1 
ATOM   2776 C CB    . TYR A 1 539 ? 12.770  35.366  67.201  1.00 133.29 ?  520 TYR A CB    1 
ATOM   2777 C CG    . TYR A 1 539 ? 12.048  35.410  68.519  1.00 132.79 ?  520 TYR A CG    1 
ATOM   2778 C CD1   . TYR A 1 539 ? 11.377  34.294  68.970  1.00 133.69 ?  520 TYR A CD1   1 
ATOM   2779 C CD2   . TYR A 1 539 ? 11.974  36.557  69.282  1.00 131.21 ?  520 TYR A CD2   1 
ATOM   2780 C CE1   . TYR A 1 539 ? 10.681  34.302  70.163  1.00 133.60 ?  520 TYR A CE1   1 
ATOM   2781 C CE2   . TYR A 1 539 ? 11.263  36.588  70.469  1.00 127.94 ?  520 TYR A CE2   1 
ATOM   2782 C CZ    . TYR A 1 539 ? 10.630  35.450  70.923  1.00 126.31 ?  520 TYR A CZ    1 
ATOM   2783 O OH    . TYR A 1 539 ? 9.930   35.441  72.090  1.00 114.55 ?  520 TYR A OH    1 
ATOM   2784 N N     . LEU A 1 540 ? 10.694  36.237  65.084  1.00 130.99 ?  521 LEU A N     1 
ATOM   2785 C CA    . LEU A 1 540 ? 9.417   36.938  64.828  1.00 128.28 ?  521 LEU A CA    1 
ATOM   2786 C C     . LEU A 1 540 ? 9.376   37.545  63.432  1.00 125.72 ?  521 LEU A C     1 
ATOM   2787 O O     . LEU A 1 540 ? 10.363  38.146  63.017  1.00 125.06 ?  521 LEU A O     1 
ATOM   2788 C CB    . LEU A 1 540 ? 9.280   38.041  65.873  1.00 131.24 ?  521 LEU A CB    1 
ATOM   2789 C CG    . LEU A 1 540 ? 8.206   37.775  66.916  1.00 130.66 ?  521 LEU A CG    1 
ATOM   2790 C CD1   . LEU A 1 540 ? 7.195   36.795  66.353  1.00 127.84 ?  521 LEU A CD1   1 
ATOM   2791 C CD2   . LEU A 1 540 ? 8.828   37.230  68.186  1.00 123.62 ?  521 LEU A CD2   1 
ATOM   2792 N N     . SER A 1 541 ? 8.231   37.403  62.777  1.00 125.75 ?  522 SER A N     1 
ATOM   2793 C CA    . SER A 1 541 ? 7.997   37.966  61.429  1.00 127.21 ?  522 SER A CA    1 
ATOM   2794 C C     . SER A 1 541 ? 7.679   39.443  61.587  1.00 123.48 ?  522 SER A C     1 
ATOM   2795 O O     . SER A 1 541 ? 7.046   39.742  62.606  1.00 130.30 ?  522 SER A O     1 
ATOM   2796 C CB    . SER A 1 541 ? 6.769   37.336  60.901  1.00 126.46 ?  522 SER A CB    1 
ATOM   2797 O OG    . SER A 1 541 ? 5.682   37.727  61.722  1.00 123.50 ?  522 SER A OG    1 
ATOM   2798 N N     . SER A 1 542 ? 8.099   40.305  60.653  1.00 117.40 ?  523 SER A N     1 
ATOM   2799 C CA    . SER A 1 542 ? 7.638   41.679  60.785  1.00 123.32 ?  523 SER A CA    1 
ATOM   2800 C C     . SER A 1 542 ? 6.122   41.765  60.926  1.00 121.30 ?  523 SER A C     1 
ATOM   2801 O O     . SER A 1 542 ? 5.615   42.790  61.385  1.00 123.55 ?  523 SER A O     1 
ATOM   2802 C CB    . SER A 1 542 ? 8.105   42.522  59.599  1.00 134.34 ?  523 SER A CB    1 
ATOM   2803 O OG    . SER A 1 542 ? 9.517   42.615  59.582  1.00 141.67 ?  523 SER A OG    1 
ATOM   2804 N N     . ARG A 1 543 ? 5.388   40.726  60.528  1.00 122.27 ?  524 ARG A N     1 
ATOM   2805 C CA    . ARG A 1 543 ? 3.955   40.693  60.798  1.00 124.55 ?  524 ARG A CA    1 
ATOM   2806 C C     . ARG A 1 543 ? 3.688   40.437  62.276  1.00 124.91 ?  524 ARG A C     1 
ATOM   2807 O O     . ARG A 1 543 ? 2.729   40.975  62.846  1.00 121.73 ?  524 ARG A O     1 
ATOM   2808 C CB    . ARG A 1 543 ? 3.286   39.619  59.944  1.00 126.41 ?  524 ARG A CB    1 
ATOM   2809 C CG    . ARG A 1 543 ? 1.828   39.870  59.654  1.00 126.72 ?  524 ARG A CG    1 
ATOM   2810 C CD    . ARG A 1 543 ? 1.323   38.864  58.651  1.00 131.70 ?  524 ARG A CD    1 
ATOM   2811 N NE    . ARG A 1 543 ? -0.084  39.071  58.326  1.00 135.78 ?  524 ARG A NE    1 
ATOM   2812 C CZ    . ARG A 1 543 ? -1.068  38.305  58.798  1.00 141.42 ?  524 ARG A CZ    1 
ATOM   2813 N NH1   . ARG A 1 543 ? -0.790  37.299  59.624  1.00 140.28 ?  524 ARG A NH1   1 
ATOM   2814 N NH2   . ARG A 1 543 ? -2.329  38.545  58.458  1.00 141.19 ?  524 ARG A NH2   1 
ATOM   2815 N N     . ASP A 1 544 ? 4.524   39.601  62.904  1.00 129.03 ?  525 ASP A N     1 
ATOM   2816 C CA    . ASP A 1 544 ? 4.429   39.344  64.343  1.00 129.17 ?  525 ASP A CA    1 
ATOM   2817 C C     . ASP A 1 544 ? 4.799   40.589  65.147  1.00 124.19 ?  525 ASP A C     1 
ATOM   2818 O O     . ASP A 1 544 ? 3.981   41.119  65.907  1.00 122.34 ?  525 ASP A O     1 
ATOM   2819 C CB    . ASP A 1 544 ? 5.339   38.165  64.732  1.00 128.13 ?  525 ASP A CB    1 
ATOM   2820 C CG    . ASP A 1 544 ? 5.052   36.894  63.920  1.00 131.16 ?  525 ASP A CG    1 
ATOM   2821 O OD1   . ASP A 1 544 ? 3.869   36.662  63.565  1.00 128.84 ?  525 ASP A OD1   1 
ATOM   2822 O OD2   . ASP A 1 544 ? 6.013   36.133  63.638  1.00 127.45 ?  525 ASP A OD2   1 
ATOM   2823 N N     . ARG A 1 545 ? 6.034   41.079  64.972  1.00 122.88 ?  526 ARG A N     1 
ATOM   2824 C CA    . ARG A 1 545 ? 6.521   42.241  65.711  1.00 114.78 ?  526 ARG A CA    1 
ATOM   2825 C C     . ARG A 1 545 ? 5.619   43.467  65.544  1.00 113.84 ?  526 ARG A C     1 
ATOM   2826 O O     . ARG A 1 545 ? 5.575   44.316  66.438  1.00 120.25 ?  526 ARG A O     1 
ATOM   2827 C CB    . ARG A 1 545 ? 7.956   42.556  65.279  1.00 114.24 ?  526 ARG A CB    1 
ATOM   2828 C CG    . ARG A 1 545 ? 8.551   43.764  65.947  1.00 114.97 ?  526 ARG A CG    1 
ATOM   2829 C CD    . ARG A 1 545 ? 8.790   43.512  67.421  1.00 121.29 ?  526 ARG A CD    1 
ATOM   2830 N NE    . ARG A 1 545 ? 8.863   44.761  68.186  1.00 123.79 ?  526 ARG A NE    1 
ATOM   2831 C CZ    . ARG A 1 545 ? 9.970   45.476  68.378  1.00 128.77 ?  526 ARG A CZ    1 
ATOM   2832 N NH1   . ARG A 1 545 ? 11.126  45.083  67.844  1.00 134.01 ?  526 ARG A NH1   1 
ATOM   2833 N NH2   . ARG A 1 545 ? 9.917   46.592  69.098  1.00 124.70 ?  526 ARG A NH2   1 
ATOM   2834 N N     . GLN A 1 546 ? 4.885   43.581  64.433  1.00 114.03 ?  527 GLN A N     1 
ATOM   2835 C CA    . GLN A 1 546 ? 3.857   44.622  64.331  1.00 116.30 ?  527 GLN A CA    1 
ATOM   2836 C C     . GLN A 1 546 ? 2.728   44.412  65.326  1.00 114.00 ?  527 GLN A C     1 
ATOM   2837 O O     . GLN A 1 546 ? 2.292   45.357  65.993  1.00 118.88 ?  527 GLN A O     1 
ATOM   2838 C CB    . GLN A 1 546 ? 3.251   44.670  62.937  1.00 127.26 ?  527 GLN A CB    1 
ATOM   2839 C CG    . GLN A 1 546 ? 3.977   45.439  61.885  1.00 129.23 ?  527 GLN A CG    1 
ATOM   2840 C CD    . GLN A 1 546 ? 3.164   45.436  60.609  1.00 126.63 ?  527 GLN A CD    1 
ATOM   2841 O OE1   . GLN A 1 546 ? 2.129   44.744  60.510  1.00 119.99 ?  527 GLN A OE1   1 
ATOM   2842 N NE2   . GLN A 1 546 ? 3.563   46.272  59.661  1.00 131.75 ?  527 GLN A NE2   1 
ATOM   2843 N N     . ILE A 1 547 ? 2.177   43.197  65.373  1.00 112.86 ?  528 ILE A N     1 
ATOM   2844 C CA    . ILE A 1 547 ? 1.104   42.896  66.313  1.00 116.84 ?  528 ILE A CA    1 
ATOM   2845 C C     . ILE A 1 547 ? 1.629   42.885  67.749  1.00 116.00 ?  528 ILE A C     1 
ATOM   2846 O O     . ILE A 1 547 ? 0.867   43.104  68.701  1.00 115.09 ?  528 ILE A O     1 
ATOM   2847 C CB    . ILE A 1 547 ? 0.452   41.545  65.949  1.00 125.10 ?  528 ILE A CB    1 
ATOM   2848 C CG1   . ILE A 1 547 ? 0.032   41.520  64.471  1.00 123.62 ?  528 ILE A CG1   1 
ATOM   2849 C CG2   . ILE A 1 547 ? -0.768  41.272  66.847  1.00 123.57 ?  528 ILE A CG2   1 
ATOM   2850 C CD1   . ILE A 1 547 ? -0.580  40.203  64.007  1.00 113.72 ?  528 ILE A CD1   1 
ATOM   2851 N N     . LEU A 1 548 ? 2.925   42.622  67.928  1.00 113.52 ?  529 LEU A N     1 
ATOM   2852 C CA    . LEU A 1 548 ? 3.540   42.766  69.238  1.00 107.86 ?  529 LEU A CA    1 
ATOM   2853 C C     . LEU A 1 548 ? 3.650   44.235  69.638  1.00 111.48 ?  529 LEU A C     1 
ATOM   2854 O O     . LEU A 1 548 ? 3.362   44.596  70.788  1.00 111.52 ?  529 LEU A O     1 
ATOM   2855 C CB    . LEU A 1 548 ? 4.919   42.125  69.229  1.00 103.67 ?  529 LEU A CB    1 
ATOM   2856 C CG    . LEU A 1 548 ? 5.545   42.258  70.599  1.00 105.25 ?  529 LEU A CG    1 
ATOM   2857 C CD1   . LEU A 1 548 ? 4.629   41.589  71.617  1.00 108.20 ?  529 LEU A CD1   1 
ATOM   2858 C CD2   . LEU A 1 548 ? 6.981   41.742  70.627  1.00 102.14 ?  529 LEU A CD2   1 
ATOM   2859 N N     . ASP A 1 549 ? 4.081   45.098  68.708  1.00 108.47 ?  530 ASP A N     1 
ATOM   2860 C CA    . ASP A 1 549 ? 4.142   46.520  69.013  1.00 103.44 ?  530 ASP A CA    1 
ATOM   2861 C C     . ASP A 1 549 ? 2.777   47.083  69.374  1.00 106.17 ?  530 ASP A C     1 
ATOM   2862 O O     . ASP A 1 549 ? 2.714   48.166  69.965  1.00 113.90 ?  530 ASP A O     1 
ATOM   2863 C CB    . ASP A 1 549 ? 4.735   47.334  67.855  1.00 103.95 ?  530 ASP A CB    1 
ATOM   2864 C CG    . ASP A 1 549 ? 6.246   47.227  67.783  1.00 104.47 ?  530 ASP A CG    1 
ATOM   2865 O OD1   . ASP A 1 549 ? 6.858   46.777  68.772  1.00 101.56 ?  530 ASP A OD1   1 
ATOM   2866 O OD2   . ASP A 1 549 ? 6.828   47.663  66.774  1.00 106.28 ?  530 ASP A OD2   1 
ATOM   2867 N N     . TRP A 1 550 ? 1.687   46.382  69.043  1.00 99.32  ?  531 TRP A N     1 
ATOM   2868 C CA    . TRP A 1 550 ? 0.378   46.809  69.522  1.00 98.47  ?  531 TRP A CA    1 
ATOM   2869 C C     . TRP A 1 550 ? 0.150   46.423  70.971  1.00 102.09 ?  531 TRP A C     1 
ATOM   2870 O O     . TRP A 1 550 ? -0.621  47.082  71.677  1.00 102.76 ?  531 TRP A O     1 
ATOM   2871 C CB    . TRP A 1 550 ? -0.719  46.199  68.686  1.00 99.19  ?  531 TRP A CB    1 
ATOM   2872 C CG    . TRP A 1 550 ? -2.105  46.631  69.054  1.00 99.22  ?  531 TRP A CG    1 
ATOM   2873 C CD1   . TRP A 1 550 ? -2.852  47.599  68.434  1.00 102.64 ?  531 TRP A CD1   1 
ATOM   2874 C CD2   . TRP A 1 550 ? -2.922  46.114  70.114  1.00 96.88  ?  531 TRP A CD2   1 
ATOM   2875 N NE1   . TRP A 1 550 ? -4.093  47.693  69.025  1.00 99.95  ?  531 TRP A NE1   1 
ATOM   2876 C CE2   . TRP A 1 550 ? -4.160  46.796  70.060  1.00 96.70  ?  531 TRP A CE2   1 
ATOM   2877 C CE3   . TRP A 1 550 ? -2.733  45.136  71.100  1.00 101.76 ?  531 TRP A CE3   1 
ATOM   2878 C CZ2   . TRP A 1 550 ? -5.198  46.533  70.950  1.00 96.38  ?  531 TRP A CZ2   1 
ATOM   2879 C CZ3   . TRP A 1 550 ? -3.765  44.871  71.983  1.00 104.84 ?  531 TRP A CZ3   1 
ATOM   2880 C CH2   . TRP A 1 550 ? -4.983  45.570  71.902  1.00 102.75 ?  531 TRP A CH2   1 
ATOM   2881 N N     . HIS A 1 551 ? 0.776   45.352  71.434  1.00 106.29 ?  532 HIS A N     1 
ATOM   2882 C CA    . HIS A 1 551 ? 0.665   45.064  72.854  1.00 111.05 ?  532 HIS A CA    1 
ATOM   2883 C C     . HIS A 1 551 ? 1.580   45.960  73.688  1.00 105.79 ?  532 HIS A C     1 
ATOM   2884 O O     . HIS A 1 551 ? 1.343   46.121  74.890  1.00 109.42 ?  532 HIS A O     1 
ATOM   2885 C CB    . HIS A 1 551 ? 0.905   43.564  73.108  1.00 111.15 ?  532 HIS A CB    1 
ATOM   2886 C CG    . HIS A 1 551 ? -0.227  42.700  72.629  1.00 110.10 ?  532 HIS A CG    1 
ATOM   2887 N ND1   . HIS A 1 551 ? -1.393  42.538  73.349  1.00 115.75 ?  532 HIS A ND1   1 
ATOM   2888 C CD2   . HIS A 1 551 ? -0.379  41.966  71.500  1.00 113.58 ?  532 HIS A CD2   1 
ATOM   2889 C CE1   . HIS A 1 551 ? -2.217  41.747  72.682  1.00 115.60 ?  532 HIS A CE1   1 
ATOM   2890 N NE2   . HIS A 1 551 ? -1.625  41.381  71.558  1.00 116.27 ?  532 HIS A NE2   1 
ATOM   2891 N N     . PHE A 1 552 ? 2.572   46.595  73.071  1.00 98.89  ?  533 PHE A N     1 
ATOM   2892 C CA    . PHE A 1 552 ? 3.360   47.580  73.794  1.00 99.20  ?  533 PHE A CA    1 
ATOM   2893 C C     . PHE A 1 552 ? 2.703   48.948  73.772  1.00 102.66 ?  533 PHE A C     1 
ATOM   2894 O O     . PHE A 1 552 ? 2.857   49.719  74.728  1.00 106.23 ?  533 PHE A O     1 
ATOM   2895 C CB    . PHE A 1 552 ? 4.759   47.659  73.206  1.00 102.66 ?  533 PHE A CB    1 
ATOM   2896 C CG    . PHE A 1 552 ? 5.508   46.395  73.325  1.00 101.73 ?  533 PHE A CG    1 
ATOM   2897 C CD1   . PHE A 1 552 ? 5.137   45.460  74.270  1.00 102.43 ?  533 PHE A CD1   1 
ATOM   2898 C CD2   . PHE A 1 552 ? 6.544   46.104  72.459  1.00 106.88 ?  533 PHE A CD2   1 
ATOM   2899 C CE1   . PHE A 1 552 ? 5.814   44.272  74.381  1.00 108.51 ?  533 PHE A CE1   1 
ATOM   2900 C CE2   . PHE A 1 552 ? 7.227   44.913  72.557  1.00 108.80 ?  533 PHE A CE2   1 
ATOM   2901 C CZ    . PHE A 1 552 ? 6.863   43.990  73.520  1.00 107.15 ?  533 PHE A CZ    1 
ATOM   2902 N N     . ALA A 1 553 ? 1.991   49.279  72.695  1.00 101.30 ?  534 ALA A N     1 
ATOM   2903 C CA    . ALA A 1 553 ? 1.131   50.452  72.741  1.00 101.17 ?  534 ALA A CA    1 
ATOM   2904 C C     . ALA A 1 553 ? 0.108   50.315  73.861  1.00 104.65 ?  534 ALA A C     1 
ATOM   2905 O O     . ALA A 1 553 ? -0.144  51.277  74.598  1.00 107.41 ?  534 ALA A O     1 
ATOM   2906 C CB    . ALA A 1 553 ? 0.441   50.667  71.394  1.00 99.87  ?  534 ALA A CB    1 
ATOM   2907 N N     . ASN A 1 554 ? -0.451  49.111  74.041  1.00 100.51 ?  535 ASN A N     1 
ATOM   2908 C CA    . ASN A 1 554 ? -1.424  48.906  75.109  1.00 101.03 ?  535 ASN A CA    1 
ATOM   2909 C C     . ASN A 1 554 ? -0.832  49.209  76.492  1.00 103.95 ?  535 ASN A C     1 
ATOM   2910 O O     . ASN A 1 554 ? -1.480  49.882  77.299  1.00 105.79 ?  535 ASN A O     1 
ATOM   2911 C CB    . ASN A 1 554 ? -1.973  47.489  75.051  1.00 103.68 ?  535 ASN A CB    1 
ATOM   2912 C CG    . ASN A 1 554 ? -3.256  47.327  75.848  1.00 110.40 ?  535 ASN A CG    1 
ATOM   2913 O OD1   . ASN A 1 554 ? -4.047  48.267  76.010  1.00 103.34 ?  535 ASN A OD1   1 
ATOM   2914 N ND2   . ASN A 1 554 ? -3.454  46.122  76.378  1.00 117.50 ?  535 ASN A ND2   1 
ATOM   2915 N N     . LEU A 1 555 ? 0.385   48.728  76.792  1.00 102.46 ?  536 LEU A N     1 
ATOM   2916 C CA    . LEU A 1 555 ? 1.083   49.189  78.000  1.00 98.59  ?  536 LEU A CA    1 
ATOM   2917 C C     . LEU A 1 555 ? 1.242   50.700  78.030  1.00 104.02 ?  536 LEU A C     1 
ATOM   2918 O O     . LEU A 1 555 ? 0.802   51.361  78.978  1.00 109.24 ?  536 LEU A O     1 
ATOM   2919 C CB    . LEU A 1 555 ? 2.455   48.553  78.157  1.00 89.40  ?  536 LEU A CB    1 
ATOM   2920 C CG    . LEU A 1 555 ? 2.396   47.314  79.004  1.00 94.18  ?  536 LEU A CG    1 
ATOM   2921 C CD1   . LEU A 1 555 ? 1.655   46.274  78.273  1.00 107.08 ?  536 LEU A CD1   1 
ATOM   2922 C CD2   . LEU A 1 555 ? 3.812   46.879  79.339  1.00 95.63  ?  536 LEU A CD2   1 
ATOM   2923 N N     . GLU A 1 556 ? 1.926   51.262  77.032  1.00 101.06 ?  537 GLU A N     1 
ATOM   2924 C CA    . GLU A 1 556 ? 2.145   52.707  76.985  1.00 100.29 ?  537 GLU A CA    1 
ATOM   2925 C C     . GLU A 1 556 ? 0.844   53.510  77.116  1.00 99.70  ?  537 GLU A C     1 
ATOM   2926 O O     . GLU A 1 556 ? 0.882   54.683  77.516  1.00 94.52  ?  537 GLU A O     1 
ATOM   2927 C CB    . GLU A 1 556 ? 2.885   53.013  75.689  1.00 101.22 ?  537 GLU A CB    1 
ATOM   2928 C CG    . GLU A 1 556 ? 4.320   52.562  75.769  1.00 99.04  ?  537 GLU A CG    1 
ATOM   2929 C CD    . GLU A 1 556 ? 5.023   52.567  74.431  1.00 104.63 ?  537 GLU A CD    1 
ATOM   2930 O OE1   . GLU A 1 556 ? 4.326   52.694  73.389  1.00 103.38 ?  537 GLU A OE1   1 
ATOM   2931 O OE2   . GLU A 1 556 ? 6.271   52.418  74.425  1.00 104.78 ?  537 GLU A OE2   1 
ATOM   2932 N N     . PHE A 1 557 ? -0.303  52.902  76.789  1.00 99.19  ?  538 PHE A N     1 
ATOM   2933 C CA    . PHE A 1 557 ? -1.595  53.492  77.123  1.00 97.47  ?  538 PHE A CA    1 
ATOM   2934 C C     . PHE A 1 557 ? -1.876  53.475  78.619  1.00 103.63 ?  538 PHE A C     1 
ATOM   2935 O O     . PHE A 1 557 ? -2.340  54.472  79.175  1.00 110.42 ?  538 PHE A O     1 
ATOM   2936 C CB    . PHE A 1 557 ? -2.711  52.772  76.387  1.00 98.58  ?  538 PHE A CB    1 
ATOM   2937 C CG    . PHE A 1 557 ? -4.031  52.931  77.046  1.00 97.53  ?  538 PHE A CG    1 
ATOM   2938 C CD1   . PHE A 1 557 ? -4.621  54.172  77.157  1.00 98.77  ?  538 PHE A CD1   1 
ATOM   2939 C CD2   . PHE A 1 557 ? -4.691  51.829  77.561  1.00 102.00 ?  538 PHE A CD2   1 
ATOM   2940 C CE1   . PHE A 1 557 ? -5.845  54.312  77.795  1.00 104.41 ?  538 PHE A CE1   1 
ATOM   2941 C CE2   . PHE A 1 557 ? -5.922  51.958  78.179  1.00 104.22 ?  538 PHE A CE2   1 
ATOM   2942 C CZ    . PHE A 1 557 ? -6.504  53.199  78.292  1.00 101.60 ?  538 PHE A CZ    1 
ATOM   2943 N N     . ALA A 1 558 ? -1.661  52.339  79.281  1.00 106.56 ?  539 ALA A N     1 
ATOM   2944 C CA    . ALA A 1 558 ? -2.006  52.240  80.700  1.00 107.86 ?  539 ALA A CA    1 
ATOM   2945 C C     . ALA A 1 558 ? -1.117  53.122  81.560  1.00 100.29 ?  539 ALA A C     1 
ATOM   2946 O O     . ALA A 1 558 ? -1.568  53.657  82.577  1.00 108.30 ?  539 ALA A O     1 
ATOM   2947 C CB    . ALA A 1 558 ? -1.902  50.795  81.177  1.00 114.68 ?  539 ALA A CB    1 
ATOM   2948 N N     . ASN A 1 559 ? 0.152   53.246  81.190  1.00 91.07  ?  540 ASN A N     1 
ATOM   2949 C CA    . ASN A 1 559 ? 1.099   54.084  81.899  1.00 90.74  ?  540 ASN A CA    1 
ATOM   2950 C C     . ASN A 1 559 ? 1.244   55.469  81.301  1.00 95.96  ?  540 ASN A C     1 
ATOM   2951 O O     . ASN A 1 559 ? 1.950   56.298  81.882  1.00 99.17  ?  540 ASN A O     1 
ATOM   2952 C CB    . ASN A 1 559 ? 2.462   53.403  81.954  1.00 80.22  ?  540 ASN A CB    1 
ATOM   2953 C CG    . ASN A 1 559 ? 2.346   52.004  82.405  1.00 89.35  ?  540 ASN A CG    1 
ATOM   2954 O OD1   . ASN A 1 559 ? 2.479   51.707  83.583  1.00 99.60  ?  540 ASN A OD1   1 
ATOM   2955 N ND2   . ASN A 1 559 ? 1.978   51.134  81.497  1.00 96.93  ?  540 ASN A ND2   1 
ATOM   2956 N N     . ALA A 1 560 ? 0.592   55.748  80.178  1.00 101.01 ?  541 ALA A N     1 
ATOM   2957 C CA    . ALA A 1 560 ? 0.696   57.053  79.517  1.00 99.78  ?  541 ALA A CA    1 
ATOM   2958 C C     . ALA A 1 560 ? 2.156   57.488  79.343  1.00 95.80  ?  541 ALA A C     1 
ATOM   2959 O O     . ALA A 1 560 ? 2.503   58.654  79.539  1.00 97.94  ?  541 ALA A O     1 
ATOM   2960 C CB    . ALA A 1 560 ? -0.105  58.111  80.284  1.00 90.93  ?  541 ALA A CB    1 
ATOM   2961 N N     . THR A 1 561 ? 2.997   56.547  78.958  1.00 90.43  ?  542 THR A N     1 
ATOM   2962 C CA    . THR A 1 561 ? 4.396   56.910  78.674  1.00 91.32  ?  542 THR A CA    1 
ATOM   2963 C C     . THR A 1 561 ? 5.023   55.811  77.837  1.00 98.84  ?  542 THR A C     1 
ATOM   2964 O O     . THR A 1 561 ? 4.458   54.730  77.737  1.00 95.54  ?  542 THR A O     1 
ATOM   2965 C CB    . THR A 1 561 ? 5.219   57.016  79.949  1.00 89.22  ?  542 THR A CB    1 
ATOM   2966 O OG1   . THR A 1 561 ? 6.601   56.907  79.628  1.00 86.18  ?  542 THR A OG1   1 
ATOM   2967 C CG2   . THR A 1 561 ? 4.818   55.932  80.909  1.00 92.93  ?  542 THR A CG2   1 
ATOM   2968 N N     . PRO A 1 562 ? 6.150   56.108  77.184  1.00 101.02 ?  543 PRO A N     1 
ATOM   2969 C CA    . PRO A 1 562 ? 6.880   55.137  76.413  1.00 97.02  ?  543 PRO A CA    1 
ATOM   2970 C C     . PRO A 1 562 ? 7.539   54.237  77.444  1.00 92.48  ?  543 PRO A C     1 
ATOM   2971 O O     . PRO A 1 562 ? 8.009   54.726  78.408  1.00 94.13  ?  543 PRO A O     1 
ATOM   2972 C CB    . PRO A 1 562 ? 8.019   55.965  75.842  1.00 101.19 ?  543 PRO A CB    1 
ATOM   2973 C CG    . PRO A 1 562 ? 7.457   57.338  75.828  1.00 98.22  ?  543 PRO A CG    1 
ATOM   2974 C CD    . PRO A 1 562 ? 6.767   57.406  77.163  1.00 98.89  ?  543 PRO A CD    1 
ATOM   2975 N N     . LEU A 1 563 ? 7.812   52.995  77.082  1.00 91.33  ?  544 LEU A N     1 
ATOM   2976 C CA    . LEU A 1 563 ? 8.379   52.022  78.043  1.00 91.09  ?  544 LEU A CA    1 
ATOM   2977 C C     . LEU A 1 563 ? 9.875   52.226  78.275  1.00 92.07  ?  544 LEU A C     1 
ATOM   2978 O O     . LEU A 1 563 ? 10.437  51.449  79.019  1.00 94.82  ?  544 LEU A O     1 
ATOM   2979 C CB    . LEU A 1 563 ? 8.055   50.608  77.578  1.00 88.07  ?  544 LEU A CB    1 
ATOM   2980 C CG    . LEU A 1 563 ? 6.663   50.441  76.984  1.00 90.91  ?  544 LEU A CG    1 
ATOM   2981 C CD1   . LEU A 1 563 ? 6.172   49.032  77.175  1.00 94.75  ?  544 LEU A CD1   1 
ATOM   2982 C CD2   . LEU A 1 563 ? 5.676   51.400  77.598  1.00 91.96  ?  544 LEU A CD2   1 
ATOM   2983 N N     . SER A 1 564 ? 10.520  53.137  77.564  1.00 91.72  ?  545 SER A N     1 
ATOM   2984 C CA    . SER A 1 564 ? 11.931  53.487  77.824  1.00 90.89  ?  545 SER A CA    1 
ATOM   2985 C C     . SER A 1 564 ? 12.018  54.104  79.212  1.00 92.54  ?  545 SER A C     1 
ATOM   2986 O O     . SER A 1 564 ? 13.048  53.923  79.835  1.00 87.46  ?  545 SER A O     1 
ATOM   2987 C CB    . SER A 1 564 ? 12.432  54.443  76.801  1.00 94.43  ?  545 SER A CB    1 
ATOM   2988 O OG    . SER A 1 564 ? 11.386  55.240  76.276  1.00 94.50  ?  545 SER A OG    1 
ATOM   2989 N N     . THR A 1 565 ? 11.042  54.950  79.555  1.00 97.62  ?  546 THR A N     1 
ATOM   2990 C CA    . THR A 1 565 ? 10.870  55.640  80.861  1.00 96.14  ?  546 THR A CA    1 
ATOM   2991 C C     . THR A 1 565 ? 10.389  54.759  82.025  1.00 102.28 ?  546 THR A C     1 
ATOM   2992 O O     . THR A 1 565 ? 10.909  54.932  83.123  1.00 110.21 ?  546 THR A O     1 
ATOM   2993 C CB    . THR A 1 565 ? 9.866   56.769  80.711  1.00 92.33  ?  546 THR A CB    1 
ATOM   2994 O OG1   . THR A 1 565 ? 8.662   56.072  80.445  1.00 88.91  ?  546 THR A OG1   1 
ATOM   2995 C CG2   . THR A 1 565 ? 10.178  57.635  79.522  1.00 97.55  ?  546 THR A CG2   1 
ATOM   2996 N N     . LEU A 1 566 ? 9.456   53.829  81.818  1.00 96.43  ?  547 LEU A N     1 
ATOM   2997 C CA    . LEU A 1 566 ? 8.885   53.057  82.958  1.00 92.07  ?  547 LEU A CA    1 
ATOM   2998 C C     . LEU A 1 566 ? 9.977   52.318  83.719  1.00 95.30  ?  547 LEU A C     1 
ATOM   2999 O O     . LEU A 1 566 ? 10.850  51.762  83.088  1.00 95.21  ?  547 LEU A O     1 
ATOM   3000 C CB    . LEU A 1 566 ? 7.856   52.066  82.423  1.00 83.90  ?  547 LEU A CB    1 
ATOM   3001 C CG    . LEU A 1 566 ? 6.497   52.675  82.141  1.00 76.06  ?  547 LEU A CG    1 
ATOM   3002 C CD1   . LEU A 1 566 ? 5.419   51.629  82.152  1.00 79.90  ?  547 LEU A CD1   1 
ATOM   3003 C CD2   . LEU A 1 566 ? 6.189   53.702  83.185  1.00 88.54  ?  547 LEU A CD2   1 
ATOM   3004 N N     . SER A 1 567 ? 9.895   52.294  85.045  1.00 97.41  ?  548 SER A N     1 
ATOM   3005 C CA    . SER A 1 567 ? 10.946  51.608  85.831  1.00 103.27 ?  548 SER A CA    1 
ATOM   3006 C C     . SER A 1 567 ? 10.748  50.104  85.762  1.00 104.48 ?  548 SER A C     1 
ATOM   3007 O O     . SER A 1 567 ? 9.615   49.653  85.907  1.00 102.26 ?  548 SER A O     1 
ATOM   3008 C CB    . SER A 1 567 ? 10.990  52.053  87.237  1.00 102.72 ?  548 SER A CB    1 
ATOM   3009 O OG    . SER A 1 567 ? 11.862  51.202  87.951  1.00 100.78 ?  548 SER A OG    1 
ATOM   3010 N N     . LEU A 1 568 ? 11.845  49.370  85.640  1.00 104.61 ?  549 LEU A N     1 
ATOM   3011 C CA    . LEU A 1 568 ? 11.727  47.923  85.449  1.00 109.20 ?  549 LEU A CA    1 
ATOM   3012 C C     . LEU A 1 568 ? 11.162  47.247  86.690  1.00 116.61 ?  549 LEU A C     1 
ATOM   3013 O O     . LEU A 1 568 ? 10.268  46.391  86.590  1.00 117.79 ?  549 LEU A O     1 
ATOM   3014 C CB    . LEU A 1 568 ? 13.071  47.286  85.081  1.00 113.19 ?  549 LEU A CB    1 
ATOM   3015 C CG    . LEU A 1 568 ? 13.010  45.745  85.114  1.00 110.90 ?  549 LEU A CG    1 
ATOM   3016 C CD1   . LEU A 1 568 ? 11.923  45.187  84.186  1.00 108.48 ?  549 LEU A CD1   1 
ATOM   3017 C CD2   . LEU A 1 568 ? 14.359  45.136  84.779  1.00 111.35 ?  549 LEU A CD2   1 
ATOM   3018 N N     . LYS A 1 569 ? 11.673  47.614  87.876  1.00 113.15 ?  550 LYS A N     1 
ATOM   3019 C CA    . LYS A 1 569 ? 11.238  46.889  89.060  1.00 105.49 ?  550 LYS A CA    1 
ATOM   3020 C C     . LYS A 1 569 ? 9.891   47.387  89.568  1.00 101.94 ?  550 LYS A C     1 
ATOM   3021 O O     . LYS A 1 569 ? 9.049   46.570  89.961  1.00 107.00 ?  550 LYS A O     1 
ATOM   3022 C CB    . LYS A 1 569 ? 12.328  46.918  90.139  1.00 99.31  ?  550 LYS A CB    1 
ATOM   3023 C CG    . LYS A 1 569 ? 12.058  45.844  91.198  1.00 112.09 ?  550 LYS A CG    1 
ATOM   3024 C CD    . LYS A 1 569 ? 12.979  45.817  92.418  1.00 117.55 ?  550 LYS A CD    1 
ATOM   3025 C CE    . LYS A 1 569 ? 14.461  45.696  92.031  1.00 124.62 ?  550 LYS A CE    1 
ATOM   3026 N NZ    . LYS A 1 569 ? 15.420  45.655  93.198  1.00 123.77 ?  550 LYS A NZ    1 
ATOM   3027 N N     . HIS A 1 570 ? 9.619   48.686  89.480  1.00 98.15  ?  551 HIS A N     1 
ATOM   3028 C CA    . HIS A 1 570 ? 8.474   49.253  90.180  1.00 102.92 ?  551 HIS A CA    1 
ATOM   3029 C C     . HIS A 1 570 ? 7.344   49.741  89.289  1.00 101.97 ?  551 HIS A C     1 
ATOM   3030 O O     . HIS A 1 570 ? 6.416   50.367  89.801  1.00 104.32 ?  551 HIS A O     1 
ATOM   3031 C CB    . HIS A 1 570 ? 8.908   50.408  91.085  1.00 103.29 ?  551 HIS A CB    1 
ATOM   3032 C CG    . HIS A 1 570 ? 10.012  50.062  92.036  1.00 104.55 ?  551 HIS A CG    1 
ATOM   3033 N ND1   . HIS A 1 570 ? 11.348  50.091  91.682  1.00 108.85 ?  551 HIS A ND1   1 
ATOM   3034 C CD2   . HIS A 1 570 ? 9.977   49.726  93.347  1.00 89.13  ?  551 HIS A CD2   1 
ATOM   3035 C CE1   . HIS A 1 570 ? 12.087  49.755  92.724  1.00 96.48  ?  551 HIS A CE1   1 
ATOM   3036 N NE2   . HIS A 1 570 ? 11.279  49.530  93.745  1.00 92.92  ?  551 HIS A NE2   1 
ATOM   3037 N N     . TRP A 1 571 ? 7.366   49.483  87.987  1.00 101.84 ?  552 TRP A N     1 
ATOM   3038 C CA    . TRP A 1 571 ? 6.312   50.076  87.163  1.00 105.17 ?  552 TRP A CA    1 
ATOM   3039 C C     . TRP A 1 571 ? 4.932   49.521  87.542  1.00 103.39 ?  552 TRP A C     1 
ATOM   3040 O O     . TRP A 1 571 ? 3.920   50.241  87.515  1.00 101.87 ?  552 TRP A O     1 
ATOM   3041 C CB    . TRP A 1 571 ? 6.619   49.857  85.675  1.00 106.37 ?  552 TRP A CB    1 
ATOM   3042 C CG    . TRP A 1 571 ? 6.296   48.468  85.169  1.00 103.25 ?  552 TRP A CG    1 
ATOM   3043 C CD1   . TRP A 1 571 ? 7.140   47.401  85.108  1.00 96.27  ?  552 TRP A CD1   1 
ATOM   3044 C CD2   . TRP A 1 571 ? 5.028   48.016  84.652  1.00 100.88 ?  552 TRP A CD2   1 
ATOM   3045 N NE1   . TRP A 1 571 ? 6.471   46.312  84.604  1.00 99.34  ?  552 TRP A NE1   1 
ATOM   3046 C CE2   . TRP A 1 571 ? 5.176   46.664  84.316  1.00 98.72  ?  552 TRP A CE2   1 
ATOM   3047 C CE3   . TRP A 1 571 ? 3.780   48.627  84.459  1.00 103.50 ?  552 TRP A CE3   1 
ATOM   3048 C CZ2   . TRP A 1 571 ? 4.128   45.908  83.793  1.00 103.38 ?  552 TRP A CZ2   1 
ATOM   3049 C CZ3   . TRP A 1 571 ? 2.743   47.876  83.941  1.00 103.29 ?  552 TRP A CZ3   1 
ATOM   3050 C CH2   . TRP A 1 571 ? 2.924   46.533  83.611  1.00 103.94 ?  552 TRP A CH2   1 
ATOM   3051 N N     . ASP A 1 572 ? 4.876   48.245  87.904  1.00 100.78 ?  553 ASP A N     1 
ATOM   3052 C CA    . ASP A 1 572 ? 3.628   47.575  88.212  1.00 104.97 ?  553 ASP A CA    1 
ATOM   3053 C C     . ASP A 1 572 ? 3.450   47.390  89.705  1.00 115.04 ?  553 ASP A C     1 
ATOM   3054 O O     . ASP A 1 572 ? 2.730   46.478  90.126  1.00 122.65 ?  553 ASP A O     1 
ATOM   3055 C CB    . ASP A 1 572 ? 3.559   46.214  87.503  1.00 113.26 ?  553 ASP A CB    1 
ATOM   3056 C CG    . ASP A 1 572 ? 4.557   45.157  88.087  1.00 118.74 ?  553 ASP A CG    1 
ATOM   3057 O OD1   . ASP A 1 572 ? 5.677   45.528  88.536  1.00 117.64 ?  553 ASP A OD1   1 
ATOM   3058 O OD2   . ASP A 1 572 ? 4.216   43.942  88.097  1.00 119.43 ?  553 ASP A OD2   1 
ATOM   3059 N N     . GLN A 1 573 ? 4.217   48.132  90.487  1.00 110.96 ?  554 GLN A N     1 
ATOM   3060 C CA    . GLN A 1 573 ? 4.201   47.927  91.951  1.00 103.36 ?  554 GLN A CA    1 
ATOM   3061 C C     . GLN A 1 573 ? 2.792   48.060  92.516  1.00 99.68  ?  554 GLN A C     1 
ATOM   3062 O O     . GLN A 1 573 ? 2.573   47.607  93.618  1.00 101.65 ?  554 GLN A O     1 
ATOM   3063 C CB    . GLN A 1 573 ? 5.084   48.975  92.603  1.00 97.83  ?  554 GLN A CB    1 
ATOM   3064 C CG    . GLN A 1 573 ? 4.634   50.371  92.252  1.00 106.38 ?  554 GLN A CG    1 
ATOM   3065 C CD    . GLN A 1 573 ? 3.882   50.992  93.394  1.00 106.51 ?  554 GLN A CD    1 
ATOM   3066 O OE1   . GLN A 1 573 ? 4.380   51.075  94.504  1.00 107.45 ?  554 GLN A OE1   1 
ATOM   3067 N NE2   . GLN A 1 573 ? 2.673   51.437  93.122  1.00 104.80 ?  554 GLN A NE2   1 
ATOM   3068 N N     . ASP A 1 574 ? 1.855   48.620  91.781  1.00 100.47 ?  555 ASP A N     1 
ATOM   3069 C CA    . ASP A 1 574 ? 0.534   48.792  92.420  1.00 101.38 ?  555 ASP A CA    1 
ATOM   3070 C C     . ASP A 1 574 ? -0.414  47.690  91.986  1.00 104.03 ?  555 ASP A C     1 
ATOM   3071 O O     . ASP A 1 574 ? -1.598  47.816  92.247  1.00 98.66  ?  555 ASP A O     1 
ATOM   3072 C CB    . ASP A 1 574 ? -0.082  50.117  92.022  1.00 108.42 ?  555 ASP A CB    1 
ATOM   3073 C CG    . ASP A 1 574 ? -0.810  50.026  90.709  1.00 118.12 ?  555 ASP A CG    1 
ATOM   3074 O OD1   . ASP A 1 574 ? -0.149  50.183  89.690  1.00 123.14 ?  555 ASP A OD1   1 
ATOM   3075 O OD2   . ASP A 1 574 ? -2.025  49.813  90.728  1.00 116.60 ?  555 ASP A OD2   1 
ATOM   3076 N N     . ASP A 1 575 ? 0.107   46.626  91.395  1.00 114.17 ?  556 ASP A N     1 
ATOM   3077 C CA    . ASP A 1 575 ? -0.766  45.553  90.853  1.00 121.73 ?  556 ASP A CA    1 
ATOM   3078 C C     . ASP A 1 575 ? -1.628  44.918  91.946  1.00 118.10 ?  556 ASP A C     1 
ATOM   3079 O O     . ASP A 1 575 ? -2.811  44.704  91.697  1.00 116.48 ?  556 ASP A O     1 
ATOM   3080 C CB    . ASP A 1 575 ? 0.041   44.521  90.066  1.00 118.56 ?  556 ASP A CB    1 
ATOM   3081 C CG    . ASP A 1 575 ? 0.327   44.955  88.642  1.00 125.21 ?  556 ASP A CG    1 
ATOM   3082 O OD1   . ASP A 1 575 ? 0.273   46.160  88.384  1.00 121.25 ?  556 ASP A OD1   1 
ATOM   3083 O OD2   . ASP A 1 575 ? 0.619   44.090  87.812  1.00 127.11 ?  556 ASP A OD2   1 
ATOM   3084 N N     . ASP A 1 576 ? -1.109  44.747  93.157  1.00 114.69 ?  557 ASP A N     1 
ATOM   3085 C CA    . ASP A 1 576 ? -1.849  44.010  94.212  1.00 112.58 ?  557 ASP A CA    1 
ATOM   3086 C C     . ASP A 1 576 ? -3.197  44.628  94.570  1.00 110.94 ?  557 ASP A C     1 
ATOM   3087 O O     . ASP A 1 576 ? -4.076  43.872  94.954  1.00 112.40 ?  557 ASP A O     1 
ATOM   3088 C CB    . ASP A 1 576 ? -0.998  43.823  95.458  1.00 114.37 ?  557 ASP A CB    1 
ATOM   3089 C CG    . ASP A 1 576 ? 0.419   43.480  95.085  1.00 123.57 ?  557 ASP A CG    1 
ATOM   3090 O OD1   . ASP A 1 576 ? 0.738   43.623  93.911  1.00 135.96 ?  557 ASP A OD1   1 
ATOM   3091 O OD2   . ASP A 1 576 ? 1.174   43.070  95.968  1.00 125.10 ?  557 ASP A OD2   1 
ATOM   3092 N N     . PHE A 1 577 ? -3.375  45.934  94.450  1.00 107.41 ?  558 PHE A N     1 
ATOM   3093 C CA    . PHE A 1 577 ? -4.657  46.527  94.885  1.00 108.86 ?  558 PHE A CA    1 
ATOM   3094 C C     . PHE A 1 577 ? -5.651  46.638  93.740  1.00 107.30 ?  558 PHE A C     1 
ATOM   3095 O O     . PHE A 1 577 ? -6.605  47.362  93.876  1.00 110.33 ?  558 PHE A O     1 
ATOM   3096 C CB    . PHE A 1 577 ? -4.405  47.865  95.560  1.00 108.95 ?  558 PHE A CB    1 
ATOM   3097 C CG    . PHE A 1 577 ? -3.296  47.802  96.568  1.00 106.61 ?  558 PHE A CG    1 
ATOM   3098 C CD1   . PHE A 1 577 ? -3.544  47.397  97.858  1.00 98.89  ?  558 PHE A CD1   1 
ATOM   3099 C CD2   . PHE A 1 577 ? -2.003  48.127  96.218  1.00 109.60 ?  558 PHE A CD2   1 
ATOM   3100 C CE1   . PHE A 1 577 ? -2.517  47.340  98.779  1.00 105.88 ?  558 PHE A CE1   1 
ATOM   3101 C CE2   . PHE A 1 577 ? -0.977  48.075  97.141  1.00 101.45 ?  558 PHE A CE2   1 
ATOM   3102 C CZ    . PHE A 1 577 ? -1.238  47.678  98.421  1.00 100.34 ?  558 PHE A CZ    1 
ATOM   3103 N N     . GLU A 1 578 ? -5.451  45.914  92.652  1.00 105.54 ?  559 GLU A N     1 
ATOM   3104 C CA    . GLU A 1 578 ? -6.418  45.997  91.537  1.00 111.38 ?  559 GLU A CA    1 
ATOM   3105 C C     . GLU A 1 578 ? -7.796  45.566  92.034  1.00 104.58 ?  559 GLU A C     1 
ATOM   3106 O O     . GLU A 1 578 ? -7.884  44.581  92.744  1.00 106.71 ?  559 GLU A O     1 
ATOM   3107 C CB    . GLU A 1 578 ? -5.933  45.074  90.420  1.00 122.65 ?  559 GLU A CB    1 
ATOM   3108 C CG    . GLU A 1 578 ? -7.042  44.496  89.561  1.00 135.54 ?  559 GLU A CG    1 
ATOM   3109 C CD    . GLU A 1 578 ? -6.644  43.480  88.502  1.00 142.24 ?  559 GLU A CD    1 
ATOM   3110 O OE1   . GLU A 1 578 ? -6.432  42.312  88.854  1.00 135.06 ?  559 GLU A OE1   1 
ATOM   3111 O OE2   . GLU A 1 578 ? -6.556  43.852  87.321  1.00 141.90 ?  559 GLU A OE2   1 
ATOM   3112 N N     . PHE A 1 579 ? -8.854  46.243  91.600  1.00 100.80 ?  560 PHE A N     1 
ATOM   3113 C CA    . PHE A 1 579 ? -10.226 45.882  92.035  1.00 104.47 ?  560 PHE A CA    1 
ATOM   3114 C C     . PHE A 1 579 ? -10.761 44.660  91.284  1.00 111.57 ?  560 PHE A C     1 
ATOM   3115 O O     . PHE A 1 579 ? -10.119 44.112  90.406  1.00 115.11 ?  560 PHE A O     1 
ATOM   3116 C CB    . PHE A 1 579 ? -11.184 47.044  91.791  1.00 103.84 ?  560 PHE A CB    1 
ATOM   3117 C CG    . PHE A 1 579 ? -10.871 48.291  92.570  1.00 107.55 ?  560 PHE A CG    1 
ATOM   3118 C CD1   . PHE A 1 579 ? -11.051 48.336  93.934  1.00 109.52 ?  560 PHE A CD1   1 
ATOM   3119 C CD2   . PHE A 1 579 ? -10.413 49.425  91.937  1.00 105.41 ?  560 PHE A CD2   1 
ATOM   3120 C CE1   . PHE A 1 579 ? -10.759 49.482  94.648  1.00 105.76 ?  560 PHE A CE1   1 
ATOM   3121 C CE2   . PHE A 1 579 ? -10.116 50.568  92.653  1.00 95.15  ?  560 PHE A CE2   1 
ATOM   3122 C CZ    . PHE A 1 579 ? -10.302 50.596  94.003  1.00 99.99  ?  560 PHE A CZ    1 
ATOM   3123 N N     . THR A 1 580 ? -11.978 44.249  91.605  1.00 106.72 ?  561 THR A N     1 
ATOM   3124 C CA    . THR A 1 580 ? -12.529 43.065  90.921  1.00 105.87 ?  561 THR A CA    1 
ATOM   3125 C C     . THR A 1 580 ? -13.759 43.452  90.119  1.00 112.67 ?  561 THR A C     1 
ATOM   3126 O O     . THR A 1 580 ? -14.334 44.485  90.427  1.00 114.89 ?  561 THR A O     1 
ATOM   3127 C CB    . THR A 1 580 ? -12.936 42.012  91.944  1.00 103.49 ?  561 THR A CB    1 
ATOM   3128 O OG1   . THR A 1 580 ? -14.208 42.379  92.469  1.00 100.91 ?  561 THR A OG1   1 
ATOM   3129 C CG2   . THR A 1 580 ? -11.934 41.922  93.066  1.00 97.59  ?  561 THR A CG2   1 
ATOM   3130 N N     . GLY A 1 581 ? -14.095 42.637  89.121  1.00 113.90 ?  562 GLY A N     1 
ATOM   3131 C CA    . GLY A 1 581 ? -15.304 42.816  88.301  1.00 112.19 ?  562 GLY A CA    1 
ATOM   3132 C C     . GLY A 1 581 ? -14.996 43.376  86.934  1.00 111.18 ?  562 GLY A C     1 
ATOM   3133 O O     . GLY A 1 581 ? -13.820 43.533  86.609  1.00 105.42 ?  562 GLY A O     1 
ATOM   3134 N N     . SER A 1 582 ? -16.042 43.732  86.185  1.00 113.62 ?  563 SER A N     1 
ATOM   3135 C CA    . SER A 1 582 ? -15.897 44.342  84.872  1.00 119.18 ?  563 SER A CA    1 
ATOM   3136 C C     . SER A 1 582 ? -15.341 45.748  85.021  1.00 117.93 ?  563 SER A C     1 
ATOM   3137 O O     . SER A 1 582 ? -15.479 46.387  86.066  1.00 124.38 ?  563 SER A O     1 
ATOM   3138 C CB    . SER A 1 582 ? -17.244 44.409  84.140  1.00 117.98 ?  563 SER A CB    1 
ATOM   3139 O OG    . SER A 1 582 ? -17.916 43.162  84.186  1.00 124.44 ?  563 SER A OG    1 
ATOM   3140 N N     . HIS A 1 583 ? -14.691 46.222  83.976  1.00 112.51 ?  564 HIS A N     1 
ATOM   3141 C CA    . HIS A 1 583 ? -14.503 47.649  83.846  1.00 105.97 ?  564 HIS A CA    1 
ATOM   3142 C C     . HIS A 1 583 ? -15.812 48.215  83.314  1.00 109.69 ?  564 HIS A C     1 
ATOM   3143 O O     . HIS A 1 583 ? -16.600 47.506  82.677  1.00 114.99 ?  564 HIS A O     1 
ATOM   3144 C CB    . HIS A 1 583 ? -13.310 47.907  82.937  1.00 103.82 ?  564 HIS A CB    1 
ATOM   3145 C CG    . HIS A 1 583 ? -12.023 47.479  83.558  1.00 106.65 ?  564 HIS A CG    1 
ATOM   3146 N ND1   . HIS A 1 583 ? -11.107 48.364  84.071  1.00 110.12 ?  564 HIS A ND1   1 
ATOM   3147 C CD2   . HIS A 1 583 ? -11.573 46.245  83.892  1.00 119.53 ?  564 HIS A CD2   1 
ATOM   3148 C CE1   . HIS A 1 583 ? -10.102 47.697  84.615  1.00 114.15 ?  564 HIS A CE1   1 
ATOM   3149 N NE2   . HIS A 1 583 ? -10.366 46.407  84.530  1.00 119.43 ?  564 HIS A NE2   1 
ATOM   3150 N N     . LEU A 1 584 ? -16.098 49.461  83.658  1.00 108.87 ?  565 LEU A N     1 
ATOM   3151 C CA    . LEU A 1 584 ? -17.370 50.039  83.261  1.00 110.57 ?  565 LEU A CA    1 
ATOM   3152 C C     . LEU A 1 584 ? -17.128 51.375  82.578  1.00 111.84 ?  565 LEU A C     1 
ATOM   3153 O O     . LEU A 1 584 ? -16.019 51.918  82.574  1.00 110.83 ?  565 LEU A O     1 
ATOM   3154 C CB    . LEU A 1 584 ? -18.311 50.237  84.455  1.00 110.64 ?  565 LEU A CB    1 
ATOM   3155 C CG    . LEU A 1 584 ? -18.884 48.967  85.080  1.00 115.80 ?  565 LEU A CG    1 
ATOM   3156 C CD1   . LEU A 1 584 ? -17.858 48.340  86.020  1.00 113.42 ?  565 LEU A CD1   1 
ATOM   3157 C CD2   . LEU A 1 584 ? -20.206 49.201  85.796  1.00 117.33 ?  565 LEU A CD2   1 
ATOM   3158 N N     . THR A 1 585 ? -18.182 51.916  81.995  1.00 110.86 ?  566 THR A N     1 
ATOM   3159 C CA    . THR A 1 585 ? -18.117 53.263  81.473  1.00 115.49 ?  566 THR A CA    1 
ATOM   3160 C C     . THR A 1 585 ? -19.333 54.034  81.929  1.00 119.84 ?  566 THR A C     1 
ATOM   3161 O O     . THR A 1 585 ? -20.366 53.454  82.289  1.00 117.03 ?  566 THR A O     1 
ATOM   3162 C CB    . THR A 1 585 ? -18.037 53.301  79.951  1.00 121.98 ?  566 THR A CB    1 
ATOM   3163 O OG1   . THR A 1 585 ? -19.171 52.625  79.385  1.00 123.97 ?  566 THR A OG1   1 
ATOM   3164 C CG2   . THR A 1 585 ? -16.751 52.680  79.490  1.00 117.35 ?  566 THR A CG2   1 
ATOM   3165 N N     . VAL A 1 586 ? -19.181 55.355  81.899  1.00 120.28 ?  567 VAL A N     1 
ATOM   3166 C CA    . VAL A 1 586 ? -20.248 56.281  82.239  1.00 122.40 ?  567 VAL A CA    1 
ATOM   3167 C C     . VAL A 1 586 ? -20.827 56.785  80.941  1.00 128.84 ?  567 VAL A C     1 
ATOM   3168 O O     . VAL A 1 586 ? -20.186 57.573  80.236  1.00 131.27 ?  567 VAL A O     1 
ATOM   3169 C CB    . VAL A 1 586 ? -19.743 57.447  83.077  1.00 120.30 ?  567 VAL A CB    1 
ATOM   3170 C CG1   . VAL A 1 586 ? -20.899 58.367  83.381  1.00 125.63 ?  567 VAL A CG1   1 
ATOM   3171 C CG2   . VAL A 1 586 ? -19.111 56.915  84.305  1.00 122.89 ?  567 VAL A CG2   1 
ATOM   3172 N N     . ARG A 1 587 ? -22.031 56.331  80.619  1.00 132.94 ?  568 ARG A N     1 
ATOM   3173 C CA    . ARG A 1 587 ? -22.592 56.681  79.327  1.00 137.75 ?  568 ARG A CA    1 
ATOM   3174 C C     . ARG A 1 587 ? -23.162 58.089  79.310  1.00 137.94 ?  568 ARG A C     1 
ATOM   3175 O O     . ARG A 1 587 ? -23.243 58.692  78.227  1.00 140.11 ?  568 ARG A O     1 
ATOM   3176 C CB    . ARG A 1 587 ? -23.657 55.666  78.911  1.00 143.35 ?  568 ARG A CB    1 
ATOM   3177 C CG    . ARG A 1 587 ? -23.133 54.255  78.738  1.00 141.34 ?  568 ARG A CG    1 
ATOM   3178 C CD    . ARG A 1 587 ? -24.252 53.362  78.268  1.00 148.03 ?  568 ARG A CD    1 
ATOM   3179 N NE    . ARG A 1 587 ? -24.584 53.554  76.862  1.00 142.24 ?  568 ARG A NE    1 
ATOM   3180 C CZ    . ARG A 1 587 ? -25.668 53.042  76.297  1.00 146.69 ?  568 ARG A CZ    1 
ATOM   3181 N NH1   . ARG A 1 587 ? -26.528 52.345  77.028  1.00 149.74 ?  568 ARG A NH1   1 
ATOM   3182 N NH2   . ARG A 1 587 ? -25.902 53.235  75.011  1.00 153.07 ?  568 ARG A NH2   1 
ATOM   3183 N N     . ASN A 1 588 ? -23.537 58.631  80.474  1.00 133.09 ?  569 ASN A N     1 
ATOM   3184 C CA    . ASN A 1 588 ? -23.994 60.013  80.569  1.00 132.17 ?  569 ASN A CA    1 
ATOM   3185 C C     . ASN A 1 588 ? -22.866 60.997  80.880  1.00 125.17 ?  569 ASN A C     1 
ATOM   3186 O O     . ASN A 1 588 ? -23.147 62.155  81.202  1.00 123.68 ?  569 ASN A O     1 
ATOM   3187 C CB    . ASN A 1 588 ? -25.117 60.132  81.604  1.00 131.48 ?  569 ASN A CB    1 
ATOM   3188 C CG    . ASN A 1 588 ? -24.723 59.568  82.947  1.00 141.82 ?  569 ASN A CG    1 
ATOM   3189 O OD1   . ASN A 1 588 ? -24.025 58.549  83.022  1.00 143.88 ?  569 ASN A OD1   1 
ATOM   3190 N ND2   . ASN A 1 588 ? -25.148 60.234  84.024  1.00 144.56 ?  569 ASN A ND2   1 
ATOM   3191 N N     . GLY A 1 589 ? -21.606 60.576  80.751  1.00 121.08 ?  570 GLY A N     1 
ATOM   3192 C CA    . GLY A 1 589 ? -20.478 61.476  80.891  1.00 113.46 ?  570 GLY A CA    1 
ATOM   3193 C C     . GLY A 1 589 ? -19.966 61.450  82.311  1.00 120.23 ?  570 GLY A C     1 
ATOM   3194 O O     . GLY A 1 589 ? -20.745 61.616  83.256  1.00 126.33 ?  570 GLY A O     1 
ATOM   3195 N N     . TYR A 1 590 ? -18.672 61.190  82.465  1.00 117.85 ?  571 TYR A N     1 
ATOM   3196 C CA    . TYR A 1 590 ? -18.029 61.059  83.794  1.00 112.51 ?  571 TYR A CA    1 
ATOM   3197 C C     . TYR A 1 590 ? -18.106 62.383  84.545  1.00 111.52 ?  571 TYR A C     1 
ATOM   3198 O O     . TYR A 1 590 ? -18.208 62.345  85.754  1.00 103.91 ?  571 TYR A O     1 
ATOM   3199 C CB    . TYR A 1 590 ? -16.584 60.616  83.594  1.00 108.44 ?  571 TYR A CB    1 
ATOM   3200 C CG    . TYR A 1 590 ? -15.928 59.813  84.688  1.00 109.20 ?  571 TYR A CG    1 
ATOM   3201 C CD1   . TYR A 1 590 ? -16.625 59.307  85.764  1.00 113.85 ?  571 TYR A CD1   1 
ATOM   3202 C CD2   . TYR A 1 590 ? -14.576 59.552  84.627  1.00 106.49 ?  571 TYR A CD2   1 
ATOM   3203 C CE1   . TYR A 1 590 ? -15.991 58.574  86.752  1.00 105.82 ?  571 TYR A CE1   1 
ATOM   3204 C CE2   . TYR A 1 590 ? -13.927 58.828  85.605  1.00 105.78 ?  571 TYR A CE2   1 
ATOM   3205 C CZ    . TYR A 1 590 ? -14.636 58.338  86.674  1.00 102.78 ?  571 TYR A CZ    1 
ATOM   3206 O OH    . TYR A 1 590 ? -13.961 57.623  87.611  1.00 95.19  ?  571 TYR A OH    1 
ATOM   3207 N N     . SER A 1 591 ? -18.015 63.509  83.846  1.00 114.30 ?  572 SER A N     1 
ATOM   3208 C CA    . SER A 1 591 ? -18.108 64.794  84.518  1.00 107.18 ?  572 SER A CA    1 
ATOM   3209 C C     . SER A 1 591 ? -19.357 64.892  85.383  1.00 109.95 ?  572 SER A C     1 
ATOM   3210 O O     . SER A 1 591 ? -19.434 65.801  86.216  1.00 111.43 ?  572 SER A O     1 
ATOM   3211 C CB    . SER A 1 591 ? -18.106 65.958  83.511  1.00 106.86 ?  572 SER A CB    1 
ATOM   3212 O OG    . SER A 1 591 ? -19.349 66.109  82.828  1.00 104.63 ?  572 SER A OG    1 
ATOM   3213 N N     . CYS A 1 592 ? -20.293 63.974  85.251  1.00 107.82 ?  573 CYS A N     1 
ATOM   3214 C CA    . CYS A 1 592 ? -21.481 64.160  86.108  1.00 111.71 ?  573 CYS A CA    1 
ATOM   3215 C C     . CYS A 1 592 ? -21.073 63.953  87.561  1.00 111.81 ?  573 CYS A C     1 
ATOM   3216 O O     . CYS A 1 592 ? -21.813 64.389  88.431  1.00 110.66 ?  573 CYS A O     1 
ATOM   3217 C CB    . CYS A 1 592 ? -22.524 63.114  85.793  1.00 119.59 ?  573 CYS A CB    1 
ATOM   3218 S SG    . CYS A 1 592 ? -22.026 61.529  86.489  1.00 134.88 ?  573 CYS A SG    1 
ATOM   3219 N N     . VAL A 1 593 ? -19.940 63.299  87.800  1.00 111.95 ?  574 VAL A N     1 
ATOM   3220 C CA    . VAL A 1 593 ? -19.527 63.042  89.210  1.00 109.21 ?  574 VAL A CA    1 
ATOM   3221 C C     . VAL A 1 593 ? -19.000 64.289  89.913  1.00 102.90 ?  574 VAL A C     1 
ATOM   3222 O O     . VAL A 1 593 ? -19.635 64.729  90.855  1.00 101.31 ?  574 VAL A O     1 
ATOM   3223 C CB    . VAL A 1 593 ? -18.453 61.951  89.249  1.00 101.82 ?  574 VAL A CB    1 
ATOM   3224 C CG1   . VAL A 1 593 ? -17.675 61.994  90.539  1.00 93.08  ?  574 VAL A CG1   1 
ATOM   3225 C CG2   . VAL A 1 593 ? -19.062 60.585  89.053  1.00 107.28 ?  574 VAL A CG2   1 
ATOM   3226 N N     . PRO A 1 594 ? -17.994 64.998  89.377  1.00 100.14 ?  575 PRO A N     1 
ATOM   3227 C CA    . PRO A 1 594 ? -17.425 66.155  90.030  1.00 99.25  ?  575 PRO A CA    1 
ATOM   3228 C C     . PRO A 1 594 ? -18.486 67.230  90.191  1.00 104.29 ?  575 PRO A C     1 
ATOM   3229 O O     . PRO A 1 594 ? -18.599 67.768  91.235  1.00 109.03 ?  575 PRO A O     1 
ATOM   3230 C CB    . PRO A 1 594 ? -16.325 66.620  89.088  1.00 90.87  ?  575 PRO A CB    1 
ATOM   3231 C CG    . PRO A 1 594 ? -16.651 65.952  87.810  1.00 99.44  ?  575 PRO A CG    1 
ATOM   3232 C CD    . PRO A 1 594 ? -17.235 64.626  88.222  1.00 105.99 ?  575 PRO A CD    1 
ATOM   3233 N N     . VAL A 1 595 ? -19.315 67.401  89.175  1.00 102.20 ?  576 VAL A N     1 
ATOM   3234 C CA    . VAL A 1 595 ? -20.433 68.366  89.271  1.00 103.71 ?  576 VAL A CA    1 
ATOM   3235 C C     . VAL A 1 595 ? -21.303 67.927  90.440  1.00 105.95 ?  576 VAL A C     1 
ATOM   3236 O O     . VAL A 1 595 ? -21.600 68.754  91.269  1.00 107.92 ?  576 VAL A O     1 
ATOM   3237 C CB    . VAL A 1 595 ? -21.261 68.279  87.988  1.00 102.52 ?  576 VAL A CB    1 
ATOM   3238 C CG1   . VAL A 1 595 ? -22.709 68.642  88.244  1.00 102.23 ?  576 VAL A CG1   1 
ATOM   3239 C CG2   . VAL A 1 595 ? -20.665 69.122  86.884  1.00 105.84 ?  576 VAL A CG2   1 
ATOM   3240 N N     . ALA A 1 596 ? -21.622 66.646  90.557  1.00 104.01 ?  577 ALA A N     1 
ATOM   3241 C CA    . ALA A 1 596 ? -22.423 66.245  91.721  1.00 109.61 ?  577 ALA A CA    1 
ATOM   3242 C C     . ALA A 1 596 ? -21.617 66.499  92.988  1.00 109.82 ?  577 ALA A C     1 
ATOM   3243 O O     . ALA A 1 596 ? -22.153 67.062  93.920  1.00 109.52 ?  577 ALA A O     1 
ATOM   3244 C CB    . ALA A 1 596 ? -22.763 64.794  91.598  1.00 110.24 ?  577 ALA A CB    1 
ATOM   3245 N N     . LEU A 1 597 ? -20.335 66.164  92.972  1.00 107.19 ?  578 LEU A N     1 
ATOM   3246 C CA    . LEU A 1 597 ? -19.498 66.307  94.184  1.00 99.34  ?  578 LEU A CA    1 
ATOM   3247 C C     . LEU A 1 597 ? -19.403 67.757  94.612  1.00 110.35 ?  578 LEU A C     1 
ATOM   3248 O O     . LEU A 1 597 ? -19.488 67.999  95.800  1.00 117.25 ?  578 LEU A O     1 
ATOM   3249 C CB    . LEU A 1 597 ? -18.101 65.769  93.907  1.00 92.00  ?  578 LEU A CB    1 
ATOM   3250 C CG    . LEU A 1 597 ? -17.946 64.295  94.232  1.00 93.88  ?  578 LEU A CG    1 
ATOM   3251 C CD1   . LEU A 1 597 ? -16.688 64.056  95.028  1.00 82.35  ?  578 LEU A CD1   1 
ATOM   3252 C CD2   . LEU A 1 597 ? -19.153 63.811  95.000  1.00 90.22  ?  578 LEU A CD2   1 
ATOM   3253 N N     . ALA A 1 598 ? -19.337 68.690  93.673  1.00 105.64 ?  579 ALA A N     1 
ATOM   3254 C CA    . ALA A 1 598 ? -19.098 70.101  94.039  1.00 105.29 ?  579 ALA A CA    1 
ATOM   3255 C C     . ALA A 1 598 ? -20.367 70.853  94.418  1.00 108.45 ?  579 ALA A C     1 
ATOM   3256 O O     . ALA A 1 598 ? -20.299 72.054  94.514  1.00 113.13 ?  579 ALA A O     1 
ATOM   3257 C CB    . ALA A 1 598 ? -18.386 70.800  92.926  1.00 113.25 ?  579 ALA A CB    1 
ATOM   3258 N N     . GLU A 1 599 ? -21.504 70.198  94.556  1.00 109.62 ?  580 GLU A N     1 
ATOM   3259 C CA    . GLU A 1 599 ? -22.679 70.997  94.940  1.00 113.63 ?  580 GLU A CA    1 
ATOM   3260 C C     . GLU A 1 599 ? -22.438 71.601  96.317  1.00 115.64 ?  580 GLU A C     1 
ATOM   3261 O O     . GLU A 1 599 ? -21.972 70.890  97.193  1.00 111.98 ?  580 GLU A O     1 
ATOM   3262 C CB    . GLU A 1 599 ? -23.896 70.090  95.048  1.00 114.22 ?  580 GLU A CB    1 
ATOM   3263 C CG    . GLU A 1 599 ? -25.086 70.781  95.656  1.00 117.46 ?  580 GLU A CG    1 
ATOM   3264 C CD    . GLU A 1 599 ? -26.309 69.896  95.669  1.00 127.65 ?  580 GLU A CD    1 
ATOM   3265 O OE1   . GLU A 1 599 ? -26.206 68.793  96.202  1.00 132.71 ?  580 GLU A OE1   1 
ATOM   3266 O OE2   . GLU A 1 599 ? -27.349 70.307  95.135  1.00 125.79 ?  580 GLU A OE2   1 
ATOM   3267 N N     . GLY A 1 600 ? -22.750 72.885  96.465  1.00 119.20 ?  581 GLY A N     1 
ATOM   3268 C CA    . GLY A 1 600 ? -22.711 73.578  97.764  1.00 115.66 ?  581 GLY A CA    1 
ATOM   3269 C C     . GLY A 1 600 ? -21.339 73.857  98.320  1.00 107.63 ?  581 GLY A C     1 
ATOM   3270 O O     . GLY A 1 600 ? -21.250 74.068  99.509  1.00 112.23 ?  581 GLY A O     1 
ATOM   3271 N N     . LEU A 1 601 ? -20.294 73.844  97.514  1.00 102.85 ?  582 LEU A N     1 
ATOM   3272 C CA    . LEU A 1 601 ? -18.973 74.162  98.097  1.00 103.48 ?  582 LEU A CA    1 
ATOM   3273 C C     . LEU A 1 601 ? -18.570 75.571  97.678  1.00 108.45 ?  582 LEU A C     1 
ATOM   3274 O O     . LEU A 1 601 ? -19.193 76.116  96.771  1.00 111.86 ?  582 LEU A O     1 
ATOM   3275 C CB    . LEU A 1 601 ? -17.945 73.186  97.536  1.00 100.34 ?  582 LEU A CB    1 
ATOM   3276 C CG    . LEU A 1 601 ? -18.079 71.742  97.987  1.00 100.46 ?  582 LEU A CG    1 
ATOM   3277 C CD1   . LEU A 1 601 ? -16.712 71.158  98.254  1.00 99.15  ?  582 LEU A CD1   1 
ATOM   3278 C CD2   . LEU A 1 601 ? -18.935 71.651  99.225  1.00 102.25 ?  582 LEU A CD2   1 
ATOM   3279 N N     . ASP A 1 602 ? -17.559 76.135  98.331  1.00 111.19 ?  583 ASP A N     1 
ATOM   3280 C CA    . ASP A 1 602 ? -17.066 77.436  97.881  1.00 115.12 ?  583 ASP A CA    1 
ATOM   3281 C C     . ASP A 1 602 ? -15.986 77.218  96.827  1.00 112.94 ?  583 ASP A C     1 
ATOM   3282 O O     . ASP A 1 602 ? -14.872 76.772  97.135  1.00 109.05 ?  583 ASP A O     1 
ATOM   3283 C CB    . ASP A 1 602 ? -16.533 78.304  99.017  1.00 113.70 ?  583 ASP A CB    1 
ATOM   3284 C CG    . ASP A 1 602 ? -16.373 79.772  98.579  1.00 119.61 ?  583 ASP A CG    1 
ATOM   3285 O OD1   . ASP A 1 602 ? -17.344 80.349  98.019  1.00 121.53 ?  583 ASP A OD1   1 
ATOM   3286 O OD2   . ASP A 1 602 ? -15.283 80.351  98.770  1.00 118.99 ?  583 ASP A OD2   1 
ATOM   3287 N N     . ILE A 1 603 ? -16.317 77.543  95.584  1.00 109.81 ?  584 ILE A N     1 
ATOM   3288 C CA    . ILE A 1 603 ? -15.409 77.364  94.469  1.00 105.40 ?  584 ILE A CA    1 
ATOM   3289 C C     . ILE A 1 603 ? -15.260 78.698  93.751  1.00 106.31 ?  584 ILE A C     1 
ATOM   3290 O O     . ILE A 1 603 ? -16.256 79.381  93.483  1.00 105.55 ?  584 ILE A O     1 
ATOM   3291 C CB    . ILE A 1 603 ? -15.926 76.272  93.527  1.00 108.89 ?  584 ILE A CB    1 
ATOM   3292 C CG1   . ILE A 1 603 ? -16.418 75.096  94.369  1.00 110.32 ?  584 ILE A CG1   1 
ATOM   3293 C CG2   . ILE A 1 603 ? -14.832 75.859  92.551  1.00 107.77 ?  584 ILE A CG2   1 
ATOM   3294 C CD1   . ILE A 1 603 ? -17.122 74.052  93.586  1.00 108.22 ?  584 ILE A CD1   1 
ATOM   3295 N N     . LYS A 1 604 ? -14.016 79.079  93.473  1.00 104.69 ?  585 LYS A N     1 
ATOM   3296 C CA    . LYS A 1 604 ? -13.691 80.327  92.788  1.00 103.75 ?  585 LYS A CA    1 
ATOM   3297 C C     . LYS A 1 604 ? -13.102 79.941  91.437  1.00 107.62 ?  585 LYS A C     1 
ATOM   3298 O O     . LYS A 1 604 ? -11.912 79.619  91.338  1.00 108.62 ?  585 LYS A O     1 
ATOM   3299 C CB    . LYS A 1 604 ? -12.716 81.180  93.605  1.00 102.62 ?  585 LYS A CB    1 
ATOM   3300 C CG    . LYS A 1 604 ? -13.212 81.580  95.007  1.00 105.30 ?  585 LYS A CG    1 
ATOM   3301 C CD    . LYS A 1 604 ? -14.632 82.160  94.968  1.00 106.56 ?  585 LYS A CD    1 
ATOM   3302 C CE    . LYS A 1 604 ? -15.195 82.430  96.354  1.00 104.10 ?  585 LYS A CE    1 
ATOM   3303 N NZ    . LYS A 1 604 ? -16.673 82.638  96.277  1.00 104.00 ?  585 LYS A NZ    1 
ATOM   3304 N N     . LEU A 1 605 ? -13.940 79.942  90.403  1.00 106.45 ?  586 LEU A N     1 
ATOM   3305 C CA    . LEU A 1 605 ? -13.469 79.562  89.082  1.00 99.28  ?  586 LEU A CA    1 
ATOM   3306 C C     . LEU A 1 605 ? -12.633 80.671  88.483  1.00 97.79  ?  586 LEU A C     1 
ATOM   3307 O O     . LEU A 1 605 ? -12.690 81.827  88.910  1.00 102.62 ?  586 LEU A O     1 
ATOM   3308 C CB    . LEU A 1 605 ? -14.642 79.237  88.168  1.00 97.11  ?  586 LEU A CB    1 
ATOM   3309 C CG    . LEU A 1 605 ? -15.421 78.026  88.658  1.00 95.08  ?  586 LEU A CG    1 
ATOM   3310 C CD1   . LEU A 1 605 ? -16.762 77.878  87.959  1.00 86.21  ?  586 LEU A CD1   1 
ATOM   3311 C CD2   . LEU A 1 605 ? -14.540 76.801  88.433  1.00 92.83  ?  586 LEU A CD2   1 
ATOM   3312 N N     . ASN A 1 606 ? -11.857 80.304  87.470  1.00 98.61  ?  587 ASN A N     1 
ATOM   3313 C CA    . ASN A 1 606 ? -11.020 81.258  86.748  1.00 104.29 ?  587 ASN A CA    1 
ATOM   3314 C C     . ASN A 1 606 ? -10.086 81.971  87.716  1.00 103.17 ?  587 ASN A C     1 
ATOM   3315 O O     . ASN A 1 606 ? -9.977  83.202  87.727  1.00 106.75 ?  587 ASN A O     1 
ATOM   3316 C CB    . ASN A 1 606 ? -11.858 82.279  85.970  1.00 105.82 ?  587 ASN A CB    1 
ATOM   3317 C CG    . ASN A 1 606 ? -12.813 81.634  85.015  1.00 107.09 ?  587 ASN A CG    1 
ATOM   3318 O OD1   . ASN A 1 606 ? -12.424 81.264  83.911  1.00 105.45 ?  587 ASN A OD1   1 
ATOM   3319 N ND2   . ASN A 1 606 ? -14.090 81.543  85.405  1.00 107.67 ?  587 ASN A ND2   1 
ATOM   3320 N N     . THR A 1 607 ? -9.439  81.193  88.567  1.00 95.75  ?  588 THR A N     1 
ATOM   3321 C CA    . THR A 1 607 ? -8.642  81.773  89.631  1.00 91.63  ?  588 THR A CA    1 
ATOM   3322 C C     . THR A 1 607 ? -7.327  81.011  89.620  1.00 89.71  ?  588 THR A C     1 
ATOM   3323 O O     . THR A 1 607 ? -7.236  79.871  90.090  1.00 91.44  ?  588 THR A O     1 
ATOM   3324 C CB    . THR A 1 607 ? -9.362  81.664  90.954  1.00 97.61  ?  588 THR A CB    1 
ATOM   3325 O OG1   . THR A 1 607 ? -10.673 82.223  90.811  1.00 100.77 ?  588 THR A OG1   1 
ATOM   3326 C CG2   . THR A 1 607 ? -8.627  82.489  91.973  1.00 97.09  ?  588 THR A CG2   1 
ATOM   3327 N N     . ALA A 1 608 ? -6.324  81.616  89.027  1.00 86.95  ?  589 ALA A N     1 
ATOM   3328 C CA    . ALA A 1 608 ? -5.058  80.939  88.838  1.00 91.00  ?  589 ALA A CA    1 
ATOM   3329 C C     . ALA A 1 608 ? -4.172  81.245  90.029  1.00 89.41  ?  589 ALA A C     1 
ATOM   3330 O O     . ALA A 1 608 ? -3.791  82.395  90.243  1.00 96.88  ?  589 ALA A O     1 
ATOM   3331 C CB    . ALA A 1 608 ? -4.402  81.384  87.531  1.00 96.35  ?  589 ALA A CB    1 
ATOM   3332 N N     . VAL A 1 609 ? -3.853  80.231  90.819  1.00 90.10  ?  590 VAL A N     1 
ATOM   3333 C CA    . VAL A 1 609 ? -2.921  80.477  91.912  1.00 98.23  ?  590 VAL A CA    1 
ATOM   3334 C C     . VAL A 1 609 ? -1.535  80.727  91.336  1.00 96.12  ?  590 VAL A C     1 
ATOM   3335 O O     . VAL A 1 609 ? -1.046  79.960  90.500  1.00 95.42  ?  590 VAL A O     1 
ATOM   3336 C CB    . VAL A 1 609 ? -2.927  79.319  92.924  1.00 100.11 ?  590 VAL A CB    1 
ATOM   3337 C CG1   . VAL A 1 609 ? -1.815  79.512  93.932  1.00 96.66  ?  590 VAL A CG1   1 
ATOM   3338 C CG2   . VAL A 1 609 ? -4.284  79.257  93.684  1.00 91.41  ?  590 VAL A CG2   1 
ATOM   3339 N N     . ARG A 1 610 ? -0.919  81.830  91.749  1.00 95.63  ?  591 ARG A N     1 
ATOM   3340 C CA    . ARG A 1 610 ? 0.430   82.205  91.340  1.00 100.49 ?  591 ARG A CA    1 
ATOM   3341 C C     . ARG A 1 610 ? 1.493   81.940  92.396  1.00 99.79  ?  591 ARG A C     1 
ATOM   3342 O O     . ARG A 1 610 ? 2.669   81.764  92.053  1.00 96.37  ?  591 ARG A O     1 
ATOM   3343 C CB    . ARG A 1 610 ? 0.479   83.701  90.986  1.00 108.98 ?  591 ARG A CB    1 
ATOM   3344 C CG    . ARG A 1 610 ? -0.246  84.152  89.736  1.00 109.23 ?  591 ARG A CG    1 
ATOM   3345 C CD    . ARG A 1 610 ? 0.511   83.636  88.514  1.00 118.83 ?  591 ARG A CD    1 
ATOM   3346 N NE    . ARG A 1 610 ? -0.102  84.017  87.240  1.00 127.59 ?  591 ARG A NE    1 
ATOM   3347 C CZ    . ARG A 1 610 ? 0.140   85.170  86.617  1.00 123.80 ?  591 ARG A CZ    1 
ATOM   3348 N NH1   . ARG A 1 610 ? -0.443  85.432  85.455  1.00 124.84 ?  591 ARG A NH1   1 
ATOM   3349 N NH2   . ARG A 1 610 ? 0.931   86.081  87.179  1.00 119.50 ?  591 ARG A NH2   1 
ATOM   3350 N N     . GLN A 1 611 ? 1.125   81.967  93.672  1.00 102.13 ?  592 GLN A N     1 
ATOM   3351 C CA    . GLN A 1 611 ? 2.129   81.958  94.721  1.00 99.11  ?  592 GLN A CA    1 
ATOM   3352 C C     . GLN A 1 611 ? 1.436   81.470  95.984  1.00 99.37  ?  592 GLN A C     1 
ATOM   3353 O O     . GLN A 1 611 ? 0.346   81.956  96.325  1.00 96.56  ?  592 GLN A O     1 
ATOM   3354 C CB    . GLN A 1 611 ? 2.730   83.364  94.917  1.00 100.77 ?  592 GLN A CB    1 
ATOM   3355 C CG    . GLN A 1 611 ? 3.905   83.437  95.887  1.00 101.74 ?  592 GLN A CG    1 
ATOM   3356 C CD    . GLN A 1 611 ? 4.603   84.805  95.923  1.00 103.36 ?  592 GLN A CD    1 
ATOM   3357 O OE1   . GLN A 1 611 ? 4.640   85.462  96.963  1.00 105.37 ?  592 GLN A OE1   1 
ATOM   3358 N NE2   . GLN A 1 611 ? 5.133   85.243  94.785  1.00 105.02 ?  592 GLN A NE2   1 
ATOM   3359 N N     . VAL A 1 612 ? 2.038   80.475  96.640  1.00 100.33 ?  593 VAL A N     1 
ATOM   3360 C CA    . VAL A 1 612 ? 1.589   79.992  97.943  1.00 96.67  ?  593 VAL A CA    1 
ATOM   3361 C C     . VAL A 1 612 ? 2.649   80.383  98.964  1.00 97.72  ?  593 VAL A C     1 
ATOM   3362 O O     . VAL A 1 612 ? 3.806   79.939  98.874  1.00 93.10  ?  593 VAL A O     1 
ATOM   3363 C CB    . VAL A 1 612 ? 1.355   78.473  97.962  1.00 92.97  ?  593 VAL A CB    1 
ATOM   3364 C CG1   . VAL A 1 612 ? 0.785   78.070  99.270  1.00 99.00  ?  593 VAL A CG1   1 
ATOM   3365 C CG2   . VAL A 1 612 ? 0.379   78.069  96.924  1.00 101.73 ?  593 VAL A CG2   1 
ATOM   3366 N N     . ARG A 1 613 ? 2.241   81.233  99.921  1.00 95.11  ?  594 ARG A N     1 
ATOM   3367 C CA    . ARG A 1 613 ? 3.039   81.648  101.068 1.00 93.41  ?  594 ARG A CA    1 
ATOM   3368 C C     . ARG A 1 613 ? 2.511   80.936  102.315 1.00 98.60  ?  594 ARG A C     1 
ATOM   3369 O O     . ARG A 1 613 ? 1.402   81.233  102.785 1.00 94.45  ?  594 ARG A O     1 
ATOM   3370 C CB    . ARG A 1 613 ? 2.982   83.165  101.241 1.00 100.87 ?  594 ARG A CB    1 
ATOM   3371 C CG    . ARG A 1 613 ? 3.703   83.940  100.157 1.00 107.17 ?  594 ARG A CG    1 
ATOM   3372 C CD    . ARG A 1 613 ? 3.696   85.480  100.348 1.00 111.04 ?  594 ARG A CD    1 
ATOM   3373 N NE    . ARG A 1 613 ? 4.948   86.079  99.865  1.00 115.08 ?  594 ARG A NE    1 
ATOM   3374 C CZ    . ARG A 1 613 ? 6.002   86.370  100.632 1.00 117.37 ?  594 ARG A CZ    1 
ATOM   3375 N NH1   . ARG A 1 613 ? 5.942   86.203  101.964 1.00 107.95 ?  594 ARG A NH1   1 
ATOM   3376 N NH2   . ARG A 1 613 ? 7.098   86.884  100.062 1.00 116.67 ?  594 ARG A NH2   1 
ATOM   3377 N N     . TYR A 1 614 ? 3.306   79.997  102.846 1.00 97.85  ?  595 TYR A N     1 
ATOM   3378 C CA    . TYR A 1 614 ? 2.991   79.266  104.070 1.00 92.58  ?  595 TYR A CA    1 
ATOM   3379 C C     . TYR A 1 614 ? 3.985   79.714  105.139 1.00 97.80  ?  595 TYR A C     1 
ATOM   3380 O O     . TYR A 1 614 ? 5.205   79.596  104.946 1.00 97.18  ?  595 TYR A O     1 
ATOM   3381 C CB    . TYR A 1 614 ? 3.038   77.741  103.849 1.00 91.09  ?  595 TYR A CB    1 
ATOM   3382 C CG    . TYR A 1 614 ? 4.340   77.177  103.277 1.00 93.46  ?  595 TYR A CG    1 
ATOM   3383 C CD1   . TYR A 1 614 ? 4.612   77.177  101.915 1.00 98.00  ?  595 TYR A CD1   1 
ATOM   3384 C CD2   . TYR A 1 614 ? 5.294   76.641  104.110 1.00 95.22  ?  595 TYR A CD2   1 
ATOM   3385 C CE1   . TYR A 1 614 ? 5.823   76.667  101.418 1.00 96.79  ?  595 TYR A CE1   1 
ATOM   3386 C CE2   . TYR A 1 614 ? 6.485   76.135  103.627 1.00 92.30  ?  595 TYR A CE2   1 
ATOM   3387 C CZ    . TYR A 1 614 ? 6.748   76.145  102.298 1.00 94.09  ?  595 TYR A CZ    1 
ATOM   3388 O OH    . TYR A 1 614 ? 7.957   75.636  101.892 1.00 96.98  ?  595 TYR A OH    1 
ATOM   3389 N N     . THR A 1 615 ? 3.468   80.256  106.251 1.00 102.56 ?  596 THR A N     1 
ATOM   3390 C CA    . THR A 1 615 ? 4.285   80.841  107.316 1.00 97.63  ?  596 THR A CA    1 
ATOM   3391 C C     . THR A 1 615 ? 3.873   80.242  108.647 1.00 96.35  ?  596 THR A C     1 
ATOM   3392 O O     . THR A 1 615 ? 2.804   79.632  108.775 1.00 95.87  ?  596 THR A O     1 
ATOM   3393 C CB    . THR A 1 615 ? 4.118   82.359  107.425 1.00 105.93 ?  596 THR A CB    1 
ATOM   3394 O OG1   . THR A 1 615 ? 2.716   82.687  107.470 1.00 105.02 ?  596 THR A OG1   1 
ATOM   3395 C CG2   . THR A 1 615 ? 4.777   83.061  106.217 1.00 108.80 ?  596 THR A CG2   1 
ATOM   3396 N N     . ALA A 1 616 ? 4.718   80.478  109.658 1.00 103.09 ?  597 ALA A N     1 
ATOM   3397 C CA    . ALA A 1 616 ? 4.508   79.839  110.957 1.00 102.33 ?  597 ALA A CA    1 
ATOM   3398 C C     . ALA A 1 616 ? 3.145   80.189  111.547 1.00 92.70  ?  597 ALA A C     1 
ATOM   3399 O O     . ALA A 1 616 ? 2.549   79.365  112.252 1.00 89.37  ?  597 ALA A O     1 
ATOM   3400 C CB    . ALA A 1 616 ? 5.639   80.207  111.914 1.00 94.38  ?  597 ALA A CB    1 
ATOM   3401 N N     . SER A 1 617 ? 2.605   81.361  111.208 1.00 89.92  ?  598 SER A N     1 
ATOM   3402 C CA    . SER A 1 617 ? 1.297   81.777  111.700 1.00 92.83  ?  598 SER A CA    1 
ATOM   3403 C C     . SER A 1 617 ? 0.136   81.523  110.734 1.00 96.47  ?  598 SER A C     1 
ATOM   3404 O O     . SER A 1 617 ? -1.025  81.598  111.158 1.00 94.20  ?  598 SER A O     1 
ATOM   3405 C CB    . SER A 1 617 ? 1.340   83.262  112.075 1.00 94.84  ?  598 SER A CB    1 
ATOM   3406 O OG    . SER A 1 617 ? 1.792   84.058  110.999 1.00 102.62 ?  598 SER A OG    1 
ATOM   3407 N N     . GLY A 1 618 ? 0.392   81.230  109.464 1.00 97.58  ?  599 GLY A N     1 
ATOM   3408 C CA    . GLY A 1 618 ? -0.709  80.969  108.557 1.00 99.75  ?  599 GLY A CA    1 
ATOM   3409 C C     . GLY A 1 618 ? -0.234  80.899  107.119 1.00 100.34 ?  599 GLY A C     1 
ATOM   3410 O O     . GLY A 1 618 ? 0.970   80.845  106.852 1.00 100.34 ?  599 GLY A O     1 
ATOM   3411 N N     . CYS A 1 619 ? -1.212  80.892  106.192 1.00 100.13 ?  600 CYS A N     1 
ATOM   3412 C CA    . CYS A 1 619 ? -0.944  80.865  104.755 1.00 99.25  ?  600 CYS A CA    1 
ATOM   3413 C C     . CYS A 1 619 ? -1.753  81.912  104.001 1.00 99.91  ?  600 CYS A C     1 
ATOM   3414 O O     . CYS A 1 619 ? -2.945  82.112  104.272 1.00 97.66  ?  600 CYS A O     1 
ATOM   3415 C CB    . CYS A 1 619 ? -1.238  79.511  104.153 1.00 95.65  ?  600 CYS A CB    1 
ATOM   3416 S SG    . CYS A 1 619 ? -0.197  78.222  104.786 1.00 102.99 ?  600 CYS A SG    1 
ATOM   3417 N N     . GLU A 1 620 ? -1.089  82.569  103.043 1.00 99.99  ?  601 GLU A N     1 
ATOM   3418 C CA    . GLU A 1 620 ? -1.728  83.517  102.135 1.00 102.92 ?  601 GLU A CA    1 
ATOM   3419 C C     . GLU A 1 620 ? -1.462  83.070  100.702 1.00 102.37 ?  601 GLU A C     1 
ATOM   3420 O O     . GLU A 1 620 ? -0.311  82.794  100.329 1.00 95.92  ?  601 GLU A O     1 
ATOM   3421 C CB    . GLU A 1 620 ? -1.259  84.968  102.385 1.00 105.84 ?  601 GLU A CB    1 
ATOM   3422 C CG    . GLU A 1 620 ? 0.256   85.229  102.242 1.00 111.86 ?  601 GLU A CG    1 
ATOM   3423 C CD    . GLU A 1 620 ? 0.693   86.653  102.668 1.00 116.95 ?  601 GLU A CD    1 
ATOM   3424 O OE1   . GLU A 1 620 ? -0.160  87.586  102.693 1.00 113.02 ?  601 GLU A OE1   1 
ATOM   3425 O OE2   . GLU A 1 620 ? 1.913   86.822  102.968 1.00 117.14 ?  601 GLU A OE2   1 
ATOM   3426 N N     . VAL A 1 621 ? -2.539  82.953  99.924  1.00 103.13 ?  602 VAL A N     1 
ATOM   3427 C CA    . VAL A 1 621 ? -2.497  82.399  98.578  1.00 102.36 ?  602 VAL A CA    1 
ATOM   3428 C C     . VAL A 1 621 ? -2.812  83.517  97.593  1.00 104.34 ?  602 VAL A C     1 
ATOM   3429 O O     . VAL A 1 621 ? -3.866  84.165  97.688  1.00 102.11 ?  602 VAL A O     1 
ATOM   3430 C CB    . VAL A 1 621 ? -3.475  81.229  98.416  1.00 101.31 ?  602 VAL A CB    1 
ATOM   3431 C CG1   . VAL A 1 621 ? -3.583  80.875  96.962  1.00 106.33 ?  602 VAL A CG1   1 
ATOM   3432 C CG2   . VAL A 1 621 ? -2.990  80.027  99.181  1.00 99.08  ?  602 VAL A CG2   1 
ATOM   3433 N N     . ILE A 1 622 ? -1.903  83.723  96.638  1.00 103.19 ?  603 ILE A N     1 
ATOM   3434 C CA    . ILE A 1 622 ? -1.959  84.837  95.701  1.00 101.61 ?  603 ILE A CA    1 
ATOM   3435 C C     . ILE A 1 622 ? -2.477  84.317  94.372  1.00 99.53  ?  603 ILE A C     1 
ATOM   3436 O O     . ILE A 1 622 ? -1.825  83.481  93.733  1.00 98.45  ?  603 ILE A O     1 
ATOM   3437 C CB    . ILE A 1 622 ? -0.578  85.477  95.520  1.00 102.32 ?  603 ILE A CB    1 
ATOM   3438 C CG1   . ILE A 1 622 ? 0.151   85.533  96.860  1.00 102.57 ?  603 ILE A CG1   1 
ATOM   3439 C CG2   . ILE A 1 622 ? -0.737  86.864  94.934  1.00 106.24 ?  603 ILE A CG2   1 
ATOM   3440 C CD1   . ILE A 1 622 ? 1.547   86.063  96.765  1.00 101.66 ?  603 ILE A CD1   1 
ATOM   3441 N N     . ALA A 1 623 ? -3.625  84.838  93.932  1.00 99.60  ?  604 ALA A N     1 
ATOM   3442 C CA    . ALA A 1 623 ? -4.315  84.313  92.759  1.00 103.60 ?  604 ALA A CA    1 
ATOM   3443 C C     . ALA A 1 623 ? -4.750  85.429  91.809  1.00 108.89 ?  604 ALA A C     1 
ATOM   3444 O O     . ALA A 1 623 ? -5.348  86.417  92.248  1.00 113.41 ?  604 ALA A O     1 
ATOM   3445 C CB    . ALA A 1 623 ? -5.535  83.499  93.192  1.00 102.82 ?  604 ALA A CB    1 
ATOM   3446 N N     . VAL A 1 624 ? -4.474  85.256  90.495  1.00 106.46 ?  605 VAL A N     1 
ATOM   3447 C CA    . VAL A 1 624 ? -4.920  86.193  89.458  1.00 99.27  ?  605 VAL A CA    1 
ATOM   3448 C C     . VAL A 1 624 ? -6.236  85.689  88.877  1.00 97.93  ?  605 VAL A C     1 
ATOM   3449 O O     . VAL A 1 624 ? -6.606  84.522  89.011  1.00 104.73 ?  605 VAL A O     1 
ATOM   3450 C CB    . VAL A 1 624 ? -3.886  86.363  88.326  1.00 97.55  ?  605 VAL A CB    1 
ATOM   3451 C CG1   . VAL A 1 624 ? -2.546  86.825  88.883  1.00 104.54 ?  605 VAL A CG1   1 
ATOM   3452 C CG2   . VAL A 1 624 ? -3.784  85.124  87.491  1.00 99.16  ?  605 VAL A CG2   1 
ATOM   3453 N N     . ASN A 1 625 ? -6.953  86.568  88.205  1.00 100.70 ?  606 ASN A N     1 
ATOM   3454 C CA    . ASN A 1 625 ? -8.135  86.154  87.459  1.00 107.83 ?  606 ASN A CA    1 
ATOM   3455 C C     . ASN A 1 625 ? -7.726  85.868  86.012  1.00 112.50 ?  606 ASN A C     1 
ATOM   3456 O O     . ASN A 1 625 ? -7.155  86.738  85.340  1.00 111.87 ?  606 ASN A O     1 
ATOM   3457 C CB    . ASN A 1 625 ? -9.228  87.219  87.548  1.00 114.68 ?  606 ASN A CB    1 
ATOM   3458 C CG    . ASN A 1 625 ? -10.472 86.851  86.765  1.00 111.76 ?  606 ASN A CG    1 
ATOM   3459 O OD1   . ASN A 1 625 ? -11.298 86.052  87.225  1.00 109.45 ?  606 ASN A OD1   1 
ATOM   3460 N ND2   . ASN A 1 625 ? -10.639 87.470  85.602  1.00 110.03 ?  606 ASN A ND2   1 
ATOM   3461 N N     . THR A 1 626 ? -8.015  84.638  85.543  1.00 116.62 ?  607 THR A N     1 
ATOM   3462 C CA    . THR A 1 626 ? -7.464  84.128  84.280  1.00 112.16 ?  607 THR A CA    1 
ATOM   3463 C C     . THR A 1 626 ? -7.887  84.981  83.095  1.00 118.69 ?  607 THR A C     1 
ATOM   3464 O O     . THR A 1 626 ? -7.130  85.126  82.123  1.00 118.48 ?  607 THR A O     1 
ATOM   3465 C CB    . THR A 1 626 ? -7.896  82.670  84.045  1.00 99.11  ?  607 THR A CB    1 
ATOM   3466 O OG1   . THR A 1 626 ? -9.296  82.511  84.336  1.00 95.24  ?  607 THR A OG1   1 
ATOM   3467 C CG2   . THR A 1 626 ? -7.067  81.700  84.882  1.00 97.88  ?  607 THR A CG2   1 
ATOM   3468 N N     . ARG A 1 627 ? -9.087  85.552  83.163  1.00 116.64 ?  608 ARG A N     1 
ATOM   3469 C CA    . ARG A 1 627 ? -9.556  86.426  82.101  1.00 117.37 ?  608 ARG A CA    1 
ATOM   3470 C C     . ARG A 1 627 ? -8.722  87.718  82.029  1.00 122.69 ?  608 ARG A C     1 
ATOM   3471 O O     . ARG A 1 627 ? -8.089  88.005  81.001  1.00 123.65 ?  608 ARG A O     1 
ATOM   3472 C CB    . ARG A 1 627 ? -11.046 86.684  82.325  1.00 115.24 ?  608 ARG A CB    1 
ATOM   3473 C CG    . ARG A 1 627 ? -11.879 85.391  82.300  1.00 107.68 ?  608 ARG A CG    1 
ATOM   3474 C CD    . ARG A 1 627 ? -13.258 85.628  82.890  1.00 116.41 ?  608 ARG A CD    1 
ATOM   3475 N NE    . ARG A 1 627 ? -13.280 85.488  84.349  1.00 128.63 ?  608 ARG A NE    1 
ATOM   3476 C CZ    . ARG A 1 627 ? -14.392 85.481  85.097  1.00 137.39 ?  608 ARG A CZ    1 
ATOM   3477 N NH1   . ARG A 1 627 ? -15.584 85.641  84.513  1.00 137.36 ?  608 ARG A NH1   1 
ATOM   3478 N NH2   . ARG A 1 627 ? -14.321 85.327  86.433  1.00 133.05 ?  608 ARG A NH2   1 
ATOM   3479 N N     . SER A 1 628 ? -8.666  88.484  83.127  1.00 122.15 ?  609 SER A N     1 
ATOM   3480 C CA    . SER A 1 628 ? -7.916  89.750  83.215  1.00 123.46 ?  609 SER A CA    1 
ATOM   3481 C C     . SER A 1 628 ? -6.733  89.597  84.179  1.00 120.81 ?  609 SER A C     1 
ATOM   3482 O O     . SER A 1 628 ? -6.850  89.975  85.351  1.00 118.40 ?  609 SER A O     1 
ATOM   3483 C CB    . SER A 1 628 ? -8.828  90.901  83.693  1.00 123.73 ?  609 SER A CB    1 
ATOM   3484 O OG    . SER A 1 628 ? -9.555  90.526  84.859  1.00 122.57 ?  609 SER A OG    1 
ATOM   3485 N N     . THR A 1 629 ? -5.562  89.081  83.675  1.00 121.12 ?  610 THR A N     1 
ATOM   3486 C CA    . THR A 1 629 ? -4.468  88.690  84.607  1.00 121.17 ?  610 THR A CA    1 
ATOM   3487 C C     . THR A 1 629 ? -3.763  89.903  85.299  1.00 124.67 ?  610 THR A C     1 
ATOM   3488 O O     . THR A 1 629 ? -2.760  89.688  86.029  1.00 124.98 ?  610 THR A O     1 
ATOM   3489 C CB    . THR A 1 629 ? -3.390  87.815  83.944  1.00 113.48 ?  610 THR A CB    1 
ATOM   3490 O OG1   . THR A 1 629 ? -2.484  88.614  83.161  1.00 110.11 ?  610 THR A OG1   1 
ATOM   3491 C CG2   . THR A 1 629 ? -4.032  86.732  83.085  1.00 118.79 ?  610 THR A CG2   1 
ATOM   3492 N N     . SER A 1 630 ? -4.191  91.155  85.140  1.00 121.55 ?  611 SER A N     1 
ATOM   3493 C CA    . SER A 1 630 ? -3.843  92.135  86.159  1.00 120.73 ?  611 SER A CA    1 
ATOM   3494 C C     . SER A 1 630 ? -4.503  91.770  87.488  1.00 118.58 ?  611 SER A C     1 
ATOM   3495 O O     . SER A 1 630 ? -3.814  91.565  88.497  1.00 117.22 ?  611 SER A O     1 
ATOM   3496 C CB    . SER A 1 630 ? -4.239  93.539  85.702  1.00 124.09 ?  611 SER A CB    1 
ATOM   3497 O OG    . SER A 1 630 ? -5.635  93.620  85.467  1.00 131.26 ?  611 SER A OG    1 
ATOM   3498 N N     . GLN A 1 631 ? -5.836  91.601  87.475  1.00 115.33 ?  612 GLN A N     1 
ATOM   3499 C CA    . GLN A 1 631 ? -6.689  91.499  88.660  1.00 112.89 ?  612 GLN A CA    1 
ATOM   3500 C C     . GLN A 1 631 ? -6.205  90.498  89.704  1.00 112.95 ?  612 GLN A C     1 
ATOM   3501 O O     . GLN A 1 631 ? -6.258  89.285  89.467  1.00 116.37 ?  612 GLN A O     1 
ATOM   3502 C CB    . GLN A 1 631 ? -8.109  91.122  88.246  1.00 112.34 ?  612 GLN A CB    1 
ATOM   3503 C CG    . GLN A 1 631 ? -9.066  91.023  89.426  1.00 114.26 ?  612 GLN A CG    1 
ATOM   3504 C CD    . GLN A 1 631 ? -10.522 91.020  88.998  1.00 119.43 ?  612 GLN A CD    1 
ATOM   3505 O OE1   . GLN A 1 631 ? -10.838 91.265  87.833  1.00 122.60 ?  612 GLN A OE1   1 
ATOM   3506 N NE2   . GLN A 1 631 ? -11.417 90.736  89.939  1.00 117.59 ?  612 GLN A NE2   1 
ATOM   3507 N N     . THR A 1 632 ? -5.788  90.986  90.878  1.00 108.44 ?  613 THR A N     1 
ATOM   3508 C CA    . THR A 1 632 ? -5.135  90.150  91.874  1.00 104.28 ?  613 THR A CA    1 
ATOM   3509 C C     . THR A 1 632 ? -6.100  89.816  93.017  1.00 104.36 ?  613 THR A C     1 
ATOM   3510 O O     . THR A 1 632 ? -6.998  90.598  93.352  1.00 103.23 ?  613 THR A O     1 
ATOM   3511 C CB    . THR A 1 632 ? -3.861  90.836  92.391  1.00 93.78  ?  613 THR A CB    1 
ATOM   3512 O OG1   . THR A 1 632 ? -2.989  91.097  91.287  1.00 88.06  ?  613 THR A OG1   1 
ATOM   3513 C CG2   . THR A 1 632 ? -3.113  89.932  93.326  1.00 95.13  ?  613 THR A CG2   1 
ATOM   3514 N N     . PHE A 1 633 ? -5.934  88.604  93.565  1.00 103.27 ?  614 PHE A N     1 
ATOM   3515 C CA    . PHE A 1 633 ? -6.678  88.078  94.711  1.00 104.54 ?  614 PHE A CA    1 
ATOM   3516 C C     . PHE A 1 633 ? -5.692  87.626  95.788  1.00 106.14 ?  614 PHE A C     1 
ATOM   3517 O O     . PHE A 1 633 ? -4.750  86.874  95.495  1.00 103.53 ?  614 PHE A O     1 
ATOM   3518 C CB    . PHE A 1 633 ? -7.570  86.881  94.318  1.00 103.71 ?  614 PHE A CB    1 
ATOM   3519 C CG    . PHE A 1 633 ? -8.842  87.253  93.582  1.00 108.56 ?  614 PHE A CG    1 
ATOM   3520 C CD1   . PHE A 1 633 ? -10.088 87.108  94.205  1.00 103.98 ?  614 PHE A CD1   1 
ATOM   3521 C CD2   . PHE A 1 633 ? -8.798  87.734  92.268  1.00 113.26 ?  614 PHE A CD2   1 
ATOM   3522 C CE1   . PHE A 1 633 ? -11.271 87.428  93.541  1.00 104.06 ?  614 PHE A CE1   1 
ATOM   3523 C CE2   . PHE A 1 633 ? -9.970  88.063  91.593  1.00 114.33 ?  614 PHE A CE2   1 
ATOM   3524 C CZ    . PHE A 1 633 ? -11.213 87.907  92.234  1.00 116.17 ?  614 PHE A CZ    1 
ATOM   3525 N N     . ILE A 1 634 ? -5.908  88.078  97.032  1.00 110.27 ?  615 ILE A N     1 
ATOM   3526 C CA    . ILE A 1 634 ? -5.172  87.581  98.196  1.00 105.46 ?  615 ILE A CA    1 
ATOM   3527 C C     . ILE A 1 634 ? -6.142  86.877  99.135  1.00 101.01 ?  615 ILE A C     1 
ATOM   3528 O O     . ILE A 1 634 ? -7.171  87.449  99.532  1.00 92.07  ?  615 ILE A O     1 
ATOM   3529 C CB    . ILE A 1 634 ? -4.390  88.680  98.938  1.00 98.63  ?  615 ILE A CB    1 
ATOM   3530 C CG1   . ILE A 1 634 ? -3.211  89.153  98.090  1.00 104.58 ?  615 ILE A CG1   1 
ATOM   3531 C CG2   . ILE A 1 634 ? -3.824  88.131  100.206 1.00 96.86  ?  615 ILE A CG2   1 
ATOM   3532 C CD1   . ILE A 1 634 ? -2.118  88.094  97.911  1.00 100.35 ?  615 ILE A CD1   1 
ATOM   3533 N N     . TYR A 1 635 ? -5.806  85.622  99.452  1.00 103.39 ?  616 TYR A N     1 
ATOM   3534 C CA    . TYR A 1 635 ? -6.553  84.719  100.320 1.00 102.17 ?  616 TYR A CA    1 
ATOM   3535 C C     . TYR A 1 635 ? -5.674  84.310  101.492 1.00 102.29 ?  616 TYR A C     1 
ATOM   3536 O O     . TYR A 1 635 ? -4.546  83.853  101.285 1.00 100.02 ?  616 TYR A O     1 
ATOM   3537 C CB    . TYR A 1 635 ? -6.992  83.472  99.545  1.00 99.86  ?  616 TYR A CB    1 
ATOM   3538 C CG    . TYR A 1 635 ? -8.110  83.705  98.545  1.00 105.57 ?  616 TYR A CG    1 
ATOM   3539 C CD1   . TYR A 1 635 ? -7.849  83.939  97.175  1.00 101.96 ?  616 TYR A CD1   1 
ATOM   3540 C CD2   . TYR A 1 635 ? -9.444  83.628  98.961  1.00 104.92 ?  616 TYR A CD2   1 
ATOM   3541 C CE1   . TYR A 1 635 ? -8.908  84.134  96.260  1.00 99.11  ?  616 TYR A CE1   1 
ATOM   3542 C CE2   . TYR A 1 635 ? -10.501 83.810  98.064  1.00 103.99 ?  616 TYR A CE2   1 
ATOM   3543 C CZ    . TYR A 1 635 ? -10.240 84.060  96.721  1.00 102.63 ?  616 TYR A CZ    1 
ATOM   3544 O OH    . TYR A 1 635 ? -11.339 84.234  95.884  1.00 98.66  ?  616 TYR A OH    1 
ATOM   3545 N N     . LYS A 1 636 ? -6.193  84.466  102.712 1.00 102.37 ?  617 LYS A N     1 
ATOM   3546 C CA    . LYS A 1 636 ? -5.523  84.056  103.942 1.00 99.37  ?  617 LYS A CA    1 
ATOM   3547 C C     . LYS A 1 636 ? -6.252  82.854  104.544 1.00 99.52  ?  617 LYS A C     1 
ATOM   3548 O O     . LYS A 1 636 ? -7.479  82.742  104.433 1.00 100.38 ?  617 LYS A O     1 
ATOM   3549 C CB    . LYS A 1 636 ? -5.494  85.209  104.954 1.00 98.92  ?  617 LYS A CB    1 
ATOM   3550 C CG    . LYS A 1 636 ? -5.095  86.592  104.402 1.00 104.05 ?  617 LYS A CG    1 
ATOM   3551 C CD    . LYS A 1 636 ? -3.578  86.795  104.282 1.00 107.70 ?  617 LYS A CD    1 
ATOM   3552 C CE    . LYS A 1 636 ? -3.226  88.169  103.675 1.00 101.43 ?  617 LYS A CE    1 
ATOM   3553 N NZ    . LYS A 1 636 ? -3.646  89.362  104.462 1.00 99.46  ?  617 LYS A NZ    1 
ATOM   3554 N N     . CYS A 1 637 ? -5.492  81.953  105.181 1.00 94.22  ?  618 CYS A N     1 
ATOM   3555 C CA    . CYS A 1 637 ? -6.046  80.698  105.688 1.00 95.42  ?  618 CYS A CA    1 
ATOM   3556 C C     . CYS A 1 637 ? -5.063  80.046  106.660 1.00 102.38 ?  618 CYS A C     1 
ATOM   3557 O O     . CYS A 1 637 ? -3.885  80.418  106.725 1.00 100.05 ?  618 CYS A O     1 
ATOM   3558 C CB    . CYS A 1 637 ? -6.328  79.721  104.552 1.00 102.83 ?  618 CYS A CB    1 
ATOM   3559 S SG    . CYS A 1 637 ? -4.795  79.032  103.831 1.00 109.75 ?  618 CYS A SG    1 
ATOM   3560 N N     . ASP A 1 638 ? -5.559  79.012  107.374 1.00 98.73  ?  619 ASP A N     1 
ATOM   3561 C CA    . ASP A 1 638 ? -4.741  78.193  108.279 1.00 98.83  ?  619 ASP A CA    1 
ATOM   3562 C C     . ASP A 1 638 ? -3.870  77.155  107.551 1.00 101.73 ?  619 ASP A C     1 
ATOM   3563 O O     . ASP A 1 638 ? -2.664  77.039  107.831 1.00 94.22  ?  619 ASP A O     1 
ATOM   3564 C CB    . ASP A 1 638 ? -5.648  77.501  109.290 1.00 101.24 ?  619 ASP A CB    1 
ATOM   3565 C CG    . ASP A 1 638 ? -6.296  78.462  110.245 1.00 102.75 ?  619 ASP A CG    1 
ATOM   3566 O OD1   . ASP A 1 638 ? -5.549  79.236  110.886 1.00 101.97 ?  619 ASP A OD1   1 
ATOM   3567 O OD2   . ASP A 1 638 ? -7.540  78.448  110.349 1.00 102.13 ?  619 ASP A OD2   1 
ATOM   3568 N N     . ALA A 1 639 ? -4.469  76.363  106.646 1.00 106.38 ?  620 ALA A N     1 
ATOM   3569 C CA    . ALA A 1 639 ? -3.750  75.348  105.881 1.00 100.15 ?  620 ALA A CA    1 
ATOM   3570 C C     . ALA A 1 639 ? -4.224  75.315  104.434 1.00 98.86  ?  620 ALA A C     1 
ATOM   3571 O O     . ALA A 1 639 ? -5.404  75.546  104.133 1.00 94.90  ?  620 ALA A O     1 
ATOM   3572 C CB    . ALA A 1 639 ? -3.919  73.956  106.481 1.00 98.61  ?  620 ALA A CB    1 
ATOM   3573 N N     . VAL A 1 640 ? -3.285  74.980  103.546 1.00 103.87 ?  621 VAL A N     1 
ATOM   3574 C CA    . VAL A 1 640 ? -3.505  75.005  102.096 1.00 103.12 ?  621 VAL A CA    1 
ATOM   3575 C C     . VAL A 1 640 ? -3.361  73.592  101.536 1.00 99.27  ?  621 VAL A C     1 
ATOM   3576 O O     . VAL A 1 640 ? -2.254  73.027  101.541 1.00 97.39  ?  621 VAL A O     1 
ATOM   3577 C CB    . VAL A 1 640 ? -2.524  75.944  101.382 1.00 96.02  ?  621 VAL A CB    1 
ATOM   3578 C CG1   . VAL A 1 640 ? -2.747  75.857  99.920  1.00 96.97  ?  621 VAL A CG1   1 
ATOM   3579 C CG2   . VAL A 1 640 ? -2.736  77.334  101.823 1.00 102.52 ?  621 VAL A CG2   1 
ATOM   3580 N N     . LEU A 1 641 ? -4.470  73.039  101.026 1.00 96.22  ?  622 LEU A N     1 
ATOM   3581 C CA    . LEU A 1 641 ? -4.491  71.716  100.412 1.00 91.28  ?  622 LEU A CA    1 
ATOM   3582 C C     . LEU A 1 641 ? -4.365  71.862  98.903  1.00 92.84  ?  622 LEU A C     1 
ATOM   3583 O O     . LEU A 1 641 ? -5.219  72.488  98.261  1.00 89.90  ?  622 LEU A O     1 
ATOM   3584 C CB    . LEU A 1 641 ? -5.768  70.952  100.744 1.00 87.37  ?  622 LEU A CB    1 
ATOM   3585 C CG    . LEU A 1 641 ? -5.685  69.583  100.081 1.00 83.48  ?  622 LEU A CG    1 
ATOM   3586 C CD1   . LEU A 1 641 ? -4.364  68.903  100.388 1.00 83.70  ?  622 LEU A CD1   1 
ATOM   3587 C CD2   . LEU A 1 641 ? -6.827  68.721  100.461 1.00 74.86  ?  622 LEU A CD2   1 
ATOM   3588 N N     . CYS A 1 642 ? -3.336  71.226  98.341  1.00 93.88  ?  623 CYS A N     1 
ATOM   3589 C CA    . CYS A 1 642 ? -2.807  71.525  97.013  1.00 90.44  ?  623 CYS A CA    1 
ATOM   3590 C C     . CYS A 1 642 ? -2.980  70.335  96.054  1.00 93.74  ?  623 CYS A C     1 
ATOM   3591 O O     . CYS A 1 642 ? -2.080  69.505  95.873  1.00 92.69  ?  623 CYS A O     1 
ATOM   3592 C CB    . CYS A 1 642 ? -1.344  71.921  97.173  1.00 88.90  ?  623 CYS A CB    1 
ATOM   3593 S SG    . CYS A 1 642 ? -0.366  71.942  95.651  1.00 106.88 ?  623 CYS A SG    1 
ATOM   3594 N N     . THR A 1 643 ? -4.135  70.266  95.400  1.00 91.62  ?  624 THR A N     1 
ATOM   3595 C CA    . THR A 1 643 ? -4.312  69.265  94.353  1.00 90.40  ?  624 THR A CA    1 
ATOM   3596 C C     . THR A 1 643 ? -3.793  69.749  92.988  1.00 92.49  ?  624 THR A C     1 
ATOM   3597 O O     . THR A 1 643 ? -4.450  69.569  91.959  1.00 93.89  ?  624 THR A O     1 
ATOM   3598 C CB    . THR A 1 643 ? -5.783  68.836  94.288  1.00 88.45  ?  624 THR A CB    1 
ATOM   3599 O OG1   . THR A 1 643 ? -6.622  69.895  93.803  1.00 86.51  ?  624 THR A OG1   1 
ATOM   3600 C CG2   . THR A 1 643 ? -6.252  68.450  95.677  1.00 84.70  ?  624 THR A CG2   1 
ATOM   3601 N N     . LEU A 1 644 ? -2.618  70.382  92.946  1.00 92.77  ?  625 LEU A N     1 
ATOM   3602 C CA    . LEU A 1 644 ? -2.045  70.746  91.657  1.00 87.19  ?  625 LEU A CA    1 
ATOM   3603 C C     . LEU A 1 644 ? -1.543  69.482  90.997  1.00 90.91  ?  625 LEU A C     1 
ATOM   3604 O O     . LEU A 1 644 ? -0.840  68.704  91.648  1.00 95.32  ?  625 LEU A O     1 
ATOM   3605 C CB    . LEU A 1 644 ? -0.878  71.723  91.759  1.00 88.29  ?  625 LEU A CB    1 
ATOM   3606 C CG    . LEU A 1 644 ? -1.117  73.193  92.108  1.00 89.41  ?  625 LEU A CG    1 
ATOM   3607 C CD1   . LEU A 1 644 ? 0.205   73.965  92.077  1.00 81.85  ?  625 LEU A CD1   1 
ATOM   3608 C CD2   . LEU A 1 644 ? -2.133  73.825  91.179  1.00 93.33  ?  625 LEU A CD2   1 
ATOM   3609 N N     . PRO A 1 645 ? -1.880  69.243  89.728  1.00 96.59  ?  626 PRO A N     1 
ATOM   3610 C CA    . PRO A 1 645 ? -1.376  68.050  89.037  1.00 91.35  ?  626 PRO A CA    1 
ATOM   3611 C C     . PRO A 1 645 ? 0.146   68.060  88.938  1.00 86.19  ?  626 PRO A C     1 
ATOM   3612 O O     . PRO A 1 645 ? 0.775   69.118  88.809  1.00 80.26  ?  626 PRO A O     1 
ATOM   3613 C CB    . PRO A 1 645 ? -2.031  68.148  87.658  1.00 87.46  ?  626 PRO A CB    1 
ATOM   3614 C CG    . PRO A 1 645 ? -3.270  68.982  87.880  1.00 88.60  ?  626 PRO A CG    1 
ATOM   3615 C CD    . PRO A 1 645 ? -2.868  69.985  88.919  1.00 94.04  ?  626 PRO A CD    1 
ATOM   3616 N N     . LEU A 1 646 ? 0.735   66.850  89.018  1.00 85.85  ?  627 LEU A N     1 
ATOM   3617 C CA    . LEU A 1 646 ? 2.196   66.726  89.049  1.00 87.20  ?  627 LEU A CA    1 
ATOM   3618 C C     . LEU A 1 646 ? 2.877   67.472  87.909  1.00 93.17  ?  627 LEU A C     1 
ATOM   3619 O O     . LEU A 1 646 ? 3.998   67.973  88.071  1.00 93.39  ?  627 LEU A O     1 
ATOM   3620 C CB    . LEU A 1 646 ? 2.622   65.257  89.032  1.00 81.57  ?  627 LEU A CB    1 
ATOM   3621 C CG    . LEU A 1 646 ? 4.153   65.018  89.006  1.00 85.25  ?  627 LEU A CG    1 
ATOM   3622 C CD1   . LEU A 1 646 ? 4.977   65.716  90.066  1.00 85.63  ?  627 LEU A CD1   1 
ATOM   3623 C CD2   . LEU A 1 646 ? 4.412   63.553  89.127  1.00 97.60  ?  627 LEU A CD2   1 
ATOM   3624 N N     . GLY A 1 647 ? 2.223   67.567  86.755  1.00 95.61  ?  628 GLY A N     1 
ATOM   3625 C CA    . GLY A 1 647 ? 2.789   68.361  85.677  1.00 92.66  ?  628 GLY A CA    1 
ATOM   3626 C C     . GLY A 1 647 ? 2.937   69.824  86.045  1.00 91.58  ?  628 GLY A C     1 
ATOM   3627 O O     . GLY A 1 647 ? 3.997   70.426  85.838  1.00 91.58  ?  628 GLY A O     1 
ATOM   3628 N N     . VAL A 1 648 ? 1.878   70.414  86.611  1.00 94.02  ?  629 VAL A N     1 
ATOM   3629 C CA    . VAL A 1 648 ? 1.927   71.839  86.927  1.00 94.28  ?  629 VAL A CA    1 
ATOM   3630 C C     . VAL A 1 648 ? 3.056   72.092  87.928  1.00 91.14  ?  629 VAL A C     1 
ATOM   3631 O O     . VAL A 1 648 ? 3.841   73.045  87.785  1.00 85.70  ?  629 VAL A O     1 
ATOM   3632 C CB    . VAL A 1 648 ? 0.558   72.320  87.457  1.00 86.60  ?  629 VAL A CB    1 
ATOM   3633 C CG1   . VAL A 1 648 ? 0.608   73.797  87.806  1.00 83.32  ?  629 VAL A CG1   1 
ATOM   3634 C CG2   . VAL A 1 648 ? -0.581  71.960  86.504  1.00 92.54  ?  629 VAL A CG2   1 
ATOM   3635 N N     . LEU A 1 649 ? 3.194   71.193  88.918  1.00 92.46  ?  630 LEU A N     1 
ATOM   3636 C CA    . LEU A 1 649 ? 4.341   71.248  89.826  1.00 94.94  ?  630 LEU A CA    1 
ATOM   3637 C C     . LEU A 1 649 ? 5.651   71.045  89.074  1.00 95.18  ?  630 LEU A C     1 
ATOM   3638 O O     . LEU A 1 649 ? 6.669   71.680  89.386  1.00 96.36  ?  630 LEU A O     1 
ATOM   3639 C CB    . LEU A 1 649 ? 4.224   70.202  90.948  1.00 92.13  ?  630 LEU A CB    1 
ATOM   3640 C CG    . LEU A 1 649 ? 2.901   70.091  91.703  1.00 87.06  ?  630 LEU A CG    1 
ATOM   3641 C CD1   . LEU A 1 649 ? 2.906   68.881  92.646  1.00 77.78  ?  630 LEU A CD1   1 
ATOM   3642 C CD2   . LEU A 1 649 ? 2.591   71.382  92.410  1.00 85.37  ?  630 LEU A CD2   1 
ATOM   3643 N N     . LYS A 1 650 ? 5.649   70.137  88.116  1.00 94.99  ?  631 LYS A N     1 
ATOM   3644 C CA    . LYS A 1 650 ? 6.932   69.826  87.453  1.00 92.37  ?  631 LYS A CA    1 
ATOM   3645 C C     . LYS A 1 650 ? 7.352   70.975  86.551  1.00 100.08 ?  631 LYS A C     1 
ATOM   3646 O O     . LYS A 1 650 ? 8.527   71.053  86.221  1.00 100.57 ?  631 LYS A O     1 
ATOM   3647 C CB    . LYS A 1 650 ? 6.749   68.603  86.562  1.00 80.67  ?  631 LYS A CB    1 
ATOM   3648 C CG    . LYS A 1 650 ? 6.672   67.270  87.280  1.00 87.14  ?  631 LYS A CG    1 
ATOM   3649 C CD    . LYS A 1 650 ? 7.194   66.130  86.447  1.00 86.57  ?  631 LYS A CD    1 
ATOM   3650 C CE    . LYS A 1 650 ? 8.268   65.323  87.130  1.00 90.59  ?  631 LYS A CE    1 
ATOM   3651 N NZ    . LYS A 1 650 ? 9.372   65.048  86.191  1.00 83.88  ?  631 LYS A NZ    1 
ATOM   3652 N N     . GLN A 1 651 ? 6.429   71.878  86.253  1.00 100.70 ?  632 GLN A N     1 
ATOM   3653 C CA    . GLN A 1 651 ? 6.700   72.917  85.234  1.00 100.89 ?  632 GLN A CA    1 
ATOM   3654 C C     . GLN A 1 651 ? 7.902   73.773  85.584  1.00 105.31 ?  632 GLN A C     1 
ATOM   3655 O O     . GLN A 1 651 ? 8.066   74.109  86.730  1.00 110.09 ?  632 GLN A O     1 
ATOM   3656 C CB    . GLN A 1 651 ? 5.516   73.862  85.153  1.00 98.22  ?  632 GLN A CB    1 
ATOM   3657 C CG    . GLN A 1 651 ? 5.023   74.072  83.741  1.00 104.83 ?  632 GLN A CG    1 
ATOM   3658 C CD    . GLN A 1 651 ? 4.424   75.445  83.629  1.00 109.85 ?  632 GLN A CD    1 
ATOM   3659 O OE1   . GLN A 1 651 ? 3.210   75.612  83.560  1.00 103.56 ?  632 GLN A OE1   1 
ATOM   3660 N NE2   . GLN A 1 651 ? 5.289   76.443  83.626  1.00 106.67 ?  632 GLN A NE2   1 
ATOM   3661 N N     . GLN A 1 652 ? 8.732   74.051  84.592  1.00 109.79 ?  633 GLN A N     1 
ATOM   3662 C CA    . GLN A 1 652 ? 9.860   74.989  84.762  1.00 117.64 ?  633 GLN A CA    1 
ATOM   3663 C C     . GLN A 1 652 ? 9.809   75.914  83.546  1.00 125.86 ?  633 GLN A C     1 
ATOM   3664 O O     . GLN A 1 652 ? 9.857   75.364  82.450  1.00 125.00 ?  633 GLN A O     1 
ATOM   3665 C CB    . GLN A 1 652 ? 11.162  74.219  84.899  1.00 118.68 ?  633 GLN A CB    1 
ATOM   3666 C CG    . GLN A 1 652 ? 11.478  73.884  86.342  1.00 113.79 ?  633 GLN A CG    1 
ATOM   3667 C CD    . GLN A 1 652 ? 12.038  75.098  87.025  1.00 123.51 ?  633 GLN A CD    1 
ATOM   3668 O OE1   . GLN A 1 652 ? 12.252  76.126  86.399  1.00 126.15 ?  633 GLN A OE1   1 
ATOM   3669 N NE2   . GLN A 1 652 ? 12.279  74.988  88.316  1.00 125.84 ?  633 GLN A NE2   1 
ATOM   3670 N N     . PRO A 1 653 ? 9.718   77.262  83.628  1.00 124.18 ?  634 PRO A N     1 
ATOM   3671 C CA    . PRO A 1 653 ? 9.532   78.045  84.855  1.00 117.58 ?  634 PRO A CA    1 
ATOM   3672 C C     . PRO A 1 653 ? 8.193   77.793  85.542  1.00 116.03 ?  634 PRO A C     1 
ATOM   3673 O O     . PRO A 1 653 ? 7.221   77.579  84.880  1.00 114.60 ?  634 PRO A O     1 
ATOM   3674 C CB    . PRO A 1 653 ? 9.542   79.487  84.368  1.00 115.98 ?  634 PRO A CB    1 
ATOM   3675 C CG    . PRO A 1 653 ? 10.354  79.406  83.122  1.00 118.83 ?  634 PRO A CG    1 
ATOM   3676 C CD    . PRO A 1 653 ? 9.826   78.146  82.483  1.00 122.50 ?  634 PRO A CD    1 
ATOM   3677 N N     . PRO A 1 654 ? 8.188   77.822  86.881  1.00 107.69 ?  635 PRO A N     1 
ATOM   3678 C CA    . PRO A 1 654 ? 7.045   77.419  87.665  1.00 106.36 ?  635 PRO A CA    1 
ATOM   3679 C C     . PRO A 1 654 ? 5.744   78.192  87.512  1.00 92.01  ?  635 PRO A C     1 
ATOM   3680 O O     . PRO A 1 654 ? 5.746   79.357  87.588  1.00 81.76  ?  635 PRO A O     1 
ATOM   3681 C CB    . PRO A 1 654 ? 7.547   77.640  89.088  1.00 107.51 ?  635 PRO A CB    1 
ATOM   3682 C CG    . PRO A 1 654 ? 9.028   77.505  88.959  1.00 111.95 ?  635 PRO A CG    1 
ATOM   3683 C CD    . PRO A 1 654 ? 9.305   78.257  87.685  1.00 107.60 ?  635 PRO A CD    1 
ATOM   3684 N N     . ALA A 1 655 ? 4.661   77.449  87.383  1.00 93.96  ?  636 ALA A N     1 
ATOM   3685 C CA    . ALA A 1 655 ? 3.337   78.070  87.276  1.00 87.02  ?  636 ALA A CA    1 
ATOM   3686 C C     . ALA A 1 655 ? 3.025   78.596  88.653  1.00 95.23  ?  636 ALA A C     1 
ATOM   3687 O O     . ALA A 1 655 ? 2.352   79.592  88.732  1.00 97.96  ?  636 ALA A O     1 
ATOM   3688 C CB    . ALA A 1 655 ? 2.324   77.040  86.894  1.00 92.05  ?  636 ALA A CB    1 
ATOM   3689 N N     . VAL A 1 656 ? 3.465   77.884  89.684  1.00 101.80 ?  637 VAL A N     1 
ATOM   3690 C CA    . VAL A 1 656 ? 3.236   78.374  91.038  1.00 94.36  ?  637 VAL A CA    1 
ATOM   3691 C C     . VAL A 1 656 ? 4.552   78.368  91.815  1.00 92.36  ?  637 VAL A C     1 
ATOM   3692 O O     . VAL A 1 656 ? 5.289   77.374  91.819  1.00 85.23  ?  637 VAL A O     1 
ATOM   3693 C CB    . VAL A 1 656 ? 2.166   77.554  91.778  1.00 90.22  ?  637 VAL A CB    1 
ATOM   3694 C CG1   . VAL A 1 656 ? 2.062   78.026  93.201  1.00 96.06  ?  637 VAL A CG1   1 
ATOM   3695 C CG2   . VAL A 1 656 ? 0.834   77.702  91.092  1.00 91.98  ?  637 VAL A CG2   1 
ATOM   3696 N N     . GLN A 1 657 ? 4.832   79.502  92.450  1.00 101.69 ?  638 GLN A N     1 
ATOM   3697 C CA    . GLN A 1 657 ? 5.993   79.785  93.281  1.00 99.31  ?  638 GLN A CA    1 
ATOM   3698 C C     . GLN A 1 657 ? 5.638   79.556  94.740  1.00 104.78 ?  638 GLN A C     1 
ATOM   3699 O O     . GLN A 1 657 ? 4.680   80.155  95.255  1.00 103.42 ?  638 GLN A O     1 
ATOM   3700 C CB    . GLN A 1 657 ? 6.398   81.243  93.062  1.00 101.99 ?  638 GLN A CB    1 
ATOM   3701 C CG    . GLN A 1 657 ? 7.319   81.877  94.061  1.00 107.37 ?  638 GLN A CG    1 
ATOM   3702 C CD    . GLN A 1 657 ? 7.401   83.384  93.800  1.00 122.20 ?  638 GLN A CD    1 
ATOM   3703 O OE1   . GLN A 1 657 ? 6.541   83.939  93.092  1.00 120.32 ?  638 GLN A OE1   1 
ATOM   3704 N NE2   . GLN A 1 657 ? 8.335   84.071  94.475  1.00 124.62 ?  638 GLN A NE2   1 
ATOM   3705 N N     . PHE A 1 658 ? 6.406   78.707  95.411  1.00 103.31 ?  639 PHE A N     1 
ATOM   3706 C CA    . PHE A 1 658 ? 6.156   78.437  96.817  1.00 99.95  ?  639 PHE A CA    1 
ATOM   3707 C C     . PHE A 1 658 ? 7.102   79.270  97.670  1.00 96.77  ?  639 PHE A C     1 
ATOM   3708 O O     . PHE A 1 658 ? 8.329   79.149  97.556  1.00 93.19  ?  639 PHE A O     1 
ATOM   3709 C CB    . PHE A 1 658 ? 6.293   76.951  97.133  1.00 104.21 ?  639 PHE A CB    1 
ATOM   3710 C CG    . PHE A 1 658 ? 5.136   76.131  96.651  1.00 97.44  ?  639 PHE A CG    1 
ATOM   3711 C CD1   . PHE A 1 658 ? 3.893   76.230  97.273  1.00 97.96  ?  639 PHE A CD1   1 
ATOM   3712 C CD2   . PHE A 1 658 ? 5.303   75.202  95.658  1.00 89.86  ?  639 PHE A CD2   1 
ATOM   3713 C CE1   . PHE A 1 658 ? 2.820   75.468  96.849  1.00 91.50  ?  639 PHE A CE1   1 
ATOM   3714 C CE2   . PHE A 1 658 ? 4.240   74.423  95.250  1.00 92.97  ?  639 PHE A CE2   1 
ATOM   3715 C CZ    . PHE A 1 658 ? 2.999   74.555  95.845  1.00 87.69  ?  639 PHE A CZ    1 
ATOM   3716 N N     . VAL A 1 659 ? 6.525   80.127  98.499  1.00 97.84  ?  640 VAL A N     1 
ATOM   3717 C CA    . VAL A 1 659 ? 7.274   80.981  99.415  1.00 98.38  ?  640 VAL A CA    1 
ATOM   3718 C C     . VAL A 1 659 ? 7.015   80.457  100.820 1.00 96.71  ?  640 VAL A C     1 
ATOM   3719 O O     . VAL A 1 659 ? 5.912   80.646  101.355 1.00 92.30  ?  640 VAL A O     1 
ATOM   3720 C CB    . VAL A 1 659 ? 6.868   82.456  99.289  1.00 104.49 ?  640 VAL A CB    1 
ATOM   3721 C CG1   . VAL A 1 659 ? 7.654   83.288  100.255 1.00 110.85 ?  640 VAL A CG1   1 
ATOM   3722 C CG2   . VAL A 1 659 ? 7.115   82.983  97.866  1.00 112.59 ?  640 VAL A CG2   1 
ATOM   3723 N N     . PRO A 1 660 ? 7.985   79.784  101.458 1.00 98.89  ?  641 PRO A N     1 
ATOM   3724 C CA    . PRO A 1 660 ? 9.370   79.512  101.032 1.00 101.35 ?  641 PRO A CA    1 
ATOM   3725 C C     . PRO A 1 660 ? 9.486   78.352  100.050 1.00 106.27 ?  641 PRO A C     1 
ATOM   3726 O O     . PRO A 1 660 ? 8.488   77.634  99.872  1.00 104.12 ?  641 PRO A O     1 
ATOM   3727 C CB    . PRO A 1 660 ? 10.062  79.112  102.331 1.00 95.52  ?  641 PRO A CB    1 
ATOM   3728 C CG    . PRO A 1 660 ? 8.977   78.471  103.083 1.00 103.89 ?  641 PRO A CG    1 
ATOM   3729 C CD    . PRO A 1 660 ? 7.742   79.286  102.816 1.00 99.36  ?  641 PRO A CD    1 
ATOM   3730 N N     . PRO A 1 661 ? 10.677  78.164  99.463  1.00 106.41 ?  642 PRO A N     1 
ATOM   3731 C CA    . PRO A 1 661 ? 10.920  76.994  98.607  1.00 104.74 ?  642 PRO A CA    1 
ATOM   3732 C C     . PRO A 1 661 ? 10.468  75.687  99.248  1.00 102.25 ?  642 PRO A C     1 
ATOM   3733 O O     . PRO A 1 661 ? 10.659  75.465  100.449 1.00 104.10 ?  642 PRO A O     1 
ATOM   3734 C CB    . PRO A 1 661 ? 12.443  77.010  98.425  1.00 98.95  ?  642 PRO A CB    1 
ATOM   3735 C CG    . PRO A 1 661 ? 12.811  78.409  98.564  1.00 97.17  ?  642 PRO A CG    1 
ATOM   3736 C CD    . PRO A 1 661 ? 11.887  78.995  99.586  1.00 106.64 ?  642 PRO A CD    1 
ATOM   3737 N N     . LEU A 1 662 ? 9.877   74.810  98.436  1.00 96.92  ?  643 LEU A N     1 
ATOM   3738 C CA    . LEU A 1 662 ? 9.691   73.450  98.901  1.00 92.48  ?  643 LEU A CA    1 
ATOM   3739 C C     . LEU A 1 662 ? 11.059  72.807  99.083  1.00 92.55  ?  643 LEU A C     1 
ATOM   3740 O O     . LEU A 1 662 ? 11.961  73.018  98.262  1.00 94.21  ?  643 LEU A O     1 
ATOM   3741 C CB    . LEU A 1 662 ? 8.828   72.638  97.940  1.00 85.74  ?  643 LEU A CB    1 
ATOM   3742 C CG    . LEU A 1 662 ? 7.500   73.348  97.698  1.00 88.98  ?  643 LEU A CG    1 
ATOM   3743 C CD1   . LEU A 1 662 ? 6.606   72.498  96.868  1.00 85.03  ?  643 LEU A CD1   1 
ATOM   3744 C CD2   . LEU A 1 662 ? 6.836   73.644  99.026  1.00 99.29  ?  643 LEU A CD2   1 
ATOM   3745 N N     . PRO A 1 663 ? 11.264  72.070  100.164 1.00 89.36  ?  644 PRO A N     1 
ATOM   3746 C CA    . PRO A 1 663 ? 12.606  71.568  100.478 1.00 87.79  ?  644 PRO A CA    1 
ATOM   3747 C C     . PRO A 1 663 ? 13.063  70.512  99.480  1.00 94.47  ?  644 PRO A C     1 
ATOM   3748 O O     . PRO A 1 663 ? 12.272  69.941  98.720  1.00 93.58  ?  644 PRO A O     1 
ATOM   3749 C CB    . PRO A 1 663 ? 12.440  70.983  101.878 1.00 86.18  ?  644 PRO A CB    1 
ATOM   3750 C CG    . PRO A 1 663 ? 10.955  70.641  101.944 1.00 85.04  ?  644 PRO A CG    1 
ATOM   3751 C CD    . PRO A 1 663 ? 10.240  71.660  101.142 1.00 85.26  ?  644 PRO A CD    1 
ATOM   3752 N N     . GLU A 1 664 ? 14.379  70.254  99.506  1.00 98.54  ?  645 GLU A N     1 
ATOM   3753 C CA    . GLU A 1 664 ? 15.031  69.412  98.494  1.00 103.24 ?  645 GLU A CA    1 
ATOM   3754 C C     . GLU A 1 664 ? 14.512  67.970  98.458  1.00 98.24  ?  645 GLU A C     1 
ATOM   3755 O O     . GLU A 1 664 ? 14.525  67.334  97.397  1.00 99.34  ?  645 GLU A O     1 
ATOM   3756 C CB    . GLU A 1 664 ? 16.543  69.405  98.727  1.00 112.96 ?  645 GLU A CB    1 
ATOM   3757 C CG    . GLU A 1 664 ? 17.314  68.545  97.735  1.00 124.03 ?  645 GLU A CG    1 
ATOM   3758 C CD    . GLU A 1 664 ? 18.816  68.586  97.955  1.00 145.18 ?  645 GLU A CD    1 
ATOM   3759 O OE1   . GLU A 1 664 ? 19.275  69.314  98.870  1.00 151.18 ?  645 GLU A OE1   1 
ATOM   3760 O OE2   . GLU A 1 664 ? 19.534  67.838  97.248  1.00 159.24 ?  645 GLU A OE2   1 
ATOM   3761 N N     . TRP A 1 665 ? 14.100  67.412  99.596  1.00 98.92  ?  646 TRP A N     1 
ATOM   3762 C CA    . TRP A 1 665 ? 13.547  66.063  99.556  1.00 93.99  ?  646 TRP A CA    1 
ATOM   3763 C C     . TRP A 1 665 ? 12.253  66.039  98.758  1.00 91.65  ?  646 TRP A C     1 
ATOM   3764 O O     . TRP A 1 665 ? 11.964  65.036  98.098  1.00 102.15 ?  646 TRP A O     1 
ATOM   3765 C CB    . TRP A 1 665 ? 13.321  65.516  100.975 1.00 91.52  ?  646 TRP A CB    1 
ATOM   3766 C CG    . TRP A 1 665 ? 12.400  66.353  101.811 1.00 85.51  ?  646 TRP A CG    1 
ATOM   3767 C CD1   . TRP A 1 665 ? 12.761  67.378  102.640 1.00 81.34  ?  646 TRP A CD1   1 
ATOM   3768 C CD2   . TRP A 1 665 ? 10.962  66.227  101.922 1.00 80.88  ?  646 TRP A CD2   1 
ATOM   3769 N NE1   . TRP A 1 665 ? 11.640  67.905  103.239 1.00 84.91  ?  646 TRP A NE1   1 
ATOM   3770 C CE2   . TRP A 1 665 ? 10.525  67.219  102.815 1.00 80.77  ?  646 TRP A CE2   1 
ATOM   3771 C CE3   . TRP A 1 665 ? 10.008  65.383  101.342 1.00 84.76  ?  646 TRP A CE3   1 
ATOM   3772 C CZ2   . TRP A 1 665 ? 9.161   67.391  103.143 1.00 77.77  ?  646 TRP A CZ2   1 
ATOM   3773 C CZ3   . TRP A 1 665 ? 8.650   65.550  101.693 1.00 82.88  ?  646 TRP A CZ3   1 
ATOM   3774 C CH2   . TRP A 1 665 ? 8.250   66.543  102.577 1.00 72.36  ?  646 TRP A CH2   1 
ATOM   3775 N N     . LYS A 1 666 ? 11.489  67.144  98.778  1.00 80.96  ?  647 LYS A N     1 
ATOM   3776 C CA    . LYS A 1 666 ? 10.228  67.243  98.050  1.00 78.39  ?  647 LYS A CA    1 
ATOM   3777 C C     . LYS A 1 666 ? 10.437  67.533  96.568  1.00 93.11  ?  647 LYS A C     1 
ATOM   3778 O O     . LYS A 1 666 ? 9.779   66.926  95.710  1.00 96.80  ?  647 LYS A O     1 
ATOM   3779 C CB    . LYS A 1 666 ? 9.358   68.334  98.649  1.00 81.24  ?  647 LYS A CB    1 
ATOM   3780 C CG    . LYS A 1 666 ? 8.127   68.663  97.801  1.00 83.04  ?  647 LYS A CG    1 
ATOM   3781 C CD    . LYS A 1 666 ? 7.045   67.604  97.809  1.00 82.10  ?  647 LYS A CD    1 
ATOM   3782 C CE    . LYS A 1 666 ? 6.396   67.547  99.188  1.00 88.41  ?  647 LYS A CE    1 
ATOM   3783 N NZ    . LYS A 1 666 ? 5.170   66.706  99.301  1.00 91.34  ?  647 LYS A NZ    1 
ATOM   3784 N N     . THR A 1 667 ? 11.307  68.499  96.245  1.00 97.59  ?  648 THR A N     1 
ATOM   3785 C CA    . THR A 1 667 ? 11.507  68.867  94.841  1.00 93.67  ?  648 THR A CA    1 
ATOM   3786 C C     . THR A 1 667 ? 12.108  67.703  94.071  1.00 98.16  ?  648 THR A C     1 
ATOM   3787 O O     . THR A 1 667 ? 11.677  67.392  92.955  1.00 99.66  ?  648 THR A O     1 
ATOM   3788 C CB    . THR A 1 667 ? 12.423  70.091  94.715  1.00 91.84  ?  648 THR A CB    1 
ATOM   3789 O OG1   . THR A 1 667 ? 13.775  69.724  95.033  1.00 98.46  ?  648 THR A OG1   1 
ATOM   3790 C CG2   . THR A 1 667 ? 11.987  71.223  95.648  1.00 86.21  ?  648 THR A CG2   1 
ATOM   3791 N N     . SER A 1 668 ? 13.106  67.046  94.667  1.00 97.30  ?  649 SER A N     1 
ATOM   3792 C CA    . SER A 1 668 ? 13.704  65.883  94.038  1.00 98.72  ?  649 SER A CA    1 
ATOM   3793 C C     . SER A 1 668 ? 12.701  64.754  93.914  1.00 96.14  ?  649 SER A C     1 
ATOM   3794 O O     . SER A 1 668 ? 12.786  63.959  92.976  1.00 103.51 ?  649 SER A O     1 
ATOM   3795 C CB    . SER A 1 668 ? 14.944  65.437  94.814  1.00 98.16  ?  649 SER A CB    1 
ATOM   3796 O OG    . SER A 1 668 ? 15.953  66.437  94.762  1.00 102.28 ?  649 SER A OG    1 
ATOM   3797 N N     . ALA A 1 669 ? 11.728  64.671  94.819  1.00 91.46  ?  650 ALA A N     1 
ATOM   3798 C CA    . ALA A 1 669 ? 10.686  63.683  94.582  1.00 94.29  ?  650 ALA A CA    1 
ATOM   3799 C C     . ALA A 1 669 ? 9.827   64.060  93.401  1.00 99.57  ?  650 ALA A C     1 
ATOM   3800 O O     . ALA A 1 669 ? 9.158   63.189  92.836  1.00 106.04 ?  650 ALA A O     1 
ATOM   3801 C CB    . ALA A 1 669 ? 9.787   63.488  95.791  1.00 95.09  ?  650 ALA A CB    1 
ATOM   3802 N N     . VAL A 1 670 ? 9.850   65.322  92.993  1.00 99.77  ?  651 VAL A N     1 
ATOM   3803 C CA    . VAL A 1 670 ? 9.049   65.708  91.840  1.00 102.10 ?  651 VAL A CA    1 
ATOM   3804 C C     . VAL A 1 670 ? 9.798   65.458  90.526  1.00 98.45  ?  651 VAL A C     1 
ATOM   3805 O O     . VAL A 1 670 ? 9.183   65.052  89.533  1.00 93.13  ?  651 VAL A O     1 
ATOM   3806 C CB    . VAL A 1 670 ? 8.600   67.172  92.015  1.00 96.32  ?  651 VAL A CB    1 
ATOM   3807 C CG1   . VAL A 1 670 ? 7.769   67.641  90.837  1.00 96.05  ?  651 VAL A CG1   1 
ATOM   3808 C CG2   . VAL A 1 670 ? 7.823   67.303  93.309  1.00 93.91  ?  651 VAL A CG2   1 
ATOM   3809 N N     . GLN A 1 671 ? 11.135  65.635  90.506  1.00 98.44  ?  652 GLN A N     1 
ATOM   3810 C CA    . GLN A 1 671 ? 11.901  65.319  89.298  1.00 99.63  ?  652 GLN A CA    1 
ATOM   3811 C C     . GLN A 1 671 ? 11.908  63.827  89.020  1.00 105.60 ?  652 GLN A C     1 
ATOM   3812 O O     . GLN A 1 671 ? 11.800  63.411  87.857  1.00 117.96 ?  652 GLN A O     1 
ATOM   3813 C CB    . GLN A 1 671 ? 13.351  65.792  89.391  1.00 104.02 ?  652 GLN A CB    1 
ATOM   3814 C CG    . GLN A 1 671 ? 13.556  67.275  89.238  1.00 119.62 ?  652 GLN A CG    1 
ATOM   3815 C CD    . GLN A 1 671 ? 14.791  67.732  89.984  1.00 135.04 ?  652 GLN A CD    1 
ATOM   3816 O OE1   . GLN A 1 671 ? 15.699  66.928  90.229  1.00 136.86 ?  652 GLN A OE1   1 
ATOM   3817 N NE2   . GLN A 1 671 ? 14.799  68.995  90.430  1.00 134.41 ?  652 GLN A NE2   1 
ATOM   3818 N N     . ARG A 1 672 ? 12.072  63.007  90.067  1.00 98.13  ?  653 ARG A N     1 
ATOM   3819 C CA    . ARG A 1 672 ? 12.212  61.568  89.860  1.00 96.17  ?  653 ARG A CA    1 
ATOM   3820 C C     . ARG A 1 672 ? 10.925  60.961  89.348  1.00 98.27  ?  653 ARG A C     1 
ATOM   3821 O O     . ARG A 1 672 ? 10.952  60.118  88.444  1.00 101.30 ?  653 ARG A O     1 
ATOM   3822 C CB    . ARG A 1 672 ? 12.636  60.878  91.149  1.00 99.73  ?  653 ARG A CB    1 
ATOM   3823 C CG    . ARG A 1 672 ? 14.051  61.206  91.561  1.00 104.13 ?  653 ARG A CG    1 
ATOM   3824 C CD    . ARG A 1 672 ? 14.478  60.353  92.712  1.00 98.52  ?  653 ARG A CD    1 
ATOM   3825 N NE    . ARG A 1 672 ? 13.454  60.410  93.759  1.00 102.13 ?  653 ARG A NE    1 
ATOM   3826 C CZ    . ARG A 1 672 ? 13.465  61.262  94.782  1.00 104.15 ?  653 ARG A CZ    1 
ATOM   3827 N NH1   . ARG A 1 672 ? 14.444  62.156  94.897  1.00 106.47 ?  653 ARG A NH1   1 
ATOM   3828 N NH2   . ARG A 1 672 ? 12.485  61.231  95.680  1.00 104.87 ?  653 ARG A NH2   1 
ATOM   3829 N N     . MET A 1 673 ? 9.788   61.387  89.890  1.00 95.76  ?  654 MET A N     1 
ATOM   3830 C CA    . MET A 1 673 ? 8.546   60.783  89.459  1.00 98.97  ?  654 MET A CA    1 
ATOM   3831 C C     . MET A 1 673 ? 8.299   61.000  87.970  1.00 99.29  ?  654 MET A C     1 
ATOM   3832 O O     . MET A 1 673 ? 9.021   61.716  87.254  1.00 93.96  ?  654 MET A O     1 
ATOM   3833 C CB    . MET A 1 673 ? 7.361   61.339  90.230  1.00 100.02 ?  654 MET A CB    1 
ATOM   3834 C CG    . MET A 1 673 ? 7.178   60.716  91.582  1.00 112.27 ?  654 MET A CG    1 
ATOM   3835 S SD    . MET A 1 673 ? 5.616   61.283  92.290  1.00 126.84 ?  654 MET A SD    1 
ATOM   3836 C CE    . MET A 1 673 ? 4.489   60.699  91.014  1.00 114.47 ?  654 MET A CE    1 
ATOM   3837 N N     . GLY A 1 674 ? 7.241   60.365  87.510  1.00 100.11 ?  655 GLY A N     1 
ATOM   3838 C CA    . GLY A 1 674 ? 6.857   60.559  86.139  1.00 100.25 ?  655 GLY A CA    1 
ATOM   3839 C C     . GLY A 1 674 ? 5.462   61.116  86.008  1.00 96.33  ?  655 GLY A C     1 
ATOM   3840 O O     . GLY A 1 674 ? 4.505   60.617  86.621  1.00 93.70  ?  655 GLY A O     1 
ATOM   3841 N N     . PHE A 1 675 ? 5.350   62.172  85.217  1.00 93.94  ?  656 PHE A N     1 
ATOM   3842 C CA    . PHE A 1 675 ? 4.083   62.542  84.625  1.00 93.92  ?  656 PHE A CA    1 
ATOM   3843 C C     . PHE A 1 675 ? 4.239   62.254  83.137  1.00 94.48  ?  656 PHE A C     1 
ATOM   3844 O O     . PHE A 1 675 ? 5.267   62.606  82.536  1.00 91.60  ?  656 PHE A O     1 
ATOM   3845 C CB    . PHE A 1 675 ? 3.734   64.001  84.956  1.00 87.26  ?  656 PHE A CB    1 
ATOM   3846 C CG    . PHE A 1 675 ? 2.248   64.294  84.972  1.00 84.94  ?  656 PHE A CG    1 
ATOM   3847 C CD1   . PHE A 1 675 ? 1.391   63.521  85.732  1.00 90.15  ?  656 PHE A CD1   1 
ATOM   3848 C CD2   . PHE A 1 675 ? 1.728   65.415  84.359  1.00 88.70  ?  656 PHE A CD2   1 
ATOM   3849 C CE1   . PHE A 1 675 ? 0.018   63.801  85.792  1.00 89.94  ?  656 PHE A CE1   1 
ATOM   3850 C CE2   . PHE A 1 675 ? 0.351   65.710  84.434  1.00 88.14  ?  656 PHE A CE2   1 
ATOM   3851 C CZ    . PHE A 1 675 ? -0.498  64.897  85.148  1.00 83.20  ?  656 PHE A CZ    1 
ATOM   3852 N N     . GLY A 1 676 ? 3.287   61.487  82.596  1.00 91.83  ?  657 GLY A N     1 
ATOM   3853 C CA    . GLY A 1 676 ? 3.259   61.125  81.203  1.00 91.03  ?  657 GLY A CA    1 
ATOM   3854 C C     . GLY A 1 676 ? 2.065   61.725  80.484  1.00 91.08  ?  657 GLY A C     1 
ATOM   3855 O O     . GLY A 1 676 ? 1.337   62.558  81.029  1.00 83.80  ?  657 GLY A O     1 
ATOM   3856 N N     . ASN A 1 677 ? 1.871   61.264  79.234  1.00 95.69  ?  658 ASN A N     1 
ATOM   3857 C CA    . ASN A 1 677 ? 0.928   61.875  78.296  1.00 90.91  ?  658 ASN A CA    1 
ATOM   3858 C C     . ASN A 1 677 ? 0.106   60.819  77.547  1.00 88.08  ?  658 ASN A C     1 
ATOM   3859 O O     . ASN A 1 677 ? 0.606   59.747  77.176  1.00 90.66  ?  658 ASN A O     1 
ATOM   3860 C CB    . ASN A 1 677 ? 1.677   62.805  77.307  1.00 87.81  ?  658 ASN A CB    1 
ATOM   3861 C CG    . ASN A 1 677 ? 0.729   63.685  76.455  1.00 93.58  ?  658 ASN A CG    1 
ATOM   3862 O OD1   . ASN A 1 677 ? -0.464  63.841  76.761  1.00 89.54  ?  658 ASN A OD1   1 
ATOM   3863 N ND2   . ASN A 1 677 ? 1.296   64.332  75.429  1.00 94.89  ?  658 ASN A ND2   1 
ATOM   3864 N N     . LEU A 1 678 ? -1.174  61.137  77.353  1.00 84.66  ?  659 LEU A N     1 
ATOM   3865 C CA    . LEU A 1 678 ? -2.163  60.288  76.697  1.00 89.99  ?  659 LEU A CA    1 
ATOM   3866 C C     . LEU A 1 678 ? -3.198  61.231  76.102  1.00 98.79  ?  659 LEU A C     1 
ATOM   3867 O O     . LEU A 1 678 ? -3.597  62.170  76.796  1.00 99.87  ?  659 LEU A O     1 
ATOM   3868 C CB    . LEU A 1 678 ? -2.864  59.368  77.687  1.00 90.93  ?  659 LEU A CB    1 
ATOM   3869 C CG    . LEU A 1 678 ? -3.921  58.537  76.975  1.00 93.79  ?  659 LEU A CG    1 
ATOM   3870 C CD1   . LEU A 1 678 ? -3.168  57.560  76.074  1.00 100.98 ?  659 LEU A CD1   1 
ATOM   3871 C CD2   . LEU A 1 678 ? -4.959  57.868  77.888  1.00 101.08 ?  659 LEU A CD2   1 
ATOM   3872 N N     . ASN A 1 679 ? -3.644  60.994  74.854  1.00 98.38  ?  660 ASN A N     1 
ATOM   3873 C CA    . ASN A 1 679 ? -4.584  61.886  74.166  1.00 89.76  ?  660 ASN A CA    1 
ATOM   3874 C C     . ASN A 1 679 ? -5.700  61.110  73.477  1.00 88.42  ?  660 ASN A C     1 
ATOM   3875 O O     . ASN A 1 679 ? -5.526  59.950  73.109  1.00 96.85  ?  660 ASN A O     1 
ATOM   3876 C CB    . ASN A 1 679 ? -3.839  62.765  73.172  1.00 88.04  ?  660 ASN A CB    1 
ATOM   3877 C CG    . ASN A 1 679 ? -3.252  63.999  73.825  1.00 93.76  ?  660 ASN A CG    1 
ATOM   3878 O OD1   . ASN A 1 679 ? -3.976  64.784  74.451  1.00 87.49  ?  660 ASN A OD1   1 
ATOM   3879 N ND2   . ASN A 1 679 ? -1.930  64.142  73.749  1.00 96.92  ?  660 ASN A ND2   1 
ATOM   3880 N N     . LYS A 1 680 ? -6.868  61.754  73.313  1.00 85.26  ?  661 LYS A N     1 
ATOM   3881 C CA    . LYS A 1 680 ? -8.028  61.117  72.676  1.00 94.98  ?  661 LYS A CA    1 
ATOM   3882 C C     . LYS A 1 680 ? -8.562  61.946  71.509  1.00 105.31 ?  661 LYS A C     1 
ATOM   3883 O O     . LYS A 1 680 ? -8.694  63.170  71.630  1.00 111.85 ?  661 LYS A O     1 
ATOM   3884 C CB    . LYS A 1 680 ? -9.180  60.886  73.669  1.00 89.32  ?  661 LYS A CB    1 
ATOM   3885 C CG    . LYS A 1 680 ? -8.786  59.972  74.778  1.00 98.97  ?  661 LYS A CG    1 
ATOM   3886 C CD    . LYS A 1 680 ? -9.903  59.699  75.785  1.00 103.59 ?  661 LYS A CD    1 
ATOM   3887 C CE    . LYS A 1 680 ? -9.402  58.661  76.800  1.00 103.76 ?  661 LYS A CE    1 
ATOM   3888 N NZ    . LYS A 1 680 ? -10.336 58.353  77.880  1.00 102.98 ?  661 LYS A NZ    1 
ATOM   3889 N N     . VAL A 1 681 ? -8.895  61.276  70.389  1.00 105.49 ?  662 VAL A N     1 
ATOM   3890 C CA    . VAL A 1 681 ? -9.597  61.887  69.254  1.00 100.77 ?  662 VAL A CA    1 
ATOM   3891 C C     . VAL A 1 681 ? -11.043 61.407  69.298  1.00 101.62 ?  662 VAL A C     1 
ATOM   3892 O O     . VAL A 1 681 ? -11.292 60.199  69.416  1.00 105.24 ?  662 VAL A O     1 
ATOM   3893 C CB    . VAL A 1 681 ? -8.967  61.509  67.901  1.00 91.24  ?  662 VAL A CB    1 
ATOM   3894 C CG1   . VAL A 1 681 ? -9.543  62.394  66.823  1.00 94.16  ?  662 VAL A CG1   1 
ATOM   3895 C CG2   . VAL A 1 681 ? -7.440  61.525  67.939  1.00 88.58  ?  662 VAL A CG2   1 
ATOM   3896 N N     . VAL A 1 682 ? -11.998 62.332  69.211  1.00 97.78  ?  663 VAL A N     1 
ATOM   3897 C CA    . VAL A 1 682 ? -13.410 61.956  69.223  1.00 104.06 ?  663 VAL A CA    1 
ATOM   3898 C C     . VAL A 1 682 ? -14.011 62.244  67.855  1.00 112.99 ?  663 VAL A C     1 
ATOM   3899 O O     . VAL A 1 682 ? -13.758 63.301  67.263  1.00 115.45 ?  663 VAL A O     1 
ATOM   3900 C CB    . VAL A 1 682 ? -14.193 62.647  70.350  1.00 102.82 ?  663 VAL A CB    1 
ATOM   3901 C CG1   . VAL A 1 682 ? -15.674 62.318  70.239  1.00 102.71 ?  663 VAL A CG1   1 
ATOM   3902 C CG2   . VAL A 1 682 ? -13.688 62.136  71.673  1.00 105.09 ?  663 VAL A CG2   1 
ATOM   3903 N N     . LEU A 1 683 ? -14.805 61.287  67.358  1.00 118.21 ?  664 LEU A N     1 
ATOM   3904 C CA    . LEU A 1 683 ? -15.316 61.233  65.988  1.00 112.71 ?  664 LEU A CA    1 
ATOM   3905 C C     . LEU A 1 683 ? -16.822 61.007  66.101  1.00 114.65 ?  664 LEU A C     1 
ATOM   3906 O O     . LEU A 1 683 ? -17.261 59.930  66.533  1.00 112.32 ?  664 LEU A O     1 
ATOM   3907 C CB    . LEU A 1 683 ? -14.616 60.102  65.221  1.00 110.81 ?  664 LEU A CB    1 
ATOM   3908 C CG    . LEU A 1 683 ? -13.074 60.186  65.179  1.00 109.57 ?  664 LEU A CG    1 
ATOM   3909 C CD1   . LEU A 1 683 ? -12.395 58.923  64.662  1.00 105.87 ?  664 LEU A CD1   1 
ATOM   3910 C CD2   . LEU A 1 683 ? -12.646 61.353  64.302  1.00 107.47 ?  664 LEU A CD2   1 
ATOM   3911 N N     . CYS A 1 684 ? -17.612 62.039  65.766  1.00 115.38 ?  665 CYS A N     1 
ATOM   3912 C CA    . CYS A 1 684 ? -19.063 62.047  65.991  1.00 121.19 ?  665 CYS A CA    1 
ATOM   3913 C C     . CYS A 1 684 ? -19.812 61.944  64.673  1.00 126.83 ?  665 CYS A C     1 
ATOM   3914 O O     . CYS A 1 684 ? -20.018 62.953  63.990  1.00 130.82 ?  665 CYS A O     1 
ATOM   3915 C CB    . CYS A 1 684 ? -19.506 63.295  66.741  1.00 123.00 ?  665 CYS A CB    1 
ATOM   3916 S SG    . CYS A 1 684 ? -18.884 63.403  68.415  1.00 132.10 ?  665 CYS A SG    1 
ATOM   3917 N N     . PHE A 1 685 ? -20.264 60.733  64.348  1.00 128.69 ?  666 PHE A N     1 
ATOM   3918 C CA    . PHE A 1 685 ? -20.947 60.489  63.089  1.00 131.52 ?  666 PHE A CA    1 
ATOM   3919 C C     . PHE A 1 685 ? -22.455 60.625  63.268  1.00 137.06 ?  666 PHE A C     1 
ATOM   3920 O O     . PHE A 1 685 ? -22.962 60.937  64.352  1.00 137.38 ?  666 PHE A O     1 
ATOM   3921 C CB    . PHE A 1 685 ? -20.562 59.118  62.544  1.00 123.39 ?  666 PHE A CB    1 
ATOM   3922 C CG    . PHE A 1 685 ? -19.091 58.938  62.428  1.00 119.12 ?  666 PHE A CG    1 
ATOM   3923 C CD1   . PHE A 1 685 ? -18.361 59.733  61.555  1.00 118.41 ?  666 PHE A CD1   1 
ATOM   3924 C CD2   . PHE A 1 685 ? -18.427 57.998  63.197  1.00 115.09 ?  666 PHE A CD2   1 
ATOM   3925 C CE1   . PHE A 1 685 ? -16.991 59.594  61.441  1.00 115.57 ?  666 PHE A CE1   1 
ATOM   3926 C CE2   . PHE A 1 685 ? -17.049 57.847  63.088  1.00 114.96 ?  666 PHE A CE2   1 
ATOM   3927 C CZ    . PHE A 1 685 ? -16.330 58.650  62.204  1.00 113.29 ?  666 PHE A CZ    1 
ATOM   3928 N N     . ASP A 1 686 ? -23.180 60.399  62.178  1.00 137.51 ?  667 ASP A N     1 
ATOM   3929 C CA    . ASP A 1 686 ? -24.635 60.453  62.164  1.00 138.45 ?  667 ASP A CA    1 
ATOM   3930 C C     . ASP A 1 686 ? -25.305 59.080  62.070  1.00 137.06 ?  667 ASP A C     1 
ATOM   3931 O O     . ASP A 1 686 ? -26.535 59.015  61.977  1.00 136.72 ?  667 ASP A O     1 
ATOM   3932 C CB    . ASP A 1 686 ? -25.089 61.361  61.018  1.00 137.46 ?  667 ASP A CB    1 
ATOM   3933 C CG    . ASP A 1 686 ? -24.438 60.992  59.707  1.00 141.24 ?  667 ASP A CG    1 
ATOM   3934 O OD1   . ASP A 1 686 ? -23.549 60.107  59.711  1.00 141.62 ?  667 ASP A OD1   1 
ATOM   3935 O OD2   . ASP A 1 686 ? -24.844 61.547  58.669  1.00 145.57 ?  667 ASP A OD2   1 
ATOM   3936 N N     . ARG A 1 687 ? -24.537 57.990  62.120  1.00 136.48 ?  668 ARG A N     1 
ATOM   3937 C CA    . ARG A 1 687 ? -25.080 56.634  62.105  1.00 132.88 ?  668 ARG A CA    1 
ATOM   3938 C C     . ARG A 1 687 ? -23.944 55.659  62.334  1.00 125.64 ?  668 ARG A C     1 
ATOM   3939 O O     . ARG A 1 687 ? -22.786 55.931  61.988  1.00 123.40 ?  668 ARG A O     1 
ATOM   3940 C CB    . ARG A 1 687 ? -25.758 56.325  60.778  1.00 138.88 ?  668 ARG A CB    1 
ATOM   3941 C CG    . ARG A 1 687 ? -24.777 56.517  59.660  1.00 140.94 ?  668 ARG A CG    1 
ATOM   3942 C CD    . ARG A 1 687 ? -25.444 57.081  58.457  1.00 145.01 ?  668 ARG A CD    1 
ATOM   3943 N NE    . ARG A 1 687 ? -24.546 57.142  57.318  1.00 149.18 ?  668 ARG A NE    1 
ATOM   3944 C CZ    . ARG A 1 687 ? -24.780 57.894  56.250  1.00 155.52 ?  668 ARG A CZ    1 
ATOM   3945 N NH1   . ARG A 1 687 ? -25.853 58.677  56.227  1.00 150.45 ?  668 ARG A NH1   1 
ATOM   3946 N NH2   . ARG A 1 687 ? -23.927 57.897  55.231  1.00 161.73 ?  668 ARG A NH2   1 
ATOM   3947 N N     . VAL A 1 688 ? -24.289 54.522  62.905  1.00 123.55 ?  669 VAL A N     1 
ATOM   3948 C CA    . VAL A 1 688 ? -23.284 53.527  63.247  1.00 129.41 ?  669 VAL A CA    1 
ATOM   3949 C C     . VAL A 1 688 ? -22.849 52.807  61.976  1.00 124.06 ?  669 VAL A C     1 
ATOM   3950 O O     . VAL A 1 688 ? -23.685 52.387  61.166  1.00 119.77 ?  669 VAL A O     1 
ATOM   3951 C CB    . VAL A 1 688 ? -23.830 52.542  64.298  1.00 126.01 ?  669 VAL A CB    1 
ATOM   3952 C CG1   . VAL A 1 688 ? -22.825 51.429  64.588  1.00 124.27 ?  669 VAL A CG1   1 
ATOM   3953 C CG2   . VAL A 1 688 ? -24.188 53.271  65.566  1.00 119.43 ?  669 VAL A CG2   1 
ATOM   3954 N N     . PHE A 1 689 ? -21.535 52.671  61.799  1.00 117.49 ?  670 PHE A N     1 
ATOM   3955 C CA    . PHE A 1 689 ? -20.975 51.851  60.740  1.00 114.22 ?  670 PHE A CA    1 
ATOM   3956 C C     . PHE A 1 689 ? -19.959 50.853  61.288  1.00 115.78 ?  670 PHE A C     1 
ATOM   3957 O O     . PHE A 1 689 ? -19.041 50.437  60.580  1.00 114.87 ?  670 PHE A O     1 
ATOM   3958 C CB    . PHE A 1 689 ? -20.329 52.717  59.665  1.00 121.45 ?  670 PHE A CB    1 
ATOM   3959 C CG    . PHE A 1 689 ? -19.116 53.474  60.129  1.00 116.67 ?  670 PHE A CG    1 
ATOM   3960 C CD1   . PHE A 1 689 ? -17.838 52.930  59.963  1.00 116.08 ?  670 PHE A CD1   1 
ATOM   3961 C CD2   . PHE A 1 689 ? -19.237 54.735  60.667  1.00 115.86 ?  670 PHE A CD2   1 
ATOM   3962 C CE1   . PHE A 1 689 ? -16.715 53.597  60.362  1.00 113.50 ?  670 PHE A CE1   1 
ATOM   3963 C CE2   . PHE A 1 689 ? -18.112 55.417  61.063  1.00 121.80 ?  670 PHE A CE2   1 
ATOM   3964 C CZ    . PHE A 1 689 ? -16.844 54.843  60.913  1.00 119.44 ?  670 PHE A CZ    1 
ATOM   3965 N N     . TRP A 1 690 ? -20.097 50.467  62.547  1.00 117.89 ?  671 TRP A N     1 
ATOM   3966 C CA    . TRP A 1 690 ? -19.168 49.554  63.202  1.00 121.60 ?  671 TRP A CA    1 
ATOM   3967 C C     . TRP A 1 690 ? -19.961 48.425  63.846  1.00 120.68 ?  671 TRP A C     1 
ATOM   3968 O O     . TRP A 1 690 ? -21.196 48.451  63.885  1.00 118.66 ?  671 TRP A O     1 
ATOM   3969 C CB    . TRP A 1 690 ? -18.294 50.288  64.247  1.00 128.37 ?  671 TRP A CB    1 
ATOM   3970 C CG    . TRP A 1 690 ? -19.108 51.187  65.178  1.00 128.97 ?  671 TRP A CG    1 
ATOM   3971 C CD1   . TRP A 1 690 ? -19.677 50.840  66.383  1.00 128.30 ?  671 TRP A CD1   1 
ATOM   3972 C CD2   . TRP A 1 690 ? -19.421 52.577  64.975  1.00 122.03 ?  671 TRP A CD2   1 
ATOM   3973 N NE1   . TRP A 1 690 ? -20.344 51.918  66.913  1.00 127.78 ?  671 TRP A NE1   1 
ATOM   3974 C CE2   . TRP A 1 690 ? -20.199 52.994  66.072  1.00 122.94 ?  671 TRP A CE2   1 
ATOM   3975 C CE3   . TRP A 1 690 ? -19.131 53.502  63.963  1.00 123.00 ?  671 TRP A CE3   1 
ATOM   3976 C CZ2   . TRP A 1 690 ? -20.684 54.296  66.186  1.00 125.34 ?  671 TRP A CZ2   1 
ATOM   3977 C CZ3   . TRP A 1 690 ? -19.618 54.794  64.077  1.00 120.29 ?  671 TRP A CZ3   1 
ATOM   3978 C CH2   . TRP A 1 690 ? -20.384 55.177  65.176  1.00 124.22 ?  671 TRP A CH2   1 
ATOM   3979 N N     . ASP A 1 691 ? -19.255 47.423  64.342  1.00 115.37 ?  672 ASP A N     1 
ATOM   3980 C CA    . ASP A 1 691 ? -19.993 46.387  65.034  1.00 123.56 ?  672 ASP A CA    1 
ATOM   3981 C C     . ASP A 1 691 ? -20.514 46.961  66.345  1.00 132.82 ?  672 ASP A C     1 
ATOM   3982 O O     . ASP A 1 691 ? -19.703 47.264  67.232  1.00 137.26 ?  672 ASP A O     1 
ATOM   3983 C CB    . ASP A 1 691 ? -19.116 45.170  65.285  1.00 129.26 ?  672 ASP A CB    1 
ATOM   3984 C CG    . ASP A 1 691 ? -19.934 43.929  65.623  1.00 137.38 ?  672 ASP A CG    1 
ATOM   3985 O OD1   . ASP A 1 691 ? -21.065 44.089  66.147  1.00 132.28 ?  672 ASP A OD1   1 
ATOM   3986 O OD2   . ASP A 1 691 ? -19.443 42.799  65.369  1.00 141.63 ?  672 ASP A OD2   1 
ATOM   3987 N N     . PRO A 1 692 ? -21.833 47.131  66.520  1.00 134.40 ?  673 PRO A N     1 
ATOM   3988 C CA    . PRO A 1 692 ? -22.320 47.851  67.715  1.00 135.86 ?  673 PRO A CA    1 
ATOM   3989 C C     . PRO A 1 692 ? -22.152 47.063  69.005  1.00 136.84 ?  673 PRO A C     1 
ATOM   3990 O O     . PRO A 1 692 ? -21.963 47.673  70.068  1.00 131.68 ?  673 PRO A O     1 
ATOM   3991 C CB    . PRO A 1 692 ? -23.807 48.102  67.403  1.00 127.82 ?  673 PRO A CB    1 
ATOM   3992 C CG    . PRO A 1 692 ? -23.991 47.711  65.962  1.00 131.41 ?  673 PRO A CG    1 
ATOM   3993 C CD    . PRO A 1 692 ? -22.944 46.680  65.672  1.00 130.57 ?  673 PRO A CD    1 
ATOM   3994 N N     . SER A 1 693 ? -22.222 45.730  68.942  1.00 136.08 ?  674 SER A N     1 
ATOM   3995 C CA    . SER A 1 693 ? -22.032 44.882  70.111  1.00 137.14 ?  674 SER A CA    1 
ATOM   3996 C C     . SER A 1 693 ? -20.564 44.668  70.448  1.00 135.35 ?  674 SER A C     1 
ATOM   3997 O O     . SER A 1 693 ? -20.265 43.957  71.419  1.00 135.45 ?  674 SER A O     1 
ATOM   3998 C CB    . SER A 1 693 ? -22.710 43.518  69.911  1.00 147.40 ?  674 SER A CB    1 
ATOM   3999 O OG    . SER A 1 693 ? -22.233 42.860  68.743  1.00 156.09 ?  674 SER A OG    1 
ATOM   4000 N N     . VAL A 1 694 ? -19.646 45.235  69.671  1.00 129.22 ?  675 VAL A N     1 
ATOM   4001 C CA    . VAL A 1 694 ? -18.243 45.294  70.055  1.00 129.51 ?  675 VAL A CA    1 
ATOM   4002 C C     . VAL A 1 694 ? -17.955 46.706  70.547  1.00 128.26 ?  675 VAL A C     1 
ATOM   4003 O O     . VAL A 1 694 ? -18.211 47.690  69.837  1.00 125.15 ?  675 VAL A O     1 
ATOM   4004 C CB    . VAL A 1 694 ? -17.313 44.886  68.905  1.00 127.88 ?  675 VAL A CB    1 
ATOM   4005 C CG1   . VAL A 1 694 ? -15.860 45.033  69.326  1.00 122.32 ?  675 VAL A CG1   1 
ATOM   4006 C CG2   . VAL A 1 694 ? -17.588 43.443  68.523  1.00 131.04 ?  675 VAL A CG2   1 
ATOM   4007 N N     . ASN A 1 695 ? -17.465 46.797  71.791  1.00 128.30 ?  676 ASN A N     1 
ATOM   4008 C CA    . ASN A 1 695 ? -17.174 48.070  72.432  1.00 118.21 ?  676 ASN A CA    1 
ATOM   4009 C C     . ASN A 1 695 ? -15.831 48.634  72.027  1.00 117.09 ?  676 ASN A C     1 
ATOM   4010 O O     . ASN A 1 695 ? -15.602 49.828  72.237  1.00 116.64 ?  676 ASN A O     1 
ATOM   4011 C CB    . ASN A 1 695 ? -17.209 47.921  73.949  1.00 114.97 ?  676 ASN A CB    1 
ATOM   4012 C CG    . ASN A 1 695 ? -18.599 47.660  74.470  1.00 123.30 ?  676 ASN A CG    1 
ATOM   4013 O OD1   . ASN A 1 695 ? -18.831 46.692  75.209  1.00 125.72 ?  676 ASN A OD1   1 
ATOM   4014 N ND2   . ASN A 1 695 ? -19.543 48.521  74.086  1.00 120.31 ?  676 ASN A ND2   1 
ATOM   4015 N N     . LEU A 1 696 ? -14.953 47.819  71.441  1.00 116.88 ?  677 LEU A N     1 
ATOM   4016 C CA    . LEU A 1 696 ? -13.614 48.304  71.130  1.00 113.41 ?  677 LEU A CA    1 
ATOM   4017 C C     . LEU A 1 696 ? -12.839 47.324  70.256  1.00 114.05 ?  677 LEU A C     1 
ATOM   4018 O O     . LEU A 1 696 ? -13.036 46.107  70.322  1.00 117.55 ?  677 LEU A O     1 
ATOM   4019 C CB    . LEU A 1 696 ? -12.846 48.608  72.409  1.00 110.88 ?  677 LEU A CB    1 
ATOM   4020 C CG    . LEU A 1 696 ? -12.355 47.490  73.290  1.00 113.79 ?  677 LEU A CG    1 
ATOM   4021 C CD1   . LEU A 1 696 ? -11.368 48.157  74.162  1.00 115.90 ?  677 LEU A CD1   1 
ATOM   4022 C CD2   . LEU A 1 696 ? -13.522 46.994  74.137  1.00 114.20 ?  677 LEU A CD2   1 
ATOM   4023 N N     . PHE A 1 697 ? -11.950 47.894  69.436  1.00 112.61 ?  678 PHE A N     1 
ATOM   4024 C CA    . PHE A 1 697 ? -11.155 47.172  68.447  1.00 108.05 ?  678 PHE A CA    1 
ATOM   4025 C C     . PHE A 1 697 ? -9.846  47.908  68.189  1.00 103.59 ?  678 PHE A C     1 
ATOM   4026 O O     . PHE A 1 697 ? -9.752  49.125  68.362  1.00 107.09 ?  678 PHE A O     1 
ATOM   4027 C CB    . PHE A 1 697 ? -11.903 47.004  67.127  1.00 105.43 ?  678 PHE A CB    1 
ATOM   4028 C CG    . PHE A 1 697 ? -12.344 48.288  66.497  1.00 100.19 ?  678 PHE A CG    1 
ATOM   4029 C CD1   . PHE A 1 697 ? -13.652 48.729  66.647  1.00 102.38 ?  678 PHE A CD1   1 
ATOM   4030 C CD2   . PHE A 1 697 ? -11.462 49.046  65.730  1.00 99.67  ?  678 PHE A CD2   1 
ATOM   4031 C CE1   . PHE A 1 697 ? -14.080 49.914  66.038  1.00 107.73 ?  678 PHE A CE1   1 
ATOM   4032 C CE2   . PHE A 1 697 ? -11.873 50.229  65.120  1.00 102.34 ?  678 PHE A CE2   1 
ATOM   4033 C CZ    . PHE A 1 697 ? -13.186 50.670  65.280  1.00 105.36 ?  678 PHE A CZ    1 
ATOM   4034 N N     . GLY A 1 698 ? -8.843  47.161  67.727  1.00 101.16 ?  679 GLY A N     1 
ATOM   4035 C CA    . GLY A 1 698 ? -7.492  47.663  67.615  1.00 100.93 ?  679 GLY A CA    1 
ATOM   4036 C C     . GLY A 1 698 ? -7.169  48.246  66.247  1.00 106.37 ?  679 GLY A C     1 
ATOM   4037 O O     . GLY A 1 698 ? -8.043  48.524  65.423  1.00 106.28 ?  679 GLY A O     1 
ATOM   4038 N N     . HIS A 1 699 ? -5.870  48.484  66.047  1.00 108.31 ?  680 HIS A N     1 
ATOM   4039 C CA    . HIS A 1 699 ? -5.231  48.910  64.798  1.00 102.67 ?  680 HIS A CA    1 
ATOM   4040 C C     . HIS A 1 699 ? -3.739  48.715  64.957  1.00 103.46 ?  680 HIS A C     1 
ATOM   4041 O O     . HIS A 1 699 ? -3.116  49.338  65.827  1.00 103.41 ?  680 HIS A O     1 
ATOM   4042 C CB    . HIS A 1 699 ? -5.510  50.351  64.440  1.00 99.31  ?  680 HIS A CB    1 
ATOM   4043 C CG    . HIS A 1 699 ? -4.585  50.868  63.385  1.00 104.84 ?  680 HIS A CG    1 
ATOM   4044 N ND1   . HIS A 1 699 ? -4.836  50.749  62.038  1.00 107.14 ?  680 HIS A ND1   1 
ATOM   4045 C CD2   . HIS A 1 699 ? -3.389  51.499  63.491  1.00 109.38 ?  680 HIS A CD2   1 
ATOM   4046 C CE1   . HIS A 1 699 ? -3.842  51.298  61.359  1.00 111.12 ?  680 HIS A CE1   1 
ATOM   4047 N NE2   . HIS A 1 699 ? -2.950  51.761  62.217  1.00 107.67 ?  680 HIS A NE2   1 
ATOM   4048 N N     . VAL A 1 700 ? -3.175  47.887  64.148  1.00 104.59 ?  681 VAL A N     1 
ATOM   4049 C CA    . VAL A 1 700 ? -1.754  47.634  64.281  1.00 108.73 ?  681 VAL A CA    1 
ATOM   4050 C C     . VAL A 1 700 ? -1.032  48.682  63.437  1.00 108.73 ?  681 VAL A C     1 
ATOM   4051 O O     . VAL A 1 700 ? -1.513  49.101  62.376  1.00 99.51  ?  681 VAL A O     1 
ATOM   4052 C CB    . VAL A 1 700 ? -1.409  46.182  63.891  1.00 105.82 ?  681 VAL A CB    1 
ATOM   4053 C CG1   . VAL A 1 700 ? 0.053   45.921  64.097  1.00 103.36 ?  681 VAL A CG1   1 
ATOM   4054 C CG2   . VAL A 1 700 ? -2.261  45.174  64.691  1.00 98.14  ?  681 VAL A CG2   1 
ATOM   4055 N N     . GLY A 1 701 ? 0.083   49.173  63.963  1.00 118.98 ?  682 GLY A N     1 
ATOM   4056 C CA    . GLY A 1 701 ? 0.779   50.307  63.392  1.00 119.11 ?  682 GLY A CA    1 
ATOM   4057 C C     . GLY A 1 701 ? 1.973   49.857  62.578  1.00 123.49 ?  682 GLY A C     1 
ATOM   4058 O O     . GLY A 1 701 ? 2.558   48.796  62.823  1.00 121.23 ?  682 GLY A O     1 
ATOM   4059 N N     . SER A 1 702 ? 2.356   50.716  61.635  1.00 126.87 ?  683 SER A N     1 
ATOM   4060 C CA    . SER A 1 702 ? 3.163   50.276  60.502  1.00 128.41 ?  683 SER A CA    1 
ATOM   4061 C C     . SER A 1 702 ? 4.614   50.048  60.887  1.00 126.55 ?  683 SER A C     1 
ATOM   4062 O O     . SER A 1 702 ? 5.234   49.070  60.456  1.00 125.61 ?  683 SER A O     1 
ATOM   4063 C CB    . SER A 1 702 ? 3.056   51.305  59.394  1.00 134.27 ?  683 SER A CB    1 
ATOM   4064 O OG    . SER A 1 702 ? 1.689   51.469  59.071  1.00 144.09 ?  683 SER A OG    1 
ATOM   4065 N N     . THR A 1 703 ? 5.175   50.931  61.672  1.00 125.30 ?  684 THR A N     1 
ATOM   4066 C CA    . THR A 1 703 ? 6.479   50.672  62.239  1.00 128.42 ?  684 THR A CA    1 
ATOM   4067 C C     . THR A 1 703 ? 6.332   50.523  63.761  1.00 125.33 ?  684 THR A C     1 
ATOM   4068 O O     . THR A 1 703 ? 5.212   50.425  64.291  1.00 119.78 ?  684 THR A O     1 
ATOM   4069 C CB    . THR A 1 703 ? 7.422   51.795  61.809  1.00 128.37 ?  684 THR A CB    1 
ATOM   4070 O OG1   . THR A 1 703 ? 8.775   51.474  62.175  1.00 131.45 ?  684 THR A OG1   1 
ATOM   4071 C CG2   . THR A 1 703 ? 6.972   53.106  62.430  1.00 121.91 ?  684 THR A CG2   1 
ATOM   4072 N N     . THR A 1 704 ? 7.470   50.463  64.468  1.00 126.29 ?  685 THR A N     1 
ATOM   4073 C CA    . THR A 1 704 ? 7.444   50.599  65.926  1.00 116.96 ?  685 THR A CA    1 
ATOM   4074 C C     . THR A 1 704 ? 7.088   52.023  66.337  1.00 114.24 ?  685 THR A C     1 
ATOM   4075 O O     . THR A 1 704 ? 6.188   52.234  67.158  1.00 111.69 ?  685 THR A O     1 
ATOM   4076 C CB    . THR A 1 704 ? 8.788   50.175  66.549  1.00 112.78 ?  685 THR A CB    1 
ATOM   4077 O OG1   . THR A 1 704 ? 9.101   48.814  66.212  1.00 109.22 ?  685 THR A OG1   1 
ATOM   4078 C CG2   . THR A 1 704 ? 8.767   50.338  68.055  1.00 114.14 ?  685 THR A CG2   1 
ATOM   4079 N N     . ALA A 1 705 ? 7.759   53.015  65.748  1.00 113.36 ?  686 ALA A N     1 
ATOM   4080 C CA    . ALA A 1 705 ? 7.624   54.395  66.203  1.00 110.77 ?  686 ALA A CA    1 
ATOM   4081 C C     . ALA A 1 705 ? 6.205   54.938  66.099  1.00 113.04 ?  686 ALA A C     1 
ATOM   4082 O O     . ALA A 1 705 ? 5.919   56.000  66.668  1.00 112.39 ?  686 ALA A O     1 
ATOM   4083 C CB    . ALA A 1 705 ? 8.556   55.289  65.400  1.00 116.87 ?  686 ALA A CB    1 
ATOM   4084 N N     . SER A 1 706 ? 5.320   54.271  65.360  1.00 113.91 ?  687 SER A N     1 
ATOM   4085 C CA    . SER A 1 706 ? 3.928   54.689  65.277  1.00 113.19 ?  687 SER A CA    1 
ATOM   4086 C C     . SER A 1 706 ? 3.007   53.735  66.025  1.00 111.34 ?  687 SER A C     1 
ATOM   4087 O O     . SER A 1 706 ? 1.804   53.700  65.738  1.00 112.98 ?  687 SER A O     1 
ATOM   4088 C CB    . SER A 1 706 ? 3.489   54.820  63.813  1.00 118.43 ?  687 SER A CB    1 
ATOM   4089 O OG    . SER A 1 706 ? 3.666   53.606  63.080  1.00 124.33 ?  687 SER A OG    1 
ATOM   4090 N N     . ARG A 1 707 ? 3.545   52.959  66.981  1.00 107.39 ?  688 ARG A N     1 
ATOM   4091 C CA    . ARG A 1 707 ? 2.755   51.863  67.543  1.00 108.04 ?  688 ARG A CA    1 
ATOM   4092 C C     . ARG A 1 707 ? 1.571   52.390  68.341  1.00 104.43 ?  688 ARG A C     1 
ATOM   4093 O O     . ARG A 1 707 ? 0.503   51.761  68.371  1.00 102.36 ?  688 ARG A O     1 
ATOM   4094 C CB    . ARG A 1 707 ? 3.628   50.905  68.382  1.00 103.53 ?  688 ARG A CB    1 
ATOM   4095 C CG    . ARG A 1 707 ? 4.316   51.413  69.651  1.00 98.66  ?  688 ARG A CG    1 
ATOM   4096 C CD    . ARG A 1 707 ? 5.193   50.295  70.232  1.00 95.26  ?  688 ARG A CD    1 
ATOM   4097 N NE    . ARG A 1 707 ? 6.085   50.703  71.319  1.00 97.03  ?  688 ARG A NE    1 
ATOM   4098 C CZ    . ARG A 1 707 ? 7.098   49.964  71.790  1.00 103.83 ?  688 ARG A CZ    1 
ATOM   4099 N NH1   . ARG A 1 707 ? 7.376   48.783  71.262  1.00 106.08 ?  688 ARG A NH1   1 
ATOM   4100 N NH2   . ARG A 1 707 ? 7.855   50.397  72.795  1.00 107.11 ?  688 ARG A NH2   1 
ATOM   4101 N N     . GLY A 1 708 ? 1.712   53.556  68.938  1.00 103.46 ?  689 GLY A N     1 
ATOM   4102 C CA    . GLY A 1 708 ? 0.539   54.091  69.576  1.00 102.57 ?  689 GLY A CA    1 
ATOM   4103 C C     . GLY A 1 708 ? -0.291  55.013  68.720  1.00 103.77 ?  689 GLY A C     1 
ATOM   4104 O O     . GLY A 1 708 ? -1.268  55.574  69.217  1.00 104.59 ?  689 GLY A O     1 
ATOM   4105 N N     . GLU A 1 709 ? 0.103   55.257  67.476  1.00 106.18 ?  690 GLU A N     1 
ATOM   4106 C CA    . GLU A 1 709 ? -0.652  56.258  66.679  1.00 102.70 ?  690 GLU A CA    1 
ATOM   4107 C C     . GLU A 1 709 ? -2.048  55.748  66.378  1.00 98.76  ?  690 GLU A C     1 
ATOM   4108 O O     . GLU A 1 709 ? -2.165  54.891  65.555  1.00 106.19 ?  690 GLU A O     1 
ATOM   4109 C CB    . GLU A 1 709 ? 0.063   56.599  65.379  1.00 102.67 ?  690 GLU A CB    1 
ATOM   4110 C CG    . GLU A 1 709 ? 0.292   58.085  65.217  1.00 100.53 ?  690 GLU A CG    1 
ATOM   4111 C CD    . GLU A 1 709 ? 1.316   58.434  64.162  1.00 113.36 ?  690 GLU A CD    1 
ATOM   4112 O OE1   . GLU A 1 709 ? 2.410   58.920  64.509  1.00 105.37 ?  690 GLU A OE1   1 
ATOM   4113 O OE2   . GLU A 1 709 ? 1.019   58.190  63.001  1.00 120.42 ?  690 GLU A OE2   1 
ATOM   4114 N N     . LEU A 1 710 ? -3.041  56.212  67.120  1.00 93.33  ?  691 LEU A N     1 
ATOM   4115 C CA    . LEU A 1 710 ? -4.464  55.821  66.959  1.00 94.13  ?  691 LEU A CA    1 
ATOM   4116 C C     . LEU A 1 710 ? -4.617  54.309  67.020  1.00 96.16  ?  691 LEU A C     1 
ATOM   4117 O O     . LEU A 1 710 ? -5.449  53.790  66.315  1.00 99.18  ?  691 LEU A O     1 
ATOM   4118 C CB    . LEU A 1 710 ? -5.007  56.379  65.651  1.00 94.61  ?  691 LEU A CB    1 
ATOM   4119 C CG    . LEU A 1 710 ? -5.272  57.875  65.686  1.00 96.31  ?  691 LEU A CG    1 
ATOM   4120 C CD1   . LEU A 1 710 ? -4.082  58.618  65.126  1.00 106.92 ?  691 LEU A CD1   1 
ATOM   4121 C CD2   . LEU A 1 710 ? -6.546  58.229  64.934  1.00 99.62  ?  691 LEU A CD2   1 
ATOM   4122 N N     . PHE A 1 711 ? -3.931  53.673  67.949  1.00 92.09  ?  692 PHE A N     1 
ATOM   4123 C CA    . PHE A 1 711 ? -3.891  52.203  68.043  1.00 99.94  ?  692 PHE A CA    1 
ATOM   4124 C C     . PHE A 1 711 ? -5.189  51.592  68.571  1.00 101.71 ?  692 PHE A C     1 
ATOM   4125 O O     . PHE A 1 711 ? -5.309  50.387  68.477  1.00 105.43 ?  692 PHE A O     1 
ATOM   4126 C CB    . PHE A 1 711 ? -2.692  51.818  68.894  1.00 99.06  ?  692 PHE A CB    1 
ATOM   4127 C CG    . PHE A 1 711 ? -3.062  51.611  70.330  1.00 102.33 ?  692 PHE A CG    1 
ATOM   4128 C CD1   . PHE A 1 711 ? -2.892  52.612  71.252  1.00 105.38 ?  692 PHE A CD1   1 
ATOM   4129 C CD2   . PHE A 1 711 ? -3.601  50.420  70.751  1.00 101.61 ?  692 PHE A CD2   1 
ATOM   4130 C CE1   . PHE A 1 711 ? -3.233  52.415  72.573  1.00 103.90 ?  692 PHE A CE1   1 
ATOM   4131 C CE2   . PHE A 1 711 ? -3.927  50.222  72.077  1.00 97.26  ?  692 PHE A CE2   1 
ATOM   4132 C CZ    . PHE A 1 711 ? -3.754  51.224  72.982  1.00 98.22  ?  692 PHE A CZ    1 
ATOM   4133 N N     . LEU A 1 712 ? -6.116  52.349  69.133  1.00 95.92  ?  693 LEU A N     1 
ATOM   4134 C CA    . LEU A 1 712 ? -7.310  51.643  69.650  1.00 92.74  ?  693 LEU A CA    1 
ATOM   4135 C C     . LEU A 1 712 ? -8.539  52.540  69.612  1.00 96.91  ?  693 LEU A C     1 
ATOM   4136 O O     . LEU A 1 712 ? -8.417  53.708  69.917  1.00 99.39  ?  693 LEU A O     1 
ATOM   4137 C CB    . LEU A 1 712 ? -7.009  51.212  71.078  1.00 92.44  ?  693 LEU A CB    1 
ATOM   4138 C CG    . LEU A 1 712 ? -8.231  50.870  71.915  1.00 100.71 ?  693 LEU A CG    1 
ATOM   4139 C CD1   . LEU A 1 712 ? -8.918  49.645  71.362  1.00 104.47 ?  693 LEU A CD1   1 
ATOM   4140 C CD2   . LEU A 1 712 ? -7.846  50.639  73.356  1.00 100.18 ?  693 LEU A CD2   1 
ATOM   4141 N N     . PHE A 1 713 ? -9.682  51.979  69.240  1.00 92.01  ?  694 PHE A N     1 
ATOM   4142 C CA    . PHE A 1 713 ? -10.947 52.734  69.125  1.00 97.71  ?  694 PHE A CA    1 
ATOM   4143 C C     . PHE A 1 713 ? -11.907 52.241  70.191  1.00 98.35  ?  694 PHE A C     1 
ATOM   4144 O O     . PHE A 1 713 ? -11.664 51.207  70.776  1.00 103.10 ?  694 PHE A O     1 
ATOM   4145 C CB    . PHE A 1 713 ? -11.507 52.594  67.711  1.00 106.54 ?  694 PHE A CB    1 
ATOM   4146 C CG    . PHE A 1 713 ? -10.663 53.260  66.659  1.00 100.79 ?  694 PHE A CG    1 
ATOM   4147 C CD1   . PHE A 1 713 ? -9.409  52.784  66.347  1.00 97.54  ?  694 PHE A CD1   1 
ATOM   4148 C CD2   . PHE A 1 713 ? -11.121 54.364  65.979  1.00 96.28  ?  694 PHE A CD2   1 
ATOM   4149 C CE1   . PHE A 1 713 ? -8.605  53.413  65.420  1.00 92.84  ?  694 PHE A CE1   1 
ATOM   4150 C CE2   . PHE A 1 713 ? -10.326 54.979  65.033  1.00 101.90 ?  694 PHE A CE2   1 
ATOM   4151 C CZ    . PHE A 1 713 ? -9.072  54.508  64.758  1.00 101.57 ?  694 PHE A CZ    1 
ATOM   4152 N N     . TRP A 1 714 ? -12.968 52.988  70.433  1.00 96.64  ?  695 TRP A N     1 
ATOM   4153 C CA    . TRP A 1 714 ? -13.895 52.585  71.504  1.00 99.63  ?  695 TRP A CA    1 
ATOM   4154 C C     . TRP A 1 714 ? -15.317 52.919  71.086  1.00 105.15 ?  695 TRP A C     1 
ATOM   4155 O O     . TRP A 1 714 ? -15.498 53.989  70.566  1.00 108.13 ?  695 TRP A O     1 
ATOM   4156 C CB    . TRP A 1 714 ? -13.557 53.462  72.694  1.00 107.22 ?  695 TRP A CB    1 
ATOM   4157 C CG    . TRP A 1 714 ? -12.257 53.278  73.409  1.00 110.55 ?  695 TRP A CG    1 
ATOM   4158 C CD1   . TRP A 1 714 ? -11.064 53.842  73.081  1.00 108.24 ?  695 TRP A CD1   1 
ATOM   4159 C CD2   . TRP A 1 714 ? -12.036 52.592  74.648  1.00 104.30 ?  695 TRP A CD2   1 
ATOM   4160 N NE1   . TRP A 1 714 ? -10.107 53.511  73.996  1.00 100.97 ?  695 TRP A NE1   1 
ATOM   4161 C CE2   . TRP A 1 714 ? -10.674 52.735  74.961  1.00 102.96 ?  695 TRP A CE2   1 
ATOM   4162 C CE3   . TRP A 1 714 ? -12.833 51.821  75.487  1.00 101.35 ?  695 TRP A CE3   1 
ATOM   4163 C CZ2   . TRP A 1 714 ? -10.103 52.154  76.081  1.00 102.85 ?  695 TRP A CZ2   1 
ATOM   4164 C CZ3   . TRP A 1 714 ? -12.275 51.255  76.600  1.00 107.28 ?  695 TRP A CZ3   1 
ATOM   4165 C CH2   . TRP A 1 714 ? -10.927 51.417  76.889  1.00 109.73 ?  695 TRP A CH2   1 
ATOM   4166 N N     . ASN A 1 715 ? -16.294 52.065  71.357  1.00 108.81 ?  696 ASN A N     1 
ATOM   4167 C CA    . ASN A 1 715 ? -17.696 52.448  71.059  1.00 118.22 ?  696 ASN A CA    1 
ATOM   4168 C C     . ASN A 1 715 ? -18.429 52.318  72.377  1.00 124.09 ?  696 ASN A C     1 
ATOM   4169 O O     . ASN A 1 715 ? -18.914 51.226  72.651  1.00 126.02 ?  696 ASN A O     1 
ATOM   4170 C CB    . ASN A 1 715 ? -18.403 51.516  70.083  1.00 120.95 ?  696 ASN A CB    1 
ATOM   4171 C CG    . ASN A 1 715 ? -19.910 51.615  70.176  1.00 127.87 ?  696 ASN A CG    1 
ATOM   4172 O OD1   . ASN A 1 715 ? -20.458 52.604  70.646  1.00 128.53 ?  696 ASN A OD1   1 
ATOM   4173 N ND2   . ASN A 1 715 ? -20.597 50.591  69.719  1.00 123.47 ?  696 ASN A ND2   1 
ATOM   4174 N N     . LEU A 1 716 ? -18.550 53.408  73.122  1.00 126.65 ?  697 LEU A N     1 
ATOM   4175 C CA    . LEU A 1 716 ? -19.150 53.278  74.466  1.00 130.22 ?  697 LEU A CA    1 
ATOM   4176 C C     . LEU A 1 716 ? -20.365 54.184  74.573  1.00 133.23 ?  697 LEU A C     1 
ATOM   4177 O O     . LEU A 1 716 ? -21.330 53.795  75.221  1.00 133.64 ?  697 LEU A O     1 
ATOM   4178 C CB    . LEU A 1 716 ? -18.097 53.696  75.488  1.00 122.75 ?  697 LEU A CB    1 
ATOM   4179 C CG    . LEU A 1 716 ? -16.822 52.864  75.480  1.00 114.15 ?  697 LEU A CG    1 
ATOM   4180 C CD1   . LEU A 1 716 ? -15.599 53.744  75.321  1.00 109.79 ?  697 LEU A CD1   1 
ATOM   4181 C CD2   . LEU A 1 716 ? -16.720 52.060  76.756  1.00 111.70 ?  697 LEU A CD2   1 
ATOM   4182 N N     . TYR A 1 717 ? -20.315 55.340  73.935  1.00 129.78 ?  698 TYR A N     1 
ATOM   4183 C CA    . TYR A 1 717 ? -21.438 56.285  74.110  1.00 133.41 ?  698 TYR A CA    1 
ATOM   4184 C C     . TYR A 1 717 ? -22.692 55.797  73.398  1.00 141.92 ?  698 TYR A C     1 
ATOM   4185 O O     . TYR A 1 717 ? -22.583 55.062  72.414  1.00 144.27 ?  698 TYR A O     1 
ATOM   4186 C CB    . TYR A 1 717 ? -20.944 57.711  73.914  1.00 131.02 ?  698 TYR A CB    1 
ATOM   4187 C CG    . TYR A 1 717 ? -19.871 58.008  74.921  1.00 132.09 ?  698 TYR A CG    1 
ATOM   4188 C CD1   . TYR A 1 717 ? -18.538 57.812  74.623  1.00 126.89 ?  698 TYR A CD1   1 
ATOM   4189 C CD2   . TYR A 1 717 ? -20.199 58.389  76.205  1.00 128.49 ?  698 TYR A CD2   1 
ATOM   4190 C CE1   . TYR A 1 717 ? -17.549 58.053  75.559  1.00 128.19 ?  698 TYR A CE1   1 
ATOM   4191 C CE2   . TYR A 1 717 ? -19.225 58.622  77.155  1.00 124.38 ?  698 TYR A CE2   1 
ATOM   4192 C CZ    . TYR A 1 717 ? -17.895 58.459  76.830  1.00 127.28 ?  698 TYR A CZ    1 
ATOM   4193 O OH    . TYR A 1 717 ? -16.938 58.691  77.769  1.00 119.08 ?  698 TYR A OH    1 
ATOM   4194 N N     . LYS A 1 718 ? -23.841 56.225  73.921  1.00 141.15 ?  699 LYS A N     1 
ATOM   4195 C CA    . LYS A 1 718 ? -25.177 55.828  73.422  1.00 146.55 ?  699 LYS A CA    1 
ATOM   4196 C C     . LYS A 1 718 ? -25.318 56.273  71.971  1.00 150.03 ?  699 LYS A C     1 
ATOM   4197 O O     . LYS A 1 718 ? -25.804 55.492  71.151  1.00 152.22 ?  699 LYS A O     1 
ATOM   4198 C CB    . LYS A 1 718 ? -26.246 56.537  74.254  1.00 141.62 ?  699 LYS A CB    1 
ATOM   4199 C CG    . LYS A 1 718 ? -26.532 55.917  75.614  1.00 142.87 ?  699 LYS A CG    1 
ATOM   4200 C CD    . LYS A 1 718 ? -27.737 56.509  76.308  1.00 144.65 ?  699 LYS A CD    1 
ATOM   4201 C CE    . LYS A 1 718 ? -27.604 56.523  77.817  1.00 149.17 ?  699 LYS A CE    1 
ATOM   4202 N NZ    . LYS A 1 718 ? -27.951 57.844  78.395  1.00 143.41 ?  699 LYS A NZ    1 
ATOM   4203 N N     . ALA A 1 719 ? -24.857 57.480  71.669  1.00 145.89 ?  700 ALA A N     1 
ATOM   4204 C CA    . ALA A 1 719 ? -24.933 58.012  70.294  1.00 138.57 ?  700 ALA A CA    1 
ATOM   4205 C C     . ALA A 1 719 ? -23.847 57.384  69.421  1.00 135.33 ?  700 ALA A C     1 
ATOM   4206 O O     . ALA A 1 719 ? -22.896 56.786  69.935  1.00 132.52 ?  700 ALA A O     1 
ATOM   4207 C CB    . ALA A 1 719 ? -24.839 59.510  70.303  1.00 130.74 ?  700 ALA A CB    1 
ATOM   4208 N N     . PRO A 1 720 ? -23.892 57.590  68.101  1.00 127.51 ?  701 PRO A N     1 
ATOM   4209 C CA    . PRO A 1 720 ? -22.938 56.949  67.238  1.00 123.19 ?  701 PRO A CA    1 
ATOM   4210 C C     . PRO A 1 720 ? -21.649 57.749  67.371  1.00 120.22 ?  701 PRO A C     1 
ATOM   4211 O O     . PRO A 1 720 ? -21.465 58.693  66.666  1.00 120.25 ?  701 PRO A O     1 
ATOM   4212 C CB    . PRO A 1 720 ? -23.548 57.295  65.885  1.00 130.56 ?  701 PRO A CB    1 
ATOM   4213 C CG    . PRO A 1 720 ? -24.112 58.653  66.118  1.00 128.73 ?  701 PRO A CG    1 
ATOM   4214 C CD    . PRO A 1 720 ? -24.824 58.468  67.430  1.00 126.93 ?  701 PRO A CD    1 
ATOM   4215 N N     . ILE A 1 721 ? -20.801 57.339  68.304  1.00 114.75 ?  702 ILE A N     1 
ATOM   4216 C CA    . ILE A 1 721 ? -19.534 58.077  68.509  1.00 113.44 ?  702 ILE A CA    1 
ATOM   4217 C C     . ILE A 1 721 ? -18.395 57.080  68.544  1.00 107.62 ?  702 ILE A C     1 
ATOM   4218 O O     . ILE A 1 721 ? -18.554 56.054  69.174  1.00 105.70 ?  702 ILE A O     1 
ATOM   4219 C CB    . ILE A 1 721 ? -19.585 58.832  69.842  1.00 121.62 ?  702 ILE A CB    1 
ATOM   4220 C CG1   . ILE A 1 721 ? -20.748 59.814  69.906  1.00 122.51 ?  702 ILE A CG1   1 
ATOM   4221 C CG2   . ILE A 1 721 ? -18.278 59.545  70.092  1.00 116.91 ?  702 ILE A CG2   1 
ATOM   4222 C CD1   . ILE A 1 721 ? -20.307 61.251  69.894  1.00 120.81 ?  702 ILE A CD1   1 
ATOM   4223 N N     . LEU A 1 722 ? -17.306 57.402  67.868  1.00 106.20 ?  703 LEU A N     1 
ATOM   4224 C CA    . LEU A 1 722 ? -16.079 56.579  67.930  1.00 111.01 ?  703 LEU A CA    1 
ATOM   4225 C C     . LEU A 1 722 ? -15.048 57.415  68.676  1.00 108.07 ?  703 LEU A C     1 
ATOM   4226 O O     . LEU A 1 722 ? -15.101 58.630  68.565  1.00 108.53 ?  703 LEU A O     1 
ATOM   4227 C CB    . LEU A 1 722 ? -15.593 56.288  66.515  1.00 118.50 ?  703 LEU A CB    1 
ATOM   4228 C CG    . LEU A 1 722 ? -15.866 54.883  65.993  1.00 117.91 ?  703 LEU A CG    1 
ATOM   4229 C CD1   . LEU A 1 722 ? -14.569 54.129  65.804  1.00 113.83 ?  703 LEU A CD1   1 
ATOM   4230 C CD2   . LEU A 1 722 ? -16.777 54.129  66.933  1.00 115.45 ?  703 LEU A CD2   1 
ATOM   4231 N N     . LEU A 1 723 ? -14.108 56.774  69.349  1.00 103.55 ?  704 LEU A N     1 
ATOM   4232 C CA    . LEU A 1 723 ? -13.144 57.499  70.167  1.00 98.08  ?  704 LEU A CA    1 
ATOM   4233 C C     . LEU A 1 723 ? -11.821 56.743  70.127  1.00 94.49  ?  704 LEU A C     1 
ATOM   4234 O O     . LEU A 1 723 ? -11.799 55.528  70.342  1.00 97.12  ?  704 LEU A O     1 
ATOM   4235 C CB    . LEU A 1 723 ? -13.673 57.607  71.602  1.00 107.17 ?  704 LEU A CB    1 
ATOM   4236 C CG    . LEU A 1 723 ? -13.040 58.480  72.691  1.00 111.94 ?  704 LEU A CG    1 
ATOM   4237 C CD1   . LEU A 1 723 ? -14.097 58.834  73.751  1.00 113.07 ?  704 LEU A CD1   1 
ATOM   4238 C CD2   . LEU A 1 723 ? -11.832 57.787  73.329  1.00 108.69 ?  704 LEU A CD2   1 
ATOM   4239 N N     . ALA A 1 724 ? -10.721 57.445  69.875  1.00 86.06  ?  705 ALA A N     1 
ATOM   4240 C CA    . ALA A 1 724 ? -9.489  56.772  69.478  1.00 88.90  ?  705 ALA A CA    1 
ATOM   4241 C C     . ALA A 1 724 ? -8.286  57.280  70.252  1.00 91.01  ?  705 ALA A C     1 
ATOM   4242 O O     . ALA A 1 724 ? -8.062  58.492  70.323  1.00 97.69  ?  705 ALA A O     1 
ATOM   4243 C CB    . ALA A 1 724 ? -9.234  56.962  67.978  1.00 106.08 ?  705 ALA A CB    1 
ATOM   4244 N N     . LEU A 1 725 ? -7.472  56.352  70.750  1.00 88.23  ?  706 LEU A N     1 
ATOM   4245 C CA    . LEU A 1 725 ? -6.339  56.642  71.632  1.00 93.68  ?  706 LEU A CA    1 
ATOM   4246 C C     . LEU A 1 725 ? -5.073  56.953  70.855  1.00 90.95  ?  706 LEU A C     1 
ATOM   4247 O O     . LEU A 1 725 ? -4.923  56.545  69.708  1.00 101.92 ?  706 LEU A O     1 
ATOM   4248 C CB    . LEU A 1 725 ? -6.104  55.457  72.563  1.00 93.59  ?  706 LEU A CB    1 
ATOM   4249 C CG    . LEU A 1 725 ? -6.873  55.520  73.881  1.00 97.34  ?  706 LEU A CG    1 
ATOM   4250 C CD1   . LEU A 1 725 ? -8.362  55.642  73.697  1.00 96.38  ?  706 LEU A CD1   1 
ATOM   4251 C CD2   . LEU A 1 725 ? -6.646  54.169  74.525  1.00 100.41 ?  706 LEU A CD2   1 
ATOM   4252 N N     . VAL A 1 726 ? -4.170  57.702  71.483  1.00 88.22  ?  707 VAL A N     1 
ATOM   4253 C CA    . VAL A 1 726 ? -2.846  58.012  70.942  1.00 89.90  ?  707 VAL A CA    1 
ATOM   4254 C C     . VAL A 1 726 ? -1.900  57.833  72.117  1.00 96.87  ?  707 VAL A C     1 
ATOM   4255 O O     . VAL A 1 726 ? -1.733  58.753  72.924  1.00 102.47 ?  707 VAL A O     1 
ATOM   4256 C CB    . VAL A 1 726 ? -2.745  59.434  70.374  1.00 89.69  ?  707 VAL A CB    1 
ATOM   4257 C CG1   . VAL A 1 726 ? -1.409  59.649  69.638  1.00 86.77  ?  707 VAL A CG1   1 
ATOM   4258 C CG2   . VAL A 1 726 ? -3.954  59.765  69.503  1.00 89.80  ?  707 VAL A CG2   1 
ATOM   4259 N N     . ALA A 1 727 ? -1.311  56.657  72.249  1.00 93.70  ?  708 ALA A N     1 
ATOM   4260 C CA    . ALA A 1 727 ? -0.454  56.418  73.396  1.00 96.79  ?  708 ALA A CA    1 
ATOM   4261 C C     . ALA A 1 727 ? 1.006   56.672  73.017  1.00 95.15  ?  708 ALA A C     1 
ATOM   4262 O O     . ALA A 1 727 ? 1.294   57.379  72.046  1.00 98.42  ?  708 ALA A O     1 
ATOM   4263 C CB    . ALA A 1 727 ? -0.690  54.995  73.919  1.00 100.89 ?  708 ALA A CB    1 
ATOM   4264 N N     . GLY A 1 728 ? 1.930   56.096  73.784  1.00 98.92  ?  709 GLY A N     1 
ATOM   4265 C CA    . GLY A 1 728 ? 3.336   56.051  73.445  1.00 99.40  ?  709 GLY A CA    1 
ATOM   4266 C C     . GLY A 1 728 ? 3.935   57.382  73.059  1.00 100.86 ?  709 GLY A C     1 
ATOM   4267 O O     . GLY A 1 728 ? 3.366   58.448  73.332  1.00 102.17 ?  709 GLY A O     1 
ATOM   4268 N N     . GLU A 1 729 ? 5.094   57.319  72.404  1.00 98.56  ?  710 GLU A N     1 
ATOM   4269 C CA    . GLU A 1 729 ? 5.732   58.517  71.876  1.00 101.21 ?  710 GLU A CA    1 
ATOM   4270 C C     . GLU A 1 729 ? 4.823   59.280  70.915  1.00 103.11 ?  710 GLU A C     1 
ATOM   4271 O O     . GLU A 1 729 ? 5.039   60.477  70.679  1.00 101.96 ?  710 GLU A O     1 
ATOM   4272 C CB    . GLU A 1 729 ? 7.011   58.092  71.181  1.00 101.46 ?  710 GLU A CB    1 
ATOM   4273 C CG    . GLU A 1 729 ? 7.859   57.180  72.049  1.00 97.68  ?  710 GLU A CG    1 
ATOM   4274 C CD    . GLU A 1 729 ? 8.900   57.975  72.780  1.00 104.52 ?  710 GLU A CD    1 
ATOM   4275 O OE1   . GLU A 1 729 ? 8.710   59.207  72.841  1.00 108.52 ?  710 GLU A OE1   1 
ATOM   4276 O OE2   . GLU A 1 729 ? 9.890   57.390  73.287  1.00 105.15 ?  710 GLU A OE2   1 
ATOM   4277 N N     . ALA A 1 730 ? 3.871   58.546  70.383  1.00 101.26 ?  711 ALA A N     1 
ATOM   4278 C CA    . ALA A 1 730 ? 2.984   59.105  69.362  1.00 98.52  ?  711 ALA A CA    1 
ATOM   4279 C C     . ALA A 1 730 ? 2.185   60.247  69.949  1.00 100.10 ?  711 ALA A C     1 
ATOM   4280 O O     . ALA A 1 730 ? 2.276   61.339  69.423  1.00 100.21 ?  711 ALA A O     1 
ATOM   4281 C CB    . ALA A 1 730 ? 2.071   58.017  68.898  1.00 101.13 ?  711 ALA A CB    1 
ATOM   4282 N N     . ALA A 1 731 ? 1.558   60.013  71.090  1.00 106.19 ?  712 ALA A N     1 
ATOM   4283 C CA    . ALA A 1 731 ? 0.610   61.006  71.633  1.00 103.69 ?  712 ALA A CA    1 
ATOM   4284 C C     . ALA A 1 731 ? 1.294   62.340  71.870  1.00 101.26 ?  712 ALA A C     1 
ATOM   4285 O O     . ALA A 1 731 ? 0.706   63.341  71.526  1.00 100.20 ?  712 ALA A O     1 
ATOM   4286 C CB    . ALA A 1 731 ? -0.012  60.480  72.890  1.00 101.81 ?  712 ALA A CB    1 
ATOM   4287 N N     . GLY A 1 732 ? 2.508   62.339  72.393  1.00 99.76  ?  713 GLY A N     1 
ATOM   4288 C CA    . GLY A 1 732 ? 3.157   63.640  72.592  1.00 105.13 ?  713 GLY A CA    1 
ATOM   4289 C C     . GLY A 1 732 ? 3.384   64.334  71.272  1.00 103.33 ?  713 GLY A C     1 
ATOM   4290 O O     . GLY A 1 732 ? 3.146   65.526  71.189  1.00 100.72 ?  713 GLY A O     1 
ATOM   4291 N N     . ILE A 1 733 ? 3.826   63.587  70.272  1.00 106.61 ?  714 ILE A N     1 
ATOM   4292 C CA    . ILE A 1 733 ? 4.145   64.176  68.944  1.00 96.66  ?  714 ILE A CA    1 
ATOM   4293 C C     . ILE A 1 733 ? 2.890   64.622  68.212  1.00 90.65  ?  714 ILE A C     1 
ATOM   4294 O O     . ILE A 1 733 ? 2.989   65.511  67.427  1.00 95.62  ?  714 ILE A O     1 
ATOM   4295 C CB    . ILE A 1 733 ? 4.943   63.199  68.087  1.00 83.46  ?  714 ILE A CB    1 
ATOM   4296 C CG1   . ILE A 1 733 ? 6.430   63.235  68.423  1.00 94.19  ?  714 ILE A CG1   1 
ATOM   4297 C CG2   . ILE A 1 733 ? 4.704   63.535  66.641  1.00 82.60  ?  714 ILE A CG2   1 
ATOM   4298 C CD1   . ILE A 1 733 ? 7.148   64.425  67.864  1.00 90.62  ?  714 ILE A CD1   1 
ATOM   4299 N N     . MET A 1 734 ? 1.736   64.042  68.483  1.00 94.90  ?  715 MET A N     1 
ATOM   4300 C CA    . MET A 1 734 ? 0.541   64.418  67.691  1.00 102.49 ?  715 MET A CA    1 
ATOM   4301 C C     . MET A 1 734 ? -0.143  65.676  68.214  1.00 106.65 ?  715 MET A C     1 
ATOM   4302 O O     . MET A 1 734 ? -1.160  66.032  67.660  1.00 104.85 ?  715 MET A O     1 
ATOM   4303 C CB    . MET A 1 734 ? -0.477  63.284  67.632  1.00 109.65 ?  715 MET A CB    1 
ATOM   4304 C CG    . MET A 1 734 ? 0.094   62.028  67.030  1.00 115.99 ?  715 MET A CG    1 
ATOM   4305 S SD    . MET A 1 734 ? -0.337  61.787  65.303  1.00 132.08 ?  715 MET A SD    1 
ATOM   4306 C CE    . MET A 1 734 ? -1.911  62.636  65.251  1.00 115.32 ?  715 MET A CE    1 
ATOM   4307 N N     . GLU A 1 735 ? 0.354   66.284  69.283  1.00 108.07 ?  716 GLU A N     1 
ATOM   4308 C CA    . GLU A 1 735 ? -0.212  67.547  69.811  1.00 108.69 ?  716 GLU A CA    1 
ATOM   4309 C C     . GLU A 1 735 ? 0.013   68.673  68.796  1.00 111.63 ?  716 GLU A C     1 
ATOM   4310 O O     . GLU A 1 735 ? -0.861  69.525  68.679  1.00 111.09 ?  716 GLU A O     1 
ATOM   4311 C CB    . GLU A 1 735 ? 0.338   67.832  71.208  1.00 108.94 ?  716 GLU A CB    1 
ATOM   4312 C CG    . GLU A 1 735 ? -0.268  66.956  72.287  1.00 107.28 ?  716 GLU A CG    1 
ATOM   4313 C CD    . GLU A 1 735 ? -0.587  67.672  73.581  1.00 102.60 ?  716 GLU A CD    1 
ATOM   4314 O OE1   . GLU A 1 735 ? 0.292   68.367  74.071  1.00 96.28  ?  716 GLU A OE1   1 
ATOM   4315 O OE2   . GLU A 1 735 ? -1.716  67.539  74.085  1.00 100.49 ?  716 GLU A OE2   1 
ATOM   4316 N N     . ASN A 1 736 ? 1.136   68.633  68.078  1.00 116.66 ?  717 ASN A N     1 
ATOM   4317 C CA    . ASN A 1 736 ? 1.586   69.647  67.087  1.00 120.31 ?  717 ASN A CA    1 
ATOM   4318 C C     . ASN A 1 736 ? 0.915   69.509  65.724  1.00 116.99 ?  717 ASN A C     1 
ATOM   4319 O O     . ASN A 1 736 ? 1.352   70.198  64.814  1.00 116.76 ?  717 ASN A O     1 
ATOM   4320 C CB    . ASN A 1 736 ? 3.041   69.428  66.704  1.00 115.59 ?  717 ASN A CB    1 
ATOM   4321 C CG    . ASN A 1 736 ? 3.958   69.775  67.841  1.00 120.24 ?  717 ASN A CG    1 
ATOM   4322 O OD1   . ASN A 1 736 ? 3.551   69.717  68.990  1.00 113.05 ?  717 ASN A OD1   1 
ATOM   4323 N ND2   . ASN A 1 736 ? 5.177   70.154  67.522  1.00 121.98 ?  717 ASN A ND2   1 
ATOM   4324 N N     . ILE A 1 737 ? -0.011  68.581  65.552  1.00 115.10 ?  718 ILE A N     1 
ATOM   4325 C CA    . ILE A 1 737 ? -0.656  68.402  64.226  1.00 111.68 ?  718 ILE A CA    1 
ATOM   4326 C C     . ILE A 1 737 ? -2.095  68.882  64.350  1.00 111.77 ?  718 ILE A C     1 
ATOM   4327 O O     . ILE A 1 737 ? -2.682  68.582  65.354  1.00 115.38 ?  718 ILE A O     1 
ATOM   4328 C CB    . ILE A 1 737 ? -0.557  66.907  63.912  1.00 108.60 ?  718 ILE A CB    1 
ATOM   4329 C CG1   . ILE A 1 737 ? 0.841   66.558  63.415  1.00 100.70 ?  718 ILE A CG1   1 
ATOM   4330 C CG2   . ILE A 1 737 ? -1.634  66.439  62.962  1.00 112.27 ?  718 ILE A CG2   1 
ATOM   4331 C CD1   . ILE A 1 737 ? 1.117   65.089  63.424  1.00 98.12  ?  718 ILE A CD1   1 
ATOM   4332 N N     . SER A 1 738 ? -2.696  69.468  63.310  1.00 111.29 ?  719 SER A N     1 
ATOM   4333 C CA    . SER A 1 738 ? -4.063  70.000  63.351  1.00 115.57 ?  719 SER A CA    1 
ATOM   4334 C C     . SER A 1 738 ? -5.111  68.911  63.574  1.00 113.11 ?  719 SER A C     1 
ATOM   4335 O O     . SER A 1 738 ? -4.836  67.733  63.311  1.00 110.44 ?  719 SER A O     1 
ATOM   4336 C CB    . SER A 1 738 ? -4.369  70.776  62.051  1.00 125.32 ?  719 SER A CB    1 
ATOM   4337 O OG    . SER A 1 738 ? -4.807  69.941  60.968  1.00 122.61 ?  719 SER A OG    1 
ATOM   4338 N N     . ASP A 1 739 ? -6.302  69.279  64.077  1.00 114.49 ?  720 ASP A N     1 
ATOM   4339 C CA    . ASP A 1 739 ? -7.399  68.307  64.152  1.00 120.53 ?  720 ASP A CA    1 
ATOM   4340 C C     . ASP A 1 739 ? -7.603  67.614  62.808  1.00 119.74 ?  720 ASP A C     1 
ATOM   4341 O O     . ASP A 1 739 ? -7.687  66.379  62.729  1.00 115.85 ?  720 ASP A O     1 
ATOM   4342 C CB    . ASP A 1 739 ? -8.732  68.954  64.589  1.00 126.26 ?  720 ASP A CB    1 
ATOM   4343 C CG    . ASP A 1 739 ? -8.668  69.678  65.938  1.00 127.50 ?  720 ASP A CG    1 
ATOM   4344 O OD1   . ASP A 1 739 ? -7.772  69.369  66.767  1.00 118.95 ?  720 ASP A OD1   1 
ATOM   4345 O OD2   . ASP A 1 739 ? -9.579  70.525  66.173  1.00 129.28 ?  720 ASP A OD2   1 
ATOM   4346 N N     . ASP A 1 740 ? -7.679  68.415  61.741  1.00 123.44 ?  721 ASP A N     1 
ATOM   4347 C CA    . ASP A 1 740 ? -7.964  67.912  60.401  1.00 116.33 ?  721 ASP A CA    1 
ATOM   4348 C C     . ASP A 1 740 ? -6.983  66.816  59.994  1.00 113.09 ?  721 ASP A C     1 
ATOM   4349 O O     . ASP A 1 740 ? -7.395  65.709  59.623  1.00 114.23 ?  721 ASP A O     1 
ATOM   4350 C CB    . ASP A 1 740 ? -7.952  69.092  59.434  1.00 112.87 ?  721 ASP A CB    1 
ATOM   4351 C CG    . ASP A 1 740 ? -8.972  70.159  59.833  1.00 125.06 ?  721 ASP A CG    1 
ATOM   4352 O OD1   . ASP A 1 740 ? -10.136 69.790  60.149  1.00 122.87 ?  721 ASP A OD1   1 
ATOM   4353 O OD2   . ASP A 1 740 ? -8.592  71.352  59.904  1.00 132.54 ?  721 ASP A OD2   1 
ATOM   4354 N N     . VAL A 1 741 ? -5.681  67.080  60.118  1.00 106.98 ?  722 VAL A N     1 
ATOM   4355 C CA    . VAL A 1 741 ? -4.679  66.053  59.833  1.00 106.75 ?  722 VAL A CA    1 
ATOM   4356 C C     . VAL A 1 741 ? -4.878  64.798  60.697  1.00 112.70 ?  722 VAL A C     1 
ATOM   4357 O O     . VAL A 1 741 ? -4.756  63.664  60.204  1.00 107.62 ?  722 VAL A O     1 
ATOM   4358 C CB    . VAL A 1 741 ? -3.279  66.640  60.026  1.00 105.65 ?  722 VAL A CB    1 
ATOM   4359 C CG1   . VAL A 1 741 ? -2.226  65.583  59.677  1.00 111.61 ?  722 VAL A CG1   1 
ATOM   4360 C CG2   . VAL A 1 741 ? -3.161  67.902  59.233  1.00 105.16 ?  722 VAL A CG2   1 
ATOM   4361 N N     . ILE A 1 742 ? -5.171  65.030  61.962  1.00 114.81 ?  723 ILE A N     1 
ATOM   4362 C CA    . ILE A 1 742 ? -5.352  63.871  62.862  1.00 113.52 ?  723 ILE A CA    1 
ATOM   4363 C C     . ILE A 1 742 ? -6.593  63.152  62.380  1.00 113.11 ?  723 ILE A C     1 
ATOM   4364 O O     . ILE A 1 742 ? -6.504  61.983  62.028  1.00 114.41 ?  723 ILE A O     1 
ATOM   4365 C CB    . ILE A 1 742 ? -5.536  64.356  64.300  1.00 113.62 ?  723 ILE A CB    1 
ATOM   4366 C CG1   . ILE A 1 742 ? -4.273  65.031  64.824  1.00 115.74 ?  723 ILE A CG1   1 
ATOM   4367 C CG2   . ILE A 1 742 ? -5.942  63.207  65.191  1.00 106.60 ?  723 ILE A CG2   1 
ATOM   4368 C CD1   . ILE A 1 742 ? -4.140  64.952  66.323  1.00 113.04 ?  723 ILE A CD1   1 
ATOM   4369 N N     . VAL A 1 743 ? -7.697  63.872  62.354  1.00 108.17 ?  724 VAL A N     1 
ATOM   4370 C CA    . VAL A 1 743 ? -8.980  63.249  61.949  1.00 109.06 ?  724 VAL A CA    1 
ATOM   4371 C C     . VAL A 1 743 ? -8.818  62.637  60.561  1.00 114.96 ?  724 VAL A C     1 
ATOM   4372 O O     . VAL A 1 743 ? -9.424  61.609  60.329  1.00 120.28 ?  724 VAL A O     1 
ATOM   4373 C CB    . VAL A 1 743 ? -10.145 64.243  61.996  1.00 106.28 ?  724 VAL A CB    1 
ATOM   4374 C CG1   . VAL A 1 743 ? -11.408 63.589  61.487  1.00 105.99 ?  724 VAL A CG1   1 
ATOM   4375 C CG2   . VAL A 1 743 ? -10.380 64.764  63.396  1.00 101.68 ?  724 VAL A CG2   1 
ATOM   4376 N N     . GLY A 1 744 ? -8.110  63.289  59.646  1.00 110.75 ?  725 GLY A N     1 
ATOM   4377 C CA    . GLY A 1 744 ? -7.898  62.659  58.336  1.00 109.66 ?  725 GLY A CA    1 
ATOM   4378 C C     . GLY A 1 744 ? -7.277  61.292  58.515  1.00 108.82 ?  725 GLY A C     1 
ATOM   4379 O O     . GLY A 1 744 ? -7.881  60.314  58.071  1.00 105.08 ?  725 GLY A O     1 
ATOM   4380 N N     . ARG A 1 745 ? -6.136  61.241  59.197  1.00 109.01 ?  726 ARG A N     1 
ATOM   4381 C CA    . ARG A 1 745 ? -5.422  59.968  59.443  1.00 108.70 ?  726 ARG A CA    1 
ATOM   4382 C C     . ARG A 1 745 ? -6.414  59.016  60.087  1.00 110.92 ?  726 ARG A C     1 
ATOM   4383 O O     . ARG A 1 745 ? -6.646  57.963  59.540  1.00 109.42 ?  726 ARG A O     1 
ATOM   4384 C CB    . ARG A 1 745 ? -4.271  60.196  60.420  1.00 106.86 ?  726 ARG A CB    1 
ATOM   4385 C CG    . ARG A 1 745 ? -3.082  60.942  59.843  1.00 106.48 ?  726 ARG A CG    1 
ATOM   4386 C CD    . ARG A 1 745 ? -1.869  60.674  60.700  1.00 110.16 ?  726 ARG A CD    1 
ATOM   4387 N NE    . ARG A 1 745 ? -0.772  61.611  60.534  1.00 113.98 ?  726 ARG A NE    1 
ATOM   4388 C CZ    . ARG A 1 745 ? 0.455   61.396  60.982  1.00 116.71 ?  726 ARG A CZ    1 
ATOM   4389 N NH1   . ARG A 1 745 ? 0.748   60.282  61.625  1.00 116.75 ?  726 ARG A NH1   1 
ATOM   4390 N NH2   . ARG A 1 745 ? 1.395   62.294  60.787  1.00 113.36 ?  726 ARG A NH2   1 
ATOM   4391 N N     . CYS A 1 746 ? -7.014  59.469  61.174  1.00 113.47 ?  727 CYS A N     1 
ATOM   4392 C CA    . CYS A 1 746 ? -8.039  58.737  61.944  1.00 117.86 ?  727 CYS A CA    1 
ATOM   4393 C C     . CYS A 1 746 ? -9.055  58.137  60.981  1.00 112.82 ?  727 CYS A C     1 
ATOM   4394 O O     . CYS A 1 746 ? -9.165  56.919  60.912  1.00 112.19 ?  727 CYS A O     1 
ATOM   4395 C CB    . CYS A 1 746 ? -8.717  59.759  62.841  1.00 115.53 ?  727 CYS A CB    1 
ATOM   4396 S SG    . CYS A 1 746 ? -9.814  59.079  64.100  1.00 117.38 ?  727 CYS A SG    1 
ATOM   4397 N N     . LEU A 1 747 ? -9.656  58.978  60.156  1.00 111.89 ?  728 LEU A N     1 
ATOM   4398 C CA    . LEU A 1 747 ? -10.686 58.510  59.207  1.00 114.60 ?  728 LEU A CA    1 
ATOM   4399 C C     . LEU A 1 747 ? -10.144 57.413  58.297  1.00 117.41 ?  728 LEU A C     1 
ATOM   4400 O O     . LEU A 1 747 ? -10.885 56.491  58.031  1.00 115.47 ?  728 LEU A O     1 
ATOM   4401 C CB    . LEU A 1 747 ? -11.132 59.706  58.377  1.00 108.86 ?  728 LEU A CB    1 
ATOM   4402 C CG    . LEU A 1 747 ? -12.260 60.512  59.001  1.00 114.22 ?  728 LEU A CG    1 
ATOM   4403 C CD1   . LEU A 1 747 ? -12.315 61.903  58.412  1.00 109.29 ?  728 LEU A CD1   1 
ATOM   4404 C CD2   . LEU A 1 747 ? -13.582 59.806  58.800  1.00 117.76 ?  728 LEU A CD2   1 
ATOM   4405 N N     . ALA A 1 748 ? -8.920  57.542  57.808  1.00 117.52 ?  729 ALA A N     1 
ATOM   4406 C CA    . ALA A 1 748 ? -8.380  56.528  56.882  1.00 115.28 ?  729 ALA A CA    1 
ATOM   4407 C C     . ALA A 1 748 ? -8.470  55.128  57.480  1.00 117.48 ?  729 ALA A C     1 
ATOM   4408 O O     . ALA A 1 748 ? -9.153  54.304  56.863  1.00 118.07 ?  729 ALA A O     1 
ATOM   4409 C CB    . ALA A 1 748 ? -6.960  56.866  56.535  1.00 111.73 ?  729 ALA A CB    1 
ATOM   4410 N N     . ILE A 1 749 ? -7.768  54.903  58.595  1.00 118.94 ?  730 ILE A N     1 
ATOM   4411 C CA    . ILE A 1 749 ? -7.689  53.587  59.289  1.00 115.25 ?  730 ILE A CA    1 
ATOM   4412 C C     . ILE A 1 749 ? -9.084  53.013  59.339  1.00 114.99 ?  730 ILE A C     1 
ATOM   4413 O O     . ILE A 1 749 ? -9.253  51.852  59.016  1.00 116.32 ?  730 ILE A O     1 
ATOM   4414 C CB    . ILE A 1 749 ? -7.157  53.747  60.715  1.00 112.57 ?  730 ILE A CB    1 
ATOM   4415 C CG1   . ILE A 1 749 ? -6.397  55.057  60.878  1.00 111.94 ?  730 ILE A CG1   1 
ATOM   4416 C CG2   . ILE A 1 749 ? -6.298  52.559  61.097  1.00 112.50 ?  730 ILE A CG2   1 
ATOM   4417 C CD1   . ILE A 1 749 ? -5.174  55.145  60.015  1.00 106.40 ?  730 ILE A CD1   1 
ATOM   4418 N N     . LEU A 1 750 ? -10.045 53.864  59.646  1.00 117.22 ?  731 LEU A N     1 
ATOM   4419 C CA    . LEU A 1 750 ? -11.423 53.352  59.682  1.00 120.53 ?  731 LEU A CA    1 
ATOM   4420 C C     . LEU A 1 750 ? -11.807 52.853  58.298  1.00 120.64 ?  731 LEU A C     1 
ATOM   4421 O O     . LEU A 1 750 ? -12.340 51.741  58.227  1.00 122.42 ?  731 LEU A O     1 
ATOM   4422 C CB    . LEU A 1 750 ? -12.339 54.500  60.084  1.00 121.61 ?  731 LEU A CB    1 
ATOM   4423 C CG    . LEU A 1 750 ? -12.572 54.630  61.580  1.00 112.46 ?  731 LEU A CG    1 
ATOM   4424 C CD1   . LEU A 1 750 ? -12.082 55.978  62.051  1.00 116.22 ?  731 LEU A CD1   1 
ATOM   4425 C CD2   . LEU A 1 750 ? -14.045 54.466  61.894  1.00 111.01 ?  731 LEU A CD2   1 
ATOM   4426 N N     . LYS A 1 751 ? -11.541 53.641  57.255  1.00 120.86 ?  732 LYS A N     1 
ATOM   4427 C CA    . LYS A 1 751 ? -11.998 53.184  55.934  1.00 125.23 ?  732 LYS A CA    1 
ATOM   4428 C C     . LYS A 1 751 ? -11.405 51.818  55.573  1.00 126.20 ?  732 LYS A C     1 
ATOM   4429 O O     . LYS A 1 751 ? -12.112 50.936  55.058  1.00 119.97 ?  732 LYS A O     1 
ATOM   4430 C CB    . LYS A 1 751 ? -11.636 54.213  54.855  1.00 119.38 ?  732 LYS A CB    1 
ATOM   4431 C CG    . LYS A 1 751 ? -12.338 55.557  54.965  1.00 120.23 ?  732 LYS A CG    1 
ATOM   4432 C CD    . LYS A 1 751 ? -11.924 56.504  53.818  1.00 120.51 ?  732 LYS A CD    1 
ATOM   4433 C CE    . LYS A 1 751 ? -12.638 57.855  53.897  1.00 113.65 ?  732 LYS A CE    1 
ATOM   4434 N NZ    . LYS A 1 751 ? -14.124 57.657  53.958  1.00 118.41 ?  732 LYS A NZ    1 
ATOM   4435 N N     . GLY A 1 752 ? -10.105 51.629  55.843  1.00 125.27 ?  733 GLY A N     1 
ATOM   4436 C CA    . GLY A 1 752 ? -9.461  50.359  55.558  1.00 118.96 ?  733 GLY A CA    1 
ATOM   4437 C C     . GLY A 1 752 ? -10.090 49.197  56.297  1.00 117.51 ?  733 GLY A C     1 
ATOM   4438 O O     . GLY A 1 752 ? -10.112 48.073  55.795  1.00 121.09 ?  733 GLY A O     1 
ATOM   4439 N N     . ILE A 1 753 ? -10.739 49.516  57.401  1.00 121.52 ?  734 ILE A N     1 
ATOM   4440 C CA    . ILE A 1 753 ? -11.372 48.428  58.180  1.00 123.30 ?  734 ILE A CA    1 
ATOM   4441 C C     . ILE A 1 753 ? -12.823 48.304  57.742  1.00 122.43 ?  734 ILE A C     1 
ATOM   4442 O O     . ILE A 1 753 ? -13.318 47.194  57.732  1.00 122.80 ?  734 ILE A O     1 
ATOM   4443 C CB    . ILE A 1 753 ? -11.272 48.733  59.679  1.00 116.08 ?  734 ILE A CB    1 
ATOM   4444 C CG1   . ILE A 1 753 ? -9.816  48.822  60.129  1.00 113.33 ?  734 ILE A CG1   1 
ATOM   4445 C CG2   . ILE A 1 753 ? -12.018 47.688  60.472  1.00 107.51 ?  734 ILE A CG2   1 
ATOM   4446 C CD1   . ILE A 1 753 ? -9.385  47.655  60.978  1.00 108.69 ?  734 ILE A CD1   1 
ATOM   4447 N N     . PHE A 1 754 ? -13.477 49.411  57.411  1.00 120.89 ?  735 PHE A N     1 
ATOM   4448 C CA    . PHE A 1 754 ? -14.920 49.297  57.089  1.00 121.45 ?  735 PHE A CA    1 
ATOM   4449 C C     . PHE A 1 754 ? -15.232 49.577  55.620  1.00 119.35 ?  735 PHE A C     1 
ATOM   4450 O O     . PHE A 1 754 ? -16.381 49.364  55.247  1.00 117.49 ?  735 PHE A O     1 
ATOM   4451 C CB    . PHE A 1 754 ? -15.721 50.272  57.948  1.00 125.80 ?  735 PHE A CB    1 
ATOM   4452 C CG    . PHE A 1 754 ? -15.963 49.850  59.373  1.00 119.80 ?  735 PHE A CG    1 
ATOM   4453 C CD1   . PHE A 1 754 ? -17.225 49.943  59.934  1.00 121.44 ?  735 PHE A CD1   1 
ATOM   4454 C CD2   . PHE A 1 754 ? -14.927 49.402  60.163  1.00 119.34 ?  735 PHE A CD2   1 
ATOM   4455 C CE1   . PHE A 1 754 ? -17.452 49.571  61.246  1.00 122.75 ?  735 PHE A CE1   1 
ATOM   4456 C CE2   . PHE A 1 754 ? -15.153 49.019  61.471  1.00 121.14 ?  735 PHE A CE2   1 
ATOM   4457 C CZ    . PHE A 1 754 ? -16.413 49.104  62.009  1.00 121.70 ?  735 PHE A CZ    1 
ATOM   4458 N N     . GLY A 1 755 ? -14.280 50.078  54.835  1.00 119.93 ?  736 GLY A N     1 
ATOM   4459 C CA    . GLY A 1 755 ? -14.571 50.351  53.413  1.00 127.39 ?  736 GLY A CA    1 
ATOM   4460 C C     . GLY A 1 755 ? -14.917 51.806  53.171  1.00 126.56 ?  736 GLY A C     1 
ATOM   4461 O O     . GLY A 1 755 ? -15.801 52.308  53.848  1.00 124.28 ?  736 GLY A O     1 
ATOM   4462 N N     . SER A 1 756 ? -14.402 52.380  52.089  1.00 128.34 ?  737 SER A N     1 
ATOM   4463 C CA    . SER A 1 756 ? -14.522 53.834  51.823  1.00 129.09 ?  737 SER A CA    1 
ATOM   4464 C C     . SER A 1 756 ? -15.968 54.310  51.723  1.00 134.16 ?  737 SER A C     1 
ATOM   4465 O O     . SER A 1 756 ? -16.226 55.445  52.106  1.00 132.76 ?  737 SER A O     1 
ATOM   4466 C CB    . SER A 1 756 ? -13.756 54.209  50.598  1.00 121.13 ?  737 SER A CB    1 
ATOM   4467 O OG    . SER A 1 756 ? -12.523 53.516  50.563  1.00 121.45 ?  737 SER A OG    1 
ATOM   4468 N N     . SER A 1 757 ? -16.856 53.527  51.133  1.00 135.46 ?  738 SER A N     1 
ATOM   4469 C CA    . SER A 1 757 ? -18.249 54.005  50.976  1.00 137.44 ?  738 SER A CA    1 
ATOM   4470 C C     . SER A 1 757 ? -18.920 54.188  52.332  1.00 132.52 ?  738 SER A C     1 
ATOM   4471 O O     . SER A 1 757 ? -19.656 55.163  52.509  1.00 127.00 ?  738 SER A O     1 
ATOM   4472 C CB    . SER A 1 757 ? -19.020 53.020  50.170  1.00 143.24 ?  738 SER A CB    1 
ATOM   4473 O OG    . SER A 1 757 ? -18.896 51.731  50.746  1.00 144.93 ?  738 SER A OG    1 
ATOM   4474 N N     . ALA A 1 758 ? -18.655 53.251  53.234  1.00 133.47 ?  739 ALA A N     1 
ATOM   4475 C CA    . ALA A 1 758 ? -19.320 53.152  54.553  1.00 137.19 ?  739 ALA A CA    1 
ATOM   4476 C C     . ALA A 1 758 ? -19.074 54.329  55.501  1.00 134.04 ?  739 ALA A C     1 
ATOM   4477 O O     . ALA A 1 758 ? -20.007 54.656  56.234  1.00 125.97 ?  739 ALA A O     1 
ATOM   4478 C CB    . ALA A 1 758 ? -18.958 51.842  55.196  1.00 126.16 ?  739 ALA A CB    1 
ATOM   4479 N N     . VAL A 1 759 ? -17.872 54.907  55.508  1.00 135.86 ?  740 VAL A N     1 
ATOM   4480 C CA    . VAL A 1 759 ? -17.493 55.965  56.490  1.00 124.87 ?  740 VAL A CA    1 
ATOM   4481 C C     . VAL A 1 759 ? -17.814 57.375  56.013  1.00 122.86 ?  740 VAL A C     1 
ATOM   4482 O O     . VAL A 1 759 ? -17.051 57.898  55.220  1.00 122.55 ?  740 VAL A O     1 
ATOM   4483 C CB    . VAL A 1 759 ? -15.978 55.921  56.677  1.00 125.05 ?  740 VAL A CB    1 
ATOM   4484 C CG1   . VAL A 1 759 ? -15.497 57.202  57.315  1.00 124.58 ?  740 VAL A CG1   1 
ATOM   4485 C CG2   . VAL A 1 759 ? -15.537 54.702  57.454  1.00 121.90 ?  740 VAL A CG2   1 
ATOM   4486 N N     . PRO A 1 760 ? -18.825 58.061  56.568  1.00 121.86 ?  741 PRO A N     1 
ATOM   4487 C CA    . PRO A 1 760 ? -19.131 59.427  56.175  1.00 125.13 ?  741 PRO A CA    1 
ATOM   4488 C C     . PRO A 1 760 ? -18.225 60.409  56.918  1.00 129.73 ?  741 PRO A C     1 
ATOM   4489 O O     . PRO A 1 760 ? -17.606 60.008  57.846  1.00 134.52 ?  741 PRO A O     1 
ATOM   4490 C CB    . PRO A 1 760 ? -20.553 59.610  56.700  1.00 122.00 ?  741 PRO A CB    1 
ATOM   4491 C CG    . PRO A 1 760 ? -20.585 58.758  57.922  1.00 127.43 ?  741 PRO A CG    1 
ATOM   4492 C CD    . PRO A 1 760 ? -19.727 57.562  57.585  1.00 122.29 ?  741 PRO A CD    1 
ATOM   4493 N N     . GLN A 1 761 ? -18.137 61.654  56.462  1.00 128.06 ?  742 GLN A N     1 
ATOM   4494 C CA    . GLN A 1 761 ? -17.331 62.628  57.232  1.00 127.68 ?  742 GLN A CA    1 
ATOM   4495 C C     . GLN A 1 761 ? -18.083 62.888  58.531  1.00 132.77 ?  742 GLN A C     1 
ATOM   4496 O O     . GLN A 1 761 ? -19.306 63.005  58.480  1.00 135.29 ?  742 GLN A O     1 
ATOM   4497 C CB    . GLN A 1 761 ? -17.153 63.929  56.461  1.00 128.81 ?  742 GLN A CB    1 
ATOM   4498 C CG    . GLN A 1 761 ? -16.172 63.813  55.311  1.00 129.54 ?  742 GLN A CG    1 
ATOM   4499 C CD    . GLN A 1 761 ? -14.772 64.194  55.711  1.00 126.01 ?  742 GLN A CD    1 
ATOM   4500 O OE1   . GLN A 1 761 ? -13.799 63.608  55.255  1.00 127.02 ?  742 GLN A OE1   1 
ATOM   4501 N NE2   . GLN A 1 761 ? -14.663 65.197  56.560  1.00 122.91 ?  742 GLN A NE2   1 
ATOM   4502 N N     . PRO A 1 762 ? -17.396 62.981  59.681  1.00 130.30 ?  743 PRO A N     1 
ATOM   4503 C CA    . PRO A 1 762 ? -18.043 63.206  60.971  1.00 125.21 ?  743 PRO A CA    1 
ATOM   4504 C C     . PRO A 1 762 ? -18.568 64.626  61.161  1.00 119.91 ?  743 PRO A C     1 
ATOM   4505 O O     . PRO A 1 762 ? -17.931 65.530  60.737  1.00 117.05 ?  743 PRO A O     1 
ATOM   4506 C CB    . PRO A 1 762 ? -16.862 63.092  61.920  1.00 127.34 ?  743 PRO A CB    1 
ATOM   4507 C CG    . PRO A 1 762 ? -15.728 63.597  61.091  1.00 118.65 ?  743 PRO A CG    1 
ATOM   4508 C CD    . PRO A 1 762 ? -15.954 62.893  59.780  1.00 121.55 ?  743 PRO A CD    1 
ATOM   4509 N N     . LYS A 1 763 ? -19.673 64.768  61.879  1.00 120.74 ?  744 LYS A N     1 
ATOM   4510 C CA    . LYS A 1 763 ? -20.258 66.111  62.081  1.00 125.49 ?  744 LYS A CA    1 
ATOM   4511 C C     . LYS A 1 763 ? -19.362 66.945  62.990  1.00 131.61 ?  744 LYS A C     1 
ATOM   4512 O O     . LYS A 1 763 ? -18.887 67.979  62.523  1.00 129.01 ?  744 LYS A O     1 
ATOM   4513 C CB    . LYS A 1 763 ? -21.678 65.987  62.623  1.00 126.04 ?  744 LYS A CB    1 
ATOM   4514 C CG    . LYS A 1 763 ? -22.631 65.293  61.667  1.00 133.96 ?  744 LYS A CG    1 
ATOM   4515 C CD    . LYS A 1 763 ? -21.949 64.891  60.382  1.00 144.26 ?  744 LYS A CD    1 
ATOM   4516 C CE    . LYS A 1 763 ? -22.589 65.490  59.146  1.00 139.67 ?  744 LYS A CE    1 
ATOM   4517 N NZ    . LYS A 1 763 ? -24.067 65.365  59.163  1.00 143.64 ?  744 LYS A NZ    1 
ATOM   4518 N N     . GLU A 1 764 ? -19.159 66.528  64.239  1.00 131.00 ?  745 GLU A N     1 
ATOM   4519 C CA    . GLU A 1 764 ? -18.300 67.307  65.133  1.00 120.83 ?  745 GLU A CA    1 
ATOM   4520 C C     . GLU A 1 764 ? -17.088 66.471  65.544  1.00 111.89 ?  745 GLU A C     1 
ATOM   4521 O O     . GLU A 1 764 ? -17.196 65.247  65.678  1.00 109.27 ?  745 GLU A O     1 
ATOM   4522 C CB    . GLU A 1 764 ? -19.081 67.791  66.373  1.00 113.35 ?  745 GLU A CB    1 
ATOM   4523 C CG    . GLU A 1 764 ? -20.185 68.833  66.094  1.00 120.72 ?  745 GLU A CG    1 
ATOM   4524 C CD    . GLU A 1 764 ? -19.644 70.179  65.537  1.00 132.43 ?  745 GLU A CD    1 
ATOM   4525 O OE1   . GLU A 1 764 ? -18.424 70.458  65.677  1.00 134.87 ?  745 GLU A OE1   1 
ATOM   4526 O OE2   . GLU A 1 764 ? -20.445 70.970  64.971  1.00 130.80 ?  745 GLU A OE2   1 
ATOM   4527 N N     . THR A 1 765 ? -15.925 67.124  65.718  1.00 108.09 ?  746 THR A N     1 
ATOM   4528 C CA    . THR A 1 765 ? -14.721 66.424  66.182  1.00 111.00 ?  746 THR A CA    1 
ATOM   4529 C C     . THR A 1 765 ? -13.849 67.262  67.128  1.00 117.38 ?  746 THR A C     1 
ATOM   4530 O O     . THR A 1 765 ? -13.677 68.481  66.953  1.00 119.56 ?  746 THR A O     1 
ATOM   4531 C CB    . THR A 1 765 ? -13.826 65.935  65.033  1.00 105.08 ?  746 THR A CB    1 
ATOM   4532 O OG1   . THR A 1 765 ? -13.504 67.024  64.164  1.00 113.79 ?  746 THR A OG1   1 
ATOM   4533 C CG2   . THR A 1 765 ? -14.477 64.816  64.282  1.00 106.87 ?  746 THR A CG2   1 
ATOM   4534 N N     . VAL A 1 766 ? -13.221 66.530  68.074  1.00 111.44 ?  747 VAL A N     1 
ATOM   4535 C CA    . VAL A 1 766 ? -12.523 67.018  69.267  1.00 101.98 ?  747 VAL A CA    1 
ATOM   4536 C C     . VAL A 1 766 ? -11.183 66.297  69.392  1.00 99.35  ?  747 VAL A C     1 
ATOM   4537 O O     . VAL A 1 766 ? -11.142 65.061  69.378  1.00 100.88 ?  747 VAL A O     1 
ATOM   4538 C CB    . VAL A 1 766 ? -13.332 66.736  70.550  1.00 100.03 ?  747 VAL A CB    1 
ATOM   4539 C CG1   . VAL A 1 766 ? -12.582 67.252  71.718  1.00 106.43 ?  747 VAL A CG1   1 
ATOM   4540 C CG2   . VAL A 1 766 ? -14.734 67.319  70.508  1.00 99.57  ?  747 VAL A CG2   1 
ATOM   4541 N N     . VAL A 1 767 ? -10.100 67.047  69.586  1.00 96.81  ?  748 VAL A N     1 
ATOM   4542 C CA    . VAL A 1 767 ? -8.780  66.456  69.819  1.00 97.89  ?  748 VAL A CA    1 
ATOM   4543 C C     . VAL A 1 767 ? -8.194  67.022  71.108  1.00 107.38 ?  748 VAL A C     1 
ATOM   4544 O O     . VAL A 1 767 ? -7.944  68.233  71.198  1.00 111.32 ?  748 VAL A O     1 
ATOM   4545 C CB    . VAL A 1 767 ? -7.818  66.715  68.654  1.00 102.96 ?  748 VAL A CB    1 
ATOM   4546 C CG1   . VAL A 1 767 ? -6.457  66.100  68.953  1.00 99.07  ?  748 VAL A CG1   1 
ATOM   4547 C CG2   . VAL A 1 767 ? -8.384  66.161  67.384  1.00 111.31 ?  748 VAL A CG2   1 
ATOM   4548 N N     . SER A 1 768 ? -7.938  66.146  72.089  1.00 105.46 ?  749 SER A N     1 
ATOM   4549 C CA    . SER A 1 768 ? -7.282  66.549  73.332  1.00 95.35  ?  749 SER A CA    1 
ATOM   4550 C C     . SER A 1 768 ? -5.778  66.720  73.126  1.00 96.68  ?  749 SER A C     1 
ATOM   4551 O O     . SER A 1 768 ? -5.160  66.070  72.281  1.00 103.44 ?  749 SER A O     1 
ATOM   4552 C CB    . SER A 1 768 ? -7.501  65.525  74.447  1.00 90.71  ?  749 SER A CB    1 
ATOM   4553 O OG    . SER A 1 768 ? -6.759  64.343  74.212  1.00 89.22  ?  749 SER A OG    1 
ATOM   4554 N N     . ARG A 1 769 ? -5.195  67.621  73.910  1.00 101.74 ?  750 ARG A N     1 
ATOM   4555 C CA    . ARG A 1 769 ? -3.745  67.852  73.959  1.00 102.65 ?  750 ARG A CA    1 
ATOM   4556 C C     . ARG A 1 769 ? -3.425  68.174  75.421  1.00 103.72 ?  750 ARG A C     1 
ATOM   4557 O O     . ARG A 1 769 ? -3.408  69.341  75.836  1.00 99.86  ?  750 ARG A O     1 
ATOM   4558 C CB    . ARG A 1 769 ? -3.278  68.953  73.013  1.00 105.96 ?  750 ARG A CB    1 
ATOM   4559 C CG    . ARG A 1 769 ? -3.396  68.620  71.522  1.00 108.15 ?  750 ARG A CG    1 
ATOM   4560 C CD    . ARG A 1 769 ? -2.982  69.787  70.620  1.00 111.02 ?  750 ARG A CD    1 
ATOM   4561 N NE    . ARG A 1 769 ? -3.116  69.385  69.224  1.00 115.95 ?  750 ARG A NE    1 
ATOM   4562 C CZ    . ARG A 1 769 ? -4.246  69.486  68.526  1.00 121.66 ?  750 ARG A CZ    1 
ATOM   4563 N NH1   . ARG A 1 769 ? -5.342  69.983  69.092  1.00 123.78 ?  750 ARG A NH1   1 
ATOM   4564 N NH2   . ARG A 1 769 ? -4.289  69.074  67.265  1.00 121.22 ?  750 ARG A NH2   1 
ATOM   4565 N N     . TRP A 1 770 ? -3.208  67.111  76.199  1.00 103.59 ?  751 TRP A N     1 
ATOM   4566 C CA    . TRP A 1 770 ? -3.058  67.265  77.635  1.00 92.49  ?  751 TRP A CA    1 
ATOM   4567 C C     . TRP A 1 770 ? -1.670  67.755  77.996  1.00 91.75  ?  751 TRP A C     1 
ATOM   4568 O O     . TRP A 1 770 ? -1.541  68.599  78.883  1.00 101.54 ?  751 TRP A O     1 
ATOM   4569 C CB    . TRP A 1 770 ? -3.369  65.956  78.356  1.00 89.67  ?  751 TRP A CB    1 
ATOM   4570 C CG    . TRP A 1 770 ? -4.828  65.580  78.340  1.00 93.83  ?  751 TRP A CG    1 
ATOM   4571 C CD1   . TRP A 1 770 ? -5.421  64.621  77.556  1.00 97.36  ?  751 TRP A CD1   1 
ATOM   4572 C CD2   . TRP A 1 770 ? -5.882  66.136  79.148  1.00 92.97  ?  751 TRP A CD2   1 
ATOM   4573 N NE1   . TRP A 1 770 ? -6.776  64.551  77.821  1.00 95.74  ?  751 TRP A NE1   1 
ATOM   4574 C CE2   . TRP A 1 770 ? -7.084  65.466  78.796  1.00 97.32  ?  751 TRP A CE2   1 
ATOM   4575 C CE3   . TRP A 1 770 ? -5.929  67.120  80.133  1.00 91.71  ?  751 TRP A CE3   1 
ATOM   4576 C CZ2   . TRP A 1 770 ? -8.322  65.765  79.394  1.00 95.62  ?  751 TRP A CZ2   1 
ATOM   4577 C CZ3   . TRP A 1 770 ? -7.168  67.409  80.735  1.00 94.86  ?  751 TRP A CZ3   1 
ATOM   4578 C CH2   . TRP A 1 770 ? -8.343  66.734  80.359  1.00 90.53  ?  751 TRP A CH2   1 
ATOM   4579 N N     . ARG A 1 771 ? -0.614  67.266  77.340  1.00 86.59  ?  752 ARG A N     1 
ATOM   4580 C CA    . ARG A 1 771 ? 0.690   67.844  77.651  1.00 85.23  ?  752 ARG A CA    1 
ATOM   4581 C C     . ARG A 1 771 ? 0.698   69.337  77.338  1.00 89.76  ?  752 ARG A C     1 
ATOM   4582 O O     . ARG A 1 771 ? 1.517   70.094  77.885  1.00 87.05  ?  752 ARG A O     1 
ATOM   4583 C CB    . ARG A 1 771 ? 1.811   67.132  76.894  1.00 88.44  ?  752 ARG A CB    1 
ATOM   4584 C CG    . ARG A 1 771 ? 3.191   67.503  77.417  1.00 83.75  ?  752 ARG A CG    1 
ATOM   4585 C CD    . ARG A 1 771 ? 3.374   66.893  78.766  1.00 87.87  ?  752 ARG A CD    1 
ATOM   4586 N NE    . ARG A 1 771 ? 3.866   65.518  78.687  1.00 94.67  ?  752 ARG A NE    1 
ATOM   4587 C CZ    . ARG A 1 771 ? 4.038   64.713  79.746  1.00 100.68 ?  752 ARG A CZ    1 
ATOM   4588 N NH1   . ARG A 1 771 ? 3.672   65.106  80.978  1.00 92.71  ?  752 ARG A NH1   1 
ATOM   4589 N NH2   . ARG A 1 771 ? 4.526   63.480  79.566  1.00 103.71 ?  752 ARG A NH2   1 
ATOM   4590 N N     . ALA A 1 772 ? -0.244  69.777  76.506  1.00 97.32  ?  753 ALA A N     1 
ATOM   4591 C CA    . ALA A 1 772 ? -0.375  71.171  76.118  1.00 98.75  ?  753 ALA A CA    1 
ATOM   4592 C C     . ALA A 1 772 ? -1.234  71.986  77.065  1.00 91.25  ?  753 ALA A C     1 
ATOM   4593 O O     . ALA A 1 772 ? -1.082  73.201  77.106  1.00 90.42  ?  753 ALA A O     1 
ATOM   4594 C CB    . ALA A 1 772 ? -0.978  71.258  74.718  1.00 102.53 ?  753 ALA A CB    1 
ATOM   4595 N N     . ASP A 1 773 ? -2.141  71.355  77.794  1.00 98.82  ?  754 ASP A N     1 
ATOM   4596 C CA    . ASP A 1 773 ? -3.023  72.052  78.737  1.00 99.39  ?  754 ASP A CA    1 
ATOM   4597 C C     . ASP A 1 773 ? -2.245  72.540  79.964  1.00 99.55  ?  754 ASP A C     1 
ATOM   4598 O O     . ASP A 1 773 ? -1.652  71.718  80.688  1.00 96.58  ?  754 ASP A O     1 
ATOM   4599 C CB    . ASP A 1 773 ? -4.147  71.120  79.198  1.00 96.77  ?  754 ASP A CB    1 
ATOM   4600 C CG    . ASP A 1 773 ? -5.190  71.839  80.042  1.00 96.59  ?  754 ASP A CG    1 
ATOM   4601 O OD1   . ASP A 1 773 ? -5.213  73.087  80.024  1.00 102.60 ?  754 ASP A OD1   1 
ATOM   4602 O OD2   . ASP A 1 773 ? -5.938  71.169  80.784  1.00 96.40  ?  754 ASP A OD2   1 
ATOM   4603 N N     . PRO A 1 774 ? -2.256  73.844  80.266  1.00 96.83  ?  755 PRO A N     1 
ATOM   4604 C CA    . PRO A 1 774 ? -1.498  74.339  81.422  1.00 97.45  ?  755 PRO A CA    1 
ATOM   4605 C C     . PRO A 1 774 ? -2.086  73.956  82.776  1.00 101.33 ?  755 PRO A C     1 
ATOM   4606 O O     . PRO A 1 774 ? -1.427  74.204  83.797  1.00 101.04 ?  755 PRO A O     1 
ATOM   4607 C CB    . PRO A 1 774 ? -1.535  75.849  81.231  1.00 94.05  ?  755 PRO A CB    1 
ATOM   4608 C CG    . PRO A 1 774 ? -2.772  76.077  80.453  1.00 90.73  ?  755 PRO A CG    1 
ATOM   4609 C CD    . PRO A 1 774 ? -2.905  74.937  79.529  1.00 91.89  ?  755 PRO A CD    1 
ATOM   4610 N N     . TRP A 1 775 ? -3.301  73.404  82.831  1.00 98.77  ?  756 TRP A N     1 
ATOM   4611 C CA    . TRP A 1 775 ? -3.888  72.912  84.073  1.00 96.85  ?  756 TRP A CA    1 
ATOM   4612 C C     . TRP A 1 775 ? -3.795  71.383  84.196  1.00 98.43  ?  756 TRP A C     1 
ATOM   4613 O O     . TRP A 1 775 ? -4.474  70.774  85.041  1.00 93.92  ?  756 TRP A O     1 
ATOM   4614 C CB    . TRP A 1 775 ? -5.337  73.409  84.195  1.00 94.77  ?  756 TRP A CB    1 
ATOM   4615 C CG    . TRP A 1 775 ? -5.575  74.873  83.766  1.00 95.56  ?  756 TRP A CG    1 
ATOM   4616 C CD1   . TRP A 1 775 ? -6.593  75.334  82.983  1.00 96.03  ?  756 TRP A CD1   1 
ATOM   4617 C CD2   . TRP A 1 775 ? -4.793  76.047  84.129  1.00 101.45 ?  756 TRP A CD2   1 
ATOM   4618 N NE1   . TRP A 1 775 ? -6.496  76.709  82.825  1.00 95.95  ?  756 TRP A NE1   1 
ATOM   4619 C CE2   . TRP A 1 775 ? -5.406  77.169  83.513  1.00 95.35  ?  756 TRP A CE2   1 
ATOM   4620 C CE3   . TRP A 1 775 ? -3.646  76.257  84.920  1.00 102.64 ?  756 TRP A CE3   1 
ATOM   4621 C CZ2   . TRP A 1 775 ? -4.912  78.470  83.656  1.00 91.24  ?  756 TRP A CZ2   1 
ATOM   4622 C CZ3   . TRP A 1 775 ? -3.153  77.566  85.057  1.00 98.85  ?  756 TRP A CZ3   1 
ATOM   4623 C CH2   . TRP A 1 775 ? -3.789  78.648  84.425  1.00 92.79  ?  756 TRP A CH2   1 
ATOM   4624 N N     . ALA A 1 776 ? -2.978  70.759  83.344  1.00 99.31  ?  757 ALA A N     1 
ATOM   4625 C CA    . ALA A 1 776 ? -2.522  69.383  83.479  1.00 93.02  ?  757 ALA A CA    1 
ATOM   4626 C C     . ALA A 1 776 ? -1.004  69.378  83.342  1.00 93.07  ?  757 ALA A C     1 
ATOM   4627 O O     . ALA A 1 776 ? -0.296  69.224  84.344  1.00 94.12  ?  757 ALA A O     1 
ATOM   4628 C CB    . ALA A 1 776 ? -3.157  68.467  82.431  1.00 89.37  ?  757 ALA A CB    1 
ATOM   4629 N N     . ARG A 1 777 ? -0.508  69.639  82.122  1.00 87.70  ?  758 ARG A N     1 
ATOM   4630 C CA    . ARG A 1 777 ? 0.891   69.439  81.750  1.00 84.79  ?  758 ARG A CA    1 
ATOM   4631 C C     . ARG A 1 777 ? 1.203   67.964  81.643  1.00 85.37  ?  758 ARG A C     1 
ATOM   4632 O O     . ARG A 1 777 ? 2.320   67.530  81.961  1.00 84.38  ?  758 ARG A O     1 
ATOM   4633 C CB    . ARG A 1 777 ? 1.864   70.111  82.720  1.00 90.24  ?  758 ARG A CB    1 
ATOM   4634 C CG    . ARG A 1 777 ? 1.775   71.580  82.636  1.00 95.23  ?  758 ARG A CG    1 
ATOM   4635 C CD    . ARG A 1 777 ? 2.593   72.087  81.495  1.00 98.23  ?  758 ARG A CD    1 
ATOM   4636 N NE    . ARG A 1 777 ? 2.493   73.539  81.433  1.00 105.26 ?  758 ARG A NE    1 
ATOM   4637 C CZ    . ARG A 1 777 ? 1.729   74.161  80.535  1.00 106.86 ?  758 ARG A CZ    1 
ATOM   4638 N NH1   . ARG A 1 777 ? 1.047   73.441  79.636  1.00 107.12 ?  758 ARG A NH1   1 
ATOM   4639 N NH2   . ARG A 1 777 ? 1.648   75.483  80.510  1.00 101.32 ?  758 ARG A NH2   1 
ATOM   4640 N N     . GLY A 1 778 ? 0.201   67.216  81.200  1.00 84.94  ?  759 GLY A N     1 
ATOM   4641 C CA    . GLY A 1 778 ? 0.294   65.781  81.047  1.00 86.84  ?  759 GLY A CA    1 
ATOM   4642 C C     . GLY A 1 778 ? -1.074  65.159  81.266  1.00 90.27  ?  759 GLY A C     1 
ATOM   4643 O O     . GLY A 1 778 ? -2.095  65.854  81.328  1.00 88.54  ?  759 GLY A O     1 
ATOM   4644 N N     . SER A 1 779 ? -1.067  63.825  81.394  1.00 85.50  ?  760 SER A N     1 
ATOM   4645 C CA    . SER A 1 779 ? -2.292  63.038  81.513  1.00 85.09  ?  760 SER A CA    1 
ATOM   4646 C C     . SER A 1 779 ? -2.459  62.461  82.913  1.00 98.65  ?  760 SER A C     1 
ATOM   4647 O O     . SER A 1 779 ? -3.270  62.956  83.695  1.00 107.93 ?  760 SER A O     1 
ATOM   4648 C CB    . SER A 1 779 ? -2.301  61.925  80.474  1.00 90.06  ?  760 SER A CB    1 
ATOM   4649 O OG    . SER A 1 779 ? -1.181  61.075  80.659  1.00 94.55  ?  760 SER A OG    1 
ATOM   4650 N N     . TYR A 1 780 ? -1.717  61.407  83.242  1.00 98.16  ?  761 TYR A N     1 
ATOM   4651 C CA    . TYR A 1 780 ? -1.588  60.947  84.621  1.00 90.06  ?  761 TYR A CA    1 
ATOM   4652 C C     . TYR A 1 780 ? -0.129  60.566  84.841  1.00 93.07  ?  761 TYR A C     1 
ATOM   4653 O O     . TYR A 1 780 ? 0.754   60.940  84.061  1.00 94.77  ?  761 TYR A O     1 
ATOM   4654 C CB    . TYR A 1 780 ? -2.582  59.820  84.941  1.00 92.37  ?  761 TYR A CB    1 
ATOM   4655 C CG    . TYR A 1 780 ? -2.836  58.825  83.834  1.00 99.93  ?  761 TYR A CG    1 
ATOM   4656 C CD1   . TYR A 1 780 ? -1.947  57.782  83.567  1.00 100.52 ?  761 TYR A CD1   1 
ATOM   4657 C CD2   . TYR A 1 780 ? -3.991  58.927  83.050  1.00 102.99 ?  761 TYR A CD2   1 
ATOM   4658 C CE1   . TYR A 1 780 ? -2.210  56.879  82.531  1.00 101.14 ?  761 TYR A CE1   1 
ATOM   4659 C CE2   . TYR A 1 780 ? -4.262  58.037  82.021  1.00 98.63  ?  761 TYR A CE2   1 
ATOM   4660 C CZ    . TYR A 1 780 ? -3.369  57.023  81.771  1.00 100.48 ?  761 TYR A CZ    1 
ATOM   4661 O OH    . TYR A 1 780 ? -3.653  56.141  80.771  1.00 108.34 ?  761 TYR A OH    1 
ATOM   4662 N N     . SER A 1 781 ? 0.145   59.843  85.920  1.00 95.81  ?  762 SER A N     1 
ATOM   4663 C CA    . SER A 1 781 ? 1.517   59.643  86.356  1.00 93.88  ?  762 SER A CA    1 
ATOM   4664 C C     . SER A 1 781 ? 1.905   58.183  86.223  1.00 98.16  ?  762 SER A C     1 
ATOM   4665 O O     . SER A 1 781 ? 1.071   57.289  86.015  1.00 99.62  ?  762 SER A O     1 
ATOM   4666 C CB    . SER A 1 781 ? 1.722   60.103  87.802  1.00 92.12  ?  762 SER A CB    1 
ATOM   4667 O OG    . SER A 1 781 ? 0.732   59.538  88.638  1.00 95.85  ?  762 SER A OG    1 
ATOM   4668 N N     . TYR A 1 782 ? 3.204   57.965  86.351  1.00 95.89  ?  763 TYR A N     1 
ATOM   4669 C CA    . TYR A 1 782 ? 3.783   56.648  86.219  1.00 95.63  ?  763 TYR A CA    1 
ATOM   4670 C C     . TYR A 1 782 ? 4.985   56.585  87.132  1.00 98.43  ?  763 TYR A C     1 
ATOM   4671 O O     . TYR A 1 782 ? 5.462   57.608  87.643  1.00 99.83  ?  763 TYR A O     1 
ATOM   4672 C CB    . TYR A 1 782 ? 4.200   56.349  84.779  1.00 93.28  ?  763 TYR A CB    1 
ATOM   4673 C CG    . TYR A 1 782 ? 5.290   57.242  84.198  1.00 90.74  ?  763 TYR A CG    1 
ATOM   4674 C CD1   . TYR A 1 782 ? 6.636   56.901  84.345  1.00 90.83  ?  763 TYR A CD1   1 
ATOM   4675 C CD2   . TYR A 1 782 ? 4.980   58.365  83.420  1.00 91.26  ?  763 TYR A CD2   1 
ATOM   4676 C CE1   . TYR A 1 782 ? 7.648   57.670  83.780  1.00 91.92  ?  763 TYR A CE1   1 
ATOM   4677 C CE2   . TYR A 1 782 ? 6.004   59.157  82.847  1.00 93.25  ?  763 TYR A CE2   1 
ATOM   4678 C CZ    . TYR A 1 782 ? 7.341   58.793  83.039  1.00 93.89  ?  763 TYR A CZ    1 
ATOM   4679 O OH    . TYR A 1 782 ? 8.387   59.534  82.517  1.00 94.54  ?  763 TYR A OH    1 
ATOM   4680 N N     . VAL A 1 783 ? 5.486   55.371  87.326  1.00 96.30  ?  764 VAL A N     1 
ATOM   4681 C CA    . VAL A 1 783 ? 6.686   55.174  88.123  1.00 95.90  ?  764 VAL A CA    1 
ATOM   4682 C C     . VAL A 1 783 ? 7.871   55.255  87.168  1.00 93.47  ?  764 VAL A C     1 
ATOM   4683 O O     . VAL A 1 783 ? 8.225   54.274  86.511  1.00 95.26  ?  764 VAL A O     1 
ATOM   4684 C CB    . VAL A 1 783 ? 6.656   53.845  88.865  1.00 99.17  ?  764 VAL A CB    1 
ATOM   4685 C CG1   . VAL A 1 783 ? 7.756   53.845  89.923  1.00 96.67  ?  764 VAL A CG1   1 
ATOM   4686 C CG2   . VAL A 1 783 ? 5.234   53.565  89.407  1.00 95.85  ?  764 VAL A CG2   1 
ATOM   4687 N N     . ALA A 1 784 ? 8.478   56.430  87.079  1.00 91.26  ?  765 ALA A N     1 
ATOM   4688 C CA    . ALA A 1 784 ? 9.592   56.601  86.169  1.00 90.72  ?  765 ALA A CA    1 
ATOM   4689 C C     . ALA A 1 784 ? 10.758  55.735  86.598  1.00 92.03  ?  765 ALA A C     1 
ATOM   4690 O O     . ALA A 1 784 ? 10.891  55.386  87.772  1.00 93.11  ?  765 ALA A O     1 
ATOM   4691 C CB    . ALA A 1 784 ? 10.022  58.058  86.130  1.00 99.41  ?  765 ALA A CB    1 
ATOM   4692 N N     . ALA A 1 785 ? 11.591  55.373  85.620  1.00 95.44  ?  766 ALA A N     1 
ATOM   4693 C CA    . ALA A 1 785 ? 12.807  54.624  85.899  1.00 100.60 ?  766 ALA A CA    1 
ATOM   4694 C C     . ALA A 1 785 ? 13.647  55.386  86.906  1.00 102.71 ?  766 ALA A C     1 
ATOM   4695 O O     . ALA A 1 785 ? 13.804  56.604  86.807  1.00 101.69 ?  766 ALA A O     1 
ATOM   4696 C CB    . ALA A 1 785 ? 13.612  54.382  84.622  1.00 100.89 ?  766 ALA A CB    1 
ATOM   4697 N N     . GLY A 1 786 ? 14.153  54.667  87.904  1.00 106.28 ?  767 GLY A N     1 
ATOM   4698 C CA    . GLY A 1 786 ? 14.832  55.301  89.015  1.00 108.65 ?  767 GLY A CA    1 
ATOM   4699 C C     . GLY A 1 786 ? 13.932  55.812  90.126  1.00 104.94 ?  767 GLY A C     1 
ATOM   4700 O O     . GLY A 1 786 ? 14.439  56.139  91.212  1.00 97.91  ?  767 GLY A O     1 
ATOM   4701 N N     . SER A 1 787 ? 12.620  55.909  89.893  1.00 104.08 ?  768 SER A N     1 
ATOM   4702 C CA    . SER A 1 787 ? 11.664  56.263  90.930  1.00 96.64  ?  768 SER A CA    1 
ATOM   4703 C C     . SER A 1 787 ? 11.107  54.970  91.538  1.00 100.56 ?  768 SER A C     1 
ATOM   4704 O O     . SER A 1 787 ? 11.461  53.854  91.136  1.00 104.83 ?  768 SER A O     1 
ATOM   4705 C CB    . SER A 1 787 ? 10.576  57.171  90.341  1.00 100.00 ?  768 SER A CB    1 
ATOM   4706 O OG    . SER A 1 787 ? 9.540   57.502  91.247  1.00 95.94  ?  768 SER A OG    1 
ATOM   4707 N N     . SER A 1 788 ? 10.239  55.115  92.534  1.00 101.22 ?  769 SER A N     1 
ATOM   4708 C CA    . SER A 1 788 ? 9.663   53.985  93.252  1.00 98.27  ?  769 SER A CA    1 
ATOM   4709 C C     . SER A 1 788 ? 8.235   54.341  93.650  1.00 95.08  ?  769 SER A C     1 
ATOM   4710 O O     . SER A 1 788 ? 7.785   55.471  93.463  1.00 98.99  ?  769 SER A O     1 
ATOM   4711 C CB    . SER A 1 788 ? 10.540  53.607  94.451  1.00 90.01  ?  769 SER A CB    1 
ATOM   4712 O OG    . SER A 1 788 ? 10.724  54.722  95.298  1.00 91.58  ?  769 SER A OG    1 
ATOM   4713 N N     . GLY A 1 789 ? 7.493   53.357  94.155  1.00 95.97  ?  770 GLY A N     1 
ATOM   4714 C CA    . GLY A 1 789 ? 6.218   53.748  94.729  1.00 101.25 ?  770 GLY A CA    1 
ATOM   4715 C C     . GLY A 1 789 ? 6.380   54.626  95.955  1.00 106.10 ?  770 GLY A C     1 
ATOM   4716 O O     . GLY A 1 789 ? 5.422   55.285  96.386  1.00 101.21 ?  770 GLY A O     1 
ATOM   4717 N N     . ASN A 1 790 ? 7.594   54.666  96.497  1.00 106.06 ?  771 ASN A N     1 
ATOM   4718 C CA    . ASN A 1 790 ? 7.898   55.396  97.709  1.00 105.95 ?  771 ASN A CA    1 
ATOM   4719 C C     . ASN A 1 790 ? 8.073   56.897  97.462  1.00 103.43 ?  771 ASN A C     1 
ATOM   4720 O O     . ASN A 1 790 ? 7.956   57.691  98.407  1.00 105.52 ?  771 ASN A O     1 
ATOM   4721 C CB    . ASN A 1 790 ? 9.136   54.755  98.345  1.00 109.19 ?  771 ASN A CB    1 
ATOM   4722 C CG    . ASN A 1 790 ? 9.670   55.547  99.493  1.00 118.95 ?  771 ASN A CG    1 
ATOM   4723 O OD1   . ASN A 1 790 ? 10.581  56.367  99.316  1.00 117.97 ?  771 ASN A OD1   1 
ATOM   4724 N ND2   . ASN A 1 790 ? 9.107   55.324  100.688 1.00 124.40 ?  771 ASN A ND2   1 
ATOM   4725 N N     . ASP A 1 791 ? 8.317   57.320  96.219  1.00 102.10 ?  772 ASP A N     1 
ATOM   4726 C CA    . ASP A 1 791 ? 8.220   58.750  95.955  1.00 98.73  ?  772 ASP A CA    1 
ATOM   4727 C C     . ASP A 1 791 ? 6.775   59.224  95.963  1.00 99.54  ?  772 ASP A C     1 
ATOM   4728 O O     . ASP A 1 791 ? 6.538   60.403  96.232  1.00 103.80 ?  772 ASP A O     1 
ATOM   4729 C CB    . ASP A 1 791 ? 8.891   59.137  94.633  1.00 93.56  ?  772 ASP A CB    1 
ATOM   4730 C CG    . ASP A 1 791 ? 10.419  59.099  94.713  1.00 93.49  ?  772 ASP A CG    1 
ATOM   4731 O OD1   . ASP A 1 791 ? 10.998  58.609  95.714  1.00 90.06  ?  772 ASP A OD1   1 
ATOM   4732 O OD2   . ASP A 1 791 ? 11.049  59.596  93.764  1.00 98.43  ?  772 ASP A OD2   1 
ATOM   4733 N N     . TYR A 1 792 ? 5.809   58.333  95.705  1.00 98.90  ?  773 TYR A N     1 
ATOM   4734 C CA    . TYR A 1 792 ? 4.398   58.696  95.841  1.00 98.84  ?  773 TYR A CA    1 
ATOM   4735 C C     . TYR A 1 792 ? 4.046   59.034  97.289  1.00 101.67 ?  773 TYR A C     1 
ATOM   4736 O O     . TYR A 1 792 ? 3.224   59.925  97.549  1.00 103.08 ?  773 TYR A O     1 
ATOM   4737 C CB    . TYR A 1 792 ? 3.515   57.554  95.348  1.00 101.53 ?  773 TYR A CB    1 
ATOM   4738 C CG    . TYR A 1 792 ? 3.367   57.443  93.840  1.00 109.44 ?  773 TYR A CG    1 
ATOM   4739 C CD1   . TYR A 1 792 ? 2.260   57.987  93.201  1.00 109.07 ?  773 TYR A CD1   1 
ATOM   4740 C CD2   . TYR A 1 792 ? 4.310   56.762  93.055  1.00 106.16 ?  773 TYR A CD2   1 
ATOM   4741 C CE1   . TYR A 1 792 ? 2.095   57.886  91.826  1.00 106.70 ?  773 TYR A CE1   1 
ATOM   4742 C CE2   . TYR A 1 792 ? 4.151   56.656  91.672  1.00 105.01 ?  773 TYR A CE2   1 
ATOM   4743 C CZ    . TYR A 1 792 ? 3.029   57.221  91.063  1.00 107.19 ?  773 TYR A CZ    1 
ATOM   4744 O OH    . TYR A 1 792 ? 2.824   57.148  89.690  1.00 114.58 ?  773 TYR A OH    1 
ATOM   4745 N N     . ASP A 1 793 ? 4.640   58.315  98.248  1.00 100.82 ?  774 ASP A N     1 
ATOM   4746 C CA    . ASP A 1 793 ? 4.434   58.639  99.653  1.00 89.36  ?  774 ASP A CA    1 
ATOM   4747 C C     . ASP A 1 793 ? 5.060   59.983  100.003 1.00 94.36  ?  774 ASP A C     1 
ATOM   4748 O O     . ASP A 1 793 ? 4.461   60.771  100.747 1.00 101.12 ?  774 ASP A O     1 
ATOM   4749 C CB    . ASP A 1 793 ? 5.002   57.530  100.545 1.00 94.54  ?  774 ASP A CB    1 
ATOM   4750 C CG    . ASP A 1 793 ? 4.053   56.316  100.684 1.00 101.64 ?  774 ASP A CG    1 
ATOM   4751 O OD1   . ASP A 1 793 ? 2.859   56.422  100.283 1.00 100.42 ?  774 ASP A OD1   1 
ATOM   4752 O OD2   . ASP A 1 793 ? 4.505   55.265  101.222 1.00 98.61  ?  774 ASP A OD2   1 
ATOM   4753 N N     . LEU A 1 794 ? 6.258   60.278  99.475  1.00 89.35  ?  775 LEU A N     1 
ATOM   4754 C CA    . LEU A 1 794 ? 6.850   61.583  99.757  1.00 82.64  ?  775 LEU A CA    1 
ATOM   4755 C C     . LEU A 1 794 ? 5.944   62.724  99.331  1.00 86.76  ?  775 LEU A C     1 
ATOM   4756 O O     . LEU A 1 794 ? 5.987   63.796  99.937  1.00 90.83  ?  775 LEU A O     1 
ATOM   4757 C CB    . LEU A 1 794 ? 8.193   61.766  99.077  1.00 80.70  ?  775 LEU A CB    1 
ATOM   4758 C CG    . LEU A 1 794 ? 9.350   60.975  99.647  1.00 83.17  ?  775 LEU A CG    1 
ATOM   4759 C CD1   . LEU A 1 794 ? 10.685  61.425  99.047  1.00 84.89  ?  775 LEU A CD1   1 
ATOM   4760 C CD2   . LEU A 1 794 ? 9.334   61.142  101.107 1.00 87.30  ?  775 LEU A CD2   1 
ATOM   4761 N N     . MET A 1 795 ? 5.116   62.522  98.305  1.00 87.06  ?  776 MET A N     1 
ATOM   4762 C CA    . MET A 1 795 ? 4.240   63.598  97.852  1.00 91.19  ?  776 MET A CA    1 
ATOM   4763 C C     . MET A 1 795 ? 3.119   63.882  98.840  1.00 93.03  ?  776 MET A C     1 
ATOM   4764 O O     . MET A 1 795 ? 2.551   64.980  98.814  1.00 96.84  ?  776 MET A O     1 
ATOM   4765 C CB    . MET A 1 795 ? 3.648   63.277  96.471  1.00 94.39  ?  776 MET A CB    1 
ATOM   4766 C CG    . MET A 1 795 ? 4.703   63.121  95.345  1.00 104.81 ?  776 MET A CG    1 
ATOM   4767 S SD    . MET A 1 795 ? 5.675   64.577  94.816  1.00 95.71  ?  776 MET A SD    1 
ATOM   4768 C CE    . MET A 1 795 ? 4.338   65.595  94.161  1.00 95.85  ?  776 MET A CE    1 
ATOM   4769 N N     . ALA A 1 796 ? 2.793   62.940  99.722  1.00 88.67  ?  777 ALA A N     1 
ATOM   4770 C CA    . ALA A 1 796 ? 1.726   63.212  100.671 1.00 92.23  ?  777 ALA A CA    1 
ATOM   4771 C C     . ALA A 1 796 ? 2.219   63.996  101.890 1.00 95.23  ?  777 ALA A C     1 
ATOM   4772 O O     . ALA A 1 796 ? 1.459   64.809  102.461 1.00 86.69  ?  777 ALA A O     1 
ATOM   4773 C CB    . ALA A 1 796 ? 1.082   61.897  101.086 1.00 95.90  ?  777 ALA A CB    1 
ATOM   4774 N N     . GLN A 1 797 ? 3.498   63.797  102.267 1.00 93.99  ?  778 GLN A N     1 
ATOM   4775 C CA    . GLN A 1 797 ? 4.030   64.287  103.533 1.00 100.42 ?  778 GLN A CA    1 
ATOM   4776 C C     . GLN A 1 797 ? 3.944   65.809  103.531 1.00 98.35  ?  778 GLN A C     1 
ATOM   4777 O O     . GLN A 1 797 ? 4.653   66.462  102.747 1.00 91.05  ?  778 GLN A O     1 
ATOM   4778 C CB    . GLN A 1 797 ? 5.477   63.832  103.757 1.00 99.49  ?  778 GLN A CB    1 
ATOM   4779 C CG    . GLN A 1 797 ? 5.678   62.304  103.863 1.00 107.87 ?  778 GLN A CG    1 
ATOM   4780 C CD    . GLN A 1 797 ? 4.800   61.617  104.899 1.00 113.97 ?  778 GLN A CD    1 
ATOM   4781 O OE1   . GLN A 1 797 ? 4.562   62.158  105.986 1.00 110.96 ?  778 GLN A OE1   1 
ATOM   4782 N NE2   . GLN A 1 797 ? 4.322   60.397  104.566 1.00 106.43 ?  778 GLN A NE2   1 
ATOM   4783 N N     . PRO A 1 798 ? 3.088   66.398  104.378 1.00 97.82  ?  779 PRO A N     1 
ATOM   4784 C CA    . PRO A 1 798 ? 2.837   67.843  104.306 1.00 96.42  ?  779 PRO A CA    1 
ATOM   4785 C C     . PRO A 1 798 ? 4.048   68.629  104.790 1.00 96.65  ?  779 PRO A C     1 
ATOM   4786 O O     . PRO A 1 798 ? 5.012   68.063  105.324 1.00 93.63  ?  779 PRO A O     1 
ATOM   4787 C CB    . PRO A 1 798 ? 1.627   68.042  105.228 1.00 92.52  ?  779 PRO A CB    1 
ATOM   4788 C CG    . PRO A 1 798 ? 1.720   66.928  106.182 1.00 87.77  ?  779 PRO A CG    1 
ATOM   4789 C CD    . PRO A 1 798 ? 2.268   65.761  105.423 1.00 94.28  ?  779 PRO A CD    1 
ATOM   4790 N N     . ILE A 1 799 ? 3.964   69.948  104.637 1.00 93.56  ?  780 ILE A N     1 
ATOM   4791 C CA    . ILE A 1 799 ? 5.130   70.780  105.025 1.00 95.30  ?  780 ILE A CA    1 
ATOM   4792 C C     . ILE A 1 799 ? 4.823   71.632  106.245 1.00 96.60  ?  780 ILE A C     1 
ATOM   4793 O O     . ILE A 1 799 ? 3.797   72.302  106.270 1.00 95.15  ?  780 ILE A O     1 
ATOM   4794 C CB    . ILE A 1 799 ? 5.604   71.651  103.861 1.00 96.59  ?  780 ILE A CB    1 
ATOM   4795 C CG1   . ILE A 1 799 ? 5.933   70.803  102.641 1.00 95.32  ?  780 ILE A CG1   1 
ATOM   4796 C CG2   . ILE A 1 799 ? 6.815   72.444  104.290 1.00 98.69  ?  780 ILE A CG2   1 
ATOM   4797 C CD1   . ILE A 1 799 ? 7.371   70.911  102.221 1.00 92.34  ?  780 ILE A CD1   1 
ATOM   4798 N N     . THR A 1 800 ? 5.723   71.572  107.216 1.00 98.89  ?  781 THR A N     1 
ATOM   4799 C CA    . THR A 1 800 ? 5.620   72.407  108.421 1.00 99.87  ?  781 THR A CA    1 
ATOM   4800 C C     . THR A 1 800 ? 6.690   73.465  108.238 1.00 98.71  ?  781 THR A C     1 
ATOM   4801 O O     . THR A 1 800 ? 7.857   73.115  108.162 1.00 94.51  ?  781 THR A O     1 
ATOM   4802 C CB    . THR A 1 800 ? 5.912   71.600  109.681 1.00 99.53  ?  781 THR A CB    1 
ATOM   4803 O OG1   . THR A 1 800 ? 5.137   70.408  109.636 1.00 95.89  ?  781 THR A OG1   1 
ATOM   4804 C CG2   . THR A 1 800 ? 5.544   72.350  110.934 1.00 103.36 ?  781 THR A CG2   1 
ATOM   4805 N N     . PRO A 1 801 ? 6.319   74.750  108.221 1.00 97.88  ?  782 PRO A N     1 
ATOM   4806 C CA    . PRO A 1 801 ? 7.254   75.819  107.988 1.00 93.72  ?  782 PRO A CA    1 
ATOM   4807 C C     . PRO A 1 801 ? 8.188   76.062  109.162 1.00 99.82  ?  782 PRO A C     1 
ATOM   4808 O O     . PRO A 1 801 ? 7.904   75.662  110.223 1.00 112.10 ?  782 PRO A O     1 
ATOM   4809 C CB    . PRO A 1 801 ? 6.344   77.035  107.954 1.00 94.06  ?  782 PRO A CB    1 
ATOM   4810 C CG    . PRO A 1 801 ? 5.199   76.636  108.808 1.00 87.35  ?  782 PRO A CG    1 
ATOM   4811 C CD    . PRO A 1 801 ? 4.958   75.216  108.382 1.00 93.30  ?  782 PRO A CD    1 
ATOM   4812 N N     . GLY A 1 802 ? 9.224   76.851  108.931 1.00 101.73 ?  783 GLY A N     1 
ATOM   4813 C CA    . GLY A 1 802 ? 10.224  77.177  109.962 1.00 107.43 ?  783 GLY A CA    1 
ATOM   4814 C C     . GLY A 1 802 ? 9.712   78.112  111.044 1.00 111.29 ?  783 GLY A C     1 
ATOM   4815 O O     . GLY A 1 802 ? 8.625   78.669  110.938 1.00 110.97 ?  783 GLY A O     1 
ATOM   4816 N N     . PRO A 1 803 ? 10.471  78.339  112.120 1.00 109.99 ?  784 PRO A N     1 
ATOM   4817 C CA    . PRO A 1 803 ? 9.972   79.172  113.185 1.00 109.26 ?  784 PRO A CA    1 
ATOM   4818 C C     . PRO A 1 803 ? 9.929   80.590  112.626 1.00 117.53 ?  784 PRO A C     1 
ATOM   4819 O O     . PRO A 1 803 ? 10.873  80.958  111.996 1.00 118.62 ?  784 PRO A O     1 
ATOM   4820 C CB    . PRO A 1 803 ? 11.156  79.121  114.140 1.00 109.35 ?  784 PRO A CB    1 
ATOM   4821 C CG    . PRO A 1 803 ? 12.335  79.045  113.218 1.00 106.19 ?  784 PRO A CG    1 
ATOM   4822 C CD    . PRO A 1 803 ? 11.878  78.010  112.225 1.00 106.91 ?  784 PRO A CD    1 
ATOM   4823 N N     . SER A 1 804 ? 8.878   81.356  112.907 1.00 123.79 ?  785 SER A N     1 
ATOM   4824 C CA    . SER A 1 804 ? 8.886   82.770  112.463 1.00 116.51 ?  785 SER A CA    1 
ATOM   4825 C C     . SER A 1 804 ? 9.903   83.484  113.349 1.00 114.74 ?  785 SER A C     1 
ATOM   4826 O O     . SER A 1 804 ? 10.960  83.868  112.850 1.00 106.61 ?  785 SER A O     1 
ATOM   4827 C CB    . SER A 1 804 ? 7.537   83.376  112.610 1.00 113.37 ?  785 SER A CB    1 
ATOM   4828 O OG    . SER A 1 804 ? 7.117   83.290  113.954 1.00 118.11 ?  785 SER A OG    1 
ATOM   4829 N N     . ILE A 1 805 ? 9.568   83.652  114.624 1.00 112.90 ?  786 ILE A N     1 
ATOM   4830 C CA    . ILE A 1 805 ? 10.510  84.253  115.602 1.00 104.20 ?  786 ILE A CA    1 
ATOM   4831 C C     . ILE A 1 805 ? 11.576  83.201  115.839 1.00 112.89 ?  786 ILE A C     1 
ATOM   4832 O O     . ILE A 1 805 ? 11.192  82.093  116.095 1.00 122.04 ?  786 ILE A O     1 
ATOM   4833 C CB    . ILE A 1 805 ? 9.769   84.518  116.909 1.00 106.18 ?  786 ILE A CB    1 
ATOM   4834 C CG1   . ILE A 1 805 ? 8.451   85.245  116.664 1.00 103.46 ?  786 ILE A CG1   1 
ATOM   4835 C CG2   . ILE A 1 805 ? 10.667  85.278  117.853 1.00 117.19 ?  786 ILE A CG2   1 
ATOM   4836 C CD1   . ILE A 1 805 ? 7.243   84.464  117.092 1.00 107.29 ?  786 ILE A CD1   1 
ATOM   4837 N N     . PRO A 1 806 ? 12.876  83.510  115.917 1.00 114.19 ?  787 PRO A N     1 
ATOM   4838 C CA    . PRO A 1 806 ? 13.884  82.475  116.055 1.00 122.51 ?  787 PRO A CA    1 
ATOM   4839 C C     . PRO A 1 806 ? 13.787  81.924  117.473 1.00 123.27 ?  787 PRO A C     1 
ATOM   4840 O O     . PRO A 1 806 ? 13.512  82.680  118.353 1.00 115.24 ?  787 PRO A O     1 
ATOM   4841 C CB    . PRO A 1 806 ? 15.174  83.272  115.959 1.00 115.70 ?  787 PRO A CB    1 
ATOM   4842 C CG    . PRO A 1 806 ? 14.795  84.537  116.655 1.00 118.08 ?  787 PRO A CG    1 
ATOM   4843 C CD    . PRO A 1 806 ? 13.423  84.837  116.095 1.00 113.56 ?  787 PRO A CD    1 
ATOM   4844 N N     . GLY A 1 807 ? 13.981  80.616  117.634 1.00 115.24 ?  788 GLY A N     1 
ATOM   4845 C CA    . GLY A 1 807 ? 13.913  79.980  118.957 1.00 110.97 ?  788 GLY A CA    1 
ATOM   4846 C C     . GLY A 1 807 ? 12.497  79.641  119.364 1.00 112.53 ?  788 GLY A C     1 
ATOM   4847 O O     . GLY A 1 807 ? 12.316  79.130  120.455 1.00 119.05 ?  788 GLY A O     1 
ATOM   4848 N N     . ALA A 1 808 ? 11.527  79.865  118.491 1.00 108.32 ?  789 ALA A N     1 
ATOM   4849 C CA    . ALA A 1 808 ? 10.124  79.551  118.804 1.00 110.40 ?  789 ALA A CA    1 
ATOM   4850 C C     . ALA A 1 808 ? 9.892   78.057  118.658 1.00 112.29 ?  789 ALA A C     1 
ATOM   4851 O O     . ALA A 1 808 ? 10.674  77.376  118.019 1.00 108.99 ?  789 ALA A O     1 
ATOM   4852 C CB    . ALA A 1 808 ? 9.207   80.308  117.902 1.00 113.07 ?  789 ALA A CB    1 
ATOM   4853 N N     . PRO A 1 809 ? 8.771   77.550  119.167 1.00 111.47 ?  790 PRO A N     1 
ATOM   4854 C CA    . PRO A 1 809 ? 8.499   76.143  119.131 1.00 109.28 ?  790 PRO A CA    1 
ATOM   4855 C C     . PRO A 1 809 ? 8.122   75.756  117.705 1.00 117.38 ?  790 PRO A C     1 
ATOM   4856 O O     . PRO A 1 809 ? 7.458   76.524  117.065 1.00 111.17 ?  790 PRO A O     1 
ATOM   4857 C CB    . PRO A 1 809 ? 7.197   76.097  119.913 1.00 104.86 ?  790 PRO A CB    1 
ATOM   4858 C CG    . PRO A 1 809 ? 6.516   77.337  119.461 1.00 108.18 ?  790 PRO A CG    1 
ATOM   4859 C CD    . PRO A 1 809 ? 7.636   78.339  119.585 1.00 114.41 ?  790 PRO A CD    1 
ATOM   4860 N N     . GLN A 1 810 ? 8.535   74.555  117.296 1.00 121.82 ?  791 GLN A N     1 
ATOM   4861 C CA    . GLN A 1 810 ? 8.194   73.983  115.973 1.00 123.04 ?  791 GLN A CA    1 
ATOM   4862 C C     . GLN A 1 810 ? 6.688   74.111  115.809 1.00 122.21 ?  791 GLN A C     1 
ATOM   4863 O O     . GLN A 1 810 ? 5.946   73.629  116.655 1.00 114.40 ?  791 GLN A O     1 
ATOM   4864 C CB    . GLN A 1 810 ? 8.560   72.504  115.926 1.00 122.20 ?  791 GLN A CB    1 
ATOM   4865 C CG    . GLN A 1 810 ? 9.061   72.050  114.570 1.00 129.63 ?  791 GLN A CG    1 
ATOM   4866 C CD    . GLN A 1 810 ? 10.493  72.483  114.403 1.00 137.52 ?  791 GLN A CD    1 
ATOM   4867 O OE1   . GLN A 1 810 ? 11.120  72.965  115.341 1.00 142.69 ?  791 GLN A OE1   1 
ATOM   4868 N NE2   . GLN A 1 810 ? 11.015  72.322  113.199 1.00 134.86 ?  791 GLN A NE2   1 
ATOM   4869 N N     . PRO A 1 811 ? 6.205   74.654  114.692 1.00 122.05 ?  792 PRO A N     1 
ATOM   4870 C CA    . PRO A 1 811 ? 4.797   74.901  114.519 1.00 122.08 ?  792 PRO A CA    1 
ATOM   4871 C C     . PRO A 1 811 ? 3.984   73.707  114.034 1.00 114.77 ?  792 PRO A C     1 
ATOM   4872 O O     . PRO A 1 811 ? 4.277   72.589  114.340 1.00 100.03 ?  792 PRO A O     1 
ATOM   4873 C CB    . PRO A 1 811 ? 4.753   75.895  113.358 1.00 107.29 ?  792 PRO A CB    1 
ATOM   4874 C CG    . PRO A 1 811 ? 6.191   76.245  113.101 1.00 109.20 ?  792 PRO A CG    1 
ATOM   4875 C CD    . PRO A 1 811 ? 6.986   75.047  113.551 1.00 111.93 ?  792 PRO A CD    1 
ATOM   4876 N N     . ILE A 1 812 ? 2.860   74.062  113.442 1.00 111.21 ?  793 ILE A N     1 
ATOM   4877 C CA    . ILE A 1 812 ? 1.928   73.113  112.795 1.00 112.55 ?  793 ILE A CA    1 
ATOM   4878 C C     . ILE A 1 812 ? 2.421   72.848  111.377 1.00 110.09 ?  793 ILE A C     1 
ATOM   4879 O O     . ILE A 1 812 ? 3.283   73.566  110.901 1.00 111.71 ?  793 ILE A O     1 
ATOM   4880 C CB    . ILE A 1 812 ? 0.549   73.769  112.748 1.00 110.48 ?  793 ILE A CB    1 
ATOM   4881 C CG1   . ILE A 1 812 ? 0.354   74.699  113.942 1.00 110.94 ?  793 ILE A CG1   1 
ATOM   4882 C CG2   . ILE A 1 812 ? -0.532  72.720  112.658 1.00 110.24 ?  793 ILE A CG2   1 
ATOM   4883 C CD1   . ILE A 1 812 ? -0.885  74.415  114.736 1.00 111.80 ?  793 ILE A CD1   1 
ATOM   4884 N N     . PRO A 1 813 ? 1.967   71.778  110.713 1.00 105.83 ?  794 PRO A N     1 
ATOM   4885 C CA    . PRO A 1 813 ? 2.289   71.544  109.326 1.00 101.03 ?  794 PRO A CA    1 
ATOM   4886 C C     . PRO A 1 813 ? 1.194   72.376  108.659 1.00 104.16 ?  794 PRO A C     1 
ATOM   4887 O O     . PRO A 1 813 ? 0.056   72.152  108.949 1.00 100.53 ?  794 PRO A O     1 
ATOM   4888 C CB    . PRO A 1 813 ? 1.966   70.064  109.177 1.00 101.75 ?  794 PRO A CB    1 
ATOM   4889 C CG    . PRO A 1 813 ? 1.911   69.572  110.585 1.00 101.54 ?  794 PRO A CG    1 
ATOM   4890 C CD    . PRO A 1 813 ? 1.201   70.702  111.284 1.00 111.61 ?  794 PRO A CD    1 
ATOM   4891 N N     . ARG A 1 814 ? 1.566   73.253  107.732 1.00 103.17 ?  795 ARG A N     1 
ATOM   4892 C CA    . ARG A 1 814 ? 0.584   74.216  107.181 1.00 100.45 ?  795 ARG A CA    1 
ATOM   4893 C C     . ARG A 1 814 ? 0.176   73.922  105.740 1.00 98.30  ?  795 ARG A C     1 
ATOM   4894 O O     . ARG A 1 814 ? -0.907  74.355  105.342 1.00 91.65  ?  795 ARG A O     1 
ATOM   4895 C CB    . ARG A 1 814 ? 1.284   75.572  107.155 1.00 95.92  ?  795 ARG A CB    1 
ATOM   4896 C CG    . ARG A 1 814 ? 1.582   76.154  108.526 1.00 86.54  ?  795 ARG A CG    1 
ATOM   4897 C CD    . ARG A 1 814 ? 0.255   76.636  109.050 1.00 93.15  ?  795 ARG A CD    1 
ATOM   4898 N NE    . ARG A 1 814 ? 0.321   77.435  110.249 1.00 98.10  ?  795 ARG A NE    1 
ATOM   4899 C CZ    . ARG A 1 814 ? -0.753  77.850  110.880 1.00 99.30  ?  795 ARG A CZ    1 
ATOM   4900 N NH1   . ARG A 1 814 ? -1.945  77.543  110.413 1.00 95.99  ?  795 ARG A NH1   1 
ATOM   4901 N NH2   . ARG A 1 814 ? -0.638  78.583  111.963 1.00 101.91 ?  795 ARG A NH2   1 
ATOM   4902 N N     . LEU A 1 815 ? 1.006   73.186  105.016 1.00 102.62 ?  796 LEU A N     1 
ATOM   4903 C CA    . LEU A 1 815 ? 0.828   72.963  103.583 1.00 100.37 ?  796 LEU A CA    1 
ATOM   4904 C C     . LEU A 1 815 ? 0.575   71.482  103.336 1.00 96.19  ?  796 LEU A C     1 
ATOM   4905 O O     . LEU A 1 815 ? 1.405   70.642  103.710 1.00 91.63  ?  796 LEU A O     1 
ATOM   4906 C CB    . LEU A 1 815 ? 2.071   73.423  102.816 1.00 101.38 ?  796 LEU A CB    1 
ATOM   4907 C CG    . LEU A 1 815 ? 1.963   73.450  101.295 1.00 95.47  ?  796 LEU A CG    1 
ATOM   4908 C CD1   . LEU A 1 815 ? 0.749   74.319  100.902 1.00 87.26  ?  796 LEU A CD1   1 
ATOM   4909 C CD2   . LEU A 1 815 ? 3.275   73.946  100.691 1.00 87.58  ?  796 LEU A CD2   1 
ATOM   4910 N N     . PHE A 1 816 ? -0.562  71.170  102.693 1.00 96.04  ?  797 PHE A N     1 
ATOM   4911 C CA    . PHE A 1 816 ? -1.008  69.800  102.450 1.00 96.54  ?  797 PHE A CA    1 
ATOM   4912 C C     . PHE A 1 816 ? -1.118  69.508  100.950 1.00 98.98  ?  797 PHE A C     1 
ATOM   4913 O O     . PHE A 1 816 ? -1.448  70.388  100.141 1.00 95.19  ?  797 PHE A O     1 
ATOM   4914 C CB    . PHE A 1 816 ? -2.371  69.521  103.131 1.00 92.32  ?  797 PHE A CB    1 
ATOM   4915 C CG    . PHE A 1 816 ? -2.329  69.581  104.638 1.00 94.09  ?  797 PHE A CG    1 
ATOM   4916 C CD1   . PHE A 1 816 ? -2.580  70.761  105.314 1.00 100.52 ?  797 PHE A CD1   1 
ATOM   4917 C CD2   . PHE A 1 816 ? -2.007  68.467  105.378 1.00 94.39  ?  797 PHE A CD2   1 
ATOM   4918 C CE1   . PHE A 1 816 ? -2.526  70.810  106.698 1.00 94.23  ?  797 PHE A CE1   1 
ATOM   4919 C CE2   . PHE A 1 816 ? -1.954  68.519  106.748 1.00 89.64  ?  797 PHE A CE2   1 
ATOM   4920 C CZ    . PHE A 1 816 ? -2.213  69.694  107.403 1.00 91.48  ?  797 PHE A CZ    1 
ATOM   4921 N N     . PHE A 1 817 ? -0.867  68.242  100.589 1.00 102.00 ?  798 PHE A N     1 
ATOM   4922 C CA    . PHE A 1 817 ? -0.869  67.778  99.202  1.00 91.66  ?  798 PHE A CA    1 
ATOM   4923 C C     . PHE A 1 817 ? -1.807  66.604  99.010  1.00 91.82  ?  798 PHE A C     1 
ATOM   4924 O O     . PHE A 1 817 ? -1.737  65.626  99.759  1.00 97.61  ?  798 PHE A O     1 
ATOM   4925 C CB    . PHE A 1 817 ? 0.495   67.302  98.762  1.00 84.15  ?  798 PHE A CB    1 
ATOM   4926 C CG    . PHE A 1 817 ? 1.521   68.331  98.830  1.00 84.51  ?  798 PHE A CG    1 
ATOM   4927 C CD1   . PHE A 1 817 ? 2.563   68.217  99.712  1.00 85.10  ?  798 PHE A CD1   1 
ATOM   4928 C CD2   . PHE A 1 817 ? 1.423   69.447  98.033  1.00 90.31  ?  798 PHE A CD2   1 
ATOM   4929 C CE1   . PHE A 1 817 ? 3.525   69.176  99.767  1.00 90.79  ?  798 PHE A CE1   1 
ATOM   4930 C CE2   . PHE A 1 817 ? 2.378   70.408  98.076  1.00 96.79  ?  798 PHE A CE2   1 
ATOM   4931 C CZ    . PHE A 1 817 ? 3.440   70.276  98.950  1.00 99.03  ?  798 PHE A CZ    1 
ATOM   4932 N N     . ALA A 1 818 ? -2.613  66.666  97.956  1.00 93.24  ?  799 ALA A N     1 
ATOM   4933 C CA    . ALA A 1 818 ? -3.479  65.557  97.581  1.00 97.85  ?  799 ALA A CA    1 
ATOM   4934 C C     . ALA A 1 818 ? -3.610  65.549  96.064  1.00 97.00  ?  799 ALA A C     1 
ATOM   4935 O O     . ALA A 1 818 ? -3.297  66.535  95.391  1.00 98.99  ?  799 ALA A O     1 
ATOM   4936 C CB    . ALA A 1 818 ? -4.854  65.652  98.269  1.00 94.59  ?  799 ALA A CB    1 
ATOM   4937 N N     . GLY A 1 819 ? -4.062  64.420  95.531  1.00 93.29  ?  800 GLY A N     1 
ATOM   4938 C CA    . GLY A 1 819 ? -4.084  64.254  94.093  1.00 99.81  ?  800 GLY A CA    1 
ATOM   4939 C C     . GLY A 1 819 ? -3.645  62.860  93.693  1.00 103.84 ?  800 GLY A C     1 
ATOM   4940 O O     . GLY A 1 819 ? -3.090  62.117  94.518  1.00 101.39 ?  800 GLY A O     1 
ATOM   4941 N N     . GLU A 1 820 ? -3.897  62.495  92.430  1.00 99.76  ?  801 GLU A N     1 
ATOM   4942 C CA    . GLU A 1 820 ? -3.636  61.131  91.990  1.00 89.75  ?  801 GLU A CA    1 
ATOM   4943 C C     . GLU A 1 820 ? -2.161  60.776  92.121  1.00 87.52  ?  801 GLU A C     1 
ATOM   4944 O O     . GLU A 1 820 ? -1.822  59.616  92.347  1.00 90.19  ?  801 GLU A O     1 
ATOM   4945 C CB    . GLU A 1 820 ? -4.158  60.966  90.553  1.00 98.44  ?  801 GLU A CB    1 
ATOM   4946 C CG    . GLU A 1 820 ? -3.499  61.865  89.495  1.00 96.46  ?  801 GLU A CG    1 
ATOM   4947 C CD    . GLU A 1 820 ? -2.280  61.241  88.858  1.00 89.06  ?  801 GLU A CD    1 
ATOM   4948 O OE1   . GLU A 1 820 ? -2.173  60.000  88.866  1.00 85.61  ?  801 GLU A OE1   1 
ATOM   4949 O OE2   . GLU A 1 820 ? -1.395  61.999  88.409  1.00 89.25  ?  801 GLU A OE2   1 
ATOM   4950 N N     . HIS A 1 821 ? -1.278  61.762  92.042  1.00 91.17  ?  802 HIS A N     1 
ATOM   4951 C CA    . HIS A 1 821 ? 0.165   61.565  92.121  1.00 92.49  ?  802 HIS A CA    1 
ATOM   4952 C C     . HIS A 1 821 ? 0.689   61.311  93.528  1.00 98.43  ?  802 HIS A C     1 
ATOM   4953 O O     . HIS A 1 821 ? 1.890   61.043  93.665  1.00 99.28  ?  802 HIS A O     1 
ATOM   4954 C CB    . HIS A 1 821 ? 0.881   62.789  91.536  1.00 99.70  ?  802 HIS A CB    1 
ATOM   4955 C CG    . HIS A 1 821 ? 0.453   64.093  92.148  1.00 98.89  ?  802 HIS A CG    1 
ATOM   4956 N ND1   . HIS A 1 821 ? -0.820  64.611  91.982  1.00 96.16  ?  802 HIS A ND1   1 
ATOM   4957 C CD2   . HIS A 1 821 ? 1.119   64.970  92.941  1.00 92.81  ?  802 HIS A CD2   1 
ATOM   4958 C CE1   . HIS A 1 821 ? -0.912  65.756  92.636  1.00 97.91  ?  802 HIS A CE1   1 
ATOM   4959 N NE2   . HIS A 1 821 ? 0.250   65.998  93.226  1.00 93.13  ?  802 HIS A NE2   1 
ATOM   4960 N N     . THR A 1 822 ? -0.170  61.381  94.560  1.00 105.14 ?  803 THR A N     1 
ATOM   4961 C CA    . THR A 1 822 ? 0.227   61.362  95.975  1.00 99.56  ?  803 THR A CA    1 
ATOM   4962 C C     . THR A 1 822 ? -0.114  60.060  96.706  1.00 100.12 ?  803 THR A C     1 
ATOM   4963 O O     . THR A 1 822 ? 0.111   59.975  97.924  1.00 105.01 ?  803 THR A O     1 
ATOM   4964 C CB    . THR A 1 822 ? -0.434  62.534  96.738  1.00 94.49  ?  803 THR A CB    1 
ATOM   4965 O OG1   . THR A 1 822 ? -1.867  62.487  96.583  1.00 88.60  ?  803 THR A OG1   1 
ATOM   4966 C CG2   . THR A 1 822 ? 0.087   63.882  96.243  1.00 93.89  ?  803 THR A CG2   1 
ATOM   4967 N N     . ILE A 1 823 ? -0.639  59.043  96.018  1.00 95.72  ?  804 ILE A N     1 
ATOM   4968 C CA    . ILE A 1 823 ? -1.321  57.923  96.671  1.00 88.81  ?  804 ILE A CA    1 
ATOM   4969 C C     . ILE A 1 823 ? -0.732  56.632  96.101  1.00 92.05  ?  804 ILE A C     1 
ATOM   4970 O O     . ILE A 1 823 ? -1.267  56.047  95.155  1.00 95.93  ?  804 ILE A O     1 
ATOM   4971 C CB    . ILE A 1 823 ? -2.848  57.999  96.507  1.00 80.62  ?  804 ILE A CB    1 
ATOM   4972 C CG1   . ILE A 1 823 ? -3.545  56.781  97.051  1.00 84.64  ?  804 ILE A CG1   1 
ATOM   4973 C CG2   . ILE A 1 823 ? -3.275  58.174  95.063  1.00 88.48  ?  804 ILE A CG2   1 
ATOM   4974 C CD1   . ILE A 1 823 ? -5.020  56.951  97.066  1.00 81.41  ?  804 ILE A CD1   1 
ATOM   4975 N N     . ARG A 1 824 ? 0.383   56.170  96.696  1.00 95.60  ?  805 ARG A N     1 
ATOM   4976 C CA    . ARG A 1 824 ? 1.163   55.013  96.231  1.00 94.71  ?  805 ARG A CA    1 
ATOM   4977 C C     . ARG A 1 824 ? 0.323   53.826  95.758  1.00 99.39  ?  805 ARG A C     1 
ATOM   4978 O O     . ARG A 1 824 ? 0.545   53.288  94.663  1.00 100.25 ?  805 ARG A O     1 
ATOM   4979 C CB    . ARG A 1 824 ? 2.103   54.557  97.359  1.00 98.91  ?  805 ARG A CB    1 
ATOM   4980 C CG    . ARG A 1 824 ? 3.013   53.357  97.061  1.00 98.77  ?  805 ARG A CG    1 
ATOM   4981 C CD    . ARG A 1 824 ? 3.472   52.665  98.345  1.00 97.83  ?  805 ARG A CD    1 
ATOM   4982 N NE    . ARG A 1 824 ? 4.755   51.966  98.189  1.00 102.83 ?  805 ARG A NE    1 
ATOM   4983 C CZ    . ARG A 1 824 ? 5.908   52.405  98.711  1.00 105.06 ?  805 ARG A CZ    1 
ATOM   4984 N NH1   . ARG A 1 824 ? 5.916   53.523  99.421  1.00 103.69 ?  805 ARG A NH1   1 
ATOM   4985 N NH2   . ARG A 1 824 ? 7.051   51.733  98.546  1.00 103.49 ?  805 ARG A NH2   1 
ATOM   4986 N N     . ASN A 1 825 ? -0.651  53.408  96.570  1.00 98.26  ?  806 ASN A N     1 
ATOM   4987 C CA    . ASN A 1 825 ? -1.416  52.198  96.294  1.00 99.21  ?  806 ASN A CA    1 
ATOM   4988 C C     . ASN A 1 825 ? -2.474  52.335  95.199  1.00 97.54  ?  806 ASN A C     1 
ATOM   4989 O O     . ASN A 1 825 ? -3.050  51.318  94.815  1.00 103.19 ?  806 ASN A O     1 
ATOM   4990 C CB    . ASN A 1 825 ? -2.076  51.695  97.577  1.00 98.18  ?  806 ASN A CB    1 
ATOM   4991 C CG    . ASN A 1 825 ? -1.102  51.001  98.485  1.00 103.94 ?  806 ASN A CG    1 
ATOM   4992 O OD1   . ASN A 1 825 ? 0.076   50.821  98.141  1.00 103.74 ?  806 ASN A OD1   1 
ATOM   4993 N ND2   . ASN A 1 825 ? -1.582  50.595  99.656  1.00 109.08 ?  806 ASN A ND2   1 
ATOM   4994 N N     . TYR A 1 826 ? -2.771  53.521  94.692  1.00 95.17  ?  807 TYR A N     1 
ATOM   4995 C CA    . TYR A 1 826 ? -3.818  53.601  93.669  1.00 97.55  ?  807 TYR A CA    1 
ATOM   4996 C C     . TYR A 1 826 ? -3.531  54.744  92.683  1.00 98.87  ?  807 TYR A C     1 
ATOM   4997 O O     . TYR A 1 826 ? -4.447  55.518  92.357  1.00 96.80  ?  807 TYR A O     1 
ATOM   4998 C CB    . TYR A 1 826 ? -5.207  53.785  94.333  1.00 96.19  ?  807 TYR A CB    1 
ATOM   4999 C CG    . TYR A 1 826 ? -5.661  52.724  95.372  1.00 93.88  ?  807 TYR A CG    1 
ATOM   5000 C CD1   . TYR A 1 826 ? -6.558  51.699  95.041  1.00 101.06 ?  807 TYR A CD1   1 
ATOM   5001 C CD2   . TYR A 1 826 ? -5.161  52.731  96.668  1.00 100.66 ?  807 TYR A CD2   1 
ATOM   5002 C CE1   . TYR A 1 826 ? -6.968  50.717  96.003  1.00 102.15 ?  807 TYR A CE1   1 
ATOM   5003 C CE2   . TYR A 1 826 ? -5.541  51.755  97.625  1.00 111.98 ?  807 TYR A CE2   1 
ATOM   5004 C CZ    . TYR A 1 826 ? -6.445  50.759  97.292  1.00 108.97 ?  807 TYR A CZ    1 
ATOM   5005 O OH    . TYR A 1 826 ? -6.793  49.846  98.278  1.00 104.13 ?  807 TYR A OH    1 
ATOM   5006 N N     . PRO A 1 827 ? -2.300  54.893  92.175  1.00 98.53  ?  808 PRO A N     1 
ATOM   5007 C CA    . PRO A 1 827 ? -1.969  56.103  91.412  1.00 92.79  ?  808 PRO A CA    1 
ATOM   5008 C C     . PRO A 1 827 ? -2.656  56.096  90.062  1.00 94.38  ?  808 PRO A C     1 
ATOM   5009 O O     . PRO A 1 827 ? -3.271  55.111  89.646  1.00 100.42 ?  808 PRO A O     1 
ATOM   5010 C CB    . PRO A 1 827 ? -0.452  56.025  91.255  1.00 92.14  ?  808 PRO A CB    1 
ATOM   5011 C CG    . PRO A 1 827 ? -0.180  54.572  91.190  1.00 102.29 ?  808 PRO A CG    1 
ATOM   5012 C CD    . PRO A 1 827 ? -1.200  53.910  92.111  1.00 100.52 ?  808 PRO A CD    1 
ATOM   5013 N N     . ALA A 1 828 ? -2.554  57.238  89.389  1.00 90.58  ?  809 ALA A N     1 
ATOM   5014 C CA    . ALA A 1 828 ? -2.951  57.352  87.996  1.00 95.34  ?  809 ALA A CA    1 
ATOM   5015 C C     . ALA A 1 828 ? -4.459  57.215  87.789  1.00 95.66  ?  809 ALA A C     1 
ATOM   5016 O O     . ALA A 1 828 ? -4.933  57.228  86.648  1.00 103.97 ?  809 ALA A O     1 
ATOM   5017 C CB    . ALA A 1 828 ? -2.199  56.311  87.147  1.00 104.32 ?  809 ALA A CB    1 
ATOM   5018 N N     . THR A 1 829 ? -5.236  57.072  88.844  1.00 89.43  ?  810 THR A N     1 
ATOM   5019 C CA    . THR A 1 829 ? -6.649  56.800  88.628  1.00 93.91  ?  810 THR A CA    1 
ATOM   5020 C C     . THR A 1 829 ? -7.485  57.917  89.232  1.00 92.72  ?  810 THR A C     1 
ATOM   5021 O O     . THR A 1 829 ? -6.965  58.915  89.720  1.00 94.44  ?  810 THR A O     1 
ATOM   5022 C CB    . THR A 1 829 ? -7.042  55.423  89.184  1.00 95.39  ?  810 THR A CB    1 
ATOM   5023 O OG1   . THR A 1 829 ? -6.745  55.366  90.579  1.00 100.93 ?  810 THR A OG1   1 
ATOM   5024 C CG2   . THR A 1 829 ? -6.296  54.292  88.470  1.00 103.11 ?  810 THR A CG2   1 
ATOM   5025 N N     . VAL A 1 830 ? -8.800  57.755  89.144  1.00 90.76  ?  811 VAL A N     1 
ATOM   5026 C CA    . VAL A 1 830 ? -9.747  58.658  89.796  1.00 85.63  ?  811 VAL A CA    1 
ATOM   5027 C C     . VAL A 1 830 ? -10.088 58.217  91.206  1.00 90.61  ?  811 VAL A C     1 
ATOM   5028 O O     . VAL A 1 830 ? -10.011 59.014  92.147  1.00 94.16  ?  811 VAL A O     1 
ATOM   5029 C CB    . VAL A 1 830 ? -11.012 58.790  88.951  1.00 86.82  ?  811 VAL A CB    1 
ATOM   5030 C CG1   . VAL A 1 830 ? -12.064 59.471  89.747  1.00 82.12  ?  811 VAL A CG1   1 
ATOM   5031 C CG2   . VAL A 1 830 ? -10.672 59.657  87.795  1.00 96.59  ?  811 VAL A CG2   1 
ATOM   5032 N N     . HIS A 1 831 ? -10.516 56.963  91.373  1.00 93.74  ?  812 HIS A N     1 
ATOM   5033 C CA    . HIS A 1 831 ? -10.671 56.422  92.719  1.00 92.00  ?  812 HIS A CA    1 
ATOM   5034 C C     . HIS A 1 831 ? -9.442  56.765  93.567  1.00 91.56  ?  812 HIS A C     1 
ATOM   5035 O O     . HIS A 1 831 ? -9.578  57.267  94.687  1.00 93.57  ?  812 HIS A O     1 
ATOM   5036 C CB    . HIS A 1 831 ? -10.953 54.905  92.653  1.00 93.58  ?  812 HIS A CB    1 
ATOM   5037 C CG    . HIS A 1 831 ? -9.944  54.107  91.868  1.00 97.01  ?  812 HIS A CG    1 
ATOM   5038 N ND1   . HIS A 1 831 ? -10.175 53.680  90.576  1.00 93.76  ?  812 HIS A ND1   1 
ATOM   5039 C CD2   . HIS A 1 831 ? -8.738  53.591  92.223  1.00 96.42  ?  812 HIS A CD2   1 
ATOM   5040 C CE1   . HIS A 1 831 ? -9.126  53.000  90.147  1.00 97.68  ?  812 HIS A CE1   1 
ATOM   5041 N NE2   . HIS A 1 831 ? -8.246  52.917  91.132  1.00 95.81  ?  812 HIS A NE2   1 
ATOM   5042 N N     . GLY A 1 832 ? -8.239  56.629  92.988  1.00 94.13  ?  813 GLY A N     1 
ATOM   5043 C CA    . GLY A 1 832 ? -7.012  56.943  93.715  1.00 91.82  ?  813 GLY A CA    1 
ATOM   5044 C C     . GLY A 1 832 ? -6.886  58.409  94.095  1.00 90.04  ?  813 GLY A C     1 
ATOM   5045 O O     . GLY A 1 832 ? -6.502  58.735  95.217  1.00 92.62  ?  813 GLY A O     1 
ATOM   5046 N N     . ALA A 1 833 ? -7.185  59.316  93.163  1.00 89.08  ?  814 ALA A N     1 
ATOM   5047 C CA    . ALA A 1 833 ? -7.132  60.734  93.497  1.00 88.46  ?  814 ALA A CA    1 
ATOM   5048 C C     . ALA A 1 833 ? -8.142  61.066  94.584  1.00 89.26  ?  814 ALA A C     1 
ATOM   5049 O O     . ALA A 1 833 ? -7.789  61.652  95.617  1.00 90.31  ?  814 ALA A O     1 
ATOM   5050 C CB    . ALA A 1 833 ? -7.377  61.588  92.254  1.00 93.75  ?  814 ALA A CB    1 
ATOM   5051 N N     . LEU A 1 834 ? -9.408  60.693  94.366  1.00 86.42  ?  815 LEU A N     1 
ATOM   5052 C CA    . LEU A 1 834 ? -10.425 60.768  95.411  1.00 88.84  ?  815 LEU A CA    1 
ATOM   5053 C C     . LEU A 1 834 ? -9.945  60.301  96.790  1.00 87.10  ?  815 LEU A C     1 
ATOM   5054 O O     . LEU A 1 834 ? -10.133 61.001  97.790  1.00 82.58  ?  815 LEU A O     1 
ATOM   5055 C CB    . LEU A 1 834 ? -11.652 59.965  94.974  1.00 85.54  ?  815 LEU A CB    1 
ATOM   5056 C CG    . LEU A 1 834 ? -12.820 59.959  95.965  1.00 79.31  ?  815 LEU A CG    1 
ATOM   5057 C CD1   . LEU A 1 834 ? -14.130 59.791  95.261  1.00 75.72  ?  815 LEU A CD1   1 
ATOM   5058 C CD2   . LEU A 1 834 ? -12.656 58.763  96.926  1.00 78.40  ?  815 LEU A CD2   1 
ATOM   5059 N N     . LEU A 1 835 ? -9.389  59.088  96.879  1.00 90.62  ?  816 LEU A N     1 
ATOM   5060 C CA    . LEU A 1 835 ? -8.937  58.607  98.180  1.00 86.84  ?  816 LEU A CA    1 
ATOM   5061 C C     . LEU A 1 835 ? -7.940  59.582  98.787  1.00 90.83  ?  816 LEU A C     1 
ATOM   5062 O O     . LEU A 1 835 ? -8.031  59.903  99.980  1.00 96.00  ?  816 LEU A O     1 
ATOM   5063 C CB    . LEU A 1 835 ? -8.307  57.212  98.086  1.00 81.07  ?  816 LEU A CB    1 
ATOM   5064 C CG    . LEU A 1 835 ? -9.160  56.030  97.605  1.00 86.21  ?  816 LEU A CG    1 
ATOM   5065 C CD1   . LEU A 1 835 ? -8.399  54.699  97.640  1.00 87.73  ?  816 LEU A CD1   1 
ATOM   5066 C CD2   . LEU A 1 835 ? -10.482 55.918  98.323  1.00 89.32  ?  816 LEU A CD2   1 
ATOM   5067 N N     . SER A 1 836 ? -7.007  60.098  97.968  1.00 86.25  ?  817 SER A N     1 
ATOM   5068 C CA    . SER A 1 836 ? -5.957  60.962  98.501  1.00 87.64  ?  817 SER A CA    1 
ATOM   5069 C C     . SER A 1 836 ? -6.549  62.217  99.135  1.00 91.98  ?  817 SER A C     1 
ATOM   5070 O O     . SER A 1 836 ? -6.062  62.674  100.180 1.00 92.37  ?  817 SER A O     1 
ATOM   5071 C CB    . SER A 1 836 ? -4.940  61.324  97.409  1.00 88.86  ?  817 SER A CB    1 
ATOM   5072 O OG    . SER A 1 836 ? -5.425  62.331  96.538  1.00 91.81  ?  817 SER A OG    1 
ATOM   5073 N N     . GLY A 1 837 ? -7.623  62.763  98.547  1.00 94.08  ?  818 GLY A N     1 
ATOM   5074 C CA    . GLY A 1 837 ? -8.287  63.934  99.113  1.00 92.77  ?  818 GLY A CA    1 
ATOM   5075 C C     . GLY A 1 837 ? -9.148  63.649  100.327 1.00 92.11  ?  818 GLY A C     1 
ATOM   5076 O O     . GLY A 1 837 ? -9.435  64.578  101.094 1.00 91.80  ?  818 GLY A O     1 
ATOM   5077 N N     . LEU A 1 838 ? -9.603  62.393  100.487 1.00 88.67  ?  819 LEU A N     1 
ATOM   5078 C CA    . LEU A 1 838 ? -10.116 61.948  101.773 1.00 80.24  ?  819 LEU A CA    1 
ATOM   5079 C C     . LEU A 1 838 ? -8.988  61.802  102.775 1.00 84.39  ?  819 LEU A C     1 
ATOM   5080 O O     . LEU A 1 838 ? -9.142  62.191  103.939 1.00 89.81  ?  819 LEU A O     1 
ATOM   5081 C CB    . LEU A 1 838 ? -10.882 60.636  101.630 1.00 77.01  ?  819 LEU A CB    1 
ATOM   5082 C CG    . LEU A 1 838 ? -12.136 60.645  100.766 1.00 76.95  ?  819 LEU A CG    1 
ATOM   5083 C CD1   . LEU A 1 838 ? -12.910 59.351  100.949 1.00 81.70  ?  819 LEU A CD1   1 
ATOM   5084 C CD2   . LEU A 1 838 ? -13.016 61.824  101.157 1.00 80.41  ?  819 LEU A CD2   1 
ATOM   5085 N N     . ARG A 1 839 ? -7.846  61.259  102.333 1.00 83.44  ?  820 ARG A N     1 
ATOM   5086 C CA    . ARG A 1 839 ? -6.650  61.186  103.168 1.00 80.65  ?  820 ARG A CA    1 
ATOM   5087 C C     . ARG A 1 839 ? -6.315  62.539  103.789 1.00 90.48  ?  820 ARG A C     1 
ATOM   5088 O O     . ARG A 1 839 ? -6.124  62.652  105.004 1.00 101.09 ?  820 ARG A O     1 
ATOM   5089 C CB    . ARG A 1 839 ? -5.456  60.685  102.356 1.00 80.32  ?  820 ARG A CB    1 
ATOM   5090 C CG    . ARG A 1 839 ? -4.238  60.482  103.205 1.00 77.33  ?  820 ARG A CG    1 
ATOM   5091 C CD    . ARG A 1 839 ? -2.978  60.089  102.457 1.00 82.98  ?  820 ARG A CD    1 
ATOM   5092 N NE    . ARG A 1 839 ? -2.392  61.187  101.686 1.00 95.19  ?  820 ARG A NE    1 
ATOM   5093 C CZ    . ARG A 1 839 ? -2.386  61.277  100.351 1.00 96.76  ?  820 ARG A CZ    1 
ATOM   5094 N NH1   . ARG A 1 839 ? -2.930  60.318  99.605  1.00 96.22  ?  820 ARG A NH1   1 
ATOM   5095 N NH2   . ARG A 1 839 ? -1.812  62.322  99.752  1.00 93.51  ?  820 ARG A NH2   1 
ATOM   5096 N N     . GLU A 1 840 ? -6.228  63.588  102.983 1.00 88.13  ?  821 GLU A N     1 
ATOM   5097 C CA    . GLU A 1 840 ? -5.848  64.850  103.594 1.00 83.24  ?  821 GLU A CA    1 
ATOM   5098 C C     . GLU A 1 840 ? -6.993  65.470  104.396 1.00 86.34  ?  821 GLU A C     1 
ATOM   5099 O O     . GLU A 1 840 ? -6.725  66.231  105.325 1.00 92.44  ?  821 GLU A O     1 
ATOM   5100 C CB    . GLU A 1 840 ? -5.307  65.789  102.516 1.00 85.10  ?  821 GLU A CB    1 
ATOM   5101 C CG    . GLU A 1 840 ? -4.117  65.165  101.789 1.00 88.84  ?  821 GLU A CG    1 
ATOM   5102 C CD    . GLU A 1 840 ? -2.916  64.879  102.685 1.00 86.86  ?  821 GLU A CD    1 
ATOM   5103 O OE1   . GLU A 1 840 ? -2.588  65.707  103.534 1.00 91.97  ?  821 GLU A OE1   1 
ATOM   5104 O OE2   . GLU A 1 840 ? -2.337  63.783  102.602 1.00 90.70  ?  821 GLU A OE2   1 
ATOM   5105 N N     . ALA A 1 841 ? -8.257  65.135  104.108 1.00 85.15  ?  822 ALA A N     1 
ATOM   5106 C CA    . ALA A 1 841 ? -9.338  65.612  104.972 1.00 87.91  ?  822 ALA A CA    1 
ATOM   5107 C C     . ALA A 1 841 ? -9.206  65.033  106.372 1.00 92.17  ?  822 ALA A C     1 
ATOM   5108 O O     . ALA A 1 841 ? -9.427  65.732  107.369 1.00 93.40  ?  822 ALA A O     1 
ATOM   5109 C CB    . ALA A 1 841 ? -10.703 65.260  104.391 1.00 87.53  ?  822 ALA A CB    1 
ATOM   5110 N N     . GLY A 1 842 ? -8.858  63.757  106.466 1.00 91.36  ?  823 GLY A N     1 
ATOM   5111 C CA    . GLY A 1 842 ? -8.460  63.200  107.742 1.00 93.88  ?  823 GLY A CA    1 
ATOM   5112 C C     . GLY A 1 842 ? -7.294  63.990  108.296 1.00 90.71  ?  823 GLY A C     1 
ATOM   5113 O O     . GLY A 1 842 ? -7.445  64.711  109.284 1.00 93.40  ?  823 GLY A O     1 
ATOM   5114 N N     . ARG A 1 843 ? -6.147  63.918  107.615 1.00 87.73  ?  824 ARG A N     1 
ATOM   5115 C CA    . ARG A 1 843 ? -4.913  64.454  108.175 1.00 85.51  ?  824 ARG A CA    1 
ATOM   5116 C C     . ARG A 1 843 ? -5.052  65.910  108.599 1.00 89.68  ?  824 ARG A C     1 
ATOM   5117 O O     . ARG A 1 843 ? -4.473  66.325  109.613 1.00 92.08  ?  824 ARG A O     1 
ATOM   5118 C CB    . ARG A 1 843 ? -3.768  64.294  107.183 1.00 84.40  ?  824 ARG A CB    1 
ATOM   5119 C CG    . ARG A 1 843 ? -2.546  64.994  107.697 1.00 89.01  ?  824 ARG A CG    1 
ATOM   5120 C CD    . ARG A 1 843 ? -1.324  64.210  107.437 1.00 89.86  ?  824 ARG A CD    1 
ATOM   5121 N NE    . ARG A 1 843 ? -1.183  63.904  106.034 1.00 93.37  ?  824 ARG A NE    1 
ATOM   5122 C CZ    . ARG A 1 843 ? -0.119  63.286  105.531 1.00 103.38 ?  824 ARG A CZ    1 
ATOM   5123 N NH1   . ARG A 1 843 ? 0.868   62.915  106.348 1.00 105.69 ?  824 ARG A NH1   1 
ATOM   5124 N NH2   . ARG A 1 843 ? -0.042  63.022  104.223 1.00 102.41 ?  824 ARG A NH2   1 
ATOM   5125 N N     . ILE A 1 844 ? -5.822  66.700  107.848 1.00 96.70  ?  825 ILE A N     1 
ATOM   5126 C CA    . ILE A 1 844 ? -5.990  68.115  108.190 1.00 98.77  ?  825 ILE A CA    1 
ATOM   5127 C C     . ILE A 1 844 ? -6.827  68.255  109.456 1.00 93.40  ?  825 ILE A C     1 
ATOM   5128 O O     . ILE A 1 844 ? -6.402  68.892  110.423 1.00 94.11  ?  825 ILE A O     1 
ATOM   5129 C CB    . ILE A 1 844 ? -6.597  68.902  107.005 1.00 93.59  ?  825 ILE A CB    1 
ATOM   5130 C CG1   . ILE A 1 844 ? -5.509  69.249  105.987 1.00 81.81  ?  825 ILE A CG1   1 
ATOM   5131 C CG2   . ILE A 1 844 ? -7.311  70.162  107.491 1.00 86.28  ?  825 ILE A CG2   1 
ATOM   5132 C CD1   . ILE A 1 844 ? -6.041  69.849  104.754 1.00 82.23  ?  825 ILE A CD1   1 
ATOM   5133 N N     . ALA A 1 845 ? -8.009  67.626  109.478 1.00 92.19  ?  826 ALA A N     1 
ATOM   5134 C CA    . ALA A 1 845 ? -8.912  67.768  110.615 1.00 91.92  ?  826 ALA A CA    1 
ATOM   5135 C C     . ALA A 1 845 ? -8.250  67.317  111.910 1.00 97.88  ?  826 ALA A C     1 
ATOM   5136 O O     . ALA A 1 845 ? -8.371  67.989  112.940 1.00 105.18 ?  826 ALA A O     1 
ATOM   5137 C CB    . ALA A 1 845 ? -10.201 66.989  110.359 1.00 92.39  ?  826 ALA A CB    1 
ATOM   5138 N N     . ASP A 1 846 ? -7.526  66.195  111.877 1.00 98.44  ?  827 ASP A N     1 
ATOM   5139 C CA    . ASP A 1 846 ? -6.766  65.758  113.050 1.00 101.40 ?  827 ASP A CA    1 
ATOM   5140 C C     . ASP A 1 846 ? -5.768  66.824  113.502 1.00 102.29 ?  827 ASP A C     1 
ATOM   5141 O O     . ASP A 1 846 ? -5.608  67.066  114.707 1.00 110.33 ?  827 ASP A O     1 
ATOM   5142 C CB    . ASP A 1 846 ? -6.038  64.446  112.739 1.00 103.63 ?  827 ASP A CB    1 
ATOM   5143 C CG    . ASP A 1 846 ? -6.984  63.246  112.618 1.00 105.16 ?  827 ASP A CG    1 
ATOM   5144 O OD1   . ASP A 1 846 ? -8.224  63.420  112.725 1.00 99.75  ?  827 ASP A OD1   1 
ATOM   5145 O OD2   . ASP A 1 846 ? -6.467  62.134  112.348 1.00 105.40 ?  827 ASP A OD2   1 
ATOM   5146 N N     . GLN A 1 847 ? -5.105  67.489  112.553 1.00 100.18 ?  828 GLN A N     1 
ATOM   5147 C CA    . GLN A 1 847 ? -4.098  68.484  112.900 1.00 101.99 ?  828 GLN A CA    1 
ATOM   5148 C C     . GLN A 1 847 ? -4.693  69.793  113.419 1.00 96.55  ?  828 GLN A C     1 
ATOM   5149 O O     . GLN A 1 847 ? -3.985  70.554  114.077 1.00 95.66  ?  828 GLN A O     1 
ATOM   5150 C CB    . GLN A 1 847 ? -3.219  68.795  111.683 1.00 104.83 ?  828 GLN A CB    1 
ATOM   5151 C CG    . GLN A 1 847 ? -1.900  69.495  112.032 1.00 106.52 ?  828 GLN A CG    1 
ATOM   5152 C CD    . GLN A 1 847 ? -0.965  68.578  112.827 1.00 118.28 ?  828 GLN A CD    1 
ATOM   5153 O OE1   . GLN A 1 847 ? -0.532  68.920  113.935 1.00 122.22 ?  828 GLN A OE1   1 
ATOM   5154 N NE2   . GLN A 1 847 ? -0.627  67.412  112.242 1.00 112.56 ?  828 GLN A NE2   1 
ATOM   5155 N N     . PHE A 1 848 ? -5.962  70.085  113.115 1.00 99.14  ?  829 PHE A N     1 
ATOM   5156 C CA    . PHE A 1 848 ? -6.582  71.380  113.407 1.00 98.73  ?  829 PHE A CA    1 
ATOM   5157 C C     . PHE A 1 848 ? -7.872  71.267  114.198 1.00 94.97  ?  829 PHE A C     1 
ATOM   5158 O O     . PHE A 1 848 ? -8.388  72.294  114.638 1.00 98.84  ?  829 PHE A O     1 
ATOM   5159 C CB    . PHE A 1 848 ? -6.841  72.182  112.095 1.00 100.29 ?  829 PHE A CB    1 
ATOM   5160 C CG    . PHE A 1 848 ? -5.578  72.738  111.463 1.00 92.89  ?  829 PHE A CG    1 
ATOM   5161 C CD1   . PHE A 1 848 ? -5.082  73.971  111.851 1.00 97.12  ?  829 PHE A CD1   1 
ATOM   5162 C CD2   . PHE A 1 848 ? -4.831  71.992  110.576 1.00 96.74  ?  829 PHE A CD2   1 
ATOM   5163 C CE1   . PHE A 1 848 ? -3.889  74.477  111.322 1.00 97.85  ?  829 PHE A CE1   1 
ATOM   5164 C CE2   . PHE A 1 848 ? -3.631  72.490  110.050 1.00 97.64  ?  829 PHE A CE2   1 
ATOM   5165 C CZ    . PHE A 1 848 ? -3.166  73.733  110.423 1.00 94.84  ?  829 PHE A CZ    1 
ATOM   5166 N N     . LEU A 1 849 ? -8.394  70.064  114.410 1.00 97.68  ?  830 LEU A N     1 
ATOM   5167 C CA    . LEU A 1 849 ? -9.606  69.865  115.194 1.00 106.39 ?  830 LEU A CA    1 
ATOM   5168 C C     . LEU A 1 849 ? -9.436  68.760  116.237 1.00 111.11 ?  830 LEU A C     1 
ATOM   5169 O O     . LEU A 1 849 ? -10.438 68.303  116.810 1.00 115.33 ?  830 LEU A O     1 
ATOM   5170 C CB    . LEU A 1 849 ? -10.781 69.529  114.272 1.00 100.97 ?  830 LEU A CB    1 
ATOM   5171 C CG    . LEU A 1 849 ? -11.144 70.539  113.187 1.00 94.38  ?  830 LEU A CG    1 
ATOM   5172 C CD1   . LEU A 1 849 ? -12.365 70.059  112.382 1.00 97.10  ?  830 LEU A CD1   1 
ATOM   5173 C CD2   . LEU A 1 849 ? -11.397 71.891  113.801 1.00 91.93  ?  830 LEU A CD2   1 
ATOM   5174 N N     . GLY A 1 850 ? -8.190  68.357  116.443 1.00 107.85 ?  831 GLY A N     1 
ATOM   5175 C CA    . GLY A 1 850 ? -7.853  67.437  117.535 1.00 116.15 ?  831 GLY A CA    1 
ATOM   5176 C C     . GLY A 1 850 ? -8.090  65.969  117.286 1.00 117.26 ?  831 GLY A C     1 
ATOM   5177 O O     . GLY A 1 850 ? -9.149  65.571  116.811 1.00 110.29 ?  831 GLY A O     1 
ATOM   5178 N N     . ALA A 1 851 ? -7.130  65.180  117.733 1.00 116.86 ?  832 ALA A N     1 
ATOM   5179 C CA    . ALA A 1 851 ? -7.234  63.721  117.621 1.00 122.71 ?  832 ALA A CA    1 
ATOM   5180 C C     . ALA A 1 851 ? -8.061  63.273  118.820 1.00 135.20 ?  832 ALA A C     1 
ATOM   5181 O O     . ALA A 1 851 ? -7.474  62.909  119.834 1.00 140.77 ?  832 ALA A O     1 
ATOM   5182 C CB    . ALA A 1 851 ? -5.842  63.156  117.690 1.00 123.12 ?  832 ALA A CB    1 
ATOM   5183 N N     . MET A 1 852 ? -9.383  63.244  118.685 1.00 135.91 ?  833 MET A N     1 
ATOM   5184 C CA    . MET A 1 852 ? -10.227 62.874  119.849 1.00 141.81 ?  833 MET A CA    1 
ATOM   5185 C C     . MET A 1 852 ? -10.534 61.377  119.843 1.00 138.06 ?  833 MET A C     1 
ATOM   5186 O O     . MET A 1 852 ? -11.434 60.974  120.589 1.00 133.65 ?  833 MET A O     1 
ATOM   5187 C CB    . MET A 1 852 ? -11.532 63.671  119.864 1.00 147.15 ?  833 MET A CB    1 
ATOM   5188 C CG    . MET A 1 852 ? -11.320 65.169  119.717 1.00 148.41 ?  833 MET A CG    1 
ATOM   5189 S SD    . MET A 1 852 ? -10.950 66.038  121.263 1.00 153.64 ?  833 MET A SD    1 
ATOM   5190 C CE    . MET A 1 852 ? -11.584 67.669  120.884 1.00 120.59 ?  833 MET A CE    1 
ATOM   5191 N N     . TYR A 1 853 ? -9.791  60.574  119.107 1.00 134.97 ?  834 TYR A N     1 
ATOM   5192 C CA    . TYR A 1 853 ? -10.169 59.145  119.158 1.00 135.06 ?  834 TYR A CA    1 
ATOM   5193 C C     . TYR A 1 853 ? -8.932  58.347  119.537 1.00 132.36 ?  834 TYR A C     1 
ATOM   5194 O O     . TYR A 1 853 ? -8.963  57.127  119.466 1.00 122.69 ?  834 TYR A O     1 
ATOM   5195 C CB    . TYR A 1 853 ? -10.821 58.720  117.843 1.00 129.95 ?  834 TYR A CB    1 
ATOM   5196 C CG    . TYR A 1 853 ? -10.030 59.130  116.631 1.00 132.99 ?  834 TYR A CG    1 
ATOM   5197 C CD1   . TYR A 1 853 ? -10.506 60.070  115.738 1.00 127.25 ?  834 TYR A CD1   1 
ATOM   5198 C CD2   . TYR A 1 853 ? -8.780  58.589  116.408 1.00 130.16 ?  834 TYR A CD2   1 
ATOM   5199 C CE1   . TYR A 1 853 ? -9.757  60.447  114.641 1.00 118.42 ?  834 TYR A CE1   1 
ATOM   5200 C CE2   . TYR A 1 853 ? -8.020  58.950  115.315 1.00 120.46 ?  834 TYR A CE2   1 
ATOM   5201 C CZ    . TYR A 1 853 ? -8.514  59.886  114.437 1.00 119.29 ?  834 TYR A CZ    1 
ATOM   5202 O OH    . TYR A 1 853 ? -7.752  60.223  113.369 1.00 122.53 ?  834 TYR A OH    1 
ATOM   5203 N N     . THR A 1 854 ? -7.878  59.028  119.964 1.00 135.70 ?  835 THR A N     1 
ATOM   5204 C CA    . THR A 1 854 ? -6.689  58.206  120.314 1.00 134.07 ?  835 THR A CA    1 
ATOM   5205 C C     . THR A 1 854 ? -6.423  58.088  121.819 1.00 137.89 ?  835 THR A C     1 
ATOM   5206 O O     . THR A 1 854 ? -5.256  57.881  122.170 1.00 139.28 ?  835 THR A O     1 
ATOM   5207 C CB    . THR A 1 854 ? -5.456  58.665  119.534 1.00 130.96 ?  835 THR A CB    1 
ATOM   5208 O OG1   . THR A 1 854 ? -4.614  59.394  120.421 1.00 144.19 ?  835 THR A OG1   1 
ATOM   5209 C CG2   . THR A 1 854 ? -5.811  59.532  118.352 1.00 120.05 ?  835 THR A CG2   1 
ATOM   5210 N N     . LEU A 1 855 ? -7.449  58.181  122.662 1.00 135.10 ?  836 LEU A N     1 
ATOM   5211 C CA    . LEU A 1 855 ? -7.263  58.030  124.119 1.00 132.95 ?  836 LEU A CA    1 
ATOM   5212 C C     . LEU A 1 855 ? -7.482  56.551  124.559 1.00 116.84 ?  836 LEU A C     1 
ATOM   5213 O O     . LEU A 1 855 ? -7.838  56.229  125.710 1.00 92.47  ?  836 LEU A O     1 
ATOM   5214 C CB    . LEU A 1 855 ? -8.211  58.979  124.880 1.00 138.07 ?  836 LEU A CB    1 
ATOM   5215 C CG    . LEU A 1 855 ? -7.775  60.412  125.266 1.00 132.72 ?  836 LEU A CG    1 
ATOM   5216 C CD1   . LEU A 1 855 ? -7.227  61.218  124.047 1.00 129.34 ?  836 LEU A CD1   1 
ATOM   5217 C CD2   . LEU A 1 855 ? -8.901  61.163  126.006 1.00 123.65 ?  836 LEU A CD2   1 
ATOM   5218 N N     . ARG B 2 12  ? 11.368  31.784  90.291  1.00 141.60 ?  308 ARG B N     1 
ATOM   5219 C CA    . ARG B 2 12  ? 12.555  30.930  90.334  1.00 148.78 ?  308 ARG B CA    1 
ATOM   5220 C C     . ARG B 2 12  ? 13.105  30.600  88.941  1.00 151.17 ?  308 ARG B C     1 
ATOM   5221 O O     . ARG B 2 12  ? 14.320  30.630  88.722  1.00 153.12 ?  308 ARG B O     1 
ATOM   5222 C CB    . ARG B 2 12  ? 12.256  29.633  91.099  1.00 150.45 ?  308 ARG B CB    1 
ATOM   5223 C CG    . ARG B 2 12  ? 12.532  29.686  92.607  1.00 156.44 ?  308 ARG B CG    1 
ATOM   5224 C CD    . ARG B 2 12  ? 14.047  29.692  92.902  1.00 161.76 ?  308 ARG B CD    1 
ATOM   5225 N NE    . ARG B 2 12  ? 14.387  30.188  94.241  1.00 168.31 ?  308 ARG B NE    1 
ATOM   5226 C CZ    . ARG B 2 12  ? 14.756  31.443  94.516  1.00 168.27 ?  308 ARG B CZ    1 
ATOM   5227 N NH1   . ARG B 2 12  ? 14.840  32.346  93.546  1.00 164.70 ?  308 ARG B NH1   1 
ATOM   5228 N NH2   . ARG B 2 12  ? 15.048  31.802  95.764  1.00 164.86 ?  308 ARG B NH2   1 
ATOM   5229 N N     . LYS B 2 13  ? 12.225  30.283  87.998  1.00 146.81 ?  309 LYS B N     1 
ATOM   5230 C CA    . LYS B 2 13  ? 12.662  29.926  86.658  1.00 142.57 ?  309 LYS B CA    1 
ATOM   5231 C C     . LYS B 2 13  ? 11.873  30.752  85.648  1.00 143.62 ?  309 LYS B C     1 
ATOM   5232 O O     . LYS B 2 13  ? 10.726  31.130  85.922  1.00 141.25 ?  309 LYS B O     1 
ATOM   5233 C CB    . LYS B 2 13  ? 12.460  28.417  86.408  1.00 147.28 ?  309 LYS B CB    1 
ATOM   5234 C CG    . LYS B 2 13  ? 13.545  27.496  87.044  1.00 147.05 ?  309 LYS B CG    1 
ATOM   5235 C CD    . LYS B 2 13  ? 13.520  26.041  86.498  1.00 140.43 ?  309 LYS B CD    1 
ATOM   5236 C CE    . LYS B 2 13  ? 14.633  25.170  87.114  1.00 128.15 ?  309 LYS B CE    1 
ATOM   5237 N NZ    . LYS B 2 13  ? 14.731  23.799  86.527  1.00 117.13 ?  309 LYS B NZ    1 
ATOM   5238 N N     . PRO B 2 14  ? 12.462  31.073  84.489  1.00 145.66 ?  310 PRO B N     1 
ATOM   5239 C CA    . PRO B 2 14  ? 11.729  31.851  83.458  1.00 139.39 ?  310 PRO B CA    1 
ATOM   5240 C C     . PRO B 2 14  ? 10.495  31.100  83.000  1.00 137.57 ?  310 PRO B C     1 
ATOM   5241 O O     . PRO B 2 14  ? 10.305  29.930  83.365  1.00 140.46 ?  310 PRO B O     1 
ATOM   5242 C CB    . PRO B 2 14  ? 12.747  31.979  82.308  1.00 132.29 ?  310 PRO B CB    1 
ATOM   5243 C CG    . PRO B 2 14  ? 14.073  31.715  82.926  1.00 137.06 ?  310 PRO B CG    1 
ATOM   5244 C CD    . PRO B 2 14  ? 13.815  30.709  84.026  1.00 143.09 ?  310 PRO B CD    1 
ATOM   5245 N N     . PRO B 2 15  ? 9.626   31.721  82.206  1.00 133.86 ?  311 PRO B N     1 
ATOM   5246 C CA    . PRO B 2 15  ? 8.615   30.926  81.506  1.00 137.74 ?  311 PRO B CA    1 
ATOM   5247 C C     . PRO B 2 15  ? 9.329   29.929  80.608  1.00 144.75 ?  311 PRO B C     1 
ATOM   5248 O O     . PRO B 2 15  ? 10.426  30.205  80.111  1.00 148.02 ?  311 PRO B O     1 
ATOM   5249 C CB    . PRO B 2 15  ? 7.829   31.964  80.696  1.00 134.27 ?  311 PRO B CB    1 
ATOM   5250 C CG    . PRO B 2 15  ? 8.075   33.253  81.393  1.00 133.13 ?  311 PRO B CG    1 
ATOM   5251 C CD    . PRO B 2 15  ? 9.477   33.159  81.935  1.00 133.81 ?  311 PRO B CD    1 
ATOM   5252 N N     . LYS B 2 16  ? 8.730   28.743  80.443  1.00 147.60 ?  312 LYS B N     1 
ATOM   5253 C CA    . LYS B 2 16  ? 9.303   27.748  79.537  1.00 144.41 ?  312 LYS B CA    1 
ATOM   5254 C C     . LYS B 2 16  ? 9.572   28.387  78.185  1.00 143.16 ?  312 LYS B C     1 
ATOM   5255 O O     . LYS B 2 16  ? 8.746   29.142  77.663  1.00 140.62 ?  312 LYS B O     1 
ATOM   5256 C CB    . LYS B 2 16  ? 8.382   26.531  79.372  1.00 138.87 ?  312 LYS B CB    1 
ATOM   5257 C CG    . LYS B 2 16  ? 8.619   25.403  80.376  1.00 141.50 ?  312 LYS B CG    1 
ATOM   5258 C CD    . LYS B 2 16  ? 8.092   25.766  81.762  1.00 149.11 ?  312 LYS B CD    1 
ATOM   5259 C CE    . LYS B 2 16  ? 8.035   24.562  82.703  1.00 146.36 ?  312 LYS B CE    1 
ATOM   5260 N NZ    . LYS B 2 16  ? 7.342   24.897  83.985  1.00 131.23 ?  312 LYS B NZ    1 
ATOM   5261 N N     . GLY B 2 17  ? 10.759  28.124  77.645  1.00 141.42 ?  313 GLY B N     1 
ATOM   5262 C CA    . GLY B 2 17  ? 11.141  28.618  76.355  1.00 143.63 ?  313 GLY B CA    1 
ATOM   5263 C C     . GLY B 2 17  ? 11.939  29.903  76.392  1.00 143.49 ?  313 GLY B C     1 
ATOM   5264 O O     . GLY B 2 17  ? 12.644  30.204  75.425  1.00 148.88 ?  313 GLY B O     1 
ATOM   5265 N N     . MET B 2 18  ? 11.836  30.677  77.466  1.00 133.46 ?  314 MET B N     1 
ATOM   5266 C CA    . MET B 2 18  ? 12.721  31.821  77.600  1.00 132.88 ?  314 MET B CA    1 
ATOM   5267 C C     . MET B 2 18  ? 14.116  31.324  77.938  1.00 132.59 ?  314 MET B C     1 
ATOM   5268 O O     . MET B 2 18  ? 14.279  30.317  78.635  1.00 133.08 ?  314 MET B O     1 
ATOM   5269 C CB    . MET B 2 18  ? 12.207  32.772  78.674  1.00 139.50 ?  314 MET B CB    1 
ATOM   5270 C CG    . MET B 2 18  ? 10.826  33.294  78.352  1.00 138.38 ?  314 MET B CG    1 
ATOM   5271 S SD    . MET B 2 18  ? 10.848  34.195  76.801  1.00 142.40 ?  314 MET B SD    1 
ATOM   5272 C CE    . MET B 2 18  ? 9.096   34.411  76.530  1.00 127.97 ?  314 MET B CE    1 
ATOM   5273 N N     . PHE B 2 19  ? 15.126  32.006  77.411  1.00 130.46 ?  315 PHE B N     1 
ATOM   5274 C CA    . PHE B 2 19  ? 16.517  31.610  77.622  1.00 135.74 ?  315 PHE B CA    1 
ATOM   5275 C C     . PHE B 2 19  ? 17.263  32.809  78.179  1.00 139.43 ?  315 PHE B C     1 
ATOM   5276 O O     . PHE B 2 19  ? 17.643  33.717  77.431  1.00 141.34 ?  315 PHE B O     1 
ATOM   5277 C CB    . PHE B 2 19  ? 17.146  31.085  76.338  1.00 139.87 ?  315 PHE B CB    1 
ATOM   5278 C CG    . PHE B 2 19  ? 16.800  29.641  76.046  1.00 142.78 ?  315 PHE B CG    1 
ATOM   5279 C CD1   . PHE B 2 19  ? 15.525  29.286  75.608  1.00 139.49 ?  315 PHE B CD1   1 
ATOM   5280 C CD2   . PHE B 2 19  ? 17.745  28.635  76.228  1.00 137.98 ?  315 PHE B CD2   1 
ATOM   5281 C CE1   . PHE B 2 19  ? 15.197  27.964  75.348  1.00 132.22 ?  315 PHE B CE1   1 
ATOM   5282 C CE2   . PHE B 2 19  ? 17.426  27.312  75.968  1.00 133.41 ?  315 PHE B CE2   1 
ATOM   5283 C CZ    . PHE B 2 19  ? 16.149  26.977  75.529  1.00 133.03 ?  315 PHE B CZ    1 
ATOM   5284 N N     . LEU B 2 20  ? 17.459  32.798  79.505  1.00 138.63 ?  316 LEU B N     1 
ATOM   5285 C CA    . LEU B 2 20  ? 17.898  33.956  80.259  1.00 140.64 ?  316 LEU B CA    1 
ATOM   5286 C C     . LEU B 2 20  ? 18.997  33.483  81.215  1.00 150.21 ?  316 LEU B C     1 
ATOM   5287 O O     . LEU B 2 20  ? 18.837  33.408  82.436  1.00 155.30 ?  316 LEU B O     1 
ATOM   5288 C CB    . LEU B 2 20  ? 16.723  34.597  81.006  1.00 134.34 ?  316 LEU B CB    1 
ATOM   5289 C CG    . LEU B 2 20  ? 15.399  34.732  80.240  1.00 127.34 ?  316 LEU B CG    1 
ATOM   5290 C CD1   . LEU B 2 20  ? 14.271  35.256  81.106  1.00 122.05 ?  316 LEU B CD1   1 
ATOM   5291 C CD2   . LEU B 2 20  ? 15.566  35.630  79.026  1.00 131.95 ?  316 LEU B CD2   1 
ATOM   5292 N N     . SER B 2 21  ? 20.143  33.117  80.653  1.00 151.48 ?  317 SER B N     1 
ATOM   5293 C CA    . SER B 2 21  ? 21.275  32.758  81.490  1.00 158.26 ?  317 SER B CA    1 
ATOM   5294 C C     . SER B 2 21  ? 21.954  34.018  81.990  1.00 156.28 ?  317 SER B C     1 
ATOM   5295 O O     . SER B 2 21  ? 21.968  35.047  81.308  1.00 151.57 ?  317 SER B O     1 
ATOM   5296 C CB    . SER B 2 21  ? 22.290  31.926  80.716  1.00 160.85 ?  317 SER B CB    1 
ATOM   5297 O OG    . SER B 2 21  ? 23.189  32.782  80.035  1.00 158.95 ?  317 SER B OG    1 
ATOM   5298 N N     . GLN B 2 22  ? 22.535  33.928  83.185  1.00 154.54 ?  318 GLN B N     1 
ATOM   5299 C CA    . GLN B 2 22  ? 23.296  35.063  83.692  1.00 160.95 ?  318 GLN B CA    1 
ATOM   5300 C C     . GLN B 2 22  ? 24.396  35.460  82.710  1.00 159.42 ?  318 GLN B C     1 
ATOM   5301 O O     . GLN B 2 22  ? 24.569  36.644  82.384  1.00 156.28 ?  318 GLN B O     1 
ATOM   5302 C CB    . GLN B 2 22  ? 23.876  34.730  85.069  1.00 161.83 ?  318 GLN B CB    1 
ATOM   5303 C CG    . GLN B 2 22  ? 24.964  35.697  85.504  1.00 163.10 ?  318 GLN B CG    1 
ATOM   5304 C CD    . GLN B 2 22  ? 24.482  37.141  85.505  1.00 163.03 ?  318 GLN B CD    1 
ATOM   5305 O OE1   . GLN B 2 22  ? 25.213  38.055  85.108  1.00 163.07 ?  318 GLN B OE1   1 
ATOM   5306 N NE2   . GLN B 2 22  ? 23.244  37.352  85.950  1.00 157.21 ?  318 GLN B NE2   1 
ATOM   5307 N N     . GLU B 2 23  ? 25.133  34.463  82.215  1.00 158.33 ?  319 GLU B N     1 
ATOM   5308 C CA    . GLU B 2 23  ? 26.195  34.674  81.236  1.00 159.19 ?  319 GLU B CA    1 
ATOM   5309 C C     . GLU B 2 23  ? 25.715  35.501  80.040  1.00 162.38 ?  319 GLU B C     1 
ATOM   5310 O O     . GLU B 2 23  ? 26.305  36.539  79.710  1.00 162.19 ?  319 GLU B O     1 
ATOM   5311 C CB    . GLU B 2 23  ? 26.708  33.300  80.794  1.00 161.53 ?  319 GLU B CB    1 
ATOM   5312 C CG    . GLU B 2 23  ? 27.909  33.257  79.865  1.00 162.07 ?  319 GLU B CG    1 
ATOM   5313 C CD    . GLU B 2 23  ? 28.213  31.831  79.404  1.00 163.01 ?  319 GLU B CD    1 
ATOM   5314 O OE1   . GLU B 2 23  ? 27.320  30.960  79.534  1.00 159.70 ?  319 GLU B OE1   1 
ATOM   5315 O OE2   . GLU B 2 23  ? 29.342  31.576  78.926  1.00 161.83 ?  319 GLU B OE2   1 
ATOM   5316 N N     . ASP B 2 24  ? 24.628  35.056  79.388  1.00 161.83 ?  320 ASP B N     1 
ATOM   5317 C CA    . ASP B 2 24  ? 24.151  35.687  78.154  1.00 156.34 ?  320 ASP B CA    1 
ATOM   5318 C C     . ASP B 2 24  ? 23.738  37.137  78.361  1.00 157.48 ?  320 ASP B C     1 
ATOM   5319 O O     . ASP B 2 24  ? 23.832  37.944  77.426  1.00 152.75 ?  320 ASP B O     1 
ATOM   5320 C CB    . ASP B 2 24  ? 22.955  34.918  77.593  1.00 151.93 ?  320 ASP B CB    1 
ATOM   5321 C CG    . ASP B 2 24  ? 23.308  33.520  77.153  1.00 153.60 ?  320 ASP B CG    1 
ATOM   5322 O OD1   . ASP B 2 24  ? 24.464  33.099  77.370  1.00 156.55 ?  320 ASP B OD1   1 
ATOM   5323 O OD2   . ASP B 2 24  ? 22.418  32.835  76.600  1.00 152.51 ?  320 ASP B OD2   1 
ATOM   5324 N N     . VAL B 2 25  ? 23.254  37.472  79.564  1.00 159.61 ?  321 VAL B N     1 
ATOM   5325 C CA    . VAL B 2 25  ? 22.655  38.783  79.807  1.00 157.04 ?  321 VAL B CA    1 
ATOM   5326 C C     . VAL B 2 25  ? 23.713  39.882  79.777  1.00 157.49 ?  321 VAL B C     1 
ATOM   5327 O O     . VAL B 2 25  ? 23.505  40.949  79.177  1.00 151.65 ?  321 VAL B O     1 
ATOM   5328 C CB    . VAL B 2 25  ? 21.886  38.764  81.139  1.00 152.05 ?  321 VAL B CB    1 
ATOM   5329 C CG1   . VAL B 2 25  ? 21.279  40.116  81.399  1.00 149.58 ?  321 VAL B CG1   1 
ATOM   5330 C CG2   . VAL B 2 25  ? 20.787  37.721  81.094  1.00 148.21 ?  321 VAL B CG2   1 
ATOM   5331 N N     . GLU B 2 26  ? 24.858  39.641  80.423  1.00 155.49 ?  322 GLU B N     1 
ATOM   5332 C CA    . GLU B 2 26  ? 25.967  40.587  80.366  1.00 156.62 ?  322 GLU B CA    1 
ATOM   5333 C C     . GLU B 2 26  ? 26.478  40.767  78.944  1.00 158.02 ?  322 GLU B C     1 
ATOM   5334 O O     . GLU B 2 26  ? 27.062  41.808  78.618  1.00 155.73 ?  322 GLU B O     1 
ATOM   5335 C CB    . GLU B 2 26  ? 27.101  40.097  81.256  1.00 158.77 ?  322 GLU B CB    1 
ATOM   5336 C CG    . GLU B 2 26  ? 26.787  40.159  82.726  1.00 163.79 ?  322 GLU B CG    1 
ATOM   5337 C CD    . GLU B 2 26  ? 27.739  39.317  83.546  1.00 168.95 ?  322 GLU B CD    1 
ATOM   5338 O OE1   . GLU B 2 26  ? 27.817  38.095  83.277  1.00 164.87 ?  322 GLU B OE1   1 
ATOM   5339 O OE2   . GLU B 2 26  ? 28.398  39.876  84.456  1.00 169.90 ?  322 GLU B OE2   1 
ATOM   5340 N N     . ALA B 2 27  ? 26.258  39.762  78.088  1.00 160.02 ?  323 ALA B N     1 
ATOM   5341 C CA    . ALA B 2 27  ? 26.885  39.700  76.772  1.00 160.30 ?  323 ALA B CA    1 
ATOM   5342 C C     . ALA B 2 27  ? 26.172  40.557  75.726  1.00 160.25 ?  323 ALA B C     1 
ATOM   5343 O O     . ALA B 2 27  ? 26.806  41.008  74.764  1.00 161.81 ?  323 ALA B O     1 
ATOM   5344 C CB    . ALA B 2 27  ? 26.952  38.243  76.309  1.00 153.37 ?  323 ALA B CB    1 
ATOM   5345 N N     . VAL B 2 28  ? 24.865  40.777  75.876  1.00 159.46 ?  324 VAL B N     1 
ATOM   5346 C CA    . VAL B 2 28  ? 24.142  41.656  74.958  1.00 159.22 ?  324 VAL B CA    1 
ATOM   5347 C C     . VAL B 2 28  ? 24.265  43.119  75.387  1.00 161.49 ?  324 VAL B C     1 
ATOM   5348 O O     . VAL B 2 28  ? 23.987  44.036  74.593  1.00 155.92 ?  324 VAL B O     1 
ATOM   5349 C CB    . VAL B 2 28  ? 22.679  41.181  74.896  1.00 154.59 ?  324 VAL B CB    1 
ATOM   5350 C CG1   . VAL B 2 28  ? 21.872  41.942  73.851  1.00 148.96 ?  324 VAL B CG1   1 
ATOM   5351 C CG2   . VAL B 2 28  ? 22.641  39.696  74.635  1.00 143.18 ?  324 VAL B CG2   1 
ATOM   5352 N N     . SER B 2 29  ? 24.739  43.347  76.613  1.00 164.20 ?  325 SER B N     1 
ATOM   5353 C CA    . SER B 2 29  ? 24.633  44.620  77.301  1.00 162.37 ?  325 SER B CA    1 
ATOM   5354 C C     . SER B 2 29  ? 25.971  45.255  77.666  1.00 162.27 ?  325 SER B C     1 
ATOM   5355 O O     . SER B 2 29  ? 25.974  46.350  78.242  1.00 163.88 ?  325 SER B O     1 
ATOM   5356 C CB    . SER B 2 29  ? 23.778  44.428  78.562  1.00 157.11 ?  325 SER B CB    1 
ATOM   5357 O OG    . SER B 2 29  ? 24.272  43.348  79.341  1.00 155.84 ?  325 SER B OG    1 
ATOM   5358 N N     . ALA B 2 30  ? 27.103  44.611  77.351  1.00 162.54 ?  326 ALA B N     1 
ATOM   5359 C CA    . ALA B 2 30  ? 28.405  45.221  77.616  1.00 165.26 ?  326 ALA B CA    1 
ATOM   5360 C C     . ALA B 2 30  ? 28.477  46.637  77.050  1.00 169.05 ?  326 ALA B C     1 
ATOM   5361 O O     . ALA B 2 30  ? 29.018  47.551  77.692  1.00 168.72 ?  326 ALA B O     1 
ATOM   5362 C CB    . ALA B 2 30  ? 29.520  44.351  77.036  1.00 163.98 ?  326 ALA B CB    1 
ATOM   5363 N N     . ASN B 2 31  ? 27.911  46.844  75.862  1.00 168.27 ?  327 ASN B N     1 
ATOM   5364 C CA    . ASN B 2 31  ? 27.796  48.181  75.292  1.00 171.42 ?  327 ASN B CA    1 
ATOM   5365 C C     . ASN B 2 31  ? 26.532  48.243  74.431  1.00 166.71 ?  327 ASN B C     1 
ATOM   5366 O O     . ASN B 2 31  ? 25.683  47.343  74.472  1.00 160.94 ?  327 ASN B O     1 
ATOM   5367 C CB    . ASN B 2 31  ? 29.085  48.548  74.539  1.00 170.77 ?  327 ASN B CB    1 
ATOM   5368 C CG    . ASN B 2 31  ? 29.371  47.623  73.378  1.00 169.69 ?  327 ASN B CG    1 
ATOM   5369 O OD1   . ASN B 2 31  ? 28.816  47.779  72.286  1.00 168.96 ?  327 ASN B OD1   1 
ATOM   5370 N ND2   . ASN B 2 31  ? 30.212  46.622  73.621  1.00 168.83 ?  327 ASN B ND2   1 
ATOM   5371 N N     . ALA B 2 32  ? 26.407  49.332  73.666  1.00 165.63 ?  328 ALA B N     1 
ATOM   5372 C CA    . ALA B 2 32  ? 25.215  49.631  72.880  1.00 164.14 ?  328 ALA B CA    1 
ATOM   5373 C C     . ALA B 2 32  ? 24.965  48.572  71.813  1.00 169.07 ?  328 ALA B C     1 
ATOM   5374 O O     . ALA B 2 32  ? 24.002  47.802  71.921  1.00 169.45 ?  328 ALA B O     1 
ATOM   5375 C CB    . ALA B 2 32  ? 25.337  51.015  72.238  1.00 160.33 ?  328 ALA B CB    1 
ATOM   5376 N N     . THR B 2 33  ? 25.825  48.519  70.785  1.00 168.64 ?  329 THR B N     1 
ATOM   5377 C CA    . THR B 2 33  ? 25.690  47.555  69.693  1.00 163.55 ?  329 THR B CA    1 
ATOM   5378 C C     . THR B 2 33  ? 26.233  46.156  70.029  1.00 162.80 ?  329 THR B C     1 
ATOM   5379 O O     . THR B 2 33  ? 26.281  45.319  69.121  1.00 162.23 ?  329 THR B O     1 
ATOM   5380 C CB    . THR B 2 33  ? 26.376  48.071  68.415  1.00 162.88 ?  329 THR B CB    1 
ATOM   5381 O OG1   . THR B 2 33  ? 27.716  48.491  68.710  1.00 163.39 ?  329 THR B OG1   1 
ATOM   5382 C CG2   . THR B 2 33  ? 25.580  49.217  67.764  1.00 157.64 ?  329 THR B CG2   1 
ATOM   5383 N N     . ALA B 2 34  ? 26.624  45.874  71.287  1.00 166.51 ?  330 ALA B N     1 
ATOM   5384 C CA    . ALA B 2 34  ? 27.008  44.519  71.707  1.00 158.22 ?  330 ALA B CA    1 
ATOM   5385 C C     . ALA B 2 34  ? 25.883  43.515  71.511  1.00 152.95 ?  330 ALA B C     1 
ATOM   5386 O O     . ALA B 2 34  ? 26.127  42.304  71.593  1.00 146.50 ?  330 ALA B O     1 
ATOM   5387 C CB    . ALA B 2 34  ? 27.446  44.507  73.175  1.00 156.71 ?  330 ALA B CB    1 
ATOM   5388 N N     . ALA B 2 35  ? 24.663  44.002  71.273  1.00 155.96 ?  331 ALA B N     1 
ATOM   5389 C CA    . ALA B 2 35  ? 23.523  43.218  70.824  1.00 153.31 ?  331 ALA B CA    1 
ATOM   5390 C C     . ALA B 2 35  ? 23.672  42.831  69.356  1.00 150.40 ?  331 ALA B C     1 
ATOM   5391 O O     . ALA B 2 35  ? 23.855  41.651  69.028  1.00 145.69 ?  331 ALA B O     1 
ATOM   5392 C CB    . ALA B 2 35  ? 22.235  44.016  71.030  1.00 149.31 ?  331 ALA B CB    1 
ATOM   5393 N N     . THR B 2 36  ? 23.596  43.823  68.463  1.00 150.46 ?  332 THR B N     1 
ATOM   5394 C CA    . THR B 2 36  ? 23.764  43.581  67.033  1.00 146.73 ?  332 THR B CA    1 
ATOM   5395 C C     . THR B 2 36  ? 25.175  43.109  66.688  1.00 145.81 ?  332 THR B C     1 
ATOM   5396 O O     . THR B 2 36  ? 25.422  42.716  65.546  1.00 148.23 ?  332 THR B O     1 
ATOM   5397 C CB    . THR B 2 36  ? 23.379  44.852  66.265  1.00 146.61 ?  332 THR B CB    1 
ATOM   5398 O OG1   . THR B 2 36  ? 22.027  45.183  66.591  1.00 148.61 ?  332 THR B OG1   1 
ATOM   5399 C CG2   . THR B 2 36  ? 23.443  44.659  64.748  1.00 151.62 ?  332 THR B CG2   1 
ATOM   5400 N N     . THR B 2 37  ? 26.100  43.113  67.646  1.00 150.35 ?  333 THR B N     1 
ATOM   5401 C CA    . THR B 2 37  ? 27.336  42.348  67.501  1.00 150.47 ?  333 THR B CA    1 
ATOM   5402 C C     . THR B 2 37  ? 27.067  40.848  67.498  1.00 150.70 ?  333 THR B C     1 
ATOM   5403 O O     . THR B 2 37  ? 27.240  40.185  66.470  1.00 153.32 ?  333 THR B O     1 
ATOM   5404 C CB    . THR B 2 37  ? 28.335  42.691  68.614  1.00 153.75 ?  333 THR B CB    1 
ATOM   5405 O OG1   . THR B 2 37  ? 28.799  44.036  68.438  1.00 161.00 ?  333 THR B OG1   1 
ATOM   5406 C CG2   . THR B 2 37  ? 29.516  41.703  68.640  1.00 146.98 ?  333 THR B CG2   1 
ATOM   5407 N N     . VAL B 2 38  ? 26.627  40.295  68.631  1.00 146.14 ?  334 VAL B N     1 
ATOM   5408 C CA    . VAL B 2 38  ? 26.580  38.842  68.754  1.00 139.73 ?  334 VAL B CA    1 
ATOM   5409 C C     . VAL B 2 38  ? 25.393  38.232  68.018  1.00 134.69 ?  334 VAL B C     1 
ATOM   5410 O O     . VAL B 2 38  ? 25.278  37.001  67.965  1.00 133.72 ?  334 VAL B O     1 
ATOM   5411 C CB    . VAL B 2 38  ? 26.653  38.543  70.264  1.00 143.20 ?  334 VAL B CB    1 
ATOM   5412 C CG1   . VAL B 2 38  ? 26.733  37.042  70.541  1.00 143.20 ?  334 VAL B CG1   1 
ATOM   5413 C CG2   . VAL B 2 38  ? 27.830  39.292  70.876  1.00 143.43 ?  334 VAL B CG2   1 
ATOM   5414 N N     . LEU B 2 39  ? 24.521  39.042  67.408  1.00 131.39 ?  335 LEU B N     1 
ATOM   5415 C CA    . LEU B 2 39  ? 23.534  38.492  66.480  1.00 133.92 ?  335 LEU B CA    1 
ATOM   5416 C C     . LEU B 2 39  ? 23.981  38.514  65.016  1.00 141.92 ?  335 LEU B C     1 
ATOM   5417 O O     . LEU B 2 39  ? 23.360  37.839  64.182  1.00 140.35 ?  335 LEU B O     1 
ATOM   5418 C CB    . LEU B 2 39  ? 22.186  39.210  66.608  1.00 131.52 ?  335 LEU B CB    1 
ATOM   5419 C CG    . LEU B 2 39  ? 21.435  39.056  67.927  1.00 122.22 ?  335 LEU B CG    1 
ATOM   5420 C CD1   . LEU B 2 39  ? 20.005  39.576  67.810  1.00 117.28 ?  335 LEU B CD1   1 
ATOM   5421 C CD2   . LEU B 2 39  ? 21.433  37.600  68.335  1.00 117.89 ?  335 LEU B CD2   1 
ATOM   5422 N N     . ARG B 2 40  ? 25.024  39.273  64.675  1.00 143.82 ?  336 ARG B N     1 
ATOM   5423 C CA    . ARG B 2 40  ? 25.687  39.061  63.393  1.00 140.43 ?  336 ARG B CA    1 
ATOM   5424 C C     . ARG B 2 40  ? 26.693  37.921  63.495  1.00 140.73 ?  336 ARG B C     1 
ATOM   5425 O O     . ARG B 2 40  ? 26.835  37.129  62.559  1.00 144.01 ?  336 ARG B O     1 
ATOM   5426 C CB    . ARG B 2 40  ? 26.382  40.339  62.931  1.00 145.04 ?  336 ARG B CB    1 
ATOM   5427 C CG    . ARG B 2 40  ? 25.480  41.390  62.301  1.00 148.55 ?  336 ARG B CG    1 
ATOM   5428 C CD    . ARG B 2 40  ? 26.303  42.276  61.377  1.00 156.33 ?  336 ARG B CD    1 
ATOM   5429 N NE    . ARG B 2 40  ? 25.515  43.350  60.787  1.00 163.15 ?  336 ARG B NE    1 
ATOM   5430 C CZ    . ARG B 2 40  ? 25.593  44.617  61.182  1.00 167.06 ?  336 ARG B CZ    1 
ATOM   5431 N NH1   . ARG B 2 40  ? 26.417  44.957  62.166  1.00 159.57 ?  336 ARG B NH1   1 
ATOM   5432 N NH2   . ARG B 2 40  ? 24.848  45.546  60.598  1.00 175.59 ?  336 ARG B NH2   1 
ATOM   5433 N N     . GLN B 2 41  ? 27.379  37.815  64.641  1.00 140.01 ?  337 GLN B N     1 
ATOM   5434 C CA    . GLN B 2 41  ? 28.262  36.685  64.938  1.00 143.59 ?  337 GLN B CA    1 
ATOM   5435 C C     . GLN B 2 41  ? 27.626  35.330  64.693  1.00 141.12 ?  337 GLN B C     1 
ATOM   5436 O O     . GLN B 2 41  ? 28.336  34.319  64.645  1.00 137.17 ?  337 GLN B O     1 
ATOM   5437 C CB    . GLN B 2 41  ? 28.718  36.710  66.405  1.00 152.76 ?  337 GLN B CB    1 
ATOM   5438 C CG    . GLN B 2 41  ? 29.461  37.948  66.801  1.00 158.27 ?  337 GLN B CG    1 
ATOM   5439 C CD    . GLN B 2 41  ? 30.700  38.101  65.952  1.00 166.71 ?  337 GLN B CD    1 
ATOM   5440 O OE1   . GLN B 2 41  ? 30.790  39.018  65.129  1.00 170.04 ?  337 GLN B OE1   1 
ATOM   5441 N NE2   . GLN B 2 41  ? 31.648  37.174  66.110  1.00 162.64 ?  337 GLN B NE2   1 
ATOM   5442 N N     . LEU B 2 42  ? 26.307  35.269  64.608  1.00 141.29 ?  338 LEU B N     1 
ATOM   5443 C CA    . LEU B 2 42  ? 25.659  34.007  64.324  1.00 138.68 ?  338 LEU B CA    1 
ATOM   5444 C C     . LEU B 2 42  ? 25.195  33.921  62.884  1.00 140.33 ?  338 LEU B C     1 
ATOM   5445 O O     . LEU B 2 42  ? 25.202  32.832  62.308  1.00 141.71 ?  338 LEU B O     1 
ATOM   5446 C CB    . LEU B 2 42  ? 24.483  33.792  65.284  1.00 130.94 ?  338 LEU B CB    1 
ATOM   5447 C CG    . LEU B 2 42  ? 24.923  33.844  66.754  1.00 128.56 ?  338 LEU B CG    1 
ATOM   5448 C CD1   . LEU B 2 42  ? 23.854  33.305  67.675  1.00 126.00 ?  338 LEU B CD1   1 
ATOM   5449 C CD2   . LEU B 2 42  ? 26.241  33.111  66.976  1.00 129.36 ?  338 LEU B CD2   1 
ATOM   5450 N N     . ASP B 2 43  ? 24.849  35.049  62.270  1.00 138.07 ?  339 ASP B N     1 
ATOM   5451 C CA    . ASP B 2 43  ? 24.340  34.986  60.909  1.00 140.86 ?  339 ASP B CA    1 
ATOM   5452 C C     . ASP B 2 43  ? 25.443  34.663  59.909  1.00 142.26 ?  339 ASP B C     1 
ATOM   5453 O O     . ASP B 2 43  ? 25.163  34.084  58.849  1.00 142.55 ?  339 ASP B O     1 
ATOM   5454 C CB    . ASP B 2 43  ? 23.643  36.296  60.562  1.00 143.89 ?  339 ASP B CB    1 
ATOM   5455 C CG    . ASP B 2 43  ? 22.277  36.393  61.199  1.00 140.69 ?  339 ASP B CG    1 
ATOM   5456 O OD1   . ASP B 2 43  ? 21.895  35.424  61.883  1.00 136.94 ?  339 ASP B OD1   1 
ATOM   5457 O OD2   . ASP B 2 43  ? 21.584  37.414  60.999  1.00 142.04 ?  339 ASP B OD2   1 
ATOM   5458 N N     . MET B 2 44  ? 26.692  35.021  60.221  1.00 141.70 ?  340 MET B N     1 
ATOM   5459 C CA    . MET B 2 44  ? 27.804  34.590  59.389  1.00 144.43 ?  340 MET B CA    1 
ATOM   5460 C C     . MET B 2 44  ? 28.442  33.303  59.903  1.00 143.48 ?  340 MET B C     1 
ATOM   5461 O O     . MET B 2 44  ? 29.145  32.625  59.154  1.00 149.66 ?  340 MET B O     1 
ATOM   5462 C CB    . MET B 2 44  ? 28.854  35.710  59.236  1.00 146.53 ?  340 MET B CB    1 
ATOM   5463 C CG    . MET B 2 44  ? 28.414  36.936  58.371  1.00 151.55 ?  340 MET B CG    1 
ATOM   5464 S SD    . MET B 2 44  ? 29.714  38.166  58.037  1.00 177.59 ?  340 MET B SD    1 
ATOM   5465 C CE    . MET B 2 44  ? 30.885  37.207  57.062  1.00 159.71 ?  340 MET B CE    1 
ATOM   5466 N N     . GLU B 2 45  ? 28.179  32.910  61.137  1.00 140.48 ?  341 GLU B N     1 
ATOM   5467 C CA    . GLU B 2 45  ? 28.510  31.560  61.588  1.00 143.97 ?  341 GLU B CA    1 
ATOM   5468 C C     . GLU B 2 45  ? 27.433  30.544  61.208  1.00 137.48 ?  341 GLU B C     1 
ATOM   5469 O O     . GLU B 2 45  ? 27.607  29.340  61.438  1.00 135.10 ?  341 GLU B O     1 
ATOM   5470 C CB    . GLU B 2 45  ? 28.743  31.557  63.112  1.00 147.25 ?  341 GLU B CB    1 
ATOM   5471 C CG    . GLU B 2 45  ? 29.119  30.228  63.809  1.00 145.66 ?  341 GLU B CG    1 
ATOM   5472 C CD    . GLU B 2 45  ? 30.462  29.695  63.432  1.00 149.92 ?  341 GLU B CD    1 
ATOM   5473 O OE1   . GLU B 2 45  ? 31.308  30.531  63.038  1.00 151.07 ?  341 GLU B OE1   1 
ATOM   5474 O OE2   . GLU B 2 45  ? 30.699  28.462  63.619  1.00 148.63 ?  341 GLU B OE2   1 
ATOM   5475 N N     . LEU B 2 46  ? 26.303  31.012  60.680  1.00 135.48 ?  342 LEU B N     1 
ATOM   5476 C CA    . LEU B 2 46  ? 25.226  30.148  60.216  1.00 133.21 ?  342 LEU B CA    1 
ATOM   5477 C C     . LEU B 2 46  ? 25.300  29.911  58.722  1.00 135.92 ?  342 LEU B C     1 
ATOM   5478 O O     . LEU B 2 46  ? 24.830  28.875  58.242  1.00 138.57 ?  342 LEU B O     1 
ATOM   5479 C CB    . LEU B 2 46  ? 23.853  30.760  60.541  1.00 134.84 ?  342 LEU B CB    1 
ATOM   5480 C CG    . LEU B 2 46  ? 22.512  30.091  60.195  1.00 134.88 ?  342 LEU B CG    1 
ATOM   5481 C CD1   . LEU B 2 46  ? 22.205  28.892  61.105  1.00 131.02 ?  342 LEU B CD1   1 
ATOM   5482 C CD2   . LEU B 2 46  ? 21.387  31.115  60.207  1.00 137.68 ?  342 LEU B CD2   1 
ATOM   5483 N N     . VAL B 2 47  ? 25.849  30.870  57.978  1.00 134.99 ?  343 VAL B N     1 
ATOM   5484 C CA    . VAL B 2 47  ? 26.107  30.632  56.570  1.00 132.57 ?  343 VAL B CA    1 
ATOM   5485 C C     . VAL B 2 47  ? 27.426  29.904  56.394  1.00 131.49 ?  343 VAL B C     1 
ATOM   5486 O O     . VAL B 2 47  ? 27.560  29.078  55.490  1.00 136.03 ?  343 VAL B O     1 
ATOM   5487 C CB    . VAL B 2 47  ? 26.067  31.959  55.799  1.00 130.58 ?  343 VAL B CB    1 
ATOM   5488 C CG1   . VAL B 2 47  ? 26.461  31.763  54.325  1.00 131.21 ?  343 VAL B CG1   1 
ATOM   5489 C CG2   . VAL B 2 47  ? 24.676  32.558  55.908  1.00 129.90 ?  343 VAL B CG2   1 
ATOM   5490 N N     . SER B 2 48  ? 28.400  30.166  57.264  1.00 131.51 ?  344 SER B N     1 
ATOM   5491 C CA    . SER B 2 48  ? 29.703  29.513  57.152  1.00 135.27 ?  344 SER B CA    1 
ATOM   5492 C C     . SER B 2 48  ? 29.583  27.988  57.179  1.00 134.70 ?  344 SER B C     1 
ATOM   5493 O O     . SER B 2 48  ? 30.294  27.284  56.449  1.00 135.55 ?  344 SER B O     1 
ATOM   5494 C CB    . SER B 2 48  ? 30.614  29.997  58.278  1.00 142.65 ?  344 SER B CB    1 
ATOM   5495 O OG    . SER B 2 48  ? 31.867  29.335  58.244  1.00 144.44 ?  344 SER B OG    1 
ATOM   5496 N N     . VAL B 2 49  ? 28.719  27.461  58.048  1.00 136.77 ?  345 VAL B N     1 
ATOM   5497 C CA    . VAL B 2 49  ? 28.389  26.040  58.011  1.00 132.72 ?  345 VAL B CA    1 
ATOM   5498 C C     . VAL B 2 49  ? 27.550  25.729  56.787  1.00 134.30 ?  345 VAL B C     1 
ATOM   5499 O O     . VAL B 2 49  ? 27.798  24.748  56.075  1.00 140.03 ?  345 VAL B O     1 
ATOM   5500 C CB    . VAL B 2 49  ? 27.660  25.622  59.303  1.00 131.03 ?  345 VAL B CB    1 
ATOM   5501 C CG1   . VAL B 2 49  ? 27.011  24.266  59.132  1.00 129.79 ?  345 VAL B CG1   1 
ATOM   5502 C CG2   . VAL B 2 49  ? 28.629  25.579  60.470  1.00 132.47 ?  345 VAL B CG2   1 
ATOM   5503 N N     . LYS B 2 50  ? 26.563  26.580  56.508  1.00 130.11 ?  346 LYS B N     1 
ATOM   5504 C CA    . LYS B 2 50  ? 25.537  26.239  55.536  1.00 132.43 ?  346 LYS B CA    1 
ATOM   5505 C C     . LYS B 2 50  ? 26.118  26.070  54.128  1.00 131.33 ?  346 LYS B C     1 
ATOM   5506 O O     . LYS B 2 50  ? 25.621  25.249  53.341  1.00 128.09 ?  346 LYS B O     1 
ATOM   5507 C CB    . LYS B 2 50  ? 24.447  27.309  55.598  1.00 132.56 ?  346 LYS B CB    1 
ATOM   5508 C CG    . LYS B 2 50  ? 23.085  26.816  55.210  1.00 136.97 ?  346 LYS B CG    1 
ATOM   5509 C CD    . LYS B 2 50  ? 21.978  27.746  55.680  1.00 134.06 ?  346 LYS B CD    1 
ATOM   5510 C CE    . LYS B 2 50  ? 20.627  27.077  55.442  1.00 137.36 ?  346 LYS B CE    1 
ATOM   5511 N NZ    . LYS B 2 50  ? 19.453  27.775  56.016  1.00 130.13 ?  346 LYS B NZ    1 
ATOM   5512 N N     . ARG B 2 51  ? 27.184  26.808  53.799  1.00 132.00 ?  347 ARG B N     1 
ATOM   5513 C CA    . ARG B 2 51  ? 27.890  26.536  52.552  1.00 135.72 ?  347 ARG B CA    1 
ATOM   5514 C C     . ARG B 2 51  ? 28.669  25.232  52.646  1.00 135.97 ?  347 ARG B C     1 
ATOM   5515 O O     . ARG B 2 51  ? 28.668  24.431  51.700  1.00 141.01 ?  347 ARG B O     1 
ATOM   5516 C CB    . ARG B 2 51  ? 28.824  27.694  52.179  1.00 135.34 ?  347 ARG B CB    1 
ATOM   5517 C CG    . ARG B 2 51  ? 30.119  27.825  52.997  1.00 130.92 ?  347 ARG B CG    1 
ATOM   5518 C CD    . ARG B 2 51  ? 30.976  28.964  52.447  1.00 135.47 ?  347 ARG B CD    1 
ATOM   5519 N NE    . ARG B 2 51  ? 30.358  30.266  52.694  1.00 138.77 ?  347 ARG B NE    1 
ATOM   5520 C CZ    . ARG B 2 51  ? 29.812  31.034  51.751  1.00 138.01 ?  347 ARG B CZ    1 
ATOM   5521 N NH1   . ARG B 2 51  ? 29.827  30.651  50.476  1.00 136.22 ?  347 ARG B NH1   1 
ATOM   5522 N NH2   . ARG B 2 51  ? 29.260  32.196  52.083  1.00 137.44 ?  347 ARG B NH2   1 
ATOM   5523 N N     . GLN B 2 52  ? 29.326  25.001  53.785  1.00 126.18 ?  348 GLN B N     1 
ATOM   5524 C CA    . GLN B 2 52  ? 30.125  23.803  53.976  1.00 126.73 ?  348 GLN B CA    1 
ATOM   5525 C C     . GLN B 2 52  ? 29.286  22.530  53.940  1.00 130.62 ?  348 GLN B C     1 
ATOM   5526 O O     . GLN B 2 52  ? 29.845  21.451  53.714  1.00 132.90 ?  348 GLN B O     1 
ATOM   5527 C CB    . GLN B 2 52  ? 30.858  23.904  55.299  1.00 134.10 ?  348 GLN B CB    1 
ATOM   5528 C CG    . GLN B 2 52  ? 31.662  22.692  55.678  1.00 140.54 ?  348 GLN B CG    1 
ATOM   5529 C CD    . GLN B 2 52  ? 32.197  22.805  57.097  1.00 152.70 ?  348 GLN B CD    1 
ATOM   5530 O OE1   . GLN B 2 52  ? 32.001  23.829  57.774  1.00 146.13 ?  348 GLN B OE1   1 
ATOM   5531 N NE2   . GLN B 2 52  ? 32.822  21.732  57.581  1.00 155.31 ?  348 GLN B NE2   1 
ATOM   5532 N N     . ILE B 2 53  ? 27.967  22.614  54.168  1.00 129.79 ?  349 ILE B N     1 
ATOM   5533 C CA    . ILE B 2 53  ? 27.097  21.477  53.846  1.00 130.02 ?  349 ILE B CA    1 
ATOM   5534 C C     . ILE B 2 53  ? 27.128  21.197  52.353  1.00 135.95 ?  349 ILE B C     1 
ATOM   5535 O O     . ILE B 2 53  ? 27.564  20.124  51.923  1.00 140.75 ?  349 ILE B O     1 
ATOM   5536 C CB    . ILE B 2 53  ? 25.651  21.695  54.325  1.00 127.41 ?  349 ILE B CB    1 
ATOM   5537 C CG1   . ILE B 2 53  ? 25.575  21.666  55.844  1.00 126.58 ?  349 ILE B CG1   1 
ATOM   5538 C CG2   . ILE B 2 53  ? 24.727  20.644  53.698  1.00 126.62 ?  349 ILE B CG2   1 
ATOM   5539 C CD1   . ILE B 2 53  ? 24.243  22.012  56.414  1.00 131.19 ?  349 ILE B CD1   1 
ATOM   5540 N N     . GLN B 2 54  ? 26.662  22.161  51.541  1.00 133.87 ?  350 GLN B N     1 
ATOM   5541 C CA    . GLN B 2 54  ? 26.676  21.997  50.088  1.00 133.88 ?  350 GLN B CA    1 
ATOM   5542 C C     . GLN B 2 54  ? 28.052  21.699  49.525  1.00 131.61 ?  350 GLN B C     1 
ATOM   5543 O O     . GLN B 2 54  ? 28.165  21.236  48.385  1.00 129.78 ?  350 GLN B O     1 
ATOM   5544 C CB    . GLN B 2 54  ? 26.174  23.243  49.400  1.00 134.93 ?  350 GLN B CB    1 
ATOM   5545 C CG    . GLN B 2 54  ? 24.740  23.525  49.596  1.00 140.78 ?  350 GLN B CG    1 
ATOM   5546 C CD    . GLN B 2 54  ? 24.366  24.759  48.824  1.00 154.96 ?  350 GLN B CD    1 
ATOM   5547 O OE1   . GLN B 2 54  ? 25.213  25.634  48.603  1.00 157.56 ?  350 GLN B OE1   1 
ATOM   5548 N NE2   . GLN B 2 54  ? 23.126  24.815  48.340  1.00 154.85 ?  350 GLN B NE2   1 
ATOM   5549 N N     . ASN B 2 55  ? 29.096  21.962  50.283  1.00 130.05 ?  351 ASN B N     1 
ATOM   5550 C CA    . ASN B 2 55  ? 30.432  21.863  49.748  1.00 128.78 ?  351 ASN B CA    1 
ATOM   5551 C C     . ASN B 2 55  ? 31.063  20.506  50.087  1.00 128.80 ?  351 ASN B C     1 
ATOM   5552 O O     . ASN B 2 55  ? 32.089  20.140  49.510  1.00 127.48 ?  351 ASN B O     1 
ATOM   5553 C CB    . ASN B 2 55  ? 31.195  23.087  50.279  1.00 130.92 ?  351 ASN B CB    1 
ATOM   5554 C CG    . ASN B 2 55  ? 32.414  23.429  49.490  1.00 127.31 ?  351 ASN B CG    1 
ATOM   5555 O OD1   . ASN B 2 55  ? 32.797  22.718  48.583  1.00 131.25 ?  351 ASN B OD1   1 
ATOM   5556 N ND2   . ASN B 2 55  ? 32.948  24.615  49.741  1.00 123.63 ?  351 ASN B ND2   1 
ATOM   5557 N N     . ILE B 2 56  ? 30.424  19.733  50.973  1.00 133.23 ?  352 ILE B N     1 
ATOM   5558 C CA    . ILE B 2 56  ? 30.649  18.300  51.170  1.00 130.50 ?  352 ILE B CA    1 
ATOM   5559 C C     . ILE B 2 56  ? 29.461  17.527  50.621  1.00 130.59 ?  352 ILE B C     1 
ATOM   5560 O O     . ILE B 2 56  ? 29.591  16.363  50.235  1.00 135.20 ?  352 ILE B O     1 
ATOM   5561 C CB    . ILE B 2 56  ? 30.897  17.944  52.654  1.00 130.23 ?  352 ILE B CB    1 
ATOM   5562 C CG1   . ILE B 2 56  ? 32.202  18.563  53.140  1.00 139.84 ?  352 ILE B CG1   1 
ATOM   5563 C CG2   . ILE B 2 56  ? 30.887  16.447  52.917  1.00 131.02 ?  352 ILE B CG2   1 
ATOM   5564 C CD1   . ILE B 2 56  ? 32.406  18.462  54.619  1.00 141.78 ?  352 ILE B CD1   1 
ATOM   5565 N N     . LYS B 2 57  ? 28.290  18.162  50.584  1.00 131.12 ?  353 LYS B N     1 
ATOM   5566 C CA    . LYS B 2 57  ? 27.140  17.528  49.948  1.00 129.78 ?  353 LYS B CA    1 
ATOM   5567 C C     . LYS B 2 57  ? 27.397  17.304  48.467  1.00 133.04 ?  353 LYS B C     1 
ATOM   5568 O O     . LYS B 2 57  ? 26.868  16.353  47.879  1.00 135.75 ?  353 LYS B O     1 
ATOM   5569 C CB    . LYS B 2 57  ? 25.890  18.385  50.145  1.00 132.71 ?  353 LYS B CB    1 
ATOM   5570 C CG    . LYS B 2 57  ? 24.569  17.656  50.055  1.00 132.93 ?  353 LYS B CG    1 
ATOM   5571 C CD    . LYS B 2 57  ? 23.416  18.614  50.327  1.00 136.52 ?  353 LYS B CD    1 
ATOM   5572 C CE    . LYS B 2 57  ? 22.090  17.871  50.398  1.00 144.15 ?  353 LYS B CE    1 
ATOM   5573 N NZ    . LYS B 2 57  ? 20.939  18.764  50.728  1.00 146.49 ?  353 LYS B NZ    1 
ATOM   5574 N N     . GLN B 2 58  ? 28.218  18.158  47.854  1.00 132.98 ?  354 GLN B N     1 
ATOM   5575 C CA    . GLN B 2 58  ? 28.565  18.001  46.448  1.00 131.22 ?  354 GLN B CA    1 
ATOM   5576 C C     . GLN B 2 58  ? 29.732  17.046  46.250  1.00 129.41 ?  354 GLN B C     1 
ATOM   5577 O O     . GLN B 2 58  ? 29.734  16.264  45.297  1.00 133.59 ?  354 GLN B O     1 
ATOM   5578 C CB    . GLN B 2 58  ? 28.897  19.359  45.835  1.00 132.19 ?  354 GLN B CB    1 
ATOM   5579 C CG    . GLN B 2 58  ? 28.952  19.332  44.323  1.00 137.01 ?  354 GLN B CG    1 
ATOM   5580 C CD    . GLN B 2 58  ? 28.425  20.612  43.696  1.00 139.34 ?  354 GLN B CD    1 
ATOM   5581 O OE1   . GLN B 2 58  ? 28.530  21.694  44.283  1.00 132.89 ?  354 GLN B OE1   1 
ATOM   5582 N NE2   . GLN B 2 58  ? 27.870  20.497  42.486  1.00 143.61 ?  354 GLN B NE2   1 
ATOM   5583 N N     . THR B 2 59  ? 30.736  17.116  47.124  1.00 129.00 ?  355 THR B N     1 
ATOM   5584 C CA    . THR B 2 59  ? 31.783  16.097  47.144  1.00 130.69 ?  355 THR B CA    1 
ATOM   5585 C C     . THR B 2 59  ? 31.197  14.693  47.325  1.00 130.86 ?  355 THR B C     1 
ATOM   5586 O O     . THR B 2 59  ? 31.617  13.751  46.644  1.00 129.32 ?  355 THR B O     1 
ATOM   5587 C CB    . THR B 2 59  ? 32.799  16.438  48.243  1.00 133.97 ?  355 THR B CB    1 
ATOM   5588 O OG1   . THR B 2 59  ? 33.485  17.657  47.903  1.00 129.09 ?  355 THR B OG1   1 
ATOM   5589 C CG2   . THR B 2 59  ? 33.802  15.301  48.469  1.00 132.70 ?  355 THR B CG2   1 
ATOM   5590 N N     . ASN B 2 60  ? 30.215  14.536  48.227  1.00 132.78 ?  356 ASN B N     1 
ATOM   5591 C CA    . ASN B 2 60  ? 29.503  13.263  48.368  1.00 129.92 ?  356 ASN B CA    1 
ATOM   5592 C C     . ASN B 2 60  ? 28.625  12.927  47.173  1.00 131.28 ?  356 ASN B C     1 
ATOM   5593 O O     . ASN B 2 60  ? 28.309  11.753  46.977  1.00 132.14 ?  356 ASN B O     1 
ATOM   5594 C CB    . ASN B 2 60  ? 28.628  13.232  49.627  1.00 124.63 ?  356 ASN B CB    1 
ATOM   5595 C CG    . ASN B 2 60  ? 29.433  13.066  50.885  1.00 125.58 ?  356 ASN B CG    1 
ATOM   5596 O OD1   . ASN B 2 60  ? 30.624  13.362  50.918  1.00 127.57 ?  356 ASN B OD1   1 
ATOM   5597 N ND2   . ASN B 2 60  ? 28.794  12.564  51.923  1.00 122.15 ?  356 ASN B ND2   1 
ATOM   5598 N N     . SER B 2 61  ? 28.189  13.910  46.392  1.00 133.76 ?  357 SER B N     1 
ATOM   5599 C CA    . SER B 2 61  ? 27.496  13.566  45.155  1.00 137.67 ?  357 SER B CA    1 
ATOM   5600 C C     . SER B 2 61  ? 28.468  13.091  44.081  1.00 139.13 ?  357 SER B C     1 
ATOM   5601 O O     . SER B 2 61  ? 28.068  12.369  43.157  1.00 136.77 ?  357 SER B O     1 
ATOM   5602 C CB    . SER B 2 61  ? 26.695  14.761  44.636  1.00 142.93 ?  357 SER B CB    1 
ATOM   5603 O OG    . SER B 2 61  ? 26.219  14.501  43.323  1.00 144.26 ?  357 SER B OG    1 
ATOM   5604 N N     . ALA B 2 62  ? 29.735  13.504  44.180  1.00 139.51 ?  358 ALA B N     1 
ATOM   5605 C CA    . ALA B 2 62  ? 30.766  13.003  43.277  1.00 137.43 ?  358 ALA B CA    1 
ATOM   5606 C C     . ALA B 2 62  ? 31.135  11.567  43.619  1.00 136.32 ?  358 ALA B C     1 
ATOM   5607 O O     . ALA B 2 62  ? 31.040  10.672  42.769  1.00 138.32 ?  358 ALA B O     1 
ATOM   5608 C CB    . ALA B 2 62  ? 31.999  13.906  43.336  1.00 133.50 ?  358 ALA B CB    1 
ATOM   5609 N N     . LEU B 2 63  ? 31.411  11.296  44.891  1.00 133.02 ?  359 LEU B N     1 
ATOM   5610 C CA    . LEU B 2 63  ? 31.738  9.905   45.295  1.00 132.67 ?  359 LEU B CA    1 
ATOM   5611 C C     . LEU B 2 63  ? 30.563  8.999   44.948  1.00 135.60 ?  359 LEU B C     1 
ATOM   5612 O O     . LEU B 2 63  ? 30.795  7.900   44.491  1.00 138.53 ?  359 LEU B O     1 
ATOM   5613 C CB    . LEU B 2 63  ? 31.996  9.861   46.796  1.00 134.00 ?  359 LEU B CB    1 
ATOM   5614 C CG    . LEU B 2 63  ? 33.055  10.839  47.277  1.00 134.77 ?  359 LEU B CG    1 
ATOM   5615 C CD1   . LEU B 2 63  ? 33.952  10.184  48.311  1.00 125.68 ?  359 LEU B CD1   1 
ATOM   5616 C CD2   . LEU B 2 63  ? 33.860  11.345  46.096  1.00 130.06 ?  359 LEU B CD2   1 
ATOM   5617 N N     . LYS B 2 64  ? 29.343  9.497   45.061  1.00 137.18 ?  360 LYS B N     1 
ATOM   5618 C CA    . LYS B 2 64  ? 28.209  8.613   44.714  1.00 139.26 ?  360 LYS B CA    1 
ATOM   5619 C C     . LYS B 2 64  ? 28.281  8.263   43.228  1.00 141.52 ?  360 LYS B C     1 
ATOM   5620 O O     . LYS B 2 64  ? 28.131  7.087   42.898  1.00 141.44 ?  360 LYS B O     1 
ATOM   5621 C CB    . LYS B 2 64  ? 26.878  9.275   45.070  1.00 138.71 ?  360 LYS B CB    1 
ATOM   5622 C CG    . LYS B 2 64  ? 26.541  9.287   46.552  1.00 131.12 ?  360 LYS B CG    1 
ATOM   5623 C CD    . LYS B 2 64  ? 25.056  9.337   46.826  1.00 133.08 ?  360 LYS B CD    1 
ATOM   5624 C CE    . LYS B 2 64  ? 24.306  10.247  45.879  1.00 138.17 ?  360 LYS B CE    1 
ATOM   5625 N NZ    . LYS B 2 64  ? 22.860  9.928   45.831  1.00 135.22 ?  360 LYS B NZ    1 
ATOM   5626 N N     . GLU B 2 65  ? 28.607  9.231   42.373  1.00 142.52 ?  361 GLU B N     1 
ATOM   5627 C CA    . GLU B 2 65  ? 28.617  8.949   40.917  1.00 142.02 ?  361 GLU B CA    1 
ATOM   5628 C C     . GLU B 2 65  ? 29.639  7.860   40.625  1.00 141.35 ?  361 GLU B C     1 
ATOM   5629 O O     . GLU B 2 65  ? 29.293  6.907   39.937  1.00 144.47 ?  361 GLU B O     1 
ATOM   5630 C CB    . GLU B 2 65  ? 28.995  10.193  40.120  1.00 138.68 ?  361 GLU B CB    1 
ATOM   5631 C CG    . GLU B 2 65  ? 27.926  10.642  39.143  1.00 151.12 ?  361 GLU B CG    1 
ATOM   5632 C CD    . GLU B 2 65  ? 27.354  9.560   38.246  1.00 170.95 ?  361 GLU B CD    1 
ATOM   5633 O OE1   . GLU B 2 65  ? 27.072  8.470   38.760  1.00 170.51 ?  361 GLU B OE1   1 
ATOM   5634 O OE2   . GLU B 2 65  ? 27.180  9.818   37.037  1.00 175.12 ?  361 GLU B OE2   1 
ATOM   5635 N N     . LYS B 2 66  ? 30.813  7.935   41.242  1.00 138.14 ?  362 LYS B N     1 
ATOM   5636 C CA    . LYS B 2 66  ? 31.852  6.915   40.974  1.00 138.60 ?  362 LYS B CA    1 
ATOM   5637 C C     . LYS B 2 66  ? 31.330  5.538   41.379  1.00 138.35 ?  362 LYS B C     1 
ATOM   5638 O O     . LYS B 2 66  ? 31.566  4.598   40.630  1.00 138.61 ?  362 LYS B O     1 
ATOM   5639 C CB    . LYS B 2 66  ? 33.166  7.282   41.661  1.00 132.90 ?  362 LYS B CB    1 
ATOM   5640 C CG    . LYS B 2 66  ? 33.788  8.584   41.188  1.00 123.65 ?  362 LYS B CG    1 
ATOM   5641 C CD    . LYS B 2 66  ? 35.286  8.597   41.352  1.00 130.99 ?  362 LYS B CD    1 
ATOM   5642 C CE    . LYS B 2 66  ? 35.795  9.715   42.235  1.00 137.29 ?  362 LYS B CE    1 
ATOM   5643 N NZ    . LYS B 2 66  ? 37.211  9.506   42.617  1.00 134.75 ?  362 LYS B NZ    1 
ATOM   5644 N N     . LEU B 2 67  ? 30.608  5.414   42.491  1.00 134.58 ?  363 LEU B N     1 
ATOM   5645 C CA    . LEU B 2 67  ? 30.061  4.084   42.853  1.00 136.75 ?  363 LEU B CA    1 
ATOM   5646 C C     . LEU B 2 67  ? 28.763  3.874   42.077  1.00 145.59 ?  363 LEU B C     1 
ATOM   5647 O O     . LEU B 2 67  ? 27.705  3.970   42.692  1.00 147.11 ?  363 LEU B O     1 
ATOM   5648 C CB    . LEU B 2 67  ? 29.757  4.063   44.350  1.00 126.41 ?  363 LEU B CB    1 
ATOM   5649 C CG    . LEU B 2 67  ? 30.971  4.196   45.259  1.00 125.26 ?  363 LEU B CG    1 
ATOM   5650 C CD1   . LEU B 2 67  ? 31.104  2.992   46.166  1.00 127.83 ?  363 LEU B CD1   1 
ATOM   5651 C CD2   . LEU B 2 67  ? 32.228  4.371   44.438  1.00 124.89 ?  363 LEU B CD2   1 
ATOM   5652 N N     . ASP B 2 68  ? 28.839  3.578   40.782  1.00 145.03 ?  364 ASP B N     1 
ATOM   5653 C CA    . ASP B 2 68  ? 27.585  3.397   40.022  1.00 145.68 ?  364 ASP B CA    1 
ATOM   5654 C C     . ASP B 2 68  ? 27.464  1.931   39.643  1.00 149.20 ?  364 ASP B C     1 
ATOM   5655 O O     . ASP B 2 68  ? 28.373  1.418   38.992  1.00 150.47 ?  364 ASP B O     1 
ATOM   5656 C CB    . ASP B 2 68  ? 27.576  4.218   38.740  1.00 147.43 ?  364 ASP B CB    1 
ATOM   5657 C CG    . ASP B 2 68  ? 26.748  3.533   37.672  1.00 154.50 ?  364 ASP B CG    1 
ATOM   5658 O OD1   . ASP B 2 68  ? 25.513  3.574   37.783  1.00 157.49 ?  364 ASP B OD1   1 
ATOM   5659 O OD2   . ASP B 2 68  ? 27.347  2.935   36.767  1.00 150.89 ?  364 ASP B OD2   1 
ATOM   5660 N N     . GLY B 2 69  ? 26.361  1.306   40.046  1.00 148.05 ?  365 GLY B N     1 
ATOM   5661 C CA    . GLY B 2 69  ? 26.088  -0.113  39.760  1.00 146.39 ?  365 GLY B CA    1 
ATOM   5662 C C     . GLY B 2 69  ? 26.605  -1.017  40.858  1.00 145.63 ?  365 GLY B C     1 
ATOM   5663 O O     . GLY B 2 69  ? 26.255  -2.194  40.855  1.00 145.03 ?  365 GLY B O     1 
ATOM   5664 N N     . GLY B 2 70  ? 27.369  -0.472  41.797  1.00 139.30 ?  366 GLY B N     1 
ATOM   5665 C CA    . GLY B 2 70  ? 27.899  -1.277  42.907  1.00 141.27 ?  366 GLY B CA    1 
ATOM   5666 C C     . GLY B 2 70  ? 28.891  -2.319  42.439  1.00 138.71 ?  366 GLY B C     1 
ATOM   5667 O O     . GLY B 2 70  ? 29.588  -2.063  41.461  1.00 138.28 ?  366 GLY B O     1 
ATOM   5668 N N     . ILE B 2 71  ? 28.944  -3.440  43.157  1.00 135.46 ?  367 ILE B N     1 
ATOM   5669 C CA    . ILE B 2 71  ? 29.850  -4.555  42.880  1.00 135.66 ?  367 ILE B CA    1 
ATOM   5670 C C     . ILE B 2 71  ? 29.064  -5.746  42.337  1.00 143.24 ?  367 ILE B C     1 
ATOM   5671 O O     . ILE B 2 71  ? 29.429  -6.908  42.568  1.00 146.73 ?  367 ILE B O     1 
ATOM   5672 C CB    . ILE B 2 71  ? 30.677  -4.978  44.116  1.00 131.36 ?  367 ILE B CB    1 
ATOM   5673 C CG1   . ILE B 2 71  ? 29.762  -5.474  45.247  1.00 133.36 ?  367 ILE B CG1   1 
ATOM   5674 C CG2   . ILE B 2 71  ? 31.633  -3.858  44.550  1.00 126.32 ?  367 ILE B CG2   1 
ATOM   5675 C CD1   . ILE B 2 71  ? 30.483  -5.917  46.505  1.00 132.31 ?  367 ILE B CD1   1 
ATOM   5676 N N     . GLU B 2 72  ? 27.993  -5.479  41.594  1.00 144.33 ?  368 GLU B N     1 
ATOM   5677 C CA    . GLU B 2 72  ? 27.250  -6.589  40.998  1.00 145.21 ?  368 GLU B CA    1 
ATOM   5678 C C     . GLU B 2 72  ? 27.996  -7.292  39.863  1.00 138.23 ?  368 GLU B C     1 
ATOM   5679 O O     . GLU B 2 72  ? 27.826  -8.508  39.701  1.00 139.48 ?  368 GLU B O     1 
ATOM   5680 C CB    . GLU B 2 72  ? 25.867  -6.117  40.540  1.00 144.50 ?  368 GLU B CB    1 
ATOM   5681 C CG    . GLU B 2 72  ? 25.087  -5.443  41.677  1.00 148.41 ?  368 GLU B CG    1 
ATOM   5682 C CD    . GLU B 2 72  ? 25.103  -6.265  42.987  1.00 149.47 ?  368 GLU B CD    1 
ATOM   5683 O OE1   . GLU B 2 72  ? 24.859  -7.502  42.971  1.00 143.49 ?  368 GLU B OE1   1 
ATOM   5684 O OE2   . GLU B 2 72  ? 25.423  -5.670  44.040  1.00 148.44 ?  368 GLU B OE2   1 
ATOM   5685 N N     . PRO B 2 73  ? 28.836  -6.611  39.072  1.00 133.83 ?  369 PRO B N     1 
ATOM   5686 C CA    . PRO B 2 73  ? 29.673  -7.348  38.113  1.00 135.54 ?  369 PRO B CA    1 
ATOM   5687 C C     . PRO B 2 73  ? 30.671  -8.319  38.747  1.00 138.19 ?  369 PRO B C     1 
ATOM   5688 O O     . PRO B 2 73  ? 31.171  -9.208  38.041  1.00 140.55 ?  369 PRO B O     1 
ATOM   5689 C CB    . PRO B 2 73  ? 30.396  -6.231  37.346  1.00 130.86 ?  369 PRO B CB    1 
ATOM   5690 C CG    . PRO B 2 73  ? 29.578  -5.022  37.565  1.00 130.56 ?  369 PRO B CG    1 
ATOM   5691 C CD    . PRO B 2 73  ? 29.027  -5.156  38.924  1.00 134.57 ?  369 PRO B CD    1 
ATOM   5692 N N     . TYR B 2 74  ? 30.949  -8.216  40.045  1.00 135.19 ?  370 TYR B N     1 
ATOM   5693 C CA    . TYR B 2 74  ? 32.154  -8.809  40.614  1.00 134.04 ?  370 TYR B CA    1 
ATOM   5694 C C     . TYR B 2 74  ? 31.851  -9.891  41.651  1.00 137.04 ?  370 TYR B C     1 
ATOM   5695 O O     . TYR B 2 74  ? 32.724  -10.230 42.462  1.00 134.53 ?  370 TYR B O     1 
ATOM   5696 C CB    . TYR B 2 74  ? 33.017  -7.705  41.226  1.00 132.77 ?  370 TYR B CB    1 
ATOM   5697 C CG    . TYR B 2 74  ? 33.363  -6.529  40.301  1.00 135.18 ?  370 TYR B CG    1 
ATOM   5698 C CD1   . TYR B 2 74  ? 34.635  -6.387  39.746  1.00 133.43 ?  370 TYR B CD1   1 
ATOM   5699 C CD2   . TYR B 2 74  ? 32.407  -5.573  39.967  1.00 134.88 ?  370 TYR B CD2   1 
ATOM   5700 C CE1   . TYR B 2 74  ? 34.946  -5.303  38.920  1.00 128.40 ?  370 TYR B CE1   1 
ATOM   5701 C CE2   . TYR B 2 74  ? 32.708  -4.505  39.134  1.00 130.80 ?  370 TYR B CE2   1 
ATOM   5702 C CZ    . TYR B 2 74  ? 33.974  -4.374  38.617  1.00 128.05 ?  370 TYR B CZ    1 
ATOM   5703 O OH    . TYR B 2 74  ? 34.256  -3.304  37.801  1.00 131.16 ?  370 TYR B OH    1 
ATOM   5704 N N     . ARG B 2 75  ? 30.628  -10.408 41.628  1.00 139.65 ?  371 ARG B N     1 
ATOM   5705 C CA    . ARG B 2 75  ? 30.242  -11.431 42.625  1.00 141.34 ?  371 ARG B CA    1 
ATOM   5706 C C     . ARG B 2 75  ? 30.377  -12.816 42.014  1.00 143.58 ?  371 ARG B C     1 
ATOM   5707 O O     . ARG B 2 75  ? 30.249  -12.931 40.800  1.00 147.78 ?  371 ARG B O     1 
ATOM   5708 C CB    . ARG B 2 75  ? 28.770  -11.265 43.002  1.00 142.63 ?  371 ARG B CB    1 
ATOM   5709 C CG    . ARG B 2 75  ? 28.475  -10.039 43.850  1.00 143.92 ?  371 ARG B CG    1 
ATOM   5710 C CD    . ARG B 2 75  ? 27.653  -10.410 45.062  1.00 143.62 ?  371 ARG B CD    1 
ATOM   5711 N NE    . ARG B 2 75  ? 27.436  -9.283  45.949  1.00 144.10 ?  371 ARG B NE    1 
ATOM   5712 C CZ    . ARG B 2 75  ? 26.659  -8.247  45.678  1.00 145.12 ?  371 ARG B CZ    1 
ATOM   5713 N NH1   . ARG B 2 75  ? 26.013  -8.172  44.529  1.00 140.91 ?  371 ARG B NH1   1 
ATOM   5714 N NH2   . ARG B 2 75  ? 26.526  -7.285  46.567  1.00 146.85 ?  371 ARG B NH2   1 
ATOM   5715 N N     . LEU B 2 76  ? 30.621  -13.816 42.852  1.00 143.06 ?  372 LEU B N     1 
ATOM   5716 C CA    . LEU B 2 76  ? 30.684  -15.218 42.384  1.00 148.85 ?  372 LEU B CA    1 
ATOM   5717 C C     . LEU B 2 76  ? 29.678  -15.978 43.228  1.00 152.37 ?  372 LEU B C     1 
ATOM   5718 O O     . LEU B 2 76  ? 29.564  -15.677 44.410  1.00 152.48 ?  372 LEU B O     1 
ATOM   5719 C CB    . LEU B 2 76  ? 32.081  -15.779 42.613  1.00 146.99 ?  372 LEU B CB    1 
ATOM   5720 C CG    . LEU B 2 76  ? 33.212  -14.783 42.407  1.00 143.33 ?  372 LEU B CG    1 
ATOM   5721 C CD1   . LEU B 2 76  ? 34.367  -15.117 43.328  1.00 136.32 ?  372 LEU B CD1   1 
ATOM   5722 C CD2   . LEU B 2 76  ? 33.675  -14.801 40.966  1.00 140.92 ?  372 LEU B CD2   1 
ATOM   5723 N N     . PRO B 2 77  ? 28.976  -16.979 42.681  1.00 152.69 ?  373 PRO B N     1 
ATOM   5724 C CA    . PRO B 2 77  ? 27.956  -17.691 43.438  1.00 158.32 ?  373 PRO B CA    1 
ATOM   5725 C C     . PRO B 2 77  ? 28.514  -18.453 44.647  1.00 160.48 ?  373 PRO B C     1 
ATOM   5726 O O     . PRO B 2 77  ? 29.653  -18.858 44.635  1.00 153.88 ?  373 PRO B O     1 
ATOM   5727 C CB    . PRO B 2 77  ? 27.342  -18.616 42.384  1.00 153.63 ?  373 PRO B CB    1 
ATOM   5728 C CG    . PRO B 2 77  ? 27.679  -17.939 41.080  1.00 146.64 ?  373 PRO B CG    1 
ATOM   5729 C CD    . PRO B 2 77  ? 29.079  -17.419 41.302  1.00 142.46 ?  373 PRO B CD    1 
ATOM   5730 N N     . GLU B 2 78  ? 27.675  -18.606 45.672  1.00 165.54 ?  374 GLU B N     1 
ATOM   5731 C CA    . GLU B 2 78  ? 28.082  -19.269 46.938  1.00 167.87 ?  374 GLU B CA    1 
ATOM   5732 C C     . GLU B 2 78  ? 28.498  -20.714 46.669  1.00 169.49 ?  374 GLU B C     1 
ATOM   5733 O O     . GLU B 2 78  ? 27.747  -21.443 46.006  1.00 167.53 ?  374 GLU B O     1 
ATOM   5734 C CB    . GLU B 2 78  ? 26.924  -19.242 47.933  1.00 166.56 ?  374 GLU B CB    1 
ATOM   5735 C CG    . GLU B 2 78  ? 25.587  -18.900 47.300  1.00 170.93 ?  374 GLU B CG    1 
ATOM   5736 C CD    . GLU B 2 78  ? 24.438  -18.820 48.291  1.00 174.19 ?  374 GLU B CD    1 
ATOM   5737 O OE1   . GLU B 2 78  ? 24.602  -18.160 49.336  1.00 172.98 ?  374 GLU B OE1   1 
ATOM   5738 O OE2   . GLU B 2 78  ? 23.386  -19.423 48.019  1.00 174.41 ?  374 GLU B OE2   1 
ATOM   5739 N N     . VAL B 2 79  ? 29.609  -21.125 47.273  1.00 169.08 ?  375 VAL B N     1 
ATOM   5740 C CA    . VAL B 2 79  ? 30.142  -22.501 47.086  1.00 169.64 ?  375 VAL B CA    1 
ATOM   5741 C C     . VAL B 2 79  ? 29.371  -23.419 48.032  1.00 171.51 ?  375 VAL B C     1 
ATOM   5742 O O     . VAL B 2 79  ? 29.883  -23.718 49.121  1.00 171.42 ?  375 VAL B O     1 
ATOM   5743 C CB    . VAL B 2 79  ? 31.647  -22.535 47.399  1.00 163.45 ?  375 VAL B CB    1 
ATOM   5744 C CG1   . VAL B 2 79  ? 32.138  -23.948 47.649  1.00 159.12 ?  375 VAL B CG1   1 
ATOM   5745 C CG2   . VAL B 2 79  ? 32.462  -21.867 46.308  1.00 151.69 ?  375 VAL B CG2   1 
ATOM   5746 N N     . ILE B 2 80  ? 28.173  -23.831 47.624  1.00 169.97 ?  376 ILE B N     1 
ATOM   5747 C CA    . ILE B 2 80  ? 27.340  -24.721 48.478  1.00 168.45 ?  376 ILE B CA    1 
ATOM   5748 C C     . ILE B 2 80  ? 27.912  -26.139 48.418  1.00 167.83 ?  376 ILE B C     1 
ATOM   5749 O O     . ILE B 2 80  ? 27.947  -26.713 47.328  1.00 170.78 ?  376 ILE B O     1 
ATOM   5750 C CB    . ILE B 2 80  ? 25.878  -24.673 48.007  1.00 163.18 ?  376 ILE B CB    1 
ATOM   5751 C CG1   . ILE B 2 80  ? 25.382  -23.232 47.898  1.00 158.35 ?  376 ILE B CG1   1 
ATOM   5752 C CG2   . ILE B 2 80  ? 24.986  -25.495 48.916  1.00 157.05 ?  376 ILE B CG2   1 
ATOM   5753 C CD1   . ILE B 2 80  ? 24.241  -22.926 48.830  1.00 153.68 ?  376 ILE B CD1   1 
ATOM   5754 N N     . GLN B 2 81  ? 28.363  -26.658 49.557  1.00 163.77 ?  377 GLN B N     1 
ATOM   5755 C CA    . GLN B 2 81  ? 28.899  -28.014 49.652  1.00 167.08 ?  377 GLN B CA    1 
ATOM   5756 C C     . GLN B 2 81  ? 28.836  -28.505 51.090  1.00 164.75 ?  377 GLN B C     1 
ATOM   5757 O O     . GLN B 2 81  ? 29.399  -27.870 51.990  1.00 163.40 ?  377 GLN B O     1 
ATOM   5758 C CB    . GLN B 2 81  ? 30.335  -28.093 49.113  1.00 166.87 ?  377 GLN B CB    1 
ATOM   5759 C CG    . GLN B 2 81  ? 31.348  -27.162 49.766  1.00 161.04 ?  377 GLN B CG    1 
ATOM   5760 C CD    . GLN B 2 81  ? 32.779  -27.513 49.388  1.00 158.37 ?  377 GLN B CD    1 
ATOM   5761 O OE1   . GLN B 2 81  ? 33.095  -28.669 49.077  1.00 156.47 ?  377 GLN B OE1   1 
ATOM   5762 N NE2   . GLN B 2 81  ? 33.645  -26.504 49.372  1.00 155.23 ?  377 GLN B NE2   1 
ATOM   5763 N N     . LYS B 2 82  ? 28.158  -29.645 51.298  1.00 160.32 ?  378 LYS B N     1 
ATOM   5764 C CA    . LYS B 2 82  ? 28.124  -30.290 52.606  1.00 153.35 ?  378 LYS B CA    1 
ATOM   5765 C C     . LYS B 2 82  ? 29.550  -30.519 53.099  1.00 153.73 ?  378 LYS B C     1 
ATOM   5766 O O     . LYS B 2 82  ? 30.504  -30.516 52.310  1.00 154.90 ?  378 LYS B O     1 
ATOM   5767 C CB    . LYS B 2 82  ? 27.338  -31.606 52.566  1.00 148.38 ?  378 LYS B CB    1 
ATOM   5768 C CG    . LYS B 2 82  ? 25.824  -31.489 52.299  1.00 146.84 ?  378 LYS B CG    1 
ATOM   5769 C CD    . LYS B 2 82  ? 25.141  -32.853 52.546  1.00 153.45 ?  378 LYS B CD    1 
ATOM   5770 C CE    . LYS B 2 82  ? 23.629  -32.866 52.273  1.00 152.69 ?  378 LYS B CE    1 
ATOM   5771 N NZ    . LYS B 2 82  ? 23.015  -34.225 52.508  1.00 146.29 ?  378 LYS B NZ    1 
ATOM   5772 N N     . CYS B 2 83  ? 29.702  -30.721 54.398  1.00 152.29 ?  379 CYS B N     1 
ATOM   5773 C CA    . CYS B 2 83  ? 30.980  -30.547 55.078  1.00 156.99 ?  379 CYS B CA    1 
ATOM   5774 C C     . CYS B 2 83  ? 31.452  -31.917 55.576  1.00 156.11 ?  379 CYS B C     1 
ATOM   5775 O O     . CYS B 2 83  ? 30.926  -32.435 56.569  1.00 153.54 ?  379 CYS B O     1 
ATOM   5776 C CB    . CYS B 2 83  ? 30.800  -29.522 56.205  1.00 162.66 ?  379 CYS B CB    1 
ATOM   5777 S SG    . CYS B 2 83  ? 32.235  -28.968 57.180  1.00 162.82 ?  379 CYS B SG    1 
ATOM   5778 N N     . ASN B 2 84  ? 32.440  -32.500 54.877  1.00 158.63 ?  380 ASN B N     1 
ATOM   5779 C CA    . ASN B 2 84  ? 32.913  -33.871 55.071  1.00 157.37 ?  380 ASN B CA    1 
ATOM   5780 C C     . ASN B 2 84  ? 33.918  -33.964 56.230  1.00 155.25 ?  380 ASN B C     1 
ATOM   5781 O O     . ASN B 2 84  ? 34.366  -32.959 56.786  1.00 154.77 ?  380 ASN B O     1 
ATOM   5782 C CB    . ASN B 2 84  ? 33.536  -34.407 53.774  1.00 150.54 ?  380 ASN B CB    1 
ATOM   5783 C CG    . ASN B 2 84  ? 33.688  -35.918 53.780  1.00 152.80 ?  380 ASN B CG    1 
ATOM   5784 O OD1   . ASN B 2 84  ? 34.711  -36.447 54.219  1.00 153.13 ?  380 ASN B OD1   1 
ATOM   5785 N ND2   . ASN B 2 84  ? 32.664  -36.622 53.305  1.00 151.58 ?  380 ASN B ND2   1 
ATOM   5786 N N     . ALA B 2 85  ? 34.280  -35.197 56.589  1.00 152.77 ?  381 ALA B N     1 
ATOM   5787 C CA    . ALA B 2 85  ? 35.061  -35.467 57.793  1.00 148.10 ?  381 ALA B CA    1 
ATOM   5788 C C     . ALA B 2 85  ? 36.468  -35.985 57.531  1.00 153.39 ?  381 ALA B C     1 
ATOM   5789 O O     . ALA B 2 85  ? 37.380  -35.692 58.315  1.00 147.32 ?  381 ALA B O     1 
ATOM   5790 C CB    . ALA B 2 85  ? 34.318  -36.472 58.676  1.00 148.06 ?  381 ALA B CB    1 
ATOM   5791 N N     . ARG B 2 86  ? 36.668  -36.768 56.469  1.00 156.90 ?  382 ARG B N     1 
ATOM   5792 C CA    . ARG B 2 86  ? 37.988  -37.288 56.138  1.00 154.05 ?  382 ARG B CA    1 
ATOM   5793 C C     . ARG B 2 86  ? 38.792  -36.227 55.385  1.00 149.98 ?  382 ARG B C     1 
ATOM   5794 O O     . ARG B 2 86  ? 38.231  -35.372 54.685  1.00 144.59 ?  382 ARG B O     1 
ATOM   5795 C CB    . ARG B 2 86  ? 37.868  -38.572 55.306  1.00 155.45 ?  382 ARG B CB    1 
ATOM   5796 C CG    . ARG B 2 86  ? 37.193  -39.735 56.044  1.00 161.46 ?  382 ARG B CG    1 
ATOM   5797 C CD    . ARG B 2 86  ? 37.129  -41.002 55.187  1.00 167.89 ?  382 ARG B CD    1 
ATOM   5798 N NE    . ARG B 2 86  ? 36.696  -42.170 55.959  1.00 175.49 ?  382 ARG B NE    1 
ATOM   5799 C CZ    . ARG B 2 86  ? 37.508  -43.118 56.432  1.00 178.17 ?  382 ARG B CZ    1 
ATOM   5800 N NH1   . ARG B 2 86  ? 38.817  -43.048 56.229  1.00 177.76 ?  382 ARG B NH1   1 
ATOM   5801 N NH2   . ARG B 2 86  ? 37.011  -44.139 57.122  1.00 179.74 ?  382 ARG B NH2   1 
ATOM   5802 N N     . TRP B 2 87  ? 40.127  -36.288 55.539  1.00 148.63 ?  383 TRP B N     1 
ATOM   5803 C CA    . TRP B 2 87  ? 41.052  -35.283 54.993  1.00 143.66 ?  383 TRP B CA    1 
ATOM   5804 C C     . TRP B 2 87  ? 41.779  -35.786 53.745  1.00 143.09 ?  383 TRP B C     1 
ATOM   5805 O O     . TRP B 2 87  ? 42.821  -36.444 53.859  1.00 145.58 ?  383 TRP B O     1 
ATOM   5806 C CB    . TRP B 2 87  ? 42.078  -34.871 56.041  1.00 138.28 ?  383 TRP B CB    1 
ATOM   5807 C CG    . TRP B 2 87  ? 41.510  -33.967 57.023  1.00 143.89 ?  383 TRP B CG    1 
ATOM   5808 C CD1   . TRP B 2 87  ? 40.869  -34.312 58.172  1.00 153.64 ?  383 TRP B CD1   1 
ATOM   5809 C CD2   . TRP B 2 87  ? 41.457  -32.536 56.940  1.00 140.50 ?  383 TRP B CD2   1 
ATOM   5810 N NE1   . TRP B 2 87  ? 40.446  -33.177 58.830  1.00 156.59 ?  383 TRP B NE1   1 
ATOM   5811 C CE2   . TRP B 2 87  ? 40.794  -32.075 58.088  1.00 146.78 ?  383 TRP B CE2   1 
ATOM   5812 C CE3   . TRP B 2 87  ? 41.920  -31.600 56.015  1.00 135.40 ?  383 TRP B CE3   1 
ATOM   5813 C CZ2   . TRP B 2 87  ? 40.580  -30.717 58.332  1.00 140.51 ?  383 TRP B CZ2   1 
ATOM   5814 C CZ3   . TRP B 2 87  ? 41.707  -30.250 56.267  1.00 131.26 ?  383 TRP B CZ3   1 
ATOM   5815 C CH2   . TRP B 2 87  ? 41.044  -29.826 57.409  1.00 127.49 ?  383 TRP B CH2   1 
ATOM   5816 N N     . THR B 2 88  ? 41.263  -35.432 52.560  1.00 132.38 ?  384 THR B N     1 
ATOM   5817 C CA    . THR B 2 88  ? 41.970  -35.748 51.322  1.00 125.93 ?  384 THR B CA    1 
ATOM   5818 C C     . THR B 2 88  ? 43.340  -35.078 51.330  1.00 123.44 ?  384 THR B C     1 
ATOM   5819 O O     . THR B 2 88  ? 43.534  -34.021 51.942  1.00 122.98 ?  384 THR B O     1 
ATOM   5820 C CB    . THR B 2 88  ? 41.171  -35.291 50.092  1.00 125.78 ?  384 THR B CB    1 
ATOM   5821 O OG1   . THR B 2 88  ? 41.229  -33.866 49.978  1.00 128.46 ?  384 THR B OG1   1 
ATOM   5822 C CG2   . THR B 2 88  ? 39.714  -35.698 50.211  1.00 128.24 ?  384 THR B CG2   1 
ATOM   5823 N N     . THR B 2 89  ? 44.307  -35.711 50.655  1.00 118.84 ?  385 THR B N     1 
ATOM   5824 C CA    . THR B 2 89  ? 45.634  -35.110 50.574  1.00 117.89 ?  385 THR B CA    1 
ATOM   5825 C C     . THR B 2 89  ? 45.590  -33.772 49.838  1.00 117.66 ?  385 THR B C     1 
ATOM   5826 O O     . THR B 2 89  ? 46.506  -32.955 49.988  1.00 113.35 ?  385 THR B O     1 
ATOM   5827 C CB    . THR B 2 89  ? 46.619  -36.085 49.914  1.00 113.70 ?  385 THR B CB    1 
ATOM   5828 O OG1   . THR B 2 89  ? 46.492  -37.376 50.516  1.00 120.33 ?  385 THR B OG1   1 
ATOM   5829 C CG2   . THR B 2 89  ? 48.030  -35.643 50.124  1.00 106.30 ?  385 THR B CG2   1 
ATOM   5830 N N     . GLU B 2 90  ? 44.523  -33.516 49.074  1.00 120.60 ?  386 GLU B N     1 
ATOM   5831 C CA    . GLU B 2 90  ? 44.277  -32.174 48.549  1.00 121.94 ?  386 GLU B CA    1 
ATOM   5832 C C     . GLU B 2 90  ? 43.883  -31.213 49.671  1.00 118.61 ?  386 GLU B C     1 
ATOM   5833 O O     . GLU B 2 90  ? 44.511  -30.163 49.858  1.00 113.99 ?  386 GLU B O     1 
ATOM   5834 C CB    . GLU B 2 90  ? 43.203  -32.236 47.443  1.00 128.01 ?  386 GLU B CB    1 
ATOM   5835 C CG    . GLU B 2 90  ? 42.694  -30.859 46.924  1.00 136.58 ?  386 GLU B CG    1 
ATOM   5836 C CD    . GLU B 2 90  ? 41.609  -30.953 45.818  1.00 145.40 ?  386 GLU B CD    1 
ATOM   5837 O OE1   . GLU B 2 90  ? 41.237  -32.090 45.426  1.00 146.75 ?  386 GLU B OE1   1 
ATOM   5838 O OE2   . GLU B 2 90  ? 41.119  -29.880 45.358  1.00 139.47 ?  386 GLU B OE2   1 
ATOM   5839 N N     . GLU B 2 91  ? 42.849  -31.570 50.444  1.00 118.40 ?  387 GLU B N     1 
ATOM   5840 C CA    . GLU B 2 91  ? 42.399  -30.710 51.530  1.00 115.92 ?  387 GLU B CA    1 
ATOM   5841 C C     . GLU B 2 91  ? 43.490  -30.502 52.571  1.00 115.91 ?  387 GLU B C     1 
ATOM   5842 O O     . GLU B 2 91  ? 43.562  -29.426 53.184  1.00 115.22 ?  387 GLU B O     1 
ATOM   5843 C CB    . GLU B 2 91  ? 41.143  -31.293 52.165  1.00 114.82 ?  387 GLU B CB    1 
ATOM   5844 C CG    . GLU B 2 91  ? 39.931  -31.206 51.276  1.00 116.44 ?  387 GLU B CG    1 
ATOM   5845 C CD    . GLU B 2 91  ? 38.874  -32.235 51.628  1.00 131.24 ?  387 GLU B CD    1 
ATOM   5846 O OE1   . GLU B 2 91  ? 39.193  -33.251 52.285  1.00 135.46 ?  387 GLU B OE1   1 
ATOM   5847 O OE2   . GLU B 2 91  ? 37.709  -32.030 51.251  1.00 137.20 ?  387 GLU B OE2   1 
ATOM   5848 N N     . GLN B 2 92  ? 44.357  -31.504 52.774  1.00 115.99 ?  388 GLN B N     1 
ATOM   5849 C CA    . GLN B 2 92  ? 45.501  -31.320 53.668  1.00 117.73 ?  388 GLN B CA    1 
ATOM   5850 C C     . GLN B 2 92  ? 46.486  -30.302 53.107  1.00 115.37 ?  388 GLN B C     1 
ATOM   5851 O O     . GLN B 2 92  ? 47.177  -29.615 53.870  1.00 111.29 ?  388 GLN B O     1 
ATOM   5852 C CB    . GLN B 2 92  ? 46.220  -32.653 53.922  1.00 119.71 ?  388 GLN B CB    1 
ATOM   5853 C CG    . GLN B 2 92  ? 45.406  -33.717 54.665  1.00 122.90 ?  388 GLN B CG    1 
ATOM   5854 C CD    . GLN B 2 92  ? 46.161  -35.027 54.831  1.00 125.15 ?  388 GLN B CD    1 
ATOM   5855 O OE1   . GLN B 2 92  ? 47.360  -35.114 54.537  1.00 121.62 ?  388 GLN B OE1   1 
ATOM   5856 N NE2   . GLN B 2 92  ? 45.463  -36.053 55.312  1.00 131.85 ?  388 GLN B NE2   1 
ATOM   5857 N N     . LEU B 2 93  ? 46.555  -30.187 51.777  1.00 118.01 ?  389 LEU B N     1 
ATOM   5858 C CA    . LEU B 2 93  ? 47.502  -29.305 51.104  1.00 112.02 ?  389 LEU B CA    1 
ATOM   5859 C C     . LEU B 2 93  ? 46.939  -27.915 50.860  1.00 109.26 ?  389 LEU B C     1 
ATOM   5860 O O     . LEU B 2 93  ? 47.691  -26.941 50.948  1.00 108.02 ?  389 LEU B O     1 
ATOM   5861 C CB    . LEU B 2 93  ? 47.973  -29.941 49.791  1.00 108.61 ?  389 LEU B CB    1 
ATOM   5862 C CG    . LEU B 2 93  ? 49.095  -30.950 50.035  1.00 106.08 ?  389 LEU B CG    1 
ATOM   5863 C CD1   . LEU B 2 93  ? 49.151  -31.993 48.980  1.00 99.57  ?  389 LEU B CD1   1 
ATOM   5864 C CD2   . LEU B 2 93  ? 50.434  -30.223 50.116  1.00 105.24 ?  389 LEU B CD2   1 
ATOM   5865 N N     . LEU B 2 94  ? 45.638  -27.798 50.551  1.00 111.30 ?  390 LEU B N     1 
ATOM   5866 C CA    . LEU B 2 94  ? 44.975  -26.494 50.618  1.00 113.73 ?  390 LEU B CA    1 
ATOM   5867 C C     . LEU B 2 94  ? 45.103  -25.884 52.005  1.00 120.15 ?  390 LEU B C     1 
ATOM   5868 O O     . LEU B 2 94  ? 45.105  -24.650 52.151  1.00 122.00 ?  390 LEU B O     1 
ATOM   5869 C CB    . LEU B 2 94  ? 43.494  -26.618 50.256  1.00 113.81 ?  390 LEU B CB    1 
ATOM   5870 C CG    . LEU B 2 94  ? 43.104  -26.895 48.811  1.00 119.25 ?  390 LEU B CG    1 
ATOM   5871 C CD1   . LEU B 2 94  ? 41.625  -27.283 48.720  1.00 121.81 ?  390 LEU B CD1   1 
ATOM   5872 C CD2   . LEU B 2 94  ? 43.388  -25.641 47.998  1.00 115.32 ?  390 LEU B CD2   1 
ATOM   5873 N N     . ALA B 2 95  ? 45.215  -26.738 53.027  1.00 118.31 ?  391 ALA B N     1 
ATOM   5874 C CA    . ALA B 2 95  ? 45.262  -26.283 54.410  1.00 109.67 ?  391 ALA B CA    1 
ATOM   5875 C C     . ALA B 2 95  ? 46.598  -25.626 54.741  1.00 104.94 ?  391 ALA B C     1 
ATOM   5876 O O     . ALA B 2 95  ? 46.638  -24.489 55.220  1.00 105.48 ?  391 ALA B O     1 
ATOM   5877 C CB    . ALA B 2 95  ? 44.990  -27.467 55.329  1.00 114.67 ?  391 ALA B CB    1 
ATOM   5878 N N     . VAL B 2 96  ? 47.710  -26.322 54.484  1.00 101.35 ?  392 VAL B N     1 
ATOM   5879 C CA    . VAL B 2 96  ? 49.033  -25.793 54.810  1.00 102.05 ?  392 VAL B CA    1 
ATOM   5880 C C     . VAL B 2 96  ? 49.335  -24.493 54.080  1.00 107.68 ?  392 VAL B C     1 
ATOM   5881 O O     . VAL B 2 96  ? 50.311  -23.806 54.406  1.00 104.97 ?  392 VAL B O     1 
ATOM   5882 C CB    . VAL B 2 96  ? 50.134  -26.820 54.466  1.00 100.85 ?  392 VAL B CB    1 
ATOM   5883 C CG1   . VAL B 2 96  ? 51.524  -26.383 55.013  1.00 91.79  ?  392 VAL B CG1   1 
ATOM   5884 C CG2   . VAL B 2 96  ? 49.737  -28.198 54.922  1.00 108.61 ?  392 VAL B CG2   1 
ATOM   5885 N N     . GLN B 2 97  ? 48.539  -24.146 53.077  1.00 108.41 ?  393 GLN B N     1 
ATOM   5886 C CA    . GLN B 2 97  ? 48.777  -22.911 52.351  1.00 113.64 ?  393 GLN B CA    1 
ATOM   5887 C C     . GLN B 2 97  ? 47.941  -21.772 52.887  1.00 118.83 ?  393 GLN B C     1 
ATOM   5888 O O     . GLN B 2 97  ? 48.398  -20.622 52.899  1.00 121.54 ?  393 GLN B O     1 
ATOM   5889 C CB    . GLN B 2 97  ? 48.479  -23.097 50.869  1.00 117.52 ?  393 GLN B CB    1 
ATOM   5890 C CG    . GLN B 2 97  ? 49.259  -24.233 50.278  1.00 116.98 ?  393 GLN B CG    1 
ATOM   5891 C CD    . GLN B 2 97  ? 49.115  -24.299 48.800  1.00 106.54 ?  393 GLN B CD    1 
ATOM   5892 O OE1   . GLN B 2 97  ? 49.637  -23.447 48.086  1.00 104.05 ?  393 GLN B OE1   1 
ATOM   5893 N NE2   . GLN B 2 97  ? 48.328  -25.252 48.326  1.00 108.38 ?  393 GLN B NE2   1 
ATOM   5894 N N     . ALA B 2 98  ? 46.718  -22.079 53.324  1.00 117.25 ?  394 ALA B N     1 
ATOM   5895 C CA    . ALA B 2 98  ? 45.910  -21.075 54.003  1.00 119.57 ?  394 ALA B CA    1 
ATOM   5896 C C     . ALA B 2 98  ? 46.572  -20.649 55.314  1.00 118.02 ?  394 ALA B C     1 
ATOM   5897 O O     . ALA B 2 98  ? 46.635  -19.457 55.639  1.00 114.86 ?  394 ALA B O     1 
ATOM   5898 C CB    . ALA B 2 98  ? 44.500  -21.628 54.226  1.00 118.18 ?  394 ALA B CB    1 
ATOM   5899 N N     . ILE B 2 99  ? 47.109  -21.617 56.059  1.00 120.54 ?  395 ILE B N     1 
ATOM   5900 C CA    . ILE B 2 99  ? 47.841  -21.333 57.291  1.00 119.65 ?  395 ILE B CA    1 
ATOM   5901 C C     . ILE B 2 99  ? 49.036  -20.422 57.023  1.00 121.09 ?  395 ILE B C     1 
ATOM   5902 O O     . ILE B 2 99  ? 49.487  -19.694 57.915  1.00 126.89 ?  395 ILE B O     1 
ATOM   5903 C CB    . ILE B 2 99  ? 48.258  -22.667 57.954  1.00 113.42 ?  395 ILE B CB    1 
ATOM   5904 C CG1   . ILE B 2 99  ? 47.016  -23.416 58.430  1.00 112.53 ?  395 ILE B CG1   1 
ATOM   5905 C CG2   . ILE B 2 99  ? 49.219  -22.470 59.110  1.00 108.13 ?  395 ILE B CG2   1 
ATOM   5906 C CD1   . ILE B 2 99  ? 47.337  -24.703 59.131  1.00 116.33 ?  395 ILE B CD1   1 
ATOM   5907 N N     . ARG B 2 100 ? 49.564  -20.427 55.805  1.00 115.17 ?  396 ARG B N     1 
ATOM   5908 C CA    . ARG B 2 100 ? 50.695  -19.566 55.517  1.00 111.71 ?  396 ARG B CA    1 
ATOM   5909 C C     . ARG B 2 100 ? 50.254  -18.210 54.997  1.00 110.63 ?  396 ARG B C     1 
ATOM   5910 O O     . ARG B 2 100 ? 51.046  -17.264 55.003  1.00 106.21 ?  396 ARG B O     1 
ATOM   5911 C CB    . ARG B 2 100 ? 51.617  -20.278 54.537  1.00 110.32 ?  396 ARG B CB    1 
ATOM   5912 C CG    . ARG B 2 100 ? 52.841  -19.525 54.128  1.00 110.97 ?  396 ARG B CG    1 
ATOM   5913 C CD    . ARG B 2 100 ? 53.610  -19.024 55.299  1.00 111.38 ?  396 ARG B CD    1 
ATOM   5914 N NE    . ARG B 2 100 ? 54.763  -18.274 54.831  1.00 113.76 ?  396 ARG B NE    1 
ATOM   5915 C CZ    . ARG B 2 100 ? 54.719  -17.021 54.408  1.00 116.98 ?  396 ARG B CZ    1 
ATOM   5916 N NH1   . ARG B 2 100 ? 53.560  -16.375 54.383  1.00 118.62 ?  396 ARG B NH1   1 
ATOM   5917 N NH2   . ARG B 2 100 ? 55.833  -16.423 53.998  1.00 115.81 ?  396 ARG B NH2   1 
ATOM   5918 N N     . LYS B 2 101 ? 48.993  -18.099 54.593  1.00 115.94 ?  397 LYS B N     1 
ATOM   5919 C CA    . LYS B 2 101 ? 48.393  -16.851 54.150  1.00 117.56 ?  397 LYS B CA    1 
ATOM   5920 C C     . LYS B 2 101 ? 47.379  -16.298 55.135  1.00 115.63 ?  397 LYS B C     1 
ATOM   5921 O O     . LYS B 2 101 ? 46.967  -15.149 54.983  1.00 117.89 ?  397 LYS B O     1 
ATOM   5922 C CB    . LYS B 2 101 ? 47.707  -17.034 52.777  1.00 117.77 ?  397 LYS B CB    1 
ATOM   5923 C CG    . LYS B 2 101 ? 47.011  -15.785 52.244  1.00 111.06 ?  397 LYS B CG    1 
ATOM   5924 C CD    . LYS B 2 101 ? 46.423  -15.934 50.874  1.00 113.02 ?  397 LYS B CD    1 
ATOM   5925 C CE    . LYS B 2 101 ? 45.705  -14.641 50.447  1.00 114.20 ?  397 LYS B CE    1 
ATOM   5926 N NZ    . LYS B 2 101 ? 46.516  -13.373 50.492  1.00 107.10 ?  397 LYS B NZ    1 
ATOM   5927 N N     . TYR B 2 102 ? 46.963  -17.089 56.110  1.00 121.26 ?  398 TYR B N     1 
ATOM   5928 C CA    . TYR B 2 102 ? 45.865  -16.532 56.931  1.00 131.72 ?  398 TYR B CA    1 
ATOM   5929 C C     . TYR B 2 102 ? 46.146  -16.583 58.430  1.00 132.55 ?  398 TYR B C     1 
ATOM   5930 O O     . TYR B 2 102 ? 45.223  -16.287 59.188  1.00 129.62 ?  398 TYR B O     1 
ATOM   5931 C CB    . TYR B 2 102 ? 44.561  -17.218 56.534  1.00 126.74 ?  398 TYR B CB    1 
ATOM   5932 C CG    . TYR B 2 102 ? 44.033  -16.802 55.187  1.00 124.35 ?  398 TYR B CG    1 
ATOM   5933 C CD1   . TYR B 2 102 ? 43.196  -15.715 55.055  1.00 123.20 ?  398 TYR B CD1   1 
ATOM   5934 C CD2   . TYR B 2 102 ? 44.389  -17.476 54.040  1.00 126.28 ?  398 TYR B CD2   1 
ATOM   5935 C CE1   . TYR B 2 102 ? 42.697  -15.327 53.828  1.00 120.04 ?  398 TYR B CE1   1 
ATOM   5936 C CE2   . TYR B 2 102 ? 43.900  -17.101 52.805  1.00 121.52 ?  398 TYR B CE2   1 
ATOM   5937 C CZ    . TYR B 2 102 ? 43.059  -16.017 52.695  1.00 118.03 ?  398 TYR B CZ    1 
ATOM   5938 O OH    . TYR B 2 102 ? 42.572  -15.624 51.490  1.00 118.46 ?  398 TYR B OH    1 
ATOM   5939 N N     . GLY B 2 103 ? 47.366  -16.901 58.845  1.00 130.12 ?  399 GLY B N     1 
ATOM   5940 C CA    . GLY B 2 103 ? 47.606  -16.947 60.296  1.00 128.76 ?  399 GLY B CA    1 
ATOM   5941 C C     . GLY B 2 103 ? 46.669  -17.932 60.974  1.00 136.98 ?  399 GLY B C     1 
ATOM   5942 O O     . GLY B 2 103 ? 46.582  -19.053 60.505  1.00 137.33 ?  399 GLY B O     1 
ATOM   5943 N N     . ARG B 2 104 ? 45.938  -17.518 62.009  1.00 142.15 ?  400 ARG B N     1 
ATOM   5944 C CA    . ARG B 2 104 ? 45.041  -18.473 62.713  1.00 141.92 ?  400 ARG B CA    1 
ATOM   5945 C C     . ARG B 2 104 ? 43.580  -18.191 62.369  1.00 137.49 ?  400 ARG B C     1 
ATOM   5946 O O     . ARG B 2 104 ? 42.706  -18.727 63.047  1.00 136.82 ?  400 ARG B O     1 
ATOM   5947 C CB    . ARG B 2 104 ? 45.264  -18.401 64.225  1.00 138.14 ?  400 ARG B CB    1 
ATOM   5948 C CG    . ARG B 2 104 ? 46.553  -17.698 64.625  1.00 139.03 ?  400 ARG B CG    1 
ATOM   5949 C CD    . ARG B 2 104 ? 47.352  -18.387 65.719  1.00 146.77 ?  400 ARG B CD    1 
ATOM   5950 N NE    . ARG B 2 104 ? 48.672  -17.793 65.910  1.00 147.90 ?  400 ARG B NE    1 
ATOM   5951 C CZ    . ARG B 2 104 ? 49.643  -18.322 66.642  1.00 139.30 ?  400 ARG B CZ    1 
ATOM   5952 N NH1   . ARG B 2 104 ? 49.454  -19.471 67.267  1.00 128.24 ?  400 ARG B NH1   1 
ATOM   5953 N NH2   . ARG B 2 104 ? 50.802  -17.700 66.741  1.00 126.49 ?  400 ARG B NH2   1 
ATOM   5954 N N     . ASP B 2 105 ? 43.321  -17.416 61.325  1.00 129.85 ?  401 ASP B N     1 
ATOM   5955 C CA    . ASP B 2 105 ? 41.895  -17.140 61.036  1.00 128.37 ?  401 ASP B CA    1 
ATOM   5956 C C     . ASP B 2 105 ? 41.285  -18.388 60.423  1.00 130.29 ?  401 ASP B C     1 
ATOM   5957 O O     . ASP B 2 105 ? 41.131  -18.436 59.208  1.00 132.29 ?  401 ASP B O     1 
ATOM   5958 C CB    . ASP B 2 105 ? 41.728  -16.004 60.036  1.00 131.13 ?  401 ASP B CB    1 
ATOM   5959 C CG    . ASP B 2 105 ? 40.276  -15.704 59.720  1.00 131.80 ?  401 ASP B CG    1 
ATOM   5960 O OD1   . ASP B 2 105 ? 39.403  -16.513 60.084  1.00 126.03 ?  401 ASP B OD1   1 
ATOM   5961 O OD2   . ASP B 2 105 ? 40.033  -14.652 59.118  1.00 126.46 ?  401 ASP B OD2   1 
ATOM   5962 N N     . PHE B 2 106 ? 40.905  -19.283 61.307  1.00 136.01 ?  402 PHE B N     1 
ATOM   5963 C CA    . PHE B 2 106 ? 40.299  -20.593 61.014  1.00 137.76 ?  402 PHE B CA    1 
ATOM   5964 C C     . PHE B 2 106 ? 39.087  -20.339 60.128  1.00 136.79 ?  402 PHE B C     1 
ATOM   5965 O O     . PHE B 2 106 ? 38.926  -21.014 59.108  1.00 139.80 ?  402 PHE B O     1 
ATOM   5966 C CB    . PHE B 2 106 ? 39.910  -21.234 62.347  1.00 137.24 ?  402 PHE B CB    1 
ATOM   5967 C CG    . PHE B 2 106 ? 40.996  -21.296 63.396  1.00 139.48 ?  402 PHE B CG    1 
ATOM   5968 C CD1   . PHE B 2 106 ? 41.100  -22.399 64.217  1.00 141.40 ?  402 PHE B CD1   1 
ATOM   5969 C CD2   . PHE B 2 106 ? 41.902  -20.267 63.589  1.00 138.02 ?  402 PHE B CD2   1 
ATOM   5970 C CE1   . PHE B 2 106 ? 42.089  -22.475 65.181  1.00 141.39 ?  402 PHE B CE1   1 
ATOM   5971 C CE2   . PHE B 2 106 ? 42.898  -20.343 64.542  1.00 143.21 ?  402 PHE B CE2   1 
ATOM   5972 C CZ    . PHE B 2 106 ? 42.984  -21.448 65.345  1.00 141.35 ?  402 PHE B CZ    1 
ATOM   5973 N N     . GLN B 2 107 ? 38.300  -19.336 60.500  1.00 132.56 ?  403 GLN B N     1 
ATOM   5974 C CA    . GLN B 2 107 ? 37.069  -18.983 59.759  1.00 133.82 ?  403 GLN B CA    1 
ATOM   5975 C C     . GLN B 2 107 ? 37.428  -18.767 58.296  1.00 140.02 ?  403 GLN B C     1 
ATOM   5976 O O     . GLN B 2 107 ? 36.762  -19.352 57.452  1.00 140.69 ?  403 GLN B O     1 
ATOM   5977 C CB    . GLN B 2 107 ? 36.448  -17.729 60.362  1.00 132.92 ?  403 GLN B CB    1 
ATOM   5978 C CG    . GLN B 2 107 ? 35.287  -17.197 59.553  1.00 137.52 ?  403 GLN B CG    1 
ATOM   5979 C CD    . GLN B 2 107 ? 34.660  -18.349 58.822  1.00 142.58 ?  403 GLN B CD    1 
ATOM   5980 O OE1   . GLN B 2 107 ? 34.056  -19.229 59.415  1.00 142.58 ?  403 GLN B OE1   1 
ATOM   5981 N NE2   . GLN B 2 107 ? 34.847  -18.366 57.521  1.00 140.27 ?  403 GLN B NE2   1 
ATOM   5982 N N     . ALA B 2 108 ? 38.451  -17.964 58.019  1.00 140.98 ?  404 ALA B N     1 
ATOM   5983 C CA    . ALA B 2 108 ? 38.846  -17.775 56.608  1.00 134.76 ?  404 ALA B CA    1 
ATOM   5984 C C     . ALA B 2 108 ? 39.258  -19.137 56.078  1.00 134.17 ?  404 ALA B C     1 
ATOM   5985 O O     . ALA B 2 108 ? 38.693  -19.596 55.091  1.00 134.71 ?  404 ALA B O     1 
ATOM   5986 C CB    . ALA B 2 108 ? 39.999  -16.817 56.519  1.00 126.20 ?  404 ALA B CB    1 
ATOM   5987 N N     . ILE B 2 109 ? 40.130  -19.805 56.822  1.00 129.53 ?  405 ILE B N     1 
ATOM   5988 C CA    . ILE B 2 109 ? 40.666  -21.126 56.404  1.00 129.05 ?  405 ILE B CA    1 
ATOM   5989 C C     . ILE B 2 109 ? 39.545  -22.106 56.081  1.00 130.75 ?  405 ILE B C     1 
ATOM   5990 O O     . ILE B 2 109 ? 39.640  -22.722 55.044  1.00 131.83 ?  405 ILE B O     1 
ATOM   5991 C CB    . ILE B 2 109 ? 41.633  -21.681 57.448  1.00 125.80 ?  405 ILE B CB    1 
ATOM   5992 C CG1   . ILE B 2 109 ? 42.814  -20.739 57.654  1.00 121.98 ?  405 ILE B CG1   1 
ATOM   5993 C CG2   . ILE B 2 109 ? 42.105  -23.045 57.015  1.00 123.07 ?  405 ILE B CG2   1 
ATOM   5994 C CD1   . ILE B 2 109 ? 44.139  -21.432 57.564  1.00 120.93 ?  405 ILE B CD1   1 
ATOM   5995 N N     . SER B 2 110 ? 38.446  -22.158 56.835  1.00 131.51 ?  406 SER B N     1 
ATOM   5996 C CA    . SER B 2 110 ? 37.364  -23.116 56.478  1.00 137.14 ?  406 SER B CA    1 
ATOM   5997 C C     . SER B 2 110 ? 36.352  -22.563 55.464  1.00 138.61 ?  406 SER B C     1 
ATOM   5998 O O     . SER B 2 110 ? 35.152  -22.785 55.669  1.00 139.79 ?  406 SER B O     1 
ATOM   5999 C CB    . SER B 2 110 ? 36.657  -23.652 57.677  1.00 137.28 ?  406 SER B CB    1 
ATOM   6000 O OG    . SER B 2 110 ? 35.485  -24.336 57.269  1.00 137.72 ?  406 SER B OG    1 
ATOM   6001 N N     . ASP B 2 111 ? 36.824  -21.853 54.442  1.00 136.62 ?  407 ASP B N     1 
ATOM   6002 C CA    . ASP B 2 111 ? 36.068  -21.336 53.281  1.00 140.34 ?  407 ASP B CA    1 
ATOM   6003 C C     . ASP B 2 111 ? 36.916  -21.787 52.103  1.00 137.84 ?  407 ASP B C     1 
ATOM   6004 O O     . ASP B 2 111 ? 36.372  -22.331 51.139  1.00 136.20 ?  407 ASP B O     1 
ATOM   6005 C CB    . ASP B 2 111 ? 36.085  -19.816 53.222  1.00 139.66 ?  407 ASP B CB    1 
ATOM   6006 C CG    . ASP B 2 111 ? 35.559  -19.180 54.481  1.00 139.57 ?  407 ASP B CG    1 
ATOM   6007 O OD1   . ASP B 2 111 ? 34.731  -19.810 55.142  1.00 138.37 ?  407 ASP B OD1   1 
ATOM   6008 O OD2   . ASP B 2 111 ? 36.001  -18.071 54.804  1.00 136.80 ?  407 ASP B OD2   1 
ATOM   6009 N N     . VAL B 2 112 ? 38.219  -21.549 52.227  1.00 133.42 ?  408 VAL B N     1 
ATOM   6010 C CA    . VAL B 2 112 ? 39.191  -22.008 51.209  1.00 124.91 ?  408 VAL B CA    1 
ATOM   6011 C C     . VAL B 2 112 ? 38.958  -23.500 51.084  1.00 128.42 ?  408 VAL B C     1 
ATOM   6012 O O     . VAL B 2 112 ? 38.672  -23.957 50.001  1.00 132.87 ?  408 VAL B O     1 
ATOM   6013 C CB    . VAL B 2 112 ? 40.611  -21.740 51.699  1.00 120.07 ?  408 VAL B CB    1 
ATOM   6014 C CG1   . VAL B 2 112 ? 41.635  -22.280 50.730  1.00 116.12 ?  408 VAL B CG1   1 
ATOM   6015 C CG2   . VAL B 2 112 ? 40.814  -20.263 51.925  1.00 121.37 ?  408 VAL B CG2   1 
ATOM   6016 N N     . ILE B 2 113 ? 39.071  -24.234 52.177  1.00 128.30 ?  409 ILE B N     1 
ATOM   6017 C CA    . ILE B 2 113 ? 38.757  -25.654 52.042  1.00 126.89 ?  409 ILE B CA    1 
ATOM   6018 C C     . ILE B 2 113 ? 37.258  -25.881 51.868  1.00 135.87 ?  409 ILE B C     1 
ATOM   6019 O O     . ILE B 2 113 ? 36.849  -26.804 51.160  1.00 145.12 ?  409 ILE B O     1 
ATOM   6020 C CB    . ILE B 2 113 ? 39.360  -26.455 53.206  1.00 119.27 ?  409 ILE B CB    1 
ATOM   6021 C CG1   . ILE B 2 113 ? 40.826  -26.032 53.364  1.00 119.12 ?  409 ILE B CG1   1 
ATOM   6022 C CG2   . ILE B 2 113 ? 39.182  -27.948 52.992  1.00 120.02 ?  409 ILE B CG2   1 
ATOM   6023 C CD1   . ILE B 2 113 ? 41.572  -26.709 54.465  1.00 114.07 ?  409 ILE B CD1   1 
ATOM   6024 N N     . GLY B 2 114 ? 36.414  -25.042 52.462  1.00 136.56 ?  410 GLY B N     1 
ATOM   6025 C CA    . GLY B 2 114 ? 35.017  -24.994 52.051  1.00 140.27 ?  410 GLY B CA    1 
ATOM   6026 C C     . GLY B 2 114 ? 34.115  -26.186 52.351  1.00 147.41 ?  410 GLY B C     1 
ATOM   6027 O O     . GLY B 2 114 ? 32.887  -26.029 52.341  1.00 147.52 ?  410 GLY B O     1 
ATOM   6028 N N     . ASN B 2 115 ? 34.676  -27.384 52.574  1.00 147.37 ?  411 ASN B N     1 
ATOM   6029 C CA    . ASN B 2 115 ? 33.897  -28.501 53.110  1.00 150.76 ?  411 ASN B CA    1 
ATOM   6030 C C     . ASN B 2 115 ? 34.486  -28.991 54.424  1.00 149.81 ?  411 ASN B C     1 
ATOM   6031 O O     . ASN B 2 115 ? 34.156  -30.095 54.872  1.00 149.70 ?  411 ASN B O     1 
ATOM   6032 C CB    . ASN B 2 115 ? 33.824  -29.700 52.161  1.00 147.46 ?  411 ASN B CB    1 
ATOM   6033 C CG    . ASN B 2 115 ? 35.114  -30.508 52.144  1.00 145.52 ?  411 ASN B CG    1 
ATOM   6034 O OD1   . ASN B 2 115 ? 36.206  -29.981 52.377  1.00 143.07 ?  411 ASN B OD1   1 
ATOM   6035 N ND2   . ASN B 2 115 ? 34.979  -31.819 51.939  1.00 147.66 ?  411 ASN B ND2   1 
ATOM   6036 N N     . LYS B 2 116 ? 35.413  -28.248 55.008  1.00 146.58 ?  412 LYS B N     1 
ATOM   6037 C CA    . LYS B 2 116 ? 35.855  -28.517 56.361  1.00 143.17 ?  412 LYS B CA    1 
ATOM   6038 C C     . LYS B 2 116 ? 35.312  -27.422 57.271  1.00 147.77 ?  412 LYS B C     1 
ATOM   6039 O O     . LYS B 2 116 ? 35.008  -26.307 56.828  1.00 144.87 ?  412 LYS B O     1 
ATOM   6040 C CB    . LYS B 2 116 ? 37.381  -28.611 56.449  1.00 137.48 ?  412 LYS B CB    1 
ATOM   6041 C CG    . LYS B 2 116 ? 37.939  -29.878 55.836  1.00 131.63 ?  412 LYS B CG    1 
ATOM   6042 C CD    . LYS B 2 116 ? 37.477  -31.087 56.588  1.00 134.76 ?  412 LYS B CD    1 
ATOM   6043 C CE    . LYS B 2 116 ? 37.900  -32.362 55.895  1.00 141.87 ?  412 LYS B CE    1 
ATOM   6044 N NZ    . LYS B 2 116 ? 37.274  -32.489 54.548  1.00 146.19 ?  412 LYS B NZ    1 
ATOM   6045 N N     . SER B 2 117 ? 35.166  -27.777 58.542  1.00 151.85 ?  413 SER B N     1 
ATOM   6046 C CA    . SER B 2 117 ? 34.533  -26.960 59.564  1.00 148.44 ?  413 SER B CA    1 
ATOM   6047 C C     . SER B 2 117 ? 35.580  -26.295 60.447  1.00 143.65 ?  413 SER B C     1 
ATOM   6048 O O     . SER B 2 117 ? 36.683  -26.819 60.635  1.00 140.37 ?  413 SER B O     1 
ATOM   6049 C CB    . SER B 2 117 ? 33.603  -27.825 60.414  1.00 148.60 ?  413 SER B CB    1 
ATOM   6050 O OG    . SER B 2 117 ? 34.347  -28.861 61.034  1.00 145.05 ?  413 SER B OG    1 
ATOM   6051 N N     . VAL B 2 118 ? 35.209  -25.137 61.006  1.00 140.53 ?  414 VAL B N     1 
ATOM   6052 C CA    . VAL B 2 118 ? 36.149  -24.364 61.814  1.00 140.50 ?  414 VAL B CA    1 
ATOM   6053 C C     . VAL B 2 118 ? 36.634  -25.178 63.004  1.00 141.52 ?  414 VAL B C     1 
ATOM   6054 O O     . VAL B 2 118 ? 37.723  -24.933 63.547  1.00 138.39 ?  414 VAL B O     1 
ATOM   6055 C CB    . VAL B 2 118 ? 35.498  -23.045 62.263  1.00 134.60 ?  414 VAL B CB    1 
ATOM   6056 C CG1   . VAL B 2 118 ? 36.532  -22.168 62.937  1.00 130.90 ?  414 VAL B CG1   1 
ATOM   6057 C CG2   . VAL B 2 118 ? 34.857  -22.330 61.078  1.00 135.49 ?  414 VAL B CG2   1 
ATOM   6058 N N     . VAL B 2 119 ? 35.836  -26.152 63.431  1.00 141.67 ?  415 VAL B N     1 
ATOM   6059 C CA    . VAL B 2 119 ? 36.291  -27.091 64.445  1.00 144.25 ?  415 VAL B CA    1 
ATOM   6060 C C     . VAL B 2 119 ? 37.368  -28.008 63.873  1.00 145.90 ?  415 VAL B C     1 
ATOM   6061 O O     . VAL B 2 119 ? 38.492  -28.066 64.389  1.00 143.40 ?  415 VAL B O     1 
ATOM   6062 C CB    . VAL B 2 119 ? 35.091  -27.858 65.041  1.00 148.08 ?  415 VAL B CB    1 
ATOM   6063 C CG1   . VAL B 2 119 ? 34.345  -28.693 64.002  1.00 142.12 ?  415 VAL B CG1   1 
ATOM   6064 C CG2   . VAL B 2 119 ? 35.557  -28.757 66.186  1.00 154.13 ?  415 VAL B CG2   1 
ATOM   6065 N N     . GLN B 2 120 ? 37.054  -28.695 62.768  1.00 146.13 ?  416 GLN B N     1 
ATOM   6066 C CA    . GLN B 2 120 ? 38.020  -29.572 62.122  1.00 144.20 ?  416 GLN B CA    1 
ATOM   6067 C C     . GLN B 2 120 ? 39.326  -28.854 61.843  1.00 141.20 ?  416 GLN B C     1 
ATOM   6068 O O     . GLN B 2 120 ? 40.403  -29.444 61.995  1.00 139.35 ?  416 GLN B O     1 
ATOM   6069 C CB    . GLN B 2 120 ? 37.410  -30.134 60.842  1.00 142.51 ?  416 GLN B CB    1 
ATOM   6070 C CG    . GLN B 2 120 ? 36.618  -31.410 61.062  1.00 144.92 ?  416 GLN B CG    1 
ATOM   6071 C CD    . GLN B 2 120 ? 35.653  -31.713 59.931  1.00 150.87 ?  416 GLN B CD    1 
ATOM   6072 O OE1   . GLN B 2 120 ? 35.285  -30.826 59.159  1.00 153.79 ?  416 GLN B OE1   1 
ATOM   6073 N NE2   . GLN B 2 120 ? 35.274  -32.978 59.799  1.00 151.03 ?  416 GLN B NE2   1 
ATOM   6074 N N     . VAL B 2 121 ? 39.151  -27.575 61.595  1.00 138.84 ?  417 VAL B N     1 
ATOM   6075 C CA    . VAL B 2 121 ? 40.286  -26.658 61.371  1.00 138.72 ?  417 VAL B CA    1 
ATOM   6076 C C     . VAL B 2 121 ? 41.126  -26.727 62.638  1.00 143.29 ?  417 VAL B C     1 
ATOM   6077 O O     . VAL B 2 121 ? 42.278  -27.129 62.547  1.00 138.90 ?  417 VAL B O     1 
ATOM   6078 C CB    . VAL B 2 121 ? 39.746  -25.238 61.152  1.00 136.80 ?  417 VAL B CB    1 
ATOM   6079 C CG1   . VAL B 2 121 ? 39.876  -24.821 59.703  1.00 131.35 ?  417 VAL B CG1   1 
ATOM   6080 C CG2   . VAL B 2 121 ? 38.300  -25.098 61.613  1.00 134.38 ?  417 VAL B CG2   1 
ATOM   6081 N N     . LYS B 2 122 ? 40.507  -26.470 63.789  1.00 144.52 ?  418 LYS B N     1 
ATOM   6082 C CA    . LYS B 2 122 ? 41.280  -26.419 65.053  1.00 142.02 ?  418 LYS B CA    1 
ATOM   6083 C C     . LYS B 2 122 ? 41.945  -27.770 65.285  1.00 144.50 ?  418 LYS B C     1 
ATOM   6084 O O     . LYS B 2 122 ? 43.161  -27.805 65.511  1.00 138.69 ?  418 LYS B O     1 
ATOM   6085 C CB    . LYS B 2 122 ? 40.330  -26.169 66.225  1.00 141.81 ?  418 LYS B CB    1 
ATOM   6086 C CG    . LYS B 2 122 ? 39.825  -24.743 66.398  1.00 141.74 ?  418 LYS B CG    1 
ATOM   6087 C CD    . LYS B 2 122 ? 39.856  -24.229 67.838  1.00 148.85 ?  418 LYS B CD    1 
ATOM   6088 C CE    . LYS B 2 122 ? 39.587  -25.273 68.905  1.00 152.86 ?  418 LYS B CE    1 
ATOM   6089 N NZ    . LYS B 2 122 ? 39.987  -24.811 70.257  1.00 127.80 ?  418 LYS B NZ    1 
ATOM   6090 N N     . ASN B 2 123 ? 41.198  -28.853 65.085  1.00 149.14 ?  419 ASN B N     1 
ATOM   6091 C CA    . ASN B 2 123 ? 41.758  -30.207 65.322  1.00 153.32 ?  419 ASN B CA    1 
ATOM   6092 C C     . ASN B 2 123 ? 42.907  -30.451 64.358  1.00 150.89 ?  419 ASN B C     1 
ATOM   6093 O O     . ASN B 2 123 ? 43.972  -30.880 64.811  1.00 149.83 ?  419 ASN B O     1 
ATOM   6094 C CB    . ASN B 2 123 ? 40.701  -31.295 65.169  1.00 157.16 ?  419 ASN B CB    1 
ATOM   6095 C CG    . ASN B 2 123 ? 39.578  -31.111 66.159  1.00 160.89 ?  419 ASN B CG    1 
ATOM   6096 O OD1   . ASN B 2 123 ? 39.481  -31.840 67.143  1.00 167.90 ?  419 ASN B OD1   1 
ATOM   6097 N ND2   . ASN B 2 123 ? 38.746  -30.117 65.915  1.00 155.72 ?  419 ASN B ND2   1 
ATOM   6098 N N     . PHE B 2 124 ? 42.719  -29.992 63.125  1.00 145.76 ?  420 PHE B N     1 
ATOM   6099 C CA    . PHE B 2 124 ? 43.755  -30.171 62.086  1.00 147.83 ?  420 PHE B CA    1 
ATOM   6100 C C     . PHE B 2 124 ? 45.070  -29.597 62.586  1.00 147.76 ?  420 PHE B C     1 
ATOM   6101 O O     . PHE B 2 124 ? 46.067  -30.316 62.540  1.00 146.56 ?  420 PHE B O     1 
ATOM   6102 C CB    . PHE B 2 124 ? 43.388  -29.447 60.798  1.00 146.69 ?  420 PHE B CB    1 
ATOM   6103 C CG    . PHE B 2 124 ? 44.380  -29.709 59.697  1.00 140.17 ?  420 PHE B CG    1 
ATOM   6104 C CD1   . PHE B 2 124 ? 44.086  -30.584 58.673  1.00 132.29 ?  420 PHE B CD1   1 
ATOM   6105 C CD2   . PHE B 2 124 ? 45.629  -29.120 59.718  1.00 133.47 ?  420 PHE B CD2   1 
ATOM   6106 C CE1   . PHE B 2 124 ? 45.002  -30.826 57.670  1.00 132.61 ?  420 PHE B CE1   1 
ATOM   6107 C CE2   . PHE B 2 124 ? 46.550  -29.371 58.718  1.00 123.49 ?  420 PHE B CE2   1 
ATOM   6108 C CZ    . PHE B 2 124 ? 46.235  -30.227 57.698  1.00 129.73 ?  420 PHE B CZ    1 
ATOM   6109 N N     . PHE B 2 125 ? 45.021  -28.386 63.130  1.00 144.51 ?  421 PHE B N     1 
ATOM   6110 C CA    . PHE B 2 125 ? 46.260  -27.768 63.644  1.00 142.22 ?  421 PHE B CA    1 
ATOM   6111 C C     . PHE B 2 125 ? 46.849  -28.689 64.706  1.00 142.21 ?  421 PHE B C     1 
ATOM   6112 O O     . PHE B 2 125 ? 48.041  -28.942 64.693  1.00 135.71 ?  421 PHE B O     1 
ATOM   6113 C CB    . PHE B 2 125 ? 45.905  -26.512 64.431  1.00 138.24 ?  421 PHE B CB    1 
ATOM   6114 C CG    . PHE B 2 125 ? 45.732  -25.263 63.613  1.00 134.04 ?  421 PHE B CG    1 
ATOM   6115 C CD1   . PHE B 2 125 ? 44.490  -24.898 63.138  1.00 134.87 ?  421 PHE B CD1   1 
ATOM   6116 C CD2   . PHE B 2 125 ? 46.804  -24.434 63.353  1.00 129.88 ?  421 PHE B CD2   1 
ATOM   6117 C CE1   . PHE B 2 125 ? 44.317  -23.746 62.397  1.00 133.18 ?  421 PHE B CE1   1 
ATOM   6118 C CE2   . PHE B 2 125 ? 46.632  -23.280 62.612  1.00 125.57 ?  421 PHE B CE2   1 
ATOM   6119 C CZ    . PHE B 2 125 ? 45.391  -22.938 62.140  1.00 130.23 ?  421 PHE B CZ    1 
ATOM   6120 N N     . VAL B 2 126 ? 45.986  -29.287 65.500  1.00 145.58 ?  422 VAL B N     1 
ATOM   6121 C CA    . VAL B 2 126 ? 46.532  -30.137 66.586  1.00 150.53 ?  422 VAL B CA    1 
ATOM   6122 C C     . VAL B 2 126 ? 47.130  -31.420 66.018  1.00 153.98 ?  422 VAL B C     1 
ATOM   6123 O O     . VAL B 2 126 ? 48.347  -31.617 66.104  1.00 155.85 ?  422 VAL B O     1 
ATOM   6124 C CB    . VAL B 2 126 ? 45.405  -30.489 67.561  1.00 145.48 ?  422 VAL B CB    1 
ATOM   6125 C CG1   . VAL B 2 126 ? 45.821  -31.602 68.503  1.00 142.67 ?  422 VAL B CG1   1 
ATOM   6126 C CG2   . VAL B 2 126 ? 44.947  -29.263 68.327  1.00 138.46 ?  422 VAL B CG2   1 
ATOM   6127 N N     . ASN B 2 127 ? 46.291  -32.235 65.378  1.00 152.68 ?  423 ASN B N     1 
ATOM   6128 C CA    . ASN B 2 127 ? 46.704  -33.590 64.939  1.00 154.01 ?  423 ASN B CA    1 
ATOM   6129 C C     . ASN B 2 127 ? 47.984  -33.579 64.111  1.00 153.02 ?  423 ASN B C     1 
ATOM   6130 O O     . ASN B 2 127 ? 48.933  -34.268 64.498  1.00 147.47 ?  423 ASN B O     1 
ATOM   6131 C CB    . ASN B 2 127 ? 45.597  -34.291 64.158  1.00 154.62 ?  423 ASN B CB    1 
ATOM   6132 C CG    . ASN B 2 127 ? 44.241  -34.083 64.787  1.00 154.83 ?  423 ASN B CG    1 
ATOM   6133 O OD1   . ASN B 2 127 ? 44.072  -34.296 65.980  1.00 154.49 ?  423 ASN B OD1   1 
ATOM   6134 N ND2   . ASN B 2 127 ? 43.274  -33.652 64.000  1.00 154.11 ?  423 ASN B ND2   1 
ATOM   6135 N N     . TYR B 2 128 ? 48.049  -32.754 63.076  1.00 150.64 ?  424 TYR B N     1 
ATOM   6136 C CA    . TYR B 2 128 ? 49.211  -32.933 62.172  1.00 145.96 ?  424 TYR B CA    1 
ATOM   6137 C C     . TYR B 2 128 ? 50.329  -31.942 62.460  1.00 140.04 ?  424 TYR B C     1 
ATOM   6138 O O     . TYR B 2 128 ? 51.252  -31.889 61.658  1.00 140.44 ?  424 TYR B O     1 
ATOM   6139 C CB    . TYR B 2 128 ? 48.767  -32.836 60.715  1.00 139.35 ?  424 TYR B CB    1 
ATOM   6140 C CG    . TYR B 2 128 ? 47.845  -33.941 60.278  1.00 139.44 ?  424 TYR B CG    1 
ATOM   6141 C CD1   . TYR B 2 128 ? 48.337  -35.174 59.899  1.00 137.68 ?  424 TYR B CD1   1 
ATOM   6142 C CD2   . TYR B 2 128 ? 46.477  -33.751 60.246  1.00 141.48 ?  424 TYR B CD2   1 
ATOM   6143 C CE1   . TYR B 2 128 ? 47.493  -36.188 59.487  1.00 143.53 ?  424 TYR B CE1   1 
ATOM   6144 C CE2   . TYR B 2 128 ? 45.616  -34.755 59.841  1.00 144.10 ?  424 TYR B CE2   1 
ATOM   6145 C CZ    . TYR B 2 128 ? 46.128  -35.981 59.465  1.00 148.12 ?  424 TYR B CZ    1 
ATOM   6146 O OH    . TYR B 2 128 ? 45.285  -36.981 59.078  1.00 148.45 ?  424 TYR B OH    1 
ATOM   6147 N N     . ARG B 2 129 ? 50.306  -31.281 63.610  1.00 138.05 ?  425 ARG B N     1 
ATOM   6148 C CA    . ARG B 2 129 ? 51.306  -30.217 63.870  1.00 140.42 ?  425 ARG B CA    1 
ATOM   6149 C C     . ARG B 2 129 ? 52.726  -30.762 63.788  1.00 135.67 ?  425 ARG B C     1 
ATOM   6150 O O     . ARG B 2 129 ? 53.586  -30.064 63.270  1.00 128.40 ?  425 ARG B O     1 
ATOM   6151 C CB    . ARG B 2 129 ? 51.114  -29.650 65.277  1.00 146.30 ?  425 ARG B CB    1 
ATOM   6152 C CG    . ARG B 2 129 ? 52.388  -29.131 65.926  1.00 148.46 ?  425 ARG B CG    1 
ATOM   6153 C CD    . ARG B 2 129 ? 52.642  -29.860 67.232  1.00 152.06 ?  425 ARG B CD    1 
ATOM   6154 N NE    . ARG B 2 129 ? 53.083  -29.023 68.334  1.00 153.52 ?  425 ARG B NE    1 
ATOM   6155 C CZ    . ARG B 2 129 ? 52.621  -27.810 68.584  1.00 157.03 ?  425 ARG B CZ    1 
ATOM   6156 N NH1   . ARG B 2 129 ? 51.703  -27.271 67.801  1.00 156.08 ?  425 ARG B NH1   1 
ATOM   6157 N NH2   . ARG B 2 129 ? 53.085  -27.135 69.617  1.00 156.16 ?  425 ARG B NH2   1 
ATOM   6158 N N     . ARG B 2 130 ? 52.971  -31.942 64.330  1.00 136.10 ?  426 ARG B N     1 
ATOM   6159 C CA    . ARG B 2 130 ? 54.350  -32.461 64.270  1.00 136.64 ?  426 ARG B CA    1 
ATOM   6160 C C     . ARG B 2 130 ? 54.748  -32.723 62.819  1.00 141.83 ?  426 ARG B C     1 
ATOM   6161 O O     . ARG B 2 130 ? 55.829  -32.288 62.411  1.00 139.91 ?  426 ARG B O     1 
ATOM   6162 C CB    . ARG B 2 130 ? 54.369  -33.825 64.961  1.00 146.29 ?  426 ARG B CB    1 
ATOM   6163 C CG    . ARG B 2 130 ? 54.783  -33.803 66.424  1.00 151.99 ?  426 ARG B CG    1 
ATOM   6164 C CD    . ARG B 2 130 ? 55.171  -35.198 66.870  1.00 152.44 ?  426 ARG B CD    1 
ATOM   6165 N NE    . ARG B 2 130 ? 56.212  -35.158 67.882  1.00 161.58 ?  426 ARG B NE    1 
ATOM   6166 C CZ    . ARG B 2 130 ? 57.486  -34.885 67.642  1.00 167.58 ?  426 ARG B CZ    1 
ATOM   6167 N NH1   . ARG B 2 130 ? 57.893  -34.633 66.412  1.00 164.06 ?  426 ARG B NH1   1 
ATOM   6168 N NH2   . ARG B 2 130 ? 58.351  -34.872 68.638  1.00 167.10 ?  426 ARG B NH2   1 
ATOM   6169 N N     . ARG B 2 131 ? 53.863  -33.383 62.075  1.00 143.73 ?  427 ARG B N     1 
ATOM   6170 C CA    . ARG B 2 131 ? 54.167  -33.862 60.701  1.00 134.96 ?  427 ARG B CA    1 
ATOM   6171 C C     . ARG B 2 131 ? 54.378  -32.742 59.687  1.00 134.59 ?  427 ARG B C     1 
ATOM   6172 O O     . ARG B 2 131 ? 55.356  -32.807 58.934  1.00 131.16 ?  427 ARG B O     1 
ATOM   6173 C CB    . ARG B 2 131 ? 53.027  -34.761 60.230  1.00 130.88 ?  427 ARG B CB    1 
ATOM   6174 C CG    . ARG B 2 131 ? 52.861  -36.018 61.065  1.00 126.88 ?  427 ARG B CG    1 
ATOM   6175 C CD    . ARG B 2 131 ? 51.917  -36.950 60.351  1.00 132.98 ?  427 ARG B CD    1 
ATOM   6176 N NE    . ARG B 2 131 ? 50.673  -37.102 61.075  1.00 138.18 ?  427 ARG B NE    1 
ATOM   6177 C CZ    . ARG B 2 131 ? 49.885  -38.152 60.950  1.00 142.25 ?  427 ARG B CZ    1 
ATOM   6178 N NH1   . ARG B 2 131 ? 50.222  -39.126 60.127  1.00 144.54 ?  427 ARG B NH1   1 
ATOM   6179 N NH2   . ARG B 2 131 ? 48.772  -38.233 61.651  1.00 143.01 ?  427 ARG B NH2   1 
ATOM   6180 N N     . PHE B 2 132 ? 53.511  -31.740 59.701  1.00 131.50 ?  428 PHE B N     1 
ATOM   6181 C CA    . PHE B 2 132 ? 53.593  -30.666 58.689  1.00 123.91 ?  428 PHE B CA    1 
ATOM   6182 C C     . PHE B 2 132 ? 54.464  -29.526 59.185  1.00 125.10 ?  428 PHE B C     1 
ATOM   6183 O O     . PHE B 2 132 ? 54.509  -28.511 58.517  1.00 123.94 ?  428 PHE B O     1 
ATOM   6184 C CB    . PHE B 2 132 ? 52.202  -30.095 58.460  1.00 115.38 ?  428 PHE B CB    1 
ATOM   6185 C CG    . PHE B 2 132 ? 51.351  -30.969 57.588  1.00 119.84 ?  428 PHE B CG    1 
ATOM   6186 C CD1   . PHE B 2 132 ? 51.935  -31.893 56.748  1.00 123.61 ?  428 PHE B CD1   1 
ATOM   6187 C CD2   . PHE B 2 132 ? 49.977  -30.865 57.602  1.00 120.97 ?  428 PHE B CD2   1 
ATOM   6188 C CE1   . PHE B 2 132 ? 51.157  -32.695 55.934  1.00 118.43 ?  428 PHE B CE1   1 
ATOM   6189 C CE2   . PHE B 2 132 ? 49.201  -31.668 56.789  1.00 123.58 ?  428 PHE B CE2   1 
ATOM   6190 C CZ    . PHE B 2 132 ? 49.792  -32.583 55.958  1.00 117.83 ?  428 PHE B CZ    1 
ATOM   6191 N N     . ASN B 2 133 ? 55.003  -29.637 60.396  1.00 129.03 ?  429 ASN B N     1 
ATOM   6192 C CA    . ASN B 2 133 ? 55.826  -28.560 61.009  1.00 128.61 ?  429 ASN B CA    1 
ATOM   6193 C C     . ASN B 2 133 ? 55.035  -27.253 61.015  1.00 128.89 ?  429 ASN B C     1 
ATOM   6194 O O     . ASN B 2 133 ? 55.653  -26.218 60.744  1.00 128.96 ?  429 ASN B O     1 
ATOM   6195 C CB    . ASN B 2 133 ? 57.168  -28.392 60.306  1.00 123.67 ?  429 ASN B CB    1 
ATOM   6196 C CG    . ASN B 2 133 ? 57.918  -29.697 60.197  1.00 126.70 ?  429 ASN B CG    1 
ATOM   6197 O OD1   . ASN B 2 133 ? 57.317  -30.744 60.001  1.00 130.10 ?  429 ASN B OD1   1 
ATOM   6198 N ND2   . ASN B 2 133 ? 59.229  -29.645 60.337  1.00 121.20 ?  429 ASN B ND2   1 
ATOM   6199 N N     . ILE B 2 134 ? 53.747  -27.316 61.372  1.00 128.76 ?  430 ILE B N     1 
ATOM   6200 C CA    . ILE B 2 134 ? 52.822  -26.159 61.327  1.00 122.60 ?  430 ILE B CA    1 
ATOM   6201 C C     . ILE B 2 134 ? 53.474  -25.050 62.111  1.00 125.87 ?  430 ILE B C     1 
ATOM   6202 O O     . ILE B 2 134 ? 53.303  -23.885 61.747  1.00 123.92 ?  430 ILE B O     1 
ATOM   6203 C CB    . ILE B 2 134 ? 51.490  -26.533 61.965  1.00 117.60 ?  430 ILE B CB    1 
ATOM   6204 C CG1   . ILE B 2 134 ? 50.706  -27.471 61.058  1.00 126.30 ?  430 ILE B CG1   1 
ATOM   6205 C CG2   . ILE B 2 134 ? 50.716  -25.277 62.283  1.00 110.38 ?  430 ILE B CG2   1 
ATOM   6206 C CD1   . ILE B 2 134 ? 49.585  -28.185 61.758  1.00 132.34 ?  430 ILE B CD1   1 
ATOM   6207 N N     . ASP B 2 135 ? 54.201  -25.449 63.140  1.00 133.13 ?  431 ASP B N     1 
ATOM   6208 C CA    . ASP B 2 135 ? 54.886  -24.429 63.923  1.00 141.11 ?  431 ASP B CA    1 
ATOM   6209 C C     . ASP B 2 135 ? 55.786  -23.576 63.029  1.00 134.56 ?  431 ASP B C     1 
ATOM   6210 O O     . ASP B 2 135 ? 55.681  -22.340 63.013  1.00 126.50 ?  431 ASP B O     1 
ATOM   6211 C CB    . ASP B 2 135 ? 55.681  -25.114 65.039  1.00 150.06 ?  431 ASP B CB    1 
ATOM   6212 C CG    . ASP B 2 135 ? 54.778  -25.840 66.054  1.00 155.53 ?  431 ASP B CG    1 
ATOM   6213 O OD1   . ASP B 2 135 ? 53.629  -25.391 66.292  1.00 154.37 ?  431 ASP B OD1   1 
ATOM   6214 O OD2   . ASP B 2 135 ? 55.206  -26.891 66.586  1.00 156.70 ?  431 ASP B OD2   1 
ATOM   6215 N N     . GLU B 2 136 ? 56.670  -24.238 62.270  1.00 135.16 ?  432 GLU B N     1 
ATOM   6216 C CA    . GLU B 2 136 ? 57.528  -23.559 61.303  1.00 129.94 ?  432 GLU B CA    1 
ATOM   6217 C C     . GLU B 2 136 ? 56.702  -22.670 60.394  1.00 130.29 ?  432 GLU B C     1 
ATOM   6218 O O     . GLU B 2 136 ? 57.100  -21.542 60.074  1.00 132.06 ?  432 GLU B O     1 
ATOM   6219 C CB    . GLU B 2 136 ? 58.269  -24.594 60.459  1.00 125.82 ?  432 GLU B CB    1 
ATOM   6220 C CG    . GLU B 2 136 ? 59.138  -25.551 61.245  1.00 133.74 ?  432 GLU B CG    1 
ATOM   6221 C CD    . GLU B 2 136 ? 59.773  -26.608 60.360  1.00 133.91 ?  432 GLU B CD    1 
ATOM   6222 O OE1   . GLU B 2 136 ? 59.484  -26.600 59.147  1.00 139.16 ?  432 GLU B OE1   1 
ATOM   6223 O OE2   . GLU B 2 136 ? 60.496  -27.493 60.876  1.00 138.30 ?  432 GLU B OE2   1 
ATOM   6224 N N     . VAL B 2 137 ? 55.542  -23.177 59.966  1.00 127.93 ?  433 VAL B N     1 
ATOM   6225 C CA    . VAL B 2 137 ? 54.654  -22.427 59.078  1.00 126.85 ?  433 VAL B CA    1 
ATOM   6226 C C     . VAL B 2 137 ? 54.263  -21.104 59.714  1.00 131.56 ?  433 VAL B C     1 
ATOM   6227 O O     . VAL B 2 137 ? 54.529  -20.020 59.169  1.00 124.70 ?  433 VAL B O     1 
ATOM   6228 C CB    . VAL B 2 137 ? 53.399  -23.254 58.756  1.00 118.85 ?  433 VAL B CB    1 
ATOM   6229 C CG1   . VAL B 2 137 ? 52.362  -22.369 58.098  1.00 105.41 ?  433 VAL B CG1   1 
ATOM   6230 C CG2   . VAL B 2 137 ? 53.764  -24.456 57.894  1.00 122.25 ?  433 VAL B CG2   1 
ATOM   6231 N N     . LEU B 2 138 ? 53.623  -21.196 60.892  1.00 134.93 ?  434 LEU B N     1 
ATOM   6232 C CA    . LEU B 2 138 ? 52.990  -20.051 61.543  1.00 128.61 ?  434 LEU B CA    1 
ATOM   6233 C C     . LEU B 2 138 ? 53.995  -18.959 61.845  1.00 126.18 ?  434 LEU B C     1 
ATOM   6234 O O     . LEU B 2 138 ? 53.696  -17.767 61.692  1.00 121.05 ?  434 LEU B O     1 
ATOM   6235 C CB    . LEU B 2 138 ? 52.277  -20.523 62.810  1.00 120.39 ?  434 LEU B CB    1 
ATOM   6236 C CG    . LEU B 2 138 ? 50.949  -21.172 62.422  1.00 120.92 ?  434 LEU B CG    1 
ATOM   6237 C CD1   . LEU B 2 138 ? 50.388  -22.112 63.458  1.00 122.80 ?  434 LEU B CD1   1 
ATOM   6238 C CD2   . LEU B 2 138 ? 49.958  -20.044 62.173  1.00 117.00 ?  434 LEU B CD2   1 
ATOM   6239 N N     . GLN B 2 139 ? 55.207  -19.350 62.231  1.00 127.75 ?  435 GLN B N     1 
ATOM   6240 C CA    . GLN B 2 139 ? 56.235  -18.368 62.538  1.00 133.50 ?  435 GLN B CA    1 
ATOM   6241 C C     . GLN B 2 139 ? 56.672  -17.563 61.305  1.00 130.56 ?  435 GLN B C     1 
ATOM   6242 O O     . GLN B 2 139 ? 57.029  -16.385 61.443  1.00 125.20 ?  435 GLN B O     1 
ATOM   6243 C CB    . GLN B 2 139 ? 57.387  -19.086 63.252  1.00 136.41 ?  435 GLN B CB    1 
ATOM   6244 C CG    . GLN B 2 139 ? 58.348  -19.849 62.366  1.00 140.48 ?  435 GLN B CG    1 
ATOM   6245 C CD    . GLN B 2 139 ? 59.396  -20.588 63.181  1.00 145.49 ?  435 GLN B CD    1 
ATOM   6246 O OE1   . GLN B 2 139 ? 59.124  -21.031 64.306  1.00 141.02 ?  435 GLN B OE1   1 
ATOM   6247 N NE2   . GLN B 2 139 ? 60.593  -20.746 62.613  1.00 149.54 ?  435 GLN B NE2   1 
ATOM   6248 N N     . GLU B 2 140 ? 56.607  -18.131 60.090  1.00 131.91 ?  436 GLU B N     1 
ATOM   6249 C CA    . GLU B 2 140 ? 56.839  -17.260 58.935  1.00 135.02 ?  436 GLU B CA    1 
ATOM   6250 C C     . GLU B 2 140 ? 55.613  -16.474 58.482  1.00 134.05 ?  436 GLU B C     1 
ATOM   6251 O O     . GLU B 2 140 ? 55.776  -15.441 57.815  1.00 131.72 ?  436 GLU B O     1 
ATOM   6252 C CB    . GLU B 2 140 ? 57.390  -18.005 57.727  1.00 128.96 ?  436 GLU B CB    1 
ATOM   6253 C CG    . GLU B 2 140 ? 58.838  -18.381 57.849  1.00 134.39 ?  436 GLU B CG    1 
ATOM   6254 C CD    . GLU B 2 140 ? 59.365  -18.959 56.552  1.00 129.21 ?  436 GLU B CD    1 
ATOM   6255 O OE1   . GLU B 2 140 ? 58.550  -19.199 55.634  1.00 133.18 ?  436 GLU B OE1   1 
ATOM   6256 O OE2   . GLU B 2 140 ? 60.594  -19.117 56.418  1.00 125.16 ?  436 GLU B OE2   1 
ATOM   6257 N N     . TRP B 2 141 ? 54.402  -16.940 58.794  1.00 133.92 ?  437 TRP B N     1 
ATOM   6258 C CA    . TRP B 2 141 ? 53.228  -16.082 58.648  1.00 132.06 ?  437 TRP B CA    1 
ATOM   6259 C C     . TRP B 2 141 ? 53.358  -14.817 59.492  1.00 135.44 ?  437 TRP B C     1 
ATOM   6260 O O     . TRP B 2 141 ? 53.029  -13.711 59.034  1.00 132.67 ?  437 TRP B O     1 
ATOM   6261 C CB    . TRP B 2 141 ? 51.970  -16.855 59.040  1.00 132.52 ?  437 TRP B CB    1 
ATOM   6262 C CG    . TRP B 2 141 ? 50.703  -16.076 58.841  1.00 132.10 ?  437 TRP B CG    1 
ATOM   6263 C CD1   . TRP B 2 141 ? 49.918  -16.061 57.726  1.00 131.56 ?  437 TRP B CD1   1 
ATOM   6264 C CD2   . TRP B 2 141 ? 50.054  -15.229 59.800  1.00 131.47 ?  437 TRP B CD2   1 
ATOM   6265 N NE1   . TRP B 2 141 ? 48.831  -15.238 57.921  1.00 132.37 ?  437 TRP B NE1   1 
ATOM   6266 C CE2   . TRP B 2 141 ? 48.887  -14.717 59.184  1.00 129.77 ?  437 TRP B CE2   1 
ATOM   6267 C CE3   . TRP B 2 141 ? 50.349  -14.846 61.109  1.00 128.63 ?  437 TRP B CE3   1 
ATOM   6268 C CZ2   . TRP B 2 141 ? 48.012  -13.854 59.834  1.00 129.45 ?  437 TRP B CZ2   1 
ATOM   6269 C CZ3   . TRP B 2 141 ? 49.482  -13.987 61.751  1.00 132.47 ?  437 TRP B CZ3   1 
ATOM   6270 C CH2   . TRP B 2 141 ? 48.324  -13.499 61.113  1.00 131.20 ?  437 TRP B CH2   1 
ATOM   6271 N N     . GLU B 2 142 ? 53.829  -14.972 60.735  1.00 133.72 ?  438 GLU B N     1 
ATOM   6272 C CA    . GLU B 2 142 ? 54.067  -13.829 61.608  1.00 134.12 ?  438 GLU B CA    1 
ATOM   6273 C C     . GLU B 2 142 ? 55.102  -12.870 61.005  1.00 138.84 ?  438 GLU B C     1 
ATOM   6274 O O     . GLU B 2 142 ? 54.973  -11.643 61.134  1.00 141.51 ?  438 GLU B O     1 
ATOM   6275 C CB    . GLU B 2 142 ? 54.476  -14.346 62.999  1.00 133.52 ?  438 GLU B CB    1 
ATOM   6276 C CG    . GLU B 2 142 ? 53.355  -15.222 63.666  1.00 137.82 ?  438 GLU B CG    1 
ATOM   6277 C CD    . GLU B 2 142 ? 53.665  -15.780 65.086  1.00 135.96 ?  438 GLU B CD    1 
ATOM   6278 O OE1   . GLU B 2 142 ? 54.825  -15.677 65.550  1.00 137.17 ?  438 GLU B OE1   1 
ATOM   6279 O OE2   . GLU B 2 142 ? 52.744  -16.365 65.722  1.00 125.14 ?  438 GLU B OE2   1 
ATOM   6280 N N     . ALA B 2 143 ? 56.106  -13.400 60.293  1.00 135.57 ?  439 ALA B N     1 
ATOM   6281 C CA    . ALA B 2 143 ? 57.121  -12.543 59.685  1.00 131.00 ?  439 ALA B CA    1 
ATOM   6282 C C     . ALA B 2 143 ? 56.588  -11.686 58.536  1.00 138.60 ?  439 ALA B C     1 
ATOM   6283 O O     . ALA B 2 143 ? 57.361  -10.911 57.962  1.00 142.82 ?  439 ALA B O     1 
ATOM   6284 C CB    . ALA B 2 143 ? 58.303  -13.387 59.202  1.00 126.77 ?  439 ALA B CB    1 
ATOM   6285 N N     . GLU B 2 144 ? 55.307  -11.789 58.182  1.00 139.17 ?  440 GLU B N     1 
ATOM   6286 C CA    . GLU B 2 144 ? 54.716  -10.850 57.221  1.00 136.00 ?  440 GLU B CA    1 
ATOM   6287 C C     . GLU B 2 144 ? 53.607  -10.016 57.872  1.00 133.05 ?  440 GLU B C     1 
ATOM   6288 O O     . GLU B 2 144 ? 52.560  -10.543 58.257  1.00 130.62 ?  440 GLU B O     1 
ATOM   6289 C CB    . GLU B 2 144 ? 54.164  -11.578 55.981  1.00 135.86 ?  440 GLU B CB    1 
ATOM   6290 C CG    . GLU B 2 144 ? 55.226  -12.288 55.104  1.00 138.71 ?  440 GLU B CG    1 
ATOM   6291 C CD    . GLU B 2 144 ? 54.716  -12.731 53.699  1.00 139.30 ?  440 GLU B CD    1 
ATOM   6292 O OE1   . GLU B 2 144 ? 53.587  -12.362 53.280  1.00 135.72 ?  440 GLU B OE1   1 
ATOM   6293 O OE2   . GLU B 2 144 ? 55.467  -13.452 53.003  1.00 134.28 ?  440 GLU B OE2   1 
ATOM   6294 N N     . ALA C 3 1   ? -1.546  52.902  85.503  1.00 106.08 ?  1   ALA C N     1 
ATOM   6295 C CA    . ALA C 3 1   ? -0.513  51.850  85.395  1.00 115.37 ?  1   ALA C CA    1 
ATOM   6296 C C     . ALA C 3 1   ? -1.172  50.558  84.922  1.00 123.96 ?  1   ALA C C     1 
ATOM   6297 O O     . ALA C 3 1   ? -2.216  50.654  84.307  1.00 126.14 ?  1   ALA C O     1 
ATOM   6298 C CB    . ALA C 3 1   ? 0.176   51.667  86.713  1.00 120.87 ?  1   ALA C CB    1 
ATOM   6299 N N     . ARG C 3 2   ? -0.654  49.390  85.307  1.00 126.81 ?  2   ARG C N     1 
ATOM   6300 C CA    . ARG C 3 2   ? -1.204  48.100  84.804  1.00 126.42 ?  2   ARG C CA    1 
ATOM   6301 C C     . ARG C 3 2   ? -2.702  47.973  85.050  1.00 126.89 ?  2   ARG C C     1 
ATOM   6302 O O     . ARG C 3 2   ? -3.396  47.544  84.149  1.00 120.97 ?  2   ARG C O     1 
ATOM   6303 C CB    . ARG C 3 2   ? -0.545  46.872  85.421  1.00 125.19 ?  2   ARG C CB    1 
ATOM   6304 C CG    . ARG C 3 2   ? -1.196  45.592  84.924  1.00 122.84 ?  2   ARG C CG    1 
ATOM   6305 C CD    . ARG C 3 2   ? -0.667  44.349  85.589  1.00 123.07 ?  2   ARG C CD    1 
ATOM   6306 N NE    . ARG C 3 2   ? 0.339   43.703  84.773  1.00 121.40 ?  2   ARG C NE    1 
ATOM   6307 C CZ    . ARG C 3 2   ? 1.589   43.543  85.157  1.00 123.73 ?  2   ARG C CZ    1 
ATOM   6308 N NH1   . ARG C 3 2   ? 1.974   43.991  86.337  1.00 126.51 ?  2   ARG C NH1   1 
ATOM   6309 N NH2   . ARG C 3 2   ? 2.450   42.935  84.368  1.00 123.23 ?  2   ARG C NH2   1 
ATOM   6310 N N     . THR C 3 3   ? -3.195  48.416  86.201  1.00 126.53 ?  3   THR C N     1 
ATOM   6311 C CA    . THR C 3 3   ? -4.637  48.363  86.527  1.00 127.30 ?  3   THR C CA    1 
ATOM   6312 C C     . THR C 3 3   ? -5.493  48.979  85.414  1.00 128.21 ?  3   THR C C     1 
ATOM   6313 O O     . THR C 3 3   ? -6.553  48.432  85.141  1.00 125.53 ?  3   THR C O     1 
ATOM   6314 C CB    . THR C 3 3   ? -4.847  49.096  87.848  1.00 123.61 ?  3   THR C CB    1 
ATOM   6315 O OG1   . THR C 3 3   ? -4.932  50.471  87.502  1.00 124.91 ?  3   THR C OG1   1 
ATOM   6316 C CG2   . THR C 3 3   ? -3.658  48.954  88.766  1.00 118.39 ?  3   THR C CG2   1 
ATOM   6317 N N     . MET C 3 4   ? -5.064  50.110  84.853  1.00 131.30 ?  4   MET C N     1 
ATOM   6318 C CA    . MET C 3 4   ? -5.777  50.866  83.794  1.00 135.09 ?  4   MET C CA    1 
ATOM   6319 C C     . MET C 3 4   ? -6.172  50.022  82.580  1.00 133.90 ?  4   MET C C     1 
ATOM   6320 O O     . MET C 3 4   ? -7.202  50.388  82.006  1.00 131.80 ?  4   MET C O     1 
ATOM   6321 C CB    . MET C 3 4   ? -4.923  52.030  83.281  1.00 130.89 ?  4   MET C CB    1 
ATOM   6322 C CG    . MET C 3 4   ? -5.119  53.333  84.015  1.00 132.40 ?  4   MET C CG    1 
ATOM   6323 S SD    . MET C 3 4   ? -6.818  53.868  83.872  1.00 141.94 ?  4   MET C SD    1 
ATOM   6324 C CE    . MET C 3 4   ? -6.627  55.469  83.093  1.00 114.33 ?  4   MET C CE    1 
ATOM   6325 N N     . GLN C 3 5   ? -5.413  48.989  82.178  1.00 131.83 ?  5   GLN C N     1 
ATOM   6326 C CA    . GLN C 3 5   ? -5.770  48.308  80.907  1.00 132.23 ?  5   GLN C CA    1 
ATOM   6327 C C     . GLN C 3 5   ? -7.187  47.763  81.025  1.00 137.55 ?  5   GLN C C     1 
ATOM   6328 O O     . GLN C 3 5   ? -7.498  47.145  82.030  1.00 133.05 ?  5   GLN C O     1 
ATOM   6329 C CB    . GLN C 3 5   ? -4.767  47.206  80.587  1.00 118.26 ?  5   GLN C CB    1 
ATOM   6330 C CG    . GLN C 3 5   ? -3.479  47.742  80.006  1.00 116.03 ?  5   GLN C CG    1 
ATOM   6331 C CD    . GLN C 3 5   ? -2.445  46.658  79.902  1.00 115.86 ?  5   GLN C CD    1 
ATOM   6332 O OE1   . GLN C 3 5   ? -2.652  45.543  80.357  1.00 116.96 ?  5   GLN C OE1   1 
ATOM   6333 N NE2   . GLN C 3 5   ? -1.316  46.978  79.298  1.00 109.47 ?  5   GLN C NE2   1 
ATOM   6334 N N     . THR C 3 6   ? -8.024  48.063  80.043  1.00 142.10 ?  6   THR C N     1 
ATOM   6335 C CA    . THR C 3 6   ? -9.422  47.597  80.082  1.00 134.67 ?  6   THR C CA    1 
ATOM   6336 C C     . THR C 3 6   ? -9.602  46.527  79.025  1.00 137.56 ?  6   THR C C     1 
ATOM   6337 O O     . THR C 3 6   ? -10.477 45.687  79.188  1.00 135.48 ?  6   THR C O     1 
ATOM   6338 C CB    . THR C 3 6   ? -10.338 48.724  79.632  1.00 129.43 ?  6   THR C CB    1 
ATOM   6339 O OG1   . THR C 3 6   ? -10.192 49.717  80.641  1.00 127.66 ?  6   THR C OG1   1 
ATOM   6340 C CG2   . THR C 3 6   ? -11.768 48.270  79.486  1.00 119.10 ?  6   THR C CG2   1 
ATOM   6341 N N     . ALA C 3 7   ? -8.774  46.588  77.988  1.00 134.03 ?  7   ALA C N     1 
ATOM   6342 C CA    . ALA C 3 7   ? -8.853  45.618  76.883  1.00 132.77 ?  7   ALA C CA    1 
ATOM   6343 C C     . ALA C 3 7   ? -7.501  44.931  76.744  1.00 128.98 ?  7   ALA C C     1 
ATOM   6344 O O     . ALA C 3 7   ? -6.482  45.610  76.785  1.00 123.63 ?  7   ALA C O     1 
ATOM   6345 C CB    . ALA C 3 7   ? -9.249  46.320  75.620  1.00 118.48 ?  7   ALA C CB    1 
ATOM   6346 N N     . ARG C 3 8   ? -7.530  43.617  76.616  1.00 126.02 ?  8   ARG C N     1 
ATOM   6347 C CA    . ARG C 3 8   ? -6.292  42.829  76.462  1.00 122.78 ?  8   ARG C CA    1 
ATOM   6348 C C     . ARG C 3 8   ? -5.342  43.095  77.622  1.00 122.88 ?  8   ARG C C     1 
ATOM   6349 O O     . ARG C 3 8   ? -4.152  43.215  77.360  1.00 119.44 ?  8   ARG C O     1 
ATOM   6350 C CB    . ARG C 3 8   ? -5.669  43.014  75.080  1.00 121.04 ?  8   ARG C CB    1 
ATOM   6351 C CG    . ARG C 3 8   ? -6.563  42.517  73.954  1.00 126.37 ?  8   ARG C CG    1 
ATOM   6352 C CD    . ARG C 3 8   ? -5.912  41.477  73.070  1.00 128.56 ?  8   ARG C CD    1 
ATOM   6353 N NE    . ARG C 3 8   ? -6.811  40.363  72.846  1.00 131.24 ?  8   ARG C NE    1 
ATOM   6354 C CZ    . ARG C 3 8   ? -7.378  40.093  71.686  1.00 128.80 ?  8   ARG C CZ    1 
ATOM   6355 N NH1   . ARG C 3 8   ? -7.159  40.873  70.646  1.00 125.23 ?  8   ARG C NH1   1 
ATOM   6356 N NH2   . ARG C 3 8   ? -8.185  39.059  71.565  1.00 122.81 ?  8   ARG C NH2   1 
ATOM   6357 N N     . LYS C 3 9   ? -5.883  43.251  78.831  1.00 119.21 ?  9   LYS C N     1 
ATOM   6358 C CA    . LYS C 3 9   ? -5.069  43.251  80.054  1.00 120.93 ?  9   LYS C CA    1 
ATOM   6359 C C     . LYS C 3 9   ? -3.916  42.265  80.008  1.00 118.41 ?  9   LYS C C     1 
ATOM   6360 O O     . LYS C 3 9   ? -4.113  41.069  79.779  1.00 122.25 ?  9   LYS C O     1 
ATOM   6361 C CB    . LYS C 3 9   ? -5.896  42.946  81.326  1.00 128.47 ?  9   LYS C CB    1 
ATOM   6362 C CG    . LYS C 3 9   ? -6.907  43.995  81.810  1.00 127.91 ?  9   LYS C CG    1 
ATOM   6363 C CD    . LYS C 3 9   ? -7.724  43.678  83.095  1.00 120.07 ?  9   LYS C CD    1 
ATOM   6364 C CE    . LYS C 3 9   ? -8.866  42.700  82.961  1.00 122.27 ?  9   LYS C CE    1 
ATOM   6365 N NZ    . LYS C 3 9   ? -9.936  43.297  82.099  1.00 111.68 ?  9   LYS C NZ    1 
ATOM   6366 N N     . SER C 3 10  ? -2.725  42.765  80.333  1.00 114.24 ?  10  SER C N     1 
ATOM   6367 C CA    . SER C 3 10  ? -1.524  41.950  80.412  1.00 119.35 ?  10  SER C CA    1 
ATOM   6368 C C     . SER C 3 10  ? -1.488  41.129  81.713  1.00 126.45 ?  10  SER C C     1 
ATOM   6369 O O     . SER C 3 10  ? -2.116  41.471  82.724  1.00 130.88 ?  10  SER C O     1 
ATOM   6370 C CB    . SER C 3 10  ? -0.279  42.834  80.269  1.00 115.95 ?  10  SER C CB    1 
ATOM   6371 O OG    . SER C 3 10  ? -0.076  43.661  81.396  1.00 122.38 ?  10  SER C OG    1 
ATOM   6372 N N     . THR C 3 11  ? -0.746  40.014  81.655  1.00 124.49 ?  11  THR C N     1 
ATOM   6373 C CA    . THR C 3 11  ? -0.641  39.002  82.705  1.00 124.11 ?  11  THR C CA    1 
ATOM   6374 C C     . THR C 3 11  ? 0.734   38.944  83.346  1.00 129.63 ?  11  THR C C     1 
ATOM   6375 O O     . THR C 3 11  ? 0.826   38.871  84.575  1.00 139.43 ?  11  THR C O     1 
ATOM   6376 C CB    . THR C 3 11  ? -1.004  37.599  82.154  1.00 124.05 ?  11  THR C CB    1 
ATOM   6377 O OG1   . THR C 3 11  ? -2.368  37.577  81.707  1.00 121.87 ?  11  THR C OG1   1 
ATOM   6378 C CG2   . THR C 3 11  ? -0.743  36.475  83.180  1.00 127.63 ?  11  THR C CG2   1 
ATOM   6379 N N     . GLY C 3 12  ? 1.808   38.956  82.558  1.00 124.54 ?  12  GLY C N     1 
ATOM   6380 C CA    . GLY C 3 12  ? 3.137   38.773  83.117  1.00 127.11 ?  12  GLY C CA    1 
ATOM   6381 C C     . GLY C 3 12  ? 3.523   39.675  84.280  1.00 134.43 ?  12  GLY C C     1 
ATOM   6382 O O     . GLY C 3 12  ? 3.404   40.897  84.164  1.00 138.87 ?  12  GLY C O     1 
ATOM   6383 N N     . GLY C 3 13  ? 3.982   39.110  85.402  1.00 134.27 ?  13  GLY C N     1 
ATOM   6384 C CA    . GLY C 3 13  ? 4.307   39.914  86.575  1.00 135.20 ?  13  GLY C CA    1 
ATOM   6385 C C     . GLY C 3 13  ? 3.150   40.221  87.511  1.00 140.96 ?  13  GLY C C     1 
ATOM   6386 O O     . GLY C 3 13  ? 3.304   41.058  88.417  1.00 140.40 ?  13  GLY C O     1 
ATOM   6387 N N     . LYS C 3 14  ? 1.997   39.585  87.311  1.00 141.50 ?  14  LYS C N     1 
ATOM   6388 C CA    . LYS C 3 14  ? 0.847   39.650  88.199  1.00 147.16 ?  14  LYS C CA    1 
ATOM   6389 C C     . LYS C 3 14  ? 0.953   38.531  89.245  1.00 156.56 ?  14  LYS C C     1 
ATOM   6390 O O     . LYS C 3 14  ? 1.874   37.707  89.214  1.00 156.36 ?  14  LYS C O     1 
ATOM   6391 C CB    . LYS C 3 14  ? -0.438  39.528  87.377  1.00 141.01 ?  14  LYS C CB    1 
ATOM   6392 C CG    . LYS C 3 14  ? -1.689  40.131  87.977  1.00 141.06 ?  14  LYS C CG    1 
ATOM   6393 C CD    . LYS C 3 14  ? -2.530  40.745  86.883  1.00 135.39 ?  14  LYS C CD    1 
ATOM   6394 C CE    . LYS C 3 14  ? -3.961  40.911  87.343  1.00 134.88 ?  14  LYS C CE    1 
ATOM   6395 N NZ    . LYS C 3 14  ? -4.728  41.846  86.477  1.00 137.61 ?  14  LYS C NZ    1 
ATOM   6396 N N     . ALA C 3 15  ? -0.012  38.502  90.190  1.00 162.23 ?  15  ALA C N     1 
ATOM   6397 C CA    . ALA C 3 15  ? -0.063  37.475  91.238  1.00 165.40 ?  15  ALA C CA    1 
ATOM   6398 C C     . ALA C 3 15  ? -1.253  36.528  91.052  1.00 168.02 ?  15  ALA C C     1 
ATOM   6399 O O     . ALA C 3 15  ? -2.189  36.542  91.870  1.00 164.55 ?  15  ALA C O     1 
ATOM   6400 C CB    . ALA C 3 15  ? -0.122  38.125  92.628  1.00 159.51 ?  15  ALA C CB    1 
ATOM   6401 N N     . PRO C 3 16  ? -1.247  35.663  90.010  1.00 168.99 ?  16  PRO C N     1 
ATOM   6402 C CA    . PRO C 3 16  ? -2.418  34.858  89.656  1.00 168.49 ?  16  PRO C CA    1 
ATOM   6403 C C     . PRO C 3 16  ? -2.428  33.473  90.298  1.00 168.48 ?  16  PRO C C     1 
ATOM   6404 O O     . PRO C 3 16  ? -2.039  32.492  89.658  1.00 171.80 ?  16  PRO C O     1 
ATOM   6405 C CB    . PRO C 3 16  ? -2.291  34.769  88.132  1.00 171.20 ?  16  PRO C CB    1 
ATOM   6406 C CG    . PRO C 3 16  ? -0.781  34.644  87.914  1.00 165.64 ?  16  PRO C CG    1 
ATOM   6407 C CD    . PRO C 3 16  ? -0.109  35.317  89.130  1.00 165.31 ?  16  PRO C CD    1 
HETATM 6408 O O2A   . HUF D 4 .   ? -5.938  67.129  87.440  1.00 99.18  ?  901 HUF A O2A   1 
HETATM 6409 P PA    . HUF D 4 .   ? -6.681  66.946  88.722  1.00 103.30 ?  901 HUF A PA    1 
HETATM 6410 O O1A   . HUF D 4 .   ? -8.155  66.715  88.659  1.00 95.35  -1 901 HUF A O1A   1 
HETATM 6411 O O3A   . HUF D 4 .   ? -6.006  65.743  89.541  1.00 96.64  ?  901 HUF A O3A   1 
HETATM 6412 P PB    . HUF D 4 .   ? -6.514  64.854  90.775  1.00 93.32  ?  901 HUF A PB    1 
HETATM 6413 O O3B   . HUF D 4 .   ? -7.468  65.656  91.597  1.00 99.52  ?  901 HUF A O3B   1 
HETATM 6414 O O2B   . HUF D 4 .   ? -5.336  64.226  91.445  1.00 85.73  -1 901 HUF A O2B   1 
HETATM 6415 O O1B   . HUF D 4 .   ? -7.338  63.705  90.018  1.00 93.43  ?  901 HUF A O1B   1 
HETATM 6416 O "O5'" . HUF D 4 .   ? -6.379  68.186  89.694  1.00 98.07  ?  901 HUF A "O5'" 1 
HETATM 6417 C "C5'" . HUF D 4 .   ? -5.821  69.395  89.121  1.00 94.34  ?  901 HUF A "C5'" 1 
HETATM 6418 C "C4'" . HUF D 4 .   ? -6.883  70.467  89.087  1.00 92.49  ?  901 HUF A "C4'" 1 
HETATM 6419 C "C3'" . HUF D 4 .   ? -7.473  70.787  87.707  1.00 98.62  ?  901 HUF A "C3'" 1 
HETATM 6420 O "O3'" . HUF D 4 .   ? -8.860  71.087  87.795  1.00 100.50 ?  901 HUF A "O3'" 1 
HETATM 6421 C "C2'" . HUF D 4 .   ? -6.660  72.008  87.269  1.00 95.90  ?  901 HUF A "C2'" 1 
HETATM 6422 O "O2'" . HUF D 4 .   ? -7.345  72.814  86.336  1.00 100.75 ?  901 HUF A "O2'" 1 
HETATM 6423 C "C1'" . HUF D 4 .   ? -6.469  72.725  88.601  1.00 92.96  ?  901 HUF A "C1'" 1 
HETATM 6424 O "O4'" . HUF D 4 .   ? -6.315  71.713  89.570  1.00 90.97  ?  901 HUF A "O4'" 1 
HETATM 6425 N N9    . HUF D 4 .   ? -5.293  73.586  88.643  1.00 92.13  ?  901 HUF A N9    1 
HETATM 6426 C C4    . HUF D 4 .   ? -5.231  74.891  89.072  1.00 91.03  ?  901 HUF A C4    1 
HETATM 6427 C C5    . HUF D 4 .   ? -3.912  75.275  88.921  1.00 89.25  ?  901 HUF A C5    1 
HETATM 6428 N N7    . HUF D 4 .   ? -3.160  74.230  88.407  1.00 87.15  ?  901 HUF A N7    1 
HETATM 6429 C C8    . HUF D 4 .   ? -4.019  73.253  88.259  1.00 90.28  ?  901 HUF A C8    1 
HETATM 6430 N N3    . HUF D 4 .   ? -6.234  75.650  89.542  1.00 88.45  ?  901 HUF A N3    1 
HETATM 6431 C C2    . HUF D 4 .   ? -5.801  76.866  89.862  1.00 89.27  ?  901 HUF A C2    1 
HETATM 6432 N N1    . HUF D 4 .   ? -4.567  77.378  89.773  1.00 90.29  ?  901 HUF A N1    1 
HETATM 6433 C C6    . HUF D 4 .   ? -3.575  76.590  89.295  1.00 93.35  ?  901 HUF A C6    1 
HETATM 6434 N N6    . HUF D 4 .   ? -2.346  77.092  89.204  1.00 95.49  ?  901 HUF A N6    1 
HETATM 6435 C C11   . HUF D 4 .   ? -5.757  62.885  81.602  1.00 94.24  ?  901 HUF A C11   1 
HETATM 6436 C C12   . HUF D 4 .   ? -6.442  61.550  81.701  1.00 99.82  ?  901 HUF A C12   1 
HETATM 6437 C C13   . HUF D 4 .   ? -6.614  60.954  82.922  1.00 106.02 ?  901 HUF A C13   1 
HETATM 6438 C C14   . HUF D 4 .   ? -7.243  59.716  83.034  1.00 105.46 ?  901 HUF A C14   1 
HETATM 6439 C C15   . HUF D 4 .   ? -7.719  59.068  81.880  1.00 104.53 ?  901 HUF A C15   1 
HETATM 6440 C C16   . HUF D 4 .   ? -7.543  59.672  80.636  1.00 108.17 ?  901 HUF A C16   1 
HETATM 6441 C C17   . HUF D 4 .   ? -6.922  60.887  80.520  1.00 102.50 ?  901 HUF A C17   1 
HETATM 6442 C C18   . HUF D 4 .   ? -6.748  61.519  79.166  1.00 99.64  ?  901 HUF A C18   1 
HETATM 6443 C C19   . HUF D 4 .   ? -8.469  56.942  80.908  1.00 113.39 ?  901 HUF A C19   1 
HETATM 6444 C C20   . HUF D 4 .   ? -8.840  57.400  83.296  1.00 106.82 ?  901 HUF A C20   1 
HETATM 6445 C C21   . HUF D 4 .   ? -8.344  58.073  84.439  1.00 107.19 ?  901 HUF A C21   1 
HETATM 6446 C C22   . HUF D 4 .   ? -9.691  56.711  85.884  1.00 105.09 ?  901 HUF A C22   1 
HETATM 6447 C C23   . HUF D 4 .   ? -9.771  56.364  83.463  1.00 104.14 ?  901 HUF A C23   1 
HETATM 6448 C C24   . HUF D 4 .   ? -6.627  59.563  85.450  1.00 102.04 ?  901 HUF A C24   1 
HETATM 6449 C C25   . HUF D 4 .   ? -7.500  60.176  86.528  1.00 101.32 ?  901 HUF A C25   1 
HETATM 6450 C C26   . HUF D 4 .   ? -6.733  61.241  87.316  1.00 96.11  ?  901 HUF A C26   1 
HETATM 6451 C C27   . HUF D 4 .   ? -7.611  62.046  88.276  1.00 97.69  ?  901 HUF A C27   1 
HETATM 6452 C C28   . HUF D 4 .   ? -6.999  63.378  88.642  1.00 101.77 ?  901 HUF A C28   1 
HETATM 6453 N N29   . HUF D 4 .   ? -8.365  57.793  82.002  1.00 107.14 ?  901 HUF A N29   1 
HETATM 6454 N N30   . HUF D 4 .   ? -8.780  57.718  85.695  1.00 106.36 ?  901 HUF A N30   1 
HETATM 6455 N N31   . HUF D 4 .   ? -10.154 56.070  84.761  1.00 108.40 ?  901 HUF A N31   1 
HETATM 6456 N N32   . HUF D 4 .   ? -7.426  59.098  84.291  1.00 105.01 ?  901 HUF A N32   1 
HETATM 6457 O O33   . HUF D 4 .   ? -8.236  55.739  80.967  1.00 119.72 ?  901 HUF A O33   1 
HETATM 6458 O O34   . HUF D 4 .   ? -10.065 56.408  87.005  1.00 95.63  ?  901 HUF A O34   1 
HETATM 6459 O O35   . HUF D 4 .   ? -10.255 55.721  82.530  1.00 99.20  ?  901 HUF A O35   1 
HETATM 6460 O O36   . HUF D 4 .   ? -8.651  60.767  85.933  1.00 99.60  ?  901 HUF A O36   1 
HETATM 6461 O O37   . HUF D 4 .   ? -5.684  60.619  88.051  1.00 91.04  ?  901 HUF A O37   1 
HETATM 6462 O O38   . HUF D 4 .   ? -8.894  62.262  87.684  1.00 98.28  ?  901 HUF A O38   1 
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